data_9BMD
# 
_entry.id   9BMD 
# 
_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   9BMD         pdb_00009bmd 10.2210/pdb9bmd/pdb 
WWPDB D_1000283550 ?            ?                   
EMDB  EMD-44696    ?            ?                   
# 
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 2025-05-28 ? 
12 'EM metadata'     1 1 2025-05-28 ? 
# 
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                        9BMD 
_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        'motor domain from full-length human dynein-1 bound to microtubules in 5mM AMPPNP condition' 
_pdbx_database_related.db_id          EMD-44696 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jack.zhang@yale.edu 
_pdbx_contact_author.name_first         Jack 
_pdbx_contact_author.name_last          Zhang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8617-2855 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chai, P.'  1 0000-0001-9702-978X 
'Zhang, K.' 2 0000-0001-8617-2855 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nat.Struct.Mol.Biol. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1545-9985 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'The mechanochemical cycle of reactive full-length human dynein 1.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41594-025-01543-3 
_citation.pdbx_database_id_PubMed   40263469 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chai, P.'       1 0000-0001-9702-978X 
primary 'Yang, J.'       2 ?                   
primary 'Geohring, I.C.' 3 ?                   
primary 'Markus, S.M.'   4 0000-0002-3098-0236 
primary 'Wang, Y.'       5 0000-0002-8020-3937 
primary 'Zhang, K.'      6 0000-0001-8617-2855 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Cytoplasmic dynein 1 heavy chain 1'          533083.250 1 ? ? ? ? 
2 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"                    427.201    1 ? ? ? ? 
3 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE"                   507.181    1 ? ? ? ? 
4 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' 506.196    2 ? ? ? ? 
5 non-polymer syn 'MAGNESIUM ION'                               24.305     4 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cytoplasmic dynein heavy chain 1,Dynein heavy chain,cytosolic' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "ADENOSINE-5'-DIPHOSPHATE"                    ADP 
3 "ADENOSINE-5'-TRIPHOSPHATE"                   ATP 
4 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ANP 
5 'MAGNESIUM ION'                               MG  
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    MET n 
1 2    SER n 
1 3    GLU n 
1 4    PRO n 
1 5    GLY n 
1 6    GLY n 
1 7    GLY n 
1 8    GLY n 
1 9    GLY n 
1 10   GLU n 
1 11   ASP n 
1 12   GLY n 
1 13   SER n 
1 14   ALA n 
1 15   GLY n 
1 16   LEU n 
1 17   GLU n 
1 18   VAL n 
1 19   SER n 
1 20   ALA n 
1 21   VAL n 
1 22   GLN n 
1 23   ASN n 
1 24   VAL n 
1 25   ALA n 
1 26   ASP n 
1 27   VAL n 
1 28   SER n 
1 29   VAL n 
1 30   LEU n 
1 31   GLN n 
1 32   LYS n 
1 33   HIS n 
1 34   LEU n 
1 35   ARG n 
1 36   LYS n 
1 37   LEU n 
1 38   VAL n 
1 39   PRO n 
1 40   LEU n 
1 41   LEU n 
1 42   LEU n 
1 43   GLU n 
1 44   ASP n 
1 45   GLY n 
1 46   GLY n 
1 47   GLU n 
1 48   ALA n 
1 49   PRO n 
1 50   ALA n 
1 51   ALA n 
1 52   LEU n 
1 53   GLU n 
1 54   ALA n 
1 55   ALA n 
1 56   LEU n 
1 57   GLU n 
1 58   GLU n 
1 59   LYS n 
1 60   SER n 
1 61   ALA n 
1 62   LEU n 
1 63   GLU n 
1 64   GLN n 
1 65   MET n 
1 66   ARG n 
1 67   LYS n 
1 68   PHE n 
1 69   LEU n 
1 70   SER n 
1 71   ASP n 
1 72   PRO n 
1 73   GLN n 
1 74   VAL n 
1 75   HIS n 
1 76   THR n 
1 77   VAL n 
1 78   LEU n 
1 79   VAL n 
1 80   GLU n 
1 81   ARG n 
1 82   SER n 
1 83   THR n 
1 84   LEU n 
1 85   LYS n 
1 86   GLU n 
1 87   ASP n 
1 88   VAL n 
1 89   GLY n 
1 90   ASP n 
1 91   GLU n 
1 92   GLY n 
1 93   GLU n 
1 94   GLU n 
1 95   GLU n 
1 96   LYS n 
1 97   GLU n 
1 98   PHE n 
1 99   ILE n 
1 100  SER n 
1 101  TYR n 
1 102  ASN n 
1 103  ILE n 
1 104  ASN n 
1 105  ILE n 
1 106  ASP n 
1 107  ILE n 
1 108  HIS n 
1 109  TYR n 
1 110  GLY n 
1 111  VAL n 
1 112  LYS n 
1 113  SER n 
1 114  ASN n 
1 115  SER n 
1 116  LEU n 
1 117  ALA n 
1 118  PHE n 
1 119  ILE n 
1 120  LYS n 
1 121  ARG n 
1 122  THR n 
1 123  PRO n 
1 124  VAL n 
1 125  ILE n 
1 126  ASP n 
1 127  ALA n 
1 128  ASP n 
1 129  LYS n 
1 130  PRO n 
1 131  VAL n 
1 132  SER n 
1 133  SER n 
1 134  GLN n 
1 135  LEU n 
1 136  ARG n 
1 137  VAL n 
1 138  LEU n 
1 139  THR n 
1 140  LEU n 
1 141  SER n 
1 142  GLU n 
1 143  ASP n 
1 144  SER n 
1 145  PRO n 
1 146  TYR n 
1 147  GLU n 
1 148  THR n 
1 149  LEU n 
1 150  HIS n 
1 151  SER n 
1 152  PHE n 
1 153  ILE n 
1 154  SER n 
1 155  ASN n 
1 156  ALA n 
1 157  VAL n 
1 158  ALA n 
1 159  PRO n 
1 160  PHE n 
1 161  PHE n 
1 162  LYS n 
1 163  SER n 
1 164  TYR n 
1 165  ILE n 
1 166  ARG n 
1 167  GLU n 
1 168  SER n 
1 169  GLY n 
1 170  LYS n 
1 171  ALA n 
1 172  ASP n 
1 173  ARG n 
1 174  ASP n 
1 175  GLY n 
1 176  ASP n 
1 177  LYS n 
1 178  MET n 
1 179  ALA n 
1 180  PRO n 
1 181  SER n 
1 182  VAL n 
1 183  GLU n 
1 184  LYS n 
1 185  LYS n 
1 186  ILE n 
1 187  ALA n 
1 188  GLU n 
1 189  LEU n 
1 190  GLU n 
1 191  MET n 
1 192  GLY n 
1 193  LEU n 
1 194  LEU n 
1 195  HIS n 
1 196  LEU n 
1 197  GLN n 
1 198  GLN n 
1 199  ASN n 
1 200  ILE n 
1 201  GLU n 
1 202  ILE n 
1 203  PRO n 
1 204  GLU n 
1 205  ILE n 
1 206  SER n 
1 207  LEU n 
1 208  PRO n 
1 209  ILE n 
1 210  HIS n 
1 211  PRO n 
1 212  MET n 
1 213  ILE n 
1 214  THR n 
1 215  ASN n 
1 216  VAL n 
1 217  ALA n 
1 218  LYS n 
1 219  GLN n 
1 220  CYS n 
1 221  TYR n 
1 222  GLU n 
1 223  ARG n 
1 224  GLY n 
1 225  GLU n 
1 226  LYS n 
1 227  PRO n 
1 228  LYS n 
1 229  VAL n 
1 230  THR n 
1 231  ASP n 
1 232  PHE n 
1 233  GLY n 
1 234  ASP n 
1 235  LYS n 
1 236  VAL n 
1 237  GLU n 
1 238  ASP n 
1 239  PRO n 
1 240  THR n 
1 241  PHE n 
1 242  LEU n 
1 243  ASN n 
1 244  GLN n 
1 245  LEU n 
1 246  GLN n 
1 247  SER n 
1 248  GLY n 
1 249  VAL n 
1 250  ASN n 
1 251  ARG n 
1 252  TRP n 
1 253  ILE n 
1 254  ARG n 
1 255  GLU n 
1 256  ILE n 
1 257  GLN n 
1 258  LYS n 
1 259  VAL n 
1 260  THR n 
1 261  LYS n 
1 262  LEU n 
1 263  ASP n 
1 264  ARG n 
1 265  ASP n 
1 266  PRO n 
1 267  ALA n 
1 268  SER n 
1 269  GLY n 
1 270  THR n 
1 271  ALA n 
1 272  LEU n 
1 273  GLN n 
1 274  GLU n 
1 275  ILE n 
1 276  SER n 
1 277  PHE n 
1 278  TRP n 
1 279  LEU n 
1 280  ASN n 
1 281  LEU n 
1 282  GLU n 
1 283  ARG n 
1 284  ALA n 
1 285  LEU n 
1 286  TYR n 
1 287  ARG n 
1 288  ILE n 
1 289  GLN n 
1 290  GLU n 
1 291  LYS n 
1 292  ARG n 
1 293  GLU n 
1 294  SER n 
1 295  PRO n 
1 296  GLU n 
1 297  VAL n 
1 298  LEU n 
1 299  LEU n 
1 300  THR n 
1 301  LEU n 
1 302  ASP n 
1 303  ILE n 
1 304  LEU n 
1 305  LYS n 
1 306  HIS n 
1 307  GLY n 
1 308  LYS n 
1 309  ARG n 
1 310  PHE n 
1 311  HIS n 
1 312  ALA n 
1 313  THR n 
1 314  VAL n 
1 315  SER n 
1 316  PHE n 
1 317  ASP n 
1 318  THR n 
1 319  ASP n 
1 320  THR n 
1 321  GLY n 
1 322  LEU n 
1 323  LYS n 
1 324  GLN n 
1 325  ALA n 
1 326  LEU n 
1 327  GLU n 
1 328  THR n 
1 329  VAL n 
1 330  ASN n 
1 331  ASP n 
1 332  TYR n 
1 333  ASN n 
1 334  PRO n 
1 335  LEU n 
1 336  MET n 
1 337  LYS n 
1 338  ASP n 
1 339  PHE n 
1 340  PRO n 
1 341  LEU n 
1 342  ASN n 
1 343  ASP n 
1 344  LEU n 
1 345  LEU n 
1 346  SER n 
1 347  ALA n 
1 348  THR n 
1 349  GLU n 
1 350  LEU n 
1 351  ASP n 
1 352  LYS n 
1 353  ILE n 
1 354  ARG n 
1 355  GLN n 
1 356  ALA n 
1 357  LEU n 
1 358  VAL n 
1 359  ALA n 
1 360  ILE n 
1 361  PHE n 
1 362  THR n 
1 363  HIS n 
1 364  LEU n 
1 365  ARG n 
1 366  LYS n 
1 367  ILE n 
1 368  ARG n 
1 369  ASN n 
1 370  THR n 
1 371  LYS n 
1 372  TYR n 
1 373  PRO n 
1 374  ILE n 
1 375  GLN n 
1 376  ARG n 
1 377  ALA n 
1 378  LEU n 
1 379  ARG n 
1 380  LEU n 
1 381  VAL n 
1 382  GLU n 
1 383  ALA n 
1 384  ILE n 
1 385  SER n 
1 386  ARG n 
1 387  ASP n 
1 388  LEU n 
1 389  SER n 
1 390  SER n 
1 391  GLN n 
1 392  LEU n 
1 393  LEU n 
1 394  LYS n 
1 395  VAL n 
1 396  LEU n 
1 397  GLY n 
1 398  THR n 
1 399  ARG n 
1 400  LYS n 
1 401  LEU n 
1 402  MET n 
1 403  HIS n 
1 404  VAL n 
1 405  ALA n 
1 406  TYR n 
1 407  GLU n 
1 408  GLU n 
1 409  PHE n 
1 410  GLU n 
1 411  LYS n 
1 412  VAL n 
1 413  MET n 
1 414  VAL n 
1 415  ALA n 
1 416  CYS n 
1 417  PHE n 
1 418  GLU n 
1 419  VAL n 
1 420  PHE n 
1 421  GLN n 
1 422  THR n 
1 423  TRP n 
1 424  ASP n 
1 425  ASP n 
1 426  GLU n 
1 427  TYR n 
1 428  GLU n 
1 429  LYS n 
1 430  LEU n 
1 431  GLN n 
1 432  VAL n 
1 433  LEU n 
1 434  LEU n 
1 435  ARG n 
1 436  ASP n 
1 437  ILE n 
1 438  VAL n 
1 439  LYS n 
1 440  ARG n 
1 441  LYS n 
1 442  ARG n 
1 443  GLU n 
1 444  GLU n 
1 445  ASN n 
1 446  LEU n 
1 447  LYS n 
1 448  MET n 
1 449  VAL n 
1 450  TRP n 
1 451  ARG n 
1 452  ILE n 
1 453  ASN n 
1 454  PRO n 
1 455  ALA n 
1 456  HIS n 
1 457  ARG n 
1 458  LYS n 
1 459  LEU n 
1 460  GLN n 
1 461  ALA n 
1 462  ARG n 
1 463  LEU n 
1 464  ASP n 
1 465  GLN n 
1 466  MET n 
1 467  ARG n 
1 468  LYS n 
1 469  PHE n 
1 470  ARG n 
1 471  ARG n 
1 472  GLN n 
1 473  HIS n 
1 474  GLU n 
1 475  GLN n 
1 476  LEU n 
1 477  ARG n 
1 478  ALA n 
1 479  VAL n 
1 480  ILE n 
1 481  VAL n 
1 482  ARG n 
1 483  VAL n 
1 484  LEU n 
1 485  ARG n 
1 486  PRO n 
1 487  GLN n 
1 488  VAL n 
1 489  THR n 
1 490  ALA n 
1 491  VAL n 
1 492  ALA n 
1 493  GLN n 
1 494  GLN n 
1 495  ASN n 
1 496  GLN n 
1 497  GLY n 
1 498  GLU n 
1 499  VAL n 
1 500  PRO n 
1 501  GLU n 
1 502  PRO n 
1 503  GLN n 
1 504  ASP n 
1 505  MET n 
1 506  LYS n 
1 507  VAL n 
1 508  ALA n 
1 509  GLU n 
1 510  VAL n 
1 511  LEU n 
1 512  PHE n 
1 513  ASP n 
1 514  ALA n 
1 515  ALA n 
1 516  ASP n 
1 517  ALA n 
1 518  ASN n 
1 519  ALA n 
1 520  ILE n 
1 521  GLU n 
1 522  GLU n 
1 523  VAL n 
1 524  ASN n 
1 525  LEU n 
1 526  ALA n 
1 527  TYR n 
1 528  GLU n 
1 529  ASN n 
1 530  VAL n 
1 531  LYS n 
1 532  GLU n 
1 533  VAL n 
1 534  ASP n 
1 535  GLY n 
1 536  LEU n 
1 537  ASP n 
1 538  VAL n 
1 539  SER n 
1 540  LYS n 
1 541  GLU n 
1 542  GLY n 
1 543  THR n 
1 544  GLU n 
1 545  ALA n 
1 546  TRP n 
1 547  GLU n 
1 548  ALA n 
1 549  ALA n 
1 550  MET n 
1 551  LYS n 
1 552  ARG n 
1 553  TYR n 
1 554  ASP n 
1 555  GLU n 
1 556  ARG n 
1 557  ILE n 
1 558  ASP n 
1 559  ARG n 
1 560  VAL n 
1 561  GLU n 
1 562  THR n 
1 563  ARG n 
1 564  ILE n 
1 565  THR n 
1 566  ALA n 
1 567  ARG n 
1 568  LEU n 
1 569  ARG n 
1 570  ASP n 
1 571  GLN n 
1 572  LEU n 
1 573  GLY n 
1 574  THR n 
1 575  ALA n 
1 576  LYS n 
1 577  ASN n 
1 578  ALA n 
1 579  ASN n 
1 580  GLU n 
1 581  MET n 
1 582  PHE n 
1 583  ARG n 
1 584  ILE n 
1 585  PHE n 
1 586  SER n 
1 587  ARG n 
1 588  PHE n 
1 589  ASN n 
1 590  ALA n 
1 591  LEU n 
1 592  PHE n 
1 593  VAL n 
1 594  ARG n 
1 595  PRO n 
1 596  HIS n 
1 597  ILE n 
1 598  ARG n 
1 599  GLY n 
1 600  ALA n 
1 601  ILE n 
1 602  ARG n 
1 603  GLU n 
1 604  TYR n 
1 605  GLN n 
1 606  THR n 
1 607  GLN n 
1 608  LEU n 
1 609  ILE n 
1 610  GLN n 
1 611  ARG n 
1 612  VAL n 
1 613  LYS n 
1 614  ASP n 
1 615  ASP n 
1 616  ILE n 
1 617  GLU n 
1 618  SER n 
1 619  LEU n 
1 620  HIS n 
1 621  ASP n 
1 622  LYS n 
1 623  PHE n 
1 624  LYS n 
1 625  VAL n 
1 626  GLN n 
1 627  TYR n 
1 628  PRO n 
1 629  GLN n 
1 630  SER n 
1 631  GLN n 
1 632  ALA n 
1 633  CYS n 
1 634  LYS n 
1 635  MET n 
1 636  SER n 
1 637  HIS n 
1 638  VAL n 
1 639  ARG n 
1 640  ASP n 
1 641  LEU n 
1 642  PRO n 
1 643  PRO n 
1 644  VAL n 
1 645  SER n 
1 646  GLY n 
1 647  SER n 
1 648  ILE n 
1 649  ILE n 
1 650  TRP n 
1 651  ALA n 
1 652  LYS n 
1 653  GLN n 
1 654  ILE n 
1 655  ASP n 
1 656  ARG n 
1 657  GLN n 
1 658  LEU n 
1 659  THR n 
1 660  ALA n 
1 661  TYR n 
1 662  MET n 
1 663  LYS n 
1 664  ARG n 
1 665  VAL n 
1 666  GLU n 
1 667  ASP n 
1 668  VAL n 
1 669  LEU n 
1 670  GLY n 
1 671  LYS n 
1 672  GLY n 
1 673  TRP n 
1 674  GLU n 
1 675  ASN n 
1 676  HIS n 
1 677  VAL n 
1 678  GLU n 
1 679  GLY n 
1 680  GLN n 
1 681  LYS n 
1 682  LEU n 
1 683  LYS n 
1 684  GLN n 
1 685  ASP n 
1 686  GLY n 
1 687  ASP n 
1 688  SER n 
1 689  PHE n 
1 690  ARG n 
1 691  MET n 
1 692  LYS n 
1 693  LEU n 
1 694  ASN n 
1 695  THR n 
1 696  GLN n 
1 697  GLU n 
1 698  ILE n 
1 699  PHE n 
1 700  ASP n 
1 701  ASP n 
1 702  TRP n 
1 703  ALA n 
1 704  ARG n 
1 705  LYS n 
1 706  VAL n 
1 707  GLN n 
1 708  GLN n 
1 709  ARG n 
1 710  ASN n 
1 711  LEU n 
1 712  GLY n 
1 713  VAL n 
1 714  SER n 
1 715  GLY n 
1 716  ARG n 
1 717  ILE n 
1 718  PHE n 
1 719  THR n 
1 720  ILE n 
1 721  GLU n 
1 722  SER n 
1 723  THR n 
1 724  ARG n 
1 725  VAL n 
1 726  ARG n 
1 727  GLY n 
1 728  ARG n 
1 729  THR n 
1 730  GLY n 
1 731  ASN n 
1 732  VAL n 
1 733  LEU n 
1 734  LYS n 
1 735  LEU n 
1 736  LYS n 
1 737  VAL n 
1 738  ASN n 
1 739  PHE n 
1 740  LEU n 
1 741  PRO n 
1 742  GLU n 
1 743  ILE n 
1 744  ILE n 
1 745  THR n 
1 746  LEU n 
1 747  SER n 
1 748  LYS n 
1 749  GLU n 
1 750  VAL n 
1 751  ARG n 
1 752  ASN n 
1 753  LEU n 
1 754  LYS n 
1 755  TRP n 
1 756  LEU n 
1 757  GLY n 
1 758  PHE n 
1 759  ARG n 
1 760  VAL n 
1 761  PRO n 
1 762  LEU n 
1 763  ALA n 
1 764  ILE n 
1 765  VAL n 
1 766  ASN n 
1 767  LYS n 
1 768  ALA n 
1 769  HIS n 
1 770  GLN n 
1 771  ALA n 
1 772  ASN n 
1 773  GLN n 
1 774  LEU n 
1 775  TYR n 
1 776  PRO n 
1 777  PHE n 
1 778  ALA n 
1 779  ILE n 
1 780  SER n 
1 781  LEU n 
1 782  ILE n 
1 783  GLU n 
1 784  SER n 
1 785  VAL n 
1 786  ARG n 
1 787  THR n 
1 788  TYR n 
1 789  GLU n 
1 790  ARG n 
1 791  THR n 
1 792  CYS n 
1 793  GLU n 
1 794  LYS n 
1 795  VAL n 
1 796  GLU n 
1 797  GLU n 
1 798  ARG n 
1 799  ASN n 
1 800  THR n 
1 801  ILE n 
1 802  SER n 
1 803  LEU n 
1 804  LEU n 
1 805  VAL n 
1 806  ALA n 
1 807  GLY n 
1 808  LEU n 
1 809  LYS n 
1 810  LYS n 
1 811  GLU n 
1 812  VAL n 
1 813  GLN n 
1 814  ALA n 
1 815  LEU n 
1 816  ILE n 
1 817  ALA n 
1 818  GLU n 
1 819  GLY n 
1 820  ILE n 
1 821  ALA n 
1 822  LEU n 
1 823  VAL n 
1 824  TRP n 
1 825  GLU n 
1 826  SER n 
1 827  TYR n 
1 828  LYS n 
1 829  LEU n 
1 830  ASP n 
1 831  PRO n 
1 832  TYR n 
1 833  VAL n 
1 834  GLN n 
1 835  ARG n 
1 836  LEU n 
1 837  ALA n 
1 838  GLU n 
1 839  THR n 
1 840  VAL n 
1 841  PHE n 
1 842  ASN n 
1 843  PHE n 
1 844  GLN n 
1 845  GLU n 
1 846  LYS n 
1 847  VAL n 
1 848  ASP n 
1 849  ASP n 
1 850  LEU n 
1 851  LEU n 
1 852  ILE n 
1 853  ILE n 
1 854  GLU n 
1 855  GLU n 
1 856  LYS n 
1 857  ILE n 
1 858  ASP n 
1 859  LEU n 
1 860  GLU n 
1 861  VAL n 
1 862  ARG n 
1 863  SER n 
1 864  LEU n 
1 865  GLU n 
1 866  THR n 
1 867  CYS n 
1 868  MET n 
1 869  TYR n 
1 870  ASP n 
1 871  HIS n 
1 872  LYS n 
1 873  THR n 
1 874  PHE n 
1 875  SER n 
1 876  GLU n 
1 877  ILE n 
1 878  LEU n 
1 879  ASN n 
1 880  ARG n 
1 881  VAL n 
1 882  GLN n 
1 883  LYS n 
1 884  ALA n 
1 885  VAL n 
1 886  ASP n 
1 887  ASP n 
1 888  LEU n 
1 889  ASN n 
1 890  LEU n 
1 891  HIS n 
1 892  SER n 
1 893  TYR n 
1 894  SER n 
1 895  ASN n 
1 896  LEU n 
1 897  PRO n 
1 898  ILE n 
1 899  TRP n 
1 900  VAL n 
1 901  ASN n 
1 902  LYS n 
1 903  LEU n 
1 904  ASP n 
1 905  MET n 
1 906  GLU n 
1 907  ILE n 
1 908  GLU n 
1 909  ARG n 
1 910  ILE n 
1 911  LEU n 
1 912  GLY n 
1 913  VAL n 
1 914  ARG n 
1 915  LEU n 
1 916  GLN n 
1 917  ALA n 
1 918  GLY n 
1 919  LEU n 
1 920  ARG n 
1 921  ALA n 
1 922  TRP n 
1 923  THR n 
1 924  GLN n 
1 925  VAL n 
1 926  LEU n 
1 927  LEU n 
1 928  GLY n 
1 929  GLN n 
1 930  ALA n 
1 931  GLU n 
1 932  ASP n 
1 933  LYS n 
1 934  ALA n 
1 935  GLU n 
1 936  VAL n 
1 937  ASP n 
1 938  MET n 
1 939  ASP n 
1 940  THR n 
1 941  ASP n 
1 942  ALA n 
1 943  PRO n 
1 944  GLN n 
1 945  VAL n 
1 946  SER n 
1 947  HIS n 
1 948  LYS n 
1 949  PRO n 
1 950  GLY n 
1 951  GLY n 
1 952  GLU n 
1 953  PRO n 
1 954  LYS n 
1 955  ILE n 
1 956  LYS n 
1 957  ASN n 
1 958  VAL n 
1 959  VAL n 
1 960  HIS n 
1 961  GLU n 
1 962  LEU n 
1 963  ARG n 
1 964  ILE n 
1 965  THR n 
1 966  ASN n 
1 967  GLN n 
1 968  VAL n 
1 969  ILE n 
1 970  TYR n 
1 971  LEU n 
1 972  ASN n 
1 973  PRO n 
1 974  PRO n 
1 975  ILE n 
1 976  GLU n 
1 977  GLU n 
1 978  CYS n 
1 979  ARG n 
1 980  TYR n 
1 981  LYS n 
1 982  LEU n 
1 983  TYR n 
1 984  GLN n 
1 985  GLU n 
1 986  MET n 
1 987  PHE n 
1 988  ALA n 
1 989  TRP n 
1 990  LYS n 
1 991  MET n 
1 992  VAL n 
1 993  VAL n 
1 994  LEU n 
1 995  SER n 
1 996  LEU n 
1 997  PRO n 
1 998  ARG n 
1 999  ILE n 
1 1000 GLN n 
1 1001 SER n 
1 1002 GLN n 
1 1003 ARG n 
1 1004 TYR n 
1 1005 GLN n 
1 1006 VAL n 
1 1007 GLY n 
1 1008 VAL n 
1 1009 HIS n 
1 1010 TYR n 
1 1011 GLU n 
1 1012 LEU n 
1 1013 THR n 
1 1014 GLU n 
1 1015 GLU n 
1 1016 GLU n 
1 1017 LYS n 
1 1018 PHE n 
1 1019 TYR n 
1 1020 ARG n 
1 1021 ASN n 
1 1022 ALA n 
1 1023 LEU n 
1 1024 THR n 
1 1025 ARG n 
1 1026 MET n 
1 1027 PRO n 
1 1028 ASP n 
1 1029 GLY n 
1 1030 PRO n 
1 1031 VAL n 
1 1032 ALA n 
1 1033 LEU n 
1 1034 GLU n 
1 1035 GLU n 
1 1036 SER n 
1 1037 TYR n 
1 1038 SER n 
1 1039 ALA n 
1 1040 VAL n 
1 1041 MET n 
1 1042 GLY n 
1 1043 ILE n 
1 1044 VAL n 
1 1045 SER n 
1 1046 GLU n 
1 1047 VAL n 
1 1048 GLU n 
1 1049 GLN n 
1 1050 TYR n 
1 1051 VAL n 
1 1052 LYS n 
1 1053 VAL n 
1 1054 TRP n 
1 1055 LEU n 
1 1056 GLN n 
1 1057 TYR n 
1 1058 GLN n 
1 1059 CYS n 
1 1060 LEU n 
1 1061 TRP n 
1 1062 ASP n 
1 1063 MET n 
1 1064 GLN n 
1 1065 ALA n 
1 1066 GLU n 
1 1067 ASN n 
1 1068 ILE n 
1 1069 TYR n 
1 1070 ASN n 
1 1071 ARG n 
1 1072 LEU n 
1 1073 GLY n 
1 1074 GLU n 
1 1075 ASP n 
1 1076 LEU n 
1 1077 ASN n 
1 1078 LYS n 
1 1079 TRP n 
1 1080 GLN n 
1 1081 ALA n 
1 1082 LEU n 
1 1083 LEU n 
1 1084 VAL n 
1 1085 GLN n 
1 1086 ILE n 
1 1087 ARG n 
1 1088 LYS n 
1 1089 ALA n 
1 1090 ARG n 
1 1091 GLY n 
1 1092 THR n 
1 1093 PHE n 
1 1094 ASP n 
1 1095 ASN n 
1 1096 ALA n 
1 1097 GLU n 
1 1098 THR n 
1 1099 LYS n 
1 1100 LYS n 
1 1101 GLU n 
1 1102 PHE n 
1 1103 GLY n 
1 1104 PRO n 
1 1105 VAL n 
1 1106 VAL n 
1 1107 ILE n 
1 1108 ASP n 
1 1109 TYR n 
1 1110 GLY n 
1 1111 LYS n 
1 1112 VAL n 
1 1113 GLN n 
1 1114 SER n 
1 1115 LYS n 
1 1116 VAL n 
1 1117 ASN n 
1 1118 LEU n 
1 1119 LYS n 
1 1120 TYR n 
1 1121 ASP n 
1 1122 SER n 
1 1123 TRP n 
1 1124 HIS n 
1 1125 LYS n 
1 1126 GLU n 
1 1127 VAL n 
1 1128 LEU n 
1 1129 SER n 
1 1130 LYS n 
1 1131 PHE n 
1 1132 GLY n 
1 1133 GLN n 
1 1134 MET n 
1 1135 LEU n 
1 1136 GLY n 
1 1137 SER n 
1 1138 ASN n 
1 1139 MET n 
1 1140 THR n 
1 1141 GLU n 
1 1142 PHE n 
1 1143 HIS n 
1 1144 SER n 
1 1145 GLN n 
1 1146 ILE n 
1 1147 SER n 
1 1148 LYS n 
1 1149 SER n 
1 1150 ARG n 
1 1151 GLN n 
1 1152 GLU n 
1 1153 LEU n 
1 1154 GLU n 
1 1155 GLN n 
1 1156 HIS n 
1 1157 SER n 
1 1158 VAL n 
1 1159 ASP n 
1 1160 THR n 
1 1161 ALA n 
1 1162 SER n 
1 1163 THR n 
1 1164 SER n 
1 1165 ASP n 
1 1166 ALA n 
1 1167 VAL n 
1 1168 THR n 
1 1169 PHE n 
1 1170 ILE n 
1 1171 THR n 
1 1172 TYR n 
1 1173 VAL n 
1 1174 GLN n 
1 1175 SER n 
1 1176 LEU n 
1 1177 LYS n 
1 1178 ARG n 
1 1179 LYS n 
1 1180 ILE n 
1 1181 LYS n 
1 1182 GLN n 
1 1183 PHE n 
1 1184 GLU n 
1 1185 LYS n 
1 1186 GLN n 
1 1187 VAL n 
1 1188 GLU n 
1 1189 LEU n 
1 1190 TYR n 
1 1191 ARG n 
1 1192 ASN n 
1 1193 GLY n 
1 1194 GLN n 
1 1195 ARG n 
1 1196 LEU n 
1 1197 LEU n 
1 1198 GLU n 
1 1199 LYS n 
1 1200 GLN n 
1 1201 ARG n 
1 1202 PHE n 
1 1203 GLN n 
1 1204 PHE n 
1 1205 PRO n 
1 1206 PRO n 
1 1207 SER n 
1 1208 TRP n 
1 1209 LEU n 
1 1210 TYR n 
1 1211 ILE n 
1 1212 ASP n 
1 1213 ASN n 
1 1214 ILE n 
1 1215 GLU n 
1 1216 GLY n 
1 1217 GLU n 
1 1218 TRP n 
1 1219 GLY n 
1 1220 ALA n 
1 1221 PHE n 
1 1222 ASN n 
1 1223 ASP n 
1 1224 ILE n 
1 1225 MET n 
1 1226 ARG n 
1 1227 ARG n 
1 1228 LYS n 
1 1229 ASP n 
1 1230 SER n 
1 1231 ALA n 
1 1232 ILE n 
1 1233 GLN n 
1 1234 GLN n 
1 1235 GLN n 
1 1236 VAL n 
1 1237 ALA n 
1 1238 ASN n 
1 1239 LEU n 
1 1240 GLN n 
1 1241 MET n 
1 1242 LYS n 
1 1243 ILE n 
1 1244 VAL n 
1 1245 GLN n 
1 1246 GLU n 
1 1247 ASP n 
1 1248 ARG n 
1 1249 ALA n 
1 1250 VAL n 
1 1251 GLU n 
1 1252 SER n 
1 1253 ARG n 
1 1254 THR n 
1 1255 THR n 
1 1256 ASP n 
1 1257 LEU n 
1 1258 LEU n 
1 1259 THR n 
1 1260 ASP n 
1 1261 TRP n 
1 1262 GLU n 
1 1263 LYS n 
1 1264 THR n 
1 1265 LYS n 
1 1266 PRO n 
1 1267 VAL n 
1 1268 THR n 
1 1269 GLY n 
1 1270 ASN n 
1 1271 LEU n 
1 1272 ARG n 
1 1273 PRO n 
1 1274 GLU n 
1 1275 GLU n 
1 1276 ALA n 
1 1277 LEU n 
1 1278 GLN n 
1 1279 ALA n 
1 1280 LEU n 
1 1281 THR n 
1 1282 ILE n 
1 1283 TYR n 
1 1284 GLU n 
1 1285 GLY n 
1 1286 LYS n 
1 1287 PHE n 
1 1288 GLY n 
1 1289 ARG n 
1 1290 LEU n 
1 1291 LYS n 
1 1292 ASP n 
1 1293 ASP n 
1 1294 ARG n 
1 1295 GLU n 
1 1296 LYS n 
1 1297 CYS n 
1 1298 ALA n 
1 1299 LYS n 
1 1300 ALA n 
1 1301 LYS n 
1 1302 GLU n 
1 1303 ALA n 
1 1304 LEU n 
1 1305 GLU n 
1 1306 LEU n 
1 1307 THR n 
1 1308 ASP n 
1 1309 THR n 
1 1310 GLY n 
1 1311 LEU n 
1 1312 LEU n 
1 1313 SER n 
1 1314 GLY n 
1 1315 SER n 
1 1316 GLU n 
1 1317 GLU n 
1 1318 ARG n 
1 1319 VAL n 
1 1320 GLN n 
1 1321 VAL n 
1 1322 ALA n 
1 1323 LEU n 
1 1324 GLU n 
1 1325 GLU n 
1 1326 LEU n 
1 1327 GLN n 
1 1328 ASP n 
1 1329 LEU n 
1 1330 LYS n 
1 1331 GLY n 
1 1332 VAL n 
1 1333 TRP n 
1 1334 SER n 
1 1335 GLU n 
1 1336 LEU n 
1 1337 SER n 
1 1338 LYS n 
1 1339 VAL n 
1 1340 TRP n 
1 1341 GLU n 
1 1342 GLN n 
1 1343 ILE n 
1 1344 ASP n 
1 1345 GLN n 
1 1346 MET n 
1 1347 LYS n 
1 1348 GLU n 
1 1349 GLN n 
1 1350 PRO n 
1 1351 TRP n 
1 1352 VAL n 
1 1353 SER n 
1 1354 VAL n 
1 1355 GLN n 
1 1356 PRO n 
1 1357 ARG n 
1 1358 LYS n 
1 1359 LEU n 
1 1360 ARG n 
1 1361 GLN n 
1 1362 ASN n 
1 1363 LEU n 
1 1364 ASP n 
1 1365 ALA n 
1 1366 LEU n 
1 1367 LEU n 
1 1368 ASN n 
1 1369 GLN n 
1 1370 LEU n 
1 1371 LYS n 
1 1372 SER n 
1 1373 PHE n 
1 1374 PRO n 
1 1375 ALA n 
1 1376 ARG n 
1 1377 LEU n 
1 1378 ARG n 
1 1379 GLN n 
1 1380 TYR n 
1 1381 ALA n 
1 1382 SER n 
1 1383 TYR n 
1 1384 GLU n 
1 1385 PHE n 
1 1386 VAL n 
1 1387 GLN n 
1 1388 ARG n 
1 1389 LEU n 
1 1390 LEU n 
1 1391 LYS n 
1 1392 GLY n 
1 1393 TYR n 
1 1394 MET n 
1 1395 LYS n 
1 1396 ILE n 
1 1397 ASN n 
1 1398 MET n 
1 1399 LEU n 
1 1400 VAL n 
1 1401 ILE n 
1 1402 GLU n 
1 1403 LEU n 
1 1404 LYS n 
1 1405 SER n 
1 1406 GLU n 
1 1407 ALA n 
1 1408 LEU n 
1 1409 LYS n 
1 1410 ASP n 
1 1411 ARG n 
1 1412 HIS n 
1 1413 TRP n 
1 1414 LYS n 
1 1415 GLN n 
1 1416 LEU n 
1 1417 MET n 
1 1418 LYS n 
1 1419 ARG n 
1 1420 LEU n 
1 1421 HIS n 
1 1422 VAL n 
1 1423 ASN n 
1 1424 TRP n 
1 1425 VAL n 
1 1426 VAL n 
1 1427 SER n 
1 1428 GLU n 
1 1429 LEU n 
1 1430 THR n 
1 1431 LEU n 
1 1432 GLY n 
1 1433 GLN n 
1 1434 ILE n 
1 1435 TRP n 
1 1436 ASP n 
1 1437 VAL n 
1 1438 ASP n 
1 1439 LEU n 
1 1440 GLN n 
1 1441 LYS n 
1 1442 ASN n 
1 1443 GLU n 
1 1444 ALA n 
1 1445 ILE n 
1 1446 VAL n 
1 1447 LYS n 
1 1448 ASP n 
1 1449 VAL n 
1 1450 LEU n 
1 1451 LEU n 
1 1452 VAL n 
1 1453 ALA n 
1 1454 GLN n 
1 1455 GLY n 
1 1456 GLU n 
1 1457 MET n 
1 1458 ALA n 
1 1459 LEU n 
1 1460 GLU n 
1 1461 GLU n 
1 1462 PHE n 
1 1463 LEU n 
1 1464 LYS n 
1 1465 GLN n 
1 1466 ILE n 
1 1467 ARG n 
1 1468 GLU n 
1 1469 VAL n 
1 1470 TRP n 
1 1471 ASN n 
1 1472 THR n 
1 1473 TYR n 
1 1474 GLU n 
1 1475 LEU n 
1 1476 ASP n 
1 1477 LEU n 
1 1478 VAL n 
1 1479 ASN n 
1 1480 TYR n 
1 1481 GLN n 
1 1482 ASN n 
1 1483 LYS n 
1 1484 CYS n 
1 1485 ARG n 
1 1486 LEU n 
1 1487 ILE n 
1 1488 ARG n 
1 1489 GLY n 
1 1490 TRP n 
1 1491 ASP n 
1 1492 ASP n 
1 1493 LEU n 
1 1494 PHE n 
1 1495 ASN n 
1 1496 LYS n 
1 1497 VAL n 
1 1498 LYS n 
1 1499 GLU n 
1 1500 HIS n 
1 1501 ILE n 
1 1502 ASN n 
1 1503 SER n 
1 1504 VAL n 
1 1505 SER n 
1 1506 ALA n 
1 1507 MET n 
1 1508 LYS n 
1 1509 LEU n 
1 1510 SER n 
1 1511 PRO n 
1 1512 TYR n 
1 1513 TYR n 
1 1514 LYS n 
1 1515 VAL n 
1 1516 PHE n 
1 1517 GLU n 
1 1518 GLU n 
1 1519 ASP n 
1 1520 ALA n 
1 1521 LEU n 
1 1522 SER n 
1 1523 TRP n 
1 1524 GLU n 
1 1525 ASP n 
1 1526 LYS n 
1 1527 LEU n 
1 1528 ASN n 
1 1529 ARG n 
1 1530 ILE n 
1 1531 MET n 
1 1532 ALA n 
1 1533 LEU n 
1 1534 PHE n 
1 1535 ASP n 
1 1536 VAL n 
1 1537 TRP n 
1 1538 ILE n 
1 1539 ASP n 
1 1540 VAL n 
1 1541 GLN n 
1 1542 ARG n 
1 1543 ARG n 
1 1544 TRP n 
1 1545 VAL n 
1 1546 TYR n 
1 1547 LEU n 
1 1548 GLU n 
1 1549 GLY n 
1 1550 ILE n 
1 1551 PHE n 
1 1552 THR n 
1 1553 GLY n 
1 1554 SER n 
1 1555 ALA n 
1 1556 ASP n 
1 1557 ILE n 
1 1558 LYS n 
1 1559 HIS n 
1 1560 LEU n 
1 1561 LEU n 
1 1562 PRO n 
1 1563 VAL n 
1 1564 GLU n 
1 1565 THR n 
1 1566 GLN n 
1 1567 ARG n 
1 1568 PHE n 
1 1569 GLN n 
1 1570 SER n 
1 1571 ILE n 
1 1572 SER n 
1 1573 THR n 
1 1574 GLU n 
1 1575 PHE n 
1 1576 LEU n 
1 1577 ALA n 
1 1578 LEU n 
1 1579 MET n 
1 1580 LYS n 
1 1581 LYS n 
1 1582 VAL n 
1 1583 SER n 
1 1584 LYS n 
1 1585 SER n 
1 1586 PRO n 
1 1587 LEU n 
1 1588 VAL n 
1 1589 MET n 
1 1590 ASP n 
1 1591 VAL n 
1 1592 LEU n 
1 1593 ASN n 
1 1594 ILE n 
1 1595 GLN n 
1 1596 GLY n 
1 1597 VAL n 
1 1598 GLN n 
1 1599 ARG n 
1 1600 SER n 
1 1601 LEU n 
1 1602 GLU n 
1 1603 ARG n 
1 1604 LEU n 
1 1605 ALA n 
1 1606 ASP n 
1 1607 LEU n 
1 1608 LEU n 
1 1609 GLY n 
1 1610 LYS n 
1 1611 ILE n 
1 1612 GLN n 
1 1613 LYS n 
1 1614 ALA n 
1 1615 LEU n 
1 1616 GLY n 
1 1617 GLU n 
1 1618 TYR n 
1 1619 LEU n 
1 1620 GLU n 
1 1621 ARG n 
1 1622 GLU n 
1 1623 ARG n 
1 1624 SER n 
1 1625 SER n 
1 1626 PHE n 
1 1627 PRO n 
1 1628 ARG n 
1 1629 PHE n 
1 1630 TYR n 
1 1631 PHE n 
1 1632 VAL n 
1 1633 GLY n 
1 1634 ASP n 
1 1635 GLU n 
1 1636 ASP n 
1 1637 LEU n 
1 1638 LEU n 
1 1639 GLU n 
1 1640 ILE n 
1 1641 ILE n 
1 1642 GLY n 
1 1643 ASN n 
1 1644 SER n 
1 1645 LYS n 
1 1646 ASN n 
1 1647 VAL n 
1 1648 ALA n 
1 1649 LYS n 
1 1650 LEU n 
1 1651 GLN n 
1 1652 LYS n 
1 1653 HIS n 
1 1654 PHE n 
1 1655 LYS n 
1 1656 LYS n 
1 1657 MET n 
1 1658 PHE n 
1 1659 ALA n 
1 1660 GLY n 
1 1661 VAL n 
1 1662 SER n 
1 1663 SER n 
1 1664 ILE n 
1 1665 ILE n 
1 1666 LEU n 
1 1667 ASN n 
1 1668 GLU n 
1 1669 ASP n 
1 1670 ASN n 
1 1671 SER n 
1 1672 VAL n 
1 1673 VAL n 
1 1674 LEU n 
1 1675 GLY n 
1 1676 ILE n 
1 1677 SER n 
1 1678 SER n 
1 1679 ARG n 
1 1680 GLU n 
1 1681 GLY n 
1 1682 GLU n 
1 1683 GLU n 
1 1684 VAL n 
1 1685 MET n 
1 1686 PHE n 
1 1687 LYS n 
1 1688 THR n 
1 1689 PRO n 
1 1690 VAL n 
1 1691 SER n 
1 1692 ILE n 
1 1693 THR n 
1 1694 GLU n 
1 1695 HIS n 
1 1696 PRO n 
1 1697 LYS n 
1 1698 ILE n 
1 1699 ASN n 
1 1700 GLU n 
1 1701 TRP n 
1 1702 LEU n 
1 1703 THR n 
1 1704 LEU n 
1 1705 VAL n 
1 1706 GLU n 
1 1707 LYS n 
1 1708 GLU n 
1 1709 MET n 
1 1710 ARG n 
1 1711 VAL n 
1 1712 THR n 
1 1713 LEU n 
1 1714 ALA n 
1 1715 LYS n 
1 1716 LEU n 
1 1717 LEU n 
1 1718 ALA n 
1 1719 GLU n 
1 1720 SER n 
1 1721 VAL n 
1 1722 THR n 
1 1723 GLU n 
1 1724 VAL n 
1 1725 GLU n 
1 1726 ILE n 
1 1727 PHE n 
1 1728 GLY n 
1 1729 LYS n 
1 1730 ALA n 
1 1731 THR n 
1 1732 SER n 
1 1733 ILE n 
1 1734 ASP n 
1 1735 PRO n 
1 1736 ASN n 
1 1737 THR n 
1 1738 TYR n 
1 1739 ILE n 
1 1740 THR n 
1 1741 TRP n 
1 1742 ILE n 
1 1743 ASP n 
1 1744 LYS n 
1 1745 TYR n 
1 1746 GLN n 
1 1747 ALA n 
1 1748 GLN n 
1 1749 LEU n 
1 1750 VAL n 
1 1751 VAL n 
1 1752 LEU n 
1 1753 SER n 
1 1754 ALA n 
1 1755 GLN n 
1 1756 ILE n 
1 1757 ALA n 
1 1758 TRP n 
1 1759 SER n 
1 1760 GLU n 
1 1761 ASN n 
1 1762 VAL n 
1 1763 GLU n 
1 1764 THR n 
1 1765 ALA n 
1 1766 LEU n 
1 1767 SER n 
1 1768 SER n 
1 1769 MET n 
1 1770 GLY n 
1 1771 GLY n 
1 1772 GLY n 
1 1773 GLY n 
1 1774 ASP n 
1 1775 ALA n 
1 1776 ALA n 
1 1777 PRO n 
1 1778 LEU n 
1 1779 HIS n 
1 1780 SER n 
1 1781 VAL n 
1 1782 LEU n 
1 1783 SER n 
1 1784 ASN n 
1 1785 VAL n 
1 1786 GLU n 
1 1787 VAL n 
1 1788 THR n 
1 1789 LEU n 
1 1790 ASN n 
1 1791 VAL n 
1 1792 LEU n 
1 1793 ALA n 
1 1794 ASP n 
1 1795 SER n 
1 1796 VAL n 
1 1797 LEU n 
1 1798 MET n 
1 1799 GLU n 
1 1800 GLN n 
1 1801 PRO n 
1 1802 PRO n 
1 1803 LEU n 
1 1804 ARG n 
1 1805 ARG n 
1 1806 ARG n 
1 1807 LYS n 
1 1808 LEU n 
1 1809 GLU n 
1 1810 HIS n 
1 1811 LEU n 
1 1812 ILE n 
1 1813 THR n 
1 1814 GLU n 
1 1815 LEU n 
1 1816 VAL n 
1 1817 HIS n 
1 1818 GLN n 
1 1819 ARG n 
1 1820 ASP n 
1 1821 VAL n 
1 1822 THR n 
1 1823 ARG n 
1 1824 SER n 
1 1825 LEU n 
1 1826 ILE n 
1 1827 LYS n 
1 1828 SER n 
1 1829 LYS n 
1 1830 ILE n 
1 1831 ASP n 
1 1832 ASN n 
1 1833 ALA n 
1 1834 LYS n 
1 1835 SER n 
1 1836 PHE n 
1 1837 GLU n 
1 1838 TRP n 
1 1839 LEU n 
1 1840 SER n 
1 1841 GLN n 
1 1842 MET n 
1 1843 ARG n 
1 1844 PHE n 
1 1845 TYR n 
1 1846 PHE n 
1 1847 ASP n 
1 1848 PRO n 
1 1849 LYS n 
1 1850 GLN n 
1 1851 THR n 
1 1852 ASP n 
1 1853 VAL n 
1 1854 LEU n 
1 1855 GLN n 
1 1856 GLN n 
1 1857 LEU n 
1 1858 SER n 
1 1859 ILE n 
1 1860 GLN n 
1 1861 MET n 
1 1862 ALA n 
1 1863 ASN n 
1 1864 ALA n 
1 1865 LYS n 
1 1866 PHE n 
1 1867 ASN n 
1 1868 TYR n 
1 1869 GLY n 
1 1870 PHE n 
1 1871 GLU n 
1 1872 TYR n 
1 1873 LEU n 
1 1874 GLY n 
1 1875 VAL n 
1 1876 GLN n 
1 1877 ASP n 
1 1878 LYS n 
1 1879 LEU n 
1 1880 VAL n 
1 1881 GLN n 
1 1882 THR n 
1 1883 PRO n 
1 1884 LEU n 
1 1885 THR n 
1 1886 ASP n 
1 1887 ARG n 
1 1888 CYS n 
1 1889 TYR n 
1 1890 LEU n 
1 1891 THR n 
1 1892 MET n 
1 1893 THR n 
1 1894 GLN n 
1 1895 ALA n 
1 1896 LEU n 
1 1897 GLU n 
1 1898 ALA n 
1 1899 ARG n 
1 1900 LEU n 
1 1901 GLY n 
1 1902 GLY n 
1 1903 SER n 
1 1904 PRO n 
1 1905 PHE n 
1 1906 GLY n 
1 1907 PRO n 
1 1908 ALA n 
1 1909 GLY n 
1 1910 THR n 
1 1911 GLY n 
1 1912 LYS n 
1 1913 THR n 
1 1914 GLU n 
1 1915 SER n 
1 1916 VAL n 
1 1917 LYS n 
1 1918 ALA n 
1 1919 LEU n 
1 1920 GLY n 
1 1921 HIS n 
1 1922 GLN n 
1 1923 LEU n 
1 1924 GLY n 
1 1925 ARG n 
1 1926 PHE n 
1 1927 VAL n 
1 1928 LEU n 
1 1929 VAL n 
1 1930 PHE n 
1 1931 ASN n 
1 1932 CYS n 
1 1933 ASP n 
1 1934 GLU n 
1 1935 THR n 
1 1936 PHE n 
1 1937 ASP n 
1 1938 PHE n 
1 1939 GLN n 
1 1940 ALA n 
1 1941 MET n 
1 1942 GLY n 
1 1943 ARG n 
1 1944 ILE n 
1 1945 PHE n 
1 1946 VAL n 
1 1947 GLY n 
1 1948 LEU n 
1 1949 CYS n 
1 1950 GLN n 
1 1951 VAL n 
1 1952 GLY n 
1 1953 ALA n 
1 1954 TRP n 
1 1955 GLY n 
1 1956 CYS n 
1 1957 PHE n 
1 1958 ASP n 
1 1959 GLU n 
1 1960 PHE n 
1 1961 ASN n 
1 1962 ARG n 
1 1963 LEU n 
1 1964 GLU n 
1 1965 GLU n 
1 1966 ARG n 
1 1967 MET n 
1 1968 LEU n 
1 1969 SER n 
1 1970 ALA n 
1 1971 VAL n 
1 1972 SER n 
1 1973 GLN n 
1 1974 GLN n 
1 1975 VAL n 
1 1976 GLN n 
1 1977 CYS n 
1 1978 ILE n 
1 1979 GLN n 
1 1980 GLU n 
1 1981 ALA n 
1 1982 LEU n 
1 1983 ARG n 
1 1984 GLU n 
1 1985 HIS n 
1 1986 SER n 
1 1987 ASN n 
1 1988 PRO n 
1 1989 ASN n 
1 1990 TYR n 
1 1991 ASP n 
1 1992 LYS n 
1 1993 THR n 
1 1994 SER n 
1 1995 ALA n 
1 1996 PRO n 
1 1997 ILE n 
1 1998 THR n 
1 1999 CYS n 
1 2000 GLU n 
1 2001 LEU n 
1 2002 LEU n 
1 2003 ASN n 
1 2004 LYS n 
1 2005 GLN n 
1 2006 VAL n 
1 2007 LYS n 
1 2008 VAL n 
1 2009 SER n 
1 2010 PRO n 
1 2011 ASP n 
1 2012 MET n 
1 2013 ALA n 
1 2014 ILE n 
1 2015 PHE n 
1 2016 ILE n 
1 2017 THR n 
1 2018 MET n 
1 2019 ASN n 
1 2020 PRO n 
1 2021 GLY n 
1 2022 TYR n 
1 2023 ALA n 
1 2024 GLY n 
1 2025 ARG n 
1 2026 SER n 
1 2027 ASN n 
1 2028 LEU n 
1 2029 PRO n 
1 2030 ASP n 
1 2031 ASN n 
1 2032 LEU n 
1 2033 LYS n 
1 2034 LYS n 
1 2035 LEU n 
1 2036 PHE n 
1 2037 ARG n 
1 2038 SER n 
1 2039 LEU n 
1 2040 ALA n 
1 2041 MET n 
1 2042 THR n 
1 2043 LYS n 
1 2044 PRO n 
1 2045 ASP n 
1 2046 ARG n 
1 2047 GLN n 
1 2048 LEU n 
1 2049 ILE n 
1 2050 ALA n 
1 2051 GLN n 
1 2052 VAL n 
1 2053 MET n 
1 2054 LEU n 
1 2055 TYR n 
1 2056 SER n 
1 2057 GLN n 
1 2058 GLY n 
1 2059 PHE n 
1 2060 ARG n 
1 2061 THR n 
1 2062 ALA n 
1 2063 GLU n 
1 2064 VAL n 
1 2065 LEU n 
1 2066 ALA n 
1 2067 ASN n 
1 2068 LYS n 
1 2069 ILE n 
1 2070 VAL n 
1 2071 PRO n 
1 2072 PHE n 
1 2073 PHE n 
1 2074 LYS n 
1 2075 LEU n 
1 2076 CYS n 
1 2077 ASP n 
1 2078 GLU n 
1 2079 GLN n 
1 2080 LEU n 
1 2081 SER n 
1 2082 SER n 
1 2083 GLN n 
1 2084 SER n 
1 2085 HIS n 
1 2086 TYR n 
1 2087 ASP n 
1 2088 PHE n 
1 2089 GLY n 
1 2090 LEU n 
1 2091 ARG n 
1 2092 ALA n 
1 2093 LEU n 
1 2094 LYS n 
1 2095 SER n 
1 2096 VAL n 
1 2097 LEU n 
1 2098 VAL n 
1 2099 SER n 
1 2100 ALA n 
1 2101 GLY n 
1 2102 ASN n 
1 2103 VAL n 
1 2104 LYS n 
1 2105 ARG n 
1 2106 GLU n 
1 2107 ARG n 
1 2108 ILE n 
1 2109 GLN n 
1 2110 LYS n 
1 2111 ILE n 
1 2112 LYS n 
1 2113 ARG n 
1 2114 GLU n 
1 2115 LYS n 
1 2116 GLU n 
1 2117 GLU n 
1 2118 ARG n 
1 2119 GLY n 
1 2120 GLU n 
1 2121 ALA n 
1 2122 VAL n 
1 2123 ASP n 
1 2124 GLU n 
1 2125 GLY n 
1 2126 GLU n 
1 2127 ILE n 
1 2128 ALA n 
1 2129 GLU n 
1 2130 ASN n 
1 2131 LEU n 
1 2132 PRO n 
1 2133 GLU n 
1 2134 GLN n 
1 2135 GLU n 
1 2136 ILE n 
1 2137 LEU n 
1 2138 ILE n 
1 2139 GLN n 
1 2140 SER n 
1 2141 VAL n 
1 2142 CYS n 
1 2143 GLU n 
1 2144 THR n 
1 2145 MET n 
1 2146 VAL n 
1 2147 PRO n 
1 2148 LYS n 
1 2149 LEU n 
1 2150 VAL n 
1 2151 ALA n 
1 2152 GLU n 
1 2153 ASP n 
1 2154 ILE n 
1 2155 PRO n 
1 2156 LEU n 
1 2157 LEU n 
1 2158 PHE n 
1 2159 SER n 
1 2160 LEU n 
1 2161 LEU n 
1 2162 SER n 
1 2163 ASP n 
1 2164 VAL n 
1 2165 PHE n 
1 2166 PRO n 
1 2167 GLY n 
1 2168 VAL n 
1 2169 GLN n 
1 2170 TYR n 
1 2171 HIS n 
1 2172 ARG n 
1 2173 GLY n 
1 2174 GLU n 
1 2175 MET n 
1 2176 THR n 
1 2177 ALA n 
1 2178 LEU n 
1 2179 ARG n 
1 2180 GLU n 
1 2181 GLU n 
1 2182 LEU n 
1 2183 LYS n 
1 2184 LYS n 
1 2185 VAL n 
1 2186 CYS n 
1 2187 GLN n 
1 2188 GLU n 
1 2189 MET n 
1 2190 TYR n 
1 2191 LEU n 
1 2192 THR n 
1 2193 TYR n 
1 2194 GLY n 
1 2195 ASP n 
1 2196 GLY n 
1 2197 GLU n 
1 2198 GLU n 
1 2199 VAL n 
1 2200 GLY n 
1 2201 GLY n 
1 2202 MET n 
1 2203 TRP n 
1 2204 VAL n 
1 2205 GLU n 
1 2206 LYS n 
1 2207 VAL n 
1 2208 LEU n 
1 2209 GLN n 
1 2210 LEU n 
1 2211 TYR n 
1 2212 GLN n 
1 2213 ILE n 
1 2214 THR n 
1 2215 GLN n 
1 2216 ILE n 
1 2217 ASN n 
1 2218 HIS n 
1 2219 GLY n 
1 2220 LEU n 
1 2221 MET n 
1 2222 MET n 
1 2223 VAL n 
1 2224 GLY n 
1 2225 PRO n 
1 2226 SER n 
1 2227 GLY n 
1 2228 SER n 
1 2229 GLY n 
1 2230 LYS n 
1 2231 SER n 
1 2232 MET n 
1 2233 ALA n 
1 2234 TRP n 
1 2235 ARG n 
1 2236 VAL n 
1 2237 LEU n 
1 2238 LEU n 
1 2239 LYS n 
1 2240 ALA n 
1 2241 LEU n 
1 2242 GLU n 
1 2243 ARG n 
1 2244 LEU n 
1 2245 GLU n 
1 2246 GLY n 
1 2247 VAL n 
1 2248 GLU n 
1 2249 GLY n 
1 2250 VAL n 
1 2251 ALA n 
1 2252 HIS n 
1 2253 ILE n 
1 2254 ILE n 
1 2255 ASP n 
1 2256 PRO n 
1 2257 LYS n 
1 2258 ALA n 
1 2259 ILE n 
1 2260 SER n 
1 2261 LYS n 
1 2262 ASP n 
1 2263 HIS n 
1 2264 LEU n 
1 2265 TYR n 
1 2266 GLY n 
1 2267 THR n 
1 2268 LEU n 
1 2269 ASP n 
1 2270 PRO n 
1 2271 ASN n 
1 2272 THR n 
1 2273 ARG n 
1 2274 GLU n 
1 2275 TRP n 
1 2276 THR n 
1 2277 ASP n 
1 2278 GLY n 
1 2279 LEU n 
1 2280 PHE n 
1 2281 THR n 
1 2282 HIS n 
1 2283 VAL n 
1 2284 LEU n 
1 2285 ARG n 
1 2286 LYS n 
1 2287 ILE n 
1 2288 ILE n 
1 2289 ASP n 
1 2290 SER n 
1 2291 VAL n 
1 2292 ARG n 
1 2293 GLY n 
1 2294 GLU n 
1 2295 LEU n 
1 2296 GLN n 
1 2297 LYS n 
1 2298 ARG n 
1 2299 GLN n 
1 2300 TRP n 
1 2301 ILE n 
1 2302 VAL n 
1 2303 PHE n 
1 2304 ASP n 
1 2305 GLY n 
1 2306 ASP n 
1 2307 VAL n 
1 2308 ASP n 
1 2309 PRO n 
1 2310 GLU n 
1 2311 TRP n 
1 2312 VAL n 
1 2313 GLU n 
1 2314 ASN n 
1 2315 LEU n 
1 2316 ASN n 
1 2317 SER n 
1 2318 VAL n 
1 2319 LEU n 
1 2320 ASP n 
1 2321 ASP n 
1 2322 ASN n 
1 2323 LYS n 
1 2324 LEU n 
1 2325 LEU n 
1 2326 THR n 
1 2327 LEU n 
1 2328 PRO n 
1 2329 ASN n 
1 2330 GLY n 
1 2331 GLU n 
1 2332 ARG n 
1 2333 LEU n 
1 2334 SER n 
1 2335 LEU n 
1 2336 PRO n 
1 2337 PRO n 
1 2338 ASN n 
1 2339 VAL n 
1 2340 ARG n 
1 2341 ILE n 
1 2342 MET n 
1 2343 PHE n 
1 2344 GLU n 
1 2345 VAL n 
1 2346 GLN n 
1 2347 ASP n 
1 2348 LEU n 
1 2349 LYS n 
1 2350 TYR n 
1 2351 ALA n 
1 2352 THR n 
1 2353 LEU n 
1 2354 ALA n 
1 2355 THR n 
1 2356 VAL n 
1 2357 SER n 
1 2358 ARG n 
1 2359 CYS n 
1 2360 GLY n 
1 2361 MET n 
1 2362 VAL n 
1 2363 TRP n 
1 2364 PHE n 
1 2365 SER n 
1 2366 GLU n 
1 2367 ASP n 
1 2368 VAL n 
1 2369 LEU n 
1 2370 SER n 
1 2371 THR n 
1 2372 ASP n 
1 2373 MET n 
1 2374 ILE n 
1 2375 PHE n 
1 2376 ASN n 
1 2377 ASN n 
1 2378 PHE n 
1 2379 LEU n 
1 2380 ALA n 
1 2381 ARG n 
1 2382 LEU n 
1 2383 ARG n 
1 2384 SER n 
1 2385 ILE n 
1 2386 PRO n 
1 2387 LEU n 
1 2388 ASP n 
1 2389 GLU n 
1 2390 GLY n 
1 2391 GLU n 
1 2392 ASP n 
1 2393 GLU n 
1 2394 ALA n 
1 2395 GLN n 
1 2396 ARG n 
1 2397 ARG n 
1 2398 ARG n 
1 2399 LYS n 
1 2400 GLY n 
1 2401 LYS n 
1 2402 GLU n 
1 2403 ASP n 
1 2404 GLU n 
1 2405 GLY n 
1 2406 GLU n 
1 2407 GLU n 
1 2408 ALA n 
1 2409 ALA n 
1 2410 SER n 
1 2411 PRO n 
1 2412 MET n 
1 2413 LEU n 
1 2414 GLN n 
1 2415 ILE n 
1 2416 GLN n 
1 2417 ARG n 
1 2418 ASP n 
1 2419 ALA n 
1 2420 ALA n 
1 2421 THR n 
1 2422 ILE n 
1 2423 MET n 
1 2424 GLN n 
1 2425 PRO n 
1 2426 TYR n 
1 2427 PHE n 
1 2428 THR n 
1 2429 SER n 
1 2430 ASN n 
1 2431 GLY n 
1 2432 LEU n 
1 2433 VAL n 
1 2434 THR n 
1 2435 LYS n 
1 2436 ALA n 
1 2437 LEU n 
1 2438 GLU n 
1 2439 HIS n 
1 2440 ALA n 
1 2441 PHE n 
1 2442 GLN n 
1 2443 LEU n 
1 2444 GLU n 
1 2445 HIS n 
1 2446 ILE n 
1 2447 MET n 
1 2448 ASP n 
1 2449 LEU n 
1 2450 THR n 
1 2451 ARG n 
1 2452 LEU n 
1 2453 ARG n 
1 2454 CYS n 
1 2455 LEU n 
1 2456 GLY n 
1 2457 SER n 
1 2458 LEU n 
1 2459 PHE n 
1 2460 SER n 
1 2461 MET n 
1 2462 LEU n 
1 2463 HIS n 
1 2464 GLN n 
1 2465 ALA n 
1 2466 CYS n 
1 2467 ARG n 
1 2468 ASN n 
1 2469 VAL n 
1 2470 ALA n 
1 2471 GLN n 
1 2472 TYR n 
1 2473 ASN n 
1 2474 ALA n 
1 2475 ASN n 
1 2476 HIS n 
1 2477 PRO n 
1 2478 ASP n 
1 2479 PHE n 
1 2480 PRO n 
1 2481 MET n 
1 2482 GLN n 
1 2483 ILE n 
1 2484 GLU n 
1 2485 GLN n 
1 2486 LEU n 
1 2487 GLU n 
1 2488 ARG n 
1 2489 TYR n 
1 2490 ILE n 
1 2491 GLN n 
1 2492 ARG n 
1 2493 TYR n 
1 2494 LEU n 
1 2495 VAL n 
1 2496 TYR n 
1 2497 ALA n 
1 2498 ILE n 
1 2499 LEU n 
1 2500 TRP n 
1 2501 SER n 
1 2502 LEU n 
1 2503 SER n 
1 2504 GLY n 
1 2505 ASP n 
1 2506 SER n 
1 2507 ARG n 
1 2508 LEU n 
1 2509 LYS n 
1 2510 MET n 
1 2511 ARG n 
1 2512 ALA n 
1 2513 GLU n 
1 2514 LEU n 
1 2515 GLY n 
1 2516 GLU n 
1 2517 TYR n 
1 2518 ILE n 
1 2519 ARG n 
1 2520 ARG n 
1 2521 ILE n 
1 2522 THR n 
1 2523 THR n 
1 2524 VAL n 
1 2525 PRO n 
1 2526 LEU n 
1 2527 PRO n 
1 2528 THR n 
1 2529 ALA n 
1 2530 PRO n 
1 2531 ASN n 
1 2532 ILE n 
1 2533 PRO n 
1 2534 ILE n 
1 2535 ILE n 
1 2536 ASP n 
1 2537 TYR n 
1 2538 GLU n 
1 2539 VAL n 
1 2540 SER n 
1 2541 ILE n 
1 2542 SER n 
1 2543 GLY n 
1 2544 GLU n 
1 2545 TRP n 
1 2546 SER n 
1 2547 PRO n 
1 2548 TRP n 
1 2549 GLN n 
1 2550 ALA n 
1 2551 LYS n 
1 2552 VAL n 
1 2553 PRO n 
1 2554 GLN n 
1 2555 ILE n 
1 2556 GLU n 
1 2557 VAL n 
1 2558 GLU n 
1 2559 THR n 
1 2560 HIS n 
1 2561 LYS n 
1 2562 VAL n 
1 2563 ALA n 
1 2564 ALA n 
1 2565 PRO n 
1 2566 ASP n 
1 2567 VAL n 
1 2568 VAL n 
1 2569 VAL n 
1 2570 PRO n 
1 2571 THR n 
1 2572 LEU n 
1 2573 ASP n 
1 2574 THR n 
1 2575 VAL n 
1 2576 ARG n 
1 2577 HIS n 
1 2578 GLU n 
1 2579 ALA n 
1 2580 LEU n 
1 2581 LEU n 
1 2582 TYR n 
1 2583 THR n 
1 2584 TRP n 
1 2585 LEU n 
1 2586 ALA n 
1 2587 GLU n 
1 2588 HIS n 
1 2589 LYS n 
1 2590 PRO n 
1 2591 LEU n 
1 2592 VAL n 
1 2593 LEU n 
1 2594 CYS n 
1 2595 GLY n 
1 2596 PRO n 
1 2597 PRO n 
1 2598 GLY n 
1 2599 SER n 
1 2600 GLY n 
1 2601 LYS n 
1 2602 THR n 
1 2603 MET n 
1 2604 THR n 
1 2605 LEU n 
1 2606 PHE n 
1 2607 SER n 
1 2608 ALA n 
1 2609 LEU n 
1 2610 ARG n 
1 2611 ALA n 
1 2612 LEU n 
1 2613 PRO n 
1 2614 ASP n 
1 2615 MET n 
1 2616 GLU n 
1 2617 VAL n 
1 2618 VAL n 
1 2619 GLY n 
1 2620 LEU n 
1 2621 ASN n 
1 2622 PHE n 
1 2623 SER n 
1 2624 SER n 
1 2625 ALA n 
1 2626 THR n 
1 2627 THR n 
1 2628 PRO n 
1 2629 GLU n 
1 2630 LEU n 
1 2631 LEU n 
1 2632 LEU n 
1 2633 LYS n 
1 2634 THR n 
1 2635 PHE n 
1 2636 ASP n 
1 2637 HIS n 
1 2638 TYR n 
1 2639 CYS n 
1 2640 GLU n 
1 2641 TYR n 
1 2642 ARG n 
1 2643 ARG n 
1 2644 THR n 
1 2645 PRO n 
1 2646 ASN n 
1 2647 GLY n 
1 2648 VAL n 
1 2649 VAL n 
1 2650 LEU n 
1 2651 ALA n 
1 2652 PRO n 
1 2653 VAL n 
1 2654 GLN n 
1 2655 LEU n 
1 2656 GLY n 
1 2657 LYS n 
1 2658 TRP n 
1 2659 LEU n 
1 2660 VAL n 
1 2661 LEU n 
1 2662 PHE n 
1 2663 CYS n 
1 2664 ASP n 
1 2665 GLU n 
1 2666 ILE n 
1 2667 ASN n 
1 2668 LEU n 
1 2669 PRO n 
1 2670 ASP n 
1 2671 MET n 
1 2672 ASP n 
1 2673 LYS n 
1 2674 TYR n 
1 2675 GLY n 
1 2676 THR n 
1 2677 GLN n 
1 2678 ARG n 
1 2679 VAL n 
1 2680 ILE n 
1 2681 SER n 
1 2682 PHE n 
1 2683 ILE n 
1 2684 ARG n 
1 2685 GLN n 
1 2686 MET n 
1 2687 VAL n 
1 2688 GLU n 
1 2689 HIS n 
1 2690 GLY n 
1 2691 GLY n 
1 2692 PHE n 
1 2693 TYR n 
1 2694 ARG n 
1 2695 THR n 
1 2696 SER n 
1 2697 ASP n 
1 2698 GLN n 
1 2699 THR n 
1 2700 TRP n 
1 2701 VAL n 
1 2702 LYS n 
1 2703 LEU n 
1 2704 GLU n 
1 2705 ARG n 
1 2706 ILE n 
1 2707 GLN n 
1 2708 PHE n 
1 2709 VAL n 
1 2710 GLY n 
1 2711 ALA n 
1 2712 CYS n 
1 2713 ASN n 
1 2714 PRO n 
1 2715 PRO n 
1 2716 THR n 
1 2717 ASP n 
1 2718 PRO n 
1 2719 GLY n 
1 2720 ARG n 
1 2721 LYS n 
1 2722 PRO n 
1 2723 LEU n 
1 2724 SER n 
1 2725 HIS n 
1 2726 ARG n 
1 2727 PHE n 
1 2728 LEU n 
1 2729 ARG n 
1 2730 HIS n 
1 2731 VAL n 
1 2732 PRO n 
1 2733 VAL n 
1 2734 VAL n 
1 2735 TYR n 
1 2736 VAL n 
1 2737 ASP n 
1 2738 TYR n 
1 2739 PRO n 
1 2740 GLY n 
1 2741 PRO n 
1 2742 ALA n 
1 2743 SER n 
1 2744 LEU n 
1 2745 THR n 
1 2746 GLN n 
1 2747 ILE n 
1 2748 TYR n 
1 2749 GLY n 
1 2750 THR n 
1 2751 PHE n 
1 2752 ASN n 
1 2753 ARG n 
1 2754 ALA n 
1 2755 MET n 
1 2756 LEU n 
1 2757 ARG n 
1 2758 LEU n 
1 2759 ILE n 
1 2760 PRO n 
1 2761 SER n 
1 2762 LEU n 
1 2763 ARG n 
1 2764 THR n 
1 2765 TYR n 
1 2766 ALA n 
1 2767 GLU n 
1 2768 PRO n 
1 2769 LEU n 
1 2770 THR n 
1 2771 ALA n 
1 2772 ALA n 
1 2773 MET n 
1 2774 VAL n 
1 2775 GLU n 
1 2776 PHE n 
1 2777 TYR n 
1 2778 THR n 
1 2779 MET n 
1 2780 SER n 
1 2781 GLN n 
1 2782 GLU n 
1 2783 ARG n 
1 2784 PHE n 
1 2785 THR n 
1 2786 GLN n 
1 2787 ASP n 
1 2788 THR n 
1 2789 GLN n 
1 2790 PRO n 
1 2791 HIS n 
1 2792 TYR n 
1 2793 ILE n 
1 2794 TYR n 
1 2795 SER n 
1 2796 PRO n 
1 2797 ARG n 
1 2798 GLU n 
1 2799 MET n 
1 2800 THR n 
1 2801 ARG n 
1 2802 TRP n 
1 2803 VAL n 
1 2804 ARG n 
1 2805 GLY n 
1 2806 ILE n 
1 2807 PHE n 
1 2808 GLU n 
1 2809 ALA n 
1 2810 LEU n 
1 2811 ARG n 
1 2812 PRO n 
1 2813 LEU n 
1 2814 GLU n 
1 2815 THR n 
1 2816 LEU n 
1 2817 PRO n 
1 2818 VAL n 
1 2819 GLU n 
1 2820 GLY n 
1 2821 LEU n 
1 2822 ILE n 
1 2823 ARG n 
1 2824 ILE n 
1 2825 TRP n 
1 2826 ALA n 
1 2827 HIS n 
1 2828 GLU n 
1 2829 ALA n 
1 2830 LEU n 
1 2831 ARG n 
1 2832 LEU n 
1 2833 PHE n 
1 2834 GLN n 
1 2835 ASP n 
1 2836 ARG n 
1 2837 LEU n 
1 2838 VAL n 
1 2839 GLU n 
1 2840 ASP n 
1 2841 GLU n 
1 2842 GLU n 
1 2843 ARG n 
1 2844 ARG n 
1 2845 TRP n 
1 2846 THR n 
1 2847 ASP n 
1 2848 GLU n 
1 2849 ASN n 
1 2850 ILE n 
1 2851 ASP n 
1 2852 THR n 
1 2853 VAL n 
1 2854 ALA n 
1 2855 LEU n 
1 2856 LYS n 
1 2857 HIS n 
1 2858 PHE n 
1 2859 PRO n 
1 2860 ASN n 
1 2861 ILE n 
1 2862 ASP n 
1 2863 ARG n 
1 2864 GLU n 
1 2865 LYS n 
1 2866 ALA n 
1 2867 MET n 
1 2868 SER n 
1 2869 ARG n 
1 2870 PRO n 
1 2871 ILE n 
1 2872 LEU n 
1 2873 TYR n 
1 2874 SER n 
1 2875 ASN n 
1 2876 TRP n 
1 2877 LEU n 
1 2878 SER n 
1 2879 LYS n 
1 2880 ASP n 
1 2881 TYR n 
1 2882 ILE n 
1 2883 PRO n 
1 2884 VAL n 
1 2885 ASP n 
1 2886 GLN n 
1 2887 GLU n 
1 2888 GLU n 
1 2889 LEU n 
1 2890 ARG n 
1 2891 ASP n 
1 2892 TYR n 
1 2893 VAL n 
1 2894 LYS n 
1 2895 ALA n 
1 2896 ARG n 
1 2897 LEU n 
1 2898 LYS n 
1 2899 VAL n 
1 2900 PHE n 
1 2901 TYR n 
1 2902 GLU n 
1 2903 GLU n 
1 2904 GLU n 
1 2905 LEU n 
1 2906 ASP n 
1 2907 VAL n 
1 2908 PRO n 
1 2909 LEU n 
1 2910 VAL n 
1 2911 LEU n 
1 2912 PHE n 
1 2913 ASN n 
1 2914 GLU n 
1 2915 VAL n 
1 2916 LEU n 
1 2917 ASP n 
1 2918 HIS n 
1 2919 VAL n 
1 2920 LEU n 
1 2921 ARG n 
1 2922 ILE n 
1 2923 ASP n 
1 2924 ARG n 
1 2925 ILE n 
1 2926 PHE n 
1 2927 ARG n 
1 2928 GLN n 
1 2929 PRO n 
1 2930 GLN n 
1 2931 GLY n 
1 2932 HIS n 
1 2933 LEU n 
1 2934 LEU n 
1 2935 LEU n 
1 2936 ILE n 
1 2937 GLY n 
1 2938 VAL n 
1 2939 SER n 
1 2940 GLY n 
1 2941 ALA n 
1 2942 GLY n 
1 2943 LYS n 
1 2944 THR n 
1 2945 THR n 
1 2946 LEU n 
1 2947 SER n 
1 2948 ARG n 
1 2949 PHE n 
1 2950 VAL n 
1 2951 ALA n 
1 2952 TRP n 
1 2953 MET n 
1 2954 ASN n 
1 2955 GLY n 
1 2956 LEU n 
1 2957 SER n 
1 2958 VAL n 
1 2959 TYR n 
1 2960 GLN n 
1 2961 ILE n 
1 2962 LYS n 
1 2963 VAL n 
1 2964 HIS n 
1 2965 ARG n 
1 2966 LYS n 
1 2967 TYR n 
1 2968 THR n 
1 2969 GLY n 
1 2970 GLU n 
1 2971 ASP n 
1 2972 PHE n 
1 2973 ASP n 
1 2974 GLU n 
1 2975 ASP n 
1 2976 LEU n 
1 2977 ARG n 
1 2978 THR n 
1 2979 VAL n 
1 2980 LEU n 
1 2981 ARG n 
1 2982 ARG n 
1 2983 SER n 
1 2984 GLY n 
1 2985 CYS n 
1 2986 LYS n 
1 2987 ASN n 
1 2988 GLU n 
1 2989 LYS n 
1 2990 ILE n 
1 2991 ALA n 
1 2992 PHE n 
1 2993 ILE n 
1 2994 MET n 
1 2995 ASP n 
1 2996 GLU n 
1 2997 SER n 
1 2998 ASN n 
1 2999 VAL n 
1 3000 LEU n 
1 3001 ASP n 
1 3002 SER n 
1 3003 GLY n 
1 3004 PHE n 
1 3005 LEU n 
1 3006 GLU n 
1 3007 ARG n 
1 3008 MET n 
1 3009 ASN n 
1 3010 THR n 
1 3011 LEU n 
1 3012 LEU n 
1 3013 ALA n 
1 3014 ASN n 
1 3015 GLY n 
1 3016 GLU n 
1 3017 VAL n 
1 3018 PRO n 
1 3019 GLY n 
1 3020 LEU n 
1 3021 PHE n 
1 3022 GLU n 
1 3023 GLY n 
1 3024 ASP n 
1 3025 GLU n 
1 3026 TYR n 
1 3027 ALA n 
1 3028 THR n 
1 3029 LEU n 
1 3030 MET n 
1 3031 THR n 
1 3032 GLN n 
1 3033 CYS n 
1 3034 LYS n 
1 3035 GLU n 
1 3036 GLY n 
1 3037 ALA n 
1 3038 GLN n 
1 3039 LYS n 
1 3040 GLU n 
1 3041 GLY n 
1 3042 LEU n 
1 3043 MET n 
1 3044 LEU n 
1 3045 ASP n 
1 3046 SER n 
1 3047 HIS n 
1 3048 GLU n 
1 3049 GLU n 
1 3050 LEU n 
1 3051 TYR n 
1 3052 LYS n 
1 3053 TRP n 
1 3054 PHE n 
1 3055 THR n 
1 3056 SER n 
1 3057 GLN n 
1 3058 VAL n 
1 3059 ILE n 
1 3060 ARG n 
1 3061 ASN n 
1 3062 LEU n 
1 3063 HIS n 
1 3064 VAL n 
1 3065 VAL n 
1 3066 PHE n 
1 3067 THR n 
1 3068 MET n 
1 3069 ASN n 
1 3070 PRO n 
1 3071 SER n 
1 3072 SER n 
1 3073 GLU n 
1 3074 GLY n 
1 3075 LEU n 
1 3076 LYS n 
1 3077 ASP n 
1 3078 ARG n 
1 3079 ALA n 
1 3080 ALA n 
1 3081 THR n 
1 3082 SER n 
1 3083 PRO n 
1 3084 ALA n 
1 3085 LEU n 
1 3086 PHE n 
1 3087 ASN n 
1 3088 ARG n 
1 3089 CYS n 
1 3090 VAL n 
1 3091 LEU n 
1 3092 ASN n 
1 3093 TRP n 
1 3094 PHE n 
1 3095 GLY n 
1 3096 ASP n 
1 3097 TRP n 
1 3098 SER n 
1 3099 THR n 
1 3100 GLU n 
1 3101 ALA n 
1 3102 LEU n 
1 3103 TYR n 
1 3104 GLN n 
1 3105 VAL n 
1 3106 GLY n 
1 3107 LYS n 
1 3108 GLU n 
1 3109 PHE n 
1 3110 THR n 
1 3111 SER n 
1 3112 LYS n 
1 3113 MET n 
1 3114 ASP n 
1 3115 LEU n 
1 3116 GLU n 
1 3117 LYS n 
1 3118 PRO n 
1 3119 ASN n 
1 3120 TYR n 
1 3121 ILE n 
1 3122 VAL n 
1 3123 PRO n 
1 3124 ASP n 
1 3125 TYR n 
1 3126 MET n 
1 3127 PRO n 
1 3128 VAL n 
1 3129 VAL n 
1 3130 TYR n 
1 3131 ASP n 
1 3132 LYS n 
1 3133 LEU n 
1 3134 PRO n 
1 3135 GLN n 
1 3136 PRO n 
1 3137 PRO n 
1 3138 SER n 
1 3139 HIS n 
1 3140 ARG n 
1 3141 GLU n 
1 3142 ALA n 
1 3143 ILE n 
1 3144 VAL n 
1 3145 ASN n 
1 3146 SER n 
1 3147 CYS n 
1 3148 VAL n 
1 3149 PHE n 
1 3150 VAL n 
1 3151 HIS n 
1 3152 GLN n 
1 3153 THR n 
1 3154 LEU n 
1 3155 HIS n 
1 3156 GLN n 
1 3157 ALA n 
1 3158 ASN n 
1 3159 ALA n 
1 3160 ARG n 
1 3161 LEU n 
1 3162 ALA n 
1 3163 LYS n 
1 3164 ARG n 
1 3165 GLY n 
1 3166 GLY n 
1 3167 ARG n 
1 3168 THR n 
1 3169 MET n 
1 3170 ALA n 
1 3171 ILE n 
1 3172 THR n 
1 3173 PRO n 
1 3174 ARG n 
1 3175 HIS n 
1 3176 TYR n 
1 3177 LEU n 
1 3178 ASP n 
1 3179 PHE n 
1 3180 ILE n 
1 3181 ASN n 
1 3182 HIS n 
1 3183 TYR n 
1 3184 ALA n 
1 3185 ASN n 
1 3186 LEU n 
1 3187 PHE n 
1 3188 HIS n 
1 3189 GLU n 
1 3190 LYS n 
1 3191 ARG n 
1 3192 SER n 
1 3193 GLU n 
1 3194 LEU n 
1 3195 GLU n 
1 3196 GLU n 
1 3197 GLN n 
1 3198 GLN n 
1 3199 MET n 
1 3200 HIS n 
1 3201 LEU n 
1 3202 ASN n 
1 3203 VAL n 
1 3204 GLY n 
1 3205 LEU n 
1 3206 ARG n 
1 3207 LYS n 
1 3208 ILE n 
1 3209 LYS n 
1 3210 GLU n 
1 3211 THR n 
1 3212 VAL n 
1 3213 ASP n 
1 3214 GLN n 
1 3215 VAL n 
1 3216 GLU n 
1 3217 GLU n 
1 3218 LEU n 
1 3219 ARG n 
1 3220 ARG n 
1 3221 ASP n 
1 3222 LEU n 
1 3223 ARG n 
1 3224 ILE n 
1 3225 LYS n 
1 3226 SER n 
1 3227 GLN n 
1 3228 GLU n 
1 3229 LEU n 
1 3230 GLU n 
1 3231 VAL n 
1 3232 LYS n 
1 3233 ASN n 
1 3234 ALA n 
1 3235 ALA n 
1 3236 ALA n 
1 3237 ASN n 
1 3238 ASP n 
1 3239 LYS n 
1 3240 LEU n 
1 3241 LYS n 
1 3242 LYS n 
1 3243 MET n 
1 3244 VAL n 
1 3245 LYS n 
1 3246 ASP n 
1 3247 GLN n 
1 3248 GLN n 
1 3249 GLU n 
1 3250 ALA n 
1 3251 GLU n 
1 3252 LYS n 
1 3253 LYS n 
1 3254 LYS n 
1 3255 VAL n 
1 3256 MET n 
1 3257 SER n 
1 3258 GLN n 
1 3259 GLU n 
1 3260 ILE n 
1 3261 GLN n 
1 3262 GLU n 
1 3263 GLN n 
1 3264 LEU n 
1 3265 HIS n 
1 3266 LYS n 
1 3267 GLN n 
1 3268 GLN n 
1 3269 GLU n 
1 3270 VAL n 
1 3271 ILE n 
1 3272 ALA n 
1 3273 ASP n 
1 3274 LYS n 
1 3275 GLN n 
1 3276 MET n 
1 3277 SER n 
1 3278 VAL n 
1 3279 LYS n 
1 3280 GLU n 
1 3281 ASP n 
1 3282 LEU n 
1 3283 ASP n 
1 3284 LYS n 
1 3285 VAL n 
1 3286 GLU n 
1 3287 PRO n 
1 3288 ALA n 
1 3289 VAL n 
1 3290 ILE n 
1 3291 GLU n 
1 3292 ALA n 
1 3293 GLN n 
1 3294 ASN n 
1 3295 ALA n 
1 3296 VAL n 
1 3297 LYS n 
1 3298 SER n 
1 3299 ILE n 
1 3300 LYS n 
1 3301 LYS n 
1 3302 GLN n 
1 3303 HIS n 
1 3304 LEU n 
1 3305 VAL n 
1 3306 GLU n 
1 3307 VAL n 
1 3308 ARG n 
1 3309 SER n 
1 3310 MET n 
1 3311 ALA n 
1 3312 ASN n 
1 3313 PRO n 
1 3314 PRO n 
1 3315 ALA n 
1 3316 ALA n 
1 3317 VAL n 
1 3318 LYS n 
1 3319 LEU n 
1 3320 ALA n 
1 3321 LEU n 
1 3322 GLU n 
1 3323 SER n 
1 3324 ILE n 
1 3325 CYS n 
1 3326 LEU n 
1 3327 LEU n 
1 3328 LEU n 
1 3329 GLY n 
1 3330 GLU n 
1 3331 SER n 
1 3332 THR n 
1 3333 THR n 
1 3334 ASP n 
1 3335 TRP n 
1 3336 LYS n 
1 3337 GLN n 
1 3338 ILE n 
1 3339 ARG n 
1 3340 SER n 
1 3341 ILE n 
1 3342 ILE n 
1 3343 MET n 
1 3344 ARG n 
1 3345 GLU n 
1 3346 ASN n 
1 3347 PHE n 
1 3348 ILE n 
1 3349 PRO n 
1 3350 THR n 
1 3351 ILE n 
1 3352 VAL n 
1 3353 ASN n 
1 3354 PHE n 
1 3355 SER n 
1 3356 ALA n 
1 3357 GLU n 
1 3358 GLU n 
1 3359 ILE n 
1 3360 SER n 
1 3361 ASP n 
1 3362 ALA n 
1 3363 ILE n 
1 3364 ARG n 
1 3365 GLU n 
1 3366 LYS n 
1 3367 MET n 
1 3368 LYS n 
1 3369 LYS n 
1 3370 ASN n 
1 3371 TYR n 
1 3372 MET n 
1 3373 SER n 
1 3374 ASN n 
1 3375 PRO n 
1 3376 SER n 
1 3377 TYR n 
1 3378 ASN n 
1 3379 TYR n 
1 3380 GLU n 
1 3381 ILE n 
1 3382 VAL n 
1 3383 ASN n 
1 3384 ARG n 
1 3385 ALA n 
1 3386 SER n 
1 3387 LEU n 
1 3388 ALA n 
1 3389 CYS n 
1 3390 GLY n 
1 3391 PRO n 
1 3392 MET n 
1 3393 VAL n 
1 3394 LYS n 
1 3395 TRP n 
1 3396 ALA n 
1 3397 ILE n 
1 3398 ALA n 
1 3399 GLN n 
1 3400 LEU n 
1 3401 ASN n 
1 3402 TYR n 
1 3403 ALA n 
1 3404 ASP n 
1 3405 MET n 
1 3406 LEU n 
1 3407 LYS n 
1 3408 ARG n 
1 3409 VAL n 
1 3410 GLU n 
1 3411 PRO n 
1 3412 LEU n 
1 3413 ARG n 
1 3414 ASN n 
1 3415 GLU n 
1 3416 LEU n 
1 3417 GLN n 
1 3418 LYS n 
1 3419 LEU n 
1 3420 GLU n 
1 3421 ASP n 
1 3422 ASP n 
1 3423 ALA n 
1 3424 LYS n 
1 3425 ASP n 
1 3426 ASN n 
1 3427 GLN n 
1 3428 GLN n 
1 3429 LYS n 
1 3430 ALA n 
1 3431 ASN n 
1 3432 GLU n 
1 3433 VAL n 
1 3434 GLU n 
1 3435 GLN n 
1 3436 MET n 
1 3437 ILE n 
1 3438 ARG n 
1 3439 ASP n 
1 3440 LEU n 
1 3441 GLU n 
1 3442 ALA n 
1 3443 SER n 
1 3444 ILE n 
1 3445 ALA n 
1 3446 ARG n 
1 3447 TYR n 
1 3448 LYS n 
1 3449 GLU n 
1 3450 GLU n 
1 3451 TYR n 
1 3452 ALA n 
1 3453 VAL n 
1 3454 LEU n 
1 3455 ILE n 
1 3456 SER n 
1 3457 GLU n 
1 3458 ALA n 
1 3459 GLN n 
1 3460 ALA n 
1 3461 ILE n 
1 3462 LYS n 
1 3463 ALA n 
1 3464 ASP n 
1 3465 LEU n 
1 3466 ALA n 
1 3467 ALA n 
1 3468 VAL n 
1 3469 GLU n 
1 3470 ALA n 
1 3471 LYS n 
1 3472 VAL n 
1 3473 ASN n 
1 3474 ARG n 
1 3475 SER n 
1 3476 THR n 
1 3477 ALA n 
1 3478 LEU n 
1 3479 LEU n 
1 3480 LYS n 
1 3481 SER n 
1 3482 LEU n 
1 3483 SER n 
1 3484 ALA n 
1 3485 GLU n 
1 3486 ARG n 
1 3487 GLU n 
1 3488 ARG n 
1 3489 TRP n 
1 3490 GLU n 
1 3491 LYS n 
1 3492 THR n 
1 3493 SER n 
1 3494 GLU n 
1 3495 THR n 
1 3496 PHE n 
1 3497 LYS n 
1 3498 ASN n 
1 3499 GLN n 
1 3500 MET n 
1 3501 SER n 
1 3502 THR n 
1 3503 ILE n 
1 3504 ALA n 
1 3505 GLY n 
1 3506 ASP n 
1 3507 CYS n 
1 3508 LEU n 
1 3509 LEU n 
1 3510 SER n 
1 3511 ALA n 
1 3512 ALA n 
1 3513 PHE n 
1 3514 ILE n 
1 3515 ALA n 
1 3516 TYR n 
1 3517 ALA n 
1 3518 GLY n 
1 3519 TYR n 
1 3520 PHE n 
1 3521 ASP n 
1 3522 GLN n 
1 3523 GLN n 
1 3524 MET n 
1 3525 ARG n 
1 3526 GLN n 
1 3527 ASN n 
1 3528 LEU n 
1 3529 PHE n 
1 3530 THR n 
1 3531 THR n 
1 3532 TRP n 
1 3533 SER n 
1 3534 HIS n 
1 3535 HIS n 
1 3536 LEU n 
1 3537 GLN n 
1 3538 GLN n 
1 3539 ALA n 
1 3540 ASN n 
1 3541 ILE n 
1 3542 GLN n 
1 3543 PHE n 
1 3544 ARG n 
1 3545 THR n 
1 3546 ASP n 
1 3547 ILE n 
1 3548 ALA n 
1 3549 ARG n 
1 3550 THR n 
1 3551 GLU n 
1 3552 TYR n 
1 3553 LEU n 
1 3554 SER n 
1 3555 ASN n 
1 3556 ALA n 
1 3557 ASP n 
1 3558 GLU n 
1 3559 ARG n 
1 3560 LEU n 
1 3561 ARG n 
1 3562 TRP n 
1 3563 GLN n 
1 3564 ALA n 
1 3565 SER n 
1 3566 SER n 
1 3567 LEU n 
1 3568 PRO n 
1 3569 ALA n 
1 3570 ASP n 
1 3571 ASP n 
1 3572 LEU n 
1 3573 CYS n 
1 3574 THR n 
1 3575 GLU n 
1 3576 ASN n 
1 3577 ALA n 
1 3578 ILE n 
1 3579 MET n 
1 3580 LEU n 
1 3581 LYS n 
1 3582 ARG n 
1 3583 PHE n 
1 3584 ASN n 
1 3585 ARG n 
1 3586 TYR n 
1 3587 PRO n 
1 3588 LEU n 
1 3589 ILE n 
1 3590 ILE n 
1 3591 ASP n 
1 3592 PRO n 
1 3593 SER n 
1 3594 GLY n 
1 3595 GLN n 
1 3596 ALA n 
1 3597 THR n 
1 3598 GLU n 
1 3599 PHE n 
1 3600 ILE n 
1 3601 MET n 
1 3602 ASN n 
1 3603 GLU n 
1 3604 TYR n 
1 3605 LYS n 
1 3606 ASP n 
1 3607 ARG n 
1 3608 LYS n 
1 3609 ILE n 
1 3610 THR n 
1 3611 ARG n 
1 3612 THR n 
1 3613 SER n 
1 3614 PHE n 
1 3615 LEU n 
1 3616 ASP n 
1 3617 ASP n 
1 3618 ALA n 
1 3619 PHE n 
1 3620 ARG n 
1 3621 LYS n 
1 3622 ASN n 
1 3623 LEU n 
1 3624 GLU n 
1 3625 SER n 
1 3626 ALA n 
1 3627 LEU n 
1 3628 ARG n 
1 3629 PHE n 
1 3630 GLY n 
1 3631 ASN n 
1 3632 PRO n 
1 3633 LEU n 
1 3634 LEU n 
1 3635 VAL n 
1 3636 GLN n 
1 3637 ASP n 
1 3638 VAL n 
1 3639 GLU n 
1 3640 SER n 
1 3641 TYR n 
1 3642 ASP n 
1 3643 PRO n 
1 3644 VAL n 
1 3645 LEU n 
1 3646 ASN n 
1 3647 PRO n 
1 3648 VAL n 
1 3649 LEU n 
1 3650 ASN n 
1 3651 ARG n 
1 3652 GLU n 
1 3653 VAL n 
1 3654 ARG n 
1 3655 ARG n 
1 3656 THR n 
1 3657 GLY n 
1 3658 GLY n 
1 3659 ARG n 
1 3660 VAL n 
1 3661 LEU n 
1 3662 ILE n 
1 3663 THR n 
1 3664 LEU n 
1 3665 GLY n 
1 3666 ASP n 
1 3667 GLN n 
1 3668 ASP n 
1 3669 ILE n 
1 3670 ASP n 
1 3671 LEU n 
1 3672 SER n 
1 3673 PRO n 
1 3674 SER n 
1 3675 PHE n 
1 3676 VAL n 
1 3677 ILE n 
1 3678 PHE n 
1 3679 LEU n 
1 3680 SER n 
1 3681 THR n 
1 3682 ARG n 
1 3683 ASP n 
1 3684 PRO n 
1 3685 THR n 
1 3686 VAL n 
1 3687 GLU n 
1 3688 PHE n 
1 3689 PRO n 
1 3690 PRO n 
1 3691 ASP n 
1 3692 LEU n 
1 3693 CYS n 
1 3694 SER n 
1 3695 ARG n 
1 3696 VAL n 
1 3697 THR n 
1 3698 PHE n 
1 3699 VAL n 
1 3700 ASN n 
1 3701 PHE n 
1 3702 THR n 
1 3703 VAL n 
1 3704 THR n 
1 3705 ARG n 
1 3706 SER n 
1 3707 SER n 
1 3708 LEU n 
1 3709 GLN n 
1 3710 SER n 
1 3711 GLN n 
1 3712 CYS n 
1 3713 LEU n 
1 3714 ASN n 
1 3715 GLU n 
1 3716 VAL n 
1 3717 LEU n 
1 3718 LYS n 
1 3719 ALA n 
1 3720 GLU n 
1 3721 ARG n 
1 3722 PRO n 
1 3723 ASP n 
1 3724 VAL n 
1 3725 ASP n 
1 3726 GLU n 
1 3727 LYS n 
1 3728 ARG n 
1 3729 SER n 
1 3730 ASP n 
1 3731 LEU n 
1 3732 LEU n 
1 3733 LYS n 
1 3734 LEU n 
1 3735 GLN n 
1 3736 GLY n 
1 3737 GLU n 
1 3738 PHE n 
1 3739 GLN n 
1 3740 LEU n 
1 3741 ARG n 
1 3742 LEU n 
1 3743 ARG n 
1 3744 GLN n 
1 3745 LEU n 
1 3746 GLU n 
1 3747 LYS n 
1 3748 SER n 
1 3749 LEU n 
1 3750 LEU n 
1 3751 GLN n 
1 3752 ALA n 
1 3753 LEU n 
1 3754 ASN n 
1 3755 GLU n 
1 3756 VAL n 
1 3757 LYS n 
1 3758 GLY n 
1 3759 ARG n 
1 3760 ILE n 
1 3761 LEU n 
1 3762 ASP n 
1 3763 ASP n 
1 3764 ASP n 
1 3765 THR n 
1 3766 ILE n 
1 3767 ILE n 
1 3768 THR n 
1 3769 THR n 
1 3770 LEU n 
1 3771 GLU n 
1 3772 ASN n 
1 3773 LEU n 
1 3774 LYS n 
1 3775 ARG n 
1 3776 GLU n 
1 3777 ALA n 
1 3778 ALA n 
1 3779 GLU n 
1 3780 VAL n 
1 3781 THR n 
1 3782 ARG n 
1 3783 LYS n 
1 3784 VAL n 
1 3785 GLU n 
1 3786 GLU n 
1 3787 THR n 
1 3788 ASP n 
1 3789 ILE n 
1 3790 VAL n 
1 3791 MET n 
1 3792 GLN n 
1 3793 GLU n 
1 3794 VAL n 
1 3795 GLU n 
1 3796 THR n 
1 3797 VAL n 
1 3798 SER n 
1 3799 GLN n 
1 3800 GLN n 
1 3801 TYR n 
1 3802 LEU n 
1 3803 PRO n 
1 3804 LEU n 
1 3805 SER n 
1 3806 THR n 
1 3807 ALA n 
1 3808 CYS n 
1 3809 SER n 
1 3810 SER n 
1 3811 ILE n 
1 3812 TYR n 
1 3813 PHE n 
1 3814 THR n 
1 3815 MET n 
1 3816 GLU n 
1 3817 SER n 
1 3818 LEU n 
1 3819 LYS n 
1 3820 GLN n 
1 3821 ILE n 
1 3822 HIS n 
1 3823 PHE n 
1 3824 LEU n 
1 3825 TYR n 
1 3826 GLN n 
1 3827 TYR n 
1 3828 SER n 
1 3829 LEU n 
1 3830 GLN n 
1 3831 PHE n 
1 3832 PHE n 
1 3833 LEU n 
1 3834 ASP n 
1 3835 ILE n 
1 3836 TYR n 
1 3837 HIS n 
1 3838 ASN n 
1 3839 VAL n 
1 3840 LEU n 
1 3841 TYR n 
1 3842 GLU n 
1 3843 ASN n 
1 3844 PRO n 
1 3845 ASN n 
1 3846 LEU n 
1 3847 LYS n 
1 3848 GLY n 
1 3849 VAL n 
1 3850 THR n 
1 3851 ASP n 
1 3852 HIS n 
1 3853 THR n 
1 3854 GLN n 
1 3855 ARG n 
1 3856 LEU n 
1 3857 SER n 
1 3858 ILE n 
1 3859 ILE n 
1 3860 THR n 
1 3861 LYS n 
1 3862 ASP n 
1 3863 LEU n 
1 3864 PHE n 
1 3865 GLN n 
1 3866 VAL n 
1 3867 ALA n 
1 3868 PHE n 
1 3869 ASN n 
1 3870 ARG n 
1 3871 VAL n 
1 3872 ALA n 
1 3873 ARG n 
1 3874 GLY n 
1 3875 MET n 
1 3876 LEU n 
1 3877 HIS n 
1 3878 GLN n 
1 3879 ASP n 
1 3880 HIS n 
1 3881 ILE n 
1 3882 THR n 
1 3883 PHE n 
1 3884 ALA n 
1 3885 MET n 
1 3886 LEU n 
1 3887 LEU n 
1 3888 ALA n 
1 3889 ARG n 
1 3890 ILE n 
1 3891 LYS n 
1 3892 LEU n 
1 3893 LYS n 
1 3894 GLY n 
1 3895 THR n 
1 3896 VAL n 
1 3897 GLY n 
1 3898 GLU n 
1 3899 PRO n 
1 3900 THR n 
1 3901 TYR n 
1 3902 ASP n 
1 3903 ALA n 
1 3904 GLU n 
1 3905 PHE n 
1 3906 GLN n 
1 3907 HIS n 
1 3908 PHE n 
1 3909 LEU n 
1 3910 ARG n 
1 3911 GLY n 
1 3912 ASN n 
1 3913 GLU n 
1 3914 ILE n 
1 3915 VAL n 
1 3916 LEU n 
1 3917 SER n 
1 3918 ALA n 
1 3919 GLY n 
1 3920 SER n 
1 3921 THR n 
1 3922 PRO n 
1 3923 ARG n 
1 3924 ILE n 
1 3925 GLN n 
1 3926 GLY n 
1 3927 LEU n 
1 3928 THR n 
1 3929 VAL n 
1 3930 GLU n 
1 3931 GLN n 
1 3932 ALA n 
1 3933 GLU n 
1 3934 ALA n 
1 3935 VAL n 
1 3936 VAL n 
1 3937 ARG n 
1 3938 LEU n 
1 3939 SER n 
1 3940 CYS n 
1 3941 LEU n 
1 3942 PRO n 
1 3943 ALA n 
1 3944 PHE n 
1 3945 LYS n 
1 3946 ASP n 
1 3947 LEU n 
1 3948 ILE n 
1 3949 ALA n 
1 3950 LYS n 
1 3951 VAL n 
1 3952 GLN n 
1 3953 ALA n 
1 3954 ASP n 
1 3955 GLU n 
1 3956 GLN n 
1 3957 PHE n 
1 3958 GLY n 
1 3959 ILE n 
1 3960 TRP n 
1 3961 LEU n 
1 3962 ASP n 
1 3963 SER n 
1 3964 SER n 
1 3965 SER n 
1 3966 PRO n 
1 3967 GLU n 
1 3968 GLN n 
1 3969 THR n 
1 3970 VAL n 
1 3971 PRO n 
1 3972 TYR n 
1 3973 LEU n 
1 3974 TRP n 
1 3975 SER n 
1 3976 GLU n 
1 3977 GLU n 
1 3978 THR n 
1 3979 PRO n 
1 3980 ALA n 
1 3981 THR n 
1 3982 PRO n 
1 3983 ILE n 
1 3984 GLY n 
1 3985 GLN n 
1 3986 ALA n 
1 3987 ILE n 
1 3988 HIS n 
1 3989 ARG n 
1 3990 LEU n 
1 3991 LEU n 
1 3992 LEU n 
1 3993 ILE n 
1 3994 GLN n 
1 3995 ALA n 
1 3996 PHE n 
1 3997 ARG n 
1 3998 PRO n 
1 3999 ASP n 
1 4000 ARG n 
1 4001 LEU n 
1 4002 LEU n 
1 4003 ALA n 
1 4004 MET n 
1 4005 ALA n 
1 4006 HIS n 
1 4007 MET n 
1 4008 PHE n 
1 4009 VAL n 
1 4010 SER n 
1 4011 THR n 
1 4012 ASN n 
1 4013 LEU n 
1 4014 GLY n 
1 4015 GLU n 
1 4016 SER n 
1 4017 PHE n 
1 4018 MET n 
1 4019 SER n 
1 4020 ILE n 
1 4021 MET n 
1 4022 GLU n 
1 4023 GLN n 
1 4024 PRO n 
1 4025 LEU n 
1 4026 ASP n 
1 4027 LEU n 
1 4028 THR n 
1 4029 HIS n 
1 4030 ILE n 
1 4031 VAL n 
1 4032 GLY n 
1 4033 THR n 
1 4034 GLU n 
1 4035 VAL n 
1 4036 LYS n 
1 4037 PRO n 
1 4038 ASN n 
1 4039 THR n 
1 4040 PRO n 
1 4041 VAL n 
1 4042 LEU n 
1 4043 MET n 
1 4044 CYS n 
1 4045 SER n 
1 4046 VAL n 
1 4047 PRO n 
1 4048 GLY n 
1 4049 TYR n 
1 4050 ASP n 
1 4051 ALA n 
1 4052 SER n 
1 4053 GLY n 
1 4054 HIS n 
1 4055 VAL n 
1 4056 GLU n 
1 4057 ASP n 
1 4058 LEU n 
1 4059 ALA n 
1 4060 ALA n 
1 4061 GLU n 
1 4062 GLN n 
1 4063 ASN n 
1 4064 THR n 
1 4065 GLN n 
1 4066 ILE n 
1 4067 THR n 
1 4068 SER n 
1 4069 ILE n 
1 4070 ALA n 
1 4071 ILE n 
1 4072 GLY n 
1 4073 SER n 
1 4074 ALA n 
1 4075 GLU n 
1 4076 GLY n 
1 4077 PHE n 
1 4078 ASN n 
1 4079 GLN n 
1 4080 ALA n 
1 4081 ASP n 
1 4082 LYS n 
1 4083 ALA n 
1 4084 ILE n 
1 4085 ASN n 
1 4086 THR n 
1 4087 ALA n 
1 4088 VAL n 
1 4089 LYS n 
1 4090 SER n 
1 4091 GLY n 
1 4092 ARG n 
1 4093 TRP n 
1 4094 VAL n 
1 4095 MET n 
1 4096 LEU n 
1 4097 LYS n 
1 4098 ASN n 
1 4099 VAL n 
1 4100 HIS n 
1 4101 LEU n 
1 4102 ALA n 
1 4103 PRO n 
1 4104 GLY n 
1 4105 TRP n 
1 4106 LEU n 
1 4107 MET n 
1 4108 GLN n 
1 4109 LEU n 
1 4110 GLU n 
1 4111 LYS n 
1 4112 LYS n 
1 4113 LEU n 
1 4114 HIS n 
1 4115 SER n 
1 4116 LEU n 
1 4117 GLN n 
1 4118 PRO n 
1 4119 HIS n 
1 4120 ALA n 
1 4121 CYS n 
1 4122 PHE n 
1 4123 ARG n 
1 4124 LEU n 
1 4125 PHE n 
1 4126 LEU n 
1 4127 THR n 
1 4128 MET n 
1 4129 GLU n 
1 4130 ILE n 
1 4131 ASN n 
1 4132 PRO n 
1 4133 LYS n 
1 4134 VAL n 
1 4135 PRO n 
1 4136 VAL n 
1 4137 ASN n 
1 4138 LEU n 
1 4139 LEU n 
1 4140 ARG n 
1 4141 ALA n 
1 4142 GLY n 
1 4143 ARG n 
1 4144 ILE n 
1 4145 PHE n 
1 4146 VAL n 
1 4147 PHE n 
1 4148 GLU n 
1 4149 PRO n 
1 4150 PRO n 
1 4151 PRO n 
1 4152 GLY n 
1 4153 VAL n 
1 4154 LYS n 
1 4155 ALA n 
1 4156 ASN n 
1 4157 MET n 
1 4158 LEU n 
1 4159 ARG n 
1 4160 THR n 
1 4161 PHE n 
1 4162 SER n 
1 4163 SER n 
1 4164 ILE n 
1 4165 PRO n 
1 4166 VAL n 
1 4167 SER n 
1 4168 ARG n 
1 4169 ILE n 
1 4170 CYS n 
1 4171 LYS n 
1 4172 SER n 
1 4173 PRO n 
1 4174 ASN n 
1 4175 GLU n 
1 4176 ARG n 
1 4177 ALA n 
1 4178 ARG n 
1 4179 LEU n 
1 4180 TYR n 
1 4181 PHE n 
1 4182 LEU n 
1 4183 LEU n 
1 4184 ALA n 
1 4185 TRP n 
1 4186 PHE n 
1 4187 HIS n 
1 4188 ALA n 
1 4189 ILE n 
1 4190 ILE n 
1 4191 GLN n 
1 4192 GLU n 
1 4193 ARG n 
1 4194 LEU n 
1 4195 ARG n 
1 4196 TYR n 
1 4197 ALA n 
1 4198 PRO n 
1 4199 LEU n 
1 4200 GLY n 
1 4201 TRP n 
1 4202 SER n 
1 4203 LYS n 
1 4204 LYS n 
1 4205 TYR n 
1 4206 GLU n 
1 4207 PHE n 
1 4208 GLY n 
1 4209 GLU n 
1 4210 SER n 
1 4211 ASP n 
1 4212 LEU n 
1 4213 ARG n 
1 4214 SER n 
1 4215 ALA n 
1 4216 CYS n 
1 4217 ASP n 
1 4218 THR n 
1 4219 VAL n 
1 4220 ASP n 
1 4221 THR n 
1 4222 TRP n 
1 4223 LEU n 
1 4224 ASP n 
1 4225 ASP n 
1 4226 THR n 
1 4227 ALA n 
1 4228 LYS n 
1 4229 GLY n 
1 4230 ARG n 
1 4231 GLN n 
1 4232 ASN n 
1 4233 ILE n 
1 4234 SER n 
1 4235 PRO n 
1 4236 ASP n 
1 4237 LYS n 
1 4238 ILE n 
1 4239 PRO n 
1 4240 TRP n 
1 4241 SER n 
1 4242 ALA n 
1 4243 LEU n 
1 4244 LYS n 
1 4245 THR n 
1 4246 LEU n 
1 4247 MET n 
1 4248 ALA n 
1 4249 GLN n 
1 4250 SER n 
1 4251 ILE n 
1 4252 TYR n 
1 4253 GLY n 
1 4254 GLY n 
1 4255 ARG n 
1 4256 VAL n 
1 4257 ASP n 
1 4258 ASN n 
1 4259 GLU n 
1 4260 PHE n 
1 4261 ASP n 
1 4262 GLN n 
1 4263 ARG n 
1 4264 LEU n 
1 4265 LEU n 
1 4266 ASN n 
1 4267 THR n 
1 4268 PHE n 
1 4269 LEU n 
1 4270 GLU n 
1 4271 ARG n 
1 4272 LEU n 
1 4273 PHE n 
1 4274 THR n 
1 4275 THR n 
1 4276 ARG n 
1 4277 SER n 
1 4278 PHE n 
1 4279 ASP n 
1 4280 SER n 
1 4281 GLU n 
1 4282 PHE n 
1 4283 LYS n 
1 4284 LEU n 
1 4285 ALA n 
1 4286 CYS n 
1 4287 LYS n 
1 4288 VAL n 
1 4289 ASP n 
1 4290 GLY n 
1 4291 HIS n 
1 4292 LYS n 
1 4293 ASP n 
1 4294 ILE n 
1 4295 GLN n 
1 4296 MET n 
1 4297 PRO n 
1 4298 ASP n 
1 4299 GLY n 
1 4300 ILE n 
1 4301 ARG n 
1 4302 ARG n 
1 4303 GLU n 
1 4304 GLU n 
1 4305 PHE n 
1 4306 VAL n 
1 4307 GLN n 
1 4308 TRP n 
1 4309 VAL n 
1 4310 GLU n 
1 4311 LEU n 
1 4312 LEU n 
1 4313 PRO n 
1 4314 ASP n 
1 4315 THR n 
1 4316 GLN n 
1 4317 THR n 
1 4318 PRO n 
1 4319 SER n 
1 4320 TRP n 
1 4321 LEU n 
1 4322 GLY n 
1 4323 LEU n 
1 4324 PRO n 
1 4325 ASN n 
1 4326 ASN n 
1 4327 ALA n 
1 4328 GLU n 
1 4329 ARG n 
1 4330 VAL n 
1 4331 LEU n 
1 4332 LEU n 
1 4333 THR n 
1 4334 THR n 
1 4335 GLN n 
1 4336 GLY n 
1 4337 VAL n 
1 4338 ASP n 
1 4339 MET n 
1 4340 ILE n 
1 4341 SER n 
1 4342 LYS n 
1 4343 MET n 
1 4344 LEU n 
1 4345 LYS n 
1 4346 MET n 
1 4347 GLN n 
1 4348 MET n 
1 4349 LEU n 
1 4350 GLU n 
1 4351 ASP n 
1 4352 GLU n 
1 4353 ASP n 
1 4354 ASP n 
1 4355 LEU n 
1 4356 ALA n 
1 4357 TYR n 
1 4358 ALA n 
1 4359 GLU n 
1 4360 THR n 
1 4361 GLU n 
1 4362 LYS n 
1 4363 LYS n 
1 4364 THR n 
1 4365 ARG n 
1 4366 THR n 
1 4367 ASP n 
1 4368 SER n 
1 4369 THR n 
1 4370 SER n 
1 4371 ASP n 
1 4372 GLY n 
1 4373 ARG n 
1 4374 PRO n 
1 4375 ALA n 
1 4376 TRP n 
1 4377 MET n 
1 4378 ARG n 
1 4379 THR n 
1 4380 LEU n 
1 4381 HIS n 
1 4382 THR n 
1 4383 THR n 
1 4384 ALA n 
1 4385 SER n 
1 4386 ASN n 
1 4387 TRP n 
1 4388 LEU n 
1 4389 HIS n 
1 4390 LEU n 
1 4391 ILE n 
1 4392 PRO n 
1 4393 GLN n 
1 4394 THR n 
1 4395 LEU n 
1 4396 SER n 
1 4397 HIS n 
1 4398 LEU n 
1 4399 LYS n 
1 4400 ARG n 
1 4401 THR n 
1 4402 VAL n 
1 4403 GLU n 
1 4404 ASN n 
1 4405 ILE n 
1 4406 LYS n 
1 4407 ASP n 
1 4408 PRO n 
1 4409 LEU n 
1 4410 PHE n 
1 4411 ARG n 
1 4412 PHE n 
1 4413 PHE n 
1 4414 GLU n 
1 4415 ARG n 
1 4416 GLU n 
1 4417 VAL n 
1 4418 LYS n 
1 4419 MET n 
1 4420 GLY n 
1 4421 ALA n 
1 4422 LYS n 
1 4423 LEU n 
1 4424 LEU n 
1 4425 GLN n 
1 4426 ASP n 
1 4427 VAL n 
1 4428 ARG n 
1 4429 GLN n 
1 4430 ASP n 
1 4431 LEU n 
1 4432 ALA n 
1 4433 ASP n 
1 4434 VAL n 
1 4435 VAL n 
1 4436 GLN n 
1 4437 VAL n 
1 4438 CYS n 
1 4439 GLU n 
1 4440 GLY n 
1 4441 LYS n 
1 4442 LYS n 
1 4443 LYS n 
1 4444 GLN n 
1 4445 THR n 
1 4446 ASN n 
1 4447 TYR n 
1 4448 LEU n 
1 4449 ARG n 
1 4450 THR n 
1 4451 LEU n 
1 4452 ILE n 
1 4453 ASN n 
1 4454 GLU n 
1 4455 LEU n 
1 4456 VAL n 
1 4457 LYS n 
1 4458 GLY n 
1 4459 ILE n 
1 4460 LEU n 
1 4461 PRO n 
1 4462 ARG n 
1 4463 SER n 
1 4464 TRP n 
1 4465 SER n 
1 4466 HIS n 
1 4467 TYR n 
1 4468 THR n 
1 4469 VAL n 
1 4470 PRO n 
1 4471 ALA n 
1 4472 GLY n 
1 4473 MET n 
1 4474 THR n 
1 4475 VAL n 
1 4476 ILE n 
1 4477 GLN n 
1 4478 TRP n 
1 4479 VAL n 
1 4480 SER n 
1 4481 ASP n 
1 4482 PHE n 
1 4483 SER n 
1 4484 GLU n 
1 4485 ARG n 
1 4486 ILE n 
1 4487 LYS n 
1 4488 GLN n 
1 4489 LEU n 
1 4490 GLN n 
1 4491 ASN n 
1 4492 ILE n 
1 4493 SER n 
1 4494 LEU n 
1 4495 ALA n 
1 4496 ALA n 
1 4497 ALA n 
1 4498 SER n 
1 4499 GLY n 
1 4500 GLY n 
1 4501 ALA n 
1 4502 LYS n 
1 4503 GLU n 
1 4504 LEU n 
1 4505 LYS n 
1 4506 ASN n 
1 4507 ILE n 
1 4508 HIS n 
1 4509 VAL n 
1 4510 CYS n 
1 4511 LEU n 
1 4512 GLY n 
1 4513 GLY n 
1 4514 LEU n 
1 4515 PHE n 
1 4516 VAL n 
1 4517 PRO n 
1 4518 GLU n 
1 4519 ALA n 
1 4520 TYR n 
1 4521 ILE n 
1 4522 THR n 
1 4523 ALA n 
1 4524 THR n 
1 4525 ARG n 
1 4526 GLN n 
1 4527 TYR n 
1 4528 VAL n 
1 4529 ALA n 
1 4530 GLN n 
1 4531 ALA n 
1 4532 ASN n 
1 4533 SER n 
1 4534 TRP n 
1 4535 SER n 
1 4536 LEU n 
1 4537 GLU n 
1 4538 GLU n 
1 4539 LEU n 
1 4540 CYS n 
1 4541 LEU n 
1 4542 GLU n 
1 4543 VAL n 
1 4544 ASN n 
1 4545 VAL n 
1 4546 THR n 
1 4547 THR n 
1 4548 SER n 
1 4549 GLN n 
1 4550 GLY n 
1 4551 ALA n 
1 4552 THR n 
1 4553 LEU n 
1 4554 ASP n 
1 4555 ALA n 
1 4556 CYS n 
1 4557 SER n 
1 4558 PHE n 
1 4559 GLY n 
1 4560 VAL n 
1 4561 THR n 
1 4562 GLY n 
1 4563 LEU n 
1 4564 LYS n 
1 4565 LEU n 
1 4566 GLN n 
1 4567 GLY n 
1 4568 ALA n 
1 4569 THR n 
1 4570 CYS n 
1 4571 ASN n 
1 4572 ASN n 
1 4573 ASN n 
1 4574 LYS n 
1 4575 LEU n 
1 4576 SER n 
1 4577 LEU n 
1 4578 SER n 
1 4579 ASN n 
1 4580 ALA n 
1 4581 ILE n 
1 4582 SER n 
1 4583 THR n 
1 4584 ALA n 
1 4585 LEU n 
1 4586 PRO n 
1 4587 LEU n 
1 4588 THR n 
1 4589 GLN n 
1 4590 LEU n 
1 4591 ARG n 
1 4592 TRP n 
1 4593 VAL n 
1 4594 LYS n 
1 4595 GLN n 
1 4596 THR n 
1 4597 ASN n 
1 4598 THR n 
1 4599 GLU n 
1 4600 LYS n 
1 4601 LYS n 
1 4602 ALA n 
1 4603 SER n 
1 4604 VAL n 
1 4605 VAL n 
1 4606 THR n 
1 4607 LEU n 
1 4608 PRO n 
1 4609 VAL n 
1 4610 TYR n 
1 4611 LEU n 
1 4612 ASN n 
1 4613 PHE n 
1 4614 THR n 
1 4615 ARG n 
1 4616 ALA n 
1 4617 ASP n 
1 4618 LEU n 
1 4619 ILE n 
1 4620 PHE n 
1 4621 THR n 
1 4622 VAL n 
1 4623 ASP n 
1 4624 PHE n 
1 4625 GLU n 
1 4626 ILE n 
1 4627 ALA n 
1 4628 THR n 
1 4629 LYS n 
1 4630 GLU n 
1 4631 ASP n 
1 4632 PRO n 
1 4633 ARG n 
1 4634 SER n 
1 4635 PHE n 
1 4636 TYR n 
1 4637 GLU n 
1 4638 ARG n 
1 4639 GLY n 
1 4640 VAL n 
1 4641 ALA n 
1 4642 VAL n 
1 4643 LEU n 
1 4644 CYS n 
1 4645 THR n 
1 4646 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   4646 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'DYNC1H1, DHC1, DNCH1, DNCL, DNECL, DYHC, KIAA0325' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               '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  
ANP non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ? 'C10 H17 N6 O12 P3' 506.196 
ARG 'L-peptide linking' y ARGININE                                      ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                                    ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                               ? 'C4 H7 N O4'        133.103 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE"                   ? 'C10 H16 N5 O13 P3' 507.181 
CYS 'L-peptide linking' y CYSTEINE                                      ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                                     ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                               ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                       ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                                     ? 'C6 H10 N3 O2 1'    156.162 
ILE 'L-peptide linking' y ISOLEUCINE                                    ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                                       ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                                        ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                                    ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'                               ? 'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE                                 ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                                       ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                                        ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                                     ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                    ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                                      ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                                        ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    MET 1    1    ?    ?   ?   A . n 
A 1 2    SER 2    2    ?    ?   ?   A . n 
A 1 3    GLU 3    3    ?    ?   ?   A . n 
A 1 4    PRO 4    4    ?    ?   ?   A . n 
A 1 5    GLY 5    5    ?    ?   ?   A . n 
A 1 6    GLY 6    6    ?    ?   ?   A . n 
A 1 7    GLY 7    7    ?    ?   ?   A . n 
A 1 8    GLY 8    8    ?    ?   ?   A . n 
A 1 9    GLY 9    9    ?    ?   ?   A . n 
A 1 10   GLU 10   10   ?    ?   ?   A . n 
A 1 11   ASP 11   11   ?    ?   ?   A . n 
A 1 12   GLY 12   12   ?    ?   ?   A . n 
A 1 13   SER 13   13   ?    ?   ?   A . n 
A 1 14   ALA 14   14   ?    ?   ?   A . n 
A 1 15   GLY 15   15   ?    ?   ?   A . n 
A 1 16   LEU 16   16   ?    ?   ?   A . n 
A 1 17   GLU 17   17   ?    ?   ?   A . n 
A 1 18   VAL 18   18   ?    ?   ?   A . n 
A 1 19   SER 19   19   ?    ?   ?   A . n 
A 1 20   ALA 20   20   ?    ?   ?   A . n 
A 1 21   VAL 21   21   ?    ?   ?   A . n 
A 1 22   GLN 22   22   ?    ?   ?   A . n 
A 1 23   ASN 23   23   ?    ?   ?   A . n 
A 1 24   VAL 24   24   ?    ?   ?   A . n 
A 1 25   ALA 25   25   ?    ?   ?   A . n 
A 1 26   ASP 26   26   ?    ?   ?   A . n 
A 1 27   VAL 27   27   ?    ?   ?   A . n 
A 1 28   SER 28   28   ?    ?   ?   A . n 
A 1 29   VAL 29   29   ?    ?   ?   A . n 
A 1 30   LEU 30   30   ?    ?   ?   A . n 
A 1 31   GLN 31   31   ?    ?   ?   A . n 
A 1 32   LYS 32   32   ?    ?   ?   A . n 
A 1 33   HIS 33   33   ?    ?   ?   A . n 
A 1 34   LEU 34   34   ?    ?   ?   A . n 
A 1 35   ARG 35   35   ?    ?   ?   A . n 
A 1 36   LYS 36   36   ?    ?   ?   A . n 
A 1 37   LEU 37   37   ?    ?   ?   A . n 
A 1 38   VAL 38   38   ?    ?   ?   A . n 
A 1 39   PRO 39   39   ?    ?   ?   A . n 
A 1 40   LEU 40   40   ?    ?   ?   A . n 
A 1 41   LEU 41   41   ?    ?   ?   A . n 
A 1 42   LEU 42   42   ?    ?   ?   A . n 
A 1 43   GLU 43   43   ?    ?   ?   A . n 
A 1 44   ASP 44   44   ?    ?   ?   A . n 
A 1 45   GLY 45   45   ?    ?   ?   A . n 
A 1 46   GLY 46   46   ?    ?   ?   A . n 
A 1 47   GLU 47   47   ?    ?   ?   A . n 
A 1 48   ALA 48   48   ?    ?   ?   A . n 
A 1 49   PRO 49   49   ?    ?   ?   A . n 
A 1 50   ALA 50   50   ?    ?   ?   A . n 
A 1 51   ALA 51   51   ?    ?   ?   A . n 
A 1 52   LEU 52   52   ?    ?   ?   A . n 
A 1 53   GLU 53   53   ?    ?   ?   A . n 
A 1 54   ALA 54   54   ?    ?   ?   A . n 
A 1 55   ALA 55   55   ?    ?   ?   A . n 
A 1 56   LEU 56   56   ?    ?   ?   A . n 
A 1 57   GLU 57   57   ?    ?   ?   A . n 
A 1 58   GLU 58   58   ?    ?   ?   A . n 
A 1 59   LYS 59   59   ?    ?   ?   A . n 
A 1 60   SER 60   60   ?    ?   ?   A . n 
A 1 61   ALA 61   61   ?    ?   ?   A . n 
A 1 62   LEU 62   62   ?    ?   ?   A . n 
A 1 63   GLU 63   63   ?    ?   ?   A . n 
A 1 64   GLN 64   64   ?    ?   ?   A . n 
A 1 65   MET 65   65   ?    ?   ?   A . n 
A 1 66   ARG 66   66   ?    ?   ?   A . n 
A 1 67   LYS 67   67   ?    ?   ?   A . n 
A 1 68   PHE 68   68   ?    ?   ?   A . n 
A 1 69   LEU 69   69   ?    ?   ?   A . n 
A 1 70   SER 70   70   ?    ?   ?   A . n 
A 1 71   ASP 71   71   ?    ?   ?   A . n 
A 1 72   PRO 72   72   ?    ?   ?   A . n 
A 1 73   GLN 73   73   ?    ?   ?   A . n 
A 1 74   VAL 74   74   ?    ?   ?   A . n 
A 1 75   HIS 75   75   ?    ?   ?   A . n 
A 1 76   THR 76   76   ?    ?   ?   A . n 
A 1 77   VAL 77   77   ?    ?   ?   A . n 
A 1 78   LEU 78   78   ?    ?   ?   A . n 
A 1 79   VAL 79   79   ?    ?   ?   A . n 
A 1 80   GLU 80   80   ?    ?   ?   A . n 
A 1 81   ARG 81   81   ?    ?   ?   A . n 
A 1 82   SER 82   82   ?    ?   ?   A . n 
A 1 83   THR 83   83   ?    ?   ?   A . n 
A 1 84   LEU 84   84   ?    ?   ?   A . n 
A 1 85   LYS 85   85   ?    ?   ?   A . n 
A 1 86   GLU 86   86   ?    ?   ?   A . n 
A 1 87   ASP 87   87   ?    ?   ?   A . n 
A 1 88   VAL 88   88   ?    ?   ?   A . n 
A 1 89   GLY 89   89   ?    ?   ?   A . n 
A 1 90   ASP 90   90   ?    ?   ?   A . n 
A 1 91   GLU 91   91   ?    ?   ?   A . n 
A 1 92   GLY 92   92   ?    ?   ?   A . n 
A 1 93   GLU 93   93   ?    ?   ?   A . n 
A 1 94   GLU 94   94   ?    ?   ?   A . n 
A 1 95   GLU 95   95   ?    ?   ?   A . n 
A 1 96   LYS 96   96   ?    ?   ?   A . n 
A 1 97   GLU 97   97   ?    ?   ?   A . n 
A 1 98   PHE 98   98   ?    ?   ?   A . n 
A 1 99   ILE 99   99   ?    ?   ?   A . n 
A 1 100  SER 100  100  ?    ?   ?   A . n 
A 1 101  TYR 101  101  ?    ?   ?   A . n 
A 1 102  ASN 102  102  ?    ?   ?   A . n 
A 1 103  ILE 103  103  ?    ?   ?   A . n 
A 1 104  ASN 104  104  ?    ?   ?   A . n 
A 1 105  ILE 105  105  ?    ?   ?   A . n 
A 1 106  ASP 106  106  ?    ?   ?   A . n 
A 1 107  ILE 107  107  ?    ?   ?   A . n 
A 1 108  HIS 108  108  ?    ?   ?   A . n 
A 1 109  TYR 109  109  ?    ?   ?   A . n 
A 1 110  GLY 110  110  ?    ?   ?   A . n 
A 1 111  VAL 111  111  ?    ?   ?   A . n 
A 1 112  LYS 112  112  ?    ?   ?   A . n 
A 1 113  SER 113  113  ?    ?   ?   A . n 
A 1 114  ASN 114  114  ?    ?   ?   A . n 
A 1 115  SER 115  115  ?    ?   ?   A . n 
A 1 116  LEU 116  116  ?    ?   ?   A . n 
A 1 117  ALA 117  117  ?    ?   ?   A . n 
A 1 118  PHE 118  118  ?    ?   ?   A . n 
A 1 119  ILE 119  119  ?    ?   ?   A . n 
A 1 120  LYS 120  120  ?    ?   ?   A . n 
A 1 121  ARG 121  121  ?    ?   ?   A . n 
A 1 122  THR 122  122  ?    ?   ?   A . n 
A 1 123  PRO 123  123  ?    ?   ?   A . n 
A 1 124  VAL 124  124  ?    ?   ?   A . n 
A 1 125  ILE 125  125  ?    ?   ?   A . n 
A 1 126  ASP 126  126  ?    ?   ?   A . n 
A 1 127  ALA 127  127  ?    ?   ?   A . n 
A 1 128  ASP 128  128  ?    ?   ?   A . n 
A 1 129  LYS 129  129  ?    ?   ?   A . n 
A 1 130  PRO 130  130  ?    ?   ?   A . n 
A 1 131  VAL 131  131  ?    ?   ?   A . n 
A 1 132  SER 132  132  ?    ?   ?   A . n 
A 1 133  SER 133  133  ?    ?   ?   A . n 
A 1 134  GLN 134  134  ?    ?   ?   A . n 
A 1 135  LEU 135  135  ?    ?   ?   A . n 
A 1 136  ARG 136  136  ?    ?   ?   A . n 
A 1 137  VAL 137  137  ?    ?   ?   A . n 
A 1 138  LEU 138  138  ?    ?   ?   A . n 
A 1 139  THR 139  139  ?    ?   ?   A . n 
A 1 140  LEU 140  140  ?    ?   ?   A . n 
A 1 141  SER 141  141  ?    ?   ?   A . n 
A 1 142  GLU 142  142  ?    ?   ?   A . n 
A 1 143  ASP 143  143  ?    ?   ?   A . n 
A 1 144  SER 144  144  ?    ?   ?   A . n 
A 1 145  PRO 145  145  ?    ?   ?   A . n 
A 1 146  TYR 146  146  ?    ?   ?   A . n 
A 1 147  GLU 147  147  ?    ?   ?   A . n 
A 1 148  THR 148  148  ?    ?   ?   A . n 
A 1 149  LEU 149  149  ?    ?   ?   A . n 
A 1 150  HIS 150  150  ?    ?   ?   A . n 
A 1 151  SER 151  151  ?    ?   ?   A . n 
A 1 152  PHE 152  152  ?    ?   ?   A . n 
A 1 153  ILE 153  153  ?    ?   ?   A . n 
A 1 154  SER 154  154  ?    ?   ?   A . n 
A 1 155  ASN 155  155  ?    ?   ?   A . n 
A 1 156  ALA 156  156  ?    ?   ?   A . n 
A 1 157  VAL 157  157  ?    ?   ?   A . n 
A 1 158  ALA 158  158  ?    ?   ?   A . n 
A 1 159  PRO 159  159  ?    ?   ?   A . n 
A 1 160  PHE 160  160  ?    ?   ?   A . n 
A 1 161  PHE 161  161  ?    ?   ?   A . n 
A 1 162  LYS 162  162  ?    ?   ?   A . n 
A 1 163  SER 163  163  ?    ?   ?   A . n 
A 1 164  TYR 164  164  ?    ?   ?   A . n 
A 1 165  ILE 165  165  ?    ?   ?   A . n 
A 1 166  ARG 166  166  ?    ?   ?   A . n 
A 1 167  GLU 167  167  ?    ?   ?   A . n 
A 1 168  SER 168  168  ?    ?   ?   A . n 
A 1 169  GLY 169  169  ?    ?   ?   A . n 
A 1 170  LYS 170  170  ?    ?   ?   A . n 
A 1 171  ALA 171  171  ?    ?   ?   A . n 
A 1 172  ASP 172  172  ?    ?   ?   A . n 
A 1 173  ARG 173  173  ?    ?   ?   A . n 
A 1 174  ASP 174  174  ?    ?   ?   A . n 
A 1 175  GLY 175  175  ?    ?   ?   A . n 
A 1 176  ASP 176  176  ?    ?   ?   A . n 
A 1 177  LYS 177  177  ?    ?   ?   A . n 
A 1 178  MET 178  178  ?    ?   ?   A . n 
A 1 179  ALA 179  179  ?    ?   ?   A . n 
A 1 180  PRO 180  180  ?    ?   ?   A . n 
A 1 181  SER 181  181  ?    ?   ?   A . n 
A 1 182  VAL 182  182  ?    ?   ?   A . n 
A 1 183  GLU 183  183  ?    ?   ?   A . n 
A 1 184  LYS 184  184  ?    ?   ?   A . n 
A 1 185  LYS 185  185  ?    ?   ?   A . n 
A 1 186  ILE 186  186  ?    ?   ?   A . n 
A 1 187  ALA 187  187  ?    ?   ?   A . n 
A 1 188  GLU 188  188  ?    ?   ?   A . n 
A 1 189  LEU 189  189  ?    ?   ?   A . n 
A 1 190  GLU 190  190  ?    ?   ?   A . n 
A 1 191  MET 191  191  ?    ?   ?   A . n 
A 1 192  GLY 192  192  ?    ?   ?   A . n 
A 1 193  LEU 193  193  ?    ?   ?   A . n 
A 1 194  LEU 194  194  ?    ?   ?   A . n 
A 1 195  HIS 195  195  ?    ?   ?   A . n 
A 1 196  LEU 196  196  ?    ?   ?   A . n 
A 1 197  GLN 197  197  ?    ?   ?   A . n 
A 1 198  GLN 198  198  ?    ?   ?   A . n 
A 1 199  ASN 199  199  ?    ?   ?   A . n 
A 1 200  ILE 200  200  ?    ?   ?   A . n 
A 1 201  GLU 201  201  ?    ?   ?   A . n 
A 1 202  ILE 202  202  ?    ?   ?   A . n 
A 1 203  PRO 203  203  ?    ?   ?   A . n 
A 1 204  GLU 204  204  ?    ?   ?   A . n 
A 1 205  ILE 205  205  ?    ?   ?   A . n 
A 1 206  SER 206  206  ?    ?   ?   A . n 
A 1 207  LEU 207  207  ?    ?   ?   A . n 
A 1 208  PRO 208  208  ?    ?   ?   A . n 
A 1 209  ILE 209  209  ?    ?   ?   A . n 
A 1 210  HIS 210  210  ?    ?   ?   A . n 
A 1 211  PRO 211  211  ?    ?   ?   A . n 
A 1 212  MET 212  212  ?    ?   ?   A . n 
A 1 213  ILE 213  213  ?    ?   ?   A . n 
A 1 214  THR 214  214  ?    ?   ?   A . n 
A 1 215  ASN 215  215  ?    ?   ?   A . n 
A 1 216  VAL 216  216  ?    ?   ?   A . n 
A 1 217  ALA 217  217  ?    ?   ?   A . n 
A 1 218  LYS 218  218  ?    ?   ?   A . n 
A 1 219  GLN 219  219  ?    ?   ?   A . n 
A 1 220  CYS 220  220  ?    ?   ?   A . n 
A 1 221  TYR 221  221  ?    ?   ?   A . n 
A 1 222  GLU 222  222  ?    ?   ?   A . n 
A 1 223  ARG 223  223  ?    ?   ?   A . n 
A 1 224  GLY 224  224  ?    ?   ?   A . n 
A 1 225  GLU 225  225  ?    ?   ?   A . n 
A 1 226  LYS 226  226  ?    ?   ?   A . n 
A 1 227  PRO 227  227  ?    ?   ?   A . n 
A 1 228  LYS 228  228  ?    ?   ?   A . n 
A 1 229  VAL 229  229  ?    ?   ?   A . n 
A 1 230  THR 230  230  ?    ?   ?   A . n 
A 1 231  ASP 231  231  ?    ?   ?   A . n 
A 1 232  PHE 232  232  ?    ?   ?   A . n 
A 1 233  GLY 233  233  ?    ?   ?   A . n 
A 1 234  ASP 234  234  ?    ?   ?   A . n 
A 1 235  LYS 235  235  ?    ?   ?   A . n 
A 1 236  VAL 236  236  ?    ?   ?   A . n 
A 1 237  GLU 237  237  ?    ?   ?   A . n 
A 1 238  ASP 238  238  ?    ?   ?   A . n 
A 1 239  PRO 239  239  ?    ?   ?   A . n 
A 1 240  THR 240  240  ?    ?   ?   A . n 
A 1 241  PHE 241  241  ?    ?   ?   A . n 
A 1 242  LEU 242  242  ?    ?   ?   A . n 
A 1 243  ASN 243  243  ?    ?   ?   A . n 
A 1 244  GLN 244  244  ?    ?   ?   A . n 
A 1 245  LEU 245  245  ?    ?   ?   A . n 
A 1 246  GLN 246  246  ?    ?   ?   A . n 
A 1 247  SER 247  247  ?    ?   ?   A . n 
A 1 248  GLY 248  248  ?    ?   ?   A . n 
A 1 249  VAL 249  249  ?    ?   ?   A . n 
A 1 250  ASN 250  250  ?    ?   ?   A . n 
A 1 251  ARG 251  251  ?    ?   ?   A . n 
A 1 252  TRP 252  252  ?    ?   ?   A . n 
A 1 253  ILE 253  253  ?    ?   ?   A . n 
A 1 254  ARG 254  254  ?    ?   ?   A . n 
A 1 255  GLU 255  255  ?    ?   ?   A . n 
A 1 256  ILE 256  256  ?    ?   ?   A . n 
A 1 257  GLN 257  257  ?    ?   ?   A . n 
A 1 258  LYS 258  258  ?    ?   ?   A . n 
A 1 259  VAL 259  259  ?    ?   ?   A . n 
A 1 260  THR 260  260  ?    ?   ?   A . n 
A 1 261  LYS 261  261  ?    ?   ?   A . n 
A 1 262  LEU 262  262  ?    ?   ?   A . n 
A 1 263  ASP 263  263  ?    ?   ?   A . n 
A 1 264  ARG 264  264  ?    ?   ?   A . n 
A 1 265  ASP 265  265  ?    ?   ?   A . n 
A 1 266  PRO 266  266  ?    ?   ?   A . n 
A 1 267  ALA 267  267  ?    ?   ?   A . n 
A 1 268  SER 268  268  ?    ?   ?   A . n 
A 1 269  GLY 269  269  ?    ?   ?   A . n 
A 1 270  THR 270  270  ?    ?   ?   A . n 
A 1 271  ALA 271  271  ?    ?   ?   A . n 
A 1 272  LEU 272  272  ?    ?   ?   A . n 
A 1 273  GLN 273  273  ?    ?   ?   A . n 
A 1 274  GLU 274  274  ?    ?   ?   A . n 
A 1 275  ILE 275  275  ?    ?   ?   A . n 
A 1 276  SER 276  276  ?    ?   ?   A . n 
A 1 277  PHE 277  277  ?    ?   ?   A . n 
A 1 278  TRP 278  278  ?    ?   ?   A . n 
A 1 279  LEU 279  279  ?    ?   ?   A . n 
A 1 280  ASN 280  280  ?    ?   ?   A . n 
A 1 281  LEU 281  281  ?    ?   ?   A . n 
A 1 282  GLU 282  282  ?    ?   ?   A . n 
A 1 283  ARG 283  283  ?    ?   ?   A . n 
A 1 284  ALA 284  284  ?    ?   ?   A . n 
A 1 285  LEU 285  285  ?    ?   ?   A . n 
A 1 286  TYR 286  286  ?    ?   ?   A . n 
A 1 287  ARG 287  287  ?    ?   ?   A . n 
A 1 288  ILE 288  288  ?    ?   ?   A . n 
A 1 289  GLN 289  289  ?    ?   ?   A . n 
A 1 290  GLU 290  290  ?    ?   ?   A . n 
A 1 291  LYS 291  291  ?    ?   ?   A . n 
A 1 292  ARG 292  292  ?    ?   ?   A . n 
A 1 293  GLU 293  293  ?    ?   ?   A . n 
A 1 294  SER 294  294  ?    ?   ?   A . n 
A 1 295  PRO 295  295  ?    ?   ?   A . n 
A 1 296  GLU 296  296  ?    ?   ?   A . n 
A 1 297  VAL 297  297  ?    ?   ?   A . n 
A 1 298  LEU 298  298  ?    ?   ?   A . n 
A 1 299  LEU 299  299  ?    ?   ?   A . n 
A 1 300  THR 300  300  ?    ?   ?   A . n 
A 1 301  LEU 301  301  ?    ?   ?   A . n 
A 1 302  ASP 302  302  ?    ?   ?   A . n 
A 1 303  ILE 303  303  ?    ?   ?   A . n 
A 1 304  LEU 304  304  ?    ?   ?   A . n 
A 1 305  LYS 305  305  ?    ?   ?   A . n 
A 1 306  HIS 306  306  ?    ?   ?   A . n 
A 1 307  GLY 307  307  ?    ?   ?   A . n 
A 1 308  LYS 308  308  ?    ?   ?   A . n 
A 1 309  ARG 309  309  ?    ?   ?   A . n 
A 1 310  PHE 310  310  ?    ?   ?   A . n 
A 1 311  HIS 311  311  ?    ?   ?   A . n 
A 1 312  ALA 312  312  ?    ?   ?   A . n 
A 1 313  THR 313  313  ?    ?   ?   A . n 
A 1 314  VAL 314  314  ?    ?   ?   A . n 
A 1 315  SER 315  315  ?    ?   ?   A . n 
A 1 316  PHE 316  316  ?    ?   ?   A . n 
A 1 317  ASP 317  317  ?    ?   ?   A . n 
A 1 318  THR 318  318  ?    ?   ?   A . n 
A 1 319  ASP 319  319  ?    ?   ?   A . n 
A 1 320  THR 320  320  ?    ?   ?   A . n 
A 1 321  GLY 321  321  ?    ?   ?   A . n 
A 1 322  LEU 322  322  ?    ?   ?   A . n 
A 1 323  LYS 323  323  ?    ?   ?   A . n 
A 1 324  GLN 324  324  ?    ?   ?   A . n 
A 1 325  ALA 325  325  ?    ?   ?   A . n 
A 1 326  LEU 326  326  ?    ?   ?   A . n 
A 1 327  GLU 327  327  ?    ?   ?   A . n 
A 1 328  THR 328  328  ?    ?   ?   A . n 
A 1 329  VAL 329  329  ?    ?   ?   A . n 
A 1 330  ASN 330  330  ?    ?   ?   A . n 
A 1 331  ASP 331  331  ?    ?   ?   A . n 
A 1 332  TYR 332  332  ?    ?   ?   A . n 
A 1 333  ASN 333  333  ?    ?   ?   A . n 
A 1 334  PRO 334  334  ?    ?   ?   A . n 
A 1 335  LEU 335  335  ?    ?   ?   A . n 
A 1 336  MET 336  336  ?    ?   ?   A . n 
A 1 337  LYS 337  337  ?    ?   ?   A . n 
A 1 338  ASP 338  338  ?    ?   ?   A . n 
A 1 339  PHE 339  339  ?    ?   ?   A . n 
A 1 340  PRO 340  340  ?    ?   ?   A . n 
A 1 341  LEU 341  341  ?    ?   ?   A . n 
A 1 342  ASN 342  342  ?    ?   ?   A . n 
A 1 343  ASP 343  343  ?    ?   ?   A . n 
A 1 344  LEU 344  344  ?    ?   ?   A . n 
A 1 345  LEU 345  345  ?    ?   ?   A . n 
A 1 346  SER 346  346  ?    ?   ?   A . n 
A 1 347  ALA 347  347  ?    ?   ?   A . n 
A 1 348  THR 348  348  ?    ?   ?   A . n 
A 1 349  GLU 349  349  ?    ?   ?   A . n 
A 1 350  LEU 350  350  ?    ?   ?   A . n 
A 1 351  ASP 351  351  ?    ?   ?   A . n 
A 1 352  LYS 352  352  ?    ?   ?   A . n 
A 1 353  ILE 353  353  ?    ?   ?   A . n 
A 1 354  ARG 354  354  ?    ?   ?   A . n 
A 1 355  GLN 355  355  ?    ?   ?   A . n 
A 1 356  ALA 356  356  ?    ?   ?   A . n 
A 1 357  LEU 357  357  ?    ?   ?   A . n 
A 1 358  VAL 358  358  ?    ?   ?   A . n 
A 1 359  ALA 359  359  ?    ?   ?   A . n 
A 1 360  ILE 360  360  ?    ?   ?   A . n 
A 1 361  PHE 361  361  ?    ?   ?   A . n 
A 1 362  THR 362  362  ?    ?   ?   A . n 
A 1 363  HIS 363  363  ?    ?   ?   A . n 
A 1 364  LEU 364  364  ?    ?   ?   A . n 
A 1 365  ARG 365  365  ?    ?   ?   A . n 
A 1 366  LYS 366  366  ?    ?   ?   A . n 
A 1 367  ILE 367  367  ?    ?   ?   A . n 
A 1 368  ARG 368  368  ?    ?   ?   A . n 
A 1 369  ASN 369  369  ?    ?   ?   A . n 
A 1 370  THR 370  370  ?    ?   ?   A . n 
A 1 371  LYS 371  371  ?    ?   ?   A . n 
A 1 372  TYR 372  372  ?    ?   ?   A . n 
A 1 373  PRO 373  373  ?    ?   ?   A . n 
A 1 374  ILE 374  374  ?    ?   ?   A . n 
A 1 375  GLN 375  375  ?    ?   ?   A . n 
A 1 376  ARG 376  376  ?    ?   ?   A . n 
A 1 377  ALA 377  377  ?    ?   ?   A . n 
A 1 378  LEU 378  378  ?    ?   ?   A . n 
A 1 379  ARG 379  379  ?    ?   ?   A . n 
A 1 380  LEU 380  380  ?    ?   ?   A . n 
A 1 381  VAL 381  381  ?    ?   ?   A . n 
A 1 382  GLU 382  382  ?    ?   ?   A . n 
A 1 383  ALA 383  383  ?    ?   ?   A . n 
A 1 384  ILE 384  384  ?    ?   ?   A . n 
A 1 385  SER 385  385  ?    ?   ?   A . n 
A 1 386  ARG 386  386  ?    ?   ?   A . n 
A 1 387  ASP 387  387  ?    ?   ?   A . n 
A 1 388  LEU 388  388  ?    ?   ?   A . n 
A 1 389  SER 389  389  ?    ?   ?   A . n 
A 1 390  SER 390  390  ?    ?   ?   A . n 
A 1 391  GLN 391  391  ?    ?   ?   A . n 
A 1 392  LEU 392  392  ?    ?   ?   A . n 
A 1 393  LEU 393  393  ?    ?   ?   A . n 
A 1 394  LYS 394  394  ?    ?   ?   A . n 
A 1 395  VAL 395  395  ?    ?   ?   A . n 
A 1 396  LEU 396  396  ?    ?   ?   A . n 
A 1 397  GLY 397  397  ?    ?   ?   A . n 
A 1 398  THR 398  398  ?    ?   ?   A . n 
A 1 399  ARG 399  399  ?    ?   ?   A . n 
A 1 400  LYS 400  400  ?    ?   ?   A . n 
A 1 401  LEU 401  401  ?    ?   ?   A . n 
A 1 402  MET 402  402  ?    ?   ?   A . n 
A 1 403  HIS 403  403  ?    ?   ?   A . n 
A 1 404  VAL 404  404  ?    ?   ?   A . n 
A 1 405  ALA 405  405  ?    ?   ?   A . n 
A 1 406  TYR 406  406  ?    ?   ?   A . n 
A 1 407  GLU 407  407  ?    ?   ?   A . n 
A 1 408  GLU 408  408  ?    ?   ?   A . n 
A 1 409  PHE 409  409  ?    ?   ?   A . n 
A 1 410  GLU 410  410  ?    ?   ?   A . n 
A 1 411  LYS 411  411  ?    ?   ?   A . n 
A 1 412  VAL 412  412  ?    ?   ?   A . n 
A 1 413  MET 413  413  ?    ?   ?   A . n 
A 1 414  VAL 414  414  ?    ?   ?   A . n 
A 1 415  ALA 415  415  ?    ?   ?   A . n 
A 1 416  CYS 416  416  ?    ?   ?   A . n 
A 1 417  PHE 417  417  ?    ?   ?   A . n 
A 1 418  GLU 418  418  ?    ?   ?   A . n 
A 1 419  VAL 419  419  ?    ?   ?   A . n 
A 1 420  PHE 420  420  ?    ?   ?   A . n 
A 1 421  GLN 421  421  ?    ?   ?   A . n 
A 1 422  THR 422  422  ?    ?   ?   A . n 
A 1 423  TRP 423  423  ?    ?   ?   A . n 
A 1 424  ASP 424  424  ?    ?   ?   A . n 
A 1 425  ASP 425  425  ?    ?   ?   A . n 
A 1 426  GLU 426  426  ?    ?   ?   A . n 
A 1 427  TYR 427  427  ?    ?   ?   A . n 
A 1 428  GLU 428  428  ?    ?   ?   A . n 
A 1 429  LYS 429  429  ?    ?   ?   A . n 
A 1 430  LEU 430  430  ?    ?   ?   A . n 
A 1 431  GLN 431  431  ?    ?   ?   A . n 
A 1 432  VAL 432  432  ?    ?   ?   A . n 
A 1 433  LEU 433  433  ?    ?   ?   A . n 
A 1 434  LEU 434  434  ?    ?   ?   A . n 
A 1 435  ARG 435  435  ?    ?   ?   A . n 
A 1 436  ASP 436  436  ?    ?   ?   A . n 
A 1 437  ILE 437  437  ?    ?   ?   A . n 
A 1 438  VAL 438  438  ?    ?   ?   A . n 
A 1 439  LYS 439  439  ?    ?   ?   A . n 
A 1 440  ARG 440  440  ?    ?   ?   A . n 
A 1 441  LYS 441  441  ?    ?   ?   A . n 
A 1 442  ARG 442  442  ?    ?   ?   A . n 
A 1 443  GLU 443  443  ?    ?   ?   A . n 
A 1 444  GLU 444  444  ?    ?   ?   A . n 
A 1 445  ASN 445  445  ?    ?   ?   A . n 
A 1 446  LEU 446  446  ?    ?   ?   A . n 
A 1 447  LYS 447  447  ?    ?   ?   A . n 
A 1 448  MET 448  448  ?    ?   ?   A . n 
A 1 449  VAL 449  449  ?    ?   ?   A . n 
A 1 450  TRP 450  450  ?    ?   ?   A . n 
A 1 451  ARG 451  451  ?    ?   ?   A . n 
A 1 452  ILE 452  452  ?    ?   ?   A . n 
A 1 453  ASN 453  453  ?    ?   ?   A . n 
A 1 454  PRO 454  454  ?    ?   ?   A . n 
A 1 455  ALA 455  455  ?    ?   ?   A . n 
A 1 456  HIS 456  456  ?    ?   ?   A . n 
A 1 457  ARG 457  457  ?    ?   ?   A . n 
A 1 458  LYS 458  458  ?    ?   ?   A . n 
A 1 459  LEU 459  459  ?    ?   ?   A . n 
A 1 460  GLN 460  460  ?    ?   ?   A . n 
A 1 461  ALA 461  461  ?    ?   ?   A . n 
A 1 462  ARG 462  462  ?    ?   ?   A . n 
A 1 463  LEU 463  463  ?    ?   ?   A . n 
A 1 464  ASP 464  464  ?    ?   ?   A . n 
A 1 465  GLN 465  465  ?    ?   ?   A . n 
A 1 466  MET 466  466  ?    ?   ?   A . n 
A 1 467  ARG 467  467  ?    ?   ?   A . n 
A 1 468  LYS 468  468  ?    ?   ?   A . n 
A 1 469  PHE 469  469  ?    ?   ?   A . n 
A 1 470  ARG 470  470  ?    ?   ?   A . n 
A 1 471  ARG 471  471  ?    ?   ?   A . n 
A 1 472  GLN 472  472  ?    ?   ?   A . n 
A 1 473  HIS 473  473  ?    ?   ?   A . n 
A 1 474  GLU 474  474  ?    ?   ?   A . n 
A 1 475  GLN 475  475  ?    ?   ?   A . n 
A 1 476  LEU 476  476  ?    ?   ?   A . n 
A 1 477  ARG 477  477  ?    ?   ?   A . n 
A 1 478  ALA 478  478  ?    ?   ?   A . n 
A 1 479  VAL 479  479  ?    ?   ?   A . n 
A 1 480  ILE 480  480  ?    ?   ?   A . n 
A 1 481  VAL 481  481  ?    ?   ?   A . n 
A 1 482  ARG 482  482  ?    ?   ?   A . n 
A 1 483  VAL 483  483  ?    ?   ?   A . n 
A 1 484  LEU 484  484  ?    ?   ?   A . n 
A 1 485  ARG 485  485  ?    ?   ?   A . n 
A 1 486  PRO 486  486  ?    ?   ?   A . n 
A 1 487  GLN 487  487  ?    ?   ?   A . n 
A 1 488  VAL 488  488  ?    ?   ?   A . n 
A 1 489  THR 489  489  ?    ?   ?   A . n 
A 1 490  ALA 490  490  ?    ?   ?   A . n 
A 1 491  VAL 491  491  ?    ?   ?   A . n 
A 1 492  ALA 492  492  ?    ?   ?   A . n 
A 1 493  GLN 493  493  ?    ?   ?   A . n 
A 1 494  GLN 494  494  ?    ?   ?   A . n 
A 1 495  ASN 495  495  ?    ?   ?   A . n 
A 1 496  GLN 496  496  ?    ?   ?   A . n 
A 1 497  GLY 497  497  ?    ?   ?   A . n 
A 1 498  GLU 498  498  ?    ?   ?   A . n 
A 1 499  VAL 499  499  ?    ?   ?   A . n 
A 1 500  PRO 500  500  ?    ?   ?   A . n 
A 1 501  GLU 501  501  ?    ?   ?   A . n 
A 1 502  PRO 502  502  ?    ?   ?   A . n 
A 1 503  GLN 503  503  ?    ?   ?   A . n 
A 1 504  ASP 504  504  ?    ?   ?   A . n 
A 1 505  MET 505  505  ?    ?   ?   A . n 
A 1 506  LYS 506  506  ?    ?   ?   A . n 
A 1 507  VAL 507  507  ?    ?   ?   A . n 
A 1 508  ALA 508  508  ?    ?   ?   A . n 
A 1 509  GLU 509  509  ?    ?   ?   A . n 
A 1 510  VAL 510  510  ?    ?   ?   A . n 
A 1 511  LEU 511  511  ?    ?   ?   A . n 
A 1 512  PHE 512  512  ?    ?   ?   A . n 
A 1 513  ASP 513  513  ?    ?   ?   A . n 
A 1 514  ALA 514  514  ?    ?   ?   A . n 
A 1 515  ALA 515  515  ?    ?   ?   A . n 
A 1 516  ASP 516  516  ?    ?   ?   A . n 
A 1 517  ALA 517  517  ?    ?   ?   A . n 
A 1 518  ASN 518  518  ?    ?   ?   A . n 
A 1 519  ALA 519  519  ?    ?   ?   A . n 
A 1 520  ILE 520  520  ?    ?   ?   A . n 
A 1 521  GLU 521  521  ?    ?   ?   A . n 
A 1 522  GLU 522  522  ?    ?   ?   A . n 
A 1 523  VAL 523  523  ?    ?   ?   A . n 
A 1 524  ASN 524  524  ?    ?   ?   A . n 
A 1 525  LEU 525  525  ?    ?   ?   A . n 
A 1 526  ALA 526  526  ?    ?   ?   A . n 
A 1 527  TYR 527  527  ?    ?   ?   A . n 
A 1 528  GLU 528  528  ?    ?   ?   A . n 
A 1 529  ASN 529  529  ?    ?   ?   A . n 
A 1 530  VAL 530  530  ?    ?   ?   A . n 
A 1 531  LYS 531  531  ?    ?   ?   A . n 
A 1 532  GLU 532  532  ?    ?   ?   A . n 
A 1 533  VAL 533  533  ?    ?   ?   A . n 
A 1 534  ASP 534  534  ?    ?   ?   A . n 
A 1 535  GLY 535  535  ?    ?   ?   A . n 
A 1 536  LEU 536  536  ?    ?   ?   A . n 
A 1 537  ASP 537  537  ?    ?   ?   A . n 
A 1 538  VAL 538  538  ?    ?   ?   A . n 
A 1 539  SER 539  539  ?    ?   ?   A . n 
A 1 540  LYS 540  540  ?    ?   ?   A . n 
A 1 541  GLU 541  541  ?    ?   ?   A . n 
A 1 542  GLY 542  542  ?    ?   ?   A . n 
A 1 543  THR 543  543  ?    ?   ?   A . n 
A 1 544  GLU 544  544  ?    ?   ?   A . n 
A 1 545  ALA 545  545  ?    ?   ?   A . n 
A 1 546  TRP 546  546  ?    ?   ?   A . n 
A 1 547  GLU 547  547  ?    ?   ?   A . n 
A 1 548  ALA 548  548  ?    ?   ?   A . n 
A 1 549  ALA 549  549  ?    ?   ?   A . n 
A 1 550  MET 550  550  ?    ?   ?   A . n 
A 1 551  LYS 551  551  ?    ?   ?   A . n 
A 1 552  ARG 552  552  ?    ?   ?   A . n 
A 1 553  TYR 553  553  ?    ?   ?   A . n 
A 1 554  ASP 554  554  ?    ?   ?   A . n 
A 1 555  GLU 555  555  ?    ?   ?   A . n 
A 1 556  ARG 556  556  ?    ?   ?   A . n 
A 1 557  ILE 557  557  ?    ?   ?   A . n 
A 1 558  ASP 558  558  ?    ?   ?   A . n 
A 1 559  ARG 559  559  ?    ?   ?   A . n 
A 1 560  VAL 560  560  ?    ?   ?   A . n 
A 1 561  GLU 561  561  ?    ?   ?   A . n 
A 1 562  THR 562  562  ?    ?   ?   A . n 
A 1 563  ARG 563  563  ?    ?   ?   A . n 
A 1 564  ILE 564  564  ?    ?   ?   A . n 
A 1 565  THR 565  565  ?    ?   ?   A . n 
A 1 566  ALA 566  566  ?    ?   ?   A . n 
A 1 567  ARG 567  567  ?    ?   ?   A . n 
A 1 568  LEU 568  568  ?    ?   ?   A . n 
A 1 569  ARG 569  569  ?    ?   ?   A . n 
A 1 570  ASP 570  570  ?    ?   ?   A . n 
A 1 571  GLN 571  571  ?    ?   ?   A . n 
A 1 572  LEU 572  572  ?    ?   ?   A . n 
A 1 573  GLY 573  573  ?    ?   ?   A . n 
A 1 574  THR 574  574  ?    ?   ?   A . n 
A 1 575  ALA 575  575  ?    ?   ?   A . n 
A 1 576  LYS 576  576  ?    ?   ?   A . n 
A 1 577  ASN 577  577  ?    ?   ?   A . n 
A 1 578  ALA 578  578  ?    ?   ?   A . n 
A 1 579  ASN 579  579  ?    ?   ?   A . n 
A 1 580  GLU 580  580  ?    ?   ?   A . n 
A 1 581  MET 581  581  ?    ?   ?   A . n 
A 1 582  PHE 582  582  ?    ?   ?   A . n 
A 1 583  ARG 583  583  ?    ?   ?   A . n 
A 1 584  ILE 584  584  ?    ?   ?   A . n 
A 1 585  PHE 585  585  ?    ?   ?   A . n 
A 1 586  SER 586  586  ?    ?   ?   A . n 
A 1 587  ARG 587  587  ?    ?   ?   A . n 
A 1 588  PHE 588  588  ?    ?   ?   A . n 
A 1 589  ASN 589  589  ?    ?   ?   A . n 
A 1 590  ALA 590  590  ?    ?   ?   A . n 
A 1 591  LEU 591  591  ?    ?   ?   A . n 
A 1 592  PHE 592  592  ?    ?   ?   A . n 
A 1 593  VAL 593  593  ?    ?   ?   A . n 
A 1 594  ARG 594  594  ?    ?   ?   A . n 
A 1 595  PRO 595  595  ?    ?   ?   A . n 
A 1 596  HIS 596  596  ?    ?   ?   A . n 
A 1 597  ILE 597  597  ?    ?   ?   A . n 
A 1 598  ARG 598  598  ?    ?   ?   A . n 
A 1 599  GLY 599  599  ?    ?   ?   A . n 
A 1 600  ALA 600  600  ?    ?   ?   A . n 
A 1 601  ILE 601  601  ?    ?   ?   A . n 
A 1 602  ARG 602  602  ?    ?   ?   A . n 
A 1 603  GLU 603  603  ?    ?   ?   A . n 
A 1 604  TYR 604  604  ?    ?   ?   A . n 
A 1 605  GLN 605  605  ?    ?   ?   A . n 
A 1 606  THR 606  606  ?    ?   ?   A . n 
A 1 607  GLN 607  607  ?    ?   ?   A . n 
A 1 608  LEU 608  608  ?    ?   ?   A . n 
A 1 609  ILE 609  609  ?    ?   ?   A . n 
A 1 610  GLN 610  610  ?    ?   ?   A . n 
A 1 611  ARG 611  611  ?    ?   ?   A . n 
A 1 612  VAL 612  612  ?    ?   ?   A . n 
A 1 613  LYS 613  613  ?    ?   ?   A . n 
A 1 614  ASP 614  614  ?    ?   ?   A . n 
A 1 615  ASP 615  615  ?    ?   ?   A . n 
A 1 616  ILE 616  616  ?    ?   ?   A . n 
A 1 617  GLU 617  617  ?    ?   ?   A . n 
A 1 618  SER 618  618  ?    ?   ?   A . n 
A 1 619  LEU 619  619  ?    ?   ?   A . n 
A 1 620  HIS 620  620  ?    ?   ?   A . n 
A 1 621  ASP 621  621  ?    ?   ?   A . n 
A 1 622  LYS 622  622  ?    ?   ?   A . n 
A 1 623  PHE 623  623  ?    ?   ?   A . n 
A 1 624  LYS 624  624  ?    ?   ?   A . n 
A 1 625  VAL 625  625  ?    ?   ?   A . n 
A 1 626  GLN 626  626  ?    ?   ?   A . n 
A 1 627  TYR 627  627  ?    ?   ?   A . n 
A 1 628  PRO 628  628  ?    ?   ?   A . n 
A 1 629  GLN 629  629  ?    ?   ?   A . n 
A 1 630  SER 630  630  ?    ?   ?   A . n 
A 1 631  GLN 631  631  ?    ?   ?   A . n 
A 1 632  ALA 632  632  ?    ?   ?   A . n 
A 1 633  CYS 633  633  ?    ?   ?   A . n 
A 1 634  LYS 634  634  ?    ?   ?   A . n 
A 1 635  MET 635  635  ?    ?   ?   A . n 
A 1 636  SER 636  636  ?    ?   ?   A . n 
A 1 637  HIS 637  637  ?    ?   ?   A . n 
A 1 638  VAL 638  638  ?    ?   ?   A . n 
A 1 639  ARG 639  639  ?    ?   ?   A . n 
A 1 640  ASP 640  640  ?    ?   ?   A . n 
A 1 641  LEU 641  641  ?    ?   ?   A . n 
A 1 642  PRO 642  642  ?    ?   ?   A . n 
A 1 643  PRO 643  643  ?    ?   ?   A . n 
A 1 644  VAL 644  644  ?    ?   ?   A . n 
A 1 645  SER 645  645  ?    ?   ?   A . n 
A 1 646  GLY 646  646  ?    ?   ?   A . n 
A 1 647  SER 647  647  ?    ?   ?   A . n 
A 1 648  ILE 648  648  ?    ?   ?   A . n 
A 1 649  ILE 649  649  ?    ?   ?   A . n 
A 1 650  TRP 650  650  ?    ?   ?   A . n 
A 1 651  ALA 651  651  ?    ?   ?   A . n 
A 1 652  LYS 652  652  ?    ?   ?   A . n 
A 1 653  GLN 653  653  ?    ?   ?   A . n 
A 1 654  ILE 654  654  ?    ?   ?   A . n 
A 1 655  ASP 655  655  ?    ?   ?   A . n 
A 1 656  ARG 656  656  ?    ?   ?   A . n 
A 1 657  GLN 657  657  ?    ?   ?   A . n 
A 1 658  LEU 658  658  ?    ?   ?   A . n 
A 1 659  THR 659  659  ?    ?   ?   A . n 
A 1 660  ALA 660  660  ?    ?   ?   A . n 
A 1 661  TYR 661  661  ?    ?   ?   A . n 
A 1 662  MET 662  662  ?    ?   ?   A . n 
A 1 663  LYS 663  663  ?    ?   ?   A . n 
A 1 664  ARG 664  664  ?    ?   ?   A . n 
A 1 665  VAL 665  665  ?    ?   ?   A . n 
A 1 666  GLU 666  666  ?    ?   ?   A . n 
A 1 667  ASP 667  667  ?    ?   ?   A . n 
A 1 668  VAL 668  668  ?    ?   ?   A . n 
A 1 669  LEU 669  669  ?    ?   ?   A . n 
A 1 670  GLY 670  670  ?    ?   ?   A . n 
A 1 671  LYS 671  671  ?    ?   ?   A . n 
A 1 672  GLY 672  672  ?    ?   ?   A . n 
A 1 673  TRP 673  673  ?    ?   ?   A . n 
A 1 674  GLU 674  674  ?    ?   ?   A . n 
A 1 675  ASN 675  675  ?    ?   ?   A . n 
A 1 676  HIS 676  676  ?    ?   ?   A . n 
A 1 677  VAL 677  677  ?    ?   ?   A . n 
A 1 678  GLU 678  678  ?    ?   ?   A . n 
A 1 679  GLY 679  679  ?    ?   ?   A . n 
A 1 680  GLN 680  680  ?    ?   ?   A . n 
A 1 681  LYS 681  681  ?    ?   ?   A . n 
A 1 682  LEU 682  682  ?    ?   ?   A . n 
A 1 683  LYS 683  683  ?    ?   ?   A . n 
A 1 684  GLN 684  684  ?    ?   ?   A . n 
A 1 685  ASP 685  685  ?    ?   ?   A . n 
A 1 686  GLY 686  686  ?    ?   ?   A . n 
A 1 687  ASP 687  687  ?    ?   ?   A . n 
A 1 688  SER 688  688  ?    ?   ?   A . n 
A 1 689  PHE 689  689  ?    ?   ?   A . n 
A 1 690  ARG 690  690  ?    ?   ?   A . n 
A 1 691  MET 691  691  ?    ?   ?   A . n 
A 1 692  LYS 692  692  ?    ?   ?   A . n 
A 1 693  LEU 693  693  ?    ?   ?   A . n 
A 1 694  ASN 694  694  ?    ?   ?   A . n 
A 1 695  THR 695  695  ?    ?   ?   A . n 
A 1 696  GLN 696  696  ?    ?   ?   A . n 
A 1 697  GLU 697  697  ?    ?   ?   A . n 
A 1 698  ILE 698  698  ?    ?   ?   A . n 
A 1 699  PHE 699  699  ?    ?   ?   A . n 
A 1 700  ASP 700  700  ?    ?   ?   A . n 
A 1 701  ASP 701  701  ?    ?   ?   A . n 
A 1 702  TRP 702  702  ?    ?   ?   A . n 
A 1 703  ALA 703  703  ?    ?   ?   A . n 
A 1 704  ARG 704  704  ?    ?   ?   A . n 
A 1 705  LYS 705  705  ?    ?   ?   A . n 
A 1 706  VAL 706  706  ?    ?   ?   A . n 
A 1 707  GLN 707  707  ?    ?   ?   A . n 
A 1 708  GLN 708  708  ?    ?   ?   A . n 
A 1 709  ARG 709  709  ?    ?   ?   A . n 
A 1 710  ASN 710  710  ?    ?   ?   A . n 
A 1 711  LEU 711  711  ?    ?   ?   A . n 
A 1 712  GLY 712  712  ?    ?   ?   A . n 
A 1 713  VAL 713  713  ?    ?   ?   A . n 
A 1 714  SER 714  714  ?    ?   ?   A . n 
A 1 715  GLY 715  715  ?    ?   ?   A . n 
A 1 716  ARG 716  716  ?    ?   ?   A . n 
A 1 717  ILE 717  717  ?    ?   ?   A . n 
A 1 718  PHE 718  718  ?    ?   ?   A . n 
A 1 719  THR 719  719  ?    ?   ?   A . n 
A 1 720  ILE 720  720  ?    ?   ?   A . n 
A 1 721  GLU 721  721  ?    ?   ?   A . n 
A 1 722  SER 722  722  ?    ?   ?   A . n 
A 1 723  THR 723  723  ?    ?   ?   A . n 
A 1 724  ARG 724  724  ?    ?   ?   A . n 
A 1 725  VAL 725  725  ?    ?   ?   A . n 
A 1 726  ARG 726  726  ?    ?   ?   A . n 
A 1 727  GLY 727  727  ?    ?   ?   A . n 
A 1 728  ARG 728  728  ?    ?   ?   A . n 
A 1 729  THR 729  729  ?    ?   ?   A . n 
A 1 730  GLY 730  730  ?    ?   ?   A . n 
A 1 731  ASN 731  731  ?    ?   ?   A . n 
A 1 732  VAL 732  732  ?    ?   ?   A . n 
A 1 733  LEU 733  733  ?    ?   ?   A . n 
A 1 734  LYS 734  734  ?    ?   ?   A . n 
A 1 735  LEU 735  735  ?    ?   ?   A . n 
A 1 736  LYS 736  736  ?    ?   ?   A . n 
A 1 737  VAL 737  737  ?    ?   ?   A . n 
A 1 738  ASN 738  738  ?    ?   ?   A . n 
A 1 739  PHE 739  739  ?    ?   ?   A . n 
A 1 740  LEU 740  740  ?    ?   ?   A . n 
A 1 741  PRO 741  741  ?    ?   ?   A . n 
A 1 742  GLU 742  742  ?    ?   ?   A . n 
A 1 743  ILE 743  743  ?    ?   ?   A . n 
A 1 744  ILE 744  744  ?    ?   ?   A . n 
A 1 745  THR 745  745  ?    ?   ?   A . n 
A 1 746  LEU 746  746  ?    ?   ?   A . n 
A 1 747  SER 747  747  ?    ?   ?   A . n 
A 1 748  LYS 748  748  ?    ?   ?   A . n 
A 1 749  GLU 749  749  ?    ?   ?   A . n 
A 1 750  VAL 750  750  ?    ?   ?   A . n 
A 1 751  ARG 751  751  ?    ?   ?   A . n 
A 1 752  ASN 752  752  ?    ?   ?   A . n 
A 1 753  LEU 753  753  ?    ?   ?   A . n 
A 1 754  LYS 754  754  ?    ?   ?   A . n 
A 1 755  TRP 755  755  ?    ?   ?   A . n 
A 1 756  LEU 756  756  ?    ?   ?   A . n 
A 1 757  GLY 757  757  ?    ?   ?   A . n 
A 1 758  PHE 758  758  ?    ?   ?   A . n 
A 1 759  ARG 759  759  ?    ?   ?   A . n 
A 1 760  VAL 760  760  ?    ?   ?   A . n 
A 1 761  PRO 761  761  ?    ?   ?   A . n 
A 1 762  LEU 762  762  ?    ?   ?   A . n 
A 1 763  ALA 763  763  ?    ?   ?   A . n 
A 1 764  ILE 764  764  ?    ?   ?   A . n 
A 1 765  VAL 765  765  ?    ?   ?   A . n 
A 1 766  ASN 766  766  ?    ?   ?   A . n 
A 1 767  LYS 767  767  ?    ?   ?   A . n 
A 1 768  ALA 768  768  ?    ?   ?   A . n 
A 1 769  HIS 769  769  ?    ?   ?   A . n 
A 1 770  GLN 770  770  ?    ?   ?   A . n 
A 1 771  ALA 771  771  ?    ?   ?   A . n 
A 1 772  ASN 772  772  ?    ?   ?   A . n 
A 1 773  GLN 773  773  ?    ?   ?   A . n 
A 1 774  LEU 774  774  ?    ?   ?   A . n 
A 1 775  TYR 775  775  ?    ?   ?   A . n 
A 1 776  PRO 776  776  ?    ?   ?   A . n 
A 1 777  PHE 777  777  ?    ?   ?   A . n 
A 1 778  ALA 778  778  ?    ?   ?   A . n 
A 1 779  ILE 779  779  ?    ?   ?   A . n 
A 1 780  SER 780  780  ?    ?   ?   A . n 
A 1 781  LEU 781  781  ?    ?   ?   A . n 
A 1 782  ILE 782  782  ?    ?   ?   A . n 
A 1 783  GLU 783  783  ?    ?   ?   A . n 
A 1 784  SER 784  784  ?    ?   ?   A . n 
A 1 785  VAL 785  785  ?    ?   ?   A . n 
A 1 786  ARG 786  786  ?    ?   ?   A . n 
A 1 787  THR 787  787  ?    ?   ?   A . n 
A 1 788  TYR 788  788  ?    ?   ?   A . n 
A 1 789  GLU 789  789  ?    ?   ?   A . n 
A 1 790  ARG 790  790  ?    ?   ?   A . n 
A 1 791  THR 791  791  ?    ?   ?   A . n 
A 1 792  CYS 792  792  ?    ?   ?   A . n 
A 1 793  GLU 793  793  ?    ?   ?   A . n 
A 1 794  LYS 794  794  ?    ?   ?   A . n 
A 1 795  VAL 795  795  ?    ?   ?   A . n 
A 1 796  GLU 796  796  ?    ?   ?   A . n 
A 1 797  GLU 797  797  ?    ?   ?   A . n 
A 1 798  ARG 798  798  ?    ?   ?   A . n 
A 1 799  ASN 799  799  ?    ?   ?   A . n 
A 1 800  THR 800  800  ?    ?   ?   A . n 
A 1 801  ILE 801  801  ?    ?   ?   A . n 
A 1 802  SER 802  802  ?    ?   ?   A . n 
A 1 803  LEU 803  803  ?    ?   ?   A . n 
A 1 804  LEU 804  804  ?    ?   ?   A . n 
A 1 805  VAL 805  805  ?    ?   ?   A . n 
A 1 806  ALA 806  806  ?    ?   ?   A . n 
A 1 807  GLY 807  807  ?    ?   ?   A . n 
A 1 808  LEU 808  808  ?    ?   ?   A . n 
A 1 809  LYS 809  809  ?    ?   ?   A . n 
A 1 810  LYS 810  810  ?    ?   ?   A . n 
A 1 811  GLU 811  811  ?    ?   ?   A . n 
A 1 812  VAL 812  812  ?    ?   ?   A . n 
A 1 813  GLN 813  813  ?    ?   ?   A . n 
A 1 814  ALA 814  814  ?    ?   ?   A . n 
A 1 815  LEU 815  815  ?    ?   ?   A . n 
A 1 816  ILE 816  816  ?    ?   ?   A . n 
A 1 817  ALA 817  817  ?    ?   ?   A . n 
A 1 818  GLU 818  818  ?    ?   ?   A . n 
A 1 819  GLY 819  819  ?    ?   ?   A . n 
A 1 820  ILE 820  820  ?    ?   ?   A . n 
A 1 821  ALA 821  821  ?    ?   ?   A . n 
A 1 822  LEU 822  822  ?    ?   ?   A . n 
A 1 823  VAL 823  823  ?    ?   ?   A . n 
A 1 824  TRP 824  824  ?    ?   ?   A . n 
A 1 825  GLU 825  825  ?    ?   ?   A . n 
A 1 826  SER 826  826  ?    ?   ?   A . n 
A 1 827  TYR 827  827  ?    ?   ?   A . n 
A 1 828  LYS 828  828  ?    ?   ?   A . n 
A 1 829  LEU 829  829  ?    ?   ?   A . n 
A 1 830  ASP 830  830  ?    ?   ?   A . n 
A 1 831  PRO 831  831  ?    ?   ?   A . n 
A 1 832  TYR 832  832  ?    ?   ?   A . n 
A 1 833  VAL 833  833  ?    ?   ?   A . n 
A 1 834  GLN 834  834  ?    ?   ?   A . n 
A 1 835  ARG 835  835  ?    ?   ?   A . n 
A 1 836  LEU 836  836  ?    ?   ?   A . n 
A 1 837  ALA 837  837  ?    ?   ?   A . n 
A 1 838  GLU 838  838  ?    ?   ?   A . n 
A 1 839  THR 839  839  ?    ?   ?   A . n 
A 1 840  VAL 840  840  ?    ?   ?   A . n 
A 1 841  PHE 841  841  ?    ?   ?   A . n 
A 1 842  ASN 842  842  ?    ?   ?   A . n 
A 1 843  PHE 843  843  ?    ?   ?   A . n 
A 1 844  GLN 844  844  ?    ?   ?   A . n 
A 1 845  GLU 845  845  ?    ?   ?   A . n 
A 1 846  LYS 846  846  ?    ?   ?   A . n 
A 1 847  VAL 847  847  ?    ?   ?   A . n 
A 1 848  ASP 848  848  ?    ?   ?   A . n 
A 1 849  ASP 849  849  ?    ?   ?   A . n 
A 1 850  LEU 850  850  ?    ?   ?   A . n 
A 1 851  LEU 851  851  ?    ?   ?   A . n 
A 1 852  ILE 852  852  ?    ?   ?   A . n 
A 1 853  ILE 853  853  ?    ?   ?   A . n 
A 1 854  GLU 854  854  ?    ?   ?   A . n 
A 1 855  GLU 855  855  ?    ?   ?   A . n 
A 1 856  LYS 856  856  ?    ?   ?   A . n 
A 1 857  ILE 857  857  ?    ?   ?   A . n 
A 1 858  ASP 858  858  ?    ?   ?   A . n 
A 1 859  LEU 859  859  ?    ?   ?   A . n 
A 1 860  GLU 860  860  ?    ?   ?   A . n 
A 1 861  VAL 861  861  ?    ?   ?   A . n 
A 1 862  ARG 862  862  ?    ?   ?   A . n 
A 1 863  SER 863  863  ?    ?   ?   A . n 
A 1 864  LEU 864  864  ?    ?   ?   A . n 
A 1 865  GLU 865  865  ?    ?   ?   A . n 
A 1 866  THR 866  866  ?    ?   ?   A . n 
A 1 867  CYS 867  867  ?    ?   ?   A . n 
A 1 868  MET 868  868  ?    ?   ?   A . n 
A 1 869  TYR 869  869  ?    ?   ?   A . n 
A 1 870  ASP 870  870  ?    ?   ?   A . n 
A 1 871  HIS 871  871  ?    ?   ?   A . n 
A 1 872  LYS 872  872  ?    ?   ?   A . n 
A 1 873  THR 873  873  ?    ?   ?   A . n 
A 1 874  PHE 874  874  ?    ?   ?   A . n 
A 1 875  SER 875  875  ?    ?   ?   A . n 
A 1 876  GLU 876  876  ?    ?   ?   A . n 
A 1 877  ILE 877  877  ?    ?   ?   A . n 
A 1 878  LEU 878  878  ?    ?   ?   A . n 
A 1 879  ASN 879  879  ?    ?   ?   A . n 
A 1 880  ARG 880  880  ?    ?   ?   A . n 
A 1 881  VAL 881  881  ?    ?   ?   A . n 
A 1 882  GLN 882  882  ?    ?   ?   A . n 
A 1 883  LYS 883  883  ?    ?   ?   A . n 
A 1 884  ALA 884  884  ?    ?   ?   A . n 
A 1 885  VAL 885  885  ?    ?   ?   A . n 
A 1 886  ASP 886  886  ?    ?   ?   A . n 
A 1 887  ASP 887  887  ?    ?   ?   A . n 
A 1 888  LEU 888  888  ?    ?   ?   A . n 
A 1 889  ASN 889  889  ?    ?   ?   A . n 
A 1 890  LEU 890  890  ?    ?   ?   A . n 
A 1 891  HIS 891  891  ?    ?   ?   A . n 
A 1 892  SER 892  892  ?    ?   ?   A . n 
A 1 893  TYR 893  893  ?    ?   ?   A . n 
A 1 894  SER 894  894  ?    ?   ?   A . n 
A 1 895  ASN 895  895  ?    ?   ?   A . n 
A 1 896  LEU 896  896  ?    ?   ?   A . n 
A 1 897  PRO 897  897  ?    ?   ?   A . n 
A 1 898  ILE 898  898  ?    ?   ?   A . n 
A 1 899  TRP 899  899  ?    ?   ?   A . n 
A 1 900  VAL 900  900  ?    ?   ?   A . n 
A 1 901  ASN 901  901  ?    ?   ?   A . n 
A 1 902  LYS 902  902  ?    ?   ?   A . n 
A 1 903  LEU 903  903  ?    ?   ?   A . n 
A 1 904  ASP 904  904  ?    ?   ?   A . n 
A 1 905  MET 905  905  ?    ?   ?   A . n 
A 1 906  GLU 906  906  ?    ?   ?   A . n 
A 1 907  ILE 907  907  ?    ?   ?   A . n 
A 1 908  GLU 908  908  ?    ?   ?   A . n 
A 1 909  ARG 909  909  ?    ?   ?   A . n 
A 1 910  ILE 910  910  ?    ?   ?   A . n 
A 1 911  LEU 911  911  ?    ?   ?   A . n 
A 1 912  GLY 912  912  ?    ?   ?   A . n 
A 1 913  VAL 913  913  ?    ?   ?   A . n 
A 1 914  ARG 914  914  ?    ?   ?   A . n 
A 1 915  LEU 915  915  ?    ?   ?   A . n 
A 1 916  GLN 916  916  ?    ?   ?   A . n 
A 1 917  ALA 917  917  ?    ?   ?   A . n 
A 1 918  GLY 918  918  ?    ?   ?   A . n 
A 1 919  LEU 919  919  ?    ?   ?   A . n 
A 1 920  ARG 920  920  ?    ?   ?   A . n 
A 1 921  ALA 921  921  ?    ?   ?   A . n 
A 1 922  TRP 922  922  ?    ?   ?   A . n 
A 1 923  THR 923  923  ?    ?   ?   A . n 
A 1 924  GLN 924  924  ?    ?   ?   A . n 
A 1 925  VAL 925  925  ?    ?   ?   A . n 
A 1 926  LEU 926  926  ?    ?   ?   A . n 
A 1 927  LEU 927  927  ?    ?   ?   A . n 
A 1 928  GLY 928  928  ?    ?   ?   A . n 
A 1 929  GLN 929  929  ?    ?   ?   A . n 
A 1 930  ALA 930  930  ?    ?   ?   A . n 
A 1 931  GLU 931  931  ?    ?   ?   A . n 
A 1 932  ASP 932  932  ?    ?   ?   A . n 
A 1 933  LYS 933  933  ?    ?   ?   A . n 
A 1 934  ALA 934  934  ?    ?   ?   A . n 
A 1 935  GLU 935  935  ?    ?   ?   A . n 
A 1 936  VAL 936  936  ?    ?   ?   A . n 
A 1 937  ASP 937  937  ?    ?   ?   A . n 
A 1 938  MET 938  938  ?    ?   ?   A . n 
A 1 939  ASP 939  939  ?    ?   ?   A . n 
A 1 940  THR 940  940  ?    ?   ?   A . n 
A 1 941  ASP 941  941  ?    ?   ?   A . n 
A 1 942  ALA 942  942  ?    ?   ?   A . n 
A 1 943  PRO 943  943  ?    ?   ?   A . n 
A 1 944  GLN 944  944  ?    ?   ?   A . n 
A 1 945  VAL 945  945  ?    ?   ?   A . n 
A 1 946  SER 946  946  ?    ?   ?   A . n 
A 1 947  HIS 947  947  ?    ?   ?   A . n 
A 1 948  LYS 948  948  ?    ?   ?   A . n 
A 1 949  PRO 949  949  ?    ?   ?   A . n 
A 1 950  GLY 950  950  ?    ?   ?   A . n 
A 1 951  GLY 951  951  ?    ?   ?   A . n 
A 1 952  GLU 952  952  ?    ?   ?   A . n 
A 1 953  PRO 953  953  ?    ?   ?   A . n 
A 1 954  LYS 954  954  ?    ?   ?   A . n 
A 1 955  ILE 955  955  ?    ?   ?   A . n 
A 1 956  LYS 956  956  ?    ?   ?   A . n 
A 1 957  ASN 957  957  ?    ?   ?   A . n 
A 1 958  VAL 958  958  ?    ?   ?   A . n 
A 1 959  VAL 959  959  ?    ?   ?   A . n 
A 1 960  HIS 960  960  ?    ?   ?   A . n 
A 1 961  GLU 961  961  ?    ?   ?   A . n 
A 1 962  LEU 962  962  ?    ?   ?   A . n 
A 1 963  ARG 963  963  ?    ?   ?   A . n 
A 1 964  ILE 964  964  ?    ?   ?   A . n 
A 1 965  THR 965  965  ?    ?   ?   A . n 
A 1 966  ASN 966  966  ?    ?   ?   A . n 
A 1 967  GLN 967  967  ?    ?   ?   A . n 
A 1 968  VAL 968  968  ?    ?   ?   A . n 
A 1 969  ILE 969  969  ?    ?   ?   A . n 
A 1 970  TYR 970  970  ?    ?   ?   A . n 
A 1 971  LEU 971  971  ?    ?   ?   A . n 
A 1 972  ASN 972  972  ?    ?   ?   A . n 
A 1 973  PRO 973  973  ?    ?   ?   A . n 
A 1 974  PRO 974  974  ?    ?   ?   A . n 
A 1 975  ILE 975  975  ?    ?   ?   A . n 
A 1 976  GLU 976  976  ?    ?   ?   A . n 
A 1 977  GLU 977  977  ?    ?   ?   A . n 
A 1 978  CYS 978  978  ?    ?   ?   A . n 
A 1 979  ARG 979  979  ?    ?   ?   A . n 
A 1 980  TYR 980  980  ?    ?   ?   A . n 
A 1 981  LYS 981  981  ?    ?   ?   A . n 
A 1 982  LEU 982  982  ?    ?   ?   A . n 
A 1 983  TYR 983  983  ?    ?   ?   A . n 
A 1 984  GLN 984  984  ?    ?   ?   A . n 
A 1 985  GLU 985  985  ?    ?   ?   A . n 
A 1 986  MET 986  986  ?    ?   ?   A . n 
A 1 987  PHE 987  987  ?    ?   ?   A . n 
A 1 988  ALA 988  988  ?    ?   ?   A . n 
A 1 989  TRP 989  989  ?    ?   ?   A . n 
A 1 990  LYS 990  990  ?    ?   ?   A . n 
A 1 991  MET 991  991  ?    ?   ?   A . n 
A 1 992  VAL 992  992  ?    ?   ?   A . n 
A 1 993  VAL 993  993  ?    ?   ?   A . n 
A 1 994  LEU 994  994  ?    ?   ?   A . n 
A 1 995  SER 995  995  ?    ?   ?   A . n 
A 1 996  LEU 996  996  ?    ?   ?   A . n 
A 1 997  PRO 997  997  ?    ?   ?   A . n 
A 1 998  ARG 998  998  ?    ?   ?   A . n 
A 1 999  ILE 999  999  ?    ?   ?   A . n 
A 1 1000 GLN 1000 1000 ?    ?   ?   A . n 
A 1 1001 SER 1001 1001 ?    ?   ?   A . n 
A 1 1002 GLN 1002 1002 ?    ?   ?   A . n 
A 1 1003 ARG 1003 1003 ?    ?   ?   A . n 
A 1 1004 TYR 1004 1004 ?    ?   ?   A . n 
A 1 1005 GLN 1005 1005 ?    ?   ?   A . n 
A 1 1006 VAL 1006 1006 ?    ?   ?   A . n 
A 1 1007 GLY 1007 1007 ?    ?   ?   A . n 
A 1 1008 VAL 1008 1008 ?    ?   ?   A . n 
A 1 1009 HIS 1009 1009 ?    ?   ?   A . n 
A 1 1010 TYR 1010 1010 ?    ?   ?   A . n 
A 1 1011 GLU 1011 1011 ?    ?   ?   A . n 
A 1 1012 LEU 1012 1012 ?    ?   ?   A . n 
A 1 1013 THR 1013 1013 ?    ?   ?   A . n 
A 1 1014 GLU 1014 1014 ?    ?   ?   A . n 
A 1 1015 GLU 1015 1015 ?    ?   ?   A . n 
A 1 1016 GLU 1016 1016 ?    ?   ?   A . n 
A 1 1017 LYS 1017 1017 ?    ?   ?   A . n 
A 1 1018 PHE 1018 1018 ?    ?   ?   A . n 
A 1 1019 TYR 1019 1019 ?    ?   ?   A . n 
A 1 1020 ARG 1020 1020 ?    ?   ?   A . n 
A 1 1021 ASN 1021 1021 ?    ?   ?   A . n 
A 1 1022 ALA 1022 1022 ?    ?   ?   A . n 
A 1 1023 LEU 1023 1023 ?    ?   ?   A . n 
A 1 1024 THR 1024 1024 ?    ?   ?   A . n 
A 1 1025 ARG 1025 1025 ?    ?   ?   A . n 
A 1 1026 MET 1026 1026 ?    ?   ?   A . n 
A 1 1027 PRO 1027 1027 ?    ?   ?   A . n 
A 1 1028 ASP 1028 1028 ?    ?   ?   A . n 
A 1 1029 GLY 1029 1029 ?    ?   ?   A . n 
A 1 1030 PRO 1030 1030 ?    ?   ?   A . n 
A 1 1031 VAL 1031 1031 ?    ?   ?   A . n 
A 1 1032 ALA 1032 1032 ?    ?   ?   A . n 
A 1 1033 LEU 1033 1033 ?    ?   ?   A . n 
A 1 1034 GLU 1034 1034 ?    ?   ?   A . n 
A 1 1035 GLU 1035 1035 ?    ?   ?   A . n 
A 1 1036 SER 1036 1036 ?    ?   ?   A . n 
A 1 1037 TYR 1037 1037 ?    ?   ?   A . n 
A 1 1038 SER 1038 1038 ?    ?   ?   A . n 
A 1 1039 ALA 1039 1039 ?    ?   ?   A . n 
A 1 1040 VAL 1040 1040 ?    ?   ?   A . n 
A 1 1041 MET 1041 1041 ?    ?   ?   A . n 
A 1 1042 GLY 1042 1042 ?    ?   ?   A . n 
A 1 1043 ILE 1043 1043 ?    ?   ?   A . n 
A 1 1044 VAL 1044 1044 ?    ?   ?   A . n 
A 1 1045 SER 1045 1045 ?    ?   ?   A . n 
A 1 1046 GLU 1046 1046 ?    ?   ?   A . n 
A 1 1047 VAL 1047 1047 ?    ?   ?   A . n 
A 1 1048 GLU 1048 1048 ?    ?   ?   A . n 
A 1 1049 GLN 1049 1049 ?    ?   ?   A . n 
A 1 1050 TYR 1050 1050 ?    ?   ?   A . n 
A 1 1051 VAL 1051 1051 ?    ?   ?   A . n 
A 1 1052 LYS 1052 1052 ?    ?   ?   A . n 
A 1 1053 VAL 1053 1053 ?    ?   ?   A . n 
A 1 1054 TRP 1054 1054 ?    ?   ?   A . n 
A 1 1055 LEU 1055 1055 ?    ?   ?   A . n 
A 1 1056 GLN 1056 1056 ?    ?   ?   A . n 
A 1 1057 TYR 1057 1057 ?    ?   ?   A . n 
A 1 1058 GLN 1058 1058 ?    ?   ?   A . n 
A 1 1059 CYS 1059 1059 ?    ?   ?   A . n 
A 1 1060 LEU 1060 1060 ?    ?   ?   A . n 
A 1 1061 TRP 1061 1061 ?    ?   ?   A . n 
A 1 1062 ASP 1062 1062 ?    ?   ?   A . n 
A 1 1063 MET 1063 1063 ?    ?   ?   A . n 
A 1 1064 GLN 1064 1064 ?    ?   ?   A . n 
A 1 1065 ALA 1065 1065 ?    ?   ?   A . n 
A 1 1066 GLU 1066 1066 ?    ?   ?   A . n 
A 1 1067 ASN 1067 1067 ?    ?   ?   A . n 
A 1 1068 ILE 1068 1068 ?    ?   ?   A . n 
A 1 1069 TYR 1069 1069 ?    ?   ?   A . n 
A 1 1070 ASN 1070 1070 ?    ?   ?   A . n 
A 1 1071 ARG 1071 1071 ?    ?   ?   A . n 
A 1 1072 LEU 1072 1072 ?    ?   ?   A . n 
A 1 1073 GLY 1073 1073 ?    ?   ?   A . n 
A 1 1074 GLU 1074 1074 ?    ?   ?   A . n 
A 1 1075 ASP 1075 1075 ?    ?   ?   A . n 
A 1 1076 LEU 1076 1076 ?    ?   ?   A . n 
A 1 1077 ASN 1077 1077 ?    ?   ?   A . n 
A 1 1078 LYS 1078 1078 ?    ?   ?   A . n 
A 1 1079 TRP 1079 1079 ?    ?   ?   A . n 
A 1 1080 GLN 1080 1080 ?    ?   ?   A . n 
A 1 1081 ALA 1081 1081 ?    ?   ?   A . n 
A 1 1082 LEU 1082 1082 ?    ?   ?   A . n 
A 1 1083 LEU 1083 1083 ?    ?   ?   A . n 
A 1 1084 VAL 1084 1084 ?    ?   ?   A . n 
A 1 1085 GLN 1085 1085 ?    ?   ?   A . n 
A 1 1086 ILE 1086 1086 ?    ?   ?   A . n 
A 1 1087 ARG 1087 1087 ?    ?   ?   A . n 
A 1 1088 LYS 1088 1088 ?    ?   ?   A . n 
A 1 1089 ALA 1089 1089 ?    ?   ?   A . n 
A 1 1090 ARG 1090 1090 ?    ?   ?   A . n 
A 1 1091 GLY 1091 1091 ?    ?   ?   A . n 
A 1 1092 THR 1092 1092 ?    ?   ?   A . n 
A 1 1093 PHE 1093 1093 ?    ?   ?   A . n 
A 1 1094 ASP 1094 1094 ?    ?   ?   A . n 
A 1 1095 ASN 1095 1095 ?    ?   ?   A . n 
A 1 1096 ALA 1096 1096 ?    ?   ?   A . n 
A 1 1097 GLU 1097 1097 ?    ?   ?   A . n 
A 1 1098 THR 1098 1098 ?    ?   ?   A . n 
A 1 1099 LYS 1099 1099 ?    ?   ?   A . n 
A 1 1100 LYS 1100 1100 ?    ?   ?   A . n 
A 1 1101 GLU 1101 1101 ?    ?   ?   A . n 
A 1 1102 PHE 1102 1102 ?    ?   ?   A . n 
A 1 1103 GLY 1103 1103 ?    ?   ?   A . n 
A 1 1104 PRO 1104 1104 ?    ?   ?   A . n 
A 1 1105 VAL 1105 1105 ?    ?   ?   A . n 
A 1 1106 VAL 1106 1106 ?    ?   ?   A . n 
A 1 1107 ILE 1107 1107 ?    ?   ?   A . n 
A 1 1108 ASP 1108 1108 ?    ?   ?   A . n 
A 1 1109 TYR 1109 1109 ?    ?   ?   A . n 
A 1 1110 GLY 1110 1110 ?    ?   ?   A . n 
A 1 1111 LYS 1111 1111 ?    ?   ?   A . n 
A 1 1112 VAL 1112 1112 ?    ?   ?   A . n 
A 1 1113 GLN 1113 1113 ?    ?   ?   A . n 
A 1 1114 SER 1114 1114 ?    ?   ?   A . n 
A 1 1115 LYS 1115 1115 ?    ?   ?   A . n 
A 1 1116 VAL 1116 1116 ?    ?   ?   A . n 
A 1 1117 ASN 1117 1117 ?    ?   ?   A . n 
A 1 1118 LEU 1118 1118 ?    ?   ?   A . n 
A 1 1119 LYS 1119 1119 ?    ?   ?   A . n 
A 1 1120 TYR 1120 1120 ?    ?   ?   A . n 
A 1 1121 ASP 1121 1121 ?    ?   ?   A . n 
A 1 1122 SER 1122 1122 ?    ?   ?   A . n 
A 1 1123 TRP 1123 1123 ?    ?   ?   A . n 
A 1 1124 HIS 1124 1124 ?    ?   ?   A . n 
A 1 1125 LYS 1125 1125 ?    ?   ?   A . n 
A 1 1126 GLU 1126 1126 ?    ?   ?   A . n 
A 1 1127 VAL 1127 1127 ?    ?   ?   A . n 
A 1 1128 LEU 1128 1128 ?    ?   ?   A . n 
A 1 1129 SER 1129 1129 ?    ?   ?   A . n 
A 1 1130 LYS 1130 1130 ?    ?   ?   A . n 
A 1 1131 PHE 1131 1131 ?    ?   ?   A . n 
A 1 1132 GLY 1132 1132 ?    ?   ?   A . n 
A 1 1133 GLN 1133 1133 ?    ?   ?   A . n 
A 1 1134 MET 1134 1134 ?    ?   ?   A . n 
A 1 1135 LEU 1135 1135 ?    ?   ?   A . n 
A 1 1136 GLY 1136 1136 ?    ?   ?   A . n 
A 1 1137 SER 1137 1137 ?    ?   ?   A . n 
A 1 1138 ASN 1138 1138 ?    ?   ?   A . n 
A 1 1139 MET 1139 1139 ?    ?   ?   A . n 
A 1 1140 THR 1140 1140 ?    ?   ?   A . n 
A 1 1141 GLU 1141 1141 ?    ?   ?   A . n 
A 1 1142 PHE 1142 1142 ?    ?   ?   A . n 
A 1 1143 HIS 1143 1143 ?    ?   ?   A . n 
A 1 1144 SER 1144 1144 ?    ?   ?   A . n 
A 1 1145 GLN 1145 1145 ?    ?   ?   A . n 
A 1 1146 ILE 1146 1146 ?    ?   ?   A . n 
A 1 1147 SER 1147 1147 ?    ?   ?   A . n 
A 1 1148 LYS 1148 1148 ?    ?   ?   A . n 
A 1 1149 SER 1149 1149 ?    ?   ?   A . n 
A 1 1150 ARG 1150 1150 ?    ?   ?   A . n 
A 1 1151 GLN 1151 1151 ?    ?   ?   A . n 
A 1 1152 GLU 1152 1152 ?    ?   ?   A . n 
A 1 1153 LEU 1153 1153 ?    ?   ?   A . n 
A 1 1154 GLU 1154 1154 ?    ?   ?   A . n 
A 1 1155 GLN 1155 1155 ?    ?   ?   A . n 
A 1 1156 HIS 1156 1156 ?    ?   ?   A . n 
A 1 1157 SER 1157 1157 ?    ?   ?   A . n 
A 1 1158 VAL 1158 1158 ?    ?   ?   A . n 
A 1 1159 ASP 1159 1159 ?    ?   ?   A . n 
A 1 1160 THR 1160 1160 ?    ?   ?   A . n 
A 1 1161 ALA 1161 1161 ?    ?   ?   A . n 
A 1 1162 SER 1162 1162 ?    ?   ?   A . n 
A 1 1163 THR 1163 1163 ?    ?   ?   A . n 
A 1 1164 SER 1164 1164 ?    ?   ?   A . n 
A 1 1165 ASP 1165 1165 ?    ?   ?   A . n 
A 1 1166 ALA 1166 1166 ?    ?   ?   A . n 
A 1 1167 VAL 1167 1167 ?    ?   ?   A . n 
A 1 1168 THR 1168 1168 ?    ?   ?   A . n 
A 1 1169 PHE 1169 1169 ?    ?   ?   A . n 
A 1 1170 ILE 1170 1170 ?    ?   ?   A . n 
A 1 1171 THR 1171 1171 ?    ?   ?   A . n 
A 1 1172 TYR 1172 1172 ?    ?   ?   A . n 
A 1 1173 VAL 1173 1173 ?    ?   ?   A . n 
A 1 1174 GLN 1174 1174 ?    ?   ?   A . n 
A 1 1175 SER 1175 1175 ?    ?   ?   A . n 
A 1 1176 LEU 1176 1176 ?    ?   ?   A . n 
A 1 1177 LYS 1177 1177 ?    ?   ?   A . n 
A 1 1178 ARG 1178 1178 ?    ?   ?   A . n 
A 1 1179 LYS 1179 1179 ?    ?   ?   A . n 
A 1 1180 ILE 1180 1180 ?    ?   ?   A . n 
A 1 1181 LYS 1181 1181 ?    ?   ?   A . n 
A 1 1182 GLN 1182 1182 ?    ?   ?   A . n 
A 1 1183 PHE 1183 1183 ?    ?   ?   A . n 
A 1 1184 GLU 1184 1184 ?    ?   ?   A . n 
A 1 1185 LYS 1185 1185 ?    ?   ?   A . n 
A 1 1186 GLN 1186 1186 ?    ?   ?   A . n 
A 1 1187 VAL 1187 1187 ?    ?   ?   A . n 
A 1 1188 GLU 1188 1188 ?    ?   ?   A . n 
A 1 1189 LEU 1189 1189 ?    ?   ?   A . n 
A 1 1190 TYR 1190 1190 ?    ?   ?   A . n 
A 1 1191 ARG 1191 1191 ?    ?   ?   A . n 
A 1 1192 ASN 1192 1192 ?    ?   ?   A . n 
A 1 1193 GLY 1193 1193 ?    ?   ?   A . n 
A 1 1194 GLN 1194 1194 ?    ?   ?   A . n 
A 1 1195 ARG 1195 1195 ?    ?   ?   A . n 
A 1 1196 LEU 1196 1196 ?    ?   ?   A . n 
A 1 1197 LEU 1197 1197 ?    ?   ?   A . n 
A 1 1198 GLU 1198 1198 ?    ?   ?   A . n 
A 1 1199 LYS 1199 1199 ?    ?   ?   A . n 
A 1 1200 GLN 1200 1200 ?    ?   ?   A . n 
A 1 1201 ARG 1201 1201 ?    ?   ?   A . n 
A 1 1202 PHE 1202 1202 ?    ?   ?   A . n 
A 1 1203 GLN 1203 1203 ?    ?   ?   A . n 
A 1 1204 PHE 1204 1204 ?    ?   ?   A . n 
A 1 1205 PRO 1205 1205 ?    ?   ?   A . n 
A 1 1206 PRO 1206 1206 ?    ?   ?   A . n 
A 1 1207 SER 1207 1207 ?    ?   ?   A . n 
A 1 1208 TRP 1208 1208 ?    ?   ?   A . n 
A 1 1209 LEU 1209 1209 ?    ?   ?   A . n 
A 1 1210 TYR 1210 1210 ?    ?   ?   A . n 
A 1 1211 ILE 1211 1211 ?    ?   ?   A . n 
A 1 1212 ASP 1212 1212 ?    ?   ?   A . n 
A 1 1213 ASN 1213 1213 ?    ?   ?   A . n 
A 1 1214 ILE 1214 1214 ?    ?   ?   A . n 
A 1 1215 GLU 1215 1215 ?    ?   ?   A . n 
A 1 1216 GLY 1216 1216 ?    ?   ?   A . n 
A 1 1217 GLU 1217 1217 ?    ?   ?   A . n 
A 1 1218 TRP 1218 1218 ?    ?   ?   A . n 
A 1 1219 GLY 1219 1219 ?    ?   ?   A . n 
A 1 1220 ALA 1220 1220 ?    ?   ?   A . n 
A 1 1221 PHE 1221 1221 ?    ?   ?   A . n 
A 1 1222 ASN 1222 1222 ?    ?   ?   A . n 
A 1 1223 ASP 1223 1223 ?    ?   ?   A . n 
A 1 1224 ILE 1224 1224 ?    ?   ?   A . n 
A 1 1225 MET 1225 1225 ?    ?   ?   A . n 
A 1 1226 ARG 1226 1226 ?    ?   ?   A . n 
A 1 1227 ARG 1227 1227 ?    ?   ?   A . n 
A 1 1228 LYS 1228 1228 ?    ?   ?   A . n 
A 1 1229 ASP 1229 1229 ?    ?   ?   A . n 
A 1 1230 SER 1230 1230 ?    ?   ?   A . n 
A 1 1231 ALA 1231 1231 ?    ?   ?   A . n 
A 1 1232 ILE 1232 1232 ?    ?   ?   A . n 
A 1 1233 GLN 1233 1233 ?    ?   ?   A . n 
A 1 1234 GLN 1234 1234 ?    ?   ?   A . n 
A 1 1235 GLN 1235 1235 ?    ?   ?   A . n 
A 1 1236 VAL 1236 1236 ?    ?   ?   A . n 
A 1 1237 ALA 1237 1237 ?    ?   ?   A . n 
A 1 1238 ASN 1238 1238 ?    ?   ?   A . n 
A 1 1239 LEU 1239 1239 ?    ?   ?   A . n 
A 1 1240 GLN 1240 1240 ?    ?   ?   A . n 
A 1 1241 MET 1241 1241 ?    ?   ?   A . n 
A 1 1242 LYS 1242 1242 ?    ?   ?   A . n 
A 1 1243 ILE 1243 1243 ?    ?   ?   A . n 
A 1 1244 VAL 1244 1244 ?    ?   ?   A . n 
A 1 1245 GLN 1245 1245 ?    ?   ?   A . n 
A 1 1246 GLU 1246 1246 ?    ?   ?   A . n 
A 1 1247 ASP 1247 1247 ?    ?   ?   A . n 
A 1 1248 ARG 1248 1248 ?    ?   ?   A . n 
A 1 1249 ALA 1249 1249 ?    ?   ?   A . n 
A 1 1250 VAL 1250 1250 ?    ?   ?   A . n 
A 1 1251 GLU 1251 1251 ?    ?   ?   A . n 
A 1 1252 SER 1252 1252 ?    ?   ?   A . n 
A 1 1253 ARG 1253 1253 ?    ?   ?   A . n 
A 1 1254 THR 1254 1254 ?    ?   ?   A . n 
A 1 1255 THR 1255 1255 ?    ?   ?   A . n 
A 1 1256 ASP 1256 1256 ?    ?   ?   A . n 
A 1 1257 LEU 1257 1257 ?    ?   ?   A . n 
A 1 1258 LEU 1258 1258 ?    ?   ?   A . n 
A 1 1259 THR 1259 1259 ?    ?   ?   A . n 
A 1 1260 ASP 1260 1260 ?    ?   ?   A . n 
A 1 1261 TRP 1261 1261 ?    ?   ?   A . n 
A 1 1262 GLU 1262 1262 ?    ?   ?   A . n 
A 1 1263 LYS 1263 1263 ?    ?   ?   A . n 
A 1 1264 THR 1264 1264 ?    ?   ?   A . n 
A 1 1265 LYS 1265 1265 ?    ?   ?   A . n 
A 1 1266 PRO 1266 1266 ?    ?   ?   A . n 
A 1 1267 VAL 1267 1267 ?    ?   ?   A . n 
A 1 1268 THR 1268 1268 ?    ?   ?   A . n 
A 1 1269 GLY 1269 1269 ?    ?   ?   A . n 
A 1 1270 ASN 1270 1270 ?    ?   ?   A . n 
A 1 1271 LEU 1271 1271 ?    ?   ?   A . n 
A 1 1272 ARG 1272 1272 ?    ?   ?   A . n 
A 1 1273 PRO 1273 1273 ?    ?   ?   A . n 
A 1 1274 GLU 1274 1274 ?    ?   ?   A . n 
A 1 1275 GLU 1275 1275 ?    ?   ?   A . n 
A 1 1276 ALA 1276 1276 ?    ?   ?   A . n 
A 1 1277 LEU 1277 1277 ?    ?   ?   A . n 
A 1 1278 GLN 1278 1278 ?    ?   ?   A . n 
A 1 1279 ALA 1279 1279 ?    ?   ?   A . n 
A 1 1280 LEU 1280 1280 ?    ?   ?   A . n 
A 1 1281 THR 1281 1281 ?    ?   ?   A . n 
A 1 1282 ILE 1282 1282 ?    ?   ?   A . n 
A 1 1283 TYR 1283 1283 ?    ?   ?   A . n 
A 1 1284 GLU 1284 1284 ?    ?   ?   A . n 
A 1 1285 GLY 1285 1285 ?    ?   ?   A . n 
A 1 1286 LYS 1286 1286 ?    ?   ?   A . n 
A 1 1287 PHE 1287 1287 ?    ?   ?   A . n 
A 1 1288 GLY 1288 1288 ?    ?   ?   A . n 
A 1 1289 ARG 1289 1289 ?    ?   ?   A . n 
A 1 1290 LEU 1290 1290 ?    ?   ?   A . n 
A 1 1291 LYS 1291 1291 ?    ?   ?   A . n 
A 1 1292 ASP 1292 1292 ?    ?   ?   A . n 
A 1 1293 ASP 1293 1293 ?    ?   ?   A . n 
A 1 1294 ARG 1294 1294 ?    ?   ?   A . n 
A 1 1295 GLU 1295 1295 ?    ?   ?   A . n 
A 1 1296 LYS 1296 1296 ?    ?   ?   A . n 
A 1 1297 CYS 1297 1297 ?    ?   ?   A . n 
A 1 1298 ALA 1298 1298 ?    ?   ?   A . n 
A 1 1299 LYS 1299 1299 ?    ?   ?   A . n 
A 1 1300 ALA 1300 1300 ?    ?   ?   A . n 
A 1 1301 LYS 1301 1301 ?    ?   ?   A . n 
A 1 1302 GLU 1302 1302 ?    ?   ?   A . n 
A 1 1303 ALA 1303 1303 ?    ?   ?   A . n 
A 1 1304 LEU 1304 1304 ?    ?   ?   A . n 
A 1 1305 GLU 1305 1305 ?    ?   ?   A . n 
A 1 1306 LEU 1306 1306 ?    ?   ?   A . n 
A 1 1307 THR 1307 1307 ?    ?   ?   A . n 
A 1 1308 ASP 1308 1308 ?    ?   ?   A . n 
A 1 1309 THR 1309 1309 ?    ?   ?   A . n 
A 1 1310 GLY 1310 1310 ?    ?   ?   A . n 
A 1 1311 LEU 1311 1311 ?    ?   ?   A . n 
A 1 1312 LEU 1312 1312 ?    ?   ?   A . n 
A 1 1313 SER 1313 1313 ?    ?   ?   A . n 
A 1 1314 GLY 1314 1314 ?    ?   ?   A . n 
A 1 1315 SER 1315 1315 ?    ?   ?   A . n 
A 1 1316 GLU 1316 1316 ?    ?   ?   A . n 
A 1 1317 GLU 1317 1317 ?    ?   ?   A . n 
A 1 1318 ARG 1318 1318 ?    ?   ?   A . n 
A 1 1319 VAL 1319 1319 ?    ?   ?   A . n 
A 1 1320 GLN 1320 1320 ?    ?   ?   A . n 
A 1 1321 VAL 1321 1321 ?    ?   ?   A . n 
A 1 1322 ALA 1322 1322 ?    ?   ?   A . n 
A 1 1323 LEU 1323 1323 ?    ?   ?   A . n 
A 1 1324 GLU 1324 1324 ?    ?   ?   A . n 
A 1 1325 GLU 1325 1325 ?    ?   ?   A . n 
A 1 1326 LEU 1326 1326 ?    ?   ?   A . n 
A 1 1327 GLN 1327 1327 1327 GLN GLN A . n 
A 1 1328 ASP 1328 1328 1328 ASP ASP A . n 
A 1 1329 LEU 1329 1329 1329 LEU LEU A . n 
A 1 1330 LYS 1330 1330 1330 LYS LYS A . n 
A 1 1331 GLY 1331 1331 1331 GLY GLY A . n 
A 1 1332 VAL 1332 1332 1332 VAL VAL A . n 
A 1 1333 TRP 1333 1333 1333 TRP TRP A . n 
A 1 1334 SER 1334 1334 1334 SER SER A . n 
A 1 1335 GLU 1335 1335 1335 GLU GLU A . n 
A 1 1336 LEU 1336 1336 1336 LEU LEU A . n 
A 1 1337 SER 1337 1337 1337 SER SER A . n 
A 1 1338 LYS 1338 1338 1338 LYS LYS A . n 
A 1 1339 VAL 1339 1339 1339 VAL VAL A . n 
A 1 1340 TRP 1340 1340 1340 TRP TRP A . n 
A 1 1341 GLU 1341 1341 1341 GLU GLU A . n 
A 1 1342 GLN 1342 1342 1342 GLN GLN A . n 
A 1 1343 ILE 1343 1343 1343 ILE ILE A . n 
A 1 1344 ASP 1344 1344 1344 ASP ASP A . n 
A 1 1345 GLN 1345 1345 1345 GLN GLN A . n 
A 1 1346 MET 1346 1346 1346 MET MET A . n 
A 1 1347 LYS 1347 1347 1347 LYS LYS A . n 
A 1 1348 GLU 1348 1348 1348 GLU GLU A . n 
A 1 1349 GLN 1349 1349 1349 GLN GLN A . n 
A 1 1350 PRO 1350 1350 1350 PRO PRO A . n 
A 1 1351 TRP 1351 1351 1351 TRP TRP A . n 
A 1 1352 VAL 1352 1352 1352 VAL VAL A . n 
A 1 1353 SER 1353 1353 1353 SER SER A . n 
A 1 1354 VAL 1354 1354 1354 VAL VAL A . n 
A 1 1355 GLN 1355 1355 1355 GLN GLN A . n 
A 1 1356 PRO 1356 1356 1356 PRO PRO A . n 
A 1 1357 ARG 1357 1357 1357 ARG ARG A . n 
A 1 1358 LYS 1358 1358 1358 LYS LYS A . n 
A 1 1359 LEU 1359 1359 1359 LEU LEU A . n 
A 1 1360 ARG 1360 1360 1360 ARG ARG A . n 
A 1 1361 GLN 1361 1361 1361 GLN GLN A . n 
A 1 1362 ASN 1362 1362 1362 ASN ASN A . n 
A 1 1363 LEU 1363 1363 1363 LEU LEU A . n 
A 1 1364 ASP 1364 1364 1364 ASP ASP A . n 
A 1 1365 ALA 1365 1365 1365 ALA ALA A . n 
A 1 1366 LEU 1366 1366 1366 LEU LEU A . n 
A 1 1367 LEU 1367 1367 1367 LEU LEU A . n 
A 1 1368 ASN 1368 1368 1368 ASN ASN A . n 
A 1 1369 GLN 1369 1369 1369 GLN GLN A . n 
A 1 1370 LEU 1370 1370 1370 LEU LEU A . n 
A 1 1371 LYS 1371 1371 1371 LYS LYS A . n 
A 1 1372 SER 1372 1372 1372 SER SER A . n 
A 1 1373 PHE 1373 1373 1373 PHE PHE A . n 
A 1 1374 PRO 1374 1374 1374 PRO PRO A . n 
A 1 1375 ALA 1375 1375 1375 ALA ALA A . n 
A 1 1376 ARG 1376 1376 1376 ARG ARG A . n 
A 1 1377 LEU 1377 1377 1377 LEU LEU A . n 
A 1 1378 ARG 1378 1378 1378 ARG ARG A . n 
A 1 1379 GLN 1379 1379 1379 GLN GLN A . n 
A 1 1380 TYR 1380 1380 1380 TYR TYR A . n 
A 1 1381 ALA 1381 1381 1381 ALA ALA A . n 
A 1 1382 SER 1382 1382 1382 SER SER A . n 
A 1 1383 TYR 1383 1383 1383 TYR TYR A . n 
A 1 1384 GLU 1384 1384 1384 GLU GLU A . n 
A 1 1385 PHE 1385 1385 1385 PHE PHE A . n 
A 1 1386 VAL 1386 1386 1386 VAL VAL A . n 
A 1 1387 GLN 1387 1387 1387 GLN GLN A . n 
A 1 1388 ARG 1388 1388 1388 ARG ARG A . n 
A 1 1389 LEU 1389 1389 1389 LEU LEU A . n 
A 1 1390 LEU 1390 1390 1390 LEU LEU A . n 
A 1 1391 LYS 1391 1391 1391 LYS LYS A . n 
A 1 1392 GLY 1392 1392 1392 GLY GLY A . n 
A 1 1393 TYR 1393 1393 1393 TYR TYR A . n 
A 1 1394 MET 1394 1394 1394 MET MET A . n 
A 1 1395 LYS 1395 1395 1395 LYS LYS A . n 
A 1 1396 ILE 1396 1396 1396 ILE ILE A . n 
A 1 1397 ASN 1397 1397 1397 ASN ASN A . n 
A 1 1398 MET 1398 1398 1398 MET MET A . n 
A 1 1399 LEU 1399 1399 1399 LEU LEU A . n 
A 1 1400 VAL 1400 1400 1400 VAL VAL A . n 
A 1 1401 ILE 1401 1401 1401 ILE ILE A . n 
A 1 1402 GLU 1402 1402 1402 GLU GLU A . n 
A 1 1403 LEU 1403 1403 1403 LEU LEU A . n 
A 1 1404 LYS 1404 1404 1404 LYS LYS A . n 
A 1 1405 SER 1405 1405 1405 SER SER A . n 
A 1 1406 GLU 1406 1406 1406 GLU GLU A . n 
A 1 1407 ALA 1407 1407 1407 ALA ALA A . n 
A 1 1408 LEU 1408 1408 1408 LEU LEU A . n 
A 1 1409 LYS 1409 1409 1409 LYS LYS A . n 
A 1 1410 ASP 1410 1410 1410 ASP ASP A . n 
A 1 1411 ARG 1411 1411 1411 ARG ARG A . n 
A 1 1412 HIS 1412 1412 1412 HIS HIS A . n 
A 1 1413 TRP 1413 1413 1413 TRP TRP A . n 
A 1 1414 LYS 1414 1414 1414 LYS LYS A . n 
A 1 1415 GLN 1415 1415 1415 GLN GLN A . n 
A 1 1416 LEU 1416 1416 1416 LEU LEU A . n 
A 1 1417 MET 1417 1417 1417 MET MET A . n 
A 1 1418 LYS 1418 1418 1418 LYS LYS A . n 
A 1 1419 ARG 1419 1419 1419 ARG ARG A . n 
A 1 1420 LEU 1420 1420 1420 LEU LEU A . n 
A 1 1421 HIS 1421 1421 1421 HIS HIS A . n 
A 1 1422 VAL 1422 1422 1422 VAL VAL A . n 
A 1 1423 ASN 1423 1423 1423 ASN ASN A . n 
A 1 1424 TRP 1424 1424 1424 TRP TRP A . n 
A 1 1425 VAL 1425 1425 1425 VAL VAL A . n 
A 1 1426 VAL 1426 1426 1426 VAL VAL A . n 
A 1 1427 SER 1427 1427 1427 SER SER A . n 
A 1 1428 GLU 1428 1428 1428 GLU GLU A . n 
A 1 1429 LEU 1429 1429 1429 LEU LEU A . n 
A 1 1430 THR 1430 1430 1430 THR THR A . n 
A 1 1431 LEU 1431 1431 1431 LEU LEU A . n 
A 1 1432 GLY 1432 1432 1432 GLY GLY A . n 
A 1 1433 GLN 1433 1433 1433 GLN GLN A . n 
A 1 1434 ILE 1434 1434 1434 ILE ILE A . n 
A 1 1435 TRP 1435 1435 1435 TRP TRP A . n 
A 1 1436 ASP 1436 1436 1436 ASP ASP A . n 
A 1 1437 VAL 1437 1437 1437 VAL VAL A . n 
A 1 1438 ASP 1438 1438 1438 ASP ASP A . n 
A 1 1439 LEU 1439 1439 1439 LEU LEU A . n 
A 1 1440 GLN 1440 1440 1440 GLN GLN A . n 
A 1 1441 LYS 1441 1441 1441 LYS LYS A . n 
A 1 1442 ASN 1442 1442 1442 ASN ASN A . n 
A 1 1443 GLU 1443 1443 1443 GLU GLU A . n 
A 1 1444 ALA 1444 1444 1444 ALA ALA A . n 
A 1 1445 ILE 1445 1445 1445 ILE ILE A . n 
A 1 1446 VAL 1446 1446 1446 VAL VAL A . n 
A 1 1447 LYS 1447 1447 1447 LYS LYS A . n 
A 1 1448 ASP 1448 1448 1448 ASP ASP A . n 
A 1 1449 VAL 1449 1449 1449 VAL VAL A . n 
A 1 1450 LEU 1450 1450 1450 LEU LEU A . n 
A 1 1451 LEU 1451 1451 1451 LEU LEU A . n 
A 1 1452 VAL 1452 1452 1452 VAL VAL A . n 
A 1 1453 ALA 1453 1453 1453 ALA ALA A . n 
A 1 1454 GLN 1454 1454 1454 GLN GLN A . n 
A 1 1455 GLY 1455 1455 1455 GLY GLY A . n 
A 1 1456 GLU 1456 1456 1456 GLU GLU A . n 
A 1 1457 MET 1457 1457 1457 MET MET A . n 
A 1 1458 ALA 1458 1458 1458 ALA ALA A . n 
A 1 1459 LEU 1459 1459 1459 LEU LEU A . n 
A 1 1460 GLU 1460 1460 1460 GLU GLU A . n 
A 1 1461 GLU 1461 1461 1461 GLU GLU A . n 
A 1 1462 PHE 1462 1462 1462 PHE PHE A . n 
A 1 1463 LEU 1463 1463 1463 LEU LEU A . n 
A 1 1464 LYS 1464 1464 1464 LYS LYS A . n 
A 1 1465 GLN 1465 1465 1465 GLN GLN A . n 
A 1 1466 ILE 1466 1466 1466 ILE ILE A . n 
A 1 1467 ARG 1467 1467 1467 ARG ARG A . n 
A 1 1468 GLU 1468 1468 1468 GLU GLU A . n 
A 1 1469 VAL 1469 1469 1469 VAL VAL A . n 
A 1 1470 TRP 1470 1470 1470 TRP TRP A . n 
A 1 1471 ASN 1471 1471 1471 ASN ASN A . n 
A 1 1472 THR 1472 1472 1472 THR THR A . n 
A 1 1473 TYR 1473 1473 1473 TYR TYR A . n 
A 1 1474 GLU 1474 1474 1474 GLU GLU A . n 
A 1 1475 LEU 1475 1475 1475 LEU LEU A . n 
A 1 1476 ASP 1476 1476 1476 ASP ASP A . n 
A 1 1477 LEU 1477 1477 1477 LEU LEU A . n 
A 1 1478 VAL 1478 1478 1478 VAL VAL A . n 
A 1 1479 ASN 1479 1479 1479 ASN ASN A . n 
A 1 1480 TYR 1480 1480 1480 TYR TYR A . n 
A 1 1481 GLN 1481 1481 1481 GLN GLN A . n 
A 1 1482 ASN 1482 1482 1482 ASN ASN A . n 
A 1 1483 LYS 1483 1483 1483 LYS LYS A . n 
A 1 1484 CYS 1484 1484 1484 CYS CYS A . n 
A 1 1485 ARG 1485 1485 1485 ARG ARG A . n 
A 1 1486 LEU 1486 1486 1486 LEU LEU A . n 
A 1 1487 ILE 1487 1487 1487 ILE ILE A . n 
A 1 1488 ARG 1488 1488 1488 ARG ARG A . n 
A 1 1489 GLY 1489 1489 1489 GLY GLY A . n 
A 1 1490 TRP 1490 1490 1490 TRP TRP A . n 
A 1 1491 ASP 1491 1491 1491 ASP ASP A . n 
A 1 1492 ASP 1492 1492 1492 ASP ASP A . n 
A 1 1493 LEU 1493 1493 1493 LEU LEU A . n 
A 1 1494 PHE 1494 1494 1494 PHE PHE A . n 
A 1 1495 ASN 1495 1495 1495 ASN ASN A . n 
A 1 1496 LYS 1496 1496 1496 LYS LYS A . n 
A 1 1497 VAL 1497 1497 1497 VAL VAL A . n 
A 1 1498 LYS 1498 1498 1498 LYS LYS A . n 
A 1 1499 GLU 1499 1499 1499 GLU GLU A . n 
A 1 1500 HIS 1500 1500 1500 HIS HIS A . n 
A 1 1501 ILE 1501 1501 1501 ILE ILE A . n 
A 1 1502 ASN 1502 1502 1502 ASN ASN A . n 
A 1 1503 SER 1503 1503 1503 SER SER A . n 
A 1 1504 VAL 1504 1504 1504 VAL VAL A . n 
A 1 1505 SER 1505 1505 1505 SER SER A . n 
A 1 1506 ALA 1506 1506 1506 ALA ALA A . n 
A 1 1507 MET 1507 1507 1507 MET MET A . n 
A 1 1508 LYS 1508 1508 1508 LYS LYS A . n 
A 1 1509 LEU 1509 1509 1509 LEU LEU A . n 
A 1 1510 SER 1510 1510 1510 SER SER A . n 
A 1 1511 PRO 1511 1511 1511 PRO PRO A . n 
A 1 1512 TYR 1512 1512 1512 TYR TYR A . n 
A 1 1513 TYR 1513 1513 1513 TYR TYR A . n 
A 1 1514 LYS 1514 1514 1514 LYS LYS A . n 
A 1 1515 VAL 1515 1515 1515 VAL VAL A . n 
A 1 1516 PHE 1516 1516 1516 PHE PHE A . n 
A 1 1517 GLU 1517 1517 1517 GLU GLU A . n 
A 1 1518 GLU 1518 1518 1518 GLU GLU A . n 
A 1 1519 ASP 1519 1519 1519 ASP ASP A . n 
A 1 1520 ALA 1520 1520 1520 ALA ALA A . n 
A 1 1521 LEU 1521 1521 1521 LEU LEU A . n 
A 1 1522 SER 1522 1522 1522 SER SER A . n 
A 1 1523 TRP 1523 1523 1523 TRP TRP A . n 
A 1 1524 GLU 1524 1524 1524 GLU GLU A . n 
A 1 1525 ASP 1525 1525 1525 ASP ASP A . n 
A 1 1526 LYS 1526 1526 1526 LYS LYS A . n 
A 1 1527 LEU 1527 1527 1527 LEU LEU A . n 
A 1 1528 ASN 1528 1528 1528 ASN ASN A . n 
A 1 1529 ARG 1529 1529 1529 ARG ARG A . n 
A 1 1530 ILE 1530 1530 1530 ILE ILE A . n 
A 1 1531 MET 1531 1531 1531 MET MET A . n 
A 1 1532 ALA 1532 1532 1532 ALA ALA A . n 
A 1 1533 LEU 1533 1533 1533 LEU LEU A . n 
A 1 1534 PHE 1534 1534 1534 PHE PHE A . n 
A 1 1535 ASP 1535 1535 1535 ASP ASP A . n 
A 1 1536 VAL 1536 1536 1536 VAL VAL A . n 
A 1 1537 TRP 1537 1537 1537 TRP TRP A . n 
A 1 1538 ILE 1538 1538 1538 ILE ILE A . n 
A 1 1539 ASP 1539 1539 1539 ASP ASP A . n 
A 1 1540 VAL 1540 1540 1540 VAL VAL A . n 
A 1 1541 GLN 1541 1541 1541 GLN GLN A . n 
A 1 1542 ARG 1542 1542 1542 ARG ARG A . n 
A 1 1543 ARG 1543 1543 1543 ARG ARG A . n 
A 1 1544 TRP 1544 1544 1544 TRP TRP A . n 
A 1 1545 VAL 1545 1545 1545 VAL VAL A . n 
A 1 1546 TYR 1546 1546 1546 TYR TYR A . n 
A 1 1547 LEU 1547 1547 1547 LEU LEU A . n 
A 1 1548 GLU 1548 1548 1548 GLU GLU A . n 
A 1 1549 GLY 1549 1549 1549 GLY GLY A . n 
A 1 1550 ILE 1550 1550 1550 ILE ILE A . n 
A 1 1551 PHE 1551 1551 1551 PHE PHE A . n 
A 1 1552 THR 1552 1552 1552 THR THR A . n 
A 1 1553 GLY 1553 1553 1553 GLY GLY A . n 
A 1 1554 SER 1554 1554 1554 SER SER A . n 
A 1 1555 ALA 1555 1555 1555 ALA ALA A . n 
A 1 1556 ASP 1556 1556 1556 ASP ASP A . n 
A 1 1557 ILE 1557 1557 1557 ILE ILE A . n 
A 1 1558 LYS 1558 1558 1558 LYS LYS A . n 
A 1 1559 HIS 1559 1559 1559 HIS HIS A . n 
A 1 1560 LEU 1560 1560 1560 LEU LEU A . n 
A 1 1561 LEU 1561 1561 1561 LEU LEU A . n 
A 1 1562 PRO 1562 1562 1562 PRO PRO A . n 
A 1 1563 VAL 1563 1563 1563 VAL VAL A . n 
A 1 1564 GLU 1564 1564 1564 GLU GLU A . n 
A 1 1565 THR 1565 1565 1565 THR THR A . n 
A 1 1566 GLN 1566 1566 1566 GLN GLN A . n 
A 1 1567 ARG 1567 1567 1567 ARG ARG A . n 
A 1 1568 PHE 1568 1568 1568 PHE PHE A . n 
A 1 1569 GLN 1569 1569 1569 GLN GLN A . n 
A 1 1570 SER 1570 1570 1570 SER SER A . n 
A 1 1571 ILE 1571 1571 1571 ILE ILE A . n 
A 1 1572 SER 1572 1572 1572 SER SER A . n 
A 1 1573 THR 1573 1573 1573 THR THR A . n 
A 1 1574 GLU 1574 1574 1574 GLU GLU A . n 
A 1 1575 PHE 1575 1575 1575 PHE PHE A . n 
A 1 1576 LEU 1576 1576 1576 LEU LEU A . n 
A 1 1577 ALA 1577 1577 1577 ALA ALA A . n 
A 1 1578 LEU 1578 1578 1578 LEU LEU A . n 
A 1 1579 MET 1579 1579 1579 MET MET A . n 
A 1 1580 LYS 1580 1580 1580 LYS LYS A . n 
A 1 1581 LYS 1581 1581 1581 LYS LYS A . n 
A 1 1582 VAL 1582 1582 1582 VAL VAL A . n 
A 1 1583 SER 1583 1583 1583 SER SER A . n 
A 1 1584 LYS 1584 1584 1584 LYS LYS A . n 
A 1 1585 SER 1585 1585 1585 SER SER A . n 
A 1 1586 PRO 1586 1586 1586 PRO PRO A . n 
A 1 1587 LEU 1587 1587 1587 LEU LEU A . n 
A 1 1588 VAL 1588 1588 1588 VAL VAL A . n 
A 1 1589 MET 1589 1589 1589 MET MET A . n 
A 1 1590 ASP 1590 1590 1590 ASP ASP A . n 
A 1 1591 VAL 1591 1591 1591 VAL VAL A . n 
A 1 1592 LEU 1592 1592 1592 LEU LEU A . n 
A 1 1593 ASN 1593 1593 1593 ASN ASN A . n 
A 1 1594 ILE 1594 1594 1594 ILE ILE A . n 
A 1 1595 GLN 1595 1595 1595 GLN GLN A . n 
A 1 1596 GLY 1596 1596 1596 GLY GLY A . n 
A 1 1597 VAL 1597 1597 1597 VAL VAL A . n 
A 1 1598 GLN 1598 1598 1598 GLN GLN A . n 
A 1 1599 ARG 1599 1599 1599 ARG ARG A . n 
A 1 1600 SER 1600 1600 1600 SER SER A . n 
A 1 1601 LEU 1601 1601 1601 LEU LEU A . n 
A 1 1602 GLU 1602 1602 1602 GLU GLU A . n 
A 1 1603 ARG 1603 1603 1603 ARG ARG A . n 
A 1 1604 LEU 1604 1604 1604 LEU LEU A . n 
A 1 1605 ALA 1605 1605 1605 ALA ALA A . n 
A 1 1606 ASP 1606 1606 1606 ASP ASP A . n 
A 1 1607 LEU 1607 1607 1607 LEU LEU A . n 
A 1 1608 LEU 1608 1608 1608 LEU LEU A . n 
A 1 1609 GLY 1609 1609 1609 GLY GLY A . n 
A 1 1610 LYS 1610 1610 1610 LYS LYS A . n 
A 1 1611 ILE 1611 1611 1611 ILE ILE A . n 
A 1 1612 GLN 1612 1612 1612 GLN GLN A . n 
A 1 1613 LYS 1613 1613 1613 LYS LYS A . n 
A 1 1614 ALA 1614 1614 1614 ALA ALA A . n 
A 1 1615 LEU 1615 1615 1615 LEU LEU A . n 
A 1 1616 GLY 1616 1616 1616 GLY GLY A . n 
A 1 1617 GLU 1617 1617 1617 GLU GLU A . n 
A 1 1618 TYR 1618 1618 1618 TYR TYR A . n 
A 1 1619 LEU 1619 1619 1619 LEU LEU A . n 
A 1 1620 GLU 1620 1620 1620 GLU GLU A . n 
A 1 1621 ARG 1621 1621 1621 ARG ARG A . n 
A 1 1622 GLU 1622 1622 1622 GLU GLU A . n 
A 1 1623 ARG 1623 1623 1623 ARG ARG A . n 
A 1 1624 SER 1624 1624 1624 SER SER A . n 
A 1 1625 SER 1625 1625 1625 SER SER A . n 
A 1 1626 PHE 1626 1626 1626 PHE PHE A . n 
A 1 1627 PRO 1627 1627 1627 PRO PRO A . n 
A 1 1628 ARG 1628 1628 1628 ARG ARG A . n 
A 1 1629 PHE 1629 1629 1629 PHE PHE A . n 
A 1 1630 TYR 1630 1630 1630 TYR TYR A . n 
A 1 1631 PHE 1631 1631 1631 PHE PHE A . n 
A 1 1632 VAL 1632 1632 1632 VAL VAL A . n 
A 1 1633 GLY 1633 1633 1633 GLY GLY A . n 
A 1 1634 ASP 1634 1634 1634 ASP ASP A . n 
A 1 1635 GLU 1635 1635 1635 GLU GLU A . n 
A 1 1636 ASP 1636 1636 1636 ASP ASP A . n 
A 1 1637 LEU 1637 1637 1637 LEU LEU A . n 
A 1 1638 LEU 1638 1638 1638 LEU LEU A . n 
A 1 1639 GLU 1639 1639 1639 GLU GLU A . n 
A 1 1640 ILE 1640 1640 1640 ILE ILE A . n 
A 1 1641 ILE 1641 1641 1641 ILE ILE A . n 
A 1 1642 GLY 1642 1642 1642 GLY GLY A . n 
A 1 1643 ASN 1643 1643 1643 ASN ASN A . n 
A 1 1644 SER 1644 1644 1644 SER SER A . n 
A 1 1645 LYS 1645 1645 1645 LYS LYS A . n 
A 1 1646 ASN 1646 1646 1646 ASN ASN A . n 
A 1 1647 VAL 1647 1647 1647 VAL VAL A . n 
A 1 1648 ALA 1648 1648 1648 ALA ALA A . n 
A 1 1649 LYS 1649 1649 1649 LYS LYS A . n 
A 1 1650 LEU 1650 1650 1650 LEU LEU A . n 
A 1 1651 GLN 1651 1651 1651 GLN GLN A . n 
A 1 1652 LYS 1652 1652 1652 LYS LYS A . n 
A 1 1653 HIS 1653 1653 1653 HIS HIS A . n 
A 1 1654 PHE 1654 1654 1654 PHE PHE A . n 
A 1 1655 LYS 1655 1655 1655 LYS LYS A . n 
A 1 1656 LYS 1656 1656 1656 LYS LYS A . n 
A 1 1657 MET 1657 1657 1657 MET MET A . n 
A 1 1658 PHE 1658 1658 1658 PHE PHE A . n 
A 1 1659 ALA 1659 1659 1659 ALA ALA A . n 
A 1 1660 GLY 1660 1660 1660 GLY GLY A . n 
A 1 1661 VAL 1661 1661 1661 VAL VAL A . n 
A 1 1662 SER 1662 1662 1662 SER SER A . n 
A 1 1663 SER 1663 1663 1663 SER SER A . n 
A 1 1664 ILE 1664 1664 1664 ILE ILE A . n 
A 1 1665 ILE 1665 1665 1665 ILE ILE A . n 
A 1 1666 LEU 1666 1666 1666 LEU LEU A . n 
A 1 1667 ASN 1667 1667 1667 ASN ASN A . n 
A 1 1668 GLU 1668 1668 1668 GLU GLU A . n 
A 1 1669 ASP 1669 1669 1669 ASP ASP A . n 
A 1 1670 ASN 1670 1670 1670 ASN ASN A . n 
A 1 1671 SER 1671 1671 1671 SER SER A . n 
A 1 1672 VAL 1672 1672 1672 VAL VAL A . n 
A 1 1673 VAL 1673 1673 1673 VAL VAL A . n 
A 1 1674 LEU 1674 1674 1674 LEU LEU A . n 
A 1 1675 GLY 1675 1675 1675 GLY GLY A . n 
A 1 1676 ILE 1676 1676 1676 ILE ILE A . n 
A 1 1677 SER 1677 1677 1677 SER SER A . n 
A 1 1678 SER 1678 1678 1678 SER SER A . n 
A 1 1679 ARG 1679 1679 1679 ARG ARG A . n 
A 1 1680 GLU 1680 1680 1680 GLU GLU A . n 
A 1 1681 GLY 1681 1681 1681 GLY GLY A . n 
A 1 1682 GLU 1682 1682 1682 GLU GLU A . n 
A 1 1683 GLU 1683 1683 1683 GLU GLU A . n 
A 1 1684 VAL 1684 1684 1684 VAL VAL A . n 
A 1 1685 MET 1685 1685 1685 MET MET A . n 
A 1 1686 PHE 1686 1686 1686 PHE PHE A . n 
A 1 1687 LYS 1687 1687 1687 LYS LYS A . n 
A 1 1688 THR 1688 1688 1688 THR THR A . n 
A 1 1689 PRO 1689 1689 1689 PRO PRO A . n 
A 1 1690 VAL 1690 1690 1690 VAL VAL A . n 
A 1 1691 SER 1691 1691 1691 SER SER A . n 
A 1 1692 ILE 1692 1692 1692 ILE ILE A . n 
A 1 1693 THR 1693 1693 1693 THR THR A . n 
A 1 1694 GLU 1694 1694 1694 GLU GLU A . n 
A 1 1695 HIS 1695 1695 1695 HIS HIS A . n 
A 1 1696 PRO 1696 1696 1696 PRO PRO A . n 
A 1 1697 LYS 1697 1697 1697 LYS LYS A . n 
A 1 1698 ILE 1698 1698 1698 ILE ILE A . n 
A 1 1699 ASN 1699 1699 1699 ASN ASN A . n 
A 1 1700 GLU 1700 1700 1700 GLU GLU A . n 
A 1 1701 TRP 1701 1701 1701 TRP TRP A . n 
A 1 1702 LEU 1702 1702 1702 LEU LEU A . n 
A 1 1703 THR 1703 1703 1703 THR THR A . n 
A 1 1704 LEU 1704 1704 1704 LEU LEU A . n 
A 1 1705 VAL 1705 1705 1705 VAL VAL A . n 
A 1 1706 GLU 1706 1706 1706 GLU GLU A . n 
A 1 1707 LYS 1707 1707 1707 LYS LYS A . n 
A 1 1708 GLU 1708 1708 1708 GLU GLU A . n 
A 1 1709 MET 1709 1709 1709 MET MET A . n 
A 1 1710 ARG 1710 1710 1710 ARG ARG A . n 
A 1 1711 VAL 1711 1711 1711 VAL VAL A . n 
A 1 1712 THR 1712 1712 1712 THR THR A . n 
A 1 1713 LEU 1713 1713 1713 LEU LEU A . n 
A 1 1714 ALA 1714 1714 1714 ALA ALA A . n 
A 1 1715 LYS 1715 1715 1715 LYS LYS A . n 
A 1 1716 LEU 1716 1716 1716 LEU LEU A . n 
A 1 1717 LEU 1717 1717 1717 LEU LEU A . n 
A 1 1718 ALA 1718 1718 1718 ALA ALA A . n 
A 1 1719 GLU 1719 1719 1719 GLU GLU A . n 
A 1 1720 SER 1720 1720 1720 SER SER A . n 
A 1 1721 VAL 1721 1721 1721 VAL VAL A . n 
A 1 1722 THR 1722 1722 1722 THR THR A . n 
A 1 1723 GLU 1723 1723 1723 GLU GLU A . n 
A 1 1724 VAL 1724 1724 1724 VAL VAL A . n 
A 1 1725 GLU 1725 1725 1725 GLU GLU A . n 
A 1 1726 ILE 1726 1726 1726 ILE ILE A . n 
A 1 1727 PHE 1727 1727 1727 PHE PHE A . n 
A 1 1728 GLY 1728 1728 1728 GLY GLY A . n 
A 1 1729 LYS 1729 1729 1729 LYS LYS A . n 
A 1 1730 ALA 1730 1730 1730 ALA ALA A . n 
A 1 1731 THR 1731 1731 1731 THR THR A . n 
A 1 1732 SER 1732 1732 1732 SER SER A . n 
A 1 1733 ILE 1733 1733 1733 ILE ILE A . n 
A 1 1734 ASP 1734 1734 1734 ASP ASP A . n 
A 1 1735 PRO 1735 1735 1735 PRO PRO A . n 
A 1 1736 ASN 1736 1736 1736 ASN ASN A . n 
A 1 1737 THR 1737 1737 1737 THR THR A . n 
A 1 1738 TYR 1738 1738 1738 TYR TYR A . n 
A 1 1739 ILE 1739 1739 1739 ILE ILE A . n 
A 1 1740 THR 1740 1740 1740 THR THR A . n 
A 1 1741 TRP 1741 1741 1741 TRP TRP A . n 
A 1 1742 ILE 1742 1742 1742 ILE ILE A . n 
A 1 1743 ASP 1743 1743 1743 ASP ASP A . n 
A 1 1744 LYS 1744 1744 1744 LYS LYS A . n 
A 1 1745 TYR 1745 1745 1745 TYR TYR A . n 
A 1 1746 GLN 1746 1746 1746 GLN GLN A . n 
A 1 1747 ALA 1747 1747 1747 ALA ALA A . n 
A 1 1748 GLN 1748 1748 1748 GLN GLN A . n 
A 1 1749 LEU 1749 1749 1749 LEU LEU A . n 
A 1 1750 VAL 1750 1750 1750 VAL VAL A . n 
A 1 1751 VAL 1751 1751 1751 VAL VAL A . n 
A 1 1752 LEU 1752 1752 1752 LEU LEU A . n 
A 1 1753 SER 1753 1753 1753 SER SER A . n 
A 1 1754 ALA 1754 1754 1754 ALA ALA A . n 
A 1 1755 GLN 1755 1755 1755 GLN GLN A . n 
A 1 1756 ILE 1756 1756 1756 ILE ILE A . n 
A 1 1757 ALA 1757 1757 1757 ALA ALA A . n 
A 1 1758 TRP 1758 1758 1758 TRP TRP A . n 
A 1 1759 SER 1759 1759 1759 SER SER A . n 
A 1 1760 GLU 1760 1760 1760 GLU GLU A . n 
A 1 1761 ASN 1761 1761 1761 ASN ASN A . n 
A 1 1762 VAL 1762 1762 1762 VAL VAL A . n 
A 1 1763 GLU 1763 1763 1763 GLU GLU A . n 
A 1 1764 THR 1764 1764 1764 THR THR A . n 
A 1 1765 ALA 1765 1765 1765 ALA ALA A . n 
A 1 1766 LEU 1766 1766 1766 LEU LEU A . n 
A 1 1767 SER 1767 1767 1767 SER SER A . n 
A 1 1768 SER 1768 1768 1768 SER SER A . n 
A 1 1769 MET 1769 1769 1769 MET MET A . n 
A 1 1770 GLY 1770 1770 1770 GLY GLY A . n 
A 1 1771 GLY 1771 1771 1771 GLY GLY A . n 
A 1 1772 GLY 1772 1772 1772 GLY GLY A . n 
A 1 1773 GLY 1773 1773 1773 GLY GLY A . n 
A 1 1774 ASP 1774 1774 1774 ASP ASP A . n 
A 1 1775 ALA 1775 1775 1775 ALA ALA A . n 
A 1 1776 ALA 1776 1776 1776 ALA ALA A . n 
A 1 1777 PRO 1777 1777 1777 PRO PRO A . n 
A 1 1778 LEU 1778 1778 1778 LEU LEU A . n 
A 1 1779 HIS 1779 1779 1779 HIS HIS A . n 
A 1 1780 SER 1780 1780 1780 SER SER A . n 
A 1 1781 VAL 1781 1781 1781 VAL VAL A . n 
A 1 1782 LEU 1782 1782 1782 LEU LEU A . n 
A 1 1783 SER 1783 1783 1783 SER SER A . n 
A 1 1784 ASN 1784 1784 1784 ASN ASN A . n 
A 1 1785 VAL 1785 1785 1785 VAL VAL A . n 
A 1 1786 GLU 1786 1786 1786 GLU GLU A . n 
A 1 1787 VAL 1787 1787 1787 VAL VAL A . n 
A 1 1788 THR 1788 1788 1788 THR THR A . n 
A 1 1789 LEU 1789 1789 1789 LEU LEU A . n 
A 1 1790 ASN 1790 1790 1790 ASN ASN A . n 
A 1 1791 VAL 1791 1791 1791 VAL VAL A . n 
A 1 1792 LEU 1792 1792 1792 LEU LEU A . n 
A 1 1793 ALA 1793 1793 1793 ALA ALA A . n 
A 1 1794 ASP 1794 1794 1794 ASP ASP A . n 
A 1 1795 SER 1795 1795 1795 SER SER A . n 
A 1 1796 VAL 1796 1796 1796 VAL VAL A . n 
A 1 1797 LEU 1797 1797 1797 LEU LEU A . n 
A 1 1798 MET 1798 1798 1798 MET MET A . n 
A 1 1799 GLU 1799 1799 1799 GLU GLU A . n 
A 1 1800 GLN 1800 1800 1800 GLN GLN A . n 
A 1 1801 PRO 1801 1801 1801 PRO PRO A . n 
A 1 1802 PRO 1802 1802 1802 PRO PRO A . n 
A 1 1803 LEU 1803 1803 1803 LEU LEU A . n 
A 1 1804 ARG 1804 1804 1804 ARG ARG A . n 
A 1 1805 ARG 1805 1805 1805 ARG ARG A . n 
A 1 1806 ARG 1806 1806 1806 ARG ARG A . n 
A 1 1807 LYS 1807 1807 1807 LYS LYS A . n 
A 1 1808 LEU 1808 1808 1808 LEU LEU A . n 
A 1 1809 GLU 1809 1809 1809 GLU GLU A . n 
A 1 1810 HIS 1810 1810 1810 HIS HIS A . n 
A 1 1811 LEU 1811 1811 1811 LEU LEU A . n 
A 1 1812 ILE 1812 1812 1812 ILE ILE A . n 
A 1 1813 THR 1813 1813 1813 THR THR A . n 
A 1 1814 GLU 1814 1814 1814 GLU GLU A . n 
A 1 1815 LEU 1815 1815 1815 LEU LEU A . n 
A 1 1816 VAL 1816 1816 1816 VAL VAL A . n 
A 1 1817 HIS 1817 1817 1817 HIS HIS A . n 
A 1 1818 GLN 1818 1818 1818 GLN GLN A . n 
A 1 1819 ARG 1819 1819 1819 ARG ARG A . n 
A 1 1820 ASP 1820 1820 1820 ASP ASP A . n 
A 1 1821 VAL 1821 1821 1821 VAL VAL A . n 
A 1 1822 THR 1822 1822 1822 THR THR A . n 
A 1 1823 ARG 1823 1823 1823 ARG ARG A . n 
A 1 1824 SER 1824 1824 1824 SER SER A . n 
A 1 1825 LEU 1825 1825 1825 LEU LEU A . n 
A 1 1826 ILE 1826 1826 1826 ILE ILE A . n 
A 1 1827 LYS 1827 1827 1827 LYS LYS A . n 
A 1 1828 SER 1828 1828 1828 SER SER A . n 
A 1 1829 LYS 1829 1829 1829 LYS LYS A . n 
A 1 1830 ILE 1830 1830 1830 ILE ILE A . n 
A 1 1831 ASP 1831 1831 1831 ASP ASP A . n 
A 1 1832 ASN 1832 1832 1832 ASN ASN A . n 
A 1 1833 ALA 1833 1833 1833 ALA ALA A . n 
A 1 1834 LYS 1834 1834 1834 LYS LYS A . n 
A 1 1835 SER 1835 1835 1835 SER SER A . n 
A 1 1836 PHE 1836 1836 1836 PHE PHE A . n 
A 1 1837 GLU 1837 1837 1837 GLU GLU A . n 
A 1 1838 TRP 1838 1838 1838 TRP TRP A . n 
A 1 1839 LEU 1839 1839 1839 LEU LEU A . n 
A 1 1840 SER 1840 1840 1840 SER SER A . n 
A 1 1841 GLN 1841 1841 1841 GLN GLN A . n 
A 1 1842 MET 1842 1842 1842 MET MET A . n 
A 1 1843 ARG 1843 1843 1843 ARG ARG A . n 
A 1 1844 PHE 1844 1844 1844 PHE PHE A . n 
A 1 1845 TYR 1845 1845 1845 TYR TYR A . n 
A 1 1846 PHE 1846 1846 1846 PHE PHE A . n 
A 1 1847 ASP 1847 1847 1847 ASP ASP A . n 
A 1 1848 PRO 1848 1848 1848 PRO PRO A . n 
A 1 1849 LYS 1849 1849 1849 LYS LYS A . n 
A 1 1850 GLN 1850 1850 1850 GLN GLN A . n 
A 1 1851 THR 1851 1851 1851 THR THR A . n 
A 1 1852 ASP 1852 1852 1852 ASP ASP A . n 
A 1 1853 VAL 1853 1853 1853 VAL VAL A . n 
A 1 1854 LEU 1854 1854 1854 LEU LEU A . n 
A 1 1855 GLN 1855 1855 1855 GLN GLN A . n 
A 1 1856 GLN 1856 1856 1856 GLN GLN A . n 
A 1 1857 LEU 1857 1857 1857 LEU LEU A . n 
A 1 1858 SER 1858 1858 1858 SER SER A . n 
A 1 1859 ILE 1859 1859 1859 ILE ILE A . n 
A 1 1860 GLN 1860 1860 1860 GLN GLN A . n 
A 1 1861 MET 1861 1861 1861 MET MET A . n 
A 1 1862 ALA 1862 1862 1862 ALA ALA A . n 
A 1 1863 ASN 1863 1863 1863 ASN ASN A . n 
A 1 1864 ALA 1864 1864 1864 ALA ALA A . n 
A 1 1865 LYS 1865 1865 1865 LYS LYS A . n 
A 1 1866 PHE 1866 1866 1866 PHE PHE A . n 
A 1 1867 ASN 1867 1867 1867 ASN ASN A . n 
A 1 1868 TYR 1868 1868 1868 TYR TYR A . n 
A 1 1869 GLY 1869 1869 1869 GLY GLY A . n 
A 1 1870 PHE 1870 1870 1870 PHE PHE A . n 
A 1 1871 GLU 1871 1871 1871 GLU GLU A . n 
A 1 1872 TYR 1872 1872 1872 TYR TYR A . n 
A 1 1873 LEU 1873 1873 1873 LEU LEU A . n 
A 1 1874 GLY 1874 1874 1874 GLY GLY A . n 
A 1 1875 VAL 1875 1875 1875 VAL VAL A . n 
A 1 1876 GLN 1876 1876 1876 GLN GLN A . n 
A 1 1877 ASP 1877 1877 1877 ASP ASP A . n 
A 1 1878 LYS 1878 1878 1878 LYS LYS A . n 
A 1 1879 LEU 1879 1879 1879 LEU LEU A . n 
A 1 1880 VAL 1880 1880 1880 VAL VAL A . n 
A 1 1881 GLN 1881 1881 1881 GLN GLN A . n 
A 1 1882 THR 1882 1882 1882 THR THR A . n 
A 1 1883 PRO 1883 1883 1883 PRO PRO A . n 
A 1 1884 LEU 1884 1884 1884 LEU LEU A . n 
A 1 1885 THR 1885 1885 1885 THR THR A . n 
A 1 1886 ASP 1886 1886 1886 ASP ASP A . n 
A 1 1887 ARG 1887 1887 1887 ARG ARG A . n 
A 1 1888 CYS 1888 1888 1888 CYS CYS A . n 
A 1 1889 TYR 1889 1889 1889 TYR TYR A . n 
A 1 1890 LEU 1890 1890 1890 LEU LEU A . n 
A 1 1891 THR 1891 1891 1891 THR THR A . n 
A 1 1892 MET 1892 1892 1892 MET MET A . n 
A 1 1893 THR 1893 1893 1893 THR THR A . n 
A 1 1894 GLN 1894 1894 1894 GLN GLN A . n 
A 1 1895 ALA 1895 1895 1895 ALA ALA A . n 
A 1 1896 LEU 1896 1896 1896 LEU LEU A . n 
A 1 1897 GLU 1897 1897 1897 GLU GLU A . n 
A 1 1898 ALA 1898 1898 1898 ALA ALA A . n 
A 1 1899 ARG 1899 1899 1899 ARG ARG A . n 
A 1 1900 LEU 1900 1900 1900 LEU LEU A . n 
A 1 1901 GLY 1901 1901 1901 GLY GLY A . n 
A 1 1902 GLY 1902 1902 1902 GLY GLY A . n 
A 1 1903 SER 1903 1903 1903 SER SER A . n 
A 1 1904 PRO 1904 1904 1904 PRO PRO A . n 
A 1 1905 PHE 1905 1905 1905 PHE PHE A . n 
A 1 1906 GLY 1906 1906 1906 GLY GLY A . n 
A 1 1907 PRO 1907 1907 1907 PRO PRO A . n 
A 1 1908 ALA 1908 1908 1908 ALA ALA A . n 
A 1 1909 GLY 1909 1909 1909 GLY GLY A . n 
A 1 1910 THR 1910 1910 1910 THR THR A . n 
A 1 1911 GLY 1911 1911 1911 GLY GLY A . n 
A 1 1912 LYS 1912 1912 1912 LYS LYS A . n 
A 1 1913 THR 1913 1913 1913 THR THR A . n 
A 1 1914 GLU 1914 1914 1914 GLU GLU A . n 
A 1 1915 SER 1915 1915 1915 SER SER A . n 
A 1 1916 VAL 1916 1916 1916 VAL VAL A . n 
A 1 1917 LYS 1917 1917 1917 LYS LYS A . n 
A 1 1918 ALA 1918 1918 1918 ALA ALA A . n 
A 1 1919 LEU 1919 1919 1919 LEU LEU A . n 
A 1 1920 GLY 1920 1920 1920 GLY GLY A . n 
A 1 1921 HIS 1921 1921 1921 HIS HIS A . n 
A 1 1922 GLN 1922 1922 1922 GLN GLN A . n 
A 1 1923 LEU 1923 1923 1923 LEU LEU A . n 
A 1 1924 GLY 1924 1924 1924 GLY GLY A . n 
A 1 1925 ARG 1925 1925 1925 ARG ARG A . n 
A 1 1926 PHE 1926 1926 1926 PHE PHE A . n 
A 1 1927 VAL 1927 1927 1927 VAL VAL A . n 
A 1 1928 LEU 1928 1928 1928 LEU LEU A . n 
A 1 1929 VAL 1929 1929 1929 VAL VAL A . n 
A 1 1930 PHE 1930 1930 1930 PHE PHE A . n 
A 1 1931 ASN 1931 1931 1931 ASN ASN A . n 
A 1 1932 CYS 1932 1932 1932 CYS CYS A . n 
A 1 1933 ASP 1933 1933 1933 ASP ASP A . n 
A 1 1934 GLU 1934 1934 1934 GLU GLU A . n 
A 1 1935 THR 1935 1935 1935 THR THR A . n 
A 1 1936 PHE 1936 1936 1936 PHE PHE A . n 
A 1 1937 ASP 1937 1937 1937 ASP ASP A . n 
A 1 1938 PHE 1938 1938 1938 PHE PHE A . n 
A 1 1939 GLN 1939 1939 1939 GLN GLN A . n 
A 1 1940 ALA 1940 1940 1940 ALA ALA A . n 
A 1 1941 MET 1941 1941 1941 MET MET A . n 
A 1 1942 GLY 1942 1942 1942 GLY GLY A . n 
A 1 1943 ARG 1943 1943 1943 ARG ARG A . n 
A 1 1944 ILE 1944 1944 1944 ILE ILE A . n 
A 1 1945 PHE 1945 1945 1945 PHE PHE A . n 
A 1 1946 VAL 1946 1946 1946 VAL VAL A . n 
A 1 1947 GLY 1947 1947 1947 GLY GLY A . n 
A 1 1948 LEU 1948 1948 1948 LEU LEU A . n 
A 1 1949 CYS 1949 1949 1949 CYS CYS A . n 
A 1 1950 GLN 1950 1950 1950 GLN GLN A . n 
A 1 1951 VAL 1951 1951 1951 VAL VAL A . n 
A 1 1952 GLY 1952 1952 1952 GLY GLY A . n 
A 1 1953 ALA 1953 1953 1953 ALA ALA A . n 
A 1 1954 TRP 1954 1954 1954 TRP TRP A . n 
A 1 1955 GLY 1955 1955 1955 GLY GLY A . n 
A 1 1956 CYS 1956 1956 1956 CYS CYS A . n 
A 1 1957 PHE 1957 1957 1957 PHE PHE A . n 
A 1 1958 ASP 1958 1958 1958 ASP ASP A . n 
A 1 1959 GLU 1959 1959 1959 GLU GLU A . n 
A 1 1960 PHE 1960 1960 1960 PHE PHE A . n 
A 1 1961 ASN 1961 1961 1961 ASN ASN A . n 
A 1 1962 ARG 1962 1962 1962 ARG ARG A . n 
A 1 1963 LEU 1963 1963 1963 LEU LEU A . n 
A 1 1964 GLU 1964 1964 1964 GLU GLU A . n 
A 1 1965 GLU 1965 1965 1965 GLU GLU A . n 
A 1 1966 ARG 1966 1966 1966 ARG ARG A . n 
A 1 1967 MET 1967 1967 1967 MET MET A . n 
A 1 1968 LEU 1968 1968 1968 LEU LEU A . n 
A 1 1969 SER 1969 1969 1969 SER SER A . n 
A 1 1970 ALA 1970 1970 1970 ALA ALA A . n 
A 1 1971 VAL 1971 1971 1971 VAL VAL A . n 
A 1 1972 SER 1972 1972 1972 SER SER A . n 
A 1 1973 GLN 1973 1973 1973 GLN GLN A . n 
A 1 1974 GLN 1974 1974 1974 GLN GLN A . n 
A 1 1975 VAL 1975 1975 1975 VAL VAL A . n 
A 1 1976 GLN 1976 1976 1976 GLN GLN A . n 
A 1 1977 CYS 1977 1977 1977 CYS CYS A . n 
A 1 1978 ILE 1978 1978 1978 ILE ILE A . n 
A 1 1979 GLN 1979 1979 1979 GLN GLN A . n 
A 1 1980 GLU 1980 1980 1980 GLU GLU A . n 
A 1 1981 ALA 1981 1981 1981 ALA ALA A . n 
A 1 1982 LEU 1982 1982 1982 LEU LEU A . n 
A 1 1983 ARG 1983 1983 1983 ARG ARG A . n 
A 1 1984 GLU 1984 1984 1984 GLU GLU A . n 
A 1 1985 HIS 1985 1985 1985 HIS HIS A . n 
A 1 1986 SER 1986 1986 1986 SER SER A . n 
A 1 1987 ASN 1987 1987 1987 ASN ASN A . n 
A 1 1988 PRO 1988 1988 1988 PRO PRO A . n 
A 1 1989 ASN 1989 1989 1989 ASN ASN A . n 
A 1 1990 TYR 1990 1990 1990 TYR TYR A . n 
A 1 1991 ASP 1991 1991 1991 ASP ASP A . n 
A 1 1992 LYS 1992 1992 1992 LYS LYS A . n 
A 1 1993 THR 1993 1993 1993 THR THR A . n 
A 1 1994 SER 1994 1994 1994 SER SER A . n 
A 1 1995 ALA 1995 1995 1995 ALA ALA A . n 
A 1 1996 PRO 1996 1996 1996 PRO PRO A . n 
A 1 1997 ILE 1997 1997 1997 ILE ILE A . n 
A 1 1998 THR 1998 1998 1998 THR THR A . n 
A 1 1999 CYS 1999 1999 1999 CYS CYS A . n 
A 1 2000 GLU 2000 2000 2000 GLU GLU A . n 
A 1 2001 LEU 2001 2001 2001 LEU LEU A . n 
A 1 2002 LEU 2002 2002 2002 LEU LEU A . n 
A 1 2003 ASN 2003 2003 2003 ASN ASN A . n 
A 1 2004 LYS 2004 2004 2004 LYS LYS A . n 
A 1 2005 GLN 2005 2005 2005 GLN GLN A . n 
A 1 2006 VAL 2006 2006 2006 VAL VAL A . n 
A 1 2007 LYS 2007 2007 2007 LYS LYS A . n 
A 1 2008 VAL 2008 2008 2008 VAL VAL A . n 
A 1 2009 SER 2009 2009 2009 SER SER A . n 
A 1 2010 PRO 2010 2010 2010 PRO PRO A . n 
A 1 2011 ASP 2011 2011 2011 ASP ASP A . n 
A 1 2012 MET 2012 2012 2012 MET MET A . n 
A 1 2013 ALA 2013 2013 2013 ALA ALA A . n 
A 1 2014 ILE 2014 2014 2014 ILE ILE A . n 
A 1 2015 PHE 2015 2015 2015 PHE PHE A . n 
A 1 2016 ILE 2016 2016 2016 ILE ILE A . n 
A 1 2017 THR 2017 2017 2017 THR THR A . n 
A 1 2018 MET 2018 2018 2018 MET MET A . n 
A 1 2019 ASN 2019 2019 2019 ASN ASN A . n 
A 1 2020 PRO 2020 2020 2020 PRO PRO A . n 
A 1 2021 GLY 2021 2021 2021 GLY GLY A . n 
A 1 2022 TYR 2022 2022 ?    ?   ?   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 2026 SER SER A . n 
A 1 2027 ASN 2027 2027 2027 ASN ASN A . n 
A 1 2028 LEU 2028 2028 2028 LEU LEU A . n 
A 1 2029 PRO 2029 2029 2029 PRO PRO A . n 
A 1 2030 ASP 2030 2030 2030 ASP ASP A . n 
A 1 2031 ASN 2031 2031 2031 ASN ASN A . n 
A 1 2032 LEU 2032 2032 2032 LEU LEU A . n 
A 1 2033 LYS 2033 2033 2033 LYS LYS A . n 
A 1 2034 LYS 2034 2034 2034 LYS LYS A . n 
A 1 2035 LEU 2035 2035 2035 LEU LEU A . n 
A 1 2036 PHE 2036 2036 2036 PHE PHE A . n 
A 1 2037 ARG 2037 2037 2037 ARG ARG A . n 
A 1 2038 SER 2038 2038 2038 SER SER A . n 
A 1 2039 LEU 2039 2039 2039 LEU LEU A . n 
A 1 2040 ALA 2040 2040 2040 ALA ALA A . n 
A 1 2041 MET 2041 2041 2041 MET MET A . n 
A 1 2042 THR 2042 2042 2042 THR THR A . n 
A 1 2043 LYS 2043 2043 2043 LYS LYS A . n 
A 1 2044 PRO 2044 2044 2044 PRO PRO A . n 
A 1 2045 ASP 2045 2045 2045 ASP ASP A . n 
A 1 2046 ARG 2046 2046 2046 ARG ARG A . n 
A 1 2047 GLN 2047 2047 2047 GLN GLN A . n 
A 1 2048 LEU 2048 2048 2048 LEU LEU A . n 
A 1 2049 ILE 2049 2049 2049 ILE ILE A . n 
A 1 2050 ALA 2050 2050 2050 ALA ALA A . n 
A 1 2051 GLN 2051 2051 2051 GLN GLN A . n 
A 1 2052 VAL 2052 2052 2052 VAL VAL A . n 
A 1 2053 MET 2053 2053 2053 MET MET A . n 
A 1 2054 LEU 2054 2054 2054 LEU LEU A . n 
A 1 2055 TYR 2055 2055 2055 TYR TYR A . n 
A 1 2056 SER 2056 2056 2056 SER SER A . n 
A 1 2057 GLN 2057 2057 2057 GLN GLN A . n 
A 1 2058 GLY 2058 2058 2058 GLY GLY A . n 
A 1 2059 PHE 2059 2059 2059 PHE PHE A . n 
A 1 2060 ARG 2060 2060 2060 ARG ARG A . n 
A 1 2061 THR 2061 2061 2061 THR THR A . n 
A 1 2062 ALA 2062 2062 2062 ALA ALA A . n 
A 1 2063 GLU 2063 2063 2063 GLU GLU A . n 
A 1 2064 VAL 2064 2064 2064 VAL VAL A . n 
A 1 2065 LEU 2065 2065 2065 LEU LEU A . n 
A 1 2066 ALA 2066 2066 2066 ALA ALA A . n 
A 1 2067 ASN 2067 2067 2067 ASN ASN A . n 
A 1 2068 LYS 2068 2068 2068 LYS LYS A . n 
A 1 2069 ILE 2069 2069 2069 ILE ILE A . n 
A 1 2070 VAL 2070 2070 2070 VAL VAL A . n 
A 1 2071 PRO 2071 2071 2071 PRO PRO A . n 
A 1 2072 PHE 2072 2072 2072 PHE PHE A . n 
A 1 2073 PHE 2073 2073 2073 PHE PHE A . n 
A 1 2074 LYS 2074 2074 2074 LYS LYS A . n 
A 1 2075 LEU 2075 2075 2075 LEU LEU A . n 
A 1 2076 CYS 2076 2076 2076 CYS CYS A . n 
A 1 2077 ASP 2077 2077 2077 ASP ASP A . n 
A 1 2078 GLU 2078 2078 2078 GLU GLU A . n 
A 1 2079 GLN 2079 2079 2079 GLN GLN A . n 
A 1 2080 LEU 2080 2080 2080 LEU LEU A . n 
A 1 2081 SER 2081 2081 2081 SER SER A . n 
A 1 2082 SER 2082 2082 2082 SER SER A . n 
A 1 2083 GLN 2083 2083 2083 GLN GLN A . n 
A 1 2084 SER 2084 2084 2084 SER SER A . n 
A 1 2085 HIS 2085 2085 2085 HIS HIS A . n 
A 1 2086 TYR 2086 2086 2086 TYR TYR A . n 
A 1 2087 ASP 2087 2087 2087 ASP ASP A . n 
A 1 2088 PHE 2088 2088 2088 PHE PHE A . n 
A 1 2089 GLY 2089 2089 2089 GLY GLY A . n 
A 1 2090 LEU 2090 2090 2090 LEU LEU A . n 
A 1 2091 ARG 2091 2091 2091 ARG ARG A . n 
A 1 2092 ALA 2092 2092 2092 ALA ALA A . n 
A 1 2093 LEU 2093 2093 2093 LEU LEU A . n 
A 1 2094 LYS 2094 2094 2094 LYS LYS A . n 
A 1 2095 SER 2095 2095 2095 SER SER A . n 
A 1 2096 VAL 2096 2096 2096 VAL VAL A . n 
A 1 2097 LEU 2097 2097 2097 LEU LEU A . n 
A 1 2098 VAL 2098 2098 2098 VAL VAL A . n 
A 1 2099 SER 2099 2099 2099 SER SER A . n 
A 1 2100 ALA 2100 2100 2100 ALA ALA A . n 
A 1 2101 GLY 2101 2101 2101 GLY GLY A . n 
A 1 2102 ASN 2102 2102 2102 ASN ASN A . n 
A 1 2103 VAL 2103 2103 2103 VAL VAL A . n 
A 1 2104 LYS 2104 2104 2104 LYS LYS A . n 
A 1 2105 ARG 2105 2105 2105 ARG ARG A . n 
A 1 2106 GLU 2106 2106 2106 GLU GLU A . n 
A 1 2107 ARG 2107 2107 2107 ARG ARG A . n 
A 1 2108 ILE 2108 2108 2108 ILE ILE A . n 
A 1 2109 GLN 2109 2109 2109 GLN GLN A . n 
A 1 2110 LYS 2110 2110 2110 LYS LYS A . n 
A 1 2111 ILE 2111 2111 2111 ILE ILE A . n 
A 1 2112 LYS 2112 2112 2112 LYS LYS A . n 
A 1 2113 ARG 2113 2113 2113 ARG ARG A . n 
A 1 2114 GLU 2114 2114 2114 GLU GLU A . n 
A 1 2115 LYS 2115 2115 2115 LYS LYS A . n 
A 1 2116 GLU 2116 2116 2116 GLU GLU A . n 
A 1 2117 GLU 2117 2117 2117 GLU GLU A . n 
A 1 2118 ARG 2118 2118 2118 ARG ARG A . n 
A 1 2119 GLY 2119 2119 2119 GLY GLY A . n 
A 1 2120 GLU 2120 2120 2120 GLU GLU A . n 
A 1 2121 ALA 2121 2121 2121 ALA ALA A . n 
A 1 2122 VAL 2122 2122 2122 VAL VAL A . n 
A 1 2123 ASP 2123 2123 2123 ASP ASP A . n 
A 1 2124 GLU 2124 2124 2124 GLU GLU A . n 
A 1 2125 GLY 2125 2125 2125 GLY GLY A . n 
A 1 2126 GLU 2126 2126 2126 GLU GLU A . n 
A 1 2127 ILE 2127 2127 2127 ILE ILE A . n 
A 1 2128 ALA 2128 2128 2128 ALA ALA A . n 
A 1 2129 GLU 2129 2129 2129 GLU GLU A . n 
A 1 2130 ASN 2130 2130 2130 ASN ASN A . n 
A 1 2131 LEU 2131 2131 2131 LEU LEU A . n 
A 1 2132 PRO 2132 2132 2132 PRO PRO A . n 
A 1 2133 GLU 2133 2133 2133 GLU GLU A . n 
A 1 2134 GLN 2134 2134 2134 GLN GLN A . n 
A 1 2135 GLU 2135 2135 2135 GLU GLU A . n 
A 1 2136 ILE 2136 2136 2136 ILE ILE A . n 
A 1 2137 LEU 2137 2137 2137 LEU LEU A . n 
A 1 2138 ILE 2138 2138 2138 ILE ILE A . n 
A 1 2139 GLN 2139 2139 2139 GLN GLN A . n 
A 1 2140 SER 2140 2140 2140 SER SER A . n 
A 1 2141 VAL 2141 2141 2141 VAL VAL A . n 
A 1 2142 CYS 2142 2142 2142 CYS CYS A . n 
A 1 2143 GLU 2143 2143 2143 GLU GLU A . n 
A 1 2144 THR 2144 2144 2144 THR THR A . n 
A 1 2145 MET 2145 2145 2145 MET MET A . n 
A 1 2146 VAL 2146 2146 2146 VAL VAL A . n 
A 1 2147 PRO 2147 2147 2147 PRO PRO A . n 
A 1 2148 LYS 2148 2148 2148 LYS LYS A . n 
A 1 2149 LEU 2149 2149 2149 LEU LEU A . n 
A 1 2150 VAL 2150 2150 2150 VAL VAL A . n 
A 1 2151 ALA 2151 2151 2151 ALA ALA A . n 
A 1 2152 GLU 2152 2152 2152 GLU GLU A . n 
A 1 2153 ASP 2153 2153 2153 ASP ASP A . n 
A 1 2154 ILE 2154 2154 2154 ILE ILE A . n 
A 1 2155 PRO 2155 2155 2155 PRO PRO A . n 
A 1 2156 LEU 2156 2156 2156 LEU LEU A . n 
A 1 2157 LEU 2157 2157 2157 LEU LEU A . n 
A 1 2158 PHE 2158 2158 2158 PHE PHE A . n 
A 1 2159 SER 2159 2159 2159 SER SER A . n 
A 1 2160 LEU 2160 2160 2160 LEU LEU A . n 
A 1 2161 LEU 2161 2161 2161 LEU LEU A . n 
A 1 2162 SER 2162 2162 2162 SER SER A . n 
A 1 2163 ASP 2163 2163 2163 ASP ASP A . n 
A 1 2164 VAL 2164 2164 2164 VAL VAL A . n 
A 1 2165 PHE 2165 2165 2165 PHE PHE A . n 
A 1 2166 PRO 2166 2166 2166 PRO PRO A . n 
A 1 2167 GLY 2167 2167 2167 GLY GLY A . n 
A 1 2168 VAL 2168 2168 2168 VAL VAL A . n 
A 1 2169 GLN 2169 2169 2169 GLN GLN A . n 
A 1 2170 TYR 2170 2170 2170 TYR TYR A . n 
A 1 2171 HIS 2171 2171 2171 HIS HIS A . n 
A 1 2172 ARG 2172 2172 2172 ARG ARG A . n 
A 1 2173 GLY 2173 2173 2173 GLY GLY A . n 
A 1 2174 GLU 2174 2174 2174 GLU GLU A . n 
A 1 2175 MET 2175 2175 2175 MET MET A . n 
A 1 2176 THR 2176 2176 2176 THR THR A . n 
A 1 2177 ALA 2177 2177 2177 ALA ALA A . n 
A 1 2178 LEU 2178 2178 2178 LEU LEU A . n 
A 1 2179 ARG 2179 2179 2179 ARG ARG A . n 
A 1 2180 GLU 2180 2180 2180 GLU GLU A . n 
A 1 2181 GLU 2181 2181 2181 GLU GLU A . n 
A 1 2182 LEU 2182 2182 2182 LEU LEU A . n 
A 1 2183 LYS 2183 2183 2183 LYS LYS A . n 
A 1 2184 LYS 2184 2184 2184 LYS LYS A . n 
A 1 2185 VAL 2185 2185 2185 VAL VAL A . n 
A 1 2186 CYS 2186 2186 2186 CYS CYS A . n 
A 1 2187 GLN 2187 2187 2187 GLN GLN A . n 
A 1 2188 GLU 2188 2188 2188 GLU GLU A . n 
A 1 2189 MET 2189 2189 2189 MET MET A . n 
A 1 2190 TYR 2190 2190 2190 TYR TYR A . n 
A 1 2191 LEU 2191 2191 2191 LEU LEU A . n 
A 1 2192 THR 2192 2192 2192 THR THR A . n 
A 1 2193 TYR 2193 2193 2193 TYR TYR A . n 
A 1 2194 GLY 2194 2194 2194 GLY GLY A . n 
A 1 2195 ASP 2195 2195 2195 ASP ASP A . n 
A 1 2196 GLY 2196 2196 2196 GLY GLY A . n 
A 1 2197 GLU 2197 2197 2197 GLU GLU A . n 
A 1 2198 GLU 2198 2198 2198 GLU GLU A . n 
A 1 2199 VAL 2199 2199 2199 VAL VAL A . n 
A 1 2200 GLY 2200 2200 2200 GLY GLY A . n 
A 1 2201 GLY 2201 2201 2201 GLY GLY A . n 
A 1 2202 MET 2202 2202 2202 MET MET A . n 
A 1 2203 TRP 2203 2203 2203 TRP TRP A . n 
A 1 2204 VAL 2204 2204 2204 VAL VAL A . n 
A 1 2205 GLU 2205 2205 2205 GLU GLU A . n 
A 1 2206 LYS 2206 2206 2206 LYS LYS A . n 
A 1 2207 VAL 2207 2207 2207 VAL VAL A . n 
A 1 2208 LEU 2208 2208 2208 LEU LEU A . n 
A 1 2209 GLN 2209 2209 2209 GLN GLN A . n 
A 1 2210 LEU 2210 2210 2210 LEU LEU A . n 
A 1 2211 TYR 2211 2211 2211 TYR TYR A . n 
A 1 2212 GLN 2212 2212 2212 GLN GLN A . n 
A 1 2213 ILE 2213 2213 2213 ILE ILE A . n 
A 1 2214 THR 2214 2214 2214 THR THR A . n 
A 1 2215 GLN 2215 2215 2215 GLN GLN A . n 
A 1 2216 ILE 2216 2216 2216 ILE ILE A . n 
A 1 2217 ASN 2217 2217 2217 ASN ASN A . n 
A 1 2218 HIS 2218 2218 2218 HIS HIS A . n 
A 1 2219 GLY 2219 2219 2219 GLY GLY A . n 
A 1 2220 LEU 2220 2220 2220 LEU LEU A . n 
A 1 2221 MET 2221 2221 2221 MET MET A . n 
A 1 2222 MET 2222 2222 2222 MET MET A . n 
A 1 2223 VAL 2223 2223 2223 VAL VAL A . n 
A 1 2224 GLY 2224 2224 2224 GLY GLY A . n 
A 1 2225 PRO 2225 2225 2225 PRO PRO A . n 
A 1 2226 SER 2226 2226 2226 SER SER A . n 
A 1 2227 GLY 2227 2227 2227 GLY GLY A . n 
A 1 2228 SER 2228 2228 2228 SER SER A . n 
A 1 2229 GLY 2229 2229 2229 GLY GLY A . n 
A 1 2230 LYS 2230 2230 2230 LYS LYS A . n 
A 1 2231 SER 2231 2231 2231 SER SER A . n 
A 1 2232 MET 2232 2232 2232 MET MET A . n 
A 1 2233 ALA 2233 2233 2233 ALA ALA A . n 
A 1 2234 TRP 2234 2234 2234 TRP TRP A . n 
A 1 2235 ARG 2235 2235 2235 ARG ARG A . n 
A 1 2236 VAL 2236 2236 2236 VAL VAL A . n 
A 1 2237 LEU 2237 2237 2237 LEU LEU A . n 
A 1 2238 LEU 2238 2238 2238 LEU LEU A . n 
A 1 2239 LYS 2239 2239 2239 LYS LYS A . n 
A 1 2240 ALA 2240 2240 2240 ALA ALA A . n 
A 1 2241 LEU 2241 2241 2241 LEU LEU A . n 
A 1 2242 GLU 2242 2242 2242 GLU GLU A . n 
A 1 2243 ARG 2243 2243 2243 ARG ARG A . n 
A 1 2244 LEU 2244 2244 2244 LEU LEU A . n 
A 1 2245 GLU 2245 2245 2245 GLU GLU A . n 
A 1 2246 GLY 2246 2246 2246 GLY GLY A . n 
A 1 2247 VAL 2247 2247 2247 VAL VAL A . n 
A 1 2248 GLU 2248 2248 2248 GLU GLU A . n 
A 1 2249 GLY 2249 2249 2249 GLY GLY A . n 
A 1 2250 VAL 2250 2250 2250 VAL VAL A . n 
A 1 2251 ALA 2251 2251 2251 ALA ALA A . n 
A 1 2252 HIS 2252 2252 2252 HIS HIS A . n 
A 1 2253 ILE 2253 2253 2253 ILE ILE A . n 
A 1 2254 ILE 2254 2254 2254 ILE ILE A . n 
A 1 2255 ASP 2255 2255 2255 ASP ASP A . n 
A 1 2256 PRO 2256 2256 2256 PRO PRO A . n 
A 1 2257 LYS 2257 2257 2257 LYS LYS A . n 
A 1 2258 ALA 2258 2258 2258 ALA ALA A . n 
A 1 2259 ILE 2259 2259 2259 ILE ILE A . n 
A 1 2260 SER 2260 2260 2260 SER SER A . n 
A 1 2261 LYS 2261 2261 2261 LYS LYS A . n 
A 1 2262 ASP 2262 2262 2262 ASP ASP A . n 
A 1 2263 HIS 2263 2263 2263 HIS HIS A . n 
A 1 2264 LEU 2264 2264 2264 LEU LEU A . n 
A 1 2265 TYR 2265 2265 2265 TYR TYR A . n 
A 1 2266 GLY 2266 2266 2266 GLY GLY A . n 
A 1 2267 THR 2267 2267 2267 THR THR A . n 
A 1 2268 LEU 2268 2268 2268 LEU LEU A . n 
A 1 2269 ASP 2269 2269 2269 ASP ASP A . n 
A 1 2270 PRO 2270 2270 2270 PRO PRO A . n 
A 1 2271 ASN 2271 2271 2271 ASN ASN A . n 
A 1 2272 THR 2272 2272 2272 THR THR A . n 
A 1 2273 ARG 2273 2273 2273 ARG ARG A . n 
A 1 2274 GLU 2274 2274 2274 GLU GLU A . n 
A 1 2275 TRP 2275 2275 2275 TRP TRP A . n 
A 1 2276 THR 2276 2276 2276 THR THR A . n 
A 1 2277 ASP 2277 2277 2277 ASP ASP A . n 
A 1 2278 GLY 2278 2278 2278 GLY GLY A . n 
A 1 2279 LEU 2279 2279 2279 LEU LEU A . n 
A 1 2280 PHE 2280 2280 2280 PHE PHE A . n 
A 1 2281 THR 2281 2281 2281 THR THR A . n 
A 1 2282 HIS 2282 2282 2282 HIS HIS A . n 
A 1 2283 VAL 2283 2283 2283 VAL VAL A . n 
A 1 2284 LEU 2284 2284 2284 LEU LEU A . n 
A 1 2285 ARG 2285 2285 2285 ARG ARG A . n 
A 1 2286 LYS 2286 2286 2286 LYS LYS A . n 
A 1 2287 ILE 2287 2287 2287 ILE ILE A . n 
A 1 2288 ILE 2288 2288 2288 ILE ILE A . n 
A 1 2289 ASP 2289 2289 2289 ASP ASP A . n 
A 1 2290 SER 2290 2290 2290 SER SER A . n 
A 1 2291 VAL 2291 2291 2291 VAL VAL A . n 
A 1 2292 ARG 2292 2292 2292 ARG ARG A . n 
A 1 2293 GLY 2293 2293 2293 GLY GLY A . n 
A 1 2294 GLU 2294 2294 2294 GLU GLU A . n 
A 1 2295 LEU 2295 2295 2295 LEU LEU A . n 
A 1 2296 GLN 2296 2296 2296 GLN GLN A . n 
A 1 2297 LYS 2297 2297 2297 LYS LYS A . n 
A 1 2298 ARG 2298 2298 2298 ARG ARG A . n 
A 1 2299 GLN 2299 2299 2299 GLN GLN A . n 
A 1 2300 TRP 2300 2300 2300 TRP TRP A . n 
A 1 2301 ILE 2301 2301 2301 ILE ILE A . n 
A 1 2302 VAL 2302 2302 2302 VAL VAL A . n 
A 1 2303 PHE 2303 2303 2303 PHE PHE A . n 
A 1 2304 ASP 2304 2304 2304 ASP ASP A . n 
A 1 2305 GLY 2305 2305 2305 GLY GLY A . n 
A 1 2306 ASP 2306 2306 2306 ASP ASP A . n 
A 1 2307 VAL 2307 2307 2307 VAL VAL A . n 
A 1 2308 ASP 2308 2308 2308 ASP ASP A . n 
A 1 2309 PRO 2309 2309 2309 PRO PRO A . n 
A 1 2310 GLU 2310 2310 2310 GLU GLU A . n 
A 1 2311 TRP 2311 2311 2311 TRP TRP A . n 
A 1 2312 VAL 2312 2312 2312 VAL VAL A . n 
A 1 2313 GLU 2313 2313 2313 GLU GLU A . n 
A 1 2314 ASN 2314 2314 2314 ASN ASN A . n 
A 1 2315 LEU 2315 2315 2315 LEU LEU A . n 
A 1 2316 ASN 2316 2316 2316 ASN ASN A . n 
A 1 2317 SER 2317 2317 2317 SER SER A . n 
A 1 2318 VAL 2318 2318 2318 VAL VAL A . n 
A 1 2319 LEU 2319 2319 2319 LEU LEU A . n 
A 1 2320 ASP 2320 2320 2320 ASP ASP A . n 
A 1 2321 ASP 2321 2321 2321 ASP ASP A . n 
A 1 2322 ASN 2322 2322 2322 ASN ASN A . n 
A 1 2323 LYS 2323 2323 2323 LYS LYS A . n 
A 1 2324 LEU 2324 2324 2324 LEU LEU A . n 
A 1 2325 LEU 2325 2325 2325 LEU LEU A . n 
A 1 2326 THR 2326 2326 2326 THR THR A . n 
A 1 2327 LEU 2327 2327 2327 LEU LEU A . n 
A 1 2328 PRO 2328 2328 2328 PRO PRO A . n 
A 1 2329 ASN 2329 2329 2329 ASN ASN A . n 
A 1 2330 GLY 2330 2330 2330 GLY GLY A . n 
A 1 2331 GLU 2331 2331 2331 GLU GLU A . n 
A 1 2332 ARG 2332 2332 2332 ARG ARG A . n 
A 1 2333 LEU 2333 2333 2333 LEU LEU A . n 
A 1 2334 SER 2334 2334 2334 SER SER A . n 
A 1 2335 LEU 2335 2335 2335 LEU LEU A . n 
A 1 2336 PRO 2336 2336 2336 PRO PRO A . n 
A 1 2337 PRO 2337 2337 2337 PRO PRO A . n 
A 1 2338 ASN 2338 2338 2338 ASN ASN A . n 
A 1 2339 VAL 2339 2339 2339 VAL VAL A . n 
A 1 2340 ARG 2340 2340 2340 ARG ARG A . n 
A 1 2341 ILE 2341 2341 2341 ILE ILE A . n 
A 1 2342 MET 2342 2342 2342 MET MET A . n 
A 1 2343 PHE 2343 2343 2343 PHE PHE A . n 
A 1 2344 GLU 2344 2344 2344 GLU GLU A . n 
A 1 2345 VAL 2345 2345 2345 VAL VAL A . n 
A 1 2346 GLN 2346 2346 2346 GLN GLN A . n 
A 1 2347 ASP 2347 2347 2347 ASP ASP A . n 
A 1 2348 LEU 2348 2348 2348 LEU LEU A . n 
A 1 2349 LYS 2349 2349 2349 LYS LYS A . n 
A 1 2350 TYR 2350 2350 2350 TYR TYR A . n 
A 1 2351 ALA 2351 2351 2351 ALA ALA A . n 
A 1 2352 THR 2352 2352 2352 THR THR A . n 
A 1 2353 LEU 2353 2353 2353 LEU LEU A . n 
A 1 2354 ALA 2354 2354 2354 ALA ALA A . n 
A 1 2355 THR 2355 2355 2355 THR THR A . n 
A 1 2356 VAL 2356 2356 2356 VAL VAL A . n 
A 1 2357 SER 2357 2357 2357 SER SER A . n 
A 1 2358 ARG 2358 2358 2358 ARG ARG A . n 
A 1 2359 CYS 2359 2359 2359 CYS CYS A . n 
A 1 2360 GLY 2360 2360 2360 GLY GLY A . n 
A 1 2361 MET 2361 2361 2361 MET MET A . n 
A 1 2362 VAL 2362 2362 2362 VAL VAL A . n 
A 1 2363 TRP 2363 2363 2363 TRP TRP A . n 
A 1 2364 PHE 2364 2364 2364 PHE PHE A . n 
A 1 2365 SER 2365 2365 2365 SER SER A . n 
A 1 2366 GLU 2366 2366 2366 GLU GLU A . n 
A 1 2367 ASP 2367 2367 2367 ASP ASP A . n 
A 1 2368 VAL 2368 2368 2368 VAL VAL A . n 
A 1 2369 LEU 2369 2369 2369 LEU LEU A . n 
A 1 2370 SER 2370 2370 2370 SER SER A . n 
A 1 2371 THR 2371 2371 2371 THR THR A . n 
A 1 2372 ASP 2372 2372 2372 ASP ASP A . n 
A 1 2373 MET 2373 2373 2373 MET MET A . n 
A 1 2374 ILE 2374 2374 2374 ILE ILE A . n 
A 1 2375 PHE 2375 2375 2375 PHE PHE A . n 
A 1 2376 ASN 2376 2376 2376 ASN ASN A . n 
A 1 2377 ASN 2377 2377 2377 ASN ASN A . n 
A 1 2378 PHE 2378 2378 2378 PHE PHE A . n 
A 1 2379 LEU 2379 2379 2379 LEU LEU A . n 
A 1 2380 ALA 2380 2380 2380 ALA ALA A . n 
A 1 2381 ARG 2381 2381 2381 ARG ARG A . n 
A 1 2382 LEU 2382 2382 2382 LEU LEU A . n 
A 1 2383 ARG 2383 2383 2383 ARG ARG A . n 
A 1 2384 SER 2384 2384 2384 SER SER A . n 
A 1 2385 ILE 2385 2385 2385 ILE ILE A . n 
A 1 2386 PRO 2386 2386 2386 PRO PRO A . n 
A 1 2387 LEU 2387 2387 2387 LEU LEU A . n 
A 1 2388 ASP 2388 2388 2388 ASP ASP A . n 
A 1 2389 GLU 2389 2389 2389 GLU GLU A . n 
A 1 2390 GLY 2390 2390 2390 GLY GLY A . n 
A 1 2391 GLU 2391 2391 2391 GLU GLU A . n 
A 1 2392 ASP 2392 2392 2392 ASP ASP A . n 
A 1 2393 GLU 2393 2393 2393 GLU GLU A . n 
A 1 2394 ALA 2394 2394 2394 ALA ALA A . n 
A 1 2395 GLN 2395 2395 2395 GLN GLN A . n 
A 1 2396 ARG 2396 2396 2396 ARG ARG A . n 
A 1 2397 ARG 2397 2397 2397 ARG ARG A . n 
A 1 2398 ARG 2398 2398 2398 ARG ARG A . n 
A 1 2399 LYS 2399 2399 2399 LYS LYS A . n 
A 1 2400 GLY 2400 2400 2400 GLY GLY A . n 
A 1 2401 LYS 2401 2401 2401 LYS LYS A . n 
A 1 2402 GLU 2402 2402 2402 GLU GLU A . n 
A 1 2403 ASP 2403 2403 2403 ASP ASP A . n 
A 1 2404 GLU 2404 2404 2404 GLU GLU A . n 
A 1 2405 GLY 2405 2405 2405 GLY GLY A . n 
A 1 2406 GLU 2406 2406 2406 GLU GLU A . n 
A 1 2407 GLU 2407 2407 2407 GLU GLU A . n 
A 1 2408 ALA 2408 2408 2408 ALA ALA A . n 
A 1 2409 ALA 2409 2409 2409 ALA ALA A . n 
A 1 2410 SER 2410 2410 2410 SER SER A . n 
A 1 2411 PRO 2411 2411 2411 PRO PRO A . n 
A 1 2412 MET 2412 2412 2412 MET MET A . n 
A 1 2413 LEU 2413 2413 2413 LEU LEU A . n 
A 1 2414 GLN 2414 2414 2414 GLN GLN A . n 
A 1 2415 ILE 2415 2415 2415 ILE ILE A . n 
A 1 2416 GLN 2416 2416 2416 GLN GLN A . n 
A 1 2417 ARG 2417 2417 2417 ARG ARG A . n 
A 1 2418 ASP 2418 2418 2418 ASP ASP A . n 
A 1 2419 ALA 2419 2419 2419 ALA ALA A . n 
A 1 2420 ALA 2420 2420 2420 ALA ALA A . n 
A 1 2421 THR 2421 2421 2421 THR THR A . n 
A 1 2422 ILE 2422 2422 2422 ILE ILE A . n 
A 1 2423 MET 2423 2423 2423 MET MET A . n 
A 1 2424 GLN 2424 2424 2424 GLN GLN A . n 
A 1 2425 PRO 2425 2425 2425 PRO PRO A . n 
A 1 2426 TYR 2426 2426 2426 TYR TYR A . n 
A 1 2427 PHE 2427 2427 2427 PHE PHE A . n 
A 1 2428 THR 2428 2428 2428 THR THR A . n 
A 1 2429 SER 2429 2429 2429 SER SER A . n 
A 1 2430 ASN 2430 2430 2430 ASN ASN A . n 
A 1 2431 GLY 2431 2431 2431 GLY GLY A . n 
A 1 2432 LEU 2432 2432 2432 LEU LEU A . n 
A 1 2433 VAL 2433 2433 2433 VAL VAL A . n 
A 1 2434 THR 2434 2434 2434 THR THR A . n 
A 1 2435 LYS 2435 2435 2435 LYS LYS A . n 
A 1 2436 ALA 2436 2436 2436 ALA ALA A . n 
A 1 2437 LEU 2437 2437 2437 LEU LEU A . n 
A 1 2438 GLU 2438 2438 2438 GLU GLU A . n 
A 1 2439 HIS 2439 2439 2439 HIS HIS A . n 
A 1 2440 ALA 2440 2440 2440 ALA ALA A . n 
A 1 2441 PHE 2441 2441 2441 PHE PHE A . n 
A 1 2442 GLN 2442 2442 2442 GLN GLN A . n 
A 1 2443 LEU 2443 2443 2443 LEU LEU A . n 
A 1 2444 GLU 2444 2444 2444 GLU GLU A . n 
A 1 2445 HIS 2445 2445 2445 HIS HIS A . n 
A 1 2446 ILE 2446 2446 2446 ILE ILE A . n 
A 1 2447 MET 2447 2447 2447 MET MET A . n 
A 1 2448 ASP 2448 2448 2448 ASP ASP A . n 
A 1 2449 LEU 2449 2449 2449 LEU LEU A . n 
A 1 2450 THR 2450 2450 2450 THR THR A . n 
A 1 2451 ARG 2451 2451 2451 ARG ARG A . n 
A 1 2452 LEU 2452 2452 2452 LEU LEU A . n 
A 1 2453 ARG 2453 2453 2453 ARG ARG A . n 
A 1 2454 CYS 2454 2454 2454 CYS CYS A . n 
A 1 2455 LEU 2455 2455 2455 LEU LEU A . n 
A 1 2456 GLY 2456 2456 2456 GLY GLY A . n 
A 1 2457 SER 2457 2457 2457 SER SER A . n 
A 1 2458 LEU 2458 2458 2458 LEU LEU A . n 
A 1 2459 PHE 2459 2459 2459 PHE PHE A . n 
A 1 2460 SER 2460 2460 2460 SER SER A . n 
A 1 2461 MET 2461 2461 2461 MET MET A . n 
A 1 2462 LEU 2462 2462 2462 LEU LEU A . n 
A 1 2463 HIS 2463 2463 2463 HIS HIS A . n 
A 1 2464 GLN 2464 2464 2464 GLN GLN A . n 
A 1 2465 ALA 2465 2465 2465 ALA ALA A . n 
A 1 2466 CYS 2466 2466 2466 CYS CYS A . n 
A 1 2467 ARG 2467 2467 2467 ARG ARG A . n 
A 1 2468 ASN 2468 2468 2468 ASN ASN A . n 
A 1 2469 VAL 2469 2469 2469 VAL VAL A . n 
A 1 2470 ALA 2470 2470 2470 ALA ALA A . n 
A 1 2471 GLN 2471 2471 2471 GLN GLN A . n 
A 1 2472 TYR 2472 2472 2472 TYR TYR A . n 
A 1 2473 ASN 2473 2473 2473 ASN ASN A . n 
A 1 2474 ALA 2474 2474 2474 ALA ALA A . n 
A 1 2475 ASN 2475 2475 2475 ASN ASN A . n 
A 1 2476 HIS 2476 2476 2476 HIS HIS A . n 
A 1 2477 PRO 2477 2477 2477 PRO PRO A . n 
A 1 2478 ASP 2478 2478 2478 ASP ASP A . n 
A 1 2479 PHE 2479 2479 2479 PHE PHE A . n 
A 1 2480 PRO 2480 2480 2480 PRO PRO A . n 
A 1 2481 MET 2481 2481 2481 MET MET A . n 
A 1 2482 GLN 2482 2482 2482 GLN GLN A . n 
A 1 2483 ILE 2483 2483 2483 ILE ILE A . n 
A 1 2484 GLU 2484 2484 2484 GLU GLU A . n 
A 1 2485 GLN 2485 2485 2485 GLN GLN A . n 
A 1 2486 LEU 2486 2486 2486 LEU LEU A . n 
A 1 2487 GLU 2487 2487 2487 GLU GLU A . n 
A 1 2488 ARG 2488 2488 2488 ARG ARG A . n 
A 1 2489 TYR 2489 2489 2489 TYR TYR A . n 
A 1 2490 ILE 2490 2490 2490 ILE ILE A . n 
A 1 2491 GLN 2491 2491 2491 GLN GLN A . n 
A 1 2492 ARG 2492 2492 2492 ARG ARG A . n 
A 1 2493 TYR 2493 2493 2493 TYR TYR A . n 
A 1 2494 LEU 2494 2494 2494 LEU LEU A . n 
A 1 2495 VAL 2495 2495 2495 VAL VAL A . n 
A 1 2496 TYR 2496 2496 2496 TYR TYR A . n 
A 1 2497 ALA 2497 2497 2497 ALA ALA A . n 
A 1 2498 ILE 2498 2498 2498 ILE ILE A . n 
A 1 2499 LEU 2499 2499 2499 LEU LEU A . n 
A 1 2500 TRP 2500 2500 2500 TRP TRP A . n 
A 1 2501 SER 2501 2501 2501 SER SER A . n 
A 1 2502 LEU 2502 2502 2502 LEU LEU A . n 
A 1 2503 SER 2503 2503 2503 SER SER A . n 
A 1 2504 GLY 2504 2504 2504 GLY GLY A . n 
A 1 2505 ASP 2505 2505 2505 ASP ASP A . n 
A 1 2506 SER 2506 2506 2506 SER SER A . n 
A 1 2507 ARG 2507 2507 2507 ARG ARG A . n 
A 1 2508 LEU 2508 2508 2508 LEU LEU A . n 
A 1 2509 LYS 2509 2509 2509 LYS LYS A . n 
A 1 2510 MET 2510 2510 2510 MET MET A . n 
A 1 2511 ARG 2511 2511 2511 ARG ARG A . n 
A 1 2512 ALA 2512 2512 2512 ALA ALA A . n 
A 1 2513 GLU 2513 2513 2513 GLU GLU A . n 
A 1 2514 LEU 2514 2514 2514 LEU LEU A . n 
A 1 2515 GLY 2515 2515 2515 GLY GLY A . n 
A 1 2516 GLU 2516 2516 2516 GLU GLU A . n 
A 1 2517 TYR 2517 2517 2517 TYR TYR A . n 
A 1 2518 ILE 2518 2518 2518 ILE ILE A . n 
A 1 2519 ARG 2519 2519 2519 ARG ARG A . n 
A 1 2520 ARG 2520 2520 2520 ARG ARG A . n 
A 1 2521 ILE 2521 2521 2521 ILE ILE A . n 
A 1 2522 THR 2522 2522 2522 THR THR A . n 
A 1 2523 THR 2523 2523 2523 THR THR A . n 
A 1 2524 VAL 2524 2524 2524 VAL VAL A . n 
A 1 2525 PRO 2525 2525 2525 PRO PRO A . n 
A 1 2526 LEU 2526 2526 2526 LEU LEU A . n 
A 1 2527 PRO 2527 2527 2527 PRO PRO A . n 
A 1 2528 THR 2528 2528 2528 THR THR A . n 
A 1 2529 ALA 2529 2529 2529 ALA ALA A . n 
A 1 2530 PRO 2530 2530 2530 PRO PRO A . n 
A 1 2531 ASN 2531 2531 2531 ASN ASN A . n 
A 1 2532 ILE 2532 2532 2532 ILE ILE A . n 
A 1 2533 PRO 2533 2533 2533 PRO PRO A . n 
A 1 2534 ILE 2534 2534 2534 ILE ILE A . n 
A 1 2535 ILE 2535 2535 2535 ILE ILE A . n 
A 1 2536 ASP 2536 2536 2536 ASP ASP A . n 
A 1 2537 TYR 2537 2537 2537 TYR TYR A . n 
A 1 2538 GLU 2538 2538 2538 GLU GLU A . n 
A 1 2539 VAL 2539 2539 2539 VAL VAL A . n 
A 1 2540 SER 2540 2540 2540 SER SER A . n 
A 1 2541 ILE 2541 2541 2541 ILE ILE A . n 
A 1 2542 SER 2542 2542 2542 SER SER A . n 
A 1 2543 GLY 2543 2543 2543 GLY GLY A . n 
A 1 2544 GLU 2544 2544 2544 GLU GLU A . n 
A 1 2545 TRP 2545 2545 2545 TRP TRP A . n 
A 1 2546 SER 2546 2546 2546 SER SER A . n 
A 1 2547 PRO 2547 2547 2547 PRO PRO A . n 
A 1 2548 TRP 2548 2548 2548 TRP TRP A . n 
A 1 2549 GLN 2549 2549 2549 GLN GLN A . n 
A 1 2550 ALA 2550 2550 2550 ALA ALA A . n 
A 1 2551 LYS 2551 2551 2551 LYS LYS A . n 
A 1 2552 VAL 2552 2552 2552 VAL VAL A . n 
A 1 2553 PRO 2553 2553 2553 PRO PRO A . n 
A 1 2554 GLN 2554 2554 2554 GLN GLN A . n 
A 1 2555 ILE 2555 2555 2555 ILE ILE A . n 
A 1 2556 GLU 2556 2556 2556 GLU GLU A . n 
A 1 2557 VAL 2557 2557 2557 VAL VAL A . n 
A 1 2558 GLU 2558 2558 2558 GLU GLU A . n 
A 1 2559 THR 2559 2559 2559 THR THR A . n 
A 1 2560 HIS 2560 2560 2560 HIS HIS A . n 
A 1 2561 LYS 2561 2561 2561 LYS LYS A . n 
A 1 2562 VAL 2562 2562 2562 VAL VAL A . n 
A 1 2563 ALA 2563 2563 2563 ALA ALA A . n 
A 1 2564 ALA 2564 2564 2564 ALA ALA A . n 
A 1 2565 PRO 2565 2565 2565 PRO PRO A . n 
A 1 2566 ASP 2566 2566 2566 ASP ASP A . n 
A 1 2567 VAL 2567 2567 2567 VAL VAL A . n 
A 1 2568 VAL 2568 2568 2568 VAL VAL A . n 
A 1 2569 VAL 2569 2569 2569 VAL VAL A . n 
A 1 2570 PRO 2570 2570 2570 PRO PRO A . n 
A 1 2571 THR 2571 2571 2571 THR THR A . n 
A 1 2572 LEU 2572 2572 2572 LEU LEU A . n 
A 1 2573 ASP 2573 2573 2573 ASP ASP A . n 
A 1 2574 THR 2574 2574 2574 THR THR A . n 
A 1 2575 VAL 2575 2575 2575 VAL VAL A . n 
A 1 2576 ARG 2576 2576 2576 ARG ARG A . n 
A 1 2577 HIS 2577 2577 2577 HIS HIS A . n 
A 1 2578 GLU 2578 2578 2578 GLU GLU A . n 
A 1 2579 ALA 2579 2579 2579 ALA ALA A . n 
A 1 2580 LEU 2580 2580 2580 LEU LEU A . n 
A 1 2581 LEU 2581 2581 2581 LEU LEU A . n 
A 1 2582 TYR 2582 2582 2582 TYR TYR A . n 
A 1 2583 THR 2583 2583 2583 THR THR A . n 
A 1 2584 TRP 2584 2584 2584 TRP TRP A . n 
A 1 2585 LEU 2585 2585 2585 LEU LEU A . n 
A 1 2586 ALA 2586 2586 2586 ALA ALA A . n 
A 1 2587 GLU 2587 2587 2587 GLU GLU A . n 
A 1 2588 HIS 2588 2588 2588 HIS HIS A . n 
A 1 2589 LYS 2589 2589 2589 LYS LYS A . n 
A 1 2590 PRO 2590 2590 2590 PRO PRO A . n 
A 1 2591 LEU 2591 2591 2591 LEU LEU A . n 
A 1 2592 VAL 2592 2592 2592 VAL VAL A . n 
A 1 2593 LEU 2593 2593 2593 LEU LEU A . n 
A 1 2594 CYS 2594 2594 2594 CYS CYS A . n 
A 1 2595 GLY 2595 2595 2595 GLY GLY A . n 
A 1 2596 PRO 2596 2596 2596 PRO PRO A . n 
A 1 2597 PRO 2597 2597 2597 PRO PRO A . n 
A 1 2598 GLY 2598 2598 2598 GLY GLY A . n 
A 1 2599 SER 2599 2599 2599 SER SER A . n 
A 1 2600 GLY 2600 2600 2600 GLY GLY A . n 
A 1 2601 LYS 2601 2601 2601 LYS LYS A . n 
A 1 2602 THR 2602 2602 2602 THR THR A . n 
A 1 2603 MET 2603 2603 2603 MET MET A . n 
A 1 2604 THR 2604 2604 2604 THR THR A . n 
A 1 2605 LEU 2605 2605 2605 LEU LEU A . n 
A 1 2606 PHE 2606 2606 2606 PHE PHE A . n 
A 1 2607 SER 2607 2607 2607 SER SER A . n 
A 1 2608 ALA 2608 2608 2608 ALA ALA A . n 
A 1 2609 LEU 2609 2609 2609 LEU LEU A . n 
A 1 2610 ARG 2610 2610 2610 ARG ARG A . n 
A 1 2611 ALA 2611 2611 2611 ALA ALA A . n 
A 1 2612 LEU 2612 2612 2612 LEU LEU A . n 
A 1 2613 PRO 2613 2613 2613 PRO PRO A . n 
A 1 2614 ASP 2614 2614 2614 ASP ASP A . n 
A 1 2615 MET 2615 2615 2615 MET MET A . n 
A 1 2616 GLU 2616 2616 2616 GLU GLU A . n 
A 1 2617 VAL 2617 2617 2617 VAL VAL A . n 
A 1 2618 VAL 2618 2618 2618 VAL VAL A . n 
A 1 2619 GLY 2619 2619 2619 GLY GLY A . n 
A 1 2620 LEU 2620 2620 2620 LEU LEU A . n 
A 1 2621 ASN 2621 2621 2621 ASN ASN A . n 
A 1 2622 PHE 2622 2622 2622 PHE PHE A . n 
A 1 2623 SER 2623 2623 2623 SER SER A . n 
A 1 2624 SER 2624 2624 2624 SER SER A . n 
A 1 2625 ALA 2625 2625 2625 ALA ALA A . n 
A 1 2626 THR 2626 2626 2626 THR THR A . n 
A 1 2627 THR 2627 2627 2627 THR THR A . n 
A 1 2628 PRO 2628 2628 2628 PRO PRO A . n 
A 1 2629 GLU 2629 2629 2629 GLU GLU A . n 
A 1 2630 LEU 2630 2630 2630 LEU LEU A . n 
A 1 2631 LEU 2631 2631 2631 LEU LEU A . n 
A 1 2632 LEU 2632 2632 2632 LEU LEU A . n 
A 1 2633 LYS 2633 2633 2633 LYS LYS A . n 
A 1 2634 THR 2634 2634 2634 THR THR A . n 
A 1 2635 PHE 2635 2635 2635 PHE PHE A . n 
A 1 2636 ASP 2636 2636 2636 ASP ASP A . n 
A 1 2637 HIS 2637 2637 2637 HIS HIS A . n 
A 1 2638 TYR 2638 2638 2638 TYR TYR A . n 
A 1 2639 CYS 2639 2639 2639 CYS CYS A . n 
A 1 2640 GLU 2640 2640 2640 GLU GLU A . n 
A 1 2641 TYR 2641 2641 2641 TYR TYR A . n 
A 1 2642 ARG 2642 2642 2642 ARG ARG A . n 
A 1 2643 ARG 2643 2643 2643 ARG ARG A . n 
A 1 2644 THR 2644 2644 2644 THR THR A . n 
A 1 2645 PRO 2645 2645 2645 PRO PRO A . n 
A 1 2646 ASN 2646 2646 2646 ASN ASN A . n 
A 1 2647 GLY 2647 2647 2647 GLY GLY A . n 
A 1 2648 VAL 2648 2648 2648 VAL VAL A . n 
A 1 2649 VAL 2649 2649 2649 VAL VAL A . n 
A 1 2650 LEU 2650 2650 2650 LEU LEU A . n 
A 1 2651 ALA 2651 2651 2651 ALA ALA A . n 
A 1 2652 PRO 2652 2652 2652 PRO PRO A . n 
A 1 2653 VAL 2653 2653 2653 VAL VAL A . n 
A 1 2654 GLN 2654 2654 2654 GLN GLN A . n 
A 1 2655 LEU 2655 2655 2655 LEU LEU A . n 
A 1 2656 GLY 2656 2656 2656 GLY GLY A . n 
A 1 2657 LYS 2657 2657 2657 LYS LYS A . n 
A 1 2658 TRP 2658 2658 2658 TRP TRP A . n 
A 1 2659 LEU 2659 2659 2659 LEU LEU A . n 
A 1 2660 VAL 2660 2660 2660 VAL VAL A . n 
A 1 2661 LEU 2661 2661 2661 LEU LEU A . n 
A 1 2662 PHE 2662 2662 2662 PHE PHE A . n 
A 1 2663 CYS 2663 2663 2663 CYS CYS A . n 
A 1 2664 ASP 2664 2664 2664 ASP ASP A . n 
A 1 2665 GLU 2665 2665 2665 GLU GLU A . n 
A 1 2666 ILE 2666 2666 2666 ILE ILE A . n 
A 1 2667 ASN 2667 2667 2667 ASN ASN A . n 
A 1 2668 LEU 2668 2668 2668 LEU LEU A . n 
A 1 2669 PRO 2669 2669 2669 PRO PRO A . n 
A 1 2670 ASP 2670 2670 2670 ASP ASP A . n 
A 1 2671 MET 2671 2671 2671 MET MET A . n 
A 1 2672 ASP 2672 2672 2672 ASP ASP A . n 
A 1 2673 LYS 2673 2673 2673 LYS LYS A . n 
A 1 2674 TYR 2674 2674 2674 TYR TYR A . n 
A 1 2675 GLY 2675 2675 2675 GLY GLY A . n 
A 1 2676 THR 2676 2676 2676 THR THR A . n 
A 1 2677 GLN 2677 2677 2677 GLN GLN A . n 
A 1 2678 ARG 2678 2678 2678 ARG ARG A . n 
A 1 2679 VAL 2679 2679 2679 VAL VAL A . n 
A 1 2680 ILE 2680 2680 2680 ILE ILE A . n 
A 1 2681 SER 2681 2681 2681 SER SER A . n 
A 1 2682 PHE 2682 2682 2682 PHE PHE A . n 
A 1 2683 ILE 2683 2683 2683 ILE ILE A . n 
A 1 2684 ARG 2684 2684 2684 ARG ARG A . n 
A 1 2685 GLN 2685 2685 2685 GLN GLN A . n 
A 1 2686 MET 2686 2686 2686 MET MET A . n 
A 1 2687 VAL 2687 2687 2687 VAL VAL A . n 
A 1 2688 GLU 2688 2688 2688 GLU GLU A . n 
A 1 2689 HIS 2689 2689 2689 HIS HIS A . n 
A 1 2690 GLY 2690 2690 2690 GLY GLY A . n 
A 1 2691 GLY 2691 2691 2691 GLY GLY A . n 
A 1 2692 PHE 2692 2692 2692 PHE PHE A . n 
A 1 2693 TYR 2693 2693 2693 TYR TYR A . n 
A 1 2694 ARG 2694 2694 2694 ARG ARG A . n 
A 1 2695 THR 2695 2695 2695 THR THR A . n 
A 1 2696 SER 2696 2696 2696 SER SER A . n 
A 1 2697 ASP 2697 2697 2697 ASP ASP A . n 
A 1 2698 GLN 2698 2698 2698 GLN GLN A . n 
A 1 2699 THR 2699 2699 2699 THR THR A . n 
A 1 2700 TRP 2700 2700 2700 TRP TRP A . n 
A 1 2701 VAL 2701 2701 2701 VAL VAL A . n 
A 1 2702 LYS 2702 2702 2702 LYS LYS A . n 
A 1 2703 LEU 2703 2703 2703 LEU LEU A . n 
A 1 2704 GLU 2704 2704 2704 GLU GLU A . n 
A 1 2705 ARG 2705 2705 2705 ARG ARG A . n 
A 1 2706 ILE 2706 2706 2706 ILE ILE A . n 
A 1 2707 GLN 2707 2707 2707 GLN GLN A . n 
A 1 2708 PHE 2708 2708 2708 PHE PHE A . n 
A 1 2709 VAL 2709 2709 2709 VAL VAL A . n 
A 1 2710 GLY 2710 2710 2710 GLY GLY A . n 
A 1 2711 ALA 2711 2711 2711 ALA ALA A . n 
A 1 2712 CYS 2712 2712 2712 CYS CYS A . n 
A 1 2713 ASN 2713 2713 2713 ASN ASN A . n 
A 1 2714 PRO 2714 2714 2714 PRO PRO A . n 
A 1 2715 PRO 2715 2715 2715 PRO PRO A . n 
A 1 2716 THR 2716 2716 2716 THR THR A . n 
A 1 2717 ASP 2717 2717 2717 ASP ASP A . n 
A 1 2718 PRO 2718 2718 2718 PRO PRO A . n 
A 1 2719 GLY 2719 2719 2719 GLY GLY A . n 
A 1 2720 ARG 2720 2720 2720 ARG ARG A . n 
A 1 2721 LYS 2721 2721 2721 LYS LYS A . n 
A 1 2722 PRO 2722 2722 2722 PRO PRO A . n 
A 1 2723 LEU 2723 2723 2723 LEU LEU A . n 
A 1 2724 SER 2724 2724 2724 SER SER A . n 
A 1 2725 HIS 2725 2725 2725 HIS HIS A . n 
A 1 2726 ARG 2726 2726 2726 ARG ARG A . n 
A 1 2727 PHE 2727 2727 2727 PHE PHE A . n 
A 1 2728 LEU 2728 2728 2728 LEU LEU A . n 
A 1 2729 ARG 2729 2729 2729 ARG ARG A . n 
A 1 2730 HIS 2730 2730 2730 HIS HIS A . n 
A 1 2731 VAL 2731 2731 2731 VAL VAL A . n 
A 1 2732 PRO 2732 2732 2732 PRO PRO A . n 
A 1 2733 VAL 2733 2733 2733 VAL VAL A . n 
A 1 2734 VAL 2734 2734 2734 VAL VAL A . n 
A 1 2735 TYR 2735 2735 2735 TYR TYR A . n 
A 1 2736 VAL 2736 2736 2736 VAL VAL A . n 
A 1 2737 ASP 2737 2737 2737 ASP ASP A . n 
A 1 2738 TYR 2738 2738 2738 TYR TYR A . n 
A 1 2739 PRO 2739 2739 2739 PRO PRO A . n 
A 1 2740 GLY 2740 2740 2740 GLY GLY A . n 
A 1 2741 PRO 2741 2741 2741 PRO PRO A . n 
A 1 2742 ALA 2742 2742 2742 ALA ALA A . n 
A 1 2743 SER 2743 2743 2743 SER SER A . n 
A 1 2744 LEU 2744 2744 2744 LEU LEU A . n 
A 1 2745 THR 2745 2745 2745 THR THR A . n 
A 1 2746 GLN 2746 2746 2746 GLN GLN A . n 
A 1 2747 ILE 2747 2747 2747 ILE ILE A . n 
A 1 2748 TYR 2748 2748 2748 TYR TYR A . n 
A 1 2749 GLY 2749 2749 2749 GLY GLY A . n 
A 1 2750 THR 2750 2750 2750 THR THR A . n 
A 1 2751 PHE 2751 2751 2751 PHE PHE A . n 
A 1 2752 ASN 2752 2752 2752 ASN ASN A . n 
A 1 2753 ARG 2753 2753 2753 ARG ARG A . n 
A 1 2754 ALA 2754 2754 2754 ALA ALA A . n 
A 1 2755 MET 2755 2755 2755 MET MET A . n 
A 1 2756 LEU 2756 2756 2756 LEU LEU A . n 
A 1 2757 ARG 2757 2757 2757 ARG ARG A . n 
A 1 2758 LEU 2758 2758 2758 LEU LEU A . n 
A 1 2759 ILE 2759 2759 2759 ILE ILE A . n 
A 1 2760 PRO 2760 2760 2760 PRO PRO A . n 
A 1 2761 SER 2761 2761 2761 SER SER A . n 
A 1 2762 LEU 2762 2762 2762 LEU LEU A . n 
A 1 2763 ARG 2763 2763 2763 ARG ARG A . n 
A 1 2764 THR 2764 2764 2764 THR THR A . n 
A 1 2765 TYR 2765 2765 2765 TYR TYR A . n 
A 1 2766 ALA 2766 2766 2766 ALA ALA A . n 
A 1 2767 GLU 2767 2767 2767 GLU GLU A . n 
A 1 2768 PRO 2768 2768 2768 PRO PRO A . n 
A 1 2769 LEU 2769 2769 2769 LEU LEU A . n 
A 1 2770 THR 2770 2770 2770 THR THR A . n 
A 1 2771 ALA 2771 2771 2771 ALA ALA A . n 
A 1 2772 ALA 2772 2772 2772 ALA ALA A . n 
A 1 2773 MET 2773 2773 2773 MET MET A . n 
A 1 2774 VAL 2774 2774 2774 VAL VAL A . n 
A 1 2775 GLU 2775 2775 2775 GLU GLU A . n 
A 1 2776 PHE 2776 2776 2776 PHE PHE A . n 
A 1 2777 TYR 2777 2777 2777 TYR TYR A . n 
A 1 2778 THR 2778 2778 2778 THR THR A . n 
A 1 2779 MET 2779 2779 2779 MET MET A . n 
A 1 2780 SER 2780 2780 2780 SER SER A . n 
A 1 2781 GLN 2781 2781 2781 GLN GLN A . n 
A 1 2782 GLU 2782 2782 2782 GLU GLU A . n 
A 1 2783 ARG 2783 2783 2783 ARG ARG A . n 
A 1 2784 PHE 2784 2784 2784 PHE PHE A . n 
A 1 2785 THR 2785 2785 2785 THR THR A . n 
A 1 2786 GLN 2786 2786 2786 GLN GLN A . n 
A 1 2787 ASP 2787 2787 2787 ASP ASP A . n 
A 1 2788 THR 2788 2788 2788 THR THR A . n 
A 1 2789 GLN 2789 2789 2789 GLN GLN A . n 
A 1 2790 PRO 2790 2790 2790 PRO PRO A . n 
A 1 2791 HIS 2791 2791 2791 HIS HIS A . n 
A 1 2792 TYR 2792 2792 2792 TYR TYR A . n 
A 1 2793 ILE 2793 2793 2793 ILE ILE A . n 
A 1 2794 TYR 2794 2794 2794 TYR TYR A . n 
A 1 2795 SER 2795 2795 2795 SER SER A . n 
A 1 2796 PRO 2796 2796 2796 PRO PRO A . n 
A 1 2797 ARG 2797 2797 2797 ARG ARG A . n 
A 1 2798 GLU 2798 2798 2798 GLU GLU A . n 
A 1 2799 MET 2799 2799 2799 MET MET A . n 
A 1 2800 THR 2800 2800 2800 THR THR A . n 
A 1 2801 ARG 2801 2801 2801 ARG ARG A . n 
A 1 2802 TRP 2802 2802 2802 TRP TRP A . n 
A 1 2803 VAL 2803 2803 2803 VAL VAL A . n 
A 1 2804 ARG 2804 2804 2804 ARG ARG A . n 
A 1 2805 GLY 2805 2805 2805 GLY GLY A . n 
A 1 2806 ILE 2806 2806 2806 ILE ILE A . n 
A 1 2807 PHE 2807 2807 2807 PHE PHE A . n 
A 1 2808 GLU 2808 2808 2808 GLU GLU A . n 
A 1 2809 ALA 2809 2809 2809 ALA ALA A . n 
A 1 2810 LEU 2810 2810 2810 LEU LEU A . n 
A 1 2811 ARG 2811 2811 2811 ARG ARG A . n 
A 1 2812 PRO 2812 2812 2812 PRO PRO A . n 
A 1 2813 LEU 2813 2813 2813 LEU LEU A . n 
A 1 2814 GLU 2814 2814 2814 GLU GLU A . n 
A 1 2815 THR 2815 2815 2815 THR THR A . n 
A 1 2816 LEU 2816 2816 2816 LEU LEU A . n 
A 1 2817 PRO 2817 2817 2817 PRO PRO A . n 
A 1 2818 VAL 2818 2818 2818 VAL VAL A . n 
A 1 2819 GLU 2819 2819 2819 GLU GLU A . n 
A 1 2820 GLY 2820 2820 2820 GLY GLY A . n 
A 1 2821 LEU 2821 2821 2821 LEU LEU A . n 
A 1 2822 ILE 2822 2822 2822 ILE ILE A . n 
A 1 2823 ARG 2823 2823 2823 ARG ARG A . n 
A 1 2824 ILE 2824 2824 2824 ILE ILE A . n 
A 1 2825 TRP 2825 2825 2825 TRP TRP A . n 
A 1 2826 ALA 2826 2826 2826 ALA ALA A . n 
A 1 2827 HIS 2827 2827 2827 HIS HIS A . n 
A 1 2828 GLU 2828 2828 2828 GLU GLU A . n 
A 1 2829 ALA 2829 2829 2829 ALA ALA A . n 
A 1 2830 LEU 2830 2830 2830 LEU LEU A . n 
A 1 2831 ARG 2831 2831 2831 ARG ARG A . n 
A 1 2832 LEU 2832 2832 2832 LEU LEU A . n 
A 1 2833 PHE 2833 2833 2833 PHE PHE A . n 
A 1 2834 GLN 2834 2834 2834 GLN GLN A . n 
A 1 2835 ASP 2835 2835 2835 ASP ASP A . n 
A 1 2836 ARG 2836 2836 2836 ARG ARG A . n 
A 1 2837 LEU 2837 2837 2837 LEU LEU A . n 
A 1 2838 VAL 2838 2838 2838 VAL VAL A . n 
A 1 2839 GLU 2839 2839 2839 GLU GLU A . n 
A 1 2840 ASP 2840 2840 2840 ASP ASP A . n 
A 1 2841 GLU 2841 2841 2841 GLU GLU A . n 
A 1 2842 GLU 2842 2842 2842 GLU GLU A . n 
A 1 2843 ARG 2843 2843 2843 ARG ARG A . n 
A 1 2844 ARG 2844 2844 2844 ARG ARG A . n 
A 1 2845 TRP 2845 2845 2845 TRP TRP A . n 
A 1 2846 THR 2846 2846 2846 THR THR A . n 
A 1 2847 ASP 2847 2847 2847 ASP ASP A . n 
A 1 2848 GLU 2848 2848 2848 GLU GLU A . n 
A 1 2849 ASN 2849 2849 2849 ASN ASN A . n 
A 1 2850 ILE 2850 2850 2850 ILE ILE A . n 
A 1 2851 ASP 2851 2851 2851 ASP ASP A . n 
A 1 2852 THR 2852 2852 2852 THR THR A . n 
A 1 2853 VAL 2853 2853 2853 VAL VAL A . n 
A 1 2854 ALA 2854 2854 2854 ALA ALA A . n 
A 1 2855 LEU 2855 2855 2855 LEU LEU A . n 
A 1 2856 LYS 2856 2856 2856 LYS LYS A . n 
A 1 2857 HIS 2857 2857 2857 HIS HIS A . n 
A 1 2858 PHE 2858 2858 2858 PHE PHE A . n 
A 1 2859 PRO 2859 2859 2859 PRO PRO A . n 
A 1 2860 ASN 2860 2860 2860 ASN ASN A . n 
A 1 2861 ILE 2861 2861 2861 ILE ILE A . n 
A 1 2862 ASP 2862 2862 2862 ASP ASP A . n 
A 1 2863 ARG 2863 2863 2863 ARG ARG A . n 
A 1 2864 GLU 2864 2864 2864 GLU GLU A . n 
A 1 2865 LYS 2865 2865 2865 LYS LYS A . n 
A 1 2866 ALA 2866 2866 2866 ALA ALA A . n 
A 1 2867 MET 2867 2867 2867 MET MET A . n 
A 1 2868 SER 2868 2868 2868 SER SER A . n 
A 1 2869 ARG 2869 2869 2869 ARG ARG A . n 
A 1 2870 PRO 2870 2870 2870 PRO PRO A . n 
A 1 2871 ILE 2871 2871 2871 ILE ILE A . n 
A 1 2872 LEU 2872 2872 2872 LEU LEU A . n 
A 1 2873 TYR 2873 2873 2873 TYR TYR A . n 
A 1 2874 SER 2874 2874 2874 SER SER A . n 
A 1 2875 ASN 2875 2875 2875 ASN ASN A . n 
A 1 2876 TRP 2876 2876 2876 TRP TRP A . n 
A 1 2877 LEU 2877 2877 2877 LEU LEU A . n 
A 1 2878 SER 2878 2878 2878 SER SER A . n 
A 1 2879 LYS 2879 2879 2879 LYS LYS A . n 
A 1 2880 ASP 2880 2880 2880 ASP ASP A . n 
A 1 2881 TYR 2881 2881 2881 TYR TYR A . n 
A 1 2882 ILE 2882 2882 2882 ILE ILE A . n 
A 1 2883 PRO 2883 2883 2883 PRO PRO A . n 
A 1 2884 VAL 2884 2884 2884 VAL VAL A . n 
A 1 2885 ASP 2885 2885 2885 ASP ASP A . n 
A 1 2886 GLN 2886 2886 2886 GLN GLN A . n 
A 1 2887 GLU 2887 2887 2887 GLU GLU A . n 
A 1 2888 GLU 2888 2888 2888 GLU GLU A . n 
A 1 2889 LEU 2889 2889 2889 LEU LEU A . n 
A 1 2890 ARG 2890 2890 2890 ARG ARG A . n 
A 1 2891 ASP 2891 2891 2891 ASP ASP A . n 
A 1 2892 TYR 2892 2892 2892 TYR TYR A . n 
A 1 2893 VAL 2893 2893 2893 VAL VAL A . n 
A 1 2894 LYS 2894 2894 2894 LYS LYS A . n 
A 1 2895 ALA 2895 2895 2895 ALA ALA A . n 
A 1 2896 ARG 2896 2896 2896 ARG ARG A . n 
A 1 2897 LEU 2897 2897 2897 LEU LEU A . n 
A 1 2898 LYS 2898 2898 2898 LYS LYS A . n 
A 1 2899 VAL 2899 2899 2899 VAL VAL A . n 
A 1 2900 PHE 2900 2900 2900 PHE PHE A . n 
A 1 2901 TYR 2901 2901 2901 TYR TYR A . n 
A 1 2902 GLU 2902 2902 2902 GLU GLU A . n 
A 1 2903 GLU 2903 2903 2903 GLU GLU A . n 
A 1 2904 GLU 2904 2904 2904 GLU GLU A . n 
A 1 2905 LEU 2905 2905 2905 LEU LEU A . n 
A 1 2906 ASP 2906 2906 2906 ASP ASP A . n 
A 1 2907 VAL 2907 2907 2907 VAL VAL A . n 
A 1 2908 PRO 2908 2908 2908 PRO PRO A . n 
A 1 2909 LEU 2909 2909 2909 LEU LEU A . n 
A 1 2910 VAL 2910 2910 2910 VAL VAL A . n 
A 1 2911 LEU 2911 2911 2911 LEU LEU A . n 
A 1 2912 PHE 2912 2912 2912 PHE PHE A . n 
A 1 2913 ASN 2913 2913 2913 ASN ASN A . n 
A 1 2914 GLU 2914 2914 2914 GLU GLU A . n 
A 1 2915 VAL 2915 2915 2915 VAL VAL A . n 
A 1 2916 LEU 2916 2916 2916 LEU LEU A . n 
A 1 2917 ASP 2917 2917 2917 ASP ASP A . n 
A 1 2918 HIS 2918 2918 2918 HIS HIS A . n 
A 1 2919 VAL 2919 2919 2919 VAL VAL A . n 
A 1 2920 LEU 2920 2920 2920 LEU LEU A . n 
A 1 2921 ARG 2921 2921 2921 ARG ARG A . n 
A 1 2922 ILE 2922 2922 2922 ILE ILE A . n 
A 1 2923 ASP 2923 2923 2923 ASP ASP A . n 
A 1 2924 ARG 2924 2924 2924 ARG ARG A . n 
A 1 2925 ILE 2925 2925 2925 ILE ILE A . n 
A 1 2926 PHE 2926 2926 2926 PHE PHE A . n 
A 1 2927 ARG 2927 2927 2927 ARG ARG A . n 
A 1 2928 GLN 2928 2928 2928 GLN GLN A . n 
A 1 2929 PRO 2929 2929 2929 PRO PRO A . n 
A 1 2930 GLN 2930 2930 2930 GLN GLN A . n 
A 1 2931 GLY 2931 2931 2931 GLY GLY A . n 
A 1 2932 HIS 2932 2932 2932 HIS HIS A . n 
A 1 2933 LEU 2933 2933 2933 LEU LEU A . n 
A 1 2934 LEU 2934 2934 2934 LEU LEU A . n 
A 1 2935 LEU 2935 2935 2935 LEU LEU A . n 
A 1 2936 ILE 2936 2936 2936 ILE ILE A . n 
A 1 2937 GLY 2937 2937 2937 GLY GLY A . n 
A 1 2938 VAL 2938 2938 2938 VAL VAL A . n 
A 1 2939 SER 2939 2939 2939 SER SER A . n 
A 1 2940 GLY 2940 2940 2940 GLY GLY A . n 
A 1 2941 ALA 2941 2941 2941 ALA ALA A . n 
A 1 2942 GLY 2942 2942 2942 GLY GLY A . n 
A 1 2943 LYS 2943 2943 2943 LYS LYS A . n 
A 1 2944 THR 2944 2944 2944 THR THR A . n 
A 1 2945 THR 2945 2945 2945 THR THR A . n 
A 1 2946 LEU 2946 2946 2946 LEU LEU A . n 
A 1 2947 SER 2947 2947 2947 SER SER A . n 
A 1 2948 ARG 2948 2948 2948 ARG ARG A . n 
A 1 2949 PHE 2949 2949 2949 PHE PHE A . n 
A 1 2950 VAL 2950 2950 2950 VAL VAL A . n 
A 1 2951 ALA 2951 2951 2951 ALA ALA A . n 
A 1 2952 TRP 2952 2952 2952 TRP TRP A . n 
A 1 2953 MET 2953 2953 2953 MET MET A . n 
A 1 2954 ASN 2954 2954 2954 ASN ASN A . n 
A 1 2955 GLY 2955 2955 2955 GLY GLY A . n 
A 1 2956 LEU 2956 2956 2956 LEU LEU A . n 
A 1 2957 SER 2957 2957 2957 SER SER A . n 
A 1 2958 VAL 2958 2958 2958 VAL VAL A . n 
A 1 2959 TYR 2959 2959 2959 TYR TYR A . n 
A 1 2960 GLN 2960 2960 2960 GLN GLN A . n 
A 1 2961 ILE 2961 2961 2961 ILE ILE A . n 
A 1 2962 LYS 2962 2962 2962 LYS LYS A . n 
A 1 2963 VAL 2963 2963 2963 VAL VAL A . n 
A 1 2964 HIS 2964 2964 2964 HIS HIS A . n 
A 1 2965 ARG 2965 2965 2965 ARG ARG A . n 
A 1 2966 LYS 2966 2966 2966 LYS LYS A . n 
A 1 2967 TYR 2967 2967 2967 TYR TYR A . n 
A 1 2968 THR 2968 2968 2968 THR THR A . n 
A 1 2969 GLY 2969 2969 2969 GLY GLY A . n 
A 1 2970 GLU 2970 2970 2970 GLU GLU A . n 
A 1 2971 ASP 2971 2971 2971 ASP ASP A . n 
A 1 2972 PHE 2972 2972 2972 PHE PHE A . n 
A 1 2973 ASP 2973 2973 2973 ASP ASP A . n 
A 1 2974 GLU 2974 2974 2974 GLU GLU A . n 
A 1 2975 ASP 2975 2975 2975 ASP ASP A . n 
A 1 2976 LEU 2976 2976 2976 LEU LEU A . n 
A 1 2977 ARG 2977 2977 2977 ARG ARG A . n 
A 1 2978 THR 2978 2978 2978 THR THR A . n 
A 1 2979 VAL 2979 2979 2979 VAL VAL A . n 
A 1 2980 LEU 2980 2980 2980 LEU LEU A . n 
A 1 2981 ARG 2981 2981 2981 ARG ARG A . n 
A 1 2982 ARG 2982 2982 2982 ARG ARG A . n 
A 1 2983 SER 2983 2983 2983 SER SER A . n 
A 1 2984 GLY 2984 2984 2984 GLY GLY A . n 
A 1 2985 CYS 2985 2985 2985 CYS CYS A . n 
A 1 2986 LYS 2986 2986 2986 LYS LYS A . n 
A 1 2987 ASN 2987 2987 2987 ASN ASN A . n 
A 1 2988 GLU 2988 2988 2988 GLU GLU A . n 
A 1 2989 LYS 2989 2989 2989 LYS LYS A . n 
A 1 2990 ILE 2990 2990 2990 ILE ILE A . n 
A 1 2991 ALA 2991 2991 2991 ALA ALA A . n 
A 1 2992 PHE 2992 2992 2992 PHE PHE A . n 
A 1 2993 ILE 2993 2993 2993 ILE ILE A . n 
A 1 2994 MET 2994 2994 2994 MET MET A . n 
A 1 2995 ASP 2995 2995 2995 ASP ASP A . n 
A 1 2996 GLU 2996 2996 2996 GLU GLU A . n 
A 1 2997 SER 2997 2997 2997 SER SER A . n 
A 1 2998 ASN 2998 2998 2998 ASN ASN A . n 
A 1 2999 VAL 2999 2999 2999 VAL VAL A . n 
A 1 3000 LEU 3000 3000 3000 LEU LEU A . n 
A 1 3001 ASP 3001 3001 3001 ASP ASP A . n 
A 1 3002 SER 3002 3002 3002 SER SER A . n 
A 1 3003 GLY 3003 3003 3003 GLY GLY A . n 
A 1 3004 PHE 3004 3004 3004 PHE PHE A . n 
A 1 3005 LEU 3005 3005 3005 LEU LEU A . n 
A 1 3006 GLU 3006 3006 3006 GLU GLU A . n 
A 1 3007 ARG 3007 3007 3007 ARG ARG A . n 
A 1 3008 MET 3008 3008 3008 MET MET A . n 
A 1 3009 ASN 3009 3009 3009 ASN ASN A . n 
A 1 3010 THR 3010 3010 3010 THR THR A . n 
A 1 3011 LEU 3011 3011 3011 LEU LEU A . n 
A 1 3012 LEU 3012 3012 3012 LEU LEU A . n 
A 1 3013 ALA 3013 3013 3013 ALA ALA A . n 
A 1 3014 ASN 3014 3014 3014 ASN ASN A . n 
A 1 3015 GLY 3015 3015 3015 GLY GLY A . n 
A 1 3016 GLU 3016 3016 3016 GLU GLU A . n 
A 1 3017 VAL 3017 3017 3017 VAL VAL A . n 
A 1 3018 PRO 3018 3018 3018 PRO PRO A . n 
A 1 3019 GLY 3019 3019 3019 GLY GLY A . n 
A 1 3020 LEU 3020 3020 3020 LEU LEU A . n 
A 1 3021 PHE 3021 3021 3021 PHE PHE A . n 
A 1 3022 GLU 3022 3022 3022 GLU GLU A . n 
A 1 3023 GLY 3023 3023 3023 GLY GLY A . n 
A 1 3024 ASP 3024 3024 3024 ASP ASP A . n 
A 1 3025 GLU 3025 3025 3025 GLU GLU A . n 
A 1 3026 TYR 3026 3026 3026 TYR TYR A . n 
A 1 3027 ALA 3027 3027 3027 ALA ALA A . n 
A 1 3028 THR 3028 3028 3028 THR THR A . n 
A 1 3029 LEU 3029 3029 3029 LEU LEU A . n 
A 1 3030 MET 3030 3030 3030 MET MET A . n 
A 1 3031 THR 3031 3031 3031 THR THR A . n 
A 1 3032 GLN 3032 3032 3032 GLN GLN A . n 
A 1 3033 CYS 3033 3033 3033 CYS CYS A . n 
A 1 3034 LYS 3034 3034 3034 LYS LYS A . n 
A 1 3035 GLU 3035 3035 3035 GLU GLU A . n 
A 1 3036 GLY 3036 3036 3036 GLY GLY A . n 
A 1 3037 ALA 3037 3037 3037 ALA ALA A . n 
A 1 3038 GLN 3038 3038 3038 GLN GLN A . n 
A 1 3039 LYS 3039 3039 3039 LYS LYS A . n 
A 1 3040 GLU 3040 3040 3040 GLU GLU A . n 
A 1 3041 GLY 3041 3041 3041 GLY GLY A . n 
A 1 3042 LEU 3042 3042 3042 LEU LEU A . n 
A 1 3043 MET 3043 3043 3043 MET MET A . n 
A 1 3044 LEU 3044 3044 3044 LEU LEU A . n 
A 1 3045 ASP 3045 3045 3045 ASP ASP A . n 
A 1 3046 SER 3046 3046 3046 SER SER A . n 
A 1 3047 HIS 3047 3047 3047 HIS HIS A . n 
A 1 3048 GLU 3048 3048 3048 GLU GLU A . n 
A 1 3049 GLU 3049 3049 3049 GLU GLU A . n 
A 1 3050 LEU 3050 3050 3050 LEU LEU A . n 
A 1 3051 TYR 3051 3051 3051 TYR TYR A . n 
A 1 3052 LYS 3052 3052 3052 LYS LYS A . n 
A 1 3053 TRP 3053 3053 3053 TRP TRP A . n 
A 1 3054 PHE 3054 3054 3054 PHE PHE A . n 
A 1 3055 THR 3055 3055 3055 THR THR A . n 
A 1 3056 SER 3056 3056 3056 SER SER A . n 
A 1 3057 GLN 3057 3057 3057 GLN GLN A . n 
A 1 3058 VAL 3058 3058 3058 VAL VAL A . n 
A 1 3059 ILE 3059 3059 3059 ILE ILE A . n 
A 1 3060 ARG 3060 3060 3060 ARG ARG A . n 
A 1 3061 ASN 3061 3061 3061 ASN ASN A . n 
A 1 3062 LEU 3062 3062 3062 LEU LEU A . n 
A 1 3063 HIS 3063 3063 3063 HIS HIS A . n 
A 1 3064 VAL 3064 3064 3064 VAL VAL A . n 
A 1 3065 VAL 3065 3065 3065 VAL VAL A . n 
A 1 3066 PHE 3066 3066 3066 PHE PHE A . n 
A 1 3067 THR 3067 3067 3067 THR THR A . n 
A 1 3068 MET 3068 3068 3068 MET MET A . n 
A 1 3069 ASN 3069 3069 3069 ASN ASN A . n 
A 1 3070 PRO 3070 3070 3070 PRO PRO A . n 
A 1 3071 SER 3071 3071 ?    ?   ?   A . n 
A 1 3072 SER 3072 3072 ?    ?   ?   A . n 
A 1 3073 GLU 3073 3073 ?    ?   ?   A . n 
A 1 3074 GLY 3074 3074 ?    ?   ?   A . n 
A 1 3075 LEU 3075 3075 ?    ?   ?   A . n 
A 1 3076 LYS 3076 3076 ?    ?   ?   A . n 
A 1 3077 ASP 3077 3077 ?    ?   ?   A . n 
A 1 3078 ARG 3078 3078 ?    ?   ?   A . n 
A 1 3079 ALA 3079 3079 ?    ?   ?   A . n 
A 1 3080 ALA 3080 3080 3080 ALA ALA A . n 
A 1 3081 THR 3081 3081 3081 THR THR A . n 
A 1 3082 SER 3082 3082 3082 SER SER A . n 
A 1 3083 PRO 3083 3083 3083 PRO PRO A . n 
A 1 3084 ALA 3084 3084 3084 ALA ALA A . n 
A 1 3085 LEU 3085 3085 3085 LEU LEU A . n 
A 1 3086 PHE 3086 3086 3086 PHE PHE A . n 
A 1 3087 ASN 3087 3087 3087 ASN ASN A . n 
A 1 3088 ARG 3088 3088 3088 ARG ARG A . n 
A 1 3089 CYS 3089 3089 3089 CYS CYS A . n 
A 1 3090 VAL 3090 3090 3090 VAL VAL A . n 
A 1 3091 LEU 3091 3091 3091 LEU LEU A . n 
A 1 3092 ASN 3092 3092 3092 ASN ASN A . n 
A 1 3093 TRP 3093 3093 3093 TRP TRP A . n 
A 1 3094 PHE 3094 3094 3094 PHE PHE A . n 
A 1 3095 GLY 3095 3095 3095 GLY GLY A . n 
A 1 3096 ASP 3096 3096 3096 ASP ASP A . n 
A 1 3097 TRP 3097 3097 3097 TRP TRP A . n 
A 1 3098 SER 3098 3098 3098 SER SER A . n 
A 1 3099 THR 3099 3099 3099 THR THR A . n 
A 1 3100 GLU 3100 3100 3100 GLU GLU A . n 
A 1 3101 ALA 3101 3101 3101 ALA ALA A . n 
A 1 3102 LEU 3102 3102 3102 LEU LEU A . n 
A 1 3103 TYR 3103 3103 3103 TYR TYR A . n 
A 1 3104 GLN 3104 3104 3104 GLN GLN A . n 
A 1 3105 VAL 3105 3105 3105 VAL VAL A . n 
A 1 3106 GLY 3106 3106 3106 GLY GLY A . n 
A 1 3107 LYS 3107 3107 3107 LYS LYS A . n 
A 1 3108 GLU 3108 3108 3108 GLU GLU A . n 
A 1 3109 PHE 3109 3109 3109 PHE PHE A . n 
A 1 3110 THR 3110 3110 3110 THR THR A . n 
A 1 3111 SER 3111 3111 3111 SER SER A . n 
A 1 3112 LYS 3112 3112 3112 LYS LYS A . n 
A 1 3113 MET 3113 3113 3113 MET MET A . n 
A 1 3114 ASP 3114 3114 3114 ASP ASP A . n 
A 1 3115 LEU 3115 3115 3115 LEU LEU A . n 
A 1 3116 GLU 3116 3116 3116 GLU GLU A . n 
A 1 3117 LYS 3117 3117 3117 LYS LYS A . n 
A 1 3118 PRO 3118 3118 3118 PRO PRO A . n 
A 1 3119 ASN 3119 3119 3119 ASN ASN A . n 
A 1 3120 TYR 3120 3120 3120 TYR TYR A . n 
A 1 3121 ILE 3121 3121 3121 ILE ILE A . n 
A 1 3122 VAL 3122 3122 3122 VAL VAL A . n 
A 1 3123 PRO 3123 3123 3123 PRO PRO A . n 
A 1 3124 ASP 3124 3124 3124 ASP ASP A . n 
A 1 3125 TYR 3125 3125 3125 TYR TYR A . n 
A 1 3126 MET 3126 3126 3126 MET MET A . n 
A 1 3127 PRO 3127 3127 3127 PRO PRO A . n 
A 1 3128 VAL 3128 3128 3128 VAL VAL A . n 
A 1 3129 VAL 3129 3129 3129 VAL VAL A . n 
A 1 3130 TYR 3130 3130 3130 TYR TYR A . n 
A 1 3131 ASP 3131 3131 3131 ASP ASP A . n 
A 1 3132 LYS 3132 3132 3132 LYS LYS A . n 
A 1 3133 LEU 3133 3133 3133 LEU LEU A . n 
A 1 3134 PRO 3134 3134 3134 PRO PRO A . n 
A 1 3135 GLN 3135 3135 3135 GLN GLN A . n 
A 1 3136 PRO 3136 3136 3136 PRO PRO A . n 
A 1 3137 PRO 3137 3137 3137 PRO PRO A . n 
A 1 3138 SER 3138 3138 3138 SER SER A . n 
A 1 3139 HIS 3139 3139 3139 HIS HIS A . n 
A 1 3140 ARG 3140 3140 3140 ARG ARG A . n 
A 1 3141 GLU 3141 3141 3141 GLU GLU A . n 
A 1 3142 ALA 3142 3142 3142 ALA ALA A . n 
A 1 3143 ILE 3143 3143 3143 ILE ILE A . n 
A 1 3144 VAL 3144 3144 3144 VAL VAL A . n 
A 1 3145 ASN 3145 3145 3145 ASN ASN A . n 
A 1 3146 SER 3146 3146 3146 SER SER A . n 
A 1 3147 CYS 3147 3147 3147 CYS CYS A . n 
A 1 3148 VAL 3148 3148 3148 VAL VAL A . n 
A 1 3149 PHE 3149 3149 3149 PHE PHE A . n 
A 1 3150 VAL 3150 3150 3150 VAL VAL A . n 
A 1 3151 HIS 3151 3151 3151 HIS HIS A . n 
A 1 3152 GLN 3152 3152 3152 GLN GLN A . n 
A 1 3153 THR 3153 3153 3153 THR THR A . n 
A 1 3154 LEU 3154 3154 3154 LEU LEU A . n 
A 1 3155 HIS 3155 3155 3155 HIS HIS A . n 
A 1 3156 GLN 3156 3156 3156 GLN GLN A . n 
A 1 3157 ALA 3157 3157 3157 ALA ALA A . n 
A 1 3158 ASN 3158 3158 3158 ASN ASN A . n 
A 1 3159 ALA 3159 3159 3159 ALA ALA A . n 
A 1 3160 ARG 3160 3160 3160 ARG ARG A . n 
A 1 3161 LEU 3161 3161 3161 LEU LEU A . n 
A 1 3162 ALA 3162 3162 3162 ALA ALA A . n 
A 1 3163 LYS 3163 3163 3163 LYS LYS A . n 
A 1 3164 ARG 3164 3164 3164 ARG ARG A . n 
A 1 3165 GLY 3165 3165 3165 GLY GLY A . n 
A 1 3166 GLY 3166 3166 3166 GLY GLY A . n 
A 1 3167 ARG 3167 3167 3167 ARG ARG A . n 
A 1 3168 THR 3168 3168 3168 THR THR A . n 
A 1 3169 MET 3169 3169 3169 MET MET A . n 
A 1 3170 ALA 3170 3170 3170 ALA ALA A . n 
A 1 3171 ILE 3171 3171 3171 ILE ILE A . n 
A 1 3172 THR 3172 3172 3172 THR THR A . n 
A 1 3173 PRO 3173 3173 3173 PRO PRO A . n 
A 1 3174 ARG 3174 3174 3174 ARG ARG A . n 
A 1 3175 HIS 3175 3175 3175 HIS HIS A . n 
A 1 3176 TYR 3176 3176 3176 TYR TYR A . n 
A 1 3177 LEU 3177 3177 3177 LEU LEU A . n 
A 1 3178 ASP 3178 3178 3178 ASP ASP A . n 
A 1 3179 PHE 3179 3179 3179 PHE PHE A . n 
A 1 3180 ILE 3180 3180 3180 ILE ILE A . n 
A 1 3181 ASN 3181 3181 3181 ASN ASN A . n 
A 1 3182 HIS 3182 3182 3182 HIS HIS A . n 
A 1 3183 TYR 3183 3183 3183 TYR TYR A . n 
A 1 3184 ALA 3184 3184 3184 ALA ALA A . n 
A 1 3185 ASN 3185 3185 3185 ASN ASN A . n 
A 1 3186 LEU 3186 3186 3186 LEU LEU A . n 
A 1 3187 PHE 3187 3187 3187 PHE PHE A . n 
A 1 3188 HIS 3188 3188 3188 HIS HIS A . n 
A 1 3189 GLU 3189 3189 3189 GLU GLU A . n 
A 1 3190 LYS 3190 3190 3190 LYS LYS A . n 
A 1 3191 ARG 3191 3191 3191 ARG ARG A . n 
A 1 3192 SER 3192 3192 3192 SER SER A . n 
A 1 3193 GLU 3193 3193 3193 GLU GLU A . n 
A 1 3194 LEU 3194 3194 3194 LEU LEU A . n 
A 1 3195 GLU 3195 3195 3195 GLU GLU A . n 
A 1 3196 GLU 3196 3196 3196 GLU GLU A . n 
A 1 3197 GLN 3197 3197 3197 GLN GLN A . n 
A 1 3198 GLN 3198 3198 3198 GLN GLN A . n 
A 1 3199 MET 3199 3199 3199 MET MET A . n 
A 1 3200 HIS 3200 3200 3200 HIS HIS A . n 
A 1 3201 LEU 3201 3201 3201 LEU LEU A . n 
A 1 3202 ASN 3202 3202 3202 ASN ASN A . n 
A 1 3203 VAL 3203 3203 3203 VAL VAL A . n 
A 1 3204 GLY 3204 3204 3204 GLY GLY A . n 
A 1 3205 LEU 3205 3205 3205 LEU LEU A . n 
A 1 3206 ARG 3206 3206 3206 ARG ARG A . n 
A 1 3207 LYS 3207 3207 3207 LYS LYS A . n 
A 1 3208 ILE 3208 3208 3208 ILE ILE A . n 
A 1 3209 LYS 3209 3209 3209 LYS LYS A . n 
A 1 3210 GLU 3210 3210 3210 GLU GLU A . n 
A 1 3211 THR 3211 3211 3211 THR THR A . n 
A 1 3212 VAL 3212 3212 3212 VAL VAL A . n 
A 1 3213 ASP 3213 3213 3213 ASP ASP A . n 
A 1 3214 GLN 3214 3214 3214 GLN GLN A . n 
A 1 3215 VAL 3215 3215 3215 VAL VAL A . n 
A 1 3216 GLU 3216 3216 3216 GLU GLU A . n 
A 1 3217 GLU 3217 3217 3217 GLU GLU A . n 
A 1 3218 LEU 3218 3218 3218 LEU LEU A . n 
A 1 3219 ARG 3219 3219 3219 ARG ARG A . n 
A 1 3220 ARG 3220 3220 3220 ARG ARG A . n 
A 1 3221 ASP 3221 3221 3221 ASP ASP A . n 
A 1 3222 LEU 3222 3222 ?    ?   ?   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 3470 ALA ALA A . n 
A 1 3471 LYS 3471 3471 3471 LYS LYS A . n 
A 1 3472 VAL 3472 3472 3472 VAL VAL A . n 
A 1 3473 ASN 3473 3473 3473 ASN ASN A . n 
A 1 3474 ARG 3474 3474 3474 ARG ARG A . n 
A 1 3475 SER 3475 3475 3475 SER SER A . n 
A 1 3476 THR 3476 3476 3476 THR THR A . n 
A 1 3477 ALA 3477 3477 3477 ALA ALA A . n 
A 1 3478 LEU 3478 3478 3478 LEU LEU A . n 
A 1 3479 LEU 3479 3479 3479 LEU LEU A . n 
A 1 3480 LYS 3480 3480 3480 LYS LYS A . n 
A 1 3481 SER 3481 3481 3481 SER SER A . n 
A 1 3482 LEU 3482 3482 3482 LEU LEU A . n 
A 1 3483 SER 3483 3483 3483 SER SER A . n 
A 1 3484 ALA 3484 3484 3484 ALA ALA A . n 
A 1 3485 GLU 3485 3485 3485 GLU GLU A . n 
A 1 3486 ARG 3486 3486 3486 ARG ARG A . n 
A 1 3487 GLU 3487 3487 3487 GLU GLU A . n 
A 1 3488 ARG 3488 3488 3488 ARG ARG A . n 
A 1 3489 TRP 3489 3489 3489 TRP TRP A . n 
A 1 3490 GLU 3490 3490 3490 GLU GLU A . n 
A 1 3491 LYS 3491 3491 3491 LYS LYS A . n 
A 1 3492 THR 3492 3492 3492 THR THR A . n 
A 1 3493 SER 3493 3493 3493 SER SER A . n 
A 1 3494 GLU 3494 3494 3494 GLU GLU A . n 
A 1 3495 THR 3495 3495 3495 THR THR A . n 
A 1 3496 PHE 3496 3496 3496 PHE PHE A . n 
A 1 3497 LYS 3497 3497 3497 LYS LYS A . n 
A 1 3498 ASN 3498 3498 3498 ASN ASN A . n 
A 1 3499 GLN 3499 3499 3499 GLN GLN A . n 
A 1 3500 MET 3500 3500 3500 MET MET A . n 
A 1 3501 SER 3501 3501 3501 SER SER A . n 
A 1 3502 THR 3502 3502 3502 THR THR A . n 
A 1 3503 ILE 3503 3503 3503 ILE ILE A . n 
A 1 3504 ALA 3504 3504 3504 ALA ALA A . n 
A 1 3505 GLY 3505 3505 3505 GLY GLY A . n 
A 1 3506 ASP 3506 3506 3506 ASP ASP A . n 
A 1 3507 CYS 3507 3507 3507 CYS CYS A . n 
A 1 3508 LEU 3508 3508 3508 LEU LEU A . n 
A 1 3509 LEU 3509 3509 3509 LEU LEU A . n 
A 1 3510 SER 3510 3510 3510 SER SER A . n 
A 1 3511 ALA 3511 3511 3511 ALA ALA A . n 
A 1 3512 ALA 3512 3512 3512 ALA ALA A . n 
A 1 3513 PHE 3513 3513 3513 PHE PHE A . n 
A 1 3514 ILE 3514 3514 3514 ILE ILE A . n 
A 1 3515 ALA 3515 3515 3515 ALA ALA A . n 
A 1 3516 TYR 3516 3516 3516 TYR TYR A . n 
A 1 3517 ALA 3517 3517 3517 ALA ALA A . n 
A 1 3518 GLY 3518 3518 3518 GLY GLY A . n 
A 1 3519 TYR 3519 3519 3519 TYR TYR A . n 
A 1 3520 PHE 3520 3520 3520 PHE PHE A . n 
A 1 3521 ASP 3521 3521 3521 ASP ASP A . n 
A 1 3522 GLN 3522 3522 3522 GLN GLN A . n 
A 1 3523 GLN 3523 3523 3523 GLN GLN A . n 
A 1 3524 MET 3524 3524 3524 MET MET A . n 
A 1 3525 ARG 3525 3525 3525 ARG ARG A . n 
A 1 3526 GLN 3526 3526 3526 GLN GLN A . n 
A 1 3527 ASN 3527 3527 3527 ASN ASN A . n 
A 1 3528 LEU 3528 3528 3528 LEU LEU A . n 
A 1 3529 PHE 3529 3529 3529 PHE PHE A . n 
A 1 3530 THR 3530 3530 3530 THR THR A . n 
A 1 3531 THR 3531 3531 3531 THR THR A . n 
A 1 3532 TRP 3532 3532 3532 TRP TRP A . n 
A 1 3533 SER 3533 3533 3533 SER SER A . n 
A 1 3534 HIS 3534 3534 3534 HIS HIS A . n 
A 1 3535 HIS 3535 3535 3535 HIS HIS A . n 
A 1 3536 LEU 3536 3536 3536 LEU LEU A . n 
A 1 3537 GLN 3537 3537 3537 GLN GLN A . n 
A 1 3538 GLN 3538 3538 3538 GLN GLN A . n 
A 1 3539 ALA 3539 3539 3539 ALA ALA A . n 
A 1 3540 ASN 3540 3540 3540 ASN ASN A . n 
A 1 3541 ILE 3541 3541 3541 ILE ILE A . n 
A 1 3542 GLN 3542 3542 3542 GLN GLN A . n 
A 1 3543 PHE 3543 3543 3543 PHE PHE A . n 
A 1 3544 ARG 3544 3544 3544 ARG ARG A . n 
A 1 3545 THR 3545 3545 3545 THR THR A . n 
A 1 3546 ASP 3546 3546 3546 ASP ASP A . n 
A 1 3547 ILE 3547 3547 3547 ILE ILE A . n 
A 1 3548 ALA 3548 3548 3548 ALA ALA A . n 
A 1 3549 ARG 3549 3549 3549 ARG ARG A . n 
A 1 3550 THR 3550 3550 3550 THR THR A . n 
A 1 3551 GLU 3551 3551 3551 GLU GLU A . n 
A 1 3552 TYR 3552 3552 3552 TYR TYR A . n 
A 1 3553 LEU 3553 3553 3553 LEU LEU A . n 
A 1 3554 SER 3554 3554 3554 SER SER A . n 
A 1 3555 ASN 3555 3555 3555 ASN ASN A . n 
A 1 3556 ALA 3556 3556 3556 ALA ALA A . n 
A 1 3557 ASP 3557 3557 3557 ASP ASP A . n 
A 1 3558 GLU 3558 3558 3558 GLU GLU A . n 
A 1 3559 ARG 3559 3559 3559 ARG ARG A . n 
A 1 3560 LEU 3560 3560 3560 LEU LEU A . n 
A 1 3561 ARG 3561 3561 3561 ARG ARG A . n 
A 1 3562 TRP 3562 3562 3562 TRP TRP A . n 
A 1 3563 GLN 3563 3563 3563 GLN GLN A . n 
A 1 3564 ALA 3564 3564 3564 ALA ALA A . n 
A 1 3565 SER 3565 3565 3565 SER SER A . n 
A 1 3566 SER 3566 3566 3566 SER SER A . n 
A 1 3567 LEU 3567 3567 3567 LEU LEU A . n 
A 1 3568 PRO 3568 3568 3568 PRO PRO A . n 
A 1 3569 ALA 3569 3569 3569 ALA ALA A . n 
A 1 3570 ASP 3570 3570 3570 ASP ASP A . n 
A 1 3571 ASP 3571 3571 3571 ASP ASP A . n 
A 1 3572 LEU 3572 3572 3572 LEU LEU A . n 
A 1 3573 CYS 3573 3573 3573 CYS CYS A . n 
A 1 3574 THR 3574 3574 3574 THR THR A . n 
A 1 3575 GLU 3575 3575 3575 GLU GLU A . n 
A 1 3576 ASN 3576 3576 3576 ASN ASN A . n 
A 1 3577 ALA 3577 3577 3577 ALA ALA A . n 
A 1 3578 ILE 3578 3578 3578 ILE ILE A . n 
A 1 3579 MET 3579 3579 3579 MET MET A . n 
A 1 3580 LEU 3580 3580 3580 LEU LEU A . n 
A 1 3581 LYS 3581 3581 3581 LYS LYS A . n 
A 1 3582 ARG 3582 3582 3582 ARG ARG A . n 
A 1 3583 PHE 3583 3583 3583 PHE PHE A . n 
A 1 3584 ASN 3584 3584 3584 ASN ASN A . n 
A 1 3585 ARG 3585 3585 3585 ARG ARG A . n 
A 1 3586 TYR 3586 3586 3586 TYR TYR A . n 
A 1 3587 PRO 3587 3587 3587 PRO PRO A . n 
A 1 3588 LEU 3588 3588 3588 LEU LEU A . n 
A 1 3589 ILE 3589 3589 3589 ILE ILE A . n 
A 1 3590 ILE 3590 3590 3590 ILE ILE A . n 
A 1 3591 ASP 3591 3591 3591 ASP ASP A . n 
A 1 3592 PRO 3592 3592 3592 PRO PRO A . n 
A 1 3593 SER 3593 3593 3593 SER SER A . n 
A 1 3594 GLY 3594 3594 3594 GLY GLY A . n 
A 1 3595 GLN 3595 3595 3595 GLN GLN A . n 
A 1 3596 ALA 3596 3596 3596 ALA ALA A . n 
A 1 3597 THR 3597 3597 3597 THR THR A . n 
A 1 3598 GLU 3598 3598 3598 GLU GLU A . n 
A 1 3599 PHE 3599 3599 3599 PHE PHE A . n 
A 1 3600 ILE 3600 3600 3600 ILE ILE A . n 
A 1 3601 MET 3601 3601 3601 MET MET A . n 
A 1 3602 ASN 3602 3602 3602 ASN ASN A . n 
A 1 3603 GLU 3603 3603 3603 GLU GLU A . n 
A 1 3604 TYR 3604 3604 3604 TYR TYR A . n 
A 1 3605 LYS 3605 3605 3605 LYS LYS A . n 
A 1 3606 ASP 3606 3606 3606 ASP ASP A . n 
A 1 3607 ARG 3607 3607 3607 ARG ARG A . n 
A 1 3608 LYS 3608 3608 3608 LYS LYS A . n 
A 1 3609 ILE 3609 3609 3609 ILE ILE A . n 
A 1 3610 THR 3610 3610 3610 THR THR A . n 
A 1 3611 ARG 3611 3611 3611 ARG ARG A . n 
A 1 3612 THR 3612 3612 3612 THR THR A . n 
A 1 3613 SER 3613 3613 3613 SER SER A . n 
A 1 3614 PHE 3614 3614 3614 PHE PHE A . n 
A 1 3615 LEU 3615 3615 3615 LEU LEU A . n 
A 1 3616 ASP 3616 3616 3616 ASP ASP A . n 
A 1 3617 ASP 3617 3617 3617 ASP ASP A . n 
A 1 3618 ALA 3618 3618 3618 ALA ALA A . n 
A 1 3619 PHE 3619 3619 3619 PHE PHE A . n 
A 1 3620 ARG 3620 3620 3620 ARG ARG A . n 
A 1 3621 LYS 3621 3621 3621 LYS LYS A . n 
A 1 3622 ASN 3622 3622 3622 ASN ASN A . n 
A 1 3623 LEU 3623 3623 3623 LEU LEU A . n 
A 1 3624 GLU 3624 3624 3624 GLU GLU A . n 
A 1 3625 SER 3625 3625 3625 SER SER A . n 
A 1 3626 ALA 3626 3626 3626 ALA ALA A . n 
A 1 3627 LEU 3627 3627 3627 LEU LEU A . n 
A 1 3628 ARG 3628 3628 3628 ARG ARG A . n 
A 1 3629 PHE 3629 3629 3629 PHE PHE A . n 
A 1 3630 GLY 3630 3630 3630 GLY GLY A . n 
A 1 3631 ASN 3631 3631 3631 ASN ASN A . n 
A 1 3632 PRO 3632 3632 3632 PRO PRO A . n 
A 1 3633 LEU 3633 3633 3633 LEU LEU A . n 
A 1 3634 LEU 3634 3634 3634 LEU LEU A . n 
A 1 3635 VAL 3635 3635 3635 VAL VAL A . n 
A 1 3636 GLN 3636 3636 3636 GLN GLN A . n 
A 1 3637 ASP 3637 3637 3637 ASP ASP A . n 
A 1 3638 VAL 3638 3638 3638 VAL VAL A . n 
A 1 3639 GLU 3639 3639 3639 GLU GLU A . n 
A 1 3640 SER 3640 3640 3640 SER SER A . n 
A 1 3641 TYR 3641 3641 3641 TYR TYR A . n 
A 1 3642 ASP 3642 3642 3642 ASP ASP A . n 
A 1 3643 PRO 3643 3643 3643 PRO PRO A . n 
A 1 3644 VAL 3644 3644 3644 VAL VAL A . n 
A 1 3645 LEU 3645 3645 3645 LEU LEU A . n 
A 1 3646 ASN 3646 3646 3646 ASN ASN A . n 
A 1 3647 PRO 3647 3647 3647 PRO PRO A . n 
A 1 3648 VAL 3648 3648 3648 VAL VAL A . n 
A 1 3649 LEU 3649 3649 3649 LEU LEU A . n 
A 1 3650 ASN 3650 3650 3650 ASN ASN A . n 
A 1 3651 ARG 3651 3651 3651 ARG ARG A . n 
A 1 3652 GLU 3652 3652 3652 GLU GLU A . n 
A 1 3653 VAL 3653 3653 3653 VAL VAL A . n 
A 1 3654 ARG 3654 3654 3654 ARG ARG A . n 
A 1 3655 ARG 3655 3655 3655 ARG ARG A . n 
A 1 3656 THR 3656 3656 3656 THR THR A . n 
A 1 3657 GLY 3657 3657 3657 GLY GLY A . n 
A 1 3658 GLY 3658 3658 3658 GLY GLY A . n 
A 1 3659 ARG 3659 3659 3659 ARG ARG A . n 
A 1 3660 VAL 3660 3660 3660 VAL VAL A . n 
A 1 3661 LEU 3661 3661 3661 LEU LEU A . n 
A 1 3662 ILE 3662 3662 3662 ILE ILE A . n 
A 1 3663 THR 3663 3663 3663 THR THR A . n 
A 1 3664 LEU 3664 3664 3664 LEU LEU A . n 
A 1 3665 GLY 3665 3665 3665 GLY GLY A . n 
A 1 3666 ASP 3666 3666 3666 ASP ASP A . n 
A 1 3667 GLN 3667 3667 3667 GLN GLN A . n 
A 1 3668 ASP 3668 3668 3668 ASP ASP A . n 
A 1 3669 ILE 3669 3669 3669 ILE ILE A . n 
A 1 3670 ASP 3670 3670 3670 ASP ASP A . n 
A 1 3671 LEU 3671 3671 3671 LEU LEU A . n 
A 1 3672 SER 3672 3672 3672 SER SER A . n 
A 1 3673 PRO 3673 3673 3673 PRO PRO A . n 
A 1 3674 SER 3674 3674 3674 SER SER A . n 
A 1 3675 PHE 3675 3675 3675 PHE PHE A . n 
A 1 3676 VAL 3676 3676 3676 VAL VAL A . n 
A 1 3677 ILE 3677 3677 3677 ILE ILE A . n 
A 1 3678 PHE 3678 3678 3678 PHE PHE A . n 
A 1 3679 LEU 3679 3679 3679 LEU LEU A . n 
A 1 3680 SER 3680 3680 3680 SER SER A . n 
A 1 3681 THR 3681 3681 3681 THR THR A . n 
A 1 3682 ARG 3682 3682 3682 ARG ARG A . n 
A 1 3683 ASP 3683 3683 3683 ASP ASP A . n 
A 1 3684 PRO 3684 3684 3684 PRO PRO A . n 
A 1 3685 THR 3685 3685 3685 THR THR A . n 
A 1 3686 VAL 3686 3686 3686 VAL VAL A . n 
A 1 3687 GLU 3687 3687 3687 GLU GLU A . n 
A 1 3688 PHE 3688 3688 3688 PHE PHE A . n 
A 1 3689 PRO 3689 3689 3689 PRO PRO A . n 
A 1 3690 PRO 3690 3690 3690 PRO PRO A . n 
A 1 3691 ASP 3691 3691 3691 ASP ASP A . n 
A 1 3692 LEU 3692 3692 3692 LEU LEU A . n 
A 1 3693 CYS 3693 3693 3693 CYS CYS A . n 
A 1 3694 SER 3694 3694 3694 SER SER A . n 
A 1 3695 ARG 3695 3695 3695 ARG ARG A . n 
A 1 3696 VAL 3696 3696 3696 VAL VAL A . n 
A 1 3697 THR 3697 3697 3697 THR THR A . n 
A 1 3698 PHE 3698 3698 3698 PHE PHE A . n 
A 1 3699 VAL 3699 3699 3699 VAL VAL A . n 
A 1 3700 ASN 3700 3700 3700 ASN ASN A . n 
A 1 3701 PHE 3701 3701 3701 PHE PHE A . n 
A 1 3702 THR 3702 3702 3702 THR THR A . n 
A 1 3703 VAL 3703 3703 3703 VAL VAL A . n 
A 1 3704 THR 3704 3704 3704 THR THR A . n 
A 1 3705 ARG 3705 3705 3705 ARG ARG A . n 
A 1 3706 SER 3706 3706 3706 SER SER A . n 
A 1 3707 SER 3707 3707 3707 SER SER A . n 
A 1 3708 LEU 3708 3708 3708 LEU LEU A . n 
A 1 3709 GLN 3709 3709 3709 GLN GLN A . n 
A 1 3710 SER 3710 3710 3710 SER SER A . n 
A 1 3711 GLN 3711 3711 3711 GLN GLN A . n 
A 1 3712 CYS 3712 3712 3712 CYS CYS A . n 
A 1 3713 LEU 3713 3713 3713 LEU LEU A . n 
A 1 3714 ASN 3714 3714 3714 ASN ASN A . n 
A 1 3715 GLU 3715 3715 3715 GLU GLU A . n 
A 1 3716 VAL 3716 3716 3716 VAL VAL A . n 
A 1 3717 LEU 3717 3717 3717 LEU LEU A . n 
A 1 3718 LYS 3718 3718 3718 LYS LYS A . n 
A 1 3719 ALA 3719 3719 3719 ALA ALA A . n 
A 1 3720 GLU 3720 3720 3720 GLU GLU A . n 
A 1 3721 ARG 3721 3721 3721 ARG ARG A . n 
A 1 3722 PRO 3722 3722 3722 PRO PRO A . n 
A 1 3723 ASP 3723 3723 3723 ASP ASP A . n 
A 1 3724 VAL 3724 3724 3724 VAL VAL A . n 
A 1 3725 ASP 3725 3725 3725 ASP ASP A . n 
A 1 3726 GLU 3726 3726 3726 GLU GLU A . n 
A 1 3727 LYS 3727 3727 3727 LYS LYS A . n 
A 1 3728 ARG 3728 3728 3728 ARG ARG A . n 
A 1 3729 SER 3729 3729 3729 SER SER A . n 
A 1 3730 ASP 3730 3730 3730 ASP ASP A . n 
A 1 3731 LEU 3731 3731 3731 LEU LEU A . n 
A 1 3732 LEU 3732 3732 3732 LEU LEU A . n 
A 1 3733 LYS 3733 3733 3733 LYS LYS A . n 
A 1 3734 LEU 3734 3734 3734 LEU LEU A . n 
A 1 3735 GLN 3735 3735 3735 GLN GLN A . n 
A 1 3736 GLY 3736 3736 3736 GLY GLY A . n 
A 1 3737 GLU 3737 3737 3737 GLU GLU A . n 
A 1 3738 PHE 3738 3738 3738 PHE PHE A . n 
A 1 3739 GLN 3739 3739 3739 GLN GLN A . n 
A 1 3740 LEU 3740 3740 3740 LEU LEU A . n 
A 1 3741 ARG 3741 3741 3741 ARG ARG A . n 
A 1 3742 LEU 3742 3742 3742 LEU LEU A . n 
A 1 3743 ARG 3743 3743 3743 ARG ARG A . n 
A 1 3744 GLN 3744 3744 3744 GLN GLN A . n 
A 1 3745 LEU 3745 3745 3745 LEU LEU A . n 
A 1 3746 GLU 3746 3746 3746 GLU GLU A . n 
A 1 3747 LYS 3747 3747 3747 LYS LYS A . n 
A 1 3748 SER 3748 3748 3748 SER SER A . n 
A 1 3749 LEU 3749 3749 3749 LEU LEU A . n 
A 1 3750 LEU 3750 3750 3750 LEU LEU A . n 
A 1 3751 GLN 3751 3751 3751 GLN GLN A . n 
A 1 3752 ALA 3752 3752 3752 ALA ALA A . n 
A 1 3753 LEU 3753 3753 3753 LEU LEU A . n 
A 1 3754 ASN 3754 3754 3754 ASN ASN A . n 
A 1 3755 GLU 3755 3755 3755 GLU GLU A . n 
A 1 3756 VAL 3756 3756 3756 VAL VAL A . n 
A 1 3757 LYS 3757 3757 3757 LYS LYS A . n 
A 1 3758 GLY 3758 3758 3758 GLY GLY A . n 
A 1 3759 ARG 3759 3759 3759 ARG ARG A . n 
A 1 3760 ILE 3760 3760 3760 ILE ILE A . n 
A 1 3761 LEU 3761 3761 3761 LEU LEU A . n 
A 1 3762 ASP 3762 3762 3762 ASP ASP A . n 
A 1 3763 ASP 3763 3763 3763 ASP ASP A . n 
A 1 3764 ASP 3764 3764 3764 ASP ASP A . n 
A 1 3765 THR 3765 3765 3765 THR THR A . n 
A 1 3766 ILE 3766 3766 3766 ILE ILE A . n 
A 1 3767 ILE 3767 3767 3767 ILE ILE A . n 
A 1 3768 THR 3768 3768 3768 THR THR A . n 
A 1 3769 THR 3769 3769 3769 THR THR A . n 
A 1 3770 LEU 3770 3770 3770 LEU LEU A . n 
A 1 3771 GLU 3771 3771 3771 GLU GLU A . n 
A 1 3772 ASN 3772 3772 3772 ASN ASN A . n 
A 1 3773 LEU 3773 3773 3773 LEU LEU A . n 
A 1 3774 LYS 3774 3774 3774 LYS LYS A . n 
A 1 3775 ARG 3775 3775 3775 ARG ARG A . n 
A 1 3776 GLU 3776 3776 3776 GLU GLU A . n 
A 1 3777 ALA 3777 3777 3777 ALA ALA A . n 
A 1 3778 ALA 3778 3778 3778 ALA ALA A . n 
A 1 3779 GLU 3779 3779 3779 GLU GLU A . n 
A 1 3780 VAL 3780 3780 3780 VAL VAL A . n 
A 1 3781 THR 3781 3781 3781 THR THR A . n 
A 1 3782 ARG 3782 3782 3782 ARG ARG A . n 
A 1 3783 LYS 3783 3783 3783 LYS LYS A . n 
A 1 3784 VAL 3784 3784 3784 VAL VAL A . n 
A 1 3785 GLU 3785 3785 3785 GLU GLU A . n 
A 1 3786 GLU 3786 3786 3786 GLU GLU A . n 
A 1 3787 THR 3787 3787 3787 THR THR A . n 
A 1 3788 ASP 3788 3788 3788 ASP ASP A . n 
A 1 3789 ILE 3789 3789 3789 ILE ILE A . n 
A 1 3790 VAL 3790 3790 3790 VAL VAL A . n 
A 1 3791 MET 3791 3791 3791 MET MET A . n 
A 1 3792 GLN 3792 3792 3792 GLN GLN A . n 
A 1 3793 GLU 3793 3793 3793 GLU GLU A . n 
A 1 3794 VAL 3794 3794 3794 VAL VAL A . n 
A 1 3795 GLU 3795 3795 3795 GLU GLU A . n 
A 1 3796 THR 3796 3796 3796 THR THR A . n 
A 1 3797 VAL 3797 3797 3797 VAL VAL A . n 
A 1 3798 SER 3798 3798 3798 SER SER A . n 
A 1 3799 GLN 3799 3799 3799 GLN GLN A . n 
A 1 3800 GLN 3800 3800 3800 GLN GLN A . n 
A 1 3801 TYR 3801 3801 3801 TYR TYR A . n 
A 1 3802 LEU 3802 3802 3802 LEU LEU A . n 
A 1 3803 PRO 3803 3803 3803 PRO PRO A . n 
A 1 3804 LEU 3804 3804 3804 LEU LEU A . n 
A 1 3805 SER 3805 3805 3805 SER SER A . n 
A 1 3806 THR 3806 3806 3806 THR THR A . n 
A 1 3807 ALA 3807 3807 3807 ALA ALA A . n 
A 1 3808 CYS 3808 3808 3808 CYS CYS A . n 
A 1 3809 SER 3809 3809 3809 SER SER A . n 
A 1 3810 SER 3810 3810 3810 SER SER A . n 
A 1 3811 ILE 3811 3811 3811 ILE ILE A . n 
A 1 3812 TYR 3812 3812 3812 TYR TYR A . n 
A 1 3813 PHE 3813 3813 3813 PHE PHE A . n 
A 1 3814 THR 3814 3814 3814 THR THR A . n 
A 1 3815 MET 3815 3815 3815 MET MET A . n 
A 1 3816 GLU 3816 3816 3816 GLU GLU A . n 
A 1 3817 SER 3817 3817 3817 SER SER A . n 
A 1 3818 LEU 3818 3818 3818 LEU LEU A . n 
A 1 3819 LYS 3819 3819 3819 LYS LYS A . n 
A 1 3820 GLN 3820 3820 3820 GLN GLN A . n 
A 1 3821 ILE 3821 3821 3821 ILE ILE A . n 
A 1 3822 HIS 3822 3822 3822 HIS HIS A . n 
A 1 3823 PHE 3823 3823 3823 PHE PHE A . n 
A 1 3824 LEU 3824 3824 3824 LEU LEU A . n 
A 1 3825 TYR 3825 3825 3825 TYR TYR A . n 
A 1 3826 GLN 3826 3826 3826 GLN GLN A . n 
A 1 3827 TYR 3827 3827 3827 TYR TYR A . n 
A 1 3828 SER 3828 3828 3828 SER SER A . n 
A 1 3829 LEU 3829 3829 3829 LEU LEU A . n 
A 1 3830 GLN 3830 3830 3830 GLN GLN A . n 
A 1 3831 PHE 3831 3831 3831 PHE PHE A . n 
A 1 3832 PHE 3832 3832 3832 PHE PHE A . n 
A 1 3833 LEU 3833 3833 3833 LEU LEU A . n 
A 1 3834 ASP 3834 3834 3834 ASP ASP A . n 
A 1 3835 ILE 3835 3835 3835 ILE ILE A . n 
A 1 3836 TYR 3836 3836 3836 TYR TYR A . n 
A 1 3837 HIS 3837 3837 3837 HIS HIS A . n 
A 1 3838 ASN 3838 3838 3838 ASN ASN A . n 
A 1 3839 VAL 3839 3839 3839 VAL VAL A . n 
A 1 3840 LEU 3840 3840 3840 LEU LEU A . n 
A 1 3841 TYR 3841 3841 3841 TYR TYR A . n 
A 1 3842 GLU 3842 3842 3842 GLU GLU A . n 
A 1 3843 ASN 3843 3843 3843 ASN ASN A . n 
A 1 3844 PRO 3844 3844 3844 PRO PRO A . n 
A 1 3845 ASN 3845 3845 3845 ASN ASN A . n 
A 1 3846 LEU 3846 3846 3846 LEU LEU A . n 
A 1 3847 LYS 3847 3847 3847 LYS LYS A . n 
A 1 3848 GLY 3848 3848 3848 GLY GLY A . n 
A 1 3849 VAL 3849 3849 3849 VAL VAL A . n 
A 1 3850 THR 3850 3850 3850 THR THR A . n 
A 1 3851 ASP 3851 3851 3851 ASP ASP A . n 
A 1 3852 HIS 3852 3852 3852 HIS HIS A . n 
A 1 3853 THR 3853 3853 3853 THR THR A . n 
A 1 3854 GLN 3854 3854 3854 GLN GLN A . n 
A 1 3855 ARG 3855 3855 3855 ARG ARG A . n 
A 1 3856 LEU 3856 3856 3856 LEU LEU A . n 
A 1 3857 SER 3857 3857 3857 SER SER A . n 
A 1 3858 ILE 3858 3858 3858 ILE ILE A . n 
A 1 3859 ILE 3859 3859 3859 ILE ILE A . n 
A 1 3860 THR 3860 3860 3860 THR THR A . n 
A 1 3861 LYS 3861 3861 3861 LYS LYS A . n 
A 1 3862 ASP 3862 3862 3862 ASP ASP A . n 
A 1 3863 LEU 3863 3863 3863 LEU LEU A . n 
A 1 3864 PHE 3864 3864 3864 PHE PHE A . n 
A 1 3865 GLN 3865 3865 3865 GLN GLN A . n 
A 1 3866 VAL 3866 3866 3866 VAL VAL A . n 
A 1 3867 ALA 3867 3867 3867 ALA ALA A . n 
A 1 3868 PHE 3868 3868 3868 PHE PHE A . n 
A 1 3869 ASN 3869 3869 3869 ASN ASN A . n 
A 1 3870 ARG 3870 3870 3870 ARG ARG A . n 
A 1 3871 VAL 3871 3871 3871 VAL VAL A . n 
A 1 3872 ALA 3872 3872 3872 ALA ALA A . n 
A 1 3873 ARG 3873 3873 3873 ARG ARG A . n 
A 1 3874 GLY 3874 3874 3874 GLY GLY A . n 
A 1 3875 MET 3875 3875 3875 MET MET A . n 
A 1 3876 LEU 3876 3876 3876 LEU LEU A . n 
A 1 3877 HIS 3877 3877 3877 HIS HIS A . n 
A 1 3878 GLN 3878 3878 3878 GLN GLN A . n 
A 1 3879 ASP 3879 3879 3879 ASP ASP A . n 
A 1 3880 HIS 3880 3880 3880 HIS HIS A . n 
A 1 3881 ILE 3881 3881 3881 ILE ILE A . n 
A 1 3882 THR 3882 3882 3882 THR THR A . n 
A 1 3883 PHE 3883 3883 3883 PHE PHE A . n 
A 1 3884 ALA 3884 3884 3884 ALA ALA A . n 
A 1 3885 MET 3885 3885 3885 MET MET A . n 
A 1 3886 LEU 3886 3886 3886 LEU LEU A . n 
A 1 3887 LEU 3887 3887 3887 LEU LEU A . n 
A 1 3888 ALA 3888 3888 3888 ALA ALA A . n 
A 1 3889 ARG 3889 3889 3889 ARG ARG A . n 
A 1 3890 ILE 3890 3890 3890 ILE ILE A . n 
A 1 3891 LYS 3891 3891 3891 LYS LYS A . n 
A 1 3892 LEU 3892 3892 3892 LEU LEU A . n 
A 1 3893 LYS 3893 3893 3893 LYS LYS A . n 
A 1 3894 GLY 3894 3894 3894 GLY GLY A . n 
A 1 3895 THR 3895 3895 3895 THR THR A . n 
A 1 3896 VAL 3896 3896 3896 VAL VAL A . n 
A 1 3897 GLY 3897 3897 3897 GLY GLY A . n 
A 1 3898 GLU 3898 3898 3898 GLU GLU A . n 
A 1 3899 PRO 3899 3899 3899 PRO PRO A . n 
A 1 3900 THR 3900 3900 3900 THR THR A . n 
A 1 3901 TYR 3901 3901 3901 TYR TYR A . n 
A 1 3902 ASP 3902 3902 3902 ASP ASP A . n 
A 1 3903 ALA 3903 3903 3903 ALA ALA A . n 
A 1 3904 GLU 3904 3904 3904 GLU GLU A . n 
A 1 3905 PHE 3905 3905 3905 PHE PHE A . n 
A 1 3906 GLN 3906 3906 3906 GLN GLN A . n 
A 1 3907 HIS 3907 3907 3907 HIS HIS A . n 
A 1 3908 PHE 3908 3908 3908 PHE PHE A . n 
A 1 3909 LEU 3909 3909 3909 LEU LEU A . n 
A 1 3910 ARG 3910 3910 3910 ARG ARG A . n 
A 1 3911 GLY 3911 3911 3911 GLY GLY A . n 
A 1 3912 ASN 3912 3912 3912 ASN ASN A . n 
A 1 3913 GLU 3913 3913 3913 GLU GLU A . n 
A 1 3914 ILE 3914 3914 3914 ILE ILE A . n 
A 1 3915 VAL 3915 3915 3915 VAL VAL A . n 
A 1 3916 LEU 3916 3916 3916 LEU LEU A . n 
A 1 3917 SER 3917 3917 3917 SER SER A . n 
A 1 3918 ALA 3918 3918 3918 ALA ALA A . n 
A 1 3919 GLY 3919 3919 3919 GLY GLY A . n 
A 1 3920 SER 3920 3920 3920 SER SER A . n 
A 1 3921 THR 3921 3921 3921 THR THR A . n 
A 1 3922 PRO 3922 3922 3922 PRO PRO A . n 
A 1 3923 ARG 3923 3923 3923 ARG ARG A . n 
A 1 3924 ILE 3924 3924 3924 ILE ILE A . n 
A 1 3925 GLN 3925 3925 3925 GLN GLN A . n 
A 1 3926 GLY 3926 3926 3926 GLY GLY A . n 
A 1 3927 LEU 3927 3927 3927 LEU LEU A . n 
A 1 3928 THR 3928 3928 3928 THR THR A . n 
A 1 3929 VAL 3929 3929 3929 VAL VAL A . n 
A 1 3930 GLU 3930 3930 3930 GLU GLU A . n 
A 1 3931 GLN 3931 3931 3931 GLN GLN A . n 
A 1 3932 ALA 3932 3932 3932 ALA ALA A . n 
A 1 3933 GLU 3933 3933 3933 GLU GLU A . n 
A 1 3934 ALA 3934 3934 3934 ALA ALA A . n 
A 1 3935 VAL 3935 3935 3935 VAL VAL A . n 
A 1 3936 VAL 3936 3936 3936 VAL VAL A . n 
A 1 3937 ARG 3937 3937 3937 ARG ARG A . n 
A 1 3938 LEU 3938 3938 3938 LEU LEU A . n 
A 1 3939 SER 3939 3939 3939 SER SER A . n 
A 1 3940 CYS 3940 3940 3940 CYS CYS A . n 
A 1 3941 LEU 3941 3941 3941 LEU LEU A . n 
A 1 3942 PRO 3942 3942 3942 PRO PRO A . n 
A 1 3943 ALA 3943 3943 3943 ALA ALA A . n 
A 1 3944 PHE 3944 3944 3944 PHE PHE A . n 
A 1 3945 LYS 3945 3945 3945 LYS LYS A . n 
A 1 3946 ASP 3946 3946 3946 ASP ASP A . n 
A 1 3947 LEU 3947 3947 3947 LEU LEU A . n 
A 1 3948 ILE 3948 3948 3948 ILE ILE A . n 
A 1 3949 ALA 3949 3949 3949 ALA ALA A . n 
A 1 3950 LYS 3950 3950 3950 LYS LYS A . n 
A 1 3951 VAL 3951 3951 3951 VAL VAL A . n 
A 1 3952 GLN 3952 3952 3952 GLN GLN A . n 
A 1 3953 ALA 3953 3953 3953 ALA ALA A . n 
A 1 3954 ASP 3954 3954 3954 ASP ASP A . n 
A 1 3955 GLU 3955 3955 3955 GLU GLU A . n 
A 1 3956 GLN 3956 3956 3956 GLN GLN A . n 
A 1 3957 PHE 3957 3957 3957 PHE PHE A . n 
A 1 3958 GLY 3958 3958 3958 GLY GLY A . n 
A 1 3959 ILE 3959 3959 3959 ILE ILE A . n 
A 1 3960 TRP 3960 3960 3960 TRP TRP A . n 
A 1 3961 LEU 3961 3961 3961 LEU LEU A . n 
A 1 3962 ASP 3962 3962 3962 ASP ASP A . n 
A 1 3963 SER 3963 3963 3963 SER SER A . n 
A 1 3964 SER 3964 3964 3964 SER SER A . n 
A 1 3965 SER 3965 3965 3965 SER SER A . n 
A 1 3966 PRO 3966 3966 3966 PRO PRO A . n 
A 1 3967 GLU 3967 3967 3967 GLU GLU A . n 
A 1 3968 GLN 3968 3968 3968 GLN GLN A . n 
A 1 3969 THR 3969 3969 3969 THR THR A . n 
A 1 3970 VAL 3970 3970 3970 VAL VAL A . n 
A 1 3971 PRO 3971 3971 3971 PRO PRO A . n 
A 1 3972 TYR 3972 3972 3972 TYR TYR A . n 
A 1 3973 LEU 3973 3973 3973 LEU LEU A . n 
A 1 3974 TRP 3974 3974 3974 TRP TRP A . n 
A 1 3975 SER 3975 3975 3975 SER SER A . n 
A 1 3976 GLU 3976 3976 3976 GLU GLU A . n 
A 1 3977 GLU 3977 3977 3977 GLU GLU A . n 
A 1 3978 THR 3978 3978 3978 THR THR A . n 
A 1 3979 PRO 3979 3979 3979 PRO PRO A . n 
A 1 3980 ALA 3980 3980 3980 ALA ALA A . n 
A 1 3981 THR 3981 3981 3981 THR THR A . n 
A 1 3982 PRO 3982 3982 3982 PRO PRO A . n 
A 1 3983 ILE 3983 3983 3983 ILE ILE A . n 
A 1 3984 GLY 3984 3984 3984 GLY GLY A . n 
A 1 3985 GLN 3985 3985 3985 GLN GLN A . n 
A 1 3986 ALA 3986 3986 3986 ALA ALA A . n 
A 1 3987 ILE 3987 3987 3987 ILE ILE A . n 
A 1 3988 HIS 3988 3988 3988 HIS HIS A . n 
A 1 3989 ARG 3989 3989 3989 ARG ARG A . n 
A 1 3990 LEU 3990 3990 3990 LEU LEU A . n 
A 1 3991 LEU 3991 3991 3991 LEU LEU A . n 
A 1 3992 LEU 3992 3992 3992 LEU LEU A . n 
A 1 3993 ILE 3993 3993 3993 ILE ILE A . n 
A 1 3994 GLN 3994 3994 3994 GLN GLN A . n 
A 1 3995 ALA 3995 3995 3995 ALA ALA A . n 
A 1 3996 PHE 3996 3996 3996 PHE PHE A . n 
A 1 3997 ARG 3997 3997 3997 ARG ARG A . n 
A 1 3998 PRO 3998 3998 3998 PRO PRO A . n 
A 1 3999 ASP 3999 3999 3999 ASP ASP A . n 
A 1 4000 ARG 4000 4000 4000 ARG ARG A . n 
A 1 4001 LEU 4001 4001 4001 LEU LEU A . n 
A 1 4002 LEU 4002 4002 4002 LEU LEU A . n 
A 1 4003 ALA 4003 4003 4003 ALA ALA A . n 
A 1 4004 MET 4004 4004 4004 MET MET A . n 
A 1 4005 ALA 4005 4005 4005 ALA ALA A . n 
A 1 4006 HIS 4006 4006 4006 HIS HIS A . n 
A 1 4007 MET 4007 4007 4007 MET MET A . n 
A 1 4008 PHE 4008 4008 4008 PHE PHE A . n 
A 1 4009 VAL 4009 4009 4009 VAL VAL A . n 
A 1 4010 SER 4010 4010 4010 SER SER A . n 
A 1 4011 THR 4011 4011 4011 THR THR A . n 
A 1 4012 ASN 4012 4012 4012 ASN ASN A . n 
A 1 4013 LEU 4013 4013 4013 LEU LEU A . n 
A 1 4014 GLY 4014 4014 4014 GLY GLY A . n 
A 1 4015 GLU 4015 4015 4015 GLU GLU A . n 
A 1 4016 SER 4016 4016 4016 SER SER A . n 
A 1 4017 PHE 4017 4017 4017 PHE PHE A . n 
A 1 4018 MET 4018 4018 4018 MET MET A . n 
A 1 4019 SER 4019 4019 4019 SER SER A . n 
A 1 4020 ILE 4020 4020 4020 ILE ILE A . n 
A 1 4021 MET 4021 4021 4021 MET MET A . n 
A 1 4022 GLU 4022 4022 4022 GLU GLU A . n 
A 1 4023 GLN 4023 4023 4023 GLN GLN A . n 
A 1 4024 PRO 4024 4024 4024 PRO PRO A . n 
A 1 4025 LEU 4025 4025 4025 LEU LEU A . n 
A 1 4026 ASP 4026 4026 4026 ASP ASP A . n 
A 1 4027 LEU 4027 4027 4027 LEU LEU A . n 
A 1 4028 THR 4028 4028 4028 THR THR A . n 
A 1 4029 HIS 4029 4029 4029 HIS HIS A . n 
A 1 4030 ILE 4030 4030 4030 ILE ILE A . n 
A 1 4031 VAL 4031 4031 4031 VAL VAL A . n 
A 1 4032 GLY 4032 4032 4032 GLY GLY A . n 
A 1 4033 THR 4033 4033 4033 THR THR A . n 
A 1 4034 GLU 4034 4034 4034 GLU GLU A . n 
A 1 4035 VAL 4035 4035 4035 VAL VAL A . n 
A 1 4036 LYS 4036 4036 4036 LYS LYS A . n 
A 1 4037 PRO 4037 4037 4037 PRO PRO A . n 
A 1 4038 ASN 4038 4038 4038 ASN ASN A . n 
A 1 4039 THR 4039 4039 4039 THR THR A . n 
A 1 4040 PRO 4040 4040 4040 PRO PRO A . n 
A 1 4041 VAL 4041 4041 4041 VAL VAL A . n 
A 1 4042 LEU 4042 4042 4042 LEU LEU A . n 
A 1 4043 MET 4043 4043 4043 MET MET A . n 
A 1 4044 CYS 4044 4044 4044 CYS CYS A . n 
A 1 4045 SER 4045 4045 4045 SER SER A . n 
A 1 4046 VAL 4046 4046 4046 VAL VAL A . n 
A 1 4047 PRO 4047 4047 4047 PRO PRO A . n 
A 1 4048 GLY 4048 4048 4048 GLY GLY A . n 
A 1 4049 TYR 4049 4049 4049 TYR TYR A . n 
A 1 4050 ASP 4050 4050 4050 ASP ASP A . n 
A 1 4051 ALA 4051 4051 4051 ALA ALA A . n 
A 1 4052 SER 4052 4052 4052 SER SER A . n 
A 1 4053 GLY 4053 4053 4053 GLY GLY A . n 
A 1 4054 HIS 4054 4054 4054 HIS HIS A . n 
A 1 4055 VAL 4055 4055 4055 VAL VAL A . n 
A 1 4056 GLU 4056 4056 4056 GLU GLU A . n 
A 1 4057 ASP 4057 4057 4057 ASP ASP A . n 
A 1 4058 LEU 4058 4058 4058 LEU LEU A . n 
A 1 4059 ALA 4059 4059 4059 ALA ALA A . n 
A 1 4060 ALA 4060 4060 4060 ALA ALA A . n 
A 1 4061 GLU 4061 4061 4061 GLU GLU A . n 
A 1 4062 GLN 4062 4062 4062 GLN GLN A . n 
A 1 4063 ASN 4063 4063 4063 ASN ASN A . n 
A 1 4064 THR 4064 4064 4064 THR THR A . n 
A 1 4065 GLN 4065 4065 4065 GLN GLN A . n 
A 1 4066 ILE 4066 4066 4066 ILE ILE A . n 
A 1 4067 THR 4067 4067 4067 THR THR A . n 
A 1 4068 SER 4068 4068 4068 SER SER A . n 
A 1 4069 ILE 4069 4069 4069 ILE ILE A . n 
A 1 4070 ALA 4070 4070 4070 ALA ALA A . n 
A 1 4071 ILE 4071 4071 4071 ILE ILE A . n 
A 1 4072 GLY 4072 4072 4072 GLY GLY A . n 
A 1 4073 SER 4073 4073 4073 SER SER A . n 
A 1 4074 ALA 4074 4074 4074 ALA ALA A . n 
A 1 4075 GLU 4075 4075 4075 GLU GLU A . n 
A 1 4076 GLY 4076 4076 4076 GLY GLY A . n 
A 1 4077 PHE 4077 4077 4077 PHE PHE A . n 
A 1 4078 ASN 4078 4078 4078 ASN ASN A . n 
A 1 4079 GLN 4079 4079 4079 GLN GLN A . n 
A 1 4080 ALA 4080 4080 4080 ALA ALA A . n 
A 1 4081 ASP 4081 4081 4081 ASP ASP A . n 
A 1 4082 LYS 4082 4082 4082 LYS LYS A . n 
A 1 4083 ALA 4083 4083 4083 ALA ALA A . n 
A 1 4084 ILE 4084 4084 4084 ILE ILE A . n 
A 1 4085 ASN 4085 4085 4085 ASN ASN A . n 
A 1 4086 THR 4086 4086 4086 THR THR A . n 
A 1 4087 ALA 4087 4087 4087 ALA ALA A . n 
A 1 4088 VAL 4088 4088 4088 VAL VAL A . n 
A 1 4089 LYS 4089 4089 4089 LYS LYS A . n 
A 1 4090 SER 4090 4090 4090 SER SER A . n 
A 1 4091 GLY 4091 4091 4091 GLY GLY A . n 
A 1 4092 ARG 4092 4092 4092 ARG ARG A . n 
A 1 4093 TRP 4093 4093 4093 TRP TRP A . n 
A 1 4094 VAL 4094 4094 4094 VAL VAL A . n 
A 1 4095 MET 4095 4095 4095 MET MET A . n 
A 1 4096 LEU 4096 4096 4096 LEU LEU A . n 
A 1 4097 LYS 4097 4097 4097 LYS LYS A . n 
A 1 4098 ASN 4098 4098 4098 ASN ASN A . n 
A 1 4099 VAL 4099 4099 4099 VAL VAL A . n 
A 1 4100 HIS 4100 4100 4100 HIS HIS A . n 
A 1 4101 LEU 4101 4101 4101 LEU LEU A . n 
A 1 4102 ALA 4102 4102 4102 ALA ALA A . n 
A 1 4103 PRO 4103 4103 4103 PRO PRO A . n 
A 1 4104 GLY 4104 4104 4104 GLY GLY A . n 
A 1 4105 TRP 4105 4105 4105 TRP TRP A . n 
A 1 4106 LEU 4106 4106 4106 LEU LEU A . n 
A 1 4107 MET 4107 4107 4107 MET MET A . n 
A 1 4108 GLN 4108 4108 4108 GLN GLN A . n 
A 1 4109 LEU 4109 4109 4109 LEU LEU A . n 
A 1 4110 GLU 4110 4110 4110 GLU GLU A . n 
A 1 4111 LYS 4111 4111 4111 LYS LYS A . n 
A 1 4112 LYS 4112 4112 4112 LYS LYS A . n 
A 1 4113 LEU 4113 4113 4113 LEU LEU A . n 
A 1 4114 HIS 4114 4114 4114 HIS HIS A . n 
A 1 4115 SER 4115 4115 4115 SER SER A . n 
A 1 4116 LEU 4116 4116 4116 LEU LEU A . n 
A 1 4117 GLN 4117 4117 4117 GLN GLN A . n 
A 1 4118 PRO 4118 4118 4118 PRO PRO A . n 
A 1 4119 HIS 4119 4119 4119 HIS HIS A . n 
A 1 4120 ALA 4120 4120 4120 ALA ALA A . n 
A 1 4121 CYS 4121 4121 4121 CYS CYS A . n 
A 1 4122 PHE 4122 4122 4122 PHE PHE A . n 
A 1 4123 ARG 4123 4123 4123 ARG ARG A . n 
A 1 4124 LEU 4124 4124 4124 LEU LEU A . n 
A 1 4125 PHE 4125 4125 4125 PHE PHE A . n 
A 1 4126 LEU 4126 4126 4126 LEU LEU A . n 
A 1 4127 THR 4127 4127 4127 THR THR A . n 
A 1 4128 MET 4128 4128 4128 MET MET A . n 
A 1 4129 GLU 4129 4129 4129 GLU GLU A . n 
A 1 4130 ILE 4130 4130 4130 ILE ILE A . n 
A 1 4131 ASN 4131 4131 4131 ASN ASN A . n 
A 1 4132 PRO 4132 4132 4132 PRO PRO A . n 
A 1 4133 LYS 4133 4133 4133 LYS LYS A . n 
A 1 4134 VAL 4134 4134 4134 VAL VAL A . n 
A 1 4135 PRO 4135 4135 4135 PRO PRO A . n 
A 1 4136 VAL 4136 4136 4136 VAL VAL A . n 
A 1 4137 ASN 4137 4137 4137 ASN ASN A . n 
A 1 4138 LEU 4138 4138 4138 LEU LEU A . n 
A 1 4139 LEU 4139 4139 4139 LEU LEU A . n 
A 1 4140 ARG 4140 4140 4140 ARG ARG A . n 
A 1 4141 ALA 4141 4141 4141 ALA ALA A . n 
A 1 4142 GLY 4142 4142 4142 GLY GLY A . n 
A 1 4143 ARG 4143 4143 4143 ARG ARG A . n 
A 1 4144 ILE 4144 4144 4144 ILE ILE A . n 
A 1 4145 PHE 4145 4145 4145 PHE PHE A . n 
A 1 4146 VAL 4146 4146 4146 VAL VAL A . n 
A 1 4147 PHE 4147 4147 4147 PHE PHE A . n 
A 1 4148 GLU 4148 4148 4148 GLU GLU A . n 
A 1 4149 PRO 4149 4149 4149 PRO PRO A . n 
A 1 4150 PRO 4150 4150 4150 PRO PRO A . n 
A 1 4151 PRO 4151 4151 4151 PRO PRO A . n 
A 1 4152 GLY 4152 4152 4152 GLY GLY A . n 
A 1 4153 VAL 4153 4153 4153 VAL VAL A . n 
A 1 4154 LYS 4154 4154 4154 LYS LYS A . n 
A 1 4155 ALA 4155 4155 4155 ALA ALA A . n 
A 1 4156 ASN 4156 4156 4156 ASN ASN A . n 
A 1 4157 MET 4157 4157 4157 MET MET A . n 
A 1 4158 LEU 4158 4158 4158 LEU LEU A . n 
A 1 4159 ARG 4159 4159 4159 ARG ARG A . n 
A 1 4160 THR 4160 4160 4160 THR THR A . n 
A 1 4161 PHE 4161 4161 4161 PHE PHE A . n 
A 1 4162 SER 4162 4162 4162 SER SER A . n 
A 1 4163 SER 4163 4163 4163 SER SER A . n 
A 1 4164 ILE 4164 4164 4164 ILE ILE A . n 
A 1 4165 PRO 4165 4165 4165 PRO PRO A . n 
A 1 4166 VAL 4166 4166 4166 VAL VAL A . n 
A 1 4167 SER 4167 4167 4167 SER SER A . n 
A 1 4168 ARG 4168 4168 4168 ARG ARG A . n 
A 1 4169 ILE 4169 4169 4169 ILE ILE A . n 
A 1 4170 CYS 4170 4170 4170 CYS CYS A . n 
A 1 4171 LYS 4171 4171 4171 LYS LYS A . n 
A 1 4172 SER 4172 4172 4172 SER SER A . n 
A 1 4173 PRO 4173 4173 4173 PRO PRO A . n 
A 1 4174 ASN 4174 4174 4174 ASN ASN A . n 
A 1 4175 GLU 4175 4175 4175 GLU GLU A . n 
A 1 4176 ARG 4176 4176 4176 ARG ARG A . n 
A 1 4177 ALA 4177 4177 4177 ALA ALA A . n 
A 1 4178 ARG 4178 4178 4178 ARG ARG A . n 
A 1 4179 LEU 4179 4179 4179 LEU LEU A . n 
A 1 4180 TYR 4180 4180 4180 TYR TYR A . n 
A 1 4181 PHE 4181 4181 4181 PHE PHE A . n 
A 1 4182 LEU 4182 4182 4182 LEU LEU A . n 
A 1 4183 LEU 4183 4183 4183 LEU LEU A . n 
A 1 4184 ALA 4184 4184 4184 ALA ALA A . n 
A 1 4185 TRP 4185 4185 4185 TRP TRP A . n 
A 1 4186 PHE 4186 4186 4186 PHE PHE A . n 
A 1 4187 HIS 4187 4187 4187 HIS HIS A . n 
A 1 4188 ALA 4188 4188 4188 ALA ALA A . n 
A 1 4189 ILE 4189 4189 4189 ILE ILE A . n 
A 1 4190 ILE 4190 4190 4190 ILE ILE A . n 
A 1 4191 GLN 4191 4191 4191 GLN GLN A . n 
A 1 4192 GLU 4192 4192 4192 GLU GLU A . n 
A 1 4193 ARG 4193 4193 4193 ARG ARG A . n 
A 1 4194 LEU 4194 4194 4194 LEU LEU A . n 
A 1 4195 ARG 4195 4195 4195 ARG ARG A . n 
A 1 4196 TYR 4196 4196 4196 TYR TYR A . n 
A 1 4197 ALA 4197 4197 4197 ALA ALA A . n 
A 1 4198 PRO 4198 4198 4198 PRO PRO A . n 
A 1 4199 LEU 4199 4199 4199 LEU LEU A . n 
A 1 4200 GLY 4200 4200 4200 GLY GLY A . n 
A 1 4201 TRP 4201 4201 4201 TRP TRP A . n 
A 1 4202 SER 4202 4202 4202 SER SER A . n 
A 1 4203 LYS 4203 4203 4203 LYS LYS A . n 
A 1 4204 LYS 4204 4204 4204 LYS LYS A . n 
A 1 4205 TYR 4205 4205 4205 TYR TYR A . n 
A 1 4206 GLU 4206 4206 4206 GLU GLU A . n 
A 1 4207 PHE 4207 4207 4207 PHE PHE A . n 
A 1 4208 GLY 4208 4208 4208 GLY GLY A . n 
A 1 4209 GLU 4209 4209 4209 GLU GLU A . n 
A 1 4210 SER 4210 4210 4210 SER SER A . n 
A 1 4211 ASP 4211 4211 4211 ASP ASP A . n 
A 1 4212 LEU 4212 4212 4212 LEU LEU A . n 
A 1 4213 ARG 4213 4213 4213 ARG ARG A . n 
A 1 4214 SER 4214 4214 4214 SER SER A . n 
A 1 4215 ALA 4215 4215 4215 ALA ALA A . n 
A 1 4216 CYS 4216 4216 4216 CYS CYS A . n 
A 1 4217 ASP 4217 4217 4217 ASP ASP A . n 
A 1 4218 THR 4218 4218 4218 THR THR A . n 
A 1 4219 VAL 4219 4219 4219 VAL VAL A . n 
A 1 4220 ASP 4220 4220 4220 ASP ASP A . n 
A 1 4221 THR 4221 4221 4221 THR THR A . n 
A 1 4222 TRP 4222 4222 4222 TRP TRP A . n 
A 1 4223 LEU 4223 4223 4223 LEU LEU A . n 
A 1 4224 ASP 4224 4224 4224 ASP ASP A . n 
A 1 4225 ASP 4225 4225 4225 ASP ASP A . n 
A 1 4226 THR 4226 4226 4226 THR THR A . n 
A 1 4227 ALA 4227 4227 4227 ALA ALA A . n 
A 1 4228 LYS 4228 4228 4228 LYS LYS A . n 
A 1 4229 GLY 4229 4229 4229 GLY GLY A . n 
A 1 4230 ARG 4230 4230 4230 ARG ARG A . n 
A 1 4231 GLN 4231 4231 4231 GLN GLN A . n 
A 1 4232 ASN 4232 4232 4232 ASN ASN A . n 
A 1 4233 ILE 4233 4233 4233 ILE ILE A . n 
A 1 4234 SER 4234 4234 4234 SER SER A . n 
A 1 4235 PRO 4235 4235 4235 PRO PRO A . n 
A 1 4236 ASP 4236 4236 4236 ASP ASP A . n 
A 1 4237 LYS 4237 4237 4237 LYS LYS A . n 
A 1 4238 ILE 4238 4238 4238 ILE ILE A . n 
A 1 4239 PRO 4239 4239 4239 PRO PRO A . n 
A 1 4240 TRP 4240 4240 4240 TRP TRP A . n 
A 1 4241 SER 4241 4241 4241 SER SER A . n 
A 1 4242 ALA 4242 4242 4242 ALA ALA A . n 
A 1 4243 LEU 4243 4243 4243 LEU LEU A . n 
A 1 4244 LYS 4244 4244 4244 LYS LYS A . n 
A 1 4245 THR 4245 4245 4245 THR THR A . n 
A 1 4246 LEU 4246 4246 4246 LEU LEU A . n 
A 1 4247 MET 4247 4247 4247 MET MET A . n 
A 1 4248 ALA 4248 4248 4248 ALA ALA A . n 
A 1 4249 GLN 4249 4249 4249 GLN GLN A . n 
A 1 4250 SER 4250 4250 4250 SER SER A . n 
A 1 4251 ILE 4251 4251 4251 ILE ILE A . n 
A 1 4252 TYR 4252 4252 4252 TYR TYR A . n 
A 1 4253 GLY 4253 4253 4253 GLY GLY A . n 
A 1 4254 GLY 4254 4254 4254 GLY GLY A . n 
A 1 4255 ARG 4255 4255 4255 ARG ARG A . n 
A 1 4256 VAL 4256 4256 4256 VAL VAL A . n 
A 1 4257 ASP 4257 4257 4257 ASP ASP A . n 
A 1 4258 ASN 4258 4258 4258 ASN ASN A . n 
A 1 4259 GLU 4259 4259 4259 GLU GLU A . n 
A 1 4260 PHE 4260 4260 4260 PHE PHE A . n 
A 1 4261 ASP 4261 4261 4261 ASP ASP A . n 
A 1 4262 GLN 4262 4262 4262 GLN GLN A . n 
A 1 4263 ARG 4263 4263 4263 ARG ARG A . n 
A 1 4264 LEU 4264 4264 4264 LEU LEU A . n 
A 1 4265 LEU 4265 4265 4265 LEU LEU A . n 
A 1 4266 ASN 4266 4266 4266 ASN ASN A . n 
A 1 4267 THR 4267 4267 4267 THR THR A . n 
A 1 4268 PHE 4268 4268 4268 PHE PHE A . n 
A 1 4269 LEU 4269 4269 4269 LEU LEU A . n 
A 1 4270 GLU 4270 4270 4270 GLU GLU A . n 
A 1 4271 ARG 4271 4271 4271 ARG ARG A . n 
A 1 4272 LEU 4272 4272 4272 LEU LEU A . n 
A 1 4273 PHE 4273 4273 4273 PHE PHE A . n 
A 1 4274 THR 4274 4274 4274 THR THR A . n 
A 1 4275 THR 4275 4275 4275 THR THR A . n 
A 1 4276 ARG 4276 4276 4276 ARG ARG A . n 
A 1 4277 SER 4277 4277 4277 SER SER A . n 
A 1 4278 PHE 4278 4278 4278 PHE PHE A . n 
A 1 4279 ASP 4279 4279 4279 ASP ASP A . n 
A 1 4280 SER 4280 4280 4280 SER SER A . n 
A 1 4281 GLU 4281 4281 4281 GLU GLU A . n 
A 1 4282 PHE 4282 4282 4282 PHE PHE A . n 
A 1 4283 LYS 4283 4283 4283 LYS LYS A . n 
A 1 4284 LEU 4284 4284 4284 LEU LEU A . n 
A 1 4285 ALA 4285 4285 4285 ALA ALA A . n 
A 1 4286 CYS 4286 4286 4286 CYS CYS A . n 
A 1 4287 LYS 4287 4287 4287 LYS LYS A . n 
A 1 4288 VAL 4288 4288 4288 VAL VAL A . n 
A 1 4289 ASP 4289 4289 4289 ASP ASP A . n 
A 1 4290 GLY 4290 4290 4290 GLY GLY A . n 
A 1 4291 HIS 4291 4291 4291 HIS HIS A . n 
A 1 4292 LYS 4292 4292 4292 LYS LYS A . n 
A 1 4293 ASP 4293 4293 4293 ASP ASP A . n 
A 1 4294 ILE 4294 4294 4294 ILE ILE A . n 
A 1 4295 GLN 4295 4295 4295 GLN GLN A . n 
A 1 4296 MET 4296 4296 4296 MET MET A . n 
A 1 4297 PRO 4297 4297 4297 PRO PRO A . n 
A 1 4298 ASP 4298 4298 4298 ASP ASP A . n 
A 1 4299 GLY 4299 4299 4299 GLY GLY A . n 
A 1 4300 ILE 4300 4300 4300 ILE ILE A . n 
A 1 4301 ARG 4301 4301 4301 ARG ARG A . n 
A 1 4302 ARG 4302 4302 4302 ARG ARG A . n 
A 1 4303 GLU 4303 4303 4303 GLU GLU A . n 
A 1 4304 GLU 4304 4304 4304 GLU GLU A . n 
A 1 4305 PHE 4305 4305 4305 PHE PHE A . n 
A 1 4306 VAL 4306 4306 4306 VAL VAL A . n 
A 1 4307 GLN 4307 4307 4307 GLN GLN A . n 
A 1 4308 TRP 4308 4308 4308 TRP TRP A . n 
A 1 4309 VAL 4309 4309 4309 VAL VAL A . n 
A 1 4310 GLU 4310 4310 4310 GLU GLU A . n 
A 1 4311 LEU 4311 4311 4311 LEU LEU A . n 
A 1 4312 LEU 4312 4312 4312 LEU LEU A . n 
A 1 4313 PRO 4313 4313 4313 PRO PRO A . n 
A 1 4314 ASP 4314 4314 4314 ASP ASP A . n 
A 1 4315 THR 4315 4315 4315 THR THR A . n 
A 1 4316 GLN 4316 4316 4316 GLN GLN A . n 
A 1 4317 THR 4317 4317 4317 THR THR A . n 
A 1 4318 PRO 4318 4318 4318 PRO PRO A . n 
A 1 4319 SER 4319 4319 4319 SER SER A . n 
A 1 4320 TRP 4320 4320 4320 TRP TRP A . n 
A 1 4321 LEU 4321 4321 4321 LEU LEU A . n 
A 1 4322 GLY 4322 4322 4322 GLY GLY A . n 
A 1 4323 LEU 4323 4323 4323 LEU LEU A . n 
A 1 4324 PRO 4324 4324 4324 PRO PRO A . n 
A 1 4325 ASN 4325 4325 4325 ASN ASN A . n 
A 1 4326 ASN 4326 4326 4326 ASN ASN A . n 
A 1 4327 ALA 4327 4327 4327 ALA ALA A . n 
A 1 4328 GLU 4328 4328 4328 GLU GLU A . n 
A 1 4329 ARG 4329 4329 4329 ARG ARG A . n 
A 1 4330 VAL 4330 4330 4330 VAL VAL A . n 
A 1 4331 LEU 4331 4331 4331 LEU LEU A . n 
A 1 4332 LEU 4332 4332 4332 LEU LEU A . n 
A 1 4333 THR 4333 4333 4333 THR THR A . n 
A 1 4334 THR 4334 4334 4334 THR THR A . n 
A 1 4335 GLN 4335 4335 4335 GLN GLN A . n 
A 1 4336 GLY 4336 4336 4336 GLY GLY A . n 
A 1 4337 VAL 4337 4337 4337 VAL VAL A . n 
A 1 4338 ASP 4338 4338 4338 ASP ASP A . n 
A 1 4339 MET 4339 4339 4339 MET MET A . n 
A 1 4340 ILE 4340 4340 4340 ILE ILE A . n 
A 1 4341 SER 4341 4341 4341 SER SER A . n 
A 1 4342 LYS 4342 4342 4342 LYS LYS A . n 
A 1 4343 MET 4343 4343 4343 MET MET A . n 
A 1 4344 LEU 4344 4344 4344 LEU LEU A . n 
A 1 4345 LYS 4345 4345 4345 LYS LYS A . n 
A 1 4346 MET 4346 4346 4346 MET MET A . n 
A 1 4347 GLN 4347 4347 4347 GLN GLN A . n 
A 1 4348 MET 4348 4348 4348 MET MET A . n 
A 1 4349 LEU 4349 4349 4349 LEU LEU A . n 
A 1 4350 GLU 4350 4350 4350 GLU GLU A . n 
A 1 4351 ASP 4351 4351 4351 ASP ASP A . n 
A 1 4352 GLU 4352 4352 4352 GLU GLU A . n 
A 1 4353 ASP 4353 4353 4353 ASP ASP 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 4646 GLU GLU 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 ANP ? ? ANP ? ? 'SUBJECT OF INVESTIGATION' ? 
3 ATP ? ? ATP ? ? 'SUBJECT OF INVESTIGATION' ? 
4 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ADP 1 4701 4701 ADP ADP A . 
C 3 ATP 1 4702 4702 ATP ATP A . 
D 4 ANP 1 4703 4703 ANP ANP A . 
E 4 ANP 1 4704 4704 ANP ANP A . 
F 5 MG  1 4705 4705 MG  MG  A . 
G 5 MG  1 4706 4706 MG  MG  A . 
H 5 MG  1 4707 4707 MG  MG  A . 
I 5 MG  1 4708 4708 MG  MG  A . 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BMD 
_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                         9BMD 
_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                   9BMD 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9BMD 
_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 ? 25124 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.526 ? 34071 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 5.723 ? 3327  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.040 ? 3817  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.005 ? 4365  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9BMD 
_struct.title                        'Motor domain from full-length human dynein-1 bound to microtubules in 5mM AMPPNP condition' 
_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        9BMD 
_struct_keywords.text            'dynein-1, MOTOR PROTEIN' 
_struct_keywords.pdbx_keywords   'MOTOR PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 5 ? 
I N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DYHC1_HUMAN 
_struct_ref.pdbx_db_accession          Q14204 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BMD 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 4646 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q14204 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  4646 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       4646 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_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 1327 ? GLU A 1348 ? GLN A 1327 GLU A 1348 1 ? 22 
HELX_P HELX_P2   AA2 GLN A 1355 ? SER A 1372 ? GLN A 1355 SER A 1372 1 ? 18 
HELX_P HELX_P3   AA3 PRO A 1374 ? GLN A 1379 ? PRO A 1374 GLN A 1379 1 ? 6  
HELX_P HELX_P4   AA4 TYR A 1380 ? ILE A 1396 ? TYR A 1380 ILE A 1396 1 ? 17 
HELX_P HELX_P5   AA5 ILE A 1396 ? LYS A 1404 ? ILE A 1396 LYS A 1404 1 ? 9  
HELX_P HELX_P6   AA6 ASP A 1410 ? LEU A 1420 ? ASP A 1410 LEU A 1420 1 ? 11 
HELX_P HELX_P7   AA7 THR A 1430 ? VAL A 1437 ? THR A 1430 VAL A 1437 1 ? 8  
HELX_P HELX_P8   AA8 ASN A 1442 ? TYR A 1473 ? ASN A 1442 TYR A 1473 1 ? 32 
HELX_P HELX_P9   AA9 GLY A 1489 ? LYS A 1508 ? GLY A 1489 LYS A 1508 1 ? 20 
HELX_P HELX_P10  AB1 PHE A 1516 ? THR A 1552 ? PHE A 1516 THR A 1552 1 ? 37 
HELX_P HELX_P11  AB2 ALA A 1555 ? LEU A 1561 ? ALA A 1555 LEU A 1561 1 ? 7  
HELX_P HELX_P12  AB3 LEU A 1561 ? SER A 1585 ? LEU A 1561 SER A 1585 1 ? 25 
HELX_P HELX_P13  AB4 LEU A 1587 ? ASN A 1593 ? LEU A 1587 ASN A 1593 1 ? 7  
HELX_P HELX_P14  AB5 GLY A 1596 ? PHE A 1626 ? GLY A 1596 PHE A 1626 1 ? 31 
HELX_P HELX_P15  AB6 PRO A 1627 ? VAL A 1632 ? PRO A 1627 VAL A 1632 5 ? 6  
HELX_P HELX_P16  AB7 GLY A 1633 ? ASN A 1643 ? GLY A 1633 ASN A 1643 1 ? 11 
HELX_P HELX_P17  AB8 ASN A 1646 ? LYS A 1652 ? ASN A 1646 LYS A 1652 5 ? 7  
HELX_P HELX_P18  AB9 HIS A 1653 ? PHE A 1658 ? HIS A 1653 PHE A 1658 1 ? 6  
HELX_P HELX_P19  AC1 LYS A 1697 ? LYS A 1729 ? LYS A 1697 LYS A 1729 1 ? 33 
HELX_P HELX_P20  AC2 ASP A 1734 ? TYR A 1745 ? ASP A 1734 TYR A 1745 1 ? 12 
HELX_P HELX_P21  AC3 GLN A 1746 ? GLY A 1773 ? GLN A 1746 GLY A 1773 1 ? 28 
HELX_P HELX_P22  AC4 ALA A 1775 ? MET A 1798 ? ALA A 1775 MET A 1798 1 ? 24 
HELX_P HELX_P23  AC5 PRO A 1801 ? SER A 1828 ? PRO A 1801 SER A 1828 1 ? 28 
HELX_P HELX_P24  AC6 SER A 1835 ? SER A 1840 ? SER A 1835 SER A 1840 1 ? 6  
HELX_P HELX_P25  AC7 ASP A 1852 ? GLN A 1855 ? ASP A 1852 GLN A 1855 5 ? 4  
HELX_P HELX_P26  AC8 THR A 1882 ? ALA A 1898 ? THR A 1882 ALA A 1898 1 ? 17 
HELX_P HELX_P27  AC9 GLY A 1911 ? LEU A 1923 ? GLY A 1911 LEU A 1923 1 ? 13 
HELX_P HELX_P28  AD1 ALA A 1940 ? GLY A 1952 ? ALA A 1940 GLY A 1952 1 ? 13 
HELX_P HELX_P29  AD2 GLU A 1959 ? LEU A 1963 ? GLU A 1959 LEU A 1963 5 ? 5  
HELX_P HELX_P30  AD3 GLU A 1964 ? GLU A 1984 ? GLU A 1964 GLU A 1984 1 ? 21 
HELX_P HELX_P31  AD4 LEU A 2032 ? LYS A 2034 ? LEU A 2032 LYS A 2034 5 ? 3  
HELX_P HELX_P32  AD5 ASP A 2045 ? GLN A 2057 ? ASP A 2045 GLN A 2057 1 ? 13 
HELX_P HELX_P33  AD6 THR A 2061 ? LEU A 2080 ? THR A 2061 LEU A 2080 1 ? 20 
HELX_P HELX_P34  AD7 GLY A 2089 ? ARG A 2118 ? GLY A 2089 ARG A 2118 1 ? 30 
HELX_P HELX_P35  AD8 ASP A 2123 ? ASN A 2130 ? ASP A 2123 ASN A 2130 1 ? 8  
HELX_P HELX_P36  AD9 PRO A 2132 ? VAL A 2146 ? PRO A 2132 VAL A 2146 1 ? 15 
HELX_P HELX_P37  AE1 PRO A 2147 ? LEU A 2149 ? PRO A 2147 LEU A 2149 5 ? 3  
HELX_P HELX_P38  AE2 GLU A 2152 ? PHE A 2165 ? GLU A 2152 PHE A 2165 1 ? 14 
HELX_P HELX_P39  AE3 MET A 2175 ? MET A 2189 ? MET A 2175 MET A 2189 1 ? 15 
HELX_P HELX_P40  AE4 GLY A 2200 ? ASN A 2217 ? GLY A 2200 ASN A 2217 1 ? 18 
HELX_P HELX_P41  AE5 GLY A 2229 ? GLY A 2246 ? GLY A 2229 GLY A 2246 1 ? 18 
HELX_P HELX_P42  AE6 SER A 2260 ? GLY A 2266 ? SER A 2260 GLY A 2266 1 ? 7  
HELX_P HELX_P43  AE7 GLY A 2278 ? SER A 2290 ? GLY A 2278 SER A 2290 1 ? 13 
HELX_P HELX_P44  AE8 GLY A 2293 ? LEU A 2295 ? GLY A 2293 LEU A 2295 5 ? 3  
HELX_P HELX_P45  AE9 LEU A 2315 ? ASP A 2320 ? LEU A 2315 ASP A 2320 1 ? 6  
HELX_P HELX_P46  AF1 THR A 2352 ? CYS A 2359 ? THR A 2352 CYS A 2359 1 ? 8  
HELX_P HELX_P47  AF2 SER A 2365 ? LEU A 2369 ? SER A 2365 LEU A 2369 5 ? 5  
HELX_P HELX_P48  AF3 SER A 2370 ? ILE A 2385 ? SER A 2370 ILE A 2385 1 ? 16 
HELX_P HELX_P49  AF4 ALA A 2394 ? GLY A 2400 ? ALA A 2394 GLY A 2400 1 ? 7  
HELX_P HELX_P50  AF5 SER A 2410 ? GLN A 2424 ? SER A 2410 GLN A 2424 1 ? 15 
HELX_P HELX_P51  AF6 PRO A 2425 ? THR A 2428 ? PRO A 2425 THR A 2428 5 ? 4  
HELX_P HELX_P52  AF7 GLY A 2431 ? LEU A 2443 ? GLY A 2431 LEU A 2443 1 ? 13 
HELX_P HELX_P53  AF8 THR A 2450 ? HIS A 2476 ? THR A 2450 HIS A 2476 1 ? 27 
HELX_P HELX_P54  AF9 GLN A 2482 ? SER A 2503 ? GLN A 2482 SER A 2503 1 ? 22 
HELX_P HELX_P55  AG1 ARG A 2507 ? THR A 2522 ? ARG A 2507 THR A 2522 1 ? 16 
HELX_P HELX_P56  AG2 PRO A 2533 ? ILE A 2535 ? PRO A 2533 ILE A 2535 5 ? 3  
HELX_P HELX_P57  AG3 GLN A 2549 ? VAL A 2552 ? GLN A 2549 VAL A 2552 5 ? 4  
HELX_P HELX_P58  AG4 THR A 2571 ? GLU A 2587 ? THR A 2571 GLU A 2587 1 ? 17 
HELX_P HELX_P59  AG5 GLY A 2600 ? LEU A 2612 ? GLY A 2600 LEU A 2612 1 ? 13 
HELX_P HELX_P60  AG6 THR A 2627 ? TYR A 2638 ? THR A 2627 TYR A 2638 1 ? 12 
HELX_P HELX_P61  AG7 GLN A 2677 ? HIS A 2689 ? GLN A 2677 HIS A 2689 1 ? 13 
HELX_P HELX_P62  AG8 SER A 2724 ? ARG A 2729 ? SER A 2724 ARG A 2729 1 ? 6  
HELX_P HELX_P63  AG9 GLY A 2740 ? ARG A 2757 ? GLY A 2740 ARG A 2757 1 ? 18 
HELX_P HELX_P64  AH1 ILE A 2759 ? THR A 2764 ? ILE A 2759 THR A 2764 5 ? 6  
HELX_P HELX_P65  AH2 TYR A 2765 ? PHE A 2784 ? TYR A 2765 PHE A 2784 1 ? 20 
HELX_P HELX_P66  AH3 SER A 2795 ? ARG A 2811 ? SER A 2795 ARG A 2811 1 ? 17 
HELX_P HELX_P67  AH4 PRO A 2817 ? PHE A 2833 ? PRO A 2817 PHE A 2833 1 ? 17 
HELX_P HELX_P68  AH5 GLU A 2839 ? PHE A 2858 ? GLU A 2839 PHE A 2858 1 ? 20 
HELX_P HELX_P69  AH6 ASP A 2862 ? MET A 2867 ? ASP A 2862 MET A 2867 1 ? 6  
HELX_P HELX_P70  AH7 ASP A 2885 ? GLU A 2903 ? ASP A 2885 GLU A 2903 1 ? 19 
HELX_P HELX_P71  AH8 PHE A 2912 ? ARG A 2927 ? PHE A 2912 ARG A 2927 1 ? 16 
HELX_P HELX_P72  AH9 GLY A 2942 ? ASN A 2954 ? GLY A 2942 ASN A 2954 1 ? 13 
HELX_P HELX_P73  AI1 THR A 2968 ? CYS A 2985 ? THR A 2968 CYS A 2985 1 ? 18 
HELX_P HELX_P74  AI2 GLU A 2996 ? LEU A 3000 ? GLU A 2996 LEU A 3000 1 ? 5  
HELX_P HELX_P75  AI3 ASP A 3001 ? ASN A 3014 ? ASP A 3001 ASN A 3014 1 ? 14 
HELX_P HELX_P76  AI4 GLY A 3023 ? GLY A 3041 ? GLY A 3023 GLY A 3041 1 ? 19 
HELX_P HELX_P77  AI5 SER A 3046 ? ASN A 3061 ? SER A 3046 ASN A 3061 1 ? 16 
HELX_P HELX_P78  AI6 SER A 3082 ? CYS A 3089 ? SER A 3082 CYS A 3089 1 ? 8  
HELX_P HELX_P79  AI7 SER A 3098 ? THR A 3110 ? SER A 3098 THR A 3110 1 ? 13 
HELX_P HELX_P80  AI8 SER A 3138 ? GLY A 3165 ? SER A 3138 GLY A 3165 1 ? 28 
HELX_P HELX_P81  AI9 THR A 3172 ? ASP A 3221 ? THR A 3172 ASP A 3221 1 ? 50 
HELX_P HELX_P82  AJ1 LYS A 3471 ? ALA A 3517 ? LYS A 3471 ALA A 3517 1 ? 47 
HELX_P HELX_P83  AJ2 ASP A 3521 ? ALA A 3539 ? ASP A 3521 ALA A 3539 1 ? 19 
HELX_P HELX_P84  AJ3 ALA A 3548 ? LEU A 3553 ? ALA A 3548 LEU A 3553 1 ? 6  
HELX_P HELX_P85  AJ4 ASN A 3555 ? SER A 3565 ? ASN A 3555 SER A 3565 1 ? 11 
HELX_P HELX_P86  AJ5 ASP A 3570 ? ARG A 3582 ? ASP A 3570 ARG A 3582 1 ? 13 
HELX_P HELX_P87  AJ6 GLY A 3594 ? TYR A 3604 ? GLY A 3594 TYR A 3604 1 ? 11 
HELX_P HELX_P88  AJ7 ALA A 3618 ? GLY A 3630 ? ALA A 3618 GLY A 3630 1 ? 13 
HELX_P HELX_P89  AJ8 ASP A 3637 ? TYR A 3641 ? ASP A 3637 TYR A 3641 5 ? 5  
HELX_P HELX_P90  AJ9 ASP A 3642 ? VAL A 3644 ? ASP A 3642 VAL A 3644 5 ? 3  
HELX_P HELX_P91  AK1 LEU A 3645 ? ARG A 3651 ? LEU A 3645 ARG A 3651 1 ? 7  
HELX_P HELX_P92  AK2 PRO A 3689 ? VAL A 3696 ? PRO A 3689 VAL A 3696 1 ? 8  
HELX_P HELX_P93  AK3 THR A 3704 ? ARG A 3721 ? THR A 3704 ARG A 3721 1 ? 18 
HELX_P HELX_P94  AK4 ARG A 3721 ? LEU A 3734 ? ARG A 3721 LEU A 3734 1 ? 14 
HELX_P HELX_P95  AK5 GLY A 3736 ? GLU A 3755 ? GLY A 3736 GLU A 3755 1 ? 20 
HELX_P HELX_P96  AK6 ILE A 3766 ? GLU A 3786 ? ILE A 3766 GLU A 3786 1 ? 21 
HELX_P HELX_P97  AK7 GLU A 3786 ? LEU A 3818 ? GLU A 3786 LEU A 3818 1 ? 33 
HELX_P HELX_P98  AK8 LYS A 3819 ? ILE A 3821 ? LYS A 3819 ILE A 3821 5 ? 3  
HELX_P HELX_P99  AK9 SER A 3828 ? TYR A 3841 ? SER A 3828 TYR A 3841 1 ? 14 
HELX_P HELX_P100 AL1 ASN A 3843 ? LYS A 3847 ? ASN A 3843 LYS A 3847 5 ? 5  
HELX_P HELX_P101 AL2 ASP A 3851 ? ARG A 3873 ? ASP A 3851 ARG A 3873 1 ? 23 
HELX_P HELX_P102 AL3 GLY A 3874 ? MET A 3875 ? GLY A 3874 MET A 3875 5 ? 2  
HELX_P HELX_P103 AL4 LEU A 3876 ? GLN A 3878 ? LEU A 3876 GLN A 3878 5 ? 3  
HELX_P HELX_P104 AL5 ASP A 3879 ? THR A 3895 ? ASP A 3879 THR A 3895 1 ? 17 
HELX_P HELX_P105 AL6 TYR A 3901 ? GLY A 3911 ? TYR A 3901 GLY A 3911 1 ? 11 
HELX_P HELX_P106 AL7 ASN A 3912 ? ILE A 3914 ? ASN A 3912 ILE A 3914 5 ? 3  
HELX_P HELX_P107 AL8 THR A 3928 ? SER A 3939 ? THR A 3928 SER A 3939 1 ? 12 
HELX_P HELX_P108 AL9 CYS A 3940 ? LYS A 3945 ? CYS A 3940 LYS A 3945 5 ? 6  
HELX_P HELX_P109 AM1 ASP A 3946 ? ASP A 3954 ? ASP A 3946 ASP A 3954 1 ? 9  
HELX_P HELX_P110 AM2 GLN A 3956 ? ASP A 3962 ? GLN A 3956 ASP A 3962 1 ? 7  
HELX_P HELX_P111 AM3 SER A 3965 ? VAL A 3970 ? SER A 3965 VAL A 3970 5 ? 6  
HELX_P HELX_P112 AM4 THR A 3981 ? ARG A 3997 ? THR A 3981 ARG A 3997 1 ? 17 
HELX_P HELX_P113 AM5 ARG A 4000 ? LEU A 4013 ? ARG A 4000 LEU A 4013 1 ? 14 
HELX_P HELX_P114 AM6 MET A 4018 ? GLN A 4023 ? MET A 4018 GLN A 4023 1 ? 6  
HELX_P HELX_P115 AM7 ASP A 4026 ? THR A 4033 ? ASP A 4026 THR A 4033 1 ? 8  
HELX_P HELX_P116 AM8 ALA A 4051 ? ASN A 4063 ? ALA A 4051 ASN A 4063 1 ? 13 
HELX_P HELX_P117 AM9 SER A 4073 ? GLY A 4091 ? SER A 4073 GLY A 4091 1 ? 19 
HELX_P HELX_P118 AN1 ASN A 4098 ? LEU A 4101 ? ASN A 4098 LEU A 4101 5 ? 4  
HELX_P HELX_P119 AN2 ALA A 4102 ? LEU A 4116 ? ALA A 4102 LEU A 4116 1 ? 15 
HELX_P HELX_P120 AN3 PRO A 4135 ? ALA A 4141 ? PRO A 4135 ALA A 4141 1 ? 7  
HELX_P HELX_P121 AN4 GLY A 4152 ? ILE A 4164 ? GLY A 4152 ILE A 4164 1 ? 13 
HELX_P HELX_P122 AN5 PRO A 4165 ? LYS A 4171 ? PRO A 4165 LYS A 4171 1 ? 7  
HELX_P HELX_P123 AN6 ASN A 4174 ? ARG A 4195 ? ASN A 4174 ARG A 4195 1 ? 22 
HELX_P HELX_P124 AN7 GLY A 4208 ? LYS A 4228 ? GLY A 4208 LYS A 4228 1 ? 21 
HELX_P HELX_P125 AN8 PRO A 4239 ? SER A 4250 ? PRO A 4239 SER A 4250 1 ? 12 
HELX_P HELX_P126 AN9 ASN A 4258 ? PHE A 4273 ? ASN A 4258 PHE A 4273 1 ? 16 
HELX_P HELX_P127 AO1 THR A 4274 ? ASP A 4279 ? THR A 4274 ASP A 4279 5 ? 6  
HELX_P HELX_P128 AO2 LYS A 4287 ? HIS A 4291 ? LYS A 4287 HIS A 4291 5 ? 5  
HELX_P HELX_P129 AO3 ARG A 4301 ? LEU A 4311 ? ARG A 4301 LEU A 4311 1 ? 11 
HELX_P HELX_P130 AO4 THR A 4317 ? GLY A 4322 ? THR A 4317 GLY A 4322 5 ? 6  
HELX_P HELX_P131 AO5 ASN A 4325 ? MET A 4346 ? ASN A 4325 MET A 4346 1 ? 22 
HELX_P HELX_P132 AO6 TRP A 4376 ? ILE A 4391 ? TRP A 4376 ILE A 4391 1 ? 16 
HELX_P HELX_P133 AO7 THR A 4401 ? LYS A 4406 ? THR A 4401 LYS A 4406 1 ? 6  
HELX_P HELX_P134 AO8 ASP A 4407 ? GLY A 4440 ? ASP A 4407 GLY A 4440 1 ? 34 
HELX_P HELX_P135 AO9 THR A 4445 ? GLY A 4458 ? THR A 4445 GLY A 4458 1 ? 14 
HELX_P HELX_P136 AP1 THR A 4474 ? SER A 4498 ? THR A 4474 SER A 4498 1 ? 25 
HELX_P HELX_P137 AP2 LYS A 4502 ? ILE A 4507 ? LYS A 4502 ILE A 4507 1 ? 6  
HELX_P HELX_P138 AP3 VAL A 4516 ? SER A 4533 ? VAL A 4516 SER A 4533 1 ? 18 
HELX_P HELX_P139 AP4 SER A 4535 ? GLU A 4537 ? SER A 4535 GLU A 4537 5 ? 3  
HELX_P HELX_P140 AP5 ASP A 4631 ? ARG A 4638 ? ASP A 4631 ARG A 4638 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A SER 2231 OG  ? ? ? 1_555 G MG . MG ? ? A SER 2231 A MG 4706 1_555 ? ? ? ? ? ? ? 1.948 ? ? 
metalc2  metalc ? ? A GLU 2344 OE2 ? ? ? 1_555 G MG . MG ? ? A GLU 2344 A MG 4706 1_555 ? ? ? ? ? ? ? 1.977 ? ? 
metalc3  metalc ? ? A THR 2602 OG1 ? ? ? 1_555 H MG . MG ? ? A THR 2602 A MG 4707 1_555 ? ? ? ? ? ? ? 1.966 ? ? 
metalc4  metalc ? ? A THR 2944 OG1 ? ? ? 1_555 I MG . MG ? ? A THR 2944 A MG 4708 1_555 ? ? ? ? ? ? ? 2.062 ? ? 
metalc5  metalc ? ? C ATP .    O2G ? ? ? 1_555 G MG . MG ? ? A ATP 4702 A MG 4706 1_555 ? ? ? ? ? ? ? 2.147 ? ? 
metalc6  metalc ? ? C ATP .    O1B ? ? ? 1_555 G MG . MG ? ? A ATP 4702 A MG 4706 1_555 ? ? ? ? ? ? ? 2.081 ? ? 
metalc7  metalc ? ? D ANP .    O3G ? ? ? 1_555 H MG . MG ? ? A ANP 4703 A MG 4707 1_555 ? ? ? ? ? ? ? 2.021 ? ? 
metalc8  metalc ? ? D ANP .    O1B ? ? ? 1_555 H MG . MG ? ? A ANP 4703 A MG 4707 1_555 ? ? ? ? ? ? ? 2.255 ? ? 
metalc9  metalc ? ? E ANP .    O1G ? ? ? 1_555 I MG . MG ? ? A ANP 4704 A MG 4708 1_555 ? ? ? ? ? ? ? 2.210 ? ? 
metalc10 metalc ? ? E ANP .    O2B ? ? ? 1_555 I MG . MG ? ? A ANP 4704 A MG 4708 1_555 ? ? ? ? ? ? ? 2.350 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 74.8  ? 
2  OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2G ? C ATP .    ? A ATP 4702 ? 1_555 160.7 ? 
3  OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2G ? C ATP .    ? A ATP 4702 ? 1_555 110.2 ? 
4  OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O1B ? C ATP .    ? A ATP 4702 ? 1_555 74.8  ? 
5  OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O1B ? C ATP .    ? A ATP 4702 ? 1_555 87.7  ? 
6  O2G ? C ATP .    ? A ATP 4702 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O1B ? C ATP .    ? A ATP 4702 ? 1_555 86.5  ? 
7  OG1 ? A THR 2602 ? A THR 2602 ? 1_555 MG ? H MG . ? A MG 4707 ? 1_555 O3G ? D ANP .    ? A ANP 4703 ? 1_555 158.9 ? 
8  OG1 ? A THR 2602 ? A THR 2602 ? 1_555 MG ? H MG . ? A MG 4707 ? 1_555 O1B ? D ANP .    ? A ANP 4703 ? 1_555 79.6  ? 
9  O3G ? D ANP .    ? A ANP 4703 ? 1_555 MG ? H MG . ? A MG 4707 ? 1_555 O1B ? D ANP .    ? A ANP 4703 ? 1_555 79.7  ? 
10 OG1 ? A THR 2944 ? A THR 2944 ? 1_555 MG ? I MG . ? A MG 4708 ? 1_555 O1G ? E ANP .    ? A ANP 4704 ? 1_555 155.1 ? 
11 OG1 ? A THR 2944 ? A THR 2944 ? 1_555 MG ? I MG . ? A MG 4708 ? 1_555 O2B ? E ANP .    ? A ANP 4704 ? 1_555 71.1  ? 
12 O1G ? E ANP .    ? A ANP 4704 ? 1_555 MG ? I MG . ? A MG 4708 ? 1_555 O2B ? E ANP .    ? A ANP 4704 ? 1_555 85.3  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLN 3135 A . ? GLN 3135 A PRO 3136 A ? PRO 3136 A 1 1.81 
2 SER 4172 A . ? SER 4172 A PRO 4173 A ? PRO 4173 A 1 1.90 
3 ALA 4197 A . ? ALA 4197 A PRO 4198 A ? PRO 4198 A 1 4.39 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
AB2 ? 5 ? 
AB3 ? 4 ? 
AB4 ? 2 ? 
AB5 ? 5 ? 
AB6 ? 5 ? 
AB7 ? 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      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? parallel      
AB2 2 3 ? parallel      
AB2 3 4 ? parallel      
AB2 4 5 ? parallel      
AB3 1 2 ? anti-parallel 
AB3 2 3 ? parallel      
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? parallel      
AB5 3 4 ? parallel      
AB5 4 5 ? parallel      
AB6 1 2 ? parallel      
AB6 2 3 ? parallel      
AB6 3 4 ? parallel      
AB6 4 5 ? parallel      
AB7 1 2 ? anti-parallel 
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 ASP A 1476 ? TYR A 1480 ? ASP A 1476 TYR A 1480 
AA1 2 CYS A 1484 ? ARG A 1488 ? CYS A 1484 ARG A 1488 
AA2 1 SER A 1663 ? LEU A 1666 ? SER A 1663 LEU A 1666 
AA2 2 VAL A 1672 ? SER A 1677 ? VAL A 1672 SER A 1677 
AA2 3 GLU A 1683 ? SER A 1691 ? GLU A 1683 SER A 1691 
AA3 1 ARG A 1843 ? PHE A 1846 ? ARG A 1843 PHE A 1846 
AA3 2 LEU A 1857 ? MET A 1861 ? LEU A 1857 MET A 1861 
AA3 3 ALA A 1864 ? ASN A 1867 ? ALA A 1864 ASN A 1867 
AA4 1 GLY A 1901 ? PHE A 1905 ? GLY A 1901 PHE A 1905 
AA4 2 PHE A 2036 ? ALA A 2040 ? PHE A 2036 ALA A 2040 
AA5 1 VAL A 1927 ? PHE A 1930 ? VAL A 1927 PHE A 1930 
AA5 2 TRP A 1954 ? PHE A 1957 ? TRP A 1954 PHE A 1957 
AA5 3 ALA A 2013 ? ILE A 2016 ? ALA A 2013 ILE A 2016 
AA6 1 THR A 1998 ? LEU A 2001 ? THR A 1998 LEU A 2001 
AA6 2 LYS A 2004 ? LYS A 2007 ? LYS A 2004 LYS A 2007 
AA7 1 GLU A 2248 ? ALA A 2251 ? GLU A 2248 ALA A 2251 
AA7 2 LYS A 2297 ? VAL A 2302 ? LYS A 2297 VAL A 2302 
AA7 3 ARG A 2340 ? GLU A 2344 ? ARG A 2340 GLU A 2344 
AA7 4 GLY A 2219 ? MET A 2222 ? GLY A 2219 MET A 2222 
AA7 5 GLY A 2360 ? VAL A 2362 ? GLY A 2360 VAL A 2362 
AA8 1 THR A 2267 ? LEU A 2268 ? THR A 2267 LEU A 2268 
AA8 2 TRP A 2275 ? THR A 2276 ? TRP A 2275 THR A 2276 
AA9 1 LEU A 2324 ? THR A 2326 ? LEU A 2324 THR A 2326 
AA9 2 ARG A 2332 ? SER A 2334 ? ARG A 2332 SER A 2334 
AB1 1 TYR A 2537 ? VAL A 2539 ? TYR A 2537 VAL A 2539 
AB1 2 TRP A 2545 ? PRO A 2547 ? TRP A 2545 PRO A 2547 
AB2 1 MET A 2615 ? LEU A 2620 ? MET A 2615 LEU A 2620 
AB2 2 TRP A 2658 ? CYS A 2663 ? TRP A 2658 CYS A 2663 
AB2 3 ILE A 2706 ? CYS A 2712 ? ILE A 2706 CYS A 2712 
AB2 4 VAL A 2592 ? CYS A 2594 ? VAL A 2592 CYS A 2594 
AB2 5 VAL A 2733 ? TYR A 2735 ? VAL A 2733 TYR A 2735 
AB3 1 CYS A 2639 ? ARG A 2643 ? CYS A 2639 ARG A 2643 
AB3 2 VAL A 2648 ? PRO A 2652 ? VAL A 2648 PRO A 2652 
AB3 3 TRP A 2700 ? LEU A 2703 ? TRP A 2700 LEU A 2703 
AB3 4 GLY A 2691 ? TYR A 2693 ? GLY A 2691 TYR A 2693 
AB4 1 TYR A 2873 ? SER A 2874 ? TYR A 2873 SER A 2874 
AB4 2 ILE A 2882 ? PRO A 2883 ? ILE A 2882 PRO A 2883 
AB5 1 SER A 2957 ? 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 LEU A 2933 ? GLY A 2937 ? LEU A 2933 GLY A 2937 
AB5 5 VAL A 3090 ? PHE A 3094 ? VAL A 3090 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 ? SER A 3680 ? ILE A 3677 SER A 3680 
AB6 4 PRO A 3587 ? ILE A 3589 ? PRO A 3587 ILE A 3589 
AB6 5 THR A 3697 ? VAL A 3699 ? THR A 3697 VAL A 3699 
AB7 1 LEU A 3661 ? LEU A 3664 ? LEU A 3661 LEU A 3664 
AB7 2 GLN A 3667 ? ASP A 3670 ? GLN A 3667 ASP A 3670 
AB8 1 ILE A 4066 ? ALA A 4070 ? ILE A 4066 ALA A 4070 
AB8 2 TRP A 4093 ? LYS A 4097 ? TRP A 4093 LYS A 4097 
AB8 3 ARG A 4123 ? MET A 4128 ? ARG A 4123 MET A 4128 
AB8 4 VAL A 4041 ? SER A 4045 ? VAL A 4041 SER A 4045 
AB8 5 ARG A 4143 ? PHE A 4147 ? ARG A 4143 PHE A 4147 
AB9 1 LYS A 4283 ? ALA A 4285 ? LYS A 4283 ALA A 4285 
AB9 2 ILE A 4294 ? GLN A 4295 ? ILE A 4294 GLN A 4295 
AC1 1 VAL A 4509 ? CYS A 4510 ? VAL A 4509 CYS A 4510 
AC1 2 SER A 4557 ? THR A 4561 ? SER A 4557 THR A 4561 
AC1 3 LEU A 4587 ? LYS A 4594 ? LEU A 4587 LYS A 4594 
AC1 4 LEU A 4539 ? THR A 4546 ? LEU A 4539 THR A 4546 
AC2 1 ALA A 4568 ? ASN A 4571 ? ALA A 4568 ASN A 4571 
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 ASP A 1476 ? N ASP A 1476 O ARG A 1488 ? O ARG A 1488 
AA2 1 2 N SER A 1663 ? N SER A 1663 O SER A 1677 ? O SER A 1677 
AA2 2 3 N VAL A 1673 ? N VAL A 1673 O VAL A 1690 ? O VAL A 1690 
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 GLU A 2248 ? N GLU A 2248 O ARG A 2298 ? O ARG A 2298 
AA7 2 3 N ILE A 2301 ? N ILE A 2301 O MET A 2342 ? O MET A 2342 
AA7 3 4 O PHE A 2343 ? O PHE A 2343 N LEU A 2220 ? N LEU A 2220 
AA7 4 5 N GLY A 2219 ? N GLY A 2219 O GLY A 2360 ? O GLY A 2360 
AA8 1 2 N THR A 2267 ? N THR A 2267 O THR A 2276 ? O THR A 2276 
AA9 1 2 N LEU A 2325 ? N LEU A 2325 O LEU A 2333 ? O LEU A 2333 
AB1 1 2 N GLU A 2538 ? N GLU A 2538 O SER A 2546 ? O SER A 2546 
AB2 1 2 N LEU A 2620 ? N LEU A 2620 O PHE A 2662 ? O PHE A 2662 
AB2 2 3 N LEU A 2659 ? N LEU A 2659 O GLN A 2707 ? O GLN A 2707 
AB2 3 4 O GLY A 2710 ? O GLY A 2710 N LEU A 2593 ? N LEU A 2593 
AB2 4 5 N CYS A 2594 ? N CYS A 2594 O VAL A 2734 ? O VAL A 2734 
AB3 1 2 N GLU A 2640 ? N GLU A 2640 O ALA A 2651 ? O ALA A 2651 
AB3 2 3 N VAL A 2648 ? N VAL A 2648 O LYS A 2702 ? O LYS A 2702 
AB3 3 4 O VAL A 2701 ? O VAL A 2701 N PHE A 2692 ? N PHE A 2692 
AB4 1 2 N SER A 2874 ? N SER A 2874 O ILE A 2882 ? O ILE A 2882 
AB5 1 2 N TYR A 2959 ? N TYR A 2959 O ALA A 2991 ? O ALA A 2991 
AB5 2 3 N PHE A 2992 ? N PHE A 2992 O HIS A 3063 ? O HIS A 3063 
AB5 3 4 O PHE A 3066 ? O PHE A 3066 N LEU A 2933 ? N LEU A 2933 
AB5 4 5 N ILE A 2936 ? N ILE A 2936 O ASN A 3092 ? O ASN A 3092 
AB6 1 2 N THR A 3612 ? N THR A 3612 O LEU A 3634 ? O LEU A 3634 
AB6 2 3 N LEU A 3633 ? N LEU A 3633 O PHE A 3678 ? O PHE A 3678 
AB6 3 4 O LEU A 3679 ? O LEU A 3679 N ILE A 3589 ? N ILE A 3589 
AB6 4 5 N LEU A 3588 ? N LEU A 3588 O THR A 3697 ? O THR A 3697 
AB7 1 2 N LEU A 3664 ? N LEU A 3664 O GLN A 3667 ? O GLN A 3667 
AB8 1 2 N THR A 4067 ? N THR A 4067 O MET A 4095 ? O MET A 4095 
AB8 2 3 N VAL A 4094 ? N VAL A 4094 O PHE A 4125 ? O PHE A 4125 
AB8 3 4 O LEU A 4124 ? O LEU A 4124 N VAL A 4041 ? N VAL A 4041 
AB8 4 5 N LEU A 4042 ? N LEU A 4042 O ARG A 4143 ? O ARG A 4143 
AB9 1 2 N ALA A 4285 ? N ALA A 4285 O ILE A 4294 ? O ILE A 4294 
AC1 1 2 N VAL A 4509 ? N VAL A 4509 O GLY A 4559 ? O GLY A 4559 
AC1 2 3 N VAL A 4560 ? N VAL A 4560 O THR A 4588 ? O THR A 4588 
AC1 3 4 O LEU A 4587 ? O LEU A 4587 N THR A 4546 ? N THR A 4546 
AC2 1 2 N ASN A 4571 ? N ASN A 4571 O LYS A 4574 ? O LYS A 4574 
AC2 2 3 N LEU A 4575 ? N LEU A 4575 O GLU A 4625 ? O GLU A 4625 
AC2 3 4 O PHE A 4620 ? O PHE A 4620 N VAL A 4609 ? N VAL A 4609 
AC2 4 5 N PRO A 4608 ? N PRO A 4608 O VAL A 4642 ? O VAL A 4642 
AC2 5 6 O ALA A 4641 ? O ALA A 4641 N GLN A 4566 ? N GLN A 4566 
AC2 6 7 N LEU A 4565 ? N LEU A 4565 O THR A 4583 ? O THR A 4583 
# 
_pdbx_entry_details.entry_id                   9BMD 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OG1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   THR 
_pdbx_validate_close_contact.auth_seq_id_1    1688 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OE2 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   GLU 
_pdbx_validate_close_contact.auth_seq_id_2    1708 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.16 
# 
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 1409 ? ? 51.20   -148.20 
2  1 LYS A 1514 ? ? -120.41 -54.75  
3  1 ALA A 1862 ? ? 56.28   -125.26 
4  1 THR A 2061 ? ? -94.38  55.18   
5  1 SER A 2082 ? ? -55.56  104.13  
6  1 PRO A 2309 ? ? -78.63  44.08   
7  1 ALA A 2408 ? ? -94.07  59.94   
8  1 SER A 2874 ? ? -172.30 147.29  
9  1 GLU A 2904 ? ? 60.47   -143.58 
10 1 MET A 3043 ? ? -93.27  51.74   
11 1 ASN A 3119 ? ? -95.25  32.03   
12 1 SER A 3566 ? ? -90.69  56.64   
13 1 LYS A 3608 ? ? 60.40   61.09   
14 1 SER A 3640 ? ? -93.61  54.76   
15 1 TYR A 3841 ? ? -91.93  -61.25  
16 1 GLU A 3842 ? ? -91.99  58.80   
17 1 ASP A 3946 ? ? -97.47  32.49   
18 1 ILE A 4130 ? ? 59.77   84.50   
19 1 GLU A 4206 ? ? -93.64  53.33   
20 1 ASP A 4289 ? ? 58.76   14.77   
21 1 LYS A 4292 ? ? 71.38   139.99  
22 1 MET A 4346 ? ? -94.28  52.71   
23 1 THR A 4628 ? ? 56.75   -164.67 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BMD 
_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                    9BMD 
_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                  2.9 
_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               241362 
_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       '30 mM HEPES pH 7.2, 60 mM KCl, 1 mM EGTA, 5 mM MgSO4, 1 mM DTT, 5 uM paclitaxel, 5mM AMPPNP' 
_em_buffer.pH            7.2 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 
'motor domain from full-length human dynein-1 bound to microtubules in 5mM AMPPNP condition' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9BMD 
_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              9BMD 
_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                9BMD 
_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 TYR 2022 ? A TYR 2022 
1328 1 Y 1 A ALA 2023 ? A ALA 2023 
1329 1 Y 1 A GLY 2024 ? A GLY 2024 
1330 1 Y 1 A ARG 2025 ? A ARG 2025 
1331 1 Y 1 A SER 3071 ? A SER 3071 
1332 1 Y 1 A SER 3072 ? A SER 3072 
1333 1 Y 1 A GLU 3073 ? A GLU 3073 
1334 1 Y 1 A GLY 3074 ? A GLY 3074 
1335 1 Y 1 A LEU 3075 ? A LEU 3075 
1336 1 Y 1 A LYS 3076 ? A LYS 3076 
1337 1 Y 1 A ASP 3077 ? A ASP 3077 
1338 1 Y 1 A ARG 3078 ? A ARG 3078 
1339 1 Y 1 A ALA 3079 ? A ALA 3079 
1340 1 Y 1 A LEU 3222 ? A LEU 3222 
1341 1 Y 1 A ARG 3223 ? A ARG 3223 
1342 1 Y 1 A ILE 3224 ? A ILE 3224 
1343 1 Y 1 A LYS 3225 ? A LYS 3225 
1344 1 Y 1 A SER 3226 ? A SER 3226 
1345 1 Y 1 A GLN 3227 ? A GLN 3227 
1346 1 Y 1 A GLU 3228 ? A GLU 3228 
1347 1 Y 1 A LEU 3229 ? A LEU 3229 
1348 1 Y 1 A GLU 3230 ? A GLU 3230 
1349 1 Y 1 A VAL 3231 ? A VAL 3231 
1350 1 Y 1 A LYS 3232 ? A LYS 3232 
1351 1 Y 1 A ASN 3233 ? A ASN 3233 
1352 1 Y 1 A ALA 3234 ? A ALA 3234 
1353 1 Y 1 A ALA 3235 ? A ALA 3235 
1354 1 Y 1 A ALA 3236 ? A ALA 3236 
1355 1 Y 1 A ASN 3237 ? A ASN 3237 
1356 1 Y 1 A ASP 3238 ? A ASP 3238 
1357 1 Y 1 A LYS 3239 ? A LYS 3239 
1358 1 Y 1 A LEU 3240 ? A LEU 3240 
1359 1 Y 1 A LYS 3241 ? A LYS 3241 
1360 1 Y 1 A LYS 3242 ? A LYS 3242 
1361 1 Y 1 A MET 3243 ? A MET 3243 
1362 1 Y 1 A VAL 3244 ? A VAL 3244 
1363 1 Y 1 A LYS 3245 ? A LYS 3245 
1364 1 Y 1 A ASP 3246 ? A ASP 3246 
1365 1 Y 1 A GLN 3247 ? A GLN 3247 
1366 1 Y 1 A GLN 3248 ? A GLN 3248 
1367 1 Y 1 A GLU 3249 ? A GLU 3249 
1368 1 Y 1 A ALA 3250 ? A ALA 3250 
1369 1 Y 1 A GLU 3251 ? A GLU 3251 
1370 1 Y 1 A LYS 3252 ? A LYS 3252 
1371 1 Y 1 A LYS 3253 ? A LYS 3253 
1372 1 Y 1 A LYS 3254 ? A LYS 3254 
1373 1 Y 1 A VAL 3255 ? A VAL 3255 
1374 1 Y 1 A MET 3256 ? A MET 3256 
1375 1 Y 1 A SER 3257 ? A SER 3257 
1376 1 Y 1 A GLN 3258 ? A GLN 3258 
1377 1 Y 1 A GLU 3259 ? A GLU 3259 
1378 1 Y 1 A ILE 3260 ? A ILE 3260 
1379 1 Y 1 A GLN 3261 ? A GLN 3261 
1380 1 Y 1 A GLU 3262 ? A GLU 3262 
1381 1 Y 1 A GLN 3263 ? A GLN 3263 
1382 1 Y 1 A LEU 3264 ? A LEU 3264 
1383 1 Y 1 A HIS 3265 ? A HIS 3265 
1384 1 Y 1 A LYS 3266 ? A LYS 3266 
1385 1 Y 1 A GLN 3267 ? A GLN 3267 
1386 1 Y 1 A GLN 3268 ? A GLN 3268 
1387 1 Y 1 A GLU 3269 ? A GLU 3269 
1388 1 Y 1 A VAL 3270 ? A VAL 3270 
1389 1 Y 1 A ILE 3271 ? A ILE 3271 
1390 1 Y 1 A ALA 3272 ? A ALA 3272 
1391 1 Y 1 A ASP 3273 ? A ASP 3273 
1392 1 Y 1 A LYS 3274 ? A LYS 3274 
1393 1 Y 1 A GLN 3275 ? A GLN 3275 
1394 1 Y 1 A MET 3276 ? A MET 3276 
1395 1 Y 1 A SER 3277 ? A SER 3277 
1396 1 Y 1 A VAL 3278 ? A VAL 3278 
1397 1 Y 1 A LYS 3279 ? A LYS 3279 
1398 1 Y 1 A GLU 3280 ? A GLU 3280 
1399 1 Y 1 A ASP 3281 ? A ASP 3281 
1400 1 Y 1 A LEU 3282 ? A LEU 3282 
1401 1 Y 1 A ASP 3283 ? A ASP 3283 
1402 1 Y 1 A LYS 3284 ? A LYS 3284 
1403 1 Y 1 A VAL 3285 ? A VAL 3285 
1404 1 Y 1 A GLU 3286 ? A GLU 3286 
1405 1 Y 1 A PRO 3287 ? A PRO 3287 
1406 1 Y 1 A ALA 3288 ? A ALA 3288 
1407 1 Y 1 A VAL 3289 ? A VAL 3289 
1408 1 Y 1 A ILE 3290 ? A ILE 3290 
1409 1 Y 1 A GLU 3291 ? A GLU 3291 
1410 1 Y 1 A ALA 3292 ? A ALA 3292 
1411 1 Y 1 A GLN 3293 ? A GLN 3293 
1412 1 Y 1 A ASN 3294 ? A ASN 3294 
1413 1 Y 1 A ALA 3295 ? A ALA 3295 
1414 1 Y 1 A VAL 3296 ? A VAL 3296 
1415 1 Y 1 A LYS 3297 ? A LYS 3297 
1416 1 Y 1 A SER 3298 ? A SER 3298 
1417 1 Y 1 A ILE 3299 ? A ILE 3299 
1418 1 Y 1 A LYS 3300 ? A LYS 3300 
1419 1 Y 1 A LYS 3301 ? A LYS 3301 
1420 1 Y 1 A GLN 3302 ? A GLN 3302 
1421 1 Y 1 A HIS 3303 ? A HIS 3303 
1422 1 Y 1 A LEU 3304 ? A LEU 3304 
1423 1 Y 1 A VAL 3305 ? A VAL 3305 
1424 1 Y 1 A GLU 3306 ? A GLU 3306 
1425 1 Y 1 A VAL 3307 ? A VAL 3307 
1426 1 Y 1 A ARG 3308 ? A ARG 3308 
1427 1 Y 1 A SER 3309 ? A SER 3309 
1428 1 Y 1 A MET 3310 ? A MET 3310 
1429 1 Y 1 A ALA 3311 ? A ALA 3311 
1430 1 Y 1 A ASN 3312 ? A ASN 3312 
1431 1 Y 1 A PRO 3313 ? A PRO 3313 
1432 1 Y 1 A PRO 3314 ? A PRO 3314 
1433 1 Y 1 A ALA 3315 ? A ALA 3315 
1434 1 Y 1 A ALA 3316 ? A ALA 3316 
1435 1 Y 1 A VAL 3317 ? A VAL 3317 
1436 1 Y 1 A LYS 3318 ? A LYS 3318 
1437 1 Y 1 A LEU 3319 ? A LEU 3319 
1438 1 Y 1 A ALA 3320 ? A ALA 3320 
1439 1 Y 1 A LEU 3321 ? A LEU 3321 
1440 1 Y 1 A GLU 3322 ? A GLU 3322 
1441 1 Y 1 A SER 3323 ? A SER 3323 
1442 1 Y 1 A ILE 3324 ? A ILE 3324 
1443 1 Y 1 A CYS 3325 ? A CYS 3325 
1444 1 Y 1 A LEU 3326 ? A LEU 3326 
1445 1 Y 1 A LEU 3327 ? A LEU 3327 
1446 1 Y 1 A LEU 3328 ? A LEU 3328 
1447 1 Y 1 A GLY 3329 ? A GLY 3329 
1448 1 Y 1 A GLU 3330 ? A GLU 3330 
1449 1 Y 1 A SER 3331 ? A SER 3331 
1450 1 Y 1 A THR 3332 ? A THR 3332 
1451 1 Y 1 A THR 3333 ? A THR 3333 
1452 1 Y 1 A ASP 3334 ? A ASP 3334 
1453 1 Y 1 A TRP 3335 ? A TRP 3335 
1454 1 Y 1 A LYS 3336 ? A LYS 3336 
1455 1 Y 1 A GLN 3337 ? A GLN 3337 
1456 1 Y 1 A ILE 3338 ? A ILE 3338 
1457 1 Y 1 A ARG 3339 ? A ARG 3339 
1458 1 Y 1 A SER 3340 ? A SER 3340 
1459 1 Y 1 A ILE 3341 ? A ILE 3341 
1460 1 Y 1 A ILE 3342 ? A ILE 3342 
1461 1 Y 1 A MET 3343 ? A MET 3343 
1462 1 Y 1 A ARG 3344 ? A ARG 3344 
1463 1 Y 1 A GLU 3345 ? A GLU 3345 
1464 1 Y 1 A ASN 3346 ? A ASN 3346 
1465 1 Y 1 A PHE 3347 ? A PHE 3347 
1466 1 Y 1 A ILE 3348 ? A ILE 3348 
1467 1 Y 1 A PRO 3349 ? A PRO 3349 
1468 1 Y 1 A THR 3350 ? A THR 3350 
1469 1 Y 1 A ILE 3351 ? A ILE 3351 
1470 1 Y 1 A VAL 3352 ? A VAL 3352 
1471 1 Y 1 A ASN 3353 ? A ASN 3353 
1472 1 Y 1 A PHE 3354 ? A PHE 3354 
1473 1 Y 1 A SER 3355 ? A SER 3355 
1474 1 Y 1 A ALA 3356 ? A ALA 3356 
1475 1 Y 1 A GLU 3357 ? A GLU 3357 
1476 1 Y 1 A GLU 3358 ? A GLU 3358 
1477 1 Y 1 A ILE 3359 ? A ILE 3359 
1478 1 Y 1 A SER 3360 ? A SER 3360 
1479 1 Y 1 A ASP 3361 ? A ASP 3361 
1480 1 Y 1 A ALA 3362 ? A ALA 3362 
1481 1 Y 1 A ILE 3363 ? A ILE 3363 
1482 1 Y 1 A ARG 3364 ? A ARG 3364 
1483 1 Y 1 A GLU 3365 ? A GLU 3365 
1484 1 Y 1 A LYS 3366 ? A LYS 3366 
1485 1 Y 1 A MET 3367 ? A MET 3367 
1486 1 Y 1 A LYS 3368 ? A LYS 3368 
1487 1 Y 1 A LYS 3369 ? A LYS 3369 
1488 1 Y 1 A ASN 3370 ? A ASN 3370 
1489 1 Y 1 A TYR 3371 ? A TYR 3371 
1490 1 Y 1 A MET 3372 ? A MET 3372 
1491 1 Y 1 A SER 3373 ? A SER 3373 
1492 1 Y 1 A ASN 3374 ? A ASN 3374 
1493 1 Y 1 A PRO 3375 ? A PRO 3375 
1494 1 Y 1 A SER 3376 ? A SER 3376 
1495 1 Y 1 A TYR 3377 ? A TYR 3377 
1496 1 Y 1 A ASN 3378 ? A ASN 3378 
1497 1 Y 1 A TYR 3379 ? A TYR 3379 
1498 1 Y 1 A GLU 3380 ? A GLU 3380 
1499 1 Y 1 A ILE 3381 ? A ILE 3381 
1500 1 Y 1 A VAL 3382 ? A VAL 3382 
1501 1 Y 1 A ASN 3383 ? A ASN 3383 
1502 1 Y 1 A ARG 3384 ? A ARG 3384 
1503 1 Y 1 A ALA 3385 ? A ALA 3385 
1504 1 Y 1 A SER 3386 ? A SER 3386 
1505 1 Y 1 A LEU 3387 ? A LEU 3387 
1506 1 Y 1 A ALA 3388 ? A ALA 3388 
1507 1 Y 1 A CYS 3389 ? A CYS 3389 
1508 1 Y 1 A GLY 3390 ? A GLY 3390 
1509 1 Y 1 A PRO 3391 ? A PRO 3391 
1510 1 Y 1 A MET 3392 ? A MET 3392 
1511 1 Y 1 A VAL 3393 ? A VAL 3393 
1512 1 Y 1 A LYS 3394 ? A LYS 3394 
1513 1 Y 1 A TRP 3395 ? A TRP 3395 
1514 1 Y 1 A ALA 3396 ? A ALA 3396 
1515 1 Y 1 A ILE 3397 ? A ILE 3397 
1516 1 Y 1 A ALA 3398 ? A ALA 3398 
1517 1 Y 1 A GLN 3399 ? A GLN 3399 
1518 1 Y 1 A LEU 3400 ? A LEU 3400 
1519 1 Y 1 A ASN 3401 ? A ASN 3401 
1520 1 Y 1 A TYR 3402 ? A TYR 3402 
1521 1 Y 1 A ALA 3403 ? A ALA 3403 
1522 1 Y 1 A ASP 3404 ? A ASP 3404 
1523 1 Y 1 A MET 3405 ? A MET 3405 
1524 1 Y 1 A LEU 3406 ? A LEU 3406 
1525 1 Y 1 A LYS 3407 ? A LYS 3407 
1526 1 Y 1 A ARG 3408 ? A ARG 3408 
1527 1 Y 1 A VAL 3409 ? A VAL 3409 
1528 1 Y 1 A GLU 3410 ? A GLU 3410 
1529 1 Y 1 A PRO 3411 ? A PRO 3411 
1530 1 Y 1 A LEU 3412 ? A LEU 3412 
1531 1 Y 1 A ARG 3413 ? A ARG 3413 
1532 1 Y 1 A ASN 3414 ? A ASN 3414 
1533 1 Y 1 A GLU 3415 ? A GLU 3415 
1534 1 Y 1 A LEU 3416 ? A LEU 3416 
1535 1 Y 1 A GLN 3417 ? A GLN 3417 
1536 1 Y 1 A LYS 3418 ? A LYS 3418 
1537 1 Y 1 A LEU 3419 ? A LEU 3419 
1538 1 Y 1 A GLU 3420 ? A GLU 3420 
1539 1 Y 1 A ASP 3421 ? A ASP 3421 
1540 1 Y 1 A ASP 3422 ? A ASP 3422 
1541 1 Y 1 A ALA 3423 ? A ALA 3423 
1542 1 Y 1 A LYS 3424 ? A LYS 3424 
1543 1 Y 1 A ASP 3425 ? A ASP 3425 
1544 1 Y 1 A ASN 3426 ? A ASN 3426 
1545 1 Y 1 A GLN 3427 ? A GLN 3427 
1546 1 Y 1 A GLN 3428 ? A GLN 3428 
1547 1 Y 1 A LYS 3429 ? A LYS 3429 
1548 1 Y 1 A ALA 3430 ? A ALA 3430 
1549 1 Y 1 A ASN 3431 ? A ASN 3431 
1550 1 Y 1 A GLU 3432 ? A GLU 3432 
1551 1 Y 1 A VAL 3433 ? A VAL 3433 
1552 1 Y 1 A GLU 3434 ? A GLU 3434 
1553 1 Y 1 A GLN 3435 ? A GLN 3435 
1554 1 Y 1 A MET 3436 ? A MET 3436 
1555 1 Y 1 A ILE 3437 ? A ILE 3437 
1556 1 Y 1 A ARG 3438 ? A ARG 3438 
1557 1 Y 1 A ASP 3439 ? A ASP 3439 
1558 1 Y 1 A LEU 3440 ? A LEU 3440 
1559 1 Y 1 A GLU 3441 ? A GLU 3441 
1560 1 Y 1 A ALA 3442 ? A ALA 3442 
1561 1 Y 1 A SER 3443 ? A SER 3443 
1562 1 Y 1 A ILE 3444 ? A ILE 3444 
1563 1 Y 1 A ALA 3445 ? A ALA 3445 
1564 1 Y 1 A ARG 3446 ? A ARG 3446 
1565 1 Y 1 A TYR 3447 ? A TYR 3447 
1566 1 Y 1 A LYS 3448 ? A LYS 3448 
1567 1 Y 1 A GLU 3449 ? A GLU 3449 
1568 1 Y 1 A GLU 3450 ? A GLU 3450 
1569 1 Y 1 A TYR 3451 ? A TYR 3451 
1570 1 Y 1 A ALA 3452 ? A ALA 3452 
1571 1 Y 1 A VAL 3453 ? A VAL 3453 
1572 1 Y 1 A LEU 3454 ? A LEU 3454 
1573 1 Y 1 A ILE 3455 ? A ILE 3455 
1574 1 Y 1 A SER 3456 ? A SER 3456 
1575 1 Y 1 A GLU 3457 ? A GLU 3457 
1576 1 Y 1 A ALA 3458 ? A ALA 3458 
1577 1 Y 1 A GLN 3459 ? A GLN 3459 
1578 1 Y 1 A ALA 3460 ? A ALA 3460 
1579 1 Y 1 A ILE 3461 ? A ILE 3461 
1580 1 Y 1 A LYS 3462 ? A LYS 3462 
1581 1 Y 1 A ALA 3463 ? A ALA 3463 
1582 1 Y 1 A ASP 3464 ? A ASP 3464 
1583 1 Y 1 A LEU 3465 ? A LEU 3465 
1584 1 Y 1 A ALA 3466 ? A ALA 3466 
1585 1 Y 1 A ALA 3467 ? A ALA 3467 
1586 1 Y 1 A VAL 3468 ? A VAL 3468 
1587 1 Y 1 A GLU 3469 ? A GLU 3469 
1588 1 Y 1 A ASP 4354 ? A ASP 4354 
1589 1 Y 1 A LEU 4355 ? A LEU 4355 
1590 1 Y 1 A ALA 4356 ? A ALA 4356 
1591 1 Y 1 A TYR 4357 ? A TYR 4357 
1592 1 Y 1 A ALA 4358 ? A ALA 4358 
1593 1 Y 1 A GLU 4359 ? A GLU 4359 
1594 1 Y 1 A THR 4360 ? A THR 4360 
1595 1 Y 1 A GLU 4361 ? A GLU 4361 
1596 1 Y 1 A LYS 4362 ? A LYS 4362 
1597 1 Y 1 A LYS 4363 ? A LYS 4363 
1598 1 Y 1 A THR 4364 ? A THR 4364 
1599 1 Y 1 A ARG 4365 ? A ARG 4365 
1600 1 Y 1 A THR 4366 ? A THR 4366 
1601 1 Y 1 A ASP 4367 ? A ASP 4367 
1602 1 Y 1 A SER 4368 ? A SER 4368 
1603 1 Y 1 A THR 4369 ? A THR 4369 
1604 1 Y 1 A SER 4370 ? A SER 4370 
1605 1 Y 1 A ASP 4371 ? A ASP 4371 
1606 1 Y 1 A GLY 4372 ? A GLY 4372 
1607 1 Y 1 A ARG 4373 ? A ARG 4373 
1608 1 Y 1 A PRO 4374 ? A PRO 4374 
# 
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  
ANP PG     P  N N 56  
ANP O1G    O  N N 57  
ANP O2G    O  N N 58  
ANP O3G    O  N N 59  
ANP PB     P  N N 60  
ANP O1B    O  N N 61  
ANP O2B    O  N N 62  
ANP N3B    N  N N 63  
ANP PA     P  N N 64  
ANP O1A    O  N N 65  
ANP O2A    O  N N 66  
ANP O3A    O  N N 67  
ANP "O5'"  O  N N 68  
ANP "C5'"  C  N N 69  
ANP "C4'"  C  N R 70  
ANP "O4'"  O  N N 71  
ANP "C3'"  C  N S 72  
ANP "O3'"  O  N N 73  
ANP "C2'"  C  N R 74  
ANP "O2'"  O  N N 75  
ANP "C1'"  C  N R 76  
ANP N9     N  Y N 77  
ANP C8     C  Y N 78  
ANP N7     N  Y N 79  
ANP C5     C  Y N 80  
ANP C6     C  Y N 81  
ANP N6     N  N N 82  
ANP N1     N  Y N 83  
ANP C2     C  Y N 84  
ANP N3     N  Y N 85  
ANP C4     C  Y N 86  
ANP HOG2   H  N N 87  
ANP HOG3   H  N N 88  
ANP HOB2   H  N N 89  
ANP HNB1   H  N N 90  
ANP HOA2   H  N N 91  
ANP "H5'1" H  N N 92  
ANP "H5'2" H  N N 93  
ANP "H4'"  H  N N 94  
ANP "H3'"  H  N N 95  
ANP "HO3'" H  N N 96  
ANP "H2'"  H  N N 97  
ANP "HO2'" H  N N 98  
ANP "H1'"  H  N N 99  
ANP H8     H  N N 100 
ANP HN61   H  N N 101 
ANP HN62   H  N N 102 
ANP H2     H  N N 103 
ARG N      N  N N 104 
ARG CA     C  N S 105 
ARG C      C  N N 106 
ARG O      O  N N 107 
ARG CB     C  N N 108 
ARG CG     C  N N 109 
ARG CD     C  N N 110 
ARG NE     N  N N 111 
ARG CZ     C  N N 112 
ARG NH1    N  N N 113 
ARG NH2    N  N N 114 
ARG OXT    O  N N 115 
ARG H      H  N N 116 
ARG H2     H  N N 117 
ARG HA     H  N N 118 
ARG HB2    H  N N 119 
ARG HB3    H  N N 120 
ARG HG2    H  N N 121 
ARG HG3    H  N N 122 
ARG HD2    H  N N 123 
ARG HD3    H  N N 124 
ARG HE     H  N N 125 
ARG HH11   H  N N 126 
ARG HH12   H  N N 127 
ARG HH21   H  N N 128 
ARG HH22   H  N N 129 
ARG HXT    H  N N 130 
ASN N      N  N N 131 
ASN CA     C  N S 132 
ASN C      C  N N 133 
ASN O      O  N N 134 
ASN CB     C  N N 135 
ASN CG     C  N N 136 
ASN OD1    O  N N 137 
ASN ND2    N  N N 138 
ASN OXT    O  N N 139 
ASN H      H  N N 140 
ASN H2     H  N N 141 
ASN HA     H  N N 142 
ASN HB2    H  N N 143 
ASN HB3    H  N N 144 
ASN HD21   H  N N 145 
ASN HD22   H  N N 146 
ASN HXT    H  N N 147 
ASP N      N  N N 148 
ASP CA     C  N S 149 
ASP C      C  N N 150 
ASP O      O  N N 151 
ASP CB     C  N N 152 
ASP CG     C  N N 153 
ASP OD1    O  N N 154 
ASP OD2    O  N N 155 
ASP OXT    O  N N 156 
ASP H      H  N N 157 
ASP H2     H  N N 158 
ASP HA     H  N N 159 
ASP HB2    H  N N 160 
ASP HB3    H  N N 161 
ASP HD2    H  N N 162 
ASP HXT    H  N N 163 
ATP PG     P  N N 164 
ATP O1G    O  N N 165 
ATP O2G    O  N N 166 
ATP O3G    O  N N 167 
ATP PB     P  N R 168 
ATP O1B    O  N N 169 
ATP O2B    O  N N 170 
ATP O3B    O  N N 171 
ATP PA     P  N R 172 
ATP O1A    O  N N 173 
ATP O2A    O  N N 174 
ATP O3A    O  N N 175 
ATP "O5'"  O  N N 176 
ATP "C5'"  C  N N 177 
ATP "C4'"  C  N R 178 
ATP "O4'"  O  N N 179 
ATP "C3'"  C  N S 180 
ATP "O3'"  O  N N 181 
ATP "C2'"  C  N R 182 
ATP "O2'"  O  N N 183 
ATP "C1'"  C  N R 184 
ATP N9     N  Y N 185 
ATP C8     C  Y N 186 
ATP N7     N  Y N 187 
ATP C5     C  Y N 188 
ATP C6     C  Y N 189 
ATP N6     N  N N 190 
ATP N1     N  Y N 191 
ATP C2     C  Y N 192 
ATP N3     N  Y N 193 
ATP C4     C  Y N 194 
ATP HOG2   H  N N 195 
ATP HOG3   H  N N 196 
ATP HOB2   H  N N 197 
ATP HOA2   H  N N 198 
ATP "H5'1" H  N N 199 
ATP "H5'2" H  N N 200 
ATP "H4'"  H  N N 201 
ATP "H3'"  H  N N 202 
ATP "HO3'" H  N N 203 
ATP "H2'"  H  N N 204 
ATP "HO2'" H  N N 205 
ATP "H1'"  H  N N 206 
ATP H8     H  N N 207 
ATP HN61   H  N N 208 
ATP HN62   H  N N 209 
ATP H2     H  N N 210 
CYS N      N  N N 211 
CYS CA     C  N R 212 
CYS C      C  N N 213 
CYS O      O  N N 214 
CYS CB     C  N N 215 
CYS SG     S  N N 216 
CYS OXT    O  N N 217 
CYS H      H  N N 218 
CYS H2     H  N N 219 
CYS HA     H  N N 220 
CYS HB2    H  N N 221 
CYS HB3    H  N N 222 
CYS HG     H  N N 223 
CYS HXT    H  N N 224 
GLN N      N  N N 225 
GLN CA     C  N S 226 
GLN C      C  N N 227 
GLN O      O  N N 228 
GLN CB     C  N N 229 
GLN CG     C  N N 230 
GLN CD     C  N N 231 
GLN OE1    O  N N 232 
GLN NE2    N  N N 233 
GLN OXT    O  N N 234 
GLN H      H  N N 235 
GLN H2     H  N N 236 
GLN HA     H  N N 237 
GLN HB2    H  N N 238 
GLN HB3    H  N N 239 
GLN HG2    H  N N 240 
GLN HG3    H  N N 241 
GLN HE21   H  N N 242 
GLN HE22   H  N N 243 
GLN HXT    H  N N 244 
GLU N      N  N N 245 
GLU CA     C  N S 246 
GLU C      C  N N 247 
GLU O      O  N N 248 
GLU CB     C  N N 249 
GLU CG     C  N N 250 
GLU CD     C  N N 251 
GLU OE1    O  N N 252 
GLU OE2    O  N N 253 
GLU OXT    O  N N 254 
GLU H      H  N N 255 
GLU H2     H  N N 256 
GLU HA     H  N N 257 
GLU HB2    H  N N 258 
GLU HB3    H  N N 259 
GLU HG2    H  N N 260 
GLU HG3    H  N N 261 
GLU HE2    H  N N 262 
GLU HXT    H  N N 263 
GLY N      N  N N 264 
GLY CA     C  N N 265 
GLY C      C  N N 266 
GLY O      O  N N 267 
GLY OXT    O  N N 268 
GLY H      H  N N 269 
GLY H2     H  N N 270 
GLY HA2    H  N N 271 
GLY HA3    H  N N 272 
GLY HXT    H  N N 273 
HIS N      N  N N 274 
HIS CA     C  N S 275 
HIS C      C  N N 276 
HIS O      O  N N 277 
HIS CB     C  N N 278 
HIS CG     C  Y N 279 
HIS ND1    N  Y N 280 
HIS CD2    C  Y N 281 
HIS CE1    C  Y N 282 
HIS NE2    N  Y N 283 
HIS OXT    O  N N 284 
HIS H      H  N N 285 
HIS H2     H  N N 286 
HIS HA     H  N N 287 
HIS HB2    H  N N 288 
HIS HB3    H  N N 289 
HIS HD1    H  N N 290 
HIS HD2    H  N N 291 
HIS HE1    H  N N 292 
HIS HE2    H  N N 293 
HIS HXT    H  N N 294 
ILE N      N  N N 295 
ILE CA     C  N S 296 
ILE C      C  N N 297 
ILE O      O  N N 298 
ILE CB     C  N S 299 
ILE CG1    C  N N 300 
ILE CG2    C  N N 301 
ILE CD1    C  N N 302 
ILE OXT    O  N N 303 
ILE H      H  N N 304 
ILE H2     H  N N 305 
ILE HA     H  N N 306 
ILE HB     H  N N 307 
ILE HG12   H  N N 308 
ILE HG13   H  N N 309 
ILE HG21   H  N N 310 
ILE HG22   H  N N 311 
ILE HG23   H  N N 312 
ILE HD11   H  N N 313 
ILE HD12   H  N N 314 
ILE HD13   H  N N 315 
ILE HXT    H  N N 316 
LEU N      N  N N 317 
LEU CA     C  N S 318 
LEU C      C  N N 319 
LEU O      O  N N 320 
LEU CB     C  N N 321 
LEU CG     C  N N 322 
LEU CD1    C  N N 323 
LEU CD2    C  N N 324 
LEU OXT    O  N N 325 
LEU H      H  N N 326 
LEU H2     H  N N 327 
LEU HA     H  N N 328 
LEU HB2    H  N N 329 
LEU HB3    H  N N 330 
LEU HG     H  N N 331 
LEU HD11   H  N N 332 
LEU HD12   H  N N 333 
LEU HD13   H  N N 334 
LEU HD21   H  N N 335 
LEU HD22   H  N N 336 
LEU HD23   H  N N 337 
LEU HXT    H  N N 338 
LYS N      N  N N 339 
LYS CA     C  N S 340 
LYS C      C  N N 341 
LYS O      O  N N 342 
LYS CB     C  N N 343 
LYS CG     C  N N 344 
LYS CD     C  N N 345 
LYS CE     C  N N 346 
LYS NZ     N  N N 347 
LYS OXT    O  N N 348 
LYS H      H  N N 349 
LYS H2     H  N N 350 
LYS HA     H  N N 351 
LYS HB2    H  N N 352 
LYS HB3    H  N N 353 
LYS HG2    H  N N 354 
LYS HG3    H  N N 355 
LYS HD2    H  N N 356 
LYS HD3    H  N N 357 
LYS HE2    H  N N 358 
LYS HE3    H  N N 359 
LYS HZ1    H  N N 360 
LYS HZ2    H  N N 361 
LYS HZ3    H  N N 362 
LYS HXT    H  N N 363 
MET N      N  N N 364 
MET CA     C  N S 365 
MET C      C  N N 366 
MET O      O  N N 367 
MET CB     C  N N 368 
MET CG     C  N N 369 
MET SD     S  N N 370 
MET CE     C  N N 371 
MET OXT    O  N N 372 
MET H      H  N N 373 
MET H2     H  N N 374 
MET HA     H  N N 375 
MET HB2    H  N N 376 
MET HB3    H  N N 377 
MET HG2    H  N N 378 
MET HG3    H  N N 379 
MET HE1    H  N N 380 
MET HE2    H  N N 381 
MET HE3    H  N N 382 
MET HXT    H  N N 383 
MG  MG     MG N N 384 
PHE N      N  N N 385 
PHE CA     C  N S 386 
PHE C      C  N N 387 
PHE O      O  N N 388 
PHE CB     C  N N 389 
PHE CG     C  Y N 390 
PHE CD1    C  Y N 391 
PHE CD2    C  Y N 392 
PHE CE1    C  Y N 393 
PHE CE2    C  Y N 394 
PHE CZ     C  Y N 395 
PHE OXT    O  N N 396 
PHE H      H  N N 397 
PHE H2     H  N N 398 
PHE HA     H  N N 399 
PHE HB2    H  N N 400 
PHE HB3    H  N N 401 
PHE HD1    H  N N 402 
PHE HD2    H  N N 403 
PHE HE1    H  N N 404 
PHE HE2    H  N N 405 
PHE HZ     H  N N 406 
PHE HXT    H  N N 407 
PRO N      N  N N 408 
PRO CA     C  N S 409 
PRO C      C  N N 410 
PRO O      O  N N 411 
PRO CB     C  N N 412 
PRO CG     C  N N 413 
PRO CD     C  N N 414 
PRO OXT    O  N N 415 
PRO H      H  N N 416 
PRO HA     H  N N 417 
PRO HB2    H  N N 418 
PRO HB3    H  N N 419 
PRO HG2    H  N N 420 
PRO HG3    H  N N 421 
PRO HD2    H  N N 422 
PRO HD3    H  N N 423 
PRO HXT    H  N N 424 
SER N      N  N N 425 
SER CA     C  N S 426 
SER C      C  N N 427 
SER O      O  N N 428 
SER CB     C  N N 429 
SER OG     O  N N 430 
SER OXT    O  N N 431 
SER H      H  N N 432 
SER H2     H  N N 433 
SER HA     H  N N 434 
SER HB2    H  N N 435 
SER HB3    H  N N 436 
SER HG     H  N N 437 
SER HXT    H  N N 438 
THR N      N  N N 439 
THR CA     C  N S 440 
THR C      C  N N 441 
THR O      O  N N 442 
THR CB     C  N R 443 
THR OG1    O  N N 444 
THR CG2    C  N N 445 
THR OXT    O  N N 446 
THR H      H  N N 447 
THR H2     H  N N 448 
THR HA     H  N N 449 
THR HB     H  N N 450 
THR HG1    H  N N 451 
THR HG21   H  N N 452 
THR HG22   H  N N 453 
THR HG23   H  N N 454 
THR HXT    H  N N 455 
TRP N      N  N N 456 
TRP CA     C  N S 457 
TRP C      C  N N 458 
TRP O      O  N N 459 
TRP CB     C  N N 460 
TRP CG     C  Y N 461 
TRP CD1    C  Y N 462 
TRP CD2    C  Y N 463 
TRP NE1    N  Y N 464 
TRP CE2    C  Y N 465 
TRP CE3    C  Y N 466 
TRP CZ2    C  Y N 467 
TRP CZ3    C  Y N 468 
TRP CH2    C  Y N 469 
TRP OXT    O  N N 470 
TRP H      H  N N 471 
TRP H2     H  N N 472 
TRP HA     H  N N 473 
TRP HB2    H  N N 474 
TRP HB3    H  N N 475 
TRP HD1    H  N N 476 
TRP HE1    H  N N 477 
TRP HE3    H  N N 478 
TRP HZ2    H  N N 479 
TRP HZ3    H  N N 480 
TRP HH2    H  N N 481 
TRP HXT    H  N N 482 
TYR N      N  N N 483 
TYR CA     C  N S 484 
TYR C      C  N N 485 
TYR O      O  N N 486 
TYR CB     C  N N 487 
TYR CG     C  Y N 488 
TYR CD1    C  Y N 489 
TYR CD2    C  Y N 490 
TYR CE1    C  Y N 491 
TYR CE2    C  Y N 492 
TYR CZ     C  Y N 493 
TYR OH     O  N N 494 
TYR OXT    O  N N 495 
TYR H      H  N N 496 
TYR H2     H  N N 497 
TYR HA     H  N N 498 
TYR HB2    H  N N 499 
TYR HB3    H  N N 500 
TYR HD1    H  N N 501 
TYR HD2    H  N N 502 
TYR HE1    H  N N 503 
TYR HE2    H  N N 504 
TYR HH     H  N N 505 
TYR HXT    H  N N 506 
VAL N      N  N N 507 
VAL CA     C  N S 508 
VAL C      C  N N 509 
VAL O      O  N N 510 
VAL CB     C  N N 511 
VAL CG1    C  N N 512 
VAL CG2    C  N N 513 
VAL OXT    O  N N 514 
VAL H      H  N N 515 
VAL H2     H  N N 516 
VAL HA     H  N N 517 
VAL HB     H  N N 518 
VAL HG11   H  N N 519 
VAL HG12   H  N N 520 
VAL HG13   H  N N 521 
VAL HG21   H  N N 522 
VAL HG22   H  N N 523 
VAL HG23   H  N N 524 
VAL HXT    H  N N 525 
# 
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  
ANP PG    O1G    doub N N 57  
ANP PG    O2G    sing N N 58  
ANP PG    O3G    sing N N 59  
ANP PG    N3B    sing N N 60  
ANP O2G   HOG2   sing N N 61  
ANP O3G   HOG3   sing N N 62  
ANP PB    O1B    doub N N 63  
ANP PB    O2B    sing N N 64  
ANP PB    N3B    sing N N 65  
ANP PB    O3A    sing N N 66  
ANP O2B   HOB2   sing N N 67  
ANP N3B   HNB1   sing N N 68  
ANP PA    O1A    doub N N 69  
ANP PA    O2A    sing N N 70  
ANP PA    O3A    sing N N 71  
ANP PA    "O5'"  sing N N 72  
ANP O2A   HOA2   sing N N 73  
ANP "O5'" "C5'"  sing N N 74  
ANP "C5'" "C4'"  sing N N 75  
ANP "C5'" "H5'1" sing N N 76  
ANP "C5'" "H5'2" sing N N 77  
ANP "C4'" "O4'"  sing N N 78  
ANP "C4'" "C3'"  sing N N 79  
ANP "C4'" "H4'"  sing N N 80  
ANP "O4'" "C1'"  sing N N 81  
ANP "C3'" "O3'"  sing N N 82  
ANP "C3'" "C2'"  sing N N 83  
ANP "C3'" "H3'"  sing N N 84  
ANP "O3'" "HO3'" sing N N 85  
ANP "C2'" "O2'"  sing N N 86  
ANP "C2'" "C1'"  sing N N 87  
ANP "C2'" "H2'"  sing N N 88  
ANP "O2'" "HO2'" sing N N 89  
ANP "C1'" N9     sing N N 90  
ANP "C1'" "H1'"  sing N N 91  
ANP N9    C8     sing Y N 92  
ANP N9    C4     sing Y N 93  
ANP C8    N7     doub Y N 94  
ANP C8    H8     sing N N 95  
ANP N7    C5     sing Y N 96  
ANP C5    C6     sing Y N 97  
ANP C5    C4     doub Y N 98  
ANP C6    N6     sing N N 99  
ANP C6    N1     doub Y N 100 
ANP N6    HN61   sing N N 101 
ANP N6    HN62   sing N N 102 
ANP N1    C2     sing Y N 103 
ANP C2    N3     doub Y N 104 
ANP C2    H2     sing N N 105 
ANP N3    C4     sing Y N 106 
ARG N     CA     sing N N 107 
ARG N     H      sing N N 108 
ARG N     H2     sing N N 109 
ARG CA    C      sing N N 110 
ARG CA    CB     sing N N 111 
ARG CA    HA     sing N N 112 
ARG C     O      doub N N 113 
ARG C     OXT    sing N N 114 
ARG CB    CG     sing N N 115 
ARG CB    HB2    sing N N 116 
ARG CB    HB3    sing N N 117 
ARG CG    CD     sing N N 118 
ARG CG    HG2    sing N N 119 
ARG CG    HG3    sing N N 120 
ARG CD    NE     sing N N 121 
ARG CD    HD2    sing N N 122 
ARG CD    HD3    sing N N 123 
ARG NE    CZ     sing N N 124 
ARG NE    HE     sing N N 125 
ARG CZ    NH1    sing N N 126 
ARG CZ    NH2    doub N N 127 
ARG NH1   HH11   sing N N 128 
ARG NH1   HH12   sing N N 129 
ARG NH2   HH21   sing N N 130 
ARG NH2   HH22   sing N N 131 
ARG OXT   HXT    sing N N 132 
ASN N     CA     sing N N 133 
ASN N     H      sing N N 134 
ASN N     H2     sing N N 135 
ASN CA    C      sing N N 136 
ASN CA    CB     sing N N 137 
ASN CA    HA     sing N N 138 
ASN C     O      doub N N 139 
ASN C     OXT    sing N N 140 
ASN CB    CG     sing N N 141 
ASN CB    HB2    sing N N 142 
ASN CB    HB3    sing N N 143 
ASN CG    OD1    doub N N 144 
ASN CG    ND2    sing N N 145 
ASN ND2   HD21   sing N N 146 
ASN ND2   HD22   sing N N 147 
ASN OXT   HXT    sing N N 148 
ASP N     CA     sing N N 149 
ASP N     H      sing N N 150 
ASP N     H2     sing N N 151 
ASP CA    C      sing N N 152 
ASP CA    CB     sing N N 153 
ASP CA    HA     sing N N 154 
ASP C     O      doub N N 155 
ASP C     OXT    sing N N 156 
ASP CB    CG     sing N N 157 
ASP CB    HB2    sing N N 158 
ASP CB    HB3    sing N N 159 
ASP CG    OD1    doub N N 160 
ASP CG    OD2    sing N N 161 
ASP OD2   HD2    sing N N 162 
ASP OXT   HXT    sing N N 163 
ATP PG    O1G    doub N N 164 
ATP PG    O2G    sing N N 165 
ATP PG    O3G    sing N N 166 
ATP PG    O3B    sing N N 167 
ATP O2G   HOG2   sing N N 168 
ATP O3G   HOG3   sing N N 169 
ATP PB    O1B    doub N N 170 
ATP PB    O2B    sing N N 171 
ATP PB    O3B    sing N N 172 
ATP PB    O3A    sing N N 173 
ATP O2B   HOB2   sing N N 174 
ATP PA    O1A    doub N N 175 
ATP PA    O2A    sing N N 176 
ATP PA    O3A    sing N N 177 
ATP PA    "O5'"  sing N N 178 
ATP O2A   HOA2   sing N N 179 
ATP "O5'" "C5'"  sing N N 180 
ATP "C5'" "C4'"  sing N N 181 
ATP "C5'" "H5'1" sing N N 182 
ATP "C5'" "H5'2" sing N N 183 
ATP "C4'" "O4'"  sing N N 184 
ATP "C4'" "C3'"  sing N N 185 
ATP "C4'" "H4'"  sing N N 186 
ATP "O4'" "C1'"  sing N N 187 
ATP "C3'" "O3'"  sing N N 188 
ATP "C3'" "C2'"  sing N N 189 
ATP "C3'" "H3'"  sing N N 190 
ATP "O3'" "HO3'" sing N N 191 
ATP "C2'" "O2'"  sing N N 192 
ATP "C2'" "C1'"  sing N N 193 
ATP "C2'" "H2'"  sing N N 194 
ATP "O2'" "HO2'" sing N N 195 
ATP "C1'" N9     sing N N 196 
ATP "C1'" "H1'"  sing N N 197 
ATP N9    C8     sing Y N 198 
ATP N9    C4     sing Y N 199 
ATP C8    N7     doub Y N 200 
ATP C8    H8     sing N N 201 
ATP N7    C5     sing Y N 202 
ATP C5    C6     sing Y N 203 
ATP C5    C4     doub Y N 204 
ATP C6    N6     sing N N 205 
ATP C6    N1     doub Y N 206 
ATP N6    HN61   sing N N 207 
ATP N6    HN62   sing N N 208 
ATP N1    C2     sing Y N 209 
ATP C2    N3     doub Y N 210 
ATP C2    H2     sing N N 211 
ATP N3    C4     sing Y N 212 
CYS N     CA     sing N N 213 
CYS N     H      sing N N 214 
CYS N     H2     sing N N 215 
CYS CA    C      sing N N 216 
CYS CA    CB     sing N N 217 
CYS CA    HA     sing N N 218 
CYS C     O      doub N N 219 
CYS C     OXT    sing N N 220 
CYS CB    SG     sing N N 221 
CYS CB    HB2    sing N N 222 
CYS CB    HB3    sing N N 223 
CYS SG    HG     sing N N 224 
CYS OXT   HXT    sing N N 225 
GLN N     CA     sing N N 226 
GLN N     H      sing N N 227 
GLN N     H2     sing N N 228 
GLN CA    C      sing N N 229 
GLN CA    CB     sing N N 230 
GLN CA    HA     sing N N 231 
GLN C     O      doub N N 232 
GLN C     OXT    sing N N 233 
GLN CB    CG     sing N N 234 
GLN CB    HB2    sing N N 235 
GLN CB    HB3    sing N N 236 
GLN CG    CD     sing N N 237 
GLN CG    HG2    sing N N 238 
GLN CG    HG3    sing N N 239 
GLN CD    OE1    doub N N 240 
GLN CD    NE2    sing N N 241 
GLN NE2   HE21   sing N N 242 
GLN NE2   HE22   sing N N 243 
GLN OXT   HXT    sing N N 244 
GLU N     CA     sing N N 245 
GLU N     H      sing N N 246 
GLU N     H2     sing N N 247 
GLU CA    C      sing N N 248 
GLU CA    CB     sing N N 249 
GLU CA    HA     sing N N 250 
GLU C     O      doub N N 251 
GLU C     OXT    sing N N 252 
GLU CB    CG     sing N N 253 
GLU CB    HB2    sing N N 254 
GLU CB    HB3    sing N N 255 
GLU CG    CD     sing N N 256 
GLU CG    HG2    sing N N 257 
GLU CG    HG3    sing N N 258 
GLU CD    OE1    doub N N 259 
GLU CD    OE2    sing N N 260 
GLU OE2   HE2    sing N N 261 
GLU OXT   HXT    sing N N 262 
GLY N     CA     sing N N 263 
GLY N     H      sing N N 264 
GLY N     H2     sing N N 265 
GLY CA    C      sing N N 266 
GLY CA    HA2    sing N N 267 
GLY CA    HA3    sing N N 268 
GLY C     O      doub N N 269 
GLY C     OXT    sing N N 270 
GLY OXT   HXT    sing N N 271 
HIS N     CA     sing N N 272 
HIS N     H      sing N N 273 
HIS N     H2     sing N N 274 
HIS CA    C      sing N N 275 
HIS CA    CB     sing N N 276 
HIS CA    HA     sing N N 277 
HIS C     O      doub N N 278 
HIS C     OXT    sing N N 279 
HIS CB    CG     sing N N 280 
HIS CB    HB2    sing N N 281 
HIS CB    HB3    sing N N 282 
HIS CG    ND1    sing Y N 283 
HIS CG    CD2    doub Y N 284 
HIS ND1   CE1    doub Y N 285 
HIS ND1   HD1    sing N N 286 
HIS CD2   NE2    sing Y N 287 
HIS CD2   HD2    sing N N 288 
HIS CE1   NE2    sing Y N 289 
HIS CE1   HE1    sing N N 290 
HIS NE2   HE2    sing N N 291 
HIS OXT   HXT    sing N N 292 
ILE N     CA     sing N N 293 
ILE N     H      sing N N 294 
ILE N     H2     sing N N 295 
ILE CA    C      sing N N 296 
ILE CA    CB     sing N N 297 
ILE CA    HA     sing N N 298 
ILE C     O      doub N N 299 
ILE C     OXT    sing N N 300 
ILE CB    CG1    sing N N 301 
ILE CB    CG2    sing N N 302 
ILE CB    HB     sing N N 303 
ILE CG1   CD1    sing N N 304 
ILE CG1   HG12   sing N N 305 
ILE CG1   HG13   sing N N 306 
ILE CG2   HG21   sing N N 307 
ILE CG2   HG22   sing N N 308 
ILE CG2   HG23   sing N N 309 
ILE CD1   HD11   sing N N 310 
ILE CD1   HD12   sing N N 311 
ILE CD1   HD13   sing N N 312 
ILE OXT   HXT    sing N N 313 
LEU N     CA     sing N N 314 
LEU N     H      sing N N 315 
LEU N     H2     sing N N 316 
LEU CA    C      sing N N 317 
LEU CA    CB     sing N N 318 
LEU CA    HA     sing N N 319 
LEU C     O      doub N N 320 
LEU C     OXT    sing N N 321 
LEU CB    CG     sing N N 322 
LEU CB    HB2    sing N N 323 
LEU CB    HB3    sing N N 324 
LEU CG    CD1    sing N N 325 
LEU CG    CD2    sing N N 326 
LEU CG    HG     sing N N 327 
LEU CD1   HD11   sing N N 328 
LEU CD1   HD12   sing N N 329 
LEU CD1   HD13   sing N N 330 
LEU CD2   HD21   sing N N 331 
LEU CD2   HD22   sing N N 332 
LEU CD2   HD23   sing N N 333 
LEU OXT   HXT    sing N N 334 
LYS N     CA     sing N N 335 
LYS N     H      sing N N 336 
LYS N     H2     sing N N 337 
LYS CA    C      sing N N 338 
LYS CA    CB     sing N N 339 
LYS CA    HA     sing N N 340 
LYS C     O      doub N N 341 
LYS C     OXT    sing N N 342 
LYS CB    CG     sing N N 343 
LYS CB    HB2    sing N N 344 
LYS CB    HB3    sing N N 345 
LYS CG    CD     sing N N 346 
LYS CG    HG2    sing N N 347 
LYS CG    HG3    sing N N 348 
LYS CD    CE     sing N N 349 
LYS CD    HD2    sing N N 350 
LYS CD    HD3    sing N N 351 
LYS CE    NZ     sing N N 352 
LYS CE    HE2    sing N N 353 
LYS CE    HE3    sing N N 354 
LYS NZ    HZ1    sing N N 355 
LYS NZ    HZ2    sing N N 356 
LYS NZ    HZ3    sing N N 357 
LYS OXT   HXT    sing N N 358 
MET N     CA     sing N N 359 
MET N     H      sing N N 360 
MET N     H2     sing N N 361 
MET CA    C      sing N N 362 
MET CA    CB     sing N N 363 
MET CA    HA     sing N N 364 
MET C     O      doub N N 365 
MET C     OXT    sing N N 366 
MET CB    CG     sing N N 367 
MET CB    HB2    sing N N 368 
MET CB    HB3    sing N N 369 
MET CG    SD     sing N N 370 
MET CG    HG2    sing N N 371 
MET CG    HG3    sing N N 372 
MET SD    CE     sing N N 373 
MET CE    HE1    sing N N 374 
MET CE    HE2    sing N N 375 
MET CE    HE3    sing N N 376 
MET OXT   HXT    sing N N 377 
PHE N     CA     sing N N 378 
PHE N     H      sing N N 379 
PHE N     H2     sing N N 380 
PHE CA    C      sing N N 381 
PHE CA    CB     sing N N 382 
PHE CA    HA     sing N N 383 
PHE C     O      doub N N 384 
PHE C     OXT    sing N N 385 
PHE CB    CG     sing N N 386 
PHE CB    HB2    sing N N 387 
PHE CB    HB3    sing N N 388 
PHE CG    CD1    doub Y N 389 
PHE CG    CD2    sing Y N 390 
PHE CD1   CE1    sing Y N 391 
PHE CD1   HD1    sing N N 392 
PHE CD2   CE2    doub Y N 393 
PHE CD2   HD2    sing N N 394 
PHE CE1   CZ     doub Y N 395 
PHE CE1   HE1    sing N N 396 
PHE CE2   CZ     sing Y N 397 
PHE CE2   HE2    sing N N 398 
PHE CZ    HZ     sing N N 399 
PHE OXT   HXT    sing N N 400 
PRO N     CA     sing N N 401 
PRO N     CD     sing N N 402 
PRO N     H      sing N N 403 
PRO CA    C      sing N N 404 
PRO CA    CB     sing N N 405 
PRO CA    HA     sing N N 406 
PRO C     O      doub N N 407 
PRO C     OXT    sing N N 408 
PRO CB    CG     sing N N 409 
PRO CB    HB2    sing N N 410 
PRO CB    HB3    sing N N 411 
PRO CG    CD     sing N N 412 
PRO CG    HG2    sing N N 413 
PRO CG    HG3    sing N N 414 
PRO CD    HD2    sing N N 415 
PRO CD    HD3    sing N N 416 
PRO OXT   HXT    sing N N 417 
SER N     CA     sing N N 418 
SER N     H      sing N N 419 
SER N     H2     sing N N 420 
SER CA    C      sing N N 421 
SER CA    CB     sing N N 422 
SER CA    HA     sing N N 423 
SER C     O      doub N N 424 
SER C     OXT    sing N N 425 
SER CB    OG     sing N N 426 
SER CB    HB2    sing N N 427 
SER CB    HB3    sing N N 428 
SER OG    HG     sing N N 429 
SER OXT   HXT    sing N N 430 
THR N     CA     sing N N 431 
THR N     H      sing N N 432 
THR N     H2     sing N N 433 
THR CA    C      sing N N 434 
THR CA    CB     sing N N 435 
THR CA    HA     sing N N 436 
THR C     O      doub N N 437 
THR C     OXT    sing N N 438 
THR CB    OG1    sing N N 439 
THR CB    CG2    sing N N 440 
THR CB    HB     sing N N 441 
THR OG1   HG1    sing N N 442 
THR CG2   HG21   sing N N 443 
THR CG2   HG22   sing N N 444 
THR CG2   HG23   sing N N 445 
THR OXT   HXT    sing N N 446 
TRP N     CA     sing N N 447 
TRP N     H      sing N N 448 
TRP N     H2     sing N N 449 
TRP CA    C      sing N N 450 
TRP CA    CB     sing N N 451 
TRP CA    HA     sing N N 452 
TRP C     O      doub N N 453 
TRP C     OXT    sing N N 454 
TRP CB    CG     sing N N 455 
TRP CB    HB2    sing N N 456 
TRP CB    HB3    sing N N 457 
TRP CG    CD1    doub Y N 458 
TRP CG    CD2    sing Y N 459 
TRP CD1   NE1    sing Y N 460 
TRP CD1   HD1    sing N N 461 
TRP CD2   CE2    doub Y N 462 
TRP CD2   CE3    sing Y N 463 
TRP NE1   CE2    sing Y N 464 
TRP NE1   HE1    sing N N 465 
TRP CE2   CZ2    sing Y N 466 
TRP CE3   CZ3    doub Y N 467 
TRP CE3   HE3    sing N N 468 
TRP CZ2   CH2    doub Y N 469 
TRP CZ2   HZ2    sing N N 470 
TRP CZ3   CH2    sing Y N 471 
TRP CZ3   HZ3    sing N N 472 
TRP CH2   HH2    sing N N 473 
TRP OXT   HXT    sing N N 474 
TYR N     CA     sing N N 475 
TYR N     H      sing N N 476 
TYR N     H2     sing N N 477 
TYR CA    C      sing N N 478 
TYR CA    CB     sing N N 479 
TYR CA    HA     sing N N 480 
TYR C     O      doub N N 481 
TYR C     OXT    sing N N 482 
TYR CB    CG     sing N N 483 
TYR CB    HB2    sing N N 484 
TYR CB    HB3    sing N N 485 
TYR CG    CD1    doub Y N 486 
TYR CG    CD2    sing Y N 487 
TYR CD1   CE1    sing Y N 488 
TYR CD1   HD1    sing N N 489 
TYR CD2   CE2    doub Y N 490 
TYR CD2   HD2    sing N N 491 
TYR CE1   CZ     doub Y N 492 
TYR CE1   HE1    sing N N 493 
TYR CE2   CZ     sing Y N 494 
TYR CE2   HE2    sing N N 495 
TYR CZ    OH     sing N N 496 
TYR OH    HH     sing N N 497 
TYR OXT   HXT    sing N N 498 
VAL N     CA     sing N N 499 
VAL N     H      sing N N 500 
VAL N     H2     sing N N 501 
VAL CA    C      sing N N 502 
VAL CA    CB     sing N N 503 
VAL CA    HA     sing N N 504 
VAL C     O      doub N N 505 
VAL C     OXT    sing N N 506 
VAL CB    CG1    sing N N 507 
VAL CB    CG2    sing N N 508 
VAL CB    HB     sing N N 509 
VAL CG1   HG11   sing N N 510 
VAL CG1   HG12   sing N N 511 
VAL CG1   HG13   sing N N 512 
VAL CG2   HG21   sing N N 513 
VAL CG2   HG22   sing N N 514 
VAL CG2   HG23   sing N N 515 
VAL OXT   HXT    sing N N 516 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-05-02 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BMD 
_em_admin.last_update        2025-05-28 
_em_admin.map_release_date   2025-04-23 
_em_admin.title              'Motor domain from full-length human dynein-1 bound to microtubules in 5mM AMPPNP condition' 
# 
_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 EPU       ? 
MASKING                    ? 3  ? ? ? ?         ? 
'CTF CORRECTION'           ? 4  1 ? ? ?         ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ?         ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?         ? 
'MODEL FITTING'            ? 7  ? ? ? ?         ? 
'MODEL REFINEMENT'         ? 8  ? ? ? PHENIX    ? 
OTHER                      ? 9  ? ? ? ?         ? 
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ?         ? 
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? cryoSPARC 4 
CLASSIFICATION             ? 12 1 ? ? ?         ? 
RECONSTRUCTION             ? 13 1 ? ? cryoSPARC 4 
# 
_em_specimen.concentration           2 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R35GM142959 1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R35GM139483 2 
# 
_atom_sites.entry_id                    9BMD 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . GLN A 1 1327 ? 170.245 155.760 249.797 1.00 160.17 ? 1327 GLN A N     1 
ATOM   2     C  CA    . GLN A 1 1327 ? 168.827 155.877 249.481 1.00 161.51 ? 1327 GLN A CA    1 
ATOM   3     C  C     . GLN A 1 1327 ? 168.602 155.847 247.975 1.00 164.17 ? 1327 GLN A C     1 
ATOM   4     O  O     . GLN A 1 1327 ? 169.401 155.279 247.230 1.00 164.40 ? 1327 GLN A O     1 
ATOM   5     C  CB    . GLN A 1 1327 ? 168.248 157.164 250.074 1.00 160.83 ? 1327 GLN A CB    1 
ATOM   6     C  CG    . GLN A 1 1327 ? 168.298 157.232 251.592 1.00 159.48 ? 1327 GLN A CG    1 
ATOM   7     C  CD    . GLN A 1 1327 ? 167.272 156.332 252.256 1.00 160.54 ? 1327 GLN A CD    1 
ATOM   8     O  OE1   . GLN A 1 1327 ? 166.432 155.728 251.590 1.00 162.75 ? 1327 GLN A OE1   1 
ATOM   9     N  NE2   . GLN A 1 1327 ? 167.337 156.241 253.579 1.00 153.29 ? 1327 GLN A NE2   1 
ATOM   10    N  N     . ASP A 1 1328 ? 167.501 156.460 247.533 1.00 165.69 ? 1328 ASP A N     1 
ATOM   11    C  CA    . ASP A 1 1328 ? 167.228 156.547 246.102 1.00 168.38 ? 1328 ASP A CA    1 
ATOM   12    C  C     . ASP A 1 1328 ? 168.298 157.364 245.389 1.00 167.64 ? 1328 ASP A C     1 
ATOM   13    O  O     . ASP A 1 1328 ? 168.721 157.015 244.280 1.00 166.63 ? 1328 ASP A O     1 
ATOM   14    C  CB    . ASP A 1 1328 ? 165.844 157.150 245.866 1.00 167.50 ? 1328 ASP A CB    1 
ATOM   15    C  CG    . ASP A 1 1328 ? 164.773 156.503 246.722 1.00 164.84 ? 1328 ASP A CG    1 
ATOM   16    O  OD1   . ASP A 1 1328 ? 164.602 155.269 246.631 1.00 164.48 ? 1328 ASP A OD1   1 
ATOM   17    O  OD2   . ASP A 1 1328 ? 164.102 157.228 247.486 1.00 163.13 ? 1328 ASP A OD2   1 
ATOM   18    N  N     . LEU A 1 1329 ? 168.743 158.460 246.009 1.00 167.37 ? 1329 LEU A N     1 
ATOM   19    C  CA    . LEU A 1 1329 ? 169.785 159.279 245.399 1.00 167.16 ? 1329 LEU A CA    1 
ATOM   20    C  C     . LEU A 1 1329 ? 171.098 158.511 245.286 1.00 167.85 ? 1329 LEU A C     1 
ATOM   21    O  O     . LEU A 1 1329 ? 171.786 158.596 244.264 1.00 167.06 ? 1329 LEU A O     1 
ATOM   22    C  CB    . LEU A 1 1329 ? 169.968 160.577 246.190 1.00 166.32 ? 1329 LEU A CB    1 
ATOM   23    C  CG    . LEU A 1 1329 ? 170.349 160.522 247.673 1.00 164.78 ? 1329 LEU A CG    1 
ATOM   24    C  CD1   . LEU A 1 1329 ? 171.859 160.616 247.862 1.00 161.36 ? 1329 LEU A CD1   1 
ATOM   25    C  CD2   . LEU A 1 1329 ? 169.635 161.623 248.446 1.00 159.53 ? 1329 LEU A CD2   1 
ATOM   26    N  N     . LYS A 1 1330 ? 171.457 157.742 246.316 1.00 167.34 ? 1330 LYS A N     1 
ATOM   27    C  CA    . LYS A 1 1330 ? 172.682 156.952 246.244 1.00 165.12 ? 1330 LYS A CA    1 
ATOM   28    C  C     . LYS A 1 1330 ? 172.584 155.883 245.161 1.00 163.70 ? 1330 LYS A C     1 
ATOM   29    O  O     . LYS A 1 1330 ? 173.546 155.644 244.420 1.00 159.56 ? 1330 LYS A O     1 
ATOM   30    C  CB    . LYS A 1 1330 ? 172.980 156.321 247.604 1.00 161.71 ? 1330 LYS A CB    1 
ATOM   31    C  CG    . LYS A 1 1330 ? 174.197 155.413 247.619 1.00 161.76 ? 1330 LYS A CG    1 
ATOM   32    C  CD    . LYS A 1 1330 ? 174.449 154.864 249.013 1.00 159.40 ? 1330 LYS A CD    1 
ATOM   33    C  CE    . LYS A 1 1330 ? 175.669 153.958 249.041 1.00 152.76 ? 1330 LYS A CE    1 
ATOM   34    N  NZ    . LYS A 1 1330 ? 175.940 153.441 250.411 1.00 150.88 ? 1330 LYS A NZ    1 
ATOM   35    N  N     . GLY A 1 1331 ? 171.422 155.236 245.049 1.00 162.76 ? 1331 GLY A N     1 
ATOM   36    C  CA    . GLY A 1 1331 ? 171.243 154.237 244.009 1.00 159.86 ? 1331 GLY A CA    1 
ATOM   37    C  C     . GLY A 1 1331 ? 171.321 154.824 242.613 1.00 162.39 ? 1331 GLY A C     1 
ATOM   38    O  O     . GLY A 1 1331 ? 171.943 154.243 241.718 1.00 159.50 ? 1331 GLY A O     1 
ATOM   39    N  N     . VAL A 1 1332 ? 170.690 155.983 242.403 1.00 165.05 ? 1332 VAL A N     1 
ATOM   40    C  CA    . VAL A 1 1332 ? 170.753 156.595 241.081 1.00 163.59 ? 1332 VAL A CA    1 
ATOM   41    C  C     . VAL A 1 1332 ? 172.161 157.104 240.797 1.00 163.27 ? 1332 VAL A C     1 
ATOM   42    O  O     . VAL A 1 1332 ? 172.602 157.094 239.646 1.00 160.48 ? 1332 VAL A O     1 
ATOM   43    C  CB    . VAL A 1 1332 ? 169.695 157.707 240.925 1.00 163.51 ? 1332 VAL A CB    1 
ATOM   44    C  CG1   . VAL A 1 1332 ? 170.007 158.897 241.807 1.00 161.11 ? 1332 VAL A CG1   1 
ATOM   45    C  CG2   . VAL A 1 1332 ? 169.574 158.129 239.465 1.00 162.45 ? 1332 VAL A CG2   1 
ATOM   46    N  N     . TRP A 1 1333 ? 172.900 157.530 241.828 1.00 165.07 ? 1333 TRP A N     1 
ATOM   47    C  CA    . TRP A 1 1333 ? 174.305 157.876 241.630 1.00 164.14 ? 1333 TRP A CA    1 
ATOM   48    C  C     . TRP A 1 1333 ? 175.115 156.661 241.193 1.00 162.56 ? 1333 TRP A C     1 
ATOM   49    O  O     . TRP A 1 1333 ? 175.969 156.761 240.306 1.00 161.24 ? 1333 TRP A O     1 
ATOM   50    C  CB    . TRP A 1 1333 ? 174.898 158.474 242.909 1.00 163.25 ? 1333 TRP A CB    1 
ATOM   51    C  CG    . TRP A 1 1333 ? 174.525 159.910 243.187 1.00 165.16 ? 1333 TRP A CG    1 
ATOM   52    C  CD1   . TRP A 1 1333 ? 174.047 160.414 244.362 1.00 167.31 ? 1333 TRP A CD1   1 
ATOM   53    C  CD2   . TRP A 1 1333 ? 174.635 161.026 242.291 1.00 166.63 ? 1333 TRP A CD2   1 
ATOM   54    N  NE1   . TRP A 1 1333 ? 173.832 161.766 244.248 1.00 169.20 ? 1333 TRP A NE1   1 
ATOM   55    C  CE2   . TRP A 1 1333 ? 174.188 162.167 242.988 1.00 169.62 ? 1333 TRP A CE2   1 
ATOM   56    C  CE3   . TRP A 1 1333 ? 175.061 161.171 240.966 1.00 161.23 ? 1333 TRP A CE3   1 
ATOM   57    C  CZ2   . TRP A 1 1333 ? 174.153 163.432 242.407 1.00 164.83 ? 1333 TRP A CZ2   1 
ATOM   58    C  CZ3   . TRP A 1 1333 ? 175.025 162.430 240.392 1.00 160.15 ? 1333 TRP A CZ3   1 
ATOM   59    C  CH2   . TRP A 1 1333 ? 174.575 163.542 241.111 1.00 160.52 ? 1333 TRP A CH2   1 
ATOM   60    N  N     . SER A 1 1334 ? 174.866 155.504 241.811 1.00 160.29 ? 1334 SER A N     1 
ATOM   61    C  CA    . SER A 1 1334 ? 175.585 154.291 241.428 1.00 158.66 ? 1334 SER A CA    1 
ATOM   62    C  C     . SER A 1 1334 ? 175.260 153.887 239.993 1.00 159.08 ? 1334 SER A C     1 
ATOM   63    O  O     . SER A 1 1334 ? 176.154 153.531 239.213 1.00 158.61 ? 1334 SER A O     1 
ATOM   64    C  CB    . SER A 1 1334 ? 175.252 153.156 242.397 1.00 158.41 ? 1334 SER A CB    1 
ATOM   65    O  OG    . SER A 1 1334 ? 175.861 151.943 241.990 1.00 153.80 ? 1334 SER A OG    1 
ATOM   66    N  N     . GLU A 1 1335 ? 173.977 153.935 239.625 1.00 161.37 ? 1335 GLU A N     1 
ATOM   67    C  CA    . GLU A 1 1335 ? 173.595 153.603 238.254 1.00 160.39 ? 1335 GLU A CA    1 
ATOM   68    C  C     . GLU A 1 1335 ? 174.169 154.609 237.264 1.00 158.40 ? 1335 GLU A C     1 
ATOM   69    O  O     . GLU A 1 1335 ? 174.583 154.239 236.158 1.00 159.12 ? 1335 GLU A O     1 
ATOM   70    C  CB    . GLU A 1 1335 ? 172.073 153.528 238.130 1.00 159.64 ? 1335 GLU A CB    1 
ATOM   71    C  CG    . GLU A 1 1335 ? 171.407 152.584 239.123 1.00 157.49 ? 1335 GLU A CG    1 
ATOM   72    C  CD    . GLU A 1 1335 ? 171.613 151.118 238.783 1.00 157.36 ? 1335 GLU A CD    1 
ATOM   73    O  OE1   . GLU A 1 1335 ? 172.216 150.820 237.729 1.00 157.10 ? 1335 GLU A OE1   1 
ATOM   74    O  OE2   . GLU A 1 1335 ? 171.168 150.260 239.573 1.00 154.77 ? 1335 GLU A OE2   1 
ATOM   75    N  N     . LEU A 1 1336 ? 174.205 155.887 237.646 1.00 156.82 ? 1336 LEU A N     1 
ATOM   76    C  CA    . LEU A 1 1336 ? 174.825 156.906 236.811 1.00 158.14 ? 1336 LEU A CA    1 
ATOM   77    C  C     . LEU A 1 1336 ? 176.304 156.621 236.609 1.00 158.87 ? 1336 LEU A C     1 
ATOM   78    O  O     . LEU A 1 1336 ? 176.830 156.786 235.505 1.00 157.54 ? 1336 LEU A O     1 
ATOM   79    C  CB    . LEU A 1 1336 ? 174.639 158.281 237.448 1.00 156.40 ? 1336 LEU A CB    1 
ATOM   80    C  CG    . LEU A 1 1336 ? 175.149 159.438 236.595 1.00 156.59 ? 1336 LEU A CG    1 
ATOM   81    C  CD1   . LEU A 1 1336 ? 174.307 159.530 235.346 1.00 155.43 ? 1336 LEU A CD1   1 
ATOM   82    C  CD2   . LEU A 1 1336 ? 175.136 160.740 237.364 1.00 152.71 ? 1336 LEU A CD2   1 
ATOM   83    N  N     . SER A 1 1337 ? 176.993 156.208 237.673 1.00 158.14 ? 1337 SER A N     1 
ATOM   84    C  CA    . SER A 1 1337 ? 178.402 155.856 237.553 1.00 156.14 ? 1337 SER A CA    1 
ATOM   85    C  C     . SER A 1 1337 ? 178.591 154.667 236.621 1.00 158.02 ? 1337 SER A C     1 
ATOM   86    O  O     . SER A 1 1337 ? 179.525 154.648 235.814 1.00 160.50 ? 1337 SER A O     1 
ATOM   87    C  CB    . SER A 1 1337 ? 178.990 155.559 238.933 1.00 155.06 ? 1337 SER A CB    1 
ATOM   88    O  OG    . SER A 1 1337 ? 178.337 154.456 239.538 1.00 157.22 ? 1337 SER A OG    1 
ATOM   89    N  N     . LYS A 1 1338 ? 177.713 153.667 236.716 1.00 158.12 ? 1338 LYS A N     1 
ATOM   90    C  CA    . LYS A 1 1338 ? 177.809 152.515 235.820 1.00 158.02 ? 1338 LYS A CA    1 
ATOM   91    C  C     . LYS A 1 1338 ? 177.617 152.932 234.363 1.00 159.90 ? 1338 LYS A C     1 
ATOM   92    O  O     . LYS A 1 1338 ? 178.369 152.506 233.474 1.00 158.66 ? 1338 LYS A O     1 
ATOM   93    C  CB    . LYS A 1 1338 ? 176.782 151.453 236.216 1.00 154.04 ? 1338 LYS A CB    1 
ATOM   94    C  CG    . LYS A 1 1338 ? 177.326 150.350 237.114 1.00 153.00 ? 1338 LYS A CG    1 
ATOM   95    C  CD    . LYS A 1 1338 ? 177.959 150.910 238.378 1.00 153.03 ? 1338 LYS A CD    1 
ATOM   96    C  CE    . LYS A 1 1338 ? 178.420 149.799 239.306 1.00 146.54 ? 1338 LYS A CE    1 
ATOM   97    N  NZ    . LYS A 1 1338 ? 178.968 150.337 240.581 1.00 144.02 ? 1338 LYS A NZ    1 
ATOM   98    N  N     . VAL A 1 1339 ? 176.615 153.774 234.103 1.00 161.13 ? 1339 VAL A N     1 
ATOM   99    C  CA    . VAL A 1 1339 ? 176.370 154.236 232.739 1.00 159.78 ? 1339 VAL A CA    1 
ATOM   100   C  C     . VAL A 1 1339 ? 177.539 155.078 232.240 1.00 157.25 ? 1339 VAL A C     1 
ATOM   101   O  O     . VAL A 1 1339 ? 177.930 154.990 231.071 1.00 156.31 ? 1339 VAL A O     1 
ATOM   102   C  CB    . VAL A 1 1339 ? 175.039 155.006 232.665 1.00 159.53 ? 1339 VAL A CB    1 
ATOM   103   C  CG1   . VAL A 1 1339 ? 174.804 155.528 231.257 1.00 157.55 ? 1339 VAL A CG1   1 
ATOM   104   C  CG2   . VAL A 1 1339 ? 173.892 154.106 233.088 1.00 159.95 ? 1339 VAL A CG2   1 
ATOM   105   N  N     . TRP A 1 1340 ? 178.116 155.904 233.115 1.00 158.60 ? 1340 TRP A N     1 
ATOM   106   C  CA    . TRP A 1 1340 ? 179.276 156.700 232.733 1.00 159.63 ? 1340 TRP A CA    1 
ATOM   107   C  C     . TRP A 1 1340 ? 180.471 155.814 232.413 1.00 159.81 ? 1340 TRP A C     1 
ATOM   108   O  O     . TRP A 1 1340 ? 181.239 156.108 231.492 1.00 159.85 ? 1340 TRP A O     1 
ATOM   109   C  CB    . TRP A 1 1340 ? 179.625 157.691 233.844 1.00 159.17 ? 1340 TRP A CB    1 
ATOM   110   C  CG    . TRP A 1 1340 ? 178.933 159.013 233.713 1.00 158.74 ? 1340 TRP A CG    1 
ATOM   111   C  CD1   . TRP A 1 1340 ? 178.068 159.575 234.605 1.00 158.04 ? 1340 TRP A CD1   1 
ATOM   112   C  CD2   . TRP A 1 1340 ? 179.049 159.941 232.627 1.00 162.78 ? 1340 TRP A CD2   1 
ATOM   113   N  NE1   . TRP A 1 1340 ? 177.637 160.794 234.143 1.00 157.82 ? 1340 TRP A NE1   1 
ATOM   114   C  CE2   . TRP A 1 1340 ? 178.224 161.043 232.930 1.00 161.62 ? 1340 TRP A CE2   1 
ATOM   115   C  CE3   . TRP A 1 1340 ? 179.769 159.948 231.428 1.00 163.92 ? 1340 TRP A CE3   1 
ATOM   116   C  CZ2   . TRP A 1 1340 ? 178.099 162.139 232.080 1.00 161.33 ? 1340 TRP A CZ2   1 
ATOM   117   C  CZ3   . TRP A 1 1340 ? 179.644 161.038 230.584 1.00 165.11 ? 1340 TRP A CZ3   1 
ATOM   118   C  CH2   . TRP A 1 1340 ? 178.815 162.118 230.915 1.00 164.57 ? 1340 TRP A CH2   1 
ATOM   119   N  N     . GLU A 1 1341 ? 180.654 154.730 233.170 1.00 159.68 ? 1341 GLU A N     1 
ATOM   120   C  CA    . GLU A 1 1341 ? 181.728 153.791 232.860 1.00 159.66 ? 1341 GLU A CA    1 
ATOM   121   C  C     . GLU A 1 1341 ? 181.508 153.130 231.505 1.00 159.61 ? 1341 GLU A C     1 
ATOM   122   O  O     . GLU A 1 1341 ? 182.456 152.967 230.729 1.00 159.28 ? 1341 GLU A O     1 
ATOM   123   C  CB    . GLU A 1 1341 ? 181.852 152.733 233.958 1.00 160.25 ? 1341 GLU A CB    1 
ATOM   124   C  CG    . GLU A 1 1341 ? 182.226 153.276 235.332 1.00 158.14 ? 1341 GLU A CG    1 
ATOM   125   C  CD    . GLU A 1 1341 ? 183.111 154.506 235.265 1.00 161.76 ? 1341 GLU A CD    1 
ATOM   126   O  OE1   . GLU A 1 1341 ? 184.242 154.405 234.743 1.00 162.28 ? 1341 GLU A OE1   1 
ATOM   127   O  OE2   . GLU A 1 1341 ? 182.675 155.577 235.737 1.00 162.64 ? 1341 GLU A OE2   1 
ATOM   128   N  N     . GLN A 1 1342 ? 180.266 152.741 231.203 1.00 159.95 ? 1342 GLN A N     1 
ATOM   129   C  CA    . GLN A 1 1342 ? 179.981 152.177 229.884 1.00 160.54 ? 1342 GLN A CA    1 
ATOM   130   C  C     . GLN A 1 1342 ? 180.262 153.188 228.776 1.00 159.82 ? 1342 GLN A C     1 
ATOM   131   O  O     . GLN A 1 1342 ? 180.856 152.847 227.743 1.00 156.97 ? 1342 GLN A O     1 
ATOM   132   C  CB    . GLN A 1 1342 ? 178.531 151.694 229.814 1.00 158.51 ? 1342 GLN A CB    1 
ATOM   133   C  CG    . GLN A 1 1342 ? 178.151 150.681 230.882 1.00 158.50 ? 1342 GLN A CG    1 
ATOM   134   C  CD    . GLN A 1 1342 ? 178.745 149.306 230.626 1.00 158.83 ? 1342 GLN A CD    1 
ATOM   135   O  OE1   . GLN A 1 1342 ? 179.350 149.060 229.582 1.00 156.93 ? 1342 GLN A OE1   1 
ATOM   136   N  NE2   . GLN A 1 1342 ? 178.569 148.400 231.582 1.00 157.61 ? 1342 GLN A NE2   1 
ATOM   137   N  N     . ILE A 1 1343 ? 179.852 154.442 228.979 1.00 162.04 ? 1343 ILE A N     1 
ATOM   138   C  CA    . ILE A 1 1343 ? 180.103 155.480 227.983 1.00 161.16 ? 1343 ILE A CA    1 
ATOM   139   C  C     . ILE A 1 1343 ? 181.599 155.692 227.798 1.00 159.04 ? 1343 ILE A C     1 
ATOM   140   O  O     . ILE A 1 1343 ? 182.082 155.852 226.673 1.00 158.24 ? 1343 ILE A O     1 
ATOM   141   C  CB    . ILE A 1 1343 ? 179.385 156.786 228.373 1.00 161.53 ? 1343 ILE A CB    1 
ATOM   142   C  CG1   . ILE A 1 1343 ? 177.867 156.589 228.347 1.00 157.60 ? 1343 ILE A CG1   1 
ATOM   143   C  CG2   . ILE A 1 1343 ? 179.792 157.923 227.447 1.00 156.18 ? 1343 ILE A CG2   1 
ATOM   144   C  CD1   . ILE A 1 1343 ? 177.089 157.775 228.872 1.00 154.35 ? 1343 ILE A CD1   1 
ATOM   145   N  N     . ASP A 1 1344 ? 182.357 155.698 228.898 1.00 159.63 ? 1344 ASP A N     1 
ATOM   146   C  CA    . ASP A 1 1344 ? 183.805 155.859 228.804 1.00 159.06 ? 1344 ASP A CA    1 
ATOM   147   C  C     . ASP A 1 1344 ? 184.446 154.698 228.053 1.00 158.93 ? 1344 ASP A C     1 
ATOM   148   O  O     . ASP A 1 1344 ? 185.338 154.909 227.224 1.00 158.93 ? 1344 ASP A O     1 
ATOM   149   C  CB    . ASP A 1 1344 ? 184.412 155.998 230.199 1.00 158.88 ? 1344 ASP A CB    1 
ATOM   150   C  CG    . ASP A 1 1344 ? 184.096 157.333 230.840 1.00 162.83 ? 1344 ASP A CG    1 
ATOM   151   O  OD1   . ASP A 1 1344 ? 183.463 158.178 230.173 1.00 161.50 ? 1344 ASP A OD1   1 
ATOM   152   O  OD2   . ASP A 1 1344 ? 184.481 157.539 232.010 1.00 165.05 ? 1344 ASP A OD2   1 
ATOM   153   N  N     . GLN A 1 1345 ? 184.007 153.467 228.329 1.00 160.43 ? 1345 GLN A N     1 
ATOM   154   C  CA    . GLN A 1 1345 ? 184.501 152.324 227.567 1.00 160.51 ? 1345 GLN A CA    1 
ATOM   155   C  C     . GLN A 1 1345 ? 184.205 152.493 226.084 1.00 158.30 ? 1345 GLN A C     1 
ATOM   156   O  O     . GLN A 1 1345 ? 185.026 152.130 225.232 1.00 154.40 ? 1345 GLN A O     1 
ATOM   157   C  CB    . GLN A 1 1345 ? 183.885 151.024 228.087 1.00 159.67 ? 1345 GLN A CB    1 
ATOM   158   C  CG    . GLN A 1 1345 ? 184.206 150.706 229.535 1.00 160.56 ? 1345 GLN A CG    1 
ATOM   159   C  CD    . GLN A 1 1345 ? 183.277 149.660 230.118 1.00 159.40 ? 1345 GLN A CD    1 
ATOM   160   O  OE1   . GLN A 1 1345 ? 182.408 149.130 229.424 1.00 158.88 ? 1345 GLN A OE1   1 
ATOM   161   N  NE2   . GLN A 1 1345 ? 183.455 149.356 231.398 1.00 156.18 ? 1345 GLN A NE2   1 
ATOM   162   N  N     . MET A 1 1346 ? 183.032 153.037 225.758 1.00 157.30 ? 1346 MET A N     1 
ATOM   163   C  CA    . MET A 1 1346 ? 182.720 153.329 224.362 1.00 154.48 ? 1346 MET A CA    1 
ATOM   164   C  C     . MET A 1 1346 ? 183.667 154.376 223.787 1.00 151.03 ? 1346 MET A C     1 
ATOM   165   O  O     . MET A 1 1346 ? 184.120 154.255 222.642 1.00 147.28 ? 1346 MET A O     1 
ATOM   166   C  CB    . MET A 1 1346 ? 181.272 153.797 224.238 1.00 153.50 ? 1346 MET A CB    1 
ATOM   167   C  CG    . MET A 1 1346 ? 180.824 154.007 222.810 1.00 155.32 ? 1346 MET A CG    1 
ATOM   168   S  SD    . MET A 1 1346 ? 180.860 152.458 221.901 1.00 163.22 ? 1346 MET A SD    1 
ATOM   169   C  CE    . MET A 1 1346 ? 179.458 151.641 222.645 1.00 151.05 ? 1346 MET A CE    1 
ATOM   170   N  N     . LYS A 1 1347 ? 183.978 155.412 224.568 1.00 151.41 ? 1347 LYS A N     1 
ATOM   171   C  CA    . LYS A 1 1347 ? 184.778 156.524 224.066 1.00 148.53 ? 1347 LYS A CA    1 
ATOM   172   C  C     . LYS A 1 1347 ? 186.236 156.133 223.857 1.00 150.21 ? 1347 LYS A C     1 
ATOM   173   O  O     . LYS A 1 1347 ? 186.891 156.659 222.951 1.00 150.20 ? 1347 LYS A O     1 
ATOM   174   C  CB    . LYS A 1 1347 ? 184.672 157.713 225.022 1.00 146.52 ? 1347 LYS A CB    1 
ATOM   175   C  CG    . LYS A 1 1347 ? 183.265 158.286 225.132 1.00 145.54 ? 1347 LYS A CG    1 
ATOM   176   C  CD    . LYS A 1 1347 ? 183.191 159.454 226.105 1.00 143.49 ? 1347 LYS A CD    1 
ATOM   177   C  CE    . LYS A 1 1347 ? 183.950 160.664 225.595 1.00 136.85 ? 1347 LYS A CE    1 
ATOM   178   N  NZ    . LYS A 1 1347 ? 183.796 161.837 226.499 1.00 133.01 ? 1347 LYS A NZ    1 
ATOM   179   N  N     . GLU A 1 1348 ? 186.761 155.217 224.674 1.00 153.13 ? 1348 GLU A N     1 
ATOM   180   C  CA    . GLU A 1 1348 ? 188.159 154.817 224.554 1.00 150.72 ? 1348 GLU A CA    1 
ATOM   181   C  C     . GLU A 1 1348 ? 188.443 154.019 223.288 1.00 148.62 ? 1348 GLU A C     1 
ATOM   182   O  O     . GLU A 1 1348 ? 189.616 153.776 222.984 1.00 148.21 ? 1348 GLU A O     1 
ATOM   183   C  CB    . GLU A 1 1348 ? 188.587 154.000 225.775 1.00 150.93 ? 1348 GLU A CB    1 
ATOM   184   C  CG    . GLU A 1 1348 ? 188.462 154.734 227.099 1.00 151.88 ? 1348 GLU A CG    1 
ATOM   185   C  CD    . GLU A 1 1348 ? 188.863 156.191 227.001 1.00 152.92 ? 1348 GLU A CD    1 
ATOM   186   O  OE1   . GLU A 1 1348 ? 190.042 156.466 226.693 1.00 156.11 ? 1348 GLU A OE1   1 
ATOM   187   O  OE2   . GLU A 1 1348 ? 187.998 157.062 227.232 1.00 150.76 ? 1348 GLU A OE2   1 
ATOM   188   N  N     . GLN A 1 1349 ? 187.417 153.605 222.557 1.00 146.22 ? 1349 GLN A N     1 
ATOM   189   C  CA    . GLN A 1 1349 ? 187.609 152.849 221.329 1.00 144.38 ? 1349 GLN A CA    1 
ATOM   190   C  C     . GLN A 1 1349 ? 188.322 153.711 220.292 1.00 143.24 ? 1349 GLN A C     1 
ATOM   191   O  O     . GLN A 1 1349 ? 187.857 154.823 219.998 1.00 139.14 ? 1349 GLN A O     1 
ATOM   192   C  CB    . GLN A 1 1349 ? 186.262 152.371 220.795 1.00 146.45 ? 1349 GLN A CB    1 
ATOM   193   C  CG    . GLN A 1 1349 ? 186.350 151.408 219.626 1.00 145.00 ? 1349 GLN A CG    1 
ATOM   194   C  CD    . GLN A 1 1349 ? 184.983 151.011 219.102 1.00 140.20 ? 1349 GLN A CD    1 
ATOM   195   O  OE1   . GLN A 1 1349 ? 183.960 151.523 219.556 1.00 137.57 ? 1349 GLN A OE1   1 
ATOM   196   N  NE2   . GLN A 1 1349 ? 184.960 150.094 218.142 1.00 136.40 ? 1349 GLN A NE2   1 
ATOM   197   N  N     . PRO A 1 1350 ? 189.440 153.256 219.728 1.00 145.67 ? 1350 PRO A N     1 
ATOM   198   C  CA    . PRO A 1 1350 ? 190.164 154.076 218.754 1.00 143.19 ? 1350 PRO A CA    1 
ATOM   199   C  C     . PRO A 1 1350 ? 189.360 154.307 217.485 1.00 141.38 ? 1350 PRO A C     1 
ATOM   200   O  O     . PRO A 1 1350 ? 188.555 153.472 217.067 1.00 141.41 ? 1350 PRO A O     1 
ATOM   201   C  CB    . PRO A 1 1350 ? 191.415 153.231 218.487 1.00 139.26 ? 1350 PRO A CB    1 
ATOM   202   C  CG    . PRO A 1 1350 ? 190.830 151.847 218.568 1.00 138.26 ? 1350 PRO A CG    1 
ATOM   203   C  CD    . PRO A 1 1350 ? 190.155 151.983 219.917 1.00 142.68 ? 1350 PRO A CD    1 
ATOM   204   N  N     . TRP A 1 1351 ? 189.596 155.470 216.870 1.00 139.58 ? 1351 TRP A N     1 
ATOM   205   C  CA    . TRP A 1 1351 ? 188.811 155.875 215.708 1.00 136.01 ? 1351 TRP A CA    1 
ATOM   206   C  C     . TRP A 1 1351 ? 189.009 154.933 214.529 1.00 132.94 ? 1351 TRP A C     1 
ATOM   207   O  O     . TRP A 1 1351 ? 188.121 154.813 213.677 1.00 133.12 ? 1351 TRP A O     1 
ATOM   208   C  CB    . TRP A 1 1351 ? 189.174 157.305 215.307 1.00 135.07 ? 1351 TRP A CB    1 
ATOM   209   C  CG    . TRP A 1 1351 ? 188.419 157.805 214.115 1.00 132.63 ? 1351 TRP A CG    1 
ATOM   210   C  CD1   . TRP A 1 1351 ? 188.924 158.063 212.875 1.00 129.62 ? 1351 TRP A CD1   1 
ATOM   211   C  CD2   . TRP A 1 1351 ? 187.022 158.113 214.052 1.00 131.63 ? 1351 TRP A CD2   1 
ATOM   212   N  NE1   . TRP A 1 1351 ? 187.928 158.511 212.043 1.00 128.07 ? 1351 TRP A NE1   1 
ATOM   213   C  CE2   . TRP A 1 1351 ? 186.750 158.551 212.741 1.00 128.00 ? 1351 TRP A CE2   1 
ATOM   214   C  CE3   . TRP A 1 1351 ? 185.974 158.058 214.976 1.00 133.31 ? 1351 TRP A CE3   1 
ATOM   215   C  CZ2   . TRP A 1 1351 ? 185.475 158.933 212.332 1.00 122.10 ? 1351 TRP A CZ2   1 
ATOM   216   C  CZ3   . TRP A 1 1351 ? 184.709 158.439 214.567 1.00 133.52 ? 1351 TRP A CZ3   1 
ATOM   217   C  CH2   . TRP A 1 1351 ? 184.471 158.870 213.257 1.00 124.27 ? 1351 TRP A CH2   1 
ATOM   218   N  N     . VAL A 1 1352 ? 190.160 154.263 214.457 1.00 132.21 ? 1352 VAL A N     1 
ATOM   219   C  CA    . VAL A 1 1352 ? 190.427 153.361 213.339 1.00 134.06 ? 1352 VAL A CA    1 
ATOM   220   C  C     . VAL A 1 1352 ? 189.451 152.191 213.349 1.00 135.25 ? 1352 VAL A C     1 
ATOM   221   O  O     . VAL A 1 1352 ? 188.927 151.791 212.302 1.00 135.28 ? 1352 VAL A O     1 
ATOM   222   C  CB    . VAL A 1 1352 ? 191.889 152.881 213.377 1.00 132.34 ? 1352 VAL A CB    1 
ATOM   223   C  CG1   . VAL A 1 1352 ? 192.148 151.871 212.269 1.00 130.80 ? 1352 VAL A CG1   1 
ATOM   224   C  CG2   . VAL A 1 1352 ? 192.838 154.065 213.261 1.00 128.01 ? 1352 VAL A CG2   1 
ATOM   225   N  N     . SER A 1 1353 ? 189.187 151.628 214.525 1.00 136.26 ? 1353 SER A N     1 
ATOM   226   C  CA    . SER A 1 1353 ? 188.338 150.450 214.649 1.00 136.11 ? 1353 SER A CA    1 
ATOM   227   C  C     . SER A 1 1353 ? 186.883 150.782 214.954 1.00 136.26 ? 1353 SER A C     1 
ATOM   228   O  O     . SER A 1 1353 ? 186.087 149.860 215.160 1.00 136.33 ? 1353 SER A O     1 
ATOM   229   C  CB    . SER A 1 1353 ? 188.885 149.518 215.735 1.00 137.44 ? 1353 SER A CB    1 
ATOM   230   O  OG    . SER A 1 1353 ? 188.673 150.062 217.025 1.00 136.40 ? 1353 SER A OG    1 
ATOM   231   N  N     . VAL A 1 1354 ? 186.514 152.063 214.995 1.00 135.23 ? 1354 VAL A N     1 
ATOM   232   C  CA    . VAL A 1 1354 ? 185.132 152.427 215.289 1.00 135.73 ? 1354 VAL A CA    1 
ATOM   233   C  C     . VAL A 1 1354 ? 184.242 151.988 214.136 1.00 136.17 ? 1354 VAL A C     1 
ATOM   234   O  O     . VAL A 1 1354 ? 184.425 152.416 212.990 1.00 133.43 ? 1354 VAL A O     1 
ATOM   235   C  CB    . VAL A 1 1354 ? 185.008 153.932 215.551 1.00 135.59 ? 1354 VAL A CB    1 
ATOM   236   C  CG1   . VAL A 1 1354 ? 183.563 154.380 215.396 1.00 132.81 ? 1354 VAL A CG1   1 
ATOM   237   C  CG2   . VAL A 1 1354 ? 185.511 154.270 216.942 1.00 137.28 ? 1354 VAL A CG2   1 
ATOM   238   N  N     . GLN A 1 1355 ? 183.275 151.120 214.434 1.00 136.53 ? 1355 GLN A N     1 
ATOM   239   C  CA    . GLN A 1 1355 ? 182.291 150.702 213.448 1.00 133.18 ? 1355 GLN A CA    1 
ATOM   240   C  C     . GLN A 1 1355 ? 180.986 151.427 213.727 1.00 132.47 ? 1355 GLN A C     1 
ATOM   241   O  O     . GLN A 1 1355 ? 180.363 151.178 214.770 1.00 133.87 ? 1355 GLN A O     1 
ATOM   242   C  CB    . GLN A 1 1355 ? 182.083 149.191 213.490 1.00 129.95 ? 1355 GLN A CB    1 
ATOM   243   C  CG    . GLN A 1 1355 ? 180.976 148.694 212.571 1.00 129.60 ? 1355 GLN A CG    1 
ATOM   244   C  CD    . GLN A 1 1355 ? 181.086 149.245 211.161 1.00 131.03 ? 1355 GLN A CD    1 
ATOM   245   O  OE1   . GLN A 1 1355 ? 180.114 149.757 210.606 1.00 129.41 ? 1355 GLN A OE1   1 
ATOM   246   N  NE2   . GLN A 1 1355 ? 182.270 149.130 210.570 1.00 131.95 ? 1355 GLN A NE2   1 
ATOM   247   N  N     . PRO A 1 1356 ? 180.542 152.330 212.851 1.00 132.23 ? 1356 PRO A N     1 
ATOM   248   C  CA    . PRO A 1 1356 ? 179.342 153.126 213.160 1.00 130.22 ? 1356 PRO A CA    1 
ATOM   249   C  C     . PRO A 1 1356 ? 178.080 152.304 213.364 1.00 132.86 ? 1356 PRO A C     1 
ATOM   250   O  O     . PRO A 1 1356 ? 177.240 152.686 214.186 1.00 131.39 ? 1356 PRO A O     1 
ATOM   251   C  CB    . PRO A 1 1356 ? 179.221 154.051 211.943 1.00 123.31 ? 1356 PRO A CB    1 
ATOM   252   C  CG    . PRO A 1 1356 ? 180.593 154.103 211.357 1.00 121.59 ? 1356 PRO A CG    1 
ATOM   253   C  CD    . PRO A 1 1356 ? 181.179 152.749 211.592 1.00 127.68 ? 1356 PRO A CD    1 
ATOM   254   N  N     . ARG A 1 1357 ? 177.907 151.197 212.638 1.00 132.20 ? 1357 ARG A N     1 
ATOM   255   C  CA    . ARG A 1 1357 ? 176.699 150.390 212.800 1.00 129.62 ? 1357 ARG A CA    1 
ATOM   256   C  C     . ARG A 1 1357 ? 176.656 149.727 214.172 1.00 133.35 ? 1357 ARG A C     1 
ATOM   257   O  O     . ARG A 1 1357 ? 175.649 149.812 214.888 1.00 133.49 ? 1357 ARG A O     1 
ATOM   258   C  CB    . ARG A 1 1357 ? 176.619 149.343 211.690 1.00 127.83 ? 1357 ARG A CB    1 
ATOM   259   C  CG    . ARG A 1 1357 ? 176.543 149.928 210.291 1.00 124.83 ? 1357 ARG A CG    1 
ATOM   260   C  CD    . ARG A 1 1357 ? 176.359 148.837 209.250 1.00 126.34 ? 1357 ARG A CD    1 
ATOM   261   N  NE    . ARG A 1 1357 ? 176.240 149.380 207.902 1.00 124.61 ? 1357 ARG A NE    1 
ATOM   262   C  CZ    . ARG A 1 1357 ? 176.062 148.645 206.813 1.00 120.62 ? 1357 ARG A CZ    1 
ATOM   263   N  NH1   . ARG A 1 1357 ? 175.976 147.326 206.876 1.00 114.64 ? 1357 ARG A NH1   1 
ATOM   264   N  NH2   . ARG A 1 1357 ? 175.970 149.248 205.631 1.00 118.08 ? 1357 ARG A NH2   1 
ATOM   265   N  N     . LYS A 1 1358 ? 177.744 149.056 214.556 1.00 133.86 ? 1358 LYS A N     1 
ATOM   266   C  CA    . LYS A 1 1358 ? 177.809 148.471 215.890 1.00 133.60 ? 1358 LYS A CA    1 
ATOM   267   C  C     . LYS A 1 1358 ? 177.790 149.549 216.963 1.00 136.02 ? 1358 LYS A C     1 
ATOM   268   O  O     . LYS A 1 1358 ? 177.270 149.322 218.062 1.00 138.51 ? 1358 LYS A O     1 
ATOM   269   C  CB    . LYS A 1 1358 ? 179.056 147.597 216.023 1.00 130.95 ? 1358 LYS A CB    1 
ATOM   270   C  CG    . LYS A 1 1358 ? 179.222 146.594 214.892 1.00 133.17 ? 1358 LYS A CG    1 
ATOM   271   C  CD    . LYS A 1 1358 ? 180.493 145.774 215.046 1.00 133.66 ? 1358 LYS A CD    1 
ATOM   272   C  CE    . LYS A 1 1358 ? 180.642 144.775 213.909 1.00 124.44 ? 1358 LYS A CE    1 
ATOM   273   N  NZ    . LYS A 1 1358 ? 181.851 143.921 214.064 1.00 112.53 ? 1358 LYS A NZ    1 
ATOM   274   N  N     . LEU A 1 1359 ? 178.339 150.727 216.663 1.00 136.10 ? 1359 LEU A N     1 
ATOM   275   C  CA    . LEU A 1 1359 ? 178.256 151.842 217.599 1.00 134.44 ? 1359 LEU A CA    1 
ATOM   276   C  C     . LEU A 1 1359 ? 176.806 152.241 217.837 1.00 135.75 ? 1359 LEU A C     1 
ATOM   277   O  O     . LEU A 1 1359 ? 176.389 152.458 218.979 1.00 139.62 ? 1359 LEU A O     1 
ATOM   278   C  CB    . LEU A 1 1359 ? 179.066 153.027 217.075 1.00 134.44 ? 1359 LEU A CB    1 
ATOM   279   C  CG    . LEU A 1 1359 ? 178.787 154.372 217.744 1.00 138.67 ? 1359 LEU A CG    1 
ATOM   280   C  CD1   . LEU A 1 1359 ? 179.252 154.336 219.187 1.00 142.13 ? 1359 LEU A CD1   1 
ATOM   281   C  CD2   . LEU A 1 1359 ? 179.461 155.503 216.987 1.00 136.32 ? 1359 LEU A CD2   1 
ATOM   282   N  N     . ARG A 1 1360 ? 176.017 152.329 216.763 1.00 133.94 ? 1360 ARG A N     1 
ATOM   283   C  CA    . ARG A 1 1360 ? 174.595 152.625 216.905 1.00 135.63 ? 1360 ARG A CA    1 
ATOM   284   C  C     . ARG A 1 1360 ? 173.880 151.538 217.695 1.00 139.67 ? 1360 ARG A C     1 
ATOM   285   O  O     . ARG A 1 1360 ? 173.037 151.834 218.551 1.00 140.24 ? 1360 ARG A O     1 
ATOM   286   C  CB    . ARG A 1 1360 ? 173.948 152.786 215.528 1.00 132.79 ? 1360 ARG A CB    1 
ATOM   287   C  CG    . ARG A 1 1360 ? 172.521 152.267 215.484 1.00 130.57 ? 1360 ARG A CG    1 
ATOM   288   C  CD    . ARG A 1 1360 ? 171.851 152.436 214.132 1.00 124.08 ? 1360 ARG A CD    1 
ATOM   289   N  NE    . ARG A 1 1360 ? 170.699 151.549 214.014 1.00 122.27 ? 1360 ARG A NE    1 
ATOM   290   C  CZ    . ARG A 1 1360 ? 169.596 151.632 214.747 1.00 123.00 ? 1360 ARG A CZ    1 
ATOM   291   N  NH1   . ARG A 1 1360 ? 169.407 152.615 215.611 1.00 127.84 ? 1360 ARG A NH1   1 
ATOM   292   N  NH2   . ARG A 1 1360 ? 168.657 150.701 214.612 1.00 114.65 ? 1360 ARG A NH2   1 
ATOM   293   N  N     . GLN A 1 1361 ? 174.194 150.270 217.414 1.00 138.88 ? 1361 GLN A N     1 
ATOM   294   C  CA    . GLN A 1 1361 ? 173.535 149.179 218.129 1.00 137.02 ? 1361 GLN A CA    1 
ATOM   295   C  C     . GLN A 1 1361 ? 173.838 149.234 219.622 1.00 140.60 ? 1361 GLN A C     1 
ATOM   296   O  O     . GLN A 1 1361 ? 172.936 149.085 220.456 1.00 141.95 ? 1361 GLN A O     1 
ATOM   297   C  CB    . GLN A 1 1361 ? 173.958 147.833 217.542 1.00 135.98 ? 1361 GLN A CB    1 
ATOM   298   C  CG    . GLN A 1 1361 ? 173.524 147.618 216.101 1.00 132.41 ? 1361 GLN A CG    1 
ATOM   299   C  CD    . GLN A 1 1361 ? 174.166 146.395 215.476 1.00 129.51 ? 1361 GLN A CD    1 
ATOM   300   O  OE1   . GLN A 1 1361 ? 174.967 145.707 216.109 1.00 132.25 ? 1361 GLN A OE1   1 
ATOM   301   N  NE2   . GLN A 1 1361 ? 173.815 146.117 214.226 1.00 121.64 ? 1361 GLN A NE2   1 
ATOM   302   N  N     . ASN A 1 1362 ? 175.101 149.466 219.981 1.00 141.46 ? 1362 ASN A N     1 
ATOM   303   C  CA    . ASN A 1 1362 ? 175.461 149.544 221.391 1.00 141.36 ? 1362 ASN A CA    1 
ATOM   304   C  C     . ASN A 1 1362 ? 174.889 150.792 222.054 1.00 145.17 ? 1362 ASN A C     1 
ATOM   305   O  O     . ASN A 1 1362 ? 174.519 150.747 223.233 1.00 148.22 ? 1362 ASN A O     1 
ATOM   306   C  CB    . ASN A 1 1362 ? 176.978 149.495 221.549 1.00 139.86 ? 1362 ASN A CB    1 
ATOM   307   C  CG    . ASN A 1 1362 ? 177.592 148.274 220.895 1.00 141.52 ? 1362 ASN A CG    1 
ATOM   308   O  OD1   . ASN A 1 1362 ? 176.885 147.415 220.370 1.00 139.24 ? 1362 ASN A OD1   1 
ATOM   309   N  ND2   . ASN A 1 1362 ? 178.917 148.192 220.922 1.00 143.48 ? 1362 ASN A ND2   1 
ATOM   310   N  N     . LEU A 1 1363 ? 174.806 151.910 221.327 1.00 145.67 ? 1363 LEU A N     1 
ATOM   311   C  CA    . LEU A 1 1363 ? 174.158 153.096 221.878 1.00 147.15 ? 1363 LEU A CA    1 
ATOM   312   C  C     . LEU A 1 1363 ? 172.681 152.839 222.144 1.00 148.35 ? 1363 LEU A C     1 
ATOM   313   O  O     . LEU A 1 1363 ? 172.137 153.287 223.159 1.00 150.29 ? 1363 LEU A O     1 
ATOM   314   C  CB    . LEU A 1 1363 ? 174.335 154.286 220.933 1.00 143.57 ? 1363 LEU A CB    1 
ATOM   315   C  CG    . LEU A 1 1363 ? 175.729 154.915 220.865 1.00 143.38 ? 1363 LEU A CG    1 
ATOM   316   C  CD1   . LEU A 1 1363 ? 175.690 156.225 220.094 1.00 138.85 ? 1363 LEU A CD1   1 
ATOM   317   C  CD2   . LEU A 1 1363 ? 176.299 155.125 222.258 1.00 144.92 ? 1363 LEU A CD2   1 
ATOM   318   N  N     . ASP A 1 1364 ? 172.014 152.119 221.240 1.00 146.82 ? 1364 ASP A N     1 
ATOM   319   C  CA    . ASP A 1 1364 ? 170.622 151.751 221.472 1.00 149.65 ? 1364 ASP A CA    1 
ATOM   320   C  C     . ASP A 1 1364 ? 170.496 150.828 222.678 1.00 152.14 ? 1364 ASP A C     1 
ATOM   321   O  O     . ASP A 1 1364 ? 169.542 150.938 223.457 1.00 154.11 ? 1364 ASP A O     1 
ATOM   322   C  CB    . ASP A 1 1364 ? 170.035 151.092 220.225 1.00 147.65 ? 1364 ASP A CB    1 
ATOM   323   C  CG    . ASP A 1 1364 ? 168.677 150.470 220.480 1.00 151.80 ? 1364 ASP A CG    1 
ATOM   324   O  OD1   . ASP A 1 1364 ? 167.745 151.211 220.861 1.00 152.57 ? 1364 ASP A OD1   1 
ATOM   325   O  OD2   . ASP A 1 1364 ? 168.540 149.242 220.299 1.00 152.66 ? 1364 ASP A OD2   1 
ATOM   326   N  N     . ALA A 1 1365 ? 171.447 149.906 222.843 1.00 148.55 ? 1365 ALA A N     1 
ATOM   327   C  CA    . ALA A 1 1365 ? 171.439 149.043 224.023 1.00 146.33 ? 1365 ALA A CA    1 
ATOM   328   C  C     . ALA A 1 1365 ? 171.594 149.857 225.304 1.00 150.40 ? 1365 ALA A C     1 
ATOM   329   O  O     . ALA A 1 1365 ? 170.911 149.598 226.303 1.00 151.97 ? 1365 ALA A O     1 
ATOM   330   C  CB    . ALA A 1 1365 ? 172.544 147.993 223.914 1.00 140.08 ? 1365 ALA A CB    1 
ATOM   331   N  N     . LEU A 1 1366 ? 172.490 150.847 225.293 1.00 150.39 ? 1366 LEU A N     1 
ATOM   332   C  CA    . LEU A 1 1366 ? 172.647 151.718 226.456 1.00 151.43 ? 1366 LEU A CA    1 
ATOM   333   C  C     . LEU A 1 1366 ? 171.381 152.527 226.714 1.00 154.56 ? 1366 LEU A C     1 
ATOM   334   O  O     . LEU A 1 1366 ? 171.007 152.761 227.869 1.00 156.11 ? 1366 LEU A O     1 
ATOM   335   C  CB    . LEU A 1 1366 ? 173.846 152.648 226.263 1.00 149.09 ? 1366 LEU A CB    1 
ATOM   336   C  CG    . LEU A 1 1366 ? 175.216 151.995 226.065 1.00 149.65 ? 1366 LEU A CG    1 
ATOM   337   C  CD1   . LEU A 1 1366 ? 176.314 153.046 226.048 1.00 150.29 ? 1366 LEU A CD1   1 
ATOM   338   C  CD2   . LEU A 1 1366 ? 175.483 150.956 227.143 1.00 150.74 ? 1366 LEU A CD2   1 
ATOM   339   N  N     . LEU A 1 1367 ? 170.713 152.972 225.648 1.00 153.16 ? 1367 LEU A N     1 
ATOM   340   C  CA    . LEU A 1 1367 ? 169.451 153.686 225.812 1.00 153.06 ? 1367 LEU A CA    1 
ATOM   341   C  C     . LEU A 1 1367 ? 168.392 152.792 226.447 1.00 155.19 ? 1367 LEU A C     1 
ATOM   342   O  O     . LEU A 1 1367 ? 167.644 153.233 227.328 1.00 156.99 ? 1367 LEU A O     1 
ATOM   343   C  CB    . LEU A 1 1367 ? 168.969 154.217 224.462 1.00 152.59 ? 1367 LEU A CB    1 
ATOM   344   C  CG    . LEU A 1 1367 ? 169.665 155.479 223.948 1.00 154.19 ? 1367 LEU A CG    1 
ATOM   345   C  CD1   . LEU A 1 1367 ? 169.100 155.895 222.599 1.00 147.61 ? 1367 LEU A CD1   1 
ATOM   346   C  CD2   . LEU A 1 1367 ? 169.536 156.610 224.958 1.00 152.33 ? 1367 LEU A CD2   1 
ATOM   347   N  N     . ASN A 1 1368 ? 168.315 151.533 226.010 1.00 154.38 ? 1368 ASN A N     1 
ATOM   348   C  CA    . ASN A 1 1368 ? 167.381 150.592 226.624 1.00 156.10 ? 1368 ASN A CA    1 
ATOM   349   C  C     . ASN A 1 1368 ? 167.723 150.359 228.089 1.00 157.74 ? 1368 ASN A C     1 
ATOM   350   O  O     . ASN A 1 1368 ? 166.827 150.239 228.933 1.00 156.38 ? 1368 ASN A O     1 
ATOM   351   C  CB    . ASN A 1 1368 ? 167.376 149.269 225.858 1.00 152.49 ? 1368 ASN A CB    1 
ATOM   352   C  CG    . ASN A 1 1368 ? 166.989 149.436 224.403 1.00 152.85 ? 1368 ASN A CG    1 
ATOM   353   O  OD1   . ASN A 1 1368 ? 167.662 148.926 223.507 1.00 153.26 ? 1368 ASN A OD1   1 
ATOM   354   N  ND2   . ASN A 1 1368 ? 165.900 150.156 224.160 1.00 152.58 ? 1368 ASN A ND2   1 
ATOM   355   N  N     . GLN A 1 1369 ? 169.017 150.281 228.408 1.00 157.35 ? 1369 GLN A N     1 
ATOM   356   C  CA    . GLN A 1 1369 ? 169.432 150.160 229.803 1.00 155.96 ? 1369 GLN A CA    1 
ATOM   357   C  C     . GLN A 1 1369 ? 168.977 151.365 230.618 1.00 156.74 ? 1369 GLN A C     1 
ATOM   358   O  O     . GLN A 1 1369 ? 168.502 151.216 231.750 1.00 156.50 ? 1369 GLN A O     1 
ATOM   359   C  CB    . GLN A 1 1369 ? 170.951 150.003 229.885 1.00 156.01 ? 1369 GLN A CB    1 
ATOM   360   C  CG    . GLN A 1 1369 ? 171.503 150.031 231.301 1.00 160.69 ? 1369 GLN A CG    1 
ATOM   361   C  CD    . GLN A 1 1369 ? 173.015 149.935 231.340 1.00 163.53 ? 1369 GLN A CD    1 
ATOM   362   O  OE1   . GLN A 1 1369 ? 173.670 149.856 230.301 1.00 161.77 ? 1369 GLN A OE1   1 
ATOM   363   N  NE2   . GLN A 1 1369 ? 173.578 149.945 232.542 1.00 164.63 ? 1369 GLN A NE2   1 
ATOM   364   N  N     . LEU A 1 1370 ? 169.120 152.568 230.057 1.00 158.01 ? 1370 LEU A N     1 
ATOM   365   C  CA    . LEU A 1 1370 ? 168.672 153.772 230.751 1.00 159.41 ? 1370 LEU A CA    1 
ATOM   366   C  C     . LEU A 1 1370 ? 167.164 153.760 230.970 1.00 158.46 ? 1370 LEU A C     1 
ATOM   367   O  O     . LEU A 1 1370 ? 166.683 154.124 232.050 1.00 158.50 ? 1370 LEU A O     1 
ATOM   368   C  CB    . LEU A 1 1370 ? 169.083 155.018 229.969 1.00 160.84 ? 1370 LEU A CB    1 
ATOM   369   C  CG    . LEU A 1 1370 ? 170.570 155.366 229.931 1.00 161.77 ? 1370 LEU A CG    1 
ATOM   370   C  CD1   . LEU A 1 1370 ? 170.797 156.601 229.077 1.00 156.08 ? 1370 LEU A CD1   1 
ATOM   371   C  CD2   . LEU A 1 1370 ? 171.093 155.584 231.338 1.00 159.44 ? 1370 LEU A CD2   1 
ATOM   372   N  N     . LYS A 1 1371 ? 166.399 153.354 229.953 1.00 157.31 ? 1371 LYS A N     1 
ATOM   373   C  CA    . LYS A 1 1371 ? 164.945 153.341 230.076 1.00 158.05 ? 1371 LYS A CA    1 
ATOM   374   C  C     . LYS A 1 1371 ? 164.452 152.288 231.060 1.00 161.92 ? 1371 LYS A C     1 
ATOM   375   O  O     . LYS A 1 1371 ? 163.337 152.417 231.576 1.00 159.15 ? 1371 LYS A O     1 
ATOM   376   C  CB    . LYS A 1 1371 ? 164.300 153.111 228.708 1.00 155.16 ? 1371 LYS A CB    1 
ATOM   377   C  CG    . LYS A 1 1371 ? 164.651 154.162 227.669 1.00 153.02 ? 1371 LYS A CG    1 
ATOM   378   C  CD    . LYS A 1 1371 ? 164.523 153.606 226.260 1.00 150.36 ? 1371 LYS A CD    1 
ATOM   379   C  CE    . LYS A 1 1371 ? 165.022 154.601 225.226 1.00 149.23 ? 1371 LYS A CE    1 
ATOM   380   N  NZ    . LYS A 1 1371 ? 165.089 154.001 223.865 1.00 152.16 ? 1371 LYS A NZ    1 
ATOM   381   N  N     . SER A 1 1372 ? 165.252 151.255 231.330 1.00 163.04 ? 1372 SER A N     1 
ATOM   382   C  CA    . SER A 1 1372 ? 164.853 150.208 232.263 1.00 159.02 ? 1372 SER A CA    1 
ATOM   383   C  C     . SER A 1 1372 ? 164.810 150.684 233.709 1.00 159.49 ? 1372 SER A C     1 
ATOM   384   O  O     . SER A 1 1372 ? 164.284 149.962 234.563 1.00 159.18 ? 1372 SER A O     1 
ATOM   385   C  CB    . SER A 1 1372 ? 165.801 149.013 232.143 1.00 155.71 ? 1372 SER A CB    1 
ATOM   386   O  OG    . SER A 1 1372 ? 167.097 149.343 232.610 1.00 155.22 ? 1372 SER A OG    1 
ATOM   387   N  N     . PHE A 1 1373 ? 165.347 151.865 234.004 1.00 160.88 ? 1373 PHE A N     1 
ATOM   388   C  CA    . PHE A 1 1373 ? 165.351 152.366 235.367 1.00 161.23 ? 1373 PHE A CA    1 
ATOM   389   C  C     . PHE A 1 1373 ? 163.933 152.728 235.810 1.00 161.89 ? 1373 PHE A C     1 
ATOM   390   O  O     . PHE A 1 1373 ? 163.087 153.082 234.984 1.00 160.58 ? 1373 PHE A O     1 
ATOM   391   C  CB    . PHE A 1 1373 ? 166.260 153.587 235.485 1.00 160.43 ? 1373 PHE A CB    1 
ATOM   392   C  CG    . PHE A 1 1373 ? 167.726 153.267 235.375 1.00 161.81 ? 1373 PHE A CG    1 
ATOM   393   C  CD1   . PHE A 1 1373 ? 168.166 151.953 235.369 1.00 160.92 ? 1373 PHE A CD1   1 
ATOM   394   C  CD2   . PHE A 1 1373 ? 168.662 154.282 235.273 1.00 161.09 ? 1373 PHE A CD2   1 
ATOM   395   C  CE1   . PHE A 1 1373 ? 169.511 151.658 235.266 1.00 159.91 ? 1373 PHE A CE1   1 
ATOM   396   C  CE2   . PHE A 1 1373 ? 170.009 153.993 235.170 1.00 162.25 ? 1373 PHE A CE2   1 
ATOM   397   C  CZ    . PHE A 1 1373 ? 170.433 152.679 235.165 1.00 162.08 ? 1373 PHE A CZ    1 
ATOM   398   N  N     . PRO A 1 1374 ? 163.649 152.642 237.109 1.00 164.07 ? 1374 PRO A N     1 
ATOM   399   C  CA    . PRO A 1 1374 ? 162.323 153.029 237.602 1.00 162.56 ? 1374 PRO A CA    1 
ATOM   400   C  C     . PRO A 1 1374 ? 162.052 154.509 237.376 1.00 162.57 ? 1374 PRO A C     1 
ATOM   401   O  O     . PRO A 1 1374 ? 162.966 155.327 237.247 1.00 161.95 ? 1374 PRO A O     1 
ATOM   402   C  CB    . PRO A 1 1374 ? 162.385 152.696 239.099 1.00 158.89 ? 1374 PRO A CB    1 
ATOM   403   C  CG    . PRO A 1 1374 ? 163.473 151.682 239.219 1.00 157.88 ? 1374 PRO A CG    1 
ATOM   404   C  CD    . PRO A 1 1374 ? 164.479 152.044 238.168 1.00 160.84 ? 1374 PRO A CD    1 
ATOM   405   N  N     . ALA A 1 1375 ? 160.760 154.844 237.324 1.00 161.71 ? 1375 ALA A N     1 
ATOM   406   C  CA    . ALA A 1 1375 ? 160.353 156.213 237.021 1.00 159.69 ? 1375 ALA A CA    1 
ATOM   407   C  C     . ALA A 1 1375 ? 160.875 157.198 238.059 1.00 161.87 ? 1375 ALA A C     1 
ATOM   408   O  O     . ALA A 1 1375 ? 161.229 158.334 237.722 1.00 161.38 ? 1375 ALA A O     1 
ATOM   409   C  CB    . ALA A 1 1375 ? 158.830 156.297 236.921 1.00 152.62 ? 1375 ALA A CB    1 
ATOM   410   N  N     . ARG A 1 1376 ? 160.922 156.786 239.329 1.00 163.53 ? 1376 ARG A N     1 
ATOM   411   C  CA    . ARG A 1 1376 ? 161.426 157.675 240.372 1.00 164.00 ? 1376 ARG A CA    1 
ATOM   412   C  C     . ARG A 1 1376 ? 162.892 158.023 240.142 1.00 165.33 ? 1376 ARG A C     1 
ATOM   413   O  O     . ARG A 1 1376 ? 163.307 159.169 240.353 1.00 163.12 ? 1376 ARG A O     1 
ATOM   414   C  CB    . ARG A 1 1376 ? 161.228 157.040 241.749 1.00 161.85 ? 1376 ARG A CB    1 
ATOM   415   C  CG    . ARG A 1 1376 ? 161.782 155.631 241.882 1.00 161.36 ? 1376 ARG A CG    1 
ATOM   416   C  CD    . ARG A 1 1376 ? 161.714 155.149 243.322 1.00 159.93 ? 1376 ARG A CD    1 
ATOM   417   N  NE    . ARG A 1 1376 ? 162.373 153.860 243.498 1.00 160.16 ? 1376 ARG A NE    1 
ATOM   418   C  CZ    . ARG A 1 1376 ? 162.487 153.230 244.659 1.00 158.14 ? 1376 ARG A CZ    1 
ATOM   419   N  NH1   . ARG A 1 1376 ? 161.996 153.744 245.775 1.00 159.36 ? 1376 ARG A NH1   1 
ATOM   420   N  NH2   . ARG A 1 1376 ? 163.110 152.056 244.702 1.00 152.34 ? 1376 ARG A NH2   1 
ATOM   421   N  N     . LEU A 1 1377 ? 163.695 157.048 239.709 1.00 164.58 ? 1377 LEU A N     1 
ATOM   422   C  CA    . LEU A 1 1377 ? 165.091 157.331 239.396 1.00 164.84 ? 1377 LEU A CA    1 
ATOM   423   C  C     . LEU A 1 1377 ? 165.229 158.100 238.089 1.00 163.81 ? 1377 LEU A C     1 
ATOM   424   O  O     . LEU A 1 1377 ? 166.207 158.833 237.904 1.00 161.77 ? 1377 LEU A O     1 
ATOM   425   C  CB    . LEU A 1 1377 ? 165.893 156.031 239.337 1.00 164.10 ? 1377 LEU A CB    1 
ATOM   426   C  CG    . LEU A 1 1377 ? 165.891 155.174 240.605 1.00 163.95 ? 1377 LEU A CG    1 
ATOM   427   C  CD1   . LEU A 1 1377 ? 166.750 153.933 240.416 1.00 159.27 ? 1377 LEU A CD1   1 
ATOM   428   C  CD2   . LEU A 1 1377 ? 166.367 155.983 241.802 1.00 161.30 ? 1377 LEU A CD2   1 
ATOM   429   N  N     . ARG A 1 1378 ? 164.269 157.947 237.174 1.00 163.06 ? 1378 ARG A N     1 
ATOM   430   C  CA    . ARG A 1 1378 ? 164.335 158.654 235.900 1.00 161.73 ? 1378 ARG A CA    1 
ATOM   431   C  C     . ARG A 1 1378 ? 164.045 160.143 236.043 1.00 161.28 ? 1378 ARG A C     1 
ATOM   432   O  O     . ARG A 1 1378 ? 164.388 160.916 235.142 1.00 160.77 ? 1378 ARG A O     1 
ATOM   433   C  CB    . ARG A 1 1378 ? 163.365 158.029 234.895 1.00 158.46 ? 1378 ARG A CB    1 
ATOM   434   C  CG    . ARG A 1 1378 ? 163.782 156.649 234.406 1.00 157.27 ? 1378 ARG A CG    1 
ATOM   435   C  CD    . ARG A 1 1378 ? 162.840 156.132 233.329 1.00 155.70 ? 1378 ARG A CD    1 
ATOM   436   N  NE    . ARG A 1 1378 ? 161.647 155.514 233.894 1.00 158.11 ? 1378 ARG A NE    1 
ATOM   437   C  CZ    . ARG A 1 1378 ? 160.689 154.943 233.176 1.00 154.97 ? 1378 ARG A CZ    1 
ATOM   438   N  NH1   . ARG A 1 1378 ? 160.750 154.894 231.856 1.00 154.64 ? 1378 ARG A NH1   1 
ATOM   439   N  NH2   . ARG A 1 1378 ? 159.644 154.406 233.800 1.00 148.38 ? 1378 ARG A NH2   1 
ATOM   440   N  N     . GLN A 1 1379 ? 163.424 160.561 237.147 1.00 160.79 ? 1379 GLN A N     1 
ATOM   441   C  CA    . GLN A 1 1379 ? 163.131 161.973 237.360 1.00 161.50 ? 1379 GLN A CA    1 
ATOM   442   C  C     . GLN A 1 1379 ? 164.367 162.788 237.717 1.00 161.42 ? 1379 GLN A C     1 
ATOM   443   O  O     . GLN A 1 1379 ? 164.288 164.021 237.735 1.00 159.89 ? 1379 GLN A O     1 
ATOM   444   C  CB    . GLN A 1 1379 ? 162.081 162.128 238.461 1.00 164.32 ? 1379 GLN A CB    1 
ATOM   445   C  CG    . GLN A 1 1379 ? 160.727 161.526 238.123 1.00 164.32 ? 1379 GLN A CG    1 
ATOM   446   C  CD    . GLN A 1 1379 ? 159.882 161.270 239.355 1.00 165.58 ? 1379 GLN A CD    1 
ATOM   447   O  OE1   . GLN A 1 1379 ? 160.301 161.547 240.479 1.00 164.91 ? 1379 GLN A OE1   1 
ATOM   448   N  NE2   . GLN A 1 1379 ? 158.684 160.734 239.151 1.00 165.57 ? 1379 GLN A NE2   1 
ATOM   449   N  N     . TYR A 1 1380 ? 165.492 162.137 238.001 1.00 162.10 ? 1380 TYR A N     1 
ATOM   450   C  CA    . TYR A 1 1380 ? 166.685 162.847 238.441 1.00 161.11 ? 1380 TYR A CA    1 
ATOM   451   C  C     . TYR A 1 1380 ? 167.322 163.614 237.288 1.00 159.04 ? 1380 TYR A C     1 
ATOM   452   O  O     . TYR A 1 1380 ? 167.298 163.174 236.136 1.00 159.28 ? 1380 TYR A O     1 
ATOM   453   C  CB    . TYR A 1 1380 ? 167.684 161.863 239.046 1.00 161.34 ? 1380 TYR A CB    1 
ATOM   454   C  CG    . TYR A 1 1380 ? 167.355 161.484 240.472 1.00 165.01 ? 1380 TYR A CG    1 
ATOM   455   C  CD1   . TYR A 1 1380 ? 167.463 162.413 241.499 1.00 164.54 ? 1380 TYR A CD1   1 
ATOM   456   C  CD2   . TYR A 1 1380 ? 166.914 160.206 240.787 1.00 164.19 ? 1380 TYR A CD2   1 
ATOM   457   C  CE1   . TYR A 1 1380 ? 167.157 162.074 242.805 1.00 165.55 ? 1380 TYR A CE1   1 
ATOM   458   C  CE2   . TYR A 1 1380 ? 166.605 159.858 242.089 1.00 165.86 ? 1380 TYR A CE2   1 
ATOM   459   C  CZ    . TYR A 1 1380 ? 166.728 160.795 243.093 1.00 165.97 ? 1380 TYR A CZ    1 
ATOM   460   O  OH    . TYR A 1 1380 ? 166.422 160.453 244.390 1.00 159.96 ? 1380 TYR A OH    1 
ATOM   461   N  N     . ALA A 1 1381 ? 167.895 164.776 237.613 1.00 157.96 ? 1381 ALA A N     1 
ATOM   462   C  CA    . ALA A 1 1381 ? 168.442 165.656 236.584 1.00 157.70 ? 1381 ALA A CA    1 
ATOM   463   C  C     . ALA A 1 1381 ? 169.647 165.033 235.889 1.00 158.57 ? 1381 ALA A C     1 
ATOM   464   O  O     . ALA A 1 1381 ? 169.803 165.165 234.670 1.00 156.44 ? 1381 ALA A O     1 
ATOM   465   C  CB    . ALA A 1 1381 ? 168.817 167.006 237.195 1.00 153.53 ? 1381 ALA A CB    1 
ATOM   466   N  N     . SER A 1 1382 ? 170.521 164.367 236.648 1.00 156.64 ? 1382 SER A N     1 
ATOM   467   C  CA    . SER A 1 1382 ? 171.714 163.772 236.051 1.00 153.66 ? 1382 SER A CA    1 
ATOM   468   C  C     . SER A 1 1382 ? 171.352 162.657 235.077 1.00 153.19 ? 1382 SER A C     1 
ATOM   469   O  O     . SER A 1 1382 ? 171.973 162.522 234.013 1.00 153.33 ? 1382 SER A O     1 
ATOM   470   C  CB    . SER A 1 1382 ? 172.643 163.251 237.147 1.00 152.74 ? 1382 SER A CB    1 
ATOM   471   O  OG    . SER A 1 1382 ? 173.148 164.314 237.937 1.00 149.57 ? 1382 SER A OG    1 
ATOM   472   N  N     . TYR A 1 1383 ? 170.354 161.842 235.427 1.00 155.13 ? 1383 TYR A N     1 
ATOM   473   C  CA    . TYR A 1 1383 ? 169.896 160.805 234.509 1.00 156.72 ? 1383 TYR A CA    1 
ATOM   474   C  C     . TYR A 1 1383 ? 169.363 161.414 233.221 1.00 155.65 ? 1383 TYR A C     1 
ATOM   475   O  O     . TYR A 1 1383 ? 169.636 160.907 232.129 1.00 154.75 ? 1383 TYR A O     1 
ATOM   476   C  CB    . TYR A 1 1383 ? 168.825 159.941 235.175 1.00 157.55 ? 1383 TYR A CB    1 
ATOM   477   C  CG    . TYR A 1 1383 ? 168.099 159.025 234.213 1.00 157.02 ? 1383 TYR A CG    1 
ATOM   478   C  CD1   . TYR A 1 1383 ? 168.614 157.777 233.889 1.00 157.44 ? 1383 TYR A CD1   1 
ATOM   479   C  CD2   . TYR A 1 1383 ? 166.899 159.410 233.629 1.00 156.56 ? 1383 TYR A CD2   1 
ATOM   480   C  CE1   . TYR A 1 1383 ? 167.954 156.939 233.009 1.00 158.20 ? 1383 TYR A CE1   1 
ATOM   481   C  CE2   . TYR A 1 1383 ? 166.234 158.581 232.748 1.00 157.39 ? 1383 TYR A CE2   1 
ATOM   482   C  CZ    . TYR A 1 1383 ? 166.764 157.347 232.443 1.00 158.52 ? 1383 TYR A CZ    1 
ATOM   483   O  OH    . TYR A 1 1383 ? 166.100 156.521 231.566 1.00 156.61 ? 1383 TYR A OH    1 
ATOM   484   N  N     . GLU A 1 1384 ? 168.591 162.497 233.330 1.00 156.55 ? 1384 GLU A N     1 
ATOM   485   C  CA    . GLU A 1 1384 ? 168.080 163.166 232.137 1.00 157.68 ? 1384 GLU A CA    1 
ATOM   486   C  C     . GLU A 1 1384 ? 169.217 163.734 231.296 1.00 156.55 ? 1384 GLU A C     1 
ATOM   487   O  O     . GLU A 1 1384 ? 169.181 163.664 230.062 1.00 153.42 ? 1384 GLU A O     1 
ATOM   488   C  CB    . GLU A 1 1384 ? 167.100 164.268 232.537 1.00 154.84 ? 1384 GLU A CB    1 
ATOM   489   C  CG    . GLU A 1 1384 ? 165.853 163.758 233.239 1.00 153.32 ? 1384 GLU A CG    1 
ATOM   490   C  CD    . GLU A 1 1384 ? 164.891 164.870 233.602 1.00 156.63 ? 1384 GLU A CD    1 
ATOM   491   O  OE1   . GLU A 1 1384 ? 165.023 165.978 233.041 1.00 157.57 ? 1384 GLU A OE1   1 
ATOM   492   O  OE2   . GLU A 1 1384 ? 164.003 164.637 234.449 1.00 157.38 ? 1384 GLU A OE2   1 
ATOM   493   N  N     . PHE A 1 1385 ? 170.231 164.304 231.950 1.00 154.99 ? 1385 PHE A N     1 
ATOM   494   C  CA    . PHE A 1 1385 ? 171.381 164.840 231.230 1.00 152.98 ? 1385 PHE A CA    1 
ATOM   495   C  C     . PHE A 1 1385 ? 172.100 163.745 230.455 1.00 153.37 ? 1385 PHE A C     1 
ATOM   496   O  O     . PHE A 1 1385 ? 172.442 163.920 229.280 1.00 152.84 ? 1385 PHE A O     1 
ATOM   497   C  CB    . PHE A 1 1385 ? 172.334 165.524 232.211 1.00 153.01 ? 1385 PHE A CB    1 
ATOM   498   C  CG    . PHE A 1 1385 ? 173.734 165.688 231.688 1.00 155.38 ? 1385 PHE A CG    1 
ATOM   499   C  CD1   . PHE A 1 1385 ? 173.981 166.421 230.538 1.00 155.31 ? 1385 PHE A CD1   1 
ATOM   500   C  CD2   . PHE A 1 1385 ? 174.804 165.105 232.347 1.00 155.41 ? 1385 PHE A CD2   1 
ATOM   501   C  CE1   . PHE A 1 1385 ? 175.268 166.570 230.057 1.00 156.22 ? 1385 PHE A CE1   1 
ATOM   502   C  CE2   . PHE A 1 1385 ? 176.093 165.251 231.870 1.00 157.14 ? 1385 PHE A CE2   1 
ATOM   503   C  CZ    . PHE A 1 1385 ? 176.325 165.984 230.724 1.00 157.60 ? 1385 PHE A CZ    1 
ATOM   504   N  N     . VAL A 1 1386 ? 172.329 162.597 231.094 1.00 154.06 ? 1386 VAL A N     1 
ATOM   505   C  CA    . VAL A 1 1386 ? 173.024 161.508 230.413 1.00 152.47 ? 1386 VAL A CA    1 
ATOM   506   C  C     . VAL A 1 1386 ? 172.157 160.924 229.302 1.00 150.69 ? 1386 VAL A C     1 
ATOM   507   O  O     . VAL A 1 1386 ? 172.658 160.568 228.228 1.00 148.22 ? 1386 VAL A O     1 
ATOM   508   C  CB    . VAL A 1 1386 ? 173.465 160.440 231.430 1.00 152.95 ? 1386 VAL A CB    1 
ATOM   509   C  CG1   . VAL A 1 1386 ? 173.826 159.141 230.729 1.00 152.93 ? 1386 VAL A CG1   1 
ATOM   510   C  CG2   . VAL A 1 1386 ? 174.660 160.953 232.208 1.00 151.19 ? 1386 VAL A CG2   1 
ATOM   511   N  N     . GLN A 1 1387 ? 170.844 160.832 229.530 1.00 151.89 ? 1387 GLN A N     1 
ATOM   512   C  CA    . GLN A 1 1387 ? 169.947 160.324 228.498 1.00 153.19 ? 1387 GLN A CA    1 
ATOM   513   C  C     . GLN A 1 1387 ? 169.946 161.228 227.273 1.00 152.25 ? 1387 GLN A C     1 
ATOM   514   O  O     . GLN A 1 1387 ? 170.017 160.745 226.138 1.00 150.97 ? 1387 GLN A O     1 
ATOM   515   C  CB    . GLN A 1 1387 ? 168.533 160.176 229.059 1.00 153.33 ? 1387 GLN A CB    1 
ATOM   516   C  CG    . GLN A 1 1387 ? 167.653 159.213 228.278 1.00 155.94 ? 1387 GLN A CG    1 
ATOM   517   C  CD    . GLN A 1 1387 ? 166.464 158.726 229.084 1.00 154.81 ? 1387 GLN A CD    1 
ATOM   518   O  OE1   . GLN A 1 1387 ? 166.306 157.528 229.316 1.00 156.16 ? 1387 GLN A OE1   1 
ATOM   519   N  NE2   . GLN A 1 1387 ? 165.620 159.656 229.513 1.00 151.10 ? 1387 GLN A NE2   1 
ATOM   520   N  N     . ARG A 1 1388 ? 169.882 162.546 227.478 1.00 151.42 ? 1388 ARG A N     1 
ATOM   521   C  CA    . ARG A 1 1388 ? 169.893 163.453 226.335 1.00 149.69 ? 1388 ARG A CA    1 
ATOM   522   C  C     . ARG A 1 1388 ? 171.269 163.514 225.682 1.00 146.90 ? 1388 ARG A C     1 
ATOM   523   O  O     . ARG A 1 1388 ? 171.364 163.723 224.469 1.00 143.05 ? 1388 ARG A O     1 
ATOM   524   C  CB    . ARG A 1 1388 ? 169.422 164.849 226.750 1.00 150.71 ? 1388 ARG A CB    1 
ATOM   525   C  CG    . ARG A 1 1388 ? 170.343 165.594 227.696 1.00 154.58 ? 1388 ARG A CG    1 
ATOM   526   C  CD    . ARG A 1 1388 ? 169.785 166.969 228.026 1.00 153.33 ? 1388 ARG A CD    1 
ATOM   527   N  NE    . ARG A 1 1388 ? 170.607 167.679 228.998 1.00 152.21 ? 1388 ARG A NE    1 
ATOM   528   C  CZ    . ARG A 1 1388 ? 171.646 168.442 228.684 1.00 152.56 ? 1388 ARG A CZ    1 
ATOM   529   N  NH1   . ARG A 1 1388 ? 172.024 168.611 227.428 1.00 152.46 ? 1388 ARG A NH1   1 
ATOM   530   N  NH2   . ARG A 1 1388 ? 172.320 169.052 229.655 1.00 153.46 ? 1388 ARG A NH2   1 
ATOM   531   N  N     . LEU A 1 1389 ? 172.342 163.313 226.454 1.00 147.93 ? 1389 LEU A N     1 
ATOM   532   C  CA    . LEU A 1 1389 ? 173.669 163.223 225.853 1.00 147.40 ? 1389 LEU A CA    1 
ATOM   533   C  C     . LEU A 1 1389 ? 173.779 162.002 224.949 1.00 146.01 ? 1389 LEU A C     1 
ATOM   534   O  O     . LEU A 1 1389 ? 174.318 162.085 223.839 1.00 143.50 ? 1389 LEU A O     1 
ATOM   535   C  CB    . LEU A 1 1389 ? 174.737 163.182 226.946 1.00 147.37 ? 1389 LEU A CB    1 
ATOM   536   C  CG    . LEU A 1 1389 ? 176.178 162.967 226.479 1.00 145.48 ? 1389 LEU A CG    1 
ATOM   537   C  CD1   . LEU A 1 1389 ? 176.771 164.269 225.965 1.00 143.28 ? 1389 LEU A CD1   1 
ATOM   538   C  CD2   . LEU A 1 1389 ? 177.029 162.392 227.602 1.00 145.70 ? 1389 LEU A CD2   1 
ATOM   539   N  N     . LEU A 1 1390 ? 173.262 160.857 225.402 1.00 146.24 ? 1390 LEU A N     1 
ATOM   540   C  CA    . LEU A 1 1390 ? 173.273 159.664 224.561 1.00 144.48 ? 1390 LEU A CA    1 
ATOM   541   C  C     . LEU A 1 1390 ? 172.352 159.829 223.358 1.00 144.17 ? 1390 LEU A C     1 
ATOM   542   O  O     . LEU A 1 1390 ? 172.643 159.315 222.273 1.00 144.63 ? 1390 LEU A O     1 
ATOM   543   C  CB    . LEU A 1 1390 ? 172.883 158.434 225.380 1.00 147.16 ? 1390 LEU A CB    1 
ATOM   544   C  CG    . LEU A 1 1390 ? 174.051 157.688 226.029 1.00 149.48 ? 1390 LEU A CG    1 
ATOM   545   C  CD1   . LEU A 1 1390 ? 173.570 156.440 226.750 1.00 152.22 ? 1390 LEU A CD1   1 
ATOM   546   C  CD2   . LEU A 1 1390 ? 175.104 157.335 224.993 1.00 147.58 ? 1390 LEU A CD2   1 
ATOM   547   N  N     . LYS A 1 1391 ? 171.236 160.540 223.529 1.00 145.68 ? 1391 LYS A N     1 
ATOM   548   C  CA    . LYS A 1 1391 ? 170.360 160.821 222.395 1.00 147.10 ? 1391 LYS A CA    1 
ATOM   549   C  C     . LYS A 1 1391 ? 171.061 161.696 221.361 1.00 144.58 ? 1391 LYS A C     1 
ATOM   550   O  O     . LYS A 1 1391 ? 170.935 161.466 220.153 1.00 141.00 ? 1391 LYS A O     1 
ATOM   551   C  CB    . LYS A 1 1391 ? 169.069 161.481 222.880 1.00 145.57 ? 1391 LYS A CB    1 
ATOM   552   C  CG    . LYS A 1 1391 ? 168.223 162.087 221.773 1.00 142.52 ? 1391 LYS A CG    1 
ATOM   553   C  CD    . LYS A 1 1391 ? 167.071 162.901 222.340 1.00 138.55 ? 1391 LYS A CD    1 
ATOM   554   C  CE    . LYS A 1 1391 ? 167.561 163.933 223.341 1.00 136.98 ? 1391 LYS A CE    1 
ATOM   555   N  NZ    . LYS A 1 1391 ? 166.437 164.706 223.934 1.00 129.17 ? 1391 LYS A NZ    1 
ATOM   556   N  N     . GLY A 1 1392 ? 171.806 162.705 221.816 1.00 143.33 ? 1392 GLY A N     1 
ATOM   557   C  CA    . GLY A 1 1392 ? 172.584 163.513 220.891 1.00 139.56 ? 1392 GLY A CA    1 
ATOM   558   C  C     . GLY A 1 1392 ? 173.687 162.722 220.216 1.00 137.12 ? 1392 GLY A C     1 
ATOM   559   O  O     . GLY A 1 1392 ? 173.993 162.942 219.040 1.00 132.56 ? 1392 GLY A O     1 
ATOM   560   N  N     . TYR A 1 1393 ? 174.305 161.795 220.951 1.00 139.55 ? 1393 TYR A N     1 
ATOM   561   C  CA    . TYR A 1 1393 ? 175.299 160.913 220.347 1.00 136.83 ? 1393 TYR A CA    1 
ATOM   562   C  C     . TYR A 1 1393 ? 174.668 160.046 219.265 1.00 134.20 ? 1393 TYR A C     1 
ATOM   563   O  O     . TYR A 1 1393 ? 175.248 159.855 218.191 1.00 134.66 ? 1393 TYR A O     1 
ATOM   564   C  CB    . TYR A 1 1393 ? 175.952 160.047 221.425 1.00 137.02 ? 1393 TYR A CB    1 
ATOM   565   C  CG    . TYR A 1 1393 ? 176.987 160.776 222.253 1.00 138.29 ? 1393 TYR A CG    1 
ATOM   566   C  CD1   . TYR A 1 1393 ? 177.659 160.133 223.284 1.00 138.61 ? 1393 TYR A CD1   1 
ATOM   567   C  CD2   . TYR A 1 1393 ? 177.293 162.109 222.003 1.00 138.52 ? 1393 TYR A CD2   1 
ATOM   568   C  CE1   . TYR A 1 1393 ? 178.604 160.797 224.045 1.00 141.73 ? 1393 TYR A CE1   1 
ATOM   569   C  CE2   . TYR A 1 1393 ? 178.238 162.780 222.757 1.00 139.02 ? 1393 TYR A CE2   1 
ATOM   570   C  CZ    . TYR A 1 1393 ? 178.890 162.119 223.775 1.00 140.99 ? 1393 TYR A CZ    1 
ATOM   571   O  OH    . TYR A 1 1393 ? 179.831 162.784 224.527 1.00 137.85 ? 1393 TYR A OH    1 
ATOM   572   N  N     . MET A 1 1394 ? 173.467 159.529 219.524 1.00 135.41 ? 1394 MET A N     1 
ATOM   573   C  CA    . MET A 1 1394 ? 172.737 158.787 218.502 1.00 136.59 ? 1394 MET A CA    1 
ATOM   574   C  C     . MET A 1 1394 ? 172.400 159.668 217.305 1.00 134.64 ? 1394 MET A C     1 
ATOM   575   O  O     . MET A 1 1394 ? 172.432 159.211 216.158 1.00 133.30 ? 1394 MET A O     1 
ATOM   576   C  CB    . MET A 1 1394 ? 171.466 158.186 219.101 1.00 137.09 ? 1394 MET A CB    1 
ATOM   577   C  CG    . MET A 1 1394 ? 170.720 157.283 218.145 1.00 140.73 ? 1394 MET A CG    1 
ATOM   578   S  SD    . MET A 1 1394 ? 171.640 155.800 217.714 1.00 147.98 ? 1394 MET A SD    1 
ATOM   579   C  CE    . MET A 1 1394 ? 170.876 155.414 216.144 1.00 132.96 ? 1394 MET A CE    1 
ATOM   580   N  N     . LYS A 1 1395 ? 172.047 160.929 217.555 1.00 132.12 ? 1395 LYS A N     1 
ATOM   581   C  CA    . LYS A 1 1395 ? 171.736 161.842 216.460 1.00 130.53 ? 1395 LYS A CA    1 
ATOM   582   C  C     . LYS A 1 1395 ? 172.962 162.108 215.593 1.00 128.03 ? 1395 LYS A C     1 
ATOM   583   O  O     . LYS A 1 1395 ? 172.859 162.161 214.362 1.00 124.75 ? 1395 LYS A O     1 
ATOM   584   C  CB    . LYS A 1 1395 ? 171.173 163.150 217.014 1.00 132.49 ? 1395 LYS A CB    1 
ATOM   585   C  CG    . LYS A 1 1395 ? 171.000 164.245 215.974 1.00 127.45 ? 1395 LYS A CG    1 
ATOM   586   C  CD    . LYS A 1 1395 ? 170.728 165.589 216.626 1.00 127.07 ? 1395 LYS A CD    1 
ATOM   587   C  CE    . LYS A 1 1395 ? 170.695 166.701 215.592 1.00 129.63 ? 1395 LYS A CE    1 
ATOM   588   N  NZ    . LYS A 1 1395 ? 170.436 168.029 216.211 1.00 131.46 ? 1395 LYS A NZ    1 
ATOM   589   N  N     . ILE A 1 1396 ? 174.130 162.273 216.213 1.00 127.44 ? 1396 ILE A N     1 
ATOM   590   C  CA    . ILE A 1 1396 ? 175.354 162.566 215.473 1.00 122.90 ? 1396 ILE A CA    1 
ATOM   591   C  C     . ILE A 1 1396 ? 176.003 161.269 215.006 1.00 122.66 ? 1396 ILE A C     1 
ATOM   592   O  O     . ILE A 1 1396 ? 177.065 161.285 214.377 1.00 122.49 ? 1396 ILE A O     1 
ATOM   593   C  CB    . ILE A 1 1396 ? 176.338 163.400 216.314 1.00 124.13 ? 1396 ILE A CB    1 
ATOM   594   C  CG1   . ILE A 1 1396 ? 176.883 162.573 217.480 1.00 130.11 ? 1396 ILE A CG1   1 
ATOM   595   C  CG2   . ILE A 1 1396 ? 175.670 164.674 216.810 1.00 123.40 ? 1396 ILE A CG2   1 
ATOM   596   C  CD1   . ILE A 1 1396 ? 177.853 163.327 218.363 1.00 133.93 ? 1396 ILE A CD1   1 
ATOM   597   N  N     . ASN A 1 1397 ? 175.382 160.133 215.325 1.00 124.56 ? 1397 ASN A N     1 
ATOM   598   C  CA    . ASN A 1 1397 ? 175.845 158.871 214.755 1.00 123.52 ? 1397 ASN A CA    1 
ATOM   599   C  C     . ASN A 1 1397 ? 175.827 158.910 213.233 1.00 120.29 ? 1397 ASN A C     1 
ATOM   600   O  O     . ASN A 1 1397 ? 176.682 158.303 212.581 1.00 120.72 ? 1397 ASN A O     1 
ATOM   601   C  CB    . ASN A 1 1397 ? 174.993 157.712 215.269 1.00 126.26 ? 1397 ASN A CB    1 
ATOM   602   C  CG    . ASN A 1 1397 ? 175.417 156.378 214.692 1.00 126.04 ? 1397 ASN A CG    1 
ATOM   603   O  OD1   . ASN A 1 1397 ? 174.611 155.664 214.096 1.00 127.94 ? 1397 ASN A OD1   1 
ATOM   604   N  ND2   . ASN A 1 1397 ? 176.687 156.033 214.865 1.00 121.81 ? 1397 ASN A ND2   1 
ATOM   605   N  N     . MET A 1 1398 ? 174.854 159.612 212.647 1.00 118.72 ? 1398 MET A N     1 
ATOM   606   C  CA    . MET A 1 1398 ? 174.820 159.753 211.194 1.00 115.67 ? 1398 MET A CA    1 
ATOM   607   C  C     . MET A 1 1398 ? 176.059 160.481 210.691 1.00 116.69 ? 1398 MET A C     1 
ATOM   608   O  O     . MET A 1 1398 ? 176.690 160.061 209.709 1.00 118.64 ? 1398 MET A O     1 
ATOM   609   C  CB    . MET A 1 1398 ? 173.548 160.486 210.778 1.00 117.25 ? 1398 MET A CB    1 
ATOM   610   C  CG    . MET A 1 1398 ? 173.332 160.587 209.283 1.00 119.86 ? 1398 MET A CG    1 
ATOM   611   S  SD    . MET A 1 1398 ? 171.796 161.458 208.932 1.00 137.42 ? 1398 MET A SD    1 
ATOM   612   C  CE    . MET A 1 1398 ? 170.604 160.220 209.436 1.00 107.57 ? 1398 MET A CE    1 
ATOM   613   N  N     . LEU A 1 1399 ? 176.443 161.561 211.375 1.00 116.43 ? 1399 LEU A N     1 
ATOM   614   C  CA    . LEU A 1 1399 ? 177.708 162.214 211.069 1.00 111.05 ? 1399 LEU A CA    1 
ATOM   615   C  C     . LEU A 1 1399 ? 178.884 161.290 211.345 1.00 109.23 ? 1399 LEU A C     1 
ATOM   616   O  O     . LEU A 1 1399 ? 179.966 161.488 210.792 1.00 110.56 ? 1399 LEU A O     1 
ATOM   617   C  CB    . LEU A 1 1399 ? 177.852 163.505 211.878 1.00 109.65 ? 1399 LEU A CB    1 
ATOM   618   C  CG    . LEU A 1 1399 ? 177.189 164.790 211.367 1.00 110.84 ? 1399 LEU A CG    1 
ATOM   619   C  CD1   . LEU A 1 1399 ? 177.792 165.215 210.037 1.00 105.38 ? 1399 LEU A CD1   1 
ATOM   620   C  CD2   . LEU A 1 1399 ? 175.674 164.662 211.262 1.00 112.27 ? 1399 LEU A CD2   1 
ATOM   621   N  N     . VAL A 1 1400 ? 178.703 160.296 212.215 1.00 111.90 ? 1400 VAL A N     1 
ATOM   622   C  CA    . VAL A 1 1400 ? 179.772 159.332 212.467 1.00 108.67 ? 1400 VAL A CA    1 
ATOM   623   C  C     . VAL A 1 1400 ? 179.976 158.425 211.257 1.00 109.62 ? 1400 VAL A C     1 
ATOM   624   O  O     . VAL A 1 1400 ? 181.114 158.175 210.841 1.00 114.19 ? 1400 VAL A O     1 
ATOM   625   C  CB    . VAL A 1 1400 ? 179.489 158.520 213.743 1.00 116.41 ? 1400 VAL A CB    1 
ATOM   626   C  CG1   . VAL A 1 1400 ? 180.412 157.316 213.821 1.00 118.13 ? 1400 VAL A CG1   1 
ATOM   627   C  CG2   . VAL A 1 1400 ? 179.649 159.394 214.971 1.00 117.77 ? 1400 VAL A CG2   1 
ATOM   628   N  N     . ILE A 1 1401 ? 178.886 157.904 210.676 1.00 110.03 ? 1401 ILE A N     1 
ATOM   629   C  CA    . ILE A 1 1401 ? 179.043 157.150 209.426 1.00 105.55 ? 1401 ILE A CA    1 
ATOM   630   C  C     . ILE A 1 1401 ? 179.642 158.042 208.347 1.00 104.20 ? 1401 ILE A C     1 
ATOM   631   O  O     . ILE A 1 1401 ? 180.528 157.624 207.592 1.00 102.54 ? 1401 ILE A O     1 
ATOM   632   C  CB    . ILE A 1 1401 ? 177.734 156.497 208.924 1.00 106.22 ? 1401 ILE A CB    1 
ATOM   633   C  CG1   . ILE A 1 1401 ? 176.949 155.709 209.974 1.00 111.65 ? 1401 ILE A CG1   1 
ATOM   634   C  CG2   . ILE A 1 1401 ? 178.017 155.582 207.739 1.00 105.29 ? 1401 ILE A CG2   1 
ATOM   635   C  CD1   . ILE A 1 1401 ? 175.857 156.435 210.626 1.00 109.57 ? 1401 ILE A CD1   1 
ATOM   636   N  N     . GLU A 1 1402 ? 179.164 159.286 208.252 1.00 106.50 ? 1402 GLU A N     1 
ATOM   637   C  CA    . GLU A 1 1402 ? 179.665 160.170 207.203 1.00 109.16 ? 1402 GLU A CA    1 
ATOM   638   C  C     . GLU A 1 1402 ? 181.137 160.529 207.401 1.00 105.77 ? 1402 GLU A C     1 
ATOM   639   O  O     . GLU A 1 1402 ? 181.863 160.713 206.418 1.00 107.08 ? 1402 GLU A O     1 
ATOM   640   C  CB    . GLU A 1 1402 ? 178.802 161.429 207.127 1.00 110.32 ? 1402 GLU A CB    1 
ATOM   641   C  CG    . GLU A 1 1402 ? 177.358 161.170 206.730 1.00 110.61 ? 1402 GLU A CG    1 
ATOM   642   C  CD    . GLU A 1 1402 ? 176.480 162.395 206.886 1.00 115.02 ? 1402 GLU A CD    1 
ATOM   643   O  OE1   . GLU A 1 1402 ? 176.991 163.445 207.329 1.00 116.35 ? 1402 GLU A OE1   1 
ATOM   644   O  OE2   . GLU A 1 1402 ? 175.277 162.310 206.563 1.00 116.53 ? 1402 GLU A OE2   1 
ATOM   645   N  N     . LEU A 1 1403 ? 181.594 160.636 208.651 1.00 102.33 ? 1403 LEU A N     1 
ATOM   646   C  CA    . LEU A 1 1403 ? 182.994 160.942 208.930 1.00 99.53  ? 1403 LEU A CA    1 
ATOM   647   C  C     . LEU A 1 1403 ? 183.891 159.729 208.723 1.00 103.74 ? 1403 LEU A C     1 
ATOM   648   O  O     . LEU A 1 1403 ? 185.007 159.861 208.211 1.00 105.67 ? 1403 LEU A O     1 
ATOM   649   C  CB    . LEU A 1 1403 ? 183.147 161.464 210.360 1.00 104.66 ? 1403 LEU A CB    1 
ATOM   650   C  CG    . LEU A 1 1403 ? 182.819 162.931 210.642 1.00 106.51 ? 1403 LEU A CG    1 
ATOM   651   C  CD1   . LEU A 1 1403 ? 183.253 163.308 212.048 1.00 104.55 ? 1403 LEU A CD1   1 
ATOM   652   C  CD2   . LEU A 1 1403 ? 183.487 163.831 209.626 1.00 103.00 ? 1403 LEU A CD2   1 
ATOM   653   N  N     . LYS A 1 1404 ? 183.427 158.544 209.116 1.00 105.95 ? 1404 LYS A N     1 
ATOM   654   C  CA    . LYS A 1 1404 ? 184.222 157.334 208.948 1.00 105.28 ? 1404 LYS A CA    1 
ATOM   655   C  C     . LYS A 1 1404 ? 184.109 156.869 207.501 1.00 107.85 ? 1404 LYS A C     1 
ATOM   656   O  O     . LYS A 1 1404 ? 183.511 155.828 207.211 1.00 106.63 ? 1404 LYS A O     1 
ATOM   657   C  CB    . LYS A 1 1404 ? 183.769 156.248 209.928 1.00 108.89 ? 1404 LYS A CB    1 
ATOM   658   C  CG    . LYS A 1 1404 ? 184.598 154.969 209.894 1.00 114.12 ? 1404 LYS A CG    1 
ATOM   659   C  CD    . LYS A 1 1404 ? 185.998 155.207 210.432 1.00 118.16 ? 1404 LYS A CD    1 
ATOM   660   C  CE    . LYS A 1 1404 ? 186.792 153.914 210.485 1.00 121.36 ? 1404 LYS A CE    1 
ATOM   661   N  NZ    . LYS A 1 1404 ? 188.190 154.141 210.941 1.00 128.22 ? 1404 LYS A NZ    1 
ATOM   662   N  N     . SER A 1 1405 ? 184.657 157.661 206.586 1.00 107.24 ? 1405 SER A N     1 
ATOM   663   C  CA    . SER A 1 1405 ? 184.606 157.365 205.167 1.00 104.16 ? 1405 SER A CA    1 
ATOM   664   C  C     . SER A 1 1405 ? 186.017 157.332 204.587 1.00 107.23 ? 1405 SER A C     1 
ATOM   665   O  O     . SER A 1 1405 ? 186.991 157.740 205.224 1.00 107.08 ? 1405 SER A O     1 
ATOM   666   C  CB    . SER A 1 1405 ? 183.736 158.392 204.447 1.00 98.46  ? 1405 SER A CB    1 
ATOM   667   O  OG    . SER A 1 1405 ? 183.697 158.140 203.056 1.00 99.08  ? 1405 SER A OG    1 
ATOM   668   N  N     . GLU A 1 1406 ? 186.130 156.836 203.356 1.00 106.06 ? 1406 GLU A N     1 
ATOM   669   C  CA    . GLU A 1 1406 ? 187.409 156.821 202.657 1.00 101.81 ? 1406 GLU A CA    1 
ATOM   670   C  C     . GLU A 1 1406 ? 187.678 158.131 201.929 1.00 103.45 ? 1406 GLU A C     1 
ATOM   671   O  O     . GLU A 1 1406 ? 188.806 158.375 201.489 1.00 104.30 ? 1406 GLU A O     1 
ATOM   672   C  CB    . GLU A 1 1406 ? 187.454 155.653 201.668 1.00 98.93  ? 1406 GLU A CB    1 
ATOM   673   C  CG    . GLU A 1 1406 ? 187.464 154.281 202.323 1.00 100.74 ? 1406 GLU A CG    1 
ATOM   674   C  CD    . GLU A 1 1406 ? 186.080 153.804 202.711 1.00 107.58 ? 1406 GLU A CD    1 
ATOM   675   O  OE1   . GLU A 1 1406 ? 185.099 154.517 202.415 1.00 109.39 ? 1406 GLU A OE1   1 
ATOM   676   O  OE2   . GLU A 1 1406 ? 185.971 152.715 203.312 1.00 109.32 ? 1406 GLU A OE2   1 
ATOM   677   N  N     . ALA A 1 1407 ? 186.659 158.984 201.800 1.00 102.33 ? 1407 ALA A N     1 
ATOM   678   C  CA    . ALA A 1 1407 ? 186.842 160.264 201.127 1.00 93.91  ? 1407 ALA A CA    1 
ATOM   679   C  C     . ALA A 1 1407 ? 187.603 161.255 201.994 1.00 99.23  ? 1407 ALA A C     1 
ATOM   680   O  O     . ALA A 1 1407 ? 188.254 162.166 201.470 1.00 100.04 ? 1407 ALA A O     1 
ATOM   681   C  CB    . ALA A 1 1407 ? 185.486 160.853 200.738 1.00 86.52  ? 1407 ALA A CB    1 
ATOM   682   N  N     . LEU A 1 1408 ? 187.536 161.094 203.316 1.00 99.16  ? 1408 LEU A N     1 
ATOM   683   C  CA    . LEU A 1 1408 ? 188.014 162.137 204.213 1.00 101.85 ? 1408 LEU A CA    1 
ATOM   684   C  C     . LEU A 1 1408 ? 189.534 162.247 204.230 1.00 103.66 ? 1408 LEU A C     1 
ATOM   685   O  O     . LEU A 1 1408 ? 190.058 163.305 204.593 1.00 102.47 ? 1408 LEU A O     1 
ATOM   686   C  CB    . LEU A 1 1408 ? 187.473 161.886 205.621 1.00 102.47 ? 1408 LEU A CB    1 
ATOM   687   C  CG    . LEU A 1 1408 ? 187.139 163.146 206.419 1.00 102.50 ? 1408 LEU A CG    1 
ATOM   688   C  CD1   . LEU A 1 1408 ? 186.270 164.075 205.591 1.00 93.97  ? 1408 LEU A CD1   1 
ATOM   689   C  CD2   . LEU A 1 1408 ? 186.432 162.781 207.706 1.00 104.62 ? 1408 LEU A CD2   1 
ATOM   690   N  N     . LYS A 1 1409 ? 190.250 161.188 203.845 1.00 105.34 ? 1409 LYS A N     1 
ATOM   691   C  CA    . LYS A 1 1409 ? 191.704 161.227 203.710 1.00 106.45 ? 1409 LYS A CA    1 
ATOM   692   C  C     . LYS A 1 1409 ? 192.382 161.781 204.959 1.00 107.13 ? 1409 LYS A C     1 
ATOM   693   O  O     . LYS A 1 1409 ? 191.894 161.586 206.075 1.00 109.10 ? 1409 LYS A O     1 
ATOM   694   C  CB    . LYS A 1 1409 ? 192.103 162.057 202.487 1.00 101.18 ? 1409 LYS A CB    1 
ATOM   695   C  CG    . LYS A 1 1409 ? 191.564 161.520 201.172 1.00 100.51 ? 1409 LYS A CG    1 
ATOM   696   C  CD    . LYS A 1 1409 ? 192.166 160.165 200.845 1.00 100.00 ? 1409 LYS A CD    1 
ATOM   697   C  CE    . LYS A 1 1409 ? 191.759 159.694 199.459 1.00 97.65  ? 1409 LYS A CE    1 
ATOM   698   N  NZ    . LYS A 1 1409 ? 190.313 159.350 199.386 1.00 90.68  ? 1409 LYS A NZ    1 
ATOM   699   N  N     . ASP A 1 1410 ? 193.514 162.458 204.779 1.00 104.14 ? 1410 ASP A N     1 
ATOM   700   C  CA    . ASP A 1 1410 ? 194.203 163.156 205.857 1.00 108.42 ? 1410 ASP A CA    1 
ATOM   701   C  C     . ASP A 1 1410 ? 194.077 164.667 205.745 1.00 107.58 ? 1410 ASP A C     1 
ATOM   702   O  O     . ASP A 1 1410 ? 193.956 165.359 206.761 1.00 107.45 ? 1410 ASP A O     1 
ATOM   703   C  CB    . ASP A 1 1410 ? 195.686 162.761 205.881 1.00 108.67 ? 1410 ASP A CB    1 
ATOM   704   C  CG    . ASP A 1 1410 ? 196.425 163.350 207.067 1.00 113.60 ? 1410 ASP A CG    1 
ATOM   705   O  OD1   . ASP A 1 1410 ? 196.228 162.859 208.198 1.00 119.42 ? 1410 ASP A OD1   1 
ATOM   706   O  OD2   . ASP A 1 1410 ? 197.203 164.307 206.867 1.00 109.73 ? 1410 ASP A OD2   1 
ATOM   707   N  N     . ARG A 1 1411 ? 194.112 165.193 204.523 1.00 105.33 ? 1411 ARG A N     1 
ATOM   708   C  CA    . ARG A 1 1411 ? 193.994 166.622 204.257 1.00 104.12 ? 1411 ARG A CA    1 
ATOM   709   C  C     . ARG A 1 1411 ? 192.666 167.202 204.736 1.00 101.99 ? 1411 ARG A C     1 
ATOM   710   O  O     . ARG A 1 1411 ? 192.639 168.298 205.305 1.00 101.26 ? 1411 ARG A O     1 
ATOM   711   C  CB    . ARG A 1 1411 ? 194.209 166.863 202.760 1.00 97.48  ? 1411 ARG A CB    1 
ATOM   712   C  CG    . ARG A 1 1411 ? 193.201 166.147 201.883 1.00 98.45  ? 1411 ARG A CG    1 
ATOM   713   C  CD    . ARG A 1 1411 ? 193.517 166.280 200.410 1.00 90.25  ? 1411 ARG A CD    1 
ATOM   714   N  NE    . ARG A 1 1411 ? 192.555 165.532 199.611 1.00 95.18  ? 1411 ARG A NE    1 
ATOM   715   C  CZ    . ARG A 1 1411 ? 192.580 165.444 198.289 1.00 90.70  ? 1411 ARG A CZ    1 
ATOM   716   N  NH1   . ARG A 1 1411 ? 193.513 166.048 197.574 1.00 88.84  ? 1411 ARG A NH1   1 
ATOM   717   N  NH2   . ARG A 1 1411 ? 191.645 164.731 197.669 1.00 87.24  ? 1411 ARG A NH2   1 
ATOM   718   N  N     . HIS A 1 1412 ? 191.562 166.485 204.524 1.00 99.85  ? 1412 HIS A N     1 
ATOM   719   C  CA    . HIS A 1 1412 ? 190.273 166.970 205.006 1.00 97.63  ? 1412 HIS A CA    1 
ATOM   720   C  C     . HIS A 1 1412 ? 190.182 166.848 206.522 1.00 105.65 ? 1412 HIS A C     1 
ATOM   721   O  O     . HIS A 1 1412 ? 189.600 167.712 207.194 1.00 108.06 ? 1412 HIS A O     1 
ATOM   722   C  CB    . HIS A 1 1412 ? 189.139 166.204 204.325 1.00 96.63  ? 1412 HIS A CB    1 
ATOM   723   C  CG    . HIS A 1 1412 ? 189.233 166.196 202.831 1.00 93.36  ? 1412 HIS A CG    1 
ATOM   724   N  ND1   . HIS A 1 1412 ? 189.356 167.349 202.088 1.00 94.03  ? 1412 HIS A ND1   1 
ATOM   725   C  CD2   . HIS A 1 1412 ? 189.229 165.174 201.943 1.00 89.55  ? 1412 HIS A CD2   1 
ATOM   726   C  CE1   . HIS A 1 1412 ? 189.421 167.039 200.806 1.00 89.33  ? 1412 HIS A CE1   1 
ATOM   727   N  NE2   . HIS A 1 1412 ? 189.345 165.726 200.691 1.00 86.70  ? 1412 HIS A NE2   1 
ATOM   728   N  N     . TRP A 1 1413 ? 190.757 165.779 207.080 1.00 107.51 ? 1413 TRP A N     1 
ATOM   729   C  CA    . TRP A 1 1413 ? 190.923 165.718 208.524 1.00 107.87 ? 1413 TRP A CA    1 
ATOM   730   C  C     . TRP A 1 1413 ? 191.791 166.855 209.032 1.00 109.74 ? 1413 TRP A C     1 
ATOM   731   O  O     . TRP A 1 1413 ? 191.562 167.344 210.138 1.00 109.56 ? 1413 TRP A O     1 
ATOM   732   C  CB    . TRP A 1 1413 ? 191.520 164.377 208.956 1.00 97.70  ? 1413 TRP A CB    1 
ATOM   733   C  CG    . TRP A 1 1413 ? 190.494 163.316 209.187 1.00 100.69 ? 1413 TRP A CG    1 
ATOM   734   C  CD1   . TRP A 1 1413 ? 190.214 162.257 208.379 1.00 101.48 ? 1413 TRP A CD1   1 
ATOM   735   C  CD2   . TRP A 1 1413 ? 189.586 163.228 210.291 1.00 107.74 ? 1413 TRP A CD2   1 
ATOM   736   N  NE1   . TRP A 1 1413 ? 189.202 161.502 208.918 1.00 101.88 ? 1413 TRP A NE1   1 
ATOM   737   C  CE2   . TRP A 1 1413 ? 188.796 162.080 210.092 1.00 108.48 ? 1413 TRP A CE2   1 
ATOM   738   C  CE3   . TRP A 1 1413 ? 189.368 164.006 211.432 1.00 111.56 ? 1413 TRP A CE3   1 
ATOM   739   C  CZ2   . TRP A 1 1413 ? 187.806 161.691 210.988 1.00 111.76 ? 1413 TRP A CZ2   1 
ATOM   740   C  CZ3   . TRP A 1 1413 ? 188.384 163.617 212.321 1.00 112.08 ? 1413 TRP A CZ3   1 
ATOM   741   C  CH2   . TRP A 1 1413 ? 187.616 162.471 212.094 1.00 113.60 ? 1413 TRP A CH2   1 
ATOM   742   N  N     . LYS A 1 1414 ? 192.770 167.304 208.243 1.00 109.09 ? 1414 LYS A N     1 
ATOM   743   C  CA    . LYS A 1 1414 ? 193.554 168.475 208.624 1.00 110.22 ? 1414 LYS A CA    1 
ATOM   744   C  C     . LYS A 1 1414 ? 192.719 169.751 208.565 1.00 110.43 ? 1414 LYS A C     1 
ATOM   745   O  O     . LYS A 1 1414 ? 192.920 170.665 209.371 1.00 110.52 ? 1414 LYS A O     1 
ATOM   746   C  CB    . LYS A 1 1414 ? 194.789 168.597 207.731 1.00 110.29 ? 1414 LYS A CB    1 
ATOM   747   C  CG    . LYS A 1 1414 ? 195.696 169.766 208.078 1.00 108.55 ? 1414 LYS A CG    1 
ATOM   748   C  CD    . LYS A 1 1414 ? 196.279 169.621 209.475 1.00 108.15 ? 1414 LYS A CD    1 
ATOM   749   C  CE    . LYS A 1 1414 ? 197.290 168.489 209.546 1.00 104.50 ? 1414 LYS A CE    1 
ATOM   750   N  NZ    . LYS A 1 1414 ? 197.911 168.386 210.896 1.00 104.39 ? 1414 LYS A NZ    1 
ATOM   751   N  N     . GLN A 1 1415 ? 191.789 169.839 207.614 1.00 109.09 ? 1415 GLN A N     1 
ATOM   752   C  CA    . GLN A 1 1415 ? 190.885 170.986 207.569 1.00 108.42 ? 1415 GLN A CA    1 
ATOM   753   C  C     . GLN A 1 1415 ? 189.987 171.028 208.802 1.00 111.37 ? 1415 GLN A C     1 
ATOM   754   O  O     . GLN A 1 1415 ? 189.769 172.094 209.391 1.00 114.44 ? 1415 GLN A O     1 
ATOM   755   C  CB    . GLN A 1 1415 ? 190.051 170.945 206.287 1.00 105.12 ? 1415 GLN A CB    1 
ATOM   756   C  CG    . GLN A 1 1415 ? 190.879 170.893 205.009 1.00 102.84 ? 1415 GLN A CG    1 
ATOM   757   C  CD    . GLN A 1 1415 ? 190.032 170.908 203.748 1.00 104.43 ? 1415 GLN A CD    1 
ATOM   758   O  OE1   . GLN A 1 1415 ? 188.803 170.944 203.810 1.00 100.41 ? 1415 GLN A OE1   1 
ATOM   759   N  NE2   . GLN A 1 1415 ? 190.690 170.876 202.594 1.00 103.68 ? 1415 GLN A NE2   1 
ATOM   760   N  N     . LEU A 1 1416 ? 189.441 169.872 209.196 1.00 108.00 ? 1416 LEU A N     1 
ATOM   761   C  CA    . LEU A 1 1416 ? 188.674 169.799 210.441 1.00 110.70 ? 1416 LEU A CA    1 
ATOM   762   C  C     . LEU A 1 1416 ? 189.551 170.136 211.639 1.00 116.29 ? 1416 LEU A C     1 
ATOM   763   O  O     . LEU A 1 1416 ? 189.128 170.854 212.553 1.00 120.19 ? 1416 LEU A O     1 
ATOM   764   C  CB    . LEU A 1 1416 ? 188.069 168.409 210.616 1.00 111.15 ? 1416 LEU A CB    1 
ATOM   765   C  CG    . LEU A 1 1416 ? 186.855 168.066 209.762 1.00 109.32 ? 1416 LEU A CG    1 
ATOM   766   C  CD1   . LEU A 1 1416 ? 186.431 166.634 210.034 1.00 103.08 ? 1416 LEU A CD1   1 
ATOM   767   C  CD2   . LEU A 1 1416 ? 185.722 169.044 210.036 1.00 110.14 ? 1416 LEU A CD2   1 
ATOM   768   N  N     . MET A 1 1417 ? 190.780 169.615 211.635 1.00 115.00 ? 1417 MET A N     1 
ATOM   769   C  CA    . MET A 1 1417 ? 191.799 169.931 212.628 1.00 116.20 ? 1417 MET A CA    1 
ATOM   770   C  C     . MET A 1 1417 ? 191.958 171.432 212.803 1.00 118.91 ? 1417 MET A C     1 
ATOM   771   O  O     . MET A 1 1417 ? 191.953 171.946 213.926 1.00 118.49 ? 1417 MET A O     1 
ATOM   772   C  CB    . MET A 1 1417 ? 193.113 169.301 212.155 1.00 111.92 ? 1417 MET A CB    1 
ATOM   773   C  CG    . MET A 1 1417 ? 194.329 169.357 213.049 1.00 114.61 ? 1417 MET A CG    1 
ATOM   774   S  SD    . MET A 1 1417 ? 194.266 168.447 214.586 1.00 129.44 ? 1417 MET A SD    1 
ATOM   775   C  CE    . MET A 1 1417 ? 195.511 169.365 215.488 1.00 126.16 ? 1417 MET A CE    1 
ATOM   776   N  N     . LYS A 1 1418 ? 192.100 172.148 211.691 1.00 119.12 ? 1418 LYS A N     1 
ATOM   777   C  CA    . LYS A 1 1418 ? 192.360 173.580 211.754 1.00 118.23 ? 1418 LYS A CA    1 
ATOM   778   C  C     . LYS A 1 1418 ? 191.113 174.355 212.162 1.00 123.27 ? 1418 LYS A C     1 
ATOM   779   O  O     . LYS A 1 1418 ? 191.168 175.212 213.052 1.00 128.83 ? 1418 LYS A O     1 
ATOM   780   C  CB    . LYS A 1 1418 ? 192.888 174.069 210.404 1.00 117.09 ? 1418 LYS A CB    1 
ATOM   781   C  CG    . LYS A 1 1418 ? 193.171 175.563 210.317 1.00 114.96 ? 1418 LYS A CG    1 
ATOM   782   C  CD    . LYS A 1 1418 ? 192.023 176.308 209.638 1.00 121.89 ? 1418 LYS A CD    1 
ATOM   783   C  CE    . LYS A 1 1418 ? 192.057 176.137 208.124 1.00 122.76 ? 1418 LYS A CE    1 
ATOM   784   N  NZ    . LYS A 1 1418 ? 190.837 176.671 207.449 1.00 121.75 ? 1418 LYS A NZ    1 
ATOM   785   N  N     . ARG A 1 1419 ? 189.976 174.072 211.524 1.00 123.72 ? 1419 ARG A N     1 
ATOM   786   C  CA    . ARG A 1 1419 ? 188.801 174.908 211.734 1.00 126.90 ? 1419 ARG A CA    1 
ATOM   787   C  C     . ARG A 1 1419 ? 188.084 174.613 213.048 1.00 127.90 ? 1419 ARG A C     1 
ATOM   788   O  O     . ARG A 1 1419 ? 187.404 175.502 213.572 1.00 126.90 ? 1419 ARG A O     1 
ATOM   789   C  CB    . ARG A 1 1419 ? 187.833 174.767 210.552 1.00 127.35 ? 1419 ARG A CB    1 
ATOM   790   C  CG    . ARG A 1 1419 ? 186.636 175.709 210.612 1.00 128.86 ? 1419 ARG A CG    1 
ATOM   791   C  CD    . ARG A 1 1419 ? 185.732 175.574 209.400 1.00 128.09 ? 1419 ARG A CD    1 
ATOM   792   N  NE    . ARG A 1 1419 ? 186.398 175.969 208.166 1.00 131.50 ? 1419 ARG A NE    1 
ATOM   793   C  CZ    . ARG A 1 1419 ? 186.696 175.133 207.181 1.00 133.49 ? 1419 ARG A CZ    1 
ATOM   794   N  NH1   . ARG A 1 1419 ? 186.400 173.846 207.256 1.00 127.92 ? 1419 ARG A NH1   1 
ATOM   795   N  NH2   . ARG A 1 1419 ? 187.301 175.601 206.093 1.00 136.85 ? 1419 ARG A NH2   1 
ATOM   796   N  N     . LEU A 1 1420 ? 188.230 173.412 213.610 1.00 129.27 ? 1420 LEU A N     1 
ATOM   797   C  CA    . LEU A 1 1420 ? 187.661 173.123 214.920 1.00 129.49 ? 1420 LEU A CA    1 
ATOM   798   C  C     . LEU A 1 1420 ? 188.544 173.590 216.069 1.00 128.82 ? 1420 LEU A C     1 
ATOM   799   O  O     . LEU A 1 1420 ? 188.091 173.573 217.220 1.00 128.05 ? 1420 LEU A O     1 
ATOM   800   C  CB    . LEU A 1 1420 ? 187.383 171.622 215.066 1.00 128.20 ? 1420 LEU A CB    1 
ATOM   801   C  CG    . LEU A 1 1420 ? 186.311 171.044 214.142 1.00 122.43 ? 1420 LEU A CG    1 
ATOM   802   C  CD1   . LEU A 1 1420 ? 185.943 169.629 214.558 1.00 118.87 ? 1420 LEU A CD1   1 
ATOM   803   C  CD2   . LEU A 1 1420 ? 185.090 171.946 214.131 1.00 121.65 ? 1420 LEU A CD2   1 
ATOM   804   N  N     . HIS A 1 1421 ? 189.778 174.016 215.783 1.00 128.69 ? 1421 HIS A N     1 
ATOM   805   C  CA    . HIS A 1 1421 ? 190.692 174.549 216.796 1.00 129.14 ? 1421 HIS A CA    1 
ATOM   806   C  C     . HIS A 1 1421 ? 190.904 173.560 217.939 1.00 130.85 ? 1421 HIS A C     1 
ATOM   807   O  O     . HIS A 1 1421 ? 190.879 173.923 219.116 1.00 133.79 ? 1421 HIS A O     1 
ATOM   808   C  CB    . HIS A 1 1421 ? 190.198 175.896 217.325 1.00 130.99 ? 1421 HIS A CB    1 
ATOM   809   C  CG    . HIS A 1 1421 ? 189.613 176.783 216.271 1.00 132.06 ? 1421 HIS A CG    1 
ATOM   810   N  ND1   . HIS A 1 1421 ? 190.332 177.203 215.173 1.00 130.81 ? 1421 HIS A ND1   1 
ATOM   811   C  CD2   . HIS A 1 1421 ? 188.380 177.330 216.145 1.00 130.14 ? 1421 HIS A CD2   1 
ATOM   812   C  CE1   . HIS A 1 1421 ? 189.569 177.971 214.417 1.00 130.46 ? 1421 HIS A CE1   1 
ATOM   813   N  NE2   . HIS A 1 1421 ? 188.380 178.064 214.984 1.00 131.32 ? 1421 HIS A NE2   1 
ATOM   814   N  N     . VAL A 1 1422 ? 191.100 172.294 217.588 1.00 131.82 ? 1422 VAL A N     1 
ATOM   815   C  CA    . VAL A 1 1422 ? 191.402 171.240 218.547 1.00 133.44 ? 1422 VAL A CA    1 
ATOM   816   C  C     . VAL A 1 1422 ? 192.690 170.553 218.122 1.00 133.03 ? 1422 VAL A C     1 
ATOM   817   O  O     . VAL A 1 1422 ? 192.920 170.324 216.930 1.00 132.91 ? 1422 VAL A O     1 
ATOM   818   C  CB    . VAL A 1 1422 ? 190.247 170.221 218.673 1.00 130.79 ? 1422 VAL A CB    1 
ATOM   819   C  CG1   . VAL A 1 1422 ? 189.087 170.823 219.456 1.00 129.76 ? 1422 VAL A CG1   1 
ATOM   820   C  CG2   . VAL A 1 1422 ? 189.784 169.771 217.302 1.00 128.83 ? 1422 VAL A CG2   1 
ATOM   821   N  N     . ASN A 1 1423 ? 193.532 170.234 219.103 1.00 134.45 ? 1423 ASN A N     1 
ATOM   822   C  CA    . ASN A 1 1423 ? 194.831 169.610 218.841 1.00 133.56 ? 1423 ASN A CA    1 
ATOM   823   C  C     . ASN A 1 1423 ? 194.718 168.092 218.983 1.00 134.79 ? 1423 ASN A C     1 
ATOM   824   O  O     . ASN A 1 1423 ? 195.068 167.494 219.999 1.00 135.62 ? 1423 ASN A O     1 
ATOM   825   C  CB    . ASN A 1 1423 ? 195.901 170.189 219.759 1.00 133.89 ? 1423 ASN A CB    1 
ATOM   826   C  CG    . ASN A 1 1423 ? 196.076 171.682 219.579 1.00 131.24 ? 1423 ASN A CG    1 
ATOM   827   O  OD1   . ASN A 1 1423 ? 195.402 172.303 218.755 1.00 128.30 ? 1423 ASN A OD1   1 
ATOM   828   N  ND2   . ASN A 1 1423 ? 196.989 172.269 220.347 1.00 127.69 ? 1423 ASN A ND2   1 
ATOM   829   N  N     . TRP A 1 1424 ? 194.225 167.471 217.914 1.00 136.02 ? 1424 TRP A N     1 
ATOM   830   C  CA    . TRP A 1 1424 ? 194.076 166.027 217.858 1.00 135.21 ? 1424 TRP A CA    1 
ATOM   831   C  C     . TRP A 1 1424 ? 195.341 165.363 217.317 1.00 133.01 ? 1424 TRP A C     1 
ATOM   832   O  O     . TRP A 1 1424 ? 196.182 165.991 216.669 1.00 132.57 ? 1424 TRP A O     1 
ATOM   833   C  CB    . TRP A 1 1424 ? 192.885 165.644 216.979 1.00 134.69 ? 1424 TRP A CB    1 
ATOM   834   C  CG    . TRP A 1 1424 ? 191.555 165.816 217.633 1.00 136.13 ? 1424 TRP A CG    1 
ATOM   835   C  CD1   . TRP A 1 1424 ? 191.312 166.060 218.952 1.00 137.26 ? 1424 TRP A CD1   1 
ATOM   836   C  CD2   . TRP A 1 1424 ? 190.275 165.751 216.993 1.00 134.51 ? 1424 TRP A CD2   1 
ATOM   837   N  NE1   . TRP A 1 1424 ? 189.959 166.153 219.174 1.00 141.46 ? 1424 TRP A NE1   1 
ATOM   838   C  CE2   . TRP A 1 1424 ? 189.301 165.967 217.986 1.00 141.35 ? 1424 TRP A CE2   1 
ATOM   839   C  CE3   . TRP A 1 1424 ? 189.860 165.532 215.676 1.00 126.80 ? 1424 TRP A CE3   1 
ATOM   840   C  CZ2   . TRP A 1 1424 ? 187.936 165.971 217.705 1.00 140.89 ? 1424 TRP A CZ2   1 
ATOM   841   C  CZ3   . TRP A 1 1424 ? 188.506 165.536 215.398 1.00 131.27 ? 1424 TRP A CZ3   1 
ATOM   842   C  CH2   . TRP A 1 1424 ? 187.560 165.755 216.407 1.00 138.29 ? 1424 TRP A CH2   1 
ATOM   843   N  N     . VAL A 1 1425 ? 195.462 164.068 217.594 1.00 133.61 ? 1425 VAL A N     1 
ATOM   844   C  CA    . VAL A 1 1425 ? 196.492 163.215 217.013 1.00 137.30 ? 1425 VAL A CA    1 
ATOM   845   C  C     . VAL A 1 1425 ? 195.784 162.124 216.223 1.00 136.41 ? 1425 VAL A C     1 
ATOM   846   O  O     . VAL A 1 1425 ? 194.961 161.387 216.778 1.00 138.24 ? 1425 VAL A O     1 
ATOM   847   C  CB    . VAL A 1 1425 ? 197.410 162.610 218.086 1.00 140.12 ? 1425 VAL A CB    1 
ATOM   848   C  CG1   . VAL A 1 1425 ? 198.472 161.732 217.435 1.00 138.73 ? 1425 VAL A CG1   1 
ATOM   849   C  CG2   . VAL A 1 1425 ? 198.051 163.710 218.915 1.00 135.81 ? 1425 VAL A CG2   1 
ATOM   850   N  N     . VAL A 1 1426 ? 196.104 162.020 214.931 1.00 136.97 ? 1426 VAL A N     1 
ATOM   851   C  CA    . VAL A 1 1426 ? 195.385 161.095 214.056 1.00 140.05 ? 1426 VAL A CA    1 
ATOM   852   C  C     . VAL A 1 1426 ? 195.582 159.656 214.519 1.00 140.42 ? 1426 VAL A C     1 
ATOM   853   O  O     . VAL A 1 1426 ? 194.629 158.871 214.587 1.00 139.53 ? 1426 VAL A O     1 
ATOM   854   C  CB    . VAL A 1 1426 ? 195.831 161.283 212.595 1.00 138.45 ? 1426 VAL A CB    1 
ATOM   855   C  CG1   . VAL A 1 1426 ? 195.190 160.230 211.704 1.00 131.65 ? 1426 VAL A CG1   1 
ATOM   856   C  CG2   . VAL A 1 1426 ? 195.484 162.681 212.114 1.00 133.86 ? 1426 VAL A CG2   1 
ATOM   857   N  N     . SER A 1 1427 ? 196.824 159.288 214.841 1.00 139.43 ? 1427 SER A N     1 
ATOM   858   C  CA    . SER A 1 1427 ? 197.087 157.940 215.334 1.00 141.02 ? 1427 SER A CA    1 
ATOM   859   C  C     . SER A 1 1427 ? 196.404 157.701 216.674 1.00 143.61 ? 1427 SER A C     1 
ATOM   860   O  O     . SER A 1 1427 ? 195.859 156.618 216.919 1.00 144.98 ? 1427 SER A O     1 
ATOM   861   C  CB    . SER A 1 1427 ? 198.592 157.706 215.447 1.00 142.61 ? 1427 SER A CB    1 
ATOM   862   O  OG    . SER A 1 1427 ? 199.176 158.587 216.389 1.00 143.16 ? 1427 SER A OG    1 
ATOM   863   N  N     . GLU A 1 1428 ? 196.420 158.700 217.553 1.00 142.61 ? 1428 GLU A N     1 
ATOM   864   C  CA    . GLU A 1 1428 ? 195.787 158.603 218.860 1.00 140.97 ? 1428 GLU A CA    1 
ATOM   865   C  C     . GLU A 1 1428 ? 194.326 159.034 218.843 1.00 142.12 ? 1428 GLU A C     1 
ATOM   866   O  O     . GLU A 1 1428 ? 193.703 159.098 219.908 1.00 139.38 ? 1428 GLU A O     1 
ATOM   867   C  CB    . GLU A 1 1428 ? 196.555 159.444 219.884 1.00 140.76 ? 1428 GLU A CB    1 
ATOM   868   C  CG    . GLU A 1 1428 ? 197.983 158.986 220.121 1.00 147.59 ? 1428 GLU A CG    1 
ATOM   869   C  CD    . GLU A 1 1428 ? 198.724 159.878 221.097 1.00 151.59 ? 1428 GLU A CD    1 
ATOM   870   O  OE1   . GLU A 1 1428 ? 198.120 160.856 221.586 1.00 150.98 ? 1428 GLU A OE1   1 
ATOM   871   O  OE2   . GLU A 1 1428 ? 199.908 159.599 221.380 1.00 150.67 ? 1428 GLU A OE2   1 
ATOM   872   N  N     . LEU A 1 1429 ? 193.773 159.340 217.671 1.00 143.83 ? 1429 LEU A N     1 
ATOM   873   C  CA    . LEU A 1 1429 ? 192.382 159.761 217.585 1.00 142.11 ? 1429 LEU A CA    1 
ATOM   874   C  C     . LEU A 1 1429 ? 191.454 158.643 218.037 1.00 141.63 ? 1429 LEU A C     1 
ATOM   875   O  O     . LEU A 1 1429 ? 191.597 157.490 217.622 1.00 137.80 ? 1429 LEU A O     1 
ATOM   876   C  CB    . LEU A 1 1429 ? 192.048 160.179 216.153 1.00 137.63 ? 1429 LEU A CB    1 
ATOM   877   C  CG    . LEU A 1 1429 ? 190.638 160.715 215.904 1.00 133.09 ? 1429 LEU A CG    1 
ATOM   878   C  CD1   . LEU A 1 1429 ? 190.365 161.930 216.777 1.00 133.98 ? 1429 LEU A CD1   1 
ATOM   879   C  CD2   . LEU A 1 1429 ? 190.453 161.051 214.433 1.00 126.83 ? 1429 LEU A CD2   1 
ATOM   880   N  N     . THR A 1 1430 ? 190.498 158.993 218.891 1.00 143.56 ? 1430 THR A N     1 
ATOM   881   C  CA    . THR A 1 1430 ? 189.502 158.062 219.391 1.00 142.05 ? 1430 THR A CA    1 
ATOM   882   C  C     . THR A 1 1430 ? 188.124 158.693 219.256 1.00 141.89 ? 1430 THR A C     1 
ATOM   883   O  O     . THR A 1 1430 ? 187.985 159.904 219.059 1.00 140.06 ? 1430 THR A O     1 
ATOM   884   C  CB    . THR A 1 1430 ? 189.771 157.673 220.852 1.00 140.01 ? 1430 THR A CB    1 
ATOM   885   O  OG1   . THR A 1 1430 ? 188.876 156.626 221.243 1.00 142.46 ? 1430 THR A OG1   1 
ATOM   886   C  CG2   . THR A 1 1430 ? 189.572 158.871 221.767 1.00 137.74 ? 1430 THR A CG2   1 
ATOM   887   N  N     . LEU A 1 1431 ? 187.096 157.850 219.359 1.00 141.48 ? 1431 LEU A N     1 
ATOM   888   C  CA    . LEU A 1 1431 ? 185.723 158.326 219.252 1.00 137.66 ? 1431 LEU A CA    1 
ATOM   889   C  C     . LEU A 1 1431 ? 185.380 159.336 220.340 1.00 138.31 ? 1431 LEU A C     1 
ATOM   890   O  O     . LEU A 1 1431 ? 184.520 160.198 220.124 1.00 138.91 ? 1431 LEU A O     1 
ATOM   891   C  CB    . LEU A 1 1431 ? 184.765 157.134 219.304 1.00 137.57 ? 1431 LEU A CB    1 
ATOM   892   C  CG    . LEU A 1 1431 ? 183.260 157.394 219.276 1.00 139.51 ? 1431 LEU A CG    1 
ATOM   893   C  CD1   . LEU A 1 1431 ? 182.825 157.834 217.889 1.00 137.15 ? 1431 LEU A CD1   1 
ATOM   894   C  CD2   . LEU A 1 1431 ? 182.512 156.145 219.703 1.00 140.25 ? 1431 LEU A CD2   1 
ATOM   895   N  N     . GLY A 1 1432 ? 186.046 159.258 221.493 1.00 141.28 ? 1432 GLY A N     1 
ATOM   896   C  CA    . GLY A 1 1432 ? 185.750 160.183 222.574 1.00 141.53 ? 1432 GLY A CA    1 
ATOM   897   C  C     . GLY A 1 1432 ? 186.088 161.622 222.236 1.00 138.88 ? 1432 GLY A C     1 
ATOM   898   O  O     . GLY A 1 1432 ? 185.346 162.542 222.590 1.00 140.00 ? 1432 GLY A O     1 
ATOM   899   N  N     . GLN A 1 1433 ? 187.218 161.840 221.560 1.00 136.93 ? 1433 GLN A N     1 
ATOM   900   C  CA    . GLN A 1 1433 ? 187.605 163.200 221.194 1.00 139.34 ? 1433 GLN A CA    1 
ATOM   901   C  C     . GLN A 1 1433 ? 186.603 163.820 220.229 1.00 140.36 ? 1433 GLN A C     1 
ATOM   902   O  O     . GLN A 1 1433 ? 186.249 164.998 220.362 1.00 138.90 ? 1433 GLN A O     1 
ATOM   903   C  CB    . GLN A 1 1433 ? 189.009 163.203 220.587 1.00 140.67 ? 1433 GLN A CB    1 
ATOM   904   C  CG    . GLN A 1 1433 ? 190.083 162.623 221.493 1.00 142.22 ? 1433 GLN A CG    1 
ATOM   905   C  CD    . GLN A 1 1433 ? 190.457 163.557 222.631 1.00 145.03 ? 1433 GLN A CD    1 
ATOM   906   O  OE1   . GLN A 1 1433 ? 189.995 164.696 222.694 1.00 144.00 ? 1433 GLN A OE1   1 
ATOM   907   N  NE2   . GLN A 1 1433 ? 191.298 163.075 223.538 1.00 143.21 ? 1433 GLN A NE2   1 
ATOM   908   N  N     . ILE A 1 1434 ? 186.136 163.046 219.249 1.00 140.77 ? 1434 ILE A N     1 
ATOM   909   C  CA    . ILE A 1 1434 ? 185.152 163.562 218.304 1.00 138.90 ? 1434 ILE A CA    1 
ATOM   910   C  C     . ILE A 1 1434 ? 183.815 163.788 218.996 1.00 140.65 ? 1434 ILE A C     1 
ATOM   911   O  O     . ILE A 1 1434 ? 183.107 164.760 218.706 1.00 140.21 ? 1434 ILE A O     1 
ATOM   912   C  CB    . ILE A 1 1434 ? 185.016 162.611 217.102 1.00 134.94 ? 1434 ILE A CB    1 
ATOM   913   C  CG1   . ILE A 1 1434 ? 186.397 162.263 216.547 1.00 134.41 ? 1434 ILE A CG1   1 
ATOM   914   C  CG2   . ILE A 1 1434 ? 184.148 163.238 216.024 1.00 129.88 ? 1434 ILE A CG2   1 
ATOM   915   C  CD1   . ILE A 1 1434 ? 186.357 161.542 215.225 1.00 126.11 ? 1434 ILE A CD1   1 
ATOM   916   N  N     . TRP A 1 1435 ? 183.443 162.895 219.916 1.00 140.98 ? 1435 TRP A N     1 
ATOM   917   C  CA    . TRP A 1 1435 ? 182.184 163.056 220.635 1.00 139.72 ? 1435 TRP A CA    1 
ATOM   918   C  C     . TRP A 1 1435 ? 182.200 164.294 221.522 1.00 141.63 ? 1435 TRP A C     1 
ATOM   919   O  O     . TRP A 1 1435 ? 181.188 164.995 221.633 1.00 143.67 ? 1435 TRP A O     1 
ATOM   920   C  CB    . TRP A 1 1435 ? 181.890 161.804 221.457 1.00 139.75 ? 1435 TRP A CB    1 
ATOM   921   C  CG    . TRP A 1 1435 ? 181.069 160.798 220.720 1.00 138.49 ? 1435 TRP A CG    1 
ATOM   922   C  CD1   . TRP A 1 1435 ? 180.579 160.913 219.453 1.00 136.03 ? 1435 TRP A CD1   1 
ATOM   923   C  CD2   . TRP A 1 1435 ? 180.647 159.518 221.200 1.00 140.80 ? 1435 TRP A CD2   1 
ATOM   924   N  NE1   . TRP A 1 1435 ? 179.872 159.786 219.115 1.00 136.80 ? 1435 TRP A NE1   1 
ATOM   925   C  CE2   . TRP A 1 1435 ? 179.899 158.913 220.171 1.00 139.74 ? 1435 TRP A CE2   1 
ATOM   926   C  CE3   . TRP A 1 1435 ? 180.827 158.824 222.400 1.00 142.24 ? 1435 TRP A CE3   1 
ATOM   927   C  CZ2   . TRP A 1 1435 ? 179.332 157.651 220.306 1.00 141.85 ? 1435 TRP A CZ2   1 
ATOM   928   C  CZ3   . TRP A 1 1435 ? 180.262 157.571 222.532 1.00 144.90 ? 1435 TRP A CZ3   1 
ATOM   929   C  CH2   . TRP A 1 1435 ? 179.524 156.997 221.491 1.00 143.18 ? 1435 TRP A CH2   1 
ATOM   930   N  N     . ASP A 1 1436 ? 183.335 164.576 222.166 1.00 140.04 ? 1436 ASP A N     1 
ATOM   931   C  CA    . ASP A 1 1436 ? 183.428 165.763 223.011 1.00 140.62 ? 1436 ASP A CA    1 
ATOM   932   C  C     . ASP A 1 1436 ? 183.247 167.035 222.193 1.00 140.09 ? 1436 ASP A C     1 
ATOM   933   O  O     . ASP A 1 1436 ? 182.613 167.992 222.651 1.00 140.22 ? 1436 ASP A O     1 
ATOM   934   C  CB    . ASP A 1 1436 ? 184.765 165.781 223.751 1.00 140.12 ? 1436 ASP A CB    1 
ATOM   935   C  CG    . ASP A 1 1436 ? 184.862 164.695 224.805 1.00 143.02 ? 1436 ASP A CG    1 
ATOM   936   O  OD1   . ASP A 1 1436 ? 183.863 163.974 225.010 1.00 143.51 ? 1436 ASP A OD1   1 
ATOM   937   O  OD2   . ASP A 1 1436 ? 185.935 164.563 225.429 1.00 144.65 ? 1436 ASP A OD2   1 
ATOM   938   N  N     . VAL A 1 1437 ? 183.801 167.067 220.982 1.00 139.77 ? 1437 VAL A N     1 
ATOM   939   C  CA    . VAL A 1 1437 ? 183.537 168.172 220.071 1.00 139.29 ? 1437 VAL A CA    1 
ATOM   940   C  C     . VAL A 1 1437 ? 182.083 168.106 219.625 1.00 139.84 ? 1437 VAL A C     1 
ATOM   941   O  O     . VAL A 1 1437 ? 181.592 167.049 219.209 1.00 140.73 ? 1437 VAL A O     1 
ATOM   942   C  CB    . VAL A 1 1437 ? 184.495 168.123 218.871 1.00 138.37 ? 1437 VAL A CB    1 
ATOM   943   C  CG1   . VAL A 1 1437 ? 184.039 169.084 217.785 1.00 135.21 ? 1437 VAL A CG1   1 
ATOM   944   C  CG2   . VAL A 1 1437 ? 185.913 168.450 219.314 1.00 135.23 ? 1437 VAL A CG2   1 
ATOM   945   N  N     . ASP A 1 1438 ? 181.384 169.235 219.716 1.00 139.56 ? 1438 ASP A N     1 
ATOM   946   C  CA    . ASP A 1 1438 ? 179.961 169.259 219.402 1.00 139.77 ? 1438 ASP A CA    1 
ATOM   947   C  C     . ASP A 1 1438 ? 179.736 169.140 217.901 1.00 134.86 ? 1438 ASP A C     1 
ATOM   948   O  O     . ASP A 1 1438 ? 179.767 170.141 217.178 1.00 130.82 ? 1438 ASP A O     1 
ATOM   949   C  CB    . ASP A 1 1438 ? 179.315 170.537 219.941 1.00 137.51 ? 1438 ASP A CB    1 
ATOM   950   C  CG    . ASP A 1 1438 ? 177.818 170.393 220.145 1.00 136.29 ? 1438 ASP A CG    1 
ATOM   951   O  OD1   . ASP A 1 1438 ? 177.110 170.061 219.171 1.00 137.79 ? 1438 ASP A OD1   1 
ATOM   952   O  OD2   . ASP A 1 1438 ? 177.348 170.614 221.281 1.00 133.28 ? 1438 ASP A OD2   1 
ATOM   953   N  N     . LEU A 1 1439 ? 179.513 167.912 217.425 1.00 133.12 ? 1439 LEU A N     1 
ATOM   954   C  CA    . LEU A 1 1439 ? 179.237 167.704 216.007 1.00 128.87 ? 1439 LEU A CA    1 
ATOM   955   C  C     . LEU A 1 1439 ? 177.922 168.355 215.601 1.00 127.87 ? 1439 LEU A C     1 
ATOM   956   O  O     . LEU A 1 1439 ? 177.799 168.879 214.488 1.00 126.27 ? 1439 LEU A O     1 
ATOM   957   C  CB    . LEU A 1 1439 ? 179.218 166.210 215.688 1.00 127.35 ? 1439 LEU A CB    1 
ATOM   958   C  CG    . LEU A 1 1439 ? 180.512 165.431 215.935 1.00 128.43 ? 1439 LEU A CG    1 
ATOM   959   C  CD1   . LEU A 1 1439 ? 180.459 164.073 215.251 1.00 121.27 ? 1439 LEU A CD1   1 
ATOM   960   C  CD2   . LEU A 1 1439 ? 181.720 166.224 215.462 1.00 125.73 ? 1439 LEU A CD2   1 
ATOM   961   N  N     . GLN A 1 1440 ? 176.925 168.323 216.489 1.00 131.62 ? 1440 GLN A N     1 
ATOM   962   C  CA    . GLN A 1 1440 ? 175.647 168.966 216.200 1.00 133.30 ? 1440 GLN A CA    1 
ATOM   963   C  C     . GLN A 1 1440 ? 175.811 170.472 216.036 1.00 132.43 ? 1440 GLN A C     1 
ATOM   964   O  O     . GLN A 1 1440 ? 175.196 171.080 215.151 1.00 131.09 ? 1440 GLN A O     1 
ATOM   965   C  CB    . GLN A 1 1440 ? 174.643 168.645 217.307 1.00 132.01 ? 1440 GLN A CB    1 
ATOM   966   C  CG    . GLN A 1 1440 ? 173.387 169.498 217.286 1.00 135.43 ? 1440 GLN A CG    1 
ATOM   967   C  CD    . GLN A 1 1440 ? 172.459 169.190 218.445 1.00 143.53 ? 1440 GLN A CD    1 
ATOM   968   O  OE1   . GLN A 1 1440 ? 172.716 168.285 219.238 1.00 146.22 ? 1440 GLN A OE1   1 
ATOM   969   N  NE2   . GLN A 1 1440 ? 171.372 169.946 218.550 1.00 145.10 ? 1440 GLN A NE2   1 
ATOM   970   N  N     . LYS A 1 1441 ? 176.633 171.096 216.882 1.00 130.40 ? 1441 LYS A N     1 
ATOM   971   C  CA    . LYS A 1 1441 ? 176.890 172.525 216.739 1.00 125.99 ? 1441 LYS A CA    1 
ATOM   972   C  C     . LYS A 1 1441 ? 177.732 172.813 215.502 1.00 127.38 ? 1441 LYS A C     1 
ATOM   973   O  O     . LYS A 1 1441 ? 177.564 173.856 214.858 1.00 123.51 ? 1441 LYS A O     1 
ATOM   974   C  CB    . LYS A 1 1441 ? 177.579 173.063 217.992 1.00 124.54 ? 1441 LYS A CB    1 
ATOM   975   C  CG    . LYS A 1 1441 ? 177.674 174.577 218.052 1.00 123.19 ? 1441 LYS A CG    1 
ATOM   976   C  CD    . LYS A 1 1441 ? 177.464 175.087 219.468 1.00 110.81 ? 1441 LYS A CD    1 
ATOM   977   C  CE    . LYS A 1 1441 ? 177.093 176.561 219.473 1.00 102.38 ? 1441 LYS A CE    1 
ATOM   978   N  NZ    . LYS A 1 1441 ? 175.619 176.763 219.466 1.00 94.58  ? 1441 LYS A NZ    1 
ATOM   979   N  N     . ASN A 1 1442 ? 178.641 171.901 215.154 1.00 129.59 ? 1442 ASN A N     1 
ATOM   980   C  CA    . ASN A 1 1442 ? 179.553 172.080 214.031 1.00 124.24 ? 1442 ASN A CA    1 
ATOM   981   C  C     . ASN A 1 1442 ? 179.097 171.328 212.786 1.00 120.55 ? 1442 ASN A C     1 
ATOM   982   O  O     . ASN A 1 1442 ? 179.932 170.840 212.018 1.00 119.67 ? 1442 ASN A O     1 
ATOM   983   C  CB    . ASN A 1 1442 ? 180.964 171.644 214.423 1.00 121.99 ? 1442 ASN A CB    1 
ATOM   984   C  CG    . ASN A 1 1442 ? 181.602 172.573 215.434 1.00 122.34 ? 1442 ASN A CG    1 
ATOM   985   O  OD1   . ASN A 1 1442 ? 181.501 173.794 215.322 1.00 120.88 ? 1442 ASN A OD1   1 
ATOM   986   N  ND2   . ASN A 1 1442 ? 182.265 171.997 216.429 1.00 123.40 ? 1442 ASN A ND2   1 
ATOM   987   N  N     . GLU A 1 1443 ? 177.784 171.220 212.571 1.00 123.71 ? 1443 GLU A N     1 
ATOM   988   C  CA    . GLU A 1 1443 ? 177.288 170.510 211.396 1.00 119.65 ? 1443 GLU A CA    1 
ATOM   989   C  C     . GLU A 1 1443 ? 177.703 171.207 210.108 1.00 116.31 ? 1443 GLU A C     1 
ATOM   990   O  O     . GLU A 1 1443 ? 178.019 170.545 209.115 1.00 114.73 ? 1443 GLU A O     1 
ATOM   991   C  CB    . GLU A 1 1443 ? 175.767 170.368 211.460 1.00 121.03 ? 1443 GLU A CB    1 
ATOM   992   C  CG    . GLU A 1 1443 ? 175.278 169.374 212.496 1.00 125.19 ? 1443 GLU A CG    1 
ATOM   993   C  CD    . GLU A 1 1443 ? 173.866 168.898 212.224 1.00 130.37 ? 1443 GLU A CD    1 
ATOM   994   O  OE1   . GLU A 1 1443 ? 173.203 169.477 211.338 1.00 126.23 ? 1443 GLU A OE1   1 
ATOM   995   O  OE2   . GLU A 1 1443 ? 173.419 167.943 212.893 1.00 133.27 ? 1443 GLU A OE2   1 
ATOM   996   N  N     . ALA A 1 1444 ? 177.700 172.542 210.099 1.00 116.98 ? 1444 ALA A N     1 
ATOM   997   C  CA    . ALA A 1 1444 ? 178.061 173.272 208.887 1.00 117.54 ? 1444 ALA A CA    1 
ATOM   998   C  C     . ALA A 1 1444 ? 179.504 172.992 208.482 1.00 117.41 ? 1444 ALA A C     1 
ATOM   999   O  O     . ALA A 1 1444 ? 179.793 172.730 207.308 1.00 116.83 ? 1444 ALA A O     1 
ATOM   1000  C  CB    . ALA A 1 1444 ? 177.836 174.770 209.093 1.00 112.83 ? 1444 ALA A CB    1 
ATOM   1001  N  N     . ILE A 1 1445 ? 180.422 173.025 209.450 1.00 114.30 ? 1445 ILE A N     1 
ATOM   1002  C  CA    . ILE A 1 1445 ? 181.836 172.790 209.160 1.00 114.21 ? 1445 ILE A CA    1 
ATOM   1003  C  C     . ILE A 1 1445 ? 182.043 171.382 208.618 1.00 110.42 ? 1445 ILE A C     1 
ATOM   1004  O  O     . ILE A 1 1445 ? 182.712 171.179 207.594 1.00 109.96 ? 1445 ILE A O     1 
ATOM   1005  C  CB    . ILE A 1 1445 ? 182.683 173.032 210.421 1.00 120.06 ? 1445 ILE A CB    1 
ATOM   1006  C  CG1   . ILE A 1 1445 ? 182.609 174.501 210.845 1.00 121.80 ? 1445 ILE A CG1   1 
ATOM   1007  C  CG2   . ILE A 1 1445 ? 184.114 172.563 210.208 1.00 120.27 ? 1445 ILE A CG2   1 
ATOM   1008  C  CD1   . ILE A 1 1445 ? 183.200 174.773 212.211 1.00 126.33 ? 1445 ILE A CD1   1 
ATOM   1009  N  N     . VAL A 1 1446 ? 181.473 170.389 209.301 1.00 109.63 ? 1446 VAL A N     1 
ATOM   1010  C  CA    . VAL A 1 1446 ? 181.664 169.000 208.898 1.00 105.32 ? 1446 VAL A CA    1 
ATOM   1011  C  C     . VAL A 1 1446 ? 181.049 168.755 207.528 1.00 104.19 ? 1446 VAL A C     1 
ATOM   1012  O  O     . VAL A 1 1446 ? 181.644 168.085 206.678 1.00 100.23 ? 1446 VAL A O     1 
ATOM   1013  C  CB    . VAL A 1 1446 ? 181.085 168.051 209.963 1.00 108.38 ? 1446 VAL A CB    1 
ATOM   1014  C  CG1   . VAL A 1 1446 ? 181.069 166.623 209.448 1.00 110.48 ? 1446 VAL A CG1   1 
ATOM   1015  C  CG2   . VAL A 1 1446 ? 181.885 168.153 211.252 1.00 106.23 ? 1446 VAL A CG2   1 
ATOM   1016  N  N     . LYS A 1 1447 ? 179.853 169.296 207.287 1.00 105.41 ? 1447 LYS A N     1 
ATOM   1017  C  CA    . LYS A 1 1447 ? 179.208 169.113 205.992 1.00 100.72 ? 1447 LYS A CA    1 
ATOM   1018  C  C     . LYS A 1 1447 ? 180.003 169.774 204.873 1.00 101.92 ? 1447 LYS A C     1 
ATOM   1019  O  O     . LYS A 1 1447 ? 180.115 169.214 203.777 1.00 101.92 ? 1447 LYS A O     1 
ATOM   1020  C  CB    . LYS A 1 1447 ? 177.778 169.652 206.033 1.00 102.70 ? 1447 LYS A CB    1 
ATOM   1021  C  CG    . LYS A 1 1447 ? 176.814 168.779 206.822 1.00 102.61 ? 1447 LYS A CG    1 
ATOM   1022  C  CD    . LYS A 1 1447 ? 175.494 169.489 207.067 1.00 104.02 ? 1447 LYS A CD    1 
ATOM   1023  C  CE    . LYS A 1 1447 ? 174.581 168.657 207.953 1.00 105.43 ? 1447 LYS A CE    1 
ATOM   1024  N  NZ    . LYS A 1 1447 ? 173.326 169.380 208.296 1.00 104.71 ? 1447 LYS A NZ    1 
ATOM   1025  N  N     . ASP A 1 1448 ? 180.562 170.961 205.122 1.00 102.08 ? 1448 ASP A N     1 
ATOM   1026  C  CA    . ASP A 1 1448 ? 181.384 171.615 204.108 1.00 100.42 ? 1448 ASP A CA    1 
ATOM   1027  C  C     . ASP A 1 1448 ? 182.624 170.783 203.795 1.00 100.05 ? 1448 ASP A C     1 
ATOM   1028  O  O     . ASP A 1 1448 ? 182.970 170.569 202.623 1.00 95.44  ? 1448 ASP A O     1 
ATOM   1029  C  CB    . ASP A 1 1448 ? 181.773 173.016 204.586 1.00 101.36 ? 1448 ASP A CB    1 
ATOM   1030  C  CG    . ASP A 1 1448 ? 182.448 173.845 203.507 1.00 108.11 ? 1448 ASP A CG    1 
ATOM   1031  O  OD1   . ASP A 1 1448 ? 182.649 173.337 202.384 1.00 107.32 ? 1448 ASP A OD1   1 
ATOM   1032  O  OD2   . ASP A 1 1448 ? 182.780 175.016 203.787 1.00 109.24 ? 1448 ASP A OD2   1 
ATOM   1033  N  N     . VAL A 1 1449 ? 183.296 170.289 204.839 1.00 99.12  ? 1449 VAL A N     1 
ATOM   1034  C  CA    . VAL A 1 1449 ? 184.492 169.477 204.635 1.00 94.05  ? 1449 VAL A CA    1 
ATOM   1035  C  C     . VAL A 1 1449 ? 184.146 168.202 203.876 1.00 92.46  ? 1449 VAL A C     1 
ATOM   1036  O  O     . VAL A 1 1449 ? 184.894 167.761 202.996 1.00 92.64  ? 1449 VAL A O     1 
ATOM   1037  C  CB    . VAL A 1 1449 ? 185.168 169.175 205.985 1.00 94.21  ? 1449 VAL A CB    1 
ATOM   1038  C  CG1   . VAL A 1 1449 ? 186.259 168.132 205.821 1.00 94.07  ? 1449 VAL A CG1   1 
ATOM   1039  C  CG2   . VAL A 1 1449 ? 185.738 170.452 206.580 1.00 99.57  ? 1449 VAL A CG2   1 
ATOM   1040  N  N     . LEU A 1 1450 ? 182.998 167.601 204.189 1.00 90.56  ? 1450 LEU A N     1 
ATOM   1041  C  CA    . LEU A 1 1450 ? 182.592 166.372 203.518 1.00 86.86  ? 1450 LEU A CA    1 
ATOM   1042  C  C     . LEU A 1 1450 ? 182.195 166.611 202.068 1.00 86.60  ? 1450 LEU A C     1 
ATOM   1043  O  O     . LEU A 1 1450 ? 182.441 165.752 201.217 1.00 89.84  ? 1450 LEU A O     1 
ATOM   1044  C  CB    . LEU A 1 1450 ? 181.450 165.717 204.288 1.00 93.57  ? 1450 LEU A CB    1 
ATOM   1045  C  CG    . LEU A 1 1450 ? 181.861 164.651 205.302 1.00 97.80  ? 1450 LEU A CG    1 
ATOM   1046  C  CD1   . LEU A 1 1450 ? 182.765 165.210 206.379 1.00 99.22  ? 1450 LEU A CD1   1 
ATOM   1047  C  CD2   . LEU A 1 1450 ? 180.617 164.084 205.928 1.00 96.12  ? 1450 LEU A CD2   1 
ATOM   1048  N  N     . LEU A 1 1451 ? 181.577 167.753 201.761 1.00 84.55  ? 1451 LEU A N     1 
ATOM   1049  C  CA    . LEU A 1 1451 ? 181.303 168.079 200.364 1.00 82.85  ? 1451 LEU A CA    1 
ATOM   1050  C  C     . LEU A 1 1451 ? 182.598 168.272 199.585 1.00 85.80  ? 1451 LEU A C     1 
ATOM   1051  O  O     . LEU A 1 1451 ? 182.722 167.811 198.439 1.00 83.23  ? 1451 LEU A O     1 
ATOM   1052  C  CB    . LEU A 1 1451 ? 180.431 169.330 200.276 1.00 80.61  ? 1451 LEU A CB    1 
ATOM   1053  C  CG    . LEU A 1 1451 ? 178.991 169.199 200.774 1.00 83.90  ? 1451 LEU A CG    1 
ATOM   1054  C  CD1   . LEU A 1 1451 ? 178.156 170.377 200.300 1.00 81.79  ? 1451 LEU A CD1   1 
ATOM   1055  C  CD2   . LEU A 1 1451 ? 178.378 167.882 200.324 1.00 82.36  ? 1451 LEU A CD2   1 
ATOM   1056  N  N     . VAL A 1 1452 ? 183.575 168.951 200.195 1.00 87.24  ? 1452 VAL A N     1 
ATOM   1057  C  CA    . VAL A 1 1452 ? 184.887 169.083 199.566 1.00 80.71  ? 1452 VAL A CA    1 
ATOM   1058  C  C     . VAL A 1 1452 ? 185.496 167.709 199.325 1.00 81.46  ? 1452 VAL A C     1 
ATOM   1059  O  O     . VAL A 1 1452 ? 186.049 167.434 198.252 1.00 83.05  ? 1452 VAL A O     1 
ATOM   1060  C  CB    . VAL A 1 1452 ? 185.806 169.967 200.430 1.00 81.10  ? 1452 VAL A CB    1 
ATOM   1061  C  CG1   . VAL A 1 1452 ? 187.231 169.922 199.909 1.00 81.92  ? 1452 VAL A CG1   1 
ATOM   1062  C  CG2   . VAL A 1 1452 ? 185.293 171.395 200.457 1.00 91.42  ? 1452 VAL A CG2   1 
ATOM   1063  N  N     . ALA A 1 1453 ? 185.395 166.823 200.319 1.00 83.20  ? 1453 ALA A N     1 
ATOM   1064  C  CA    . ALA A 1 1453 ? 185.936 165.477 200.182 1.00 79.49  ? 1453 ALA A CA    1 
ATOM   1065  C  C     . ALA A 1 1453 ? 185.247 164.715 199.059 1.00 72.94  ? 1453 ALA A C     1 
ATOM   1066  O  O     . ALA A 1 1453 ? 185.902 164.001 198.296 1.00 79.35  ? 1453 ALA A O     1 
ATOM   1067  C  CB    . ALA A 1 1453 ? 185.801 164.721 201.503 1.00 83.65  ? 1453 ALA A CB    1 
ATOM   1068  N  N     . GLN A 1 1454 ? 183.927 164.858 198.941 1.00 71.20  ? 1454 GLN A N     1 
ATOM   1069  C  CA    . GLN A 1 1454 ? 183.191 164.160 197.891 1.00 73.33  ? 1454 GLN A CA    1 
ATOM   1070  C  C     . GLN A 1 1454 ? 183.626 164.630 196.509 1.00 74.90  ? 1454 GLN A C     1 
ATOM   1071  O  O     . GLN A 1 1454 ? 183.918 163.814 195.624 1.00 79.62  ? 1454 GLN A O     1 
ATOM   1072  C  CB    . GLN A 1 1454 ? 181.689 164.369 198.087 1.00 70.88  ? 1454 GLN A CB    1 
ATOM   1073  C  CG    . GLN A 1 1454 ? 180.815 163.462 197.245 1.00 69.85  ? 1454 GLN A CG    1 
ATOM   1074  C  CD    . GLN A 1 1454 ? 179.382 163.946 197.180 1.00 72.22  ? 1454 GLN A CD    1 
ATOM   1075  O  OE1   . GLN A 1 1454 ? 178.768 164.239 198.204 1.00 78.43  ? 1454 GLN A OE1   1 
ATOM   1076  N  NE2   . GLN A 1 1454 ? 178.842 164.036 195.972 1.00 67.69  ? 1454 GLN A NE2   1 
ATOM   1077  N  N     . GLY A 1 1455 ? 183.696 165.948 196.308 1.00 67.98  ? 1455 GLY A N     1 
ATOM   1078  C  CA    . GLY A 1 1455 ? 184.123 166.456 195.011 1.00 69.93  ? 1455 GLY A CA    1 
ATOM   1079  C  C     . GLY A 1 1455 ? 185.548 166.061 194.665 1.00 75.88  ? 1455 GLY A C     1 
ATOM   1080  O  O     . GLY A 1 1455 ? 185.835 165.625 193.541 1.00 78.75  ? 1455 GLY A O     1 
ATOM   1081  N  N     . GLU A 1 1456 ? 186.459 166.185 195.631 1.00 71.16  ? 1456 GLU A N     1 
ATOM   1082  C  CA    . GLU A 1 1456 ? 187.850 165.859 195.352 1.00 67.34  ? 1456 GLU A CA    1 
ATOM   1083  C  C     . GLU A 1 1456 ? 188.049 164.362 195.162 1.00 70.87  ? 1456 GLU A C     1 
ATOM   1084  O  O     . GLU A 1 1456 ? 188.913 163.955 194.383 1.00 78.50  ? 1456 GLU A O     1 
ATOM   1085  C  CB    . GLU A 1 1456 ? 188.748 166.397 196.462 1.00 68.57  ? 1456 GLU A CB    1 
ATOM   1086  C  CG    . GLU A 1 1456 ? 188.722 167.910 196.557 1.00 73.77  ? 1456 GLU A CG    1 
ATOM   1087  C  CD    . GLU A 1 1456 ? 189.888 168.472 197.336 1.00 83.94  ? 1456 GLU A CD    1 
ATOM   1088  O  OE1   . GLU A 1 1456 ? 190.741 167.682 197.784 1.00 88.16  ? 1456 GLU A OE1   1 
ATOM   1089  O  OE2   . GLU A 1 1456 ? 189.956 169.709 197.492 1.00 86.42  ? 1456 GLU A OE2   1 
ATOM   1090  N  N     . MET A 1 1457 ? 187.255 163.527 195.833 1.00 66.58  ? 1457 MET A N     1 
ATOM   1091  C  CA    . MET A 1 1457 ? 187.353 162.093 195.598 1.00 68.58  ? 1457 MET A CA    1 
ATOM   1092  C  C     . MET A 1 1457 ? 186.790 161.731 194.233 1.00 70.56  ? 1457 MET A C     1 
ATOM   1093  O  O     . MET A 1 1457 ? 187.274 160.797 193.586 1.00 75.91  ? 1457 MET A O     1 
ATOM   1094  C  CB    . MET A 1 1457 ? 186.639 161.319 196.703 1.00 73.77  ? 1457 MET A CB    1 
ATOM   1095  C  CG    . MET A 1 1457 ? 186.779 159.810 196.576 1.00 84.41  ? 1457 MET A CG    1 
ATOM   1096  S  SD    . MET A 1 1457 ? 186.011 158.931 197.946 1.00 104.97 ? 1457 MET A SD    1 
ATOM   1097  C  CE    . MET A 1 1457 ? 186.257 157.227 197.470 1.00 97.03  ? 1457 MET A CE    1 
ATOM   1098  N  N     . ALA A 1 1458 ? 185.770 162.460 193.774 1.00 70.22  ? 1458 ALA A N     1 
ATOM   1099  C  CA    . ALA A 1 1458 ? 185.313 162.287 192.399 1.00 72.60  ? 1458 ALA A CA    1 
ATOM   1100  C  C     . ALA A 1 1458 ? 186.445 162.567 191.418 1.00 69.34  ? 1458 ALA A C     1 
ATOM   1101  O  O     . ALA A 1 1458 ? 186.697 161.782 190.492 1.00 72.78  ? 1458 ALA A O     1 
ATOM   1102  C  CB    . ALA A 1 1458 ? 184.120 163.201 192.125 1.00 69.58  ? 1458 ALA A CB    1 
ATOM   1103  N  N     . LEU A 1 1459 ? 187.158 163.678 191.626 1.00 67.70  ? 1459 LEU A N     1 
ATOM   1104  C  CA    . LEU A 1 1459 ? 188.302 163.992 190.769 1.00 65.77  ? 1459 LEU A CA    1 
ATOM   1105  C  C     . LEU A 1 1459 ? 189.372 162.905 190.849 1.00 68.49  ? 1459 LEU A C     1 
ATOM   1106  O  O     . LEU A 1 1459 ? 189.921 162.474 189.825 1.00 73.49  ? 1459 LEU A O     1 
ATOM   1107  C  CB    . LEU A 1 1459 ? 188.897 165.345 191.154 1.00 65.19  ? 1459 LEU A CB    1 
ATOM   1108  C  CG    . LEU A 1 1459 ? 188.072 166.602 190.896 1.00 65.22  ? 1459 LEU A CG    1 
ATOM   1109  C  CD1   . LEU A 1 1459 ? 188.835 167.818 191.366 1.00 66.67  ? 1459 LEU A CD1   1 
ATOM   1110  C  CD2   . LEU A 1 1459 ? 187.763 166.719 189.432 1.00 61.10  ? 1459 LEU A CD2   1 
ATOM   1111  N  N     . GLU A 1 1460 ? 189.684 162.455 192.066 1.00 67.06  ? 1460 GLU A N     1 
ATOM   1112  C  CA    . GLU A 1 1460 ? 190.747 161.474 192.255 1.00 67.76  ? 1460 GLU A CA    1 
ATOM   1113  C  C     . GLU A 1 1460 ? 190.405 160.150 191.591 1.00 65.74  ? 1460 GLU A C     1 
ATOM   1114  O  O     . GLU A 1 1460 ? 191.267 159.514 190.977 1.00 70.41  ? 1460 GLU A O     1 
ATOM   1115  C  CB    . GLU A 1 1460 ? 191.011 161.269 193.745 1.00 71.53  ? 1460 GLU A CB    1 
ATOM   1116  C  CG    . GLU A 1 1460 ? 192.157 160.322 194.039 1.00 82.23  ? 1460 GLU A CG    1 
ATOM   1117  C  CD    . GLU A 1 1460 ? 192.425 160.181 195.521 1.00 101.58 ? 1460 GLU A CD    1 
ATOM   1118  O  OE1   . GLU A 1 1460 ? 191.699 160.810 196.319 1.00 98.74  ? 1460 GLU A OE1   1 
ATOM   1119  O  OE2   . GLU A 1 1460 ? 193.358 159.436 195.888 1.00 110.65 ? 1460 GLU A OE2   1 
ATOM   1120  N  N     . GLU A 1 1461 ? 189.153 159.714 191.701 1.00 63.89  ? 1461 GLU A N     1 
ATOM   1121  C  CA    . GLU A 1 1461 ? 188.763 158.466 191.064 1.00 65.80  ? 1461 GLU A CA    1 
ATOM   1122  C  C     . GLU A 1 1461 ? 188.662 158.597 189.553 1.00 67.97  ? 1461 GLU A C     1 
ATOM   1123  O  O     . GLU A 1 1461 ? 188.905 157.617 188.843 1.00 75.88  ? 1461 GLU A O     1 
ATOM   1124  C  CB    . GLU A 1 1461 ? 187.456 157.952 191.662 1.00 68.43  ? 1461 GLU A CB    1 
ATOM   1125  C  CG    . GLU A 1 1461 ? 187.677 157.257 192.991 1.00 83.13  ? 1461 GLU A CG    1 
ATOM   1126  C  CD    . GLU A 1 1461 ? 186.395 156.932 193.717 1.00 93.35  ? 1461 GLU A CD    1 
ATOM   1127  O  OE1   . GLU A 1 1461 ? 185.345 157.509 193.373 1.00 89.97  ? 1461 GLU A OE1   1 
ATOM   1128  O  OE2   . GLU A 1 1461 ? 186.438 156.071 194.618 1.00 98.79  ? 1461 GLU A OE2   1 
ATOM   1129  N  N     . PHE A 1 1462 ? 188.346 159.782 189.027 1.00 64.60  ? 1462 PHE A N     1 
ATOM   1130  C  CA    . PHE A 1 1462 ? 188.454 159.930 187.580 1.00 60.43  ? 1462 PHE A CA    1 
ATOM   1131  C  C     . PHE A 1 1462 ? 189.904 159.826 187.122 1.00 61.79  ? 1462 PHE A C     1 
ATOM   1132  O  O     . PHE A 1 1462 ? 190.194 159.204 186.091 1.00 69.02  ? 1462 PHE A O     1 
ATOM   1133  C  CB    . PHE A 1 1462 ? 187.855 161.245 187.103 1.00 61.82  ? 1462 PHE A CB    1 
ATOM   1134  C  CG    . PHE A 1 1462 ? 188.048 161.466 185.638 1.00 61.21  ? 1462 PHE A CG    1 
ATOM   1135  C  CD1   . PHE A 1 1462 ? 187.653 160.497 184.736 1.00 61.78  ? 1462 PHE A CD1   1 
ATOM   1136  C  CD2   . PHE A 1 1462 ? 188.652 162.610 185.163 1.00 57.84  ? 1462 PHE A CD2   1 
ATOM   1137  C  CE1   . PHE A 1 1462 ? 187.840 160.673 183.390 1.00 58.17  ? 1462 PHE A CE1   1 
ATOM   1138  C  CE2   . PHE A 1 1462 ? 188.838 162.792 183.816 1.00 57.40  ? 1462 PHE A CE2   1 
ATOM   1139  C  CZ    . PHE A 1 1462 ? 188.436 161.818 182.931 1.00 57.78  ? 1462 PHE A CZ    1 
ATOM   1140  N  N     . LEU A 1 1463 ? 190.830 160.435 187.866 1.00 62.19  ? 1463 LEU A N     1 
ATOM   1141  C  CA    . LEU A 1 1463 ? 192.243 160.290 187.520 1.00 62.06  ? 1463 LEU A CA    1 
ATOM   1142  C  C     . LEU A 1 1463 ? 192.688 158.837 187.635 1.00 65.21  ? 1463 LEU A C     1 
ATOM   1143  O  O     . LEU A 1 1463 ? 193.509 158.362 186.841 1.00 68.54  ? 1463 LEU A O     1 
ATOM   1144  C  CB    . LEU A 1 1463 ? 193.103 161.191 188.404 1.00 60.16  ? 1463 LEU A CB    1 
ATOM   1145  C  CG    . LEU A 1 1463 ? 193.154 162.663 187.999 1.00 60.52  ? 1463 LEU A CG    1 
ATOM   1146  C  CD1   . LEU A 1 1463 ? 194.324 163.358 188.667 1.00 69.95  ? 1463 LEU A CD1   1 
ATOM   1147  C  CD2   . LEU A 1 1463 ? 193.249 162.795 186.490 1.00 58.46  ? 1463 LEU A CD2   1 
ATOM   1148  N  N     . LYS A 1 1464 ? 192.154 158.116 188.622 1.00 68.01  ? 1464 LYS A N     1 
ATOM   1149  C  CA    . LYS A 1 1464 ? 192.437 156.690 188.749 1.00 62.26  ? 1464 LYS A CA    1 
ATOM   1150  C  C     . LYS A 1 1464 ? 191.934 155.919 187.537 1.00 63.57  ? 1464 LYS A C     1 
ATOM   1151  O  O     . LYS A 1 1464 ? 192.616 155.016 187.038 1.00 72.23  ? 1464 LYS A O     1 
ATOM   1152  C  CB    . LYS A 1 1464 ? 191.802 156.150 190.028 1.00 67.63  ? 1464 LYS A CB    1 
ATOM   1153  C  CG    . LYS A 1 1464 ? 192.319 154.796 190.467 1.00 76.17  ? 1464 LYS A CG    1 
ATOM   1154  C  CD    . LYS A 1 1464 ? 191.766 154.422 191.833 1.00 80.72  ? 1464 LYS A CD    1 
ATOM   1155  C  CE    . LYS A 1 1464 ? 191.866 155.584 192.808 1.00 82.74  ? 1464 LYS A CE    1 
ATOM   1156  N  NZ    . LYS A 1 1464 ? 191.183 155.289 194.097 1.00 86.58  ? 1464 LYS A NZ    1 
ATOM   1157  N  N     . GLN A 1 1465 ? 190.735 156.255 187.056 1.00 62.52  ? 1465 GLN A N     1 
ATOM   1158  C  CA    . GLN A 1 1465 ? 190.215 155.617 185.851 1.00 62.91  ? 1465 GLN A CA    1 
ATOM   1159  C  C     . GLN A 1 1465 ? 191.110 155.897 184.653 1.00 63.89  ? 1465 GLN A C     1 
ATOM   1160  O  O     . GLN A 1 1465 ? 191.386 154.997 183.852 1.00 72.14  ? 1465 GLN A O     1 
ATOM   1161  C  CB    . GLN A 1 1465 ? 188.790 156.093 185.569 1.00 67.37  ? 1465 GLN A CB    1 
ATOM   1162  C  CG    . GLN A 1 1465 ? 187.775 155.713 186.627 1.00 70.49  ? 1465 GLN A CG    1 
ATOM   1163  C  CD    . GLN A 1 1465 ? 186.350 155.835 186.130 1.00 81.58  ? 1465 GLN A CD    1 
ATOM   1164  O  OE1   . GLN A 1 1465 ? 186.113 156.124 184.957 1.00 80.58  ? 1465 GLN A OE1   1 
ATOM   1165  N  NE2   . GLN A 1 1465 ? 185.391 155.618 187.021 1.00 84.20  ? 1465 GLN A NE2   1 
ATOM   1166  N  N     . ILE A 1 1466 ? 191.567 157.144 184.514 1.00 62.77  ? 1466 ILE A N     1 
ATOM   1167  C  CA    . ILE A 1 1466 ? 192.470 157.490 183.416 1.00 62.17  ? 1466 ILE A CA    1 
ATOM   1168  C  C     . ILE A 1 1466 ? 193.740 156.653 183.490 1.00 66.94  ? 1466 ILE A C     1 
ATOM   1169  O  O     . ILE A 1 1466 ? 194.177 156.064 182.493 1.00 71.20  ? 1466 ILE A O     1 
ATOM   1170  C  CB    . ILE A 1 1466 ? 192.799 158.993 183.433 1.00 58.63  ? 1466 ILE A CB    1 
ATOM   1171  C  CG1   . ILE A 1 1466 ? 191.597 159.827 183.001 1.00 61.90  ? 1466 ILE A CG1   1 
ATOM   1172  C  CG2   . ILE A 1 1466 ? 193.984 159.290 182.535 1.00 62.03  ? 1466 ILE A CG2   1 
ATOM   1173  C  CD1   . ILE A 1 1466 ? 191.879 161.308 183.031 1.00 65.11  ? 1466 ILE A CD1   1 
ATOM   1174  N  N     . ARG A 1 1467 ? 194.355 156.594 184.673 1.00 62.96  ? 1467 ARG A N     1 
ATOM   1175  C  CA    . ARG A 1 1467 ? 195.598 155.844 184.821 1.00 57.06  ? 1467 ARG A CA    1 
ATOM   1176  C  C     . ARG A 1 1467 ? 195.389 154.372 184.503 1.00 62.19  ? 1467 ARG A C     1 
ATOM   1177  O  O     . ARG A 1 1467 ? 196.181 153.766 183.774 1.00 74.54  ? 1467 ARG A O     1 
ATOM   1178  C  CB    . ARG A 1 1467 ? 196.159 156.016 186.232 1.00 62.90  ? 1467 ARG A CB    1 
ATOM   1179  C  CG    . ARG A 1 1467 ? 196.669 157.412 186.527 1.00 70.21  ? 1467 ARG A CG    1 
ATOM   1180  C  CD    . ARG A 1 1467 ? 197.399 157.473 187.856 1.00 73.79  ? 1467 ARG A CD    1 
ATOM   1181  N  NE    . ARG A 1 1467 ? 196.517 157.183 188.979 1.00 79.30  ? 1467 ARG A NE    1 
ATOM   1182  C  CZ    . ARG A 1 1467 ? 195.795 158.095 189.616 1.00 79.68  ? 1467 ARG A CZ    1 
ATOM   1183  N  NH1   . ARG A 1 1467 ? 195.817 159.368 189.257 1.00 76.94  ? 1467 ARG A NH1   1 
ATOM   1184  N  NH2   . ARG A 1 1467 ? 195.031 157.721 190.638 1.00 78.93  ? 1467 ARG A NH2   1 
ATOM   1185  N  N     . GLU A 1 1468 ? 194.308 153.784 185.018 1.00 62.71  ? 1468 GLU A N     1 
ATOM   1186  C  CA    . GLU A 1 1468 ? 194.042 152.374 184.755 1.00 65.63  ? 1468 GLU A CA    1 
ATOM   1187  C  C     . GLU A 1 1468 ? 193.871 152.118 183.264 1.00 70.13  ? 1468 GLU A C     1 
ATOM   1188  O  O     . GLU A 1 1468 ? 194.539 151.247 182.692 1.00 76.32  ? 1468 GLU A O     1 
ATOM   1189  C  CB    . GLU A 1 1468 ? 192.802 151.924 185.528 1.00 66.65  ? 1468 GLU A CB    1 
ATOM   1190  C  CG    . GLU A 1 1468 ? 192.559 150.421 185.513 1.00 75.35  ? 1468 GLU A CG    1 
ATOM   1191  C  CD    . GLU A 1 1468 ? 191.763 149.966 184.302 1.00 90.63  ? 1468 GLU A CD    1 
ATOM   1192  O  OE1   . GLU A 1 1468 ? 190.971 150.774 183.772 1.00 88.87  ? 1468 GLU A OE1   1 
ATOM   1193  O  OE2   . GLU A 1 1468 ? 191.924 148.800 183.884 1.00 93.85  ? 1468 GLU A OE2   1 
ATOM   1194  N  N     . VAL A 1 1469 ? 192.993 152.885 182.610 1.00 69.33  ? 1469 VAL A N     1 
ATOM   1195  C  CA    . VAL A 1 1469 ? 192.683 152.614 181.209 1.00 70.68  ? 1469 VAL A CA    1 
ATOM   1196  C  C     . VAL A 1 1469 ? 193.914 152.824 180.337 1.00 67.28  ? 1469 VAL A C     1 
ATOM   1197  O  O     . VAL A 1 1469 ? 194.202 152.017 179.449 1.00 70.15  ? 1469 VAL A O     1 
ATOM   1198  C  CB    . VAL A 1 1469 ? 191.484 153.459 180.734 1.00 67.96  ? 1469 VAL A CB    1 
ATOM   1199  C  CG1   . VAL A 1 1469 ? 191.803 154.931 180.755 1.00 63.34  ? 1469 VAL A CG1   1 
ATOM   1200  C  CG2   . VAL A 1 1469 ? 191.063 153.034 179.337 1.00 68.94  ? 1469 VAL A CG2   1 
ATOM   1201  N  N     . TRP A 1 1470 ? 194.679 153.886 180.587 1.00 61.85  ? 1470 TRP A N     1 
ATOM   1202  C  CA    . TRP A 1 1470 ? 195.832 154.170 179.745 1.00 62.28  ? 1470 TRP A CA    1 
ATOM   1203  C  C     . TRP A 1 1470 ? 197.078 153.400 180.154 1.00 66.63  ? 1470 TRP A C     1 
ATOM   1204  O  O     . TRP A 1 1470 ? 198.097 153.497 179.465 1.00 76.47  ? 1470 TRP A O     1 
ATOM   1205  C  CB    . TRP A 1 1470 ? 196.118 155.674 179.723 1.00 61.74  ? 1470 TRP A CB    1 
ATOM   1206  C  CG    . TRP A 1 1470 ? 195.107 156.421 178.916 1.00 61.62  ? 1470 TRP A CG    1 
ATOM   1207  C  CD1   . TRP A 1 1470 ? 194.312 157.442 179.337 1.00 60.59  ? 1470 TRP A CD1   1 
ATOM   1208  C  CD2   . TRP A 1 1470 ? 194.773 156.192 177.542 1.00 60.59  ? 1470 TRP A CD2   1 
ATOM   1209  N  NE1   . TRP A 1 1470 ? 193.503 157.866 178.311 1.00 57.60  ? 1470 TRP A NE1   1 
ATOM   1210  C  CE2   . TRP A 1 1470 ? 193.769 157.114 177.198 1.00 57.66  ? 1470 TRP A CE2   1 
ATOM   1211  C  CE3   . TRP A 1 1470 ? 195.230 155.298 176.568 1.00 57.97  ? 1470 TRP A CE3   1 
ATOM   1212  C  CZ2   . TRP A 1 1470 ? 193.213 157.167 175.924 1.00 60.35  ? 1470 TRP A CZ2   1 
ATOM   1213  C  CZ3   . TRP A 1 1470 ? 194.676 155.352 175.308 1.00 51.58  ? 1470 TRP A CZ3   1 
ATOM   1214  C  CH2   . TRP A 1 1470 ? 193.679 156.278 174.996 1.00 56.26  ? 1470 TRP A CH2   1 
ATOM   1215  N  N     . ASN A 1 1471 ? 197.026 152.633 181.240 1.00 62.24  ? 1471 ASN A N     1 
ATOM   1216  C  CA    . ASN A 1 1471 ? 198.095 151.693 181.530 1.00 61.64  ? 1471 ASN A CA    1 
ATOM   1217  C  C     . ASN A 1 1471 ? 197.783 150.276 181.073 1.00 69.06  ? 1471 ASN A C     1 
ATOM   1218  O  O     . ASN A 1 1471 ? 198.718 149.496 180.859 1.00 69.96  ? 1471 ASN A O     1 
ATOM   1219  C  CB    . ASN A 1 1471 ? 198.405 151.684 183.031 1.00 63.91  ? 1471 ASN A CB    1 
ATOM   1220  C  CG    . ASN A 1 1471 ? 199.125 152.938 183.482 1.00 70.90  ? 1471 ASN A CG    1 
ATOM   1221  O  OD1   . ASN A 1 1471 ? 199.384 153.838 182.683 1.00 63.65  ? 1471 ASN A OD1   1 
ATOM   1222  N  ND2   . ASN A 1 1471 ? 199.453 153.004 184.767 1.00 75.14  ? 1471 ASN A ND2   1 
ATOM   1223  N  N     . THR A 1 1472 ? 196.508 149.919 180.913 1.00 71.43  ? 1472 THR A N     1 
ATOM   1224  C  CA    . THR A 1 1472 ? 196.152 148.584 180.446 1.00 73.77  ? 1472 THR A CA    1 
ATOM   1225  C  C     . THR A 1 1472 ? 195.660 148.562 179.003 1.00 74.64  ? 1472 THR A C     1 
ATOM   1226  O  O     . THR A 1 1472 ? 195.248 147.502 178.521 1.00 77.67  ? 1472 THR A O     1 
ATOM   1227  C  CB    . THR A 1 1472 ? 195.089 147.958 181.351 1.00 83.18  ? 1472 THR A CB    1 
ATOM   1228  O  OG1   . THR A 1 1472 ? 194.896 146.589 180.977 1.00 89.02  ? 1472 THR A OG1   1 
ATOM   1229  C  CG2   . THR A 1 1472 ? 193.767 148.682 181.189 1.00 76.97  ? 1472 THR A CG2   1 
ATOM   1230  N  N     . TYR A 1 1473 ? 195.691 149.692 178.298 1.00 73.40  ? 1473 TYR A N     1 
ATOM   1231  C  CA    . TYR A 1 1473 ? 195.140 149.758 176.950 1.00 73.77  ? 1473 TYR A CA    1 
ATOM   1232  C  C     . TYR A 1 1473 ? 196.210 149.366 175.942 1.00 71.68  ? 1473 TYR A C     1 
ATOM   1233  O  O     . TYR A 1 1473 ? 197.320 149.907 175.961 1.00 70.40  ? 1473 TYR A O     1 
ATOM   1234  C  CB    . TYR A 1 1473 ? 194.609 151.158 176.639 1.00 69.19  ? 1473 TYR A CB    1 
ATOM   1235  C  CG    . TYR A 1 1473 ? 193.922 151.277 175.300 1.00 67.90  ? 1473 TYR A CG    1 
ATOM   1236  C  CD1   . TYR A 1 1473 ? 192.639 150.783 175.115 1.00 72.33  ? 1473 TYR A CD1   1 
ATOM   1237  C  CD2   . TYR A 1 1473 ? 194.546 151.887 174.227 1.00 67.31  ? 1473 TYR A CD2   1 
ATOM   1238  C  CE1   . TYR A 1 1473 ? 192.001 150.890 173.898 1.00 71.13  ? 1473 TYR A CE1   1 
ATOM   1239  C  CE2   . TYR A 1 1473 ? 193.917 151.997 173.005 1.00 71.18  ? 1473 TYR A CE2   1 
ATOM   1240  C  CZ    . TYR A 1 1473 ? 192.645 151.497 172.846 1.00 70.21  ? 1473 TYR A CZ    1 
ATOM   1241  O  OH    . TYR A 1 1473 ? 192.013 151.605 171.630 1.00 69.83  ? 1473 TYR A OH    1 
ATOM   1242  N  N     . GLU A 1 1474 ? 195.869 148.430 175.062 1.00 71.95  ? 1474 GLU A N     1 
ATOM   1243  C  CA    . GLU A 1 1474 ? 196.788 147.900 174.070 1.00 67.69  ? 1474 GLU A CA    1 
ATOM   1244  C  C     . GLU A 1 1474 ? 196.260 148.183 172.672 1.00 69.67  ? 1474 GLU A C     1 
ATOM   1245  O  O     . GLU A 1 1474 ? 195.051 148.130 172.425 1.00 72.33  ? 1474 GLU A O     1 
ATOM   1246  C  CB    . GLU A 1 1474 ? 196.982 146.391 174.254 1.00 66.99  ? 1474 GLU A CB    1 
ATOM   1247  C  CG    . GLU A 1 1474 ? 198.118 145.800 173.445 1.00 67.01  ? 1474 GLU A CG    1 
ATOM   1248  C  CD    . GLU A 1 1474 ? 198.607 144.483 174.010 1.00 76.03  ? 1474 GLU A CD    1 
ATOM   1249  O  OE1   . GLU A 1 1474 ? 198.067 143.430 173.612 1.00 82.41  ? 1474 GLU A OE1   1 
ATOM   1250  O  OE2   . GLU A 1 1474 ? 199.530 144.498 174.849 1.00 76.67  ? 1474 GLU A OE2   1 
ATOM   1251  N  N     . LEU A 1 1475 ? 197.176 148.491 171.758 1.00 66.93  ? 1475 LEU A N     1 
ATOM   1252  C  CA    . LEU A 1 1475 ? 196.812 148.699 170.364 1.00 62.86  ? 1475 LEU A CA    1 
ATOM   1253  C  C     . LEU A 1 1475 ? 196.408 147.374 169.731 1.00 65.25  ? 1475 LEU A C     1 
ATOM   1254  O  O     . LEU A 1 1475 ? 197.102 146.365 169.886 1.00 69.43  ? 1475 LEU A O     1 
ATOM   1255  C  CB    . LEU A 1 1475 ? 197.974 149.320 169.591 1.00 57.35  ? 1475 LEU A CB    1 
ATOM   1256  C  CG    . LEU A 1 1475 ? 198.313 150.779 169.895 1.00 49.93  ? 1475 LEU A CG    1 
ATOM   1257  C  CD1   . LEU A 1 1475 ? 199.582 151.182 169.174 1.00 45.28  ? 1475 LEU A CD1   1 
ATOM   1258  C  CD2   . LEU A 1 1475 ? 197.164 151.684 169.496 1.00 53.53  ? 1475 LEU A CD2   1 
ATOM   1259  N  N     . ASP A 1 1476 ? 195.286 147.380 169.020 1.00 59.71  ? 1476 ASP A N     1 
ATOM   1260  C  CA    . ASP A 1 1476 ? 194.810 146.185 168.336 1.00 66.78  ? 1476 ASP A CA    1 
ATOM   1261  C  C     . ASP A 1 1476 ? 195.519 146.063 166.994 1.00 68.47  ? 1476 ASP A C     1 
ATOM   1262  O  O     . ASP A 1 1476 ? 195.462 146.983 166.172 1.00 70.26  ? 1476 ASP A O     1 
ATOM   1263  C  CB    . ASP A 1 1476 ? 193.296 146.247 168.151 1.00 73.44  ? 1476 ASP A CB    1 
ATOM   1264  C  CG    . ASP A 1 1476 ? 192.726 144.968 167.573 1.00 83.70  ? 1476 ASP A CG    1 
ATOM   1265  O  OD1   . ASP A 1 1476 ? 192.644 143.965 168.313 1.00 86.39  ? 1476 ASP A OD1   1 
ATOM   1266  O  OD2   . ASP A 1 1476 ? 192.356 144.966 166.380 1.00 80.92  ? 1476 ASP A OD2   1 
ATOM   1267  N  N     . LEU A 1 1477 ? 196.188 144.938 166.770 1.00 69.29  ? 1477 LEU A N     1 
ATOM   1268  C  CA    . LEU A 1 1477 ? 196.948 144.707 165.550 1.00 67.58  ? 1477 LEU A CA    1 
ATOM   1269  C  C     . LEU A 1 1477 ? 196.339 143.549 164.773 1.00 72.72  ? 1477 LEU A C     1 
ATOM   1270  O  O     . LEU A 1 1477 ? 196.025 142.502 165.349 1.00 75.00  ? 1477 LEU A O     1 
ATOM   1271  C  CB    . LEU A 1 1477 ? 198.418 144.421 165.862 1.00 67.92  ? 1477 LEU A CB    1 
ATOM   1272  C  CG    . LEU A 1 1477 ? 199.172 145.500 166.639 1.00 60.50  ? 1477 LEU A CG    1 
ATOM   1273  C  CD1   . LEU A 1 1477 ? 200.663 145.247 166.577 1.00 64.48  ? 1477 LEU A CD1   1 
ATOM   1274  C  CD2   . LEU A 1 1477 ? 198.848 146.874 166.088 1.00 56.42  ? 1477 LEU A CD2   1 
ATOM   1275  N  N     . VAL A 1 1478 ? 196.177 143.745 163.468 1.00 69.88  ? 1478 VAL A N     1 
ATOM   1276  C  CA    . VAL A 1 1478 ? 195.639 142.735 162.567 1.00 70.11  ? 1478 VAL A CA    1 
ATOM   1277  C  C     . VAL A 1 1478 ? 196.606 142.560 161.406 1.00 71.76  ? 1478 VAL A C     1 
ATOM   1278  O  O     . VAL A 1 1478 ? 197.140 143.541 160.877 1.00 71.97  ? 1478 VAL A O     1 
ATOM   1279  C  CB    . VAL A 1 1478 ? 194.232 143.112 162.057 1.00 73.27  ? 1478 VAL A CB    1 
ATOM   1280  C  CG1   . VAL A 1 1478 ? 193.212 142.981 163.175 1.00 76.84  ? 1478 VAL A CG1   1 
ATOM   1281  C  CG2   . VAL A 1 1478 ? 194.227 144.522 161.495 1.00 72.55  ? 1478 VAL A CG2   1 
ATOM   1282  N  N     . ASN A 1 1479 ? 196.848 141.309 161.025 1.00 76.82  ? 1479 ASN A N     1 
ATOM   1283  C  CA    . ASN A 1 1479 ? 197.744 141.030 159.911 1.00 78.37  ? 1479 ASN A CA    1 
ATOM   1284  C  C     . ASN A 1 1479 ? 197.165 141.584 158.616 1.00 78.72  ? 1479 ASN A C     1 
ATOM   1285  O  O     . ASN A 1 1479 ? 195.951 141.560 158.400 1.00 83.08  ? 1479 ASN A O     1 
ATOM   1286  C  CB    . ASN A 1 1479 ? 197.979 139.525 159.788 1.00 79.95  ? 1479 ASN A CB    1 
ATOM   1287  C  CG    . ASN A 1 1479 ? 198.746 139.156 158.537 1.00 83.74  ? 1479 ASN A CG    1 
ATOM   1288  O  OD1   . ASN A 1 1479 ? 199.944 139.415 158.431 1.00 84.46  ? 1479 ASN A OD1   1 
ATOM   1289  N  ND2   . ASN A 1 1479 ? 198.058 138.546 157.580 1.00 86.10  ? 1479 ASN A ND2   1 
ATOM   1290  N  N     . TYR A 1 1480 ? 198.040 142.087 157.750 1.00 73.68  ? 1480 TYR A N     1 
ATOM   1291  C  CA    . TYR A 1 1480 ? 197.641 142.734 156.504 1.00 75.69  ? 1480 TYR A CA    1 
ATOM   1292  C  C     . TYR A 1 1480 ? 198.390 142.064 155.357 1.00 83.64  ? 1480 TYR A C     1 
ATOM   1293  O  O     . TYR A 1 1480 ? 199.521 142.442 155.039 1.00 87.40  ? 1480 TYR A O     1 
ATOM   1294  C  CB    . TYR A 1 1480 ? 197.928 144.232 156.564 1.00 68.74  ? 1480 TYR A CB    1 
ATOM   1295  C  CG    . TYR A 1 1480 ? 197.574 144.978 155.301 1.00 71.80  ? 1480 TYR A CG    1 
ATOM   1296  C  CD1   . TYR A 1 1480 ? 196.250 145.191 154.947 1.00 75.96  ? 1480 TYR A CD1   1 
ATOM   1297  C  CD2   . TYR A 1 1480 ? 198.564 145.467 154.461 1.00 69.41  ? 1480 TYR A CD2   1 
ATOM   1298  C  CE1   . TYR A 1 1480 ? 195.921 145.872 153.794 1.00 74.72  ? 1480 TYR A CE1   1 
ATOM   1299  C  CE2   . TYR A 1 1480 ? 198.245 146.149 153.306 1.00 69.30  ? 1480 TYR A CE2   1 
ATOM   1300  C  CZ    . TYR A 1 1480 ? 196.922 146.348 152.977 1.00 75.10  ? 1480 TYR A CZ    1 
ATOM   1301  O  OH    . TYR A 1 1480 ? 196.597 147.027 151.826 1.00 74.54  ? 1480 TYR A OH    1 
ATOM   1302  N  N     . GLN A 1 1481 ? 197.753 141.064 154.746 1.00 85.10  ? 1481 GLN A N     1 
ATOM   1303  C  CA    . GLN A 1 1481 ? 198.284 140.391 153.559 1.00 82.80  ? 1481 GLN A CA    1 
ATOM   1304  C  C     . GLN A 1 1481 ? 199.654 139.771 153.826 1.00 83.15  ? 1481 GLN A C     1 
ATOM   1305  O  O     . GLN A 1 1481 ? 200.518 139.735 152.948 1.00 85.38  ? 1481 GLN A O     1 
ATOM   1306  C  CB    . GLN A 1 1481 ? 198.345 141.352 152.370 1.00 78.64  ? 1481 GLN A CB    1 
ATOM   1307  C  CG    . GLN A 1 1481 ? 196.996 141.925 151.980 1.00 81.31  ? 1481 GLN A CG    1 
ATOM   1308  C  CD    . GLN A 1 1481 ? 197.111 143.060 150.988 1.00 87.24  ? 1481 GLN A CD    1 
ATOM   1309  O  OE1   . GLN A 1 1481 ? 196.107 143.608 150.536 1.00 93.68  ? 1481 GLN A OE1   1 
ATOM   1310  N  NE2   . GLN A 1 1481 ? 198.341 143.423 150.644 1.00 84.75  ? 1481 GLN A NE2   1 
ATOM   1311  N  N     . ASN A 1 1482 ? 199.850 139.281 155.052 1.00 81.53  ? 1482 ASN A N     1 
ATOM   1312  C  CA    . ASN A 1 1482 ? 201.090 138.615 155.460 1.00 81.71  ? 1482 ASN A CA    1 
ATOM   1313  C  C     . ASN A 1 1482 ? 202.315 139.490 155.211 1.00 83.57  ? 1482 ASN A C     1 
ATOM   1314  O  O     . ASN A 1 1482 ? 203.389 138.991 154.868 1.00 84.02  ? 1482 ASN A O     1 
ATOM   1315  C  CB    . ASN A 1 1482 ? 201.252 137.264 154.759 1.00 84.39  ? 1482 ASN A CB    1 
ATOM   1316  C  CG    . ASN A 1 1482 ? 200.298 136.216 155.290 1.00 88.57  ? 1482 ASN A CG    1 
ATOM   1317  O  OD1   . ASN A 1 1482 ? 199.084 136.312 155.105 1.00 84.29  ? 1482 ASN A OD1   1 
ATOM   1318  N  ND2   . ASN A 1 1482 ? 200.842 135.204 155.954 1.00 91.30  ? 1482 ASN A ND2   1 
ATOM   1319  N  N     . LYS A 1 1483 ? 202.164 140.797 155.381 1.00 81.43  ? 1483 LYS A N     1 
ATOM   1320  C  CA    . LYS A 1 1483 ? 203.247 141.747 155.170 1.00 80.67  ? 1483 LYS A CA    1 
ATOM   1321  C  C     . LYS A 1 1483 ? 203.595 142.535 156.421 1.00 84.03  ? 1483 LYS A C     1 
ATOM   1322  O  O     . LYS A 1 1483 ? 204.778 142.711 156.725 1.00 82.38  ? 1483 LYS A O     1 
ATOM   1323  C  CB    . LYS A 1 1483 ? 202.876 142.713 154.037 1.00 79.13  ? 1483 LYS A CB    1 
ATOM   1324  C  CG    . LYS A 1 1483 ? 203.981 143.667 153.631 1.00 79.68  ? 1483 LYS A CG    1 
ATOM   1325  C  CD    . LYS A 1 1483 ? 203.494 144.619 152.552 1.00 87.25  ? 1483 LYS A CD    1 
ATOM   1326  C  CE    . LYS A 1 1483 ? 203.361 143.908 151.214 1.00 86.75  ? 1483 LYS A CE    1 
ATOM   1327  N  NZ    . LYS A 1 1483 ? 202.997 144.846 150.117 1.00 83.61  ? 1483 LYS A NZ    1 
ATOM   1328  N  N     . CYS A 1 1484 ? 202.593 143.013 157.154 1.00 83.95  ? 1484 CYS A N     1 
ATOM   1329  C  CA    . CYS A 1 1484 ? 202.808 143.720 158.408 1.00 73.93  ? 1484 CYS A CA    1 
ATOM   1330  C  C     . CYS A 1 1484 ? 201.530 143.642 159.226 1.00 74.50  ? 1484 CYS A C     1 
ATOM   1331  O  O     . CYS A 1 1484 ? 200.453 143.351 158.701 1.00 74.35  ? 1484 CYS A O     1 
ATOM   1332  C  CB    . CYS A 1 1484 ? 203.210 145.178 158.173 1.00 68.45  ? 1484 CYS A CB    1 
ATOM   1333  S  SG    . CYS A 1 1484 ? 202.084 146.096 157.104 1.00 77.96  ? 1484 CYS A SG    1 
ATOM   1334  N  N     . ARG A 1 1485 ? 201.658 143.919 160.519 1.00 75.70  ? 1485 ARG A N     1 
ATOM   1335  C  CA    . ARG A 1 1485 ? 200.516 143.934 161.429 1.00 71.93  ? 1485 ARG A CA    1 
ATOM   1336  C  C     . ARG A 1 1485 ? 200.070 145.381 161.590 1.00 64.84  ? 1485 ARG A C     1 
ATOM   1337  O  O     . ARG A 1 1485 ? 200.674 146.149 162.340 1.00 64.97  ? 1485 ARG A O     1 
ATOM   1338  C  CB    . ARG A 1 1485 ? 200.877 143.301 162.767 1.00 72.83  ? 1485 ARG A CB    1 
ATOM   1339  C  CG    . ARG A 1 1485 ? 201.761 142.074 162.649 1.00 78.92  ? 1485 ARG A CG    1 
ATOM   1340  C  CD    . ARG A 1 1485 ? 201.820 141.326 163.965 1.00 83.46  ? 1485 ARG A CD    1 
ATOM   1341  N  NE    . ARG A 1 1485 ? 200.519 141.289 164.619 1.00 85.37  ? 1485 ARG A NE    1 
ATOM   1342  C  CZ    . ARG A 1 1485 ? 200.342 141.160 165.926 1.00 82.85  ? 1485 ARG A CZ    1 
ATOM   1343  N  NH1   . ARG A 1 1485 ? 201.367 141.065 166.756 1.00 79.66  ? 1485 ARG A NH1   1 
ATOM   1344  N  NH2   . ARG A 1 1485 ? 199.105 141.125 166.413 1.00 80.16  ? 1485 ARG A NH2   1 
ATOM   1345  N  N     . LEU A 1 1486 ? 199.001 145.746 160.888 1.00 62.19  ? 1486 LEU A N     1 
ATOM   1346  C  CA    . LEU A 1 1486 ? 198.494 147.106 160.928 1.00 57.16  ? 1486 LEU A CA    1 
ATOM   1347  C  C     . LEU A 1 1486 ? 197.614 147.309 162.160 1.00 63.10  ? 1486 LEU A C     1 
ATOM   1348  O  O     . LEU A 1 1486 ? 197.247 146.364 162.861 1.00 71.18  ? 1486 LEU A O     1 
ATOM   1349  C  CB    . LEU A 1 1486 ? 197.708 147.420 159.659 1.00 53.07  ? 1486 LEU A CB    1 
ATOM   1350  C  CG    . LEU A 1 1486 ? 198.523 147.575 158.377 1.00 55.82  ? 1486 LEU A CG    1 
ATOM   1351  C  CD1   . LEU A 1 1486 ? 197.630 148.057 157.257 1.00 56.11  ? 1486 LEU A CD1   1 
ATOM   1352  C  CD2   . LEU A 1 1486 ? 199.682 148.528 158.586 1.00 54.01  ? 1486 LEU A CD2   1 
ATOM   1353  N  N     . ILE A 1 1487 ? 197.268 148.565 162.414 1.00 56.51  ? 1487 ILE A N     1 
ATOM   1354  C  CA    . ILE A 1 1487 ? 196.488 148.932 163.589 1.00 55.42  ? 1487 ILE A CA    1 
ATOM   1355  C  C     . ILE A 1 1487 ? 195.015 149.013 163.214 1.00 59.86  ? 1487 ILE A C     1 
ATOM   1356  O  O     . ILE A 1 1487 ? 194.634 149.741 162.289 1.00 62.43  ? 1487 ILE A O     1 
ATOM   1357  C  CB    . ILE A 1 1487 ? 196.980 150.262 164.180 1.00 51.68  ? 1487 ILE A CB    1 
ATOM   1358  C  CG1   . ILE A 1 1487 ? 198.487 150.204 164.431 1.00 52.53  ? 1487 ILE A CG1   1 
ATOM   1359  C  CG2   . ILE A 1 1487 ? 196.231 150.583 165.461 1.00 55.09  ? 1487 ILE A CG2   1 
ATOM   1360  C  CD1   . ILE A 1 1487 ? 199.024 151.389 165.192 1.00 55.30  ? 1487 ILE A CD1   1 
ATOM   1361  N  N     . ARG A 1 1488 ? 194.188 148.262 163.933 1.00 63.48  ? 1488 ARG A N     1 
ATOM   1362  C  CA    . ARG A 1 1488 ? 192.742 148.281 163.793 1.00 65.01  ? 1488 ARG A CA    1 
ATOM   1363  C  C     . ARG A 1 1488 ? 192.128 148.857 165.062 1.00 72.91  ? 1488 ARG A C     1 
ATOM   1364  O  O     . ARG A 1 1488 ? 192.728 148.819 166.139 1.00 78.10  ? 1488 ARG A O     1 
ATOM   1365  C  CB    . ARG A 1 1488 ? 192.195 146.871 163.517 1.00 68.91  ? 1488 ARG A CB    1 
ATOM   1366  C  CG    . ARG A 1 1488 ? 190.697 146.806 163.249 1.00 79.85  ? 1488 ARG A CG    1 
ATOM   1367  C  CD    . ARG A 1 1488 ? 190.241 145.392 162.939 1.00 83.74  ? 1488 ARG A CD    1 
ATOM   1368  N  NE    . ARG A 1 1488 ? 190.793 144.922 161.675 1.00 92.57  ? 1488 ARG A NE    1 
ATOM   1369  C  CZ    . ARG A 1 1488 ? 190.254 145.171 160.489 1.00 93.30  ? 1488 ARG A CZ    1 
ATOM   1370  N  NH1   . ARG A 1 1488 ? 189.135 145.867 160.371 1.00 93.88  ? 1488 ARG A NH1   1 
ATOM   1371  N  NH2   . ARG A 1 1488 ? 190.854 144.715 159.394 1.00 90.81  ? 1488 ARG A NH2   1 
ATOM   1372  N  N     . GLY A 1 1489 ? 190.924 149.403 164.927 1.00 71.85  ? 1489 GLY A N     1 
ATOM   1373  C  CA    . GLY A 1 1489 ? 190.265 150.035 166.048 1.00 70.49  ? 1489 GLY A CA    1 
ATOM   1374  C  C     . GLY A 1 1489 ? 190.562 151.506 166.186 1.00 69.12  ? 1489 GLY A C     1 
ATOM   1375  O  O     . GLY A 1 1489 ? 190.633 152.011 167.312 1.00 77.40  ? 1489 GLY A O     1 
ATOM   1376  N  N     . TRP A 1 1490 ? 190.748 152.211 165.070 1.00 67.38  ? 1490 TRP A N     1 
ATOM   1377  C  CA    . TRP A 1 1490 ? 191.059 153.634 165.128 1.00 67.43  ? 1490 TRP A CA    1 
ATOM   1378  C  C     . TRP A 1 1490 ? 189.921 154.425 165.756 1.00 69.81  ? 1490 TRP A C     1 
ATOM   1379  O  O     . TRP A 1 1490 ? 190.158 155.349 166.541 1.00 68.56  ? 1490 TRP A O     1 
ATOM   1380  C  CB    . TRP A 1 1490 ? 191.363 154.155 163.726 1.00 66.51  ? 1490 TRP A CB    1 
ATOM   1381  C  CG    . TRP A 1 1490 ? 192.702 153.743 163.207 1.00 62.73  ? 1490 TRP A CG    1 
ATOM   1382  C  CD1   . TRP A 1 1490 ? 192.953 152.995 162.097 1.00 57.46  ? 1490 TRP A CD1   1 
ATOM   1383  C  CD2   . TRP A 1 1490 ? 193.978 154.081 163.761 1.00 60.49  ? 1490 TRP A CD2   1 
ATOM   1384  N  NE1   . TRP A 1 1490 ? 194.305 152.832 161.932 1.00 58.45  ? 1490 TRP A NE1   1 
ATOM   1385  C  CE2   . TRP A 1 1490 ? 194.957 153.491 162.940 1.00 58.94  ? 1490 TRP A CE2   1 
ATOM   1386  C  CE3   . TRP A 1 1490 ? 194.387 154.820 164.874 1.00 58.24  ? 1490 TRP A CE3   1 
ATOM   1387  C  CZ2   . TRP A 1 1490 ? 196.318 153.617 163.197 1.00 55.32  ? 1490 TRP A CZ2   1 
ATOM   1388  C  CZ3   . TRP A 1 1490 ? 195.738 154.943 165.126 1.00 55.76  ? 1490 TRP A CZ3   1 
ATOM   1389  C  CH2   . TRP A 1 1490 ? 196.688 154.344 164.292 1.00 52.80  ? 1490 TRP A CH2   1 
ATOM   1390  N  N     . ASP A 1 1491 ? 188.677 154.082 165.417 1.00 78.17  ? 1491 ASP A N     1 
ATOM   1391  C  CA    . ASP A 1 1491 ? 187.535 154.827 165.938 1.00 76.15  ? 1491 ASP A CA    1 
ATOM   1392  C  C     . ASP A 1 1491 ? 187.455 154.725 167.456 1.00 75.64  ? 1491 ASP A C     1 
ATOM   1393  O  O     . ASP A 1 1491 ? 187.244 155.729 168.144 1.00 80.10  ? 1491 ASP A O     1 
ATOM   1394  C  CB    . ASP A 1 1491 ? 186.243 154.328 165.290 1.00 81.50  ? 1491 ASP A CB    1 
ATOM   1395  C  CG    . ASP A 1 1491 ? 186.118 152.818 165.324 1.00 87.41  ? 1491 ASP A CG    1 
ATOM   1396  O  OD1   . ASP A 1 1491 ? 186.966 152.136 164.711 1.00 88.21  ? 1491 ASP A OD1   1 
ATOM   1397  O  OD2   . ASP A 1 1491 ? 185.172 152.311 165.962 1.00 86.32  ? 1491 ASP A OD2   1 
ATOM   1398  N  N     . ASP A 1 1492 ? 187.639 153.520 167.999 1.00 71.96  ? 1492 ASP A N     1 
ATOM   1399  C  CA    . ASP A 1 1492 ? 187.559 153.336 169.445 1.00 74.16  ? 1492 ASP A CA    1 
ATOM   1400  C  C     . ASP A 1 1492 ? 188.668 154.100 170.160 1.00 70.39  ? 1492 ASP A C     1 
ATOM   1401  O  O     . ASP A 1 1492 ? 188.424 154.785 171.162 1.00 75.88  ? 1492 ASP A O     1 
ATOM   1402  C  CB    . ASP A 1 1492 ? 187.630 151.847 169.782 1.00 80.30  ? 1492 ASP A CB    1 
ATOM   1403  C  CG    . ASP A 1 1492 ? 186.398 151.087 169.334 1.00 89.77  ? 1492 ASP A CG    1 
ATOM   1404  O  OD1   . ASP A 1 1492 ? 185.308 151.694 169.283 1.00 93.10  ? 1492 ASP A OD1   1 
ATOM   1405  O  OD2   . ASP A 1 1492 ? 186.520 149.882 169.030 1.00 87.02  ? 1492 ASP A OD2   1 
ATOM   1406  N  N     . LEU A 1 1493 ? 189.898 153.993 169.653 1.00 65.11  ? 1493 LEU A N     1 
ATOM   1407  C  CA    . LEU A 1 1493 ? 191.026 154.681 170.272 1.00 62.56  ? 1493 LEU A CA    1 
ATOM   1408  C  C     . LEU A 1 1493 ? 190.842 156.191 170.228 1.00 67.30  ? 1493 LEU A C     1 
ATOM   1409  O  O     . LEU A 1 1493 ? 191.076 156.887 171.223 1.00 72.24  ? 1493 LEU A O     1 
ATOM   1410  C  CB    . LEU A 1 1493 ? 192.324 154.274 169.578 1.00 63.72  ? 1493 LEU A CB    1 
ATOM   1411  C  CG    . LEU A 1 1493 ? 193.537 155.182 169.777 1.00 60.54  ? 1493 LEU A CG    1 
ATOM   1412  C  CD1   . LEU A 1 1493 ? 194.173 154.962 171.134 1.00 59.64  ? 1493 LEU A CD1   1 
ATOM   1413  C  CD2   . LEU A 1 1493 ? 194.544 154.943 168.670 1.00 57.18  ? 1493 LEU A CD2   1 
ATOM   1414  N  N     . PHE A 1 1494 ? 190.421 156.718 169.077 1.00 68.34  ? 1494 PHE A N     1 
ATOM   1415  C  CA    . PHE A 1 1494 ? 190.226 158.157 168.959 1.00 66.66  ? 1494 PHE A CA    1 
ATOM   1416  C  C     . PHE A 1 1494 ? 189.083 158.636 169.842 1.00 68.72  ? 1494 PHE A C     1 
ATOM   1417  O  O     . PHE A 1 1494 ? 189.172 159.710 170.444 1.00 72.95  ? 1494 PHE A O     1 
ATOM   1418  C  CB    . PHE A 1 1494 ? 189.987 158.542 167.501 1.00 68.22  ? 1494 PHE A CB    1 
ATOM   1419  C  CG    . PHE A 1 1494 ? 191.246 158.632 166.690 1.00 64.78  ? 1494 PHE A CG    1 
ATOM   1420  C  CD1   . PHE A 1 1494 ? 192.305 159.407 167.125 1.00 63.51  ? 1494 PHE A CD1   1 
ATOM   1421  C  CD2   . PHE A 1 1494 ? 191.372 157.948 165.495 1.00 63.94  ? 1494 PHE A CD2   1 
ATOM   1422  C  CE1   . PHE A 1 1494 ? 193.465 159.496 166.388 1.00 61.19  ? 1494 PHE A CE1   1 
ATOM   1423  C  CE2   . PHE A 1 1494 ? 192.530 158.032 164.754 1.00 59.99  ? 1494 PHE A CE2   1 
ATOM   1424  C  CZ    . PHE A 1 1494 ? 193.578 158.808 165.201 1.00 59.00  ? 1494 PHE A CZ    1 
ATOM   1425  N  N     . ASN A 1 1495 ? 188.002 157.857 169.937 1.00 65.06  ? 1495 ASN A N     1 
ATOM   1426  C  CA    . ASN A 1 1495 ? 186.912 158.224 170.831 1.00 65.88  ? 1495 ASN A CA    1 
ATOM   1427  C  C     . ASN A 1 1495 ? 187.387 158.276 172.275 1.00 68.70  ? 1495 ASN A C     1 
ATOM   1428  O  O     . ASN A 1 1495 ? 187.063 159.217 173.007 1.00 77.96  ? 1495 ASN A O     1 
ATOM   1429  C  CB    . ASN A 1 1495 ? 185.755 157.238 170.682 1.00 68.88  ? 1495 ASN A CB    1 
ATOM   1430  C  CG    . ASN A 1 1495 ? 184.987 157.434 169.392 1.00 78.82  ? 1495 ASN A CG    1 
ATOM   1431  O  OD1   . ASN A 1 1495 ? 185.257 158.363 168.631 1.00 75.27  ? 1495 ASN A OD1   1 
ATOM   1432  N  ND2   . ASN A 1 1495 ? 184.024 156.556 169.137 1.00 79.23  ? 1495 ASN A ND2   1 
ATOM   1433  N  N     . LYS A 1 1496 ? 188.173 157.282 172.697 1.00 65.98  ? 1496 LYS A N     1 
ATOM   1434  C  CA    . LYS A 1 1496 ? 188.687 157.280 174.063 1.00 61.96  ? 1496 LYS A CA    1 
ATOM   1435  C  C     . LYS A 1 1496 ? 189.592 158.480 174.316 1.00 64.69  ? 1496 LYS A C     1 
ATOM   1436  O  O     . LYS A 1 1496 ? 189.473 159.151 175.350 1.00 69.61  ? 1496 LYS A O     1 
ATOM   1437  C  CB    . LYS A 1 1496 ? 189.437 155.976 174.333 1.00 61.49  ? 1496 LYS A CB    1 
ATOM   1438  C  CG    . LYS A 1 1496 ? 189.851 155.781 175.778 1.00 69.77  ? 1496 LYS A CG    1 
ATOM   1439  C  CD    . LYS A 1 1496 ? 188.640 155.600 176.675 1.00 77.78  ? 1496 LYS A CD    1 
ATOM   1440  C  CE    . LYS A 1 1496 ? 187.959 154.267 176.413 1.00 73.56  ? 1496 LYS A CE    1 
ATOM   1441  N  NZ    . LYS A 1 1496 ? 186.808 154.037 177.328 1.00 63.88  ? 1496 LYS A NZ    1 
ATOM   1442  N  N     . VAL A 1 1497 ? 190.494 158.776 173.376 1.00 64.76  ? 1497 VAL A N     1 
ATOM   1443  C  CA    . VAL A 1 1497 ? 191.428 159.885 173.564 1.00 61.46  ? 1497 VAL A CA    1 
ATOM   1444  C  C     . VAL A 1 1497 ? 190.679 161.210 173.624 1.00 68.07  ? 1497 VAL A C     1 
ATOM   1445  O  O     . VAL A 1 1497 ? 190.948 162.056 174.484 1.00 70.65  ? 1497 VAL A O     1 
ATOM   1446  C  CB    . VAL A 1 1497 ? 192.491 159.894 172.451 1.00 64.52  ? 1497 VAL A CB    1 
ATOM   1447  C  CG1   . VAL A 1 1497 ? 193.364 161.126 172.575 1.00 64.12  ? 1497 VAL A CG1   1 
ATOM   1448  C  CG2   . VAL A 1 1497 ? 193.341 158.648 172.518 1.00 67.49  ? 1497 VAL A CG2   1 
ATOM   1449  N  N     . LYS A 1 1498 ? 189.735 161.417 172.701 1.00 67.86  ? 1498 LYS A N     1 
ATOM   1450  C  CA    . LYS A 1 1498 ? 188.971 162.659 172.686 1.00 66.83  ? 1498 LYS A CA    1 
ATOM   1451  C  C     . LYS A 1 1498 ? 188.135 162.806 173.949 1.00 69.66  ? 1498 LYS A C     1 
ATOM   1452  O  O     . LYS A 1 1498 ? 188.061 163.898 174.527 1.00 74.34  ? 1498 LYS A O     1 
ATOM   1453  C  CB    . LYS A 1 1498 ? 188.088 162.715 171.441 1.00 65.93  ? 1498 LYS A CB    1 
ATOM   1454  C  CG    . LYS A 1 1498 ? 188.861 162.832 170.139 1.00 75.89  ? 1498 LYS A CG    1 
ATOM   1455  C  CD    . LYS A 1 1498 ? 187.968 162.570 168.936 1.00 83.20  ? 1498 LYS A CD    1 
ATOM   1456  C  CE    . LYS A 1 1498 ? 186.920 163.656 168.768 1.00 94.54  ? 1498 LYS A CE    1 
ATOM   1457  N  NZ    . LYS A 1 1498 ? 187.537 164.991 168.533 1.00 97.35  ? 1498 LYS A NZ    1 
ATOM   1458  N  N     . GLU A 1 1499 ? 187.503 161.718 174.397 1.00 66.71  ? 1499 GLU A N     1 
ATOM   1459  C  CA    . GLU A 1 1499 ? 186.720 161.769 175.624 1.00 63.62  ? 1499 GLU A CA    1 
ATOM   1460  C  C     . GLU A 1 1499 ? 187.590 162.145 176.813 1.00 64.88  ? 1499 GLU A C     1 
ATOM   1461  O  O     . GLU A 1 1499 ? 187.203 162.985 177.633 1.00 68.20  ? 1499 GLU A O     1 
ATOM   1462  C  CB    . GLU A 1 1499 ? 186.039 160.421 175.857 1.00 65.47  ? 1499 GLU A CB    1 
ATOM   1463  C  CG    . GLU A 1 1499 ? 185.478 160.232 177.253 1.00 73.38  ? 1499 GLU A CG    1 
ATOM   1464  C  CD    . GLU A 1 1499 ? 185.449 158.776 177.674 1.00 84.90  ? 1499 GLU A CD    1 
ATOM   1465  O  OE1   . GLU A 1 1499 ? 185.474 157.899 176.786 1.00 80.20  ? 1499 GLU A OE1   1 
ATOM   1466  O  OE2   . GLU A 1 1499 ? 185.402 158.508 178.893 1.00 89.74  ? 1499 GLU A OE2   1 
ATOM   1467  N  N     . HIS A 1 1500 ? 188.783 161.557 176.913 1.00 64.14  ? 1500 HIS A N     1 
ATOM   1468  C  CA    . HIS A 1 1500 ? 189.637 161.848 178.060 1.00 59.69  ? 1500 HIS A CA    1 
ATOM   1469  C  C     . HIS A 1 1500 ? 190.204 163.260 177.994 1.00 58.87  ? 1500 HIS A C     1 
ATOM   1470  O  O     . HIS A 1 1500 ? 190.356 163.918 179.028 1.00 63.97  ? 1500 HIS A O     1 
ATOM   1471  C  CB    . HIS A 1 1500 ? 190.752 160.814 178.158 1.00 59.01  ? 1500 HIS A CB    1 
ATOM   1472  C  CG    . HIS A 1 1500 ? 190.309 159.523 178.765 1.00 59.65  ? 1500 HIS A CG    1 
ATOM   1473  N  ND1   . HIS A 1 1500 ? 190.960 158.936 179.827 1.00 63.30  ? 1500 HIS A ND1   1 
ATOM   1474  C  CD2   . HIS A 1 1500 ? 189.272 158.708 178.461 1.00 60.67  ? 1500 HIS A CD2   1 
ATOM   1475  C  CE1   . HIS A 1 1500 ? 190.342 157.816 180.152 1.00 69.54  ? 1500 HIS A CE1   1 
ATOM   1476  N  NE2   . HIS A 1 1500 ? 189.317 157.651 179.336 1.00 66.53  ? 1500 HIS A NE2   1 
ATOM   1477  N  N     . ILE A 1 1501 ? 190.513 163.751 176.791 1.00 57.28  ? 1501 ILE A N     1 
ATOM   1478  C  CA    . ILE A 1 1501 ? 190.989 165.126 176.653 1.00 58.22  ? 1501 ILE A CA    1 
ATOM   1479  C  C     . ILE A 1 1501 ? 189.899 166.107 177.063 1.00 61.80  ? 1501 ILE A C     1 
ATOM   1480  O  O     . ILE A 1 1501 ? 190.146 167.068 177.805 1.00 62.54  ? 1501 ILE A O     1 
ATOM   1481  C  CB    . ILE A 1 1501 ? 191.471 165.387 175.215 1.00 59.09  ? 1501 ILE A CB    1 
ATOM   1482  C  CG1   . ILE A 1 1501 ? 192.774 164.636 174.943 1.00 62.23  ? 1501 ILE A CG1   1 
ATOM   1483  C  CG2   . ILE A 1 1501 ? 191.657 166.875 174.976 1.00 63.04  ? 1501 ILE A CG2   1 
ATOM   1484  C  CD1   . ILE A 1 1501 ? 193.290 164.809 173.538 1.00 62.26  ? 1501 ILE A CD1   1 
ATOM   1485  N  N     . ASN A 1 1502 ? 188.669 165.871 176.595 1.00 60.33  ? 1502 ASN A N     1 
ATOM   1486  C  CA    . ASN A 1 1502 ? 187.555 166.735 176.971 1.00 59.52  ? 1502 ASN A CA    1 
ATOM   1487  C  C     . ASN A 1 1502 ? 187.306 166.685 178.471 1.00 60.19  ? 1502 ASN A C     1 
ATOM   1488  O  O     . ASN A 1 1502 ? 187.025 167.713 179.099 1.00 63.21  ? 1502 ASN A O     1 
ATOM   1489  C  CB    . ASN A 1 1502 ? 186.296 166.329 176.207 1.00 57.32  ? 1502 ASN A CB    1 
ATOM   1490  C  CG    . ASN A 1 1502 ? 186.445 166.491 174.711 1.00 69.47  ? 1502 ASN A CG    1 
ATOM   1491  O  OD1   . ASN A 1 1502 ? 187.459 166.990 174.227 1.00 74.07  ? 1502 ASN A OD1   1 
ATOM   1492  N  ND2   . ASN A 1 1502 ? 185.432 166.064 173.966 1.00 67.70  ? 1502 ASN A ND2   1 
ATOM   1493  N  N     . SER A 1 1503 ? 187.417 165.498 179.068 1.00 57.27  ? 1503 SER A N     1 
ATOM   1494  C  CA    . SER A 1 1503 ? 187.156 165.366 180.494 1.00 52.82  ? 1503 SER A CA    1 
ATOM   1495  C  C     . SER A 1 1503 ? 188.246 166.027 181.330 1.00 52.93  ? 1503 SER A C     1 
ATOM   1496  O  O     . SER A 1 1503 ? 187.957 166.600 182.383 1.00 60.57  ? 1503 SER A O     1 
ATOM   1497  C  CB    . SER A 1 1503 ? 187.007 163.893 180.855 1.00 54.44  ? 1503 SER A CB    1 
ATOM   1498  O  OG    . SER A 1 1503 ? 185.915 163.309 180.168 1.00 65.81  ? 1503 SER A OG    1 
ATOM   1499  N  N     . VAL A 1 1504 ? 189.503 165.969 180.886 1.00 53.63  ? 1504 VAL A N     1 
ATOM   1500  C  CA    . VAL A 1 1504 ? 190.562 166.672 181.606 1.00 54.72  ? 1504 VAL A CA    1 
ATOM   1501  C  C     . VAL A 1 1504 ? 190.389 168.182 181.468 1.00 58.64  ? 1504 VAL A C     1 
ATOM   1502  O  O     . VAL A 1 1504 ? 190.605 168.941 182.426 1.00 63.09  ? 1504 VAL A O     1 
ATOM   1503  C  CB    . VAL A 1 1504 ? 191.945 166.204 181.115 1.00 57.03  ? 1504 VAL A CB    1 
ATOM   1504  C  CG1   . VAL A 1 1504 ? 193.035 167.137 181.614 1.00 58.08  ? 1504 VAL A CG1   1 
ATOM   1505  C  CG2   . VAL A 1 1504 ? 192.215 164.783 181.576 1.00 55.04  ? 1504 VAL A CG2   1 
ATOM   1506  N  N     . SER A 1 1505 ? 189.978 168.644 180.285 1.00 57.68  ? 1505 SER A N     1 
ATOM   1507  C  CA    . SER A 1 1505 ? 189.688 170.064 180.119 1.00 59.40  ? 1505 SER A CA    1 
ATOM   1508  C  C     . SER A 1 1505 ? 188.559 170.503 181.044 1.00 63.44  ? 1505 SER A C     1 
ATOM   1509  O  O     . SER A 1 1505 ? 188.609 171.594 181.624 1.00 64.74  ? 1505 SER A O     1 
ATOM   1510  C  CB    . SER A 1 1505 ? 189.340 170.363 178.662 1.00 53.01  ? 1505 SER A CB    1 
ATOM   1511  O  OG    . SER A 1 1505 ? 188.130 169.730 178.290 1.00 62.33  ? 1505 SER A OG    1 
ATOM   1512  N  N     . ALA A 1 1506 ? 187.529 169.666 181.189 1.00 60.79  ? 1506 ALA A N     1 
ATOM   1513  C  CA    . ALA A 1 1506 ? 186.446 169.972 182.120 1.00 54.89  ? 1506 ALA A CA    1 
ATOM   1514  C  C     . ALA A 1 1506 ? 186.929 169.950 183.566 1.00 57.90  ? 1506 ALA A C     1 
ATOM   1515  O  O     . ALA A 1 1506 ? 186.498 170.775 184.380 1.00 67.97  ? 1506 ALA A O     1 
ATOM   1516  C  CB    . ALA A 1 1506 ? 185.292 168.993 181.920 1.00 51.17  ? 1506 ALA A CB    1 
ATOM   1517  N  N     . MET A 1 1507 ? 187.806 169.001 183.908 1.00 54.40  ? 1507 MET A N     1 
ATOM   1518  C  CA    . MET A 1 1507 ? 188.454 169.007 185.217 1.00 52.76  ? 1507 MET A CA    1 
ATOM   1519  C  C     . MET A 1 1507 ? 189.122 170.341 185.492 1.00 58.34  ? 1507 MET A C     1 
ATOM   1520  O  O     . MET A 1 1507 ? 189.073 170.851 186.617 1.00 63.37  ? 1507 MET A O     1 
ATOM   1521  C  CB    . MET A 1 1507 ? 189.495 167.893 185.307 1.00 55.24  ? 1507 MET A CB    1 
ATOM   1522  C  CG    . MET A 1 1507 ? 190.134 167.782 186.682 1.00 61.42  ? 1507 MET A CG    1 
ATOM   1523  S  SD    . MET A 1 1507 ? 191.373 166.482 186.816 1.00 68.57  ? 1507 MET A SD    1 
ATOM   1524  C  CE    . MET A 1 1507 ? 190.344 165.029 186.785 1.00 64.10  ? 1507 MET A CE    1 
ATOM   1525  N  N     . LYS A 1 1508 ? 189.759 170.919 184.474 1.00 61.97  ? 1508 LYS A N     1 
ATOM   1526  C  CA    . LYS A 1 1508 ? 190.426 172.202 184.662 1.00 66.13  ? 1508 LYS A CA    1 
ATOM   1527  C  C     . LYS A 1 1508 ? 189.451 173.303 185.067 1.00 65.61  ? 1508 LYS A C     1 
ATOM   1528  O  O     . LYS A 1 1508 ? 189.884 174.343 185.574 1.00 65.70  ? 1508 LYS A O     1 
ATOM   1529  C  CB    . LYS A 1 1508 ? 191.175 172.598 183.389 1.00 67.41  ? 1508 LYS A CB    1 
ATOM   1530  C  CG    . LYS A 1 1508 ? 192.558 171.976 183.275 1.00 73.09  ? 1508 LYS A CG    1 
ATOM   1531  C  CD    . LYS A 1 1508 ? 193.001 171.864 181.827 1.00 79.08  ? 1508 LYS A CD    1 
ATOM   1532  C  CE    . LYS A 1 1508 ? 193.368 173.224 181.258 1.00 87.70  ? 1508 LYS A CE    1 
ATOM   1533  N  NZ    . LYS A 1 1508 ? 193.093 173.311 179.798 1.00 87.41  ? 1508 LYS A NZ    1 
ATOM   1534  N  N     . LEU A 1 1509 ? 188.151 173.100 184.857 1.00 65.37  ? 1509 LEU A N     1 
ATOM   1535  C  CA    . LEU A 1 1509 ? 187.126 174.053 185.257 1.00 63.43  ? 1509 LEU A CA    1 
ATOM   1536  C  C     . LEU A 1 1509 ? 186.423 173.669 186.554 1.00 65.27  ? 1509 LEU A C     1 
ATOM   1537  O  O     . LEU A 1 1509 ? 185.504 174.378 186.976 1.00 71.16  ? 1509 LEU A O     1 
ATOM   1538  C  CB    . LEU A 1 1509 ? 186.088 174.204 184.141 1.00 60.56  ? 1509 LEU A CB    1 
ATOM   1539  C  CG    . LEU A 1 1509 ? 186.590 174.827 182.840 1.00 66.21  ? 1509 LEU A CG    1 
ATOM   1540  C  CD1   . LEU A 1 1509 ? 185.504 174.790 181.779 1.00 66.75  ? 1509 LEU A CD1   1 
ATOM   1541  C  CD2   . LEU A 1 1509 ? 187.070 176.249 183.074 1.00 65.56  ? 1509 LEU A CD2   1 
ATOM   1542  N  N     . SER A 1 1510 ? 186.824 172.572 187.190 1.00 64.99  ? 1510 SER A N     1 
ATOM   1543  C  CA    . SER A 1 1510 ? 186.146 172.116 188.392 1.00 60.86  ? 1510 SER A CA    1 
ATOM   1544  C  C     . SER A 1 1510 ? 186.488 173.011 189.583 1.00 68.72  ? 1510 SER A C     1 
ATOM   1545  O  O     . SER A 1 1510 ? 187.613 173.502 189.700 1.00 70.98  ? 1510 SER A O     1 
ATOM   1546  C  CB    . SER A 1 1510 ? 186.532 170.674 188.704 1.00 62.00  ? 1510 SER A CB    1 
ATOM   1547  O  OG    . SER A 1 1510 ? 185.906 170.220 189.889 1.00 64.24  ? 1510 SER A OG    1 
ATOM   1548  N  N     . PRO A 1 1511 ? 185.527 173.240 190.485 1.00 71.44  ? 1511 PRO A N     1 
ATOM   1549  C  CA    . PRO A 1 1511 ? 185.824 174.016 191.700 1.00 73.60  ? 1511 PRO A CA    1 
ATOM   1550  C  C     . PRO A 1 1511 ? 186.775 173.321 192.660 1.00 76.17  ? 1511 PRO A C     1 
ATOM   1551  O  O     . PRO A 1 1511 ? 187.331 173.992 193.539 1.00 77.69  ? 1511 PRO A O     1 
ATOM   1552  C  CB    . PRO A 1 1511 ? 184.442 174.212 192.336 1.00 69.12  ? 1511 PRO A CB    1 
ATOM   1553  C  CG    . PRO A 1 1511 ? 183.626 173.088 191.815 1.00 64.03  ? 1511 PRO A CG    1 
ATOM   1554  C  CD    . PRO A 1 1511 ? 184.111 172.843 190.418 1.00 63.66  ? 1511 PRO A CD    1 
ATOM   1555  N  N     . TYR A 1 1512 ? 186.977 172.010 192.528 1.00 78.95  ? 1512 TYR A N     1 
ATOM   1556  C  CA    . TYR A 1 1512 ? 187.863 171.254 193.405 1.00 79.16  ? 1512 TYR A CA    1 
ATOM   1557  C  C     . TYR A 1 1512 ? 189.209 170.956 192.753 1.00 81.97  ? 1512 TYR A C     1 
ATOM   1558  O  O     . TYR A 1 1512 ? 189.985 170.154 193.281 1.00 84.94  ? 1512 TYR A O     1 
ATOM   1559  C  CB    . TYR A 1 1512 ? 187.187 169.955 193.842 1.00 75.25  ? 1512 TYR A CB    1 
ATOM   1560  C  CG    . TYR A 1 1512 ? 185.763 170.138 194.311 1.00 73.77  ? 1512 TYR A CG    1 
ATOM   1561  C  CD1   . TYR A 1 1512 ? 185.488 170.736 195.532 1.00 76.60  ? 1512 TYR A CD1   1 
ATOM   1562  C  CD2   . TYR A 1 1512 ? 184.694 169.723 193.529 1.00 67.41  ? 1512 TYR A CD2   1 
ATOM   1563  C  CE1   . TYR A 1 1512 ? 184.190 170.909 195.966 1.00 75.24  ? 1512 TYR A CE1   1 
ATOM   1564  C  CE2   . TYR A 1 1512 ? 183.391 169.894 193.954 1.00 66.81  ? 1512 TYR A CE2   1 
ATOM   1565  C  CZ    . TYR A 1 1512 ? 183.146 170.488 195.174 1.00 70.18  ? 1512 TYR A CZ    1 
ATOM   1566  O  OH    . TYR A 1 1512 ? 181.853 170.661 195.606 1.00 60.92  ? 1512 TYR A OH    1 
ATOM   1567  N  N     . TYR A 1 1513 ? 189.504 171.590 191.618 1.00 80.26  ? 1513 TYR A N     1 
ATOM   1568  C  CA    . TYR A 1 1513 ? 190.742 171.334 190.882 1.00 76.40  ? 1513 TYR A CA    1 
ATOM   1569  C  C     . TYR A 1 1513 ? 191.847 172.219 191.469 1.00 82.46  ? 1513 TYR A C     1 
ATOM   1570  O  O     . TYR A 1 1513 ? 192.237 173.256 190.937 1.00 87.18  ? 1513 TYR A O     1 
ATOM   1571  C  CB    . TYR A 1 1513 ? 190.501 171.535 189.385 1.00 71.38  ? 1513 TYR A CB    1 
ATOM   1572  C  CG    . TYR A 1 1513 ? 191.693 171.734 188.459 1.00 76.55  ? 1513 TYR A CG    1 
ATOM   1573  C  CD1   . TYR A 1 1513 ? 192.212 172.998 188.200 1.00 77.32  ? 1513 TYR A CD1   1 
ATOM   1574  C  CD2   . TYR A 1 1513 ? 192.288 170.649 187.831 1.00 74.84  ? 1513 TYR A CD2   1 
ATOM   1575  C  CE1   . TYR A 1 1513 ? 193.286 173.174 187.356 1.00 75.66  ? 1513 TYR A CE1   1 
ATOM   1576  C  CE2   . TYR A 1 1513 ? 193.365 170.816 186.983 1.00 77.46  ? 1513 TYR A CE2   1 
ATOM   1577  C  CZ    . TYR A 1 1513 ? 193.859 172.081 186.749 1.00 80.16  ? 1513 TYR A CZ    1 
ATOM   1578  O  OH    . TYR A 1 1513 ? 194.932 172.256 185.907 1.00 87.29  ? 1513 TYR A OH    1 
ATOM   1579  N  N     . LYS A 1 1514 ? 192.292 171.821 192.660 1.00 79.96  ? 1514 LYS A N     1 
ATOM   1580  C  CA    . LYS A 1 1514 ? 193.423 172.469 193.317 1.00 78.54  ? 1514 LYS A CA    1 
ATOM   1581  C  C     . LYS A 1 1514 ? 194.560 171.492 193.579 1.00 83.78  ? 1514 LYS A C     1 
ATOM   1582  O  O     . LYS A 1 1514 ? 195.694 171.746 193.161 1.00 85.65  ? 1514 LYS A O     1 
ATOM   1583  C  CB    . LYS A 1 1514 ? 192.975 173.134 194.628 1.00 82.86  ? 1514 LYS A CB    1 
ATOM   1584  C  CG    . LYS A 1 1514 ? 192.311 174.500 194.468 1.00 88.03  ? 1514 LYS A CG    1 
ATOM   1585  C  CD    . LYS A 1 1514 ? 190.903 174.406 193.903 1.00 85.85  ? 1514 LYS A CD    1 
ATOM   1586  C  CE    . LYS A 1 1514 ? 190.243 175.773 193.847 1.00 89.46  ? 1514 LYS A CE    1 
ATOM   1587  N  NZ    . LYS A 1 1514 ? 188.908 175.723 193.188 1.00 89.86  ? 1514 LYS A NZ    1 
ATOM   1588  N  N     . VAL A 1 1515 ? 194.290 170.380 194.262 1.00 84.68  ? 1515 VAL A N     1 
ATOM   1589  C  CA    . VAL A 1 1515 ? 195.336 169.404 194.547 1.00 85.38  ? 1515 VAL A CA    1 
ATOM   1590  C  C     . VAL A 1 1515 ? 195.688 168.608 193.300 1.00 84.44  ? 1515 VAL A C     1 
ATOM   1591  O  O     . VAL A 1 1515 ? 196.862 168.321 193.042 1.00 87.10  ? 1515 VAL A O     1 
ATOM   1592  C  CB    . VAL A 1 1515 ? 194.902 168.485 195.702 1.00 88.34  ? 1515 VAL A CB    1 
ATOM   1593  C  CG1   . VAL A 1 1515 ? 196.008 167.496 196.033 1.00 90.44  ? 1515 VAL A CG1   1 
ATOM   1594  C  CG2   . VAL A 1 1515 ? 194.529 169.311 196.923 1.00 87.27  ? 1515 VAL A CG2   1 
ATOM   1595  N  N     . PHE A 1 1516 ? 194.683 168.241 192.507 1.00 81.64  ? 1516 PHE A N     1 
ATOM   1596  C  CA    . PHE A 1 1516 ? 194.877 167.437 191.309 1.00 78.45  ? 1516 PHE A CA    1 
ATOM   1597  C  C     . PHE A 1 1516 ? 195.322 168.256 190.113 1.00 79.46  ? 1516 PHE A C     1 
ATOM   1598  O  O     . PHE A 1 1516 ? 195.204 167.779 188.980 1.00 84.45  ? 1516 PHE A O     1 
ATOM   1599  C  CB    . PHE A 1 1516 ? 193.591 166.680 190.974 1.00 76.11  ? 1516 PHE A CB    1 
ATOM   1600  C  CG    . PHE A 1 1516 ? 192.954 166.029 192.162 1.00 80.66  ? 1516 PHE A CG    1 
ATOM   1601  C  CD1   . PHE A 1 1516 ? 191.900 166.636 192.820 1.00 76.56  ? 1516 PHE A CD1   1 
ATOM   1602  C  CD2   . PHE A 1 1516 ? 193.423 164.816 192.634 1.00 83.42  ? 1516 PHE A CD2   1 
ATOM   1603  C  CE1   . PHE A 1 1516 ? 191.318 166.039 193.917 1.00 75.88  ? 1516 PHE A CE1   1 
ATOM   1604  C  CE2   . PHE A 1 1516 ? 192.847 164.218 193.732 1.00 79.80  ? 1516 PHE A CE2   1 
ATOM   1605  C  CZ    . PHE A 1 1516 ? 191.794 164.830 194.374 1.00 77.70  ? 1516 PHE A CZ    1 
ATOM   1606  N  N     . GLU A 1 1517 ? 195.819 169.473 190.334 1.00 80.19  ? 1517 GLU A N     1 
ATOM   1607  C  CA    . GLU A 1 1517 ? 196.261 170.306 189.222 1.00 77.33  ? 1517 GLU A CA    1 
ATOM   1608  C  C     . GLU A 1 1517 ? 197.413 169.650 188.472 1.00 79.37  ? 1517 GLU A C     1 
ATOM   1609  O  O     . GLU A 1 1517 ? 197.252 169.215 187.323 1.00 81.50  ? 1517 GLU A O     1 
ATOM   1610  C  CB    . GLU A 1 1517 ? 196.668 171.685 189.742 1.00 79.15  ? 1517 GLU A CB    1 
ATOM   1611  C  CG    . GLU A 1 1517 ? 196.556 172.805 188.724 1.00 81.14  ? 1517 GLU A CG    1 
ATOM   1612  C  CD    . GLU A 1 1517 ? 197.833 173.014 187.939 1.00 91.46  ? 1517 GLU A CD    1 
ATOM   1613  O  OE1   . GLU A 1 1517 ? 198.842 172.347 188.250 1.00 91.18  ? 1517 GLU A OE1   1 
ATOM   1614  O  OE2   . GLU A 1 1517 ? 197.829 173.850 187.012 1.00 95.13  ? 1517 GLU A OE2   1 
ATOM   1615  N  N     . GLU A 1 1518 ? 198.568 169.514 189.134 1.00 78.56  ? 1518 GLU A N     1 
ATOM   1616  C  CA    . GLU A 1 1518 ? 199.776 169.042 188.462 1.00 81.27  ? 1518 GLU A CA    1 
ATOM   1617  C  C     . GLU A 1 1518 ? 199.531 167.721 187.748 1.00 79.10  ? 1518 GLU A C     1 
ATOM   1618  O  O     . GLU A 1 1518 ? 199.767 167.607 186.538 1.00 76.41  ? 1518 GLU A O     1 
ATOM   1619  C  CB    . GLU A 1 1518 ? 200.915 168.897 189.472 1.00 82.05  ? 1518 GLU A CB    1 
ATOM   1620  C  CG    . GLU A 1 1518 ? 201.389 170.202 190.085 1.00 87.21  ? 1518 GLU A CG    1 
ATOM   1621  C  CD    . GLU A 1 1518 ? 202.206 171.037 189.118 1.00 91.33  ? 1518 GLU A CD    1 
ATOM   1622  O  OE1   . GLU A 1 1518 ? 201.606 171.723 188.265 1.00 90.16  ? 1518 GLU A OE1   1 
ATOM   1623  O  OE2   . GLU A 1 1518 ? 203.451 171.002 189.209 1.00 87.86  ? 1518 GLU A OE2   1 
ATOM   1624  N  N     . ASP A 1 1519 ? 199.006 166.729 188.473 1.00 74.24  ? 1519 ASP A N     1 
ATOM   1625  C  CA    . ASP A 1 1519 ? 198.713 165.440 187.859 1.00 72.29  ? 1519 ASP A CA    1 
ATOM   1626  C  C     . ASP A 1 1519 ? 197.877 165.615 186.602 1.00 72.94  ? 1519 ASP A C     1 
ATOM   1627  O  O     . ASP A 1 1519 ? 198.266 165.148 185.523 1.00 80.06  ? 1519 ASP A O     1 
ATOM   1628  C  CB    . ASP A 1 1519 ? 197.993 164.535 188.860 1.00 74.92  ? 1519 ASP A CB    1 
ATOM   1629  C  CG    . ASP A 1 1519 ? 198.097 163.067 188.499 1.00 80.22  ? 1519 ASP A CG    1 
ATOM   1630  O  OD1   . ASP A 1 1519 ? 198.660 162.752 187.431 1.00 85.28  ? 1519 ASP A OD1   1 
ATOM   1631  O  OD2   . ASP A 1 1519 ? 197.614 162.226 189.286 1.00 78.59  ? 1519 ASP A OD2   1 
ATOM   1632  N  N     . ALA A 1 1520 ? 196.767 166.355 186.705 1.00 70.23  ? 1520 ALA A N     1 
ATOM   1633  C  CA    . ALA A 1 1520 ? 195.928 166.572 185.534 1.00 66.81  ? 1520 ALA A CA    1 
ATOM   1634  C  C     . ALA A 1 1520 ? 196.744 167.157 184.396 1.00 70.59  ? 1520 ALA A C     1 
ATOM   1635  O  O     . ALA A 1 1520 ? 196.727 166.627 183.276 1.00 71.81  ? 1520 ALA A O     1 
ATOM   1636  C  CB    . ALA A 1 1520 ? 194.754 167.485 185.880 1.00 67.83  ? 1520 ALA A CB    1 
ATOM   1637  N  N     . LEU A 1 1521 ? 197.526 168.203 184.687 1.00 70.91  ? 1521 LEU A N     1 
ATOM   1638  C  CA    . LEU A 1 1521 ? 198.370 168.795 183.657 1.00 67.13  ? 1521 LEU A CA    1 
ATOM   1639  C  C     . LEU A 1 1521 ? 199.217 167.731 182.983 1.00 69.20  ? 1521 LEU A C     1 
ATOM   1640  O  O     . LEU A 1 1521 ? 199.178 167.590 181.753 1.00 71.83  ? 1521 LEU A O     1 
ATOM   1641  C  CB    . LEU A 1 1521 ? 199.256 169.884 184.259 1.00 69.69  ? 1521 LEU A CB    1 
ATOM   1642  C  CG    . LEU A 1 1521 ? 198.581 171.187 184.685 1.00 75.13  ? 1521 LEU A CG    1 
ATOM   1643  C  CD1   . LEU A 1 1521 ? 199.596 172.316 184.721 1.00 76.70  ? 1521 LEU A CD1   1 
ATOM   1644  C  CD2   . LEU A 1 1521 ? 197.424 171.532 183.761 1.00 73.23  ? 1521 LEU A CD2   1 
ATOM   1645  N  N     . SER A 1 1522 ? 199.921 166.918 183.779 1.00 69.13  ? 1522 SER A N     1 
ATOM   1646  C  CA    . SER A 1 1522 ? 200.747 165.870 183.195 1.00 66.25  ? 1522 SER A CA    1 
ATOM   1647  C  C     . SER A 1 1522 ? 199.915 164.983 182.288 1.00 60.93  ? 1522 SER A C     1 
ATOM   1648  O  O     . SER A 1 1522 ? 200.250 164.800 181.110 1.00 65.92  ? 1522 SER A O     1 
ATOM   1649  C  CB    . SER A 1 1522 ? 201.415 165.044 184.294 1.00 67.73  ? 1522 SER A CB    1 
ATOM   1650  O  OG    . SER A 1 1522 ? 200.455 164.318 185.040 1.00 74.30  ? 1522 SER A OG    1 
ATOM   1651  N  N     . TRP A 1 1523 ? 198.774 164.502 182.790 1.00 57.51  ? 1523 TRP A N     1 
ATOM   1652  C  CA    . TRP A 1 1523 ? 197.930 163.656 181.961 1.00 58.71  ? 1523 TRP A CA    1 
ATOM   1653  C  C     . TRP A 1 1523 ? 197.507 164.386 180.703 1.00 62.04  ? 1523 TRP A C     1 
ATOM   1654  O  O     . TRP A 1 1523 ? 197.616 163.826 179.603 1.00 62.81  ? 1523 TRP A O     1 
ATOM   1655  C  CB    . TRP A 1 1523 ? 196.713 163.178 182.748 1.00 62.37  ? 1523 TRP A CB    1 
ATOM   1656  C  CG    . TRP A 1 1523 ? 196.924 161.828 183.344 1.00 65.71  ? 1523 TRP A CG    1 
ATOM   1657  C  CD1   . TRP A 1 1523 ? 196.899 161.502 184.666 1.00 67.95  ? 1523 TRP A CD1   1 
ATOM   1658  C  CD2   . TRP A 1 1523 ? 197.207 160.615 182.636 1.00 64.80  ? 1523 TRP A CD2   1 
ATOM   1659  N  NE1   . TRP A 1 1523 ? 197.146 160.162 184.826 1.00 68.33  ? 1523 TRP A NE1   1 
ATOM   1660  C  CE2   . TRP A 1 1523 ? 197.338 159.595 183.594 1.00 67.86  ? 1523 TRP A CE2   1 
ATOM   1661  C  CE3   . TRP A 1 1523 ? 197.358 160.294 181.283 1.00 66.14  ? 1523 TRP A CE3   1 
ATOM   1662  C  CZ2   . TRP A 1 1523 ? 197.615 158.276 183.244 1.00 71.21  ? 1523 TRP A CZ2   1 
ATOM   1663  C  CZ3   . TRP A 1 1523 ? 197.633 158.986 180.939 1.00 69.55  ? 1523 TRP A CZ3   1 
ATOM   1664  C  CH2   . TRP A 1 1523 ? 197.758 157.992 181.915 1.00 71.10  ? 1523 TRP A CH2   1 
ATOM   1665  N  N     . GLU A 1 1524 ? 197.103 165.653 180.836 1.00 64.63  ? 1524 GLU A N     1 
ATOM   1666  C  CA    . GLU A 1 1524 ? 196.750 166.428 179.656 1.00 61.02  ? 1524 GLU A CA    1 
ATOM   1667  C  C     . GLU A 1 1524 ? 197.863 166.351 178.628 1.00 60.68  ? 1524 GLU A C     1 
ATOM   1668  O  O     . GLU A 1 1524 ? 197.631 165.932 177.485 1.00 63.28  ? 1524 GLU A O     1 
ATOM   1669  C  CB    . GLU A 1 1524 ? 196.473 167.880 180.041 1.00 65.20  ? 1524 GLU A CB    1 
ATOM   1670  C  CG    . GLU A 1 1524 ? 196.052 168.758 178.878 1.00 69.95  ? 1524 GLU A CG    1 
ATOM   1671  C  CD    . GLU A 1 1524 ? 195.835 170.201 179.286 1.00 81.62  ? 1524 GLU A CD    1 
ATOM   1672  O  OE1   . GLU A 1 1524 ? 196.057 170.524 180.471 1.00 86.13  ? 1524 GLU A OE1   1 
ATOM   1673  O  OE2   . GLU A 1 1524 ? 195.441 171.011 178.423 1.00 87.58  ? 1524 GLU A OE2   1 
ATOM   1674  N  N     . ASP A 1 1525 ? 199.098 166.634 179.054 1.00 58.77  ? 1525 ASP A N     1 
ATOM   1675  C  CA    . ASP A 1 1525 ? 200.221 166.569 178.131 1.00 53.83  ? 1525 ASP A CA    1 
ATOM   1676  C  C     . ASP A 1 1525 ? 200.271 165.209 177.456 1.00 55.53  ? 1525 ASP A C     1 
ATOM   1677  O  O     . ASP A 1 1525 ? 200.189 165.114 176.224 1.00 59.35  ? 1525 ASP A O     1 
ATOM   1678  C  CB    . ASP A 1 1525 ? 201.525 166.856 178.874 1.00 59.66  ? 1525 ASP A CB    1 
ATOM   1679  C  CG    . ASP A 1 1525 ? 202.750 166.610 178.018 1.00 68.04  ? 1525 ASP A CG    1 
ATOM   1680  O  OD1   . ASP A 1 1525 ? 203.068 167.471 177.172 1.00 74.35  ? 1525 ASP A OD1   1 
ATOM   1681  O  OD2   . ASP A 1 1525 ? 203.395 165.556 178.193 1.00 62.93  ? 1525 ASP A OD2   1 
ATOM   1682  N  N     . LYS A 1 1526 ? 200.281 164.138 178.258 1.00 55.00  ? 1526 LYS A N     1 
ATOM   1683  C  CA    . LYS A 1 1526 ? 200.330 162.803 177.680 1.00 49.41  ? 1526 LYS A CA    1 
ATOM   1684  C  C     . LYS A 1 1526 ? 199.187 162.611 176.704 1.00 49.74  ? 1526 LYS A C     1 
ATOM   1685  O  O     . LYS A 1 1526 ? 199.408 162.237 175.544 1.00 53.27  ? 1526 LYS A O     1 
ATOM   1686  C  CB    . LYS A 1 1526 ? 200.285 161.738 178.774 1.00 48.14  ? 1526 LYS A CB    1 
ATOM   1687  C  CG    . LYS A 1 1526 ? 201.491 161.731 179.690 1.00 55.81  ? 1526 LYS A CG    1 
ATOM   1688  C  CD    . LYS A 1 1526 ? 201.294 160.762 180.843 1.00 65.15  ? 1526 LYS A CD    1 
ATOM   1689  C  CE    . LYS A 1 1526 ? 202.413 160.880 181.863 1.00 73.12  ? 1526 LYS A CE    1 
ATOM   1690  N  NZ    . LYS A 1 1526 ? 202.143 160.062 183.077 1.00 72.49  ? 1526 LYS A NZ    1 
ATOM   1691  N  N     . LEU A 1 1527 ? 197.968 162.959 177.127 1.00 51.66  ? 1527 LEU A N     1 
ATOM   1692  C  CA    . LEU A 1 1527 ? 196.822 162.772 176.250 1.00 52.25  ? 1527 LEU A CA    1 
ATOM   1693  C  C     . LEU A 1 1527 ? 197.046 163.488 174.932 1.00 51.71  ? 1527 LEU A C     1 
ATOM   1694  O  O     . LEU A 1 1527 ? 196.938 162.873 173.862 1.00 52.85  ? 1527 LEU A O     1 
ATOM   1695  C  CB    . LEU A 1 1527 ? 195.548 163.262 176.935 1.00 52.86  ? 1527 LEU A CB    1 
ATOM   1696  C  CG    . LEU A 1 1527 ? 194.976 162.316 177.990 1.00 52.35  ? 1527 LEU A CG    1 
ATOM   1697  C  CD1   . LEU A 1 1527 ? 193.747 162.920 178.643 1.00 59.50  ? 1527 LEU A CD1   1 
ATOM   1698  C  CD2   . LEU A 1 1527 ? 194.649 160.967 177.377 1.00 50.28  ? 1527 LEU A CD2   1 
ATOM   1699  N  N     . ASN A 1 1528 ? 197.460 164.758 174.994 1.00 53.68  ? 1528 ASN A N     1 
ATOM   1700  C  CA    . ASN A 1 1528 ? 197.704 165.496 173.764 1.00 51.42  ? 1528 ASN A CA    1 
ATOM   1701  C  C     . ASN A 1 1528 ? 198.683 164.742 172.884 1.00 53.02  ? 1528 ASN A C     1 
ATOM   1702  O  O     . ASN A 1 1528 ? 198.373 164.435 171.725 1.00 57.79  ? 1528 ASN A O     1 
ATOM   1703  C  CB    . ASN A 1 1528 ? 198.222 166.898 174.079 1.00 51.39  ? 1528 ASN A CB    1 
ATOM   1704  C  CG    . ASN A 1 1528 ? 197.132 167.818 174.586 1.00 62.30  ? 1528 ASN A CG    1 
ATOM   1705  O  OD1   . ASN A 1 1528 ? 197.286 168.474 175.615 1.00 69.48  ? 1528 ASN A OD1   1 
ATOM   1706  N  ND2   . ASN A 1 1528 ? 196.017 167.866 173.868 1.00 59.93  ? 1528 ASN A ND2   1 
ATOM   1707  N  N     . ARG A 1 1529 ? 199.825 164.343 173.455 1.00 49.12  ? 1529 ARG A N     1 
ATOM   1708  C  CA    . ARG A 1 1529 ? 200.807 163.601 172.677 1.00 44.89  ? 1529 ARG A CA    1 
ATOM   1709  C  C     . ARG A 1 1529 ? 200.162 162.394 172.024 1.00 46.41  ? 1529 ARG A C     1 
ATOM   1710  O  O     . ARG A 1 1529 ? 200.233 162.236 170.797 1.00 53.13  ? 1529 ARG A O     1 
ATOM   1711  C  CB    . ARG A 1 1529 ? 201.977 163.176 173.562 1.00 45.44  ? 1529 ARG A CB    1 
ATOM   1712  C  CG    . ARG A 1 1529 ? 202.917 164.308 173.927 1.00 53.47  ? 1529 ARG A CG    1 
ATOM   1713  C  CD    . ARG A 1 1529 ? 203.587 164.056 175.263 1.00 55.31  ? 1529 ARG A CD    1 
ATOM   1714  N  NE    . ARG A 1 1529 ? 204.005 162.669 175.414 1.00 51.48  ? 1529 ARG A NE    1 
ATOM   1715  C  CZ    . ARG A 1 1529 ? 204.544 162.168 176.516 1.00 56.69  ? 1529 ARG A CZ    1 
ATOM   1716  N  NH1   . ARG A 1 1529 ? 204.747 162.917 177.587 1.00 64.24  ? 1529 ARG A NH1   1 
ATOM   1717  N  NH2   . ARG A 1 1529 ? 204.887 160.884 176.546 1.00 60.70  ? 1529 ARG A NH2   1 
ATOM   1718  N  N     . ILE A 1 1530 ? 199.449 161.585 172.815 1.00 45.02  ? 1530 ILE A N     1 
ATOM   1719  C  CA    . ILE A 1 1530 ? 198.761 160.428 172.258 1.00 44.13  ? 1530 ILE A CA    1 
ATOM   1720  C  C     . ILE A 1 1530 ? 197.935 160.857 171.058 1.00 47.33  ? 1530 ILE A C     1 
ATOM   1721  O  O     . ILE A 1 1530 ? 198.186 160.425 169.924 1.00 52.38  ? 1530 ILE A O     1 
ATOM   1722  C  CB    . ILE A 1 1530 ? 197.892 159.748 173.331 1.00 47.58  ? 1530 ILE A CB    1 
ATOM   1723  C  CG1   . ILE A 1 1530 ? 198.770 159.111 174.407 1.00 45.90  ? 1530 ILE A CG1   1 
ATOM   1724  C  CG2   . ILE A 1 1530 ? 196.992 158.703 172.703 1.00 50.25  ? 1530 ILE A CG2   1 
ATOM   1725  C  CD1   . ILE A 1 1530 ? 197.990 158.479 175.531 1.00 48.35  ? 1530 ILE A CD1   1 
ATOM   1726  N  N     . MET A 1 1531 ? 197.009 161.794 171.280 1.00 50.60  ? 1531 MET A N     1 
ATOM   1727  C  CA    . MET A 1 1531 ? 196.187 162.302 170.191 1.00 49.69  ? 1531 MET A CA    1 
ATOM   1728  C  C     . MET A 1 1531 ? 197.063 162.690 169.014 1.00 50.76  ? 1531 MET A C     1 
ATOM   1729  O  O     . MET A 1 1531 ? 196.947 162.114 167.922 1.00 55.45  ? 1531 MET A O     1 
ATOM   1730  C  CB    . MET A 1 1531 ? 195.367 163.498 170.675 1.00 54.95  ? 1531 MET A CB    1 
ATOM   1731  C  CG    . MET A 1 1531 ? 194.342 164.027 169.688 1.00 59.95  ? 1531 MET A CG    1 
ATOM   1732  S  SD    . MET A 1 1531 ? 193.021 162.843 169.373 1.00 83.55  ? 1531 MET A SD    1 
ATOM   1733  C  CE    . MET A 1 1531 ? 192.445 163.388 167.771 1.00 69.01  ? 1531 MET A CE    1 
ATOM   1734  N  N     . ALA A 1 1532 ? 198.027 163.582 169.259 1.00 49.20  ? 1532 ALA A N     1 
ATOM   1735  C  CA    . ALA A 1 1532 ? 198.875 164.069 168.181 1.00 47.71  ? 1532 ALA A CA    1 
ATOM   1736  C  C     . ALA A 1 1532 ? 199.487 162.906 167.424 1.00 52.89  ? 1532 ALA A C     1 
ATOM   1737  O  O     . ALA A 1 1532 ? 199.340 162.804 166.198 1.00 59.80  ? 1532 ALA A O     1 
ATOM   1738  C  CB    . ALA A 1 1532 ? 199.961 164.988 168.739 1.00 42.21  ? 1532 ALA A CB    1 
ATOM   1739  N  N     . LEU A 1 1533 ? 200.091 161.964 168.154 1.00 51.63  ? 1533 LEU A N     1 
ATOM   1740  C  CA    . LEU A 1 1533 ? 200.752 160.847 167.494 1.00 45.79  ? 1533 LEU A CA    1 
ATOM   1741  C  C     . LEU A 1 1533 ? 199.778 160.120 166.586 1.00 45.70  ? 1533 LEU A C     1 
ATOM   1742  O  O     . LEU A 1 1533 ? 200.013 159.984 165.380 1.00 54.81  ? 1533 LEU A O     1 
ATOM   1743  C  CB    . LEU A 1 1533 ? 201.343 159.895 168.532 1.00 47.49  ? 1533 LEU A CB    1 
ATOM   1744  C  CG    . LEU A 1 1533 ? 202.203 158.751 167.993 1.00 46.51  ? 1533 LEU A CG    1 
ATOM   1745  C  CD1   . LEU A 1 1533 ? 203.592 159.249 167.642 1.00 51.90  ? 1533 LEU A CD1   1 
ATOM   1746  C  CD2   . LEU A 1 1533 ? 202.281 157.625 169.006 1.00 53.32  ? 1533 LEU A CD2   1 
ATOM   1747  N  N     . PHE A 1 1534 ? 198.630 159.732 167.123 1.00 45.31  ? 1534 PHE A N     1 
ATOM   1748  C  CA    . PHE A 1 1534 ? 197.737 158.948 166.294 1.00 47.55  ? 1534 PHE A CA    1 
ATOM   1749  C  C     . PHE A 1 1534 ? 197.123 159.791 165.192 1.00 52.63  ? 1534 PHE A C     1 
ATOM   1750  O  O     . PHE A 1 1534 ? 196.842 159.260 164.112 1.00 57.72  ? 1534 PHE A O     1 
ATOM   1751  C  CB    . PHE A 1 1534 ? 196.684 158.276 167.169 1.00 48.45  ? 1534 PHE A CB    1 
ATOM   1752  C  CG    . PHE A 1 1534 ? 197.254 157.192 168.037 1.00 54.73  ? 1534 PHE A CG    1 
ATOM   1753  C  CD1   . PHE A 1 1534 ? 197.974 156.150 167.476 1.00 53.03  ? 1534 PHE A CD1   1 
ATOM   1754  C  CD2   . PHE A 1 1534 ? 197.109 157.233 169.411 1.00 54.74  ? 1534 PHE A CD2   1 
ATOM   1755  C  CE1   . PHE A 1 1534 ? 198.518 155.160 168.265 1.00 46.21  ? 1534 PHE A CE1   1 
ATOM   1756  C  CE2   . PHE A 1 1534 ? 197.650 156.242 170.207 1.00 55.52  ? 1534 PHE A CE2   1 
ATOM   1757  C  CZ    . PHE A 1 1534 ? 198.356 155.205 169.632 1.00 51.65  ? 1534 PHE A CZ    1 
ATOM   1758  N  N     . ASP A 1 1535 ? 197.003 161.106 165.410 1.00 51.51  ? 1535 ASP A N     1 
ATOM   1759  C  CA    . ASP A 1 1535 ? 196.491 161.977 164.359 1.00 49.70  ? 1535 ASP A CA    1 
ATOM   1760  C  C     . ASP A 1 1535 ? 197.347 161.891 163.107 1.00 56.24  ? 1535 ASP A C     1 
ATOM   1761  O  O     . ASP A 1 1535 ? 196.843 162.066 161.991 1.00 63.29  ? 1535 ASP A O     1 
ATOM   1762  C  CB    . ASP A 1 1535 ? 196.403 163.419 164.853 1.00 56.76  ? 1535 ASP A CB    1 
ATOM   1763  C  CG    . ASP A 1 1535 ? 195.030 163.763 165.378 1.00 71.10  ? 1535 ASP A CG    1 
ATOM   1764  O  OD1   . ASP A 1 1535 ? 194.100 162.965 165.143 1.00 70.80  ? 1535 ASP A OD1   1 
ATOM   1765  O  OD2   . ASP A 1 1535 ? 194.878 164.827 166.014 1.00 73.96  ? 1535 ASP A OD2   1 
ATOM   1766  N  N     . VAL A 1 1536 ? 198.644 161.622 163.261 1.00 49.15  ? 1536 VAL A N     1 
ATOM   1767  C  CA    . VAL A 1 1536 ? 199.447 161.409 162.065 1.00 44.49  ? 1536 VAL A CA    1 
ATOM   1768  C  C     . VAL A 1 1536 ? 199.493 159.926 161.721 1.00 46.79  ? 1536 VAL A C     1 
ATOM   1769  O  O     . VAL A 1 1536 ? 199.463 159.550 160.541 1.00 51.95  ? 1536 VAL A O     1 
ATOM   1770  C  CB    . VAL A 1 1536 ? 200.852 162.027 162.224 1.00 43.58  ? 1536 VAL A CB    1 
ATOM   1771  C  CG1   . VAL A 1 1536 ? 201.648 161.346 163.307 1.00 47.72  ? 1536 VAL A CG1   1 
ATOM   1772  C  CG2   . VAL A 1 1536 ? 201.601 161.974 160.913 1.00 53.15  ? 1536 VAL A CG2   1 
ATOM   1773  N  N     . TRP A 1 1537 ? 199.480 159.060 162.740 1.00 48.54  ? 1537 TRP A N     1 
ATOM   1774  C  CA    . TRP A 1 1537 ? 199.706 157.638 162.500 1.00 45.42  ? 1537 TRP A CA    1 
ATOM   1775  C  C     . TRP A 1 1537 ? 198.691 157.075 161.522 1.00 45.94  ? 1537 TRP A C     1 
ATOM   1776  O  O     . TRP A 1 1537 ? 199.067 156.570 160.455 1.00 49.93  ? 1537 TRP A O     1 
ATOM   1777  C  CB    . TRP A 1 1537 ? 199.653 156.865 163.813 1.00 49.87  ? 1537 TRP A CB    1 
ATOM   1778  C  CG    . TRP A 1 1537 ? 200.359 155.556 163.754 1.00 52.31  ? 1537 TRP A CG    1 
ATOM   1779  C  CD1   . TRP A 1 1537 ? 200.017 154.474 162.999 1.00 52.29  ? 1537 TRP A CD1   1 
ATOM   1780  C  CD2   . TRP A 1 1537 ? 201.534 155.187 164.476 1.00 56.37  ? 1537 TRP A CD2   1 
ATOM   1781  N  NE1   . TRP A 1 1537 ? 200.908 153.452 163.209 1.00 52.68  ? 1537 TRP A NE1   1 
ATOM   1782  C  CE2   . TRP A 1 1537 ? 201.850 153.866 164.113 1.00 51.30  ? 1537 TRP A CE2   1 
ATOM   1783  C  CE3   . TRP A 1 1537 ? 202.352 155.847 165.398 1.00 57.55  ? 1537 TRP A CE3   1 
ATOM   1784  C  CZ2   . TRP A 1 1537 ? 202.946 153.193 164.637 1.00 47.12  ? 1537 TRP A CZ2   1 
ATOM   1785  C  CZ3   . TRP A 1 1537 ? 203.437 155.177 165.916 1.00 55.00  ? 1537 TRP A CZ3   1 
ATOM   1786  C  CH2   . TRP A 1 1537 ? 203.726 153.866 165.535 1.00 48.46  ? 1537 TRP A CH2   1 
ATOM   1787  N  N     . ILE A 1 1538 ? 197.401 157.229 161.828 1.00 50.09  ? 1538 ILE A N     1 
ATOM   1788  C  CA    . ILE A 1 1538 ? 196.368 156.733 160.928 1.00 52.34  ? 1538 ILE A CA    1 
ATOM   1789  C  C     . ILE A 1 1538 ? 196.584 157.295 159.534 1.00 51.67  ? 1538 ILE A C     1 
ATOM   1790  O  O     . ILE A 1 1538 ? 196.599 156.546 158.547 1.00 52.00  ? 1538 ILE A O     1 
ATOM   1791  C  CB    . ILE A 1 1538 ? 194.964 157.060 161.479 1.00 52.08  ? 1538 ILE A CB    1 
ATOM   1792  C  CG1   . ILE A 1 1538 ? 193.882 156.438 160.596 1.00 54.74  ? 1538 ILE A CG1   1 
ATOM   1793  C  CG2   . ILE A 1 1538 ? 194.754 158.561 161.663 1.00 49.50  ? 1538 ILE A CG2   1 
ATOM   1794  C  CD1   . ILE A 1 1538 ? 192.494 156.537 161.180 1.00 62.76  ? 1538 ILE A CD1   1 
ATOM   1795  N  N     . ASP A 1 1539 ? 196.863 158.599 159.443 1.00 51.22  ? 1539 ASP A N     1 
ATOM   1796  C  CA    . ASP A 1 1539 ? 197.087 159.210 158.141 1.00 49.43  ? 1539 ASP A CA    1 
ATOM   1797  C  C     . ASP A 1 1539 ? 198.164 158.453 157.387 1.00 47.33  ? 1539 ASP A C     1 
ATOM   1798  O  O     . ASP A 1 1539 ? 197.908 157.907 156.304 1.00 50.45  ? 1539 ASP A O     1 
ATOM   1799  C  CB    . ASP A 1 1539 ? 197.472 160.678 158.317 1.00 49.36  ? 1539 ASP A CB    1 
ATOM   1800  C  CG    . ASP A 1 1539 ? 197.795 161.356 157.006 1.00 60.97  ? 1539 ASP A CG    1 
ATOM   1801  O  OD1   . ASP A 1 1539 ? 196.914 161.398 156.123 1.00 66.14  ? 1539 ASP A OD1   1 
ATOM   1802  O  OD2   . ASP A 1 1539 ? 198.932 161.852 156.861 1.00 62.35  ? 1539 ASP A OD2   1 
ATOM   1803  N  N     . VAL A 1 1540 ? 199.332 158.285 158.016 1.00 46.16  ? 1540 VAL A N     1 
ATOM   1804  C  CA    . VAL A 1 1540 ? 200.418 157.573 157.356 1.00 38.30  ? 1540 VAL A CA    1 
ATOM   1805  C  C     . VAL A 1 1540 ? 199.934 156.203 156.928 1.00 39.75  ? 1540 VAL A C     1 
ATOM   1806  O  O     . VAL A 1 1540 ? 199.994 155.849 155.741 1.00 47.67  ? 1540 VAL A O     1 
ATOM   1807  C  CB    . VAL A 1 1540 ? 201.641 157.469 158.285 1.00 35.19  ? 1540 VAL A CB    1 
ATOM   1808  C  CG1   . VAL A 1 1540 ? 202.703 156.585 157.663 1.00 35.02  ? 1540 VAL A CG1   1 
ATOM   1809  C  CG2   . VAL A 1 1540 ? 202.194 158.840 158.590 1.00 39.31  ? 1540 VAL A CG2   1 
ATOM   1810  N  N     . GLN A 1 1541 ? 199.327 155.468 157.864 1.00 38.98  ? 1541 GLN A N     1 
ATOM   1811  C  CA    . GLN A 1 1541 ? 198.867 154.126 157.550 1.00 39.36  ? 1541 GLN A CA    1 
ATOM   1812  C  C     . GLN A 1 1541 ? 197.986 154.147 156.318 1.00 44.30  ? 1541 GLN A C     1 
ATOM   1813  O  O     . GLN A 1 1541 ? 198.282 153.463 155.328 1.00 48.08  ? 1541 GLN A O     1 
ATOM   1814  C  CB    . GLN A 1 1541 ? 198.121 153.533 158.742 1.00 43.34  ? 1541 GLN A CB    1 
ATOM   1815  C  CG    . GLN A 1 1541 ? 197.695 152.096 158.548 1.00 47.66  ? 1541 GLN A CG    1 
ATOM   1816  C  CD    . GLN A 1 1541 ? 197.146 151.485 159.814 1.00 49.76  ? 1541 GLN A CD    1 
ATOM   1817  O  OE1   . GLN A 1 1541 ? 197.850 151.371 160.815 1.00 55.77  ? 1541 GLN A OE1   1 
ATOM   1818  N  NE2   . GLN A 1 1541 ? 195.880 151.090 159.780 1.00 48.49  ? 1541 GLN A NE2   1 
ATOM   1819  N  N     . ARG A 1 1542 ? 196.971 155.018 156.314 1.00 46.96  ? 1542 ARG A N     1 
ATOM   1820  C  CA    . ARG A 1 1542 ? 196.053 155.050 155.186 1.00 46.80  ? 1542 ARG A CA    1 
ATOM   1821  C  C     . ARG A 1 1542 ? 196.824 155.242 153.894 1.00 44.52  ? 1542 ARG A C     1 
ATOM   1822  O  O     . ARG A 1 1542 ? 196.758 154.401 152.986 1.00 44.78  ? 1542 ARG A O     1 
ATOM   1823  C  CB    . ARG A 1 1542 ? 195.016 156.157 155.375 1.00 48.95  ? 1542 ARG A CB    1 
ATOM   1824  C  CG    . ARG A 1 1542 ? 193.981 155.855 156.444 1.00 57.98  ? 1542 ARG A CG    1 
ATOM   1825  C  CD    . ARG A 1 1542 ? 192.805 156.813 156.362 1.00 64.09  ? 1542 ARG A CD    1 
ATOM   1826  N  NE    . ARG A 1 1542 ? 193.227 158.209 156.390 1.00 66.94  ? 1542 ARG A NE    1 
ATOM   1827  C  CZ    . ARG A 1 1542 ? 192.831 159.091 157.297 1.00 63.49  ? 1542 ARG A CZ    1 
ATOM   1828  N  NH1   . ARG A 1 1542 ? 192.002 158.756 158.271 1.00 58.06  ? 1542 ARG A NH1   1 
ATOM   1829  N  NH2   . ARG A 1 1542 ? 193.278 160.342 157.224 1.00 57.00  ? 1542 ARG A NH2   1 
ATOM   1830  N  N     . ARG A 1 1543 ? 197.663 156.280 153.848 1.00 41.54  ? 1543 ARG A N     1 
ATOM   1831  C  CA    . ARG A 1 1543 ? 198.400 156.550 152.625 1.00 37.94  ? 1543 ARG A CA    1 
ATOM   1832  C  C     . ARG A 1 1543 ? 199.224 155.340 152.234 1.00 39.83  ? 1543 ARG A C     1 
ATOM   1833  O  O     . ARG A 1 1543 ? 199.106 154.841 151.107 1.00 51.45  ? 1543 ARG A O     1 
ATOM   1834  C  CB    . ARG A 1 1543 ? 199.273 157.790 152.801 1.00 38.96  ? 1543 ARG A CB    1 
ATOM   1835  C  CG    . ARG A 1 1543 ? 198.454 159.043 153.044 1.00 47.06  ? 1543 ARG A CG    1 
ATOM   1836  C  CD    . ARG A 1 1543 ? 199.309 160.247 153.371 1.00 50.11  ? 1543 ARG A CD    1 
ATOM   1837  N  NE    . ARG A 1 1543 ? 198.508 161.465 153.397 1.00 58.85  ? 1543 ARG A NE    1 
ATOM   1838  C  CZ    . ARG A 1 1543 ? 198.976 162.666 153.703 1.00 64.94  ? 1543 ARG A CZ    1 
ATOM   1839  N  NH1   . ARG A 1 1543 ? 200.245 162.851 154.030 1.00 61.04  ? 1543 ARG A NH1   1 
ATOM   1840  N  NH2   . ARG A 1 1543 ? 198.150 163.708 153.686 1.00 63.90  ? 1543 ARG A NH2   1 
ATOM   1841  N  N     . TRP A 1 1544 ? 199.966 154.779 153.194 1.00 39.68  ? 1544 TRP A N     1 
ATOM   1842  C  CA    . TRP A 1 1544 ? 200.806 153.635 152.875 1.00 39.94  ? 1544 TRP A CA    1 
ATOM   1843  C  C     . TRP A 1 1544 ? 199.972 152.526 152.263 1.00 45.42  ? 1544 TRP A C     1 
ATOM   1844  O  O     . TRP A 1 1544 ? 200.296 152.026 151.178 1.00 53.20  ? 1544 TRP A O     1 
ATOM   1845  C  CB    . TRP A 1 1544 ? 201.536 153.142 154.123 1.00 38.76  ? 1544 TRP A CB    1 
ATOM   1846  C  CG    . TRP A 1 1544 ? 202.511 152.042 153.845 1.00 40.62  ? 1544 TRP A CG    1 
ATOM   1847  C  CD1   . TRP A 1 1544 ? 203.836 152.177 153.558 1.00 42.12  ? 1544 TRP A CD1   1 
ATOM   1848  C  CD2   . TRP A 1 1544 ? 202.243 150.635 153.845 1.00 42.62  ? 1544 TRP A CD2   1 
ATOM   1849  N  NE1   . TRP A 1 1544 ? 204.409 150.945 153.371 1.00 40.92  ? 1544 TRP A NE1   1 
ATOM   1850  C  CE2   . TRP A 1 1544 ? 203.451 149.981 153.542 1.00 43.42  ? 1544 TRP A CE2   1 
ATOM   1851  C  CE3   . TRP A 1 1544 ? 201.098 149.866 154.070 1.00 45.29  ? 1544 TRP A CE3   1 
ATOM   1852  C  CZ2   . TRP A 1 1544 ? 203.547 148.596 153.457 1.00 45.26  ? 1544 TRP A CZ2   1 
ATOM   1853  C  CZ3   . TRP A 1 1544 ? 201.195 148.492 153.984 1.00 49.95  ? 1544 TRP A CZ3   1 
ATOM   1854  C  CH2   . TRP A 1 1544 ? 202.410 147.871 153.680 1.00 51.08  ? 1544 TRP A CH2   1 
ATOM   1855  N  N     . VAL A 1 1545 ? 198.835 152.209 152.888 1.00 43.80  ? 1545 VAL A N     1 
ATOM   1856  C  CA    . VAL A 1 1545 ? 197.988 151.150 152.355 1.00 48.10  ? 1545 VAL A CA    1 
ATOM   1857  C  C     . VAL A 1 1545 ? 197.629 151.466 150.915 1.00 51.46  ? 1545 VAL A C     1 
ATOM   1858  O  O     . VAL A 1 1545 ? 197.962 150.709 149.993 1.00 54.34  ? 1545 VAL A O     1 
ATOM   1859  C  CB    . VAL A 1 1545 ? 196.733 150.972 153.227 1.00 48.97  ? 1545 VAL A CB    1 
ATOM   1860  C  CG1   . VAL A 1 1545 ? 195.711 150.109 152.511 1.00 52.95  ? 1545 VAL A CG1   1 
ATOM   1861  C  CG2   . VAL A 1 1545 ? 197.102 150.371 154.567 1.00 45.26  ? 1545 VAL A CG2   1 
ATOM   1862  N  N     . TYR A 1 1546 ? 197.063 152.655 150.689 1.00 47.93  ? 1546 TYR A N     1 
ATOM   1863  C  CA    . TYR A 1 1546 ? 196.699 153.028 149.331 1.00 47.77  ? 1546 TYR A CA    1 
ATOM   1864  C  C     . TYR A 1 1546 ? 197.901 152.900 148.417 1.00 47.44  ? 1546 TYR A C     1 
ATOM   1865  O  O     . TYR A 1 1546 ? 197.839 152.217 147.386 1.00 56.96  ? 1546 TYR A O     1 
ATOM   1866  C  CB    . TYR A 1 1546 ? 196.145 154.451 149.303 1.00 49.42  ? 1546 TYR A CB    1 
ATOM   1867  C  CG    . TYR A 1 1546 ? 195.903 154.991 147.912 1.00 56.01  ? 1546 TYR A CG    1 
ATOM   1868  C  CD1   . TYR A 1 1546 ? 194.917 154.451 147.098 1.00 59.17  ? 1546 TYR A CD1   1 
ATOM   1869  C  CD2   . TYR A 1 1546 ? 196.660 156.040 147.414 1.00 57.87  ? 1546 TYR A CD2   1 
ATOM   1870  C  CE1   . TYR A 1 1546 ? 194.693 154.943 145.828 1.00 66.02  ? 1546 TYR A CE1   1 
ATOM   1871  C  CE2   . TYR A 1 1546 ? 196.444 156.538 146.145 1.00 58.12  ? 1546 TYR A CE2   1 
ATOM   1872  C  CZ    . TYR A 1 1546 ? 195.460 155.986 145.357 1.00 65.10  ? 1546 TYR A CZ    1 
ATOM   1873  O  OH    . TYR A 1 1546 ? 195.243 156.481 144.092 1.00 69.52  ? 1546 TYR A OH    1 
ATOM   1874  N  N     . LEU A 1 1547 ? 199.038 153.449 148.842 1.00 41.73  ? 1547 LEU A N     1 
ATOM   1875  C  CA    . LEU A 1 1547 ? 200.190 153.483 147.958 1.00 39.41  ? 1547 LEU A CA    1 
ATOM   1876  C  C     . LEU A 1 1547 ? 200.677 152.078 147.643 1.00 45.07  ? 1547 LEU A C     1 
ATOM   1877  O  O     . LEU A 1 1547 ? 201.049 151.795 146.499 1.00 53.46  ? 1547 LEU A O     1 
ATOM   1878  C  CB    . LEU A 1 1547 ? 201.298 154.336 148.567 1.00 41.49  ? 1547 LEU A CB    1 
ATOM   1879  C  CG    . LEU A 1 1547 ? 201.341 155.770 148.034 1.00 44.38  ? 1547 LEU A CG    1 
ATOM   1880  C  CD1   . LEU A 1 1547 ? 200.056 156.510 148.345 1.00 45.08  ? 1547 LEU A CD1   1 
ATOM   1881  C  CD2   . LEU A 1 1547 ? 202.523 156.511 148.607 1.00 46.17  ? 1547 LEU A CD2   1 
ATOM   1882  N  N     . GLU A 1 1548 ? 200.646 151.166 148.621 1.00 46.28  ? 1548 GLU A N     1 
ATOM   1883  C  CA    . GLU A 1 1548 ? 201.123 149.831 148.285 1.00 52.94  ? 1548 GLU A CA    1 
ATOM   1884  C  C     . GLU A 1 1548 ? 200.158 149.156 147.324 1.00 61.72  ? 1548 GLU A C     1 
ATOM   1885  O  O     . GLU A 1 1548 ? 200.594 148.468 146.393 1.00 66.04  ? 1548 GLU A O     1 
ATOM   1886  C  CB    . GLU A 1 1548 ? 201.359 148.986 149.543 1.00 49.95  ? 1548 GLU A CB    1 
ATOM   1887  C  CG    . GLU A 1 1548 ? 200.145 148.679 150.388 1.00 62.64  ? 1548 GLU A CG    1 
ATOM   1888  C  CD    . GLU A 1 1548 ? 199.422 147.427 149.937 1.00 74.86  ? 1548 GLU A CD    1 
ATOM   1889  O  OE1   . GLU A 1 1548 ? 200.047 146.598 149.244 1.00 75.23  ? 1548 GLU A OE1   1 
ATOM   1890  O  OE2   . GLU A 1 1548 ? 198.229 147.273 150.270 1.00 79.01  ? 1548 GLU A OE2   1 
ATOM   1891  N  N     . GLY A 1 1549 ? 198.856 149.415 147.481 1.00 57.47  ? 1549 GLY A N     1 
ATOM   1892  C  CA    . GLY A 1 1549 ? 197.895 148.901 146.523 1.00 56.76  ? 1549 GLY A CA    1 
ATOM   1893  C  C     . GLY A 1 1549 ? 198.164 149.410 145.122 1.00 59.87  ? 1549 GLY A C     1 
ATOM   1894  O  O     . GLY A 1 1549 ? 197.789 148.774 144.134 1.00 73.30  ? 1549 GLY A O     1 
ATOM   1895  N  N     . ILE A 1 1550 ? 198.821 150.566 145.017 1.00 53.95  ? 1550 ILE A N     1 
ATOM   1896  C  CA    . ILE A 1 1550 ? 199.184 151.092 143.708 1.00 49.50  ? 1550 ILE A CA    1 
ATOM   1897  C  C     . ILE A 1 1550 ? 200.462 150.432 143.211 1.00 58.25  ? 1550 ILE A C     1 
ATOM   1898  O  O     . ILE A 1 1550 ? 200.604 150.134 142.020 1.00 70.95  ? 1550 ILE A O     1 
ATOM   1899  C  CB    . ILE A 1 1550 ? 199.327 152.623 143.766 1.00 48.32  ? 1550 ILE A CB    1 
ATOM   1900  C  CG1   . ILE A 1 1550 ? 198.074 153.259 144.372 1.00 52.41  ? 1550 ILE A CG1   1 
ATOM   1901  C  CG2   . ILE A 1 1550 ? 199.608 153.184 142.386 1.00 51.08  ? 1550 ILE A CG2   1 
ATOM   1902  C  CD1   . ILE A 1 1550 ? 196.779 152.741 143.806 1.00 53.04  ? 1550 ILE A CD1   1 
ATOM   1903  N  N     . PHE A 1 1551 ? 201.408 150.187 144.114 1.00 58.02  ? 1551 PHE A N     1 
ATOM   1904  C  CA    . PHE A 1 1551 ? 202.741 149.759 143.716 1.00 59.18  ? 1551 PHE A CA    1 
ATOM   1905  C  C     . PHE A 1 1551 ? 202.936 148.251 143.802 1.00 67.92  ? 1551 PHE A C     1 
ATOM   1906  O  O     . PHE A 1 1551 ? 204.045 147.770 143.549 1.00 69.24  ? 1551 PHE A O     1 
ATOM   1907  C  CB    . PHE A 1 1551 ? 203.793 150.476 144.569 1.00 52.48  ? 1551 PHE A CB    1 
ATOM   1908  C  CG    . PHE A 1 1551 ? 203.983 151.921 144.199 1.00 52.30  ? 1551 PHE A CG    1 
ATOM   1909  C  CD1   . PHE A 1 1551 ? 204.630 152.271 143.029 1.00 60.67  ? 1551 PHE A CD1   1 
ATOM   1910  C  CD2   . PHE A 1 1551 ? 203.497 152.928 145.013 1.00 50.95  ? 1551 PHE A CD2   1 
ATOM   1911  C  CE1   . PHE A 1 1551 ? 204.800 153.599 142.685 1.00 61.22  ? 1551 PHE A CE1   1 
ATOM   1912  C  CE2   . PHE A 1 1551 ? 203.662 154.256 144.673 1.00 49.75  ? 1551 PHE A CE2   1 
ATOM   1913  C  CZ    . PHE A 1 1551 ? 204.314 154.591 143.508 1.00 51.74  ? 1551 PHE A CZ    1 
ATOM   1914  N  N     . THR A 1 1552 ? 201.894 147.498 144.153 1.00 72.10  ? 1552 THR A N     1 
ATOM   1915  C  CA    . THR A 1 1552 ? 201.941 146.041 144.179 1.00 83.26  ? 1552 THR A CA    1 
ATOM   1916  C  C     . THR A 1 1552 ? 200.765 145.437 143.417 1.00 88.99  ? 1552 THR A C     1 
ATOM   1917  O  O     . THR A 1 1552 ? 200.397 144.283 143.641 1.00 91.56  ? 1552 THR A O     1 
ATOM   1918  C  CB    . THR A 1 1552 ? 201.966 145.517 145.615 1.00 82.78  ? 1552 THR A CB    1 
ATOM   1919  O  OG1   . THR A 1 1552 ? 200.757 145.895 146.285 1.00 79.43  ? 1552 THR A OG1   1 
ATOM   1920  C  CG2   . THR A 1 1552 ? 203.163 146.076 146.376 1.00 73.58  ? 1552 THR A CG2   1 
ATOM   1921  N  N     . GLY A 1 1553 ? 200.166 146.210 142.515 1.00 88.86  ? 1553 GLY A N     1 
ATOM   1922  C  CA    . GLY A 1 1553 ? 199.036 145.738 141.741 1.00 92.49  ? 1553 GLY A CA    1 
ATOM   1923  C  C     . GLY A 1 1553 ? 199.384 145.474 140.292 1.00 101.22 ? 1553 GLY A C     1 
ATOM   1924  O  O     . GLY A 1 1553 ? 198.800 144.592 139.655 1.00 103.57 ? 1553 GLY A O     1 
ATOM   1925  N  N     . SER A 1 1554 ? 200.339 146.234 139.760 1.00 101.36 ? 1554 SER A N     1 
ATOM   1926  C  CA    . SER A 1 1554 ? 200.797 146.055 138.389 1.00 104.60 ? 1554 SER A CA    1 
ATOM   1927  C  C     . SER A 1 1554 ? 202.288 146.347 138.336 1.00 104.55 ? 1554 SER A C     1 
ATOM   1928  O  O     . SER A 1 1554 ? 202.753 147.319 138.938 1.00 92.70  ? 1554 SER A O     1 
ATOM   1929  C  CB    . SER A 1 1554 ? 200.036 146.969 137.422 1.00 99.61  ? 1554 SER A CB    1 
ATOM   1930  O  OG    . SER A 1 1554 ? 200.625 146.947 136.133 1.00 99.65  ? 1554 SER A OG    1 
ATOM   1931  N  N     . ALA A 1 1555 ? 203.030 145.500 137.619 1.00 110.71 ? 1555 ALA A N     1 
ATOM   1932  C  CA    . ALA A 1 1555 ? 204.478 145.657 137.558 1.00 106.97 ? 1555 ALA A CA    1 
ATOM   1933  C  C     . ALA A 1 1555 ? 204.885 146.867 136.728 1.00 102.72 ? 1555 ALA A C     1 
ATOM   1934  O  O     . ALA A 1 1555 ? 205.934 147.467 136.987 1.00 100.66 ? 1555 ALA A O     1 
ATOM   1935  C  CB    . ALA A 1 1555 ? 205.121 144.389 136.997 1.00 101.38 ? 1555 ALA A CB    1 
ATOM   1936  N  N     . ASP A 1 1556 ? 204.072 147.252 135.741 1.00 98.32  ? 1556 ASP A N     1 
ATOM   1937  C  CA    . ASP A 1 1556 ? 204.441 148.369 134.881 1.00 93.15  ? 1556 ASP A CA    1 
ATOM   1938  C  C     . ASP A 1 1556 ? 204.287 149.716 135.574 1.00 90.66  ? 1556 ASP A C     1 
ATOM   1939  O  O     . ASP A 1 1556 ? 204.856 150.705 135.102 1.00 87.17  ? 1556 ASP A O     1 
ATOM   1940  C  CB    . ASP A 1 1556 ? 203.616 148.344 133.594 1.00 93.47  ? 1556 ASP A CB    1 
ATOM   1941  C  CG    . ASP A 1 1556 ? 203.978 147.177 132.693 1.00 107.03 ? 1556 ASP A CG    1 
ATOM   1942  O  OD1   . ASP A 1 1556 ? 205.144 146.733 132.735 1.00 110.21 ? 1556 ASP A OD1   1 
ATOM   1943  O  OD2   . ASP A 1 1556 ? 203.097 146.699 131.948 1.00 102.99 ? 1556 ASP A OD2   1 
ATOM   1944  N  N     . ILE A 1 1557 ? 203.543 149.775 136.683 1.00 92.30  ? 1557 ILE A N     1 
ATOM   1945  C  CA    . ILE A 1 1557 ? 203.418 151.022 137.433 1.00 85.53  ? 1557 ILE A CA    1 
ATOM   1946  C  C     . ILE A 1 1557 ? 204.784 151.485 137.922 1.00 79.28  ? 1557 ILE A C     1 
ATOM   1947  O  O     . ILE A 1 1557 ? 205.079 152.686 137.950 1.00 73.34  ? 1557 ILE A O     1 
ATOM   1948  C  CB    . ILE A 1 1557 ? 202.429 150.846 138.601 1.00 81.42  ? 1557 ILE A CB    1 
ATOM   1949  C  CG1   . ILE A 1 1557 ? 201.042 150.473 138.078 1.00 82.43  ? 1557 ILE A CG1   1 
ATOM   1950  C  CG2   . ILE A 1 1557 ? 202.352 152.114 139.435 1.00 65.43  ? 1557 ILE A CG2   1 
ATOM   1951  C  CD1   . ILE A 1 1557 ? 200.459 151.481 137.120 1.00 76.82  ? 1557 ILE A CD1   1 
ATOM   1952  N  N     . LYS A 1 1558 ? 205.638 150.539 138.317 1.00 82.38  ? 1558 LYS A N     1 
ATOM   1953  C  CA    . LYS A 1 1558 ? 206.991 150.889 138.734 1.00 79.20  ? 1558 LYS A CA    1 
ATOM   1954  C  C     . LYS A 1 1558 ? 207.801 151.464 137.577 1.00 82.20  ? 1558 LYS A C     1 
ATOM   1955  O  O     . LYS A 1 1558 ? 208.592 152.394 137.769 1.00 81.67  ? 1558 LYS A O     1 
ATOM   1956  C  CB    . LYS A 1 1558 ? 207.686 149.665 139.329 1.00 81.43  ? 1558 LYS A CB    1 
ATOM   1957  C  CG    . LYS A 1 1558 ? 206.787 148.828 140.227 1.00 82.01  ? 1558 LYS A CG    1 
ATOM   1958  C  CD    . LYS A 1 1558 ? 207.473 147.546 140.668 1.00 89.69  ? 1558 LYS A CD    1 
ATOM   1959  C  CE    . LYS A 1 1558 ? 206.540 146.681 141.499 1.00 95.44  ? 1558 LYS A CE    1 
ATOM   1960  N  NZ    . LYS A 1 1558 ? 207.205 145.433 141.967 1.00 97.29  ? 1558 LYS A NZ    1 
ATOM   1961  N  N     . HIS A 1 1559 ? 207.631 150.918 136.370 1.00 82.95  ? 1559 HIS A N     1 
ATOM   1962  C  CA    . HIS A 1 1559 ? 208.323 151.478 135.212 1.00 82.66  ? 1559 HIS A CA    1 
ATOM   1963  C  C     . HIS A 1 1559 ? 207.815 152.877 134.883 1.00 80.57  ? 1559 HIS A C     1 
ATOM   1964  O  O     . HIS A 1 1559 ? 208.596 153.750 134.487 1.00 82.55  ? 1559 HIS A O     1 
ATOM   1965  C  CB    . HIS A 1 1559 ? 208.190 150.559 133.993 1.00 89.07  ? 1559 HIS A CB    1 
ATOM   1966  C  CG    . HIS A 1 1559 ? 208.452 149.111 134.275 1.00 98.00  ? 1559 HIS A CG    1 
ATOM   1967  N  ND1   . HIS A 1 1559 ? 207.722 148.374 135.182 1.00 97.82  ? 1559 HIS A ND1   1 
ATOM   1968  C  CD2   . HIS A 1 1559 ? 209.373 148.262 133.760 1.00 99.14  ? 1559 HIS A CD2   1 
ATOM   1969  C  CE1   . HIS A 1 1559 ? 208.182 147.135 135.213 1.00 98.76  ? 1559 HIS A CE1   1 
ATOM   1970  N  NE2   . HIS A 1 1559 ? 209.184 147.041 134.359 1.00 102.30 ? 1559 HIS A NE2   1 
ATOM   1971  N  N     . LEU A 1 1560 ? 206.507 153.106 135.024 1.00 77.72  ? 1560 LEU A N     1 
ATOM   1972  C  CA    . LEU A 1 1560 ? 205.961 154.437 134.770 1.00 73.77  ? 1560 LEU A CA    1 
ATOM   1973  C  C     . LEU A 1 1560 ? 206.500 155.459 135.762 1.00 73.65  ? 1560 LEU A C     1 
ATOM   1974  O  O     . LEU A 1 1560 ? 206.820 156.593 135.386 1.00 73.98  ? 1560 LEU A O     1 
ATOM   1975  C  CB    . LEU A 1 1560 ? 204.435 154.409 134.826 1.00 71.24  ? 1560 LEU A CB    1 
ATOM   1976  C  CG    . LEU A 1 1560 ? 203.702 153.339 134.026 1.00 73.35  ? 1560 LEU A CG    1 
ATOM   1977  C  CD1   . LEU A 1 1560 ? 202.268 153.252 134.496 1.00 70.93  ? 1560 LEU A CD1   1 
ATOM   1978  C  CD2   . LEU A 1 1560 ? 203.766 153.638 132.541 1.00 73.49  ? 1560 LEU A CD2   1 
ATOM   1979  N  N     . LEU A 1 1561 ? 206.605 155.079 137.032 1.00 72.43  ? 1561 LEU A N     1 
ATOM   1980  C  CA    . LEU A 1 1561 ? 207.024 155.980 138.106 1.00 66.30  ? 1561 LEU A CA    1 
ATOM   1981  C  C     . LEU A 1 1561 ? 208.198 155.356 138.848 1.00 66.92  ? 1561 LEU A C     1 
ATOM   1982  O  O     . LEU A 1 1561 ? 208.044 154.836 139.958 1.00 67.98  ? 1561 LEU A O     1 
ATOM   1983  C  CB    . LEU A 1 1561 ? 205.861 156.265 139.058 1.00 63.62  ? 1561 LEU A CB    1 
ATOM   1984  C  CG    . LEU A 1 1561 ? 204.735 157.153 138.529 1.00 57.65  ? 1561 LEU A CG    1 
ATOM   1985  C  CD1   . LEU A 1 1561 ? 203.727 157.447 139.623 1.00 49.51  ? 1561 LEU A CD1   1 
ATOM   1986  C  CD2   . LEU A 1 1561 ? 205.298 158.443 137.963 1.00 65.11  ? 1561 LEU A CD2   1 
ATOM   1987  N  N     . PRO A 1 1562 ? 209.395 155.389 138.256 1.00 69.52  ? 1562 PRO A N     1 
ATOM   1988  C  CA    . PRO A 1 1562 ? 210.542 154.751 138.923 1.00 69.60  ? 1562 PRO A CA    1 
ATOM   1989  C  C     . PRO A 1 1562 ? 211.006 155.493 140.163 1.00 71.20  ? 1562 PRO A C     1 
ATOM   1990  O  O     . PRO A 1 1562 ? 211.275 154.860 141.193 1.00 75.31  ? 1562 PRO A O     1 
ATOM   1991  C  CB    . PRO A 1 1562 ? 211.615 154.739 137.826 1.00 75.67  ? 1562 PRO A CB    1 
ATOM   1992  C  CG    . PRO A 1 1562 ? 211.261 155.893 136.951 1.00 71.54  ? 1562 PRO A CG    1 
ATOM   1993  C  CD    . PRO A 1 1562 ? 209.762 155.980 136.958 1.00 70.75  ? 1562 PRO A CD    1 
ATOM   1994  N  N     . VAL A 1 1563 ? 211.074 156.823 140.079 1.00 69.71  ? 1563 VAL A N     1 
ATOM   1995  C  CA    . VAL A 1 1563 ? 211.471 157.647 141.259 1.00 67.33  ? 1563 VAL A CA    1 
ATOM   1996  C  C     . VAL A 1 1563 ? 210.475 157.383 142.398 1.00 64.78  ? 1563 VAL A C     1 
ATOM   1997  O  O     . VAL A 1 1563 ? 210.932 157.073 143.516 1.00 67.40  ? 1563 VAL A O     1 
ATOM   1998  C  CB    . VAL A 1 1563 ? 211.513 159.140 140.890 1.00 67.66  ? 1563 VAL A CB    1 
ATOM   1999  C  CG1   . VAL A 1 1563 ? 212.062 159.988 142.030 1.00 78.71  ? 1563 VAL A CG1   1 
ATOM   2000  C  CG2   . VAL A 1 1563 ? 212.308 159.382 139.614 1.00 64.59  ? 1563 VAL A CG2   1 
ATOM   2001  N  N     . GLU A 1 1564 ? 209.174 157.478 142.115 1.00 61.10  ? 1564 GLU A N     1 
ATOM   2002  C  CA    . GLU A 1 1564 ? 208.139 157.301 143.169 1.00 58.47  ? 1564 GLU A CA    1 
ATOM   2003  C  C     . GLU A 1 1564 ? 208.214 155.879 143.751 1.00 59.07  ? 1564 GLU A C     1 
ATOM   2004  O  O     . GLU A 1 1564 ? 208.038 155.739 144.978 1.00 64.35  ? 1564 GLU A O     1 
ATOM   2005  C  CB    . GLU A 1 1564 ? 206.742 157.588 142.620 1.00 60.53  ? 1564 GLU A CB    1 
ATOM   2006  C  CG    . GLU A 1 1564 ? 206.406 159.075 142.563 1.00 62.75  ? 1564 GLU A CG    1 
ATOM   2007  C  CD    . GLU A 1 1564 ? 207.332 159.897 141.685 1.00 76.83  ? 1564 GLU A CD    1 
ATOM   2008  O  OE1   . GLU A 1 1564 ? 207.409 159.605 140.474 1.00 77.86  ? 1564 GLU A OE1   1 
ATOM   2009  O  OE2   . GLU A 1 1564 ? 207.978 160.825 142.213 1.00 81.95  ? 1564 GLU A OE2   1 
ATOM   2010  N  N     . THR A 1 1565 ? 208.448 154.871 142.907 1.00 58.28  ? 1565 THR A N     1 
ATOM   2011  C  CA    . THR A 1 1565 ? 208.526 153.476 143.393 1.00 56.74  ? 1565 THR A CA    1 
ATOM   2012  C  C     . THR A 1 1565 ? 209.701 153.355 144.333 1.00 62.92  ? 1565 THR A C     1 
ATOM   2013  O  O     . THR A 1 1565 ? 209.529 152.767 145.420 1.00 72.27  ? 1565 THR A O     1 
ATOM   2014  C  CB    . THR A 1 1565 ? 208.654 152.507 142.221 1.00 66.25  ? 1565 THR A CB    1 
ATOM   2015  O  OG1   . THR A 1 1565 ? 207.539 152.782 141.381 1.00 79.16  ? 1565 THR A OG1   1 
ATOM   2016  C  CG2   . THR A 1 1565 ? 208.626 151.057 142.666 1.00 61.98  ? 1565 THR A CG2   1 
ATOM   2017  N  N     . GLN A 1 1566 ? 210.854 153.905 143.944 1.00 60.86  ? 1566 GLN A N     1 
ATOM   2018  C  CA    . GLN A 1 1566 ? 212.055 153.871 144.816 1.00 60.56  ? 1566 GLN A CA    1 
ATOM   2019  C  C     . GLN A 1 1566 ? 211.732 154.584 146.137 1.00 60.68  ? 1566 GLN A C     1 
ATOM   2020  O  O     . GLN A 1 1566 ? 212.045 154.021 147.209 1.00 63.91  ? 1566 GLN A O     1 
ATOM   2021  C  CB    . GLN A 1 1566 ? 213.227 154.544 144.106 1.00 65.51  ? 1566 GLN A CB    1 
ATOM   2022  C  CG    . GLN A 1 1566 ? 214.502 154.615 144.939 1.00 75.29  ? 1566 GLN A CG    1 
ATOM   2023  C  CD    . GLN A 1 1566 ? 215.609 155.393 144.263 1.00 82.83  ? 1566 GLN A CD    1 
ATOM   2024  O  OE1   . GLN A 1 1566 ? 215.446 155.914 143.154 1.00 90.23  ? 1566 GLN A OE1   1 
ATOM   2025  N  NE2   . GLN A 1 1566 ? 216.750 155.482 144.930 1.00 76.11  ? 1566 GLN A NE2   1 
ATOM   2026  N  N     . ARG A 1 1567 ? 211.110 155.763 146.059 1.00 57.21  ? 1567 ARG A N     1 
ATOM   2027  C  CA    . ARG A 1 1567 ? 210.764 156.533 147.280 1.00 53.23  ? 1567 ARG A CA    1 
ATOM   2028  C  C     . ARG A 1 1567 ? 209.834 155.694 148.167 1.00 51.22  ? 1567 ARG A C     1 
ATOM   2029  O  O     . ARG A 1 1567 ? 210.099 155.615 149.383 1.00 59.22  ? 1567 ARG A O     1 
ATOM   2030  C  CB    . ARG A 1 1567 ? 210.079 157.854 146.918 1.00 30.00  ? 1567 ARG A CB    1 
ATOM   2031  C  CG    . ARG A 1 1567 ? 210.927 158.864 146.160 1.00 30.00  ? 1567 ARG A CG    1 
ATOM   2032  C  CD    . ARG A 1 1567 ? 210.053 160.000 145.656 1.00 30.00  ? 1567 ARG A CD    1 
ATOM   2033  N  NE    . ARG A 1 1567 ? 210.820 161.042 144.966 1.00 30.00  ? 1567 ARG A NE    1 
ATOM   2034  C  CZ    . ARG A 1 1567 ? 210.284 162.121 144.409 1.00 30.00  ? 1567 ARG A CZ    1 
ATOM   2035  N  NH1   . ARG A 1 1567 ? 208.972 162.273 144.394 1.00 30.00  ? 1567 ARG A NH1   1 
ATOM   2036  N  NH2   . ARG A 1 1567 ? 211.062 163.040 143.866 1.00 30.00  ? 1567 ARG A NH2   1 
ATOM   2037  N  N     . PHE A 1 1568 ? 208.792 155.095 147.586 1.00 47.42  ? 1568 PHE A N     1 
ATOM   2038  C  CA    . PHE A 1 1568 ? 207.810 154.332 148.405 1.00 44.90  ? 1568 PHE A CA    1 
ATOM   2039  C  C     . PHE A 1 1568 ? 208.509 153.117 149.007 1.00 48.75  ? 1568 PHE A C     1 
ATOM   2040  O  O     . PHE A 1 1568 ? 208.260 152.798 150.185 1.00 56.11  ? 1568 PHE A O     1 
ATOM   2041  C  CB    . PHE A 1 1568 ? 206.562 153.917 147.621 1.00 42.33  ? 1568 PHE A CB    1 
ATOM   2042  C  CG    . PHE A 1 1568 ? 205.613 153.051 148.437 1.00 38.95  ? 1568 PHE A CG    1 
ATOM   2043  C  CD1   . PHE A 1 1568 ? 204.748 153.622 149.362 1.00 38.67  ? 1568 PHE A CD1   1 
ATOM   2044  C  CD2   . PHE A 1 1568 ? 205.586 151.670 148.276 1.00 41.78  ? 1568 PHE A CD2   1 
ATOM   2045  C  CE1   . PHE A 1 1568 ? 203.890 152.834 150.111 1.00 42.41  ? 1568 PHE A CE1   1 
ATOM   2046  C  CE2   . PHE A 1 1568 ? 204.723 150.888 149.025 1.00 44.88  ? 1568 PHE A CE2   1 
ATOM   2047  C  CZ    . PHE A 1 1568 ? 203.877 151.471 149.939 1.00 46.75  ? 1568 PHE A CZ    1 
ATOM   2048  N  N     . GLN A 1 1569 ? 209.371 152.464 148.227 1.00 47.02  ? 1569 GLN A N     1 
ATOM   2049  C  CA    . GLN A 1 1569 ? 210.129 151.298 148.747 1.00 53.83  ? 1569 GLN A CA    1 
ATOM   2050  C  C     . GLN A 1 1569 ? 210.922 151.736 149.986 1.00 56.01  ? 1569 GLN A C     1 
ATOM   2051  O  O     . GLN A 1 1569 ? 210.893 151.003 150.998 1.00 58.88  ? 1569 GLN A O     1 
ATOM   2052  C  CB    . GLN A 1 1569 ? 211.051 150.756 147.656 1.00 63.98  ? 1569 GLN A CB    1 
ATOM   2053  C  CG    . GLN A 1 1569 ? 212.006 149.666 148.130 1.00 74.22  ? 1569 GLN A CG    1 
ATOM   2054  C  CD    . GLN A 1 1569 ? 212.967 149.214 147.052 1.00 89.94  ? 1569 GLN A CD    1 
ATOM   2055  O  OE1   . GLN A 1 1569 ? 212.939 149.703 145.917 1.00 89.03  ? 1569 GLN A OE1   1 
ATOM   2056  N  NE2   . GLN A 1 1569 ? 213.830 148.271 147.400 1.00 89.80  ? 1569 GLN A NE2   1 
ATOM   2057  N  N     . SER A 1 1570 ? 211.589 152.892 149.912 1.00 55.88  ? 1570 SER A N     1 
ATOM   2058  C  CA    . SER A 1 1570 ? 212.370 153.413 151.064 1.00 53.23  ? 1570 SER A CA    1 
ATOM   2059  C  C     . SER A 1 1570 ? 211.433 153.694 152.248 1.00 48.55  ? 1570 SER A C     1 
ATOM   2060  O  O     . SER A 1 1570 ? 211.751 153.251 153.371 1.00 49.10  ? 1570 SER A O     1 
ATOM   2061  C  CB    . SER A 1 1570 ? 213.137 154.646 150.675 1.00 52.52  ? 1570 SER A CB    1 
ATOM   2062  O  OG    . SER A 1 1570 ? 213.944 154.400 149.533 1.00 57.93  ? 1570 SER A OG    1 
ATOM   2063  N  N     . ILE A 1 1571 ? 210.327 154.399 152.002 1.00 47.37  ? 1571 ILE A N     1 
ATOM   2064  C  CA    . ILE A 1 1571 ? 209.335 154.687 153.081 1.00 41.50  ? 1571 ILE A CA    1 
ATOM   2065  C  C     . ILE A 1 1571 ? 208.803 153.351 153.615 1.00 46.12  ? 1571 ILE A C     1 
ATOM   2066  O  O     . ILE A 1 1571 ? 208.819 153.163 154.847 1.00 54.86  ? 1571 ILE A O     1 
ATOM   2067  C  CB    . ILE A 1 1571 ? 208.192 155.572 152.555 1.00 38.72  ? 1571 ILE A CB    1 
ATOM   2068  C  CG1   . ILE A 1 1571 ? 208.707 156.917 152.059 1.00 41.36  ? 1571 ILE A CG1   1 
ATOM   2069  C  CG2   . ILE A 1 1571 ? 207.101 155.741 153.612 1.00 40.72  ? 1571 ILE A CG2   1 
ATOM   2070  C  CD1   . ILE A 1 1571 ? 207.636 157.780 151.421 1.00 45.73  ? 1571 ILE A CD1   1 
ATOM   2071  N  N     . SER A 1 1572 ? 208.352 152.465 152.725 1.00 43.42  ? 1572 SER A N     1 
ATOM   2072  C  CA    . SER A 1 1572 ? 207.784 151.205 153.181 1.00 40.58  ? 1572 SER A CA    1 
ATOM   2073  C  C     . SER A 1 1572 ? 208.750 150.467 154.092 1.00 46.67  ? 1572 SER A C     1 
ATOM   2074  O  O     . SER A 1 1572 ? 208.330 149.861 155.079 1.00 53.04  ? 1572 SER A O     1 
ATOM   2075  C  CB    . SER A 1 1572 ? 207.406 150.337 151.983 1.00 45.11  ? 1572 SER A CB    1 
ATOM   2076  O  OG    . SER A 1 1572 ? 206.822 149.118 152.402 1.00 50.69  ? 1572 SER A OG    1 
ATOM   2077  N  N     . THR A 1 1573 ? 210.045 150.498 153.776 1.00 44.35  ? 1573 THR A N     1 
ATOM   2078  C  CA    . THR A 1 1573 ? 211.030 149.892 154.667 1.00 43.06  ? 1573 THR A CA    1 
ATOM   2079  C  C     . THR A 1 1573 ? 210.980 150.534 156.047 1.00 50.95  ? 1573 THR A C     1 
ATOM   2080  O  O     . THR A 1 1573 ? 210.907 149.839 157.072 1.00 57.82  ? 1573 THR A O     1 
ATOM   2081  C  CB    . THR A 1 1573 ? 212.429 150.020 154.067 1.00 46.84  ? 1573 THR A CB    1 
ATOM   2082  O  OG1   . THR A 1 1573 ? 212.487 149.308 152.824 1.00 59.00  ? 1573 THR A OG1   1 
ATOM   2083  C  CG2   . THR A 1 1573 ? 213.469 149.455 155.018 1.00 53.44  ? 1573 THR A CG2   1 
ATOM   2084  N  N     . GLU A 1 1574 ? 210.999 151.870 156.090 1.00 52.11  ? 1574 GLU A N     1 
ATOM   2085  C  CA    . GLU A 1 1574 ? 210.960 152.561 157.378 1.00 42.90  ? 1574 GLU A CA    1 
ATOM   2086  C  C     . GLU A 1 1574 ? 209.660 152.275 158.125 1.00 41.42  ? 1574 GLU A C     1 
ATOM   2087  O  O     . GLU A 1 1574 ? 209.670 152.027 159.338 1.00 51.39  ? 1574 GLU A O     1 
ATOM   2088  C  CB    . GLU A 1 1574 ? 211.143 154.064 157.176 1.00 44.62  ? 1574 GLU A CB    1 
ATOM   2089  C  CG    . GLU A 1 1574 ? 211.343 154.836 158.467 1.00 58.33  ? 1574 GLU A CG    1 
ATOM   2090  C  CD    . GLU A 1 1574 ? 211.482 156.329 158.244 1.00 73.40  ? 1574 GLU A CD    1 
ATOM   2091  O  OE1   . GLU A 1 1574 ? 212.328 156.732 157.419 1.00 75.13  ? 1574 GLU A OE1   1 
ATOM   2092  O  OE2   . GLU A 1 1574 ? 210.749 157.099 158.898 1.00 71.86  ? 1574 GLU A OE2   1 
ATOM   2093  N  N     . PHE A 1 1575 ? 208.533 152.294 157.412 1.00 39.45  ? 1575 PHE A N     1 
ATOM   2094  C  CA    . PHE A 1 1575 ? 207.236 152.058 158.034 1.00 39.58  ? 1575 PHE A CA    1 
ATOM   2095  C  C     . PHE A 1 1575 ? 207.127 150.639 158.574 1.00 48.18  ? 1575 PHE A C     1 
ATOM   2096  O  O     . PHE A 1 1575 ? 206.572 150.425 159.655 1.00 57.08  ? 1575 PHE A O     1 
ATOM   2097  C  CB    . PHE A 1 1575 ? 206.123 152.336 157.025 1.00 37.22  ? 1575 PHE A CB    1 
ATOM   2098  C  CG    . PHE A 1 1575 ? 204.740 152.221 157.593 1.00 35.32  ? 1575 PHE A CG    1 
ATOM   2099  C  CD1   . PHE A 1 1575 ? 204.253 153.177 158.465 1.00 41.67  ? 1575 PHE A CD1   1 
ATOM   2100  C  CD2   . PHE A 1 1575 ? 203.925 151.157 157.252 1.00 37.77  ? 1575 PHE A CD2   1 
ATOM   2101  C  CE1   . PHE A 1 1575 ? 202.979 153.074 158.984 1.00 44.51  ? 1575 PHE A CE1   1 
ATOM   2102  C  CE2   . PHE A 1 1575 ? 202.652 151.050 157.769 1.00 41.19  ? 1575 PHE A CE2   1 
ATOM   2103  C  CZ    . PHE A 1 1575 ? 202.179 152.009 158.636 1.00 44.36  ? 1575 PHE A CZ    1 
ATOM   2104  N  N     . LEU A 1 1576 ? 207.646 149.654 157.839 1.00 45.79  ? 1576 LEU A N     1 
ATOM   2105  C  CA    . LEU A 1 1576 ? 207.589 148.275 158.309 1.00 45.42  ? 1576 LEU A CA    1 
ATOM   2106  C  C     . LEU A 1 1576 ? 208.494 148.065 159.515 1.00 48.42  ? 1576 LEU A C     1 
ATOM   2107  O  O     . LEU A 1 1576 ? 208.142 147.318 160.434 1.00 58.77  ? 1576 LEU A O     1 
ATOM   2108  C  CB    . LEU A 1 1576 ? 207.958 147.314 157.180 1.00 54.92  ? 1576 LEU A CB    1 
ATOM   2109  C  CG    . LEU A 1 1576 ? 206.977 147.194 156.009 1.00 55.64  ? 1576 LEU A CG    1 
ATOM   2110  C  CD1   . LEU A 1 1576 ? 207.164 145.871 155.287 1.00 59.72  ? 1576 LEU A CD1   1 
ATOM   2111  C  CD2   . LEU A 1 1576 ? 205.541 147.354 156.475 1.00 51.94  ? 1576 LEU A CD2   1 
ATOM   2112  N  N     . ALA A 1 1577 ? 209.663 148.713 159.536 1.00 46.27  ? 1577 ALA A N     1 
ATOM   2113  C  CA    . ALA A 1 1577 ? 210.496 148.652 160.735 1.00 48.92  ? 1577 ALA A CA    1 
ATOM   2114  C  C     . ALA A 1 1577 ? 209.774 149.257 161.934 1.00 49.49  ? 1577 ALA A C     1 
ATOM   2115  O  O     . ALA A 1 1577 ? 209.787 148.690 163.036 1.00 54.65  ? 1577 ALA A O     1 
ATOM   2116  C  CB    . ALA A 1 1577 ? 211.825 149.365 160.491 1.00 45.69  ? 1577 ALA A CB    1 
ATOM   2117  N  N     . LEU A 1 1578 ? 209.117 150.401 161.728 1.00 44.52  ? 1578 LEU A N     1 
ATOM   2118  C  CA    . LEU A 1 1578 ? 208.337 151.016 162.796 1.00 44.30  ? 1578 LEU A CA    1 
ATOM   2119  C  C     . LEU A 1 1578 ? 207.227 150.091 163.279 1.00 47.28  ? 1578 LEU A C     1 
ATOM   2120  O  O     . LEU A 1 1578 ? 206.986 149.971 164.487 1.00 58.34  ? 1578 LEU A O     1 
ATOM   2121  C  CB    . LEU A 1 1578 ? 207.746 152.335 162.310 1.00 45.77  ? 1578 LEU A CB    1 
ATOM   2122  C  CG    . LEU A 1 1578 ? 206.593 152.886 163.146 1.00 48.50  ? 1578 LEU A CG    1 
ATOM   2123  C  CD1   . LEU A 1 1578 ? 207.097 153.486 164.449 1.00 49.14  ? 1578 LEU A CD1   1 
ATOM   2124  C  CD2   . LEU A 1 1578 ? 205.783 153.886 162.342 1.00 50.73  ? 1578 LEU A CD2   1 
ATOM   2125  N  N     . MET A 1 1579 ? 206.529 149.439 162.351 1.00 44.86  ? 1579 MET A N     1 
ATOM   2126  C  CA    . MET A 1 1579 ? 205.404 148.600 162.742 1.00 48.52  ? 1579 MET A CA    1 
ATOM   2127  C  C     . MET A 1 1579 ? 205.878 147.334 163.441 1.00 53.68  ? 1579 MET A C     1 
ATOM   2128  O  O     . MET A 1 1579 ? 205.183 146.808 164.314 1.00 60.63  ? 1579 MET A O     1 
ATOM   2129  C  CB    . MET A 1 1579 ? 204.544 148.267 161.526 1.00 48.36  ? 1579 MET A CB    1 
ATOM   2130  C  CG    . MET A 1 1579 ? 203.872 149.487 160.923 1.00 51.85  ? 1579 MET A CG    1 
ATOM   2131  S  SD    . MET A 1 1579 ? 202.761 150.342 162.052 1.00 65.62  ? 1579 MET A SD    1 
ATOM   2132  C  CE    . MET A 1 1579 ? 201.438 149.157 162.197 1.00 64.76  ? 1579 MET A CE    1 
ATOM   2133  N  N     . LYS A 1 1580 ? 207.061 146.831 163.082 1.00 51.49  ? 1580 LYS A N     1 
ATOM   2134  C  CA    . LYS A 1 1580 ? 207.654 145.742 163.854 1.00 54.42  ? 1580 LYS A CA    1 
ATOM   2135  C  C     . LYS A 1 1580 ? 207.981 146.192 165.271 1.00 56.91  ? 1580 LYS A C     1 
ATOM   2136  O  O     . LYS A 1 1580 ? 207.720 145.465 166.241 1.00 61.55  ? 1580 LYS A O     1 
ATOM   2137  C  CB    . LYS A 1 1580 ? 208.908 145.216 163.156 1.00 57.33  ? 1580 LYS A CB    1 
ATOM   2138  C  CG    . LYS A 1 1580 ? 208.628 144.381 161.922 1.00 60.66  ? 1580 LYS A CG    1 
ATOM   2139  C  CD    . LYS A 1 1580 ? 209.105 142.951 162.115 1.00 65.31  ? 1580 LYS A CD    1 
ATOM   2140  C  CE    . LYS A 1 1580 ? 208.874 142.117 160.866 1.00 72.66  ? 1580 LYS A CE    1 
ATOM   2141  N  NZ    . LYS A 1 1580 ? 208.804 140.663 161.177 1.00 69.93  ? 1580 LYS A NZ    1 
ATOM   2142  N  N     . LYS A 1 1581 ? 208.545 147.397 165.412 1.00 54.88  ? 1581 LYS A N     1 
ATOM   2143  C  CA    . LYS A 1 1581 ? 208.803 147.936 166.745 1.00 51.34  ? 1581 LYS A CA    1 
ATOM   2144  C  C     . LYS A 1 1581 ? 207.517 148.030 167.556 1.00 52.57  ? 1581 LYS A C     1 
ATOM   2145  O  O     . LYS A 1 1581 ? 207.503 147.723 168.752 1.00 59.80  ? 1581 LYS A O     1 
ATOM   2146  C  CB    . LYS A 1 1581 ? 209.462 149.310 166.643 1.00 45.96  ? 1581 LYS A CB    1 
ATOM   2147  C  CG    . LYS A 1 1581 ? 210.964 149.300 166.832 1.00 54.17  ? 1581 LYS A CG    1 
ATOM   2148  C  CD    . LYS A 1 1581 ? 211.524 150.712 166.817 1.00 57.34  ? 1581 LYS A CD    1 
ATOM   2149  C  CE    . LYS A 1 1581 ? 212.632 150.875 167.844 1.00 67.31  ? 1581 LYS A CE    1 
ATOM   2150  N  NZ    . LYS A 1 1581 ? 212.974 152.305 168.071 1.00 71.28  ? 1581 LYS A NZ    1 
ATOM   2151  N  N     . VAL A 1 1582 ? 206.429 148.458 166.917 1.00 53.03  ? 1582 VAL A N     1 
ATOM   2152  C  CA    . VAL A 1 1582 ? 205.151 148.576 167.614 1.00 48.95  ? 1582 VAL A CA    1 
ATOM   2153  C  C     . VAL A 1 1582 ? 204.603 147.202 167.979 1.00 56.68  ? 1582 VAL A C     1 
ATOM   2154  O  O     . VAL A 1 1582 ? 204.063 147.007 169.073 1.00 68.00  ? 1582 VAL A O     1 
ATOM   2155  C  CB    . VAL A 1 1582 ? 204.154 149.378 166.762 1.00 42.80  ? 1582 VAL A CB    1 
ATOM   2156  C  CG1   . VAL A 1 1582 ? 202.766 149.325 167.371 1.00 44.56  ? 1582 VAL A CG1   1 
ATOM   2157  C  CG2   . VAL A 1 1582 ? 204.624 150.804 166.644 1.00 48.41  ? 1582 VAL A CG2   1 
ATOM   2158  N  N     . SER A 1 1583 ? 204.724 146.231 167.074 1.00 54.70  ? 1583 SER A N     1 
ATOM   2159  C  CA    . SER A 1 1583 ? 204.239 144.887 167.363 1.00 60.61  ? 1583 SER A CA    1 
ATOM   2160  C  C     . SER A 1 1583 ? 205.010 144.250 168.509 1.00 66.36  ? 1583 SER A C     1 
ATOM   2161  O  O     . SER A 1 1583 ? 204.463 143.411 169.233 1.00 66.99  ? 1583 SER A O     1 
ATOM   2162  C  CB    . SER A 1 1583 ? 204.329 144.014 166.112 1.00 69.27  ? 1583 SER A CB    1 
ATOM   2163  O  OG    . SER A 1 1583 ? 205.627 143.465 165.965 1.00 74.09  ? 1583 SER A OG    1 
ATOM   2164  N  N     . LYS A 1 1584 ? 206.281 144.624 168.684 1.00 63.89  ? 1584 LYS A N     1 
ATOM   2165  C  CA    . LYS A 1 1584 ? 207.026 144.144 169.844 1.00 63.02  ? 1584 LYS A CA    1 
ATOM   2166  C  C     . LYS A 1 1584 ? 206.415 144.652 171.146 1.00 66.48  ? 1584 LYS A C     1 
ATOM   2167  O  O     . LYS A 1 1584 ? 206.247 143.887 172.102 1.00 68.95  ? 1584 LYS A O     1 
ATOM   2168  C  CB    . LYS A 1 1584 ? 208.491 144.565 169.741 1.00 62.93  ? 1584 LYS A CB    1 
ATOM   2169  C  CG    . LYS A 1 1584 ? 209.360 143.591 168.966 1.00 66.92  ? 1584 LYS A CG    1 
ATOM   2170  C  CD    . LYS A 1 1584 ? 210.821 143.711 169.366 1.00 72.35  ? 1584 LYS A CD    1 
ATOM   2171  C  CE    . LYS A 1 1584 ? 211.284 145.159 169.352 1.00 72.85  ? 1584 LYS A CE    1 
ATOM   2172  N  NZ    . LYS A 1 1584 ? 212.767 145.265 169.414 1.00 76.62  ? 1584 LYS A NZ    1 
ATOM   2173  N  N     . SER A 1 1585 ? 206.068 145.938 171.199 1.00 64.36  ? 1585 SER A N     1 
ATOM   2174  C  CA    . SER A 1 1585 ? 205.531 146.580 172.400 1.00 63.13  ? 1585 SER A CA    1 
ATOM   2175  C  C     . SER A 1 1585 ? 204.251 147.314 172.027 1.00 62.19  ? 1585 SER A C     1 
ATOM   2176  O  O     . SER A 1 1585 ? 204.267 148.524 171.767 1.00 61.30  ? 1585 SER A O     1 
ATOM   2177  C  CB    . SER A 1 1585 ? 206.552 147.534 173.018 1.00 67.28  ? 1585 SER A CB    1 
ATOM   2178  O  OG    . SER A 1 1585 ? 206.947 148.525 172.086 1.00 65.50  ? 1585 SER A OG    1 
ATOM   2179  N  N     . PRO A 1 1586 ? 203.118 146.610 171.988 1.00 60.32  ? 1586 PRO A N     1 
ATOM   2180  C  CA    . PRO A 1 1586 ? 201.875 147.219 171.498 1.00 60.39  ? 1586 PRO A CA    1 
ATOM   2181  C  C     . PRO A 1 1586 ? 201.173 148.128 172.494 1.00 67.85  ? 1586 PRO A C     1 
ATOM   2182  O  O     . PRO A 1 1586 ? 200.115 148.671 172.159 1.00 69.32  ? 1586 PRO A O     1 
ATOM   2183  C  CB    . PRO A 1 1586 ? 201.008 145.997 171.172 1.00 59.74  ? 1586 PRO A CB    1 
ATOM   2184  C  CG    . PRO A 1 1586 ? 201.479 144.952 172.113 1.00 62.98  ? 1586 PRO A CG    1 
ATOM   2185  C  CD    . PRO A 1 1586 ? 202.948 145.187 172.324 1.00 61.37  ? 1586 PRO A CD    1 
ATOM   2186  N  N     . LEU A 1 1587 ? 201.710 148.310 173.698 1.00 71.03  ? 1587 LEU A N     1 
ATOM   2187  C  CA    . LEU A 1 1587 ? 201.087 149.213 174.656 1.00 63.96  ? 1587 LEU A CA    1 
ATOM   2188  C  C     . LEU A 1 1587 ? 201.179 150.651 174.163 1.00 60.63  ? 1587 LEU A C     1 
ATOM   2189  O  O     . LEU A 1 1587 ? 202.209 151.078 173.636 1.00 65.08  ? 1587 LEU A O     1 
ATOM   2190  C  CB    . LEU A 1 1587 ? 201.750 149.090 176.028 1.00 64.84  ? 1587 LEU A CB    1 
ATOM   2191  C  CG    . LEU A 1 1587 ? 201.298 147.977 176.980 1.00 67.72  ? 1587 LEU A CG    1 
ATOM   2192  C  CD1   . LEU A 1 1587 ? 199.838 148.161 177.361 1.00 67.81  ? 1587 LEU A CD1   1 
ATOM   2193  C  CD2   . LEU A 1 1587 ? 201.543 146.588 176.408 1.00 71.40  ? 1587 LEU A CD2   1 
ATOM   2194  N  N     . VAL A 1 1588 ? 200.091 151.401 174.345 1.00 55.46  ? 1588 VAL A N     1 
ATOM   2195  C  CA    . VAL A 1 1588 ? 200.040 152.774 173.847 1.00 52.90  ? 1588 VAL A CA    1 
ATOM   2196  C  C     . VAL A 1 1588 ? 201.092 153.634 174.534 1.00 57.59  ? 1588 VAL A C     1 
ATOM   2197  O  O     . VAL A 1 1588 ? 201.715 154.497 173.905 1.00 62.72  ? 1588 VAL A O     1 
ATOM   2198  C  CB    . VAL A 1 1588 ? 198.624 153.351 174.020 1.00 49.50  ? 1588 VAL A CB    1 
ATOM   2199  C  CG1   . VAL A 1 1588 ? 198.616 154.840 173.734 1.00 49.15  ? 1588 VAL A CG1   1 
ATOM   2200  C  CG2   . VAL A 1 1588 ? 197.667 152.641 173.093 1.00 51.88  ? 1588 VAL A CG2   1 
ATOM   2201  N  N     . MET A 1 1589 ? 201.311 153.416 175.831 1.00 56.92  ? 1589 MET A N     1 
ATOM   2202  C  CA    . MET A 1 1589 ? 202.368 154.145 176.523 1.00 61.15  ? 1589 MET A CA    1 
ATOM   2203  C  C     . MET A 1 1589 ? 203.743 153.743 176.004 1.00 66.79  ? 1589 MET A C     1 
ATOM   2204  O  O     . MET A 1 1589 ? 204.648 154.581 175.911 1.00 68.88  ? 1589 MET A O     1 
ATOM   2205  C  CB    . MET A 1 1589 ? 202.269 153.915 178.031 1.00 66.72  ? 1589 MET A CB    1 
ATOM   2206  C  CG    . MET A 1 1589 ? 200.990 154.448 178.678 1.00 69.42  ? 1589 MET A CG    1 
ATOM   2207  S  SD    . MET A 1 1589 ? 200.431 156.112 178.226 1.00 81.93  ? 1589 MET A SD    1 
ATOM   2208  C  CE    . MET A 1 1589 ? 201.952 157.064 178.239 1.00 66.64  ? 1589 MET A CE    1 
ATOM   2209  N  N     . ASP A 1 1590 ? 203.925 152.463 175.672 1.00 67.13  ? 1590 ASP A N     1 
ATOM   2210  C  CA    . ASP A 1 1590 ? 205.192 152.025 175.094 1.00 67.70  ? 1590 ASP A CA    1 
ATOM   2211  C  C     . ASP A 1 1590 ? 205.405 152.626 173.711 1.00 65.11  ? 1590 ASP A C     1 
ATOM   2212  O  O     . ASP A 1 1590 ? 206.520 153.036 173.369 1.00 70.55  ? 1590 ASP A O     1 
ATOM   2213  C  CB    . ASP A 1 1590 ? 205.243 150.499 175.032 1.00 69.86  ? 1590 ASP A CB    1 
ATOM   2214  C  CG    . ASP A 1 1590 ? 205.349 149.864 176.404 1.00 80.31  ? 1590 ASP A CG    1 
ATOM   2215  O  OD1   . ASP A 1 1590 ? 205.923 150.500 177.312 1.00 86.21  ? 1590 ASP A OD1   1 
ATOM   2216  O  OD2   . ASP A 1 1590 ? 204.865 148.726 176.576 1.00 78.59  ? 1590 ASP A OD2   1 
ATOM   2217  N  N     . VAL A 1 1591 ? 204.347 152.681 172.897 1.00 59.60  ? 1591 VAL A N     1 
ATOM   2218  C  CA    . VAL A 1 1591 ? 204.452 153.286 171.572 1.00 56.83  ? 1591 VAL A CA    1 
ATOM   2219  C  C     . VAL A 1 1591 ? 204.764 154.772 171.686 1.00 64.02  ? 1591 VAL A C     1 
ATOM   2220  O  O     . VAL A 1 1591 ? 205.581 155.312 170.930 1.00 67.33  ? 1591 VAL A O     1 
ATOM   2221  C  CB    . VAL A 1 1591 ? 203.163 153.036 170.768 1.00 52.34  ? 1591 VAL A CB    1 
ATOM   2222  C  CG1   . VAL A 1 1591 ? 203.223 153.752 169.433 1.00 55.32  ? 1591 VAL A CG1   1 
ATOM   2223  C  CG2   . VAL A 1 1591 ? 202.957 151.550 170.558 1.00 56.19  ? 1591 VAL A CG2   1 
ATOM   2224  N  N     . LEU A 1 1592 ? 204.116 155.458 172.630 1.00 65.13  ? 1592 LEU A N     1 
ATOM   2225  C  CA    . LEU A 1 1592 ? 204.353 156.885 172.814 1.00 62.28  ? 1592 LEU A CA    1 
ATOM   2226  C  C     . LEU A 1 1592 ? 205.772 157.169 173.285 1.00 64.14  ? 1592 LEU A C     1 
ATOM   2227  O  O     . LEU A 1 1592 ? 206.271 158.286 173.110 1.00 64.34  ? 1592 LEU A O     1 
ATOM   2228  C  CB    . LEU A 1 1592 ? 203.345 157.454 173.811 1.00 54.09  ? 1592 LEU A CB    1 
ATOM   2229  C  CG    . LEU A 1 1592 ? 203.086 158.956 173.741 1.00 54.84  ? 1592 LEU A CG    1 
ATOM   2230  C  CD1   . LEU A 1 1592 ? 202.346 159.311 172.465 1.00 57.61  ? 1592 LEU A CD1   1 
ATOM   2231  C  CD2   . LEU A 1 1592 ? 202.314 159.416 174.964 1.00 54.24  ? 1592 LEU A CD2   1 
ATOM   2232  N  N     . ASN A 1 1593 ? 206.433 156.182 173.882 1.00 65.40  ? 1593 ASN A N     1 
ATOM   2233  C  CA    . ASN A 1 1593 ? 207.774 156.360 174.420 1.00 72.89  ? 1593 ASN A CA    1 
ATOM   2234  C  C     . ASN A 1 1593 ? 208.870 155.964 173.440 1.00 73.47  ? 1593 ASN A C     1 
ATOM   2235  O  O     . ASN A 1 1593 ? 210.050 156.017 173.803 1.00 77.10  ? 1593 ASN A O     1 
ATOM   2236  C  CB    . ASN A 1 1593 ? 207.928 155.562 175.717 1.00 76.44  ? 1593 ASN A CB    1 
ATOM   2237  C  CG    . ASN A 1 1593 ? 207.288 156.254 176.903 1.00 81.56  ? 1593 ASN A CG    1 
ATOM   2238  O  OD1   . ASN A 1 1593 ? 207.025 157.456 176.866 1.00 79.46  ? 1593 ASN A OD1   1 
ATOM   2239  N  ND2   . ASN A 1 1593 ? 207.034 155.497 177.964 1.00 80.80  ? 1593 ASN A ND2   1 
ATOM   2240  N  N     . ILE A 1 1594 ? 208.516 155.564 172.217 1.00 67.40  ? 1594 ILE A N     1 
ATOM   2241  C  CA    . ILE A 1 1594 ? 209.530 155.255 171.218 1.00 68.79  ? 1594 ILE A CA    1 
ATOM   2242  C  C     . ILE A 1 1594 ? 210.292 156.525 170.869 1.00 71.26  ? 1594 ILE A C     1 
ATOM   2243  O  O     . ILE A 1 1594 ? 209.707 157.607 170.729 1.00 69.08  ? 1594 ILE A O     1 
ATOM   2244  C  CB    . ILE A 1 1594 ? 208.886 154.620 169.975 1.00 67.62  ? 1594 ILE A CB    1 
ATOM   2245  C  CG1   . ILE A 1 1594 ? 208.133 153.345 170.358 1.00 62.83  ? 1594 ILE A CG1   1 
ATOM   2246  C  CG2   . ILE A 1 1594 ? 209.936 154.305 168.924 1.00 64.65  ? 1594 ILE A CG2   1 
ATOM   2247  C  CD1   . ILE A 1 1594 ? 207.459 152.663 169.194 1.00 58.37  ? 1594 ILE A CD1   1 
ATOM   2248  N  N     . GLN A 1 1595 ? 211.611 156.399 170.739 1.00 72.68  ? 1595 GLN A N     1 
ATOM   2249  C  CA    . GLN A 1 1595 ? 212.463 157.562 170.535 1.00 77.26  ? 1595 GLN A CA    1 
ATOM   2250  C  C     . GLN A 1 1595 ? 212.180 158.212 169.186 1.00 80.52  ? 1595 GLN A C     1 
ATOM   2251  O  O     . GLN A 1 1595 ? 212.326 157.580 168.135 1.00 80.78  ? 1595 GLN A O     1 
ATOM   2252  C  CB    . GLN A 1 1595 ? 213.933 157.159 170.627 1.00 78.07  ? 1595 GLN A CB    1 
ATOM   2253  C  CG    . GLN A 1 1595 ? 214.902 158.322 170.514 1.00 85.95  ? 1595 GLN A CG    1 
ATOM   2254  C  CD    . GLN A 1 1595 ? 216.347 157.893 170.667 1.00 93.70  ? 1595 GLN A CD    1 
ATOM   2255  O  OE1   . GLN A 1 1595 ? 216.640 156.708 170.824 1.00 94.09  ? 1595 GLN A OE1   1 
ATOM   2256  N  NE2   . GLN A 1 1595 ? 217.259 158.856 170.620 1.00 95.30  ? 1595 GLN A NE2   1 
ATOM   2257  N  N     . GLY A 1 1596 ? 211.777 159.481 169.220 1.00 75.96  ? 1596 GLY A N     1 
ATOM   2258  C  CA    . GLY A 1 1596 ? 211.532 160.232 168.004 1.00 69.90  ? 1596 GLY A CA    1 
ATOM   2259  C  C     . GLY A 1 1596 ? 210.444 159.671 167.121 1.00 66.64  ? 1596 GLY A C     1 
ATOM   2260  O  O     . GLY A 1 1596 ? 210.510 159.824 165.900 1.00 67.30  ? 1596 GLY A O     1 
ATOM   2261  N  N     . VAL A 1 1597 ? 209.439 159.018 167.705 1.00 65.59  ? 1597 VAL A N     1 
ATOM   2262  C  CA    . VAL A 1 1597 ? 208.386 158.409 166.899 1.00 58.09  ? 1597 VAL A CA    1 
ATOM   2263  C  C     . VAL A 1 1597 ? 207.522 159.480 166.243 1.00 54.69  ? 1597 VAL A C     1 
ATOM   2264  O  O     . VAL A 1 1597 ? 207.085 159.325 165.098 1.00 59.80  ? 1597 VAL A O     1 
ATOM   2265  C  CB    . VAL A 1 1597 ? 207.553 157.435 167.754 1.00 59.03  ? 1597 VAL A CB    1 
ATOM   2266  C  CG1   . VAL A 1 1597 ? 206.956 158.143 168.961 1.00 64.00  ? 1597 VAL A CG1   1 
ATOM   2267  C  CG2   . VAL A 1 1597 ? 206.472 156.777 166.918 1.00 51.16  ? 1597 VAL A CG2   1 
ATOM   2268  N  N     . GLN A 1 1598 ? 207.264 160.584 166.947 1.00 54.92  ? 1598 GLN A N     1 
ATOM   2269  C  CA    . GLN A 1 1598 ? 206.432 161.643 166.384 1.00 53.89  ? 1598 GLN A CA    1 
ATOM   2270  C  C     . GLN A 1 1598 ? 207.088 162.270 165.159 1.00 58.83  ? 1598 GLN A C     1 
ATOM   2271  O  O     . GLN A 1 1598 ? 206.436 162.480 164.130 1.00 62.69  ? 1598 GLN A O     1 
ATOM   2272  C  CB    . GLN A 1 1598 ? 206.149 162.706 167.444 1.00 61.03  ? 1598 GLN A CB    1 
ATOM   2273  C  CG    . GLN A 1 1598 ? 205.395 163.917 166.923 1.00 63.51  ? 1598 GLN A CG    1 
ATOM   2274  C  CD    . GLN A 1 1598 ? 203.912 163.659 166.772 1.00 66.50  ? 1598 GLN A CD    1 
ATOM   2275  O  OE1   . GLN A 1 1598 ? 203.429 162.564 167.052 1.00 61.29  ? 1598 GLN A OE1   1 
ATOM   2276  N  NE2   . GLN A 1 1598 ? 203.178 164.672 166.328 1.00 70.54  ? 1598 GLN A NE2   1 
ATOM   2277  N  N     . ARG A 1 1599 ? 208.384 162.576 165.253 1.00 62.69  ? 1599 ARG A N     1 
ATOM   2278  C  CA    . ARG A 1 1599 ? 209.088 163.165 164.119 1.00 62.72  ? 1599 ARG A CA    1 
ATOM   2279  C  C     . ARG A 1 1599 ? 209.148 162.199 162.945 1.00 58.38  ? 1599 ARG A C     1 
ATOM   2280  O  O     . ARG A 1 1599 ? 208.975 162.604 161.788 1.00 59.97  ? 1599 ARG A O     1 
ATOM   2281  C  CB    . ARG A 1 1599 ? 210.495 163.587 164.539 1.00 67.06  ? 1599 ARG A CB    1 
ATOM   2282  C  CG    . ARG A 1 1599 ? 210.523 164.651 165.620 1.00 73.49  ? 1599 ARG A CG    1 
ATOM   2283  C  CD    . ARG A 1 1599 ? 209.892 165.951 165.130 1.00 77.91  ? 1599 ARG A CD    1 
ATOM   2284  N  NE    . ARG A 1 1599 ? 210.690 166.661 164.133 1.00 85.16  ? 1599 ARG A NE    1 
ATOM   2285  C  CZ    . ARG A 1 1599 ? 211.966 167.006 164.263 1.00 83.85  ? 1599 ARG A CZ    1 
ATOM   2286  N  NH1   . ARG A 1 1599 ? 212.635 166.800 165.386 1.00 79.65  ? 1599 ARG A NH1   1 
ATOM   2287  N  NH2   . ARG A 1 1599 ? 212.582 167.599 163.244 1.00 84.69  ? 1599 ARG A NH2   1 
ATOM   2288  N  N     . SER A 1 1600 ? 209.394 160.917 163.223 1.00 54.99  ? 1600 SER A N     1 
ATOM   2289  C  CA    . SER A 1 1600 ? 209.430 159.920 162.160 1.00 48.25  ? 1600 SER A CA    1 
ATOM   2290  C  C     . SER A 1 1600 ? 208.079 159.802 161.469 1.00 47.78  ? 1600 SER A C     1 
ATOM   2291  O  O     . SER A 1 1600 ? 208.010 159.723 160.238 1.00 54.85  ? 1600 SER A O     1 
ATOM   2292  C  CB    . SER A 1 1600 ? 209.865 158.570 162.727 1.00 48.31  ? 1600 SER A CB    1 
ATOM   2293  O  OG    . SER A 1 1600 ? 209.662 157.533 161.785 1.00 55.29  ? 1600 SER A OG    1 
ATOM   2294  N  N     . LEU A 1 1601 ? 206.991 159.794 162.241 1.00 43.45  ? 1601 LEU A N     1 
ATOM   2295  C  CA    . LEU A 1 1601 ? 205.664 159.711 161.640 1.00 42.42  ? 1601 LEU A CA    1 
ATOM   2296  C  C     . LEU A 1 1601 ? 205.329 160.963 160.841 1.00 48.81  ? 1601 LEU A C     1 
ATOM   2297  O  O     . LEU A 1 1601 ? 204.688 160.875 159.790 1.00 56.21  ? 1601 LEU A O     1 
ATOM   2298  C  CB    . LEU A 1 1601 ? 204.605 159.458 162.711 1.00 45.17  ? 1601 LEU A CB    1 
ATOM   2299  C  CG    . LEU A 1 1601 ? 204.277 158.007 163.066 1.00 46.68  ? 1601 LEU A CG    1 
ATOM   2300  C  CD1   . LEU A 1 1601 ? 203.574 157.335 161.903 1.00 49.90  ? 1601 LEU A CD1   1 
ATOM   2301  C  CD2   . LEU A 1 1601 ? 205.517 157.233 163.439 1.00 51.02  ? 1601 LEU A CD2   1 
ATOM   2302  N  N     . GLU A 1 1602 ? 205.742 162.140 161.318 1.00 50.35  ? 1602 GLU A N     1 
ATOM   2303  C  CA    . GLU A 1 1602 ? 205.512 163.355 160.541 1.00 50.86  ? 1602 GLU A CA    1 
ATOM   2304  C  C     . GLU A 1 1602 ? 206.278 163.322 159.223 1.00 53.95  ? 1602 GLU A C     1 
ATOM   2305  O  O     . GLU A 1 1602 ? 205.744 163.703 158.173 1.00 56.78  ? 1602 GLU A O     1 
ATOM   2306  C  CB    . GLU A 1 1602 ? 205.897 164.589 161.354 1.00 59.70  ? 1602 GLU A CB    1 
ATOM   2307  C  CG    . GLU A 1 1602 ? 205.007 164.849 162.555 1.00 63.77  ? 1602 GLU A CG    1 
ATOM   2308  C  CD    . GLU A 1 1602 ? 205.438 166.071 163.340 1.00 77.81  ? 1602 GLU A CD    1 
ATOM   2309  O  OE1   . GLU A 1 1602 ? 206.502 166.641 163.019 1.00 81.97  ? 1602 GLU A OE1   1 
ATOM   2310  O  OE2   . GLU A 1 1602 ? 204.713 166.464 164.278 1.00 75.26  ? 1602 GLU A OE2   1 
ATOM   2311  N  N     . ARG A 1 1603 ? 207.534 162.869 159.258 1.00 53.56  ? 1603 ARG A N     1 
ATOM   2312  C  CA    . ARG A 1 1603 ? 208.312 162.752 158.028 1.00 51.14  ? 1603 ARG A CA    1 
ATOM   2313  C  C     . ARG A 1 1603 ? 207.682 161.746 157.074 1.00 50.33  ? 1603 ARG A C     1 
ATOM   2314  O  O     . ARG A 1 1603 ? 207.608 161.987 155.862 1.00 54.05  ? 1603 ARG A O     1 
ATOM   2315  C  CB    . ARG A 1 1603 ? 209.752 162.359 158.356 1.00 51.45  ? 1603 ARG A CB    1 
ATOM   2316  C  CG    . ARG A 1 1603 ? 210.421 161.491 157.306 1.00 59.19  ? 1603 ARG A CG    1 
ATOM   2317  C  CD    . ARG A 1 1603 ? 211.872 161.212 157.659 1.00 67.80  ? 1603 ARG A CD    1 
ATOM   2318  N  NE    . ARG A 1 1603 ? 212.710 162.392 157.490 1.00 90.80  ? 1603 ARG A NE    1 
ATOM   2319  C  CZ    . ARG A 1 1603 ? 214.024 162.411 157.669 1.00 103.72 ? 1603 ARG A CZ    1 
ATOM   2320  N  NH1   . ARG A 1 1603 ? 214.689 161.323 158.022 1.00 108.03 ? 1603 ARG A NH1   1 
ATOM   2321  N  NH2   . ARG A 1 1603 ? 214.688 163.550 157.490 1.00 104.29 ? 1603 ARG A NH2   1 
ATOM   2322  N  N     . LEU A 1 1604 ? 207.217 160.612 157.603 1.00 47.14  ? 1604 LEU A N     1 
ATOM   2323  C  CA    . LEU A 1 1604 ? 206.560 159.617 156.764 1.00 42.12  ? 1604 LEU A CA    1 
ATOM   2324  C  C     . LEU A 1 1604 ? 205.284 160.172 156.150 1.00 45.13  ? 1604 LEU A C     1 
ATOM   2325  O  O     . LEU A 1 1604 ? 204.996 159.921 154.978 1.00 50.78  ? 1604 LEU A O     1 
ATOM   2326  C  CB    . LEU A 1 1604 ? 206.261 158.355 157.571 1.00 40.75  ? 1604 LEU A CB    1 
ATOM   2327  C  CG    . LEU A 1 1604 ? 207.467 157.491 157.933 1.00 43.81  ? 1604 LEU A CG    1 
ATOM   2328  C  CD1   . LEU A 1 1604 ? 207.016 156.161 158.503 1.00 45.77  ? 1604 LEU A CD1   1 
ATOM   2329  C  CD2   . LEU A 1 1604 ? 208.351 157.288 156.720 1.00 43.04  ? 1604 LEU A CD2   1 
ATOM   2330  N  N     . ALA A 1 1605 ? 204.503 160.926 156.927 1.00 44.12  ? 1605 ALA A N     1 
ATOM   2331  C  CA    . ALA A 1 1605 ? 203.288 161.527 156.390 1.00 45.19  ? 1605 ALA A CA    1 
ATOM   2332  C  C     . ALA A 1 1605 ? 203.608 162.513 155.279 1.00 51.77  ? 1605 ALA A C     1 
ATOM   2333  O  O     . ALA A 1 1605 ? 202.939 162.524 154.242 1.00 58.73  ? 1605 ALA A O     1 
ATOM   2334  C  CB    . ALA A 1 1605 ? 202.505 162.223 157.501 1.00 47.67  ? 1605 ALA A CB    1 
ATOM   2335  N  N     . ASP A 1 1606 ? 204.653 163.316 155.478 1.00 50.86  ? 1606 ASP A N     1 
ATOM   2336  C  CA    . ASP A 1 1606 ? 205.071 164.293 154.437 1.00 47.55  ? 1606 ASP A CA    1 
ATOM   2337  C  C     . ASP A 1 1606 ? 205.466 163.541 153.164 1.00 49.49  ? 1606 ASP A C     1 
ATOM   2338  O  O     . ASP A 1 1606 ? 204.883 163.838 152.101 1.00 57.95  ? 1606 ASP A O     1 
ATOM   2339  C  CB    . ASP A 1 1606 ? 206.194 165.183 154.942 1.00 55.09  ? 1606 ASP A CB    1 
ATOM   2340  C  CG    . ASP A 1 1606 ? 206.867 166.051 153.889 1.00 66.96  ? 1606 ASP A CG    1 
ATOM   2341  O  OD1   . ASP A 1 1606 ? 206.160 166.872 153.268 1.00 71.92  ? 1606 ASP A OD1   1 
ATOM   2342  O  OD2   . ASP A 1 1606 ? 208.092 165.898 153.703 1.00 66.60  ? 1606 ASP A OD2   1 
ATOM   2343  N  N     . LEU A 1 1607 ? 206.403 162.596 153.270 1.00 46.50  ? 1607 LEU A N     1 
ATOM   2344  C  CA    . LEU A 1 1607 ? 206.908 161.875 152.071 1.00 47.70  ? 1607 LEU A CA    1 
ATOM   2345  C  C     . LEU A 1 1607 ? 205.772 161.091 151.390 1.00 45.98  ? 1607 LEU A C     1 
ATOM   2346  O  O     . LEU A 1 1607 ? 205.682 161.149 150.147 1.00 48.49  ? 1607 LEU A O     1 
ATOM   2347  C  CB    . LEU A 1 1607 ? 208.059 160.965 152.491 1.00 46.99  ? 1607 LEU A CB    1 
ATOM   2348  C  CG    . LEU A 1 1607 ? 209.273 161.665 153.108 1.00 47.80  ? 1607 LEU A CG    1 
ATOM   2349  C  CD1   . LEU A 1 1607 ? 210.367 160.661 153.421 1.00 41.84  ? 1607 LEU A CD1   1 
ATOM   2350  C  CD2   . LEU A 1 1607 ? 209.791 162.760 152.193 1.00 52.78  ? 1607 LEU A CD2   1 
ATOM   2351  N  N     . LEU A 1 1608 ? 204.947 160.386 152.169 1.00 43.20  ? 1608 LEU A N     1 
ATOM   2352  C  CA    . LEU A 1 1608 ? 203.844 159.575 151.587 1.00 43.06  ? 1608 LEU A CA    1 
ATOM   2353  C  C     . LEU A 1 1608 ? 202.870 160.505 150.848 1.00 46.46  ? 1608 LEU A C     1 
ATOM   2354  O  O     . LEU A 1 1608 ? 202.413 160.130 149.750 1.00 56.06  ? 1608 LEU A O     1 
ATOM   2355  C  CB    . LEU A 1 1608 ? 203.129 158.756 152.660 1.00 41.83  ? 1608 LEU A CB    1 
ATOM   2356  C  CG    . LEU A 1 1608 ? 203.804 157.440 153.057 1.00 40.55  ? 1608 LEU A CG    1 
ATOM   2357  C  CD1   . LEU A 1 1608 ? 202.987 156.723 154.113 1.00 40.17  ? 1608 LEU A CD1   1 
ATOM   2358  C  CD2   . LEU A 1 1608 ? 203.992 156.552 151.842 1.00 41.61  ? 1608 LEU A CD2   1 
ATOM   2359  N  N     . GLY A 1 1609 ? 202.573 161.670 151.427 1.00 42.37  ? 1609 GLY A N     1 
ATOM   2360  C  CA    . GLY A 1 1609 ? 201.681 162.639 150.764 1.00 41.83  ? 1609 GLY A CA    1 
ATOM   2361  C  C     . GLY A 1 1609 ? 202.274 163.098 149.449 1.00 46.42  ? 1609 GLY A C     1 
ATOM   2362  O  O     . GLY A 1 1609 ? 201.509 163.232 148.474 1.00 55.37  ? 1609 GLY A O     1 
ATOM   2363  N  N     . LYS A 1 1610 ? 203.591 163.320 149.415 1.00 45.87  ? 1610 LYS A N     1 
ATOM   2364  C  CA    . LYS A 1 1610 ? 204.273 163.755 148.169 1.00 47.27  ? 1610 LYS A CA    1 
ATOM   2365  C  C     . LYS A 1 1610 ? 204.096 162.681 147.084 1.00 49.14  ? 1610 LYS A C     1 
ATOM   2366  O  O     . LYS A 1 1610 ? 203.740 163.047 145.946 1.00 51.05  ? 1610 LYS A O     1 
ATOM   2367  C  CB    . LYS A 1 1610 ? 205.764 163.997 148.425 1.00 30.00  ? 1610 LYS A CB    1 
ATOM   2368  C  CG    . LYS A 1 1610 ? 206.094 165.167 149.336 1.00 30.00  ? 1610 LYS A CG    1 
ATOM   2369  C  CD    . LYS A 1 1610 ? 207.580 165.233 149.664 1.00 30.00  ? 1610 LYS A CD    1 
ATOM   2370  C  CE    . LYS A 1 1610 ? 207.949 166.463 150.427 1.00 30.00  ? 1610 LYS A CE    1 
ATOM   2371  N  NZ    . LYS A 1 1610 ? 209.359 166.446 150.823 1.00 30.00  ? 1610 LYS A NZ    1 
ATOM   2372  N  N     . ILE A 1 1611 ? 204.336 161.413 147.426 1.00 47.13  ? 1611 ILE A N     1 
ATOM   2373  C  CA    . ILE A 1 1611 ? 204.221 160.308 146.426 1.00 42.69  ? 1611 ILE A CA    1 
ATOM   2374  C  C     . ILE A 1 1611 ? 202.761 160.218 145.958 1.00 45.21  ? 1611 ILE A C     1 
ATOM   2375  O  O     . ILE A 1 1611 ? 202.540 160.088 144.737 1.00 54.68  ? 1611 ILE A O     1 
ATOM   2376  C  CB    . ILE A 1 1611 ? 204.708 158.972 147.011 1.00 41.18  ? 1611 ILE A CB    1 
ATOM   2377  C  CG1   . ILE A 1 1611 ? 206.116 159.087 147.578 1.00 48.77  ? 1611 ILE A CG1   1 
ATOM   2378  C  CG2   . ILE A 1 1611 ? 204.614 157.854 145.973 1.00 43.22  ? 1611 ILE A CG2   1 
ATOM   2379  C  CD1   . ILE A 1 1611 ? 206.674 157.773 148.086 1.00 48.29  ? 1611 ILE A CD1   1 
ATOM   2380  N  N     . GLN A 1 1612 ? 201.811 160.294 146.893 1.00 44.17  ? 1612 GLN A N     1 
ATOM   2381  C  CA    . GLN A 1 1612 ? 200.373 160.191 146.534 1.00 44.29  ? 1612 GLN A CA    1 
ATOM   2382  C  C     . GLN A 1 1612 ? 200.019 161.351 145.593 1.00 46.53  ? 1612 GLN A C     1 
ATOM   2383  O  O     . GLN A 1 1612 ? 199.252 161.122 144.635 1.00 49.42  ? 1612 GLN A O     1 
ATOM   2384  C  CB    . GLN A 1 1612 ? 199.508 160.207 147.792 1.00 43.46  ? 1612 GLN A CB    1 
ATOM   2385  C  CG    . GLN A 1 1612 ? 198.074 159.742 147.563 1.00 49.85  ? 1612 GLN A CG    1 
ATOM   2386  C  CD    . GLN A 1 1612 ? 197.293 159.579 148.848 1.00 62.30  ? 1612 GLN A CD    1 
ATOM   2387  O  OE1   . GLN A 1 1612 ? 197.803 159.825 149.946 1.00 66.29  ? 1612 GLN A OE1   1 
ATOM   2388  N  NE2   . GLN A 1 1612 ? 196.042 159.162 148.721 1.00 64.35  ? 1612 GLN A NE2   1 
ATOM   2389  N  N     . LYS A 1 1613 ? 200.558 162.543 145.860 1.00 46.41  ? 1613 LYS A N     1 
ATOM   2390  C  CA    . LYS A 1 1613 ? 200.312 163.716 144.982 1.00 44.84  ? 1613 LYS A CA    1 
ATOM   2391  C  C     . LYS A 1 1613 ? 200.978 163.475 143.621 1.00 47.85  ? 1613 LYS A C     1 
ATOM   2392  O  O     . LYS A 1 1613 ? 200.312 163.697 142.591 1.00 51.64  ? 1613 LYS A O     1 
ATOM   2393  C  CB    . LYS A 1 1613 ? 200.867 164.978 145.650 1.00 52.63  ? 1613 LYS A CB    1 
ATOM   2394  C  CG    . LYS A 1 1613 ? 200.892 166.235 144.797 1.00 59.87  ? 1613 LYS A CG    1 
ATOM   2395  C  CD    . LYS A 1 1613 ? 201.565 167.396 145.519 1.00 62.25  ? 1613 LYS A CD    1 
ATOM   2396  C  CE    . LYS A 1 1613 ? 201.588 168.653 144.712 1.00 71.86  ? 1613 LYS A CE    1 
ATOM   2397  N  NZ    . LYS A 1 1613 ? 202.271 169.737 145.423 1.00 77.89  ? 1613 LYS A NZ    1 
ATOM   2398  N  N     . ALA A 1 1614 ? 202.237 163.030 143.624 1.00 48.85  ? 1614 ALA A N     1 
ATOM   2399  C  CA    . ALA A 1 1614 ? 202.961 162.753 142.361 1.00 48.79  ? 1614 ALA A CA    1 
ATOM   2400  C  C     . ALA A 1 1614 ? 202.173 161.731 141.545 1.00 47.31  ? 1614 ALA A C     1 
ATOM   2401  O  O     . ALA A 1 1614 ? 202.148 161.842 140.302 1.00 53.02  ? 1614 ALA A O     1 
ATOM   2402  C  CB    . ALA A 1 1614 ? 204.356 162.261 142.662 1.00 51.18  ? 1614 ALA A CB    1 
ATOM   2403  N  N     . LEU A 1 1615 ? 201.551 160.765 142.222 1.00 46.14  ? 1615 LEU A N     1 
ATOM   2404  C  CA    . LEU A 1 1615 ? 200.727 159.785 141.519 1.00 44.89  ? 1615 LEU A CA    1 
ATOM   2405  C  C     . LEU A 1 1615 ? 199.449 160.420 140.984 1.00 45.18  ? 1615 LEU A C     1 
ATOM   2406  O  O     . LEU A 1 1615 ? 199.032 160.141 139.852 1.00 51.44  ? 1615 LEU A O     1 
ATOM   2407  C  CB    . LEU A 1 1615 ? 200.399 158.614 142.442 1.00 43.92  ? 1615 LEU A CB    1 
ATOM   2408  C  CG    . LEU A 1 1615 ? 199.325 157.650 141.940 1.00 42.03  ? 1615 LEU A CG    1 
ATOM   2409  C  CD1   . LEU A 1 1615 ? 199.827 156.867 140.740 1.00 39.14  ? 1615 LEU A CD1   1 
ATOM   2410  C  CD2   . LEU A 1 1615 ? 198.892 156.713 143.051 1.00 50.53  ? 1615 LEU A CD2   1 
ATOM   2411  N  N     . GLY A 1 1616 ? 198.810 161.273 141.786 1.00 45.64  ? 1616 GLY A N     1 
ATOM   2412  C  CA    . GLY A 1 1616 ? 197.623 161.965 141.313 1.00 41.24  ? 1616 GLY A CA    1 
ATOM   2413  C  C     . GLY A 1 1616 ? 197.911 162.876 140.137 1.00 43.15  ? 1616 GLY A C     1 
ATOM   2414  O  O     . GLY A 1 1616 ? 197.118 162.963 139.198 1.00 53.02  ? 1616 GLY A O     1 
ATOM   2415  N  N     . GLU A 1 1617 ? 199.052 163.566 140.170 1.00 41.99  ? 1617 GLU A N     1 
ATOM   2416  C  CA    . GLU A 1 1617 ? 199.437 164.412 139.047 1.00 45.76  ? 1617 GLU A CA    1 
ATOM   2417  C  C     . GLU A 1 1617 ? 199.699 163.585 137.798 1.00 48.97  ? 1617 GLU A C     1 
ATOM   2418  O  O     . GLU A 1 1617 ? 199.352 164.001 136.688 1.00 58.13  ? 1617 GLU A O     1 
ATOM   2419  C  CB    . GLU A 1 1617 ? 200.669 165.241 139.406 1.00 53.08  ? 1617 GLU A CB    1 
ATOM   2420  C  CG    . GLU A 1 1617 ? 200.407 166.330 140.427 1.00 57.55  ? 1617 GLU A CG    1 
ATOM   2421  C  CD    . GLU A 1 1617 ? 201.628 167.185 140.684 1.00 72.46  ? 1617 GLU A CD    1 
ATOM   2422  O  OE1   . GLU A 1 1617 ? 202.686 166.909 140.081 1.00 77.64  ? 1617 GLU A OE1   1 
ATOM   2423  O  OE2   . GLU A 1 1617 ? 201.529 168.136 141.487 1.00 76.09  ? 1617 GLU A OE2   1 
ATOM   2424  N  N     . TYR A 1 1618 ? 200.325 162.417 137.954 1.00 48.44  ? 1618 TYR A N     1 
ATOM   2425  C  CA    . TYR A 1 1618 ? 200.545 161.544 136.805 1.00 46.76  ? 1618 TYR A CA    1 
ATOM   2426  C  C     . TYR A 1 1618 ? 199.223 161.073 136.211 1.00 46.20  ? 1618 TYR A C     1 
ATOM   2427  O  O     . TYR A 1 1618 ? 199.049 161.062 134.985 1.00 50.44  ? 1618 TYR A O     1 
ATOM   2428  C  CB    . TYR A 1 1618 ? 201.412 160.353 137.213 1.00 47.41  ? 1618 TYR A CB    1 
ATOM   2429  C  CG    . TYR A 1 1618 ? 201.655 159.355 136.106 1.00 51.76  ? 1618 TYR A CG    1 
ATOM   2430  C  CD1   . TYR A 1 1618 ? 202.718 159.511 135.230 1.00 58.28  ? 1618 TYR A CD1   1 
ATOM   2431  C  CD2   . TYR A 1 1618 ? 200.834 158.247 135.949 1.00 51.21  ? 1618 TYR A CD2   1 
ATOM   2432  C  CE1   . TYR A 1 1618 ? 202.948 158.601 134.219 1.00 59.42  ? 1618 TYR A CE1   1 
ATOM   2433  C  CE2   . TYR A 1 1618 ? 201.057 157.333 134.943 1.00 56.33  ? 1618 TYR A CE2   1 
ATOM   2434  C  CZ    . TYR A 1 1618 ? 202.115 157.515 134.081 1.00 61.73  ? 1618 TYR A CZ    1 
ATOM   2435  O  OH    . TYR A 1 1618 ? 202.342 156.605 133.076 1.00 72.07  ? 1618 TYR A OH    1 
ATOM   2436  N  N     . LEU A 1 1619 ? 198.276 160.685 137.068 1.00 46.59  ? 1619 LEU A N     1 
ATOM   2437  C  CA    . LEU A 1 1619 ? 196.964 160.274 136.576 1.00 41.55  ? 1619 LEU A CA    1 
ATOM   2438  C  C     . LEU A 1 1619 ? 196.253 161.425 135.876 1.00 46.13  ? 1619 LEU A C     1 
ATOM   2439  O  O     . LEU A 1 1619 ? 195.608 161.227 134.841 1.00 54.10  ? 1619 LEU A O     1 
ATOM   2440  C  CB    . LEU A 1 1619 ? 196.108 159.737 137.722 1.00 40.80  ? 1619 LEU A CB    1 
ATOM   2441  C  CG    . LEU A 1 1619 ? 196.568 158.431 138.367 1.00 48.55  ? 1619 LEU A CG    1 
ATOM   2442  C  CD1   . LEU A 1 1619 ? 195.612 158.025 139.475 1.00 53.06  ? 1619 LEU A CD1   1 
ATOM   2443  C  CD2   . LEU A 1 1619 ? 196.695 157.332 137.330 1.00 40.18  ? 1619 LEU A CD2   1 
ATOM   2444  N  N     . GLU A 1 1620 ? 196.356 162.636 136.427 1.00 46.42  ? 1620 GLU A N     1 
ATOM   2445  C  CA    . GLU A 1 1620 ? 195.725 163.790 135.796 1.00 43.69  ? 1620 GLU A CA    1 
ATOM   2446  C  C     . GLU A 1 1620 ? 196.367 164.105 134.450 1.00 46.57  ? 1620 GLU A C     1 
ATOM   2447  O  O     . GLU A 1 1620 ? 195.675 164.496 133.507 1.00 53.87  ? 1620 GLU A O     1 
ATOM   2448  C  CB    . GLU A 1 1620 ? 195.793 165.000 136.724 1.00 48.89  ? 1620 GLU A CB    1 
ATOM   2449  C  CG    . GLU A 1 1620 ? 194.904 166.162 136.305 1.00 63.65  ? 1620 GLU A CG    1 
ATOM   2450  C  CD    . GLU A 1 1620 ? 195.570 167.082 135.301 1.00 75.90  ? 1620 GLU A CD    1 
ATOM   2451  O  OE1   . GLU A 1 1620 ? 196.815 167.185 135.321 1.00 77.48  ? 1620 GLU A OE1   1 
ATOM   2452  O  OE2   . GLU A 1 1620 ? 194.849 167.702 134.492 1.00 71.95  ? 1620 GLU A OE2   1 
ATOM   2453  N  N     . ARG A 1 1621 ? 197.688 163.953 134.343 1.00 46.69  ? 1621 ARG A N     1 
ATOM   2454  C  CA    . ARG A 1 1621 ? 198.354 164.164 133.062 1.00 46.24  ? 1621 ARG A CA    1 
ATOM   2455  C  C     . ARG A 1 1621 ? 197.906 163.136 132.031 1.00 48.16  ? 1621 ARG A C     1 
ATOM   2456  O  O     . ARG A 1 1621 ? 197.664 163.478 130.866 1.00 51.08  ? 1621 ARG A O     1 
ATOM   2457  C  CB    . ARG A 1 1621 ? 199.870 164.114 133.244 1.00 49.89  ? 1621 ARG A CB    1 
ATOM   2458  C  CG    . ARG A 1 1621 ? 200.496 165.448 133.607 1.00 60.15  ? 1621 ARG A CG    1 
ATOM   2459  C  CD    . ARG A 1 1621 ? 202.010 165.399 133.483 1.00 65.75  ? 1621 ARG A CD    1 
ATOM   2460  N  NE    . ARG A 1 1621 ? 202.580 164.269 134.205 1.00 67.85  ? 1621 ARG A NE    1 
ATOM   2461  C  CZ    . ARG A 1 1621 ? 202.962 164.306 135.474 1.00 66.04  ? 1621 ARG A CZ    1 
ATOM   2462  N  NH1   . ARG A 1 1621 ? 202.847 165.407 136.198 1.00 61.51  ? 1621 ARG A NH1   1 
ATOM   2463  N  NH2   . ARG A 1 1621 ? 203.470 163.211 136.032 1.00 59.23  ? 1621 ARG A NH2   1 
ATOM   2464  N  N     . GLU A 1 1622 ? 197.790 161.870 132.441 1.00 46.28  ? 1622 GLU A N     1 
ATOM   2465  C  CA    . GLU A 1 1622 ? 197.296 160.844 131.527 1.00 42.65  ? 1622 GLU A CA    1 
ATOM   2466  C  C     . GLU A 1 1622 ? 195.865 161.135 131.095 1.00 43.69  ? 1622 GLU A C     1 
ATOM   2467  O  O     . GLU A 1 1622 ? 195.510 160.944 129.926 1.00 45.01  ? 1622 GLU A O     1 
ATOM   2468  C  CB    . GLU A 1 1622 ? 197.389 159.464 132.175 1.00 41.92  ? 1622 GLU A CB    1 
ATOM   2469  C  CG    . GLU A 1 1622 ? 198.807 159.013 132.460 1.00 56.74  ? 1622 GLU A CG    1 
ATOM   2470  C  CD    . GLU A 1 1622 ? 199.668 158.976 131.214 1.00 62.09  ? 1622 GLU A CD    1 
ATOM   2471  O  OE1   . GLU A 1 1622 ? 199.379 158.158 130.316 1.00 61.14  ? 1622 GLU A OE1   1 
ATOM   2472  O  OE2   . GLU A 1 1622 ? 200.632 159.765 131.133 1.00 58.87  ? 1622 GLU A OE2   1 
ATOM   2473  N  N     . ARG A 1 1623 ? 195.027 161.592 132.027 1.00 41.16  ? 1623 ARG A N     1 
ATOM   2474  C  CA    . ARG A 1 1623 ? 193.655 161.949 131.684 1.00 32.23  ? 1623 ARG A CA    1 
ATOM   2475  C  C     . ARG A 1 1623 ? 193.614 163.135 130.729 1.00 36.95  ? 1623 ARG A C     1 
ATOM   2476  O  O     . ARG A 1 1623 ? 192.783 163.178 129.817 1.00 46.87  ? 1623 ARG A O     1 
ATOM   2477  C  CB    . ARG A 1 1623 ? 192.863 162.258 132.952 1.00 30.29  ? 1623 ARG A CB    1 
ATOM   2478  C  CG    . ARG A 1 1623 ? 192.453 161.035 133.749 1.00 31.12  ? 1623 ARG A CG    1 
ATOM   2479  C  CD    . ARG A 1 1623 ? 191.121 161.270 134.427 1.00 33.46  ? 1623 ARG A CD    1 
ATOM   2480  N  NE    . ARG A 1 1623 ? 190.608 160.078 135.089 1.00 32.83  ? 1623 ARG A NE    1 
ATOM   2481  C  CZ    . ARG A 1 1623 ? 190.997 159.657 136.283 1.00 39.66  ? 1623 ARG A CZ    1 
ATOM   2482  N  NH1   . ARG A 1 1623 ? 191.906 160.313 136.984 1.00 48.56  ? 1623 ARG A NH1   1 
ATOM   2483  N  NH2   . ARG A 1 1623 ? 190.455 158.555 136.789 1.00 46.97  ? 1623 ARG A NH2   1 
ATOM   2484  N  N     . SER A 1 1624 ? 194.493 164.116 130.932 1.00 38.32  ? 1624 SER A N     1 
ATOM   2485  C  CA    . SER A 1 1624 ? 194.523 165.281 130.056 1.00 40.13  ? 1624 SER A CA    1 
ATOM   2486  C  C     . SER A 1 1624 ? 194.974 164.908 128.651 1.00 43.97  ? 1624 SER A C     1 
ATOM   2487  O  O     . SER A 1 1624 ? 194.471 165.462 127.667 1.00 52.91  ? 1624 SER A O     1 
ATOM   2488  C  CB    . SER A 1 1624 ? 195.436 166.356 130.643 1.00 43.44  ? 1624 SER A CB    1 
ATOM   2489  O  OG    . SER A 1 1624 ? 194.943 166.816 131.889 1.00 51.09  ? 1624 SER A OG    1 
ATOM   2490  N  N     . SER A 1 1625 ? 195.932 163.986 128.535 1.00 41.96  ? 1625 SER A N     1 
ATOM   2491  C  CA    . SER A 1 1625 ? 196.379 163.558 127.212 1.00 40.47  ? 1625 SER A CA    1 
ATOM   2492  C  C     . SER A 1 1625 ? 195.264 162.850 126.449 1.00 42.23  ? 1625 SER A C     1 
ATOM   2493  O  O     . SER A 1 1625 ? 195.085 163.075 125.247 1.00 42.24  ? 1625 SER A O     1 
ATOM   2494  C  CB    . SER A 1 1625 ? 197.603 162.655 127.340 1.00 41.63  ? 1625 SER A CB    1 
ATOM   2495  O  OG    . SER A 1 1625 ? 198.756 163.408 127.671 1.00 52.92  ? 1625 SER A OG    1 
ATOM   2496  N  N     . PHE A 1 1626 ? 194.509 161.989 127.126 1.00 39.78  ? 1626 PHE A N     1 
ATOM   2497  C  CA    . PHE A 1 1626 ? 193.373 161.286 126.529 1.00 31.78  ? 1626 PHE A CA    1 
ATOM   2498  C  C     . PHE A 1 1626 ? 192.121 161.613 127.329 1.00 33.18  ? 1626 PHE A C     1 
ATOM   2499  O  O     . PHE A 1 1626 ? 191.829 160.936 128.331 1.00 32.77  ? 1626 PHE A O     1 
ATOM   2500  C  CB    . PHE A 1 1626 ? 193.618 159.779 126.500 1.00 31.83  ? 1626 PHE A CB    1 
ATOM   2501  C  CG    . PHE A 1 1626 ? 192.666 159.024 125.620 1.00 31.98  ? 1626 PHE A CG    1 
ATOM   2502  C  CD1   . PHE A 1 1626 ? 192.659 159.224 124.253 1.00 36.93  ? 1626 PHE A CD1   1 
ATOM   2503  C  CD2   . PHE A 1 1626 ? 191.778 158.113 126.160 1.00 30.68  ? 1626 PHE A CD2   1 
ATOM   2504  C  CE1   . PHE A 1 1626 ? 191.786 158.529 123.443 1.00 32.90  ? 1626 PHE A CE1   1 
ATOM   2505  C  CE2   . PHE A 1 1626 ? 190.903 157.417 125.355 1.00 29.41  ? 1626 PHE A CE2   1 
ATOM   2506  C  CZ    . PHE A 1 1626 ? 190.906 157.626 123.996 1.00 29.86  ? 1626 PHE A CZ    1 
ATOM   2507  N  N     . PRO A 1 1627 ? 191.351 162.629 126.930 1.00 33.39  ? 1627 PRO A N     1 
ATOM   2508  C  CA    . PRO A 1 1627 ? 190.247 163.101 127.784 1.00 28.68  ? 1627 PRO A CA    1 
ATOM   2509  C  C     . PRO A 1 1627 ? 189.199 162.049 128.098 1.00 30.67  ? 1627 PRO A C     1 
ATOM   2510  O  O     . PRO A 1 1627 ? 188.557 162.133 129.152 1.00 33.75  ? 1627 PRO A O     1 
ATOM   2511  C  CB    . PRO A 1 1627 ? 189.655 164.255 126.967 1.00 35.76  ? 1627 PRO A CB    1 
ATOM   2512  C  CG    . PRO A 1 1627 ? 190.777 164.723 126.115 1.00 40.25  ? 1627 PRO A CG    1 
ATOM   2513  C  CD    . PRO A 1 1627 ? 191.545 163.491 125.754 1.00 37.69  ? 1627 PRO A CD    1 
ATOM   2514  N  N     . ARG A 1 1628 ? 188.999 161.061 127.225 1.00 33.13  ? 1628 ARG A N     1 
ATOM   2515  C  CA    . ARG A 1 1628 ? 188.017 160.019 127.503 1.00 28.70  ? 1628 ARG A CA    1 
ATOM   2516  C  C     . ARG A 1 1628 ? 188.340 159.234 128.766 1.00 30.61  ? 1628 ARG A C     1 
ATOM   2517  O  O     . ARG A 1 1628 ? 187.432 158.634 129.354 1.00 31.68  ? 1628 ARG A O     1 
ATOM   2518  C  CB    . ARG A 1 1628 ? 187.908 159.072 126.310 1.00 28.57  ? 1628 ARG A CB    1 
ATOM   2519  C  CG    . ARG A 1 1628 ? 187.197 159.679 125.115 1.00 28.38  ? 1628 ARG A CG    1 
ATOM   2520  C  CD    . ARG A 1 1628 ? 187.232 158.750 123.918 1.00 32.89  ? 1628 ARG A CD    1 
ATOM   2521  N  NE    . ARG A 1 1628 ? 186.529 159.307 122.768 1.00 33.10  ? 1628 ARG A NE    1 
ATOM   2522  C  CZ    . ARG A 1 1628 ? 185.210 159.382 122.656 1.00 34.83  ? 1628 ARG A CZ    1 
ATOM   2523  N  NH1   . ARG A 1 1628 ? 184.408 158.935 123.608 1.00 32.99  ? 1628 ARG A NH1   1 
ATOM   2524  N  NH2   . ARG A 1 1628 ? 184.682 159.915 121.559 1.00 36.97  ? 1628 ARG A NH2   1 
ATOM   2525  N  N     . PHE A 1 1629 ? 189.597 159.252 129.215 1.00 31.29  ? 1629 PHE A N     1 
ATOM   2526  C  CA    . PHE A 1 1629 ? 189.968 158.616 130.471 1.00 27.38  ? 1629 PHE A CA    1 
ATOM   2527  C  C     . PHE A 1 1629 ? 189.281 159.245 131.671 1.00 27.57  ? 1629 PHE A C     1 
ATOM   2528  O  O     . PHE A 1 1629 ? 189.287 158.645 132.749 1.00 32.44  ? 1629 PHE A O     1 
ATOM   2529  C  CB    . PHE A 1 1629 ? 191.481 158.671 130.668 1.00 26.13  ? 1629 PHE A CB    1 
ATOM   2530  C  CG    . PHE A 1 1629 ? 192.217 157.569 129.976 1.00 27.81  ? 1629 PHE A CG    1 
ATOM   2531  C  CD1   . PHE A 1 1629 ? 191.682 156.296 129.918 1.00 27.03  ? 1629 PHE A CD1   1 
ATOM   2532  C  CD2   . PHE A 1 1629 ? 193.454 157.795 129.407 1.00 30.04  ? 1629 PHE A CD2   1 
ATOM   2533  C  CE1   . PHE A 1 1629 ? 192.357 155.279 129.289 1.00 34.42  ? 1629 PHE A CE1   1 
ATOM   2534  C  CE2   . PHE A 1 1629 ? 194.132 156.779 128.777 1.00 32.98  ? 1629 PHE A CE2   1 
ATOM   2535  C  CZ    . PHE A 1 1629 ? 193.585 155.521 128.719 1.00 38.30  ? 1629 PHE A CZ    1 
ATOM   2536  N  N     . TYR A 1 1630 ? 188.704 160.436 131.518 1.00 27.96  ? 1630 TYR A N     1 
ATOM   2537  C  CA    . TYR A 1 1630 ? 187.902 161.009 132.587 1.00 26.42  ? 1630 TYR A CA    1 
ATOM   2538  C  C     . TYR A 1 1630 ? 186.640 160.204 132.861 1.00 32.85  ? 1630 TYR A C     1 
ATOM   2539  O  O     . TYR A 1 1630 ? 186.002 160.423 133.895 1.00 38.32  ? 1630 TYR A O     1 
ATOM   2540  C  CB    . TYR A 1 1630 ? 187.522 162.446 132.244 1.00 24.86  ? 1630 TYR A CB    1 
ATOM   2541  C  CG    . TYR A 1 1630 ? 188.609 163.467 132.490 1.00 29.54  ? 1630 TYR A CG    1 
ATOM   2542  C  CD1   . TYR A 1 1630 ? 188.899 163.908 133.771 1.00 31.83  ? 1630 TYR A CD1   1 
ATOM   2543  C  CD2   . TYR A 1 1630 ? 189.331 164.002 131.435 1.00 29.64  ? 1630 TYR A CD2   1 
ATOM   2544  C  CE1   . TYR A 1 1630 ? 189.886 164.843 133.994 1.00 33.12  ? 1630 TYR A CE1   1 
ATOM   2545  C  CE2   . TYR A 1 1630 ? 190.317 164.938 131.649 1.00 33.78  ? 1630 TYR A CE2   1 
ATOM   2546  C  CZ    . TYR A 1 1630 ? 190.591 165.356 132.929 1.00 36.23  ? 1630 TYR A CZ    1 
ATOM   2547  O  OH    . TYR A 1 1630 ? 191.576 166.290 133.143 1.00 49.08  ? 1630 TYR A OH    1 
ATOM   2548  N  N     . PHE A 1 1631 ? 186.262 159.290 131.968 1.00 31.16  ? 1631 PHE A N     1 
ATOM   2549  C  CA    . PHE A 1 1631 ? 185.069 158.479 132.166 1.00 28.30  ? 1631 PHE A CA    1 
ATOM   2550  C  C     . PHE A 1 1631 ? 185.334 157.192 132.936 1.00 37.73  ? 1631 PHE A C     1 
ATOM   2551  O  O     . PHE A 1 1631 ? 184.382 156.463 133.232 1.00 46.93  ? 1631 PHE A O     1 
ATOM   2552  C  CB    . PHE A 1 1631 ? 184.426 158.143 130.818 1.00 27.13  ? 1631 PHE A CB    1 
ATOM   2553  C  CG    . PHE A 1 1631 ? 184.010 159.350 130.029 1.00 27.74  ? 1631 PHE A CG    1 
ATOM   2554  C  CD1   . PHE A 1 1631 ? 183.151 160.284 130.574 1.00 32.46  ? 1631 PHE A CD1   1 
ATOM   2555  C  CD2   . PHE A 1 1631 ? 184.469 159.545 128.741 1.00 27.56  ? 1631 PHE A CD2   1 
ATOM   2556  C  CE1   . PHE A 1 1631 ? 182.767 161.391 129.854 1.00 32.35  ? 1631 PHE A CE1   1 
ATOM   2557  C  CE2   . PHE A 1 1631 ? 184.084 160.650 128.017 1.00 28.84  ? 1631 PHE A CE2   1 
ATOM   2558  C  CZ    . PHE A 1 1631 ? 183.233 161.573 128.574 1.00 29.55  ? 1631 PHE A CZ    1 
ATOM   2559  N  N     . VAL A 1 1632 ? 186.588 156.896 133.271 1.00 37.73  ? 1632 VAL A N     1 
ATOM   2560  C  CA    . VAL A 1 1632 ? 186.940 155.721 134.057 1.00 38.45  ? 1632 VAL A CA    1 
ATOM   2561  C  C     . VAL A 1 1632 ? 187.576 156.183 135.360 1.00 41.55  ? 1632 VAL A C     1 
ATOM   2562  O  O     . VAL A 1 1632 ? 188.244 157.221 135.403 1.00 40.23  ? 1632 VAL A O     1 
ATOM   2563  C  CB    . VAL A 1 1632 ? 187.886 154.772 133.289 1.00 35.95  ? 1632 VAL A CB    1 
ATOM   2564  C  CG1   . VAL A 1 1632 ? 187.169 154.161 132.102 1.00 37.08  ? 1632 VAL A CG1   1 
ATOM   2565  C  CG2   . VAL A 1 1632 ? 189.133 155.500 132.836 1.00 32.66  ? 1632 VAL A CG2   1 
ATOM   2566  N  N     . GLY A 1 1633 ? 187.364 155.412 136.421 1.00 44.57  ? 1633 GLY A N     1 
ATOM   2567  C  CA    . GLY A 1 1633 ? 187.867 155.769 137.729 1.00 45.17  ? 1633 GLY A CA    1 
ATOM   2568  C  C     . GLY A 1 1633 ? 189.367 155.578 137.845 1.00 49.93  ? 1633 GLY A C     1 
ATOM   2569  O  O     . GLY A 1 1633 ? 190.055 155.141 136.922 1.00 53.96  ? 1633 GLY A O     1 
ATOM   2570  N  N     . ASP A 1 1634 ? 189.884 155.926 139.026 1.00 52.36  ? 1634 ASP A N     1 
ATOM   2571  C  CA    . ASP A 1 1634 ? 191.321 155.831 139.260 1.00 53.40  ? 1634 ASP A CA    1 
ATOM   2572  C  C     . ASP A 1 1634 ? 191.804 154.388 139.196 1.00 55.30  ? 1634 ASP A C     1 
ATOM   2573  O  O     . ASP A 1 1634 ? 192.871 154.111 138.640 1.00 54.48  ? 1634 ASP A O     1 
ATOM   2574  C  CB    . ASP A 1 1634 ? 191.680 156.456 140.607 1.00 64.00  ? 1634 ASP A CB    1 
ATOM   2575  C  CG    . ASP A 1 1634 ? 191.754 157.966 140.544 1.00 68.49  ? 1634 ASP A CG    1 
ATOM   2576  O  OD1   . ASP A 1 1634 ? 191.920 158.507 139.431 1.00 59.92  ? 1634 ASP A OD1   1 
ATOM   2577  O  OD2   . ASP A 1 1634 ? 191.652 158.612 141.608 1.00 76.79  ? 1634 ASP A OD2   1 
ATOM   2578  N  N     . GLU A 1 1635 ? 191.041 153.455 139.770 1.00 56.98  ? 1635 GLU A N     1 
ATOM   2579  C  CA    . GLU A 1 1635 ? 191.426 152.049 139.694 1.00 55.21  ? 1635 GLU A CA    1 
ATOM   2580  C  C     . GLU A 1 1635 ? 191.377 151.537 138.258 1.00 55.26  ? 1635 GLU A C     1 
ATOM   2581  O  O     . GLU A 1 1635 ? 192.292 150.832 137.813 1.00 57.39  ? 1635 GLU A O     1 
ATOM   2582  C  CB    . GLU A 1 1635 ? 190.535 151.212 140.616 1.00 51.31  ? 1635 GLU A CB    1 
ATOM   2583  C  CG    . GLU A 1 1635 ? 189.059 151.203 140.250 1.00 63.56  ? 1635 GLU A CG    1 
ATOM   2584  C  CD    . GLU A 1 1635 ? 188.248 152.180 141.078 1.00 74.82  ? 1635 GLU A CD    1 
ATOM   2585  O  OE1   . GLU A 1 1635 ? 188.851 153.091 141.683 1.00 73.25  ? 1635 GLU A OE1   1 
ATOM   2586  O  OE2   . GLU A 1 1635 ? 187.008 152.041 141.119 1.00 76.80  ? 1635 GLU A OE2   1 
ATOM   2587  N  N     . ASP A 1 1636 ? 190.335 151.905 137.507 1.00 50.78  ? 1636 ASP A N     1 
ATOM   2588  C  CA    . ASP A 1 1636 ? 190.247 151.499 136.109 1.00 47.59  ? 1636 ASP A CA    1 
ATOM   2589  C  C     . ASP A 1 1636 ? 191.353 152.135 135.277 1.00 47.09  ? 1636 ASP A C     1 
ATOM   2590  O  O     . ASP A 1 1636 ? 191.943 151.477 134.414 1.00 55.26  ? 1636 ASP A O     1 
ATOM   2591  C  CB    . ASP A 1 1636 ? 188.876 151.861 135.542 1.00 50.57  ? 1636 ASP A CB    1 
ATOM   2592  C  CG    . ASP A 1 1636 ? 187.738 151.323 136.383 1.00 60.18  ? 1636 ASP A CG    1 
ATOM   2593  O  OD1   . ASP A 1 1636 ? 187.680 150.093 136.591 1.00 65.17  ? 1636 ASP A OD1   1 
ATOM   2594  O  OD2   . ASP A 1 1636 ? 186.898 152.128 136.835 1.00 61.15  ? 1636 ASP A OD2   1 
ATOM   2595  N  N     . LEU A 1 1637 ? 191.644 153.413 135.518 1.00 44.35  ? 1637 LEU A N     1 
ATOM   2596  C  CA    . LEU A 1 1637 ? 192.715 154.084 134.788 1.00 42.36  ? 1637 LEU A CA    1 
ATOM   2597  C  C     . LEU A 1 1637 ? 194.066 153.444 135.085 1.00 52.51  ? 1637 LEU A C     1 
ATOM   2598  O  O     . LEU A 1 1637 ? 194.890 153.248 134.181 1.00 58.08  ? 1637 LEU A O     1 
ATOM   2599  C  CB    . LEU A 1 1637 ? 192.722 155.569 135.150 1.00 38.62  ? 1637 LEU A CB    1 
ATOM   2600  C  CG    . LEU A 1 1637 ? 193.730 156.494 134.477 1.00 35.43  ? 1637 LEU A CG    1 
ATOM   2601  C  CD1   . LEU A 1 1637 ? 193.317 156.721 133.054 1.00 40.79  ? 1637 LEU A CD1   1 
ATOM   2602  C  CD2   . LEU A 1 1637 ? 193.807 157.812 135.212 1.00 46.34  ? 1637 LEU A CD2   1 
ATOM   2603  N  N     . LEU A 1 1638 ? 194.312 153.115 136.354 1.00 56.83  ? 1638 LEU A N     1 
ATOM   2604  C  CA    . LEU A 1 1638 ? 195.558 152.455 136.724 1.00 54.26  ? 1638 LEU A CA    1 
ATOM   2605  C  C     . LEU A 1 1638 ? 195.655 151.080 136.085 1.00 57.04  ? 1638 LEU A C     1 
ATOM   2606  O  O     . LEU A 1 1638 ? 196.737 150.657 135.670 1.00 65.36  ? 1638 LEU A O     1 
ATOM   2607  C  CB    . LEU A 1 1638 ? 195.663 152.357 138.243 1.00 51.21  ? 1638 LEU A CB    1 
ATOM   2608  C  CG    . LEU A 1 1638 ? 196.189 153.621 138.923 1.00 51.32  ? 1638 LEU A CG    1 
ATOM   2609  C  CD1   . LEU A 1 1638 ? 196.105 153.489 140.425 1.00 53.57  ? 1638 LEU A CD1   1 
ATOM   2610  C  CD2   . LEU A 1 1638 ? 197.619 153.900 138.490 1.00 51.74  ? 1638 LEU A CD2   1 
ATOM   2611  N  N     . GLU A 1 1639 ? 194.531 150.368 135.993 1.00 55.76  ? 1639 GLU A N     1 
ATOM   2612  C  CA    . GLU A 1 1639 ? 194.521 149.100 135.272 1.00 55.95  ? 1639 GLU A CA    1 
ATOM   2613  C  C     . GLU A 1 1639 ? 194.845 149.302 133.796 1.00 59.71  ? 1639 GLU A C     1 
ATOM   2614  O  O     . GLU A 1 1639 ? 195.577 148.505 133.199 1.00 66.96  ? 1639 GLU A O     1 
ATOM   2615  C  CB    . GLU A 1 1639 ? 193.164 148.421 135.436 1.00 53.12  ? 1639 GLU A CB    1 
ATOM   2616  C  CG    . GLU A 1 1639 ? 192.977 147.187 134.579 1.00 65.53  ? 1639 GLU A CG    1 
ATOM   2617  C  CD    . GLU A 1 1639 ? 191.812 146.338 135.039 1.00 81.47  ? 1639 GLU A CD    1 
ATOM   2618  O  OE1   . GLU A 1 1639 ? 191.707 145.177 134.591 1.00 87.71  ? 1639 GLU A OE1   1 
ATOM   2619  O  OE2   . GLU A 1 1639 ? 190.998 146.834 135.847 1.00 76.07  ? 1639 GLU A OE2   1 
ATOM   2620  N  N     . ILE A 1 1640 ? 194.304 150.362 133.191 1.00 57.17  ? 1640 ILE A N     1 
ATOM   2621  C  CA    . ILE A 1 1640 ? 194.482 150.576 131.755 1.00 53.48  ? 1640 ILE A CA    1 
ATOM   2622  C  C     . ILE A 1 1640 ? 195.941 150.872 131.427 1.00 58.44  ? 1640 ILE A C     1 
ATOM   2623  O  O     . ILE A 1 1640 ? 196.535 150.235 130.549 1.00 66.92  ? 1640 ILE A O     1 
ATOM   2624  C  CB    . ILE A 1 1640 ? 193.557 151.701 131.258 1.00 48.29  ? 1640 ILE A CB    1 
ATOM   2625  C  CG1   . ILE A 1 1640 ? 192.101 151.239 131.276 1.00 45.00  ? 1640 ILE A CG1   1 
ATOM   2626  C  CG2   . ILE A 1 1640 ? 193.960 152.140 129.864 1.00 48.48  ? 1640 ILE A CG2   1 
ATOM   2627  C  CD1   . ILE A 1 1640 ? 191.111 152.344 131.017 1.00 38.99  ? 1640 ILE A CD1   1 
ATOM   2628  N  N     . ILE A 1 1641 ? 196.544 151.841 132.119 1.00 58.86  ? 1641 ILE A N     1 
ATOM   2629  C  CA    . ILE A 1 1641 ? 197.936 152.174 131.804 1.00 65.60  ? 1641 ILE A CA    1 
ATOM   2630  C  C     . ILE A 1 1641 ? 198.889 151.104 132.330 1.00 69.17  ? 1641 ILE A C     1 
ATOM   2631  O  O     . ILE A 1 1641 ? 199.898 150.789 131.687 1.00 74.80  ? 1641 ILE A O     1 
ATOM   2632  C  CB    . ILE A 1 1641 ? 198.322 153.582 132.301 1.00 65.46  ? 1641 ILE A CB    1 
ATOM   2633  C  CG1   . ILE A 1 1641 ? 197.515 154.667 131.586 1.00 59.95  ? 1641 ILE A CG1   1 
ATOM   2634  C  CG2   . ILE A 1 1641 ? 199.789 153.856 132.047 1.00 68.22  ? 1641 ILE A CG2   1 
ATOM   2635  C  CD1   . ILE A 1 1641 ? 196.236 155.030 132.219 1.00 57.92  ? 1641 ILE A CD1   1 
ATOM   2636  N  N     . GLY A 1 1642 ? 198.592 150.524 133.493 1.00 65.46  ? 1642 GLY A N     1 
ATOM   2637  C  CA    . GLY A 1 1642 ? 199.470 149.502 134.039 1.00 72.67  ? 1642 GLY A CA    1 
ATOM   2638  C  C     . GLY A 1 1642 ? 199.540 148.254 133.180 1.00 80.08  ? 1642 GLY A C     1 
ATOM   2639  O  O     . GLY A 1 1642 ? 200.620 147.699 132.965 1.00 85.07  ? 1642 GLY A O     1 
ATOM   2640  N  N     . ASN A 1 1643 ? 198.396 147.794 132.676 1.00 77.34  ? 1643 ASN A N     1 
ATOM   2641  C  CA    . ASN A 1 1643 ? 198.374 146.602 131.837 1.00 77.71  ? 1643 ASN A CA    1 
ATOM   2642  C  C     . ASN A 1 1643 ? 198.611 146.955 130.375 1.00 79.50  ? 1643 ASN A C     1 
ATOM   2643  O  O     . ASN A 1 1643 ? 197.778 146.651 129.516 1.00 81.87  ? 1643 ASN A O     1 
ATOM   2644  C  CB    . ASN A 1 1643 ? 197.048 145.859 131.996 1.00 77.34  ? 1643 ASN A CB    1 
ATOM   2645  C  CG    . ASN A 1 1643 ? 196.841 145.334 133.401 1.00 87.80  ? 1643 ASN A CG    1 
ATOM   2646  O  OD1   . ASN A 1 1643 ? 195.936 145.768 134.111 1.00 91.12  ? 1643 ASN A OD1   1 
ATOM   2647  N  ND2   . ASN A 1 1643 ? 197.686 144.396 133.812 1.00 91.54  ? 1643 ASN A ND2   1 
ATOM   2648  N  N     . SER A 1 1644 ? 199.742 147.600 130.084 1.00 79.74  ? 1644 SER A N     1 
ATOM   2649  C  CA    . SER A 1 1644 ? 200.045 147.976 128.707 1.00 84.59  ? 1644 SER A CA    1 
ATOM   2650  C  C     . SER A 1 1644 ? 200.298 146.751 127.836 1.00 90.88  ? 1644 SER A C     1 
ATOM   2651  O  O     . SER A 1 1644 ? 199.797 146.672 126.708 1.00 92.29  ? 1644 SER A O     1 
ATOM   2652  C  CB    . SER A 1 1644 ? 201.249 148.915 128.672 1.00 87.40  ? 1644 SER A CB    1 
ATOM   2653  O  OG    . SER A 1 1644 ? 202.422 148.259 129.118 1.00 89.64  ? 1644 SER A OG    1 
ATOM   2654  N  N     . LYS A 1 1645 ? 201.079 145.790 128.335 1.00 91.99  ? 1645 LYS A N     1 
ATOM   2655  C  CA    . LYS A 1 1645 ? 201.384 144.602 127.542 1.00 94.56  ? 1645 LYS A CA    1 
ATOM   2656  C  C     . LYS A 1 1645 ? 200.136 143.763 127.289 1.00 92.25  ? 1645 LYS A C     1 
ATOM   2657  O  O     . LYS A 1 1645 ? 199.902 143.314 126.161 1.00 93.03  ? 1645 LYS A O     1 
ATOM   2658  C  CB    . LYS A 1 1645 ? 202.459 143.767 128.237 1.00 98.20  ? 1645 LYS A CB    1 
ATOM   2659  C  CG    . LYS A 1 1645 ? 203.724 144.537 128.575 1.00 104.24 ? 1645 LYS A CG    1 
ATOM   2660  C  CD    . LYS A 1 1645 ? 204.918 143.604 128.696 1.00 106.18 ? 1645 LYS A CD    1 
ATOM   2661  C  CE    . LYS A 1 1645 ? 206.219 144.379 128.840 1.00 107.53 ? 1645 LYS A CE    1 
ATOM   2662  N  NZ    . LYS A 1 1645 ? 206.798 144.747 127.518 1.00 100.46 ? 1645 LYS A NZ    1 
ATOM   2663  N  N     . ASN A 1 1646 ? 199.322 143.545 128.322 1.00 87.26  ? 1646 ASN A N     1 
ATOM   2664  C  CA    . ASN A 1 1646 ? 198.089 142.770 128.191 1.00 86.57  ? 1646 ASN A CA    1 
ATOM   2665  C  C     . ASN A 1 1646 ? 196.986 143.693 127.682 1.00 86.57  ? 1646 ASN A C     1 
ATOM   2666  O  O     . ASN A 1 1646 ? 196.155 144.205 128.435 1.00 85.06  ? 1646 ASN A O     1 
ATOM   2667  C  CB    . ASN A 1 1646 ? 197.714 142.120 129.516 1.00 85.01  ? 1646 ASN A CB    1 
ATOM   2668  C  CG    . ASN A 1 1646 ? 197.040 140.775 129.335 1.00 91.11  ? 1646 ASN A CG    1 
ATOM   2669  O  OD1   . ASN A 1 1646 ? 196.459 140.495 128.286 1.00 90.97  ? 1646 ASN A OD1   1 
ATOM   2670  N  ND2   . ASN A 1 1646 ? 197.123 139.928 130.354 1.00 94.65  ? 1646 ASN A ND2   1 
ATOM   2671  N  N     . VAL A 1 1647 ? 196.985 143.905 126.363 1.00 85.39  ? 1647 VAL A N     1 
ATOM   2672  C  CA    . VAL A 1 1647 ? 195.974 144.761 125.751 1.00 78.12  ? 1647 VAL A CA    1 
ATOM   2673  C  C     . VAL A 1 1647 ? 194.582 144.179 125.952 1.00 78.03  ? 1647 VAL A C     1 
ATOM   2674  O  O     . VAL A 1 1647 ? 193.597 144.922 126.040 1.00 77.82  ? 1647 VAL A O     1 
ATOM   2675  C  CB    . VAL A 1 1647 ? 196.286 144.976 124.257 1.00 70.26  ? 1647 VAL A CB    1 
ATOM   2676  C  CG1   . VAL A 1 1647 ? 195.396 146.062 123.682 1.00 68.59  ? 1647 VAL A CG1   1 
ATOM   2677  C  CG2   . VAL A 1 1647 ? 197.749 145.328 124.066 1.00 72.07  ? 1647 VAL A CG2   1 
ATOM   2678  N  N     . ALA A 1 1648 ? 194.475 142.852 126.042 1.00 78.73  ? 1648 ALA A N     1 
ATOM   2679  C  CA    . ALA A 1 1648 ? 193.180 142.199 126.192 1.00 73.17  ? 1648 ALA A CA    1 
ATOM   2680  C  C     . ALA A 1 1648 ? 192.486 142.533 127.506 1.00 70.89  ? 1648 ALA A C     1 
ATOM   2681  O  O     . ALA A 1 1648 ? 191.281 142.289 127.621 1.00 71.95  ? 1648 ALA A O     1 
ATOM   2682  C  CB    . ALA A 1 1648 ? 193.337 140.684 126.071 1.00 79.51  ? 1648 ALA A CB    1 
ATOM   2683  N  N     . LYS A 1 1649 ? 193.202 143.066 128.497 1.00 69.29  ? 1649 LYS A N     1 
ATOM   2684  C  CA    . LYS A 1 1649 ? 192.545 143.524 129.715 1.00 75.75  ? 1649 LYS A CA    1 
ATOM   2685  C  C     . LYS A 1 1649 ? 191.899 144.891 129.562 1.00 74.12  ? 1649 LYS A C     1 
ATOM   2686  O  O     . LYS A 1 1649 ? 191.110 145.283 130.429 1.00 74.96  ? 1649 LYS A O     1 
ATOM   2687  C  CB    . LYS A 1 1649 ? 193.528 143.569 130.889 1.00 85.16  ? 1649 LYS A CB    1 
ATOM   2688  C  CG    . LYS A 1 1649 ? 194.031 142.217 131.356 1.00 90.97  ? 1649 LYS A CG    1 
ATOM   2689  C  CD    . LYS A 1 1649 ? 194.945 142.378 132.559 1.00 93.76  ? 1649 LYS A CD    1 
ATOM   2690  C  CE    . LYS A 1 1649 ? 195.522 141.047 132.998 1.00 101.60 ? 1649 LYS A CE    1 
ATOM   2691  N  NZ    . LYS A 1 1649 ? 194.470 140.148 133.545 1.00 105.22 ? 1649 LYS A NZ    1 
ATOM   2692  N  N     . LEU A 1 1650 ? 192.212 145.624 128.496 1.00 72.08  ? 1650 LEU A N     1 
ATOM   2693  C  CA    . LEU A 1 1650 ? 191.623 146.934 128.262 1.00 66.66  ? 1650 LEU A CA    1 
ATOM   2694  C  C     . LEU A 1 1650 ? 190.237 146.858 127.641 1.00 61.91  ? 1650 LEU A C     1 
ATOM   2695  O  O     . LEU A 1 1650 ? 189.514 147.859 127.657 1.00 61.34  ? 1650 LEU A O     1 
ATOM   2696  C  CB    . LEU A 1 1650 ? 192.530 147.776 127.355 1.00 60.55  ? 1650 LEU A CB    1 
ATOM   2697  C  CG    . LEU A 1 1650 ? 193.745 148.504 127.940 1.00 66.92  ? 1650 LEU A CG    1 
ATOM   2698  C  CD1   . LEU A 1 1650 ? 194.709 147.570 128.655 1.00 70.07  ? 1650 LEU A CD1   1 
ATOM   2699  C  CD2   . LEU A 1 1650 ? 194.464 149.276 126.844 1.00 68.96  ? 1650 LEU A CD2   1 
ATOM   2700  N  N     . GLN A 1 1651 ? 189.847 145.698 127.110 1.00 57.79  ? 1651 GLN A N     1 
ATOM   2701  C  CA    . GLN A 1 1651 ? 188.585 145.575 126.393 1.00 54.17  ? 1651 GLN A CA    1 
ATOM   2702  C  C     . GLN A 1 1651 ? 187.367 145.741 127.291 1.00 58.73  ? 1651 GLN A C     1 
ATOM   2703  O  O     . GLN A 1 1651 ? 186.269 145.964 126.772 1.00 60.07  ? 1651 GLN A O     1 
ATOM   2704  C  CB    . GLN A 1 1651 ? 188.518 144.223 125.683 1.00 52.71  ? 1651 GLN A CB    1 
ATOM   2705  C  CG    . GLN A 1 1651 ? 189.818 143.809 125.020 1.00 57.52  ? 1651 GLN A CG    1 
ATOM   2706  C  CD    . GLN A 1 1651 ? 190.021 144.468 123.675 1.00 53.79  ? 1651 GLN A CD    1 
ATOM   2707  O  OE1   . GLN A 1 1651 ? 189.147 145.175 123.181 1.00 55.55  ? 1651 GLN A OE1   1 
ATOM   2708  N  NE2   . GLN A 1 1651 ? 191.181 144.243 123.075 1.00 57.52  ? 1651 GLN A NE2   1 
ATOM   2709  N  N     . LYS A 1 1652 ? 187.524 145.641 128.607 1.00 57.11  ? 1652 LYS A N     1 
ATOM   2710  C  CA    . LYS A 1 1652 ? 186.405 145.790 129.525 1.00 57.63  ? 1652 LYS A CA    1 
ATOM   2711  C  C     . LYS A 1 1652 ? 186.115 147.243 129.874 1.00 59.31  ? 1652 LYS A C     1 
ATOM   2712  O  O     . LYS A 1 1652 ? 185.107 147.515 130.534 1.00 64.11  ? 1652 LYS A O     1 
ATOM   2713  C  CB    . LYS A 1 1652 ? 186.664 144.996 130.810 1.00 60.49  ? 1652 LYS A CB    1 
ATOM   2714  C  CG    . LYS A 1 1652 ? 187.750 145.580 131.695 1.00 66.67  ? 1652 LYS A CG    1 
ATOM   2715  C  CD    . LYS A 1 1652 ? 188.409 144.506 132.541 1.00 71.34  ? 1652 LYS A CD    1 
ATOM   2716  C  CE    . LYS A 1 1652 ? 187.393 143.807 133.427 1.00 81.07  ? 1652 LYS A CE    1 
ATOM   2717  N  NZ    . LYS A 1 1652 ? 186.852 144.714 134.476 1.00 79.49  ? 1652 LYS A NZ    1 
ATOM   2718  N  N     . HIS A 1 1653 ? 186.965 148.178 129.449 1.00 51.32  ? 1653 HIS A N     1 
ATOM   2719  C  CA    . HIS A 1 1653 ? 186.779 149.588 129.751 1.00 46.15  ? 1653 HIS A CA    1 
ATOM   2720  C  C     . HIS A 1 1653 ? 186.377 150.422 128.545 1.00 47.43  ? 1653 HIS A C     1 
ATOM   2721  O  O     . HIS A 1 1653 ? 186.008 151.587 128.719 1.00 50.30  ? 1653 HIS A O     1 
ATOM   2722  C  CB    . HIS A 1 1653 ? 188.060 150.177 130.361 1.00 52.18  ? 1653 HIS A CB    1 
ATOM   2723  C  CG    . HIS A 1 1653 ? 188.544 149.446 131.575 1.00 56.56  ? 1653 HIS A CG    1 
ATOM   2724  N  ND1   . HIS A 1 1653 ? 187.810 149.367 132.738 1.00 53.82  ? 1653 HIS A ND1   1 
ATOM   2725  C  CD2   . HIS A 1 1653 ? 189.691 148.765 131.807 1.00 57.30  ? 1653 HIS A CD2   1 
ATOM   2726  C  CE1   . HIS A 1 1653 ? 188.482 148.667 133.634 1.00 59.61  ? 1653 HIS A CE1   1 
ATOM   2727  N  NE2   . HIS A 1 1653 ? 189.626 148.290 133.094 1.00 56.89  ? 1653 HIS A NE2   1 
ATOM   2728  N  N     . PHE A 1 1654 ? 186.437 149.864 127.333 1.00 49.77  ? 1654 PHE A N     1 
ATOM   2729  C  CA    . PHE A 1 1654 ? 186.081 150.631 126.143 1.00 40.01  ? 1654 PHE A CA    1 
ATOM   2730  C  C     . PHE A 1 1654 ? 184.615 151.038 126.147 1.00 37.48  ? 1654 PHE A C     1 
ATOM   2731  O  O     . PHE A 1 1654 ? 184.247 152.028 125.506 1.00 39.02  ? 1654 PHE A O     1 
ATOM   2732  C  CB    . PHE A 1 1654 ? 186.399 149.828 124.885 1.00 38.20  ? 1654 PHE A CB    1 
ATOM   2733  C  CG    . PHE A 1 1654 ? 187.853 149.807 124.533 1.00 38.08  ? 1654 PHE A CG    1 
ATOM   2734  C  CD1   . PHE A 1 1654 ? 188.531 150.983 124.274 1.00 41.46  ? 1654 PHE A CD1   1 
ATOM   2735  C  CD2   . PHE A 1 1654 ? 188.544 148.615 124.460 1.00 38.77  ? 1654 PHE A CD2   1 
ATOM   2736  C  CE1   . PHE A 1 1654 ? 189.870 150.968 123.947 1.00 42.29  ? 1654 PHE A CE1   1 
ATOM   2737  C  CE2   . PHE A 1 1654 ? 189.883 148.595 124.135 1.00 44.73  ? 1654 PHE A CE2   1 
ATOM   2738  C  CZ    . PHE A 1 1654 ? 190.546 149.773 123.878 1.00 43.06  ? 1654 PHE A CZ    1 
ATOM   2739  N  N     . LYS A 1 1655 ? 183.763 150.290 126.849 1.00 41.11  ? 1655 LYS A N     1 
ATOM   2740  C  CA    . LYS A 1 1655 ? 182.347 150.636 126.892 1.00 40.01  ? 1655 LYS A CA    1 
ATOM   2741  C  C     . LYS A 1 1655 ? 182.118 151.930 127.661 1.00 42.04  ? 1655 LYS A C     1 
ATOM   2742  O  O     . LYS A 1 1655 ? 181.198 152.692 127.343 1.00 50.94  ? 1655 LYS A O     1 
ATOM   2743  C  CB    . LYS A 1 1655 ? 181.548 149.490 127.509 1.00 43.78  ? 1655 LYS A CB    1 
ATOM   2744  C  CG    . LYS A 1 1655 ? 182.185 148.890 128.745 1.00 54.17  ? 1655 LYS A CG    1 
ATOM   2745  C  CD    . LYS A 1 1655 ? 181.538 147.568 129.106 1.00 59.71  ? 1655 LYS A CD    1 
ATOM   2746  C  CE    . LYS A 1 1655 ? 181.708 146.561 127.981 1.00 64.70  ? 1655 LYS A CE    1 
ATOM   2747  N  NZ    . LYS A 1 1655 ? 183.133 146.428 127.569 1.00 55.66  ? 1655 LYS A NZ    1 
ATOM   2748  N  N     . LYS A 1 1656 ? 182.938 152.194 128.679 1.00 42.16  ? 1656 LYS A N     1 
ATOM   2749  C  CA    . LYS A 1 1656 ? 182.813 153.436 129.432 1.00 41.76  ? 1656 LYS A CA    1 
ATOM   2750  C  C     . LYS A 1 1656 ? 183.386 154.620 128.663 1.00 36.81  ? 1656 LYS A C     1 
ATOM   2751  O  O     . LYS A 1 1656 ? 182.822 155.719 128.701 1.00 32.90  ? 1656 LYS A O     1 
ATOM   2752  C  CB    . LYS A 1 1656 ? 183.506 153.300 130.788 1.00 39.97  ? 1656 LYS A CB    1 
ATOM   2753  C  CG    . LYS A 1 1656 ? 183.513 151.885 131.337 1.00 51.09  ? 1656 LYS A CG    1 
ATOM   2754  C  CD    . LYS A 1 1656 ? 184.399 151.771 132.563 1.00 56.86  ? 1656 LYS A CD    1 
ATOM   2755  C  CE    . LYS A 1 1656 ? 184.528 150.326 133.017 1.00 60.46  ? 1656 LYS A CE    1 
ATOM   2756  N  NZ    . LYS A 1 1656 ? 183.206 149.714 133.314 1.00 67.93  ? 1656 LYS A NZ    1 
ATOM   2757  N  N     . MET A 1 1657 ? 184.505 154.417 127.967 1.00 35.72  ? 1657 MET A N     1 
ATOM   2758  C  CA    . MET A 1 1657 ? 185.159 155.525 127.280 1.00 33.19  ? 1657 MET A CA    1 
ATOM   2759  C  C     . MET A 1 1657 ? 184.412 155.925 126.014 1.00 36.44  ? 1657 MET A C     1 
ATOM   2760  O  O     . MET A 1 1657 ? 184.249 157.118 125.736 1.00 37.68  ? 1657 MET A O     1 
ATOM   2761  C  CB    . MET A 1 1657 ? 186.605 155.158 126.950 1.00 32.83  ? 1657 MET A CB    1 
ATOM   2762  C  CG    . MET A 1 1657 ? 187.545 155.186 128.140 1.00 30.53  ? 1657 MET A CG    1 
ATOM   2763  S  SD    . MET A 1 1657 ? 189.184 154.567 127.725 1.00 44.51  ? 1657 MET A SD    1 
ATOM   2764  C  CE    . MET A 1 1657 ? 188.925 152.802 127.843 1.00 41.54  ? 1657 MET A CE    1 
ATOM   2765  N  N     . PHE A 1 1658 ? 183.956 154.950 125.232 1.00 37.70  ? 1658 PHE A N     1 
ATOM   2766  C  CA    . PHE A 1 1658 ? 183.359 155.197 123.927 1.00 34.54  ? 1658 PHE A CA    1 
ATOM   2767  C  C     . PHE A 1 1658 ? 181.859 154.916 123.960 1.00 37.27  ? 1658 PHE A C     1 
ATOM   2768  O  O     . PHE A 1 1658 ? 181.314 154.404 124.941 1.00 36.68  ? 1658 PHE A O     1 
ATOM   2769  C  CB    . PHE A 1 1658 ? 184.041 154.349 122.853 1.00 30.32  ? 1658 PHE A CB    1 
ATOM   2770  C  CG    . PHE A 1 1658 ? 185.483 154.697 122.622 1.00 30.09  ? 1658 PHE A CG    1 
ATOM   2771  C  CD1   . PHE A 1 1658 ? 186.464 154.275 123.500 1.00 32.05  ? 1658 PHE A CD1   1 
ATOM   2772  C  CD2   . PHE A 1 1658 ? 185.858 155.442 121.519 1.00 33.01  ? 1658 PHE A CD2   1 
ATOM   2773  C  CE1   . PHE A 1 1658 ? 187.788 154.591 123.283 1.00 33.97  ? 1658 PHE A CE1   1 
ATOM   2774  C  CE2   . PHE A 1 1658 ? 187.180 155.761 121.299 1.00 35.62  ? 1658 PHE A CE2   1 
ATOM   2775  C  CZ    . PHE A 1 1658 ? 188.145 155.335 122.182 1.00 36.29  ? 1658 PHE A CZ    1 
ATOM   2776  N  N     . ALA A 1 1659 ? 181.193 155.253 122.856 1.00 39.84  ? 1659 ALA A N     1 
ATOM   2777  C  CA    . ALA A 1 1659 ? 179.746 155.100 122.737 1.00 37.76  ? 1659 ALA A CA    1 
ATOM   2778  C  C     . ALA A 1 1659 ? 179.361 153.702 122.264 1.00 39.97  ? 1659 ALA A C     1 
ATOM   2779  O  O     . ALA A 1 1659 ? 178.625 152.987 122.950 1.00 41.20  ? 1659 ALA A O     1 
ATOM   2780  C  CB    . ALA A 1 1659 ? 179.183 156.155 121.778 1.00 32.91  ? 1659 ALA A CB    1 
ATOM   2781  N  N     . GLY A 1 1660 ? 179.847 153.305 121.093 1.00 41.48  ? 1660 GLY A N     1 
ATOM   2782  C  CA    . GLY A 1 1660 ? 179.506 152.012 120.539 1.00 36.19  ? 1660 GLY A CA    1 
ATOM   2783  C  C     . GLY A 1 1660 ? 180.686 151.072 120.443 1.00 34.74  ? 1660 GLY A C     1 
ATOM   2784  O  O     . GLY A 1 1660 ? 180.530 149.909 120.064 1.00 42.12  ? 1660 GLY A O     1 
ATOM   2785  N  N     . VAL A 1 1661 ? 181.874 151.564 120.781 1.00 33.48  ? 1661 VAL A N     1 
ATOM   2786  C  CA    . VAL A 1 1661 ? 183.080 150.745 120.756 1.00 34.45  ? 1661 VAL A CA    1 
ATOM   2787  C  C     . VAL A 1 1661 ? 183.100 149.903 122.027 1.00 37.75  ? 1661 VAL A C     1 
ATOM   2788  O  O     . VAL A 1 1661 ? 183.337 150.419 123.121 1.00 43.30  ? 1661 VAL A O     1 
ATOM   2789  C  CB    . VAL A 1 1661 ? 184.344 151.603 120.642 1.00 34.64  ? 1661 VAL A CB    1 
ATOM   2790  C  CG1   . VAL A 1 1661 ? 185.584 150.731 120.690 1.00 28.77  ? 1661 VAL A CG1   1 
ATOM   2791  C  CG2   . VAL A 1 1661 ? 184.309 152.428 119.376 1.00 38.21  ? 1661 VAL A CG2   1 
ATOM   2792  N  N     . SER A 1 1662 ? 182.839 148.606 121.886 1.00 38.25  ? 1662 SER A N     1 
ATOM   2793  C  CA    . SER A 1 1662 ? 182.908 147.686 123.010 1.00 39.51  ? 1662 SER A CA    1 
ATOM   2794  C  C     . SER A 1 1662 ? 184.240 146.959 123.098 1.00 43.64  ? 1662 SER A C     1 
ATOM   2795  O  O     . SER A 1 1662 ? 184.561 146.412 124.158 1.00 51.11  ? 1662 SER A O     1 
ATOM   2796  C  CB    . SER A 1 1662 ? 181.777 146.656 122.926 1.00 46.23  ? 1662 SER A CB    1 
ATOM   2797  O  OG    . SER A 1 1662 ? 181.809 145.771 124.031 1.00 56.86  ? 1662 SER A OG    1 
ATOM   2798  N  N     . SER A 1 1663 ? 185.016 146.951 122.020 1.00 37.23  ? 1663 SER A N     1 
ATOM   2799  C  CA    . SER A 1 1663 ? 186.322 146.309 121.997 1.00 39.21  ? 1663 SER A CA    1 
ATOM   2800  C  C     . SER A 1 1663 ? 187.088 146.846 120.796 1.00 36.85  ? 1663 SER A C     1 
ATOM   2801  O  O     . SER A 1 1663 ? 186.536 147.550 119.947 1.00 45.56  ? 1663 SER A O     1 
ATOM   2802  C  CB    . SER A 1 1663 ? 186.189 144.786 121.942 1.00 49.35  ? 1663 SER A CB    1 
ATOM   2803  O  OG    . SER A 1 1663 ? 185.447 144.380 120.806 1.00 56.23  ? 1663 SER A OG    1 
ATOM   2804  N  N     . ILE A 1 1664 ? 188.373 146.515 120.736 1.00 36.00  ? 1664 ILE A N     1 
ATOM   2805  C  CA    . ILE A 1 1664 ? 189.214 146.835 119.592 1.00 39.39  ? 1664 ILE A CA    1 
ATOM   2806  C  C     . ILE A 1 1664 ? 189.765 145.533 119.036 1.00 46.36  ? 1664 ILE A C     1 
ATOM   2807  O  O     . ILE A 1 1664 ? 190.067 144.602 119.791 1.00 56.74  ? 1664 ILE A O     1 
ATOM   2808  C  CB    . ILE A 1 1664 ? 190.363 147.798 119.957 1.00 44.57  ? 1664 ILE A CB    1 
ATOM   2809  C  CG1   . ILE A 1 1664 ? 191.185 147.242 121.118 1.00 48.03  ? 1664 ILE A CG1   1 
ATOM   2810  C  CG2   . ILE A 1 1664 ? 189.816 149.170 120.304 1.00 49.40  ? 1664 ILE A CG2   1 
ATOM   2811  C  CD1   . ILE A 1 1664 ? 192.426 148.040 121.418 1.00 47.51  ? 1664 ILE A CD1   1 
ATOM   2812  N  N     . ILE A 1 1665 ? 189.878 145.459 117.714 1.00 45.80  ? 1665 ILE A N     1 
ATOM   2813  C  CA    . ILE A 1 1665 ? 190.383 144.260 117.054 1.00 51.92  ? 1665 ILE A CA    1 
ATOM   2814  C  C     . ILE A 1 1665 ? 191.883 144.430 116.849 1.00 55.20  ? 1665 ILE A C     1 
ATOM   2815  O  O     . ILE A 1 1665 ? 192.334 145.419 116.268 1.00 58.12  ? 1665 ILE A O     1 
ATOM   2816  C  CB    . ILE A 1 1665 ? 189.657 144.003 115.731 1.00 50.16  ? 1665 ILE A CB    1 
ATOM   2817  C  CG1   . ILE A 1 1665 ? 188.170 144.310 115.901 1.00 48.73  ? 1665 ILE A CG1   1 
ATOM   2818  C  CG2   . ILE A 1 1665 ? 189.861 142.570 115.281 1.00 57.95  ? 1665 ILE A CG2   1 
ATOM   2819  C  CD1   . ILE A 1 1665 ? 187.392 144.285 114.628 1.00 48.88  ? 1665 ILE A CD1   1 
ATOM   2820  N  N     . LEU A 1 1666 ? 192.659 143.468 117.336 1.00 54.86  ? 1666 LEU A N     1 
ATOM   2821  C  CA    . LEU A 1 1666 ? 194.107 143.575 117.338 1.00 58.63  ? 1666 LEU A CA    1 
ATOM   2822  C  C     . LEU A 1 1666 ? 194.713 142.784 116.184 1.00 64.33  ? 1666 LEU A C     1 
ATOM   2823  O  O     . LEU A 1 1666 ? 194.026 142.080 115.442 1.00 69.22  ? 1666 LEU A O     1 
ATOM   2824  C  CB    . LEU A 1 1666 ? 194.683 143.081 118.667 1.00 62.86  ? 1666 LEU A CB    1 
ATOM   2825  C  CG    . LEU A 1 1666 ? 194.721 144.029 119.870 1.00 58.70  ? 1666 LEU A CG    1 
ATOM   2826  C  CD1   . LEU A 1 1666 ? 195.605 145.227 119.577 1.00 58.56  ? 1666 LEU A CD1   1 
ATOM   2827  C  CD2   . LEU A 1 1666 ? 193.334 144.463 120.313 1.00 52.66  ? 1666 LEU A CD2   1 
ATOM   2828  N  N     . ASN A 1 1667 ? 196.028 142.909 116.043 1.00 67.74  ? 1667 ASN A N     1 
ATOM   2829  C  CA    . ASN A 1 1667 ? 196.781 142.158 115.049 1.00 65.89  ? 1667 ASN A CA    1 
ATOM   2830  C  C     . ASN A 1 1667 ? 197.054 140.756 115.594 1.00 76.70  ? 1667 ASN A C     1 
ATOM   2831  O  O     . ASN A 1 1667 ? 196.488 140.335 116.606 1.00 77.77  ? 1667 ASN A O     1 
ATOM   2832  C  CB    . ASN A 1 1667 ? 198.060 142.908 114.689 1.00 67.65  ? 1667 ASN A CB    1 
ATOM   2833  C  CG    . ASN A 1 1667 ? 198.617 142.502 113.341 1.00 77.13  ? 1667 ASN A CG    1 
ATOM   2834  O  OD1   . ASN A 1 1667 ? 197.946 142.621 112.318 1.00 85.99  ? 1667 ASN A OD1   1 
ATOM   2835  N  ND2   . ASN A 1 1667 ? 199.856 142.025 113.333 1.00 79.63  ? 1667 ASN A ND2   1 
ATOM   2836  N  N     . GLU A 1 1668 ? 197.926 140.007 114.916 1.00 86.74  ? 1668 GLU A N     1 
ATOM   2837  C  CA    . GLU A 1 1668 ? 198.281 138.674 115.391 1.00 90.64  ? 1668 GLU A CA    1 
ATOM   2838  C  C     . GLU A 1 1668 ? 198.994 138.736 116.737 1.00 90.51  ? 1668 GLU A C     1 
ATOM   2839  O  O     . GLU A 1 1668 ? 198.723 137.924 117.630 1.00 92.29  ? 1668 GLU A O     1 
ATOM   2840  C  CB    . GLU A 1 1668 ? 199.152 137.963 114.355 1.00 88.50  ? 1668 GLU A CB    1 
ATOM   2841  C  CG    . GLU A 1 1668 ? 198.441 137.647 113.044 1.00 98.56  ? 1668 GLU A CG    1 
ATOM   2842  C  CD    . GLU A 1 1668 ? 197.496 136.461 113.148 1.00 110.36 ? 1668 GLU A CD    1 
ATOM   2843  O  OE1   . GLU A 1 1668 ? 197.346 135.901 114.254 1.00 108.65 ? 1668 GLU A OE1   1 
ATOM   2844  O  OE2   . GLU A 1 1668 ? 196.901 136.089 112.115 1.00 112.94 ? 1668 GLU A OE2   1 
ATOM   2845  N  N     . ASP A 1 1669 ? 199.907 139.693 116.902 1.00 87.29  ? 1669 ASP A N     1 
ATOM   2846  C  CA    . ASP A 1 1669 ? 200.700 139.825 118.116 1.00 83.08  ? 1669 ASP A CA    1 
ATOM   2847  C  C     . ASP A 1 1669 ? 200.281 141.019 118.967 1.00 80.92  ? 1669 ASP A C     1 
ATOM   2848  O  O     . ASP A 1 1669 ? 201.073 141.487 119.792 1.00 85.45  ? 1669 ASP A O     1 
ATOM   2849  C  CB    . ASP A 1 1669 ? 202.185 139.922 117.764 1.00 85.49  ? 1669 ASP A CB    1 
ATOM   2850  C  CG    . ASP A 1 1669 ? 202.448 140.863 116.605 1.00 86.97  ? 1669 ASP A CG    1 
ATOM   2851  O  OD1   . ASP A 1 1669 ? 201.522 141.604 116.215 1.00 84.77  ? 1669 ASP A OD1   1 
ATOM   2852  O  OD2   . ASP A 1 1669 ? 203.582 140.859 116.080 1.00 83.97  ? 1669 ASP A OD2   1 
ATOM   2853  N  N     . ASN A 1 1670 ? 199.057 141.517 118.782 1.00 77.56  ? 1670 ASN A N     1 
ATOM   2854  C  CA    . ASN A 1 1670 ? 198.543 142.667 119.529 1.00 70.64  ? 1670 ASN A CA    1 
ATOM   2855  C  C     . ASN A 1 1670 ? 199.465 143.877 119.400 1.00 70.64  ? 1670 ASN A C     1 
ATOM   2856  O  O     . ASN A 1 1670 ? 199.711 144.599 120.367 1.00 73.22  ? 1670 ASN A O     1 
ATOM   2857  C  CB    . ASN A 1 1670 ? 198.311 142.318 121.000 1.00 68.29  ? 1670 ASN A CB    1 
ATOM   2858  C  CG    . ASN A 1 1670 ? 197.536 141.031 121.177 1.00 77.75  ? 1670 ASN A CG    1 
ATOM   2859  O  OD1   . ASN A 1 1670 ? 196.427 140.888 120.665 1.00 78.67  ? 1670 ASN A OD1   1 
ATOM   2860  N  ND2   . ASN A 1 1670 ? 198.115 140.087 121.908 1.00 84.31  ? 1670 ASN A ND2   1 
ATOM   2861  N  N     . SER A 1 1671 ? 199.980 144.101 118.193 1.00 68.89  ? 1671 SER A N     1 
ATOM   2862  C  CA    . SER A 1 1671 ? 200.843 145.239 117.920 1.00 70.44  ? 1671 SER A CA    1 
ATOM   2863  C  C     . SER A 1 1671 ? 200.225 146.247 116.965 1.00 72.06  ? 1671 SER A C     1 
ATOM   2864  O  O     . SER A 1 1671 ? 200.764 147.349 116.821 1.00 75.02  ? 1671 SER A O     1 
ATOM   2865  C  CB    . SER A 1 1671 ? 202.186 144.763 117.346 1.00 74.63  ? 1671 SER A CB    1 
ATOM   2866  O  OG    . SER A 1 1671 ? 202.009 144.153 116.080 1.00 80.75  ? 1671 SER A OG    1 
ATOM   2867  N  N     . VAL A 1 1672 ? 199.124 145.900 116.305 1.00 70.72  ? 1672 VAL A N     1 
ATOM   2868  C  CA    . VAL A 1 1672 ? 198.442 146.791 115.373 1.00 64.21  ? 1672 VAL A CA    1 
ATOM   2869  C  C     . VAL A 1 1672 ? 196.949 146.715 115.649 1.00 61.42  ? 1672 VAL A C     1 
ATOM   2870  O  O     . VAL A 1 1672 ? 196.388 145.619 115.753 1.00 66.16  ? 1672 VAL A O     1 
ATOM   2871  C  CB    . VAL A 1 1672 ? 198.743 146.422 113.906 1.00 63.56  ? 1672 VAL A CB    1 
ATOM   2872  C  CG1   . VAL A 1 1672 ? 197.811 147.157 112.973 1.00 57.74  ? 1672 VAL A CG1   1 
ATOM   2873  C  CG2   . VAL A 1 1672 ? 200.189 146.734 113.563 1.00 71.01  ? 1672 VAL A CG2   1 
ATOM   2874  N  N     . VAL A 1 1673 ? 196.306 147.871 115.776 1.00 59.63  ? 1673 VAL A N     1 
ATOM   2875  C  CA    . VAL A 1 1673 ? 194.861 147.940 115.958 1.00 53.85  ? 1673 VAL A CA    1 
ATOM   2876  C  C     . VAL A 1 1673 ? 194.228 147.991 114.573 1.00 55.79  ? 1673 VAL A C     1 
ATOM   2877  O  O     . VAL A 1 1673 ? 194.256 149.027 113.905 1.00 57.89  ? 1673 VAL A O     1 
ATOM   2878  C  CB    . VAL A 1 1673 ? 194.453 149.153 116.803 1.00 50.65  ? 1673 VAL A CB    1 
ATOM   2879  C  CG1   . VAL A 1 1673 ? 192.959 149.139 117.061 1.00 44.67  ? 1673 VAL A CG1   1 
ATOM   2880  C  CG2   . VAL A 1 1673 ? 195.217 149.165 118.111 1.00 57.85  ? 1673 VAL A CG2   1 
ATOM   2881  N  N     . LEU A 1 1674 ? 193.661 146.866 114.137 1.00 54.91  ? 1674 LEU A N     1 
ATOM   2882  C  CA    . LEU A 1 1674 ? 193.090 146.779 112.800 1.00 49.26  ? 1674 LEU A CA    1 
ATOM   2883  C  C     . LEU A 1 1674 ? 191.727 147.443 112.692 1.00 50.01  ? 1674 LEU A C     1 
ATOM   2884  O  O     . LEU A 1 1674 ? 191.271 147.700 111.573 1.00 57.68  ? 1674 LEU A O     1 
ATOM   2885  C  CB    . LEU A 1 1674 ? 192.976 145.315 112.372 1.00 50.89  ? 1674 LEU A CB    1 
ATOM   2886  C  CG    . LEU A 1 1674 ? 194.281 144.536 112.230 1.00 57.62  ? 1674 LEU A CG    1 
ATOM   2887  C  CD1   . LEU A 1 1674 ? 193.994 143.088 111.880 1.00 61.04  ? 1674 LEU A CD1   1 
ATOM   2888  C  CD2   . LEU A 1 1674 ? 195.172 145.177 111.181 1.00 58.24  ? 1674 LEU A CD2   1 
ATOM   2889  N  N     . GLY A 1 1675 ? 191.070 147.723 113.808 1.00 45.46  ? 1675 GLY A N     1 
ATOM   2890  C  CA    . GLY A 1 1675 ? 189.759 148.337 113.762 1.00 41.58  ? 1675 GLY A CA    1 
ATOM   2891  C  C     . GLY A 1 1675 ? 189.106 148.303 115.132 1.00 38.07  ? 1675 GLY A C     1 
ATOM   2892  O  O     . GLY A 1 1675 ? 189.770 148.115 116.147 1.00 47.17  ? 1675 GLY A O     1 
ATOM   2893  N  N     . ILE A 1 1676 ? 187.789 148.493 115.122 1.00 33.17  ? 1676 ILE A N     1 
ATOM   2894  C  CA    . ILE A 1 1676 ? 186.983 148.529 116.334 1.00 36.62  ? 1676 ILE A CA    1 
ATOM   2895  C  C     . ILE A 1 1676 ? 185.760 147.647 116.142 1.00 37.05  ? 1676 ILE A C     1 
ATOM   2896  O  O     . ILE A 1 1676 ? 185.392 147.291 115.023 1.00 48.23  ? 1676 ILE A O     1 
ATOM   2897  C  CB    . ILE A 1 1676 ? 186.567 149.966 116.709 1.00 39.91  ? 1676 ILE A CB    1 
ATOM   2898  C  CG1   . ILE A 1 1676 ? 185.742 150.584 115.580 1.00 41.21  ? 1676 ILE A CG1   1 
ATOM   2899  C  CG2   . ILE A 1 1676 ? 187.780 150.811 117.055 1.00 40.93  ? 1676 ILE A CG2   1 
ATOM   2900  C  CD1   . ILE A 1 1676 ? 185.117 151.895 115.930 1.00 33.82  ? 1676 ILE A CD1   1 
ATOM   2901  N  N     . SER A 1 1677 ? 185.135 147.283 117.256 1.00 31.56  ? 1677 SER A N     1 
ATOM   2902  C  CA    . SER A 1 1677 ? 183.997 146.378 117.239 1.00 37.21  ? 1677 SER A CA    1 
ATOM   2903  C  C     . SER A 1 1677 ? 182.909 146.885 118.172 1.00 40.32  ? 1677 SER A C     1 
ATOM   2904  O  O     . SER A 1 1677 ? 183.186 147.533 119.184 1.00 46.50  ? 1677 SER A O     1 
ATOM   2905  C  CB    . SER A 1 1677 ? 184.409 144.958 117.645 1.00 51.09  ? 1677 SER A CB    1 
ATOM   2906  O  OG    . SER A 1 1677 ? 183.298 144.080 117.627 1.00 59.70  ? 1677 SER A OG    1 
ATOM   2907  N  N     . SER A 1 1678 ? 181.666 146.582 117.819 1.00 46.90  ? 1678 SER A N     1 
ATOM   2908  C  CA    . SER A 1 1678 ? 180.517 146.922 118.640 1.00 47.67  ? 1678 SER A CA    1 
ATOM   2909  C  C     . SER A 1 1678 ? 180.174 145.767 119.577 1.00 54.76  ? 1678 SER A C     1 
ATOM   2910  O  O     . SER A 1 1678 ? 180.696 144.657 119.457 1.00 61.85  ? 1678 SER A O     1 
ATOM   2911  C  CB    . SER A 1 1678 ? 179.318 147.274 117.761 1.00 52.31  ? 1678 SER A CB    1 
ATOM   2912  O  OG    . SER A 1 1678 ? 178.200 147.643 118.547 1.00 59.36  ? 1678 SER A OG    1 
ATOM   2913  N  N     . ARG A 1 1679 ? 179.281 146.043 120.529 1.00 51.81  ? 1679 ARG A N     1 
ATOM   2914  C  CA    . ARG A 1 1679 ? 178.849 144.996 121.450 1.00 55.78  ? 1679 ARG A CA    1 
ATOM   2915  C  C     . ARG A 1 1679 ? 178.051 143.919 120.726 1.00 67.91  ? 1679 ARG A C     1 
ATOM   2916  O  O     . ARG A 1 1679 ? 178.129 142.736 121.079 1.00 70.15  ? 1679 ARG A O     1 
ATOM   2917  C  CB    . ARG A 1 1679 ? 178.037 145.601 122.597 1.00 59.98  ? 1679 ARG A CB    1 
ATOM   2918  C  CG    . ARG A 1 1679 ? 176.725 146.236 122.178 1.00 73.02  ? 1679 ARG A CG    1 
ATOM   2919  C  CD    . ARG A 1 1679 ? 175.965 146.784 123.373 1.00 83.14  ? 1679 ARG A CD    1 
ATOM   2920  N  NE    . ARG A 1 1679 ? 174.743 147.467 122.964 1.00 93.91  ? 1679 ARG A NE    1 
ATOM   2921  C  CZ    . ARG A 1 1679 ? 173.574 146.869 122.788 1.00 100.72 ? 1679 ARG A CZ    1 
ATOM   2922  N  NH1   . ARG A 1 1679 ? 173.427 145.568 122.978 1.00 103.70 ? 1679 ARG A NH1   1 
ATOM   2923  N  NH2   . ARG A 1 1679 ? 172.525 147.594 122.409 1.00 98.63  ? 1679 ARG A NH2   1 
ATOM   2924  N  N     . GLU A 1 1680 ? 177.272 144.308 119.714 1.00 69.26  ? 1680 GLU A N     1 
ATOM   2925  C  CA    . GLU A 1 1680 ? 176.531 143.326 118.930 1.00 63.36  ? 1680 GLU A CA    1 
ATOM   2926  C  C     . GLU A 1 1680 ? 177.471 142.440 118.124 1.00 65.18  ? 1680 GLU A C     1 
ATOM   2927  O  O     . GLU A 1 1680 ? 177.249 141.230 118.010 1.00 74.57  ? 1680 GLU A O     1 
ATOM   2928  C  CB    . GLU A 1 1680 ? 175.537 144.029 118.007 1.00 60.19  ? 1680 GLU A CB    1 
ATOM   2929  C  CG    . GLU A 1 1680 ? 174.472 144.835 118.731 1.00 68.65  ? 1680 GLU A CG    1 
ATOM   2930  C  CD    . GLU A 1 1680 ? 174.929 146.242 119.064 1.00 74.23  ? 1680 GLU A CD    1 
ATOM   2931  O  OE1   . GLU A 1 1680 ? 176.050 146.614 118.661 1.00 73.32  ? 1680 GLU A OE1   1 
ATOM   2932  O  OE2   . GLU A 1 1680 ? 174.168 146.975 119.729 1.00 77.43  ? 1680 GLU A OE2   1 
ATOM   2933  N  N     . GLY A 1 1681 ? 178.524 143.023 117.558 1.00 57.97  ? 1681 GLY A N     1 
ATOM   2934  C  CA    . GLY A 1 1681 ? 179.460 142.271 116.748 1.00 63.20  ? 1681 GLY A CA    1 
ATOM   2935  C  C     . GLY A 1 1681 ? 179.862 143.004 115.487 1.00 63.14  ? 1681 GLY A C     1 
ATOM   2936  O  O     . GLY A 1 1681 ? 180.767 142.567 114.770 1.00 65.53  ? 1681 GLY A O     1 
ATOM   2937  N  N     . GLU A 1 1682 ? 179.189 144.116 115.202 1.00 60.83  ? 1682 GLU A N     1 
ATOM   2938  C  CA    . GLU A 1 1682 ? 179.533 144.923 114.040 1.00 55.13  ? 1682 GLU A CA    1 
ATOM   2939  C  C     . GLU A 1 1682 ? 180.940 145.486 114.185 1.00 52.15  ? 1682 GLU A C     1 
ATOM   2940  O  O     . GLU A 1 1682 ? 181.330 145.960 115.255 1.00 56.81  ? 1682 GLU A O     1 
ATOM   2941  C  CB    . GLU A 1 1682 ? 178.524 146.057 113.869 1.00 50.95  ? 1682 GLU A CB    1 
ATOM   2942  C  CG    . GLU A 1 1682 ? 178.647 146.800 112.554 1.00 51.43  ? 1682 GLU A CG    1 
ATOM   2943  C  CD    . GLU A 1 1682 ? 177.512 147.773 112.331 1.00 51.30  ? 1682 GLU A CD    1 
ATOM   2944  O  OE1   . GLU A 1 1682 ? 177.381 148.727 113.123 1.00 54.30  ? 1682 GLU A OE1   1 
ATOM   2945  O  OE2   . GLU A 1 1682 ? 176.747 147.581 111.363 1.00 49.59  ? 1682 GLU A OE2   1 
ATOM   2946  N  N     . GLU A 1 1683 ? 181.705 145.437 113.099 1.00 49.89  ? 1683 GLU A N     1 
ATOM   2947  C  CA    . GLU A 1 1683 ? 183.105 145.831 113.111 1.00 48.79  ? 1683 GLU A CA    1 
ATOM   2948  C  C     . GLU A 1 1683 ? 183.354 146.936 112.097 1.00 49.02  ? 1683 GLU A C     1 
ATOM   2949  O  O     . GLU A 1 1683 ? 182.741 146.962 111.025 1.00 57.34  ? 1683 GLU A O     1 
ATOM   2950  C  CB    . GLU A 1 1683 ? 184.015 144.637 112.808 1.00 55.29  ? 1683 GLU A CB    1 
ATOM   2951  C  CG    . GLU A 1 1683 ? 183.864 143.481 113.780 1.00 65.25  ? 1683 GLU A CG    1 
ATOM   2952  C  CD    . GLU A 1 1683 ? 184.718 142.288 113.402 1.00 78.75  ? 1683 GLU A CD    1 
ATOM   2953  O  OE1   . GLU A 1 1683 ? 185.425 142.363 112.375 1.00 79.56  ? 1683 GLU A OE1   1 
ATOM   2954  O  OE2   . GLU A 1 1683 ? 184.684 141.275 114.132 1.00 78.88  ? 1683 GLU A OE2   1 
ATOM   2955  N  N     . VAL A 1 1684 ? 184.257 147.846 112.448 1.00 44.83  ? 1684 VAL A N     1 
ATOM   2956  C  CA    . VAL A 1 1684 ? 184.720 148.907 111.564 1.00 46.04  ? 1684 VAL A CA    1 
ATOM   2957  C  C     . VAL A 1 1684 ? 186.210 148.695 111.343 1.00 45.27  ? 1684 VAL A C     1 
ATOM   2958  O  O     . VAL A 1 1684 ? 186.988 148.680 112.306 1.00 47.51  ? 1684 VAL A O     1 
ATOM   2959  C  CB    . VAL A 1 1684 ? 184.442 150.301 112.149 1.00 43.89  ? 1684 VAL A CB    1 
ATOM   2960  C  CG1   . VAL A 1 1684 ? 185.112 151.377 111.310 1.00 39.49  ? 1684 VAL A CG1   1 
ATOM   2961  C  CG2   . VAL A 1 1684 ? 182.951 150.547 112.248 1.00 48.22  ? 1684 VAL A CG2   1 
ATOM   2962  N  N     . MET A 1 1685 ? 186.603 148.527 110.083 1.00 46.54  ? 1685 MET A N     1 
ATOM   2963  C  CA    . MET A 1 1685 ? 187.998 148.324 109.716 1.00 46.19  ? 1685 MET A CA    1 
ATOM   2964  C  C     . MET A 1 1685 ? 188.651 149.669 109.432 1.00 45.62  ? 1685 MET A C     1 
ATOM   2965  O  O     . MET A 1 1685 ? 188.194 150.411 108.558 1.00 56.55  ? 1685 MET A O     1 
ATOM   2966  C  CB    . MET A 1 1685 ? 188.113 147.431 108.479 1.00 61.00  ? 1685 MET A CB    1 
ATOM   2967  C  CG    . MET A 1 1685 ? 187.632 145.999 108.649 1.00 72.83  ? 1685 MET A CG    1 
ATOM   2968  S  SD    . MET A 1 1685 ? 188.540 145.067 109.891 1.00 80.24  ? 1685 MET A SD    1 
ATOM   2969  C  CE    . MET A 1 1685 ? 187.353 145.078 111.224 1.00 58.44  ? 1685 MET A CE    1 
ATOM   2970  N  N     . PHE A 1 1686 ? 189.724 149.972 110.155 1.00 42.49  ? 1686 PHE A N     1 
ATOM   2971  C  CA    . PHE A 1 1686 ? 190.430 151.227 109.944 1.00 44.65  ? 1686 PHE A CA    1 
ATOM   2972  C  C     . PHE A 1 1686 ? 191.045 151.269 108.552 1.00 49.91  ? 1686 PHE A C     1 
ATOM   2973  O  O     . PHE A 1 1686 ? 191.549 150.263 108.048 1.00 56.12  ? 1686 PHE A O     1 
ATOM   2974  C  CB    . PHE A 1 1686 ? 191.519 151.414 110.999 1.00 47.31  ? 1686 PHE A CB    1 
ATOM   2975  C  CG    . PHE A 1 1686 ? 190.994 151.721 112.371 1.00 44.05  ? 1686 PHE A CG    1 
ATOM   2976  C  CD1   . PHE A 1 1686 ? 189.645 151.937 112.583 1.00 40.92  ? 1686 PHE A CD1   1 
ATOM   2977  C  CD2   . PHE A 1 1686 ? 191.856 151.800 113.448 1.00 46.51  ? 1686 PHE A CD2   1 
ATOM   2978  C  CE1   . PHE A 1 1686 ? 189.168 152.221 113.842 1.00 43.08  ? 1686 PHE A CE1   1 
ATOM   2979  C  CE2   . PHE A 1 1686 ? 191.384 152.082 114.709 1.00 43.08  ? 1686 PHE A CE2   1 
ATOM   2980  C  CZ    . PHE A 1 1686 ? 190.040 152.295 114.906 1.00 42.25  ? 1686 PHE A CZ    1 
ATOM   2981  N  N     . LYS A 1 1687 ? 190.991 152.446 107.925 1.00 50.72  ? 1687 LYS A N     1 
ATOM   2982  C  CA    . LYS A 1 1687 ? 191.605 152.611 106.611 1.00 56.65  ? 1687 LYS A CA    1 
ATOM   2983  C  C     . LYS A 1 1687 ? 193.118 152.454 106.695 1.00 65.87  ? 1687 LYS A C     1 
ATOM   2984  O  O     . LYS A 1 1687 ? 193.726 151.731 105.898 1.00 68.20  ? 1687 LYS A O     1 
ATOM   2985  C  CB    . LYS A 1 1687 ? 191.231 153.973 106.028 1.00 58.49  ? 1687 LYS A CB    1 
ATOM   2986  C  CG    . LYS A 1 1687 ? 189.744 154.147 105.778 1.00 58.44  ? 1687 LYS A CG    1 
ATOM   2987  C  CD    . LYS A 1 1687 ? 189.240 153.149 104.751 1.00 59.29  ? 1687 LYS A CD    1 
ATOM   2988  C  CE    . LYS A 1 1687 ? 187.820 153.468 104.326 1.00 53.43  ? 1687 LYS A CE    1 
ATOM   2989  N  NZ    . LYS A 1 1687 ? 187.368 152.584 103.219 1.00 58.00  ? 1687 LYS A NZ    1 
ATOM   2990  N  N     . THR A 1 1688 ? 193.742 153.128 107.657 1.00 66.63  ? 1688 THR A N     1 
ATOM   2991  C  CA    . THR A 1 1688 ? 195.160 152.946 107.965 1.00 64.03  ? 1688 THR A CA    1 
ATOM   2992  C  C     . THR A 1 1688 ? 195.264 152.455 109.400 1.00 65.27  ? 1688 THR A C     1 
ATOM   2993  O  O     . THR A 1 1688 ? 195.058 153.240 110.343 1.00 63.42  ? 1688 THR A O     1 
ATOM   2994  C  CB    . THR A 1 1688 ? 195.949 154.241 107.779 1.00 65.67  ? 1688 THR A CB    1 
ATOM   2995  O  OG1   . THR A 1 1688 ? 195.631 155.152 108.838 1.00 68.32  ? 1688 THR A OG1   1 
ATOM   2996  C  CG2   . THR A 1 1688 ? 195.612 154.886 106.443 1.00 65.09  ? 1688 THR A CG2   1 
ATOM   2997  N  N     . PRO A 1 1689 ? 195.561 151.175 109.618 1.00 67.58  ? 1689 PRO A N     1 
ATOM   2998  C  CA    . PRO A 1 1689 ? 195.534 150.630 110.980 1.00 64.15  ? 1689 PRO A CA    1 
ATOM   2999  C  C     . PRO A 1 1689 ? 196.532 151.322 111.898 1.00 64.88  ? 1689 PRO A C     1 
ATOM   3000  O  O     . PRO A 1 1689 ? 197.616 151.730 111.478 1.00 65.12  ? 1689 PRO A O     1 
ATOM   3001  C  CB    . PRO A 1 1689 ? 195.891 149.154 110.772 1.00 62.46  ? 1689 PRO A CB    1 
ATOM   3002  C  CG    . PRO A 1 1689 ? 195.521 148.873 109.354 1.00 60.38  ? 1689 PRO A CG    1 
ATOM   3003  C  CD    . PRO A 1 1689 ? 195.831 150.136 108.613 1.00 62.30  ? 1689 PRO A CD    1 
ATOM   3004  N  N     . VAL A 1 1690 ? 196.147 151.452 113.164 1.00 61.70  ? 1690 VAL A N     1 
ATOM   3005  C  CA    . VAL A 1 1690 ? 196.991 152.083 114.171 1.00 58.72  ? 1690 VAL A CA    1 
ATOM   3006  C  C     . VAL A 1 1690 ? 197.972 151.053 114.713 1.00 65.72  ? 1690 VAL A C     1 
ATOM   3007  O  O     . VAL A 1 1690 ? 197.577 149.953 115.116 1.00 70.52  ? 1690 VAL A O     1 
ATOM   3008  C  CB    . VAL A 1 1690 ? 196.135 152.678 115.299 1.00 54.25  ? 1690 VAL A CB    1 
ATOM   3009  C  CG1   . VAL A 1 1690 ? 197.018 153.216 116.409 1.00 54.58  ? 1690 VAL A CG1   1 
ATOM   3010  C  CG2   . VAL A 1 1690 ? 195.229 153.766 114.754 1.00 55.98  ? 1690 VAL A CG2   1 
ATOM   3011  N  N     . SER A 1 1691 ? 199.254 151.408 114.731 1.00 64.37  ? 1691 SER A N     1 
ATOM   3012  C  CA    . SER A 1 1691 ? 200.312 150.509 115.170 1.00 64.34  ? 1691 SER A CA    1 
ATOM   3013  C  C     . SER A 1 1691 ? 200.685 150.827 116.613 1.00 68.31  ? 1691 SER A C     1 
ATOM   3014  O  O     . SER A 1 1691 ? 201.182 151.920 116.903 1.00 72.47  ? 1691 SER A O     1 
ATOM   3015  C  CB    . SER A 1 1691 ? 201.535 150.629 114.262 1.00 67.65  ? 1691 SER A CB    1 
ATOM   3016  O  OG    . SER A 1 1691 ? 202.553 149.729 114.660 1.00 75.96  ? 1691 SER A OG    1 
ATOM   3017  N  N     . ILE A 1 1692 ? 200.445 149.870 117.512 1.00 65.84  ? 1692 ILE A N     1 
ATOM   3018  C  CA    . ILE A 1 1692 ? 200.809 150.052 118.913 1.00 58.76  ? 1692 ILE A CA    1 
ATOM   3019  C  C     . ILE A 1 1692 ? 202.323 150.046 119.084 1.00 61.08  ? 1692 ILE A C     1 
ATOM   3020  O  O     . ILE A 1 1692 ? 202.867 150.775 119.919 1.00 70.86  ? 1692 ILE A O     1 
ATOM   3021  C  CB    . ILE A 1 1692 ? 200.138 148.977 119.786 1.00 55.86  ? 1692 ILE A CB    1 
ATOM   3022  C  CG1   . ILE A 1 1692 ? 198.620 149.041 119.642 1.00 59.08  ? 1692 ILE A CG1   1 
ATOM   3023  C  CG2   . ILE A 1 1692 ? 200.531 149.143 121.242 1.00 58.75  ? 1692 ILE A CG2   1 
ATOM   3024  C  CD1   . ILE A 1 1692 ? 197.909 147.900 120.317 1.00 61.39  ? 1692 ILE A CD1   1 
ATOM   3025  N  N     . THR A 1 1693 ? 203.025 149.216 118.312 1.00 64.27  ? 1693 THR A N     1 
ATOM   3026  C  CA    . THR A 1 1693 ? 204.474 149.114 118.456 1.00 71.07  ? 1693 THR A CA    1 
ATOM   3027  C  C     . THR A 1 1693 ? 205.156 150.445 118.161 1.00 71.63  ? 1693 THR A C     1 
ATOM   3028  O  O     . THR A 1 1693 ? 206.061 150.865 118.890 1.00 77.93  ? 1693 THR A O     1 
ATOM   3029  C  CB    . THR A 1 1693 ? 205.015 148.015 117.540 1.00 78.28  ? 1693 THR A CB    1 
ATOM   3030  O  OG1   . THR A 1 1693 ? 204.660 146.733 118.073 1.00 82.66  ? 1693 THR A OG1   1 
ATOM   3031  C  CG2   . THR A 1 1693 ? 206.528 148.106 117.422 1.00 74.38  ? 1693 THR A CG2   1 
ATOM   3032  N  N     . GLU A 1 1694 ? 204.727 151.131 117.101 1.00 68.78  ? 1694 GLU A N     1 
ATOM   3033  C  CA    . GLU A 1 1694 ? 205.318 152.422 116.769 1.00 72.08  ? 1694 GLU A CA    1 
ATOM   3034  C  C     . GLU A 1 1694 ? 204.879 153.523 117.723 1.00 74.25  ? 1694 GLU A C     1 
ATOM   3035  O  O     . GLU A 1 1694 ? 205.540 154.565 117.793 1.00 76.47  ? 1694 GLU A O     1 
ATOM   3036  C  CB    . GLU A 1 1694 ? 204.969 152.807 115.331 1.00 76.43  ? 1694 GLU A CB    1 
ATOM   3037  C  CG    . GLU A 1 1694 ? 205.795 152.083 114.283 1.00 87.34  ? 1694 GLU A CG    1 
ATOM   3038  C  CD    . GLU A 1 1694 ? 204.958 151.582 113.124 1.00 90.77  ? 1694 GLU A CD    1 
ATOM   3039  O  OE1   . GLU A 1 1694 ? 203.953 152.242 112.787 1.00 87.69  ? 1694 GLU A OE1   1 
ATOM   3040  O  OE2   . GLU A 1 1694 ? 205.301 150.526 112.553 1.00 88.33  ? 1694 GLU A OE2   1 
ATOM   3041  N  N     . HIS A 1 1695 ? 203.785 153.320 118.453 1.00 69.56  ? 1695 HIS A N     1 
ATOM   3042  C  CA    . HIS A 1 1695 ? 203.265 154.294 119.412 1.00 64.42  ? 1695 HIS A CA    1 
ATOM   3043  C  C     . HIS A 1 1695 ? 202.984 153.576 120.725 1.00 65.30  ? 1695 HIS A C     1 
ATOM   3044  O  O     . HIS A 1 1695 ? 201.825 153.377 121.106 1.00 63.45  ? 1695 HIS A O     1 
ATOM   3045  C  CB    . HIS A 1 1695 ? 202.008 154.971 118.868 1.00 59.74  ? 1695 HIS A CB    1 
ATOM   3046  C  CG    . HIS A 1 1695 ? 202.196 155.585 117.517 1.00 66.31  ? 1695 HIS A CG    1 
ATOM   3047  N  ND1   . HIS A 1 1695 ? 202.967 156.708 117.310 1.00 67.81  ? 1695 HIS A ND1   1 
ATOM   3048  C  CD2   . HIS A 1 1695 ? 201.736 155.216 116.298 1.00 72.02  ? 1695 HIS A CD2   1 
ATOM   3049  C  CE1   . HIS A 1 1695 ? 202.958 157.016 116.025 1.00 72.09  ? 1695 HIS A CE1   1 
ATOM   3050  N  NE2   . HIS A 1 1695 ? 202.219 156.125 115.389 1.00 75.30  ? 1695 HIS A NE2   1 
ATOM   3051  N  N     . PRO A 1 1696 ? 204.034 153.161 121.439 1.00 64.50  ? 1696 PRO A N     1 
ATOM   3052  C  CA    . PRO A 1 1696 ? 203.828 152.298 122.615 1.00 59.13  ? 1696 PRO A CA    1 
ATOM   3053  C  C     . PRO A 1 1696 ? 203.023 152.944 123.728 1.00 60.54  ? 1696 PRO A C     1 
ATOM   3054  O  O     . PRO A 1 1696 ? 202.367 152.227 124.492 1.00 60.16  ? 1696 PRO A O     1 
ATOM   3055  C  CB    . PRO A 1 1696 ? 205.260 151.979 123.063 1.00 57.17  ? 1696 PRO A CB    1 
ATOM   3056  C  CG    . PRO A 1 1696 ? 206.072 153.118 122.555 1.00 63.14  ? 1696 PRO A CG    1 
ATOM   3057  C  CD    . PRO A 1 1696 ? 205.453 153.506 121.248 1.00 62.20  ? 1696 PRO A CD    1 
ATOM   3058  N  N     . LYS A 1 1697 ? 203.058 154.269 123.851 1.00 63.67  ? 1697 LYS A N     1 
ATOM   3059  C  CA    . LYS A 1 1697 ? 202.309 154.938 124.907 1.00 62.53  ? 1697 LYS A CA    1 
ATOM   3060  C  C     . LYS A 1 1697 ? 200.817 154.702 124.727 1.00 56.21  ? 1697 LYS A C     1 
ATOM   3061  O  O     . LYS A 1 1697 ? 200.286 154.833 123.622 1.00 58.05  ? 1697 LYS A O     1 
ATOM   3062  C  CB    . LYS A 1 1697 ? 202.613 156.435 124.902 1.00 62.95  ? 1697 LYS A CB    1 
ATOM   3063  C  CG    . LYS A 1 1697 ? 204.087 156.771 125.003 1.00 71.77  ? 1697 LYS A CG    1 
ATOM   3064  C  CD    . LYS A 1 1697 ? 204.309 158.273 125.003 1.00 86.32  ? 1697 LYS A CD    1 
ATOM   3065  C  CE    . LYS A 1 1697 ? 205.791 158.611 125.005 1.00 97.93  ? 1697 LYS A CE    1 
ATOM   3066  N  NZ    . LYS A 1 1697 ? 206.508 157.977 123.863 1.00 99.11  ? 1697 LYS A NZ    1 
ATOM   3067  N  N     . ILE A 1 1698 ? 200.138 154.362 125.825 1.00 51.07  ? 1698 ILE A N     1 
ATOM   3068  C  CA    . ILE A 1 1698 ? 198.712 154.053 125.753 1.00 48.97  ? 1698 ILE A CA    1 
ATOM   3069  C  C     . ILE A 1 1698 ? 197.927 155.265 125.274 1.00 51.26  ? 1698 ILE A C     1 
ATOM   3070  O  O     . ILE A 1 1698 ? 197.022 155.146 124.440 1.00 54.67  ? 1698 ILE A O     1 
ATOM   3071  C  CB    . ILE A 1 1698 ? 198.201 153.552 127.116 1.00 57.55  ? 1698 ILE A CB    1 
ATOM   3072  C  CG1   . ILE A 1 1698 ? 199.115 152.453 127.656 1.00 72.47  ? 1698 ILE A CG1   1 
ATOM   3073  C  CG2   . ILE A 1 1698 ? 196.772 153.047 126.993 1.00 46.63  ? 1698 ILE A CG2   1 
ATOM   3074  C  CD1   . ILE A 1 1698 ? 199.100 151.187 126.828 1.00 74.29  ? 1698 ILE A CD1   1 
ATOM   3075  N  N     . ASN A 1 1699 ? 198.261 156.448 125.791 1.00 51.86  ? 1699 ASN A N     1 
ATOM   3076  C  CA    . ASN A 1 1699 ? 197.559 157.660 125.382 1.00 45.83  ? 1699 ASN A CA    1 
ATOM   3077  C  C     . ASN A 1 1699 ? 197.725 157.909 123.891 1.00 46.68  ? 1699 ASN A C     1 
ATOM   3078  O  O     . ASN A 1 1699 ? 196.756 158.219 123.191 1.00 50.18  ? 1699 ASN A O     1 
ATOM   3079  C  CB    . ASN A 1 1699 ? 198.071 158.859 126.179 1.00 47.15  ? 1699 ASN A CB    1 
ATOM   3080  C  CG    . ASN A 1 1699 ? 197.671 158.806 127.636 1.00 53.51  ? 1699 ASN A CG    1 
ATOM   3081  O  OD1   . ASN A 1 1699 ? 197.995 159.704 128.410 1.00 56.13  ? 1699 ASN A OD1   1 
ATOM   3082  N  ND2   . ASN A 1 1699 ? 196.964 157.753 128.020 1.00 54.35  ? 1699 ASN A ND2   1 
ATOM   3083  N  N     . GLU A 1 1700 ? 198.950 157.758 123.384 1.00 49.09  ? 1700 GLU A N     1 
ATOM   3084  C  CA    . GLU A 1 1700 ? 199.225 158.074 121.987 1.00 48.79  ? 1700 GLU A CA    1 
ATOM   3085  C  C     . GLU A 1 1700 ? 198.449 157.159 121.047 1.00 49.58  ? 1700 GLU A C     1 
ATOM   3086  O  O     . GLU A 1 1700 ? 197.724 157.629 120.160 1.00 49.85  ? 1700 GLU A O     1 
ATOM   3087  C  CB    . GLU A 1 1700 ? 200.727 157.971 121.723 1.00 50.83  ? 1700 GLU A CB    1 
ATOM   3088  C  CG    . GLU A 1 1700 ? 201.143 158.355 120.317 1.00 64.09  ? 1700 GLU A CG    1 
ATOM   3089  C  CD    . GLU A 1 1700 ? 202.643 158.285 120.118 1.00 76.60  ? 1700 GLU A CD    1 
ATOM   3090  O  OE1   . GLU A 1 1700 ? 203.355 157.915 121.075 1.00 74.77  ? 1700 GLU A OE1   1 
ATOM   3091  O  OE2   . GLU A 1 1700 ? 203.111 158.595 119.003 1.00 79.89  ? 1700 GLU A OE2   1 
ATOM   3092  N  N     . TRP A 1 1701 ? 198.568 155.843 121.239 1.00 47.42  ? 1701 TRP A N     1 
ATOM   3093  C  CA    . TRP A 1 1701 ? 197.908 154.934 120.311 1.00 41.93  ? 1701 TRP A CA    1 
ATOM   3094  C  C     . TRP A 1 1701 ? 196.402 154.909 120.526 1.00 41.38  ? 1701 TRP A C     1 
ATOM   3095  O  O     . TRP A 1 1701 ? 195.656 154.690 119.571 1.00 52.08  ? 1701 TRP A O     1 
ATOM   3096  C  CB    . TRP A 1 1701 ? 198.523 153.529 120.395 1.00 45.13  ? 1701 TRP A CB    1 
ATOM   3097  C  CG    . TRP A 1 1701 ? 198.140 152.671 121.569 1.00 47.33  ? 1701 TRP A CG    1 
ATOM   3098  C  CD1   . TRP A 1 1701 ? 198.901 152.413 122.667 1.00 50.20  ? 1701 TRP A CD1   1 
ATOM   3099  C  CD2   . TRP A 1 1701 ? 196.939 151.903 121.728 1.00 46.73  ? 1701 TRP A CD2   1 
ATOM   3100  N  NE1   . TRP A 1 1701 ? 198.240 151.565 123.518 1.00 47.88  ? 1701 TRP A NE1   1 
ATOM   3101  C  CE2   . TRP A 1 1701 ? 197.033 151.235 122.963 1.00 45.21  ? 1701 TRP A CE2   1 
ATOM   3102  C  CE3   . TRP A 1 1701 ? 195.788 151.730 120.956 1.00 47.64  ? 1701 TRP A CE3   1 
ATOM   3103  C  CZ2   . TRP A 1 1701 ? 196.022 150.409 123.444 1.00 43.88  ? 1701 TRP A CZ2   1 
ATOM   3104  C  CZ3   . TRP A 1 1701 ? 194.785 150.910 121.437 1.00 47.11  ? 1701 TRP A CZ3   1 
ATOM   3105  C  CH2   . TRP A 1 1701 ? 194.909 150.260 122.668 1.00 42.99  ? 1701 TRP A CH2   1 
ATOM   3106  N  N     . LEU A 1 1702 ? 195.925 155.184 121.742 1.00 35.17  ? 1702 LEU A N     1 
ATOM   3107  C  CA    . LEU A 1 1702 ? 194.482 155.262 121.952 1.00 34.16  ? 1702 LEU A CA    1 
ATOM   3108  C  C     . LEU A 1 1702 ? 193.891 156.501 121.282 1.00 36.92  ? 1702 LEU A C     1 
ATOM   3109  O  O     . LEU A 1 1702 ? 192.802 156.441 120.692 1.00 44.95  ? 1702 LEU A O     1 
ATOM   3110  C  CB    . LEU A 1 1702 ? 194.180 155.244 123.448 1.00 37.68  ? 1702 LEU A CB    1 
ATOM   3111  C  CG    . LEU A 1 1702 ? 192.880 154.576 123.890 1.00 36.39  ? 1702 LEU A CG    1 
ATOM   3112  C  CD1   . LEU A 1 1702 ? 192.700 153.249 123.183 1.00 37.08  ? 1702 LEU A CD1   1 
ATOM   3113  C  CD2   . LEU A 1 1702 ? 192.889 154.373 125.392 1.00 32.08  ? 1702 LEU A CD2   1 
ATOM   3114  N  N     . THR A 1 1703 ? 194.600 157.631 121.348 1.00 38.66  ? 1703 THR A N     1 
ATOM   3115  C  CA    . THR A 1 1703 ? 194.170 158.820 120.621 1.00 37.04  ? 1703 THR A CA    1 
ATOM   3116  C  C     . THR A 1 1703 ? 194.180 158.570 119.120 1.00 40.88  ? 1703 THR A C     1 
ATOM   3117  O  O     . THR A 1 1703 ? 193.273 159.010 118.402 1.00 45.03  ? 1703 THR A O     1 
ATOM   3118  C  CB    . THR A 1 1703 ? 195.073 160.002 120.975 1.00 41.38  ? 1703 THR A CB    1 
ATOM   3119  O  OG1   . THR A 1 1703 ? 194.893 160.346 122.354 1.00 43.44  ? 1703 THR A OG1   1 
ATOM   3120  C  CG2   . THR A 1 1703 ? 194.742 161.208 120.116 1.00 43.63  ? 1703 THR A CG2   1 
ATOM   3121  N  N     . LEU A 1 1704 ? 195.202 157.868 118.626 1.00 40.91  ? 1704 LEU A N     1 
ATOM   3122  C  CA    . LEU A 1 1704 ? 195.229 157.522 117.209 1.00 40.29  ? 1704 LEU A CA    1 
ATOM   3123  C  C     . LEU A 1 1704 ? 194.070 156.603 116.842 1.00 40.74  ? 1704 LEU A C     1 
ATOM   3124  O  O     . LEU A 1 1704 ? 193.511 156.713 115.748 1.00 45.00  ? 1704 LEU A O     1 
ATOM   3125  C  CB    . LEU A 1 1704 ? 196.565 156.881 116.844 1.00 43.35  ? 1704 LEU A CB    1 
ATOM   3126  C  CG    . LEU A 1 1704 ? 197.771 157.815 116.925 1.00 49.99  ? 1704 LEU A CG    1 
ATOM   3127  C  CD1   . LEU A 1 1704 ? 198.986 157.162 116.310 1.00 50.42  ? 1704 LEU A CD1   1 
ATOM   3128  C  CD2   . LEU A 1 1704 ? 197.466 159.132 116.237 1.00 55.71  ? 1704 LEU A CD2   1 
ATOM   3129  N  N     . VAL A 1 1705 ? 193.694 155.691 117.741 1.00 37.42  ? 1705 VAL A N     1 
ATOM   3130  C  CA    . VAL A 1 1705 ? 192.538 154.831 117.492 1.00 35.33  ? 1705 VAL A CA    1 
ATOM   3131  C  C     . VAL A 1 1705 ? 191.270 155.663 117.365 1.00 37.72  ? 1705 VAL A C     1 
ATOM   3132  O  O     . VAL A 1 1705 ? 190.453 155.439 116.469 1.00 45.20  ? 1705 VAL A O     1 
ATOM   3133  C  CB    . VAL A 1 1705 ? 192.404 153.763 118.592 1.00 37.74  ? 1705 VAL A CB    1 
ATOM   3134  C  CG1   . VAL A 1 1705 ? 191.100 153.012 118.436 1.00 39.27  ? 1705 VAL A CG1   1 
ATOM   3135  C  CG2   . VAL A 1 1705 ? 193.542 152.779 118.496 1.00 41.65  ? 1705 VAL A CG2   1 
ATOM   3136  N  N     . GLU A 1 1706 ? 191.082 156.634 118.261 1.00 37.03  ? 1706 GLU A N     1 
ATOM   3137  C  CA    . GLU A 1 1706 ? 189.889 157.477 118.172 1.00 33.82  ? 1706 GLU A CA    1 
ATOM   3138  C  C     . GLU A 1 1706 ? 189.879 158.301 116.884 1.00 35.71  ? 1706 GLU A C     1 
ATOM   3139  O  O     . GLU A 1 1706 ? 188.849 158.398 116.196 1.00 41.16  ? 1706 GLU A O     1 
ATOM   3140  C  CB    . GLU A 1 1706 ? 189.799 158.392 119.391 1.00 30.21  ? 1706 GLU A CB    1 
ATOM   3141  C  CG    . GLU A 1 1706 ? 188.573 159.279 119.397 1.00 38.80  ? 1706 GLU A CG    1 
ATOM   3142  C  CD    . GLU A 1 1706 ? 188.606 160.314 120.500 1.00 54.09  ? 1706 GLU A CD    1 
ATOM   3143  O  OE1   . GLU A 1 1706 ? 189.638 160.409 121.196 1.00 58.78  ? 1706 GLU A OE1   1 
ATOM   3144  O  OE2   . GLU A 1 1706 ? 187.598 161.030 120.676 1.00 51.39  ? 1706 GLU A OE2   1 
ATOM   3145  N  N     . LYS A 1 1707 ? 191.022 158.897 116.540 1.00 34.35  ? 1707 LYS A N     1 
ATOM   3146  C  CA    . LYS A 1 1707 ? 191.102 159.708 115.330 1.00 33.40  ? 1707 LYS A CA    1 
ATOM   3147  C  C     . LYS A 1 1707 ? 190.858 158.867 114.084 1.00 36.41  ? 1707 LYS A C     1 
ATOM   3148  O  O     . LYS A 1 1707 ? 190.164 159.302 113.157 1.00 42.33  ? 1707 LYS A O     1 
ATOM   3149  C  CB    . LYS A 1 1707 ? 192.460 160.406 115.263 1.00 44.41  ? 1707 LYS A CB    1 
ATOM   3150  C  CG    . LYS A 1 1707 ? 192.991 160.637 113.862 1.00 45.29  ? 1707 LYS A CG    1 
ATOM   3151  C  CD    . LYS A 1 1707 ? 194.482 160.924 113.891 1.00 56.80  ? 1707 LYS A CD    1 
ATOM   3152  C  CE    . LYS A 1 1707 ? 195.080 160.899 112.495 1.00 74.82  ? 1707 LYS A CE    1 
ATOM   3153  N  NZ    . LYS A 1 1707 ? 196.565 161.018 112.526 1.00 83.29  ? 1707 LYS A NZ    1 
ATOM   3154  N  N     . GLU A 1 1708 ? 191.412 157.654 114.043 1.00 36.52  ? 1708 GLU A N     1 
ATOM   3155  C  CA    . GLU A 1 1708 ? 191.185 156.781 112.901 1.00 33.95  ? 1708 GLU A CA    1 
ATOM   3156  C  C     . GLU A 1 1708 ? 189.758 156.261 112.867 1.00 33.97  ? 1708 GLU A C     1 
ATOM   3157  O  O     . GLU A 1 1708 ? 189.221 156.027 111.785 1.00 39.70  ? 1708 GLU A O     1 
ATOM   3158  C  CB    . GLU A 1 1708 ? 192.176 155.621 112.910 1.00 39.89  ? 1708 GLU A CB    1 
ATOM   3159  C  CG    . GLU A 1 1708 ? 193.345 155.827 111.966 1.00 49.67  ? 1708 GLU A CG    1 
ATOM   3160  C  CD    . GLU A 1 1708 ? 192.957 155.652 110.511 1.00 58.72  ? 1708 GLU A CD    1 
ATOM   3161  O  OE1   . GLU A 1 1708 ? 191.816 155.222 110.240 1.00 51.07  ? 1708 GLU A OE1   1 
ATOM   3162  O  OE2   . GLU A 1 1708 ? 193.789 155.957 109.634 1.00 68.82  ? 1708 GLU A OE2   1 
ATOM   3163  N  N     . MET A 1 1709 ? 189.129 156.079 114.029 1.00 32.46  ? 1709 MET A N     1 
ATOM   3164  C  CA    . MET A 1 1709 ? 187.698 155.804 114.065 1.00 31.18  ? 1709 MET A CA    1 
ATOM   3165  C  C     . MET A 1 1709 ? 186.925 156.880 113.324 1.00 33.35  ? 1709 MET A C     1 
ATOM   3166  O  O     . MET A 1 1709 ? 186.116 156.586 112.435 1.00 35.44  ? 1709 MET A O     1 
ATOM   3167  C  CB    . MET A 1 1709 ? 187.222 155.726 115.513 1.00 30.81  ? 1709 MET A CB    1 
ATOM   3168  C  CG    . MET A 1 1709 ? 185.754 155.403 115.666 1.00 33.56  ? 1709 MET A CG    1 
ATOM   3169  S  SD    . MET A 1 1709 ? 185.261 155.313 117.394 1.00 48.30  ? 1709 MET A SD    1 
ATOM   3170  C  CE    . MET A 1 1709 ? 185.323 157.044 117.845 1.00 25.67  ? 1709 MET A CE    1 
ATOM   3171  N  N     . ARG A 1 1710 ? 187.172 158.141 113.678 1.00 35.51  ? 1710 ARG A N     1 
ATOM   3172  C  CA    . ARG A 1 1710 ? 186.439 159.235 113.045 1.00 26.61  ? 1710 ARG A CA    1 
ATOM   3173  C  C     . ARG A 1 1710 ? 186.742 159.321 111.552 1.00 29.72  ? 1710 ARG A C     1 
ATOM   3174  O  O     . ARG A 1 1710 ? 185.829 159.492 110.733 1.00 35.94  ? 1710 ARG A O     1 
ATOM   3175  C  CB    . ARG A 1 1710 ? 186.766 160.551 113.746 1.00 28.13  ? 1710 ARG A CB    1 
ATOM   3176  C  CG    . ARG A 1 1710 ? 186.199 160.632 115.150 1.00 31.55  ? 1710 ARG A CG    1 
ATOM   3177  C  CD    . ARG A 1 1710 ? 186.777 161.797 115.922 1.00 38.01  ? 1710 ARG A CD    1 
ATOM   3178  N  NE    . ARG A 1 1710 ? 186.161 161.926 117.237 1.00 42.87  ? 1710 ARG A NE    1 
ATOM   3179  C  CZ    . ARG A 1 1710 ? 186.580 162.758 118.180 1.00 60.36  ? 1710 ARG A CZ    1 
ATOM   3180  N  NH1   . ARG A 1 1710 ? 187.620 163.552 117.988 1.00 61.78  ? 1710 ARG A NH1   1 
ATOM   3181  N  NH2   . ARG A 1 1710 ? 185.941 162.792 119.346 1.00 57.68  ? 1710 ARG A NH2   1 
ATOM   3182  N  N     . VAL A 1 1711 ? 188.016 159.188 111.175 1.00 29.96  ? 1711 VAL A N     1 
ATOM   3183  C  CA    . VAL A 1 1711 ? 188.396 159.297 109.768 1.00 30.10  ? 1711 VAL A CA    1 
ATOM   3184  C  C     . VAL A 1 1711 ? 187.790 158.161 108.950 1.00 34.97  ? 1711 VAL A C     1 
ATOM   3185  O  O     . VAL A 1 1711 ? 187.280 158.376 107.841 1.00 40.31  ? 1711 VAL A O     1 
ATOM   3186  C  CB    . VAL A 1 1711 ? 189.929 159.336 109.636 1.00 30.17  ? 1711 VAL A CB    1 
ATOM   3187  C  CG1   . VAL A 1 1711 ? 190.341 159.213 108.185 1.00 36.44  ? 1711 VAL A CG1   1 
ATOM   3188  C  CG2   . VAL A 1 1711 ? 190.476 160.619 110.231 1.00 31.33  ? 1711 VAL A CG2   1 
ATOM   3189  N  N     . THR A 1 1712 ? 187.844 156.934 109.474 1.00 32.54  ? 1712 THR A N     1 
ATOM   3190  C  CA    . THR A 1 1712 ? 187.264 155.794 108.780 1.00 29.88  ? 1712 THR A CA    1 
ATOM   3191  C  C     . THR A 1 1712 ? 185.760 155.945 108.637 1.00 32.24  ? 1712 THR A C     1 
ATOM   3192  O  O     . THR A 1 1712 ? 185.200 155.636 107.581 1.00 43.15  ? 1712 THR A O     1 
ATOM   3193  C  CB    . THR A 1 1712 ? 187.597 154.504 109.524 1.00 34.15  ? 1712 THR A CB    1 
ATOM   3194  O  OG1   . THR A 1 1712 ? 189.018 154.378 109.647 1.00 48.22  ? 1712 THR A OG1   1 
ATOM   3195  C  CG2   . THR A 1 1712 ? 187.049 153.311 108.776 1.00 35.80  ? 1712 THR A CG2   1 
ATOM   3196  N  N     . LEU A 1 1713 ? 185.084 156.409 109.691 1.00 30.74  ? 1713 LEU A N     1 
ATOM   3197  C  CA    . LEU A 1 1713 ? 183.647 156.627 109.588 1.00 27.18  ? 1713 LEU A CA    1 
ATOM   3198  C  C     . LEU A 1 1713 ? 183.328 157.666 108.522 1.00 30.06  ? 1713 LEU A C     1 
ATOM   3199  O  O     . LEU A 1 1713 ? 182.388 157.491 107.742 1.00 34.20  ? 1713 LEU A O     1 
ATOM   3200  C  CB    . LEU A 1 1713 ? 183.078 157.048 110.940 1.00 27.35  ? 1713 LEU A CB    1 
ATOM   3201  C  CG    . LEU A 1 1713 ? 182.765 155.912 111.911 1.00 29.34  ? 1713 LEU A CG    1 
ATOM   3202  C  CD1   . LEU A 1 1713 ? 182.052 156.448 113.131 1.00 31.18  ? 1713 LEU A CD1   1 
ATOM   3203  C  CD2   . LEU A 1 1713 ? 181.929 154.845 111.232 1.00 28.72  ? 1713 LEU A CD2   1 
ATOM   3204  N  N     . ALA A 1 1714 ? 184.112 158.743 108.458 1.00 28.46  ? 1714 ALA A N     1 
ATOM   3205  C  CA    . ALA A 1 1714 ? 183.874 159.767 107.444 1.00 25.95  ? 1714 ALA A CA    1 
ATOM   3206  C  C     . ALA A 1 1714 ? 184.057 159.209 106.036 1.00 31.88  ? 1714 ALA A C     1 
ATOM   3207  O  O     . ALA A 1 1714 ? 183.229 159.447 105.148 1.00 40.87  ? 1714 ALA A O     1 
ATOM   3208  C  CB    . ALA A 1 1714 ? 184.802 160.958 107.677 1.00 35.65  ? 1714 ALA A CB    1 
ATOM   3209  N  N     . LYS A 1 1715 ? 185.138 158.457 105.812 1.00 32.46  ? 1715 LYS A N     1 
ATOM   3210  C  CA    . LYS A 1 1715 ? 185.391 157.924 104.474 1.00 32.76  ? 1715 LYS A CA    1 
ATOM   3211  C  C     . LYS A 1 1715 ? 184.340 156.894 104.073 1.00 37.28  ? 1715 LYS A C     1 
ATOM   3212  O  O     . LYS A 1 1715 ? 183.876 156.880 102.923 1.00 45.67  ? 1715 LYS A O     1 
ATOM   3213  C  CB    . LYS A 1 1715 ? 186.792 157.320 104.400 1.00 37.74  ? 1715 LYS A CB    1 
ATOM   3214  C  CG    . LYS A 1 1715 ? 187.911 158.339 104.527 1.00 48.15  ? 1715 LYS A CG    1 
ATOM   3215  C  CD    . LYS A 1 1715 ? 189.273 157.681 104.389 1.00 61.37  ? 1715 LYS A CD    1 
ATOM   3216  C  CE    . LYS A 1 1715 ? 190.393 158.684 104.594 1.00 61.39  ? 1715 LYS A CE    1 
ATOM   3217  N  NZ    . LYS A 1 1715 ? 190.442 159.691 103.499 1.00 58.93  ? 1715 LYS A NZ    1 
ATOM   3218  N  N     . LEU A 1 1716 ? 183.950 156.024 105.006 1.00 35.63  ? 1716 LEU A N     1 
ATOM   3219  C  CA    . LEU A 1 1716 ? 182.921 155.037 104.707 1.00 34.73  ? 1716 LEU A CA    1 
ATOM   3220  C  C     . LEU A 1 1716 ? 181.577 155.704 104.457 1.00 34.99  ? 1716 LEU A C     1 
ATOM   3221  O  O     . LEU A 1 1716 ? 180.803 155.244 103.614 1.00 39.71  ? 1716 LEU A O     1 
ATOM   3222  C  CB    . LEU A 1 1716 ? 182.818 154.023 105.843 1.00 30.97  ? 1716 LEU A CB    1 
ATOM   3223  C  CG    . LEU A 1 1716 ? 183.995 153.072 106.042 1.00 32.04  ? 1716 LEU A CG    1 
ATOM   3224  C  CD1   . LEU A 1 1716 ? 183.673 152.067 107.129 1.00 31.25  ? 1716 LEU A CD1   1 
ATOM   3225  C  CD2   . LEU A 1 1716 ? 184.333 152.368 104.745 1.00 40.94  ? 1716 LEU A CD2   1 
ATOM   3226  N  N     . LEU A 1 1717 ? 181.280 156.792 105.173 1.00 31.72  ? 1717 LEU A N     1 
ATOM   3227  C  CA    . LEU A 1 1717 ? 180.059 157.541 104.899 1.00 31.11  ? 1717 LEU A CA    1 
ATOM   3228  C  C     . LEU A 1 1717 ? 180.098 158.168 103.515 1.00 31.19  ? 1717 LEU A C     1 
ATOM   3229  O  O     . LEU A 1 1717 ? 179.083 158.200 102.814 1.00 39.12  ? 1717 LEU A O     1 
ATOM   3230  C  CB    . LEU A 1 1717 ? 179.846 158.618 105.961 1.00 30.49  ? 1717 LEU A CB    1 
ATOM   3231  C  CG    . LEU A 1 1717 ? 178.670 159.550 105.680 1.00 26.92  ? 1717 LEU A CG    1 
ATOM   3232  C  CD1   . LEU A 1 1717 ? 177.370 158.780 105.719 1.00 24.80  ? 1717 LEU A CD1   1 
ATOM   3233  C  CD2   . LEU A 1 1717 ? 178.641 160.700 106.661 1.00 35.47  ? 1717 LEU A CD2   1 
ATOM   3234  N  N     . ALA A 1 1718 ? 181.258 158.684 103.106 1.00 30.11  ? 1718 ALA A N     1 
ATOM   3235  C  CA    . ALA A 1 1718 ? 181.378 159.234 101.759 1.00 34.00  ? 1718 ALA A CA    1 
ATOM   3236  C  C     . ALA A 1 1718 ? 181.107 158.166 100.707 1.00 37.74  ? 1718 ALA A C     1 
ATOM   3237  O  O     . ALA A 1 1718 ? 180.349 158.389 99.753  1.00 42.10  ? 1718 ALA A O     1 
ATOM   3238  C  CB    . ALA A 1 1718 ? 182.763 159.848 101.563 1.00 34.46  ? 1718 ALA A CB    1 
ATOM   3239  N  N     . GLU A 1 1719 ? 181.708 156.985 100.877 1.00 37.85  ? 1719 GLU A N     1 
ATOM   3240  C  CA    . GLU A 1 1719 ? 181.474 155.897 99.929  1.00 40.06  ? 1719 GLU A CA    1 
ATOM   3241  C  C     . GLU A 1 1719 ? 180.011 155.460 99.931  1.00 39.07  ? 1719 GLU A C     1 
ATOM   3242  O  O     . GLU A 1 1719 ? 179.421 155.221 98.869  1.00 44.99  ? 1719 GLU A O     1 
ATOM   3243  C  CB    . GLU A 1 1719 ? 182.381 154.710 100.249 1.00 44.38  ? 1719 GLU A CB    1 
ATOM   3244  C  CG    . GLU A 1 1719 ? 183.864 155.025 100.247 1.00 50.17  ? 1719 GLU A CG    1 
ATOM   3245  C  CD    . GLU A 1 1719 ? 184.709 153.814 100.590 1.00 62.00  ? 1719 GLU A CD    1 
ATOM   3246  O  OE1   . GLU A 1 1719 ? 184.135 152.722 100.784 1.00 60.72  ? 1719 GLU A OE1   1 
ATOM   3247  O  OE2   . GLU A 1 1719 ? 185.947 153.953 100.665 1.00 69.99  ? 1719 GLU A OE2   1 
ATOM   3248  N  N     . SER A 1 1720 ? 179.412 155.347 101.117 1.00 33.34  ? 1720 SER A N     1 
ATOM   3249  C  CA    . SER A 1 1720 ? 178.022 154.921 101.217 1.00 31.58  ? 1720 SER A CA    1 
ATOM   3250  C  C     . SER A 1 1720 ? 177.086 155.924 100.561 1.00 35.96  ? 1720 SER A C     1 
ATOM   3251  O  O     . SER A 1 1720 ? 176.121 155.536 99.897  1.00 42.50  ? 1720 SER A O     1 
ATOM   3252  C  CB    . SER A 1 1720 ? 177.644 154.716 102.681 1.00 33.37  ? 1720 SER A CB    1 
ATOM   3253  O  OG    . SER A 1 1720 ? 176.283 154.352 102.807 1.00 37.22  ? 1720 SER A OG    1 
ATOM   3254  N  N     . VAL A 1 1721 ? 177.344 157.219 100.750 1.00 38.73  ? 1721 VAL A N     1 
ATOM   3255  C  CA    . VAL A 1 1721 ? 176.527 158.244 100.109 1.00 33.29  ? 1721 VAL A CA    1 
ATOM   3256  C  C     . VAL A 1 1721 ? 176.677 158.169 98.597  1.00 41.30  ? 1721 VAL A C     1 
ATOM   3257  O  O     . VAL A 1 1721 ? 175.691 158.262 97.854  1.00 52.20  ? 1721 VAL A O     1 
ATOM   3258  C  CB    . VAL A 1 1721 ? 176.894 159.636 100.651 1.00 31.48  ? 1721 VAL A CB    1 
ATOM   3259  C  CG1   . VAL A 1 1721 ? 176.403 160.722 99.713  1.00 36.87  ? 1721 VAL A CG1   1 
ATOM   3260  C  CG2   . VAL A 1 1721 ? 176.310 159.829 102.036 1.00 33.96  ? 1721 VAL A CG2   1 
ATOM   3261  N  N     . THR A 1 1722 ? 177.911 157.990 98.117  1.00 41.80  ? 1722 THR A N     1 
ATOM   3262  C  CA    . THR A 1 1722 ? 178.127 157.868 96.680  1.00 43.75  ? 1722 THR A CA    1 
ATOM   3263  C  C     . THR A 1 1722 ? 177.358 156.684 96.108  1.00 45.00  ? 1722 THR A C     1 
ATOM   3264  O  O     . THR A 1 1722 ? 176.811 156.765 95.002  1.00 54.43  ? 1722 THR A O     1 
ATOM   3265  C  CB    . THR A 1 1722 ? 179.619 157.735 96.380  1.00 48.51  ? 1722 THR A CB    1 
ATOM   3266  O  OG1   . THR A 1 1722 ? 180.319 158.864 96.918  1.00 54.53  ? 1722 THR A OG1   1 
ATOM   3267  C  CG2   . THR A 1 1722 ? 179.857 157.674 94.881  1.00 46.46  ? 1722 THR A CG2   1 
ATOM   3268  N  N     . GLU A 1 1723 ? 177.301 155.575 96.848  1.00 44.28  ? 1723 GLU A N     1 
ATOM   3269  C  CA    . GLU A 1 1723 ? 176.556 154.415 96.362  1.00 44.32  ? 1723 GLU A CA    1 
ATOM   3270  C  C     . GLU A 1 1723 ? 175.048 154.638 96.430  1.00 46.70  ? 1723 GLU A C     1 
ATOM   3271  O  O     . GLU A 1 1723 ? 174.321 154.261 95.505  1.00 53.18  ? 1723 GLU A O     1 
ATOM   3272  C  CB    . GLU A 1 1723 ? 176.942 153.164 97.149  1.00 43.11  ? 1723 GLU A CB    1 
ATOM   3273  C  CG    . GLU A 1 1723 ? 178.407 152.786 97.040  1.00 51.00  ? 1723 GLU A CG    1 
ATOM   3274  C  CD    . GLU A 1 1723 ? 178.678 151.379 97.526  1.00 55.29  ? 1723 GLU A CD    1 
ATOM   3275  O  OE1   . GLU A 1 1723 ? 177.705 150.656 97.824  1.00 49.35  ? 1723 GLU A OE1   1 
ATOM   3276  O  OE2   . GLU A 1 1723 ? 179.864 150.997 97.613  1.00 60.65  ? 1723 GLU A OE2   1 
ATOM   3277  N  N     . VAL A 1 1724 ? 174.558 155.245 97.513  1.00 43.85  ? 1724 VAL A N     1 
ATOM   3278  C  CA    . VAL A 1 1724 ? 173.116 155.365 97.710  1.00 42.55  ? 1724 VAL A CA    1 
ATOM   3279  C  C     . VAL A 1 1724 ? 172.504 156.458 96.842  1.00 50.59  ? 1724 VAL A C     1 
ATOM   3280  O  O     . VAL A 1 1724 ? 171.287 156.450 96.615  1.00 59.93  ? 1724 VAL A O     1 
ATOM   3281  C  CB    . VAL A 1 1724 ? 172.791 155.615 99.194  1.00 38.18  ? 1724 VAL A CB    1 
ATOM   3282  C  CG1   . VAL A 1 1724 ? 173.168 157.027 99.598  1.00 39.99  ? 1724 VAL A CG1   1 
ATOM   3283  C  CG2   . VAL A 1 1724 ? 171.326 155.331 99.490  1.00 39.64  ? 1724 VAL A CG2   1 
ATOM   3284  N  N     . GLU A 1 1725 ? 173.309 157.402 96.342  1.00 49.02  ? 1725 GLU A N     1 
ATOM   3285  C  CA    . GLU A 1 1725 ? 172.776 158.364 95.383  1.00 51.47  ? 1725 GLU A CA    1 
ATOM   3286  C  C     . GLU A 1 1725 ? 172.280 157.677 94.117  1.00 60.62  ? 1725 GLU A C     1 
ATOM   3287  O  O     . GLU A 1 1725 ? 171.399 158.206 93.429  1.00 63.62  ? 1725 GLU A O     1 
ATOM   3288  C  CB    . GLU A 1 1725 ? 173.828 159.418 95.038  1.00 51.89  ? 1725 GLU A CB    1 
ATOM   3289  C  CG    . GLU A 1 1725 ? 174.174 160.345 96.186  1.00 57.74  ? 1725 GLU A CG    1 
ATOM   3290  C  CD    . GLU A 1 1725 ? 175.235 161.359 95.814  1.00 71.13  ? 1725 GLU A CD    1 
ATOM   3291  O  OE1   . GLU A 1 1725 ? 175.789 161.258 94.699  1.00 72.56  ? 1725 GLU A OE1   1 
ATOM   3292  O  OE2   . GLU A 1 1725 ? 175.515 162.255 96.636  1.00 73.14  ? 1725 GLU A OE2   1 
ATOM   3293  N  N     . ILE A 1 1726 ? 172.834 156.508 93.788  1.00 58.97  ? 1726 ILE A N     1 
ATOM   3294  C  CA    . ILE A 1 1726 ? 172.335 155.744 92.648  1.00 58.00  ? 1726 ILE A CA    1 
ATOM   3295  C  C     . ILE A 1 1726 ? 170.920 155.249 92.916  1.00 58.65  ? 1726 ILE A C     1 
ATOM   3296  O  O     . ILE A 1 1726 ? 170.043 155.330 92.047  1.00 65.11  ? 1726 ILE A O     1 
ATOM   3297  C  CB    . ILE A 1 1726 ? 173.290 154.581 92.322  1.00 61.21  ? 1726 ILE A CB    1 
ATOM   3298  C  CG1   . ILE A 1 1726 ? 174.728 155.088 92.203  1.00 55.89  ? 1726 ILE A CG1   1 
ATOM   3299  C  CG2   . ILE A 1 1726 ? 172.862 153.885 91.044  1.00 64.80  ? 1726 ILE A CG2   1 
ATOM   3300  C  CD1   . ILE A 1 1726 ? 174.909 156.176 91.171  1.00 51.20  ? 1726 ILE A CD1   1 
ATOM   3301  N  N     . PHE A 1 1727 ? 170.674 154.724 94.119  1.00 57.49  ? 1727 PHE A N     1 
ATOM   3302  C  CA    . PHE A 1 1727 ? 169.331 154.270 94.468  1.00 62.57  ? 1727 PHE A CA    1 
ATOM   3303  C  C     . PHE A 1 1727 ? 168.358 155.438 94.546  1.00 64.92  ? 1727 PHE A C     1 
ATOM   3304  O  O     . PHE A 1 1727 ? 167.194 155.312 94.149  1.00 69.79  ? 1727 PHE A O     1 
ATOM   3305  C  CB    . PHE A 1 1727 ? 169.353 153.508 95.792  1.00 61.48  ? 1727 PHE A CB    1 
ATOM   3306  C  CG    . PHE A 1 1727 ? 170.392 152.429 95.853  1.00 60.35  ? 1727 PHE A CG    1 
ATOM   3307  C  CD1   . PHE A 1 1727 ? 170.487 151.488 94.846  1.00 63.32  ? 1727 PHE A CD1   1 
ATOM   3308  C  CD2   . PHE A 1 1727 ? 171.265 152.351 96.922  1.00 53.93  ? 1727 PHE A CD2   1 
ATOM   3309  C  CE1   . PHE A 1 1727 ? 171.439 150.496 94.899  1.00 64.99  ? 1727 PHE A CE1   1 
ATOM   3310  C  CE2   . PHE A 1 1727 ? 172.219 151.360 96.981  1.00 53.34  ? 1727 PHE A CE2   1 
ATOM   3311  C  CZ    . PHE A 1 1727 ? 172.307 150.431 95.969  1.00 60.14  ? 1727 PHE A CZ    1 
ATOM   3312  N  N     . GLY A 1 1728 ? 168.811 156.578 95.070  1.00 59.96  ? 1728 GLY A N     1 
ATOM   3313  C  CA    . GLY A 1 1728 ? 167.942 157.741 95.142  1.00 63.34  ? 1728 GLY A CA    1 
ATOM   3314  C  C     . GLY A 1 1728 ? 167.511 158.236 93.774  1.00 69.07  ? 1728 GLY A C     1 
ATOM   3315  O  O     . GLY A 1 1728 ? 166.344 158.576 93.565  1.00 67.62  ? 1728 GLY A O     1 
ATOM   3316  N  N     . LYS A 1 1729 ? 168.443 158.282 92.825  1.00 72.69  ? 1729 LYS A N     1 
ATOM   3317  C  CA    . LYS A 1 1729 ? 168.141 158.702 91.457  1.00 75.22  ? 1729 LYS A CA    1 
ATOM   3318  C  C     . LYS A 1 1729 ? 167.792 157.487 90.594  1.00 76.11  ? 1729 LYS A C     1 
ATOM   3319  O  O     . LYS A 1 1729 ? 168.464 157.161 89.616  1.00 75.53  ? 1729 LYS A O     1 
ATOM   3320  C  CB    . LYS A 1 1729 ? 169.316 159.477 90.872  1.00 73.82  ? 1729 LYS A CB    1 
ATOM   3321  C  CG    . LYS A 1 1729 ? 169.611 160.796 91.570  1.00 71.93  ? 1729 LYS A CG    1 
ATOM   3322  C  CD    . LYS A 1 1729 ? 168.400 161.711 91.567  1.00 78.49  ? 1729 LYS A CD    1 
ATOM   3323  C  CE    . LYS A 1 1729 ? 168.817 163.173 91.585  1.00 80.90  ? 1729 LYS A CE    1 
ATOM   3324  N  NZ    . LYS A 1 1729 ? 168.156 163.930 92.683  1.00 76.22  ? 1729 LYS A NZ    1 
ATOM   3325  N  N     . ALA A 1 1730 ? 166.712 156.811 90.980  1.00 77.57  ? 1730 ALA A N     1 
ATOM   3326  C  CA    . ALA A 1 1730 ? 166.277 155.616 90.272  1.00 88.00  ? 1730 ALA A CA    1 
ATOM   3327  C  C     . ALA A 1 1730 ? 164.782 155.433 90.475  1.00 92.21  ? 1730 ALA A C     1 
ATOM   3328  O  O     . ALA A 1 1730 ? 164.190 155.981 91.408  1.00 87.72  ? 1730 ALA A O     1 
ATOM   3329  C  CB    . ALA A 1 1730 ? 167.041 154.374 90.742  1.00 78.06  ? 1730 ALA A CB    1 
ATOM   3330  N  N     . THR A 1 1731 ? 164.179 154.646 89.583  1.00 95.20  ? 1731 THR A N     1 
ATOM   3331  C  CA    . THR A 1 1731 ? 162.757 154.348 89.639  1.00 94.17  ? 1731 THR A CA    1 
ATOM   3332  C  C     . THR A 1 1731 ? 162.454 152.902 90.002  1.00 92.94  ? 1731 THR A C     1 
ATOM   3333  O  O     . THR A 1 1731 ? 161.286 152.574 90.238  1.00 94.44  ? 1731 THR A O     1 
ATOM   3334  C  CB    . THR A 1 1731 ? 162.088 154.675 88.296  1.00 92.39  ? 1731 THR A CB    1 
ATOM   3335  O  OG1   . THR A 1 1731 ? 162.666 153.867 87.263  1.00 91.25  ? 1731 THR A OG1   1 
ATOM   3336  C  CG2   . THR A 1 1731 ? 162.278 156.144 87.950  1.00 92.57  ? 1731 THR A CG2   1 
ATOM   3337  N  N     . SER A 1 1732 ? 163.463 152.032 90.048  1.00 90.98  ? 1732 SER A N     1 
ATOM   3338  C  CA    . SER A 1 1732 ? 163.251 150.632 90.415  1.00 87.01  ? 1732 SER A CA    1 
ATOM   3339  C  C     . SER A 1 1732 ? 164.530 150.136 91.083  1.00 81.51  ? 1732 SER A C     1 
ATOM   3340  O  O     . SER A 1 1732 ? 165.486 149.763 90.398  1.00 82.25  ? 1732 SER A O     1 
ATOM   3341  C  CB    . SER A 1 1732 ? 162.894 149.791 89.198  1.00 93.84  ? 1732 SER A CB    1 
ATOM   3342  O  OG    . SER A 1 1732 ? 163.958 149.774 88.262  1.00 99.75  ? 1732 SER A OG    1 
ATOM   3343  N  N     . ILE A 1 1733 ? 164.536 150.133 92.411  1.00 77.44  ? 1733 ILE A N     1 
ATOM   3344  C  CA    . ILE A 1 1733 ? 165.687 149.651 93.165  1.00 72.37  ? 1733 ILE A CA    1 
ATOM   3345  C  C     . ILE A 1 1733 ? 165.682 148.130 93.154  1.00 74.00  ? 1733 ILE A C     1 
ATOM   3346  O  O     . ILE A 1 1733 ? 164.694 147.496 93.546  1.00 72.20  ? 1733 ILE A O     1 
ATOM   3347  C  CB    . ILE A 1 1733 ? 165.672 150.194 94.604  1.00 68.89  ? 1733 ILE A CB    1 
ATOM   3348  C  CG1   . ILE A 1 1733 ? 165.787 151.722 94.623  1.00 74.90  ? 1733 ILE A CG1   1 
ATOM   3349  C  CG2   . ILE A 1 1733 ? 166.789 149.568 95.418  1.00 63.85  ? 1733 ILE A CG2   1 
ATOM   3350  C  CD1   . ILE A 1 1733 ? 164.465 152.456 94.555  1.00 71.29  ? 1733 ILE A CD1   1 
ATOM   3351  N  N     . ASP A 1 1734 ? 166.779 147.541 92.702  1.00 74.03  ? 1734 ASP A N     1 
ATOM   3352  C  CA    . ASP A 1 1734 ? 166.915 146.091 92.722  1.00 68.46  ? 1734 ASP A CA    1 
ATOM   3353  C  C     . ASP A 1 1734 ? 167.084 145.625 94.162  1.00 67.77  ? 1734 ASP A C     1 
ATOM   3354  O  O     . ASP A 1 1734 ? 167.978 146.121 94.860  1.00 69.12  ? 1734 ASP A O     1 
ATOM   3355  C  CB    . ASP A 1 1734 ? 168.104 145.655 91.872  1.00 65.74  ? 1734 ASP A CB    1 
ATOM   3356  C  CG    . ASP A 1 1734 ? 168.345 144.160 91.930  1.00 69.11  ? 1734 ASP A CG    1 
ATOM   3357  O  OD1   . ASP A 1 1734 ? 167.410 143.394 91.620  1.00 72.72  ? 1734 ASP A OD1   1 
ATOM   3358  O  OD2   . ASP A 1 1734 ? 169.471 143.750 92.279  1.00 70.76  ? 1734 ASP A OD2   1 
ATOM   3359  N  N     . PRO A 1 1735 ? 166.251 144.704 94.653  1.00 65.50  ? 1735 PRO A N     1 
ATOM   3360  C  CA    . PRO A 1 1735 ? 166.376 144.288 96.060  1.00 60.05  ? 1735 PRO A CA    1 
ATOM   3361  C  C     . PRO A 1 1735 ? 167.736 143.712 96.405  1.00 62.26  ? 1735 PRO A C     1 
ATOM   3362  O  O     . PRO A 1 1735 ? 168.249 143.959 97.504  1.00 64.63  ? 1735 PRO A O     1 
ATOM   3363  C  CB    . PRO A 1 1735 ? 165.261 143.243 96.212  1.00 66.73  ? 1735 PRO A CB    1 
ATOM   3364  C  CG    . PRO A 1 1735 ? 164.289 143.559 95.125  1.00 72.62  ? 1735 PRO A CG    1 
ATOM   3365  C  CD    . PRO A 1 1735 ? 165.115 144.055 93.979  1.00 70.06  ? 1735 PRO A CD    1 
ATOM   3366  N  N     . ASN A 1 1736 ? 168.344 142.957 95.488  1.00 65.93  ? 1736 ASN A N     1 
ATOM   3367  C  CA    . ASN A 1 1736 ? 169.634 142.338 95.775  1.00 67.88  ? 1736 ASN A CA    1 
ATOM   3368  C  C     . ASN A 1 1736 ? 170.725 143.390 95.937  1.00 65.89  ? 1736 ASN A C     1 
ATOM   3369  O  O     . ASN A 1 1736 ? 171.535 143.322 96.869  1.00 65.10  ? 1736 ASN A O     1 
ATOM   3370  C  CB    . ASN A 1 1736 ? 169.992 141.346 94.668  1.00 73.02  ? 1736 ASN A CB    1 
ATOM   3371  C  CG    . ASN A 1 1736 ? 171.282 140.600 94.944  1.00 85.23  ? 1736 ASN A CG    1 
ATOM   3372  O  OD1   . ASN A 1 1736 ? 172.373 141.165 94.862  1.00 87.48  ? 1736 ASN A OD1   1 
ATOM   3373  N  ND2   . ASN A 1 1736 ? 171.162 139.320 95.280  1.00 84.14  ? 1736 ASN A ND2   1 
ATOM   3374  N  N     . THR A 1 1737 ? 170.761 144.376 95.038  1.00 62.95  ? 1737 THR A N     1 
ATOM   3375  C  CA    . THR A 1 1737 ? 171.768 145.428 95.133  1.00 61.07  ? 1737 THR A CA    1 
ATOM   3376  C  C     . THR A 1 1737 ? 171.575 146.268 96.390  1.00 56.07  ? 1737 THR A C     1 
ATOM   3377  O  O     . THR A 1 1737 ? 172.550 146.634 97.059  1.00 57.56  ? 1737 THR A O     1 
ATOM   3378  C  CB    . THR A 1 1737 ? 171.724 146.310 93.886  1.00 66.33  ? 1737 THR A CB    1 
ATOM   3379  O  OG1   . THR A 1 1737 ? 171.963 145.506 92.724  1.00 77.13  ? 1737 THR A OG1   1 
ATOM   3380  C  CG2   . THR A 1 1737 ? 172.787 147.389 93.961  1.00 64.36  ? 1737 THR A CG2   1 
ATOM   3381  N  N     . TYR A 1 1738 ? 170.322 146.583 96.725  1.00 53.71  ? 1738 TYR A N     1 
ATOM   3382  C  CA    . TYR A 1 1738 ? 170.052 147.351 97.935  1.00 50.54  ? 1738 TYR A CA    1 
ATOM   3383  C  C     . TYR A 1 1738 ? 170.481 146.585 99.180  1.00 48.56  ? 1738 TYR A C     1 
ATOM   3384  O  O     . TYR A 1 1738 ? 171.080 147.161 100.095 1.00 52.70  ? 1738 TYR A O     1 
ATOM   3385  C  CB    . TYR A 1 1738 ? 168.569 147.709 98.006  1.00 49.73  ? 1738 TYR A CB    1 
ATOM   3386  C  CG    . TYR A 1 1738 ? 168.274 148.922 98.854  1.00 50.88  ? 1738 TYR A CG    1 
ATOM   3387  C  CD1   . TYR A 1 1738 ? 168.787 150.166 98.521  1.00 56.77  ? 1738 TYR A CD1   1 
ATOM   3388  C  CD2   . TYR A 1 1738 ? 167.482 148.823 99.988  1.00 45.99  ? 1738 TYR A CD2   1 
ATOM   3389  C  CE1   . TYR A 1 1738 ? 168.522 151.276 99.293  1.00 54.10  ? 1738 TYR A CE1   1 
ATOM   3390  C  CE2   . TYR A 1 1738 ? 167.213 149.928 100.766 1.00 43.01  ? 1738 TYR A CE2   1 
ATOM   3391  C  CZ    . TYR A 1 1738 ? 167.734 151.151 100.415 1.00 51.92  ? 1738 TYR A CZ    1 
ATOM   3392  O  OH    . TYR A 1 1738 ? 167.465 152.255 101.190 1.00 46.83  ? 1738 TYR A OH    1 
ATOM   3393  N  N     . ILE A 1 1739 ? 170.193 145.283 99.229  1.00 49.11  ? 1739 ILE A N     1 
ATOM   3394  C  CA    . ILE A 1 1739 ? 170.597 144.482 100.379 1.00 45.93  ? 1739 ILE A CA    1 
ATOM   3395  C  C     . ILE A 1 1739 ? 172.115 144.378 100.455 1.00 47.68  ? 1739 ILE A C     1 
ATOM   3396  O  O     . ILE A 1 1739 ? 172.697 144.393 101.546 1.00 50.02  ? 1739 ILE A O     1 
ATOM   3397  C  CB    . ILE A 1 1739 ? 169.926 143.097 100.326 1.00 48.07  ? 1739 ILE A CB    1 
ATOM   3398  C  CG1   . ILE A 1 1739 ? 168.426 143.230 100.584 1.00 51.12  ? 1739 ILE A CG1   1 
ATOM   3399  C  CG2   . ILE A 1 1739 ? 170.545 142.157 101.341 1.00 46.66  ? 1739 ILE A CG2   1 
ATOM   3400  C  CD1   . ILE A 1 1739 ? 168.091 143.645 101.995 1.00 49.34  ? 1739 ILE A CD1   1 
ATOM   3401  N  N     . THR A 1 1740 ? 172.783 144.276 99.303  1.00 47.36  ? 1740 THR A N     1 
ATOM   3402  C  CA    . THR A 1 1740 ? 174.243 144.259 99.297  1.00 48.18  ? 1740 THR A CA    1 
ATOM   3403  C  C     . THR A 1 1740 ? 174.810 145.557 99.859  1.00 49.30  ? 1740 THR A C     1 
ATOM   3404  O  O     . THR A 1 1740 ? 175.743 145.539 100.672 1.00 54.02  ? 1740 THR A O     1 
ATOM   3405  C  CB    . THR A 1 1740 ? 174.758 144.021 97.879  1.00 49.04  ? 1740 THR A CB    1 
ATOM   3406  O  OG1   . THR A 1 1740 ? 174.276 142.760 97.400  1.00 60.31  ? 1740 THR A OG1   1 
ATOM   3407  C  CG2   . THR A 1 1740 ? 176.276 144.016 97.856  1.00 45.55  ? 1740 THR A CG2   1 
ATOM   3408  N  N     . TRP A 1 1741 ? 174.249 146.696 99.444  1.00 47.73  ? 1741 TRP A N     1 
ATOM   3409  C  CA    . TRP A 1 1741 ? 174.701 147.978 99.975  1.00 41.17  ? 1741 TRP A CA    1 
ATOM   3410  C  C     . TRP A 1 1741 ? 174.462 148.067 101.477 1.00 40.17  ? 1741 TRP A C     1 
ATOM   3411  O  O     . TRP A 1 1741 ? 175.315 148.564 102.220 1.00 42.07  ? 1741 TRP A O     1 
ATOM   3412  C  CB    . TRP A 1 1741 ? 173.996 149.129 99.260  1.00 42.66  ? 1741 TRP A CB    1 
ATOM   3413  C  CG    . TRP A 1 1741 ? 174.212 150.449 99.931  1.00 42.85  ? 1741 TRP A CG    1 
ATOM   3414  C  CD1   . TRP A 1 1741 ? 175.335 151.219 99.879  1.00 40.34  ? 1741 TRP A CD1   1 
ATOM   3415  C  CD2   . TRP A 1 1741 ? 173.288 151.143 100.776 1.00 40.88  ? 1741 TRP A CD2   1 
ATOM   3416  N  NE1   . TRP A 1 1741 ? 175.163 152.355 100.629 1.00 37.02  ? 1741 TRP A NE1   1 
ATOM   3417  C  CE2   . TRP A 1 1741 ? 173.915 152.331 101.192 1.00 37.89  ? 1741 TRP A CE2   1 
ATOM   3418  C  CE3   . TRP A 1 1741 ? 171.990 150.877 101.218 1.00 36.71  ? 1741 TRP A CE3   1 
ATOM   3419  C  CZ2   . TRP A 1 1741 ? 173.290 153.250 102.026 1.00 34.35  ? 1741 TRP A CZ2   1 
ATOM   3420  C  CZ3   . TRP A 1 1741 ? 171.372 151.790 102.046 1.00 33.56  ? 1741 TRP A CZ3   1 
ATOM   3421  C  CH2   . TRP A 1 1741 ? 172.021 152.963 102.440 1.00 30.49  ? 1741 TRP A CH2   1 
ATOM   3422  N  N     . ILE A 1 1742 ? 173.302 147.597 101.939 1.00 38.77  ? 1742 ILE A N     1 
ATOM   3423  C  CA    . ILE A 1 1742 ? 173.003 147.626 103.369 1.00 36.27  ? 1742 ILE A CA    1 
ATOM   3424  C  C     . ILE A 1 1742 ? 173.997 146.771 104.142 1.00 42.55  ? 1742 ILE A C     1 
ATOM   3425  O  O     . ILE A 1 1742 ? 174.481 147.166 105.210 1.00 45.02  ? 1742 ILE A O     1 
ATOM   3426  C  CB    . ILE A 1 1742 ? 171.553 147.173 103.618 1.00 33.16  ? 1742 ILE A CB    1 
ATOM   3427  C  CG1   . ILE A 1 1742 ? 170.574 148.163 102.994 1.00 37.60  ? 1742 ILE A CG1   1 
ATOM   3428  C  CG2   . ILE A 1 1742 ? 171.283 147.026 105.099 1.00 31.87  ? 1742 ILE A CG2   1 
ATOM   3429  C  CD1   . ILE A 1 1742 ? 169.175 147.628 102.874 1.00 42.63  ? 1742 ILE A CD1   1 
ATOM   3430  N  N     . ASP A 1 1743 ? 174.316 145.586 103.620 1.00 43.04  ? 1743 ASP A N     1 
ATOM   3431  C  CA    . ASP A 1 1743 ? 175.264 144.707 104.296 1.00 41.58  ? 1743 ASP A CA    1 
ATOM   3432  C  C     . ASP A 1 1743 ? 176.667 145.299 104.304 1.00 42.38  ? 1743 ASP A C     1 
ATOM   3433  O  O     . ASP A 1 1743 ? 177.437 145.069 105.244 1.00 44.67  ? 1743 ASP A O     1 
ATOM   3434  C  CB    . ASP A 1 1743 ? 175.274 143.331 103.632 1.00 45.03  ? 1743 ASP A CB    1 
ATOM   3435  C  CG    . ASP A 1 1743 ? 174.071 142.495 104.005 1.00 51.57  ? 1743 ASP A CG    1 
ATOM   3436  O  OD1   . ASP A 1 1743 ? 173.869 142.250 105.211 1.00 49.36  ? 1743 ASP A OD1   1 
ATOM   3437  O  OD2   . ASP A 1 1743 ? 173.331 142.077 103.092 1.00 49.50  ? 1743 ASP A OD2   1 
ATOM   3438  N  N     . LYS A 1 1744 ? 177.022 146.056 103.265 1.00 39.20  ? 1744 LYS A N     1 
ATOM   3439  C  CA    . LYS A 1 1744 ? 178.389 146.556 103.157 1.00 38.05  ? 1744 LYS A CA    1 
ATOM   3440  C  C     . LYS A 1 1744 ? 178.717 147.563 104.255 1.00 41.97  ? 1744 LYS A C     1 
ATOM   3441  O  O     . LYS A 1 1744 ? 179.842 147.583 104.768 1.00 42.67  ? 1744 LYS A O     1 
ATOM   3442  C  CB    . LYS A 1 1744 ? 178.615 147.176 101.780 1.00 38.96  ? 1744 LYS A CB    1 
ATOM   3443  C  CG    . LYS A 1 1744 ? 180.071 147.196 101.352 1.00 42.28  ? 1744 LYS A CG    1 
ATOM   3444  C  CD    . LYS A 1 1744 ? 180.330 148.265 100.309 1.00 46.73  ? 1744 LYS A CD    1 
ATOM   3445  C  CE    . LYS A 1 1744 ? 181.575 147.953 99.498  1.00 56.47  ? 1744 LYS A CE    1 
ATOM   3446  N  NZ    . LYS A 1 1744 ? 182.810 148.450 100.163 1.00 63.40  ? 1744 LYS A NZ    1 
ATOM   3447  N  N     . TYR A 1 1745 ? 177.759 148.406 104.630 1.00 43.91  ? 1745 TYR A N     1 
ATOM   3448  C  CA    . TYR A 1 1745 ? 178.030 149.546 105.492 1.00 37.15  ? 1745 TYR A CA    1 
ATOM   3449  C  C     . TYR A 1 1745 ? 177.346 149.401 106.846 1.00 36.61  ? 1745 TYR A C     1 
ATOM   3450  O  O     . TYR A 1 1745 ? 176.366 148.668 106.995 1.00 42.13  ? 1745 TYR A O     1 
ATOM   3451  C  CB    . TYR A 1 1745 ? 177.589 150.848 104.821 1.00 31.40  ? 1745 TYR A CB    1 
ATOM   3452  C  CG    . TYR A 1 1745 ? 178.407 151.167 103.595 1.00 33.20  ? 1745 TYR A CG    1 
ATOM   3453  C  CD1   . TYR A 1 1745 ? 179.682 151.697 103.708 1.00 30.94  ? 1745 TYR A CD1   1 
ATOM   3454  C  CD2   . TYR A 1 1745 ? 177.911 150.918 102.326 1.00 35.73  ? 1745 TYR A CD2   1 
ATOM   3455  C  CE1   . TYR A 1 1745 ? 180.436 151.978 102.590 1.00 34.43  ? 1745 TYR A CE1   1 
ATOM   3456  C  CE2   . TYR A 1 1745 ? 178.656 151.196 101.205 1.00 38.24  ? 1745 TYR A CE2   1 
ATOM   3457  C  CZ    . TYR A 1 1745 ? 179.917 151.726 101.341 1.00 42.64  ? 1745 TYR A CZ    1 
ATOM   3458  O  OH    . TYR A 1 1745 ? 180.662 152.005 100.221 1.00 48.35  ? 1745 TYR A OH    1 
ATOM   3459  N  N     . GLN A 1 1746 ? 177.884 150.116 107.831 1.00 33.75  ? 1746 GLN A N     1 
ATOM   3460  C  CA    . GLN A 1 1746 ? 177.388 150.043 109.197 1.00 34.46  ? 1746 GLN A CA    1 
ATOM   3461  C  C     . GLN A 1 1746 ? 176.008 150.682 109.305 1.00 34.22  ? 1746 GLN A C     1 
ATOM   3462  O  O     . GLN A 1 1746 ? 175.619 151.525 108.495 1.00 39.92  ? 1746 GLN A O     1 
ATOM   3463  C  CB    . GLN A 1 1746 ? 178.367 150.725 110.151 1.00 35.17  ? 1746 GLN A CB    1 
ATOM   3464  C  CG    . GLN A 1 1746 ? 179.647 149.939 110.375 1.00 44.02  ? 1746 GLN A CG    1 
ATOM   3465  C  CD    . GLN A 1 1746 ? 180.677 150.184 109.294 1.00 46.78  ? 1746 GLN A CD    1 
ATOM   3466  O  OE1   . GLN A 1 1746 ? 180.514 151.066 108.455 1.00 49.07  ? 1746 GLN A OE1   1 
ATOM   3467  N  NE2   . GLN A 1 1746 ? 181.742 149.395 109.303 1.00 46.09  ? 1746 GLN A NE2   1 
ATOM   3468  N  N     . ALA A 1 1747 ? 175.266 150.270 110.336 1.00 33.02  ? 1747 ALA A N     1 
ATOM   3469  C  CA    . ALA A 1 1747 ? 173.870 150.679 110.468 1.00 32.75  ? 1747 ALA A CA    1 
ATOM   3470  C  C     . ALA A 1 1747 ? 173.738 152.193 110.561 1.00 30.56  ? 1747 ALA A C     1 
ATOM   3471  O  O     . ALA A 1 1747 ? 172.906 152.800 109.873 1.00 34.53  ? 1747 ALA A O     1 
ATOM   3472  C  CB    . ALA A 1 1747 ? 173.244 150.007 111.690 1.00 32.87  ? 1747 ALA A CB    1 
ATOM   3473  N  N     . GLN A 1 1748 ? 174.558 152.825 111.404 1.00 26.67  ? 1748 GLN A N     1 
ATOM   3474  C  CA    . GLN A 1 1748 ? 174.496 154.276 111.527 1.00 23.71  ? 1748 GLN A CA    1 
ATOM   3475  C  C     . GLN A 1 1748 ? 174.873 154.946 110.214 1.00 22.74  ? 1748 GLN A C     1 
ATOM   3476  O  O     . GLN A 1 1748 ? 174.246 155.932 109.813 1.00 24.33  ? 1748 GLN A O     1 
ATOM   3477  C  CB    . GLN A 1 1748 ? 175.389 154.755 112.678 1.00 26.39  ? 1748 GLN A CB    1 
ATOM   3478  C  CG    . GLN A 1 1748 ? 176.867 154.920 112.355 1.00 26.10  ? 1748 GLN A CG    1 
ATOM   3479  C  CD    . GLN A 1 1748 ? 177.583 155.820 113.341 1.00 27.54  ? 1748 GLN A CD    1 
ATOM   3480  O  OE1   . GLN A 1 1748 ? 177.615 155.544 114.537 1.00 31.07  ? 1748 GLN A OE1   1 
ATOM   3481  N  NE2   . GLN A 1 1748 ? 178.162 156.904 112.842 1.00 25.10  ? 1748 GLN A NE2   1 
ATOM   3482  N  N     . LEU A 1 1749 ? 175.862 154.398 109.507 1.00 22.33  ? 1749 LEU A N     1 
ATOM   3483  C  CA    . LEU A 1 1749 ? 176.256 154.969 108.225 1.00 23.13  ? 1749 LEU A CA    1 
ATOM   3484  C  C     . LEU A 1 1749 ? 175.192 154.733 107.164 1.00 25.18  ? 1749 LEU A C     1 
ATOM   3485  O  O     . LEU A 1 1749 ? 174.967 155.594 106.312 1.00 27.07  ? 1749 LEU A O     1 
ATOM   3486  C  CB    . LEU A 1 1749 ? 177.596 154.393 107.781 1.00 24.85  ? 1749 LEU A CB    1 
ATOM   3487  C  CG    . LEU A 1 1749 ? 178.783 154.817 108.642 1.00 29.04  ? 1749 LEU A CG    1 
ATOM   3488  C  CD1   . LEU A 1 1749 ? 180.070 154.524 107.918 1.00 27.98  ? 1749 LEU A CD1   1 
ATOM   3489  C  CD2   . LEU A 1 1749 ? 178.694 156.292 108.997 1.00 27.68  ? 1749 LEU A CD2   1 
ATOM   3490  N  N     . VAL A 1 1750 ? 174.519 153.583 107.204 1.00 29.38  ? 1750 VAL A N     1 
ATOM   3491  C  CA    . VAL A 1 1750 ? 173.438 153.319 106.256 1.00 27.87  ? 1750 VAL A CA    1 
ATOM   3492  C  C     . VAL A 1 1750 ? 172.308 154.326 106.440 1.00 28.58  ? 1750 VAL A C     1 
ATOM   3493  O  O     . VAL A 1 1750 ? 171.853 154.967 105.480 1.00 36.14  ? 1750 VAL A O     1 
ATOM   3494  C  CB    . VAL A 1 1750 ? 172.940 151.871 106.409 1.00 25.11  ? 1750 VAL A CB    1 
ATOM   3495  C  CG1   . VAL A 1 1750 ? 171.654 151.674 105.657 1.00 33.22  ? 1750 VAL A CG1   1 
ATOM   3496  C  CG2   . VAL A 1 1750 ? 173.979 150.906 105.885 1.00 28.36  ? 1750 VAL A CG2   1 
ATOM   3497  N  N     . VAL A 1 1751 ? 171.854 154.496 107.684 1.00 23.77  ? 1751 VAL A N     1 
ATOM   3498  C  CA    . VAL A 1 1751 ? 170.759 155.426 107.950 1.00 20.89  ? 1751 VAL A CA    1 
ATOM   3499  C  C     . VAL A 1 1751 ? 171.178 156.854 107.623 1.00 24.91  ? 1751 VAL A C     1 
ATOM   3500  O  O     . VAL A 1 1751 ? 170.414 157.620 107.022 1.00 28.78  ? 1751 VAL A O     1 
ATOM   3501  C  CB    . VAL A 1 1751 ? 170.286 155.291 109.407 1.00 18.11  ? 1751 VAL A CB    1 
ATOM   3502  C  CG1   . VAL A 1 1751 ? 169.201 156.304 109.707 1.00 24.75  ? 1751 VAL A CG1   1 
ATOM   3503  C  CG2   . VAL A 1 1751 ? 169.791 153.887 109.668 1.00 26.64  ? 1751 VAL A CG2   1 
ATOM   3504  N  N     . LEU A 1 1752 ? 172.399 157.235 108.006 1.00 26.65  ? 1752 LEU A N     1 
ATOM   3505  C  CA    . LEU A 1 1752 ? 172.876 158.585 107.736 1.00 22.15  ? 1752 LEU A CA    1 
ATOM   3506  C  C     . LEU A 1 1752 ? 173.004 158.843 106.242 1.00 23.45  ? 1752 LEU A C     1 
ATOM   3507  O  O     . LEU A 1 1752 ? 172.680 159.935 105.770 1.00 29.50  ? 1752 LEU A O     1 
ATOM   3508  C  CB    . LEU A 1 1752 ? 174.213 158.806 108.438 1.00 20.49  ? 1752 LEU A CB    1 
ATOM   3509  C  CG    . LEU A 1 1752 ? 174.722 160.238 108.564 1.00 21.73  ? 1752 LEU A CG    1 
ATOM   3510  C  CD1   . LEU A 1 1752 ? 173.768 161.073 109.394 1.00 22.64  ? 1752 LEU A CD1   1 
ATOM   3511  C  CD2   . LEU A 1 1752 ? 176.098 160.223 109.184 1.00 23.76  ? 1752 LEU A CD2   1 
ATOM   3512  N  N     . SER A 1 1753 ? 173.477 157.855 105.480 1.00 22.66  ? 1753 SER A N     1 
ATOM   3513  C  CA    . SER A 1 1753 ? 173.604 158.021 104.039 1.00 24.47  ? 1753 SER A CA    1 
ATOM   3514  C  C     . SER A 1 1753 ? 172.244 158.181 103.384 1.00 26.99  ? 1753 SER A C     1 
ATOM   3515  O  O     . SER A 1 1753 ? 172.081 158.999 102.473 1.00 31.58  ? 1753 SER A O     1 
ATOM   3516  C  CB    . SER A 1 1753 ? 174.342 156.828 103.440 1.00 28.47  ? 1753 SER A CB    1 
ATOM   3517  O  OG    . SER A 1 1753 ? 175.577 156.621 104.097 1.00 33.59  ? 1753 SER A OG    1 
ATOM   3518  N  N     . ALA A 1 1754 ? 171.256 157.402 103.828 1.00 25.95  ? 1754 ALA A N     1 
ATOM   3519  C  CA    . ALA A 1 1754 ? 169.917 157.557 103.269 1.00 24.20  ? 1754 ALA A CA    1 
ATOM   3520  C  C     . ALA A 1 1754 ? 169.329 158.923 103.612 1.00 28.37  ? 1754 ALA A C     1 
ATOM   3521  O  O     . ALA A 1 1754 ? 168.692 159.563 102.765 1.00 34.36  ? 1754 ALA A O     1 
ATOM   3522  C  CB    . ALA A 1 1754 ? 169.015 156.426 103.752 1.00 23.46  ? 1754 ALA A CB    1 
ATOM   3523  N  N     . GLN A 1 1755 ? 169.549 159.396 104.846 1.00 26.24  ? 1755 GLN A N     1 
ATOM   3524  C  CA    . GLN A 1 1755 ? 169.102 160.739 105.218 1.00 22.40  ? 1755 GLN A CA    1 
ATOM   3525  C  C     . GLN A 1 1755 ? 169.771 161.806 104.361 1.00 24.94  ? 1755 GLN A C     1 
ATOM   3526  O  O     . GLN A 1 1755 ? 169.115 162.752 103.909 1.00 30.39  ? 1755 GLN A O     1 
ATOM   3527  C  CB    . GLN A 1 1755 ? 169.380 161.000 106.699 1.00 19.26  ? 1755 GLN A CB    1 
ATOM   3528  C  CG    . GLN A 1 1755 ? 168.399 160.340 107.646 1.00 22.14  ? 1755 GLN A CG    1 
ATOM   3529  C  CD    . GLN A 1 1755 ? 168.731 160.566 109.101 1.00 23.94  ? 1755 GLN A CD    1 
ATOM   3530  O  OE1   . GLN A 1 1755 ? 169.829 160.254 109.554 1.00 25.76  ? 1755 GLN A OE1   1 
ATOM   3531  N  NE2   . GLN A 1 1755 ? 167.771 161.088 109.850 1.00 22.58  ? 1755 GLN A NE2   1 
ATOM   3532  N  N     . ILE A 1 1756 ? 171.079 161.674 104.133 1.00 24.06  ? 1756 ILE A N     1 
ATOM   3533  C  CA    . ILE A 1 1756 ? 171.808 162.647 103.324 1.00 24.00  ? 1756 ILE A CA    1 
ATOM   3534  C  C     . ILE A 1 1756 ? 171.278 162.654 101.898 1.00 27.78  ? 1756 ILE A C     1 
ATOM   3535  O  O     . ILE A 1 1756 ? 171.075 163.716 101.297 1.00 36.21  ? 1756 ILE A O     1 
ATOM   3536  C  CB    . ILE A 1 1756 ? 173.317 162.350 103.359 1.00 22.75  ? 1756 ILE A CB    1 
ATOM   3537  C  CG1   . ILE A 1 1756 ? 173.891 162.632 104.746 1.00 23.95  ? 1756 ILE A CG1   1 
ATOM   3538  C  CG2   . ILE A 1 1756 ? 174.044 163.161 102.306 1.00 30.50  ? 1756 ILE A CG2   1 
ATOM   3539  C  CD1   . ILE A 1 1756 ? 175.303 162.147 104.917 1.00 24.08  ? 1756 ILE A CD1   1 
ATOM   3540  N  N     . ALA A 1 1757 ? 171.056 161.466 101.332 1.00 26.32  ? 1757 ALA A N     1 
ATOM   3541  C  CA    . ALA A 1 1757 ? 170.549 161.379 99.968  1.00 25.43  ? 1757 ALA A CA    1 
ATOM   3542  C  C     . ALA A 1 1757 ? 169.171 162.014 99.852  1.00 30.31  ? 1757 ALA A C     1 
ATOM   3543  O  O     . ALA A 1 1757 ? 168.902 162.758 98.901  1.00 34.87  ? 1757 ALA A O     1 
ATOM   3544  C  CB    . ALA A 1 1757 ? 170.508 159.922 99.514  1.00 30.68  ? 1757 ALA A CB    1 
ATOM   3545  N  N     . TRP A 1 1758 ? 168.287 161.744 100.816 1.00 29.98  ? 1758 TRP A N     1 
ATOM   3546  C  CA    . TRP A 1 1758 ? 166.956 162.339 100.768 1.00 29.43  ? 1758 TRP A CA    1 
ATOM   3547  C  C     . TRP A 1 1758 ? 167.019 163.854 100.905 1.00 30.94  ? 1758 TRP A C     1 
ATOM   3548  O  O     . TRP A 1 1758 ? 166.308 164.575 100.197 1.00 38.04  ? 1758 TRP A O     1 
ATOM   3549  C  CB    . TRP A 1 1758 ? 166.068 161.748 101.857 1.00 33.50  ? 1758 TRP A CB    1 
ATOM   3550  C  CG    . TRP A 1 1758 ? 164.769 162.477 102.023 1.00 34.47  ? 1758 TRP A CG    1 
ATOM   3551  C  CD1   . TRP A 1 1758 ? 163.682 162.410 101.203 1.00 34.56  ? 1758 TRP A CD1   1 
ATOM   3552  C  CD2   . TRP A 1 1758 ? 164.421 163.381 103.077 1.00 30.21  ? 1758 TRP A CD2   1 
ATOM   3553  N  NE1   . TRP A 1 1758 ? 162.679 163.215 101.680 1.00 27.30  ? 1758 TRP A NE1   1 
ATOM   3554  C  CE2   . TRP A 1 1758 ? 163.108 163.823 102.829 1.00 27.69  ? 1758 TRP A CE2   1 
ATOM   3555  C  CE3   . TRP A 1 1758 ? 165.091 163.859 104.205 1.00 30.38  ? 1758 TRP A CE3   1 
ATOM   3556  C  CZ2   . TRP A 1 1758 ? 162.455 164.718 103.667 1.00 25.16  ? 1758 TRP A CZ2   1 
ATOM   3557  C  CZ3   . TRP A 1 1758 ? 164.440 164.748 105.034 1.00 29.55  ? 1758 TRP A CZ3   1 
ATOM   3558  C  CH2   . TRP A 1 1758 ? 163.136 165.168 104.762 1.00 28.41  ? 1758 TRP A CH2   1 
ATOM   3559  N  N     . SER A 1 1759 ? 167.853 164.358 101.818 1.00 32.97  ? 1759 SER A N     1 
ATOM   3560  C  CA    . SER A 1 1759 ? 167.962 165.803 101.991 1.00 34.65  ? 1759 SER A CA    1 
ATOM   3561  C  C     . SER A 1 1759 ? 168.491 166.471 100.730 1.00 38.11  ? 1759 SER A C     1 
ATOM   3562  O  O     . SER A 1 1759 ? 167.976 167.514 100.310 1.00 46.80  ? 1759 SER A O     1 
ATOM   3563  C  CB    . SER A 1 1759 ? 168.860 166.124 103.184 1.00 33.70  ? 1759 SER A CB    1 
ATOM   3564  O  OG    . SER A 1 1759 ? 168.355 165.535 104.368 1.00 40.70  ? 1759 SER A OG    1 
ATOM   3565  N  N     . GLU A 1 1760 ? 169.515 165.881 100.108 1.00 38.72  ? 1760 GLU A N     1 
ATOM   3566  C  CA    . GLU A 1 1760 ? 170.048 166.442 98.871  1.00 39.66  ? 1760 GLU A CA    1 
ATOM   3567  C  C     . GLU A 1 1760 ? 169.000 166.424 97.766  1.00 42.74  ? 1760 GLU A C     1 
ATOM   3568  O  O     . GLU A 1 1760 ? 168.845 167.408 97.032  1.00 53.86  ? 1760 GLU A O     1 
ATOM   3569  C  CB    . GLU A 1 1760 ? 171.292 165.667 98.436  1.00 43.74  ? 1760 GLU A CB    1 
ATOM   3570  C  CG    . GLU A 1 1760 ? 172.484 165.795 99.374  1.00 55.47  ? 1760 GLU A CG    1 
ATOM   3571  C  CD    . GLU A 1 1760 ? 173.061 167.194 99.418  1.00 73.55  ? 1760 GLU A CD    1 
ATOM   3572  O  OE1   . GLU A 1 1760 ? 173.003 167.896 98.387  1.00 82.79  ? 1760 GLU A OE1   1 
ATOM   3573  O  OE2   . GLU A 1 1760 ? 173.579 167.590 100.483 1.00 60.57  ? 1760 GLU A OE2   1 
ATOM   3574  N  N     . ASN A 1 1761 ? 168.265 165.315 97.636  1.00 39.49  ? 1761 ASN A N     1 
ATOM   3575  C  CA    . ASN A 1 1761 ? 167.245 165.223 96.598  1.00 42.35  ? 1761 ASN A CA    1 
ATOM   3576  C  C     . ASN A 1 1761 ? 166.145 166.253 96.809  1.00 44.34  ? 1761 ASN A C     1 
ATOM   3577  O  O     . ASN A 1 1761 ? 165.704 166.901 95.855  1.00 52.99  ? 1761 ASN A O     1 
ATOM   3578  C  CB    . ASN A 1 1761 ? 166.655 163.814 96.559  1.00 44.39  ? 1761 ASN A CB    1 
ATOM   3579  C  CG    . ASN A 1 1761 ? 167.630 162.790 96.017  1.00 53.05  ? 1761 ASN A CG    1 
ATOM   3580  O  OD1   . ASN A 1 1761 ? 168.714 163.134 95.550  1.00 54.33  ? 1761 ASN A OD1   1 
ATOM   3581  N  ND2   . ASN A 1 1761 ? 167.248 161.520 96.079  1.00 50.45  ? 1761 ASN A ND2   1 
ATOM   3582  N  N     . VAL A 1 1762 ? 165.694 166.426 98.052  1.00 39.93  ? 1762 VAL A N     1 
ATOM   3583  C  CA    . VAL A 1 1762 ? 164.613 167.371 98.317  1.00 37.26  ? 1762 VAL A CA    1 
ATOM   3584  C  C     . VAL A 1 1762 ? 165.086 168.803 98.104  1.00 43.90  ? 1762 VAL A C     1 
ATOM   3585  O  O     . VAL A 1 1762 ? 164.345 169.638 97.576  1.00 53.34  ? 1762 VAL A O     1 
ATOM   3586  C  CB    . VAL A 1 1762 ? 164.047 167.162 99.732  1.00 31.96  ? 1762 VAL A CB    1 
ATOM   3587  C  CG1   . VAL A 1 1762 ? 163.070 168.265 100.076 1.00 33.74  ? 1762 VAL A CG1   1 
ATOM   3588  C  CG2   . VAL A 1 1762 ? 163.358 165.822 99.822  1.00 34.30  ? 1762 VAL A CG2   1 
ATOM   3589  N  N     . GLU A 1 1763 ? 166.320 169.116 98.506  1.00 45.20  ? 1763 GLU A N     1 
ATOM   3590  C  CA    . GLU A 1 1763 ? 166.836 170.461 98.278  1.00 41.09  ? 1763 GLU A CA    1 
ATOM   3591  C  C     . GLU A 1 1763 ? 166.976 170.755 96.790  1.00 50.23  ? 1763 GLU A C     1 
ATOM   3592  O  O     . GLU A 1 1763 ? 166.630 171.850 96.334  1.00 63.03  ? 1763 GLU A O     1 
ATOM   3593  C  CB    . GLU A 1 1763 ? 168.173 170.643 98.993  1.00 44.42  ? 1763 GLU A CB    1 
ATOM   3594  C  CG    . GLU A 1 1763 ? 168.035 170.912 100.479 1.00 49.16  ? 1763 GLU A CG    1 
ATOM   3595  C  CD    . GLU A 1 1763 ? 168.269 172.366 100.829 1.00 58.41  ? 1763 GLU A CD    1 
ATOM   3596  O  OE1   . GLU A 1 1763 ? 168.553 173.160 99.909  1.00 64.86  ? 1763 GLU A OE1   1 
ATOM   3597  O  OE2   . GLU A 1 1763 ? 168.167 172.715 102.023 1.00 54.61  ? 1763 GLU A OE2   1 
ATOM   3598  N  N     . THR A 1 1764 ? 167.473 169.787 96.015  1.00 50.15  ? 1764 THR A N     1 
ATOM   3599  C  CA    . THR A 1 1764 ? 167.563 169.976 94.570  1.00 54.18  ? 1764 THR A CA    1 
ATOM   3600  C  C     . THR A 1 1764 ? 166.180 170.142 93.952  1.00 62.93  ? 1764 THR A C     1 
ATOM   3601  O  O     . THR A 1 1764 ? 165.977 170.993 93.075  1.00 65.31  ? 1764 THR A O     1 
ATOM   3602  C  CB    . THR A 1 1764 ? 168.297 168.797 93.932  1.00 54.14  ? 1764 THR A CB    1 
ATOM   3603  O  OG1   . THR A 1 1764 ? 169.606 168.682 94.503  1.00 57.21  ? 1764 THR A OG1   1 
ATOM   3604  C  CG2   . THR A 1 1764 ? 168.425 168.996 92.432  1.00 60.21  ? 1764 THR A CG2   1 
ATOM   3605  N  N     . ALA A 1 1765 ? 165.214 169.342 94.406  1.00 61.71  ? 1765 ALA A N     1 
ATOM   3606  C  CA    . ALA A 1 1765 ? 163.851 169.447 93.903  1.00 63.24  ? 1765 ALA A CA    1 
ATOM   3607  C  C     . ALA A 1 1765 ? 163.267 170.824 94.184  1.00 68.92  ? 1765 ALA A C     1 
ATOM   3608  O  O     . ALA A 1 1765 ? 162.674 171.449 93.301  1.00 75.50  ? 1765 ALA A O     1 
ATOM   3609  C  CB    . ALA A 1 1765 ? 162.983 168.357 94.530  1.00 56.65  ? 1765 ALA A CB    1 
ATOM   3610  N  N     . LEU A 1 1766 ? 163.427 171.312 95.415  1.00 64.39  ? 1766 LEU A N     1 
ATOM   3611  C  CA    . LEU A 1 1766 ? 162.896 172.624 95.770  1.00 62.67  ? 1766 LEU A CA    1 
ATOM   3612  C  C     . LEU A 1 1766 ? 163.590 173.731 94.989  1.00 71.26  ? 1766 LEU A C     1 
ATOM   3613  O  O     . LEU A 1 1766 ? 162.944 174.693 94.558  1.00 81.23  ? 1766 LEU A O     1 
ATOM   3614  C  CB    . LEU A 1 1766 ? 163.032 172.856 97.274  1.00 55.61  ? 1766 LEU A CB    1 
ATOM   3615  C  CG    . LEU A 1 1766 ? 162.061 172.070 98.155  1.00 46.57  ? 1766 LEU A CG    1 
ATOM   3616  C  CD1   . LEU A 1 1766 ? 162.350 172.314 99.622  1.00 40.75  ? 1766 LEU A CD1   1 
ATOM   3617  C  CD2   . LEU A 1 1766 ? 160.625 172.427 97.823  1.00 58.64  ? 1766 LEU A CD2   1 
ATOM   3618  N  N     . SER A 1 1767 ? 164.905 173.612 94.789  1.00 67.63  ? 1767 SER A N     1 
ATOM   3619  C  CA    . SER A 1 1767 ? 165.620 174.604 93.994  1.00 74.42  ? 1767 SER A CA    1 
ATOM   3620  C  C     . SER A 1 1767 ? 165.101 174.636 92.563  1.00 81.08  ? 1767 SER A C     1 
ATOM   3621  O  O     . SER A 1 1767 ? 164.945 175.713 91.975  1.00 88.03  ? 1767 SER A O     1 
ATOM   3622  C  CB    . SER A 1 1767 ? 167.120 174.312 94.016  1.00 76.11  ? 1767 SER A CB    1 
ATOM   3623  O  OG    . SER A 1 1767 ? 167.619 174.311 95.342  1.00 83.27  ? 1767 SER A OG    1 
ATOM   3624  N  N     . SER A 1 1768 ? 164.829 173.464 91.982  1.00 81.48  ? 1768 SER A N     1 
ATOM   3625  C  CA    . SER A 1 1768 ? 164.256 173.431 90.640  1.00 84.68  ? 1768 SER A CA    1 
ATOM   3626  C  C     . SER A 1 1768 ? 162.853 174.028 90.603  1.00 85.18  ? 1768 SER A C     1 
ATOM   3627  O  O     . SER A 1 1768 ? 162.551 174.841 89.721  1.00 88.63  ? 1768 SER A O     1 
ATOM   3628  C  CB    . SER A 1 1768 ? 164.235 171.997 90.113  1.00 86.72  ? 1768 SER A CB    1 
ATOM   3629  O  OG    . SER A 1 1768 ? 165.534 171.430 90.131  1.00 94.62  ? 1768 SER A OG    1 
ATOM   3630  N  N     . MET A 1 1769 ? 161.990 173.652 91.551  1.00 88.21  ? 1769 MET A N     1 
ATOM   3631  C  CA    . MET A 1 1769 ? 160.625 174.170 91.579  1.00 93.86  ? 1769 MET A CA    1 
ATOM   3632  C  C     . MET A 1 1769 ? 160.560 175.656 91.895  1.00 96.92  ? 1769 MET A C     1 
ATOM   3633  O  O     . MET A 1 1769 ? 159.524 176.281 91.642  1.00 99.13  ? 1769 MET A O     1 
ATOM   3634  C  CB    . MET A 1 1769 ? 159.775 173.413 92.601  1.00 91.55  ? 1769 MET A CB    1 
ATOM   3635  C  CG    . MET A 1 1769 ? 159.850 171.905 92.512  1.00 87.85  ? 1769 MET A CG    1 
ATOM   3636  S  SD    . MET A 1 1769 ? 158.363 171.132 93.156  1.00 94.01  ? 1769 MET A SD    1 
ATOM   3637  C  CE    . MET A 1 1769 ? 158.194 172.013 94.698  1.00 79.18  ? 1769 MET A CE    1 
ATOM   3638  N  N     . GLY A 1 1770 ? 161.625 176.229 92.459  1.00 96.36  ? 1770 GLY A N     1 
ATOM   3639  C  CA    . GLY A 1 1770 ? 161.634 177.663 92.698  1.00 99.78  ? 1770 GLY A CA    1 
ATOM   3640  C  C     . GLY A 1 1770 ? 161.425 178.463 91.427  1.00 107.95 ? 1770 GLY A C     1 
ATOM   3641  O  O     . GLY A 1 1770 ? 160.723 179.478 91.427  1.00 112.89 ? 1770 GLY A O     1 
ATOM   3642  N  N     . GLY A 1 1771 ? 162.025 178.016 90.327  1.00 111.21 ? 1771 GLY A N     1 
ATOM   3643  C  CA    . GLY A 1 1771 ? 161.824 178.651 89.041  1.00 114.37 ? 1771 GLY A CA    1 
ATOM   3644  C  C     . GLY A 1 1771 ? 160.789 177.945 88.190  1.00 118.47 ? 1771 GLY A C     1 
ATOM   3645  O  O     . GLY A 1 1771 ? 159.950 178.595 87.558  1.00 118.31 ? 1771 GLY A O     1 
ATOM   3646  N  N     . GLY A 1 1772 ? 160.839 176.611 88.161  1.00 115.09 ? 1772 GLY A N     1 
ATOM   3647  C  CA    . GLY A 1 1772 ? 159.902 175.865 87.337  1.00 114.03 ? 1772 GLY A CA    1 
ATOM   3648  C  C     . GLY A 1 1772 ? 158.466 175.986 87.811  1.00 121.57 ? 1772 GLY A C     1 
ATOM   3649  O  O     . GLY A 1 1772 ? 157.551 176.174 87.004  1.00 124.77 ? 1772 GLY A O     1 
ATOM   3650  N  N     . GLY A 1 1773 ? 158.245 175.878 89.119  1.00 119.12 ? 1773 GLY A N     1 
ATOM   3651  C  CA    . GLY A 1 1773 ? 156.914 175.963 89.678  1.00 118.32 ? 1773 GLY A CA    1 
ATOM   3652  C  C     . GLY A 1 1773 ? 156.086 174.703 89.567  1.00 120.08 ? 1773 GLY A C     1 
ATOM   3653  O  O     . GLY A 1 1773 ? 154.930 174.701 90.011  1.00 121.34 ? 1773 GLY A O     1 
ATOM   3654  N  N     . ASP A 1 1774 ? 156.633 173.633 88.997  1.00 119.47 ? 1774 ASP A N     1 
ATOM   3655  C  CA    . ASP A 1 1774 ? 155.919 172.377 88.824  1.00 114.33 ? 1774 ASP A CA    1 
ATOM   3656  C  C     . ASP A 1 1774 ? 156.307 171.404 89.928  1.00 105.99 ? 1774 ASP A C     1 
ATOM   3657  O  O     . ASP A 1 1774 ? 157.491 171.237 90.232  1.00 98.11  ? 1774 ASP A O     1 
ATOM   3658  C  CB    . ASP A 1 1774 ? 156.223 171.761 87.457  1.00 114.24 ? 1774 ASP A CB    1 
ATOM   3659  C  CG    . ASP A 1 1774 ? 155.224 170.692 87.064  1.00 117.79 ? 1774 ASP A CG    1 
ATOM   3660  O  OD1   . ASP A 1 1774 ? 154.261 170.467 87.827  1.00 115.73 ? 1774 ASP A OD1   1 
ATOM   3661  O  OD2   . ASP A 1 1774 ? 155.404 170.074 85.994  1.00 119.13 ? 1774 ASP A OD2   1 
ATOM   3662  N  N     . ALA A 1 1775 ? 155.303 170.753 90.515  1.00 105.73 ? 1775 ALA A N     1 
ATOM   3663  C  CA    . ALA A 1 1775 ? 155.506 169.834 91.628  1.00 99.41  ? 1775 ALA A CA    1 
ATOM   3664  C  C     . ALA A 1 1775 ? 156.089 168.492 91.203  1.00 93.46  ? 1775 ALA A C     1 
ATOM   3665  O  O     . ALA A 1 1775 ? 156.123 167.566 92.020  1.00 88.55  ? 1775 ALA A O     1 
ATOM   3666  C  CB    . ALA A 1 1775 ? 154.186 169.609 92.371  1.00 95.71  ? 1775 ALA A CB    1 
ATOM   3667  N  N     . ALA A 1 1776 ? 156.540 168.367 89.956  1.00 94.43  ? 1776 ALA A N     1 
ATOM   3668  C  CA    . ALA A 1 1776 ? 157.076 167.093 89.486  1.00 86.16  ? 1776 ALA A CA    1 
ATOM   3669  C  C     . ALA A 1 1776 ? 158.289 166.601 90.272  1.00 84.32  ? 1776 ALA A C     1 
ATOM   3670  O  O     . ALA A 1 1776 ? 158.332 165.398 90.582  1.00 83.41  ? 1776 ALA A O     1 
ATOM   3671  C  CB    . ALA A 1 1776 ? 157.402 167.192 87.990  1.00 82.74  ? 1776 ALA A CB    1 
ATOM   3672  N  N     . PRO A 1 1777 ? 159.299 167.423 90.594  1.00 82.29  ? 1777 PRO A N     1 
ATOM   3673  C  CA    . PRO A 1 1777 ? 160.455 166.876 91.329  1.00 72.31  ? 1777 PRO A CA    1 
ATOM   3674  C  C     . PRO A 1 1777 ? 160.115 166.321 92.704  1.00 69.47  ? 1777 PRO A C     1 
ATOM   3675  O  O     . PRO A 1 1777 ? 160.637 165.264 93.080  1.00 77.39  ? 1777 PRO A O     1 
ATOM   3676  C  CB    . PRO A 1 1777 ? 161.404 168.078 91.415  1.00 77.15  ? 1777 PRO A CB    1 
ATOM   3677  C  CG    . PRO A 1 1777 ? 161.033 168.928 90.263  1.00 82.21  ? 1777 PRO A CG    1 
ATOM   3678  C  CD    . PRO A 1 1777 ? 159.547 168.813 90.173  1.00 87.20  ? 1777 PRO A CD    1 
ATOM   3679  N  N     . LEU A 1 1778 ? 159.252 166.993 93.472  1.00 62.67  ? 1778 LEU A N     1 
ATOM   3680  C  CA    . LEU A 1 1778 ? 158.869 166.447 94.772  1.00 62.45  ? 1778 LEU A CA    1 
ATOM   3681  C  C     . LEU A 1 1778 ? 158.045 165.177 94.619  1.00 64.46  ? 1778 LEU A C     1 
ATOM   3682  O  O     . LEU A 1 1778 ? 158.153 164.257 95.439  1.00 66.11  ? 1778 LEU A O     1 
ATOM   3683  C  CB    . LEU A 1 1778 ? 158.104 167.484 95.593  1.00 59.50  ? 1778 LEU A CB    1 
ATOM   3684  C  CG    . LEU A 1 1778 ? 158.954 168.451 96.414  1.00 64.66  ? 1778 LEU A CG    1 
ATOM   3685  C  CD1   . LEU A 1 1778 ? 158.071 169.450 97.138  1.00 65.12  ? 1778 LEU A CD1   1 
ATOM   3686  C  CD2   . LEU A 1 1778 ? 159.818 167.689 97.401  1.00 49.51  ? 1778 LEU A CD2   1 
ATOM   3687  N  N     . HIS A 1 1779 ? 157.211 165.107 93.582  1.00 66.62  ? 1779 HIS A N     1 
ATOM   3688  C  CA    . HIS A 1 1779 ? 156.481 163.873 93.318  1.00 66.94  ? 1779 HIS A CA    1 
ATOM   3689  C  C     . HIS A 1 1779 ? 157.439 162.735 92.992  1.00 65.91  ? 1779 HIS A C     1 
ATOM   3690  O  O     . HIS A 1 1779 ? 157.238 161.599 93.434  1.00 66.06  ? 1779 HIS A O     1 
ATOM   3691  C  CB    . HIS A 1 1779 ? 155.480 164.085 92.186  1.00 73.73  ? 1779 HIS A CB    1 
ATOM   3692  C  CG    . HIS A 1 1779 ? 154.215 164.756 92.621  1.00 76.10  ? 1779 HIS A CG    1 
ATOM   3693  N  ND1   . HIS A 1 1779 ? 153.408 164.244 93.615  1.00 75.75  ? 1779 HIS A ND1   1 
ATOM   3694  C  CD2   . HIS A 1 1779 ? 153.618 165.896 92.203  1.00 76.89  ? 1779 HIS A CD2   1 
ATOM   3695  C  CE1   . HIS A 1 1779 ? 152.369 165.041 93.788  1.00 76.38  ? 1779 HIS A CE1   1 
ATOM   3696  N  NE2   . HIS A 1 1779 ? 152.473 166.051 92.944  1.00 81.43  ? 1779 HIS A NE2   1 
ATOM   3697  N  N     . SER A 1 1780 ? 158.493 163.026 92.227  1.00 64.64  ? 1780 SER A N     1 
ATOM   3698  C  CA    . SER A 1 1780 ? 159.507 162.016 91.942  1.00 66.70  ? 1780 SER A CA    1 
ATOM   3699  C  C     . SER A 1 1780 ? 160.224 161.579 93.214  1.00 63.34  ? 1780 SER A C     1 
ATOM   3700  O  O     . SER A 1 1780 ? 160.505 160.389 93.400  1.00 63.41  ? 1780 SER A O     1 
ATOM   3701  C  CB    . SER A 1 1780 ? 160.506 162.555 90.920  1.00 68.81  ? 1780 SER A CB    1 
ATOM   3702  O  OG    . SER A 1 1780 ? 161.580 161.652 90.729  1.00 86.87  ? 1780 SER A OG    1 
ATOM   3703  N  N     . VAL A 1 1781 ? 160.535 162.530 94.096  1.00 56.13  ? 1781 VAL A N     1 
ATOM   3704  C  CA    . VAL A 1 1781 ? 161.192 162.196 95.360  1.00 51.00  ? 1781 VAL A CA    1 
ATOM   3705  C  C     . VAL A 1 1781 ? 160.307 161.275 96.193  1.00 54.43  ? 1781 VAL A C     1 
ATOM   3706  O  O     . VAL A 1 1781 ? 160.765 160.262 96.738  1.00 58.38  ? 1781 VAL A O     1 
ATOM   3707  C  CB    . VAL A 1 1781 ? 161.553 163.478 96.131  1.00 44.07  ? 1781 VAL A CB    1 
ATOM   3708  C  CG1   . VAL A 1 1781 ? 162.009 163.143 97.536  1.00 47.51  ? 1781 VAL A CG1   1 
ATOM   3709  C  CG2   . VAL A 1 1781 ? 162.633 164.248 95.396  1.00 48.45  ? 1781 VAL A CG2   1 
ATOM   3710  N  N     . LEU A 1 1782 ? 159.021 161.615 96.302  1.00 54.27  ? 1782 LEU A N     1 
ATOM   3711  C  CA    . LEU A 1 1782 ? 158.100 160.790 97.077  1.00 48.77  ? 1782 LEU A CA    1 
ATOM   3712  C  C     . LEU A 1 1782 ? 157.932 159.412 96.450  1.00 53.61  ? 1782 LEU A C     1 
ATOM   3713  O  O     . LEU A 1 1782 ? 157.848 158.405 97.162  1.00 54.83  ? 1782 LEU A O     1 
ATOM   3714  C  CB    . LEU A 1 1782 ? 156.750 161.491 97.211  1.00 50.47  ? 1782 LEU A CB    1 
ATOM   3715  C  CG    . LEU A 1 1782 ? 155.730 160.798 98.113  1.00 50.82  ? 1782 LEU A CG    1 
ATOM   3716  C  CD1   . LEU A 1 1782 ? 156.191 160.828 99.557  1.00 44.43  ? 1782 LEU A CD1   1 
ATOM   3717  C  CD2   . LEU A 1 1782 ? 154.370 161.454 97.973  1.00 54.92  ? 1782 LEU A CD2   1 
ATOM   3718  N  N     . SER A 1 1783 ? 157.878 159.347 95.118  1.00 55.03  ? 1783 SER A N     1 
ATOM   3719  C  CA    . SER A 1 1783 ? 157.768 158.058 94.444  1.00 57.13  ? 1783 SER A CA    1 
ATOM   3720  C  C     . SER A 1 1783 ? 158.995 157.194 94.702  1.00 57.10  ? 1783 SER A C     1 
ATOM   3721  O  O     . SER A 1 1783 ? 158.874 155.986 94.928  1.00 62.17  ? 1783 SER A O     1 
ATOM   3722  C  CB    . SER A 1 1783 ? 157.567 158.269 92.944  1.00 64.49  ? 1783 SER A CB    1 
ATOM   3723  O  OG    . SER A 1 1783 ? 157.571 157.032 92.253  1.00 77.92  ? 1783 SER A OG    1 
ATOM   3724  N  N     . ASN A 1 1784 ? 160.186 157.795 94.665  1.00 52.82  ? 1784 ASN A N     1 
ATOM   3725  C  CA    . ASN A 1 1784 ? 161.401 157.040 94.953  1.00 51.27  ? 1784 ASN A CA    1 
ATOM   3726  C  C     . ASN A 1 1784 ? 161.407 156.534 96.389  1.00 48.17  ? 1784 ASN A C     1 
ATOM   3727  O  O     . ASN A 1 1784 ? 161.792 155.387 96.651  1.00 55.11  ? 1784 ASN A O     1 
ATOM   3728  C  CB    . ASN A 1 1784 ? 162.632 157.903 94.683  1.00 54.30  ? 1784 ASN A CB    1 
ATOM   3729  C  CG    . ASN A 1 1784 ? 163.924 157.179 94.987  1.00 62.11  ? 1784 ASN A CG    1 
ATOM   3730  O  OD1   . ASN A 1 1784 ? 164.679 157.579 95.872  1.00 63.85  ? 1784 ASN A OD1   1 
ATOM   3731  N  ND2   . ASN A 1 1784 ? 164.185 156.103 94.255  1.00 67.75  ? 1784 ASN A ND2   1 
ATOM   3732  N  N     . VAL A 1 1785 ? 160.984 157.377 97.334  1.00 45.73  ? 1785 VAL A N     1 
ATOM   3733  C  CA    . VAL A 1 1785 ? 160.917 156.947 98.728  1.00 41.92  ? 1785 VAL A CA    1 
ATOM   3734  C  C     . VAL A 1 1785 ? 159.941 155.787 98.879  1.00 45.73  ? 1785 VAL A C     1 
ATOM   3735  O  O     . VAL A 1 1785 ? 160.214 154.816 99.592  1.00 47.40  ? 1785 VAL A O     1 
ATOM   3736  C  CB    . VAL A 1 1785 ? 160.541 158.128 99.641  1.00 41.65  ? 1785 VAL A CB    1 
ATOM   3737  C  CG1   . VAL A 1 1785 ? 160.264 157.641 101.049 1.00 31.43  ? 1785 VAL A CG1   1 
ATOM   3738  C  CG2   . VAL A 1 1785 ? 161.652 159.162 99.653  1.00 37.87  ? 1785 VAL A CG2   1 
ATOM   3739  N  N     . GLU A 1 1786 ? 158.793 155.862 98.202  1.00 52.77  ? 1786 GLU A N     1 
ATOM   3740  C  CA    . GLU A 1 1786 ? 157.806 154.790 98.294  1.00 49.31  ? 1786 GLU A CA    1 
ATOM   3741  C  C     . GLU A 1 1786 ? 158.320 153.495 97.672  1.00 49.63  ? 1786 GLU A C     1 
ATOM   3742  O  O     . GLU A 1 1786 ? 158.066 152.406 98.198  1.00 53.04  ? 1786 GLU A O     1 
ATOM   3743  C  CB    . GLU A 1 1786 ? 156.500 155.222 97.633  1.00 49.75  ? 1786 GLU A CB    1 
ATOM   3744  C  CG    . GLU A 1 1786 ? 155.645 156.129 98.496  1.00 54.04  ? 1786 GLU A CG    1 
ATOM   3745  C  CD    . GLU A 1 1786 ? 154.299 156.426 97.869  1.00 75.28  ? 1786 GLU A CD    1 
ATOM   3746  O  OE1   . GLU A 1 1786 ? 154.045 155.937 96.748  1.00 81.91  ? 1786 GLU A OE1   1 
ATOM   3747  O  OE2   . GLU A 1 1786 ? 153.495 157.147 98.496  1.00 74.90  ? 1786 GLU A OE2   1 
ATOM   3748  N  N     . VAL A 1 1787 ? 159.035 153.589 96.549  1.00 48.93  ? 1787 VAL A N     1 
ATOM   3749  C  CA    . VAL A 1 1787 ? 159.594 152.392 95.925  1.00 50.40  ? 1787 VAL A CA    1 
ATOM   3750  C  C     . VAL A 1 1787 ? 160.629 151.748 96.839  1.00 52.71  ? 1787 VAL A C     1 
ATOM   3751  O  O     . VAL A 1 1787 ? 160.651 150.520 97.016  1.00 57.84  ? 1787 VAL A O     1 
ATOM   3752  C  CB    . VAL A 1 1787 ? 160.190 152.734 94.547  1.00 50.03  ? 1787 VAL A CB    1 
ATOM   3753  C  CG1   . VAL A 1 1787 ? 160.976 151.558 94.004  1.00 54.21  ? 1787 VAL A CG1   1 
ATOM   3754  C  CG2   . VAL A 1 1787 ? 159.088 153.120 93.578  1.00 57.80  ? 1787 VAL A CG2   1 
ATOM   3755  N  N     . THR A 1 1788 ? 161.501 152.562 97.437  1.00 49.14  ? 1788 THR A N     1 
ATOM   3756  C  CA    . THR A 1 1788 ? 162.494 152.018 98.356  1.00 43.40  ? 1788 THR A CA    1 
ATOM   3757  C  C     . THR A 1 1788 ? 161.828 151.417 99.588  1.00 41.66  ? 1788 THR A C     1 
ATOM   3758  O  O     . THR A 1 1788 ? 162.295 150.406 100.123 1.00 45.76  ? 1788 THR A O     1 
ATOM   3759  C  CB    . THR A 1 1788 ? 163.495 153.100 98.754  1.00 47.90  ? 1788 THR A CB    1 
ATOM   3760  O  OG1   . THR A 1 1788 ? 163.967 153.767 97.578  1.00 55.35  ? 1788 THR A OG1   1 
ATOM   3761  C  CG2   . THR A 1 1788 ? 164.679 152.480 99.462  1.00 51.55  ? 1788 THR A CG2   1 
ATOM   3762  N  N     . LEU A 1 1789 ? 160.727 152.016 100.046 1.00 42.77  ? 1789 LEU A N     1 
ATOM   3763  C  CA    . LEU A 1 1789 ? 159.985 151.452 101.170 1.00 41.41  ? 1789 LEU A CA    1 
ATOM   3764  C  C     . LEU A 1 1789 ? 159.357 150.112 100.808 1.00 44.36  ? 1789 LEU A C     1 
ATOM   3765  O  O     . LEU A 1 1789 ? 159.322 149.194 101.634 1.00 47.48  ? 1789 LEU A O     1 
ATOM   3766  C  CB    . LEU A 1 1789 ? 158.914 152.436 101.636 1.00 39.59  ? 1789 LEU A CB    1 
ATOM   3767  C  CG    . LEU A 1 1789 ? 159.257 153.277 102.863 1.00 30.80  ? 1789 LEU A CG    1 
ATOM   3768  C  CD1   . LEU A 1 1789 ? 158.068 154.116 103.282 1.00 35.80  ? 1789 LEU A CD1   1 
ATOM   3769  C  CD2   . LEU A 1 1789 ? 159.707 152.382 104.000 1.00 33.30  ? 1789 LEU A CD2   1 
ATOM   3770  N  N     . ASN A 1 1790 ? 158.840 149.985 99.585  1.00 44.33  ? 1790 ASN A N     1 
ATOM   3771  C  CA    . ASN A 1 1790 ? 158.312 148.699 99.137  1.00 49.78  ? 1790 ASN A CA    1 
ATOM   3772  C  C     . ASN A 1 1790 ? 159.407 147.642 99.098  1.00 56.56  ? 1790 ASN A C     1 
ATOM   3773  O  O     . ASN A 1 1790 ? 159.195 146.497 99.520  1.00 61.40  ? 1790 ASN A O     1 
ATOM   3774  C  CB    . ASN A 1 1790 ? 157.663 148.846 97.762  1.00 50.97  ? 1790 ASN A CB    1 
ATOM   3775  C  CG    . ASN A 1 1790 ? 156.422 149.712 97.792  1.00 65.21  ? 1790 ASN A CG    1 
ATOM   3776  O  OD1   . ASN A 1 1790 ? 155.997 150.171 98.852  1.00 62.47  ? 1790 ASN A OD1   1 
ATOM   3777  N  ND2   . ASN A 1 1790 ? 155.834 149.943 96.625  1.00 70.63  ? 1790 ASN A ND2   1 
ATOM   3778  N  N     . VAL A 1 1791 ? 160.586 148.010 98.594  1.00 54.82  ? 1791 VAL A N     1 
ATOM   3779  C  CA    . VAL A 1 1791 ? 161.710 147.076 98.578  1.00 48.40  ? 1791 VAL A CA    1 
ATOM   3780  C  C     . VAL A 1 1791 ? 162.088 146.673 99.999  1.00 45.90  ? 1791 VAL A C     1 
ATOM   3781  O  O     . VAL A 1 1791 ? 162.359 145.498 100.277 1.00 51.79  ? 1791 VAL A O     1 
ATOM   3782  C  CB    . VAL A 1 1791 ? 162.904 147.689 97.824  1.00 48.81  ? 1791 VAL A CB    1 
ATOM   3783  C  CG1   . VAL A 1 1791 ? 164.150 146.845 98.020  1.00 47.56  ? 1791 VAL A CG1   1 
ATOM   3784  C  CG2   . VAL A 1 1791 ? 162.581 147.826 96.348  1.00 54.14  ? 1791 VAL A CG2   1 
ATOM   3785  N  N     . LEU A 1 1792 ? 162.111 147.640 100.918 1.00 42.89  ? 1792 LEU A N     1 
ATOM   3786  C  CA    . LEU A 1 1792 ? 162.450 147.346 102.307 1.00 41.57  ? 1792 LEU A CA    1 
ATOM   3787  C  C     . LEU A 1 1792 ? 161.433 146.408 102.943 1.00 48.90  ? 1792 LEU A C     1 
ATOM   3788  O  O     . LEU A 1 1792 ? 161.802 145.503 103.699 1.00 55.70  ? 1792 LEU A O     1 
ATOM   3789  C  CB    . LEU A 1 1792 ? 162.548 148.643 103.105 1.00 41.21  ? 1792 LEU A CB    1 
ATOM   3790  C  CG    . LEU A 1 1792 ? 163.819 149.466 102.917 1.00 40.80  ? 1792 LEU A CG    1 
ATOM   3791  C  CD1   . LEU A 1 1792 ? 163.820 150.639 103.870 1.00 37.42  ? 1792 LEU A CD1   1 
ATOM   3792  C  CD2   . LEU A 1 1792 ? 165.039 148.599 103.138 1.00 37.94  ? 1792 LEU A CD2   1 
ATOM   3793  N  N     . ALA A 1 1793 ? 160.145 146.620 102.666 1.00 48.99  ? 1793 ALA A N     1 
ATOM   3794  C  CA    . ALA A 1 1793 ? 159.122 145.722 103.193 1.00 48.60  ? 1793 ALA A CA    1 
ATOM   3795  C  C     . ALA A 1 1793 ? 159.293 144.312 102.644 1.00 53.80  ? 1793 ALA A C     1 
ATOM   3796  O  O     . ALA A 1 1793 ? 159.252 143.330 103.398 1.00 55.53  ? 1793 ALA A O     1 
ATOM   3797  C  CB    . ALA A 1 1793 ? 157.731 146.262 102.868 1.00 49.55  ? 1793 ALA A CB    1 
ATOM   3798  N  N     . ASP A 1 1794 ? 159.515 144.192 101.332 1.00 54.51  ? 1794 ASP A N     1 
ATOM   3799  C  CA    . ASP A 1 1794 ? 159.748 142.876 100.747 1.00 54.45  ? 1794 ASP A CA    1 
ATOM   3800  C  C     . ASP A 1 1794 ? 160.950 142.197 101.389 1.00 58.28  ? 1794 ASP A C     1 
ATOM   3801  O  O     . ASP A 1 1794 ? 160.927 140.987 101.645 1.00 64.09  ? 1794 ASP A O     1 
ATOM   3802  C  CB    . ASP A 1 1794 ? 159.944 142.996 99.236  1.00 59.02  ? 1794 ASP A CB    1 
ATOM   3803  C  CG    . ASP A 1 1794 ? 158.729 143.568 98.535  1.00 65.48  ? 1794 ASP A CG    1 
ATOM   3804  O  OD1   . ASP A 1 1794 ? 158.710 143.577 97.287  1.00 65.41  ? 1794 ASP A OD1   1 
ATOM   3805  O  OD2   . ASP A 1 1794 ? 157.790 144.004 99.233  1.00 68.91  ? 1794 ASP A OD2   1 
ATOM   3806  N  N     . SER A 1 1795 ? 162.011 142.960 101.657 1.00 54.26  ? 1795 SER A N     1 
ATOM   3807  C  CA    . SER A 1 1795 ? 163.188 142.391 102.303 1.00 50.18  ? 1795 SER A CA    1 
ATOM   3808  C  C     . SER A 1 1795 ? 162.887 141.949 103.730 1.00 49.08  ? 1795 SER A C     1 
ATOM   3809  O  O     . SER A 1 1795 ? 163.372 140.904 104.176 1.00 55.66  ? 1795 SER A O     1 
ATOM   3810  C  CB    . SER A 1 1795 ? 164.335 143.401 102.287 1.00 50.63  ? 1795 SER A CB    1 
ATOM   3811  O  OG    . SER A 1 1795 ? 164.677 143.761 100.962 1.00 58.54  ? 1795 SER A OG    1 
ATOM   3812  N  N     . VAL A 1 1796 ? 162.094 142.732 104.466 1.00 47.27  ? 1796 VAL A N     1 
ATOM   3813  C  CA    . VAL A 1 1796 ? 161.907 142.439 105.882 1.00 52.18  ? 1796 VAL A CA    1 
ATOM   3814  C  C     . VAL A 1 1796 ? 160.911 141.305 106.098 1.00 55.35  ? 1796 VAL A C     1 
ATOM   3815  O  O     . VAL A 1 1796 ? 160.933 140.666 107.157 1.00 55.01  ? 1796 VAL A O     1 
ATOM   3816  C  CB    . VAL A 1 1796 ? 161.485 143.707 106.654 1.00 49.02  ? 1796 VAL A CB    1 
ATOM   3817  C  CG1   . VAL A 1 1796 ? 160.073 144.124 106.295 1.00 47.41  ? 1796 VAL A CG1   1 
ATOM   3818  C  CG2   . VAL A 1 1796 ? 161.642 143.507 108.155 1.00 44.87  ? 1796 VAL A CG2   1 
ATOM   3819  N  N     . LEU A 1 1797 ? 160.036 141.022 105.127 1.00 54.12  ? 1797 LEU A N     1 
ATOM   3820  C  CA    . LEU A 1 1797 ? 159.260 139.784 105.216 1.00 51.52  ? 1797 LEU A CA    1 
ATOM   3821  C  C     . LEU A 1 1797 ? 160.159 138.554 105.134 1.00 55.10  ? 1797 LEU A C     1 
ATOM   3822  O  O     . LEU A 1 1797 ? 159.914 137.555 105.820 1.00 58.27  ? 1797 LEU A O     1 
ATOM   3823  C  CB    . LEU A 1 1797 ? 158.178 139.725 104.135 1.00 53.13  ? 1797 LEU A CB    1 
ATOM   3824  C  CG    . LEU A 1 1797 ? 156.821 140.405 104.362 1.00 50.93  ? 1797 LEU A CG    1 
ATOM   3825  C  CD1   . LEU A 1 1797 ? 156.113 139.732 105.525 1.00 50.84  ? 1797 LEU A CD1   1 
ATOM   3826  C  CD2   . LEU A 1 1797 ? 156.912 141.891 104.604 1.00 57.68  ? 1797 LEU A CD2   1 
ATOM   3827  N  N     . MET A 1 1798 ? 161.198 138.604 104.305 1.00 57.42  ? 1798 MET A N     1 
ATOM   3828  C  CA    . MET A 1 1798 ? 162.091 137.468 104.133 1.00 59.95  ? 1798 MET A CA    1 
ATOM   3829  C  C     . MET A 1 1798 ? 162.884 137.201 105.413 1.00 60.13  ? 1798 MET A C     1 
ATOM   3830  O  O     . MET A 1 1798 ? 162.816 137.948 106.393 1.00 66.65  ? 1798 MET A O     1 
ATOM   3831  C  CB    . MET A 1 1798 ? 163.046 137.714 102.967 1.00 57.76  ? 1798 MET A CB    1 
ATOM   3832  C  CG    . MET A 1 1798 ? 162.367 137.769 101.612 1.00 69.82  ? 1798 MET A CG    1 
ATOM   3833  S  SD    . MET A 1 1798 ? 163.384 138.575 100.363 1.00 96.37  ? 1798 MET A SD    1 
ATOM   3834  C  CE    . MET A 1 1798 ? 164.951 137.752 100.624 1.00 77.08  ? 1798 MET A CE    1 
ATOM   3835  N  N     . GLU A 1 1799 ? 163.647 136.111 105.397 1.00 56.84  ? 1799 GLU A N     1 
ATOM   3836  C  CA    . GLU A 1 1799 ? 164.512 135.754 106.513 1.00 60.19  ? 1799 GLU A CA    1 
ATOM   3837  C  C     . GLU A 1 1799 ? 165.860 136.443 106.357 1.00 62.81  ? 1799 GLU A C     1 
ATOM   3838  O  O     . GLU A 1 1799 ? 166.555 136.243 105.356 1.00 64.42  ? 1799 GLU A O     1 
ATOM   3839  C  CB    . GLU A 1 1799 ? 164.702 134.241 106.595 1.00 72.33  ? 1799 GLU A CB    1 
ATOM   3840  C  CG    . GLU A 1 1799 ? 165.535 133.794 107.784 1.00 78.36  ? 1799 GLU A CG    1 
ATOM   3841  C  CD    . GLU A 1 1799 ? 165.669 132.288 107.871 1.00 93.37  ? 1799 GLU A CD    1 
ATOM   3842  O  OE1   . GLU A 1 1799 ? 165.127 131.587 106.991 1.00 95.59  ? 1799 GLU A OE1   1 
ATOM   3843  O  OE2   . GLU A 1 1799 ? 166.320 131.805 108.821 1.00 99.03  ? 1799 GLU A OE2   1 
ATOM   3844  N  N     . GLN A 1 1800 ? 166.229 137.241 107.349 1.00 61.45  ? 1800 GLN A N     1 
ATOM   3845  C  CA    . GLN A 1 1800 ? 167.430 138.057 107.319 1.00 54.57  ? 1800 GLN A CA    1 
ATOM   3846  C  C     . GLN A 1 1800 ? 168.257 137.804 108.567 1.00 53.88  ? 1800 GLN A C     1 
ATOM   3847  O  O     . GLN A 1 1800 ? 167.722 137.410 109.609 1.00 56.67  ? 1800 GLN A O     1 
ATOM   3848  C  CB    . GLN A 1 1800 ? 167.082 139.552 107.230 1.00 47.72  ? 1800 GLN A CB    1 
ATOM   3849  C  CG    . GLN A 1 1800 ? 165.992 139.900 106.229 1.00 48.46  ? 1800 GLN A CG    1 
ATOM   3850  C  CD    . GLN A 1 1800 ? 166.476 139.868 104.794 1.00 54.62  ? 1800 GLN A CD    1 
ATOM   3851  O  OE1   . GLN A 1 1800 ? 167.645 139.601 104.525 1.00 54.55  ? 1800 GLN A OE1   1 
ATOM   3852  N  NE2   . GLN A 1 1800 ? 165.575 140.147 103.862 1.00 59.51  ? 1800 GLN A NE2   1 
ATOM   3853  N  N     . PRO A 1 1801 ? 169.568 138.014 108.493 1.00 50.72  ? 1801 PRO A N     1 
ATOM   3854  C  CA    . PRO A 1 1801 ? 170.400 137.964 109.698 1.00 46.31  ? 1801 PRO A CA    1 
ATOM   3855  C  C     . PRO A 1 1801 ? 169.988 139.049 110.675 1.00 46.11  ? 1801 PRO A C     1 
ATOM   3856  O  O     . PRO A 1 1801 ? 169.429 140.077 110.267 1.00 52.19  ? 1801 PRO A O     1 
ATOM   3857  C  CB    . PRO A 1 1801 ? 171.817 138.208 109.159 1.00 45.36  ? 1801 PRO A CB    1 
ATOM   3858  C  CG    . PRO A 1 1801 ? 171.753 137.797 107.732 1.00 49.24  ? 1801 PRO A CG    1 
ATOM   3859  C  CD    . PRO A 1 1801 ? 170.375 138.152 107.269 1.00 46.94  ? 1801 PRO A CD    1 
ATOM   3860  N  N     . PRO A 1 1802 ? 170.226 138.850 111.975 1.00 45.74  ? 1802 PRO A N     1 
ATOM   3861  C  CA    . PRO A 1 1802 ? 169.778 139.854 112.957 1.00 48.02  ? 1802 PRO A CA    1 
ATOM   3862  C  C     . PRO A 1 1802 ? 170.332 141.245 112.707 1.00 45.85  ? 1802 PRO A C     1 
ATOM   3863  O  O     . PRO A 1 1802 ? 169.611 142.235 112.884 1.00 47.94  ? 1802 PRO A O     1 
ATOM   3864  C  CB    . PRO A 1 1802 ? 170.273 139.276 114.291 1.00 47.81  ? 1802 PRO A CB    1 
ATOM   3865  C  CG    . PRO A 1 1802 ? 170.424 137.814 114.039 1.00 48.61  ? 1802 PRO A CG    1 
ATOM   3866  C  CD    . PRO A 1 1802 ? 170.874 137.696 112.618 1.00 45.52  ? 1802 PRO A CD    1 
ATOM   3867  N  N     . LEU A 1 1803 ? 171.594 141.351 112.287 1.00 44.89  ? 1803 LEU A N     1 
ATOM   3868  C  CA    . LEU A 1 1803 ? 172.178 142.661 112.020 1.00 40.56  ? 1803 LEU A CA    1 
ATOM   3869  C  C     . LEU A 1 1803 ? 171.531 143.311 110.804 1.00 40.87  ? 1803 LEU A C     1 
ATOM   3870  O  O     . LEU A 1 1803 ? 171.168 144.494 110.836 1.00 50.29  ? 1803 LEU A O     1 
ATOM   3871  C  CB    . LEU A 1 1803 ? 173.687 142.533 111.825 1.00 45.19  ? 1803 LEU A CB    1 
ATOM   3872  C  CG    . LEU A 1 1803 ? 174.442 143.846 111.629 1.00 48.78  ? 1803 LEU A CG    1 
ATOM   3873  C  CD1   . LEU A 1 1803 ? 174.486 144.616 112.932 1.00 46.41  ? 1803 LEU A CD1   1 
ATOM   3874  C  CD2   . LEU A 1 1803 ? 175.846 143.587 111.108 1.00 50.16  ? 1803 LEU A CD2   1 
ATOM   3875  N  N     . ARG A 1 1804 ? 171.378 142.551 109.717 1.00 35.36  ? 1804 ARG A N     1 
ATOM   3876  C  CA    . ARG A 1 1804 ? 170.692 143.086 108.549 1.00 32.37  ? 1804 ARG A CA    1 
ATOM   3877  C  C     . ARG A 1 1804 ? 169.231 143.377 108.854 1.00 35.91  ? 1804 ARG A C     1 
ATOM   3878  O  O     . ARG A 1 1804 ? 168.669 144.337 108.322 1.00 40.68  ? 1804 ARG A O     1 
ATOM   3879  C  CB    . ARG A 1 1804 ? 170.806 142.122 107.371 1.00 34.52  ? 1804 ARG A CB    1 
ATOM   3880  C  CG    . ARG A 1 1804 ? 170.229 142.675 106.082 1.00 35.49  ? 1804 ARG A CG    1 
ATOM   3881  C  CD    . ARG A 1 1804 ? 170.072 141.599 105.026 1.00 46.03  ? 1804 ARG A CD    1 
ATOM   3882  N  NE    . ARG A 1 1804 ? 171.306 140.858 104.805 1.00 54.88  ? 1804 ARG A NE    1 
ATOM   3883  C  CZ    . ARG A 1 1804 ? 171.426 139.838 103.968 1.00 50.98  ? 1804 ARG A CZ    1 
ATOM   3884  N  NH1   . ARG A 1 1804 ? 170.399 139.403 103.257 1.00 48.60  ? 1804 ARG A NH1   1 
ATOM   3885  N  NH2   . ARG A 1 1804 ? 172.606 139.239 103.840 1.00 50.93  ? 1804 ARG A NH2   1 
ATOM   3886  N  N     . ARG A 1 1805 ? 168.602 142.566 109.705 1.00 36.97  ? 1805 ARG A N     1 
ATOM   3887  C  CA    . ARG A 1 1805 ? 167.230 142.844 110.113 1.00 34.11  ? 1805 ARG A CA    1 
ATOM   3888  C  C     . ARG A 1 1805 ? 167.131 144.174 110.848 1.00 38.45  ? 1805 ARG A C     1 
ATOM   3889  O  O     . ARG A 1 1805 ? 166.214 144.966 110.597 1.00 42.25  ? 1805 ARG A O     1 
ATOM   3890  C  CB    . ARG A 1 1805 ? 166.710 141.705 110.988 1.00 41.71  ? 1805 ARG A CB    1 
ATOM   3891  C  CG    . ARG A 1 1805 ? 165.373 141.974 111.645 1.00 47.33  ? 1805 ARG A CG    1 
ATOM   3892  C  CD    . ARG A 1 1805 ? 164.272 142.159 110.620 1.00 59.95  ? 1805 ARG A CD    1 
ATOM   3893  N  NE    . ARG A 1 1805 ? 164.258 141.095 109.624 1.00 63.45  ? 1805 ARG A NE    1 
ATOM   3894  C  CZ    . ARG A 1 1805 ? 163.877 139.849 109.862 1.00 56.91  ? 1805 ARG A CZ    1 
ATOM   3895  N  NH1   . ARG A 1 1805 ? 163.514 139.457 111.071 1.00 59.50  ? 1805 ARG A NH1   1 
ATOM   3896  N  NH2   . ARG A 1 1805 ? 163.866 138.971 108.864 1.00 54.99  ? 1805 ARG A NH2   1 
ATOM   3897  N  N     . ARG A 1 1806 ? 168.069 144.439 111.759 1.00 38.38  ? 1806 ARG A N     1 
ATOM   3898  C  CA    . ARG A 1 1806 ? 168.062 145.711 112.473 1.00 35.43  ? 1806 ARG A CA    1 
ATOM   3899  C  C     . ARG A 1 1806 ? 168.323 146.875 111.526 1.00 34.43  ? 1806 ARG A C     1 
ATOM   3900  O  O     . ARG A 1 1806 ? 167.706 147.939 111.653 1.00 37.60  ? 1806 ARG A O     1 
ATOM   3901  C  CB    . ARG A 1 1806 ? 169.092 145.688 113.600 1.00 40.09  ? 1806 ARG A CB    1 
ATOM   3902  C  CG    . ARG A 1 1806 ? 168.635 146.405 114.854 1.00 52.23  ? 1806 ARG A CG    1 
ATOM   3903  C  CD    . ARG A 1 1806 ? 169.393 145.920 116.075 1.00 60.37  ? 1806 ARG A CD    1 
ATOM   3904  N  NE    . ARG A 1 1806 ? 169.177 146.786 117.227 1.00 66.63  ? 1806 ARG A NE    1 
ATOM   3905  C  CZ    . ARG A 1 1806 ? 169.808 146.659 118.386 1.00 73.75  ? 1806 ARG A CZ    1 
ATOM   3906  N  NH1   . ARG A 1 1806 ? 170.709 145.710 118.582 1.00 69.77  ? 1806 ARG A NH1   1 
ATOM   3907  N  NH2   . ARG A 1 1806 ? 169.527 147.504 119.373 1.00 77.19  ? 1806 ARG A NH2   1 
ATOM   3908  N  N     . LYS A 1 1807 ? 169.237 146.693 110.569 1.00 31.57  ? 1807 LYS A N     1 
ATOM   3909  C  CA    . LYS A 1 1807 ? 169.475 147.735 109.573 1.00 28.42  ? 1807 LYS A CA    1 
ATOM   3910  C  C     . LYS A 1 1807 ? 168.221 148.013 108.754 1.00 31.01  ? 1807 LYS A C     1 
ATOM   3911  O  O     . LYS A 1 1807 ? 167.896 149.173 108.477 1.00 39.99  ? 1807 LYS A O     1 
ATOM   3912  C  CB    . LYS A 1 1807 ? 170.625 147.338 108.652 1.00 27.24  ? 1807 LYS A CB    1 
ATOM   3913  C  CG    . LYS A 1 1807 ? 171.982 147.256 109.318 1.00 31.39  ? 1807 LYS A CG    1 
ATOM   3914  C  CD    . LYS A 1 1807 ? 173.051 146.956 108.286 1.00 31.22  ? 1807 LYS A CD    1 
ATOM   3915  C  CE    . LYS A 1 1807 ? 174.396 146.714 108.928 1.00 29.95  ? 1807 LYS A CE    1 
ATOM   3916  N  NZ    . LYS A 1 1807 ? 175.408 146.324 107.914 1.00 33.94  ? 1807 LYS A NZ    1 
ATOM   3917  N  N     . LEU A 1 1808 ? 167.510 146.959 108.347 1.00 29.47  ? 1808 LEU A N     1 
ATOM   3918  C  CA    . LEU A 1 1808 ? 166.277 147.134 107.586 1.00 26.85  ? 1808 LEU A CA    1 
ATOM   3919  C  C     . LEU A 1 1808 ? 165.221 147.860 108.405 1.00 27.50  ? 1808 LEU A C     1 
ATOM   3920  O  O     . LEU A 1 1808 ? 164.511 148.726 107.886 1.00 32.14  ? 1808 LEU A O     1 
ATOM   3921  C  CB    . LEU A 1 1808 ? 165.745 145.778 107.122 1.00 32.78  ? 1808 LEU A CB    1 
ATOM   3922  C  CG    . LEU A 1 1808 ? 166.544 145.007 106.074 1.00 31.95  ? 1808 LEU A CG    1 
ATOM   3923  C  CD1   . LEU A 1 1808 ? 165.833 143.718 105.722 1.00 39.27  ? 1808 LEU A CD1   1 
ATOM   3924  C  CD2   . LEU A 1 1808 ? 166.751 145.847 104.838 1.00 30.85  ? 1808 LEU A CD2   1 
ATOM   3925  N  N     . GLU A 1 1809 ? 165.093 147.512 109.687 1.00 27.32  ? 1809 GLU A N     1 
ATOM   3926  C  CA    . GLU A 1 1809 ? 164.121 148.194 110.537 1.00 30.31  ? 1809 GLU A CA    1 
ATOM   3927  C  C     . GLU A 1 1809 ? 164.470 149.667 110.703 1.00 28.62  ? 1809 GLU A C     1 
ATOM   3928  O  O     . GLU A 1 1809 ? 163.586 150.531 110.659 1.00 32.27  ? 1809 GLU A O     1 
ATOM   3929  C  CB    . GLU A 1 1809 ? 164.036 147.502 111.896 1.00 39.08  ? 1809 GLU A CB    1 
ATOM   3930  C  CG    . GLU A 1 1809 ? 163.422 146.115 111.842 1.00 47.36  ? 1809 GLU A CG    1 
ATOM   3931  C  CD    . GLU A 1 1809 ? 163.465 145.408 113.179 1.00 60.62  ? 1809 GLU A CD    1 
ATOM   3932  O  OE1   . GLU A 1 1809 ? 163.957 146.011 114.155 1.00 57.43  ? 1809 GLU A OE1   1 
ATOM   3933  O  OE2   . GLU A 1 1809 ? 163.009 144.248 113.254 1.00 66.06  ? 1809 GLU A OE2   1 
ATOM   3934  N  N     . HIS A 1 1810 ? 165.756 149.974 110.893 1.00 27.84  ? 1810 HIS A N     1 
ATOM   3935  C  CA    . HIS A 1 1810 ? 166.178 151.367 111.000 1.00 25.83  ? 1810 HIS A CA    1 
ATOM   3936  C  C     . HIS A 1 1810 ? 165.891 152.128 109.713 1.00 25.07  ? 1810 HIS A C     1 
ATOM   3937  O  O     . HIS A 1 1810 ? 165.410 153.267 109.747 1.00 31.46  ? 1810 HIS A O     1 
ATOM   3938  C  CB    . HIS A 1 1810 ? 167.667 151.441 111.336 1.00 27.31  ? 1810 HIS A CB    1 
ATOM   3939  C  CG    . HIS A 1 1810 ? 168.000 150.985 112.721 1.00 33.30  ? 1810 HIS A CG    1 
ATOM   3940  N  ND1   . HIS A 1 1810 ? 167.038 150.630 113.640 1.00 35.74  ? 1810 HIS A ND1   1 
ATOM   3941  C  CD2   . HIS A 1 1810 ? 169.192 150.825 113.342 1.00 35.70  ? 1810 HIS A CD2   1 
ATOM   3942  C  CE1   . HIS A 1 1810 ? 167.622 150.270 114.769 1.00 41.38  ? 1810 HIS A CE1   1 
ATOM   3943  N  NE2   . HIS A 1 1810 ? 168.929 150.380 114.614 1.00 43.65  ? 1810 HIS A NE2   1 
ATOM   3944  N  N     . LEU A 1 1811 ? 166.176 151.509 108.567 1.00 25.51  ? 1811 LEU A N     1 
ATOM   3945  C  CA    . LEU A 1 1811 ? 165.926 152.160 107.287 1.00 24.63  ? 1811 LEU A CA    1 
ATOM   3946  C  C     . LEU A 1 1811 ? 164.438 152.388 107.062 1.00 29.34  ? 1811 LEU A C     1 
ATOM   3947  O  O     . LEU A 1 1811 ? 164.042 153.418 106.512 1.00 33.64  ? 1811 LEU A O     1 
ATOM   3948  C  CB    . LEU A 1 1811 ? 166.516 151.325 106.154 1.00 25.48  ? 1811 LEU A CB    1 
ATOM   3949  C  CG    . LEU A 1 1811 ? 167.950 151.628 105.727 1.00 26.59  ? 1811 LEU A CG    1 
ATOM   3950  C  CD1   . LEU A 1 1811 ? 168.348 150.703 104.601 1.00 34.12  ? 1811 LEU A CD1   1 
ATOM   3951  C  CD2   . LEU A 1 1811 ? 168.093 153.071 105.299 1.00 24.67  ? 1811 LEU A CD2   1 
ATOM   3952  N  N     . ILE A 1 1812 ? 163.598 151.437 107.472 1.00 29.55  ? 1812 ILE A N     1 
ATOM   3953  C  CA    . ILE A 1 1812 ? 162.155 151.613 107.334 1.00 25.63  ? 1812 ILE A CA    1 
ATOM   3954  C  C     . ILE A 1 1812 ? 161.665 152.743 108.230 1.00 27.00  ? 1812 ILE A C     1 
ATOM   3955  O  O     . ILE A 1 1812 ? 160.846 153.570 107.812 1.00 35.57  ? 1812 ILE A O     1 
ATOM   3956  C  CB    . ILE A 1 1812 ? 161.423 150.294 107.635 1.00 28.20  ? 1812 ILE A CB    1 
ATOM   3957  C  CG1   . ILE A 1 1812 ? 161.649 149.289 106.509 1.00 32.17  ? 1812 ILE A CG1   1 
ATOM   3958  C  CG2   . ILE A 1 1812 ? 159.941 150.541 107.821 1.00 29.50  ? 1812 ILE A CG2   1 
ATOM   3959  C  CD1   . ILE A 1 1812 ? 160.871 148.013 106.672 1.00 34.50  ? 1812 ILE A CD1   1 
ATOM   3960  N  N     . THR A 1 1813 ? 162.145 152.792 109.475 1.00 25.95  ? 1813 THR A N     1 
ATOM   3961  C  CA    . THR A 1 1813 ? 161.752 153.870 110.378 1.00 23.35  ? 1813 THR A CA    1 
ATOM   3962  C  C     . THR A 1 1813 ? 162.173 155.226 109.825 1.00 26.12  ? 1813 THR A C     1 
ATOM   3963  O  O     . THR A 1 1813 ? 161.435 156.211 109.936 1.00 31.67  ? 1813 THR A O     1 
ATOM   3964  C  CB    . THR A 1 1813 ? 162.364 153.642 111.761 1.00 25.64  ? 1813 THR A CB    1 
ATOM   3965  O  OG1   . THR A 1 1813 ? 161.816 152.450 112.336 1.00 31.64  ? 1813 THR A OG1   1 
ATOM   3966  C  CG2   . THR A 1 1813 ? 162.074 154.813 112.677 1.00 27.70  ? 1813 THR A CG2   1 
ATOM   3967  N  N     . GLU A 1 1814 ? 163.358 155.289 109.223 1.00 28.00  ? 1814 GLU A N     1 
ATOM   3968  C  CA    . GLU A 1 1814 ? 163.806 156.501 108.548 1.00 27.60  ? 1814 GLU A CA    1 
ATOM   3969  C  C     . GLU A 1 1814 ? 162.900 156.873 107.380 1.00 26.93  ? 1814 GLU A C     1 
ATOM   3970  O  O     . GLU A 1 1814 ? 162.447 158.019 107.268 1.00 33.66  ? 1814 GLU A O     1 
ATOM   3971  C  CB    . GLU A 1 1814 ? 165.227 156.296 108.048 1.00 25.85  ? 1814 GLU A CB    1 
ATOM   3972  C  CG    . GLU A 1 1814 ? 165.807 157.480 107.355 1.00 28.44  ? 1814 GLU A CG    1 
ATOM   3973  C  CD    . GLU A 1 1814 ? 166.915 157.055 106.438 1.00 41.43  ? 1814 GLU A CD    1 
ATOM   3974  O  OE1   . GLU A 1 1814 ? 166.869 155.898 105.978 1.00 40.46  ? 1814 GLU A OE1   1 
ATOM   3975  O  OE2   . GLU A 1 1814 ? 167.811 157.865 106.152 1.00 47.19  ? 1814 GLU A OE2   1 
ATOM   3976  N  N     . LEU A 1 1815 ? 162.647 155.921 106.480 1.00 25.76  ? 1815 LEU A N     1 
ATOM   3977  C  CA    . LEU A 1 1815 ? 161.970 156.248 105.233 1.00 24.69  ? 1815 LEU A CA    1 
ATOM   3978  C  C     . LEU A 1 1815 ? 160.495 156.536 105.449 1.00 27.52  ? 1815 LEU A C     1 
ATOM   3979  O  O     . LEU A 1 1815 ? 159.895 157.268 104.661 1.00 32.70  ? 1815 LEU A O     1 
ATOM   3980  C  CB    . LEU A 1 1815 ? 162.145 155.121 104.220 1.00 25.41  ? 1815 LEU A CB    1 
ATOM   3981  C  CG    . LEU A 1 1815 ? 163.555 154.856 103.696 1.00 24.91  ? 1815 LEU A CG    1 
ATOM   3982  C  CD1   . LEU A 1 1815 ? 163.490 153.994 102.460 1.00 32.30  ? 1815 LEU A CD1   1 
ATOM   3983  C  CD2   . LEU A 1 1815 ? 164.275 156.149 103.397 1.00 23.80  ? 1815 LEU A CD2   1 
ATOM   3984  N  N     . VAL A 1 1816 ? 159.891 155.984 106.502 1.00 27.49  ? 1816 VAL A N     1 
ATOM   3985  C  CA    . VAL A 1 1816 ? 158.521 156.359 106.837 1.00 27.95  ? 1816 VAL A CA    1 
ATOM   3986  C  C     . VAL A 1 1816 ? 158.454 157.843 107.169 1.00 32.70  ? 1816 VAL A C     1 
ATOM   3987  O  O     . VAL A 1 1816 ? 157.587 158.574 106.675 1.00 38.07  ? 1816 VAL A O     1 
ATOM   3988  C  CB    . VAL A 1 1816 ? 157.997 155.493 107.995 1.00 26.84  ? 1816 VAL A CB    1 
ATOM   3989  C  CG1   . VAL A 1 1816 ? 156.781 156.138 108.628 1.00 34.81  ? 1816 VAL A CG1   1 
ATOM   3990  C  CG2   . VAL A 1 1816 ? 157.663 154.100 107.499 1.00 29.50  ? 1816 VAL A CG2   1 
ATOM   3991  N  N     . HIS A 1 1817 ? 159.392 158.315 107.993 1.00 29.97  ? 1817 HIS A N     1 
ATOM   3992  C  CA    . HIS A 1 1817 ? 159.458 159.735 108.320 1.00 28.77  ? 1817 HIS A CA    1 
ATOM   3993  C  C     . HIS A 1 1817 ? 159.758 160.576 107.087 1.00 28.01  ? 1817 HIS A C     1 
ATOM   3994  O  O     . HIS A 1 1817 ? 159.194 161.662 106.916 1.00 33.24  ? 1817 HIS A O     1 
ATOM   3995  C  CB    . HIS A 1 1817 ? 160.514 159.970 109.398 1.00 28.02  ? 1817 HIS A CB    1 
ATOM   3996  C  CG    . HIS A 1 1817 ? 160.826 161.414 109.632 1.00 31.22  ? 1817 HIS A CG    1 
ATOM   3997  N  ND1   . HIS A 1 1817 ? 159.907 162.301 110.148 1.00 38.39  ? 1817 HIS A ND1   1 
ATOM   3998  C  CD2   . HIS A 1 1817 ? 161.956 162.127 109.415 1.00 32.06  ? 1817 HIS A CD2   1 
ATOM   3999  C  CE1   . HIS A 1 1817 ? 160.459 163.498 110.242 1.00 39.25  ? 1817 HIS A CE1   1 
ATOM   4000  N  NE2   . HIS A 1 1817 ? 161.701 163.419 109.803 1.00 41.06  ? 1817 HIS A NE2   1 
ATOM   4001  N  N     . GLN A 1 1818 ? 160.659 160.101 106.226 1.00 27.10  ? 1818 GLN A N     1 
ATOM   4002  C  CA    . GLN A 1 1818 ? 160.984 160.854 105.017 1.00 25.67  ? 1818 GLN A CA    1 
ATOM   4003  C  C     . GLN A 1 1818 ? 159.779 160.967 104.092 1.00 29.33  ? 1818 GLN A C     1 
ATOM   4004  O  O     . GLN A 1 1818 ? 159.529 162.031 103.514 1.00 33.68  ? 1818 GLN A O     1 
ATOM   4005  C  CB    . GLN A 1 1818 ? 162.157 160.203 104.289 1.00 25.71  ? 1818 GLN A CB    1 
ATOM   4006  C  CG    . GLN A 1 1818 ? 163.455 160.239 105.065 1.00 25.30  ? 1818 GLN A CG    1 
ATOM   4007  C  CD    . GLN A 1 1818 ? 164.619 159.727 104.256 1.00 27.63  ? 1818 GLN A CD    1 
ATOM   4008  O  OE1   . GLN A 1 1818 ? 164.460 159.328 103.105 1.00 32.05  ? 1818 GLN A OE1   1 
ATOM   4009  N  NE2   . GLN A 1 1818 ? 165.802 159.739 104.850 1.00 27.06  ? 1818 GLN A NE2   1 
ATOM   4010  N  N     . ARG A 1 1819 ? 159.021 159.881 103.939 1.00 31.70  ? 1819 ARG A N     1 
ATOM   4011  C  CA    . ARG A 1 1819 ? 157.809 159.920 103.129 1.00 28.75  ? 1819 ARG A CA    1 
ATOM   4012  C  C     . ARG A 1 1819 ? 156.772 160.848 103.742 1.00 33.94  ? 1819 ARG A C     1 
ATOM   4013  O  O     . ARG A 1 1819 ? 156.094 161.590 103.024 1.00 37.42  ? 1819 ARG A O     1 
ATOM   4014  C  CB    . ARG A 1 1819 ? 157.245 158.509 102.971 1.00 32.27  ? 1819 ARG A CB    1 
ATOM   4015  C  CG    . ARG A 1 1819 ? 155.836 158.453 102.417 1.00 42.67  ? 1819 ARG A CG    1 
ATOM   4016  C  CD    . ARG A 1 1819 ? 155.249 157.062 102.559 1.00 41.79  ? 1819 ARG A CD    1 
ATOM   4017  N  NE    . ARG A 1 1819 ? 155.097 156.675 103.955 1.00 37.20  ? 1819 ARG A NE    1 
ATOM   4018  C  CZ    . ARG A 1 1819 ? 154.719 155.470 104.360 1.00 43.10  ? 1819 ARG A CZ    1 
ATOM   4019  N  NH1   . ARG A 1 1819 ? 154.456 154.503 103.497 1.00 40.07  ? 1819 ARG A NH1   1 
ATOM   4020  N  NH2   . ARG A 1 1819 ? 154.602 155.231 105.662 1.00 40.14  ? 1819 ARG A NH2   1 
ATOM   4021  N  N     . ASP A 1 1820 ? 156.634 160.823 105.070 1.00 34.58  ? 1820 ASP A N     1 
ATOM   4022  C  CA    . ASP A 1 1820 ? 155.707 161.734 105.732 1.00 31.96  ? 1820 ASP A CA    1 
ATOM   4023  C  C     . ASP A 1 1820 ? 156.089 163.187 105.482 1.00 34.10  ? 1820 ASP A C     1 
ATOM   4024  O  O     . ASP A 1 1820 ? 155.231 164.020 105.161 1.00 44.02  ? 1820 ASP A O     1 
ATOM   4025  C  CB    . ASP A 1 1820 ? 155.674 161.441 107.231 1.00 34.74  ? 1820 ASP A CB    1 
ATOM   4026  C  CG    . ASP A 1 1820 ? 154.946 160.153 107.559 1.00 53.58  ? 1820 ASP A CG    1 
ATOM   4027  O  OD1   . ASP A 1 1820 ? 154.874 159.269 106.680 1.00 53.24  ? 1820 ASP A OD1   1 
ATOM   4028  O  OD2   . ASP A 1 1820 ? 154.454 160.019 108.698 1.00 60.28  ? 1820 ASP A OD2   1 
ATOM   4029  N  N     . VAL A 1 1821 ? 157.377 163.507 105.611 1.00 30.54  ? 1821 VAL A N     1 
ATOM   4030  C  CA    . VAL A 1 1821 ? 157.831 164.879 105.406 1.00 28.08  ? 1821 VAL A CA    1 
ATOM   4031  C  C     . VAL A 1 1821 ? 157.632 165.301 103.957 1.00 33.67  ? 1821 VAL A C     1 
ATOM   4032  O  O     . VAL A 1 1821 ? 157.211 166.429 103.679 1.00 42.21  ? 1821 VAL A O     1 
ATOM   4033  C  CB    . VAL A 1 1821 ? 159.299 165.030 105.845 1.00 28.10  ? 1821 VAL A CB    1 
ATOM   4034  C  CG1   . VAL A 1 1821 ? 159.846 166.372 105.406 1.00 33.34  ? 1821 VAL A CG1   1 
ATOM   4035  C  CG2   . VAL A 1 1821 ? 159.406 164.891 107.344 1.00 28.62  ? 1821 VAL A CG2   1 
ATOM   4036  N  N     . THR A 1 1822 ? 157.941 164.413 103.009 1.00 31.38  ? 1822 THR A N     1 
ATOM   4037  C  CA    . THR A 1 1822 ? 157.758 164.753 101.602 1.00 31.33  ? 1822 THR A CA    1 
ATOM   4038  C  C     . THR A 1 1822 ? 156.284 164.956 101.269 1.00 39.06  ? 1822 THR A C     1 
ATOM   4039  O  O     . THR A 1 1822 ? 155.932 165.858 100.500 1.00 51.71  ? 1822 THR A O     1 
ATOM   4040  C  CB    . THR A 1 1822 ? 158.365 163.670 100.713 1.00 31.01  ? 1822 THR A CB    1 
ATOM   4041  O  OG1   . THR A 1 1822 ? 159.671 163.336 101.194 1.00 33.56  ? 1822 THR A OG1   1 
ATOM   4042  C  CG2   . THR A 1 1822 ? 158.476 164.166 99.285  1.00 33.87  ? 1822 THR A CG2   1 
ATOM   4043  N  N     . ARG A 1 1823 ? 155.407 164.125 101.837 1.00 35.25  ? 1823 ARG A N     1 
ATOM   4044  C  CA    . ARG A 1 1823 ? 153.975 164.316 101.637 1.00 35.44  ? 1823 ARG A CA    1 
ATOM   4045  C  C     . ARG A 1 1823 ? 153.516 165.649 102.207 1.00 42.25  ? 1823 ARG A C     1 
ATOM   4046  O  O     . ARG A 1 1823 ? 152.697 166.342 101.597 1.00 49.77  ? 1823 ARG A O     1 
ATOM   4047  C  CB    . ARG A 1 1823 ? 153.194 163.168 102.275 1.00 37.94  ? 1823 ARG A CB    1 
ATOM   4048  C  CG    . ARG A 1 1823 ? 153.211 161.880 101.478 1.00 42.92  ? 1823 ARG A CG    1 
ATOM   4049  C  CD    . ARG A 1 1823 ? 152.504 160.768 102.231 1.00 45.45  ? 1823 ARG A CD    1 
ATOM   4050  N  NE    . ARG A 1 1823 ? 152.396 159.553 101.434 1.00 56.15  ? 1823 ARG A NE    1 
ATOM   4051  C  CZ    . ARG A 1 1823 ? 151.937 158.397 101.893 1.00 59.22  ? 1823 ARG A CZ    1 
ATOM   4052  N  NH1   . ARG A 1 1823 ? 151.536 158.261 103.146 1.00 54.97  ? 1823 ARG A NH1   1 
ATOM   4053  N  NH2   . ARG A 1 1823 ? 151.879 157.351 101.074 1.00 59.14  ? 1823 ARG A NH2   1 
ATOM   4054  N  N     . SER A 1 1824 ? 154.027 166.020 103.383 1.00 43.12  ? 1824 SER A N     1 
ATOM   4055  C  CA    . SER A 1 1824 ? 153.684 167.317 103.958 1.00 41.72  ? 1824 SER A CA    1 
ATOM   4056  C  C     . SER A 1 1824 ? 154.164 168.459 103.070 1.00 44.64  ? 1824 SER A C     1 
ATOM   4057  O  O     . SER A 1 1824 ? 153.444 169.443 102.866 1.00 51.23  ? 1824 SER A O     1 
ATOM   4058  C  CB    . SER A 1 1824 ? 154.276 167.439 105.361 1.00 42.96  ? 1824 SER A CB    1 
ATOM   4059  O  OG    . SER A 1 1824 ? 153.997 168.708 105.922 1.00 62.17  ? 1824 SER A OG    1 
ATOM   4060  N  N     . LEU A 1 1825 ? 155.381 168.343 102.534 1.00 44.02  ? 1825 LEU A N     1 
ATOM   4061  C  CA    . LEU A 1 1825 ? 155.910 169.380 101.653 1.00 43.00  ? 1825 LEU A CA    1 
ATOM   4062  C  C     . LEU A 1 1825 ? 155.072 169.512 100.390 1.00 48.02  ? 1825 LEU A C     1 
ATOM   4063  O  O     . LEU A 1 1825 ? 154.820 170.626 99.917  1.00 57.31  ? 1825 LEU A O     1 
ATOM   4064  C  CB    . LEU A 1 1825 ? 157.365 169.082 101.293 1.00 40.65  ? 1825 LEU A CB    1 
ATOM   4065  C  CG    . LEU A 1 1825 ? 158.401 169.108 102.416 1.00 38.87  ? 1825 LEU A CG    1 
ATOM   4066  C  CD1   . LEU A 1 1825 ? 159.801 169.044 101.838 1.00 36.80  ? 1825 LEU A CD1   1 
ATOM   4067  C  CD2   . LEU A 1 1825 ? 158.233 170.343 103.277 1.00 44.72  ? 1825 LEU A CD2   1 
ATOM   4068  N  N     . ILE A 1 1826 ? 154.645 168.386 99.817  1.00 49.39  ? 1826 ILE A N     1 
ATOM   4069  C  CA    . ILE A 1 1826 ? 153.808 168.433 98.622  1.00 49.14  ? 1826 ILE A CA    1 
ATOM   4070  C  C     . ILE A 1 1826 ? 152.445 169.034 98.945  1.00 53.87  ? 1826 ILE A C     1 
ATOM   4071  O  O     . ILE A 1 1826 ? 151.928 169.873 98.198  1.00 56.55  ? 1826 ILE A O     1 
ATOM   4072  C  CB    . ILE A 1 1826 ? 153.679 167.030 98.003  1.00 46.01  ? 1826 ILE A CB    1 
ATOM   4073  C  CG1   . ILE A 1 1826 ? 155.034 166.557 97.477  1.00 50.08  ? 1826 ILE A CG1   1 
ATOM   4074  C  CG2   . ILE A 1 1826 ? 152.652 167.030 96.886  1.00 50.41  ? 1826 ILE A CG2   1 
ATOM   4075  C  CD1   . ILE A 1 1826 ? 154.996 165.189 96.844  1.00 55.94  ? 1826 ILE A CD1   1 
ATOM   4076  N  N     . LYS A 1 1827 ? 151.843 168.617 100.062 1.00 55.99  ? 1827 LYS A N     1 
ATOM   4077  C  CA    . LYS A 1 1827 ? 150.509 169.091 100.414 1.00 55.81  ? 1827 LYS A CA    1 
ATOM   4078  C  C     . LYS A 1 1827 ? 150.503 170.588 100.695 1.00 58.66  ? 1827 LYS A C     1 
ATOM   4079  O  O     . LYS A 1 1827 ? 149.598 171.305 100.253 1.00 66.63  ? 1827 LYS A O     1 
ATOM   4080  C  CB    . LYS A 1 1827 ? 149.983 168.317 101.622 1.00 58.46  ? 1827 LYS A CB    1 
ATOM   4081  C  CG    . LYS A 1 1827 ? 148.721 168.898 102.232 1.00 68.28  ? 1827 LYS A CG    1 
ATOM   4082  C  CD    . LYS A 1 1827 ? 148.301 168.130 103.472 1.00 78.80  ? 1827 LYS A CD    1 
ATOM   4083  C  CE    . LYS A 1 1827 ? 147.067 168.747 104.109 1.00 85.16  ? 1827 LYS A CE    1 
ATOM   4084  N  NZ    . LYS A 1 1827 ? 146.658 168.029 105.346 1.00 82.02  ? 1827 LYS A NZ    1 
ATOM   4085  N  N     . SER A 1 1828 ? 151.504 171.082 101.422 1.00 56.91  ? 1828 SER A N     1 
ATOM   4086  C  CA    . SER A 1 1828 ? 151.548 172.500 101.752 1.00 59.61  ? 1828 SER A CA    1 
ATOM   4087  C  C     . SER A 1 1828 ? 152.086 173.357 100.614 1.00 65.88  ? 1828 SER A C     1 
ATOM   4088  O  O     . SER A 1 1828 ? 152.133 174.584 100.758 1.00 72.01  ? 1828 SER A O     1 
ATOM   4089  C  CB    . SER A 1 1828 ? 152.384 172.720 103.013 1.00 62.76  ? 1828 SER A CB    1 
ATOM   4090  O  OG    . SER A 1 1828 ? 151.842 172.015 104.115 1.00 60.92  ? 1828 SER A OG    1 
ATOM   4091  N  N     . LYS A 1 1829 ? 152.498 172.744 99.503  1.00 64.66  ? 1829 LYS A N     1 
ATOM   4092  C  CA    . LYS A 1 1829 ? 152.892 173.459 98.286  1.00 63.40  ? 1829 LYS A CA    1 
ATOM   4093  C  C     . LYS A 1 1829 ? 154.091 174.377 98.528  1.00 70.00  ? 1829 LYS A C     1 
ATOM   4094  O  O     . LYS A 1 1829 ? 154.074 175.560 98.183  1.00 78.00  ? 1829 LYS A O     1 
ATOM   4095  C  CB    . LYS A 1 1829 ? 151.713 174.244 97.704  1.00 66.80  ? 1829 LYS A CB    1 
ATOM   4096  C  CG    . LYS A 1 1829 ? 150.435 173.436 97.532  1.00 68.53  ? 1829 LYS A CG    1 
ATOM   4097  C  CD    . LYS A 1 1829 ? 150.626 172.291 96.551  1.00 72.38  ? 1829 LYS A CD    1 
ATOM   4098  C  CE    . LYS A 1 1829 ? 150.904 172.801 95.148  1.00 75.23  ? 1829 LYS A CE    1 
ATOM   4099  N  NZ    . LYS A 1 1829 ? 149.766 173.595 94.613  1.00 69.01  ? 1829 LYS A NZ    1 
ATOM   4100  N  N     . ILE A 1 1830 ? 155.143 173.822 99.128  1.00 66.44  ? 1830 ILE A N     1 
ATOM   4101  C  CA    . ILE A 1 1830 ? 156.394 174.559 99.267  1.00 68.78  ? 1830 ILE A CA    1 
ATOM   4102  C  C     . ILE A 1 1830 ? 157.126 174.564 97.935  1.00 73.95  ? 1830 ILE A C     1 
ATOM   4103  O  O     . ILE A 1 1830 ? 157.287 173.519 97.292  1.00 78.54  ? 1830 ILE A O     1 
ATOM   4104  C  CB    . ILE A 1 1830 ? 157.271 173.962 100.378 1.00 64.54  ? 1830 ILE A CB    1 
ATOM   4105  C  CG1   . ILE A 1 1830 ? 156.590 174.078 101.742 1.00 66.34  ? 1830 ILE A CG1   1 
ATOM   4106  C  CG2   . ILE A 1 1830 ? 158.633 174.633 100.409 1.00 62.03  ? 1830 ILE A CG2   1 
ATOM   4107  C  CD1   . ILE A 1 1830 ? 155.713 172.923 102.097 1.00 63.32  ? 1830 ILE A CD1   1 
ATOM   4108  N  N     . ASP A 1 1831 ? 157.574 175.746 97.511  1.00 72.22  ? 1831 ASP A N     1 
ATOM   4109  C  CA    . ASP A 1 1831 ? 158.322 175.892 96.273  1.00 78.16  ? 1831 ASP A CA    1 
ATOM   4110  C  C     . ASP A 1 1831 ? 159.723 176.451 96.460  1.00 78.54  ? 1831 ASP A C     1 
ATOM   4111  O  O     . ASP A 1 1831 ? 160.487 176.477 95.490  1.00 81.43  ? 1831 ASP A O     1 
ATOM   4112  C  CB    . ASP A 1 1831 ? 157.560 176.796 95.290  1.00 86.05  ? 1831 ASP A CB    1 
ATOM   4113  C  CG    . ASP A 1 1831 ? 157.489 178.236 95.756  1.00 90.30  ? 1831 ASP A CG    1 
ATOM   4114  O  OD1   . ASP A 1 1831 ? 158.270 179.068 95.248  1.00 93.83  ? 1831 ASP A OD1   1 
ATOM   4115  O  OD2   . ASP A 1 1831 ? 156.653 178.537 96.634  1.00 87.81  ? 1831 ASP A OD2   1 
ATOM   4116  N  N     . ASN A 1 1832 ? 160.083 176.890 97.663  1.00 72.13  ? 1832 ASN A N     1 
ATOM   4117  C  CA    . ASN A 1 1832 ? 161.374 177.507 97.924  1.00 65.56  ? 1832 ASN A CA    1 
ATOM   4118  C  C     . ASN A 1 1832 ? 162.126 176.699 98.971  1.00 63.50  ? 1832 ASN A C     1 
ATOM   4119  O  O     . ASN A 1 1832 ? 161.528 176.186 99.922  1.00 67.07  ? 1832 ASN A O     1 
ATOM   4120  C  CB    . ASN A 1 1832 ? 161.202 178.954 98.401  1.00 66.36  ? 1832 ASN A CB    1 
ATOM   4121  C  CG    . ASN A 1 1832 ? 162.517 179.705 98.479  1.00 72.88  ? 1832 ASN A CG    1 
ATOM   4122  O  OD1   . ASN A 1 1832 ? 163.580 179.154 98.196  1.00 76.80  ? 1832 ASN A OD1   1 
ATOM   4123  N  ND2   . ASN A 1 1832 ? 162.449 180.973 98.867  1.00 75.48  ? 1832 ASN A ND2   1 
ATOM   4124  N  N     . ALA A 1 1833 ? 163.444 176.590 98.792  1.00 60.27  ? 1833 ALA A N     1 
ATOM   4125  C  CA    . ALA A 1 1833 ? 164.268 175.861 99.747  1.00 55.87  ? 1833 ALA A CA    1 
ATOM   4126  C  C     . ALA A 1 1833 ? 164.465 176.626 101.048 1.00 55.43  ? 1833 ALA A C     1 
ATOM   4127  O  O     . ALA A 1 1833 ? 164.918 176.037 102.035 1.00 57.82  ? 1833 ALA A O     1 
ATOM   4128  C  CB    . ALA A 1 1833 ? 165.627 175.534 99.128  1.00 53.99  ? 1833 ALA A CB    1 
ATOM   4129  N  N     . LYS A 1 1834 ? 164.146 177.918 101.073 1.00 56.24  ? 1834 LYS A N     1 
ATOM   4130  C  CA    . LYS A 1 1834 ? 164.265 178.728 102.277 1.00 52.21  ? 1834 LYS A CA    1 
ATOM   4131  C  C     . LYS A 1 1834 ? 162.961 178.839 103.053 1.00 51.61  ? 1834 LYS A C     1 
ATOM   4132  O  O     . LYS A 1 1834 ? 162.918 179.547 104.063 1.00 53.58  ? 1834 LYS A O     1 
ATOM   4133  C  CB    . LYS A 1 1834 ? 164.770 180.130 101.924 1.00 56.67  ? 1834 LYS A CB    1 
ATOM   4134  C  CG    . LYS A 1 1834 ? 165.927 180.143 100.943 1.00 63.38  ? 1834 LYS A CG    1 
ATOM   4135  C  CD    . LYS A 1 1834 ? 167.217 179.702 101.612 1.00 64.51  ? 1834 LYS A CD    1 
ATOM   4136  C  CE    . LYS A 1 1834 ? 167.677 180.716 102.645 1.00 66.23  ? 1834 LYS A CE    1 
ATOM   4137  N  NZ    . LYS A 1 1834 ? 168.483 180.084 103.725 1.00 63.57  ? 1834 LYS A NZ    1 
ATOM   4138  N  N     . SER A 1 1835 ? 161.901 178.171 102.607 1.00 49.29  ? 1835 SER A N     1 
ATOM   4139  C  CA    . SER A 1 1835 ? 160.650 178.179 103.349 1.00 48.36  ? 1835 SER A CA    1 
ATOM   4140  C  C     . SER A 1 1835 ? 160.822 177.449 104.673 1.00 45.20  ? 1835 SER A C     1 
ATOM   4141  O  O     . SER A 1 1835 ? 161.532 176.444 104.756 1.00 47.55  ? 1835 SER A O     1 
ATOM   4142  C  CB    . SER A 1 1835 ? 159.540 177.528 102.526 1.00 53.29  ? 1835 SER A CB    1 
ATOM   4143  O  OG    . SER A 1 1835 ? 158.377 177.328 103.309 1.00 61.73  ? 1835 SER A OG    1 
ATOM   4144  N  N     . PHE A 1 1836 ? 160.168 177.960 105.718 1.00 41.01  ? 1836 PHE A N     1 
ATOM   4145  C  CA    . PHE A 1 1836 ? 160.325 177.361 107.037 1.00 40.60  ? 1836 PHE A CA    1 
ATOM   4146  C  C     . PHE A 1 1836 ? 159.706 175.975 107.129 1.00 45.01  ? 1836 PHE A C     1 
ATOM   4147  O  O     . PHE A 1 1836 ? 160.052 175.219 108.041 1.00 48.45  ? 1836 PHE A O     1 
ATOM   4148  C  CB    . PHE A 1 1836 ? 159.724 178.256 108.117 1.00 34.20  ? 1836 PHE A CB    1 
ATOM   4149  C  CG    . PHE A 1 1836 ? 160.142 177.877 109.505 1.00 28.30  ? 1836 PHE A CG    1 
ATOM   4150  C  CD1   . PHE A 1 1836 ? 161.427 178.126 109.946 1.00 28.92  ? 1836 PHE A CD1   1 
ATOM   4151  C  CD2   . PHE A 1 1836 ? 159.257 177.250 110.361 1.00 29.07  ? 1836 PHE A CD2   1 
ATOM   4152  C  CE1   . PHE A 1 1836 ? 161.816 177.771 111.219 1.00 32.97  ? 1836 PHE A CE1   1 
ATOM   4153  C  CE2   . PHE A 1 1836 ? 159.644 176.891 111.635 1.00 27.91  ? 1836 PHE A CE2   1 
ATOM   4154  C  CZ    . PHE A 1 1836 ? 160.923 177.153 112.064 1.00 29.20  ? 1836 PHE A CZ    1 
ATOM   4155  N  N     . GLU A 1 1837 ? 158.797 175.622 106.219 1.00 46.00  ? 1837 GLU A N     1 
ATOM   4156  C  CA    . GLU A 1 1837 ? 158.282 174.259 106.211 1.00 50.30  ? 1837 GLU A CA    1 
ATOM   4157  C  C     . GLU A 1 1837 ? 159.382 173.260 105.882 1.00 49.28  ? 1837 GLU A C     1 
ATOM   4158  O  O     . GLU A 1 1837 ? 159.324 172.105 106.317 1.00 50.40  ? 1837 GLU A O     1 
ATOM   4159  C  CB    . GLU A 1 1837 ? 157.129 174.133 105.219 1.00 58.47  ? 1837 GLU A CB    1 
ATOM   4160  C  CG    . GLU A 1 1837 ? 155.769 174.491 105.793 1.00 70.29  ? 1837 GLU A CG    1 
ATOM   4161  C  CD    . GLU A 1 1837 ? 155.549 175.989 105.881 1.00 79.31  ? 1837 GLU A CD    1 
ATOM   4162  O  OE1   . GLU A 1 1837 ? 156.249 176.736 105.165 1.00 73.57  ? 1837 GLU A OE1   1 
ATOM   4163  O  OE2   . GLU A 1 1837 ? 154.676 176.419 106.662 1.00 77.06  ? 1837 GLU A OE2   1 
ATOM   4164  N  N     . TRP A 1 1838 ? 160.387 173.685 105.118 1.00 45.72  ? 1838 TRP A N     1 
ATOM   4165  C  CA    . TRP A 1 1838 ? 161.559 172.866 104.841 1.00 38.22  ? 1838 TRP A CA    1 
ATOM   4166  C  C     . TRP A 1 1838 ? 162.699 173.141 105.812 1.00 40.31  ? 1838 TRP A C     1 
ATOM   4167  O  O     . TRP A 1 1838 ? 163.418 172.214 106.196 1.00 49.13  ? 1838 TRP A O     1 
ATOM   4168  C  CB    . TRP A 1 1838 ? 162.036 173.096 103.405 1.00 35.36  ? 1838 TRP A CB    1 
ATOM   4169  C  CG    . TRP A 1 1838 ? 163.277 172.333 103.037 1.00 36.11  ? 1838 TRP A CG    1 
ATOM   4170  C  CD1   . TRP A 1 1838 ? 164.408 172.843 102.477 1.00 38.24  ? 1838 TRP A CD1   1 
ATOM   4171  C  CD2   . TRP A 1 1838 ? 163.509 170.926 103.195 1.00 40.11  ? 1838 TRP A CD2   1 
ATOM   4172  N  NE1   . TRP A 1 1838 ? 165.331 171.848 102.280 1.00 41.61  ? 1838 TRP A NE1   1 
ATOM   4173  C  CE2   . TRP A 1 1838 ? 164.803 170.661 102.712 1.00 37.69  ? 1838 TRP A CE2   1 
ATOM   4174  C  CE3   . TRP A 1 1838 ? 162.749 169.866 103.700 1.00 41.27  ? 1838 TRP A CE3   1 
ATOM   4175  C  CZ2   . TRP A 1 1838 ? 165.353 169.383 102.716 1.00 37.22  ? 1838 TRP A CZ2   1 
ATOM   4176  C  CZ3   . TRP A 1 1838 ? 163.299 168.600 103.705 1.00 38.81  ? 1838 TRP A CZ3   1 
ATOM   4177  C  CH2   . TRP A 1 1838 ? 164.588 168.369 103.219 1.00 38.03  ? 1838 TRP A CH2   1 
ATOM   4178  N  N     . LEU A 1 1839 ? 162.879 174.400 106.219 1.00 39.66  ? 1839 LEU A N     1 
ATOM   4179  C  CA    . LEU A 1 1839 ? 163.956 174.730 107.147 1.00 34.78  ? 1839 LEU A CA    1 
ATOM   4180  C  C     . LEU A 1 1839 ? 163.745 174.090 108.512 1.00 35.42  ? 1839 LEU A C     1 
ATOM   4181  O  O     . LEU A 1 1839 ? 164.719 173.720 109.175 1.00 39.41  ? 1839 LEU A O     1 
ATOM   4182  C  CB    . LEU A 1 1839 ? 164.089 176.244 107.292 1.00 34.66  ? 1839 LEU A CB    1 
ATOM   4183  C  CG    . LEU A 1 1839 ? 164.582 177.021 106.073 1.00 39.43  ? 1839 LEU A CG    1 
ATOM   4184  C  CD1   . LEU A 1 1839 ? 164.937 178.442 106.464 1.00 45.06  ? 1839 LEU A CD1   1 
ATOM   4185  C  CD2   . LEU A 1 1839 ? 165.774 176.330 105.436 1.00 37.18  ? 1839 LEU A CD2   1 
ATOM   4186  N  N     . SER A 1 1840 ? 162.493 173.950 108.951 1.00 33.15  ? 1840 SER A N     1 
ATOM   4187  C  CA    . SER A 1 1840 ? 162.223 173.336 110.244 1.00 31.03  ? 1840 SER A CA    1 
ATOM   4188  C  C     . SER A 1 1840 ? 162.558 171.853 110.276 1.00 40.34  ? 1840 SER A C     1 
ATOM   4189  O  O     . SER A 1 1840 ? 162.643 171.281 111.367 1.00 42.09  ? 1840 SER A O     1 
ATOM   4190  C  CB    . SER A 1 1840 ? 160.759 173.537 110.629 1.00 34.35  ? 1840 SER A CB    1 
ATOM   4191  O  OG    . SER A 1 1840 ? 159.902 173.209 109.552 1.00 41.18  ? 1840 SER A OG    1 
ATOM   4192  N  N     . GLN A 1 1841 ? 162.746 171.221 109.122 1.00 41.69  ? 1841 GLN A N     1 
ATOM   4193  C  CA    . GLN A 1 1841 ? 163.105 169.814 109.064 1.00 35.10  ? 1841 GLN A CA    1 
ATOM   4194  C  C     . GLN A 1 1841 ? 164.613 169.658 109.174 1.00 32.84  ? 1841 GLN A C     1 
ATOM   4195  O  O     . GLN A 1 1841 ? 165.375 170.465 108.634 1.00 32.74  ? 1841 GLN A O     1 
ATOM   4196  C  CB    . GLN A 1 1841 ? 162.611 169.177 107.764 1.00 29.13  ? 1841 GLN A CB    1 
ATOM   4197  C  CG    . GLN A 1 1841 ? 161.245 169.656 107.317 1.00 34.51  ? 1841 GLN A CG    1 
ATOM   4198  C  CD    . GLN A 1 1841 ? 160.121 169.082 108.151 1.00 40.42  ? 1841 GLN A CD    1 
ATOM   4199  O  OE1   . GLN A 1 1841 ? 160.341 168.235 109.015 1.00 34.85  ? 1841 GLN A OE1   1 
ATOM   4200  N  NE2   . GLN A 1 1841 ? 158.905 169.546 107.898 1.00 47.47  ? 1841 GLN A NE2   1 
ATOM   4201  N  N     . MET A 1 1842 ? 165.039 168.617 109.882 1.00 32.63  ? 1842 MET A N     1 
ATOM   4202  C  CA    . MET A 1 1842 ? 166.460 168.341 110.022 1.00 29.75  ? 1842 MET A CA    1 
ATOM   4203  C  C     . MET A 1 1842 ? 167.043 167.921 108.681 1.00 28.63  ? 1842 MET A C     1 
ATOM   4204  O  O     . MET A 1 1842 ? 166.626 166.917 108.098 1.00 34.73  ? 1842 MET A O     1 
ATOM   4205  C  CB    . MET A 1 1842 ? 166.681 167.259 111.074 1.00 26.26  ? 1842 MET A CB    1 
ATOM   4206  C  CG    . MET A 1 1842 ? 168.123 167.101 111.489 1.00 30.46  ? 1842 MET A CG    1 
ATOM   4207  S  SD    . MET A 1 1842 ? 168.327 165.959 112.860 1.00 63.16  ? 1842 MET A SD    1 
ATOM   4208  C  CE    . MET A 1 1842 ? 168.275 167.087 114.248 1.00 34.39  ? 1842 MET A CE    1 
ATOM   4209  N  N     . ARG A 1 1843 ? 168.009 168.693 108.196 1.00 24.66  ? 1843 ARG A N     1 
ATOM   4210  C  CA    . ARG A 1 1843 ? 168.569 168.529 106.865 1.00 26.64  ? 1843 ARG A CA    1 
ATOM   4211  C  C     . ARG A 1 1843 ? 170.052 168.216 106.975 1.00 30.61  ? 1843 ARG A C     1 
ATOM   4212  O  O     . ARG A 1 1843 ? 170.737 168.723 107.867 1.00 31.51  ? 1843 ARG A O     1 
ATOM   4213  C  CB    . ARG A 1 1843 ? 168.361 169.789 106.029 1.00 30.20  ? 1843 ARG A CB    1 
ATOM   4214  C  CG    . ARG A 1 1843 ? 166.910 170.077 105.714 1.00 32.03  ? 1843 ARG A CG    1 
ATOM   4215  C  CD    . ARG A 1 1843 ? 166.658 171.565 105.591 1.00 31.77  ? 1843 ARG A CD    1 
ATOM   4216  N  NE    . ARG A 1 1843 ? 166.652 172.228 106.888 1.00 27.08  ? 1843 ARG A NE    1 
ATOM   4217  C  CZ    . ARG A 1 1843 ? 167.469 173.215 107.224 1.00 30.88  ? 1843 ARG A CZ    1 
ATOM   4218  N  NH1   . ARG A 1 1843 ? 168.371 173.684 106.379 1.00 30.61  ? 1843 ARG A NH1   1 
ATOM   4219  N  NH2   . ARG A 1 1843 ? 167.377 173.747 108.439 1.00 33.61  ? 1843 ARG A NH2   1 
ATOM   4220  N  N     . PHE A 1 1844 ? 170.544 167.383 106.065 1.00 30.81  ? 1844 PHE A N     1 
ATOM   4221  C  CA    . PHE A 1 1844 ? 171.921 166.909 106.092 1.00 26.68  ? 1844 PHE A CA    1 
ATOM   4222  C  C     . PHE A 1 1844 ? 172.623 167.347 104.817 1.00 34.31  ? 1844 PHE A C     1 
ATOM   4223  O  O     . PHE A 1 1844 ? 172.216 166.961 103.716 1.00 44.03  ? 1844 PHE A O     1 
ATOM   4224  C  CB    . PHE A 1 1844 ? 171.970 165.390 106.245 1.00 23.20  ? 1844 PHE A CB    1 
ATOM   4225  C  CG    . PHE A 1 1844 ? 171.208 164.878 107.430 1.00 21.62  ? 1844 PHE A CG    1 
ATOM   4226  C  CD1   . PHE A 1 1844 ? 169.839 164.695 107.366 1.00 21.12  ? 1844 PHE A CD1   1 
ATOM   4227  C  CD2   . PHE A 1 1844 ? 171.860 164.586 108.610 1.00 24.13  ? 1844 PHE A CD2   1 
ATOM   4228  C  CE1   . PHE A 1 1844 ? 169.140 164.229 108.455 1.00 24.62  ? 1844 PHE A CE1   1 
ATOM   4229  C  CE2   . PHE A 1 1844 ? 171.164 164.121 109.702 1.00 24.56  ? 1844 PHE A CE2   1 
ATOM   4230  C  CZ    . PHE A 1 1844 ? 169.803 163.943 109.625 1.00 24.30  ? 1844 PHE A CZ    1 
ATOM   4231  N  N     . TYR A 1 1845 ? 173.676 168.143 104.968 1.00 32.54  ? 1845 TYR A N     1 
ATOM   4232  C  CA    . TYR A 1 1845 ? 174.474 168.639 103.852 1.00 40.77  ? 1845 TYR A CA    1 
ATOM   4233  C  C     . TYR A 1 1845 ? 175.854 168.005 103.972 1.00 43.81  ? 1845 TYR A C     1 
ATOM   4234  O  O     . TYR A 1 1845 ? 176.625 168.342 104.876 1.00 45.38  ? 1845 TYR A O     1 
ATOM   4235  C  CB    . TYR A 1 1845 ? 174.541 170.163 103.869 1.00 41.32  ? 1845 TYR A CB    1 
ATOM   4236  C  CG    . TYR A 1 1845 ? 173.180 170.816 103.891 1.00 41.32  ? 1845 TYR A CG    1 
ATOM   4237  C  CD1   . TYR A 1 1845 ? 172.337 170.744 102.792 1.00 43.11  ? 1845 TYR A CD1   1 
ATOM   4238  C  CD2   . TYR A 1 1845 ? 172.733 171.493 105.014 1.00 38.99  ? 1845 TYR A CD2   1 
ATOM   4239  C  CE1   . TYR A 1 1845 ? 171.090 171.332 102.809 1.00 41.71  ? 1845 TYR A CE1   1 
ATOM   4240  C  CE2   . TYR A 1 1845 ? 171.488 172.085 105.041 1.00 38.85  ? 1845 TYR A CE2   1 
ATOM   4241  C  CZ    . TYR A 1 1845 ? 170.671 172.002 103.936 1.00 40.50  ? 1845 TYR A CZ    1 
ATOM   4242  O  OH    . TYR A 1 1845 ? 169.430 172.593 103.960 1.00 42.73  ? 1845 TYR A OH    1 
ATOM   4243  N  N     . PHE A 1 1846 ? 176.156 167.074 103.076 1.00 46.33  ? 1846 PHE A N     1 
ATOM   4244  C  CA    . PHE A 1 1846 ? 177.413 166.343 103.103 1.00 45.49  ? 1846 PHE A CA    1 
ATOM   4245  C  C     . PHE A 1 1846 ? 178.391 166.983 102.129 1.00 54.61  ? 1846 PHE A C     1 
ATOM   4246  O  O     . PHE A 1 1846 ? 178.070 167.170 100.951 1.00 58.82  ? 1846 PHE A O     1 
ATOM   4247  C  CB    . PHE A 1 1846 ? 177.196 164.872 102.749 1.00 46.80  ? 1846 PHE A CB    1 
ATOM   4248  C  CG    . PHE A 1 1846 ? 178.402 164.014 102.974 1.00 46.59  ? 1846 PHE A CG    1 
ATOM   4249  C  CD1   . PHE A 1 1846 ? 178.982 163.928 104.226 1.00 46.27  ? 1846 PHE A CD1   1 
ATOM   4250  C  CD2   . PHE A 1 1846 ? 178.958 163.295 101.934 1.00 46.28  ? 1846 PHE A CD2   1 
ATOM   4251  C  CE1   . PHE A 1 1846 ? 180.092 163.142 104.436 1.00 43.20  ? 1846 PHE A CE1   1 
ATOM   4252  C  CE2   . PHE A 1 1846 ? 180.066 162.508 102.139 1.00 49.89  ? 1846 PHE A CE2   1 
ATOM   4253  C  CZ    . PHE A 1 1846 ? 180.635 162.431 103.392 1.00 45.44  ? 1846 PHE A CZ    1 
ATOM   4254  N  N     . ASP A 1 1847 ? 179.579 167.317 102.626 1.00 57.42  ? 1847 ASP A N     1 
ATOM   4255  C  CA    . ASP A 1 1847 ? 180.627 167.944 101.825 1.00 61.91  ? 1847 ASP A CA    1 
ATOM   4256  C  C     . ASP A 1 1847 ? 181.869 167.072 101.942 1.00 68.26  ? 1847 ASP A C     1 
ATOM   4257  O  O     . ASP A 1 1847 ? 182.662 167.225 102.881 1.00 71.77  ? 1847 ASP A O     1 
ATOM   4258  C  CB    . ASP A 1 1847 ? 180.897 169.373 102.286 1.00 64.33  ? 1847 ASP A CB    1 
ATOM   4259  C  CG    . ASP A 1 1847 ? 181.776 170.134 101.325 1.00 78.19  ? 1847 ASP A CG    1 
ATOM   4260  O  OD1   . ASP A 1 1847 ? 182.064 169.593 100.239 1.00 82.60  ? 1847 ASP A OD1   1 
ATOM   4261  O  OD2   . ASP A 1 1847 ? 182.183 171.269 101.652 1.00 84.22  ? 1847 ASP A OD2   1 
ATOM   4262  N  N     . PRO A 1 1848 ? 182.067 166.137 101.010 1.00 71.29  ? 1848 PRO A N     1 
ATOM   4263  C  CA    . PRO A 1 1848 ? 183.189 165.194 101.145 1.00 69.16  ? 1848 PRO A CA    1 
ATOM   4264  C  C     . PRO A 1 1848 ? 184.551 165.817 100.900 1.00 77.87  ? 1848 PRO A C     1 
ATOM   4265  O  O     . PRO A 1 1848 ? 185.559 165.232 101.316 1.00 79.54  ? 1848 PRO A O     1 
ATOM   4266  C  CB    . PRO A 1 1848 ? 182.877 164.118 100.092 1.00 72.07  ? 1848 PRO A CB    1 
ATOM   4267  C  CG    . PRO A 1 1848 ? 181.489 164.433 99.575  1.00 68.10  ? 1848 PRO A CG    1 
ATOM   4268  C  CD    . PRO A 1 1848 ? 181.291 165.892 99.787  1.00 68.38  ? 1848 PRO A CD    1 
ATOM   4269  N  N     . LYS A 1 1849 ? 184.623 166.976 100.241 1.00 81.99  ? 1849 LYS A N     1 
ATOM   4270  C  CA    . LYS A 1 1849 ? 185.917 167.563 99.915  1.00 82.43  ? 1849 LYS A CA    1 
ATOM   4271  C  C     . LYS A 1 1849 ? 186.585 168.216 101.118 1.00 82.65  ? 1849 LYS A C     1 
ATOM   4272  O  O     . LYS A 1 1849 ? 187.773 168.547 101.044 1.00 84.29  ? 1849 LYS A O     1 
ATOM   4273  C  CB    . LYS A 1 1849 ? 185.764 168.589 98.791  1.00 82.74  ? 1849 LYS A CB    1 
ATOM   4274  C  CG    . LYS A 1 1849 ? 184.944 169.804 99.175  1.00 86.80  ? 1849 LYS A CG    1 
ATOM   4275  C  CD    . LYS A 1 1849 ? 184.855 170.803 98.035  1.00 90.15  ? 1849 LYS A CD    1 
ATOM   4276  C  CE    . LYS A 1 1849 ? 183.951 170.292 96.927  1.00 88.45  ? 1849 LYS A CE    1 
ATOM   4277  N  NZ    . LYS A 1 1849 ? 182.536 170.184 97.375  1.00 86.33  ? 1849 LYS A NZ    1 
ATOM   4278  N  N     . GLN A 1 1850 ? 185.854 168.417 102.213 1.00 78.98  ? 1850 GLN A N     1 
ATOM   4279  C  CA    . GLN A 1 1850 ? 186.436 169.039 103.396 1.00 80.92  ? 1850 GLN A CA    1 
ATOM   4280  C  C     . GLN A 1 1850 ? 187.543 168.165 103.972 1.00 84.82  ? 1850 GLN A C     1 
ATOM   4281  O  O     . GLN A 1 1850 ? 187.365 166.959 104.161 1.00 79.35  ? 1850 GLN A O     1 
ATOM   4282  C  CB    . GLN A 1 1850 ? 185.356 169.286 104.448 1.00 77.44  ? 1850 GLN A CB    1 
ATOM   4283  C  CG    . GLN A 1 1850 ? 184.374 170.381 104.084 1.00 79.74  ? 1850 GLN A CG    1 
ATOM   4284  C  CD    . GLN A 1 1850 ? 185.039 171.736 103.968 1.00 85.84  ? 1850 GLN A CD    1 
ATOM   4285  O  OE1   . GLN A 1 1850 ? 185.637 172.229 104.923 1.00 84.32  ? 1850 GLN A OE1   1 
ATOM   4286  N  NE2   . GLN A 1 1850 ? 184.940 172.345 102.792 1.00 89.95  ? 1850 GLN A NE2   1 
ATOM   4287  N  N     . THR A 1 1851 ? 188.691 168.785 104.251 1.00 89.46  ? 1851 THR A N     1 
ATOM   4288  C  CA    . THR A 1 1851 ? 189.817 168.040 104.806 1.00 92.16  ? 1851 THR A CA    1 
ATOM   4289  C  C     . THR A 1 1851 ? 189.524 167.567 106.224 1.00 89.78  ? 1851 THR A C     1 
ATOM   4290  O  O     . THR A 1 1851 ? 189.825 166.421 106.577 1.00 91.40  ? 1851 THR A O     1 
ATOM   4291  C  CB    . THR A 1 1851 ? 191.081 168.899 104.776 1.00 98.41  ? 1851 THR A CB    1 
ATOM   4292  O  OG1   . THR A 1 1851 ? 191.292 169.394 103.448 1.00 100.07 ? 1851 THR A OG1   1 
ATOM   4293  C  CG2   . THR A 1 1851 ? 192.292 168.082 105.204 1.00 98.30  ? 1851 THR A CG2   1 
ATOM   4294  N  N     . ASP A 1 1852 ? 188.936 168.429 107.049 1.00 83.07  ? 1852 ASP A N     1 
ATOM   4295  C  CA    . ASP A 1 1852 ? 188.616 168.059 108.421 1.00 80.20  ? 1852 ASP A CA    1 
ATOM   4296  C  C     . ASP A 1 1852 ? 187.378 167.173 108.435 1.00 77.40  ? 1852 ASP A C     1 
ATOM   4297  O  O     . ASP A 1 1852 ? 186.317 167.571 107.943 1.00 78.34  ? 1852 ASP A O     1 
ATOM   4298  C  CB    . ASP A 1 1852 ? 188.396 169.311 109.267 1.00 81.99  ? 1852 ASP A CB    1 
ATOM   4299  C  CG    . ASP A 1 1852 ? 188.381 169.016 110.754 1.00 83.07  ? 1852 ASP A CG    1 
ATOM   4300  O  OD1   . ASP A 1 1852 ? 189.394 168.500 111.270 1.00 80.26  ? 1852 ASP A OD1   1 
ATOM   4301  O  OD2   . ASP A 1 1852 ? 187.359 169.305 111.409 1.00 81.93  ? 1852 ASP A OD2   1 
ATOM   4302  N  N     . VAL A 1 1853 ? 187.512 165.970 108.998 1.00 72.69  ? 1853 VAL A N     1 
ATOM   4303  C  CA    . VAL A 1 1853 ? 186.391 165.035 109.007 1.00 65.61  ? 1853 VAL A CA    1 
ATOM   4304  C  C     . VAL A 1 1853 ? 185.246 165.568 109.856 1.00 63.53  ? 1853 VAL A C     1 
ATOM   4305  O  O     . VAL A 1 1853 ? 184.073 165.354 109.529 1.00 62.44  ? 1853 VAL A O     1 
ATOM   4306  C  CB    . VAL A 1 1853 ? 186.850 163.642 109.477 1.00 57.32  ? 1853 VAL A CB    1 
ATOM   4307  C  CG1   . VAL A 1 1853 ? 187.893 163.086 108.527 1.00 59.39  ? 1853 VAL A CG1   1 
ATOM   4308  C  CG2   . VAL A 1 1853 ? 187.397 163.700 110.893 1.00 55.86  ? 1853 VAL A CG2   1 
ATOM   4309  N  N     . LEU A 1 1854 ? 185.552 166.273 110.943 1.00 65.38  ? 1854 LEU A N     1 
ATOM   4310  C  CA    . LEU A 1 1854 ? 184.504 166.812 111.800 1.00 67.88  ? 1854 LEU A CA    1 
ATOM   4311  C  C     . LEU A 1 1854 ? 183.736 167.952 111.150 1.00 70.96  ? 1854 LEU A C     1 
ATOM   4312  O  O     . LEU A 1 1854 ? 182.714 168.373 111.700 1.00 67.28  ? 1854 LEU A O     1 
ATOM   4313  C  CB    . LEU A 1 1854 ? 185.102 167.275 113.130 1.00 64.23  ? 1854 LEU A CB    1 
ATOM   4314  C  CG    . LEU A 1 1854 ? 185.829 166.192 113.932 1.00 66.66  ? 1854 LEU A CG    1 
ATOM   4315  C  CD1   . LEU A 1 1854 ? 186.797 166.810 114.927 1.00 68.45  ? 1854 LEU A CD1   1 
ATOM   4316  C  CD2   . LEU A 1 1854 ? 184.834 165.287 114.640 1.00 55.02  ? 1854 LEU A CD2   1 
ATOM   4317  N  N     . GLN A 1 1855 ? 184.194 168.461 110.003 1.00 72.63  ? 1855 GLN A N     1 
ATOM   4318  C  CA    . GLN A 1 1855 ? 183.494 169.522 109.289 1.00 66.24  ? 1855 GLN A CA    1 
ATOM   4319  C  C     . GLN A 1 1855 ? 183.054 169.078 107.898 1.00 62.88  ? 1855 GLN A C     1 
ATOM   4320  O  O     . GLN A 1 1855 ? 182.856 169.921 107.019 1.00 65.58  ? 1855 GLN A O     1 
ATOM   4321  C  CB    . GLN A 1 1855 ? 184.367 170.775 109.190 1.00 67.89  ? 1855 GLN A CB    1 
ATOM   4322  C  CG    . GLN A 1 1855 ? 184.245 171.702 110.385 1.00 72.18  ? 1855 GLN A CG    1 
ATOM   4323  C  CD    . GLN A 1 1855 ? 185.561 172.350 110.753 1.00 76.72  ? 1855 GLN A CD    1 
ATOM   4324  O  OE1   . GLN A 1 1855 ? 186.336 172.746 109.884 1.00 81.30  ? 1855 GLN A OE1   1 
ATOM   4325  N  NE2   . GLN A 1 1855 ? 185.820 172.464 112.050 1.00 77.79  ? 1855 GLN A NE2   1 
ATOM   4326  N  N     . GLN A 1 1856 ? 182.897 167.774 107.680 1.00 59.61  ? 1856 GLN A N     1 
ATOM   4327  C  CA    . GLN A 1 1856 ? 182.493 167.261 106.378 1.00 53.86  ? 1856 GLN A CA    1 
ATOM   4328  C  C     . GLN A 1 1856 ? 180.984 167.176 106.214 1.00 47.71  ? 1856 GLN A C     1 
ATOM   4329  O  O     . GLN A 1 1856 ? 180.480 167.362 105.101 1.00 54.75  ? 1856 GLN A O     1 
ATOM   4330  C  CB    . GLN A 1 1856 ? 183.109 165.879 106.143 1.00 54.96  ? 1856 GLN A CB    1 
ATOM   4331  C  CG    . GLN A 1 1856 ? 184.568 165.920 105.728 1.00 67.67  ? 1856 GLN A CG    1 
ATOM   4332  C  CD    . GLN A 1 1856 ? 185.096 164.564 105.314 1.00 72.72  ? 1856 GLN A CD    1 
ATOM   4333  O  OE1   . GLN A 1 1856 ? 186.122 164.106 105.814 1.00 68.28  ? 1856 GLN A OE1   1 
ATOM   4334  N  NE2   . GLN A 1 1856 ? 184.393 163.911 104.398 1.00 75.57  ? 1856 GLN A NE2   1 
ATOM   4335  N  N     . LEU A 1 1857 ? 180.251 166.905 107.290 1.00 39.19  ? 1857 LEU A N     1 
ATOM   4336  C  CA    . LEU A 1 1857 ? 178.801 166.775 107.250 1.00 36.08  ? 1857 LEU A CA    1 
ATOM   4337  C  C     . LEU A 1 1857 ? 178.179 167.782 108.204 1.00 37.77  ? 1857 LEU A C     1 
ATOM   4338  O  O     . LEU A 1 1857 ? 178.591 167.878 109.364 1.00 43.89  ? 1857 LEU A O     1 
ATOM   4339  C  CB    . LEU A 1 1857 ? 178.367 165.355 107.619 1.00 37.67  ? 1857 LEU A CB    1 
ATOM   4340  C  CG    . LEU A 1 1857 ? 176.868 165.130 107.806 1.00 33.72  ? 1857 LEU A CG    1 
ATOM   4341  C  CD1   . LEU A 1 1857 ? 176.132 165.358 106.504 1.00 37.61  ? 1857 LEU A CD1   1 
ATOM   4342  C  CD2   . LEU A 1 1857 ? 176.607 163.735 108.327 1.00 27.50  ? 1857 LEU A CD2   1 
ATOM   4343  N  N     . SER A 1 1858 ? 177.189 168.527 107.718 1.00 36.30  ? 1858 SER A N     1 
ATOM   4344  C  CA    . SER A 1 1858 ? 176.498 169.541 108.504 1.00 30.12  ? 1858 SER A CA    1 
ATOM   4345  C  C     . SER A 1 1858 ? 175.039 169.137 108.665 1.00 27.81  ? 1858 SER A C     1 
ATOM   4346  O  O     . SER A 1 1858 ? 174.364 168.825 107.680 1.00 35.65  ? 1858 SER A O     1 
ATOM   4347  C  CB    . SER A 1 1858 ? 176.606 170.912 107.839 1.00 34.56  ? 1858 SER A CB    1 
ATOM   4348  O  OG    . SER A 1 1858 ? 175.935 171.900 108.598 1.00 41.70  ? 1858 SER A OG    1 
ATOM   4349  N  N     . ILE A 1 1859 ? 174.556 169.145 109.900 1.00 23.46  ? 1859 ILE A N     1 
ATOM   4350  C  CA    . ILE A 1 1859 ? 173.175 168.804 110.214 1.00 24.00  ? 1859 ILE A CA    1 
ATOM   4351  C  C     . ILE A 1 1859 ? 172.494 170.073 110.703 1.00 32.61  ? 1859 ILE A C     1 
ATOM   4352  O  O     . ILE A 1 1859 ? 172.820 170.587 111.777 1.00 40.70  ? 1859 ILE A O     1 
ATOM   4353  C  CB    . ILE A 1 1859 ? 173.093 167.690 111.262 1.00 20.74  ? 1859 ILE A CB    1 
ATOM   4354  C  CG1   . ILE A 1 1859 ? 173.980 166.518 110.849 1.00 24.07  ? 1859 ILE A CG1   1 
ATOM   4355  C  CG2   . ILE A 1 1859 ? 171.663 167.245 111.451 1.00 24.56  ? 1859 ILE A CG2   1 
ATOM   4356  C  CD1   . ILE A 1 1859 ? 174.088 165.457 111.895 1.00 27.63  ? 1859 ILE A CD1   1 
ATOM   4357  N  N     . GLN A 1 1860 ? 171.542 170.581 109.929 1.00 27.35  ? 1860 GLN A N     1 
ATOM   4358  C  CA    . GLN A 1 1860 ? 170.924 171.869 110.208 1.00 26.37  ? 1860 GLN A CA    1 
ATOM   4359  C  C     . GLN A 1 1860 ? 169.431 171.694 110.433 1.00 27.51  ? 1860 GLN A C     1 
ATOM   4360  O  O     . GLN A 1 1860 ? 168.740 171.096 109.606 1.00 36.26  ? 1860 GLN A O     1 
ATOM   4361  C  CB    . GLN A 1 1860 ? 171.182 172.851 109.065 1.00 27.84  ? 1860 GLN A CB    1 
ATOM   4362  C  CG    . GLN A 1 1860 ? 172.617 172.843 108.579 1.00 32.16  ? 1860 GLN A CG    1 
ATOM   4363  C  CD    . GLN A 1 1860 ? 172.878 173.876 107.508 1.00 44.11  ? 1860 GLN A CD    1 
ATOM   4364  O  OE1   . GLN A 1 1860 ? 171.988 174.637 107.135 1.00 48.23  ? 1860 GLN A OE1   1 
ATOM   4365  N  NE2   . GLN A 1 1860 ? 174.106 173.909 107.006 1.00 44.70  ? 1860 GLN A NE2   1 
ATOM   4366  N  N     . MET A 1 1861 ? 168.939 172.228 111.547 1.00 25.58  ? 1861 MET A N     1 
ATOM   4367  C  CA    . MET A 1 1861 ? 167.511 172.237 111.847 1.00 26.32  ? 1861 MET A CA    1 
ATOM   4368  C  C     . MET A 1 1861 ? 167.118 173.664 112.197 1.00 33.92  ? 1861 MET A C     1 
ATOM   4369  O  O     . MET A 1 1861 ? 167.589 174.209 113.201 1.00 35.96  ? 1861 MET A O     1 
ATOM   4370  C  CB    . MET A 1 1861 ? 167.171 171.283 112.989 1.00 27.64  ? 1861 MET A CB    1 
ATOM   4371  C  CG    . MET A 1 1861 ? 165.701 170.920 113.055 1.00 33.04  ? 1861 MET A CG    1 
ATOM   4372  S  SD    . MET A 1 1861 ? 165.347 169.612 114.236 1.00 51.91  ? 1861 MET A SD    1 
ATOM   4373  C  CE    . MET A 1 1861 ? 163.610 169.343 113.915 1.00 35.29  ? 1861 MET A CE    1 
ATOM   4374  N  N     . ALA A 1 1862 ? 166.265 174.262 111.369 1.00 35.81  ? 1862 ALA A N     1 
ATOM   4375  C  CA    . ALA A 1 1862 ? 165.795 175.644 111.540 1.00 33.48  ? 1862 ALA A CA    1 
ATOM   4376  C  C     . ALA A 1 1862 ? 167.030 176.541 111.592 1.00 34.66  ? 1862 ALA A C     1 
ATOM   4377  O  O     . ALA A 1 1862 ? 167.850 176.499 110.661 1.00 31.27  ? 1862 ALA A O     1 
ATOM   4378  C  CB    . ALA A 1 1862 ? 164.869 175.723 112.745 1.00 30.70  ? 1862 ALA A CB    1 
ATOM   4379  N  N     . ASN A 1 1863 ? 167.203 177.359 112.630 1.00 39.67  ? 1863 ASN A N     1 
ATOM   4380  C  CA    . ASN A 1 1863 ? 168.392 178.196 112.731 1.00 35.74  ? 1863 ASN A CA    1 
ATOM   4381  C  C     . ASN A 1 1863 ? 169.635 177.370 113.041 1.00 40.14  ? 1863 ASN A C     1 
ATOM   4382  O  O     . ASN A 1 1863 ? 170.724 177.667 112.538 1.00 45.12  ? 1863 ASN A O     1 
ATOM   4383  C  CB    . ASN A 1 1863 ? 168.180 179.266 113.801 1.00 35.97  ? 1863 ASN A CB    1 
ATOM   4384  C  CG    . ASN A 1 1863 ? 169.128 180.432 113.654 1.00 55.37  ? 1863 ASN A CG    1 
ATOM   4385  O  OD1   . ASN A 1 1863 ? 169.905 180.732 114.559 1.00 64.86  ? 1863 ASN A OD1   1 
ATOM   4386  N  ND2   . ASN A 1 1863 ? 169.072 181.098 112.507 1.00 61.31  ? 1863 ASN A ND2   1 
ATOM   4387  N  N     . ALA A 1 1864 ? 169.493 176.331 113.863 1.00 34.53  ? 1864 ALA A N     1 
ATOM   4388  C  CA    . ALA A 1 1864 ? 170.655 175.622 114.384 1.00 29.57  ? 1864 ALA A CA    1 
ATOM   4389  C  C     . ALA A 1 1864 ? 171.371 174.855 113.282 1.00 32.85  ? 1864 ALA A C     1 
ATOM   4390  O  O     . ALA A 1 1864 ? 170.745 174.330 112.360 1.00 35.08  ? 1864 ALA A O     1 
ATOM   4391  C  CB    . ALA A 1 1864 ? 170.231 174.665 115.496 1.00 28.56  ? 1864 ALA A CB    1 
ATOM   4392  N  N     . LYS A 1 1865 ? 172.698 174.780 113.392 1.00 38.57  ? 1865 LYS A N     1 
ATOM   4393  C  CA    . LYS A 1 1865 ? 173.526 174.046 112.433 1.00 36.36  ? 1865 LYS A CA    1 
ATOM   4394  C  C     . LYS A 1 1865 ? 174.707 173.436 113.185 1.00 38.81  ? 1865 LYS A C     1 
ATOM   4395  O  O     . LYS A 1 1865 ? 175.574 174.154 113.691 1.00 46.15  ? 1865 LYS A O     1 
ATOM   4396  C  CB    . LYS A 1 1865 ? 173.978 174.949 111.289 1.00 37.47  ? 1865 LYS A CB    1 
ATOM   4397  C  CG    . LYS A 1 1865 ? 174.646 176.247 111.711 1.00 48.30  ? 1865 LYS A CG    1 
ATOM   4398  C  CD    . LYS A 1 1865 ? 175.330 176.933 110.539 1.00 49.80  ? 1865 LYS A CD    1 
ATOM   4399  C  CE    . LYS A 1 1865 ? 174.439 176.968 109.309 1.00 46.38  ? 1865 LYS A CE    1 
ATOM   4400  N  NZ    . LYS A 1 1865 ? 173.121 177.603 109.589 1.00 49.46  ? 1865 LYS A NZ    1 
ATOM   4401  N  N     . PHE A 1 1866 ? 174.718 172.110 113.276 1.00 34.78  ? 1866 PHE A N     1 
ATOM   4402  C  CA    . PHE A 1 1866 ? 175.748 171.347 113.956 1.00 33.91  ? 1866 PHE A CA    1 
ATOM   4403  C  C     . PHE A 1 1866 ? 176.594 170.595 112.935 1.00 34.29  ? 1866 PHE A C     1 
ATOM   4404  O  O     . PHE A 1 1866 ? 176.287 170.549 111.743 1.00 38.18  ? 1866 PHE A O     1 
ATOM   4405  C  CB    . PHE A 1 1866 ? 175.108 170.373 114.943 1.00 30.39  ? 1866 PHE A CB    1 
ATOM   4406  C  CG    . PHE A 1 1866 ? 174.103 171.007 115.855 1.00 32.40  ? 1866 PHE A CG    1 
ATOM   4407  C  CD1   . PHE A 1 1866 ? 174.494 171.933 116.803 1.00 37.23  ? 1866 PHE A CD1   1 
ATOM   4408  C  CD2   . PHE A 1 1866 ? 172.762 170.700 115.742 1.00 29.18  ? 1866 PHE A CD2   1 
ATOM   4409  C  CE1   . PHE A 1 1866 ? 173.568 172.519 117.638 1.00 38.59  ? 1866 PHE A CE1   1 
ATOM   4410  C  CE2   . PHE A 1 1866 ? 171.834 171.285 116.571 1.00 33.28  ? 1866 PHE A CE2   1 
ATOM   4411  C  CZ    . PHE A 1 1866 ? 172.237 172.195 117.520 1.00 34.72  ? 1866 PHE A CZ    1 
ATOM   4412  N  N     . ASN A 1 1867 ? 177.664 169.973 113.417 1.00 35.17  ? 1867 ASN A N     1 
ATOM   4413  C  CA    . ASN A 1 1867 ? 178.481 169.080 112.613 1.00 36.40  ? 1867 ASN A CA    1 
ATOM   4414  C  C     . ASN A 1 1867 ? 178.378 167.669 113.171 1.00 38.35  ? 1867 ASN A C     1 
ATOM   4415  O  O     . ASN A 1 1867 ? 178.214 167.474 114.379 1.00 43.62  ? 1867 ASN A O     1 
ATOM   4416  C  CB    . ASN A 1 1867 ? 179.950 169.518 112.592 1.00 39.48  ? 1867 ASN A CB    1 
ATOM   4417  C  CG    . ASN A 1 1867 ? 180.153 170.859 111.921 1.00 47.29  ? 1867 ASN A CG    1 
ATOM   4418  O  OD1   . ASN A 1 1867 ? 180.556 171.829 112.560 1.00 56.63  ? 1867 ASN A OD1   1 
ATOM   4419  N  ND2   . ASN A 1 1867 ? 179.882 170.919 110.625 1.00 45.39  ? 1867 ASN A ND2   1 
ATOM   4420  N  N     . TYR A 1 1868 ? 178.470 166.682 112.285 1.00 29.95  ? 1868 TYR A N     1 
ATOM   4421  C  CA    . TYR A 1 1868 ? 178.475 165.290 112.711 1.00 28.59  ? 1868 TYR A CA    1 
ATOM   4422  C  C     . TYR A 1 1868 ? 179.789 164.994 113.422 1.00 36.31  ? 1868 TYR A C     1 
ATOM   4423  O  O     . TYR A 1 1868 ? 180.867 165.208 112.860 1.00 42.21  ? 1868 TYR A O     1 
ATOM   4424  C  CB    . TYR A 1 1868 ? 178.285 164.357 111.519 1.00 30.24  ? 1868 TYR A CB    1 
ATOM   4425  C  CG    . TYR A 1 1868 ? 177.720 163.006 111.890 1.00 28.45  ? 1868 TYR A CG    1 
ATOM   4426  C  CD1   . TYR A 1 1868 ? 176.400 162.870 112.283 1.00 27.87  ? 1868 TYR A CD1   1 
ATOM   4427  C  CD2   . TYR A 1 1868 ? 178.510 161.870 111.858 1.00 26.88  ? 1868 TYR A CD2   1 
ATOM   4428  C  CE1   . TYR A 1 1868 ? 175.881 161.642 112.623 1.00 26.62  ? 1868 TYR A CE1   1 
ATOM   4429  C  CE2   . TYR A 1 1868 ? 178.000 160.637 112.201 1.00 26.45  ? 1868 TYR A CE2   1 
ATOM   4430  C  CZ    . TYR A 1 1868 ? 176.685 160.530 112.584 1.00 29.59  ? 1868 TYR A CZ    1 
ATOM   4431  O  OH    . TYR A 1 1868 ? 176.166 159.304 112.926 1.00 36.98  ? 1868 TYR A OH    1 
ATOM   4432  N  N     . GLY A 1 1869 ? 179.700 164.503 114.657 1.00 32.22  ? 1869 GLY A N     1 
ATOM   4433  C  CA    . GLY A 1 1869 ? 180.894 164.175 115.409 1.00 28.78  ? 1869 GLY A CA    1 
ATOM   4434  C  C     . GLY A 1 1869 ? 181.595 162.913 114.970 1.00 27.41  ? 1869 GLY A C     1 
ATOM   4435  O  O     . GLY A 1 1869 ? 182.736 162.683 115.379 1.00 38.16  ? 1869 GLY A O     1 
ATOM   4436  N  N     . PHE A 1 1870 ? 180.938 162.100 114.144 1.00 30.35  ? 1870 PHE A N     1 
ATOM   4437  C  CA    . PHE A 1 1870 ? 181.512 160.865 113.611 1.00 26.85  ? 1870 PHE A CA    1 
ATOM   4438  C  C     . PHE A 1 1870 ? 181.988 159.943 114.728 1.00 25.54  ? 1870 PHE A C     1 
ATOM   4439  O  O     . PHE A 1 1870 ? 183.056 159.335 114.654 1.00 34.40  ? 1870 PHE A O     1 
ATOM   4440  C  CB    . PHE A 1 1870 ? 182.638 161.166 112.624 1.00 26.31  ? 1870 PHE A CB    1 
ATOM   4441  C  CG    . PHE A 1 1870 ? 182.148 161.543 111.261 1.00 30.16  ? 1870 PHE A CG    1 
ATOM   4442  C  CD1   . PHE A 1 1870 ? 181.404 160.651 110.514 1.00 30.84  ? 1870 PHE A CD1   1 
ATOM   4443  C  CD2   . PHE A 1 1870 ? 182.416 162.791 110.731 1.00 34.23  ? 1870 PHE A CD2   1 
ATOM   4444  C  CE1   . PHE A 1 1870 ? 180.944 160.993 109.263 1.00 32.35  ? 1870 PHE A CE1   1 
ATOM   4445  C  CE2   . PHE A 1 1870 ? 181.957 163.138 109.478 1.00 36.16  ? 1870 PHE A CE2   1 
ATOM   4446  C  CZ    . PHE A 1 1870 ? 181.221 162.238 108.744 1.00 33.84  ? 1870 PHE A CZ    1 
ATOM   4447  N  N     . GLU A 1 1871 ? 181.179 159.843 115.776 1.00 22.52  ? 1871 GLU A N     1 
ATOM   4448  C  CA    . GLU A 1 1871 ? 181.413 158.899 116.856 1.00 22.08  ? 1871 GLU A CA    1 
ATOM   4449  C  C     . GLU A 1 1871 ? 180.740 157.579 116.511 1.00 27.97  ? 1871 GLU A C     1 
ATOM   4450  O  O     . GLU A 1 1871 ? 179.568 157.560 116.125 1.00 37.04  ? 1871 GLU A O     1 
ATOM   4451  C  CB    . GLU A 1 1871 ? 180.868 159.446 118.174 1.00 25.02  ? 1871 GLU A CB    1 
ATOM   4452  C  CG    . GLU A 1 1871 ? 180.801 158.430 119.297 1.00 29.50  ? 1871 GLU A CG    1 
ATOM   4453  C  CD    . GLU A 1 1871 ? 182.040 158.439 120.165 1.00 42.32  ? 1871 GLU A CD    1 
ATOM   4454  O  OE1   . GLU A 1 1871 ? 182.923 159.290 119.936 1.00 43.53  ? 1871 GLU A OE1   1 
ATOM   4455  O  OE2   . GLU A 1 1871 ? 182.132 157.592 121.076 1.00 46.57  ? 1871 GLU A OE2   1 
ATOM   4456  N  N     . TYR A 1 1872 ? 181.481 156.480 116.639 1.00 30.28  ? 1872 TYR A N     1 
ATOM   4457  C  CA    . TYR A 1 1872 ? 180.916 155.163 116.369 1.00 28.10  ? 1872 TYR A CA    1 
ATOM   4458  C  C     . TYR A 1 1872 ? 179.889 154.833 117.442 1.00 28.27  ? 1872 TYR A C     1 
ATOM   4459  O  O     . TYR A 1 1872 ? 180.240 154.635 118.608 1.00 35.31  ? 1872 TYR A O     1 
ATOM   4460  C  CB    . TYR A 1 1872 ? 182.005 154.099 116.327 1.00 30.29  ? 1872 TYR A CB    1 
ATOM   4461  C  CG    . TYR A 1 1872 ? 181.494 152.753 115.870 1.00 37.60  ? 1872 TYR A CG    1 
ATOM   4462  C  CD1   . TYR A 1 1872 ? 180.671 152.647 114.759 1.00 41.19  ? 1872 TYR A CD1   1 
ATOM   4463  C  CD2   . TYR A 1 1872 ? 181.798 151.595 116.570 1.00 37.56  ? 1872 TYR A CD2   1 
ATOM   4464  C  CE1   . TYR A 1 1872 ? 180.193 151.424 114.342 1.00 39.10  ? 1872 TYR A CE1   1 
ATOM   4465  C  CE2   . TYR A 1 1872 ? 181.324 150.369 116.160 1.00 38.42  ? 1872 TYR A CE2   1 
ATOM   4466  C  CZ    . TYR A 1 1872 ? 180.521 150.290 115.047 1.00 40.30  ? 1872 TYR A CZ    1 
ATOM   4467  O  OH    . TYR A 1 1872 ? 180.043 149.070 114.635 1.00 54.79  ? 1872 TYR A OH    1 
ATOM   4468  N  N     . LEU A 1 1873 ? 178.621 154.775 117.052 1.00 26.96  ? 1873 LEU A N     1 
ATOM   4469  C  CA    . LEU A 1 1873 ? 177.535 154.492 117.975 1.00 30.76  ? 1873 LEU A CA    1 
ATOM   4470  C  C     . LEU A 1 1873 ? 177.131 153.027 117.975 1.00 34.20  ? 1873 LEU A C     1 
ATOM   4471  O  O     . LEU A 1 1873 ? 176.194 152.657 118.687 1.00 37.43  ? 1873 LEU A O     1 
ATOM   4472  C  CB    . LEU A 1 1873 ? 176.325 155.364 117.632 1.00 29.48  ? 1873 LEU A CB    1 
ATOM   4473  C  CG    . LEU A 1 1873 ? 176.654 156.844 117.446 1.00 26.87  ? 1873 LEU A CG    1 
ATOM   4474  C  CD1   . LEU A 1 1873 ? 175.530 157.555 116.732 1.00 25.69  ? 1873 LEU A CD1   1 
ATOM   4475  C  CD2   . LEU A 1 1873 ? 176.946 157.502 118.781 1.00 28.58  ? 1873 LEU A CD2   1 
ATOM   4476  N  N     . GLY A 1 1874 ? 177.818 152.185 117.207 1.00 38.54  ? 1874 GLY A N     1 
ATOM   4477  C  CA    . GLY A 1 1874 ? 177.409 150.802 117.106 1.00 38.17  ? 1874 GLY A CA    1 
ATOM   4478  C  C     . GLY A 1 1874 ? 176.081 150.681 116.381 1.00 41.42  ? 1874 GLY A C     1 
ATOM   4479  O  O     . GLY A 1 1874 ? 175.777 151.427 115.446 1.00 45.44  ? 1874 GLY A O     1 
ATOM   4480  N  N     . VAL A 1 1875 ? 175.278 149.718 116.822 1.00 46.45  ? 1875 VAL A N     1 
ATOM   4481  C  CA    . VAL A 1 1875 ? 173.934 149.540 116.288 1.00 48.55  ? 1875 VAL A CA    1 
ATOM   4482  C  C     . VAL A 1 1875 ? 172.938 150.000 117.342 1.00 49.32  ? 1875 VAL A C     1 
ATOM   4483  O  O     . VAL A 1 1875 ? 172.555 149.233 118.232 1.00 50.93  ? 1875 VAL A O     1 
ATOM   4484  C  CB    . VAL A 1 1875 ? 173.684 148.080 115.875 1.00 51.30  ? 1875 VAL A CB    1 
ATOM   4485  C  CG1   . VAL A 1 1875 ? 172.311 147.935 115.248 1.00 51.97  ? 1875 VAL A CG1   1 
ATOM   4486  C  CG2   . VAL A 1 1875 ? 174.764 147.617 114.919 1.00 47.63  ? 1875 VAL A CG2   1 
ATOM   4487  N  N     . GLN A 1 1876 ? 172.518 151.258 117.252 1.00 46.40  ? 1876 GLN A N     1 
ATOM   4488  C  CA    . GLN A 1 1876 ? 171.651 151.854 118.251 1.00 46.96  ? 1876 GLN A CA    1 
ATOM   4489  C  C     . GLN A 1 1876 ? 170.189 151.561 117.924 1.00 49.47  ? 1876 GLN A C     1 
ATOM   4490  O  O     . GLN A 1 1876 ? 169.856 150.998 116.879 1.00 54.84  ? 1876 GLN A O     1 
ATOM   4491  C  CB    . GLN A 1 1876 ? 171.910 153.357 118.345 1.00 46.74  ? 1876 GLN A CB    1 
ATOM   4492  C  CG    . GLN A 1 1876 ? 171.830 153.913 119.756 1.00 46.25  ? 1876 GLN A CG    1 
ATOM   4493  C  CD    . GLN A 1 1876 ? 172.926 153.382 120.656 1.00 44.54  ? 1876 GLN A CD    1 
ATOM   4494  O  OE1   . GLN A 1 1876 ? 174.111 153.531 120.364 1.00 37.75  ? 1876 GLN A OE1   1 
ATOM   4495  N  NE2   . GLN A 1 1876 ? 172.534 152.759 121.759 1.00 49.23  ? 1876 GLN A NE2   1 
ATOM   4496  N  N     . ASP A 1 1877 ? 169.301 151.949 118.834 1.00 43.96  ? 1877 ASP A N     1 
ATOM   4497  C  CA    . ASP A 1 1877 ? 167.864 151.744 118.675 1.00 50.55  ? 1877 ASP A CA    1 
ATOM   4498  C  C     . ASP A 1 1877 ? 167.255 153.044 118.164 1.00 50.55  ? 1877 ASP A C     1 
ATOM   4499  O  O     . ASP A 1 1877 ? 167.046 153.987 118.931 1.00 56.55  ? 1877 ASP A O     1 
ATOM   4500  C  CB    . ASP A 1 1877 ? 167.231 151.308 119.991 1.00 59.18  ? 1877 ASP A CB    1 
ATOM   4501  C  CG    . ASP A 1 1877 ? 165.716 151.283 119.929 1.00 70.11  ? 1877 ASP A CG    1 
ATOM   4502  O  OD1   . ASP A 1 1877 ? 165.167 150.526 119.102 1.00 69.30  ? 1877 ASP A OD1   1 
ATOM   4503  O  OD2   . ASP A 1 1877 ? 165.075 152.019 120.708 1.00 73.07  ? 1877 ASP A OD2   1 
ATOM   4504  N  N     . LYS A 1 1878 ? 166.972 153.092 116.865 1.00 46.50  ? 1878 LYS A N     1 
ATOM   4505  C  CA    . LYS A 1 1878 ? 166.359 154.274 116.279 1.00 45.96  ? 1878 LYS A CA    1 
ATOM   4506  C  C     . LYS A 1 1878 ? 164.941 154.458 116.800 1.00 45.98  ? 1878 LYS A C     1 
ATOM   4507  O  O     . LYS A 1 1878 ? 164.205 153.491 117.010 1.00 42.34  ? 1878 LYS A O     1 
ATOM   4508  C  CB    . LYS A 1 1878 ? 166.348 154.175 114.756 1.00 43.04  ? 1878 LYS A CB    1 
ATOM   4509  C  CG    . LYS A 1 1878 ? 167.541 154.829 114.085 1.00 45.24  ? 1878 LYS A CG    1 
ATOM   4510  C  CD    . LYS A 1 1878 ? 167.253 155.135 112.627 1.00 40.42  ? 1878 LYS A CD    1 
ATOM   4511  C  CE    . LYS A 1 1878 ? 165.995 155.969 112.466 1.00 36.22  ? 1878 LYS A CE    1 
ATOM   4512  N  NZ    . LYS A 1 1878 ? 166.117 157.297 113.125 1.00 40.76  ? 1878 LYS A NZ    1 
ATOM   4513  N  N     . LEU A 1 1879 ? 164.562 155.714 117.004 1.00 44.17  ? 1879 LEU A N     1 
ATOM   4514  C  CA    . LEU A 1 1879 ? 163.249 156.074 117.512 1.00 38.03  ? 1879 LEU A CA    1 
ATOM   4515  C  C     . LEU A 1 1879 ? 162.340 156.480 116.362 1.00 38.60  ? 1879 LEU A C     1 
ATOM   4516  O  O     . LEU A 1 1879 ? 162.790 157.087 115.386 1.00 40.51  ? 1879 LEU A O     1 
ATOM   4517  C  CB    . LEU A 1 1879 ? 163.355 157.219 118.520 1.00 30.12  ? 1879 LEU A CB    1 
ATOM   4518  C  CG    . LEU A 1 1879 ? 163.311 156.851 120.002 1.00 37.87  ? 1879 LEU A CG    1 
ATOM   4519  C  CD1   . LEU A 1 1879 ? 164.474 155.955 120.374 1.00 43.54  ? 1879 LEU A CD1   1 
ATOM   4520  C  CD2   . LEU A 1 1879 ? 163.318 158.110 120.846 1.00 35.42  ? 1879 LEU A CD2   1 
ATOM   4521  N  N     . VAL A 1 1880 ? 161.059 156.132 116.477 1.00 35.56  ? 1880 VAL A N     1 
ATOM   4522  C  CA    . VAL A 1 1880 ? 160.075 156.592 115.509 1.00 33.41  ? 1880 VAL A CA    1 
ATOM   4523  C  C     . VAL A 1 1880 ? 159.934 158.101 115.636 1.00 35.86  ? 1880 VAL A C     1 
ATOM   4524  O  O     . VAL A 1 1880 ? 159.697 158.629 116.730 1.00 36.17  ? 1880 VAL A O     1 
ATOM   4525  C  CB    . VAL A 1 1880 ? 158.732 155.881 115.723 1.00 33.15  ? 1880 VAL A CB    1 
ATOM   4526  C  CG1   . VAL A 1 1880 ? 157.666 156.492 114.836 1.00 33.43  ? 1880 VAL A CG1   1 
ATOM   4527  C  CG2   . VAL A 1 1880 ? 158.873 154.395 115.454 1.00 30.56  ? 1880 VAL A CG2   1 
ATOM   4528  N  N     . GLN A 1 1881 ? 160.077 158.805 114.515 1.00 39.59  ? 1881 GLN A N     1 
ATOM   4529  C  CA    . GLN A 1 1881 ? 160.188 160.261 114.526 1.00 38.29  ? 1881 GLN A CA    1 
ATOM   4530  C  C     . GLN A 1 1881 ? 158.779 160.850 114.574 1.00 41.74  ? 1881 GLN A C     1 
ATOM   4531  O  O     . GLN A 1 1881 ? 158.232 161.340 113.584 1.00 44.31  ? 1881 GLN A O     1 
ATOM   4532  C  CB    . GLN A 1 1881 ? 160.968 160.739 113.310 1.00 41.61  ? 1881 GLN A CB    1 
ATOM   4533  C  CG    . GLN A 1 1881 ? 161.226 162.230 113.268 1.00 43.55  ? 1881 GLN A CG    1 
ATOM   4534  C  CD    . GLN A 1 1881 ? 162.077 162.694 114.428 1.00 50.06  ? 1881 GLN A CD    1 
ATOM   4535  O  OE1   . GLN A 1 1881 ? 161.584 163.301 115.376 1.00 56.64  ? 1881 GLN A OE1   1 
ATOM   4536  N  NE2   . GLN A 1 1881 ? 163.367 162.403 114.359 1.00 49.87  ? 1881 GLN A NE2   1 
ATOM   4537  N  N     . THR A 1 1882 ? 158.179 160.784 115.761 1.00 35.40  ? 1882 THR A N     1 
ATOM   4538  C  CA    . THR A 1 1882 ? 156.831 161.284 115.960 1.00 33.06  ? 1882 THR A CA    1 
ATOM   4539  C  C     . THR A 1 1882 ? 156.830 162.811 116.009 1.00 38.44  ? 1882 THR A C     1 
ATOM   4540  O  O     . THR A 1 1882 ? 157.882 163.435 116.161 1.00 42.01  ? 1882 THR A O     1 
ATOM   4541  C  CB    . THR A 1 1882 ? 156.238 160.715 117.247 1.00 33.91  ? 1882 THR A CB    1 
ATOM   4542  O  OG1   . THR A 1 1882 ? 157.102 161.006 118.350 1.00 32.06  ? 1882 THR A OG1   1 
ATOM   4543  C  CG2   . THR A 1 1882 ? 156.075 159.217 117.132 1.00 36.43  ? 1882 THR A CG2   1 
ATOM   4544  N  N     . PRO A 1 1883 ? 155.659 163.439 115.856 1.00 36.42  ? 1883 PRO A N     1 
ATOM   4545  C  CA    . PRO A 1 1883 ? 155.595 164.900 116.020 1.00 31.47  ? 1883 PRO A CA    1 
ATOM   4546  C  C     . PRO A 1 1883 ? 156.083 165.382 117.374 1.00 31.03  ? 1883 PRO A C     1 
ATOM   4547  O  O     . PRO A 1 1883 ? 156.650 166.478 117.458 1.00 38.40  ? 1883 PRO A O     1 
ATOM   4548  C  CB    . PRO A 1 1883 ? 154.107 165.217 115.807 1.00 35.96  ? 1883 PRO A CB    1 
ATOM   4549  C  CG    . PRO A 1 1883 ? 153.401 163.896 115.808 1.00 34.40  ? 1883 PRO A CG    1 
ATOM   4550  C  CD    . PRO A 1 1883 ? 154.395 162.900 115.332 1.00 37.34  ? 1883 PRO A CD    1 
ATOM   4551  N  N     . LEU A 1 1884 ? 155.881 164.605 118.440 1.00 29.41  ? 1884 LEU A N     1 
ATOM   4552  C  CA    . LEU A 1 1884 ? 156.454 164.975 119.731 1.00 27.58  ? 1884 LEU A CA    1 
ATOM   4553  C  C     . LEU A 1 1884 ? 157.975 164.955 119.683 1.00 29.48  ? 1884 LEU A C     1 
ATOM   4554  O  O     . LEU A 1 1884 ? 158.631 165.862 120.206 1.00 34.34  ? 1884 LEU A O     1 
ATOM   4555  C  CB    . LEU A 1 1884 ? 155.943 164.045 120.828 1.00 32.10  ? 1884 LEU A CB    1 
ATOM   4556  C  CG    . LEU A 1 1884 ? 156.446 164.381 122.233 1.00 30.57  ? 1884 LEU A CG    1 
ATOM   4557  C  CD1   . LEU A 1 1884 ? 155.985 165.763 122.648 1.00 32.24  ? 1884 LEU A CD1   1 
ATOM   4558  C  CD2   . LEU A 1 1884 ? 155.988 163.342 123.236 1.00 33.95  ? 1884 LEU A CD2   1 
ATOM   4559  N  N     . THR A 1 1885 ? 158.558 163.933 119.054 1.00 29.52  ? 1885 THR A N     1 
ATOM   4560  C  CA    . THR A 1 1885 ? 160.010 163.900 118.920 1.00 29.10  ? 1885 THR A CA    1 
ATOM   4561  C  C     . THR A 1 1885 ? 160.509 164.963 117.953 1.00 30.20  ? 1885 THR A C     1 
ATOM   4562  O  O     . THR A 1 1885 ? 161.619 165.471 118.122 1.00 37.11  ? 1885 THR A O     1 
ATOM   4563  C  CB    . THR A 1 1885 ? 160.480 162.517 118.475 1.00 30.52  ? 1885 THR A CB    1 
ATOM   4564  O  OG1   . THR A 1 1885 ? 159.927 162.211 117.191 1.00 39.97  ? 1885 THR A OG1   1 
ATOM   4565  C  CG2   . THR A 1 1885 ? 160.057 161.461 119.480 1.00 34.10  ? 1885 THR A CG2   1 
ATOM   4566  N  N     . ASP A 1 1886 ? 159.715 165.317 116.942 1.00 29.21  ? 1886 ASP A N     1 
ATOM   4567  C  CA    . ASP A 1 1886 ? 160.091 166.430 116.075 1.00 30.24  ? 1886 ASP A CA    1 
ATOM   4568  C  C     . ASP A 1 1886 ? 160.129 167.739 116.853 1.00 30.79  ? 1886 ASP A C     1 
ATOM   4569  O  O     . ASP A 1 1886 ? 161.056 168.543 116.693 1.00 31.67  ? 1886 ASP A O     1 
ATOM   4570  C  CB    . ASP A 1 1886 ? 159.121 166.528 114.901 1.00 42.27  ? 1886 ASP A CB    1 
ATOM   4571  C  CG    . ASP A 1 1886 ? 159.627 165.811 113.669 1.00 52.30  ? 1886 ASP A CG    1 
ATOM   4572  O  OD1   . ASP A 1 1886 ? 160.828 165.475 113.631 1.00 53.05  ? 1886 ASP A OD1   1 
ATOM   4573  O  OD2   . ASP A 1 1886 ? 158.824 165.581 112.740 1.00 51.88  ? 1886 ASP A OD2   1 
ATOM   4574  N  N     . ARG A 1 1887 ? 159.129 167.965 117.709 1.00 30.02  ? 1887 ARG A N     1 
ATOM   4575  C  CA    . ARG A 1 1887 ? 159.137 169.143 118.569 1.00 25.40  ? 1887 ARG A CA    1 
ATOM   4576  C  C     . ARG A 1 1887 ? 160.316 169.114 119.529 1.00 28.34  ? 1887 ARG A C     1 
ATOM   4577  O  O     . ARG A 1 1887 ? 160.924 170.153 119.806 1.00 33.49  ? 1887 ARG A O     1 
ATOM   4578  C  CB    . ARG A 1 1887 ? 157.826 169.239 119.345 1.00 28.79  ? 1887 ARG A CB    1 
ATOM   4579  C  CG    . ARG A 1 1887 ? 157.640 170.562 120.057 1.00 34.91  ? 1887 ARG A CG    1 
ATOM   4580  C  CD    . ARG A 1 1887 ? 156.177 170.907 120.224 1.00 35.42  ? 1887 ARG A CD    1 
ATOM   4581  N  NE    . ARG A 1 1887 ? 155.919 171.557 121.502 1.00 42.90  ? 1887 ARG A NE    1 
ATOM   4582  C  CZ    . ARG A 1 1887 ? 154.710 171.833 121.970 1.00 47.00  ? 1887 ARG A CZ    1 
ATOM   4583  N  NH1   . ARG A 1 1887 ? 153.620 171.537 121.284 1.00 47.37  ? 1887 ARG A NH1   1 
ATOM   4584  N  NH2   . ARG A 1 1887 ? 154.593 172.422 123.156 1.00 46.93  ? 1887 ARG A NH2   1 
ATOM   4585  N  N     . CYS A 1 1888 ? 160.641 167.935 120.062 1.00 30.73  ? 1888 CYS A N     1 
ATOM   4586  C  CA    . CYS A 1 1888 ? 161.789 167.814 120.953 1.00 27.73  ? 1888 CYS A CA    1 
ATOM   4587  C  C     . CYS A 1 1888 ? 163.083 168.158 120.230 1.00 26.05  ? 1888 CYS A C     1 
ATOM   4588  O  O     . CYS A 1 1888 ? 163.926 168.891 120.756 1.00 30.54  ? 1888 CYS A O     1 
ATOM   4589  C  CB    . CYS A 1 1888 ? 161.855 166.402 121.535 1.00 31.40  ? 1888 CYS A CB    1 
ATOM   4590  S  SG    . CYS A 1 1888 ? 163.320 166.080 122.540 1.00 63.90  ? 1888 CYS A SG    1 
ATOM   4591  N  N     . TYR A 1 1889 ? 163.253 167.639 119.014 1.00 24.42  ? 1889 TYR A N     1 
ATOM   4592  C  CA    . TYR A 1 1889 ? 164.436 167.957 118.225 1.00 24.36  ? 1889 TYR A CA    1 
ATOM   4593  C  C     . TYR A 1 1889 ? 164.527 169.452 117.970 1.00 24.68  ? 1889 TYR A C     1 
ATOM   4594  O  O     . TYR A 1 1889 ? 165.584 170.060 118.156 1.00 28.99  ? 1889 TYR A O     1 
ATOM   4595  C  CB    . TYR A 1 1889 ? 164.406 167.190 116.903 1.00 26.96  ? 1889 TYR A CB    1 
ATOM   4596  C  CG    . TYR A 1 1889 ? 164.896 165.763 116.986 1.00 30.38  ? 1889 TYR A CG    1 
ATOM   4597  C  CD1   . TYR A 1 1889 ? 164.663 164.989 118.113 1.00 31.81  ? 1889 TYR A CD1   1 
ATOM   4598  C  CD2   . TYR A 1 1889 ? 165.571 165.182 115.924 1.00 30.84  ? 1889 TYR A CD2   1 
ATOM   4599  C  CE1   . TYR A 1 1889 ? 165.101 163.686 118.185 1.00 29.44  ? 1889 TYR A CE1   1 
ATOM   4600  C  CE2   . TYR A 1 1889 ? 166.012 163.880 115.987 1.00 31.12  ? 1889 TYR A CE2   1 
ATOM   4601  C  CZ    . TYR A 1 1889 ? 165.775 163.137 117.119 1.00 31.79  ? 1889 TYR A CZ    1 
ATOM   4602  O  OH    . TYR A 1 1889 ? 166.213 161.837 117.185 1.00 38.39  ? 1889 TYR A OH    1 
ATOM   4603  N  N     . LEU A 1 1890 ? 163.415 170.069 117.562 1.00 25.69  ? 1890 LEU A N     1 
ATOM   4604  C  CA    . LEU A 1 1890 ? 163.429 171.500 117.276 1.00 26.57  ? 1890 LEU A CA    1 
ATOM   4605  C  C     . LEU A 1 1890 ? 163.779 172.307 118.520 1.00 27.22  ? 1890 LEU A C     1 
ATOM   4606  O  O     . LEU A 1 1890 ? 164.640 173.193 118.476 1.00 34.77  ? 1890 LEU A O     1 
ATOM   4607  C  CB    . LEU A 1 1890 ? 162.076 171.933 116.713 1.00 24.68  ? 1890 LEU A CB    1 
ATOM   4608  C  CG    . LEU A 1 1890 ? 161.945 173.403 116.316 1.00 21.28  ? 1890 LEU A CG    1 
ATOM   4609  C  CD1   . LEU A 1 1890 ? 162.639 173.669 114.994 1.00 22.83  ? 1890 LEU A CD1   1 
ATOM   4610  C  CD2   . LEU A 1 1890 ? 160.483 173.807 116.244 1.00 28.65  ? 1890 LEU A CD2   1 
ATOM   4611  N  N     . THR A 1 1891 ? 163.137 171.998 119.648 1.00 24.93  ? 1891 THR A N     1 
ATOM   4612  C  CA    . THR A 1 1891 ? 163.366 172.763 120.868 1.00 24.54  ? 1891 THR A CA    1 
ATOM   4613  C  C     . THR A 1 1891 ? 164.794 172.599 121.371 1.00 28.33  ? 1891 THR A C     1 
ATOM   4614  O  O     . THR A 1 1891 ? 165.440 173.581 121.753 1.00 33.47  ? 1891 THR A O     1 
ATOM   4615  C  CB    . THR A 1 1891 ? 162.371 172.341 121.946 1.00 27.64  ? 1891 THR A CB    1 
ATOM   4616  O  OG1   . THR A 1 1891 ? 161.038 172.456 121.437 1.00 31.53  ? 1891 THR A OG1   1 
ATOM   4617  C  CG2   . THR A 1 1891 ? 162.512 173.222 123.172 1.00 29.26  ? 1891 THR A CG2   1 
ATOM   4618  N  N     . MET A 1 1892 ? 165.309 171.366 121.378 1.00 27.76  ? 1892 MET A N     1 
ATOM   4619  C  CA    . MET A 1 1892 ? 166.655 171.143 121.889 1.00 21.96  ? 1892 MET A CA    1 
ATOM   4620  C  C     . MET A 1 1892 ? 167.712 171.723 120.960 1.00 22.82  ? 1892 MET A C     1 
ATOM   4621  O  O     . MET A 1 1892 ? 168.722 172.254 121.429 1.00 33.68  ? 1892 MET A O     1 
ATOM   4622  C  CB    . MET A 1 1892 ? 166.895 169.655 122.128 1.00 19.72  ? 1892 MET A CB    1 
ATOM   4623  C  CG    . MET A 1 1892 ? 165.923 169.020 123.103 1.00 24.81  ? 1892 MET A CG    1 
ATOM   4624  S  SD    . MET A 1 1892 ? 165.824 169.950 124.641 1.00 52.28  ? 1892 MET A SD    1 
ATOM   4625  C  CE    . MET A 1 1892 ? 164.056 170.009 124.897 1.00 35.15  ? 1892 MET A CE    1 
ATOM   4626  N  N     . THR A 1 1893 ? 167.506 171.649 119.644 1.00 19.42  ? 1893 THR A N     1 
ATOM   4627  C  CA    . THR A 1 1893 ? 168.451 172.287 118.734 1.00 21.88  ? 1893 THR A CA    1 
ATOM   4628  C  C     . THR A 1 1893 ? 168.418 173.803 118.879 1.00 25.78  ? 1893 THR A C     1 
ATOM   4629  O  O     . THR A 1 1893 ? 169.462 174.460 118.800 1.00 33.45  ? 1893 THR A O     1 
ATOM   4630  C  CB    . THR A 1 1893 ? 168.165 171.876 117.291 1.00 25.99  ? 1893 THR A CB    1 
ATOM   4631  O  OG1   . THR A 1 1893 ? 166.786 172.112 116.988 1.00 33.40  ? 1893 THR A OG1   1 
ATOM   4632  C  CG2   . THR A 1 1893 ? 168.487 170.407 117.080 1.00 23.64  ? 1893 THR A CG2   1 
ATOM   4633  N  N     . GLN A 1 1894 ? 167.232 174.379 119.093 1.00 25.16  ? 1894 GLN A N     1 
ATOM   4634  C  CA    . GLN A 1 1894 ? 167.145 175.818 119.314 1.00 25.91  ? 1894 GLN A CA    1 
ATOM   4635  C  C     . GLN A 1 1894 ? 167.848 176.221 120.603 1.00 28.26  ? 1894 GLN A C     1 
ATOM   4636  O  O     . GLN A 1 1894 ? 168.528 177.252 120.651 1.00 34.05  ? 1894 GLN A O     1 
ATOM   4637  C  CB    . GLN A 1 1894 ? 165.682 176.259 119.338 1.00 24.49  ? 1894 GLN A CB    1 
ATOM   4638  C  CG    . GLN A 1 1894 ? 165.035 176.334 117.968 1.00 25.25  ? 1894 GLN A CG    1 
ATOM   4639  C  CD    . GLN A 1 1894 ? 165.769 177.264 117.028 1.00 31.57  ? 1894 GLN A CD    1 
ATOM   4640  O  OE1   . GLN A 1 1894 ? 166.278 176.841 115.992 1.00 35.64  ? 1894 GLN A OE1   1 
ATOM   4641  N  NE2   . GLN A 1 1894 ? 165.827 178.540 117.382 1.00 31.26  ? 1894 GLN A NE2   1 
ATOM   4642  N  N     . ALA A 1 1895 ? 167.685 175.426 121.663 1.00 25.42  ? 1895 ALA A N     1 
ATOM   4643  C  CA    . ALA A 1 1895 ? 168.381 175.707 122.914 1.00 23.58  ? 1895 ALA A CA    1 
ATOM   4644  C  C     . ALA A 1 1895 ? 169.890 175.581 122.749 1.00 24.40  ? 1895 ALA A C     1 
ATOM   4645  O  O     . ALA A 1 1895 ? 170.651 176.397 123.279 1.00 32.89  ? 1895 ALA A O     1 
ATOM   4646  C  CB    . ALA A 1 1895 ? 167.883 174.771 124.013 1.00 21.99  ? 1895 ALA A CB    1 
ATOM   4647  N  N     . LEU A 1 1896 ? 170.339 174.561 122.017 1.00 24.97  ? 1896 LEU A N     1 
ATOM   4648  C  CA    . LEU A 1 1896 ? 171.767 174.372 121.786 1.00 23.51  ? 1896 LEU A CA    1 
ATOM   4649  C  C     . LEU A 1 1896 ? 172.360 175.521 120.984 1.00 28.81  ? 1896 LEU A C     1 
ATOM   4650  O  O     . LEU A 1 1896 ? 173.470 175.981 121.273 1.00 39.23  ? 1896 LEU A O     1 
ATOM   4651  C  CB    . LEU A 1 1896 ? 171.999 173.046 121.068 1.00 24.76  ? 1896 LEU A CB    1 
ATOM   4652  C  CG    . LEU A 1 1896 ? 172.407 171.846 121.916 1.00 26.05  ? 1896 LEU A CG    1 
ATOM   4653  C  CD1   . LEU A 1 1896 ? 171.429 171.620 123.044 1.00 19.46  ? 1896 LEU A CD1   1 
ATOM   4654  C  CD2   . LEU A 1 1896 ? 172.461 170.635 121.025 1.00 25.03  ? 1896 LEU A CD2   1 
ATOM   4655  N  N     . GLU A 1 1897 ? 171.643 175.989 119.960 1.00 30.22  ? 1897 GLU A N     1 
ATOM   4656  C  CA    . GLU A 1 1897 ? 172.114 177.143 119.203 1.00 31.72  ? 1897 GLU A CA    1 
ATOM   4657  C  C     . GLU A 1 1897 ? 172.117 178.402 120.058 1.00 31.95  ? 1897 GLU A C     1 
ATOM   4658  O  O     . GLU A 1 1897 ? 172.975 179.273 119.875 1.00 35.38  ? 1897 GLU A O     1 
ATOM   4659  C  CB    . GLU A 1 1897 ? 171.252 177.344 117.958 1.00 33.54  ? 1897 GLU A CB    1 
ATOM   4660  C  CG    . GLU A 1 1897 ? 171.790 178.381 116.983 1.00 40.08  ? 1897 GLU A CG    1 
ATOM   4661  C  CD    . GLU A 1 1897 ? 172.955 177.869 116.154 1.00 55.42  ? 1897 GLU A CD    1 
ATOM   4662  O  OE1   . GLU A 1 1897 ? 173.336 176.690 116.313 1.00 55.24  ? 1897 GLU A OE1   1 
ATOM   4663  O  OE2   . GLU A 1 1897 ? 173.489 178.647 115.335 1.00 55.55  ? 1897 GLU A OE2   1 
ATOM   4664  N  N     . ALA A 1 1898 ? 171.179 178.512 120.992 1.00 30.02  ? 1898 ALA A N     1 
ATOM   4665  C  CA    . ALA A 1 1898 ? 171.132 179.620 121.932 1.00 28.28  ? 1898 ALA A CA    1 
ATOM   4666  C  C     . ALA A 1 1898 ? 172.031 179.399 123.138 1.00 35.60  ? 1898 ALA A C     1 
ATOM   4667  O  O     . ALA A 1 1898 ? 171.968 180.183 124.088 1.00 46.66  ? 1898 ALA A O     1 
ATOM   4668  C  CB    . ALA A 1 1898 ? 169.694 179.856 122.400 1.00 24.65  ? 1898 ALA A CB    1 
ATOM   4669  N  N     . ARG A 1 1899 ? 172.844 178.345 123.126 1.00 32.83  ? 1899 ARG A N     1 
ATOM   4670  C  CA    . ARG A 1 1899 ? 173.785 177.998 124.186 1.00 30.24  ? 1899 ARG A CA    1 
ATOM   4671  C  C     . ARG A 1 1899 ? 173.099 177.683 125.506 1.00 31.55  ? 1899 ARG A C     1 
ATOM   4672  O  O     . ARG A 1 1899 ? 173.743 177.723 126.559 1.00 38.30  ? 1899 ARG A O     1 
ATOM   4673  C  CB    . ARG A 1 1899 ? 174.832 179.097 124.388 1.00 35.62  ? 1899 ARG A CB    1 
ATOM   4674  C  CG    . ARG A 1 1899 ? 175.875 179.143 123.292 1.00 40.05  ? 1899 ARG A CG    1 
ATOM   4675  C  CD    . ARG A 1 1899 ? 176.506 177.781 123.093 1.00 37.01  ? 1899 ARG A CD    1 
ATOM   4676  N  NE    . ARG A 1 1899 ? 177.469 177.782 122.000 1.00 46.82  ? 1899 ARG A NE    1 
ATOM   4677  C  CZ    . ARG A 1 1899 ? 178.222 176.743 121.668 1.00 57.25  ? 1899 ARG A CZ    1 
ATOM   4678  N  NH1   . ARG A 1 1899 ? 178.155 175.601 122.331 1.00 51.83  ? 1899 ARG A NH1   1 
ATOM   4679  N  NH2   . ARG A 1 1899 ? 179.063 176.853 120.644 1.00 59.13  ? 1899 ARG A NH2   1 
ATOM   4680  N  N     . LEU A 1 1900 ? 171.811 177.368 125.479 1.00 31.84  ? 1900 LEU A N     1 
ATOM   4681  C  CA    . LEU A 1 1900 ? 171.073 176.959 126.662 1.00 30.46  ? 1900 LEU A CA    1 
ATOM   4682  C  C     . LEU A 1 1900 ? 170.925 175.444 126.677 1.00 30.28  ? 1900 LEU A C     1 
ATOM   4683  O  O     . LEU A 1 1900 ? 170.852 174.800 125.629 1.00 40.43  ? 1900 LEU A O     1 
ATOM   4684  C  CB    . LEU A 1 1900 ? 169.692 177.615 126.698 1.00 30.87  ? 1900 LEU A CB    1 
ATOM   4685  C  CG    . LEU A 1 1900 ? 169.661 179.140 126.763 1.00 34.57  ? 1900 LEU A CG    1 
ATOM   4686  C  CD1   . LEU A 1 1900 ? 168.271 179.653 126.445 1.00 34.75  ? 1900 LEU A CD1   1 
ATOM   4687  C  CD2   . LEU A 1 1900 ? 170.113 179.626 128.125 1.00 42.25  ? 1900 LEU A CD2   1 
ATOM   4688  N  N     . GLY A 1 1901 ? 170.886 174.878 127.875 1.00 25.49  ? 1901 GLY A N     1 
ATOM   4689  C  CA    . GLY A 1 1901 ? 170.658 173.457 128.004 1.00 24.39  ? 1901 GLY A CA    1 
ATOM   4690  C  C     . GLY A 1 1901 ? 169.217 173.099 127.713 1.00 30.28  ? 1901 GLY A C     1 
ATOM   4691  O  O     . GLY A 1 1901 ? 168.350 173.952 127.546 1.00 41.90  ? 1901 GLY A O     1 
ATOM   4692  N  N     . GLY A 1 1902 ? 168.955 171.801 127.653 1.00 24.19  ? 1902 GLY A N     1 
ATOM   4693  C  CA    . GLY A 1 1902 ? 167.618 171.285 127.399 1.00 23.25  ? 1902 GLY A CA    1 
ATOM   4694  C  C     . GLY A 1 1902 ? 167.063 170.618 128.644 1.00 25.52  ? 1902 GLY A C     1 
ATOM   4695  O  O     . GLY A 1 1902 ? 167.809 170.009 129.414 1.00 32.02  ? 1902 GLY A O     1 
ATOM   4696  N  N     . SER A 1 1903 ? 165.754 170.741 128.840 1.00 25.61  ? 1903 SER A N     1 
ATOM   4697  C  CA    . SER A 1 1903 ? 165.063 170.124 129.970 1.00 25.54  ? 1903 SER A CA    1 
ATOM   4698  C  C     . SER A 1 1903 ? 163.717 169.583 129.510 1.00 32.53  ? 1903 SER A C     1 
ATOM   4699  O  O     . SER A 1 1903 ? 162.688 170.256 129.625 1.00 42.50  ? 1903 SER A O     1 
ATOM   4700  C  CB    . SER A 1 1903 ? 164.891 171.119 131.116 1.00 28.27  ? 1903 SER A CB    1 
ATOM   4701  O  OG    . SER A 1 1903 ? 164.225 170.519 132.212 1.00 31.54  ? 1903 SER A OG    1 
ATOM   4702  N  N     . PRO A 1 1904 ? 163.694 168.379 128.940 1.00 28.63  ? 1904 PRO A N     1 
ATOM   4703  C  CA    . PRO A 1 1904 ? 162.408 167.720 128.690 1.00 24.98  ? 1904 PRO A CA    1 
ATOM   4704  C  C     . PRO A 1 1904 ? 161.824 167.193 129.991 1.00 27.20  ? 1904 PRO A C     1 
ATOM   4705  O  O     . PRO A 1 1904 ? 162.479 166.454 130.727 1.00 31.85  ? 1904 PRO A O     1 
ATOM   4706  C  CB    . PRO A 1 1904 ? 162.769 166.586 127.726 1.00 24.80  ? 1904 PRO A CB    1 
ATOM   4707  C  CG    . PRO A 1 1904 ? 164.212 166.342 127.955 1.00 26.35  ? 1904 PRO A CG    1 
ATOM   4708  C  CD    . PRO A 1 1904 ? 164.812 167.664 128.304 1.00 29.05  ? 1904 PRO A CD    1 
ATOM   4709  N  N     . PHE A 1 1905 ? 160.586 167.584 130.276 1.00 27.81  ? 1905 PHE A N     1 
ATOM   4710  C  CA    . PHE A 1 1905 ? 159.903 167.179 131.493 1.00 29.85  ? 1905 PHE A CA    1 
ATOM   4711  C  C     . PHE A 1 1905 ? 158.575 166.528 131.143 1.00 34.01  ? 1905 PHE A C     1 
ATOM   4712  O  O     . PHE A 1 1905 ? 157.957 166.845 130.124 1.00 38.71  ? 1905 PHE A O     1 
ATOM   4713  C  CB    . PHE A 1 1905 ? 159.686 168.370 132.445 1.00 31.12  ? 1905 PHE A CB    1 
ATOM   4714  C  CG    . PHE A 1 1905 ? 158.712 169.398 131.938 1.00 32.79  ? 1905 PHE A CG    1 
ATOM   4715  C  CD1   . PHE A 1 1905 ? 157.354 169.269 132.174 1.00 31.64  ? 1905 PHE A CD1   1 
ATOM   4716  C  CD2   . PHE A 1 1905 ? 159.157 170.500 131.233 1.00 33.37  ? 1905 PHE A CD2   1 
ATOM   4717  C  CE1   . PHE A 1 1905 ? 156.464 170.212 131.711 1.00 30.81  ? 1905 PHE A CE1   1 
ATOM   4718  C  CE2   . PHE A 1 1905 ? 158.270 171.446 130.770 1.00 32.67  ? 1905 PHE A CE2   1 
ATOM   4719  C  CZ    . PHE A 1 1905 ? 156.923 171.301 131.009 1.00 30.62  ? 1905 PHE A CZ    1 
ATOM   4720  N  N     . GLY A 1 1906 ? 158.146 165.607 131.998 1.00 36.05  ? 1906 GLY A N     1 
ATOM   4721  C  CA    . GLY A 1 1906 ? 156.897 164.915 131.811 1.00 36.50  ? 1906 GLY A CA    1 
ATOM   4722  C  C     . GLY A 1 1906 ? 156.831 163.651 132.640 1.00 42.29  ? 1906 GLY A C     1 
ATOM   4723  O  O     . GLY A 1 1906 ? 157.737 163.345 133.420 1.00 47.47  ? 1906 GLY A O     1 
ATOM   4724  N  N     . PRO A 1 1907 ? 155.748 162.895 132.493 1.00 42.92  ? 1907 PRO A N     1 
ATOM   4725  C  CA    . PRO A 1 1907 ? 155.641 161.615 133.198 1.00 40.14  ? 1907 PRO A CA    1 
ATOM   4726  C  C     . PRO A 1 1907 ? 156.684 160.626 132.702 1.00 43.62  ? 1907 PRO A C     1 
ATOM   4727  O  O     . PRO A 1 1907 ? 157.188 160.718 131.581 1.00 47.16  ? 1907 PRO A O     1 
ATOM   4728  C  CB    . PRO A 1 1907 ? 154.223 161.139 132.864 1.00 42.16  ? 1907 PRO A CB    1 
ATOM   4729  C  CG    . PRO A 1 1907 ? 153.498 162.367 132.414 1.00 41.29  ? 1907 PRO A CG    1 
ATOM   4730  C  CD    . PRO A 1 1907 ? 154.527 163.209 131.737 1.00 42.39  ? 1907 PRO A CD    1 
ATOM   4731  N  N     . ALA A 1 1908 ? 157.019 159.677 133.571 1.00 44.21  ? 1908 ALA A N     1 
ATOM   4732  C  CA    . ALA A 1 1908 ? 157.997 158.661 133.213 1.00 44.37  ? 1908 ALA A CA    1 
ATOM   4733  C  C     . ALA A 1 1908 ? 157.471 157.791 132.080 1.00 40.04  ? 1908 ALA A C     1 
ATOM   4734  O  O     . ALA A 1 1908 ? 156.287 157.446 132.037 1.00 44.57  ? 1908 ALA A O     1 
ATOM   4735  C  CB    . ALA A 1 1908 ? 158.336 157.798 134.428 1.00 48.68  ? 1908 ALA A CB    1 
ATOM   4736  N  N     . GLY A 1 1909 ? 158.359 157.440 131.155 1.00 38.24  ? 1909 GLY A N     1 
ATOM   4737  C  CA    . GLY A 1 1909 ? 157.994 156.620 130.021 1.00 35.03  ? 1909 GLY A CA    1 
ATOM   4738  C  C     . GLY A 1 1909 ? 157.509 157.370 128.803 1.00 35.67  ? 1909 GLY A C     1 
ATOM   4739  O  O     . GLY A 1 1909 ? 156.947 156.744 127.898 1.00 41.07  ? 1909 GLY A O     1 
ATOM   4740  N  N     . THR A 1 1910 ? 157.706 158.685 128.746 1.00 34.82  ? 1910 THR A N     1 
ATOM   4741  C  CA    . THR A 1 1910 ? 157.273 159.491 127.613 1.00 30.81  ? 1910 THR A CA    1 
ATOM   4742  C  C     . THR A 1 1910 ? 158.362 159.677 126.567 1.00 34.51  ? 1910 THR A C     1 
ATOM   4743  O  O     . THR A 1 1910 ? 158.156 160.424 125.606 1.00 39.52  ? 1910 THR A O     1 
ATOM   4744  C  CB    . THR A 1 1910 ? 156.786 160.862 128.089 1.00 33.24  ? 1910 THR A CB    1 
ATOM   4745  O  OG1   . THR A 1 1910 ? 157.777 161.458 128.932 1.00 38.04  ? 1910 THR A OG1   1 
ATOM   4746  C  CG2   . THR A 1 1910 ? 155.488 160.722 128.863 1.00 40.63  ? 1910 THR A CG2   1 
ATOM   4747  N  N     . GLY A 1 1911 ? 159.508 159.024 126.726 1.00 37.66  ? 1911 GLY A N     1 
ATOM   4748  C  CA    . GLY A 1 1911 ? 160.565 159.131 125.743 1.00 29.49  ? 1911 GLY A CA    1 
ATOM   4749  C  C     . GLY A 1 1911 ? 161.425 160.365 125.858 1.00 27.44  ? 1911 GLY A C     1 
ATOM   4750  O  O     . GLY A 1 1911 ? 161.935 160.845 124.845 1.00 31.96  ? 1911 GLY A O     1 
ATOM   4751  N  N     . LYS A 1 1912 ? 161.605 160.897 127.067 1.00 28.65  ? 1912 LYS A N     1 
ATOM   4752  C  CA    . LYS A 1 1912 ? 162.396 162.113 127.232 1.00 25.93  ? 1912 LYS A CA    1 
ATOM   4753  C  C     . LYS A 1 1912 ? 163.882 161.832 127.049 1.00 28.28  ? 1912 LYS A C     1 
ATOM   4754  O  O     . LYS A 1 1912 ? 164.527 162.376 126.143 1.00 31.73  ? 1912 LYS A O     1 
ATOM   4755  C  CB    . LYS A 1 1912 ? 162.133 162.723 128.608 1.00 23.74  ? 1912 LYS A CB    1 
ATOM   4756  C  CG    . LYS A 1 1912 ? 160.741 163.281 128.795 1.00 28.62  ? 1912 LYS A CG    1 
ATOM   4757  C  CD    . LYS A 1 1912 ? 160.397 163.384 130.265 1.00 26.70  ? 1912 LYS A CD    1 
ATOM   4758  C  CE    . LYS A 1 1912 ? 160.526 162.041 130.953 1.00 30.84  ? 1912 LYS A CE    1 
ATOM   4759  N  NZ    . LYS A 1 1912 ? 160.128 162.109 132.383 1.00 40.04  ? 1912 LYS A NZ    1 
ATOM   4760  N  N     . THR A 1 1913 ? 164.447 160.983 127.909 1.00 30.16  ? 1913 THR A N     1 
ATOM   4761  C  CA    . THR A 1 1913 ? 165.867 160.677 127.802 1.00 26.51  ? 1913 THR A CA    1 
ATOM   4762  C  C     . THR A 1 1913 ? 166.175 159.896 126.532 1.00 27.50  ? 1913 THR A C     1 
ATOM   4763  O  O     . THR A 1 1913 ? 167.260 160.052 125.963 1.00 33.00  ? 1913 THR A O     1 
ATOM   4764  C  CB    . THR A 1 1913 ? 166.347 159.921 129.044 1.00 29.70  ? 1913 THR A CB    1 
ATOM   4765  O  OG1   . THR A 1 1913 ? 167.775 159.807 129.014 1.00 32.09  ? 1913 THR A OG1   1 
ATOM   4766  C  CG2   . THR A 1 1913 ? 165.735 158.539 129.122 1.00 34.14  ? 1913 THR A CG2   1 
ATOM   4767  N  N     . GLU A 1 1914 ? 165.233 159.079 126.057 1.00 31.79  ? 1914 GLU A N     1 
ATOM   4768  C  CA    . GLU A 1 1914 ? 165.430 158.406 124.779 1.00 31.90  ? 1914 GLU A CA    1 
ATOM   4769  C  C     . GLU A 1 1914 ? 165.485 159.405 123.632 1.00 31.22  ? 1914 GLU A C     1 
ATOM   4770  O  O     . GLU A 1 1914 ? 166.301 159.256 122.720 1.00 35.36  ? 1914 GLU A O     1 
ATOM   4771  C  CB    . GLU A 1 1914 ? 164.330 157.375 124.541 1.00 35.45  ? 1914 GLU A CB    1 
ATOM   4772  C  CG    . GLU A 1 1914 ? 164.452 156.137 125.410 1.00 47.06  ? 1914 GLU A CG    1 
ATOM   4773  C  CD    . GLU A 1 1914 ? 165.693 155.322 125.102 1.00 61.86  ? 1914 GLU A CD    1 
ATOM   4774  O  OE1   . GLU A 1 1914 ? 166.118 155.301 123.928 1.00 68.03  ? 1914 GLU A OE1   1 
ATOM   4775  O  OE2   . GLU A 1 1914 ? 166.243 154.702 126.035 1.00 61.30  ? 1914 GLU A OE2   1 
ATOM   4776  N  N     . SER A 1 1915 ? 164.630 160.431 123.658 1.00 29.03  ? 1915 SER A N     1 
ATOM   4777  C  CA    . SER A 1 1915 ? 164.680 161.452 122.615 1.00 23.89  ? 1915 SER A CA    1 
ATOM   4778  C  C     . SER A 1 1915 ? 165.968 162.258 122.686 1.00 26.50  ? 1915 SER A C     1 
ATOM   4779  O  O     . SER A 1 1915 ? 166.548 162.599 121.650 1.00 31.37  ? 1915 SER A O     1 
ATOM   4780  C  CB    . SER A 1 1915 ? 163.471 162.378 122.714 1.00 27.05  ? 1915 SER A CB    1 
ATOM   4781  O  OG    . SER A 1 1915 ? 162.271 161.673 122.455 1.00 36.80  ? 1915 SER A OG    1 
ATOM   4782  N  N     . VAL A 1 1916 ? 166.431 162.576 123.897 1.00 27.19  ? 1916 VAL A N     1 
ATOM   4783  C  CA    . VAL A 1 1916 ? 167.691 163.304 124.037 1.00 22.25  ? 1916 VAL A CA    1 
ATOM   4784  C  C     . VAL A 1 1916 ? 168.846 162.476 123.487 1.00 23.77  ? 1916 VAL A C     1 
ATOM   4785  O  O     . VAL A 1 1916 ? 169.695 162.974 122.736 1.00 26.19  ? 1916 VAL A O     1 
ATOM   4786  C  CB    . VAL A 1 1916 ? 167.925 163.690 125.507 1.00 18.53  ? 1916 VAL A CB    1 
ATOM   4787  C  CG1   . VAL A 1 1916 ? 169.337 164.204 125.696 1.00 21.55  ? 1916 VAL A CG1   1 
ATOM   4788  C  CG2   . VAL A 1 1916 ? 166.913 164.726 125.947 1.00 21.90  ? 1916 VAL A CG2   1 
ATOM   4789  N  N     . LYS A 1 1917 ? 168.885 161.191 123.846 1.00 23.63  ? 1917 LYS A N     1 
ATOM   4790  C  CA    . LYS A 1 1917 ? 169.939 160.307 123.362 1.00 23.25  ? 1917 LYS A CA    1 
ATOM   4791  C  C     . LYS A 1 1917 ? 169.857 160.122 121.851 1.00 24.47  ? 1917 LYS A C     1 
ATOM   4792  O  O     . LYS A 1 1917 ? 170.885 160.058 121.170 1.00 32.18  ? 1917 LYS A O     1 
ATOM   4793  C  CB    . LYS A 1 1917 ? 169.845 158.967 124.091 1.00 25.63  ? 1917 LYS A CB    1 
ATOM   4794  C  CG    . LYS A 1 1917 ? 170.651 157.850 123.478 1.00 33.71  ? 1917 LYS A CG    1 
ATOM   4795  C  CD    . LYS A 1 1917 ? 170.473 156.557 124.251 1.00 38.37  ? 1917 LYS A CD    1 
ATOM   4796  C  CE    . LYS A 1 1917 ? 171.134 156.631 125.609 1.00 38.61  ? 1917 LYS A CE    1 
ATOM   4797  N  NZ    . LYS A 1 1917 ? 172.583 156.943 125.494 1.00 40.34  ? 1917 LYS A NZ    1 
ATOM   4798  N  N     . ALA A 1 1918 ? 168.641 160.040 121.308 1.00 21.73  ? 1918 ALA A N     1 
ATOM   4799  C  CA    . ALA A 1 1918 ? 168.470 159.889 119.868 1.00 21.43  ? 1918 ALA A CA    1 
ATOM   4800  C  C     . ALA A 1 1918 ? 168.925 161.131 119.119 1.00 21.90  ? 1918 ALA A C     1 
ATOM   4801  O  O     . ALA A 1 1918 ? 169.528 161.026 118.047 1.00 27.87  ? 1918 ALA A O     1 
ATOM   4802  C  CB    . ALA A 1 1918 ? 167.010 159.576 119.545 1.00 25.43  ? 1918 ALA A CB    1 
ATOM   4803  N  N     . LEU A 1 1919 ? 168.627 162.317 119.652 1.00 22.44  ? 1919 LEU A N     1 
ATOM   4804  C  CA    . LEU A 1 1919 ? 169.119 163.543 119.033 1.00 20.87  ? 1919 LEU A CA    1 
ATOM   4805  C  C     . LEU A 1 1919 ? 170.637 163.615 119.101 1.00 23.08  ? 1919 LEU A C     1 
ATOM   4806  O  O     . LEU A 1 1919 ? 171.290 164.035 118.140 1.00 27.15  ? 1919 LEU A O     1 
ATOM   4807  C  CB    . LEU A 1 1919 ? 168.495 164.765 119.703 1.00 20.07  ? 1919 LEU A CB    1 
ATOM   4808  C  CG    . LEU A 1 1919 ? 169.125 166.115 119.358 1.00 17.54  ? 1919 LEU A CG    1 
ATOM   4809  C  CD1   . LEU A 1 1919 ? 169.011 166.412 117.873 1.00 21.11  ? 1919 LEU A CD1   1 
ATOM   4810  C  CD2   . LEU A 1 1919 ? 168.487 167.214 120.170 1.00 17.37  ? 1919 LEU A CD2   1 
ATOM   4811  N  N     . GLY A 1 1920 ? 171.217 163.211 120.232 1.00 22.16  ? 1920 GLY A N     1 
ATOM   4812  C  CA    . GLY A 1 1920 ? 172.666 163.183 120.334 1.00 18.41  ? 1920 GLY A CA    1 
ATOM   4813  C  C     . GLY A 1 1920 ? 173.303 162.234 119.340 1.00 22.70  ? 1920 GLY A C     1 
ATOM   4814  O  O     . GLY A 1 1920 ? 174.331 162.548 118.738 1.00 31.84  ? 1920 GLY A O     1 
ATOM   4815  N  N     . HIS A 1 1921 ? 172.700 161.059 119.152 1.00 22.64  ? 1921 HIS A N     1 
ATOM   4816  C  CA    . HIS A 1 1921 ? 173.236 160.096 118.198 1.00 22.71  ? 1921 HIS A CA    1 
ATOM   4817  C  C     . HIS A 1 1921 ? 173.018 160.543 116.759 1.00 24.37  ? 1921 HIS A C     1 
ATOM   4818  O  O     . HIS A 1 1921 ? 173.821 160.212 115.881 1.00 28.22  ? 1921 HIS A O     1 
ATOM   4819  C  CB    . HIS A 1 1921 ? 172.606 158.725 118.428 1.00 20.92  ? 1921 HIS A CB    1 
ATOM   4820  C  CG    . HIS A 1 1921 ? 172.974 158.108 119.740 1.00 27.18  ? 1921 HIS A CG    1 
ATOM   4821  N  ND1   . HIS A 1 1921 ? 174.196 158.314 120.341 1.00 29.43  ? 1921 HIS A ND1   1 
ATOM   4822  C  CD2   . HIS A 1 1921 ? 172.290 157.273 120.556 1.00 28.24  ? 1921 HIS A CD2   1 
ATOM   4823  C  CE1   . HIS A 1 1921 ? 174.245 157.643 121.478 1.00 30.05  ? 1921 HIS A CE1   1 
ATOM   4824  N  NE2   . HIS A 1 1921 ? 173.102 157.001 121.630 1.00 28.71  ? 1921 HIS A NE2   1 
ATOM   4825  N  N     . GLN A 1 1922 ? 171.938 161.281 116.495 1.00 26.87  ? 1922 GLN A N     1 
ATOM   4826  C  CA    . GLN A 1 1922 ? 171.710 161.812 115.156 1.00 25.42  ? 1922 GLN A CA    1 
ATOM   4827  C  C     . GLN A 1 1922 ? 172.801 162.795 114.764 1.00 26.27  ? 1922 GLN A C     1 
ATOM   4828  O  O     . GLN A 1 1922 ? 173.180 162.881 113.591 1.00 29.23  ? 1922 GLN A O     1 
ATOM   4829  C  CB    . GLN A 1 1922 ? 170.338 162.479 115.084 1.00 24.09  ? 1922 GLN A CB    1 
ATOM   4830  C  CG    . GLN A 1 1922 ? 169.997 163.023 113.715 1.00 28.54  ? 1922 GLN A CG    1 
ATOM   4831  C  CD    . GLN A 1 1922 ? 169.720 161.932 112.708 1.00 39.39  ? 1922 GLN A CD    1 
ATOM   4832  O  OE1   . GLN A 1 1922 ? 168.649 161.326 112.711 1.00 49.79  ? 1922 GLN A OE1   1 
ATOM   4833  N  NE2   . GLN A 1 1922 ? 170.688 161.670 111.839 1.00 33.37  ? 1922 GLN A NE2   1 
ATOM   4834  N  N     . LEU A 1 1923 ? 173.317 163.545 115.732 1.00 25.80  ? 1923 LEU A N     1 
ATOM   4835  C  CA    . LEU A 1 1923 ? 174.394 164.495 115.500 1.00 25.20  ? 1923 LEU A CA    1 
ATOM   4836  C  C     . LEU A 1 1923 ? 175.770 163.850 115.574 1.00 29.20  ? 1923 LEU A C     1 
ATOM   4837  O  O     . LEU A 1 1923 ? 176.775 164.564 115.500 1.00 32.89  ? 1923 LEU A O     1 
ATOM   4838  C  CB    . LEU A 1 1923 ? 174.304 165.639 116.512 1.00 24.05  ? 1923 LEU A CB    1 
ATOM   4839  C  CG    . LEU A 1 1923 ? 173.001 166.438 116.510 1.00 20.01  ? 1923 LEU A CG    1 
ATOM   4840  C  CD1   . LEU A 1 1923 ? 173.086 167.589 117.489 1.00 17.83  ? 1923 LEU A CD1   1 
ATOM   4841  C  CD2   . LEU A 1 1923 ? 172.678 166.942 115.117 1.00 25.22  ? 1923 LEU A CD2   1 
ATOM   4842  N  N     . GLY A 1 1924 ? 175.837 162.531 115.718 1.00 26.54  ? 1924 GLY A N     1 
ATOM   4843  C  CA    . GLY A 1 1924 ? 177.105 161.836 115.850 1.00 24.42  ? 1924 GLY A CA    1 
ATOM   4844  C  C     . GLY A 1 1924 ? 177.833 162.154 117.134 1.00 28.35  ? 1924 GLY A C     1 
ATOM   4845  O  O     . GLY A 1 1924 ? 179.063 162.275 117.132 1.00 34.57  ? 1924 GLY A O     1 
ATOM   4846  N  N     . ARG A 1 1925 ? 177.104 162.287 118.233 1.00 25.00  ? 1925 ARG A N     1 
ATOM   4847  C  CA    . ARG A 1 1925 ? 177.673 162.679 119.509 1.00 24.98  ? 1925 ARG A CA    1 
ATOM   4848  C  C     . ARG A 1 1925 ? 177.599 161.523 120.496 1.00 30.67  ? 1925 ARG A C     1 
ATOM   4849  O  O     . ARG A 1 1925 ? 176.805 160.592 120.341 1.00 37.90  ? 1925 ARG A O     1 
ATOM   4850  C  CB    . ARG A 1 1925 ? 176.947 163.902 120.076 1.00 25.25  ? 1925 ARG A CB    1 
ATOM   4851  C  CG    . ARG A 1 1925 ? 177.862 164.886 120.767 1.00 34.58  ? 1925 ARG A CG    1 
ATOM   4852  C  CD    . ARG A 1 1925 ? 178.732 165.630 119.775 1.00 35.31  ? 1925 ARG A CD    1 
ATOM   4853  N  NE    . ARG A 1 1925 ? 177.938 166.434 118.856 1.00 34.81  ? 1925 ARG A NE    1 
ATOM   4854  C  CZ    . ARG A 1 1925 ? 178.444 167.152 117.864 1.00 44.26  ? 1925 ARG A CZ    1 
ATOM   4855  N  NH1   . ARG A 1 1925 ? 179.745 167.187 117.630 1.00 44.12  ? 1925 ARG A NH1   1 
ATOM   4856  N  NH2   . ARG A 1 1925 ? 177.624 167.855 117.088 1.00 38.64  ? 1925 ARG A NH2   1 
ATOM   4857  N  N     . PHE A 1 1926 ? 178.446 161.593 121.516 1.00 26.79  ? 1926 PHE A N     1 
ATOM   4858  C  CA    . PHE A 1 1926 ? 178.516 160.577 122.558 1.00 25.44  ? 1926 PHE A CA    1 
ATOM   4859  C  C     . PHE A 1 1926 ? 177.708 161.082 123.747 1.00 26.23  ? 1926 PHE A C     1 
ATOM   4860  O  O     . PHE A 1 1926 ? 178.092 162.057 124.398 1.00 33.18  ? 1926 PHE A O     1 
ATOM   4861  C  CB    . PHE A 1 1926 ? 179.972 160.291 122.922 1.00 27.10  ? 1926 PHE A CB    1 
ATOM   4862  C  CG    . PHE A 1 1926 ? 180.154 159.406 124.126 1.00 31.82  ? 1926 PHE A CG    1 
ATOM   4863  C  CD1   . PHE A 1 1926 ? 179.290 158.357 124.380 1.00 32.87  ? 1926 PHE A CD1   1 
ATOM   4864  C  CD2   . PHE A 1 1926 ? 181.231 159.594 124.973 1.00 34.02  ? 1926 PHE A CD2   1 
ATOM   4865  C  CE1   . PHE A 1 1926 ? 179.473 157.540 125.477 1.00 31.24  ? 1926 PHE A CE1   1 
ATOM   4866  C  CE2   . PHE A 1 1926 ? 181.420 158.777 126.066 1.00 33.49  ? 1926 PHE A CE2   1 
ATOM   4867  C  CZ    . PHE A 1 1926 ? 180.539 157.751 126.319 1.00 33.05  ? 1926 PHE A CZ    1 
ATOM   4868  N  N     . VAL A 1 1927 ? 176.582 160.428 124.018 1.00 25.97  ? 1927 VAL A N     1 
ATOM   4869  C  CA    . VAL A 1 1927 ? 175.644 160.851 125.050 1.00 24.92  ? 1927 VAL A CA    1 
ATOM   4870  C  C     . VAL A 1 1927 ? 175.789 159.923 126.244 1.00 28.43  ? 1927 VAL A C     1 
ATOM   4871  O  O     . VAL A 1 1927 ? 175.712 158.697 126.099 1.00 33.40  ? 1927 VAL A O     1 
ATOM   4872  C  CB    . VAL A 1 1927 ? 174.196 160.849 124.530 1.00 22.57  ? 1927 VAL A CB    1 
ATOM   4873  C  CG1   . VAL A 1 1927 ? 173.245 161.319 125.615 1.00 22.77  ? 1927 VAL A CG1   1 
ATOM   4874  C  CG2   . VAL A 1 1927 ? 174.076 161.716 123.298 1.00 25.02  ? 1927 VAL A CG2   1 
ATOM   4875  N  N     . LEU A 1 1928 ? 175.999 160.504 127.420 1.00 25.62  ? 1928 LEU A N     1 
ATOM   4876  C  CA    . LEU A 1 1928 ? 176.079 159.758 128.667 1.00 25.32  ? 1928 LEU A CA    1 
ATOM   4877  C  C     . LEU A 1 1928 ? 174.826 160.043 129.478 1.00 25.88  ? 1928 LEU A C     1 
ATOM   4878  O  O     . LEU A 1 1928 ? 174.553 161.199 129.815 1.00 30.16  ? 1928 LEU A O     1 
ATOM   4879  C  CB    . LEU A 1 1928 ? 177.325 160.137 129.466 1.00 26.32  ? 1928 LEU A CB    1 
ATOM   4880  C  CG    . LEU A 1 1928 ? 178.683 159.687 128.932 1.00 32.21  ? 1928 LEU A CG    1 
ATOM   4881  C  CD1   . LEU A 1 1928 ? 179.205 160.672 127.906 1.00 30.31  ? 1928 LEU A CD1   1 
ATOM   4882  C  CD2   . LEU A 1 1928 ? 179.665 159.522 130.073 1.00 35.59  ? 1928 LEU A CD2   1 
ATOM   4883  N  N     . VAL A 1 1929 ? 174.072 158.996 129.790 1.00 25.04  ? 1929 VAL A N     1 
ATOM   4884  C  CA    . VAL A 1 1929 ? 172.850 159.127 130.572 1.00 28.01  ? 1929 VAL A CA    1 
ATOM   4885  C  C     . VAL A 1 1929 ? 173.188 158.789 132.018 1.00 35.15  ? 1929 VAL A C     1 
ATOM   4886  O  O     . VAL A 1 1929 ? 173.619 157.674 132.322 1.00 45.75  ? 1929 VAL A O     1 
ATOM   4887  C  CB    . VAL A 1 1929 ? 171.736 158.225 130.032 1.00 25.88  ? 1929 VAL A CB    1 
ATOM   4888  C  CG1   . VAL A 1 1929 ? 170.544 158.242 130.970 1.00 28.97  ? 1929 VAL A CG1   1 
ATOM   4889  C  CG2   . VAL A 1 1929 ? 171.327 158.673 128.643 1.00 27.75  ? 1929 VAL A CG2   1 
ATOM   4890  N  N     . PHE A 1 1930 ? 173.000 159.756 132.911 1.00 31.22  ? 1930 PHE A N     1 
ATOM   4891  C  CA    . PHE A 1 1930 ? 173.277 159.582 134.330 1.00 34.90  ? 1930 PHE A CA    1 
ATOM   4892  C  C     . PHE A 1 1930 ? 171.964 159.293 135.045 1.00 42.98  ? 1930 PHE A C     1 
ATOM   4893  O  O     . PHE A 1 1930 ? 171.147 160.196 135.245 1.00 47.37  ? 1930 PHE A O     1 
ATOM   4894  C  CB    . PHE A 1 1930 ? 173.954 160.820 134.911 1.00 32.30  ? 1930 PHE A CB    1 
ATOM   4895  C  CG    . PHE A 1 1930 ? 175.067 161.355 134.063 1.00 30.96  ? 1930 PHE A CG    1 
ATOM   4896  C  CD1   . PHE A 1 1930 ? 176.176 160.580 133.786 1.00 32.79  ? 1930 PHE A CD1   1 
ATOM   4897  C  CD2   . PHE A 1 1930 ? 175.007 162.635 133.546 1.00 36.14  ? 1930 PHE A CD2   1 
ATOM   4898  C  CE1   . PHE A 1 1930 ? 177.201 161.070 133.006 1.00 33.93  ? 1930 PHE A CE1   1 
ATOM   4899  C  CE2   . PHE A 1 1930 ? 176.029 163.130 132.768 1.00 36.75  ? 1930 PHE A CE2   1 
ATOM   4900  C  CZ    . PHE A 1 1930 ? 177.127 162.347 132.497 1.00 33.24  ? 1930 PHE A CZ    1 
ATOM   4901  N  N     . ASN A 1 1931 ? 171.762 158.035 135.424 1.00 45.98  ? 1931 ASN A N     1 
ATOM   4902  C  CA    . ASN A 1 1931 ? 170.582 157.666 136.192 1.00 55.97  ? 1931 ASN A CA    1 
ATOM   4903  C  C     . ASN A 1 1931 ? 170.665 158.299 137.574 1.00 64.76  ? 1931 ASN A C     1 
ATOM   4904  O  O     . ASN A 1 1931 ? 171.594 158.020 138.338 1.00 68.63  ? 1931 ASN A O     1 
ATOM   4905  C  CB    . ASN A 1 1931 ? 170.472 156.148 136.296 1.00 63.71  ? 1931 ASN A CB    1 
ATOM   4906  C  CG    . ASN A 1 1931 ? 170.126 155.498 134.972 1.00 67.46  ? 1931 ASN A CG    1 
ATOM   4907  O  OD1   . ASN A 1 1931 ? 169.284 155.995 134.225 1.00 70.00  ? 1931 ASN A OD1   1 
ATOM   4908  N  ND2   . ASN A 1 1931 ? 170.780 154.383 134.670 1.00 70.58  ? 1931 ASN A ND2   1 
ATOM   4909  N  N     . CYS A 1 1932 ? 169.691 159.151 137.898 1.00 58.43  ? 1932 CYS A N     1 
ATOM   4910  C  CA    . CYS A 1 1932 ? 169.697 159.904 139.146 1.00 60.22  ? 1932 CYS A CA    1 
ATOM   4911  C  C     . CYS A 1 1932 ? 168.954 159.190 140.266 1.00 71.81  ? 1932 CYS A C     1 
ATOM   4912  O  O     . CYS A 1 1932 ? 168.408 159.845 141.163 1.00 69.05  ? 1932 CYS A O     1 
ATOM   4913  C  CB    . CYS A 1 1932 ? 169.115 161.299 138.920 1.00 45.91  ? 1932 CYS A CB    1 
ATOM   4914  S  SG    . CYS A 1 1932 ? 170.043 162.309 137.750 1.00 41.72  ? 1932 CYS A SG    1 
ATOM   4915  N  N     . ASP A 1 1933 ? 168.917 157.862 140.236 1.00 75.72  ? 1933 ASP A N     1 
ATOM   4916  C  CA    . ASP A 1 1933 ? 168.326 157.080 141.312 1.00 79.04  ? 1933 ASP A CA    1 
ATOM   4917  C  C     . ASP A 1 1933 ? 169.327 156.967 142.462 1.00 88.54  ? 1933 ASP A C     1 
ATOM   4918  O  O     . ASP A 1 1933 ? 170.334 157.678 142.514 1.00 85.32  ? 1933 ASP A O     1 
ATOM   4919  C  CB    . ASP A 1 1933 ? 167.862 155.724 140.781 1.00 79.97  ? 1933 ASP A CB    1 
ATOM   4920  C  CG    . ASP A 1 1933 ? 168.981 154.928 140.126 1.00 88.12  ? 1933 ASP A CG    1 
ATOM   4921  O  OD1   . ASP A 1 1933 ? 170.109 154.900 140.659 1.00 89.18  ? 1933 ASP A OD1   1 
ATOM   4922  O  OD2   . ASP A 1 1933 ? 168.726 154.324 139.063 1.00 91.57  ? 1933 ASP A OD2   1 
ATOM   4923  N  N     . GLU A 1 1934 ? 169.049 156.071 143.413 1.00 91.60  ? 1934 GLU A N     1 
ATOM   4924  C  CA    . GLU A 1 1934 ? 169.937 155.910 144.561 1.00 90.88  ? 1934 GLU A CA    1 
ATOM   4925  C  C     . GLU A 1 1934 ? 171.323 155.432 144.144 1.00 87.20  ? 1934 GLU A C     1 
ATOM   4926  O  O     . GLU A 1 1934 ? 172.306 155.698 144.844 1.00 80.74  ? 1934 GLU A O     1 
ATOM   4927  C  CB    . GLU A 1 1934 ? 169.323 154.940 145.573 1.00 93.70  ? 1934 GLU A CB    1 
ATOM   4928  C  CG    . GLU A 1 1934 ? 169.064 153.540 145.033 1.00 94.23  ? 1934 GLU A CG    1 
ATOM   4929  C  CD    . GLU A 1 1934 ? 167.753 153.434 144.277 1.00 99.22  ? 1934 GLU A CD    1 
ATOM   4930  O  OE1   . GLU A 1 1934 ? 167.007 154.435 144.235 1.00 96.83  ? 1934 GLU A OE1   1 
ATOM   4931  O  OE2   . GLU A 1 1934 ? 167.469 152.351 143.724 1.00 101.77 ? 1934 GLU A OE2   1 
ATOM   4932  N  N     . THR A 1 1935 ? 171.425 154.732 143.015 1.00 87.44  ? 1935 THR A N     1 
ATOM   4933  C  CA    . THR A 1 1935 ? 172.712 154.248 142.515 1.00 88.74  ? 1935 THR A CA    1 
ATOM   4934  C  C     . THR A 1 1935 ? 173.321 155.295 141.580 1.00 89.71  ? 1935 THR A C     1 
ATOM   4935  O  O     . THR A 1 1935 ? 173.475 155.099 140.374 1.00 91.44  ? 1935 THR A O     1 
ATOM   4936  C  CB    . THR A 1 1935 ? 172.541 152.905 141.817 1.00 93.94  ? 1935 THR A CB    1 
ATOM   4937  O  OG1   . THR A 1 1935 ? 171.729 153.074 140.649 1.00 91.32  ? 1935 THR A OG1   1 
ATOM   4938  C  CG2   . THR A 1 1935 ? 171.873 151.905 142.748 1.00 89.52  ? 1935 THR A CG2   1 
ATOM   4939  N  N     . PHE A 1 1936 ? 173.669 156.434 142.174 1.00 85.86  ? 1936 PHE A N     1 
ATOM   4940  C  CA    . PHE A 1 1936 ? 174.237 157.564 141.452 1.00 79.71  ? 1936 PHE A CA    1 
ATOM   4941  C  C     . PHE A 1 1936 ? 175.638 157.845 141.973 1.00 78.55  ? 1936 PHE A C     1 
ATOM   4942  O  O     . PHE A 1 1936 ? 175.834 158.005 143.182 1.00 77.01  ? 1936 PHE A O     1 
ATOM   4943  C  CB    . PHE A 1 1936 ? 173.353 158.806 141.601 1.00 69.72  ? 1936 PHE A CB    1 
ATOM   4944  C  CG    . PHE A 1 1936 ? 173.824 159.985 140.802 1.00 61.93  ? 1936 PHE A CG    1 
ATOM   4945  C  CD1   . PHE A 1 1936 ? 173.974 159.894 139.430 1.00 59.62  ? 1936 PHE A CD1   1 
ATOM   4946  C  CD2   . PHE A 1 1936 ? 174.116 161.186 141.424 1.00 56.11  ? 1936 PHE A CD2   1 
ATOM   4947  C  CE1   . PHE A 1 1936 ? 174.407 160.976 138.696 1.00 55.44  ? 1936 PHE A CE1   1 
ATOM   4948  C  CE2   . PHE A 1 1936 ? 174.549 162.270 140.694 1.00 56.24  ? 1936 PHE A CE2   1 
ATOM   4949  C  CZ    . PHE A 1 1936 ? 174.694 162.165 139.328 1.00 54.08  ? 1936 PHE A CZ    1 
ATOM   4950  N  N     . ASP A 1 1937 ? 176.607 157.910 141.061 1.00 75.72  ? 1937 ASP A N     1 
ATOM   4951  C  CA    . ASP A 1 1937 ? 178.001 158.168 141.421 1.00 77.29  ? 1937 ASP A CA    1 
ATOM   4952  C  C     . ASP A 1 1937 ? 178.194 159.668 141.598 1.00 72.92  ? 1937 ASP A C     1 
ATOM   4953  O  O     . ASP A 1 1937 ? 178.506 160.395 140.654 1.00 70.02  ? 1937 ASP A O     1 
ATOM   4954  C  CB    . ASP A 1 1937 ? 178.944 157.607 140.365 1.00 82.42  ? 1937 ASP A CB    1 
ATOM   4955  C  CG    . ASP A 1 1937 ? 178.956 156.091 140.338 1.00 94.79  ? 1937 ASP A CG    1 
ATOM   4956  O  OD1   . ASP A 1 1937 ? 178.719 155.476 141.398 1.00 99.02  ? 1937 ASP A OD1   1 
ATOM   4957  O  OD2   . ASP A 1 1937 ? 179.205 155.515 139.258 1.00 100.55 ? 1937 ASP A OD2   1 
ATOM   4958  N  N     . PHE A 1 1938 ? 178.003 160.138 142.831 1.00 72.82  ? 1938 PHE A N     1 
ATOM   4959  C  CA    . PHE A 1 1938 ? 178.220 161.550 143.129 1.00 69.32  ? 1938 PHE A CA    1 
ATOM   4960  C  C     . PHE A 1 1938 ? 179.697 161.919 143.080 1.00 71.14  ? 1938 PHE A C     1 
ATOM   4961  O  O     . PHE A 1 1938 ? 180.059 162.977 142.554 1.00 68.43  ? 1938 PHE A O     1 
ATOM   4962  C  CB    . PHE A 1 1938 ? 177.629 161.897 144.494 1.00 73.92  ? 1938 PHE A CB    1 
ATOM   4963  C  CG    . PHE A 1 1938 ? 177.791 163.339 144.870 1.00 77.13  ? 1938 PHE A CG    1 
ATOM   4964  C  CD1   . PHE A 1 1938 ? 177.002 164.315 144.292 1.00 72.74  ? 1938 PHE A CD1   1 
ATOM   4965  C  CD2   . PHE A 1 1938 ? 178.736 163.715 145.809 1.00 77.32  ? 1938 PHE A CD2   1 
ATOM   4966  C  CE1   . PHE A 1 1938 ? 177.159 165.641 144.639 1.00 70.89  ? 1938 PHE A CE1   1 
ATOM   4967  C  CE2   . PHE A 1 1938 ? 178.894 165.038 146.162 1.00 75.09  ? 1938 PHE A CE2   1 
ATOM   4968  C  CZ    . PHE A 1 1938 ? 178.105 166.002 145.577 1.00 69.77  ? 1938 PHE A CZ    1 
ATOM   4969  N  N     . GLN A 1 1939 ? 180.564 161.070 143.636 1.00 75.70  ? 1939 GLN A N     1 
ATOM   4970  C  CA    . GLN A 1 1939 ? 181.984 161.404 143.700 1.00 73.65  ? 1939 GLN A CA    1 
ATOM   4971  C  C     . GLN A 1 1939 ? 182.613 161.477 142.316 1.00 73.88  ? 1939 GLN A C     1 
ATOM   4972  O  O     . GLN A 1 1939 ? 183.601 162.193 142.123 1.00 73.02  ? 1939 GLN A O     1 
ATOM   4973  C  CB    . GLN A 1 1939 ? 182.723 160.389 144.574 1.00 73.21  ? 1939 GLN A CB    1 
ATOM   4974  C  CG    . GLN A 1 1939 ? 182.626 158.946 144.100 1.00 78.50  ? 1939 GLN A CG    1 
ATOM   4975  C  CD    . GLN A 1 1939 ? 183.743 158.565 143.147 1.00 84.74  ? 1939 GLN A CD    1 
ATOM   4976  O  OE1   . GLN A 1 1939 ? 184.842 159.116 143.207 1.00 79.02  ? 1939 GLN A OE1   1 
ATOM   4977  N  NE2   . GLN A 1 1939 ? 183.467 157.612 142.264 1.00 86.76  ? 1939 GLN A NE2   1 
ATOM   4978  N  N     . ALA A 1 1940 ? 182.060 160.755 141.346 1.00 69.07  ? 1940 ALA A N     1 
ATOM   4979  C  CA    . ALA A 1 1940 ? 182.577 160.752 139.986 1.00 61.04  ? 1940 ALA A CA    1 
ATOM   4980  C  C     . ALA A 1 1940 ? 181.940 161.815 139.104 1.00 56.69  ? 1940 ALA A C     1 
ATOM   4981  O  O     . ALA A 1 1940 ? 182.316 161.930 137.935 1.00 54.62  ? 1940 ALA A O     1 
ATOM   4982  C  CB    . ALA A 1 1940 ? 182.375 159.375 139.351 1.00 60.09  ? 1940 ALA A CB    1 
ATOM   4983  N  N     . MET A 1 1941 ? 180.993 162.594 139.630 1.00 61.44  ? 1941 MET A N     1 
ATOM   4984  C  CA    . MET A 1 1941 ? 180.269 163.543 138.790 1.00 55.20  ? 1941 MET A CA    1 
ATOM   4985  C  C     . MET A 1 1941 ? 181.180 164.651 138.275 1.00 45.61  ? 1941 MET A C     1 
ATOM   4986  O  O     . MET A 1 1941 ? 181.073 165.052 137.113 1.00 50.18  ? 1941 MET A O     1 
ATOM   4987  C  CB    . MET A 1 1941 ? 179.086 164.131 139.555 1.00 53.76  ? 1941 MET A CB    1 
ATOM   4988  C  CG    . MET A 1 1941 ? 177.933 164.595 138.671 1.00 48.67  ? 1941 MET A CG    1 
ATOM   4989  S  SD    . MET A 1 1941 ? 177.361 163.358 137.485 1.00 62.72  ? 1941 MET A SD    1 
ATOM   4990  C  CE    . MET A 1 1941 ? 178.167 163.894 135.976 1.00 44.62  ? 1941 MET A CE    1 
ATOM   4991  N  N     . GLY A 1 1942 ? 182.074 165.164 139.120 1.00 42.15  ? 1942 GLY A N     1 
ATOM   4992  C  CA    . GLY A 1 1942 ? 182.980 166.207 138.666 1.00 40.24  ? 1942 GLY A CA    1 
ATOM   4993  C  C     . GLY A 1 1942 ? 183.941 165.721 137.599 1.00 42.78  ? 1942 GLY A C     1 
ATOM   4994  O  O     . GLY A 1 1942 ? 184.194 166.417 136.611 1.00 52.09  ? 1942 GLY A O     1 
ATOM   4995  N  N     . ARG A 1 1943 ? 184.483 164.517 137.780 1.00 40.53  ? 1943 ARG A N     1 
ATOM   4996  C  CA    . ARG A 1 1943 ? 185.386 163.947 136.787 1.00 37.53  ? 1943 ARG A CA    1 
ATOM   4997  C  C     . ARG A 1 1943 ? 184.671 163.716 135.461 1.00 39.98  ? 1943 ARG A C     1 
ATOM   4998  O  O     . ARG A 1 1943 ? 185.216 164.012 134.391 1.00 41.64  ? 1943 ARG A O     1 
ATOM   4999  C  CB    . ARG A 1 1943 ? 185.975 162.643 137.321 1.00 38.44  ? 1943 ARG A CB    1 
ATOM   5000  C  CG    . ARG A 1 1943 ? 187.121 162.084 136.510 1.00 43.05  ? 1943 ARG A CG    1 
ATOM   5001  C  CD    . ARG A 1 1943 ? 187.367 160.634 136.877 1.00 41.81  ? 1943 ARG A CD    1 
ATOM   5002  N  NE    . ARG A 1 1943 ? 186.239 159.788 136.514 1.00 37.71  ? 1943 ARG A NE    1 
ATOM   5003  C  CZ    . ARG A 1 1943 ? 185.526 159.080 137.379 1.00 44.37  ? 1943 ARG A CZ    1 
ATOM   5004  N  NH1   . ARG A 1 1943 ? 185.795 159.100 138.673 1.00 59.38  ? 1943 ARG A NH1   1 
ATOM   5005  N  NH2   . ARG A 1 1943 ? 184.519 158.336 136.934 1.00 42.82  ? 1943 ARG A NH2   1 
ATOM   5006  N  N     . ILE A 1 1944 ? 183.442 163.200 135.512 1.00 41.75  ? 1944 ILE A N     1 
ATOM   5007  C  CA    . ILE A 1 1944 ? 182.687 162.970 134.285 1.00 35.79  ? 1944 ILE A CA    1 
ATOM   5008  C  C     . ILE A 1 1944 ? 182.328 164.292 133.619 1.00 35.84  ? 1944 ILE A C     1 
ATOM   5009  O  O     . ILE A 1 1944 ? 182.305 164.391 132.389 1.00 39.97  ? 1944 ILE A O     1 
ATOM   5010  C  CB    . ILE A 1 1944 ? 181.440 162.116 134.576 1.00 37.29  ? 1944 ILE A CB    1 
ATOM   5011  C  CG1   . ILE A 1 1944 ? 181.850 160.733 135.075 1.00 41.03  ? 1944 ILE A CG1   1 
ATOM   5012  C  CG2   . ILE A 1 1944 ? 180.591 161.972 133.330 1.00 38.10  ? 1944 ILE A CG2   1 
ATOM   5013  C  CD1   . ILE A 1 1944 ? 180.682 159.845 135.423 1.00 39.62  ? 1944 ILE A CD1   1 
ATOM   5014  N  N     . PHE A 1 1945 ? 182.035 165.326 134.411 1.00 32.10  ? 1945 PHE A N     1 
ATOM   5015  C  CA    . PHE A 1 1945 ? 181.764 166.640 133.834 1.00 27.40  ? 1945 PHE A CA    1 
ATOM   5016  C  C     . PHE A 1 1945 ? 182.991 167.195 133.125 1.00 28.12  ? 1945 PHE A C     1 
ATOM   5017  O  O     . PHE A 1 1945 ? 182.884 167.758 132.028 1.00 34.71  ? 1945 PHE A O     1 
ATOM   5018  C  CB    . PHE A 1 1945 ? 181.293 167.607 134.918 1.00 32.45  ? 1945 PHE A CB    1 
ATOM   5019  C  CG    . PHE A 1 1945 ? 179.814 167.577 135.155 1.00 36.52  ? 1945 PHE A CG    1 
ATOM   5020  C  CD1   . PHE A 1 1945 ? 178.929 167.547 134.094 1.00 41.75  ? 1945 PHE A CD1   1 
ATOM   5021  C  CD2   . PHE A 1 1945 ? 179.307 167.593 136.440 1.00 41.18  ? 1945 PHE A CD2   1 
ATOM   5022  C  CE1   . PHE A 1 1945 ? 177.569 167.524 134.311 1.00 41.92  ? 1945 PHE A CE1   1 
ATOM   5023  C  CE2   . PHE A 1 1945 ? 177.948 167.570 136.662 1.00 38.96  ? 1945 PHE A CE2   1 
ATOM   5024  C  CZ    . PHE A 1 1945 ? 177.078 167.536 135.597 1.00 41.31  ? 1945 PHE A CZ    1 
ATOM   5025  N  N     . VAL A 1 1946 ? 184.167 167.052 133.740 1.00 28.55  ? 1946 VAL A N     1 
ATOM   5026  C  CA    . VAL A 1 1946 ? 185.401 167.471 133.080 1.00 30.28  ? 1946 VAL A CA    1 
ATOM   5027  C  C     . VAL A 1 1946 ? 185.602 166.688 131.790 1.00 34.30  ? 1946 VAL A C     1 
ATOM   5028  O  O     . VAL A 1 1946 ? 186.018 167.241 130.765 1.00 37.73  ? 1946 VAL A O     1 
ATOM   5029  C  CB    . VAL A 1 1946 ? 186.602 167.315 134.030 1.00 31.40  ? 1946 VAL A CB    1 
ATOM   5030  C  CG1   . VAL A 1 1946 ? 187.887 167.674 133.316 1.00 33.67  ? 1946 VAL A CG1   1 
ATOM   5031  C  CG2   . VAL A 1 1946 ? 186.425 168.187 135.254 1.00 45.26  ? 1946 VAL A CG2   1 
ATOM   5032  N  N     . GLY A 1 1947 ? 185.301 165.389 131.818 1.00 33.30  ? 1947 GLY A N     1 
ATOM   5033  C  CA    . GLY A 1 1947 ? 185.411 164.592 130.608 1.00 28.02  ? 1947 GLY A CA    1 
ATOM   5034  C  C     . GLY A 1 1947 ? 184.476 165.056 129.510 1.00 30.08  ? 1947 GLY A C     1 
ATOM   5035  O  O     . GLY A 1 1947 ? 184.872 165.151 128.348 1.00 37.33  ? 1947 GLY A O     1 
ATOM   5036  N  N     . LEU A 1 1948 ? 183.226 165.357 129.864 1.00 29.25  ? 1948 LEU A N     1 
ATOM   5037  C  CA    . LEU A 1 1948 ? 182.268 165.857 128.883 1.00 26.19  ? 1948 LEU A CA    1 
ATOM   5038  C  C     . LEU A 1 1948 ? 182.746 167.170 128.284 1.00 29.63  ? 1948 LEU A C     1 
ATOM   5039  O  O     . LEU A 1 1948 ? 182.641 167.391 127.073 1.00 30.09  ? 1948 LEU A O     1 
ATOM   5040  C  CB    . LEU A 1 1948 ? 180.893 166.042 129.525 1.00 23.09  ? 1948 LEU A CB    1 
ATOM   5041  C  CG    . LEU A 1 1948 ? 180.150 164.828 130.079 1.00 26.85  ? 1948 LEU A CG    1 
ATOM   5042  C  CD1   . LEU A 1 1948 ? 179.156 165.259 131.140 1.00 26.85  ? 1948 LEU A CD1   1 
ATOM   5043  C  CD2   . LEU A 1 1948 ? 179.449 164.085 128.972 1.00 27.31  ? 1948 LEU A CD2   1 
ATOM   5044  N  N     . CYS A 1 1949 ? 183.270 168.061 129.127 1.00 29.60  ? 1949 CYS A N     1 
ATOM   5045  C  CA    . CYS A 1 1949 ? 183.780 169.334 128.631 1.00 29.32  ? 1949 CYS A CA    1 
ATOM   5046  C  C     . CYS A 1 1949 ? 184.970 169.131 127.701 1.00 36.75  ? 1949 CYS A C     1 
ATOM   5047  O  O     . CYS A 1 1949 ? 185.127 169.860 126.716 1.00 47.48  ? 1949 CYS A O     1 
ATOM   5048  C  CB    . CYS A 1 1949 ? 184.163 170.238 129.800 1.00 34.04  ? 1949 CYS A CB    1 
ATOM   5049  S  SG    . CYS A 1 1949 ? 182.787 170.688 130.876 1.00 40.75  ? 1949 CYS A SG    1 
ATOM   5050  N  N     . GLN A 1 1950 ? 185.821 168.147 127.998 1.00 36.48  ? 1950 GLN A N     1 
ATOM   5051  C  CA    . GLN A 1 1950 ? 187.055 167.990 127.235 1.00 37.39  ? 1950 GLN A CA    1 
ATOM   5052  C  C     . GLN A 1 1950 ? 186.861 167.227 125.929 1.00 36.63  ? 1950 GLN A C     1 
ATOM   5053  O  O     . GLN A 1 1950 ? 187.510 167.559 124.931 1.00 40.07  ? 1950 GLN A O     1 
ATOM   5054  C  CB    . GLN A 1 1950 ? 188.113 167.295 128.091 1.00 37.77  ? 1950 GLN A CB    1 
ATOM   5055  C  CG    . GLN A 1 1950 ? 188.636 168.147 129.230 1.00 43.05  ? 1950 GLN A CG    1 
ATOM   5056  C  CD    . GLN A 1 1950 ? 190.017 168.695 128.951 1.00 56.15  ? 1950 GLN A CD    1 
ATOM   5057  O  OE1   . GLN A 1 1950 ? 190.969 167.941 128.753 1.00 64.54  ? 1950 GLN A OE1   1 
ATOM   5058  N  NE2   . GLN A 1 1950 ? 190.135 170.016 128.930 1.00 61.76  ? 1950 GLN A NE2   1 
ATOM   5059  N  N     . VAL A 1 1951 ? 185.996 166.213 125.900 1.00 33.74  ? 1951 VAL A N     1 
ATOM   5060  C  CA    . VAL A 1 1951 ? 185.808 165.405 124.697 1.00 32.94  ? 1951 VAL A CA    1 
ATOM   5061  C  C     . VAL A 1 1951 ? 184.632 165.885 123.855 1.00 35.84  ? 1951 VAL A C     1 
ATOM   5062  O  O     . VAL A 1 1951 ? 184.483 165.431 122.708 1.00 41.02  ? 1951 VAL A O     1 
ATOM   5063  C  CB    . VAL A 1 1951 ? 185.645 163.906 125.041 1.00 27.98  ? 1951 VAL A CB    1 
ATOM   5064  C  CG1   . VAL A 1 1951 ? 184.350 163.644 125.782 1.00 28.33  ? 1951 VAL A CG1   1 
ATOM   5065  C  CG2   . VAL A 1 1951 ? 185.780 163.016 123.810 1.00 38.53  ? 1951 VAL A CG2   1 
ATOM   5066  N  N     . GLY A 1 1952 ? 183.830 166.819 124.353 1.00 28.02  ? 1952 GLY A N     1 
ATOM   5067  C  CA    . GLY A 1 1952 ? 182.663 167.268 123.616 1.00 26.98  ? 1952 GLY A CA    1 
ATOM   5068  C  C     . GLY A 1 1952 ? 181.540 166.258 123.572 1.00 28.69  ? 1952 GLY A C     1 
ATOM   5069  O  O     . GLY A 1 1952 ? 180.924 166.064 122.517 1.00 34.36  ? 1952 GLY A O     1 
ATOM   5070  N  N     . ALA A 1 1953 ? 181.261 165.607 124.692 1.00 23.80  ? 1953 ALA A N     1 
ATOM   5071  C  CA    . ALA A 1 1953 ? 180.197 164.623 124.796 1.00 21.18  ? 1953 ALA A CA    1 
ATOM   5072  C  C     . ALA A 1 1953 ? 178.976 165.235 125.471 1.00 22.81  ? 1953 ALA A C     1 
ATOM   5073  O  O     . ALA A 1 1953 ? 179.060 166.259 126.151 1.00 30.86  ? 1953 ALA A O     1 
ATOM   5074  C  CB    . ALA A 1 1953 ? 180.674 163.397 125.577 1.00 23.81  ? 1953 ALA A CB    1 
ATOM   5075  N  N     . TRP A 1 1954 ? 177.832 164.593 125.273 1.00 21.33  ? 1954 TRP A N     1 
ATOM   5076  C  CA    . TRP A 1 1954 ? 176.589 165.048 125.872 1.00 17.80  ? 1954 TRP A CA    1 
ATOM   5077  C  C     . TRP A 1 1954 ? 176.332 164.321 127.183 1.00 21.83  ? 1954 TRP A C     1 
ATOM   5078  O  O     . TRP A 1 1954 ? 176.743 163.175 127.372 1.00 28.61  ? 1954 TRP A O     1 
ATOM   5079  C  CB    . TRP A 1 1954 ? 175.411 164.825 124.926 1.00 17.94  ? 1954 TRP A CB    1 
ATOM   5080  C  CG    . TRP A 1 1954 ? 175.374 165.761 123.771 1.00 18.59  ? 1954 TRP A CG    1 
ATOM   5081  C  CD1   . TRP A 1 1954 ? 176.404 166.504 123.284 1.00 19.53  ? 1954 TRP A CD1   1 
ATOM   5082  C  CD2   . TRP A 1 1954 ? 174.242 166.058 122.952 1.00 20.41  ? 1954 TRP A CD2   1 
ATOM   5083  N  NE1   . TRP A 1 1954 ? 175.986 167.244 122.208 1.00 18.74  ? 1954 TRP A NE1   1 
ATOM   5084  C  CE2   . TRP A 1 1954 ? 174.660 166.988 121.985 1.00 20.10  ? 1954 TRP A CE2   1 
ATOM   5085  C  CE3   . TRP A 1 1954 ? 172.914 165.626 122.941 1.00 17.62  ? 1954 TRP A CE3   1 
ATOM   5086  C  CZ2   . TRP A 1 1954 ? 173.801 167.491 121.018 1.00 17.30  ? 1954 TRP A CZ2   1 
ATOM   5087  C  CZ3   . TRP A 1 1954 ? 172.062 166.131 121.985 1.00 18.20  ? 1954 TRP A CZ3   1 
ATOM   5088  C  CH2   . TRP A 1 1954 ? 172.508 167.052 121.036 1.00 17.28  ? 1954 TRP A CH2   1 
ATOM   5089  N  N     . GLY A 1 1955 ? 175.642 165.002 128.089 1.00 16.08  ? 1955 GLY A N     1 
ATOM   5090  C  CA    . GLY A 1 1955 ? 175.293 164.408 129.360 1.00 18.92  ? 1955 GLY A CA    1 
ATOM   5091  C  C     . GLY A 1 1955 ? 173.827 164.581 129.684 1.00 22.85  ? 1955 GLY A C     1 
ATOM   5092  O  O     . GLY A 1 1955 ? 173.339 165.708 129.784 1.00 35.64  ? 1955 GLY A O     1 
ATOM   5093  N  N     . CYS A 1 1956 ? 173.113 163.474 129.849 1.00 22.18  ? 1956 CYS A N     1 
ATOM   5094  C  CA    . CYS A 1 1956 ? 171.690 163.494 130.150 1.00 24.87  ? 1956 CYS A CA    1 
ATOM   5095  C  C     . CYS A 1 1956 ? 171.463 162.936 131.546 1.00 28.95  ? 1956 CYS A C     1 
ATOM   5096  O  O     . CYS A 1 1956 ? 172.060 161.923 131.919 1.00 37.81  ? 1956 CYS A O     1 
ATOM   5097  C  CB    . CYS A 1 1956 ? 170.900 162.685 129.120 1.00 25.52  ? 1956 CYS A CB    1 
ATOM   5098  S  SG    . CYS A 1 1956 ? 169.109 162.860 129.252 1.00 37.92  ? 1956 CYS A SG    1 
ATOM   5099  N  N     . PHE A 1 1957 ? 170.609 163.602 132.314 1.00 24.74  ? 1957 PHE A N     1 
ATOM   5100  C  CA    . PHE A 1 1957 ? 170.226 163.147 133.642 1.00 28.95  ? 1957 PHE A CA    1 
ATOM   5101  C  C     . PHE A 1 1957 ? 168.831 162.544 133.553 1.00 33.17  ? 1957 PHE A C     1 
ATOM   5102  O  O     . PHE A 1 1957 ? 167.893 163.215 133.118 1.00 43.35  ? 1957 PHE A O     1 
ATOM   5103  C  CB    . PHE A 1 1957 ? 170.269 164.304 134.637 1.00 31.83  ? 1957 PHE A CB    1 
ATOM   5104  C  CG    . PHE A 1 1957 ? 171.659 164.776 134.946 1.00 38.77  ? 1957 PHE A CG    1 
ATOM   5105  C  CD1   . PHE A 1 1957 ? 172.445 164.104 135.865 1.00 35.16  ? 1957 PHE A CD1   1 
ATOM   5106  C  CD2   . PHE A 1 1957 ? 172.191 165.874 134.296 1.00 39.20  ? 1957 PHE A CD2   1 
ATOM   5107  C  CE1   . PHE A 1 1957 ? 173.724 164.531 136.143 1.00 32.01  ? 1957 PHE A CE1   1 
ATOM   5108  C  CE2   . PHE A 1 1957 ? 173.471 166.303 134.568 1.00 36.98  ? 1957 PHE A CE2   1 
ATOM   5109  C  CZ    . PHE A 1 1957 ? 174.238 165.631 135.493 1.00 32.80  ? 1957 PHE A CZ    1 
ATOM   5110  N  N     . ASP A 1 1958 ? 168.701 161.279 133.963 1.00 35.79  ? 1958 ASP A N     1 
ATOM   5111  C  CA    . ASP A 1 1958 ? 167.473 160.533 133.705 1.00 41.66  ? 1958 ASP A CA    1 
ATOM   5112  C  C     . ASP A 1 1958 ? 166.268 161.202 134.356 1.00 49.09  ? 1958 ASP A C     1 
ATOM   5113  O  O     . ASP A 1 1958 ? 165.248 161.441 133.701 1.00 56.02  ? 1958 ASP A O     1 
ATOM   5114  C  CB    . ASP A 1 1958 ? 167.623 159.094 134.196 1.00 50.94  ? 1958 ASP A CB    1 
ATOM   5115  C  CG    . ASP A 1 1958 ? 166.601 158.159 133.582 1.00 66.52  ? 1958 ASP A CG    1 
ATOM   5116  O  OD1   . ASP A 1 1958 ? 165.794 158.619 132.749 1.00 69.26  ? 1958 ASP A OD1   1 
ATOM   5117  O  OD2   . ASP A 1 1958 ? 166.604 156.961 133.933 1.00 79.33  ? 1958 ASP A OD2   1 
ATOM   5118  N  N     . GLU A 1 1959 ? 166.365 161.508 135.649 1.00 45.71  ? 1959 GLU A N     1 
ATOM   5119  C  CA    . GLU A 1 1959 ? 165.337 162.289 136.340 1.00 43.24  ? 1959 GLU A CA    1 
ATOM   5120  C  C     . GLU A 1 1959 ? 166.056 163.100 137.417 1.00 49.33  ? 1959 GLU A C     1 
ATOM   5121  O  O     . GLU A 1 1959 ? 166.286 162.618 138.527 1.00 60.51  ? 1959 GLU A O     1 
ATOM   5122  C  CB    . GLU A 1 1959 ? 164.244 161.411 136.930 1.00 50.19  ? 1959 GLU A CB    1 
ATOM   5123  C  CG    . GLU A 1 1959 ? 163.123 161.075 135.963 1.00 61.93  ? 1959 GLU A CG    1 
ATOM   5124  C  CD    . GLU A 1 1959 ? 162.183 160.018 136.502 1.00 76.94  ? 1959 GLU A CD    1 
ATOM   5125  O  OE1   . GLU A 1 1959 ? 161.630 160.218 137.602 1.00 78.77  ? 1959 GLU A OE1   1 
ATOM   5126  O  OE2   . GLU A 1 1959 ? 161.996 158.986 135.824 1.00 76.09  ? 1959 GLU A OE2   1 
ATOM   5127  N  N     . PHE A 1 1960 ? 166.393 164.342 137.071 1.00 43.51  ? 1960 PHE A N     1 
ATOM   5128  C  CA    . PHE A 1 1960 ? 167.220 165.177 137.931 1.00 37.65  ? 1960 PHE A CA    1 
ATOM   5129  C  C     . PHE A 1 1960 ? 166.557 165.483 139.266 1.00 46.05  ? 1960 PHE A C     1 
ATOM   5130  O  O     . PHE A 1 1960 ? 167.260 165.778 140.237 1.00 54.36  ? 1960 PHE A O     1 
ATOM   5131  C  CB    . PHE A 1 1960 ? 167.553 166.472 137.198 1.00 35.17  ? 1960 PHE A CB    1 
ATOM   5132  C  CG    . PHE A 1 1960 ? 168.763 167.181 137.722 1.00 37.66  ? 1960 PHE A CG    1 
ATOM   5133  C  CD1   . PHE A 1 1960 ? 169.972 166.523 137.829 1.00 37.97  ? 1960 PHE A CD1   1 
ATOM   5134  C  CD2   . PHE A 1 1960 ? 168.701 168.518 138.074 1.00 39.58  ? 1960 PHE A CD2   1 
ATOM   5135  C  CE1   . PHE A 1 1960 ? 171.087 167.176 138.299 1.00 38.52  ? 1960 PHE A CE1   1 
ATOM   5136  C  CE2   . PHE A 1 1960 ? 169.817 169.176 138.540 1.00 36.06  ? 1960 PHE A CE2   1 
ATOM   5137  C  CZ    . PHE A 1 1960 ? 171.010 168.504 138.654 1.00 37.85  ? 1960 PHE A CZ    1 
ATOM   5138  N  N     . ASN A 1 1961 ? 165.228 165.417 139.341 1.00 46.93  ? 1961 ASN A N     1 
ATOM   5139  C  CA    . ASN A 1 1961 ? 164.539 165.708 140.590 1.00 46.32  ? 1961 ASN A CA    1 
ATOM   5140  C  C     . ASN A 1 1961 ? 164.565 164.540 141.567 1.00 47.34  ? 1961 ASN A C     1 
ATOM   5141  O  O     . ASN A 1 1961 ? 164.178 164.715 142.727 1.00 50.99  ? 1961 ASN A O     1 
ATOM   5142  C  CB    . ASN A 1 1961 ? 163.094 166.126 140.309 1.00 52.24  ? 1961 ASN A CB    1 
ATOM   5143  C  CG    . ASN A 1 1961 ? 162.320 165.082 139.529 1.00 56.35  ? 1961 ASN A CG    1 
ATOM   5144  O  OD1   . ASN A 1 1961 ? 162.822 163.996 139.246 1.00 59.43  ? 1961 ASN A OD1   1 
ATOM   5145  N  ND2   . ASN A 1 1961 ? 161.085 165.409 139.178 1.00 58.40  ? 1961 ASN A ND2   1 
ATOM   5146  N  N     . ARG A 1 1962 ? 165.008 163.359 141.131 1.00 46.12  ? 1962 ARG A N     1 
ATOM   5147  C  CA    . ARG A 1 1962 ? 165.145 162.228 142.040 1.00 49.28  ? 1962 ARG A CA    1 
ATOM   5148  C  C     . ARG A 1 1962 ? 166.355 162.351 142.954 1.00 53.34  ? 1962 ARG A C     1 
ATOM   5149  O  O     . ARG A 1 1962 ? 166.454 161.595 143.925 1.00 56.21  ? 1962 ARG A O     1 
ATOM   5150  C  CB    . ARG A 1 1962 ? 165.233 160.921 141.252 1.00 54.08  ? 1962 ARG A CB    1 
ATOM   5151  C  CG    . ARG A 1 1962 ? 164.003 160.599 140.424 1.00 62.15  ? 1962 ARG A CG    1 
ATOM   5152  C  CD    . ARG A 1 1962 ? 163.835 159.097 140.269 1.00 67.37  ? 1962 ARG A CD    1 
ATOM   5153  N  NE    . ARG A 1 1962 ? 164.970 158.496 139.578 1.00 75.31  ? 1962 ARG A NE    1 
ATOM   5154  C  CZ    . ARG A 1 1962 ? 164.887 157.837 138.431 1.00 75.96  ? 1962 ARG A CZ    1 
ATOM   5155  N  NH1   . ARG A 1 1962 ? 163.727 157.647 137.825 1.00 74.46  ? 1962 ARG A NH1   1 
ATOM   5156  N  NH2   . ARG A 1 1962 ? 165.996 157.353 137.879 1.00 76.69  ? 1962 ARG A NH2   1 
ATOM   5157  N  N     . LEU A 1 1963 ? 167.270 163.271 142.667 1.00 54.33  ? 1963 LEU A N     1 
ATOM   5158  C  CA    . LEU A 1 1963 ? 168.439 163.465 143.510 1.00 55.15  ? 1963 LEU A CA    1 
ATOM   5159  C  C     . LEU A 1 1963 ? 168.042 164.093 144.842 1.00 58.93  ? 1963 LEU A C     1 
ATOM   5160  O  O     . LEU A 1 1963 ? 167.107 164.893 144.922 1.00 63.10  ? 1963 LEU A O     1 
ATOM   5161  C  CB    . LEU A 1 1963 ? 169.461 164.352 142.800 1.00 48.63  ? 1963 LEU A CB    1 
ATOM   5162  C  CG    . LEU A 1 1963 ? 170.256 163.703 141.669 1.00 43.85  ? 1963 LEU A CG    1 
ATOM   5163  C  CD1   . LEU A 1 1963 ? 171.398 164.602 141.234 1.00 41.78  ? 1963 LEU A CD1   1 
ATOM   5164  C  CD2   . LEU A 1 1963 ? 170.776 162.347 142.101 1.00 52.85  ? 1963 LEU A CD2   1 
ATOM   5165  N  N     . GLU A 1 1964 ? 168.763 163.720 145.897 1.00 57.74  ? 1964 GLU A N     1 
ATOM   5166  C  CA    . GLU A 1 1964 ? 168.529 164.337 147.193 1.00 67.36  ? 1964 GLU A CA    1 
ATOM   5167  C  C     . GLU A 1 1964 ? 169.046 165.774 147.184 1.00 70.97  ? 1964 GLU A C     1 
ATOM   5168  O  O     . GLU A 1 1964 ? 169.762 166.198 146.276 1.00 70.83  ? 1964 GLU A O     1 
ATOM   5169  C  CB    . GLU A 1 1964 ? 169.196 163.537 148.310 1.00 75.43  ? 1964 GLU A CB    1 
ATOM   5170  C  CG    . GLU A 1 1964 ? 170.711 163.555 148.275 1.00 80.14  ? 1964 GLU A CG    1 
ATOM   5171  C  CD    . GLU A 1 1964 ? 171.326 162.710 149.371 1.00 85.54  ? 1964 GLU A CD    1 
ATOM   5172  O  OE1   . GLU A 1 1964 ? 170.565 162.091 150.143 1.00 90.00  ? 1964 GLU A OE1   1 
ATOM   5173  O  OE2   . GLU A 1 1964 ? 172.570 162.664 149.462 1.00 87.43  ? 1964 GLU A OE2   1 
ATOM   5174  N  N     . GLU A 1 1965 ? 168.687 166.520 148.232 1.00 74.80  ? 1965 GLU A N     1 
ATOM   5175  C  CA    . GLU A 1 1965 ? 168.915 167.963 148.238 1.00 71.66  ? 1965 GLU A CA    1 
ATOM   5176  C  C     . GLU A 1 1965 ? 170.394 168.310 148.104 1.00 71.25  ? 1965 GLU A C     1 
ATOM   5177  O  O     . GLU A 1 1965 ? 170.752 169.223 147.352 1.00 69.71  ? 1965 GLU A O     1 
ATOM   5178  C  CB    . GLU A 1 1965 ? 168.337 168.576 149.511 1.00 81.98  ? 1965 GLU A CB    1 
ATOM   5179  C  CG    . GLU A 1 1965 ? 166.952 169.173 149.338 1.00 94.38  ? 1965 GLU A CG    1 
ATOM   5180  C  CD    . GLU A 1 1965 ? 166.476 169.905 150.576 1.00 104.80 ? 1965 GLU A CD    1 
ATOM   5181  O  OE1   . GLU A 1 1965 ? 167.330 170.336 151.379 1.00 100.31 ? 1965 GLU A OE1   1 
ATOM   5182  O  OE2   . GLU A 1 1965 ? 165.247 170.049 150.747 1.00 108.21 ? 1965 GLU A OE2   1 
ATOM   5183  N  N     . ARG A 1 1966 ? 171.268 167.600 148.818 1.00 69.45  ? 1966 ARG A N     1 
ATOM   5184  C  CA    . ARG A 1 1966 ? 172.692 167.921 148.765 1.00 71.02  ? 1966 ARG A CA    1 
ATOM   5185  C  C     . ARG A 1 1966 ? 173.279 167.607 147.394 1.00 71.21  ? 1966 ARG A C     1 
ATOM   5186  O  O     . ARG A 1 1966 ? 173.972 168.443 146.794 1.00 69.72  ? 1966 ARG A O     1 
ATOM   5187  C  CB    . ARG A 1 1966 ? 173.440 167.165 149.863 1.00 77.66  ? 1966 ARG A CB    1 
ATOM   5188  C  CG    . ARG A 1 1966 ? 174.951 167.328 149.811 1.00 79.24  ? 1966 ARG A CG    1 
ATOM   5189  C  CD    . ARG A 1 1966 ? 175.659 166.218 150.573 1.00 79.23  ? 1966 ARG A CD    1 
ATOM   5190  N  NE    . ARG A 1 1966 ? 175.975 165.077 149.724 1.00 82.91  ? 1966 ARG A NE    1 
ATOM   5191  C  CZ    . ARG A 1 1966 ? 175.382 163.894 149.808 1.00 87.04  ? 1966 ARG A CZ    1 
ATOM   5192  N  NH1   . ARG A 1 1966 ? 174.431 163.659 150.697 1.00 93.73  ? 1966 ARG A NH1   1 
ATOM   5193  N  NH2   . ARG A 1 1966 ? 175.753 162.922 148.980 1.00 79.68  ? 1966 ARG A NH2   1 
ATOM   5194  N  N     . MET A 1 1967 ? 173.014 166.403 146.879 1.00 69.24  ? 1967 MET A N     1 
ATOM   5195  C  CA    . MET A 1 1967 ? 173.493 166.052 145.547 1.00 58.68  ? 1967 MET A CA    1 
ATOM   5196  C  C     . MET A 1 1967 ? 172.859 166.941 144.490 1.00 56.02  ? 1967 MET A C     1 
ATOM   5197  O  O     . MET A 1 1967 ? 173.529 167.361 143.539 1.00 61.12  ? 1967 MET A O     1 
ATOM   5198  C  CB    . MET A 1 1967 ? 173.209 164.580 145.247 1.00 55.74  ? 1967 MET A CB    1 
ATOM   5199  C  CG    . MET A 1 1967 ? 173.988 163.606 146.109 1.00 68.23  ? 1967 MET A CG    1 
ATOM   5200  S  SD    . MET A 1 1967 ? 173.840 161.899 145.545 1.00 81.47  ? 1967 MET A SD    1 
ATOM   5201  C  CE    . MET A 1 1967 ? 172.067 161.664 145.585 1.00 63.18  ? 1967 MET A CE    1 
ATOM   5202  N  N     . LEU A 1 1968 ? 171.566 167.237 144.638 1.00 53.34  ? 1968 LEU A N     1 
ATOM   5203  C  CA    . LEU A 1 1968 ? 170.897 168.132 143.701 1.00 50.72  ? 1968 LEU A CA    1 
ATOM   5204  C  C     . LEU A 1 1968 ? 171.592 169.484 143.656 1.00 51.42  ? 1968 LEU A C     1 
ATOM   5205  O  O     . LEU A 1 1968 ? 171.893 170.000 142.578 1.00 52.44  ? 1968 LEU A O     1 
ATOM   5206  C  CB    . LEU A 1 1968 ? 169.427 168.299 144.089 1.00 55.26  ? 1968 LEU A CB    1 
ATOM   5207  C  CG    . LEU A 1 1968 ? 168.472 168.934 143.078 1.00 53.49  ? 1968 LEU A CG    1 
ATOM   5208  C  CD1   . LEU A 1 1968 ? 168.673 168.335 141.706 1.00 46.55  ? 1968 LEU A CD1   1 
ATOM   5209  C  CD2   . LEU A 1 1968 ? 167.035 168.761 143.530 1.00 56.43  ? 1968 LEU A CD2   1 
ATOM   5210  N  N     . SER A 1 1969 ? 171.888 170.055 144.826 1.00 54.43  ? 1969 SER A N     1 
ATOM   5211  C  CA    . SER A 1 1969 ? 172.515 171.373 144.875 1.00 53.37  ? 1969 SER A CA    1 
ATOM   5212  C  C     . SER A 1 1969 ? 173.923 171.349 144.293 1.00 54.41  ? 1969 SER A C     1 
ATOM   5213  O  O     . SER A 1 1969 ? 174.305 172.252 143.539 1.00 59.91  ? 1969 SER A O     1 
ATOM   5214  C  CB    . SER A 1 1969 ? 172.538 171.883 146.314 1.00 57.67  ? 1969 SER A CB    1 
ATOM   5215  O  OG    . SER A 1 1969 ? 171.226 171.980 146.839 1.00 62.83  ? 1969 SER A OG    1 
ATOM   5216  N  N     . ALA A 1 1970 ? 174.712 170.323 144.623 1.00 48.61  ? 1970 ALA A N     1 
ATOM   5217  C  CA    . ALA A 1 1970 ? 176.088 170.278 144.136 1.00 43.40  ? 1970 ALA A CA    1 
ATOM   5218  C  C     . ALA A 1 1970 ? 176.137 170.077 142.623 1.00 50.06  ? 1970 ALA A C     1 
ATOM   5219  O  O     . ALA A 1 1970 ? 176.869 170.782 141.909 1.00 52.13  ? 1970 ALA A O     1 
ATOM   5220  C  CB    . ALA A 1 1970 ? 176.859 169.174 144.854 1.00 46.65  ? 1970 ALA A CB    1 
ATOM   5221  N  N     . VAL A 1 1971 ? 175.361 169.118 142.113 1.00 50.58  ? 1971 VAL A N     1 
ATOM   5222  C  CA    . VAL A 1 1971 ? 175.331 168.893 140.675 1.00 46.02  ? 1971 VAL A CA    1 
ATOM   5223  C  C     . VAL A 1 1971 ? 174.732 170.097 139.962 1.00 47.47  ? 1971 VAL A C     1 
ATOM   5224  O  O     . VAL A 1 1971 ? 175.134 170.419 138.841 1.00 49.85  ? 1971 VAL A O     1 
ATOM   5225  C  CB    . VAL A 1 1971 ? 174.571 167.594 140.352 1.00 42.58  ? 1971 VAL A CB    1 
ATOM   5226  C  CG1   . VAL A 1 1971 ? 174.495 167.380 138.854 1.00 46.67  ? 1971 VAL A CG1   1 
ATOM   5227  C  CG2   . VAL A 1 1971 ? 175.247 166.412 141.019 1.00 44.25  ? 1971 VAL A CG2   1 
ATOM   5228  N  N     . SER A 1 1972 ? 173.780 170.791 140.590 1.00 42.19  ? 1972 SER A N     1 
ATOM   5229  C  CA    . SER A 1 1972 ? 173.237 172.005 139.995 1.00 41.82  ? 1972 SER A CA    1 
ATOM   5230  C  C     . SER A 1 1972 ? 174.296 173.090 139.896 1.00 45.02  ? 1972 SER A C     1 
ATOM   5231  O  O     . SER A 1 1972 ? 174.351 173.817 138.903 1.00 50.05  ? 1972 SER A O     1 
ATOM   5232  C  CB    . SER A 1 1972 ? 172.041 172.495 140.808 1.00 45.80  ? 1972 SER A CB    1 
ATOM   5233  O  OG    . SER A 1 1972 ? 171.114 171.448 141.027 1.00 55.03  ? 1972 SER A OG    1 
ATOM   5234  N  N     . GLN A 1 1973 ? 175.144 173.220 140.918 1.00 46.48  ? 1973 GLN A N     1 
ATOM   5235  C  CA    . GLN A 1 1973 ? 176.231 174.193 140.849 1.00 44.97  ? 1973 GLN A CA    1 
ATOM   5236  C  C     . GLN A 1 1973 ? 177.196 173.859 139.718 1.00 47.47  ? 1973 GLN A C     1 
ATOM   5237  O  O     . GLN A 1 1973 ? 177.621 174.747 138.963 1.00 52.88  ? 1973 GLN A O     1 
ATOM   5238  C  CB    . GLN A 1 1973 ? 176.971 174.245 142.185 1.00 43.78  ? 1973 GLN A CB    1 
ATOM   5239  C  CG    . GLN A 1 1973 ? 176.384 175.221 143.192 1.00 55.96  ? 1973 GLN A CG    1 
ATOM   5240  C  CD    . GLN A 1 1973 ? 176.294 176.635 142.656 1.00 65.99  ? 1973 GLN A CD    1 
ATOM   5241  O  OE1   . GLN A 1 1973 ? 175.203 177.152 142.418 1.00 65.49  ? 1973 GLN A OE1   1 
ATOM   5242  N  NE2   . GLN A 1 1973 ? 177.444 177.270 142.465 1.00 62.68  ? 1973 GLN A NE2   1 
ATOM   5243  N  N     . GLN A 1 1974 ? 177.549 172.578 139.581 1.00 44.49  ? 1974 GLN A N     1 
ATOM   5244  C  CA    . GLN A 1 1974 ? 178.451 172.180 138.500 1.00 40.56  ? 1974 GLN A CA    1 
ATOM   5245  C  C     . GLN A 1 1974 ? 177.821 172.419 137.129 1.00 42.99  ? 1974 GLN A C     1 
ATOM   5246  O  O     . GLN A 1 1974 ? 178.468 172.957 136.218 1.00 47.54  ? 1974 GLN A O     1 
ATOM   5247  C  CB    . GLN A 1 1974 ? 178.851 170.716 138.671 1.00 41.88  ? 1974 GLN A CB    1 
ATOM   5248  C  CG    . GLN A 1 1974 ? 179.559 170.432 139.986 1.00 46.55  ? 1974 GLN A CG    1 
ATOM   5249  C  CD    . GLN A 1 1974 ? 179.725 168.951 140.258 1.00 52.18  ? 1974 GLN A CD    1 
ATOM   5250  O  OE1   . GLN A 1 1974 ? 179.301 168.112 139.468 1.00 55.36  ? 1974 GLN A OE1   1 
ATOM   5251  N  NE2   . GLN A 1 1974 ? 180.344 168.623 141.385 1.00 56.68  ? 1974 GLN A NE2   1 
ATOM   5252  N  N     . VAL A 1 1975 ? 176.553 172.039 136.967 1.00 44.95  ? 1975 VAL A N     1 
ATOM   5253  C  CA    . VAL A 1 1975 ? 175.858 172.266 135.705 1.00 35.58  ? 1975 VAL A CA    1 
ATOM   5254  C  C     . VAL A 1 1975 ? 175.762 173.757 135.416 1.00 37.36  ? 1975 VAL A C     1 
ATOM   5255  O  O     . VAL A 1 1975 ? 175.885 174.188 134.267 1.00 43.19  ? 1975 VAL A O     1 
ATOM   5256  C  CB    . VAL A 1 1975 ? 174.470 171.601 135.734 1.00 30.48  ? 1975 VAL A CB    1 
ATOM   5257  C  CG1   . VAL A 1 1975 ? 173.651 172.034 134.543 1.00 31.97  ? 1975 VAL A CG1   1 
ATOM   5258  C  CG2   . VAL A 1 1975 ? 174.608 170.094 135.749 1.00 37.77  ? 1975 VAL A CG2   1 
ATOM   5259  N  N     . GLN A 1 1976 ? 175.555 174.568 136.455 1.00 40.02  ? 1976 GLN A N     1 
ATOM   5260  C  CA    . GLN A 1 1976 ? 175.454 176.008 136.267 1.00 40.39  ? 1976 GLN A CA    1 
ATOM   5261  C  C     . GLN A 1 1976 ? 176.766 176.599 135.780 1.00 42.24  ? 1976 GLN A C     1 
ATOM   5262  O  O     . GLN A 1 1976 ? 176.772 177.442 134.878 1.00 47.26  ? 1976 GLN A O     1 
ATOM   5263  C  CB    . GLN A 1 1976 ? 175.024 176.681 137.568 1.00 43.39  ? 1976 GLN A CB    1 
ATOM   5264  C  CG    . GLN A 1 1976 ? 174.928 178.191 137.461 1.00 48.64  ? 1976 GLN A CG    1 
ATOM   5265  C  CD    . GLN A 1 1976 ? 174.678 178.855 138.795 1.00 58.21  ? 1976 GLN A CD    1 
ATOM   5266  O  OE1   . GLN A 1 1976 ? 174.585 178.190 139.824 1.00 61.60  ? 1976 GLN A OE1   1 
ATOM   5267  N  NE2   . GLN A 1 1976 ? 174.572 180.177 138.785 1.00 60.99  ? 1976 GLN A NE2   1 
ATOM   5268  N  N     . CYS A 1 1977 ? 177.892 176.186 136.366 1.00 40.44  ? 1977 CYS A N     1 
ATOM   5269  C  CA    . CYS A 1 1977 ? 179.162 176.752 135.917 1.00 42.92  ? 1977 CYS A CA    1 
ATOM   5270  C  C     . CYS A 1 1977 ? 179.475 176.311 134.490 1.00 44.37  ? 1977 CYS A C     1 
ATOM   5271  O  O     . CYS A 1 1977 ? 179.937 177.114 133.668 1.00 49.84  ? 1977 CYS A O     1 
ATOM   5272  C  CB    . CYS A 1 1977 ? 180.304 176.395 136.874 1.00 44.97  ? 1977 CYS A CB    1 
ATOM   5273  S  SG    . CYS A 1 1977 ? 180.677 174.656 137.117 1.00 63.60  ? 1977 CYS A SG    1 
ATOM   5274  N  N     . ILE A 1 1978 ? 179.186 175.047 134.159 1.00 44.97  ? 1978 ILE A N     1 
ATOM   5275  C  CA    . ILE A 1 1978 ? 179.430 174.590 132.790 1.00 38.68  ? 1978 ILE A CA    1 
ATOM   5276  C  C     . ILE A 1 1978 ? 178.522 175.314 131.800 1.00 39.72  ? 1978 ILE A C     1 
ATOM   5277  O  O     . ILE A 1 1978 ? 178.949 175.677 130.697 1.00 41.87  ? 1978 ILE A O     1 
ATOM   5278  C  CB    . ILE A 1 1978 ? 179.276 173.063 132.684 1.00 32.80  ? 1978 ILE A CB    1 
ATOM   5279  C  CG1   . ILE A 1 1978 ? 180.134 172.363 133.731 1.00 38.29  ? 1978 ILE A CG1   1 
ATOM   5280  C  CG2   . ILE A 1 1978 ? 179.672 172.594 131.305 1.00 42.39  ? 1978 ILE A CG2   1 
ATOM   5281  C  CD1   . ILE A 1 1978 ? 179.956 170.873 133.748 1.00 39.45  ? 1978 ILE A CD1   1 
ATOM   5282  N  N     . GLN A 1 1979 ? 177.260 175.544 132.169 1.00 38.61  ? 1979 GLN A N     1 
ATOM   5283  C  CA    . GLN A 1 1979 ? 176.344 176.210 131.251 1.00 35.99  ? 1979 GLN A CA    1 
ATOM   5284  C  C     . GLN A 1 1979 ? 176.654 177.692 131.112 1.00 41.04  ? 1979 GLN A C     1 
ATOM   5285  O  O     . GLN A 1 1979 ? 176.442 178.263 130.041 1.00 47.71  ? 1979 GLN A O     1 
ATOM   5286  C  CB    . GLN A 1 1979 ? 174.899 176.005 131.696 1.00 31.84  ? 1979 GLN A CB    1 
ATOM   5287  C  CG    . GLN A 1 1979 ? 174.281 174.758 131.107 1.00 34.54  ? 1979 GLN A CG    1 
ATOM   5288  C  CD    . GLN A 1 1979 ? 174.012 174.900 129.624 1.00 43.26  ? 1979 GLN A CD    1 
ATOM   5289  O  OE1   . GLN A 1 1979 ? 174.064 175.999 129.073 1.00 36.64  ? 1979 GLN A OE1   1 
ATOM   5290  N  NE2   . GLN A 1 1979 ? 173.755 173.781 128.962 1.00 43.68  ? 1979 GLN A NE2   1 
ATOM   5291  N  N     . GLU A 1 1980 ? 177.150 178.334 132.170 1.00 38.61  ? 1980 GLU A N     1 
ATOM   5292  C  CA    . GLU A 1 1980 ? 177.629 179.704 132.026 1.00 39.95  ? 1980 GLU A CA    1 
ATOM   5293  C  C     . GLU A 1 1980 ? 178.840 179.758 131.105 1.00 44.31  ? 1980 GLU A C     1 
ATOM   5294  O  O     . GLU A 1 1980 ? 178.964 180.671 130.279 1.00 48.50  ? 1980 GLU A O     1 
ATOM   5295  C  CB    . GLU A 1 1980 ? 177.955 180.290 133.398 1.00 43.50  ? 1980 GLU A CB    1 
ATOM   5296  C  CG    . GLU A 1 1980 ? 176.723 180.673 134.201 1.00 53.43  ? 1980 GLU A CG    1 
ATOM   5297  C  CD    . GLU A 1 1980 ? 177.045 181.022 135.640 1.00 65.00  ? 1980 GLU A CD    1 
ATOM   5298  O  OE1   . GLU A 1 1980 ? 178.230 180.934 136.025 1.00 69.12  ? 1980 GLU A OE1   1 
ATOM   5299  O  OE2   . GLU A 1 1980 ? 176.111 181.382 136.386 1.00 58.13  ? 1980 GLU A OE2   1 
ATOM   5300  N  N     . ALA A 1 1981 ? 179.734 178.772 131.214 1.00 42.93  ? 1981 ALA A N     1 
ATOM   5301  C  CA    . ALA A 1 1981 ? 180.851 178.693 130.279 1.00 39.13  ? 1981 ALA A CA    1 
ATOM   5302  C  C     . ALA A 1 1981 ? 180.359 178.529 128.846 1.00 45.48  ? 1981 ALA A C     1 
ATOM   5303  O  O     . ALA A 1 1981 ? 180.913 179.130 127.919 1.00 54.53  ? 1981 ALA A O     1 
ATOM   5304  C  CB    . ALA A 1 1981 ? 181.778 177.543 130.663 1.00 44.94  ? 1981 ALA A CB    1 
ATOM   5305  N  N     . LEU A 1 1982 ? 179.325 177.708 128.645 1.00 44.96  ? 1982 LEU A N     1 
ATOM   5306  C  CA    . LEU A 1 1982 ? 178.757 177.539 127.308 1.00 39.62  ? 1982 LEU A CA    1 
ATOM   5307  C  C     . LEU A 1 1982 ? 178.135 178.835 126.798 1.00 45.21  ? 1982 LEU A C     1 
ATOM   5308  O  O     . LEU A 1 1982 ? 178.327 179.207 125.635 1.00 52.52  ? 1982 LEU A O     1 
ATOM   5309  C  CB    . LEU A 1 1982 ? 177.722 176.416 127.312 1.00 35.71  ? 1982 LEU A CB    1 
ATOM   5310  C  CG    . LEU A 1 1982 ? 178.274 174.993 127.253 1.00 37.82  ? 1982 LEU A CG    1 
ATOM   5311  C  CD1   . LEU A 1 1982 ? 177.144 173.983 127.271 1.00 36.11  ? 1982 LEU A CD1   1 
ATOM   5312  C  CD2   . LEU A 1 1982 ? 179.142 174.809 126.022 1.00 43.20  ? 1982 LEU A CD2   1 
ATOM   5313  N  N     . ARG A 1 1983 ? 177.376 179.527 127.651 1.00 42.57  ? 1983 ARG A N     1 
ATOM   5314  C  CA    . ARG A 1 1983 ? 176.840 180.839 127.297 1.00 44.89  ? 1983 ARG A CA    1 
ATOM   5315  C  C     . ARG A 1 1983 ? 177.945 181.805 126.898 1.00 54.18  ? 1983 ARG A C     1 
ATOM   5316  O  O     . ARG A 1 1983 ? 177.738 182.661 126.031 1.00 59.56  ? 1983 ARG A O     1 
ATOM   5317  C  CB    . ARG A 1 1983 ? 176.043 181.414 128.469 1.00 43.28  ? 1983 ARG A CB    1 
ATOM   5318  C  CG    . ARG A 1 1983 ? 174.801 180.631 128.850 1.00 40.54  ? 1983 ARG A CG    1 
ATOM   5319  C  CD    . ARG A 1 1983 ? 173.723 180.742 127.793 1.00 46.48  ? 1983 ARG A CD    1 
ATOM   5320  N  NE    . ARG A 1 1983 ? 173.231 182.110 127.684 1.00 50.37  ? 1983 ARG A NE    1 
ATOM   5321  C  CZ    . ARG A 1 1983 ? 172.532 182.582 126.661 1.00 56.78  ? 1983 ARG A CZ    1 
ATOM   5322  N  NH1   . ARG A 1 1983 ? 172.220 181.820 125.627 1.00 50.89  ? 1983 ARG A NH1   1 
ATOM   5323  N  NH2   . ARG A 1 1983 ? 172.134 183.850 126.677 1.00 64.20  ? 1983 ARG A NH2   1 
ATOM   5324  N  N     . GLU A 1 1984 ? 179.122 181.684 127.515 1.00 58.61  ? 1984 GLU A N     1 
ATOM   5325  C  CA    . GLU A 1 1984 ? 180.242 182.548 127.163 1.00 61.80  ? 1984 GLU A CA    1 
ATOM   5326  C  C     . GLU A 1 1984 ? 180.753 182.316 125.745 1.00 67.47  ? 1984 GLU A C     1 
ATOM   5327  O  O     . GLU A 1 1984 ? 181.550 183.124 125.259 1.00 76.53  ? 1984 GLU A O     1 
ATOM   5328  C  CB    . GLU A 1 1984 ? 181.388 182.366 128.160 1.00 56.65  ? 1984 GLU A CB    1 
ATOM   5329  C  CG    . GLU A 1 1984 ? 181.091 182.911 129.547 1.00 56.28  ? 1984 GLU A CG    1 
ATOM   5330  C  CD    . GLU A 1 1984 ? 182.184 182.593 130.548 1.00 69.25  ? 1984 GLU A CD    1 
ATOM   5331  O  OE1   . GLU A 1 1984 ? 183.188 181.964 130.156 1.00 72.73  ? 1984 GLU A OE1   1 
ATOM   5332  O  OE2   . GLU A 1 1984 ? 182.036 182.968 131.729 1.00 70.07  ? 1984 GLU A OE2   1 
ATOM   5333  N  N     . HIS A 1 1985 ? 180.341 181.234 125.080 1.00 63.29  ? 1985 HIS A N     1 
ATOM   5334  C  CA    . HIS A 1 1985 ? 180.699 181.030 123.681 1.00 67.81  ? 1985 HIS A CA    1 
ATOM   5335  C  C     . HIS A 1 1985 ? 179.834 181.837 122.723 1.00 75.98  ? 1985 HIS A C     1 
ATOM   5336  O  O     . HIS A 1 1985 ? 180.198 181.973 121.550 1.00 84.84  ? 1985 HIS A O     1 
ATOM   5337  C  CB    . HIS A 1 1985 ? 180.590 179.550 123.300 1.00 60.55  ? 1985 HIS A CB    1 
ATOM   5338  C  CG    . HIS A 1 1985 ? 181.693 178.695 123.840 1.00 65.43  ? 1985 HIS A CG    1 
ATOM   5339  N  ND1   . HIS A 1 1985 ? 181.610 178.052 125.056 1.00 66.80  ? 1985 HIS A ND1   1 
ATOM   5340  C  CD2   . HIS A 1 1985 ? 182.898 178.364 123.321 1.00 63.57  ? 1985 HIS A CD2   1 
ATOM   5341  C  CE1   . HIS A 1 1985 ? 182.720 177.367 125.266 1.00 63.52  ? 1985 HIS A CE1   1 
ATOM   5342  N  NE2   . HIS A 1 1985 ? 183.519 177.541 124.228 1.00 61.64  ? 1985 HIS A NE2   1 
ATOM   5343  N  N     . SER A 1 1986 ? 178.704 182.369 123.185 1.00 77.47  ? 1986 SER A N     1 
ATOM   5344  C  CA    . SER A 1 1986 ? 177.721 182.977 122.299 1.00 81.18  ? 1986 SER A CA    1 
ATOM   5345  C  C     . SER A 1 1986 ? 177.919 184.473 122.090 1.00 95.06  ? 1986 SER A C     1 
ATOM   5346  O  O     . SER A 1 1986 ? 177.212 185.060 121.264 1.00 97.28  ? 1986 SER A O     1 
ATOM   5347  C  CB    . SER A 1 1986 ? 176.306 182.728 122.834 1.00 75.56  ? 1986 SER A CB    1 
ATOM   5348  O  OG    . SER A 1 1986 ? 176.041 183.530 123.971 1.00 77.41  ? 1986 SER A OG    1 
ATOM   5349  N  N     . ASN A 1 1987 ? 178.841 185.103 122.802 1.00 101.03 ? 1987 ASN A N     1 
ATOM   5350  C  CA    . ASN A 1 1987 ? 179.034 186.542 122.649 1.00 111.44 ? 1987 ASN A CA    1 
ATOM   5351  C  C     . ASN A 1 1987 ? 179.695 186.840 121.309 1.00 119.59 ? 1987 ASN A C     1 
ATOM   5352  O  O     . ASN A 1 1987 ? 180.784 186.318 121.035 1.00 117.01 ? 1987 ASN A O     1 
ATOM   5353  C  CB    . ASN A 1 1987 ? 179.868 187.096 123.800 1.00 110.86 ? 1987 ASN A CB    1 
ATOM   5354  C  CG    . ASN A 1 1987 ? 181.105 186.271 124.072 1.00 111.45 ? 1987 ASN A CG    1 
ATOM   5355  O  OD1   . ASN A 1 1987 ? 181.278 185.193 123.509 1.00 110.11 ? 1987 ASN A OD1   1 
ATOM   5356  N  ND2   . ASN A 1 1987 ? 181.976 186.775 124.939 1.00 112.52 ? 1987 ASN A ND2   1 
ATOM   5357  N  N     . PRO A 1 1988 ? 179.081 187.655 120.447 1.00 128.31 ? 1988 PRO A N     1 
ATOM   5358  C  CA    . PRO A 1 1988 ? 179.687 187.909 119.130 1.00 129.24 ? 1988 PRO A CA    1 
ATOM   5359  C  C     . PRO A 1 1988 ? 180.998 188.671 119.200 1.00 128.83 ? 1988 PRO A C     1 
ATOM   5360  O  O     . PRO A 1 1988 ? 181.852 188.487 118.325 1.00 125.43 ? 1988 PRO A O     1 
ATOM   5361  C  CB    . PRO A 1 1988 ? 178.603 188.712 118.399 1.00 127.83 ? 1988 PRO A CB    1 
ATOM   5362  C  CG    . PRO A 1 1988 ? 177.852 189.397 119.490 1.00 125.92 ? 1988 PRO A CG    1 
ATOM   5363  C  CD    . PRO A 1 1988 ? 177.863 188.455 120.665 1.00 124.34 ? 1988 PRO A CD    1 
ATOM   5364  N  N     . ASN A 1 1989 ? 181.187 189.518 120.213 1.00 129.31 ? 1989 ASN A N     1 
ATOM   5365  C  CA    . ASN A 1 1989 ? 182.409 190.307 120.324 1.00 132.03 ? 1989 ASN A CA    1 
ATOM   5366  C  C     . ASN A 1 1989 ? 183.621 189.473 120.712 1.00 133.88 ? 1989 ASN A C     1 
ATOM   5367  O  O     . ASN A 1 1989 ? 184.744 189.988 120.664 1.00 133.57 ? 1989 ASN A O     1 
ATOM   5368  C  CB    . ASN A 1 1989 ? 182.217 191.430 121.344 1.00 131.84 ? 1989 ASN A CB    1 
ATOM   5369  C  CG    . ASN A 1 1989 ? 181.848 190.910 122.719 1.00 131.63 ? 1989 ASN A CG    1 
ATOM   5370  O  OD1   . ASN A 1 1989 ? 180.805 190.279 122.898 1.00 125.79 ? 1989 ASN A OD1   1 
ATOM   5371  N  ND2   . ASN A 1 1989 ? 182.705 191.169 123.699 1.00 131.97 ? 1989 ASN A ND2   1 
ATOM   5372  N  N     . TYR A 1 1990 ? 183.426 188.214 121.096 1.00 131.98 ? 1990 TYR A N     1 
ATOM   5373  C  CA    . TYR A 1 1990 ? 184.536 187.384 121.538 1.00 131.52 ? 1990 TYR A CA    1 
ATOM   5374  C  C     . TYR A 1 1990 ? 185.477 187.075 120.381 1.00 134.59 ? 1990 TYR A C     1 
ATOM   5375  O  O     . TYR A 1 1990 ? 185.049 186.908 119.235 1.00 132.09 ? 1990 TYR A O     1 
ATOM   5376  C  CB    . TYR A 1 1990 ? 184.012 186.087 122.151 1.00 125.38 ? 1990 TYR A CB    1 
ATOM   5377  C  CG    . TYR A 1 1990 ? 185.029 185.357 122.993 1.00 127.42 ? 1990 TYR A CG    1 
ATOM   5378  C  CD1   . TYR A 1 1990 ? 185.320 185.778 124.283 1.00 125.94 ? 1990 TYR A CD1   1 
ATOM   5379  C  CD2   . TYR A 1 1990 ? 185.698 184.246 122.500 1.00 129.44 ? 1990 TYR A CD2   1 
ATOM   5380  C  CE1   . TYR A 1 1990 ? 186.251 185.114 125.059 1.00 125.22 ? 1990 TYR A CE1   1 
ATOM   5381  C  CE2   . TYR A 1 1990 ? 186.628 183.577 123.267 1.00 129.87 ? 1990 TYR A CE2   1 
ATOM   5382  C  CZ    . TYR A 1 1990 ? 186.902 184.014 124.545 1.00 127.02 ? 1990 TYR A CZ    1 
ATOM   5383  O  OH    . TYR A 1 1990 ? 187.830 183.347 125.311 1.00 116.92 ? 1990 TYR A OH    1 
ATOM   5384  N  N     . ASP A 1 1991 ? 186.770 186.998 120.689 1.00 138.38 ? 1991 ASP A N     1 
ATOM   5385  C  CA    . ASP A 1 1991 ? 187.789 186.702 119.687 1.00 138.89 ? 1991 ASP A CA    1 
ATOM   5386  C  C     . ASP A 1 1991 ? 187.795 185.202 119.419 1.00 135.06 ? 1991 ASP A C     1 
ATOM   5387  O  O     . ASP A 1 1991 ? 188.193 184.411 120.280 1.00 132.08 ? 1991 ASP A O     1 
ATOM   5388  C  CB    . ASP A 1 1991 ? 189.156 187.185 120.163 1.00 141.21 ? 1991 ASP A CB    1 
ATOM   5389  C  CG    . ASP A 1 1991 ? 190.275 186.783 119.224 1.00 142.74 ? 1991 ASP A CG    1 
ATOM   5390  O  OD1   . ASP A 1 1991 ? 190.254 187.215 118.052 1.00 143.61 ? 1991 ASP A OD1   1 
ATOM   5391  O  OD2   . ASP A 1 1991 ? 191.177 186.035 119.657 1.00 140.52 ? 1991 ASP A OD2   1 
ATOM   5392  N  N     . LYS A 1 1992 ? 187.351 184.808 118.224 1.00 133.05 ? 1992 LYS A N     1 
ATOM   5393  C  CA    . LYS A 1 1992 ? 187.254 183.394 117.885 1.00 135.74 ? 1992 LYS A CA    1 
ATOM   5394  C  C     . LYS A 1 1992 ? 188.596 182.771 117.527 1.00 139.12 ? 1992 LYS A C     1 
ATOM   5395  O  O     . LYS A 1 1992 ? 188.705 181.540 117.519 1.00 138.45 ? 1992 LYS A O     1 
ATOM   5396  C  CB    . LYS A 1 1992 ? 186.270 183.199 116.729 1.00 136.16 ? 1992 LYS A CB    1 
ATOM   5397  C  CG    . LYS A 1 1992 ? 184.866 183.702 117.024 1.00 134.05 ? 1992 LYS A CG    1 
ATOM   5398  C  CD    . LYS A 1 1992 ? 184.356 183.160 118.350 1.00 131.90 ? 1992 LYS A CD    1 
ATOM   5399  C  CE    . LYS A 1 1992 ? 183.010 183.759 118.713 1.00 127.23 ? 1992 LYS A CE    1 
ATOM   5400  N  NZ    . LYS A 1 1992 ? 182.502 183.226 120.007 1.00 123.69 ? 1992 LYS A NZ    1 
ATOM   5401  N  N     . THR A 1 1993 ? 189.612 183.583 117.222 1.00 141.41 ? 1993 THR A N     1 
ATOM   5402  C  CA    . THR A 1 1993 ? 190.928 183.030 116.914 1.00 139.44 ? 1993 THR A CA    1 
ATOM   5403  C  C     . THR A 1 1993 ? 191.518 182.317 118.124 1.00 138.43 ? 1993 THR A C     1 
ATOM   5404  O  O     . THR A 1 1993 ? 192.066 181.215 118.001 1.00 135.73 ? 1993 THR A O     1 
ATOM   5405  C  CB    . THR A 1 1993 ? 191.868 184.134 116.433 1.00 138.90 ? 1993 THR A CB    1 
ATOM   5406  O  OG1   . THR A 1 1993 ? 192.105 185.063 117.499 1.00 141.08 ? 1993 THR A OG1   1 
ATOM   5407  C  CG2   . THR A 1 1993 ? 191.261 184.873 115.249 1.00 134.93 ? 1993 THR A CG2   1 
ATOM   5408  N  N     . SER A 1 1994 ? 191.415 182.930 119.301 1.00 139.16 ? 1994 SER A N     1 
ATOM   5409  C  CA    . SER A 1 1994 ? 191.839 182.326 120.559 1.00 138.52 ? 1994 SER A CA    1 
ATOM   5410  C  C     . SER A 1 1994 ? 190.639 182.324 121.496 1.00 134.24 ? 1994 SER A C     1 
ATOM   5411  O  O     . SER A 1 1994 ? 190.244 183.378 122.007 1.00 130.59 ? 1994 SER A O     1 
ATOM   5412  C  CB    . SER A 1 1994 ? 193.017 183.084 121.170 1.00 136.42 ? 1994 SER A CB    1 
ATOM   5413  O  OG    . SER A 1 1994 ? 194.103 183.161 120.264 1.00 130.68 ? 1994 SER A OG    1 
ATOM   5414  N  N     . ALA A 1 1995 ? 190.064 181.146 121.725 1.00 133.04 ? 1995 ALA A N     1 
ATOM   5415  C  CA    . ALA A 1 1995 ? 188.842 180.998 122.515 1.00 125.92 ? 1995 ALA A CA    1 
ATOM   5416  C  C     . ALA A 1 1995 ? 189.056 179.961 123.610 1.00 116.55 ? 1995 ALA A C     1 
ATOM   5417  O  O     . ALA A 1 1995 ? 188.540 178.839 123.533 1.00 112.49 ? 1995 ALA A O     1 
ATOM   5418  C  CB    . ALA A 1 1995 ? 187.662 180.615 121.621 1.00 120.45 ? 1995 ALA A CB    1 
ATOM   5419  N  N     . PRO A 1 1996 ? 189.818 180.305 124.654 1.00 113.50 ? 1996 PRO A N     1 
ATOM   5420  C  CA    . PRO A 1 1996 ? 190.018 179.367 125.776 1.00 101.13 ? 1996 PRO A CA    1 
ATOM   5421  C  C     . PRO A 1 1996 ? 188.973 179.546 126.874 1.00 91.03  ? 1996 PRO A C     1 
ATOM   5422  O  O     . PRO A 1 1996 ? 189.268 179.929 128.013 1.00 91.91  ? 1996 PRO A O     1 
ATOM   5423  C  CB    . PRO A 1 1996 ? 191.430 179.723 126.242 1.00 105.26 ? 1996 PRO A CB    1 
ATOM   5424  C  CG    . PRO A 1 1996 ? 191.523 181.205 125.999 1.00 110.53 ? 1996 PRO A CG    1 
ATOM   5425  C  CD    . PRO A 1 1996 ? 190.603 181.540 124.837 1.00 113.74 ? 1996 PRO A CD    1 
ATOM   5426  N  N     . ILE A 1 1997 ? 187.713 179.268 126.536 1.00 80.74  ? 1997 ILE A N     1 
ATOM   5427  C  CA    . ILE A 1 1997 ? 186.647 179.345 127.528 1.00 72.92  ? 1997 ILE A CA    1 
ATOM   5428  C  C     . ILE A 1 1997 ? 186.797 178.193 128.510 1.00 69.67  ? 1997 ILE A C     1 
ATOM   5429  O  O     . ILE A 1 1997 ? 186.855 177.022 128.115 1.00 75.38  ? 1997 ILE A O     1 
ATOM   5430  C  CB    . ILE A 1 1997 ? 185.266 179.326 126.857 1.00 70.72  ? 1997 ILE A CB    1 
ATOM   5431  C  CG1   . ILE A 1 1997 ? 185.062 180.564 125.978 1.00 80.36  ? 1997 ILE A CG1   1 
ATOM   5432  C  CG2   . ILE A 1 1997 ? 184.171 179.227 127.905 1.00 62.26  ? 1997 ILE A CG2   1 
ATOM   5433  C  CD1   . ILE A 1 1997 ? 185.514 180.397 124.545 1.00 90.84  ? 1997 ILE A CD1   1 
ATOM   5434  N  N     . THR A 1 1998 ? 186.860 178.521 129.797 1.00 66.23  ? 1998 THR A N     1 
ATOM   5435  C  CA    . THR A 1 1998 ? 187.096 177.537 130.841 1.00 59.47  ? 1998 THR A CA    1 
ATOM   5436  C  C     . THR A 1 1998 ? 186.089 177.725 131.966 1.00 56.16  ? 1998 THR A C     1 
ATOM   5437  O  O     . THR A 1 1998 ? 185.521 178.804 132.152 1.00 62.01  ? 1998 THR A O     1 
ATOM   5438  C  CB    . THR A 1 1998 ? 188.522 177.635 131.405 1.00 66.57  ? 1998 THR A CB    1 
ATOM   5439  O  OG1   . THR A 1 1998 ? 188.719 178.928 131.990 1.00 72.18  ? 1998 THR A OG1   1 
ATOM   5440  C  CG2   . THR A 1 1998 ? 189.555 177.416 130.309 1.00 67.04  ? 1998 THR A CG2   1 
ATOM   5441  N  N     . CYS A 1 1999 ? 185.876 176.649 132.715 1.00 56.27  ? 1999 CYS A N     1 
ATOM   5442  C  CA    . CYS A 1 1999 ? 184.990 176.650 133.867 1.00 60.65  ? 1999 CYS A CA    1 
ATOM   5443  C  C     . CYS A 1 1999 ? 185.727 176.082 135.071 1.00 66.11  ? 1999 CYS A C     1 
ATOM   5444  O  O     . CYS A 1 1999 ? 186.724 175.369 134.938 1.00 68.72  ? 1999 CYS A O     1 
ATOM   5445  C  CB    . CYS A 1 1999 ? 183.711 175.846 133.599 1.00 57.23  ? 1999 CYS A CB    1 
ATOM   5446  S  SG    . CYS A 1 1999 ? 183.986 174.101 133.253 1.00 59.97  ? 1999 CYS A SG    1 
ATOM   5447  N  N     . GLU A 1 2000 ? 185.229 176.415 136.259 1.00 67.47  ? 2000 GLU A N     1 
ATOM   5448  C  CA    . GLU A 1 2000 ? 185.857 175.996 137.512 1.00 70.88  ? 2000 GLU A CA    1 
ATOM   5449  C  C     . GLU A 1 2000 ? 185.281 174.638 137.893 1.00 69.15  ? 2000 GLU A C     1 
ATOM   5450  O  O     . GLU A 1 2000 ? 184.217 174.535 138.505 1.00 66.54  ? 2000 GLU A O     1 
ATOM   5451  C  CB    . GLU A 1 2000 ? 185.643 177.055 138.589 1.00 80.19  ? 2000 GLU A CB    1 
ATOM   5452  C  CG    . GLU A 1 2000 ? 186.438 176.865 139.878 1.00 81.53  ? 2000 GLU A CG    1 
ATOM   5453  C  CD    . GLU A 1 2000 ? 185.771 175.926 140.864 1.00 89.21  ? 2000 GLU A CD    1 
ATOM   5454  O  OE1   . GLU A 1 2000 ? 184.525 175.840 140.857 1.00 91.37  ? 2000 GLU A OE1   1 
ATOM   5455  O  OE2   . GLU A 1 2000 ? 186.489 175.282 141.655 1.00 89.30  ? 2000 GLU A OE2   1 
ATOM   5456  N  N     . LEU A 1 2001 ? 185.988 173.578 137.507 1.00 67.94  ? 2001 LEU A N     1 
ATOM   5457  C  CA    . LEU A 1 2001 ? 185.588 172.207 137.797 1.00 70.75  ? 2001 LEU A CA    1 
ATOM   5458  C  C     . LEU A 1 2001 ? 186.726 171.499 138.515 1.00 70.86  ? 2001 LEU A C     1 
ATOM   5459  O  O     . LEU A 1 2001 ? 187.886 171.625 138.112 1.00 71.17  ? 2001 LEU A O     1 
ATOM   5460  C  CB    . LEU A 1 2001 ? 185.222 171.444 136.521 1.00 64.74  ? 2001 LEU A CB    1 
ATOM   5461  C  CG    . LEU A 1 2001 ? 183.852 171.702 135.897 1.00 57.58  ? 2001 LEU A CG    1 
ATOM   5462  C  CD1   . LEU A 1 2001 ? 183.642 170.782 134.715 1.00 49.41  ? 2001 LEU A CD1   1 
ATOM   5463  C  CD2   . LEU A 1 2001 ? 182.754 171.504 136.924 1.00 53.16  ? 2001 LEU A CD2   1 
ATOM   5464  N  N     . LEU A 1 2002 ? 186.388 170.759 139.572 1.00 72.99  ? 2002 LEU A N     1 
ATOM   5465  C  CA    . LEU A 1 2002 ? 187.376 170.054 140.390 1.00 75.00  ? 2002 LEU A CA    1 
ATOM   5466  C  C     . LEU A 1 2002 ? 188.465 171.006 140.877 1.00 81.24  ? 2002 LEU A C     1 
ATOM   5467  O  O     . LEU A 1 2002 ? 189.637 170.638 140.983 1.00 83.32  ? 2002 LEU A O     1 
ATOM   5468  C  CB    . LEU A 1 2002 ? 187.984 168.872 139.634 1.00 66.65  ? 2002 LEU A CB    1 
ATOM   5469  C  CG    . LEU A 1 2002 ? 187.040 167.713 139.318 1.00 59.89  ? 2002 LEU A CG    1 
ATOM   5470  C  CD1   . LEU A 1 2002 ? 187.814 166.535 138.753 1.00 58.75  ? 2002 LEU A CD1   1 
ATOM   5471  C  CD2   . LEU A 1 2002 ? 186.265 167.305 140.560 1.00 56.78  ? 2002 LEU A CD2   1 
ATOM   5472  N  N     . ASN A 1 2003 ? 188.066 172.245 141.171 1.00 81.01  ? 2003 ASN A N     1 
ATOM   5473  C  CA    . ASN A 1 2003 ? 188.978 173.295 141.624 1.00 79.84  ? 2003 ASN A CA    1 
ATOM   5474  C  C     . ASN A 1 2003 ? 190.109 173.519 140.619 1.00 81.39  ? 2003 ASN A C     1 
ATOM   5475  O  O     . ASN A 1 2003 ? 191.265 173.728 140.991 1.00 83.64  ? 2003 ASN A O     1 
ATOM   5476  C  CB    . ASN A 1 2003 ? 189.528 172.982 143.019 1.00 87.39  ? 2003 ASN A CB    1 
ATOM   5477  C  CG    . ASN A 1 2003 ? 190.235 174.167 143.648 1.00 95.85  ? 2003 ASN A CG    1 
ATOM   5478  O  OD1   . ASN A 1 2003 ? 189.771 175.303 143.555 1.00 100.07 ? 2003 ASN A OD1   1 
ATOM   5479  N  ND2   . ASN A 1 2003 ? 191.366 173.906 144.294 1.00 96.56  ? 2003 ASN A ND2   1 
ATOM   5480  N  N     . LYS A 1 2004 ? 189.777 173.470 139.330 1.00 82.24  ? 2004 LYS A N     1 
ATOM   5481  C  CA    . LYS A 1 2004 ? 190.741 173.815 138.297 1.00 77.65  ? 2004 LYS A CA    1 
ATOM   5482  C  C     . LYS A 1 2004 ? 190.001 174.376 137.092 1.00 74.35  ? 2004 LYS A C     1 
ATOM   5483  O  O     . LYS A 1 2004 ? 188.786 174.209 136.947 1.00 74.04  ? 2004 LYS A O     1 
ATOM   5484  C  CB    . LYS A 1 2004 ? 191.603 172.616 137.876 1.00 72.66  ? 2004 LYS A CB    1 
ATOM   5485  C  CG    . LYS A 1 2004 ? 190.843 171.486 137.208 1.00 76.63  ? 2004 LYS A CG    1 
ATOM   5486  C  CD    . LYS A 1 2004 ? 191.763 170.322 136.876 1.00 85.47  ? 2004 LYS A CD    1 
ATOM   5487  C  CE    . LYS A 1 2004 ? 191.010 169.200 136.176 1.00 74.20  ? 2004 LYS A CE    1 
ATOM   5488  N  NZ    . LYS A 1 2004 ? 190.019 168.540 137.066 1.00 70.20  ? 2004 LYS A NZ    1 
ATOM   5489  N  N     . GLN A 1 2005 ? 190.755 175.051 136.227 1.00 68.22  ? 2005 GLN A N     1 
ATOM   5490  C  CA    . GLN A 1 2005 ? 190.201 175.650 135.018 1.00 68.59  ? 2005 GLN A CA    1 
ATOM   5491  C  C     . GLN A 1 2005 ? 190.158 174.593 133.922 1.00 66.21  ? 2005 GLN A C     1 
ATOM   5492  O  O     . GLN A 1 2005 ? 191.194 174.238 133.351 1.00 67.74  ? 2005 GLN A O     1 
ATOM   5493  C  CB    . GLN A 1 2005 ? 191.035 176.853 134.589 1.00 70.22  ? 2005 GLN A CB    1 
ATOM   5494  C  CG    . GLN A 1 2005 ? 190.871 178.076 135.475 1.00 76.28  ? 2005 GLN A CG    1 
ATOM   5495  C  CD    . GLN A 1 2005 ? 189.434 178.545 135.568 1.00 73.83  ? 2005 GLN A CD    1 
ATOM   5496  O  OE1   . GLN A 1 2005 ? 188.804 178.853 134.558 1.00 72.69  ? 2005 GLN A OE1   1 
ATOM   5497  N  NE2   . GLN A 1 2005 ? 188.909 178.604 136.786 1.00 68.70  ? 2005 GLN A NE2   1 
ATOM   5498  N  N     . VAL A 1 2006 ? 188.963 174.096 133.621 1.00 61.86  ? 2006 VAL A N     1 
ATOM   5499  C  CA    . VAL A 1 2006 ? 188.756 173.063 132.615 1.00 56.81  ? 2006 VAL A CA    1 
ATOM   5500  C  C     . VAL A 1 2006 ? 188.211 173.733 131.365 1.00 58.24  ? 2006 VAL A C     1 
ATOM   5501  O  O     . VAL A 1 2006 ? 187.181 174.416 131.420 1.00 64.99  ? 2006 VAL A O     1 
ATOM   5502  C  CB    . VAL A 1 2006 ? 187.796 171.973 133.113 1.00 55.98  ? 2006 VAL A CB    1 
ATOM   5503  C  CG1   . VAL A 1 2006 ? 187.430 171.035 131.979 1.00 55.95  ? 2006 VAL A CG1   1 
ATOM   5504  C  CG2   . VAL A 1 2006 ? 188.417 171.210 134.268 1.00 61.32  ? 2006 VAL A CG2   1 
ATOM   5505  N  N     . LYS A 1 2007 ? 188.902 173.552 130.244 1.00 57.89  ? 2007 LYS A N     1 
ATOM   5506  C  CA    . LYS A 1 2007 ? 188.431 174.105 128.983 1.00 58.59  ? 2007 LYS A CA    1 
ATOM   5507  C  C     . LYS A 1 2007 ? 187.152 173.405 128.547 1.00 55.91  ? 2007 LYS A C     1 
ATOM   5508  O  O     . LYS A 1 2007 ? 187.039 172.179 128.619 1.00 56.62  ? 2007 LYS A O     1 
ATOM   5509  C  CB    . LYS A 1 2007 ? 189.504 173.965 127.906 1.00 60.71  ? 2007 LYS A CB    1 
ATOM   5510  C  CG    . LYS A 1 2007 ? 189.375 174.964 126.771 1.00 67.55  ? 2007 LYS A CG    1 
ATOM   5511  C  CD    . LYS A 1 2007 ? 190.437 174.744 125.706 1.00 78.58  ? 2007 LYS A CD    1 
ATOM   5512  C  CE    . LYS A 1 2007 ? 191.793 174.438 126.321 1.00 77.11  ? 2007 LYS A CE    1 
ATOM   5513  N  NZ    . LYS A 1 2007 ? 192.354 175.609 127.050 1.00 77.20  ? 2007 LYS A NZ    1 
ATOM   5514  N  N     . VAL A 1 2008 ? 186.184 174.192 128.089 1.00 49.99  ? 2008 VAL A N     1 
ATOM   5515  C  CA    . VAL A 1 2008 ? 184.878 173.688 127.681 1.00 47.54  ? 2008 VAL A CA    1 
ATOM   5516  C  C     . VAL A 1 2008 ? 184.819 173.704 126.163 1.00 54.20  ? 2008 VAL A C     1 
ATOM   5517  O  O     . VAL A 1 2008 ? 184.939 174.767 125.541 1.00 57.73  ? 2008 VAL A O     1 
ATOM   5518  C  CB    . VAL A 1 2008 ? 183.735 174.517 128.283 1.00 46.79  ? 2008 VAL A CB    1 
ATOM   5519  C  CG1   . VAL A 1 2008 ? 182.398 173.865 127.988 1.00 42.22  ? 2008 VAL A CG1   1 
ATOM   5520  C  CG2   . VAL A 1 2008 ? 183.930 174.673 129.772 1.00 51.03  ? 2008 VAL A CG2   1 
ATOM   5521  N  N     . SER A 1 2009 ? 184.641 172.531 125.569 1.00 50.19  ? 2009 SER A N     1 
ATOM   5522  C  CA    . SER A 1 2009 ? 184.467 172.459 124.127 1.00 40.42  ? 2009 SER A CA    1 
ATOM   5523  C  C     . SER A 1 2009 ? 183.074 172.955 123.749 1.00 45.54  ? 2009 SER A C     1 
ATOM   5524  O  O     . SER A 1 2009 ? 182.103 172.675 124.455 1.00 43.07  ? 2009 SER A O     1 
ATOM   5525  C  CB    . SER A 1 2009 ? 184.662 171.031 123.632 1.00 34.29  ? 2009 SER A CB    1 
ATOM   5526  O  OG    . SER A 1 2009 ? 183.790 170.146 124.307 1.00 37.87  ? 2009 SER A OG    1 
ATOM   5527  N  N     . PRO A 1 2010 ? 182.949 173.700 122.648 1.00 49.00  ? 2010 PRO A N     1 
ATOM   5528  C  CA    . PRO A 1 2010 ? 181.629 174.217 122.262 1.00 47.24  ? 2010 PRO A CA    1 
ATOM   5529  C  C     . PRO A 1 2010 ? 180.638 173.136 121.874 1.00 46.24  ? 2010 PRO A C     1 
ATOM   5530  O  O     . PRO A 1 2010 ? 179.432 173.409 121.844 1.00 45.58  ? 2010 PRO A O     1 
ATOM   5531  C  CB    . PRO A 1 2010 ? 181.946 175.134 121.074 1.00 51.47  ? 2010 PRO A CB    1 
ATOM   5532  C  CG    . PRO A 1 2010 ? 183.228 174.607 120.528 1.00 47.47  ? 2010 PRO A CG    1 
ATOM   5533  C  CD    . PRO A 1 2010 ? 184.004 174.111 121.707 1.00 46.99  ? 2010 PRO A CD    1 
ATOM   5534  N  N     . ASP A 1 2011 ? 181.103 171.922 121.578 1.00 44.21  ? 2011 ASP A N     1 
ATOM   5535  C  CA    . ASP A 1 2011 ? 180.244 170.867 121.060 1.00 35.37  ? 2011 ASP A CA    1 
ATOM   5536  C  C     . ASP A 1 2011 ? 179.526 170.075 122.144 1.00 29.75  ? 2011 ASP A C     1 
ATOM   5537  O  O     . ASP A 1 2011 ? 178.638 169.283 121.816 1.00 34.38  ? 2011 ASP A O     1 
ATOM   5538  C  CB    . ASP A 1 2011 ? 181.066 169.911 120.196 1.00 41.98  ? 2011 ASP A CB    1 
ATOM   5539  C  CG    . ASP A 1 2011 ? 181.557 170.561 118.920 1.00 57.20  ? 2011 ASP A CG    1 
ATOM   5540  O  OD1   . ASP A 1 2011 ? 180.872 171.476 118.419 1.00 59.04  ? 2011 ASP A OD1   1 
ATOM   5541  O  OD2   . ASP A 1 2011 ? 182.628 170.161 118.420 1.00 64.80  ? 2011 ASP A OD2   1 
ATOM   5542  N  N     . MET A 1 2012 ? 179.880 170.255 123.412 1.00 29.10  ? 2012 MET A N     1 
ATOM   5543  C  CA    . MET A 1 2012 ? 179.230 169.484 124.457 1.00 25.86  ? 2012 MET A CA    1 
ATOM   5544  C  C     . MET A 1 2012 ? 177.951 170.177 124.916 1.00 28.64  ? 2012 MET A C     1 
ATOM   5545  O  O     . MET A 1 2012 ? 177.758 171.379 124.723 1.00 36.85  ? 2012 MET A O     1 
ATOM   5546  C  CB    . MET A 1 2012 ? 180.182 169.256 125.635 1.00 27.66  ? 2012 MET A CB    1 
ATOM   5547  C  CG    . MET A 1 2012 ? 180.685 170.499 126.354 1.00 32.63  ? 2012 MET A CG    1 
ATOM   5548  S  SD    . MET A 1 2012 ? 179.519 171.207 127.530 1.00 48.79  ? 2012 MET A SD    1 
ATOM   5549  C  CE    . MET A 1 2012 ? 179.556 169.963 128.815 1.00 30.87  ? 2012 MET A CE    1 
ATOM   5550  N  N     . ALA A 1 2013 ? 177.067 169.393 125.526 1.00 23.00  ? 2013 ALA A N     1 
ATOM   5551  C  CA    . ALA A 1 2013 ? 175.798 169.911 126.007 1.00 21.07  ? 2013 ALA A CA    1 
ATOM   5552  C  C     . ALA A 1 2013 ? 175.374 169.121 127.233 1.00 21.84  ? 2013 ALA A C     1 
ATOM   5553  O  O     . ALA A 1 2013 ? 175.802 167.984 127.442 1.00 24.72  ? 2013 ALA A O     1 
ATOM   5554  C  CB    . ALA A 1 2013 ? 174.715 169.845 124.926 1.00 20.19  ? 2013 ALA A CB    1 
ATOM   5555  N  N     . ILE A 1 2014 ? 174.527 169.742 128.046 1.00 22.79  ? 2014 ILE A N     1 
ATOM   5556  C  CA    . ILE A 1 2014 ? 173.975 169.122 129.243 1.00 23.34  ? 2014 ILE A CA    1 
ATOM   5557  C  C     . ILE A 1 2014 ? 172.460 169.144 129.128 1.00 23.40  ? 2014 ILE A C     1 
ATOM   5558  O  O     . ILE A 1 2014 ? 171.869 170.197 128.866 1.00 28.73  ? 2014 ILE A O     1 
ATOM   5559  C  CB    . ILE A 1 2014 ? 174.434 169.837 130.526 1.00 27.41  ? 2014 ILE A CB    1 
ATOM   5560  C  CG1   . ILE A 1 2014 ? 175.958 169.940 130.568 1.00 28.34  ? 2014 ILE A CG1   1 
ATOM   5561  C  CG2   . ILE A 1 2014 ? 173.919 169.109 131.753 1.00 28.98  ? 2014 ILE A CG2   1 
ATOM   5562  C  CD1   . ILE A 1 2014 ? 176.475 170.739 131.735 1.00 37.28  ? 2014 ILE A CD1   1 
ATOM   5563  N  N     . PHE A 1 2015 ? 171.838 167.987 129.319 1.00 20.55  ? 2015 PHE A N     1 
ATOM   5564  C  CA    . PHE A 1 2015 ? 170.391 167.857 129.294 1.00 21.10  ? 2015 PHE A CA    1 
ATOM   5565  C  C     . PHE A 1 2015 ? 169.907 167.363 130.646 1.00 25.88  ? 2015 PHE A C     1 
ATOM   5566  O  O     . PHE A 1 2015 ? 170.525 166.489 131.258 1.00 34.67  ? 2015 PHE A O     1 
ATOM   5567  C  CB    . PHE A 1 2015 ? 169.933 166.912 128.187 1.00 19.95  ? 2015 PHE A CB    1 
ATOM   5568  C  CG    . PHE A 1 2015 ? 170.127 167.465 126.809 1.00 19.09  ? 2015 PHE A CG    1 
ATOM   5569  C  CD1   . PHE A 1 2015 ? 171.377 167.475 126.221 1.00 19.24  ? 2015 PHE A CD1   1 
ATOM   5570  C  CD2   . PHE A 1 2015 ? 169.060 167.990 126.107 1.00 20.42  ? 2015 PHE A CD2   1 
ATOM   5571  C  CE1   . PHE A 1 2015 ? 171.555 167.991 124.959 1.00 20.22  ? 2015 PHE A CE1   1 
ATOM   5572  C  CE2   . PHE A 1 2015 ? 169.234 168.506 124.844 1.00 19.00  ? 2015 PHE A CE2   1 
ATOM   5573  C  CZ    . PHE A 1 2015 ? 170.482 168.505 124.270 1.00 18.56  ? 2015 PHE A CZ    1 
ATOM   5574  N  N     . ILE A 1 2016 ? 168.801 167.934 131.108 1.00 25.67  ? 2016 ILE A N     1 
ATOM   5575  C  CA    . ILE A 1 2016 ? 168.277 167.688 132.444 1.00 27.02  ? 2016 ILE A CA    1 
ATOM   5576  C  C     . ILE A 1 2016 ? 166.827 167.256 132.274 1.00 31.61  ? 2016 ILE A C     1 
ATOM   5577  O  O     . ILE A 1 2016 ? 165.926 168.095 132.175 1.00 41.61  ? 2016 ILE A O     1 
ATOM   5578  C  CB    . ILE A 1 2016 ? 168.397 168.922 133.346 1.00 26.87  ? 2016 ILE A CB    1 
ATOM   5579  C  CG1   . ILE A 1 2016 ? 169.865 169.188 133.673 1.00 28.41  ? 2016 ILE A CG1   1 
ATOM   5580  C  CG2   . ILE A 1 2016 ? 167.609 168.749 134.623 1.00 29.92  ? 2016 ILE A CG2   1 
ATOM   5581  C  CD1   . ILE A 1 2016 ? 170.072 170.266 134.700 1.00 31.42  ? 2016 ILE A CD1   1 
ATOM   5582  N  N     . THR A 1 2017 ? 166.598 165.949 132.219 1.00 26.05  ? 2017 THR A N     1 
ATOM   5583  C  CA    . THR A 1 2017 ? 165.247 165.418 132.137 1.00 23.70  ? 2017 THR A CA    1 
ATOM   5584  C  C     . THR A 1 2017 ? 164.607 165.442 133.518 1.00 30.53  ? 2017 THR A C     1 
ATOM   5585  O  O     . THR A 1 2017 ? 165.212 164.998 134.497 1.00 40.67  ? 2017 THR A O     1 
ATOM   5586  C  CB    . THR A 1 2017 ? 165.267 163.995 131.582 1.00 26.91  ? 2017 THR A CB    1 
ATOM   5587  O  OG1   . THR A 1 2017 ? 165.765 164.010 130.239 1.00 30.76  ? 2017 THR A OG1   1 
ATOM   5588  C  CG2   . THR A 1 2017 ? 163.881 163.397 131.599 1.00 31.83  ? 2017 THR A CG2   1 
ATOM   5589  N  N     . MET A 1 2018 ? 163.388 165.965 133.599 1.00 32.51  ? 2018 MET A N     1 
ATOM   5590  C  CA    . MET A 1 2018 ? 162.707 166.141 134.871 1.00 35.36  ? 2018 MET A CA    1 
ATOM   5591  C  C     . MET A 1 2018 ? 161.361 165.433 134.858 1.00 40.82  ? 2018 MET A C     1 
ATOM   5592  O  O     . MET A 1 2018 ? 160.797 165.153 133.798 1.00 40.98  ? 2018 MET A O     1 
ATOM   5593  C  CB    . MET A 1 2018 ? 162.503 167.623 135.193 1.00 37.07  ? 2018 MET A CB    1 
ATOM   5594  C  CG    . MET A 1 2018 ? 163.791 168.399 135.375 1.00 34.76  ? 2018 MET A CG    1 
ATOM   5595  S  SD    . MET A 1 2018 ? 164.448 168.228 137.040 1.00 55.40  ? 2018 MET A SD    1 
ATOM   5596  C  CE    . MET A 1 2018 ? 163.182 169.057 137.986 1.00 48.76  ? 2018 MET A CE    1 
ATOM   5597  N  N     . ASN A 1 2019 ? 160.858 165.136 136.052 1.00 47.06  ? 2019 ASN A N     1 
ATOM   5598  C  CA    . ASN A 1 2019 ? 159.548 164.511 136.230 1.00 51.91  ? 2019 ASN A CA    1 
ATOM   5599  C  C     . ASN A 1 2019 ? 158.696 165.390 137.134 1.00 59.38  ? 2019 ASN A C     1 
ATOM   5600  O  O     . ASN A 1 2019 ? 158.858 165.355 138.367 1.00 67.42  ? 2019 ASN A O     1 
ATOM   5601  C  CB    . ASN A 1 2019 ? 159.691 163.110 136.820 1.00 53.62  ? 2019 ASN A CB    1 
ATOM   5602  C  CG    . ASN A 1 2019 ? 158.398 162.324 136.780 1.00 58.15  ? 2019 ASN A CG    1 
ATOM   5603  O  OD1   . ASN A 1 2019 ? 157.367 162.824 136.335 1.00 60.98  ? 2019 ASN A OD1   1 
ATOM   5604  N  ND2   . ASN A 1 2019 ? 158.448 161.081 137.241 1.00 66.31  ? 2019 ASN A ND2   1 
ATOM   5605  N  N     . PRO A 1 2020 ? 157.789 166.195 136.582 1.00 60.53  ? 2020 PRO A N     1 
ATOM   5606  C  CA    . PRO A 1 2020 ? 156.949 167.048 137.433 1.00 66.66  ? 2020 PRO A CA    1 
ATOM   5607  C  C     . PRO A 1 2020 ? 156.023 166.207 138.300 1.00 71.74  ? 2020 PRO A C     1 
ATOM   5608  O  O     . PRO A 1 2020 ? 155.419 165.240 137.831 1.00 68.22  ? 2020 PRO A O     1 
ATOM   5609  C  CB    . PRO A 1 2020 ? 156.166 167.895 136.424 1.00 61.33  ? 2020 PRO A CB    1 
ATOM   5610  C  CG    . PRO A 1 2020 ? 156.149 167.073 135.183 1.00 53.71  ? 2020 PRO A CG    1 
ATOM   5611  C  CD    . PRO A 1 2020 ? 157.460 166.344 135.155 1.00 54.40  ? 2020 PRO A CD    1 
ATOM   5612  N  N     . GLY A 1 2021 ? 155.916 166.585 139.568 1.00 69.71  ? 2021 GLY A N     1 
ATOM   5613  C  CA    . GLY A 1 2021 ? 155.098 165.847 140.512 1.00 73.10  ? 2021 GLY A CA    1 
ATOM   5614  C  C     . GLY A 1 2021 ? 155.654 164.474 140.829 1.00 73.20  ? 2021 GLY A C     1 
ATOM   5615  O  O     . GLY A 1 2021 ? 156.810 164.178 140.527 1.00 66.85  ? 2021 GLY A O     1 
ATOM   5616  N  N     . SER A 1 2026 ? 160.397 169.143 141.658 1.00 69.22  ? 2026 SER A N     1 
ATOM   5617  C  CA    . SER A 1 2026 ? 159.419 169.159 140.577 1.00 75.52  ? 2026 SER A CA    1 
ATOM   5618  C  C     . SER A 1 2026 ? 159.909 170.000 139.404 1.00 76.01  ? 2026 SER A C     1 
ATOM   5619  O  O     . SER A 1 2026 ? 159.846 169.572 138.252 1.00 73.04  ? 2026 SER A O     1 
ATOM   5620  C  CB    . SER A 1 2026 ? 158.075 169.689 141.077 1.00 80.21  ? 2026 SER A CB    1 
ATOM   5621  O  OG    . SER A 1 2026 ? 157.548 168.858 142.097 1.00 96.01  ? 2026 SER A OG    1 
ATOM   5622  N  N     . ASN A 1 2027 ? 160.398 171.196 139.705 1.00 75.18  ? 2027 ASN A N     1 
ATOM   5623  C  CA    . ASN A 1 2027 ? 160.888 172.134 138.706 1.00 66.12  ? 2027 ASN A CA    1 
ATOM   5624  C  C     . ASN A 1 2027 ? 162.405 172.250 138.811 1.00 59.00  ? 2027 ASN A C     1 
ATOM   5625  O  O     . ASN A 1 2027 ? 163.029 171.732 139.739 1.00 62.41  ? 2027 ASN A O     1 
ATOM   5626  C  CB    . ASN A 1 2027 ? 160.222 173.503 138.871 1.00 69.96  ? 2027 ASN A CB    1 
ATOM   5627  C  CG    . ASN A 1 2027 ? 159.865 174.139 137.545 1.00 76.61  ? 2027 ASN A CG    1 
ATOM   5628  O  OD1   . ASN A 1 2027 ? 160.655 174.118 136.601 1.00 73.85  ? 2027 ASN A OD1   1 
ATOM   5629  N  ND2   . ASN A 1 2027 ? 158.670 174.712 137.466 1.00 76.18  ? 2027 ASN A ND2   1 
ATOM   5630  N  N     . LEU A 1 2028 ? 162.994 172.942 137.840 1.00 53.26  ? 2028 LEU A N     1 
ATOM   5631  C  CA    . LEU A 1 2028 ? 164.436 173.110 137.806 1.00 50.19  ? 2028 LEU A CA    1 
ATOM   5632  C  C     . LEU A 1 2028 ? 164.916 173.888 139.028 1.00 50.66  ? 2028 LEU A C     1 
ATOM   5633  O  O     . LEU A 1 2028 ? 164.175 174.701 139.587 1.00 53.50  ? 2028 LEU A O     1 
ATOM   5634  C  CB    . LEU A 1 2028 ? 164.858 173.847 136.539 1.00 43.13  ? 2028 LEU A CB    1 
ATOM   5635  C  CG    . LEU A 1 2028 ? 164.952 173.055 135.239 1.00 39.74  ? 2028 LEU A CG    1 
ATOM   5636  C  CD1   . LEU A 1 2028 ? 165.118 174.002 134.071 1.00 40.22  ? 2028 LEU A CD1   1 
ATOM   5637  C  CD2   . LEU A 1 2028 ? 166.116 172.091 135.303 1.00 37.42  ? 2028 LEU A CD2   1 
ATOM   5638  N  N     . PRO A 1 2029 ? 166.147 173.643 139.474 1.00 49.11  ? 2029 PRO A N     1 
ATOM   5639  C  CA    . PRO A 1 2029 ? 166.722 174.483 140.527 1.00 45.74  ? 2029 PRO A CA    1 
ATOM   5640  C  C     . PRO A 1 2029 ? 166.779 175.935 140.081 1.00 45.76  ? 2029 PRO A C     1 
ATOM   5641  O  O     . PRO A 1 2029 ? 166.957 176.237 138.899 1.00 46.45  ? 2029 PRO A O     1 
ATOM   5642  C  CB    . PRO A 1 2029 ? 168.123 173.896 140.724 1.00 43.92  ? 2029 PRO A CB    1 
ATOM   5643  C  CG    . PRO A 1 2029 ? 168.002 172.485 140.270 1.00 42.22  ? 2029 PRO A CG    1 
ATOM   5644  C  CD    . PRO A 1 2029 ? 167.016 172.503 139.139 1.00 42.75  ? 2029 PRO A CD    1 
ATOM   5645  N  N     . ASP A 1 2030 ? 166.614 176.838 141.050 1.00 50.73  ? 2030 ASP A N     1 
ATOM   5646  C  CA    . ASP A 1 2030 ? 166.457 178.254 140.733 1.00 54.58  ? 2030 ASP A CA    1 
ATOM   5647  C  C     . ASP A 1 2030 ? 167.649 178.808 139.964 1.00 51.49  ? 2030 ASP A C     1 
ATOM   5648  O  O     . ASP A 1 2030 ? 167.497 179.759 139.189 1.00 49.23  ? 2030 ASP A O     1 
ATOM   5649  C  CB    . ASP A 1 2030 ? 166.237 179.053 142.017 1.00 62.02  ? 2030 ASP A CB    1 
ATOM   5650  C  CG    . ASP A 1 2030 ? 164.898 178.761 142.663 1.00 77.15  ? 2030 ASP A CG    1 
ATOM   5651  O  OD1   . ASP A 1 2030 ? 163.943 178.423 141.932 1.00 80.23  ? 2030 ASP A OD1   1 
ATOM   5652  O  OD2   . ASP A 1 2030 ? 164.799 178.869 143.903 1.00 86.59  ? 2030 ASP A OD2   1 
ATOM   5653  N  N     . ASN A 1 2031 ? 168.837 178.237 140.160 1.00 47.20  ? 2031 ASN A N     1 
ATOM   5654  C  CA    . ASN A 1 2031 ? 170.010 178.709 139.435 1.00 46.57  ? 2031 ASN A CA    1 
ATOM   5655  C  C     . ASN A 1 2031 ? 170.024 178.238 137.986 1.00 45.95  ? 2031 ASN A C     1 
ATOM   5656  O  O     . ASN A 1 2031 ? 170.610 178.909 137.129 1.00 46.35  ? 2031 ASN A O     1 
ATOM   5657  C  CB    . ASN A 1 2031 ? 171.286 178.263 140.150 1.00 43.70  ? 2031 ASN A CB    1 
ATOM   5658  C  CG    . ASN A 1 2031 ? 171.328 176.770 140.395 1.00 46.35  ? 2031 ASN A CG    1 
ATOM   5659  O  OD1   . ASN A 1 2031 ? 170.425 176.040 139.997 1.00 54.53  ? 2031 ASN A OD1   1 
ATOM   5660  N  ND2   . ASN A 1 2031 ? 172.384 176.308 141.050 1.00 47.46  ? 2031 ASN A ND2   1 
ATOM   5661  N  N     . LEU A 1 2032 ? 169.397 177.100 137.691 1.00 41.90  ? 2032 LEU A N     1 
ATOM   5662  C  CA    . LEU A 1 2032 ? 169.381 176.539 136.347 1.00 37.41  ? 2032 LEU A CA    1 
ATOM   5663  C  C     . LEU A 1 2032 ? 168.145 176.922 135.547 1.00 39.79  ? 2032 LEU A C     1 
ATOM   5664  O  O     . LEU A 1 2032 ? 168.043 176.541 134.378 1.00 41.93  ? 2032 LEU A O     1 
ATOM   5665  C  CB    . LEU A 1 2032 ? 169.488 175.013 136.410 1.00 31.96  ? 2032 LEU A CB    1 
ATOM   5666  C  CG    . LEU A 1 2032 ? 170.729 174.441 137.089 1.00 35.73  ? 2032 LEU A CG    1 
ATOM   5667  C  CD1   . LEU A 1 2032 ? 170.633 172.935 137.174 1.00 33.87  ? 2032 LEU A CD1   1 
ATOM   5668  C  CD2   . LEU A 1 2032 ? 171.972 174.857 136.337 1.00 36.72  ? 2032 LEU A CD2   1 
ATOM   5669  N  N     . LYS A 1 2033 ? 167.204 177.655 136.142 1.00 43.11  ? 2033 LYS A N     1 
ATOM   5670  C  CA    . LYS A 1 2033 ? 165.968 177.982 135.437 1.00 39.66  ? 2033 LYS A CA    1 
ATOM   5671  C  C     . LYS A 1 2033 ? 166.228 178.887 134.239 1.00 43.33  ? 2033 LYS A C     1 
ATOM   5672  O  O     . LYS A 1 2033 ? 165.629 178.700 133.174 1.00 49.46  ? 2033 LYS A O     1 
ATOM   5673  C  CB    . LYS A 1 2033 ? 164.973 178.627 136.398 1.00 42.69  ? 2033 LYS A CB    1 
ATOM   5674  C  CG    . LYS A 1 2033 ? 164.209 177.625 137.243 1.00 50.82  ? 2033 LYS A CG    1 
ATOM   5675  C  CD    . LYS A 1 2033 ? 163.220 178.311 138.163 1.00 55.12  ? 2033 LYS A CD    1 
ATOM   5676  C  CE    . LYS A 1 2033 ? 162.373 177.296 138.907 1.00 59.86  ? 2033 LYS A CE    1 
ATOM   5677  N  NZ    . LYS A 1 2033 ? 161.527 177.933 139.951 1.00 62.64  ? 2033 LYS A NZ    1 
ATOM   5678  N  N     . LYS A 1 2034 ? 167.113 179.868 134.388 1.00 43.72  ? 2034 LYS A N     1 
ATOM   5679  C  CA    . LYS A 1 2034 ? 167.410 180.806 133.314 1.00 45.80  ? 2034 LYS A CA    1 
ATOM   5680  C  C     . LYS A 1 2034 ? 168.440 180.276 132.328 1.00 42.09  ? 2034 LYS A C     1 
ATOM   5681  O  O     . LYS A 1 2034 ? 168.708 180.939 131.321 1.00 41.04  ? 2034 LYS A O     1 
ATOM   5682  C  CB    . LYS A 1 2034 ? 167.899 182.136 133.893 1.00 51.56  ? 2034 LYS A CB    1 
ATOM   5683  C  CG    . LYS A 1 2034 ? 166.832 182.923 134.631 1.00 61.60  ? 2034 LYS A CG    1 
ATOM   5684  C  CD    . LYS A 1 2034 ? 167.408 184.193 135.232 1.00 63.96  ? 2034 LYS A CD    1 
ATOM   5685  C  CE    . LYS A 1 2034 ? 167.758 185.198 134.148 1.00 72.43  ? 2034 LYS A CE    1 
ATOM   5686  N  NZ    . LYS A 1 2034 ? 166.545 185.723 133.461 1.00 68.96  ? 2034 LYS A NZ    1 
ATOM   5687  N  N     . LEU A 1 2035 ? 169.024 179.109 132.590 1.00 39.31  ? 2035 LEU A N     1 
ATOM   5688  C  CA    . LEU A 1 2035 ? 170.031 178.532 131.715 1.00 32.25  ? 2035 LEU A CA    1 
ATOM   5689  C  C     . LEU A 1 2035 ? 169.521 177.360 130.891 1.00 34.24  ? 2035 LEU A C     1 
ATOM   5690  O  O     . LEU A 1 2035 ? 170.260 176.864 130.035 1.00 34.10  ? 2035 LEU A O     1 
ATOM   5691  C  CB    . LEU A 1 2035 ? 171.245 178.074 132.535 1.00 31.01  ? 2035 LEU A CB    1 
ATOM   5692  C  CG    . LEU A 1 2035 ? 172.160 179.164 133.089 1.00 30.35  ? 2035 LEU A CG    1 
ATOM   5693  C  CD1   . LEU A 1 2035 ? 173.295 178.545 133.877 1.00 38.09  ? 2035 LEU A CD1   1 
ATOM   5694  C  CD2   . LEU A 1 2035 ? 172.699 180.030 131.967 1.00 31.98  ? 2035 LEU A CD2   1 
ATOM   5695  N  N     . PHE A 1 2036 ? 168.293 176.906 131.120 1.00 37.24  ? 2036 PHE A N     1 
ATOM   5696  C  CA    . PHE A 1 2036 ? 167.759 175.719 130.471 1.00 30.63  ? 2036 PHE A CA    1 
ATOM   5697  C  C     . PHE A 1 2036 ? 166.404 176.014 129.846 1.00 34.57  ? 2036 PHE A C     1 
ATOM   5698  O  O     . PHE A 1 2036 ? 165.597 176.759 130.409 1.00 42.00  ? 2036 PHE A O     1 
ATOM   5699  C  CB    . PHE A 1 2036 ? 167.628 174.561 131.464 1.00 28.54  ? 2036 PHE A CB    1 
ATOM   5700  C  CG    . PHE A 1 2036 ? 168.901 173.798 131.670 1.00 29.17  ? 2036 PHE A CG    1 
ATOM   5701  C  CD1   . PHE A 1 2036 ? 169.954 174.356 132.368 1.00 27.28  ? 2036 PHE A CD1   1 
ATOM   5702  C  CD2   . PHE A 1 2036 ? 169.049 172.525 131.155 1.00 29.57  ? 2036 PHE A CD2   1 
ATOM   5703  C  CE1   . PHE A 1 2036 ? 171.125 173.658 132.550 1.00 27.84  ? 2036 PHE A CE1   1 
ATOM   5704  C  CE2   . PHE A 1 2036 ? 170.217 171.824 131.334 1.00 26.80  ? 2036 PHE A CE2   1 
ATOM   5705  C  CZ    . PHE A 1 2036 ? 171.256 172.391 132.032 1.00 29.27  ? 2036 PHE A CZ    1 
ATOM   5706  N  N     . ARG A 1 2037 ? 166.167 175.424 128.679 1.00 33.15  ? 2037 ARG A N     1 
ATOM   5707  C  CA    A ARG A 1 2037 ? 164.899 175.542 127.972 0.57 32.76  ? 2037 ARG A CA    1 
ATOM   5708  C  CA    B ARG A 1 2037 ? 164.902 175.541 127.968 0.43 32.62  ? 2037 ARG A CA    1 
ATOM   5709  C  C     . ARG A 1 2037 ? 164.071 174.295 128.244 1.00 33.53  ? 2037 ARG A C     1 
ATOM   5710  O  O     . ARG A 1 2037 ? 164.495 173.181 127.921 1.00 39.55  ? 2037 ARG A O     1 
ATOM   5711  C  CB    A ARG A 1 2037 ? 165.123 175.718 126.472 0.57 31.57  ? 2037 ARG A CB    1 
ATOM   5712  C  CB    B ARG A 1 2037 ? 165.143 175.713 126.469 0.43 31.81  ? 2037 ARG A CB    1 
ATOM   5713  C  CG    A ARG A 1 2037 ? 165.769 177.035 126.095 0.57 32.95  ? 2037 ARG A CG    1 
ATOM   5714  C  CG    B ARG A 1 2037 ? 163.913 176.111 125.674 0.43 33.62  ? 2037 ARG A CG    1 
ATOM   5715  C  CD    A ARG A 1 2037 ? 164.759 177.993 125.488 0.57 34.45  ? 2037 ARG A CD    1 
ATOM   5716  C  CD    B ARG A 1 2037 ? 163.979 177.568 125.248 0.43 34.29  ? 2037 ARG A CD    1 
ATOM   5717  N  NE    A ARG A 1 2037 ? 164.204 177.478 124.243 0.57 32.69  ? 2037 ARG A NE    1 
ATOM   5718  N  NE    B ARG A 1 2037 ? 164.245 178.447 126.379 0.43 34.32  ? 2037 ARG A NE    1 
ATOM   5719  C  CZ    A ARG A 1 2037 ? 164.446 177.995 123.047 0.57 31.57  ? 2037 ARG A CZ    1 
ATOM   5720  C  CZ    B ARG A 1 2037 ? 163.374 179.315 126.876 0.43 35.67  ? 2037 ARG A CZ    1 
ATOM   5721  N  NH1   A ARG A 1 2037 ? 165.240 179.042 122.894 0.57 30.70  ? 2037 ARG A NH1   1 
ATOM   5722  N  NH1   B ARG A 1 2037 ? 162.163 179.449 126.363 0.43 36.54  ? 2037 ARG A NH1   1 
ATOM   5723  N  NH2   A ARG A 1 2037 ? 163.879 177.446 121.977 0.57 34.08  ? 2037 ARG A NH2   1 
ATOM   5724  N  NH2   B ARG A 1 2037 ? 163.727 180.063 127.916 0.43 38.90  ? 2037 ARG A NH2   1 
ATOM   5725  N  N     . SER A 1 2038 ? 162.900 174.483 128.841 1.00 30.61  ? 2038 SER A N     1 
ATOM   5726  C  CA    . SER A 1 2038 ? 162.036 173.372 129.205 1.00 29.36  ? 2038 SER A CA    1 
ATOM   5727  C  C     . SER A 1 2038 ? 161.113 173.000 128.054 1.00 32.35  ? 2038 SER A C     1 
ATOM   5728  O  O     . SER A 1 2038 ? 160.713 173.845 127.250 1.00 39.63  ? 2038 SER A O     1 
ATOM   5729  C  CB    . SER A 1 2038 ? 161.207 173.716 130.443 1.00 36.24  ? 2038 SER A CB    1 
ATOM   5730  O  OG    . SER A 1 2038 ? 160.353 174.816 130.190 1.00 41.64  ? 2038 SER A OG    1 
ATOM   5731  N  N     . LEU A 1 2039 ? 160.784 171.713 127.980 1.00 27.92  ? 2039 LEU A N     1 
ATOM   5732  C  CA    . LEU A 1 2039 ? 159.873 171.201 126.967 1.00 28.40  ? 2039 LEU A CA    1 
ATOM   5733  C  C     . LEU A 1 2039 ? 158.962 170.148 127.573 1.00 29.99  ? 2039 LEU A C     1 
ATOM   5734  O  O     . LEU A 1 2039 ? 159.436 169.191 128.188 1.00 33.65  ? 2039 LEU A O     1 
ATOM   5735  C  CB    . LEU A 1 2039 ? 160.621 170.587 125.788 1.00 29.48  ? 2039 LEU A CB    1 
ATOM   5736  C  CG    . LEU A 1 2039 ? 159.675 170.051 124.715 1.00 33.29  ? 2039 LEU A CG    1 
ATOM   5737  C  CD1   . LEU A 1 2039 ? 159.029 171.181 123.928 1.00 33.59  ? 2039 LEU A CD1   1 
ATOM   5738  C  CD2   . LEU A 1 2039 ? 160.396 169.096 123.811 1.00 30.80  ? 2039 LEU A CD2   1 
ATOM   5739  N  N     . ALA A 1 2040 ? 157.660 170.304 127.361 1.00 31.17  ? 2040 ALA A N     1 
ATOM   5740  C  CA    . ALA A 1 2040 ? 156.667 169.387 127.913 1.00 29.98  ? 2040 ALA A CA    1 
ATOM   5741  C  C     . ALA A 1 2040 ? 156.562 168.169 127.006 1.00 34.92  ? 2040 ALA A C     1 
ATOM   5742  O  O     . ALA A 1 2040 ? 155.878 168.200 125.981 1.00 44.32  ? 2040 ALA A O     1 
ATOM   5743  C  CB    . ALA A 1 2040 ? 155.321 170.082 128.065 1.00 33.08  ? 2040 ALA A CB    1 
ATOM   5744  N  N     . MET A 1 2041 ? 157.246 167.088 127.381 1.00 29.72  ? 2041 MET A N     1 
ATOM   5745  C  CA    . MET A 1 2041 ? 157.097 165.797 126.712 1.00 36.58  ? 2041 MET A CA    1 
ATOM   5746  C  C     . MET A 1 2041 ? 156.213 164.928 127.600 1.00 43.35  ? 2041 MET A C     1 
ATOM   5747  O  O     . MET A 1 2041 ? 156.684 164.123 128.402 1.00 46.76  ? 2041 MET A O     1 
ATOM   5748  C  CB    . MET A 1 2041 ? 158.454 165.153 126.452 1.00 33.23  ? 2041 MET A CB    1 
ATOM   5749  C  CG    . MET A 1 2041 ? 159.345 165.939 125.514 1.00 38.51  ? 2041 MET A CG    1 
ATOM   5750  S  SD    . MET A 1 2041 ? 160.802 165.012 125.015 1.00 46.54  ? 2041 MET A SD    1 
ATOM   5751  C  CE    . MET A 1 2041 ? 160.045 163.489 124.466 1.00 32.29  ? 2041 MET A CE    1 
ATOM   5752  N  N     . THR A 1 2042 ? 154.900 165.104 127.448 1.00 46.96  ? 2042 THR A N     1 
ATOM   5753  C  CA    . THR A 1 2042 ? 153.936 164.514 128.365 1.00 47.64  ? 2042 THR A CA    1 
ATOM   5754  C  C     . THR A 1 2042 ? 153.086 163.407 127.761 1.00 49.13  ? 2042 THR A C     1 
ATOM   5755  O  O     . THR A 1 2042 ? 152.566 162.578 128.513 1.00 52.66  ? 2042 THR A O     1 
ATOM   5756  C  CB    . THR A 1 2042 ? 153.006 165.600 128.926 1.00 44.17  ? 2042 THR A CB    1 
ATOM   5757  O  OG1   . THR A 1 2042 ? 152.094 165.016 129.863 1.00 54.49  ? 2042 THR A OG1   1 
ATOM   5758  C  CG2   . THR A 1 2042 ? 152.227 166.272 127.808 1.00 46.52  ? 2042 THR A CG2   1 
ATOM   5759  N  N     . LYS A 1 2043 ? 152.931 163.364 126.439 1.00 45.78  ? 2043 LYS A N     1 
ATOM   5760  C  CA    . LYS A 1 2043 ? 152.090 162.362 125.786 1.00 46.90  ? 2043 LYS A CA    1 
ATOM   5761  C  C     . LYS A 1 2043 ? 152.768 161.887 124.508 1.00 44.85  ? 2043 LYS A C     1 
ATOM   5762  O  O     . LYS A 1 2043 ? 152.655 162.541 123.458 1.00 46.35  ? 2043 LYS A O     1 
ATOM   5763  C  CB    . LYS A 1 2043 ? 150.698 162.915 125.487 1.00 48.80  ? 2043 LYS A CB    1 
ATOM   5764  C  CG    . LYS A 1 2043 ? 149.702 162.734 126.620 1.00 55.42  ? 2043 LYS A CG    1 
ATOM   5765  C  CD    . LYS A 1 2043 ? 148.491 163.632 126.437 1.00 63.97  ? 2043 LYS A CD    1 
ATOM   5766  C  CE    . LYS A 1 2043 ? 148.589 164.877 127.306 1.00 58.25  ? 2043 LYS A CE    1 
ATOM   5767  N  NZ    . LYS A 1 2043 ? 148.471 164.553 128.754 1.00 55.01  ? 2043 LYS A NZ    1 
ATOM   5768  N  N     . PRO A 1 2044 ? 153.479 160.764 124.555 1.00 37.69  ? 2044 PRO A N     1 
ATOM   5769  C  CA    . PRO A 1 2044 ? 154.059 160.212 123.328 1.00 36.00  ? 2044 PRO A CA    1 
ATOM   5770  C  C     . PRO A 1 2044 ? 152.976 159.767 122.361 1.00 41.32  ? 2044 PRO A C     1 
ATOM   5771  O  O     . PRO A 1 2044 ? 151.896 159.323 122.758 1.00 42.37  ? 2044 PRO A O     1 
ATOM   5772  C  CB    . PRO A 1 2044 ? 154.883 159.021 123.828 1.00 33.87  ? 2044 PRO A CB    1 
ATOM   5773  C  CG    . PRO A 1 2044 ? 154.247 158.641 125.116 1.00 36.80  ? 2044 PRO A CG    1 
ATOM   5774  C  CD    . PRO A 1 2044 ? 153.754 159.919 125.727 1.00 37.01  ? 2044 PRO A CD    1 
ATOM   5775  N  N     . ASP A 1 2045 ? 153.278 159.893 121.069 1.00 40.14  ? 2045 ASP A N     1 
ATOM   5776  C  CA    . ASP A 1 2045 ? 152.344 159.497 120.017 1.00 39.52  ? 2045 ASP A CA    1 
ATOM   5777  C  C     . ASP A 1 2045 ? 152.474 157.992 119.810 1.00 39.65  ? 2045 ASP A C     1 
ATOM   5778  O  O     . ASP A 1 2045 ? 153.128 157.506 118.884 1.00 40.05  ? 2045 ASP A O     1 
ATOM   5779  C  CB    . ASP A 1 2045 ? 152.612 160.277 118.737 1.00 42.13  ? 2045 ASP A CB    1 
ATOM   5780  C  CG    . ASP A 1 2045 ? 151.450 160.222 117.766 1.00 51.89  ? 2045 ASP A CG    1 
ATOM   5781  O  OD1   . ASP A 1 2045 ? 150.289 160.221 118.225 1.00 52.68  ? 2045 ASP A OD1   1 
ATOM   5782  O  OD2   . ASP A 1 2045 ? 151.693 160.202 116.544 1.00 49.47  ? 2045 ASP A OD2   1 
ATOM   5783  N  N     . ARG A 1 2046 ? 151.827 157.240 120.705 1.00 39.03  ? 2046 ARG A N     1 
ATOM   5784  C  CA    . ARG A 1 2046 ? 151.969 155.788 120.701 1.00 31.69  ? 2046 ARG A CA    1 
ATOM   5785  C  C     . ARG A 1 2046 ? 151.374 155.158 119.452 1.00 32.12  ? 2046 ARG A C     1 
ATOM   5786  O  O     . ARG A 1 2046 ? 151.860 154.118 118.996 1.00 37.28  ? 2046 ARG A O     1 
ATOM   5787  C  CB    . ARG A 1 2046 ? 151.319 155.190 121.948 1.00 31.32  ? 2046 ARG A CB    1 
ATOM   5788  C  CG    . ARG A 1 2046 ? 151.846 155.738 123.258 1.00 32.37  ? 2046 ARG A CG    1 
ATOM   5789  C  CD    . ARG A 1 2046 ? 150.751 155.787 124.304 1.00 33.98  ? 2046 ARG A CD    1 
ATOM   5790  N  NE    . ARG A 1 2046 ? 151.184 156.458 125.523 1.00 43.05  ? 2046 ARG A NE    1 
ATOM   5791  C  CZ    . ARG A 1 2046 ? 151.837 155.863 126.511 1.00 50.89  ? 2046 ARG A CZ    1 
ATOM   5792  N  NH1   . ARG A 1 2046 ? 152.142 154.577 126.462 1.00 43.73  ? 2046 ARG A NH1   1 
ATOM   5793  N  NH2   . ARG A 1 2046 ? 152.191 156.576 127.576 1.00 50.13  ? 2046 ARG A NH2   1 
ATOM   5794  N  N     . GLN A 1 2047 ? 150.322 155.754 118.891 1.00 31.80  ? 2047 GLN A N     1 
ATOM   5795  C  CA    . GLN A 1 2047 ? 149.706 155.183 117.697 1.00 33.79  ? 2047 GLN A CA    1 
ATOM   5796  C  C     . GLN A 1 2047 ? 150.684 155.167 116.530 1.00 34.05  ? 2047 GLN A C     1 
ATOM   5797  O  O     . GLN A 1 2047 ? 150.826 154.154 115.840 1.00 39.61  ? 2047 GLN A O     1 
ATOM   5798  C  CB    . GLN A 1 2047 ? 148.442 155.960 117.332 1.00 39.48  ? 2047 GLN A CB    1 
ATOM   5799  C  CG    . GLN A 1 2047 ? 147.174 155.418 117.966 1.00 41.00  ? 2047 GLN A CG    1 
ATOM   5800  C  CD    . GLN A 1 2047 ? 146.859 156.076 119.293 1.00 47.92  ? 2047 GLN A CD    1 
ATOM   5801  O  OE1   . GLN A 1 2047 ? 147.594 156.947 119.757 1.00 44.25  ? 2047 GLN A OE1   1 
ATOM   5802  N  NE2   . GLN A 1 2047 ? 145.759 155.662 119.912 1.00 46.28  ? 2047 GLN A NE2   1 
ATOM   5803  N  N     . LEU A 1 2048 ? 151.389 156.278 116.309 1.00 35.57  ? 2048 LEU A N     1 
ATOM   5804  C  CA    . LEU A 1 2048 ? 152.338 156.331 115.203 1.00 33.11  ? 2048 LEU A CA    1 
ATOM   5805  C  C     . LEU A 1 2048 ? 153.558 155.462 115.477 1.00 30.24  ? 2048 LEU A C     1 
ATOM   5806  O  O     . LEU A 1 2048 ? 154.101 154.843 114.558 1.00 34.91  ? 2048 LEU A O     1 
ATOM   5807  C  CB    . LEU A 1 2048 ? 152.756 157.774 114.931 1.00 31.60  ? 2048 LEU A CB    1 
ATOM   5808  C  CG    . LEU A 1 2048 ? 153.823 157.967 113.856 1.00 30.15  ? 2048 LEU A CG    1 
ATOM   5809  C  CD1   . LEU A 1 2048 ? 153.263 157.608 112.494 1.00 37.56  ? 2048 LEU A CD1   1 
ATOM   5810  C  CD2   . LEU A 1 2048 ? 154.333 159.394 113.864 1.00 37.35  ? 2048 LEU A CD2   1 
ATOM   5811  N  N     . ILE A 1 2049 ? 154.002 155.401 116.734 1.00 28.22  ? 2049 ILE A N     1 
ATOM   5812  C  CA    . ILE A 1 2049 ? 155.115 154.524 117.087 1.00 24.96  ? 2049 ILE A CA    1 
ATOM   5813  C  C     . ILE A 1 2049 ? 154.767 153.079 116.762 1.00 30.23  ? 2049 ILE A C     1 
ATOM   5814  O  O     . ILE A 1 2049 ? 155.537 152.362 116.108 1.00 37.59  ? 2049 ILE A O     1 
ATOM   5815  C  CB    . ILE A 1 2049 ? 155.476 154.692 118.573 1.00 27.67  ? 2049 ILE A CB    1 
ATOM   5816  C  CG1   . ILE A 1 2049 ? 156.059 156.078 118.827 1.00 28.20  ? 2049 ILE A CG1   1 
ATOM   5817  C  CG2   . ILE A 1 2049 ? 156.449 153.613 119.009 1.00 30.12  ? 2049 ILE A CG2   1 
ATOM   5818  C  CD1   . ILE A 1 2049 ? 156.011 156.496 120.270 1.00 27.08  ? 2049 ILE A CD1   1 
ATOM   5819  N  N     . ALA A 1 2050 ? 153.590 152.635 117.209 1.00 29.94  ? 2050 ALA A N     1 
ATOM   5820  C  CA    . ALA A 1 2050 ? 153.156 151.271 116.941 1.00 25.62  ? 2050 ALA A CA    1 
ATOM   5821  C  C     . ALA A 1 2050 ? 152.978 151.030 115.450 1.00 27.61  ? 2050 ALA A C     1 
ATOM   5822  O  O     . ALA A 1 2050 ? 153.358 149.972 114.940 1.00 35.37  ? 2050 ALA A O     1 
ATOM   5823  C  CB    . ALA A 1 2050 ? 151.860 150.975 117.694 1.00 24.52  ? 2050 ALA A CB    1 
ATOM   5824  N  N     . GLN A 1 2051 ? 152.414 152.003 114.732 1.00 26.31  ? 2051 GLN A N     1 
ATOM   5825  C  CA    . GLN A 1 2051 ? 152.216 151.849 113.296 1.00 29.19  ? 2051 GLN A CA    1 
ATOM   5826  C  C     . GLN A 1 2051 ? 153.542 151.678 112.570 1.00 29.21  ? 2051 GLN A C     1 
ATOM   5827  O  O     . GLN A 1 2051 ? 153.689 150.790 111.725 1.00 31.95  ? 2051 GLN A O     1 
ATOM   5828  C  CB    . GLN A 1 2051 ? 151.459 153.054 112.742 1.00 33.53  ? 2051 GLN A CB    1 
ATOM   5829  C  CG    . GLN A 1 2051 ? 151.318 153.045 111.235 1.00 39.11  ? 2051 GLN A CG    1 
ATOM   5830  C  CD    . GLN A 1 2051 ? 150.867 154.379 110.692 1.00 55.50  ? 2051 GLN A CD    1 
ATOM   5831  O  OE1   . GLN A 1 2051 ? 149.827 154.903 111.089 1.00 63.69  ? 2051 GLN A OE1   1 
ATOM   5832  N  NE2   . GLN A 1 2051 ? 151.647 154.938 109.776 1.00 57.81  ? 2051 GLN A NE2   1 
ATOM   5833  N  N     . VAL A 1 2052 ? 154.526 152.516 112.896 1.00 29.63  ? 2052 VAL A N     1 
ATOM   5834  C  CA    . VAL A 1 2052 ? 155.801 152.457 112.193 1.00 27.93  ? 2052 VAL A CA    1 
ATOM   5835  C  C     . VAL A 1 2052 ? 156.551 151.181 112.547 1.00 31.80  ? 2052 VAL A C     1 
ATOM   5836  O  O     . VAL A 1 2052 ? 157.170 150.552 111.681 1.00 35.99  ? 2052 VAL A O     1 
ATOM   5837  C  CB    . VAL A 1 2052 ? 156.637 153.713 112.490 1.00 29.27  ? 2052 VAL A CB    1 
ATOM   5838  C  CG1   . VAL A 1 2052 ? 158.003 153.602 111.846 1.00 30.94  ? 2052 VAL A CG1   1 
ATOM   5839  C  CG2   . VAL A 1 2052 ? 155.921 154.946 111.981 1.00 31.59  ? 2052 VAL A CG2   1 
ATOM   5840  N  N     . MET A 1 2053 ? 156.508 150.767 113.817 1.00 31.10  ? 2053 MET A N     1 
ATOM   5841  C  CA    . MET A 1 2053 ? 157.193 149.532 114.184 1.00 31.87  ? 2053 MET A CA    1 
ATOM   5842  C  C     . MET A 1 2053 ? 156.533 148.315 113.548 1.00 33.12  ? 2053 MET A C     1 
ATOM   5843  O  O     . MET A 1 2053 ? 157.223 147.394 113.099 1.00 39.15  ? 2053 MET A O     1 
ATOM   5844  C  CB    . MET A 1 2053 ? 157.257 149.379 115.698 1.00 27.92  ? 2053 MET A CB    1 
ATOM   5845  C  CG    . MET A 1 2053 ? 158.129 150.415 116.361 1.00 36.45  ? 2053 MET A CG    1 
ATOM   5846  S  SD    . MET A 1 2053 ? 158.113 150.216 118.138 1.00 69.22  ? 2053 MET A SD    1 
ATOM   5847  C  CE    . MET A 1 2053 ? 159.048 148.695 118.263 1.00 44.93  ? 2053 MET A CE    1 
ATOM   5848  N  N     . LEU A 1 2054 ? 155.200 148.289 113.497 1.00 27.83  ? 2054 LEU A N     1 
ATOM   5849  C  CA    . LEU A 1 2054 ? 154.511 147.184 112.843 1.00 24.53  ? 2054 LEU A CA    1 
ATOM   5850  C  C     . LEU A 1 2054 ? 154.775 147.173 111.345 1.00 29.46  ? 2054 LEU A C     1 
ATOM   5851  O  O     . LEU A 1 2054 ? 154.872 146.100 110.742 1.00 37.37  ? 2054 LEU A O     1 
ATOM   5852  C  CB    . LEU A 1 2054 ? 153.015 147.270 113.127 1.00 28.13  ? 2054 LEU A CB    1 
ATOM   5853  C  CG    . LEU A 1 2054 ? 152.584 146.675 114.466 1.00 26.73  ? 2054 LEU A CG    1 
ATOM   5854  C  CD1   . LEU A 1 2054 ? 151.110 146.897 114.690 1.00 27.70  ? 2054 LEU A CD1   1 
ATOM   5855  C  CD2   . LEU A 1 2054 ? 152.916 145.197 114.528 1.00 30.61  ? 2054 LEU A CD2   1 
ATOM   5856  N  N     . TYR A 1 2055 ? 154.885 148.351 110.728 1.00 30.09  ? 2055 TYR A N     1 
ATOM   5857  C  CA    . TYR A 1 2055 ? 155.276 148.422 109.325 1.00 31.85  ? 2055 TYR A CA    1 
ATOM   5858  C  C     . TYR A 1 2055 ? 156.684 147.881 109.123 1.00 33.33  ? 2055 TYR A C     1 
ATOM   5859  O  O     . TYR A 1 2055 ? 156.959 147.195 108.132 1.00 33.63  ? 2055 TYR A O     1 
ATOM   5860  C  CB    . TYR A 1 2055 ? 155.179 149.864 108.833 1.00 32.00  ? 2055 TYR A CB    1 
ATOM   5861  C  CG    . TYR A 1 2055 ? 155.174 150.007 107.332 1.00 37.36  ? 2055 TYR A CG    1 
ATOM   5862  C  CD1   . TYR A 1 2055 ? 154.268 149.305 106.552 1.00 47.01  ? 2055 TYR A CD1   1 
ATOM   5863  C  CD2   . TYR A 1 2055 ? 156.080 150.843 106.695 1.00 38.51  ? 2055 TYR A CD2   1 
ATOM   5864  C  CE1   . TYR A 1 2055 ? 154.262 149.435 105.178 1.00 60.13  ? 2055 TYR A CE1   1 
ATOM   5865  C  CE2   . TYR A 1 2055 ? 156.083 150.977 105.323 1.00 44.71  ? 2055 TYR A CE2   1 
ATOM   5866  C  CZ    . TYR A 1 2055 ? 155.173 150.272 104.569 1.00 60.65  ? 2055 TYR A CZ    1 
ATOM   5867  O  OH    . TYR A 1 2055 ? 155.172 150.405 103.200 1.00 58.16  ? 2055 TYR A OH    1 
ATOM   5868  N  N     . SER A 1 2056 ? 157.593 148.184 110.052 1.00 30.22  ? 2056 SER A N     1 
ATOM   5869  C  CA    . SER A 1 2056 ? 158.960 147.692 109.948 1.00 31.35  ? 2056 SER A CA    1 
ATOM   5870  C  C     . SER A 1 2056 ? 159.064 146.202 110.238 1.00 41.10  ? 2056 SER A C     1 
ATOM   5871  O  O     . SER A 1 2056 ? 160.102 145.601 109.948 1.00 49.69  ? 2056 SER A O     1 
ATOM   5872  C  CB    . SER A 1 2056 ? 159.873 148.468 110.896 1.00 35.43  ? 2056 SER A CB    1 
ATOM   5873  O  OG    . SER A 1 2056 ? 159.503 148.257 112.245 1.00 36.20  ? 2056 SER A OG    1 
ATOM   5874  N  N     . GLN A 1 2057 ? 158.026 145.598 110.813 1.00 39.63  ? 2057 GLN A N     1 
ATOM   5875  C  CA    . GLN A 1 2057 ? 157.996 144.162 111.051 1.00 34.93  ? 2057 GLN A CA    1 
ATOM   5876  C  C     . GLN A 1 2057 ? 157.287 143.396 109.943 1.00 33.24  ? 2057 GLN A C     1 
ATOM   5877  O  O     . GLN A 1 2057 ? 157.128 142.176 110.056 1.00 32.92  ? 2057 GLN A O     1 
ATOM   5878  C  CB    . GLN A 1 2057 ? 157.330 143.858 112.397 1.00 29.02  ? 2057 GLN A CB    1 
ATOM   5879  C  CG    . GLN A 1 2057 ? 158.085 144.403 113.597 1.00 31.59  ? 2057 GLN A CG    1 
ATOM   5880  C  CD    . GLN A 1 2057 ? 159.411 143.706 113.831 1.00 45.86  ? 2057 GLN A CD    1 
ATOM   5881  O  OE1   . GLN A 1 2057 ? 159.687 142.655 113.255 1.00 50.13  ? 2057 GLN A OE1   1 
ATOM   5882  N  NE2   . GLN A 1 2057 ? 160.245 144.298 114.675 1.00 54.41  ? 2057 GLN A NE2   1 
ATOM   5883  N  N     . GLY A 1 2058 ? 156.858 144.076 108.884 1.00 34.23  ? 2058 GLY A N     1 
ATOM   5884  C  CA    . GLY A 1 2058 ? 156.241 143.429 107.748 1.00 34.92  ? 2058 GLY A CA    1 
ATOM   5885  C  C     . GLY A 1 2058 ? 154.729 143.421 107.740 1.00 37.70  ? 2058 GLY A C     1 
ATOM   5886  O  O     . GLY A 1 2058 ? 154.139 142.858 106.811 1.00 44.90  ? 2058 GLY A O     1 
ATOM   5887  N  N     . PHE A 1 2059 ? 154.084 144.021 108.735 1.00 31.71  ? 2059 PHE A N     1 
ATOM   5888  C  CA    . PHE A 1 2059 ? 152.629 144.019 108.783 1.00 33.68  ? 2059 PHE A CA    1 
ATOM   5889  C  C     . PHE A 1 2059 ? 152.069 145.017 107.778 1.00 43.61  ? 2059 PHE A C     1 
ATOM   5890  O  O     . PHE A 1 2059 ? 152.392 146.207 107.823 1.00 46.15  ? 2059 PHE A O     1 
ATOM   5891  C  CB    . PHE A 1 2059 ? 152.144 144.355 110.191 1.00 33.05  ? 2059 PHE A CB    1 
ATOM   5892  C  CG    . PHE A 1 2059 ? 152.344 143.245 111.182 1.00 34.56  ? 2059 PHE A CG    1 
ATOM   5893  C  CD1   . PHE A 1 2059 ? 153.602 142.949 111.668 1.00 34.91  ? 2059 PHE A CD1   1 
ATOM   5894  C  CD2   . PHE A 1 2059 ? 151.273 142.492 111.619 1.00 42.75  ? 2059 PHE A CD2   1 
ATOM   5895  C  CE1   . PHE A 1 2059 ? 153.784 141.930 112.576 1.00 37.71  ? 2059 PHE A CE1   1 
ATOM   5896  C  CE2   . PHE A 1 2059 ? 151.449 141.471 112.526 1.00 41.49  ? 2059 PHE A CE2   1 
ATOM   5897  C  CZ    . PHE A 1 2059 ? 152.705 141.190 113.005 1.00 37.65  ? 2059 PHE A CZ    1 
ATOM   5898  N  N     . ARG A 1 2060 ? 151.227 144.529 106.865 1.00 49.63  ? 2060 ARG A N     1 
ATOM   5899  C  CA    . ARG A 1 2060 ? 150.651 145.413 105.857 1.00 52.19  ? 2060 ARG A CA    1 
ATOM   5900  C  C     . ARG A 1 2060 ? 149.592 146.327 106.463 1.00 55.91  ? 2060 ARG A C     1 
ATOM   5901  O  O     . ARG A 1 2060 ? 149.477 147.495 106.074 1.00 61.17  ? 2060 ARG A O     1 
ATOM   5902  C  CB    . ARG A 1 2060 ? 150.070 144.592 104.704 1.00 56.95  ? 2060 ARG A CB    1 
ATOM   5903  C  CG    . ARG A 1 2060 ? 148.892 143.714 105.083 1.00 70.13  ? 2060 ARG A CG    1 
ATOM   5904  C  CD    . ARG A 1 2060 ? 148.349 142.956 103.886 1.00 78.62  ? 2060 ARG A CD    1 
ATOM   5905  N  NE    . ARG A 1 2060 ? 147.266 142.057 104.267 1.00 85.75  ? 2060 ARG A NE    1 
ATOM   5906  C  CZ    . ARG A 1 2060 ? 145.990 142.411 104.329 1.00 95.62  ? 2060 ARG A CZ    1 
ATOM   5907  N  NH1   . ARG A 1 2060 ? 145.599 143.641 104.036 1.00 95.57  ? 2060 ARG A NH1   1 
ATOM   5908  N  NH2   . ARG A 1 2060 ? 145.084 141.510 104.695 1.00 97.22  ? 2060 ARG A NH2   1 
ATOM   5909  N  N     . THR A 1 2061 ? 148.812 145.818 107.416 1.00 49.44  ? 2061 THR A N     1 
ATOM   5910  C  CA    . THR A 1 2061 ? 147.792 146.615 108.098 1.00 51.53  ? 2061 THR A CA    1 
ATOM   5911  C  C     . THR A 1 2061 ? 148.353 147.199 109.395 1.00 48.91  ? 2061 THR A C     1 
ATOM   5912  O  O     . THR A 1 2061 ? 147.816 147.013 110.485 1.00 54.51  ? 2061 THR A O     1 
ATOM   5913  C  CB    . THR A 1 2061 ? 146.552 145.770 108.365 1.00 54.51  ? 2061 THR A CB    1 
ATOM   5914  O  OG1   . THR A 1 2061 ? 146.857 144.770 109.344 1.00 57.64  ? 2061 THR A OG1   1 
ATOM   5915  C  CG2   . THR A 1 2061 ? 146.088 145.092 107.089 1.00 60.98  ? 2061 THR A CG2   1 
ATOM   5916  N  N     . ALA A 1 2062 ? 149.468 147.918 109.253 1.00 40.00  ? 2062 ALA A N     1 
ATOM   5917  C  CA    . ALA A 1 2062 ? 150.143 148.476 110.420 1.00 35.68  ? 2062 ALA A CA    1 
ATOM   5918  C  C     . ALA A 1 2062 ? 149.291 149.533 111.111 1.00 41.19  ? 2062 ALA A C     1 
ATOM   5919  O  O     . ALA A 1 2062 ? 149.235 149.579 112.345 1.00 41.73  ? 2062 ALA A O     1 
ATOM   5920  C  CB    . ALA A 1 2062 ? 151.493 149.059 110.012 1.00 38.94  ? 2062 ALA A CB    1 
ATOM   5921  N  N     . GLU A 1 2063 ? 148.624 150.393 110.338 1.00 42.20  ? 2063 GLU A N     1 
ATOM   5922  C  CA    . GLU A 1 2063 ? 147.861 151.487 110.934 1.00 46.73  ? 2063 GLU A CA    1 
ATOM   5923  C  C     . GLU A 1 2063 ? 146.666 150.969 111.724 1.00 49.56  ? 2063 GLU A C     1 
ATOM   5924  O  O     . GLU A 1 2063 ? 146.407 151.423 112.845 1.00 54.81  ? 2063 GLU A O     1 
ATOM   5925  C  CB    . GLU A 1 2063 ? 147.406 152.460 109.848 1.00 52.89  ? 2063 GLU A CB    1 
ATOM   5926  C  CG    . GLU A 1 2063 ? 146.635 153.655 110.379 1.00 60.28  ? 2063 GLU A CG    1 
ATOM   5927  C  CD    . GLU A 1 2063 ? 146.605 154.810 109.400 1.00 79.46  ? 2063 GLU A CD    1 
ATOM   5928  O  OE1   . GLU A 1 2063 ? 146.140 154.612 108.259 1.00 88.31  ? 2063 GLU A OE1   1 
ATOM   5929  O  OE2   . GLU A 1 2063 ? 147.041 155.918 109.775 1.00 80.13  ? 2063 GLU A OE2   1 
ATOM   5930  N  N     . VAL A 1 2064 ? 145.922 150.021 111.150 1.00 45.59  ? 2064 VAL A N     1 
ATOM   5931  C  CA    . VAL A 1 2064 ? 144.765 149.457 111.840 1.00 41.16  ? 2064 VAL A CA    1 
ATOM   5932  C  C     . VAL A 1 2064 ? 145.200 148.739 113.109 1.00 37.76  ? 2064 VAL A C     1 
ATOM   5933  O  O     . VAL A 1 2064 ? 144.604 148.913 114.180 1.00 39.66  ? 2064 VAL A O     1 
ATOM   5934  C  CB    . VAL A 1 2064 ? 143.992 148.519 110.895 1.00 39.28  ? 2064 VAL A CB    1 
ATOM   5935  C  CG1   . VAL A 1 2064 ? 142.870 147.822 111.639 1.00 45.27  ? 2064 VAL A CG1   1 
ATOM   5936  C  CG2   . VAL A 1 2064 ? 143.452 149.294 109.706 1.00 45.96  ? 2064 VAL A CG2   1 
ATOM   5937  N  N     . LEU A 1 2065 ? 146.259 147.935 113.015 1.00 37.26  ? 2065 LEU A N     1 
ATOM   5938  C  CA    . LEU A 1 2065 ? 146.730 147.198 114.180 1.00 33.84  ? 2065 LEU A CA    1 
ATOM   5939  C  C     . LEU A 1 2065 ? 147.251 148.135 115.260 1.00 34.97  ? 2065 LEU A C     1 
ATOM   5940  O  O     . LEU A 1 2065 ? 147.101 147.855 116.451 1.00 38.82  ? 2065 LEU A O     1 
ATOM   5941  C  CB    . LEU A 1 2065 ? 147.804 146.197 113.765 1.00 37.24  ? 2065 LEU A CB    1 
ATOM   5942  C  CG    . LEU A 1 2065 ? 147.307 144.998 112.967 1.00 33.42  ? 2065 LEU A CG    1 
ATOM   5943  C  CD1   . LEU A 1 2065 ? 148.412 143.984 112.824 1.00 37.14  ? 2065 LEU A CD1   1 
ATOM   5944  C  CD2   . LEU A 1 2065 ? 146.109 144.388 113.655 1.00 43.67  ? 2065 LEU A CD2   1 
ATOM   5945  N  N     . ALA A 1 2066 ? 147.866 149.253 114.869 1.00 34.27  ? 2066 ALA A N     1 
ATOM   5946  C  CA    . ALA A 1 2066 ? 148.324 150.228 115.856 1.00 34.16  ? 2066 ALA A CA    1 
ATOM   5947  C  C     . ALA A 1 2066 ? 147.148 150.906 116.547 1.00 36.92  ? 2066 ALA A C     1 
ATOM   5948  O  O     . ALA A 1 2066 ? 147.113 151.019 117.782 1.00 38.45  ? 2066 ALA A O     1 
ATOM   5949  C  CB    . ALA A 1 2066 ? 149.221 151.264 115.183 1.00 32.31  ? 2066 ALA A CB    1 
ATOM   5950  N  N     . ASN A 1 2067 ? 146.169 151.361 115.759 1.00 41.04  ? 2067 ASN A N     1 
ATOM   5951  C  CA    . ASN A 1 2067 ? 144.975 151.982 116.317 1.00 40.72  ? 2067 ASN A CA    1 
ATOM   5952  C  C     . ASN A 1 2067 ? 144.150 151.002 117.137 1.00 44.32  ? 2067 ASN A C     1 
ATOM   5953  O  O     . ASN A 1 2067 ? 143.249 151.429 117.864 1.00 52.32  ? 2067 ASN A O     1 
ATOM   5954  C  CB    . ASN A 1 2067 ? 144.113 152.568 115.200 1.00 38.95  ? 2067 ASN A CB    1 
ATOM   5955  C  CG    . ASN A 1 2067 ? 144.817 153.664 114.430 1.00 48.44  ? 2067 ASN A CG    1 
ATOM   5956  O  OD1   . ASN A 1 2067 ? 145.936 154.054 114.759 1.00 58.06  ? 2067 ASN A OD1   1 
ATOM   5957  N  ND2   . ASN A 1 2067 ? 144.162 154.166 113.391 1.00 50.14  ? 2067 ASN A ND2   1 
ATOM   5958  N  N     . LYS A 1 2068 ? 144.409 149.702 117.003 1.00 41.07  ? 2068 LYS A N     1 
ATOM   5959  C  CA    . LYS A 1 2068 ? 143.795 148.722 117.890 1.00 34.79  ? 2068 LYS A CA    1 
ATOM   5960  C  C     . LYS A 1 2068 ? 144.631 148.456 119.138 1.00 36.62  ? 2068 LYS A C     1 
ATOM   5961  O  O     . LYS A 1 2068 ? 144.083 148.360 120.239 1.00 44.30  ? 2068 LYS A O     1 
ATOM   5962  C  CB    . LYS A 1 2068 ? 143.558 147.408 117.143 1.00 35.45  ? 2068 LYS A CB    1 
ATOM   5963  C  CG    . LYS A 1 2068 ? 142.450 147.502 116.130 1.00 41.57  ? 2068 LYS A CG    1 
ATOM   5964  C  CD    . LYS A 1 2068 ? 142.155 146.188 115.454 1.00 47.27  ? 2068 LYS A CD    1 
ATOM   5965  C  CE    . LYS A 1 2068 ? 140.936 146.328 114.569 1.00 49.86  ? 2068 LYS A CE    1 
ATOM   5966  N  NZ    . LYS A 1 2068 ? 140.565 145.070 113.889 1.00 63.19  ? 2068 LYS A NZ    1 
ATOM   5967  N  N     . ILE A 1 2069 ? 145.951 148.355 118.996 1.00 36.33  ? 2069 ILE A N     1 
ATOM   5968  C  CA    . ILE A 1 2069 ? 146.770 147.864 120.096 1.00 34.73  ? 2069 ILE A CA    1 
ATOM   5969  C  C     . ILE A 1 2069 ? 147.098 148.966 121.095 1.00 37.48  ? 2069 ILE A C     1 
ATOM   5970  O  O     . ILE A 1 2069 ? 147.397 148.675 122.259 1.00 41.33  ? 2069 ILE A O     1 
ATOM   5971  C  CB    . ILE A 1 2069 ? 148.044 147.201 119.544 1.00 35.57  ? 2069 ILE A CB    1 
ATOM   5972  C  CG1   . ILE A 1 2069 ? 148.664 146.283 120.596 1.00 40.66  ? 2069 ILE A CG1   1 
ATOM   5973  C  CG2   . ILE A 1 2069 ? 149.045 148.247 119.097 1.00 33.78  ? 2069 ILE A CG2   1 
ATOM   5974  C  CD1   . ILE A 1 2069 ? 147.695 145.270 121.169 1.00 45.74  ? 2069 ILE A CD1   1 
ATOM   5975  N  N     . VAL A 1 2070 ? 147.054 150.232 120.691 1.00 39.44  ? 2070 VAL A N     1 
ATOM   5976  C  CA    . VAL A 1 2070 ? 147.343 151.295 121.655 1.00 36.54  ? 2070 VAL A CA    1 
ATOM   5977  C  C     . VAL A 1 2070 ? 146.176 151.461 122.630 1.00 39.31  ? 2070 VAL A C     1 
ATOM   5978  O  O     . VAL A 1 2070 ? 146.397 151.417 123.854 1.00 44.12  ? 2070 VAL A O     1 
ATOM   5979  C  CB    . VAL A 1 2070 ? 147.694 152.613 120.947 1.00 37.04  ? 2070 VAL A CB    1 
ATOM   5980  C  CG1   . VAL A 1 2070 ? 147.945 153.699 121.967 1.00 40.73  ? 2070 VAL A CG1   1 
ATOM   5981  C  CG2   . VAL A 1 2070 ? 148.912 152.423 120.066 1.00 34.17  ? 2070 VAL A CG2   1 
ATOM   5982  N  N     . PRO A 1 2071 ? 144.929 151.652 122.170 1.00 38.58  ? 2071 PRO A N     1 
ATOM   5983  C  CA    . PRO A 1 2071 ? 143.822 151.721 123.137 1.00 36.57  ? 2071 PRO A CA    1 
ATOM   5984  C  C     . PRO A 1 2071 ? 143.648 150.447 123.937 1.00 43.77  ? 2071 PRO A C     1 
ATOM   5985  O  O     . PRO A 1 2071 ? 143.189 150.507 125.082 1.00 49.20  ? 2071 PRO A O     1 
ATOM   5986  C  CB    . PRO A 1 2071 ? 142.596 152.004 122.259 1.00 34.17  ? 2071 PRO A CB    1 
ATOM   5987  C  CG    . PRO A 1 2071 ? 142.970 151.536 120.928 1.00 37.12  ? 2071 PRO A CG    1 
ATOM   5988  C  CD    . PRO A 1 2071 ? 144.431 151.803 120.791 1.00 36.33  ? 2071 PRO A CD    1 
ATOM   5989  N  N     . PHE A 1 2072 ? 143.999 149.290 123.373 1.00 45.51  ? 2072 PHE A N     1 
ATOM   5990  C  CA    . PHE A 1 2072 ? 143.924 148.052 124.140 1.00 40.41  ? 2072 PHE A CA    1 
ATOM   5991  C  C     . PHE A 1 2072 ? 144.891 148.071 125.316 1.00 40.38  ? 2072 PHE A C     1 
ATOM   5992  O  O     . PHE A 1 2072 ? 144.540 147.654 126.426 1.00 47.96  ? 2072 PHE A O     1 
ATOM   5993  C  CB    . PHE A 1 2072 ? 144.213 146.852 123.243 1.00 43.48  ? 2072 PHE A CB    1 
ATOM   5994  C  CG    . PHE A 1 2072 ? 144.336 145.566 123.996 1.00 47.17  ? 2072 PHE A CG    1 
ATOM   5995  C  CD1   . PHE A 1 2072 ? 143.256 145.050 124.687 1.00 49.87  ? 2072 PHE A CD1   1 
ATOM   5996  C  CD2   . PHE A 1 2072 ? 145.538 144.888 124.042 1.00 45.10  ? 2072 PHE A CD2   1 
ATOM   5997  C  CE1   . PHE A 1 2072 ? 143.367 143.872 125.391 1.00 48.68  ? 2072 PHE A CE1   1 
ATOM   5998  C  CE2   . PHE A 1 2072 ? 145.653 143.714 124.746 1.00 47.29  ? 2072 PHE A CE2   1 
ATOM   5999  C  CZ    . PHE A 1 2072 ? 144.568 143.203 125.419 1.00 51.21  ? 2072 PHE A CZ    1 
ATOM   6000  N  N     . PHE A 1 2073 ? 146.118 148.542 125.092 1.00 39.85  ? 2073 PHE A N     1 
ATOM   6001  C  CA    . PHE A 1 2073 ? 147.072 148.640 126.190 1.00 37.72  ? 2073 PHE A CA    1 
ATOM   6002  C  C     . PHE A 1 2073 ? 146.635 149.687 127.203 1.00 42.94  ? 2073 PHE A C     1 
ATOM   6003  O  O     . PHE A 1 2073 ? 146.858 149.522 128.407 1.00 48.76  ? 2073 PHE A O     1 
ATOM   6004  C  CB    . PHE A 1 2073 ? 148.468 148.947 125.655 1.00 36.82  ? 2073 PHE A CB    1 
ATOM   6005  C  CG    . PHE A 1 2073 ? 149.324 147.728 125.477 1.00 39.78  ? 2073 PHE A CG    1 
ATOM   6006  C  CD1   . PHE A 1 2073 ? 148.974 146.748 124.568 1.00 40.67  ? 2073 PHE A CD1   1 
ATOM   6007  C  CD2   . PHE A 1 2073 ? 150.469 147.554 126.231 1.00 39.47  ? 2073 PHE A CD2   1 
ATOM   6008  C  CE1   . PHE A 1 2073 ? 149.755 145.625 124.407 1.00 36.90  ? 2073 PHE A CE1   1 
ATOM   6009  C  CE2   . PHE A 1 2073 ? 151.252 146.431 126.074 1.00 38.76  ? 2073 PHE A CE2   1 
ATOM   6010  C  CZ    . PHE A 1 2073 ? 150.894 145.466 125.161 1.00 37.12  ? 2073 PHE A CZ    1 
ATOM   6011  N  N     . LYS A 1 2074 ? 145.940 150.724 126.732 1.00 46.82  ? 2074 LYS A N     1 
ATOM   6012  C  CA    . LYS A 1 2074 ? 145.378 151.716 127.684 1.00 47.89  ? 2074 LYS A CA    1 
ATOM   6013  C  C     . LYS A 1 2074 ? 144.312 151.006 128.534 1.00 51.91  ? 2074 LYS A C     1 
ATOM   6014  O  O     . LYS A 1 2074 ? 144.312 151.197 129.771 1.00 55.76  ? 2074 LYS A O     1 
ATOM   6015  C  CB    . LYS A 1 2074 ? 144.771 152.902 126.930 1.00 48.43  ? 2074 LYS A CB    1 
ATOM   6016  C  CG    . LYS A 1 2074 ? 143.969 153.861 127.798 1.00 60.80  ? 2074 LYS A CG    1 
ATOM   6017  C  CD    . LYS A 1 2074 ? 143.275 154.962 127.007 1.00 62.22  ? 2074 LYS A CD    1 
ATOM   6018  C  CE    . LYS A 1 2074 ? 142.454 155.853 127.883 1.00 64.98  ? 2074 LYS A CE    1 
ATOM   6019  N  NZ    . LYS A 1 2074 ? 143.273 156.499 128.912 1.00 56.99  ? 2074 LYS A NZ    1 
ATOM   6020  N  N     . LEU A 1 2075 ? 143.457 150.201 127.893 1.00 48.78  ? 2075 LEU A N     1 
ATOM   6021  C  CA    . LEU A 1 2075 ? 142.375 149.482 128.618 1.00 45.72  ? 2075 LEU A CA    1 
ATOM   6022  C  C     . LEU A 1 2075 ? 142.990 148.570 129.688 1.00 52.04  ? 2075 LEU A C     1 
ATOM   6023  O  O     . LEU A 1 2075 ? 142.535 148.635 130.847 1.00 56.10  ? 2075 LEU A O     1 
ATOM   6024  C  CB    . LEU A 1 2075 ? 141.541 148.664 127.635 1.00 40.17  ? 2075 LEU A CB    1 
ATOM   6025  C  CG    . LEU A 1 2075 ? 140.704 149.452 126.624 1.00 42.16  ? 2075 LEU A CG    1 
ATOM   6026  C  CD1   . LEU A 1 2075 ? 139.887 148.478 125.795 1.00 46.09  ? 2075 LEU A CD1   1 
ATOM   6027  C  CD2   . LEU A 1 2075 ? 139.799 150.445 127.331 1.00 44.77  ? 2075 LEU A CD2   1 
ATOM   6028  N  N     . CYS A 1 2076 ? 143.977 147.755 129.309 1.00 45.93  ? 2076 CYS A N     1 
ATOM   6029  C  CA    . CYS A 1 2076 ? 144.590 146.797 130.266 1.00 40.15  ? 2076 CYS A CA    1 
ATOM   6030  C  C     . CYS A 1 2076 ? 145.237 147.572 131.421 1.00 46.75  ? 2076 CYS A C     1 
ATOM   6031  O  O     . CYS A 1 2076 ? 145.121 147.117 132.579 1.00 54.70  ? 2076 CYS A O     1 
ATOM   6032  C  CB    . CYS A 1 2076 ? 145.648 145.946 129.577 1.00 42.20  ? 2076 CYS A CB    1 
ATOM   6033  S  SG    . CYS A 1 2076 ? 145.026 145.065 128.122 1.00 54.78  ? 2076 CYS A SG    1 
ATOM   6034  N  N     . ASP A 1 2077 ? 145.883 148.699 131.113 1.00 48.94  ? 2077 ASP A N     1 
ATOM   6035  C  CA    . ASP A 1 2077 ? 146.594 149.486 132.158 1.00 52.64  ? 2077 ASP A CA    1 
ATOM   6036  C  C     . ASP A 1 2077 ? 145.572 150.145 133.090 1.00 58.69  ? 2077 ASP A C     1 
ATOM   6037  O  O     . ASP A 1 2077 ? 145.979 150.604 134.178 1.00 61.25  ? 2077 ASP A O     1 
ATOM   6038  C  CB    . ASP A 1 2077 ? 147.541 150.494 131.525 1.00 54.27  ? 2077 ASP A CB    1 
ATOM   6039  C  CG    . ASP A 1 2077 ? 148.714 150.930 132.391 1.00 67.72  ? 2077 ASP A CG    1 
ATOM   6040  O  OD1   . ASP A 1 2077 ? 148.465 151.494 133.476 1.00 67.03  ? 2077 ASP A OD1   1 
ATOM   6041  O  OD2   . ASP A 1 2077 ? 149.868 150.702 131.971 1.00 72.58  ? 2077 ASP A OD2   1 
ATOM   6042  N  N     . GLU A 1 2078 ? 144.297 150.187 132.688 1.00 60.69  ? 2078 GLU A N     1 
ATOM   6043  C  CA    . GLU A 1 2078 ? 143.276 150.897 133.502 1.00 58.29  ? 2078 GLU A CA    1 
ATOM   6044  C  C     . GLU A 1 2078 ? 142.119 149.958 133.885 1.00 58.59  ? 2078 GLU A C     1 
ATOM   6045  O  O     . GLU A 1 2078 ? 141.172 150.441 134.543 1.00 60.28  ? 2078 GLU A O     1 
ATOM   6046  C  CB    . GLU A 1 2078 ? 142.758 152.095 132.707 1.00 58.35  ? 2078 GLU A CB    1 
ATOM   6047  C  CG    . GLU A 1 2078 ? 143.863 153.066 132.303 1.00 62.21  ? 2078 GLU A CG    1 
ATOM   6048  C  CD    . GLU A 1 2078 ? 143.456 154.074 131.244 1.00 72.20  ? 2078 GLU A CD    1 
ATOM   6049  O  OE1   . GLU A 1 2078 ? 142.294 154.021 130.788 1.00 73.43  ? 2078 GLU A OE1   1 
ATOM   6050  O  OE2   . GLU A 1 2078 ? 144.305 154.912 130.874 1.00 72.24  ? 2078 GLU A OE2   1 
ATOM   6051  N  N     . GLN A 1 2079 ? 142.180 148.682 133.492 1.00 55.97  ? 2079 GLN A N     1 
ATOM   6052  C  CA    . GLN A 1 2079 ? 141.041 147.760 133.762 1.00 56.52  ? 2079 GLN A CA    1 
ATOM   6053  C  C     . GLN A 1 2079 ? 141.550 146.430 134.344 1.00 58.69  ? 2079 GLN A C     1 
ATOM   6054  O  O     . GLN A 1 2079 ? 140.703 145.563 134.651 1.00 64.01  ? 2079 GLN A O     1 
ATOM   6055  C  CB    . GLN A 1 2079 ? 140.219 147.544 132.491 1.00 46.71  ? 2079 GLN A CB    1 
ATOM   6056  C  CG    . GLN A 1 2079 ? 139.406 148.765 132.073 1.00 52.26  ? 2079 GLN A CG    1 
ATOM   6057  C  CD    . GLN A 1 2079 ? 138.598 148.547 130.813 1.00 58.04  ? 2079 GLN A CD    1 
ATOM   6058  O  OE1   . GLN A 1 2079 ? 139.143 148.329 129.725 1.00 61.58  ? 2079 GLN A OE1   1 
ATOM   6059  N  NE2   . GLN A 1 2079 ? 137.282 148.617 130.947 1.00 55.69  ? 2079 GLN A NE2   1 
ATOM   6060  N  N     . LEU A 1 2080 ? 142.869 146.274 134.490 1.00 57.70  ? 2080 LEU A N     1 
ATOM   6061  C  CA    . LEU A 1 2080 ? 143.419 145.044 135.121 1.00 50.15  ? 2080 LEU A CA    1 
ATOM   6062  C  C     . LEU A 1 2080 ? 143.787 145.362 136.579 1.00 53.84  ? 2080 LEU A C     1 
ATOM   6063  O  O     . LEU A 1 2080 ? 144.138 146.530 136.856 1.00 56.90  ? 2080 LEU A O     1 
ATOM   6064  C  CB    . LEU A 1 2080 ? 144.612 144.512 134.328 1.00 44.58  ? 2080 LEU A CB    1 
ATOM   6065  C  CG    . LEU A 1 2080 ? 144.290 143.960 132.936 1.00 43.29  ? 2080 LEU A CG    1 
ATOM   6066  C  CD1   . LEU A 1 2080 ? 145.503 143.282 132.325 1.00 38.79  ? 2080 LEU A CD1   1 
ATOM   6067  C  CD2   . LEU A 1 2080 ? 143.111 143.004 132.990 1.00 44.43  ? 2080 LEU A CD2   1 
ATOM   6068  N  N     . SER A 1 2081 ? 143.708 144.368 137.469 1.00 50.97  ? 2081 SER A N     1 
ATOM   6069  C  CA    . SER A 1 2081 ? 143.974 144.613 138.911 1.00 50.33  ? 2081 SER A CA    1 
ATOM   6070  C  C     . SER A 1 2081 ? 145.321 145.329 139.082 1.00 50.16  ? 2081 SER A C     1 
ATOM   6071  O  O     . SER A 1 2081 ? 146.294 144.929 138.407 1.00 53.48  ? 2081 SER A O     1 
ATOM   6072  C  CB    . SER A 1 2081 ? 143.937 143.329 139.700 1.00 53.75  ? 2081 SER A CB    1 
ATOM   6073  O  OG    . SER A 1 2081 ? 145.024 142.484 139.348 1.00 52.85  ? 2081 SER A OG    1 
ATOM   6074  N  N     . SER A 1 2082 ? 145.367 146.350 139.942 1.00 53.35  ? 2082 SER A N     1 
ATOM   6075  C  CA    . SER A 1 2082 ? 146.636 147.077 140.204 1.00 59.69  ? 2082 SER A CA    1 
ATOM   6076  C  C     . SER A 1 2082 ? 147.711 146.078 140.652 1.00 63.68  ? 2082 SER A C     1 
ATOM   6077  O  O     . SER A 1 2082 ? 147.652 145.632 141.818 1.00 68.80  ? 2082 SER A O     1 
ATOM   6078  C  CB    . SER A 1 2082 ? 146.440 148.165 141.226 1.00 62.26  ? 2082 SER A CB    1 
ATOM   6079  O  OG    . SER A 1 2082 ? 147.667 148.829 141.498 1.00 60.14  ? 2082 SER A OG    1 
ATOM   6080  N  N     . GLN A 1 2083 ? 148.647 145.740 139.761 1.00 54.10  ? 2083 GLN A N     1 
ATOM   6081  C  CA    . GLN A 1 2083 ? 149.695 144.790 140.097 1.00 48.48  ? 2083 GLN A CA    1 
ATOM   6082  C  C     . GLN A 1 2083 ? 151.047 145.393 139.752 1.00 47.82  ? 2083 GLN A C     1 
ATOM   6083  O  O     . GLN A 1 2083 ? 151.201 146.046 138.715 1.00 53.55  ? 2083 GLN A O     1 
ATOM   6084  C  CB    . GLN A 1 2083 ? 149.505 143.467 139.356 1.00 49.19  ? 2083 GLN A CB    1 
ATOM   6085  C  CG    . GLN A 1 2083 ? 148.142 142.831 139.552 1.00 50.35  ? 2083 GLN A CG    1 
ATOM   6086  C  CD    . GLN A 1 2083 ? 147.941 142.303 140.955 1.00 52.37  ? 2083 GLN A CD    1 
ATOM   6087  O  OE1   . GLN A 1 2083 ? 148.711 141.473 141.435 1.00 52.07  ? 2083 GLN A OE1   1 
ATOM   6088  N  NE2   . GLN A 1 2083 ? 146.896 142.778 141.620 1.00 54.43  ? 2083 GLN A NE2   1 
ATOM   6089  N  N     . SER A 1 2084 ? 152.024 145.174 140.632 1.00 46.24  ? 2084 SER A N     1 
ATOM   6090  C  CA    . SER A 1 2084 ? 153.348 145.754 140.433 1.00 49.37  ? 2084 SER A CA    1 
ATOM   6091  C  C     . SER A 1 2084 ? 154.027 145.186 139.193 1.00 52.91  ? 2084 SER A C     1 
ATOM   6092  O  O     . SER A 1 2084 ? 154.687 145.921 138.451 1.00 56.67  ? 2084 SER A O     1 
ATOM   6093  C  CB    . SER A 1 2084 ? 154.211 145.522 141.671 1.00 54.96  ? 2084 SER A CB    1 
ATOM   6094  O  OG    . SER A 1 2084 ? 154.483 144.144 141.848 1.00 64.14  ? 2084 SER A OG    1 
ATOM   6095  N  N     . HIS A 1 2085 ? 153.881 143.882 138.951 1.00 48.99  ? 2085 HIS A N     1 
ATOM   6096  C  CA    . HIS A 1 2085 ? 154.546 143.261 137.813 1.00 45.40  ? 2085 HIS A CA    1 
ATOM   6097  C  C     . HIS A 1 2085 ? 153.889 143.604 136.484 1.00 46.68  ? 2085 HIS A C     1 
ATOM   6098  O  O     . HIS A 1 2085 ? 154.468 143.308 135.435 1.00 53.26  ? 2085 HIS A O     1 
ATOM   6099  C  CB    . HIS A 1 2085 ? 154.592 141.743 137.993 1.00 43.03  ? 2085 HIS A CB    1 
ATOM   6100  C  CG    . HIS A 1 2085 ? 153.247 141.110 138.163 1.00 44.37  ? 2085 HIS A CG    1 
ATOM   6101  N  ND1   . HIS A 1 2085 ? 152.602 141.049 139.379 1.00 48.86  ? 2085 HIS A ND1   1 
ATOM   6102  C  CD2   . HIS A 1 2085 ? 152.434 140.493 137.275 1.00 42.98  ? 2085 HIS A CD2   1 
ATOM   6103  C  CE1   . HIS A 1 2085 ? 151.443 140.432 139.230 1.00 45.06  ? 2085 HIS A CE1   1 
ATOM   6104  N  NE2   . HIS A 1 2085 ? 151.318 140.084 137.962 1.00 42.23  ? 2085 HIS A NE2   1 
ATOM   6105  N  N     . TYR A 1 2086 ? 152.706 144.212 136.501 1.00 45.19  ? 2086 TYR A N     1 
ATOM   6106  C  CA    . TYR A 1 2086 ? 152.067 144.645 135.267 1.00 44.63  ? 2086 TYR A CA    1 
ATOM   6107  C  C     . TYR A 1 2086 ? 152.856 145.789 134.647 1.00 49.19  ? 2086 TYR A C     1 
ATOM   6108  O  O     . TYR A 1 2086 ? 153.287 146.711 135.346 1.00 53.25  ? 2086 TYR A O     1 
ATOM   6109  C  CB    . TYR A 1 2086 ? 150.633 145.094 135.536 1.00 44.46  ? 2086 TYR A CB    1 
ATOM   6110  C  CG    . TYR A 1 2086 ? 149.643 143.974 135.740 1.00 46.26  ? 2086 TYR A CG    1 
ATOM   6111  C  CD1   . TYR A 1 2086 ? 150.048 142.649 135.758 1.00 42.41  ? 2086 TYR A CD1   1 
ATOM   6112  C  CD2   . TYR A 1 2086 ? 148.296 144.247 135.916 1.00 47.60  ? 2086 TYR A CD2   1 
ATOM   6113  C  CE1   . TYR A 1 2086 ? 149.139 141.630 135.946 1.00 40.50  ? 2086 TYR A CE1   1 
ATOM   6114  C  CE2   . TYR A 1 2086 ? 147.384 143.239 136.104 1.00 43.22  ? 2086 TYR A CE2   1 
ATOM   6115  C  CZ    . TYR A 1 2086 ? 147.808 141.933 136.118 1.00 40.38  ? 2086 TYR A CZ    1 
ATOM   6116  O  OH    . TYR A 1 2086 ? 146.890 140.929 136.306 1.00 44.47  ? 2086 TYR A OH    1 
ATOM   6117  N  N     . ASP A 1 2087 ? 153.040 145.735 133.331 1.00 49.87  ? 2087 ASP A N     1 
ATOM   6118  C  CA    . ASP A 1 2087 ? 153.722 146.802 132.599 1.00 48.14  ? 2087 ASP A CA    1 
ATOM   6119  C  C     . ASP A 1 2087 ? 153.061 146.910 131.230 1.00 50.80  ? 2087 ASP A C     1 
ATOM   6120  O  O     . ASP A 1 2087 ? 153.280 146.063 130.360 1.00 50.88  ? 2087 ASP A O     1 
ATOM   6121  C  CB    . ASP A 1 2087 ? 155.217 146.531 132.480 1.00 53.63  ? 2087 ASP A CB    1 
ATOM   6122  C  CG    . ASP A 1 2087 ? 155.963 147.665 131.806 1.00 63.53  ? 2087 ASP A CG    1 
ATOM   6123  O  OD1   . ASP A 1 2087 ? 155.890 148.806 132.307 1.00 69.50  ? 2087 ASP A OD1   1 
ATOM   6124  O  OD2   . ASP A 1 2087 ? 156.628 147.416 130.779 1.00 60.90  ? 2087 ASP A OD2   1 
ATOM   6125  N  N     . PHE A 1 2088 ? 152.240 147.943 131.053 1.00 54.02  ? 2088 PHE A N     1 
ATOM   6126  C  CA    . PHE A 1 2088 ? 151.567 148.218 129.790 1.00 48.66  ? 2088 PHE A CA    1 
ATOM   6127  C  C     . PHE A 1 2088 ? 152.056 149.522 129.169 1.00 49.15  ? 2088 PHE A C     1 
ATOM   6128  O  O     . PHE A 1 2088 ? 151.309 150.202 128.464 1.00 52.86  ? 2088 PHE A O     1 
ATOM   6129  C  CB    . PHE A 1 2088 ? 150.054 148.254 129.988 1.00 45.08  ? 2088 PHE A CB    1 
ATOM   6130  C  CG    . PHE A 1 2088 ? 149.501 147.016 130.628 1.00 44.75  ? 2088 PHE A CG    1 
ATOM   6131  C  CD1   . PHE A 1 2088 ? 149.450 145.824 129.930 1.00 44.36  ? 2088 PHE A CD1   1 
ATOM   6132  C  CD2   . PHE A 1 2088 ? 149.045 147.041 131.933 1.00 46.27  ? 2088 PHE A CD2   1 
ATOM   6133  C  CE1   . PHE A 1 2088 ? 148.947 144.684 130.518 1.00 45.31  ? 2088 PHE A CE1   1 
ATOM   6134  C  CE2   . PHE A 1 2088 ? 148.541 145.902 132.526 1.00 47.87  ? 2088 PHE A CE2   1 
ATOM   6135  C  CZ    . PHE A 1 2088 ? 148.493 144.723 131.817 1.00 48.14  ? 2088 PHE A CZ    1 
ATOM   6136  N  N     . GLY A 1 2089 ? 153.310 149.879 129.427 1.00 48.69  ? 2089 GLY A N     1 
ATOM   6137  C  CA    . GLY A 1 2089 ? 153.879 151.107 128.923 1.00 42.39  ? 2089 GLY A CA    1 
ATOM   6138  C  C     . GLY A 1 2089 ? 154.303 150.990 127.473 1.00 39.01  ? 2089 GLY A C     1 
ATOM   6139  O  O     . GLY A 1 2089 ? 153.945 150.059 126.752 1.00 41.23  ? 2089 GLY A O     1 
ATOM   6140  N  N     . LEU A 1 2090 ? 155.087 151.979 127.042 1.00 36.72  ? 2090 LEU A N     1 
ATOM   6141  C  CA    . LEU A 1 2090 ? 155.527 152.015 125.653 1.00 30.20  ? 2090 LEU A CA    1 
ATOM   6142  C  C     . LEU A 1 2090 ? 156.591 150.960 125.377 1.00 32.83  ? 2090 LEU A C     1 
ATOM   6143  O  O     . LEU A 1 2090 ? 156.615 150.368 124.294 1.00 41.07  ? 2090 LEU A O     1 
ATOM   6144  C  CB    . LEU A 1 2090 ? 156.043 153.410 125.309 1.00 31.86  ? 2090 LEU A CB    1 
ATOM   6145  C  CG    . LEU A 1 2090 ? 156.092 153.791 123.831 1.00 31.13  ? 2090 LEU A CG    1 
ATOM   6146  C  CD1   . LEU A 1 2090 ? 154.831 153.352 123.120 1.00 33.26  ? 2090 LEU A CD1   1 
ATOM   6147  C  CD2   . LEU A 1 2090 ? 156.277 155.287 123.702 1.00 31.84  ? 2090 LEU A CD2   1 
ATOM   6148  N  N     . ARG A 1 2091 ? 157.478 150.709 126.343 1.00 31.55  ? 2091 ARG A N     1 
ATOM   6149  C  CA    . ARG A 1 2091 ? 158.497 149.678 126.165 1.00 33.90  ? 2091 ARG A CA    1 
ATOM   6150  C  C     . ARG A 1 2091 ? 157.864 148.299 126.020 1.00 42.92  ? 2091 ARG A C     1 
ATOM   6151  O  O     . ARG A 1 2091 ? 158.260 147.504 125.157 1.00 44.27  ? 2091 ARG A O     1 
ATOM   6152  C  CB    . ARG A 1 2091 ? 159.472 149.708 127.342 1.00 39.14  ? 2091 ARG A CB    1 
ATOM   6153  C  CG    . ARG A 1 2091 ? 160.506 148.597 127.329 1.00 42.80  ? 2091 ARG A CG    1 
ATOM   6154  C  CD    . ARG A 1 2091 ? 161.636 148.880 128.307 1.00 48.74  ? 2091 ARG A CD    1 
ATOM   6155  N  NE    . ARG A 1 2091 ? 162.555 149.898 127.811 1.00 55.68  ? 2091 ARG A NE    1 
ATOM   6156  C  CZ    . ARG A 1 2091 ? 162.793 151.054 128.416 1.00 58.60  ? 2091 ARG A CZ    1 
ATOM   6157  N  NH1   . ARG A 1 2091 ? 162.187 151.382 129.545 1.00 53.46  ? 2091 ARG A NH1   1 
ATOM   6158  N  NH2   . ARG A 1 2091 ? 163.660 151.903 127.873 1.00 54.37  ? 2091 ARG A NH2   1 
ATOM   6159  N  N     . ALA A 1 2092 ? 156.868 148.001 126.857 1.00 42.05  ? 2092 ALA A N     1 
ATOM   6160  C  CA    . ALA A 1 2092 ? 156.171 146.724 126.760 1.00 35.36  ? 2092 ALA A CA    1 
ATOM   6161  C  C     . ALA A 1 2092 ? 155.418 146.605 125.443 1.00 35.02  ? 2092 ALA A C     1 
ATOM   6162  O  O     . ALA A 1 2092 ? 155.384 145.531 124.833 1.00 39.19  ? 2092 ALA A O     1 
ATOM   6163  C  CB    . ALA A 1 2092 ? 155.218 146.557 127.939 1.00 38.83  ? 2092 ALA A CB    1 
ATOM   6164  N  N     . LEU A 1 2093 ? 154.802 147.699 124.991 1.00 33.34  ? 2093 LEU A N     1 
ATOM   6165  C  CA    . LEU A 1 2093 ? 154.120 147.684 123.703 1.00 30.09  ? 2093 LEU A CA    1 
ATOM   6166  C  C     . LEU A 1 2093 ? 155.095 147.408 122.567 1.00 32.28  ? 2093 LEU A C     1 
ATOM   6167  O  O     . LEU A 1 2093 ? 154.793 146.630 121.655 1.00 39.37  ? 2093 LEU A O     1 
ATOM   6168  C  CB    . LEU A 1 2093 ? 153.397 149.011 123.482 1.00 31.12  ? 2093 LEU A CB    1 
ATOM   6169  C  CG    . LEU A 1 2093 ? 152.646 149.190 122.164 1.00 30.64  ? 2093 LEU A CG    1 
ATOM   6170  C  CD1   . LEU A 1 2093 ? 151.330 148.440 122.189 1.00 37.15  ? 2093 LEU A CD1   1 
ATOM   6171  C  CD2   . LEU A 1 2093 ? 152.417 150.663 121.887 1.00 29.99  ? 2093 LEU A CD2   1 
ATOM   6172  N  N     . LYS A 1 2094 ? 156.273 148.033 122.606 1.00 31.68  ? 2094 LYS A N     1 
ATOM   6173  C  CA    . LYS A 1 2094 ? 157.272 147.794 121.570 1.00 33.62  ? 2094 LYS A CA    1 
ATOM   6174  C  C     . LYS A 1 2094 ? 157.748 146.348 121.586 1.00 35.27  ? 2094 LYS A C     1 
ATOM   6175  O  O     . LYS A 1 2094 ? 157.928 145.731 120.528 1.00 41.27  ? 2094 LYS A O     1 
ATOM   6176  C  CB    . LYS A 1 2094 ? 158.449 148.752 121.749 1.00 35.88  ? 2094 LYS A CB    1 
ATOM   6177  C  CG    . LYS A 1 2094 ? 158.084 150.216 121.580 1.00 33.53  ? 2094 LYS A CG    1 
ATOM   6178  C  CD    . LYS A 1 2094 ? 159.221 151.127 121.995 1.00 34.24  ? 2094 LYS A CD    1 
ATOM   6179  C  CE    . LYS A 1 2094 ? 160.473 150.829 121.194 1.00 41.06  ? 2094 LYS A CE    1 
ATOM   6180  N  NZ    . LYS A 1 2094 ? 161.589 151.746 121.536 1.00 47.63  ? 2094 LYS A NZ    1 
ATOM   6181  N  N     . SER A 1 2095 ? 157.960 145.790 122.780 1.00 34.09  ? 2095 SER A N     1 
ATOM   6182  C  CA    . SER A 1 2095 ? 158.352 144.387 122.876 1.00 34.82  ? 2095 SER A CA    1 
ATOM   6183  C  C     . SER A 1 2095 ? 157.267 143.476 122.317 1.00 34.78  ? 2095 SER A C     1 
ATOM   6184  O  O     . SER A 1 2095 ? 157.564 142.489 121.632 1.00 39.98  ? 2095 SER A O     1 
ATOM   6185  C  CB    . SER A 1 2095 ? 158.663 144.028 124.328 1.00 41.27  ? 2095 SER A CB    1 
ATOM   6186  O  OG    . SER A 1 2095 ? 157.492 144.072 125.123 1.00 45.76  ? 2095 SER A OG    1 
ATOM   6187  N  N     . VAL A 1 2096 ? 156.001 143.794 122.596 1.00 31.03  ? 2096 VAL A N     1 
ATOM   6188  C  CA    . VAL A 1 2096 ? 154.891 143.009 122.064 1.00 27.83  ? 2096 VAL A CA    1 
ATOM   6189  C  C     . VAL A 1 2096 ? 154.868 143.074 120.543 1.00 31.04  ? 2096 VAL A C     1 
ATOM   6190  O  O     . VAL A 1 2096 ? 154.623 142.069 119.870 1.00 38.01  ? 2096 VAL A O     1 
ATOM   6191  C  CB    . VAL A 1 2096 ? 153.560 143.488 122.673 1.00 29.28  ? 2096 VAL A CB    1 
ATOM   6192  C  CG1   . VAL A 1 2096 ? 152.391 143.010 121.840 1.00 30.22  ? 2096 VAL A CG1   1 
ATOM   6193  C  CG2   . VAL A 1 2096 ? 153.426 142.995 124.099 1.00 36.55  ? 2096 VAL A CG2   1 
ATOM   6194  N  N     . LEU A 1 2097 ? 155.112 144.257 119.975 1.00 32.32  ? 2097 LEU A N     1 
ATOM   6195  C  CA    . LEU A 1 2097 ? 155.121 144.387 118.519 1.00 28.96  ? 2097 LEU A CA    1 
ATOM   6196  C  C     . LEU A 1 2097 ? 156.268 143.601 117.895 1.00 32.08  ? 2097 LEU A C     1 
ATOM   6197  O  O     . LEU A 1 2097 ? 156.102 142.974 116.840 1.00 37.05  ? 2097 LEU A O     1 
ATOM   6198  C  CB    . LEU A 1 2097 ? 155.202 145.858 118.121 1.00 27.39  ? 2097 LEU A CB    1 
ATOM   6199  C  CG    . LEU A 1 2097 ? 154.083 146.752 118.645 1.00 28.27  ? 2097 LEU A CG    1 
ATOM   6200  C  CD1   . LEU A 1 2097 ? 154.339 148.183 118.249 1.00 32.08  ? 2097 LEU A CD1   1 
ATOM   6201  C  CD2   . LEU A 1 2097 ? 152.738 146.283 118.128 1.00 32.17  ? 2097 LEU A CD2   1 
ATOM   6202  N  N     . VAL A 1 2098 ? 157.445 143.630 118.523 1.00 32.79  ? 2098 VAL A N     1 
ATOM   6203  C  CA    . VAL A 1 2098 ? 158.570 142.846 118.016 1.00 33.67  ? 2098 VAL A CA    1 
ATOM   6204  C  C     . VAL A 1 2098 ? 158.250 141.356 118.076 1.00 38.34  ? 2098 VAL A C     1 
ATOM   6205  O  O     . VAL A 1 2098 ? 158.547 140.599 117.141 1.00 40.55  ? 2098 VAL A O     1 
ATOM   6206  C  CB    . VAL A 1 2098 ? 159.853 143.184 118.796 1.00 35.90  ? 2098 VAL A CB    1 
ATOM   6207  C  CG1   . VAL A 1 2098 ? 160.985 142.269 118.374 1.00 41.60  ? 2098 VAL A CG1   1 
ATOM   6208  C  CG2   . VAL A 1 2098 ? 160.235 144.634 118.572 1.00 35.51  ? 2098 VAL A CG2   1 
ATOM   6209  N  N     . SER A 1 2099 ? 157.636 140.913 119.175 1.00 35.07  ? 2099 SER A N     1 
ATOM   6210  C  CA    . SER A 1 2099 ? 157.250 139.511 119.292 1.00 32.85  ? 2099 SER A CA    1 
ATOM   6211  C  C     . SER A 1 2099 ? 156.201 139.138 118.251 1.00 35.34  ? 2099 SER A C     1 
ATOM   6212  O  O     . SER A 1 2099 ? 156.209 138.022 117.724 1.00 41.42  ? 2099 SER A O     1 
ATOM   6213  C  CB    . SER A 1 2099 ? 156.740 139.229 120.702 1.00 31.26  ? 2099 SER A CB    1 
ATOM   6214  O  OG    . SER A 1 2099 ? 156.268 137.900 120.814 1.00 53.19  ? 2099 SER A OG    1 
ATOM   6215  N  N     . ALA A 1 2100 ? 155.283 140.058 117.949 1.00 33.74  ? 2100 ALA A N     1 
ATOM   6216  C  CA    . ALA A 1 2100 ? 154.291 139.808 116.908 1.00 30.02  ? 2100 ALA A CA    1 
ATOM   6217  C  C     . ALA A 1 2100 ? 154.951 139.671 115.544 1.00 33.66  ? 2100 ALA A C     1 
ATOM   6218  O  O     . ALA A 1 2100 ? 154.551 138.829 114.733 1.00 45.24  ? 2100 ALA A O     1 
ATOM   6219  C  CB    . ALA A 1 2100 ? 153.252 140.928 116.892 1.00 28.68  ? 2100 ALA A CB    1 
ATOM   6220  N  N     . GLY A 1 2101 ? 155.956 140.499 115.268 1.00 34.39  ? 2101 GLY A N     1 
ATOM   6221  C  CA    . GLY A 1 2101 ? 156.715 140.328 114.041 1.00 37.63  ? 2101 GLY A CA    1 
ATOM   6222  C  C     . GLY A 1 2101 ? 157.409 138.982 113.978 1.00 38.92  ? 2101 GLY A C     1 
ATOM   6223  O  O     . GLY A 1 2101 ? 157.437 138.331 112.929 1.00 45.00  ? 2101 GLY A O     1 
ATOM   6224  N  N     . ASN A 1 2102 ? 157.973 138.543 115.106 1.00 39.20  ? 2102 ASN A N     1 
ATOM   6225  C  CA    . ASN A 1 2102 ? 158.596 137.222 115.160 1.00 44.25  ? 2102 ASN A CA    1 
ATOM   6226  C  C     . ASN A 1 2102 ? 157.582 136.119 114.884 1.00 46.47  ? 2102 ASN A C     1 
ATOM   6227  O  O     . ASN A 1 2102 ? 157.882 135.154 114.173 1.00 49.09  ? 2102 ASN A O     1 
ATOM   6228  C  CB    . ASN A 1 2102 ? 159.258 137.005 116.519 1.00 45.17  ? 2102 ASN A CB    1 
ATOM   6229  C  CG    . ASN A 1 2102 ? 160.424 137.939 116.756 1.00 56.00  ? 2102 ASN A CG    1 
ATOM   6230  O  OD1   . ASN A 1 2102 ? 160.808 138.707 115.875 1.00 58.44  ? 2102 ASN A OD1   1 
ATOM   6231  N  ND2   . ASN A 1 2102 ? 160.995 137.878 117.952 1.00 56.01  ? 2102 ASN A ND2   1 
ATOM   6232  N  N     . VAL A 1 2103 ? 156.380 136.238 115.451 1.00 45.82  ? 2103 VAL A N     1 
ATOM   6233  C  CA    . VAL A 1 2103 ? 155.337 135.239 115.219 1.00 40.01  ? 2103 VAL A CA    1 
ATOM   6234  C  C     . VAL A 1 2103 ? 154.930 135.220 113.750 1.00 44.53  ? 2103 VAL A C     1 
ATOM   6235  O  O     . VAL A 1 2103 ? 154.732 134.152 113.158 1.00 54.45  ? 2103 VAL A O     1 
ATOM   6236  C  CB    . VAL A 1 2103 ? 154.130 135.500 116.138 1.00 37.15  ? 2103 VAL A CB    1 
ATOM   6237  C  CG1   . VAL A 1 2103 ? 152.997 134.552 115.802 1.00 45.81  ? 2103 VAL A CG1   1 
ATOM   6238  C  CG2   . VAL A 1 2103 ? 154.529 135.345 117.590 1.00 41.47  ? 2103 VAL A CG2   1 
ATOM   6239  N  N     . LYS A 1 2104 ? 154.787 136.399 113.143 1.00 42.26  ? 2104 LYS A N     1 
ATOM   6240  C  CA    . LYS A 1 2104 ? 154.442 136.466 111.726 1.00 40.45  ? 2104 LYS A CA    1 
ATOM   6241  C  C     . LYS A 1 2104 ? 155.505 135.784 110.876 1.00 47.18  ? 2104 LYS A C     1 
ATOM   6242  O  O     . LYS A 1 2104 ? 155.192 134.997 109.972 1.00 54.05  ? 2104 LYS A O     1 
ATOM   6243  C  CB    . LYS A 1 2104 ? 154.267 137.924 111.303 1.00 39.74  ? 2104 LYS A CB    1 
ATOM   6244  C  CG    . LYS A 1 2104 ? 153.835 138.121 109.861 1.00 39.43  ? 2104 LYS A CG    1 
ATOM   6245  C  CD    . LYS A 1 2104 ? 153.778 139.601 109.524 1.00 43.85  ? 2104 LYS A CD    1 
ATOM   6246  C  CE    . LYS A 1 2104 ? 153.383 139.844 108.078 1.00 47.48  ? 2104 LYS A CE    1 
ATOM   6247  N  NZ    . LYS A 1 2104 ? 151.993 139.415 107.787 1.00 53.33  ? 2104 LYS A NZ    1 
ATOM   6248  N  N     . ARG A 1 2105 ? 156.776 136.058 111.170 1.00 49.76  ? 2105 ARG A N     1 
ATOM   6249  C  CA    . ARG A 1 2105 ? 157.849 135.453 110.393 1.00 52.01  ? 2105 ARG A CA    1 
ATOM   6250  C  C     . ARG A 1 2105 ? 157.935 133.950 110.617 1.00 57.35  ? 2105 ARG A C     1 
ATOM   6251  O  O     . ARG A 1 2105 ? 158.239 133.207 109.679 1.00 66.02  ? 2105 ARG A O     1 
ATOM   6252  C  CB    . ARG A 1 2105 ? 159.178 136.125 110.723 1.00 49.75  ? 2105 ARG A CB    1 
ATOM   6253  C  CG    . ARG A 1 2105 ? 159.350 137.470 110.051 1.00 45.89  ? 2105 ARG A CG    1 
ATOM   6254  C  CD    . ARG A 1 2105 ? 160.713 138.051 110.345 1.00 53.64  ? 2105 ARG A CD    1 
ATOM   6255  N  NE    . ARG A 1 2105 ? 160.815 138.555 111.709 1.00 52.56  ? 2105 ARG A NE    1 
ATOM   6256  C  CZ    . ARG A 1 2105 ? 160.254 139.677 112.138 1.00 51.49  ? 2105 ARG A CZ    1 
ATOM   6257  N  NH1   . ARG A 1 2105 ? 159.538 140.444 111.334 1.00 50.28  ? 2105 ARG A NH1   1 
ATOM   6258  N  NH2   . ARG A 1 2105 ? 160.423 140.043 113.406 1.00 50.53  ? 2105 ARG A NH2   1 
ATOM   6259  N  N     . GLU A 1 2106 ? 157.667 133.475 111.836 1.00 55.24  ? 2106 GLU A N     1 
ATOM   6260  C  CA    . GLU A 1 2106 ? 157.709 132.034 112.064 1.00 58.96  ? 2106 GLU A CA    1 
ATOM   6261  C  C     . GLU A 1 2106 ? 156.546 131.328 111.378 1.00 63.28  ? 2106 GLU A C     1 
ATOM   6262  O  O     . GLU A 1 2106 ? 156.718 130.215 110.871 1.00 72.06  ? 2106 GLU A O     1 
ATOM   6263  C  CB    . GLU A 1 2106 ? 157.737 131.720 113.564 1.00 55.98  ? 2106 GLU A CB    1 
ATOM   6264  C  CG    . GLU A 1 2106 ? 156.404 131.810 114.283 1.00 60.53  ? 2106 GLU A CG    1 
ATOM   6265  C  CD    . GLU A 1 2106 ? 156.511 131.469 115.756 1.00 68.69  ? 2106 GLU A CD    1 
ATOM   6266  O  OE1   . GLU A 1 2106 ? 157.640 131.222 116.228 1.00 74.25  ? 2106 GLU A OE1   1 
ATOM   6267  O  OE2   . GLU A 1 2106 ? 155.467 131.444 116.441 1.00 68.02  ? 2106 GLU A OE2   1 
ATOM   6268  N  N     . ARG A 1 2107 ? 155.368 131.957 111.325 1.00 58.95  ? 2107 ARG A N     1 
ATOM   6269  C  CA    . ARG A 1 2107 ? 154.274 131.390 110.541 1.00 59.43  ? 2107 ARG A CA    1 
ATOM   6270  C  C     . ARG A 1 2107 ? 154.633 131.339 109.062 1.00 68.51  ? 2107 ARG A C     1 
ATOM   6271  O  O     . ARG A 1 2107 ? 154.344 130.349 108.376 1.00 80.69  ? 2107 ARG A O     1 
ATOM   6272  C  CB    . ARG A 1 2107 ? 152.994 132.198 110.746 1.00 53.63  ? 2107 ARG A CB    1 
ATOM   6273  C  CG    . ARG A 1 2107 ? 152.436 132.163 112.155 1.00 51.52  ? 2107 ARG A CG    1 
ATOM   6274  C  CD    . ARG A 1 2107 ? 150.955 132.500 112.151 1.00 49.64  ? 2107 ARG A CD    1 
ATOM   6275  N  NE    . ARG A 1 2107 ? 150.378 132.481 113.490 1.00 56.95  ? 2107 ARG A NE    1 
ATOM   6276  C  CZ    . ARG A 1 2107 ? 149.088 132.642 113.750 1.00 58.30  ? 2107 ARG A CZ    1 
ATOM   6277  N  NH1   . ARG A 1 2107 ? 148.205 132.822 112.782 1.00 59.53  ? 2107 ARG A NH1   1 
ATOM   6278  N  NH2   . ARG A 1 2107 ? 148.674 132.621 115.013 1.00 54.80  ? 2107 ARG A NH2   1 
ATOM   6279  N  N     . ILE A 1 2108 ? 155.264 132.401 108.553 1.00 72.89  ? 2108 ILE A N     1 
ATOM   6280  C  CA    . ILE A 1 2108 ? 155.676 132.420 107.151 1.00 76.77  ? 2108 ILE A CA    1 
ATOM   6281  C  C     . ILE A 1 2108 ? 156.672 131.300 106.875 1.00 79.54  ? 2108 ILE A C     1 
ATOM   6282  O  O     . ILE A 1 2108 ? 156.576 130.592 105.866 1.00 83.49  ? 2108 ILE A O     1 
ATOM   6283  C  CB    . ILE A 1 2108 ? 156.256 133.798 106.782 1.00 74.13  ? 2108 ILE A CB    1 
ATOM   6284  C  CG1   . ILE A 1 2108 ? 155.132 134.770 106.425 1.00 72.26  ? 2108 ILE A CG1   1 
ATOM   6285  C  CG2   . ILE A 1 2108 ? 157.233 133.683 105.625 1.00 77.63  ? 2108 ILE A CG2   1 
ATOM   6286  C  CD1   . ILE A 1 2108 ? 155.576 136.209 106.369 1.00 69.52  ? 2108 ILE A CD1   1 
ATOM   6287  N  N     . GLN A 1 2109 ? 157.645 131.122 107.772 1.00 76.54  ? 2109 GLN A N     1 
ATOM   6288  C  CA    . GLN A 1 2109 ? 158.633 130.061 107.598 1.00 79.41  ? 2109 GLN A CA    1 
ATOM   6289  C  C     . GLN A 1 2109 ? 157.989 128.683 107.669 1.00 87.99  ? 2109 GLN A C     1 
ATOM   6290  O  O     . GLN A 1 2109 ? 158.371 127.778 106.919 1.00 93.72  ? 2109 GLN A O     1 
ATOM   6291  C  CB    . GLN A 1 2109 ? 159.739 130.190 108.644 1.00 78.39  ? 2109 GLN A CB    1 
ATOM   6292  C  CG    . GLN A 1 2109 ? 160.603 131.427 108.485 1.00 83.60  ? 2109 GLN A CG    1 
ATOM   6293  C  CD    . GLN A 1 2109 ? 161.133 131.585 107.075 1.00 94.33  ? 2109 GLN A CD    1 
ATOM   6294  O  OE1   . GLN A 1 2109 ? 161.799 130.695 106.549 1.00 98.40  ? 2109 GLN A OE1   1 
ATOM   6295  N  NE2   . GLN A 1 2109 ? 160.841 132.722 106.456 1.00 89.81  ? 2109 GLN A NE2   1 
ATOM   6296  N  N     . LYS A 1 2110 ? 157.022 128.498 108.569 1.00 87.28  ? 2110 LYS A N     1 
ATOM   6297  C  CA    . LYS A 1 2110 ? 156.328 127.217 108.659 1.00 85.56  ? 2110 LYS A CA    1 
ATOM   6298  C  C     . LYS A 1 2110 ? 155.586 126.907 107.365 1.00 87.09  ? 2110 LYS A C     1 
ATOM   6299  O  O     . LYS A 1 2110 ? 155.657 125.785 106.847 1.00 93.77  ? 2110 LYS A O     1 
ATOM   6300  C  CB    . LYS A 1 2110 ? 155.362 127.233 109.843 1.00 79.26  ? 2110 LYS A CB    1 
ATOM   6301  C  CG    . LYS A 1 2110 ? 154.836 125.866 110.242 1.00 82.04  ? 2110 LYS A CG    1 
ATOM   6302  C  CD    . LYS A 1 2110 ? 153.524 125.977 111.006 1.00 81.65  ? 2110 LYS A CD    1 
ATOM   6303  C  CE    . LYS A 1 2110 ? 153.549 127.119 112.012 1.00 83.36  ? 2110 LYS A CE    1 
ATOM   6304  N  NZ    . LYS A 1 2110 ? 154.616 126.951 113.039 1.00 87.36  ? 2110 LYS A NZ    1 
ATOM   6305  N  N     . ILE A 1 2111 ? 154.876 127.899 106.822 1.00 85.24  ? 2111 ILE A N     1 
ATOM   6306  C  CA    . ILE A 1 2111 ? 154.158 127.692 105.566 1.00 88.89  ? 2111 ILE A CA    1 
ATOM   6307  C  C     . ILE A 1 2111 ? 155.135 127.393 104.435 1.00 98.32  ? 2111 ILE A C     1 
ATOM   6308  O  O     . ILE A 1 2111 ? 154.891 126.512 103.600 1.00 101.98 ? 2111 ILE A O     1 
ATOM   6309  C  CB    . ILE A 1 2111 ? 153.274 128.911 105.246 1.00 88.73  ? 2111 ILE A CB    1 
ATOM   6310  C  CG1   . ILE A 1 2111 ? 152.213 129.101 106.330 1.00 85.77  ? 2111 ILE A CG1   1 
ATOM   6311  C  CG2   . ILE A 1 2111 ? 152.613 128.748 103.887 1.00 92.11  ? 2111 ILE A CG2   1 
ATOM   6312  C  CD1   . ILE A 1 2111 ? 151.229 127.959 106.428 1.00 93.30  ? 2111 ILE A CD1   1 
ATOM   6313  N  N     . LYS A 1 2112 ? 156.253 128.123 104.386 1.00 99.19  ? 2112 LYS A N     1 
ATOM   6314  C  CA    . LYS A 1 2112 ? 157.239 127.896 103.334 1.00 102.33 ? 2112 LYS A CA    1 
ATOM   6315  C  C     . LYS A 1 2112 ? 157.833 126.496 103.423 1.00 108.17 ? 2112 LYS A C     1 
ATOM   6316  O  O     . LYS A 1 2112 ? 158.003 125.824 102.402 1.00 115.55 ? 2112 LYS A O     1 
ATOM   6317  C  CB    . LYS A 1 2112 ? 158.345 128.948 103.408 1.00 101.48 ? 2112 LYS A CB    1 
ATOM   6318  C  CG    . LYS A 1 2112 ? 159.413 128.779 102.340 1.00 107.62 ? 2112 LYS A CG    1 
ATOM   6319  C  CD    . LYS A 1 2112 ? 160.381 129.946 102.315 1.00 106.66 ? 2112 LYS A CD    1 
ATOM   6320  C  CE    . LYS A 1 2112 ? 161.368 129.867 103.463 1.00 107.22 ? 2112 LYS A CE    1 
ATOM   6321  N  NZ    . LYS A 1 2112 ? 162.323 128.739 103.289 1.00 107.27 ? 2112 LYS A NZ    1 
ATOM   6322  N  N     . ARG A 1 2113 ? 158.157 126.041 104.635 1.00 106.29 ? 2113 ARG A N     1 
ATOM   6323  C  CA    . ARG A 1 2113 ? 158.695 124.695 104.802 1.00 106.16 ? 2113 ARG A CA    1 
ATOM   6324  C  C     . ARG A 1 2113 ? 157.671 123.639 104.408 1.00 109.71 ? 2113 ARG A C     1 
ATOM   6325  O  O     . ARG A 1 2113 ? 158.016 122.640 103.764 1.00 114.40 ? 2113 ARG A O     1 
ATOM   6326  C  CB    . ARG A 1 2113 ? 159.153 124.488 106.245 1.00 102.89 ? 2113 ARG A CB    1 
ATOM   6327  C  CG    . ARG A 1 2113 ? 160.634 124.737 106.467 1.00 104.46 ? 2113 ARG A CG    1 
ATOM   6328  C  CD    . ARG A 1 2113 ? 161.017 124.510 107.918 1.00 104.72 ? 2113 ARG A CD    1 
ATOM   6329  N  NE    . ARG A 1 2113 ? 161.130 125.762 108.655 1.00 105.31 ? 2113 ARG A NE    1 
ATOM   6330  C  CZ    . ARG A 1 2113 ? 160.411 126.068 109.727 1.00 103.66 ? 2113 ARG A CZ    1 
ATOM   6331  N  NH1   . ARG A 1 2113 ? 159.513 125.230 110.218 1.00 98.99  ? 2113 ARG A NH1   1 
ATOM   6332  N  NH2   . ARG A 1 2113 ? 160.598 127.243 110.320 1.00 101.25 ? 2113 ARG A NH2   1 
ATOM   6333  N  N     . GLU A 1 2114 ? 156.405 123.844 104.785 1.00 106.74 ? 2114 GLU A N     1 
ATOM   6334  C  CA    . GLU A 1 2114 ? 155.359 122.904 104.399 1.00 109.60 ? 2114 GLU A CA    1 
ATOM   6335  C  C     . GLU A 1 2114 ? 155.220 122.824 102.885 1.00 115.08 ? 2114 GLU A C     1 
ATOM   6336  O  O     . GLU A 1 2114 ? 155.076 121.732 102.323 1.00 118.21 ? 2114 GLU A O     1 
ATOM   6337  C  CB    . GLU A 1 2114 ? 154.031 123.308 105.038 1.00 105.40 ? 2114 GLU A CB    1 
ATOM   6338  C  CG    . GLU A 1 2114 ? 152.834 122.531 104.525 1.00 111.81 ? 2114 GLU A CG    1 
ATOM   6339  C  CD    . GLU A 1 2114 ? 151.519 123.204 104.858 1.00 114.36 ? 2114 GLU A CD    1 
ATOM   6340  O  OE1   . GLU A 1 2114 ? 151.250 123.426 106.058 1.00 110.04 ? 2114 GLU A OE1   1 
ATOM   6341  O  OE2   . GLU A 1 2114 ? 150.754 123.512 103.921 1.00 120.57 ? 2114 GLU A OE2   1 
ATOM   6342  N  N     . LYS A 1 2115 ? 155.265 123.972 102.205 1.00 115.29 ? 2115 LYS A N     1 
ATOM   6343  C  CA    . LYS A 1 2115 ? 155.155 123.968 100.749 1.00 119.73 ? 2115 LYS A CA    1 
ATOM   6344  C  C     . LYS A 1 2115 ? 156.387 123.350 100.098 1.00 121.54 ? 2115 LYS A C     1 
ATOM   6345  O  O     . LYS A 1 2115 ? 156.278 122.687 99.060  1.00 127.75 ? 2115 LYS A O     1 
ATOM   6346  C  CB    . LYS A 1 2115 ? 154.922 125.389 100.237 1.00 121.75 ? 2115 LYS A CB    1 
ATOM   6347  C  CG    . LYS A 1 2115 ? 153.604 125.992 100.701 1.00 123.02 ? 2115 LYS A CG    1 
ATOM   6348  C  CD    . LYS A 1 2115 ? 153.196 127.176 99.843  1.00 118.97 ? 2115 LYS A CD    1 
ATOM   6349  C  CE    . LYS A 1 2115 ? 154.304 128.209 99.770  1.00 121.07 ? 2115 LYS A CE    1 
ATOM   6350  N  NZ    . LYS A 1 2115 ? 153.951 129.334 98.862  1.00 123.84 ? 2115 LYS A NZ    1 
ATOM   6351  N  N     . GLU A 1 2116 ? 157.568 123.560 100.685 1.00 119.58 ? 2116 GLU A N     1 
ATOM   6352  C  CA    . GLU A 1 2116 ? 158.777 122.931 100.160 1.00 120.44 ? 2116 GLU A CA    1 
ATOM   6353  C  C     . GLU A 1 2116 ? 158.708 121.416 100.284 1.00 121.17 ? 2116 GLU A C     1 
ATOM   6354  O  O     . GLU A 1 2116 ? 159.135 120.692 99.377  1.00 121.53 ? 2116 GLU A O     1 
ATOM   6355  C  CB    . GLU A 1 2116 ? 160.014 123.473 100.878 1.00 119.42 ? 2116 GLU A CB    1 
ATOM   6356  C  CG    . GLU A 1 2116 ? 160.364 124.913 100.536 1.00 122.97 ? 2116 GLU A CG    1 
ATOM   6357  C  CD    . GLU A 1 2116 ? 161.012 125.057 99.171  1.00 131.46 ? 2116 GLU A CD    1 
ATOM   6358  O  OE1   . GLU A 1 2116 ? 161.269 124.026 98.515  1.00 130.06 ? 2116 GLU A OE1   1 
ATOM   6359  O  OE2   . GLU A 1 2116 ? 161.265 126.207 98.753  1.00 131.96 ? 2116 GLU A OE2   1 
ATOM   6360  N  N     . GLU A 1 2117 ? 158.181 120.916 101.405 1.00 121.54 ? 2117 GLU A N     1 
ATOM   6361  C  CA    . GLU A 1 2117 ? 157.994 119.475 101.545 1.00 123.29 ? 2117 GLU A CA    1 
ATOM   6362  C  C     . GLU A 1 2117 ? 157.015 118.945 100.503 1.00 125.80 ? 2117 GLU A C     1 
ATOM   6363  O  O     . GLU A 1 2117 ? 157.206 117.851 99.960  1.00 124.41 ? 2117 GLU A O     1 
ATOM   6364  C  CB    . GLU A 1 2117 ? 157.518 119.135 102.957 1.00 119.73 ? 2117 GLU A CB    1 
ATOM   6365  C  CG    . GLU A 1 2117 ? 158.536 119.441 104.044 1.00 117.90 ? 2117 GLU A CG    1 
ATOM   6366  C  CD    . GLU A 1 2117 ? 157.898 119.638 105.405 1.00 120.79 ? 2117 GLU A CD    1 
ATOM   6367  O  OE1   . GLU A 1 2117 ? 156.659 119.519 105.506 1.00 121.39 ? 2117 GLU A OE1   1 
ATOM   6368  O  OE2   . GLU A 1 2117 ? 158.636 119.911 106.375 1.00 117.39 ? 2117 GLU A OE2   1 
ATOM   6369  N  N     . ARG A 1 2118 ? 155.963 119.706 100.212 1.00 128.10 ? 2118 ARG A N     1 
ATOM   6370  C  CA    . ARG A 1 2118 ? 155.012 119.340 99.171  1.00 128.21 ? 2118 ARG A CA    1 
ATOM   6371  C  C     . ARG A 1 2118 ? 155.576 119.728 97.805  1.00 133.26 ? 2118 ARG A C     1 
ATOM   6372  O  O     . ARG A 1 2118 ? 156.741 120.111 97.667  1.00 133.69 ? 2118 ARG A O     1 
ATOM   6373  C  CB    . ARG A 1 2118 ? 153.661 119.998 99.431  1.00 128.28 ? 2118 ARG A CB    1 
ATOM   6374  C  CG    . ARG A 1 2118 ? 153.049 119.669 100.778 1.00 129.68 ? 2118 ARG A CG    1 
ATOM   6375  C  CD    . ARG A 1 2118 ? 151.969 120.677 101.140 1.00 130.72 ? 2118 ARG A CD    1 
ATOM   6376  N  NE    . ARG A 1 2118 ? 150.973 120.820 100.083 1.00 141.78 ? 2118 ARG A NE    1 
ATOM   6377  C  CZ    . ARG A 1 2118 ? 150.054 119.912 99.785  1.00 144.92 ? 2118 ARG A CZ    1 
ATOM   6378  N  NH1   . ARG A 1 2118 ? 149.954 118.779 100.462 1.00 140.04 ? 2118 ARG A NH1   1 
ATOM   6379  N  NH2   . ARG A 1 2118 ? 149.209 120.148 98.785  1.00 145.09 ? 2118 ARG A NH2   1 
ATOM   6380  N  N     . GLY A 1 2119 ? 154.743 119.632 96.772  1.00 134.21 ? 2119 GLY A N     1 
ATOM   6381  C  CA    . GLY A 1 2119 ? 155.145 120.007 95.430  1.00 135.51 ? 2119 GLY A CA    1 
ATOM   6382  C  C     . GLY A 1 2119 ? 154.661 121.384 95.027  1.00 134.91 ? 2119 GLY A C     1 
ATOM   6383  O  O     . GLY A 1 2119 ? 154.595 121.703 93.836  1.00 136.56 ? 2119 GLY A O     1 
ATOM   6384  N  N     . GLU A 1 2120 ? 154.314 122.208 96.012  1.00 132.12 ? 2120 GLU A N     1 
ATOM   6385  C  CA    . GLU A 1 2120 ? 153.756 123.528 95.758  1.00 134.46 ? 2120 GLU A CA    1 
ATOM   6386  C  C     . GLU A 1 2120 ? 154.864 124.575 95.711  1.00 136.10 ? 2120 GLU A C     1 
ATOM   6387  O  O     . GLU A 1 2120 ? 155.842 124.496 96.459  1.00 133.62 ? 2120 GLU A O     1 
ATOM   6388  C  CB    . GLU A 1 2120 ? 152.731 123.886 96.838  1.00 132.03 ? 2120 GLU A CB    1 
ATOM   6389  C  CG    . GLU A 1 2120 ? 152.127 125.275 96.707  1.00 132.33 ? 2120 GLU A CG    1 
ATOM   6390  C  CD    . GLU A 1 2120 ? 151.570 125.536 95.322  1.00 131.82 ? 2120 GLU A CD    1 
ATOM   6391  O  OE1   . GLU A 1 2120 ? 150.650 124.803 94.902  1.00 128.36 ? 2120 GLU A OE1   1 
ATOM   6392  O  OE2   . GLU A 1 2120 ? 152.054 126.473 94.652  1.00 130.95 ? 2120 GLU A OE2   1 
ATOM   6393  N  N     . ALA A 1 2121 ? 154.703 125.553 94.821  1.00 136.48 ? 2121 ALA A N     1 
ATOM   6394  C  CA    . ALA A 1 2121 ? 155.676 126.626 94.686  1.00 133.26 ? 2121 ALA A CA    1 
ATOM   6395  C  C     . ALA A 1 2121 ? 155.661 127.528 95.919  1.00 133.52 ? 2121 ALA A C     1 
ATOM   6396  O  O     . ALA A 1 2121 ? 154.720 127.524 96.716  1.00 131.47 ? 2121 ALA A O     1 
ATOM   6397  C  CB    . ALA A 1 2121 ? 155.396 127.451 93.430  1.00 127.64 ? 2121 ALA A CB    1 
ATOM   6398  N  N     . VAL A 1 2122 ? 156.726 128.314 96.063  1.00 133.73 ? 2122 VAL A N     1 
ATOM   6399  C  CA    . VAL A 1 2122 ? 156.959 129.137 97.245  1.00 132.31 ? 2122 VAL A CA    1 
ATOM   6400  C  C     . VAL A 1 2122 ? 157.042 130.598 96.826  1.00 132.25 ? 2122 VAL A C     1 
ATOM   6401  O  O     . VAL A 1 2122 ? 157.754 130.937 95.873  1.00 132.03 ? 2122 VAL A O     1 
ATOM   6402  C  CB    . VAL A 1 2122 ? 158.240 128.709 97.985  1.00 130.14 ? 2122 VAL A CB    1 
ATOM   6403  C  CG1   . VAL A 1 2122 ? 158.627 129.748 99.021  1.00 123.62 ? 2122 VAL A CG1   1 
ATOM   6404  C  CG2   . VAL A 1 2122 ? 158.044 127.350 98.637  1.00 124.86 ? 2122 VAL A CG2   1 
ATOM   6405  N  N     . ASP A 1 2123 ? 156.313 131.458 97.537  1.00 127.93 ? 2123 ASP A N     1 
ATOM   6406  C  CA    . ASP A 1 2123 ? 156.376 132.901 97.314  1.00 125.30 ? 2123 ASP A CA    1 
ATOM   6407  C  C     . ASP A 1 2123 ? 156.165 133.584 98.659  1.00 118.41 ? 2123 ASP A C     1 
ATOM   6408  O  O     . ASP A 1 2123 ? 155.086 133.468 99.247  1.00 116.95 ? 2123 ASP A O     1 
ATOM   6409  C  CB    . ASP A 1 2123 ? 155.330 133.348 96.296  1.00 125.99 ? 2123 ASP A CB    1 
ATOM   6410  C  CG    . ASP A 1 2123 ? 155.524 134.785 95.852  1.00 126.58 ? 2123 ASP A CG    1 
ATOM   6411  O  OD1   . ASP A 1 2123 ? 156.522 135.411 96.267  1.00 121.79 ? 2123 ASP A OD1   1 
ATOM   6412  O  OD2   . ASP A 1 2123 ? 154.676 135.288 95.085  1.00 127.67 ? 2123 ASP A OD2   1 
ATOM   6413  N  N     . GLU A 1 2124 ? 157.190 134.296 99.138  1.00 115.06 ? 2124 GLU A N     1 
ATOM   6414  C  CA    . GLU A 1 2124 ? 157.115 134.913 100.461 1.00 113.69 ? 2124 GLU A CA    1 
ATOM   6415  C  C     . GLU A 1 2124 ? 156.001 135.951 100.533 1.00 110.07 ? 2124 GLU A C     1 
ATOM   6416  O  O     . GLU A 1 2124 ? 155.254 136.005 101.518 1.00 106.45 ? 2124 GLU A O     1 
ATOM   6417  C  CB    . GLU A 1 2124 ? 158.458 135.548 100.819 1.00 114.46 ? 2124 GLU A CB    1 
ATOM   6418  C  CG    . GLU A 1 2124 ? 159.641 134.600 100.740 1.00 112.23 ? 2124 GLU A CG    1 
ATOM   6419  C  CD    . GLU A 1 2124 ? 159.952 133.949 102.071 1.00 113.98 ? 2124 GLU A CD    1 
ATOM   6420  O  OE1   . GLU A 1 2124 ? 159.227 134.220 103.051 1.00 108.47 ? 2124 GLU A OE1   1 
ATOM   6421  O  OE2   . GLU A 1 2124 ? 160.925 133.169 102.140 1.00 115.19 ? 2124 GLU A OE2   1 
ATOM   6422  N  N     . GLY A 1 2125 ? 155.878 136.788 99.502  1.00 111.72 ? 2125 GLY A N     1 
ATOM   6423  C  CA    . GLY A 1 2125 ? 154.825 137.791 99.502  1.00 108.60 ? 2125 GLY A CA    1 
ATOM   6424  C  C     . GLY A 1 2125 ? 153.439 137.179 99.472  1.00 111.31 ? 2125 GLY A C     1 
ATOM   6425  O  O     . GLY A 1 2125 ? 152.519 137.670 100.132 1.00 108.59 ? 2125 GLY A O     1 
ATOM   6426  N  N     . GLU A 1 2126 ? 153.269 136.100 98.705  1.00 111.96 ? 2126 GLU A N     1 
ATOM   6427  C  CA    . GLU A 1 2126 ? 151.977 135.424 98.660  1.00 108.87 ? 2126 GLU A CA    1 
ATOM   6428  C  C     . GLU A 1 2126 ? 151.619 134.827 100.015 1.00 106.26 ? 2126 GLU A C     1 
ATOM   6429  O  O     . GLU A 1 2126 ? 150.465 134.908 100.451 1.00 104.67 ? 2126 GLU A O     1 
ATOM   6430  C  CB    . GLU A 1 2126 ? 151.987 134.342 97.581  1.00 110.48 ? 2126 GLU A CB    1 
ATOM   6431  C  CG    . GLU A 1 2126 ? 150.662 133.613 97.434  1.00 111.86 ? 2126 GLU A CG    1 
ATOM   6432  C  CD    . GLU A 1 2126 ? 149.547 134.519 96.947  1.00 112.92 ? 2126 GLU A CD    1 
ATOM   6433  O  OE1   . GLU A 1 2126 ? 149.844 135.528 96.273  1.00 118.20 ? 2126 GLU A OE1   1 
ATOM   6434  O  OE2   . GLU A 1 2126 ? 148.371 134.225 97.243  1.00 110.96 ? 2126 GLU A OE2   1 
ATOM   6435  N  N     . ILE A 1 2127 ? 152.597 134.222 100.694 1.00 105.03 ? 2127 ILE A N     1 
ATOM   6436  C  CA    . ILE A 1 2127 ? 152.352 133.683 102.030 1.00 100.34 ? 2127 ILE A CA    1 
ATOM   6437  C  C     . ILE A 1 2127 ? 151.989 134.803 102.994 1.00 98.21  ? 2127 ILE A C     1 
ATOM   6438  O  O     . ILE A 1 2127 ? 151.102 134.651 103.843 1.00 97.70  ? 2127 ILE A O     1 
ATOM   6439  C  CB    . ILE A 1 2127 ? 153.577 132.890 102.521 1.00 101.51 ? 2127 ILE A CB    1 
ATOM   6440  C  CG1   . ILE A 1 2127 ? 153.871 131.718 101.586 1.00 103.15 ? 2127 ILE A CG1   1 
ATOM   6441  C  CG2   . ILE A 1 2127 ? 153.359 132.394 103.940 1.00 95.10  ? 2127 ILE A CG2   1 
ATOM   6442  C  CD1   . ILE A 1 2127 ? 155.191 131.035 101.868 1.00 101.32 ? 2127 ILE A CD1   1 
ATOM   6443  N  N     . ALA A 1 2128 ? 152.672 135.945 102.884 1.00 95.90  ? 2128 ALA A N     1 
ATOM   6444  C  CA    . ALA A 1 2128 ? 152.374 137.071 103.762 1.00 90.48  ? 2128 ALA A CA    1 
ATOM   6445  C  C     . ALA A 1 2128 ? 150.974 137.620 103.513 1.00 97.23  ? 2128 ALA A C     1 
ATOM   6446  O  O     . ALA A 1 2128 ? 150.292 138.047 104.452 1.00 95.90  ? 2128 ALA A O     1 
ATOM   6447  C  CB    . ALA A 1 2128 ? 153.421 138.168 103.580 1.00 89.56  ? 2128 ALA A CB    1 
ATOM   6448  N  N     . GLU A 1 2129 ? 150.530 137.629 102.253 1.00 98.04  ? 2129 GLU A N     1 
ATOM   6449  C  CA    . GLU A 1 2129 ? 149.230 138.216 101.938 1.00 98.56  ? 2129 GLU A CA    1 
ATOM   6450  C  C     . GLU A 1 2129 ? 148.084 137.387 102.506 1.00 95.96  ? 2129 GLU A C     1 
ATOM   6451  O  O     . GLU A 1 2129 ? 147.176 137.929 103.146 1.00 100.07 ? 2129 GLU A O     1 
ATOM   6452  C  CB    . GLU A 1 2129 ? 149.076 138.376 100.425 1.00 108.19 ? 2129 GLU A CB    1 
ATOM   6453  C  CG    . GLU A 1 2129 ? 149.854 139.547 99.842  1.00 114.58 ? 2129 GLU A CG    1 
ATOM   6454  C  CD    . GLU A 1 2129 ? 149.224 140.892 100.161 1.00 115.57 ? 2129 GLU A CD    1 
ATOM   6455  O  OE1   . GLU A 1 2129 ? 148.105 140.917 100.716 1.00 110.10 ? 2129 GLU A OE1   1 
ATOM   6456  O  OE2   . GLU A 1 2129 ? 149.853 141.928 99.858  1.00 116.75 ? 2129 GLU A OE2   1 
ATOM   6457  N  N     . ASN A 1 2130 ? 148.108 136.072 102.287 1.00 95.84  ? 2130 ASN A N     1 
ATOM   6458  C  CA    . ASN A 1 2130 ? 147.053 135.185 102.781 1.00 92.60  ? 2130 ASN A CA    1 
ATOM   6459  C  C     . ASN A 1 2130 ? 147.384 134.758 104.211 1.00 89.67  ? 2130 ASN A C     1 
ATOM   6460  O  O     . ASN A 1 2130 ? 147.592 133.584 104.524 1.00 83.96  ? 2130 ASN A O     1 
ATOM   6461  C  CB    . ASN A 1 2130 ? 146.859 134.006 101.830 1.00 95.19  ? 2130 ASN A CB    1 
ATOM   6462  C  CG    . ASN A 1 2130 ? 148.104 133.136 101.683 1.00 100.52 ? 2130 ASN A CG    1 
ATOM   6463  O  OD1   . ASN A 1 2130 ? 149.106 133.322 102.372 1.00 99.70  ? 2130 ASN A OD1   1 
ATOM   6464  N  ND2   . ASN A 1 2130 ? 148.039 132.177 100.768 1.00 97.63  ? 2130 ASN A ND2   1 
ATOM   6465  N  N     . LEU A 1 2131 ? 147.387 135.745 105.102 1.00 88.78  ? 2131 LEU A N     1 
ATOM   6466  C  CA    . LEU A 1 2131 ? 147.865 135.549 106.463 1.00 80.92  ? 2131 LEU A CA    1 
ATOM   6467  C  C     . LEU A 1 2131 ? 147.222 136.556 107.412 1.00 73.98  ? 2131 LEU A C     1 
ATOM   6468  O  O     . LEU A 1 2131 ? 147.240 137.764 107.144 1.00 73.08  ? 2131 LEU A O     1 
ATOM   6469  C  CB    . LEU A 1 2131 ? 149.391 135.651 106.479 1.00 78.86  ? 2131 LEU A CB    1 
ATOM   6470  C  CG    . LEU A 1 2131 ? 150.183 135.371 107.749 1.00 69.53  ? 2131 LEU A CG    1 
ATOM   6471  C  CD1   . LEU A 1 2131 ? 151.546 134.824 107.392 1.00 69.00  ? 2131 LEU A CD1   1 
ATOM   6472  C  CD2   . LEU A 1 2131 ? 150.345 136.669 108.487 1.00 62.76  ? 2131 LEU A CD2   1 
ATOM   6473  N  N     . PRO A 1 2132 ? 146.644 136.098 108.532 1.00 73.65  ? 2132 PRO A N     1 
ATOM   6474  C  CA    . PRO A 1 2132 ? 145.955 137.021 109.446 1.00 66.88  ? 2132 PRO A CA    1 
ATOM   6475  C  C     . PRO A 1 2132 ? 146.901 137.763 110.377 1.00 62.37  ? 2132 PRO A C     1 
ATOM   6476  O  O     . PRO A 1 2132 ? 147.553 137.154 111.231 1.00 62.41  ? 2132 PRO A O     1 
ATOM   6477  C  CB    . PRO A 1 2132 ? 145.018 136.095 110.229 1.00 60.48  ? 2132 PRO A CB    1 
ATOM   6478  C  CG    . PRO A 1 2132 ? 145.715 134.776 110.227 1.00 61.92  ? 2132 PRO A CG    1 
ATOM   6479  C  CD    . PRO A 1 2132 ? 146.519 134.692 108.956 1.00 68.41  ? 2132 PRO A CD    1 
ATOM   6480  N  N     . GLU A 1 2133 ? 146.980 139.086 110.221 1.00 56.48  ? 2133 GLU A N     1 
ATOM   6481  C  CA    . GLU A 1 2133 ? 147.850 139.879 111.082 1.00 49.23  ? 2133 GLU A CA    1 
ATOM   6482  C  C     . GLU A 1 2133 ? 147.228 140.087 112.458 1.00 47.78  ? 2133 GLU A C     1 
ATOM   6483  O  O     . GLU A 1 2133 ? 147.942 140.140 113.467 1.00 54.70  ? 2133 GLU A O     1 
ATOM   6484  C  CB    . GLU A 1 2133 ? 148.152 141.223 110.420 1.00 50.54  ? 2133 GLU A CB    1 
ATOM   6485  C  CG    . GLU A 1 2133 ? 149.126 141.141 109.257 1.00 55.89  ? 2133 GLU A CG    1 
ATOM   6486  C  CD    . GLU A 1 2133 ? 148.443 140.812 107.946 1.00 73.25  ? 2133 GLU A CD    1 
ATOM   6487  O  OE1   . GLU A 1 2133 ? 147.199 140.701 107.933 1.00 74.53  ? 2133 GLU A OE1   1 
ATOM   6488  O  OE2   . GLU A 1 2133 ? 149.149 140.664 106.926 1.00 80.69  ? 2133 GLU A OE2   1 
ATOM   6489  N  N     . GLN A 1 2134 ? 145.902 140.216 112.518 1.00 45.16  ? 2134 GLN A N     1 
ATOM   6490  C  CA    . GLN A 1 2134 ? 145.235 140.451 113.794 1.00 44.52  ? 2134 GLN A CA    1 
ATOM   6491  C  C     . GLN A 1 2134 ? 145.380 139.251 114.717 1.00 48.76  ? 2134 GLN A C     1 
ATOM   6492  O  O     . GLN A 1 2134 ? 145.577 139.407 115.928 1.00 45.47  ? 2134 GLN A O     1 
ATOM   6493  C  CB    . GLN A 1 2134 ? 143.761 140.769 113.557 1.00 52.45  ? 2134 GLN A CB    1 
ATOM   6494  C  CG    . GLN A 1 2134 ? 143.544 142.060 112.799 1.00 55.93  ? 2134 GLN A CG    1 
ATOM   6495  C  CD    . GLN A 1 2134 ? 142.086 142.412 112.640 1.00 61.75  ? 2134 GLN A CD    1 
ATOM   6496  O  OE1   . GLN A 1 2134 ? 141.740 143.428 112.039 1.00 67.94  ? 2134 GLN A OE1   1 
ATOM   6497  N  NE2   . GLN A 1 2134 ? 141.219 141.594 113.219 1.00 64.50  ? 2134 GLN A NE2   1 
ATOM   6498  N  N     . GLU A 1 2135 ? 145.281 138.041 114.160 1.00 52.24  ? 2135 GLU A N     1 
ATOM   6499  C  CA    . GLU A 1 2135 ? 145.458 136.835 114.960 1.00 45.06  ? 2135 GLU A CA    1 
ATOM   6500  C  C     . GLU A 1 2135 ? 146.879 136.735 115.498 1.00 46.20  ? 2135 GLU A C     1 
ATOM   6501  O  O     . GLU A 1 2135 ? 147.091 136.307 116.636 1.00 45.10  ? 2135 GLU A O     1 
ATOM   6502  C  CB    . GLU A 1 2135 ? 145.099 135.601 114.137 1.00 52.34  ? 2135 GLU A CB    1 
ATOM   6503  C  CG    . GLU A 1 2135 ? 143.630 135.534 113.757 1.00 65.40  ? 2135 GLU A CG    1 
ATOM   6504  C  CD    . GLU A 1 2135 ? 143.066 134.131 113.841 1.00 74.44  ? 2135 GLU A CD    1 
ATOM   6505  O  OE1   . GLU A 1 2135 ? 143.668 133.288 114.539 1.00 74.68  ? 2135 GLU A OE1   1 
ATOM   6506  O  OE2   . GLU A 1 2135 ? 142.018 133.872 113.212 1.00 73.46  ? 2135 GLU A OE2   1 
ATOM   6507  N  N     . ILE A 1 2136 ? 147.867 137.135 114.702 1.00 48.35  ? 2136 ILE A N     1 
ATOM   6508  C  CA    . ILE A 1 2136 ? 149.246 137.122 115.178 1.00 41.53  ? 2136 ILE A CA    1 
ATOM   6509  C  C     . ILE A 1 2136 ? 149.449 138.152 116.281 1.00 39.23  ? 2136 ILE A C     1 
ATOM   6510  O  O     . ILE A 1 2136 ? 150.132 137.889 117.279 1.00 43.93  ? 2136 ILE A O     1 
ATOM   6511  C  CB    . ILE A 1 2136 ? 150.208 137.341 114.000 1.00 37.00  ? 2136 ILE A CB    1 
ATOM   6512  C  CG1   . ILE A 1 2136 ? 150.167 136.121 113.089 1.00 43.14  ? 2136 ILE A CG1   1 
ATOM   6513  C  CG2   . ILE A 1 2136 ? 151.607 137.617 114.491 1.00 36.18  ? 2136 ILE A CG2   1 
ATOM   6514  C  CD1   . ILE A 1 2136 ? 150.899 136.307 111.823 1.00 46.52  ? 2136 ILE A CD1   1 
ATOM   6515  N  N     . LEU A 1 2137 ? 148.863 139.340 116.123 1.00 38.95  ? 2137 LEU A N     1 
ATOM   6516  C  CA    . LEU A 1 2137 ? 148.998 140.360 117.156 1.00 39.71  ? 2137 LEU A CA    1 
ATOM   6517  C  C     . LEU A 1 2137 ? 148.350 139.912 118.462 1.00 42.46  ? 2137 LEU A C     1 
ATOM   6518  O  O     . LEU A 1 2137 ? 148.935 140.071 119.541 1.00 41.02  ? 2137 LEU A O     1 
ATOM   6519  C  CB    . LEU A 1 2137 ? 148.395 141.678 116.672 1.00 41.47  ? 2137 LEU A CB    1 
ATOM   6520  C  CG    . LEU A 1 2137 ? 148.676 142.905 117.538 1.00 42.20  ? 2137 LEU A CG    1 
ATOM   6521  C  CD1   . LEU A 1 2137 ? 150.162 143.214 117.549 1.00 41.28  ? 2137 LEU A CD1   1 
ATOM   6522  C  CD2   . LEU A 1 2137 ? 147.887 144.100 117.041 1.00 39.54  ? 2137 LEU A CD2   1 
ATOM   6523  N  N     . ILE A 1 2138 ? 147.149 139.330 118.384 1.00 45.59  ? 2138 ILE A N     1 
ATOM   6524  C  CA    . ILE A 1 2138 ? 146.479 138.858 119.593 1.00 43.05  ? 2138 ILE A CA    1 
ATOM   6525  C  C     . ILE A 1 2138 ? 147.250 137.697 120.213 1.00 44.24  ? 2138 ILE A C     1 
ATOM   6526  O  O     . ILE A 1 2138 ? 147.342 137.586 121.441 1.00 45.74  ? 2138 ILE A O     1 
ATOM   6527  C  CB    . ILE A 1 2138 ? 145.013 138.485 119.291 1.00 46.15  ? 2138 ILE A CB    1 
ATOM   6528  C  CG1   . ILE A 1 2138 ? 144.287 138.029 120.545 1.00 52.61  ? 2138 ILE A CG1   1 
ATOM   6529  C  CG2   . ILE A 1 2138 ? 144.911 137.349 118.336 1.00 56.17  ? 2138 ILE A CG2   1 
ATOM   6530  C  CD1   . ILE A 1 2138 ? 142.797 137.871 120.333 1.00 65.33  ? 2138 ILE A CD1   1 
ATOM   6531  N  N     . GLN A 1 2139 ? 147.837 136.827 119.383 1.00 44.13  ? 2139 GLN A N     1 
ATOM   6532  C  CA    . GLN A 1 2139 ? 148.636 135.726 119.910 1.00 41.31  ? 2139 GLN A CA    1 
ATOM   6533  C  C     . GLN A 1 2139 ? 149.860 136.236 120.655 1.00 44.69  ? 2139 GLN A C     1 
ATOM   6534  O  O     . GLN A 1 2139 ? 150.186 135.739 121.737 1.00 50.95  ? 2139 GLN A O     1 
ATOM   6535  C  CB    . GLN A 1 2139 ? 149.056 134.793 118.777 1.00 42.32  ? 2139 GLN A CB    1 
ATOM   6536  C  CG    . GLN A 1 2139 ? 150.220 133.886 119.128 1.00 45.46  ? 2139 GLN A CG    1 
ATOM   6537  C  CD    . GLN A 1 2139 ? 150.568 132.927 118.013 1.00 54.02  ? 2139 GLN A CD    1 
ATOM   6538  O  OE1   . GLN A 1 2139 ? 149.900 132.890 116.981 1.00 55.75  ? 2139 GLN A OE1   1 
ATOM   6539  N  NE2   . GLN A 1 2139 ? 151.621 132.145 118.212 1.00 53.40  ? 2139 GLN A NE2   1 
ATOM   6540  N  N     . SER A 1 2140 ? 150.556 137.223 120.087 1.00 42.52  ? 2140 SER A N     1 
ATOM   6541  C  CA    . SER A 1 2140 ? 151.720 137.787 120.763 1.00 36.96  ? 2140 SER A CA    1 
ATOM   6542  C  C     . SER A 1 2140 ? 151.325 138.468 122.066 1.00 35.69  ? 2140 SER A C     1 
ATOM   6543  O  O     . SER A 1 2140 ? 151.994 138.299 123.095 1.00 37.15  ? 2140 SER A O     1 
ATOM   6544  C  CB    . SER A 1 2140 ? 152.434 138.770 119.842 1.00 31.48  ? 2140 SER A CB    1 
ATOM   6545  O  OG    . SER A 1 2140 ? 153.526 139.375 120.504 1.00 35.75  ? 2140 SER A OG    1 
ATOM   6546  N  N     . VAL A 1 2141 ? 150.230 139.232 122.046 1.00 38.69  ? 2141 VAL A N     1 
ATOM   6547  C  CA    . VAL A 1 2141 ? 149.767 139.900 123.259 1.00 38.19  ? 2141 VAL A CA    1 
ATOM   6548  C  C     . VAL A 1 2141 ? 149.453 138.877 124.342 1.00 40.51  ? 2141 VAL A C     1 
ATOM   6549  O  O     . VAL A 1 2141 ? 149.840 139.039 125.505 1.00 45.81  ? 2141 VAL A O     1 
ATOM   6550  C  CB    . VAL A 1 2141 ? 148.545 140.783 122.956 1.00 37.49  ? 2141 VAL A CB    1 
ATOM   6551  C  CG1   . VAL A 1 2141 ? 147.927 141.264 124.246 1.00 37.10  ? 2141 VAL A CG1   1 
ATOM   6552  C  CG2   . VAL A 1 2141 ? 148.945 141.958 122.094 1.00 39.41  ? 2141 VAL A CG2   1 
ATOM   6553  N  N     . CYS A 1 2142 ? 148.740 137.810 123.977 1.00 41.13  ? 2142 CYS A N     1 
ATOM   6554  C  CA    . CYS A 1 2142 ? 148.402 136.787 124.958 1.00 44.40  ? 2142 CYS A CA    1 
ATOM   6555  C  C     . CYS A 1 2142 ? 149.648 136.087 125.482 1.00 46.08  ? 2142 CYS A C     1 
ATOM   6556  O  O     . CYS A 1 2142 ? 149.830 135.973 126.696 1.00 52.37  ? 2142 CYS A O     1 
ATOM   6557  C  CB    . CYS A 1 2142 ? 147.431 135.777 124.352 1.00 50.50  ? 2142 CYS A CB    1 
ATOM   6558  S  SG    . CYS A 1 2142 ? 145.811 136.455 123.952 1.00 64.32  ? 2142 CYS A SG    1 
ATOM   6559  N  N     . GLU A 1 2143 ? 150.537 135.652 124.588 1.00 41.23  ? 2143 GLU A N     1 
ATOM   6560  C  CA    . GLU A 1 2143 ? 151.741 134.952 125.012 1.00 40.24  ? 2143 GLU A CA    1 
ATOM   6561  C  C     . GLU A 1 2143 ? 152.645 135.819 125.874 1.00 40.67  ? 2143 GLU A C     1 
ATOM   6562  O  O     . GLU A 1 2143 ? 153.449 135.280 126.640 1.00 44.41  ? 2143 GLU A O     1 
ATOM   6563  C  CB    . GLU A 1 2143 ? 152.512 134.452 123.792 1.00 42.85  ? 2143 GLU A CB    1 
ATOM   6564  C  CG    . GLU A 1 2143 ? 152.263 132.993 123.466 1.00 59.62  ? 2143 GLU A CG    1 
ATOM   6565  C  CD    . GLU A 1 2143 ? 152.955 132.557 122.193 1.00 70.63  ? 2143 GLU A CD    1 
ATOM   6566  O  OE1   . GLU A 1 2143 ? 153.637 133.396 121.569 1.00 64.19  ? 2143 GLU A OE1   1 
ATOM   6567  O  OE2   . GLU A 1 2143 ? 152.814 131.375 121.815 1.00 70.08  ? 2143 GLU A OE2   1 
ATOM   6568  N  N     . THR A 1 2144 ? 152.539 137.143 125.769 1.00 40.87  ? 2144 THR A N     1 
ATOM   6569  C  CA    . THR A 1 2144 ? 153.350 138.005 126.617 1.00 37.79  ? 2144 THR A CA    1 
ATOM   6570  C  C     . THR A 1 2144 ? 152.666 138.373 127.930 1.00 40.22  ? 2144 THR A C     1 
ATOM   6571  O  O     . THR A 1 2144 ? 153.347 138.499 128.953 1.00 42.47  ? 2144 THR A O     1 
ATOM   6572  C  CB    . THR A 1 2144 ? 153.730 139.281 125.858 1.00 41.12  ? 2144 THR A CB    1 
ATOM   6573  O  OG1   . THR A 1 2144 ? 154.246 138.933 124.567 1.00 37.27  ? 2144 THR A OG1   1 
ATOM   6574  C  CG2   . THR A 1 2144 ? 154.792 140.057 126.614 1.00 42.73  ? 2144 THR A CG2   1 
ATOM   6575  N  N     . MET A 1 2145 ? 151.341 138.529 127.943 1.00 40.52  ? 2145 MET A N     1 
ATOM   6576  C  CA    . MET A 1 2145 ? 150.656 139.056 129.119 1.00 37.10  ? 2145 MET A CA    1 
ATOM   6577  C  C     . MET A 1 2145 ? 149.955 138.003 129.968 1.00 35.70  ? 2145 MET A C     1 
ATOM   6578  O  O     . MET A 1 2145 ? 149.882 138.173 131.188 1.00 41.63  ? 2145 MET A O     1 
ATOM   6579  C  CB    . MET A 1 2145 ? 149.626 140.113 128.704 1.00 42.30  ? 2145 MET A CB    1 
ATOM   6580  C  CG    . MET A 1 2145 ? 150.173 141.213 127.810 1.00 48.77  ? 2145 MET A CG    1 
ATOM   6581  S  SD    . MET A 1 2145 ? 151.043 142.490 128.736 1.00 79.74  ? 2145 MET A SD    1 
ATOM   6582  C  CE    . MET A 1 2145 ? 152.508 142.703 127.731 1.00 53.96  ? 2145 MET A CE    1 
ATOM   6583  N  N     . VAL A 1 2146 ? 149.422 136.936 129.365 1.00 33.68  ? 2146 VAL A N     1 
ATOM   6584  C  CA    . VAL A 1 2146 ? 148.633 135.966 130.133 1.00 36.90  ? 2146 VAL A CA    1 
ATOM   6585  C  C     . VAL A 1 2146 ? 149.425 135.328 131.265 1.00 42.48  ? 2146 VAL A C     1 
ATOM   6586  O  O     . VAL A 1 2146 ? 148.881 135.206 132.373 1.00 44.85  ? 2146 VAL A O     1 
ATOM   6587  C  CB    . VAL A 1 2146 ? 148.000 134.937 129.186 1.00 34.56  ? 2146 VAL A CB    1 
ATOM   6588  C  CG1   . VAL A 1 2146 ? 147.502 133.730 129.961 1.00 40.00  ? 2146 VAL A CG1   1 
ATOM   6589  C  CG2   . VAL A 1 2146 ? 146.864 135.572 128.405 1.00 38.03  ? 2146 VAL A CG2   1 
ATOM   6590  N  N     . PRO A 1 2147 ? 150.680 134.897 131.085 1.00 36.12  ? 2147 PRO A N     1 
ATOM   6591  C  CA    . PRO A 1 2147 ? 151.402 134.305 132.224 1.00 32.00  ? 2147 PRO A CA    1 
ATOM   6592  C  C     . PRO A 1 2147 ? 151.546 135.234 133.418 1.00 32.00  ? 2147 PRO A C     1 
ATOM   6593  O  O     . PRO A 1 2147 ? 151.655 134.752 134.551 1.00 38.53  ? 2147 PRO A O     1 
ATOM   6594  C  CB    . PRO A 1 2147 ? 152.766 133.948 131.620 1.00 33.26  ? 2147 PRO A CB    1 
ATOM   6595  C  CG    . PRO A 1 2147 ? 152.484 133.730 130.191 1.00 34.62  ? 2147 PRO A CG    1 
ATOM   6596  C  CD    . PRO A 1 2147 ? 151.445 134.743 129.834 1.00 34.94  ? 2147 PRO A CD    1 
ATOM   6597  N  N     . LYS A 1 2148 ? 151.548 136.546 133.207 1.00 32.67  ? 2148 LYS A N     1 
ATOM   6598  C  CA    . LYS A 1 2148 ? 151.695 137.505 134.292 1.00 33.08  ? 2148 LYS A CA    1 
ATOM   6599  C  C     . LYS A 1 2148 ? 150.374 137.859 134.960 1.00 34.34  ? 2148 LYS A C     1 
ATOM   6600  O  O     . LYS A 1 2148 ? 150.376 138.590 135.955 1.00 37.40  ? 2148 LYS A O     1 
ATOM   6601  C  CB    . LYS A 1 2148 ? 152.355 138.786 133.776 1.00 34.75  ? 2148 LYS A CB    1 
ATOM   6602  C  CG    . LYS A 1 2148 ? 153.499 138.547 132.812 1.00 39.56  ? 2148 LYS A CG    1 
ATOM   6603  C  CD    . LYS A 1 2148 ? 154.060 139.854 132.285 1.00 43.18  ? 2148 LYS A CD    1 
ATOM   6604  C  CE    . LYS A 1 2148 ? 155.262 139.607 131.392 1.00 47.76  ? 2148 LYS A CE    1 
ATOM   6605  N  NZ    . LYS A 1 2148 ? 155.824 140.874 130.856 1.00 56.95  ? 2148 LYS A NZ    1 
ATOM   6606  N  N     . LEU A 1 2149 ? 149.254 137.362 134.447 1.00 34.28  ? 2149 LEU A N     1 
ATOM   6607  C  CA    . LEU A 1 2149 ? 147.941 137.778 134.915 1.00 38.25  ? 2149 LEU A CA    1 
ATOM   6608  C  C     . LEU A 1 2149 ? 147.489 136.950 136.108 1.00 45.15  ? 2149 LEU A C     1 
ATOM   6609  O  O     . LEU A 1 2149 ? 147.693 135.734 136.153 1.00 50.24  ? 2149 LEU A O     1 
ATOM   6610  C  CB    . LEU A 1 2149 ? 146.908 137.656 133.796 1.00 39.23  ? 2149 LEU A CB    1 
ATOM   6611  C  CG    . LEU A 1 2149 ? 146.963 138.671 132.659 1.00 35.24  ? 2149 LEU A CG    1 
ATOM   6612  C  CD1   . LEU A 1 2149 ? 145.643 138.661 131.939 1.00 35.68  ? 2149 LEU A CD1   1 
ATOM   6613  C  CD2   . LEU A 1 2149 ? 147.281 140.062 133.171 1.00 31.84  ? 2149 LEU A CD2   1 
ATOM   6614  N  N     . VAL A 1 2150 ? 146.861 137.621 137.071 1.00 39.61  ? 2150 VAL A N     1 
ATOM   6615  C  CA    . VAL A 1 2150 ? 146.203 136.946 138.181 1.00 41.50  ? 2150 VAL A CA    1 
ATOM   6616  C  C     . VAL A 1 2150 ? 144.912 136.334 137.656 1.00 48.37  ? 2150 VAL A C     1 
ATOM   6617  O  O     . VAL A 1 2150 ? 144.479 136.643 136.541 1.00 49.68  ? 2150 VAL A O     1 
ATOM   6618  C  CB    . VAL A 1 2150 ? 145.938 137.912 139.348 1.00 41.21  ? 2150 VAL A CB    1 
ATOM   6619  C  CG1   . VAL A 1 2150 ? 147.222 138.609 139.755 1.00 38.08  ? 2150 VAL A CG1   1 
ATOM   6620  C  CG2   . VAL A 1 2150 ? 144.882 138.924 138.963 1.00 46.20  ? 2150 VAL A CG2   1 
ATOM   6621  N  N     . ALA A 1 2151 ? 144.289 135.460 138.449 1.00 53.81  ? 2151 ALA A N     1 
ATOM   6622  C  CA    . ALA A 1 2151 ? 143.116 134.733 137.972 1.00 53.35  ? 2151 ALA A CA    1 
ATOM   6623  C  C     . ALA A 1 2151 ? 141.952 135.664 137.659 1.00 54.85  ? 2151 ALA A C     1 
ATOM   6624  O  O     . ALA A 1 2151 ? 141.146 135.369 136.770 1.00 54.07  ? 2151 ALA A O     1 
ATOM   6625  C  CB    . ALA A 1 2151 ? 142.689 133.689 139.003 1.00 59.22  ? 2151 ALA A CB    1 
ATOM   6626  N  N     . GLU A 1 2152 ? 141.842 136.783 138.376 1.00 55.24  ? 2152 GLU A N     1 
ATOM   6627  C  CA    . GLU A 1 2152 ? 140.719 137.688 138.156 1.00 57.05  ? 2152 GLU A CA    1 
ATOM   6628  C  C     . GLU A 1 2152 ? 140.876 138.492 136.871 1.00 57.26  ? 2152 GLU A C     1 
ATOM   6629  O  O     . GLU A 1 2152 ? 139.874 138.910 136.280 1.00 57.48  ? 2152 GLU A O     1 
ATOM   6630  C  CB    . GLU A 1 2152 ? 140.558 138.629 139.350 1.00 54.24  ? 2152 GLU A CB    1 
ATOM   6631  C  CG    . GLU A 1 2152 ? 140.523 137.931 140.702 1.00 68.23  ? 2152 GLU A CG    1 
ATOM   6632  C  CD    . GLU A 1 2152 ? 141.903 137.753 141.308 1.00 72.97  ? 2152 GLU A CD    1 
ATOM   6633  O  OE1   . GLU A 1 2152 ? 142.657 138.747 141.375 1.00 71.78  ? 2152 GLU A OE1   1 
ATOM   6634  O  OE2   . GLU A 1 2152 ? 142.233 136.621 141.719 1.00 67.63  ? 2152 GLU A OE2   1 
ATOM   6635  N  N     . ASP A 1 2153 ? 142.111 138.717 136.425 1.00 51.80  ? 2153 ASP A N     1 
ATOM   6636  C  CA    . ASP A 1 2153 ? 142.378 139.602 135.300 1.00 41.60  ? 2153 ASP A CA    1 
ATOM   6637  C  C     . ASP A 1 2153 ? 142.355 138.907 133.946 1.00 45.95  ? 2153 ASP A C     1 
ATOM   6638  O  O     . ASP A 1 2153 ? 142.380 139.594 132.921 1.00 51.42  ? 2153 ASP A O     1 
ATOM   6639  C  CB    . ASP A 1 2153 ? 143.735 140.285 135.482 1.00 36.20  ? 2153 ASP A CB    1 
ATOM   6640  C  CG    . ASP A 1 2153 ? 143.742 141.260 136.635 1.00 48.37  ? 2153 ASP A CG    1 
ATOM   6641  O  OD1   . ASP A 1 2153 ? 142.660 141.520 137.201 1.00 59.09  ? 2153 ASP A OD1   1 
ATOM   6642  O  OD2   . ASP A 1 2153 ? 144.829 141.763 136.981 1.00 43.03  ? 2153 ASP A OD2   1 
ATOM   6643  N  N     . ILE A 1 2154 ? 142.316 137.580 133.904 1.00 48.77  ? 2154 ILE A N     1 
ATOM   6644  C  CA    . ILE A 1 2154 ? 142.312 136.866 132.628 1.00 50.45  ? 2154 ILE A CA    1 
ATOM   6645  C  C     . ILE A 1 2154 ? 140.968 137.049 131.927 1.00 53.62  ? 2154 ILE A C     1 
ATOM   6646  O  O     . ILE A 1 2154 ? 140.952 137.392 130.733 1.00 56.23  ? 2154 ILE A O     1 
ATOM   6647  C  CB    . ILE A 1 2154 ? 142.660 135.380 132.815 1.00 49.83  ? 2154 ILE A CB    1 
ATOM   6648  C  CG1   . ILE A 1 2154 ? 143.877 135.230 133.726 1.00 49.66  ? 2154 ILE A CG1   1 
ATOM   6649  C  CG2   . ILE A 1 2154 ? 142.928 134.725 131.476 1.00 45.85  ? 2154 ILE A CG2   1 
ATOM   6650  C  CD1   . ILE A 1 2154 ? 144.330 133.802 133.910 1.00 52.53  ? 2154 ILE A CD1   1 
ATOM   6651  N  N     . PRO A 1 2155 ? 139.809 136.846 132.600 1.00 52.37  ? 2155 PRO A N     1 
ATOM   6652  C  CA    . PRO A 1 2155 ? 138.526 137.108 131.964 1.00 51.10  ? 2155 PRO A CA    1 
ATOM   6653  C  C     . PRO A 1 2155 ? 138.474 138.561 131.519 1.00 54.62  ? 2155 PRO A C     1 
ATOM   6654  O  O     . PRO A 1 2155 ? 138.010 138.838 130.394 1.00 54.18  ? 2155 PRO A O     1 
ATOM   6655  C  CB    . PRO A 1 2155 ? 137.495 136.791 133.058 1.00 50.41  ? 2155 PRO A CB    1 
ATOM   6656  C  CG    . PRO A 1 2155 ? 138.284 136.881 134.344 1.00 51.42  ? 2155 PRO A CG    1 
ATOM   6657  C  CD    . PRO A 1 2155 ? 139.663 136.366 133.972 1.00 52.24  ? 2155 PRO A CD    1 
ATOM   6658  N  N     . LEU A 1 2156 ? 138.948 139.470 132.376 1.00 50.42  ? 2156 LEU A N     1 
ATOM   6659  C  CA    . LEU A 1 2156 ? 138.951 140.917 132.036 1.00 45.58  ? 2156 LEU A CA    1 
ATOM   6660  C  C     . LEU A 1 2156 ? 139.799 141.131 130.774 1.00 53.89  ? 2156 LEU A C     1 
ATOM   6661  O  O     . LEU A 1 2156 ? 139.310 141.789 129.832 1.00 61.32  ? 2156 LEU A O     1 
ATOM   6662  C  CB    . LEU A 1 2156 ? 139.499 141.720 133.214 1.00 41.08  ? 2156 LEU A CB    1 
ATOM   6663  C  CG    . LEU A 1 2156 ? 138.827 141.471 134.567 1.00 55.05  ? 2156 LEU A CG    1 
ATOM   6664  C  CD1   . LEU A 1 2156 ? 139.505 142.284 135.656 1.00 54.24  ? 2156 LEU A CD1   1 
ATOM   6665  C  CD2   . LEU A 1 2156 ? 137.344 141.795 134.499 1.00 68.50  ? 2156 LEU A CD2   1 
ATOM   6666  N  N     . LEU A 1 2157 ? 141.016 140.580 130.757 1.00 48.09  ? 2157 LEU A N     1 
ATOM   6667  C  CA    . LEU A 1 2157 ? 141.913 140.748 129.585 1.00 42.00  ? 2157 LEU A CA    1 
ATOM   6668  C  C     . LEU A 1 2157 ? 141.171 140.287 128.324 1.00 47.41  ? 2157 LEU A C     1 
ATOM   6669  O  O     . LEU A 1 2157 ? 141.179 141.039 127.326 1.00 57.73  ? 2157 LEU A O     1 
ATOM   6670  C  CB    . LEU A 1 2157 ? 143.209 139.961 129.768 1.00 43.17  ? 2157 LEU A CB    1 
ATOM   6671  C  CG    . LEU A 1 2157 ? 144.173 139.998 128.578 1.00 44.52  ? 2157 LEU A CG    1 
ATOM   6672  C  CD1   . LEU A 1 2157 ? 144.853 141.351 128.463 1.00 50.34  ? 2157 LEU A CD1   1 
ATOM   6673  C  CD2   . LEU A 1 2157 ? 145.195 138.876 128.620 1.00 49.99  ? 2157 LEU A CD2   1 
ATOM   6674  N  N     . PHE A 1 2158 ? 140.551 139.104 128.372 1.00 46.48  ? 2158 PHE A N     1 
ATOM   6675  C  CA    . PHE A 1 2158 ? 139.900 138.576 127.179 1.00 48.42  ? 2158 PHE A CA    1 
ATOM   6676  C  C     . PHE A 1 2158 ? 138.661 139.383 126.806 1.00 50.40  ? 2158 PHE A C     1 
ATOM   6677  O  O     . PHE A 1 2158 ? 138.345 139.507 125.619 1.00 52.02  ? 2158 PHE A O     1 
ATOM   6678  C  CB    . PHE A 1 2158 ? 139.567 137.100 127.373 1.00 55.77  ? 2158 PHE A CB    1 
ATOM   6679  C  CG    . PHE A 1 2158 ? 140.741 136.197 127.155 1.00 56.12  ? 2158 PHE A CG    1 
ATOM   6680  C  CD1   . PHE A 1 2158 ? 141.367 136.145 125.924 1.00 55.28  ? 2158 PHE A CD1   1 
ATOM   6681  C  CD2   . PHE A 1 2158 ? 141.231 135.420 128.184 1.00 55.35  ? 2158 PHE A CD2   1 
ATOM   6682  C  CE1   . PHE A 1 2158 ? 142.451 135.330 125.724 1.00 56.23  ? 2158 PHE A CE1   1 
ATOM   6683  C  CE2   . PHE A 1 2158 ? 142.312 134.602 127.987 1.00 54.48  ? 2158 PHE A CE2   1 
ATOM   6684  C  CZ    . PHE A 1 2158 ? 142.924 134.557 126.756 1.00 57.70  ? 2158 PHE A CZ    1 
ATOM   6685  N  N     . SER A 1 2159 ? 137.986 139.950 127.810 1.00 50.19  ? 2159 SER A N     1 
ATOM   6686  C  CA    . SER A 1 2159 ? 136.806 140.811 127.532 1.00 49.11  ? 2159 SER A CA    1 
ATOM   6687  C  C     . SER A 1 2159 ? 137.268 142.084 126.809 1.00 51.16  ? 2159 SER A C     1 
ATOM   6688  O  O     . SER A 1 2159 ? 136.694 142.403 125.746 1.00 52.83  ? 2159 SER A O     1 
ATOM   6689  C  CB    . SER A 1 2159 ? 136.053 141.138 128.796 1.00 51.03  ? 2159 SER A CB    1 
ATOM   6690  O  OG    . SER A 1 2159 ? 136.851 141.910 129.682 1.00 57.43  ? 2159 SER A OG    1 
ATOM   6691  N  N     . LEU A 1 2160 ? 138.273 142.772 127.361 1.00 49.84  ? 2160 LEU A N     1 
ATOM   6692  C  CA    . LEU A 1 2160 ? 138.812 143.997 126.715 1.00 51.24  ? 2160 LEU A CA    1 
ATOM   6693  C  C     . LEU A 1 2160 ? 139.344 143.621 125.326 1.00 49.12  ? 2160 LEU A C     1 
ATOM   6694  O  O     . LEU A 1 2160 ? 139.103 144.386 124.367 1.00 55.32  ? 2160 LEU A O     1 
ATOM   6695  C  CB    . LEU A 1 2160 ? 139.910 144.602 127.587 1.00 47.82  ? 2160 LEU A CB    1 
ATOM   6696  C  CG    . LEU A 1 2160 ? 139.591 144.728 129.079 1.00 47.66  ? 2160 LEU A CG    1 
ATOM   6697  C  CD1   . LEU A 1 2160 ? 140.710 145.438 129.820 1.00 43.44  ? 2160 LEU A CD1   1 
ATOM   6698  C  CD2   . LEU A 1 2160 ? 138.258 145.419 129.310 1.00 55.56  ? 2160 LEU A CD2   1 
ATOM   6699  N  N     . LEU A 1 2161 ? 140.037 142.483 125.229 1.00 49.60  ? 2161 LEU A N     1 
ATOM   6700  C  CA    . LEU A 1 2161 ? 140.579 142.018 123.927 1.00 50.37  ? 2161 LEU A CA    1 
ATOM   6701  C  C     . LEU A 1 2161 ? 139.431 141.922 122.912 1.00 54.03  ? 2161 LEU A C     1 
ATOM   6702  O  O     . LEU A 1 2161 ? 139.499 142.620 121.878 1.00 58.26  ? 2161 LEU A O     1 
ATOM   6703  C  CB    . LEU A 1 2161 ? 141.264 140.671 124.148 1.00 50.58  ? 2161 LEU A CB    1 
ATOM   6704  C  CG    . LEU A 1 2161 ? 142.238 140.219 123.058 1.00 49.95  ? 2161 LEU A CG    1 
ATOM   6705  C  CD1   . LEU A 1 2161 ? 143.148 141.366 122.656 1.00 49.10  ? 2161 LEU A CD1   1 
ATOM   6706  C  CD2   . LEU A 1 2161 ? 143.059 139.058 123.592 1.00 52.82  ? 2161 LEU A CD2   1 
ATOM   6707  N  N     . SER A 1 2162 ? 138.418 141.099 123.201 1.00 54.75  ? 2162 SER A N     1 
ATOM   6708  C  CA    . SER A 1 2162 ? 137.270 140.981 122.305 1.00 54.89  ? 2162 SER A CA    1 
ATOM   6709  C  C     . SER A 1 2162 ? 136.670 142.342 121.972 1.00 59.10  ? 2162 SER A C     1 
ATOM   6710  O  O     . SER A 1 2162 ? 136.178 142.544 120.856 1.00 61.44  ? 2162 SER A O     1 
ATOM   6711  C  CB    . SER A 1 2162 ? 136.206 140.076 122.923 1.00 56.29  ? 2162 SER A CB    1 
ATOM   6712  O  OG    . SER A 1 2162 ? 135.642 140.671 124.079 1.00 60.58  ? 2162 SER A OG    1 
ATOM   6713  N  N     . ASP A 1 2163 ? 136.686 143.277 122.927 1.00 59.64  ? 2163 ASP A N     1 
ATOM   6714  C  CA    . ASP A 1 2163 ? 136.153 144.613 122.670 1.00 56.92  ? 2163 ASP A CA    1 
ATOM   6715  C  C     . ASP A 1 2163 ? 136.947 145.326 121.585 1.00 52.10  ? 2163 ASP A C     1 
ATOM   6716  O  O     . ASP A 1 2163 ? 136.367 145.978 120.709 1.00 55.78  ? 2163 ASP A O     1 
ATOM   6717  C  CB    . ASP A 1 2163 ? 136.154 145.441 123.956 1.00 59.77  ? 2163 ASP A CB    1 
ATOM   6718  C  CG    . ASP A 1 2163 ? 135.135 144.954 124.968 1.00 69.43  ? 2163 ASP A CG    1 
ATOM   6719  O  OD1   . ASP A 1 2163 ? 134.414 143.979 124.668 1.00 70.51  ? 2163 ASP A OD1   1 
ATOM   6720  O  OD2   . ASP A 1 2163 ? 135.057 145.545 126.066 1.00 67.86  ? 2163 ASP A OD2   1 
ATOM   6721  N  N     . VAL A 1 2164 ? 138.273 145.217 121.626 1.00 52.05  ? 2164 VAL A N     1 
ATOM   6722  C  CA    . VAL A 1 2164 ? 139.106 145.907 120.648 1.00 46.61  ? 2164 VAL A CA    1 
ATOM   6723  C  C     . VAL A 1 2164 ? 139.254 145.075 119.382 1.00 51.92  ? 2164 VAL A C     1 
ATOM   6724  O  O     . VAL A 1 2164 ? 139.129 145.590 118.265 1.00 54.71  ? 2164 VAL A O     1 
ATOM   6725  C  CB    . VAL A 1 2164 ? 140.475 146.250 121.261 1.00 41.62  ? 2164 VAL A CB    1 
ATOM   6726  C  CG1   . VAL A 1 2164 ? 141.281 147.069 120.286 1.00 42.95  ? 2164 VAL A CG1   1 
ATOM   6727  C  CG2   . VAL A 1 2164 ? 140.298 146.999 122.569 1.00 51.95  ? 2164 VAL A CG2   1 
ATOM   6728  N  N     . PHE A 1 2165 ? 139.532 143.779 119.533 1.00 53.25  ? 2165 PHE A N     1 
ATOM   6729  C  CA    . PHE A 1 2165 ? 139.617 142.855 118.411 1.00 52.40  ? 2165 PHE A CA    1 
ATOM   6730  C  C     . PHE A 1 2165 ? 138.354 142.004 118.392 1.00 61.70  ? 2165 PHE A C     1 
ATOM   6731  O  O     . PHE A 1 2165 ? 138.299 140.975 119.081 1.00 65.89  ? 2165 PHE A O     1 
ATOM   6732  C  CB    . PHE A 1 2165 ? 140.859 141.969 118.530 1.00 52.19  ? 2165 PHE A CB    1 
ATOM   6733  C  CG    . PHE A 1 2165 ? 142.157 142.719 118.453 1.00 50.24  ? 2165 PHE A CG    1 
ATOM   6734  C  CD1   . PHE A 1 2165 ? 142.727 143.026 117.232 1.00 49.83  ? 2165 PHE A CD1   1 
ATOM   6735  C  CD2   . PHE A 1 2165 ? 142.806 143.121 119.607 1.00 49.10  ? 2165 PHE A CD2   1 
ATOM   6736  C  CE1   . PHE A 1 2165 ? 143.923 143.714 117.166 1.00 45.91  ? 2165 PHE A CE1   1 
ATOM   6737  C  CE2   . PHE A 1 2165 ? 143.997 143.810 119.545 1.00 43.80  ? 2165 PHE A CE2   1 
ATOM   6738  C  CZ    . PHE A 1 2165 ? 144.555 144.108 118.323 1.00 39.28  ? 2165 PHE A CZ    1 
ATOM   6739  N  N     . PRO A 1 2166 ? 137.321 142.374 117.632 1.00 64.54  ? 2166 PRO A N     1 
ATOM   6740  C  CA    . PRO A 1 2166 ? 136.071 141.601 117.644 1.00 62.84  ? 2166 PRO A CA    1 
ATOM   6741  C  C     . PRO A 1 2166 ? 136.144 140.436 116.668 1.00 69.03  ? 2166 PRO A C     1 
ATOM   6742  O  O     . PRO A 1 2166 ? 136.517 140.608 115.505 1.00 72.05  ? 2166 PRO A O     1 
ATOM   6743  C  CB    . PRO A 1 2166 ? 135.014 142.629 117.216 1.00 65.06  ? 2166 PRO A CB    1 
ATOM   6744  C  CG    . PRO A 1 2166 ? 135.784 143.852 116.747 1.00 64.69  ? 2166 PRO A CG    1 
ATOM   6745  C  CD    . PRO A 1 2166 ? 137.239 143.507 116.703 1.00 64.42  ? 2166 PRO A CD    1 
ATOM   6746  N  N     . GLY A 1 2167 ? 135.786 139.246 117.145 1.00 70.60  ? 2167 GLY A N     1 
ATOM   6747  C  CA    . GLY A 1 2167 ? 135.751 138.066 116.313 1.00 72.22  ? 2167 GLY A CA    1 
ATOM   6748  C  C     . GLY A 1 2167 ? 137.078 137.366 116.135 1.00 76.73  ? 2167 GLY A C     1 
ATOM   6749  O  O     . GLY A 1 2167 ? 137.127 136.331 115.459 1.00 81.82  ? 2167 GLY A O     1 
ATOM   6750  N  N     . VAL A 1 2168 ? 138.152 137.891 116.713 1.00 77.09  ? 2168 VAL A N     1 
ATOM   6751  C  CA    . VAL A 1 2168 ? 139.471 137.279 116.607 1.00 81.50  ? 2168 VAL A CA    1 
ATOM   6752  C  C     . VAL A 1 2168 ? 139.728 136.486 117.881 1.00 82.32  ? 2168 VAL A C     1 
ATOM   6753  O  O     . VAL A 1 2168 ? 139.669 137.035 118.986 1.00 85.21  ? 2168 VAL A O     1 
ATOM   6754  C  CB    . VAL A 1 2168 ? 140.560 138.336 116.381 1.00 78.04  ? 2168 VAL A CB    1 
ATOM   6755  C  CG1   . VAL A 1 2168 ? 141.925 137.686 116.363 1.00 70.66  ? 2168 VAL A CG1   1 
ATOM   6756  C  CG2   . VAL A 1 2168 ? 140.308 139.082 115.083 1.00 77.37  ? 2168 VAL A CG2   1 
ATOM   6757  N  N     . GLN A 1 2169 ? 140.013 135.197 117.728 1.00 82.94  ? 2169 GLN A N     1 
ATOM   6758  C  CA    . GLN A 1 2169 ? 140.159 134.285 118.851 1.00 87.11  ? 2169 GLN A CA    1 
ATOM   6759  C  C     . GLN A 1 2169 ? 141.607 133.833 118.975 1.00 85.12  ? 2169 GLN A C     1 
ATOM   6760  O  O     . GLN A 1 2169 ? 142.283 133.596 117.969 1.00 82.44  ? 2169 GLN A O     1 
ATOM   6761  C  CB    . GLN A 1 2169 ? 139.241 133.070 118.686 1.00 92.00  ? 2169 GLN A CB    1 
ATOM   6762  C  CG    . GLN A 1 2169 ? 139.274 132.103 119.855 1.00 101.19 ? 2169 GLN A CG    1 
ATOM   6763  C  CD    . GLN A 1 2169 ? 138.803 132.742 121.146 1.00 105.29 ? 2169 GLN A CD    1 
ATOM   6764  O  OE1   . GLN A 1 2169 ? 139.605 133.063 122.023 1.00 103.93 ? 2169 GLN A OE1   1 
ATOM   6765  N  NE2   . GLN A 1 2169 ? 137.494 132.935 121.268 1.00 102.70 ? 2169 GLN A NE2   1 
ATOM   6766  N  N     . TYR A 1 2170 ? 142.076 133.718 120.214 1.00 87.15  ? 2170 TYR A N     1 
ATOM   6767  C  CA    . TYR A 1 2170 ? 143.428 133.266 120.511 1.00 84.41  ? 2170 TYR A CA    1 
ATOM   6768  C  C     . TYR A 1 2170 ? 143.400 131.768 120.784 1.00 90.95  ? 2170 TYR A C     1 
ATOM   6769  O  O     . TYR A 1 2170 ? 142.745 131.318 121.730 1.00 95.07  ? 2170 TYR A O     1 
ATOM   6770  C  CB    . TYR A 1 2170 ? 144.000 134.017 121.713 1.00 76.42  ? 2170 TYR A CB    1 
ATOM   6771  C  CG    . TYR A 1 2170 ? 145.283 133.430 122.255 1.00 72.42  ? 2170 TYR A CG    1 
ATOM   6772  C  CD1   . TYR A 1 2170 ? 146.419 133.344 121.463 1.00 71.75  ? 2170 TYR A CD1   1 
ATOM   6773  C  CD2   . TYR A 1 2170 ? 145.358 132.962 123.560 1.00 69.62  ? 2170 TYR A CD2   1 
ATOM   6774  C  CE1   . TYR A 1 2170 ? 147.594 132.810 121.955 1.00 72.89  ? 2170 TYR A CE1   1 
ATOM   6775  C  CE2   . TYR A 1 2170 ? 146.528 132.426 124.060 1.00 70.30  ? 2170 TYR A CE2   1 
ATOM   6776  C  CZ    . TYR A 1 2170 ? 147.643 132.354 123.254 1.00 71.08  ? 2170 TYR A CZ    1 
ATOM   6777  O  OH    . TYR A 1 2170 ? 148.811 131.821 123.747 1.00 67.22  ? 2170 TYR A OH    1 
ATOM   6778  N  N     . HIS A 1 2171 ? 144.110 131.004 119.961 1.00 88.81  ? 2171 HIS A N     1 
ATOM   6779  C  CA    . HIS A 1 2171 ? 144.202 129.558 120.107 1.00 88.72  ? 2171 HIS A CA    1 
ATOM   6780  C  C     . HIS A 1 2171 ? 145.600 129.209 120.594 1.00 90.30  ? 2171 HIS A C     1 
ATOM   6781  O  O     . HIS A 1 2171 ? 146.588 129.487 119.906 1.00 96.63  ? 2171 HIS A O     1 
ATOM   6782  C  CB    . HIS A 1 2171 ? 143.894 128.853 118.787 1.00 90.51  ? 2171 HIS A CB    1 
ATOM   6783  C  CG    . HIS A 1 2171 ? 142.431 128.684 118.521 1.00 98.47  ? 2171 HIS A CG    1 
ATOM   6784  N  ND1   . HIS A 1 2171 ? 141.746 127.529 118.834 1.00 104.72 ? 2171 HIS A ND1   1 
ATOM   6785  C  CD2   . HIS A 1 2171 ? 141.520 129.525 117.975 1.00 101.11 ? 2171 HIS A CD2   1 
ATOM   6786  C  CE1   . HIS A 1 2171 ? 140.477 127.665 118.490 1.00 107.90 ? 2171 HIS A CE1   1 
ATOM   6787  N  NE2   . HIS A 1 2171 ? 140.314 128.867 117.968 1.00 106.62 ? 2171 HIS A NE2   1 
ATOM   6788  N  N     . ARG A 1 2172 ? 145.679 128.603 121.775 1.00 88.92  ? 2172 ARG A N     1 
ATOM   6789  C  CA    . ARG A 1 2172 ? 146.968 128.261 122.357 1.00 89.93  ? 2172 ARG A CA    1 
ATOM   6790  C  C     . ARG A 1 2172 ? 147.635 127.150 121.555 1.00 99.13  ? 2172 ARG A C     1 
ATOM   6791  O  O     . ARG A 1 2172 ? 146.975 126.222 121.079 1.00 102.13 ? 2172 ARG A O     1 
ATOM   6792  C  CB    . ARG A 1 2172 ? 146.791 127.832 123.813 1.00 86.46  ? 2172 ARG A CB    1 
ATOM   6793  C  CG    . ARG A 1 2172 ? 148.079 127.438 124.512 1.00 90.89  ? 2172 ARG A CG    1 
ATOM   6794  C  CD    . ARG A 1 2172 ? 148.993 128.637 124.687 1.00 97.09  ? 2172 ARG A CD    1 
ATOM   6795  N  NE    . ARG A 1 2172 ? 150.241 128.281 125.350 1.00 93.03  ? 2172 ARG A NE    1 
ATOM   6796  C  CZ    . ARG A 1 2172 ? 150.422 128.292 126.663 1.00 74.14  ? 2172 ARG A CZ    1 
ATOM   6797  N  NH1   . ARG A 1 2172 ? 149.447 128.627 127.492 1.00 69.71  ? 2172 ARG A NH1   1 
ATOM   6798  N  NH2   . ARG A 1 2172 ? 151.610 127.960 127.157 1.00 62.45  ? 2172 ARG A NH2   1 
ATOM   6799  N  N     . GLY A 1 2173 ? 148.952 127.257 121.397 1.00 97.57  ? 2173 GLY A N     1 
ATOM   6800  C  CA    . GLY A 1 2173 ? 149.713 126.269 120.658 1.00 101.09 ? 2173 GLY A CA    1 
ATOM   6801  C  C     . GLY A 1 2173 ? 149.621 124.874 121.239 1.00 100.73 ? 2173 GLY A C     1 
ATOM   6802  O  O     . GLY A 1 2173 ? 149.720 124.693 122.457 1.00 99.76  ? 2173 GLY A O     1 
ATOM   6803  N  N     . GLU A 1 2174 ? 149.428 123.878 120.379 1.00 98.30  ? 2174 GLU A N     1 
ATOM   6804  C  CA    . GLU A 1 2174 ? 149.341 122.492 120.811 1.00 96.93  ? 2174 GLU A CA    1 
ATOM   6805  C  C     . GLU A 1 2174 ? 150.737 121.890 120.904 1.00 97.91  ? 2174 GLU A C     1 
ATOM   6806  O  O     . GLU A 1 2174 ? 151.573 122.088 120.018 1.00 96.30  ? 2174 GLU A O     1 
ATOM   6807  C  CB    . GLU A 1 2174 ? 148.474 121.681 119.847 1.00 96.29  ? 2174 GLU A CB    1 
ATOM   6808  C  CG    . GLU A 1 2174 ? 148.290 120.233 120.255 1.00 100.07 ? 2174 GLU A CG    1 
ATOM   6809  C  CD    . GLU A 1 2174 ? 147.518 120.085 121.555 1.00 104.38 ? 2174 GLU A CD    1 
ATOM   6810  O  OE1   . GLU A 1 2174 ? 146.724 120.990 121.886 1.00 107.12 ? 2174 GLU A OE1   1 
ATOM   6811  O  OE2   . GLU A 1 2174 ? 147.708 119.063 122.248 1.00 99.52  ? 2174 GLU A OE2   1 
ATOM   6812  N  N     . MET A 1 2175 ? 150.984 121.154 121.986 1.00 87.51  ? 2175 MET A N     1 
ATOM   6813  C  CA    . MET A 1 2175 ? 152.317 120.680 122.349 1.00 77.88  ? 2175 MET A CA    1 
ATOM   6814  C  C     . MET A 1 2175 ? 152.275 119.204 122.727 1.00 72.72  ? 2175 MET A C     1 
ATOM   6815  O  O     . MET A 1 2175 ? 152.773 118.793 123.776 1.00 75.64  ? 2175 MET A O     1 
ATOM   6816  C  CB    . MET A 1 2175 ? 152.881 121.530 123.482 1.00 69.85  ? 2175 MET A CB    1 
ATOM   6817  C  CG    . MET A 1 2175 ? 153.143 122.968 123.072 1.00 75.45  ? 2175 MET A CG    1 
ATOM   6818  S  SD    . MET A 1 2175 ? 153.735 124.006 124.414 1.00 89.78  ? 2175 MET A SD    1 
ATOM   6819  C  CE    . MET A 1 2175 ? 155.378 123.335 124.619 1.00 72.92  ? 2175 MET A CE    1 
ATOM   6820  N  N     . THR A 1 2176 ? 151.689 118.388 121.843 1.00 71.65  ? 2176 THR A N     1 
ATOM   6821  C  CA    . THR A 1 2176 ? 151.296 117.020 122.185 1.00 69.34  ? 2176 THR A CA    1 
ATOM   6822  C  C     . THR A 1 2176 ? 152.427 116.215 122.817 1.00 70.37  ? 2176 THR A C     1 
ATOM   6823  O  O     . THR A 1 2176 ? 152.191 115.433 123.746 1.00 75.84  ? 2176 THR A O     1 
ATOM   6824  C  CB    . THR A 1 2176 ? 150.788 116.297 120.938 1.00 73.20  ? 2176 THR A CB    1 
ATOM   6825  O  OG1   . THR A 1 2176 ? 151.764 116.401 119.894 1.00 82.99  ? 2176 THR A OG1   1 
ATOM   6826  C  CG2   . THR A 1 2176 ? 149.479 116.900 120.465 1.00 72.11  ? 2176 THR A CG2   1 
ATOM   6827  N  N     . ALA A 1 2177 ? 153.655 116.369 122.320 1.00 67.31  ? 2177 ALA A N     1 
ATOM   6828  C  CA    . ALA A 1 2177 ? 154.771 115.607 122.876 1.00 69.08  ? 2177 ALA A CA    1 
ATOM   6829  C  C     . ALA A 1 2177 ? 155.006 115.967 124.339 1.00 68.25  ? 2177 ALA A C     1 
ATOM   6830  O  O     . ALA A 1 2177 ? 155.051 115.089 125.214 1.00 72.39  ? 2177 ALA A O     1 
ATOM   6831  C  CB    . ALA A 1 2177 ? 156.033 115.848 122.050 1.00 71.51  ? 2177 ALA A CB    1 
ATOM   6832  N  N     . LEU A 1 2178 ? 155.145 117.261 124.626 1.00 62.92  ? 2178 LEU A N     1 
ATOM   6833  C  CA    . LEU A 1 2178 ? 155.320 117.677 126.010 1.00 57.49  ? 2178 LEU A CA    1 
ATOM   6834  C  C     . LEU A 1 2178 ? 154.080 117.377 126.835 1.00 59.42  ? 2178 LEU A C     1 
ATOM   6835  O  O     . LEU A 1 2178 ? 154.191 117.087 128.026 1.00 64.93  ? 2178 LEU A O     1 
ATOM   6836  C  CB    . LEU A 1 2178 ? 155.664 119.163 126.087 1.00 57.18  ? 2178 LEU A CB    1 
ATOM   6837  C  CG    . LEU A 1 2178 ? 155.875 119.682 127.510 1.00 52.43  ? 2178 LEU A CG    1 
ATOM   6838  C  CD1   . LEU A 1 2178 ? 157.089 119.018 128.136 1.00 55.57  ? 2178 LEU A CD1   1 
ATOM   6839  C  CD2   . LEU A 1 2178 ? 156.018 121.186 127.528 1.00 53.67  ? 2178 LEU A CD2   1 
ATOM   6840  N  N     . ARG A 1 2179 ? 152.896 117.424 126.224 1.00 60.87  ? 2179 ARG A N     1 
ATOM   6841  C  CA    . ARG A 1 2179 ? 151.675 117.127 126.967 1.00 58.88  ? 2179 ARG A CA    1 
ATOM   6842  C  C     . ARG A 1 2179 ? 151.658 115.675 127.431 1.00 60.73  ? 2179 ARG A C     1 
ATOM   6843  O  O     . ARG A 1 2179 ? 151.313 115.383 128.581 1.00 67.25  ? 2179 ARG A O     1 
ATOM   6844  C  CB    . ARG A 1 2179 ? 150.448 117.441 126.112 1.00 59.99  ? 2179 ARG A CB    1 
ATOM   6845  C  CG    . ARG A 1 2179 ? 150.363 118.900 125.705 1.00 65.36  ? 2179 ARG A CG    1 
ATOM   6846  C  CD    . ARG A 1 2179 ? 150.104 119.811 126.885 1.00 58.65  ? 2179 ARG A CD    1 
ATOM   6847  N  NE    . ARG A 1 2179 ? 148.807 119.577 127.505 1.00 59.24  ? 2179 ARG A NE    1 
ATOM   6848  C  CZ    . ARG A 1 2179 ? 147.684 120.160 127.113 1.00 61.58  ? 2179 ARG A CZ    1 
ATOM   6849  N  NH1   . ARG A 1 2179 ? 147.664 121.006 126.096 1.00 63.25  ? 2179 ARG A NH1   1 
ATOM   6850  N  NH2   . ARG A 1 2179 ? 146.554 119.896 127.761 1.00 65.00  ? 2179 ARG A NH2   1 
ATOM   6851  N  N     . GLU A 1 2180 ? 152.043 114.745 126.553 1.00 61.57  ? 2180 GLU A N     1 
ATOM   6852  C  CA    . GLU A 1 2180 ? 152.052 113.339 126.947 1.00 64.75  ? 2180 GLU A CA    1 
ATOM   6853  C  C     . GLU A 1 2180 ? 153.174 113.051 127.939 1.00 67.35  ? 2180 GLU A C     1 
ATOM   6854  O  O     . GLU A 1 2180 ? 152.998 112.246 128.864 1.00 68.15  ? 2180 GLU A O     1 
ATOM   6855  C  CB    . GLU A 1 2180 ? 152.155 112.435 125.716 1.00 66.62  ? 2180 GLU A CB    1 
ATOM   6856  C  CG    . GLU A 1 2180 ? 153.486 112.465 124.993 1.00 72.42  ? 2180 GLU A CG    1 
ATOM   6857  C  CD    . GLU A 1 2180 ? 153.494 111.596 123.752 1.00 85.36  ? 2180 GLU A CD    1 
ATOM   6858  O  OE1   . GLU A 1 2180 ? 152.630 110.701 123.645 1.00 90.98  ? 2180 GLU A OE1   1 
ATOM   6859  O  OE2   . GLU A 1 2180 ? 154.368 111.806 122.884 1.00 86.63  ? 2180 GLU A OE2   1 
ATOM   6860  N  N     . GLU A 1 2181 ? 154.328 113.709 127.783 1.00 66.69  ? 2181 GLU A N     1 
ATOM   6861  C  CA    . GLU A 1 2181 ? 155.379 113.557 128.787 1.00 62.63  ? 2181 GLU A CA    1 
ATOM   6862  C  C     . GLU A 1 2181 ? 154.922 114.080 130.144 1.00 59.83  ? 2181 GLU A C     1 
ATOM   6863  O  O     . GLU A 1 2181 ? 155.180 113.456 131.180 1.00 63.65  ? 2181 GLU A O     1 
ATOM   6864  C  CB    . GLU A 1 2181 ? 156.653 114.270 128.336 1.00 60.55  ? 2181 GLU A CB    1 
ATOM   6865  C  CG    . GLU A 1 2181 ? 157.236 113.740 127.039 1.00 69.97  ? 2181 GLU A CG    1 
ATOM   6866  C  CD    . GLU A 1 2181 ? 157.903 112.388 127.197 1.00 79.40  ? 2181 GLU A CD    1 
ATOM   6867  O  OE1   . GLU A 1 2181 ? 158.030 111.909 128.343 1.00 83.74  ? 2181 GLU A OE1   1 
ATOM   6868  O  OE2   . GLU A 1 2181 ? 158.299 111.799 126.169 1.00 81.14  ? 2181 GLU A OE2   1 
ATOM   6869  N  N     . LEU A 1 2182 ? 154.228 115.220 130.153 1.00 57.44  ? 2182 LEU A N     1 
ATOM   6870  C  CA    . LEU A 1 2182 ? 153.695 115.774 131.390 1.00 50.76  ? 2182 LEU A CA    1 
ATOM   6871  C  C     . LEU A 1 2182 ? 152.679 114.833 132.015 1.00 52.70  ? 2182 LEU A C     1 
ATOM   6872  O  O     . LEU A 1 2182 ? 152.646 114.671 133.238 1.00 57.32  ? 2182 LEU A O     1 
ATOM   6873  C  CB    . LEU A 1 2182 ? 153.049 117.131 131.117 1.00 47.71  ? 2182 LEU A CB    1 
ATOM   6874  C  CG    . LEU A 1 2182 ? 153.937 118.359 130.944 1.00 49.89  ? 2182 LEU A CG    1 
ATOM   6875  C  CD1   . LEU A 1 2182 ? 153.075 119.562 130.628 1.00 53.94  ? 2182 LEU A CD1   1 
ATOM   6876  C  CD2   . LEU A 1 2182 ? 154.768 118.612 132.179 1.00 47.56  ? 2182 LEU A CD2   1 
ATOM   6877  N  N     . LYS A 1 2183 ? 151.824 114.225 131.193 1.00 54.21  ? 2183 LYS A N     1 
ATOM   6878  C  CA    . LYS A 1 2183 ? 150.831 113.295 131.719 1.00 52.29  ? 2183 LYS A CA    1 
ATOM   6879  C  C     . LYS A 1 2183 ? 151.498 112.078 132.347 1.00 54.24  ? 2183 LYS A C     1 
ATOM   6880  O  O     . LYS A 1 2183 ? 151.097 111.629 133.429 1.00 57.73  ? 2183 LYS A O     1 
ATOM   6881  C  CB    . LYS A 1 2183 ? 149.867 112.880 130.609 1.00 55.66  ? 2183 LYS A CB    1 
ATOM   6882  C  CG    . LYS A 1 2183 ? 149.125 111.587 130.871 1.00 65.38  ? 2183 LYS A CG    1 
ATOM   6883  C  CD    . LYS A 1 2183 ? 148.162 111.273 129.741 1.00 64.90  ? 2183 LYS A CD    1 
ATOM   6884  C  CE    . LYS A 1 2183 ? 146.816 111.937 129.967 1.00 64.47  ? 2183 LYS A CE    1 
ATOM   6885  N  NZ    . LYS A 1 2183 ? 146.124 111.396 131.169 1.00 53.11  ? 2183 LYS A NZ    1 
ATOM   6886  N  N     . LYS A 1 2184 ? 152.532 111.541 131.693 1.00 55.73  ? 2184 LYS A N     1 
ATOM   6887  C  CA    . LYS A 1 2184 ? 153.260 110.416 132.274 1.00 52.67  ? 2184 LYS A CA    1 
ATOM   6888  C  C     . LYS A 1 2184 ? 153.924 110.805 133.589 1.00 50.05  ? 2184 LYS A C     1 
ATOM   6889  O  O     . LYS A 1 2184 ? 153.882 110.043 134.563 1.00 54.38  ? 2184 LYS A O     1 
ATOM   6890  C  CB    . LYS A 1 2184 ? 154.302 109.888 131.288 1.00 60.99  ? 2184 LYS A CB    1 
ATOM   6891  C  CG    . LYS A 1 2184 ? 153.722 109.244 130.043 1.00 69.29  ? 2184 LYS A CG    1 
ATOM   6892  C  CD    . LYS A 1 2184 ? 154.816 108.604 129.205 1.00 76.67  ? 2184 LYS A CD    1 
ATOM   6893  C  CE    . LYS A 1 2184 ? 155.649 109.654 128.489 1.00 78.60  ? 2184 LYS A CE    1 
ATOM   6894  N  NZ    . LYS A 1 2184 ? 156.656 109.044 127.579 1.00 89.04  ? 2184 LYS A NZ    1 
ATOM   6895  N  N     . VAL A 1 2185 ? 154.542 111.988 133.639 1.00 49.41  ? 2185 VAL A N     1 
ATOM   6896  C  CA    . VAL A 1 2185 ? 155.201 112.427 134.868 1.00 45.07  ? 2185 VAL A CA    1 
ATOM   6897  C  C     . VAL A 1 2185 ? 154.183 112.619 135.985 1.00 48.96  ? 2185 VAL A C     1 
ATOM   6898  O  O     . VAL A 1 2185 ? 154.417 112.224 137.133 1.00 55.86  ? 2185 VAL A O     1 
ATOM   6899  C  CB    . VAL A 1 2185 ? 156.009 113.712 134.614 1.00 45.29  ? 2185 VAL A CB    1 
ATOM   6900  C  CG1   . VAL A 1 2185 ? 156.551 114.256 135.916 1.00 44.27  ? 2185 VAL A CG1   1 
ATOM   6901  C  CG2   . VAL A 1 2185 ? 157.144 113.439 133.654 1.00 53.11  ? 2185 VAL A CG2   1 
ATOM   6902  N  N     . CYS A 1 2186 ? 153.039 113.230 135.669 1.00 48.14  ? 2186 CYS A N     1 
ATOM   6903  C  CA    . CYS A 1 2186 ? 152.005 113.451 136.673 1.00 41.91  ? 2186 CYS A CA    1 
ATOM   6904  C  C     . CYS A 1 2186 ? 151.462 112.132 137.201 1.00 47.28  ? 2186 CYS A C     1 
ATOM   6905  O  O     . CYS A 1 2186 ? 151.198 111.997 138.401 1.00 49.44  ? 2186 CYS A O     1 
ATOM   6906  C  CB    . CYS A 1 2186 ? 150.879 114.301 136.088 1.00 43.24  ? 2186 CYS A CB    1 
ATOM   6907  S  SG    . CYS A 1 2186 ? 151.325 116.023 135.789 1.00 50.88  ? 2186 CYS A SG    1 
ATOM   6908  N  N     . GLN A 1 2187 ? 151.276 111.148 136.319 1.00 52.36  ? 2187 GLN A N     1 
ATOM   6909  C  CA    . GLN A 1 2187 ? 150.891 109.819 136.780 1.00 52.63  ? 2187 GLN A CA    1 
ATOM   6910  C  C     . GLN A 1 2187 ? 151.958 109.228 137.691 1.00 50.90  ? 2187 GLN A C     1 
ATOM   6911  O  O     . GLN A 1 2187 ? 151.641 108.604 138.710 1.00 54.08  ? 2187 GLN A O     1 
ATOM   6912  C  CB    . GLN A 1 2187 ? 150.634 108.901 135.585 1.00 59.30  ? 2187 GLN A CB    1 
ATOM   6913  C  CG    . GLN A 1 2187 ? 150.414 107.444 135.955 1.00 65.72  ? 2187 GLN A CG    1 
ATOM   6914  C  CD    . GLN A 1 2187 ? 148.949 107.099 136.128 1.00 77.02  ? 2187 GLN A CD    1 
ATOM   6915  O  OE1   . GLN A 1 2187 ? 148.143 107.941 136.522 1.00 81.41  ? 2187 GLN A OE1   1 
ATOM   6916  N  NE2   . GLN A 1 2187 ? 148.596 105.854 135.831 1.00 75.79  ? 2187 GLN A NE2   1 
ATOM   6917  N  N     . GLU A 1 2188 ? 153.231 109.418 137.340 1.00 52.60  ? 2188 GLU A N     1 
ATOM   6918  C  CA    . GLU A 1 2188 ? 154.315 108.901 138.168 1.00 54.73  ? 2188 GLU A CA    1 
ATOM   6919  C  C     . GLU A 1 2188 ? 154.353 109.581 139.534 1.00 53.47  ? 2188 GLU A C     1 
ATOM   6920  O  O     . GLU A 1 2188 ? 154.581 108.921 140.554 1.00 58.96  ? 2188 GLU A O     1 
ATOM   6921  C  CB    . GLU A 1 2188 ? 155.648 109.068 137.438 1.00 57.83  ? 2188 GLU A CB    1 
ATOM   6922  C  CG    . GLU A 1 2188 ? 156.872 108.975 138.328 1.00 62.31  ? 2188 GLU A CG    1 
ATOM   6923  C  CD    . GLU A 1 2188 ? 158.143 109.385 137.612 1.00 68.99  ? 2188 GLU A CD    1 
ATOM   6924  O  OE1   . GLU A 1 2188 ? 158.067 109.724 136.412 1.00 69.19  ? 2188 GLU A OE1   1 
ATOM   6925  O  OE2   . GLU A 1 2188 ? 159.217 109.371 138.247 1.00 68.00  ? 2188 GLU A OE2   1 
ATOM   6926  N  N     . MET A 1 2189 ? 154.126 110.893 139.579 1.00 45.08  ? 2189 MET A N     1 
ATOM   6927  C  CA    . MET A 1 2189 ? 154.212 111.659 140.816 1.00 40.56  ? 2189 MET A CA    1 
ATOM   6928  C  C     . MET A 1 2189 ? 152.864 111.849 141.498 1.00 43.65  ? 2189 MET A C     1 
ATOM   6929  O  O     . MET A 1 2189 ? 152.736 112.736 142.348 1.00 44.26  ? 2189 MET A O     1 
ATOM   6930  C  CB    . MET A 1 2189 ? 154.853 113.022 140.555 1.00 42.99  ? 2189 MET A CB    1 
ATOM   6931  C  CG    . MET A 1 2189 ? 156.206 112.955 139.879 1.00 54.95  ? 2189 MET A CG    1 
ATOM   6932  S  SD    . MET A 1 2189 ? 156.843 114.585 139.451 1.00 71.93  ? 2189 MET A SD    1 
ATOM   6933  C  CE    . MET A 1 2189 ? 156.749 115.420 141.031 1.00 45.90  ? 2189 MET A CE    1 
ATOM   6934  N  N     . TYR A 1 2190 ? 151.858 111.052 141.138 1.00 46.76  ? 2190 TYR A N     1 
ATOM   6935  C  CA    . TYR A 1 2190 ? 150.538 111.057 141.766 1.00 42.45  ? 2190 TYR A CA    1 
ATOM   6936  C  C     . TYR A 1 2190 ? 149.804 112.379 141.589 1.00 43.80  ? 2190 TYR A C     1 
ATOM   6937  O  O     . TYR A 1 2190 ? 148.851 112.660 142.320 1.00 44.41  ? 2190 TYR A O     1 
ATOM   6938  C  CB    . TYR A 1 2190 ? 150.630 110.710 143.256 1.00 36.96  ? 2190 TYR A CB    1 
ATOM   6939  C  CG    . TYR A 1 2190 ? 151.511 109.518 143.539 1.00 44.31  ? 2190 TYR A CG    1 
ATOM   6940  C  CD1   . TYR A 1 2190 ? 151.216 108.274 143.005 1.00 47.94  ? 2190 TYR A CD1   1 
ATOM   6941  C  CD2   . TYR A 1 2190 ? 152.645 109.641 144.326 1.00 40.98  ? 2190 TYR A CD2   1 
ATOM   6942  C  CE1   . TYR A 1 2190 ? 152.022 107.186 143.251 1.00 47.01  ? 2190 TYR A CE1   1 
ATOM   6943  C  CE2   . TYR A 1 2190 ? 153.457 108.558 144.578 1.00 43.23  ? 2190 TYR A CE2   1 
ATOM   6944  C  CZ    . TYR A 1 2190 ? 153.140 107.332 144.040 1.00 50.10  ? 2190 TYR A CZ    1 
ATOM   6945  O  OH    . TYR A 1 2190 ? 153.945 106.245 144.288 1.00 66.12  ? 2190 TYR A OH    1 
ATOM   6946  N  N     . LEU A 1 2191 ? 150.223 113.198 140.632 1.00 45.92  ? 2191 LEU A N     1 
ATOM   6947  C  CA    . LEU A 1 2191 ? 149.587 114.481 140.382 1.00 38.67  ? 2191 LEU A CA    1 
ATOM   6948  C  C     . LEU A 1 2191 ? 148.415 114.317 139.419 1.00 42.63  ? 2191 LEU A C     1 
ATOM   6949  O  O     . LEU A 1 2191 ? 148.282 113.306 138.726 1.00 44.56  ? 2191 LEU A O     1 
ATOM   6950  C  CB    . LEU A 1 2191 ? 150.596 115.482 139.820 1.00 31.35  ? 2191 LEU A CB    1 
ATOM   6951  C  CG    . LEU A 1 2191 ? 151.786 115.828 140.717 1.00 34.95  ? 2191 LEU A CG    1 
ATOM   6952  C  CD1   . LEU A 1 2191 ? 152.402 117.136 140.284 1.00 35.03  ? 2191 LEU A CD1   1 
ATOM   6953  C  CD2   . LEU A 1 2191 ? 151.371 115.898 142.174 1.00 38.30  ? 2191 LEU A CD2   1 
ATOM   6954  N  N     . THR A 1 2192 ? 147.560 115.332 139.387 1.00 39.96  ? 2192 THR A N     1 
ATOM   6955  C  CA    . THR A 1 2192 ? 146.368 115.324 138.553 1.00 38.32  ? 2192 THR A CA    1 
ATOM   6956  C  C     . THR A 1 2192 ? 146.623 116.108 137.273 1.00 40.67  ? 2192 THR A C     1 
ATOM   6957  O  O     . THR A 1 2192 ? 147.140 117.229 137.309 1.00 39.42  ? 2192 THR A O     1 
ATOM   6958  C  CB    . THR A 1 2192 ? 145.172 115.914 139.301 1.00 41.49  ? 2192 THR A CB    1 
ATOM   6959  O  OG1   . THR A 1 2192 ? 144.936 115.157 140.494 1.00 53.38  ? 2192 THR A OG1   1 
ATOM   6960  C  CG2   . THR A 1 2192 ? 143.926 115.870 138.437 1.00 37.01  ? 2192 THR A CG2   1 
ATOM   6961  N  N     . TYR A 1 2193 ? 146.256 115.510 136.145 1.00 49.35  ? 2193 TYR A N     1 
ATOM   6962  C  CA    . TYR A 1 2193 ? 146.477 116.081 134.827 1.00 46.66  ? 2193 TYR A CA    1 
ATOM   6963  C  C     . TYR A 1 2193 ? 145.139 116.322 134.143 1.00 50.95  ? 2193 TYR A C     1 
ATOM   6964  O  O     . TYR A 1 2193 ? 144.182 115.570 134.350 1.00 51.53  ? 2193 TYR A O     1 
ATOM   6965  C  CB    . TYR A 1 2193 ? 147.348 115.153 133.973 1.00 50.26  ? 2193 TYR A CB    1 
ATOM   6966  C  CG    . TYR A 1 2193 ? 147.746 115.725 132.634 1.00 55.36  ? 2193 TYR A CG    1 
ATOM   6967  C  CD1   . TYR A 1 2193 ? 146.962 115.517 131.508 1.00 59.09  ? 2193 TYR A CD1   1 
ATOM   6968  C  CD2   . TYR A 1 2193 ? 148.910 116.463 132.493 1.00 52.58  ? 2193 TYR A CD2   1 
ATOM   6969  C  CE1   . TYR A 1 2193 ? 147.322 116.036 130.285 1.00 59.43  ? 2193 TYR A CE1   1 
ATOM   6970  C  CE2   . TYR A 1 2193 ? 149.277 116.986 131.272 1.00 52.30  ? 2193 TYR A CE2   1 
ATOM   6971  C  CZ    . TYR A 1 2193 ? 148.480 116.769 130.172 1.00 58.44  ? 2193 TYR A CZ    1 
ATOM   6972  O  OH    . TYR A 1 2193 ? 148.841 117.287 128.953 1.00 65.45  ? 2193 TYR A OH    1 
ATOM   6973  N  N     . GLY A 1 2194 ? 145.077 117.374 133.334 1.00 50.36  ? 2194 GLY A N     1 
ATOM   6974  C  CA    . GLY A 1 2194 ? 143.867 117.680 132.596 1.00 57.35  ? 2194 GLY A CA    1 
ATOM   6975  C  C     . GLY A 1 2194 ? 144.164 118.561 131.407 1.00 61.64  ? 2194 GLY A C     1 
ATOM   6976  O  O     . GLY A 1 2194 ? 145.168 119.280 131.374 1.00 60.77  ? 2194 GLY A O     1 
ATOM   6977  N  N     . ASP A 1 2195 ? 143.271 118.501 130.424 1.00 64.42  ? 2195 ASP A N     1 
ATOM   6978  C  CA    . ASP A 1 2195 ? 143.396 119.269 129.195 1.00 67.69  ? 2195 ASP A CA    1 
ATOM   6979  C  C     . ASP A 1 2195 ? 142.280 120.301 129.125 1.00 67.57  ? 2195 ASP A C     1 
ATOM   6980  O  O     . ASP A 1 2195 ? 141.099 119.950 129.203 1.00 69.65  ? 2195 ASP A O     1 
ATOM   6981  C  CB    . ASP A 1 2195 ? 143.342 118.354 127.969 1.00 71.79  ? 2195 ASP A CB    1 
ATOM   6982  C  CG    . ASP A 1 2195 ? 144.564 117.464 127.850 1.00 77.89  ? 2195 ASP A CG    1 
ATOM   6983  O  OD1   . ASP A 1 2195 ? 145.648 117.873 128.313 1.00 74.78  ? 2195 ASP A OD1   1 
ATOM   6984  O  OD2   . ASP A 1 2195 ? 144.441 116.355 127.289 1.00 85.68  ? 2195 ASP A OD2   1 
ATOM   6985  N  N     . GLY A 1 2196 ? 142.656 121.568 128.974 1.00 66.76  ? 2196 GLY A N     1 
ATOM   6986  C  CA    . GLY A 1 2196 ? 141.683 122.630 128.816 1.00 67.62  ? 2196 GLY A CA    1 
ATOM   6987  C  C     . GLY A 1 2196 ? 140.825 122.870 130.040 1.00 70.33  ? 2196 GLY A C     1 
ATOM   6988  O  O     . GLY A 1 2196 ? 141.307 123.376 131.058 1.00 69.60  ? 2196 GLY A O     1 
ATOM   6989  N  N     . GLU A 1 2197 ? 139.545 122.518 129.948 1.00 76.95  ? 2197 GLU A N     1 
ATOM   6990  C  CA    . GLU A 1 2197 ? 138.595 122.719 131.034 1.00 78.47  ? 2197 GLU A CA    1 
ATOM   6991  C  C     . GLU A 1 2197 ? 138.578 121.568 132.030 1.00 76.74  ? 2197 GLU A C     1 
ATOM   6992  O  O     . GLU A 1 2197 ? 137.861 121.647 133.033 1.00 76.97  ? 2197 GLU A O     1 
ATOM   6993  C  CB    . GLU A 1 2197 ? 137.184 122.931 130.471 1.00 83.85  ? 2197 GLU A CB    1 
ATOM   6994  C  CG    . GLU A 1 2197 ? 136.463 121.651 130.055 1.00 88.00  ? 2197 GLU A CG    1 
ATOM   6995  C  CD    . GLU A 1 2197 ? 137.136 120.933 128.897 1.00 91.95  ? 2197 GLU A CD    1 
ATOM   6996  O  OE1   . GLU A 1 2197 ? 137.837 121.598 128.106 1.00 90.21  ? 2197 GLU A OE1   1 
ATOM   6997  O  OE2   . GLU A 1 2197 ? 136.962 119.702 128.780 1.00 91.81  ? 2197 GLU A OE2   1 
ATOM   6998  N  N     . GLU A 1 2198 ? 139.342 120.508 131.783 1.00 71.19  ? 2198 GLU A N     1 
ATOM   6999  C  CA    . GLU A 1 2198 ? 139.388 119.385 132.701 1.00 65.91  ? 2198 GLU A CA    1 
ATOM   7000  C  C     . GLU A 1 2198 ? 140.090 119.786 133.996 1.00 60.96  ? 2198 GLU A C     1 
ATOM   7001  O  O     . GLU A 1 2198 ? 140.759 120.820 134.080 1.00 60.09  ? 2198 GLU A O     1 
ATOM   7002  C  CB    . GLU A 1 2198 ? 140.103 118.197 132.061 1.00 67.75  ? 2198 GLU A CB    1 
ATOM   7003  C  CG    . GLU A 1 2198 ? 139.295 117.480 130.998 1.00 75.51  ? 2198 GLU A CG    1 
ATOM   7004  C  CD    . GLU A 1 2198 ? 140.059 116.333 130.370 1.00 83.19  ? 2198 GLU A CD    1 
ATOM   7005  O  OE1   . GLU A 1 2198 ? 141.307 116.371 130.383 1.00 78.21  ? 2198 GLU A OE1   1 
ATOM   7006  O  OE2   . GLU A 1 2198 ? 139.413 115.392 129.863 1.00 87.62  ? 2198 GLU A OE2   1 
ATOM   7007  N  N     . VAL A 1 2199 ? 139.924 118.951 135.020 1.00 60.03  ? 2199 VAL A N     1 
ATOM   7008  C  CA    . VAL A 1 2199 ? 140.590 119.191 136.295 1.00 55.58  ? 2199 VAL A CA    1 
ATOM   7009  C  C     . VAL A 1 2199 ? 142.096 119.093 136.085 1.00 54.76  ? 2199 VAL A C     1 
ATOM   7010  O  O     . VAL A 1 2199 ? 142.597 118.143 135.472 1.00 55.86  ? 2199 VAL A O     1 
ATOM   7011  C  CB    . VAL A 1 2199 ? 140.089 118.217 137.372 1.00 55.13  ? 2199 VAL A CB    1 
ATOM   7012  C  CG1   . VAL A 1 2199 ? 140.438 116.776 137.029 1.00 59.71  ? 2199 VAL A CG1   1 
ATOM   7013  C  CG2   . VAL A 1 2199 ? 140.658 118.593 138.730 1.00 51.02  ? 2199 VAL A CG2   1 
ATOM   7014  N  N     . GLY A 1 2200 ? 142.824 120.097 136.563 1.00 51.31  ? 2200 GLY A N     1 
ATOM   7015  C  CA    . GLY A 1 2200 ? 144.238 120.213 136.290 1.00 44.45  ? 2200 GLY A CA    1 
ATOM   7016  C  C     . GLY A 1 2200 ? 144.580 120.960 135.022 1.00 46.12  ? 2200 GLY A C     1 
ATOM   7017  O  O     . GLY A 1 2200 ? 145.768 121.132 134.731 1.00 45.25  ? 2200 GLY A O     1 
ATOM   7018  N  N     . GLY A 1 2201 ? 143.581 121.411 134.262 1.00 49.97  ? 2201 GLY A N     1 
ATOM   7019  C  CA    . GLY A 1 2201 ? 143.866 122.113 133.021 1.00 47.67  ? 2201 GLY A CA    1 
ATOM   7020  C  C     . GLY A 1 2201 ? 144.586 123.428 133.240 1.00 44.78  ? 2201 GLY A C     1 
ATOM   7021  O  O     . GLY A 1 2201 ? 145.505 123.774 132.494 1.00 48.18  ? 2201 GLY A O     1 
ATOM   7022  N  N     . MET A 1 2202 ? 144.177 124.183 134.261 1.00 43.11  ? 2202 MET A N     1 
ATOM   7023  C  CA    . MET A 1 2202 ? 144.852 125.441 134.563 1.00 36.98  ? 2202 MET A CA    1 
ATOM   7024  C  C     . MET A 1 2202 ? 146.289 125.200 135.004 1.00 36.34  ? 2202 MET A C     1 
ATOM   7025  O  O     . MET A 1 2202 ? 147.198 125.941 134.617 1.00 41.29  ? 2202 MET A O     1 
ATOM   7026  C  CB    . MET A 1 2202 ? 144.078 126.207 135.634 1.00 42.32  ? 2202 MET A CB    1 
ATOM   7027  C  CG    . MET A 1 2202 ? 142.714 126.692 135.178 1.00 52.23  ? 2202 MET A CG    1 
ATOM   7028  S  SD    . MET A 1 2202 ? 141.793 127.520 136.485 1.00 81.25  ? 2202 MET A SD    1 
ATOM   7029  C  CE    . MET A 1 2202 ? 142.732 129.035 136.650 1.00 63.24  ? 2202 MET A CE    1 
ATOM   7030  N  N     . TRP A 1 2203 ? 146.516 124.163 135.811 1.00 34.42  ? 2203 TRP A N     1 
ATOM   7031  C  CA    . TRP A 1 2203 ? 147.873 123.842 136.240 1.00 29.89  ? 2203 TRP A CA    1 
ATOM   7032  C  C     . TRP A 1 2203 ? 148.744 123.425 135.061 1.00 33.42  ? 2203 TRP A C     1 
ATOM   7033  O  O     . TRP A 1 2203 ? 149.918 123.809 134.977 1.00 36.46  ? 2203 TRP A O     1 
ATOM   7034  C  CB    . TRP A 1 2203 ? 147.831 122.745 137.300 1.00 29.46  ? 2203 TRP A CB    1 
ATOM   7035  C  CG    . TRP A 1 2203 ? 149.153 122.460 137.918 1.00 30.07  ? 2203 TRP A CG    1 
ATOM   7036  C  CD1   . TRP A 1 2203 ? 149.799 123.208 138.854 1.00 30.02  ? 2203 TRP A CD1   1 
ATOM   7037  C  CD2   . TRP A 1 2203 ? 150.001 121.343 137.641 1.00 29.86  ? 2203 TRP A CD2   1 
ATOM   7038  N  NE1   . TRP A 1 2203 ? 150.998 122.625 139.179 1.00 31.01  ? 2203 TRP A NE1   1 
ATOM   7039  C  CE2   . TRP A 1 2203 ? 151.144 121.478 138.446 1.00 26.91  ? 2203 TRP A CE2   1 
ATOM   7040  C  CE3   . TRP A 1 2203 ? 149.902 120.241 136.789 1.00 30.24  ? 2203 TRP A CE3   1 
ATOM   7041  C  CZ2   . TRP A 1 2203 ? 152.179 120.552 138.426 1.00 27.10  ? 2203 TRP A CZ2   1 
ATOM   7042  C  CZ3   . TRP A 1 2203 ? 150.930 119.328 136.768 1.00 25.01  ? 2203 TRP A CZ3   1 
ATOM   7043  C  CH2   . TRP A 1 2203 ? 152.054 119.487 137.580 1.00 29.11  ? 2203 TRP A CH2   1 
ATOM   7044  N  N     . VAL A 1 2204 ? 148.189 122.638 134.139 1.00 33.24  ? 2204 VAL A N     1 
ATOM   7045  C  CA    . VAL A 1 2204 ? 148.956 122.212 132.975 1.00 29.92  ? 2204 VAL A CA    1 
ATOM   7046  C  C     . VAL A 1 2204 ? 149.259 123.397 132.068 1.00 37.87  ? 2204 VAL A C     1 
ATOM   7047  O  O     . VAL A 1 2204 ? 150.365 123.515 131.529 1.00 49.01  ? 2204 VAL A O     1 
ATOM   7048  C  CB    . VAL A 1 2204 ? 148.215 121.091 132.228 1.00 37.71  ? 2204 VAL A CB    1 
ATOM   7049  C  CG1   . VAL A 1 2204 ? 148.905 120.781 130.915 1.00 46.58  ? 2204 VAL A CG1   1 
ATOM   7050  C  CG2   . VAL A 1 2204 ? 148.152 119.849 133.090 1.00 43.75  ? 2204 VAL A CG2   1 
ATOM   7051  N  N     . GLU A 1 2205 ? 148.295 124.301 131.883 1.00 36.03  ? 2205 GLU A N     1 
ATOM   7052  C  CA    . GLU A 1 2205 ? 148.597 125.478 131.078 1.00 35.47  ? 2205 GLU A CA    1 
ATOM   7053  C  C     . GLU A 1 2205 ? 149.634 126.358 131.763 1.00 37.58  ? 2205 GLU A C     1 
ATOM   7054  O  O     . GLU A 1 2205 ? 150.467 126.967 131.085 1.00 42.96  ? 2205 GLU A O     1 
ATOM   7055  C  CB    . GLU A 1 2205 ? 147.323 126.269 130.766 1.00 41.05  ? 2205 GLU A CB    1 
ATOM   7056  C  CG    . GLU A 1 2205 ? 146.887 127.253 131.834 1.00 50.08  ? 2205 GLU A CG    1 
ATOM   7057  C  CD    . GLU A 1 2205 ? 145.635 128.016 131.451 1.00 65.08  ? 2205 GLU A CD    1 
ATOM   7058  O  OE1   . GLU A 1 2205 ? 145.062 127.720 130.382 1.00 71.39  ? 2205 GLU A OE1   1 
ATOM   7059  O  OE2   . GLU A 1 2205 ? 145.228 128.913 132.217 1.00 67.71  ? 2205 GLU A OE2   1 
ATOM   7060  N  N     . LYS A 1 2206 ? 149.625 126.414 133.097 1.00 35.95  ? 2206 LYS A N     1 
ATOM   7061  C  CA    . LYS A 1 2206 ? 150.645 127.176 133.811 1.00 31.78  ? 2206 LYS A CA    1 
ATOM   7062  C  C     . LYS A 1 2206 ? 152.027 126.563 133.630 1.00 32.07  ? 2206 LYS A C     1 
ATOM   7063  O  O     . LYS A 1 2206 ? 153.014 127.287 133.461 1.00 39.36  ? 2206 LYS A O     1 
ATOM   7064  C  CB    . LYS A 1 2206 ? 150.290 127.272 135.292 1.00 30.38  ? 2206 LYS A CB    1 
ATOM   7065  C  CG    . LYS A 1 2206 ? 149.350 128.411 135.618 1.00 30.30  ? 2206 LYS A CG    1 
ATOM   7066  C  CD    . LYS A 1 2206 ? 150.012 129.748 135.354 1.00 26.94  ? 2206 LYS A CD    1 
ATOM   7067  C  CE    . LYS A 1 2206 ? 148.991 130.794 134.958 1.00 32.09  ? 2206 LYS A CE    1 
ATOM   7068  N  NZ    . LYS A 1 2206 ? 149.457 132.167 135.284 1.00 36.29  ? 2206 LYS A NZ    1 
ATOM   7069  N  N     . VAL A 1 2207 ? 152.126 125.233 133.671 1.00 32.17  ? 2207 VAL A N     1 
ATOM   7070  C  CA    . VAL A 1 2207 ? 153.435 124.616 133.473 1.00 33.82  ? 2207 VAL A CA    1 
ATOM   7071  C  C     . VAL A 1 2207 ? 153.895 124.779 132.024 1.00 35.87  ? 2207 VAL A C     1 
ATOM   7072  O  O     . VAL A 1 2207 ? 155.093 124.940 131.762 1.00 41.79  ? 2207 VAL A O     1 
ATOM   7073  C  CB    . VAL A 1 2207 ? 153.427 123.142 133.931 1.00 31.35  ? 2207 VAL A CB    1 
ATOM   7074  C  CG1   . VAL A 1 2207 ? 152.673 122.259 132.977 1.00 32.89  ? 2207 VAL A CG1   1 
ATOM   7075  C  CG2   . VAL A 1 2207 ? 154.838 122.637 134.081 1.00 38.96  ? 2207 VAL A CG2   1 
ATOM   7076  N  N     . LEU A 1 2208 ? 152.963 124.780 131.065 1.00 35.21  ? 2208 LEU A N     1 
ATOM   7077  C  CA    . LEU A 1 2208 ? 153.331 125.072 129.680 1.00 36.66  ? 2208 LEU A CA    1 
ATOM   7078  C  C     . LEU A 1 2208 ? 153.835 126.505 129.528 1.00 39.48  ? 2208 LEU A C     1 
ATOM   7079  O  O     . LEU A 1 2208 ? 154.807 126.757 128.802 1.00 42.86  ? 2208 LEU A O     1 
ATOM   7080  C  CB    . LEU A 1 2208 ? 152.139 124.826 128.758 1.00 36.99  ? 2208 LEU A CB    1 
ATOM   7081  C  CG    . LEU A 1 2208 ? 151.610 123.396 128.657 1.00 32.37  ? 2208 LEU A CG    1 
ATOM   7082  C  CD1   . LEU A 1 2208 ? 150.504 123.320 127.627 1.00 42.16  ? 2208 LEU A CD1   1 
ATOM   7083  C  CD2   . LEU A 1 2208 ? 152.724 122.435 128.310 1.00 39.46  ? 2208 LEU A CD2   1 
ATOM   7084  N  N     . GLN A 1 2209 ? 153.179 127.457 130.194 1.00 35.30  ? 2209 GLN A N     1 
ATOM   7085  C  CA    . GLN A 1 2209 ? 153.652 128.837 130.176 1.00 33.57  ? 2209 GLN A CA    1 
ATOM   7086  C  C     . GLN A 1 2209 ? 155.031 128.948 130.806 1.00 38.87  ? 2209 GLN A C     1 
ATOM   7087  O  O     . GLN A 1 2209 ? 155.887 129.697 130.323 1.00 47.02  ? 2209 GLN A O     1 
ATOM   7088  C  CB    . GLN A 1 2209 ? 152.661 129.742 130.905 1.00 31.00  ? 2209 GLN A CB    1 
ATOM   7089  C  CG    . GLN A 1 2209 ? 151.297 129.823 130.257 1.00 37.06  ? 2209 GLN A CG    1 
ATOM   7090  C  CD    . GLN A 1 2209 ? 150.292 130.548 131.121 1.00 40.21  ? 2209 GLN A CD    1 
ATOM   7091  O  OE1   . GLN A 1 2209 ? 150.628 131.049 132.192 1.00 38.94  ? 2209 GLN A OE1   1 
ATOM   7092  N  NE2   . GLN A 1 2209 ? 149.049 130.604 130.664 1.00 39.12  ? 2209 GLN A NE2   1 
ATOM   7093  N  N     . LEU A 1 2210 ? 155.262 128.216 131.895 1.00 38.69  ? 2210 LEU A N     1 
ATOM   7094  C  CA    . LEU A 1 2210 ? 156.577 128.228 132.524 1.00 37.08  ? 2210 LEU A CA    1 
ATOM   7095  C  C     . LEU A 1 2210 ? 157.629 127.670 131.574 1.00 37.11  ? 2210 LEU A C     1 
ATOM   7096  O  O     . LEU A 1 2210 ? 158.754 128.175 131.513 1.00 40.33  ? 2210 LEU A O     1 
ATOM   7097  C  CB    . LEU A 1 2210 ? 156.529 127.434 133.831 1.00 37.09  ? 2210 LEU A CB    1 
ATOM   7098  C  CG    . LEU A 1 2210 ? 157.681 127.516 134.837 1.00 45.65  ? 2210 LEU A CG    1 
ATOM   7099  C  CD1   . LEU A 1 2210 ? 157.143 127.225 136.225 1.00 40.96  ? 2210 LEU A CD1   1 
ATOM   7100  C  CD2   . LEU A 1 2210 ? 158.824 126.576 134.513 1.00 45.04  ? 2210 LEU A CD2   1 
ATOM   7101  N  N     . TYR A 1 2211 ? 157.273 126.633 130.811 1.00 38.47  ? 2211 TYR A N     1 
ATOM   7102  C  CA    . TYR A 1 2211 ? 158.197 126.085 129.823 1.00 38.98  ? 2211 TYR A CA    1 
ATOM   7103  C  C     . TYR A 1 2211 ? 158.523 127.104 128.739 1.00 43.42  ? 2211 TYR A C     1 
ATOM   7104  O  O     . TYR A 1 2211 ? 159.683 127.250 128.334 1.00 49.91  ? 2211 TYR A O     1 
ATOM   7105  C  CB    . TYR A 1 2211 ? 157.614 124.821 129.197 1.00 40.70  ? 2211 TYR A CB    1 
ATOM   7106  C  CG    . TYR A 1 2211 ? 158.469 124.260 128.088 1.00 50.59  ? 2211 TYR A CG    1 
ATOM   7107  C  CD1   . TYR A 1 2211 ? 159.818 124.012 128.286 1.00 53.55  ? 2211 TYR A CD1   1 
ATOM   7108  C  CD2   . TYR A 1 2211 ? 157.930 123.983 126.844 1.00 56.18  ? 2211 TYR A CD2   1 
ATOM   7109  C  CE1   . TYR A 1 2211 ? 160.604 123.500 127.276 1.00 58.26  ? 2211 TYR A CE1   1 
ATOM   7110  C  CE2   . TYR A 1 2211 ? 158.707 123.468 125.828 1.00 57.38  ? 2211 TYR A CE2   1 
ATOM   7111  C  CZ    . TYR A 1 2211 ? 160.043 123.228 126.050 1.00 61.76  ? 2211 TYR A CZ    1 
ATOM   7112  O  OH    . TYR A 1 2211 ? 160.821 122.718 125.037 1.00 67.22  ? 2211 TYR A OH    1 
ATOM   7113  N  N     . GLN A 1 2212 ? 157.506 127.808 128.238 1.00 47.18  ? 2212 GLN A N     1 
ATOM   7114  C  CA    . GLN A 1 2212 ? 157.774 128.799 127.200 1.00 44.71  ? 2212 GLN A CA    1 
ATOM   7115  C  C     . GLN A 1 2212 ? 158.612 129.953 127.742 1.00 44.02  ? 2212 GLN A C     1 
ATOM   7116  O  O     . GLN A 1 2212 ? 159.454 130.499 127.019 1.00 47.76  ? 2212 GLN A O     1 
ATOM   7117  C  CB    . GLN A 1 2212 ? 156.465 129.303 126.582 1.00 42.71  ? 2212 GLN A CB    1 
ATOM   7118  C  CG    . GLN A 1 2212 ? 155.786 130.443 127.323 1.00 50.54  ? 2212 GLN A CG    1 
ATOM   7119  C  CD    . GLN A 1 2212 ? 154.360 130.676 126.864 1.00 59.47  ? 2212 GLN A CD    1 
ATOM   7120  O  OE1   . GLN A 1 2212 ? 153.859 129.985 125.978 1.00 62.08  ? 2212 GLN A OE1   1 
ATOM   7121  N  NE2   . GLN A 1 2212 ? 153.698 131.656 127.467 1.00 53.18  ? 2212 GLN A NE2   1 
ATOM   7122  N  N     . ILE A 1 2213 ? 158.422 130.315 129.013 1.00 43.62  ? 2213 ILE A N     1 
ATOM   7123  C  CA    . ILE A 1 2213 ? 159.252 131.351 129.618 1.00 42.32  ? 2213 ILE A CA    1 
ATOM   7124  C  C     . ILE A 1 2213 ? 160.691 130.866 129.767 1.00 45.42  ? 2213 ILE A C     1 
ATOM   7125  O  O     . ILE A 1 2213 ? 161.640 131.633 129.570 1.00 47.13  ? 2213 ILE A O     1 
ATOM   7126  C  CB    . ILE A 1 2213 ? 158.656 131.800 130.965 1.00 39.88  ? 2213 ILE A CB    1 
ATOM   7127  C  CG1   . ILE A 1 2213 ? 157.290 132.452 130.756 1.00 38.58  ? 2213 ILE A CG1   1 
ATOM   7128  C  CG2   . ILE A 1 2213 ? 159.579 132.781 131.654 1.00 43.19  ? 2213 ILE A CG2   1 
ATOM   7129  C  CD1   . ILE A 1 2213 ? 157.342 133.734 129.966 1.00 47.19  ? 2213 ILE A CD1   1 
ATOM   7130  N  N     . THR A 1 2214 ? 160.880 129.589 130.119 1.00 48.12  ? 2214 THR A N     1 
ATOM   7131  C  CA    . THR A 1 2214 ? 162.231 129.033 130.154 1.00 47.42  ? 2214 THR A CA    1 
ATOM   7132  C  C     . THR A 1 2214 ? 162.876 129.093 128.778 1.00 50.67  ? 2214 THR A C     1 
ATOM   7133  O  O     . THR A 1 2214 ? 164.071 129.385 128.655 1.00 54.05  ? 2214 THR A O     1 
ATOM   7134  C  CB    . THR A 1 2214 ? 162.219 127.586 130.656 1.00 47.84  ? 2214 THR A CB    1 
ATOM   7135  O  OG1   . THR A 1 2214 ? 161.338 126.799 129.847 1.00 53.20  ? 2214 THR A OG1   1 
ATOM   7136  C  CG2   . THR A 1 2214 ? 161.780 127.507 132.104 1.00 48.57  ? 2214 THR A CG2   1 
ATOM   7137  N  N     . GLN A 1 2215 ? 162.103 128.801 127.731 1.00 51.62  ? 2215 GLN A N     1 
ATOM   7138  C  CA    . GLN A 1 2215 ? 162.630 128.911 126.373 1.00 52.37  ? 2215 GLN A CA    1 
ATOM   7139  C  C     . GLN A 1 2215 ? 163.038 130.342 126.045 1.00 57.10  ? 2215 GLN A C     1 
ATOM   7140  O  O     . GLN A 1 2215 ? 164.093 130.571 125.442 1.00 57.06  ? 2215 GLN A O     1 
ATOM   7141  C  CB    . GLN A 1 2215 ? 161.604 128.410 125.358 1.00 51.63  ? 2215 GLN A CB    1 
ATOM   7142  C  CG    . GLN A 1 2215 ? 161.527 126.904 125.224 1.00 51.24  ? 2215 GLN A CG    1 
ATOM   7143  C  CD    . GLN A 1 2215 ? 160.544 126.478 124.152 1.00 59.94  ? 2215 GLN A CD    1 
ATOM   7144  O  OE1   . GLN A 1 2215 ? 159.777 127.292 123.639 1.00 60.40  ? 2215 GLN A OE1   1 
ATOM   7145  N  NE2   . GLN A 1 2215 ? 160.577 125.201 123.792 1.00 64.90  ? 2215 GLN A NE2   1 
ATOM   7146  N  N     . ILE A 1 2216 ? 162.217 131.320 126.426 1.00 57.69  ? 2216 ILE A N     1 
ATOM   7147  C  CA    . ILE A 1 2216 ? 162.481 132.703 126.033 1.00 51.81  ? 2216 ILE A CA    1 
ATOM   7148  C  C     . ILE A 1 2216 ? 163.566 133.324 126.908 1.00 55.67  ? 2216 ILE A C     1 
ATOM   7149  O  O     . ILE A 1 2216 ? 164.605 133.770 126.409 1.00 57.66  ? 2216 ILE A O     1 
ATOM   7150  C  CB    . ILE A 1 2216 ? 161.183 133.531 126.063 1.00 48.53  ? 2216 ILE A CB    1 
ATOM   7151  C  CG1   . ILE A 1 2216 ? 160.149 132.923 125.117 1.00 51.30  ? 2216 ILE A CG1   1 
ATOM   7152  C  CG2   . ILE A 1 2216 ? 161.458 134.958 125.640 1.00 50.83  ? 2216 ILE A CG2   1 
ATOM   7153  C  CD1   . ILE A 1 2216 ? 160.593 132.890 123.672 1.00 53.14  ? 2216 ILE A CD1   1 
ATOM   7154  N  N     . ASN A 1 2217 ? 163.345 133.366 128.219 1.00 55.30  ? 2217 ASN A N     1 
ATOM   7155  C  CA    . ASN A 1 2217 ? 164.263 134.014 129.146 1.00 52.78  ? 2217 ASN A CA    1 
ATOM   7156  C  C     . ASN A 1 2217 ? 165.158 133.004 129.855 1.00 55.16  ? 2217 ASN A C     1 
ATOM   7157  O  O     . ASN A 1 2217 ? 164.886 131.802 129.884 1.00 58.63  ? 2217 ASN A O     1 
ATOM   7158  C  CB    . ASN A 1 2217 ? 163.498 134.834 130.189 1.00 51.98  ? 2217 ASN A CB    1 
ATOM   7159  C  CG    . ASN A 1 2217 ? 162.645 135.915 129.570 1.00 59.83  ? 2217 ASN A CG    1 
ATOM   7160  O  OD1   . ASN A 1 2217 ? 162.542 136.016 128.351 1.00 63.65  ? 2217 ASN A OD1   1 
ATOM   7161  N  ND2   . ASN A 1 2217 ? 162.035 136.739 130.409 1.00 56.40  ? 2217 ASN A ND2   1 
ATOM   7162  N  N     . HIS A 1 2218 ? 166.246 133.520 130.429 1.00 60.60  ? 2218 HIS A N     1 
ATOM   7163  C  CA    . HIS A 1 2218 ? 167.133 132.736 131.277 1.00 58.43  ? 2218 HIS A CA    1 
ATOM   7164  C  C     . HIS A 1 2218 ? 166.885 132.954 132.763 1.00 60.13  ? 2218 HIS A C     1 
ATOM   7165  O  O     . HIS A 1 2218 ? 167.334 132.139 133.576 1.00 63.21  ? 2218 HIS A O     1 
ATOM   7166  C  CB    . HIS A 1 2218 ? 168.598 133.054 130.952 1.00 58.69  ? 2218 HIS A CB    1 
ATOM   7167  C  CG    . HIS A 1 2218 ? 168.986 134.473 131.229 1.00 67.71  ? 2218 HIS A CG    1 
ATOM   7168  N  ND1   . HIS A 1 2218 ? 169.159 135.404 130.228 1.00 75.72  ? 2218 HIS A ND1   1 
ATOM   7169  C  CD2   . HIS A 1 2218 ? 169.249 135.117 132.391 1.00 67.78  ? 2218 HIS A CD2   1 
ATOM   7170  C  CE1   . HIS A 1 2218 ? 169.500 136.563 130.762 1.00 79.85  ? 2218 HIS A CE1   1 
ATOM   7171  N  NE2   . HIS A 1 2218 ? 169.562 136.415 132.073 1.00 75.38  ? 2218 HIS A NE2   1 
ATOM   7172  N  N     . GLY A 1 2219 ? 166.199 134.022 133.130 1.00 57.54  ? 2219 GLY A N     1 
ATOM   7173  C  CA    . GLY A 1 2219 ? 165.778 134.227 134.506 1.00 48.55  ? 2219 GLY A CA    1 
ATOM   7174  C  C     . GLY A 1 2219 ? 164.290 134.486 134.556 1.00 55.25  ? 2219 GLY A C     1 
ATOM   7175  O  O     . GLY A 1 2219 ? 163.749 135.209 133.722 1.00 67.62  ? 2219 GLY A O     1 
ATOM   7176  N  N     . LEU A 1 2220 ? 163.629 133.888 135.545 1.00 50.53  ? 2220 LEU A N     1 
ATOM   7177  C  CA    . LEU A 1 2220 ? 162.173 133.922 135.582 1.00 47.60  ? 2220 LEU A CA    1 
ATOM   7178  C  C     . LEU A 1 2220 ? 161.686 133.719 137.009 1.00 44.80  ? 2220 LEU A C     1 
ATOM   7179  O  O     . LEU A 1 2220 ? 162.428 133.275 137.887 1.00 50.83  ? 2220 LEU A O     1 
ATOM   7180  C  CB    . LEU A 1 2220 ? 161.589 132.878 134.627 1.00 49.10  ? 2220 LEU A CB    1 
ATOM   7181  C  CG    . LEU A 1 2220 ? 161.937 131.409 134.858 1.00 53.09  ? 2220 LEU A CG    1 
ATOM   7182  C  CD1   . LEU A 1 2220 ? 160.952 130.723 135.792 1.00 49.90  ? 2220 LEU A CD1   1 
ATOM   7183  C  CD2   . LEU A 1 2220 ? 162.027 130.690 133.533 1.00 55.20  ? 2220 LEU A CD2   1 
ATOM   7184  N  N     . MET A 1 2221 ? 160.413 134.056 137.223 1.00 44.09  ? 2221 MET A N     1 
ATOM   7185  C  CA    . MET A 1 2221 ? 159.789 134.048 138.536 1.00 38.62  ? 2221 MET A CA    1 
ATOM   7186  C  C     . MET A 1 2221 ? 158.446 133.331 138.490 1.00 37.66  ? 2221 MET A C     1 
ATOM   7187  O  O     . MET A 1 2221 ? 157.701 133.425 137.506 1.00 39.93  ? 2221 MET A O     1 
ATOM   7188  C  CB    . MET A 1 2221 ? 159.571 135.474 139.063 1.00 35.09  ? 2221 MET A CB    1 
ATOM   7189  C  CG    . MET A 1 2221 ? 160.708 136.437 138.787 1.00 43.51  ? 2221 MET A CG    1 
ATOM   7190  S  SD    . MET A 1 2221 ? 160.554 137.968 139.728 1.00 72.67  ? 2221 MET A SD    1 
ATOM   7191  C  CE    . MET A 1 2221 ? 160.769 137.371 141.400 1.00 50.49  ? 2221 MET A CE    1 
ATOM   7192  N  N     . MET A 1 2222 ? 158.158 132.603 139.570 1.00 31.81  ? 2222 MET A N     1 
ATOM   7193  C  CA    . MET A 1 2222 ? 156.828 132.088 139.880 1.00 27.09  ? 2222 MET A CA    1 
ATOM   7194  C  C     . MET A 1 2222 ? 156.351 132.851 141.108 1.00 33.28  ? 2222 MET A C     1 
ATOM   7195  O  O     . MET A 1 2222 ? 156.913 132.687 142.195 1.00 40.05  ? 2222 MET A O     1 
ATOM   7196  C  CB    . MET A 1 2222 ? 156.851 130.589 140.164 1.00 28.57  ? 2222 MET A CB    1 
ATOM   7197  C  CG    . MET A 1 2222 ? 156.980 129.696 138.952 1.00 34.13  ? 2222 MET A CG    1 
ATOM   7198  S  SD    . MET A 1 2222 ? 158.641 129.727 138.280 1.00 63.55  ? 2222 MET A SD    1 
ATOM   7199  C  CE    . MET A 1 2222 ? 159.482 128.750 139.517 1.00 35.50  ? 2222 MET A CE    1 
ATOM   7200  N  N     . VAL A 1 2223 ? 155.324 133.682 140.948 1.00 28.90  ? 2223 VAL A N     1 
ATOM   7201  C  CA    . VAL A 1 2223 ? 154.937 134.582 142.029 1.00 31.50  ? 2223 VAL A CA    1 
ATOM   7202  C  C     . VAL A 1 2223 ? 153.512 134.274 142.471 1.00 32.98  ? 2223 VAL A C     1 
ATOM   7203  O  O     . VAL A 1 2223 ? 152.751 135.169 142.850 1.00 45.52  ? 2223 VAL A O     1 
ATOM   7204  C  CB    . VAL A 1 2223 ? 155.097 136.054 141.605 1.00 39.48  ? 2223 VAL A CB    1 
ATOM   7205  C  CG1   . VAL A 1 2223 ? 155.019 136.979 142.811 1.00 45.10  ? 2223 VAL A CG1   1 
ATOM   7206  C  CG2   . VAL A 1 2223 ? 156.410 136.248 140.886 1.00 42.42  ? 2223 VAL A CG2   1 
ATOM   7207  N  N     . GLY A 1 2224 ? 153.131 133.007 142.423 1.00 27.94  ? 2224 GLY A N     1 
ATOM   7208  C  CA    . GLY A 1 2224 ? 151.845 132.614 142.937 1.00 31.63  ? 2224 GLY A CA    1 
ATOM   7209  C  C     . GLY A 1 2224 ? 151.816 132.627 144.451 1.00 35.25  ? 2224 GLY A C     1 
ATOM   7210  O  O     . GLY A 1 2224 ? 152.858 132.588 145.109 1.00 39.67  ? 2224 GLY A O     1 
ATOM   7211  N  N     . PRO A 1 2225 ? 150.617 132.687 145.037 1.00 34.52  ? 2225 PRO A N     1 
ATOM   7212  C  CA    . PRO A 1 2225 ? 150.507 132.558 146.497 1.00 37.80  ? 2225 PRO A CA    1 
ATOM   7213  C  C     . PRO A 1 2225 ? 150.939 131.187 146.988 1.00 40.38  ? 2225 PRO A C     1 
ATOM   7214  O  O     . PRO A 1 2225 ? 151.241 130.299 146.186 1.00 43.47  ? 2225 PRO A O     1 
ATOM   7215  C  CB    . PRO A 1 2225 ? 149.017 132.803 146.761 1.00 31.87  ? 2225 PRO A CB    1 
ATOM   7216  C  CG    . PRO A 1 2225 ? 148.549 133.587 145.592 1.00 36.69  ? 2225 PRO A CG    1 
ATOM   7217  C  CD    . PRO A 1 2225 ? 149.343 133.095 144.424 1.00 35.07  ? 2225 PRO A CD    1 
ATOM   7218  N  N     . SER A 1 2226 ? 150.973 131.004 148.305 1.00 38.63  ? 2226 SER A N     1 
ATOM   7219  C  CA    . SER A 1 2226 ? 151.410 129.735 148.867 1.00 34.59  ? 2226 SER A CA    1 
ATOM   7220  C  C     . SER A 1 2226 ? 150.427 128.626 148.521 1.00 32.82  ? 2226 SER A C     1 
ATOM   7221  O  O     . SER A 1 2226 ? 149.210 128.820 148.543 1.00 40.06  ? 2226 SER A O     1 
ATOM   7222  C  CB    . SER A 1 2226 ? 151.559 129.848 150.382 1.00 35.72  ? 2226 SER A CB    1 
ATOM   7223  O  OG    . SER A 1 2226 ? 151.947 128.608 150.943 1.00 37.49  ? 2226 SER A OG    1 
ATOM   7224  N  N     . GLY A 1 2227 ? 150.966 127.453 148.203 1.00 34.57  ? 2227 GLY A N     1 
ATOM   7225  C  CA    . GLY A 1 2227 ? 150.147 126.307 147.871 1.00 32.52  ? 2227 GLY A CA    1 
ATOM   7226  C  C     . GLY A 1 2227 ? 149.353 126.453 146.591 1.00 30.29  ? 2227 GLY A C     1 
ATOM   7227  O  O     . GLY A 1 2227 ? 148.162 126.132 146.553 1.00 35.79  ? 2227 GLY A O     1 
ATOM   7228  N  N     . SER A 1 2228 ? 149.999 126.942 145.535 1.00 30.80  ? 2228 SER A N     1 
ATOM   7229  C  CA    . SER A 1 2228 ? 149.356 127.117 144.241 1.00 28.05  ? 2228 SER A CA    1 
ATOM   7230  C  C     . SER A 1 2228 ? 149.978 126.253 143.152 1.00 30.57  ? 2228 SER A C     1 
ATOM   7231  O  O     . SER A 1 2228 ? 149.645 126.423 141.975 1.00 33.63  ? 2228 SER A O     1 
ATOM   7232  C  CB    . SER A 1 2228 ? 149.396 128.586 143.831 1.00 28.03  ? 2228 SER A CB    1 
ATOM   7233  O  OG    . SER A 1 2228 ? 150.730 129.042 143.714 1.00 28.50  ? 2228 SER A OG    1 
ATOM   7234  N  N     . GLY A 1 2229 ? 150.869 125.335 143.510 1.00 32.09  ? 2229 GLY A N     1 
ATOM   7235  C  CA    . GLY A 1 2229 ? 151.418 124.398 142.552 1.00 28.61  ? 2229 GLY A CA    1 
ATOM   7236  C  C     . GLY A 1 2229 ? 152.682 124.830 141.848 1.00 30.91  ? 2229 GLY A C     1 
ATOM   7237  O  O     . GLY A 1 2229 ? 153.024 124.239 140.821 1.00 35.19  ? 2229 GLY A O     1 
ATOM   7238  N  N     . LYS A 1 2230 ? 153.388 125.838 142.362 1.00 28.07  ? 2230 LYS A N     1 
ATOM   7239  C  CA    . LYS A 1 2230 ? 154.600 126.320 141.705 1.00 24.98  ? 2230 LYS A CA    1 
ATOM   7240  C  C     . LYS A 1 2230 ? 155.688 125.253 141.689 1.00 29.13  ? 2230 LYS A C     1 
ATOM   7241  O  O     . LYS A 1 2230 ? 156.243 124.925 140.629 1.00 36.07  ? 2230 LYS A O     1 
ATOM   7242  C  CB    . LYS A 1 2230 ? 155.103 127.570 142.422 1.00 23.23  ? 2230 LYS A CB    1 
ATOM   7243  C  CG    . LYS A 1 2230 ? 154.155 128.742 142.360 1.00 27.75  ? 2230 LYS A CG    1 
ATOM   7244  C  CD    . LYS A 1 2230 ? 154.699 129.913 143.142 1.00 26.73  ? 2230 LYS A CD    1 
ATOM   7245  C  CE    . LYS A 1 2230 ? 154.565 129.659 144.629 1.00 27.04  ? 2230 LYS A CE    1 
ATOM   7246  N  NZ    . LYS A 1 2230 ? 154.964 130.834 145.437 1.00 37.84  ? 2230 LYS A NZ    1 
ATOM   7247  N  N     . SER A 1 2231 ? 156.002 124.698 142.862 1.00 28.99  ? 2231 SER A N     1 
ATOM   7248  C  CA    . SER A 1 2231 ? 157.088 123.732 142.967 1.00 28.78  ? 2231 SER A CA    1 
ATOM   7249  C  C     . SER A 1 2231 ? 156.783 122.482 142.161 1.00 31.90  ? 2231 SER A C     1 
ATOM   7250  O  O     . SER A 1 2231 ? 157.640 121.976 141.429 1.00 37.82  ? 2231 SER A O     1 
ATOM   7251  C  CB    . SER A 1 2231 ? 157.338 123.379 144.432 1.00 32.97  ? 2231 SER A CB    1 
ATOM   7252  O  OG    . SER A 1 2231 ? 157.601 124.539 145.200 1.00 38.52  ? 2231 SER A OG    1 
ATOM   7253  N  N     . MET A 1 2232 ? 155.558 121.971 142.280 1.00 31.81  ? 2232 MET A N     1 
ATOM   7254  C  CA    . MET A 1 2232 ? 155.178 120.806 141.494 1.00 32.31  ? 2232 MET A CA    1 
ATOM   7255  C  C     . MET A 1 2232 ? 155.219 121.118 140.008 1.00 35.63  ? 2232 MET A C     1 
ATOM   7256  O  O     . MET A 1 2232 ? 155.636 120.278 139.206 1.00 41.55  ? 2232 MET A O     1 
ATOM   7257  C  CB    . MET A 1 2232 ? 153.794 120.312 141.909 1.00 30.44  ? 2232 MET A CB    1 
ATOM   7258  C  CG    . MET A 1 2232 ? 153.722 119.737 143.318 1.00 36.09  ? 2232 MET A CG    1 
ATOM   7259  S  SD    . MET A 1 2232 ? 154.185 117.998 143.470 1.00 61.71  ? 2232 MET A SD    1 
ATOM   7260  C  CE    . MET A 1 2232 ? 155.972 118.082 143.551 1.00 44.09  ? 2232 MET A CE    1 
ATOM   7261  N  N     . ALA A 1 2233 ? 154.815 122.331 139.623 1.00 34.67  ? 2233 ALA A N     1 
ATOM   7262  C  CA    . ALA A 1 2233 ? 154.861 122.706 138.214 1.00 31.57  ? 2233 ALA A CA    1 
ATOM   7263  C  C     . ALA A 1 2233 ? 156.277 122.620 137.669 1.00 30.64  ? 2233 ALA A C     1 
ATOM   7264  O  O     . ALA A 1 2233 ? 156.523 121.948 136.661 1.00 34.67  ? 2233 ALA A O     1 
ATOM   7265  C  CB    . ALA A 1 2233 ? 154.301 124.113 138.016 1.00 29.90  ? 2233 ALA A CB    1 
ATOM   7266  N  N     . TRP A 1 2234 ? 157.235 123.271 138.334 1.00 30.16  ? 2234 TRP A N     1 
ATOM   7267  C  CA    . TRP A 1 2234 ? 158.572 123.285 137.750 1.00 32.76  ? 2234 TRP A CA    1 
ATOM   7268  C  C     . TRP A 1 2234 ? 159.271 121.936 137.891 1.00 36.72  ? 2234 TRP A C     1 
ATOM   7269  O  O     . TRP A 1 2234 ? 160.037 121.552 137.002 1.00 42.02  ? 2234 TRP A O     1 
ATOM   7270  C  CB    . TRP A 1 2234 ? 159.416 124.431 138.323 1.00 31.67  ? 2234 TRP A CB    1 
ATOM   7271  C  CG    . TRP A 1 2234 ? 159.901 124.293 139.727 1.00 32.98  ? 2234 TRP A CG    1 
ATOM   7272  C  CD1   . TRP A 1 2234 ? 159.399 124.917 140.825 1.00 33.79  ? 2234 TRP A CD1   1 
ATOM   7273  C  CD2   . TRP A 1 2234 ? 161.021 123.524 140.180 1.00 37.45  ? 2234 TRP A CD2   1 
ATOM   7274  N  NE1   . TRP A 1 2234 ? 160.116 124.568 141.940 1.00 34.59  ? 2234 TRP A NE1   1 
ATOM   7275  C  CE2   . TRP A 1 2234 ? 161.119 123.713 141.571 1.00 39.20  ? 2234 TRP A CE2   1 
ATOM   7276  C  CE3   . TRP A 1 2234 ? 161.943 122.686 139.548 1.00 39.55  ? 2234 TRP A CE3   1 
ATOM   7277  C  CZ2   . TRP A 1 2234 ? 162.099 123.094 142.339 1.00 41.19  ? 2234 TRP A CZ2   1 
ATOM   7278  C  CZ3   . TRP A 1 2234 ? 162.909 122.073 140.310 1.00 39.36  ? 2234 TRP A CZ3   1 
ATOM   7279  C  CH2   . TRP A 1 2234 ? 162.983 122.280 141.691 1.00 41.33  ? 2234 TRP A CH2   1 
ATOM   7280  N  N     . ARG A 1 2235 ? 158.996 121.177 138.959 1.00 36.48  ? 2235 ARG A N     1 
ATOM   7281  C  CA    . ARG A 1 2235 ? 159.567 119.836 139.064 1.00 35.95  ? 2235 ARG A CA    1 
ATOM   7282  C  C     . ARG A 1 2235 ? 159.036 118.914 137.971 1.00 40.56  ? 2235 ARG A C     1 
ATOM   7283  O  O     . ARG A 1 2235 ? 159.804 118.172 137.342 1.00 46.63  ? 2235 ARG A O     1 
ATOM   7284  C  CB    . ARG A 1 2235 ? 159.275 119.243 140.441 1.00 37.30  ? 2235 ARG A CB    1 
ATOM   7285  C  CG    . ARG A 1 2235 ? 159.971 119.937 141.594 1.00 37.54  ? 2235 ARG A CG    1 
ATOM   7286  C  CD    . ARG A 1 2235 ? 159.424 119.442 142.922 1.00 42.29  ? 2235 ARG A CD    1 
ATOM   7287  N  NE    . ARG A 1 2235 ? 159.850 120.270 144.044 1.00 45.06  ? 2235 ARG A NE    1 
ATOM   7288  C  CZ    . ARG A 1 2235 ? 161.075 120.282 144.550 1.00 49.59  ? 2235 ARG A CZ    1 
ATOM   7289  N  NH1   . ARG A 1 2235 ? 162.029 119.498 144.074 1.00 43.72  ? 2235 ARG A NH1   1 
ATOM   7290  N  NH2   . ARG A 1 2235 ? 161.350 121.097 145.564 1.00 53.43  ? 2235 ARG A NH2   1 
ATOM   7291  N  N     . VAL A 1 2236 ? 157.722 118.940 137.735 1.00 37.41  ? 2236 VAL A N     1 
ATOM   7292  C  CA    . VAL A 1 2236 ? 157.129 118.095 136.706 1.00 36.37  ? 2236 VAL A CA    1 
ATOM   7293  C  C     . VAL A 1 2236 ? 157.629 118.507 135.332 1.00 42.18  ? 2236 VAL A C     1 
ATOM   7294  O  O     . VAL A 1 2236 ? 157.889 117.658 134.474 1.00 46.82  ? 2236 VAL A O     1 
ATOM   7295  C  CB    . VAL A 1 2236 ? 155.593 118.144 136.797 1.00 32.70  ? 2236 VAL A CB    1 
ATOM   7296  C  CG1   . VAL A 1 2236 ? 154.963 117.555 135.556 1.00 35.89  ? 2236 VAL A CG1   1 
ATOM   7297  C  CG2   . VAL A 1 2236 ? 155.125 117.390 138.017 1.00 41.62  ? 2236 VAL A CG2   1 
ATOM   7298  N  N     . LEU A 1 2237 ? 157.779 119.813 135.098 1.00 42.61  ? 2237 LEU A N     1 
ATOM   7299  C  CA    . LEU A 1 2237 ? 158.335 120.260 133.826 1.00 40.08  ? 2237 LEU A CA    1 
ATOM   7300  C  C     . LEU A 1 2237 ? 159.768 119.781 133.653 1.00 44.41  ? 2237 LEU A C     1 
ATOM   7301  O  O     . LEU A 1 2237 ? 160.158 119.360 132.560 1.00 54.36  ? 2237 LEU A O     1 
ATOM   7302  C  CB    . LEU A 1 2237 ? 158.274 121.779 133.719 1.00 36.55  ? 2237 LEU A CB    1 
ATOM   7303  C  CG    . LEU A 1 2237 ? 158.838 122.278 132.392 1.00 37.05  ? 2237 LEU A CG    1 
ATOM   7304  C  CD1   . LEU A 1 2237 ? 157.936 121.859 131.246 1.00 40.97  ? 2237 LEU A CD1   1 
ATOM   7305  C  CD2   . LEU A 1 2237 ? 159.027 123.769 132.419 1.00 37.72  ? 2237 LEU A CD2   1 
ATOM   7306  N  N     . LEU A 1 2238 ? 160.570 119.846 134.717 1.00 38.86  ? 2238 LEU A N     1 
ATOM   7307  C  CA    . LEU A 1 2238 ? 161.950 119.384 134.633 1.00 42.46  ? 2238 LEU A CA    1 
ATOM   7308  C  C     . LEU A 1 2238 ? 162.009 117.902 134.284 1.00 46.74  ? 2238 LEU A C     1 
ATOM   7309  O  O     . LEU A 1 2238 ? 162.773 117.489 133.404 1.00 50.40  ? 2238 LEU A O     1 
ATOM   7310  C  CB    . LEU A 1 2238 ? 162.666 119.662 135.955 1.00 41.10  ? 2238 LEU A CB    1 
ATOM   7311  C  CG    . LEU A 1 2238 ? 164.182 119.489 136.017 1.00 47.85  ? 2238 LEU A CG    1 
ATOM   7312  C  CD1   . LEU A 1 2238 ? 164.873 120.461 135.083 1.00 54.53  ? 2238 LEU A CD1   1 
ATOM   7313  C  CD2   . LEU A 1 2238 ? 164.664 119.683 137.441 1.00 47.92  ? 2238 LEU A CD2   1 
ATOM   7314  N  N     . LYS A 1 2239 ? 161.183 117.088 134.945 1.00 47.42  ? 2239 LYS A N     1 
ATOM   7315  C  CA    . LYS A 1 2239 ? 161.184 115.655 134.657 1.00 48.64  ? 2239 LYS A CA    1 
ATOM   7316  C  C     . LYS A 1 2239 ? 160.650 115.359 133.258 1.00 54.32  ? 2239 LYS A C     1 
ATOM   7317  O  O     . LYS A 1 2239 ? 161.162 114.469 132.566 1.00 61.89  ? 2239 LYS A O     1 
ATOM   7318  C  CB    . LYS A 1 2239 ? 160.377 114.906 135.715 1.00 48.10  ? 2239 LYS A CB    1 
ATOM   7319  C  CG    . LYS A 1 2239 ? 160.910 115.089 137.123 1.00 53.82  ? 2239 LYS A CG    1 
ATOM   7320  C  CD    . LYS A 1 2239 ? 160.103 114.297 138.132 1.00 59.47  ? 2239 LYS A CD    1 
ATOM   7321  C  CE    . LYS A 1 2239 ? 160.068 112.822 137.774 1.00 69.13  ? 2239 LYS A CE    1 
ATOM   7322  N  NZ    . LYS A 1 2239 ? 159.358 112.025 138.809 1.00 66.79  ? 2239 LYS A NZ    1 
ATOM   7323  N  N     . ALA A 1 2240 ? 159.617 116.086 132.824 1.00 51.17  ? 2240 ALA A N     1 
ATOM   7324  C  CA    . ALA A 1 2240 ? 159.075 115.875 131.487 1.00 52.74  ? 2240 ALA A CA    1 
ATOM   7325  C  C     . ALA A 1 2240 ? 160.092 116.240 130.417 1.00 56.79  ? 2240 ALA A C     1 
ATOM   7326  O  O     . ALA A 1 2240 ? 160.229 115.531 129.417 1.00 64.69  ? 2240 ALA A O     1 
ATOM   7327  C  CB    . ALA A 1 2240 ? 157.791 116.683 131.307 1.00 51.66  ? 2240 ALA A CB    1 
ATOM   7328  N  N     . LEU A 1 2241 ? 160.813 117.346 130.608 1.00 54.61  ? 2241 LEU A N     1 
ATOM   7329  C  CA    . LEU A 1 2241 ? 161.879 117.710 129.683 1.00 56.75  ? 2241 LEU A CA    1 
ATOM   7330  C  C     . LEU A 1 2241 ? 162.990 116.670 129.700 1.00 63.69  ? 2241 LEU A C     1 
ATOM   7331  O  O     . LEU A 1 2241 ? 163.563 116.342 128.654 1.00 64.90  ? 2241 LEU A O     1 
ATOM   7332  C  CB    . LEU A 1 2241 ? 162.426 119.090 130.040 1.00 50.72  ? 2241 LEU A CB    1 
ATOM   7333  C  CG    . LEU A 1 2241 ? 161.517 120.277 129.725 1.00 51.02  ? 2241 LEU A CG    1 
ATOM   7334  C  CD1   . LEU A 1 2241 ? 162.280 121.582 129.855 1.00 52.13  ? 2241 LEU A CD1   1 
ATOM   7335  C  CD2   . LEU A 1 2241 ? 160.915 120.136 128.339 1.00 53.17  ? 2241 LEU A CD2   1 
ATOM   7336  N  N     . GLU A 1 2242 ? 163.307 116.144 130.884 1.00 65.11  ? 2242 GLU A N     1 
ATOM   7337  C  CA    . GLU A 1 2242 ? 164.294 115.077 131.005 1.00 62.85  ? 2242 GLU A CA    1 
ATOM   7338  C  C     . GLU A 1 2242 ? 163.909 113.874 130.155 1.00 67.76  ? 2242 GLU A C     1 
ATOM   7339  O  O     . GLU A 1 2242 ? 164.741 113.319 129.428 1.00 74.73  ? 2242 GLU A O     1 
ATOM   7340  C  CB    . GLU A 1 2242 ? 164.420 114.677 132.474 1.00 63.72  ? 2242 GLU A CB    1 
ATOM   7341  C  CG    . GLU A 1 2242 ? 165.492 113.661 132.786 1.00 74.61  ? 2242 GLU A CG    1 
ATOM   7342  C  CD    . GLU A 1 2242 ? 165.871 113.679 134.253 1.00 86.34  ? 2242 GLU A CD    1 
ATOM   7343  O  OE1   . GLU A 1 2242 ? 165.023 114.070 135.081 1.00 77.56  ? 2242 GLU A OE1   1 
ATOM   7344  O  OE2   . GLU A 1 2242 ? 167.010 113.296 134.582 1.00 93.33  ? 2242 GLU A OE2   1 
ATOM   7345  N  N     . ARG A 1 2243 ? 162.646 113.455 130.236 1.00 66.58  ? 2243 ARG A N     1 
ATOM   7346  C  CA    . ARG A 1 2243 ? 162.211 112.283 129.480 1.00 65.22  ? 2243 ARG A CA    1 
ATOM   7347  C  C     . ARG A 1 2243 ? 162.037 112.585 127.996 1.00 68.64  ? 2243 ARG A C     1 
ATOM   7348  O  O     . ARG A 1 2243 ? 162.210 111.691 127.161 1.00 73.67  ? 2243 ARG A O     1 
ATOM   7349  C  CB    . ARG A 1 2243 ? 160.909 111.730 130.058 1.00 66.64  ? 2243 ARG A CB    1 
ATOM   7350  C  CG    . ARG A 1 2243 ? 160.973 111.402 131.536 1.00 72.82  ? 2243 ARG A CG    1 
ATOM   7351  C  CD    . ARG A 1 2243 ? 159.583 111.338 132.137 1.00 73.01  ? 2243 ARG A CD    1 
ATOM   7352  N  NE    . ARG A 1 2243 ? 159.099 109.971 132.280 1.00 82.15  ? 2243 ARG A NE    1 
ATOM   7353  C  CZ    . ARG A 1 2243 ? 159.094 109.295 133.421 1.00 85.75  ? 2243 ARG A CZ    1 
ATOM   7354  N  NH1   . ARG A 1 2243 ? 159.548 109.830 134.542 1.00 79.89  ? 2243 ARG A NH1   1 
ATOM   7355  N  NH2   . ARG A 1 2243 ? 158.620 108.053 133.437 1.00 87.47  ? 2243 ARG A NH2   1 
ATOM   7356  N  N     . LEU A 1 2244 ? 161.696 113.826 127.646 1.00 69.10  ? 2244 LEU A N     1 
ATOM   7357  C  CA    . LEU A 1 2244 ? 161.409 114.172 126.258 1.00 68.57  ? 2244 LEU A CA    1 
ATOM   7358  C  C     . LEU A 1 2244 ? 162.685 114.461 125.473 1.00 73.43  ? 2244 LEU A C     1 
ATOM   7359  O  O     . LEU A 1 2244 ? 163.000 113.769 124.500 1.00 74.55  ? 2244 LEU A O     1 
ATOM   7360  C  CB    . LEU A 1 2244 ? 160.465 115.377 126.214 1.00 63.98  ? 2244 LEU A CB    1 
ATOM   7361  C  CG    . LEU A 1 2244 ? 160.069 115.934 124.848 1.00 65.91  ? 2244 LEU A CG    1 
ATOM   7362  C  CD1   . LEU A 1 2244 ? 159.107 114.997 124.140 1.00 69.55  ? 2244 LEU A CD1   1 
ATOM   7363  C  CD2   . LEU A 1 2244 ? 159.460 117.317 125.001 1.00 62.22  ? 2244 LEU A CD2   1 
ATOM   7364  N  N     . GLU A 1 2245 ? 163.431 115.486 125.886 1.00 75.42  ? 2245 GLU A N     1 
ATOM   7365  C  CA    . GLU A 1 2245 ? 164.627 115.891 125.159 1.00 74.22  ? 2245 GLU A CA    1 
ATOM   7366  C  C     . GLU A 1 2245 ? 165.813 114.973 125.414 1.00 77.91  ? 2245 GLU A C     1 
ATOM   7367  O  O     . GLU A 1 2245 ? 166.769 114.990 124.632 1.00 89.73  ? 2245 GLU A O     1 
ATOM   7368  C  CB    . GLU A 1 2245 ? 165.000 117.327 125.532 1.00 68.08  ? 2245 GLU A CB    1 
ATOM   7369  C  CG    . GLU A 1 2245 ? 163.843 118.305 125.436 1.00 67.25  ? 2245 GLU A CG    1 
ATOM   7370  C  CD    . GLU A 1 2245 ? 164.204 119.687 125.940 1.00 68.90  ? 2245 GLU A CD    1 
ATOM   7371  O  OE1   . GLU A 1 2245 ? 165.340 119.864 126.425 1.00 74.00  ? 2245 GLU A OE1   1 
ATOM   7372  O  OE2   . GLU A 1 2245 ? 163.353 120.596 125.847 1.00 63.67  ? 2245 GLU A OE2   1 
ATOM   7373  N  N     . GLY A 1 2246 ? 165.776 114.178 126.479 1.00 72.73  ? 2246 GLY A N     1 
ATOM   7374  C  CA    . GLY A 1 2246 ? 166.891 113.329 126.832 1.00 74.76  ? 2246 GLY A CA    1 
ATOM   7375  C  C     . GLY A 1 2246 ? 168.005 114.023 127.581 1.00 82.86  ? 2246 GLY A C     1 
ATOM   7376  O  O     . GLY A 1 2246 ? 168.988 113.364 127.943 1.00 86.55  ? 2246 GLY A O     1 
ATOM   7377  N  N     . VAL A 1 2247 ? 167.886 115.323 127.828 1.00 79.17  ? 2247 VAL A N     1 
ATOM   7378  C  CA    . VAL A 1 2247 ? 168.896 116.076 128.562 1.00 81.72  ? 2247 VAL A CA    1 
ATOM   7379  C  C     . VAL A 1 2247 ? 168.616 115.927 130.051 1.00 81.46  ? 2247 VAL A C     1 
ATOM   7380  O  O     . VAL A 1 2247 ? 167.497 116.181 130.510 1.00 78.20  ? 2247 VAL A O     1 
ATOM   7381  C  CB    . VAL A 1 2247 ? 168.898 117.554 128.146 1.00 83.92  ? 2247 VAL A CB    1 
ATOM   7382  C  CG1   . VAL A 1 2247 ? 169.953 118.323 128.924 1.00 82.85  ? 2247 VAL A CG1   1 
ATOM   7383  C  CG2   . VAL A 1 2247 ? 169.133 117.682 126.651 1.00 79.93  ? 2247 VAL A CG2   1 
ATOM   7384  N  N     . GLU A 1 2248 ? 169.631 115.510 130.803 1.00 85.71  ? 2248 GLU A N     1 
ATOM   7385  C  CA    . GLU A 1 2248 ? 169.469 115.318 132.237 1.00 88.00  ? 2248 GLU A CA    1 
ATOM   7386  C  C     . GLU A 1 2248 ? 169.156 116.648 132.912 1.00 84.86  ? 2248 GLU A C     1 
ATOM   7387  O  O     . GLU A 1 2248 ? 169.736 117.684 132.576 1.00 87.00  ? 2248 GLU A O     1 
ATOM   7388  C  CB    . GLU A 1 2248 ? 170.741 114.712 132.832 1.00 92.77  ? 2248 GLU A CB    1 
ATOM   7389  C  CG    . GLU A 1 2248 ? 170.650 114.378 134.309 1.00 93.41  ? 2248 GLU A CG    1 
ATOM   7390  C  CD    . GLU A 1 2248 ? 170.005 113.030 134.566 1.00 102.93 ? 2248 GLU A CD    1 
ATOM   7391  O  OE1   . GLU A 1 2248 ? 170.120 112.524 135.701 1.00 104.86 ? 2248 GLU A OE1   1 
ATOM   7392  O  OE2   . GLU A 1 2248 ? 169.408 112.462 133.627 1.00 101.73 ? 2248 GLU A OE2   1 
ATOM   7393  N  N     . GLY A 1 2249 ? 168.232 116.618 133.867 1.00 77.78  ? 2249 GLY A N     1 
ATOM   7394  C  CA    . GLY A 1 2249 ? 167.800 117.811 134.575 1.00 71.10  ? 2249 GLY A CA    1 
ATOM   7395  C  C     . GLY A 1 2249 ? 168.224 117.759 136.034 1.00 68.64  ? 2249 GLY A C     1 
ATOM   7396  O  O     . GLY A 1 2249 ? 167.990 116.765 136.723 1.00 79.20  ? 2249 GLY A O     1 
ATOM   7397  N  N     . VAL A 1 2250 ? 168.846 118.844 136.488 1.00 59.32  ? 2250 VAL A N     1 
ATOM   7398  C  CA    . VAL A 1 2250 ? 169.298 118.986 137.865 1.00 57.45  ? 2250 VAL A CA    1 
ATOM   7399  C  C     . VAL A 1 2250 ? 168.857 120.352 138.370 1.00 56.32  ? 2250 VAL A C     1 
ATOM   7400  O  O     . VAL A 1 2250 ? 169.033 121.359 137.676 1.00 60.27  ? 2250 VAL A O     1 
ATOM   7401  C  CB    . VAL A 1 2250 ? 170.827 118.825 137.983 1.00 64.33  ? 2250 VAL A CB    1 
ATOM   7402  C  CG1   . VAL A 1 2250 ? 171.330 119.399 139.297 1.00 65.27  ? 2250 VAL A CG1   1 
ATOM   7403  C  CG2   . VAL A 1 2250 ? 171.213 117.362 137.856 1.00 67.41  ? 2250 VAL A CG2   1 
ATOM   7404  N  N     . ALA A 1 2251 ? 168.282 120.382 139.569 1.00 52.68  ? 2251 ALA A N     1 
ATOM   7405  C  CA    . ALA A 1 2251 ? 167.784 121.604 140.180 1.00 48.28  ? 2251 ALA A CA    1 
ATOM   7406  C  C     . ALA A 1 2251 ? 168.540 121.883 141.470 1.00 49.71  ? 2251 ALA A C     1 
ATOM   7407  O  O     . ALA A 1 2251 ? 168.825 120.965 142.245 1.00 61.10  ? 2251 ALA A O     1 
ATOM   7408  C  CB    . ALA A 1 2251 ? 166.289 121.507 140.466 1.00 47.71  ? 2251 ALA A CB    1 
ATOM   7409  N  N     . HIS A 1 2252 ? 168.861 123.154 141.697 1.00 48.79  ? 2252 HIS A N     1 
ATOM   7410  C  CA    . HIS A 1 2252 ? 169.610 123.594 142.871 1.00 53.72  ? 2252 HIS A CA    1 
ATOM   7411  C  C     . HIS A 1 2252 ? 168.744 124.586 143.638 1.00 52.04  ? 2252 HIS A C     1 
ATOM   7412  O  O     . HIS A 1 2252 ? 168.843 125.797 143.430 1.00 55.44  ? 2252 HIS A O     1 
ATOM   7413  C  CB    . HIS A 1 2252 ? 170.944 124.220 142.466 1.00 54.21  ? 2252 HIS A CB    1 
ATOM   7414  C  CG    . HIS A 1 2252 ? 171.842 123.295 141.706 1.00 59.53  ? 2252 HIS A CG    1 
ATOM   7415  N  ND1   . HIS A 1 2252 ? 172.477 122.224 142.295 1.00 65.44  ? 2252 HIS A ND1   1 
ATOM   7416  C  CD2   . HIS A 1 2252 ? 172.211 123.282 140.403 1.00 59.01  ? 2252 HIS A CD2   1 
ATOM   7417  C  CE1   . HIS A 1 2252 ? 173.199 121.591 141.388 1.00 61.12  ? 2252 HIS A CE1   1 
ATOM   7418  N  NE2   . HIS A 1 2252 ? 173.055 122.212 140.232 1.00 63.30  ? 2252 HIS A NE2   1 
ATOM   7419  N  N     . ILE A 1 2253 ? 167.905 124.076 144.533 1.00 46.59  ? 2253 ILE A N     1 
ATOM   7420  C  CA    . ILE A 1 2253 ? 167.048 124.932 145.346 1.00 44.67  ? 2253 ILE A CA    1 
ATOM   7421  C  C     . ILE A 1 2253 ? 167.913 125.624 146.391 1.00 51.35  ? 2253 ILE A C     1 
ATOM   7422  O  O     . ILE A 1 2253 ? 168.501 124.969 147.257 1.00 60.54  ? 2253 ILE A O     1 
ATOM   7423  C  CB    . ILE A 1 2253 ? 165.917 124.130 146.004 1.00 45.86  ? 2253 ILE A CB    1 
ATOM   7424  C  CG1   . ILE A 1 2253 ? 165.009 123.508 144.942 1.00 44.62  ? 2253 ILE A CG1   1 
ATOM   7425  C  CG2   . ILE A 1 2253 ? 165.106 125.021 146.923 1.00 55.03  ? 2253 ILE A CG2   1 
ATOM   7426  C  CD1   . ILE A 1 2253 ? 165.321 122.063 144.634 1.00 44.58  ? 2253 ILE A CD1   1 
ATOM   7427  N  N     . ILE A 1 2254 ? 167.989 126.950 146.314 1.00 47.87  ? 2254 ILE A N     1 
ATOM   7428  C  CA    . ILE A 1 2254 ? 168.882 127.749 147.148 1.00 53.22  ? 2254 ILE A CA    1 
ATOM   7429  C  C     . ILE A 1 2254 ? 168.032 128.799 147.851 1.00 53.14  ? 2254 ILE A C     1 
ATOM   7430  O  O     . ILE A 1 2254 ? 167.779 129.873 147.294 1.00 55.89  ? 2254 ILE A O     1 
ATOM   7431  C  CB    . ILE A 1 2254 ? 170.003 128.406 146.335 1.00 50.80  ? 2254 ILE A CB    1 
ATOM   7432  C  CG1   . ILE A 1 2254 ? 170.883 127.344 145.677 1.00 48.07  ? 2254 ILE A CG1   1 
ATOM   7433  C  CG2   . ILE A 1 2254 ? 170.839 129.325 147.209 1.00 49.23  ? 2254 ILE A CG2   1 
ATOM   7434  C  CD1   . ILE A 1 2254 ? 171.958 127.916 144.791 1.00 51.40  ? 2254 ILE A CD1   1 
ATOM   7435  N  N     . ASP A 1 2255 ? 167.601 128.506 149.069 1.00 56.61  ? 2255 ASP A N     1 
ATOM   7436  C  CA    . ASP A 1 2255 ? 166.874 129.491 149.861 1.00 56.97  ? 2255 ASP A CA    1 
ATOM   7437  C  C     . ASP A 1 2255 ? 167.802 130.659 150.170 1.00 60.11  ? 2255 ASP A C     1 
ATOM   7438  O  O     . ASP A 1 2255 ? 168.780 130.477 150.906 1.00 64.48  ? 2255 ASP A O     1 
ATOM   7439  C  CB    . ASP A 1 2255 ? 166.351 128.863 151.151 1.00 59.19  ? 2255 ASP A CB    1 
ATOM   7440  C  CG    . ASP A 1 2255 ? 165.341 129.744 151.865 1.00 62.79  ? 2255 ASP A CG    1 
ATOM   7441  O  OD1   . ASP A 1 2255 ? 165.685 130.890 152.218 1.00 63.64  ? 2255 ASP A OD1   1 
ATOM   7442  O  OD2   . ASP A 1 2255 ? 164.199 129.286 152.078 1.00 59.06  ? 2255 ASP A OD2   1 
ATOM   7443  N  N     . PRO A 1 2256 ? 167.542 131.859 149.646 1.00 54.61  ? 2256 PRO A N     1 
ATOM   7444  C  CA    . PRO A 1 2256 ? 168.514 132.951 149.757 1.00 56.63  ? 2256 PRO A CA    1 
ATOM   7445  C  C     . PRO A 1 2256 ? 168.513 133.666 151.097 1.00 62.84  ? 2256 PRO A C     1 
ATOM   7446  O  O     . PRO A 1 2256 ? 169.378 134.519 151.320 1.00 65.91  ? 2256 PRO A O     1 
ATOM   7447  C  CB    . PRO A 1 2256 ? 168.071 133.897 148.638 1.00 58.56  ? 2256 PRO A CB    1 
ATOM   7448  C  CG    . PRO A 1 2256 ? 166.596 133.712 148.592 1.00 55.93  ? 2256 PRO A CG    1 
ATOM   7449  C  CD    . PRO A 1 2256 ? 166.342 132.262 148.896 1.00 52.10  ? 2256 PRO A CD    1 
ATOM   7450  N  N     . LYS A 1 2257 ? 167.575 133.351 151.990 1.00 63.26  ? 2257 LYS A N     1 
ATOM   7451  C  CA    . LYS A 1 2257 ? 167.466 134.046 153.263 1.00 60.88  ? 2257 LYS A CA    1 
ATOM   7452  C  C     . LYS A 1 2257 ? 167.841 133.194 154.463 1.00 64.35  ? 2257 LYS A C     1 
ATOM   7453  O  O     . LYS A 1 2257 ? 168.099 133.750 155.534 1.00 69.92  ? 2257 LYS A O     1 
ATOM   7454  C  CB    . LYS A 1 2257 ? 166.040 134.572 153.455 1.00 60.49  ? 2257 LYS A CB    1 
ATOM   7455  C  CG    . LYS A 1 2257 ? 165.698 135.696 152.514 1.00 60.14  ? 2257 LYS A CG    1 
ATOM   7456  C  CD    . LYS A 1 2257 ? 164.517 136.474 153.021 1.00 69.24  ? 2257 LYS A CD    1 
ATOM   7457  C  CE    . LYS A 1 2257 ? 164.279 137.688 152.169 1.00 74.61  ? 2257 LYS A CE    1 
ATOM   7458  N  NZ    . LYS A 1 2257 ? 165.468 138.579 152.137 1.00 77.79  ? 2257 LYS A NZ    1 
ATOM   7459  N  N     . ALA A 1 2258 ? 167.872 131.869 154.318 1.00 57.64  ? 2258 ALA A N     1 
ATOM   7460  C  CA    . ALA A 1 2258 ? 168.416 131.030 155.375 1.00 56.54  ? 2258 ALA A CA    1 
ATOM   7461  C  C     . ALA A 1 2258 ? 169.906 131.269 155.570 1.00 69.49  ? 2258 ALA A C     1 
ATOM   7462  O  O     . ALA A 1 2258 ? 170.451 130.915 156.621 1.00 68.36  ? 2258 ALA A O     1 
ATOM   7463  C  CB    . ALA A 1 2258 ? 168.151 129.558 155.065 1.00 53.78  ? 2258 ALA A CB    1 
ATOM   7464  N  N     . ILE A 1 2259 ? 170.570 131.864 154.581 1.00 72.46  ? 2259 ILE A N     1 
ATOM   7465  C  CA    . ILE A 1 2259 ? 171.984 132.197 154.645 1.00 68.58  ? 2259 ILE A CA    1 
ATOM   7466  C  C     . ILE A 1 2259 ? 172.139 133.689 154.381 1.00 70.06  ? 2259 ILE A C     1 
ATOM   7467  O  O     . ILE A 1 2259 ? 171.263 134.339 153.806 1.00 73.14  ? 2259 ILE A O     1 
ATOM   7468  C  CB    . ILE A 1 2259 ? 172.821 131.379 153.641 1.00 62.73  ? 2259 ILE A CB    1 
ATOM   7469  C  CG1   . ILE A 1 2259 ? 172.511 131.821 152.211 1.00 61.64  ? 2259 ILE A CG1   1 
ATOM   7470  C  CG2   . ILE A 1 2259 ? 172.556 129.894 153.807 1.00 66.73  ? 2259 ILE A CG2   1 
ATOM   7471  C  CD1   . ILE A 1 2259 ? 173.234 131.021 151.159 1.00 70.97  ? 2259 ILE A CD1   1 
ATOM   7472  N  N     . SER A 1 2260 ? 173.270 134.231 154.819 1.00 76.85  ? 2260 SER A N     1 
ATOM   7473  C  CA    . SER A 1 2260 ? 173.540 135.648 154.645 1.00 76.18  ? 2260 SER A CA    1 
ATOM   7474  C  C     . SER A 1 2260 ? 173.954 135.943 153.205 1.00 77.58  ? 2260 SER A C     1 
ATOM   7475  O  O     . SER A 1 2260 ? 174.221 135.042 152.405 1.00 80.63  ? 2260 SER A O     1 
ATOM   7476  C  CB    . SER A 1 2260 ? 174.626 136.109 155.614 1.00 78.70  ? 2260 SER A CB    1 
ATOM   7477  O  OG    . SER A 1 2260 ? 175.874 135.519 155.298 1.00 82.96  ? 2260 SER A OG    1 
ATOM   7478  N  N     . LYS A 1 2261 ? 173.996 137.236 152.876 1.00 78.21  ? 2261 LYS A N     1 
ATOM   7479  C  CA    . LYS A 1 2261 ? 174.448 137.650 151.551 1.00 84.08  ? 2261 LYS A CA    1 
ATOM   7480  C  C     . LYS A 1 2261 ? 175.901 137.256 151.321 1.00 82.72  ? 2261 LYS A C     1 
ATOM   7481  O  O     . LYS A 1 2261 ? 176.272 136.823 150.222 1.00 78.10  ? 2261 LYS A O     1 
ATOM   7482  C  CB    . LYS A 1 2261 ? 174.276 139.158 151.388 1.00 85.53  ? 2261 LYS A CB    1 
ATOM   7483  C  CG    . LYS A 1 2261 ? 174.500 139.664 149.977 1.00 82.77  ? 2261 LYS A CG    1 
ATOM   7484  C  CD    . LYS A 1 2261 ? 174.805 141.151 149.978 1.00 88.05  ? 2261 LYS A CD    1 
ATOM   7485  C  CE    . LYS A 1 2261 ? 173.659 141.951 150.570 1.00 86.47  ? 2261 LYS A CE    1 
ATOM   7486  N  NZ    . LYS A 1 2261 ? 173.860 143.416 150.398 1.00 83.46  ? 2261 LYS A NZ    1 
ATOM   7487  N  N     . ASP A 1 2262 ? 176.742 137.418 152.345 1.00 81.91  ? 2262 ASP A N     1 
ATOM   7488  C  CA    . ASP A 1 2262 ? 178.137 137.011 152.235 1.00 81.41  ? 2262 ASP A CA    1 
ATOM   7489  C  C     . ASP A 1 2262 ? 178.257 135.505 152.045 1.00 79.72  ? 2262 ASP A C     1 
ATOM   7490  O  O     . ASP A 1 2262 ? 179.112 135.033 151.290 1.00 84.46  ? 2262 ASP A O     1 
ATOM   7491  C  CB    . ASP A 1 2262 ? 178.910 137.464 153.472 1.00 86.71  ? 2262 ASP A CB    1 
ATOM   7492  C  CG    . ASP A 1 2262 ? 178.634 138.910 153.832 1.00 94.50  ? 2262 ASP A CG    1 
ATOM   7493  O  OD1   . ASP A 1 2262 ? 178.881 139.794 152.984 1.00 98.36  ? 2262 ASP A OD1   1 
ATOM   7494  O  OD2   . ASP A 1 2262 ? 178.166 139.165 154.962 1.00 92.48  ? 2262 ASP A OD2   1 
ATOM   7495  N  N     . HIS A 1 2263 ? 177.412 134.732 152.728 1.00 77.08  ? 2263 HIS A N     1 
ATOM   7496  C  CA    . HIS A 1 2263 ? 177.407 133.288 152.538 1.00 75.97  ? 2263 HIS A CA    1 
ATOM   7497  C  C     . HIS A 1 2263 ? 176.699 132.868 151.258 1.00 72.29  ? 2263 HIS A C     1 
ATOM   7498  O  O     . HIS A 1 2263 ? 176.747 131.684 150.906 1.00 74.92  ? 2263 HIS A O     1 
ATOM   7499  C  CB    . HIS A 1 2263 ? 176.755 132.602 153.738 1.00 75.41  ? 2263 HIS A CB    1 
ATOM   7500  C  CG    . HIS A 1 2263 ? 177.660 132.474 154.922 1.00 80.85  ? 2263 HIS A CG    1 
ATOM   7501  N  ND1   . HIS A 1 2263 ? 177.191 132.450 156.218 1.00 82.23  ? 2263 HIS A ND1   1 
ATOM   7502  C  CD2   . HIS A 1 2263 ? 179.006 132.365 155.008 1.00 84.69  ? 2263 HIS A CD2   1 
ATOM   7503  C  CE1   . HIS A 1 2263 ? 178.209 132.330 157.050 1.00 91.11  ? 2263 HIS A CE1   1 
ATOM   7504  N  NE2   . HIS A 1 2263 ? 179.322 132.277 156.341 1.00 90.75  ? 2263 HIS A NE2   1 
ATOM   7505  N  N     . LEU A 1 2264 ? 176.048 133.797 150.560 1.00 71.38  ? 2264 LEU A N     1 
ATOM   7506  C  CA    . LEU A 1 2264 ? 175.374 133.488 149.305 1.00 71.61  ? 2264 LEU A CA    1 
ATOM   7507  C  C     . LEU A 1 2264 ? 176.244 133.794 148.092 1.00 75.23  ? 2264 LEU A C     1 
ATOM   7508  O  O     . LEU A 1 2264 ? 176.305 132.989 147.158 1.00 71.56  ? 2264 LEU A O     1 
ATOM   7509  C  CB    . LEU A 1 2264 ? 174.057 134.263 149.213 1.00 72.31  ? 2264 LEU A CB    1 
ATOM   7510  C  CG    . LEU A 1 2264 ? 173.250 134.132 147.920 1.00 67.38  ? 2264 LEU A CG    1 
ATOM   7511  C  CD1   . LEU A 1 2264 ? 172.742 132.713 147.736 1.00 61.48  ? 2264 LEU A CD1   1 
ATOM   7512  C  CD2   . LEU A 1 2264 ? 172.096 135.118 147.915 1.00 63.53  ? 2264 LEU A CD2   1 
ATOM   7513  N  N     . TYR A 1 2265 ? 176.923 134.942 148.088 1.00 81.58  ? 2265 TYR A N     1 
ATOM   7514  C  CA    . TYR A 1 2265 ? 177.768 135.343 146.969 1.00 81.00  ? 2265 TYR A CA    1 
ATOM   7515  C  C     . TYR A 1 2265 ? 179.255 135.230 147.276 1.00 82.24  ? 2265 TYR A C     1 
ATOM   7516  O  O     . TYR A 1 2265 ? 180.080 135.516 146.402 1.00 83.50  ? 2265 TYR A O     1 
ATOM   7517  C  CB    . TYR A 1 2265 ? 177.445 136.775 146.543 1.00 78.46  ? 2265 TYR A CB    1 
ATOM   7518  C  CG    . TYR A 1 2265 ? 176.068 136.946 145.957 1.00 73.47  ? 2265 TYR A CG    1 
ATOM   7519  C  CD1   . TYR A 1 2265 ? 175.667 136.211 144.853 1.00 67.51  ? 2265 TYR A CD1   1 
ATOM   7520  C  CD2   . TYR A 1 2265 ? 175.173 137.850 146.504 1.00 75.65  ? 2265 TYR A CD2   1 
ATOM   7521  C  CE1   . TYR A 1 2265 ? 174.410 136.367 144.316 1.00 70.41  ? 2265 TYR A CE1   1 
ATOM   7522  C  CE2   . TYR A 1 2265 ? 173.917 138.013 145.975 1.00 73.74  ? 2265 TYR A CE2   1 
ATOM   7523  C  CZ    . TYR A 1 2265 ? 173.539 137.270 144.881 1.00 71.98  ? 2265 TYR A CZ    1 
ATOM   7524  O  OH    . TYR A 1 2265 ? 172.282 137.435 144.353 1.00 76.26  ? 2265 TYR A OH    1 
ATOM   7525  N  N     . GLY A 1 2266 ? 179.619 134.832 148.485 1.00 83.48  ? 2266 GLY A N     1 
ATOM   7526  C  CA    . GLY A 1 2266 ? 181.011 134.756 148.863 1.00 86.27  ? 2266 GLY A CA    1 
ATOM   7527  C  C     . GLY A 1 2266 ? 181.551 136.086 149.356 1.00 89.97  ? 2266 GLY A C     1 
ATOM   7528  O  O     . GLY A 1 2266 ? 180.936 137.142 149.211 1.00 88.63  ? 2266 GLY A O     1 
ATOM   7529  N  N     . THR A 1 2267 ? 182.737 136.022 149.956 1.00 90.26  ? 2267 THR A N     1 
ATOM   7530  C  CA    . THR A 1 2267 ? 183.384 137.210 150.488 1.00 95.13  ? 2267 THR A CA    1 
ATOM   7531  C  C     . THR A 1 2267 ? 184.887 136.989 150.510 1.00 100.55 ? 2267 THR A C     1 
ATOM   7532  O  O     . THR A 1 2267 ? 185.363 135.852 150.563 1.00 102.82 ? 2267 THR A O     1 
ATOM   7533  C  CB    . THR A 1 2267 ? 182.879 137.548 151.897 1.00 96.42  ? 2267 THR A CB    1 
ATOM   7534  O  OG1   . THR A 1 2267 ? 183.581 138.692 152.398 1.00 100.50 ? 2267 THR A OG1   1 
ATOM   7535  C  CG2   . THR A 1 2267 ? 183.095 136.373 152.839 1.00 93.00  ? 2267 THR A CG2   1 
ATOM   7536  N  N     . LEU A 1 2268 ? 185.629 138.090 150.465 1.00 101.03 ? 2268 LEU A N     1 
ATOM   7537  C  CA    . LEU A 1 2268 ? 187.080 138.069 150.558 1.00 100.02 ? 2268 LEU A CA    1 
ATOM   7538  C  C     . LEU A 1 2268 ? 187.516 138.863 151.781 1.00 104.32 ? 2268 LEU A C     1 
ATOM   7539  O  O     . LEU A 1 2268 ? 186.955 139.922 152.079 1.00 105.58 ? 2268 LEU A O     1 
ATOM   7540  C  CB    . LEU A 1 2268 ? 187.735 138.639 149.294 1.00 100.54 ? 2268 LEU A CB    1 
ATOM   7541  C  CG    . LEU A 1 2268 ? 187.694 140.146 149.026 1.00 103.60 ? 2268 LEU A CG    1 
ATOM   7542  C  CD1   . LEU A 1 2268 ? 188.703 140.511 147.951 1.00 103.59 ? 2268 LEU A CD1   1 
ATOM   7543  C  CD2   . LEU A 1 2268 ? 186.304 140.611 148.628 1.00 104.20 ? 2268 LEU A CD2   1 
ATOM   7544  N  N     . ASP A 1 2269 ? 188.502 138.340 152.492 1.00 105.57 ? 2269 ASP A N     1 
ATOM   7545  C  CA    . ASP A 1 2269 ? 188.990 139.000 153.695 1.00 104.19 ? 2269 ASP A CA    1 
ATOM   7546  C  C     . ASP A 1 2269 ? 189.787 140.239 153.310 1.00 105.08 ? 2269 ASP A C     1 
ATOM   7547  O  O     . ASP A 1 2269 ? 190.785 140.120 152.588 1.00 101.42 ? 2269 ASP A O     1 
ATOM   7548  C  CB    . ASP A 1 2269 ? 189.853 138.037 154.505 1.00 102.78 ? 2269 ASP A CB    1 
ATOM   7549  C  CG    . ASP A 1 2269 ? 189.949 138.423 155.966 1.00 103.69 ? 2269 ASP A CG    1 
ATOM   7550  O  OD1   . ASP A 1 2269 ? 189.427 139.493 156.339 1.00 102.98 ? 2269 ASP A OD1   1 
ATOM   7551  O  OD2   . ASP A 1 2269 ? 190.548 137.652 156.745 1.00 103.88 ? 2269 ASP A OD2   1 
ATOM   7552  N  N     . PRO A 1 2270 ? 189.391 141.436 153.749 1.00 106.50 ? 2270 PRO A N     1 
ATOM   7553  C  CA    . PRO A 1 2270 ? 190.187 142.630 153.421 1.00 105.57 ? 2270 PRO A CA    1 
ATOM   7554  C  C     . PRO A 1 2270 ? 191.601 142.578 153.969 1.00 104.75 ? 2270 PRO A C     1 
ATOM   7555  O  O     . PRO A 1 2270 ? 192.507 143.185 153.386 1.00 101.56 ? 2270 PRO A O     1 
ATOM   7556  C  CB    . PRO A 1 2270 ? 189.376 143.774 154.046 1.00 104.21 ? 2270 PRO A CB    1 
ATOM   7557  C  CG    . PRO A 1 2270 ? 188.534 143.121 155.094 1.00 100.75 ? 2270 PRO A CG    1 
ATOM   7558  C  CD    . PRO A 1 2270 ? 188.202 141.767 154.553 1.00 102.55 ? 2270 PRO A CD    1 
ATOM   7559  N  N     . ASN A 1 2271 ? 191.816 141.869 155.079 1.00 105.41 ? 2271 ASN A N     1 
ATOM   7560  C  CA    . ASN A 1 2271 ? 193.144 141.816 155.678 1.00 98.09  ? 2271 ASN A CA    1 
ATOM   7561  C  C     . ASN A 1 2271 ? 194.087 140.928 154.876 1.00 95.17  ? 2271 ASN A C     1 
ATOM   7562  O  O     . ASN A 1 2271 ? 195.250 141.286 154.660 1.00 93.72  ? 2271 ASN A O     1 
ATOM   7563  C  CB    . ASN A 1 2271 ? 193.045 141.320 157.119 1.00 95.11  ? 2271 ASN A CB    1 
ATOM   7564  C  CG    . ASN A 1 2271 ? 192.299 142.285 158.015 1.00 93.28  ? 2271 ASN A CG    1 
ATOM   7565  O  OD1   . ASN A 1 2271 ? 192.813 143.346 158.368 1.00 90.56  ? 2271 ASN A OD1   1 
ATOM   7566  N  ND2   . ASN A 1 2271 ? 191.079 141.920 158.390 1.00 92.15  ? 2271 ASN A ND2   1 
ATOM   7567  N  N     . THR A 1 2272 ? 193.609 139.767 154.425 1.00 97.31  ? 2272 THR A N     1 
ATOM   7568  C  CA    . THR A 1 2272 ? 194.463 138.784 153.776 1.00 98.79  ? 2272 THR A CA    1 
ATOM   7569  C  C     . THR A 1 2272 ? 194.134 138.534 152.311 1.00 103.72 ? 2272 THR A C     1 
ATOM   7570  O  O     . THR A 1 2272 ? 194.860 137.772 151.663 1.00 102.31 ? 2272 THR A O     1 
ATOM   7571  C  CB    . THR A 1 2272 ? 194.402 137.445 154.527 1.00 100.74 ? 2272 THR A CB    1 
ATOM   7572  O  OG1   . THR A 1 2272 ? 193.102 136.865 154.369 1.00 108.67 ? 2272 THR A OG1   1 
ATOM   7573  C  CG2   . THR A 1 2272 ? 194.680 137.652 156.006 1.00 96.85  ? 2272 THR A CG2   1 
ATOM   7574  N  N     . ARG A 1 2273 ? 193.078 139.149 151.772 1.00 104.32 ? 2273 ARG A N     1 
ATOM   7575  C  CA    . ARG A 1 2273 ? 192.677 138.960 150.375 1.00 110.03 ? 2273 ARG A CA    1 
ATOM   7576  C  C     . ARG A 1 2273 ? 192.476 137.482 150.045 1.00 113.31 ? 2273 ARG A C     1 
ATOM   7577  O  O     . ARG A 1 2273 ? 192.875 137.003 148.981 1.00 115.40 ? 2273 ARG A O     1 
ATOM   7578  C  CB    . ARG A 1 2273 ? 193.682 139.602 149.416 1.00 111.30 ? 2273 ARG A CB    1 
ATOM   7579  C  CG    . ARG A 1 2273 ? 193.236 140.950 148.874 1.00 109.30 ? 2273 ARG A CG    1 
ATOM   7580  C  CD    . ARG A 1 2273 ? 193.314 142.032 149.936 1.00 112.92 ? 2273 ARG A CD    1 
ATOM   7581  N  NE    . ARG A 1 2273 ? 192.805 143.310 149.452 1.00 119.79 ? 2273 ARG A NE    1 
ATOM   7582  C  CZ    . ARG A 1 2273 ? 193.490 144.151 148.689 1.00 120.71 ? 2273 ARG A CZ    1 
ATOM   7583  N  NH1   . ARG A 1 2273 ? 194.726 143.885 148.302 1.00 115.09 ? 2273 ARG A NH1   1 
ATOM   7584  N  NH2   . ARG A 1 2273 ? 192.920 145.290 148.307 1.00 119.92 ? 2273 ARG A NH2   1 
ATOM   7585  N  N     . GLU A 1 2274 ? 191.851 136.754 150.965 1.00 110.97 ? 2274 GLU A N     1 
ATOM   7586  C  CA    . GLU A 1 2274 ? 191.533 135.346 150.774 1.00 110.60 ? 2274 GLU A CA    1 
ATOM   7587  C  C     . GLU A 1 2274 ? 190.072 135.239 150.357 1.00 111.01 ? 2274 GLU A C     1 
ATOM   7588  O  O     . GLU A 1 2274 ? 189.179 135.664 151.098 1.00 109.05 ? 2274 GLU A O     1 
ATOM   7589  C  CB    . GLU A 1 2274 ? 191.804 134.551 152.052 1.00 114.75 ? 2274 GLU A CB    1 
ATOM   7590  C  CG    . GLU A 1 2274 ? 191.731 133.036 151.899 1.00 118.67 ? 2274 GLU A CG    1 
ATOM   7591  C  CD    . GLU A 1 2274 ? 190.317 132.496 152.000 1.00 124.17 ? 2274 GLU A CD    1 
ATOM   7592  O  OE1   . GLU A 1 2274 ? 189.487 133.122 152.693 1.00 123.41 ? 2274 GLU A OE1   1 
ATOM   7593  O  OE2   . GLU A 1 2274 ? 190.036 131.443 151.390 1.00 122.49 ? 2274 GLU A OE2   1 
ATOM   7594  N  N     . TRP A 1 2275 ? 189.833 134.675 149.177 1.00 110.84 ? 2275 TRP A N     1 
ATOM   7595  C  CA    . TRP A 1 2275 ? 188.498 134.629 148.599 1.00 104.04 ? 2275 TRP A CA    1 
ATOM   7596  C  C     . TRP A 1 2275 ? 187.772 133.357 149.009 1.00 106.95 ? 2275 TRP A C     1 
ATOM   7597  O  O     . TRP A 1 2275 ? 188.358 132.271 149.039 1.00 110.03 ? 2275 TRP A O     1 
ATOM   7598  C  CB    . TRP A 1 2275 ? 188.566 134.713 147.074 1.00 98.92  ? 2275 TRP A CB    1 
ATOM   7599  C  CG    . TRP A 1 2275 ? 187.248 134.462 146.410 1.00 99.06  ? 2275 TRP A CG    1 
ATOM   7600  C  CD1   . TRP A 1 2275 ? 186.913 133.394 145.630 1.00 97.87  ? 2275 TRP A CD1   1 
ATOM   7601  C  CD2   . TRP A 1 2275 ? 186.087 135.298 146.466 1.00 97.22  ? 2275 TRP A CD2   1 
ATOM   7602  N  NE1   . TRP A 1 2275 ? 185.614 133.512 145.200 1.00 92.64  ? 2275 TRP A NE1   1 
ATOM   7603  C  CE2   . TRP A 1 2275 ? 185.085 134.673 145.699 1.00 93.29  ? 2275 TRP A CE2   1 
ATOM   7604  C  CE3   . TRP A 1 2275 ? 185.797 136.514 147.091 1.00 96.31  ? 2275 TRP A CE3   1 
ATOM   7605  C  CZ2   . TRP A 1 2275 ? 183.817 135.222 145.542 1.00 90.46  ? 2275 TRP A CZ2   1 
ATOM   7606  C  CZ3   . TRP A 1 2275 ? 184.537 137.057 146.932 1.00 91.05  ? 2275 TRP A CZ3   1 
ATOM   7607  C  CH2   . TRP A 1 2275 ? 183.563 136.412 146.164 1.00 89.26  ? 2275 TRP A CH2   1 
ATOM   7608  N  N     . THR A 1 2276 ? 186.488 133.501 149.325 1.00 104.47 ? 2276 THR A N     1 
ATOM   7609  C  CA    . THR A 1 2276 ? 185.613 132.383 149.642 1.00 100.43 ? 2276 THR A CA    1 
ATOM   7610  C  C     . THR A 1 2276 ? 184.433 132.383 148.682 1.00 96.50  ? 2276 THR A C     1 
ATOM   7611  O  O     . THR A 1 2276 ? 183.855 133.436 148.397 1.00 99.13  ? 2276 THR A O     1 
ATOM   7612  C  CB    . THR A 1 2276 ? 185.107 132.463 151.086 1.00 103.09 ? 2276 THR A CB    1 
ATOM   7613  O  OG1   . THR A 1 2276 ? 184.174 133.544 151.206 1.00 102.51 ? 2276 THR A OG1   1 
ATOM   7614  C  CG2   . THR A 1 2276 ? 186.263 132.694 152.046 1.00 103.95 ? 2276 THR A CG2   1 
ATOM   7615  N  N     . ASP A 1 2277 ? 184.081 131.204 148.177 1.00 90.90  ? 2277 ASP A N     1 
ATOM   7616  C  CA    . ASP A 1 2277 ? 182.936 131.058 147.290 1.00 86.47  ? 2277 ASP A CA    1 
ATOM   7617  C  C     . ASP A 1 2277 ? 181.658 130.927 148.106 1.00 87.72  ? 2277 ASP A C     1 
ATOM   7618  O  O     . ASP A 1 2277 ? 181.593 130.128 149.045 1.00 94.77  ? 2277 ASP A O     1 
ATOM   7619  C  CB    . ASP A 1 2277 ? 183.099 129.840 146.379 1.00 80.63  ? 2277 ASP A CB    1 
ATOM   7620  C  CG    . ASP A 1 2277 ? 184.008 130.110 145.201 1.00 87.02  ? 2277 ASP A CG    1 
ATOM   7621  O  OD1   . ASP A 1 2277 ? 184.079 131.275 144.757 1.00 88.72  ? 2277 ASP A OD1   1 
ATOM   7622  O  OD2   . ASP A 1 2277 ? 184.646 129.155 144.711 1.00 88.47  ? 2277 ASP A OD2   1 
ATOM   7623  N  N     . GLY A 1 2278 ? 180.649 131.713 147.748 1.00 78.84  ? 2278 GLY A N     1 
ATOM   7624  C  CA    . GLY A 1 2278 ? 179.336 131.582 148.337 1.00 72.81  ? 2278 GLY A CA    1 
ATOM   7625  C  C     . GLY A 1 2278 ? 178.573 130.432 147.712 1.00 70.52  ? 2278 GLY A C     1 
ATOM   7626  O  O     . GLY A 1 2278 ? 179.044 129.750 146.802 1.00 72.69  ? 2278 GLY A O     1 
ATOM   7627  N  N     . LEU A 1 2279 ? 177.360 130.221 148.220 1.00 70.36  ? 2279 LEU A N     1 
ATOM   7628  C  CA    . LEU A 1 2279 ? 176.554 129.092 147.765 1.00 66.80  ? 2279 LEU A CA    1 
ATOM   7629  C  C     . LEU A 1 2279 ? 176.204 129.216 146.286 1.00 67.84  ? 2279 LEU A C     1 
ATOM   7630  O  O     . LEU A 1 2279 ? 176.450 128.294 145.498 1.00 70.26  ? 2279 LEU A O     1 
ATOM   7631  C  CB    . LEU A 1 2279 ? 175.292 128.988 148.617 1.00 59.07  ? 2279 LEU A CB    1 
ATOM   7632  C  CG    . LEU A 1 2279 ? 174.373 127.807 148.337 1.00 58.33  ? 2279 LEU A CG    1 
ATOM   7633  C  CD1   . LEU A 1 2279 ? 175.150 126.508 148.396 1.00 61.17  ? 2279 LEU A CD1   1 
ATOM   7634  C  CD2   . LEU A 1 2279 ? 173.258 127.806 149.354 1.00 59.88  ? 2279 LEU A CD2   1 
ATOM   7635  N  N     . PHE A 1 2280 ? 175.639 130.358 145.889 1.00 63.82  ? 2280 PHE A N     1 
ATOM   7636  C  CA    . PHE A 1 2280 ? 175.289 130.558 144.487 1.00 60.62  ? 2280 PHE A CA    1 
ATOM   7637  C  C     . PHE A 1 2280 ? 176.533 130.586 143.610 1.00 63.46  ? 2280 PHE A C     1 
ATOM   7638  O  O     . PHE A 1 2280 ? 176.545 130.010 142.516 1.00 62.62  ? 2280 PHE A O     1 
ATOM   7639  C  CB    . PHE A 1 2280 ? 174.486 131.847 144.324 1.00 58.54  ? 2280 PHE A CB    1 
ATOM   7640  C  CG    . PHE A 1 2280 ? 174.179 132.192 142.897 1.00 57.56  ? 2280 PHE A CG    1 
ATOM   7641  C  CD1   . PHE A 1 2280 ? 173.413 131.346 142.118 1.00 56.88  ? 2280 PHE A CD1   1 
ATOM   7642  C  CD2   . PHE A 1 2280 ? 174.658 133.360 142.335 1.00 60.97  ? 2280 PHE A CD2   1 
ATOM   7643  C  CE1   . PHE A 1 2280 ? 173.131 131.660 140.805 1.00 56.38  ? 2280 PHE A CE1   1 
ATOM   7644  C  CE2   . PHE A 1 2280 ? 174.378 133.679 141.023 1.00 60.56  ? 2280 PHE A CE2   1 
ATOM   7645  C  CZ    . PHE A 1 2280 ? 173.614 132.827 140.257 1.00 56.91  ? 2280 PHE A CZ    1 
ATOM   7646  N  N     . THR A 1 2281 ? 177.592 131.252 144.076 1.00 68.00  ? 2281 THR A N     1 
ATOM   7647  C  CA    . THR A 1 2281 ? 178.832 131.289 143.311 1.00 61.20  ? 2281 THR A CA    1 
ATOM   7648  C  C     . THR A 1 2281 ? 179.454 129.904 143.204 1.00 62.94  ? 2281 THR A C     1 
ATOM   7649  O  O     . THR A 1 2281 ? 179.990 129.542 142.154 1.00 72.82  ? 2281 THR A O     1 
ATOM   7650  C  CB    . THR A 1 2281 ? 179.819 132.271 143.938 1.00 67.57  ? 2281 THR A CB    1 
ATOM   7651  O  OG1   . THR A 1 2281 ? 180.112 131.868 145.280 1.00 80.38  ? 2281 THR A OG1   1 
ATOM   7652  C  CG2   . THR A 1 2281 ? 179.230 133.667 143.953 1.00 68.34  ? 2281 THR A CG2   1 
ATOM   7653  N  N     . HIS A 1 2282 ? 179.396 129.114 144.280 1.00 62.83  ? 2282 HIS A N     1 
ATOM   7654  C  CA    . HIS A 1 2282 ? 179.918 127.752 144.212 1.00 65.48  ? 2282 HIS A CA    1 
ATOM   7655  C  C     . HIS A 1 2282 ? 179.144 126.917 143.203 1.00 68.39  ? 2282 HIS A C     1 
ATOM   7656  O  O     . HIS A 1 2282 ? 179.741 126.180 142.410 1.00 71.63  ? 2282 HIS A O     1 
ATOM   7657  C  CB    . HIS A 1 2282 ? 179.872 127.090 145.588 1.00 72.30  ? 2282 HIS A CB    1 
ATOM   7658  C  CG    . HIS A 1 2282 ? 180.087 125.609 145.553 1.00 76.25  ? 2282 HIS A CG    1 
ATOM   7659  N  ND1   . HIS A 1 2282 ? 181.264 125.038 145.123 1.00 76.69  ? 2282 HIS A ND1   1 
ATOM   7660  C  CD2   . HIS A 1 2282 ? 179.271 124.582 145.888 1.00 75.55  ? 2282 HIS A CD2   1 
ATOM   7661  C  CE1   . HIS A 1 2282 ? 181.167 123.723 145.199 1.00 76.45  ? 2282 HIS A CE1   1 
ATOM   7662  N  NE2   . HIS A 1 2282 ? 179.967 123.420 145.660 1.00 74.37  ? 2282 HIS A NE2   1 
ATOM   7663  N  N     . VAL A 1 2283 ? 177.812 127.024 143.211 1.00 67.82  ? 2283 VAL A N     1 
ATOM   7664  C  CA    . VAL A 1 2283 ? 177.003 126.260 142.263 1.00 67.00  ? 2283 VAL A CA    1 
ATOM   7665  C  C     . VAL A 1 2283 ? 177.326 126.677 140.833 1.00 67.95  ? 2283 VAL A C     1 
ATOM   7666  O  O     . VAL A 1 2283 ? 177.534 125.834 139.950 1.00 72.45  ? 2283 VAL A O     1 
ATOM   7667  C  CB    . VAL A 1 2283 ? 175.505 126.432 142.575 1.00 65.85  ? 2283 VAL A CB    1 
ATOM   7668  C  CG1   . VAL A 1 2283 ? 174.661 125.861 141.451 1.00 64.59  ? 2283 VAL A CG1   1 
ATOM   7669  C  CG2   . VAL A 1 2283 ? 175.157 125.767 143.895 1.00 61.46  ? 2283 VAL A CG2   1 
ATOM   7670  N  N     . LEU A 1 2284 ? 177.384 127.989 140.588 1.00 66.94  ? 2284 LEU A N     1 
ATOM   7671  C  CA    . LEU A 1 2284 ? 177.662 128.480 139.243 1.00 63.97  ? 2284 LEU A CA    1 
ATOM   7672  C  C     . LEU A 1 2284 ? 179.050 128.064 138.774 1.00 68.74  ? 2284 LEU A C     1 
ATOM   7673  O  O     . LEU A 1 2284 ? 179.225 127.663 137.620 1.00 70.68  ? 2284 LEU A O     1 
ATOM   7674  C  CB    . LEU A 1 2284 ? 177.512 129.999 139.198 1.00 61.22  ? 2284 LEU A CB    1 
ATOM   7675  C  CG    . LEU A 1 2284 ? 177.117 130.582 137.842 1.00 68.87  ? 2284 LEU A CG    1 
ATOM   7676  C  CD1   . LEU A 1 2284 ? 175.837 129.938 137.346 1.00 70.85  ? 2284 LEU A CD1   1 
ATOM   7677  C  CD2   . LEU A 1 2284 ? 176.958 132.090 137.936 1.00 66.18  ? 2284 LEU A CD2   1 
ATOM   7678  N  N     . ARG A 1 2285 ? 180.049 128.154 139.655 1.00 68.44  ? 2285 ARG A N     1 
ATOM   7679  C  CA    . ARG A 1 2285 ? 181.402 127.752 139.290 1.00 65.95  ? 2285 ARG A CA    1 
ATOM   7680  C  C     . ARG A 1 2285 ? 181.476 126.260 138.999 1.00 71.09  ? 2285 ARG A C     1 
ATOM   7681  O  O     . ARG A 1 2285 ? 182.156 125.842 138.056 1.00 78.79  ? 2285 ARG A O     1 
ATOM   7682  C  CB    . ARG A 1 2285 ? 182.376 128.131 140.404 1.00 70.67  ? 2285 ARG A CB    1 
ATOM   7683  C  CG    . ARG A 1 2285 ? 183.836 128.067 139.997 1.00 77.61  ? 2285 ARG A CG    1 
ATOM   7684  C  CD    . ARG A 1 2285 ? 184.732 128.658 141.069 1.00 78.37  ? 2285 ARG A CD    1 
ATOM   7685  N  NE    . ARG A 1 2285 ? 184.271 129.970 141.503 1.00 79.18  ? 2285 ARG A NE    1 
ATOM   7686  C  CZ    . ARG A 1 2285 ? 184.952 131.095 141.333 1.00 86.73  ? 2285 ARG A CZ    1 
ATOM   7687  N  NH1   . ARG A 1 2285 ? 186.129 131.106 140.732 1.00 88.49  ? 2285 ARG A NH1   1 
ATOM   7688  N  NH2   . ARG A 1 2285 ? 184.438 132.238 141.778 1.00 92.79  ? 2285 ARG A NH2   1 
ATOM   7689  N  N     . LYS A 1 2286 ? 180.787 125.441 139.798 1.00 72.54  ? 2286 LYS A N     1 
ATOM   7690  C  CA    . LYS A 1 2286 ? 180.779 124.006 139.541 1.00 78.47  ? 2286 LYS A CA    1 
ATOM   7691  C  C     . LYS A 1 2286 ? 180.133 123.694 138.199 1.00 79.44  ? 2286 LYS A C     1 
ATOM   7692  O  O     . LYS A 1 2286 ? 180.593 122.806 137.472 1.00 82.90  ? 2286 LYS A O     1 
ATOM   7693  C  CB    . LYS A 1 2286 ? 180.060 123.269 140.670 1.00 78.59  ? 2286 LYS A CB    1 
ATOM   7694  C  CG    . LYS A 1 2286 ? 180.139 121.757 140.557 1.00 84.24  ? 2286 LYS A CG    1 
ATOM   7695  C  CD    . LYS A 1 2286 ? 179.310 121.071 141.628 1.00 90.14  ? 2286 LYS A CD    1 
ATOM   7696  C  CE    . LYS A 1 2286 ? 179.982 121.164 142.988 1.00 92.36  ? 2286 LYS A CE    1 
ATOM   7697  N  NZ    . LYS A 1 2286 ? 179.235 120.401 144.026 1.00 99.29  ? 2286 LYS A NZ    1 
ATOM   7698  N  N     . ILE A 1 2287 ? 179.059 124.408 137.855 1.00 78.75  ? 2287 ILE A N     1 
ATOM   7699  C  CA    . ILE A 1 2287 ? 178.435 124.204 136.549 1.00 79.85  ? 2287 ILE A CA    1 
ATOM   7700  C  C     . ILE A 1 2287 ? 179.378 124.631 135.429 1.00 83.12  ? 2287 ILE A C     1 
ATOM   7701  O  O     . ILE A 1 2287 ? 179.511 123.939 134.413 1.00 85.24  ? 2287 ILE A O     1 
ATOM   7702  C  CB    . ILE A 1 2287 ? 177.091 124.948 136.466 1.00 75.29  ? 2287 ILE A CB    1 
ATOM   7703  C  CG1   . ILE A 1 2287 ? 176.126 124.431 137.533 1.00 70.51  ? 2287 ILE A CG1   1 
ATOM   7704  C  CG2   . ILE A 1 2287 ? 176.487 124.777 135.089 1.00 77.52  ? 2287 ILE A CG2   1 
ATOM   7705  C  CD1   . ILE A 1 2287 ? 174.886 125.278 137.692 1.00 64.38  ? 2287 ILE A CD1   1 
ATOM   7706  N  N     . ILE A 1 2288 ? 180.046 125.775 135.597 1.00 80.27  ? 2288 ILE A N     1 
ATOM   7707  C  CA    . ILE A 1 2288 ? 180.914 126.303 134.546 1.00 79.02  ? 2288 ILE A CA    1 
ATOM   7708  C  C     . ILE A 1 2288 ? 182.102 125.379 134.306 1.00 85.31  ? 2288 ILE A C     1 
ATOM   7709  O  O     . ILE A 1 2288 ? 182.479 125.118 133.157 1.00 90.94  ? 2288 ILE A O     1 
ATOM   7710  C  CB    . ILE A 1 2288 ? 181.366 127.731 134.900 1.00 75.10  ? 2288 ILE A CB    1 
ATOM   7711  C  CG1   . ILE A 1 2288 ? 180.177 128.686 134.836 1.00 77.34  ? 2288 ILE A CG1   1 
ATOM   7712  C  CG2   . ILE A 1 2288 ? 182.471 128.194 133.969 1.00 79.71  ? 2288 ILE A CG2   1 
ATOM   7713  C  CD1   . ILE A 1 2288 ? 180.509 130.090 135.235 1.00 77.44  ? 2288 ILE A CD1   1 
ATOM   7714  N  N     . ASP A 1 2289 ? 182.711 124.872 135.381 1.00 82.90  ? 2289 ASP A N     1 
ATOM   7715  C  CA    . ASP A 1 2289 ? 183.868 123.995 135.225 1.00 84.79  ? 2289 ASP A CA    1 
ATOM   7716  C  C     . ASP A 1 2289 ? 183.500 122.722 134.474 1.00 90.60  ? 2289 ASP A C     1 
ATOM   7717  O  O     . ASP A 1 2289 ? 184.284 122.230 133.654 1.00 93.69  ? 2289 ASP A O     1 
ATOM   7718  C  CB    . ASP A 1 2289 ? 184.467 123.660 136.591 1.00 86.37  ? 2289 ASP A CB    1 
ATOM   7719  C  CG    . ASP A 1 2289 ? 185.038 124.877 137.291 1.00 88.36  ? 2289 ASP A CG    1 
ATOM   7720  O  OD1   . ASP A 1 2289 ? 185.780 125.644 136.643 1.00 92.53  ? 2289 ASP A OD1   1 
ATOM   7721  O  OD2   . ASP A 1 2289 ? 184.760 125.059 138.494 1.00 88.59  ? 2289 ASP A OD2   1 
ATOM   7722  N  N     . SER A 1 2290 ? 182.313 122.178 134.742 1.00 89.96  ? 2290 SER A N     1 
ATOM   7723  C  CA    . SER A 1 2290 ? 181.790 121.011 134.032 1.00 95.18  ? 2290 SER A CA    1 
ATOM   7724  C  C     . SER A 1 2290 ? 182.737 119.820 134.147 1.00 101.94 ? 2290 SER A C     1 
ATOM   7725  O  O     . SER A 1 2290 ? 183.127 119.202 133.155 1.00 105.96 ? 2290 SER A O     1 
ATOM   7726  C  CB    . SER A 1 2290 ? 181.504 121.344 132.568 1.00 92.27  ? 2290 SER A CB    1 
ATOM   7727  O  OG    . SER A 1 2290 ? 180.853 120.267 131.918 1.00 95.47  ? 2290 SER A OG    1 
ATOM   7728  N  N     . VAL A 1 2291 ? 183.116 119.503 135.386 1.00 104.29 ? 2291 VAL A N     1 
ATOM   7729  C  CA    . VAL A 1 2291 ? 183.968 118.342 135.624 1.00 111.18 ? 2291 VAL A CA    1 
ATOM   7730  C  C     . VAL A 1 2291 ? 183.224 117.059 135.276 1.00 114.43 ? 2291 VAL A C     1 
ATOM   7731  O  O     . VAL A 1 2291 ? 183.807 116.110 134.738 1.00 111.61 ? 2291 VAL A O     1 
ATOM   7732  C  CB    . VAL A 1 2291 ? 184.466 118.336 137.082 1.00 106.32 ? 2291 VAL A CB    1 
ATOM   7733  C  CG1   . VAL A 1 2291 ? 185.370 117.139 137.334 1.00 107.48 ? 2291 VAL A CG1   1 
ATOM   7734  C  CG2   . VAL A 1 2291 ? 185.190 119.634 137.397 1.00 96.82  ? 2291 VAL A CG2   1 
ATOM   7735  N  N     . ARG A 1 2292 ? 181.927 117.013 135.567 1.00 111.60 ? 2292 ARG A N     1 
ATOM   7736  C  CA    . ARG A 1 2292 ? 181.091 115.849 135.303 1.00 110.73 ? 2292 ARG A CA    1 
ATOM   7737  C  C     . ARG A 1 2292 ? 180.001 116.174 134.287 1.00 105.90 ? 2292 ARG A C     1 
ATOM   7738  O  O     . ARG A 1 2292 ? 178.850 115.758 134.428 1.00 104.34 ? 2292 ARG A O     1 
ATOM   7739  C  CB    . ARG A 1 2292 ? 180.480 115.315 136.596 1.00 114.34 ? 2292 ARG A CB    1 
ATOM   7740  C  CG    . ARG A 1 2292 ? 181.490 115.086 137.707 1.00 115.32 ? 2292 ARG A CG    1 
ATOM   7741  C  CD    . ARG A 1 2292 ? 180.811 114.580 138.971 1.00 116.54 ? 2292 ARG A CD    1 
ATOM   7742  N  NE    . ARG A 1 2292 ? 180.021 113.377 138.733 1.00 122.65 ? 2292 ARG A NE    1 
ATOM   7743  C  CZ    . ARG A 1 2292 ? 180.528 112.183 138.453 1.00 123.82 ? 2292 ARG A CZ    1 
ATOM   7744  N  NH1   . ARG A 1 2292 ? 181.834 111.982 138.386 1.00 121.22 ? 2292 ARG A NH1   1 
ATOM   7745  N  NH2   . ARG A 1 2292 ? 179.702 111.162 138.240 1.00 123.09 ? 2292 ARG A NH2   1 
ATOM   7746  N  N     . GLY A 1 2293 ? 180.359 116.921 133.246 1.00 105.03 ? 2293 GLY A N     1 
ATOM   7747  C  CA    . GLY A 1 2293 ? 179.429 117.235 132.179 1.00 104.74 ? 2293 GLY A CA    1 
ATOM   7748  C  C     . GLY A 1 2293 ? 178.249 118.085 132.602 1.00 103.10 ? 2293 GLY A C     1 
ATOM   7749  O  O     . GLY A 1 2293 ? 177.107 117.788 132.244 1.00 101.26 ? 2293 GLY A O     1 
ATOM   7750  N  N     . GLU A 1 2294 ? 178.512 119.146 133.368 1.00 101.26 ? 2294 GLU A N     1 
ATOM   7751  C  CA    . GLU A 1 2294 ? 177.435 120.029 133.805 1.00 92.74  ? 2294 GLU A CA    1 
ATOM   7752  C  C     . GLU A 1 2294 ? 176.788 120.746 132.626 1.00 89.26  ? 2294 GLU A C     1 
ATOM   7753  O  O     . GLU A 1 2294 ? 175.571 120.960 132.617 1.00 88.68  ? 2294 GLU A O     1 
ATOM   7754  C  CB    . GLU A 1 2294 ? 177.964 121.036 134.826 1.00 89.30  ? 2294 GLU A CB    1 
ATOM   7755  C  CG    . GLU A 1 2294 ? 178.755 120.409 135.962 1.00 96.89  ? 2294 GLU A CG    1 
ATOM   7756  C  CD    . GLU A 1 2294 ? 177.876 119.953 137.108 1.00 98.08  ? 2294 GLU A CD    1 
ATOM   7757  O  OE1   . GLU A 1 2294 ? 176.835 120.597 137.354 1.00 95.38  ? 2294 GLU A OE1   1 
ATOM   7758  O  OE2   . GLU A 1 2294 ? 178.226 118.950 137.765 1.00 99.44  ? 2294 GLU A OE2   1 
ATOM   7759  N  N     . LEU A 1 2295 ? 177.584 121.133 131.625 1.00 93.25  ? 2295 LEU A N     1 
ATOM   7760  C  CA    . LEU A 1 2295 ? 177.020 121.749 130.427 1.00 93.72  ? 2295 LEU A CA    1 
ATOM   7761  C  C     . LEU A 1 2295 ? 176.166 120.780 129.621 1.00 93.10  ? 2295 LEU A C     1 
ATOM   7762  O  O     . LEU A 1 2295 ? 175.353 121.224 128.805 1.00 96.13  ? 2295 LEU A O     1 
ATOM   7763  C  CB    . LEU A 1 2295 ? 178.127 122.320 129.537 1.00 95.15  ? 2295 LEU A CB    1 
ATOM   7764  C  CG    . LEU A 1 2295 ? 178.687 123.714 129.840 1.00 95.40  ? 2295 LEU A CG    1 
ATOM   7765  C  CD1   . LEU A 1 2295 ? 177.599 124.764 129.667 1.00 89.69  ? 2295 LEU A CD1   1 
ATOM   7766  C  CD2   . LEU A 1 2295 ? 179.313 123.810 131.218 1.00 87.46  ? 2295 LEU A CD2   1 
ATOM   7767  N  N     . GLN A 1 2296 ? 176.330 119.477 129.826 1.00 91.33  ? 2296 GLN A N     1 
ATOM   7768  C  CA    . GLN A 1 2296 ? 175.511 118.477 129.157 1.00 95.48  ? 2296 GLN A CA    1 
ATOM   7769  C  C     . GLN A 1 2296 ? 174.199 118.216 129.884 1.00 93.80  ? 2296 GLN A C     1 
ATOM   7770  O  O     . GLN A 1 2296 ? 173.395 117.406 129.412 1.00 95.57  ? 2296 GLN A O     1 
ATOM   7771  C  CB    . GLN A 1 2296 ? 176.292 117.166 129.013 1.00 101.57 ? 2296 GLN A CB    1 
ATOM   7772  C  CG    . GLN A 1 2296 ? 177.201 117.108 127.792 1.00 100.85 ? 2296 GLN A CG    1 
ATOM   7773  C  CD    . GLN A 1 2296 ? 178.333 118.117 127.852 1.00 103.31 ? 2296 GLN A CD    1 
ATOM   7774  O  OE1   . GLN A 1 2296 ? 179.343 117.895 128.519 1.00 99.00  ? 2296 GLN A OE1   1 
ATOM   7775  N  NE2   . GLN A 1 2296 ? 178.169 119.233 127.151 1.00 100.95 ? 2296 GLN A NE2   1 
ATOM   7776  N  N     . LYS A 1 2297 ? 173.966 118.883 131.011 1.00 90.54  ? 2297 LYS A N     1 
ATOM   7777  C  CA    . LYS A 1 2297 ? 172.772 118.696 131.818 1.00 83.05  ? 2297 LYS A CA    1 
ATOM   7778  C  C     . LYS A 1 2297 ? 172.075 120.036 131.996 1.00 77.97  ? 2297 LYS A C     1 
ATOM   7779  O  O     . LYS A 1 2297 ? 172.722 121.085 132.059 1.00 82.77  ? 2297 LYS A O     1 
ATOM   7780  C  CB    . LYS A 1 2297 ? 173.119 118.101 133.190 1.00 84.12  ? 2297 LYS A CB    1 
ATOM   7781  C  CG    . LYS A 1 2297 ? 174.095 116.936 133.131 1.00 93.40  ? 2297 LYS A CG    1 
ATOM   7782  C  CD    . LYS A 1 2297 ? 174.908 116.827 134.414 1.00 97.68  ? 2297 LYS A CD    1 
ATOM   7783  C  CE    . LYS A 1 2297 ? 174.047 116.476 135.611 1.00 95.04  ? 2297 LYS A CE    1 
ATOM   7784  N  NZ    . LYS A 1 2297 ? 173.497 115.101 135.501 1.00 90.17  ? 2297 LYS A NZ    1 
ATOM   7785  N  N     . ARG A 1 2298 ? 170.747 119.997 132.072 1.00 71.77  ? 2298 ARG A N     1 
ATOM   7786  C  CA    . ARG A 1 2298 ? 169.961 121.210 132.261 1.00 68.63  ? 2298 ARG A CA    1 
ATOM   7787  C  C     . ARG A 1 2298 ? 169.981 121.609 133.731 1.00 65.25  ? 2298 ARG A C     1 
ATOM   7788  O  O     . ARG A 1 2298 ? 169.355 120.949 134.567 1.00 66.27  ? 2298 ARG A O     1 
ATOM   7789  C  CB    . ARG A 1 2298 ? 168.528 120.999 131.780 1.00 67.83  ? 2298 ARG A CB    1 
ATOM   7790  C  CG    . ARG A 1 2298 ? 167.578 122.124 132.152 1.00 59.85  ? 2298 ARG A CG    1 
ATOM   7791  C  CD    . ARG A 1 2298 ? 166.335 122.114 131.283 1.00 57.38  ? 2298 ARG A CD    1 
ATOM   7792  N  NE    . ARG A 1 2298 ? 166.022 120.776 130.796 1.00 65.82  ? 2298 ARG A NE    1 
ATOM   7793  C  CZ    . ARG A 1 2298 ? 165.936 120.449 129.514 1.00 66.13  ? 2298 ARG A CZ    1 
ATOM   7794  N  NH1   . ARG A 1 2298 ? 166.111 121.347 128.559 1.00 59.87  ? 2298 ARG A NH1   1 
ATOM   7795  N  NH2   . ARG A 1 2298 ? 165.668 119.190 129.183 1.00 66.60  ? 2298 ARG A NH2   1 
ATOM   7796  N  N     . GLN A 1 2299 ? 170.690 122.690 134.043 1.00 61.73  ? 2299 GLN A N     1 
ATOM   7797  C  CA    . GLN A 1 2299 ? 170.854 123.165 135.411 1.00 57.35  ? 2299 GLN A CA    1 
ATOM   7798  C  C     . GLN A 1 2299 ? 169.868 124.293 135.675 1.00 59.16  ? 2299 GLN A C     1 
ATOM   7799  O  O     . GLN A 1 2299 ? 169.928 125.340 135.022 1.00 60.59  ? 2299 GLN A O     1 
ATOM   7800  C  CB    . GLN A 1 2299 ? 172.285 123.643 135.657 1.00 60.42  ? 2299 GLN A CB    1 
ATOM   7801  C  CG    . GLN A 1 2299 ? 173.363 122.660 135.239 1.00 67.71  ? 2299 GLN A CG    1 
ATOM   7802  C  CD    . GLN A 1 2299 ? 173.321 121.377 136.040 1.00 70.51  ? 2299 GLN A CD    1 
ATOM   7803  O  OE1   . GLN A 1 2299 ? 173.207 120.288 135.484 1.00 77.78  ? 2299 GLN A OE1   1 
ATOM   7804  N  NE2   . GLN A 1 2299 ? 173.411 121.501 137.357 1.00 63.64  ? 2299 GLN A NE2   1 
ATOM   7805  N  N     . TRP A 1 2300 ? 168.971 124.080 136.634 1.00 57.41  ? 2300 TRP A N     1 
ATOM   7806  C  CA    . TRP A 1 2300 ? 168.020 125.094 137.069 1.00 50.27  ? 2300 TRP A CA    1 
ATOM   7807  C  C     . TRP A 1 2300 ? 168.369 125.488 138.495 1.00 50.15  ? 2300 TRP A C     1 
ATOM   7808  O  O     . TRP A 1 2300 ? 168.379 124.638 139.389 1.00 62.83  ? 2300 TRP A O     1 
ATOM   7809  C  CB    . TRP A 1 2300 ? 166.582 124.577 136.993 1.00 47.12  ? 2300 TRP A CB    1 
ATOM   7810  C  CG    . TRP A 1 2300 ? 166.022 124.551 135.609 1.00 50.17  ? 2300 TRP A CG    1 
ATOM   7811  C  CD1   . TRP A 1 2300 ? 166.670 124.882 134.459 1.00 52.06  ? 2300 TRP A CD1   1 
ATOM   7812  C  CD2   . TRP A 1 2300 ? 164.694 124.176 135.228 1.00 51.03  ? 2300 TRP A CD2   1 
ATOM   7813  N  NE1   . TRP A 1 2300 ? 165.830 124.737 133.383 1.00 53.49  ? 2300 TRP A NE1   1 
ATOM   7814  C  CE2   . TRP A 1 2300 ? 164.610 124.304 133.830 1.00 53.50  ? 2300 TRP A CE2   1 
ATOM   7815  C  CE3   . TRP A 1 2300 ? 163.569 123.744 135.934 1.00 50.49  ? 2300 TRP A CE3   1 
ATOM   7816  C  CZ2   . TRP A 1 2300 ? 163.446 124.015 133.124 1.00 55.15  ? 2300 TRP A CZ2   1 
ATOM   7817  C  CZ3   . TRP A 1 2300 ? 162.416 123.458 135.232 1.00 48.26  ? 2300 TRP A CZ3   1 
ATOM   7818  C  CH2   . TRP A 1 2300 ? 162.363 123.595 133.842 1.00 51.01  ? 2300 TRP A CH2   1 
ATOM   7819  N  N     . ILE A 1 2301 ? 168.654 126.767 138.706 1.00 43.50  ? 2301 ILE A N     1 
ATOM   7820  C  CA    . ILE A 1 2301 ? 168.989 127.282 140.030 1.00 46.04  ? 2301 ILE A CA    1 
ATOM   7821  C  C     . ILE A 1 2301 ? 167.720 127.939 140.560 1.00 47.69  ? 2301 ILE A C     1 
ATOM   7822  O  O     . ILE A 1 2301 ? 167.444 129.108 140.297 1.00 57.81  ? 2301 ILE A O     1 
ATOM   7823  C  CB    . ILE A 1 2301 ? 170.172 128.245 139.990 1.00 50.69  ? 2301 ILE A CB    1 
ATOM   7824  C  CG1   . ILE A 1 2301 ? 171.371 127.582 139.312 1.00 52.10  ? 2301 ILE A CG1   1 
ATOM   7825  C  CG2   . ILE A 1 2301 ? 170.534 128.700 141.394 1.00 49.29  ? 2301 ILE A CG2   1 
ATOM   7826  C  CD1   . ILE A 1 2301 ? 172.628 128.416 139.346 1.00 51.13  ? 2301 ILE A CD1   1 
ATOM   7827  N  N     . VAL A 1 2302 ? 166.930 127.167 141.297 1.00 43.06  ? 2302 VAL A N     1 
ATOM   7828  C  CA    . VAL A 1 2302 ? 165.708 127.673 141.911 1.00 43.50  ? 2302 VAL A CA    1 
ATOM   7829  C  C     . VAL A 1 2302 ? 166.060 128.283 143.259 1.00 43.89  ? 2302 VAL A C     1 
ATOM   7830  O  O     . VAL A 1 2302 ? 166.951 127.794 143.961 1.00 53.00  ? 2302 VAL A O     1 
ATOM   7831  C  CB    . VAL A 1 2302 ? 164.670 126.546 142.050 1.00 42.98  ? 2302 VAL A CB    1 
ATOM   7832  C  CG1   . VAL A 1 2302 ? 163.407 127.052 142.725 1.00 39.62  ? 2302 VAL A CG1   1 
ATOM   7833  C  CG2   . VAL A 1 2302 ? 164.350 125.949 140.694 1.00 42.99  ? 2302 VAL A CG2   1 
ATOM   7834  N  N     . PHE A 1 2303 ? 165.378 129.362 143.626 1.00 38.86  ? 2303 PHE A N     1 
ATOM   7835  C  CA    . PHE A 1 2303 ? 165.701 130.068 144.859 1.00 47.37  ? 2303 PHE A CA    1 
ATOM   7836  C  C     . PHE A 1 2303 ? 164.703 129.838 145.982 1.00 54.80  ? 2303 PHE A C     1 
ATOM   7837  O  O     . PHE A 1 2303 ? 165.115 129.693 147.133 1.00 65.58  ? 2303 PHE A O     1 
ATOM   7838  C  CB    . PHE A 1 2303 ? 165.846 131.565 144.579 1.00 46.56  ? 2303 PHE A CB    1 
ATOM   7839  C  CG    . PHE A 1 2303 ? 167.237 131.956 144.167 1.00 55.16  ? 2303 PHE A CG    1 
ATOM   7840  C  CD1   . PHE A 1 2303 ? 168.216 132.187 145.116 1.00 56.23  ? 2303 PHE A CD1   1 
ATOM   7841  C  CD2   . PHE A 1 2303 ? 167.579 132.035 142.831 1.00 52.29  ? 2303 PHE A CD2   1 
ATOM   7842  C  CE1   . PHE A 1 2303 ? 169.497 132.530 144.737 1.00 53.57  ? 2303 PHE A CE1   1 
ATOM   7843  C  CE2   . PHE A 1 2303 ? 168.857 132.378 142.448 1.00 46.67  ? 2303 PHE A CE2   1 
ATOM   7844  C  CZ    . PHE A 1 2303 ? 169.817 132.624 143.402 1.00 48.24  ? 2303 PHE A CZ    1 
ATOM   7845  N  N     . ASP A 1 2304 ? 163.405 129.786 145.687 1.00 44.12  ? 2304 ASP A N     1 
ATOM   7846  C  CA    . ASP A 1 2304 ? 162.397 129.349 146.656 1.00 40.26  ? 2304 ASP A CA    1 
ATOM   7847  C  C     . ASP A 1 2304 ? 162.468 130.158 147.951 1.00 43.18  ? 2304 ASP A C     1 
ATOM   7848  O  O     . ASP A 1 2304 ? 162.481 129.613 149.055 1.00 50.56  ? 2304 ASP A O     1 
ATOM   7849  C  CB    . ASP A 1 2304 ? 162.541 127.854 146.942 1.00 43.89  ? 2304 ASP A CB    1 
ATOM   7850  C  CG    . ASP A 1 2304 ? 161.232 127.204 147.336 1.00 51.89  ? 2304 ASP A CG    1 
ATOM   7851  O  OD1   . ASP A 1 2304 ? 160.604 127.662 148.312 1.00 52.16  ? 2304 ASP A OD1   1 
ATOM   7852  O  OD2   . ASP A 1 2304 ? 160.832 126.227 146.670 1.00 54.10  ? 2304 ASP A OD2   1 
ATOM   7853  N  N     . GLY A 1 2305 ? 162.526 131.477 147.807 1.00 45.04  ? 2305 GLY A N     1 
ATOM   7854  C  CA    . GLY A 1 2305 ? 162.577 132.342 148.971 1.00 50.45  ? 2305 GLY A CA    1 
ATOM   7855  C  C     . GLY A 1 2305 ? 162.191 133.754 148.599 1.00 61.32  ? 2305 GLY A C     1 
ATOM   7856  O  O     . GLY A 1 2305 ? 162.126 134.113 147.422 1.00 68.68  ? 2305 GLY A O     1 
ATOM   7857  N  N     . ASP A 1 2306 ? 161.943 134.558 149.629 1.00 57.44  ? 2306 ASP A N     1 
ATOM   7858  C  CA    . ASP A 1 2306 ? 161.501 135.929 149.419 1.00 61.61  ? 2306 ASP A CA    1 
ATOM   7859  C  C     . ASP A 1 2306 ? 162.565 136.734 148.684 1.00 64.31  ? 2306 ASP A C     1 
ATOM   7860  O  O     . ASP A 1 2306 ? 163.765 136.569 148.916 1.00 67.11  ? 2306 ASP A O     1 
ATOM   7861  C  CB    . ASP A 1 2306 ? 161.175 136.591 150.757 1.00 68.24  ? 2306 ASP A CB    1 
ATOM   7862  C  CG    . ASP A 1 2306 ? 159.943 136.004 151.413 1.00 75.78  ? 2306 ASP A CG    1 
ATOM   7863  O  OD1   . ASP A 1 2306 ? 159.049 135.529 150.683 1.00 75.97  ? 2306 ASP A OD1   1 
ATOM   7864  O  OD2   . ASP A 1 2306 ? 159.869 136.020 152.660 1.00 73.49  ? 2306 ASP A OD2   1 
ATOM   7865  N  N     . VAL A 1 2307 ? 162.115 137.611 147.790 1.00 67.86  ? 2307 VAL A N     1 
ATOM   7866  C  CA    . VAL A 1 2307 ? 162.995 138.456 146.991 1.00 69.32  ? 2307 VAL A CA    1 
ATOM   7867  C  C     . VAL A 1 2307 ? 163.002 139.853 147.591 1.00 75.27  ? 2307 VAL A C     1 
ATOM   7868  O  O     . VAL A 1 2307 ? 161.940 140.452 147.800 1.00 79.72  ? 2307 VAL A O     1 
ATOM   7869  C  CB    . VAL A 1 2307 ? 162.548 138.490 145.519 1.00 61.92  ? 2307 VAL A CB    1 
ATOM   7870  C  CG1   . VAL A 1 2307 ? 163.116 139.710 144.819 1.00 67.90  ? 2307 VAL A CG1   1 
ATOM   7871  C  CG2   . VAL A 1 2307 ? 162.985 137.228 144.806 1.00 61.43  ? 2307 VAL A CG2   1 
ATOM   7872  N  N     . ASP A 1 2308 ? 164.190 140.370 147.869 1.00 72.32  ? 2308 ASP A N     1 
ATOM   7873  C  CA    . ASP A 1 2308 ? 164.382 141.701 148.420 1.00 76.19  ? 2308 ASP A CA    1 
ATOM   7874  C  C     . ASP A 1 2308 ? 165.478 142.417 147.651 1.00 80.46  ? 2308 ASP A C     1 
ATOM   7875  O  O     . ASP A 1 2308 ? 166.312 141.777 147.004 1.00 80.33  ? 2308 ASP A O     1 
ATOM   7876  C  CB    . ASP A 1 2308 ? 164.753 141.646 149.908 1.00 78.14  ? 2308 ASP A CB    1 
ATOM   7877  C  CG    . ASP A 1 2308 ? 163.613 141.174 150.767 1.00 86.95  ? 2308 ASP A CG    1 
ATOM   7878  O  OD1   . ASP A 1 2308 ? 162.447 141.395 150.381 1.00 85.91  ? 2308 ASP A OD1   1 
ATOM   7879  O  OD2   . ASP A 1 2308 ? 163.878 140.632 151.856 1.00 95.33  ? 2308 ASP A OD2   1 
ATOM   7880  N  N     . PRO A 1 2309 ? 165.509 143.754 147.703 1.00 82.14  ? 2309 PRO A N     1 
ATOM   7881  C  CA    . PRO A 1 2309 ? 166.593 144.479 147.032 1.00 83.80  ? 2309 PRO A CA    1 
ATOM   7882  C  C     . PRO A 1 2309 ? 167.888 144.470 147.823 1.00 84.58  ? 2309 PRO A C     1 
ATOM   7883  O  O     . PRO A 1 2309 ? 168.554 145.504 147.940 1.00 85.67  ? 2309 PRO A O     1 
ATOM   7884  C  CB    . PRO A 1 2309 ? 166.032 145.899 146.917 1.00 82.59  ? 2309 PRO A CB    1 
ATOM   7885  C  CG    . PRO A 1 2309 ? 165.129 146.025 148.084 1.00 79.38  ? 2309 PRO A CG    1 
ATOM   7886  C  CD    . PRO A 1 2309 ? 164.505 144.672 148.272 1.00 78.16  ? 2309 PRO A CD    1 
ATOM   7887  N  N     . GLU A 1 2310 ? 168.258 143.325 148.365 1.00 82.48  ? 2310 GLU A N     1 
ATOM   7888  C  CA    . GLU A 1 2310 ? 169.549 143.210 149.027 1.00 78.70  ? 2310 GLU A CA    1 
ATOM   7889  C  C     . GLU A 1 2310 ? 170.369 142.038 148.516 1.00 76.76  ? 2310 GLU A C     1 
ATOM   7890  O  O     . GLU A 1 2310 ? 171.570 142.192 148.286 1.00 81.15  ? 2310 GLU A O     1 
ATOM   7891  C  CB    . GLU A 1 2310 ? 169.351 143.086 150.545 1.00 79.46  ? 2310 GLU A CB    1 
ATOM   7892  C  CG    . GLU A 1 2310 ? 168.762 144.328 151.193 1.00 88.21  ? 2310 GLU A CG    1 
ATOM   7893  C  CD    . GLU A 1 2310 ? 169.695 145.522 151.138 1.00 96.18  ? 2310 GLU A CD    1 
ATOM   7894  O  OE1   . GLU A 1 2310 ? 170.926 145.320 151.177 1.00 99.45  ? 2310 GLU A OE1   1 
ATOM   7895  O  OE2   . GLU A 1 2310 ? 169.194 146.663 151.051 1.00 93.20  ? 2310 GLU A OE2   1 
ATOM   7896  N  N     . TRP A 1 2311 ? 169.747 140.882 148.304 1.00 69.25  ? 2311 TRP A N     1 
ATOM   7897  C  CA    . TRP A 1 2311 ? 170.451 139.702 147.825 1.00 65.33  ? 2311 TRP A CA    1 
ATOM   7898  C  C     . TRP A 1 2311 ? 170.328 139.505 146.321 1.00 72.33  ? 2311 TRP A C     1 
ATOM   7899  O  O     . TRP A 1 2311 ? 170.919 138.564 145.785 1.00 78.78  ? 2311 TRP A O     1 
ATOM   7900  C  CB    . TRP A 1 2311 ? 169.951 138.453 148.563 1.00 62.07  ? 2311 TRP A CB    1 
ATOM   7901  C  CG    . TRP A 1 2311 ? 168.549 138.047 148.221 1.00 63.37  ? 2311 TRP A CG    1 
ATOM   7902  C  CD1   . TRP A 1 2311 ? 167.409 138.435 148.859 1.00 62.64  ? 2311 TRP A CD1   1 
ATOM   7903  C  CD2   . TRP A 1 2311 ? 168.140 137.157 147.175 1.00 59.33  ? 2311 TRP A CD2   1 
ATOM   7904  N  NE1   . TRP A 1 2311 ? 166.315 137.853 148.270 1.00 61.65  ? 2311 TRP A NE1   1 
ATOM   7905  C  CE2   . TRP A 1 2311 ? 166.737 137.064 147.233 1.00 58.53  ? 2311 TRP A CE2   1 
ATOM   7906  C  CE3   . TRP A 1 2311 ? 168.822 136.436 146.192 1.00 56.52  ? 2311 TRP A CE3   1 
ATOM   7907  C  CZ2   . TRP A 1 2311 ? 166.005 136.280 146.347 1.00 58.74  ? 2311 TRP A CZ2   1 
ATOM   7908  C  CZ3   . TRP A 1 2311 ? 168.094 135.660 145.314 1.00 56.25  ? 2311 TRP A CZ3   1 
ATOM   7909  C  CH2   . TRP A 1 2311 ? 166.700 135.586 145.398 1.00 56.71  ? 2311 TRP A CH2   1 
ATOM   7910  N  N     . VAL A 1 2312 ? 169.592 140.373 145.625 1.00 71.16  ? 2312 VAL A N     1 
ATOM   7911  C  CA    . VAL A 1 2312 ? 169.464 140.282 144.176 1.00 70.21  ? 2312 VAL A CA    1 
ATOM   7912  C  C     . VAL A 1 2312 ? 170.285 141.338 143.455 1.00 78.84  ? 2312 VAL A C     1 
ATOM   7913  O  O     . VAL A 1 2312 ? 170.280 141.374 142.217 1.00 82.37  ? 2312 VAL A O     1 
ATOM   7914  C  CB    . VAL A 1 2312 ? 167.989 140.376 143.741 1.00 69.75  ? 2312 VAL A CB    1 
ATOM   7915  C  CG1   . VAL A 1 2312 ? 167.163 139.309 144.433 1.00 65.83  ? 2312 VAL A CG1   1 
ATOM   7916  C  CG2   . VAL A 1 2312 ? 167.440 141.760 144.034 1.00 78.75  ? 2312 VAL A CG2   1 
ATOM   7917  N  N     . GLU A 1 2313 ? 170.985 142.206 144.190 1.00 81.23  ? 2313 GLU A N     1 
ATOM   7918  C  CA    . GLU A 1 2313 ? 171.791 143.240 143.547 1.00 81.42  ? 2313 GLU A CA    1 
ATOM   7919  C  C     . GLU A 1 2313 ? 172.903 142.630 142.706 1.00 83.64  ? 2313 GLU A C     1 
ATOM   7920  O  O     . GLU A 1 2313 ? 173.144 143.064 141.573 1.00 86.00  ? 2313 GLU A O     1 
ATOM   7921  C  CB    . GLU A 1 2313 ? 172.371 144.183 144.599 1.00 77.98  ? 2313 GLU A CB    1 
ATOM   7922  C  CG    . GLU A 1 2313 ? 171.327 144.829 145.490 1.00 83.17  ? 2313 GLU A CG    1 
ATOM   7923  C  CD    . GLU A 1 2313 ? 170.164 145.397 144.703 1.00 95.77  ? 2313 GLU A CD    1 
ATOM   7924  O  OE1   . GLU A 1 2313 ? 170.383 146.342 143.916 1.00 98.23  ? 2313 GLU A OE1   1 
ATOM   7925  O  OE2   . GLU A 1 2313 ? 169.031 144.897 144.868 1.00 95.95  ? 2313 GLU A OE2   1 
ATOM   7926  N  N     . ASN A 1 2314 ? 173.594 141.622 143.241 1.00 78.26  ? 2314 ASN A N     1 
ATOM   7927  C  CA    . ASN A 1 2314 ? 174.632 140.951 142.467 1.00 80.73  ? 2314 ASN A CA    1 
ATOM   7928  C  C     . ASN A 1 2314 ? 174.035 140.086 141.366 1.00 83.08  ? 2314 ASN A C     1 
ATOM   7929  O  O     . ASN A 1 2314 ? 174.716 139.782 140.381 1.00 87.06  ? 2314 ASN A O     1 
ATOM   7930  C  CB    . ASN A 1 2314 ? 175.513 140.108 143.387 1.00 78.59  ? 2314 ASN A CB    1 
ATOM   7931  C  CG    . ASN A 1 2314 ? 176.336 140.951 144.336 1.00 84.79  ? 2314 ASN A CG    1 
ATOM   7932  O  OD1   . ASN A 1 2314 ? 177.494 141.264 144.061 1.00 90.91  ? 2314 ASN A OD1   1 
ATOM   7933  N  ND2   . ASN A 1 2314 ? 175.742 141.327 145.462 1.00 83.44  ? 2314 ASN A ND2   1 
ATOM   7934  N  N     . LEU A 1 2315 ? 172.775 139.680 141.515 1.00 79.70  ? 2315 LEU A N     1 
ATOM   7935  C  CA    . LEU A 1 2315 ? 172.101 138.882 140.501 1.00 76.70  ? 2315 LEU A CA    1 
ATOM   7936  C  C     . LEU A 1 2315 ? 171.541 139.716 139.359 1.00 75.38  ? 2315 LEU A C     1 
ATOM   7937  O  O     . LEU A 1 2315 ? 171.103 139.141 138.359 1.00 78.58  ? 2315 LEU A O     1 
ATOM   7938  C  CB    . LEU A 1 2315 ? 170.966 138.072 141.133 1.00 73.67  ? 2315 LEU A CB    1 
ATOM   7939  C  CG    . LEU A 1 2315 ? 171.237 136.597 141.426 1.00 65.90  ? 2315 LEU A CG    1 
ATOM   7940  C  CD1   . LEU A 1 2315 ? 170.012 135.953 142.044 1.00 66.21  ? 2315 LEU A CD1   1 
ATOM   7941  C  CD2   . LEU A 1 2315 ? 171.642 135.869 140.161 1.00 65.95  ? 2315 LEU A CD2   1 
ATOM   7942  N  N     . ASN A 1 2316 ? 171.532 141.045 139.482 1.00 75.18  ? 2316 ASN A N     1 
ATOM   7943  C  CA    . ASN A 1 2316 ? 170.937 141.877 138.441 1.00 79.86  ? 2316 ASN A CA    1 
ATOM   7944  C  C     . ASN A 1 2316 ? 171.703 141.760 137.130 1.00 84.60  ? 2316 ASN A C     1 
ATOM   7945  O  O     . ASN A 1 2316 ? 171.100 141.723 136.051 1.00 85.63  ? 2316 ASN A O     1 
ATOM   7946  C  CB    . ASN A 1 2316 ? 170.874 143.331 138.902 1.00 80.41  ? 2316 ASN A CB    1 
ATOM   7947  C  CG    . ASN A 1 2316 ? 169.675 143.608 139.787 1.00 82.01  ? 2316 ASN A CG    1 
ATOM   7948  O  OD1   . ASN A 1 2316 ? 168.836 142.735 140.002 1.00 82.17  ? 2316 ASN A OD1   1 
ATOM   7949  N  ND2   . ASN A 1 2316 ? 169.589 144.827 140.302 1.00 79.91  ? 2316 ASN A ND2   1 
ATOM   7950  N  N     . SER A 1 2317 ? 173.034 141.705 137.199 1.00 81.50  ? 2317 SER A N     1 
ATOM   7951  C  CA    . SER A 1 2317 ? 173.824 141.540 135.984 1.00 78.37  ? 2317 SER A CA    1 
ATOM   7952  C  C     . SER A 1 2317 ? 173.676 140.139 135.404 1.00 76.55  ? 2317 SER A C     1 
ATOM   7953  O  O     . SER A 1 2317 ? 173.815 139.956 134.190 1.00 78.96  ? 2317 SER A O     1 
ATOM   7954  C  CB    . SER A 1 2317 ? 175.293 141.852 136.266 1.00 88.48  ? 2317 SER A CB    1 
ATOM   7955  O  OG    . SER A 1 2317 ? 175.792 141.050 137.322 1.00 90.49  ? 2317 SER A OG    1 
ATOM   7956  N  N     . VAL A 1 2318 ? 173.412 139.141 136.250 1.00 76.22  ? 2318 VAL A N     1 
ATOM   7957  C  CA    . VAL A 1 2318 ? 173.175 137.788 135.755 1.00 77.20  ? 2318 VAL A CA    1 
ATOM   7958  C  C     . VAL A 1 2318 ? 171.835 137.709 135.036 1.00 76.14  ? 2318 VAL A C     1 
ATOM   7959  O  O     . VAL A 1 2318 ? 171.716 137.079 133.979 1.00 76.34  ? 2318 VAL A O     1 
ATOM   7960  C  CB    . VAL A 1 2318 ? 173.251 136.777 136.913 1.00 70.77  ? 2318 VAL A CB    1 
ATOM   7961  C  CG1   . VAL A 1 2318 ? 173.212 135.356 136.380 1.00 64.90  ? 2318 VAL A CG1   1 
ATOM   7962  C  CG2   . VAL A 1 2318 ? 174.500 137.008 137.737 1.00 75.53  ? 2318 VAL A CG2   1 
ATOM   7963  N  N     . LEU A 1 2319 ? 170.806 138.341 135.600 1.00 76.21  ? 2319 LEU A N     1 
ATOM   7964  C  CA    . LEU A 1 2319 ? 169.478 138.296 135.000 1.00 73.98  ? 2319 LEU A CA    1 
ATOM   7965  C  C     . LEU A 1 2319 ? 169.393 139.170 133.758 1.00 79.09  ? 2319 LEU A C     1 
ATOM   7966  O  O     . LEU A 1 2319 ? 168.575 138.906 132.870 1.00 81.65  ? 2319 LEU A O     1 
ATOM   7967  C  CB    . LEU A 1 2319 ? 168.431 138.724 136.027 1.00 69.49  ? 2319 LEU A CB    1 
ATOM   7968  C  CG    . LEU A 1 2319 ? 168.392 137.892 137.309 1.00 67.86  ? 2319 LEU A CG    1 
ATOM   7969  C  CD1   . LEU A 1 2319 ? 167.531 138.563 138.364 1.00 70.64  ? 2319 LEU A CD1   1 
ATOM   7970  C  CD2   . LEU A 1 2319 ? 167.893 136.489 137.017 1.00 64.20  ? 2319 LEU A CD2   1 
ATOM   7971  N  N     . ASP A 1 2320 ? 170.224 140.205 133.676 1.00 83.01  ? 2320 ASP A N     1 
ATOM   7972  C  CA    . ASP A 1 2320 ? 170.233 141.091 132.524 1.00 86.00  ? 2320 ASP A CA    1 
ATOM   7973  C  C     . ASP A 1 2320 ? 170.761 140.343 131.299 1.00 86.83  ? 2320 ASP A C     1 
ATOM   7974  O  O     . ASP A 1 2320 ? 171.157 139.176 131.367 1.00 84.96  ? 2320 ASP A O     1 
ATOM   7975  C  CB    . ASP A 1 2320 ? 171.072 142.332 132.831 1.00 88.43  ? 2320 ASP A CB    1 
ATOM   7976  C  CG    . ASP A 1 2320 ? 170.774 143.495 131.901 1.00 96.42  ? 2320 ASP A CG    1 
ATOM   7977  O  OD1   . ASP A 1 2320 ? 170.551 143.264 130.694 1.00 101.98 ? 2320 ASP A OD1   1 
ATOM   7978  O  OD2   . ASP A 1 2320 ? 170.768 144.648 132.381 1.00 96.74  ? 2320 ASP A OD2   1 
ATOM   7979  N  N     . ASP A 1 2321 ? 170.768 141.029 130.156 1.00 91.01  ? 2321 ASP A N     1 
ATOM   7980  C  CA    . ASP A 1 2321 ? 171.285 140.437 128.930 1.00 95.55  ? 2321 ASP A CA    1 
ATOM   7981  C  C     . ASP A 1 2321 ? 172.781 140.166 128.997 1.00 96.39  ? 2321 ASP A C     1 
ATOM   7982  O  O     . ASP A 1 2321 ? 173.300 139.436 128.145 1.00 95.66  ? 2321 ASP A O     1 
ATOM   7983  C  CB    . ASP A 1 2321 ? 170.975 141.345 127.739 1.00 104.03 ? 2321 ASP A CB    1 
ATOM   7984  C  CG    . ASP A 1 2321 ? 170.885 140.583 126.432 1.00 113.25 ? 2321 ASP A CG    1 
ATOM   7985  O  OD1   . ASP A 1 2321 ? 170.999 139.339 126.459 1.00 112.49 ? 2321 ASP A OD1   1 
ATOM   7986  O  OD2   . ASP A 1 2321 ? 170.698 141.227 125.378 1.00 116.21 ? 2321 ASP A OD2   1 
ATOM   7987  N  N     . ASN A 1 2322 ? 173.482 140.737 129.980 1.00 96.00  ? 2322 ASN A N     1 
ATOM   7988  C  CA    . ASN A 1 2322 ? 174.905 140.456 130.141 1.00 90.76  ? 2322 ASN A CA    1 
ATOM   7989  C  C     . ASN A 1 2322 ? 175.142 138.990 130.481 1.00 88.28  ? 2322 ASN A C     1 
ATOM   7990  O  O     . ASN A 1 2322 ? 176.099 138.380 129.990 1.00 88.98  ? 2322 ASN A O     1 
ATOM   7991  C  CB    . ASN A 1 2322 ? 175.498 141.355 131.224 1.00 87.44  ? 2322 ASN A CB    1 
ATOM   7992  C  CG    . ASN A 1 2322 ? 175.434 142.823 130.862 1.00 95.39  ? 2322 ASN A CG    1 
ATOM   7993  O  OD1   . ASN A 1 2322 ? 174.738 143.604 131.510 1.00 94.10  ? 2322 ASN A OD1   1 
ATOM   7994  N  ND2   . ASN A 1 2322 ? 176.162 143.207 129.820 1.00 100.53 ? 2322 ASN A ND2   1 
ATOM   7995  N  N     . LYS A 1 2323 ? 174.277 138.411 131.318 1.00 84.05  ? 2323 LYS A N     1 
ATOM   7996  C  CA    . LYS A 1 2323 ? 174.429 137.035 131.793 1.00 82.75  ? 2323 LYS A CA    1 
ATOM   7997  C  C     . LYS A 1 2323 ? 175.795 136.827 132.442 1.00 87.59  ? 2323 LYS A C     1 
ATOM   7998  O  O     . LYS A 1 2323 ? 176.486 135.842 132.180 1.00 89.14  ? 2323 LYS A O     1 
ATOM   7999  C  CB    . LYS A 1 2323 ? 174.202 136.026 130.665 1.00 80.66  ? 2323 LYS A CB    1 
ATOM   8000  C  CG    . LYS A 1 2323 ? 172.858 136.161 129.977 1.00 82.91  ? 2323 LYS A CG    1 
ATOM   8001  C  CD    . LYS A 1 2323 ? 172.488 134.892 129.227 1.00 77.72  ? 2323 LYS A CD    1 
ATOM   8002  C  CE    . LYS A 1 2323 ? 173.610 134.445 128.311 1.00 82.32  ? 2323 LYS A CE    1 
ATOM   8003  N  NZ    . LYS A 1 2323 ? 173.281 133.167 127.623 1.00 98.54  ? 2323 LYS A NZ    1 
ATOM   8004  N  N     . LEU A 1 2324 ? 176.189 137.771 133.292 1.00 84.80  ? 2324 LEU A N     1 
ATOM   8005  C  CA    . LEU A 1 2324 ? 177.501 137.760 133.919 1.00 87.25  ? 2324 LEU A CA    1 
ATOM   8006  C  C     . LEU A 1 2324 ? 177.369 138.103 135.395 1.00 87.81  ? 2324 LEU A C     1 
ATOM   8007  O  O     . LEU A 1 2324 ? 176.594 138.987 135.768 1.00 92.09  ? 2324 LEU A O     1 
ATOM   8008  C  CB    . LEU A 1 2324 ? 178.442 138.754 133.231 1.00 90.67  ? 2324 LEU A CB    1 
ATOM   8009  C  CG    . LEU A 1 2324 ? 179.881 138.820 133.734 1.00 90.63  ? 2324 LEU A CG    1 
ATOM   8010  C  CD1   . LEU A 1 2324 ? 180.727 137.774 133.033 1.00 87.38  ? 2324 LEU A CD1   1 
ATOM   8011  C  CD2   . LEU A 1 2324 ? 180.450 140.210 133.521 1.00 89.88  ? 2324 LEU A CD2   1 
ATOM   8012  N  N     . LEU A 1 2325 ? 178.129 137.399 136.228 1.00 85.80  ? 2325 LEU A N     1 
ATOM   8013  C  CA    . LEU A 1 2325 ? 178.187 137.653 137.660 1.00 88.81  ? 2325 LEU A CA    1 
ATOM   8014  C  C     . LEU A 1 2325 ? 179.530 138.295 137.985 1.00 90.10  ? 2325 LEU A C     1 
ATOM   8015  O  O     . LEU A 1 2325 ? 180.584 137.724 137.684 1.00 88.89  ? 2325 LEU A O     1 
ATOM   8016  C  CB    . LEU A 1 2325 ? 178.001 136.358 138.450 1.00 87.03  ? 2325 LEU A CB    1 
ATOM   8017  C  CG    . LEU A 1 2325 ? 178.068 136.439 139.976 1.00 80.92  ? 2325 LEU A CG    1 
ATOM   8018  C  CD1   . LEU A 1 2325 ? 176.917 137.261 140.526 1.00 78.41  ? 2325 LEU A CD1   1 
ATOM   8019  C  CD2   . LEU A 1 2325 ? 178.065 135.046 140.581 1.00 71.78  ? 2325 LEU A CD2   1 
ATOM   8020  N  N     . THR A 1 2326 ? 179.487 139.479 138.588 1.00 94.30  ? 2326 THR A N     1 
ATOM   8021  C  CA    . THR A 1 2326 ? 180.686 140.211 138.972 1.00 96.66  ? 2326 THR A CA    1 
ATOM   8022  C  C     . THR A 1 2326 ? 180.907 140.035 140.469 1.00 99.11  ? 2326 THR A C     1 
ATOM   8023  O  O     . THR A 1 2326 ? 180.013 140.324 141.272 1.00 97.66  ? 2326 THR A O     1 
ATOM   8024  C  CB    . THR A 1 2326 ? 180.565 141.692 138.614 1.00 99.95  ? 2326 THR A CB    1 
ATOM   8025  O  OG1   . THR A 1 2326 ? 180.726 141.857 137.200 1.00 96.70  ? 2326 THR A OG1   1 
ATOM   8026  C  CG2   . THR A 1 2326 ? 181.628 142.506 139.336 1.00 100.23 ? 2326 THR A CG2   1 
ATOM   8027  N  N     . LEU A 1 2327 ? 182.076 139.569 140.832 1.00 97.61  ? 2327 LEU A N     1 
ATOM   8028  C  CA    . LEU A 1 2327 ? 182.432 139.259 142.203 1.00 94.02  ? 2327 LEU A CA    1 
ATOM   8029  C  C     . LEU A 1 2327 ? 183.285 140.370 142.804 1.00 101.60 ? 2327 LEU A C     1 
ATOM   8030  O  O     . LEU A 1 2327 ? 184.002 141.069 142.082 1.00 102.85 ? 2327 LEU A O     1 
ATOM   8031  C  CB    . LEU A 1 2327 ? 183.203 137.937 142.262 1.00 92.35  ? 2327 LEU A CB    1 
ATOM   8032  C  CG    . LEU A 1 2327 ? 182.370 136.677 142.032 1.00 89.15  ? 2327 LEU A CG    1 
ATOM   8033  C  CD1   . LEU A 1 2327 ? 183.245 135.437 142.082 1.00 92.71  ? 2327 LEU A CD1   1 
ATOM   8034  C  CD2   . LEU A 1 2327 ? 181.256 136.591 143.057 1.00 85.93  ? 2327 LEU A CD2   1 
ATOM   8035  N  N     . PRO A 1 2328 ? 183.223 140.565 144.124 1.00 105.55 ? 2328 PRO A N     1 
ATOM   8036  C  CA    . PRO A 1 2328 ? 184.132 141.532 144.761 1.00 105.58 ? 2328 PRO A CA    1 
ATOM   8037  C  C     . PRO A 1 2328 ? 185.596 141.175 144.589 1.00 103.41 ? 2328 PRO A C     1 
ATOM   8038  O  O     . PRO A 1 2328 ? 186.452 142.063 144.683 1.00 98.78  ? 2328 PRO A O     1 
ATOM   8039  C  CB    . PRO A 1 2328 ? 183.710 141.499 146.237 1.00 99.76  ? 2328 PRO A CB    1 
ATOM   8040  C  CG    . PRO A 1 2328 ? 182.967 140.214 146.403 1.00 96.58  ? 2328 PRO A CG    1 
ATOM   8041  C  CD    . PRO A 1 2328 ? 182.298 139.953 145.091 1.00 100.33 ? 2328 PRO A CD    1 
ATOM   8042  N  N     . ASN A 1 2329 ? 185.909 139.900 144.349 1.00 105.44 ? 2329 ASN A N     1 
ATOM   8043  C  CA    . ASN A 1 2329 ? 187.268 139.521 143.981 1.00 104.44 ? 2329 ASN A CA    1 
ATOM   8044  C  C     . ASN A 1 2329 ? 187.683 140.200 142.683 1.00 106.11 ? 2329 ASN A C     1 
ATOM   8045  O  O     . ASN A 1 2329 ? 188.807 140.702 142.565 1.00 111.15 ? 2329 ASN A O     1 
ATOM   8046  C  CB    . ASN A 1 2329 ? 187.357 137.997 143.849 1.00 102.79 ? 2329 ASN A CB    1 
ATOM   8047  C  CG    . ASN A 1 2329 ? 188.784 137.493 143.677 1.00 109.15 ? 2329 ASN A CG    1 
ATOM   8048  O  OD1   . ASN A 1 2329 ? 189.596 138.092 142.973 1.00 114.73 ? 2329 ASN A OD1   1 
ATOM   8049  N  ND2   . ASN A 1 2329 ? 189.087 136.372 144.317 1.00 105.81 ? 2329 ASN A ND2   1 
ATOM   8050  N  N     . GLY A 1 2330 ? 186.784 140.238 141.706 1.00 104.16 ? 2330 GLY A N     1 
ATOM   8051  C  CA    . GLY A 1 2330 ? 187.082 140.743 140.379 1.00 104.90 ? 2330 GLY A CA    1 
ATOM   8052  C  C     . GLY A 1 2330 ? 186.812 139.756 139.268 1.00 101.78 ? 2330 GLY A C     1 
ATOM   8053  O  O     . GLY A 1 2330 ? 186.851 140.144 138.091 1.00 99.45  ? 2330 GLY A O     1 
ATOM   8054  N  N     . GLU A 1 2331 ? 186.543 138.494 139.589 1.00 102.60 ? 2331 GLU A N     1 
ATOM   8055  C  CA    . GLU A 1 2331 ? 186.219 137.506 138.573 1.00 103.40 ? 2331 GLU A CA    1 
ATOM   8056  C  C     . GLU A 1 2331 ? 184.883 137.831 137.916 1.00 100.36 ? 2331 GLU A C     1 
ATOM   8057  O  O     . GLU A 1 2331 ? 183.969 138.371 138.544 1.00 101.44 ? 2331 GLU A O     1 
ATOM   8058  C  CB    . GLU A 1 2331 ? 186.170 136.106 139.183 1.00 104.06 ? 2331 GLU A CB    1 
ATOM   8059  C  CG    . GLU A 1 2331 ? 187.489 135.626 139.756 1.00 104.32 ? 2331 GLU A CG    1 
ATOM   8060  C  CD    . GLU A 1 2331 ? 187.358 134.295 140.465 1.00 104.82 ? 2331 GLU A CD    1 
ATOM   8061  O  OE1   . GLU A 1 2331 ? 186.216 133.812 140.612 1.00 103.80 ? 2331 GLU A OE1   1 
ATOM   8062  O  OE2   . GLU A 1 2331 ? 188.394 133.731 140.876 1.00 106.99 ? 2331 GLU A OE2   1 
ATOM   8063  N  N     . ARG A 1 2332 ? 184.779 137.497 136.635 1.00 96.53  ? 2332 ARG A N     1 
ATOM   8064  C  CA    . ARG A 1 2332 ? 183.568 137.716 135.849 1.00 93.43  ? 2332 ARG A CA    1 
ATOM   8065  C  C     . ARG A 1 2332 ? 183.079 136.350 135.381 1.00 93.94  ? 2332 ARG A C     1 
ATOM   8066  O  O     . ARG A 1 2332 ? 183.604 135.794 134.412 1.00 94.57  ? 2332 ARG A O     1 
ATOM   8067  C  CB    . ARG A 1 2332 ? 183.842 138.655 134.679 1.00 92.27  ? 2332 ARG A CB    1 
ATOM   8068  C  CG    . ARG A 1 2332 ? 183.808 140.126 135.055 1.00 91.33  ? 2332 ARG A CG    1 
ATOM   8069  C  CD    . ARG A 1 2332 ? 184.960 140.888 134.416 1.00 90.96  ? 2332 ARG A CD    1 
ATOM   8070  N  NE    . ARG A 1 2332 ? 184.766 141.096 132.986 1.00 97.61  ? 2332 ARG A NE    1 
ATOM   8071  C  CZ    . ARG A 1 2332 ? 183.882 141.933 132.459 1.00 96.23  ? 2332 ARG A CZ    1 
ATOM   8072  N  NH1   . ARG A 1 2332 ? 183.098 142.681 133.219 1.00 90.16  ? 2332 ARG A NH1   1 
ATOM   8073  N  NH2   . ARG A 1 2332 ? 183.787 142.028 131.136 1.00 91.52  ? 2332 ARG A NH2   1 
ATOM   8074  N  N     . LEU A 1 2333 ? 182.078 135.810 136.071 1.00 95.41  ? 2333 LEU A N     1 
ATOM   8075  C  CA    . LEU A 1 2333 ? 181.597 134.460 135.811 1.00 93.59  ? 2333 LEU A CA    1 
ATOM   8076  C  C     . LEU A 1 2333 ? 180.447 134.524 134.813 1.00 91.67  ? 2333 LEU A C     1 
ATOM   8077  O  O     . LEU A 1 2333 ? 179.386 135.073 135.120 1.00 88.65  ? 2333 LEU A O     1 
ATOM   8078  C  CB    . LEU A 1 2333 ? 181.145 133.798 137.112 1.00 89.99  ? 2333 LEU A CB    1 
ATOM   8079  C  CG    . LEU A 1 2333 ? 182.175 132.948 137.861 1.00 92.05  ? 2333 LEU A CG    1 
ATOM   8080  C  CD1   . LEU A 1 2333 ? 181.516 132.184 139.003 1.00 80.67  ? 2333 LEU A CD1   1 
ATOM   8081  C  CD2   . LEU A 1 2333 ? 182.933 132.012 136.929 1.00 88.14  ? 2333 LEU A CD2   1 
ATOM   8082  N  N     . SER A 1 2334 ? 180.654 133.967 133.624 1.00 91.60  ? 2334 SER A N     1 
ATOM   8083  C  CA    . SER A 1 2334 ? 179.650 134.016 132.570 1.00 89.05  ? 2334 SER A CA    1 
ATOM   8084  C  C     . SER A 1 2334 ? 178.591 132.946 132.795 1.00 88.84  ? 2334 SER A C     1 
ATOM   8085  O  O     . SER A 1 2334 ? 178.910 131.791 133.088 1.00 87.94  ? 2334 SER A O     1 
ATOM   8086  C  CB    . SER A 1 2334 ? 180.297 133.826 131.198 1.00 86.68  ? 2334 SER A CB    1 
ATOM   8087  O  OG    . SER A 1 2334 ? 180.837 132.523 131.069 1.00 92.01  ? 2334 SER A OG    1 
ATOM   8088  N  N     . LEU A 1 2335 ? 177.332 133.334 132.646 1.00 83.71  ? 2335 LEU A N     1 
ATOM   8089  C  CA    . LEU A 1 2335 ? 176.231 132.398 132.838 1.00 79.48  ? 2335 LEU A CA    1 
ATOM   8090  C  C     . LEU A 1 2335 ? 176.196 131.395 131.693 1.00 81.42  ? 2335 LEU A C     1 
ATOM   8091  O  O     . LEU A 1 2335 ? 176.093 131.803 130.529 1.00 82.10  ? 2335 LEU A O     1 
ATOM   8092  C  CB    . LEU A 1 2335 ? 174.904 133.145 132.926 1.00 77.46  ? 2335 LEU A CB    1 
ATOM   8093  C  CG    . LEU A 1 2335 ? 173.711 132.344 133.447 1.00 76.43  ? 2335 LEU A CG    1 
ATOM   8094  C  CD1   . LEU A 1 2335 ? 173.978 131.859 134.859 1.00 71.81  ? 2335 LEU A CD1   1 
ATOM   8095  C  CD2   . LEU A 1 2335 ? 172.436 133.170 133.395 1.00 73.78  ? 2335 LEU A CD2   1 
ATOM   8096  N  N     . PRO A 1 2336 ? 176.281 130.092 131.966 1.00 78.65  ? 2336 PRO A N     1 
ATOM   8097  C  CA    . PRO A 1 2336 ? 176.218 129.116 130.881 1.00 76.81  ? 2336 PRO A CA    1 
ATOM   8098  C  C     . PRO A 1 2336 ? 174.848 129.118 130.233 1.00 74.47  ? 2336 PRO A C     1 
ATOM   8099  O  O     . PRO A 1 2336 ? 173.847 129.505 130.861 1.00 75.39  ? 2336 PRO A O     1 
ATOM   8100  C  CB    . PRO A 1 2336 ? 176.503 127.780 131.591 1.00 75.43  ? 2336 PRO A CB    1 
ATOM   8101  C  CG    . PRO A 1 2336 ? 177.202 128.159 132.850 1.00 77.27  ? 2336 PRO A CG    1 
ATOM   8102  C  CD    . PRO A 1 2336 ? 176.601 129.465 133.258 1.00 72.67  ? 2336 PRO A CD    1 
ATOM   8103  N  N     . PRO A 1 2337 ? 174.751 128.712 128.964 1.00 77.56  ? 2337 PRO A N     1 
ATOM   8104  C  CA    . PRO A 1 2337 ? 173.439 128.703 128.297 1.00 79.10  ? 2337 PRO A CA    1 
ATOM   8105  C  C     . PRO A 1 2337 ? 172.419 127.789 128.954 1.00 76.58  ? 2337 PRO A C     1 
ATOM   8106  O  O     . PRO A 1 2337 ? 171.222 128.102 128.935 1.00 71.92  ? 2337 PRO A O     1 
ATOM   8107  C  CB    . PRO A 1 2337 ? 173.777 128.239 126.873 1.00 75.19  ? 2337 PRO A CB    1 
ATOM   8108  C  CG    . PRO A 1 2337 ? 175.072 127.511 127.006 1.00 71.47  ? 2337 PRO A CG    1 
ATOM   8109  C  CD    . PRO A 1 2337 ? 175.825 128.228 128.081 1.00 75.34  ? 2337 PRO A CD    1 
ATOM   8110  N  N     . ASN A 1 2338 ? 172.850 126.666 129.533 1.00 74.95  ? 2338 ASN A N     1 
ATOM   8111  C  CA    . ASN A 1 2338 ? 171.902 125.722 130.116 1.00 71.42  ? 2338 ASN A CA    1 
ATOM   8112  C  C     . ASN A 1 2338 ? 171.363 126.192 131.460 1.00 69.31  ? 2338 ASN A C     1 
ATOM   8113  O  O     . ASN A 1 2338 ? 170.252 125.807 131.842 1.00 66.50  ? 2338 ASN A O     1 
ATOM   8114  C  CB    . ASN A 1 2338 ? 172.552 124.346 130.271 1.00 69.99  ? 2338 ASN A CB    1 
ATOM   8115  C  CG    . ASN A 1 2338 ? 173.764 124.372 131.180 1.00 76.95  ? 2338 ASN A CG    1 
ATOM   8116  O  OD1   . ASN A 1 2338 ? 174.262 125.436 131.541 1.00 78.54  ? 2338 ASN A OD1   1 
ATOM   8117  N  ND2   . ASN A 1 2338 ? 174.239 123.194 131.562 1.00 76.46  ? 2338 ASN A ND2   1 
ATOM   8118  N  N     . VAL A 1 2339 ? 172.125 127.005 132.191 1.00 65.90  ? 2339 VAL A N     1 
ATOM   8119  C  CA    . VAL A 1 2339 ? 171.704 127.439 133.518 1.00 59.92  ? 2339 VAL A CA    1 
ATOM   8120  C  C     . VAL A 1 2339 ? 170.496 128.355 133.397 1.00 58.87  ? 2339 VAL A C     1 
ATOM   8121  O  O     . VAL A 1 2339 ? 170.468 129.269 132.564 1.00 59.94  ? 2339 VAL A O     1 
ATOM   8122  C  CB    . VAL A 1 2339 ? 172.857 128.137 134.251 1.00 62.87  ? 2339 VAL A CB    1 
ATOM   8123  C  CG1   . VAL A 1 2339 ? 172.400 128.622 135.615 1.00 58.84  ? 2339 VAL A CG1   1 
ATOM   8124  C  CG2   . VAL A 1 2339 ? 174.022 127.193 134.397 1.00 68.83  ? 2339 VAL A CG2   1 
ATOM   8125  N  N     . ARG A 1 2340 ? 169.490 128.112 134.233 1.00 57.84  ? 2340 ARG A N     1 
ATOM   8126  C  CA    . ARG A 1 2340 ? 168.270 128.914 134.263 1.00 52.09  ? 2340 ARG A CA    1 
ATOM   8127  C  C     . ARG A 1 2340 ? 168.056 129.366 135.704 1.00 48.25  ? 2340 ARG A C     1 
ATOM   8128  O  O     . ARG A 1 2340 ? 167.785 128.543 136.582 1.00 53.10  ? 2340 ARG A O     1 
ATOM   8129  C  CB    . ARG A 1 2340 ? 167.081 128.114 133.746 1.00 51.92  ? 2340 ARG A CB    1 
ATOM   8130  C  CG    . ARG A 1 2340 ? 165.949 128.950 133.191 1.00 54.69  ? 2340 ARG A CG    1 
ATOM   8131  C  CD    . ARG A 1 2340 ? 166.228 129.327 131.750 1.00 54.89  ? 2340 ARG A CD    1 
ATOM   8132  N  NE    . ARG A 1 2340 ? 166.652 128.180 130.958 1.00 52.93  ? 2340 ARG A NE    1 
ATOM   8133  C  CZ    . ARG A 1 2340 ? 167.002 128.242 129.680 1.00 56.40  ? 2340 ARG A CZ    1 
ATOM   8134  N  NH1   . ARG A 1 2340 ? 166.996 129.385 129.017 1.00 59.33  ? 2340 ARG A NH1   1 
ATOM   8135  N  NH2   . ARG A 1 2340 ? 167.366 127.128 129.053 1.00 59.82  ? 2340 ARG A NH2   1 
ATOM   8136  N  N     . ILE A 1 2341 ? 168.198 130.667 135.953 1.00 45.33  ? 2341 ILE A N     1 
ATOM   8137  C  CA    . ILE A 1 2341 ? 167.914 131.207 137.276 1.00 46.79  ? 2341 ILE A CA    1 
ATOM   8138  C  C     . ILE A 1 2341 ? 166.408 131.335 137.442 1.00 51.23  ? 2341 ILE A C     1 
ATOM   8139  O  O     . ILE A 1 2341 ? 165.729 131.958 136.618 1.00 62.01  ? 2341 ILE A O     1 
ATOM   8140  C  CB    . ILE A 1 2341 ? 168.611 132.561 137.471 1.00 48.29  ? 2341 ILE A CB    1 
ATOM   8141  C  CG1   . ILE A 1 2341 ? 170.100 132.451 137.145 1.00 50.54  ? 2341 ILE A CG1   1 
ATOM   8142  C  CG2   . ILE A 1 2341 ? 168.409 133.059 138.891 1.00 49.09  ? 2341 ILE A CG2   1 
ATOM   8143  C  CD1   . ILE A 1 2341 ? 170.840 131.457 138.003 1.00 52.31  ? 2341 ILE A CD1   1 
ATOM   8144  N  N     . MET A 1 2342 ? 165.875 130.745 138.505 1.00 42.44  ? 2342 MET A N     1 
ATOM   8145  C  CA    . MET A 1 2342 ? 164.439 130.665 138.707 1.00 39.29  ? 2342 MET A CA    1 
ATOM   8146  C  C     . MET A 1 2342 ? 164.106 131.108 140.121 1.00 43.76  ? 2342 MET A C     1 
ATOM   8147  O  O     . MET A 1 2342 ? 164.718 130.644 141.086 1.00 49.26  ? 2342 MET A O     1 
ATOM   8148  C  CB    . MET A 1 2342 ? 163.943 129.238 138.453 1.00 37.73  ? 2342 MET A CB    1 
ATOM   8149  C  CG    . MET A 1 2342 ? 164.235 128.748 137.043 1.00 46.93  ? 2342 MET A CG    1 
ATOM   8150  S  SD    . MET A 1 2342 ? 163.487 127.170 136.609 1.00 63.83  ? 2342 MET A SD    1 
ATOM   8151  C  CE    . MET A 1 2342 ? 162.003 127.202 137.599 1.00 46.76  ? 2342 MET A CE    1 
ATOM   8152  N  N     . PHE A 1 2343 ? 163.143 132.015 140.238 1.00 41.30  ? 2343 PHE A N     1 
ATOM   8153  C  CA    . PHE A 1 2343 ? 162.654 132.483 141.526 1.00 36.73  ? 2343 PHE A CA    1 
ATOM   8154  C  C     . PHE A 1 2343 ? 161.275 131.891 141.763 1.00 41.00  ? 2343 PHE A C     1 
ATOM   8155  O  O     . PHE A 1 2343 ? 160.393 132.006 140.907 1.00 50.27  ? 2343 PHE A O     1 
ATOM   8156  C  CB    . PHE A 1 2343 ? 162.572 134.011 141.579 1.00 40.23  ? 2343 PHE A CB    1 
ATOM   8157  C  CG    . PHE A 1 2343 ? 163.894 134.712 141.423 1.00 48.16  ? 2343 PHE A CG    1 
ATOM   8158  C  CD1   . PHE A 1 2343 ? 165.087 134.030 141.545 1.00 54.46  ? 2343 PHE A CD1   1 
ATOM   8159  C  CD2   . PHE A 1 2343 ? 163.936 136.068 141.160 1.00 52.12  ? 2343 PHE A CD2   1 
ATOM   8160  C  CE1   . PHE A 1 2343 ? 166.292 134.690 141.400 1.00 54.66  ? 2343 PHE A CE1   1 
ATOM   8161  C  CE2   . PHE A 1 2343 ? 165.135 136.728 141.018 1.00 53.61  ? 2343 PHE A CE2   1 
ATOM   8162  C  CZ    . PHE A 1 2343 ? 166.314 136.038 141.138 1.00 54.62  ? 2343 PHE A CZ    1 
ATOM   8163  N  N     . GLU A 1 2344 ? 161.089 131.257 142.912 1.00 37.00  ? 2344 GLU A N     1 
ATOM   8164  C  CA    . GLU A 1 2344 ? 159.775 130.788 143.336 1.00 32.16  ? 2344 GLU A CA    1 
ATOM   8165  C  C     . GLU A 1 2344 ? 159.404 131.593 144.574 1.00 37.54  ? 2344 GLU A C     1 
ATOM   8166  O  O     . GLU A 1 2344 ? 159.889 131.319 145.674 1.00 46.77  ? 2344 GLU A O     1 
ATOM   8167  C  CB    . GLU A 1 2344 ? 159.771 129.290 143.611 1.00 31.24  ? 2344 GLU A CB    1 
ATOM   8168  C  CG    . GLU A 1 2344 ? 158.518 128.808 144.320 1.00 35.40  ? 2344 GLU A CG    1 
ATOM   8169  C  CD    . GLU A 1 2344 ? 158.511 127.315 144.540 1.00 37.20  ? 2344 GLU A CD    1 
ATOM   8170  O  OE1   . GLU A 1 2344 ? 159.057 126.588 143.686 1.00 39.68  ? 2344 GLU A OE1   1 
ATOM   8171  O  OE2   . GLU A 1 2344 ? 157.963 126.866 145.566 1.00 36.56  ? 2344 GLU A OE2   1 
ATOM   8172  N  N     . VAL A 1 2345 ? 158.546 132.593 144.387 1.00 33.05  ? 2345 VAL A N     1 
ATOM   8173  C  CA    . VAL A 1 2345 ? 158.189 133.518 145.449 1.00 33.44  ? 2345 VAL A CA    1 
ATOM   8174  C  C     . VAL A 1 2345 ? 156.684 133.477 145.658 1.00 35.73  ? 2345 VAL A C     1 
ATOM   8175  O  O     . VAL A 1 2345 ? 155.934 132.900 144.870 1.00 38.76  ? 2345 VAL A O     1 
ATOM   8176  C  CB    . VAL A 1 2345 ? 158.647 134.959 145.145 1.00 39.56  ? 2345 VAL A CB    1 
ATOM   8177  C  CG1   . VAL A 1 2345 ? 160.144 135.066 145.261 1.00 46.71  ? 2345 VAL A CG1   1 
ATOM   8178  C  CG2   . VAL A 1 2345 ? 158.214 135.361 143.762 1.00 35.93  ? 2345 VAL A CG2   1 
ATOM   8179  N  N     . GLN A 1 2346 ? 156.254 134.095 146.752 1.00 38.09  ? 2346 GLN A N     1 
ATOM   8180  C  CA    . GLN A 1 2346 ? 154.842 134.221 147.080 1.00 37.46  ? 2346 GLN A CA    1 
ATOM   8181  C  C     . GLN A 1 2346 ? 154.285 135.563 146.618 1.00 44.05  ? 2346 GLN A C     1 
ATOM   8182  O  O     . GLN A 1 2346 ? 153.111 135.662 146.249 1.00 42.96  ? 2346 GLN A O     1 
ATOM   8183  C  CB    . GLN A 1 2346 ? 154.651 134.049 148.589 1.00 41.89  ? 2346 GLN A CB    1 
ATOM   8184  C  CG    . GLN A 1 2346 ? 153.231 134.234 149.078 1.00 50.38  ? 2346 GLN A CG    1 
ATOM   8185  C  CD    . GLN A 1 2346 ? 153.080 133.882 150.541 1.00 54.67  ? 2346 GLN A CD    1 
ATOM   8186  O  OE1   . GLN A 1 2346 ? 152.225 133.080 150.915 1.00 58.30  ? 2346 GLN A OE1   1 
ATOM   8187  N  NE2   . GLN A 1 2346 ? 153.917 134.479 151.379 1.00 48.98  ? 2346 GLN A NE2   1 
ATOM   8188  N  N     . ASP A 1 2347 ? 155.120 136.597 146.627 1.00 46.01  ? 2347 ASP A N     1 
ATOM   8189  C  CA    . ASP A 1 2347 ? 154.681 137.960 146.378 1.00 44.53  ? 2347 ASP A CA    1 
ATOM   8190  C  C     . ASP A 1 2347 ? 155.867 138.809 145.941 1.00 51.93  ? 2347 ASP A C     1 
ATOM   8191  O  O     . ASP A 1 2347 ? 157.027 138.402 146.047 1.00 53.37  ? 2347 ASP A O     1 
ATOM   8192  C  CB    . ASP A 1 2347 ? 153.989 138.532 147.622 1.00 50.62  ? 2347 ASP A CB    1 
ATOM   8193  C  CG    . ASP A 1 2347 ? 154.911 138.605 148.832 1.00 64.84  ? 2347 ASP A CG    1 
ATOM   8194  O  OD1   . ASP A 1 2347 ? 156.083 138.181 148.740 1.00 72.43  ? 2347 ASP A OD1   1 
ATOM   8195  O  OD2   . ASP A 1 2347 ? 154.451 139.054 149.900 1.00 63.72  ? 2347 ASP A OD2   1 
ATOM   8196  N  N     . LEU A 1 2348 ? 155.564 140.005 145.435 1.00 58.26  ? 2348 LEU A N     1 
ATOM   8197  C  CA    . LEU A 1 2348 ? 156.579 140.949 144.983 1.00 58.43  ? 2348 LEU A CA    1 
ATOM   8198  C  C     . LEU A 1 2348 ? 156.462 142.291 145.699 1.00 62.96  ? 2348 LEU A C     1 
ATOM   8199  O  O     . LEU A 1 2348 ? 156.733 143.337 145.108 1.00 70.45  ? 2348 LEU A O     1 
ATOM   8200  C  CB    . LEU A 1 2348 ? 156.497 141.157 143.472 1.00 56.31  ? 2348 LEU A CB    1 
ATOM   8201  C  CG    . LEU A 1 2348 ? 156.827 139.984 142.553 1.00 48.06  ? 2348 LEU A CG    1 
ATOM   8202  C  CD1   . LEU A 1 2348 ? 156.114 140.151 141.225 1.00 46.09  ? 2348 LEU A CD1   1 
ATOM   8203  C  CD2   . LEU A 1 2348 ? 158.318 139.873 142.343 1.00 50.61  ? 2348 LEU A CD2   1 
ATOM   8204  N  N     . LYS A 1 2349 ? 156.052 142.279 146.968 1.00 62.46  ? 2349 LYS A N     1 
ATOM   8205  C  CA    . LYS A 1 2349 ? 155.880 143.535 147.693 1.00 70.90  ? 2349 LYS A CA    1 
ATOM   8206  C  C     . LYS A 1 2349 ? 157.210 144.249 147.895 1.00 74.26  ? 2349 LYS A C     1 
ATOM   8207  O  O     . LYS A 1 2349 ? 157.278 145.482 147.826 1.00 72.95  ? 2349 LYS A O     1 
ATOM   8208  C  CB    . LYS A 1 2349 ? 155.196 143.282 149.034 1.00 68.42  ? 2349 LYS A CB    1 
ATOM   8209  C  CG    . LYS A 1 2349 ? 153.772 142.773 148.908 1.00 69.87  ? 2349 LYS A CG    1 
ATOM   8210  C  CD    . LYS A 1 2349 ? 153.368 141.966 150.123 1.00 80.38  ? 2349 LYS A CD    1 
ATOM   8211  C  CE    . LYS A 1 2349 ? 153.376 142.826 151.373 1.00 85.75  ? 2349 LYS A CE    1 
ATOM   8212  N  NZ    . LYS A 1 2349 ? 152.282 142.443 152.305 1.00 80.68  ? 2349 LYS A NZ    1 
ATOM   8213  N  N     . TYR A 1 2350 ? 158.275 143.497 148.144 1.00 72.88  ? 2350 TYR A N     1 
ATOM   8214  C  CA    . TYR A 1 2350 ? 159.597 144.051 148.406 1.00 75.11  ? 2350 TYR A CA    1 
ATOM   8215  C  C     . TYR A 1 2350 ? 160.581 143.667 147.309 1.00 75.72  ? 2350 TYR A C     1 
ATOM   8216  O  O     . TYR A 1 2350 ? 161.728 143.311 147.576 1.00 79.76  ? 2350 TYR A O     1 
ATOM   8217  C  CB    . TYR A 1 2350 ? 160.113 143.602 149.771 1.00 74.43  ? 2350 TYR A CB    1 
ATOM   8218  C  CG    . TYR A 1 2350 ? 159.085 143.698 150.872 1.00 73.91  ? 2350 TYR A CG    1 
ATOM   8219  C  CD1   . TYR A 1 2350 ? 158.861 144.895 151.535 1.00 72.99  ? 2350 TYR A CD1   1 
ATOM   8220  C  CD2   . TYR A 1 2350 ? 158.325 142.595 151.237 1.00 76.19  ? 2350 TYR A CD2   1 
ATOM   8221  C  CE1   . TYR A 1 2350 ? 157.920 144.989 152.540 1.00 73.88  ? 2350 TYR A CE1   1 
ATOM   8222  C  CE2   . TYR A 1 2350 ? 157.379 142.681 152.237 1.00 76.36  ? 2350 TYR A CE2   1 
ATOM   8223  C  CZ    . TYR A 1 2350 ? 157.182 143.879 152.886 1.00 78.11  ? 2350 TYR A CZ    1 
ATOM   8224  O  OH    . TYR A 1 2350 ? 156.241 143.967 153.886 1.00 84.27  ? 2350 TYR A OH    1 
ATOM   8225  N  N     . ALA A 1 2351 ? 160.143 143.735 146.056 1.00 74.31  ? 2351 ALA A N     1 
ATOM   8226  C  CA    . ALA A 1 2351 ? 160.993 143.441 144.913 1.00 76.53  ? 2351 ALA A CA    1 
ATOM   8227  C  C     . ALA A 1 2351 ? 161.109 144.673 144.028 1.00 88.01  ? 2351 ALA A C     1 
ATOM   8228  O  O     . ALA A 1 2351 ? 160.122 145.376 143.793 1.00 90.37  ? 2351 ALA A O     1 
ATOM   8229  C  CB    . ALA A 1 2351 ? 160.447 142.264 144.103 1.00 67.23  ? 2351 ALA A CB    1 
ATOM   8230  N  N     . THR A 1 2352 ? 162.321 144.932 143.544 1.00 88.26  ? 2352 THR A N     1 
ATOM   8231  C  CA    . THR A 1 2352 ? 162.564 146.073 142.674 1.00 84.09  ? 2352 THR A CA    1 
ATOM   8232  C  C     . THR A 1 2352 ? 161.945 145.850 141.304 1.00 81.14  ? 2352 THR A C     1 
ATOM   8233  O  O     . THR A 1 2352 ? 161.753 144.711 140.869 1.00 85.43  ? 2352 THR A O     1 
ATOM   8234  C  CB    . THR A 1 2352 ? 164.063 146.327 142.519 1.00 88.95  ? 2352 THR A CB    1 
ATOM   8235  O  OG1   . THR A 1 2352 ? 164.698 145.158 141.988 1.00 90.02  ? 2352 THR A OG1   1 
ATOM   8236  C  CG2   . THR A 1 2352 ? 164.681 146.680 143.849 1.00 86.95  ? 2352 THR A CG2   1 
ATOM   8237  N  N     . LEU A 1 2353 ? 161.630 146.953 140.623 1.00 79.19  ? 2353 LEU A N     1 
ATOM   8238  C  CA    . LEU A 1 2353 ? 161.132 146.852 139.257 1.00 81.60  ? 2353 LEU A CA    1 
ATOM   8239  C  C     . LEU A 1 2353 ? 162.220 146.383 138.303 1.00 78.41  ? 2353 LEU A C     1 
ATOM   8240  O  O     . LEU A 1 2353 ? 161.916 145.813 137.250 1.00 77.97  ? 2353 LEU A O     1 
ATOM   8241  C  CB    . LEU A 1 2353 ? 160.560 148.193 138.796 1.00 84.46  ? 2353 LEU A CB    1 
ATOM   8242  C  CG    . LEU A 1 2353 ? 159.118 148.537 139.188 1.00 91.49  ? 2353 LEU A CG    1 
ATOM   8243  C  CD1   . LEU A 1 2353 ? 158.147 147.553 138.550 1.00 80.32  ? 2353 LEU A CD1   1 
ATOM   8244  C  CD2   . LEU A 1 2353 ? 158.919 148.595 140.699 1.00 86.93  ? 2353 LEU A CD2   1 
ATOM   8245  N  N     . ALA A 1 2354 ? 163.489 146.613 138.647 1.00 75.66  ? 2354 ALA A N     1 
ATOM   8246  C  CA    . ALA A 1 2354 ? 164.582 146.123 137.814 1.00 77.30  ? 2354 ALA A CA    1 
ATOM   8247  C  C     . ALA A 1 2354 ? 164.602 144.600 137.778 1.00 79.51  ? 2354 ALA A C     1 
ATOM   8248  O  O     . ALA A 1 2354 ? 164.697 143.992 136.705 1.00 85.05  ? 2354 ALA A O     1 
ATOM   8249  C  CB    . ALA A 1 2354 ? 165.915 146.668 138.325 1.00 80.55  ? 2354 ALA A CB    1 
ATOM   8250  N  N     . THR A 1 2355 ? 164.502 143.965 138.948 1.00 75.95  ? 2355 THR A N     1 
ATOM   8251  C  CA    . THR A 1 2355 ? 164.496 142.506 139.004 1.00 75.99  ? 2355 THR A CA    1 
ATOM   8252  C  C     . THR A 1 2355 ? 163.273 141.933 138.300 1.00 77.21  ? 2355 THR A C     1 
ATOM   8253  O  O     . THR A 1 2355 ? 163.372 140.927 137.588 1.00 76.46  ? 2355 THR A O     1 
ATOM   8254  C  CB    . THR A 1 2355 ? 164.545 142.037 140.458 1.00 78.27  ? 2355 THR A CB    1 
ATOM   8255  O  OG1   . THR A 1 2355 ? 165.642 142.669 141.128 1.00 89.13  ? 2355 THR A OG1   1 
ATOM   8256  C  CG2   . THR A 1 2355 ? 164.720 140.529 140.527 1.00 70.50  ? 2355 THR A CG2   1 
ATOM   8257  N  N     . VAL A 1 2356 ? 162.109 142.558 138.491 1.00 72.32  ? 2356 VAL A N     1 
ATOM   8258  C  CA    . VAL A 1 2356 ? 160.891 142.085 137.840 1.00 66.24  ? 2356 VAL A CA    1 
ATOM   8259  C  C     . VAL A 1 2356 ? 161.015 142.202 136.326 1.00 70.32  ? 2356 VAL A C     1 
ATOM   8260  O  O     . VAL A 1 2356 ? 160.626 141.293 135.582 1.00 73.02  ? 2356 VAL A O     1 
ATOM   8261  C  CB    . VAL A 1 2356 ? 159.670 142.858 138.372 1.00 60.47  ? 2356 VAL A CB    1 
ATOM   8262  C  CG1   . VAL A 1 2356 ? 158.425 142.493 137.586 1.00 61.84  ? 2356 VAL A CG1   1 
ATOM   8263  C  CG2   . VAL A 1 2356 ? 159.472 142.580 139.851 1.00 64.71  ? 2356 VAL A CG2   1 
ATOM   8264  N  N     . SER A 1 2357 ? 161.559 143.322 135.845 1.00 70.36  ? 2357 SER A N     1 
ATOM   8265  C  CA    . SER A 1 2357 ? 161.681 143.535 134.407 1.00 68.76  ? 2357 SER A CA    1 
ATOM   8266  C  C     . SER A 1 2357 ? 162.707 142.596 133.787 1.00 68.79  ? 2357 SER A C     1 
ATOM   8267  O  O     . SER A 1 2357 ? 162.535 142.148 132.647 1.00 70.69  ? 2357 SER A O     1 
ATOM   8268  C  CB    . SER A 1 2357 ? 162.046 144.992 134.128 1.00 64.13  ? 2357 SER A CB    1 
ATOM   8269  O  OG    . SER A 1 2357 ? 163.238 145.354 134.801 1.00 68.23  ? 2357 SER A OG    1 
ATOM   8270  N  N     . ARG A 1 2358 ? 163.782 142.286 134.514 1.00 65.47  ? 2358 ARG A N     1 
ATOM   8271  C  CA    . ARG A 1 2358 ? 164.822 141.424 133.964 1.00 66.89  ? 2358 ARG A CA    1 
ATOM   8272  C  C     . ARG A 1 2358 ? 164.407 139.960 133.897 1.00 66.72  ? 2358 ARG A C     1 
ATOM   8273  O  O     . ARG A 1 2358 ? 165.101 139.165 133.254 1.00 63.51  ? 2358 ARG A O     1 
ATOM   8274  C  CB    . ARG A 1 2358 ? 166.106 141.556 134.784 1.00 73.75  ? 2358 ARG A CB    1 
ATOM   8275  C  CG    . ARG A 1 2358 ? 166.809 142.891 134.632 1.00 81.12  ? 2358 ARG A CG    1 
ATOM   8276  C  CD    . ARG A 1 2358 ? 168.077 142.942 135.467 1.00 81.21  ? 2358 ARG A CD    1 
ATOM   8277  N  NE    . ARG A 1 2358 ? 168.250 144.223 136.144 1.00 81.03  ? 2358 ARG A NE    1 
ATOM   8278  C  CZ    . ARG A 1 2358 ? 168.500 145.374 135.534 1.00 81.40  ? 2358 ARG A CZ    1 
ATOM   8279  N  NH1   . ARG A 1 2358 ? 168.642 145.446 134.220 1.00 86.81  ? 2358 ARG A NH1   1 
ATOM   8280  N  NH2   . ARG A 1 2358 ? 168.621 146.480 136.261 1.00 82.32  ? 2358 ARG A NH2   1 
ATOM   8281  N  N     . CYS A 1 2359 ? 163.305 139.582 134.538 1.00 69.17  ? 2359 CYS A N     1 
ATOM   8282  C  CA    . CYS A 1 2359 ? 162.894 138.189 134.637 1.00 61.90  ? 2359 CYS A CA    1 
ATOM   8283  C  C     . CYS A 1 2359 ? 161.534 137.974 133.988 1.00 60.27  ? 2359 CYS A C     1 
ATOM   8284  O  O     . CYS A 1 2359 ? 160.662 138.846 134.045 1.00 61.43  ? 2359 CYS A O     1 
ATOM   8285  C  CB    . CYS A 1 2359 ? 162.829 137.740 136.099 1.00 56.82  ? 2359 CYS A CB    1 
ATOM   8286  S  SG    . CYS A 1 2359 ? 164.362 137.937 137.016 1.00 74.01  ? 2359 CYS A SG    1 
ATOM   8287  N  N     . GLY A 1 2360 ? 161.360 136.805 133.375 1.00 49.78  ? 2360 GLY A N     1 
ATOM   8288  C  CA    . GLY A 1 2360 ? 160.045 136.396 132.934 1.00 42.88  ? 2360 GLY A CA    1 
ATOM   8289  C  C     . GLY A 1 2360 ? 159.125 136.135 134.108 1.00 45.85  ? 2360 GLY A C     1 
ATOM   8290  O  O     . GLY A 1 2360 ? 159.557 135.929 135.238 1.00 52.64  ? 2360 GLY A O     1 
ATOM   8291  N  N     . MET A 1 2361 ? 157.825 136.150 133.840 1.00 44.72  ? 2361 MET A N     1 
ATOM   8292  C  CA    . MET A 1 2361 ? 156.832 136.111 134.902 1.00 38.58  ? 2361 MET A CA    1 
ATOM   8293  C  C     . MET A 1 2361 ? 155.812 135.022 134.614 1.00 38.95  ? 2361 MET A C     1 
ATOM   8294  O  O     . MET A 1 2361 ? 155.256 134.972 133.513 1.00 40.79  ? 2361 MET A O     1 
ATOM   8295  C  CB    . MET A 1 2361 ? 156.137 137.468 135.027 1.00 42.78  ? 2361 MET A CB    1 
ATOM   8296  C  CG    . MET A 1 2361 ? 155.177 137.577 136.181 1.00 45.83  ? 2361 MET A CG    1 
ATOM   8297  S  SD    . MET A 1 2361 ? 156.074 137.407 137.720 1.00 60.09  ? 2361 MET A SD    1 
ATOM   8298  C  CE    . MET A 1 2361 ? 156.944 138.969 137.775 1.00 52.19  ? 2361 MET A CE    1 
ATOM   8299  N  N     . VAL A 1 2362 ? 155.566 134.154 135.595 1.00 35.43  ? 2362 VAL A N     1 
ATOM   8300  C  CA    . VAL A 1 2362 ? 154.468 133.194 135.536 1.00 29.82  ? 2362 VAL A CA    1 
ATOM   8301  C  C     . VAL A 1 2362 ? 153.763 133.247 136.882 1.00 33.61  ? 2362 VAL A C     1 
ATOM   8302  O  O     . VAL A 1 2362 ? 154.320 132.807 137.894 1.00 43.24  ? 2362 VAL A O     1 
ATOM   8303  C  CB    . VAL A 1 2362 ? 154.941 131.767 135.226 1.00 26.86  ? 2362 VAL A CB    1 
ATOM   8304  C  CG1   . VAL A 1 2362 ? 153.750 130.867 134.973 1.00 29.58  ? 2362 VAL A CG1   1 
ATOM   8305  C  CG2   . VAL A 1 2362 ? 155.872 131.754 134.033 1.00 34.61  ? 2362 VAL A CG2   1 
ATOM   8306  N  N     . TRP A 1 2363 ? 152.543 133.776 136.901 1.00 29.70  ? 2363 TRP A N     1 
ATOM   8307  C  CA    . TRP A 1 2363 ? 151.794 133.934 138.140 1.00 30.09  ? 2363 TRP A CA    1 
ATOM   8308  C  C     . TRP A 1 2363 ? 150.915 132.710 138.359 1.00 33.93  ? 2363 TRP A C     1 
ATOM   8309  O  O     . TRP A 1 2363 ? 150.084 132.376 137.509 1.00 33.14  ? 2363 TRP A O     1 
ATOM   8310  C  CB    . TRP A 1 2363 ? 150.953 135.208 138.107 1.00 28.54  ? 2363 TRP A CB    1 
ATOM   8311  C  CG    . TRP A 1 2363 ? 150.264 135.490 139.402 1.00 31.39  ? 2363 TRP A CG    1 
ATOM   8312  C  CD1   . TRP A 1 2363 ? 149.121 134.911 139.866 1.00 35.48  ? 2363 TRP A CD1   1 
ATOM   8313  C  CD2   . TRP A 1 2363 ? 150.688 136.406 140.415 1.00 29.06  ? 2363 TRP A CD2   1 
ATOM   8314  N  NE1   . TRP A 1 2363 ? 148.801 135.417 141.100 1.00 32.40  ? 2363 TRP A NE1   1 
ATOM   8315  C  CE2   . TRP A 1 2363 ? 149.749 136.337 141.460 1.00 26.95  ? 2363 TRP A CE2   1 
ATOM   8316  C  CE3   . TRP A 1 2363 ? 151.769 137.282 140.538 1.00 31.26  ? 2363 TRP A CE3   1 
ATOM   8317  C  CZ2   . TRP A 1 2363 ? 149.857 137.108 142.611 1.00 29.69  ? 2363 TRP A CZ2   1 
ATOM   8318  C  CZ3   . TRP A 1 2363 ? 151.874 138.047 141.680 1.00 32.99  ? 2363 TRP A CZ3   1 
ATOM   8319  C  CH2   . TRP A 1 2363 ? 150.924 137.956 142.702 1.00 36.71  ? 2363 TRP A CH2   1 
ATOM   8320  N  N     . PHE A 1 2364 ? 151.096 132.048 139.503 1.00 32.81  ? 2364 PHE A N     1 
ATOM   8321  C  CA    . PHE A 1 2364 ? 150.334 130.851 139.852 1.00 28.62  ? 2364 PHE A CA    1 
ATOM   8322  C  C     . PHE A 1 2364 ? 149.240 131.239 140.841 1.00 33.40  ? 2364 PHE A C     1 
ATOM   8323  O  O     . PHE A 1 2364 ? 149.388 131.110 142.052 1.00 40.54  ? 2364 PHE A O     1 
ATOM   8324  C  CB    . PHE A 1 2364 ? 151.247 129.779 140.437 1.00 25.29  ? 2364 PHE A CB    1 
ATOM   8325  C  CG    . PHE A 1 2364 ? 152.029 129.016 139.413 1.00 23.42  ? 2364 PHE A CG    1 
ATOM   8326  C  CD1   . PHE A 1 2364 ? 153.120 129.584 138.788 1.00 20.55  ? 2364 PHE A CD1   1 
ATOM   8327  C  CD2   . PHE A 1 2364 ? 151.670 127.726 139.080 1.00 27.97  ? 2364 PHE A CD2   1 
ATOM   8328  C  CE1   . PHE A 1 2364 ? 153.834 128.878 137.852 1.00 25.81  ? 2364 PHE A CE1   1 
ATOM   8329  C  CE2   . PHE A 1 2364 ? 152.382 127.019 138.145 1.00 27.12  ? 2364 PHE A CE2   1 
ATOM   8330  C  CZ    . PHE A 1 2364 ? 153.466 127.594 137.531 1.00 30.00  ? 2364 PHE A CZ    1 
ATOM   8331  N  N     . SER A 1 2365 ? 148.115 131.703 140.311 1.00 36.87  ? 2365 SER A N     1 
ATOM   8332  C  CA    . SER A 1 2365 ? 146.993 132.043 141.173 1.00 36.18  ? 2365 SER A CA    1 
ATOM   8333  C  C     . SER A 1 2365 ? 146.486 130.797 141.890 1.00 41.43  ? 2365 SER A C     1 
ATOM   8334  O  O     . SER A 1 2365 ? 146.638 129.674 141.409 1.00 46.76  ? 2365 SER A O     1 
ATOM   8335  C  CB    . SER A 1 2365 ? 145.874 132.686 140.357 1.00 43.06  ? 2365 SER A CB    1 
ATOM   8336  O  OG    . SER A 1 2365 ? 145.518 131.874 139.253 1.00 50.10  ? 2365 SER A OG    1 
ATOM   8337  N  N     . GLU A 1 2366 ? 145.892 131.000 143.069 1.00 44.81  ? 2366 GLU A N     1 
ATOM   8338  C  CA    . GLU A 1 2366 ? 145.418 129.869 143.862 1.00 44.19  ? 2366 GLU A CA    1 
ATOM   8339  C  C     . GLU A 1 2366 ? 144.342 129.065 143.148 1.00 47.51  ? 2366 GLU A C     1 
ATOM   8340  O  O     . GLU A 1 2366 ? 144.130 127.896 143.488 1.00 46.79  ? 2366 GLU A O     1 
ATOM   8341  C  CB    . GLU A 1 2366 ? 144.889 130.349 145.213 1.00 50.28  ? 2366 GLU A CB    1 
ATOM   8342  C  CG    . GLU A 1 2366 ? 145.951 130.917 146.135 1.00 62.00  ? 2366 GLU A CG    1 
ATOM   8343  C  CD    . GLU A 1 2366 ? 145.377 131.399 147.453 1.00 75.11  ? 2366 GLU A CD    1 
ATOM   8344  O  OE1   . GLU A 1 2366 ? 144.137 131.405 147.595 1.00 81.60  ? 2366 GLU A OE1   1 
ATOM   8345  O  OE2   . GLU A 1 2366 ? 146.165 131.771 148.348 1.00 69.65  ? 2366 GLU A OE2   1 
ATOM   8346  N  N     . ASP A 1 2367 ? 143.651 129.662 142.175 1.00 49.56  ? 2367 ASP A N     1 
ATOM   8347  C  CA    . ASP A 1 2367 ? 142.683 128.928 141.371 1.00 47.87  ? 2367 ASP A CA    1 
ATOM   8348  C  C     . ASP A 1 2367 ? 143.336 127.883 140.478 1.00 48.37  ? 2367 ASP A C     1 
ATOM   8349  O  O     . ASP A 1 2367 ? 142.636 126.996 139.978 1.00 50.02  ? 2367 ASP A O     1 
ATOM   8350  C  CB    . ASP A 1 2367 ? 141.871 129.903 140.519 1.00 53.08  ? 2367 ASP A CB    1 
ATOM   8351  C  CG    . ASP A 1 2367 ? 141.171 130.955 141.351 1.00 63.95  ? 2367 ASP A CG    1 
ATOM   8352  O  OD1   . ASP A 1 2367 ? 141.823 131.955 141.718 1.00 60.69  ? 2367 ASP A OD1   1 
ATOM   8353  O  OD2   . ASP A 1 2367 ? 139.969 130.781 141.642 1.00 69.39  ? 2367 ASP A OD2   1 
ATOM   8354  N  N     . VAL A 1 2368 ? 144.649 127.974 140.262 1.00 44.85  ? 2368 VAL A N     1 
ATOM   8355  C  CA    . VAL A 1 2368 ? 145.362 126.959 139.492 1.00 36.97  ? 2368 VAL A CA    1 
ATOM   8356  C  C     . VAL A 1 2368 ? 145.258 125.603 140.176 1.00 40.06  ? 2368 VAL A C     1 
ATOM   8357  O  O     . VAL A 1 2368 ? 144.999 124.582 139.528 1.00 42.42  ? 2368 VAL A O     1 
ATOM   8358  C  CB    . VAL A 1 2368 ? 146.828 127.387 139.294 1.00 33.36  ? 2368 VAL A CB    1 
ATOM   8359  C  CG1   . VAL A 1 2368 ? 147.663 126.235 138.802 1.00 38.09  ? 2368 VAL A CG1   1 
ATOM   8360  C  CG2   . VAL A 1 2368 ? 146.909 128.552 138.329 1.00 35.87  ? 2368 VAL A CG2   1 
ATOM   8361  N  N     . LEU A 1 2369 ? 145.446 125.574 141.491 1.00 42.46  ? 2369 LEU A N     1 
ATOM   8362  C  CA    . LEU A 1 2369 ? 145.368 124.343 142.265 1.00 39.96  ? 2369 LEU A CA    1 
ATOM   8363  C  C     . LEU A 1 2369 ? 143.981 124.211 142.878 1.00 43.39  ? 2369 LEU A C     1 
ATOM   8364  O  O     . LEU A 1 2369 ? 143.569 125.051 143.683 1.00 46.64  ? 2369 LEU A O     1 
ATOM   8365  C  CB    . LEU A 1 2369 ? 146.432 124.334 143.361 1.00 32.33  ? 2369 LEU A CB    1 
ATOM   8366  C  CG    . LEU A 1 2369 ? 146.830 122.973 143.925 1.00 29.83  ? 2369 LEU A CG    1 
ATOM   8367  C  CD1   . LEU A 1 2369 ? 147.609 122.202 142.893 1.00 33.39  ? 2369 LEU A CD1   1 
ATOM   8368  C  CD2   . LEU A 1 2369 ? 147.643 123.143 145.191 1.00 29.97  ? 2369 LEU A CD2   1 
ATOM   8369  N  N     . SER A 1 2370 ? 143.272 123.153 142.505 1.00 37.70  ? 2370 SER A N     1 
ATOM   8370  C  CA    . SER A 1 2370 ? 141.918 122.912 142.977 1.00 35.60  ? 2370 SER A CA    1 
ATOM   8371  C  C     . SER A 1 2370 ? 141.934 121.967 144.171 1.00 42.57  ? 2370 SER A C     1 
ATOM   8372  O  O     . SER A 1 2370 ? 142.848 121.156 144.331 1.00 46.23  ? 2370 SER A O     1 
ATOM   8373  C  CB    . SER A 1 2370 ? 141.052 122.328 141.861 1.00 37.29  ? 2370 SER A CB    1 
ATOM   8374  O  OG    . SER A 1 2370 ? 139.736 122.077 142.318 1.00 52.85  ? 2370 SER A OG    1 
ATOM   8375  N  N     . THR A 1 2371 ? 140.909 122.086 145.019 1.00 45.66  ? 2371 THR A N     1 
ATOM   8376  C  CA    . THR A 1 2371 ? 140.805 121.202 146.176 1.00 39.50  ? 2371 THR A CA    1 
ATOM   8377  C  C     . THR A 1 2371 ? 140.603 119.758 145.743 1.00 40.47  ? 2371 THR A C     1 
ATOM   8378  O  O     . THR A 1 2371 ? 141.090 118.831 146.400 1.00 46.99  ? 2371 THR A O     1 
ATOM   8379  C  CB    . THR A 1 2371 ? 139.661 121.646 147.084 1.00 46.40  ? 2371 THR A CB    1 
ATOM   8380  O  OG1   . THR A 1 2371 ? 138.413 121.239 146.510 1.00 61.72  ? 2371 THR A OG1   1 
ATOM   8381  C  CG2   . THR A 1 2371 ? 139.663 123.154 147.242 1.00 52.59  ? 2371 THR A CG2   1 
ATOM   8382  N  N     . ASP A 1 2372 ? 139.880 119.546 144.642 1.00 39.92  ? 2372 ASP A N     1 
ATOM   8383  C  CA    . ASP A 1 2372 ? 139.720 118.197 144.112 1.00 42.08  ? 2372 ASP A CA    1 
ATOM   8384  C  C     . ASP A 1 2372 ? 141.059 117.623 143.674 1.00 40.43  ? 2372 ASP A C     1 
ATOM   8385  O  O     . ASP A 1 2372 ? 141.306 116.422 143.816 1.00 41.21  ? 2372 ASP A O     1 
ATOM   8386  C  CB    . ASP A 1 2372 ? 138.733 118.206 142.948 1.00 52.70  ? 2372 ASP A CB    1 
ATOM   8387  C  CG    . ASP A 1 2372 ? 137.446 118.928 143.285 1.00 73.26  ? 2372 ASP A CG    1 
ATOM   8388  O  OD1   . ASP A 1 2372 ? 137.142 119.945 142.626 1.00 73.07  ? 2372 ASP A OD1   1 
ATOM   8389  O  OD2   . ASP A 1 2372 ? 136.743 118.484 144.215 1.00 78.69  ? 2372 ASP A OD2   1 
ATOM   8390  N  N     . MET A 1 2373 ? 141.937 118.471 143.140 1.00 40.00  ? 2373 MET A N     1 
ATOM   8391  C  CA    . MET A 1 2373 ? 143.261 118.016 142.733 1.00 33.48  ? 2373 MET A CA    1 
ATOM   8392  C  C     . MET A 1 2373 ? 144.065 117.536 143.935 1.00 35.70  ? 2373 MET A C     1 
ATOM   8393  O  O     . MET A 1 2373 ? 144.723 116.490 143.879 1.00 41.02  ? 2373 MET A O     1 
ATOM   8394  C  CB    . MET A 1 2373 ? 143.984 119.152 142.013 1.00 34.98  ? 2373 MET A CB    1 
ATOM   8395  C  CG    . MET A 1 2373 ? 143.897 119.075 140.505 1.00 37.05  ? 2373 MET A CG    1 
ATOM   8396  S  SD    . MET A 1 2373 ? 144.417 120.605 139.716 1.00 54.43  ? 2373 MET A SD    1 
ATOM   8397  C  CE    . MET A 1 2373 ? 146.165 120.593 140.061 1.00 37.69  ? 2373 MET A CE    1 
ATOM   8398  N  N     . ILE A 1 2374 ? 144.003 118.279 145.041 1.00 35.41  ? 2374 ILE A N     1 
ATOM   8399  C  CA    . ILE A 1 2374 ? 144.720 117.885 146.250 1.00 31.09  ? 2374 ILE A CA    1 
ATOM   8400  C  C     . ILE A 1 2374 ? 144.111 116.625 146.850 1.00 34.89  ? 2374 ILE A C     1 
ATOM   8401  O  O     . ILE A 1 2374 ? 144.829 115.757 147.359 1.00 42.07  ? 2374 ILE A O     1 
ATOM   8402  C  CB    . ILE A 1 2374 ? 144.734 119.046 147.259 1.00 25.67  ? 2374 ILE A CB    1 
ATOM   8403  C  CG1   . ILE A 1 2374 ? 145.091 120.351 146.553 1.00 27.85  ? 2374 ILE A CG1   1 
ATOM   8404  C  CG2   . ILE A 1 2374 ? 145.724 118.767 148.368 1.00 35.13  ? 2374 ILE A CG2   1 
ATOM   8405  C  CD1   . ILE A 1 2374 ? 144.989 121.562 147.432 1.00 27.60  ? 2374 ILE A CD1   1 
ATOM   8406  N  N     . PHE A 1 2375 ? 142.782 116.505 146.811 1.00 30.42  ? 2375 PHE A N     1 
ATOM   8407  C  CA    . PHE A 1 2375 ? 142.138 115.290 147.301 1.00 28.76  ? 2375 PHE A CA    1 
ATOM   8408  C  C     . PHE A 1 2375 ? 142.562 114.078 146.483 1.00 37.42  ? 2375 PHE A C     1 
ATOM   8409  O  O     . PHE A 1 2375 ? 142.840 113.008 147.039 1.00 44.51  ? 2375 PHE A O     1 
ATOM   8410  C  CB    . PHE A 1 2375 ? 140.620 115.448 147.265 1.00 34.70  ? 2375 PHE A CB    1 
ATOM   8411  C  CG    . PHE A 1 2375 ? 140.087 116.445 148.253 1.00 36.76  ? 2375 PHE A CG    1 
ATOM   8412  C  CD1   . PHE A 1 2375 ? 140.893 116.954 149.253 1.00 37.77  ? 2375 PHE A CD1   1 
ATOM   8413  C  CD2   . PHE A 1 2375 ? 138.777 116.879 148.172 1.00 41.77  ? 2375 PHE A CD2   1 
ATOM   8414  C  CE1   . PHE A 1 2375 ? 140.402 117.870 150.154 1.00 38.04  ? 2375 PHE A CE1   1 
ATOM   8415  C  CE2   . PHE A 1 2375 ? 138.283 117.796 149.071 1.00 44.54  ? 2375 PHE A CE2   1 
ATOM   8416  C  CZ    . PHE A 1 2375 ? 139.098 118.292 150.062 1.00 41.92  ? 2375 PHE A CZ    1 
ATOM   8417  N  N     . ASN A 1 2376 ? 142.613 114.227 145.157 1.00 39.37  ? 2376 ASN A N     1 
ATOM   8418  C  CA    . ASN A 1 2376 ? 143.062 113.137 144.299 1.00 35.56  ? 2376 ASN A CA    1 
ATOM   8419  C  C     . ASN A 1 2376 ? 144.514 112.781 144.579 1.00 35.15  ? 2376 ASN A C     1 
ATOM   8420  O  O     . ASN A 1 2376 ? 144.876 111.601 144.595 1.00 40.19  ? 2376 ASN A O     1 
ATOM   8421  C  CB    . ASN A 1 2376 ? 142.879 113.512 142.829 1.00 37.78  ? 2376 ASN A CB    1 
ATOM   8422  C  CG    . ASN A 1 2376 ? 141.425 113.688 142.450 1.00 50.81  ? 2376 ASN A CG    1 
ATOM   8423  O  OD1   . ASN A 1 2376 ? 140.530 113.526 143.279 1.00 55.13  ? 2376 ASN A OD1   1 
ATOM   8424  N  ND2   . ASN A 1 2376 ? 141.180 114.023 141.189 1.00 48.17  ? 2376 ASN A ND2   1 
ATOM   8425  N  N     . ASN A 1 2377 ? 145.364 113.789 144.791 1.00 35.11  ? 2377 ASN A N     1 
ATOM   8426  C  CA    . ASN A 1 2377 ? 146.758 113.513 145.124 1.00 37.83  ? 2377 ASN A CA    1 
ATOM   8427  C  C     . ASN A 1 2377 ? 146.866 112.739 146.431 1.00 40.04  ? 2377 ASN A C     1 
ATOM   8428  O  O     . ASN A 1 2377 ? 147.624 111.767 146.528 1.00 41.03  ? 2377 ASN A O     1 
ATOM   8429  C  CB    . ASN A 1 2377 ? 147.552 114.814 145.212 1.00 37.29  ? 2377 ASN A CB    1 
ATOM   8430  C  CG    . ASN A 1 2377 ? 149.045 114.576 145.266 1.00 39.26  ? 2377 ASN A CG    1 
ATOM   8431  O  OD1   . ASN A 1 2377 ? 149.510 113.448 145.122 1.00 44.30  ? 2377 ASN A OD1   1 
ATOM   8432  N  ND2   . ASN A 1 2377 ? 149.806 115.636 145.485 1.00 39.39  ? 2377 ASN A ND2   1 
ATOM   8433  N  N     . PHE A 1 2378 ? 146.115 113.160 147.450 1.00 36.77  ? 2378 PHE A N     1 
ATOM   8434  C  CA    . PHE A 1 2378 ? 146.153 112.470 148.734 1.00 31.52  ? 2378 PHE A CA    1 
ATOM   8435  C  C     . PHE A 1 2378 ? 145.689 111.028 148.592 1.00 33.50  ? 2378 PHE A C     1 
ATOM   8436  O  O     . PHE A 1 2378 ? 146.317 110.107 149.126 1.00 41.28  ? 2378 PHE A O     1 
ATOM   8437  C  CB    . PHE A 1 2378 ? 145.288 113.207 149.755 1.00 31.99  ? 2378 PHE A CB    1 
ATOM   8438  C  CG    . PHE A 1 2378 ? 144.859 112.353 150.916 1.00 37.10  ? 2378 PHE A CG    1 
ATOM   8439  C  CD1   . PHE A 1 2378 ? 145.795 111.816 151.784 1.00 37.20  ? 2378 PHE A CD1   1 
ATOM   8440  C  CD2   . PHE A 1 2378 ? 143.521 112.083 151.136 1.00 38.69  ? 2378 PHE A CD2   1 
ATOM   8441  C  CE1   . PHE A 1 2378 ? 145.403 111.030 152.847 1.00 35.30  ? 2378 PHE A CE1   1 
ATOM   8442  C  CE2   . PHE A 1 2378 ? 143.126 111.298 152.199 1.00 37.01  ? 2378 PHE A CE2   1 
ATOM   8443  C  CZ    . PHE A 1 2378 ? 144.069 110.771 153.053 1.00 33.35  ? 2378 PHE A CZ    1 
ATOM   8444  N  N     . LEU A 1 2379 ? 144.589 110.814 147.870 1.00 33.51  ? 2379 LEU A N     1 
ATOM   8445  C  CA    . LEU A 1 2379 ? 144.066 109.462 147.710 1.00 32.57  ? 2379 LEU A CA    1 
ATOM   8446  C  C     . LEU A 1 2379 ? 145.028 108.581 146.922 1.00 36.43  ? 2379 LEU A C     1 
ATOM   8447  O  O     . LEU A 1 2379 ? 145.227 107.411 147.267 1.00 42.09  ? 2379 LEU A O     1 
ATOM   8448  C  CB    . LEU A 1 2379 ? 142.694 109.517 147.042 1.00 34.58  ? 2379 LEU A CB    1 
ATOM   8449  C  CG    . LEU A 1 2379 ? 141.594 110.092 147.936 1.00 36.88  ? 2379 LEU A CG    1 
ATOM   8450  C  CD1   . LEU A 1 2379 ? 140.283 110.193 147.189 1.00 47.96  ? 2379 LEU A CD1   1 
ATOM   8451  C  CD2   . LEU A 1 2379 ? 141.427 109.245 149.183 1.00 38.37  ? 2379 LEU A CD2   1 
ATOM   8452  N  N     . ALA A 1 2380 ? 145.643 109.123 145.868 1.00 35.00  ? 2380 ALA A N     1 
ATOM   8453  C  CA    . ALA A 1 2380 ? 146.599 108.345 145.087 1.00 34.85  ? 2380 ALA A CA    1 
ATOM   8454  C  C     . ALA A 1 2380 ? 147.831 107.991 145.909 1.00 41.38  ? 2380 ALA A C     1 
ATOM   8455  O  O     . ALA A 1 2380 ? 148.314 106.854 145.856 1.00 48.72  ? 2380 ALA A O     1 
ATOM   8456  C  CB    . ALA A 1 2380 ? 146.996 109.115 143.830 1.00 34.51  ? 2380 ALA A CB    1 
ATOM   8457  N  N     . ARG A 1 2381 ? 148.357 108.952 146.674 1.00 38.70  ? 2381 ARG A N     1 
ATOM   8458  C  CA    . ARG A 1 2381 ? 149.506 108.666 147.525 1.00 37.17  ? 2381 ARG A CA    1 
ATOM   8459  C  C     . ARG A 1 2381 ? 149.162 107.628 148.583 1.00 42.91  ? 2381 ARG A C     1 
ATOM   8460  O  O     . ARG A 1 2381 ? 149.969 106.737 148.874 1.00 51.76  ? 2381 ARG A O     1 
ATOM   8461  C  CB    . ARG A 1 2381 ? 150.009 109.950 148.183 1.00 34.62  ? 2381 ARG A CB    1 
ATOM   8462  C  CG    . ARG A 1 2381 ? 150.586 110.962 147.218 1.00 38.34  ? 2381 ARG A CG    1 
ATOM   8463  C  CD    . ARG A 1 2381 ? 151.078 112.195 147.953 1.00 40.02  ? 2381 ARG A CD    1 
ATOM   8464  N  NE    . ARG A 1 2381 ? 152.170 111.898 148.871 1.00 42.92  ? 2381 ARG A NE    1 
ATOM   8465  C  CZ    . ARG A 1 2381 ? 153.408 111.605 148.499 1.00 44.27  ? 2381 ARG A CZ    1 
ATOM   8466  N  NH1   . ARG A 1 2381 ? 153.758 111.574 147.225 1.00 50.22  ? 2381 ARG A NH1   1 
ATOM   8467  N  NH2   . ARG A 1 2381 ? 154.319 111.342 149.430 1.00 42.92  ? 2381 ARG A NH2   1 
ATOM   8468  N  N     . LEU A 1 2382 ? 147.970 107.727 149.173 1.00 38.86  ? 2382 LEU A N     1 
ATOM   8469  C  CA    . LEU A 1 2382 ? 147.559 106.756 150.179 1.00 41.14  ? 2382 LEU A CA    1 
ATOM   8470  C  C     . LEU A 1 2382 ? 147.414 105.365 149.575 1.00 47.45  ? 2382 LEU A C     1 
ATOM   8471  O  O     . LEU A 1 2382 ? 147.818 104.371 150.187 1.00 56.30  ? 2382 LEU A O     1 
ATOM   8472  C  CB    . LEU A 1 2382 ? 146.250 107.205 150.826 1.00 40.27  ? 2382 LEU A CB    1 
ATOM   8473  C  CG    . LEU A 1 2382 ? 145.767 106.425 152.046 1.00 44.73  ? 2382 LEU A CG    1 
ATOM   8474  C  CD1   . LEU A 1 2382 ? 146.588 106.790 153.268 1.00 50.41  ? 2382 LEU A CD1   1 
ATOM   8475  C  CD2   . LEU A 1 2382 ? 144.302 106.703 152.290 1.00 44.99  ? 2382 LEU A CD2   1 
ATOM   8476  N  N     . ARG A 1 2383 ? 146.847 105.275 148.372 1.00 43.65  ? 2383 ARG A N     1 
ATOM   8477  C  CA    . ARG A 1 2383 ? 146.672 103.982 147.724 1.00 49.30  ? 2383 ARG A CA    1 
ATOM   8478  C  C     . ARG A 1 2383 ? 147.979 103.410 147.193 1.00 53.57  ? 2383 ARG A C     1 
ATOM   8479  O  O     . ARG A 1 2383 ? 148.062 102.199 146.966 1.00 58.85  ? 2383 ARG A O     1 
ATOM   8480  C  CB    . ARG A 1 2383 ? 145.668 104.104 146.579 1.00 47.11  ? 2383 ARG A CB    1 
ATOM   8481  C  CG    . ARG A 1 2383 ? 144.220 103.970 147.000 1.00 42.75  ? 2383 ARG A CG    1 
ATOM   8482  C  CD    . ARG A 1 2383 ? 143.316 103.834 145.792 1.00 46.58  ? 2383 ARG A CD    1 
ATOM   8483  N  NE    . ARG A 1 2383 ? 141.930 104.156 146.108 1.00 60.67  ? 2383 ARG A NE    1 
ATOM   8484  C  CZ    . ARG A 1 2383 ? 141.343 105.306 145.809 1.00 59.55  ? 2383 ARG A CZ    1 
ATOM   8485  N  NH1   . ARG A 1 2383 ? 141.994 106.272 145.183 1.00 53.22  ? 2383 ARG A NH1   1 
ATOM   8486  N  NH2   . ARG A 1 2383 ? 140.070 105.491 146.145 1.00 54.51  ? 2383 ARG A NH2   1 
ATOM   8487  N  N     . SER A 1 2384 ? 148.997 104.245 146.983 1.00 51.64  ? 2384 SER A N     1 
ATOM   8488  C  CA    . SER A 1 2384 ? 150.238 103.804 146.356 1.00 50.76  ? 2384 SER A CA    1 
ATOM   8489  C  C     . SER A 1 2384 ? 151.384 103.655 147.352 1.00 52.54  ? 2384 SER A C     1 
ATOM   8490  O  O     . SER A 1 2384 ? 152.025 102.602 147.408 1.00 65.20  ? 2384 SER A O     1 
ATOM   8491  C  CB    . SER A 1 2384 ? 150.627 104.782 145.241 1.00 56.86  ? 2384 SER A CB    1 
ATOM   8492  O  OG    . SER A 1 2384 ? 149.644 104.807 144.220 1.00 63.55  ? 2384 SER A OG    1 
ATOM   8493  N  N     . ILE A 1 2385 ? 151.664 104.695 148.132 1.00 52.62  ? 2385 ILE A N     1 
ATOM   8494  C  CA    . ILE A 1 2385 ? 152.814 104.698 149.034 1.00 56.78  ? 2385 ILE A CA    1 
ATOM   8495  C  C     . ILE A 1 2385 ? 152.453 104.043 150.362 1.00 64.01  ? 2385 ILE A C     1 
ATOM   8496  O  O     . ILE A 1 2385 ? 151.558 104.530 151.067 1.00 66.09  ? 2385 ILE A O     1 
ATOM   8497  C  CB    . ILE A 1 2385 ? 153.334 106.124 149.266 1.00 50.83  ? 2385 ILE A CB    1 
ATOM   8498  C  CG1   . ILE A 1 2385 ? 153.837 106.731 147.958 1.00 51.89  ? 2385 ILE A CG1   1 
ATOM   8499  C  CG2   . ILE A 1 2385 ? 154.435 106.124 150.313 1.00 57.99  ? 2385 ILE A CG2   1 
ATOM   8500  C  CD1   . ILE A 1 2385 ? 154.122 108.207 148.055 1.00 49.26  ? 2385 ILE A CD1   1 
ATOM   8501  N  N     . PRO A 1 2386 ? 153.117 102.953 150.747 1.00 65.47  ? 2386 PRO A N     1 
ATOM   8502  C  CA    . PRO A 1 2386 ? 152.883 102.385 152.079 1.00 66.14  ? 2386 PRO A CA    1 
ATOM   8503  C  C     . PRO A 1 2386 ? 153.497 103.262 153.158 1.00 71.81  ? 2386 PRO A C     1 
ATOM   8504  O  O     . PRO A 1 2386 ? 154.620 103.752 153.021 1.00 78.66  ? 2386 PRO A O     1 
ATOM   8505  C  CB    . PRO A 1 2386 ? 153.572 101.015 152.013 1.00 78.58  ? 2386 PRO A CB    1 
ATOM   8506  C  CG    . PRO A 1 2386 ? 153.870 100.783 150.557 1.00 79.78  ? 2386 PRO A CG    1 
ATOM   8507  C  CD    . PRO A 1 2386 ? 154.050 102.136 149.959 1.00 72.36  ? 2386 PRO A CD    1 
ATOM   8508  N  N     . LEU A 1 2387 ? 152.746 103.458 154.243 1.00 72.17  ? 2387 LEU A N     1 
ATOM   8509  C  CA    . LEU A 1 2387 ? 153.200 104.351 155.303 1.00 76.58  ? 2387 LEU A CA    1 
ATOM   8510  C  C     . LEU A 1 2387 ? 154.307 103.730 156.146 1.00 88.23  ? 2387 LEU A C     1 
ATOM   8511  O  O     . LEU A 1 2387 ? 155.283 104.408 156.485 1.00 92.42  ? 2387 LEU A O     1 
ATOM   8512  C  CB    . LEU A 1 2387 ? 152.025 104.749 156.192 1.00 66.06  ? 2387 LEU A CB    1 
ATOM   8513  C  CG    . LEU A 1 2387 ? 150.903 105.527 155.511 1.00 63.87  ? 2387 LEU A CG    1 
ATOM   8514  C  CD1   . LEU A 1 2387 ? 150.016 106.142 156.560 1.00 56.91  ? 2387 LEU A CD1   1 
ATOM   8515  C  CD2   . LEU A 1 2387 ? 151.467 106.598 154.593 1.00 64.68  ? 2387 LEU A CD2   1 
ATOM   8516  N  N     . ASP A 1 2388 ? 154.172 102.450 156.500 1.00 92.55  ? 2388 ASP A N     1 
ATOM   8517  C  CA    . ASP A 1 2388 ? 155.159 101.820 157.372 1.00 98.21  ? 2388 ASP A CA    1 
ATOM   8518  C  C     . ASP A 1 2388 ? 156.521 101.721 156.697 1.00 105.61 ? 2388 ASP A C     1 
ATOM   8519  O  O     . ASP A 1 2388 ? 157.556 101.909 157.347 1.00 112.07 ? 2388 ASP A O     1 
ATOM   8520  C  CB    . ASP A 1 2388 ? 154.672 100.438 157.811 1.00 103.99 ? 2388 ASP A CB    1 
ATOM   8521  C  CG    . ASP A 1 2388 ? 154.458 99.493  156.646 1.00 104.63 ? 2388 ASP A CG    1 
ATOM   8522  O  OD1   . ASP A 1 2388 ? 154.505 99.949  155.485 1.00 103.98 ? 2388 ASP A OD1   1 
ATOM   8523  O  OD2   . ASP A 1 2388 ? 154.240 98.289  156.891 1.00 107.29 ? 2388 ASP A OD2   1 
ATOM   8524  N  N     . GLU A 1 2389 ? 156.543 101.426 155.400 1.00 108.20 ? 2389 GLU A N     1 
ATOM   8525  C  CA    . GLU A 1 2389 ? 157.805 101.254 154.696 1.00 114.30 ? 2389 GLU A CA    1 
ATOM   8526  C  C     . GLU A 1 2389 ? 158.536 102.585 154.588 1.00 118.42 ? 2389 GLU A C     1 
ATOM   8527  O  O     . GLU A 1 2389 ? 157.953 103.598 154.190 1.00 114.33 ? 2389 GLU A O     1 
ATOM   8528  C  CB    . GLU A 1 2389 ? 157.561 100.666 153.305 1.00 119.33 ? 2389 GLU A CB    1 
ATOM   8529  C  CG    . GLU A 1 2389 ? 156.796 99.347  153.303 1.00 122.00 ? 2389 GLU A CG    1 
ATOM   8530  C  CD    . GLU A 1 2389 ? 157.598 98.185  153.866 1.00 128.68 ? 2389 GLU A CD    1 
ATOM   8531  O  OE1   . GLU A 1 2389 ? 158.819 98.340  154.084 1.00 134.43 ? 2389 GLU A OE1   1 
ATOM   8532  O  OE2   . GLU A 1 2389 ? 157.003 97.110  154.092 1.00 122.54 ? 2389 GLU A OE2   1 
ATOM   8533  N  N     . GLY A 1 2390 ? 159.817 102.580 154.947 1.00 124.61 ? 2390 GLY A N     1 
ATOM   8534  C  CA    . GLY A 1 2390 ? 160.631 103.776 154.878 1.00 130.10 ? 2390 GLY A CA    1 
ATOM   8535  C  C     . GLY A 1 2390 ? 161.552 103.774 153.677 1.00 138.07 ? 2390 GLY A C     1 
ATOM   8536  O  O     . GLY A 1 2390 ? 161.122 104.072 152.559 1.00 139.35 ? 2390 GLY A O     1 
ATOM   8537  N  N     . GLU A 1 2391 ? 162.827 103.446 153.899 1.00 139.82 ? 2391 GLU A N     1 
ATOM   8538  C  CA    . GLU A 1 2391 ? 163.768 103.357 152.788 1.00 142.94 ? 2391 GLU A CA    1 
ATOM   8539  C  C     . GLU A 1 2391 ? 163.370 102.252 151.816 1.00 145.68 ? 2391 GLU A C     1 
ATOM   8540  O  O     . GLU A 1 2391 ? 163.453 102.430 150.595 1.00 146.31 ? 2391 GLU A O     1 
ATOM   8541  C  CB    . GLU A 1 2391 ? 165.185 103.134 153.316 1.00 139.20 ? 2391 GLU A CB    1 
ATOM   8542  C  CG    . GLU A 1 2391 ? 165.306 102.017 154.341 1.00 140.58 ? 2391 GLU A CG    1 
ATOM   8543  C  CD    . GLU A 1 2391 ? 166.733 101.807 154.807 1.00 139.17 ? 2391 GLU A CD    1 
ATOM   8544  O  OE1   . GLU A 1 2391 ? 167.628 102.539 154.336 1.00 135.97 ? 2391 GLU A OE1   1 
ATOM   8545  O  OE2   . GLU A 1 2391 ? 166.959 100.908 155.644 1.00 138.51 ? 2391 GLU A OE2   1 
ATOM   8546  N  N     . ASP A 1 2392 ? 162.936 101.107 152.336 1.00 145.91 ? 2392 ASP A N     1 
ATOM   8547  C  CA    . ASP A 1 2392 ? 162.456 100.034 151.480 1.00 147.70 ? 2392 ASP A CA    1 
ATOM   8548  C  C     . ASP A 1 2392 ? 161.115 100.412 150.861 1.00 147.35 ? 2392 ASP A C     1 
ATOM   8549  O  O     . ASP A 1 2392 ? 160.306 101.124 151.463 1.00 142.40 ? 2392 ASP A O     1 
ATOM   8550  C  CB    . ASP A 1 2392 ? 162.328 98.733  152.270 1.00 148.05 ? 2392 ASP A CB    1 
ATOM   8551  C  CG    . ASP A 1 2392 ? 162.316 97.507  151.376 1.00 150.56 ? 2392 ASP A CG    1 
ATOM   8552  O  OD1   . ASP A 1 2392 ? 162.412 97.669  150.142 1.00 150.30 ? 2392 ASP A OD1   1 
ATOM   8553  O  OD2   . ASP A 1 2392 ? 162.209 96.382  151.908 1.00 147.56 ? 2392 ASP A OD2   1 
ATOM   8554  N  N     . GLU A 1 2393 ? 160.892 99.934  149.638 1.00 150.46 ? 2393 GLU A N     1 
ATOM   8555  C  CA    . GLU A 1 2393 ? 159.725 100.248 148.816 1.00 149.04 ? 2393 GLU A CA    1 
ATOM   8556  C  C     . GLU A 1 2393 ? 159.607 101.733 148.492 1.00 150.40 ? 2393 GLU A C     1 
ATOM   8557  O  O     . GLU A 1 2393 ? 158.570 102.169 147.979 1.00 151.52 ? 2393 GLU A O     1 
ATOM   8558  C  CB    . GLU A 1 2393 ? 158.421 99.749  149.458 1.00 145.84 ? 2393 GLU A CB    1 
ATOM   8559  C  CG    . GLU A 1 2393 ? 158.143 98.269  149.235 1.00 145.82 ? 2393 GLU A CG    1 
ATOM   8560  C  CD    . GLU A 1 2393 ? 158.768 97.388  150.296 1.00 146.31 ? 2393 GLU A CD    1 
ATOM   8561  O  OE1   . GLU A 1 2393 ? 159.322 97.934  151.271 1.00 147.50 ? 2393 GLU A OE1   1 
ATOM   8562  O  OE2   . GLU A 1 2393 ? 158.705 96.149  150.155 1.00 144.61 ? 2393 GLU A OE2   1 
ATOM   8563  N  N     . ALA A 1 2394 ? 160.640 102.524 148.779 1.00 148.27 ? 2394 ALA A N     1 
ATOM   8564  C  CA    . ALA A 1 2394 ? 160.685 103.915 148.348 1.00 148.05 ? 2394 ALA A CA    1 
ATOM   8565  C  C     . ALA A 1 2394 ? 161.410 104.052 147.015 1.00 151.82 ? 2394 ALA A C     1 
ATOM   8566  O  O     . ALA A 1 2394 ? 160.903 104.691 146.088 1.00 149.74 ? 2394 ALA A O     1 
ATOM   8567  C  CB    . ALA A 1 2394 ? 161.359 104.783 149.414 1.00 140.46 ? 2394 ALA A CB    1 
ATOM   8568  N  N     . GLN A 1 2395 ? 162.599 103.454 146.907 1.00 152.82 ? 2395 GLN A N     1 
ATOM   8569  C  CA    . GLN A 1 2395 ? 163.280 103.369 145.622 1.00 150.95 ? 2395 GLN A CA    1 
ATOM   8570  C  C     . GLN A 1 2395 ? 162.643 102.330 144.712 1.00 152.42 ? 2395 GLN A C     1 
ATOM   8571  O  O     . GLN A 1 2395 ? 162.825 102.394 143.492 1.00 153.84 ? 2395 GLN A O     1 
ATOM   8572  C  CB    . GLN A 1 2395 ? 164.760 103.046 145.830 1.00 148.76 ? 2395 GLN A CB    1 
ATOM   8573  C  CG    . GLN A 1 2395 ? 165.523 104.108 146.602 1.00 148.96 ? 2395 GLN A CG    1 
ATOM   8574  C  CD    . GLN A 1 2395 ? 165.548 103.834 148.093 1.00 145.30 ? 2395 GLN A CD    1 
ATOM   8575  O  OE1   . GLN A 1 2395 ? 165.345 102.702 148.530 1.00 142.01 ? 2395 GLN A OE1   1 
ATOM   8576  N  NE2   . GLN A 1 2395 ? 165.795 104.873 148.882 1.00 143.86 ? 2395 GLN A NE2   1 
ATOM   8577  N  N     . ARG A 1 2396 ? 161.903 101.374 145.280 1.00 152.02 ? 2396 ARG A N     1 
ATOM   8578  C  CA    . ARG A 1 2396 ? 161.200 100.396 144.458 1.00 153.15 ? 2396 ARG A CA    1 
ATOM   8579  C  C     . ARG A 1 2396 ? 160.065 101.039 143.674 1.00 152.83 ? 2396 ARG A C     1 
ATOM   8580  O  O     . ARG A 1 2396 ? 159.657 100.512 142.633 1.00 153.28 ? 2396 ARG A O     1 
ATOM   8581  C  CB    . ARG A 1 2396 ? 160.676 99.255  145.331 1.00 151.59 ? 2396 ARG A CB    1 
ATOM   8582  C  CG    . ARG A 1 2396 ? 161.744 98.615  146.205 1.00 150.58 ? 2396 ARG A CG    1 
ATOM   8583  C  CD    . ARG A 1 2396 ? 161.219 97.388  146.932 1.00 154.05 ? 2396 ARG A CD    1 
ATOM   8584  N  NE    . ARG A 1 2396 ? 160.929 96.292  146.015 1.00 157.37 ? 2396 ARG A NE    1 
ATOM   8585  C  CZ    . ARG A 1 2396 ? 159.880 95.488  146.116 1.00 156.10 ? 2396 ARG A CZ    1 
ATOM   8586  N  NH1   . ARG A 1 2396 ? 159.001 95.618  147.097 1.00 155.78 ? 2396 ARG A NH1   1 
ATOM   8587  N  NH2   . ARG A 1 2396 ? 159.710 94.526  145.214 1.00 154.04 ? 2396 ARG A NH2   1 
ATOM   8588  N  N     . ARG A 1 2397 ? 159.538 102.167 144.159 1.00 151.41 ? 2397 ARG A N     1 
ATOM   8589  C  CA    . ARG A 1 2397 ? 158.561 102.918 143.378 1.00 152.13 ? 2397 ARG A CA    1 
ATOM   8590  C  C     . ARG A 1 2397 ? 159.178 103.430 142.083 1.00 151.99 ? 2397 ARG A C     1 
ATOM   8591  O  O     . ARG A 1 2397 ? 158.553 103.365 141.018 1.00 151.57 ? 2397 ARG A O     1 
ATOM   8592  C  CB    . ARG A 1 2397 ? 158.010 104.082 144.203 1.00 149.49 ? 2397 ARG A CB    1 
ATOM   8593  C  CG    . ARG A 1 2397 ? 157.177 103.677 145.415 1.00 143.94 ? 2397 ARG A CG    1 
ATOM   8594  C  CD    . ARG A 1 2397 ? 155.791 103.185 145.017 1.00 136.05 ? 2397 ARG A CD    1 
ATOM   8595  N  NE    . ARG A 1 2397 ? 155.778 101.771 144.660 1.00 147.71 ? 2397 ARG A NE    1 
ATOM   8596  C  CZ    . ARG A 1 2397 ? 155.932 100.774 145.521 1.00 149.69 ? 2397 ARG A CZ    1 
ATOM   8597  N  NH1   . ARG A 1 2397 ? 156.086 100.994 146.816 1.00 141.15 ? 2397 ARG A NH1   1 
ATOM   8598  N  NH2   . ARG A 1 2397 ? 155.924 99.522  145.071 1.00 152.97 ? 2397 ARG A NH2   1 
ATOM   8599  N  N     . ARG A 1 2398 ? 160.408 103.945 142.157 1.00 153.39 ? 2398 ARG A N     1 
ATOM   8600  C  CA    . ARG A 1 2398 ? 161.089 104.420 140.957 1.00 156.23 ? 2398 ARG A CA    1 
ATOM   8601  C  C     . ARG A 1 2398 ? 161.554 103.259 140.087 1.00 157.30 ? 2398 ARG A C     1 
ATOM   8602  O  O     . ARG A 1 2398 ? 161.499 103.338 138.854 1.00 156.97 ? 2398 ARG A O     1 
ATOM   8603  C  CB    . ARG A 1 2398 ? 162.270 105.308 141.348 1.00 155.01 ? 2398 ARG A CB    1 
ATOM   8604  C  CG    . ARG A 1 2398 ? 163.131 105.761 140.180 1.00 153.92 ? 2398 ARG A CG    1 
ATOM   8605  C  CD    . ARG A 1 2398 ? 164.505 106.204 140.653 1.00 153.03 ? 2398 ARG A CD    1 
ATOM   8606  N  NE    . ARG A 1 2398 ? 165.251 105.106 141.256 1.00 157.01 ? 2398 ARG A NE    1 
ATOM   8607  C  CZ    . ARG A 1 2398 ? 165.559 105.026 142.543 1.00 156.52 ? 2398 ARG A CZ    1 
ATOM   8608  N  NH1   . ARG A 1 2398 ? 165.192 105.965 143.401 1.00 153.57 ? 2398 ARG A NH1   1 
ATOM   8609  N  NH2   . ARG A 1 2398 ? 166.251 103.979 142.981 1.00 157.38 ? 2398 ARG A NH2   1 
ATOM   8610  N  N     . LYS A 1 2399 ? 162.017 102.171 140.710 1.00 156.65 ? 2399 LYS A N     1 
ATOM   8611  C  CA    . LYS A 1 2399 ? 162.490 101.025 139.941 1.00 154.95 ? 2399 LYS A CA    1 
ATOM   8612  C  C     . LYS A 1 2399 ? 161.354 100.333 139.199 1.00 156.79 ? 2399 LYS A C     1 
ATOM   8613  O  O     . LYS A 1 2399 ? 161.597 99.634  138.209 1.00 156.26 ? 2399 LYS A O     1 
ATOM   8614  C  CB    . LYS A 1 2399 ? 163.210 100.034 140.858 1.00 151.46 ? 2399 LYS A CB    1 
ATOM   8615  C  CG    . LYS A 1 2399 ? 162.331 98.907  141.380 1.00 152.24 ? 2399 LYS A CG    1 
ATOM   8616  C  CD    . LYS A 1 2399 ? 163.108 97.977  142.297 1.00 149.78 ? 2399 LYS A CD    1 
ATOM   8617  C  CE    . LYS A 1 2399 ? 162.219 96.870  142.840 1.00 147.30 ? 2399 LYS A CE    1 
ATOM   8618  N  NZ    . LYS A 1 2399 ? 162.966 95.956  143.748 1.00 147.08 ? 2399 LYS A NZ    1 
ATOM   8619  N  N     . GLY A 1 2400 ? 160.116 100.511 139.655 1.00 156.60 ? 2400 GLY A N     1 
ATOM   8620  C  CA    . GLY A 1 2400 ? 158.976 99.894  139.008 1.00 158.42 ? 2400 GLY A CA    1 
ATOM   8621  C  C     . GLY A 1 2400 ? 158.125 100.883 138.240 1.00 163.45 ? 2400 GLY A C     1 
ATOM   8622  O  O     . GLY A 1 2400 ? 157.504 101.769 138.836 1.00 160.82 ? 2400 GLY A O     1 
ATOM   8623  N  N     . LYS A 1 2401 ? 158.093 100.744 136.912 1.00 168.65 ? 2401 LYS A N     1 
ATOM   8624  C  CA    . LYS A 1 2401 ? 157.281 101.640 136.094 1.00 167.33 ? 2401 LYS A CA    1 
ATOM   8625  C  C     . LYS A 1 2401 ? 155.800 101.491 136.418 1.00 166.73 ? 2401 LYS A C     1 
ATOM   8626  O  O     . LYS A 1 2401 ? 155.072 102.488 136.502 1.00 164.10 ? 2401 LYS A O     1 
ATOM   8627  C  CB    . LYS A 1 2401 ? 157.537 101.374 134.610 1.00 162.10 ? 2401 LYS A CB    1 
ATOM   8628  C  CG    . LYS A 1 2401 ? 159.009 101.306 134.231 1.00 157.74 ? 2401 LYS A CG    1 
ATOM   8629  C  CD    . LYS A 1 2401 ? 159.740 102.588 134.600 1.00 157.04 ? 2401 LYS A CD    1 
ATOM   8630  C  CE    . LYS A 1 2401 ? 161.216 102.505 134.243 1.00 155.75 ? 2401 LYS A CE    1 
ATOM   8631  N  NZ    . LYS A 1 2401 ? 162.019 103.552 134.933 1.00 153.11 ? 2401 LYS A NZ    1 
ATOM   8632  N  N     . GLU A 1 2402 ? 155.336 100.256 136.602 1.00 166.46 ? 2402 GLU A N     1 
ATOM   8633  C  CA    . GLU A 1 2402 ? 153.956 99.991  136.980 1.00 165.49 ? 2402 GLU A CA    1 
ATOM   8634  C  C     . GLU A 1 2402 ? 153.835 99.151  138.243 1.00 165.34 ? 2402 GLU A C     1 
ATOM   8635  O  O     . GLU A 1 2402 ? 152.713 98.940  138.721 1.00 165.73 ? 2402 GLU A O     1 
ATOM   8636  C  CB    . GLU A 1 2402 ? 153.208 99.298  135.831 1.00 164.45 ? 2402 GLU A CB    1 
ATOM   8637  C  CG    . GLU A 1 2402 ? 153.675 97.880  135.544 1.00 166.61 ? 2402 GLU A CG    1 
ATOM   8638  C  CD    . GLU A 1 2402 ? 154.833 97.832  134.568 1.00 172.07 ? 2402 GLU A CD    1 
ATOM   8639  O  OE1   . GLU A 1 2402 ? 155.449 98.889  134.320 1.00 171.80 ? 2402 GLU A OE1   1 
ATOM   8640  O  OE2   . GLU A 1 2402 ? 155.129 96.736  134.047 1.00 174.42 ? 2402 GLU A OE2   1 
ATOM   8641  N  N     . ASP A 1 2403 ? 154.953 98.673  138.797 1.00 164.22 ? 2403 ASP A N     1 
ATOM   8642  C  CA    . ASP A 1 2403 ? 154.959 97.861  140.016 1.00 161.26 ? 2403 ASP A CA    1 
ATOM   8643  C  C     . ASP A 1 2403 ? 154.066 96.629  139.875 1.00 159.88 ? 2403 ASP A C     1 
ATOM   8644  O  O     . ASP A 1 2403 ? 153.310 96.280  140.784 1.00 156.72 ? 2403 ASP A O     1 
ATOM   8645  C  CB    . ASP A 1 2403 ? 154.553 98.690  141.237 1.00 156.59 ? 2403 ASP A CB    1 
ATOM   8646  C  CG    . ASP A 1 2403 ? 155.678 99.571  141.742 1.00 154.28 ? 2403 ASP A CG    1 
ATOM   8647  O  OD1   . ASP A 1 2403 ? 156.847 99.136  141.685 1.00 153.94 ? 2403 ASP A OD1   1 
ATOM   8648  O  OD2   . ASP A 1 2403 ? 155.393 100.700 142.196 1.00 155.17 ? 2403 ASP A OD2   1 
ATOM   8649  N  N     . GLU A 1 2404 ? 154.150 95.969  138.722 1.00 159.52 ? 2404 GLU A N     1 
ATOM   8650  C  CA    . GLU A 1 2404 ? 153.383 94.751  138.501 1.00 160.21 ? 2404 GLU A CA    1 
ATOM   8651  C  C     . GLU A 1 2404 ? 153.851 93.650  139.444 1.00 157.88 ? 2404 GLU A C     1 
ATOM   8652  O  O     . GLU A 1 2404 ? 155.052 93.446  139.643 1.00 154.18 ? 2404 GLU A O     1 
ATOM   8653  C  CB    . GLU A 1 2404 ? 153.519 94.295  137.048 1.00 161.44 ? 2404 GLU A CB    1 
ATOM   8654  C  CG    . GLU A 1 2404 ? 152.701 93.061  136.702 1.00 159.20 ? 2404 GLU A CG    1 
ATOM   8655  C  CD    . GLU A 1 2404 ? 151.220 93.247  136.969 1.00 157.96 ? 2404 GLU A CD    1 
ATOM   8656  O  OE1   . GLU A 1 2404 ? 150.617 94.162  136.370 1.00 158.20 ? 2404 GLU A OE1   1 
ATOM   8657  O  OE2   . GLU A 1 2404 ? 150.658 92.478  137.778 1.00 153.00 ? 2404 GLU A OE2   1 
ATOM   8658  N  N     . GLY A 1 2405 ? 152.890 92.937  140.029 1.00 155.64 ? 2405 GLY A N     1 
ATOM   8659  C  CA    . GLY A 1 2405 ? 153.199 91.897  140.987 1.00 153.55 ? 2405 GLY A CA    1 
ATOM   8660  C  C     . GLY A 1 2405 ? 153.503 92.384  142.385 1.00 150.96 ? 2405 GLY A C     1 
ATOM   8661  O  O     . GLY A 1 2405 ? 153.830 91.565  143.251 1.00 147.51 ? 2405 GLY A O     1 
ATOM   8662  N  N     . GLU A 1 2406 ? 153.404 93.689  142.636 1.00 151.90 ? 2406 GLU A N     1 
ATOM   8663  C  CA    . GLU A 1 2406 ? 153.668 94.264  143.948 1.00 149.61 ? 2406 GLU A CA    1 
ATOM   8664  C  C     . GLU A 1 2406 ? 152.438 94.984  144.493 1.00 143.44 ? 2406 GLU A C     1 
ATOM   8665  O  O     . GLU A 1 2406 ? 152.556 95.922  145.284 1.00 136.68 ? 2406 GLU A O     1 
ATOM   8666  C  CB    . GLU A 1 2406 ? 154.866 95.211  143.891 1.00 154.28 ? 2406 GLU A CB    1 
ATOM   8667  C  CG    . GLU A 1 2406 ? 155.653 95.302  145.190 1.00 153.91 ? 2406 GLU A CG    1 
ATOM   8668  C  CD    . GLU A 1 2406 ? 156.652 96.441  145.187 1.00 154.36 ? 2406 GLU A CD    1 
ATOM   8669  O  OE1   . GLU A 1 2406 ? 156.973 96.951  144.092 1.00 154.88 ? 2406 GLU A OE1   1 
ATOM   8670  O  OE2   . GLU A 1 2406 ? 157.115 96.829  146.280 1.00 151.25 ? 2406 GLU A OE2   1 
ATOM   8671  N  N     . GLU A 1 2407 ? 151.248 94.558  144.063 1.00 145.73 ? 2407 GLU A N     1 
ATOM   8672  C  CA    . GLU A 1 2407 ? 150.019 95.171  144.558 1.00 138.39 ? 2407 GLU A CA    1 
ATOM   8673  C  C     . GLU A 1 2407 ? 149.846 94.928  146.052 1.00 135.69 ? 2407 GLU A C     1 
ATOM   8674  O  O     . GLU A 1 2407 ? 149.474 95.840  146.799 1.00 124.45 ? 2407 GLU A O     1 
ATOM   8675  C  CB    . GLU A 1 2407 ? 148.816 94.636  143.782 1.00 137.60 ? 2407 GLU A CB    1 
ATOM   8676  C  CG    . GLU A 1 2407 ? 148.811 95.005  142.305 1.00 143.10 ? 2407 GLU A CG    1 
ATOM   8677  C  CD    . GLU A 1 2407 ? 149.618 94.040  141.457 1.00 152.85 ? 2407 GLU A CD    1 
ATOM   8678  O  OE1   . GLU A 1 2407 ? 150.112 93.032  142.005 1.00 156.71 ? 2407 GLU A OE1   1 
ATOM   8679  O  OE2   . GLU A 1 2407 ? 149.760 94.291  140.241 1.00 152.85 ? 2407 GLU A OE2   1 
ATOM   8680  N  N     . ALA A 1 2408 ? 150.113 93.705  146.505 1.00 137.87 ? 2408 ALA A N     1 
ATOM   8681  C  CA    . ALA A 1 2408 ? 150.050 93.373  147.928 1.00 133.90 ? 2408 ALA A CA    1 
ATOM   8682  C  C     . ALA A 1 2408 ? 151.435 93.512  148.564 1.00 132.22 ? 2408 ALA A C     1 
ATOM   8683  O  O     . ALA A 1 2408 ? 152.013 92.566  149.097 1.00 134.86 ? 2408 ALA A O     1 
ATOM   8684  C  CB    . ALA A 1 2408 ? 149.485 91.970  148.119 1.00 135.25 ? 2408 ALA A CB    1 
ATOM   8685  N  N     . ALA A 1 2409 ? 151.965 94.735  148.484 1.00 128.66 ? 2409 ALA A N     1 
ATOM   8686  C  CA    . ALA A 1 2409 ? 153.314 94.995  148.977 1.00 126.31 ? 2409 ALA A CA    1 
ATOM   8687  C  C     . ALA A 1 2409 ? 153.413 94.769  150.481 1.00 122.29 ? 2409 ALA A C     1 
ATOM   8688  O  O     . ALA A 1 2409 ? 154.387 94.180  150.964 1.00 123.87 ? 2409 ALA A O     1 
ATOM   8689  C  CB    . ALA A 1 2409 ? 153.737 96.420  148.621 1.00 121.52 ? 2409 ALA A CB    1 
ATOM   8690  N  N     . SER A 1 2410 ? 152.418 95.227  151.236 1.00 112.23 ? 2410 SER A N     1 
ATOM   8691  C  CA    . SER A 1 2410 ? 152.440 95.117  152.686 1.00 108.49 ? 2410 SER A CA    1 
ATOM   8692  C  C     . SER A 1 2410 ? 151.013 95.141  153.204 1.00 103.61 ? 2410 SER A C     1 
ATOM   8693  O  O     . SER A 1 2410 ? 150.115 95.638  152.513 1.00 99.10  ? 2410 SER A O     1 
ATOM   8694  C  CB    . SER A 1 2410 ? 153.249 96.258  153.323 1.00 107.82 ? 2410 SER A CB    1 
ATOM   8695  O  OG    . SER A 1 2410 ? 154.581 96.277  152.839 1.00 114.11 ? 2410 SER A OG    1 
ATOM   8696  N  N     . PRO A 1 2411 ? 150.764 94.599  154.399 1.00 100.90 ? 2411 PRO A N     1 
ATOM   8697  C  CA    . PRO A 1 2411 ? 149.441 94.781  155.018 1.00 96.35  ? 2411 PRO A CA    1 
ATOM   8698  C  C     . PRO A 1 2411 ? 149.089 96.239  155.242 1.00 91.45  ? 2411 PRO A C     1 
ATOM   8699  O  O     . PRO A 1 2411 ? 147.907 96.603  155.177 1.00 87.51  ? 2411 PRO A O     1 
ATOM   8700  C  CB    . PRO A 1 2411 ? 149.565 94.015  156.343 1.00 94.35  ? 2411 PRO A CB    1 
ATOM   8701  C  CG    . PRO A 1 2411 ? 150.668 93.035  156.115 1.00 92.85  ? 2411 PRO A CG    1 
ATOM   8702  C  CD    . PRO A 1 2411 ? 151.632 93.712  155.192 1.00 95.83  ? 2411 PRO A CD    1 
ATOM   8703  N  N     . MET A 1 2412 ? 150.087 97.085  155.510 1.00 87.52  ? 2412 MET A N     1 
ATOM   8704  C  CA    . MET A 1 2412 ? 149.853 98.520  155.620 1.00 82.57  ? 2412 MET A CA    1 
ATOM   8705  C  C     . MET A 1 2412 ? 149.229 99.070  154.347 1.00 77.92  ? 2412 MET A C     1 
ATOM   8706  O  O     . MET A 1 2412 ? 148.276 99.858  154.393 1.00 76.33  ? 2412 MET A O     1 
ATOM   8707  C  CB    . MET A 1 2412 ? 151.172 99.237  155.912 1.00 85.61  ? 2412 MET A CB    1 
ATOM   8708  C  CG    . MET A 1 2412 ? 151.033 100.602 156.561 1.00 87.57  ? 2412 MET A CG    1 
ATOM   8709  S  SD    . MET A 1 2412 ? 150.068 100.574 158.076 1.00 81.96  ? 2412 MET A SD    1 
ATOM   8710  C  CE    . MET A 1 2412 ? 148.601 101.466 157.574 1.00 60.02  ? 2412 MET A CE    1 
ATOM   8711  N  N     . LEU A 1 2413 ? 149.767 98.668  153.194 1.00 80.46  ? 2413 LEU A N     1 
ATOM   8712  C  CA    . LEU A 1 2413 ? 149.262 99.178  151.925 1.00 73.44  ? 2413 LEU A CA    1 
ATOM   8713  C  C     . LEU A 1 2413 ? 147.824 98.739  151.690 1.00 69.01  ? 2413 LEU A C     1 
ATOM   8714  O  O     . LEU A 1 2413 ? 146.997 99.531  151.230 1.00 73.16  ? 2413 LEU A O     1 
ATOM   8715  C  CB    . LEU A 1 2413 ? 150.162 98.721  150.779 1.00 76.39  ? 2413 LEU A CB    1 
ATOM   8716  C  CG    . LEU A 1 2413 ? 149.986 99.473  149.461 1.00 67.11  ? 2413 LEU A CG    1 
ATOM   8717  C  CD1   . LEU A 1 2413 ? 149.854 100.961 149.717 1.00 61.41  ? 2413 LEU A CD1   1 
ATOM   8718  C  CD2   . LEU A 1 2413 ? 151.149 99.192  148.531 1.00 81.39  ? 2413 LEU A CD2   1 
ATOM   8719  N  N     . GLN A 1 2414 ? 147.502 97.484  152.007 1.00 66.69  ? 2414 GLN A N     1 
ATOM   8720  C  CA    . GLN A 1 2414 ? 146.129 97.014  151.849 1.00 66.34  ? 2414 GLN A CA    1 
ATOM   8721  C  C     . GLN A 1 2414 ? 145.181 97.758  152.781 1.00 72.30  ? 2414 GLN A C     1 
ATOM   8722  O  O     . GLN A 1 2414 ? 144.070 98.134  152.383 1.00 75.26  ? 2414 GLN A O     1 
ATOM   8723  C  CB    . GLN A 1 2414 ? 146.060 95.510  152.103 1.00 70.57  ? 2414 GLN A CB    1 
ATOM   8724  C  CG    . GLN A 1 2414 ? 144.684 94.910  151.891 1.00 76.88  ? 2414 GLN A CG    1 
ATOM   8725  C  CD    . GLN A 1 2414 ? 144.203 95.057  150.465 1.00 85.26  ? 2414 GLN A CD    1 
ATOM   8726  O  OE1   . GLN A 1 2414 ? 143.343 95.886  150.170 1.00 90.16  ? 2414 GLN A OE1   1 
ATOM   8727  N  NE2   . GLN A 1 2414 ? 144.759 94.252  149.568 1.00 77.97  ? 2414 GLN A NE2   1 
ATOM   8728  N  N     . ILE A 1 2415 ? 145.608 97.985  154.026 1.00 76.60  ? 2415 ILE A N     1 
ATOM   8729  C  CA    . ILE A 1 2415 ? 144.768 98.697  154.986 1.00 71.48  ? 2415 ILE A CA    1 
ATOM   8730  C  C     . ILE A 1 2415 ? 144.493 100.115 154.506 1.00 66.29  ? 2415 ILE A C     1 
ATOM   8731  O  O     . ILE A 1 2415 ? 143.350 100.587 154.541 1.00 66.73  ? 2415 ILE A O     1 
ATOM   8732  C  CB    . ILE A 1 2415 ? 145.423 98.687  156.379 1.00 70.28  ? 2415 ILE A CB    1 
ATOM   8733  C  CG1   . ILE A 1 2415 ? 145.335 97.291  156.998 1.00 76.11  ? 2415 ILE A CG1   1 
ATOM   8734  C  CG2   . ILE A 1 2415 ? 144.782 99.723  157.281 1.00 62.29  ? 2415 ILE A CG2   1 
ATOM   8735  C  CD1   . ILE A 1 2415 ? 146.183 97.120  158.229 1.00 79.11  ? 2415 ILE A CD1   1 
ATOM   8736  N  N     . GLN A 1 2416 ? 145.526 100.814 154.032 1.00 62.18  ? 2416 GLN A N     1 
ATOM   8737  C  CA    . GLN A 1 2416 ? 145.308 102.189 153.597 1.00 59.25  ? 2416 GLN A CA    1 
ATOM   8738  C  C     . GLN A 1 2416 ? 144.574 102.251 152.263 1.00 60.13  ? 2416 GLN A C     1 
ATOM   8739  O  O     . GLN A 1 2416 ? 143.877 103.233 151.994 1.00 60.58  ? 2416 GLN A O     1 
ATOM   8740  C  CB    . GLN A 1 2416 ? 146.629 102.953 153.532 1.00 53.00  ? 2416 GLN A CB    1 
ATOM   8741  C  CG    . GLN A 1 2416 ? 147.668 102.366 152.618 1.00 60.19  ? 2416 GLN A CG    1 
ATOM   8742  C  CD    . GLN A 1 2416 ? 149.040 102.943 152.878 1.00 61.83  ? 2416 GLN A CD    1 
ATOM   8743  O  OE1   . GLN A 1 2416 ? 149.612 102.755 153.950 1.00 65.88  ? 2416 GLN A OE1   1 
ATOM   8744  N  NE2   . GLN A 1 2416 ? 149.576 103.657 151.898 1.00 60.84  ? 2416 GLN A NE2   1 
ATOM   8745  N  N     . ARG A 1 2417 ? 144.691 101.219 151.424 1.00 62.32  ? 2417 ARG A N     1 
ATOM   8746  C  CA    . ARG A 1 2417 ? 143.869 101.163 150.218 1.00 64.26  ? 2417 ARG A CA    1 
ATOM   8747  C  C     . ARG A 1 2417 ? 142.394 101.007 150.564 1.00 67.73  ? 2417 ARG A C     1 
ATOM   8748  O  O     . ARG A 1 2417 ? 141.536 101.663 149.962 1.00 71.77  ? 2417 ARG A O     1 
ATOM   8749  C  CB    . ARG A 1 2417 ? 144.337 100.024 149.313 1.00 57.36  ? 2417 ARG A CB    1 
ATOM   8750  C  CG    . ARG A 1 2417 ? 145.587 100.352 148.519 1.00 56.61  ? 2417 ARG A CG    1 
ATOM   8751  C  CD    . ARG A 1 2417 ? 145.839 99.328  147.431 1.00 59.88  ? 2417 ARG A CD    1 
ATOM   8752  N  NE    . ARG A 1 2417 ? 147.261 99.181  147.146 1.00 69.77  ? 2417 ARG A NE    1 
ATOM   8753  C  CZ    . ARG A 1 2417 ? 147.760 98.905  145.950 1.00 80.67  ? 2417 ARG A CZ    1 
ATOM   8754  N  NH1   . ARG A 1 2417 ? 146.977 98.745  144.895 1.00 85.20  ? 2417 ARG A NH1   1 
ATOM   8755  N  NH2   . ARG A 1 2417 ? 149.077 98.789  145.807 1.00 79.50  ? 2417 ARG A NH2   1 
ATOM   8756  N  N     . ASP A 1 2418 ? 142.080 100.148 151.537 1.00 66.01  ? 2418 ASP A N     1 
ATOM   8757  C  CA    . ASP A 1 2418 ? 140.701 100.041 152.004 1.00 65.21  ? 2418 ASP A CA    1 
ATOM   8758  C  C     . ASP A 1 2418 ? 140.229 101.358 152.612 1.00 67.23  ? 2418 ASP A C     1 
ATOM   8759  O  O     . ASP A 1 2418 ? 139.083 101.782 152.401 1.00 67.41  ? 2418 ASP A O     1 
ATOM   8760  C  CB    . ASP A 1 2418 ? 140.579 98.904  153.017 1.00 73.23  ? 2418 ASP A CB    1 
ATOM   8761  C  CG    . ASP A 1 2418 ? 140.123 97.605  152.383 1.00 89.28  ? 2418 ASP A CG    1 
ATOM   8762  O  OD1   . ASP A 1 2418 ? 140.040 97.546  151.138 1.00 90.76  ? 2418 ASP A OD1   1 
ATOM   8763  O  OD2   . ASP A 1 2418 ? 139.852 96.641  153.128 1.00 98.56  ? 2418 ASP A OD2   1 
ATOM   8764  N  N     . ALA A 1 2419 ? 141.108 102.021 153.367 1.00 65.85  ? 2419 ALA A N     1 
ATOM   8765  C  CA    . ALA A 1 2419 ? 140.774 103.320 153.940 1.00 63.76  ? 2419 ALA A CA    1 
ATOM   8766  C  C     . ALA A 1 2419 ? 140.454 104.338 152.854 1.00 66.77  ? 2419 ALA A C     1 
ATOM   8767  O  O     . ALA A 1 2419 ? 139.484 105.094 152.968 1.00 67.84  ? 2419 ALA A O     1 
ATOM   8768  C  CB    . ALA A 1 2419 ? 141.928 103.817 154.809 1.00 59.18  ? 2419 ALA A CB    1 
ATOM   8769  N  N     . ALA A 1 2420 ? 141.267 104.377 151.797 1.00 59.84  ? 2420 ALA A N     1 
ATOM   8770  C  CA    . ALA A 1 2420 ? 141.019 105.300 150.697 1.00 58.61  ? 2420 ALA A CA    1 
ATOM   8771  C  C     . ALA A 1 2420 ? 139.715 104.968 149.988 1.00 61.55  ? 2420 ALA A C     1 
ATOM   8772  O  O     . ALA A 1 2420 ? 138.970 105.870 149.591 1.00 62.60  ? 2420 ALA A O     1 
ATOM   8773  C  CB    . ALA A 1 2420 ? 142.187 105.271 149.715 1.00 58.48  ? 2420 ALA A CB    1 
ATOM   8774  N  N     . THR A 1 2421 ? 139.424 103.678 149.820 1.00 63.01  ? 2421 THR A N     1 
ATOM   8775  C  CA    . THR A 1 2421 ? 138.164 103.285 149.200 1.00 64.56  ? 2421 THR A CA    1 
ATOM   8776  C  C     . THR A 1 2421 ? 136.976 103.785 150.011 1.00 59.99  ? 2421 THR A C     1 
ATOM   8777  O  O     . THR A 1 2421 ? 135.984 104.262 149.448 1.00 59.08  ? 2421 THR A O     1 
ATOM   8778  C  CB    . THR A 1 2421 ? 138.104 101.766 149.046 1.00 65.82  ? 2421 THR A CB    1 
ATOM   8779  O  OG1   . THR A 1 2421 ? 139.227 101.317 148.277 1.00 68.35  ? 2421 THR A OG1   1 
ATOM   8780  C  CG2   . THR A 1 2421 ? 136.821 101.352 148.345 1.00 65.13  ? 2421 THR A CG2   1 
ATOM   8781  N  N     . ILE A 1 2422 ? 137.060 103.686 151.338 1.00 64.05  ? 2422 ILE A N     1 
ATOM   8782  C  CA    . ILE A 1 2422 ? 135.951 104.133 152.178 1.00 65.62  ? 2422 ILE A CA    1 
ATOM   8783  C  C     . ILE A 1 2422 ? 135.860 105.656 152.209 1.00 65.41  ? 2422 ILE A C     1 
ATOM   8784  O  O     . ILE A 1 2422 ? 134.761 106.222 152.250 1.00 69.73  ? 2422 ILE A O     1 
ATOM   8785  C  CB    . ILE A 1 2422 ? 136.081 103.531 153.586 1.00 67.57  ? 2422 ILE A CB    1 
ATOM   8786  C  CG1   . ILE A 1 2422 ? 135.842 102.027 153.510 1.00 72.51  ? 2422 ILE A CG1   1 
ATOM   8787  C  CG2   . ILE A 1 2422 ? 135.095 104.172 154.547 1.00 67.08  ? 2422 ILE A CG2   1 
ATOM   8788  C  CD1   . ILE A 1 2422 ? 136.667 101.249 154.455 1.00 71.15  ? 2422 ILE A CD1   1 
ATOM   8789  N  N     . MET A 1 2423 ? 136.999 106.345 152.191 1.00 63.94  ? 2423 MET A N     1 
ATOM   8790  C  CA    . MET A 1 2423 ? 137.003 107.803 152.241 1.00 58.65  ? 2423 MET A CA    1 
ATOM   8791  C  C     . MET A 1 2423 ? 136.749 108.454 150.888 1.00 63.84  ? 2423 MET A C     1 
ATOM   8792  O  O     . MET A 1 2423 ? 136.592 109.678 150.833 1.00 66.79  ? 2423 MET A O     1 
ATOM   8793  C  CB    . MET A 1 2423 ? 138.332 108.311 152.803 1.00 53.53  ? 2423 MET A CB    1 
ATOM   8794  C  CG    . MET A 1 2423 ? 138.563 107.959 154.255 1.00 58.39  ? 2423 MET A CG    1 
ATOM   8795  S  SD    . MET A 1 2423 ? 140.104 108.628 154.902 1.00 69.93  ? 2423 MET A SD    1 
ATOM   8796  C  CE    . MET A 1 2423 ? 141.300 107.551 154.129 1.00 49.99  ? 2423 MET A CE    1 
ATOM   8797  N  N     . GLN A 1 2424 ? 136.725 107.678 149.805 1.00 62.90  ? 2424 GLN A N     1 
ATOM   8798  C  CA    . GLN A 1 2424 ? 136.470 108.248 148.483 1.00 60.03  ? 2424 GLN A CA    1 
ATOM   8799  C  C     . GLN A 1 2424 ? 135.167 109.038 148.402 1.00 59.06  ? 2424 GLN A C     1 
ATOM   8800  O  O     . GLN A 1 2424 ? 135.184 110.146 147.840 1.00 59.65  ? 2424 GLN A O     1 
ATOM   8801  C  CB    . GLN A 1 2424 ? 136.507 107.130 147.435 1.00 63.53  ? 2424 GLN A CB    1 
ATOM   8802  C  CG    . GLN A 1 2424 ? 136.477 107.614 145.998 1.00 65.48  ? 2424 GLN A CG    1 
ATOM   8803  C  CD    . GLN A 1 2424 ? 137.793 108.224 145.573 1.00 66.22  ? 2424 GLN A CD    1 
ATOM   8804  O  OE1   . GLN A 1 2424 ? 138.858 107.680 145.859 1.00 65.62  ? 2424 GLN A OE1   1 
ATOM   8805  N  NE2   . GLN A 1 2424 ? 137.730 109.360 144.890 1.00 61.30  ? 2424 GLN A NE2   1 
ATOM   8806  N  N     . PRO A 1 2425 ? 134.024 108.552 148.906 1.00 59.24  ? 2425 PRO A N     1 
ATOM   8807  C  CA    . PRO A 1 2425 ? 132.789 109.349 148.789 1.00 60.01  ? 2425 PRO A CA    1 
ATOM   8808  C  C     . PRO A 1 2425 ? 132.859 110.712 149.455 1.00 60.52  ? 2425 PRO A C     1 
ATOM   8809  O  O     . PRO A 1 2425 ? 132.227 111.658 148.968 1.00 62.93  ? 2425 PRO A O     1 
ATOM   8810  C  CB    . PRO A 1 2425 ? 131.735 108.457 149.459 1.00 54.98  ? 2425 PRO A CB    1 
ATOM   8811  C  CG    . PRO A 1 2425 ? 132.256 107.090 149.305 1.00 60.03  ? 2425 PRO A CG    1 
ATOM   8812  C  CD    . PRO A 1 2425 ? 133.740 107.207 149.439 1.00 58.97  ? 2425 PRO A CD    1 
ATOM   8813  N  N     . TYR A 1 2426 ? 133.594 110.845 150.556 1.00 57.95  ? 2426 TYR A N     1 
ATOM   8814  C  CA    . TYR A 1 2426 ? 133.651 112.110 151.276 1.00 55.75  ? 2426 TYR A CA    1 
ATOM   8815  C  C     . TYR A 1 2426 ? 134.649 113.094 150.684 1.00 58.67  ? 2426 TYR A C     1 
ATOM   8816  O  O     . TYR A 1 2426 ? 134.626 114.270 151.060 1.00 59.10  ? 2426 TYR A O     1 
ATOM   8817  C  CB    . TYR A 1 2426 ? 133.988 111.856 152.744 1.00 54.49  ? 2426 TYR A CB    1 
ATOM   8818  C  CG    . TYR A 1 2426 ? 133.126 110.794 153.384 1.00 60.24  ? 2426 TYR A CG    1 
ATOM   8819  C  CD1   . TYR A 1 2426 ? 131.800 111.050 153.699 1.00 63.80  ? 2426 TYR A CD1   1 
ATOM   8820  C  CD2   . TYR A 1 2426 ? 133.631 109.530 153.655 1.00 58.89  ? 2426 TYR A CD2   1 
ATOM   8821  C  CE1   . TYR A 1 2426 ? 131.005 110.084 154.277 1.00 64.15  ? 2426 TYR A CE1   1 
ATOM   8822  C  CE2   . TYR A 1 2426 ? 132.843 108.558 154.233 1.00 61.63  ? 2426 TYR A CE2   1 
ATOM   8823  C  CZ    . TYR A 1 2426 ? 131.531 108.841 154.541 1.00 65.93  ? 2426 TYR A CZ    1 
ATOM   8824  O  OH    . TYR A 1 2426 ? 130.738 107.877 155.117 1.00 72.94  ? 2426 TYR A OH    1 
ATOM   8825  N  N     . PHE A 1 2427 ? 135.511 112.654 149.771 1.00 59.22  ? 2427 PHE A N     1 
ATOM   8826  C  CA    . PHE A 1 2427 ? 136.501 113.516 149.139 1.00 54.04  ? 2427 PHE A CA    1 
ATOM   8827  C  C     . PHE A 1 2427 ? 136.124 113.851 147.699 1.00 61.05  ? 2427 PHE A C     1 
ATOM   8828  O  O     . PHE A 1 2427 ? 136.995 113.962 146.832 1.00 63.77  ? 2427 PHE A O     1 
ATOM   8829  C  CB    . PHE A 1 2427 ? 137.883 112.870 149.193 1.00 50.67  ? 2427 PHE A CB    1 
ATOM   8830  C  CG    . PHE A 1 2427 ? 138.575 113.033 150.514 1.00 53.93  ? 2427 PHE A CG    1 
ATOM   8831  C  CD1   . PHE A 1 2427 ? 138.218 112.255 151.599 1.00 52.91  ? 2427 PHE A CD1   1 
ATOM   8832  C  CD2   . PHE A 1 2427 ? 139.581 113.969 150.672 1.00 54.43  ? 2427 PHE A CD2   1 
ATOM   8833  C  CE1   . PHE A 1 2427 ? 138.850 112.405 152.813 1.00 49.83  ? 2427 PHE A CE1   1 
ATOM   8834  C  CE2   . PHE A 1 2427 ? 140.216 114.123 151.884 1.00 44.41  ? 2427 PHE A CE2   1 
ATOM   8835  C  CZ    . PHE A 1 2427 ? 139.850 113.341 152.956 1.00 46.77  ? 2427 PHE A CZ    1 
ATOM   8836  N  N     . THR A 1 2428 ? 134.832 114.010 147.430 1.00 68.07  ? 2428 THR A N     1 
ATOM   8837  C  CA    . THR A 1 2428 ? 134.348 114.318 146.094 1.00 70.31  ? 2428 THR A CA    1 
ATOM   8838  C  C     . THR A 1 2428 ? 134.307 115.833 145.897 1.00 76.07  ? 2428 THR A C     1 
ATOM   8839  O  O     . THR A 1 2428 ? 134.812 116.604 146.717 1.00 77.14  ? 2428 THR A O     1 
ATOM   8840  C  CB    . THR A 1 2428 ? 132.981 113.678 145.864 1.00 64.91  ? 2428 THR A CB    1 
ATOM   8841  O  OG1   . THR A 1 2428 ? 132.077 114.094 146.894 1.00 66.54  ? 2428 THR A OG1   1 
ATOM   8842  C  CG2   . THR A 1 2428 ? 133.094 112.164 145.874 1.00 55.61  ? 2428 THR A CG2   1 
ATOM   8843  N  N     . SER A 1 2429 ? 133.704 116.275 144.791 1.00 73.78  ? 2429 SER A N     1 
ATOM   8844  C  CA    . SER A 1 2429 ? 133.646 117.703 144.495 1.00 78.14  ? 2429 SER A CA    1 
ATOM   8845  C  C     . SER A 1 2429 ? 132.784 118.450 145.504 1.00 81.09  ? 2429 SER A C     1 
ATOM   8846  O  O     . SER A 1 2429 ? 133.140 119.552 145.938 1.00 85.88  ? 2429 SER A O     1 
ATOM   8847  C  CB    . SER A 1 2429 ? 133.126 117.921 143.075 1.00 81.66  ? 2429 SER A CB    1 
ATOM   8848  O  OG    . SER A 1 2429 ? 134.010 117.363 142.119 1.00 78.12  ? 2429 SER A OG    1 
ATOM   8849  N  N     . ASN A 1 2430 ? 131.649 117.873 145.887 1.00 78.31  ? 2430 ASN A N     1 
ATOM   8850  C  CA    . ASN A 1 2430 ? 130.730 118.475 146.847 1.00 81.00  ? 2430 ASN A CA    1 
ATOM   8851  C  C     . ASN A 1 2430 ? 130.620 117.645 148.125 1.00 82.62  ? 2430 ASN A C     1 
ATOM   8852  O  O     . ASN A 1 2430 ? 129.628 117.720 148.853 1.00 85.45  ? 2430 ASN A O     1 
ATOM   8853  C  CB    . ASN A 1 2430 ? 129.366 118.719 146.194 1.00 86.64  ? 2430 ASN A CB    1 
ATOM   8854  C  CG    . ASN A 1 2430 ? 128.565 117.436 145.936 1.00 93.00  ? 2430 ASN A CG    1 
ATOM   8855  O  OD1   . ASN A 1 2430 ? 128.550 116.499 146.732 1.00 92.69  ? 2430 ASN A OD1   1 
ATOM   8856  N  ND2   . ASN A 1 2430 ? 127.888 117.406 144.794 1.00 94.18  ? 2430 ASN A ND2   1 
ATOM   8857  N  N     . GLY A 1 2431 ? 131.660 116.869 148.425 1.00 76.35  ? 2431 GLY A N     1 
ATOM   8858  C  CA    . GLY A 1 2431 ? 131.632 115.992 149.574 1.00 67.92  ? 2431 GLY A CA    1 
ATOM   8859  C  C     . GLY A 1 2431 ? 131.698 116.736 150.892 1.00 63.73  ? 2431 GLY A C     1 
ATOM   8860  O  O     . GLY A 1 2431 ? 131.707 117.965 150.952 1.00 64.08  ? 2431 GLY A O     1 
ATOM   8861  N  N     . LEU A 1 2432 ? 131.742 115.955 151.973 1.00 58.90  ? 2432 LEU A N     1 
ATOM   8862  C  CA    . LEU A 1 2432 ? 131.736 116.534 153.312 1.00 53.99  ? 2432 LEU A CA    1 
ATOM   8863  C  C     . LEU A 1 2432 ? 132.966 117.399 153.549 1.00 53.89  ? 2432 LEU A C     1 
ATOM   8864  O  O     . LEU A 1 2432 ? 132.871 118.473 154.157 1.00 57.42  ? 2432 LEU A O     1 
ATOM   8865  C  CB    . LEU A 1 2432 ? 131.651 115.424 154.359 1.00 52.40  ? 2432 LEU A CB    1 
ATOM   8866  C  CG    . LEU A 1 2432 ? 131.934 115.820 155.808 1.00 53.51  ? 2432 LEU A CG    1 
ATOM   8867  C  CD1   . LEU A 1 2432 ? 130.781 116.628 156.366 1.00 62.20  ? 2432 LEU A CD1   1 
ATOM   8868  C  CD2   . LEU A 1 2432 ? 132.187 114.590 156.660 1.00 54.51  ? 2432 LEU A CD2   1 
ATOM   8869  N  N     . VAL A 1 2433 ? 134.129 116.950 153.075 1.00 53.39  ? 2433 VAL A N     1 
ATOM   8870  C  CA    . VAL A 1 2433 ? 135.372 117.668 153.344 1.00 45.87  ? 2433 VAL A CA    1 
ATOM   8871  C  C     . VAL A 1 2433 ? 135.341 119.056 152.717 1.00 51.94  ? 2433 VAL A C     1 
ATOM   8872  O  O     . VAL A 1 2433 ? 135.764 120.036 153.337 1.00 53.97  ? 2433 VAL A O     1 
ATOM   8873  C  CB    . VAL A 1 2433 ? 136.581 116.853 152.853 1.00 41.70  ? 2433 VAL A CB    1 
ATOM   8874  C  CG1   . VAL A 1 2433 ? 137.867 117.544 153.247 1.00 41.83  ? 2433 VAL A CG1   1 
ATOM   8875  C  CG2   . VAL A 1 2433 ? 136.538 115.452 153.427 1.00 46.45  ? 2433 VAL A CG2   1 
ATOM   8876  N  N     . THR A 1 2434 ? 134.841 119.165 151.485 1.00 58.44  ? 2434 THR A N     1 
ATOM   8877  C  CA    . THR A 1 2434 ? 134.841 120.454 150.798 1.00 57.00  ? 2434 THR A CA    1 
ATOM   8878  C  C     . THR A 1 2434 ? 133.906 121.451 151.477 1.00 55.21  ? 2434 THR A C     1 
ATOM   8879  O  O     . THR A 1 2434 ? 134.277 122.609 151.708 1.00 58.82  ? 2434 THR A O     1 
ATOM   8880  C  CB    . THR A 1 2434 ? 134.454 120.266 149.332 1.00 57.86  ? 2434 THR A CB    1 
ATOM   8881  O  OG1   . THR A 1 2434 ? 135.186 119.163 148.784 1.00 54.26  ? 2434 THR A OG1   1 
ATOM   8882  C  CG2   . THR A 1 2434 ? 134.773 121.518 148.537 1.00 59.81  ? 2434 THR A CG2   1 
ATOM   8883  N  N     . LYS A 1 2435 ? 132.683 121.022 151.798 1.00 51.21  ? 2435 LYS A N     1 
ATOM   8884  C  CA    . LYS A 1 2435 ? 131.744 121.910 152.477 1.00 57.58  ? 2435 LYS A CA    1 
ATOM   8885  C  C     . LYS A 1 2435 ? 132.268 122.311 153.849 1.00 58.50  ? 2435 LYS A C     1 
ATOM   8886  O  O     . LYS A 1 2435 ? 132.151 123.475 154.257 1.00 61.34  ? 2435 LYS A O     1 
ATOM   8887  C  CB    . LYS A 1 2435 ? 130.379 121.234 152.599 1.00 61.36  ? 2435 LYS A CB    1 
ATOM   8888  C  CG    . LYS A 1 2435 ? 129.887 120.598 151.310 1.00 61.92  ? 2435 LYS A CG    1 
ATOM   8889  C  CD    . LYS A 1 2435 ? 128.377 120.685 151.190 1.00 58.77  ? 2435 LYS A CD    1 
ATOM   8890  C  CE    . LYS A 1 2435 ? 127.930 122.115 150.941 1.00 64.29  ? 2435 LYS A CE    1 
ATOM   8891  N  NZ    . LYS A 1 2435 ? 128.474 122.652 149.664 1.00 59.87  ? 2435 LYS A NZ    1 
ATOM   8892  N  N     . ALA A 1 2436 ? 132.855 121.357 154.574 1.00 55.80  ? 2436 ALA A N     1 
ATOM   8893  C  CA    . ALA A 1 2436 ? 133.445 121.669 155.868 1.00 48.98  ? 2436 ALA A CA    1 
ATOM   8894  C  C     . ALA A 1 2436 ? 134.590 122.661 155.724 1.00 50.14  ? 2436 ALA A C     1 
ATOM   8895  O  O     . ALA A 1 2436 ? 134.774 123.532 156.578 1.00 59.45  ? 2436 ALA A O     1 
ATOM   8896  C  CB    . ALA A 1 2436 ? 133.920 120.385 156.543 1.00 44.00  ? 2436 ALA A CB    1 
ATOM   8897  N  N     . LEU A 1 2437 ? 135.372 122.544 154.650 1.00 47.32  ? 2437 LEU A N     1 
ATOM   8898  C  CA    . LEU A 1 2437 ? 136.475 123.473 154.429 1.00 48.22  ? 2437 LEU A CA    1 
ATOM   8899  C  C     . LEU A 1 2437 ? 135.966 124.879 154.136 1.00 52.46  ? 2437 LEU A C     1 
ATOM   8900  O  O     . LEU A 1 2437 ? 136.535 125.863 154.621 1.00 58.06  ? 2437 LEU A O     1 
ATOM   8901  C  CB    . LEU A 1 2437 ? 137.361 122.966 153.292 1.00 46.97  ? 2437 LEU A CB    1 
ATOM   8902  C  CG    . LEU A 1 2437 ? 138.639 123.749 152.999 1.00 48.57  ? 2437 LEU A CG    1 
ATOM   8903  C  CD1   . LEU A 1 2437 ? 139.605 123.653 154.164 1.00 47.70  ? 2437 LEU A CD1   1 
ATOM   8904  C  CD2   . LEU A 1 2437 ? 139.286 123.233 151.729 1.00 44.91  ? 2437 LEU A CD2   1 
ATOM   8905  N  N     . GLU A 1 2438 ? 134.893 124.997 153.350 1.00 51.25  ? 2438 GLU A N     1 
ATOM   8906  C  CA    . GLU A 1 2438 ? 134.308 126.319 153.128 1.00 53.03  ? 2438 GLU A CA    1 
ATOM   8907  C  C     . GLU A 1 2438 ? 133.773 126.910 154.427 1.00 57.45  ? 2438 GLU A C     1 
ATOM   8908  O  O     . GLU A 1 2438 ? 133.953 128.106 154.698 1.00 60.42  ? 2438 GLU A O     1 
ATOM   8909  C  CB    . GLU A 1 2438 ? 133.201 126.259 152.072 1.00 59.86  ? 2438 GLU A CB    1 
ATOM   8910  C  CG    . GLU A 1 2438 ? 133.489 125.393 150.847 1.00 67.10  ? 2438 GLU A CG    1 
ATOM   8911  C  CD    . GLU A 1 2438 ? 134.852 125.642 150.211 1.00 72.32  ? 2438 GLU A CD    1 
ATOM   8912  O  OE1   . GLU A 1 2438 ? 135.398 126.759 150.338 1.00 74.08  ? 2438 GLU A OE1   1 
ATOM   8913  O  OE2   . GLU A 1 2438 ? 135.384 124.704 149.581 1.00 66.13  ? 2438 GLU A OE2   1 
ATOM   8914  N  N     . HIS A 1 2439 ? 133.119 126.087 155.252 1.00 58.92  ? 2439 HIS A N     1 
ATOM   8915  C  CA    . HIS A 1 2439 ? 132.629 126.585 156.534 1.00 56.39  ? 2439 HIS A CA    1 
ATOM   8916  C  C     . HIS A 1 2439 ? 133.778 127.026 157.433 1.00 53.53  ? 2439 HIS A C     1 
ATOM   8917  O  O     . HIS A 1 2439 ? 133.681 128.048 158.122 1.00 55.65  ? 2439 HIS A O     1 
ATOM   8918  C  CB    . HIS A 1 2439 ? 131.786 125.525 157.235 1.00 52.25  ? 2439 HIS A CB    1 
ATOM   8919  C  CG    . HIS A 1 2439 ? 130.811 126.092 158.219 1.00 61.04  ? 2439 HIS A CG    1 
ATOM   8920  N  ND1   . HIS A 1 2439 ? 129.971 127.140 157.912 1.00 69.25  ? 2439 HIS A ND1   1 
ATOM   8921  C  CD2   . HIS A 1 2439 ? 130.561 125.776 159.511 1.00 63.60  ? 2439 HIS A CD2   1 
ATOM   8922  C  CE1   . HIS A 1 2439 ? 129.233 127.434 158.968 1.00 69.97  ? 2439 HIS A CE1   1 
ATOM   8923  N  NE2   . HIS A 1 2439 ? 129.572 126.621 159.951 1.00 68.94  ? 2439 HIS A NE2   1 
ATOM   8924  N  N     . ALA A 1 2440 ? 134.872 126.261 157.448 1.00 47.86  ? 2440 ALA A N     1 
ATOM   8925  C  CA    . ALA A 1 2440 ? 136.041 126.650 158.228 1.00 44.92  ? 2440 ALA A CA    1 
ATOM   8926  C  C     . ALA A 1 2440 ? 136.628 127.958 157.719 1.00 51.02  ? 2440 ALA A C     1 
ATOM   8927  O  O     . ALA A 1 2440 ? 137.105 128.781 158.508 1.00 57.31  ? 2440 ALA A O     1 
ATOM   8928  C  CB    . ALA A 1 2440 ? 137.089 125.541 158.188 1.00 41.95  ? 2440 ALA A CB    1 
ATOM   8929  N  N     . PHE A 1 2441 ? 136.614 128.160 156.401 1.00 54.49  ? 2441 PHE A N     1 
ATOM   8930  C  CA    . PHE A 1 2441 ? 137.021 129.447 155.850 1.00 53.99  ? 2441 PHE A CA    1 
ATOM   8931  C  C     . PHE A 1 2441 ? 136.112 130.564 156.342 1.00 55.25  ? 2441 PHE A C     1 
ATOM   8932  O  O     . PHE A 1 2441 ? 136.563 131.696 156.547 1.00 56.33  ? 2441 PHE A O     1 
ATOM   8933  C  CB    . PHE A 1 2441 ? 137.022 129.391 154.323 1.00 54.62  ? 2441 PHE A CB    1 
ATOM   8934  C  CG    . PHE A 1 2441 ? 138.290 128.841 153.741 1.00 60.54  ? 2441 PHE A CG    1 
ATOM   8935  C  CD1   . PHE A 1 2441 ? 138.253 127.959 152.677 1.00 64.16  ? 2441 PHE A CD1   1 
ATOM   8936  C  CD2   . PHE A 1 2441 ? 139.518 129.211 154.256 1.00 51.96  ? 2441 PHE A CD2   1 
ATOM   8937  C  CE1   . PHE A 1 2441 ? 139.418 127.455 152.140 1.00 57.98  ? 2441 PHE A CE1   1 
ATOM   8938  C  CE2   . PHE A 1 2441 ? 140.684 128.711 153.724 1.00 51.93  ? 2441 PHE A CE2   1 
ATOM   8939  C  CZ    . PHE A 1 2441 ? 140.634 127.832 152.665 1.00 58.89  ? 2441 PHE A CZ    1 
ATOM   8940  N  N     . GLN A 1 2442 ? 134.823 130.267 156.529 1.00 61.27  ? 2442 GLN A N     1 
ATOM   8941  C  CA    . GLN A 1 2442 ? 133.911 131.273 157.067 1.00 60.96  ? 2442 GLN A CA    1 
ATOM   8942  C  C     . GLN A 1 2442 ? 134.286 131.664 158.493 1.00 58.43  ? 2442 GLN A C     1 
ATOM   8943  O  O     . GLN A 1 2442 ? 134.213 132.842 158.860 1.00 62.91  ? 2442 GLN A O     1 
ATOM   8944  C  CB    . GLN A 1 2442 ? 132.470 130.765 157.013 1.00 59.68  ? 2442 GLN A CB    1 
ATOM   8945  C  CG    . GLN A 1 2442 ? 131.765 131.035 155.695 1.00 65.65  ? 2442 GLN A CG    1 
ATOM   8946  C  CD    . GLN A 1 2442 ? 130.487 130.234 155.547 1.00 77.15  ? 2442 GLN A CD    1 
ATOM   8947  O  OE1   . GLN A 1 2442 ? 129.821 129.919 156.532 1.00 81.46  ? 2442 GLN A OE1   1 
ATOM   8948  N  NE2   . GLN A 1 2442 ? 130.138 129.900 154.310 1.00 78.12  ? 2442 GLN A NE2   1 
ATOM   8949  N  N     . LEU A 1 2443 ? 134.688 130.693 159.311 1.00 58.73  ? 2443 LEU A N     1 
ATOM   8950  C  CA    . LEU A 1 2443 ? 135.017 130.956 160.705 1.00 56.56  ? 2443 LEU A CA    1 
ATOM   8951  C  C     . LEU A 1 2443 ? 136.306 131.771 160.816 1.00 58.93  ? 2443 LEU A C     1 
ATOM   8952  O  O     . LEU A 1 2443 ? 137.023 131.998 159.838 1.00 62.80  ? 2443 LEU A O     1 
ATOM   8953  C  CB    . LEU A 1 2443 ? 135.166 129.646 161.478 1.00 50.04  ? 2443 LEU A CB    1 
ATOM   8954  C  CG    . LEU A 1 2443 ? 134.020 128.637 161.386 1.00 51.80  ? 2443 LEU A CG    1 
ATOM   8955  C  CD1   . LEU A 1 2443 ? 134.318 127.412 162.232 1.00 44.40  ? 2443 LEU A CD1   1 
ATOM   8956  C  CD2   . LEU A 1 2443 ? 132.708 129.274 161.808 1.00 58.82  ? 2443 LEU A CD2   1 
ATOM   8957  N  N     . GLU A 1 2444 ? 136.594 132.216 162.036 1.00 58.48  ? 2444 GLU A N     1 
ATOM   8958  C  CA    . GLU A 1 2444 ? 137.826 132.923 162.350 1.00 58.39  ? 2444 GLU A CA    1 
ATOM   8959  C  C     . GLU A 1 2444 ? 138.747 132.034 163.176 1.00 59.63  ? 2444 GLU A C     1 
ATOM   8960  O  O     . GLU A 1 2444 ? 138.295 131.245 164.012 1.00 56.91  ? 2444 GLU A O     1 
ATOM   8961  C  CB    . GLU A 1 2444 ? 137.552 134.232 163.101 1.00 59.72  ? 2444 GLU A CB    1 
ATOM   8962  C  CG    . GLU A 1 2444 ? 136.844 135.304 162.277 1.00 74.72  ? 2444 GLU A CG    1 
ATOM   8963  C  CD    . GLU A 1 2444 ? 135.340 135.127 162.222 1.00 79.73  ? 2444 GLU A CD    1 
ATOM   8964  O  OE1   . GLU A 1 2444 ? 134.822 134.202 162.878 1.00 81.92  ? 2444 GLU A OE1   1 
ATOM   8965  O  OE2   . GLU A 1 2444 ? 134.676 135.915 161.516 1.00 75.01  ? 2444 GLU A OE2   1 
ATOM   8966  N  N     . HIS A 1 2445 ? 140.047 132.178 162.935 1.00 57.56  ? 2445 HIS A N     1 
ATOM   8967  C  CA    . HIS A 1 2445 ? 141.060 131.304 163.504 1.00 46.37  ? 2445 HIS A CA    1 
ATOM   8968  C  C     . HIS A 1 2445 ? 142.176 132.136 164.117 1.00 48.97  ? 2445 HIS A C     1 
ATOM   8969  O  O     . HIS A 1 2445 ? 142.335 133.321 163.816 1.00 56.67  ? 2445 HIS A O     1 
ATOM   8970  C  CB    . HIS A 1 2445 ? 141.630 130.354 162.443 1.00 45.44  ? 2445 HIS A CB    1 
ATOM   8971  C  CG    . HIS A 1 2445 ? 140.582 129.579 161.710 1.00 46.87  ? 2445 HIS A CG    1 
ATOM   8972  N  ND1   . HIS A 1 2445 ? 140.319 128.253 161.971 1.00 45.25  ? 2445 HIS A ND1   1 
ATOM   8973  C  CD2   . HIS A 1 2445 ? 139.718 129.949 160.735 1.00 50.06  ? 2445 HIS A CD2   1 
ATOM   8974  C  CE1   . HIS A 1 2445 ? 139.344 127.836 161.185 1.00 44.44  ? 2445 HIS A CE1   1 
ATOM   8975  N  NE2   . HIS A 1 2445 ? 138.960 128.847 160.427 1.00 49.37  ? 2445 HIS A NE2   1 
ATOM   8976  N  N     . ILE A 1 2446 ? 142.952 131.493 164.994 1.00 49.07  ? 2446 ILE A N     1 
ATOM   8977  C  CA    . ILE A 1 2446 ? 144.036 132.187 165.677 1.00 49.18  ? 2446 ILE A CA    1 
ATOM   8978  C  C     . ILE A 1 2446 ? 145.188 132.505 164.732 1.00 52.10  ? 2446 ILE A C     1 
ATOM   8979  O  O     . ILE A 1 2446 ? 145.974 133.419 165.004 1.00 54.60  ? 2446 ILE A O     1 
ATOM   8980  C  CB    . ILE A 1 2446 ? 144.517 131.362 166.886 1.00 45.14  ? 2446 ILE A CB    1 
ATOM   8981  C  CG1   . ILE A 1 2446 ? 145.219 132.265 167.899 1.00 50.34  ? 2446 ILE A CG1   1 
ATOM   8982  C  CG2   . ILE A 1 2446 ? 145.431 130.231 166.447 1.00 46.28  ? 2446 ILE A CG2   1 
ATOM   8983  C  CD1   . ILE A 1 2446 ? 144.381 133.444 168.334 1.00 56.64  ? 2446 ILE A CD1   1 
ATOM   8984  N  N     . MET A 1 2447 ? 145.307 131.780 163.623 1.00 49.84  ? 2447 MET A N     1 
ATOM   8985  C  CA    . MET A 1 2447 ? 146.306 132.047 162.602 1.00 49.69  ? 2447 MET A CA    1 
ATOM   8986  C  C     . MET A 1 2447 ? 145.620 132.298 161.267 1.00 55.11  ? 2447 MET A C     1 
ATOM   8987  O  O     . MET A 1 2447 ? 144.476 131.890 161.047 1.00 59.47  ? 2447 MET A O     1 
ATOM   8988  C  CB    . MET A 1 2447 ? 147.298 130.885 162.462 1.00 48.31  ? 2447 MET A CB    1 
ATOM   8989  C  CG    . MET A 1 2447 ? 148.014 130.501 163.743 1.00 52.96  ? 2447 MET A CG    1 
ATOM   8990  S  SD    . MET A 1 2447 ? 149.599 131.340 163.912 1.00 60.48  ? 2447 MET A SD    1 
ATOM   8991  C  CE    . MET A 1 2447 ? 150.249 130.554 165.381 1.00 47.15  ? 2447 MET A CE    1 
ATOM   8992  N  N     . ASP A 1 2448 ? 146.329 132.991 160.380 1.00 59.82  ? 2448 ASP A N     1 
ATOM   8993  C  CA    . ASP A 1 2448 ? 145.827 133.221 159.032 1.00 58.01  ? 2448 ASP A CA    1 
ATOM   8994  C  C     . ASP A 1 2448 ? 145.566 131.889 158.345 1.00 54.96  ? 2448 ASP A C     1 
ATOM   8995  O  O     . ASP A 1 2448 ? 146.497 131.117 158.094 1.00 54.41  ? 2448 ASP A O     1 
ATOM   8996  C  CB    . ASP A 1 2448 ? 146.828 134.049 158.230 1.00 59.63  ? 2448 ASP A CB    1 
ATOM   8997  C  CG    . ASP A 1 2448 ? 146.620 135.539 158.400 1.00 70.65  ? 2448 ASP A CG    1 
ATOM   8998  O  OD1   . ASP A 1 2448 ? 145.452 135.977 158.435 1.00 75.40  ? 2448 ASP A OD1   1 
ATOM   8999  O  OD2   . ASP A 1 2448 ? 147.625 136.272 158.498 1.00 71.92  ? 2448 ASP A OD2   1 
ATOM   9000  N  N     . LEU A 1 2449 ? 144.299 131.619 158.048 1.00 48.96  ? 2449 LEU A N     1 
ATOM   9001  C  CA    . LEU A 1 2449 ? 143.918 130.314 157.528 1.00 45.89  ? 2449 LEU A CA    1 
ATOM   9002  C  C     . LEU A 1 2449 ? 144.425 130.128 156.106 1.00 54.65  ? 2449 LEU A C     1 
ATOM   9003  O  O     . LEU A 1 2449 ? 144.360 131.047 155.284 1.00 61.68  ? 2449 LEU A O     1 
ATOM   9004  C  CB    . LEU A 1 2449 ? 142.402 130.146 157.555 1.00 48.25  ? 2449 LEU A CB    1 
ATOM   9005  C  CG    . LEU A 1 2449 ? 141.987 128.682 157.429 1.00 47.54  ? 2449 LEU A CG    1 
ATOM   9006  C  CD1   . LEU A 1 2449 ? 142.794 127.860 158.412 1.00 42.64  ? 2449 LEU A CD1   1 
ATOM   9007  C  CD2   . LEU A 1 2449 ? 140.501 128.483 157.633 1.00 55.11  ? 2449 LEU A CD2   1 
ATOM   9008  N  N     . THR A 1 2450 ? 144.927 128.931 155.818 1.00 47.96  ? 2450 THR A N     1 
ATOM   9009  C  CA    . THR A 1 2450 ? 145.281 128.522 154.468 1.00 41.25  ? 2450 THR A CA    1 
ATOM   9010  C  C     . THR A 1 2450 ? 144.689 127.147 154.210 1.00 39.44  ? 2450 THR A C     1 
ATOM   9011  O  O     . THR A 1 2450 ? 144.543 126.344 155.136 1.00 41.66  ? 2450 THR A O     1 
ATOM   9012  C  CB    . THR A 1 2450 ? 146.800 128.494 154.258 1.00 46.83  ? 2450 THR A CB    1 
ATOM   9013  O  OG1   . THR A 1 2450 ? 147.417 127.719 155.292 1.00 43.33  ? 2450 THR A OG1   1 
ATOM   9014  C  CG2   . THR A 1 2450 ? 147.369 129.900 154.274 1.00 48.01  ? 2450 THR A CG2   1 
ATOM   9015  N  N     . ARG A 1 2451 ? 144.337 126.885 152.951 1.00 36.04  ? 2451 ARG A N     1 
ATOM   9016  C  CA    . ARG A 1 2451 ? 143.718 125.610 152.606 1.00 33.14  ? 2451 ARG A CA    1 
ATOM   9017  C  C     . ARG A 1 2451 ? 144.663 124.441 152.854 1.00 33.28  ? 2451 ARG A C     1 
ATOM   9018  O  O     . ARG A 1 2451 ? 144.254 123.404 153.393 1.00 40.56  ? 2451 ARG A O     1 
ATOM   9019  C  CB    . ARG A 1 2451 ? 143.265 125.629 151.147 1.00 32.64  ? 2451 ARG A CB    1 
ATOM   9020  C  CG    . ARG A 1 2451 ? 142.724 124.301 150.658 1.00 35.89  ? 2451 ARG A CG    1 
ATOM   9021  C  CD    . ARG A 1 2451 ? 142.439 124.323 149.167 1.00 44.38  ? 2451 ARG A CD    1 
ATOM   9022  N  NE    . ARG A 1 2451 ? 143.644 124.482 148.363 1.00 40.26  ? 2451 ARG A NE    1 
ATOM   9023  C  CZ    . ARG A 1 2451 ? 143.753 125.316 147.338 1.00 35.46  ? 2451 ARG A CZ    1 
ATOM   9024  N  NH1   . ARG A 1 2451 ? 142.737 126.065 146.946 1.00 37.26  ? 2451 ARG A NH1   1 
ATOM   9025  N  NH2   . ARG A 1 2451 ? 144.908 125.394 146.685 1.00 32.22  ? 2451 ARG A NH2   1 
ATOM   9026  N  N     . LEU A 1 2452 ? 145.933 124.589 152.478 1.00 31.15  ? 2452 LEU A N     1 
ATOM   9027  C  CA    . LEU A 1 2452 ? 146.832 123.443 152.513 1.00 30.31  ? 2452 LEU A CA    1 
ATOM   9028  C  C     . LEU A 1 2452 ? 147.287 123.102 153.923 1.00 31.89  ? 2452 LEU A C     1 
ATOM   9029  O  O     . LEU A 1 2452 ? 147.605 121.943 154.190 1.00 34.82  ? 2452 LEU A O     1 
ATOM   9030  C  CB    . LEU A 1 2452 ? 148.031 123.675 151.602 1.00 29.64  ? 2452 LEU A CB    1 
ATOM   9031  C  CG    . LEU A 1 2452 ? 147.740 123.210 150.178 1.00 33.96  ? 2452 LEU A CG    1 
ATOM   9032  C  CD1   . LEU A 1 2452 ? 148.949 123.391 149.311 1.00 31.99  ? 2452 LEU A CD1   1 
ATOM   9033  C  CD2   . LEU A 1 2452 ? 147.311 121.757 150.189 1.00 31.76  ? 2452 LEU A CD2   1 
ATOM   9034  N  N     . ARG A 1 2453 ? 147.314 124.069 154.840 1.00 33.10  ? 2453 ARG A N     1 
ATOM   9035  C  CA    . ARG A 1 2453 ? 147.594 123.731 156.232 1.00 30.44  ? 2453 ARG A CA    1 
ATOM   9036  C  C     . ARG A 1 2453 ? 146.538 122.776 156.779 1.00 35.31  ? 2453 ARG A C     1 
ATOM   9037  O  O     . ARG A 1 2453 ? 146.861 121.713 157.328 1.00 48.44  ? 2453 ARG A O     1 
ATOM   9038  C  CB    . ARG A 1 2453 ? 147.661 125.000 157.077 1.00 27.72  ? 2453 ARG A CB    1 
ATOM   9039  C  CG    . ARG A 1 2453 ? 147.461 124.756 158.561 1.00 30.13  ? 2453 ARG A CG    1 
ATOM   9040  C  CD    . ARG A 1 2453 ? 148.166 125.804 159.398 1.00 32.72  ? 2453 ARG A CD    1 
ATOM   9041  N  NE    . ARG A 1 2453 ? 147.449 127.072 159.420 1.00 39.25  ? 2453 ARG A NE    1 
ATOM   9042  C  CZ    . ARG A 1 2453 ? 146.288 127.267 160.027 1.00 40.98  ? 2453 ARG A CZ    1 
ATOM   9043  N  NH1   . ARG A 1 2453 ? 145.679 126.294 160.684 1.00 38.55  ? 2453 ARG A NH1   1 
ATOM   9044  N  NH2   . ARG A 1 2453 ? 145.728 128.471 159.986 1.00 41.34  ? 2453 ARG A NH2   1 
ATOM   9045  N  N     . CYS A 1 2454 ? 145.263 123.134 156.608 1.00 27.03  ? 2454 CYS A N     1 
ATOM   9046  C  CA    . CYS A 1 2454 ? 144.175 122.269 157.047 1.00 25.28  ? 2454 CYS A CA    1 
ATOM   9047  C  C     . CYS A 1 2454 ? 144.198 120.936 156.320 1.00 28.69  ? 2454 CYS A C     1 
ATOM   9048  O  O     . CYS A 1 2454 ? 143.984 119.884 156.931 1.00 34.03  ? 2454 CYS A O     1 
ATOM   9049  C  CB    . CYS A 1 2454 ? 142.834 122.958 156.822 1.00 27.98  ? 2454 CYS A CB    1 
ATOM   9050  S  SG    . CYS A 1 2454 ? 142.800 124.679 157.292 1.00 58.74  ? 2454 CYS A SG    1 
ATOM   9051  N  N     . LEU A 1 2455 ? 144.438 120.959 155.009 1.00 25.44  ? 2455 LEU A N     1 
ATOM   9052  C  CA    . LEU A 1 2455 ? 144.417 119.717 154.245 1.00 26.51  ? 2455 LEU A CA    1 
ATOM   9053  C  C     . LEU A 1 2455 ? 145.555 118.788 154.654 1.00 28.32  ? 2455 LEU A C     1 
ATOM   9054  O  O     . LEU A 1 2455 ? 145.353 117.577 154.776 1.00 37.71  ? 2455 LEU A O     1 
ATOM   9055  C  CB    . LEU A 1 2455 ? 144.459 120.026 152.750 1.00 30.86  ? 2455 LEU A CB    1 
ATOM   9056  C  CG    . LEU A 1 2455 ? 143.098 119.928 152.055 1.00 29.01  ? 2455 LEU A CG    1 
ATOM   9057  C  CD1   . LEU A 1 2455 ? 142.085 120.840 152.715 1.00 26.38  ? 2455 LEU A CD1   1 
ATOM   9058  C  CD2   . LEU A 1 2455 ? 143.225 120.266 150.585 1.00 36.64  ? 2455 LEU A CD2   1 
ATOM   9059  N  N     . GLY A 1 2456 ? 146.752 119.330 154.884 1.00 22.71  ? 2456 GLY A N     1 
ATOM   9060  C  CA    . GLY A 1 2456 ? 147.853 118.499 155.337 1.00 27.78  ? 2456 GLY A CA    1 
ATOM   9061  C  C     . GLY A 1 2456 ? 147.622 117.934 156.724 1.00 33.16  ? 2456 GLY A C     1 
ATOM   9062  O  O     . GLY A 1 2456 ? 147.929 116.768 156.989 1.00 40.26  ? 2456 GLY A O     1 
ATOM   9063  N  N     . SER A 1 2457 ? 147.070 118.750 157.627 1.00 29.89  ? 2457 SER A N     1 
ATOM   9064  C  CA    . SER A 1 2457 ? 146.718 118.241 158.948 1.00 29.76  ? 2457 SER A CA    1 
ATOM   9065  C  C     . SER A 1 2457 ? 145.695 117.114 158.850 1.00 33.77  ? 2457 SER A C     1 
ATOM   9066  O  O     . SER A 1 2457 ? 145.836 116.076 159.510 1.00 43.18  ? 2457 SER A O     1 
ATOM   9067  C  CB    . SER A 1 2457 ? 146.190 119.382 159.813 1.00 31.81  ? 2457 SER A CB    1 
ATOM   9068  O  OG    . SER A 1 2457 ? 145.412 118.887 160.882 1.00 47.37  ? 2457 SER A OG    1 
ATOM   9069  N  N     . LEU A 1 2458 ? 144.671 117.293 158.012 1.00 26.43  ? 2458 LEU A N     1 
ATOM   9070  C  CA    . LEU A 1 2458 ? 143.665 116.254 157.810 1.00 27.70  ? 2458 LEU A CA    1 
ATOM   9071  C  C     . LEU A 1 2458 ? 144.285 114.978 157.259 1.00 32.03  ? 2458 LEU A C     1 
ATOM   9072  O  O     . LEU A 1 2458 ? 143.966 113.873 157.717 1.00 38.12  ? 2458 LEU A O     1 
ATOM   9073  C  CB    . LEU A 1 2458 ? 142.585 116.771 156.862 1.00 29.79  ? 2458 LEU A CB    1 
ATOM   9074  C  CG    . LEU A 1 2458 ? 141.407 115.868 156.504 1.00 29.57  ? 2458 LEU A CG    1 
ATOM   9075  C  CD1   . LEU A 1 2458 ? 140.579 115.544 157.721 1.00 35.84  ? 2458 LEU A CD1   1 
ATOM   9076  C  CD2   . LEU A 1 2458 ? 140.559 116.538 155.450 1.00 30.74  ? 2458 LEU A CD2   1 
ATOM   9077  N  N     . PHE A 1 2459 ? 145.166 115.109 156.268 1.00 28.83  ? 2459 PHE A N     1 
ATOM   9078  C  CA    . PHE A 1 2459 ? 145.777 113.936 155.658 1.00 29.23  ? 2459 PHE A CA    1 
ATOM   9079  C  C     . PHE A 1 2459 ? 146.646 113.189 156.660 1.00 36.16  ? 2459 PHE A C     1 
ATOM   9080  O  O     . PHE A 1 2459 ? 146.650 111.954 156.689 1.00 43.89  ? 2459 PHE A O     1 
ATOM   9081  C  CB    . PHE A 1 2459 ? 146.592 114.350 154.433 1.00 27.50  ? 2459 PHE A CB    1 
ATOM   9082  C  CG    . PHE A 1 2459 ? 145.779 115.014 153.355 1.00 27.45  ? 2459 PHE A CG    1 
ATOM   9083  C  CD1   . PHE A 1 2459 ? 144.405 114.858 153.300 1.00 29.13  ? 2459 PHE A CD1   1 
ATOM   9084  C  CD2   . PHE A 1 2459 ? 146.391 115.809 152.403 1.00 30.46  ? 2459 PHE A CD2   1 
ATOM   9085  C  CE1   . PHE A 1 2459 ? 143.661 115.475 152.313 1.00 26.27  ? 2459 PHE A CE1   1 
ATOM   9086  C  CE2   . PHE A 1 2459 ? 145.651 116.428 151.415 1.00 29.41  ? 2459 PHE A CE2   1 
ATOM   9087  C  CZ    . PHE A 1 2459 ? 144.286 116.260 151.371 1.00 27.46  ? 2459 PHE A CZ    1 
ATOM   9088  N  N     . SER A 1 2460 ? 147.384 113.922 157.496 1.00 32.77  ? 2460 SER A N     1 
ATOM   9089  C  CA    . SER A 1 2460 ? 148.197 113.274 158.519 1.00 35.21  ? 2460 SER A CA    1 
ATOM   9090  C  C     . SER A 1 2460 ? 147.331 112.563 159.554 1.00 38.13  ? 2460 SER A C     1 
ATOM   9091  O  O     . SER A 1 2460 ? 147.673 111.466 160.014 1.00 43.18  ? 2460 SER A O     1 
ATOM   9092  C  CB    . SER A 1 2460 ? 149.104 114.303 159.181 1.00 36.47  ? 2460 SER A CB    1 
ATOM   9093  O  OG    . SER A 1 2460 ? 149.737 115.088 158.190 1.00 45.21  ? 2460 SER A OG    1 
ATOM   9094  N  N     . MET A 1 2461 ? 146.205 113.171 159.936 1.00 33.61  ? 2461 MET A N     1 
ATOM   9095  C  CA    . MET A 1 2461 ? 145.299 112.502 160.865 1.00 31.50  ? 2461 MET A CA    1 
ATOM   9096  C  C     . MET A 1 2461 ? 144.729 111.221 160.262 1.00 39.50  ? 2461 MET A C     1 
ATOM   9097  O  O     . MET A 1 2461 ? 144.589 110.207 160.955 1.00 44.83  ? 2461 MET A O     1 
ATOM   9098  C  CB    . MET A 1 2461 ? 144.178 113.450 161.284 1.00 31.15  ? 2461 MET A CB    1 
ATOM   9099  C  CG    . MET A 1 2461 ? 144.651 114.704 161.997 1.00 32.85  ? 2461 MET A CG    1 
ATOM   9100  S  SD    . MET A 1 2461 ? 143.537 115.243 163.305 1.00 41.43  ? 2461 MET A SD    1 
ATOM   9101  C  CE    . MET A 1 2461 ? 143.550 113.809 164.371 1.00 42.45  ? 2461 MET A CE    1 
ATOM   9102  N  N     . LEU A 1 2462 ? 144.395 111.245 158.970 1.00 37.85  ? 2462 LEU A N     1 
ATOM   9103  C  CA    . LEU A 1 2462 ? 143.900 110.033 158.317 1.00 35.98  ? 2462 LEU A CA    1 
ATOM   9104  C  C     . LEU A 1 2462 ? 144.987 108.965 158.224 1.00 42.02  ? 2462 LEU A C     1 
ATOM   9105  O  O     . LEU A 1 2462 ? 144.710 107.762 158.360 1.00 51.47  ? 2462 LEU A O     1 
ATOM   9106  C  CB    . LEU A 1 2462 ? 143.352 110.378 156.935 1.00 34.28  ? 2462 LEU A CB    1 
ATOM   9107  C  CG    . LEU A 1 2462 ? 142.189 111.369 156.971 1.00 37.90  ? 2462 LEU A CG    1 
ATOM   9108  C  CD1   . LEU A 1 2462 ? 141.721 111.715 155.572 1.00 41.12  ? 2462 LEU A CD1   1 
ATOM   9109  C  CD2   . LEU A 1 2462 ? 141.050 110.809 157.801 1.00 41.01  ? 2462 LEU A CD2   1 
ATOM   9110  N  N     . HIS A 1 2463 ? 146.231 109.386 157.987 1.00 36.33  ? 2463 HIS A N     1 
ATOM   9111  C  CA    . HIS A 1 2463 ? 147.350 108.454 158.026 1.00 41.05  ? 2463 HIS A CA    1 
ATOM   9112  C  C     . HIS A 1 2463 ? 147.462 107.797 159.394 1.00 47.64  ? 2463 HIS A C     1 
ATOM   9113  O  O     . HIS A 1 2463 ? 147.675 106.583 159.499 1.00 53.40  ? 2463 HIS A O     1 
ATOM   9114  C  CB    . HIS A 1 2463 ? 148.647 109.183 157.681 1.00 46.83  ? 2463 HIS A CB    1 
ATOM   9115  C  CG    . HIS A 1 2463 ? 148.722 109.645 156.260 1.00 44.28  ? 2463 HIS A CG    1 
ATOM   9116  N  ND1   . HIS A 1 2463 ? 149.779 110.383 155.774 1.00 44.21  ? 2463 HIS A ND1   1 
ATOM   9117  C  CD2   . HIS A 1 2463 ? 147.872 109.476 155.221 1.00 44.85  ? 2463 HIS A CD2   1 
ATOM   9118  C  CE1   . HIS A 1 2463 ? 149.577 110.649 154.497 1.00 48.47  ? 2463 HIS A CE1   1 
ATOM   9119  N  NE2   . HIS A 1 2463 ? 148.427 110.109 154.136 1.00 47.73  ? 2463 HIS A NE2   1 
ATOM   9120  N  N     . GLN A 1 2464 ? 147.317 108.586 160.459 1.00 48.76  ? 2464 GLN A N     1 
ATOM   9121  C  CA    . GLN A 1 2464 ? 147.344 108.010 161.799 1.00 48.14  ? 2464 GLN A CA    1 
ATOM   9122  C  C     . GLN A 1 2464 ? 146.167 107.072 162.028 1.00 48.80  ? 2464 GLN A C     1 
ATOM   9123  O  O     . GLN A 1 2464 ? 146.302 106.076 162.743 1.00 57.36  ? 2464 GLN A O     1 
ATOM   9124  C  CB    . GLN A 1 2464 ? 147.359 109.115 162.853 1.00 48.91  ? 2464 GLN A CB    1 
ATOM   9125  C  CG    . GLN A 1 2464 ? 147.299 108.603 164.283 1.00 51.50  ? 2464 GLN A CG    1 
ATOM   9126  C  CD    . GLN A 1 2464 ? 148.564 107.879 164.709 1.00 54.78  ? 2464 GLN A CD    1 
ATOM   9127  O  OE1   . GLN A 1 2464 ? 149.573 107.895 164.006 1.00 58.26  ? 2464 GLN A OE1   1 
ATOM   9128  N  NE2   . GLN A 1 2464 ? 148.509 107.229 165.863 1.00 57.18  ? 2464 GLN A NE2   1 
ATOM   9129  N  N     . ALA A 1 2465 ? 145.010 107.369 161.437 1.00 49.25  ? 2465 ALA A N     1 
ATOM   9130  C  CA    . ALA A 1 2465 ? 143.867 106.467 161.555 1.00 51.60  ? 2465 ALA A CA    1 
ATOM   9131  C  C     . ALA A 1 2465 ? 144.175 105.105 160.946 1.00 54.58  ? 2465 ALA A C     1 
ATOM   9132  O  O     . ALA A 1 2465 ? 143.898 104.057 161.548 1.00 61.41  ? 2465 ALA A O     1 
ATOM   9133  C  CB    . ALA A 1 2465 ? 142.640 107.082 160.885 1.00 47.18  ? 2465 ALA A CB    1 
ATOM   9134  N  N     . CYS A 1 2466 ? 144.748 105.096 159.743 1.00 51.46  ? 2466 CYS A N     1 
ATOM   9135  C  CA    . CYS A 1 2466 ? 145.063 103.807 159.134 1.00 53.23  ? 2466 CYS A CA    1 
ATOM   9136  C  C     . CYS A 1 2466 ? 146.200 103.106 159.875 1.00 58.63  ? 2466 CYS A C     1 
ATOM   9137  O  O     . CYS A 1 2466 ? 146.224 101.871 159.945 1.00 67.36  ? 2466 CYS A O     1 
ATOM   9138  C  CB    . CYS A 1 2466 ? 145.380 103.972 157.646 1.00 51.84  ? 2466 CYS A CB    1 
ATOM   9139  S  SG    . CYS A 1 2466 ? 146.993 104.645 157.254 1.00 86.10  ? 2466 CYS A SG    1 
ATOM   9140  N  N     . ARG A 1 2467 ? 147.126 103.867 160.468 1.00 52.48  ? 2467 ARG A N     1 
ATOM   9141  C  CA    . ARG A 1 2467 ? 148.142 103.252 161.321 1.00 50.27  ? 2467 ARG A CA    1 
ATOM   9142  C  C     . ARG A 1 2467 ? 147.520 102.615 162.560 1.00 55.47  ? 2467 ARG A C     1 
ATOM   9143  O  O     . ARG A 1 2467 ? 147.987 101.574 163.034 1.00 62.35  ? 2467 ARG A O     1 
ATOM   9144  C  CB    . ARG A 1 2467 ? 149.191 104.286 161.723 1.00 52.12  ? 2467 ARG A CB    1 
ATOM   9145  C  CG    . ARG A 1 2467 ? 150.091 104.722 160.590 1.00 58.14  ? 2467 ARG A CG    1 
ATOM   9146  C  CD    . ARG A 1 2467 ? 150.940 105.910 160.990 1.00 54.14  ? 2467 ARG A CD    1 
ATOM   9147  N  NE    . ARG A 1 2467 ? 151.753 106.389 159.881 1.00 62.94  ? 2467 ARG A NE    1 
ATOM   9148  C  CZ    . ARG A 1 2467 ? 152.472 107.501 159.908 1.00 65.67  ? 2467 ARG A CZ    1 
ATOM   9149  N  NH1   . ARG A 1 2467 ? 152.476 108.292 160.967 1.00 65.66  ? 2467 ARG A NH1   1 
ATOM   9150  N  NH2   . ARG A 1 2467 ? 153.199 107.831 158.845 1.00 64.68  ? 2467 ARG A NH2   1 
ATOM   9151  N  N     . ASN A 1 2468 ? 146.483 103.244 163.115 1.00 56.70  ? 2468 ASN A N     1 
ATOM   9152  C  CA    . ASN A 1 2468 ? 145.764 102.647 164.236 1.00 54.67  ? 2468 ASN A CA    1 
ATOM   9153  C  C     . ASN A 1 2468 ? 145.084 101.351 163.820 1.00 60.57  ? 2468 ASN A C     1 
ATOM   9154  O  O     . ASN A 1 2468 ? 145.082 100.369 164.574 1.00 68.85  ? 2468 ASN A O     1 
ATOM   9155  C  CB    . ASN A 1 2468 ? 144.736 103.633 164.788 1.00 52.73  ? 2468 ASN A CB    1 
ATOM   9156  C  CG    . ASN A 1 2468 ? 145.374 104.867 165.380 1.00 56.30  ? 2468 ASN A CG    1 
ATOM   9157  O  OD1   . ASN A 1 2468 ? 146.597 104.967 165.468 1.00 57.29  ? 2468 ASN A OD1   1 
ATOM   9158  N  ND2   . ASN A 1 2468 ? 144.547 105.822 165.787 1.00 57.47  ? 2468 ASN A ND2   1 
ATOM   9159  N  N     . VAL A 1 2469 ? 144.489 101.334 162.626 1.00 61.71  ? 2469 VAL A N     1 
ATOM   9160  C  CA    . VAL A 1 2469 ? 143.940 100.084 162.101 1.00 64.51  ? 2469 VAL A CA    1 
ATOM   9161  C  C     . VAL A 1 2469 ? 145.034 99.027  162.011 1.00 63.72  ? 2469 VAL A C     1 
ATOM   9162  O  O     . VAL A 1 2469 ? 144.823 97.855  162.351 1.00 71.16  ? 2469 VAL A O     1 
ATOM   9163  C  CB    . VAL A 1 2469 ? 143.270 100.316 160.734 1.00 60.02  ? 2469 VAL A CB    1 
ATOM   9164  C  CG1   . VAL A 1 2469 ? 142.714 99.011  160.197 1.00 63.52  ? 2469 VAL A CG1   1 
ATOM   9165  C  CG2   . VAL A 1 2469 ? 142.176 101.352 160.846 1.00 58.48  ? 2469 VAL A CG2   1 
ATOM   9166  N  N     . ALA A 1 2470 ? 146.223 99.429  161.559 1.00 57.27  ? 2470 ALA A N     1 
ATOM   9167  C  CA    . ALA A 1 2470 ? 147.333 98.488  161.443 1.00 57.78  ? 2470 ALA A CA    1 
ATOM   9168  C  C     . ALA A 1 2470 ? 147.749 97.933  162.800 1.00 65.84  ? 2470 ALA A C     1 
ATOM   9169  O  O     . ALA A 1 2470 ? 148.009 96.732  162.930 1.00 75.67  ? 2470 ALA A O     1 
ATOM   9170  C  CB    . ALA A 1 2470 ? 148.521 99.160  160.765 1.00 61.69  ? 2470 ALA A CB    1 
ATOM   9171  N  N     . GLN A 1 2471 ? 147.839 98.790  163.819 1.00 68.48  ? 2471 GLN A N     1 
ATOM   9172  C  CA    . GLN A 1 2471 ? 148.277 98.302  165.125 1.00 67.01  ? 2471 GLN A CA    1 
ATOM   9173  C  C     . GLN A 1 2471 ? 147.212 97.416  165.757 1.00 71.56  ? 2471 GLN A C     1 
ATOM   9174  O  O     . GLN A 1 2471 ? 147.536 96.461  166.472 1.00 81.08  ? 2471 GLN A O     1 
ATOM   9175  C  CB    . GLN A 1 2471 ? 148.643 99.456  166.062 1.00 65.13  ? 2471 GLN A CB    1 
ATOM   9176  C  CG    . GLN A 1 2471 ? 147.503 100.364 166.465 1.00 68.69  ? 2471 GLN A CG    1 
ATOM   9177  C  CD    . GLN A 1 2471 ? 147.957 101.509 167.347 1.00 74.77  ? 2471 GLN A CD    1 
ATOM   9178  O  OE1   . GLN A 1 2471 ? 149.131 101.603 167.705 1.00 76.00  ? 2471 GLN A OE1   1 
ATOM   9179  N  NE2   . GLN A 1 2471 ? 147.026 102.382 167.710 1.00 78.74  ? 2471 GLN A NE2   1 
ATOM   9180  N  N     . TYR A 1 2472 ? 145.933 97.711  165.504 1.00 72.10  ? 2472 TYR A N     1 
ATOM   9181  C  CA    . TYR A 1 2472 ? 144.879 96.806  165.950 1.00 73.79  ? 2472 TYR A CA    1 
ATOM   9182  C  C     . TYR A 1 2472 ? 144.989 95.450  165.267 1.00 78.90  ? 2472 TYR A C     1 
ATOM   9183  O  O     . TYR A 1 2472 ? 144.800 94.409  165.906 1.00 85.20  ? 2472 TYR A O     1 
ATOM   9184  C  CB    . TYR A 1 2472 ? 143.504 97.416  165.699 1.00 74.73  ? 2472 TYR A CB    1 
ATOM   9185  C  CG    . TYR A 1 2472 ? 142.368 96.535  166.163 1.00 83.04  ? 2472 TYR A CG    1 
ATOM   9186  C  CD1   . TYR A 1 2472 ? 142.061 96.411  167.510 1.00 89.69  ? 2472 TYR A CD1   1 
ATOM   9187  C  CD2   . TYR A 1 2472 ? 141.596 95.830  165.249 1.00 81.99  ? 2472 TYR A CD2   1 
ATOM   9188  C  CE1   . TYR A 1 2472 ? 141.017 95.611  167.935 1.00 91.20  ? 2472 TYR A CE1   1 
ATOM   9189  C  CE2   . TYR A 1 2472 ? 140.554 95.026  165.663 1.00 86.06  ? 2472 TYR A CE2   1 
ATOM   9190  C  CZ    . TYR A 1 2472 ? 140.269 94.920  167.007 1.00 91.61  ? 2472 TYR A CZ    1 
ATOM   9191  O  OH    . TYR A 1 2472 ? 139.231 94.119  167.424 1.00 97.29  ? 2472 TYR A OH    1 
ATOM   9192  N  N     . ASN A 1 2473 ? 145.285 95.442  163.966 1.00 80.20  ? 2473 ASN A N     1 
ATOM   9193  C  CA    . ASN A 1 2473 ? 145.462 94.173  163.268 1.00 81.22  ? 2473 ASN A CA    1 
ATOM   9194  C  C     . ASN A 1 2473 ? 146.664 93.410  163.813 1.00 82.77  ? 2473 ASN A C     1 
ATOM   9195  O  O     . ASN A 1 2473 ? 146.631 92.179  163.924 1.00 87.18  ? 2473 ASN A O     1 
ATOM   9196  C  CB    . ASN A 1 2473 ? 145.609 94.414  161.768 1.00 74.86  ? 2473 ASN A CB    1 
ATOM   9197  C  CG    . ASN A 1 2473 ? 144.278 94.399  161.046 1.00 85.08  ? 2473 ASN A CG    1 
ATOM   9198  O  OD1   . ASN A 1 2473 ? 143.254 94.028  161.617 1.00 89.04  ? 2473 ASN A OD1   1 
ATOM   9199  N  ND2   . ASN A 1 2473 ? 144.286 94.800  159.781 1.00 87.38  ? 2473 ASN A ND2   1 
ATOM   9200  N  N     . ALA A 1 2474 ? 147.736 94.127  164.156 1.00 80.16  ? 2474 ALA A N     1 
ATOM   9201  C  CA    . ALA A 1 2474 ? 148.920 93.478  164.709 1.00 82.62  ? 2474 ALA A CA    1 
ATOM   9202  C  C     . ALA A 1 2474 ? 148.665 92.919  166.103 1.00 90.71  ? 2474 ALA A C     1 
ATOM   9203  O  O     . ALA A 1 2474 ? 149.196 91.858  166.449 1.00 92.32  ? 2474 ALA A O     1 
ATOM   9204  C  CB    . ALA A 1 2474 ? 150.092 94.458  164.738 1.00 80.25  ? 2474 ALA A CB    1 
ATOM   9205  N  N     . ASN A 1 2475 ? 147.869 93.614  166.918 1.00 90.84  ? 2475 ASN A N     1 
ATOM   9206  C  CA    . ASN A 1 2475 ? 147.576 93.144  168.267 1.00 89.75  ? 2475 ASN A CA    1 
ATOM   9207  C  C     . ASN A 1 2475 ? 146.585 91.988  168.291 1.00 96.66  ? 2475 ASN A C     1 
ATOM   9208  O  O     . ASN A 1 2475 ? 146.503 91.286  169.305 1.00 102.76 ? 2475 ASN A O     1 
ATOM   9209  C  CB    . ASN A 1 2475 ? 147.039 94.292  169.125 1.00 91.03  ? 2475 ASN A CB    1 
ATOM   9210  C  CG    . ASN A 1 2475 ? 148.080 95.364  169.380 1.00 93.28  ? 2475 ASN A CG    1 
ATOM   9211  O  OD1   . ASN A 1 2475 ? 149.227 95.246  168.951 1.00 91.24  ? 2475 ASN A OD1   1 
ATOM   9212  N  ND2   . ASN A 1 2475 ? 147.683 96.418  170.082 1.00 90.41  ? 2475 ASN A ND2   1 
ATOM   9213  N  N     . HIS A 1 2476 ? 145.835 91.772  167.212 1.00 97.44  ? 2476 HIS A N     1 
ATOM   9214  C  CA    . HIS A 1 2476 ? 144.861 90.683  167.123 1.00 100.65 ? 2476 HIS A CA    1 
ATOM   9215  C  C     . HIS A 1 2476 ? 145.067 89.913  165.824 1.00 103.97 ? 2476 HIS A C     1 
ATOM   9216  O  O     . HIS A 1 2476 ? 144.277 90.052  164.880 1.00 108.29 ? 2476 HIS A O     1 
ATOM   9217  C  CB    . HIS A 1 2476 ? 143.432 91.218  167.216 1.00 100.29 ? 2476 HIS A CB    1 
ATOM   9218  C  CG    . HIS A 1 2476 ? 143.108 91.850  168.533 1.00 102.39 ? 2476 HIS A CG    1 
ATOM   9219  N  ND1   . HIS A 1 2476 ? 142.871 91.114  169.673 1.00 107.20 ? 2476 HIS A ND1   1 
ATOM   9220  C  CD2   . HIS A 1 2476 ? 142.991 93.150  168.893 1.00 99.87  ? 2476 HIS A CD2   1 
ATOM   9221  C  CE1   . HIS A 1 2476 ? 142.615 91.932  170.678 1.00 109.94 ? 2476 HIS A CE1   1 
ATOM   9222  N  NE2   . HIS A 1 2476 ? 142.682 93.173  170.231 1.00 106.00 ? 2476 HIS A NE2   1 
ATOM   9223  N  N     . PRO A 1 2477 ? 146.128 89.102  165.733 1.00 105.40 ? 2477 PRO A N     1 
ATOM   9224  C  CA    . PRO A 1 2477 ? 146.309 88.290  164.517 1.00 108.27 ? 2477 PRO A CA    1 
ATOM   9225  C  C     . PRO A 1 2477 ? 145.134 87.376  164.222 1.00 110.93 ? 2477 PRO A C     1 
ATOM   9226  O  O     . PRO A 1 2477 ? 144.790 87.171  163.051 1.00 109.91 ? 2477 PRO A O     1 
ATOM   9227  C  CB    . PRO A 1 2477 ? 147.576 87.482  164.822 1.00 105.71 ? 2477 PRO A CB    1 
ATOM   9228  C  CG    . PRO A 1 2477 ? 148.329 88.285  165.805 1.00 105.01 ? 2477 PRO A CG    1 
ATOM   9229  C  CD    . PRO A 1 2477 ? 147.358 89.166  166.544 1.00 100.52 ? 2477 PRO A CD    1 
ATOM   9230  N  N     . ASP A 1 2478 ? 144.511 86.812  165.259 1.00 113.02 ? 2478 ASP A N     1 
ATOM   9231  C  CA    . ASP A 1 2478 ? 143.424 85.859  165.051 1.00 116.59 ? 2478 ASP A CA    1 
ATOM   9232  C  C     . ASP A 1 2478 ? 142.221 86.518  164.388 1.00 116.72 ? 2478 ASP A C     1 
ATOM   9233  O  O     . ASP A 1 2478 ? 141.588 85.924  163.508 1.00 115.81 ? 2478 ASP A O     1 
ATOM   9234  C  CB    . ASP A 1 2478 ? 143.021 85.228  166.382 1.00 117.70 ? 2478 ASP A CB    1 
ATOM   9235  C  CG    . ASP A 1 2478 ? 144.175 84.525  167.066 1.00 119.97 ? 2478 ASP A CG    1 
ATOM   9236  O  OD1   . ASP A 1 2478 ? 145.299 84.558  166.524 1.00 116.03 ? 2478 ASP A OD1   1 
ATOM   9237  O  OD2   . ASP A 1 2478 ? 143.958 83.940  168.148 1.00 124.04 ? 2478 ASP A OD2   1 
ATOM   9238  N  N     . PHE A 1 2479 ? 141.889 87.743  164.797 1.00 113.88 ? 2479 PHE A N     1 
ATOM   9239  C  CA    . PHE A 1 2479 ? 140.730 88.469  164.281 1.00 112.05 ? 2479 PHE A CA    1 
ATOM   9240  C  C     . PHE A 1 2479 ? 141.196 89.751  163.605 1.00 111.96 ? 2479 PHE A C     1 
ATOM   9241  O  O     . PHE A 1 2479 ? 141.394 90.779  164.272 1.00 113.54 ? 2479 PHE A O     1 
ATOM   9242  C  CB    . PHE A 1 2479 ? 139.736 88.774  165.399 1.00 112.29 ? 2479 PHE A CB    1 
ATOM   9243  C  CG    . PHE A 1 2479 ? 138.502 89.492  164.932 1.00 118.63 ? 2479 PHE A CG    1 
ATOM   9244  C  CD1   . PHE A 1 2479 ? 137.482 88.806  164.295 1.00 117.98 ? 2479 PHE A CD1   1 
ATOM   9245  C  CD2   . PHE A 1 2479 ? 138.363 90.856  165.133 1.00 115.75 ? 2479 PHE A CD2   1 
ATOM   9246  C  CE1   . PHE A 1 2479 ? 136.346 89.467  163.867 1.00 115.79 ? 2479 PHE A CE1   1 
ATOM   9247  C  CE2   . PHE A 1 2479 ? 137.230 91.522  164.707 1.00 115.83 ? 2479 PHE A CE2   1 
ATOM   9248  C  CZ    . PHE A 1 2479 ? 136.220 90.826  164.075 1.00 115.17 ? 2479 PHE A CZ    1 
ATOM   9249  N  N     . PRO A 1 2480 ? 141.389 89.738  162.289 1.00 108.84 ? 2480 PRO A N     1 
ATOM   9250  C  CA    . PRO A 1 2480 ? 141.660 90.986  161.574 1.00 103.39 ? 2480 PRO A CA    1 
ATOM   9251  C  C     . PRO A 1 2480 ? 140.447 91.902  161.603 1.00 105.42 ? 2480 PRO A C     1 
ATOM   9252  O  O     . PRO A 1 2480 ? 139.299 91.461  161.686 1.00 107.97 ? 2480 PRO A O     1 
ATOM   9253  C  CB    . PRO A 1 2480 ? 141.976 90.521  160.150 1.00 105.24 ? 2480 PRO A CB    1 
ATOM   9254  C  CG    . PRO A 1 2480 ? 141.260 89.220  160.020 1.00 107.31 ? 2480 PRO A CG    1 
ATOM   9255  C  CD    . PRO A 1 2480 ? 141.326 88.581  161.381 1.00 110.15 ? 2480 PRO A CD    1 
ATOM   9256  N  N     . MET A 1 2481 ? 140.722 93.200  161.541 1.00 103.06 ? 2481 MET A N     1 
ATOM   9257  C  CA    . MET A 1 2481 ? 139.665 94.196  161.664 1.00 98.93  ? 2481 MET A CA    1 
ATOM   9258  C  C     . MET A 1 2481 ? 138.741 94.119  160.455 1.00 101.84 ? 2481 MET A C     1 
ATOM   9259  O  O     . MET A 1 2481 ? 139.153 94.408  159.328 1.00 103.04 ? 2481 MET A O     1 
ATOM   9260  C  CB    . MET A 1 2481 ? 140.287 95.584  161.798 1.00 91.97  ? 2481 MET A CB    1 
ATOM   9261  C  CG    . MET A 1 2481 ? 139.319 96.747  161.745 1.00 86.24  ? 2481 MET A CG    1 
ATOM   9262  S  SD    . MET A 1 2481 ? 140.055 98.162  162.588 1.00 87.59  ? 2481 MET A SD    1 
ATOM   9263  C  CE    . MET A 1 2481 ? 138.699 99.324  162.597 1.00 76.58  ? 2481 MET A CE    1 
ATOM   9264  N  N     . GLN A 1 2482 ? 137.492 93.725  160.693 1.00 106.20 ? 2482 GLN A N     1 
ATOM   9265  C  CA    . GLN A 1 2482 ? 136.571 93.427  159.607 1.00 105.70 ? 2482 GLN A CA    1 
ATOM   9266  C  C     . GLN A 1 2482 ? 136.188 94.689  158.840 1.00 99.88  ? 2482 GLN A C     1 
ATOM   9267  O  O     . GLN A 1 2482 ? 136.441 95.817  159.269 1.00 96.53  ? 2482 GLN A O     1 
ATOM   9268  C  CB    . GLN A 1 2482 ? 135.314 92.738  160.135 1.00 106.76 ? 2482 GLN A CB    1 
ATOM   9269  C  CG    . GLN A 1 2482 ? 135.570 91.367  160.724 1.00 109.44 ? 2482 GLN A CG    1 
ATOM   9270  C  CD    . GLN A 1 2482 ? 136.110 90.390  159.699 1.00 105.61 ? 2482 GLN A CD    1 
ATOM   9271  O  OE1   . GLN A 1 2482 ? 137.278 90.005  159.746 1.00 101.05 ? 2482 GLN A OE1   1 
ATOM   9272  N  NE2   . GLN A 1 2482 ? 135.261 89.985  158.763 1.00 99.71  ? 2482 GLN A NE2   1 
ATOM   9273  N  N     . ILE A 1 2483 ? 135.565 94.474  157.680 1.00 103.07 ? 2483 ILE A N     1 
ATOM   9274  C  CA    . ILE A 1 2483 ? 135.271 95.574  156.769 1.00 102.61 ? 2483 ILE A CA    1 
ATOM   9275  C  C     . ILE A 1 2483 ? 134.244 96.524  157.372 1.00 98.65  ? 2483 ILE A C     1 
ATOM   9276  O  O     . ILE A 1 2483 ? 134.384 97.745  157.267 1.00 98.20  ? 2483 ILE A O     1 
ATOM   9277  C  CB    . ILE A 1 2483 ? 134.810 95.029  155.406 1.00 109.42 ? 2483 ILE A CB    1 
ATOM   9278  C  CG1   . ILE A 1 2483 ? 135.824 94.018  154.870 1.00 110.91 ? 2483 ILE A CG1   1 
ATOM   9279  C  CG2   . ILE A 1 2483 ? 134.623 96.167  154.417 1.00 102.34 ? 2483 ILE A CG2   1 
ATOM   9280  C  CD1   . ILE A 1 2483 ? 137.238 94.555  154.787 1.00 103.57 ? 2483 ILE A CD1   1 
ATOM   9281  N  N     . GLU A 1 2484 ? 133.193 95.990  157.997 1.00 99.97  ? 2484 GLU A N     1 
ATOM   9282  C  CA    . GLU A 1 2484 ? 132.158 96.852  158.563 1.00 101.96 ? 2484 GLU A CA    1 
ATOM   9283  C  C     . GLU A 1 2484 ? 132.716 97.722  159.684 1.00 96.31  ? 2484 GLU A C     1 
ATOM   9284  O  O     . GLU A 1 2484 ? 132.496 98.942  159.712 1.00 94.38  ? 2484 GLU A O     1 
ATOM   9285  C  CB    . GLU A 1 2484 ? 130.992 96.002  159.070 1.00 106.52 ? 2484 GLU A CB    1 
ATOM   9286  C  CG    . GLU A 1 2484 ? 129.870 96.800  159.712 1.00 104.18 ? 2484 GLU A CG    1 
ATOM   9287  C  CD    . GLU A 1 2484 ? 129.366 97.916  158.819 1.00 109.76 ? 2484 GLU A CD    1 
ATOM   9288  O  OE1   . GLU A 1 2484 ? 128.910 97.618  157.695 1.00 111.33 ? 2484 GLU A OE1   1 
ATOM   9289  O  OE2   . GLU A 1 2484 ? 129.422 99.089  159.240 1.00 106.18 ? 2484 GLU A OE2   1 
ATOM   9290  N  N     . GLN A 1 2485 ? 133.447 97.108  160.617 1.00 92.80  ? 2485 GLN A N     1 
ATOM   9291  C  CA    . GLN A 1 2485 ? 134.058 97.863  161.704 1.00 88.80  ? 2485 GLN A CA    1 
ATOM   9292  C  C     . GLN A 1 2485 ? 135.047 98.888  161.171 1.00 84.80  ? 2485 GLN A C     1 
ATOM   9293  O  O     . GLN A 1 2485 ? 135.125 100.011 161.679 1.00 82.43  ? 2485 GLN A O     1 
ATOM   9294  C  CB    . GLN A 1 2485 ? 134.756 96.912  162.674 1.00 90.02  ? 2485 GLN A CB    1 
ATOM   9295  C  CG    . GLN A 1 2485 ? 135.318 97.590  163.909 1.00 81.16  ? 2485 GLN A CG    1 
ATOM   9296  C  CD    . GLN A 1 2485 ? 136.201 96.670  164.721 1.00 78.72  ? 2485 GLN A CD    1 
ATOM   9297  O  OE1   . GLN A 1 2485 ? 137.348 96.997  165.020 1.00 79.07  ? 2485 GLN A OE1   1 
ATOM   9298  N  NE2   . GLN A 1 2485 ? 135.673 95.506  165.078 1.00 84.40  ? 2485 GLN A NE2   1 
ATOM   9299  N  N     . LEU A 1 2486 ? 135.819 98.511  160.151 1.00 84.62  ? 2486 LEU A N     1 
ATOM   9300  C  CA    . LEU A 1 2486 ? 136.819 99.418  159.601 1.00 76.71  ? 2486 LEU A CA    1 
ATOM   9301  C  C     . LEU A 1 2486 ? 136.155 100.601 158.903 1.00 71.82  ? 2486 LEU A C     1 
ATOM   9302  O  O     . LEU A 1 2486 ? 136.622 101.739 159.019 1.00 71.59  ? 2486 LEU A O     1 
ATOM   9303  C  CB    . LEU A 1 2486 ? 137.748 98.629  158.673 1.00 81.75  ? 2486 LEU A CB    1 
ATOM   9304  C  CG    . LEU A 1 2486 ? 139.031 99.190  158.062 1.00 75.55  ? 2486 LEU A CG    1 
ATOM   9305  C  CD1   . LEU A 1 2486 ? 140.016 98.060  157.847 1.00 72.29  ? 2486 LEU A CD1   1 
ATOM   9306  C  CD2   . LEU A 1 2486 ? 138.734 99.806  156.740 1.00 73.30  ? 2486 LEU A CD2   1 
ATOM   9307  N  N     . GLU A 1 2487 ? 135.031 100.359 158.222 1.00 78.28  ? 2487 GLU A N     1 
ATOM   9308  C  CA    . GLU A 1 2487 ? 134.254 101.449 157.636 1.00 79.76  ? 2487 GLU A CA    1 
ATOM   9309  C  C     . GLU A 1 2487 ? 133.734 102.397 158.709 1.00 76.01  ? 2487 GLU A C     1 
ATOM   9310  O  O     . GLU A 1 2487 ? 133.862 103.621 158.584 1.00 76.18  ? 2487 GLU A O     1 
ATOM   9311  C  CB    . GLU A 1 2487 ? 133.086 100.892 156.819 1.00 85.72  ? 2487 GLU A CB    1 
ATOM   9312  C  CG    . GLU A 1 2487 ? 133.479 100.125 155.571 1.00 93.05  ? 2487 GLU A CG    1 
ATOM   9313  C  CD    . GLU A 1 2487 ? 132.411 100.178 154.496 1.00 100.98 ? 2487 GLU A CD    1 
ATOM   9314  O  OE1   . GLU A 1 2487 ? 132.176 101.271 153.938 1.00 96.72  ? 2487 GLU A OE1   1 
ATOM   9315  O  OE2   . GLU A 1 2487 ? 131.805 99.124  154.209 1.00 107.67 ? 2487 GLU A OE2   1 
ATOM   9316  N  N     . ARG A 1 2488 ? 133.127 101.849 159.767 1.00 77.98  ? 2488 ARG A N     1 
ATOM   9317  C  CA    . ARG A 1 2488 ? 132.615 102.703 160.839 1.00 76.32  ? 2488 ARG A CA    1 
ATOM   9318  C  C     . ARG A 1 2488 ? 133.733 103.532 161.455 1.00 68.49  ? 2488 ARG A C     1 
ATOM   9319  O  O     . ARG A 1 2488 ? 133.605 104.754 161.619 1.00 68.73  ? 2488 ARG A O     1 
ATOM   9320  C  CB    . ARG A 1 2488 ? 131.932 101.865 161.920 1.00 80.52  ? 2488 ARG A CB    1 
ATOM   9321  C  CG    . ARG A 1 2488 ? 130.856 100.924 161.431 1.00 87.44  ? 2488 ARG A CG    1 
ATOM   9322  C  CD    . ARG A 1 2488 ? 130.095 100.332 162.603 1.00 88.72  ? 2488 ARG A CD    1 
ATOM   9323  N  NE    . ARG A 1 2488 ? 130.949 100.174 163.775 1.00 86.86  ? 2488 ARG A NE    1 
ATOM   9324  C  CZ    . ARG A 1 2488 ? 131.202 99.016  164.369 1.00 90.71  ? 2488 ARG A CZ    1 
ATOM   9325  N  NH1   . ARG A 1 2488 ? 130.689 97.882  163.922 1.00 95.74  ? 2488 ARG A NH1   1 
ATOM   9326  N  NH2   . ARG A 1 2488 ? 131.993 98.995  165.438 1.00 83.80  ? 2488 ARG A NH2   1 
ATOM   9327  N  N     . TYR A 1 2489 ? 134.845 102.877 161.791 1.00 62.17  ? 2489 TYR A N     1 
ATOM   9328  C  CA    . TYR A 1 2489 ? 135.956 103.569 162.428 1.00 59.00  ? 2489 TYR A CA    1 
ATOM   9329  C  C     . TYR A 1 2489 ? 136.509 104.662 161.531 1.00 59.93  ? 2489 TYR A C     1 
ATOM   9330  O  O     . TYR A 1 2489 ? 136.812 105.760 162.003 1.00 59.70  ? 2489 TYR A O     1 
ATOM   9331  C  CB    . TYR A 1 2489 ? 137.054 102.574 162.792 1.00 57.70  ? 2489 TYR A CB    1 
ATOM   9332  C  CG    . TYR A 1 2489 ? 138.332 103.227 163.261 1.00 55.33  ? 2489 TYR A CG    1 
ATOM   9333  C  CD1   . TYR A 1 2489 ? 138.318 104.172 164.271 1.00 57.49  ? 2489 TYR A CD1   1 
ATOM   9334  C  CD2   . TYR A 1 2489 ? 139.551 102.898 162.694 1.00 56.76  ? 2489 TYR A CD2   1 
ATOM   9335  C  CE1   . TYR A 1 2489 ? 139.478 104.775 164.703 1.00 57.98  ? 2489 TYR A CE1   1 
ATOM   9336  C  CE2   . TYR A 1 2489 ? 140.719 103.495 163.122 1.00 58.54  ? 2489 TYR A CE2   1 
ATOM   9337  C  CZ    . TYR A 1 2489 ? 140.676 104.431 164.127 1.00 59.16  ? 2489 TYR A CZ    1 
ATOM   9338  O  OH    . TYR A 1 2489 ? 141.837 105.029 164.556 1.00 62.84  ? 2489 TYR A OH    1 
ATOM   9339  N  N     . ILE A 1 2490 ? 136.640 104.390 160.233 1.00 63.30  ? 2490 ILE A N     1 
ATOM   9340  C  CA    . ILE A 1 2490 ? 137.266 105.365 159.351 1.00 55.06  ? 2490 ILE A CA    1 
ATOM   9341  C  C     . ILE A 1 2490 ? 136.333 106.538 159.078 1.00 58.78  ? 2490 ILE A C     1 
ATOM   9342  O  O     . ILE A 1 2490 ? 136.783 107.683 158.993 1.00 65.29  ? 2490 ILE A O     1 
ATOM   9343  C  CB    . ILE A 1 2490 ? 137.752 104.679 158.067 1.00 53.09  ? 2490 ILE A CB    1 
ATOM   9344  C  CG1   . ILE A 1 2490 ? 139.094 104.015 158.356 1.00 56.59  ? 2490 ILE A CG1   1 
ATOM   9345  C  CG2   . ILE A 1 2490 ? 137.879 105.671 156.933 1.00 59.54  ? 2490 ILE A CG2   1 
ATOM   9346  C  CD1   . ILE A 1 2490 ? 139.559 103.104 157.291 1.00 69.40  ? 2490 ILE A CD1   1 
ATOM   9347  N  N     . GLN A 1 2491 ? 135.026 106.293 158.960 1.00 60.14  ? 2491 GLN A N     1 
ATOM   9348  C  CA    . GLN A 1 2491 ? 134.095 107.413 158.824 1.00 58.26  ? 2491 GLN A CA    1 
ATOM   9349  C  C     . GLN A 1 2491 ? 134.118 108.295 160.069 1.00 61.35  ? 2491 GLN A C     1 
ATOM   9350  O  O     . GLN A 1 2491 ? 134.202 109.532 159.978 1.00 62.27  ? 2491 GLN A O     1 
ATOM   9351  C  CB    . GLN A 1 2491 ? 132.682 106.895 158.559 1.00 62.79  ? 2491 GLN A CB    1 
ATOM   9352  C  CG    . GLN A 1 2491 ? 132.530 106.132 157.258 1.00 71.91  ? 2491 GLN A CG    1 
ATOM   9353  C  CD    . GLN A 1 2491 ? 131.176 105.465 157.133 1.00 76.53  ? 2491 GLN A CD    1 
ATOM   9354  O  OE1   . GLN A 1 2491 ? 130.466 105.658 156.147 1.00 79.53  ? 2491 GLN A OE1   1 
ATOM   9355  N  NE2   . GLN A 1 2491 ? 130.809 104.678 158.136 1.00 78.47  ? 2491 GLN A NE2   1 
ATOM   9356  N  N     . ARG A 1 2492 ? 134.057 107.671 161.249 1.00 63.45  ? 2492 ARG A N     1 
ATOM   9357  C  CA    . ARG A 1 2492 ? 134.079 108.442 162.486 1.00 60.00  ? 2492 ARG A CA    1 
ATOM   9358  C  C     . ARG A 1 2492 ? 135.387 109.210 162.633 1.00 55.49  ? 2492 ARG A C     1 
ATOM   9359  O  O     . ARG A 1 2492 ? 135.388 110.382 163.026 1.00 55.09  ? 2492 ARG A O     1 
ATOM   9360  C  CB    . ARG A 1 2492 ? 133.863 107.515 163.678 1.00 61.45  ? 2492 ARG A CB    1 
ATOM   9361  C  CG    . ARG A 1 2492 ? 132.439 107.441 164.185 1.00 69.24  ? 2492 ARG A CG    1 
ATOM   9362  C  CD    . ARG A 1 2492 ? 131.656 106.334 163.515 1.00 74.47  ? 2492 ARG A CD    1 
ATOM   9363  N  NE    . ARG A 1 2492 ? 130.492 105.952 164.304 1.00 83.30  ? 2492 ARG A NE    1 
ATOM   9364  C  CZ    . ARG A 1 2492 ? 129.662 104.968 163.986 1.00 87.80  ? 2492 ARG A CZ    1 
ATOM   9365  N  NH1   . ARG A 1 2492 ? 129.832 104.248 162.890 1.00 83.83  ? 2492 ARG A NH1   1 
ATOM   9366  N  NH2   . ARG A 1 2492 ? 128.636 104.701 164.789 1.00 92.10  ? 2492 ARG A NH2   1 
ATOM   9367  N  N     . TYR A 1 2493 ? 136.513 108.568 162.312 1.00 49.41  ? 2493 TYR A N     1 
ATOM   9368  C  CA    . TYR A 1 2493 ? 137.803 109.236 162.414 1.00 45.40  ? 2493 TYR A CA    1 
ATOM   9369  C  C     . TYR A 1 2493 ? 137.952 110.325 161.365 1.00 48.56  ? 2493 TYR A C     1 
ATOM   9370  O  O     . TYR A 1 2493 ? 138.661 111.302 161.596 1.00 55.49  ? 2493 TYR A O     1 
ATOM   9371  C  CB    . TYR A 1 2493 ? 138.937 108.219 162.290 1.00 40.06  ? 2493 TYR A CB    1 
ATOM   9372  C  CG    . TYR A 1 2493 ? 140.229 108.654 162.946 1.00 42.86  ? 2493 TYR A CG    1 
ATOM   9373  C  CD1   . TYR A 1 2493 ? 141.009 109.661 162.395 1.00 43.57  ? 2493 TYR A CD1   1 
ATOM   9374  C  CD2   . TYR A 1 2493 ? 140.669 108.056 164.116 1.00 52.13  ? 2493 TYR A CD2   1 
ATOM   9375  C  CE1   . TYR A 1 2493 ? 142.187 110.058 162.989 1.00 42.81  ? 2493 TYR A CE1   1 
ATOM   9376  C  CE2   . TYR A 1 2493 ? 141.847 108.447 164.718 1.00 55.74  ? 2493 TYR A CE2   1 
ATOM   9377  C  CZ    . TYR A 1 2493 ? 142.602 109.449 164.150 1.00 53.52  ? 2493 TYR A CZ    1 
ATOM   9378  O  OH    . TYR A 1 2493 ? 143.777 109.843 164.746 1.00 56.65  ? 2493 TYR A OH    1 
ATOM   9379  N  N     . LEU A 1 2494 ? 137.303 110.182 160.211 1.00 49.27  ? 2494 LEU A N     1 
ATOM   9380  C  CA    . LEU A 1 2494 ? 137.308 111.264 159.236 1.00 46.56  ? 2494 LEU A CA    1 
ATOM   9381  C  C     . LEU A 1 2494 ? 136.579 112.483 159.776 1.00 46.71  ? 2494 LEU A C     1 
ATOM   9382  O  O     . LEU A 1 2494 ? 137.044 113.614 159.606 1.00 52.43  ? 2494 LEU A O     1 
ATOM   9383  C  CB    . LEU A 1 2494 ? 136.683 110.796 157.926 1.00 49.41  ? 2494 LEU A CB    1 
ATOM   9384  C  CG    . LEU A 1 2494 ? 136.621 111.848 156.821 1.00 49.29  ? 2494 LEU A CG    1 
ATOM   9385  C  CD1   . LEU A 1 2494 ? 138.006 112.373 156.495 1.00 47.20  ? 2494 LEU A CD1   1 
ATOM   9386  C  CD2   . LEU A 1 2494 ? 135.984 111.250 155.595 1.00 59.53  ? 2494 LEU A CD2   1 
ATOM   9387  N  N     . VAL A 1 2495 ? 135.440 112.273 160.440 1.00 47.64  ? 2495 VAL A N     1 
ATOM   9388  C  CA    . VAL A 1 2495 ? 134.757 113.401 161.076 1.00 45.66  ? 2495 VAL A CA    1 
ATOM   9389  C  C     . VAL A 1 2495 ? 135.634 114.013 162.166 1.00 44.05  ? 2495 VAL A C     1 
ATOM   9390  O  O     . VAL A 1 2495 ? 135.761 115.241 162.274 1.00 43.82  ? 2495 VAL A O     1 
ATOM   9391  C  CB    . VAL A 1 2495 ? 133.391 112.959 161.628 1.00 47.33  ? 2495 VAL A CB    1 
ATOM   9392  C  CG1   . VAL A 1 2495 ? 132.771 114.068 162.456 1.00 43.01  ? 2495 VAL A CG1   1 
ATOM   9393  C  CG2   . VAL A 1 2495 ? 132.480 112.581 160.490 1.00 54.34  ? 2495 VAL A CG2   1 
ATOM   9394  N  N     . TYR A 1 2496 ? 136.251 113.160 162.986 1.00 43.32  ? 2496 TYR A N     1 
ATOM   9395  C  CA    . TYR A 1 2496 ? 137.154 113.613 164.042 1.00 40.63  ? 2496 TYR A CA    1 
ATOM   9396  C  C     . TYR A 1 2496 ? 138.292 114.455 163.473 1.00 39.36  ? 2496 TYR A C     1 
ATOM   9397  O  O     . TYR A 1 2496 ? 138.597 115.543 163.981 1.00 42.98  ? 2496 TYR A O     1 
ATOM   9398  C  CB    . TYR A 1 2496 ? 137.691 112.385 164.781 1.00 44.44  ? 2496 TYR A CB    1 
ATOM   9399  C  CG    . TYR A 1 2496 ? 138.756 112.634 165.821 1.00 46.56  ? 2496 TYR A CG    1 
ATOM   9400  C  CD1   . TYR A 1 2496 ? 138.452 113.235 167.032 1.00 55.78  ? 2496 TYR A CD1   1 
ATOM   9401  C  CD2   . TYR A 1 2496 ? 140.066 112.236 165.599 1.00 42.34  ? 2496 TYR A CD2   1 
ATOM   9402  C  CE1   . TYR A 1 2496 ? 139.427 113.447 167.985 1.00 54.33  ? 2496 TYR A CE1   1 
ATOM   9403  C  CE2   . TYR A 1 2496 ? 141.046 112.445 166.543 1.00 43.00  ? 2496 TYR A CE2   1 
ATOM   9404  C  CZ    . TYR A 1 2496 ? 140.722 113.051 167.734 1.00 50.12  ? 2496 TYR A CZ    1 
ATOM   9405  O  OH    . TYR A 1 2496 ? 141.701 113.260 168.677 1.00 57.03  ? 2496 TYR A OH    1 
ATOM   9406  N  N     . ALA A 1 2497 ? 138.919 113.969 162.404 1.00 39.21  ? 2497 ALA A N     1 
ATOM   9407  C  CA    . ALA A 1 2497 ? 140.044 114.658 161.791 1.00 33.43  ? 2497 ALA A CA    1 
ATOM   9408  C  C     . ALA A 1 2497 ? 139.610 115.959 161.134 1.00 34.86  ? 2497 ALA A C     1 
ATOM   9409  O  O     . ALA A 1 2497 ? 140.349 116.946 161.167 1.00 38.28  ? 2497 ALA A O     1 
ATOM   9410  C  CB    . ALA A 1 2497 ? 140.717 113.740 160.774 1.00 32.19  ? 2497 ALA A CB    1 
ATOM   9411  N  N     . ILE A 1 2498 ? 138.423 115.982 160.527 1.00 37.84  ? 2498 ILE A N     1 
ATOM   9412  C  CA    . ILE A 1 2498 ? 137.916 117.221 159.945 1.00 38.94  ? 2498 ILE A CA    1 
ATOM   9413  C  C     . ILE A 1 2498 ? 137.724 118.270 161.031 1.00 36.61  ? 2498 ILE A C     1 
ATOM   9414  O  O     . ILE A 1 2498 ? 138.134 119.428 160.883 1.00 38.09  ? 2498 ILE A O     1 
ATOM   9415  C  CB    . ILE A 1 2498 ? 136.611 116.956 159.174 1.00 36.99  ? 2498 ILE A CB    1 
ATOM   9416  C  CG1   . ILE A 1 2498 ? 136.917 116.325 157.816 1.00 36.90  ? 2498 ILE A CG1   1 
ATOM   9417  C  CG2   . ILE A 1 2498 ? 135.821 118.240 158.997 1.00 34.76  ? 2498 ILE A CG2   1 
ATOM   9418  C  CD1   . ILE A 1 2498 ? 135.693 116.074 156.976 1.00 43.85  ? 2498 ILE A CD1   1 
ATOM   9419  N  N     . LEU A 1 2499 ? 137.120 117.870 162.152 1.00 37.10  ? 2499 LEU A N     1 
ATOM   9420  C  CA    . LEU A 1 2499 ? 136.909 118.812 163.247 1.00 37.79  ? 2499 LEU A CA    1 
ATOM   9421  C  C     . LEU A 1 2499 ? 138.232 119.314 163.811 1.00 39.85  ? 2499 LEU A C     1 
ATOM   9422  O  O     . LEU A 1 2499 ? 138.378 120.503 164.112 1.00 42.14  ? 2499 LEU A O     1 
ATOM   9423  C  CB    . LEU A 1 2499 ? 136.069 118.167 164.348 1.00 39.88  ? 2499 LEU A CB    1 
ATOM   9424  C  CG    . LEU A 1 2499 ? 134.609 117.882 164.007 1.00 42.07  ? 2499 LEU A CG    1 
ATOM   9425  C  CD1   . LEU A 1 2499 ? 133.846 117.550 165.266 1.00 46.35  ? 2499 LEU A CD1   1 
ATOM   9426  C  CD2   . LEU A 1 2499 ? 133.988 119.073 163.306 1.00 47.50  ? 2499 LEU A CD2   1 
ATOM   9427  N  N     . TRP A 1 2500 ? 139.211 118.422 163.966 1.00 38.73  ? 2500 TRP A N     1 
ATOM   9428  C  CA    . TRP A 1 2500 ? 140.460 118.822 164.601 1.00 34.97  ? 2500 TRP A CA    1 
ATOM   9429  C  C     . TRP A 1 2500 ? 141.444 119.482 163.646 1.00 37.85  ? 2500 TRP A C     1 
ATOM   9430  O  O     . TRP A 1 2500 ? 142.419 120.084 164.107 1.00 40.35  ? 2500 TRP A O     1 
ATOM   9431  C  CB    . TRP A 1 2500 ? 141.120 117.618 165.271 1.00 31.69  ? 2500 TRP A CB    1 
ATOM   9432  C  CG    . TRP A 1 2500 ? 140.858 117.572 166.735 1.00 38.42  ? 2500 TRP A CG    1 
ATOM   9433  C  CD1   . TRP A 1 2500 ? 140.269 116.561 167.430 1.00 42.78  ? 2500 TRP A CD1   1 
ATOM   9434  C  CD2   . TRP A 1 2500 ? 141.163 118.593 167.692 1.00 43.07  ? 2500 TRP A CD2   1 
ATOM   9435  N  NE1   . TRP A 1 2500 ? 140.194 116.883 168.762 1.00 46.82  ? 2500 TRP A NE1   1 
ATOM   9436  C  CE2   . TRP A 1 2500 ? 140.736 118.127 168.948 1.00 42.98  ? 2500 TRP A CE2   1 
ATOM   9437  C  CE3   . TRP A 1 2500 ? 141.760 119.854 167.608 1.00 45.33  ? 2500 TRP A CE3   1 
ATOM   9438  C  CZ2   . TRP A 1 2500 ? 140.885 118.877 170.108 1.00 40.90  ? 2500 TRP A CZ2   1 
ATOM   9439  C  CZ3   . TRP A 1 2500 ? 141.906 120.595 168.761 1.00 42.89  ? 2500 TRP A CZ3   1 
ATOM   9440  C  CH2   . TRP A 1 2500 ? 141.472 120.104 169.994 1.00 44.72  ? 2500 TRP A CH2   1 
ATOM   9441  N  N     . SER A 1 2501 ? 141.219 119.392 162.338 1.00 36.84  ? 2501 SER A N     1 
ATOM   9442  C  CA    . SER A 1 2501 ? 142.083 120.038 161.361 1.00 30.94  ? 2501 SER A CA    1 
ATOM   9443  C  C     . SER A 1 2501 ? 141.540 121.369 160.878 1.00 36.13  ? 2501 SER A C     1 
ATOM   9444  O  O     . SER A 1 2501 ? 142.318 122.310 160.690 1.00 45.18  ? 2501 SER A O     1 
ATOM   9445  C  CB    . SER A 1 2501 ? 142.291 119.122 160.153 1.00 30.13  ? 2501 SER A CB    1 
ATOM   9446  O  OG    . SER A 1 2501 ? 142.722 117.839 160.563 1.00 38.23  ? 2501 SER A OG    1 
ATOM   9447  N  N     . LEU A 1 2502 ? 140.229 121.473 160.675 1.00 36.31  ? 2502 LEU A N     1 
ATOM   9448  C  CA    . LEU A 1 2502 ? 139.641 122.722 160.216 1.00 35.10  ? 2502 LEU A CA    1 
ATOM   9449  C  C     . LEU A 1 2502 ? 139.386 123.692 161.361 1.00 39.46  ? 2502 LEU A C     1 
ATOM   9450  O  O     . LEU A 1 2502 ? 139.538 124.904 161.186 1.00 48.22  ? 2502 LEU A O     1 
ATOM   9451  C  CB    . LEU A 1 2502 ? 138.341 122.438 159.465 1.00 36.81  ? 2502 LEU A CB    1 
ATOM   9452  C  CG    . LEU A 1 2502 ? 138.443 121.416 158.331 1.00 37.75  ? 2502 LEU A CG    1 
ATOM   9453  C  CD1   . LEU A 1 2502 ? 137.149 121.353 157.569 1.00 41.35  ? 2502 LEU A CD1   1 
ATOM   9454  C  CD2   . LEU A 1 2502 ? 139.578 121.751 157.392 1.00 36.10  ? 2502 LEU A CD2   1 
ATOM   9455  N  N     . SER A 1 2503 ? 139.006 123.185 162.532 1.00 40.44  ? 2503 SER A N     1 
ATOM   9456  C  CA    . SER A 1 2503 ? 138.711 124.019 163.687 1.00 39.68  ? 2503 SER A CA    1 
ATOM   9457  C  C     . SER A 1 2503 ? 139.758 123.903 164.787 1.00 44.44  ? 2503 SER A C     1 
ATOM   9458  O  O     . SER A 1 2503 ? 139.477 124.267 165.932 1.00 50.24  ? 2503 SER A O     1 
ATOM   9459  C  CB    . SER A 1 2503 ? 137.332 123.672 164.248 1.00 44.08  ? 2503 SER A CB    1 
ATOM   9460  O  OG    . SER A 1 2503 ? 137.326 122.369 164.800 1.00 50.27  ? 2503 SER A OG    1 
ATOM   9461  N  N     . GLY A 1 2504 ? 140.952 123.402 164.473 1.00 43.98  ? 2504 GLY A N     1 
ATOM   9462  C  CA    . GLY A 1 2504 ? 141.989 123.307 165.489 1.00 38.04  ? 2504 GLY A CA    1 
ATOM   9463  C  C     . GLY A 1 2504 ? 142.435 124.665 165.995 1.00 37.77  ? 2504 GLY A C     1 
ATOM   9464  O  O     . GLY A 1 2504 ? 142.727 124.831 167.180 1.00 39.02  ? 2504 GLY A O     1 
ATOM   9465  N  N     . ASP A 1 2505 ? 142.501 125.653 165.100 1.00 38.60  ? 2505 ASP A N     1 
ATOM   9466  C  CA    . ASP A 1 2505 ? 142.863 127.010 165.492 1.00 35.61  ? 2505 ASP A CA    1 
ATOM   9467  C  C     . ASP A 1 2505 ? 141.716 127.742 166.163 1.00 45.21  ? 2505 ASP A C     1 
ATOM   9468  O  O     . ASP A 1 2505 ? 141.940 128.742 166.853 1.00 55.34  ? 2505 ASP A O     1 
ATOM   9469  C  CB    . ASP A 1 2505 ? 143.299 127.812 164.273 1.00 39.69  ? 2505 ASP A CB    1 
ATOM   9470  C  CG    . ASP A 1 2505 ? 144.594 127.336 163.710 1.00 53.00  ? 2505 ASP A CG    1 
ATOM   9471  O  OD1   . ASP A 1 2505 ? 145.407 126.817 164.494 1.00 53.21  ? 2505 ASP A OD1   1 
ATOM   9472  O  OD2   . ASP A 1 2505 ? 144.799 127.482 162.491 1.00 58.31  ? 2505 ASP A OD2   1 
ATOM   9473  N  N     . SER A 1 2506 ? 140.491 127.282 165.954 1.00 41.39  ? 2506 SER A N     1 
ATOM   9474  C  CA    . SER A 1 2506 ? 139.334 128.031 166.399 1.00 41.41  ? 2506 SER A CA    1 
ATOM   9475  C  C     . SER A 1 2506 ? 139.130 127.878 167.901 1.00 44.66  ? 2506 SER A C     1 
ATOM   9476  O  O     . SER A 1 2506 ? 139.609 126.933 168.532 1.00 42.96  ? 2506 SER A O     1 
ATOM   9477  C  CB    . SER A 1 2506 ? 138.091 127.569 165.645 1.00 51.40  ? 2506 SER A CB    1 
ATOM   9478  O  OG    . SER A 1 2506 ? 138.200 127.859 164.264 1.00 55.57  ? 2506 SER A OG    1 
ATOM   9479  N  N     . ARG A 1 2507 ? 138.406 128.836 168.473 1.00 51.23  ? 2507 ARG A N     1 
ATOM   9480  C  CA    . ARG A 1 2507 ? 138.008 128.754 169.867 1.00 50.17  ? 2507 ARG A CA    1 
ATOM   9481  C  C     . ARG A 1 2507 ? 137.017 127.606 170.046 1.00 57.93  ? 2507 ARG A C     1 
ATOM   9482  O  O     . ARG A 1 2507 ? 136.574 126.973 169.084 1.00 64.78  ? 2507 ARG A O     1 
ATOM   9483  C  CB    . ARG A 1 2507 ? 137.405 130.079 170.329 1.00 47.93  ? 2507 ARG A CB    1 
ATOM   9484  C  CG    . ARG A 1 2507 ? 138.037 131.329 169.721 1.00 56.07  ? 2507 ARG A CG    1 
ATOM   9485  C  CD    . ARG A 1 2507 ? 139.547 131.360 169.912 1.00 64.73  ? 2507 ARG A CD    1 
ATOM   9486  N  NE    . ARG A 1 2507 ? 140.199 132.368 169.084 1.00 67.26  ? 2507 ARG A NE    1 
ATOM   9487  C  CZ    . ARG A 1 2507 ? 140.194 133.669 169.340 1.00 73.97  ? 2507 ARG A CZ    1 
ATOM   9488  N  NH1   . ARG A 1 2507 ? 139.582 134.163 170.404 1.00 72.30  ? 2507 ARG A NH1   1 
ATOM   9489  N  NH2   . ARG A 1 2507 ? 140.822 134.496 168.509 1.00 78.02  ? 2507 ARG A NH2   1 
ATOM   9490  N  N     . LEU A 1 2508 ? 136.656 127.331 171.300 1.00 57.87  ? 2508 LEU A N     1 
ATOM   9491  C  CA    . LEU A 1 2508 ? 135.727 126.238 171.566 1.00 56.30  ? 2508 LEU A CA    1 
ATOM   9492  C  C     . LEU A 1 2508 ? 134.360 126.517 170.954 1.00 57.33  ? 2508 LEU A C     1 
ATOM   9493  O  O     . LEU A 1 2508 ? 133.675 125.594 170.495 1.00 60.25  ? 2508 LEU A O     1 
ATOM   9494  C  CB    . LEU A 1 2508 ? 135.606 125.997 173.071 1.00 64.05  ? 2508 LEU A CB    1 
ATOM   9495  C  CG    . LEU A 1 2508 ? 136.677 125.145 173.767 1.00 68.12  ? 2508 LEU A CG    1 
ATOM   9496  C  CD1   . LEU A 1 2508 ? 136.643 123.712 173.252 1.00 61.47  ? 2508 LEU A CD1   1 
ATOM   9497  C  CD2   . LEU A 1 2508 ? 138.078 125.736 173.638 1.00 62.62  ? 2508 LEU A CD2   1 
ATOM   9498  N  N     . LYS A 1 2509 ? 133.951 127.788 170.927 1.00 58.73  ? 2509 LYS A N     1 
ATOM   9499  C  CA    . LYS A 1 2509 ? 132.677 128.145 170.312 1.00 62.38  ? 2509 LYS A CA    1 
ATOM   9500  C  C     . LYS A 1 2509 ? 132.672 127.809 168.827 1.00 62.71  ? 2509 LYS A C     1 
ATOM   9501  O  O     . LYS A 1 2509 ? 131.709 127.231 168.311 1.00 64.92  ? 2509 LYS A O     1 
ATOM   9502  C  CB    . LYS A 1 2509 ? 132.391 129.631 170.527 1.00 66.93  ? 2509 LYS A CB    1 
ATOM   9503  C  CG    . LYS A 1 2509 ? 131.484 130.243 169.471 1.00 66.02  ? 2509 LYS A CG    1 
ATOM   9504  C  CD    . LYS A 1 2509 ? 130.935 131.588 169.914 1.00 73.05  ? 2509 LYS A CD    1 
ATOM   9505  C  CE    . LYS A 1 2509 ? 131.932 132.704 169.647 1.00 78.24  ? 2509 LYS A CE    1 
ATOM   9506  N  NZ    . LYS A 1 2509 ? 131.285 134.043 169.674 1.00 72.00  ? 2509 LYS A NZ    1 
ATOM   9507  N  N     . MET A 1 2510 ? 133.750 128.150 168.122 1.00 59.56  ? 2510 MET A N     1 
ATOM   9508  C  CA    . MET A 1 2510 ? 133.799 127.886 166.690 1.00 53.18  ? 2510 MET A CA    1 
ATOM   9509  C  C     . MET A 1 2510 ? 134.014 126.408 166.393 1.00 52.71  ? 2510 MET A C     1 
ATOM   9510  O  O     . MET A 1 2510 ? 133.540 125.911 165.366 1.00 62.54  ? 2510 MET A O     1 
ATOM   9511  C  CB    . MET A 1 2510 ? 134.887 128.738 166.042 1.00 44.09  ? 2510 MET A CB    1 
ATOM   9512  C  CG    . MET A 1 2510 ? 134.619 130.226 166.156 1.00 56.83  ? 2510 MET A CG    1 
ATOM   9513  S  SD    . MET A 1 2510 ? 133.266 130.785 165.107 1.00 84.11  ? 2510 MET A SD    1 
ATOM   9514  C  CE    . MET A 1 2510 ? 133.483 132.558 165.202 1.00 65.77  ? 2510 MET A CE    1 
ATOM   9515  N  N     . ARG A 1 2511 ? 134.704 125.688 167.280 1.00 49.63  ? 2511 ARG A N     1 
ATOM   9516  C  CA    . ARG A 1 2511 ? 134.755 124.235 167.161 1.00 49.31  ? 2511 ARG A CA    1 
ATOM   9517  C  C     . ARG A 1 2511 ? 133.360 123.636 167.274 1.00 55.32  ? 2511 ARG A C     1 
ATOM   9518  O  O     . ARG A 1 2511 ? 132.998 122.731 166.512 1.00 59.74  ? 2511 ARG A O     1 
ATOM   9519  C  CB    . ARG A 1 2511 ? 135.673 123.649 168.232 1.00 49.69  ? 2511 ARG A CB    1 
ATOM   9520  C  CG    . ARG A 1 2511 ? 137.138 123.987 168.054 1.00 49.40  ? 2511 ARG A CG    1 
ATOM   9521  C  CD    . ARG A 1 2511 ? 137.948 123.548 169.259 1.00 51.50  ? 2511 ARG A CD    1 
ATOM   9522  N  NE    . ARG A 1 2511 ? 139.347 123.937 169.153 1.00 48.45  ? 2511 ARG A NE    1 
ATOM   9523  C  CZ    . ARG A 1 2511 ? 140.258 123.707 170.087 1.00 48.57  ? 2511 ARG A CZ    1 
ATOM   9524  N  NH1   . ARG A 1 2511 ? 139.952 123.083 171.211 1.00 57.81  ? 2511 ARG A NH1   1 
ATOM   9525  N  NH2   . ARG A 1 2511 ? 141.507 124.116 169.890 1.00 44.18  ? 2511 ARG A NH2   1 
ATOM   9526  N  N     . ALA A 1 2512 ? 132.557 124.141 168.214 1.00 56.36  ? 2512 ALA A N     1 
ATOM   9527  C  CA    . ALA A 1 2512 ? 131.177 123.682 168.335 1.00 59.35  ? 2512 ALA A CA    1 
ATOM   9528  C  C     . ALA A 1 2512 ? 130.364 124.042 167.098 1.00 61.24  ? 2512 ALA A C     1 
ATOM   9529  O  O     . ALA A 1 2512 ? 129.516 123.260 166.655 1.00 64.21  ? 2512 ALA A O     1 
ATOM   9530  C  CB    . ALA A 1 2512 ? 130.536 124.273 169.590 1.00 56.74  ? 2512 ALA A CB    1 
ATOM   9531  N  N     . GLU A 1 2513 ? 130.595 125.231 166.538 1.00 57.34  ? 2513 GLU A N     1 
ATOM   9532  C  CA    . GLU A 1 2513 ? 129.884 125.635 165.327 1.00 58.83  ? 2513 GLU A CA    1 
ATOM   9533  C  C     . GLU A 1 2513 ? 130.203 124.702 164.166 1.00 65.57  ? 2513 GLU A C     1 
ATOM   9534  O  O     . GLU A 1 2513 ? 129.305 124.273 163.430 1.00 72.13  ? 2513 GLU A O     1 
ATOM   9535  C  CB    . GLU A 1 2513 ? 130.234 127.078 164.965 1.00 52.23  ? 2513 GLU A CB    1 
ATOM   9536  C  CG    . GLU A 1 2513 ? 129.743 128.108 165.963 1.00 65.73  ? 2513 GLU A CG    1 
ATOM   9537  C  CD    . GLU A 1 2513 ? 129.797 129.519 165.416 1.00 74.90  ? 2513 GLU A CD    1 
ATOM   9538  O  OE1   . GLU A 1 2513 ? 129.934 129.674 164.185 1.00 84.80  ? 2513 GLU A OE1   1 
ATOM   9539  O  OE2   . GLU A 1 2513 ? 129.706 130.474 166.216 1.00 69.79  ? 2513 GLU A OE2   1 
ATOM   9540  N  N     . LEU A 1 2514 ? 131.484 124.373 163.986 1.00 58.04  ? 2514 LEU A N     1 
ATOM   9541  C  CA    . LEU A 1 2514 ? 131.855 123.443 162.925 1.00 53.15  ? 2514 LEU A CA    1 
ATOM   9542  C  C     . LEU A 1 2514 ? 131.277 122.057 163.181 1.00 56.24  ? 2514 LEU A C     1 
ATOM   9543  O  O     . LEU A 1 2514 ? 130.839 121.382 162.245 1.00 66.83  ? 2514 LEU A O     1 
ATOM   9544  C  CB    . LEU A 1 2514 ? 133.373 123.370 162.777 1.00 52.72  ? 2514 LEU A CB    1 
ATOM   9545  C  CG    . LEU A 1 2514 ? 133.833 122.557 161.563 1.00 49.70  ? 2514 LEU A CG    1 
ATOM   9546  C  CD1   . LEU A 1 2514 ? 133.536 123.302 160.275 1.00 48.43  ? 2514 LEU A CD1   1 
ATOM   9547  C  CD2   . LEU A 1 2514 ? 135.304 122.214 161.651 1.00 49.93  ? 2514 LEU A CD2   1 
ATOM   9548  N  N     . GLY A 1 2515 ? 131.272 121.613 164.439 1.00 53.61  ? 2515 GLY A N     1 
ATOM   9549  C  CA    . GLY A 1 2515 ? 130.671 120.327 164.751 1.00 54.69  ? 2515 GLY A CA    1 
ATOM   9550  C  C     . GLY A 1 2515 ? 129.190 120.284 164.429 1.00 59.93  ? 2515 GLY A C     1 
ATOM   9551  O  O     . GLY A 1 2515 ? 128.690 119.294 163.889 1.00 65.46  ? 2515 GLY A O     1 
ATOM   9552  N  N     . GLU A 1 2516 ? 128.468 121.358 164.755 1.00 62.84  ? 2516 GLU A N     1 
ATOM   9553  C  CA    . GLU A 1 2516 ? 127.048 121.426 164.428 1.00 66.82  ? 2516 GLU A CA    1 
ATOM   9554  C  C     . GLU A 1 2516 ? 126.828 121.452 162.922 1.00 67.35  ? 2516 GLU A C     1 
ATOM   9555  O  O     . GLU A 1 2516 ? 125.896 120.815 162.415 1.00 73.42  ? 2516 GLU A O     1 
ATOM   9556  C  CB    . GLU A 1 2516 ? 126.412 122.650 165.086 1.00 67.00  ? 2516 GLU A CB    1 
ATOM   9557  C  CG    . GLU A 1 2516 ? 126.312 122.558 166.601 1.00 81.04  ? 2516 GLU A CG    1 
ATOM   9558  C  CD    . GLU A 1 2516 ? 125.632 121.284 167.067 1.00 90.52  ? 2516 GLU A CD    1 
ATOM   9559  O  OE1   . GLU A 1 2516 ? 124.385 121.227 167.037 1.00 84.03  ? 2516 GLU A OE1   1 
ATOM   9560  O  OE2   . GLU A 1 2516 ? 126.345 120.340 167.467 1.00 91.25  ? 2516 GLU A OE2   1 
ATOM   9561  N  N     . TYR A 1 2517 ? 127.672 122.180 162.188 1.00 61.34  ? 2517 TYR A N     1 
ATOM   9562  C  CA    . TYR A 1 2517 ? 127.557 122.182 160.732 1.00 60.16  ? 2517 TYR A CA    1 
ATOM   9563  C  C     . TYR A 1 2517 ? 127.773 120.786 160.162 1.00 60.28  ? 2517 TYR A C     1 
ATOM   9564  O  O     . TYR A 1 2517 ? 127.022 120.340 159.285 1.00 67.28  ? 2517 TYR A O     1 
ATOM   9565  C  CB    . TYR A 1 2517 ? 128.555 123.162 160.124 1.00 58.99  ? 2517 TYR A CB    1 
ATOM   9566  C  CG    . TYR A 1 2517 ? 128.371 123.364 158.640 1.00 62.39  ? 2517 TYR A CG    1 
ATOM   9567  C  CD1   . TYR A 1 2517 ? 127.186 123.874 158.134 1.00 67.31  ? 2517 TYR A CD1   1 
ATOM   9568  C  CD2   . TYR A 1 2517 ? 129.375 123.031 157.744 1.00 63.70  ? 2517 TYR A CD2   1 
ATOM   9569  C  CE1   . TYR A 1 2517 ? 127.008 124.059 156.779 1.00 69.52  ? 2517 TYR A CE1   1 
ATOM   9570  C  CE2   . TYR A 1 2517 ? 129.207 123.212 156.385 1.00 65.86  ? 2517 TYR A CE2   1 
ATOM   9571  C  CZ    . TYR A 1 2517 ? 128.021 123.725 155.909 1.00 71.39  ? 2517 TYR A CZ    1 
ATOM   9572  O  OH    . TYR A 1 2517 ? 127.847 123.907 154.557 1.00 76.69  ? 2517 TYR A OH    1 
ATOM   9573  N  N     . ILE A 1 2518 ? 128.793 120.079 160.653 1.00 59.40  ? 2518 ILE A N     1 
ATOM   9574  C  CA    . ILE A 1 2518 ? 129.032 118.710 160.208 1.00 59.15  ? 2518 ILE A CA    1 
ATOM   9575  C  C     . ILE A 1 2518 ? 127.819 117.843 160.510 1.00 67.62  ? 2518 ILE A C     1 
ATOM   9576  O  O     . ILE A 1 2518 ? 127.335 117.103 159.648 1.00 76.39  ? 2518 ILE A O     1 
ATOM   9577  C  CB    . ILE A 1 2518 ? 130.305 118.140 160.859 1.00 56.36  ? 2518 ILE A CB    1 
ATOM   9578  C  CG1   . ILE A 1 2518 ? 131.532 118.943 160.435 1.00 51.70  ? 2518 ILE A CG1   1 
ATOM   9579  C  CG2   . ILE A 1 2518 ? 130.475 116.676 160.501 1.00 57.37  ? 2518 ILE A CG2   1 
ATOM   9580  C  CD1   . ILE A 1 2518 ? 131.579 119.239 158.964 1.00 57.91  ? 2518 ILE A CD1   1 
ATOM   9581  N  N     . ARG A 1 2519 ? 127.292 117.948 161.733 1.00 66.47  ? 2519 ARG A N     1 
ATOM   9582  C  CA    . ARG A 1 2519 ? 126.112 117.175 162.109 1.00 67.16  ? 2519 ARG A CA    1 
ATOM   9583  C  C     . ARG A 1 2519 ? 124.946 117.457 161.172 1.00 68.21  ? 2519 ARG A C     1 
ATOM   9584  O  O     . ARG A 1 2519 ? 124.174 116.551 160.838 1.00 72.06  ? 2519 ARG A O     1 
ATOM   9585  C  CB    . ARG A 1 2519 ? 125.724 117.485 163.554 1.00 65.90  ? 2519 ARG A CB    1 
ATOM   9586  C  CG    . ARG A 1 2519 ? 124.589 116.633 164.092 1.00 71.39  ? 2519 ARG A CG    1 
ATOM   9587  C  CD    . ARG A 1 2519 ? 124.255 116.995 165.530 1.00 76.41  ? 2519 ARG A CD    1 
ATOM   9588  N  NE    . ARG A 1 2519 ? 125.348 116.696 166.447 1.00 82.28  ? 2519 ARG A NE    1 
ATOM   9589  C  CZ    . ARG A 1 2519 ? 125.558 115.508 166.998 1.00 85.79  ? 2519 ARG A CZ    1 
ATOM   9590  N  NH1   . ARG A 1 2519 ? 124.771 114.477 166.737 1.00 86.44  ? 2519 ARG A NH1   1 
ATOM   9591  N  NH2   . ARG A 1 2519 ? 126.580 115.352 167.834 1.00 82.83  ? 2519 ARG A NH2   1 
ATOM   9592  N  N     . ARG A 1 2520 ? 124.806 118.708 160.734 1.00 64.72  ? 2520 ARG A N     1 
ATOM   9593  C  CA    . ARG A 1 2520 ? 123.716 119.046 159.826 1.00 69.93  ? 2520 ARG A CA    1 
ATOM   9594  C  C     . ARG A 1 2520 ? 123.949 118.501 158.422 1.00 74.10  ? 2520 ARG A C     1 
ATOM   9595  O  O     . ARG A 1 2520 ? 122.986 118.146 157.734 1.00 76.83  ? 2520 ARG A O     1 
ATOM   9596  C  CB    . ARG A 1 2520 ? 123.518 120.560 159.772 1.00 68.04  ? 2520 ARG A CB    1 
ATOM   9597  C  CG    . ARG A 1 2520 ? 122.996 121.167 161.063 1.00 69.68  ? 2520 ARG A CG    1 
ATOM   9598  C  CD    . ARG A 1 2520 ? 122.424 122.571 160.868 1.00 72.74  ? 2520 ARG A CD    1 
ATOM   9599  N  NE    . ARG A 1 2520 ? 123.323 123.480 160.164 1.00 78.75  ? 2520 ARG A NE    1 
ATOM   9600  C  CZ    . ARG A 1 2520 ? 123.263 123.741 158.865 1.00 79.25  ? 2520 ARG A CZ    1 
ATOM   9601  N  NH1   . ARG A 1 2520 ? 122.368 123.160 158.083 1.00 77.23  ? 2520 ARG A NH1   1 
ATOM   9602  N  NH2   . ARG A 1 2520 ? 124.119 124.611 158.337 1.00 72.19  ? 2520 ARG A NH2   1 
ATOM   9603  N  N     . ILE A 1 2521 ? 125.202 118.426 157.973 1.00 72.92  ? 2521 ILE A N     1 
ATOM   9604  C  CA    . ILE A 1 2521 ? 125.488 118.136 156.572 1.00 69.91  ? 2521 ILE A CA    1 
ATOM   9605  C  C     . ILE A 1 2521 ? 126.043 116.731 156.360 1.00 72.77  ? 2521 ILE A C     1 
ATOM   9606  O  O     . ILE A 1 2521 ? 126.514 116.422 155.260 1.00 80.67  ? 2521 ILE A O     1 
ATOM   9607  C  CB    . ILE A 1 2521 ? 126.432 119.186 155.964 1.00 69.46  ? 2521 ILE A CB    1 
ATOM   9608  C  CG1   . ILE A 1 2521 ? 127.861 118.986 156.474 1.00 65.50  ? 2521 ILE A CG1   1 
ATOM   9609  C  CG2   . ILE A 1 2521 ? 125.935 120.590 156.265 1.00 69.08  ? 2521 ILE A CG2   1 
ATOM   9610  C  CD1   . ILE A 1 2521 ? 128.903 119.730 155.675 1.00 61.84  ? 2521 ILE A CD1   1 
ATOM   9611  N  N     . THR A 1 2522 ? 125.995 115.860 157.364 1.00 73.16  ? 2522 THR A N     1 
ATOM   9612  C  CA    . THR A 1 2522 ? 126.509 114.509 157.183 1.00 81.99  ? 2522 THR A CA    1 
ATOM   9613  C  C     . THR A 1 2522 ? 125.462 113.479 157.586 1.00 89.61  ? 2522 THR A C     1 
ATOM   9614  O  O     . THR A 1 2522 ? 124.462 113.786 158.240 1.00 86.95  ? 2522 THR A O     1 
ATOM   9615  C  CB    . THR A 1 2522 ? 127.793 114.270 157.989 1.00 77.17  ? 2522 THR A CB    1 
ATOM   9616  O  OG1   . THR A 1 2522 ? 128.400 113.050 157.550 1.00 82.33  ? 2522 THR A OG1   1 
ATOM   9617  C  CG2   . THR A 1 2522 ? 127.466 114.112 159.461 1.00 79.88  ? 2522 THR A CG2   1 
ATOM   9618  N  N     . THR A 1 2523 ? 125.713 112.235 157.174 1.00 94.20  ? 2523 THR A N     1 
ATOM   9619  C  CA    . THR A 1 2523 ? 124.878 111.100 157.532 1.00 95.24  ? 2523 THR A CA    1 
ATOM   9620  C  C     . THR A 1 2523 ? 125.588 110.080 158.409 1.00 95.22  ? 2523 THR A C     1 
ATOM   9621  O  O     . THR A 1 2523 ? 124.941 109.131 158.867 1.00 99.70  ? 2523 THR A O     1 
ATOM   9622  C  CB    . THR A 1 2523 ? 124.360 110.391 156.271 1.00 97.89  ? 2523 THR A CB    1 
ATOM   9623  O  OG1   . THR A 1 2523 ? 123.613 109.228 156.647 1.00 99.89  ? 2523 THR A OG1   1 
ATOM   9624  C  CG2   . THR A 1 2523 ? 125.522 109.976 155.383 1.00 93.67  ? 2523 THR A CG2   1 
ATOM   9625  N  N     . VAL A 1 2524 ? 126.888 110.237 158.644 1.00 91.22  ? 2524 VAL A N     1 
ATOM   9626  C  CA    . VAL A 1 2524 ? 127.619 109.320 159.524 1.00 92.58  ? 2524 VAL A CA    1 
ATOM   9627  C  C     . VAL A 1 2524 ? 127.083 109.462 160.943 1.00 92.42  ? 2524 VAL A C     1 
ATOM   9628  O  O     . VAL A 1 2524 ? 126.708 110.579 161.353 1.00 94.27  ? 2524 VAL A O     1 
ATOM   9629  C  CB    . VAL A 1 2524 ? 129.129 109.617 159.465 1.00 88.29  ? 2524 VAL A CB    1 
ATOM   9630  C  CG1   . VAL A 1 2524 ? 129.399 111.048 159.874 1.00 79.92  ? 2524 VAL A CG1   1 
ATOM   9631  C  CG2   . VAL A 1 2524 ? 129.924 108.652 160.331 1.00 85.00  ? 2524 VAL A CG2   1 
ATOM   9632  N  N     . PRO A 1 2525 ? 126.987 108.384 161.729 1.00 89.88  ? 2525 PRO A N     1 
ATOM   9633  C  CA    . PRO A 1 2525 ? 126.470 108.526 163.096 1.00 91.94  ? 2525 PRO A CA    1 
ATOM   9634  C  C     . PRO A 1 2525 ? 127.400 109.315 164.003 1.00 90.91  ? 2525 PRO A C     1 
ATOM   9635  O  O     . PRO A 1 2525 ? 128.465 108.831 164.399 1.00 87.35  ? 2525 PRO A O     1 
ATOM   9636  C  CB    . PRO A 1 2525 ? 126.329 107.074 163.570 1.00 90.73  ? 2525 PRO A CB    1 
ATOM   9637  C  CG    . PRO A 1 2525 ? 126.210 106.277 162.321 1.00 89.73  ? 2525 PRO A CG    1 
ATOM   9638  C  CD    . PRO A 1 2525 ? 127.078 106.971 161.321 1.00 88.85  ? 2525 PRO A CD    1 
ATOM   9639  N  N     . LEU A 1 2526 ? 126.999 110.537 164.332 1.00 88.37  ? 2526 LEU A N     1 
ATOM   9640  C  CA    . LEU A 1 2526 ? 127.712 111.361 165.291 1.00 85.24  ? 2526 LEU A CA    1 
ATOM   9641  C  C     . LEU A 1 2526 ? 127.250 111.028 166.707 1.00 92.52  ? 2526 LEU A C     1 
ATOM   9642  O  O     . LEU A 1 2526 ? 126.190 110.425 166.893 1.00 94.67  ? 2526 LEU A O     1 
ATOM   9643  C  CB    . LEU A 1 2526 ? 127.483 112.838 164.981 1.00 81.62  ? 2526 LEU A CB    1 
ATOM   9644  C  CG    . LEU A 1 2526 ? 128.083 113.371 163.679 1.00 76.60  ? 2526 LEU A CG    1 
ATOM   9645  C  CD1   . LEU A 1 2526 ? 128.343 114.860 163.792 1.00 69.44  ? 2526 LEU A CD1   1 
ATOM   9646  C  CD2   . LEU A 1 2526 ? 129.362 112.634 163.322 1.00 77.46  ? 2526 LEU A CD2   1 
ATOM   9647  N  N     . PRO A 1 2527 ? 128.036 111.388 167.725 1.00 90.34  ? 2527 PRO A N     1 
ATOM   9648  C  CA    . PRO A 1 2527 ? 127.611 111.112 169.103 1.00 89.26  ? 2527 PRO A CA    1 
ATOM   9649  C  C     . PRO A 1 2527 ? 126.283 111.783 169.419 1.00 97.73  ? 2527 PRO A C     1 
ATOM   9650  O  O     . PRO A 1 2527 ? 126.024 112.917 169.013 1.00 94.93  ? 2527 PRO A O     1 
ATOM   9651  C  CB    . PRO A 1 2527 ? 128.752 111.689 169.950 1.00 81.35  ? 2527 PRO A CB    1 
ATOM   9652  C  CG    . PRO A 1 2527 ? 129.455 112.647 169.050 1.00 76.84  ? 2527 PRO A CG    1 
ATOM   9653  C  CD    . PRO A 1 2527 ? 129.356 112.038 167.690 1.00 82.72  ? 2527 PRO A CD    1 
ATOM   9654  N  N     . THR A 1 2528 ? 125.439 111.063 170.158 1.00 105.39 ? 2528 THR A N     1 
ATOM   9655  C  CA    . THR A 1 2528 ? 124.101 111.521 170.502 1.00 110.48 ? 2528 THR A CA    1 
ATOM   9656  C  C     . THR A 1 2528 ? 124.070 112.328 171.794 1.00 114.51 ? 2528 THR A C     1 
ATOM   9657  O  O     . THR A 1 2528 ? 123.013 112.421 172.430 1.00 116.24 ? 2528 THR A O     1 
ATOM   9658  C  CB    . THR A 1 2528 ? 123.147 110.329 170.603 1.00 108.43 ? 2528 THR A CB    1 
ATOM   9659  O  OG1   . THR A 1 2528 ? 121.834 110.792 170.942 1.00 105.87 ? 2528 THR A OG1   1 
ATOM   9660  C  CG2   . THR A 1 2528 ? 123.627 109.347 171.662 1.00 108.01 ? 2528 THR A CG2   1 
ATOM   9661  N  N     . ALA A 1 2529 ? 125.195 112.906 172.192 1.00 112.67 ? 2529 ALA A N     1 
ATOM   9662  C  CA    . ALA A 1 2529 ? 125.240 113.687 173.421 1.00 114.35 ? 2529 ALA A CA    1 
ATOM   9663  C  C     . ALA A 1 2529 ? 124.357 114.923 173.287 1.00 118.63 ? 2529 ALA A C     1 
ATOM   9664  O  O     . ALA A 1 2529 ? 124.460 115.648 172.291 1.00 117.59 ? 2529 ALA A O     1 
ATOM   9665  C  CB    . ALA A 1 2529 ? 126.675 114.095 173.738 1.00 107.40 ? 2529 ALA A CB    1 
ATOM   9666  N  N     . PRO A 1 2530 ? 123.476 115.189 174.251 1.00 121.28 ? 2530 PRO A N     1 
ATOM   9667  C  CA    . PRO A 1 2530 ? 122.604 116.367 174.153 1.00 123.51 ? 2530 PRO A CA    1 
ATOM   9668  C  C     . PRO A 1 2530 ? 123.364 117.684 174.208 1.00 122.78 ? 2530 PRO A C     1 
ATOM   9669  O  O     . PRO A 1 2530 ? 123.153 118.558 173.362 1.00 121.06 ? 2530 PRO A O     1 
ATOM   9670  C  CB    . PRO A 1 2530 ? 121.673 116.212 175.364 1.00 122.38 ? 2530 PRO A CB    1 
ATOM   9671  C  CG    . PRO A 1 2530 ? 121.690 114.751 175.669 1.00 122.12 ? 2530 PRO A CG    1 
ATOM   9672  C  CD    . PRO A 1 2530 ? 123.089 114.306 175.364 1.00 120.84 ? 2530 PRO A CD    1 
ATOM   9673  N  N     . ASN A 1 2531 ? 124.245 117.840 175.193 1.00 118.79 ? 2531 ASN A N     1 
ATOM   9674  C  CA    . ASN A 1 2531 ? 124.943 119.101 175.436 1.00 116.18 ? 2531 ASN A CA    1 
ATOM   9675  C  C     . ASN A 1 2531 ? 126.435 118.866 175.635 1.00 109.82 ? 2531 ASN A C     1 
ATOM   9676  O  O     . ASN A 1 2531 ? 127.055 119.390 176.564 1.00 108.93 ? 2531 ASN A O     1 
ATOM   9677  C  CB    . ASN A 1 2531 ? 124.352 119.827 176.641 1.00 119.70 ? 2531 ASN A CB    1 
ATOM   9678  C  CG    . ASN A 1 2531 ? 122.952 120.346 176.382 1.00 126.62 ? 2531 ASN A CG    1 
ATOM   9679  O  OD1   . ASN A 1 2531 ? 122.022 119.573 176.152 1.00 130.44 ? 2531 ASN A OD1   1 
ATOM   9680  N  ND2   . ASN A 1 2531 ? 122.795 121.664 176.421 1.00 125.21 ? 2531 ASN A ND2   1 
ATOM   9681  N  N     . ILE A 1 2532 ? 127.037 118.070 174.758 1.00 105.92 ? 2532 ILE A N     1 
ATOM   9682  C  CA    . ILE A 1 2532 ? 128.481 117.854 174.786 1.00 100.00 ? 2532 ILE A CA    1 
ATOM   9683  C  C     . ILE A 1 2532 ? 129.019 117.996 173.367 1.00 97.65  ? 2532 ILE A C     1 
ATOM   9684  O  O     . ILE A 1 2532 ? 128.479 117.379 172.437 1.00 94.60  ? 2532 ILE A O     1 
ATOM   9685  C  CB    . ILE A 1 2532 ? 128.835 116.485 175.387 1.00 99.26  ? 2532 ILE A CB    1 
ATOM   9686  C  CG1   . ILE A 1 2532 ? 128.629 116.497 176.902 1.00 98.28  ? 2532 ILE A CG1   1 
ATOM   9687  C  CG2   . ILE A 1 2532 ? 130.272 116.116 175.066 1.00 93.77  ? 2532 ILE A CG2   1 
ATOM   9688  C  CD1   . ILE A 1 2532 ? 128.754 115.135 177.545 1.00 92.82  ? 2532 ILE A CD1   1 
ATOM   9689  N  N     . PRO A 1 2533 ? 130.063 118.797 173.152 1.00 92.86  ? 2533 PRO A N     1 
ATOM   9690  C  CA    . PRO A 1 2533 ? 130.576 118.993 171.792 1.00 83.10  ? 2533 PRO A CA    1 
ATOM   9691  C  C     . PRO A 1 2533 ? 131.114 117.700 171.199 1.00 77.86  ? 2533 PRO A C     1 
ATOM   9692  O  O     . PRO A 1 2533 ? 131.570 116.804 171.912 1.00 80.57  ? 2533 PRO A O     1 
ATOM   9693  C  CB    . PRO A 1 2533 ? 131.695 120.026 171.979 1.00 77.98  ? 2533 PRO A CB    1 
ATOM   9694  C  CG    . PRO A 1 2533 ? 131.384 120.696 173.277 1.00 83.18  ? 2533 PRO A CG    1 
ATOM   9695  C  CD    . PRO A 1 2533 ? 130.766 119.637 174.134 1.00 87.06  ? 2533 PRO A CD    1 
ATOM   9696  N  N     . ILE A 1 2534 ? 131.045 117.611 169.868 1.00 70.33  ? 2534 ILE A N     1 
ATOM   9697  C  CA    . ILE A 1 2534 ? 131.549 116.430 169.174 1.00 63.78  ? 2534 ILE A CA    1 
ATOM   9698  C  C     . ILE A 1 2534 ? 133.054 116.312 169.359 1.00 66.46  ? 2534 ILE A C     1 
ATOM   9699  O  O     . ILE A 1 2534 ? 133.592 115.203 169.462 1.00 66.59  ? 2534 ILE A O     1 
ATOM   9700  C  CB    . ILE A 1 2534 ? 131.168 116.465 167.678 1.00 65.76  ? 2534 ILE A CB    1 
ATOM   9701  C  CG1   . ILE A 1 2534 ? 129.649 116.530 167.490 1.00 78.52  ? 2534 ILE A CG1   1 
ATOM   9702  C  CG2   . ILE A 1 2534 ? 131.701 115.234 166.965 1.00 62.94  ? 2534 ILE A CG2   1 
ATOM   9703  C  CD1   . ILE A 1 2534 ? 129.064 117.933 167.481 1.00 79.31  ? 2534 ILE A CD1   1 
ATOM   9704  N  N     . ILE A 1 2535 ? 133.757 117.445 169.417 1.00 69.97  ? 2535 ILE A N     1 
ATOM   9705  C  CA    . ILE A 1 2535 ? 135.204 117.438 169.596 1.00 65.83  ? 2535 ILE A CA    1 
ATOM   9706  C  C     . ILE A 1 2535 ? 135.627 116.910 170.959 1.00 68.54  ? 2535 ILE A C     1 
ATOM   9707  O  O     . ILE A 1 2535 ? 136.813 116.631 171.165 1.00 67.54  ? 2535 ILE A O     1 
ATOM   9708  C  CB    . ILE A 1 2535 ? 135.767 118.856 169.372 1.00 54.50  ? 2535 ILE A CB    1 
ATOM   9709  C  CG1   . ILE A 1 2535 ? 137.221 118.790 168.906 1.00 52.07  ? 2535 ILE A CG1   1 
ATOM   9710  C  CG2   . ILE A 1 2535 ? 135.642 119.689 170.637 1.00 54.35  ? 2535 ILE A CG2   1 
ATOM   9711  C  CD1   . ILE A 1 2535 ? 137.704 120.057 168.247 1.00 52.35  ? 2535 ILE A CD1   1 
ATOM   9712  N  N     . ASP A 1 2536 ? 134.687 116.752 171.890 1.00 64.96  ? 2536 ASP A N     1 
ATOM   9713  C  CA    . ASP A 1 2536 ? 134.977 116.176 173.196 1.00 61.70  ? 2536 ASP A CA    1 
ATOM   9714  C  C     . ASP A 1 2536 ? 135.021 114.654 173.173 1.00 65.93  ? 2536 ASP A C     1 
ATOM   9715  O  O     . ASP A 1 2536 ? 135.310 114.043 174.207 1.00 64.54  ? 2536 ASP A O     1 
ATOM   9716  C  CB    . ASP A 1 2536 ? 133.936 116.640 174.217 1.00 71.26  ? 2536 ASP A CB    1 
ATOM   9717  C  CG    . ASP A 1 2536 ? 134.381 117.867 174.987 1.00 79.84  ? 2536 ASP A CG    1 
ATOM   9718  O  OD1   . ASP A 1 2536 ? 135.559 118.259 174.858 1.00 79.20  ? 2536 ASP A OD1   1 
ATOM   9719  O  OD2   . ASP A 1 2536 ? 133.551 118.442 175.722 1.00 84.61  ? 2536 ASP A OD2   1 
ATOM   9720  N  N     . TYR A 1 2537 ? 134.742 114.033 172.031 1.00 67.75  ? 2537 TYR A N     1 
ATOM   9721  C  CA    . TYR A 1 2537 ? 134.707 112.586 171.899 1.00 63.29  ? 2537 TYR A CA    1 
ATOM   9722  C  C     . TYR A 1 2537 ? 135.894 112.101 171.078 1.00 63.53  ? 2537 TYR A C     1 
ATOM   9723  O  O     . TYR A 1 2537 ? 136.331 112.777 170.142 1.00 61.94  ? 2537 TYR A O     1 
ATOM   9724  C  CB    . TYR A 1 2537 ? 133.409 112.128 171.231 1.00 64.81  ? 2537 TYR A CB    1 
ATOM   9725  C  CG    . TYR A 1 2537 ? 132.214 112.073 172.150 1.00 67.57  ? 2537 TYR A CG    1 
ATOM   9726  C  CD1   . TYR A 1 2537 ? 131.417 113.191 172.351 1.00 67.25  ? 2537 TYR A CD1   1 
ATOM   9727  C  CD2   . TYR A 1 2537 ? 131.876 110.901 172.810 1.00 70.26  ? 2537 TYR A CD2   1 
ATOM   9728  C  CE1   . TYR A 1 2537 ? 130.323 113.144 173.186 1.00 71.18  ? 2537 TYR A CE1   1 
ATOM   9729  C  CE2   . TYR A 1 2537 ? 130.783 110.845 173.648 1.00 75.56  ? 2537 TYR A CE2   1 
ATOM   9730  C  CZ    . TYR A 1 2537 ? 130.010 111.970 173.832 1.00 78.53  ? 2537 TYR A CZ    1 
ATOM   9731  O  OH    . TYR A 1 2537 ? 128.919 111.918 174.668 1.00 88.16  ? 2537 TYR A OH    1 
ATOM   9732  N  N     . GLU A 1 2538 ? 136.409 110.931 171.436 1.00 64.97  ? 2538 GLU A N     1 
ATOM   9733  C  CA    . GLU A 1 2538 ? 137.418 110.222 170.669 1.00 60.39  ? 2538 GLU A CA    1 
ATOM   9734  C  C     . GLU A 1 2538 ? 136.748 109.109 169.882 1.00 68.02  ? 2538 GLU A C     1 
ATOM   9735  O  O     . GLU A 1 2538 ? 135.735 108.552 170.317 1.00 74.87  ? 2538 GLU A O     1 
ATOM   9736  C  CB    . GLU A 1 2538 ? 138.482 109.610 171.581 1.00 59.66  ? 2538 GLU A CB    1 
ATOM   9737  C  CG    . GLU A 1 2538 ? 139.613 108.921 170.833 1.00 66.32  ? 2538 GLU A CG    1 
ATOM   9738  C  CD    . GLU A 1 2538 ? 140.628 108.303 171.760 1.00 68.01  ? 2538 GLU A CD    1 
ATOM   9739  O  OE1   . GLU A 1 2538 ? 140.419 108.375 172.985 1.00 72.77  ? 2538 GLU A OE1   1 
ATOM   9740  O  OE2   . GLU A 1 2538 ? 141.631 107.744 171.268 1.00 63.36  ? 2538 GLU A OE2   1 
ATOM   9741  N  N     . VAL A 1 2539 ? 137.310 108.788 168.722 1.00 65.03  ? 2539 VAL A N     1 
ATOM   9742  C  CA    . VAL A 1 2539 ? 136.917 107.586 167.999 1.00 63.43  ? 2539 VAL A CA    1 
ATOM   9743  C  C     . VAL A 1 2539 ? 137.826 106.451 168.455 1.00 66.40  ? 2539 VAL A C     1 
ATOM   9744  O  O     . VAL A 1 2539 ? 139.023 106.447 168.161 1.00 68.38  ? 2539 VAL A O     1 
ATOM   9745  C  CB    . VAL A 1 2539 ? 136.997 107.783 166.484 1.00 58.65  ? 2539 VAL A CB    1 
ATOM   9746  C  CG1   . VAL A 1 2539 ? 136.404 106.585 165.788 1.00 61.13  ? 2539 VAL A CG1   1 
ATOM   9747  C  CG2   . VAL A 1 2539 ? 136.274 109.053 166.081 1.00 58.01  ? 2539 VAL A CG2   1 
ATOM   9748  N  N     . SER A 1 2540 ? 137.258 105.483 169.169 1.00 67.62  ? 2540 SER A N     1 
ATOM   9749  C  CA    . SER A 1 2540 ? 138.024 104.327 169.604 1.00 69.74  ? 2540 SER A CA    1 
ATOM   9750  C  C     . SER A 1 2540 ? 138.339 103.437 168.404 1.00 64.75  ? 2540 SER A C     1 
ATOM   9751  O  O     . SER A 1 2540 ? 138.010 103.752 167.258 1.00 67.90  ? 2540 SER A O     1 
ATOM   9752  C  CB    . SER A 1 2540 ? 137.259 103.557 170.677 1.00 70.12  ? 2540 SER A CB    1 
ATOM   9753  O  OG    . SER A 1 2540 ? 135.994 103.142 170.198 1.00 76.18  ? 2540 SER A OG    1 
ATOM   9754  N  N     . ILE A 1 2541 ? 138.994 102.306 168.669 1.00 59.95  ? 2541 ILE A N     1 
ATOM   9755  C  CA    . ILE A 1 2541 ? 139.291 101.365 167.593 1.00 63.11  ? 2541 ILE A CA    1 
ATOM   9756  C  C     . ILE A 1 2541 ? 138.004 100.876 166.947 1.00 70.67  ? 2541 ILE A C     1 
ATOM   9757  O  O     . ILE A 1 2541 ? 137.890 100.820 165.717 1.00 79.69  ? 2541 ILE A O     1 
ATOM   9758  C  CB    . ILE A 1 2541 ? 140.137 100.194 168.120 1.00 72.17  ? 2541 ILE A CB    1 
ATOM   9759  C  CG1   . ILE A 1 2541 ? 141.599 100.619 168.277 1.00 82.04  ? 2541 ILE A CG1   1 
ATOM   9760  C  CG2   . ILE A 1 2541 ? 140.005 99.006  167.197 1.00 74.75  ? 2541 ILE A CG2   1 
ATOM   9761  C  CD1   . ILE A 1 2541 ? 142.353 100.709 166.966 1.00 74.18  ? 2541 ILE A CD1   1 
ATOM   9762  N  N     . SER A 1 2542 ? 137.014 100.523 167.760 1.00 74.29  ? 2542 SER A N     1 
ATOM   9763  C  CA    . SER A 1 2542 ? 135.697 100.220 167.231 1.00 74.21  ? 2542 SER A CA    1 
ATOM   9764  C  C     . SER A 1 2542 ? 135.039 101.495 166.710 1.00 71.95  ? 2542 SER A C     1 
ATOM   9765  O  O     . SER A 1 2542 ? 135.454 102.614 167.021 1.00 73.20  ? 2542 SER A O     1 
ATOM   9766  C  CB    . SER A 1 2542 ? 134.824 99.571  168.304 1.00 73.80  ? 2542 SER A CB    1 
ATOM   9767  O  OG    . SER A 1 2542 ? 135.454 98.421  168.839 1.00 73.83  ? 2542 SER A OG    1 
ATOM   9768  N  N     . GLY A 1 2543 ? 133.996 101.314 165.901 1.00 73.86  ? 2543 GLY A N     1 
ATOM   9769  C  CA    . GLY A 1 2543 ? 133.319 102.456 165.313 1.00 81.15  ? 2543 GLY A CA    1 
ATOM   9770  C  C     . GLY A 1 2543 ? 132.662 103.373 166.322 1.00 84.23  ? 2543 GLY A C     1 
ATOM   9771  O  O     . GLY A 1 2543 ? 132.409 104.541 166.011 1.00 84.01  ? 2543 GLY A O     1 
ATOM   9772  N  N     . GLU A 1 2544 ? 132.382 102.876 167.523 1.00 83.47  ? 2544 GLU A N     1 
ATOM   9773  C  CA    . GLU A 1 2544 ? 131.703 103.677 168.530 1.00 81.14  ? 2544 GLU A CA    1 
ATOM   9774  C  C     . GLU A 1 2544 ? 132.603 104.796 169.044 1.00 82.09  ? 2544 GLU A C     1 
ATOM   9775  O  O     . GLU A 1 2544 ? 133.826 104.658 169.123 1.00 77.48  ? 2544 GLU A O     1 
ATOM   9776  C  CB    . GLU A 1 2544 ? 131.257 102.794 169.695 1.00 78.69  ? 2544 GLU A CB    1 
ATOM   9777  C  CG    . GLU A 1 2544 ? 132.389 102.016 170.344 1.00 83.25  ? 2544 GLU A CG    1 
ATOM   9778  C  CD    . GLU A 1 2544 ? 132.010 101.450 171.697 1.00 92.77  ? 2544 GLU A CD    1 
ATOM   9779  O  OE1   . GLU A 1 2544 ? 132.041 102.209 172.689 1.00 93.22  ? 2544 GLU A OE1   1 
ATOM   9780  O  OE2   . GLU A 1 2544 ? 131.685 100.247 171.771 1.00 94.83  ? 2544 GLU A OE2   1 
ATOM   9781  N  N     . TRP A 1 2545 ? 131.979 105.921 169.385 1.00 81.41  ? 2545 TRP A N     1 
ATOM   9782  C  CA    . TRP A 1 2545 ? 132.689 107.000 170.050 1.00 75.60  ? 2545 TRP A CA    1 
ATOM   9783  C  C     . TRP A 1 2545 ? 132.895 106.669 171.526 1.00 79.09  ? 2545 TRP A C     1 
ATOM   9784  O  O     . TRP A 1 2545 ? 132.275 105.758 172.081 1.00 82.27  ? 2545 TRP A O     1 
ATOM   9785  C  CB    . TRP A 1 2545 ? 131.921 108.317 169.930 1.00 71.68  ? 2545 TRP A CB    1 
ATOM   9786  C  CG    . TRP A 1 2545 ? 131.629 108.747 168.529 1.00 72.42  ? 2545 TRP A CG    1 
ATOM   9787  C  CD1   . TRP A 1 2545 ? 130.638 108.280 167.719 1.00 76.39  ? 2545 TRP A CD1   1 
ATOM   9788  C  CD2   . TRP A 1 2545 ? 132.322 109.750 167.779 1.00 70.80  ? 2545 TRP A CD2   1 
ATOM   9789  N  NE1   . TRP A 1 2545 ? 130.675 108.924 166.507 1.00 78.49  ? 2545 TRP A NE1   1 
ATOM   9790  C  CE2   . TRP A 1 2545 ? 131.701 109.831 166.518 1.00 74.13  ? 2545 TRP A CE2   1 
ATOM   9791  C  CE3   . TRP A 1 2545 ? 133.410 110.585 168.048 1.00 66.85  ? 2545 TRP A CE3   1 
ATOM   9792  C  CZ2   . TRP A 1 2545 ? 132.132 110.713 165.530 1.00 68.07  ? 2545 TRP A CZ2   1 
ATOM   9793  C  CZ3   . TRP A 1 2545 ? 133.835 111.458 167.067 1.00 63.11  ? 2545 TRP A CZ3   1 
ATOM   9794  C  CH2   . TRP A 1 2545 ? 133.198 111.515 165.824 1.00 62.58  ? 2545 TRP A CH2   1 
ATOM   9795  N  N     . SER A 1 2546 ? 133.783 107.431 172.164 1.00 77.65  ? 2546 SER A N     1 
ATOM   9796  C  CA    . SER A 1 2546 ? 134.007 107.292 173.589 1.00 75.46  ? 2546 SER A CA    1 
ATOM   9797  C  C     . SER A 1 2546 ? 134.443 108.652 174.113 1.00 72.12  ? 2546 SER A C     1 
ATOM   9798  O  O     . SER A 1 2546 ? 135.315 109.282 173.501 1.00 77.64  ? 2546 SER A O     1 
ATOM   9799  C  CB    . SER A 1 2546 ? 135.065 106.239 173.912 1.00 77.57  ? 2546 SER A CB    1 
ATOM   9800  O  OG    . SER A 1 2546 ? 136.336 106.626 173.420 1.00 80.19  ? 2546 SER A OG    1 
ATOM   9801  N  N     . PRO A 1 2547 ? 133.867 109.133 175.211 1.00 67.09  ? 2547 PRO A N     1 
ATOM   9802  C  CA    . PRO A 1 2547 ? 134.269 110.444 175.731 1.00 66.68  ? 2547 PRO A CA    1 
ATOM   9803  C  C     . PRO A 1 2547 ? 135.740 110.464 176.116 1.00 68.88  ? 2547 PRO A C     1 
ATOM   9804  O  O     . PRO A 1 2547 ? 136.298 109.468 176.582 1.00 69.91  ? 2547 PRO A O     1 
ATOM   9805  C  CB    . PRO A 1 2547 ? 133.365 110.635 176.955 1.00 67.78  ? 2547 PRO A CB    1 
ATOM   9806  C  CG    . PRO A 1 2547 ? 132.902 109.259 177.312 1.00 70.95  ? 2547 PRO A CG    1 
ATOM   9807  C  CD    . PRO A 1 2547 ? 132.805 108.516 176.022 1.00 68.94  ? 2547 PRO A CD    1 
ATOM   9808  N  N     . TRP A 1 2548 ? 136.375 111.619 175.895 1.00 65.60  ? 2548 TRP A N     1 
ATOM   9809  C  CA    . TRP A 1 2548 ? 137.767 111.788 176.297 1.00 62.68  ? 2548 TRP A CA    1 
ATOM   9810  C  C     . TRP A 1 2548 ? 137.931 111.678 177.805 1.00 67.73  ? 2548 TRP A C     1 
ATOM   9811  O  O     . TRP A 1 2548 ? 138.988 111.254 178.286 1.00 65.80  ? 2548 TRP A O     1 
ATOM   9812  C  CB    . TRP A 1 2548 ? 138.296 113.137 175.812 1.00 58.49  ? 2548 TRP A CB    1 
ATOM   9813  C  CG    . TRP A 1 2548 ? 138.887 113.122 174.437 1.00 56.15  ? 2548 TRP A CG    1 
ATOM   9814  C  CD1   . TRP A 1 2548 ? 138.468 113.844 173.361 1.00 58.99  ? 2548 TRP A CD1   1 
ATOM   9815  C  CD2   . TRP A 1 2548 ? 140.025 112.372 173.997 1.00 51.62  ? 2548 TRP A CD2   1 
ATOM   9816  N  NE1   . TRP A 1 2548 ? 139.262 113.580 172.274 1.00 55.89  ? 2548 TRP A NE1   1 
ATOM   9817  C  CE2   . TRP A 1 2548 ? 140.227 112.680 172.639 1.00 50.67  ? 2548 TRP A CE2   1 
ATOM   9818  C  CE3   . TRP A 1 2548 ? 140.888 111.466 174.618 1.00 52.53  ? 2548 TRP A CE3   1 
ATOM   9819  C  CZ2   . TRP A 1 2548 ? 141.254 112.116 171.892 1.00 47.85  ? 2548 TRP A CZ2   1 
ATOM   9820  C  CZ3   . TRP A 1 2548 ? 141.908 110.909 173.874 1.00 52.30  ? 2548 TRP A CZ3   1 
ATOM   9821  C  CH2   . TRP A 1 2548 ? 142.081 111.234 172.525 1.00 50.73  ? 2548 TRP A CH2   1 
ATOM   9822  N  N     . GLN A 1 2549 ? 136.896 112.049 178.565 1.00 69.93  ? 2549 GLN A N     1 
ATOM   9823  C  CA    . GLN A 1 2549 ? 136.988 112.026 180.020 1.00 66.83  ? 2549 GLN A CA    1 
ATOM   9824  C  C     . GLN A 1 2549 ? 137.248 110.619 180.544 1.00 68.65  ? 2549 GLN A C     1 
ATOM   9825  O  O     . GLN A 1 2549 ? 137.798 110.457 181.639 1.00 73.56  ? 2549 GLN A O     1 
ATOM   9826  C  CB    . GLN A 1 2549 ? 135.707 112.597 180.629 1.00 66.29  ? 2549 GLN A CB    1 
ATOM   9827  C  CG    . GLN A 1 2549 ? 135.788 112.878 182.120 1.00 75.63  ? 2549 GLN A CG    1 
ATOM   9828  C  CD    . GLN A 1 2549 ? 136.951 113.779 182.482 1.00 81.51  ? 2549 GLN A CD    1 
ATOM   9829  O  OE1   . GLN A 1 2549 ? 137.820 113.405 183.269 1.00 77.45  ? 2549 GLN A OE1   1 
ATOM   9830  N  NE2   . GLN A 1 2549 ? 136.971 114.977 181.911 1.00 76.92  ? 2549 GLN A NE2   1 
ATOM   9831  N  N     . ALA A 1 2550 ? 136.862 109.594 179.782 1.00 66.90  ? 2550 ALA A N     1 
ATOM   9832  C  CA    . ALA A 1 2550 ? 137.138 108.223 180.195 1.00 67.50  ? 2550 ALA A CA    1 
ATOM   9833  C  C     . ALA A 1 2550 ? 138.632 107.925 180.200 1.00 66.80  ? 2550 ALA A C     1 
ATOM   9834  O  O     . ALA A 1 2550 ? 139.098 107.121 181.014 1.00 65.81  ? 2550 ALA A O     1 
ATOM   9835  C  CB    . ALA A 1 2550 ? 136.406 107.241 179.283 1.00 68.85  ? 2550 ALA A CB    1 
ATOM   9836  N  N     . LYS A 1 2551 ? 139.394 108.557 179.309 1.00 66.06  ? 2551 LYS A N     1 
ATOM   9837  C  CA    . LYS A 1 2551 ? 140.833 108.335 179.246 1.00 67.58  ? 2551 LYS A CA    1 
ATOM   9838  C  C     . LYS A 1 2551 ? 141.610 109.202 180.224 1.00 67.62  ? 2551 LYS A C     1 
ATOM   9839  O  O     . LYS A 1 2551 ? 142.840 109.095 180.277 1.00 70.22  ? 2551 LYS A O     1 
ATOM   9840  C  CB    . LYS A 1 2551 ? 141.349 108.584 177.828 1.00 65.35  ? 2551 LYS A CB    1 
ATOM   9841  C  CG    . LYS A 1 2551 ? 140.692 107.729 176.764 1.00 64.78  ? 2551 LYS A CG    1 
ATOM   9842  C  CD    . LYS A 1 2551 ? 141.670 107.417 175.648 1.00 62.67  ? 2551 LYS A CD    1 
ATOM   9843  C  CE    . LYS A 1 2551 ? 142.436 106.137 175.924 1.00 71.26  ? 2551 LYS A CE    1 
ATOM   9844  N  NZ    . LYS A 1 2551 ? 141.531 104.957 175.993 1.00 74.71  ? 2551 LYS A NZ    1 
ATOM   9845  N  N     . VAL A 1 2552 ? 140.935 110.052 180.987 1.00 69.74  ? 2552 VAL A N     1 
ATOM   9846  C  CA    . VAL A 1 2552 ? 141.590 110.963 181.918 1.00 66.14  ? 2552 VAL A CA    1 
ATOM   9847  C  C     . VAL A 1 2552 ? 141.721 110.249 183.261 1.00 69.14  ? 2552 VAL A C     1 
ATOM   9848  O  O     . VAL A 1 2552 ? 140.693 109.929 183.879 1.00 69.26  ? 2552 VAL A O     1 
ATOM   9849  C  CB    . VAL A 1 2552 ? 140.803 112.269 182.066 1.00 64.61  ? 2552 VAL A CB    1 
ATOM   9850  C  CG1   . VAL A 1 2552 ? 141.208 112.994 183.331 1.00 69.82  ? 2552 VAL A CG1   1 
ATOM   9851  C  CG2   . VAL A 1 2552 ? 141.014 113.148 180.853 1.00 58.38  ? 2552 VAL A CG2   1 
ATOM   9852  N  N     . PRO A 1 2553 ? 142.930 109.973 183.733 1.00 73.82  ? 2553 PRO A N     1 
ATOM   9853  C  CA    . PRO A 1 2553 ? 143.101 109.355 185.047 1.00 78.58  ? 2553 PRO A CA    1 
ATOM   9854  C  C     . PRO A 1 2553 ? 143.024 110.391 186.164 1.00 83.57  ? 2553 PRO A C     1 
ATOM   9855  O  O     . PRO A 1 2553 ? 142.991 111.601 185.931 1.00 82.18  ? 2553 PRO A O     1 
ATOM   9856  C  CB    . PRO A 1 2553 ? 144.505 108.746 184.955 1.00 75.45  ? 2553 PRO A CB    1 
ATOM   9857  C  CG    . PRO A 1 2553 ? 145.233 109.671 184.047 1.00 68.77  ? 2553 PRO A CG    1 
ATOM   9858  C  CD    . PRO A 1 2553 ? 144.218 110.180 183.049 1.00 70.54  ? 2553 PRO A CD    1 
ATOM   9859  N  N     . GLN A 1 2554 ? 142.993 109.885 187.391 1.00 80.47  ? 2554 GLN A N     1 
ATOM   9860  C  CA    . GLN A 1 2554 ? 142.937 110.711 188.594 1.00 80.82  ? 2554 GLN A CA    1 
ATOM   9861  C  C     . GLN A 1 2554 ? 144.245 110.487 189.349 1.00 81.66  ? 2554 GLN A C     1 
ATOM   9862  O  O     . GLN A 1 2554 ? 144.335 109.623 190.223 1.00 86.67  ? 2554 GLN A O     1 
ATOM   9863  C  CB    . GLN A 1 2554 ? 141.719 110.355 189.442 1.00 82.85  ? 2554 GLN A CB    1 
ATOM   9864  C  CG    . GLN A 1 2554 ? 141.536 111.218 190.677 1.00 87.18  ? 2554 GLN A CG    1 
ATOM   9865  C  CD    . GLN A 1 2554 ? 141.312 112.676 190.336 1.00 92.36  ? 2554 GLN A CD    1 
ATOM   9866  O  OE1   . GLN A 1 2554 ? 142.208 113.506 190.490 1.00 94.05  ? 2554 GLN A OE1   1 
ATOM   9867  N  NE2   . GLN A 1 2554 ? 140.113 112.997 189.866 1.00 87.72  ? 2554 GLN A NE2   1 
ATOM   9868  N  N     . ILE A 1 2555 ? 145.265 111.270 189.001 1.00 79.53  ? 2555 ILE A N     1 
ATOM   9869  C  CA    . ILE A 1 2555 ? 146.588 111.110 189.594 1.00 77.82  ? 2555 ILE A CA    1 
ATOM   9870  C  C     . ILE A 1 2555 ? 146.624 111.789 190.954 1.00 79.06  ? 2555 ILE A C     1 
ATOM   9871  O  O     . ILE A 1 2555 ? 145.733 112.576 191.293 1.00 77.98  ? 2555 ILE A O     1 
ATOM   9872  C  CB    . ILE A 1 2555 ? 147.691 111.673 188.679 1.00 66.79  ? 2555 ILE A CB    1 
ATOM   9873  C  CG1   . ILE A 1 2555 ? 147.660 113.201 188.684 1.00 61.07  ? 2555 ILE A CG1   1 
ATOM   9874  C  CG2   . ILE A 1 2555 ? 147.541 111.134 187.267 1.00 69.79  ? 2555 ILE A CG2   1 
ATOM   9875  C  CD1   . ILE A 1 2555 ? 148.939 113.837 188.194 1.00 60.23  ? 2555 ILE A CD1   1 
ATOM   9876  N  N     . GLU A 1 2556 ? 147.651 111.484 191.743 1.00 78.69  ? 2556 GLU A N     1 
ATOM   9877  C  CA    . GLU A 1 2556 ? 147.857 112.102 193.046 1.00 79.09  ? 2556 GLU A CA    1 
ATOM   9878  C  C     . GLU A 1 2556 ? 149.283 112.623 193.116 1.00 78.56  ? 2556 GLU A C     1 
ATOM   9879  O  O     . GLU A 1 2556 ? 150.232 111.876 192.855 1.00 79.95  ? 2556 GLU A O     1 
ATOM   9880  C  CB    . GLU A 1 2556 ? 147.588 111.110 194.180 1.00 80.74  ? 2556 GLU A CB    1 
ATOM   9881  C  CG    . GLU A 1 2556 ? 146.118 110.946 194.512 1.00 83.45  ? 2556 GLU A CG    1 
ATOM   9882  C  CD    . GLU A 1 2556 ? 145.436 112.272 194.780 1.00 86.81  ? 2556 GLU A CD    1 
ATOM   9883  O  OE1   . GLU A 1 2556 ? 145.890 113.004 195.684 1.00 80.96  ? 2556 GLU A OE1   1 
ATOM   9884  O  OE2   . GLU A 1 2556 ? 144.449 112.584 194.082 1.00 83.86  ? 2556 GLU A OE2   1 
ATOM   9885  N  N     . VAL A 1 2557 ? 149.431 113.894 193.465 1.00 78.71  ? 2557 VAL A N     1 
ATOM   9886  C  CA    . VAL A 1 2557 ? 150.748 114.507 193.583 1.00 79.61  ? 2557 VAL A CA    1 
ATOM   9887  C  C     . VAL A 1 2557 ? 151.249 114.348 195.012 1.00 85.07  ? 2557 VAL A C     1 
ATOM   9888  O  O     . VAL A 1 2557 ? 150.466 114.293 195.968 1.00 88.40  ? 2557 VAL A O     1 
ATOM   9889  C  CB    . VAL A 1 2557 ? 150.690 115.989 193.161 1.00 77.52  ? 2557 VAL A CB    1 
ATOM   9890  C  CG1   . VAL A 1 2557 ? 152.089 116.548 192.960 1.00 84.76  ? 2557 VAL A CG1   1 
ATOM   9891  C  CG2   . VAL A 1 2557 ? 149.864 116.148 191.899 1.00 73.16  ? 2557 VAL A CG2   1 
ATOM   9892  N  N     . GLU A 1 2558 ? 152.568 114.265 195.164 1.00 87.25  ? 2558 GLU A N     1 
ATOM   9893  C  CA    . GLU A 1 2558 ? 153.165 114.162 196.485 1.00 88.90  ? 2558 GLU A CA    1 
ATOM   9894  C  C     . GLU A 1 2558 ? 153.067 115.501 197.215 1.00 90.75  ? 2558 GLU A C     1 
ATOM   9895  O  O     . GLU A 1 2558 ? 152.675 116.524 196.647 1.00 94.29  ? 2558 GLU A O     1 
ATOM   9896  C  CB    . GLU A 1 2558 ? 154.617 113.700 196.376 1.00 92.48  ? 2558 GLU A CB    1 
ATOM   9897  C  CG    . GLU A 1 2558 ? 154.764 112.309 195.776 1.00 106.11 ? 2558 GLU A CG    1 
ATOM   9898  C  CD    . GLU A 1 2558 ? 156.203 111.943 195.473 1.00 111.71 ? 2558 GLU A CD    1 
ATOM   9899  O  OE1   . GLU A 1 2558 ? 157.090 112.800 195.660 1.00 110.97 ? 2558 GLU A OE1   1 
ATOM   9900  O  OE2   . GLU A 1 2558 ? 156.448 110.794 195.050 1.00 107.74 ? 2558 GLU A OE2   1 
ATOM   9901  N  N     . THR A 1 2559 ? 153.417 115.480 198.504 1.00 90.95  ? 2559 THR A N     1 
ATOM   9902  C  CA    . THR A 1 2559 ? 153.287 116.678 199.331 1.00 85.93  ? 2559 THR A CA    1 
ATOM   9903  C  C     . THR A 1 2559 ? 154.125 117.823 198.776 1.00 85.89  ? 2559 THR A C     1 
ATOM   9904  O  O     . THR A 1 2559 ? 153.622 118.933 198.572 1.00 83.87  ? 2559 THR A O     1 
ATOM   9905  C  CB    . THR A 1 2559 ? 153.689 116.367 200.772 1.00 93.98  ? 2559 THR A CB    1 
ATOM   9906  O  OG1   . THR A 1 2559 ? 155.060 115.953 200.810 1.00 99.28  ? 2559 THR A OG1   1 
ATOM   9907  C  CG2   . THR A 1 2559 ? 152.817 115.257 201.336 1.00 91.89  ? 2559 THR A CG2   1 
ATOM   9908  N  N     . HIS A 1 2560 ? 155.405 117.571 198.518 1.00 89.07  ? 2560 HIS A N     1 
ATOM   9909  C  CA    . HIS A 1 2560 ? 156.229 118.544 197.822 1.00 90.62  ? 2560 HIS A CA    1 
ATOM   9910  C  C     . HIS A 1 2560 ? 155.946 118.465 196.324 1.00 92.83  ? 2560 HIS A C     1 
ATOM   9911  O  O     . HIS A 1 2560 ? 155.084 117.707 195.873 1.00 93.29  ? 2560 HIS A O     1 
ATOM   9912  C  CB    . HIS A 1 2560 ? 157.708 118.321 198.132 1.00 95.04  ? 2560 HIS A CB    1 
ATOM   9913  C  CG    . HIS A 1 2560 ? 158.229 116.985 197.701 1.00 102.78 ? 2560 HIS A CG    1 
ATOM   9914  N  ND1   . HIS A 1 2560 ? 157.594 115.801 198.009 1.00 104.14 ? 2560 HIS A ND1   1 
ATOM   9915  C  CD2   . HIS A 1 2560 ? 159.327 116.647 196.985 1.00 104.26 ? 2560 HIS A CD2   1 
ATOM   9916  C  CE1   . HIS A 1 2560 ? 158.280 114.791 197.504 1.00 105.83 ? 2560 HIS A CE1   1 
ATOM   9917  N  NE2   . HIS A 1 2560 ? 159.335 115.277 196.876 1.00 107.90 ? 2560 HIS A NE2   1 
ATOM   9918  N  N     . LYS A 1 2561 ? 156.671 119.274 195.546 1.00 94.57  ? 2561 LYS A N     1 
ATOM   9919  C  CA    . LYS A 1 2561 ? 156.478 119.378 194.093 1.00 96.54  ? 2561 LYS A CA    1 
ATOM   9920  C  C     . LYS A 1 2561 ? 155.006 119.607 193.734 1.00 89.00  ? 2561 LYS A C     1 
ATOM   9921  O  O     . LYS A 1 2561 ? 154.550 119.272 192.637 1.00 89.59  ? 2561 LYS A O     1 
ATOM   9922  C  CB    . LYS A 1 2561 ? 157.070 118.157 193.367 1.00 94.56  ? 2561 LYS A CB    1 
ATOM   9923  C  CG    . LYS A 1 2561 ? 156.178 116.925 193.212 1.00 97.20  ? 2561 LYS A CG    1 
ATOM   9924  C  CD    . LYS A 1 2561 ? 156.966 115.716 192.739 1.00 102.67 ? 2561 LYS A CD    1 
ATOM   9925  C  CE    . LYS A 1 2561 ? 156.096 114.783 191.911 1.00 99.38  ? 2561 LYS A CE    1 
ATOM   9926  N  NZ    . LYS A 1 2561 ? 156.727 113.447 191.733 1.00 95.58  ? 2561 LYS A NZ    1 
ATOM   9927  N  N     . VAL A 1 2562 ? 154.268 120.242 194.650 1.00 84.03  ? 2562 VAL A N     1 
ATOM   9928  C  CA    . VAL A 1 2562 ? 152.826 120.408 194.481 1.00 81.78  ? 2562 VAL A CA    1 
ATOM   9929  C  C     . VAL A 1 2562 ? 152.518 121.226 193.232 1.00 79.80  ? 2562 VAL A C     1 
ATOM   9930  O  O     . VAL A 1 2562 ? 151.558 120.939 192.508 1.00 81.60  ? 2562 VAL A O     1 
ATOM   9931  C  CB    . VAL A 1 2562 ? 152.209 121.034 195.747 1.00 74.62  ? 2562 VAL A CB    1 
ATOM   9932  C  CG1   . VAL A 1 2562 ? 152.858 122.372 196.066 1.00 75.46  ? 2562 VAL A CG1   1 
ATOM   9933  C  CG2   . VAL A 1 2562 ? 150.709 121.190 195.589 1.00 65.63  ? 2562 VAL A CG2   1 
ATOM   9934  N  N     . ALA A 1 2563 ? 153.324 122.244 192.951 1.00 76.61  ? 2563 ALA A N     1 
ATOM   9935  C  CA    . ALA A 1 2563 ? 153.163 123.060 191.755 1.00 75.15  ? 2563 ALA A CA    1 
ATOM   9936  C  C     . ALA A 1 2563 ? 154.463 123.109 190.971 1.00 85.83  ? 2563 ALA A C     1 
ATOM   9937  O  O     . ALA A 1 2563 ? 154.894 124.168 190.505 1.00 86.92  ? 2563 ALA A O     1 
ATOM   9938  C  CB    . ALA A 1 2563 ? 152.685 124.465 192.108 1.00 68.86  ? 2563 ALA A CB    1 
ATOM   9939  N  N     . ALA A 1 2564 ? 155.108 121.956 190.821 1.00 87.40  ? 2564 ALA A N     1 
ATOM   9940  C  CA    . ALA A 1 2564 ? 156.379 121.890 190.122 1.00 89.27  ? 2564 ALA A CA    1 
ATOM   9941  C  C     . ALA A 1 2564 ? 156.192 122.220 188.642 1.00 94.74  ? 2564 ALA A C     1 
ATOM   9942  O  O     . ALA A 1 2564 ? 155.124 121.977 188.072 1.00 94.39  ? 2564 ALA A O     1 
ATOM   9943  C  CB    . ALA A 1 2564 ? 156.997 120.503 190.274 1.00 90.31  ? 2564 ALA A CB    1 
ATOM   9944  N  N     . PRO A 1 2565 ? 157.217 122.781 187.995 1.00 96.54  ? 2565 PRO A N     1 
ATOM   9945  C  CA    . PRO A 1 2565 ? 157.080 123.155 186.581 1.00 98.33  ? 2565 PRO A CA    1 
ATOM   9946  C  C     . PRO A 1 2565 ? 157.168 121.972 185.629 1.00 94.69  ? 2565 PRO A C     1 
ATOM   9947  O  O     . PRO A 1 2565 ? 157.254 122.160 184.412 1.00 90.74  ? 2565 PRO A O     1 
ATOM   9948  C  CB    . PRO A 1 2565 ? 158.244 124.129 186.368 1.00 99.20  ? 2565 PRO A CB    1 
ATOM   9949  C  CG    . PRO A 1 2565 ? 159.269 123.691 187.354 1.00 94.87  ? 2565 PRO A CG    1 
ATOM   9950  C  CD    . PRO A 1 2565 ? 158.505 123.221 188.561 1.00 92.18  ? 2565 PRO A CD    1 
ATOM   9951  N  N     . ASP A 1 2566 ? 157.152 120.750 186.162 1.00 93.41  ? 2566 ASP A N     1 
ATOM   9952  C  CA    . ASP A 1 2566 ? 157.186 119.553 185.335 1.00 91.82  ? 2566 ASP A CA    1 
ATOM   9953  C  C     . ASP A 1 2566 ? 156.056 118.577 185.630 1.00 88.12  ? 2566 ASP A C     1 
ATOM   9954  O  O     . ASP A 1 2566 ? 155.986 117.524 184.986 1.00 87.64  ? 2566 ASP A O     1 
ATOM   9955  C  CB    . ASP A 1 2566 ? 158.539 118.839 185.481 1.00 100.67 ? 2566 ASP A CB    1 
ATOM   9956  C  CG    . ASP A 1 2566 ? 158.804 118.350 186.896 1.00 106.46 ? 2566 ASP A CG    1 
ATOM   9957  O  OD1   . ASP A 1 2566 ? 157.968 118.594 187.792 1.00 106.93 ? 2566 ASP A OD1   1 
ATOM   9958  O  OD2   . ASP A 1 2566 ? 159.856 117.714 187.111 1.00 103.92 ? 2566 ASP A OD2   1 
ATOM   9959  N  N     . VAL A 1 2567 ? 155.175 118.886 186.575 1.00 84.96  ? 2567 VAL A N     1 
ATOM   9960  C  CA    . VAL A 1 2567 ? 154.028 118.035 186.870 1.00 82.05  ? 2567 VAL A CA    1 
ATOM   9961  C  C     . VAL A 1 2567 ? 152.834 118.536 186.065 1.00 74.14  ? 2567 VAL A C     1 
ATOM   9962  O  O     . VAL A 1 2567 ? 152.528 119.733 186.058 1.00 76.62  ? 2567 VAL A O     1 
ATOM   9963  C  CB    . VAL A 1 2567 ? 153.730 117.993 188.380 1.00 82.56  ? 2567 VAL A CB    1 
ATOM   9964  C  CG1   . VAL A 1 2567 ? 153.198 119.324 188.898 1.00 78.12  ? 2567 VAL A CG1   1 
ATOM   9965  C  CG2   . VAL A 1 2567 ? 152.748 116.873 188.691 1.00 78.78  ? 2567 VAL A CG2   1 
ATOM   9966  N  N     . VAL A 1 2568 ? 152.194 117.626 185.337 1.00 64.21  ? 2568 VAL A N     1 
ATOM   9967  C  CA    . VAL A 1 2568 ? 151.038 117.942 184.509 1.00 56.03  ? 2568 VAL A CA    1 
ATOM   9968  C  C     . VAL A 1 2568 ? 149.908 117.023 184.942 1.00 55.39  ? 2568 VAL A C     1 
ATOM   9969  O  O     . VAL A 1 2568 ? 150.002 115.798 184.790 1.00 58.73  ? 2568 VAL A O     1 
ATOM   9970  C  CB    . VAL A 1 2568 ? 151.336 117.783 183.012 1.00 52.85  ? 2568 VAL A CB    1 
ATOM   9971  C  CG1   . VAL A 1 2568 ? 150.168 118.286 182.185 1.00 51.20  ? 2568 VAL A CG1   1 
ATOM   9972  C  CG2   . VAL A 1 2568 ? 152.604 118.526 182.643 1.00 56.34  ? 2568 VAL A CG2   1 
ATOM   9973  N  N     . VAL A 1 2569 ? 148.844 117.606 185.481 1.00 50.81  ? 2569 VAL A N     1 
ATOM   9974  C  CA    . VAL A 1 2569 ? 147.675 116.835 185.890 1.00 50.05  ? 2569 VAL A CA    1 
ATOM   9975  C  C     . VAL A 1 2569 ? 146.884 116.480 184.639 1.00 50.73  ? 2569 VAL A C     1 
ATOM   9976  O  O     . VAL A 1 2569 ? 146.459 117.380 183.901 1.00 52.88  ? 2569 VAL A O     1 
ATOM   9977  C  CB    . VAL A 1 2569 ? 146.818 117.614 186.898 1.00 47.66  ? 2569 VAL A CB    1 
ATOM   9978  C  CG1   . VAL A 1 2569 ? 145.624 116.784 187.328 1.00 51.50  ? 2569 VAL A CG1   1 
ATOM   9979  C  CG2   . VAL A 1 2569 ? 147.657 118.006 188.099 1.00 45.97  ? 2569 VAL A CG2   1 
ATOM   9980  N  N     . PRO A 1 2570 ? 146.675 115.196 184.352 1.00 52.87  ? 2570 PRO A N     1 
ATOM   9981  C  CA    . PRO A 1 2570 ? 145.935 114.818 183.141 1.00 54.22  ? 2570 PRO A CA    1 
ATOM   9982  C  C     . PRO A 1 2570 ? 144.497 115.305 183.201 1.00 56.56  ? 2570 PRO A C     1 
ATOM   9983  O  O     . PRO A 1 2570 ? 143.743 114.964 184.114 1.00 61.53  ? 2570 PRO A O     1 
ATOM   9984  C  CB    . PRO A 1 2570 ? 146.016 113.288 183.144 1.00 55.15  ? 2570 PRO A CB    1 
ATOM   9985  C  CG    . PRO A 1 2570 ? 147.203 112.971 183.980 1.00 53.51  ? 2570 PRO A CG    1 
ATOM   9986  C  CD    . PRO A 1 2570 ? 147.234 114.023 185.040 1.00 54.03  ? 2570 PRO A CD    1 
ATOM   9987  N  N     . THR A 1 2571 ? 144.123 116.113 182.215 1.00 49.57  ? 2571 THR A N     1 
ATOM   9988  C  CA    . THR A 1 2571 ? 142.759 116.587 182.056 1.00 52.28  ? 2571 THR A CA    1 
ATOM   9989  C  C     . THR A 1 2571 ? 142.312 116.299 180.630 1.00 54.22  ? 2571 THR A C     1 
ATOM   9990  O  O     . THR A 1 2571 ? 143.078 115.785 179.811 1.00 57.74  ? 2571 THR A O     1 
ATOM   9991  C  CB    . THR A 1 2571 ? 142.640 118.081 182.382 1.00 55.19  ? 2571 THR A CB    1 
ATOM   9992  O  OG1   . THR A 1 2571 ? 141.288 118.505 182.177 1.00 68.04  ? 2571 THR A OG1   1 
ATOM   9993  C  CG2   . THR A 1 2571 ? 143.559 118.898 181.495 1.00 53.69  ? 2571 THR A CG2   1 
ATOM   9994  N  N     . LEU A 1 2572 ? 141.052 116.624 180.337 1.00 56.08  ? 2572 LEU A N     1 
ATOM   9995  C  CA    . LEU A 1 2572 ? 140.494 116.334 179.020 1.00 51.27  ? 2572 LEU A CA    1 
ATOM   9996  C  C     . LEU A 1 2572 ? 141.294 117.029 177.925 1.00 51.46  ? 2572 LEU A C     1 
ATOM   9997  O  O     . LEU A 1 2572 ? 141.671 116.409 176.921 1.00 58.20  ? 2572 LEU A O     1 
ATOM   9998  C  CB    . LEU A 1 2572 ? 139.026 116.759 178.983 1.00 50.53  ? 2572 LEU A CB    1 
ATOM   9999  C  CG    . LEU A 1 2572 ? 138.137 116.263 177.845 1.00 62.17  ? 2572 LEU A CG    1 
ATOM   10000 C  CD1   . LEU A 1 2572 ? 136.725 116.045 178.353 1.00 67.94  ? 2572 LEU A CD1   1 
ATOM   10001 C  CD2   . LEU A 1 2572 ? 138.132 117.254 176.704 1.00 63.84  ? 2572 LEU A CD2   1 
ATOM   10002 N  N     . ASP A 1 2573 ? 141.587 118.316 178.120 1.00 50.95  ? 2573 ASP A N     1 
ATOM   10003 C  CA    . ASP A 1 2573 ? 142.395 119.050 177.153 1.00 49.49  ? 2573 ASP A CA    1 
ATOM   10004 C  C     . ASP A 1 2573 ? 143.784 118.442 177.024 1.00 44.16  ? 2573 ASP A C     1 
ATOM   10005 O  O     . ASP A 1 2573 ? 144.320 118.335 175.916 1.00 49.33  ? 2573 ASP A O     1 
ATOM   10006 C  CB    . ASP A 1 2573 ? 142.492 120.520 177.558 1.00 56.29  ? 2573 ASP A CB    1 
ATOM   10007 C  CG    . ASP A 1 2573 ? 141.135 121.175 177.712 1.00 63.04  ? 2573 ASP A CG    1 
ATOM   10008 O  OD1   . ASP A 1 2573 ? 140.334 120.699 178.543 1.00 66.93  ? 2573 ASP A OD1   1 
ATOM   10009 O  OD2   . ASP A 1 2573 ? 140.870 122.172 177.007 1.00 58.03  ? 2573 ASP A OD2   1 
ATOM   10010 N  N     . THR A 1 2574 ? 144.380 118.034 178.145 1.00 45.91  ? 2574 THR A N     1 
ATOM   10011 C  CA    . THR A 1 2574 ? 145.737 117.499 178.112 1.00 46.83  ? 2574 THR A CA    1 
ATOM   10012 C  C     . THR A 1 2574 ? 145.809 116.217 177.291 1.00 45.78  ? 2574 THR A C     1 
ATOM   10013 O  O     . THR A 1 2574 ? 146.659 116.086 176.405 1.00 48.69  ? 2574 THR A O     1 
ATOM   10014 C  CB    . THR A 1 2574 ? 146.244 117.260 179.535 1.00 50.21  ? 2574 THR A CB    1 
ATOM   10015 O  OG1   . THR A 1 2574 ? 146.585 118.514 180.136 1.00 59.52  ? 2574 THR A OG1   1 
ATOM   10016 C  CG2   . THR A 1 2574 ? 147.472 116.365 179.525 1.00 39.38  ? 2574 THR A CG2   1 
ATOM   10017 N  N     . VAL A 1 2575 ? 144.917 115.260 177.560 1.00 49.12  ? 2575 VAL A N     1 
ATOM   10018 C  CA    . VAL A 1 2575 ? 144.961 113.992 176.835 1.00 47.64  ? 2575 VAL A CA    1 
ATOM   10019 C  C     . VAL A 1 2575 ? 144.580 114.194 175.373 1.00 42.05  ? 2575 VAL A C     1 
ATOM   10020 O  O     . VAL A 1 2575 ? 145.163 113.575 174.473 1.00 43.29  ? 2575 VAL A O     1 
ATOM   10021 C  CB    . VAL A 1 2575 ? 144.067 112.941 177.522 1.00 42.33  ? 2575 VAL A CB    1 
ATOM   10022 C  CG1   . VAL A 1 2575 ? 144.607 112.608 178.903 1.00 45.59  ? 2575 VAL A CG1   1 
ATOM   10023 C  CG2   . VAL A 1 2575 ? 142.631 113.417 177.611 1.00 40.33  ? 2575 VAL A CG2   1 
ATOM   10024 N  N     . ARG A 1 2576 ? 143.609 115.071 175.111 1.00 40.12  ? 2576 ARG A N     1 
ATOM   10025 C  CA    . ARG A 1 2576 ? 143.200 115.348 173.739 1.00 38.83  ? 2576 ARG A CA    1 
ATOM   10026 C  C     . ARG A 1 2576 ? 144.358 115.927 172.928 1.00 37.70  ? 2576 ARG A C     1 
ATOM   10027 O  O     . ARG A 1 2576 ? 144.686 115.441 171.832 1.00 40.87  ? 2576 ARG A O     1 
ATOM   10028 C  CB    . ARG A 1 2576 ? 142.011 116.305 173.779 1.00 39.87  ? 2576 ARG A CB    1 
ATOM   10029 C  CG    . ARG A 1 2576 ? 141.167 116.376 172.545 1.00 50.91  ? 2576 ARG A CG    1 
ATOM   10030 C  CD    . ARG A 1 2576 ? 139.894 117.135 172.870 1.00 55.44  ? 2576 ARG A CD    1 
ATOM   10031 N  NE    . ARG A 1 2576 ? 140.183 118.498 173.295 1.00 51.05  ? 2576 ARG A NE    1 
ATOM   10032 C  CZ    . ARG A 1 2576 ? 139.284 119.332 173.799 1.00 56.07  ? 2576 ARG A CZ    1 
ATOM   10033 N  NH1   . ARG A 1 2576 ? 138.017 118.980 173.939 1.00 56.91  ? 2576 ARG A NH1   1 
ATOM   10034 N  NH2   . ARG A 1 2576 ? 139.665 120.551 174.168 1.00 57.41  ? 2576 ARG A NH2   1 
ATOM   10035 N  N     . HIS A 1 2577 ? 145.019 116.948 173.475 1.00 38.06  ? 2577 HIS A N     1 
ATOM   10036 C  CA    . HIS A 1 2577 ? 146.150 117.547 172.787 1.00 33.15  ? 2577 HIS A CA    1 
ATOM   10037 C  C     . HIS A 1 2577 ? 147.316 116.578 172.679 1.00 37.88  ? 2577 HIS A C     1 
ATOM   10038 O  O     . HIS A 1 2577 ? 148.018 116.585 171.670 1.00 43.08  ? 2577 HIS A O     1 
ATOM   10039 C  CB    . HIS A 1 2577 ? 146.577 118.827 173.500 1.00 32.57  ? 2577 HIS A CB    1 
ATOM   10040 C  CG    . HIS A 1 2577 ? 145.660 119.983 173.254 1.00 38.53  ? 2577 HIS A CG    1 
ATOM   10041 N  ND1   . HIS A 1 2577 ? 144.309 119.928 173.515 1.00 41.81  ? 2577 HIS A ND1   1 
ATOM   10042 C  CD2   . HIS A 1 2577 ? 145.897 121.221 172.761 1.00 45.76  ? 2577 HIS A CD2   1 
ATOM   10043 C  CE1   . HIS A 1 2577 ? 143.753 121.084 173.200 1.00 42.00  ? 2577 HIS A CE1   1 
ATOM   10044 N  NE2   . HIS A 1 2577 ? 144.696 121.886 172.739 1.00 45.34  ? 2577 HIS A NE2   1 
ATOM   10045 N  N     . GLU A 1 2578 ? 147.538 115.740 173.693 1.00 40.29  ? 2578 GLU A N     1 
ATOM   10046 C  CA    . GLU A 1 2578 ? 148.611 114.754 173.618 1.00 40.08  ? 2578 GLU A CA    1 
ATOM   10047 C  C     . GLU A 1 2578 ? 148.368 113.766 172.486 1.00 41.95  ? 2578 GLU A C     1 
ATOM   10048 O  O     . GLU A 1 2578 ? 149.304 113.378 171.775 1.00 46.56  ? 2578 GLU A O     1 
ATOM   10049 C  CB    . GLU A 1 2578 ? 148.739 114.033 174.959 1.00 40.75  ? 2578 GLU A CB    1 
ATOM   10050 C  CG    . GLU A 1 2578 ? 149.458 112.703 174.903 1.00 49.72  ? 2578 GLU A CG    1 
ATOM   10051 C  CD    . GLU A 1 2578 ? 149.248 111.881 176.160 1.00 61.19  ? 2578 GLU A CD    1 
ATOM   10052 O  OE1   . GLU A 1 2578 ? 149.769 112.276 177.224 1.00 68.87  ? 2578 GLU A OE1   1 
ATOM   10053 O  OE2   . GLU A 1 2578 ? 148.561 110.841 176.085 1.00 60.35  ? 2578 GLU A OE2   1 
ATOM   10054 N  N     . ALA A 1 2579 ? 147.112 113.353 172.298 1.00 40.87  ? 2579 ALA A N     1 
ATOM   10055 C  CA    . ALA A 1 2579 ? 146.778 112.516 171.151 1.00 36.50  ? 2579 ALA A CA    1 
ATOM   10056 C  C     . ALA A 1 2579 ? 147.070 113.239 169.843 1.00 36.43  ? 2579 ALA A C     1 
ATOM   10057 O  O     . ALA A 1 2579 ? 147.598 112.640 168.897 1.00 39.75  ? 2579 ALA A O     1 
ATOM   10058 C  CB    . ALA A 1 2579 ? 145.312 112.093 171.217 1.00 32.87  ? 2579 ALA A CB    1 
ATOM   10059 N  N     . LEU A 1 2580 ? 146.735 114.530 169.769 1.00 38.86  ? 2580 LEU A N     1 
ATOM   10060 C  CA    . LEU A 1 2580 ? 147.048 115.292 168.557 1.00 35.01  ? 2580 LEU A CA    1 
ATOM   10061 C  C     . LEU A 1 2580 ? 148.553 115.376 168.307 1.00 36.79  ? 2580 LEU A C     1 
ATOM   10062 O  O     . LEU A 1 2580 ? 149.007 115.245 167.162 1.00 38.82  ? 2580 LEU A O     1 
ATOM   10063 C  CB    . LEU A 1 2580 ? 146.443 116.690 168.637 1.00 34.66  ? 2580 LEU A CB    1 
ATOM   10064 C  CG    . LEU A 1 2580 ? 144.929 116.751 168.800 1.00 38.01  ? 2580 LEU A CG    1 
ATOM   10065 C  CD1   . LEU A 1 2580 ? 144.495 118.182 169.019 1.00 37.38  ? 2580 LEU A CD1   1 
ATOM   10066 C  CD2   . LEU A 1 2580 ? 144.256 116.165 167.576 1.00 36.90  ? 2580 LEU A CD2   1 
ATOM   10067 N  N     . LEU A 1 2581 ? 149.341 115.622 169.358 1.00 37.90  ? 2581 LEU A N     1 
ATOM   10068 C  CA    . LEU A 1 2581 ? 150.796 115.632 169.213 1.00 39.09  ? 2581 LEU A CA    1 
ATOM   10069 C  C     . LEU A 1 2581 ? 151.313 114.296 168.709 1.00 39.79  ? 2581 LEU A C     1 
ATOM   10070 O  O     . LEU A 1 2581 ? 152.172 114.250 167.828 1.00 45.87  ? 2581 LEU A O     1 
ATOM   10071 C  CB    . LEU A 1 2581 ? 151.503 115.988 170.523 1.00 39.59  ? 2581 LEU A CB    1 
ATOM   10072 C  CG    . LEU A 1 2581 ? 151.706 117.384 171.125 1.00 43.23  ? 2581 LEU A CG    1 
ATOM   10073 C  CD1   . LEU A 1 2581 ? 150.491 118.074 171.687 1.00 40.33  ? 2581 LEU A CD1   1 
ATOM   10074 C  CD2   . LEU A 1 2581 ? 152.773 117.251 172.191 1.00 41.94  ? 2581 LEU A CD2   1 
ATOM   10075 N  N     . TYR A 1 2582 ? 150.830 113.194 169.279 1.00 40.18  ? 2582 TYR A N     1 
ATOM   10076 C  CA    . TYR A 1 2582 ? 151.309 111.892 168.831 1.00 40.26  ? 2582 TYR A CA    1 
ATOM   10077 C  C     . TYR A 1 2582 ? 150.948 111.657 167.370 1.00 44.84  ? 2582 TYR A C     1 
ATOM   10078 O  O     . TYR A 1 2582 ? 151.775 111.169 166.587 1.00 48.82  ? 2582 TYR A O     1 
ATOM   10079 C  CB    . TYR A 1 2582 ? 150.751 110.788 169.727 1.00 42.10  ? 2582 TYR A CB    1 
ATOM   10080 C  CG    . TYR A 1 2582 ? 151.304 110.821 171.137 1.00 50.97  ? 2582 TYR A CG    1 
ATOM   10081 C  CD1   . TYR A 1 2582 ? 152.357 111.663 171.473 1.00 46.93  ? 2582 TYR A CD1   1 
ATOM   10082 C  CD2   . TYR A 1 2582 ? 150.776 110.010 172.130 1.00 52.79  ? 2582 TYR A CD2   1 
ATOM   10083 C  CE1   . TYR A 1 2582 ? 152.865 111.699 172.753 1.00 43.31  ? 2582 TYR A CE1   1 
ATOM   10084 C  CE2   . TYR A 1 2582 ? 151.280 110.039 173.416 1.00 54.93  ? 2582 TYR A CE2   1 
ATOM   10085 C  CZ    . TYR A 1 2582 ? 152.323 110.885 173.721 1.00 54.52  ? 2582 TYR A CZ    1 
ATOM   10086 O  OH    . TYR A 1 2582 ? 152.828 110.918 175.000 1.00 62.39  ? 2582 TYR A OH    1 
ATOM   10087 N  N     . THR A 1 2583 ? 149.731 112.042 166.977 1.00 45.76  ? 2583 THR A N     1 
ATOM   10088 C  CA    . THR A 1 2583 ? 149.318 111.906 165.584 1.00 39.02  ? 2583 THR A CA    1 
ATOM   10089 C  C     . THR A 1 2583 ? 150.240 112.683 164.652 1.00 39.29  ? 2583 THR A C     1 
ATOM   10090 O  O     . THR A 1 2583 ? 150.781 112.124 163.694 1.00 44.38  ? 2583 THR A O     1 
ATOM   10091 C  CB    . THR A 1 2583 ? 147.873 112.378 165.419 1.00 39.97  ? 2583 THR A CB    1 
ATOM   10092 O  OG1   . THR A 1 2583 ? 146.985 111.432 166.024 1.00 43.73  ? 2583 THR A OG1   1 
ATOM   10093 C  CG2   . THR A 1 2583 ? 147.526 112.532 163.952 1.00 37.21  ? 2583 THR A CG2   1 
ATOM   10094 N  N     . TRP A 1 2584 ? 150.452 113.969 164.929 1.00 41.37  ? 2584 TRP A N     1 
ATOM   10095 C  CA    . TRP A 1 2584 ? 151.210 114.810 164.009 1.00 38.08  ? 2584 TRP A CA    1 
ATOM   10096 C  C     . TRP A 1 2584 ? 152.717 114.676 164.156 1.00 41.30  ? 2584 TRP A C     1 
ATOM   10097 O  O     . TRP A 1 2584 ? 153.451 115.207 163.317 1.00 45.97  ? 2584 TRP A O     1 
ATOM   10098 C  CB    . TRP A 1 2584 ? 150.824 116.278 164.178 1.00 36.08  ? 2584 TRP A CB    1 
ATOM   10099 C  CG    . TRP A 1 2584 ? 149.489 116.591 163.615 1.00 34.78  ? 2584 TRP A CG    1 
ATOM   10100 C  CD1   . TRP A 1 2584 ? 149.000 116.206 162.404 1.00 34.59  ? 2584 TRP A CD1   1 
ATOM   10101 C  CD2   . TRP A 1 2584 ? 148.460 117.358 164.239 1.00 32.24  ? 2584 TRP A CD2   1 
ATOM   10102 N  NE1   . TRP A 1 2584 ? 147.726 116.684 162.237 1.00 33.59  ? 2584 TRP A NE1   1 
ATOM   10103 C  CE2   . TRP A 1 2584 ? 147.372 117.397 163.351 1.00 32.47  ? 2584 TRP A CE2   1 
ATOM   10104 C  CE3   . TRP A 1 2584 ? 148.353 118.016 165.465 1.00 33.28  ? 2584 TRP A CE3   1 
ATOM   10105 C  CZ2   . TRP A 1 2584 ? 146.192 118.067 163.650 1.00 34.67  ? 2584 TRP A CZ2   1 
ATOM   10106 C  CZ3   . TRP A 1 2584 ? 147.185 118.678 165.758 1.00 37.87  ? 2584 TRP A CZ3   1 
ATOM   10107 C  CH2   . TRP A 1 2584 ? 146.120 118.702 164.855 1.00 36.55  ? 2584 TRP A CH2   1 
ATOM   10108 N  N     . LEU A 1 2585 ? 153.199 113.994 165.191 1.00 42.71  ? 2585 LEU A N     1 
ATOM   10109 C  CA    . LEU A 1 2585 ? 154.619 113.718 165.325 1.00 44.31  ? 2585 LEU A CA    1 
ATOM   10110 C  C     . LEU A 1 2585 ? 154.992 112.337 164.821 1.00 50.77  ? 2585 LEU A C     1 
ATOM   10111 O  O     . LEU A 1 2585 ? 156.176 112.082 164.583 1.00 56.13  ? 2585 LEU A O     1 
ATOM   10112 C  CB    . LEU A 1 2585 ? 155.051 113.859 166.787 1.00 45.52  ? 2585 LEU A CB    1 
ATOM   10113 C  CG    . LEU A 1 2585 ? 155.143 115.298 167.294 1.00 47.85  ? 2585 LEU A CG    1 
ATOM   10114 C  CD1   . LEU A 1 2585 ? 155.394 115.312 168.786 1.00 36.69  ? 2585 LEU A CD1   1 
ATOM   10115 C  CD2   . LEU A 1 2585 ? 156.222 116.066 166.554 1.00 51.91  ? 2585 LEU A CD2   1 
ATOM   10116 N  N     . ALA A 1 2586 ? 154.014 111.441 164.663 1.00 51.43  ? 2586 ALA A N     1 
ATOM   10117 C  CA    . ALA A 1 2586 ? 154.280 110.207 163.936 1.00 52.64  ? 2586 ALA A CA    1 
ATOM   10118 C  C     . ALA A 1 2586 ? 154.660 110.492 162.489 1.00 54.55  ? 2586 ALA A C     1 
ATOM   10119 O  O     . ALA A 1 2586 ? 155.431 109.734 161.891 1.00 59.60  ? 2586 ALA A O     1 
ATOM   10120 C  CB    . ALA A 1 2586 ? 153.065 109.285 164.005 1.00 48.33  ? 2586 ALA A CB    1 
ATOM   10121 N  N     . GLU A 1 2587 ? 154.137 111.574 161.913 1.00 49.50  ? 2587 GLU A N     1 
ATOM   10122 C  CA    . GLU A 1 2587 ? 154.491 112.000 160.566 1.00 52.09  ? 2587 GLU A CA    1 
ATOM   10123 C  C     . GLU A 1 2587 ? 155.528 113.116 160.554 1.00 52.37  ? 2587 GLU A C     1 
ATOM   10124 O  O     . GLU A 1 2587 ? 155.820 113.664 159.486 1.00 54.87  ? 2587 GLU A O     1 
ATOM   10125 C  CB    . GLU A 1 2587 ? 153.243 112.439 159.797 1.00 49.68  ? 2587 GLU A CB    1 
ATOM   10126 C  CG    . GLU A 1 2587 ? 152.296 111.300 159.456 1.00 57.52  ? 2587 GLU A CG    1 
ATOM   10127 C  CD    . GLU A 1 2587 ? 151.160 111.169 160.449 1.00 59.38  ? 2587 GLU A CD    1 
ATOM   10128 O  OE1   . GLU A 1 2587 ? 150.743 112.203 161.004 1.00 61.02  ? 2587 GLU A OE1   1 
ATOM   10129 O  OE2   . GLU A 1 2587 ? 150.689 110.036 160.679 1.00 54.08  ? 2587 GLU A OE2   1 
ATOM   10130 N  N     . HIS A 1 2588 ? 156.076 113.473 161.718 1.00 49.10  ? 2588 HIS A N     1 
ATOM   10131 C  CA    . HIS A 1 2588 ? 157.218 114.384 161.822 1.00 47.18  ? 2588 HIS A CA    1 
ATOM   10132 C  C     . HIS A 1 2588 ? 156.889 115.779 161.292 1.00 43.89  ? 2588 HIS A C     1 
ATOM   10133 O  O     . HIS A 1 2588 ? 157.724 116.437 160.669 1.00 46.22  ? 2588 HIS A O     1 
ATOM   10134 C  CB    . HIS A 1 2588 ? 158.441 113.807 161.105 1.00 48.81  ? 2588 HIS A CB    1 
ATOM   10135 C  CG    . HIS A 1 2588 ? 158.706 112.371 161.432 1.00 59.18  ? 2588 HIS A CG    1 
ATOM   10136 N  ND1   . HIS A 1 2588 ? 158.881 111.920 162.722 1.00 62.77  ? 2588 HIS A ND1   1 
ATOM   10137 C  CD2   . HIS A 1 2588 ? 158.821 111.282 160.636 1.00 63.72  ? 2588 HIS A CD2   1 
ATOM   10138 C  CE1   . HIS A 1 2588 ? 159.094 110.617 162.708 1.00 60.10  ? 2588 HIS A CE1   1 
ATOM   10139 N  NE2   . HIS A 1 2588 ? 159.062 110.204 161.453 1.00 64.31  ? 2588 HIS A NE2   1 
ATOM   10140 N  N     . LYS A 1 2589 ? 155.667 116.239 161.543 1.00 40.69  ? 2589 LYS A N     1 
ATOM   10141 C  CA    . LYS A 1 2589 ? 155.286 117.574 161.110 1.00 34.94  ? 2589 LYS A CA    1 
ATOM   10142 C  C     . LYS A 1 2589 ? 155.689 118.620 162.149 1.00 36.16  ? 2589 LYS A C     1 
ATOM   10143 O  O     . LYS A 1 2589 ? 155.802 118.313 163.338 1.00 42.36  ? 2589 LYS A O     1 
ATOM   10144 C  CB    . LYS A 1 2589 ? 153.785 117.647 160.866 1.00 35.68  ? 2589 LYS A CB    1 
ATOM   10145 C  CG    . LYS A 1 2589 ? 153.255 116.554 159.969 1.00 41.28  ? 2589 LYS A CG    1 
ATOM   10146 C  CD    . LYS A 1 2589 ? 151.803 116.800 159.635 1.00 39.27  ? 2589 LYS A CD    1 
ATOM   10147 C  CE    . LYS A 1 2589 ? 151.633 118.057 158.804 1.00 35.89  ? 2589 LYS A CE    1 
ATOM   10148 N  NZ    . LYS A 1 2589 ? 152.412 117.988 157.540 1.00 35.51  ? 2589 LYS A NZ    1 
ATOM   10149 N  N     . PRO A 1 2590 ? 155.910 119.868 161.723 1.00 33.07  ? 2590 PRO A N     1 
ATOM   10150 C  CA    . PRO A 1 2590 ? 156.293 120.935 162.673 1.00 28.93  ? 2590 PRO A CA    1 
ATOM   10151 C  C     . PRO A 1 2590 ? 155.101 121.465 163.460 1.00 28.69  ? 2590 PRO A C     1 
ATOM   10152 O  O     . PRO A 1 2590 ? 154.687 122.618 163.337 1.00 31.26  ? 2590 PRO A O     1 
ATOM   10153 C  CB    . PRO A 1 2590 ? 156.909 121.996 161.750 1.00 31.26  ? 2590 PRO A CB    1 
ATOM   10154 C  CG    . PRO A 1 2590 ? 157.022 121.363 160.391 1.00 38.42  ? 2590 PRO A CG    1 
ATOM   10155 C  CD    . PRO A 1 2590 ? 155.957 120.340 160.334 1.00 35.82  ? 2590 PRO A CD    1 
ATOM   10156 N  N     . LEU A 1 2591 ? 154.542 120.604 164.305 1.00 29.60  ? 2591 LEU A N     1 
ATOM   10157 C  CA    . LEU A 1 2591 ? 153.350 120.955 165.066 1.00 28.29  ? 2591 LEU A CA    1 
ATOM   10158 C  C     . LEU A 1 2591 ? 153.585 122.186 165.931 1.00 26.60  ? 2591 LEU A C     1 
ATOM   10159 O  O     . LEU A 1 2591 ? 154.606 122.305 166.613 1.00 34.19  ? 2591 LEU A O     1 
ATOM   10160 C  CB    . LEU A 1 2591 ? 152.931 119.777 165.941 1.00 31.44  ? 2591 LEU A CB    1 
ATOM   10161 C  CG    . LEU A 1 2591 ? 152.004 120.099 167.110 1.00 35.89  ? 2591 LEU A CG    1 
ATOM   10162 C  CD1   . LEU A 1 2591 ? 150.621 120.490 166.628 1.00 35.98  ? 2591 LEU A CD1   1 
ATOM   10163 C  CD2   . LEU A 1 2591 ? 151.927 118.911 168.022 1.00 41.34  ? 2591 LEU A CD2   1 
ATOM   10164 N  N     . VAL A 1 2592 ? 152.624 123.106 165.901 1.00 24.63  ? 2592 VAL A N     1 
ATOM   10165 C  CA    . VAL A 1 2592 ? 152.667 124.339 166.677 1.00 25.05  ? 2592 VAL A CA    1 
ATOM   10166 C  C     . VAL A 1 2592 ? 151.411 124.418 167.530 1.00 28.59  ? 2592 VAL A C     1 
ATOM   10167 O  O     . VAL A 1 2592 ? 150.303 124.214 167.024 1.00 30.73  ? 2592 VAL A O     1 
ATOM   10168 C  CB    . VAL A 1 2592 ? 152.775 125.579 165.770 1.00 25.97  ? 2592 VAL A CB    1 
ATOM   10169 C  CG1   . VAL A 1 2592 ? 152.680 126.840 166.590 1.00 22.00  ? 2592 VAL A CG1   1 
ATOM   10170 C  CG2   . VAL A 1 2592 ? 154.076 125.554 164.994 1.00 28.21  ? 2592 VAL A CG2   1 
ATOM   10171 N  N     . LEU A 1 2593 ? 151.579 124.704 168.819 1.00 26.46  ? 2593 LEU A N     1 
ATOM   10172 C  CA    . LEU A 1 2593 ? 150.448 125.016 169.691 1.00 24.99  ? 2593 LEU A CA    1 
ATOM   10173 C  C     . LEU A 1 2593 ? 150.439 126.516 169.951 1.00 26.10  ? 2593 LEU A C     1 
ATOM   10174 O  O     . LEU A 1 2593 ? 151.440 127.078 170.401 1.00 36.84  ? 2593 LEU A O     1 
ATOM   10175 C  CB    . LEU A 1 2593 ? 150.485 124.254 171.014 1.00 22.82  ? 2593 LEU A CB    1 
ATOM   10176 C  CG    . LEU A 1 2593 ? 150.339 122.735 171.074 1.00 31.14  ? 2593 LEU A CG    1 
ATOM   10177 C  CD1   . LEU A 1 2593 ? 150.523 122.279 172.499 1.00 28.28  ? 2593 LEU A CD1   1 
ATOM   10178 C  CD2   . LEU A 1 2593 ? 149.016 122.258 170.546 1.00 43.14  ? 2593 LEU A CD2   1 
ATOM   10179 N  N     . CYS A 1 2594 ? 149.309 127.155 169.680 1.00 25.26  ? 2594 CYS A N     1 
ATOM   10180 C  CA    . CYS A 1 2594 ? 149.122 128.570 169.950 1.00 27.26  ? 2594 CYS A CA    1 
ATOM   10181 C  C     . CYS A 1 2594 ? 148.025 128.753 170.989 1.00 36.49  ? 2594 CYS A C     1 
ATOM   10182 O  O     . CYS A 1 2594 ? 147.163 127.891 171.163 1.00 43.20  ? 2594 CYS A O     1 
ATOM   10183 C  CB    . CYS A 1 2594 ? 148.767 129.328 168.671 1.00 32.54  ? 2594 CYS A CB    1 
ATOM   10184 S  SG    . CYS A 1 2594 ? 148.501 131.095 168.896 1.00 62.95  ? 2594 CYS A SG    1 
ATOM   10185 N  N     . GLY A 1 2595 ? 148.072 129.877 171.695 1.00 35.73  ? 2595 GLY A N     1 
ATOM   10186 C  CA    . GLY A 1 2595 ? 147.069 130.172 172.687 1.00 33.95  ? 2595 GLY A CA    1 
ATOM   10187 C  C     . GLY A 1 2595 ? 147.480 131.278 173.633 1.00 38.73  ? 2595 GLY A C     1 
ATOM   10188 O  O     . GLY A 1 2595 ? 148.622 131.744 173.625 1.00 42.54  ? 2595 GLY A O     1 
ATOM   10189 N  N     . PRO A 1 2596 ? 146.545 131.717 174.477 1.00 41.93  ? 2596 PRO A N     1 
ATOM   10190 C  CA    . PRO A 1 2596 ? 146.861 132.782 175.423 1.00 39.25  ? 2596 PRO A CA    1 
ATOM   10191 C  C     . PRO A 1 2596 ? 147.868 132.305 176.452 1.00 40.01  ? 2596 PRO A C     1 
ATOM   10192 O  O     . PRO A 1 2596 ? 147.989 131.095 176.709 1.00 40.91  ? 2596 PRO A O     1 
ATOM   10193 C  CB    . PRO A 1 2596 ? 145.500 133.094 176.070 1.00 36.80  ? 2596 PRO A CB    1 
ATOM   10194 C  CG    . PRO A 1 2596 ? 144.731 131.832 175.922 1.00 37.27  ? 2596 PRO A CG    1 
ATOM   10195 C  CD    . PRO A 1 2596 ? 145.152 131.258 174.607 1.00 41.69  ? 2596 PRO A CD    1 
ATOM   10196 N  N     . PRO A 1 2597 ? 148.628 133.217 177.058 1.00 38.52  ? 2597 PRO A N     1 
ATOM   10197 C  CA    . PRO A 1 2597 ? 149.637 132.799 178.036 1.00 37.99  ? 2597 PRO A CA    1 
ATOM   10198 C  C     . PRO A 1 2597 ? 149.005 132.155 179.260 1.00 37.75  ? 2597 PRO A C     1 
ATOM   10199 O  O     . PRO A 1 2597 ? 147.911 132.522 179.691 1.00 42.40  ? 2597 PRO A O     1 
ATOM   10200 C  CB    . PRO A 1 2597 ? 150.346 134.110 178.396 1.00 37.02  ? 2597 PRO A CB    1 
ATOM   10201 C  CG    . PRO A 1 2597 ? 149.354 135.169 178.083 1.00 39.62  ? 2597 PRO A CG    1 
ATOM   10202 C  CD    . PRO A 1 2597 ? 148.596 134.680 176.890 1.00 36.82  ? 2597 PRO A CD    1 
ATOM   10203 N  N     . GLY A 1 2598 ? 149.718 131.182 179.821 1.00 32.51  ? 2598 GLY A N     1 
ATOM   10204 C  CA    . GLY A 1 2598 ? 149.256 130.453 180.981 1.00 30.25  ? 2598 GLY A CA    1 
ATOM   10205 C  C     . GLY A 1 2598 ? 148.346 129.284 180.688 1.00 32.76  ? 2598 GLY A C     1 
ATOM   10206 O  O     . GLY A 1 2598 ? 147.950 128.583 181.627 1.00 33.30  ? 2598 GLY A O     1 
ATOM   10207 N  N     . SER A 1 2599 ? 148.005 129.041 179.420 1.00 35.76  ? 2599 SER A N     1 
ATOM   10208 C  CA    . SER A 1 2599 ? 147.093 127.951 179.092 1.00 34.16  ? 2599 SER A CA    1 
ATOM   10209 C  C     . SER A 1 2599 ? 147.723 126.587 179.342 1.00 34.70  ? 2599 SER A C     1 
ATOM   10210 O  O     . SER A 1 2599 ? 147.019 125.642 179.712 1.00 36.74  ? 2599 SER A O     1 
ATOM   10211 C  CB    . SER A 1 2599 ? 146.636 128.068 177.640 1.00 30.76  ? 2599 SER A CB    1 
ATOM   10212 O  OG    . SER A 1 2599 ? 147.725 128.357 176.785 1.00 34.13  ? 2599 SER A OG    1 
ATOM   10213 N  N     . GLY A 1 2600 ? 149.031 126.461 179.145 1.00 31.93  ? 2600 GLY A N     1 
ATOM   10214 C  CA    . GLY A 1 2600 ? 149.707 125.208 179.413 1.00 27.19  ? 2600 GLY A CA    1 
ATOM   10215 C  C     . GLY A 1 2600 ? 150.373 124.611 178.193 1.00 29.41  ? 2600 GLY A C     1 
ATOM   10216 O  O     . GLY A 1 2600 ? 150.556 123.395 178.114 1.00 33.86  ? 2600 GLY A O     1 
ATOM   10217 N  N     . LYS A 1 2601 ? 150.737 125.459 177.232 1.00 27.65  ? 2601 LYS A N     1 
ATOM   10218 C  CA    . LYS A 1 2601 ? 151.365 124.972 176.009 1.00 23.85  ? 2601 LYS A CA    1 
ATOM   10219 C  C     . LYS A 1 2601 ? 152.718 124.334 176.297 1.00 29.13  ? 2601 LYS A C     1 
ATOM   10220 O  O     . LYS A 1 2601 ? 152.976 123.190 175.905 1.00 36.09  ? 2601 LYS A O     1 
ATOM   10221 C  CB    . LYS A 1 2601 ? 151.519 126.124 175.020 1.00 23.08  ? 2601 LYS A CB    1 
ATOM   10222 C  CG    . LYS A 1 2601 ? 150.214 126.776 174.627 1.00 25.39  ? 2601 LYS A CG    1 
ATOM   10223 C  CD    . LYS A 1 2601 ? 150.462 127.976 173.745 1.00 27.45  ? 2601 LYS A CD    1 
ATOM   10224 C  CE    . LYS A 1 2601 ? 151.089 129.100 174.538 1.00 25.73  ? 2601 LYS A CE    1 
ATOM   10225 N  NZ    . LYS A 1 2601 ? 150.153 129.615 175.569 1.00 29.12  ? 2601 LYS A NZ    1 
ATOM   10226 N  N     . THR A 1 2602 ? 153.591 125.061 176.999 1.00 31.89  ? 2602 THR A N     1 
ATOM   10227 C  CA    . THR A 1 2602 ? 154.960 124.596 177.196 1.00 31.67  ? 2602 THR A CA    1 
ATOM   10228 C  C     . THR A 1 2602 ? 155.006 123.313 178.013 1.00 32.93  ? 2602 THR A C     1 
ATOM   10229 O  O     . THR A 1 2602 ? 155.718 122.369 177.656 1.00 42.06  ? 2602 THR A O     1 
ATOM   10230 C  CB    . THR A 1 2602 ? 155.790 125.686 177.872 1.00 33.04  ? 2602 THR A CB    1 
ATOM   10231 O  OG1   . THR A 1 2602 ? 155.808 126.857 177.047 1.00 39.45  ? 2602 THR A OG1   1 
ATOM   10232 C  CG2   . THR A 1 2602 ? 157.212 125.213 178.092 1.00 36.56  ? 2602 THR A CG2   1 
ATOM   10233 N  N     . MET A 1 2603 ? 154.247 123.253 179.108 1.00 34.37  ? 2603 MET A N     1 
ATOM   10234 C  CA    . MET A 1 2603 ? 154.311 122.081 179.975 1.00 40.30  ? 2603 MET A CA    1 
ATOM   10235 C  C     . MET A 1 2603 ? 153.701 120.857 179.307 1.00 39.86  ? 2603 MET A C     1 
ATOM   10236 O  O     . MET A 1 2603 ? 154.242 119.752 179.413 1.00 46.73  ? 2603 MET A O     1 
ATOM   10237 C  CB    . MET A 1 2603 ? 153.632 122.370 181.311 1.00 43.26  ? 2603 MET A CB    1 
ATOM   10238 C  CG    . MET A 1 2603 ? 154.368 123.400 182.141 1.00 53.78  ? 2603 MET A CG    1 
ATOM   10239 S  SD    . MET A 1 2603 ? 153.522 123.786 183.674 1.00 76.77  ? 2603 MET A SD    1 
ATOM   10240 C  CE    . MET A 1 2603 ? 153.771 122.267 184.583 1.00 74.85  ? 2603 MET A CE    1 
ATOM   10241 N  N     . THR A 1 2604 ? 152.571 121.026 178.617 1.00 35.40  ? 2604 THR A N     1 
ATOM   10242 C  CA    . THR A 1 2604 ? 151.982 119.889 177.916 1.00 37.09  ? 2604 THR A CA    1 
ATOM   10243 C  C     . THR A 1 2604 ? 152.905 119.385 176.815 1.00 39.84  ? 2604 THR A C     1 
ATOM   10244 O  O     . THR A 1 2604 ? 153.104 118.172 176.675 1.00 50.40  ? 2604 THR A O     1 
ATOM   10245 C  CB    . THR A 1 2604 ? 150.615 120.257 177.340 1.00 35.38  ? 2604 THR A CB    1 
ATOM   10246 O  OG1   . THR A 1 2604 ? 150.718 121.470 176.586 1.00 36.88  ? 2604 THR A OG1   1 
ATOM   10247 C  CG2   . THR A 1 2604 ? 149.594 120.432 178.456 1.00 43.07  ? 2604 THR A CG2   1 
ATOM   10248 N  N     . LEU A 1 2605 ? 153.492 120.298 176.037 1.00 35.70  ? 2605 LEU A N     1 
ATOM   10249 C  CA    . LEU A 1 2605 ? 154.431 119.889 174.997 1.00 36.93  ? 2605 LEU A CA    1 
ATOM   10250 C  C     . LEU A 1 2605 ? 155.626 119.151 175.585 1.00 40.05  ? 2605 LEU A C     1 
ATOM   10251 O  O     . LEU A 1 2605 ? 155.997 118.076 175.103 1.00 49.91  ? 2605 LEU A O     1 
ATOM   10252 C  CB    . LEU A 1 2605 ? 154.878 121.108 174.193 1.00 35.82  ? 2605 LEU A CB    1 
ATOM   10253 C  CG    . LEU A 1 2605 ? 153.779 121.612 173.263 1.00 39.62  ? 2605 LEU A CG    1 
ATOM   10254 C  CD1   . LEU A 1 2605 ? 154.066 122.957 172.640 1.00 42.32  ? 2605 LEU A CD1   1 
ATOM   10255 C  CD2   . LEU A 1 2605 ? 153.618 120.598 172.160 1.00 37.26  ? 2605 LEU A CD2   1 
ATOM   10256 N  N     . PHE A 1 2606 ? 156.231 119.699 176.640 1.00 34.90  ? 2606 PHE A N     1 
ATOM   10257 C  CA    . PHE A 1 2606 ? 157.399 119.052 177.225 1.00 37.21  ? 2606 PHE A CA    1 
ATOM   10258 C  C     . PHE A 1 2606 ? 157.048 117.691 177.810 1.00 40.39  ? 2606 PHE A C     1 
ATOM   10259 O  O     . PHE A 1 2606 ? 157.786 116.720 177.615 1.00 45.99  ? 2606 PHE A O     1 
ATOM   10260 C  CB    . PHE A 1 2606 ? 158.025 119.949 178.289 1.00 37.76  ? 2606 PHE A CB    1 
ATOM   10261 C  CG    . PHE A 1 2606 ? 159.114 120.835 177.766 1.00 37.73  ? 2606 PHE A CG    1 
ATOM   10262 C  CD1   . PHE A 1 2606 ? 160.173 120.302 177.054 1.00 42.15  ? 2606 PHE A CD1   1 
ATOM   10263 C  CD2   . PHE A 1 2606 ? 159.084 122.198 177.990 1.00 42.34  ? 2606 PHE A CD2   1 
ATOM   10264 C  CE1   . PHE A 1 2606 ? 161.179 121.113 176.571 1.00 48.92  ? 2606 PHE A CE1   1 
ATOM   10265 C  CE2   . PHE A 1 2606 ? 160.087 123.013 177.509 1.00 46.24  ? 2606 PHE A CE2   1 
ATOM   10266 C  CZ    . PHE A 1 2606 ? 161.136 122.469 176.800 1.00 48.81  ? 2606 PHE A CZ    1 
ATOM   10267 N  N     . SER A 1 2607 ? 155.924 117.594 178.523 1.00 39.13  ? 2607 SER A N     1 
ATOM   10268 C  CA    . SER A 1 2607 ? 155.546 116.327 179.137 1.00 43.04  ? 2607 SER A CA    1 
ATOM   10269 C  C     . SER A 1 2607 ? 155.260 115.268 178.082 1.00 46.84  ? 2607 SER A C     1 
ATOM   10270 O  O     . SER A 1 2607 ? 155.693 114.116 178.209 1.00 54.73  ? 2607 SER A O     1 
ATOM   10271 C  CB    . SER A 1 2607 ? 154.333 116.526 180.044 1.00 44.68  ? 2607 SER A CB    1 
ATOM   10272 O  OG    . SER A 1 2607 ? 153.176 116.829 179.286 1.00 48.36  ? 2607 SER A OG    1 
ATOM   10273 N  N     . ALA A 1 2608 ? 154.537 115.639 177.023 1.00 41.21  ? 2608 ALA A N     1 
ATOM   10274 C  CA    . ALA A 1 2608 ? 154.233 114.670 175.976 1.00 43.61  ? 2608 ALA A CA    1 
ATOM   10275 C  C     . ALA A 1 2608 ? 155.491 114.248 175.227 1.00 49.88  ? 2608 ALA A C     1 
ATOM   10276 O  O     . ALA A 1 2608 ? 155.653 113.067 174.898 1.00 52.49  ? 2608 ALA A O     1 
ATOM   10277 C  CB    . ALA A 1 2608 ? 153.197 115.245 175.016 1.00 40.72  ? 2608 ALA A CB    1 
ATOM   10278 N  N     . LEU A 1 2609 ? 156.392 115.193 174.946 1.00 46.48  ? 2609 LEU A N     1 
ATOM   10279 C  CA    . LEU A 1 2609 ? 157.632 114.848 174.260 1.00 44.06  ? 2609 LEU A CA    1 
ATOM   10280 C  C     . LEU A 1 2609 ? 158.503 113.935 175.112 1.00 55.60  ? 2609 LEU A C     1 
ATOM   10281 O  O     . LEU A 1 2609 ? 159.103 112.983 174.599 1.00 63.18  ? 2609 LEU A O     1 
ATOM   10282 C  CB    . LEU A 1 2609 ? 158.391 116.119 173.884 1.00 39.69  ? 2609 LEU A CB    1 
ATOM   10283 C  CG    . LEU A 1 2609 ? 157.776 117.001 172.798 1.00 38.08  ? 2609 LEU A CG    1 
ATOM   10284 C  CD1   . LEU A 1 2609 ? 158.767 118.051 172.337 1.00 37.68  ? 2609 LEU A CD1   1 
ATOM   10285 C  CD2   . LEU A 1 2609 ? 157.332 116.147 171.637 1.00 42.73  ? 2609 LEU A CD2   1 
ATOM   10286 N  N     . ARG A 1 2610 ? 158.589 114.206 176.417 1.00 51.76  ? 2610 ARG A N     1 
ATOM   10287 C  CA    . ARG A 1 2610 ? 159.398 113.364 177.290 1.00 53.70  ? 2610 ARG A CA    1 
ATOM   10288 C  C     . ARG A 1 2610 ? 158.736 112.016 177.539 1.00 57.89  ? 2610 ARG A C     1 
ATOM   10289 O  O     . ARG A 1 2610 ? 159.419 111.049 177.896 1.00 63.71  ? 2610 ARG A O     1 
ATOM   10290 C  CB    . ARG A 1 2610 ? 159.666 114.083 178.611 1.00 48.44  ? 2610 ARG A CB    1 
ATOM   10291 C  CG    . ARG A 1 2610 ? 160.449 115.375 178.456 1.00 47.76  ? 2610 ARG A CG    1 
ATOM   10292 C  CD    . ARG A 1 2610 ? 160.702 116.041 179.799 1.00 50.38  ? 2610 ARG A CD    1 
ATOM   10293 N  NE    . ARG A 1 2610 ? 161.126 117.430 179.663 1.00 49.68  ? 2610 ARG A NE    1 
ATOM   10294 C  CZ    . ARG A 1 2610 ? 162.289 117.822 179.159 1.00 53.36  ? 2610 ARG A CZ    1 
ATOM   10295 N  NH1   . ARG A 1 2610 ? 163.192 116.951 178.738 1.00 54.17  ? 2610 ARG A NH1   1 
ATOM   10296 N  NH2   . ARG A 1 2610 ? 162.557 119.122 179.083 1.00 53.51  ? 2610 ARG A NH2   1 
ATOM   10297 N  N     . ALA A 1 2611 ? 157.416 111.930 177.363 1.00 52.93  ? 2611 ALA A N     1 
ATOM   10298 C  CA    . ALA A 1 2611 ? 156.738 110.644 177.492 1.00 59.45  ? 2611 ALA A CA    1 
ATOM   10299 C  C     . ALA A 1 2611 ? 157.168 109.681 176.393 1.00 67.53  ? 2611 ALA A C     1 
ATOM   10300 O  O     . ALA A 1 2611 ? 157.249 108.469 176.619 1.00 67.67  ? 2611 ALA A O     1 
ATOM   10301 C  CB    . ALA A 1 2611 ? 155.224 110.844 177.471 1.00 57.55  ? 2611 ALA A CB    1 
ATOM   10302 N  N     . LEU A 1 2612 ? 157.438 110.198 175.201 1.00 66.17  ? 2612 LEU A N     1 
ATOM   10303 C  CA    . LEU A 1 2612 ? 157.905 109.371 174.098 1.00 65.40  ? 2612 LEU A CA    1 
ATOM   10304 C  C     . LEU A 1 2612 ? 159.302 108.842 174.407 1.00 73.75  ? 2612 LEU A C     1 
ATOM   10305 O  O     . LEU A 1 2612 ? 160.201 109.638 174.718 1.00 71.25  ? 2612 LEU A O     1 
ATOM   10306 C  CB    . LEU A 1 2612 ? 157.911 110.175 172.802 1.00 61.13  ? 2612 LEU A CB    1 
ATOM   10307 C  CG    . LEU A 1 2612 ? 156.534 110.543 172.249 1.00 54.56  ? 2612 LEU A CG    1 
ATOM   10308 C  CD1   . LEU A 1 2612 ? 156.659 111.241 170.905 1.00 51.44  ? 2612 LEU A CD1   1 
ATOM   10309 C  CD2   . LEU A 1 2612 ? 155.659 109.309 172.134 1.00 56.91  ? 2612 LEU A CD2   1 
ATOM   10310 N  N     . PRO A 1 2613 ? 159.529 107.528 174.339 1.00 80.61  ? 2613 PRO A N     1 
ATOM   10311 C  CA    . PRO A 1 2613 ? 160.821 106.974 174.771 1.00 77.76  ? 2613 PRO A CA    1 
ATOM   10312 C  C     . PRO A 1 2613 ? 161.995 107.391 173.897 1.00 81.03  ? 2613 PRO A C     1 
ATOM   10313 O  O     . PRO A 1 2613 ? 162.995 107.909 174.402 1.00 83.12  ? 2613 PRO A O     1 
ATOM   10314 C  CB    . PRO A 1 2613 ? 160.587 105.460 174.708 1.00 77.49  ? 2613 PRO A CB    1 
ATOM   10315 C  CG    . PRO A 1 2613 ? 159.498 105.287 173.705 1.00 78.07  ? 2613 PRO A CG    1 
ATOM   10316 C  CD    . PRO A 1 2613 ? 158.609 106.485 173.856 1.00 78.09  ? 2613 PRO A CD    1 
ATOM   10317 N  N     . ASP A 1 2614 ? 161.886 107.172 172.590 1.00 80.86  ? 2614 ASP A N     1 
ATOM   10318 C  CA    . ASP A 1 2614 ? 162.977 107.455 171.658 1.00 76.64  ? 2614 ASP A CA    1 
ATOM   10319 C  C     . ASP A 1 2614 ? 162.896 108.879 171.120 1.00 73.14  ? 2614 ASP A C     1 
ATOM   10320 O  O     . ASP A 1 2614 ? 162.698 109.104 169.928 1.00 74.15  ? 2614 ASP A O     1 
ATOM   10321 C  CB    . ASP A 1 2614 ? 162.960 106.441 170.521 1.00 78.64  ? 2614 ASP A CB    1 
ATOM   10322 C  CG    . ASP A 1 2614 ? 163.334 105.047 170.980 1.00 89.95  ? 2614 ASP A CG    1 
ATOM   10323 O  OD1   . ASP A 1 2614 ? 164.107 104.928 171.953 1.00 90.23  ? 2614 ASP A OD1   1 
ATOM   10324 O  OD2   . ASP A 1 2614 ? 162.855 104.070 170.368 1.00 98.25  ? 2614 ASP A OD2   1 
ATOM   10325 N  N     . MET A 1 2615 ? 163.052 109.859 172.007 1.00 69.02  ? 2615 MET A N     1 
ATOM   10326 C  CA    . MET A 1 2615 ? 162.846 111.254 171.648 1.00 62.66  ? 2615 MET A CA    1 
ATOM   10327 C  C     . MET A 1 2615 ? 163.739 112.127 172.516 1.00 65.50  ? 2615 MET A C     1 
ATOM   10328 O  O     . MET A 1 2615 ? 163.596 112.132 173.741 1.00 71.81  ? 2615 MET A O     1 
ATOM   10329 C  CB    . MET A 1 2615 ? 161.376 111.643 171.838 1.00 62.59  ? 2615 MET A CB    1 
ATOM   10330 C  CG    . MET A 1 2615 ? 161.015 113.034 171.369 1.00 60.67  ? 2615 MET A CG    1 
ATOM   10331 S  SD    . MET A 1 2615 ? 161.232 113.200 169.590 1.00 80.71  ? 2615 MET A SD    1 
ATOM   10332 C  CE    . MET A 1 2615 ? 159.848 112.231 168.999 1.00 57.16  ? 2615 MET A CE    1 
ATOM   10333 N  N     . GLU A 1 2616 ? 164.655 112.859 171.886 1.00 59.38  ? 2616 GLU A N     1 
ATOM   10334 C  CA    . GLU A 1 2616 ? 165.513 113.810 172.583 1.00 55.76  ? 2616 GLU A CA    1 
ATOM   10335 C  C     . GLU A 1 2616 ? 164.918 115.202 172.428 1.00 52.21  ? 2616 GLU A C     1 
ATOM   10336 O  O     . GLU A 1 2616 ? 164.882 115.739 171.319 1.00 54.31  ? 2616 GLU A O     1 
ATOM   10337 C  CB    . GLU A 1 2616 ? 166.937 113.801 172.030 1.00 60.70  ? 2616 GLU A CB    1 
ATOM   10338 C  CG    . GLU A 1 2616 ? 167.684 112.492 172.128 1.00 78.97  ? 2616 GLU A CG    1 
ATOM   10339 C  CD    . GLU A 1 2616 ? 168.770 112.387 171.073 1.00 90.61  ? 2616 GLU A CD    1 
ATOM   10340 O  OE1   . GLU A 1 2616 ? 169.752 113.155 171.155 1.00 96.22  ? 2616 GLU A OE1   1 
ATOM   10341 O  OE2   . GLU A 1 2616 ? 168.641 111.553 170.155 1.00 84.76  ? 2616 GLU A OE2   1 
ATOM   10342 N  N     . VAL A 1 2617 ? 164.484 115.793 173.534 1.00 48.54  ? 2617 VAL A N     1 
ATOM   10343 C  CA    . VAL A 1 2617 ? 163.815 117.088 173.522 1.00 42.31  ? 2617 VAL A CA    1 
ATOM   10344 C  C     . VAL A 1 2617 ? 164.853 118.166 173.793 1.00 46.43  ? 2617 VAL A C     1 
ATOM   10345 O  O     . VAL A 1 2617 ? 165.591 118.090 174.782 1.00 53.09  ? 2617 VAL A O     1 
ATOM   10346 C  CB    . VAL A 1 2617 ? 162.686 117.139 174.560 1.00 47.89  ? 2617 VAL A CB    1 
ATOM   10347 C  CG1   . VAL A 1 2617 ? 161.849 118.391 174.372 1.00 47.32  ? 2617 VAL A CG1   1 
ATOM   10348 C  CG2   . VAL A 1 2617 ? 161.840 115.885 174.475 1.00 46.68  ? 2617 VAL A CG2   1 
ATOM   10349 N  N     . VAL A 1 2618 ? 164.918 119.173 172.924 1.00 43.99  ? 2618 VAL A N     1 
ATOM   10350 C  CA    . VAL A 1 2618 ? 165.842 120.289 173.097 1.00 44.44  ? 2618 VAL A CA    1 
ATOM   10351 C  C     . VAL A 1 2618 ? 165.036 121.578 173.066 1.00 50.18  ? 2618 VAL A C     1 
ATOM   10352 O  O     . VAL A 1 2618 ? 164.420 121.903 172.046 1.00 56.84  ? 2618 VAL A O     1 
ATOM   10353 C  CB    . VAL A 1 2618 ? 166.937 120.308 172.024 1.00 46.48  ? 2618 VAL A CB    1 
ATOM   10354 C  CG1   . VAL A 1 2618 ? 167.802 121.541 172.180 1.00 50.53  ? 2618 VAL A CG1   1 
ATOM   10355 C  CG2   . VAL A 1 2618 ? 167.782 119.061 172.129 1.00 52.39  ? 2618 VAL A CG2   1 
ATOM   10356 N  N     . GLY A 1 2619 ? 165.048 122.316 174.173 1.00 52.40  ? 2619 GLY A N     1 
ATOM   10357 C  CA    . GLY A 1 2619 ? 164.348 123.583 174.245 1.00 48.27  ? 2619 GLY A CA    1 
ATOM   10358 C  C     . GLY A 1 2619 ? 165.160 124.734 173.690 1.00 58.14  ? 2619 GLY A C     1 
ATOM   10359 O  O     . GLY A 1 2619 ? 166.262 125.014 174.169 1.00 64.62  ? 2619 GLY A O     1 
ATOM   10360 N  N     . LEU A 1 2620 ? 164.624 125.410 172.677 1.00 52.21  ? 2620 LEU A N     1 
ATOM   10361 C  CA    . LEU A 1 2620 ? 165.285 126.516 171.992 1.00 55.44  ? 2620 LEU A CA    1 
ATOM   10362 C  C     . LEU A 1 2620 ? 164.357 127.722 172.073 1.00 55.88  ? 2620 LEU A C     1 
ATOM   10363 O  O     . LEU A 1 2620 ? 163.492 127.912 171.215 1.00 57.09  ? 2620 LEU A O     1 
ATOM   10364 C  CB    . LEU A 1 2620 ? 165.599 126.151 170.552 1.00 46.22  ? 2620 LEU A CB    1 
ATOM   10365 C  CG    . LEU A 1 2620 ? 166.474 124.915 170.370 1.00 56.29  ? 2620 LEU A CG    1 
ATOM   10366 C  CD1   . LEU A 1 2620 ? 166.727 124.659 168.898 1.00 58.25  ? 2620 LEU A CD1   1 
ATOM   10367 C  CD2   . LEU A 1 2620 ? 167.779 125.078 171.125 1.00 61.99  ? 2620 LEU A CD2   1 
ATOM   10368 N  N     . ASN A 1 2621 ? 164.538 128.535 173.106 1.00 51.38  ? 2621 ASN A N     1 
ATOM   10369 C  CA    . ASN A 1 2621 ? 163.692 129.704 173.304 1.00 50.74  ? 2621 ASN A CA    1 
ATOM   10370 C  C     . ASN A 1 2621 ? 164.030 130.767 172.267 1.00 50.69  ? 2621 ASN A C     1 
ATOM   10371 O  O     . ASN A 1 2621 ? 165.153 131.280 172.237 1.00 54.72  ? 2621 ASN A O     1 
ATOM   10372 C  CB    . ASN A 1 2621 ? 163.883 130.245 174.714 1.00 59.11  ? 2621 ASN A CB    1 
ATOM   10373 C  CG    . ASN A 1 2621 ? 163.311 129.325 175.766 1.00 71.54  ? 2621 ASN A CG    1 
ATOM   10374 O  OD1   . ASN A 1 2621 ? 162.225 128.777 175.606 1.00 69.10  ? 2621 ASN A OD1   1 
ATOM   10375 N  ND2   . ASN A 1 2621 ? 164.063 129.118 176.835 1.00 79.31  ? 2621 ASN A ND2   1 
ATOM   10376 N  N     . PHE A 1 2622 ? 163.063 131.096 171.419 1.00 47.71  ? 2622 PHE A N     1 
ATOM   10377 C  CA    . PHE A 1 2622 ? 163.261 132.098 170.385 1.00 46.88  ? 2622 PHE A CA    1 
ATOM   10378 C  C     . PHE A 1 2622 ? 162.944 133.490 170.913 1.00 50.71  ? 2622 PHE A C     1 
ATOM   10379 O  O     . PHE A 1 2622 ? 162.127 133.665 171.820 1.00 54.03  ? 2622 PHE A O     1 
ATOM   10380 C  CB    . PHE A 1 2622 ? 162.391 131.809 169.163 1.00 40.19  ? 2622 PHE A CB    1 
ATOM   10381 C  CG    . PHE A 1 2622 ? 162.917 130.720 168.275 1.00 41.56  ? 2622 PHE A CG    1 
ATOM   10382 C  CD1   . PHE A 1 2622 ? 164.020 129.972 168.642 1.00 48.69  ? 2622 PHE A CD1   1 
ATOM   10383 C  CD2   . PHE A 1 2622 ? 162.315 130.461 167.059 1.00 38.87  ? 2622 PHE A CD2   1 
ATOM   10384 C  CE1   . PHE A 1 2622 ? 164.501 128.980 167.819 1.00 49.88  ? 2622 PHE A CE1   1 
ATOM   10385 C  CE2   . PHE A 1 2622 ? 162.792 129.473 166.233 1.00 41.54  ? 2622 PHE A CE2   1 
ATOM   10386 C  CZ    . PHE A 1 2622 ? 163.888 128.733 166.612 1.00 44.35  ? 2622 PHE A CZ    1 
ATOM   10387 N  N     . SER A 1 2623 ? 163.611 134.484 170.332 1.00 49.91  ? 2623 SER A N     1 
ATOM   10388 C  CA    . SER A 1 2623 ? 163.385 135.885 170.646 1.00 48.98  ? 2623 SER A CA    1 
ATOM   10389 C  C     . SER A 1 2623 ? 163.646 136.696 169.385 1.00 51.36  ? 2623 SER A C     1 
ATOM   10390 O  O     . SER A 1 2623 ? 163.957 136.144 168.326 1.00 54.72  ? 2623 SER A O     1 
ATOM   10391 C  CB    . SER A 1 2623 ? 164.270 136.338 171.812 1.00 57.71  ? 2623 SER A CB    1 
ATOM   10392 O  OG    . SER A 1 2623 ? 165.641 136.305 171.460 1.00 63.31  ? 2623 SER A OG    1 
ATOM   10393 N  N     . SER A 1 2624 ? 163.519 138.021 169.492 1.00 52.87  ? 2624 SER A N     1 
ATOM   10394 C  CA    . SER A 1 2624 ? 163.759 138.873 168.332 1.00 54.71  ? 2624 SER A CA    1 
ATOM   10395 C  C     . SER A 1 2624 ? 165.195 138.777 167.837 1.00 60.00  ? 2624 SER A C     1 
ATOM   10396 O  O     . SER A 1 2624 ? 165.457 139.070 166.666 1.00 60.07  ? 2624 SER A O     1 
ATOM   10397 C  CB    . SER A 1 2624 ? 163.422 140.327 168.659 1.00 59.21  ? 2624 SER A CB    1 
ATOM   10398 O  OG    . SER A 1 2624 ? 162.073 140.453 169.069 1.00 67.75  ? 2624 SER A OG    1 
ATOM   10399 N  N     . ALA A 1 2625 ? 166.125 138.368 168.692 1.00 59.05  ? 2625 ALA A N     1 
ATOM   10400 C  CA    . ALA A 1 2625 ? 167.517 138.205 168.303 1.00 58.40  ? 2625 ALA A CA    1 
ATOM   10401 C  C     . ALA A 1 2625 ? 167.816 136.821 167.747 1.00 58.64  ? 2625 ALA A C     1 
ATOM   10402 O  O     . ALA A 1 2625 ? 168.980 136.524 167.461 1.00 62.49  ? 2625 ALA A O     1 
ATOM   10403 C  CB    . ALA A 1 2625 ? 168.434 138.489 169.496 1.00 63.18  ? 2625 ALA A CB    1 
ATOM   10404 N  N     . THR A 1 2626 ? 166.804 135.971 167.592 1.00 53.81  ? 2626 THR A N     1 
ATOM   10405 C  CA    . THR A 1 2626 ? 167.032 134.618 167.103 1.00 54.93  ? 2626 THR A CA    1 
ATOM   10406 C  C     . THR A 1 2626 ? 167.318 134.632 165.607 1.00 57.10  ? 2626 THR A C     1 
ATOM   10407 O  O     . THR A 1 2626 ? 166.605 135.272 164.829 1.00 55.83  ? 2626 THR A O     1 
ATOM   10408 C  CB    . THR A 1 2626 ? 165.825 133.733 167.402 1.00 50.92  ? 2626 THR A CB    1 
ATOM   10409 O  OG1   . THR A 1 2626 ? 165.590 133.710 168.814 1.00 54.04  ? 2626 THR A OG1   1 
ATOM   10410 C  CG2   . THR A 1 2626 ? 166.072 132.317 166.919 1.00 50.99  ? 2626 THR A CG2   1 
ATOM   10411 N  N     . THR A 1 2627 ? 168.368 133.926 165.214 1.00 62.12  ? 2627 THR A N     1 
ATOM   10412 C  CA    . THR A 1 2627 ? 168.805 133.798 163.834 1.00 62.31  ? 2627 THR A CA    1 
ATOM   10413 C  C     . THR A 1 2627 ? 169.131 132.334 163.584 1.00 64.55  ? 2627 THR A C     1 
ATOM   10414 O  O     . THR A 1 2627 ? 169.278 131.560 164.535 1.00 71.73  ? 2627 THR A O     1 
ATOM   10415 C  CB    . THR A 1 2627 ? 170.024 134.688 163.552 1.00 71.64  ? 2627 THR A CB    1 
ATOM   10416 O  OG1   . THR A 1 2627 ? 171.018 134.480 164.563 1.00 69.93  ? 2627 THR A OG1   1 
ATOM   10417 C  CG2   . THR A 1 2627 ? 169.624 136.158 163.525 1.00 70.96  ? 2627 THR A CG2   1 
ATOM   10418 N  N     . PRO A 1 2628 ? 169.227 131.916 162.317 1.00 62.70  ? 2628 PRO A N     1 
ATOM   10419 C  CA    . PRO A 1 2628 ? 169.500 130.495 162.036 1.00 63.85  ? 2628 PRO A CA    1 
ATOM   10420 C  C     . PRO A 1 2628 ? 170.756 129.953 162.700 1.00 67.97  ? 2628 PRO A C     1 
ATOM   10421 O  O     . PRO A 1 2628 ? 170.851 128.735 162.907 1.00 72.50  ? 2628 PRO A O     1 
ATOM   10422 C  CB    . PRO A 1 2628 ? 169.620 130.461 160.508 1.00 58.83  ? 2628 PRO A CB    1 
ATOM   10423 C  CG    . PRO A 1 2628 ? 168.758 131.573 160.054 1.00 60.15  ? 2628 PRO A CG    1 
ATOM   10424 C  CD    . PRO A 1 2628 ? 168.910 132.658 161.083 1.00 60.42  ? 2628 PRO A CD    1 
ATOM   10425 N  N     . GLU A 1 2629 ? 171.722 130.809 163.044 1.00 68.78  ? 2629 GLU A N     1 
ATOM   10426 C  CA    . GLU A 1 2629 ? 172.915 130.326 163.730 1.00 71.78  ? 2629 GLU A CA    1 
ATOM   10427 C  C     . GLU A 1 2629 ? 172.582 129.681 165.070 1.00 70.61  ? 2629 GLU A C     1 
ATOM   10428 O  O     . GLU A 1 2629 ? 173.343 128.836 165.546 1.00 74.71  ? 2629 GLU A O     1 
ATOM   10429 C  CB    . GLU A 1 2629 ? 173.929 131.457 163.909 1.00 78.55  ? 2629 GLU A CB    1 
ATOM   10430 C  CG    . GLU A 1 2629 ? 174.547 131.952 162.605 1.00 86.50  ? 2629 GLU A CG    1 
ATOM   10431 C  CD    . GLU A 1 2629 ? 173.680 132.952 161.872 1.00 85.89  ? 2629 GLU A CD    1 
ATOM   10432 O  OE1   . GLU A 1 2629 ? 172.616 133.320 162.404 1.00 74.75  ? 2629 GLU A OE1   1 
ATOM   10433 O  OE2   . GLU A 1 2629 ? 174.063 133.366 160.757 1.00 91.52  ? 2629 GLU A OE2   1 
ATOM   10434 N  N     . LEU A 1 2630 ? 171.454 130.042 165.685 1.00 65.08  ? 2630 LEU A N     1 
ATOM   10435 C  CA    . LEU A 1 2630 ? 171.014 129.325 166.879 1.00 64.58  ? 2630 LEU A CA    1 
ATOM   10436 C  C     . LEU A 1 2630 ? 170.733 127.862 166.556 1.00 66.06  ? 2630 LEU A C     1 
ATOM   10437 O  O     . LEU A 1 2630 ? 171.158 126.954 167.284 1.00 70.15  ? 2630 LEU A O     1 
ATOM   10438 C  CB    . LEU A 1 2630 ? 169.773 130.001 167.469 1.00 64.76  ? 2630 LEU A CB    1 
ATOM   10439 C  CG    . LEU A 1 2630 ? 169.431 129.794 168.950 1.00 66.74  ? 2630 LEU A CG    1 
ATOM   10440 C  CD1   . LEU A 1 2630 ? 168.449 130.856 169.415 1.00 61.83  ? 2630 LEU A CD1   1 
ATOM   10441 C  CD2   . LEU A 1 2630 ? 168.865 128.410 169.227 1.00 61.71  ? 2630 LEU A CD2   1 
ATOM   10442 N  N     . LEU A 1 2631 ? 170.029 127.613 165.450 1.00 65.02  ? 2631 LEU A N     1 
ATOM   10443 C  CA    . LEU A 1 2631 ? 169.759 126.240 165.040 1.00 63.67  ? 2631 LEU A CA    1 
ATOM   10444 C  C     . LEU A 1 2631 ? 171.041 125.523 164.642 1.00 66.21  ? 2631 LEU A C     1 
ATOM   10445 O  O     . LEU A 1 2631 ? 171.196 124.325 164.904 1.00 68.53  ? 2631 LEU A O     1 
ATOM   10446 C  CB    . LEU A 1 2631 ? 168.752 126.224 163.891 1.00 60.55  ? 2631 LEU A CB    1 
ATOM   10447 C  CG    . LEU A 1 2631 ? 167.323 126.657 164.223 1.00 59.66  ? 2631 LEU A CG    1 
ATOM   10448 C  CD1   . LEU A 1 2631 ? 166.348 126.067 163.226 1.00 48.37  ? 2631 LEU A CD1   1 
ATOM   10449 C  CD2   . LEU A 1 2631 ? 166.945 126.252 165.636 1.00 60.44  ? 2631 LEU A CD2   1 
ATOM   10450 N  N     . LEU A 1 2632 ? 171.971 126.238 164.005 1.00 67.66  ? 2632 LEU A N     1 
ATOM   10451 C  CA    . LEU A 1 2632 ? 173.251 125.625 163.659 1.00 64.69  ? 2632 LEU A CA    1 
ATOM   10452 C  C     . LEU A 1 2632 ? 174.037 125.235 164.907 1.00 68.58  ? 2632 LEU A C     1 
ATOM   10453 O  O     . LEU A 1 2632 ? 174.655 124.166 164.949 1.00 71.86  ? 2632 LEU A O     1 
ATOM   10454 C  CB    . LEU A 1 2632 ? 174.074 126.563 162.775 1.00 65.09  ? 2632 LEU A CB    1 
ATOM   10455 C  CG    . LEU A 1 2632 ? 173.828 126.522 161.262 1.00 62.38  ? 2632 LEU A CG    1 
ATOM   10456 C  CD1   . LEU A 1 2632 ? 174.192 125.153 160.707 1.00 66.98  ? 2632 LEU A CD1   1 
ATOM   10457 C  CD2   . LEU A 1 2632 ? 172.407 126.888 160.890 1.00 58.41  ? 2632 LEU A CD2   1 
ATOM   10458 N  N     . LYS A 1 2633 ? 174.030 126.091 165.931 1.00 67.97  ? 2633 LYS A N     1 
ATOM   10459 C  CA    . LYS A 1 2633 ? 174.678 125.749 167.194 1.00 67.62  ? 2633 LYS A CA    1 
ATOM   10460 C  C     . LYS A 1 2633 ? 174.012 124.546 167.846 1.00 67.98  ? 2633 LYS A C     1 
ATOM   10461 O  O     . LYS A 1 2633 ? 174.692 123.678 168.406 1.00 72.49  ? 2633 LYS A O     1 
ATOM   10462 C  CB    . LYS A 1 2633 ? 174.656 126.946 168.142 1.00 69.46  ? 2633 LYS A CB    1 
ATOM   10463 C  CG    . LYS A 1 2633 ? 175.492 128.130 167.685 1.00 70.07  ? 2633 LYS A CG    1 
ATOM   10464 C  CD    . LYS A 1 2633 ? 175.179 129.390 168.488 1.00 72.66  ? 2633 LYS A CD    1 
ATOM   10465 C  CE    . LYS A 1 2633 ? 174.509 129.073 169.818 1.00 72.86  ? 2633 LYS A CE    1 
ATOM   10466 N  NZ    . LYS A 1 2633 ? 174.332 130.290 170.654 1.00 76.16  ? 2633 LYS A NZ    1 
ATOM   10467 N  N     . THR A 1 2634 ? 172.681 124.482 167.794 1.00 66.48  ? 2634 THR A N     1 
ATOM   10468 C  CA    . THR A 1 2634 ? 171.982 123.325 168.346 1.00 67.36  ? 2634 THR A CA    1 
ATOM   10469 C  C     . THR A 1 2634 ? 172.369 122.045 167.612 1.00 67.73  ? 2634 THR A C     1 
ATOM   10470 O  O     . THR A 1 2634 ? 172.582 121.000 168.238 1.00 69.47  ? 2634 THR A O     1 
ATOM   10471 C  CB    . THR A 1 2634 ? 170.472 123.542 168.282 1.00 64.23  ? 2634 THR A CB    1 
ATOM   10472 O  OG1   . THR A 1 2634 ? 170.140 124.778 168.926 1.00 63.54  ? 2634 THR A OG1   1 
ATOM   10473 C  CG2   . THR A 1 2634 ? 169.748 122.409 168.983 1.00 60.53  ? 2634 THR A CG2   1 
ATOM   10474 N  N     . PHE A 1 2635 ? 172.460 122.109 166.281 1.00 65.43  ? 2635 PHE A N     1 
ATOM   10475 C  CA    . PHE A 1 2635 ? 172.873 120.942 165.507 1.00 65.43  ? 2635 PHE A CA    1 
ATOM   10476 C  C     . PHE A 1 2635 ? 174.308 120.543 165.826 1.00 72.95  ? 2635 PHE A C     1 
ATOM   10477 O  O     . PHE A 1 2635 ? 174.620 119.351 165.915 1.00 74.27  ? 2635 PHE A O     1 
ATOM   10478 C  CB    . PHE A 1 2635 ? 172.714 121.215 164.012 1.00 59.27  ? 2635 PHE A CB    1 
ATOM   10479 C  CG    . PHE A 1 2635 ? 171.292 121.423 163.582 1.00 59.98  ? 2635 PHE A CG    1 
ATOM   10480 C  CD1   . PHE A 1 2635 ? 170.256 120.794 164.249 1.00 58.94  ? 2635 PHE A CD1   1 
ATOM   10481 C  CD2   . PHE A 1 2635 ? 170.993 122.237 162.506 1.00 59.58  ? 2635 PHE A CD2   1 
ATOM   10482 C  CE1   . PHE A 1 2635 ? 168.950 120.979 163.855 1.00 51.78  ? 2635 PHE A CE1   1 
ATOM   10483 C  CE2   . PHE A 1 2635 ? 169.686 122.426 162.109 1.00 56.02  ? 2635 PHE A CE2   1 
ATOM   10484 C  CZ    . PHE A 1 2635 ? 168.663 121.796 162.785 1.00 53.84  ? 2635 PHE A CZ    1 
ATOM   10485 N  N     . ASP A 1 2636 ? 175.197 121.525 165.989 1.00 74.47  ? 2636 ASP A N     1 
ATOM   10486 C  CA    . ASP A 1 2636 ? 176.572 121.219 166.367 1.00 74.47  ? 2636 ASP A CA    1 
ATOM   10487 C  C     . ASP A 1 2636 ? 176.638 120.562 167.738 1.00 74.97  ? 2636 ASP A C     1 
ATOM   10488 O  O     . ASP A 1 2636 ? 177.451 119.657 167.955 1.00 76.88  ? 2636 ASP A O     1 
ATOM   10489 C  CB    . ASP A 1 2636 ? 177.420 122.491 166.350 1.00 74.72  ? 2636 ASP A CB    1 
ATOM   10490 C  CG    . ASP A 1 2636 ? 177.938 122.829 164.966 1.00 81.23  ? 2636 ASP A CG    1 
ATOM   10491 O  OD1   . ASP A 1 2636 ? 177.402 123.766 164.339 1.00 83.00  ? 2636 ASP A OD1   1 
ATOM   10492 O  OD2   . ASP A 1 2636 ? 178.885 122.157 164.504 1.00 84.12  ? 2636 ASP A OD2   1 
ATOM   10493 N  N     . HIS A 1 2637 ? 175.795 121.003 168.671 1.00 73.28  ? 2637 HIS A N     1 
ATOM   10494 C  CA    . HIS A 1 2637 ? 175.832 120.465 170.024 1.00 72.79  ? 2637 HIS A CA    1 
ATOM   10495 C  C     . HIS A 1 2637 ? 175.245 119.059 170.096 1.00 70.62  ? 2637 HIS A C     1 
ATOM   10496 O  O     . HIS A 1 2637 ? 175.814 118.184 170.756 1.00 72.96  ? 2637 HIS A O     1 
ATOM   10497 C  CB    . HIS A 1 2637 ? 175.089 121.407 170.974 1.00 69.84  ? 2637 HIS A CB    1 
ATOM   10498 C  CG    . HIS A 1 2637 ? 175.233 121.051 172.421 1.00 76.11  ? 2637 HIS A CG    1 
ATOM   10499 N  ND1   . HIS A 1 2637 ? 174.541 121.705 173.418 1.00 79.72  ? 2637 HIS A ND1   1 
ATOM   10500 C  CD2   . HIS A 1 2637 ? 175.991 120.116 173.041 1.00 77.97  ? 2637 HIS A CD2   1 
ATOM   10501 C  CE1   . HIS A 1 2637 ? 174.864 121.186 174.589 1.00 82.43  ? 2637 HIS A CE1   1 
ATOM   10502 N  NE2   . HIS A 1 2637 ? 175.741 120.219 174.388 1.00 84.52  ? 2637 HIS A NE2   1 
ATOM   10503 N  N     . TYR A 1 2638 ? 174.121 118.813 169.420 1.00 69.08  ? 2638 TYR A N     1 
ATOM   10504 C  CA    . TYR A 1 2638 ? 173.400 117.558 169.586 1.00 66.01  ? 2638 TYR A CA    1 
ATOM   10505 C  C     . TYR A 1 2638 ? 173.517 116.600 168.409 1.00 69.29  ? 2638 TYR A C     1 
ATOM   10506 O  O     . TYR A 1 2638 ? 173.160 115.427 168.559 1.00 70.95  ? 2638 TYR A O     1 
ATOM   10507 C  CB    . TYR A 1 2638 ? 171.911 117.828 169.855 1.00 63.99  ? 2638 TYR A CB    1 
ATOM   10508 C  CG    . TYR A 1 2638 ? 171.638 118.590 171.130 1.00 64.85  ? 2638 TYR A CG    1 
ATOM   10509 C  CD1   . TYR A 1 2638 ? 171.742 119.973 171.173 1.00 65.98  ? 2638 TYR A CD1   1 
ATOM   10510 C  CD2   . TYR A 1 2638 ? 171.280 117.924 172.293 1.00 66.66  ? 2638 TYR A CD2   1 
ATOM   10511 C  CE1   . TYR A 1 2638 ? 171.494 120.671 172.337 1.00 66.71  ? 2638 TYR A CE1   1 
ATOM   10512 C  CE2   . TYR A 1 2638 ? 171.032 118.614 173.463 1.00 68.50  ? 2638 TYR A CE2   1 
ATOM   10513 C  CZ    . TYR A 1 2638 ? 171.140 119.987 173.479 1.00 68.56  ? 2638 TYR A CZ    1 
ATOM   10514 O  OH    . TYR A 1 2638 ? 170.893 120.680 174.641 1.00 69.72  ? 2638 TYR A OH    1 
ATOM   10515 N  N     . CYS A 1 2639 ? 174.001 117.049 167.254 1.00 72.59  ? 2639 CYS A N     1 
ATOM   10516 C  CA    . CYS A 1 2639 ? 174.046 116.210 166.065 1.00 71.37  ? 2639 CYS A CA    1 
ATOM   10517 C  C     . CYS A 1 2639 ? 175.453 116.188 165.486 1.00 70.02  ? 2639 CYS A C     1 
ATOM   10518 O  O     . CYS A 1 2639 ? 176.349 116.914 165.924 1.00 73.88  ? 2639 CYS A O     1 
ATOM   10519 C  CB    . CYS A 1 2639 ? 173.055 116.693 164.999 1.00 66.96  ? 2639 CYS A CB    1 
ATOM   10520 S  SG    . CYS A 1 2639 ? 171.412 117.079 165.617 1.00 67.14  ? 2639 CYS A SG    1 
ATOM   10521 N  N     . GLU A 1 2640 ? 175.631 115.333 164.481 1.00 67.08  ? 2640 GLU A N     1 
ATOM   10522 C  CA    . GLU A 1 2640 ? 176.889 115.195 163.768 1.00 71.96  ? 2640 GLU A CA    1 
ATOM   10523 C  C     . GLU A 1 2640 ? 176.612 115.092 162.276 1.00 69.80  ? 2640 GLU A C     1 
ATOM   10524 O  O     . GLU A 1 2640 ? 175.544 114.633 161.854 1.00 69.56  ? 2640 GLU A O     1 
ATOM   10525 C  CB    . GLU A 1 2640 ? 177.674 113.961 164.228 1.00 78.26  ? 2640 GLU A CB    1 
ATOM   10526 C  CG    . GLU A 1 2640 ? 176.993 112.644 163.894 1.00 83.54  ? 2640 GLU A CG    1 
ATOM   10527 C  CD    . GLU A 1 2640 ? 177.761 111.441 164.401 1.00 97.68  ? 2640 GLU A CD    1 
ATOM   10528 O  OE1   . GLU A 1 2640 ? 178.819 111.633 165.035 1.00 101.15 ? 2640 GLU A OE1   1 
ATOM   10529 O  OE2   . GLU A 1 2640 ? 177.306 110.303 164.162 1.00 102.33 ? 2640 GLU A OE2   1 
ATOM   10530 N  N     . TYR A 1 2641 ? 177.593 115.517 161.484 1.00 67.18  ? 2641 TYR A N     1 
ATOM   10531 C  CA    . TYR A 1 2641 ? 177.549 115.403 160.033 1.00 63.27  ? 2641 TYR A CA    1 
ATOM   10532 C  C     . TYR A 1 2641 ? 178.348 114.174 159.618 1.00 66.90  ? 2641 TYR A C     1 
ATOM   10533 O  O     . TYR A 1 2641 ? 179.494 114.002 160.044 1.00 74.01  ? 2641 TYR A O     1 
ATOM   10534 C  CB    . TYR A 1 2641 ? 178.113 116.652 159.355 1.00 59.62  ? 2641 TYR A CB    1 
ATOM   10535 C  CG    . TYR A 1 2641 ? 177.463 117.957 159.756 1.00 61.14  ? 2641 TYR A CG    1 
ATOM   10536 C  CD1   . TYR A 1 2641 ? 177.767 118.568 160.965 1.00 68.31  ? 2641 TYR A CD1   1 
ATOM   10537 C  CD2   . TYR A 1 2641 ? 176.557 118.587 158.916 1.00 61.14  ? 2641 TYR A CD2   1 
ATOM   10538 C  CE1   . TYR A 1 2641 ? 177.180 119.764 161.328 1.00 68.75  ? 2641 TYR A CE1   1 
ATOM   10539 C  CE2   . TYR A 1 2641 ? 175.965 119.783 159.271 1.00 61.86  ? 2641 TYR A CE2   1 
ATOM   10540 C  CZ    . TYR A 1 2641 ? 176.280 120.367 160.478 1.00 63.63  ? 2641 TYR A CZ    1 
ATOM   10541 O  OH    . TYR A 1 2641 ? 175.693 121.558 160.836 1.00 66.80  ? 2641 TYR A OH    1 
ATOM   10542 N  N     . ARG A 1 2642 ? 177.744 113.327 158.792 1.00 66.94  ? 2642 ARG A N     1 
ATOM   10543 C  CA    . ARG A 1 2642 ? 178.380 112.121 158.286 1.00 76.11  ? 2642 ARG A CA    1 
ATOM   10544 C  C     . ARG A 1 2642 ? 178.321 112.120 156.766 1.00 80.93  ? 2642 ARG A C     1 
ATOM   10545 O  O     . ARG A 1 2642 ? 177.285 112.439 156.177 1.00 80.24  ? 2642 ARG A O     1 
ATOM   10546 C  CB    . ARG A 1 2642 ? 177.701 110.870 158.843 1.00 81.04  ? 2642 ARG A CB    1 
ATOM   10547 C  CG    . ARG A 1 2642 ? 178.377 109.566 158.468 1.00 93.94  ? 2642 ARG A CG    1 
ATOM   10548 C  CD    . ARG A 1 2642 ? 177.671 108.396 159.124 1.00 101.26 ? 2642 ARG A CD    1 
ATOM   10549 N  NE    . ARG A 1 2642 ? 176.308 108.250 158.629 1.00 107.30 ? 2642 ARG A NE    1 
ATOM   10550 C  CZ    . ARG A 1 2642 ? 175.220 108.440 159.364 1.00 104.34 ? 2642 ARG A CZ    1 
ATOM   10551 N  NH1   . ARG A 1 2642 ? 175.299 108.792 160.637 1.00 100.03 ? 2642 ARG A NH1   1 
ATOM   10552 N  NH2   . ARG A 1 2642 ? 174.024 108.274 158.807 1.00 102.23 ? 2642 ARG A NH2   1 
ATOM   10553 N  N     . ARG A 1 2643 ? 179.434 111.758 156.131 1.00 85.27  ? 2643 ARG A N     1 
ATOM   10554 C  CA    . ARG A 1 2643 ? 179.531 111.784 154.672 1.00 85.24  ? 2643 ARG A CA    1 
ATOM   10555 C  C     . ARG A 1 2643 ? 179.108 110.424 154.135 1.00 89.67  ? 2643 ARG A C     1 
ATOM   10556 O  O     . ARG A 1 2643 ? 179.933 109.558 153.842 1.00 94.47  ? 2643 ARG A O     1 
ATOM   10557 C  CB    . ARG A 1 2643 ? 180.940 112.158 154.231 1.00 85.78  ? 2643 ARG A CB    1 
ATOM   10558 C  CG    . ARG A 1 2643 ? 181.110 112.262 152.725 1.00 84.19  ? 2643 ARG A CG    1 
ATOM   10559 C  CD    . ARG A 1 2643 ? 180.282 113.402 152.164 1.00 85.35  ? 2643 ARG A CD    1 
ATOM   10560 N  NE    . ARG A 1 2643 ? 180.659 114.686 152.741 1.00 90.77  ? 2643 ARG A NE    1 
ATOM   10561 C  CZ    . ARG A 1 2643 ? 181.660 115.440 152.307 1.00 91.26  ? 2643 ARG A CZ    1 
ATOM   10562 N  NH1   . ARG A 1 2643 ? 182.407 115.073 151.279 1.00 98.26  ? 2643 ARG A NH1   1 
ATOM   10563 N  NH2   . ARG A 1 2643 ? 181.914 116.594 152.917 1.00 84.23  ? 2643 ARG A NH2   1 
ATOM   10564 N  N     . THR A 1 2644 ? 177.798 110.233 154.014 1.00 89.75  ? 2644 THR A N     1 
ATOM   10565 C  CA    . THR A 1 2644 ? 177.266 109.033 153.397 1.00 92.91  ? 2644 THR A CA    1 
ATOM   10566 C  C     . THR A 1 2644 ? 177.486 109.089 151.886 1.00 97.38  ? 2644 THR A C     1 
ATOM   10567 O  O     . THR A 1 2644 ? 177.727 110.161 151.326 1.00 100.27 ? 2644 THR A O     1 
ATOM   10568 C  CB    . THR A 1 2644 ? 175.779 108.890 153.714 1.00 93.07  ? 2644 THR A CB    1 
ATOM   10569 O  OG1   . THR A 1 2644 ? 175.131 110.159 153.568 1.00 89.58  ? 2644 THR A OG1   1 
ATOM   10570 C  CG2   . THR A 1 2644 ? 175.587 108.391 155.137 1.00 91.16  ? 2644 THR A CG2   1 
ATOM   10571 N  N     . PRO A 1 2645 ? 177.434 107.939 151.203 1.00 97.08  ? 2645 PRO A N     1 
ATOM   10572 C  CA    . PRO A 1 2645 ? 177.574 107.964 149.738 1.00 98.82  ? 2645 PRO A CA    1 
ATOM   10573 C  C     . PRO A 1 2645 ? 176.540 108.836 149.049 1.00 101.86 ? 2645 PRO A C     1 
ATOM   10574 O  O     . PRO A 1 2645 ? 176.847 109.451 148.020 1.00 100.11 ? 2645 PRO A O     1 
ATOM   10575 C  CB    . PRO A 1 2645 ? 177.424 106.486 149.343 1.00 100.88 ? 2645 PRO A CB    1 
ATOM   10576 C  CG    . PRO A 1 2645 ? 176.813 105.817 150.539 1.00 98.30  ? 2645 PRO A CG    1 
ATOM   10577 C  CD    . PRO A 1 2645 ? 177.345 106.562 151.715 1.00 95.69  ? 2645 PRO A CD    1 
ATOM   10578 N  N     . ASN A 1 2646 ? 175.318 108.904 149.582 1.00 102.60 ? 2646 ASN A N     1 
ATOM   10579 C  CA    . ASN A 1 2646 ? 174.317 109.807 149.023 1.00 100.46 ? 2646 ASN A CA    1 
ATOM   10580 C  C     . ASN A 1 2646 ? 174.716 111.264 149.220 1.00 94.81  ? 2646 ASN A C     1 
ATOM   10581 O  O     . ASN A 1 2646 ? 174.514 112.095 148.327 1.00 96.60  ? 2646 ASN A O     1 
ATOM   10582 C  CB    . ASN A 1 2646 ? 172.954 109.530 149.655 1.00 101.96 ? 2646 ASN A CB    1 
ATOM   10583 C  CG    . ASN A 1 2646 ? 172.400 108.173 149.270 1.00 108.09 ? 2646 ASN A CG    1 
ATOM   10584 O  OD1   . ASN A 1 2646 ? 173.003 107.445 148.482 1.00 105.51 ? 2646 ASN A OD1   1 
ATOM   10585 N  ND2   . ASN A 1 2646 ? 171.246 107.824 149.827 1.00 111.52 ? 2646 ASN A ND2   1 
ATOM   10586 N  N     . GLY A 1 2647 ? 175.279 111.593 150.373 1.00 88.63  ? 2647 GLY A N     1 
ATOM   10587 C  CA    . GLY A 1 2647 ? 175.694 112.951 150.649 1.00 81.94  ? 2647 GLY A CA    1 
ATOM   10588 C  C     . GLY A 1 2647 ? 175.832 113.170 152.142 1.00 81.39  ? 2647 GLY A C     1 
ATOM   10589 O  O     . GLY A 1 2647 ? 175.760 112.234 152.937 1.00 86.52  ? 2647 GLY A O     1 
ATOM   10590 N  N     . VAL A 1 2648 ? 176.032 114.437 152.502 1.00 75.38  ? 2648 VAL A N     1 
ATOM   10591 C  CA    . VAL A 1 2648 ? 176.171 114.803 153.906 1.00 70.07  ? 2648 VAL A CA    1 
ATOM   10592 C  C     . VAL A 1 2648 ? 174.833 114.625 154.608 1.00 66.96  ? 2648 VAL A C     1 
ATOM   10593 O  O     . VAL A 1 2648 ? 173.795 115.103 154.132 1.00 70.56  ? 2648 VAL A O     1 
ATOM   10594 C  CB    . VAL A 1 2648 ? 176.675 116.246 154.042 1.00 63.25  ? 2648 VAL A CB    1 
ATOM   10595 C  CG1   . VAL A 1 2648 ? 176.913 116.586 155.502 1.00 57.02  ? 2648 VAL A CG1   1 
ATOM   10596 C  CG2   . VAL A 1 2648 ? 177.936 116.446 153.227 1.00 71.42  ? 2648 VAL A CG2   1 
ATOM   10597 N  N     . VAL A 1 2649 ? 174.850 113.939 155.747 1.00 59.93  ? 2649 VAL A N     1 
ATOM   10598 C  CA    . VAL A 1 2649 ? 173.655 113.692 156.541 1.00 52.29  ? 2649 VAL A CA    1 
ATOM   10599 C  C     . VAL A 1 2649 ? 173.907 114.198 157.952 1.00 54.97  ? 2649 VAL A C     1 
ATOM   10600 O  O     . VAL A 1 2649 ? 174.911 113.838 158.574 1.00 69.64  ? 2649 VAL A O     1 
ATOM   10601 C  CB    . VAL A 1 2649 ? 173.284 112.197 156.560 1.00 55.90  ? 2649 VAL A CB    1 
ATOM   10602 C  CG1   . VAL A 1 2649 ? 172.318 111.902 157.689 1.00 58.15  ? 2649 VAL A CG1   1 
ATOM   10603 C  CG2   . VAL A 1 2649 ? 172.693 111.784 155.227 1.00 62.60  ? 2649 VAL A CG2   1 
ATOM   10604 N  N     . LEU A 1 2650 ? 173.003 115.033 158.453 1.00 51.78  ? 2650 LEU A N     1 
ATOM   10605 C  CA    . LEU A 1 2650 ? 173.074 115.545 159.816 1.00 54.32  ? 2650 LEU A CA    1 
ATOM   10606 C  C     . LEU A 1 2650 ? 172.123 114.729 160.680 1.00 57.06  ? 2650 LEU A C     1 
ATOM   10607 O  O     . LEU A 1 2650 ? 170.902 114.796 160.503 1.00 56.21  ? 2650 LEU A O     1 
ATOM   10608 C  CB    . LEU A 1 2650 ? 172.725 117.029 159.863 1.00 47.34  ? 2650 LEU A CB    1 
ATOM   10609 C  CG    . LEU A 1 2650 ? 172.727 117.668 161.249 1.00 49.98  ? 2650 LEU A CG    1 
ATOM   10610 C  CD1   . LEU A 1 2650 ? 174.148 117.870 161.731 1.00 60.58  ? 2650 LEU A CD1   1 
ATOM   10611 C  CD2   . LEU A 1 2650 ? 171.986 118.985 161.217 1.00 56.10  ? 2650 LEU A CD2   1 
ATOM   10612 N  N     . ALA A 1 2651 ? 172.679 113.963 161.612 1.00 56.56  ? 2651 ALA A N     1 
ATOM   10613 C  CA    . ALA A 1 2651 ? 171.877 113.071 162.434 1.00 57.50  ? 2651 ALA A CA    1 
ATOM   10614 C  C     . ALA A 1 2651 ? 172.300 113.169 163.890 1.00 71.34  ? 2651 ALA A C     1 
ATOM   10615 O  O     . ALA A 1 2651 ? 173.454 113.490 164.183 1.00 78.15  ? 2651 ALA A O     1 
ATOM   10616 C  CB    . ALA A 1 2651 ? 172.007 111.618 161.958 1.00 59.83  ? 2651 ALA A CB    1 
ATOM   10617 N  N     . PRO A 1 2652 ? 171.388 112.899 164.825 1.00 68.09  ? 2652 PRO A N     1 
ATOM   10618 C  CA    . PRO A 1 2652 ? 171.758 112.941 166.244 1.00 68.82  ? 2652 PRO A CA    1 
ATOM   10619 C  C     . PRO A 1 2652 ? 172.840 111.923 166.569 1.00 77.96  ? 2652 PRO A C     1 
ATOM   10620 O  O     . PRO A 1 2652 ? 172.924 110.855 165.961 1.00 79.52  ? 2652 PRO A O     1 
ATOM   10621 C  CB    . PRO A 1 2652 ? 170.445 112.611 166.963 1.00 63.59  ? 2652 PRO A CB    1 
ATOM   10622 C  CG    . PRO A 1 2652 ? 169.382 112.965 165.989 1.00 56.88  ? 2652 PRO A CG    1 
ATOM   10623 C  CD    . PRO A 1 2652 ? 169.949 112.651 164.642 1.00 57.08  ? 2652 PRO A CD    1 
ATOM   10624 N  N     . VAL A 1 2653 ? 173.683 112.276 167.542 1.00 79.26  ? 2653 VAL A N     1 
ATOM   10625 C  CA    . VAL A 1 2653 ? 174.781 111.395 167.929 1.00 80.42  ? 2653 VAL A CA    1 
ATOM   10626 C  C     . VAL A 1 2653 ? 174.244 110.101 168.530 1.00 80.17  ? 2653 VAL A C     1 
ATOM   10627 O  O     . VAL A 1 2653 ? 174.824 109.025 168.339 1.00 85.22  ? 2653 VAL A O     1 
ATOM   10628 C  CB    . VAL A 1 2653 ? 175.739 112.120 168.893 1.00 84.66  ? 2653 VAL A CB    1 
ATOM   10629 C  CG1   . VAL A 1 2653 ? 176.466 113.239 168.167 1.00 84.48  ? 2653 VAL A CG1   1 
ATOM   10630 C  CG2   . VAL A 1 2653 ? 174.982 112.675 170.089 1.00 81.89  ? 2653 VAL A CG2   1 
ATOM   10631 N  N     . GLN A 1 2654 ? 173.134 110.181 169.259 1.00 80.83  ? 2654 GLN A N     1 
ATOM   10632 C  CA    . GLN A 1 2654 ? 172.532 108.998 169.860 1.00 82.28  ? 2654 GLN A CA    1 
ATOM   10633 C  C     . GLN A 1 2654 ? 171.700 108.268 168.813 1.00 80.81  ? 2654 GLN A C     1 
ATOM   10634 O  O     . GLN A 1 2654 ? 170.709 108.809 168.311 1.00 81.48  ? 2654 GLN A O     1 
ATOM   10635 C  CB    . GLN A 1 2654 ? 171.675 109.389 171.061 1.00 84.72  ? 2654 GLN A CB    1 
ATOM   10636 C  CG    . GLN A 1 2654 ? 172.474 109.949 172.224 1.00 94.24  ? 2654 GLN A CG    1 
ATOM   10637 C  CD    . GLN A 1 2654 ? 171.602 110.345 173.399 1.00 100.71 ? 2654 GLN A CD    1 
ATOM   10638 O  OE1   . GLN A 1 2654 ? 170.376 110.265 173.333 1.00 90.90  ? 2654 GLN A OE1   1 
ATOM   10639 N  NE2   . GLN A 1 2654 ? 172.234 110.777 174.484 1.00 104.22 ? 2654 GLN A NE2   1 
ATOM   10640 N  N     . LEU A 1 2655 ? 172.100 107.043 168.486 1.00 78.07  ? 2655 LEU A N     1 
ATOM   10641 C  CA    . LEU A 1 2655 ? 171.421 106.287 167.445 1.00 79.03  ? 2655 LEU A CA    1 
ATOM   10642 C  C     . LEU A 1 2655 ? 170.055 105.807 167.923 1.00 80.30  ? 2655 LEU A C     1 
ATOM   10643 O  O     . LEU A 1 2655 ? 169.814 105.630 169.120 1.00 82.84  ? 2655 LEU A O     1 
ATOM   10644 C  CB    . LEU A 1 2655 ? 172.270 105.092 167.010 1.00 82.46  ? 2655 LEU A CB    1 
ATOM   10645 C  CG    . LEU A 1 2655 ? 173.119 105.268 165.749 1.00 82.66  ? 2655 LEU A CG    1 
ATOM   10646 C  CD1   . LEU A 1 2655 ? 174.065 106.451 165.885 1.00 78.21  ? 2655 LEU A CD1   1 
ATOM   10647 C  CD2   . LEU A 1 2655 ? 173.890 103.995 165.439 1.00 79.69  ? 2655 LEU A CD2   1 
ATOM   10648 N  N     . GLY A 1 2656 ? 169.156 105.597 166.965 1.00 76.59  ? 2656 GLY A N     1 
ATOM   10649 C  CA    . GLY A 1 2656 ? 167.821 105.114 167.274 1.00 75.67  ? 2656 GLY A CA    1 
ATOM   10650 C  C     . GLY A 1 2656 ? 166.991 106.068 168.101 1.00 79.86  ? 2656 GLY A C     1 
ATOM   10651 O  O     . GLY A 1 2656 ? 166.160 105.626 168.901 1.00 82.09  ? 2656 GLY A O     1 
ATOM   10652 N  N     . LYS A 1 2657 ? 167.191 107.372 167.928 1.00 75.38  ? 2657 LYS A N     1 
ATOM   10653 C  CA    . LYS A 1 2657 ? 166.441 108.382 168.658 1.00 70.09  ? 2657 LYS A CA    1 
ATOM   10654 C  C     . LYS A 1 2657 ? 166.185 109.569 167.744 1.00 62.72  ? 2657 LYS A C     1 
ATOM   10655 O  O     . LYS A 1 2657 ? 167.062 109.967 166.973 1.00 69.01  ? 2657 LYS A O     1 
ATOM   10656 C  CB    . LYS A 1 2657 ? 167.191 108.840 169.914 1.00 73.96  ? 2657 LYS A CB    1 
ATOM   10657 C  CG    . LYS A 1 2657 ? 167.121 107.872 171.082 1.00 82.40  ? 2657 LYS A CG    1 
ATOM   10658 C  CD    . LYS A 1 2657 ? 166.984 108.612 172.401 1.00 82.71  ? 2657 LYS A CD    1 
ATOM   10659 C  CE    . LYS A 1 2657 ? 166.950 107.647 173.574 1.00 76.37  ? 2657 LYS A CE    1 
ATOM   10660 N  NZ    . LYS A 1 2657 ? 165.560 107.362 174.023 1.00 68.16  ? 2657 LYS A NZ    1 
ATOM   10661 N  N     . TRP A 1 2658 ? 164.986 110.134 167.839 1.00 60.73  ? 2658 TRP A N     1 
ATOM   10662 C  CA    . TRP A 1 2658 ? 164.596 111.288 167.041 1.00 53.14  ? 2658 TRP A CA    1 
ATOM   10663 C  C     . TRP A 1 2658 ? 164.797 112.548 167.871 1.00 51.48  ? 2658 TRP A C     1 
ATOM   10664 O  O     . TRP A 1 2658 ? 164.349 112.616 169.019 1.00 59.46  ? 2658 TRP A O     1 
ATOM   10665 C  CB    . TRP A 1 2658 ? 163.143 111.170 166.584 1.00 49.41  ? 2658 TRP A CB    1 
ATOM   10666 C  CG    . TRP A 1 2658 ? 162.978 110.365 165.337 1.00 53.88  ? 2658 TRP A CG    1 
ATOM   10667 C  CD1   . TRP A 1 2658 ? 163.060 109.010 165.221 1.00 55.75  ? 2658 TRP A CD1   1 
ATOM   10668 C  CD2   . TRP A 1 2658 ? 162.716 110.865 164.021 1.00 52.91  ? 2658 TRP A CD2   1 
ATOM   10669 N  NE1   . TRP A 1 2658 ? 162.859 108.634 163.917 1.00 58.04  ? 2658 TRP A NE1   1 
ATOM   10670 C  CE2   . TRP A 1 2658 ? 162.647 109.755 163.160 1.00 58.06  ? 2658 TRP A CE2   1 
ATOM   10671 C  CE3   . TRP A 1 2658 ? 162.530 112.143 163.489 1.00 50.27  ? 2658 TRP A CE3   1 
ATOM   10672 C  CZ2   . TRP A 1 2658 ? 162.400 109.884 161.796 1.00 61.64  ? 2658 TRP A CZ2   1 
ATOM   10673 C  CZ3   . TRP A 1 2658 ? 162.287 112.269 162.136 1.00 52.23  ? 2658 TRP A CZ3   1 
ATOM   10674 C  CH2   . TRP A 1 2658 ? 162.224 111.147 161.304 1.00 58.57  ? 2658 TRP A CH2   1 
ATOM   10675 N  N     . LEU A 1 2659 ? 165.475 113.534 167.297 1.00 44.65  ? 2659 LEU A N     1 
ATOM   10676 C  CA    . LEU A 1 2659 ? 165.714 114.800 167.976 1.00 40.19  ? 2659 LEU A CA    1 
ATOM   10677 C  C     . LEU A 1 2659 ? 164.583 115.763 167.644 1.00 40.07  ? 2659 LEU A C     1 
ATOM   10678 O  O     . LEU A 1 2659 ? 164.332 116.049 166.469 1.00 47.93  ? 2659 LEU A O     1 
ATOM   10679 C  CB    . LEU A 1 2659 ? 167.055 115.398 167.559 1.00 42.42  ? 2659 LEU A CB    1 
ATOM   10680 C  CG    . LEU A 1 2659 ? 167.413 116.704 168.269 1.00 43.28  ? 2659 LEU A CG    1 
ATOM   10681 C  CD1   . LEU A 1 2659 ? 167.636 116.447 169.739 1.00 48.11  ? 2659 LEU A CD1   1 
ATOM   10682 C  CD2   . LEU A 1 2659 ? 168.627 117.355 167.650 1.00 45.15  ? 2659 LEU A CD2   1 
ATOM   10683 N  N     . VAL A 1 2660 ? 163.904 116.263 168.670 1.00 41.26  ? 2660 VAL A N     1 
ATOM   10684 C  CA    . VAL A 1 2660 ? 162.856 117.261 168.514 1.00 40.92  ? 2660 VAL A CA    1 
ATOM   10685 C  C     . VAL A 1 2660 ? 163.366 118.578 169.080 1.00 40.09  ? 2660 VAL A C     1 
ATOM   10686 O  O     . VAL A 1 2660 ? 163.903 118.623 170.197 1.00 46.55  ? 2660 VAL A O     1 
ATOM   10687 C  CB    . VAL A 1 2660 ? 161.542 116.820 169.182 1.00 33.27  ? 2660 VAL A CB    1 
ATOM   10688 C  CG1   . VAL A 1 2660 ? 161.743 116.539 170.652 1.00 43.04  ? 2660 VAL A CG1   1 
ATOM   10689 C  CG2   . VAL A 1 2660 ? 160.483 117.878 168.992 1.00 34.90  ? 2660 VAL A CG2   1 
ATOM   10690 N  N     . LEU A 1 2661 ? 163.240 119.637 168.285 1.00 35.28  ? 2661 LEU A N     1 
ATOM   10691 C  CA    . LEU A 1 2661 ? 163.695 120.973 168.651 1.00 35.95  ? 2661 LEU A CA    1 
ATOM   10692 C  C     . LEU A 1 2661 ? 162.468 121.781 169.048 1.00 38.67  ? 2661 LEU A C     1 
ATOM   10693 O  O     . LEU A 1 2661 ? 161.845 122.438 168.212 1.00 48.17  ? 2661 LEU A O     1 
ATOM   10694 C  CB    . LEU A 1 2661 ? 164.443 121.630 167.498 1.00 44.30  ? 2661 LEU A CB    1 
ATOM   10695 C  CG    . LEU A 1 2661 ? 165.763 120.999 167.058 1.00 47.24  ? 2661 LEU A CG    1 
ATOM   10696 C  CD1   . LEU A 1 2661 ? 166.494 121.939 166.123 1.00 52.06  ? 2661 LEU A CD1   1 
ATOM   10697 C  CD2   . LEU A 1 2661 ? 166.626 120.651 168.253 1.00 51.25  ? 2661 LEU A CD2   1 
ATOM   10698 N  N     . PHE A 1 2662 ? 162.123 121.728 170.327 1.00 38.65  ? 2662 PHE A N     1 
ATOM   10699 C  CA    . PHE A 1 2662 ? 161.017 122.508 170.869 1.00 34.82  ? 2662 PHE A CA    1 
ATOM   10700 C  C     . PHE A 1 2662 ? 161.385 123.982 170.854 1.00 40.33  ? 2662 PHE A C     1 
ATOM   10701 O  O     . PHE A 1 2662 ? 162.103 124.463 171.728 1.00 49.22  ? 2662 PHE A O     1 
ATOM   10702 C  CB    . PHE A 1 2662 ? 160.685 122.041 172.278 1.00 37.95  ? 2662 PHE A CB    1 
ATOM   10703 C  CG    . PHE A 1 2662 ? 159.563 122.793 172.902 1.00 41.29  ? 2662 PHE A CG    1 
ATOM   10704 C  CD1   . PHE A 1 2662 ? 158.263 122.566 172.527 1.00 43.96  ? 2662 PHE A CD1   1 
ATOM   10705 C  CD2   . PHE A 1 2662 ? 159.818 123.734 173.880 1.00 51.03  ? 2662 PHE A CD2   1 
ATOM   10706 C  CE1   . PHE A 1 2662 ? 157.246 123.272 173.103 1.00 40.10  ? 2662 PHE A CE1   1 
ATOM   10707 C  CE2   . PHE A 1 2662 ? 158.795 124.434 174.464 1.00 46.58  ? 2662 PHE A CE2   1 
ATOM   10708 C  CZ    . PHE A 1 2662 ? 157.505 124.202 174.074 1.00 41.70  ? 2662 PHE A CZ    1 
ATOM   10709 N  N     . CYS A 1 2663 ? 160.875 124.707 169.865 1.00 37.37  ? 2663 CYS A N     1 
ATOM   10710 C  CA    . CYS A 1 2663 ? 161.122 126.136 169.721 1.00 37.99  ? 2663 CYS A CA    1 
ATOM   10711 C  C     . CYS A 1 2663 ? 159.971 126.873 170.398 1.00 40.47  ? 2663 CYS A C     1 
ATOM   10712 O  O     . CYS A 1 2663 ? 158.853 126.899 169.878 1.00 44.46  ? 2663 CYS A O     1 
ATOM   10713 C  CB    . CYS A 1 2663 ? 161.239 126.504 168.246 1.00 35.17  ? 2663 CYS A CB    1 
ATOM   10714 S  SG    . CYS A 1 2663 ? 162.634 125.725 167.405 1.00 62.79  ? 2663 CYS A SG    1 
ATOM   10715 N  N     . ASP A 1 2664 ? 160.251 127.480 171.554 1.00 40.64  ? 2664 ASP A N     1 
ATOM   10716 C  CA    . ASP A 1 2664 ? 159.181 127.856 172.474 1.00 39.73  ? 2664 ASP A CA    1 
ATOM   10717 C  C     . ASP A 1 2664 ? 158.363 129.043 171.984 1.00 44.54  ? 2664 ASP A C     1 
ATOM   10718 O  O     . ASP A 1 2664 ? 157.169 129.126 172.289 1.00 52.80  ? 2664 ASP A O     1 
ATOM   10719 C  CB    . ASP A 1 2664 ? 159.756 128.165 173.852 1.00 52.22  ? 2664 ASP A CB    1 
ATOM   10720 C  CG    . ASP A 1 2664 ? 158.755 127.935 174.967 1.00 58.74  ? 2664 ASP A CG    1 
ATOM   10721 O  OD1   . ASP A 1 2664 ? 157.709 128.616 174.983 1.00 53.52  ? 2664 ASP A OD1   1 
ATOM   10722 O  OD2   . ASP A 1 2664 ? 159.025 127.089 175.844 1.00 61.00  ? 2664 ASP A OD2   1 
ATOM   10723 N  N     . GLU A 1 2665 ? 158.971 129.987 171.267 1.00 41.08  ? 2665 GLU A N     1 
ATOM   10724 C  CA    . GLU A 1 2665 ? 158.264 131.188 170.811 1.00 41.69  ? 2665 GLU A CA    1 
ATOM   10725 C  C     . GLU A 1 2665 ? 158.528 131.397 169.323 1.00 44.29  ? 2665 GLU A C     1 
ATOM   10726 O  O     . GLU A 1 2665 ? 159.410 132.170 168.948 1.00 50.45  ? 2665 GLU A O     1 
ATOM   10727 C  CB    . GLU A 1 2665 ? 158.688 132.401 171.628 1.00 45.78  ? 2665 GLU A CB    1 
ATOM   10728 C  CG    . GLU A 1 2665 ? 158.254 132.367 173.085 1.00 50.86  ? 2665 GLU A CG    1 
ATOM   10729 C  CD    . GLU A 1 2665 ? 156.788 132.713 173.273 1.00 61.75  ? 2665 GLU A CD    1 
ATOM   10730 O  OE1   . GLU A 1 2665 ? 156.137 133.123 172.288 1.00 58.12  ? 2665 GLU A OE1   1 
ATOM   10731 O  OE2   . GLU A 1 2665 ? 156.287 132.578 174.408 1.00 63.46  ? 2665 GLU A OE2   1 
ATOM   10732 N  N     . ILE A 1 2666 ? 157.731 130.742 168.479 1.00 37.40  ? 2666 ILE A N     1 
ATOM   10733 C  CA    . ILE A 1 2666 ? 157.933 130.841 167.037 1.00 34.75  ? 2666 ILE A CA    1 
ATOM   10734 C  C     . ILE A 1 2666 ? 157.702 132.268 166.553 1.00 42.19  ? 2666 ILE A C     1 
ATOM   10735 O  O     . ILE A 1 2666 ? 158.413 132.762 165.671 1.00 45.69  ? 2666 ILE A O     1 
ATOM   10736 C  CB    . ILE A 1 2666 ? 157.019 129.842 166.307 1.00 38.85  ? 2666 ILE A CB    1 
ATOM   10737 C  CG1   . ILE A 1 2666 ? 157.312 128.420 166.759 1.00 39.03  ? 2666 ILE A CG1   1 
ATOM   10738 C  CG2   . ILE A 1 2666 ? 157.238 129.915 164.822 1.00 46.85  ? 2666 ILE A CG2   1 
ATOM   10739 C  CD1   . ILE A 1 2666 ? 158.713 127.997 166.455 1.00 41.15  ? 2666 ILE A CD1   1 
ATOM   10740 N  N     . ASN A 1 2667 ? 156.706 132.952 167.119 1.00 40.12  ? 2667 ASN A N     1 
ATOM   10741 C  CA    . ASN A 1 2667 ? 156.324 134.271 166.627 1.00 37.65  ? 2667 ASN A CA    1 
ATOM   10742 C  C     . ASN A 1 2667 ? 157.393 135.324 166.888 1.00 45.87  ? 2667 ASN A C     1 
ATOM   10743 O  O     . ASN A 1 2667 ? 157.534 136.265 166.101 1.00 51.72  ? 2667 ASN A O     1 
ATOM   10744 C  CB    . ASN A 1 2667 ? 155.009 134.703 167.272 1.00 39.66  ? 2667 ASN A CB    1 
ATOM   10745 C  CG    . ASN A 1 2667 ? 153.804 134.071 166.620 1.00 50.16  ? 2667 ASN A CG    1 
ATOM   10746 O  OD1   . ASN A 1 2667 ? 152.866 133.659 167.297 1.00 53.49  ? 2667 ASN A OD1   1 
ATOM   10747 N  ND2   . ASN A 1 2667 ? 153.818 133.995 165.295 1.00 53.00  ? 2667 ASN A ND2   1 
ATOM   10748 N  N     . LEU A 1 2668 ? 158.141 135.189 167.981 1.00 46.59  ? 2668 LEU A N     1 
ATOM   10749 C  CA    . LEU A 1 2668 ? 158.991 136.285 168.442 1.00 43.96  ? 2668 LEU A CA    1 
ATOM   10750 C  C     . LEU A 1 2668 ? 160.074 136.721 167.459 1.00 46.41  ? 2668 LEU A C     1 
ATOM   10751 O  O     . LEU A 1 2668 ? 160.281 137.941 167.334 1.00 47.91  ? 2668 LEU A O     1 
ATOM   10752 C  CB    . LEU A 1 2668 ? 159.609 135.924 169.797 1.00 44.42  ? 2668 LEU A CB    1 
ATOM   10753 C  CG    . LEU A 1 2668 ? 158.643 136.061 170.969 1.00 41.10  ? 2668 LEU A CG    1 
ATOM   10754 C  CD1   . LEU A 1 2668 ? 159.370 135.871 172.286 1.00 49.73  ? 2668 LEU A CD1   1 
ATOM   10755 C  CD2   . LEU A 1 2668 ? 157.955 137.410 170.918 1.00 47.25  ? 2668 LEU A CD2   1 
ATOM   10756 N  N     . PRO A 1 2669 ? 160.823 135.817 166.773 1.00 43.60  ? 2669 PRO A N     1 
ATOM   10757 C  CA    . PRO A 1 2669 ? 161.872 136.275 165.847 1.00 44.67  ? 2669 PRO A CA    1 
ATOM   10758 C  C     . PRO A 1 2669 ? 161.455 137.440 164.965 1.00 51.78  ? 2669 PRO A C     1 
ATOM   10759 O  O     . PRO A 1 2669 ? 160.443 137.368 164.263 1.00 55.53  ? 2669 PRO A O     1 
ATOM   10760 C  CB    . PRO A 1 2669 ? 162.154 135.026 165.010 1.00 39.17  ? 2669 PRO A CB    1 
ATOM   10761 C  CG    . PRO A 1 2669 ? 161.899 133.901 165.937 1.00 43.27  ? 2669 PRO A CG    1 
ATOM   10762 C  CD    . PRO A 1 2669 ? 160.891 134.357 166.968 1.00 44.36  ? 2669 PRO A CD    1 
ATOM   10763 N  N     . ASP A 1 2670 ? 162.225 138.523 165.008 1.00 54.44  ? 2670 ASP A N     1 
ATOM   10764 C  CA    . ASP A 1 2670 ? 161.824 139.747 164.333 1.00 57.61  ? 2670 ASP A CA    1 
ATOM   10765 C  C     . ASP A 1 2670 ? 161.955 139.620 162.821 1.00 59.61  ? 2670 ASP A C     1 
ATOM   10766 O  O     . ASP A 1 2670 ? 162.791 138.871 162.309 1.00 61.68  ? 2670 ASP A O     1 
ATOM   10767 C  CB    . ASP A 1 2670 ? 162.641 140.937 164.848 1.00 62.57  ? 2670 ASP A CB    1 
ATOM   10768 C  CG    . ASP A 1 2670 ? 164.134 140.791 164.598 1.00 74.34  ? 2670 ASP A CG    1 
ATOM   10769 O  OD1   . ASP A 1 2670 ? 164.573 139.748 164.075 1.00 71.32  ? 2670 ASP A OD1   1 
ATOM   10770 O  OD2   . ASP A 1 2670 ? 164.877 141.738 164.932 1.00 78.87  ? 2670 ASP A OD2   1 
ATOM   10771 N  N     . MET A 1 2671 ? 161.100 140.345 162.110 1.00 59.92  ? 2671 MET A N     1 
ATOM   10772 C  CA    . MET A 1 2671 ? 161.173 140.403 160.663 1.00 62.41  ? 2671 MET A CA    1 
ATOM   10773 C  C     . MET A 1 2671 ? 162.203 141.439 160.230 1.00 71.76  ? 2671 MET A C     1 
ATOM   10774 O  O     . MET A 1 2671 ? 162.554 142.356 160.977 1.00 73.63  ? 2671 MET A O     1 
ATOM   10775 C  CB    . MET A 1 2671 ? 159.807 140.742 160.069 1.00 58.15  ? 2671 MET A CB    1 
ATOM   10776 C  CG    . MET A 1 2671 ? 158.833 139.581 160.050 1.00 58.39  ? 2671 MET A CG    1 
ATOM   10777 S  SD    . MET A 1 2671 ? 157.114 140.116 160.034 1.00 80.93  ? 2671 MET A SD    1 
ATOM   10778 C  CE    . MET A 1 2671 ? 156.313 138.643 159.408 1.00 54.87  ? 2671 MET A CE    1 
ATOM   10779 N  N     . ASP A 1 2672 ? 162.689 141.284 159.003 1.00 72.25  ? 2672 ASP A N     1 
ATOM   10780 C  CA    . ASP A 1 2672 ? 163.568 142.285 158.424 1.00 73.59  ? 2672 ASP A CA    1 
ATOM   10781 C  C     . ASP A 1 2672 ? 162.764 143.540 158.092 1.00 79.95  ? 2672 ASP A C     1 
ATOM   10782 O  O     . ASP A 1 2672 ? 161.559 143.630 158.343 1.00 77.67  ? 2672 ASP A O     1 
ATOM   10783 C  CB    . ASP A 1 2672 ? 164.253 141.736 157.176 1.00 71.67  ? 2672 ASP A CB    1 
ATOM   10784 C  CG    . ASP A 1 2672 ? 164.966 140.427 157.431 1.00 77.52  ? 2672 ASP A CG    1 
ATOM   10785 O  OD1   . ASP A 1 2672 ? 164.978 139.972 158.594 1.00 79.39  ? 2672 ASP A OD1   1 
ATOM   10786 O  OD2   . ASP A 1 2672 ? 165.514 139.852 156.468 1.00 80.85  ? 2672 ASP A OD2   1 
ATOM   10787 N  N     . LYS A 1 2673 ? 163.441 144.528 157.508 1.00 84.06  ? 2673 LYS A N     1 
ATOM   10788 C  CA    . LYS A 1 2673 ? 162.717 145.679 156.989 1.00 83.35  ? 2673 LYS A CA    1 
ATOM   10789 C  C     . LYS A 1 2673 ? 161.893 145.326 155.760 1.00 81.44  ? 2673 LYS A C     1 
ATOM   10790 O  O     . LYS A 1 2673 ? 161.102 146.156 155.301 1.00 79.94  ? 2673 LYS A O     1 
ATOM   10791 C  CB    . LYS A 1 2673 ? 163.688 146.825 156.691 1.00 79.82  ? 2673 LYS A CB    1 
ATOM   10792 C  CG    . LYS A 1 2673 ? 164.942 146.436 155.926 1.00 83.69  ? 2673 LYS A CG    1 
ATOM   10793 C  CD    . LYS A 1 2673 ? 165.959 147.568 155.987 1.00 89.35  ? 2673 LYS A CD    1 
ATOM   10794 C  CE    . LYS A 1 2673 ? 167.181 147.296 155.127 1.00 89.41  ? 2673 LYS A CE    1 
ATOM   10795 N  NZ    . LYS A 1 2673 ? 166.869 147.337 153.676 1.00 91.84  ? 2673 LYS A NZ    1 
ATOM   10796 N  N     . TYR A 1 2674 ? 162.062 144.116 155.225 1.00 82.24  ? 2674 TYR A N     1 
ATOM   10797 C  CA    . TYR A 1 2674 ? 161.220 143.581 154.165 1.00 79.01  ? 2674 TYR A CA    1 
ATOM   10798 C  C     . TYR A 1 2674 ? 160.277 142.495 154.670 1.00 77.45  ? 2674 TYR A C     1 
ATOM   10799 O  O     . TYR A 1 2674 ? 159.789 141.686 153.875 1.00 74.31  ? 2674 TYR A O     1 
ATOM   10800 C  CB    . TYR A 1 2674 ? 162.083 143.039 153.031 1.00 76.17  ? 2674 TYR A CB    1 
ATOM   10801 C  CG    . TYR A 1 2674 ? 163.177 143.977 152.587 1.00 80.59  ? 2674 TYR A CG    1 
ATOM   10802 C  CD1   . TYR A 1 2674 ? 162.875 145.169 151.945 1.00 82.87  ? 2674 TYR A CD1   1 
ATOM   10803 C  CD2   . TYR A 1 2674 ? 164.511 143.673 152.812 1.00 80.25  ? 2674 TYR A CD2   1 
ATOM   10804 C  CE1   . TYR A 1 2674 ? 163.870 146.030 151.537 1.00 85.16  ? 2674 TYR A CE1   1 
ATOM   10805 C  CE2   . TYR A 1 2674 ? 165.512 144.527 152.408 1.00 83.38  ? 2674 TYR A CE2   1 
ATOM   10806 C  CZ    . TYR A 1 2674 ? 165.187 145.703 151.769 1.00 86.81  ? 2674 TYR A CZ    1 
ATOM   10807 O  OH    . TYR A 1 2674 ? 166.184 146.560 151.366 1.00 86.62  ? 2674 TYR A OH    1 
ATOM   10808 N  N     . GLY A 1 2675 ? 160.026 142.449 155.976 1.00 78.87  ? 2675 GLY A N     1 
ATOM   10809 C  CA    . GLY A 1 2675 ? 159.062 141.528 156.545 1.00 72.46  ? 2675 GLY A CA    1 
ATOM   10810 C  C     . GLY A 1 2675 ? 159.348 140.060 156.301 1.00 70.82  ? 2675 GLY A C     1 
ATOM   10811 O  O     . GLY A 1 2675 ? 158.595 139.389 155.590 1.00 74.58  ? 2675 GLY A O     1 
ATOM   10812 N  N     . THR A 1 2676 ? 160.429 139.547 156.882 1.00 64.28  ? 2676 THR A N     1 
ATOM   10813 C  CA    . THR A 1 2676 ? 160.758 138.132 156.763 1.00 59.93  ? 2676 THR A CA    1 
ATOM   10814 C  C     . THR A 1 2676 ? 161.556 137.696 157.980 1.00 60.43  ? 2676 THR A C     1 
ATOM   10815 O  O     . THR A 1 2676 ? 162.545 138.342 158.338 1.00 66.51  ? 2676 THR A O     1 
ATOM   10816 C  CB    . THR A 1 2676 ? 161.554 137.845 155.487 1.00 63.21  ? 2676 THR A CB    1 
ATOM   10817 O  OG1   . THR A 1 2676 ? 160.762 138.181 154.342 1.00 74.12  ? 2676 THR A OG1   1 
ATOM   10818 C  CG2   . THR A 1 2676 ? 161.929 136.376 155.421 1.00 56.70  ? 2676 THR A CG2   1 
ATOM   10819 N  N     . GLN A 1 2677 ? 161.127 136.604 158.606 1.00 54.38  ? 2677 GLN A N     1 
ATOM   10820 C  CA    . GLN A 1 2677 ? 161.848 136.010 159.726 1.00 46.02  ? 2677 GLN A CA    1 
ATOM   10821 C  C     . GLN A 1 2677 ? 162.820 134.980 159.164 1.00 51.78  ? 2677 GLN A C     1 
ATOM   10822 O  O     . GLN A 1 2677 ? 162.400 133.959 158.609 1.00 55.04  ? 2677 GLN A O     1 
ATOM   10823 C  CB    . GLN A 1 2677 ? 160.875 135.377 160.715 1.00 40.71  ? 2677 GLN A CB    1 
ATOM   10824 C  CG    . GLN A 1 2677 ? 159.868 136.352 161.292 1.00 44.60  ? 2677 GLN A CG    1 
ATOM   10825 C  CD    . GLN A 1 2677 ? 158.809 135.673 162.133 1.00 43.15  ? 2677 GLN A CD    1 
ATOM   10826 O  OE1   . GLN A 1 2677 ? 159.114 135.034 163.136 1.00 45.06  ? 2677 GLN A OE1   1 
ATOM   10827 N  NE2   . GLN A 1 2677 ? 157.555 135.808 161.727 1.00 47.09  ? 2677 GLN A NE2   1 
ATOM   10828 N  N     . ARG A 1 2678 ? 164.119 135.252 159.299 1.00 56.71  ? 2678 ARG A N     1 
ATOM   10829 C  CA    . ARG A 1 2678 ? 165.125 134.404 158.667 1.00 52.99  ? 2678 ARG A CA    1 
ATOM   10830 C  C     . ARG A 1 2678 ? 165.143 133.005 159.269 1.00 49.52  ? 2678 ARG A C     1 
ATOM   10831 O  O     . ARG A 1 2678 ? 165.282 132.015 158.542 1.00 52.20  ? 2678 ARG A O     1 
ATOM   10832 C  CB    . ARG A 1 2678 ? 166.501 135.056 158.778 1.00 59.74  ? 2678 ARG A CB    1 
ATOM   10833 C  CG    . ARG A 1 2678 ? 166.524 136.510 158.343 1.00 61.67  ? 2678 ARG A CG    1 
ATOM   10834 C  CD    . ARG A 1 2678 ? 167.922 137.088 158.428 1.00 73.52  ? 2678 ARG A CD    1 
ATOM   10835 N  NE    . ARG A 1 2678 ? 168.905 136.228 157.782 1.00 84.15  ? 2678 ARG A NE    1 
ATOM   10836 C  CZ    . ARG A 1 2678 ? 169.371 136.417 156.555 1.00 81.55  ? 2678 ARG A CZ    1 
ATOM   10837 N  NH1   . ARG A 1 2678 ? 168.956 137.425 155.806 1.00 75.28  ? 2678 ARG A NH1   1 
ATOM   10838 N  NH2   . ARG A 1 2678 ? 170.276 135.573 156.068 1.00 74.04  ? 2678 ARG A NH2   1 
ATOM   10839 N  N     . VAL A 1 2679 ? 165.014 132.899 160.593 1.00 46.04  ? 2679 VAL A N     1 
ATOM   10840 C  CA    . VAL A 1 2679 ? 164.999 131.581 161.219 1.00 44.19  ? 2679 VAL A CA    1 
ATOM   10841 C  C     . VAL A 1 2679 ? 163.749 130.809 160.819 1.00 45.03  ? 2679 VAL A C     1 
ATOM   10842 O  O     . VAL A 1 2679 ? 163.791 129.582 160.668 1.00 48.70  ? 2679 VAL A O     1 
ATOM   10843 C  CB    . VAL A 1 2679 ? 165.136 131.706 162.748 1.00 41.56  ? 2679 VAL A CB    1 
ATOM   10844 C  CG1   . VAL A 1 2679 ? 163.955 132.442 163.338 1.00 41.32  ? 2679 VAL A CG1   1 
ATOM   10845 C  CG2   . VAL A 1 2679 ? 165.287 130.335 163.383 1.00 42.24  ? 2679 VAL A CG2   1 
ATOM   10846 N  N     . ILE A 1 2680 ? 162.623 131.500 160.632 1.00 43.60  ? 2680 ILE A N     1 
ATOM   10847 C  CA    . ILE A 1 2680 ? 161.408 130.825 160.188 1.00 40.01  ? 2680 ILE A CA    1 
ATOM   10848 C  C     . ILE A 1 2680 ? 161.578 130.298 158.770 1.00 43.24  ? 2680 ILE A C     1 
ATOM   10849 O  O     . ILE A 1 2680 ? 161.134 129.192 158.449 1.00 46.80  ? 2680 ILE A O     1 
ATOM   10850 C  CB    . ILE A 1 2680 ? 160.199 131.768 160.311 1.00 37.99  ? 2680 ILE A CB    1 
ATOM   10851 C  CG1   . ILE A 1 2680 ? 159.927 132.074 161.783 1.00 38.56  ? 2680 ILE A CG1   1 
ATOM   10852 C  CG2   . ILE A 1 2680 ? 158.972 131.164 159.654 1.00 33.33  ? 2680 ILE A CG2   1 
ATOM   10853 C  CD1   . ILE A 1 2680 ? 159.892 130.849 162.654 1.00 39.09  ? 2680 ILE A CD1   1 
ATOM   10854 N  N     . SER A 1 2681 ? 162.234 131.072 157.902 1.00 42.22  ? 2681 SER A N     1 
ATOM   10855 C  CA    . SER A 1 2681 ? 162.527 130.587 156.556 1.00 40.32  ? 2681 SER A CA    1 
ATOM   10856 C  C     . SER A 1 2681 ? 163.485 129.404 156.595 1.00 41.55  ? 2681 SER A C     1 
ATOM   10857 O  O     . SER A 1 2681 ? 163.361 128.467 155.797 1.00 45.29  ? 2681 SER A O     1 
ATOM   10858 C  CB    . SER A 1 2681 ? 163.101 131.717 155.705 1.00 42.99  ? 2681 SER A CB    1 
ATOM   10859 O  OG    . SER A 1 2681 ? 164.364 132.128 156.194 1.00 51.71  ? 2681 SER A OG    1 
ATOM   10860 N  N     . PHE A 1 2682 ? 164.452 129.432 157.514 1.00 40.24  ? 2682 PHE A N     1 
ATOM   10861 C  CA    . PHE A 1 2682 ? 165.370 128.307 157.674 1.00 39.02  ? 2682 PHE A CA    1 
ATOM   10862 C  C     . PHE A 1 2682 ? 164.622 127.044 158.085 1.00 42.72  ? 2682 PHE A C     1 
ATOM   10863 O  O     . PHE A 1 2682 ? 164.847 125.961 157.530 1.00 49.52  ? 2682 PHE A O     1 
ATOM   10864 C  CB    . PHE A 1 2682 ? 166.439 128.668 158.705 1.00 39.60  ? 2682 PHE A CB    1 
ATOM   10865 C  CG    . PHE A 1 2682 ? 167.535 127.653 158.830 1.00 47.58  ? 2682 PHE A CG    1 
ATOM   10866 C  CD1   . PHE A 1 2682 ? 168.197 127.188 157.710 1.00 51.91  ? 2682 PHE A CD1   1 
ATOM   10867 C  CD2   . PHE A 1 2682 ? 167.915 127.176 160.071 1.00 52.12  ? 2682 PHE A CD2   1 
ATOM   10868 C  CE1   . PHE A 1 2682 ? 169.211 126.262 157.825 1.00 53.79  ? 2682 PHE A CE1   1 
ATOM   10869 C  CE2   . PHE A 1 2682 ? 168.928 126.249 160.191 1.00 52.05  ? 2682 PHE A CE2   1 
ATOM   10870 C  CZ    . PHE A 1 2682 ? 169.575 125.791 159.067 1.00 53.28  ? 2682 PHE A CZ    1 
ATOM   10871 N  N     . ILE A 1 2683 ? 163.715 127.169 159.056 1.00 38.40  ? 2683 ILE A N     1 
ATOM   10872 C  CA    . ILE A 1 2683 ? 162.921 126.024 159.493 1.00 32.98  ? 2683 ILE A CA    1 
ATOM   10873 C  C     . ILE A 1 2683 ? 162.025 125.536 158.363 1.00 38.74  ? 2683 ILE A C     1 
ATOM   10874 O  O     . ILE A 1 2683 ? 161.839 124.328 158.176 1.00 44.16  ? 2683 ILE A O     1 
ATOM   10875 C  CB    . ILE A 1 2683 ? 162.105 126.384 160.748 1.00 33.12  ? 2683 ILE A CB    1 
ATOM   10876 C  CG1   . ILE A 1 2683 ? 163.035 126.744 161.904 1.00 38.78  ? 2683 ILE A CG1   1 
ATOM   10877 C  CG2   . ILE A 1 2683 ? 161.197 125.234 161.145 1.00 35.50  ? 2683 ILE A CG2   1 
ATOM   10878 C  CD1   . ILE A 1 2683 ? 162.312 127.174 163.155 1.00 36.99  ? 2683 ILE A CD1   1 
ATOM   10879 N  N     . ARG A 1 2684 ? 161.455 126.465 157.594 1.00 37.52  ? 2684 ARG A N     1 
ATOM   10880 C  CA    . ARG A 1 2684 ? 160.612 126.085 156.466 1.00 32.88  ? 2684 ARG A CA    1 
ATOM   10881 C  C     . ARG A 1 2684 ? 161.402 125.303 155.428 1.00 39.60  ? 2684 ARG A C     1 
ATOM   10882 O  O     . ARG A 1 2684 ? 160.910 124.310 154.882 1.00 45.66  ? 2684 ARG A O     1 
ATOM   10883 C  CB    . ARG A 1 2684 ? 159.992 127.330 155.839 1.00 30.35  ? 2684 ARG A CB    1 
ATOM   10884 C  CG    . ARG A 1 2684 ? 158.745 127.058 155.029 1.00 39.42  ? 2684 ARG A CG    1 
ATOM   10885 C  CD    . ARG A 1 2684 ? 159.062 126.849 153.566 1.00 39.85  ? 2684 ARG A CD    1 
ATOM   10886 N  NE    . ARG A 1 2684 ? 159.699 128.020 152.981 1.00 43.45  ? 2684 ARG A NE    1 
ATOM   10887 C  CZ    . ARG A 1 2684 ? 159.971 128.155 151.691 1.00 46.71  ? 2684 ARG A CZ    1 
ATOM   10888 N  NH1   . ARG A 1 2684 ? 159.651 127.217 150.816 1.00 40.76  ? 2684 ARG A NH1   1 
ATOM   10889 N  NH2   . ARG A 1 2684 ? 160.578 129.261 151.270 1.00 49.89  ? 2684 ARG A NH2   1 
ATOM   10890 N  N     . GLN A 1 2685 ? 162.625 125.744 155.133 1.00 38.45  ? 2685 GLN A N     1 
ATOM   10891 C  CA    . GLN A 1 2685 ? 163.473 125.010 154.201 1.00 39.89  ? 2685 GLN A CA    1 
ATOM   10892 C  C     . GLN A 1 2685 ? 163.805 123.626 154.741 1.00 42.41  ? 2685 GLN A C     1 
ATOM   10893 O  O     . GLN A 1 2685 ? 163.792 122.636 154.002 1.00 44.32  ? 2685 GLN A O     1 
ATOM   10894 C  CB    . GLN A 1 2685 ? 164.752 125.799 153.923 1.00 39.30  ? 2685 GLN A CB    1 
ATOM   10895 C  CG    . GLN A 1 2685 ? 165.935 124.933 153.534 1.00 44.92  ? 2685 GLN A CG    1 
ATOM   10896 C  CD    . GLN A 1 2685 ? 167.127 125.741 153.077 1.00 53.05  ? 2685 GLN A CD    1 
ATOM   10897 O  OE1   . GLN A 1 2685 ? 167.643 126.579 153.814 1.00 54.07  ? 2685 GLN A OE1   1 
ATOM   10898 N  NE2   . GLN A 1 2685 ? 167.575 125.492 151.853 1.00 54.12  ? 2685 GLN A NE2   1 
ATOM   10899 N  N     . MET A 1 2686 ? 164.098 123.539 156.039 1.00 40.10  ? 2686 MET A N     1 
ATOM   10900 C  CA    . MET A 1 2686 ? 164.511 122.265 156.616 1.00 38.88  ? 2686 MET A CA    1 
ATOM   10901 C  C     . MET A 1 2686 ? 163.345 121.296 156.778 1.00 40.25  ? 2686 MET A C     1 
ATOM   10902 O  O     . MET A 1 2686 ? 163.565 120.086 156.893 1.00 43.70  ? 2686 MET A O     1 
ATOM   10903 C  CB    . MET A 1 2686 ? 165.211 122.513 157.950 1.00 35.39  ? 2686 MET A CB    1 
ATOM   10904 C  CG    . MET A 1 2686 ? 166.664 122.919 157.780 1.00 43.81  ? 2686 MET A CG    1 
ATOM   10905 S  SD    . MET A 1 2686 ? 167.594 122.946 159.315 1.00 60.00  ? 2686 MET A SD    1 
ATOM   10906 C  CE    . MET A 1 2686 ? 166.429 123.782 160.378 1.00 45.12  ? 2686 MET A CE    1 
ATOM   10907 N  N     . VAL A 1 2687 ? 162.108 121.793 156.793 1.00 39.16  ? 2687 VAL A N     1 
ATOM   10908 C  CA    . VAL A 1 2687 ? 160.958 120.894 156.862 1.00 39.40  ? 2687 VAL A CA    1 
ATOM   10909 C  C     . VAL A 1 2687 ? 160.339 120.611 155.498 1.00 41.54  ? 2687 VAL A C     1 
ATOM   10910 O  O     . VAL A 1 2687 ? 159.638 119.600 155.346 1.00 45.61  ? 2687 VAL A O     1 
ATOM   10911 C  CB    . VAL A 1 2687 ? 159.870 121.431 157.810 1.00 37.16  ? 2687 VAL A CB    1 
ATOM   10912 C  CG1   . VAL A 1 2687 ? 160.448 121.698 159.189 1.00 39.17  ? 2687 VAL A CG1   1 
ATOM   10913 C  CG2   . VAL A 1 2687 ? 159.223 122.678 157.239 1.00 36.38  ? 2687 VAL A CG2   1 
ATOM   10914 N  N     . GLU A 1 2688 ? 160.574 121.464 154.502 1.00 39.69  ? 2688 GLU A N     1 
ATOM   10915 C  CA    . GLU A 1 2688 ? 160.058 121.226 153.158 1.00 40.39  ? 2688 GLU A CA    1 
ATOM   10916 C  C     . GLU A 1 2688 ? 161.042 120.413 152.322 1.00 48.73  ? 2688 GLU A C     1 
ATOM   10917 O  O     . GLU A 1 2688 ? 160.696 119.348 151.802 1.00 50.74  ? 2688 GLU A O     1 
ATOM   10918 C  CB    . GLU A 1 2688 ? 159.744 122.557 152.466 1.00 38.75  ? 2688 GLU A CB    1 
ATOM   10919 C  CG    . GLU A 1 2688 ? 159.214 122.388 151.053 1.00 47.46  ? 2688 GLU A CG    1 
ATOM   10920 C  CD    . GLU A 1 2688 ? 158.572 123.646 150.506 1.00 56.30  ? 2688 GLU A CD    1 
ATOM   10921 O  OE1   . GLU A 1 2688 ? 158.559 124.670 151.220 1.00 61.62  ? 2688 GLU A OE1   1 
ATOM   10922 O  OE2   . GLU A 1 2688 ? 158.075 123.608 149.361 1.00 47.78  ? 2688 GLU A OE2   1 
ATOM   10923 N  N     . HIS A 1 2689 ? 162.270 120.907 152.187 1.00 47.68  ? 2689 HIS A N     1 
ATOM   10924 C  CA    . HIS A 1 2689 ? 163.293 120.234 151.402 1.00 43.54  ? 2689 HIS A CA    1 
ATOM   10925 C  C     . HIS A 1 2689 ? 164.067 119.191 152.195 1.00 47.18  ? 2689 HIS A C     1 
ATOM   10926 O  O     . HIS A 1 2689 ? 164.891 118.481 151.612 1.00 52.62  ? 2689 HIS A O     1 
ATOM   10927 C  CB    . HIS A 1 2689 ? 164.265 121.264 150.820 1.00 43.88  ? 2689 HIS A CB    1 
ATOM   10928 C  CG    . HIS A 1 2689 ? 163.587 122.402 150.124 1.00 50.43  ? 2689 HIS A CG    1 
ATOM   10929 N  ND1   . HIS A 1 2689 ? 163.722 123.712 150.532 1.00 54.81  ? 2689 HIS A ND1   1 
ATOM   10930 C  CD2   . HIS A 1 2689 ? 162.767 122.427 149.047 1.00 49.12  ? 2689 HIS A CD2   1 
ATOM   10931 C  CE1   . HIS A 1 2689 ? 163.015 124.494 149.737 1.00 52.30  ? 2689 HIS A CE1   1 
ATOM   10932 N  NE2   . HIS A 1 2689 ? 162.426 123.739 148.827 1.00 54.36  ? 2689 HIS A NE2   1 
ATOM   10933 N  N     . GLY A 1 2690 ? 163.821 119.079 153.497 1.00 49.27  ? 2690 GLY A N     1 
ATOM   10934 C  CA    . GLY A 1 2690 ? 164.482 118.069 154.300 1.00 46.27  ? 2690 GLY A CA    1 
ATOM   10935 C  C     . GLY A 1 2690 ? 165.974 118.251 154.439 1.00 44.49  ? 2690 GLY A C     1 
ATOM   10936 O  O     . GLY A 1 2690 ? 166.714 117.264 154.417 1.00 48.59  ? 2690 GLY A O     1 
ATOM   10937 N  N     . GLY A 1 2691 ? 166.439 119.485 154.578 1.00 39.37  ? 2691 GLY A N     1 
ATOM   10938 C  CA    . GLY A 1 2691 ? 167.858 119.730 154.714 1.00 40.66  ? 2691 GLY A CA    1 
ATOM   10939 C  C     . GLY A 1 2691 ? 168.164 121.207 154.574 1.00 45.55  ? 2691 GLY A C     1 
ATOM   10940 O  O     . GLY A 1 2691 ? 167.264 122.048 154.544 1.00 53.92  ? 2691 GLY A O     1 
ATOM   10941 N  N     . PHE A 1 2692 ? 169.457 121.499 154.489 1.00 46.41  ? 2692 PHE A N     1 
ATOM   10942 C  CA    . PHE A 1 2692 ? 169.931 122.873 154.362 1.00 47.85  ? 2692 PHE A CA    1 
ATOM   10943 C  C     . PHE A 1 2692 ? 171.298 122.857 153.686 1.00 51.15  ? 2692 PHE A C     1 
ATOM   10944 O  O     . PHE A 1 2692 ? 171.716 121.846 153.116 1.00 52.49  ? 2692 PHE A O     1 
ATOM   10945 C  CB    . PHE A 1 2692 ? 169.950 123.567 155.730 1.00 47.01  ? 2692 PHE A CB    1 
ATOM   10946 C  CG    . PHE A 1 2692 ? 170.958 123.003 156.690 1.00 51.62  ? 2692 PHE A CG    1 
ATOM   10947 C  CD1   . PHE A 1 2692 ? 170.695 121.837 157.384 1.00 53.90  ? 2692 PHE A CD1   1 
ATOM   10948 C  CD2   . PHE A 1 2692 ? 172.160 123.651 156.912 1.00 56.96  ? 2692 PHE A CD2   1 
ATOM   10949 C  CE1   . PHE A 1 2692 ? 171.616 121.320 158.270 1.00 55.53  ? 2692 PHE A CE1   1 
ATOM   10950 C  CE2   . PHE A 1 2692 ? 173.084 123.138 157.796 1.00 57.18  ? 2692 PHE A CE2   1 
ATOM   10951 C  CZ    . PHE A 1 2692 ? 172.811 121.972 158.475 1.00 57.61  ? 2692 PHE A CZ    1 
ATOM   10952 N  N     . TYR A 1 2693 ? 171.992 123.991 153.733 1.00 52.24  ? 2693 TYR A N     1 
ATOM   10953 C  CA    . TYR A 1 2693 ? 173.294 124.148 153.098 1.00 53.20  ? 2693 TYR A CA    1 
ATOM   10954 C  C     . TYR A 1 2693 ? 174.316 124.601 154.130 1.00 60.70  ? 2693 TYR A C     1 
ATOM   10955 O  O     . TYR A 1 2693 ? 174.093 125.591 154.834 1.00 65.77  ? 2693 TYR A O     1 
ATOM   10956 C  CB    . TYR A 1 2693 ? 173.225 125.165 151.956 1.00 54.63  ? 2693 TYR A CB    1 
ATOM   10957 C  CG    . TYR A 1 2693 ? 172.774 124.596 150.630 1.00 57.39  ? 2693 TYR A CG    1 
ATOM   10958 C  CD1   . TYR A 1 2693 ? 173.599 123.757 149.897 1.00 58.19  ? 2693 TYR A CD1   1 
ATOM   10959 C  CD2   . TYR A 1 2693 ? 171.526 124.906 150.108 1.00 55.67  ? 2693 TYR A CD2   1 
ATOM   10960 C  CE1   . TYR A 1 2693 ? 173.194 123.242 148.683 1.00 55.80  ? 2693 TYR A CE1   1 
ATOM   10961 C  CE2   . TYR A 1 2693 ? 171.114 124.396 148.896 1.00 53.99  ? 2693 TYR A CE2   1 
ATOM   10962 C  CZ    . TYR A 1 2693 ? 171.950 123.563 148.188 1.00 56.40  ? 2693 TYR A CZ    1 
ATOM   10963 O  OH    . TYR A 1 2693 ? 171.543 123.049 146.979 1.00 60.65  ? 2693 TYR A OH    1 
ATOM   10964 N  N     . ARG A 1 2694 ? 175.433 123.883 154.215 1.00 61.67  ? 2694 ARG A N     1 
ATOM   10965 C  CA    . ARG A 1 2694 ? 176.534 124.327 155.059 1.00 66.65  ? 2694 ARG A CA    1 
ATOM   10966 C  C     . ARG A 1 2694 ? 177.183 125.573 154.474 1.00 73.43  ? 2694 ARG A C     1 
ATOM   10967 O  O     . ARG A 1 2694 ? 177.442 125.653 153.270 1.00 76.24  ? 2694 ARG A O     1 
ATOM   10968 C  CB    . ARG A 1 2694 ? 177.579 123.223 155.214 1.00 68.63  ? 2694 ARG A CB    1 
ATOM   10969 C  CG    . ARG A 1 2694 ? 177.319 122.269 156.364 1.00 65.04  ? 2694 ARG A CG    1 
ATOM   10970 C  CD    . ARG A 1 2694 ? 178.605 121.590 156.812 1.00 67.39  ? 2694 ARG A CD    1 
ATOM   10971 N  NE    . ARG A 1 2694 ? 179.232 120.830 155.738 1.00 74.26  ? 2694 ARG A NE    1 
ATOM   10972 C  CZ    . ARG A 1 2694 ? 179.474 119.527 155.784 1.00 73.17  ? 2694 ARG A CZ    1 
ATOM   10973 N  NH1   . ARG A 1 2694 ? 179.163 118.804 156.847 1.00 68.05  ? 2694 ARG A NH1   1 
ATOM   10974 N  NH2   . ARG A 1 2694 ? 180.046 118.935 154.740 1.00 74.18  ? 2694 ARG A NH2   1 
ATOM   10975 N  N     . THR A 1 2695 ? 177.455 126.550 155.336 1.00 73.77  ? 2695 THR A N     1 
ATOM   10976 C  CA    . THR A 1 2695 ? 178.065 127.800 154.905 1.00 80.33  ? 2695 THR A CA    1 
ATOM   10977 C  C     . THR A 1 2695 ? 179.574 127.697 154.729 1.00 84.61  ? 2695 THR A C     1 
ATOM   10978 O  O     . THR A 1 2695 ? 180.189 128.646 154.233 1.00 89.12  ? 2695 THR A O     1 
ATOM   10979 C  CB    . THR A 1 2695 ? 177.745 128.917 155.901 1.00 85.32  ? 2695 THR A CB    1 
ATOM   10980 O  OG1   . THR A 1 2695 ? 178.285 128.582 157.186 1.00 89.74  ? 2695 THR A OG1   1 
ATOM   10981 C  CG2   . THR A 1 2695 ? 176.242 129.106 156.022 1.00 80.36  ? 2695 THR A CG2   1 
ATOM   10982 N  N     . SER A 1 2696 ? 180.183 126.579 155.120 1.00 80.08  ? 2696 SER A N     1 
ATOM   10983 C  CA    . SER A 1 2696 ? 181.619 126.378 154.978 1.00 81.88  ? 2696 SER A CA    1 
ATOM   10984 C  C     . SER A 1 2696 ? 181.980 125.512 153.780 1.00 80.55  ? 2696 SER A C     1 
ATOM   10985 O  O     . SER A 1 2696 ? 182.930 125.826 153.057 1.00 83.15  ? 2696 SER A O     1 
ATOM   10986 C  CB    . SER A 1 2696 ? 182.191 125.747 156.250 1.00 83.17  ? 2696 SER A CB    1 
ATOM   10987 O  OG    . SER A 1 2696 ? 181.650 124.455 156.461 1.00 78.98  ? 2696 SER A OG    1 
ATOM   10988 N  N     . ASP A 1 2697 ? 181.241 124.429 153.555 1.00 76.11  ? 2697 ASP A N     1 
ATOM   10989 C  CA    . ASP A 1 2697 ? 181.502 123.526 152.445 1.00 78.28  ? 2697 ASP A CA    1 
ATOM   10990 C  C     . ASP A 1 2697 ? 180.690 123.887 151.206 1.00 80.10  ? 2697 ASP A C     1 
ATOM   10991 O  O     . ASP A 1 2697 ? 181.105 123.553 150.091 1.00 79.19  ? 2697 ASP A O     1 
ATOM   10992 C  CB    . ASP A 1 2697 ? 181.206 122.085 152.892 1.00 83.33  ? 2697 ASP A CB    1 
ATOM   10993 C  CG    . ASP A 1 2697 ? 181.758 121.024 151.943 1.00 87.42  ? 2697 ASP A CG    1 
ATOM   10994 O  OD1   . ASP A 1 2697 ? 182.354 120.051 152.449 1.00 87.45  ? 2697 ASP A OD1   1 
ATOM   10995 O  OD2   . ASP A 1 2697 ? 181.578 121.120 150.714 1.00 85.69  ? 2697 ASP A OD2   1 
ATOM   10996 N  N     . GLN A 1 2698 ? 179.575 124.603 151.377 1.00 79.30  ? 2698 GLN A N     1 
ATOM   10997 C  CA    . GLN A 1 2698 ? 178.631 124.893 150.295 1.00 73.77  ? 2698 GLN A CA    1 
ATOM   10998 C  C     . GLN A 1 2698 ? 178.058 123.598 149.721 1.00 69.61  ? 2698 GLN A C     1 
ATOM   10999 O  O     . GLN A 1 2698 ? 177.957 123.418 148.506 1.00 71.31  ? 2698 GLN A O     1 
ATOM   11000 C  CB    . GLN A 1 2698 ? 179.273 125.744 149.194 1.00 72.85  ? 2698 GLN A CB    1 
ATOM   11001 C  CG    . GLN A 1 2698 ? 179.311 127.237 149.473 1.00 72.65  ? 2698 GLN A CG    1 
ATOM   11002 C  CD    . GLN A 1 2698 ? 180.249 127.601 150.603 1.00 83.71  ? 2698 GLN A CD    1 
ATOM   11003 O  OE1   . GLN A 1 2698 ? 181.444 127.314 150.550 1.00 86.40  ? 2698 GLN A OE1   1 
ATOM   11004 N  NE2   . GLN A 1 2698 ? 179.713 128.249 151.630 1.00 83.41  ? 2698 GLN A NE2   1 
ATOM   11005 N  N     . THR A 1 2699 ? 177.675 122.691 150.615 1.00 64.24  ? 2699 THR A N     1 
ATOM   11006 C  CA    . THR A 1 2699 ? 177.155 121.389 150.231 1.00 68.97  ? 2699 THR A CA    1 
ATOM   11007 C  C     . THR A 1 2699 ? 175.805 121.159 150.895 1.00 69.47  ? 2699 THR A C     1 
ATOM   11008 O  O     . THR A 1 2699 ? 175.505 121.710 151.957 1.00 70.22  ? 2699 THR A O     1 
ATOM   11009 C  CB    . THR A 1 2699 ? 178.126 120.257 150.604 1.00 72.03  ? 2699 THR A CB    1 
ATOM   11010 O  OG1   . THR A 1 2699 ? 177.679 119.028 150.019 1.00 75.48  ? 2699 THR A OG1   1 
ATOM   11011 C  CG2   . THR A 1 2699 ? 178.212 120.093 152.111 1.00 64.95  ? 2699 THR A CG2   1 
ATOM   11012 N  N     . TRP A 1 2700 ? 174.985 120.342 150.242 1.00 65.99  ? 2700 TRP A N     1 
ATOM   11013 C  CA    . TRP A 1 2700 ? 173.675 120.011 150.780 1.00 56.79  ? 2700 TRP A CA    1 
ATOM   11014 C  C     . TRP A 1 2700 ? 173.806 119.033 151.938 1.00 55.53  ? 2700 TRP A C     1 
ATOM   11015 O  O     . TRP A 1 2700 ? 174.465 117.996 151.826 1.00 59.08  ? 2700 TRP A O     1 
ATOM   11016 C  CB    . TRP A 1 2700 ? 172.789 119.414 149.687 1.00 52.97  ? 2700 TRP A CB    1 
ATOM   11017 C  CG    . TRP A 1 2700 ? 171.398 119.097 150.140 1.00 49.41  ? 2700 TRP A CG    1 
ATOM   11018 C  CD1   . TRP A 1 2700 ? 170.874 117.860 150.368 1.00 49.44  ? 2700 TRP A CD1   1 
ATOM   11019 C  CD2   . TRP A 1 2700 ? 170.349 120.032 150.411 1.00 46.40  ? 2700 TRP A CD2   1 
ATOM   11020 N  NE1   . TRP A 1 2700 ? 169.566 117.965 150.769 1.00 46.67  ? 2700 TRP A NE1   1 
ATOM   11021 C  CE2   . TRP A 1 2700 ? 169.219 119.290 150.803 1.00 46.17  ? 2700 TRP A CE2   1 
ATOM   11022 C  CE3   . TRP A 1 2700 ? 170.255 121.425 150.362 1.00 47.61  ? 2700 TRP A CE3   1 
ATOM   11023 C  CZ2   . TRP A 1 2700 ? 168.013 119.892 151.143 1.00 47.87  ? 2700 TRP A CZ2   1 
ATOM   11024 C  CZ3   . TRP A 1 2700 ? 169.057 122.020 150.701 1.00 48.80  ? 2700 TRP A CZ3   1 
ATOM   11025 C  CH2   . TRP A 1 2700 ? 167.953 121.256 151.086 1.00 48.04  ? 2700 TRP A CH2   1 
ATOM   11026 N  N     . VAL A 1 2701 ? 173.171 119.368 153.057 1.00 52.93  ? 2701 VAL A N     1 
ATOM   11027 C  CA    . VAL A 1 2701 ? 173.136 118.520 154.240 1.00 47.90  ? 2701 VAL A CA    1 
ATOM   11028 C  C     . VAL A 1 2701 ? 171.695 118.088 154.448 1.00 43.59  ? 2701 VAL A C     1 
ATOM   11029 O  O     . VAL A 1 2701 ? 170.820 118.927 154.690 1.00 49.54  ? 2701 VAL A O     1 
ATOM   11030 C  CB    . VAL A 1 2701 ? 173.672 119.246 155.481 1.00 48.68  ? 2701 VAL A CB    1 
ATOM   11031 C  CG1   . VAL A 1 2701 ? 173.688 118.311 156.669 1.00 51.36  ? 2701 VAL A CG1   1 
ATOM   11032 C  CG2   . VAL A 1 2701 ? 175.058 119.789 155.211 1.00 60.73  ? 2701 VAL A CG2   1 
ATOM   11033 N  N     . LYS A 1 2702 ? 171.452 116.785 154.352 1.00 43.18  ? 2702 LYS A N     1 
ATOM   11034 C  CA    . LYS A 1 2702 ? 170.125 116.218 154.538 1.00 43.06  ? 2702 LYS A CA    1 
ATOM   11035 C  C     . LYS A 1 2702 ? 169.914 115.894 156.010 1.00 46.30  ? 2702 LYS A C     1 
ATOM   11036 O  O     . LYS A 1 2702 ? 170.759 115.250 156.636 1.00 54.15  ? 2702 LYS A O     1 
ATOM   11037 C  CB    . LYS A 1 2702 ? 169.961 114.958 153.689 1.00 48.77  ? 2702 LYS A CB    1 
ATOM   11038 C  CG    . LYS A 1 2702 ? 168.599 114.302 153.794 1.00 51.58  ? 2702 LYS A CG    1 
ATOM   11039 C  CD    . LYS A 1 2702 ? 168.528 113.058 152.926 1.00 58.77  ? 2702 LYS A CD    1 
ATOM   11040 C  CE    . LYS A 1 2702 ? 169.317 111.914 153.543 1.00 66.06  ? 2702 LYS A CE    1 
ATOM   11041 N  NZ    . LYS A 1 2702 ? 169.165 110.649 152.774 1.00 74.00  ? 2702 LYS A NZ    1 
ATOM   11042 N  N     . LEU A 1 2703 ? 168.793 116.349 156.559 1.00 46.96  ? 2703 LEU A N     1 
ATOM   11043 C  CA    . LEU A 1 2703 ? 168.485 116.053 157.947 1.00 41.84  ? 2703 LEU A CA    1 
ATOM   11044 C  C     . LEU A 1 2703 ? 168.121 114.581 158.107 1.00 43.35  ? 2703 LEU A C     1 
ATOM   11045 O  O     . LEU A 1 2703 ? 167.646 113.924 157.178 1.00 50.29  ? 2703 LEU A O     1 
ATOM   11046 C  CB    . LEU A 1 2703 ? 167.338 116.929 158.446 1.00 37.58  ? 2703 LEU A CB    1 
ATOM   11047 C  CG    . LEU A 1 2703 ? 167.616 118.425 158.581 1.00 37.58  ? 2703 LEU A CG    1 
ATOM   11048 C  CD1   . LEU A 1 2703 ? 166.393 119.137 159.125 1.00 38.45  ? 2703 LEU A CD1   1 
ATOM   11049 C  CD2   . LEU A 1 2703 ? 168.819 118.673 159.461 1.00 38.04  ? 2703 LEU A CD2   1 
ATOM   11050 N  N     . GLU A 1 2704 ? 168.353 114.062 159.309 1.00 43.93  ? 2704 GLU A N     1 
ATOM   11051 C  CA    . GLU A 1 2704 ? 167.967 112.698 159.633 1.00 50.62  ? 2704 GLU A CA    1 
ATOM   11052 C  C     . GLU A 1 2704 ? 167.578 112.651 161.100 1.00 53.85  ? 2704 GLU A C     1 
ATOM   11053 O  O     . GLU A 1 2704 ? 168.339 113.115 161.954 1.00 60.25  ? 2704 GLU A O     1 
ATOM   11054 C  CB    . GLU A 1 2704 ? 169.108 111.717 159.350 1.00 52.91  ? 2704 GLU A CB    1 
ATOM   11055 C  CG    . GLU A 1 2704 ? 168.719 110.253 159.444 1.00 55.65  ? 2704 GLU A CG    1 
ATOM   11056 C  CD    . GLU A 1 2704 ? 167.698 109.853 158.399 1.00 71.65  ? 2704 GLU A CD    1 
ATOM   11057 O  OE1   . GLU A 1 2704 ? 168.005 109.969 157.194 1.00 77.25  ? 2704 GLU A OE1   1 
ATOM   11058 O  OE2   . GLU A 1 2704 ? 166.591 109.420 158.781 1.00 76.08  ? 2704 GLU A OE2   1 
ATOM   11059 N  N     . ARG A 1 2705 ? 166.399 112.099 161.382 1.00 47.32  ? 2705 ARG A N     1 
ATOM   11060 C  CA    . ARG A 1 2705 ? 165.914 111.933 162.751 1.00 47.44  ? 2705 ARG A CA    1 
ATOM   11061 C  C     . ARG A 1 2705 ? 165.896 113.258 163.509 1.00 47.23  ? 2705 ARG A C     1 
ATOM   11062 O  O     . ARG A 1 2705 ? 166.300 113.334 164.671 1.00 52.26  ? 2705 ARG A O     1 
ATOM   11063 C  CB    . ARG A 1 2705 ? 166.744 110.890 163.500 1.00 48.19  ? 2705 ARG A CB    1 
ATOM   11064 C  CG    . ARG A 1 2705 ? 166.475 109.461 163.070 1.00 48.85  ? 2705 ARG A CG    1 
ATOM   11065 C  CD    . ARG A 1 2705 ? 167.271 108.478 163.906 1.00 52.59  ? 2705 ARG A CD    1 
ATOM   11066 N  NE    . ARG A 1 2705 ? 168.705 108.617 163.689 1.00 53.40  ? 2705 ARG A NE    1 
ATOM   11067 C  CZ    . ARG A 1 2705 ? 169.584 108.899 164.640 1.00 62.13  ? 2705 ARG A CZ    1 
ATOM   11068 N  NH1   . ARG A 1 2705 ? 169.208 109.089 165.894 1.00 67.89  ? 2705 ARG A NH1   1 
ATOM   11069 N  NH2   . ARG A 1 2705 ? 170.872 108.994 164.327 1.00 63.36  ? 2705 ARG A NH2   1 
ATOM   11070 N  N     . ILE A 1 2706 ? 165.432 114.316 162.848 1.00 40.64  ? 2706 ILE A N     1 
ATOM   11071 C  CA    . ILE A 1 2706 ? 165.317 115.637 163.455 1.00 38.89  ? 2706 ILE A CA    1 
ATOM   11072 C  C     . ILE A 1 2706 ? 163.921 116.178 163.179 1.00 41.69  ? 2706 ILE A C     1 
ATOM   11073 O  O     . ILE A 1 2706 ? 163.474 116.192 162.027 1.00 48.00  ? 2706 ILE A O     1 
ATOM   11074 C  CB    . ILE A 1 2706 ? 166.392 116.607 162.927 1.00 37.65  ? 2706 ILE A CB    1 
ATOM   11075 C  CG1   . ILE A 1 2706 ? 167.779 116.165 163.392 1.00 39.24  ? 2706 ILE A CG1   1 
ATOM   11076 C  CG2   . ILE A 1 2706 ? 166.110 118.022 163.393 1.00 37.55  ? 2706 ILE A CG2   1 
ATOM   11077 C  CD1   . ILE A 1 2706 ? 168.908 116.947 162.771 1.00 42.85  ? 2706 ILE A CD1   1 
ATOM   11078 N  N     . GLN A 1 2707 ? 163.238 116.621 164.231 1.00 37.13  ? 2707 GLN A N     1 
ATOM   11079 C  CA    . GLN A 1 2707 ? 161.896 117.175 164.144 1.00 35.03  ? 2707 GLN A CA    1 
ATOM   11080 C  C     . GLN A 1 2707 ? 161.894 118.612 164.646 1.00 38.45  ? 2707 GLN A C     1 
ATOM   11081 O  O     . GLN A 1 2707 ? 162.904 119.132 165.124 1.00 41.27  ? 2707 GLN A O     1 
ATOM   11082 C  CB    . GLN A 1 2707 ? 160.895 116.351 164.961 1.00 34.12  ? 2707 GLN A CB    1 
ATOM   11083 C  CG    . GLN A 1 2707 ? 160.828 114.893 164.591 1.00 40.16  ? 2707 GLN A CG    1 
ATOM   11084 C  CD    . GLN A 1 2707 ? 159.842 114.136 165.448 1.00 51.12  ? 2707 GLN A CD    1 
ATOM   11085 O  OE1   . GLN A 1 2707 ? 159.116 114.728 166.242 1.00 60.31  ? 2707 GLN A OE1   1 
ATOM   11086 N  NE2   . GLN A 1 2707 ? 159.821 112.818 165.306 1.00 58.60  ? 2707 GLN A NE2   1 
ATOM   11087 N  N     . PHE A 1 2708 ? 160.733 119.254 164.528 1.00 36.90  ? 2708 PHE A N     1 
ATOM   11088 C  CA    . PHE A 1 2708 ? 160.529 120.596 165.051 1.00 31.00  ? 2708 PHE A CA    1 
ATOM   11089 C  C     . PHE A 1 2708 ? 159.143 120.685 165.667 1.00 38.38  ? 2708 PHE A C     1 
ATOM   11090 O  O     . PHE A 1 2708 ? 158.174 120.160 165.113 1.00 41.20  ? 2708 PHE A O     1 
ATOM   11091 C  CB    . PHE A 1 2708 ? 160.683 121.664 163.962 1.00 32.84  ? 2708 PHE A CB    1 
ATOM   11092 C  CG    . PHE A 1 2708 ? 162.023 121.653 163.290 1.00 39.69  ? 2708 PHE A CG    1 
ATOM   11093 C  CD1   . PHE A 1 2708 ? 162.276 120.794 162.235 1.00 39.19  ? 2708 PHE A CD1   1 
ATOM   11094 C  CD2   . PHE A 1 2708 ? 163.037 122.487 163.724 1.00 39.63  ? 2708 PHE A CD2   1 
ATOM   11095 C  CE1   . PHE A 1 2708 ? 163.505 120.774 161.622 1.00 36.49  ? 2708 PHE A CE1   1 
ATOM   11096 C  CE2   . PHE A 1 2708 ? 164.268 122.470 163.113 1.00 35.83  ? 2708 PHE A CE2   1 
ATOM   11097 C  CZ    . PHE A 1 2708 ? 164.501 121.609 162.063 1.00 37.53  ? 2708 PHE A CZ    1 
ATOM   11098 N  N     . VAL A 1 2709 ? 159.061 121.337 166.823 1.00 37.93  ? 2709 VAL A N     1 
ATOM   11099 C  CA    . VAL A 1 2709 ? 157.801 121.612 167.505 1.00 28.29  ? 2709 VAL A CA    1 
ATOM   11100 C  C     . VAL A 1 2709 ? 157.861 123.042 168.021 1.00 33.20  ? 2709 VAL A C     1 
ATOM   11101 O  O     . VAL A 1 2709 ? 158.910 123.497 168.487 1.00 45.93  ? 2709 VAL A O     1 
ATOM   11102 C  CB    . VAL A 1 2709 ? 157.538 120.613 168.652 1.00 27.40  ? 2709 VAL A CB    1 
ATOM   11103 C  CG1   . VAL A 1 2709 ? 156.306 121.008 169.439 1.00 33.88  ? 2709 VAL A CG1   1 
ATOM   11104 C  CG2   . VAL A 1 2709 ? 157.348 119.220 168.098 1.00 31.89  ? 2709 VAL A CG2   1 
ATOM   11105 N  N     . GLY A 1 2710 ? 156.742 123.758 167.924 1.00 28.82  ? 2710 GLY A N     1 
ATOM   11106 C  CA    . GLY A 1 2710 ? 156.708 125.151 168.300 1.00 25.28  ? 2710 GLY A CA    1 
ATOM   11107 C  C     . GLY A 1 2710 ? 155.522 125.484 169.183 1.00 27.23  ? 2710 GLY A C     1 
ATOM   11108 O  O     . GLY A 1 2710 ? 154.490 124.812 169.174 1.00 33.28  ? 2710 GLY A O     1 
ATOM   11109 N  N     . ALA A 1 2711 ? 155.692 126.557 169.949 1.00 27.83  ? 2711 ALA A N     1 
ATOM   11110 C  CA    . ALA A 1 2711 ? 154.624 127.135 170.745 1.00 22.62  ? 2711 ALA A CA    1 
ATOM   11111 C  C     . ALA A 1 2711 ? 154.579 128.628 170.470 1.00 27.00  ? 2711 ALA A C     1 
ATOM   11112 O  O     . ALA A 1 2711 ? 155.596 129.245 170.148 1.00 34.33  ? 2711 ALA A O     1 
ATOM   11113 C  CB    . ALA A 1 2711 ? 154.816 126.870 172.242 1.00 26.46  ? 2711 ALA A CB    1 
ATOM   11114 N  N     . CYS A 1 2712 ? 153.385 129.201 170.571 1.00 28.53  ? 2712 CYS A N     1 
ATOM   11115 C  CA    . CYS A 1 2712 ? 153.202 130.609 170.257 1.00 31.90  ? 2712 CYS A CA    1 
ATOM   11116 C  C     . CYS A 1 2712 ? 152.115 131.200 171.136 1.00 39.39  ? 2712 CYS A C     1 
ATOM   11117 O  O     . CYS A 1 2712 ? 151.279 130.490 171.698 1.00 42.83  ? 2712 CYS A O     1 
ATOM   11118 C  CB    . CYS A 1 2712 ? 152.820 130.835 168.789 1.00 33.97  ? 2712 CYS A CB    1 
ATOM   11119 S  SG    . CYS A 1 2712 ? 153.813 129.984 167.564 1.00 65.08  ? 2712 CYS A SG    1 
ATOM   11120 N  N     . ASN A 1 2713 ? 152.147 132.506 171.241 1.00 42.23  ? 2713 ASN A N     1 
ATOM   11121 C  CA    . ASN A 1 2713 ? 151.043 133.334 171.676 1.00 40.31  ? 2713 ASN A CA    1 
ATOM   11122 C  C     . ASN A 1 2713 ? 150.349 133.908 170.452 1.00 42.42  ? 2713 ASN A C     1 
ATOM   11123 O  O     . ASN A 1 2713 ? 150.934 133.947 169.366 1.00 51.20  ? 2713 ASN A O     1 
ATOM   11124 C  CB    . ASN A 1 2713 ? 151.552 134.460 172.581 1.00 44.29  ? 2713 ASN A CB    1 
ATOM   11125 C  CG    . ASN A 1 2713 ? 151.800 133.994 173.999 1.00 40.76  ? 2713 ASN A CG    1 
ATOM   11126 O  OD1   . ASN A 1 2713 ? 152.930 134.015 174.482 1.00 46.32  ? 2713 ASN A OD1   1 
ATOM   11127 N  ND2   . ASN A 1 2713 ? 150.745 133.561 174.671 1.00 39.32  ? 2713 ASN A ND2   1 
ATOM   11128 N  N     . PRO A 1 2714 ? 149.095 134.337 170.568 1.00 45.06  ? 2714 PRO A N     1 
ATOM   11129 C  CA    . PRO A 1 2714 ? 148.371 134.823 169.389 1.00 51.40  ? 2714 PRO A CA    1 
ATOM   11130 C  C     . PRO A 1 2714 ? 149.123 135.954 168.712 1.00 57.58  ? 2714 PRO A C     1 
ATOM   11131 O  O     . PRO A 1 2714 ? 149.700 136.818 169.387 1.00 61.54  ? 2714 PRO A O     1 
ATOM   11132 C  CB    . PRO A 1 2714 ? 147.037 135.310 169.971 1.00 58.28  ? 2714 PRO A CB    1 
ATOM   11133 C  CG    . PRO A 1 2714 ? 146.852 134.488 171.187 1.00 55.39  ? 2714 PRO A CG    1 
ATOM   11134 C  CD    . PRO A 1 2714 ? 148.226 134.288 171.756 1.00 52.83  ? 2714 PRO A CD    1 
ATOM   11135 N  N     . PRO A 1 2715 ? 149.150 135.974 167.377 1.00 55.41  ? 2715 PRO A N     1 
ATOM   11136 C  CA    . PRO A 1 2715 ? 149.934 137.002 166.672 1.00 55.09  ? 2715 PRO A CA    1 
ATOM   11137 C  C     . PRO A 1 2715 ? 149.454 138.417 166.929 1.00 58.53  ? 2715 PRO A C     1 
ATOM   11138 O  O     . PRO A 1 2715 ? 150.205 139.364 166.670 1.00 58.25  ? 2715 PRO A O     1 
ATOM   11139 C  CB    . PRO A 1 2715 ? 149.774 136.614 165.196 1.00 55.79  ? 2715 PRO A CB    1 
ATOM   11140 C  CG    . PRO A 1 2715 ? 148.536 135.781 165.151 1.00 59.47  ? 2715 PRO A CG    1 
ATOM   11141 C  CD    . PRO A 1 2715 ? 148.500 135.038 166.447 1.00 53.68  ? 2715 PRO A CD    1 
ATOM   11142 N  N     . THR A 1 2716 ? 148.227 138.594 167.421 1.00 58.52  ? 2716 THR A N     1 
ATOM   11143 C  CA    . THR A 1 2716 ? 147.750 139.925 167.767 1.00 61.06  ? 2716 THR A CA    1 
ATOM   11144 C  C     . THR A 1 2716 ? 148.434 140.480 169.009 1.00 61.45  ? 2716 THR A C     1 
ATOM   11145 O  O     . THR A 1 2716 ? 148.358 141.689 169.254 1.00 62.16  ? 2716 THR A O     1 
ATOM   11146 C  CB    . THR A 1 2716 ? 146.237 139.902 167.980 1.00 65.37  ? 2716 THR A CB    1 
ATOM   11147 O  OG1   . THR A 1 2716 ? 145.930 139.123 169.143 1.00 65.35  ? 2716 THR A OG1   1 
ATOM   11148 C  CG2   . THR A 1 2716 ? 145.544 139.291 166.774 1.00 54.35  ? 2716 THR A CG2   1 
ATOM   11149 N  N     . ASP A 1 2717 ? 149.093 139.632 169.795 1.00 59.61  ? 2717 ASP A N     1 
ATOM   11150 C  CA    . ASP A 1 2717 ? 149.777 140.100 170.987 1.00 60.66  ? 2717 ASP A CA    1 
ATOM   11151 C  C     . ASP A 1 2717 ? 150.983 140.958 170.604 1.00 61.77  ? 2717 ASP A C     1 
ATOM   11152 O  O     . ASP A 1 2717 ? 151.571 140.773 169.536 1.00 63.59  ? 2717 ASP A O     1 
ATOM   11153 C  CB    . ASP A 1 2717 ? 150.227 138.921 171.843 1.00 56.72  ? 2717 ASP A CB    1 
ATOM   11154 C  CG    . ASP A 1 2717 ? 149.079 138.266 172.582 1.00 68.29  ? 2717 ASP A CG    1 
ATOM   11155 O  OD1   . ASP A 1 2717 ? 147.919 138.669 172.356 1.00 71.48  ? 2717 ASP A OD1   1 
ATOM   11156 O  OD2   . ASP A 1 2717 ? 149.336 137.354 173.395 1.00 67.06  ? 2717 ASP A OD2   1 
ATOM   11157 N  N     . PRO A 1 2718 ? 151.358 141.916 171.451 1.00 62.22  ? 2718 PRO A N     1 
ATOM   11158 C  CA    . PRO A 1 2718 ? 152.512 142.764 171.131 1.00 59.79  ? 2718 PRO A CA    1 
ATOM   11159 C  C     . PRO A 1 2718 ? 153.807 141.968 171.093 1.00 60.28  ? 2718 PRO A C     1 
ATOM   11160 O  O     . PRO A 1 2718 ? 154.077 141.138 171.965 1.00 60.40  ? 2718 PRO A O     1 
ATOM   11161 C  CB    . PRO A 1 2718 ? 152.521 143.794 172.268 1.00 60.34  ? 2718 PRO A CB    1 
ATOM   11162 C  CG    . PRO A 1 2718 ? 151.763 143.145 173.374 1.00 56.26  ? 2718 PRO A CG    1 
ATOM   11163 C  CD    . PRO A 1 2718 ? 150.711 142.317 172.711 1.00 59.90  ? 2718 PRO A CD    1 
ATOM   11164 N  N     . GLY A 1 2719 ? 154.615 142.237 170.069 1.00 57.09  ? 2719 GLY A N     1 
ATOM   11165 C  CA    . GLY A 1 2719 ? 155.891 141.583 169.897 1.00 52.82  ? 2719 GLY A CA    1 
ATOM   11166 C  C     . GLY A 1 2719 ? 155.863 140.311 169.077 1.00 55.46  ? 2719 GLY A C     1 
ATOM   11167 O  O     . GLY A 1 2719 ? 156.933 139.788 168.742 1.00 58.24  ? 2719 GLY A O     1 
ATOM   11168 N  N     . ARG A 1 2720 ? 154.683 139.801 168.735 1.00 52.45  ? 2720 ARG A N     1 
ATOM   11169 C  CA    . ARG A 1 2720 ? 154.551 138.575 167.961 1.00 46.12  ? 2720 ARG A CA    1 
ATOM   11170 C  C     . ARG A 1 2720 ? 154.243 138.919 166.511 1.00 48.55  ? 2720 ARG A C     1 
ATOM   11171 O  O     . ARG A 1 2720 ? 153.343 139.719 166.236 1.00 54.72  ? 2720 ARG A O     1 
ATOM   11172 C  CB    . ARG A 1 2720 ? 153.450 137.677 168.527 1.00 47.00  ? 2720 ARG A CB    1 
ATOM   11173 C  CG    . ARG A 1 2720 ? 153.100 137.935 169.977 1.00 51.67  ? 2720 ARG A CG    1 
ATOM   11174 C  CD    . ARG A 1 2720 ? 154.147 137.389 170.928 1.00 55.15  ? 2720 ARG A CD    1 
ATOM   11175 N  NE    . ARG A 1 2720 ? 153.804 137.681 172.314 1.00 63.13  ? 2720 ARG A NE    1 
ATOM   11176 C  CZ    . ARG A 1 2720 ? 154.552 137.357 173.359 1.00 61.91  ? 2720 ARG A CZ    1 
ATOM   11177 N  NH1   . ARG A 1 2720 ? 155.699 136.718 173.217 1.00 58.35  ? 2720 ARG A NH1   1 
ATOM   11178 N  NH2   . ARG A 1 2720 ? 154.135 137.681 174.580 1.00 61.67  ? 2720 ARG A NH2   1 
ATOM   11179 N  N     . LYS A 1 2721 ? 154.986 138.316 165.594 1.00 47.33  ? 2721 LYS A N     1 
ATOM   11180 C  CA    . LYS A 1 2721 ? 154.774 138.545 164.176 1.00 46.06  ? 2721 LYS A CA    1 
ATOM   11181 C  C     . LYS A 1 2721 ? 154.011 137.382 163.554 1.00 45.57  ? 2721 LYS A C     1 
ATOM   11182 O  O     . LYS A 1 2721 ? 154.186 136.229 163.957 1.00 48.52  ? 2721 LYS A O     1 
ATOM   11183 C  CB    . LYS A 1 2721 ? 156.108 138.721 163.445 1.00 43.28  ? 2721 LYS A CB    1 
ATOM   11184 C  CG    . LYS A 1 2721 ? 156.893 139.955 163.854 1.00 43.35  ? 2721 LYS A CG    1 
ATOM   11185 C  CD    . LYS A 1 2721 ? 157.838 139.660 165.002 1.00 47.89  ? 2721 LYS A CD    1 
ATOM   11186 C  CE    . LYS A 1 2721 ? 158.569 140.912 165.450 1.00 52.74  ? 2721 LYS A CE    1 
ATOM   11187 N  NZ    . LYS A 1 2721 ? 159.431 140.647 166.634 1.00 53.76  ? 2721 LYS A NZ    1 
ATOM   11188 N  N     . PRO A 1 2722 ? 153.149 137.653 162.576 1.00 44.27  ? 2722 PRO A N     1 
ATOM   11189 C  CA    . PRO A 1 2722 ? 152.448 136.559 161.898 1.00 43.25  ? 2722 PRO A CA    1 
ATOM   11190 C  C     . PRO A 1 2722 ? 153.406 135.731 161.058 1.00 44.22  ? 2722 PRO A C     1 
ATOM   11191 O  O     . PRO A 1 2722 ? 154.251 136.265 160.336 1.00 48.11  ? 2722 PRO A O     1 
ATOM   11192 C  CB    . PRO A 1 2722 ? 151.417 137.283 161.026 1.00 44.09  ? 2722 PRO A CB    1 
ATOM   11193 C  CG    . PRO A 1 2722 ? 152.002 138.631 160.804 1.00 44.89  ? 2722 PRO A CG    1 
ATOM   11194 C  CD    . PRO A 1 2722 ? 152.742 138.972 162.064 1.00 45.89  ? 2722 PRO A CD    1 
ATOM   11195 N  N     . LEU A 1 2723 ? 153.267 134.414 161.161 1.00 40.01  ? 2723 LEU A N     1 
ATOM   11196 C  CA    . LEU A 1 2723 ? 154.136 133.511 160.424 1.00 37.32  ? 2723 LEU A CA    1 
ATOM   11197 C  C     . LEU A 1 2723 ? 153.784 133.514 158.942 1.00 40.76  ? 2723 LEU A C     1 
ATOM   11198 O  O     . LEU A 1 2723 ? 152.639 133.754 158.551 1.00 42.53  ? 2723 LEU A O     1 
ATOM   11199 C  CB    . LEU A 1 2723 ? 154.029 132.096 160.987 1.00 37.05  ? 2723 LEU A CB    1 
ATOM   11200 C  CG    . LEU A 1 2723 ? 154.497 131.958 162.433 1.00 35.51  ? 2723 LEU A CG    1 
ATOM   11201 C  CD1   . LEU A 1 2723 ? 154.262 130.551 162.944 1.00 32.96  ? 2723 LEU A CD1   1 
ATOM   11202 C  CD2   . LEU A 1 2723 ? 155.960 132.334 162.535 1.00 35.93  ? 2723 LEU A CD2   1 
ATOM   11203 N  N     . SER A 1 2724 ? 154.790 133.249 158.115 1.00 38.27  ? 2724 SER A N     1 
ATOM   11204 C  CA    . SER A 1 2724 ? 154.588 133.216 156.676 1.00 37.20  ? 2724 SER A CA    1 
ATOM   11205 C  C     . SER A 1 2724 ? 153.690 132.049 156.287 1.00 37.56  ? 2724 SER A C     1 
ATOM   11206 O  O     . SER A 1 2724 ? 153.703 130.988 156.914 1.00 37.05  ? 2724 SER A O     1 
ATOM   11207 C  CB    . SER A 1 2724 ? 155.927 133.110 155.950 1.00 39.11  ? 2724 SER A CB    1 
ATOM   11208 O  OG    . SER A 1 2724 ? 156.561 131.878 156.235 1.00 43.80  ? 2724 SER A OG    1 
ATOM   11209 N  N     . HIS A 1 2725 ? 152.895 132.261 155.236 1.00 36.07  ? 2725 HIS A N     1 
ATOM   11210 C  CA    . HIS A 1 2725 ? 151.990 131.215 154.776 1.00 32.82  ? 2725 HIS A CA    1 
ATOM   11211 C  C     . HIS A 1 2725 ? 152.749 130.035 154.189 1.00 35.88  ? 2725 HIS A C     1 
ATOM   11212 O  O     . HIS A 1 2725 ? 152.255 128.903 154.226 1.00 38.98  ? 2725 HIS A O     1 
ATOM   11213 C  CB    . HIS A 1 2725 ? 151.012 131.782 153.752 1.00 39.94  ? 2725 HIS A CB    1 
ATOM   11214 C  CG    . HIS A 1 2725 ? 150.062 132.788 154.319 1.00 50.64  ? 2725 HIS A CG    1 
ATOM   11215 N  ND1   . HIS A 1 2725 ? 149.965 134.074 153.835 1.00 55.65  ? 2725 HIS A ND1   1 
ATOM   11216 C  CD2   . HIS A 1 2725 ? 149.169 132.699 155.332 1.00 55.52  ? 2725 HIS A CD2   1 
ATOM   11217 C  CE1   . HIS A 1 2725 ? 149.051 134.734 154.523 1.00 57.89  ? 2725 HIS A CE1   1 
ATOM   11218 N  NE2   . HIS A 1 2725 ? 148.553 133.922 155.437 1.00 59.62  ? 2725 HIS A NE2   1 
ATOM   11219 N  N     . ARG A 1 2726 ? 153.940 130.275 153.637 1.00 37.34  ? 2726 ARG A N     1 
ATOM   11220 C  CA    . ARG A 1 2726 ? 154.765 129.178 153.149 1.00 34.69  ? 2726 ARG A CA    1 
ATOM   11221 C  C     . ARG A 1 2726 ? 155.289 128.314 154.286 1.00 35.46  ? 2726 ARG A C     1 
ATOM   11222 O  O     . ARG A 1 2726 ? 155.632 127.149 154.058 1.00 41.08  ? 2726 ARG A O     1 
ATOM   11223 C  CB    . ARG A 1 2726 ? 155.925 129.724 152.316 1.00 38.31  ? 2726 ARG A CB    1 
ATOM   11224 C  CG    . ARG A 1 2726 ? 155.475 130.509 151.096 1.00 40.01  ? 2726 ARG A CG    1 
ATOM   11225 C  CD    . ARG A 1 2726 ? 156.556 131.451 150.590 1.00 48.22  ? 2726 ARG A CD    1 
ATOM   11226 N  NE    . ARG A 1 2726 ? 157.657 130.759 149.929 1.00 44.55  ? 2726 ARG A NE    1 
ATOM   11227 C  CZ    . ARG A 1 2726 ? 157.571 130.162 148.748 1.00 36.13  ? 2726 ARG A CZ    1 
ATOM   11228 N  NH1   . ARG A 1 2726 ? 156.441 130.144 148.062 1.00 41.04  ? 2726 ARG A NH1   1 
ATOM   11229 N  NH2   . ARG A 1 2726 ? 158.647 129.571 148.241 1.00 35.03  ? 2726 ARG A NH2   1 
ATOM   11230 N  N     . PHE A 1 2727 ? 155.360 128.856 155.501 1.00 32.20  ? 2727 PHE A N     1 
ATOM   11231 C  CA    . PHE A 1 2727 ? 155.733 128.080 156.676 1.00 26.06  ? 2727 PHE A CA    1 
ATOM   11232 C  C     . PHE A 1 2727 ? 154.523 127.450 157.350 1.00 28.47  ? 2727 PHE A C     1 
ATOM   11233 O  O     . PHE A 1 2727 ? 154.583 126.289 157.767 1.00 34.92  ? 2727 PHE A O     1 
ATOM   11234 C  CB    . PHE A 1 2727 ? 156.482 128.962 157.677 1.00 27.99  ? 2727 PHE A CB    1 
ATOM   11235 C  CG    . PHE A 1 2727 ? 156.788 128.277 158.977 1.00 30.39  ? 2727 PHE A CG    1 
ATOM   11236 C  CD1   . PHE A 1 2727 ? 157.585 127.147 159.008 1.00 28.52  ? 2727 PHE A CD1   1 
ATOM   11237 C  CD2   . PHE A 1 2727 ? 156.281 128.764 160.167 1.00 30.67  ? 2727 PHE A CD2   1 
ATOM   11238 C  CE1   . PHE A 1 2727 ? 157.868 126.517 160.200 1.00 27.06  ? 2727 PHE A CE1   1 
ATOM   11239 C  CE2   . PHE A 1 2727 ? 156.561 128.136 161.362 1.00 26.63  ? 2727 PHE A CE2   1 
ATOM   11240 C  CZ    . PHE A 1 2727 ? 157.356 127.014 161.378 1.00 29.54  ? 2727 PHE A CZ    1 
ATOM   11241 N  N     . LEU A 1 2728 ? 153.421 128.195 157.461 1.00 26.26  ? 2728 LEU A N     1 
ATOM   11242 C  CA    . LEU A 1 2728 ? 152.207 127.658 158.061 1.00 25.55  ? 2728 LEU A CA    1 
ATOM   11243 C  C     . LEU A 1 2728 ? 151.612 126.518 157.251 1.00 30.63  ? 2728 LEU A C     1 
ATOM   11244 O  O     . LEU A 1 2728 ? 150.799 125.758 157.784 1.00 35.12  ? 2728 LEU A O     1 
ATOM   11245 C  CB    . LEU A 1 2728 ? 151.166 128.765 158.229 1.00 26.68  ? 2728 LEU A CB    1 
ATOM   11246 C  CG    . LEU A 1 2728 ? 151.443 129.829 159.288 1.00 32.49  ? 2728 LEU A CG    1 
ATOM   11247 C  CD1   . LEU A 1 2728 ? 150.252 130.758 159.421 1.00 46.80  ? 2728 LEU A CD1   1 
ATOM   11248 C  CD2   . LEU A 1 2728 ? 151.754 129.178 160.618 1.00 26.63  ? 2728 LEU A CD2   1 
ATOM   11249 N  N     . ARG A 1 2729 ? 151.996 126.380 155.982 1.00 30.21  ? 2729 ARG A N     1 
ATOM   11250 C  CA    . ARG A 1 2729 ? 151.462 125.301 155.159 1.00 26.36  ? 2729 ARG A CA    1 
ATOM   11251 C  C     . ARG A 1 2729 ? 151.825 123.937 155.732 1.00 28.55  ? 2729 ARG A C     1 
ATOM   11252 O  O     . ARG A 1 2729 ? 151.016 123.003 155.696 1.00 31.69  ? 2729 ARG A O     1 
ATOM   11253 C  CB    . ARG A 1 2729 ? 151.974 125.440 153.727 1.00 31.18  ? 2729 ARG A CB    1 
ATOM   11254 C  CG    . ARG A 1 2729 ? 151.730 124.226 152.859 1.00 37.17  ? 2729 ARG A CG    1 
ATOM   11255 C  CD    . ARG A 1 2729 ? 151.692 124.591 151.389 1.00 35.50  ? 2729 ARG A CD    1 
ATOM   11256 N  NE    . ARG A 1 2729 ? 152.165 123.495 150.554 1.00 32.13  ? 2729 ARG A NE    1 
ATOM   11257 C  CZ    . ARG A 1 2729 ? 153.441 123.181 150.385 1.00 34.10  ? 2729 ARG A CZ    1 
ATOM   11258 N  NH1   . ARG A 1 2729 ? 154.406 123.889 150.945 1.00 34.48  ? 2729 ARG A NH1   1 
ATOM   11259 N  NH2   . ARG A 1 2729 ? 153.757 122.135 149.629 1.00 36.60  ? 2729 ARG A NH2   1 
ATOM   11260 N  N     . HIS A 1 2730 ? 153.033 123.805 156.273 1.00 28.21  ? 2730 HIS A N     1 
ATOM   11261 C  CA    . HIS A 1 2730 ? 153.496 122.531 156.804 1.00 28.98  ? 2730 HIS A CA    1 
ATOM   11262 C  C     . HIS A 1 2730 ? 153.125 122.318 158.263 1.00 28.03  ? 2730 HIS A C     1 
ATOM   11263 O  O     . HIS A 1 2730 ? 152.970 121.169 158.690 1.00 31.46  ? 2730 HIS A O     1 
ATOM   11264 C  CB    . HIS A 1 2730 ? 155.014 122.418 156.652 1.00 28.68  ? 2730 HIS A CB    1 
ATOM   11265 C  CG    . HIS A 1 2730 ? 155.506 122.733 155.276 1.00 32.45  ? 2730 HIS A CG    1 
ATOM   11266 N  ND1   . HIS A 1 2730 ? 156.083 123.940 154.950 1.00 35.13  ? 2730 HIS A ND1   1 
ATOM   11267 C  CD2   . HIS A 1 2730 ? 155.509 121.996 154.141 1.00 32.26  ? 2730 HIS A CD2   1 
ATOM   11268 C  CE1   . HIS A 1 2730 ? 156.418 123.935 153.673 1.00 39.40  ? 2730 HIS A CE1   1 
ATOM   11269 N  NE2   . HIS A 1 2730 ? 156.081 122.766 153.159 1.00 40.72  ? 2730 HIS A NE2   1 
ATOM   11270 N  N     . VAL A 1 2731 ? 152.984 123.382 159.039 1.00 28.08  ? 2731 VAL A N     1 
ATOM   11271 C  CA    . VAL A 1 2731 ? 152.761 123.231 160.477 1.00 30.39  ? 2731 VAL A CA    1 
ATOM   11272 C  C     . VAL A 1 2731 ? 151.270 123.024 160.734 1.00 30.62  ? 2731 VAL A C     1 
ATOM   11273 O  O     . VAL A 1 2731 ? 150.440 123.711 160.119 1.00 33.84  ? 2731 VAL A O     1 
ATOM   11274 C  CB    . VAL A 1 2731 ? 153.299 124.442 161.243 1.00 25.18  ? 2731 VAL A CB    1 
ATOM   11275 C  CG1   . VAL A 1 2731 ? 154.718 124.741 160.810 1.00 30.24  ? 2731 VAL A CG1   1 
ATOM   11276 C  CG2   . VAL A 1 2731 ? 152.433 125.664 161.055 1.00 24.07  ? 2731 VAL A CG2   1 
ATOM   11277 N  N     . PRO A 1 2732 ? 150.892 122.052 161.557 1.00 27.84  ? 2732 PRO A N     1 
ATOM   11278 C  CA    . PRO A 1 2732 ? 149.527 122.032 162.091 1.00 28.73  ? 2732 PRO A CA    1 
ATOM   11279 C  C     . PRO A 1 2732 ? 149.440 122.867 163.356 1.00 31.14  ? 2732 PRO A C     1 
ATOM   11280 O  O     . PRO A 1 2732 ? 150.181 122.621 164.310 1.00 34.43  ? 2732 PRO A O     1 
ATOM   11281 C  CB    . PRO A 1 2732 ? 149.274 120.544 162.373 1.00 29.73  ? 2732 PRO A CB    1 
ATOM   11282 C  CG    . PRO A 1 2732 ? 150.476 119.808 161.829 1.00 27.97  ? 2732 PRO A CG    1 
ATOM   11283 C  CD    . PRO A 1 2732 ? 151.593 120.787 161.812 1.00 27.60  ? 2732 PRO A CD    1 
ATOM   11284 N  N     . VAL A 1 2733 ? 148.550 123.853 163.382 1.00 34.49  ? 2733 VAL A N     1 
ATOM   11285 C  CA    . VAL A 1 2733 ? 148.429 124.776 164.503 1.00 30.38  ? 2733 VAL A CA    1 
ATOM   11286 C  C     . VAL A 1 2733 ? 147.189 124.405 165.303 1.00 31.64  ? 2733 VAL A C     1 
ATOM   11287 O  O     . VAL A 1 2733 ? 146.129 124.135 164.728 1.00 37.93  ? 2733 VAL A O     1 
ATOM   11288 C  CB    . VAL A 1 2733 ? 148.367 126.237 164.029 1.00 29.94  ? 2733 VAL A CB    1 
ATOM   11289 C  CG1   . VAL A 1 2733 ? 148.511 127.180 165.206 1.00 30.32  ? 2733 VAL A CG1   1 
ATOM   11290 C  CG2   . VAL A 1 2733 ? 149.442 126.505 162.997 1.00 36.20  ? 2733 VAL A CG2   1 
ATOM   11291 N  N     . VAL A 1 2734 ? 147.330 124.372 166.625 1.00 29.61  ? 2734 VAL A N     1 
ATOM   11292 C  CA    . VAL A 1 2734 ? 146.242 124.043 167.538 1.00 34.23  ? 2734 VAL A CA    1 
ATOM   11293 C  C     . VAL A 1 2734 ? 146.116 125.162 168.560 1.00 32.39  ? 2734 VAL A C     1 
ATOM   11294 O  O     . VAL A 1 2734 ? 147.118 125.599 169.135 1.00 33.38  ? 2734 VAL A O     1 
ATOM   11295 C  CB    . VAL A 1 2734 ? 146.474 122.692 168.235 1.00 32.71  ? 2734 VAL A CB    1 
ATOM   11296 C  CG1   . VAL A 1 2734 ? 145.492 122.499 169.377 1.00 35.24  ? 2734 VAL A CG1   1 
ATOM   11297 C  CG2   . VAL A 1 2734 ? 146.347 121.570 167.243 1.00 37.56  ? 2734 VAL A CG2   1 
ATOM   11298 N  N     . TYR A 1 2735 ? 144.889 125.622 168.781 1.00 34.45  ? 2735 TYR A N     1 
ATOM   11299 C  CA    . TYR A 1 2735 ? 144.627 126.677 169.751 1.00 34.84  ? 2735 TYR A CA    1 
ATOM   11300 C  C     . TYR A 1 2735 ? 144.475 126.054 171.132 1.00 39.67  ? 2735 TYR A C     1 
ATOM   11301 O  O     . TYR A 1 2735 ? 143.473 125.391 171.414 1.00 43.64  ? 2735 TYR A O     1 
ATOM   11302 C  CB    . TYR A 1 2735 ? 143.375 127.457 169.366 1.00 37.98  ? 2735 TYR A CB    1 
ATOM   11303 C  CG    . TYR A 1 2735 ? 143.136 128.676 170.219 1.00 39.86  ? 2735 TYR A CG    1 
ATOM   11304 C  CD1   . TYR A 1 2735 ? 143.960 129.784 170.120 1.00 43.68  ? 2735 TYR A CD1   1 
ATOM   11305 C  CD2   . TYR A 1 2735 ? 142.093 128.715 171.129 1.00 39.35  ? 2735 TYR A CD2   1 
ATOM   11306 C  CE1   . TYR A 1 2735 ? 143.749 130.900 170.896 1.00 46.19  ? 2735 TYR A CE1   1 
ATOM   11307 C  CE2   . TYR A 1 2735 ? 141.877 129.825 171.912 1.00 43.30  ? 2735 TYR A CE2   1 
ATOM   11308 C  CZ    . TYR A 1 2735 ? 142.706 130.916 171.791 1.00 46.89  ? 2735 TYR A CZ    1 
ATOM   11309 O  OH    . TYR A 1 2735 ? 142.490 132.028 172.570 1.00 52.32  ? 2735 TYR A OH    1 
ATOM   11310 N  N     . VAL A 1 2736 ? 145.469 126.261 171.993 1.00 36.31  ? 2736 VAL A N     1 
ATOM   11311 C  CA    . VAL A 1 2736 ? 145.415 125.779 173.374 1.00 32.50  ? 2736 VAL A CA    1 
ATOM   11312 C  C     . VAL A 1 2736 ? 144.761 126.892 174.187 1.00 39.69  ? 2736 VAL A C     1 
ATOM   11313 O  O     . VAL A 1 2736 ? 145.415 127.829 174.642 1.00 44.15  ? 2736 VAL A O     1 
ATOM   11314 C  CB    . VAL A 1 2736 ? 146.794 125.401 173.906 1.00 27.70  ? 2736 VAL A CB    1 
ATOM   11315 C  CG1   . VAL A 1 2736 ? 146.685 124.869 175.322 1.00 31.44  ? 2736 VAL A CG1   1 
ATOM   11316 C  CG2   . VAL A 1 2736 ? 147.436 124.371 173.009 1.00 27.45  ? 2736 VAL A CG2   1 
ATOM   11317 N  N     . ASP A 1 2737 ? 143.448 126.789 174.361 1.00 40.50  ? 2737 ASP A N     1 
ATOM   11318 C  CA    . ASP A 1 2737 ? 142.708 127.763 175.144 1.00 41.11  ? 2737 ASP A CA    1 
ATOM   11319 C  C     . ASP A 1 2737 ? 142.847 127.444 176.631 1.00 46.32  ? 2737 ASP A C     1 
ATOM   11320 O  O     . ASP A 1 2737 ? 143.448 126.442 177.026 1.00 53.16  ? 2737 ASP A O     1 
ATOM   11321 C  CB    . ASP A 1 2737 ? 141.244 127.784 174.712 1.00 47.69  ? 2737 ASP A CB    1 
ATOM   11322 C  CG    . ASP A 1 2737 ? 140.560 129.098 175.033 1.00 59.64  ? 2737 ASP A CG    1 
ATOM   11323 O  OD1   . ASP A 1 2737 ? 141.223 129.990 175.602 1.00 56.98  ? 2737 ASP A OD1   1 
ATOM   11324 O  OD2   . ASP A 1 2737 ? 139.361 129.239 174.715 1.00 61.96  ? 2737 ASP A OD2   1 
ATOM   11325 N  N     . TYR A 1 2738 ? 142.287 128.311 177.470 1.00 43.12  ? 2738 TYR A N     1 
ATOM   11326 C  CA    . TYR A 1 2738 ? 142.346 128.095 178.904 1.00 42.03  ? 2738 TYR A CA    1 
ATOM   11327 C  C     . TYR A 1 2738 ? 141.564 126.838 179.282 1.00 44.95  ? 2738 TYR A C     1 
ATOM   11328 O  O     . TYR A 1 2738 ? 140.556 126.511 178.651 1.00 51.72  ? 2738 TYR A O     1 
ATOM   11329 C  CB    . TYR A 1 2738 ? 141.796 129.306 179.649 1.00 46.30  ? 2738 TYR A CB    1 
ATOM   11330 C  CG    . TYR A 1 2738 ? 142.707 130.510 179.593 1.00 40.21  ? 2738 TYR A CG    1 
ATOM   11331 C  CD1   . TYR A 1 2738 ? 144.064 130.388 179.852 1.00 36.75  ? 2738 TYR A CD1   1 
ATOM   11332 C  CD2   . TYR A 1 2738 ? 142.213 131.766 179.275 1.00 37.87  ? 2738 TYR A CD2   1 
ATOM   11333 C  CE1   . TYR A 1 2738 ? 144.900 131.481 179.801 1.00 35.19  ? 2738 TYR A CE1   1 
ATOM   11334 C  CE2   . TYR A 1 2738 ? 143.044 132.865 179.221 1.00 36.34  ? 2738 TYR A CE2   1 
ATOM   11335 C  CZ    . TYR A 1 2738 ? 144.386 132.716 179.485 1.00 38.03  ? 2738 TYR A CZ    1 
ATOM   11336 O  OH    . TYR A 1 2738 ? 145.217 133.809 179.432 1.00 45.18  ? 2738 TYR A OH    1 
ATOM   11337 N  N     . PRO A 1 2739 ? 142.022 126.109 180.305 1.00 42.31  ? 2739 PRO A N     1 
ATOM   11338 C  CA    . PRO A 1 2739 ? 141.422 124.796 180.602 1.00 50.25  ? 2739 PRO A CA    1 
ATOM   11339 C  C     . PRO A 1 2739 ? 139.926 124.827 180.873 1.00 51.88  ? 2739 PRO A C     1 
ATOM   11340 O  O     . PRO A 1 2739 ? 139.214 123.906 180.455 1.00 59.83  ? 2739 PRO A O     1 
ATOM   11341 C  CB    . PRO A 1 2739 ? 142.214 124.324 181.834 1.00 46.46  ? 2739 PRO A CB    1 
ATOM   11342 C  CG    . PRO A 1 2739 ? 143.034 125.489 182.276 1.00 39.14  ? 2739 PRO A CG    1 
ATOM   11343 C  CD    . PRO A 1 2739 ? 143.248 126.339 181.080 1.00 40.32  ? 2739 PRO A CD    1 
ATOM   11344 N  N     . GLY A 1 2740 ? 139.422 125.849 181.555 1.00 44.23  ? 2740 GLY A N     1 
ATOM   11345 C  CA    . GLY A 1 2740 ? 138.012 125.920 181.860 1.00 45.34  ? 2740 GLY A CA    1 
ATOM   11346 C  C     . GLY A 1 2740 ? 137.684 125.372 183.234 1.00 46.40  ? 2740 GLY A C     1 
ATOM   11347 O  O     . GLY A 1 2740 ? 138.514 124.731 183.885 1.00 47.99  ? 2740 GLY A O     1 
ATOM   11348 N  N     . PRO A 1 2741 ? 136.452 125.608 183.695 1.00 47.56  ? 2741 PRO A N     1 
ATOM   11349 C  CA    . PRO A 1 2741 ? 136.124 125.300 185.101 1.00 47.86  ? 2741 PRO A CA    1 
ATOM   11350 C  C     . PRO A 1 2741 ? 136.344 123.849 185.501 1.00 47.82  ? 2741 PRO A C     1 
ATOM   11351 O  O     . PRO A 1 2741 ? 136.832 123.589 186.605 1.00 50.28  ? 2741 PRO A O     1 
ATOM   11352 C  CB    . PRO A 1 2741 ? 134.646 125.703 185.201 1.00 50.56  ? 2741 PRO A CB    1 
ATOM   11353 C  CG    . PRO A 1 2741 ? 134.455 126.711 184.120 1.00 57.16  ? 2741 PRO A CG    1 
ATOM   11354 C  CD    . PRO A 1 2741 ? 135.336 126.264 182.996 1.00 55.16  ? 2741 PRO A CD    1 
ATOM   11355 N  N     . ALA A 1 2742 ? 136.009 122.892 184.635 1.00 47.59  ? 2742 ALA A N     1 
ATOM   11356 C  CA    . ALA A 1 2742 ? 136.156 121.487 185.008 1.00 47.62  ? 2742 ALA A CA    1 
ATOM   11357 C  C     . ALA A 1 2742 ? 137.621 121.067 185.035 1.00 46.96  ? 2742 ALA A C     1 
ATOM   11358 O  O     . ALA A 1 2742 ? 138.063 120.389 185.972 1.00 48.88  ? 2742 ALA A O     1 
ATOM   11359 C  CB    . ALA A 1 2742 ? 135.361 120.603 184.050 1.00 53.45  ? 2742 ALA A CB    1 
ATOM   11360 N  N     . SER A 1 2743 ? 138.387 121.454 184.014 1.00 48.59  ? 2743 SER A N     1 
ATOM   11361 C  CA    . SER A 1 2743 ? 139.804 121.112 183.984 1.00 47.15  ? 2743 SER A CA    1 
ATOM   11362 C  C     . SER A 1 2743 ? 140.564 121.797 185.113 1.00 47.77  ? 2743 SER A C     1 
ATOM   11363 O  O     . SER A 1 2743 ? 141.415 121.175 185.761 1.00 50.63  ? 2743 SER A O     1 
ATOM   11364 C  CB    . SER A 1 2743 ? 140.399 121.483 182.628 1.00 48.41  ? 2743 SER A CB    1 
ATOM   11365 O  OG    . SER A 1 2743 ? 139.731 120.809 181.577 1.00 58.33  ? 2743 SER A OG    1 
ATOM   11366 N  N     . LEU A 1 2744 ? 140.273 123.077 185.361 1.00 45.17  ? 2744 LEU A N     1 
ATOM   11367 C  CA    . LEU A 1 2744 ? 140.878 123.766 186.495 1.00 38.69  ? 2744 LEU A CA    1 
ATOM   11368 C  C     . LEU A 1 2744 ? 140.496 123.095 187.804 1.00 40.49  ? 2744 LEU A C     1 
ATOM   11369 O  O     . LEU A 1 2744 ? 141.338 122.923 188.693 1.00 48.57  ? 2744 LEU A O     1 
ATOM   11370 C  CB    . LEU A 1 2744 ? 140.455 125.234 186.515 1.00 32.80  ? 2744 LEU A CB    1 
ATOM   11371 C  CG    . LEU A 1 2744 ? 140.941 126.152 185.398 1.00 35.48  ? 2744 LEU A CG    1 
ATOM   11372 C  CD1   . LEU A 1 2744 ? 140.007 127.336 185.275 1.00 38.06  ? 2744 LEU A CD1   1 
ATOM   11373 C  CD2   . LEU A 1 2744 ? 142.354 126.618 185.661 1.00 35.06  ? 2744 LEU A CD2   1 
ATOM   11374 N  N     . THR A 1 2745 ? 139.226 122.708 187.940 1.00 36.45  ? 2745 THR A N     1 
ATOM   11375 C  CA    . THR A 1 2745 ? 138.786 122.039 189.155 1.00 36.55  ? 2745 THR A CA    1 
ATOM   11376 C  C     . THR A 1 2745 ? 139.566 120.755 189.381 1.00 40.68  ? 2745 THR A C     1 
ATOM   11377 O  O     . THR A 1 2745 ? 140.033 120.500 190.490 1.00 48.17  ? 2745 THR A O     1 
ATOM   11378 C  CB    . THR A 1 2745 ? 137.288 121.752 189.092 1.00 38.26  ? 2745 THR A CB    1 
ATOM   11379 O  OG1   . THR A 1 2745 ? 136.572 122.979 188.910 1.00 43.77  ? 2745 THR A OG1   1 
ATOM   11380 C  CG2   . THR A 1 2745 ? 136.821 121.093 190.378 1.00 34.10  ? 2745 THR A CG2   1 
ATOM   11381 N  N     . GLN A 1 2746 ? 139.760 119.956 188.331 1.00 44.02  ? 2746 GLN A N     1 
ATOM   11382 C  CA    . GLN A 1 2746 ? 140.513 118.713 188.491 1.00 46.79  ? 2746 GLN A CA    1 
ATOM   11383 C  C     . GLN A 1 2746 ? 141.972 118.983 188.845 1.00 46.26  ? 2746 GLN A C     1 
ATOM   11384 O  O     . GLN A 1 2746 ? 142.504 118.417 189.813 1.00 56.90  ? 2746 GLN A O     1 
ATOM   11385 C  CB    . GLN A 1 2746 ? 140.423 117.873 187.220 1.00 49.18  ? 2746 GLN A CB    1 
ATOM   11386 C  CG    . GLN A 1 2746 ? 141.170 116.559 187.328 1.00 61.57  ? 2746 GLN A CG    1 
ATOM   11387 C  CD    . GLN A 1 2746 ? 141.030 115.702 186.093 1.00 68.29  ? 2746 GLN A CD    1 
ATOM   11388 O  OE1   . GLN A 1 2746 ? 141.585 114.607 186.022 1.00 72.73  ? 2746 GLN A OE1   1 
ATOM   11389 N  NE2   . GLN A 1 2746 ? 140.284 116.194 185.112 1.00 67.76  ? 2746 GLN A NE2   1 
ATOM   11390 N  N     . ILE A 1 2747 ? 142.633 119.854 188.075 1.00 40.89  ? 2747 ILE A N     1 
ATOM   11391 C  CA    . ILE A 1 2747 ? 144.057 120.112 188.280 1.00 42.88  ? 2747 ILE A CA    1 
ATOM   11392 C  C     . ILE A 1 2747 ? 144.306 120.619 189.692 1.00 44.45  ? 2747 ILE A C     1 
ATOM   11393 O  O     . ILE A 1 2747 ? 145.150 120.093 190.432 1.00 46.02  ? 2747 ILE A O     1 
ATOM   11394 C  CB    . ILE A 1 2747 ? 144.577 121.116 187.236 1.00 39.24  ? 2747 ILE A CB    1 
ATOM   11395 C  CG1   . ILE A 1 2747 ? 144.461 120.546 185.826 1.00 49.16  ? 2747 ILE A CG1   1 
ATOM   11396 C  CG2   . ILE A 1 2747 ? 146.012 121.494 187.534 1.00 42.10  ? 2747 ILE A CG2   1 
ATOM   11397 C  CD1   . ILE A 1 2747 ? 144.587 121.592 184.749 1.00 45.43  ? 2747 ILE A CD1   1 
ATOM   11398 N  N     . TYR A 1 2748 ? 143.554 121.632 190.104 1.00 42.49  ? 2748 TYR A N     1 
ATOM   11399 C  CA    . TYR A 1 2748 ? 143.835 122.231 191.393 1.00 40.89  ? 2748 TYR A CA    1 
ATOM   11400 C  C     . TYR A 1 2748 ? 143.152 121.510 192.542 1.00 44.78  ? 2748 TYR A C     1 
ATOM   11401 O  O     . TYR A 1 2748 ? 143.545 121.723 193.685 1.00 53.73  ? 2748 TYR A O     1 
ATOM   11402 C  CB    . TYR A 1 2748 ? 143.476 123.712 191.342 1.00 35.85  ? 2748 TYR A CB    1 
ATOM   11403 C  CG    . TYR A 1 2748 ? 144.307 124.405 190.289 1.00 37.82  ? 2748 TYR A CG    1 
ATOM   11404 C  CD1   . TYR A 1 2748 ? 145.659 124.637 190.490 1.00 37.72  ? 2748 TYR A CD1   1 
ATOM   11405 C  CD2   . TYR A 1 2748 ? 143.759 124.762 189.070 1.00 38.93  ? 2748 TYR A CD2   1 
ATOM   11406 C  CE1   . TYR A 1 2748 ? 146.427 125.245 189.521 1.00 31.34  ? 2748 TYR A CE1   1 
ATOM   11407 C  CE2   . TYR A 1 2748 ? 144.518 125.371 188.100 1.00 38.19  ? 2748 TYR A CE2   1 
ATOM   11408 C  CZ    . TYR A 1 2748 ? 145.849 125.608 188.327 1.00 33.30  ? 2748 TYR A CZ    1 
ATOM   11409 O  OH    . TYR A 1 2748 ? 146.599 126.214 187.351 1.00 31.33  ? 2748 TYR A OH    1 
ATOM   11410 N  N     . GLY A 1 2749 ? 142.213 120.600 192.277 1.00 41.05  ? 2749 GLY A N     1 
ATOM   11411 C  CA    . GLY A 1 2749 ? 141.818 119.656 193.303 1.00 42.82  ? 2749 GLY A CA    1 
ATOM   11412 C  C     . GLY A 1 2749 ? 142.932 118.685 193.626 1.00 50.79  ? 2749 GLY A C     1 
ATOM   11413 O  O     . GLY A 1 2749 ? 143.197 118.399 194.797 1.00 58.18  ? 2749 GLY A O     1 
ATOM   11414 N  N     . THR A 1 2750 ? 143.615 118.178 192.595 1.00 49.57  ? 2750 THR A N     1 
ATOM   11415 C  CA    . THR A 1 2750 ? 144.792 117.350 192.845 1.00 53.42  ? 2750 THR A CA    1 
ATOM   11416 C  C     . THR A 1 2750 ? 145.861 118.138 193.591 1.00 51.63  ? 2750 THR A C     1 
ATOM   11417 O  O     . THR A 1 2750 ? 146.453 117.643 194.563 1.00 55.30  ? 2750 THR A O     1 
ATOM   11418 C  CB    . THR A 1 2750 ? 145.355 116.813 191.530 1.00 55.52  ? 2750 THR A CB    1 
ATOM   11419 O  OG1   . THR A 1 2750 ? 145.705 117.908 190.678 1.00 53.68  ? 2750 THR A OG1   1 
ATOM   11420 C  CG2   . THR A 1 2750 ? 144.331 115.945 190.824 1.00 62.01  ? 2750 THR A CG2   1 
ATOM   11421 N  N     . PHE A 1 2751 ? 146.109 119.378 193.160 1.00 48.45  ? 2751 PHE A N     1 
ATOM   11422 C  CA    . PHE A 1 2751 ? 147.111 120.204 193.825 1.00 46.51  ? 2751 PHE A CA    1 
ATOM   11423 C  C     . PHE A 1 2751 ? 146.731 120.491 195.275 1.00 50.37  ? 2751 PHE A C     1 
ATOM   11424 O  O     . PHE A 1 2751 ? 147.587 120.453 196.164 1.00 55.79  ? 2751 PHE A O     1 
ATOM   11425 C  CB    . PHE A 1 2751 ? 147.315 121.508 193.057 1.00 41.91  ? 2751 PHE A CB    1 
ATOM   11426 C  CG    . PHE A 1 2751 ? 148.164 121.361 191.830 1.00 41.68  ? 2751 PHE A CG    1 
ATOM   11427 C  CD1   . PHE A 1 2751 ? 148.760 120.152 191.525 1.00 47.67  ? 2751 PHE A CD1   1 
ATOM   11428 C  CD2   . PHE A 1 2751 ? 148.369 122.434 190.983 1.00 45.12  ? 2751 PHE A CD2   1 
ATOM   11429 C  CE1   . PHE A 1 2751 ? 149.542 120.015 190.397 1.00 51.80  ? 2751 PHE A CE1   1 
ATOM   11430 C  CE2   . PHE A 1 2751 ? 149.150 122.302 189.854 1.00 48.75  ? 2751 PHE A CE2   1 
ATOM   11431 C  CZ    . PHE A 1 2751 ? 149.738 121.091 189.562 1.00 49.39  ? 2751 PHE A CZ    1 
ATOM   11432 N  N     . ASN A 1 2752 ? 145.453 120.775 195.536 1.00 49.53  ? 2752 ASN A N     1 
ATOM   11433 C  CA    . ASN A 1 2752 ? 145.017 121.073 196.895 1.00 46.86  ? 2752 ASN A CA    1 
ATOM   11434 C  C     . ASN A 1 2752 ? 145.071 119.839 197.782 1.00 54.63  ? 2752 ASN A C     1 
ATOM   11435 O  O     . ASN A 1 2752 ? 145.386 119.945 198.969 1.00 64.18  ? 2752 ASN A O     1 
ATOM   11436 C  CB    . ASN A 1 2752 ? 143.607 121.659 196.879 1.00 44.42  ? 2752 ASN A CB    1 
ATOM   11437 C  CG    . ASN A 1 2752 ? 143.572 123.079 196.354 1.00 49.27  ? 2752 ASN A CG    1 
ATOM   11438 O  OD1   . ASN A 1 2752 ? 142.517 123.707 196.303 1.00 53.77  ? 2752 ASN A OD1   1 
ATOM   11439 N  ND2   . ASN A 1 2752 ? 144.730 123.594 195.961 1.00 49.64  ? 2752 ASN A ND2   1 
ATOM   11440 N  N     . ARG A 1 2753 ? 144.753 118.663 197.238 1.00 54.83  ? 2753 ARG A N     1 
ATOM   11441 C  CA    . ARG A 1 2753 ? 144.910 117.442 198.021 1.00 56.14  ? 2753 ARG A CA    1 
ATOM   11442 C  C     . ARG A 1 2753 ? 146.372 117.206 198.377 1.00 61.24  ? 2753 ARG A C     1 
ATOM   11443 O  O     . ARG A 1 2753 ? 146.692 116.861 199.523 1.00 69.57  ? 2753 ARG A O     1 
ATOM   11444 C  CB    . ARG A 1 2753 ? 144.341 116.247 197.259 1.00 63.18  ? 2753 ARG A CB    1 
ATOM   11445 C  CG    . ARG A 1 2753 ? 142.827 116.236 197.162 1.00 60.71  ? 2753 ARG A CG    1 
ATOM   11446 C  CD    . ARG A 1 2753 ? 142.315 114.844 196.840 1.00 61.01  ? 2753 ARG A CD    1 
ATOM   11447 N  NE    . ARG A 1 2753 ? 142.795 114.369 195.549 1.00 64.39  ? 2753 ARG A NE    1 
ATOM   11448 C  CZ    . ARG A 1 2753 ? 142.353 114.801 194.376 1.00 66.70  ? 2753 ARG A CZ    1 
ATOM   11449 N  NH1   . ARG A 1 2753 ? 141.397 115.711 194.289 1.00 65.09  ? 2753 ARG A NH1   1 
ATOM   11450 N  NH2   . ARG A 1 2753 ? 142.879 114.303 193.261 1.00 69.05  ? 2753 ARG A NH2   1 
ATOM   11451 N  N     . ALA A 1 2754 ? 147.277 117.408 197.415 1.00 56.50  ? 2754 ALA A N     1 
ATOM   11452 C  CA    . ALA A 1 2754 ? 148.700 117.266 197.708 1.00 64.90  ? 2754 ALA A CA    1 
ATOM   11453 C  C     . ALA A 1 2754 ? 149.154 118.278 198.755 1.00 70.29  ? 2754 ALA A C     1 
ATOM   11454 O  O     . ALA A 1 2754 ? 149.954 117.951 199.639 1.00 76.14  ? 2754 ALA A O     1 
ATOM   11455 C  CB    . ALA A 1 2754 ? 149.517 117.417 196.427 1.00 70.87  ? 2754 ALA A CB    1 
ATOM   11456 N  N     . MET A 1 2755 ? 148.659 119.513 198.661 1.00 67.41  ? 2755 MET A N     1 
ATOM   11457 C  CA    . MET A 1 2755 ? 149.015 120.555 199.618 1.00 62.98  ? 2755 MET A CA    1 
ATOM   11458 C  C     . MET A 1 2755 ? 148.480 120.263 201.014 1.00 65.23  ? 2755 MET A C     1 
ATOM   11459 O  O     . MET A 1 2755 ? 149.191 120.471 202.004 1.00 73.71  ? 2755 MET A O     1 
ATOM   11460 C  CB    . MET A 1 2755 ? 148.487 121.898 199.122 1.00 58.42  ? 2755 MET A CB    1 
ATOM   11461 C  CG    . MET A 1 2755 ? 148.802 123.077 200.009 1.00 55.68  ? 2755 MET A CG    1 
ATOM   11462 S  SD    . MET A 1 2755 ? 148.121 124.582 199.298 1.00 69.15  ? 2755 MET A SD    1 
ATOM   11463 C  CE    . MET A 1 2755 ? 146.373 124.298 199.558 1.00 51.41  ? 2755 MET A CE    1 
ATOM   11464 N  N     . LEU A 1 2756 ? 147.243 119.791 201.117 1.00 63.50  ? 2756 LEU A N     1 
ATOM   11465 C  CA    . LEU A 1 2756 ? 146.598 119.537 202.396 1.00 68.76  ? 2756 LEU A CA    1 
ATOM   11466 C  C     . LEU A 1 2756 ? 146.929 118.166 202.961 1.00 76.83  ? 2756 LEU A C     1 
ATOM   11467 O  O     . LEU A 1 2756 ? 146.457 117.833 204.053 1.00 79.74  ? 2756 LEU A O     1 
ATOM   11468 C  CB    . LEU A 1 2756 ? 145.080 119.687 202.260 1.00 64.67  ? 2756 LEU A CB    1 
ATOM   11469 C  CG    . LEU A 1 2756 ? 144.577 121.107 201.997 1.00 60.52  ? 2756 LEU A CG    1 
ATOM   11470 C  CD1   . LEU A 1 2756 ? 143.065 121.159 202.054 1.00 66.90  ? 2756 LEU A CD1   1 
ATOM   11471 C  CD2   . LEU A 1 2756 ? 145.182 122.080 202.987 1.00 68.66  ? 2756 LEU A CD2   1 
ATOM   11472 N  N     . ARG A 1 2757 ? 147.716 117.359 202.246 1.00 75.86  ? 2757 ARG A N     1 
ATOM   11473 C  CA    . ARG A 1 2757 ? 148.234 116.135 202.844 1.00 79.22  ? 2757 ARG A CA    1 
ATOM   11474 C  C     . ARG A 1 2757 ? 149.125 116.419 204.048 1.00 85.84  ? 2757 ARG A C     1 
ATOM   11475 O  O     . ARG A 1 2757 ? 149.334 115.523 204.873 1.00 91.23  ? 2757 ARG A O     1 
ATOM   11476 C  CB    . ARG A 1 2757 ? 149.006 115.322 201.804 1.00 78.72  ? 2757 ARG A CB    1 
ATOM   11477 C  CG    . ARG A 1 2757 ? 148.852 113.819 201.961 1.00 79.21  ? 2757 ARG A CG    1 
ATOM   11478 C  CD    . ARG A 1 2757 ? 149.827 113.062 201.070 1.00 82.61  ? 2757 ARG A CD    1 
ATOM   11479 N  NE    . ARG A 1 2757 ? 149.770 113.504 199.682 1.00 84.68  ? 2757 ARG A NE    1 
ATOM   11480 C  CZ    . ARG A 1 2757 ? 148.772 113.243 198.848 1.00 83.60  ? 2757 ARG A CZ    1 
ATOM   11481 N  NH1   . ARG A 1 2757 ? 147.724 112.528 199.224 1.00 86.41  ? 2757 ARG A NH1   1 
ATOM   11482 N  NH2   . ARG A 1 2757 ? 148.829 113.708 197.604 1.00 82.18  ? 2757 ARG A NH2   1 
ATOM   11483 N  N     . LEU A 1 2758 ? 149.656 117.640 204.162 1.00 85.48  ? 2758 LEU A N     1 
ATOM   11484 C  CA    . LEU A 1 2758 ? 150.446 118.007 205.334 1.00 90.00  ? 2758 LEU A CA    1 
ATOM   11485 C  C     . LEU A 1 2758 ? 149.602 117.995 206.603 1.00 94.45  ? 2758 LEU A C     1 
ATOM   11486 O  O     . LEU A 1 2758 ? 150.045 117.501 207.646 1.00 96.48  ? 2758 LEU A O     1 
ATOM   11487 C  CB    . LEU A 1 2758 ? 151.073 119.386 205.135 1.00 81.77  ? 2758 LEU A CB    1 
ATOM   11488 C  CG    . LEU A 1 2758 ? 151.810 119.647 203.823 1.00 83.08  ? 2758 LEU A CG    1 
ATOM   11489 C  CD1   . LEU A 1 2758 ? 152.374 121.056 203.810 1.00 74.52  ? 2758 LEU A CD1   1 
ATOM   11490 C  CD2   . LEU A 1 2758 ? 152.914 118.626 203.624 1.00 89.22  ? 2758 LEU A CD2   1 
ATOM   11491 N  N     . ILE A 1 2759 ? 148.389 118.535 206.536 1.00 93.60  ? 2759 ILE A N     1 
ATOM   11492 C  CA    . ILE A 1 2759 ? 147.526 118.657 207.708 1.00 96.29  ? 2759 ILE A CA    1 
ATOM   11493 C  C     . ILE A 1 2759 ? 146.367 117.676 207.584 1.00 99.21  ? 2759 ILE A C     1 
ATOM   11494 O  O     . ILE A 1 2759 ? 145.444 117.905 206.789 1.00 99.65  ? 2759 ILE A O     1 
ATOM   11495 C  CB    . ILE A 1 2759 ? 147.019 120.097 207.874 1.00 93.72  ? 2759 ILE A CB    1 
ATOM   11496 C  CG1   . ILE A 1 2759 ? 148.191 121.076 207.815 1.00 93.25  ? 2759 ILE A CG1   1 
ATOM   11497 C  CG2   . ILE A 1 2759 ? 146.261 120.247 209.180 1.00 96.47  ? 2759 ILE A CG2   1 
ATOM   11498 C  CD1   . ILE A 1 2759 ? 147.777 122.520 207.892 1.00 88.02  ? 2759 ILE A CD1   1 
ATOM   11499 N  N     . PRO A 1 2760 ? 146.372 116.579 208.344 1.00 100.31 ? 2760 PRO A N     1 
ATOM   11500 C  CA    . PRO A 1 2760 ? 145.272 115.604 208.233 1.00 99.74  ? 2760 PRO A CA    1 
ATOM   11501 C  C     . PRO A 1 2760 ? 143.920 116.161 208.637 1.00 99.10  ? 2760 PRO A C     1 
ATOM   11502 O  O     . PRO A 1 2760 ? 142.893 115.582 208.261 1.00 100.89 ? 2760 PRO A O     1 
ATOM   11503 C  CB    . PRO A 1 2760 ? 145.697 114.459 209.165 1.00 102.01 ? 2760 PRO A CB    1 
ATOM   11504 C  CG    . PRO A 1 2760 ? 147.030 114.803 209.705 1.00 104.99 ? 2760 PRO A CG    1 
ATOM   11505 C  CD    . PRO A 1 2760 ? 147.440 116.161 209.265 1.00 100.10 ? 2760 PRO A CD    1 
ATOM   11506 N  N     . SER A 1 2761 ? 143.879 117.260 209.390 1.00 98.70  ? 2761 SER A N     1 
ATOM   11507 C  CA    . SER A 1 2761 ? 142.610 117.801 209.858 1.00 101.05 ? 2761 SER A CA    1 
ATOM   11508 C  C     . SER A 1 2761 ? 141.868 118.596 208.792 1.00 97.76  ? 2761 SER A C     1 
ATOM   11509 O  O     . SER A 1 2761 ? 140.683 118.891 208.983 1.00 93.19  ? 2761 SER A O     1 
ATOM   11510 C  CB    . SER A 1 2761 ? 142.841 118.684 211.085 1.00 100.52 ? 2761 SER A CB    1 
ATOM   11511 O  OG    . SER A 1 2761 ? 143.533 117.977 212.099 1.00 100.13 ? 2761 SER A OG    1 
ATOM   11512 N  N     . LEU A 1 2762 ? 142.521 118.947 207.683 1.00 93.90  ? 2762 LEU A N     1 
ATOM   11513 C  CA    . LEU A 1 2762 ? 141.903 119.774 206.652 1.00 90.71  ? 2762 LEU A CA    1 
ATOM   11514 C  C     . LEU A 1 2762 ? 141.676 119.013 205.351 1.00 89.01  ? 2762 LEU A C     1 
ATOM   11515 O  O     . LEU A 1 2762 ? 141.252 119.613 204.357 1.00 87.58  ? 2762 LEU A O     1 
ATOM   11516 C  CB    . LEU A 1 2762 ? 142.749 121.022 206.388 1.00 89.22  ? 2762 LEU A CB    1 
ATOM   11517 C  CG    . LEU A 1 2762 ? 142.844 122.048 207.517 1.00 86.53  ? 2762 LEU A CG    1 
ATOM   11518 C  CD1   . LEU A 1 2762 ? 144.118 122.863 207.386 1.00 72.86  ? 2762 LEU A CD1   1 
ATOM   11519 C  CD2   . LEU A 1 2762 ? 141.623 122.951 207.525 1.00 83.60  ? 2762 LEU A CD2   1 
ATOM   11520 N  N     . ARG A 1 2763 ? 141.930 117.701 205.339 1.00 90.70  ? 2763 ARG A N     1 
ATOM   11521 C  CA    . ARG A 1 2763 ? 141.790 116.934 204.105 1.00 88.09  ? 2763 ARG A CA    1 
ATOM   11522 C  C     . ARG A 1 2763 ? 140.370 116.998 203.555 1.00 82.25  ? 2763 ARG A C     1 
ATOM   11523 O  O     . ARG A 1 2763 ? 140.185 117.154 202.342 1.00 77.29  ? 2763 ARG A O     1 
ATOM   11524 C  CB    . ARG A 1 2763 ? 142.223 115.482 204.331 1.00 92.07  ? 2763 ARG A CB    1 
ATOM   11525 C  CG    . ARG A 1 2763 ? 141.324 114.677 205.261 1.00 94.85  ? 2763 ARG A CG    1 
ATOM   11526 C  CD    . ARG A 1 2763 ? 141.818 113.249 205.434 1.00 99.75  ? 2763 ARG A CD    1 
ATOM   11527 N  NE    . ARG A 1 2763 ? 143.113 113.178 206.099 1.00 109.06 ? 2763 ARG A NE    1 
ATOM   11528 C  CZ    . ARG A 1 2763 ? 144.247 112.849 205.495 1.00 113.66 ? 2763 ARG A CZ    1 
ATOM   11529 N  NH1   . ARG A 1 2763 ? 144.283 112.555 204.205 1.00 114.12 ? 2763 ARG A NH1   1 
ATOM   11530 N  NH2   . ARG A 1 2763 ? 145.372 112.810 206.202 1.00 111.15 ? 2763 ARG A NH2   1 
ATOM   11531 N  N     . THR A 1 2764 ? 139.360 116.923 204.424 1.00 83.10  ? 2764 THR A N     1 
ATOM   11532 C  CA    . THR A 1 2764 ? 137.975 116.986 203.976 1.00 84.27  ? 2764 THR A CA    1 
ATOM   11533 C  C     . THR A 1 2764 ? 137.618 118.331 203.364 1.00 81.50  ? 2764 THR A C     1 
ATOM   11534 O  O     . THR A 1 2764 ? 136.569 118.440 202.719 1.00 75.02  ? 2764 THR A O     1 
ATOM   11535 C  CB    . THR A 1 2764 ? 137.028 116.687 205.140 1.00 89.00  ? 2764 THR A CB    1 
ATOM   11536 O  OG1   . THR A 1 2764 ? 137.061 117.771 206.075 1.00 83.74  ? 2764 THR A OG1   1 
ATOM   11537 C  CG2   . THR A 1 2764 ? 137.441 115.405 205.845 1.00 86.64  ? 2764 THR A CG2   1 
ATOM   11538 N  N     . TYR A 1 2765 ? 138.452 119.351 203.550 1.00 83.84  ? 2765 TYR A N     1 
ATOM   11539 C  CA    . TYR A 1 2765 ? 138.233 120.653 202.941 1.00 76.94  ? 2765 TYR A CA    1 
ATOM   11540 C  C     . TYR A 1 2765 ? 139.015 120.836 201.649 1.00 73.39  ? 2765 TYR A C     1 
ATOM   11541 O  O     . TYR A 1 2765 ? 139.033 121.944 201.106 1.00 73.79  ? 2765 TYR A O     1 
ATOM   11542 C  CB    . TYR A 1 2765 ? 138.592 121.765 203.930 1.00 76.10  ? 2765 TYR A CB    1 
ATOM   11543 C  CG    . TYR A 1 2765 ? 137.829 121.678 205.230 1.00 81.47  ? 2765 TYR A CG    1 
ATOM   11544 C  CD1   . TYR A 1 2765 ? 136.512 122.108 205.313 1.00 78.65  ? 2765 TYR A CD1   1 
ATOM   11545 C  CD2   . TYR A 1 2765 ? 138.422 121.161 206.373 1.00 84.48  ? 2765 TYR A CD2   1 
ATOM   11546 C  CE1   . TYR A 1 2765 ? 135.808 122.028 206.497 1.00 79.81  ? 2765 TYR A CE1   1 
ATOM   11547 C  CE2   . TYR A 1 2765 ? 137.726 121.077 207.562 1.00 86.79  ? 2765 TYR A CE2   1 
ATOM   11548 C  CZ    . TYR A 1 2765 ? 136.420 121.512 207.619 1.00 86.56  ? 2765 TYR A CZ    1 
ATOM   11549 O  OH    . TYR A 1 2765 ? 135.724 121.430 208.802 1.00 86.90  ? 2765 TYR A OH    1 
ATOM   11550 N  N     . ALA A 1 2766 ? 139.667 119.784 201.150 1.00 73.40  ? 2766 ALA A N     1 
ATOM   11551 C  CA    . ALA A 1 2766 ? 140.396 119.899 199.891 1.00 65.77  ? 2766 ALA A CA    1 
ATOM   11552 C  C     . ALA A 1 2766 ? 139.445 120.138 198.724 1.00 64.82  ? 2766 ALA A C     1 
ATOM   11553 O  O     . ALA A 1 2766 ? 139.671 121.027 197.896 1.00 61.23  ? 2766 ALA A O     1 
ATOM   11554 C  CB    . ALA A 1 2766 ? 141.235 118.644 199.655 1.00 66.76  ? 2766 ALA A CB    1 
ATOM   11555 N  N     . GLU A 1 2767 ? 138.377 119.344 198.638 1.00 70.61  ? 2767 GLU A N     1 
ATOM   11556 C  CA    . GLU A 1 2767 ? 137.419 119.507 197.546 1.00 71.21  ? 2767 GLU A CA    1 
ATOM   11557 C  C     . GLU A 1 2767 ? 136.684 120.842 197.585 1.00 68.67  ? 2767 GLU A C     1 
ATOM   11558 O  O     . GLU A 1 2767 ? 136.604 121.502 196.535 1.00 66.91  ? 2767 GLU A O     1 
ATOM   11559 C  CB    . GLU A 1 2767 ? 136.439 118.329 197.538 1.00 71.64  ? 2767 GLU A CB    1 
ATOM   11560 C  CG    . GLU A 1 2767 ? 135.374 118.426 196.459 1.00 75.39  ? 2767 GLU A CG    1 
ATOM   11561 C  CD    . GLU A 1 2767 ? 134.062 117.792 196.875 1.00 84.87  ? 2767 GLU A CD    1 
ATOM   11562 O  OE1   . GLU A 1 2767 ? 133.660 117.965 198.044 1.00 79.23  ? 2767 GLU A OE1   1 
ATOM   11563 O  OE2   . GLU A 1 2767 ? 133.431 117.122 196.030 1.00 92.46  ? 2767 GLU A OE2   1 
ATOM   11564 N  N     . PRO A 1 2768 ? 136.119 121.295 198.714 1.00 68.88  ? 2768 PRO A N     1 
ATOM   11565 C  CA    . PRO A 1 2768 ? 135.429 122.597 198.688 1.00 62.76  ? 2768 PRO A CA    1 
ATOM   11566 C  C     . PRO A 1 2768 ? 136.351 123.758 198.370 1.00 62.84  ? 2768 PRO A C     1 
ATOM   11567 O  O     . PRO A 1 2768 ? 136.033 124.570 197.490 1.00 62.05  ? 2768 PRO A O     1 
ATOM   11568 C  CB    . PRO A 1 2768 ? 134.843 122.711 200.102 1.00 63.21  ? 2768 PRO A CB    1 
ATOM   11569 C  CG    . PRO A 1 2768 ? 134.747 121.318 200.587 1.00 69.37  ? 2768 PRO A CG    1 
ATOM   11570 C  CD    . PRO A 1 2768 ? 135.937 120.622 200.013 1.00 68.04  ? 2768 PRO A CD    1 
ATOM   11571 N  N     . LEU A 1 2769 ? 137.499 123.841 199.050 1.00 63.28  ? 2769 LEU A N     1 
ATOM   11572 C  CA    . LEU A 1 2769 ? 138.423 124.952 198.840 1.00 58.13  ? 2769 LEU A CA    1 
ATOM   11573 C  C     . LEU A 1 2769 ? 138.737 125.137 197.364 1.00 55.27  ? 2769 LEU A C     1 
ATOM   11574 O  O     . LEU A 1 2769 ? 138.577 126.240 196.824 1.00 56.08  ? 2769 LEU A O     1 
ATOM   11575 C  CB    . LEU A 1 2769 ? 139.710 124.716 199.630 1.00 55.30  ? 2769 LEU A CB    1 
ATOM   11576 C  CG    . LEU A 1 2769 ? 140.764 125.823 199.602 1.00 53.46  ? 2769 LEU A CG    1 
ATOM   11577 C  CD1   . LEU A 1 2769 ? 140.452 126.888 200.636 1.00 57.57  ? 2769 LEU A CD1   1 
ATOM   11578 C  CD2   . LEU A 1 2769 ? 142.149 125.242 199.827 1.00 51.80  ? 2769 LEU A CD2   1 
ATOM   11579 N  N     . THR A 1 2770 ? 139.131 124.055 196.685 1.00 52.70  ? 2770 THR A N     1 
ATOM   11580 C  CA    . THR A 1 2770 ? 139.405 124.135 195.255 1.00 49.14  ? 2770 THR A CA    1 
ATOM   11581 C  C     . THR A 1 2770 ? 138.244 124.771 194.512 1.00 47.90  ? 2770 THR A C     1 
ATOM   11582 O  O     . THR A 1 2770 ? 138.431 125.753 193.782 1.00 51.47  ? 2770 THR A O     1 
ATOM   11583 C  CB    . THR A 1 2770 ? 139.682 122.744 194.690 1.00 49.52  ? 2770 THR A CB    1 
ATOM   11584 O  OG1   . THR A 1 2770 ? 140.792 122.156 195.378 1.00 60.87  ? 2770 THR A OG1   1 
ATOM   11585 C  CG2   . THR A 1 2770 ? 139.985 122.833 193.206 1.00 43.88  ? 2770 THR A CG2   1 
ATOM   11586 N  N     . ALA A 1 2771 ? 137.028 124.262 194.736 1.00 48.86  ? 2771 ALA A N     1 
ATOM   11587 C  CA    . ALA A 1 2771 ? 135.861 124.841 194.085 1.00 46.00  ? 2771 ALA A CA    1 
ATOM   11588 C  C     . ALA A 1 2771 ? 135.814 126.341 194.312 1.00 48.71  ? 2771 ALA A C     1 
ATOM   11589 O  O     . ALA A 1 2771 ? 135.750 127.118 193.350 1.00 47.20  ? 2771 ALA A O     1 
ATOM   11590 C  CB    . ALA A 1 2771 ? 134.585 124.176 194.599 1.00 47.44  ? 2771 ALA A CB    1 
ATOM   11591 N  N     . ALA A 1 2772 ? 135.940 126.766 195.574 1.00 53.87  ? 2772 ALA A N     1 
ATOM   11592 C  CA    . ALA A 1 2772 ? 135.939 128.192 195.867 1.00 47.63  ? 2772 ALA A CA    1 
ATOM   11593 C  C     . ALA A 1 2772 ? 136.981 128.905 195.026 1.00 44.50  ? 2772 ALA A C     1 
ATOM   11594 O  O     . ALA A 1 2772 ? 136.644 129.817 194.256 1.00 47.63  ? 2772 ALA A O     1 
ATOM   11595 C  CB    . ALA A 1 2772 ? 136.195 128.424 197.355 1.00 44.31  ? 2772 ALA A CB    1 
ATOM   11596 N  N     . MET A 1 2773 ? 138.230 128.427 195.081 1.00 40.40  ? 2773 MET A N     1 
ATOM   11597 C  CA    . MET A 1 2773 ? 139.278 128.986 194.237 1.00 39.37  ? 2773 MET A CA    1 
ATOM   11598 C  C     . MET A 1 2773 ? 138.781 129.135 192.813 1.00 42.36  ? 2773 MET A C     1 
ATOM   11599 O  O     . MET A 1 2773 ? 138.656 130.257 192.300 1.00 46.74  ? 2773 MET A O     1 
ATOM   11600 C  CB    . MET A 1 2773 ? 140.521 128.097 194.278 1.00 39.18  ? 2773 MET A CB    1 
ATOM   11601 C  CG    . MET A 1 2773 ? 141.103 127.880 195.661 1.00 42.09  ? 2773 MET A CG    1 
ATOM   11602 S  SD    . MET A 1 2773 ? 142.702 127.049 195.608 1.00 50.47  ? 2773 MET A SD    1 
ATOM   11603 C  CE    . MET A 1 2773 ? 143.434 127.816 194.168 1.00 39.93  ? 2773 MET A CE    1 
ATOM   11604 N  N     . VAL A 1 2774 ? 138.371 128.018 192.206 1.00 45.02  ? 2774 VAL A N     1 
ATOM   11605 C  CA    . VAL A 1 2774 ? 137.988 128.045 190.804 1.00 42.01  ? 2774 VAL A CA    1 
ATOM   11606 C  C     . VAL A 1 2774 ? 136.919 129.098 190.586 1.00 46.97  ? 2774 VAL A C     1 
ATOM   11607 O  O     . VAL A 1 2774 ? 137.083 130.000 189.752 1.00 50.41  ? 2774 VAL A O     1 
ATOM   11608 C  CB    . VAL A 1 2774 ? 137.514 126.653 190.350 1.00 36.53  ? 2774 VAL A CB    1 
ATOM   11609 C  CG1   . VAL A 1 2774 ? 137.003 126.708 188.924 1.00 37.98  ? 2774 VAL A CG1   1 
ATOM   11610 C  CG2   . VAL A 1 2774 ? 138.633 125.640 190.484 1.00 39.40  ? 2774 VAL A CG2   1 
ATOM   11611 N  N     . GLU A 1 2775 ? 135.872 129.078 191.417 1.00 42.79  ? 2775 GLU A N     1 
ATOM   11612 C  CA    . GLU A 1 2775 ? 134.777 130.013 191.210 1.00 41.27  ? 2775 GLU A CA    1 
ATOM   11613 C  C     . GLU A 1 2775 ? 135.300 131.436 191.203 1.00 44.51  ? 2775 GLU A C     1 
ATOM   11614 O  O     . GLU A 1 2775 ? 135.120 132.168 190.220 1.00 48.16  ? 2775 GLU A O     1 
ATOM   11615 C  CB    . GLU A 1 2775 ? 133.707 129.845 192.284 1.00 45.21  ? 2775 GLU A CB    1 
ATOM   11616 C  CG    . GLU A 1 2775 ? 132.555 130.818 192.106 1.00 53.10  ? 2775 GLU A CG    1 
ATOM   11617 C  CD    . GLU A 1 2775 ? 131.547 130.744 193.224 1.00 63.31  ? 2775 GLU A CD    1 
ATOM   11618 O  OE1   . GLU A 1 2775 ? 131.773 129.966 194.170 1.00 64.10  ? 2775 GLU A OE1   1 
ATOM   11619 O  OE2   . GLU A 1 2775 ? 130.530 131.465 193.160 1.00 66.05  ? 2775 GLU A OE2   1 
ATOM   11620 N  N     . PHE A 1 2776 ? 136.049 131.807 192.245 1.00 43.38  ? 2776 PHE A N     1 
ATOM   11621 C  CA    . PHE A 1 2776 ? 136.513 133.183 192.316 1.00 42.91  ? 2776 PHE A CA    1 
ATOM   11622 C  C     . PHE A 1 2776 ? 137.343 133.520 191.094 1.00 44.02  ? 2776 PHE A C     1 
ATOM   11623 O  O     . PHE A 1 2776 ? 137.107 134.546 190.442 1.00 47.09  ? 2776 PHE A O     1 
ATOM   11624 C  CB    . PHE A 1 2776 ? 137.310 133.427 193.592 1.00 41.76  ? 2776 PHE A CB    1 
ATOM   11625 C  CG    . PHE A 1 2776 ? 137.628 134.872 193.820 1.00 44.92  ? 2776 PHE A CG    1 
ATOM   11626 C  CD1   . PHE A 1 2776 ? 136.611 135.801 193.948 1.00 51.00  ? 2776 PHE A CD1   1 
ATOM   11627 C  CD2   . PHE A 1 2776 ? 138.937 135.309 193.876 1.00 45.43  ? 2776 PHE A CD2   1 
ATOM   11628 C  CE1   . PHE A 1 2776 ? 136.895 137.132 194.142 1.00 50.67  ? 2776 PHE A CE1   1 
ATOM   11629 C  CE2   . PHE A 1 2776 ? 139.224 136.640 194.071 1.00 49.31  ? 2776 PHE A CE2   1 
ATOM   11630 C  CZ    . PHE A 1 2776 ? 138.203 137.552 194.202 1.00 49.36  ? 2776 PHE A CZ    1 
ATOM   11631 N  N     . TYR A 1 2777 ? 138.254 132.620 190.716 1.00 42.21  ? 2777 TYR A N     1 
ATOM   11632 C  CA    . TYR A 1 2777 ? 139.075 132.872 189.543 1.00 37.38  ? 2777 TYR A CA    1 
ATOM   11633 C  C     . TYR A 1 2777 ? 138.187 133.160 188.345 1.00 41.37  ? 2777 TYR A C     1 
ATOM   11634 O  O     . TYR A 1 2777 ? 138.276 134.237 187.737 1.00 47.74  ? 2777 TYR A O     1 
ATOM   11635 C  CB    . TYR A 1 2777 ? 139.992 131.677 189.282 1.00 39.49  ? 2777 TYR A CB    1 
ATOM   11636 C  CG    . TYR A 1 2777 ? 140.611 131.656 187.906 1.00 42.75  ? 2777 TYR A CG    1 
ATOM   11637 C  CD1   . TYR A 1 2777 ? 141.586 132.574 187.549 1.00 36.52  ? 2777 TYR A CD1   1 
ATOM   11638 C  CD2   . TYR A 1 2777 ? 140.222 130.716 186.967 1.00 47.51  ? 2777 TYR A CD2   1 
ATOM   11639 C  CE1   . TYR A 1 2777 ? 142.151 132.557 186.295 1.00 35.11  ? 2777 TYR A CE1   1 
ATOM   11640 C  CE2   . TYR A 1 2777 ? 140.781 130.693 185.713 1.00 45.54  ? 2777 TYR A CE2   1 
ATOM   11641 C  CZ    . TYR A 1 2777 ? 141.744 131.613 185.381 1.00 41.06  ? 2777 TYR A CZ    1 
ATOM   11642 O  OH    . TYR A 1 2777 ? 142.297 131.583 184.124 1.00 43.04  ? 2777 TYR A OH    1 
ATOM   11643 N  N     . THR A 1 2778 ? 137.232 132.263 188.080 1.00 42.17  ? 2778 THR A N     1 
ATOM   11644 C  CA    . THR A 1 2778 ? 136.338 132.465 186.950 1.00 45.83  ? 2778 THR A CA    1 
ATOM   11645 C  C     . THR A 1 2778 ? 135.646 133.812 187.057 1.00 47.87  ? 2778 THR A C     1 
ATOM   11646 O  O     . THR A 1 2778 ? 135.667 134.603 186.105 1.00 50.03  ? 2778 THR A O     1 
ATOM   11647 C  CB    . THR A 1 2778 ? 135.311 131.337 186.873 1.00 46.75  ? 2778 THR A CB    1 
ATOM   11648 O  OG1   . THR A 1 2778 ? 134.632 131.222 188.129 1.00 54.83  ? 2778 THR A OG1   1 
ATOM   11649 C  CG2   . THR A 1 2778 ? 135.993 130.017 186.552 1.00 46.20  ? 2778 THR A CG2   1 
ATOM   11650 N  N     . MET A 1 2779 ? 135.109 134.125 188.241 1.00 46.52  ? 2779 MET A N     1 
ATOM   11651 C  CA    . MET A 1 2779 ? 134.413 135.392 188.416 1.00 47.21  ? 2779 MET A CA    1 
ATOM   11652 C  C     . MET A 1 2779 ? 135.301 136.551 188.000 1.00 47.10  ? 2779 MET A C     1 
ATOM   11653 O  O     . MET A 1 2779 ? 134.915 137.365 187.152 1.00 52.39  ? 2779 MET A O     1 
ATOM   11654 C  CB    . MET A 1 2779 ? 133.963 135.553 189.867 1.00 45.22  ? 2779 MET A CB    1 
ATOM   11655 C  CG    . MET A 1 2779 ? 132.896 134.567 190.302 1.00 50.87  ? 2779 MET A CG    1 
ATOM   11656 S  SD    . MET A 1 2779 ? 132.467 134.750 192.043 1.00 77.37  ? 2779 MET A SD    1 
ATOM   11657 C  CE    . MET A 1 2779 ? 131.602 136.315 192.013 1.00 62.26  ? 2779 MET A CE    1 
ATOM   11658 N  N     . SER A 1 2780 ? 136.532 136.589 188.518 1.00 41.36  ? 2780 SER A N     1 
ATOM   11659 C  CA    . SER A 1 2780 ? 137.410 137.703 188.192 1.00 40.09  ? 2780 SER A CA    1 
ATOM   11660 C  C     . SER A 1 2780 ? 137.666 137.758 186.697 1.00 43.41  ? 2780 SER A C     1 
ATOM   11661 O  O     . SER A 1 2780 ? 137.596 138.831 186.086 1.00 48.65  ? 2780 SER A O     1 
ATOM   11662 C  CB    . SER A 1 2780 ? 138.720 137.585 188.968 1.00 46.54  ? 2780 SER A CB    1 
ATOM   11663 O  OG    . SER A 1 2780 ? 138.469 137.380 190.346 1.00 51.08  ? 2780 SER A OG    1 
ATOM   11664 N  N     . GLN A 1 2781 ? 137.891 136.596 186.080 1.00 43.23  ? 2781 GLN A N     1 
ATOM   11665 C  CA    . GLN A 1 2781 ? 138.198 136.577 184.657 1.00 43.95  ? 2781 GLN A CA    1 
ATOM   11666 C  C     . GLN A 1 2781 ? 137.021 137.096 183.842 1.00 50.97  ? 2781 GLN A C     1 
ATOM   11667 O  O     . GLN A 1 2781 ? 137.211 137.686 182.772 1.00 54.78  ? 2781 GLN A O     1 
ATOM   11668 C  CB    . GLN A 1 2781 ? 138.591 135.164 184.229 1.00 40.64  ? 2781 GLN A CB    1 
ATOM   11669 C  CG    . GLN A 1 2781 ? 139.046 135.050 182.789 1.00 46.90  ? 2781 GLN A CG    1 
ATOM   11670 C  CD    . GLN A 1 2781 ? 139.757 133.745 182.514 1.00 46.32  ? 2781 GLN A CD    1 
ATOM   11671 O  OE1   . GLN A 1 2781 ? 140.860 133.730 181.969 1.00 42.15  ? 2781 GLN A OE1   1 
ATOM   11672 N  NE2   . GLN A 1 2781 ? 139.133 132.639 182.897 1.00 49.41  ? 2781 GLN A NE2   1 
ATOM   11673 N  N     . GLU A 1 2782 ? 135.795 136.899 184.335 1.00 51.07  ? 2782 GLU A N     1 
ATOM   11674 C  CA    . GLU A 1 2782 ? 134.649 137.485 183.651 1.00 50.38  ? 2782 GLU A CA    1 
ATOM   11675 C  C     . GLU A 1 2782 ? 134.524 138.970 183.960 1.00 51.82  ? 2782 GLU A C     1 
ATOM   11676 O  O     . GLU A 1 2782 ? 134.162 139.764 183.083 1.00 56.45  ? 2782 GLU A O     1 
ATOM   11677 C  CB    . GLU A 1 2782 ? 133.364 136.750 184.029 1.00 53.08  ? 2782 GLU A CB    1 
ATOM   11678 C  CG    . GLU A 1 2782 ? 133.464 135.238 183.973 1.00 63.78  ? 2782 GLU A CG    1 
ATOM   11679 C  CD    . GLU A 1 2782 ? 132.176 134.555 184.389 1.00 74.47  ? 2782 GLU A CD    1 
ATOM   11680 O  OE1   . GLU A 1 2782 ? 131.275 135.247 184.906 1.00 75.47  ? 2782 GLU A OE1   1 
ATOM   11681 O  OE2   . GLU A 1 2782 ? 132.064 133.326 184.197 1.00 76.44  ? 2782 GLU A OE2   1 
ATOM   11682 N  N     . ARG A 1 2783 ? 134.821 139.367 185.198 1.00 49.15  ? 2783 ARG A N     1 
ATOM   11683 C  CA    . ARG A 1 2783 ? 134.555 140.741 185.610 1.00 45.79  ? 2783 ARG A CA    1 
ATOM   11684 C  C     . ARG A 1 2783 ? 135.581 141.703 185.025 1.00 48.90  ? 2783 ARG A C     1 
ATOM   11685 O  O     . ARG A 1 2783 ? 135.226 142.775 184.523 1.00 53.42  ? 2783 ARG A O     1 
ATOM   11686 C  CB    . ARG A 1 2783 ? 134.530 140.830 187.136 1.00 49.32  ? 2783 ARG A CB    1 
ATOM   11687 C  CG    . ARG A 1 2783 ? 134.393 142.238 187.690 1.00 53.09  ? 2783 ARG A CG    1 
ATOM   11688 C  CD    . ARG A 1 2783 ? 133.250 143.001 187.046 1.00 52.17  ? 2783 ARG A CD    1 
ATOM   11689 N  NE    . ARG A 1 2783 ? 133.447 144.442 187.141 1.00 66.35  ? 2783 ARG A NE    1 
ATOM   11690 C  CZ    . ARG A 1 2783 ? 133.176 145.169 188.216 1.00 70.65  ? 2783 ARG A CZ    1 
ATOM   11691 N  NH1   . ARG A 1 2783 ? 132.677 144.623 189.312 1.00 66.26  ? 2783 ARG A NH1   1 
ATOM   11692 N  NH2   . ARG A 1 2783 ? 133.411 146.478 188.189 1.00 66.33  ? 2783 ARG A NH2   1 
ATOM   11693 N  N     . PHE A 1 2784 ? 136.856 141.334 185.069 1.00 48.78  ? 2784 PHE A N     1 
ATOM   11694 C  CA    . PHE A 1 2784 ? 137.944 142.217 184.670 1.00 45.46  ? 2784 PHE A CA    1 
ATOM   11695 C  C     . PHE A 1 2784 ? 138.575 141.682 183.394 1.00 50.44  ? 2784 PHE A C     1 
ATOM   11696 O  O     . PHE A 1 2784 ? 139.055 140.544 183.363 1.00 56.17  ? 2784 PHE A O     1 
ATOM   11697 C  CB    . PHE A 1 2784 ? 138.979 142.331 185.787 1.00 40.56  ? 2784 PHE A CB    1 
ATOM   11698 C  CG    . PHE A 1 2784 ? 138.389 142.708 187.113 1.00 42.22  ? 2784 PHE A CG    1 
ATOM   11699 C  CD1   . PHE A 1 2784 ? 137.736 143.913 187.274 1.00 44.05  ? 2784 PHE A CD1   1 
ATOM   11700 C  CD2   . PHE A 1 2784 ? 138.469 141.847 188.191 1.00 45.80  ? 2784 PHE A CD2   1 
ATOM   11701 C  CE1   . PHE A 1 2784 ? 137.183 144.256 188.485 1.00 44.53  ? 2784 PHE A CE1   1 
ATOM   11702 C  CE2   . PHE A 1 2784 ? 137.916 142.188 189.406 1.00 45.53  ? 2784 PHE A CE2   1 
ATOM   11703 C  CZ    . PHE A 1 2784 ? 137.274 143.394 189.552 1.00 44.38  ? 2784 PHE A CZ    1 
ATOM   11704 N  N     . THR A 1 2785 ? 138.576 142.503 182.349 1.00 46.11  ? 2785 THR A N     1 
ATOM   11705 C  CA    . THR A 1 2785 ? 139.103 142.120 181.051 1.00 48.71  ? 2785 THR A CA    1 
ATOM   11706 C  C     . THR A 1 2785 ? 140.156 143.126 180.615 1.00 46.53  ? 2785 THR A C     1 
ATOM   11707 O  O     . THR A 1 2785 ? 140.246 144.234 181.148 1.00 49.93  ? 2785 THR A O     1 
ATOM   11708 C  CB    . THR A 1 2785 ? 137.993 142.027 179.995 1.00 57.29  ? 2785 THR A CB    1 
ATOM   11709 O  OG1   . THR A 1 2785 ? 137.355 143.302 179.858 1.00 67.43  ? 2785 THR A OG1   1 
ATOM   11710 C  CG2   . THR A 1 2785 ? 136.959 140.986 180.395 1.00 57.54  ? 2785 THR A CG2   1 
ATOM   11711 N  N     . GLN A 1 2786 ? 140.959 142.723 179.631 1.00 44.73  ? 2786 GLN A N     1 
ATOM   11712 C  CA    . GLN A 1 2786 ? 142.069 143.549 179.176 1.00 44.31  ? 2786 GLN A CA    1 
ATOM   11713 C  C     . GLN A 1 2786 ? 141.619 144.808 178.449 1.00 50.21  ? 2786 GLN A C     1 
ATOM   11714 O  O     . GLN A 1 2786 ? 142.454 145.685 178.201 1.00 54.13  ? 2786 GLN A O     1 
ATOM   11715 C  CB    . GLN A 1 2786 ? 142.988 142.733 178.268 1.00 43.61  ? 2786 GLN A CB    1 
ATOM   11716 C  CG    . GLN A 1 2786 ? 143.667 141.571 178.969 1.00 45.15  ? 2786 GLN A CG    1 
ATOM   11717 C  CD    . GLN A 1 2786 ? 144.888 141.078 178.223 1.00 55.08  ? 2786 GLN A CD    1 
ATOM   11718 O  OE1   . GLN A 1 2786 ? 145.841 141.827 178.008 1.00 55.83  ? 2786 GLN A OE1   1 
ATOM   11719 N  NE2   . GLN A 1 2786 ? 144.866 139.813 177.823 1.00 55.50  ? 2786 GLN A NE2   1 
ATOM   11720 N  N     . ASP A 1 2787 ? 140.339 144.920 178.092 1.00 52.98  ? 2787 ASP A N     1 
ATOM   11721 C  CA    . ASP A 1 2787 ? 139.868 146.137 177.439 1.00 55.16  ? 2787 ASP A CA    1 
ATOM   11722 C  C     . ASP A 1 2787 ? 139.905 147.330 178.388 1.00 57.92  ? 2787 ASP A C     1 
ATOM   11723 O  O     . ASP A 1 2787 ? 140.244 148.445 177.976 1.00 61.23  ? 2787 ASP A O     1 
ATOM   11724 C  CB    . ASP A 1 2787 ? 138.463 145.923 176.868 1.00 59.84  ? 2787 ASP A CB    1 
ATOM   11725 C  CG    . ASP A 1 2787 ? 137.428 145.615 177.934 1.00 63.00  ? 2787 ASP A CG    1 
ATOM   11726 O  OD1   . ASP A 1 2787 ? 137.790 145.519 179.125 1.00 61.91  ? 2787 ASP A OD1   1 
ATOM   11727 O  OD2   . ASP A 1 2787 ? 136.240 145.468 177.578 1.00 68.76  ? 2787 ASP A OD2   1 
ATOM   11728 N  N     . THR A 1 2788 ? 139.562 147.117 179.660 1.00 54.62  ? 2788 THR A N     1 
ATOM   11729 C  CA    . THR A 1 2788 ? 139.623 148.202 180.634 1.00 49.42  ? 2788 THR A CA    1 
ATOM   11730 C  C     . THR A 1 2788 ? 141.068 148.563 180.957 1.00 49.67  ? 2788 THR A C     1 
ATOM   11731 O  O     . THR A 1 2788 ? 141.504 149.698 180.733 1.00 54.39  ? 2788 THR A O     1 
ATOM   11732 C  CB    . THR A 1 2788 ? 138.868 147.815 181.906 1.00 47.86  ? 2788 THR A CB    1 
ATOM   11733 O  OG1   . THR A 1 2788 ? 139.468 146.651 182.484 1.00 49.35  ? 2788 THR A OG1   1 
ATOM   11734 C  CG2   . THR A 1 2788 ? 137.408 147.526 181.598 1.00 51.06  ? 2788 THR A CG2   1 
ATOM   11735 N  N     . GLN A 1 2789 ? 141.829 147.605 181.483 1.00 45.49  ? 2789 GLN A N     1 
ATOM   11736 C  CA    . GLN A 1 2789 ? 143.237 147.803 181.783 1.00 43.23  ? 2789 GLN A CA    1 
ATOM   11737 C  C     . GLN A 1 2789 ? 144.058 146.689 181.150 1.00 38.98  ? 2789 GLN A C     1 
ATOM   11738 O  O     . GLN A 1 2789 ? 143.689 145.513 181.247 1.00 41.89  ? 2789 GLN A O     1 
ATOM   11739 C  CB    . GLN A 1 2789 ? 143.482 147.835 183.298 1.00 43.67  ? 2789 GLN A CB    1 
ATOM   11740 C  CG    . GLN A 1 2789 ? 142.750 148.953 184.022 1.00 48.90  ? 2789 GLN A CG    1 
ATOM   11741 C  CD    . GLN A 1 2789 ? 143.360 150.317 183.770 1.00 51.01  ? 2789 GLN A CD    1 
ATOM   11742 O  OE1   . GLN A 1 2789 ? 144.416 150.436 183.150 1.00 48.62  ? 2789 GLN A OE1   1 
ATOM   11743 N  NE2   . GLN A 1 2789 ? 142.691 151.359 184.248 1.00 58.69  ? 2789 GLN A NE2   1 
ATOM   11744 N  N     . PRO A 1 2790 ? 145.173 147.025 180.499 1.00 39.01  ? 2790 PRO A N     1 
ATOM   11745 C  CA    . PRO A 1 2790 ? 145.944 145.998 179.779 1.00 41.23  ? 2790 PRO A CA    1 
ATOM   11746 C  C     . PRO A 1 2790 ? 146.521 144.914 180.670 1.00 40.62  ? 2790 PRO A C     1 
ATOM   11747 O  O     . PRO A 1 2790 ? 146.850 143.835 180.163 1.00 43.46  ? 2790 PRO A O     1 
ATOM   11748 C  CB    . PRO A 1 2790 ? 147.054 146.807 179.094 1.00 47.07  ? 2790 PRO A CB    1 
ATOM   11749 C  CG    . PRO A 1 2790 ? 147.143 148.074 179.872 1.00 49.28  ? 2790 PRO A CG    1 
ATOM   11750 C  CD    . PRO A 1 2790 ? 145.751 148.368 180.333 1.00 44.96  ? 2790 PRO A CD    1 
ATOM   11751 N  N     . HIS A 1 2791 ? 146.657 145.153 181.971 1.00 39.71  ? 2791 HIS A N     1 
ATOM   11752 C  CA    . HIS A 1 2791 ? 147.219 144.162 182.876 1.00 35.59  ? 2791 HIS A CA    1 
ATOM   11753 C  C     . HIS A 1 2791 ? 146.155 143.323 183.567 1.00 38.94  ? 2791 HIS A C     1 
ATOM   11754 O  O     . HIS A 1 2791 ? 146.478 142.583 184.498 1.00 44.52  ? 2791 HIS A O     1 
ATOM   11755 C  CB    . HIS A 1 2791 ? 148.110 144.835 183.925 1.00 34.89  ? 2791 HIS A CB    1 
ATOM   11756 C  CG    . HIS A 1 2791 ? 147.393 145.819 184.794 1.00 34.98  ? 2791 HIS A CG    1 
ATOM   11757 N  ND1   . HIS A 1 2791 ? 146.975 147.050 184.339 1.00 36.63  ? 2791 HIS A ND1   1 
ATOM   11758 C  CD2   . HIS A 1 2791 ? 147.023 145.754 186.094 1.00 34.99  ? 2791 HIS A CD2   1 
ATOM   11759 C  CE1   . HIS A 1 2791 ? 146.378 147.701 185.321 1.00 36.85  ? 2791 HIS A CE1   1 
ATOM   11760 N  NE2   . HIS A 1 2791 ? 146.394 146.936 186.397 1.00 36.37  ? 2791 HIS A NE2   1 
ATOM   11761 N  N     . TYR A 1 2792 ? 144.898 143.417 183.139 1.00 40.31  ? 2792 TYR A N     1 
ATOM   11762 C  CA    . TYR A 1 2792 ? 143.845 142.614 183.745 1.00 39.94  ? 2792 TYR A CA    1 
ATOM   11763 C  C     . TYR A 1 2792 ? 143.802 141.226 183.121 1.00 42.17  ? 2792 TYR A C     1 
ATOM   11764 O  O     . TYR A 1 2792 ? 142.744 140.775 182.674 1.00 48.06  ? 2792 TYR A O     1 
ATOM   11765 C  CB    . TYR A 1 2792 ? 142.489 143.301 183.592 1.00 36.63  ? 2792 TYR A CB    1 
ATOM   11766 C  CG    . TYR A 1 2792 ? 142.228 144.392 184.601 1.00 38.23  ? 2792 TYR A CG    1 
ATOM   11767 C  CD1   . TYR A 1 2792 ? 143.201 144.774 185.511 1.00 38.63  ? 2792 TYR A CD1   1 
ATOM   11768 C  CD2   . TYR A 1 2792 ? 141.005 145.042 184.642 1.00 44.03  ? 2792 TYR A CD2   1 
ATOM   11769 C  CE1   . TYR A 1 2792 ? 142.963 145.772 186.430 1.00 39.99  ? 2792 TYR A CE1   1 
ATOM   11770 C  CE2   . TYR A 1 2792 ? 140.758 146.039 185.557 1.00 45.64  ? 2792 TYR A CE2   1 
ATOM   11771 C  CZ    . TYR A 1 2792 ? 141.739 146.400 186.448 1.00 44.76  ? 2792 TYR A CZ    1 
ATOM   11772 O  OH    . TYR A 1 2792 ? 141.488 147.396 187.360 1.00 53.54  ? 2792 TYR A OH    1 
ATOM   11773 N  N     . ILE A 1 2793 ? 144.940 140.540 183.093 1.00 39.64  ? 2793 ILE A N     1 
ATOM   11774 C  CA    . ILE A 1 2793 ? 145.041 139.208 182.507 1.00 37.51  ? 2793 ILE A CA    1 
ATOM   11775 C  C     . ILE A 1 2793 ? 144.999 138.166 183.613 1.00 40.99  ? 2793 ILE A C     1 
ATOM   11776 O  O     . ILE A 1 2793 ? 145.641 138.317 184.661 1.00 48.04  ? 2793 ILE A O     1 
ATOM   11777 C  CB    . ILE A 1 2793 ? 146.312 139.061 181.646 1.00 40.96  ? 2793 ILE A CB    1 
ATOM   11778 C  CG1   . ILE A 1 2793 ? 146.260 137.748 180.863 1.00 50.97  ? 2793 ILE A CG1   1 
ATOM   11779 C  CG2   . ILE A 1 2793 ? 147.575 139.176 182.486 1.00 40.41  ? 2793 ILE A CG2   1 
ATOM   11780 C  CD1   . ILE A 1 2793 ? 147.278 137.644 179.766 1.00 53.86  ? 2793 ILE A CD1   1 
ATOM   11781 N  N     . TYR A 1 2794 ? 144.214 137.117 183.391 1.00 39.64  ? 2794 TYR A N     1 
ATOM   11782 C  CA    . TYR A 1 2794 ? 144.064 136.022 184.334 1.00 37.95  ? 2794 TYR A CA    1 
ATOM   11783 C  C     . TYR A 1 2794 ? 144.283 134.709 183.602 1.00 40.13  ? 2794 TYR A C     1 
ATOM   11784 O  O     . TYR A 1 2794 ? 143.870 134.556 182.449 1.00 46.44  ? 2794 TYR A O     1 
ATOM   11785 C  CB    . TYR A 1 2794 ? 142.686 136.045 184.990 1.00 37.91  ? 2794 TYR A CB    1 
ATOM   11786 C  CG    . TYR A 1 2794 ? 142.384 137.339 185.703 1.00 41.91  ? 2794 TYR A CG    1 
ATOM   11787 C  CD1   . TYR A 1 2794 ? 142.818 137.555 187.002 1.00 38.23  ? 2794 TYR A CD1   1 
ATOM   11788 C  CD2   . TYR A 1 2794 ? 141.685 138.355 185.069 1.00 46.64  ? 2794 TYR A CD2   1 
ATOM   11789 C  CE1   . TYR A 1 2794 ? 142.549 138.740 187.654 1.00 41.33  ? 2794 TYR A CE1   1 
ATOM   11790 C  CE2   . TYR A 1 2794 ? 141.413 139.543 185.713 1.00 46.18  ? 2794 TYR A CE2   1 
ATOM   11791 C  CZ    . TYR A 1 2794 ? 141.847 139.730 187.005 1.00 48.19  ? 2794 TYR A CZ    1 
ATOM   11792 O  OH    . TYR A 1 2794 ? 141.578 140.913 187.651 1.00 50.47  ? 2794 TYR A OH    1 
ATOM   11793 N  N     . SER A 1 2795 ? 144.929 133.769 184.274 1.00 32.69  ? 2795 SER A N     1 
ATOM   11794 C  CA    . SER A 1 2795 ? 145.318 132.509 183.659 1.00 30.64  ? 2795 SER A CA    1 
ATOM   11795 C  C     . SER A 1 2795 ? 145.472 131.478 184.762 1.00 31.95  ? 2795 SER A C     1 
ATOM   11796 O  O     . SER A 1 2795 ? 145.394 131.810 185.950 1.00 41.37  ? 2795 SER A O     1 
ATOM   11797 C  CB    . SER A 1 2795 ? 146.620 132.663 182.864 1.00 30.99  ? 2795 SER A CB    1 
ATOM   11798 O  OG    . SER A 1 2795 ? 147.746 132.549 183.712 1.00 36.71  ? 2795 SER A OG    1 
ATOM   11799 N  N     . PRO A 1 2796 ? 145.668 130.206 184.405 1.00 26.57  ? 2796 PRO A N     1 
ATOM   11800 C  CA    . PRO A 1 2796 ? 145.977 129.205 185.437 1.00 26.08  ? 2796 PRO A CA    1 
ATOM   11801 C  C     . PRO A 1 2796 ? 147.254 129.490 186.206 1.00 33.45  ? 2796 PRO A C     1 
ATOM   11802 O  O     . PRO A 1 2796 ? 147.466 128.884 187.263 1.00 35.15  ? 2796 PRO A O     1 
ATOM   11803 C  CB    . PRO A 1 2796 ? 146.084 127.905 184.634 1.00 27.79  ? 2796 PRO A CB    1 
ATOM   11804 C  CG    . PRO A 1 2796 ? 145.172 128.118 183.500 1.00 30.93  ? 2796 PRO A CG    1 
ATOM   11805 C  CD    . PRO A 1 2796 ? 145.292 129.566 183.132 1.00 31.12  ? 2796 PRO A CD    1 
ATOM   11806 N  N     . ARG A 1 2797 ? 148.122 130.376 185.709 1.00 32.92  ? 2797 ARG A N     1 
ATOM   11807 C  CA    . ARG A 1 2797 ? 149.302 130.752 186.477 1.00 26.97  ? 2797 ARG A CA    1 
ATOM   11808 C  C     . ARG A 1 2797 ? 148.924 131.447 187.777 1.00 34.03  ? 2797 ARG A C     1 
ATOM   11809 O  O     . ARG A 1 2797 ? 149.571 131.224 188.805 1.00 42.53  ? 2797 ARG A O     1 
ATOM   11810 C  CB    . ARG A 1 2797 ? 150.222 131.640 185.643 1.00 25.64  ? 2797 ARG A CB    1 
ATOM   11811 C  CG    . ARG A 1 2797 ? 151.019 130.867 184.619 1.00 31.24  ? 2797 ARG A CG    1 
ATOM   11812 C  CD    . ARG A 1 2797 ? 151.819 131.775 183.714 1.00 28.18  ? 2797 ARG A CD    1 
ATOM   11813 N  NE    . ARG A 1 2797 ? 153.044 131.134 183.259 1.00 23.89  ? 2797 ARG A NE    1 
ATOM   11814 C  CZ    . ARG A 1 2797 ? 153.657 131.429 182.123 1.00 31.04  ? 2797 ARG A CZ    1 
ATOM   11815 N  NH1   . ARG A 1 2797 ? 153.187 132.356 181.307 1.00 33.44  ? 2797 ARG A NH1   1 
ATOM   11816 N  NH2   . ARG A 1 2797 ? 154.764 130.772 181.794 1.00 35.15  ? 2797 ARG A NH2   1 
ATOM   11817 N  N     . GLU A 1 2798 ? 147.887 132.288 187.758 1.00 31.81  ? 2798 GLU A N     1 
ATOM   11818 C  CA    . GLU A 1 2798 ? 147.406 132.881 189.002 1.00 28.95  ? 2798 GLU A CA    1 
ATOM   11819 C  C     . GLU A 1 2798 ? 146.886 131.820 189.964 1.00 31.86  ? 2798 GLU A C     1 
ATOM   11820 O  O     . GLU A 1 2798 ? 147.080 131.931 191.177 1.00 43.43  ? 2798 GLU A O     1 
ATOM   11821 C  CB    . GLU A 1 2798 ? 146.330 133.931 188.719 1.00 27.61  ? 2798 GLU A CB    1 
ATOM   11822 C  CG    . GLU A 1 2798 ? 146.860 135.238 188.141 1.00 39.69  ? 2798 GLU A CG    1 
ATOM   11823 C  CD    . GLU A 1 2798 ? 147.099 135.188 186.650 1.00 44.76  ? 2798 GLU A CD    1 
ATOM   11824 O  OE1   . GLU A 1 2798 ? 146.792 134.153 186.032 1.00 45.43  ? 2798 GLU A OE1   1 
ATOM   11825 O  OE2   . GLU A 1 2798 ? 147.599 136.189 186.094 1.00 42.86  ? 2798 GLU A OE2   1 
ATOM   11826 N  N     . MET A 1 2799 ? 146.231 130.780 189.448 1.00 29.96  ? 2799 MET A N     1 
ATOM   11827 C  CA    . MET A 1 2799 ? 145.747 129.724 190.332 1.00 31.29  ? 2799 MET A CA    1 
ATOM   11828 C  C     . MET A 1 2799 ? 146.902 128.915 190.915 1.00 32.19  ? 2799 MET A C     1 
ATOM   11829 O  O     . MET A 1 2799 ? 146.860 128.514 192.085 1.00 33.65  ? 2799 MET A O     1 
ATOM   11830 C  CB    . MET A 1 2799 ? 144.766 128.825 189.584 1.00 31.92  ? 2799 MET A CB    1 
ATOM   11831 C  CG    . MET A 1 2799 ? 143.408 129.470 189.393 1.00 33.82  ? 2799 MET A CG    1 
ATOM   11832 S  SD    . MET A 1 2799 ? 142.196 128.941 190.612 1.00 54.70  ? 2799 MET A SD    1 
ATOM   11833 C  CE    . MET A 1 2799 ? 141.744 127.345 189.962 1.00 44.40  ? 2799 MET A CE    1 
ATOM   11834 N  N     . THR A 1 2800 ? 147.945 128.667 190.118 1.00 31.39  ? 2800 THR A N     1 
ATOM   11835 C  CA    . THR A 1 2800 ? 149.131 128.003 190.651 1.00 34.50  ? 2800 THR A CA    1 
ATOM   11836 C  C     . THR A 1 2800 ? 149.816 128.863 191.702 1.00 38.34  ? 2800 THR A C     1 
ATOM   11837 O  O     . THR A 1 2800 ? 150.311 128.347 192.707 1.00 45.14  ? 2800 THR A O     1 
ATOM   11838 C  CB    . THR A 1 2800 ? 150.113 127.666 189.531 1.00 34.96  ? 2800 THR A CB    1 
ATOM   11839 O  OG1   . THR A 1 2800 ? 150.490 128.866 188.847 1.00 39.79  ? 2800 THR A OG1   1 
ATOM   11840 C  CG2   . THR A 1 2800 ? 149.487 126.703 188.553 1.00 36.24  ? 2800 THR A CG2   1 
ATOM   11841 N  N     . ARG A 1 2801 ? 149.869 130.177 191.479 1.00 32.23  ? 2801 ARG A N     1 
ATOM   11842 C  CA    . ARG A 1 2801 ? 150.436 131.075 192.480 1.00 28.29  ? 2801 ARG A CA    1 
ATOM   11843 C  C     . ARG A 1 2801 ? 149.600 131.074 193.752 1.00 29.94  ? 2801 ARG A C     1 
ATOM   11844 O  O     . ARG A 1 2801 ? 150.138 131.164 194.858 1.00 35.47  ? 2801 ARG A O     1 
ATOM   11845 C  CB    . ARG A 1 2801 ? 150.557 132.484 191.903 1.00 24.37  ? 2801 ARG A CB    1 
ATOM   11846 C  CG    . ARG A 1 2801 ? 151.650 132.607 190.861 1.00 30.86  ? 2801 ARG A CG    1 
ATOM   11847 C  CD    . ARG A 1 2801 ? 151.988 134.050 190.553 1.00 30.27  ? 2801 ARG A CD    1 
ATOM   11848 N  NE    . ARG A 1 2801 ? 150.975 134.682 189.719 1.00 31.82  ? 2801 ARG A NE    1 
ATOM   11849 C  CZ    . ARG A 1 2801 ? 151.154 135.004 188.446 1.00 34.51  ? 2801 ARG A CZ    1 
ATOM   11850 N  NH1   . ARG A 1 2801 ? 152.288 134.740 187.820 1.00 32.06  ? 2801 ARG A NH1   1 
ATOM   11851 N  NH2   . ARG A 1 2801 ? 150.168 135.601 187.783 1.00 37.05  ? 2801 ARG A NH2   1 
ATOM   11852 N  N     . TRP A 1 2802 ? 148.280 130.971 193.609 1.00 29.74  ? 2802 TRP A N     1 
ATOM   11853 C  CA    . TRP A 1 2802 ? 147.392 130.848 194.761 1.00 27.92  ? 2802 TRP A CA    1 
ATOM   11854 C  C     . TRP A 1 2802 ? 147.705 129.591 195.563 1.00 33.20  ? 2802 TRP A C     1 
ATOM   11855 O  O     . TRP A 1 2802 ? 147.852 129.636 196.794 1.00 41.43  ? 2802 TRP A O     1 
ATOM   11856 C  CB    . TRP A 1 2802 ? 145.949 130.830 194.261 1.00 27.69  ? 2802 TRP A CB    1 
ATOM   11857 C  CG    . TRP A 1 2802 ? 144.912 131.175 195.259 1.00 31.87  ? 2802 TRP A CG    1 
ATOM   11858 C  CD1   . TRP A 1 2802 ? 145.037 131.175 196.612 1.00 34.12  ? 2802 TRP A CD1   1 
ATOM   11859 C  CD2   . TRP A 1 2802 ? 143.568 131.567 194.977 1.00 30.96  ? 2802 TRP A CD2   1 
ATOM   11860 N  NE1   . TRP A 1 2802 ? 143.852 131.550 197.195 1.00 35.82  ? 2802 TRP A NE1   1 
ATOM   11861 C  CE2   . TRP A 1 2802 ? 142.934 131.795 196.208 1.00 33.30  ? 2802 TRP A CE2   1 
ATOM   11862 C  CE3   . TRP A 1 2802 ? 142.840 131.750 193.799 1.00 28.79  ? 2802 TRP A CE3   1 
ATOM   11863 C  CZ2   . TRP A 1 2802 ? 141.607 132.196 196.297 1.00 34.83  ? 2802 TRP A CZ2   1 
ATOM   11864 C  CZ3   . TRP A 1 2802 ? 141.524 132.146 193.889 1.00 32.85  ? 2802 TRP A CZ3   1 
ATOM   11865 C  CH2   . TRP A 1 2802 ? 140.920 132.366 195.129 1.00 35.68  ? 2802 TRP A CH2   1 
ATOM   11866 N  N     . VAL A 1 2803 ? 147.814 128.455 194.871 1.00 35.42  ? 2803 VAL A N     1 
ATOM   11867 C  CA    . VAL A 1 2803 ? 148.126 127.196 195.540 1.00 36.05  ? 2803 VAL A CA    1 
ATOM   11868 C  C     . VAL A 1 2803 ? 149.496 127.268 196.201 1.00 36.97  ? 2803 VAL A C     1 
ATOM   11869 O  O     . VAL A 1 2803 ? 149.682 126.796 197.327 1.00 42.14  ? 2803 VAL A O     1 
ATOM   11870 C  CB    . VAL A 1 2803 ? 148.034 126.024 194.545 1.00 37.91  ? 2803 VAL A CB    1 
ATOM   11871 C  CG1   . VAL A 1 2803 ? 148.499 124.735 195.197 1.00 43.75  ? 2803 VAL A CG1   1 
ATOM   11872 C  CG2   . VAL A 1 2803 ? 146.613 125.875 194.039 1.00 39.89  ? 2803 VAL A CG2   1 
ATOM   11873 N  N     . ARG A 1 2804 ? 150.474 127.864 195.516 1.00 35.22  ? 2804 ARG A N     1 
ATOM   11874 C  CA    . ARG A 1 2804 ? 151.814 127.989 196.081 1.00 39.21  ? 2804 ARG A CA    1 
ATOM   11875 C  C     . ARG A 1 2804 ? 151.822 128.883 197.312 1.00 44.49  ? 2804 ARG A C     1 
ATOM   11876 O  O     . ARG A 1 2804 ? 152.534 128.605 198.280 1.00 52.81  ? 2804 ARG A O     1 
ATOM   11877 C  CB    . ARG A 1 2804 ? 152.781 128.530 195.031 1.00 42.06  ? 2804 ARG A CB    1 
ATOM   11878 C  CG    . ARG A 1 2804 ? 153.201 127.523 193.985 1.00 44.67  ? 2804 ARG A CG    1 
ATOM   11879 C  CD    . ARG A 1 2804 ? 154.449 127.999 193.272 1.00 61.33  ? 2804 ARG A CD    1 
ATOM   11880 N  NE    . ARG A 1 2804 ? 154.749 127.206 192.087 1.00 66.53  ? 2804 ARG A NE    1 
ATOM   11881 C  CZ    . ARG A 1 2804 ? 154.850 127.708 190.864 1.00 66.47  ? 2804 ARG A CZ    1 
ATOM   11882 N  NH1   . ARG A 1 2804 ? 154.651 128.994 190.627 1.00 63.45  ? 2804 ARG A NH1   1 
ATOM   11883 N  NH2   . ARG A 1 2804 ? 155.152 126.898 189.854 1.00 67.71  ? 2804 ARG A NH2   1 
ATOM   11884 N  N     . GLY A 1 2805 ? 151.054 129.973 197.289 1.00 38.41  ? 2805 GLY A N     1 
ATOM   11885 C  CA    . GLY A 1 2805 ? 150.986 130.837 198.455 1.00 38.56  ? 2805 GLY A CA    1 
ATOM   11886 C  C     . GLY A 1 2805 ? 150.371 130.143 199.652 1.00 43.63  ? 2805 GLY A C     1 
ATOM   11887 O  O     . GLY A 1 2805 ? 150.891 130.230 200.770 1.00 55.37  ? 2805 GLY A O     1 
ATOM   11888 N  N     . ILE A 1 2806 ? 149.265 129.428 199.435 1.00 36.70  ? 2806 ILE A N     1 
ATOM   11889 C  CA    . ILE A 1 2806 ? 148.661 128.683 200.536 1.00 33.97  ? 2806 ILE A CA    1 
ATOM   11890 C  C     . ILE A 1 2806 ? 149.614 127.599 201.030 1.00 42.05  ? 2806 ILE A C     1 
ATOM   11891 O  O     . ILE A 1 2806 ? 149.711 127.338 202.235 1.00 49.54  ? 2806 ILE A O     1 
ATOM   11892 C  CB    . ILE A 1 2806 ? 147.300 128.099 200.117 1.00 34.86  ? 2806 ILE A CB    1 
ATOM   11893 C  CG1   . ILE A 1 2806 ? 146.396 129.197 199.565 1.00 38.03  ? 2806 ILE A CG1   1 
ATOM   11894 C  CG2   . ILE A 1 2806 ? 146.620 127.447 201.302 1.00 37.91  ? 2806 ILE A CG2   1 
ATOM   11895 C  CD1   . ILE A 1 2806 ? 145.043 128.700 199.122 1.00 38.55  ? 2806 ILE A CD1   1 
ATOM   11896 N  N     . PHE A 1 2807 ? 150.346 126.964 200.111 1.00 45.61  ? 2807 PHE A N     1 
ATOM   11897 C  CA    . PHE A 1 2807 ? 151.295 125.923 200.494 1.00 49.61  ? 2807 PHE A CA    1 
ATOM   11898 C  C     . PHE A 1 2807 ? 152.437 126.486 201.329 1.00 52.67  ? 2807 PHE A C     1 
ATOM   11899 O  O     . PHE A 1 2807 ? 152.843 125.880 202.325 1.00 61.15  ? 2807 PHE A O     1 
ATOM   11900 C  CB    . PHE A 1 2807 ? 151.837 125.233 199.242 1.00 50.88  ? 2807 PHE A CB    1 
ATOM   11901 C  CG    . PHE A 1 2807 ? 152.814 124.132 199.529 1.00 56.52  ? 2807 PHE A CG    1 
ATOM   11902 C  CD1   . PHE A 1 2807 ? 152.431 123.019 200.254 1.00 59.95  ? 2807 PHE A CD1   1 
ATOM   11903 C  CD2   . PHE A 1 2807 ? 154.117 124.210 199.073 1.00 60.93  ? 2807 PHE A CD2   1 
ATOM   11904 C  CE1   . PHE A 1 2807 ? 153.328 122.005 200.517 1.00 62.68  ? 2807 PHE A CE1   1 
ATOM   11905 C  CE2   . PHE A 1 2807 ? 155.018 123.200 199.335 1.00 64.88  ? 2807 PHE A CE2   1 
ATOM   11906 C  CZ    . PHE A 1 2807 ? 154.623 122.097 200.057 1.00 65.28  ? 2807 PHE A CZ    1 
ATOM   11907 N  N     . GLU A 1 2808 ? 152.978 127.640 200.933 1.00 49.19  ? 2808 GLU A N     1 
ATOM   11908 C  CA    . GLU A 1 2808 ? 154.054 128.256 201.700 1.00 54.93  ? 2808 GLU A CA    1 
ATOM   11909 C  C     . GLU A 1 2808 ? 153.569 128.731 203.061 1.00 57.84  ? 2808 GLU A C     1 
ATOM   11910 O  O     . GLU A 1 2808 ? 154.324 128.677 204.038 1.00 64.62  ? 2808 GLU A O     1 
ATOM   11911 C  CB    . GLU A 1 2808 ? 154.667 129.421 200.923 1.00 50.86  ? 2808 GLU A CB    1 
ATOM   11912 C  CG    . GLU A 1 2808 ? 155.341 129.021 199.623 1.00 57.53  ? 2808 GLU A CG    1 
ATOM   11913 C  CD    . GLU A 1 2808 ? 156.691 128.363 199.833 1.00 75.47  ? 2808 GLU A CD    1 
ATOM   11914 O  OE1   . GLU A 1 2808 ? 157.173 128.334 200.985 1.00 77.35  ? 2808 GLU A OE1   1 
ATOM   11915 O  OE2   . GLU A 1 2808 ? 157.273 127.871 198.844 1.00 79.07  ? 2808 GLU A OE2   1 
ATOM   11916 N  N     . ALA A 1 2809 ? 152.326 129.203 203.148 1.00 51.18  ? 2809 ALA A N     1 
ATOM   11917 C  CA    . ALA A 1 2809 ? 151.796 129.621 204.438 1.00 51.63  ? 2809 ALA A CA    1 
ATOM   11918 C  C     . ALA A 1 2809 ? 151.438 128.449 205.342 1.00 59.82  ? 2809 ALA A C     1 
ATOM   11919 O  O     . ALA A 1 2809 ? 151.455 128.604 206.567 1.00 66.56  ? 2809 ALA A O     1 
ATOM   11920 C  CB    . ALA A 1 2809 ? 150.570 130.507 204.238 1.00 48.23  ? 2809 ALA A CB    1 
ATOM   11921 N  N     . LEU A 1 2810 ? 151.113 127.286 204.774 1.00 61.37  ? 2810 LEU A N     1 
ATOM   11922 C  CA    . LEU A 1 2810 ? 150.712 126.130 205.565 1.00 62.31  ? 2810 LEU A CA    1 
ATOM   11923 C  C     . LEU A 1 2810 ? 151.851 125.165 205.864 1.00 68.01  ? 2810 LEU A C     1 
ATOM   11924 O  O     . LEU A 1 2810 ? 151.709 124.332 206.765 1.00 75.19  ? 2810 LEU A O     1 
ATOM   11925 C  CB    . LEU A 1 2810 ? 149.598 125.359 204.846 1.00 54.01  ? 2810 LEU A CB    1 
ATOM   11926 C  CG    . LEU A 1 2810 ? 148.151 125.653 205.239 1.00 59.74  ? 2810 LEU A CG    1 
ATOM   11927 C  CD1   . LEU A 1 2810 ? 147.834 127.129 205.080 1.00 63.00  ? 2810 LEU A CD1   1 
ATOM   11928 C  CD2   . LEU A 1 2810 ? 147.205 124.809 204.407 1.00 50.86  ? 2810 LEU A CD2   1 
ATOM   11929 N  N     . ARG A 1 2811 ? 152.960 125.247 205.131 1.00 64.10  ? 2811 ARG A N     1 
ATOM   11930 C  CA    . ARG A 1 2811 ? 154.023 124.254 205.277 1.00 67.27  ? 2811 ARG A CA    1 
ATOM   11931 C  C     . ARG A 1 2811 ? 154.660 124.244 206.662 1.00 76.13  ? 2811 ARG A C     1 
ATOM   11932 O  O     . ARG A 1 2811 ? 154.755 123.158 207.260 1.00 79.99  ? 2811 ARG A O     1 
ATOM   11933 C  CB    . ARG A 1 2811 ? 155.072 124.465 204.181 1.00 67.47  ? 2811 ARG A CB    1 
ATOM   11934 C  CG    . ARG A 1 2811 ? 156.161 123.410 204.158 1.00 74.18  ? 2811 ARG A CG    1 
ATOM   11935 C  CD    . ARG A 1 2811 ? 157.033 123.555 202.926 1.00 78.83  ? 2811 ARG A CD    1 
ATOM   11936 N  NE    . ARG A 1 2811 ? 157.537 124.914 202.780 1.00 85.80  ? 2811 ARG A NE    1 
ATOM   11937 C  CZ    . ARG A 1 2811 ? 158.297 125.327 201.775 1.00 84.55  ? 2811 ARG A CZ    1 
ATOM   11938 N  NH1   . ARG A 1 2811 ? 158.666 124.505 200.806 1.00 81.12  ? 2811 ARG A NH1   1 
ATOM   11939 N  NH2   . ARG A 1 2811 ? 158.695 126.595 201.741 1.00 78.63  ? 2811 ARG A NH2   1 
ATOM   11940 N  N     . PRO A 1 2812 ? 155.110 125.369 207.231 1.00 80.32  ? 2812 PRO A N     1 
ATOM   11941 C  CA    . PRO A 1 2812 ? 155.762 125.282 208.547 1.00 81.54  ? 2812 PRO A CA    1 
ATOM   11942 C  C     . PRO A 1 2812 ? 154.787 125.055 209.686 1.00 84.41  ? 2812 PRO A C     1 
ATOM   11943 O  O     . PRO A 1 2812 ? 155.177 124.491 210.715 1.00 87.82  ? 2812 PRO A O     1 
ATOM   11944 C  CB    . PRO A 1 2812 ? 156.473 126.634 208.674 1.00 82.30  ? 2812 PRO A CB    1 
ATOM   11945 C  CG    . PRO A 1 2812 ? 155.628 127.557 207.886 1.00 79.76  ? 2812 PRO A CG    1 
ATOM   11946 C  CD    . PRO A 1 2812 ? 155.108 126.755 206.724 1.00 78.10  ? 2812 PRO A CD    1 
ATOM   11947 N  N     . LEU A 1 2813 ? 153.535 125.473 209.534 1.00 83.82  ? 2813 LEU A N     1 
ATOM   11948 C  CA    . LEU A 1 2813 ? 152.569 125.362 210.616 1.00 89.89  ? 2813 LEU A CA    1 
ATOM   11949 C  C     . LEU A 1 2813 ? 152.175 123.908 210.841 1.00 94.94  ? 2813 LEU A C     1 
ATOM   11950 O  O     . LEU A 1 2813 ? 151.909 123.164 209.893 1.00 96.96  ? 2813 LEU A O     1 
ATOM   11951 C  CB    . LEU A 1 2813 ? 151.336 126.205 210.305 1.00 89.09  ? 2813 LEU A CB    1 
ATOM   11952 C  CG    . LEU A 1 2813 ? 151.568 127.716 210.252 1.00 93.76  ? 2813 LEU A CG    1 
ATOM   11953 C  CD1   . LEU A 1 2813 ? 150.314 128.439 209.798 1.00 84.29  ? 2813 LEU A CD1   1 
ATOM   11954 C  CD2   . LEU A 1 2813 ? 152.025 128.236 211.606 1.00 100.46 ? 2813 LEU A CD2   1 
ATOM   11955 N  N     . GLU A 1 2814 ? 152.141 123.504 212.113 1.00 99.07  ? 2814 GLU A N     1 
ATOM   11956 C  CA    . GLU A 1 2814 ? 151.820 122.118 212.441 1.00 102.78 ? 2814 GLU A CA    1 
ATOM   11957 C  C     . GLU A 1 2814 ? 150.343 121.818 212.217 1.00 102.73 ? 2814 GLU A C     1 
ATOM   11958 O  O     . GLU A 1 2814 ? 149.996 120.763 211.674 1.00 103.47 ? 2814 GLU A O     1 
ATOM   11959 C  CB    . GLU A 1 2814 ? 152.216 121.816 213.885 1.00 109.73 ? 2814 GLU A CB    1 
ATOM   11960 C  CG    . GLU A 1 2814 ? 153.714 121.863 214.142 1.00 119.27 ? 2814 GLU A CG    1 
ATOM   11961 C  CD    . GLU A 1 2814 ? 154.466 120.761 213.422 1.00 125.55 ? 2814 GLU A CD    1 
ATOM   11962 O  OE1   . GLU A 1 2814 ? 153.892 119.666 213.240 1.00 124.74 ? 2814 GLU A OE1   1 
ATOM   11963 O  OE2   . GLU A 1 2814 ? 155.632 120.988 213.037 1.00 130.28 ? 2814 GLU A OE2   1 
ATOM   11964 N  N     . THR A 1 2815 ? 149.460 122.724 212.631 1.00 102.39 ? 2815 THR A N     1 
ATOM   11965 C  CA    . THR A 1 2815 ? 148.029 122.507 212.481 1.00 97.80  ? 2815 THR A CA    1 
ATOM   11966 C  C     . THR A 1 2815 ? 147.323 123.846 212.326 1.00 93.35  ? 2815 THR A C     1 
ATOM   11967 O  O     . THR A 1 2815 ? 147.785 124.872 212.833 1.00 94.15  ? 2815 THR A O     1 
ATOM   11968 C  CB    . THR A 1 2815 ? 147.444 121.743 213.676 1.00 96.93  ? 2815 THR A CB    1 
ATOM   11969 O  OG1   . THR A 1 2815 ? 146.026 121.614 213.516 1.00 96.02  ? 2815 THR A OG1   1 
ATOM   11970 C  CG2   . THR A 1 2815 ? 147.737 122.477 214.976 1.00 96.15  ? 2815 THR A CG2   1 
ATOM   11971 N  N     . LEU A 1 2816 ? 146.203 123.823 211.611 1.00 91.10  ? 2816 LEU A N     1 
ATOM   11972 C  CA    . LEU A 1 2816 ? 145.340 124.980 211.448 1.00 88.84  ? 2816 LEU A CA    1 
ATOM   11973 C  C     . LEU A 1 2816 ? 143.889 124.578 211.642 1.00 86.80  ? 2816 LEU A C     1 
ATOM   11974 O  O     . LEU A 1 2816 ? 143.511 123.436 211.363 1.00 90.16  ? 2816 LEU A O     1 
ATOM   11975 C  CB    . LEU A 1 2816 ? 145.483 125.620 210.057 1.00 87.46  ? 2816 LEU A CB    1 
ATOM   11976 C  CG    . LEU A 1 2816 ? 146.671 126.514 209.706 1.00 88.25  ? 2816 LEU A CG    1 
ATOM   11977 C  CD1   . LEU A 1 2816 ? 147.942 125.710 209.559 1.00 88.90  ? 2816 LEU A CD1   1 
ATOM   11978 C  CD2   . LEU A 1 2816 ? 146.374 127.290 208.435 1.00 68.88  ? 2816 LEU A CD2   1 
ATOM   11979 N  N     . PRO A 1 2817 ? 143.056 125.493 212.121 1.00 83.58  ? 2817 PRO A N     1 
ATOM   11980 C  CA    . PRO A 1 2817 ? 141.610 125.308 212.005 1.00 81.35  ? 2817 PRO A CA    1 
ATOM   11981 C  C     . PRO A 1 2817 ? 141.140 125.663 210.602 1.00 82.32  ? 2817 PRO A C     1 
ATOM   11982 O  O     . PRO A 1 2817 ? 141.879 126.223 209.791 1.00 81.81  ? 2817 PRO A O     1 
ATOM   11983 C  CB    . PRO A 1 2817 ? 141.044 126.279 213.044 1.00 80.90  ? 2817 PRO A CB    1 
ATOM   11984 C  CG    . PRO A 1 2817 ? 142.059 127.365 213.112 1.00 82.76  ? 2817 PRO A CG    1 
ATOM   11985 C  CD    . PRO A 1 2817 ? 143.399 126.712 212.876 1.00 84.71  ? 2817 PRO A CD    1 
ATOM   11986 N  N     . VAL A 1 2818 ? 139.882 125.319 210.326 1.00 80.78  ? 2818 VAL A N     1 
ATOM   11987 C  CA    . VAL A 1 2818 ? 139.307 125.616 209.017 1.00 76.59  ? 2818 VAL A CA    1 
ATOM   11988 C  C     . VAL A 1 2818 ? 139.238 127.122 208.791 1.00 76.83  ? 2818 VAL A C     1 
ATOM   11989 O  O     . VAL A 1 2818 ? 139.424 127.606 207.666 1.00 74.29  ? 2818 VAL A O     1 
ATOM   11990 C  CB    . VAL A 1 2818 ? 137.930 124.940 208.875 1.00 77.56  ? 2818 VAL A CB    1 
ATOM   11991 C  CG1   . VAL A 1 2818 ? 136.949 125.491 209.892 1.00 81.06  ? 2818 VAL A CG1   1 
ATOM   11992 C  CG2   . VAL A 1 2818 ? 137.394 125.121 207.466 1.00 77.71  ? 2818 VAL A CG2   1 
ATOM   11993 N  N     . GLU A 1 2819 ? 138.988 127.889 209.857 1.00 78.65  ? 2819 GLU A N     1 
ATOM   11994 C  CA    . GLU A 1 2819 ? 138.944 129.341 209.728 1.00 75.38  ? 2819 GLU A CA    1 
ATOM   11995 C  C     . GLU A 1 2819 ? 140.295 129.897 209.297 1.00 70.82  ? 2819 GLU A C     1 
ATOM   11996 O  O     . GLU A 1 2819 ? 140.357 130.835 208.496 1.00 72.80  ? 2819 GLU A O     1 
ATOM   11997 C  CB    . GLU A 1 2819 ? 138.493 129.979 211.042 1.00 80.26  ? 2819 GLU A CB    1 
ATOM   11998 C  CG    . GLU A 1 2819 ? 137.051 129.683 211.424 1.00 86.97  ? 2819 GLU A CG    1 
ATOM   11999 C  CD    . GLU A 1 2819 ? 136.885 128.344 212.112 1.00 94.45  ? 2819 GLU A CD    1 
ATOM   12000 O  OE1   . GLU A 1 2819 ? 137.906 127.666 212.352 1.00 92.02  ? 2819 GLU A OE1   1 
ATOM   12001 O  OE2   . GLU A 1 2819 ? 135.733 127.970 212.414 1.00 98.73  ? 2819 GLU A OE2   1 
ATOM   12002 N  N     . GLY A 1 2820 ? 141.388 129.335 209.815 1.00 65.60  ? 2820 GLY A N     1 
ATOM   12003 C  CA    . GLY A 1 2820 ? 142.705 129.784 209.392 1.00 65.00  ? 2820 GLY A CA    1 
ATOM   12004 C  C     . GLY A 1 2820 ? 142.978 129.497 207.927 1.00 64.12  ? 2820 GLY A C     1 
ATOM   12005 O  O     . GLY A 1 2820 ? 143.568 130.323 207.222 1.00 62.25  ? 2820 GLY A O     1 
ATOM   12006 N  N     . LEU A 1 2821 ? 142.558 128.323 207.450 1.00 69.42  ? 2821 LEU A N     1 
ATOM   12007 C  CA    . LEU A 1 2821 ? 142.728 127.999 206.038 1.00 63.93  ? 2821 LEU A CA    1 
ATOM   12008 C  C     . LEU A 1 2821 ? 141.913 128.936 205.158 1.00 59.03  ? 2821 LEU A C     1 
ATOM   12009 O  O     . LEU A 1 2821 ? 142.394 129.397 204.117 1.00 55.76  ? 2821 LEU A O     1 
ATOM   12010 C  CB    . LEU A 1 2821 ? 142.338 126.544 205.779 1.00 58.17  ? 2821 LEU A CB    1 
ATOM   12011 C  CG    . LEU A 1 2821 ? 142.309 126.121 204.311 1.00 52.64  ? 2821 LEU A CG    1 
ATOM   12012 C  CD1   . LEU A 1 2821 ? 143.705 126.167 203.718 1.00 56.54  ? 2821 LEU A CD1   1 
ATOM   12013 C  CD2   . LEU A 1 2821 ? 141.711 124.734 204.165 1.00 62.36  ? 2821 LEU A CD2   1 
ATOM   12014 N  N     . ILE A 1 2822 ? 140.679 129.240 205.562 1.00 59.27  ? 2822 ILE A N     1 
ATOM   12015 C  CA    . ILE A 1 2822 ? 139.870 130.175 204.786 1.00 51.33  ? 2822 ILE A CA    1 
ATOM   12016 C  C     . ILE A 1 2822 ? 140.479 131.572 204.824 1.00 57.09  ? 2822 ILE A C     1 
ATOM   12017 O  O     . ILE A 1 2822 ? 140.430 132.313 203.834 1.00 55.99  ? 2822 ILE A O     1 
ATOM   12018 C  CB    . ILE A 1 2822 ? 138.418 130.167 205.291 1.00 55.82  ? 2822 ILE A CB    1 
ATOM   12019 C  CG1   . ILE A 1 2822 ? 137.852 128.751 205.219 1.00 66.94  ? 2822 ILE A CG1   1 
ATOM   12020 C  CG2   . ILE A 1 2822 ? 137.564 131.105 204.465 1.00 57.19  ? 2822 ILE A CG2   1 
ATOM   12021 C  CD1   . ILE A 1 2822 ? 136.589 128.560 206.008 1.00 72.45  ? 2822 ILE A CD1   1 
ATOM   12022 N  N     . ARG A 1 2823 ? 141.070 131.954 205.959 1.00 58.76  ? 2823 ARG A N     1 
ATOM   12023 C  CA    . ARG A 1 2823 ? 141.705 133.263 206.064 1.00 51.89  ? 2823 ARG A CA    1 
ATOM   12024 C  C     . ARG A 1 2823 ? 142.907 133.373 205.135 1.00 48.78  ? 2823 ARG A C     1 
ATOM   12025 O  O     . ARG A 1 2823 ? 143.089 134.391 204.460 1.00 49.57  ? 2823 ARG A O     1 
ATOM   12026 C  CB    . ARG A 1 2823 ? 142.117 133.537 207.509 1.00 57.09  ? 2823 ARG A CB    1 
ATOM   12027 C  CG    . ARG A 1 2823 ? 142.553 134.969 207.752 1.00 62.42  ? 2823 ARG A CG    1 
ATOM   12028 C  CD    . ARG A 1 2823 ? 142.918 135.211 209.206 1.00 64.71  ? 2823 ARG A CD    1 
ATOM   12029 N  NE    . ARG A 1 2823 ? 143.249 136.609 209.455 1.00 71.78  ? 2823 ARG A NE    1 
ATOM   12030 C  CZ    . ARG A 1 2823 ? 142.370 137.602 209.473 1.00 71.48  ? 2823 ARG A CZ    1 
ATOM   12031 N  NH1   . ARG A 1 2823 ? 141.077 137.385 209.303 1.00 75.05  ? 2823 ARG A NH1   1 
ATOM   12032 N  NH2   . ARG A 1 2823 ? 142.800 138.844 209.671 1.00 78.78  ? 2823 ARG A NH2   1 
ATOM   12033 N  N     . ILE A 1 2824 ? 143.750 132.339 205.092 1.00 45.79  ? 2824 ILE A N     1 
ATOM   12034 C  CA    . ILE A 1 2824 ? 144.892 132.395 204.181 1.00 44.72  ? 2824 ILE A CA    1 
ATOM   12035 C  C     . ILE A 1 2824 ? 144.435 132.306 202.730 1.00 45.00  ? 2824 ILE A C     1 
ATOM   12036 O  O     . ILE A 1 2824 ? 145.050 132.908 201.840 1.00 48.55  ? 2824 ILE A O     1 
ATOM   12037 C  CB    . ILE A 1 2824 ? 145.941 131.320 204.526 1.00 41.80  ? 2824 ILE A CB    1 
ATOM   12038 C  CG1   . ILE A 1 2824 ? 147.234 131.601 203.764 1.00 42.57  ? 2824 ILE A CG1   1 
ATOM   12039 C  CG2   . ILE A 1 2824 ? 145.441 129.931 204.211 1.00 45.85  ? 2824 ILE A CG2   1 
ATOM   12040 C  CD1   . ILE A 1 2824 ? 147.920 132.879 204.172 1.00 50.82  ? 2824 ILE A CD1   1 
ATOM   12041 N  N     . TRP A 1 2825 ? 143.348 131.580 202.465 1.00 44.87  ? 2825 TRP A N     1 
ATOM   12042 C  CA    . TRP A 1 2825 ? 142.757 131.578 201.132 1.00 41.47  ? 2825 TRP A CA    1 
ATOM   12043 C  C     . TRP A 1 2825 ? 142.359 132.989 200.715 1.00 44.15  ? 2825 TRP A C     1 
ATOM   12044 O  O     . TRP A 1 2825 ? 142.694 133.446 199.616 1.00 43.53  ? 2825 TRP A O     1 
ATOM   12045 C  CB    . TRP A 1 2825 ? 141.554 130.632 201.121 1.00 40.91  ? 2825 TRP A CB    1 
ATOM   12046 C  CG    . TRP A 1 2825 ? 140.731 130.656 199.875 1.00 38.29  ? 2825 TRP A CG    1 
ATOM   12047 C  CD1   . TRP A 1 2825 ? 140.879 129.858 198.783 1.00 38.98  ? 2825 TRP A CD1   1 
ATOM   12048 C  CD2   . TRP A 1 2825 ? 139.608 131.503 199.605 1.00 40.04  ? 2825 TRP A CD2   1 
ATOM   12049 N  NE1   . TRP A 1 2825 ? 139.927 130.162 197.844 1.00 45.12  ? 2825 TRP A NE1   1 
ATOM   12050 C  CE2   . TRP A 1 2825 ? 139.136 131.171 198.323 1.00 39.24  ? 2825 TRP A CE2   1 
ATOM   12051 C  CE3   . TRP A 1 2825 ? 138.962 132.515 200.319 1.00 46.59  ? 2825 TRP A CE3   1 
ATOM   12052 C  CZ2   . TRP A 1 2825 ? 138.050 131.814 197.740 1.00 43.88  ? 2825 TRP A CZ2   1 
ATOM   12053 C  CZ3   . TRP A 1 2825 ? 137.884 133.152 199.738 1.00 46.12  ? 2825 TRP A CZ3   1 
ATOM   12054 C  CH2   . TRP A 1 2825 ? 137.439 132.800 198.462 1.00 45.40  ? 2825 TRP A CH2   1 
ATOM   12055 N  N     . ALA A 1 2826 ? 141.665 133.705 201.603 1.00 44.28  ? 2826 ALA A N     1 
ATOM   12056 C  CA    . ALA A 1 2826 ? 141.252 135.073 201.307 1.00 39.07  ? 2826 ALA A CA    1 
ATOM   12057 C  C     . ALA A 1 2826 ? 142.453 135.999 201.164 1.00 45.88  ? 2826 ALA A C     1 
ATOM   12058 O  O     . ALA A 1 2826 ? 142.452 136.902 200.322 1.00 50.10  ? 2826 ALA A O     1 
ATOM   12059 C  CB    . ALA A 1 2826 ? 140.310 135.583 202.395 1.00 44.17  ? 2826 ALA A CB    1 
ATOM   12060 N  N     . HIS A 1 2827 ? 143.483 135.799 201.988 1.00 46.30  ? 2827 HIS A N     1 
ATOM   12061 C  CA    . HIS A 1 2827 ? 144.685 136.622 201.898 1.00 41.36  ? 2827 HIS A CA    1 
ATOM   12062 C  C     . HIS A 1 2827 ? 145.359 136.461 200.542 1.00 42.21  ? 2827 HIS A C     1 
ATOM   12063 O  O     . HIS A 1 2827 ? 145.726 137.449 199.894 1.00 41.73  ? 2827 HIS A O     1 
ATOM   12064 C  CB    . HIS A 1 2827 ? 145.650 136.256 203.025 1.00 40.79  ? 2827 HIS A CB    1 
ATOM   12065 C  CG    . HIS A 1 2827 ? 146.952 136.992 202.971 1.00 45.52  ? 2827 HIS A CG    1 
ATOM   12066 N  ND1   . HIS A 1 2827 ? 147.034 138.366 203.014 1.00 49.41  ? 2827 HIS A ND1   1 
ATOM   12067 C  CD2   . HIS A 1 2827 ? 148.226 136.542 202.876 1.00 48.21  ? 2827 HIS A CD2   1 
ATOM   12068 C  CE1   . HIS A 1 2827 ? 148.301 138.732 202.949 1.00 51.29  ? 2827 HIS A CE1   1 
ATOM   12069 N  NE2   . HIS A 1 2827 ? 149.045 137.645 202.863 1.00 52.51  ? 2827 HIS A NE2   1 
ATOM   12070 N  N     . GLU A 1 2828 ? 145.526 135.217 200.091 1.00 42.01  ? 2828 GLU A N     1 
ATOM   12071 C  CA    . GLU A 1 2828 ? 146.144 134.988 198.790 1.00 36.69  ? 2828 GLU A CA    1 
ATOM   12072 C  C     . GLU A 1 2828 ? 145.264 135.509 197.661 1.00 39.74  ? 2828 GLU A C     1 
ATOM   12073 O  O     . GLU A 1 2828 ? 145.773 136.042 196.667 1.00 40.19  ? 2828 GLU A O     1 
ATOM   12074 C  CB    . GLU A 1 2828 ? 146.443 133.503 198.605 1.00 36.08  ? 2828 GLU A CB    1 
ATOM   12075 C  CG    . GLU A 1 2828 ? 147.417 132.950 199.622 1.00 41.17  ? 2828 GLU A CG    1 
ATOM   12076 C  CD    . GLU A 1 2828 ? 148.789 133.574 199.499 1.00 55.06  ? 2828 GLU A CD    1 
ATOM   12077 O  OE1   . GLU A 1 2828 ? 149.188 133.910 198.365 1.00 56.61  ? 2828 GLU A OE1   1 
ATOM   12078 O  OE2   . GLU A 1 2828 ? 149.467 133.732 200.536 1.00 59.86  ? 2828 GLU A OE2   1 
ATOM   12079 N  N     . ALA A 1 2829 ? 143.942 135.373 197.798 1.00 39.38  ? 2829 ALA A N     1 
ATOM   12080 C  CA    . ALA A 1 2829 ? 143.038 135.932 196.799 1.00 35.56  ? 2829 ALA A CA    1 
ATOM   12081 C  C     . ALA A 1 2829 ? 143.196 137.442 196.700 1.00 44.27  ? 2829 ALA A C     1 
ATOM   12082 O  O     . ALA A 1 2829 ? 143.229 138.000 195.598 1.00 46.85  ? 2829 ALA A O     1 
ATOM   12083 C  CB    . ALA A 1 2829 ? 141.594 135.569 197.137 1.00 34.00  ? 2829 ALA A CB    1 
ATOM   12084 N  N     . LEU A 1 2830 ? 143.295 138.119 197.845 1.00 45.43  ? 2830 LEU A N     1 
ATOM   12085 C  CA    . LEU A 1 2830 ? 143.495 139.564 197.850 1.00 36.68  ? 2830 LEU A CA    1 
ATOM   12086 C  C     . LEU A 1 2830 ? 144.827 139.934 197.213 1.00 36.32  ? 2830 LEU A C     1 
ATOM   12087 O  O     . LEU A 1 2830 ? 144.914 140.892 196.438 1.00 39.68  ? 2830 LEU A O     1 
ATOM   12088 C  CB    . LEU A 1 2830 ? 143.421 140.093 199.281 1.00 36.29  ? 2830 LEU A CB    1 
ATOM   12089 C  CG    . LEU A 1 2830 ? 142.041 140.153 199.933 1.00 37.66  ? 2830 LEU A CG    1 
ATOM   12090 C  CD1   . LEU A 1 2830 ? 142.172 140.396 201.424 1.00 43.72  ? 2830 LEU A CD1   1 
ATOM   12091 C  CD2   . LEU A 1 2830 ? 141.201 141.235 199.290 1.00 43.08  ? 2830 LEU A CD2   1 
ATOM   12092 N  N     . ARG A 1 2831 ? 145.882 139.181 197.532 1.00 37.12  ? 2831 ARG A N     1 
ATOM   12093 C  CA    . ARG A 1 2831 ? 147.206 139.523 197.023 1.00 36.68  ? 2831 ARG A CA    1 
ATOM   12094 C  C     . ARG A 1 2831 ? 147.327 139.260 195.528 1.00 36.68  ? 2831 ARG A C     1 
ATOM   12095 O  O     . ARG A 1 2831 ? 148.124 139.914 194.849 1.00 34.71  ? 2831 ARG A O     1 
ATOM   12096 C  CB    . ARG A 1 2831 ? 148.281 138.750 197.785 1.00 34.01  ? 2831 ARG A CB    1 
ATOM   12097 C  CG    . ARG A 1 2831 ? 148.344 139.060 199.273 1.00 36.21  ? 2831 ARG A CG    1 
ATOM   12098 C  CD    . ARG A 1 2831 ? 149.064 140.372 199.560 1.00 38.96  ? 2831 ARG A CD    1 
ATOM   12099 N  NE    . ARG A 1 2831 ? 148.222 141.540 199.330 1.00 44.49  ? 2831 ARG A NE    1 
ATOM   12100 C  CZ    . ARG A 1 2831 ? 147.188 141.887 200.085 1.00 44.43  ? 2831 ARG A CZ    1 
ATOM   12101 N  NH1   . ARG A 1 2831 ? 146.849 141.193 201.158 1.00 45.63  ? 2831 ARG A NH1   1 
ATOM   12102 N  NH2   . ARG A 1 2831 ? 146.478 142.962 199.755 1.00 39.00  ? 2831 ARG A NH2   1 
ATOM   12103 N  N     . LEU A 1 2832 ? 146.555 138.313 194.997 1.00 37.39  ? 2832 LEU A N     1 
ATOM   12104 C  CA    . LEU A 1 2832 ? 146.672 137.965 193.587 1.00 37.45  ? 2832 LEU A CA    1 
ATOM   12105 C  C     . LEU A 1 2832 ? 145.663 138.671 192.693 1.00 37.80  ? 2832 LEU A C     1 
ATOM   12106 O  O     . LEU A 1 2832 ? 145.941 138.856 191.503 1.00 38.81  ? 2832 LEU A O     1 
ATOM   12107 C  CB    . LEU A 1 2832 ? 146.522 136.455 193.402 1.00 35.64  ? 2832 LEU A CB    1 
ATOM   12108 C  CG    . LEU A 1 2832 ? 147.684 135.604 193.905 1.00 30.52  ? 2832 LEU A CG    1 
ATOM   12109 C  CD1   . LEU A 1 2832 ? 147.425 134.167 193.562 1.00 25.75  ? 2832 LEU A CD1   1 
ATOM   12110 C  CD2   . LEU A 1 2832 ? 148.991 136.069 193.292 1.00 30.38  ? 2832 LEU A CD2   1 
ATOM   12111 N  N     . PHE A 1 2833 ? 144.510 139.070 193.222 1.00 39.58  ? 2833 PHE A N     1 
ATOM   12112 C  CA    . PHE A 1 2833 ? 143.440 139.623 192.402 1.00 36.89  ? 2833 PHE A CA    1 
ATOM   12113 C  C     . PHE A 1 2833 ? 143.163 141.087 192.698 1.00 39.98  ? 2833 PHE A C     1 
ATOM   12114 O  O     . PHE A 1 2833 ? 143.058 141.891 191.765 1.00 44.13  ? 2833 PHE A O     1 
ATOM   12115 C  CB    . PHE A 1 2833 ? 142.162 138.794 192.597 1.00 37.97  ? 2833 PHE A CB    1 
ATOM   12116 C  CG    . PHE A 1 2833 ? 142.258 137.402 192.044 1.00 44.66  ? 2833 PHE A CG    1 
ATOM   12117 C  CD1   . PHE A 1 2833 ? 142.238 137.182 190.679 1.00 47.30  ? 2833 PHE A CD1   1 
ATOM   12118 C  CD2   . PHE A 1 2833 ? 142.390 136.315 192.887 1.00 40.44  ? 2833 PHE A CD2   1 
ATOM   12119 C  CE1   . PHE A 1 2833 ? 142.332 135.907 190.168 1.00 38.77  ? 2833 PHE A CE1   1 
ATOM   12120 C  CE2   . PHE A 1 2833 ? 142.486 135.039 192.380 1.00 39.63  ? 2833 PHE A CE2   1 
ATOM   12121 C  CZ    . PHE A 1 2833 ? 142.458 134.835 191.019 1.00 39.52  ? 2833 PHE A CZ    1 
ATOM   12122 N  N     . GLN A 1 2834 ? 143.040 141.460 193.973 1.00 39.72  ? 2834 GLN A N     1 
ATOM   12123 C  CA    . GLN A 1 2834 ? 142.707 142.839 194.313 1.00 37.83  ? 2834 GLN A CA    1 
ATOM   12124 C  C     . GLN A 1 2834 ? 143.886 143.781 194.099 1.00 38.70  ? 2834 GLN A C     1 
ATOM   12125 O  O     . GLN A 1 2834 ? 143.685 144.973 193.844 1.00 45.53  ? 2834 GLN A O     1 
ATOM   12126 C  CB    . GLN A 1 2834 ? 142.224 142.912 195.761 1.00 36.84  ? 2834 GLN A CB    1 
ATOM   12127 C  CG    . GLN A 1 2834 ? 141.794 144.294 196.205 1.00 40.76  ? 2834 GLN A CG    1 
ATOM   12128 C  CD    . GLN A 1 2834 ? 141.070 144.281 197.529 1.00 48.84  ? 2834 GLN A CD    1 
ATOM   12129 O  OE1   . GLN A 1 2834 ? 139.956 143.774 197.635 1.00 52.79  ? 2834 GLN A OE1   1 
ATOM   12130 N  NE2   . GLN A 1 2834 ? 141.705 144.832 198.555 1.00 54.93  ? 2834 GLN A NE2   1 
ATOM   12131 N  N     . ASP A 1 2835 ? 145.113 143.270 194.194 1.00 37.33  ? 2835 ASP A N     1 
ATOM   12132 C  CA    . ASP A 1 2835 ? 146.289 144.130 194.109 1.00 38.92  ? 2835 ASP A CA    1 
ATOM   12133 C  C     . ASP A 1 2835 ? 146.417 144.777 192.736 1.00 40.30  ? 2835 ASP A C     1 
ATOM   12134 O  O     . ASP A 1 2835 ? 146.797 145.948 192.629 1.00 43.39  ? 2835 ASP A O     1 
ATOM   12135 C  CB    . ASP A 1 2835 ? 147.542 143.324 194.437 1.00 41.23  ? 2835 ASP A CB    1 
ATOM   12136 C  CG    . ASP A 1 2835 ? 147.764 143.179 195.923 1.00 50.33  ? 2835 ASP A CG    1 
ATOM   12137 O  OD1   . ASP A 1 2835 ? 146.850 143.529 196.699 1.00 44.56  ? 2835 ASP A OD1   1 
ATOM   12138 O  OD2   . ASP A 1 2835 ? 148.848 142.700 196.316 1.00 55.45  ? 2835 ASP A OD2   1 
ATOM   12139 N  N     . ARG A 1 2836 ? 146.112 144.030 191.674 1.00 35.22  ? 2836 ARG A N     1 
ATOM   12140 C  CA    . ARG A 1 2836 ? 146.264 144.546 190.320 1.00 32.54  ? 2836 ARG A CA    1 
ATOM   12141 C  C     . ARG A 1 2836 ? 145.221 145.599 189.969 1.00 40.22  ? 2836 ARG A C     1 
ATOM   12142 O  O     . ARG A 1 2836 ? 145.398 146.319 188.981 1.00 42.88  ? 2836 ARG A O     1 
ATOM   12143 C  CB    . ARG A 1 2836 ? 146.182 143.396 189.318 1.00 37.85  ? 2836 ARG A CB    1 
ATOM   12144 C  CG    . ARG A 1 2836 ? 144.763 142.924 189.069 1.00 42.90  ? 2836 ARG A CG    1 
ATOM   12145 C  CD    . ARG A 1 2836 ? 144.676 141.887 187.969 1.00 39.63  ? 2836 ARG A CD    1 
ATOM   12146 N  NE    . ARG A 1 2836 ? 145.122 140.576 188.420 1.00 41.67  ? 2836 ARG A NE    1 
ATOM   12147 C  CZ    . ARG A 1 2836 ? 145.888 139.760 187.711 1.00 44.75  ? 2836 ARG A CZ    1 
ATOM   12148 N  NH1   . ARG A 1 2836 ? 146.286 140.074 186.491 1.00 44.25  ? 2836 ARG A NH1   1 
ATOM   12149 N  NH2   . ARG A 1 2836 ? 146.253 138.594 188.235 1.00 43.93  ? 2836 ARG A NH2   1 
ATOM   12150 N  N     . LEU A 1 2837 ? 144.149 145.709 190.749 1.00 39.41  ? 2837 LEU A N     1 
ATOM   12151 C  CA    . LEU A 1 2837 ? 143.018 146.543 190.365 1.00 35.28  ? 2837 LEU A CA    1 
ATOM   12152 C  C     . LEU A 1 2837 ? 143.348 148.021 190.524 1.00 41.08  ? 2837 LEU A C     1 
ATOM   12153 O  O     . LEU A 1 2837 ? 143.964 148.431 191.511 1.00 47.74  ? 2837 LEU A O     1 
ATOM   12154 C  CB    . LEU A 1 2837 ? 141.795 146.178 191.200 1.00 35.87  ? 2837 LEU A CB    1 
ATOM   12155 C  CG    . LEU A 1 2837 ? 141.354 144.725 191.045 1.00 36.26  ? 2837 LEU A CG    1 
ATOM   12156 C  CD1   . LEU A 1 2837 ? 140.084 144.467 191.821 1.00 41.14  ? 2837 LEU A CD1   1 
ATOM   12157 C  CD2   . LEU A 1 2837 ? 141.165 144.388 189.582 1.00 39.65  ? 2837 LEU A CD2   1 
ATOM   12158 N  N     . VAL A 1 2838 ? 142.925 148.821 189.549 1.00 41.96  ? 2838 VAL A N     1 
ATOM   12159 C  CA    . VAL A 1 2838 ? 143.221 150.250 189.532 1.00 40.82  ? 2838 VAL A CA    1 
ATOM   12160 C  C     . VAL A 1 2838 ? 142.156 151.052 190.268 1.00 50.23  ? 2838 VAL A C     1 
ATOM   12161 O  O     . VAL A 1 2838 ? 142.466 151.844 191.161 1.00 60.39  ? 2838 VAL A O     1 
ATOM   12162 C  CB    . VAL A 1 2838 ? 143.380 150.733 188.076 1.00 41.41  ? 2838 VAL A CB    1 
ATOM   12163 C  CG1   . VAL A 1 2838 ? 143.482 152.244 188.027 1.00 42.89  ? 2838 VAL A CG1   1 
ATOM   12164 C  CG2   . VAL A 1 2838 ? 144.591 150.090 187.434 1.00 45.64  ? 2838 VAL A CG2   1 
ATOM   12165 N  N     . GLU A 1 2839 ? 140.889 150.870 189.906 1.00 54.41  ? 2839 GLU A N     1 
ATOM   12166 C  CA    . GLU A 1 2839 ? 139.815 151.662 190.484 1.00 58.28  ? 2839 GLU A CA    1 
ATOM   12167 C  C     . GLU A 1 2839 ? 139.365 151.087 191.825 1.00 62.33  ? 2839 GLU A C     1 
ATOM   12168 O  O     . GLU A 1 2839 ? 139.604 149.921 192.147 1.00 61.00  ? 2839 GLU A O     1 
ATOM   12169 C  CB    . GLU A 1 2839 ? 138.630 151.748 189.522 1.00 60.21  ? 2839 GLU A CB    1 
ATOM   12170 C  CG    . GLU A 1 2839 ? 138.909 152.542 188.252 1.00 65.40  ? 2839 GLU A CG    1 
ATOM   12171 C  CD    . GLU A 1 2839 ? 139.614 151.729 187.185 1.00 72.53  ? 2839 GLU A CD    1 
ATOM   12172 O  OE1   . GLU A 1 2839 ? 139.838 150.521 187.404 1.00 69.50  ? 2839 GLU A OE1   1 
ATOM   12173 O  OE2   . GLU A 1 2839 ? 139.947 152.301 186.126 1.00 72.04  ? 2839 GLU A OE2   1 
ATOM   12174 N  N     . ASP A 1 2840 ? 138.701 151.937 192.610 1.00 65.77  ? 2840 ASP A N     1 
ATOM   12175 C  CA    . ASP A 1 2840 ? 138.249 151.573 193.947 1.00 68.01  ? 2840 ASP A CA    1 
ATOM   12176 C  C     . ASP A 1 2840 ? 137.034 150.657 193.940 1.00 68.40  ? 2840 ASP A C     1 
ATOM   12177 O  O     . ASP A 1 2840 ? 136.937 149.765 194.793 1.00 70.91  ? 2840 ASP A O     1 
ATOM   12178 C  CB    . ASP A 1 2840 ? 137.920 152.834 194.753 1.00 73.68  ? 2840 ASP A CB    1 
ATOM   12179 C  CG    . ASP A 1 2840 ? 139.152 153.650 195.093 1.00 81.59  ? 2840 ASP A CG    1 
ATOM   12180 O  OD1   . ASP A 1 2840 ? 140.243 153.059 195.227 1.00 77.53  ? 2840 ASP A OD1   1 
ATOM   12181 O  OD2   . ASP A 1 2840 ? 139.029 154.885 195.228 1.00 84.93  ? 2840 ASP A OD2   1 
ATOM   12182 N  N     . GLU A 1 2841 ? 136.100 150.861 193.009 1.00 66.61  ? 2841 GLU A N     1 
ATOM   12183 C  CA    . GLU A 1 2841 ? 134.908 150.021 192.970 1.00 65.56  ? 2841 GLU A CA    1 
ATOM   12184 C  C     . GLU A 1 2841 ? 135.260 148.581 192.618 1.00 69.18  ? 2841 GLU A C     1 
ATOM   12185 O  O     . GLU A 1 2841 ? 134.621 147.642 193.105 1.00 72.25  ? 2841 GLU A O     1 
ATOM   12186 C  CB    . GLU A 1 2841 ? 133.884 150.598 191.989 1.00 68.49  ? 2841 GLU A CB    1 
ATOM   12187 C  CG    . GLU A 1 2841 ? 134.081 150.199 190.536 1.00 71.98  ? 2841 GLU A CG    1 
ATOM   12188 C  CD    . GLU A 1 2841 ? 134.884 151.221 189.758 1.00 77.82  ? 2841 GLU A CD    1 
ATOM   12189 O  OE1   . GLU A 1 2841 ? 135.186 150.964 188.573 1.00 75.40  ? 2841 GLU A OE1   1 
ATOM   12190 O  OE2   . GLU A 1 2841 ? 135.211 152.281 190.330 1.00 78.12  ? 2841 GLU A OE2   1 
ATOM   12191 N  N     . GLU A 1 2842 ? 136.287 148.384 191.787 1.00 64.47  ? 2842 GLU A N     1 
ATOM   12192 C  CA    . GLU A 1 2842 ? 136.740 147.032 191.478 1.00 56.77  ? 2842 GLU A CA    1 
ATOM   12193 C  C     . GLU A 1 2842 ? 137.309 146.345 192.712 1.00 56.70  ? 2842 GLU A C     1 
ATOM   12194 O  O     . GLU A 1 2842 ? 137.032 145.164 192.960 1.00 59.64  ? 2842 GLU A O     1 
ATOM   12195 C  CB    . GLU A 1 2842 ? 137.776 147.078 190.358 1.00 51.57  ? 2842 GLU A CB    1 
ATOM   12196 C  CG    . GLU A 1 2842 ? 137.300 147.818 189.125 1.00 59.79  ? 2842 GLU A CG    1 
ATOM   12197 C  CD    . GLU A 1 2842 ? 138.339 147.853 188.028 1.00 58.65  ? 2842 GLU A CD    1 
ATOM   12198 O  OE1   . GLU A 1 2842 ? 139.425 147.273 188.219 1.00 55.16  ? 2842 GLU A OE1   1 
ATOM   12199 O  OE2   . GLU A 1 2842 ? 138.065 148.453 186.969 1.00 66.84  ? 2842 GLU A OE2   1 
ATOM   12200 N  N     . ARG A 1 2843 ? 138.107 147.069 193.499 1.00 51.25  ? 2843 ARG A N     1 
ATOM   12201 C  CA    . ARG A 1 2843 ? 138.646 146.502 194.729 1.00 47.44  ? 2843 ARG A CA    1 
ATOM   12202 C  C     . ARG A 1 2843 ? 137.534 146.175 195.715 1.00 54.70  ? 2843 ARG A C     1 
ATOM   12203 O  O     . ARG A 1 2843 ? 137.569 145.133 196.381 1.00 62.43  ? 2843 ARG A O     1 
ATOM   12204 C  CB    . ARG A 1 2843 ? 139.651 147.469 195.352 1.00 51.10  ? 2843 ARG A CB    1 
ATOM   12205 C  CG    . ARG A 1 2843 ? 140.995 147.497 194.653 1.00 55.66  ? 2843 ARG A CG    1 
ATOM   12206 C  CD    . ARG A 1 2843 ? 141.947 148.459 195.333 1.00 52.87  ? 2843 ARG A CD    1 
ATOM   12207 N  NE    . ARG A 1 2843 ? 142.216 149.627 194.506 1.00 63.52  ? 2843 ARG A NE    1 
ATOM   12208 C  CZ    . ARG A 1 2843 ? 142.315 150.865 194.969 1.00 71.74  ? 2843 ARG A CZ    1 
ATOM   12209 N  NH1   . ARG A 1 2843 ? 142.158 151.137 196.254 1.00 78.59  ? 2843 ARG A NH1   1 
ATOM   12210 N  NH2   . ARG A 1 2843 ? 142.575 151.856 194.121 1.00 64.44  ? 2843 ARG A NH2   1 
ATOM   12211 N  N     . ARG A 1 2844 ? 136.536 147.055 195.822 1.00 56.95  ? 2844 ARG A N     1 
ATOM   12212 C  CA    . ARG A 1 2844 ? 135.398 146.783 196.695 1.00 58.76  ? 2844 ARG A CA    1 
ATOM   12213 C  C     . ARG A 1 2844 ? 134.635 145.545 196.238 1.00 64.06  ? 2844 ARG A C     1 
ATOM   12214 O  O     . ARG A 1 2844 ? 134.252 144.701 197.059 1.00 67.89  ? 2844 ARG A O     1 
ATOM   12215 C  CB    . ARG A 1 2844 ? 134.481 148.005 196.735 1.00 65.96  ? 2844 ARG A CB    1 
ATOM   12216 C  CG    . ARG A 1 2844 ? 133.429 147.980 197.826 1.00 73.25  ? 2844 ARG A CG    1 
ATOM   12217 C  CD    . ARG A 1 2844 ? 132.124 148.595 197.341 1.00 81.61  ? 2844 ARG A CD    1 
ATOM   12218 N  NE    . ARG A 1 2844 ? 131.311 147.649 196.584 1.00 87.39  ? 2844 ARG A NE    1 
ATOM   12219 C  CZ    . ARG A 1 2844 ? 130.945 147.816 195.320 1.00 84.62  ? 2844 ARG A CZ    1 
ATOM   12220 N  NH1   . ARG A 1 2844 ? 131.306 148.886 194.631 1.00 80.51  ? 2844 ARG A NH1   1 
ATOM   12221 N  NH2   . ARG A 1 2844 ? 130.197 146.887 194.733 1.00 76.96  ? 2844 ARG A NH2   1 
ATOM   12222 N  N     . TRP A 1 2845 ? 134.417 145.417 194.928 1.00 63.91  ? 2845 TRP A N     1 
ATOM   12223 C  CA    . TRP A 1 2845 ? 133.743 144.245 194.379 1.00 63.87  ? 2845 TRP A CA    1 
ATOM   12224 C  C     . TRP A 1 2845 ? 134.509 142.970 194.704 1.00 61.24  ? 2845 TRP A C     1 
ATOM   12225 O  O     . TRP A 1 2845 ? 133.923 141.969 195.134 1.00 59.80  ? 2845 TRP A O     1 
ATOM   12226 C  CB    . TRP A 1 2845 ? 133.590 144.413 192.866 1.00 63.05  ? 2845 TRP A CB    1 
ATOM   12227 C  CG    . TRP A 1 2845 ? 132.932 143.266 192.166 1.00 68.43  ? 2845 TRP A CG    1 
ATOM   12228 C  CD1   . TRP A 1 2845 ? 131.605 143.128 191.885 1.00 69.36  ? 2845 TRP A CD1   1 
ATOM   12229 C  CD2   . TRP A 1 2845 ? 133.578 142.102 191.639 1.00 67.90  ? 2845 TRP A CD2   1 
ATOM   12230 N  NE1   . TRP A 1 2845 ? 131.384 141.946 191.222 1.00 69.42  ? 2845 TRP A NE1   1 
ATOM   12231 C  CE2   . TRP A 1 2845 ? 132.581 141.300 191.054 1.00 69.32  ? 2845 TRP A CE2   1 
ATOM   12232 C  CE3   . TRP A 1 2845 ? 134.903 141.660 191.605 1.00 62.44  ? 2845 TRP A CE3   1 
ATOM   12233 C  CZ2   . TRP A 1 2845 ? 132.865 140.077 190.454 1.00 66.08  ? 2845 TRP A CZ2   1 
ATOM   12234 C  CZ3   . TRP A 1 2845 ? 135.183 140.449 191.005 1.00 57.49  ? 2845 TRP A CZ3   1 
ATOM   12235 C  CH2   . TRP A 1 2845 ? 134.170 139.672 190.439 1.00 60.20  ? 2845 TRP A CH2   1 
ATOM   12236 N  N     . THR A 1 2846 ? 135.829 142.994 194.505 1.00 59.45  ? 2846 THR A N     1 
ATOM   12237 C  CA    . THR A 1 2846 ? 136.646 141.821 194.801 1.00 52.14  ? 2846 THR A CA    1 
ATOM   12238 C  C     . THR A 1 2846 ? 136.585 141.465 196.280 1.00 53.23  ? 2846 THR A C     1 
ATOM   12239 O  O     . THR A 1 2846 ? 136.465 140.287 196.640 1.00 58.93  ? 2846 THR A O     1 
ATOM   12240 C  CB    . THR A 1 2846 ? 138.091 142.068 194.368 1.00 44.84  ? 2846 THR A CB    1 
ATOM   12241 O  OG1   . THR A 1 2846 ? 138.156 142.151 192.940 1.00 50.14  ? 2846 THR A OG1   1 
ATOM   12242 C  CG2   . THR A 1 2846 ? 138.992 140.946 194.842 1.00 43.59  ? 2846 THR A CG2   1 
ATOM   12243 N  N     . ASP A 1 2847 ? 136.656 142.471 197.155 1.00 57.15  ? 2847 ASP A N     1 
ATOM   12244 C  CA    . ASP A 1 2847 ? 136.627 142.201 198.588 1.00 60.19  ? 2847 ASP A CA    1 
ATOM   12245 C  C     . ASP A 1 2847 ? 135.295 141.595 199.017 1.00 65.05  ? 2847 ASP A C     1 
ATOM   12246 O  O     . ASP A 1 2847 ? 135.269 140.652 199.815 1.00 69.98  ? 2847 ASP A O     1 
ATOM   12247 C  CB    . ASP A 1 2847 ? 136.918 143.479 199.372 1.00 70.98  ? 2847 ASP A CB    1 
ATOM   12248 C  CG    . ASP A 1 2847 ? 137.715 143.215 200.634 1.00 86.84  ? 2847 ASP A CG    1 
ATOM   12249 O  OD1   . ASP A 1 2847 ? 137.417 142.220 201.328 1.00 94.07  ? 2847 ASP A OD1   1 
ATOM   12250 O  OD2   . ASP A 1 2847 ? 138.643 143.997 200.931 1.00 86.05  ? 2847 ASP A OD2   1 
ATOM   12251 N  N     . GLU A 1 2848 ? 134.176 142.121 198.508 1.00 67.23  ? 2848 GLU A N     1 
ATOM   12252 C  CA    . GLU A 1 2848 ? 132.885 141.529 198.861 1.00 69.50  ? 2848 GLU A CA    1 
ATOM   12253 C  C     . GLU A 1 2848 ? 132.737 140.121 198.296 1.00 67.39  ? 2848 GLU A C     1 
ATOM   12254 O  O     . GLU A 1 2848 ? 132.204 139.228 198.968 1.00 65.83  ? 2848 GLU A O     1 
ATOM   12255 C  CB    . GLU A 1 2848 ? 131.723 142.403 198.386 1.00 72.80  ? 2848 GLU A CB    1 
ATOM   12256 C  CG    . GLU A 1 2848 ? 131.829 143.880 198.700 1.00 79.31  ? 2848 GLU A CG    1 
ATOM   12257 C  CD    . GLU A 1 2848 ? 130.767 144.689 197.979 1.00 85.27  ? 2848 GLU A CD    1 
ATOM   12258 O  OE1   . GLU A 1 2848 ? 130.015 144.094 197.177 1.00 83.98  ? 2848 GLU A OE1   1 
ATOM   12259 O  OE2   . GLU A 1 2848 ? 130.672 145.910 198.222 1.00 83.72  ? 2848 GLU A OE2   1 
ATOM   12260 N  N     . ASN A 1 2849 ? 133.186 139.898 197.061 1.00 65.76  ? 2849 ASN A N     1 
ATOM   12261 C  CA    . ASN A 1 2849 ? 132.977 138.590 196.455 1.00 61.57  ? 2849 ASN A CA    1 
ATOM   12262 C  C     . ASN A 1 2849 ? 133.901 137.525 197.023 1.00 58.33  ? 2849 ASN A C     1 
ATOM   12263 O  O     . ASN A 1 2849 ? 133.559 136.342 196.962 1.00 65.52  ? 2849 ASN A O     1 
ATOM   12264 C  CB    . ASN A 1 2849 ? 133.121 138.689 194.942 1.00 62.73  ? 2849 ASN A CB    1 
ATOM   12265 C  CG    . ASN A 1 2849 ? 131.856 139.190 194.284 1.00 72.42  ? 2849 ASN A CG    1 
ATOM   12266 O  OD1   . ASN A 1 2849 ? 131.871 140.171 193.550 1.00 71.38  ? 2849 ASN A OD1   1 
ATOM   12267 N  ND2   . ASN A 1 2849 ? 130.746 138.513 194.549 1.00 71.42  ? 2849 ASN A ND2   1 
ATOM   12268 N  N     . ILE A 1 2850 ? 135.042 137.906 197.597 1.00 59.19  ? 2850 ILE A N     1 
ATOM   12269 C  CA    . ILE A 1 2850 ? 135.836 136.934 198.346 1.00 56.79  ? 2850 ILE A CA    1 
ATOM   12270 C  C     . ILE A 1 2850 ? 135.022 136.384 199.512 1.00 61.76  ? 2850 ILE A C     1 
ATOM   12271 O  O     . ILE A 1 2850 ? 134.955 135.167 199.730 1.00 66.77  ? 2850 ILE A O     1 
ATOM   12272 C  CB    . ILE A 1 2850 ? 137.156 137.565 198.820 1.00 59.61  ? 2850 ILE A CB    1 
ATOM   12273 C  CG1   . ILE A 1 2850 ? 138.146 137.642 197.659 1.00 56.12  ? 2850 ILE A CG1   1 
ATOM   12274 C  CG2   . ILE A 1 2850 ? 137.745 136.778 199.974 1.00 60.87  ? 2850 ILE A CG2   1 
ATOM   12275 C  CD1   . ILE A 1 2850 ? 139.376 138.446 197.962 1.00 55.99  ? 2850 ILE A CD1   1 
ATOM   12276 N  N     . ASP A 1 2851 ? 134.367 137.276 200.260 1.00 63.14  ? 2851 ASP A N     1 
ATOM   12277 C  CA    . ASP A 1 2851 ? 133.470 136.841 201.326 1.00 66.47  ? 2851 ASP A CA    1 
ATOM   12278 C  C     . ASP A 1 2851 ? 132.332 135.993 200.778 1.00 66.33  ? 2851 ASP A C     1 
ATOM   12279 O  O     . ASP A 1 2851 ? 131.964 134.976 201.375 1.00 68.13  ? 2851 ASP A O     1 
ATOM   12280 C  CB    . ASP A 1 2851 ? 132.902 138.051 202.066 1.00 74.05  ? 2851 ASP A CB    1 
ATOM   12281 C  CG    . ASP A 1 2851 ? 133.947 138.797 202.860 1.00 83.46  ? 2851 ASP A CG    1 
ATOM   12282 O  OD1   . ASP A 1 2851 ? 133.914 138.694 204.101 1.00 85.90  ? 2851 ASP A OD1   1 
ATOM   12283 O  OD2   . ASP A 1 2851 ? 134.796 139.479 202.254 1.00 82.08  ? 2851 ASP A OD2   1 
ATOM   12284 N  N     . THR A 1 2852 ? 131.746 136.413 199.656 1.00 61.73  ? 2852 THR A N     1 
ATOM   12285 C  CA    . THR A 1 2852 ? 130.620 135.676 199.090 1.00 57.65  ? 2852 THR A CA    1 
ATOM   12286 C  C     . THR A 1 2852 ? 131.017 134.245 198.748 1.00 60.23  ? 2852 THR A C     1 
ATOM   12287 O  O     . THR A 1 2852 ? 130.317 133.291 199.107 1.00 67.14  ? 2852 THR A O     1 
ATOM   12288 C  CB    . THR A 1 2852 ? 130.089 136.398 197.852 1.00 62.21  ? 2852 THR A CB    1 
ATOM   12289 O  OG1   . THR A 1 2852 ? 129.766 137.753 198.189 1.00 69.61  ? 2852 THR A OG1   1 
ATOM   12290 C  CG2   . THR A 1 2852 ? 128.847 135.703 197.326 1.00 61.12  ? 2852 THR A CG2   1 
ATOM   12291 N  N     . VAL A 1 2853 ? 132.155 134.077 198.072 1.00 56.99  ? 2853 VAL A N     1 
ATOM   12292 C  CA    . VAL A 1 2853 ? 132.624 132.746 197.702 1.00 52.93  ? 2853 VAL A CA    1 
ATOM   12293 C  C     . VAL A 1 2853 ? 132.967 131.930 198.943 1.00 58.29  ? 2853 VAL A C     1 
ATOM   12294 O  O     . VAL A 1 2853 ? 132.638 130.739 199.029 1.00 63.35  ? 2853 VAL A O     1 
ATOM   12295 C  CB    . VAL A 1 2853 ? 133.822 132.854 196.742 1.00 44.66  ? 2853 VAL A CB    1 
ATOM   12296 C  CG1   . VAL A 1 2853 ? 134.410 131.487 196.474 1.00 49.54  ? 2853 VAL A CG1   1 
ATOM   12297 C  CG2   . VAL A 1 2853 ? 133.399 133.510 195.441 1.00 45.05  ? 2853 VAL A CG2   1 
ATOM   12298 N  N     . ALA A 1 2854 ? 133.630 132.551 199.924 1.00 61.46  ? 2854 ALA A N     1 
ATOM   12299 C  CA    . ALA A 1 2854 ? 134.007 131.823 201.130 1.00 64.17  ? 2854 ALA A CA    1 
ATOM   12300 C  C     . ALA A 1 2854 ? 132.782 131.317 201.881 1.00 71.23  ? 2854 ALA A C     1 
ATOM   12301 O  O     . ALA A 1 2854 ? 132.760 130.173 202.343 1.00 74.12  ? 2854 ALA A O     1 
ATOM   12302 C  CB    . ALA A 1 2854 ? 134.863 132.709 202.034 1.00 65.49  ? 2854 ALA A CB    1 
ATOM   12303 N  N     . LEU A 1 2855 ? 131.749 132.152 202.012 1.00 71.75  ? 2855 LEU A N     1 
ATOM   12304 C  CA    . LEU A 1 2855 ? 130.521 131.691 202.652 1.00 72.65  ? 2855 LEU A CA    1 
ATOM   12305 C  C     . LEU A 1 2855 ? 129.800 130.644 201.814 1.00 73.92  ? 2855 LEU A C     1 
ATOM   12306 O  O     . LEU A 1 2855 ? 129.208 129.713 202.372 1.00 82.04  ? 2855 LEU A O     1 
ATOM   12307 C  CB    . LEU A 1 2855 ? 129.582 132.863 202.946 1.00 72.39  ? 2855 LEU A CB    1 
ATOM   12308 C  CG    . LEU A 1 2855 ? 129.794 133.673 204.230 1.00 78.87  ? 2855 LEU A CG    1 
ATOM   12309 C  CD1   . LEU A 1 2855 ? 129.564 132.789 205.448 1.00 78.38  ? 2855 LEU A CD1   1 
ATOM   12310 C  CD2   . LEU A 1 2855 ? 131.162 134.320 204.294 1.00 80.00  ? 2855 LEU A CD2   1 
ATOM   12311 N  N     . LYS A 1 2856 ? 129.826 130.776 200.486 1.00 68.66  ? 2856 LYS A N     1 
ATOM   12312 C  CA    . LYS A 1 2856 ? 129.102 129.827 199.648 1.00 70.80  ? 2856 LYS A CA    1 
ATOM   12313 C  C     . LYS A 1 2856 ? 129.717 128.435 199.728 1.00 70.83  ? 2856 LYS A C     1 
ATOM   12314 O  O     . LYS A 1 2856 ? 128.999 127.436 199.847 1.00 74.12  ? 2856 LYS A O     1 
ATOM   12315 C  CB    . LYS A 1 2856 ? 129.068 130.318 198.201 1.00 68.41  ? 2856 LYS A CB    1 
ATOM   12316 C  CG    . LYS A 1 2856 ? 127.853 129.827 197.432 1.00 74.83  ? 2856 LYS A CG    1 
ATOM   12317 C  CD    . LYS A 1 2856 ? 127.827 130.360 196.014 1.00 69.13  ? 2856 LYS A CD    1 
ATOM   12318 C  CE    . LYS A 1 2856 ? 128.757 129.567 195.121 1.00 69.54  ? 2856 LYS A CE    1 
ATOM   12319 N  NZ    . LYS A 1 2856 ? 128.305 128.156 194.980 1.00 72.52  ? 2856 LYS A NZ    1 
ATOM   12320 N  N     . HIS A 1 2857 ? 131.044 128.344 199.670 1.00 68.40  ? 2857 HIS A N     1 
ATOM   12321 C  CA    . HIS A 1 2857 ? 131.703 127.044 199.643 1.00 67.81  ? 2857 HIS A CA    1 
ATOM   12322 C  C     . HIS A 1 2857 ? 132.146 126.558 201.015 1.00 73.23  ? 2857 HIS A C     1 
ATOM   12323 O  O     . HIS A 1 2857 ? 132.509 125.385 201.149 1.00 76.32  ? 2857 HIS A O     1 
ATOM   12324 C  CB    . HIS A 1 2857 ? 132.908 127.083 198.703 1.00 63.32  ? 2857 HIS A CB    1 
ATOM   12325 C  CG    . HIS A 1 2857 ? 132.536 127.196 197.261 1.00 63.46  ? 2857 HIS A CG    1 
ATOM   12326 N  ND1   . HIS A 1 2857 ? 132.265 126.099 196.473 1.00 62.58  ? 2857 HIS A ND1   1 
ATOM   12327 C  CD2   . HIS A 1 2857 ? 132.380 128.279 196.465 1.00 63.92  ? 2857 HIS A CD2   1 
ATOM   12328 C  CE1   . HIS A 1 2857 ? 131.962 126.501 195.252 1.00 64.65  ? 2857 HIS A CE1   1 
ATOM   12329 N  NE2   . HIS A 1 2857 ? 132.024 127.820 195.221 1.00 64.87  ? 2857 HIS A NE2   1 
ATOM   12330 N  N     . PHE A 1 2858 ? 132.121 127.413 202.033 1.00 75.21  ? 2858 PHE A N     1 
ATOM   12331 C  CA    . PHE A 1 2858 ? 132.536 127.049 203.386 1.00 75.36  ? 2858 PHE A CA    1 
ATOM   12332 C  C     . PHE A 1 2858 ? 131.453 127.483 204.364 1.00 85.52  ? 2858 PHE A C     1 
ATOM   12333 O  O     . PHE A 1 2858 ? 131.602 128.484 205.075 1.00 91.29  ? 2858 PHE A O     1 
ATOM   12334 C  CB    . PHE A 1 2858 ? 133.881 127.685 203.735 1.00 72.71  ? 2858 PHE A CB    1 
ATOM   12335 C  CG    . PHE A 1 2858 ? 135.065 126.926 203.219 1.00 71.59  ? 2858 PHE A CG    1 
ATOM   12336 C  CD1   . PHE A 1 2858 ? 135.351 125.656 203.686 1.00 74.49  ? 2858 PHE A CD1   1 
ATOM   12337 C  CD2   . PHE A 1 2858 ? 135.890 127.482 202.256 1.00 67.45  ? 2858 PHE A CD2   1 
ATOM   12338 C  CE1   . PHE A 1 2858 ? 136.442 124.958 203.209 1.00 72.12  ? 2858 PHE A CE1   1 
ATOM   12339 C  CE2   . PHE A 1 2858 ? 136.979 126.790 201.774 1.00 68.44  ? 2858 PHE A CE2   1 
ATOM   12340 C  CZ    . PHE A 1 2858 ? 137.256 125.526 202.251 1.00 72.92  ? 2858 PHE A CZ    1 
ATOM   12341 N  N     . PRO A 1 2859 ? 130.340 126.762 204.413 1.00 88.99  ? 2859 PRO A N     1 
ATOM   12342 C  CA    . PRO A 1 2859 ? 129.264 127.118 205.340 1.00 90.28  ? 2859 PRO A CA    1 
ATOM   12343 C  C     . PRO A 1 2859 ? 129.620 126.728 206.769 1.00 98.12  ? 2859 PRO A C     1 
ATOM   12344 O  O     . PRO A 1 2859 ? 130.561 125.975 207.023 1.00 99.41  ? 2859 PRO A O     1 
ATOM   12345 C  CB    . PRO A 1 2859 ? 128.076 126.307 204.820 1.00 88.14  ? 2859 PRO A CB    1 
ATOM   12346 C  CG    . PRO A 1 2859 ? 128.704 125.098 204.223 1.00 86.42  ? 2859 PRO A CG    1 
ATOM   12347 C  CD    . PRO A 1 2859 ? 130.026 125.542 203.648 1.00 88.14  ? 2859 PRO A CD    1 
ATOM   12348 N  N     . ASN A 1 2860 ? 128.838 127.267 207.706 1.00 98.94  ? 2860 ASN A N     1 
ATOM   12349 C  CA    . ASN A 1 2860 ? 129.010 126.994 209.134 1.00 103.37 ? 2860 ASN A CA    1 
ATOM   12350 C  C     . ASN A 1 2860 ? 130.411 127.374 209.605 1.00 103.55 ? 2860 ASN A C     1 
ATOM   12351 O  O     . ASN A 1 2860 ? 131.076 126.618 210.316 1.00 104.60 ? 2860 ASN A O     1 
ATOM   12352 C  CB    . ASN A 1 2860 ? 128.708 125.528 209.454 1.00 107.15 ? 2860 ASN A CB    1 
ATOM   12353 C  CG    . ASN A 1 2860 ? 127.241 125.190 209.299 1.00 112.24 ? 2860 ASN A CG    1 
ATOM   12354 O  OD1   . ASN A 1 2860 ? 126.369 125.962 209.697 1.00 117.39 ? 2860 ASN A OD1   1 
ATOM   12355 N  ND2   . ASN A 1 2860 ? 126.960 124.032 208.712 1.00 106.94 ? 2860 ASN A ND2   1 
ATOM   12356 N  N     . ILE A 1 2861 ? 130.865 128.558 209.204 1.00 100.61 ? 2861 ILE A N     1 
ATOM   12357 C  CA    . ILE A 1 2861 ? 132.205 129.039 209.512 1.00 102.07 ? 2861 ILE A CA    1 
ATOM   12358 C  C     . ILE A 1 2861 ? 132.096 130.394 210.196 1.00 108.61 ? 2861 ILE A C     1 
ATOM   12359 O  O     . ILE A 1 2861 ? 131.301 131.245 209.783 1.00 110.85 ? 2861 ILE A O     1 
ATOM   12360 C  CB    . ILE A 1 2861 ? 133.077 129.140 208.241 1.00 97.21  ? 2861 ILE A CB    1 
ATOM   12361 C  CG1   . ILE A 1 2861 ? 133.313 127.751 207.651 1.00 95.24  ? 2861 ILE A CG1   1 
ATOM   12362 C  CG2   . ILE A 1 2861 ? 134.399 129.821 208.544 1.00 95.95  ? 2861 ILE A CG2   1 
ATOM   12363 C  CD1   . ILE A 1 2861 ? 133.897 126.771 208.630 1.00 94.52  ? 2861 ILE A CD1   1 
ATOM   12364 N  N     . ASP A 1 2862 ? 132.893 130.591 211.246 1.00 107.27 ? 2862 ASP A N     1 
ATOM   12365 C  CA    . ASP A 1 2862 ? 132.950 131.883 211.914 1.00 108.79 ? 2862 ASP A CA    1 
ATOM   12366 C  C     . ASP A 1 2862 ? 133.657 132.891 211.020 1.00 102.21 ? 2862 ASP A C     1 
ATOM   12367 O  O     . ASP A 1 2862 ? 134.890 132.959 211.002 1.00 101.20 ? 2862 ASP A O     1 
ATOM   12368 C  CB    . ASP A 1 2862 ? 133.666 131.767 213.261 1.00 108.53 ? 2862 ASP A CB    1 
ATOM   12369 C  CG    . ASP A 1 2862 ? 132.836 131.046 214.302 1.00 115.83 ? 2862 ASP A CG    1 
ATOM   12370 O  OD1   . ASP A 1 2862 ? 131.592 131.118 214.226 1.00 113.15 ? 2862 ASP A OD1   1 
ATOM   12371 O  OD2   . ASP A 1 2862 ? 133.428 130.408 215.198 1.00 117.65 ? 2862 ASP A OD2   1 
ATOM   12372 N  N     . ARG A 1 2863 ? 132.881 133.677 210.271 1.00 98.79  ? 2863 ARG A N     1 
ATOM   12373 C  CA    . ARG A 1 2863 ? 133.463 134.618 209.323 1.00 96.86  ? 2863 ARG A CA    1 
ATOM   12374 C  C     . ARG A 1 2863 ? 134.227 135.740 210.012 1.00 99.41  ? 2863 ARG A C     1 
ATOM   12375 O  O     . ARG A 1 2863 ? 135.061 136.388 209.373 1.00 99.58  ? 2863 ARG A O     1 
ATOM   12376 C  CB    . ARG A 1 2863 ? 132.368 135.197 208.425 1.00 95.78  ? 2863 ARG A CB    1 
ATOM   12377 C  CG    . ARG A 1 2863 ? 132.881 135.826 207.140 1.00 97.78  ? 2863 ARG A CG    1 
ATOM   12378 C  CD    . ARG A 1 2863 ? 133.905 134.931 206.456 1.00 97.33  ? 2863 ARG A CD    1 
ATOM   12379 N  NE    . ARG A 1 2863 ? 134.464 135.555 205.262 1.00 92.59  ? 2863 ARG A NE    1 
ATOM   12380 C  CZ    . ARG A 1 2863 ? 135.511 135.090 204.595 1.00 85.54  ? 2863 ARG A CZ    1 
ATOM   12381 N  NH1   . ARG A 1 2863 ? 136.142 133.994 204.978 1.00 82.98  ? 2863 ARG A NH1   1 
ATOM   12382 N  NH2   . ARG A 1 2863 ? 135.942 135.748 203.522 1.00 76.86  ? 2863 ARG A NH2   1 
ATOM   12383 N  N     . GLU A 1 2864 ? 133.961 135.988 211.295 1.00 102.54 ? 2864 GLU A N     1 
ATOM   12384 C  CA    . GLU A 1 2864 ? 134.702 137.022 212.011 1.00 101.24 ? 2864 GLU A CA    1 
ATOM   12385 C  C     . GLU A 1 2864 ? 136.176 136.656 212.130 1.00 99.19  ? 2864 GLU A C     1 
ATOM   12386 O  O     . GLU A 1 2864 ? 137.056 137.502 211.934 1.00 95.90  ? 2864 GLU A O     1 
ATOM   12387 C  CB    . GLU A 1 2864 ? 134.083 137.248 213.391 1.00 103.47 ? 2864 GLU A CB    1 
ATOM   12388 C  CG    . GLU A 1 2864 ? 132.686 137.853 213.353 1.00 110.25 ? 2864 GLU A CG    1 
ATOM   12389 C  CD    . GLU A 1 2864 ? 131.600 136.819 213.119 1.00 115.73 ? 2864 GLU A CD    1 
ATOM   12390 O  OE1   . GLU A 1 2864 ? 131.927 135.615 213.048 1.00 112.65 ? 2864 GLU A OE1   1 
ATOM   12391 O  OE2   . GLU A 1 2864 ? 130.420 137.211 213.003 1.00 119.05 ? 2864 GLU A OE2   1 
ATOM   12392 N  N     . LYS A 1 2865 ? 136.466 135.393 212.449 1.00 97.62  ? 2865 LYS A N     1 
ATOM   12393 C  CA    . LYS A 1 2865 ? 137.854 134.953 212.534 1.00 90.38  ? 2865 LYS A CA    1 
ATOM   12394 C  C     . LYS A 1 2865 ? 138.451 134.706 211.154 1.00 90.07  ? 2865 LYS A C     1 
ATOM   12395 O  O     . LYS A 1 2865 ? 139.629 134.996 210.924 1.00 89.59  ? 2865 LYS A O     1 
ATOM   12396 C  CB    . LYS A 1 2865 ? 137.955 133.693 213.394 1.00 89.21  ? 2865 LYS A CB    1 
ATOM   12397 C  CG    . LYS A 1 2865 ? 137.361 133.847 214.782 1.00 95.40  ? 2865 LYS A CG    1 
ATOM   12398 C  CD    . LYS A 1 2865 ? 137.352 132.528 215.533 1.00 103.80 ? 2865 LYS A CD    1 
ATOM   12399 C  CE    . LYS A 1 2865 ? 137.346 132.751 217.037 1.00 103.78 ? 2865 LYS A CE    1 
ATOM   12400 N  NZ    . LYS A 1 2865 ? 136.218 132.044 217.703 1.00 102.80 ? 2865 LYS A NZ    1 
ATOM   12401 N  N     . ALA A 1 2866 ? 137.655 134.171 210.226 1.00 91.54  ? 2866 ALA A N     1 
ATOM   12402 C  CA    . ALA A 1 2866 ? 138.149 133.914 208.880 1.00 81.72  ? 2866 ALA A CA    1 
ATOM   12403 C  C     . ALA A 1 2866 ? 138.197 135.175 208.030 1.00 82.68  ? 2866 ALA A C     1 
ATOM   12404 O  O     . ALA A 1 2866 ? 138.775 135.150 206.939 1.00 80.37  ? 2866 ALA A O     1 
ATOM   12405 C  CB    . ALA A 1 2866 ? 137.283 132.857 208.194 1.00 79.08  ? 2866 ALA A CB    1 
ATOM   12406 N  N     . MET A 1 2867 ? 137.607 136.272 208.500 1.00 89.23  ? 2867 MET A N     1 
ATOM   12407 C  CA    . MET A 1 2867 ? 137.596 137.515 207.733 1.00 89.39  ? 2867 MET A CA    1 
ATOM   12408 C  C     . MET A 1 2867 ? 137.514 138.688 208.697 1.00 97.39  ? 2867 MET A C     1 
ATOM   12409 O  O     . MET A 1 2867 ? 136.433 138.995 209.208 1.00 104.17 ? 2867 MET A O     1 
ATOM   12410 C  CB    . MET A 1 2867 ? 136.431 137.542 206.758 1.00 90.96  ? 2867 MET A CB    1 
ATOM   12411 C  CG    . MET A 1 2867 ? 136.426 138.737 205.819 1.00 98.60  ? 2867 MET A CG    1 
ATOM   12412 S  SD    . MET A 1 2867 ? 137.787 138.784 204.643 1.00 122.19 ? 2867 MET A SD    1 
ATOM   12413 C  CE    . MET A 1 2867 ? 137.859 140.536 204.274 1.00 93.08  ? 2867 MET A CE    1 
ATOM   12414 N  N     . SER A 1 2868 ? 138.646 139.333 208.938 1.00 93.76  ? 2868 SER A N     1 
ATOM   12415 C  CA    . SER A 1 2868 ? 138.681 140.666 209.508 1.00 92.54  ? 2868 SER A CA    1 
ATOM   12416 C  C     . SER A 1 2868 ? 139.044 141.636 208.395 1.00 93.40  ? 2868 SER A C     1 
ATOM   12417 O  O     . SER A 1 2868 ? 139.728 141.266 207.437 1.00 95.66  ? 2868 SER A O     1 
ATOM   12418 C  CB    . SER A 1 2868 ? 139.690 140.759 210.655 1.00 97.42  ? 2868 SER A CB    1 
ATOM   12419 O  OG    . SER A 1 2868 ? 139.308 139.924 211.734 1.00 91.73  ? 2868 SER A OG    1 
ATOM   12420 N  N     . ARG A 1 2869 ? 138.560 142.870 208.506 1.00 99.58  ? 2869 ARG A N     1 
ATOM   12421 C  CA    . ARG A 1 2869 ? 138.791 143.849 207.446 1.00 108.53 ? 2869 ARG A CA    1 
ATOM   12422 C  C     . ARG A 1 2869 ? 140.269 144.020 207.112 1.00 103.90 ? 2869 ARG A C     1 
ATOM   12423 O  O     . ARG A 1 2869 ? 140.609 144.022 205.919 1.00 106.23 ? 2869 ARG A O     1 
ATOM   12424 C  CB    . ARG A 1 2869 ? 138.140 145.187 207.827 1.00 116.80 ? 2869 ARG A CB    1 
ATOM   12425 C  CG    . ARG A 1 2869 ? 136.619 145.155 207.861 1.00 117.81 ? 2869 ARG A CG    1 
ATOM   12426 C  CD    . ARG A 1 2869 ? 136.035 144.811 206.500 1.00 126.70 ? 2869 ARG A CD    1 
ATOM   12427 N  NE    . ARG A 1 2869 ? 136.513 145.705 205.451 1.00 129.77 ? 2869 ARG A NE    1 
ATOM   12428 C  CZ    . ARG A 1 2869 ? 137.170 145.305 204.371 1.00 120.07 ? 2869 ARG A CZ    1 
ATOM   12429 N  NH1   . ARG A 1 2869 ? 137.450 144.029 204.166 1.00 113.76 ? 2869 ARG A NH1   1 
ATOM   12430 N  NH2   . ARG A 1 2869 ? 137.556 146.209 203.475 1.00 114.44 ? 2869 ARG A NH2   1 
ATOM   12431 N  N     . PRO A 1 2870 ? 141.190 144.164 208.081 1.00 96.45  ? 2870 PRO A N     1 
ATOM   12432 C  CA    . PRO A 1 2870 ? 142.625 144.133 207.733 1.00 88.91  ? 2870 PRO A CA    1 
ATOM   12433 C  C     . PRO A 1 2870 ? 143.251 142.739 207.812 1.00 84.31  ? 2870 PRO A C     1 
ATOM   12434 O  O     . PRO A 1 2870 ? 143.968 142.384 208.750 1.00 86.92  ? 2870 PRO A O     1 
ATOM   12435 C  CB    . PRO A 1 2870 ? 143.235 145.084 208.762 1.00 91.43  ? 2870 PRO A CB    1 
ATOM   12436 C  CG    . PRO A 1 2870 ? 142.389 144.882 209.973 1.00 95.28  ? 2870 PRO A CG    1 
ATOM   12437 C  CD    . PRO A 1 2870 ? 140.999 144.507 209.504 1.00 93.46  ? 2870 PRO A CD    1 
ATOM   12438 N  N     . ILE A 1 2871 ? 142.967 141.903 206.813 1.00 81.57  ? 2871 ILE A N     1 
ATOM   12439 C  CA    . ILE A 1 2871 ? 143.639 140.609 206.724 1.00 74.73  ? 2871 ILE A CA    1 
ATOM   12440 C  C     . ILE A 1 2871 ? 145.121 140.857 206.488 1.00 66.76  ? 2871 ILE A C     1 
ATOM   12441 O  O     . ILE A 1 2871 ? 145.507 141.523 205.520 1.00 61.54  ? 2871 ILE A O     1 
ATOM   12442 C  CB    . ILE A 1 2871 ? 143.039 139.740 205.612 1.00 75.21  ? 2871 ILE A CB    1 
ATOM   12443 C  CG1   . ILE A 1 2871 ? 141.752 139.071 206.084 1.00 72.93  ? 2871 ILE A CG1   1 
ATOM   12444 C  CG2   . ILE A 1 2871 ? 144.032 138.679 205.175 1.00 67.28  ? 2871 ILE A CG2   1 
ATOM   12445 C  CD1   . ILE A 1 2871 ? 141.153 138.154 205.054 1.00 60.78  ? 2871 ILE A CD1   1 
ATOM   12446 N  N     . LEU A 1 2872 ? 145.960 140.325 207.372 1.00 66.75  ? 2872 LEU A N     1 
ATOM   12447 C  CA    . LEU A 1 2872 ? 147.365 140.690 207.380 1.00 62.39  ? 2872 LEU A CA    1 
ATOM   12448 C  C     . LEU A 1 2872 ? 148.199 139.472 207.744 1.00 58.79  ? 2872 LEU A C     1 
ATOM   12449 O  O     . LEU A 1 2872 ? 147.860 138.738 208.676 1.00 62.20  ? 2872 LEU A O     1 
ATOM   12450 C  CB    . LEU A 1 2872 ? 147.618 141.821 208.379 1.00 63.85  ? 2872 LEU A CB    1 
ATOM   12451 C  CG    . LEU A 1 2872 ? 147.359 143.231 207.845 1.00 65.78  ? 2872 LEU A CG    1 
ATOM   12452 C  CD1   . LEU A 1 2872 ? 147.552 144.268 208.939 1.00 72.76  ? 2872 LEU A CD1   1 
ATOM   12453 C  CD2   . LEU A 1 2872 ? 148.180 143.546 206.616 1.00 59.17  ? 2872 LEU A CD2   1 
ATOM   12454 N  N     . TYR A 1 2873 ? 149.288 139.260 207.007 1.00 51.68  ? 2873 TYR A N     1 
ATOM   12455 C  CA    . TYR A 1 2873 ? 150.182 138.134 207.245 1.00 54.62  ? 2873 TYR A CA    1 
ATOM   12456 C  C     . TYR A 1 2873 ? 151.625 138.592 207.107 1.00 55.12  ? 2873 TYR A C     1 
ATOM   12457 O  O     . TYR A 1 2873 ? 151.963 139.297 206.152 1.00 58.55  ? 2873 TYR A O     1 
ATOM   12458 C  CB    . TYR A 1 2873 ? 149.912 136.984 206.266 1.00 58.18  ? 2873 TYR A CB    1 
ATOM   12459 C  CG    . TYR A 1 2873 ? 148.784 136.060 206.666 1.00 56.67  ? 2873 TYR A CG    1 
ATOM   12460 C  CD1   . TYR A 1 2873 ? 147.459 136.455 206.550 1.00 54.51  ? 2873 TYR A CD1   1 
ATOM   12461 C  CD2   . TYR A 1 2873 ? 149.046 134.791 207.159 1.00 53.46  ? 2873 TYR A CD2   1 
ATOM   12462 C  CE1   . TYR A 1 2873 ? 146.431 135.615 206.914 1.00 48.41  ? 2873 TYR A CE1   1 
ATOM   12463 C  CE2   . TYR A 1 2873 ? 148.023 133.945 207.527 1.00 51.94  ? 2873 TYR A CE2   1 
ATOM   12464 C  CZ    . TYR A 1 2873 ? 146.719 134.362 207.401 1.00 51.33  ? 2873 TYR A CZ    1 
ATOM   12465 O  OH    . TYR A 1 2873 ? 145.696 133.519 207.767 1.00 62.55  ? 2873 TYR A OH    1 
ATOM   12466 N  N     . SER A 1 2874 ? 152.467 138.182 208.055 1.00 54.53  ? 2874 SER A N     1 
ATOM   12467 C  CA    . SER A 1 2874 ? 153.905 138.412 207.997 1.00 56.82  ? 2874 SER A CA    1 
ATOM   12468 C  C     . SER A 1 2874 ? 154.565 137.650 209.134 1.00 63.47  ? 2874 SER A C     1 
ATOM   12469 O  O     . SER A 1 2874 ? 153.983 137.497 210.211 1.00 61.98  ? 2874 SER A O     1 
ATOM   12470 C  CB    . SER A 1 2874 ? 154.253 139.901 208.099 1.00 61.85  ? 2874 SER A CB    1 
ATOM   12471 O  OG    . SER A 1 2874 ? 154.170 140.343 209.440 1.00 73.48  ? 2874 SER A OG    1 
ATOM   12472 N  N     . ASN A 1 2875 ? 155.787 137.181 208.886 1.00 65.90  ? 2875 ASN A N     1 
ATOM   12473 C  CA    . ASN A 1 2875 ? 156.598 136.536 209.909 1.00 66.97  ? 2875 ASN A CA    1 
ATOM   12474 C  C     . ASN A 1 2875 ? 157.706 137.439 210.430 1.00 70.91  ? 2875 ASN A C     1 
ATOM   12475 O  O     . ASN A 1 2875 ? 158.672 136.943 211.017 1.00 76.78  ? 2875 ASN A O     1 
ATOM   12476 C  CB    . ASN A 1 2875 ? 157.193 135.229 209.380 1.00 69.70  ? 2875 ASN A CB    1 
ATOM   12477 C  CG    . ASN A 1 2875 ? 158.148 135.438 208.221 1.00 70.57  ? 2875 ASN A CG    1 
ATOM   12478 O  OD1   . ASN A 1 2875 ? 158.399 136.563 207.794 1.00 65.98  ? 2875 ASN A OD1   1 
ATOM   12479 N  ND2   . ASN A 1 2875 ? 158.700 134.342 207.714 1.00 73.65  ? 2875 ASN A ND2   1 
ATOM   12480 N  N     . TRP A 1 2876 ? 157.595 138.750 210.214 1.00 69.07  ? 2876 TRP A N     1 
ATOM   12481 C  CA    . TRP A 1 2876 ? 158.616 139.673 210.695 1.00 62.90  ? 2876 TRP A CA    1 
ATOM   12482 C  C     . TRP A 1 2876 ? 158.675 139.695 212.216 1.00 65.95  ? 2876 TRP A C     1 
ATOM   12483 O  O     . TRP A 1 2876 ? 159.760 139.782 212.802 1.00 65.93  ? 2876 TRP A O     1 
ATOM   12484 C  CB    . TRP A 1 2876 ? 158.348 141.074 210.152 1.00 60.73  ? 2876 TRP A CB    1 
ATOM   12485 C  CG    . TRP A 1 2876 ? 158.908 141.305 208.793 1.00 55.40  ? 2876 TRP A CG    1 
ATOM   12486 C  CD1   . TRP A 1 2876 ? 159.945 140.642 208.211 1.00 52.01  ? 2876 TRP A CD1   1 
ATOM   12487 C  CD2   . TRP A 1 2876 ? 158.464 142.273 207.839 1.00 52.91  ? 2876 TRP A CD2   1 
ATOM   12488 N  NE1   . TRP A 1 2876 ? 160.176 141.137 206.952 1.00 48.10  ? 2876 TRP A NE1   1 
ATOM   12489 C  CE2   . TRP A 1 2876 ? 159.278 142.140 206.699 1.00 48.03  ? 2876 TRP A CE2   1 
ATOM   12490 C  CE3   . TRP A 1 2876 ? 157.455 143.241 207.837 1.00 50.28  ? 2876 TRP A CE3   1 
ATOM   12491 C  CZ2   . TRP A 1 2876 ? 159.116 142.936 205.571 1.00 47.23  ? 2876 TRP A CZ2   1 
ATOM   12492 C  CZ3   . TRP A 1 2876 ? 157.297 144.029 206.717 1.00 46.89  ? 2876 TRP A CZ3   1 
ATOM   12493 C  CH2   . TRP A 1 2876 ? 158.121 143.872 205.599 1.00 50.70  ? 2876 TRP A CH2   1 
ATOM   12494 N  N     . LEU A 1 2877 ? 157.519 139.622 212.874 1.00 65.61  ? 2877 LEU A N     1 
ATOM   12495 C  CA    . LEU A 1 2877 ? 157.438 139.736 214.322 1.00 72.68  ? 2877 LEU A CA    1 
ATOM   12496 C  C     . LEU A 1 2877 ? 157.299 138.384 215.011 1.00 74.41  ? 2877 LEU A C     1 
ATOM   12497 O  O     . LEU A 1 2877 ? 156.992 138.333 216.207 1.00 78.84  ? 2877 LEU A O     1 
ATOM   12498 C  CB    . LEU A 1 2877 ? 156.275 140.645 214.719 1.00 74.34  ? 2877 LEU A CB    1 
ATOM   12499 C  CG    . LEU A 1 2877 ? 156.481 142.155 214.577 1.00 71.83  ? 2877 LEU A CG    1 
ATOM   12500 C  CD1   . LEU A 1 2877 ? 156.443 142.602 213.123 1.00 69.22  ? 2877 LEU A CD1   1 
ATOM   12501 C  CD2   . LEU A 1 2877 ? 155.453 142.896 215.394 1.00 75.09  ? 2877 LEU A CD2   1 
ATOM   12502 N  N     . SER A 1 2878 ? 157.518 137.292 214.288 1.00 76.52  ? 2878 SER A N     1 
ATOM   12503 C  CA    . SER A 1 2878 ? 157.419 135.959 214.864 1.00 84.09  ? 2878 SER A CA    1 
ATOM   12504 C  C     . SER A 1 2878 ? 158.395 135.046 214.130 1.00 86.66  ? 2878 SER A C     1 
ATOM   12505 O  O     . SER A 1 2878 ? 159.288 135.509 213.414 1.00 83.63  ? 2878 SER A O     1 
ATOM   12506 C  CB    . SER A 1 2878 ? 155.977 135.443 214.794 1.00 83.69  ? 2878 SER A CB    1 
ATOM   12507 O  OG    . SER A 1 2878 ? 155.542 135.323 213.452 1.00 78.50  ? 2878 SER A OG    1 
ATOM   12508 N  N     . LYS A 1 2879 ? 158.226 133.740 214.319 1.00 89.35  ? 2879 LYS A N     1 
ATOM   12509 C  CA    . LYS A 1 2879 ? 159.040 132.744 213.636 1.00 90.14  ? 2879 LYS A CA    1 
ATOM   12510 C  C     . LYS A 1 2879 ? 158.335 132.137 212.433 1.00 91.87  ? 2879 LYS A C     1 
ATOM   12511 O  O     . LYS A 1 2879 ? 159.002 131.735 211.474 1.00 92.88  ? 2879 LYS A O     1 
ATOM   12512 C  CB    . LYS A 1 2879 ? 159.447 131.641 214.625 1.00 86.76  ? 2879 LYS A CB    1 
ATOM   12513 C  CG    . LYS A 1 2879 ? 160.453 130.611 214.112 1.00 94.32  ? 2879 LYS A CG    1 
ATOM   12514 C  CD    . LYS A 1 2879 ? 159.780 129.395 213.494 1.00 100.38 ? 2879 LYS A CD    1 
ATOM   12515 C  CE    . LYS A 1 2879 ? 160.800 128.356 213.062 1.00 106.49 ? 2879 LYS A CE    1 
ATOM   12516 N  NZ    . LYS A 1 2879 ? 160.151 127.178 212.424 1.00 108.91 ? 2879 LYS A NZ    1 
ATOM   12517 N  N     . ASP A 1 2880 ? 157.007 132.082 212.451 1.00 88.76  ? 2880 ASP A N     1 
ATOM   12518 C  CA    . ASP A 1 2880 ? 156.217 131.535 211.360 1.00 84.47  ? 2880 ASP A CA    1 
ATOM   12519 C  C     . ASP A 1 2880 ? 155.367 132.626 210.721 1.00 78.16  ? 2880 ASP A C     1 
ATOM   12520 O  O     . ASP A 1 2880 ? 155.111 133.677 211.313 1.00 80.98  ? 2880 ASP A O     1 
ATOM   12521 C  CB    . ASP A 1 2880 ? 155.322 130.393 211.853 1.00 89.07  ? 2880 ASP A CB    1 
ATOM   12522 C  CG    . ASP A 1 2880 ? 155.991 129.039 211.739 1.00 97.00  ? 2880 ASP A CG    1 
ATOM   12523 O  OD1   . ASP A 1 2880 ? 157.231 128.997 211.607 1.00 97.80  ? 2880 ASP A OD1   1 
ATOM   12524 O  OD2   . ASP A 1 2880 ? 155.279 128.015 211.785 1.00 95.51  ? 2880 ASP A OD2   1 
ATOM   12525 N  N     . TYR A 1 2881 ? 154.928 132.353 209.492 1.00 72.31  ? 2881 TYR A N     1 
ATOM   12526 C  CA    . TYR A 1 2881 ? 154.119 133.287 208.707 1.00 63.27  ? 2881 TYR A CA    1 
ATOM   12527 C  C     . TYR A 1 2881 ? 152.678 133.260 209.219 1.00 66.83  ? 2881 TYR A C     1 
ATOM   12528 O  O     . TYR A 1 2881 ? 151.767 132.695 208.611 1.00 69.44  ? 2881 TYR A O     1 
ATOM   12529 C  CB    . TYR A 1 2881 ? 154.206 132.930 207.231 1.00 64.03  ? 2881 TYR A CB    1 
ATOM   12530 C  CG    . TYR A 1 2881 ? 153.709 133.994 206.283 1.00 56.24  ? 2881 TYR A CG    1 
ATOM   12531 C  CD1   . TYR A 1 2881 ? 154.428 135.160 206.079 1.00 54.84  ? 2881 TYR A CD1   1 
ATOM   12532 C  CD2   . TYR A 1 2881 ? 152.534 133.816 205.567 1.00 59.23  ? 2881 TYR A CD2   1 
ATOM   12533 C  CE1   . TYR A 1 2881 ? 153.981 136.128 205.206 1.00 56.84  ? 2881 TYR A CE1   1 
ATOM   12534 C  CE2   . TYR A 1 2881 ? 152.081 134.778 204.689 1.00 53.60  ? 2881 TYR A CE2   1 
ATOM   12535 C  CZ    . TYR A 1 2881 ? 152.809 135.932 204.513 1.00 52.20  ? 2881 TYR A CZ    1 
ATOM   12536 O  OH    . TYR A 1 2881 ? 152.364 136.897 203.642 1.00 54.39  ? 2881 TYR A OH    1 
ATOM   12537 N  N     . ILE A 1 2882 ? 152.484 133.893 210.372 1.00 69.64  ? 2882 ILE A N     1 
ATOM   12538 C  CA    . ILE A 1 2882 ? 151.203 133.876 211.076 1.00 67.93  ? 2882 ILE A CA    1 
ATOM   12539 C  C     . ILE A 1 2882 ? 150.469 135.192 210.843 1.00 66.97  ? 2882 ILE A C     1 
ATOM   12540 O  O     . ILE A 1 2882 ? 151.094 136.181 210.433 1.00 67.06  ? 2882 ILE A O     1 
ATOM   12541 C  CB    . ILE A 1 2882 ? 151.405 133.621 212.578 1.00 67.88  ? 2882 ILE A CB    1 
ATOM   12542 C  CG1   . ILE A 1 2882 ? 152.229 134.748 213.202 1.00 70.93  ? 2882 ILE A CG1   1 
ATOM   12543 C  CG2   . ILE A 1 2882 ? 152.073 132.276 212.803 1.00 69.83  ? 2882 ILE A CG2   1 
ATOM   12544 C  CD1   . ILE A 1 2882 ? 152.278 134.705 214.711 1.00 73.52  ? 2882 ILE A CD1   1 
ATOM   12545 N  N     . PRO A 1 2883 ? 149.155 135.254 211.071 1.00 67.38  ? 2883 PRO A N     1 
ATOM   12546 C  CA    . PRO A 1 2883 ? 148.465 136.547 211.024 1.00 67.69  ? 2883 PRO A CA    1 
ATOM   12547 C  C     . PRO A 1 2883 ? 148.974 137.479 212.114 1.00 71.52  ? 2883 PRO A C     1 
ATOM   12548 O  O     . PRO A 1 2883 ? 149.382 137.046 213.193 1.00 73.41  ? 2883 PRO A O     1 
ATOM   12549 C  CB    . PRO A 1 2883 ? 146.993 136.176 211.245 1.00 62.32  ? 2883 PRO A CB    1 
ATOM   12550 C  CG    . PRO A 1 2883 ? 147.030 134.837 211.884 1.00 63.10  ? 2883 PRO A CG    1 
ATOM   12551 C  CD    . PRO A 1 2883 ? 148.213 134.146 211.291 1.00 67.26  ? 2883 PRO A CD    1 
ATOM   12552 N  N     . VAL A 1 2884 ? 148.944 138.778 211.817 1.00 72.74  ? 2884 VAL A N     1 
ATOM   12553 C  CA    . VAL A 1 2884 ? 149.516 139.797 212.687 1.00 70.03  ? 2884 VAL A CA    1 
ATOM   12554 C  C     . VAL A 1 2884 ? 148.696 141.073 212.548 1.00 74.82  ? 2884 VAL A C     1 
ATOM   12555 O  O     . VAL A 1 2884 ? 148.135 141.363 211.490 1.00 79.53  ? 2884 VAL A O     1 
ATOM   12556 C  CB    . VAL A 1 2884 ? 151.010 140.030 212.349 1.00 68.65  ? 2884 VAL A CB    1 
ATOM   12557 C  CG1   . VAL A 1 2884 ? 151.148 140.585 210.952 1.00 65.96  ? 2884 VAL A CG1   1 
ATOM   12558 C  CG2   . VAL A 1 2884 ? 151.672 140.950 213.369 1.00 74.38  ? 2884 VAL A CG2   1 
ATOM   12559 N  N     . ASP A 1 2885 ? 148.619 141.835 213.636 1.00 76.55  ? 2885 ASP A N     1 
ATOM   12560 C  CA    . ASP A 1 2885 ? 147.777 143.021 213.711 1.00 83.79  ? 2885 ASP A CA    1 
ATOM   12561 C  C     . ASP A 1 2885 ? 148.455 144.212 213.043 1.00 82.24  ? 2885 ASP A C     1 
ATOM   12562 O  O     . ASP A 1 2885 ? 149.662 144.206 212.791 1.00 80.53  ? 2885 ASP A O     1 
ATOM   12563 C  CB    . ASP A 1 2885 ? 147.441 143.358 215.165 1.00 89.67  ? 2885 ASP A CB    1 
ATOM   12564 C  CG    . ASP A 1 2885 ? 146.284 144.325 215.285 1.00 96.07  ? 2885 ASP A CG    1 
ATOM   12565 O  OD1   . ASP A 1 2885 ? 145.685 144.660 214.241 1.00 94.13  ? 2885 ASP A OD1   1 
ATOM   12566 O  OD2   . ASP A 1 2885 ? 145.968 144.742 216.419 1.00 96.28  ? 2885 ASP A OD2   1 
ATOM   12567 N  N     . GLN A 1 2886 ? 147.649 145.236 212.748 1.00 84.05  ? 2886 GLN A N     1 
ATOM   12568 C  CA    . GLN A 1 2886 ? 148.126 146.375 211.969 1.00 81.62  ? 2886 GLN A CA    1 
ATOM   12569 C  C     . GLN A 1 2886 ? 149.126 147.212 212.760 1.00 83.03  ? 2886 GLN A C     1 
ATOM   12570 O  O     . GLN A 1 2886 ? 150.119 147.702 212.206 1.00 80.40  ? 2886 GLN A O     1 
ATOM   12571 C  CB    . GLN A 1 2886 ? 146.930 147.234 211.548 1.00 82.67  ? 2886 GLN A CB    1 
ATOM   12572 C  CG    . GLN A 1 2886 ? 147.256 148.408 210.646 1.00 84.62  ? 2886 GLN A CG    1 
ATOM   12573 C  CD    . GLN A 1 2886 ? 147.824 147.962 209.322 1.00 91.02  ? 2886 GLN A CD    1 
ATOM   12574 O  OE1   . GLN A 1 2886 ? 149.021 148.060 209.080 1.00 88.11  ? 2886 GLN A OE1   1 
ATOM   12575 N  NE2   . GLN A 1 2886 ? 146.955 147.482 208.442 1.00 86.26  ? 2886 GLN A NE2   1 
ATOM   12576 N  N     . GLU A 1 2887 ? 148.875 147.384 214.061 1.00 86.39  ? 2887 GLU A N     1 
ATOM   12577 C  CA    . GLU A 1 2887 ? 149.624 148.352 214.859 1.00 86.59  ? 2887 GLU A CA    1 
ATOM   12578 C  C     . GLU A 1 2887 ? 151.079 147.932 215.033 1.00 85.24  ? 2887 GLU A C     1 
ATOM   12579 O  O     . GLU A 1 2887 ? 151.994 148.749 214.874 1.00 84.65  ? 2887 GLU A O     1 
ATOM   12580 C  CB    . GLU A 1 2887 ? 148.951 148.536 216.219 1.00 87.57  ? 2887 GLU A CB    1 
ATOM   12581 C  CG    . GLU A 1 2887 ? 147.901 149.635 216.265 1.00 96.82  ? 2887 GLU A CG    1 
ATOM   12582 C  CD    . GLU A 1 2887 ? 148.371 150.923 215.622 1.00 104.09 ? 2887 GLU A CD    1 
ATOM   12583 O  OE1   . GLU A 1 2887 ? 149.497 151.372 215.924 1.00 100.88 ? 2887 GLU A OE1   1 
ATOM   12584 O  OE2   . GLU A 1 2887 ? 147.608 151.487 214.811 1.00 104.32 ? 2887 GLU A OE2   1 
ATOM   12585 N  N     . GLU A 1 2888 ? 151.314 146.665 215.383 1.00 85.16  ? 2888 GLU A N     1 
ATOM   12586 C  CA    . GLU A 1 2888 ? 152.688 146.222 215.577 1.00 79.60  ? 2888 GLU A CA    1 
ATOM   12587 C  C     . GLU A 1 2888 ? 153.459 146.186 214.263 1.00 75.75  ? 2888 GLU A C     1 
ATOM   12588 O  O     . GLU A 1 2888 ? 154.665 146.452 214.254 1.00 75.47  ? 2888 GLU A O     1 
ATOM   12589 C  CB    . GLU A 1 2888 ? 152.726 144.859 216.266 1.00 76.63  ? 2888 GLU A CB    1 
ATOM   12590 C  CG    . GLU A 1 2888 ? 151.714 143.848 215.776 1.00 84.51  ? 2888 GLU A CG    1 
ATOM   12591 C  CD    . GLU A 1 2888 ? 150.488 143.789 216.661 1.00 91.76  ? 2888 GLU A CD    1 
ATOM   12592 O  OE1   . GLU A 1 2888 ? 150.066 144.848 217.169 1.00 93.62  ? 2888 GLU A OE1   1 
ATOM   12593 O  OE2   . GLU A 1 2888 ? 149.959 142.677 216.868 1.00 91.26  ? 2888 GLU A OE2   1 
ATOM   12594 N  N     . LEU A 1 2889 ? 152.789 145.880 213.149 1.00 72.36  ? 2889 LEU A N     1 
ATOM   12595 C  CA    . LEU A 1 2889 ? 153.436 146.015 211.847 1.00 69.86  ? 2889 LEU A CA    1 
ATOM   12596 C  C     . LEU A 1 2889 ? 153.852 147.454 211.591 1.00 72.90  ? 2889 LEU A C     1 
ATOM   12597 O  O     . LEU A 1 2889 ? 154.963 147.715 211.117 1.00 73.36  ? 2889 LEU A O     1 
ATOM   12598 C  CB    . LEU A 1 2889 ? 152.509 145.538 210.733 1.00 74.69  ? 2889 LEU A CB    1 
ATOM   12599 C  CG    . LEU A 1 2889 ? 152.159 144.061 210.688 1.00 80.65  ? 2889 LEU A CG    1 
ATOM   12600 C  CD1   . LEU A 1 2889 ? 151.128 143.827 209.607 1.00 75.49  ? 2889 LEU A CD1   1 
ATOM   12601 C  CD2   . LEU A 1 2889 ? 153.420 143.273 210.411 1.00 80.15  ? 2889 LEU A CD2   1 
ATOM   12602 N  N     . ARG A 1 2890 ? 152.963 148.405 211.884 1.00 73.99  ? 2890 ARG A N     1 
ATOM   12603 C  CA    . ARG A 1 2890 ? 153.309 149.804 211.665 1.00 70.81  ? 2890 ARG A CA    1 
ATOM   12604 C  C     . ARG A 1 2890 ? 154.499 150.211 212.523 1.00 72.18  ? 2890 ARG A C     1 
ATOM   12605 O  O     . ARG A 1 2890 ? 155.418 150.882 212.042 1.00 73.90  ? 2890 ARG A O     1 
ATOM   12606 C  CB    . ARG A 1 2890 ? 152.102 150.696 211.946 1.00 76.45  ? 2890 ARG A CB    1 
ATOM   12607 C  CG    . ARG A 1 2890 ? 152.379 152.176 211.766 1.00 77.96  ? 2890 ARG A CG    1 
ATOM   12608 C  CD    . ARG A 1 2890 ? 151.091 152.977 211.786 1.00 76.01  ? 2890 ARG A CD    1 
ATOM   12609 N  NE    . ARG A 1 2890 ? 150.116 152.451 210.839 1.00 75.56  ? 2890 ARG A NE    1 
ATOM   12610 C  CZ    . ARG A 1 2890 ? 150.136 152.687 209.534 1.00 75.43  ? 2890 ARG A CZ    1 
ATOM   12611 N  NH1   . ARG A 1 2890 ? 151.071 153.444 208.983 1.00 67.06  ? 2890 ARG A NH1   1 
ATOM   12612 N  NH2   . ARG A 1 2890 ? 149.194 152.152 208.763 1.00 76.16  ? 2890 ARG A NH2   1 
ATOM   12613 N  N     . ASP A 1 2891 ? 154.512 149.786 213.788 1.00 75.47  ? 2891 ASP A N     1 
ATOM   12614 C  CA    . ASP A 1 2891 ? 155.629 150.113 214.672 1.00 74.84  ? 2891 ASP A CA    1 
ATOM   12615 C  C     . ASP A 1 2891 ? 156.935 149.503 214.168 1.00 71.51  ? 2891 ASP A C     1 
ATOM   12616 O  O     . ASP A 1 2891 ? 157.976 150.173 214.128 1.00 74.10  ? 2891 ASP A O     1 
ATOM   12617 C  CB    . ASP A 1 2891 ? 155.325 149.634 216.091 1.00 74.61  ? 2891 ASP A CB    1 
ATOM   12618 C  CG    . ASP A 1 2891 ? 154.060 150.247 216.654 1.00 84.55  ? 2891 ASP A CG    1 
ATOM   12619 O  OD1   . ASP A 1 2891 ? 153.433 151.067 215.951 1.00 83.94  ? 2891 ASP A OD1   1 
ATOM   12620 O  OD2   . ASP A 1 2891 ? 153.691 149.910 217.798 1.00 91.53  ? 2891 ASP A OD2   1 
ATOM   12621 N  N     . TYR A 1 2892 ? 156.895 148.228 213.774 1.00 66.70  ? 2892 TYR A N     1 
ATOM   12622 C  CA    . TYR A 1 2892 ? 158.103 147.548 213.321 1.00 64.90  ? 2892 TYR A CA    1 
ATOM   12623 C  C     . TYR A 1 2892 ? 158.648 148.179 212.047 1.00 64.65  ? 2892 TYR A C     1 
ATOM   12624 O  O     . TYR A 1 2892 ? 159.861 148.388 211.916 1.00 68.80  ? 2892 TYR A O     1 
ATOM   12625 C  CB    . TYR A 1 2892 ? 157.807 146.063 213.109 1.00 58.36  ? 2892 TYR A CB    1 
ATOM   12626 C  CG    . TYR A 1 2892 ? 158.942 145.277 212.498 1.00 56.27  ? 2892 TYR A CG    1 
ATOM   12627 C  CD1   . TYR A 1 2892 ? 160.058 144.939 213.247 1.00 58.66  ? 2892 TYR A CD1   1 
ATOM   12628 C  CD2   . TYR A 1 2892 ? 158.893 144.866 211.175 1.00 58.65  ? 2892 TYR A CD2   1 
ATOM   12629 C  CE1   . TYR A 1 2892 ? 161.096 144.219 212.693 1.00 61.93  ? 2892 TYR A CE1   1 
ATOM   12630 C  CE2   . TYR A 1 2892 ? 159.926 144.146 210.614 1.00 56.96  ? 2892 TYR A CE2   1 
ATOM   12631 C  CZ    . TYR A 1 2892 ? 161.024 143.825 211.376 1.00 62.54  ? 2892 TYR A CZ    1 
ATOM   12632 O  OH    . TYR A 1 2892 ? 162.056 143.107 210.817 1.00 70.93  ? 2892 TYR A OH    1 
ATOM   12633 N  N     . VAL A 1 2893 ? 157.769 148.499 211.096 1.00 57.97  ? 2893 VAL A N     1 
ATOM   12634 C  CA    . VAL A 1 2893 ? 158.236 149.087 209.848 1.00 58.17  ? 2893 VAL A CA    1 
ATOM   12635 C  C     . VAL A 1 2893 ? 158.691 150.528 210.057 1.00 63.88  ? 2893 VAL A C     1 
ATOM   12636 O  O     . VAL A 1 2893 ? 159.599 150.997 209.367 1.00 68.03  ? 2893 VAL A O     1 
ATOM   12637 C  CB    . VAL A 1 2893 ? 157.155 148.964 208.761 1.00 61.06  ? 2893 VAL A CB    1 
ATOM   12638 C  CG1   . VAL A 1 2893 ? 157.651 149.540 207.450 1.00 57.61  ? 2893 VAL A CG1   1 
ATOM   12639 C  CG2   . VAL A 1 2893 ? 156.790 147.506 208.567 1.00 62.49  ? 2893 VAL A CG2   1 
ATOM   12640 N  N     . LYS A 1 2894 ? 158.098 151.253 211.011 1.00 64.69  ? 2894 LYS A N     1 
ATOM   12641 C  CA    . LYS A 1 2894 ? 158.621 152.577 211.341 1.00 61.18  ? 2894 LYS A CA    1 
ATOM   12642 C  C     . LYS A 1 2894 ? 160.024 152.482 211.924 1.00 59.68  ? 2894 LYS A C     1 
ATOM   12643 O  O     . LYS A 1 2894 ? 160.907 153.277 211.576 1.00 63.76  ? 2894 LYS A O     1 
ATOM   12644 C  CB    . LYS A 1 2894 ? 157.684 153.292 212.313 1.00 65.23  ? 2894 LYS A CB    1 
ATOM   12645 C  CG    . LYS A 1 2894 ? 156.452 153.892 211.661 1.00 67.45  ? 2894 LYS A CG    1 
ATOM   12646 C  CD    . LYS A 1 2894 ? 155.454 154.367 212.701 1.00 73.19  ? 2894 LYS A CD    1 
ATOM   12647 C  CE    . LYS A 1 2894 ? 156.072 155.406 213.620 1.00 81.25  ? 2894 LYS A CE    1 
ATOM   12648 N  NZ    . LYS A 1 2894 ? 156.551 156.595 212.864 1.00 85.17  ? 2894 LYS A NZ    1 
ATOM   12649 N  N     . ALA A 1 2895 ? 160.253 151.512 212.812 1.00 57.54  ? 2895 ALA A N     1 
ATOM   12650 C  CA    . ALA A 1 2895 ? 161.596 151.311 213.347 1.00 62.57  ? 2895 ALA A CA    1 
ATOM   12651 C  C     . ALA A 1 2895 ? 162.580 150.950 212.240 1.00 67.19  ? 2895 ALA A C     1 
ATOM   12652 O  O     . ALA A 1 2895 ? 163.711 151.455 212.206 1.00 69.62  ? 2895 ALA A O     1 
ATOM   12653 C  CB    . ALA A 1 2895 ? 161.576 150.228 214.423 1.00 64.10  ? 2895 ALA A CB    1 
ATOM   12654 N  N     . ARG A 1 2896 ? 162.165 150.084 211.315 1.00 63.18  ? 2896 ARG A N     1 
ATOM   12655 C  CA    . ARG A 1 2896 ? 163.057 149.700 210.229 1.00 60.03  ? 2896 ARG A CA    1 
ATOM   12656 C  C     . ARG A 1 2896 ? 163.302 150.853 209.262 1.00 59.86  ? 2896 ARG A C     1 
ATOM   12657 O  O     . ARG A 1 2896 ? 164.383 150.940 208.679 1.00 63.61  ? 2896 ARG A O     1 
ATOM   12658 C  CB    . ARG A 1 2896 ? 162.500 148.483 209.497 1.00 61.98  ? 2896 ARG A CB    1 
ATOM   12659 C  CG    . ARG A 1 2896 ? 162.453 147.239 210.364 1.00 64.42  ? 2896 ARG A CG    1 
ATOM   12660 C  CD    . ARG A 1 2896 ? 163.840 146.851 210.844 1.00 63.95  ? 2896 ARG A CD    1 
ATOM   12661 N  NE    . ARG A 1 2896 ? 164.711 146.453 209.745 1.00 70.78  ? 2896 ARG A NE    1 
ATOM   12662 C  CZ    . ARG A 1 2896 ? 165.992 146.143 209.882 1.00 73.20  ? 2896 ARG A CZ    1 
ATOM   12663 N  NH1   . ARG A 1 2896 ? 166.593 146.198 211.059 1.00 74.61  ? 2896 ARG A NH1   1 
ATOM   12664 N  NH2   . ARG A 1 2896 ? 166.687 145.770 208.812 1.00 65.30  ? 2896 ARG A NH2   1 
ATOM   12665 N  N     . LEU A 1 2897 ? 162.326 151.743 209.076 1.00 59.50  ? 2897 LEU A N     1 
ATOM   12666 C  CA    . LEU A 1 2897 ? 162.564 152.956 208.298 1.00 59.00  ? 2897 LEU A CA    1 
ATOM   12667 C  C     . LEU A 1 2897 ? 163.558 153.873 208.998 1.00 69.28  ? 2897 LEU A C     1 
ATOM   12668 O  O     . LEU A 1 2897 ? 164.409 154.494 208.348 1.00 72.08  ? 2897 LEU A O     1 
ATOM   12669 C  CB    . LEU A 1 2897 ? 161.248 153.690 208.047 1.00 49.71  ? 2897 LEU A CB    1 
ATOM   12670 C  CG    . LEU A 1 2897 ? 160.346 153.143 206.943 1.00 50.40  ? 2897 LEU A CG    1 
ATOM   12671 C  CD1   . LEU A 1 2897 ? 158.967 153.765 207.021 1.00 52.43  ? 2897 LEU A CD1   1 
ATOM   12672 C  CD2   . LEU A 1 2897 ? 160.969 153.416 205.591 1.00 50.92  ? 2897 LEU A CD2   1 
ATOM   12673 N  N     . LYS A 1 2898 ? 163.459 153.979 210.324 1.00 71.58  ? 2898 LYS A N     1 
ATOM   12674 C  CA    . LYS A 1 2898 ? 164.452 154.742 211.073 1.00 72.88  ? 2898 LYS A CA    1 
ATOM   12675 C  C     . LYS A 1 2898 ? 165.846 154.164 210.866 1.00 77.38  ? 2898 LYS A C     1 
ATOM   12676 O  O     . LYS A 1 2898 ? 166.821 154.909 210.721 1.00 82.53  ? 2898 LYS A O     1 
ATOM   12677 C  CB    . LYS A 1 2898 ? 164.090 154.759 212.557 1.00 70.01  ? 2898 LYS A CB    1 
ATOM   12678 C  CG    . LYS A 1 2898 ? 162.830 155.544 212.873 1.00 72.95  ? 2898 LYS A CG    1 
ATOM   12679 C  CD    . LYS A 1 2898 ? 162.538 155.545 214.363 1.00 75.46  ? 2898 LYS A CD    1 
ATOM   12680 C  CE    . LYS A 1 2898 ? 161.261 156.310 214.671 1.00 80.51  ? 2898 LYS A CE    1 
ATOM   12681 N  NZ    . LYS A 1 2898 ? 160.951 156.310 216.126 1.00 77.84  ? 2898 LYS A NZ    1 
ATOM   12682 N  N     . VAL A 1 2899 ? 165.957 152.834 210.855 1.00 72.17  ? 2899 VAL A N     1 
ATOM   12683 C  CA    . VAL A 1 2899 ? 167.241 152.201 210.554 1.00 73.02  ? 2899 VAL A CA    1 
ATOM   12684 C  C     . VAL A 1 2899 ? 167.677 152.520 209.127 1.00 73.19  ? 2899 VAL A C     1 
ATOM   12685 O  O     . VAL A 1 2899 ? 168.831 152.887 208.879 1.00 82.38  ? 2899 VAL A O     1 
ATOM   12686 C  CB    . VAL A 1 2899 ? 167.158 150.682 210.784 1.00 76.67  ? 2899 VAL A CB    1 
ATOM   12687 C  CG1   . VAL A 1 2899 ? 168.510 150.034 210.528 1.00 79.98  ? 2899 VAL A CG1   1 
ATOM   12688 C  CG2   . VAL A 1 2899 ? 166.665 150.378 212.181 1.00 80.86  ? 2899 VAL A CG2   1 
ATOM   12689 N  N     . PHE A 1 2900 ? 166.755 152.392 208.171 1.00 65.81  ? 2900 PHE A N     1 
ATOM   12690 C  CA    . PHE A 1 2900 ? 167.047 152.604 206.757 1.00 65.61  ? 2900 PHE A CA    1 
ATOM   12691 C  C     . PHE A 1 2900 ? 167.403 154.051 206.453 1.00 77.73  ? 2900 PHE A C     1 
ATOM   12692 O  O     . PHE A 1 2900 ? 167.897 154.343 205.360 1.00 80.96  ? 2900 PHE A O     1 
ATOM   12693 C  CB    . PHE A 1 2900 ? 165.837 152.159 205.929 1.00 61.65  ? 2900 PHE A CB    1 
ATOM   12694 C  CG    . PHE A 1 2900 ? 166.075 152.132 204.446 1.00 60.37  ? 2900 PHE A CG    1 
ATOM   12695 C  CD1   . PHE A 1 2900 ? 166.991 151.258 203.891 1.00 62.70  ? 2900 PHE A CD1   1 
ATOM   12696 C  CD2   . PHE A 1 2900 ? 165.353 152.956 203.604 1.00 59.74  ? 2900 PHE A CD2   1 
ATOM   12697 C  CE1   . PHE A 1 2900 ? 167.200 151.226 202.527 1.00 56.50  ? 2900 PHE A CE1   1 
ATOM   12698 C  CE2   . PHE A 1 2900 ? 165.557 152.925 202.240 1.00 58.30  ? 2900 PHE A CE2   1 
ATOM   12699 C  CZ    . PHE A 1 2900 ? 166.482 152.060 201.702 1.00 55.05  ? 2900 PHE A CZ    1 
ATOM   12700 N  N     . TYR A 1 2901 ? 167.119 154.970 207.374 1.00 82.81  ? 2901 TYR A N     1 
ATOM   12701 C  CA    . TYR A 1 2901 ? 167.578 156.345 207.199 1.00 83.48  ? 2901 TYR A CA    1 
ATOM   12702 C  C     . TYR A 1 2901 ? 169.098 156.436 207.273 1.00 87.33  ? 2901 TYR A C     1 
ATOM   12703 O  O     . TYR A 1 2901 ? 169.720 157.176 206.503 1.00 93.65  ? 2901 TYR A O     1 
ATOM   12704 C  CB    . TYR A 1 2901 ? 166.932 157.255 208.240 1.00 81.87  ? 2901 TYR A CB    1 
ATOM   12705 C  CG    . TYR A 1 2901 ? 165.468 157.523 207.983 1.00 80.96  ? 2901 TYR A CG    1 
ATOM   12706 C  CD1   . TYR A 1 2901 ? 164.885 157.188 206.769 1.00 70.36  ? 2901 TYR A CD1   1 
ATOM   12707 C  CD2   . TYR A 1 2901 ? 164.670 158.110 208.954 1.00 79.38  ? 2901 TYR A CD2   1 
ATOM   12708 C  CE1   . TYR A 1 2901 ? 163.549 157.428 206.531 1.00 62.98  ? 2901 TYR A CE1   1 
ATOM   12709 C  CE2   . TYR A 1 2901 ? 163.332 158.355 208.725 1.00 72.09  ? 2901 TYR A CE2   1 
ATOM   12710 C  CZ    . TYR A 1 2901 ? 162.777 158.012 207.512 1.00 66.48  ? 2901 TYR A CZ    1 
ATOM   12711 O  OH    . TYR A 1 2901 ? 161.444 158.256 207.283 1.00 64.15  ? 2901 TYR A OH    1 
ATOM   12712 N  N     . GLU A 1 2902 ? 169.717 155.692 208.194 1.00 86.14  ? 2902 GLU A N     1 
ATOM   12713 C  CA    . GLU A 1 2902 ? 171.169 155.748 208.339 1.00 92.32  ? 2902 GLU A CA    1 
ATOM   12714 C  C     . GLU A 1 2902 ? 171.870 154.948 207.246 1.00 90.63  ? 2902 GLU A C     1 
ATOM   12715 O  O     . GLU A 1 2902 ? 172.614 155.507 206.433 1.00 94.09  ? 2902 GLU A O     1 
ATOM   12716 C  CB    . GLU A 1 2902 ? 171.581 155.241 209.724 1.00 94.04  ? 2902 GLU A CB    1 
ATOM   12717 C  CG    . GLU A 1 2902 ? 171.163 156.149 210.870 1.00 103.96 ? 2902 GLU A CG    1 
ATOM   12718 C  CD    . GLU A 1 2902 ? 169.762 155.859 211.367 1.00 102.43 ? 2902 GLU A CD    1 
ATOM   12719 O  OE1   . GLU A 1 2902 ? 169.520 154.728 211.838 1.00 101.67 ? 2902 GLU A OE1   1 
ATOM   12720 O  OE2   . GLU A 1 2902 ? 168.904 156.762 211.287 1.00 98.81  ? 2902 GLU A OE2   1 
ATOM   12721 N  N     . GLU A 1 2903 ? 171.644 153.638 207.209 1.00 91.10  ? 2903 GLU A N     1 
ATOM   12722 C  CA    . GLU A 1 2903 ? 172.182 152.812 206.137 1.00 91.85  ? 2903 GLU A CA    1 
ATOM   12723 C  C     . GLU A 1 2903 ? 171.423 153.097 204.847 1.00 91.84  ? 2903 GLU A C     1 
ATOM   12724 O  O     . GLU A 1 2903 ? 170.201 153.257 204.865 1.00 87.99  ? 2903 GLU A O     1 
ATOM   12725 C  CB    . GLU A 1 2903 ? 172.092 151.328 206.498 1.00 90.42  ? 2903 GLU A CB    1 
ATOM   12726 C  CG    . GLU A 1 2903 ? 173.003 150.891 207.640 1.00 100.14 ? 2903 GLU A CG    1 
ATOM   12727 C  CD    . GLU A 1 2903 ? 172.409 151.148 209.011 1.00 102.20 ? 2903 GLU A CD    1 
ATOM   12728 O  OE1   . GLU A 1 2903 ? 171.252 151.607 209.085 1.00 95.68  ? 2903 GLU A OE1   1 
ATOM   12729 O  OE2   . GLU A 1 2903 ? 173.100 150.889 210.018 1.00 109.24 ? 2903 GLU A OE2   1 
ATOM   12730 N  N     . GLU A 1 2904 ? 172.149 153.153 203.729 1.00 95.67  ? 2904 GLU A N     1 
ATOM   12731 C  CA    . GLU A 1 2904 ? 171.590 153.545 202.437 1.00 93.21  ? 2904 GLU A CA    1 
ATOM   12732 C  C     . GLU A 1 2904 ? 171.025 154.962 202.479 1.00 91.58  ? 2904 GLU A C     1 
ATOM   12733 O  O     . GLU A 1 2904 ? 171.590 155.837 203.144 1.00 90.63  ? 2904 GLU A O     1 
ATOM   12734 C  CB    . GLU A 1 2904 ? 170.524 152.552 201.957 1.00 81.16  ? 2904 GLU A CB    1 
ATOM   12735 C  CG    . GLU A 1 2904 ? 171.078 151.216 201.473 1.00 80.95  ? 2904 GLU A CG    1 
ATOM   12736 C  CD    . GLU A 1 2904 ? 171.256 150.197 202.578 1.00 79.78  ? 2904 GLU A CD    1 
ATOM   12737 O  OE1   . GLU A 1 2904 ? 170.847 150.477 203.721 1.00 75.99  ? 2904 GLU A OE1   1 
ATOM   12738 O  OE2   . GLU A 1 2904 ? 171.808 149.112 202.301 1.00 80.47  ? 2904 GLU A OE2   1 
ATOM   12739 N  N     . LEU A 1 2905 ? 169.919 155.195 201.771 1.00 83.50  ? 2905 LEU A N     1 
ATOM   12740 C  CA    . LEU A 1 2905 ? 169.457 156.556 201.518 1.00 84.95  ? 2905 LEU A CA    1 
ATOM   12741 C  C     . LEU A 1 2905 ? 169.089 157.276 202.809 1.00 88.03  ? 2905 LEU A C     1 
ATOM   12742 O  O     . LEU A 1 2905 ? 168.645 156.663 203.784 1.00 88.36  ? 2905 LEU A O     1 
ATOM   12743 C  CB    . LEU A 1 2905 ? 168.264 156.545 200.556 1.00 76.40  ? 2905 LEU A CB    1 
ATOM   12744 C  CG    . LEU A 1 2905 ? 166.960 155.828 200.925 1.00 81.83  ? 2905 LEU A CG    1 
ATOM   12745 C  CD1   . LEU A 1 2905 ? 166.035 156.671 201.796 1.00 76.12  ? 2905 LEU A CD1   1 
ATOM   12746 C  CD2   . LEU A 1 2905 ? 166.234 155.401 199.659 1.00 81.45  ? 2905 LEU A CD2   1 
ATOM   12747 N  N     . ASP A 1 2906 ? 169.275 158.595 202.803 1.00 86.70  ? 2906 ASP A N     1 
ATOM   12748 C  CA    . ASP A 1 2906 ? 169.042 159.440 203.964 1.00 87.10  ? 2906 ASP A CA    1 
ATOM   12749 C  C     . ASP A 1 2906 ? 167.764 160.263 203.865 1.00 85.89  ? 2906 ASP A C     1 
ATOM   12750 O  O     . ASP A 1 2906 ? 167.349 160.853 204.867 1.00 84.95  ? 2906 ASP A O     1 
ATOM   12751 C  CB    . ASP A 1 2906 ? 170.236 160.377 204.173 1.00 89.55  ? 2906 ASP A CB    1 
ATOM   12752 C  CG    . ASP A 1 2906 ? 170.334 160.890 205.592 1.00 101.06 ? 2906 ASP A CG    1 
ATOM   12753 O  OD1   . ASP A 1 2906 ? 169.555 160.423 206.449 1.00 98.87  ? 2906 ASP A OD1   1 
ATOM   12754 O  OD2   . ASP A 1 2906 ? 171.188 161.765 205.849 1.00 106.19 ? 2906 ASP A OD2   1 
ATOM   12755 N  N     . VAL A 1 2907 ? 167.138 160.326 202.696 1.00 81.84  ? 2907 VAL A N     1 
ATOM   12756 C  CA    . VAL A 1 2907 ? 165.915 161.127 202.562 1.00 75.38  ? 2907 VAL A CA    1 
ATOM   12757 C  C     . VAL A 1 2907 ? 164.805 160.495 203.393 1.00 70.85  ? 2907 VAL A C     1 
ATOM   12758 O  O     . VAL A 1 2907 ? 164.692 159.256 203.432 1.00 74.84  ? 2907 VAL A O     1 
ATOM   12759 C  CB    . VAL A 1 2907 ? 165.512 161.254 201.089 1.00 68.83  ? 2907 VAL A CB    1 
ATOM   12760 C  CG1   . VAL A 1 2907 ? 166.599 161.975 200.310 1.00 74.49  ? 2907 VAL A CG1   1 
ATOM   12761 C  CG2   . VAL A 1 2907 ? 165.246 159.893 200.474 1.00 66.63  ? 2907 VAL A CG2   1 
ATOM   12762 N  N     . PRO A 1 2908 ? 163.996 161.283 204.096 1.00 61.61  ? 2908 PRO A N     1 
ATOM   12763 C  CA    . PRO A 1 2908 ? 162.979 160.702 204.976 1.00 58.51  ? 2908 PRO A CA    1 
ATOM   12764 C  C     . PRO A 1 2908 ? 161.868 160.015 204.198 1.00 54.30  ? 2908 PRO A C     1 
ATOM   12765 O  O     . PRO A 1 2908 ? 161.597 160.330 203.038 1.00 58.28  ? 2908 PRO A O     1 
ATOM   12766 C  CB    . PRO A 1 2908 ? 162.441 161.914 205.748 1.00 58.08  ? 2908 PRO A CB    1 
ATOM   12767 C  CG    . PRO A 1 2908 ? 163.484 162.975 205.585 1.00 55.30  ? 2908 PRO A CG    1 
ATOM   12768 C  CD    . PRO A 1 2908 ? 164.072 162.745 204.233 1.00 58.47  ? 2908 PRO A CD    1 
ATOM   12769 N  N     . LEU A 1 2909 ? 161.225 159.059 204.863 1.00 47.86  ? 2909 LEU A N     1 
ATOM   12770 C  CA    . LEU A 1 2909 ? 160.081 158.347 204.319 1.00 42.93  ? 2909 LEU A CA    1 
ATOM   12771 C  C     . LEU A 1 2909 ? 158.935 158.388 205.317 1.00 46.78  ? 2909 LEU A C     1 
ATOM   12772 O  O     . LEU A 1 2909 ? 159.145 158.361 206.532 1.00 51.31  ? 2909 LEU A O     1 
ATOM   12773 C  CB    . LEU A 1 2909 ? 160.419 156.891 203.990 1.00 45.35  ? 2909 LEU A CB    1 
ATOM   12774 C  CG    . LEU A 1 2909 ? 160.801 156.561 202.549 1.00 44.69  ? 2909 LEU A CG    1 
ATOM   12775 C  CD1   . LEU A 1 2909 ? 162.176 157.103 202.204 1.00 49.84  ? 2909 LEU A CD1   1 
ATOM   12776 C  CD2   . LEU A 1 2909 ? 160.742 155.060 202.344 1.00 44.70  ? 2909 LEU A CD2   1 
ATOM   12777 N  N     . VAL A 1 2910 ? 157.717 158.451 204.789 1.00 45.17  ? 2910 VAL A N     1 
ATOM   12778 C  CA    . VAL A 1 2910 ? 156.502 158.488 205.591 1.00 44.87  ? 2910 VAL A CA    1 
ATOM   12779 C  C     . VAL A 1 2910 ? 155.773 157.169 205.395 1.00 48.24  ? 2910 VAL A C     1 
ATOM   12780 O  O     . VAL A 1 2910 ? 155.528 156.751 204.257 1.00 48.17  ? 2910 VAL A O     1 
ATOM   12781 C  CB    . VAL A 1 2910 ? 155.605 159.675 205.204 1.00 41.81  ? 2910 VAL A CB    1 
ATOM   12782 C  CG1   . VAL A 1 2910 ? 154.234 159.536 205.844 1.00 43.18  ? 2910 VAL A CG1   1 
ATOM   12783 C  CG2   . VAL A 1 2910 ? 156.257 160.981 205.600 1.00 41.22  ? 2910 VAL A CG2   1 
ATOM   12784 N  N     . LEU A 1 2911 ? 155.431 156.513 206.499 1.00 47.50  ? 2911 LEU A N     1 
ATOM   12785 C  CA    . LEU A 1 2911 ? 154.745 155.224 206.459 1.00 47.41  ? 2911 LEU A CA    1 
ATOM   12786 C  C     . LEU A 1 2911 ? 153.258 155.466 206.685 1.00 51.17  ? 2911 LEU A C     1 
ATOM   12787 O  O     . LEU A 1 2911 ? 152.775 155.474 207.817 1.00 56.77  ? 2911 LEU A O     1 
ATOM   12788 C  CB    . LEU A 1 2911 ? 155.322 154.267 207.495 1.00 52.69  ? 2911 LEU A CB    1 
ATOM   12789 C  CG    . LEU A 1 2911 ? 154.699 152.870 207.494 1.00 54.47  ? 2911 LEU A CG    1 
ATOM   12790 C  CD1   . LEU A 1 2911 ? 155.291 152.032 206.380 1.00 54.93  ? 2911 LEU A CD1   1 
ATOM   12791 C  CD2   . LEU A 1 2911 ? 154.889 152.188 208.834 1.00 57.20  ? 2911 LEU A CD2   1 
ATOM   12792 N  N     . PHE A 1 2912 ? 152.526 155.668 205.595 1.00 49.25  ? 2912 PHE A N     1 
ATOM   12793 C  CA    . PHE A 1 2912 ? 151.076 155.694 205.652 1.00 47.68  ? 2912 PHE A CA    1 
ATOM   12794 C  C     . PHE A 1 2912 ? 150.534 154.344 205.189 1.00 50.35  ? 2912 PHE A C     1 
ATOM   12795 O  O     . PHE A 1 2912 ? 151.287 153.420 204.876 1.00 56.68  ? 2912 PHE A O     1 
ATOM   12796 C  CB    . PHE A 1 2912 ? 150.511 156.866 204.842 1.00 44.40  ? 2912 PHE A CB    1 
ATOM   12797 C  CG    . PHE A 1 2912 ? 151.092 157.010 203.463 1.00 39.49  ? 2912 PHE A CG    1 
ATOM   12798 C  CD1   . PHE A 1 2912 ? 150.584 156.288 202.400 1.00 41.09  ? 2912 PHE A CD1   1 
ATOM   12799 C  CD2   . PHE A 1 2912 ? 152.131 157.891 203.228 1.00 36.86  ? 2912 PHE A CD2   1 
ATOM   12800 C  CE1   . PHE A 1 2912 ? 151.110 156.435 201.132 1.00 35.45  ? 2912 PHE A CE1   1 
ATOM   12801 C  CE2   . PHE A 1 2912 ? 152.660 158.037 201.964 1.00 33.31  ? 2912 PHE A CE2   1 
ATOM   12802 C  CZ    . PHE A 1 2912 ? 152.147 157.311 200.916 1.00 29.49  ? 2912 PHE A CZ    1 
ATOM   12803 N  N     . ASN A 1 2913 ? 149.205 154.228 205.160 1.00 53.06  ? 2913 ASN A N     1 
ATOM   12804 C  CA    . ASN A 1 2913 ? 148.580 152.919 204.987 1.00 53.68  ? 2913 ASN A CA    1 
ATOM   12805 C  C     . ASN A 1 2913 ? 148.960 152.279 203.658 1.00 48.09  ? 2913 ASN A C     1 
ATOM   12806 O  O     . ASN A 1 2913 ? 149.284 151.087 203.608 1.00 51.74  ? 2913 ASN A O     1 
ATOM   12807 C  CB    . ASN A 1 2913 ? 147.064 153.048 205.111 1.00 60.02  ? 2913 ASN A CB    1 
ATOM   12808 C  CG    . ASN A 1 2913 ? 146.641 153.626 206.443 1.00 68.34  ? 2913 ASN A CG    1 
ATOM   12809 O  OD1   . ASN A 1 2913 ? 147.479 153.956 207.281 1.00 67.98  ? 2913 ASN A OD1   1 
ATOM   12810 N  ND2   . ASN A 1 2913 ? 145.336 153.754 206.648 1.00 71.18  ? 2913 ASN A ND2   1 
ATOM   12811 N  N     . GLU A 1 2914 ? 148.937 153.054 202.572 1.00 42.42  ? 2914 GLU A N     1 
ATOM   12812 C  CA    . GLU A 1 2914 ? 149.260 152.495 201.263 1.00 42.28  ? 2914 GLU A CA    1 
ATOM   12813 C  C     . GLU A 1 2914 ? 150.703 152.009 201.209 1.00 44.61  ? 2914 GLU A C     1 
ATOM   12814 O  O     . GLU A 1 2914 ? 150.984 150.933 200.664 1.00 51.90  ? 2914 GLU A O     1 
ATOM   12815 C  CB    . GLU A 1 2914 ? 148.997 153.530 200.168 1.00 42.79  ? 2914 GLU A CB    1 
ATOM   12816 C  CG    . GLU A 1 2914 ? 147.525 153.830 199.922 1.00 52.20  ? 2914 GLU A CG    1 
ATOM   12817 C  CD    . GLU A 1 2914 ? 146.907 154.699 201.001 1.00 64.36  ? 2914 GLU A CD    1 
ATOM   12818 O  OE1   . GLU A 1 2914 ? 147.333 155.863 201.149 1.00 63.86  ? 2914 GLU A OE1   1 
ATOM   12819 O  OE2   . GLU A 1 2914 ? 145.998 154.213 201.705 1.00 72.40  ? 2914 GLU A OE2   1 
ATOM   12820 N  N     . VAL A 1 2915 ? 151.629 152.782 201.780 1.00 37.00  ? 2915 VAL A N     1 
ATOM   12821 C  CA    . VAL A 1 2915 ? 153.031 152.375 201.802 1.00 35.77  ? 2915 VAL A CA    1 
ATOM   12822 C  C     . VAL A 1 2915 ? 153.201 151.068 202.561 1.00 40.74  ? 2915 VAL A C     1 
ATOM   12823 O  O     . VAL A 1 2915 ? 153.909 150.165 202.109 1.00 47.80  ? 2915 VAL A O     1 
ATOM   12824 C  CB    . VAL A 1 2915 ? 153.905 153.491 202.402 1.00 41.49  ? 2915 VAL A CB    1 
ATOM   12825 C  CG1   . VAL A 1 2915 ? 155.243 152.931 202.837 1.00 38.61  ? 2915 VAL A CG1   1 
ATOM   12826 C  CG2   . VAL A 1 2915 ? 154.127 154.584 201.380 1.00 45.14  ? 2915 VAL A CG2   1 
ATOM   12827 N  N     . LEU A 1 2916 ? 152.563 150.946 203.723 1.00 41.21  ? 2916 LEU A N     1 
ATOM   12828 C  CA    . LEU A 1 2916 ? 152.713 149.735 204.523 1.00 40.86  ? 2916 LEU A CA    1 
ATOM   12829 C  C     . LEU A 1 2916 ? 152.089 148.525 203.831 1.00 42.85  ? 2916 LEU A C     1 
ATOM   12830 O  O     . LEU A 1 2916 ? 152.658 147.424 203.852 1.00 47.19  ? 2916 LEU A O     1 
ATOM   12831 C  CB    . LEU A 1 2916 ? 152.120 149.973 205.909 1.00 45.60  ? 2916 LEU A CB    1 
ATOM   12832 C  CG    . LEU A 1 2916 ? 152.233 148.862 206.940 1.00 53.60  ? 2916 LEU A CG    1 
ATOM   12833 C  CD1   . LEU A 1 2916 ? 153.686 148.566 207.159 1.00 57.25  ? 2916 LEU A CD1   1 
ATOM   12834 C  CD2   . LEU A 1 2916 ? 151.621 149.350 208.231 1.00 67.21  ? 2916 LEU A CD2   1 
ATOM   12835 N  N     . ASP A 1 2917 ? 150.928 148.712 203.195 1.00 44.18  ? 2917 ASP A N     1 
ATOM   12836 C  CA    . ASP A 1 2917 ? 150.336 147.630 202.413 1.00 36.81  ? 2917 ASP A CA    1 
ATOM   12837 C  C     . ASP A 1 2917 ? 151.270 147.176 201.300 1.00 39.06  ? 2917 ASP A C     1 
ATOM   12838 O  O     . ASP A 1 2917 ? 151.474 145.971 201.105 1.00 51.60  ? 2917 ASP A O     1 
ATOM   12839 C  CB    . ASP A 1 2917 ? 148.999 148.075 201.823 1.00 42.10  ? 2917 ASP A CB    1 
ATOM   12840 C  CG    . ASP A 1 2917 ? 148.013 148.515 202.879 1.00 55.58  ? 2917 ASP A CG    1 
ATOM   12841 O  OD1   . ASP A 1 2917 ? 148.351 148.446 204.079 1.00 60.31  ? 2917 ASP A OD1   1 
ATOM   12842 O  OD2   . ASP A 1 2917 ? 146.894 148.926 202.506 1.00 53.31  ? 2917 ASP A OD2   1 
ATOM   12843 N  N     . HIS A 1 2918 ? 151.854 148.123 200.563 1.00 34.83  ? 2918 HIS A N     1 
ATOM   12844 C  CA    . HIS A 1 2918 ? 152.767 147.743 199.492 1.00 34.24  ? 2918 HIS A CA    1 
ATOM   12845 C  C     . HIS A 1 2918 ? 154.031 147.085 200.031 1.00 35.91  ? 2918 HIS A C     1 
ATOM   12846 O  O     . HIS A 1 2918 ? 154.562 146.170 199.398 1.00 40.93  ? 2918 HIS A O     1 
ATOM   12847 C  CB    . HIS A 1 2918 ? 153.118 148.956 198.633 1.00 36.90  ? 2918 HIS A CB    1 
ATOM   12848 C  CG    . HIS A 1 2918 ? 151.951 149.522 197.886 1.00 40.02  ? 2918 HIS A CG    1 
ATOM   12849 N  ND1   . HIS A 1 2918 ? 150.929 150.206 198.506 1.00 44.13  ? 2918 HIS A ND1   1 
ATOM   12850 C  CD2   . HIS A 1 2918 ? 151.635 149.484 196.571 1.00 40.72  ? 2918 HIS A CD2   1 
ATOM   12851 C  CE1   . HIS A 1 2918 ? 150.041 150.579 197.603 1.00 46.54  ? 2918 HIS A CE1   1 
ATOM   12852 N  NE2   . HIS A 1 2918 ? 150.445 150.153 196.421 1.00 44.10  ? 2918 HIS A NE2   1 
ATOM   12853 N  N     . VAL A 1 2919 ? 154.524 147.531 201.187 1.00 37.25  ? 2919 VAL A N     1 
ATOM   12854 C  CA    . VAL A 1 2919 ? 155.675 146.878 201.806 1.00 37.80  ? 2919 VAL A CA    1 
ATOM   12855 C  C     . VAL A 1 2919 ? 155.355 145.423 202.113 1.00 37.19  ? 2919 VAL A C     1 
ATOM   12856 O  O     . VAL A 1 2919 ? 156.164 144.524 201.852 1.00 42.52  ? 2919 VAL A O     1 
ATOM   12857 C  CB    . VAL A 1 2919 ? 156.111 147.642 203.070 1.00 34.40  ? 2919 VAL A CB    1 
ATOM   12858 C  CG1   . VAL A 1 2919 ? 157.136 146.844 203.840 1.00 38.26  ? 2919 VAL A CG1   1 
ATOM   12859 C  CG2   . VAL A 1 2919 ? 156.704 148.983 202.692 1.00 30.72  ? 2919 VAL A CG2   1 
ATOM   12860 N  N     . LEU A 1 2920 ? 154.170 145.167 202.667 1.00 33.03  ? 2920 LEU A N     1 
ATOM   12861 C  CA    . LEU A 1 2920 ? 153.785 143.791 202.964 1.00 33.37  ? 2920 LEU A CA    1 
ATOM   12862 C  C     . LEU A 1 2920 ? 153.632 142.965 201.692 1.00 37.10  ? 2920 LEU A C     1 
ATOM   12863 O  O     . LEU A 1 2920 ? 154.016 141.790 201.658 1.00 43.30  ? 2920 LEU A O     1 
ATOM   12864 C  CB    . LEU A 1 2920 ? 152.502 143.778 203.787 1.00 36.71  ? 2920 LEU A CB    1 
ATOM   12865 C  CG    . LEU A 1 2920 ? 152.729 144.283 205.209 1.00 41.34  ? 2920 LEU A CG    1 
ATOM   12866 C  CD1   . LEU A 1 2920 ? 151.533 144.003 206.059 1.00 43.75  ? 2920 LEU A CD1   1 
ATOM   12867 C  CD2   . LEU A 1 2920 ? 153.951 143.622 205.810 1.00 49.87  ? 2920 LEU A CD2   1 
ATOM   12868 N  N     . ARG A 1 2921 ? 153.076 143.560 200.634 1.00 33.65  ? 2921 ARG A N     1 
ATOM   12869 C  CA    . ARG A 1 2921 ? 152.951 142.842 199.367 1.00 31.80  ? 2921 ARG A CA    1 
ATOM   12870 C  C     . ARG A 1 2921 ? 154.317 142.469 198.804 1.00 34.73  ? 2921 ARG A C     1 
ATOM   12871 O  O     . ARG A 1 2921 ? 154.531 141.336 198.353 1.00 42.14  ? 2921 ARG A O     1 
ATOM   12872 C  CB    . ARG A 1 2921 ? 152.170 143.681 198.356 1.00 33.26  ? 2921 ARG A CB    1 
ATOM   12873 C  CG    . ARG A 1 2921 ? 150.756 144.019 198.775 1.00 36.14  ? 2921 ARG A CG    1 
ATOM   12874 C  CD    . ARG A 1 2921 ? 150.167 145.091 197.880 1.00 33.67  ? 2921 ARG A CD    1 
ATOM   12875 N  NE    . ARG A 1 2921 ? 148.897 145.590 198.391 1.00 38.44  ? 2921 ARG A NE    1 
ATOM   12876 C  CZ    . ARG A 1 2921 ? 148.202 146.573 197.836 1.00 43.85  ? 2921 ARG A CZ    1 
ATOM   12877 N  NH1   . ARG A 1 2921 ? 148.619 147.179 196.737 1.00 43.70  ? 2921 ARG A NH1   1 
ATOM   12878 N  NH2   . ARG A 1 2921 ? 147.059 146.955 198.397 1.00 44.75  ? 2921 ARG A NH2   1 
ATOM   12879 N  N     . ILE A 1 2922 ? 155.260 143.412 198.822 1.00 33.74  ? 2922 ILE A N     1 
ATOM   12880 C  CA    . ILE A 1 2922 ? 156.588 143.142 198.281 1.00 31.36  ? 2922 ILE A CA    1 
ATOM   12881 C  C     . ILE A 1 2922 ? 157.320 142.117 199.140 1.00 34.58  ? 2922 ILE A C     1 
ATOM   12882 O  O     . ILE A 1 2922 ? 158.071 141.283 198.623 1.00 39.29  ? 2922 ILE A O     1 
ATOM   12883 C  CB    . ILE A 1 2922 ? 157.388 144.448 198.136 1.00 28.06  ? 2922 ILE A CB    1 
ATOM   12884 C  CG1   . ILE A 1 2922 ? 156.603 145.465 197.311 1.00 27.49  ? 2922 ILE A CG1   1 
ATOM   12885 C  CG2   . ILE A 1 2922 ? 158.706 144.186 197.456 1.00 32.55  ? 2922 ILE A CG2   1 
ATOM   12886 C  CD1   . ILE A 1 2922 ? 157.277 146.805 197.190 1.00 31.84  ? 2922 ILE A CD1   1 
ATOM   12887 N  N     . ASP A 1 2923 ? 157.115 142.153 200.459 1.00 37.29  ? 2923 ASP A N     1 
ATOM   12888 C  CA    . ASP A 1 2923 ? 157.699 141.130 201.322 1.00 41.46  ? 2923 ASP A CA    1 
ATOM   12889 C  C     . ASP A 1 2923 ? 157.140 139.748 201.001 1.00 45.08  ? 2923 ASP A C     1 
ATOM   12890 O  O     . ASP A 1 2923 ? 157.893 138.767 200.901 1.00 49.01  ? 2923 ASP A O     1 
ATOM   12891 C  CB    . ASP A 1 2923 ? 157.451 141.482 202.786 1.00 41.28  ? 2923 ASP A CB    1 
ATOM   12892 C  CG    . ASP A 1 2923 ? 157.732 140.324 203.719 1.00 49.84  ? 2923 ASP A CG    1 
ATOM   12893 O  OD1   . ASP A 1 2923 ? 158.880 139.834 203.729 1.00 55.12  ? 2923 ASP A OD1   1 
ATOM   12894 O  OD2   . ASP A 1 2923 ? 156.804 139.905 204.444 1.00 49.26  ? 2923 ASP A OD2   1 
ATOM   12895 N  N     . ARG A 1 2924 ? 155.818 139.653 200.827 1.00 42.22  ? 2924 ARG A N     1 
ATOM   12896 C  CA    . ARG A 1 2924 ? 155.213 138.386 200.435 1.00 42.61  ? 2924 ARG A CA    1 
ATOM   12897 C  C     . ARG A 1 2924 ? 155.804 137.881 199.129 1.00 42.83  ? 2924 ARG A C     1 
ATOM   12898 O  O     . ARG A 1 2924 ? 156.095 136.689 198.990 1.00 47.35  ? 2924 ARG A O     1 
ATOM   12899 C  CB    . ARG A 1 2924 ? 153.700 138.540 200.301 1.00 41.80  ? 2924 ARG A CB    1 
ATOM   12900 C  CG    . ARG A 1 2924 ? 152.940 137.235 200.415 1.00 44.09  ? 2924 ARG A CG    1 
ATOM   12901 C  CD    . ARG A 1 2924 ? 151.485 137.424 200.039 1.00 46.35  ? 2924 ARG A CD    1 
ATOM   12902 N  NE    . ARG A 1 2924 ? 151.290 137.354 198.596 1.00 47.01  ? 2924 ARG A NE    1 
ATOM   12903 C  CZ    . ARG A 1 2924 ? 151.278 136.230 197.894 1.00 44.63  ? 2924 ARG A CZ    1 
ATOM   12904 N  NH1   . ARG A 1 2924 ? 151.415 135.051 198.476 1.00 49.15  ? 2924 ARG A NH1   1 
ATOM   12905 N  NH2   . ARG A 1 2924 ? 151.121 136.290 196.576 1.00 36.68  ? 2924 ARG A NH2   1 
ATOM   12906 N  N     . ILE A 1 2925 ? 155.989 138.778 198.160 1.00 41.59  ? 2925 ILE A N     1 
ATOM   12907 C  CA    . ILE A 1 2925 ? 156.599 138.382 196.894 1.00 36.41  ? 2925 ILE A CA    1 
ATOM   12908 C  C     . ILE A 1 2925 ? 158.016 137.876 197.119 1.00 41.05  ? 2925 ILE A C     1 
ATOM   12909 O  O     . ILE A 1 2925 ? 158.425 136.859 196.549 1.00 48.17  ? 2925 ILE A O     1 
ATOM   12910 C  CB    . ILE A 1 2925 ? 156.565 139.553 195.897 1.00 34.92  ? 2925 ILE A CB    1 
ATOM   12911 C  CG1   . ILE A 1 2925 ? 155.120 139.860 195.515 1.00 42.85  ? 2925 ILE A CG1   1 
ATOM   12912 C  CG2   . ILE A 1 2925 ? 157.397 139.237 194.672 1.00 34.38  ? 2925 ILE A CG2   1 
ATOM   12913 C  CD1   . ILE A 1 2925 ? 154.358 138.642 195.065 1.00 42.27  ? 2925 ILE A CD1   1 
ATOM   12914 N  N     . PHE A 1 2926 ? 158.785 138.571 197.957 1.00 45.68  ? 2926 PHE A N     1 
ATOM   12915 C  CA    . PHE A 1 2926 ? 160.166 138.172 198.196 1.00 43.13  ? 2926 PHE A CA    1 
ATOM   12916 C  C     . PHE A 1 2926 ? 160.275 136.874 198.982 1.00 47.91  ? 2926 PHE A C     1 
ATOM   12917 O  O     . PHE A 1 2926 ? 161.363 136.295 199.039 1.00 51.76  ? 2926 PHE A O     1 
ATOM   12918 C  CB    . PHE A 1 2926 ? 160.927 139.276 198.928 1.00 35.55  ? 2926 PHE A CB    1 
ATOM   12919 C  CG    . PHE A 1 2926 ? 161.324 140.420 198.047 1.00 35.95  ? 2926 PHE A CG    1 
ATOM   12920 C  CD1   . PHE A 1 2926 ? 161.639 140.209 196.718 1.00 35.01  ? 2926 PHE A CD1   1 
ATOM   12921 C  CD2   . PHE A 1 2926 ? 161.411 141.703 198.553 1.00 38.37  ? 2926 PHE A CD2   1 
ATOM   12922 C  CE1   . PHE A 1 2926 ? 162.011 141.256 195.906 1.00 32.51  ? 2926 PHE A CE1   1 
ATOM   12923 C  CE2   . PHE A 1 2926 ? 161.789 142.753 197.745 1.00 38.72  ? 2926 PHE A CE2   1 
ATOM   12924 C  CZ    . PHE A 1 2926 ? 162.086 142.530 196.420 1.00 35.62  ? 2926 PHE A CZ    1 
ATOM   12925 N  N     . ARG A 1 2927 ? 159.196 136.410 199.606 1.00 49.63  ? 2927 ARG A N     1 
ATOM   12926 C  CA    . ARG A 1 2927 ? 159.245 135.130 200.301 1.00 49.22  ? 2927 ARG A CA    1 
ATOM   12927 C  C     . ARG A 1 2927 ? 158.507 134.011 199.574 1.00 53.88  ? 2927 ARG A C     1 
ATOM   12928 O  O     . ARG A 1 2927 ? 158.301 132.945 200.161 1.00 57.05  ? 2927 ARG A O     1 
ATOM   12929 C  CB    . ARG A 1 2927 ? 158.700 135.277 201.722 1.00 49.57  ? 2927 ARG A CB    1 
ATOM   12930 C  CG    . ARG A 1 2927 ? 157.223 135.571 201.819 1.00 50.32  ? 2927 ARG A CG    1 
ATOM   12931 C  CD    . ARG A 1 2927 ? 156.840 135.700 203.273 1.00 54.56  ? 2927 ARG A CD    1 
ATOM   12932 N  NE    . ARG A 1 2927 ? 157.492 136.850 203.888 1.00 60.13  ? 2927 ARG A NE    1 
ATOM   12933 C  CZ    . ARG A 1 2927 ? 158.485 136.768 204.762 1.00 61.00  ? 2927 ARG A CZ    1 
ATOM   12934 N  NH1   . ARG A 1 2927 ? 158.995 135.601 205.118 1.00 63.82  ? 2927 ARG A NH1   1 
ATOM   12935 N  NH2   . ARG A 1 2927 ? 158.988 137.884 205.282 1.00 58.85  ? 2927 ARG A NH2   1 
ATOM   12936 N  N     . GLN A 1 2928 ? 158.101 134.222 198.294 1.00 54.84  ? 2928 GLN A N     1 
ATOM   12937 C  CA    . GLN A 1 2928 ? 157.425 133.207 197.497 1.00 53.96  ? 2928 GLN A CA    1 
ATOM   12938 C  C     . GLN A 1 2928 ? 158.411 132.479 196.587 1.00 58.14  ? 2928 GLN A C     1 
ATOM   12939 O  O     . GLN A 1 2928 ? 159.467 133.020 196.245 1.00 55.36  ? 2928 GLN A O     1 
ATOM   12940 C  CB    . GLN A 1 2928 ? 156.327 133.838 196.645 1.00 45.33  ? 2928 GLN A CB    1 
ATOM   12941 C  CG    . GLN A 1 2928 ? 155.071 134.214 197.405 1.00 40.32  ? 2928 GLN A CG    1 
ATOM   12942 C  CD    . GLN A 1 2928 ? 154.552 133.089 198.272 1.00 50.37  ? 2928 GLN A CD    1 
ATOM   12943 O  OE1   . GLN A 1 2928 ? 154.338 131.974 197.799 1.00 65.17  ? 2928 GLN A OE1   1 
ATOM   12944 N  NE2   . GLN A 1 2928 ? 154.335 133.378 199.550 1.00 48.40  ? 2928 GLN A NE2   1 
ATOM   12945 N  N     . PRO A 1 2929 ? 158.096 131.246 196.190 1.00 65.38  ? 2929 PRO A N     1 
ATOM   12946 C  CA    . PRO A 1 2929 ? 158.912 130.573 195.172 1.00 62.19  ? 2929 PRO A CA    1 
ATOM   12947 C  C     . PRO A 1 2929 ? 158.714 131.213 193.808 1.00 59.55  ? 2929 PRO A C     1 
ATOM   12948 O  O     . PRO A 1 2929 ? 157.584 131.435 193.367 1.00 58.78  ? 2929 PRO A O     1 
ATOM   12949 C  CB    . PRO A 1 2929 ? 158.396 129.130 195.197 1.00 54.80  ? 2929 PRO A CB    1 
ATOM   12950 C  CG    . PRO A 1 2929 ? 157.014 129.237 195.734 1.00 56.92  ? 2929 PRO A CG    1 
ATOM   12951 C  CD    . PRO A 1 2929 ? 157.038 130.367 196.717 1.00 64.81  ? 2929 PRO A CD    1 
ATOM   12952 N  N     . GLN A 1 2930 ? 159.835 131.502 193.146 1.00 62.54  ? 2930 GLN A N     1 
ATOM   12953 C  CA    . GLN A 1 2930 ? 159.890 132.290 191.909 1.00 55.50  ? 2930 GLN A CA    1 
ATOM   12954 C  C     . GLN A 1 2930 ? 158.921 133.469 191.958 1.00 51.54  ? 2930 GLN A C     1 
ATOM   12955 O  O     . GLN A 1 2930 ? 158.192 133.760 191.007 1.00 49.92  ? 2930 GLN A O     1 
ATOM   12956 C  CB    . GLN A 1 2930 ? 159.660 131.425 190.661 1.00 52.64  ? 2930 GLN A CB    1 
ATOM   12957 C  CG    . GLN A 1 2930 ? 158.296 130.770 190.500 1.00 57.20  ? 2930 GLN A CG    1 
ATOM   12958 C  CD    . GLN A 1 2930 ? 158.214 129.908 189.255 1.00 65.79  ? 2930 GLN A CD    1 
ATOM   12959 O  OE1   . GLN A 1 2930 ? 157.200 129.260 189.002 1.00 76.22  ? 2930 GLN A OE1   1 
ATOM   12960 N  NE2   . GLN A 1 2930 ? 159.280 129.901 188.467 1.00 58.53  ? 2930 GLN A NE2   1 
ATOM   12961 N  N     . GLY A 1 2931 ? 158.933 134.172 193.085 1.00 51.47  ? 2931 GLY A N     1 
ATOM   12962 C  CA    . GLY A 1 2931 ? 158.059 135.313 193.244 1.00 47.72  ? 2931 GLY A CA    1 
ATOM   12963 C  C     . GLY A 1 2931 ? 158.615 136.550 192.576 1.00 42.57  ? 2931 GLY A C     1 
ATOM   12964 O  O     . GLY A 1 2931 ? 159.535 137.188 193.093 1.00 43.69  ? 2931 GLY A O     1 
ATOM   12965 N  N     . HIS A 1 2932 ? 158.059 136.895 191.420 1.00 40.71  ? 2932 HIS A N     1 
ATOM   12966 C  CA    . HIS A 1 2932 ? 158.455 138.073 190.668 1.00 32.86  ? 2932 HIS A CA    1 
ATOM   12967 C  C     . HIS A 1 2932 ? 157.332 139.096 190.712 1.00 36.32  ? 2932 HIS A C     1 
ATOM   12968 O  O     . HIS A 1 2932 ? 156.153 138.744 190.605 1.00 43.19  ? 2932 HIS A O     1 
ATOM   12969 C  CB    . HIS A 1 2932 ? 158.794 137.717 189.220 1.00 33.67  ? 2932 HIS A CB    1 
ATOM   12970 C  CG    . HIS A 1 2932 ? 159.721 136.550 189.091 1.00 34.51  ? 2932 HIS A CG    1 
ATOM   12971 N  ND1   . HIS A 1 2932 ? 160.988 136.546 189.631 1.00 35.91  ? 2932 HIS A ND1   1 
ATOM   12972 C  CD2   . HIS A 1 2932 ? 159.565 135.349 188.489 1.00 42.47  ? 2932 HIS A CD2   1 
ATOM   12973 C  CE1   . HIS A 1 2932 ? 161.575 135.393 189.364 1.00 39.83  ? 2932 HIS A CE1   1 
ATOM   12974 N  NE2   . HIS A 1 2932 ? 160.732 134.648 188.673 1.00 47.42  ? 2932 HIS A NE2   1 
ATOM   12975 N  N     . LEU A 1 2933 ? 157.704 140.358 190.875 1.00 32.38  ? 2933 LEU A N     1 
ATOM   12976 C  CA    . LEU A 1 2933 ? 156.758 141.434 191.114 1.00 30.70  ? 2933 LEU A CA    1 
ATOM   12977 C  C     . LEU A 1 2933 ? 156.796 142.422 189.961 1.00 32.52  ? 2933 LEU A C     1 
ATOM   12978 O  O     . LEU A 1 2933 ? 157.855 142.671 189.380 1.00 36.12  ? 2933 LEU A O     1 
ATOM   12979 C  CB    . LEU A 1 2933 ? 157.084 142.150 192.424 1.00 32.32  ? 2933 LEU A CB    1 
ATOM   12980 C  CG    . LEU A 1 2933 ? 156.164 143.260 192.918 1.00 33.79  ? 2933 LEU A CG    1 
ATOM   12981 C  CD1   . LEU A 1 2933 ? 154.777 142.726 193.213 1.00 33.95  ? 2933 LEU A CD1   1 
ATOM   12982 C  CD2   . LEU A 1 2933 ? 156.770 143.893 194.146 1.00 34.49  ? 2933 LEU A CD2   1 
ATOM   12983 N  N     . LEU A 1 2934 ? 155.635 142.969 189.625 1.00 31.65  ? 2934 LEU A N     1 
ATOM   12984 C  CA    . LEU A 1 2934 ? 155.512 144.092 188.701 1.00 32.50  ? 2934 LEU A CA    1 
ATOM   12985 C  C     . LEU A 1 2934 ? 154.779 145.211 189.428 1.00 35.00  ? 2934 LEU A C     1 
ATOM   12986 O  O     . LEU A 1 2934 ? 153.563 145.145 189.630 1.00 41.20  ? 2934 LEU A O     1 
ATOM   12987 C  CB    . LEU A 1 2934 ? 154.807 143.681 187.413 1.00 34.03  ? 2934 LEU A CB    1 
ATOM   12988 C  CG    . LEU A 1 2934 ? 154.572 144.778 186.369 1.00 36.47  ? 2934 LEU A CG    1 
ATOM   12989 C  CD1   . LEU A 1 2934 ? 155.841 145.420 185.920 1.00 44.15  ? 2934 LEU A CD1   1 
ATOM   12990 C  CD2   . LEU A 1 2934 ? 153.921 144.169 185.160 1.00 37.81  ? 2934 LEU A CD2   1 
ATOM   12991 N  N     . LEU A 1 2935 ? 155.541 146.221 189.843 1.00 32.28  ? 2935 LEU A N     1 
ATOM   12992 C  CA    . LEU A 1 2935 ? 155.003 147.441 190.432 1.00 30.13  ? 2935 LEU A CA    1 
ATOM   12993 C  C     . LEU A 1 2935 ? 154.634 148.363 189.281 1.00 36.65  ? 2935 LEU A C     1 
ATOM   12994 O  O     . LEU A 1 2935 ? 155.502 148.980 188.657 1.00 44.06  ? 2935 LEU A O     1 
ATOM   12995 C  CB    . LEU A 1 2935 ? 156.028 148.088 191.355 1.00 34.57  ? 2935 LEU A CB    1 
ATOM   12996 C  CG    . LEU A 1 2935 ? 156.326 147.404 192.687 1.00 32.82  ? 2935 LEU A CG    1 
ATOM   12997 C  CD1   . LEU A 1 2935 ? 157.101 148.331 193.601 1.00 34.61  ? 2935 LEU A CD1   1 
ATOM   12998 C  CD2   . LEU A 1 2935 ? 155.039 146.977 193.345 1.00 37.97  ? 2935 LEU A CD2   1 
ATOM   12999 N  N     . ILE A 1 2936 ? 153.344 148.450 188.985 1.00 35.50  ? 2936 ILE A N     1 
ATOM   13000 C  CA    . ILE A 1 2936 ? 152.838 149.315 187.932 1.00 36.30  ? 2936 ILE A CA    1 
ATOM   13001 C  C     . ILE A 1 2936 ? 152.054 150.436 188.593 1.00 37.17  ? 2936 ILE A C     1 
ATOM   13002 O  O     . ILE A 1 2936 ? 151.261 150.198 189.509 1.00 39.66  ? 2936 ILE A O     1 
ATOM   13003 C  CB    . ILE A 1 2936 ? 151.985 148.526 186.911 1.00 36.62  ? 2936 ILE A CB    1 
ATOM   13004 C  CG1   . ILE A 1 2936 ? 151.675 149.380 185.682 1.00 43.16  ? 2936 ILE A CG1   1 
ATOM   13005 C  CG2   . ILE A 1 2936 ? 150.732 147.940 187.547 1.00 37.01  ? 2936 ILE A CG2   1 
ATOM   13006 C  CD1   . ILE A 1 2936 ? 151.149 148.583 184.515 1.00 42.45  ? 2936 ILE A CD1   1 
ATOM   13007 N  N     . GLY A 1 2937 ? 152.330 151.664 188.184 1.00 36.33  ? 2937 GLY A N     1 
ATOM   13008 C  CA    . GLY A 1 2937 ? 151.675 152.789 188.819 1.00 33.81  ? 2937 GLY A CA    1 
ATOM   13009 C  C     . GLY A 1 2937 ? 152.230 154.109 188.340 1.00 38.77  ? 2937 GLY A C     1 
ATOM   13010 O  O     . GLY A 1 2937 ? 153.141 154.171 187.511 1.00 43.83  ? 2937 GLY A O     1 
ATOM   13011 N  N     . VAL A 1 2938 ? 151.657 155.177 188.899 1.00 42.42  ? 2938 VAL A N     1 
ATOM   13012 C  CA    . VAL A 1 2938 ? 152.024 156.524 188.483 1.00 42.51  ? 2938 VAL A CA    1 
ATOM   13013 C  C     . VAL A 1 2938 ? 153.456 156.836 188.905 1.00 38.30  ? 2938 VAL A C     1 
ATOM   13014 O  O     . VAL A 1 2938 ? 154.012 156.244 189.837 1.00 39.70  ? 2938 VAL A O     1 
ATOM   13015 C  CB    . VAL A 1 2938 ? 151.039 157.557 189.053 1.00 37.98  ? 2938 VAL A CB    1 
ATOM   13016 C  CG1   . VAL A 1 2938 ? 149.611 157.170 188.709 1.00 40.57  ? 2938 VAL A CG1   1 
ATOM   13017 C  CG2   . VAL A 1 2938 ? 151.212 157.682 190.556 1.00 39.44  ? 2938 VAL A CG2   1 
ATOM   13018 N  N     . SER A 1 2939 ? 154.063 157.780 188.193 1.00 33.99  ? 2939 SER A N     1 
ATOM   13019 C  CA    . SER A 1 2939 ? 155.417 158.203 188.507 1.00 36.25  ? 2939 SER A CA    1 
ATOM   13020 C  C     . SER A 1 2939 ? 155.443 158.995 189.809 1.00 37.21  ? 2939 SER A C     1 
ATOM   13021 O  O     . SER A 1 2939 ? 154.513 159.736 190.131 1.00 44.10  ? 2939 SER A O     1 
ATOM   13022 C  CB    . SER A 1 2939 ? 155.988 159.045 187.370 1.00 40.47  ? 2939 SER A CB    1 
ATOM   13023 O  OG    . SER A 1 2939 ? 157.291 159.501 187.682 1.00 46.42  ? 2939 SER A OG    1 
ATOM   13024 N  N     . GLY A 1 2940 ? 156.523 158.824 190.566 1.00 32.78  ? 2940 GLY A N     1 
ATOM   13025 C  CA    . GLY A 1 2940 ? 156.681 159.508 191.829 1.00 31.23  ? 2940 GLY A CA    1 
ATOM   13026 C  C     . GLY A 1 2940 ? 155.927 158.899 192.988 1.00 34.96  ? 2940 GLY A C     1 
ATOM   13027 O  O     . GLY A 1 2940 ? 155.992 159.441 194.098 1.00 38.88  ? 2940 GLY A O     1 
ATOM   13028 N  N     . ALA A 1 2941 ? 155.220 157.788 192.773 1.00 32.13  ? 2941 ALA A N     1 
ATOM   13029 C  CA    . ALA A 1 2941 ? 154.440 157.183 193.846 1.00 33.07  ? 2941 ALA A CA    1 
ATOM   13030 C  C     . ALA A 1 2941 ? 155.328 156.572 194.920 1.00 37.74  ? 2941 ALA A C     1 
ATOM   13031 O  O     . ALA A 1 2941 ? 154.957 156.566 196.098 1.00 42.74  ? 2941 ALA A O     1 
ATOM   13032 C  CB    . ALA A 1 2941 ? 153.496 156.126 193.276 1.00 37.36  ? 2941 ALA A CB    1 
ATOM   13033 N  N     . GLY A 1 2942 ? 156.493 156.056 194.541 1.00 36.82  ? 2942 GLY A N     1 
ATOM   13034 C  CA    . GLY A 1 2942 ? 157.384 155.430 195.496 1.00 34.23  ? 2942 GLY A CA    1 
ATOM   13035 C  C     . GLY A 1 2942 ? 157.637 153.971 195.188 1.00 38.01  ? 2942 GLY A C     1 
ATOM   13036 O  O     . GLY A 1 2942 ? 157.892 153.173 196.093 1.00 42.10  ? 2942 GLY A O     1 
ATOM   13037 N  N     . LYS A 1 2943 ? 157.554 153.608 193.907 1.00 34.51  ? 2943 LYS A N     1 
ATOM   13038 C  CA    . LYS A 1 2943 ? 157.764 152.219 193.513 1.00 32.43  ? 2943 LYS A CA    1 
ATOM   13039 C  C     . LYS A 1 2943 ? 159.206 151.789 193.747 1.00 31.24  ? 2943 LYS A C     1 
ATOM   13040 O  O     . LYS A 1 2943 ? 159.463 150.783 194.419 1.00 38.36  ? 2943 LYS A O     1 
ATOM   13041 C  CB    . LYS A 1 2943 ? 157.374 152.040 192.047 1.00 34.62  ? 2943 LYS A CB    1 
ATOM   13042 C  CG    . LYS A 1 2943 ? 155.922 152.378 191.763 1.00 32.85  ? 2943 LYS A CG    1 
ATOM   13043 C  CD    . LYS A 1 2943 ? 155.525 152.004 190.355 1.00 33.28  ? 2943 LYS A CD    1 
ATOM   13044 C  CE    . LYS A 1 2943 ? 156.136 152.957 189.349 1.00 32.53  ? 2943 LYS A CE    1 
ATOM   13045 N  NZ    . LYS A 1 2943 ? 155.604 154.333 189.505 1.00 34.61  ? 2943 LYS A NZ    1 
ATOM   13046 N  N     . THR A 1 2944 ? 160.164 152.549 193.210 1.00 30.80  ? 2944 THR A N     1 
ATOM   13047 C  CA    . THR A 1 2944 ? 161.571 152.214 193.401 1.00 31.99  ? 2944 THR A CA    1 
ATOM   13048 C  C     . THR A 1 2944 ? 161.963 152.303 194.868 1.00 32.04  ? 2944 THR A C     1 
ATOM   13049 O  O     . THR A 1 2944 ? 162.677 151.433 195.381 1.00 37.81  ? 2944 THR A O     1 
ATOM   13050 C  CB    . THR A 1 2944 ? 162.456 153.135 192.564 1.00 31.36  ? 2944 THR A CB    1 
ATOM   13051 O  OG1   . THR A 1 2944 ? 161.980 153.167 191.214 1.00 40.43  ? 2944 THR A OG1   1 
ATOM   13052 C  CG2   . THR A 1 2944 ? 163.889 152.643 192.577 1.00 38.92  ? 2944 THR A CG2   1 
ATOM   13053 N  N     . THR A 1 2945 ? 161.502 153.348 195.555 1.00 31.24  ? 2945 THR A N     1 
ATOM   13054 C  CA    . THR A 1 2945 ? 161.850 153.532 196.958 1.00 34.36  ? 2945 THR A CA    1 
ATOM   13055 C  C     . THR A 1 2945 ? 161.381 152.354 197.799 1.00 37.62  ? 2945 THR A C     1 
ATOM   13056 O  O     . THR A 1 2945 ? 162.156 151.792 198.580 1.00 40.35  ? 2945 THR A O     1 
ATOM   13057 C  CB    . THR A 1 2945 ? 161.247 154.835 197.480 1.00 37.08  ? 2945 THR A CB    1 
ATOM   13058 O  OG1   . THR A 1 2945 ? 161.701 155.926 196.673 1.00 44.49  ? 2945 THR A OG1   1 
ATOM   13059 C  CG2   . THR A 1 2945 ? 161.665 155.073 198.911 1.00 37.46  ? 2945 THR A CG2   1 
ATOM   13060 N  N     . LEU A 1 2946 ? 160.120 151.948 197.637 1.00 37.69  ? 2946 LEU A N     1 
ATOM   13061 C  CA    . LEU A 1 2946 ? 159.597 150.859 198.454 1.00 34.58  ? 2946 LEU A CA    1 
ATOM   13062 C  C     . LEU A 1 2946 ? 160.196 149.520 198.052 1.00 37.80  ? 2946 LEU A C     1 
ATOM   13063 O  O     . LEU A 1 2946 ? 160.451 148.672 198.914 1.00 44.42  ? 2946 LEU A O     1 
ATOM   13064 C  CB    . LEU A 1 2946 ? 158.073 150.811 198.371 1.00 36.90  ? 2946 LEU A CB    1 
ATOM   13065 C  CG    . LEU A 1 2946 ? 157.378 151.929 199.142 1.00 42.69  ? 2946 LEU A CG    1 
ATOM   13066 C  CD1   . LEU A 1 2946 ? 155.871 151.765 199.082 1.00 40.79  ? 2946 LEU A CD1   1 
ATOM   13067 C  CD2   . LEU A 1 2946 ? 157.869 151.953 200.577 1.00 38.67  ? 2946 LEU A CD2   1 
ATOM   13068 N  N     . SER A 1 2947 ? 160.430 149.303 196.756 1.00 33.96  ? 2947 SER A N     1 
ATOM   13069 C  CA    . SER A 1 2947 ? 161.058 148.054 196.339 1.00 32.47  ? 2947 SER A CA    1 
ATOM   13070 C  C     . SER A 1 2947 ? 162.445 147.915 196.956 1.00 38.10  ? 2947 SER A C     1 
ATOM   13071 O  O     . SER A 1 2947 ? 162.783 146.869 197.523 1.00 44.31  ? 2947 SER A O     1 
ATOM   13072 C  CB    . SER A 1 2947 ? 161.128 147.980 194.815 1.00 28.56  ? 2947 SER A CB    1 
ATOM   13073 O  OG    . SER A 1 2947 ? 162.063 148.907 194.299 1.00 39.46  ? 2947 SER A OG    1 
ATOM   13074 N  N     . ARG A 1 2948 ? 163.247 148.982 196.895 1.00 33.75  ? 2948 ARG A N     1 
ATOM   13075 C  CA    . ARG A 1 2948 ? 164.581 148.934 197.486 1.00 31.57  ? 2948 ARG A CA    1 
ATOM   13076 C  C     . ARG A 1 2948 ? 164.513 148.823 199.003 1.00 32.55  ? 2948 ARG A C     1 
ATOM   13077 O  O     . ARG A 1 2948 ? 165.331 148.126 199.615 1.00 36.83  ? 2948 ARG A O     1 
ATOM   13078 C  CB    . ARG A 1 2948 ? 165.383 150.166 197.081 1.00 36.51  ? 2948 ARG A CB    1 
ATOM   13079 C  CG    . ARG A 1 2948 ? 165.875 150.149 195.649 1.00 41.32  ? 2948 ARG A CG    1 
ATOM   13080 C  CD    . ARG A 1 2948 ? 166.738 151.362 195.388 1.00 51.47  ? 2948 ARG A CD    1 
ATOM   13081 N  NE    . ARG A 1 2948 ? 167.443 151.772 196.597 1.00 56.65  ? 2948 ARG A NE    1 
ATOM   13082 C  CZ    . ARG A 1 2948 ? 167.544 153.023 197.021 1.00 57.39  ? 2948 ARG A CZ    1 
ATOM   13083 N  NH1   . ARG A 1 2948 ? 166.974 154.023 196.368 1.00 54.46  ? 2948 ARG A NH1   1 
ATOM   13084 N  NH2   . ARG A 1 2948 ? 168.232 153.278 198.130 1.00 60.88  ? 2948 ARG A NH2   1 
ATOM   13085 N  N     . PHE A 1 2949 ? 163.552 149.505 199.630 1.00 33.05  ? 2949 PHE A N     1 
ATOM   13086 C  CA    . PHE A 1 2949 ? 163.425 149.433 201.079 1.00 34.81  ? 2949 PHE A CA    1 
ATOM   13087 C  C     . PHE A 1 2949 ? 163.103 148.018 201.533 1.00 37.58  ? 2949 PHE A C     1 
ATOM   13088 O  O     . PHE A 1 2949 ? 163.713 147.513 202.479 1.00 42.28  ? 2949 PHE A O     1 
ATOM   13089 C  CB    . PHE A 1 2949 ? 162.352 150.407 201.563 1.00 39.15  ? 2949 PHE A CB    1 
ATOM   13090 C  CG    . PHE A 1 2949 ? 161.902 150.161 202.974 1.00 38.52  ? 2949 PHE A CG    1 
ATOM   13091 C  CD1   . PHE A 1 2949 ? 162.814 150.148 204.014 1.00 38.96  ? 2949 PHE A CD1   1 
ATOM   13092 C  CD2   . PHE A 1 2949 ? 160.568 149.940 203.260 1.00 36.48  ? 2949 PHE A CD2   1 
ATOM   13093 C  CE1   . PHE A 1 2949 ? 162.404 149.920 205.309 1.00 41.72  ? 2949 PHE A CE1   1 
ATOM   13094 C  CE2   . PHE A 1 2949 ? 160.152 149.712 204.554 1.00 36.41  ? 2949 PHE A CE2   1 
ATOM   13095 C  CZ    . PHE A 1 2949 ? 161.071 149.701 205.579 1.00 41.37  ? 2949 PHE A CZ    1 
ATOM   13096 N  N     . VAL A 1 2950 ? 162.159 147.354 200.866 1.00 38.28  ? 2950 VAL A N     1 
ATOM   13097 C  CA    . VAL A 1 2950 ? 161.805 145.994 201.259 1.00 36.69  ? 2950 VAL A CA    1 
ATOM   13098 C  C     . VAL A 1 2950 ? 162.940 145.029 200.936 1.00 42.22  ? 2950 VAL A C     1 
ATOM   13099 O  O     . VAL A 1 2950 ? 163.195 144.079 201.687 1.00 44.85  ? 2950 VAL A O     1 
ATOM   13100 C  CB    . VAL A 1 2950 ? 160.483 145.566 200.600 1.00 33.05  ? 2950 VAL A CB    1 
ATOM   13101 C  CG1   . VAL A 1 2950 ? 160.088 144.180 201.071 1.00 43.35  ? 2950 VAL A CG1   1 
ATOM   13102 C  CG2   . VAL A 1 2950 ? 159.389 146.553 200.940 1.00 32.73  ? 2950 VAL A CG2   1 
ATOM   13103 N  N     . ALA A 1 2951 ? 163.642 145.250 199.820 1.00 41.08  ? 2951 ALA A N     1 
ATOM   13104 C  CA    . ALA A 1 2951 ? 164.778 144.394 199.495 1.00 35.53  ? 2951 ALA A CA    1 
ATOM   13105 C  C     . ALA A 1 2951 ? 165.868 144.495 200.555 1.00 40.59  ? 2951 ALA A C     1 
ATOM   13106 O  O     . ALA A 1 2951 ? 166.437 143.478 200.967 1.00 48.39  ? 2951 ALA A O     1 
ATOM   13107 C  CB    . ALA A 1 2951 ? 165.328 144.754 198.117 1.00 29.72  ? 2951 ALA A CB    1 
ATOM   13108 N  N     . TRP A 1 2952 ? 166.174 145.713 201.008 1.00 39.72  ? 2952 TRP A N     1 
ATOM   13109 C  CA    . TRP A 1 2952 ? 167.128 145.876 202.102 1.00 41.92  ? 2952 TRP A CA    1 
ATOM   13110 C  C     . TRP A 1 2952 ? 166.589 145.278 203.395 1.00 42.94  ? 2952 TRP A C     1 
ATOM   13111 O  O     . TRP A 1 2952 ? 167.340 144.678 204.172 1.00 48.72  ? 2952 TRP A O     1 
ATOM   13112 C  CB    . TRP A 1 2952 ? 167.455 147.357 202.297 1.00 43.03  ? 2952 TRP A CB    1 
ATOM   13113 C  CG    . TRP A 1 2952 ? 168.136 147.655 203.600 1.00 47.57  ? 2952 TRP A CG    1 
ATOM   13114 C  CD1   . TRP A 1 2952 ? 169.476 147.632 203.846 1.00 50.09  ? 2952 TRP A CD1   1 
ATOM   13115 C  CD2   . TRP A 1 2952 ? 167.508 148.010 204.838 1.00 46.74  ? 2952 TRP A CD2   1 
ATOM   13116 N  NE1   . TRP A 1 2952 ? 169.723 147.955 205.156 1.00 46.63  ? 2952 TRP A NE1   1 
ATOM   13117 C  CE2   . TRP A 1 2952 ? 168.531 148.190 205.787 1.00 45.52  ? 2952 TRP A CE2   1 
ATOM   13118 C  CE3   . TRP A 1 2952 ? 166.181 148.193 205.235 1.00 49.63  ? 2952 TRP A CE3   1 
ATOM   13119 C  CZ2   . TRP A 1 2952 ? 168.269 148.545 207.106 1.00 53.13  ? 2952 TRP A CZ2   1 
ATOM   13120 C  CZ3   . TRP A 1 2952 ? 165.924 148.544 206.544 1.00 49.64  ? 2952 TRP A CZ3   1 
ATOM   13121 C  CH2   . TRP A 1 2952 ? 166.962 148.717 207.463 1.00 54.63  ? 2952 TRP A CH2   1 
ATOM   13122 N  N     . MET A 1 2953 ? 165.288 145.438 203.637 1.00 37.92  ? 2953 MET A N     1 
ATOM   13123 C  CA    . MET A 1 2953 ? 164.681 144.999 204.886 1.00 40.07  ? 2953 MET A CA    1 
ATOM   13124 C  C     . MET A 1 2953 ? 164.720 143.484 205.019 1.00 45.94  ? 2953 MET A C     1 
ATOM   13125 O  O     . MET A 1 2953 ? 164.894 142.953 206.121 1.00 51.27  ? 2953 MET A O     1 
ATOM   13126 C  CB    . MET A 1 2953 ? 163.247 145.522 204.943 1.00 41.49  ? 2953 MET A CB    1 
ATOM   13127 C  CG    . MET A 1 2953 ? 162.450 145.180 206.175 1.00 47.72  ? 2953 MET A CG    1 
ATOM   13128 S  SD    . MET A 1 2953 ? 160.847 145.993 206.052 1.00 59.04  ? 2953 MET A SD    1 
ATOM   13129 C  CE    . MET A 1 2953 ? 160.329 146.019 207.759 1.00 59.05  ? 2953 MET A CE    1 
ATOM   13130 N  N     . ASN A 1 2954 ? 164.558 142.772 203.908 1.00 43.97  ? 2954 ASN A N     1 
ATOM   13131 C  CA    . ASN A 1 2954 ? 164.602 141.317 203.903 1.00 42.18  ? 2954 ASN A CA    1 
ATOM   13132 C  C     . ASN A 1 2954 ? 165.992 140.764 203.613 1.00 44.81  ? 2954 ASN A C     1 
ATOM   13133 O  O     . ASN A 1 2954 ? 166.157 139.541 203.558 1.00 47.76  ? 2954 ASN A O     1 
ATOM   13134 C  CB    . ASN A 1 2954 ? 163.603 140.765 202.884 1.00 40.77  ? 2954 ASN A CB    1 
ATOM   13135 C  CG    . ASN A 1 2954 ? 162.170 140.912 203.339 1.00 42.97  ? 2954 ASN A CG    1 
ATOM   13136 O  OD1   . ASN A 1 2954 ? 161.904 141.352 204.455 1.00 45.26  ? 2954 ASN A OD1   1 
ATOM   13137 N  ND2   . ASN A 1 2954 ? 161.235 140.543 202.475 1.00 49.91  ? 2954 ASN A ND2   1 
ATOM   13138 N  N     . GLY A 1 2955 ? 166.989 141.625 203.429 1.00 42.62  ? 2955 GLY A N     1 
ATOM   13139 C  CA    . GLY A 1 2955 ? 168.348 141.186 203.205 1.00 41.90  ? 2955 GLY A CA    1 
ATOM   13140 C  C     . GLY A 1 2955 ? 168.704 140.861 201.772 1.00 45.89  ? 2955 GLY A C     1 
ATOM   13141 O  O     . GLY A 1 2955 ? 169.830 140.414 201.521 1.00 50.29  ? 2955 GLY A O     1 
ATOM   13142 N  N     . LEU A 1 2956 ? 167.792 141.062 200.828 1.00 41.18  ? 2956 LEU A N     1 
ATOM   13143 C  CA    . LEU A 1 2956 ? 168.095 140.781 199.433 1.00 37.36  ? 2956 LEU A CA    1 
ATOM   13144 C  C     . LEU A 1 2956 ? 169.116 141.769 198.888 1.00 38.43  ? 2956 LEU A C     1 
ATOM   13145 O  O     . LEU A 1 2956 ? 169.139 142.946 199.257 1.00 44.84  ? 2956 LEU A O     1 
ATOM   13146 C  CB    . LEU A 1 2956 ? 166.828 140.826 198.580 1.00 38.18  ? 2956 LEU A CB    1 
ATOM   13147 C  CG    . LEU A 1 2956 ? 165.907 139.606 198.598 1.00 41.11  ? 2956 LEU A CG    1 
ATOM   13148 C  CD1   . LEU A 1 2956 ? 165.128 139.490 199.896 1.00 37.11  ? 2956 LEU A CD1   1 
ATOM   13149 C  CD2   . LEU A 1 2956 ? 164.975 139.645 197.407 1.00 38.08  ? 2956 LEU A CD2   1 
ATOM   13150 N  N     . SER A 1 2957 ? 169.968 141.275 197.995 1.00 39.15  ? 2957 SER A N     1 
ATOM   13151 C  CA    . SER A 1 2957 ? 170.990 142.090 197.351 1.00 41.79  ? 2957 SER A CA    1 
ATOM   13152 C  C     . SER A 1 2957 ? 170.395 142.692 196.085 1.00 42.36  ? 2957 SER A C     1 
ATOM   13153 O  O     . SER A 1 2957 ? 170.046 141.966 195.150 1.00 47.57  ? 2957 SER A O     1 
ATOM   13154 C  CB    . SER A 1 2957 ? 172.225 141.252 197.037 1.00 47.07  ? 2957 SER A CB    1 
ATOM   13155 O  OG    . SER A 1 2957 ? 172.788 140.715 198.221 1.00 53.24  ? 2957 SER A OG    1 
ATOM   13156 N  N     . VAL A 1 2958 ? 170.281 144.017 196.050 1.00 43.64  ? 2958 VAL A N     1 
ATOM   13157 C  CA    . VAL A 1 2958 ? 169.669 144.687 194.910 1.00 44.63  ? 2958 VAL A CA    1 
ATOM   13158 C  C     . VAL A 1 2958 ? 170.663 144.714 193.758 1.00 52.74  ? 2958 VAL A C     1 
ATOM   13159 O  O     . VAL A 1 2958 ? 171.796 145.184 193.908 1.00 62.12  ? 2958 VAL A O     1 
ATOM   13160 C  CB    . VAL A 1 2958 ? 169.218 146.104 195.283 1.00 48.63  ? 2958 VAL A CB    1 
ATOM   13161 C  CG1   . VAL A 1 2958 ? 168.740 146.850 194.049 1.00 49.93  ? 2958 VAL A CG1   1 
ATOM   13162 C  CG2   . VAL A 1 2958 ? 168.130 146.052 196.335 1.00 46.33  ? 2958 VAL A CG2   1 
ATOM   13163 N  N     . TYR A 1 2959 ? 170.243 144.207 192.603 1.00 49.46  ? 2959 TYR A N     1 
ATOM   13164 C  CA    . TYR A 1 2959 ? 171.045 144.246 191.389 1.00 56.75  ? 2959 TYR A CA    1 
ATOM   13165 C  C     . TYR A 1 2959 ? 170.202 144.873 190.290 1.00 63.57  ? 2959 TYR A C     1 
ATOM   13166 O  O     . TYR A 1 2959 ? 169.046 144.483 190.095 1.00 64.80  ? 2959 TYR A O     1 
ATOM   13167 C  CB    . TYR A 1 2959 ? 171.508 142.842 190.985 1.00 59.10  ? 2959 TYR A CB    1 
ATOM   13168 C  CG    . TYR A 1 2959 ? 172.341 142.795 189.722 1.00 67.66  ? 2959 TYR A CG    1 
ATOM   13169 C  CD1   . TYR A 1 2959 ? 173.726 142.781 189.789 1.00 71.17  ? 2959 TYR A CD1   1 
ATOM   13170 C  CD2   . TYR A 1 2959 ? 171.749 142.771 188.468 1.00 69.21  ? 2959 TYR A CD2   1 
ATOM   13171 C  CE1   . TYR A 1 2959 ? 174.496 142.740 188.645 1.00 77.41  ? 2959 TYR A CE1   1 
ATOM   13172 C  CE2   . TYR A 1 2959 ? 172.511 142.735 187.317 1.00 72.12  ? 2959 TYR A CE2   1 
ATOM   13173 C  CZ    . TYR A 1 2959 ? 173.884 142.717 187.412 1.00 78.93  ? 2959 TYR A CZ    1 
ATOM   13174 O  OH    . TYR A 1 2959 ? 174.650 142.677 186.271 1.00 84.30  ? 2959 TYR A OH    1 
ATOM   13175 N  N     . GLN A 1 2960 ? 170.771 145.844 189.580 1.00 69.41  ? 2960 GLN A N     1 
ATOM   13176 C  CA    . GLN A 1 2960 ? 170.060 146.552 188.523 1.00 72.23  ? 2960 GLN A CA    1 
ATOM   13177 C  C     . GLN A 1 2960 ? 170.887 146.537 187.248 1.00 81.81  ? 2960 GLN A C     1 
ATOM   13178 O  O     . GLN A 1 2960 ? 172.115 146.653 187.297 1.00 85.05  ? 2960 GLN A O     1 
ATOM   13179 C  CB    . GLN A 1 2960 ? 169.745 147.995 188.930 1.00 67.85  ? 2960 GLN A CB    1 
ATOM   13180 C  CG    . GLN A 1 2960 ? 169.252 148.151 190.356 1.00 64.96  ? 2960 GLN A CG    1 
ATOM   13181 C  CD    . GLN A 1 2960 ? 168.479 149.436 190.562 1.00 74.24  ? 2960 GLN A CD    1 
ATOM   13182 O  OE1   . GLN A 1 2960 ? 168.026 150.060 189.604 1.00 77.99  ? 2960 GLN A OE1   1 
ATOM   13183 N  NE2   . GLN A 1 2960 ? 168.320 149.837 191.818 1.00 71.65  ? 2960 GLN A NE2   1 
ATOM   13184 N  N     . ILE A 1 2961 ? 170.207 146.392 186.109 1.00 86.73  ? 2961 ILE A N     1 
ATOM   13185 C  CA    . ILE A 1 2961 ? 170.890 146.409 184.823 1.00 93.62  ? 2961 ILE A CA    1 
ATOM   13186 C  C     . ILE A 1 2961 ? 171.297 147.832 184.472 1.00 96.39  ? 2961 ILE A C     1 
ATOM   13187 O  O     . ILE A 1 2961 ? 170.543 148.790 184.690 1.00 96.86  ? 2961 ILE A O     1 
ATOM   13188 C  CB    . ILE A 1 2961 ? 169.991 145.798 183.734 1.00 95.15  ? 2961 ILE A CB    1 
ATOM   13189 C  CG1   . ILE A 1 2961 ? 169.662 144.350 184.080 1.00 92.68  ? 2961 ILE A CG1   1 
ATOM   13190 C  CG2   . ILE A 1 2961 ? 170.664 145.859 182.375 1.00 100.06 ? 2961 ILE A CG2   1 
ATOM   13191 C  CD1   . ILE A 1 2961 ? 170.880 143.461 184.139 1.00 91.06  ? 2961 ILE A CD1   1 
ATOM   13192 N  N     . LYS A 1 2962 ? 172.501 147.977 183.929 1.00 98.44  ? 2962 LYS A N     1 
ATOM   13193 C  CA    . LYS A 1 2962 ? 173.031 149.265 183.492 1.00 102.20 ? 2962 LYS A CA    1 
ATOM   13194 C  C     . LYS A 1 2962 ? 173.191 149.213 181.974 1.00 106.53 ? 2962 LYS A C     1 
ATOM   13195 O  O     . LYS A 1 2962 ? 174.263 148.893 181.458 1.00 107.39 ? 2962 LYS A O     1 
ATOM   13196 C  CB    . LYS A 1 2962 ? 174.353 149.572 184.190 1.00 103.54 ? 2962 LYS A CB    1 
ATOM   13197 C  CG    . LYS A 1 2962 ? 174.253 149.620 185.706 1.00 101.07 ? 2962 LYS A CG    1 
ATOM   13198 C  CD    . LYS A 1 2962 ? 175.531 150.150 186.331 1.00 96.71  ? 2962 LYS A CD    1 
ATOM   13199 C  CE    . LYS A 1 2962 ? 176.740 149.358 185.868 1.00 98.79  ? 2962 LYS A CE    1 
ATOM   13200 N  NZ    . LYS A 1 2962 ? 176.620 147.915 186.212 1.00 99.46  ? 2962 LYS A NZ    1 
ATOM   13201 N  N     . VAL A 1 2963 ? 172.112 149.531 181.260 1.00 111.23 ? 2963 VAL A N     1 
ATOM   13202 C  CA    . VAL A 1 2963 ? 172.133 149.575 179.802 1.00 117.76 ? 2963 VAL A CA    1 
ATOM   13203 C  C     . VAL A 1 2963 ? 172.825 150.857 179.365 1.00 119.84 ? 2963 VAL A C     1 
ATOM   13204 O  O     . VAL A 1 2963 ? 172.906 151.821 180.133 1.00 121.91 ? 2963 VAL A O     1 
ATOM   13205 C  CB    . VAL A 1 2963 ? 170.714 149.485 179.213 1.00 117.35 ? 2963 VAL A CB    1 
ATOM   13206 C  CG1   . VAL A 1 2963 ? 170.111 148.121 179.493 1.00 116.62 ? 2963 VAL A CG1   1 
ATOM   13207 C  CG2   . VAL A 1 2963 ? 169.836 150.592 179.776 1.00 113.58 ? 2963 VAL A CG2   1 
ATOM   13208 N  N     . HIS A 1 2964 ? 173.317 150.885 178.130 1.00 120.26 ? 2964 HIS A N     1 
ATOM   13209 C  CA    . HIS A 1 2964 ? 174.100 152.017 177.656 1.00 123.45 ? 2964 HIS A CA    1 
ATOM   13210 C  C     . HIS A 1 2964 ? 173.782 152.260 176.186 1.00 132.48 ? 2964 HIS A C     1 
ATOM   13211 O  O     . HIS A 1 2964 ? 172.811 151.724 175.642 1.00 125.74 ? 2964 HIS A O     1 
ATOM   13212 C  CB    . HIS A 1 2964 ? 175.597 151.772 177.880 1.00 120.38 ? 2964 HIS A CB    1 
ATOM   13213 C  CG    . HIS A 1 2964 ? 176.113 150.525 177.231 1.00 123.74 ? 2964 HIS A CG    1 
ATOM   13214 N  ND1   . HIS A 1 2964 ? 176.703 149.504 177.944 1.00 124.91 ? 2964 HIS A ND1   1 
ATOM   13215 C  CD2   . HIS A 1 2964 ? 176.139 150.138 175.933 1.00 128.07 ? 2964 HIS A CD2   1 
ATOM   13216 C  CE1   . HIS A 1 2964 ? 177.064 148.540 177.116 1.00 127.66 ? 2964 HIS A CE1   1 
ATOM   13217 N  NE2   . HIS A 1 2964 ? 176.733 148.900 175.890 1.00 129.21 ? 2964 HIS A NE2   1 
ATOM   13218 N  N     . ARG A 1 2965 ? 174.612 153.082 175.546 1.00 138.33 ? 2965 ARG A N     1 
ATOM   13219 C  CA    . ARG A 1 2965 ? 174.490 153.376 174.126 1.00 139.00 ? 2965 ARG A CA    1 
ATOM   13220 C  C     . ARG A 1 2965 ? 174.743 152.114 173.310 1.00 136.64 ? 2965 ARG A C     1 
ATOM   13221 O  O     . ARG A 1 2965 ? 175.867 151.601 173.284 1.00 132.98 ? 2965 ARG A O     1 
ATOM   13222 C  CB    . ARG A 1 2965 ? 175.466 154.490 173.736 1.00 138.82 ? 2965 ARG A CB    1 
ATOM   13223 C  CG    . ARG A 1 2965 ? 175.326 155.004 172.314 1.00 139.40 ? 2965 ARG A CG    1 
ATOM   13224 C  CD    . ARG A 1 2965 ? 174.012 155.741 172.110 1.00 139.36 ? 2965 ARG A CD    1 
ATOM   13225 N  NE    . ARG A 1 2965 ? 172.958 154.862 171.618 1.00 139.61 ? 2965 ARG A NE    1 
ATOM   13226 C  CZ    . ARG A 1 2965 ? 171.678 155.200 171.537 1.00 141.57 ? 2965 ARG A CZ    1 
ATOM   13227 N  NH1   . ARG A 1 2965 ? 171.254 156.396 171.911 1.00 140.27 ? 2965 ARG A NH1   1 
ATOM   13228 N  NH2   . ARG A 1 2965 ? 170.802 154.315 171.069 1.00 139.07 ? 2965 ARG A NH2   1 
ATOM   13229 N  N     . LYS A 1 2966 ? 173.701 151.611 172.644 1.00 138.01 ? 2966 LYS A N     1 
ATOM   13230 C  CA    . LYS A 1 2966 ? 173.742 150.341 171.917 1.00 136.64 ? 2966 LYS A CA    1 
ATOM   13231 C  C     . LYS A 1 2966 ? 174.122 149.188 172.850 1.00 133.88 ? 2966 LYS A C     1 
ATOM   13232 O  O     . LYS A 1 2966 ? 175.159 148.540 172.697 1.00 133.17 ? 2966 LYS A O     1 
ATOM   13233 C  CB    . LYS A 1 2966 ? 174.689 150.409 170.712 1.00 135.89 ? 2966 LYS A CB    1 
ATOM   13234 C  CG    . LYS A 1 2966 ? 174.210 151.295 169.573 1.00 134.36 ? 2966 LYS A CG    1 
ATOM   13235 C  CD    . LYS A 1 2966 ? 174.722 152.713 169.723 1.00 138.81 ? 2966 LYS A CD    1 
ATOM   13236 C  CE    . LYS A 1 2966 ? 174.228 153.606 168.599 1.00 138.07 ? 2966 LYS A CE    1 
ATOM   13237 N  NZ    . LYS A 1 2966 ? 174.775 154.987 168.714 1.00 139.75 ? 2966 LYS A NZ    1 
ATOM   13238 N  N     . TYR A 1 2967 ? 173.256 148.947 173.832 1.00 131.28 ? 2967 TYR A N     1 
ATOM   13239 C  CA    . TYR A 1 2967 ? 173.455 147.824 174.736 1.00 127.24 ? 2967 TYR A CA    1 
ATOM   13240 C  C     . TYR A 1 2967 ? 173.276 146.513 173.982 1.00 125.97 ? 2967 TYR A C     1 
ATOM   13241 O  O     . TYR A 1 2967 ? 172.261 146.292 173.315 1.00 125.65 ? 2967 TYR A O     1 
ATOM   13242 C  CB    . TYR A 1 2967 ? 172.473 147.906 175.904 1.00 125.05 ? 2967 TYR A CB    1 
ATOM   13243 C  CG    . TYR A 1 2967 ? 172.781 146.966 177.048 1.00 122.27 ? 2967 TYR A CG    1 
ATOM   13244 C  CD1   . TYR A 1 2967 ? 173.932 147.119 177.807 1.00 119.58 ? 2967 TYR A CD1   1 
ATOM   13245 C  CD2   . TYR A 1 2967 ? 171.913 145.934 177.377 1.00 119.54 ? 2967 TYR A CD2   1 
ATOM   13246 C  CE1   . TYR A 1 2967 ? 174.213 146.268 178.857 1.00 114.11 ? 2967 TYR A CE1   1 
ATOM   13247 C  CE2   . TYR A 1 2967 ? 172.186 145.078 178.427 1.00 112.77 ? 2967 TYR A CE2   1 
ATOM   13248 C  CZ    . TYR A 1 2967 ? 173.337 145.250 179.162 1.00 109.45 ? 2967 TYR A CZ    1 
ATOM   13249 O  OH    . TYR A 1 2967 ? 173.613 144.399 180.207 1.00 104.58 ? 2967 TYR A OH    1 
ATOM   13250 N  N     . THR A 1 2968 ? 174.268 145.637 174.095 1.00 122.97 ? 2968 THR A N     1 
ATOM   13251 C  CA    . THR A 1 2968 ? 174.313 144.401 173.329 1.00 121.50 ? 2968 THR A CA    1 
ATOM   13252 C  C     . THR A 1 2968 ? 173.616 143.284 174.094 1.00 118.08 ? 2968 THR A C     1 
ATOM   13253 O  O     . THR A 1 2968 ? 173.705 143.210 175.323 1.00 117.50 ? 2968 THR A O     1 
ATOM   13254 C  CB    . THR A 1 2968 ? 175.762 144.006 173.026 1.00 122.33 ? 2968 THR A CB    1 
ATOM   13255 O  OG1   . THR A 1 2968 ? 176.433 145.102 172.391 1.00 129.68 ? 2968 THR A OG1   1 
ATOM   13256 C  CG2   . THR A 1 2968 ? 175.816 142.796 172.104 1.00 116.86 ? 2968 THR A CG2   1 
ATOM   13257 N  N     . GLY A 1 2969 ? 172.912 142.420 173.357 1.00 117.86 ? 2969 GLY A N     1 
ATOM   13258 C  CA    . GLY A 1 2969 ? 172.291 141.264 173.978 1.00 113.82 ? 2969 GLY A CA    1 
ATOM   13259 C  C     . GLY A 1 2969 ? 173.290 140.347 174.654 1.00 111.80 ? 2969 GLY A C     1 
ATOM   13260 O  O     . GLY A 1 2969 ? 172.947 139.644 175.608 1.00 114.01 ? 2969 GLY A O     1 
ATOM   13261 N  N     . GLU A 1 2970 ? 174.536 140.338 174.174 1.00 109.03 ? 2970 GLU A N     1 
ATOM   13262 C  CA    . GLU A 1 2970 ? 175.586 139.584 174.851 1.00 109.69 ? 2970 GLU A CA    1 
ATOM   13263 C  C     . GLU A 1 2970 ? 175.855 140.148 176.239 1.00 110.00 ? 2970 GLU A C     1 
ATOM   13264 O  O     . GLU A 1 2970 ? 176.109 139.395 177.187 1.00 108.76 ? 2970 GLU A O     1 
ATOM   13265 C  CB    . GLU A 1 2970 ? 176.861 139.589 174.007 1.00 115.76 ? 2970 GLU A CB    1 
ATOM   13266 C  CG    . GLU A 1 2970 ? 177.891 138.543 174.411 1.00 119.50 ? 2970 GLU A CG    1 
ATOM   13267 C  CD    . GLU A 1 2970 ? 178.799 139.015 175.532 1.00 120.12 ? 2970 GLU A CD    1 
ATOM   13268 O  OE1   . GLU A 1 2970 ? 179.068 140.232 175.609 1.00 119.97 ? 2970 GLU A OE1   1 
ATOM   13269 O  OE2   . GLU A 1 2970 ? 179.244 138.168 176.335 1.00 115.90 ? 2970 GLU A OE2   1 
ATOM   13270 N  N     . ASP A 1 2971 ? 175.815 141.475 176.379 1.00 112.68 ? 2971 ASP A N     1 
ATOM   13271 C  CA    . ASP A 1 2971 ? 175.989 142.084 177.693 1.00 110.02 ? 2971 ASP A CA    1 
ATOM   13272 C  C     . ASP A 1 2971 ? 174.856 141.696 178.635 1.00 105.36 ? 2971 ASP A C     1 
ATOM   13273 O  O     . ASP A 1 2971 ? 175.088 141.412 179.816 1.00 100.56 ? 2971 ASP A O     1 
ATOM   13274 C  CB    . ASP A 1 2971 ? 176.081 143.604 177.558 1.00 113.14 ? 2971 ASP A CB    1 
ATOM   13275 C  CG    . ASP A 1 2971 ? 177.190 144.039 176.621 1.00 117.67 ? 2971 ASP A CG    1 
ATOM   13276 O  OD1   . ASP A 1 2971 ? 177.921 143.163 176.115 1.00 118.59 ? 2971 ASP A OD1   1 
ATOM   13277 O  OD2   . ASP A 1 2971 ? 177.330 145.258 176.390 1.00 121.40 ? 2971 ASP A OD2   1 
ATOM   13278 N  N     . PHE A 1 2972 ? 173.619 141.681 178.130 1.00 103.19 ? 2972 PHE A N     1 
ATOM   13279 C  CA    . PHE A 1 2972 ? 172.494 141.239 178.947 1.00 100.31 ? 2972 PHE A CA    1 
ATOM   13280 C  C     . PHE A 1 2972 ? 172.643 139.775 179.335 1.00 94.33  ? 2972 PHE A C     1 
ATOM   13281 O  O     . PHE A 1 2972 ? 172.317 139.386 180.464 1.00 95.00  ? 2972 PHE A O     1 
ATOM   13282 C  CB    . PHE A 1 2972 ? 171.181 141.469 178.199 1.00 100.26 ? 2972 PHE A CB    1 
ATOM   13283 C  CG    . PHE A 1 2972 ? 169.958 141.128 179.002 1.00 100.58 ? 2972 PHE A CG    1 
ATOM   13284 C  CD1   . PHE A 1 2972 ? 169.708 141.758 180.209 1.00 96.65  ? 2972 PHE A CD1   1 
ATOM   13285 C  CD2   . PHE A 1 2972 ? 169.059 140.180 178.549 1.00 98.93  ? 2972 PHE A CD2   1 
ATOM   13286 C  CE1   . PHE A 1 2972 ? 168.585 141.447 180.949 1.00 86.09  ? 2972 PHE A CE1   1 
ATOM   13287 C  CE2   . PHE A 1 2972 ? 167.934 139.865 179.285 1.00 93.91  ? 2972 PHE A CE2   1 
ATOM   13288 C  CZ    . PHE A 1 2972 ? 167.697 140.499 180.486 1.00 88.25  ? 2972 PHE A CZ    1 
ATOM   13289 N  N     . ASP A 1 2973 ? 173.135 138.948 178.411 1.00 92.29  ? 2973 ASP A N     1 
ATOM   13290 C  CA    . ASP A 1 2973 ? 173.381 137.546 178.729 1.00 92.36  ? 2973 ASP A CA    1 
ATOM   13291 C  C     . ASP A 1 2973 ? 174.433 137.406 179.821 1.00 93.59  ? 2973 ASP A C     1 
ATOM   13292 O  O     . ASP A 1 2973 ? 174.295 136.572 180.719 1.00 92.40  ? 2973 ASP A O     1 
ATOM   13293 C  CB    . ASP A 1 2973 ? 173.808 136.789 177.473 1.00 97.60  ? 2973 ASP A CB    1 
ATOM   13294 C  CG    . ASP A 1 2973 ? 172.688 136.665 176.460 1.00 102.77 ? 2973 ASP A CG    1 
ATOM   13295 O  OD1   . ASP A 1 2973 ? 172.969 136.293 175.301 1.00 104.07 ? 2973 ASP A OD1   1 
ATOM   13296 O  OD2   . ASP A 1 2973 ? 171.527 136.942 176.824 1.00 101.29 ? 2973 ASP A OD2   1 
ATOM   13297 N  N     . GLU A 1 2974 ? 175.496 138.211 179.758 1.00 95.65  ? 2974 GLU A N     1 
ATOM   13298 C  CA    . GLU A 1 2974 ? 176.522 138.168 180.798 1.00 92.08  ? 2974 GLU A CA    1 
ATOM   13299 C  C     . GLU A 1 2974 ? 175.964 138.614 182.145 1.00 89.77  ? 2974 GLU A C     1 
ATOM   13300 O  O     . GLU A 1 2974 ? 176.291 138.032 183.189 1.00 86.81  ? 2974 GLU A O     1 
ATOM   13301 C  CB    . GLU A 1 2974 ? 177.716 139.035 180.397 1.00 97.69  ? 2974 GLU A CB    1 
ATOM   13302 C  CG    . GLU A 1 2974 ? 178.787 138.313 179.582 1.00 106.05 ? 2974 GLU A CG    1 
ATOM   13303 C  CD    . GLU A 1 2974 ? 179.640 137.351 180.402 1.00 102.50 ? 2974 GLU A CD    1 
ATOM   13304 O  OE1   . GLU A 1 2974 ? 179.244 136.983 181.527 1.00 99.13  ? 2974 GLU A OE1   1 
ATOM   13305 O  OE2   . GLU A 1 2974 ? 180.720 136.961 179.910 1.00 98.93  ? 2974 GLU A OE2   1 
ATOM   13306 N  N     . ASP A 1 2975 ? 175.130 139.656 182.143 1.00 93.12  ? 2975 ASP A N     1 
ATOM   13307 C  CA    . ASP A 1 2975 ? 174.492 140.092 183.382 1.00 89.89  ? 2975 ASP A CA    1 
ATOM   13308 C  C     . ASP A 1 2975 ? 173.621 138.987 183.964 1.00 82.08  ? 2975 ASP A C     1 
ATOM   13309 O  O     . ASP A 1 2975 ? 173.638 138.745 185.177 1.00 80.46  ? 2975 ASP A O     1 
ATOM   13310 C  CB    . ASP A 1 2975 ? 173.664 141.352 183.134 1.00 88.84  ? 2975 ASP A CB    1 
ATOM   13311 C  CG    . ASP A 1 2975 ? 174.501 142.511 182.634 1.00 97.82  ? 2975 ASP A CG    1 
ATOM   13312 O  OD1   . ASP A 1 2975 ? 175.716 142.320 182.420 1.00 107.33 ? 2975 ASP A OD1   1 
ATOM   13313 O  OD2   . ASP A 1 2975 ? 173.943 143.613 182.454 1.00 97.44  ? 2975 ASP A OD2   1 
ATOM   13314 N  N     . LEU A 1 2976 ? 172.858 138.300 183.111 1.00 81.66  ? 2976 LEU A N     1 
ATOM   13315 C  CA    . LEU A 1 2976 ? 172.064 137.169 183.577 1.00 78.51  ? 2976 LEU A CA    1 
ATOM   13316 C  C     . LEU A 1 2976 ? 172.952 136.057 184.119 1.00 79.98  ? 2976 LEU A C     1 
ATOM   13317 O  O     . LEU A 1 2976 ? 172.618 135.425 185.125 1.00 79.95  ? 2976 LEU A O     1 
ATOM   13318 C  CB    . LEU A 1 2976 ? 171.176 136.642 182.451 1.00 79.37  ? 2976 LEU A CB    1 
ATOM   13319 C  CG    . LEU A 1 2976 ? 169.985 137.511 182.053 1.00 81.32  ? 2976 LEU A CG    1 
ATOM   13320 C  CD1   . LEU A 1 2976 ? 169.262 136.907 180.862 1.00 79.79  ? 2976 LEU A CD1   1 
ATOM   13321 C  CD2   . LEU A 1 2976 ? 169.041 137.678 183.228 1.00 79.57  ? 2976 LEU A CD2   1 
ATOM   13322 N  N     . ARG A 1 2977 ? 174.079 135.790 183.457 1.00 78.47  ? 2977 ARG A N     1 
ATOM   13323 C  CA    . ARG A 1 2977 ? 175.001 134.774 183.954 1.00 74.87  ? 2977 ARG A CA    1 
ATOM   13324 C  C     . ARG A 1 2977 ? 175.466 135.110 185.363 1.00 72.37  ? 2977 ARG A C     1 
ATOM   13325 O  O     . ARG A 1 2977 ? 175.441 134.257 186.255 1.00 72.97  ? 2977 ARG A O     1 
ATOM   13326 C  CB    . ARG A 1 2977 ? 176.200 134.632 183.015 1.00 81.63  ? 2977 ARG A CB    1 
ATOM   13327 C  CG    . ARG A 1 2977 ? 175.869 134.072 181.647 1.00 86.63  ? 2977 ARG A CG    1 
ATOM   13328 C  CD    . ARG A 1 2977 ? 176.993 134.327 180.659 1.00 94.49  ? 2977 ARG A CD    1 
ATOM   13329 N  NE    . ARG A 1 2977 ? 176.522 134.261 179.281 1.00 98.78  ? 2977 ARG A NE    1 
ATOM   13330 C  CZ    . ARG A 1 2977 ? 177.256 134.569 178.221 1.00 101.93 ? 2977 ARG A CZ    1 
ATOM   13331 N  NH1   . ARG A 1 2977 ? 178.512 134.968 178.342 1.00 104.08 ? 2977 ARG A NH1   1 
ATOM   13332 N  NH2   . ARG A 1 2977 ? 176.716 134.476 177.009 1.00 103.28 ? 2977 ARG A NH2   1 
ATOM   13333 N  N     . THR A 1 2978 ? 175.870 136.362 185.585 1.00 71.23  ? 2978 THR A N     1 
ATOM   13334 C  CA    . THR A 1 2978 ? 176.317 136.768 186.917 1.00 73.01  ? 2978 THR A CA    1 
ATOM   13335 C  C     . THR A 1 2978 ? 175.191 136.642 187.939 1.00 72.87  ? 2978 THR A C     1 
ATOM   13336 O  O     . THR A 1 2978 ? 175.393 136.120 189.044 1.00 73.89  ? 2978 THR A O     1 
ATOM   13337 C  CB    . THR A 1 2978 ? 176.851 138.200 186.885 1.00 75.32  ? 2978 THR A CB    1 
ATOM   13338 O  OG1   . THR A 1 2978 ? 175.787 139.104 186.563 1.00 76.18  ? 2978 THR A OG1   1 
ATOM   13339 C  CG2   . THR A 1 2978 ? 177.964 138.338 185.860 1.00 82.69  ? 2978 THR A CG2   1 
ATOM   13340 N  N     . VAL A 1 2979 ? 173.991 137.106 187.580 1.00 70.71  ? 2979 VAL A N     1 
ATOM   13341 C  CA    . VAL A 1 2979 ? 172.881 137.113 188.531 1.00 60.40  ? 2979 VAL A CA    1 
ATOM   13342 C  C     . VAL A 1 2979 ? 172.493 135.690 188.915 1.00 66.26  ? 2979 VAL A C     1 
ATOM   13343 O  O     . VAL A 1 2979 ? 172.321 135.376 190.098 1.00 67.30  ? 2979 VAL A O     1 
ATOM   13344 C  CB    . VAL A 1 2979 ? 171.684 137.889 187.956 1.00 60.68  ? 2979 VAL A CB    1 
ATOM   13345 C  CG1   . VAL A 1 2979 ? 170.481 137.728 188.850 1.00 63.06  ? 2979 VAL A CG1   1 
ATOM   13346 C  CG2   . VAL A 1 2979 ? 172.031 139.349 187.821 1.00 68.09  ? 2979 VAL A CG2   1 
ATOM   13347 N  N     . LEU A 1 2980 ? 172.347 134.806 187.925 1.00 70.58  ? 2980 LEU A N     1 
ATOM   13348 C  CA    . LEU A 1 2980 ? 171.981 133.426 188.227 1.00 67.46  ? 2980 LEU A CA    1 
ATOM   13349 C  C     . LEU A 1 2980 ? 173.109 132.672 188.915 1.00 70.64  ? 2980 LEU A C     1 
ATOM   13350 O  O     . LEU A 1 2980 ? 172.841 131.784 189.729 1.00 74.04  ? 2980 LEU A O     1 
ATOM   13351 C  CB    . LEU A 1 2980 ? 171.542 132.685 186.963 1.00 63.13  ? 2980 LEU A CB    1 
ATOM   13352 C  CG    . LEU A 1 2980 ? 170.120 132.900 186.432 1.00 63.04  ? 2980 LEU A CG    1 
ATOM   13353 C  CD1   . LEU A 1 2980 ? 169.905 134.267 185.823 1.00 66.57  ? 2980 LEU A CD1   1 
ATOM   13354 C  CD2   . LEU A 1 2980 ? 169.771 131.817 185.427 1.00 70.41  ? 2980 LEU A CD2   1 
ATOM   13355 N  N     . ARG A 1 2981 ? 174.367 132.998 188.612 1.00 69.95  ? 2981 ARG A N     1 
ATOM   13356 C  CA    . ARG A 1 2981 ? 175.474 132.368 189.318 1.00 72.51  ? 2981 ARG A CA    1 
ATOM   13357 C  C     . ARG A 1 2981 ? 175.456 132.742 190.793 1.00 72.18  ? 2981 ARG A C     1 
ATOM   13358 O  O     . ARG A 1 2981 ? 175.712 131.901 191.662 1.00 71.45  ? 2981 ARG A O     1 
ATOM   13359 C  CB    . ARG A 1 2981 ? 176.799 132.765 188.669 1.00 69.51  ? 2981 ARG A CB    1 
ATOM   13360 C  CG    . ARG A 1 2981 ? 177.758 131.607 188.478 1.00 74.28  ? 2981 ARG A CG    1 
ATOM   13361 C  CD    . ARG A 1 2981 ? 179.093 132.079 187.937 1.00 79.22  ? 2981 ARG A CD    1 
ATOM   13362 N  NE    . ARG A 1 2981 ? 179.012 132.452 186.530 1.00 81.44  ? 2981 ARG A NE    1 
ATOM   13363 C  CZ    . ARG A 1 2981 ? 179.350 131.655 185.526 1.00 86.10  ? 2981 ARG A CZ    1 
ATOM   13364 N  NH1   . ARG A 1 2981 ? 179.787 130.425 185.737 1.00 88.35  ? 2981 ARG A NH1   1 
ATOM   13365 N  NH2   . ARG A 1 2981 ? 179.247 132.104 184.279 1.00 92.24  ? 2981 ARG A NH2   1 
ATOM   13366 N  N     . ARG A 1 2982 ? 175.151 134.005 191.097 1.00 68.07  ? 2982 ARG A N     1 
ATOM   13367 C  CA    . ARG A 1 2982 ? 175.064 134.410 192.495 1.00 61.69  ? 2982 ARG A CA    1 
ATOM   13368 C  C     . ARG A 1 2982 ? 173.830 133.821 193.172 1.00 60.49  ? 2982 ARG A C     1 
ATOM   13369 O  O     . ARG A 1 2982 ? 173.892 133.411 194.335 1.00 67.00  ? 2982 ARG A O     1 
ATOM   13370 C  CB    . ARG A 1 2982 ? 175.067 135.933 192.606 1.00 60.56  ? 2982 ARG A CB    1 
ATOM   13371 C  CG    . ARG A 1 2982 ? 176.344 136.591 192.114 1.00 63.21  ? 2982 ARG A CG    1 
ATOM   13372 C  CD    . ARG A 1 2982 ? 176.172 138.094 191.970 1.00 61.28  ? 2982 ARG A CD    1 
ATOM   13373 N  NE    . ARG A 1 2982 ? 175.481 138.676 193.115 1.00 65.49  ? 2982 ARG A NE    1 
ATOM   13374 C  CZ    . ARG A 1 2982 ? 175.168 139.959 193.228 1.00 63.12  ? 2982 ARG A CZ    1 
ATOM   13375 N  NH1   . ARG A 1 2982 ? 175.466 140.830 192.278 1.00 63.67  ? 2982 ARG A NH1   1 
ATOM   13376 N  NH2   . ARG A 1 2982 ? 174.541 140.380 194.323 1.00 53.73  ? 2982 ARG A NH2   1 
ATOM   13377 N  N     . SER A 1 2983 ? 172.701 133.769 192.461 1.00 60.80  ? 2983 SER A N     1 
ATOM   13378 C  CA    . SER A 1 2983 ? 171.457 133.308 193.073 1.00 63.14  ? 2983 SER A CA    1 
ATOM   13379 C  C     . SER A 1 2983 ? 171.478 131.806 193.330 1.00 69.37  ? 2983 SER A C     1 
ATOM   13380 O  O     . SER A 1 2983 ? 171.107 131.347 194.416 1.00 69.50  ? 2983 SER A O     1 
ATOM   13381 C  CB    . SER A 1 2983 ? 170.268 133.678 192.187 1.00 59.13  ? 2983 SER A CB    1 
ATOM   13382 O  OG    . SER A 1 2983 ? 170.113 135.081 192.097 1.00 60.56  ? 2983 SER A OG    1 
ATOM   13383 N  N     . GLY A 1 2984 ? 171.902 131.023 192.342 1.00 67.69  ? 2984 GLY A N     1 
ATOM   13384 C  CA    . GLY A 1 2984 ? 171.853 129.579 192.449 1.00 61.41  ? 2984 GLY A CA    1 
ATOM   13385 C  C     . GLY A 1 2984 ? 173.082 128.954 193.074 1.00 70.77  ? 2984 GLY A C     1 
ATOM   13386 O  O     . GLY A 1 2984 ? 172.974 128.194 194.040 1.00 73.29  ? 2984 GLY A O     1 
ATOM   13387 N  N     . CYS A 1 2985 ? 174.260 129.264 192.529 1.00 69.97  ? 2985 CYS A N     1 
ATOM   13388 C  CA    . CYS A 1 2985 ? 175.483 128.639 193.021 1.00 75.93  ? 2985 CYS A CA    1 
ATOM   13389 C  C     . CYS A 1 2985 ? 175.877 129.177 194.391 1.00 78.67  ? 2985 CYS A C     1 
ATOM   13390 O  O     . CYS A 1 2985 ? 176.232 128.404 195.288 1.00 85.38  ? 2985 CYS A O     1 
ATOM   13391 C  CB    . CYS A 1 2985 ? 176.616 128.848 192.017 1.00 79.75  ? 2985 CYS A CB    1 
ATOM   13392 S  SG    . CYS A 1 2985 ? 176.417 127.933 190.474 1.00 94.55  ? 2985 CYS A SG    1 
ATOM   13393 N  N     . LYS A 1 2986 ? 175.816 130.493 194.576 1.00 73.18  ? 2986 LYS A N     1 
ATOM   13394 C  CA    . LYS A 1 2986 ? 176.268 131.125 195.808 1.00 67.53  ? 2986 LYS A CA    1 
ATOM   13395 C  C     . LYS A 1 2986 ? 175.183 131.214 196.872 1.00 63.48  ? 2986 LYS A C     1 
ATOM   13396 O  O     . LYS A 1 2986 ? 175.466 131.680 197.981 1.00 64.51  ? 2986 LYS A O     1 
ATOM   13397 C  CB    . LYS A 1 2986 ? 176.812 132.525 195.511 1.00 68.44  ? 2986 LYS A CB    1 
ATOM   13398 C  CG    . LYS A 1 2986 ? 178.074 132.528 194.668 1.00 67.81  ? 2986 LYS A CG    1 
ATOM   13399 C  CD    . LYS A 1 2986 ? 178.425 133.931 194.207 1.00 69.61  ? 2986 LYS A CD    1 
ATOM   13400 C  CE    . LYS A 1 2986 ? 179.683 133.931 193.356 1.00 73.30  ? 2986 LYS A CE    1 
ATOM   13401 N  NZ    . LYS A 1 2986 ? 179.374 133.788 191.907 1.00 75.59  ? 2986 LYS A NZ    1 
ATOM   13402 N  N     . ASN A 1 2987 ? 173.961 130.778 196.566 1.00 64.17  ? 2987 ASN A N     1 
ATOM   13403 C  CA    . ASN A 1 2987 ? 172.848 130.790 197.516 1.00 70.50  ? 2987 ASN A CA    1 
ATOM   13404 C  C     . ASN A 1 2987 ? 172.622 132.192 198.080 1.00 69.59  ? 2987 ASN A C     1 
ATOM   13405 O  O     . ASN A 1 2987 ? 172.463 132.392 199.285 1.00 69.66  ? 2987 ASN A O     1 
ATOM   13406 C  CB    . ASN A 1 2987 ? 173.078 129.773 198.635 1.00 75.77  ? 2987 ASN A CB    1 
ATOM   13407 C  CG    . ASN A 1 2987 ? 171.830 129.513 199.453 1.00 80.58  ? 2987 ASN A CG    1 
ATOM   13408 O  OD1   . ASN A 1 2987 ? 170.811 129.065 198.927 1.00 73.51  ? 2987 ASN A OD1   1 
ATOM   13409 N  ND2   . ASN A 1 2987 ? 171.904 129.793 200.748 1.00 88.19  ? 2987 ASN A ND2   1 
ATOM   13410 N  N     . GLU A 1 2988 ? 172.611 133.174 197.184 1.00 69.59  ? 2988 GLU A N     1 
ATOM   13411 C  CA    . GLU A 1 2988 ? 172.462 134.576 197.546 1.00 60.17  ? 2988 GLU A CA    1 
ATOM   13412 C  C     . GLU A 1 2988 ? 171.117 135.092 197.056 1.00 63.78  ? 2988 GLU A C     1 
ATOM   13413 O  O     . GLU A 1 2988 ? 170.805 134.988 195.865 1.00 64.58  ? 2988 GLU A O     1 
ATOM   13414 C  CB    . GLU A 1 2988 ? 173.596 135.411 196.949 1.00 54.98  ? 2988 GLU A CB    1 
ATOM   13415 C  CG    . GLU A 1 2988 ? 173.403 136.908 197.069 1.00 55.91  ? 2988 GLU A CG    1 
ATOM   13416 C  CD    . GLU A 1 2988 ? 174.598 137.684 196.558 1.00 70.38  ? 2988 GLU A CD    1 
ATOM   13417 O  OE1   . GLU A 1 2988 ? 175.698 137.098 196.482 1.00 71.32  ? 2988 GLU A OE1   1 
ATOM   13418 O  OE2   . GLU A 1 2988 ? 174.440 138.878 196.230 1.00 72.82  ? 2988 GLU A OE2   1 
ATOM   13419 N  N     . LYS A 1 2989 ? 170.326 135.646 197.971 1.00 61.80  ? 2989 LYS A N     1 
ATOM   13420 C  CA    . LYS A 1 2989 ? 169.054 136.245 197.594 1.00 49.41  ? 2989 LYS A CA    1 
ATOM   13421 C  C     . LYS A 1 2989 ? 169.296 137.573 196.890 1.00 46.45  ? 2989 LYS A C     1 
ATOM   13422 O  O     . LYS A 1 2989 ? 169.991 138.447 197.415 1.00 55.94  ? 2989 LYS A O     1 
ATOM   13423 C  CB    . LYS A 1 2989 ? 168.177 136.448 198.826 1.00 44.63  ? 2989 LYS A CB    1 
ATOM   13424 C  CG    . LYS A 1 2989 ? 167.324 135.247 199.186 1.00 58.50  ? 2989 LYS A CG    1 
ATOM   13425 C  CD    . LYS A 1 2989 ? 168.010 134.367 200.216 1.00 69.93  ? 2989 LYS A CD    1 
ATOM   13426 C  CE    . LYS A 1 2989 ? 167.268 133.053 200.400 1.00 77.11  ? 2989 LYS A CE    1 
ATOM   13427 N  NZ    . LYS A 1 2989 ? 168.100 132.032 201.093 1.00 75.82  ? 2989 LYS A NZ    1 
ATOM   13428 N  N     . ILE A 1 2990 ? 168.722 137.726 195.700 1.00 40.09  ? 2990 ILE A N     1 
ATOM   13429 C  CA    . ILE A 1 2990 ? 168.922 138.912 194.877 1.00 42.20  ? 2990 ILE A CA    1 
ATOM   13430 C  C     . ILE A 1 2990 ? 167.566 139.474 194.481 1.00 44.46  ? 2990 ILE A C     1 
ATOM   13431 O  O     . ILE A 1 2990 ? 166.678 138.726 194.060 1.00 49.21  ? 2990 ILE A O     1 
ATOM   13432 C  CB    . ILE A 1 2990 ? 169.766 138.608 193.625 1.00 41.50  ? 2990 ILE A CB    1 
ATOM   13433 C  CG1   . ILE A 1 2990 ? 171.168 138.159 194.026 1.00 48.89  ? 2990 ILE A CG1   1 
ATOM   13434 C  CG2   . ILE A 1 2990 ? 169.843 139.818 192.713 1.00 47.82  ? 2990 ILE A CG2   1 
ATOM   13435 C  CD1   . ILE A 1 2990 ? 171.963 137.608 192.882 1.00 59.30  ? 2990 ILE A CD1   1 
ATOM   13436 N  N     . ALA A 1 2991 ? 167.407 140.786 194.628 1.00 40.55  ? 2991 ALA A N     1 
ATOM   13437 C  CA    . ALA A 1 2991 ? 166.242 141.508 194.128 1.00 34.13  ? 2991 ALA A CA    1 
ATOM   13438 C  C     . ALA A 1 2991 ? 166.645 142.139 192.801 1.00 39.76  ? 2991 ALA A C     1 
ATOM   13439 O  O     . ALA A 1 2991 ? 167.315 143.173 192.770 1.00 49.62  ? 2991 ALA A O     1 
ATOM   13440 C  CB    . ALA A 1 2991 ? 165.769 142.551 195.132 1.00 38.99  ? 2991 ALA A CB    1 
ATOM   13441 N  N     . PHE A 1 2992 ? 166.237 141.507 191.702 1.00 39.75  ? 2992 PHE A N     1 
ATOM   13442 C  CA    . PHE A 1 2992 ? 166.622 141.932 190.357 1.00 40.14  ? 2992 PHE A CA    1 
ATOM   13443 C  C     . PHE A 1 2992 ? 165.657 143.022 189.899 1.00 44.99  ? 2992 PHE A C     1 
ATOM   13444 O  O     . PHE A 1 2992 ? 164.611 142.769 189.298 1.00 50.95  ? 2992 PHE A O     1 
ATOM   13445 C  CB    . PHE A 1 2992 ? 166.627 140.737 189.414 1.00 44.60  ? 2992 PHE A CB    1 
ATOM   13446 C  CG    . PHE A 1 2992 ? 167.247 141.014 188.080 1.00 50.36  ? 2992 PHE A CG    1 
ATOM   13447 C  CD1   . PHE A 1 2992 ? 168.563 141.415 187.981 1.00 55.67  ? 2992 PHE A CD1   1 
ATOM   13448 C  CD2   . PHE A 1 2992 ? 166.515 140.850 186.922 1.00 56.28  ? 2992 PHE A CD2   1 
ATOM   13449 C  CE1   . PHE A 1 2992 ? 169.130 141.660 186.750 1.00 60.01  ? 2992 PHE A CE1   1 
ATOM   13450 C  CE2   . PHE A 1 2992 ? 167.080 141.093 185.692 1.00 60.30  ? 2992 PHE A CE2   1 
ATOM   13451 C  CZ    . PHE A 1 2992 ? 168.387 141.497 185.607 1.00 59.59  ? 2992 PHE A CZ    1 
ATOM   13452 N  N     . ILE A 1 2993 ? 166.024 144.265 190.192 1.00 47.33  ? 2993 ILE A N     1 
ATOM   13453 C  CA    . ILE A 1 2993 ? 165.137 145.399 189.957 1.00 49.25  ? 2993 ILE A CA    1 
ATOM   13454 C  C     . ILE A 1 2993 ? 165.383 145.959 188.563 1.00 52.65  ? 2993 ILE A C     1 
ATOM   13455 O  O     . ILE A 1 2993 ? 166.526 146.228 188.179 1.00 58.55  ? 2993 ILE A O     1 
ATOM   13456 C  CB    . ILE A 1 2993 ? 165.335 146.475 191.036 1.00 48.49  ? 2993 ILE A CB    1 
ATOM   13457 C  CG1   . ILE A 1 2993 ? 164.996 145.904 192.412 1.00 40.83  ? 2993 ILE A CG1   1 
ATOM   13458 C  CG2   . ILE A 1 2993 ? 164.471 147.686 190.742 1.00 50.42  ? 2993 ILE A CG2   1 
ATOM   13459 C  CD1   . ILE A 1 2993 ? 165.020 146.921 193.517 1.00 39.47  ? 2993 ILE A CD1   1 
ATOM   13460 N  N     . MET A 1 2994 ? 164.304 146.135 187.802 1.00 51.77  ? 2994 MET A N     1 
ATOM   13461 C  CA    . MET A 1 2994 ? 164.358 146.675 186.451 1.00 64.19  ? 2994 MET A CA    1 
ATOM   13462 C  C     . MET A 1 2994 ? 163.342 147.800 186.328 1.00 73.62  ? 2994 MET A C     1 
ATOM   13463 O  O     . MET A 1 2994 ? 162.223 147.687 186.837 1.00 69.53  ? 2994 MET A O     1 
ATOM   13464 C  CB    . MET A 1 2994 ? 164.075 145.586 185.409 1.00 65.24  ? 2994 MET A CB    1 
ATOM   13465 C  CG    . MET A 1 2994 ? 164.913 144.331 185.582 1.00 66.04  ? 2994 MET A CG    1 
ATOM   13466 S  SD    . MET A 1 2994 ? 164.874 143.238 184.150 1.00 75.49  ? 2994 MET A SD    1 
ATOM   13467 C  CE    . MET A 1 2994 ? 164.862 144.419 182.806 1.00 79.51  ? 2994 MET A CE    1 
ATOM   13468 N  N     . ASP A 1 2995 ? 163.730 148.879 185.654 1.00 81.20  ? 2995 ASP A N     1 
ATOM   13469 C  CA    . ASP A 1 2995 ? 162.876 150.040 185.461 1.00 80.78  ? 2995 ASP A CA    1 
ATOM   13470 C  C     . ASP A 1 2995 ? 162.728 150.331 183.974 1.00 98.09  ? 2995 ASP A C     1 
ATOM   13471 O  O     . ASP A 1 2995 ? 163.478 149.814 183.142 1.00 105.12 ? 2995 ASP A O     1 
ATOM   13472 C  CB    . ASP A 1 2995 ? 163.439 151.270 186.182 1.00 80.87  ? 2995 ASP A CB    1 
ATOM   13473 C  CG    . ASP A 1 2995 ? 163.839 150.975 187.614 1.00 84.36  ? 2995 ASP A CG    1 
ATOM   13474 O  OD1   . ASP A 1 2995 ? 162.940 150.734 188.446 1.00 77.91  ? 2995 ASP A OD1   1 
ATOM   13475 O  OD2   . ASP A 1 2995 ? 165.052 150.988 187.909 1.00 89.18  ? 2995 ASP A OD2   1 
ATOM   13476 N  N     . GLU A 1 2996 ? 161.764 151.199 183.647 1.00 97.98  ? 2996 GLU A N     1 
ATOM   13477 C  CA    . GLU A 1 2996 ? 161.461 151.488 182.249 1.00 101.09 ? 2996 GLU A CA    1 
ATOM   13478 C  C     . GLU A 1 2996 ? 162.646 152.081 181.501 1.00 111.24 ? 2996 GLU A C     1 
ATOM   13479 O  O     . GLU A 1 2996 ? 162.639 152.087 180.265 1.00 118.57 ? 2996 GLU A O     1 
ATOM   13480 C  CB    . GLU A 1 2996 ? 160.271 152.442 182.137 1.00 95.10  ? 2996 GLU A CB    1 
ATOM   13481 C  CG    . GLU A 1 2996 ? 158.935 151.854 182.545 1.00 83.35  ? 2996 GLU A CG    1 
ATOM   13482 C  CD    . GLU A 1 2996 ? 157.804 152.852 182.396 1.00 81.89  ? 2996 GLU A CD    1 
ATOM   13483 O  OE1   . GLU A 1 2996 ? 158.089 154.034 182.114 1.00 80.73  ? 2996 GLU A OE1   1 
ATOM   13484 O  OE2   . GLU A 1 2996 ? 156.629 152.456 182.544 1.00 77.31  ? 2996 GLU A OE2   1 
ATOM   13485 N  N     . SER A 1 2997 ? 163.653 152.592 182.214 1.00 109.04 ? 2997 SER A N     1 
ATOM   13486 C  CA    . SER A 1 2997 ? 164.862 153.064 181.547 1.00 113.05 ? 2997 SER A CA    1 
ATOM   13487 C  C     . SER A 1 2997 ? 165.530 151.950 180.750 1.00 119.33 ? 2997 SER A C     1 
ATOM   13488 O  O     . SER A 1 2997 ? 166.248 152.225 179.782 1.00 120.39 ? 2997 SER A O     1 
ATOM   13489 C  CB    . SER A 1 2997 ? 165.834 153.645 182.575 1.00 109.11 ? 2997 SER A CB    1 
ATOM   13490 O  OG    . SER A 1 2997 ? 166.958 154.230 181.941 1.00 102.90 ? 2997 SER A OG    1 
ATOM   13491 N  N     . ASN A 1 2998 ? 165.308 150.692 181.140 1.00 119.05 ? 2998 ASN A N     1 
ATOM   13492 C  CA    . ASN A 1 2998 ? 165.801 149.547 180.389 1.00 118.82 ? 2998 ASN A CA    1 
ATOM   13493 C  C     . ASN A 1 2998 ? 164.735 148.505 180.075 1.00 112.38 ? 2998 ASN A C     1 
ATOM   13494 O  O     . ASN A 1 2998 ? 165.001 147.607 179.268 1.00 110.28 ? 2998 ASN A O     1 
ATOM   13495 C  CB    . ASN A 1 2998 ? 166.960 148.871 181.139 1.00 119.41 ? 2998 ASN A CB    1 
ATOM   13496 C  CG    . ASN A 1 2998 ? 166.577 148.437 182.539 1.00 115.54 ? 2998 ASN A CG    1 
ATOM   13497 O  OD1   . ASN A 1 2998 ? 166.212 149.259 183.379 1.00 109.14 ? 2998 ASN A OD1   1 
ATOM   13498 N  ND2   . ASN A 1 2998 ? 166.672 147.141 182.801 1.00 111.14 ? 2998 ASN A ND2   1 
ATOM   13499 N  N     . VAL A 1 2999 ? 163.548 148.589 180.681 1.00 112.36 ? 2999 VAL A N     1 
ATOM   13500 C  CA    . VAL A 1 2999 ? 162.457 147.683 180.326 1.00 117.13 ? 2999 VAL A CA    1 
ATOM   13501 C  C     . VAL A 1 2999 ? 161.936 147.978 178.922 1.00 120.46 ? 2999 VAL A C     1 
ATOM   13502 O  O     . VAL A 1 2999 ? 161.411 147.083 178.248 1.00 119.87 ? 2999 VAL A O     1 
ATOM   13503 C  CB    . VAL A 1 2999 ? 161.341 147.762 181.390 1.00 114.16 ? 2999 VAL A CB    1 
ATOM   13504 C  CG1   . VAL A 1 2999 ? 160.133 146.941 180.988 1.00 109.80 ? 2999 VAL A CG1   1 
ATOM   13505 C  CG2   . VAL A 1 2999 ? 161.855 147.245 182.719 1.00 100.85 ? 2999 VAL A CG2   1 
ATOM   13506 N  N     . LEU A 1 3000 ? 162.098 149.215 178.442 1.00 121.81 ? 3000 LEU A N     1 
ATOM   13507 C  CA    . LEU A 1 3000 ? 161.534 149.598 177.150 1.00 124.07 ? 3000 LEU A CA    1 
ATOM   13508 C  C     . LEU A 1 3000 ? 162.059 148.746 175.999 1.00 126.19 ? 3000 LEU A C     1 
ATOM   13509 O  O     . LEU A 1 3000 ? 161.394 148.651 174.962 1.00 123.46 ? 3000 LEU A O     1 
ATOM   13510 C  CB    . LEU A 1 3000 ? 161.803 151.084 176.883 1.00 122.40 ? 3000 LEU A CB    1 
ATOM   13511 C  CG    . LEU A 1 3000 ? 163.240 151.615 176.827 1.00 123.31 ? 3000 LEU A CG    1 
ATOM   13512 C  CD1   . LEU A 1 3000 ? 163.865 151.451 175.448 1.00 123.39 ? 3000 LEU A CD1   1 
ATOM   13513 C  CD2   . LEU A 1 3000 ? 163.274 153.075 177.252 1.00 120.35 ? 3000 LEU A CD2   1 
ATOM   13514 N  N     . ASP A 1 3001 ? 163.227 148.126 176.152 1.00 127.90 ? 3001 ASP A N     1 
ATOM   13515 C  CA    . ASP A 1 3001 ? 163.753 147.205 175.146 1.00 125.15 ? 3001 ASP A CA    1 
ATOM   13516 C  C     . ASP A 1 3001 ? 163.129 145.834 175.376 1.00 117.03 ? 3001 ASP A C     1 
ATOM   13517 O  O     . ASP A 1 3001 ? 163.544 145.090 176.267 1.00 114.24 ? 3001 ASP A O     1 
ATOM   13518 C  CB    . ASP A 1 3001 ? 165.274 147.141 175.215 1.00 125.52 ? 3001 ASP A CB    1 
ATOM   13519 C  CG    . ASP A 1 3001 ? 165.939 148.257 174.439 1.00 128.48 ? 3001 ASP A CG    1 
ATOM   13520 O  OD1   . ASP A 1 3001 ? 165.220 149.027 173.771 1.00 127.66 ? 3001 ASP A OD1   1 
ATOM   13521 O  OD2   . ASP A 1 3001 ? 167.181 148.364 174.498 1.00 132.88 ? 3001 ASP A OD2   1 
ATOM   13522 N  N     . SER A 1 3002 ? 162.125 145.495 174.564 1.00 113.48 ? 3002 SER A N     1 
ATOM   13523 C  CA    . SER A 1 3002 ? 161.423 144.226 174.718 1.00 110.48 ? 3002 SER A CA    1 
ATOM   13524 C  C     . SER A 1 3002 ? 162.267 143.025 174.314 1.00 102.34 ? 3002 SER A C     1 
ATOM   13525 O  O     . SER A 1 3002 ? 161.918 141.897 174.679 1.00 96.91  ? 3002 SER A O     1 
ATOM   13526 C  CB    . SER A 1 3002 ? 160.127 144.242 173.907 1.00 110.71 ? 3002 SER A CB    1 
ATOM   13527 O  OG    . SER A 1 3002 ? 159.266 145.279 174.345 1.00 113.49 ? 3002 SER A OG    1 
ATOM   13528 N  N     . GLY A 1 3003 ? 163.355 143.234 173.570 1.00 101.38 ? 3003 GLY A N     1 
ATOM   13529 C  CA    . GLY A 1 3003 ? 164.225 142.125 173.223 1.00 92.91  ? 3003 GLY A CA    1 
ATOM   13530 C  C     . GLY A 1 3003 ? 164.839 141.459 174.437 1.00 95.54  ? 3003 GLY A C     1 
ATOM   13531 O  O     . GLY A 1 3003 ? 165.018 140.238 174.456 1.00 92.35  ? 3003 GLY A O     1 
ATOM   13532 N  N     . PHE A 1 3004 ? 165.178 142.245 175.460 1.00 99.32  ? 3004 PHE A N     1 
ATOM   13533 C  CA    . PHE A 1 3004 ? 165.636 141.667 176.717 1.00 99.48  ? 3004 PHE A CA    1 
ATOM   13534 C  C     . PHE A 1 3004 ? 164.481 141.133 177.554 1.00 93.89  ? 3004 PHE A C     1 
ATOM   13535 O  O     . PHE A 1 3004 ? 164.662 140.168 178.299 1.00 87.89  ? 3004 PHE A O     1 
ATOM   13536 C  CB    . PHE A 1 3004 ? 166.436 142.698 177.516 1.00 100.82 ? 3004 PHE A CB    1 
ATOM   13537 C  CG    . PHE A 1 3004 ? 167.444 143.454 176.697 1.00 110.86 ? 3004 PHE A CG    1 
ATOM   13538 C  CD1   . PHE A 1 3004 ? 168.309 142.783 175.848 1.00 110.19 ? 3004 PHE A CD1   1 
ATOM   13539 C  CD2   . PHE A 1 3004 ? 167.538 144.832 176.788 1.00 118.70 ? 3004 PHE A CD2   1 
ATOM   13540 C  CE1   . PHE A 1 3004 ? 169.239 143.473 175.096 1.00 113.86 ? 3004 PHE A CE1   1 
ATOM   13541 C  CE2   . PHE A 1 3004 ? 168.468 145.528 176.039 1.00 121.96 ? 3004 PHE A CE2   1 
ATOM   13542 C  CZ    . PHE A 1 3004 ? 169.319 144.847 175.192 1.00 121.00 ? 3004 PHE A CZ    1 
ATOM   13543 N  N     . LEU A 1 3005 ? 163.296 141.741 177.448 1.00 92.95  ? 3005 LEU A N     1 
ATOM   13544 C  CA    . LEU A 1 3005 ? 162.149 141.276 178.224 1.00 88.30  ? 3005 LEU A CA    1 
ATOM   13545 C  C     . LEU A 1 3005 ? 161.708 139.884 177.794 1.00 80.99  ? 3005 LEU A C     1 
ATOM   13546 O  O     . LEU A 1 3005 ? 161.344 139.051 178.633 1.00 79.59  ? 3005 LEU A O     1 
ATOM   13547 C  CB    . LEU A 1 3005 ? 160.987 142.255 178.085 1.00 95.16  ? 3005 LEU A CB    1 
ATOM   13548 C  CG    . LEU A 1 3005 ? 160.857 143.410 179.077 1.00 100.91 ? 3005 LEU A CG    1 
ATOM   13549 C  CD1   . LEU A 1 3005 ? 162.188 144.099 179.333 1.00 99.43  ? 3005 LEU A CD1   1 
ATOM   13550 C  CD2   . LEU A 1 3005 ? 159.812 144.388 178.569 1.00 102.65 ? 3005 LEU A CD2   1 
ATOM   13551 N  N     . GLU A 1 3006 ? 161.706 139.622 176.488 1.00 80.58  ? 3006 GLU A N     1 
ATOM   13552 C  CA    . GLU A 1 3006 ? 161.267 138.320 176.002 1.00 79.85  ? 3006 GLU A CA    1 
ATOM   13553 C  C     . GLU A 1 3006 ? 162.261 137.221 176.356 1.00 79.85  ? 3006 GLU A C     1 
ATOM   13554 O  O     . GLU A 1 3006 ? 161.891 136.042 176.393 1.00 76.47  ? 3006 GLU A O     1 
ATOM   13555 C  CB    . GLU A 1 3006 ? 161.028 138.391 174.497 1.00 79.39  ? 3006 GLU A CB    1 
ATOM   13556 C  CG    . GLU A 1 3006 ? 162.265 138.720 173.698 1.00 81.94  ? 3006 GLU A CG    1 
ATOM   13557 C  CD    . GLU A 1 3006 ? 161.958 138.960 172.239 1.00 74.93  ? 3006 GLU A CD    1 
ATOM   13558 O  OE1   . GLU A 1 3006 ? 160.770 138.897 171.860 1.00 68.61  ? 3006 GLU A OE1   1 
ATOM   13559 O  OE2   . GLU A 1 3006 ? 162.905 139.218 171.473 1.00 70.63  ? 3006 GLU A OE2   1 
ATOM   13560 N  N     . ARG A 1 3007 ? 163.520 137.581 176.614 1.00 81.26  ? 3007 ARG A N     1 
ATOM   13561 C  CA    . ARG A 1 3007 ? 164.470 136.608 177.144 1.00 82.92  ? 3007 ARG A CA    1 
ATOM   13562 C  C     . ARG A 1 3007 ? 164.350 136.497 178.658 1.00 77.16  ? 3007 ARG A C     1 
ATOM   13563 O  O     . ARG A 1 3007 ? 164.616 135.433 179.229 1.00 75.71  ? 3007 ARG A O     1 
ATOM   13564 C  CB    . ARG A 1 3007 ? 165.892 136.998 176.738 1.00 85.91  ? 3007 ARG A CB    1 
ATOM   13565 C  CG    . ARG A 1 3007 ? 166.963 136.005 177.149 1.00 88.48  ? 3007 ARG A CG    1 
ATOM   13566 C  CD    . ARG A 1 3007 ? 168.322 136.427 176.620 1.00 85.73  ? 3007 ARG A CD    1 
ATOM   13567 N  NE    . ARG A 1 3007 ? 169.383 135.531 177.064 1.00 92.46  ? 3007 ARG A NE    1 
ATOM   13568 C  CZ    . ARG A 1 3007 ? 169.730 134.417 176.435 1.00 95.15  ? 3007 ARG A CZ    1 
ATOM   13569 N  NH1   . ARG A 1 3007 ? 169.118 134.030 175.328 1.00 93.46  ? 3007 ARG A NH1   1 
ATOM   13570 N  NH2   . ARG A 1 3007 ? 170.716 133.673 176.927 1.00 95.59  ? 3007 ARG A NH2   1 
ATOM   13571 N  N     . MET A 1 3008 ? 163.951 137.587 179.316 1.00 74.44  ? 3008 MET A N     1 
ATOM   13572 C  CA    . MET A 1 3008 ? 163.680 137.567 180.748 1.00 69.72  ? 3008 MET A CA    1 
ATOM   13573 C  C     . MET A 1 3008 ? 162.495 136.673 181.081 1.00 66.80  ? 3008 MET A C     1 
ATOM   13574 O  O     . MET A 1 3008 ? 162.440 136.097 182.174 1.00 67.78  ? 3008 MET A O     1 
ATOM   13575 C  CB    . MET A 1 3008 ? 163.415 138.994 181.231 1.00 72.06  ? 3008 MET A CB    1 
ATOM   13576 C  CG    . MET A 1 3008 ? 163.384 139.172 182.730 1.00 60.57  ? 3008 MET A CG    1 
ATOM   13577 S  SD    . MET A 1 3008 ? 165.024 139.485 183.393 1.00 69.76  ? 3008 MET A SD    1 
ATOM   13578 C  CE    . MET A 1 3008 ? 165.043 138.332 184.755 1.00 62.01  ? 3008 MET A CE    1 
ATOM   13579 N  N     . ASN A 1 3009 ? 161.535 136.570 180.159 1.00 65.81  ? 3009 ASN A N     1 
ATOM   13580 C  CA    . ASN A 1 3009 ? 160.328 135.790 180.418 1.00 57.91  ? 3009 ASN A CA    1 
ATOM   13581 C  C     . ASN A 1 3009 ? 160.640 134.323 180.683 1.00 57.02  ? 3009 ASN A C     1 
ATOM   13582 O  O     . ASN A 1 3009 ? 159.933 133.673 181.460 1.00 60.97  ? 3009 ASN A O     1 
ATOM   13583 C  CB    . ASN A 1 3009 ? 159.355 135.915 179.246 1.00 57.05  ? 3009 ASN A CB    1 
ATOM   13584 C  CG    . ASN A 1 3009 ? 158.754 137.300 179.133 1.00 65.56  ? 3009 ASN A CG    1 
ATOM   13585 O  OD1   . ASN A 1 3009 ? 158.752 137.903 178.062 1.00 72.53  ? 3009 ASN A OD1   1 
ATOM   13586 N  ND2   . ASN A 1 3009 ? 158.250 137.816 180.246 1.00 61.73  ? 3009 ASN A ND2   1 
ATOM   13587 N  N     . THR A 1 3010 ? 161.683 133.782 180.052 1.00 57.40  ? 3010 THR A N     1 
ATOM   13588 C  CA    . THR A 1 3010 ? 162.053 132.392 180.305 1.00 59.32  ? 3010 THR A CA    1 
ATOM   13589 C  C     . THR A 1 3010 ? 162.455 132.187 181.760 1.00 58.43  ? 3010 THR A C     1 
ATOM   13590 O  O     . THR A 1 3010 ? 162.039 131.216 182.402 1.00 60.44  ? 3010 THR A O     1 
ATOM   13591 C  CB    . THR A 1 3010 ? 163.190 131.971 179.379 1.00 67.76  ? 3010 THR A CB    1 
ATOM   13592 O  OG1   . THR A 1 3010 ? 162.803 132.178 178.015 1.00 75.38  ? 3010 THR A OG1   1 
ATOM   13593 C  CG2   . THR A 1 3010 ? 163.516 130.509 179.596 1.00 67.05  ? 3010 THR A CG2   1 
ATOM   13594 N  N     . LEU A 1 3011 ? 163.272 133.096 182.293 1.00 60.78  ? 3011 LEU A N     1 
ATOM   13595 C  CA    . LEU A 1 3011 ? 163.668 133.013 183.695 1.00 60.13  ? 3011 LEU A CA    1 
ATOM   13596 C  C     . LEU A 1 3011 ? 162.479 133.268 184.612 1.00 59.21  ? 3011 LEU A C     1 
ATOM   13597 O  O     . LEU A 1 3011 ? 162.361 132.660 185.681 1.00 57.93  ? 3011 LEU A O     1 
ATOM   13598 C  CB    . LEU A 1 3011 ? 164.793 134.007 183.975 1.00 59.47  ? 3011 LEU A CB    1 
ATOM   13599 C  CG    . LEU A 1 3011 ? 165.381 134.015 185.383 1.00 58.76  ? 3011 LEU A CG    1 
ATOM   13600 C  CD1   . LEU A 1 3011 ? 166.019 132.678 185.696 1.00 65.47  ? 3011 LEU A CD1   1 
ATOM   13601 C  CD2   . LEU A 1 3011 ? 166.397 135.127 185.502 1.00 65.53  ? 3011 LEU A CD2   1 
ATOM   13602 N  N     . LEU A 1 3012 ? 161.591 134.179 184.209 1.00 57.72  ? 3012 LEU A N     1 
ATOM   13603 C  CA    . LEU A 1 3012 ? 160.403 134.455 185.009 1.00 52.08  ? 3012 LEU A CA    1 
ATOM   13604 C  C     . LEU A 1 3012 ? 159.501 133.233 185.116 1.00 54.84  ? 3012 LEU A C     1 
ATOM   13605 O  O     . LEU A 1 3012 ? 158.916 132.984 186.175 1.00 58.07  ? 3012 LEU A O     1 
ATOM   13606 C  CB    . LEU A 1 3012 ? 159.628 135.629 184.413 1.00 45.91  ? 3012 LEU A CB    1 
ATOM   13607 C  CG    . LEU A 1 3012 ? 160.304 136.999 184.417 1.00 42.53  ? 3012 LEU A CG    1 
ATOM   13608 C  CD1   . LEU A 1 3012 ? 159.348 138.058 183.904 1.00 47.30  ? 3012 LEU A CD1   1 
ATOM   13609 C  CD2   . LEU A 1 3012 ? 160.796 137.349 185.805 1.00 40.95  ? 3012 LEU A CD2   1 
ATOM   13610 N  N     . ALA A 1 3013 ? 159.375 132.463 184.036 1.00 51.95  ? 3013 ALA A N     1 
ATOM   13611 C  CA    . ALA A 1 3013 ? 158.463 131.324 184.008 1.00 49.84  ? 3013 ALA A CA    1 
ATOM   13612 C  C     . ALA A 1 3013 ? 159.097 130.061 184.583 1.00 60.76  ? 3013 ALA A C     1 
ATOM   13613 O  O     . ALA A 1 3013 ? 158.596 129.496 185.560 1.00 63.01  ? 3013 ALA A O     1 
ATOM   13614 C  CB    . ALA A 1 3013 ? 157.992 131.069 182.573 1.00 46.42  ? 3013 ALA A CB    1 
ATOM   13615 N  N     . ASN A 1 3014 ? 160.199 129.609 183.987 1.00 63.09  ? 3014 ASN A N     1 
ATOM   13616 C  CA    . ASN A 1 3014 ? 160.788 128.328 184.347 1.00 61.65  ? 3014 ASN A CA    1 
ATOM   13617 C  C     . ASN A 1 3014 ? 161.785 128.440 185.493 1.00 65.32  ? 3014 ASN A C     1 
ATOM   13618 O  O     . ASN A 1 3014 ? 161.944 127.480 186.254 1.00 73.79  ? 3014 ASN A O     1 
ATOM   13619 C  CB    . ASN A 1 3014 ? 161.481 127.721 183.116 1.00 67.68  ? 3014 ASN A CB    1 
ATOM   13620 C  CG    . ASN A 1 3014 ? 161.928 126.282 183.326 1.00 77.62  ? 3014 ASN A CG    1 
ATOM   13621 O  OD1   . ASN A 1 3014 ? 161.752 125.702 184.394 1.00 80.60  ? 3014 ASN A OD1   1 
ATOM   13622 N  ND2   . ASN A 1 3014 ? 162.527 125.703 182.292 1.00 74.90  ? 3014 ASN A ND2   1 
ATOM   13623 N  N     . GLY A 1 3015 ? 162.420 129.593 185.665 1.00 61.30  ? 3015 GLY A N     1 
ATOM   13624 C  CA    . GLY A 1 3015 ? 163.478 129.735 186.639 1.00 60.53  ? 3015 GLY A CA    1 
ATOM   13625 C  C     . GLY A 1 3015 ? 164.861 129.433 186.115 1.00 64.30  ? 3015 GLY A C     1 
ATOM   13626 O  O     . GLY A 1 3015 ? 165.789 129.274 186.915 1.00 65.82  ? 3015 GLY A O     1 
ATOM   13627 N  N     . GLU A 1 3016 ? 165.025 129.343 184.800 1.00 67.97  ? 3016 GLU A N     1 
ATOM   13628 C  CA    . GLU A 1 3016 ? 166.318 129.082 184.190 1.00 71.95  ? 3016 GLU A CA    1 
ATOM   13629 C  C     . GLU A 1 3016 ? 166.298 129.655 182.784 1.00 71.50  ? 3016 GLU A C     1 
ATOM   13630 O  O     . GLU A 1 3016 ? 165.235 129.895 182.209 1.00 72.41  ? 3016 GLU A O     1 
ATOM   13631 C  CB    . GLU A 1 3016 ? 166.633 127.584 184.157 1.00 76.81  ? 3016 GLU A CB    1 
ATOM   13632 C  CG    . GLU A 1 3016 ? 165.986 126.848 182.995 1.00 78.24  ? 3016 GLU A CG    1 
ATOM   13633 C  CD    . GLU A 1 3016 ? 165.971 125.346 183.186 1.00 83.86  ? 3016 GLU A CD    1 
ATOM   13634 O  OE1   . GLU A 1 3016 ? 165.806 124.893 184.338 1.00 74.04  ? 3016 GLU A OE1   1 
ATOM   13635 O  OE2   . GLU A 1 3016 ? 166.125 124.617 182.184 1.00 96.05  ? 3016 GLU A OE2   1 
ATOM   13636 N  N     . VAL A 1 3017 ? 167.489 129.877 182.240 1.00 73.57  ? 3017 VAL A N     1 
ATOM   13637 C  CA    . VAL A 1 3017 ? 167.620 130.329 180.858 1.00 74.22  ? 3017 VAL A CA    1 
ATOM   13638 C  C     . VAL A 1 3017 ? 168.446 129.293 180.106 1.00 83.85  ? 3017 VAL A C     1 
ATOM   13639 O  O     . VAL A 1 3017 ? 169.683 129.353 180.136 1.00 87.05  ? 3017 VAL A O     1 
ATOM   13640 C  CB    . VAL A 1 3017 ? 168.256 131.725 180.778 1.00 70.00  ? 3017 VAL A CB    1 
ATOM   13641 C  CG1   . VAL A 1 3017 ? 168.357 132.180 179.330 1.00 73.91  ? 3017 VAL A CG1   1 
ATOM   13642 C  CG2   . VAL A 1 3017 ? 167.454 132.721 181.596 1.00 66.11  ? 3017 VAL A CG2   1 
ATOM   13643 N  N     . PRO A 1 3018 ? 167.818 128.317 179.453 1.00 85.93  ? 3018 PRO A N     1 
ATOM   13644 C  CA    . PRO A 1 3018 ? 168.592 127.338 178.681 1.00 88.30  ? 3018 PRO A CA    1 
ATOM   13645 C  C     . PRO A 1 3018 ? 169.368 128.016 177.563 1.00 86.41  ? 3018 PRO A C     1 
ATOM   13646 O  O     . PRO A 1 3018 ? 168.876 128.936 176.907 1.00 84.20  ? 3018 PRO A O     1 
ATOM   13647 C  CB    . PRO A 1 3018 ? 167.521 126.386 178.136 1.00 88.24  ? 3018 PRO A CB    1 
ATOM   13648 C  CG    . PRO A 1 3018 ? 166.257 127.171 178.176 1.00 79.09  ? 3018 PRO A CG    1 
ATOM   13649 C  CD    . PRO A 1 3018 ? 166.371 128.064 179.372 1.00 80.52  ? 3018 PRO A CD    1 
ATOM   13650 N  N     . GLY A 1 3019 ? 170.595 127.548 177.350 1.00 87.14  ? 3019 GLY A N     1 
ATOM   13651 C  CA    . GLY A 1 3019 ? 171.483 128.164 176.392 1.00 91.07  ? 3019 GLY A CA    1 
ATOM   13652 C  C     . GLY A 1 3019 ? 172.280 129.335 176.919 1.00 93.84  ? 3019 GLY A C     1 
ATOM   13653 O  O     . GLY A 1 3019 ? 173.125 129.866 176.188 1.00 100.25 ? 3019 GLY A O     1 
ATOM   13654 N  N     . LEU A 1 3020 ? 172.038 129.761 178.160 1.00 88.97  ? 3020 LEU A N     1 
ATOM   13655 C  CA    . LEU A 1 3020 ? 172.820 130.845 178.742 1.00 88.14  ? 3020 LEU A CA    1 
ATOM   13656 C  C     . LEU A 1 3020 ? 174.219 130.379 179.126 1.00 94.43  ? 3020 LEU A C     1 
ATOM   13657 O  O     . LEU A 1 3020 ? 175.201 131.090 178.888 1.00 97.92  ? 3020 LEU A O     1 
ATOM   13658 C  CB    . LEU A 1 3020 ? 172.094 131.416 179.959 1.00 80.71  ? 3020 LEU A CB    1 
ATOM   13659 C  CG    . LEU A 1 3020 ? 172.666 132.682 180.595 1.00 78.23  ? 3020 LEU A CG    1 
ATOM   13660 C  CD1   . LEU A 1 3020 ? 172.559 133.859 179.646 1.00 79.50  ? 3020 LEU A CD1   1 
ATOM   13661 C  CD2   . LEU A 1 3020 ? 171.960 132.980 181.905 1.00 75.20  ? 3020 LEU A CD2   1 
ATOM   13662 N  N     . PHE A 1 3021 ? 174.326 129.192 179.716 1.00 88.97  ? 3021 PHE A N     1 
ATOM   13663 C  CA    . PHE A 1 3021 ? 175.603 128.627 180.138 1.00 91.80  ? 3021 PHE A CA    1 
ATOM   13664 C  C     . PHE A 1 3021 ? 175.972 127.505 179.175 1.00 97.62  ? 3021 PHE A C     1 
ATOM   13665 O  O     . PHE A 1 3021 ? 175.324 126.453 179.160 1.00 97.31  ? 3021 PHE A O     1 
ATOM   13666 C  CB    . PHE A 1 3021 ? 175.516 128.116 181.573 1.00 93.54  ? 3021 PHE A CB    1 
ATOM   13667 C  CG    . PHE A 1 3021 ? 175.227 129.190 182.582 1.00 90.84  ? 3021 PHE A CG    1 
ATOM   13668 C  CD1   . PHE A 1 3021 ? 176.193 130.123 182.916 1.00 88.76  ? 3021 PHE A CD1   1 
ATOM   13669 C  CD2   . PHE A 1 3021 ? 173.985 129.274 183.187 1.00 85.35  ? 3021 PHE A CD2   1 
ATOM   13670 C  CE1   . PHE A 1 3021 ? 175.928 131.112 183.841 1.00 83.99  ? 3021 PHE A CE1   1 
ATOM   13671 C  CE2   . PHE A 1 3021 ? 173.715 130.260 184.112 1.00 78.56  ? 3021 PHE A CE2   1 
ATOM   13672 C  CZ    . PHE A 1 3021 ? 174.688 131.181 184.439 1.00 82.26  ? 3021 PHE A CZ    1 
ATOM   13673 N  N     . GLU A 1 3022 ? 177.013 127.727 178.376 1.00 102.13 ? 3022 GLU A N     1 
ATOM   13674 C  CA    . GLU A 1 3022 ? 177.429 126.766 177.366 1.00 104.10 ? 3022 GLU A CA    1 
ATOM   13675 C  C     . GLU A 1 3022 ? 178.948 126.700 177.308 1.00 109.47 ? 3022 GLU A C     1 
ATOM   13676 O  O     . GLU A 1 3022 ? 179.640 127.677 177.604 1.00 108.45 ? 3022 GLU A O     1 
ATOM   13677 C  CB    . GLU A 1 3022 ? 176.873 127.129 175.984 1.00 102.90 ? 3022 GLU A CB    1 
ATOM   13678 C  CG    . GLU A 1 3022 ? 175.423 126.732 175.772 1.00 101.46 ? 3022 GLU A CG    1 
ATOM   13679 C  CD    . GLU A 1 3022 ? 174.736 127.588 174.729 1.00 99.24  ? 3022 GLU A CD    1 
ATOM   13680 O  OE1   . GLU A 1 3022 ? 175.296 128.642 174.361 1.00 99.81  ? 3022 GLU A OE1   1 
ATOM   13681 O  OE2   . GLU A 1 3022 ? 173.641 127.203 174.270 1.00 96.13  ? 3022 GLU A OE2   1 
ATOM   13682 N  N     . GLY A 1 3023 ? 179.454 125.538 176.911 1.00 112.94 ? 3023 GLY A N     1 
ATOM   13683 C  CA    . GLY A 1 3023 ? 180.888 125.372 176.733 1.00 113.37 ? 3023 GLY A CA    1 
ATOM   13684 C  C     . GLY A 1 3023 ? 181.633 125.508 178.046 1.00 113.73 ? 3023 GLY A C     1 
ATOM   13685 O  O     . GLY A 1 3023 ? 181.349 124.807 179.025 1.00 112.75 ? 3023 GLY A O     1 
ATOM   13686 N  N     . ASP A 1 3024 ? 182.612 126.415 178.068 1.00 118.60 ? 3024 ASP A N     1 
ATOM   13687 C  CA    . ASP A 1 3024 ? 183.380 126.649 179.287 1.00 119.91 ? 3024 ASP A CA    1 
ATOM   13688 C  C     . ASP A 1 3024 ? 182.494 127.183 180.404 1.00 113.09 ? 3024 ASP A C     1 
ATOM   13689 O  O     . ASP A 1 3024 ? 182.637 126.782 181.566 1.00 107.66 ? 3024 ASP A O     1 
ATOM   13690 C  CB    . ASP A 1 3024 ? 184.530 127.615 179.003 1.00 123.14 ? 3024 ASP A CB    1 
ATOM   13691 C  CG    . ASP A 1 3024 ? 184.076 128.863 178.269 1.00 121.47 ? 3024 ASP A CG    1 
ATOM   13692 O  OD1   . ASP A 1 3024 ? 182.876 128.956 177.935 1.00 117.81 ? 3024 ASP A OD1   1 
ATOM   13693 O  OD2   . ASP A 1 3024 ? 184.919 129.752 178.027 1.00 123.19 ? 3024 ASP A OD2   1 
ATOM   13694 N  N     . GLU A 1 3025 ? 181.572 128.091 180.069 1.00 113.05 ? 3025 GLU A N     1 
ATOM   13695 C  CA    . GLU A 1 3025 ? 180.675 128.649 181.075 1.00 109.10 ? 3025 GLU A CA    1 
ATOM   13696 C  C     . GLU A 1 3025 ? 179.856 127.558 181.749 1.00 103.57 ? 3025 GLU A C     1 
ATOM   13697 O  O     . GLU A 1 3025 ? 179.675 127.574 182.970 1.00 101.67 ? 3025 GLU A O     1 
ATOM   13698 C  CB    . GLU A 1 3025 ? 179.754 129.692 180.440 1.00 108.72 ? 3025 GLU A CB    1 
ATOM   13699 C  CG    . GLU A 1 3025 ? 180.477 130.865 179.800 1.00 113.01 ? 3025 GLU A CG    1 
ATOM   13700 C  CD    . GLU A 1 3025 ? 180.917 131.908 180.811 1.00 115.98 ? 3025 GLU A CD    1 
ATOM   13701 O  OE1   . GLU A 1 3025 ? 180.726 131.687 182.025 1.00 112.72 ? 3025 GLU A OE1   1 
ATOM   13702 O  OE2   . GLU A 1 3025 ? 181.455 132.954 180.389 1.00 115.75 ? 3025 GLU A OE2   1 
ATOM   13703 N  N     . TYR A 1 3026 ? 179.358 126.596 180.969 1.00 102.28 ? 3026 TYR A N     1 
ATOM   13704 C  CA    . TYR A 1 3026 ? 178.593 125.499 181.551 1.00 100.95 ? 3026 TYR A CA    1 
ATOM   13705 C  C     . TYR A 1 3026 ? 179.463 124.645 182.465 1.00 103.29 ? 3026 TYR A C     1 
ATOM   13706 O  O     . TYR A 1 3026 ? 179.000 124.181 183.513 1.00 104.01 ? 3026 TYR A O     1 
ATOM   13707 C  CB    . TYR A 1 3026 ? 177.973 124.646 180.446 1.00 104.63 ? 3026 TYR A CB    1 
ATOM   13708 C  CG    . TYR A 1 3026 ? 177.119 123.510 180.961 1.00 110.44 ? 3026 TYR A CG    1 
ATOM   13709 C  CD1   . TYR A 1 3026 ? 175.847 123.748 181.463 1.00 107.54 ? 3026 TYR A CD1   1 
ATOM   13710 C  CD2   . TYR A 1 3026 ? 177.583 122.202 180.948 1.00 111.87 ? 3026 TYR A CD2   1 
ATOM   13711 C  CE1   . TYR A 1 3026 ? 175.061 122.717 181.935 1.00 104.91 ? 3026 TYR A CE1   1 
ATOM   13712 C  CE2   . TYR A 1 3026 ? 176.804 121.163 181.419 1.00 110.51 ? 3026 TYR A CE2   1 
ATOM   13713 C  CZ    . TYR A 1 3026 ? 175.543 121.427 181.911 1.00 112.70 ? 3026 TYR A CZ    1 
ATOM   13714 O  OH    . TYR A 1 3026 ? 174.762 120.397 182.382 1.00 115.55 ? 3026 TYR A OH    1 
ATOM   13715 N  N     . ALA A 1 3027 ? 180.723 124.422 182.086 1.00 106.38 ? 3027 ALA A N     1 
ATOM   13716 C  CA    . ALA A 1 3027 ? 181.618 123.632 182.926 1.00 106.19 ? 3027 ALA A CA    1 
ATOM   13717 C  C     . ALA A 1 3027 ? 181.885 124.323 184.259 1.00 108.40 ? 3027 ALA A C     1 
ATOM   13718 O  O     . ALA A 1 3027 ? 181.829 123.686 185.319 1.00 107.04 ? 3027 ALA A O     1 
ATOM   13719 C  CB    . ALA A 1 3027 ? 182.929 123.362 182.189 1.00 105.63 ? 3027 ALA A CB    1 
ATOM   13720 N  N     . THR A 1 3028 ? 182.173 125.627 184.229 1.00 108.30 ? 3028 THR A N     1 
ATOM   13721 C  CA    . THR A 1 3028 ? 182.370 126.354 185.480 1.00 101.28 ? 3028 THR A CA    1 
ATOM   13722 C  C     . THR A 1 3028 ? 181.088 126.397 186.302 1.00 100.04 ? 3028 THR A C     1 
ATOM   13723 O  O     . THR A 1 3028 ? 181.134 126.322 187.536 1.00 99.46  ? 3028 THR A O     1 
ATOM   13724 C  CB    . THR A 1 3028 ? 182.880 127.771 185.212 1.00 98.02  ? 3028 THR A CB    1 
ATOM   13725 O  OG1   . THR A 1 3028 ? 181.793 128.605 184.791 1.00 98.80  ? 3028 THR A OG1   1 
ATOM   13726 C  CG2   . THR A 1 3028 ? 183.978 127.768 184.161 1.00 102.97 ? 3028 THR A CG2   1 
ATOM   13727 N  N     . LEU A 1 3029 ? 179.935 126.525 185.639 1.00 102.30 ? 3029 LEU A N     1 
ATOM   13728 C  CA    . LEU A 1 3029 ? 178.667 126.505 186.358 1.00 99.43  ? 3029 LEU A CA    1 
ATOM   13729 C  C     . LEU A 1 3029 ? 178.464 125.174 187.067 1.00 101.20 ? 3029 LEU A C     1 
ATOM   13730 O  O     . LEU A 1 3029 ? 178.045 125.143 188.227 1.00 102.87 ? 3029 LEU A O     1 
ATOM   13731 C  CB    . LEU A 1 3029 ? 177.512 126.782 185.396 1.00 94.73  ? 3029 LEU A CB    1 
ATOM   13732 C  CG    . LEU A 1 3029 ? 176.126 126.367 185.892 1.00 89.30  ? 3029 LEU A CG    1 
ATOM   13733 C  CD1   . LEU A 1 3029 ? 175.666 127.285 187.009 1.00 89.21  ? 3029 LEU A CD1   1 
ATOM   13734 C  CD2   . LEU A 1 3029 ? 175.119 126.351 184.758 1.00 86.17  ? 3029 LEU A CD2   1 
ATOM   13735 N  N     . MET A 1 3030 ? 178.765 124.065 186.388 1.00 100.66 ? 3030 MET A N     1 
ATOM   13736 C  CA    . MET A 1 3030 ? 178.658 122.753 187.022 1.00 102.97 ? 3030 MET A CA    1 
ATOM   13737 C  C     . MET A 1 3030 ? 179.635 122.611 188.182 1.00 107.79 ? 3030 MET A C     1 
ATOM   13738 O  O     . MET A 1 3030 ? 179.292 122.036 189.220 1.00 107.33 ? 3030 MET A O     1 
ATOM   13739 C  CB    . MET A 1 3030 ? 178.881 121.646 185.993 1.00 105.44 ? 3030 MET A CB    1 
ATOM   13740 C  CG    . MET A 1 3030 ? 177.811 121.552 184.915 1.00 110.79 ? 3030 MET A CG    1 
ATOM   13741 S  SD    . MET A 1 3030 ? 176.176 121.176 185.583 1.00 109.93 ? 3030 MET A SD    1 
ATOM   13742 C  CE    . MET A 1 3030 ? 175.387 122.781 185.537 1.00 101.55 ? 3030 MET A CE    1 
ATOM   13743 N  N     . THR A 1 3031 ? 180.858 123.121 188.026 1.00 107.68 ? 3031 THR A N     1 
ATOM   13744 C  CA    . THR A 1 3031 ? 181.835 123.033 189.110 1.00 105.92 ? 3031 THR A CA    1 
ATOM   13745 C  C     . THR A 1 3031 ? 181.360 123.796 190.343 1.00 106.09 ? 3031 THR A C     1 
ATOM   13746 O  O     . THR A 1 3031 ? 181.368 123.267 191.464 1.00 102.66 ? 3031 THR A O     1 
ATOM   13747 C  CB    . THR A 1 3031 ? 183.189 123.564 188.640 1.00 105.75 ? 3031 THR A CB    1 
ATOM   13748 O  OG1   . THR A 1 3031 ? 183.623 122.824 187.492 1.00 108.27 ? 3031 THR A OG1   1 
ATOM   13749 C  CG2   . THR A 1 3031 ? 184.225 123.431 189.744 1.00 104.70 ? 3031 THR A CG2   1 
ATOM   13750 N  N     . GLN A 1 3032 ? 180.929 125.045 190.151 1.00 105.84 ? 3032 GLN A N     1 
ATOM   13751 C  CA    . GLN A 1 3032 ? 180.453 125.841 191.277 1.00 101.22 ? 3032 GLN A CA    1 
ATOM   13752 C  C     . GLN A 1 3032 ? 179.166 125.275 191.861 1.00 103.04 ? 3032 GLN A C     1 
ATOM   13753 O  O     . GLN A 1 3032 ? 178.949 125.361 193.074 1.00 106.26 ? 3032 GLN A O     1 
ATOM   13754 C  CB    . GLN A 1 3032 ? 180.258 127.294 190.850 1.00 94.12  ? 3032 GLN A CB    1 
ATOM   13755 C  CG    . GLN A 1 3032 ? 181.508 127.936 190.277 1.00 93.68  ? 3032 GLN A CG    1 
ATOM   13756 C  CD    . GLN A 1 3032 ? 181.202 128.923 189.172 1.00 96.76  ? 3032 GLN A CD    1 
ATOM   13757 O  OE1   . GLN A 1 3032 ? 180.045 129.124 188.808 1.00 97.93  ? 3032 GLN A OE1   1 
ATOM   13758 N  NE2   . GLN A 1 3032 ? 182.242 129.545 188.629 1.00 94.81  ? 3032 GLN A NE2   1 
ATOM   13759 N  N     . CYS A 1 3033 ? 178.309 124.686 191.025 1.00 101.63 ? 3033 CYS A N     1 
ATOM   13760 C  CA    . CYS A 1 3033 ? 177.094 124.057 191.525 1.00 102.83 ? 3033 CYS A CA    1 
ATOM   13761 C  C     . CYS A 1 3033 ? 177.417 122.833 192.370 1.00 106.13 ? 3033 CYS A C     1 
ATOM   13762 O  O     . CYS A 1 3033 ? 176.774 122.596 193.398 1.00 106.95 ? 3033 CYS A O     1 
ATOM   13763 C  CB    . CYS A 1 3033 ? 176.187 123.687 190.354 1.00 101.09 ? 3033 CYS A CB    1 
ATOM   13764 S  SG    . CYS A 1 3033 ? 174.489 123.326 190.812 1.00 93.72  ? 3033 CYS A SG    1 
ATOM   13765 N  N     . LYS A 1 3034 ? 178.408 122.043 191.951 1.00 106.99 ? 3034 LYS A N     1 
ATOM   13766 C  CA    . LYS A 1 3034 ? 178.865 120.923 192.767 1.00 108.45 ? 3034 LYS A CA    1 
ATOM   13767 C  C     . LYS A 1 3034 ? 179.411 121.408 194.102 1.00 111.41 ? 3034 LYS A C     1 
ATOM   13768 O  O     . LYS A 1 3034 ? 179.109 120.829 195.154 1.00 110.96 ? 3034 LYS A O     1 
ATOM   13769 C  CB    . LYS A 1 3034 ? 179.931 120.132 192.009 1.00 111.69 ? 3034 LYS A CB    1 
ATOM   13770 C  CG    . LYS A 1 3034 ? 180.477 118.930 192.758 1.00 113.63 ? 3034 LYS A CG    1 
ATOM   13771 C  CD    . LYS A 1 3034 ? 179.434 117.839 192.870 1.00 116.31 ? 3034 LYS A CD    1 
ATOM   13772 C  CE    . LYS A 1 3034 ? 180.004 116.584 193.507 1.00 115.77 ? 3034 LYS A CE    1 
ATOM   13773 N  NZ    . LYS A 1 3034 ? 178.965 115.533 193.682 1.00 113.65 ? 3034 LYS A NZ    1 
ATOM   13774 N  N     . GLU A 1 3035 ? 180.216 122.473 194.078 1.00 111.22 ? 3035 GLU A N     1 
ATOM   13775 C  CA    . GLU A 1 3035 ? 180.756 123.017 195.321 1.00 110.20 ? 3035 GLU A CA    1 
ATOM   13776 C  C     . GLU A 1 3035 ? 179.638 123.490 196.244 1.00 108.65 ? 3035 GLU A C     1 
ATOM   13777 O  O     . GLU A 1 3035 ? 179.653 123.215 197.449 1.00 106.00 ? 3035 GLU A O     1 
ATOM   13778 C  CB    . GLU A 1 3035 ? 181.727 124.159 195.019 1.00 109.00 ? 3035 GLU A CB    1 
ATOM   13779 C  CG    . GLU A 1 3035 ? 182.963 123.736 194.242 1.00 109.39 ? 3035 GLU A CG    1 
ATOM   13780 C  CD    . GLU A 1 3035 ? 183.723 124.916 193.669 1.00 111.89 ? 3035 GLU A CD    1 
ATOM   13781 O  OE1   . GLU A 1 3035 ? 183.268 126.064 193.853 1.00 107.31 ? 3035 GLU A OE1   1 
ATOM   13782 O  OE2   . GLU A 1 3035 ? 184.776 124.695 193.036 1.00 116.07 ? 3035 GLU A OE2   1 
ATOM   13783 N  N     . GLY A 1 3036 ? 178.649 124.193 195.689 1.00 109.87 ? 3036 GLY A N     1 
ATOM   13784 C  CA    . GLY A 1 3036 ? 177.545 124.673 196.504 1.00 109.15 ? 3036 GLY A CA    1 
ATOM   13785 C  C     . GLY A 1 3036 ? 176.683 123.552 197.053 1.00 111.00 ? 3036 GLY A C     1 
ATOM   13786 O  O     . GLY A 1 3036 ? 176.226 123.614 198.197 1.00 112.90 ? 3036 GLY A O     1 
ATOM   13787 N  N     . ALA A 1 3037 ? 176.438 122.519 196.244 1.00 108.19 ? 3037 ALA A N     1 
ATOM   13788 C  CA    . ALA A 1 3037 ? 175.661 121.378 196.712 1.00 108.27 ? 3037 ALA A CA    1 
ATOM   13789 C  C     . ALA A 1 3037 ? 176.382 120.645 197.834 1.00 115.50 ? 3037 ALA A C     1 
ATOM   13790 O  O     . ALA A 1 3037 ? 175.757 120.242 198.823 1.00 117.11 ? 3037 ALA A O     1 
ATOM   13791 C  CB    . ALA A 1 3037 ? 175.368 120.431 195.549 1.00 108.70 ? 3037 ALA A CB    1 
ATOM   13792 N  N     . GLN A 1 3038 ? 177.697 120.455 197.698 1.00 116.80 ? 3038 GLN A N     1 
ATOM   13793 C  CA    . GLN A 1 3038 ? 178.461 119.857 198.788 1.00 116.68 ? 3038 GLN A CA    1 
ATOM   13794 C  C     . GLN A 1 3038 ? 178.439 120.734 200.033 1.00 117.73 ? 3038 GLN A C     1 
ATOM   13795 O  O     . GLN A 1 3038 ? 178.342 120.216 201.151 1.00 116.59 ? 3038 GLN A O     1 
ATOM   13796 C  CB    . GLN A 1 3038 ? 179.902 119.596 198.353 1.00 116.43 ? 3038 GLN A CB    1 
ATOM   13797 C  CG    . GLN A 1 3038 ? 180.052 118.540 197.273 1.00 119.06 ? 3038 GLN A CG    1 
ATOM   13798 C  CD    . GLN A 1 3038 ? 181.493 118.355 196.844 1.00 121.36 ? 3038 GLN A CD    1 
ATOM   13799 O  OE1   . GLN A 1 3038 ? 181.799 117.507 196.007 1.00 125.16 ? 3038 GLN A OE1   1 
ATOM   13800 N  NE2   . GLN A 1 3038 ? 182.388 119.150 197.418 1.00 115.41 ? 3038 GLN A NE2   1 
ATOM   13801 N  N     . LYS A 1 3039 ? 178.534 122.055 199.861 1.00 116.10 ? 3039 LYS A N     1 
ATOM   13802 C  CA    . LYS A 1 3039 ? 178.492 122.958 201.006 1.00 114.27 ? 3039 LYS A CA    1 
ATOM   13803 C  C     . LYS A 1 3039 ? 177.152 122.873 201.726 1.00 117.50 ? 3039 LYS A C     1 
ATOM   13804 O  O     . LYS A 1 3039 ? 177.101 122.874 202.961 1.00 120.55 ? 3039 LYS A O     1 
ATOM   13805 C  CB    . LYS A 1 3039 ? 178.775 124.388 200.547 1.00 109.17 ? 3039 LYS A CB    1 
ATOM   13806 C  CG    . LYS A 1 3039 ? 178.423 125.459 201.562 1.00 107.84 ? 3039 LYS A CG    1 
ATOM   13807 C  CD    . LYS A 1 3039 ? 179.434 126.592 201.524 1.00 101.10 ? 3039 LYS A CD    1 
ATOM   13808 C  CE    . LYS A 1 3039 ? 179.469 127.249 200.156 1.00 97.86  ? 3039 LYS A CE    1 
ATOM   13809 N  NZ    . LYS A 1 3039 ? 180.661 128.123 199.990 1.00 93.04  ? 3039 LYS A NZ    1 
ATOM   13810 N  N     . GLU A 1 3040 ? 176.056 122.797 200.971 1.00 117.18 ? 3040 GLU A N     1 
ATOM   13811 C  CA    . GLU A 1 3040 ? 174.738 122.639 201.572 1.00 120.36 ? 3040 GLU A CA    1 
ATOM   13812 C  C     . GLU A 1 3040 ? 174.497 121.229 202.094 1.00 121.99 ? 3040 GLU A C     1 
ATOM   13813 O  O     . GLU A 1 3040 ? 173.708 121.058 203.030 1.00 121.23 ? 3040 GLU A O     1 
ATOM   13814 C  CB    . GLU A 1 3040 ? 173.648 123.008 200.564 1.00 120.76 ? 3040 GLU A CB    1 
ATOM   13815 C  CG    . GLU A 1 3040 ? 173.624 124.480 200.190 1.00 121.72 ? 3040 GLU A CG    1 
ATOM   13816 C  CD    . GLU A 1 3040 ? 173.230 125.369 201.351 1.00 126.02 ? 3040 GLU A CD    1 
ATOM   13817 O  OE1   . GLU A 1 3040 ? 172.413 124.929 202.188 1.00 134.00 ? 3040 GLU A OE1   1 
ATOM   13818 O  OE2   . GLU A 1 3040 ? 173.739 126.507 201.430 1.00 116.90 ? 3040 GLU A OE2   1 
ATOM   13819 N  N     . GLY A 1 3041 ? 175.150 120.222 201.518 1.00 121.56 ? 3041 GLY A N     1 
ATOM   13820 C  CA    . GLY A 1 3041 ? 175.021 118.866 202.012 1.00 121.97 ? 3041 GLY A CA    1 
ATOM   13821 C  C     . GLY A 1 3041 ? 174.438 117.876 201.024 1.00 123.69 ? 3041 GLY A C     1 
ATOM   13822 O  O     . GLY A 1 3041 ? 173.896 116.842 201.427 1.00 123.34 ? 3041 GLY A O     1 
ATOM   13823 N  N     . LEU A 1 3042 ? 174.540 118.174 199.731 1.00 123.95 ? 3042 LEU A N     1 
ATOM   13824 C  CA    . LEU A 1 3042 ? 174.076 117.282 198.674 1.00 122.42 ? 3042 LEU A CA    1 
ATOM   13825 C  C     . LEU A 1 3042 ? 175.266 116.853 197.829 1.00 122.10 ? 3042 LEU A C     1 
ATOM   13826 O  O     . LEU A 1 3042 ? 175.971 117.699 197.269 1.00 121.87 ? 3042 LEU A O     1 
ATOM   13827 C  CB    . LEU A 1 3042 ? 173.016 117.957 197.799 1.00 118.20 ? 3042 LEU A CB    1 
ATOM   13828 C  CG    . LEU A 1 3042 ? 171.735 118.449 198.476 1.00 117.32 ? 3042 LEU A CG    1 
ATOM   13829 C  CD1   . LEU A 1 3042 ? 170.651 118.690 197.438 1.00 109.84 ? 3042 LEU A CD1   1 
ATOM   13830 C  CD2   . LEU A 1 3042 ? 171.256 117.459 199.525 1.00 118.11 ? 3042 LEU A CD2   1 
ATOM   13831 N  N     . MET A 1 3043 ? 175.488 115.546 197.741 1.00 121.34 ? 3043 MET A N     1 
ATOM   13832 C  CA    . MET A 1 3043 ? 176.538 114.998 196.883 1.00 123.77 ? 3043 MET A CA    1 
ATOM   13833 C  C     . MET A 1 3043 ? 176.004 114.626 195.499 1.00 124.35 ? 3043 MET A C     1 
ATOM   13834 O  O     . MET A 1 3043 ? 176.215 113.527 194.988 1.00 123.65 ? 3043 MET A O     1 
ATOM   13835 C  CB    . MET A 1 3043 ? 177.198 113.809 197.577 1.00 127.30 ? 3043 MET A CB    1 
ATOM   13836 C  CG    . MET A 1 3043 ? 176.293 112.609 197.834 1.00 132.88 ? 3043 MET A CG    1 
ATOM   13837 S  SD    . MET A 1 3043 ? 177.137 111.304 198.747 1.00 144.98 ? 3043 MET A SD    1 
ATOM   13838 C  CE    . MET A 1 3043 ? 177.217 112.029 200.383 1.00 125.91 ? 3043 MET A CE    1 
ATOM   13839 N  N     . LEU A 1 3044 ? 175.324 115.576 194.865 1.00 124.20 ? 3044 LEU A N     1 
ATOM   13840 C  CA    . LEU A 1 3044 ? 174.819 115.360 193.517 1.00 126.01 ? 3044 LEU A CA    1 
ATOM   13841 C  C     . LEU A 1 3044 ? 175.966 115.418 192.517 1.00 125.39 ? 3044 LEU A C     1 
ATOM   13842 O  O     . LEU A 1 3044 ? 176.744 116.373 192.499 1.00 123.28 ? 3044 LEU A O     1 
ATOM   13843 C  CB    . LEU A 1 3044 ? 173.762 116.409 193.177 1.00 122.16 ? 3044 LEU A CB    1 
ATOM   13844 C  CG    . LEU A 1 3044 ? 172.555 116.438 194.118 1.00 122.88 ? 3044 LEU A CG    1 
ATOM   13845 C  CD1   . LEU A 1 3044 ? 171.574 117.527 193.716 1.00 111.71 ? 3044 LEU A CD1   1 
ATOM   13846 C  CD2   . LEU A 1 3044 ? 171.872 115.080 194.160 1.00 121.06 ? 3044 LEU A CD2   1 
ATOM   13847 N  N     . ASP A 1 3045 ? 176.066 114.393 191.677 1.00 124.58 ? 3045 ASP A N     1 
ATOM   13848 C  CA    . ASP A 1 3045 ? 177.206 114.253 190.776 1.00 123.06 ? 3045 ASP A CA    1 
ATOM   13849 C  C     . ASP A 1 3045 ? 176.862 114.462 189.310 1.00 121.56 ? 3045 ASP A C     1 
ATOM   13850 O  O     . ASP A 1 3045 ? 177.632 115.103 188.591 1.00 117.94 ? 3045 ASP A O     1 
ATOM   13851 C  CB    . ASP A 1 3045 ? 177.850 112.870 190.956 1.00 124.48 ? 3045 ASP A CB    1 
ATOM   13852 C  CG    . ASP A 1 3045 ? 176.876 111.736 190.709 1.00 128.29 ? 3045 ASP A CG    1 
ATOM   13853 O  OD1   . ASP A 1 3045 ? 175.657 112.000 190.643 1.00 126.73 ? 3045 ASP A OD1   1 
ATOM   13854 O  OD2   . ASP A 1 3045 ? 177.330 110.579 190.582 1.00 129.46 ? 3045 ASP A OD2   1 
ATOM   13855 N  N     . SER A 1 3046 ? 175.733 113.935 188.842 1.00 121.99 ? 3046 SER A N     1 
ATOM   13856 C  CA    . SER A 1 3046 ? 175.379 114.059 187.435 1.00 121.74 ? 3046 SER A CA    1 
ATOM   13857 C  C     . SER A 1 3046 ? 175.088 115.511 187.079 1.00 116.72 ? 3046 SER A C     1 
ATOM   13858 O  O     . SER A 1 3046 ? 174.541 116.269 187.884 1.00 113.88 ? 3046 SER A O     1 
ATOM   13859 C  CB    . SER A 1 3046 ? 174.170 113.181 187.111 1.00 116.27 ? 3046 SER A CB    1 
ATOM   13860 O  OG    . SER A 1 3046 ? 173.048 113.550 187.891 1.00 117.61 ? 3046 SER A OG    1 
ATOM   13861 N  N     . HIS A 1 3047 ? 175.466 115.898 185.857 1.00 115.65 ? 3047 HIS A N     1 
ATOM   13862 C  CA    . HIS A 1 3047 ? 175.293 117.284 185.432 1.00 110.82 ? 3047 HIS A CA    1 
ATOM   13863 C  C     . HIS A 1 3047 ? 173.821 117.664 185.355 1.00 107.99 ? 3047 HIS A C     1 
ATOM   13864 O  O     . HIS A 1 3047 ? 173.455 118.809 185.641 1.00 106.65 ? 3047 HIS A O     1 
ATOM   13865 C  CB    . HIS A 1 3047 ? 175.979 117.512 184.085 1.00 108.30 ? 3047 HIS A CB    1 
ATOM   13866 C  CG    . HIS A 1 3047 ? 177.452 117.755 184.191 1.00 110.92 ? 3047 HIS A CG    1 
ATOM   13867 N  ND1   . HIS A 1 3047 ? 178.224 118.131 183.113 1.00 109.54 ? 3047 HIS A ND1   1 
ATOM   13868 C  CD2   . HIS A 1 3047 ? 178.295 117.674 185.247 1.00 110.88 ? 3047 HIS A CD2   1 
ATOM   13869 C  CE1   . HIS A 1 3047 ? 179.478 118.273 183.501 1.00 106.74 ? 3047 HIS A CE1   1 
ATOM   13870 N  NE2   . HIS A 1 3047 ? 179.549 118.002 184.792 1.00 107.22 ? 3047 HIS A NE2   1 
ATOM   13871 N  N     . GLU A 1 3048 ? 172.962 116.725 184.954 1.00 109.34 ? 3048 GLU A N     1 
ATOM   13872 C  CA    . GLU A 1 3048 ? 171.534 117.019 184.887 1.00 107.56 ? 3048 GLU A CA    1 
ATOM   13873 C  C     . GLU A 1 3048 ? 170.962 117.303 186.270 1.00 102.58 ? 3048 GLU A C     1 
ATOM   13874 O  O     . GLU A 1 3048 ? 170.184 118.248 186.448 1.00 103.54 ? 3048 GLU A O     1 
ATOM   13875 C  CB    . GLU A 1 3048 ? 170.790 115.862 184.222 1.00 113.11 ? 3048 GLU A CB    1 
ATOM   13876 C  CG    . GLU A 1 3048 ? 171.385 115.427 182.893 1.00 120.88 ? 3048 GLU A CG    1 
ATOM   13877 C  CD    . GLU A 1 3048 ? 171.742 116.602 182.002 1.00 124.59 ? 3048 GLU A CD    1 
ATOM   13878 O  OE1   . GLU A 1 3048 ? 170.829 117.366 181.625 1.00 124.97 ? 3048 GLU A OE1   1 
ATOM   13879 O  OE2   . GLU A 1 3048 ? 172.938 116.762 181.679 1.00 124.30 ? 3048 GLU A OE2   1 
ATOM   13880 N  N     . GLU A 1 3049 ? 171.345 116.503 187.268 1.00 103.00 ? 3049 GLU A N     1 
ATOM   13881 C  CA    . GLU A 1 3049 ? 170.863 116.746 188.623 1.00 103.14 ? 3049 GLU A CA    1 
ATOM   13882 C  C     . GLU A 1 3049 ? 171.441 118.033 189.197 1.00 99.80  ? 3049 GLU A C     1 
ATOM   13883 O  O     . GLU A 1 3049 ? 170.752 118.744 189.938 1.00 94.34  ? 3049 GLU A O     1 
ATOM   13884 C  CB    . GLU A 1 3049 ? 171.199 115.558 189.524 1.00 109.56 ? 3049 GLU A CB    1 
ATOM   13885 C  CG    . GLU A 1 3049 ? 170.457 115.552 190.849 1.00 113.38 ? 3049 GLU A CG    1 
ATOM   13886 C  CD    . GLU A 1 3049 ? 169.002 115.140 190.708 1.00 115.30 ? 3049 GLU A CD    1 
ATOM   13887 O  OE1   . GLU A 1 3049 ? 168.601 114.724 189.601 1.00 112.53 ? 3049 GLU A OE1   1 
ATOM   13888 O  OE2   . GLU A 1 3049 ? 168.258 115.232 191.707 1.00 116.68 ? 3049 GLU A OE2   1 
ATOM   13889 N  N     . LEU A 1 3050 ? 172.694 118.350 188.864 1.00 99.89  ? 3050 LEU A N     1 
ATOM   13890 C  CA    . LEU A 1 3050 ? 173.268 119.624 189.283 1.00 92.87  ? 3050 LEU A CA    1 
ATOM   13891 C  C     . LEU A 1 3050 ? 172.510 120.796 188.673 1.00 88.00  ? 3050 LEU A C     1 
ATOM   13892 O  O     . LEU A 1 3050 ? 172.243 121.791 189.354 1.00 84.75  ? 3050 LEU A O     1 
ATOM   13893 C  CB    . LEU A 1 3050 ? 174.747 119.690 188.904 1.00 97.85  ? 3050 LEU A CB    1 
ATOM   13894 C  CG    . LEU A 1 3050 ? 175.691 118.792 189.702 1.00 105.17 ? 3050 LEU A CG    1 
ATOM   13895 C  CD1   . LEU A 1 3050 ? 177.114 118.932 189.192 1.00 106.33 ? 3050 LEU A CD1   1 
ATOM   13896 C  CD2   . LEU A 1 3050 ? 175.612 119.132 191.178 1.00 104.28 ? 3050 LEU A CD2   1 
ATOM   13897 N  N     . TYR A 1 3051 ? 172.156 120.699 187.390 1.00 89.31  ? 3051 TYR A N     1 
ATOM   13898 C  CA    . TYR A 1 3051 ? 171.380 121.763 186.763 1.00 80.79  ? 3051 TYR A CA    1 
ATOM   13899 C  C     . TYR A 1 3051 ? 169.995 121.870 187.382 1.00 79.70  ? 3051 TYR A C     1 
ATOM   13900 O  O     . TYR A 1 3051 ? 169.457 122.972 187.528 1.00 83.30  ? 3051 TYR A O     1 
ATOM   13901 C  CB    . TYR A 1 3051 ? 171.274 121.530 185.258 1.00 84.08  ? 3051 TYR A CB    1 
ATOM   13902 C  CG    . TYR A 1 3051 ? 171.039 122.800 184.474 1.00 85.26  ? 3051 TYR A CG    1 
ATOM   13903 C  CD1   . TYR A 1 3051 ? 172.015 123.784 184.402 1.00 87.81  ? 3051 TYR A CD1   1 
ATOM   13904 C  CD2   . TYR A 1 3051 ? 169.838 123.021 183.817 1.00 81.35  ? 3051 TYR A CD2   1 
ATOM   13905 C  CE1   . TYR A 1 3051 ? 171.805 124.947 183.689 1.00 86.48  ? 3051 TYR A CE1   1 
ATOM   13906 C  CE2   . TYR A 1 3051 ? 169.618 124.182 183.103 1.00 81.18  ? 3051 TYR A CE2   1 
ATOM   13907 C  CZ    . TYR A 1 3051 ? 170.605 125.141 183.043 1.00 81.61  ? 3051 TYR A CZ    1 
ATOM   13908 O  OH    . TYR A 1 3051 ? 170.392 126.300 182.333 1.00 77.41  ? 3051 TYR A OH    1 
ATOM   13909 N  N     . LYS A 1 3052 ? 169.395 120.735 187.742 1.00 81.78  ? 3052 LYS A N     1 
ATOM   13910 C  CA    . LYS A 1 3052 ? 168.100 120.770 188.414 1.00 80.87  ? 3052 LYS A CA    1 
ATOM   13911 C  C     . LYS A 1 3052 ? 168.201 121.470 189.766 1.00 75.50  ? 3052 LYS A C     1 
ATOM   13912 O  O     . LYS A 1 3052 ? 167.342 122.287 190.120 1.00 76.55  ? 3052 LYS A O     1 
ATOM   13913 C  CB    . LYS A 1 3052 ? 167.562 119.349 188.580 1.00 89.48  ? 3052 LYS A CB    1 
ATOM   13914 C  CG    . LYS A 1 3052 ? 166.050 119.238 188.490 1.00 87.17  ? 3052 LYS A CG    1 
ATOM   13915 C  CD    . LYS A 1 3052 ? 165.540 119.734 187.144 1.00 89.64  ? 3052 LYS A CD    1 
ATOM   13916 C  CE    . LYS A 1 3052 ? 166.172 118.968 185.990 1.00 81.45  ? 3052 LYS A CE    1 
ATOM   13917 N  NZ    . LYS A 1 3052 ? 165.820 119.563 184.672 1.00 80.28  ? 3052 LYS A NZ    1 
ATOM   13918 N  N     . TRP A 1 3053 ? 169.254 121.169 190.530 1.00 75.98  ? 3053 TRP A N     1 
ATOM   13919 C  CA    . TRP A 1 3053 ? 169.461 121.838 191.811 1.00 73.04  ? 3053 TRP A CA    1 
ATOM   13920 C  C     . TRP A 1 3053 ? 169.708 123.330 191.622 1.00 72.30  ? 3053 TRP A C     1 
ATOM   13921 O  O     . TRP A 1 3053 ? 169.217 124.153 192.402 1.00 74.20  ? 3053 TRP A O     1 
ATOM   13922 C  CB    . TRP A 1 3053 ? 170.631 121.197 192.556 1.00 74.05  ? 3053 TRP A CB    1 
ATOM   13923 C  CG    . TRP A 1 3053 ? 170.822 121.731 193.939 1.00 76.98  ? 3053 TRP A CG    1 
ATOM   13924 C  CD1   . TRP A 1 3053 ? 170.129 121.376 195.058 1.00 81.63  ? 3053 TRP A CD1   1 
ATOM   13925 C  CD2   . TRP A 1 3053 ? 171.762 122.730 194.349 1.00 75.20  ? 3053 TRP A CD2   1 
ATOM   13926 N  NE1   . TRP A 1 3053 ? 170.586 122.086 196.142 1.00 80.70  ? 3053 TRP A NE1   1 
ATOM   13927 C  CE2   . TRP A 1 3053 ? 171.588 122.925 195.732 1.00 79.36  ? 3053 TRP A CE2   1 
ATOM   13928 C  CE3   . TRP A 1 3053 ? 172.736 123.477 193.681 1.00 71.68  ? 3053 TRP A CE3   1 
ATOM   13929 C  CZ2   . TRP A 1 3053 ? 172.350 123.834 196.458 1.00 84.15  ? 3053 TRP A CZ2   1 
ATOM   13930 C  CZ3   . TRP A 1 3053 ? 173.491 124.377 194.402 1.00 76.44  ? 3053 TRP A CZ3   1 
ATOM   13931 C  CH2   . TRP A 1 3053 ? 173.295 124.549 195.776 1.00 84.14  ? 3053 TRP A CH2   1 
ATOM   13932 N  N     . PHE A 1 3054 ? 170.481 123.694 190.597 1.00 72.17  ? 3054 PHE A N     1 
ATOM   13933 C  CA    . PHE A 1 3054 ? 170.733 125.101 190.306 1.00 66.46  ? 3054 PHE A CA    1 
ATOM   13934 C  C     . PHE A 1 3054 ? 169.443 125.825 189.941 1.00 65.40  ? 3054 PHE A C     1 
ATOM   13935 O  O     . PHE A 1 3054 ? 169.213 126.960 190.374 1.00 68.50  ? 3054 PHE A O     1 
ATOM   13936 C  CB    . PHE A 1 3054 ? 171.768 125.206 189.184 1.00 69.60  ? 3054 PHE A CB    1 
ATOM   13937 C  CG    . PHE A 1 3054 ? 171.804 126.539 188.496 1.00 63.78  ? 3054 PHE A CG    1 
ATOM   13938 C  CD1   . PHE A 1 3054 ? 172.580 127.568 188.995 1.00 65.82  ? 3054 PHE A CD1   1 
ATOM   13939 C  CD2   . PHE A 1 3054 ? 171.095 126.750 187.325 1.00 64.46  ? 3054 PHE A CD2   1 
ATOM   13940 C  CE1   . PHE A 1 3054 ? 172.626 128.790 188.357 1.00 67.67  ? 3054 PHE A CE1   1 
ATOM   13941 C  CE2   . PHE A 1 3054 ? 171.137 127.970 186.684 1.00 65.85  ? 3054 PHE A CE2   1 
ATOM   13942 C  CZ    . PHE A 1 3054 ? 171.904 128.991 187.200 1.00 63.44  ? 3054 PHE A CZ    1 
ATOM   13943 N  N     . THR A 1 3055 ? 168.588 125.179 189.147 1.00 65.86  ? 3055 THR A N     1 
ATOM   13944 C  CA    . THR A 1 3055 ? 167.296 125.764 188.810 1.00 64.42  ? 3055 THR A CA    1 
ATOM   13945 C  C     . THR A 1 3055 ? 166.432 125.939 190.051 1.00 64.83  ? 3055 THR A C     1 
ATOM   13946 O  O     . THR A 1 3055 ? 165.769 126.968 190.212 1.00 70.34  ? 3055 THR A O     1 
ATOM   13947 C  CB    . THR A 1 3055 ? 166.580 124.897 187.774 1.00 70.96  ? 3055 THR A CB    1 
ATOM   13948 O  OG1   . THR A 1 3055 ? 167.342 124.872 186.561 1.00 79.46  ? 3055 THR A OG1   1 
ATOM   13949 C  CG2   . THR A 1 3055 ? 165.194 125.444 187.482 1.00 71.35  ? 3055 THR A CG2   1 
ATOM   13950 N  N     . SER A 1 3056 ? 166.431 124.948 190.945 1.00 62.66  ? 3056 SER A N     1 
ATOM   13951 C  CA    . SER A 1 3056 ? 165.669 125.076 192.185 1.00 62.58  ? 3056 SER A CA    1 
ATOM   13952 C  C     . SER A 1 3056 ? 166.189 126.228 193.040 1.00 66.12  ? 3056 SER A C     1 
ATOM   13953 O  O     . SER A 1 3056 ? 165.404 126.981 193.633 1.00 69.62  ? 3056 SER A O     1 
ATOM   13954 C  CB    . SER A 1 3056 ? 165.717 123.764 192.966 1.00 61.89  ? 3056 SER A CB    1 
ATOM   13955 O  OG    . SER A 1 3056 ? 165.091 123.903 194.229 1.00 74.20  ? 3056 SER A OG    1 
ATOM   13956 N  N     . GLN A 1 3057 ? 167.512 126.375 193.120 1.00 63.72  ? 3057 GLN A N     1 
ATOM   13957 C  CA    . GLN A 1 3057 ? 168.091 127.471 193.889 1.00 62.87  ? 3057 GLN A CA    1 
ATOM   13958 C  C     . GLN A 1 3057 ? 167.735 128.823 193.284 1.00 60.48  ? 3057 GLN A C     1 
ATOM   13959 O  O     . GLN A 1 3057 ? 167.458 129.781 194.012 1.00 62.23  ? 3057 GLN A O     1 
ATOM   13960 C  CB    . GLN A 1 3057 ? 169.606 127.306 193.988 1.00 60.36  ? 3057 GLN A CB    1 
ATOM   13961 C  CG    . GLN A 1 3057 ? 170.044 126.166 194.883 1.00 67.38  ? 3057 GLN A CG    1 
ATOM   13962 C  CD    . GLN A 1 3057 ? 169.641 126.378 196.327 1.00 70.14  ? 3057 GLN A CD    1 
ATOM   13963 O  OE1   . GLN A 1 3057 ? 168.568 125.952 196.754 1.00 69.78  ? 3057 GLN A OE1   1 
ATOM   13964 N  NE2   . GLN A 1 3057 ? 170.500 127.044 197.089 1.00 70.51  ? 3057 GLN A NE2   1 
ATOM   13965 N  N     . VAL A 1 3058 ? 167.746 128.924 191.954 1.00 54.77  ? 3058 VAL A N     1 
ATOM   13966 C  CA    . VAL A 1 3058 ? 167.342 130.172 191.311 1.00 47.52  ? 3058 VAL A CA    1 
ATOM   13967 C  C     . VAL A 1 3058 ? 165.861 130.438 191.556 1.00 52.63  ? 3058 VAL A C     1 
ATOM   13968 O  O     . VAL A 1 3058 ? 165.439 131.589 191.715 1.00 61.70  ? 3058 VAL A O     1 
ATOM   13969 C  CB    . VAL A 1 3058 ? 167.680 130.136 189.810 1.00 45.70  ? 3058 VAL A CB    1 
ATOM   13970 C  CG1   . VAL A 1 3058 ? 167.050 131.312 189.088 1.00 45.99  ? 3058 VAL A CG1   1 
ATOM   13971 C  CG2   . VAL A 1 3058 ? 169.183 130.139 189.607 1.00 58.02  ? 3058 VAL A CG2   1 
ATOM   13972 N  N     . ILE A 1 3059 ? 165.050 129.379 191.597 1.00 55.17  ? 3059 ILE A N     1 
ATOM   13973 C  CA    . ILE A 1 3059 ? 163.630 129.527 191.909 1.00 55.89  ? 3059 ILE A CA    1 
ATOM   13974 C  C     . ILE A 1 3059 ? 163.452 130.122 193.300 1.00 60.27  ? 3059 ILE A C     1 
ATOM   13975 O  O     . ILE A 1 3059 ? 162.682 131.068 193.500 1.00 63.44  ? 3059 ILE A O     1 
ATOM   13976 C  CB    . ILE A 1 3059 ? 162.913 128.170 191.788 1.00 56.75  ? 3059 ILE A CB    1 
ATOM   13977 C  CG1   . ILE A 1 3059 ? 162.760 127.759 190.326 1.00 57.28  ? 3059 ILE A CG1   1 
ATOM   13978 C  CG2   . ILE A 1 3059 ? 161.558 128.214 192.470 1.00 58.99  ? 3059 ILE A CG2   1 
ATOM   13979 C  CD1   . ILE A 1 3059 ? 161.810 128.622 189.563 1.00 62.52  ? 3059 ILE A CD1   1 
ATOM   13980 N  N     . ARG A 1 3060 ? 164.171 129.582 194.277 1.00 60.69  ? 3060 ARG A N     1 
ATOM   13981 C  CA    . ARG A 1 3060 ? 163.999 129.978 195.669 1.00 60.70  ? 3060 ARG A CA    1 
ATOM   13982 C  C     . ARG A 1 3060 ? 164.853 131.172 196.079 1.00 65.22  ? 3060 ARG A C     1 
ATOM   13983 O  O     . ARG A 1 3060 ? 164.761 131.606 197.231 1.00 73.67  ? 3060 ARG A O     1 
ATOM   13984 C  CB    . ARG A 1 3060 ? 164.309 128.795 196.591 1.00 63.32  ? 3060 ARG A CB    1 
ATOM   13985 C  CG    . ARG A 1 3060 ? 163.389 127.601 196.406 1.00 69.67  ? 3060 ARG A CG    1 
ATOM   13986 C  CD    . ARG A 1 3060 ? 161.971 127.939 196.833 1.00 73.48  ? 3060 ARG A CD    1 
ATOM   13987 N  NE    . ARG A 1 3060 ? 161.902 128.232 198.260 1.00 78.74  ? 3060 ARG A NE    1 
ATOM   13988 C  CZ    . ARG A 1 3060 ? 160.894 128.856 198.854 1.00 75.36  ? 3060 ARG A CZ    1 
ATOM   13989 N  NH1   . ARG A 1 3060 ? 159.843 129.277 198.172 1.00 71.97  ? 3060 ARG A NH1   1 
ATOM   13990 N  NH2   . ARG A 1 3060 ? 160.942 129.062 200.167 1.00 75.22  ? 3060 ARG A NH2   1 
ATOM   13991 N  N     . ASN A 1 3061 ? 165.674 131.718 195.184 1.00 58.82  ? 3061 ASN A N     1 
ATOM   13992 C  CA    . ASN A 1 3061 ? 166.630 132.736 195.603 1.00 54.66  ? 3061 ASN A CA    1 
ATOM   13993 C  C     . ASN A 1 3061 ? 166.506 134.037 194.822 1.00 50.77  ? 3061 ASN A C     1 
ATOM   13994 O  O     . ASN A 1 3061 ? 166.676 135.118 195.392 1.00 59.11  ? 3061 ASN A O     1 
ATOM   13995 C  CB    . ASN A 1 3061 ? 168.057 132.198 195.477 1.00 55.52  ? 3061 ASN A CB    1 
ATOM   13996 C  CG    . ASN A 1 3061 ? 168.427 131.263 196.607 1.00 65.91  ? 3061 ASN A CG    1 
ATOM   13997 O  OD1   . ASN A 1 3061 ? 167.649 130.390 196.987 1.00 70.20  ? 3061 ASN A OD1   1 
ATOM   13998 N  ND2   . ASN A 1 3061 ? 169.619 131.445 197.157 1.00 66.70  ? 3061 ASN A ND2   1 
ATOM   13999 N  N     . LEU A 1 3062 ? 166.216 133.958 193.528 1.00 46.81  ? 3062 LEU A N     1 
ATOM   14000 C  CA    . LEU A 1 3062 ? 166.198 135.129 192.663 1.00 42.11  ? 3062 LEU A CA    1 
ATOM   14001 C  C     . LEU A 1 3062 ? 164.775 135.636 192.487 1.00 47.83  ? 3062 LEU A C     1 
ATOM   14002 O  O     . LEU A 1 3062 ? 163.877 134.871 192.120 1.00 51.97  ? 3062 LEU A O     1 
ATOM   14003 C  CB    . LEU A 1 3062 ? 166.817 134.820 191.301 1.00 42.59  ? 3062 LEU A CB    1 
ATOM   14004 C  CG    . LEU A 1 3062 ? 166.741 135.974 190.305 1.00 43.88  ? 3062 LEU A CG    1 
ATOM   14005 C  CD1   . LEU A 1 3062 ? 167.548 137.149 190.805 1.00 46.12  ? 3062 LEU A CD1   1 
ATOM   14006 C  CD2   . LEU A 1 3062 ? 167.251 135.527 188.955 1.00 48.85  ? 3062 LEU A CD2   1 
ATOM   14007 N  N     . HIS A 1 3063 ? 164.580 136.927 192.748 1.00 43.64  ? 3063 HIS A N     1 
ATOM   14008 C  CA    . HIS A 1 3063 ? 163.299 137.597 192.576 1.00 38.03  ? 3063 HIS A CA    1 
ATOM   14009 C  C     . HIS A 1 3063 ? 163.505 138.819 191.698 1.00 38.79  ? 3063 HIS A C     1 
ATOM   14010 O  O     . HIS A 1 3063 ? 164.426 139.607 191.934 1.00 46.43  ? 3063 HIS A O     1 
ATOM   14011 C  CB    . HIS A 1 3063 ? 162.704 138.002 193.925 1.00 32.05  ? 3063 HIS A CB    1 
ATOM   14012 C  CG    . HIS A 1 3063 ? 162.563 136.864 194.884 1.00 38.97  ? 3063 HIS A CG    1 
ATOM   14013 N  ND1   . HIS A 1 3063 ? 163.339 136.745 196.016 1.00 42.62  ? 3063 HIS A ND1   1 
ATOM   14014 C  CD2   . HIS A 1 3063 ? 161.731 135.796 194.884 1.00 43.36  ? 3063 HIS A CD2   1 
ATOM   14015 C  CE1   . HIS A 1 3063 ? 162.998 135.649 196.667 1.00 47.44  ? 3063 HIS A CE1   1 
ATOM   14016 N  NE2   . HIS A 1 3063 ? 162.022 135.056 196.004 1.00 49.99  ? 3063 HIS A NE2   1 
ATOM   14017 N  N     . VAL A 1 3064 ? 162.654 138.972 190.690 1.00 39.75  ? 3064 VAL A N     1 
ATOM   14018 C  CA    . VAL A 1 3064 ? 162.751 140.059 189.724 1.00 36.83  ? 3064 VAL A CA    1 
ATOM   14019 C  C     . VAL A 1 3064 ? 161.657 141.069 190.026 1.00 42.01  ? 3064 VAL A C     1 
ATOM   14020 O  O     . VAL A 1 3064 ? 160.480 140.705 190.131 1.00 47.33  ? 3064 VAL A O     1 
ATOM   14021 C  CB    . VAL A 1 3064 ? 162.636 139.540 188.282 1.00 34.27  ? 3064 VAL A CB    1 
ATOM   14022 C  CG1   . VAL A 1 3064 ? 162.874 140.665 187.296 1.00 37.44  ? 3064 VAL A CG1   1 
ATOM   14023 C  CG2   . VAL A 1 3064 ? 163.617 138.410 188.057 1.00 42.51  ? 3064 VAL A CG2   1 
ATOM   14024 N  N     . VAL A 1 3065 ? 162.042 142.332 190.170 1.00 39.58  ? 3065 VAL A N     1 
ATOM   14025 C  CA    . VAL A 1 3065 ? 161.110 143.416 190.451 1.00 37.13  ? 3065 VAL A CA    1 
ATOM   14026 C  C     . VAL A 1 3065 ? 161.111 144.358 189.258 1.00 40.30  ? 3065 VAL A C     1 
ATOM   14027 O  O     . VAL A 1 3065 ? 162.081 145.092 189.036 1.00 50.93  ? 3065 VAL A O     1 
ATOM   14028 C  CB    . VAL A 1 3065 ? 161.476 144.162 191.742 1.00 35.21  ? 3065 VAL A CB    1 
ATOM   14029 C  CG1   . VAL A 1 3065 ? 160.410 145.189 192.077 1.00 38.18  ? 3065 VAL A CG1   1 
ATOM   14030 C  CG2   . VAL A 1 3065 ? 161.659 143.180 192.884 1.00 33.78  ? 3065 VAL A CG2   1 
ATOM   14031 N  N     . PHE A 1 3066 ? 160.028 144.339 188.493 1.00 37.66  ? 3066 PHE A N     1 
ATOM   14032 C  CA    . PHE A 1 3066 ? 159.830 145.247 187.375 1.00 41.21  ? 3066 PHE A CA    1 
ATOM   14033 C  C     . PHE A 1 3066 ? 159.068 146.463 187.880 1.00 46.29  ? 3066 PHE A C     1 
ATOM   14034 O  O     . PHE A 1 3066 ? 158.190 146.332 188.736 1.00 52.29  ? 3066 PHE A O     1 
ATOM   14035 C  CB    . PHE A 1 3066 ? 159.046 144.566 186.257 1.00 44.42  ? 3066 PHE A CB    1 
ATOM   14036 C  CG    . PHE A 1 3066 ? 159.843 143.595 185.447 1.00 52.92  ? 3066 PHE A CG    1 
ATOM   14037 C  CD1   . PHE A 1 3066 ? 160.793 144.036 184.548 1.00 61.94  ? 3066 PHE A CD1   1 
ATOM   14038 C  CD2   . PHE A 1 3066 ? 159.633 142.235 185.581 1.00 45.73  ? 3066 PHE A CD2   1 
ATOM   14039 C  CE1   . PHE A 1 3066 ? 161.516 143.139 183.797 1.00 68.30  ? 3066 PHE A CE1   1 
ATOM   14040 C  CE2   . PHE A 1 3066 ? 160.358 141.335 184.837 1.00 48.35  ? 3066 PHE A CE2   1 
ATOM   14041 C  CZ    . PHE A 1 3066 ? 161.301 141.787 183.943 1.00 60.96  ? 3066 PHE A CZ    1 
ATOM   14042 N  N     . THR A 1 3067 ? 159.409 147.636 187.363 1.00 50.59  ? 3067 THR A N     1 
ATOM   14043 C  CA    . THR A 1 3067 ? 158.787 148.891 187.770 1.00 46.73  ? 3067 THR A CA    1 
ATOM   14044 C  C     . THR A 1 3067 ? 158.373 149.645 186.514 1.00 54.67  ? 3067 THR A C     1 
ATOM   14045 O  O     . THR A 1 3067 ? 159.226 150.008 185.697 1.00 70.04  ? 3067 THR A O     1 
ATOM   14046 C  CB    . THR A 1 3067 ? 159.748 149.722 188.619 1.00 51.53  ? 3067 THR A CB    1 
ATOM   14047 O  OG1   . THR A 1 3067 ? 160.081 149.007 189.815 1.00 45.62  ? 3067 THR A OG1   1 
ATOM   14048 C  CG2   . THR A 1 3067 ? 159.124 151.052 188.986 1.00 49.11  ? 3067 THR A CG2   1 
ATOM   14049 N  N     . MET A 1 3068 ? 157.072 149.876 186.350 1.00 49.44  ? 3068 MET A N     1 
ATOM   14050 C  CA    . MET A 1 3068 ? 156.580 150.571 185.170 1.00 51.93  ? 3068 MET A CA    1 
ATOM   14051 C  C     . MET A 1 3068 ? 155.374 151.439 185.501 1.00 49.11  ? 3068 MET A C     1 
ATOM   14052 O  O     . MET A 1 3068 ? 154.737 151.291 186.549 1.00 47.44  ? 3068 MET A O     1 
ATOM   14053 C  CB    . MET A 1 3068 ? 156.225 149.590 184.044 1.00 48.74  ? 3068 MET A CB    1 
ATOM   14054 C  CG    . MET A 1 3068 ? 155.074 148.657 184.349 1.00 53.23  ? 3068 MET A CG    1 
ATOM   14055 S  SD    . MET A 1 3068 ? 154.722 147.561 182.964 1.00 79.19  ? 3068 MET A SD    1 
ATOM   14056 C  CE    . MET A 1 3068 ? 153.983 148.709 181.805 1.00 60.37  ? 3068 MET A CE    1 
ATOM   14057 N  N     . ASN A 1 3069 ? 155.075 152.360 184.586 1.00 49.95  ? 3069 ASN A N     1 
ATOM   14058 C  CA    . ASN A 1 3069 ? 154.007 153.341 184.573 1.00 49.41  ? 3069 ASN A CA    1 
ATOM   14059 C  C     . ASN A 1 3069 ? 152.908 152.925 183.602 1.00 52.96  ? 3069 ASN A C     1 
ATOM   14060 O  O     . ASN A 1 3069 ? 153.180 152.273 182.590 1.00 57.36  ? 3069 ASN A O     1 
ATOM   14061 C  CB    . ASN A 1 3069 ? 154.548 154.716 184.171 1.00 50.82  ? 3069 ASN A CB    1 
ATOM   14062 C  CG    . ASN A 1 3069 ? 155.567 155.249 185.155 1.00 55.45  ? 3069 ASN A CG    1 
ATOM   14063 O  OD1   . ASN A 1 3069 ? 156.714 155.510 184.798 1.00 57.11  ? 3069 ASN A OD1   1 
ATOM   14064 N  ND2   . ASN A 1 3069 ? 155.153 155.412 186.404 1.00 54.20  ? 3069 ASN A ND2   1 
ATOM   14065 N  N     . PRO A 1 3070 ? 151.646 153.286 183.877 1.00 50.25  ? 3070 PRO A N     1 
ATOM   14066 C  CA    . PRO A 1 3070 ? 150.543 152.923 182.985 1.00 54.24  ? 3070 PRO A CA    1 
ATOM   14067 C  C     . PRO A 1 3070 ? 150.485 153.799 181.738 1.00 58.64  ? 3070 PRO A C     1 
ATOM   14068 O  O     . PRO A 1 3070 ? 151.442 153.804 180.963 1.00 60.42  ? 3070 PRO A O     1 
ATOM   14069 C  CB    . PRO A 1 3070 ? 149.310 153.141 183.859 1.00 56.36  ? 3070 PRO A CB    1 
ATOM   14070 C  CG    . PRO A 1 3070 ? 149.707 154.241 184.773 1.00 52.39  ? 3070 PRO A CG    1 
ATOM   14071 C  CD    . PRO A 1 3070 ? 151.178 154.059 185.041 1.00 49.12  ? 3070 PRO A CD    1 
ATOM   14072 N  N     . ALA A 1 3080 ? 151.933 147.618 174.501 1.00 74.75  ? 3080 ALA A N     1 
ATOM   14073 C  CA    . ALA A 1 3080 ? 153.372 147.738 174.703 1.00 75.20  ? 3080 ALA A CA    1 
ATOM   14074 C  C     . ALA A 1 3080 ? 153.925 146.505 175.405 1.00 73.30  ? 3080 ALA A C     1 
ATOM   14075 O  O     . ALA A 1 3080 ? 154.529 145.639 174.773 1.00 78.22  ? 3080 ALA A O     1 
ATOM   14076 C  CB    . ALA A 1 3080 ? 153.693 148.992 175.500 1.00 67.97  ? 3080 ALA A CB    1 
ATOM   14077 N  N     . THR A 1 3081 ? 153.721 146.434 176.718 1.00 65.44  ? 3081 THR A N     1 
ATOM   14078 C  CA    . THR A 1 3081 ? 154.185 145.286 177.482 1.00 62.02  ? 3081 THR A CA    1 
ATOM   14079 C  C     . THR A 1 3081 ? 153.348 144.059 177.145 1.00 61.21  ? 3081 THR A C     1 
ATOM   14080 O  O     . THR A 1 3081 ? 152.115 144.101 177.172 1.00 61.14  ? 3081 THR A O     1 
ATOM   14081 C  CB    . THR A 1 3081 ? 154.120 145.580 178.980 1.00 67.06  ? 3081 THR A CB    1 
ATOM   14082 O  OG1   . THR A 1 3081 ? 155.120 146.547 179.321 1.00 74.31  ? 3081 THR A OG1   1 
ATOM   14083 C  CG2   . THR A 1 3081 ? 154.361 144.315 179.786 1.00 58.35  ? 3081 THR A CG2   1 
ATOM   14084 N  N     . SER A 1 3082 ? 154.029 142.964 176.824 1.00 61.37  ? 3082 SER A N     1 
ATOM   14085 C  CA    . SER A 1 3082 ? 153.338 141.758 176.398 1.00 59.39  ? 3082 SER A CA    1 
ATOM   14086 C  C     . SER A 1 3082 ? 152.519 141.178 177.548 1.00 53.18  ? 3082 SER A C     1 
ATOM   14087 O  O     . SER A 1 3082 ? 152.953 141.218 178.703 1.00 49.06  ? 3082 SER A O     1 
ATOM   14088 C  CB    . SER A 1 3082 ? 154.339 140.722 175.891 1.00 55.16  ? 3082 SER A CB    1 
ATOM   14089 O  OG    . SER A 1 3082 ? 155.210 140.304 176.927 1.00 53.44  ? 3082 SER A OG    1 
ATOM   14090 N  N     . PRO A 1 3083 ? 151.327 140.646 177.267 1.00 49.82  ? 3083 PRO A N     1 
ATOM   14091 C  CA    . PRO A 1 3083 ? 150.527 140.037 178.341 1.00 45.39  ? 3083 PRO A CA    1 
ATOM   14092 C  C     . PRO A 1 3083 ? 151.193 138.832 178.979 1.00 44.65  ? 3083 PRO A C     1 
ATOM   14093 O  O     . PRO A 1 3083 ? 150.851 138.474 180.113 1.00 46.94  ? 3083 PRO A O     1 
ATOM   14094 C  CB    . PRO A 1 3083 ? 149.222 139.654 177.630 1.00 47.73  ? 3083 PRO A CB    1 
ATOM   14095 C  CG    . PRO A 1 3083 ? 149.572 139.593 176.183 1.00 51.08  ? 3083 PRO A CG    1 
ATOM   14096 C  CD    . PRO A 1 3083 ? 150.626 140.629 175.974 1.00 55.89  ? 3083 PRO A CD    1 
ATOM   14097 N  N     . ALA A 1 3084 ? 152.132 138.189 178.283 1.00 47.04  ? 3084 ALA A N     1 
ATOM   14098 C  CA    . ALA A 1 3084 ? 152.885 137.099 178.893 1.00 42.02  ? 3084 ALA A CA    1 
ATOM   14099 C  C     . ALA A 1 3084 ? 153.717 137.598 180.066 1.00 44.80  ? 3084 ALA A C     1 
ATOM   14100 O  O     . ALA A 1 3084 ? 153.801 136.934 181.106 1.00 48.52  ? 3084 ALA A O     1 
ATOM   14101 C  CB    . ALA A 1 3084 ? 153.773 136.427 177.847 1.00 40.34  ? 3084 ALA A CB    1 
ATOM   14102 N  N     . LEU A 1 3085 ? 154.341 138.768 179.916 1.00 46.18  ? 3085 LEU A N     1 
ATOM   14103 C  CA    . LEU A 1 3085 ? 155.087 139.357 181.023 1.00 43.98  ? 3085 LEU A CA    1 
ATOM   14104 C  C     . LEU A 1 3085 ? 154.163 139.725 182.175 1.00 40.66  ? 3085 LEU A C     1 
ATOM   14105 O  O     . LEU A 1 3085 ? 154.518 139.543 183.344 1.00 45.73  ? 3085 LEU A O     1 
ATOM   14106 C  CB    . LEU A 1 3085 ? 155.865 140.579 180.539 1.00 48.38  ? 3085 LEU A CB    1 
ATOM   14107 C  CG    . LEU A 1 3085 ? 157.023 141.063 181.414 1.00 50.07  ? 3085 LEU A CG    1 
ATOM   14108 C  CD1   . LEU A 1 3085 ? 158.093 141.676 180.542 1.00 65.54  ? 3085 LEU A CD1   1 
ATOM   14109 C  CD2   . LEU A 1 3085 ? 156.553 142.073 182.447 1.00 53.35  ? 3085 LEU A CD2   1 
ATOM   14110 N  N     . PHE A 1 3086 ? 152.976 140.252 181.865 1.00 36.65  ? 3086 PHE A N     1 
ATOM   14111 C  CA    . PHE A 1 3086 ? 152.005 140.551 182.912 1.00 34.07  ? 3086 PHE A CA    1 
ATOM   14112 C  C     . PHE A 1 3086 ? 151.613 139.290 183.666 1.00 34.79  ? 3086 PHE A C     1 
ATOM   14113 O  O     . PHE A 1 3086 ? 151.452 139.312 184.891 1.00 41.18  ? 3086 PHE A O     1 
ATOM   14114 C  CB    . PHE A 1 3086 ? 150.762 141.206 182.310 1.00 34.89  ? 3086 PHE A CB    1 
ATOM   14115 C  CG    . PHE A 1 3086 ? 150.934 142.659 181.988 1.00 41.70  ? 3086 PHE A CG    1 
ATOM   14116 C  CD1   . PHE A 1 3086 ? 151.337 143.553 182.959 1.00 39.99  ? 3086 PHE A CD1   1 
ATOM   14117 C  CD2   . PHE A 1 3086 ? 150.676 143.132 180.716 1.00 47.84  ? 3086 PHE A CD2   1 
ATOM   14118 C  CE1   . PHE A 1 3086 ? 151.494 144.891 182.665 1.00 41.93  ? 3086 PHE A CE1   1 
ATOM   14119 C  CE2   . PHE A 1 3086 ? 150.829 144.469 180.417 1.00 47.15  ? 3086 PHE A CE2   1 
ATOM   14120 C  CZ    . PHE A 1 3086 ? 151.238 145.349 181.394 1.00 44.15  ? 3086 PHE A CZ    1 
ATOM   14121 N  N     . ASN A 1 3087 ? 151.448 138.181 182.947 1.00 35.84  ? 3087 ASN A N     1 
ATOM   14122 C  CA    . ASN A 1 3087 ? 150.977 136.952 183.569 1.00 34.89  ? 3087 ASN A CA    1 
ATOM   14123 C  C     . ASN A 1 3087 ? 152.089 136.220 184.312 1.00 33.64  ? 3087 ASN A C     1 
ATOM   14124 O  O     . ASN A 1 3087 ? 151.805 135.420 185.210 1.00 34.33  ? 3087 ASN A O     1 
ATOM   14125 C  CB    . ASN A 1 3087 ? 150.352 136.050 182.506 1.00 33.76  ? 3087 ASN A CB    1 
ATOM   14126 C  CG    . ASN A 1 3087 ? 149.365 135.069 183.086 1.00 41.84  ? 3087 ASN A CG    1 
ATOM   14127 O  OD1   . ASN A 1 3087 ? 149.661 133.891 183.243 1.00 42.92  ? 3087 ASN A OD1   1 
ATOM   14128 N  ND2   . ASN A 1 3087 ? 148.179 135.557 183.420 1.00 44.22  ? 3087 ASN A ND2   1 
ATOM   14129 N  N     . ARG A 1 3088 ? 153.351 136.471 183.956 1.00 31.89  ? 3088 ARG A N     1 
ATOM   14130 C  CA    . ARG A 1 3088 ? 154.459 135.833 184.662 1.00 30.55  ? 3088 ARG A CA    1 
ATOM   14131 C  C     . ARG A 1 3088 ? 154.745 136.491 186.007 1.00 40.71  ? 3088 ARG A C     1 
ATOM   14132 O  O     . ARG A 1 3088 ? 155.285 135.840 186.908 1.00 40.14  ? 3088 ARG A O     1 
ATOM   14133 C  CB    . ARG A 1 3088 ? 155.713 135.847 183.793 1.00 32.02  ? 3088 ARG A CB    1 
ATOM   14134 C  CG    . ARG A 1 3088 ? 155.730 134.779 182.725 1.00 34.19  ? 3088 ARG A CG    1 
ATOM   14135 C  CD    . ARG A 1 3088 ? 156.902 134.962 181.787 1.00 40.56  ? 3088 ARG A CD    1 
ATOM   14136 N  NE    . ARG A 1 3088 ? 157.129 133.788 180.954 1.00 48.53  ? 3088 ARG A NE    1 
ATOM   14137 C  CZ    . ARG A 1 3088 ? 156.319 133.375 179.988 1.00 44.63  ? 3088 ARG A CZ    1 
ATOM   14138 N  NH1   . ARG A 1 3088 ? 155.212 134.030 179.685 1.00 43.26  ? 3088 ARG A NH1   1 
ATOM   14139 N  NH2   . ARG A 1 3088 ? 156.632 132.277 179.307 1.00 44.90  ? 3088 ARG A NH2   1 
ATOM   14140 N  N     . CYS A 1 3089 ? 154.407 137.766 186.161 1.00 42.46  ? 3089 CYS A N     1 
ATOM   14141 C  CA    . CYS A 1 3089 ? 154.715 138.519 187.368 1.00 29.18  ? 3089 CYS A CA    1 
ATOM   14142 C  C     . CYS A 1 3089 ? 153.453 138.770 188.180 1.00 31.06  ? 3089 CYS A C     1 
ATOM   14143 O  O     . CYS A 1 3089 ? 152.357 138.883 187.625 1.00 33.33  ? 3089 CYS A O     1 
ATOM   14144 C  CB    . CYS A 1 3089 ? 155.375 139.853 187.018 1.00 30.87  ? 3089 CYS A CB    1 
ATOM   14145 S  SG    . CYS A 1 3089 ? 156.857 139.712 186.002 1.00 50.09  ? 3089 CYS A SG    1 
ATOM   14146 N  N     . VAL A 1 3090 ? 153.612 138.852 189.497 1.00 33.64  ? 3090 VAL A N     1 
ATOM   14147 C  CA    . VAL A 1 3090 ? 152.515 139.246 190.372 1.00 34.84  ? 3090 VAL A CA    1 
ATOM   14148 C  C     . VAL A 1 3090 ? 152.339 140.754 190.276 1.00 35.54  ? 3090 VAL A C     1 
ATOM   14149 O  O     . VAL A 1 3090 ? 153.290 141.516 190.473 1.00 38.32  ? 3090 VAL A O     1 
ATOM   14150 C  CB    . VAL A 1 3090 ? 152.781 138.812 191.820 1.00 32.91  ? 3090 VAL A CB    1 
ATOM   14151 C  CG1   . VAL A 1 3090 ? 151.670 139.308 192.727 1.00 29.63  ? 3090 VAL A CG1   1 
ATOM   14152 C  CG2   . VAL A 1 3090 ? 152.911 137.305 191.906 1.00 40.48  ? 3090 VAL A CG2   1 
ATOM   14153 N  N     . LEU A 1 3091 ? 151.120 141.186 189.980 1.00 34.82  ? 3091 LEU A N     1 
ATOM   14154 C  CA    . LEU A 1 3091 ? 150.836 142.574 189.651 1.00 35.23  ? 3091 LEU A CA    1 
ATOM   14155 C  C     . LEU A 1 3091 ? 150.470 143.348 190.908 1.00 42.14  ? 3091 LEU A C     1 
ATOM   14156 O  O     . LEU A 1 3091 ? 149.616 142.909 191.684 1.00 51.82  ? 3091 LEU A O     1 
ATOM   14157 C  CB    . LEU A 1 3091 ? 149.697 142.649 188.636 1.00 38.46  ? 3091 LEU A CB    1 
ATOM   14158 C  CG    . LEU A 1 3091 ? 150.067 142.095 187.265 1.00 36.40  ? 3091 LEU A CG    1 
ATOM   14159 C  CD1   . LEU A 1 3091 ? 148.857 141.990 186.385 1.00 38.07  ? 3091 LEU A CD1   1 
ATOM   14160 C  CD2   . LEU A 1 3091 ? 151.076 142.996 186.632 1.00 33.12  ? 3091 LEU A CD2   1 
ATOM   14161 N  N     . ASN A 1 3092 ? 151.113 144.498 191.103 1.00 37.25  ? 3092 ASN A N     1 
ATOM   14162 C  CA    . ASN A 1 3092 ? 150.787 145.403 192.192 1.00 35.30  ? 3092 ASN A CA    1 
ATOM   14163 C  C     . ASN A 1 3092 ? 150.618 146.800 191.619 1.00 38.36  ? 3092 ASN A C     1 
ATOM   14164 O  O     . ASN A 1 3092 ? 151.348 147.195 190.706 1.00 39.86  ? 3092 ASN A O     1 
ATOM   14165 C  CB    . ASN A 1 3092 ? 151.869 145.390 193.271 1.00 36.04  ? 3092 ASN A CB    1 
ATOM   14166 C  CG    . ASN A 1 3092 ? 151.420 146.051 194.554 1.00 47.23  ? 3092 ASN A CG    1 
ATOM   14167 O  OD1   . ASN A 1 3092 ? 150.226 146.141 194.833 1.00 48.72  ? 3092 ASN A OD1   1 
ATOM   14168 N  ND2   . ASN A 1 3092 ? 152.377 146.518 195.346 1.00 45.90  ? 3092 ASN A ND2   1 
ATOM   14169 N  N     . TRP A 1 3093 ? 149.641 147.536 192.143 1.00 41.65  ? 3093 TRP A N     1 
ATOM   14170 C  CA    . TRP A 1 3093 ? 149.271 148.842 191.617 1.00 36.98  ? 3093 TRP A CA    1 
ATOM   14171 C  C     . TRP A 1 3093 ? 149.626 149.933 192.617 1.00 45.55  ? 3093 TRP A C     1 
ATOM   14172 O  O     . TRP A 1 3093 ? 149.195 149.890 193.773 1.00 54.47  ? 3093 TRP A O     1 
ATOM   14173 C  CB    . TRP A 1 3093 ? 147.778 148.899 191.290 1.00 33.48  ? 3093 TRP A CB    1 
ATOM   14174 C  CG    . TRP A 1 3093 ? 147.340 150.232 190.769 1.00 38.75  ? 3093 TRP A CG    1 
ATOM   14175 C  CD1   . TRP A 1 3093 ? 146.586 151.158 191.426 1.00 40.18  ? 3093 TRP A CD1   1 
ATOM   14176 C  CD2   . TRP A 1 3093 ? 147.633 150.793 189.485 1.00 37.93  ? 3093 TRP A CD2   1 
ATOM   14177 N  NE1   . TRP A 1 3093 ? 146.392 152.261 190.632 1.00 37.97  ? 3093 TRP A NE1   1 
ATOM   14178 C  CE2   . TRP A 1 3093 ? 147.025 152.061 189.434 1.00 36.13  ? 3093 TRP A CE2   1 
ATOM   14179 C  CE3   . TRP A 1 3093 ? 148.350 150.345 188.372 1.00 35.40  ? 3093 TRP A CE3   1 
ATOM   14180 C  CZ2   . TRP A 1 3093 ? 147.113 152.884 188.318 1.00 37.93  ? 3093 TRP A CZ2   1 
ATOM   14181 C  CZ3   . TRP A 1 3093 ? 148.435 151.164 187.266 1.00 32.54  ? 3093 TRP A CZ3   1 
ATOM   14182 C  CH2   . TRP A 1 3093 ? 147.820 152.418 187.246 1.00 38.70  ? 3093 TRP A CH2   1 
ATOM   14183 N  N     . PHE A 1 3094 ? 150.409 150.906 192.162 1.00 39.45  ? 3094 PHE A N     1 
ATOM   14184 C  CA    . PHE A 1 3094 ? 150.728 152.109 192.928 1.00 41.65  ? 3094 PHE A CA    1 
ATOM   14185 C  C     . PHE A 1 3094 ? 149.845 153.242 192.421 1.00 47.11  ? 3094 PHE A C     1 
ATOM   14186 O  O     . PHE A 1 3094 ? 150.140 153.861 191.397 1.00 48.56  ? 3094 PHE A O     1 
ATOM   14187 C  CB    . PHE A 1 3094 ? 152.201 152.478 192.793 1.00 44.70  ? 3094 PHE A CB    1 
ATOM   14188 C  CG    . PHE A 1 3094 ? 153.074 151.910 193.866 1.00 44.56  ? 3094 PHE A CG    1 
ATOM   14189 C  CD1   . PHE A 1 3094 ? 153.492 152.703 194.919 1.00 42.79  ? 3094 PHE A CD1   1 
ATOM   14190 C  CD2   . PHE A 1 3094 ? 153.499 150.597 193.813 1.00 43.87  ? 3094 PHE A CD2   1 
ATOM   14191 C  CE1   . PHE A 1 3094 ? 154.303 152.193 195.907 1.00 41.90  ? 3094 PHE A CE1   1 
ATOM   14192 C  CE2   . PHE A 1 3094 ? 154.313 150.083 194.798 1.00 47.66  ? 3094 PHE A CE2   1 
ATOM   14193 C  CZ    . PHE A 1 3094 ? 154.715 150.882 195.847 1.00 45.61  ? 3094 PHE A CZ    1 
ATOM   14194 N  N     . GLY A 1 3095 ? 148.767 153.520 193.139 1.00 42.49  ? 3095 GLY A N     1 
ATOM   14195 C  CA    . GLY A 1 3095 ? 147.943 154.655 192.799 1.00 44.46  ? 3095 GLY A CA    1 
ATOM   14196 C  C     . GLY A 1 3095 ? 148.540 155.957 193.292 1.00 46.98  ? 3095 GLY A C     1 
ATOM   14197 O  O     . GLY A 1 3095 ? 149.471 155.985 194.095 1.00 48.21  ? 3095 GLY A O     1 
ATOM   14198 N  N     . ASP A 1 3096 ? 147.993 157.058 192.787 1.00 46.17  ? 3096 ASP A N     1 
ATOM   14199 C  CA    . ASP A 1 3096 ? 148.364 158.363 193.310 1.00 44.28  ? 3096 ASP A CA    1 
ATOM   14200 C  C     . ASP A 1 3096 ? 147.947 158.457 194.772 1.00 47.84  ? 3096 ASP A C     1 
ATOM   14201 O  O     . ASP A 1 3096 ? 146.932 157.891 195.186 1.00 54.61  ? 3096 ASP A O     1 
ATOM   14202 C  CB    . ASP A 1 3096 ? 147.706 159.475 192.493 1.00 50.44  ? 3096 ASP A CB    1 
ATOM   14203 C  CG    . ASP A 1 3096 ? 148.399 160.814 192.661 1.00 61.74  ? 3096 ASP A CG    1 
ATOM   14204 O  OD1   . ASP A 1 3096 ? 148.451 161.327 193.799 1.00 54.93  ? 3096 ASP A OD1   1 
ATOM   14205 O  OD2   . ASP A 1 3096 ? 148.891 161.358 191.650 1.00 65.95  ? 3096 ASP A OD2   1 
ATOM   14206 N  N     . TRP A 1 3097 ? 148.755 159.160 195.563 1.00 40.60  ? 3097 TRP A N     1 
ATOM   14207 C  CA    . TRP A 1 3097 ? 148.514 159.227 196.999 1.00 35.26  ? 3097 TRP A CA    1 
ATOM   14208 C  C     . TRP A 1 3097 ? 147.137 159.808 197.286 1.00 35.77  ? 3097 TRP A C     1 
ATOM   14209 O  O     . TRP A 1 3097 ? 146.755 160.842 196.732 1.00 35.81  ? 3097 TRP A O     1 
ATOM   14210 C  CB    . TRP A 1 3097 ? 149.593 160.066 197.682 1.00 29.71  ? 3097 TRP A CB    1 
ATOM   14211 C  CG    . TRP A 1 3097 ? 150.974 159.507 197.561 1.00 34.91  ? 3097 TRP A CG    1 
ATOM   14212 C  CD1   . TRP A 1 3097 ? 151.342 158.355 196.935 1.00 38.23  ? 3097 TRP A CD1   1 
ATOM   14213 C  CD2   . TRP A 1 3097 ? 152.175 160.079 198.087 1.00 35.80  ? 3097 TRP A CD2   1 
ATOM   14214 N  NE1   . TRP A 1 3097 ? 152.699 158.174 197.036 1.00 34.17  ? 3097 TRP A NE1   1 
ATOM   14215 C  CE2   . TRP A 1 3097 ? 153.233 159.219 197.740 1.00 32.18  ? 3097 TRP A CE2   1 
ATOM   14216 C  CE3   . TRP A 1 3097 ? 152.459 161.235 198.818 1.00 35.53  ? 3097 TRP A CE3   1 
ATOM   14217 C  CZ2   . TRP A 1 3097 ? 154.552 159.480 198.096 1.00 33.14  ? 3097 TRP A CZ2   1 
ATOM   14218 C  CZ3   . TRP A 1 3097 ? 153.768 161.491 199.170 1.00 30.92  ? 3097 TRP A CZ3   1 
ATOM   14219 C  CH2   . TRP A 1 3097 ? 154.797 160.618 198.810 1.00 34.81  ? 3097 TRP A CH2   1 
ATOM   14220 N  N     . SER A 1 3098 ? 146.393 159.134 198.156 1.00 35.16  ? 3098 SER A N     1 
ATOM   14221 C  CA    . SER A 1 3098 ? 145.049 159.565 198.495 1.00 35.74  ? 3098 SER A CA    1 
ATOM   14222 C  C     . SER A 1 3098 ? 145.108 160.783 199.412 1.00 34.86  ? 3098 SER A C     1 
ATOM   14223 O  O     . SER A 1 3098 ? 146.178 161.256 199.799 1.00 38.92  ? 3098 SER A O     1 
ATOM   14224 C  CB    . SER A 1 3098 ? 144.275 158.420 199.143 1.00 41.74  ? 3098 SER A CB    1 
ATOM   14225 O  OG    . SER A 1 3098 ? 144.925 157.963 200.315 1.00 42.73  ? 3098 SER A OG    1 
ATOM   14226 N  N     . THR A 1 3099 ? 143.929 161.300 199.763 1.00 32.69  ? 3099 THR A N     1 
ATOM   14227 C  CA    . THR A 1 3099 ? 143.869 162.451 200.656 1.00 30.40  ? 3099 THR A CA    1 
ATOM   14228 C  C     . THR A 1 3099 ? 144.463 162.119 202.018 1.00 36.61  ? 3099 THR A C     1 
ATOM   14229 O  O     . THR A 1 3099 ? 145.158 162.946 202.619 1.00 44.56  ? 3099 THR A O     1 
ATOM   14230 C  CB    . THR A 1 3099 ? 142.425 162.927 200.801 1.00 35.28  ? 3099 THR A CB    1 
ATOM   14231 O  OG1   . THR A 1 3099 ? 141.904 163.271 199.512 1.00 44.46  ? 3099 THR A OG1   1 
ATOM   14232 C  CG2   . THR A 1 3099 ? 142.358 164.143 201.701 1.00 41.35  ? 3099 THR A CG2   1 
ATOM   14233 N  N     . GLU A 1 3100 ? 144.204 160.911 202.521 1.00 34.53  ? 3100 GLU A N     1 
ATOM   14234 C  CA    . GLU A 1 3100 ? 144.793 160.502 203.791 1.00 36.76  ? 3100 GLU A CA    1 
ATOM   14235 C  C     . GLU A 1 3100 ? 146.309 160.408 203.690 1.00 37.53  ? 3100 GLU A C     1 
ATOM   14236 O  O     . GLU A 1 3100 ? 147.025 160.813 204.612 1.00 43.00  ? 3100 GLU A O     1 
ATOM   14237 C  CB    . GLU A 1 3100 ? 144.202 159.169 204.241 1.00 47.36  ? 3100 GLU A CB    1 
ATOM   14238 C  CG    . GLU A 1 3100 ? 144.818 158.625 205.515 1.00 56.70  ? 3100 GLU A CG    1 
ATOM   14239 C  CD    . GLU A 1 3100 ? 144.348 157.222 205.835 1.00 73.37  ? 3100 GLU A CD    1 
ATOM   14240 O  OE1   . GLU A 1 3100 ? 143.134 157.038 206.063 1.00 77.95  ? 3100 GLU A OE1   1 
ATOM   14241 O  OE2   . GLU A 1 3100 ? 145.193 156.303 205.857 1.00 75.08  ? 3100 GLU A OE2   1 
ATOM   14242 N  N     . ALA A 1 3101 ? 146.818 159.869 202.580 1.00 36.54  ? 3101 ALA A N     1 
ATOM   14243 C  CA    . ALA A 1 3101 ? 148.262 159.786 202.394 1.00 33.24  ? 3101 ALA A CA    1 
ATOM   14244 C  C     . ALA A 1 3101 ? 148.890 161.170 202.335 1.00 33.74  ? 3101 ALA A C     1 
ATOM   14245 O  O     . ALA A 1 3101 ? 149.939 161.412 202.945 1.00 35.99  ? 3101 ALA A O     1 
ATOM   14246 C  CB    . ALA A 1 3101 ? 148.582 158.999 201.125 1.00 32.99  ? 3101 ALA A CB    1 
ATOM   14247 N  N     . LEU A 1 3102 ? 148.259 162.095 201.608 1.00 32.79  ? 3102 LEU A N     1 
ATOM   14248 C  CA    . LEU A 1 3102 ? 148.763 163.462 201.540 1.00 26.84  ? 3102 LEU A CA    1 
ATOM   14249 C  C     . LEU A 1 3102 ? 148.749 164.119 202.912 1.00 31.56  ? 3102 LEU A C     1 
ATOM   14250 O  O     . LEU A 1 3102 ? 149.700 164.815 203.284 1.00 34.53  ? 3102 LEU A O     1 
ATOM   14251 C  CB    . LEU A 1 3102 ? 147.932 164.278 200.553 1.00 20.71  ? 3102 LEU A CB    1 
ATOM   14252 C  CG    . LEU A 1 3102 ? 147.967 163.860 199.086 1.00 22.42  ? 3102 LEU A CG    1 
ATOM   14253 C  CD1   . LEU A 1 3102 ? 147.222 164.873 198.246 1.00 21.36  ? 3102 LEU A CD1   1 
ATOM   14254 C  CD2   . LEU A 1 3102 ? 149.394 163.704 198.603 1.00 24.37  ? 3102 LEU A CD2   1 
ATOM   14255 N  N     . TYR A 1 3103 ? 147.677 163.910 203.677 1.00 28.76  ? 3103 TYR A N     1 
ATOM   14256 C  CA    . TYR A 1 3103 ? 147.590 164.492 205.011 1.00 29.82  ? 3103 TYR A CA    1 
ATOM   14257 C  C     . TYR A 1 3103 ? 148.668 163.935 205.932 1.00 36.35  ? 3103 TYR A C     1 
ATOM   14258 O  O     . TYR A 1 3103 ? 149.288 164.682 206.696 1.00 39.84  ? 3103 TYR A O     1 
ATOM   14259 C  CB    . TYR A 1 3103 ? 146.205 164.236 205.598 1.00 33.42  ? 3103 TYR A CB    1 
ATOM   14260 C  CG    . TYR A 1 3103 ? 145.999 164.842 206.961 1.00 35.98  ? 3103 TYR A CG    1 
ATOM   14261 C  CD1   . TYR A 1 3103 ? 145.796 166.203 207.112 1.00 32.82  ? 3103 TYR A CD1   1 
ATOM   14262 C  CD2   . TYR A 1 3103 ? 146.019 164.053 208.099 1.00 42.10  ? 3103 TYR A CD2   1 
ATOM   14263 C  CE1   . TYR A 1 3103 ? 145.608 166.760 208.356 1.00 36.34  ? 3103 TYR A CE1   1 
ATOM   14264 C  CE2   . TYR A 1 3103 ? 145.831 164.600 209.345 1.00 42.38  ? 3103 TYR A CE2   1 
ATOM   14265 C  CZ    . TYR A 1 3103 ? 145.628 165.954 209.468 1.00 43.54  ? 3103 TYR A CZ    1 
ATOM   14266 O  OH    . TYR A 1 3103 ? 145.444 166.501 210.712 1.00 55.63  ? 3103 TYR A OH    1 
ATOM   14267 N  N     . GLN A 1 3104 ? 148.897 162.621 205.882 1.00 37.91  ? 3104 GLN A N     1 
ATOM   14268 C  CA    . GLN A 1 3104 ? 149.926 162.017 206.722 1.00 38.10  ? 3104 GLN A CA    1 
ATOM   14269 C  C     . GLN A 1 3104 ? 151.314 162.513 206.340 1.00 35.95  ? 3104 GLN A C     1 
ATOM   14270 O  O     . GLN A 1 3104 ? 152.137 162.810 207.214 1.00 41.64  ? 3104 GLN A O     1 
ATOM   14271 C  CB    . GLN A 1 3104 ? 149.857 160.494 206.624 1.00 40.74  ? 3104 GLN A CB    1 
ATOM   14272 C  CG    . GLN A 1 3104 ? 148.606 159.889 207.231 1.00 43.12  ? 3104 GLN A CG    1 
ATOM   14273 C  CD    . GLN A 1 3104 ? 148.854 158.516 207.814 1.00 59.56  ? 3104 GLN A CD    1 
ATOM   14274 O  OE1   . GLN A 1 3104 ? 149.988 158.161 208.133 1.00 63.19  ? 3104 GLN A OE1   1 
ATOM   14275 N  NE2   . GLN A 1 3104 ? 147.793 157.732 207.952 1.00 65.32  ? 3104 GLN A NE2   1 
ATOM   14276 N  N     . VAL A 1 3105 ? 151.592 162.609 205.037 1.00 29.46  ? 3105 VAL A N     1 
ATOM   14277 C  CA    . VAL A 1 3105 ? 152.887 163.111 204.588 1.00 31.50  ? 3105 VAL A CA    1 
ATOM   14278 C  C     . VAL A 1 3105 ? 153.080 164.555 205.030 1.00 33.49  ? 3105 VAL A C     1 
ATOM   14279 O  O     . VAL A 1 3105 ? 154.160 164.938 205.493 1.00 37.32  ? 3105 VAL A O     1 
ATOM   14280 C  CB    . VAL A 1 3105 ? 153.018 162.959 203.061 1.00 31.19  ? 3105 VAL A CB    1 
ATOM   14281 C  CG1   . VAL A 1 3105 ? 154.182 163.784 202.542 1.00 29.68  ? 3105 VAL A CG1   1 
ATOM   14282 C  CG2   . VAL A 1 3105 ? 153.193 161.502 202.692 1.00 32.82  ? 3105 VAL A CG2   1 
ATOM   14283 N  N     . GLY A 1 3106 ? 152.036 165.376 204.902 1.00 30.53  ? 3106 GLY A N     1 
ATOM   14284 C  CA    . GLY A 1 3106 ? 152.134 166.752 205.353 1.00 27.60  ? 3106 GLY A CA    1 
ATOM   14285 C  C     . GLY A 1 3106 ? 152.374 166.866 206.845 1.00 29.72  ? 3106 GLY A C     1 
ATOM   14286 O  O     . GLY A 1 3106 ? 153.223 167.641 207.287 1.00 36.07  ? 3106 GLY A O     1 
ATOM   14287 N  N     . LYS A 1 3107 ? 151.638 166.092 207.644 1.00 31.42  ? 3107 LYS A N     1 
ATOM   14288 C  CA    . LYS A 1 3107 ? 151.813 166.161 209.091 1.00 31.86  ? 3107 LYS A CA    1 
ATOM   14289 C  C     . LYS A 1 3107 ? 153.199 165.693 209.510 1.00 35.86  ? 3107 LYS A C     1 
ATOM   14290 O  O     . LYS A 1 3107 ? 153.807 166.275 210.414 1.00 38.67  ? 3107 LYS A O     1 
ATOM   14291 C  CB    . LYS A 1 3107 ? 150.739 165.339 209.800 1.00 33.44  ? 3107 LYS A CB    1 
ATOM   14292 C  CG    . LYS A 1 3107 ? 149.396 166.028 209.898 1.00 35.46  ? 3107 LYS A CG    1 
ATOM   14293 C  CD    . LYS A 1 3107 ? 148.642 165.566 211.131 1.00 45.17  ? 3107 LYS A CD    1 
ATOM   14294 C  CE    . LYS A 1 3107 ? 149.329 166.022 212.402 1.00 44.84  ? 3107 LYS A CE    1 
ATOM   14295 N  NZ    . LYS A 1 3107 ? 149.422 167.503 212.469 1.00 46.40  ? 3107 LYS A NZ    1 
ATOM   14296 N  N     . GLU A 1 3108 ? 153.715 164.637 208.877 1.00 36.86  ? 3108 GLU A N     1 
ATOM   14297 C  CA    . GLU A 1 3108 ? 155.036 164.146 209.248 1.00 40.79  ? 3108 GLU A CA    1 
ATOM   14298 C  C     . GLU A 1 3108 ? 156.132 165.107 208.807 1.00 43.94  ? 3108 GLU A C     1 
ATOM   14299 O  O     . GLU A 1 3108 ? 157.092 165.345 209.549 1.00 48.84  ? 3108 GLU A O     1 
ATOM   14300 C  CB    . GLU A 1 3108 ? 155.267 162.758 208.654 1.00 45.80  ? 3108 GLU A CB    1 
ATOM   14301 C  CG    . GLU A 1 3108 ? 156.610 162.151 209.018 1.00 55.68  ? 3108 GLU A CG    1 
ATOM   14302 C  CD    . GLU A 1 3108 ? 156.579 161.426 210.348 1.00 70.71  ? 3108 GLU A CD    1 
ATOM   14303 O  OE1   . GLU A 1 3108 ? 157.467 161.681 211.188 1.00 71.00  ? 3108 GLU A OE1   1 
ATOM   14304 O  OE2   . GLU A 1 3108 ? 155.665 160.600 210.554 1.00 73.98  ? 3108 GLU A OE2   1 
ATOM   14305 N  N     . PHE A 1 3109 ? 156.007 165.675 207.607 1.00 38.71  ? 3109 PHE A N     1 
ATOM   14306 C  CA    . PHE A 1 3109 ? 157.051 166.535 207.068 1.00 36.02  ? 3109 PHE A CA    1 
ATOM   14307 C  C     . PHE A 1 3109 ? 156.967 167.969 207.575 1.00 37.64  ? 3109 PHE A C     1 
ATOM   14308 O  O     . PHE A 1 3109 ? 157.934 168.721 207.414 1.00 43.93  ? 3109 PHE A O     1 
ATOM   14309 C  CB    . PHE A 1 3109 ? 156.992 166.527 205.542 1.00 31.61  ? 3109 PHE A CB    1 
ATOM   14310 C  CG    . PHE A 1 3109 ? 157.757 165.404 204.908 1.00 38.50  ? 3109 PHE A CG    1 
ATOM   14311 C  CD1   . PHE A 1 3109 ? 158.179 164.322 205.659 1.00 44.14  ? 3109 PHE A CD1   1 
ATOM   14312 C  CD2   . PHE A 1 3109 ? 158.044 165.425 203.557 1.00 43.67  ? 3109 PHE A CD2   1 
ATOM   14313 C  CE1   . PHE A 1 3109 ? 158.880 163.290 205.075 1.00 47.01  ? 3109 PHE A CE1   1 
ATOM   14314 C  CE2   . PHE A 1 3109 ? 158.743 164.394 202.968 1.00 49.25  ? 3109 PHE A CE2   1 
ATOM   14315 C  CZ    . PHE A 1 3109 ? 159.161 163.325 203.728 1.00 47.72  ? 3109 PHE A CZ    1 
ATOM   14316 N  N     . THR A 1 3110 ? 155.847 168.368 208.172 1.00 35.80  ? 3110 THR A N     1 
ATOM   14317 C  CA    . THR A 1 3110 ? 155.690 169.694 208.760 1.00 35.59  ? 3110 THR A CA    1 
ATOM   14318 C  C     . THR A 1 3110 ? 155.619 169.610 210.280 1.00 44.80  ? 3110 THR A C     1 
ATOM   14319 O  O     . THR A 1 3110 ? 154.970 170.426 210.935 1.00 51.78  ? 3110 THR A O     1 
ATOM   14320 C  CB    . THR A 1 3110 ? 154.449 170.399 208.218 1.00 33.95  ? 3110 THR A CB    1 
ATOM   14321 O  OG1   . THR A 1 3110 ? 153.279 169.676 208.614 1.00 38.48  ? 3110 THR A OG1   1 
ATOM   14322 C  CG2   . THR A 1 3110 ? 154.493 170.473 206.703 1.00 31.65  ? 3110 THR A CG2   1 
ATOM   14323 N  N     . SER A 1 3111 ? 156.281 168.609 210.858 1.00 45.00  ? 3111 SER A N     1 
ATOM   14324 C  CA    . SER A 1 3111 ? 156.275 168.430 212.303 1.00 52.69  ? 3111 SER A CA    1 
ATOM   14325 C  C     . SER A 1 3111 ? 157.346 169.254 213.000 1.00 58.62  ? 3111 SER A C     1 
ATOM   14326 O  O     . SER A 1 3111 ? 157.171 169.626 214.165 1.00 58.67  ? 3111 SER A O     1 
ATOM   14327 C  CB    . SER A 1 3111 ? 156.456 166.952 212.653 1.00 54.58  ? 3111 SER A CB    1 
ATOM   14328 O  OG    . SER A 1 3111 ? 157.596 166.414 212.007 1.00 60.11  ? 3111 SER A OG    1 
ATOM   14329 N  N     . LYS A 1 3112 ? 158.452 169.547 212.315 1.00 58.13  ? 3112 LYS A N     1 
ATOM   14330 C  CA    . LYS A 1 3112 ? 159.484 170.393 212.901 1.00 61.67  ? 3112 LYS A CA    1 
ATOM   14331 C  C     . LYS A 1 3112 ? 159.095 171.865 212.869 1.00 62.52  ? 3112 LYS A C     1 
ATOM   14332 O  O     . LYS A 1 3112 ? 159.682 172.672 213.597 1.00 59.26  ? 3112 LYS A O     1 
ATOM   14333 C  CB    . LYS A 1 3112 ? 160.814 170.187 212.173 1.00 64.05  ? 3112 LYS A CB    1 
ATOM   14334 C  CG    . LYS A 1 3112 ? 161.647 169.029 212.704 1.00 65.19  ? 3112 LYS A CG    1 
ATOM   14335 C  CD    . LYS A 1 3112 ? 161.105 167.688 212.239 1.00 65.42  ? 3112 LYS A CD    1 
ATOM   14336 C  CE    . LYS A 1 3112 ? 161.249 167.531 210.733 1.00 70.63  ? 3112 LYS A CE    1 
ATOM   14337 N  NZ    . LYS A 1 3112 ? 160.788 166.197 210.260 1.00 64.22  ? 3112 LYS A NZ    1 
ATOM   14338 N  N     . MET A 1 3113 ? 158.120 172.226 212.041 1.00 58.81  ? 3113 MET A N     1 
ATOM   14339 C  CA    . MET A 1 3113 ? 157.659 173.603 211.964 1.00 50.14  ? 3113 MET A CA    1 
ATOM   14340 C  C     . MET A 1 3113 ? 156.957 173.997 213.256 1.00 56.85  ? 3113 MET A C     1 
ATOM   14341 O  O     . MET A 1 3113 ? 156.468 173.147 214.005 1.00 61.53  ? 3113 MET A O     1 
ATOM   14342 C  CB    . MET A 1 3113 ? 156.690 173.778 210.802 1.00 41.15  ? 3113 MET A CB    1 
ATOM   14343 C  CG    . MET A 1 3113 ? 157.314 174.119 209.472 1.00 37.45  ? 3113 MET A CG    1 
ATOM   14344 S  SD    . MET A 1 3113 ? 156.011 174.224 208.237 1.00 56.40  ? 3113 MET A SD    1 
ATOM   14345 C  CE    . MET A 1 3113 ? 156.698 173.234 206.929 1.00 35.05  ? 3113 MET A CE    1 
ATOM   14346 N  N     . ASP A 1 3114 ? 156.914 175.301 213.523 1.00 56.14  ? 3114 ASP A N     1 
ATOM   14347 C  CA    . ASP A 1 3114 ? 156.139 175.788 214.656 1.00 58.31  ? 3114 ASP A CA    1 
ATOM   14348 C  C     . ASP A 1 3114 ? 154.658 175.502 214.433 1.00 62.98  ? 3114 ASP A C     1 
ATOM   14349 O  O     . ASP A 1 3114 ? 154.072 174.678 215.143 1.00 69.41  ? 3114 ASP A O     1 
ATOM   14350 C  CB    . ASP A 1 3114 ? 156.380 177.283 214.870 1.00 61.19  ? 3114 ASP A CB    1 
ATOM   14351 C  CG    . ASP A 1 3114 ? 155.818 177.783 216.186 1.00 74.10  ? 3114 ASP A CG    1 
ATOM   14352 O  OD1   . ASP A 1 3114 ? 154.582 177.757 216.363 1.00 73.01  ? 3114 ASP A OD1   1 
ATOM   14353 O  OD2   . ASP A 1 3114 ? 156.617 178.203 217.049 1.00 82.85  ? 3114 ASP A OD2   1 
ATOM   14354 N  N     . LEU A 1 3115 ? 154.064 176.160 213.432 1.00 54.37  ? 3115 LEU A N     1 
ATOM   14355 C  CA    . LEU A 1 3115 ? 152.684 175.916 212.991 1.00 50.50  ? 3115 LEU A CA    1 
ATOM   14356 C  C     . LEU A 1 3115 ? 151.719 175.729 214.158 1.00 57.03  ? 3115 LEU A C     1 
ATOM   14357 O  O     . LEU A 1 3115 ? 150.860 174.846 214.144 1.00 53.89  ? 3115 LEU A O     1 
ATOM   14358 C  CB    . LEU A 1 3115 ? 152.616 174.712 212.052 1.00 42.67  ? 3115 LEU A CB    1 
ATOM   14359 C  CG    . LEU A 1 3115 ? 153.310 174.827 210.700 1.00 35.87  ? 3115 LEU A CG    1 
ATOM   14360 C  CD1   . LEU A 1 3115 ? 152.841 173.714 209.788 1.00 32.28  ? 3115 LEU A CD1   1 
ATOM   14361 C  CD2   . LEU A 1 3115 ? 153.042 176.181 210.080 1.00 40.90  ? 3115 LEU A CD2   1 
ATOM   14362 N  N     . GLU A 1 3116 ? 151.851 176.569 215.180 1.00 64.04  ? 3116 GLU A N     1 
ATOM   14363 C  CA    . GLU A 1 3116 ? 151.018 176.449 216.373 1.00 67.81  ? 3116 GLU A CA    1 
ATOM   14364 C  C     . GLU A 1 3116 ? 150.631 177.842 216.845 1.00 73.26  ? 3116 GLU A C     1 
ATOM   14365 O  O     . GLU A 1 3116 ? 151.466 178.571 217.390 1.00 74.70  ? 3116 GLU A O     1 
ATOM   14366 C  CB    . GLU A 1 3116 ? 151.743 175.676 217.473 1.00 68.09  ? 3116 GLU A CB    1 
ATOM   14367 C  CG    . GLU A 1 3116 ? 151.344 174.213 217.547 1.00 72.45  ? 3116 GLU A CG    1 
ATOM   14368 C  CD    . GLU A 1 3116 ? 152.325 173.380 218.344 1.00 85.62  ? 3116 GLU A CD    1 
ATOM   14369 O  OE1   . GLU A 1 3116 ? 153.325 173.945 218.834 1.00 87.42  ? 3116 GLU A OE1   1 
ATOM   14370 O  OE2   . GLU A 1 3116 ? 152.099 172.159 218.478 1.00 89.64  ? 3116 GLU A OE2   1 
ATOM   14371 N  N     . LYS A 1 3117 ? 149.371 178.208 216.632 1.00 71.92  ? 3117 LYS A N     1 
ATOM   14372 C  CA    . LYS A 1 3117 ? 148.819 179.448 217.162 1.00 71.02  ? 3117 LYS A CA    1 
ATOM   14373 C  C     . LYS A 1 3117 ? 147.848 179.111 218.282 1.00 74.04  ? 3117 LYS A C     1 
ATOM   14374 O  O     . LYS A 1 3117 ? 146.774 178.551 218.011 1.00 74.18  ? 3117 LYS A O     1 
ATOM   14375 C  CB    . LYS A 1 3117 ? 148.114 180.248 216.066 1.00 70.71  ? 3117 LYS A CB    1 
ATOM   14376 C  CG    . LYS A 1 3117 ? 148.977 181.321 215.427 1.00 73.16  ? 3117 LYS A CG    1 
ATOM   14377 C  CD    . LYS A 1 3117 ? 148.274 181.964 214.245 1.00 72.52  ? 3117 LYS A CD    1 
ATOM   14378 C  CE    . LYS A 1 3117 ? 146.875 182.422 214.619 1.00 82.41  ? 3117 LYS A CE    1 
ATOM   14379 N  NZ    . LYS A 1 3117 ? 146.898 183.466 215.680 1.00 83.77  ? 3117 LYS A NZ    1 
ATOM   14380 N  N     . PRO A 1 3118 ? 148.177 179.406 219.541 1.00 77.54  ? 3118 PRO A N     1 
ATOM   14381 C  CA    . PRO A 1 3118 ? 147.236 179.105 220.631 1.00 76.16  ? 3118 PRO A CA    1 
ATOM   14382 C  C     . PRO A 1 3118 ? 145.904 179.819 220.494 1.00 76.90  ? 3118 PRO A C     1 
ATOM   14383 O  O     . PRO A 1 3118 ? 144.874 179.279 220.917 1.00 77.66  ? 3118 PRO A O     1 
ATOM   14384 C  CB    . PRO A 1 3118 ? 147.997 179.566 221.882 1.00 75.35  ? 3118 PRO A CB    1 
ATOM   14385 C  CG    . PRO A 1 3118 ? 149.436 179.504 221.490 1.00 76.13  ? 3118 PRO A CG    1 
ATOM   14386 C  CD    . PRO A 1 3118 ? 149.469 179.902 220.045 1.00 74.88  ? 3118 PRO A CD    1 
ATOM   14387 N  N     . ASN A 1 3119 ? 145.891 181.018 219.908 1.00 76.83  ? 3119 ASN A N     1 
ATOM   14388 C  CA    . ASN A 1 3119 ? 144.671 181.798 219.739 1.00 77.05  ? 3119 ASN A CA    1 
ATOM   14389 C  C     . ASN A 1 3119 ? 144.030 181.596 218.372 1.00 79.68  ? 3119 ASN A C     1 
ATOM   14390 O  O     . ASN A 1 3119 ? 143.419 182.527 217.833 1.00 84.87  ? 3119 ASN A O     1 
ATOM   14391 C  CB    . ASN A 1 3119 ? 144.958 183.281 219.981 1.00 82.67  ? 3119 ASN A CB    1 
ATOM   14392 C  CG    . ASN A 1 3119 ? 146.118 183.795 219.151 1.00 86.38  ? 3119 ASN A CG    1 
ATOM   14393 O  OD1   . ASN A 1 3119 ? 146.724 183.054 218.378 1.00 84.10  ? 3119 ASN A OD1   1 
ATOM   14394 N  ND2   . ASN A 1 3119 ? 146.435 185.074 219.311 1.00 81.25  ? 3119 ASN A ND2   1 
ATOM   14395 N  N     . TYR A 1 3120 ? 144.161 180.407 217.791 1.00 74.46  ? 3120 TYR A N     1 
ATOM   14396 C  CA    . TYR A 1 3120 ? 143.539 180.116 216.506 1.00 67.54  ? 3120 TYR A CA    1 
ATOM   14397 C  C     . TYR A 1 3120 ? 142.046 179.877 216.697 1.00 72.40  ? 3120 TYR A C     1 
ATOM   14398 O  O     . TYR A 1 3120 ? 141.644 178.904 217.343 1.00 76.35  ? 3120 TYR A O     1 
ATOM   14399 C  CB    . TYR A 1 3120 ? 144.202 178.898 215.869 1.00 62.36  ? 3120 TYR A CB    1 
ATOM   14400 C  CG    . TYR A 1 3120 ? 143.545 178.425 214.593 1.00 57.93  ? 3120 TYR A CG    1 
ATOM   14401 C  CD1   . TYR A 1 3120 ? 143.551 179.212 213.453 1.00 57.44  ? 3120 TYR A CD1   1 
ATOM   14402 C  CD2   . TYR A 1 3120 ? 142.919 177.190 214.531 1.00 59.88  ? 3120 TYR A CD2   1 
ATOM   14403 C  CE1   . TYR A 1 3120 ? 142.954 178.780 212.286 1.00 54.57  ? 3120 TYR A CE1   1 
ATOM   14404 C  CE2   . TYR A 1 3120 ? 142.319 176.751 213.370 1.00 59.19  ? 3120 TYR A CE2   1 
ATOM   14405 C  CZ    . TYR A 1 3120 ? 142.339 177.550 212.251 1.00 52.80  ? 3120 TYR A CZ    1 
ATOM   14406 O  OH    . TYR A 1 3120 ? 141.742 177.117 211.092 1.00 56.42  ? 3120 TYR A OH    1 
ATOM   14407 N  N     . ILE A 1 3121 ? 141.226 180.762 216.139 1.00 70.66  ? 3121 ILE A N     1 
ATOM   14408 C  CA    . ILE A 1 3121 ? 139.776 180.610 216.209 1.00 68.40  ? 3121 ILE A CA    1 
ATOM   14409 C  C     . ILE A 1 3121 ? 139.338 179.661 215.103 1.00 69.72  ? 3121 ILE A C     1 
ATOM   14410 O  O     . ILE A 1 3121 ? 139.575 179.921 213.919 1.00 71.05  ? 3121 ILE A O     1 
ATOM   14411 C  CB    . ILE A 1 3121 ? 139.060 181.964 216.087 1.00 72.05  ? 3121 ILE A CB    1 
ATOM   14412 C  CG1   . ILE A 1 3121 ? 139.416 182.891 217.254 1.00 74.47  ? 3121 ILE A CG1   1 
ATOM   14413 C  CG2   . ILE A 1 3121 ? 137.554 181.763 216.009 1.00 71.27  ? 3121 ILE A CG2   1 
ATOM   14414 C  CD1   . ILE A 1 3121 ? 140.621 183.772 217.012 1.00 69.41  ? 3121 ILE A CD1   1 
ATOM   14415 N  N     . VAL A 1 3122 ? 138.693 178.563 215.484 1.00 73.04  ? 3122 VAL A N     1 
ATOM   14416 C  CA    . VAL A 1 3122 ? 138.225 177.577 214.514 1.00 77.48  ? 3122 VAL A CA    1 
ATOM   14417 C  C     . VAL A 1 3122 ? 137.054 178.171 213.742 1.00 82.26  ? 3122 VAL A C     1 
ATOM   14418 O  O     . VAL A 1 3122 ? 136.034 178.535 214.346 1.00 86.22  ? 3122 VAL A O     1 
ATOM   14419 C  CB    . VAL A 1 3122 ? 137.827 176.262 215.199 1.00 81.54  ? 3122 VAL A CB    1 
ATOM   14420 C  CG1   . VAL A 1 3122 ? 137.339 175.259 214.169 1.00 77.76  ? 3122 VAL A CG1   1 
ATOM   14421 C  CG2   . VAL A 1 3122 ? 139.000 175.698 215.985 1.00 78.54  ? 3122 VAL A CG2   1 
ATOM   14422 N  N     . PRO A 1 3123 ? 137.152 178.290 212.421 1.00 79.42  ? 3123 PRO A N     1 
ATOM   14423 C  CA    . PRO A 1 3123 ? 136.040 178.857 211.651 1.00 82.84  ? 3123 PRO A CA    1 
ATOM   14424 C  C     . PRO A 1 3123 ? 134.853 177.911 211.598 1.00 94.57  ? 3123 PRO A C     1 
ATOM   14425 O  O     . PRO A 1 3123 ? 135.009 176.688 211.565 1.00 98.62  ? 3123 PRO A O     1 
ATOM   14426 C  CB    . PRO A 1 3123 ? 136.646 179.066 210.260 1.00 79.24  ? 3123 PRO A CB    1 
ATOM   14427 C  CG    . PRO A 1 3123 ? 137.736 178.061 210.181 1.00 75.66  ? 3123 PRO A CG    1 
ATOM   14428 C  CD    . PRO A 1 3123 ? 138.300 177.947 211.566 1.00 74.90  ? 3123 PRO A CD    1 
ATOM   14429 N  N     . ASP A 1 3124 ? 133.657 178.490 211.588 1.00 97.49  ? 3124 ASP A N     1 
ATOM   14430 C  CA    . ASP A 1 3124 ? 132.461 177.701 211.333 1.00 102.27 ? 3124 ASP A CA    1 
ATOM   14431 C  C     . ASP A 1 3124 ? 132.366 177.340 209.854 1.00 110.06 ? 3124 ASP A C     1 
ATOM   14432 O  O     . ASP A 1 3124 ? 132.688 178.144 208.976 1.00 111.31 ? 3124 ASP A O     1 
ATOM   14433 C  CB    . ASP A 1 3124 ? 131.213 178.448 211.823 1.00 108.88 ? 3124 ASP A CB    1 
ATOM   14434 C  CG    . ASP A 1 3124 ? 130.986 179.780 211.115 1.00 112.59 ? 3124 ASP A CG    1 
ATOM   14435 O  OD1   . ASP A 1 3124 ? 131.805 180.188 210.267 1.00 110.70 ? 3124 ASP A OD1   1 
ATOM   14436 O  OD2   . ASP A 1 3124 ? 129.967 180.434 211.423 1.00 113.10 ? 3124 ASP A OD2   1 
ATOM   14437 N  N     . TYR A 1 3125 ? 131.950 176.104 209.586 1.00 112.07 ? 3125 TYR A N     1 
ATOM   14438 C  CA    . TYR A 1 3125 ? 131.967 175.530 208.242 1.00 113.10 ? 3125 TYR A CA    1 
ATOM   14439 C  C     . TYR A 1 3125 ? 133.358 175.667 207.618 1.00 112.61 ? 3125 TYR A C     1 
ATOM   14440 O  O     . TYR A 1 3125 ? 133.569 176.369 206.628 1.00 112.86 ? 3125 TYR A O     1 
ATOM   14441 C  CB    . TYR A 1 3125 ? 130.889 176.161 207.354 1.00 113.60 ? 3125 TYR A CB    1 
ATOM   14442 C  CG    . TYR A 1 3125 ? 130.894 175.646 205.931 1.00 124.50 ? 3125 TYR A CG    1 
ATOM   14443 C  CD1   . TYR A 1 3125 ? 130.798 174.287 205.663 1.00 127.65 ? 3125 TYR A CD1   1 
ATOM   14444 C  CD2   . TYR A 1 3125 ? 131.008 176.519 204.856 1.00 127.02 ? 3125 TYR A CD2   1 
ATOM   14445 C  CE1   . TYR A 1 3125 ? 130.809 173.812 204.364 1.00 133.72 ? 3125 TYR A CE1   1 
ATOM   14446 C  CE2   . TYR A 1 3125 ? 131.019 176.054 203.555 1.00 131.74 ? 3125 TYR A CE2   1 
ATOM   14447 C  CZ    . TYR A 1 3125 ? 130.920 174.700 203.315 1.00 137.32 ? 3125 TYR A CZ    1 
ATOM   14448 O  OH    . TYR A 1 3125 ? 130.930 174.235 202.019 1.00 139.93 ? 3125 TYR A OH    1 
ATOM   14449 N  N     . MET A 1 3126 ? 134.320 175.005 208.244 1.00 104.98 ? 3126 MET A N     1 
ATOM   14450 C  CA    . MET A 1 3126 ? 135.680 175.018 207.723 1.00 95.19  ? 3126 MET A CA    1 
ATOM   14451 C  C     . MET A 1 3126 ? 135.750 174.211 206.433 1.00 93.15  ? 3126 MET A C     1 
ATOM   14452 O  O     . MET A 1 3126 ? 135.179 173.117 206.362 1.00 98.25  ? 3126 MET A O     1 
ATOM   14453 C  CB    . MET A 1 3126 ? 136.660 174.451 208.744 1.00 91.00  ? 3126 MET A CB    1 
ATOM   14454 C  CG    . MET A 1 3126 ? 138.092 174.900 208.517 1.00 87.09  ? 3126 MET A CG    1 
ATOM   14455 S  SD    . MET A 1 3126 ? 139.280 174.069 209.581 1.00 96.67  ? 3126 MET A SD    1 
ATOM   14456 C  CE    . MET A 1 3126 ? 140.717 174.045 208.515 1.00 67.68  ? 3126 MET A CE    1 
ATOM   14457 N  N     . PRO A 1 3127 ? 136.429 174.706 205.400 1.00 86.86  ? 3127 PRO A N     1 
ATOM   14458 C  CA    . PRO A 1 3127 ? 136.611 173.896 204.190 1.00 78.86  ? 3127 PRO A CA    1 
ATOM   14459 C  C     . PRO A 1 3127 ? 137.521 172.714 204.465 1.00 78.46  ? 3127 PRO A C     1 
ATOM   14460 O  O     . PRO A 1 3127 ? 138.719 172.887 204.711 1.00 84.96  ? 3127 PRO A O     1 
ATOM   14461 C  CB    . PRO A 1 3127 ? 137.238 174.881 203.197 1.00 76.24  ? 3127 PRO A CB    1 
ATOM   14462 C  CG    . PRO A 1 3127 ? 137.895 175.909 204.053 1.00 74.07  ? 3127 PRO A CG    1 
ATOM   14463 C  CD    . PRO A 1 3127 ? 137.040 176.039 205.276 1.00 79.77  ? 3127 PRO A CD    1 
ATOM   14464 N  N     . VAL A 1 3128 ? 136.966 171.507 204.431 1.00 76.39  ? 3128 VAL A N     1 
ATOM   14465 C  CA    . VAL A 1 3128 ? 137.680 170.302 204.829 1.00 73.62  ? 3128 VAL A CA    1 
ATOM   14466 C  C     . VAL A 1 3128 ? 137.857 169.410 203.606 1.00 68.91  ? 3128 VAL A C     1 
ATOM   14467 O  O     . VAL A 1 3128 ? 136.908 169.189 202.844 1.00 65.54  ? 3128 VAL A O     1 
ATOM   14468 C  CB    . VAL A 1 3128 ? 136.953 169.566 205.972 1.00 73.19  ? 3128 VAL A CB    1 
ATOM   14469 C  CG1   . VAL A 1 3128 ? 135.569 169.090 205.541 1.00 77.07  ? 3128 VAL A CG1   1 
ATOM   14470 C  CG2   . VAL A 1 3128 ? 137.792 168.410 206.478 1.00 69.29  ? 3128 VAL A CG2   1 
ATOM   14471 N  N     . VAL A 1 3129 ? 139.085 168.936 203.400 1.00 61.62  ? 3129 VAL A N     1 
ATOM   14472 C  CA    . VAL A 1 3129 ? 139.375 168.002 202.326 1.00 64.88  ? 3129 VAL A CA    1 
ATOM   14473 C  C     . VAL A 1 3129 ? 139.733 166.615 202.849 1.00 69.68  ? 3129 VAL A C     1 
ATOM   14474 O  O     . VAL A 1 3129 ? 139.533 165.628 202.132 1.00 69.08  ? 3129 VAL A O     1 
ATOM   14475 C  CB    . VAL A 1 3129 ? 140.491 168.544 201.409 1.00 54.90  ? 3129 VAL A CB    1 
ATOM   14476 C  CG1   . VAL A 1 3129 ? 140.048 169.835 200.747 1.00 54.77  ? 3129 VAL A CG1   1 
ATOM   14477 C  CG2   . VAL A 1 3129 ? 141.771 168.756 202.189 1.00 50.46  ? 3129 VAL A CG2   1 
ATOM   14478 N  N     . TYR A 1 3130 ? 140.246 166.510 204.072 1.00 63.33  ? 3130 TYR A N     1 
ATOM   14479 C  CA    . TYR A 1 3130 ? 140.520 165.229 204.712 1.00 62.80  ? 3130 TYR A CA    1 
ATOM   14480 C  C     . TYR A 1 3130 ? 139.339 164.898 205.617 1.00 73.01  ? 3130 TYR A C     1 
ATOM   14481 O  O     . TYR A 1 3130 ? 139.117 165.570 206.628 1.00 71.07  ? 3130 TYR A O     1 
ATOM   14482 C  CB    . TYR A 1 3130 ? 141.828 165.284 205.497 1.00 56.45  ? 3130 TYR A CB    1 
ATOM   14483 C  CG    . TYR A 1 3130 ? 142.183 163.991 206.193 1.00 58.62  ? 3130 TYR A CG    1 
ATOM   14484 C  CD1   . TYR A 1 3130 ? 142.147 162.783 205.515 1.00 58.66  ? 3130 TYR A CD1   1 
ATOM   14485 C  CD2   . TYR A 1 3130 ? 142.561 163.981 207.527 1.00 59.04  ? 3130 TYR A CD2   1 
ATOM   14486 C  CE1   . TYR A 1 3130 ? 142.471 161.602 206.149 1.00 60.35  ? 3130 TYR A CE1   1 
ATOM   14487 C  CE2   . TYR A 1 3130 ? 142.886 162.805 208.168 1.00 58.13  ? 3130 TYR A CE2   1 
ATOM   14488 C  CZ    . TYR A 1 3130 ? 142.843 161.620 207.474 1.00 63.22  ? 3130 TYR A CZ    1 
ATOM   14489 O  OH    . TYR A 1 3130 ? 143.169 160.445 208.110 1.00 68.61  ? 3130 TYR A OH    1 
ATOM   14490 N  N     . ASP A 1 3131 ? 138.586 163.858 205.252 1.00 77.14  ? 3131 ASP A N     1 
ATOM   14491 C  CA    . ASP A 1 3131 ? 137.341 163.557 205.955 1.00 76.12  ? 3131 ASP A CA    1 
ATOM   14492 C  C     . ASP A 1 3131 ? 137.584 163.195 207.416 1.00 78.56  ? 3131 ASP A C     1 
ATOM   14493 O  O     . ASP A 1 3131 ? 136.807 163.586 208.295 1.00 78.17  ? 3131 ASP A O     1 
ATOM   14494 C  CB    . ASP A 1 3131 ? 136.589 162.440 205.227 1.00 79.94  ? 3131 ASP A CB    1 
ATOM   14495 C  CG    . ASP A 1 3131 ? 137.363 161.132 205.186 1.00 87.34  ? 3131 ASP A CG    1 
ATOM   14496 O  OD1   . ASP A 1 3131 ? 138.509 161.086 205.681 1.00 82.19  ? 3131 ASP A OD1   1 
ATOM   14497 O  OD2   . ASP A 1 3131 ? 136.819 160.143 204.653 1.00 89.29  ? 3131 ASP A OD2   1 
ATOM   14498 N  N     . LYS A 1 3132 ? 138.653 162.452 207.699 1.00 75.41  ? 3132 LYS A N     1 
ATOM   14499 C  CA    . LYS A 1 3132 ? 138.959 162.016 209.054 1.00 75.61  ? 3132 LYS A CA    1 
ATOM   14500 C  C     . LYS A 1 3132 ? 139.775 163.040 209.837 1.00 75.50  ? 3132 LYS A C     1 
ATOM   14501 O  O     . LYS A 1 3132 ? 140.393 162.684 210.847 1.00 78.87  ? 3132 LYS A O     1 
ATOM   14502 C  CB    . LYS A 1 3132 ? 139.692 160.674 209.022 1.00 72.34  ? 3132 LYS A CB    1 
ATOM   14503 C  CG    . LYS A 1 3132 ? 138.843 159.519 208.519 1.00 69.95  ? 3132 LYS A CG    1 
ATOM   14504 C  CD    . LYS A 1 3132 ? 139.359 158.182 209.027 1.00 75.28  ? 3132 LYS A CD    1 
ATOM   14505 C  CE    . LYS A 1 3132 ? 140.878 158.125 209.011 1.00 75.95  ? 3132 LYS A CE    1 
ATOM   14506 N  NZ    . LYS A 1 3132 ? 141.378 156.753 208.718 1.00 79.93  ? 3132 LYS A NZ    1 
ATOM   14507 N  N     . LEU A 1 3133 ? 139.793 164.293 209.396 1.00 69.66  ? 3133 LEU A N     1 
ATOM   14508 C  CA    . LEU A 1 3133 ? 140.546 165.320 210.099 1.00 71.87  ? 3133 LEU A CA    1 
ATOM   14509 C  C     . LEU A 1 3133 ? 139.890 165.618 211.446 1.00 77.98  ? 3133 LEU A C     1 
ATOM   14510 O  O     . LEU A 1 3133 ? 138.663 165.728 211.528 1.00 80.71  ? 3133 LEU A O     1 
ATOM   14511 C  CB    . LEU A 1 3133 ? 140.634 166.585 209.242 1.00 73.14  ? 3133 LEU A CB    1 
ATOM   14512 C  CG    . LEU A 1 3133 ? 141.516 167.767 209.651 1.00 66.95  ? 3133 LEU A CG    1 
ATOM   14513 C  CD1   . LEU A 1 3133 ? 141.935 168.517 208.410 1.00 56.17  ? 3133 LEU A CD1   1 
ATOM   14514 C  CD2   . LEU A 1 3133 ? 140.787 168.710 210.582 1.00 67.56  ? 3133 LEU A CD2   1 
ATOM   14515 N  N     . PRO A 1 3134 ? 140.675 165.738 212.516 1.00 76.75  ? 3134 PRO A N     1 
ATOM   14516 C  CA    . PRO A 1 3134 ? 140.087 165.916 213.851 1.00 78.68  ? 3134 PRO A CA    1 
ATOM   14517 C  C     . PRO A 1 3134 ? 139.274 167.199 213.948 1.00 82.33  ? 3134 PRO A C     1 
ATOM   14518 O  O     . PRO A 1 3134 ? 139.696 168.261 213.490 1.00 84.42  ? 3134 PRO A O     1 
ATOM   14519 C  CB    . PRO A 1 3134 ? 141.312 165.954 214.773 1.00 73.20  ? 3134 PRO A CB    1 
ATOM   14520 C  CG    . PRO A 1 3134 ? 142.386 165.256 214.008 1.00 73.20  ? 3134 PRO A CG    1 
ATOM   14521 C  CD    . PRO A 1 3134 ? 142.139 165.590 212.571 1.00 70.48  ? 3134 PRO A CD    1 
ATOM   14522 N  N     . GLN A 1 3135 ? 138.100 167.092 214.569 1.00 86.60  ? 3135 GLN A N     1 
ATOM   14523 C  CA    . GLN A 1 3135 ? 137.210 168.228 214.761 1.00 89.64  ? 3135 GLN A CA    1 
ATOM   14524 C  C     . GLN A 1 3135 ? 136.992 168.454 216.248 1.00 95.15  ? 3135 GLN A C     1 
ATOM   14525 O  O     . GLN A 1 3135 ? 136.536 167.534 216.944 1.00 97.10  ? 3135 GLN A O     1 
ATOM   14526 C  CB    . GLN A 1 3135 ? 135.875 167.996 214.055 1.00 88.20  ? 3135 GLN A CB    1 
ATOM   14527 C  CG    . GLN A 1 3135 ? 136.011 167.458 212.640 1.00 87.31  ? 3135 GLN A CG    1 
ATOM   14528 C  CD    . GLN A 1 3135 ? 136.006 168.558 211.596 1.00 89.35  ? 3135 GLN A CD    1 
ATOM   14529 O  OE1   . GLN A 1 3135 ? 135.890 169.739 211.921 1.00 90.35  ? 3135 GLN A OE1   1 
ATOM   14530 N  NE2   . GLN A 1 3135 ? 136.138 168.173 210.332 1.00 85.01  ? 3135 GLN A NE2   1 
ATOM   14531 N  N     . PRO A 1 3136 ? 137.293 169.644 216.784 1.00 94.97  ? 3136 PRO A N     1 
ATOM   14532 C  CA    . PRO A 1 3136 ? 137.799 170.837 216.094 1.00 87.49  ? 3136 PRO A CA    1 
ATOM   14533 C  C     . PRO A 1 3136 ? 139.288 170.746 215.781 1.00 83.35  ? 3136 PRO A C     1 
ATOM   14534 O  O     . PRO A 1 3136 ? 140.066 170.201 216.559 1.00 81.86  ? 3136 PRO A O     1 
ATOM   14535 C  CB    . PRO A 1 3136 ? 137.489 171.955 217.094 1.00 86.45  ? 3136 PRO A CB    1 
ATOM   14536 C  CG    . PRO A 1 3136 ? 137.649 171.291 218.433 1.00 86.31  ? 3136 PRO A CG    1 
ATOM   14537 C  CD    . PRO A 1 3136 ? 137.203 169.856 218.240 1.00 91.65  ? 3136 PRO A CD    1 
ATOM   14538 N  N     . PRO A 1 3137 ? 139.705 171.275 214.637 1.00 80.80  ? 3137 PRO A N     1 
ATOM   14539 C  CA    . PRO A 1 3137 ? 141.117 171.207 214.256 1.00 75.14  ? 3137 PRO A CA    1 
ATOM   14540 C  C     . PRO A 1 3137 ? 141.965 172.221 215.010 1.00 71.01  ? 3137 PRO A C     1 
ATOM   14541 O  O     . PRO A 1 3137 ? 141.470 173.186 215.594 1.00 74.94  ? 3137 PRO A O     1 
ATOM   14542 C  CB    . PRO A 1 3137 ? 141.091 171.528 212.760 1.00 66.95  ? 3137 PRO A CB    1 
ATOM   14543 C  CG    . PRO A 1 3137 ? 139.894 172.387 212.596 1.00 74.22  ? 3137 PRO A CG    1 
ATOM   14544 C  CD    . PRO A 1 3137 ? 138.879 171.902 213.592 1.00 80.49  ? 3137 PRO A CD    1 
ATOM   14545 N  N     . SER A 1 3138 ? 143.270 171.976 214.984 1.00 61.19  ? 3138 SER A N     1 
ATOM   14546 C  CA    . SER A 1 3138 ? 144.253 172.916 215.490 1.00 61.56  ? 3138 SER A CA    1 
ATOM   14547 C  C     . SER A 1 3138 ? 144.837 173.704 214.321 1.00 57.28  ? 3138 SER A C     1 
ATOM   14548 O  O     . SER A 1 3138 ? 144.450 173.526 213.165 1.00 58.17  ? 3138 SER A O     1 
ATOM   14549 C  CB    . SER A 1 3138 ? 145.343 172.183 216.275 1.00 62.33  ? 3138 SER A CB    1 
ATOM   14550 O  OG    . SER A 1 3138 ? 146.158 171.408 215.415 1.00 58.62  ? 3138 SER A OG    1 
ATOM   14551 N  N     . HIS A 1 3139 ? 145.778 174.598 214.628 1.00 54.18  ? 3139 HIS A N     1 
ATOM   14552 C  CA    . HIS A 1 3139 ? 146.390 175.394 213.571 1.00 52.70  ? 3139 HIS A CA    1 
ATOM   14553 C  C     . HIS A 1 3139 ? 147.222 174.528 212.634 1.00 49.75  ? 3139 HIS A C     1 
ATOM   14554 O  O     . HIS A 1 3139 ? 147.158 174.690 211.411 1.00 52.45  ? 3139 HIS A O     1 
ATOM   14555 C  CB    . HIS A 1 3139 ? 147.243 176.508 214.172 1.00 55.39  ? 3139 HIS A CB    1 
ATOM   14556 C  CG    . HIS A 1 3139 ? 147.701 177.520 213.170 1.00 51.93  ? 3139 HIS A CG    1 
ATOM   14557 N  ND1   . HIS A 1 3139 ? 149.030 177.827 212.975 1.00 51.67  ? 3139 HIS A ND1   1 
ATOM   14558 C  CD2   . HIS A 1 3139 ? 147.006 178.292 212.302 1.00 49.51  ? 3139 HIS A CD2   1 
ATOM   14559 C  CE1   . HIS A 1 3139 ? 149.133 178.745 212.031 1.00 52.67  ? 3139 HIS A CE1   1 
ATOM   14560 N  NE2   . HIS A 1 3139 ? 147.919 179.044 211.607 1.00 51.57  ? 3139 HIS A NE2   1 
ATOM   14561 N  N     . ARG A 1 3140 ? 148.008 173.602 213.189 1.00 43.89  ? 3140 ARG A N     1 
ATOM   14562 C  CA    . ARG A 1 3140 ? 148.816 172.718 212.355 1.00 40.17  ? 3140 ARG A CA    1 
ATOM   14563 C  C     . ARG A 1 3140 ? 147.938 171.830 211.482 1.00 45.98  ? 3140 ARG A C     1 
ATOM   14564 O  O     . ARG A 1 3140 ? 148.242 171.602 210.303 1.00 49.21  ? 3140 ARG A O     1 
ATOM   14565 C  CB    . ARG A 1 3140 ? 149.737 171.874 213.235 1.00 41.49  ? 3140 ARG A CB    1 
ATOM   14566 C  CG    . ARG A 1 3140 ? 150.401 170.715 212.520 1.00 41.91  ? 3140 ARG A CG    1 
ATOM   14567 C  CD    . ARG A 1 3140 ? 151.532 170.137 213.350 1.00 45.91  ? 3140 ARG A CD    1 
ATOM   14568 N  NE    . ARG A 1 3140 ? 152.709 170.996 213.348 1.00 48.87  ? 3140 ARG A NE    1 
ATOM   14569 C  CZ    . ARG A 1 3140 ? 153.244 171.534 214.435 1.00 56.13  ? 3140 ARG A CZ    1 
ATOM   14570 N  NH1   . ARG A 1 3140 ? 152.722 171.333 215.633 1.00 61.80  ? 3140 ARG A NH1   1 
ATOM   14571 N  NH2   . ARG A 1 3140 ? 154.330 172.291 214.318 1.00 53.91  ? 3140 ARG A NH2   1 
ATOM   14572 N  N     . GLU A 1 3141 ? 146.844 171.317 212.048 1.00 46.91  ? 3141 GLU A N     1 
ATOM   14573 C  CA    . GLU A 1 3141 ? 145.915 170.510 211.268 1.00 42.01  ? 3141 GLU A CA    1 
ATOM   14574 C  C     . GLU A 1 3141 ? 145.315 171.320 210.128 1.00 42.20  ? 3141 GLU A C     1 
ATOM   14575 O  O     . GLU A 1 3141 ? 145.180 170.821 209.006 1.00 47.51  ? 3141 GLU A O     1 
ATOM   14576 C  CB    . GLU A 1 3141 ? 144.818 169.957 212.178 1.00 51.56  ? 3141 GLU A CB    1 
ATOM   14577 C  CG    . GLU A 1 3141 ? 145.219 168.698 212.926 1.00 58.96  ? 3141 GLU A CG    1 
ATOM   14578 C  CD    . GLU A 1 3141 ? 144.439 168.501 214.210 1.00 70.77  ? 3141 GLU A CD    1 
ATOM   14579 O  OE1   . GLU A 1 3141 ? 143.194 168.578 214.171 1.00 75.43  ? 3141 GLU A OE1   1 
ATOM   14580 O  OE2   . GLU A 1 3141 ? 145.071 168.264 215.260 1.00 70.82  ? 3141 GLU A OE2   1 
ATOM   14581 N  N     . ALA A 1 3142 ? 144.964 172.580 210.395 1.00 41.45  ? 3142 ALA A N     1 
ATOM   14582 C  CA    . ALA A 1 3142 ? 144.445 173.449 209.345 1.00 34.35  ? 3142 ALA A CA    1 
ATOM   14583 C  C     . ALA A 1 3142 ? 145.486 173.692 208.260 1.00 34.95  ? 3142 ALA A C     1 
ATOM   14584 O  O     . ALA A 1 3142 ? 145.155 173.728 207.070 1.00 38.74  ? 3142 ALA A O     1 
ATOM   14585 C  CB    . ALA A 1 3142 ? 143.981 174.774 209.947 1.00 40.18  ? 3142 ALA A CB    1 
ATOM   14586 N  N     . ILE A 1 3143 ? 146.749 173.868 208.650 1.00 34.66  ? 3143 ILE A N     1 
ATOM   14587 C  CA    . ILE A 1 3143 ? 147.808 174.096 207.668 1.00 33.46  ? 3143 ILE A CA    1 
ATOM   14588 C  C     . ILE A 1 3143 ? 147.965 172.882 206.759 1.00 35.50  ? 3143 ILE A C     1 
ATOM   14589 O  O     . ILE A 1 3143 ? 148.071 173.008 205.532 1.00 38.02  ? 3143 ILE A O     1 
ATOM   14590 C  CB    . ILE A 1 3143 ? 149.130 174.441 208.374 1.00 31.70  ? 3143 ILE A CB    1 
ATOM   14591 C  CG1   . ILE A 1 3143 ? 149.024 175.785 209.094 1.00 30.36  ? 3143 ILE A CG1   1 
ATOM   14592 C  CG2   . ILE A 1 3143 ? 150.260 174.470 207.375 1.00 32.16  ? 3143 ILE A CG2   1 
ATOM   14593 C  CD1   . ILE A 1 3143 ? 148.891 176.960 208.167 1.00 31.76  ? 3143 ILE A CD1   1 
ATOM   14594 N  N     . VAL A 1 3144 ? 147.988 171.684 207.348 1.00 34.33  ? 3144 VAL A N     1 
ATOM   14595 C  CA    . VAL A 1 3144 ? 148.144 170.479 206.537 1.00 30.80  ? 3144 VAL A CA    1 
ATOM   14596 C  C     . VAL A 1 3144 ? 146.919 170.266 205.654 1.00 36.40  ? 3144 VAL A C     1 
ATOM   14597 O  O     . VAL A 1 3144 ? 147.030 169.811 204.506 1.00 40.46  ? 3144 VAL A O     1 
ATOM   14598 C  CB    . VAL A 1 3144 ? 148.426 169.259 207.429 1.00 27.24  ? 3144 VAL A CB    1 
ATOM   14599 C  CG1   . VAL A 1 3144 ? 148.735 168.051 206.574 1.00 33.25  ? 3144 VAL A CG1   1 
ATOM   14600 C  CG2   . VAL A 1 3144 ? 149.585 169.549 208.359 1.00 31.37  ? 3144 VAL A CG2   1 
ATOM   14601 N  N     . ASN A 1 3145 ? 145.733 170.599 206.170 1.00 31.44  ? 3145 ASN A N     1 
ATOM   14602 C  CA    . ASN A 1 3145 ? 144.524 170.547 205.358 1.00 30.71  ? 3145 ASN A CA    1 
ATOM   14603 C  C     . ASN A 1 3145 ? 144.633 171.475 204.157 1.00 34.99  ? 3145 ASN A C     1 
ATOM   14604 O  O     . ASN A 1 3145 ? 144.249 171.109 203.041 1.00 36.45  ? 3145 ASN A O     1 
ATOM   14605 C  CB    . ASN A 1 3145 ? 143.317 170.919 206.218 1.00 37.05  ? 3145 ASN A CB    1 
ATOM   14606 C  CG    . ASN A 1 3145 ? 142.001 170.657 205.525 1.00 49.58  ? 3145 ASN A CG    1 
ATOM   14607 O  OD1   . ASN A 1 3145 ? 141.646 169.512 205.256 1.00 57.93  ? 3145 ASN A OD1   1 
ATOM   14608 N  ND2   . ASN A 1 3145 ? 141.261 171.721 205.241 1.00 49.54  ? 3145 ASN A ND2   1 
ATOM   14609 N  N     . SER A 1 3146 ? 145.161 172.681 204.369 1.00 34.40  ? 3146 SER A N     1 
ATOM   14610 C  CA    . SER A 1 3146 ? 145.338 173.621 203.268 1.00 30.55  ? 3146 SER A CA    1 
ATOM   14611 C  C     . SER A 1 3146 ? 146.345 173.100 202.252 1.00 29.75  ? 3146 SER A C     1 
ATOM   14612 O  O     . SER A 1 3146 ? 146.183 173.311 201.047 1.00 33.04  ? 3146 SER A O     1 
ATOM   14613 C  CB    . SER A 1 3146 ? 145.771 174.982 203.808 1.00 31.42  ? 3146 SER A CB    1 
ATOM   14614 O  OG    . SER A 1 3146 ? 144.763 175.544 204.627 1.00 30.88  ? 3146 SER A OG    1 
ATOM   14615 N  N     . CYS A 1 3147 ? 147.399 172.428 202.718 1.00 28.55  ? 3147 CYS A N     1 
ATOM   14616 C  CA    . CYS A 1 3147 ? 148.369 171.838 201.794 1.00 24.79  ? 3147 CYS A CA    1 
ATOM   14617 C  C     . CYS A 1 3147 ? 147.719 170.770 200.916 1.00 29.52  ? 3147 CYS A C     1 
ATOM   14618 O  O     . CYS A 1 3147 ? 147.925 170.730 199.690 1.00 34.52  ? 3147 CYS A O     1 
ATOM   14619 C  CB    . CYS A 1 3147 ? 149.539 171.248 202.580 1.00 23.19  ? 3147 CYS A CB    1 
ATOM   14620 S  SG    . CYS A 1 3147 ? 150.477 172.446 203.548 1.00 37.45  ? 3147 CYS A SG    1 
ATOM   14621 N  N     . VAL A 1 3148 ? 146.927 169.890 201.534 1.00 29.22  ? 3148 VAL A N     1 
ATOM   14622 C  CA    . VAL A 1 3148 ? 146.213 168.871 200.769 1.00 26.47  ? 3148 VAL A CA    1 
ATOM   14623 C  C     . VAL A 1 3148 ? 145.260 169.529 199.779 1.00 31.03  ? 3148 VAL A C     1 
ATOM   14624 O  O     . VAL A 1 3148 ? 145.126 169.087 198.630 1.00 32.18  ? 3148 VAL A O     1 
ATOM   14625 C  CB    . VAL A 1 3148 ? 145.474 167.909 201.716 1.00 25.96  ? 3148 VAL A CB    1 
ATOM   14626 C  CG1   . VAL A 1 3148 ? 144.752 166.837 200.923 1.00 29.13  ? 3148 VAL A CG1   1 
ATOM   14627 C  CG2   . VAL A 1 3148 ? 146.446 167.282 202.694 1.00 30.09  ? 3148 VAL A CG2   1 
ATOM   14628 N  N     . PHE A 1 3149 ? 144.592 170.602 200.207 1.00 31.91  ? 3149 PHE A N     1 
ATOM   14629 C  CA    . PHE A 1 3149 ? 143.699 171.326 199.310 1.00 28.95  ? 3149 PHE A CA    1 
ATOM   14630 C  C     . PHE A 1 3149 ? 144.458 171.919 198.133 1.00 30.05  ? 3149 PHE A C     1 
ATOM   14631 O  O     . PHE A 1 3149 ? 143.941 171.956 197.016 1.00 38.91  ? 3149 PHE A O     1 
ATOM   14632 C  CB    . PHE A 1 3149 ? 142.964 172.428 200.067 1.00 32.93  ? 3149 PHE A CB    1 
ATOM   14633 C  CG    . PHE A 1 3149 ? 142.034 173.230 199.205 1.00 42.62  ? 3149 PHE A CG    1 
ATOM   14634 C  CD1   . PHE A 1 3149 ? 140.817 172.707 198.806 1.00 54.55  ? 3149 PHE A CD1   1 
ATOM   14635 C  CD2   . PHE A 1 3149 ? 142.385 174.496 198.773 1.00 37.22  ? 3149 PHE A CD2   1 
ATOM   14636 C  CE1   . PHE A 1 3149 ? 139.962 173.436 198.010 1.00 52.34  ? 3149 PHE A CE1   1 
ATOM   14637 C  CE2   . PHE A 1 3149 ? 141.533 175.228 197.977 1.00 42.78  ? 3149 PHE A CE2   1 
ATOM   14638 C  CZ    . PHE A 1 3149 ? 140.320 174.699 197.596 1.00 51.43  ? 3149 PHE A CZ    1 
ATOM   14639 N  N     . VAL A 1 3150 ? 145.675 172.414 198.367 1.00 26.99  ? 3150 VAL A N     1 
ATOM   14640 C  CA    . VAL A 1 3150 ? 146.474 172.976 197.280 1.00 22.82  ? 3150 VAL A CA    1 
ATOM   14641 C  C     . VAL A 1 3150 ? 146.806 171.902 196.250 1.00 23.55  ? 3150 VAL A C     1 
ATOM   14642 O  O     . VAL A 1 3150 ? 146.691 172.123 195.034 1.00 28.98  ? 3150 VAL A O     1 
ATOM   14643 C  CB    . VAL A 1 3150 ? 147.745 173.641 197.838 1.00 19.30  ? 3150 VAL A CB    1 
ATOM   14644 C  CG1   . VAL A 1 3150 ? 148.680 174.005 196.715 1.00 21.74  ? 3150 VAL A CG1   1 
ATOM   14645 C  CG2   . VAL A 1 3150 ? 147.388 174.882 198.630 1.00 16.50  ? 3150 VAL A CG2   1 
ATOM   14646 N  N     . HIS A 1 3151 ? 147.212 170.720 196.718 1.00 24.09  ? 3151 HIS A N     1 
ATOM   14647 C  CA    . HIS A 1 3151 ? 147.465 169.624 195.782 1.00 24.52  ? 3151 HIS A CA    1 
ATOM   14648 C  C     . HIS A 1 3151 ? 146.205 169.272 194.992 1.00 32.04  ? 3151 HIS A C     1 
ATOM   14649 O  O     . HIS A 1 3151 ? 146.247 169.089 193.762 1.00 36.09  ? 3151 HIS A O     1 
ATOM   14650 C  CB    . HIS A 1 3151 ? 147.986 168.402 196.537 1.00 23.41  ? 3151 HIS A CB    1 
ATOM   14651 C  CG    . HIS A 1 3151 ? 148.713 167.419 195.674 1.00 27.09  ? 3151 HIS A CG    1 
ATOM   14652 N  ND1   . HIS A 1 3151 ? 149.916 167.708 195.067 1.00 28.89  ? 3151 HIS A ND1   1 
ATOM   14653 C  CD2   . HIS A 1 3151 ? 148.406 166.152 195.313 1.00 32.56  ? 3151 HIS A CD2   1 
ATOM   14654 C  CE1   . HIS A 1 3151 ? 150.319 166.659 194.373 1.00 28.86  ? 3151 HIS A CE1   1 
ATOM   14655 N  NE2   . HIS A 1 3151 ? 149.420 165.702 194.505 1.00 32.76  ? 3151 HIS A NE2   1 
ATOM   14656 N  N     . GLN A 1 3152 ? 145.065 169.197 195.682 1.00 34.01  ? 3152 GLN A N     1 
ATOM   14657 C  CA    . GLN A 1 3152 ? 143.814 168.867 195.009 1.00 34.64  ? 3152 GLN A CA    1 
ATOM   14658 C  C     . GLN A 1 3152 ? 143.416 169.947 194.009 1.00 34.16  ? 3152 GLN A C     1 
ATOM   14659 O  O     . GLN A 1 3152 ? 142.824 169.647 192.967 1.00 41.18  ? 3152 GLN A O     1 
ATOM   14660 C  CB    . GLN A 1 3152 ? 142.712 168.645 196.043 1.00 37.22  ? 3152 GLN A CB    1 
ATOM   14661 C  CG    . GLN A 1 3152 ? 142.975 167.462 196.960 1.00 40.69  ? 3152 GLN A CG    1 
ATOM   14662 C  CD    . GLN A 1 3152 ? 141.717 166.929 197.606 1.00 55.48  ? 3152 GLN A CD    1 
ATOM   14663 O  OE1   . GLN A 1 3152 ? 140.990 167.661 198.274 1.00 58.71  ? 3152 GLN A OE1   1 
ATOM   14664 N  NE2   . GLN A 1 3152 ? 141.455 165.642 197.414 1.00 52.04  ? 3152 GLN A NE2   1 
ATOM   14665 N  N     . THR A 1 3153 ? 143.725 171.211 194.306 1.00 28.76  ? 3153 THR A N     1 
ATOM   14666 C  CA    . THR A 1 3153 ? 143.412 172.285 193.369 1.00 27.04  ? 3153 THR A CA    1 
ATOM   14667 C  C     . THR A 1 3153 ? 144.282 172.205 192.128 1.00 31.16  ? 3153 THR A C     1 
ATOM   14668 O  O     . THR A 1 3153 ? 143.825 172.533 191.032 1.00 40.16  ? 3153 THR A O     1 
ATOM   14669 C  CB    . THR A 1 3153 ? 143.567 173.655 194.022 1.00 26.00  ? 3153 THR A CB    1 
ATOM   14670 O  OG1   . THR A 1 3153 ? 144.843 173.749 194.661 1.00 29.11  ? 3153 THR A OG1   1 
ATOM   14671 C  CG2   . THR A 1 3153 ? 142.471 173.885 195.023 1.00 35.43  ? 3153 THR A CG2   1 
ATOM   14672 N  N     . LEU A 1 3154 ? 145.541 171.793 192.272 1.00 31.32  ? 3154 LEU A N     1 
ATOM   14673 C  CA    . LEU A 1 3154 ? 146.331 171.535 191.068 1.00 28.60  ? 3154 LEU A CA    1 
ATOM   14674 C  C     . LEU A 1 3154 ? 145.717 170.418 190.234 1.00 34.12  ? 3154 LEU A C     1 
ATOM   14675 O  O     . LEU A 1 3154 ? 145.661 170.514 189.001 1.00 40.58  ? 3154 LEU A O     1 
ATOM   14676 C  CB    . LEU A 1 3154 ? 147.784 171.218 191.411 1.00 29.55  ? 3154 LEU A CB    1 
ATOM   14677 C  CG    . LEU A 1 3154 ? 148.707 172.420 191.604 1.00 32.82  ? 3154 LEU A CG    1 
ATOM   14678 C  CD1   . LEU A 1 3154 ? 148.812 173.171 190.288 1.00 32.13  ? 3154 LEU A CD1   1 
ATOM   14679 C  CD2   . LEU A 1 3154 ? 148.251 173.349 192.702 1.00 27.97  ? 3154 LEU A CD2   1 
ATOM   14680 N  N     . HIS A 1 3155 ? 145.245 169.352 190.886 1.00 38.20  ? 3155 HIS A N     1 
ATOM   14681 C  CA    . HIS A 1 3155 ? 144.584 168.288 190.127 1.00 38.87  ? 3155 HIS A CA    1 
ATOM   14682 C  C     . HIS A 1 3155 ? 143.340 168.801 189.402 1.00 39.59  ? 3155 HIS A C     1 
ATOM   14683 O  O     . HIS A 1 3155 ? 143.136 168.510 188.215 1.00 42.81  ? 3155 HIS A O     1 
ATOM   14684 C  CB    . HIS A 1 3155 ? 144.229 167.120 191.045 1.00 39.29  ? 3155 HIS A CB    1 
ATOM   14685 C  CG    . HIS A 1 3155 ? 145.389 166.230 191.359 1.00 42.03  ? 3155 HIS A CG    1 
ATOM   14686 N  ND1   . HIS A 1 3155 ? 146.041 165.495 190.393 1.00 44.14  ? 3155 HIS A ND1   1 
ATOM   14687 C  CD2   . HIS A 1 3155 ? 146.008 165.947 192.528 1.00 41.58  ? 3155 HIS A CD2   1 
ATOM   14688 C  CE1   . HIS A 1 3155 ? 147.017 164.803 190.952 1.00 47.22  ? 3155 HIS A CE1   1 
ATOM   14689 N  NE2   . HIS A 1 3155 ? 147.018 165.060 192.247 1.00 47.53  ? 3155 HIS A NE2   1 
ATOM   14690 N  N     . GLN A 1 3156 ? 142.505 169.577 190.095 1.00 38.80  ? 3156 GLN A N     1 
ATOM   14691 C  CA    . GLN A 1 3156 ? 141.293 170.113 189.478 1.00 38.88  ? 3156 GLN A CA    1 
ATOM   14692 C  C     . GLN A 1 3156 ? 141.622 171.082 188.349 1.00 43.45  ? 3156 GLN A C     1 
ATOM   14693 O  O     . GLN A 1 3156 ? 140.934 171.104 187.324 1.00 50.38  ? 3156 GLN A O     1 
ATOM   14694 C  CB    . GLN A 1 3156 ? 140.423 170.801 190.529 1.00 35.17  ? 3156 GLN A CB    1 
ATOM   14695 C  CG    . GLN A 1 3156 ? 139.958 169.891 191.647 1.00 40.01  ? 3156 GLN A CG    1 
ATOM   14696 C  CD    . GLN A 1 3156 ? 139.402 170.662 192.825 1.00 48.24  ? 3156 GLN A CD    1 
ATOM   14697 O  OE1   . GLN A 1 3156 ? 139.382 171.893 192.822 1.00 46.76  ? 3156 GLN A OE1   1 
ATOM   14698 N  NE2   . GLN A 1 3156 ? 138.943 169.942 193.842 1.00 49.99  ? 3156 GLN A NE2   1 
ATOM   14699 N  N     . ALA A 1 3157 ? 142.655 171.905 188.529 1.00 40.96  ? 3157 ALA A N     1 
ATOM   14700 C  CA    . ALA A 1 3157 ? 143.063 172.840 187.490 1.00 39.24  ? 3157 ALA A CA    1 
ATOM   14701 C  C     . ALA A 1 3157 ? 143.537 172.107 186.246 1.00 46.16  ? 3157 ALA A C     1 
ATOM   14702 O  O     . ALA A 1 3157 ? 143.201 172.495 185.122 1.00 54.82  ? 3157 ALA A O     1 
ATOM   14703 C  CB    . ALA A 1 3157 ? 144.162 173.754 188.023 1.00 33.53  ? 3157 ALA A CB    1 
ATOM   14704 N  N     . ASN A 1 3158 ? 144.324 171.045 186.424 1.00 44.53  ? 3158 ASN A N     1 
ATOM   14705 C  CA    . ASN A 1 3158 ? 144.759 170.264 185.273 1.00 45.85  ? 3158 ASN A CA    1 
ATOM   14706 C  C     . ASN A 1 3158 ? 143.574 169.598 184.586 1.00 50.84  ? 3158 ASN A C     1 
ATOM   14707 O  O     . ASN A 1 3158 ? 143.520 169.533 183.353 1.00 58.09  ? 3158 ASN A O     1 
ATOM   14708 C  CB    . ASN A 1 3158 ? 145.796 169.230 185.702 1.00 45.21  ? 3158 ASN A CB    1 
ATOM   14709 C  CG    . ASN A 1 3158 ? 147.213 169.732 185.536 1.00 49.05  ? 3158 ASN A CG    1 
ATOM   14710 O  OD1   . ASN A 1 3158 ? 147.677 169.958 184.422 1.00 54.50  ? 3158 ASN A OD1   1 
ATOM   14711 N  ND2   . ASN A 1 3158 ? 147.899 169.936 186.647 1.00 47.88  ? 3158 ASN A ND2   1 
ATOM   14712 N  N     . ALA A 1 3159 ? 142.608 169.108 185.368 1.00 49.14  ? 3159 ALA A N     1 
ATOM   14713 C  CA    . ALA A 1 3159 ? 141.412 168.518 184.772 1.00 52.09  ? 3159 ALA A CA    1 
ATOM   14714 C  C     . ALA A 1 3159 ? 140.630 169.546 183.959 1.00 55.46  ? 3159 ALA A C     1 
ATOM   14715 O  O     . ALA A 1 3159 ? 140.169 169.253 182.850 1.00 61.99  ? 3159 ALA A O     1 
ATOM   14716 C  CB    . ALA A 1 3159 ? 140.528 167.911 185.860 1.00 49.60  ? 3159 ALA A CB    1 
ATOM   14717 N  N     . ARG A 1 3160 ? 140.474 170.758 184.496 1.00 53.81  ? 3160 ARG A N     1 
ATOM   14718 C  CA    . ARG A 1 3160 ? 139.754 171.806 183.778 1.00 57.53  ? 3160 ARG A CA    1 
ATOM   14719 C  C     . ARG A 1 3160 ? 140.485 172.212 182.503 1.00 61.71  ? 3160 ARG A C     1 
ATOM   14720 O  O     . ARG A 1 3160 ? 139.857 172.422 181.458 1.00 69.90  ? 3160 ARG A O     1 
ATOM   14721 C  CB    . ARG A 1 3160 ? 139.549 173.015 184.691 1.00 64.40  ? 3160 ARG A CB    1 
ATOM   14722 C  CG    . ARG A 1 3160 ? 139.532 174.353 183.971 1.00 75.42  ? 3160 ARG A CG    1 
ATOM   14723 C  CD    . ARG A 1 3160 ? 139.160 175.485 184.917 1.00 83.48  ? 3160 ARG A CD    1 
ATOM   14724 N  NE    . ARG A 1 3160 ? 137.752 175.455 185.296 1.00 95.27  ? 3160 ARG A NE    1 
ATOM   14725 C  CZ    . ARG A 1 3160 ? 136.748 175.774 184.490 1.00 97.59  ? 3160 ARG A CZ    1 
ATOM   14726 N  NH1   . ARG A 1 3160 ? 136.958 176.172 183.246 1.00 96.69  ? 3160 ARG A NH1   1 
ATOM   14727 N  NH2   . ARG A 1 3160 ? 135.501 175.700 184.947 1.00 94.13  ? 3160 ARG A NH2   1 
ATOM   14728 N  N     . LEU A 1 3161 ? 141.813 172.333 182.569 1.00 61.04  ? 3161 LEU A N     1 
ATOM   14729 C  CA    . LEU A 1 3161 ? 142.583 172.665 181.374 1.00 61.58  ? 3161 LEU A CA    1 
ATOM   14730 C  C     . LEU A 1 3161 ? 142.469 171.572 180.321 1.00 62.22  ? 3161 LEU A C     1 
ATOM   14731 O  O     . LEU A 1 3161 ? 142.374 171.862 179.124 1.00 67.29  ? 3161 LEU A O     1 
ATOM   14732 C  CB    . LEU A 1 3161 ? 144.048 172.910 181.734 1.00 62.05  ? 3161 LEU A CB    1 
ATOM   14733 C  CG    . LEU A 1 3161 ? 144.488 174.345 182.027 1.00 68.01  ? 3161 LEU A CG    1 
ATOM   14734 C  CD1   . LEU A 1 3161 ? 143.664 174.975 183.137 1.00 69.49  ? 3161 LEU A CD1   1 
ATOM   14735 C  CD2   . LEU A 1 3161 ? 145.966 174.376 182.374 1.00 66.28  ? 3161 LEU A CD2   1 
ATOM   14736 N  N     . ALA A 1 3162 ? 142.487 170.306 180.746 1.00 61.15  ? 3162 ALA A N     1 
ATOM   14737 C  CA    . ALA A 1 3162 ? 142.307 169.212 179.798 1.00 62.64  ? 3162 ALA A CA    1 
ATOM   14738 C  C     . ALA A 1 3162 ? 140.922 169.255 179.168 1.00 65.90  ? 3162 ALA A C     1 
ATOM   14739 O  O     . ALA A 1 3162 ? 140.770 169.007 177.966 1.00 66.71  ? 3162 ALA A O     1 
ATOM   14740 C  CB    . ALA A 1 3162 ? 142.543 167.871 180.491 1.00 57.46  ? 3162 ALA A CB    1 
ATOM   14741 N  N     . LYS A 1 3163 ? 139.896 169.564 179.966 1.00 69.73  ? 3163 LYS A N     1 
ATOM   14742 C  CA    . LYS A 1 3163 ? 138.546 169.677 179.424 1.00 66.97  ? 3163 LYS A CA    1 
ATOM   14743 C  C     . LYS A 1 3163 ? 138.451 170.802 178.402 1.00 71.36  ? 3163 LYS A C     1 
ATOM   14744 O  O     . LYS A 1 3163 ? 137.826 170.640 177.348 1.00 80.35  ? 3163 LYS A O     1 
ATOM   14745 C  CB    . LYS A 1 3163 ? 137.539 169.896 180.552 1.00 65.50  ? 3163 LYS A CB    1 
ATOM   14746 C  CG    . LYS A 1 3163 ? 137.139 168.629 181.285 1.00 66.89  ? 3163 LYS A CG    1 
ATOM   14747 C  CD    . LYS A 1 3163 ? 135.969 167.947 180.597 1.00 80.66  ? 3163 LYS A CD    1 
ATOM   14748 C  CE    . LYS A 1 3163 ? 134.709 168.794 180.681 1.00 80.53  ? 3163 LYS A CE    1 
ATOM   14749 N  NZ    . LYS A 1 3163 ? 133.477 167.974 180.526 1.00 65.94  ? 3163 LYS A NZ    1 
ATOM   14750 N  N     . ARG A 1 3164 ? 139.063 171.951 178.694 1.00 71.52  ? 3164 ARG A N     1 
ATOM   14751 C  CA    . ARG A 1 3164 ? 139.042 173.062 177.751 1.00 71.14  ? 3164 ARG A CA    1 
ATOM   14752 C  C     . ARG A 1 3164 ? 139.837 172.766 176.485 1.00 73.45  ? 3164 ARG A C     1 
ATOM   14753 O  O     . ARG A 1 3164 ? 139.571 173.381 175.447 1.00 81.24  ? 3164 ARG A O     1 
ATOM   14754 C  CB    . ARG A 1 3164 ? 139.570 174.333 178.425 1.00 71.95  ? 3164 ARG A CB    1 
ATOM   14755 C  CG    . ARG A 1 3164 ? 139.461 175.583 177.564 1.00 81.46  ? 3164 ARG A CG    1 
ATOM   14756 C  CD    . ARG A 1 3164 ? 139.928 176.838 178.284 1.00 88.06  ? 3164 ARG A CD    1 
ATOM   14757 N  NE    . ARG A 1 3164 ? 141.349 176.807 178.605 1.00 90.89  ? 3164 ARG A NE    1 
ATOM   14758 C  CZ    . ARG A 1 3164 ? 141.840 176.762 179.835 1.00 92.66  ? 3164 ARG A CZ    1 
ATOM   14759 N  NH1   . ARG A 1 3164 ? 141.048 176.747 180.895 1.00 92.83  ? 3164 ARG A NH1   1 
ATOM   14760 N  NH2   . ARG A 1 3164 ? 143.158 176.739 180.008 1.00 87.34  ? 3164 ARG A NH2   1 
ATOM   14761 N  N     . GLY A 1 3165 ? 140.781 171.829 176.534 1.00 72.69  ? 3165 GLY A N     1 
ATOM   14762 C  CA    . GLY A 1 3165 ? 141.557 171.451 175.372 1.00 73.70  ? 3165 GLY A CA    1 
ATOM   14763 C  C     . GLY A 1 3165 ? 143.015 171.851 175.404 1.00 76.23  ? 3165 GLY A C     1 
ATOM   14764 O  O     . GLY A 1 3165 ? 143.726 171.599 174.424 1.00 78.42  ? 3165 GLY A O     1 
ATOM   14765 N  N     . GLY A 1 3166 ? 143.486 172.458 176.492 1.00 76.02  ? 3166 GLY A N     1 
ATOM   14766 C  CA    . GLY A 1 3166 ? 144.871 172.864 176.579 1.00 72.48  ? 3166 GLY A CA    1 
ATOM   14767 C  C     . GLY A 1 3166 ? 145.800 171.724 176.949 1.00 73.88  ? 3166 GLY A C     1 
ATOM   14768 O  O     . GLY A 1 3166 ? 145.380 170.626 177.311 1.00 70.10  ? 3166 GLY A O     1 
ATOM   14769 N  N     . ARG A 1 3167 ? 147.097 172.003 176.848 1.00 75.39  ? 3167 ARG A N     1 
ATOM   14770 C  CA    . ARG A 1 3167 ? 148.117 171.025 177.199 1.00 71.01  ? 3167 ARG A CA    1 
ATOM   14771 C  C     . ARG A 1 3167 ? 148.352 171.044 178.703 1.00 64.09  ? 3167 ARG A C     1 
ATOM   14772 O  O     . ARG A 1 3167 ? 148.543 172.109 179.296 1.00 68.62  ? 3167 ARG A O     1 
ATOM   14773 C  CB    . ARG A 1 3167 ? 149.418 171.318 176.454 1.00 70.13  ? 3167 ARG A CB    1 
ATOM   14774 C  CG    . ARG A 1 3167 ? 149.397 170.919 174.990 1.00 74.80  ? 3167 ARG A CG    1 
ATOM   14775 C  CD    . ARG A 1 3167 ? 150.202 171.896 174.149 1.00 76.03  ? 3167 ARG A CD    1 
ATOM   14776 N  NE    . ARG A 1 3167 ? 150.008 171.697 172.717 1.00 82.21  ? 3167 ARG A NE    1 
ATOM   14777 C  CZ    . ARG A 1 3167 ? 150.452 170.652 172.032 1.00 87.14  ? 3167 ARG A CZ    1 
ATOM   14778 N  NH1   . ARG A 1 3167 ? 151.136 169.681 172.614 1.00 85.80  ? 3167 ARG A NH1   1 
ATOM   14779 N  NH2   . ARG A 1 3167 ? 150.209 170.584 170.726 1.00 86.68  ? 3167 ARG A NH2   1 
ATOM   14780 N  N     . THR A 1 3168 ? 148.340 169.864 179.317 1.00 59.24  ? 3168 THR A N     1 
ATOM   14781 C  CA    . THR A 1 3168 ? 148.462 169.736 180.760 1.00 57.31  ? 3168 THR A CA    1 
ATOM   14782 C  C     . THR A 1 3168 ? 149.626 168.818 181.103 1.00 59.29  ? 3168 THR A C     1 
ATOM   14783 O  O     . THR A 1 3168 ? 149.998 167.932 180.330 1.00 64.77  ? 3168 THR A O     1 
ATOM   14784 C  CB    . THR A 1 3168 ? 147.176 169.188 181.395 1.00 54.90  ? 3168 THR A CB    1 
ATOM   14785 O  OG1   . THR A 1 3168 ? 147.045 167.795 181.088 1.00 59.84  ? 3168 THR A OG1   1 
ATOM   14786 C  CG2   . THR A 1 3168 ? 145.963 169.930 180.873 1.00 61.22  ? 3168 THR A CG2   1 
ATOM   14787 N  N     . MET A 1 3169 ? 150.198 169.045 182.281 1.00 53.48  ? 3169 MET A N     1 
ATOM   14788 C  CA    . MET A 1 3169 ? 151.259 168.213 182.823 1.00 48.20  ? 3169 MET A CA    1 
ATOM   14789 C  C     . MET A 1 3169 ? 150.749 167.468 184.050 1.00 52.52  ? 3169 MET A C     1 
ATOM   14790 O  O     . MET A 1 3169 ? 149.817 167.908 184.728 1.00 59.51  ? 3169 MET A O     1 
ATOM   14791 C  CB    . MET A 1 3169 ? 152.486 169.056 183.184 1.00 47.58  ? 3169 MET A CB    1 
ATOM   14792 C  CG    . MET A 1 3169 ? 153.157 169.713 181.989 1.00 49.21  ? 3169 MET A CG    1 
ATOM   14793 S  SD    . MET A 1 3169 ? 153.842 168.533 180.813 1.00 74.59  ? 3169 MET A SD    1 
ATOM   14794 C  CE    . MET A 1 3169 ? 154.315 169.622 179.475 1.00 52.06  ? 3169 MET A CE    1 
ATOM   14795 N  N     . ALA A 1 3170 ? 151.373 166.329 184.331 1.00 45.10  ? 3170 ALA A N     1 
ATOM   14796 C  CA    . ALA A 1 3170 ? 150.937 165.458 185.414 1.00 41.55  ? 3170 ALA A CA    1 
ATOM   14797 C  C     . ALA A 1 3170 ? 151.442 165.979 186.753 1.00 41.74  ? 3170 ALA A C     1 
ATOM   14798 O  O     . ALA A 1 3170 ? 152.602 166.385 186.871 1.00 45.27  ? 3170 ALA A O     1 
ATOM   14799 C  CB    . ALA A 1 3170 ? 151.428 164.029 185.184 1.00 45.59  ? 3170 ALA A CB    1 
ATOM   14800 N  N     . ILE A 1 3171 ? 150.568 165.967 187.755 1.00 39.70  ? 3171 ILE A N     1 
ATOM   14801 C  CA    . ILE A 1 3171 ? 150.919 166.376 189.114 1.00 36.27  ? 3171 ILE A CA    1 
ATOM   14802 C  C     . ILE A 1 3171 ? 151.119 165.093 189.913 1.00 38.28  ? 3171 ILE A C     1 
ATOM   14803 O  O     . ILE A 1 3171 ? 150.170 164.480 190.404 1.00 43.32  ? 3171 ILE A O     1 
ATOM   14804 C  CB    . ILE A 1 3171 ? 149.859 167.283 189.732 1.00 40.07  ? 3171 ILE A CB    1 
ATOM   14805 C  CG1   . ILE A 1 3171 ? 149.626 168.505 188.850 1.00 39.20  ? 3171 ILE A CG1   1 
ATOM   14806 C  CG2   . ILE A 1 3171 ? 150.282 167.723 191.117 1.00 40.75  ? 3171 ILE A CG2   1 
ATOM   14807 C  CD1   . ILE A 1 3171 ? 150.832 169.399 188.712 1.00 39.61  ? 3171 ILE A CD1   1 
ATOM   14808 N  N     . THR A 1 3172 ? 152.373 164.686 190.043 1.00 35.60  ? 3172 THR A N     1 
ATOM   14809 C  CA    . THR A 1 3172 ? 152.737 163.487 190.777 1.00 37.75  ? 3172 THR A CA    1 
ATOM   14810 C  C     . THR A 1 3172 ? 152.887 163.804 192.259 1.00 34.34  ? 3172 THR A C     1 
ATOM   14811 O  O     . THR A 1 3172 ? 152.937 164.969 192.656 1.00 35.46  ? 3172 THR A O     1 
ATOM   14812 C  CB    . THR A 1 3172 ? 154.027 162.913 190.198 1.00 36.82  ? 3172 THR A CB    1 
ATOM   14813 O  OG1   . THR A 1 3172 ? 155.115 163.796 190.491 1.00 39.59  ? 3172 THR A OG1   1 
ATOM   14814 C  CG2   . THR A 1 3172 ? 153.901 162.753 188.693 1.00 37.76  ? 3172 THR A CG2   1 
ATOM   14815 N  N     . PRO A 1 3173 ? 152.940 162.781 193.118 1.00 30.73  ? 3173 PRO A N     1 
ATOM   14816 C  CA    . PRO A 1 3173 ? 153.228 163.038 194.538 1.00 26.32  ? 3173 PRO A CA    1 
ATOM   14817 C  C     . PRO A 1 3173 ? 154.578 163.688 194.772 1.00 28.37  ? 3173 PRO A C     1 
ATOM   14818 O  O     . PRO A 1 3173 ? 154.785 164.293 195.834 1.00 34.11  ? 3173 PRO A O     1 
ATOM   14819 C  CB    . PRO A 1 3173 ? 153.162 161.642 195.165 1.00 30.73  ? 3173 PRO A CB    1 
ATOM   14820 C  CG    . PRO A 1 3173 ? 152.258 160.880 194.271 1.00 33.24  ? 3173 PRO A CG    1 
ATOM   14821 C  CD    . PRO A 1 3173 ? 152.540 161.381 192.890 1.00 31.52  ? 3173 PRO A CD    1 
ATOM   14822 N  N     . ARG A 1 3174 ? 155.507 163.574 193.822 1.00 30.90  ? 3174 ARG A N     1 
ATOM   14823 C  CA    . ARG A 1 3174 ? 156.766 164.299 193.931 1.00 29.26  ? 3174 ARG A CA    1 
ATOM   14824 C  C     . ARG A 1 3174 ? 156.533 165.802 193.977 1.00 30.69  ? 3174 ARG A C     1 
ATOM   14825 O  O     . ARG A 1 3174 ? 157.270 166.522 194.657 1.00 35.18  ? 3174 ARG A O     1 
ATOM   14826 C  CB    . ARG A 1 3174 ? 157.686 163.932 192.769 1.00 29.21  ? 3174 ARG A CB    1 
ATOM   14827 C  CG    . ARG A 1 3174 ? 159.076 164.529 192.871 1.00 34.31  ? 3174 ARG A CG    1 
ATOM   14828 C  CD    . ARG A 1 3174 ? 159.935 163.757 193.860 1.00 39.45  ? 3174 ARG A CD    1 
ATOM   14829 N  NE    . ARG A 1 3174 ? 161.035 164.556 194.391 1.00 36.36  ? 3174 ARG A NE    1 
ATOM   14830 C  CZ    . ARG A 1 3174 ? 160.890 165.603 195.191 1.00 40.40  ? 3174 ARG A CZ    1 
ATOM   14831 N  NH1   . ARG A 1 3174 ? 159.698 166.008 195.595 1.00 39.57  ? 3174 ARG A NH1   1 
ATOM   14832 N  NH2   . ARG A 1 3174 ? 161.971 166.259 195.602 1.00 47.24  ? 3174 ARG A NH2   1 
ATOM   14833 N  N     . HIS A 1 3175 ? 155.504 166.291 193.280 1.00 31.87  ? 3175 HIS A N     1 
ATOM   14834 C  CA    . HIS A 1 3175 ? 155.143 167.701 193.385 1.00 25.50  ? 3175 HIS A CA    1 
ATOM   14835 C  C     . HIS A 1 3175 ? 154.715 168.057 194.802 1.00 24.03  ? 3175 HIS A C     1 
ATOM   14836 O  O     . HIS A 1 3175 ? 155.069 169.123 195.314 1.00 29.93  ? 3175 HIS A O     1 
ATOM   14837 C  CB    . HIS A 1 3175 ? 154.032 168.040 192.393 1.00 27.31  ? 3175 HIS A CB    1 
ATOM   14838 C  CG    . HIS A 1 3175 ? 154.454 167.961 190.960 1.00 33.86  ? 3175 HIS A CG    1 
ATOM   14839 N  ND1   . HIS A 1 3175 ? 154.781 166.774 190.343 1.00 36.41  ? 3175 HIS A ND1   1 
ATOM   14840 C  CD2   . HIS A 1 3175 ? 154.594 168.924 190.019 1.00 35.47  ? 3175 HIS A CD2   1 
ATOM   14841 C  CE1   . HIS A 1 3175 ? 155.110 167.009 189.085 1.00 39.21  ? 3175 HIS A CE1   1 
ATOM   14842 N  NE2   . HIS A 1 3175 ? 155.005 168.306 188.864 1.00 35.24  ? 3175 HIS A NE2   1 
ATOM   14843 N  N     . TYR A 1 3176 ? 153.947 167.179 195.451 1.00 22.13  ? 3176 TYR A N     1 
ATOM   14844 C  CA    . TYR A 1 3176 ? 153.526 167.442 196.824 1.00 21.93  ? 3176 TYR A CA    1 
ATOM   14845 C  C     . TYR A 1 3176 ? 154.713 167.442 197.777 1.00 23.98  ? 3176 TYR A C     1 
ATOM   14846 O  O     . TYR A 1 3176 ? 154.797 168.285 198.679 1.00 28.87  ? 3176 TYR A O     1 
ATOM   14847 C  CB    . TYR A 1 3176 ? 152.494 166.407 197.263 1.00 23.23  ? 3176 TYR A CB    1 
ATOM   14848 C  CG    . TYR A 1 3176 ? 151.948 166.642 198.649 1.00 20.65  ? 3176 TYR A CG    1 
ATOM   14849 C  CD1   . TYR A 1 3176 ? 151.141 167.736 198.920 1.00 20.35  ? 3176 TYR A CD1   1 
ATOM   14850 C  CD2   . TYR A 1 3176 ? 152.242 165.774 199.687 1.00 21.14  ? 3176 TYR A CD2   1 
ATOM   14851 C  CE1   . TYR A 1 3176 ? 150.640 167.954 200.182 1.00 21.09  ? 3176 TYR A CE1   1 
ATOM   14852 C  CE2   . TYR A 1 3176 ? 151.745 165.986 200.953 1.00 22.74  ? 3176 TYR A CE2   1 
ATOM   14853 C  CZ    . TYR A 1 3176 ? 150.945 167.077 201.195 1.00 23.29  ? 3176 TYR A CZ    1 
ATOM   14854 O  OH    . TYR A 1 3176 ? 150.447 167.291 202.457 1.00 28.94  ? 3176 TYR A OH    1 
ATOM   14855 N  N     . LEU A 1 3177 ? 155.632 166.491 197.605 1.00 24.87  ? 3177 LEU A N     1 
ATOM   14856 C  CA    . LEU A 1 3177 ? 156.827 166.471 198.442 1.00 24.44  ? 3177 LEU A CA    1 
ATOM   14857 C  C     . LEU A 1 3177 ? 157.664 167.724 198.226 1.00 27.88  ? 3177 LEU A C     1 
ATOM   14858 O  O     . LEU A 1 3177 ? 158.195 168.300 199.183 1.00 30.46  ? 3177 LEU A O     1 
ATOM   14859 C  CB    . LEU A 1 3177 ? 157.649 165.218 198.148 1.00 27.70  ? 3177 LEU A CB    1 
ATOM   14860 C  CG    . LEU A 1 3177 ? 156.938 163.887 198.372 1.00 24.38  ? 3177 LEU A CG    1 
ATOM   14861 C  CD1   . LEU A 1 3177 ? 157.724 162.772 197.727 1.00 31.12  ? 3177 LEU A CD1   1 
ATOM   14862 C  CD2   . LEU A 1 3177 ? 156.749 163.625 199.852 1.00 24.18  ? 3177 LEU A CD2   1 
ATOM   14863 N  N     . ASP A 1 3178 ? 157.781 168.164 196.972 1.00 27.53  ? 3178 ASP A N     1 
ATOM   14864 C  CA    . ASP A 1 3178 ? 158.475 169.409 196.668 1.00 24.57  ? 3178 ASP A CA    1 
ATOM   14865 C  C     . ASP A 1 3178 ? 157.801 170.597 197.340 1.00 25.60  ? 3178 ASP A C     1 
ATOM   14866 O  O     . ASP A 1 3178 ? 158.476 171.479 197.878 1.00 30.57  ? 3178 ASP A O     1 
ATOM   14867 C  CB    . ASP A 1 3178 ? 158.527 169.609 195.155 1.00 29.27  ? 3178 ASP A CB    1 
ATOM   14868 C  CG    . ASP A 1 3178 ? 159.598 170.582 194.734 1.00 46.34  ? 3178 ASP A CG    1 
ATOM   14869 O  OD1   . ASP A 1 3178 ? 160.544 170.787 195.517 1.00 46.56  ? 3178 ASP A OD1   1 
ATOM   14870 O  OD2   . ASP A 1 3178 ? 159.497 171.142 193.622 1.00 52.08  ? 3178 ASP A OD2   1 
ATOM   14871 N  N     . PHE A 1 3179 ? 156.468 170.638 197.315 1.00 23.03  ? 3179 PHE A N     1 
ATOM   14872 C  CA    . PHE A 1 3179 ? 155.745 171.748 197.924 1.00 18.33  ? 3179 PHE A CA    1 
ATOM   14873 C  C     . PHE A 1 3179 ? 155.939 171.772 199.433 1.00 21.62  ? 3179 PHE A C     1 
ATOM   14874 O  O     . PHE A 1 3179 ? 156.136 172.840 200.022 1.00 27.44  ? 3179 PHE A O     1 
ATOM   14875 C  CB    . PHE A 1 3179 ? 154.264 171.660 197.545 1.00 19.86  ? 3179 PHE A CB    1 
ATOM   14876 C  CG    . PHE A 1 3179 ? 153.335 172.359 198.497 1.00 22.31  ? 3179 PHE A CG    1 
ATOM   14877 C  CD1   . PHE A 1 3179 ? 153.494 173.698 198.798 1.00 24.54  ? 3179 PHE A CD1   1 
ATOM   14878 C  CD2   . PHE A 1 3179 ? 152.272 171.680 199.059 1.00 23.05  ? 3179 PHE A CD2   1 
ATOM   14879 C  CE1   . PHE A 1 3179 ? 152.634 174.334 199.666 1.00 22.69  ? 3179 PHE A CE1   1 
ATOM   14880 C  CE2   . PHE A 1 3179 ? 151.410 172.314 199.919 1.00 21.28  ? 3179 PHE A CE2   1 
ATOM   14881 C  CZ    . PHE A 1 3179 ? 151.591 173.641 200.224 1.00 22.05  ? 3179 PHE A CZ    1 
ATOM   14882 N  N     . ILE A 1 3180 ? 155.912 170.606 200.078 1.00 22.23  ? 3180 ILE A N     1 
ATOM   14883 C  CA    . ILE A 1 3180 ? 156.100 170.574 201.526 1.00 22.95  ? 3180 ILE A CA    1 
ATOM   14884 C  C     . ILE A 1 3180 ? 157.535 170.941 201.894 1.00 26.20  ? 3180 ILE A C     1 
ATOM   14885 O  O     . ILE A 1 3180 ? 157.776 171.645 202.884 1.00 26.13  ? 3180 ILE A O     1 
ATOM   14886 C  CB    . ILE A 1 3180 ? 155.696 169.202 202.089 1.00 20.54  ? 3180 ILE A CB    1 
ATOM   14887 C  CG1   . ILE A 1 3180 ? 154.224 168.927 201.797 1.00 21.66  ? 3180 ILE A CG1   1 
ATOM   14888 C  CG2   . ILE A 1 3180 ? 155.912 169.172 203.577 1.00 28.96  ? 3180 ILE A CG2   1 
ATOM   14889 C  CD1   . ILE A 1 3180 ? 153.284 169.922 202.433 1.00 21.13  ? 3180 ILE A CD1   1 
ATOM   14890 N  N     . ASN A 1 3181 ? 158.512 170.479 201.108 1.00 28.35  ? 3181 ASN A N     1 
ATOM   14891 C  CA    . ASN A 1 3181 ? 159.899 170.861 201.354 1.00 28.91  ? 3181 ASN A CA    1 
ATOM   14892 C  C     . ASN A 1 3181 ? 160.095 172.362 201.179 1.00 32.54  ? 3181 ASN A C     1 
ATOM   14893 O  O     . ASN A 1 3181 ? 160.794 173.005 201.973 1.00 38.29  ? 3181 ASN A O     1 
ATOM   14894 C  CB    . ASN A 1 3181 ? 160.826 170.085 200.422 1.00 31.45  ? 3181 ASN A CB    1 
ATOM   14895 C  CG    . ASN A 1 3181 ? 162.263 170.081 200.898 1.00 47.99  ? 3181 ASN A CG    1 
ATOM   14896 O  OD1   . ASN A 1 3181 ? 162.595 170.687 201.916 1.00 46.52  ? 3181 ASN A OD1   1 
ATOM   14897 N  ND2   . ASN A 1 3181 ? 163.127 169.396 200.161 1.00 56.60  ? 3181 ASN A ND2   1 
ATOM   14898 N  N     . HIS A 1 3182 ? 159.488 172.937 200.138 1.00 28.07  ? 3182 HIS A N     1 
ATOM   14899 C  CA    . HIS A 1 3182 ? 159.551 174.378 199.933 1.00 24.94  ? 3182 HIS A CA    1 
ATOM   14900 C  C     . HIS A 1 3182 ? 158.911 175.122 201.092 1.00 26.99  ? 3182 HIS A C     1 
ATOM   14901 O  O     . HIS A 1 3182 ? 159.414 176.163 201.523 1.00 32.29  ? 3182 HIS A O     1 
ATOM   14902 C  CB    . HIS A 1 3182 ? 158.860 174.753 198.625 1.00 23.30  ? 3182 HIS A CB    1 
ATOM   14903 C  CG    . HIS A 1 3182 ? 159.746 174.671 197.424 1.00 24.37  ? 3182 HIS A CG    1 
ATOM   14904 N  ND1   . HIS A 1 3182 ? 159.400 173.964 196.294 1.00 26.85  ? 3182 HIS A ND1   1 
ATOM   14905 C  CD2   . HIS A 1 3182 ? 160.960 175.211 197.173 1.00 29.73  ? 3182 HIS A CD2   1 
ATOM   14906 C  CE1   . HIS A 1 3182 ? 160.364 174.071 195.399 1.00 32.59  ? 3182 HIS A CE1   1 
ATOM   14907 N  NE2   . HIS A 1 3182 ? 161.323 174.822 195.908 1.00 36.62  ? 3182 HIS A NE2   1 
ATOM   14908 N  N     . TYR A 1 3183 ? 157.788 174.611 201.597 1.00 23.30  ? 3183 TYR A N     1 
ATOM   14909 C  CA    . TYR A 1 3183 ? 157.139 175.235 202.742 1.00 23.46  ? 3183 TYR A CA    1 
ATOM   14910 C  C     . TYR A 1 3183 ? 158.056 175.228 203.955 1.00 29.58  ? 3183 TYR A C     1 
ATOM   14911 O  O     . TYR A 1 3183 ? 158.191 176.241 204.648 1.00 33.75  ? 3183 TYR A O     1 
ATOM   14912 C  CB    . TYR A 1 3183 ? 155.823 174.518 203.045 1.00 22.41  ? 3183 TYR A CB    1 
ATOM   14913 C  CG    . TYR A 1 3183 ? 154.953 175.212 204.064 1.00 27.00  ? 3183 TYR A CG    1 
ATOM   14914 C  CD1   . TYR A 1 3183 ? 155.172 176.536 204.409 1.00 31.45  ? 3183 TYR A CD1   1 
ATOM   14915 C  CD2   . TYR A 1 3183 ? 153.916 174.541 204.686 1.00 28.78  ? 3183 TYR A CD2   1 
ATOM   14916 C  CE1   . TYR A 1 3183 ? 154.386 177.169 205.342 1.00 30.52  ? 3183 TYR A CE1   1 
ATOM   14917 C  CE2   . TYR A 1 3183 ? 153.125 175.168 205.618 1.00 28.95  ? 3183 TYR A CE2   1 
ATOM   14918 C  CZ    . TYR A 1 3183 ? 153.363 176.482 205.942 1.00 28.73  ? 3183 TYR A CZ    1 
ATOM   14919 O  OH    . TYR A 1 3183 ? 152.576 177.116 206.872 1.00 37.28  ? 3183 TYR A OH    1 
ATOM   14920 N  N     . ALA A 1 3184 ? 158.710 174.096 204.219 1.00 30.02  ? 3184 ALA A N     1 
ATOM   14921 C  CA    . ALA A 1 3184 ? 159.621 174.024 205.357 1.00 28.85  ? 3184 ALA A CA    1 
ATOM   14922 C  C     . ALA A 1 3184 ? 160.768 175.014 205.205 1.00 35.65  ? 3184 ALA A C     1 
ATOM   14923 O  O     . ALA A 1 3184 ? 161.074 175.779 206.131 1.00 40.88  ? 3184 ALA A O     1 
ATOM   14924 C  CB    . ALA A 1 3184 ? 160.150 172.600 205.514 1.00 38.15  ? 3184 ALA A CB    1 
ATOM   14925 N  N     . ASN A 1 3185 ? 161.397 175.028 204.028 1.00 34.20  ? 3185 ASN A N     1 
ATOM   14926 C  CA    . ASN A 1 3185 ? 162.527 175.923 203.802 1.00 33.43  ? 3185 ASN A CA    1 
ATOM   14927 C  C     . ASN A 1 3185 ? 162.112 177.381 203.942 1.00 37.93  ? 3185 ASN A C     1 
ATOM   14928 O  O     . ASN A 1 3185 ? 162.783 178.164 204.622 1.00 43.60  ? 3185 ASN A O     1 
ATOM   14929 C  CB    . ASN A 1 3185 ? 163.129 175.665 202.421 1.00 31.43  ? 3185 ASN A CB    1 
ATOM   14930 C  CG    . ASN A 1 3185 ? 163.563 174.230 202.236 1.00 39.64  ? 3185 ASN A CG    1 
ATOM   14931 O  OD1   . ASN A 1 3185 ? 163.480 173.421 203.159 1.00 41.55  ? 3185 ASN A OD1   1 
ATOM   14932 N  ND2   . ASN A 1 3185 ? 164.029 173.903 201.038 1.00 43.28  ? 3185 ASN A ND2   1 
ATOM   14933 N  N     . LEU A 1 3186 ? 160.997 177.762 203.315 1.00 32.21  ? 3186 LEU A N     1 
ATOM   14934 C  CA    . LEU A 1 3186 ? 160.557 179.151 203.351 1.00 29.77  ? 3186 LEU A CA    1 
ATOM   14935 C  C     . LEU A 1 3186 ? 160.142 179.572 204.753 1.00 31.08  ? 3186 LEU A C     1 
ATOM   14936 O  O     . LEU A 1 3186 ? 160.466 180.680 205.191 1.00 36.91  ? 3186 LEU A O     1 
ATOM   14937 C  CB    . LEU A 1 3186 ? 159.410 179.361 202.368 1.00 27.40  ? 3186 LEU A CB    1 
ATOM   14938 C  CG    . LEU A 1 3186 ? 159.837 179.658 200.934 1.00 28.37  ? 3186 LEU A CG    1 
ATOM   14939 C  CD1   . LEU A 1 3186 ? 158.660 179.550 199.990 1.00 31.36  ? 3186 LEU A CD1   1 
ATOM   14940 C  CD2   . LEU A 1 3186 ? 160.445 181.039 200.872 1.00 35.59  ? 3186 LEU A CD2   1 
ATOM   14941 N  N     . PHE A 1 3187 ? 159.415 178.711 205.466 1.00 28.52  ? 3187 PHE A N     1 
ATOM   14942 C  CA    . PHE A 1 3187 ? 158.996 179.039 206.822 1.00 30.09  ? 3187 PHE A CA    1 
ATOM   14943 C  C     . PHE A 1 3187 ? 160.206 179.258 207.718 1.00 38.54  ? 3187 PHE A C     1 
ATOM   14944 O  O     . PHE A 1 3187 ? 160.289 180.265 208.433 1.00 44.54  ? 3187 PHE A O     1 
ATOM   14945 C  CB    . PHE A 1 3187 ? 158.100 177.922 207.360 1.00 31.32  ? 3187 PHE A CB    1 
ATOM   14946 C  CG    . PHE A 1 3187 ? 157.477 178.218 208.695 1.00 32.28  ? 3187 PHE A CG    1 
ATOM   14947 C  CD1   . PHE A 1 3187 ? 158.175 178.005 209.869 1.00 39.51  ? 3187 PHE A CD1   1 
ATOM   14948 C  CD2   . PHE A 1 3187 ? 156.184 178.699 208.772 1.00 37.46  ? 3187 PHE A CD2   1 
ATOM   14949 C  CE1   . PHE A 1 3187 ? 157.596 178.272 211.090 1.00 44.84  ? 3187 PHE A CE1   1 
ATOM   14950 C  CE2   . PHE A 1 3187 ? 155.604 178.969 209.990 1.00 39.71  ? 3187 PHE A CE2   1 
ATOM   14951 C  CZ    . PHE A 1 3187 ? 156.309 178.755 211.149 1.00 41.35  ? 3187 PHE A CZ    1 
ATOM   14952 N  N     . HIS A 1 3188 ? 161.176 178.340 207.665 1.00 42.73  ? 3188 HIS A N     1 
ATOM   14953 C  CA    . HIS A 1 3188 ? 162.365 178.490 208.495 1.00 42.72  ? 3188 HIS A CA    1 
ATOM   14954 C  C     . HIS A 1 3188 ? 163.159 179.731 208.106 1.00 43.51  ? 3188 HIS A C     1 
ATOM   14955 O  O     . HIS A 1 3188 ? 163.639 180.464 208.977 1.00 52.19  ? 3188 HIS A O     1 
ATOM   14956 C  CB    . HIS A 1 3188 ? 163.230 177.235 208.402 1.00 48.05  ? 3188 HIS A CB    1 
ATOM   14957 C  CG    . HIS A 1 3188 ? 162.589 176.020 208.998 1.00 60.73  ? 3188 HIS A CG    1 
ATOM   14958 N  ND1   . HIS A 1 3188 ? 161.709 176.089 210.057 1.00 55.97  ? 3188 HIS A ND1   1 
ATOM   14959 C  CD2   . HIS A 1 3188 ? 162.696 174.708 208.683 1.00 62.36  ? 3188 HIS A CD2   1 
ATOM   14960 C  CE1   . HIS A 1 3188 ? 161.303 174.871 210.370 1.00 57.91  ? 3188 HIS A CE1   1 
ATOM   14961 N  NE2   . HIS A 1 3188 ? 161.887 174.015 209.551 1.00 62.32  ? 3188 HIS A NE2   1 
ATOM   14962 N  N     . GLU A 1 3189 ? 163.285 179.998 206.804 1.00 43.10  ? 3189 GLU A N     1 
ATOM   14963 C  CA    . GLU A 1 3189 ? 164.060 181.149 206.350 1.00 42.76  ? 3189 GLU A CA    1 
ATOM   14964 C  C     . GLU A 1 3189 ? 163.428 182.459 206.801 1.00 46.06  ? 3189 GLU A C     1 
ATOM   14965 O  O     . GLU A 1 3189 ? 164.111 183.335 207.343 1.00 52.91  ? 3189 GLU A O     1 
ATOM   14966 C  CB    . GLU A 1 3189 ? 164.192 181.114 204.830 1.00 42.44  ? 3189 GLU A CB    1 
ATOM   14967 C  CG    . GLU A 1 3189 ? 164.757 182.382 204.229 1.00 46.06  ? 3189 GLU A CG    1 
ATOM   14968 C  CD    . GLU A 1 3189 ? 164.625 182.412 202.724 1.00 52.24  ? 3189 GLU A CD    1 
ATOM   14969 O  OE1   . GLU A 1 3189 ? 165.094 181.458 202.068 1.00 48.87  ? 3189 GLU A OE1   1 
ATOM   14970 O  OE2   . GLU A 1 3189 ? 164.059 183.389 202.193 1.00 52.30  ? 3189 GLU A OE2   1 
ATOM   14971 N  N     . LYS A 1 3190 ? 162.120 182.616 206.578 1.00 43.55  ? 3190 LYS A N     1 
ATOM   14972 C  CA    . LYS A 1 3190 ? 161.444 183.847 206.972 1.00 38.90  ? 3190 LYS A CA    1 
ATOM   14973 C  C     . LYS A 1 3190 ? 161.450 184.025 208.484 1.00 46.73  ? 3190 LYS A C     1 
ATOM   14974 O  O     . LYS A 1 3190 ? 161.651 185.142 208.982 1.00 59.63  ? 3190 LYS A O     1 
ATOM   14975 C  CB    . LYS A 1 3190 ? 160.014 183.857 206.436 1.00 37.04  ? 3190 LYS A CB    1 
ATOM   14976 C  CG    . LYS A 1 3190 ? 159.920 183.853 204.923 1.00 37.67  ? 3190 LYS A CG    1 
ATOM   14977 C  CD    . LYS A 1 3190 ? 160.750 184.966 204.316 1.00 46.20  ? 3190 LYS A CD    1 
ATOM   14978 C  CE    . LYS A 1 3190 ? 160.697 184.920 202.801 1.00 46.30  ? 3190 LYS A CE    1 
ATOM   14979 N  NZ    . LYS A 1 3190 ? 161.503 186.008 202.187 1.00 51.89  ? 3190 LYS A NZ    1 
ATOM   14980 N  N     . ARG A 1 3191 ? 161.235 182.939 209.234 1.00 46.48  ? 3191 ARG A N     1 
ATOM   14981 C  CA    . ARG A 1 3191 ? 161.289 183.044 210.685 1.00 52.98  ? 3191 ARG A CA    1 
ATOM   14982 C  C     . ARG A 1 3191 ? 162.674 183.465 211.154 1.00 59.69  ? 3191 ARG A C     1 
ATOM   14983 O  O     . ARG A 1 3191 ? 162.801 184.327 212.028 1.00 70.29  ? 3191 ARG A O     1 
ATOM   14984 C  CB    . ARG A 1 3191 ? 160.879 181.719 211.325 1.00 53.58  ? 3191 ARG A CB    1 
ATOM   14985 C  CG    . ARG A 1 3191 ? 159.950 181.880 212.515 1.00 65.09  ? 3191 ARG A CG    1 
ATOM   14986 C  CD    . ARG A 1 3191 ? 159.583 180.537 213.120 1.00 67.80  ? 3191 ARG A CD    1 
ATOM   14987 N  NE    . ARG A 1 3191 ? 158.699 180.671 214.272 1.00 76.61  ? 3191 ARG A NE    1 
ATOM   14988 C  CZ    . ARG A 1 3191 ? 157.426 181.036 214.210 1.00 79.89  ? 3191 ARG A CZ    1 
ATOM   14989 N  NH1   . ARG A 1 3191 ? 156.839 181.310 213.056 1.00 76.49  ? 3191 ARG A NH1   1 
ATOM   14990 N  NH2   . ARG A 1 3191 ? 156.720 181.125 215.334 1.00 77.10  ? 3191 ARG A NH2   1 
ATOM   14991 N  N     . SER A 1 3192 ? 163.727 182.884 210.573 1.00 56.02  ? 3192 SER A N     1 
ATOM   14992 C  CA    . SER A 1 3192 ? 165.083 183.265 210.956 1.00 60.81  ? 3192 SER A CA    1 
ATOM   14993 C  C     . SER A 1 3192 ? 165.360 184.727 210.631 1.00 67.36  ? 3192 SER A C     1 
ATOM   14994 O  O     . SER A 1 3192 ? 165.953 185.451 211.444 1.00 76.45  ? 3192 SER A O     1 
ATOM   14995 C  CB    . SER A 1 3192 ? 166.095 182.360 210.256 1.00 59.94  ? 3192 SER A CB    1 
ATOM   14996 O  OG    . SER A 1 3192 ? 167.417 182.822 210.461 1.00 75.77  ? 3192 SER A OG    1 
ATOM   14997 N  N     . GLU A 1 3193 ? 164.934 185.180 209.449 1.00 64.02  ? 3193 GLU A N     1 
ATOM   14998 C  CA    . GLU A 1 3193 ? 165.149 186.573 209.074 1.00 65.12  ? 3193 GLU A CA    1 
ATOM   14999 C  C     . GLU A 1 3193 ? 164.466 187.512 210.054 1.00 71.47  ? 3193 GLU A C     1 
ATOM   15000 O  O     . GLU A 1 3193 ? 165.059 188.501 210.503 1.00 79.09  ? 3193 GLU A O     1 
ATOM   15001 C  CB    . GLU A 1 3193 ? 164.643 186.835 207.654 1.00 55.26  ? 3193 GLU A CB    1 
ATOM   15002 C  CG    . GLU A 1 3193 ? 165.361 186.064 206.566 1.00 63.32  ? 3193 GLU A CG    1 
ATOM   15003 C  CD    . GLU A 1 3193 ? 164.761 186.310 205.196 1.00 68.80  ? 3193 GLU A CD    1 
ATOM   15004 O  OE1   . GLU A 1 3193 ? 163.787 187.085 205.106 1.00 65.02  ? 3193 GLU A OE1   1 
ATOM   15005 O  OE2   . GLU A 1 3193 ? 165.263 185.731 204.209 1.00 68.65  ? 3193 GLU A OE2   1 
ATOM   15006 N  N     . LEU A 1 3194 ? 163.211 187.214 210.395 1.00 68.67  ? 3194 LEU A N     1 
ATOM   15007 C  CA    . LEU A 1 3194 ? 162.462 188.145 211.279 1.00 74.01  ? 3194 LEU A CA    1 
ATOM   15008 C  C     . LEU A 1 3194 ? 163.060 188.091 212.697 1.00 81.32  ? 3194 LEU A C     1 
ATOM   15009 O  O     . LEU A 1 3194 ? 163.142 189.159 213.342 1.00 89.32  ? 3194 LEU A O     1 
ATOM   15010 C  CB    . LEU A 1 3194 ? 160.963 187.846 211.278 1.00 68.48  ? 3194 LEU A CB    1 
ATOM   15011 C  CG    . LEU A 1 3194 ? 160.058 189.022 211.661 1.00 86.08  ? 3194 LEU A CG    1 
ATOM   15012 C  CD1   . LEU A 1 3194 ? 158.665 188.846 211.088 1.00 89.91  ? 3194 LEU A CD1   1 
ATOM   15013 C  CD2   . LEU A 1 3194 ? 159.994 189.223 213.165 1.00 92.61  ? 3194 LEU A CD2   1 
ATOM   15014 N  N     . GLU A 1 3195 ? 163.475 186.904 213.155 1.00 78.24  ? 3195 GLU A N     1 
ATOM   15015 C  CA    . GLU A 1 3195 ? 164.072 186.805 214.484 1.00 77.87  ? 3195 GLU A CA    1 
ATOM   15016 C  C     . GLU A 1 3195 ? 165.367 187.600 214.572 1.00 82.36  ? 3195 GLU A C     1 
ATOM   15017 O  O     . GLU A 1 3195 ? 165.619 188.276 215.577 1.00 94.22  ? 3195 GLU A O     1 
ATOM   15018 C  CB    . GLU A 1 3195 ? 164.319 185.344 214.860 1.00 82.10  ? 3195 GLU A CB    1 
ATOM   15019 C  CG    . GLU A 1 3195 ? 163.064 184.505 215.021 1.00 88.35  ? 3195 GLU A CG    1 
ATOM   15020 C  CD    . GLU A 1 3195 ? 163.291 183.282 215.888 1.00 98.91  ? 3195 GLU A CD    1 
ATOM   15021 O  OE1   . GLU A 1 3195 ? 163.350 182.165 215.333 1.00 90.05  ? 3195 GLU A OE1   1 
ATOM   15022 O  OE2   . GLU A 1 3195 ? 163.407 183.435 217.122 1.00 105.89 ? 3195 GLU A OE2   1 
ATOM   15023 N  N     . GLU A 1 3196 ? 166.206 187.538 213.534 1.00 80.59  ? 3196 GLU A N     1 
ATOM   15024 C  CA    . GLU A 1 3196 ? 167.430 188.331 213.580 1.00 85.83  ? 3196 GLU A CA    1 
ATOM   15025 C  C     . GLU A 1 3196 ? 167.120 189.822 213.472 1.00 87.86  ? 3196 GLU A C     1 
ATOM   15026 O  O     . GLU A 1 3196 ? 167.771 190.645 214.127 1.00 92.02  ? 3196 GLU A O     1 
ATOM   15027 C  CB    . GLU A 1 3196 ? 168.421 187.874 212.504 1.00 85.68  ? 3196 GLU A CB    1 
ATOM   15028 C  CG    . GLU A 1 3196 ? 167.977 188.010 211.063 1.00 83.79  ? 3196 GLU A CG    1 
ATOM   15029 C  CD    . GLU A 1 3196 ? 168.280 189.374 210.483 1.00 91.17  ? 3196 GLU A CD    1 
ATOM   15030 O  OE1   . GLU A 1 3196 ? 169.139 190.082 211.049 1.00 93.97  ? 3196 GLU A OE1   1 
ATOM   15031 O  OE2   . GLU A 1 3196 ? 167.668 189.736 209.456 1.00 91.84  ? 3196 GLU A OE2   1 
ATOM   15032 N  N     . GLN A 1 3197 ? 166.097 190.188 212.693 1.00 84.23  ? 3197 GLN A N     1 
ATOM   15033 C  CA    . GLN A 1 3197 ? 165.667 191.584 212.666 1.00 86.98  ? 3197 GLN A CA    1 
ATOM   15034 C  C     . GLN A 1 3197 ? 165.185 192.042 214.039 1.00 92.79  ? 3197 GLN A C     1 
ATOM   15035 O  O     . GLN A 1 3197 ? 165.483 193.162 214.470 1.00 102.72 ? 3197 GLN A O     1 
ATOM   15036 C  CB    . GLN A 1 3197 ? 164.568 191.778 211.623 1.00 86.66  ? 3197 GLN A CB    1 
ATOM   15037 C  CG    . GLN A 1 3197 ? 165.046 191.666 210.189 1.00 90.16  ? 3197 GLN A CG    1 
ATOM   15038 C  CD    . GLN A 1 3197 ? 163.915 191.769 209.188 1.00 95.09  ? 3197 GLN A CD    1 
ATOM   15039 O  OE1   . GLN A 1 3197 ? 162.752 191.920 209.562 1.00 98.39  ? 3197 GLN A OE1   1 
ATOM   15040 N  NE2   . GLN A 1 3197 ? 164.249 191.687 207.907 1.00 91.74  ? 3197 GLN A NE2   1 
ATOM   15041 N  N     . GLN A 1 3198 ? 164.442 191.186 214.743 1.00 90.67  ? 3198 GLN A N     1 
ATOM   15042 C  CA    . GLN A 1 3198 ? 163.899 191.567 216.041 1.00 91.43  ? 3198 GLN A CA    1 
ATOM   15043 C  C     . GLN A 1 3198 ? 164.990 191.666 217.098 1.00 95.96  ? 3198 GLN A C     1 
ATOM   15044 O  O     . GLN A 1 3198 ? 164.933 192.539 217.968 1.00 102.93 ? 3198 GLN A O     1 
ATOM   15045 C  CB    . GLN A 1 3198 ? 162.822 190.578 216.481 1.00 93.34  ? 3198 GLN A CB    1 
ATOM   15046 C  CG    . GLN A 1 3198 ? 161.822 191.180 217.456 1.00 99.66  ? 3198 GLN A CG    1 
ATOM   15047 C  CD    . GLN A 1 3198 ? 160.437 190.578 217.328 1.00 105.50 ? 3198 GLN A CD    1 
ATOM   15048 O  OE1   . GLN A 1 3198 ? 160.210 189.676 216.523 1.00 104.20 ? 3198 GLN A OE1   1 
ATOM   15049 N  NE2   . GLN A 1 3198 ? 159.499 191.083 218.121 1.00 105.89 ? 3198 GLN A NE2   1 
ATOM   15050 N  N     . MET A 1 3199 ? 165.988 190.780 217.054 1.00 94.50  ? 3199 MET A N     1 
ATOM   15051 C  CA    . MET A 1 3199 ? 167.087 190.915 218.006 1.00 94.58  ? 3199 MET A CA    1 
ATOM   15052 C  C     . MET A 1 3199 ? 167.924 192.151 217.693 1.00 97.66  ? 3199 MET A C     1 
ATOM   15053 O  O     . MET A 1 3199 ? 168.421 192.819 218.610 1.00 103.47 ? 3199 MET A O     1 
ATOM   15054 C  CB    . MET A 1 3199 ? 167.942 189.644 218.040 1.00 95.47  ? 3199 MET A CB    1 
ATOM   15055 C  CG    . MET A 1 3199 ? 168.631 189.247 216.747 1.00 100.07 ? 3199 MET A CG    1 
ATOM   15056 S  SD    . MET A 1 3199 ? 170.143 190.162 216.383 1.00 122.88 ? 3199 MET A SD    1 
ATOM   15057 C  CE    . MET A 1 3199 ? 171.243 189.496 217.629 1.00 108.48 ? 3199 MET A CE    1 
ATOM   15058 N  N     . HIS A 1 3200 ? 168.070 192.487 216.406 1.00 95.80  ? 3200 HIS A N     1 
ATOM   15059 C  CA    . HIS A 1 3200 ? 168.686 193.759 216.039 1.00 101.35 ? 3200 HIS A CA    1 
ATOM   15060 C  C     . HIS A 1 3200 ? 167.915 194.934 216.628 1.00 102.12 ? 3200 HIS A C     1 
ATOM   15061 O  O     . HIS A 1 3200 ? 168.509 195.862 217.188 1.00 105.82 ? 3200 HIS A O     1 
ATOM   15062 C  CB    . HIS A 1 3200 ? 168.757 193.879 214.516 1.00 102.31 ? 3200 HIS A CB    1 
ATOM   15063 C  CG    . HIS A 1 3200 ? 169.509 195.081 214.034 1.00 112.28 ? 3200 HIS A CG    1 
ATOM   15064 N  ND1   . HIS A 1 3200 ? 169.465 195.507 212.724 1.00 112.12 ? 3200 HIS A ND1   1 
ATOM   15065 C  CD2   . HIS A 1 3200 ? 170.325 195.945 214.683 1.00 119.26 ? 3200 HIS A CD2   1 
ATOM   15066 C  CE1   . HIS A 1 3200 ? 170.220 196.583 212.588 1.00 116.02 ? 3200 HIS A CE1   1 
ATOM   15067 N  NE2   . HIS A 1 3200 ? 170.753 196.869 213.762 1.00 121.91 ? 3200 HIS A NE2   1 
ATOM   15068 N  N     . LEU A 1 3201 ? 166.588 194.904 216.520 1.00 98.95  ? 3201 LEU A N     1 
ATOM   15069 C  CA    . LEU A 1 3201 ? 165.782 195.999 217.049 1.00 96.90  ? 3201 LEU A CA    1 
ATOM   15070 C  C     . LEU A 1 3201 ? 165.874 196.070 218.570 1.00 103.22 ? 3201 LEU A C     1 
ATOM   15071 O  O     . LEU A 1 3201 ? 165.905 197.163 219.145 1.00 109.99 ? 3201 LEU A O     1 
ATOM   15072 C  CB    . LEU A 1 3201 ? 164.332 195.843 216.595 1.00 96.64  ? 3201 LEU A CB    1 
ATOM   15073 C  CG    . LEU A 1 3201 ? 163.460 197.094 216.677 1.00 105.51 ? 3201 LEU A CG    1 
ATOM   15074 C  CD1   . LEU A 1 3201 ? 163.860 198.082 215.594 1.00 109.85 ? 3201 LEU A CD1   1 
ATOM   15075 C  CD2   . LEU A 1 3201 ? 161.997 196.723 216.539 1.00 103.94 ? 3201 LEU A CD2   1 
ATOM   15076 N  N     . ASN A 1 3202 ? 165.930 194.915 219.237 1.00 102.87 ? 3202 ASN A N     1 
ATOM   15077 C  CA    . ASN A 1 3202 ? 166.041 194.901 220.694 1.00 101.34 ? 3202 ASN A CA    1 
ATOM   15078 C  C     . ASN A 1 3202 ? 167.383 195.454 221.162 1.00 103.79 ? 3202 ASN A C     1 
ATOM   15079 O  O     . ASN A 1 3202 ? 167.436 196.241 222.118 1.00 107.51 ? 3202 ASN A O     1 
ATOM   15080 C  CB    . ASN A 1 3202 ? 165.832 193.483 221.224 1.00 98.66  ? 3202 ASN A CB    1 
ATOM   15081 C  CG    . ASN A 1 3202 ? 164.400 193.012 221.077 1.00 105.71 ? 3202 ASN A CG    1 
ATOM   15082 O  OD1   . ASN A 1 3202 ? 163.471 193.817 221.028 1.00 111.04 ? 3202 ASN A OD1   1 
ATOM   15083 N  ND2   . ASN A 1 3202 ? 164.213 191.699 221.009 1.00 102.85 ? 3202 ASN A ND2   1 
ATOM   15084 N  N     . VAL A 1 3203 ? 168.481 195.050 220.517 1.00 102.70 ? 3203 VAL A N     1 
ATOM   15085 C  CA    . VAL A 1 3203 ? 169.781 195.584 220.916 1.00 107.14 ? 3203 VAL A CA    1 
ATOM   15086 C  C     . VAL A 1 3203 ? 169.861 197.069 220.587 1.00 112.47 ? 3203 VAL A C     1 
ATOM   15087 O  O     . VAL A 1 3203 ? 170.506 197.844 221.304 1.00 115.43 ? 3203 VAL A O     1 
ATOM   15088 C  CB    . VAL A 1 3203 ? 170.934 194.784 220.276 1.00 103.02 ? 3203 VAL A CB    1 
ATOM   15089 C  CG1   . VAL A 1 3203 ? 170.894 193.334 220.737 1.00 103.36 ? 3203 VAL A CG1   1 
ATOM   15090 C  CG2   . VAL A 1 3203 ? 170.911 194.878 218.766 1.00 101.01 ? 3203 VAL A CG2   1 
ATOM   15091 N  N     . GLY A 1 3204 ? 169.184 197.498 219.518 1.00 110.84 ? 3204 GLY A N     1 
ATOM   15092 C  CA    . GLY A 1 3204 ? 169.091 198.922 219.245 1.00 111.13 ? 3204 GLY A CA    1 
ATOM   15093 C  C     . GLY A 1 3204 ? 168.344 199.676 220.328 1.00 111.78 ? 3204 GLY A C     1 
ATOM   15094 O  O     . GLY A 1 3204 ? 168.728 200.785 220.703 1.00 115.91 ? 3204 GLY A O     1 
ATOM   15095 N  N     . LEU A 1 3205 ? 167.253 199.094 220.829 1.00 109.46 ? 3205 LEU A N     1 
ATOM   15096 C  CA    . LEU A 1 3205 ? 166.519 199.719 221.927 1.00 113.99 ? 3205 LEU A CA    1 
ATOM   15097 C  C     . LEU A 1 3205 ? 167.385 199.824 223.176 1.00 118.34 ? 3205 LEU A C     1 
ATOM   15098 O  O     . LEU A 1 3205 ? 167.376 200.852 223.868 1.00 118.33 ? 3205 LEU A O     1 
ATOM   15099 C  CB    . LEU A 1 3205 ? 165.247 198.927 222.225 1.00 109.88 ? 3205 LEU A CB    1 
ATOM   15100 C  CG    . LEU A 1 3205 ? 163.997 199.327 221.445 1.00 108.75 ? 3205 LEU A CG    1 
ATOM   15101 C  CD1   . LEU A 1 3205 ? 162.806 198.497 221.890 1.00 109.08 ? 3205 LEU A CD1   1 
ATOM   15102 C  CD2   . LEU A 1 3205 ? 163.719 200.807 221.628 1.00 113.42 ? 3205 LEU A CD2   1 
ATOM   15103 N  N     . ARG A 1 3206 ? 168.137 198.764 223.482 1.00 116.91 ? 3206 ARG A N     1 
ATOM   15104 C  CA    . ARG A 1 3206 ? 169.055 198.816 224.616 1.00 121.18 ? 3206 ARG A CA    1 
ATOM   15105 C  C     . ARG A 1 3206 ? 170.095 199.913 224.425 1.00 127.38 ? 3206 ARG A C     1 
ATOM   15106 O  O     . ARG A 1 3206 ? 170.405 200.661 225.362 1.00 130.72 ? 3206 ARG A O     1 
ATOM   15107 C  CB    . ARG A 1 3206 ? 169.740 197.463 224.805 1.00 117.85 ? 3206 ARG A CB    1 
ATOM   15108 C  CG    . ARG A 1 3206 ? 171.009 197.535 225.640 1.00 117.83 ? 3206 ARG A CG    1 
ATOM   15109 C  CD    . ARG A 1 3206 ? 171.751 196.211 225.658 1.00 116.21 ? 3206 ARG A CD    1 
ATOM   15110 N  NE    . ARG A 1 3206 ? 172.197 195.815 224.328 1.00 116.41 ? 3206 ARG A NE    1 
ATOM   15111 C  CZ    . ARG A 1 3206 ? 172.894 194.717 224.070 1.00 121.61 ? 3206 ARG A CZ    1 
ATOM   15112 N  NH1   . ARG A 1 3206 ? 173.237 193.875 225.031 1.00 128.26 ? 3206 ARG A NH1   1 
ATOM   15113 N  NH2   . ARG A 1 3206 ? 173.258 194.458 222.818 1.00 119.11 ? 3206 ARG A NH2   1 
ATOM   15114 N  N     . LYS A 1 3207 ? 170.639 200.025 223.212 1.00 126.38 ? 3207 LYS A N     1 
ATOM   15115 C  CA    . LYS A 1 3207 ? 171.628 201.057 222.923 1.00 124.72 ? 3207 LYS A CA    1 
ATOM   15116 C  C     . LYS A 1 3207 ? 171.034 202.452 223.070 1.00 127.37 ? 3207 LYS A C     1 
ATOM   15117 O  O     . LYS A 1 3207 ? 171.694 203.368 223.574 1.00 129.26 ? 3207 LYS A O     1 
ATOM   15118 C  CB    . LYS A 1 3207 ? 172.179 200.852 221.514 1.00 118.43 ? 3207 LYS A CB    1 
ATOM   15119 C  CG    . LYS A 1 3207 ? 173.271 201.816 221.126 1.00 125.01 ? 3207 LYS A CG    1 
ATOM   15120 C  CD    . LYS A 1 3207 ? 174.518 201.575 221.949 1.00 130.56 ? 3207 LYS A CD    1 
ATOM   15121 C  CE    . LYS A 1 3207 ? 175.614 202.522 221.528 1.00 131.82 ? 3207 LYS A CE    1 
ATOM   15122 N  NZ    . LYS A 1 3207 ? 176.012 202.206 220.135 1.00 130.55 ? 3207 LYS A NZ    1 
ATOM   15123 N  N     . ILE A 1 3208 ? 169.790 202.635 222.624 1.00 127.16 ? 3208 ILE A N     1 
ATOM   15124 C  CA    . ILE A 1 3208 ? 169.134 203.934 222.743 1.00 128.03 ? 3208 ILE A CA    1 
ATOM   15125 C  C     . ILE A 1 3208 ? 168.925 204.294 224.207 1.00 129.89 ? 3208 ILE A C     1 
ATOM   15126 O  O     . ILE A 1 3208 ? 169.144 205.440 224.615 1.00 132.88 ? 3208 ILE A O     1 
ATOM   15127 C  CB    . ILE A 1 3208 ? 167.810 203.941 221.958 1.00 127.24 ? 3208 ILE A CB    1 
ATOM   15128 C  CG1   . ILE A 1 3208 ? 168.092 204.025 220.459 1.00 124.75 ? 3208 ILE A CG1   1 
ATOM   15129 C  CG2   . ILE A 1 3208 ? 166.917 205.090 222.406 1.00 125.63 ? 3208 ILE A CG2   1 
ATOM   15130 C  CD1   . ILE A 1 3208 ? 168.773 205.304 220.036 1.00 125.06 ? 3208 ILE A CD1   1 
ATOM   15131 N  N     . LYS A 1 3209 ? 168.495 203.326 225.020 1.00 130.96 ? 3209 LYS A N     1 
ATOM   15132 C  CA    . LYS A 1 3209 ? 168.339 203.593 226.447 1.00 134.73 ? 3209 LYS A CA    1 
ATOM   15133 C  C     . LYS A 1 3209 ? 169.679 203.939 227.090 1.00 135.21 ? 3209 LYS A C     1 
ATOM   15134 O  O     . LYS A 1 3209 ? 169.762 204.845 227.930 1.00 136.01 ? 3209 LYS A O     1 
ATOM   15135 C  CB    . LYS A 1 3209 ? 167.699 202.392 227.142 1.00 134.85 ? 3209 LYS A CB    1 
ATOM   15136 C  CG    . LYS A 1 3209 ? 167.545 202.557 228.645 1.00 136.19 ? 3209 LYS A CG    1 
ATOM   15137 C  CD    . LYS A 1 3209 ? 166.951 201.310 229.279 1.00 137.30 ? 3209 LYS A CD    1 
ATOM   15138 C  CE    . LYS A 1 3209 ? 166.863 201.448 230.790 1.00 140.04 ? 3209 LYS A CE    1 
ATOM   15139 N  NZ    . LYS A 1 3209 ? 166.300 200.224 231.423 1.00 139.64 ? 3209 LYS A NZ    1 
ATOM   15140 N  N     . GLU A 1 3210 ? 170.742 203.232 226.698 1.00 134.84 ? 3210 GLU A N     1 
ATOM   15141 C  CA    . GLU A 1 3210 ? 172.071 203.530 227.225 1.00 136.09 ? 3210 GLU A CA    1 
ATOM   15142 C  C     . GLU A 1 3210 ? 172.513 204.939 226.848 1.00 138.91 ? 3210 GLU A C     1 
ATOM   15143 O  O     . GLU A 1 3210 ? 173.080 205.663 227.675 1.00 138.32 ? 3210 GLU A O     1 
ATOM   15144 C  CB    . GLU A 1 3210 ? 173.076 202.498 226.715 1.00 134.14 ? 3210 GLU A CB    1 
ATOM   15145 C  CG    . GLU A 1 3210 ? 174.525 202.824 227.035 1.00 136.50 ? 3210 GLU A CG    1 
ATOM   15146 C  CD    . GLU A 1 3210 ? 175.497 201.918 226.306 1.00 137.71 ? 3210 GLU A CD    1 
ATOM   15147 O  OE1   . GLU A 1 3210 ? 175.037 201.056 225.527 1.00 131.34 ? 3210 GLU A OE1   1 
ATOM   15148 O  OE2   . GLU A 1 3210 ? 176.719 202.067 226.512 1.00 141.74 ? 3210 GLU A OE2   1 
ATOM   15149 N  N     . THR A 1 3211 ? 172.260 205.349 225.604 1.00 138.94 ? 3211 THR A N     1 
ATOM   15150 C  CA    . THR A 1 3211 ? 172.636 206.694 225.178 1.00 138.70 ? 3211 THR A CA    1 
ATOM   15151 C  C     . THR A 1 3211 ? 171.790 207.753 225.878 1.00 138.53 ? 3211 THR A C     1 
ATOM   15152 O  O     . THR A 1 3211 ? 172.276 208.853 226.167 1.00 140.33 ? 3211 THR A O     1 
ATOM   15153 C  CB    . THR A 1 3211 ? 172.515 206.818 223.660 1.00 138.40 ? 3211 THR A CB    1 
ATOM   15154 O  OG1   . THR A 1 3211 ? 173.270 205.772 223.038 1.00 136.20 ? 3211 THR A OG1   1 
ATOM   15155 C  CG2   . THR A 1 3211 ? 173.048 208.162 223.186 1.00 136.33 ? 3211 THR A CG2   1 
ATOM   15156 N  N     . VAL A 1 3212 ? 170.523 207.441 226.157 1.00 139.12 ? 3212 VAL A N     1 
ATOM   15157 C  CA    . VAL A 1 3212 ? 169.684 208.355 226.928 1.00 141.11 ? 3212 VAL A CA    1 
ATOM   15158 C  C     . VAL A 1 3212 ? 170.256 208.543 228.327 1.00 143.46 ? 3212 VAL A C     1 
ATOM   15159 O  O     . VAL A 1 3212 ? 170.341 209.669 228.835 1.00 145.36 ? 3212 VAL A O     1 
ATOM   15160 C  CB    . VAL A 1 3212 ? 168.231 207.845 226.970 1.00 140.42 ? 3212 VAL A CB    1 
ATOM   15161 C  CG1   . VAL A 1 3212 ? 167.456 208.533 228.082 1.00 142.11 ? 3212 VAL A CG1   1 
ATOM   15162 C  CG2   . VAL A 1 3212 ? 167.551 208.074 225.630 1.00 135.29 ? 3212 VAL A CG2   1 
ATOM   15163 N  N     . ASP A 1 3213 ? 170.666 207.447 228.967 1.00 142.17 ? 3213 ASP A N     1 
ATOM   15164 C  CA    . ASP A 1 3213 ? 171.317 207.563 230.269 1.00 144.02 ? 3213 ASP A CA    1 
ATOM   15165 C  C     . ASP A 1 3213 ? 172.612 208.363 230.167 1.00 143.45 ? 3213 ASP A C     1 
ATOM   15166 O  O     . ASP A 1 3213 ? 172.934 209.156 231.060 1.00 142.56 ? 3213 ASP A O     1 
ATOM   15167 C  CB    . ASP A 1 3213 ? 171.587 206.179 230.858 1.00 145.72 ? 3213 ASP A CB    1 
ATOM   15168 C  CG    . ASP A 1 3213 ? 170.332 205.339 230.974 1.00 143.26 ? 3213 ASP A CG    1 
ATOM   15169 O  OD1   . ASP A 1 3213 ? 169.320 205.851 231.497 1.00 142.15 ? 3213 ASP A OD1   1 
ATOM   15170 O  OD2   . ASP A 1 3213 ? 170.361 204.163 230.556 1.00 142.42 ? 3213 ASP A OD2   1 
ATOM   15171 N  N     . GLN A 1 3214 ? 173.366 208.167 229.084 1.00 141.55 ? 3214 GLN A N     1 
ATOM   15172 C  CA    . GLN A 1 3214 ? 174.621 208.891 228.906 1.00 142.02 ? 3214 GLN A CA    1 
ATOM   15173 C  C     . GLN A 1 3214 ? 174.386 210.394 228.802 1.00 143.69 ? 3214 GLN A C     1 
ATOM   15174 O  O     . GLN A 1 3214 ? 175.080 211.189 229.446 1.00 144.76 ? 3214 GLN A O     1 
ATOM   15175 C  CB    . GLN A 1 3214 ? 175.352 208.376 227.666 1.00 143.41 ? 3214 GLN A CB    1 
ATOM   15176 C  CG    . GLN A 1 3214 ? 176.475 209.284 227.189 1.00 142.22 ? 3214 GLN A CG    1 
ATOM   15177 C  CD    . GLN A 1 3214 ? 176.897 208.994 225.762 1.00 143.88 ? 3214 GLN A CD    1 
ATOM   15178 O  OE1   . GLN A 1 3214 ? 176.342 208.113 225.105 1.00 144.46 ? 3214 GLN A OE1   1 
ATOM   15179 N  NE2   . GLN A 1 3214 ? 177.885 209.734 225.275 1.00 144.33 ? 3214 GLN A NE2   1 
ATOM   15180 N  N     . VAL A 1 3215 ? 173.407 210.806 227.992 1.00 144.16 ? 3215 VAL A N     1 
ATOM   15181 C  CA    . VAL A 1 3215 ? 173.154 212.238 227.846 1.00 143.15 ? 3215 VAL A CA    1 
ATOM   15182 C  C     . VAL A 1 3215 ? 172.536 212.810 229.116 1.00 144.66 ? 3215 VAL A C     1 
ATOM   15183 O  O     . VAL A 1 3215 ? 172.762 213.980 229.447 1.00 144.32 ? 3215 VAL A O     1 
ATOM   15184 C  CB    . VAL A 1 3215 ? 172.289 212.536 226.605 1.00 138.96 ? 3215 VAL A CB    1 
ATOM   15185 C  CG1   . VAL A 1 3215 ? 173.082 212.280 225.331 1.00 135.65 ? 3215 VAL A CG1   1 
ATOM   15186 C  CG2   . VAL A 1 3215 ? 171.016 211.726 226.619 1.00 138.14 ? 3215 VAL A CG2   1 
ATOM   15187 N  N     . GLU A 1 3216 ? 171.761 212.010 229.856 1.00 144.48 ? 3216 GLU A N     1 
ATOM   15188 C  CA    . GLU A 1 3216 ? 171.278 212.465 231.157 1.00 145.58 ? 3216 GLU A CA    1 
ATOM   15189 C  C     . GLU A 1 3216 ? 172.436 212.713 232.117 1.00 148.20 ? 3216 GLU A C     1 
ATOM   15190 O  O     . GLU A 1 3216 ? 172.445 213.710 232.849 1.00 145.52 ? 3216 GLU A O     1 
ATOM   15191 C  CB    . GLU A 1 3216 ? 170.302 211.444 231.742 1.00 142.11 ? 3216 GLU A CB    1 
ATOM   15192 C  CG    . GLU A 1 3216 ? 168.923 211.468 231.106 1.00 142.73 ? 3216 GLU A CG    1 
ATOM   15193 C  CD    . GLU A 1 3216 ? 168.143 212.720 231.456 1.00 142.70 ? 3216 GLU A CD    1 
ATOM   15194 O  OE1   . GLU A 1 3216 ? 167.953 212.986 232.662 1.00 139.69 ? 3216 GLU A OE1   1 
ATOM   15195 O  OE2   . GLU A 1 3216 ? 167.720 213.437 230.527 1.00 143.61 ? 3216 GLU A OE2   1 
ATOM   15196 N  N     . GLU A 1 3217 ? 173.424 211.815 232.127 1.00 149.38 ? 3217 GLU A N     1 
ATOM   15197 C  CA    . GLU A 1 3217 ? 174.606 212.021 232.960 1.00 149.39 ? 3217 GLU A CA    1 
ATOM   15198 C  C     . GLU A 1 3217 ? 175.392 213.246 232.510 1.00 148.80 ? 3217 GLU A C     1 
ATOM   15199 O  O     . GLU A 1 3217 ? 175.933 213.986 233.339 1.00 148.13 ? 3217 GLU A O     1 
ATOM   15200 C  CB    . GLU A 1 3217 ? 175.492 210.775 232.936 1.00 147.66 ? 3217 GLU A CB    1 
ATOM   15201 C  CG    . GLU A 1 3217 ? 174.880 209.561 233.617 1.00 146.11 ? 3217 GLU A CG    1 
ATOM   15202 C  CD    . GLU A 1 3217 ? 174.750 209.738 235.118 1.00 147.88 ? 3217 GLU A CD    1 
ATOM   15203 O  OE1   . GLU A 1 3217 ? 175.586 210.453 235.709 1.00 149.83 ? 3217 GLU A OE1   1 
ATOM   15204 O  OE2   . GLU A 1 3217 ? 173.812 209.161 235.706 1.00 147.77 ? 3217 GLU A OE2   1 
ATOM   15205 N  N     . LEU A 1 3218 ? 175.480 213.466 231.196 1.00 148.00 ? 3218 LEU A N     1 
ATOM   15206 C  CA    . LEU A 1 3218 ? 176.166 214.650 230.687 1.00 145.33 ? 3218 LEU A CA    1 
ATOM   15207 C  C     . LEU A 1 3218 ? 175.449 215.927 231.112 1.00 146.42 ? 3218 LEU A C     1 
ATOM   15208 O  O     . LEU A 1 3218 ? 176.092 216.939 231.413 1.00 146.67 ? 3218 LEU A O     1 
ATOM   15209 C  CB    . LEU A 1 3218 ? 176.286 214.573 229.164 1.00 145.02 ? 3218 LEU A CB    1 
ATOM   15210 C  CG    . LEU A 1 3218 ? 177.196 213.466 228.623 1.00 146.35 ? 3218 LEU A CG    1 
ATOM   15211 C  CD1   . LEU A 1 3218 ? 177.633 213.762 227.198 1.00 142.96 ? 3218 LEU A CD1   1 
ATOM   15212 C  CD2   . LEU A 1 3218 ? 178.409 213.271 229.523 1.00 147.27 ? 3218 LEU A CD2   1 
ATOM   15213 N  N     . ARG A 1 3219 ? 174.114 215.901 231.130 1.00 147.69 ? 3219 ARG A N     1 
ATOM   15214 C  CA    . ARG A 1 3219 ? 173.358 217.025 231.675 1.00 149.74 ? 3219 ARG A CA    1 
ATOM   15215 C  C     . ARG A 1 3219 ? 173.619 217.192 233.167 1.00 150.54 ? 3219 ARG A C     1 
ATOM   15216 O  O     . ARG A 1 3219 ? 173.663 218.318 233.676 1.00 149.16 ? 3219 ARG A O     1 
ATOM   15217 C  CB    . ARG A 1 3219 ? 171.863 216.836 231.418 1.00 146.53 ? 3219 ARG A CB    1 
ATOM   15218 C  CG    . ARG A 1 3219 ? 171.454 216.926 229.961 1.00 146.82 ? 3219 ARG A CG    1 
ATOM   15219 C  CD    . ARG A 1 3219 ? 169.941 216.908 229.834 1.00 146.80 ? 3219 ARG A CD    1 
ATOM   15220 N  NE    . ARG A 1 3219 ? 169.322 217.980 230.605 1.00 146.50 ? 3219 ARG A NE    1 
ATOM   15221 C  CZ    . ARG A 1 3219 ? 168.015 218.181 230.693 1.00 146.08 ? 3219 ARG A CZ    1 
ATOM   15222 N  NH1   . ARG A 1 3219 ? 167.151 217.399 230.067 1.00 143.33 ? 3219 ARG A NH1   1 
ATOM   15223 N  NH2   . ARG A 1 3219 ? 167.562 219.192 231.429 1.00 145.12 ? 3219 ARG A NH2   1 
ATOM   15224 N  N     . ARG A 1 3220 ? 173.780 216.077 233.885 1.00 150.89 ? 3220 ARG A N     1 
ATOM   15225 C  CA    . ARG A 1 3220 ? 174.049 216.138 235.319 1.00 153.21 ? 3220 ARG A CA    1 
ATOM   15226 C  C     . ARG A 1 3220 ? 175.324 216.920 235.620 1.00 154.68 ? 3220 ARG A C     1 
ATOM   15227 O  O     . ARG A 1 3220 ? 175.435 217.539 236.685 1.00 153.81 ? 3220 ARG A O     1 
ATOM   15228 C  CB    . ARG A 1 3220 ? 174.135 214.718 235.885 1.00 154.78 ? 3220 ARG A CB    1 
ATOM   15229 C  CG    . ARG A 1 3220 ? 174.685 214.611 237.299 1.00 155.93 ? 3220 ARG A CG    1 
ATOM   15230 C  CD    . ARG A 1 3220 ? 173.722 215.192 238.324 1.00 158.41 ? 3220 ARG A CD    1 
ATOM   15231 N  NE    . ARG A 1 3220 ? 174.259 215.134 239.679 1.00 163.06 ? 3220 ARG A NE    1 
ATOM   15232 C  CZ    . ARG A 1 3220 ? 174.437 214.018 240.374 1.00 162.61 ? 3220 ARG A CZ    1 
ATOM   15233 N  NH1   . ARG A 1 3220 ? 174.104 212.835 239.884 1.00 163.95 ? 3220 ARG A NH1   1 
ATOM   15234 N  NH2   . ARG A 1 3220 ? 174.958 214.092 241.596 1.00 157.80 ? 3220 ARG A NH2   1 
ATOM   15235 N  N     . ASP A 1 3221 ? 176.281 216.916 234.696 1.00 155.35 ? 3221 ASP A N     1 
ATOM   15236 C  CA    . ASP A 1 3221 ? 177.532 217.652 234.859 1.00 153.29 ? 3221 ASP A CA    1 
ATOM   15237 C  C     . ASP A 1 3221 ? 177.288 219.140 235.098 1.00 150.93 ? 3221 ASP A C     1 
ATOM   15238 O  O     . ASP A 1 3221 ? 177.945 219.991 234.499 1.00 147.57 ? 3221 ASP A O     1 
ATOM   15239 C  CB    . ASP A 1 3221 ? 178.422 217.466 233.629 1.00 151.43 ? 3221 ASP A CB    1 
ATOM   15240 C  CG    . ASP A 1 3221 ? 178.850 216.026 233.432 1.00 153.93 ? 3221 ASP A CG    1 
ATOM   15241 O  OD1   . ASP A 1 3221 ? 178.522 215.185 234.294 1.00 151.37 ? 3221 ASP A OD1   1 
ATOM   15242 O  OD2   . ASP A 1 3221 ? 179.513 215.737 232.414 1.00 156.44 ? 3221 ASP A OD2   1 
ATOM   15243 N  N     . ALA A 1 3470 ? 173.064 227.195 225.216 1.00 148.68 ? 3470 ALA A N     1 
ATOM   15244 C  CA    . ALA A 1 3470 ? 172.811 226.744 223.853 1.00 152.54 ? 3470 ALA A CA    1 
ATOM   15245 C  C     . ALA A 1 3470 ? 173.036 225.241 223.726 1.00 153.96 ? 3470 ALA A C     1 
ATOM   15246 O  O     . ALA A 1 3470 ? 172.269 224.543 223.062 1.00 153.56 ? 3470 ALA A O     1 
ATOM   15247 C  CB    . ALA A 1 3470 ? 173.694 227.500 222.871 1.00 149.57 ? 3470 ALA A CB    1 
ATOM   15248 N  N     . LYS A 1 3471 ? 174.099 224.751 224.367 1.00 153.35 ? 3471 LYS A N     1 
ATOM   15249 C  CA    . LYS A 1 3471 ? 174.397 223.323 224.323 1.00 150.99 ? 3471 LYS A CA    1 
ATOM   15250 C  C     . LYS A 1 3471 ? 173.338 222.511 225.058 1.00 151.38 ? 3471 LYS A C     1 
ATOM   15251 O  O     . LYS A 1 3471 ? 173.012 221.390 224.649 1.00 150.58 ? 3471 LYS A O     1 
ATOM   15252 C  CB    . LYS A 1 3471 ? 175.785 223.062 224.907 1.00 145.77 ? 3471 LYS A CB    1 
ATOM   15253 C  CG    . LYS A 1 3471 ? 176.030 223.723 226.254 1.00 146.64 ? 3471 LYS A CG    1 
ATOM   15254 C  CD    . LYS A 1 3471 ? 177.459 223.509 226.724 1.00 151.14 ? 3471 LYS A CD    1 
ATOM   15255 C  CE    . LYS A 1 3471 ? 177.737 224.260 228.017 1.00 149.05 ? 3471 LYS A CE    1 
ATOM   15256 N  NZ    . LYS A 1 3471 ? 177.569 225.730 227.855 1.00 141.52 ? 3471 LYS A NZ    1 
ATOM   15257 N  N     . VAL A 1 3472 ? 172.789 223.057 226.146 1.00 150.27 ? 3472 VAL A N     1 
ATOM   15258 C  CA    . VAL A 1 3472 ? 171.778 222.333 226.910 1.00 148.20 ? 3472 VAL A CA    1 
ATOM   15259 C  C     . VAL A 1 3472 ? 170.499 222.170 226.095 1.00 148.11 ? 3472 VAL A C     1 
ATOM   15260 O  O     . VAL A 1 3472 ? 169.852 221.115 226.135 1.00 149.33 ? 3472 VAL A O     1 
ATOM   15261 C  CB    . VAL A 1 3472 ? 171.519 223.035 228.255 1.00 146.12 ? 3472 VAL A CB    1 
ATOM   15262 C  CG1   . VAL A 1 3472 ? 172.728 222.888 229.164 1.00 141.41 ? 3472 VAL A CG1   1 
ATOM   15263 C  CG2   . VAL A 1 3472 ? 171.195 224.507 228.043 1.00 145.69 ? 3472 VAL A CG2   1 
ATOM   15264 N  N     . ASN A 1 3473 ? 170.113 223.203 225.341 1.00 147.63 ? 3473 ASN A N     1 
ATOM   15265 C  CA    . ASN A 1 3473 ? 168.933 223.092 224.488 1.00 148.34 ? 3473 ASN A CA    1 
ATOM   15266 C  C     . ASN A 1 3473 ? 169.141 222.049 223.399 1.00 148.47 ? 3473 ASN A C     1 
ATOM   15267 O  O     . ASN A 1 3473 ? 168.225 221.285 223.071 1.00 146.23 ? 3473 ASN A O     1 
ATOM   15268 C  CB    . ASN A 1 3473 ? 168.601 224.453 223.877 1.00 147.92 ? 3473 ASN A CB    1 
ATOM   15269 C  CG    . ASN A 1 3473 ? 168.487 225.547 224.919 1.00 148.32 ? 3473 ASN A CG    1 
ATOM   15270 O  OD1   . ASN A 1 3473 ? 169.199 226.550 224.863 1.00 147.73 ? 3473 ASN A OD1   1 
ATOM   15271 N  ND2   . ASN A 1 3473 ? 167.591 225.358 225.881 1.00 148.13 ? 3473 ASN A ND2   1 
ATOM   15272 N  N     . ARG A 1 3474 ? 170.346 222.000 222.828 1.00 149.18 ? 3474 ARG A N     1 
ATOM   15273 C  CA    . ARG A 1 3474 ? 170.655 220.984 221.828 1.00 148.98 ? 3474 ARG A CA    1 
ATOM   15274 C  C     . ARG A 1 3474 ? 170.615 219.586 222.434 1.00 147.80 ? 3474 ARG A C     1 
ATOM   15275 O  O     . ARG A 1 3474 ? 170.146 218.636 221.796 1.00 148.11 ? 3474 ARG A O     1 
ATOM   15276 C  CB    . ARG A 1 3474 ? 172.016 221.279 221.198 1.00 149.69 ? 3474 ARG A CB    1 
ATOM   15277 C  CG    . ARG A 1 3474 ? 171.956 222.304 220.074 1.00 150.04 ? 3474 ARG A CG    1 
ATOM   15278 C  CD    . ARG A 1 3474 ? 173.170 223.228 220.056 1.00 153.89 ? 3474 ARG A CD    1 
ATOM   15279 N  NE    . ARG A 1 3474 ? 174.425 222.527 220.304 1.00 156.14 ? 3474 ARG A NE    1 
ATOM   15280 C  CZ    . ARG A 1 3474 ? 175.495 223.083 220.855 1.00 155.55 ? 3474 ARG A CZ    1 
ATOM   15281 N  NH1   . ARG A 1 3474 ? 175.499 224.351 221.232 1.00 152.85 ? 3474 ARG A NH1   1 
ATOM   15282 N  NH2   . ARG A 1 3474 ? 176.591 222.350 221.030 1.00 153.70 ? 3474 ARG A NH2   1 
ATOM   15283 N  N     . SER A 1 3475 ? 171.093 219.439 223.673 1.00 146.63 ? 3475 SER A N     1 
ATOM   15284 C  CA    . SER A 1 3475 ? 171.013 218.144 224.345 1.00 146.80 ? 3475 SER A CA    1 
ATOM   15285 C  C     . SER A 1 3475 ? 169.564 217.739 224.602 1.00 146.29 ? 3475 SER A C     1 
ATOM   15286 O  O     . SER A 1 3475 ? 169.211 216.562 224.473 1.00 143.83 ? 3475 SER A O     1 
ATOM   15287 C  CB    . SER A 1 3475 ? 171.803 218.180 225.652 1.00 143.58 ? 3475 SER A CB    1 
ATOM   15288 O  OG    . SER A 1 3475 ? 171.293 219.164 226.533 1.00 142.74 ? 3475 SER A OG    1 
ATOM   15289 N  N     . THR A 1 3476 ? 168.713 218.697 224.979 1.00 146.85 ? 3476 THR A N     1 
ATOM   15290 C  CA    . THR A 1 3476 ? 167.297 218.389 225.169 1.00 144.67 ? 3476 THR A CA    1 
ATOM   15291 C  C     . THR A 1 3476 ? 166.638 217.984 223.854 1.00 144.16 ? 3476 THR A C     1 
ATOM   15292 O  O     . THR A 1 3476 ? 165.793 217.079 223.823 1.00 141.31 ? 3476 THR A O     1 
ATOM   15293 C  CB    . THR A 1 3476 ? 166.570 219.583 225.786 1.00 143.16 ? 3476 THR A CB    1 
ATOM   15294 O  OG1   . THR A 1 3476 ? 166.736 220.734 224.949 1.00 146.34 ? 3476 THR A OG1   1 
ATOM   15295 C  CG2   . THR A 1 3476 ? 167.114 219.881 227.176 1.00 138.21 ? 3476 THR A CG2   1 
ATOM   15296 N  N     . ALA A 1 3477 ? 167.006 218.652 222.757 1.00 143.73 ? 3477 ALA A N     1 
ATOM   15297 C  CA    . ALA A 1 3477 ? 166.503 218.249 221.447 1.00 142.33 ? 3477 ALA A CA    1 
ATOM   15298 C  C     . ALA A 1 3477 ? 166.961 216.839 221.096 1.00 143.67 ? 3477 ALA A C     1 
ATOM   15299 O  O     . ALA A 1 3477 ? 166.198 216.051 220.522 1.00 143.42 ? 3477 ALA A O     1 
ATOM   15300 C  CB    . ALA A 1 3477 ? 166.956 219.246 220.381 1.00 137.00 ? 3477 ALA A CB    1 
ATOM   15301 N  N     . LEU A 1 3478 ? 168.210 216.506 221.433 1.00 141.88 ? 3478 LEU A N     1 
ATOM   15302 C  CA    . LEU A 1 3478 ? 168.697 215.144 221.237 1.00 139.80 ? 3478 LEU A CA    1 
ATOM   15303 C  C     . LEU A 1 3478 ? 167.885 214.145 222.049 1.00 139.63 ? 3478 LEU A C     1 
ATOM   15304 O  O     . LEU A 1 3478 ? 167.563 213.055 221.565 1.00 140.07 ? 3478 LEU A O     1 
ATOM   15305 C  CB    . LEU A 1 3478 ? 170.178 215.060 221.608 1.00 138.85 ? 3478 LEU A CB    1 
ATOM   15306 C  CG    . LEU A 1 3478 ? 170.835 213.681 221.521 1.00 134.40 ? 3478 LEU A CG    1 
ATOM   15307 C  CD1   . LEU A 1 3478 ? 170.721 213.106 220.119 1.00 134.84 ? 3478 LEU A CD1   1 
ATOM   15308 C  CD2   . LEU A 1 3478 ? 172.289 213.759 221.955 1.00 133.59 ? 3478 LEU A CD2   1 
ATOM   15309 N  N     . LEU A 1 3479 ? 167.555 214.498 223.292 1.00 137.54 ? 3479 LEU A N     1 
ATOM   15310 C  CA    . LEU A 1 3479 ? 166.731 213.624 224.122 1.00 137.36 ? 3479 LEU A CA    1 
ATOM   15311 C  C     . LEU A 1 3479 ? 165.360 213.399 223.495 1.00 137.45 ? 3479 LEU A C     1 
ATOM   15312 O  O     . LEU A 1 3479 ? 164.856 212.268 223.466 1.00 136.99 ? 3479 LEU A O     1 
ATOM   15313 C  CB    . LEU A 1 3479 ? 166.588 214.220 225.521 1.00 139.19 ? 3479 LEU A CB    1 
ATOM   15314 C  CG    . LEU A 1 3479 ? 167.721 213.955 226.511 1.00 138.89 ? 3479 LEU A CG    1 
ATOM   15315 C  CD1   . LEU A 1 3479 ? 167.717 215.000 227.611 1.00 141.07 ? 3479 LEU A CD1   1 
ATOM   15316 C  CD2   . LEU A 1 3479 ? 167.572 212.566 227.102 1.00 140.58 ? 3479 LEU A CD2   1 
ATOM   15317 N  N     . LYS A 1 3480 ? 164.742 214.468 222.987 1.00 138.16 ? 3480 LYS A N     1 
ATOM   15318 C  CA    . LYS A 1 3480 ? 163.435 214.334 222.347 1.00 139.09 ? 3480 LYS A CA    1 
ATOM   15319 C  C     . LYS A 1 3480 ? 163.516 213.452 221.105 1.00 138.08 ? 3480 LYS A C     1 
ATOM   15320 O  O     . LYS A 1 3480 ? 162.647 212.598 220.878 1.00 137.87 ? 3480 LYS A O     1 
ATOM   15321 C  CB    . LYS A 1 3480 ? 162.882 215.714 221.994 1.00 138.57 ? 3480 LYS A CB    1 
ATOM   15322 C  CG    . LYS A 1 3480 ? 161.607 215.686 221.165 1.00 139.88 ? 3480 LYS A CG    1 
ATOM   15323 C  CD    . LYS A 1 3480 ? 160.505 214.899 221.859 1.00 139.88 ? 3480 LYS A CD    1 
ATOM   15324 C  CE    . LYS A 1 3480 ? 159.307 214.709 220.944 1.00 136.10 ? 3480 LYS A CE    1 
ATOM   15325 N  NZ    . LYS A 1 3480 ? 158.261 213.854 221.566 1.00 137.06 ? 3480 LYS A NZ    1 
ATOM   15326 N  N     . SER A 1 3481 ? 164.556 213.644 220.289 1.00 138.53 ? 3481 SER A N     1 
ATOM   15327 C  CA    . SER A 1 3481 ? 164.727 212.816 219.099 1.00 137.63 ? 3481 SER A CA    1 
ATOM   15328 C  C     . SER A 1 3481 ? 164.933 211.352 219.471 1.00 135.06 ? 3481 SER A C     1 
ATOM   15329 O  O     . SER A 1 3481 ? 164.384 210.453 218.822 1.00 132.19 ? 3481 SER A O     1 
ATOM   15330 C  CB    . SER A 1 3481 ? 165.903 213.330 218.269 1.00 136.90 ? 3481 SER A CB    1 
ATOM   15331 O  OG    . SER A 1 3481 ? 165.786 214.721 218.030 1.00 140.60 ? 3481 SER A OG    1 
ATOM   15332 N  N     . LEU A 1 3482 ? 165.725 211.097 220.517 1.00 134.07 ? 3482 LEU A N     1 
ATOM   15333 C  CA    . LEU A 1 3482 ? 165.946 209.728 220.969 1.00 131.81 ? 3482 LEU A CA    1 
ATOM   15334 C  C     . LEU A 1 3482 ? 164.648 209.090 221.443 1.00 134.04 ? 3482 LEU A C     1 
ATOM   15335 O  O     . LEU A 1 3482 ? 164.383 207.920 221.150 1.00 135.57 ? 3482 LEU A O     1 
ATOM   15336 C  CB    . LEU A 1 3482 ? 166.991 209.707 222.084 1.00 130.58 ? 3482 LEU A CB    1 
ATOM   15337 C  CG    . LEU A 1 3482 ? 168.450 209.931 221.678 1.00 132.16 ? 3482 LEU A CG    1 
ATOM   15338 C  CD1   . LEU A 1 3482 ? 169.365 209.824 222.888 1.00 136.03 ? 3482 LEU A CD1   1 
ATOM   15339 C  CD2   . LEU A 1 3482 ? 168.870 208.946 220.602 1.00 128.84 ? 3482 LEU A CD2   1 
ATOM   15340 N  N     . SER A 1 3483 ? 163.825 209.844 222.178 1.00 132.97 ? 3483 SER A N     1 
ATOM   15341 C  CA    . SER A 1 3483 ? 162.545 209.308 222.633 1.00 130.66 ? 3483 SER A CA    1 
ATOM   15342 C  C     . SER A 1 3483 ? 161.627 208.984 221.458 1.00 127.63 ? 3483 SER A C     1 
ATOM   15343 O  O     . SER A 1 3483 ? 160.969 207.933 221.440 1.00 125.81 ? 3483 SER A O     1 
ATOM   15344 C  CB    . SER A 1 3483 ? 161.871 210.297 223.583 1.00 129.87 ? 3483 SER A CB    1 
ATOM   15345 O  OG    . SER A 1 3483 ? 160.581 209.848 223.956 1.00 127.36 ? 3483 SER A OG    1 
ATOM   15346 N  N     . ALA A 1 3484 ? 161.565 209.881 220.469 1.00 128.15 ? 3484 ALA A N     1 
ATOM   15347 C  CA    . ALA A 1 3484 ? 160.723 209.628 219.302 1.00 129.13 ? 3484 ALA A CA    1 
ATOM   15348 C  C     . ALA A 1 3484 ? 161.190 208.392 218.543 1.00 128.25 ? 3484 ALA A C     1 
ATOM   15349 O  O     . ALA A 1 3484 ? 160.372 207.555 218.132 1.00 127.12 ? 3484 ALA A O     1 
ATOM   15350 C  CB    . ALA A 1 3484 ? 160.714 210.852 218.387 1.00 130.39 ? 3484 ALA A CB    1 
ATOM   15351 N  N     . GLU A 1 3485 ? 162.505 208.257 218.355 1.00 127.38 ? 3485 GLU A N     1 
ATOM   15352 C  CA    . GLU A 1 3485 ? 163.039 207.078 217.682 1.00 125.83 ? 3485 GLU A CA    1 
ATOM   15353 C  C     . GLU A 1 3485 ? 162.742 205.813 218.479 1.00 126.33 ? 3485 GLU A C     1 
ATOM   15354 O  O     . GLU A 1 3485 ? 162.415 204.766 217.904 1.00 124.34 ? 3485 GLU A O     1 
ATOM   15355 C  CB    . GLU A 1 3485 ? 164.541 207.248 217.461 1.00 120.93 ? 3485 GLU A CB    1 
ATOM   15356 C  CG    . GLU A 1 3485 ? 165.232 206.026 216.901 1.00 123.97 ? 3485 GLU A CG    1 
ATOM   15357 C  CD    . GLU A 1 3485 ? 166.503 206.372 216.157 1.00 124.34 ? 3485 GLU A CD    1 
ATOM   15358 O  OE1   . GLU A 1 3485 ? 167.568 206.456 216.804 1.00 121.80 ? 3485 GLU A OE1   1 
ATOM   15359 O  OE2   . GLU A 1 3485 ? 166.437 206.561 214.924 1.00 126.97 ? 3485 GLU A OE2   1 
ATOM   15360 N  N     . ARG A 1 3486 ? 162.838 205.894 219.807 1.00 123.76 ? 3486 ARG A N     1 
ATOM   15361 C  CA    . ARG A 1 3486 ? 162.484 204.756 220.647 1.00 120.67 ? 3486 ARG A CA    1 
ATOM   15362 C  C     . ARG A 1 3486 ? 161.049 204.314 220.389 1.00 121.09 ? 3486 ARG A C     1 
ATOM   15363 O  O     . ARG A 1 3486 ? 160.800 203.145 220.069 1.00 120.58 ? 3486 ARG A O     1 
ATOM   15364 C  CB    . ARG A 1 3486 ? 162.687 205.116 222.119 1.00 121.57 ? 3486 ARG A CB    1 
ATOM   15365 C  CG    . ARG A 1 3486 ? 162.522 203.953 223.080 1.00 120.01 ? 3486 ARG A CG    1 
ATOM   15366 C  CD    . ARG A 1 3486 ? 162.662 204.413 224.523 1.00 118.03 ? 3486 ARG A CD    1 
ATOM   15367 N  NE    . ARG A 1 3486 ? 161.662 205.408 224.892 1.00 126.09 ? 3486 ARG A NE    1 
ATOM   15368 C  CZ    . ARG A 1 3486 ? 160.371 205.154 225.062 1.00 127.39 ? 3486 ARG A CZ    1 
ATOM   15369 N  NH1   . ARG A 1 3486 ? 159.879 203.935 224.916 1.00 127.18 ? 3486 ARG A NH1   1 
ATOM   15370 N  NH2   . ARG A 1 3486 ? 159.553 206.150 225.392 1.00 122.38 ? 3486 ARG A NH2   1 
ATOM   15371 N  N     . GLU A 1 3487 ? 160.099 205.253 220.474 1.00 120.03 ? 3487 GLU A N     1 
ATOM   15372 C  CA    . GLU A 1 3487 ? 158.693 204.908 220.260 1.00 119.58 ? 3487 GLU A CA    1 
ATOM   15373 C  C     . GLU A 1 3487 ? 158.477 204.312 218.873 1.00 119.24 ? 3487 GLU A C     1 
ATOM   15374 O  O     . GLU A 1 3487 ? 157.707 203.349 218.706 1.00 117.06 ? 3487 GLU A O     1 
ATOM   15375 C  CB    . GLU A 1 3487 ? 157.811 206.140 220.462 1.00 123.44 ? 3487 GLU A CB    1 
ATOM   15376 C  CG    . GLU A 1 3487 ? 158.018 206.839 221.795 1.00 127.64 ? 3487 GLU A CG    1 
ATOM   15377 C  CD    . GLU A 1 3487 ? 157.722 208.324 221.727 1.00 133.16 ? 3487 GLU A CD    1 
ATOM   15378 O  OE1   . GLU A 1 3487 ? 157.611 208.960 222.796 1.00 133.47 ? 3487 GLU A OE1   1 
ATOM   15379 O  OE2   . GLU A 1 3487 ? 157.602 208.857 220.604 1.00 131.84 ? 3487 GLU A OE2   1 
ATOM   15380 N  N     . ARG A 1 3488 ? 159.155 204.870 217.866 1.00 121.61 ? 3488 ARG A N     1 
ATOM   15381 C  CA    . ARG A 1 3488 ? 159.152 204.258 216.542 1.00 118.18 ? 3488 ARG A CA    1 
ATOM   15382 C  C     . ARG A 1 3488 ? 159.609 202.807 216.611 1.00 116.00 ? 3488 ARG A C     1 
ATOM   15383 O  O     . ARG A 1 3488 ? 159.081 201.940 215.905 1.00 115.03 ? 3488 ARG A O     1 
ATOM   15384 C  CB    . ARG A 1 3488 ? 160.048 205.061 215.597 1.00 114.31 ? 3488 ARG A CB    1 
ATOM   15385 C  CG    . ARG A 1 3488 ? 159.891 204.713 214.129 1.00 112.39 ? 3488 ARG A CG    1 
ATOM   15386 C  CD    . ARG A 1 3488 ? 161.036 205.283 213.311 1.00 116.69 ? 3488 ARG A CD    1 
ATOM   15387 N  NE    . ARG A 1 3488 ? 162.180 204.382 213.262 1.00 120.02 ? 3488 ARG A NE    1 
ATOM   15388 C  CZ    . ARG A 1 3488 ? 163.299 204.629 212.595 1.00 120.20 ? 3488 ARG A CZ    1 
ATOM   15389 N  NH1   . ARG A 1 3488 ? 163.468 205.754 211.920 1.00 121.57 ? 3488 ARG A NH1   1 
ATOM   15390 N  NH2   . ARG A 1 3488 ? 164.273 203.723 212.603 1.00 120.60 ? 3488 ARG A NH2   1 
ATOM   15391 N  N     . TRP A 1 3489 ? 160.577 202.515 217.475 1.00 113.80 ? 3489 TRP A N     1 
ATOM   15392 C  CA    . TRP A 1 3489 ? 161.086 201.150 217.523 1.00 112.74 ? 3489 TRP A CA    1 
ATOM   15393 C  C     . TRP A 1 3489 ? 160.146 200.191 218.255 1.00 111.73 ? 3489 TRP A C     1 
ATOM   15394 O  O     . TRP A 1 3489 ? 160.050 199.023 217.862 1.00 113.62 ? 3489 TRP A O     1 
ATOM   15395 C  CB    . TRP A 1 3489 ? 162.490 201.138 218.125 1.00 112.36 ? 3489 TRP A CB    1 
ATOM   15396 C  CG    . TRP A 1 3489 ? 163.474 201.833 217.227 1.00 110.50 ? 3489 TRP A CG    1 
ATOM   15397 C  CD1   . TRP A 1 3489 ? 163.191 202.499 216.070 1.00 114.89 ? 3489 TRP A CD1   1 
ATOM   15398 C  CD2   . TRP A 1 3489 ? 164.892 201.915 217.396 1.00 111.29 ? 3489 TRP A CD2   1 
ATOM   15399 N  NE1   . TRP A 1 3489 ? 164.339 203.002 215.517 1.00 118.52 ? 3489 TRP A NE1   1 
ATOM   15400 C  CE2   . TRP A 1 3489 ? 165.399 202.654 216.309 1.00 116.39 ? 3489 TRP A CE2   1 
ATOM   15401 C  CE3   . TRP A 1 3489 ? 165.781 201.440 218.359 1.00 117.51 ? 3489 TRP A CE3   1 
ATOM   15402 C  CZ2   . TRP A 1 3489 ? 166.754 202.932 216.164 1.00 119.48 ? 3489 TRP A CZ2   1 
ATOM   15403 C  CZ3   . TRP A 1 3489 ? 167.125 201.714 218.208 1.00 123.47 ? 3489 TRP A CZ3   1 
ATOM   15404 C  CH2   . TRP A 1 3489 ? 167.599 202.455 217.122 1.00 123.03 ? 3489 TRP A CH2   1 
ATOM   15405 N  N     . GLU A 1 3490 ? 159.424 200.640 219.290 1.00 112.13 ? 3490 GLU A N     1 
ATOM   15406 C  CA    . GLU A 1 3490 ? 158.408 199.731 219.840 1.00 113.21 ? 3490 GLU A CA    1 
ATOM   15407 C  C     . GLU A 1 3490 ? 157.270 199.487 218.849 1.00 113.14 ? 3490 GLU A C     1 
ATOM   15408 O  O     . GLU A 1 3490 ? 156.745 198.367 218.770 1.00 111.16 ? 3490 GLU A O     1 
ATOM   15409 C  CB    . GLU A 1 3490 ? 157.819 200.166 221.194 1.00 111.69 ? 3490 GLU A CB    1 
ATOM   15410 C  CG    . GLU A 1 3490 ? 158.743 200.116 222.418 1.00 115.10 ? 3490 GLU A CG    1 
ATOM   15411 C  CD    . GLU A 1 3490 ? 159.585 201.337 222.601 1.00 119.83 ? 3490 GLU A CD    1 
ATOM   15412 O  OE1   . GLU A 1 3490 ? 159.396 202.275 221.825 1.00 123.29 ? 3490 GLU A OE1   1 
ATOM   15413 O  OE2   . GLU A 1 3490 ? 160.434 201.358 223.518 1.00 119.03 ? 3490 GLU A OE2   1 
ATOM   15414 N  N     . LYS A 1 3491 ? 156.862 200.505 218.082 1.00 113.54 ? 3491 LYS A N     1 
ATOM   15415 C  CA    . LYS A 1 3491 ? 155.823 200.208 217.094 1.00 111.44 ? 3491 LYS A CA    1 
ATOM   15416 C  C     . LYS A 1 3491 ? 156.358 199.295 215.990 1.00 109.21 ? 3491 LYS A C     1 
ATOM   15417 O  O     . LYS A 1 3491 ? 155.613 198.464 215.448 1.00 108.11 ? 3491 LYS A O     1 
ATOM   15418 C  CB    . LYS A 1 3491 ? 155.217 201.492 216.518 1.00 109.03 ? 3491 LYS A CB    1 
ATOM   15419 C  CG    . LYS A 1 3491 ? 156.128 202.354 215.676 1.00 109.97 ? 3491 LYS A CG    1 
ATOM   15420 C  CD    . LYS A 1 3491 ? 155.400 203.610 215.217 1.00 114.24 ? 3491 LYS A CD    1 
ATOM   15421 C  CE    . LYS A 1 3491 ? 156.285 204.487 214.347 1.00 117.86 ? 3491 LYS A CE    1 
ATOM   15422 N  NZ    . LYS A 1 3491 ? 155.583 205.722 213.902 1.00 114.56 ? 3491 LYS A NZ    1 
ATOM   15423 N  N     . THR A 1 3492 ? 157.654 199.398 215.678 1.00 108.01 ? 3492 THR A N     1 
ATOM   15424 C  CA    . THR A 1 3492 ? 158.275 198.436 214.772 1.00 106.92 ? 3492 THR A CA    1 
ATOM   15425 C  C     . THR A 1 3492 ? 158.235 197.026 215.354 1.00 109.55 ? 3492 THR A C     1 
ATOM   15426 O  O     . THR A 1 3492 ? 158.019 196.050 214.626 1.00 108.20 ? 3492 THR A O     1 
ATOM   15427 C  CB    . THR A 1 3492 ? 159.714 198.853 214.474 1.00 102.16 ? 3492 THR A CB    1 
ATOM   15428 O  OG1   . THR A 1 3492 ? 159.752 200.251 214.161 1.00 102.79 ? 3492 THR A OG1   1 
ATOM   15429 C  CG2   . THR A 1 3492 ? 160.260 198.069 213.294 1.00 103.77 ? 3492 THR A CG2   1 
ATOM   15430 N  N     . SER A 1 3493 ? 158.454 196.899 216.666 1.00 110.68 ? 3493 SER A N     1 
ATOM   15431 C  CA    . SER A 1 3493 ? 158.340 195.595 217.319 1.00 108.88 ? 3493 SER A CA    1 
ATOM   15432 C  C     . SER A 1 3493 ? 156.927 195.035 217.189 1.00 107.62 ? 3493 SER A C     1 
ATOM   15433 O  O     . SER A 1 3493 ? 156.739 193.830 216.969 1.00 106.85 ? 3493 SER A O     1 
ATOM   15434 C  CB    . SER A 1 3493 ? 158.731 195.708 218.792 1.00 105.75 ? 3493 SER A CB    1 
ATOM   15435 O  OG    . SER A 1 3493 ? 160.103 196.021 218.943 1.00 100.86 ? 3493 SER A OG    1 
ATOM   15436 N  N     . GLU A 1 3494 ? 155.920 195.897 217.342 1.00 106.66 ? 3494 GLU A N     1 
ATOM   15437 C  CA    . GLU A 1 3494 ? 154.539 195.455 217.154 1.00 109.92 ? 3494 GLU A CA    1 
ATOM   15438 C  C     . GLU A 1 3494 ? 154.317 194.944 215.733 1.00 107.40 ? 3494 GLU A C     1 
ATOM   15439 O  O     . GLU A 1 3494 ? 153.672 193.904 215.523 1.00 106.75 ? 3494 GLU A O     1 
ATOM   15440 C  CB    . GLU A 1 3494 ? 153.577 196.600 217.470 1.00 108.05 ? 3494 GLU A CB    1 
ATOM   15441 C  CG    . GLU A 1 3494 ? 153.430 196.900 218.952 1.00 111.72 ? 3494 GLU A CG    1 
ATOM   15442 C  CD    . GLU A 1 3494 ? 152.805 195.757 219.723 1.00 119.08 ? 3494 GLU A CD    1 
ATOM   15443 O  OE1   . GLU A 1 3494 ? 151.733 195.271 219.304 1.00 116.55 ? 3494 GLU A OE1   1 
ATOM   15444 O  OE2   . GLU A 1 3494 ? 153.387 195.343 220.748 1.00 120.17 ? 3494 GLU A OE2   1 
ATOM   15445 N  N     . THR A 1 3495 ? 154.851 195.662 214.742 1.00 105.49 ? 3495 THR A N     1 
ATOM   15446 C  CA    . THR A 1 3495 ? 154.751 195.196 213.360 1.00 105.19 ? 3495 THR A CA    1 
ATOM   15447 C  C     . THR A 1 3495 ? 155.443 193.846 213.182 1.00 102.26 ? 3495 THR A C     1 
ATOM   15448 O  O     . THR A 1 3495 ? 154.959 192.979 212.442 1.00 99.82  ? 3495 THR A O     1 
ATOM   15449 C  CB    . THR A 1 3495 ? 155.345 196.237 212.410 1.00 108.20 ? 3495 THR A CB    1 
ATOM   15450 O  OG1   . THR A 1 3495 ? 154.736 197.511 212.654 1.00 105.62 ? 3495 THR A OG1   1 
ATOM   15451 C  CG2   . THR A 1 3495 ? 155.101 195.842 210.963 1.00 104.90 ? 3495 THR A CG2   1 
ATOM   15452 N  N     . PHE A 1 3496 ? 156.578 193.652 213.857 1.00 102.93 ? 3496 PHE A N     1 
ATOM   15453 C  CA    . PHE A 1 3496 ? 157.279 192.372 213.783 1.00 101.27 ? 3496 PHE A CA    1 
ATOM   15454 C  C     . PHE A 1 3496 ? 156.426 191.242 214.348 1.00 98.47  ? 3496 PHE A C     1 
ATOM   15455 O  O     . PHE A 1 3496 ? 156.415 190.128 213.809 1.00 97.26  ? 3496 PHE A O     1 
ATOM   15456 C  CB    . PHE A 1 3496 ? 158.610 192.456 214.529 1.00 102.92 ? 3496 PHE A CB    1 
ATOM   15457 C  CG    . PHE A 1 3496 ? 159.707 193.121 213.746 1.00 103.57 ? 3496 PHE A CG    1 
ATOM   15458 C  CD1   . PHE A 1 3496 ? 159.972 192.744 212.442 1.00 100.09 ? 3496 PHE A CD1   1 
ATOM   15459 C  CD2   . PHE A 1 3496 ? 160.483 194.112 214.322 1.00 102.17 ? 3496 PHE A CD2   1 
ATOM   15460 C  CE1   . PHE A 1 3496 ? 160.982 193.352 211.723 1.00 97.18  ? 3496 PHE A CE1   1 
ATOM   15461 C  CE2   . PHE A 1 3496 ? 161.495 194.721 213.608 1.00 100.52 ? 3496 PHE A CE2   1 
ATOM   15462 C  CZ    . PHE A 1 3496 ? 161.744 194.341 212.307 1.00 98.48  ? 3496 PHE A CZ    1 
ATOM   15463 N  N     . LYS A 1 3497 ? 155.721 191.505 215.450 1.00 98.55  ? 3497 LYS A N     1 
ATOM   15464 C  CA    . LYS A 1 3497 ? 154.824 190.493 216.007 1.00 94.69  ? 3497 LYS A CA    1 
ATOM   15465 C  C     . LYS A 1 3497 ? 153.691 190.161 215.038 1.00 95.10  ? 3497 LYS A C     1 
ATOM   15466 O  O     . LYS A 1 3497 ? 153.315 188.990 214.878 1.00 93.37  ? 3497 LYS A O     1 
ATOM   15467 C  CB    . LYS A 1 3497 ? 154.274 190.965 217.352 1.00 96.05  ? 3497 LYS A CB    1 
ATOM   15468 C  CG    . LYS A 1 3497 ? 155.339 191.083 218.431 1.00 102.40 ? 3497 LYS A CG    1 
ATOM   15469 C  CD    . LYS A 1 3497 ? 154.757 191.539 219.756 1.00 106.82 ? 3497 LYS A CD    1 
ATOM   15470 C  CE    . LYS A 1 3497 ? 155.821 191.558 220.842 1.00 102.76 ? 3497 LYS A CE    1 
ATOM   15471 N  NZ    . LYS A 1 3497 ? 156.863 192.591 220.591 1.00 97.99  ? 3497 LYS A NZ    1 
ATOM   15472 N  N     . ASN A 1 3498 ? 153.140 191.177 214.371 1.00 99.28  ? 3498 ASN A N     1 
ATOM   15473 C  CA    . ASN A 1 3498 ? 152.125 190.901 213.353 1.00 94.87  ? 3498 ASN A CA    1 
ATOM   15474 C  C     . ASN A 1 3498 ? 152.689 190.037 212.226 1.00 89.40  ? 3498 ASN A C     1 
ATOM   15475 O  O     . ASN A 1 3498 ? 152.009 189.138 211.711 1.00 88.51  ? 3498 ASN A O     1 
ATOM   15476 C  CB    . ASN A 1 3498 ? 151.558 192.208 212.802 1.00 97.95  ? 3498 ASN A CB    1 
ATOM   15477 C  CG    . ASN A 1 3498 ? 150.659 192.918 213.795 1.00 102.47 ? 3498 ASN A CG    1 
ATOM   15478 O  OD1   . ASN A 1 3498 ? 151.068 193.229 214.913 1.00 101.34 ? 3498 ASN A OD1   1 
ATOM   15479 N  ND2   . ASN A 1 3498 ? 149.423 193.179 213.388 1.00 107.33 ? 3498 ASN A ND2   1 
ATOM   15480 N  N     . GLN A 1 3499 ? 153.936 190.284 211.832 1.00 87.60  ? 3499 GLN A N     1 
ATOM   15481 C  CA    . GLN A 1 3499 ? 154.513 189.474 210.764 1.00 84.83  ? 3499 GLN A CA    1 
ATOM   15482 C  C     . GLN A 1 3499 ? 154.776 188.039 211.225 1.00 79.94  ? 3499 GLN A C     1 
ATOM   15483 O  O     . GLN A 1 3499 ? 154.661 187.101 210.429 1.00 78.45  ? 3499 GLN A O     1 
ATOM   15484 C  CB    . GLN A 1 3499 ? 155.778 190.137 210.232 1.00 90.92  ? 3499 GLN A CB    1 
ATOM   15485 C  CG    . GLN A 1 3499 ? 155.512 191.455 209.522 1.00 99.14  ? 3499 GLN A CG    1 
ATOM   15486 C  CD    . GLN A 1 3499 ? 156.775 192.118 209.013 1.00 101.72 ? 3499 GLN A CD    1 
ATOM   15487 O  OE1   . GLN A 1 3499 ? 157.882 191.632 209.240 1.00 96.61  ? 3499 GLN A OE1   1 
ATOM   15488 N  NE2   . GLN A 1 3499 ? 156.614 193.235 208.312 1.00 106.88 ? 3499 GLN A NE2   1 
ATOM   15489 N  N     . MET A 1 3500 ? 155.146 187.849 212.497 1.00 82.50  ? 3500 MET A N     1 
ATOM   15490 C  CA    . MET A 1 3500 ? 155.040 186.517 213.102 1.00 79.75  ? 3500 MET A CA    1 
ATOM   15491 C  C     . MET A 1 3500 ? 153.666 185.905 212.883 1.00 79.14  ? 3500 MET A C     1 
ATOM   15492 O  O     . MET A 1 3500 ? 153.556 184.732 212.507 1.00 81.44  ? 3500 MET A O     1 
ATOM   15493 C  CB    . MET A 1 3500 ? 155.359 186.575 214.599 1.00 88.98  ? 3500 MET A CB    1 
ATOM   15494 C  CG    . MET A 1 3500 ? 156.795 186.863 214.958 1.00 98.82  ? 3500 MET A CG    1 
ATOM   15495 S  SD    . MET A 1 3500 ? 157.788 185.468 214.363 1.00 118.20 ? 3500 MET A SD    1 
ATOM   15496 C  CE    . MET A 1 3500 ? 158.531 186.067 212.870 1.00 93.00  ? 3500 MET A CE    1 
ATOM   15497 N  N     . SER A 1 3501 ? 152.609 186.678 213.123 1.00 80.46  ? 3501 SER A N     1 
ATOM   15498 C  CA    . SER A 1 3501 ? 151.264 186.137 212.941 1.00 79.64  ? 3501 SER A CA    1 
ATOM   15499 C  C     . SER A 1 3501 ? 151.004 185.753 211.485 1.00 71.78  ? 3501 SER A C     1 
ATOM   15500 O  O     . SER A 1 3501 ? 150.187 184.868 211.206 1.00 72.99  ? 3501 SER A O     1 
ATOM   15501 C  CB    . SER A 1 3501 ? 150.216 187.141 213.425 1.00 81.62  ? 3501 SER A CB    1 
ATOM   15502 O  OG    . SER A 1 3501 ? 148.904 186.643 213.224 1.00 78.69  ? 3501 SER A OG    1 
ATOM   15503 N  N     . THR A 1 3502 ? 151.692 186.403 210.545 1.00 69.20  ? 3502 THR A N     1 
ATOM   15504 C  CA    . THR A 1 3502 ? 151.352 186.286 209.125 1.00 60.90  ? 3502 THR A CA    1 
ATOM   15505 C  C     . THR A 1 3502 ? 152.231 185.297 208.336 1.00 53.45  ? 3502 THR A C     1 
ATOM   15506 O  O     . THR A 1 3502 ? 151.799 184.794 207.278 1.00 49.59  ? 3502 THR A O     1 
ATOM   15507 C  CB    . THR A 1 3502 ? 151.421 187.691 208.507 1.00 70.35  ? 3502 THR A CB    1 
ATOM   15508 O  OG1   . THR A 1 3502 ? 150.494 188.542 209.190 1.00 76.95  ? 3502 THR A OG1   1 
ATOM   15509 C  CG2   . THR A 1 3502 ? 151.027 187.685 207.061 1.00 66.84  ? 3502 THR A CG2   1 
ATOM   15510 N  N     . ILE A 1 3503 ? 153.431 184.981 208.839 1.00 60.41  ? 3503 ILE A N     1 
ATOM   15511 C  CA    . ILE A 1 3503 ? 154.411 184.211 208.063 1.00 56.08  ? 3503 ILE A CA    1 
ATOM   15512 C  C     . ILE A 1 3503 ? 153.913 182.822 207.678 1.00 43.24  ? 3503 ILE A C     1 
ATOM   15513 O  O     . ILE A 1 3503 ? 154.242 182.329 206.595 1.00 38.95  ? 3503 ILE A O     1 
ATOM   15514 C  CB    . ILE A 1 3503 ? 155.761 184.135 208.810 1.00 53.49  ? 3503 ILE A CB    1 
ATOM   15515 C  CG1   . ILE A 1 3503 ? 156.485 185.475 208.735 1.00 61.78  ? 3503 ILE A CG1   1 
ATOM   15516 C  CG2   . ILE A 1 3503 ? 156.649 183.034 208.267 1.00 42.09  ? 3503 ILE A CG2   1 
ATOM   15517 C  CD1   . ILE A 1 3503 ? 157.722 185.534 209.565 1.00 66.44  ? 3503 ILE A CD1   1 
ATOM   15518 N  N     . ALA A 1 3504 ? 153.150 182.153 208.542 1.00 46.28  ? 3504 ALA A N     1 
ATOM   15519 C  CA    . ALA A 1 3504 ? 152.716 180.793 208.222 1.00 39.52  ? 3504 ALA A CA    1 
ATOM   15520 C  C     . ALA A 1 3504 ? 151.935 180.758 206.911 1.00 40.49  ? 3504 ALA A C     1 
ATOM   15521 O  O     . ALA A 1 3504 ? 152.269 180.003 205.986 1.00 40.80  ? 3504 ALA A O     1 
ATOM   15522 C  CB    . ALA A 1 3504 ? 151.876 180.228 209.369 1.00 37.13  ? 3504 ALA A CB    1 
ATOM   15523 N  N     . GLY A 1 3505 ? 150.910 181.604 206.802 1.00 37.78  ? 3505 GLY A N     1 
ATOM   15524 C  CA    . GLY A 1 3505 ? 150.136 181.660 205.573 1.00 31.11  ? 3505 GLY A CA    1 
ATOM   15525 C  C     . GLY A 1 3505 ? 150.940 182.174 204.395 1.00 32.83  ? 3505 GLY A C     1 
ATOM   15526 O  O     . GLY A 1 3505 ? 150.821 181.655 203.277 1.00 30.48  ? 3505 GLY A O     1 
ATOM   15527 N  N     . ASP A 1 3506 ? 151.768 183.205 204.622 1.00 36.48  ? 3506 ASP A N     1 
ATOM   15528 C  CA    . ASP A 1 3506 ? 152.582 183.720 203.522 1.00 31.44  ? 3506 ASP A CA    1 
ATOM   15529 C  C     . ASP A 1 3506 ? 153.465 182.630 202.929 1.00 32.38  ? 3506 ASP A C     1 
ATOM   15530 O  O     . ASP A 1 3506 ? 153.528 182.463 201.705 1.00 33.65  ? 3506 ASP A O     1 
ATOM   15531 C  CB    . ASP A 1 3506 ? 153.438 184.895 203.986 1.00 40.09  ? 3506 ASP A CB    1 
ATOM   15532 C  CG    . ASP A 1 3506 ? 152.619 186.020 204.549 1.00 54.28  ? 3506 ASP A CG    1 
ATOM   15533 O  OD1   . ASP A 1 3506 ? 151.377 185.903 204.543 1.00 54.31  ? 3506 ASP A OD1   1 
ATOM   15534 O  OD2   . ASP A 1 3506 ? 153.218 187.028 204.979 1.00 61.77  ? 3506 ASP A OD2   1 
ATOM   15535 N  N     . CYS A 1 3507 ? 154.151 181.874 203.785 1.00 33.96  ? 3507 CYS A N     1 
ATOM   15536 C  CA    . CYS A 1 3507 ? 155.062 180.845 203.305 1.00 27.44  ? 3507 CYS A CA    1 
ATOM   15537 C  C     . CYS A 1 3507 ? 154.316 179.679 202.680 1.00 28.70  ? 3507 CYS A C     1 
ATOM   15538 O  O     . CYS A 1 3507 ? 154.805 179.097 201.707 1.00 29.02  ? 3507 CYS A O     1 
ATOM   15539 C  CB    . CYS A 1 3507 ? 155.955 180.361 204.443 1.00 25.98  ? 3507 CYS A CB    1 
ATOM   15540 S  SG    . CYS A 1 3507 ? 157.076 181.624 205.064 1.00 50.33  ? 3507 CYS A SG    1 
ATOM   15541 N  N     . LEU A 1 3508 ? 153.137 179.326 203.201 1.00 29.49  ? 3508 LEU A N     1 
ATOM   15542 C  CA    . LEU A 1 3508 ? 152.351 178.286 202.546 1.00 25.30  ? 3508 LEU A CA    1 
ATOM   15543 C  C     . LEU A 1 3508 ? 152.023 178.686 201.113 1.00 26.50  ? 3508 LEU A C     1 
ATOM   15544 O  O     . LEU A 1 3508 ? 152.254 177.917 200.169 1.00 28.15  ? 3508 LEU A O     1 
ATOM   15545 C  CB    . LEU A 1 3508 ? 151.074 178.009 203.344 1.00 25.62  ? 3508 LEU A CB    1 
ATOM   15546 C  CG    . LEU A 1 3508 ? 150.198 176.807 202.969 1.00 23.44  ? 3508 LEU A CG    1 
ATOM   15547 C  CD1   . LEU A 1 3508 ? 149.441 176.326 204.190 1.00 26.51  ? 3508 LEU A CD1   1 
ATOM   15548 C  CD2   . LEU A 1 3508 ? 149.225 177.125 201.851 1.00 24.30  ? 3508 LEU A CD2   1 
ATOM   15549 N  N     . LEU A 1 3509 ? 151.509 179.907 200.930 1.00 29.07  ? 3509 LEU A N     1 
ATOM   15550 C  CA    . LEU A 1 3509 ? 151.155 180.360 199.586 1.00 26.74  ? 3509 LEU A CA    1 
ATOM   15551 C  C     . LEU A 1 3509 ? 152.378 180.440 198.680 1.00 25.79  ? 3509 LEU A C     1 
ATOM   15552 O  O     . LEU A 1 3509 ? 152.326 180.021 197.518 1.00 26.51  ? 3509 LEU A O     1 
ATOM   15553 C  CB    . LEU A 1 3509 ? 150.456 181.716 199.653 1.00 26.36  ? 3509 LEU A CB    1 
ATOM   15554 C  CG    . LEU A 1 3509 ? 149.140 181.781 200.422 1.00 25.23  ? 3509 LEU A CG    1 
ATOM   15555 C  CD1   . LEU A 1 3509 ? 148.567 183.176 200.347 1.00 27.94  ? 3509 LEU A CD1   1 
ATOM   15556 C  CD2   . LEU A 1 3509 ? 148.162 180.776 199.859 1.00 24.37  ? 3509 LEU A CD2   1 
ATOM   15557 N  N     . SER A 1 3510 ? 153.488 180.973 199.193 1.00 23.55  ? 3510 SER A N     1 
ATOM   15558 C  CA    . SER A 1 3510 ? 154.678 181.139 198.365 1.00 22.42  ? 3510 SER A CA    1 
ATOM   15559 C  C     . SER A 1 3510 ? 155.265 179.795 197.950 1.00 26.35  ? 3510 SER A C     1 
ATOM   15560 O  O     . SER A 1 3510 ? 155.673 179.617 196.796 1.00 31.33  ? 3510 SER A O     1 
ATOM   15561 C  CB    . SER A 1 3510 ? 155.714 181.973 199.110 1.00 26.33  ? 3510 SER A CB    1 
ATOM   15562 O  OG    . SER A 1 3510 ? 155.180 183.239 199.448 1.00 30.02  ? 3510 SER A OG    1 
ATOM   15563 N  N     . ALA A 1 3511 ? 155.323 178.837 198.878 1.00 23.82  ? 3511 ALA A N     1 
ATOM   15564 C  CA    . ALA A 1 3511 ? 155.828 177.512 198.545 1.00 20.22  ? 3511 ALA A CA    1 
ATOM   15565 C  C     . ALA A 1 3511 ? 154.931 176.813 197.538 1.00 20.83  ? 3511 ALA A C     1 
ATOM   15566 O  O     . ALA A 1 3511 ? 155.424 176.144 196.622 1.00 21.98  ? 3511 ALA A O     1 
ATOM   15567 C  CB    . ALA A 1 3511 ? 155.956 176.674 199.809 1.00 21.63  ? 3511 ALA A CB    1 
ATOM   15568 N  N     . ALA A 1 3512 ? 153.610 176.943 197.696 1.00 22.07  ? 3512 ALA A N     1 
ATOM   15569 C  CA    . ALA A 1 3512 ? 152.702 176.373 196.708 1.00 19.81  ? 3512 ALA A CA    1 
ATOM   15570 C  C     . ALA A 1 3512 ? 152.933 176.990 195.337 1.00 20.81  ? 3512 ALA A C     1 
ATOM   15571 O  O     . ALA A 1 3512 ? 152.954 176.281 194.324 1.00 21.94  ? 3512 ALA A O     1 
ATOM   15572 C  CB    . ALA A 1 3512 ? 151.254 176.568 197.152 1.00 19.09  ? 3512 ALA A CB    1 
ATOM   15573 N  N     . PHE A 1 3513 ? 153.131 178.309 195.290 1.00 23.41  ? 3513 PHE A N     1 
ATOM   15574 C  CA    . PHE A 1 3513 ? 153.389 178.974 194.018 1.00 25.14  ? 3513 PHE A CA    1 
ATOM   15575 C  C     . PHE A 1 3513 ? 154.676 178.469 193.377 1.00 27.21  ? 3513 PHE A C     1 
ATOM   15576 O  O     . PHE A 1 3513 ? 154.713 178.208 192.169 1.00 29.73  ? 3513 PHE A O     1 
ATOM   15577 C  CB    . PHE A 1 3513 ? 153.454 180.486 194.225 1.00 28.03  ? 3513 PHE A CB    1 
ATOM   15578 C  CG    . PHE A 1 3513 ? 153.795 181.251 192.982 1.00 38.64  ? 3513 PHE A CG    1 
ATOM   15579 C  CD1   . PHE A 1 3513 ? 152.886 181.354 191.945 1.00 39.59  ? 3513 PHE A CD1   1 
ATOM   15580 C  CD2   . PHE A 1 3513 ? 155.032 181.857 192.845 1.00 40.57  ? 3513 PHE A CD2   1 
ATOM   15581 C  CE1   . PHE A 1 3513 ? 153.200 182.052 190.800 1.00 42.28  ? 3513 PHE A CE1   1 
ATOM   15582 C  CE2   . PHE A 1 3513 ? 155.351 182.556 191.701 1.00 44.11  ? 3513 PHE A CE2   1 
ATOM   15583 C  CZ    . PHE A 1 3513 ? 154.433 182.654 190.678 1.00 46.55  ? 3513 PHE A CZ    1 
ATOM   15584 N  N     . ILE A 1 3514 ? 155.742 178.329 194.167 1.00 26.93  ? 3514 ILE A N     1 
ATOM   15585 C  CA    . ILE A 1 3514 ? 157.019 177.878 193.615 1.00 23.62  ? 3514 ILE A CA    1 
ATOM   15586 C  C     . ILE A 1 3514 ? 156.907 176.451 193.097 1.00 25.54  ? 3514 ILE A C     1 
ATOM   15587 O  O     . ILE A 1 3514 ? 157.334 176.141 191.979 1.00 27.67  ? 3514 ILE A O     1 
ATOM   15588 C  CB    . ILE A 1 3514 ? 158.140 177.997 194.662 1.00 21.54  ? 3514 ILE A CB    1 
ATOM   15589 C  CG1   . ILE A 1 3514 ? 158.321 179.441 195.113 1.00 25.13  ? 3514 ILE A CG1   1 
ATOM   15590 C  CG2   . ILE A 1 3514 ? 159.440 177.466 194.103 1.00 20.47  ? 3514 ILE A CG2   1 
ATOM   15591 C  CD1   . ILE A 1 3514 ? 159.327 179.584 196.227 1.00 27.87  ? 3514 ILE A CD1   1 
ATOM   15592 N  N     . ALA A 1 3515 ? 156.330 175.558 193.903 1.00 25.86  ? 3515 ALA A N     1 
ATOM   15593 C  CA    . ALA A 1 3515 ? 156.355 174.139 193.571 1.00 25.27  ? 3515 ALA A CA    1 
ATOM   15594 C  C     . ALA A 1 3515 ? 155.367 173.782 192.470 1.00 29.00  ? 3515 ALA A C     1 
ATOM   15595 O  O     . ALA A 1 3515 ? 155.651 172.910 191.642 1.00 33.54  ? 3515 ALA A O     1 
ATOM   15596 C  CB    . ALA A 1 3515 ? 156.068 173.309 194.815 1.00 19.96  ? 3515 ALA A CB    1 
ATOM   15597 N  N     . TYR A 1 3516 ? 154.206 174.432 192.443 1.00 26.09  ? 3516 TYR A N     1 
ATOM   15598 C  CA    . TYR A 1 3516 ? 153.110 174.017 191.579 1.00 23.48  ? 3516 TYR A CA    1 
ATOM   15599 C  C     . TYR A 1 3516 ? 152.983 174.870 190.325 1.00 30.01  ? 3516 TYR A C     1 
ATOM   15600 O  O     . TYR A 1 3516 ? 152.938 174.334 189.215 1.00 32.87  ? 3516 TYR A O     1 
ATOM   15601 C  CB    . TYR A 1 3516 ? 151.807 174.043 192.378 1.00 22.71  ? 3516 TYR A CB    1 
ATOM   15602 C  CG    . TYR A 1 3516 ? 151.678 172.869 193.315 1.00 24.16  ? 3516 TYR A CG    1 
ATOM   15603 C  CD1   . TYR A 1 3516 ? 151.909 171.578 192.871 1.00 24.19  ? 3516 TYR A CD1   1 
ATOM   15604 C  CD2   . TYR A 1 3516 ? 151.355 173.054 194.647 1.00 22.75  ? 3516 TYR A CD2   1 
ATOM   15605 C  CE1   . TYR A 1 3516 ? 151.798 170.505 193.720 1.00 22.26  ? 3516 TYR A CE1   1 
ATOM   15606 C  CE2   . TYR A 1 3516 ? 151.247 171.986 195.504 1.00 22.27  ? 3516 TYR A CE2   1 
ATOM   15607 C  CZ    . TYR A 1 3516 ? 151.469 170.716 195.036 1.00 24.77  ? 3516 TYR A CZ    1 
ATOM   15608 O  OH    . TYR A 1 3516 ? 151.358 169.650 195.893 1.00 35.88  ? 3516 TYR A OH    1 
ATOM   15609 N  N     . ALA A 1 3517 ? 152.912 176.187 190.478 1.00 31.04  ? 3517 ALA A N     1 
ATOM   15610 C  CA    . ALA A 1 3517 ? 152.907 177.061 189.319 1.00 23.46  ? 3517 ALA A CA    1 
ATOM   15611 C  C     . ALA A 1 3517 ? 154.273 177.040 188.643 1.00 32.62  ? 3517 ALA A C     1 
ATOM   15612 O  O     . ALA A 1 3517 ? 155.287 176.667 189.237 1.00 48.00  ? 3517 ALA A O     1 
ATOM   15613 C  CB    . ALA A 1 3517 ? 152.538 178.487 189.721 1.00 25.58  ? 3517 ALA A CB    1 
ATOM   15614 N  N     . GLY A 1 3518 ? 154.292 177.442 187.379 1.00 28.35  ? 3518 GLY A N     1 
ATOM   15615 C  CA    . GLY A 1 3518 ? 155.531 177.451 186.632 1.00 28.26  ? 3518 GLY A CA    1 
ATOM   15616 C  C     . GLY A 1 3518 ? 155.371 176.938 185.221 1.00 29.41  ? 3518 GLY A C     1 
ATOM   15617 O  O     . GLY A 1 3518 ? 156.064 177.394 184.309 1.00 37.72  ? 3518 GLY A O     1 
ATOM   15618 N  N     . TYR A 1 3519 ? 154.465 175.985 185.028 1.00 28.83  ? 3519 TYR A N     1 
ATOM   15619 C  CA    . TYR A 1 3519 ? 154.065 175.600 183.684 1.00 30.97  ? 3519 TYR A CA    1 
ATOM   15620 C  C     . TYR A 1 3519 ? 152.891 176.422 183.178 1.00 37.91  ? 3519 TYR A C     1 
ATOM   15621 O  O     . TYR A 1 3519 ? 152.739 176.595 181.964 1.00 49.04  ? 3519 TYR A O     1 
ATOM   15622 C  CB    . TYR A 1 3519 ? 153.701 174.114 183.636 1.00 31.42  ? 3519 TYR A CB    1 
ATOM   15623 C  CG    . TYR A 1 3519 ? 153.299 173.649 182.258 1.00 37.10  ? 3519 TYR A CG    1 
ATOM   15624 C  CD1   . TYR A 1 3519 ? 154.224 173.591 181.228 1.00 40.88  ? 3519 TYR A CD1   1 
ATOM   15625 C  CD2   . TYR A 1 3519 ? 151.988 173.289 181.981 1.00 39.89  ? 3519 TYR A CD2   1 
ATOM   15626 C  CE1   . TYR A 1 3519 ? 153.860 173.177 179.965 1.00 47.04  ? 3519 TYR A CE1   1 
ATOM   15627 C  CE2   . TYR A 1 3519 ? 151.615 172.874 180.721 1.00 45.13  ? 3519 TYR A CE2   1 
ATOM   15628 C  CZ    . TYR A 1 3519 ? 152.554 172.820 179.717 1.00 51.59  ? 3519 TYR A CZ    1 
ATOM   15629 O  OH    . TYR A 1 3519 ? 152.188 172.406 178.457 1.00 59.93  ? 3519 TYR A OH    1 
ATOM   15630 N  N     . PHE A 1 3520 ? 152.072 176.943 184.083 1.00 33.66  ? 3520 PHE A N     1 
ATOM   15631 C  CA    . PHE A 1 3520 ? 150.857 177.640 183.705 1.00 32.34  ? 3520 PHE A CA    1 
ATOM   15632 C  C     . PHE A 1 3520 ? 151.160 179.071 183.276 1.00 36.99  ? 3520 PHE A C     1 
ATOM   15633 O  O     . PHE A 1 3520 ? 152.223 179.626 183.563 1.00 36.71  ? 3520 PHE A O     1 
ATOM   15634 C  CB    . PHE A 1 3520 ? 149.858 177.640 184.862 1.00 32.27  ? 3520 PHE A CB    1 
ATOM   15635 C  CG    . PHE A 1 3520 ? 149.621 176.283 185.460 1.00 34.68  ? 3520 PHE A CG    1 
ATOM   15636 C  CD1   . PHE A 1 3520 ? 150.415 175.817 186.490 1.00 36.36  ? 3520 PHE A CD1   1 
ATOM   15637 C  CD2   . PHE A 1 3520 ? 148.614 175.467 184.978 1.00 40.20  ? 3520 PHE A CD2   1 
ATOM   15638 C  CE1   . PHE A 1 3520 ? 150.200 174.569 187.037 1.00 39.17  ? 3520 PHE A CE1   1 
ATOM   15639 C  CE2   . PHE A 1 3520 ? 148.396 174.219 185.521 1.00 37.38  ? 3520 PHE A CE2   1 
ATOM   15640 C  CZ    . PHE A 1 3520 ? 149.190 173.769 186.551 1.00 39.70  ? 3520 PHE A CZ    1 
ATOM   15641 N  N     . ASP A 1 3521 ? 150.202 179.666 182.570 1.00 42.84  ? 3521 ASP A N     1 
ATOM   15642 C  CA    . ASP A 1 3521 ? 150.323 181.049 182.139 1.00 42.80  ? 3521 ASP A CA    1 
ATOM   15643 C  C     . ASP A 1 3521 ? 150.034 181.988 183.308 1.00 39.46  ? 3521 ASP A C     1 
ATOM   15644 O  O     . ASP A 1 3521 ? 149.730 181.563 184.424 1.00 43.35  ? 3521 ASP A O     1 
ATOM   15645 C  CB    . ASP A 1 3521 ? 149.392 181.318 180.959 1.00 49.01  ? 3521 ASP A CB    1 
ATOM   15646 C  CG    . ASP A 1 3521 ? 147.958 180.927 181.246 1.00 57.96  ? 3521 ASP A CG    1 
ATOM   15647 O  OD1   . ASP A 1 3521 ? 147.702 179.724 181.464 1.00 56.61  ? 3521 ASP A OD1   1 
ATOM   15648 O  OD2   . ASP A 1 3521 ? 147.084 181.819 181.248 1.00 61.82  ? 3521 ASP A OD2   1 
ATOM   15649 N  N     . GLN A 1 3522 ? 150.134 183.292 183.043 1.00 41.81  ? 3522 GLN A N     1 
ATOM   15650 C  CA    . GLN A 1 3522 ? 150.034 184.277 184.116 1.00 43.15  ? 3522 GLN A CA    1 
ATOM   15651 C  C     . GLN A 1 3522 ? 148.648 184.283 184.754 1.00 47.69  ? 3522 GLN A C     1 
ATOM   15652 O  O     . GLN A 1 3522 ? 148.525 184.289 185.986 1.00 49.02  ? 3522 GLN A O     1 
ATOM   15653 C  CB    . GLN A 1 3522 ? 150.394 185.662 183.581 1.00 42.74  ? 3522 GLN A CB    1 
ATOM   15654 C  CG    . GLN A 1 3522 ? 150.857 186.635 184.646 1.00 50.11  ? 3522 GLN A CG    1 
ATOM   15655 C  CD    . GLN A 1 3522 ? 151.168 188.005 184.085 1.00 60.88  ? 3522 GLN A CD    1 
ATOM   15656 O  OE1   . GLN A 1 3522 ? 152.057 188.158 183.248 1.00 60.91  ? 3522 GLN A OE1   1 
ATOM   15657 N  NE2   . GLN A 1 3522 ? 150.435 189.012 184.542 1.00 65.73  ? 3522 GLN A NE2   1 
ATOM   15658 N  N     . GLN A 1 3523 ? 147.589 184.275 183.937 1.00 47.15  ? 3523 GLN A N     1 
ATOM   15659 C  CA    . GLN A 1 3523 ? 146.242 184.216 184.497 1.00 45.50  ? 3523 GLN A CA    1 
ATOM   15660 C  C     . GLN A 1 3523 ? 146.007 182.922 185.255 1.00 47.01  ? 3523 GLN A C     1 
ATOM   15661 O  O     . GLN A 1 3523 ? 145.303 182.915 186.266 1.00 47.85  ? 3523 GLN A O     1 
ATOM   15662 C  CB    . GLN A 1 3523 ? 145.178 184.379 183.414 1.00 49.23  ? 3523 GLN A CB    1 
ATOM   15663 C  CG    . GLN A 1 3523 ? 145.093 185.757 182.826 1.00 58.39  ? 3523 GLN A CG    1 
ATOM   15664 C  CD    . GLN A 1 3523 ? 144.672 186.795 183.844 1.00 68.98  ? 3523 GLN A CD    1 
ATOM   15665 O  OE1   . GLN A 1 3523 ? 145.472 187.631 184.265 1.00 71.90  ? 3523 GLN A OE1   1 
ATOM   15666 N  NE2   . GLN A 1 3523 ? 143.408 186.749 184.245 1.00 71.55  ? 3523 GLN A NE2   1 
ATOM   15667 N  N     . MET A 1 3524 ? 146.562 181.811 184.777 1.00 45.65  ? 3524 MET A N     1 
ATOM   15668 C  CA    . MET A 1 3524 ? 146.298 180.550 185.457 1.00 40.80  ? 3524 MET A CA    1 
ATOM   15669 C  C     . MET A 1 3524 ? 147.016 180.502 186.802 1.00 35.81  ? 3524 MET A C     1 
ATOM   15670 O  O     . MET A 1 3524 ? 146.460 180.013 187.794 1.00 37.31  ? 3524 MET A O     1 
ATOM   15671 C  CB    . MET A 1 3524 ? 146.707 179.377 184.575 1.00 42.17  ? 3524 MET A CB    1 
ATOM   15672 C  CG    . MET A 1 3524 ? 146.284 178.056 185.153 1.00 47.05  ? 3524 MET A CG    1 
ATOM   15673 S  SD    . MET A 1 3524 ? 144.485 178.007 185.143 1.00 69.73  ? 3524 MET A SD    1 
ATOM   15674 C  CE    . MET A 1 3524 ? 144.166 176.827 186.437 1.00 49.39  ? 3524 MET A CE    1 
ATOM   15675 N  N     . ARG A 1 3525 ? 148.243 181.028 186.857 1.00 34.72  ? 3525 ARG A N     1 
ATOM   15676 C  CA    . ARG A 1 3525 ? 148.932 181.171 188.135 1.00 29.32  ? 3525 ARG A CA    1 
ATOM   15677 C  C     . ARG A 1 3525 ? 148.156 182.079 189.076 1.00 36.49  ? 3525 ARG A C     1 
ATOM   15678 O  O     . ARG A 1 3525 ? 148.048 181.796 190.275 1.00 42.80  ? 3525 ARG A O     1 
ATOM   15679 C  CB    . ARG A 1 3525 ? 150.339 181.727 187.927 1.00 23.34  ? 3525 ARG A CB    1 
ATOM   15680 C  CG    . ARG A 1 3525 ? 151.271 180.855 187.120 1.00 28.60  ? 3525 ARG A CG    1 
ATOM   15681 C  CD    . ARG A 1 3525 ? 152.633 181.515 187.018 1.00 31.12  ? 3525 ARG A CD    1 
ATOM   15682 N  NE    . ARG A 1 3525 ? 153.520 180.827 186.090 1.00 32.45  ? 3525 ARG A NE    1 
ATOM   15683 C  CZ    . ARG A 1 3525 ? 154.771 181.189 185.851 1.00 29.52  ? 3525 ARG A CZ    1 
ATOM   15684 N  NH1   . ARG A 1 3525 ? 155.317 182.227 186.460 1.00 34.89  ? 3525 ARG A NH1   1 
ATOM   15685 N  NH2   . ARG A 1 3525 ? 155.493 180.493 184.978 1.00 26.02  ? 3525 ARG A NH2   1 
ATOM   15686 N  N     . GLN A 1 3526 ? 147.619 183.185 188.556 1.00 35.29  ? 3526 GLN A N     1 
ATOM   15687 C  CA    . GLN A 1 3526 ? 146.859 184.097 189.404 1.00 34.51  ? 3526 GLN A CA    1 
ATOM   15688 C  C     . GLN A 1 3526 ? 145.578 183.445 189.909 1.00 35.05  ? 3526 GLN A C     1 
ATOM   15689 O  O     . GLN A 1 3526 ? 145.177 183.660 191.056 1.00 38.49  ? 3526 GLN A O     1 
ATOM   15690 C  CB    . GLN A 1 3526 ? 146.546 185.385 188.646 1.00 44.89  ? 3526 GLN A CB    1 
ATOM   15691 C  CG    . GLN A 1 3526 ? 145.966 186.479 189.521 1.00 48.33  ? 3526 GLN A CG    1 
ATOM   15692 C  CD    . GLN A 1 3526 ? 146.765 186.689 190.790 1.00 51.08  ? 3526 GLN A CD    1 
ATOM   15693 O  OE1   . GLN A 1 3526 ? 147.960 186.976 190.743 1.00 57.09  ? 3526 GLN A OE1   1 
ATOM   15694 N  NE2   . GLN A 1 3526 ? 146.107 186.548 191.934 1.00 44.56  ? 3526 GLN A NE2   1 
ATOM   15695 N  N     . ASN A 1 3527 ? 144.920 182.648 189.065 1.00 34.03  ? 3527 ASN A N     1 
ATOM   15696 C  CA    . ASN A 1 3527 ? 143.724 181.930 189.494 1.00 33.26  ? 3527 ASN A CA    1 
ATOM   15697 C  C     . ASN A 1 3527 ? 144.051 180.926 190.588 1.00 37.33  ? 3527 ASN A C     1 
ATOM   15698 O  O     . ASN A 1 3527 ? 143.315 180.810 191.576 1.00 38.85  ? 3527 ASN A O     1 
ATOM   15699 C  CB    . ASN A 1 3527 ? 143.079 181.222 188.303 1.00 33.54  ? 3527 ASN A CB    1 
ATOM   15700 C  CG    . ASN A 1 3527 ? 142.591 182.186 187.244 1.00 45.29  ? 3527 ASN A CG    1 
ATOM   15701 O  OD1   . ASN A 1 3527 ? 142.631 183.402 187.426 1.00 51.84  ? 3527 ASN A OD1   1 
ATOM   15702 N  ND2   . ASN A 1 3527 ? 142.130 181.646 186.122 1.00 44.84  ? 3527 ASN A ND2   1 
ATOM   15703 N  N     . LEU A 1 3528 ? 145.151 180.187 190.428 1.00 33.64  ? 3528 LEU A N     1 
ATOM   15704 C  CA    . LEU A 1 3528 ? 145.566 179.248 191.465 1.00 23.46  ? 3528 LEU A CA    1 
ATOM   15705 C  C     . LEU A 1 3528 ? 145.872 179.972 192.770 1.00 28.80  ? 3528 LEU A C     1 
ATOM   15706 O  O     . LEU A 1 3528 ? 145.455 179.530 193.849 1.00 38.00  ? 3528 LEU A O     1 
ATOM   15707 C  CB    . LEU A 1 3528 ? 146.783 178.456 190.995 1.00 20.90  ? 3528 LEU A CB    1 
ATOM   15708 C  CG    . LEU A 1 3528 ? 146.529 177.352 189.972 1.00 25.09  ? 3528 LEU A CG    1 
ATOM   15709 C  CD1   . LEU A 1 3528 ? 147.844 176.806 189.447 1.00 28.36  ? 3528 LEU A CD1   1 
ATOM   15710 C  CD2   . LEU A 1 3528 ? 145.691 176.246 190.582 1.00 28.05  ? 3528 LEU A CD2   1 
ATOM   15711 N  N     . PHE A 1 3529 ? 146.595 181.091 192.690 1.00 25.43  ? 3529 PHE A N     1 
ATOM   15712 C  CA    . PHE A 1 3529 ? 146.925 181.847 193.891 1.00 26.26  ? 3529 PHE A CA    1 
ATOM   15713 C  C     . PHE A 1 3529 ? 145.673 182.389 194.564 1.00 29.62  ? 3529 PHE A C     1 
ATOM   15714 O  O     . PHE A 1 3529 ? 145.574 182.392 195.795 1.00 31.60  ? 3529 PHE A O     1 
ATOM   15715 C  CB    . PHE A 1 3529 ? 147.881 182.988 193.551 1.00 32.46  ? 3529 PHE A CB    1 
ATOM   15716 C  CG    . PHE A 1 3529 ? 148.703 183.455 194.714 1.00 35.49  ? 3529 PHE A CG    1 
ATOM   15717 C  CD1   . PHE A 1 3529 ? 149.769 182.703 195.171 1.00 37.00  ? 3529 PHE A CD1   1 
ATOM   15718 C  CD2   . PHE A 1 3529 ? 148.401 184.640 195.359 1.00 32.72  ? 3529 PHE A CD2   1 
ATOM   15719 C  CE1   . PHE A 1 3529 ? 150.525 183.131 196.241 1.00 34.47  ? 3529 PHE A CE1   1 
ATOM   15720 C  CE2   . PHE A 1 3529 ? 149.153 185.070 196.431 1.00 34.82  ? 3529 PHE A CE2   1 
ATOM   15721 C  CZ    . PHE A 1 3529 ? 150.216 184.314 196.872 1.00 33.29  ? 3529 PHE A CZ    1 
ATOM   15722 N  N     . THR A 1 3530 ? 144.708 182.861 193.773 1.00 32.74  ? 3530 THR A N     1 
ATOM   15723 C  CA    . THR A 1 3530 ? 143.464 183.367 194.342 1.00 33.61  ? 3530 THR A CA    1 
ATOM   15724 C  C     . THR A 1 3530 ? 142.674 182.252 195.011 1.00 36.79  ? 3530 THR A C     1 
ATOM   15725 O  O     . THR A 1 3530 ? 142.086 182.455 196.079 1.00 44.33  ? 3530 THR A O     1 
ATOM   15726 C  CB    . THR A 1 3530 ? 142.629 184.045 193.257 1.00 36.88  ? 3530 THR A CB    1 
ATOM   15727 O  OG1   . THR A 1 3530 ? 143.348 185.170 192.735 1.00 41.24  ? 3530 THR A OG1   1 
ATOM   15728 C  CG2   . THR A 1 3530 ? 141.304 184.526 193.823 1.00 35.83  ? 3530 THR A CG2   1 
ATOM   15729 N  N     . THR A 1 3531 ? 142.651 181.063 194.404 1.00 32.82  ? 3531 THR A N     1 
ATOM   15730 C  CA    . THR A 1 3531 ? 141.976 179.928 195.028 1.00 30.11  ? 3531 THR A CA    1 
ATOM   15731 C  C     . THR A 1 3531 ? 142.624 179.571 196.360 1.00 35.67  ? 3531 THR A C     1 
ATOM   15732 O  O     . THR A 1 3531 ? 141.933 179.345 197.364 1.00 40.93  ? 3531 THR A O     1 
ATOM   15733 C  CB    . THR A 1 3531 ? 141.996 178.724 194.087 1.00 27.67  ? 3531 THR A CB    1 
ATOM   15734 O  OG1   . THR A 1 3531 ? 141.507 179.114 192.799 1.00 35.74  ? 3531 THR A OG1   1 
ATOM   15735 C  CG2   . THR A 1 3531 ? 141.124 177.611 194.635 1.00 30.84  ? 3531 THR A CG2   1 
ATOM   15736 N  N     . TRP A 1 3532 ? 143.958 179.522 196.390 1.00 31.47  ? 3532 TRP A N     1 
ATOM   15737 C  CA    . TRP A 1 3532 ? 144.654 179.198 197.632 1.00 26.40  ? 3532 TRP A CA    1 
ATOM   15738 C  C     . TRP A 1 3532 ? 144.417 180.265 198.693 1.00 34.73  ? 3532 TRP A C     1 
ATOM   15739 O  O     . TRP A 1 3532 ? 144.221 179.946 199.872 1.00 46.43  ? 3532 TRP A O     1 
ATOM   15740 C  CB    . TRP A 1 3532 ? 146.150 179.030 197.375 1.00 20.48  ? 3532 TRP A CB    1 
ATOM   15741 C  CG    . TRP A 1 3532 ? 146.480 178.051 196.302 1.00 20.96  ? 3532 TRP A CG    1 
ATOM   15742 C  CD1   . TRP A 1 3532 ? 145.725 176.993 195.894 1.00 21.90  ? 3532 TRP A CD1   1 
ATOM   15743 C  CD2   . TRP A 1 3532 ? 147.662 178.034 195.500 1.00 18.95  ? 3532 TRP A CD2   1 
ATOM   15744 N  NE1   . TRP A 1 3532 ? 146.363 176.321 194.882 1.00 16.93  ? 3532 TRP A NE1   1 
ATOM   15745 C  CE2   . TRP A 1 3532 ? 147.556 176.941 194.623 1.00 19.43  ? 3532 TRP A CE2   1 
ATOM   15746 C  CE3   . TRP A 1 3532 ? 148.801 178.841 195.436 1.00 17.49  ? 3532 TRP A CE3   1 
ATOM   15747 C  CZ2   . TRP A 1 3532 ? 148.543 176.634 193.695 1.00 22.08  ? 3532 TRP A CZ2   1 
ATOM   15748 C  CZ3   . TRP A 1 3532 ? 149.777 178.535 194.514 1.00 18.94  ? 3532 TRP A CZ3   1 
ATOM   15749 C  CH2   . TRP A 1 3532 ? 149.643 177.441 193.656 1.00 22.44  ? 3532 TRP A CH2   1 
ATOM   15750 N  N     . SER A 1 3533 ? 144.444 181.540 198.297 1.00 31.62  ? 3533 SER A N     1 
ATOM   15751 C  CA    . SER A 1 3533 ? 144.191 182.619 199.244 1.00 34.74  ? 3533 SER A CA    1 
ATOM   15752 C  C     . SER A 1 3533 ? 142.773 182.548 199.791 1.00 40.52  ? 3533 SER A C     1 
ATOM   15753 O  O     . SER A 1 3533 ? 142.547 182.780 200.983 1.00 48.82  ? 3533 SER A O     1 
ATOM   15754 C  CB    . SER A 1 3533 ? 144.440 183.971 198.578 1.00 33.50  ? 3533 SER A CB    1 
ATOM   15755 O  OG    . SER A 1 3533 ? 145.734 184.029 198.008 1.00 35.37  ? 3533 SER A OG    1 
ATOM   15756 N  N     . HIS A 1 3534 ? 141.802 182.237 198.930 1.00 36.87  ? 3534 HIS A N     1 
ATOM   15757 C  CA    . HIS A 1 3534 ? 140.424 182.104 199.383 1.00 43.26  ? 3534 HIS A CA    1 
ATOM   15758 C  C     . HIS A 1 3534 ? 140.280 180.954 200.369 1.00 49.85  ? 3534 HIS A C     1 
ATOM   15759 O  O     . HIS A 1 3534 ? 139.564 181.071 201.369 1.00 57.67  ? 3534 HIS A O     1 
ATOM   15760 C  CB    . HIS A 1 3534 ? 139.498 181.907 198.183 1.00 47.91  ? 3534 HIS A CB    1 
ATOM   15761 C  CG    . HIS A 1 3534 ? 138.070 181.660 198.554 1.00 61.62  ? 3534 HIS A CG    1 
ATOM   15762 N  ND1   . HIS A 1 3534 ? 137.342 182.531 199.336 1.00 67.10  ? 3534 HIS A ND1   1 
ATOM   15763 C  CD2   . HIS A 1 3534 ? 137.232 180.641 198.246 1.00 66.50  ? 3534 HIS A CD2   1 
ATOM   15764 C  CE1   . HIS A 1 3534 ? 136.119 182.058 199.496 1.00 67.84  ? 3534 HIS A CE1   1 
ATOM   15765 N  NE2   . HIS A 1 3534 ? 136.027 180.913 198.845 1.00 70.36  ? 3534 HIS A NE2   1 
ATOM   15766 N  N     . HIS A 1 3535 ? 140.954 179.832 200.105 1.00 46.62  ? 3535 HIS A N     1 
ATOM   15767 C  CA    . HIS A 1 3535 ? 140.901 178.717 201.046 1.00 45.32  ? 3535 HIS A CA    1 
ATOM   15768 C  C     . HIS A 1 3535 ? 141.541 179.081 202.379 1.00 43.16  ? 3535 HIS A C     1 
ATOM   15769 O  O     . HIS A 1 3535 ? 141.008 178.747 203.443 1.00 48.55  ? 3535 HIS A O     1 
ATOM   15770 C  CB    . HIS A 1 3535 ? 141.586 177.489 200.461 1.00 38.60  ? 3535 HIS A CB    1 
ATOM   15771 C  CG    . HIS A 1 3535 ? 141.563 176.300 201.370 1.00 44.59  ? 3535 HIS A CG    1 
ATOM   15772 N  ND1   . HIS A 1 3535 ? 140.408 175.607 201.658 1.00 50.77  ? 3535 HIS A ND1   1 
ATOM   15773 C  CD2   . HIS A 1 3535 ? 142.551 175.689 202.064 1.00 45.17  ? 3535 HIS A CD2   1 
ATOM   15774 C  CE1   . HIS A 1 3535 ? 140.687 174.615 202.485 1.00 50.03  ? 3535 HIS A CE1   1 
ATOM   15775 N  NE2   . HIS A 1 3535 ? 141.980 174.644 202.748 1.00 46.36  ? 3535 HIS A NE2   1 
ATOM   15776 N  N     . LEU A 1 3536 ? 142.694 179.752 202.344 1.00 39.53  ? 3536 LEU A N     1 
ATOM   15777 C  CA    . LEU A 1 3536 ? 143.363 180.130 203.584 1.00 41.36  ? 3536 LEU A CA    1 
ATOM   15778 C  C     . LEU A 1 3536 ? 142.524 181.118 204.383 1.00 47.25  ? 3536 LEU A C     1 
ATOM   15779 O  O     . LEU A 1 3536 ? 142.474 181.047 205.616 1.00 51.46  ? 3536 LEU A O     1 
ATOM   15780 C  CB    . LEU A 1 3536 ? 144.742 180.714 203.283 1.00 37.66  ? 3536 LEU A CB    1 
ATOM   15781 C  CG    . LEU A 1 3536 ? 145.929 179.769 203.469 1.00 34.41  ? 3536 LEU A CG    1 
ATOM   15782 C  CD1   . LEU A 1 3536 ? 145.920 178.676 202.419 1.00 28.67  ? 3536 LEU A CD1   1 
ATOM   15783 C  CD2   . LEU A 1 3536 ? 147.230 180.541 203.426 1.00 37.97  ? 3536 LEU A CD2   1 
ATOM   15784 N  N     . GLN A 1 3537 ? 141.867 182.055 203.697 1.00 48.30  ? 3537 GLN A N     1 
ATOM   15785 C  CA    . GLN A 1 3537 ? 140.965 182.980 204.372 1.00 48.41  ? 3537 GLN A CA    1 
ATOM   15786 C  C     . GLN A 1 3537 ? 139.768 182.248 204.963 1.00 51.29  ? 3537 GLN A C     1 
ATOM   15787 O  O     . GLN A 1 3537 ? 139.302 182.588 206.056 1.00 52.40  ? 3537 GLN A O     1 
ATOM   15788 C  CB    . GLN A 1 3537 ? 140.503 184.058 203.393 1.00 49.77  ? 3537 GLN A CB    1 
ATOM   15789 C  CG    . GLN A 1 3537 ? 140.266 185.414 204.022 1.00 62.85  ? 3537 GLN A CG    1 
ATOM   15790 C  CD    . GLN A 1 3537 ? 140.247 186.525 202.996 1.00 67.83  ? 3537 GLN A CD    1 
ATOM   15791 O  OE1   . GLN A 1 3537 ? 140.249 186.272 201.792 1.00 62.28  ? 3537 GLN A OE1   1 
ATOM   15792 N  NE2   . GLN A 1 3537 ? 140.229 187.766 203.467 1.00 75.99  ? 3537 GLN A NE2   1 
ATOM   15793 N  N     . GLN A 1 3538 ? 139.254 181.245 204.248 1.00 55.05  ? 3538 GLN A N     1 
ATOM   15794 C  CA    . GLN A 1 3538 ? 138.101 180.492 204.726 1.00 55.79  ? 3538 GLN A CA    1 
ATOM   15795 C  C     . GLN A 1 3538 ? 138.420 179.705 205.990 1.00 59.76  ? 3538 GLN A C     1 
ATOM   15796 O  O     . GLN A 1 3538 ? 137.517 179.421 206.784 1.00 69.28  ? 3538 GLN A O     1 
ATOM   15797 C  CB    . GLN A 1 3538 ? 137.607 179.554 203.627 1.00 55.90  ? 3538 GLN A CB    1 
ATOM   15798 C  CG    . GLN A 1 3538 ? 136.104 179.363 203.589 1.00 69.97  ? 3538 GLN A CG    1 
ATOM   15799 C  CD    . GLN A 1 3538 ? 135.675 178.365 202.532 1.00 79.09  ? 3538 GLN A CD    1 
ATOM   15800 O  OE1   . GLN A 1 3538 ? 136.422 178.075 201.598 1.00 74.17  ? 3538 GLN A OE1   1 
ATOM   15801 N  NE2   . GLN A 1 3538 ? 134.467 177.834 202.674 1.00 86.18  ? 3538 GLN A NE2   1 
ATOM   15802 N  N     . ALA A 1 3539 ? 139.684 179.341 206.191 1.00 56.22  ? 3539 ALA A N     1 
ATOM   15803 C  CA    . ALA A 1 3539 ? 140.104 178.568 207.352 1.00 53.13  ? 3539 ALA A CA    1 
ATOM   15804 C  C     . ALA A 1 3539 ? 140.730 179.421 208.447 1.00 54.22  ? 3539 ALA A C     1 
ATOM   15805 O  O     . ALA A 1 3539 ? 141.284 178.864 209.399 1.00 61.27  ? 3539 ALA A O     1 
ATOM   15806 C  CB    . ALA A 1 3539 ? 141.090 177.477 206.927 1.00 50.16  ? 3539 ALA A CB    1 
ATOM   15807 N  N     . ASN A 1 3540 ? 140.658 180.749 208.333 1.00 54.46  ? 3540 ASN A N     1 
ATOM   15808 C  CA    . ASN A 1 3540 ? 141.236 181.671 209.315 1.00 54.32  ? 3540 ASN A CA    1 
ATOM   15809 C  C     . ASN A 1 3540 ? 142.728 181.424 209.519 1.00 55.94  ? 3540 ASN A C     1 
ATOM   15810 O  O     . ASN A 1 3540 ? 143.242 181.500 210.636 1.00 59.60  ? 3540 ASN A O     1 
ATOM   15811 C  CB    . ASN A 1 3540 ? 140.492 181.611 210.651 1.00 57.03  ? 3540 ASN A CB    1 
ATOM   15812 C  CG    . ASN A 1 3540 ? 139.179 182.362 210.618 1.00 70.68  ? 3540 ASN A CG    1 
ATOM   15813 O  OD1   . ASN A 1 3540 ? 138.109 181.771 210.738 1.00 79.73  ? 3540 ASN A OD1   1 
ATOM   15814 N  ND2   . ASN A 1 3540 ? 139.255 183.677 210.455 1.00 72.03  ? 3540 ASN A ND2   1 
ATOM   15815 N  N     . ILE A 1 3541 ? 143.431 181.128 208.431 1.00 54.54  ? 3541 ILE A N     1 
ATOM   15816 C  CA    . ILE A 1 3541 ? 144.887 181.063 208.443 1.00 52.45  ? 3541 ILE A CA    1 
ATOM   15817 C  C     . ILE A 1 3541 ? 145.398 182.432 208.015 1.00 56.20  ? 3541 ILE A C     1 
ATOM   15818 O  O     . ILE A 1 3541 ? 145.212 182.845 206.868 1.00 55.72  ? 3541 ILE A O     1 
ATOM   15819 C  CB    . ILE A 1 3541 ? 145.412 179.952 207.527 1.00 44.78  ? 3541 ILE A CB    1 
ATOM   15820 C  CG1   . ILE A 1 3541 ? 144.936 178.589 208.028 1.00 42.76  ? 3541 ILE A CG1   1 
ATOM   15821 C  CG2   . ILE A 1 3541 ? 146.926 179.996 207.450 1.00 39.92  ? 3541 ILE A CG2   1 
ATOM   15822 C  CD1   . ILE A 1 3541 ? 145.353 177.446 207.150 1.00 39.98  ? 3541 ILE A CD1   1 
ATOM   15823 N  N     . GLN A 1 3542 ? 146.035 183.141 208.942 1.00 54.93  ? 3542 GLN A N     1 
ATOM   15824 C  CA    . GLN A 1 3542 ? 146.406 184.528 208.700 1.00 54.06  ? 3542 GLN A CA    1 
ATOM   15825 C  C     . GLN A 1 3542 ? 147.475 184.625 207.621 1.00 52.20  ? 3542 GLN A C     1 
ATOM   15826 O  O     . GLN A 1 3542 ? 148.475 183.902 207.650 1.00 59.53  ? 3542 GLN A O     1 
ATOM   15827 C  CB    . GLN A 1 3542 ? 146.900 185.177 209.991 1.00 59.11  ? 3542 GLN A CB    1 
ATOM   15828 C  CG    . GLN A 1 3542 ? 145.837 185.302 211.063 1.00 58.91  ? 3542 GLN A CG    1 
ATOM   15829 C  CD    . GLN A 1 3542 ? 144.689 186.190 210.633 1.00 66.53  ? 3542 GLN A CD    1 
ATOM   15830 O  OE1   . GLN A 1 3542 ? 143.580 185.715 210.387 1.00 64.80  ? 3542 GLN A OE1   1 
ATOM   15831 N  NE2   . GLN A 1 3542 ? 144.951 187.488 210.534 1.00 70.21  ? 3542 GLN A NE2   1 
ATOM   15832 N  N     . PHE A 1 3543 ? 147.253 185.521 206.666 1.00 49.57  ? 3543 PHE A N     1 
ATOM   15833 C  CA    . PHE A 1 3543 ? 148.240 185.846 205.649 1.00 49.04  ? 3543 PHE A CA    1 
ATOM   15834 C  C     . PHE A 1 3543 ? 147.953 187.257 205.163 1.00 57.32  ? 3543 PHE A C     1 
ATOM   15835 O  O     . PHE A 1 3543 ? 146.842 187.770 205.319 1.00 62.18  ? 3543 PHE A O     1 
ATOM   15836 C  CB    . PHE A 1 3543 ? 148.216 184.847 204.487 1.00 44.21  ? 3543 PHE A CB    1 
ATOM   15837 C  CG    . PHE A 1 3543 ? 146.975 184.919 203.646 1.00 42.02  ? 3543 PHE A CG    1 
ATOM   15838 C  CD1   . PHE A 1 3543 ? 145.782 184.384 204.095 1.00 44.99  ? 3543 PHE A CD1   1 
ATOM   15839 C  CD2   . PHE A 1 3543 ? 147.003 185.521 202.403 1.00 41.93  ? 3543 PHE A CD2   1 
ATOM   15840 C  CE1   . PHE A 1 3543 ? 144.643 184.452 203.322 1.00 41.51  ? 3543 PHE A CE1   1 
ATOM   15841 C  CE2   . PHE A 1 3543 ? 145.867 185.591 201.626 1.00 46.34  ? 3543 PHE A CE2   1 
ATOM   15842 C  CZ    . PHE A 1 3543 ? 144.686 185.056 202.086 1.00 37.93  ? 3543 PHE A CZ    1 
ATOM   15843 N  N     . ARG A 1 3544 ? 148.971 187.884 204.582 1.00 55.09  ? 3544 ARG A N     1 
ATOM   15844 C  CA    . ARG A 1 3544 ? 148.806 189.237 204.074 1.00 57.41  ? 3544 ARG A CA    1 
ATOM   15845 C  C     . ARG A 1 3544 ? 147.875 189.226 202.871 1.00 64.24  ? 3544 ARG A C     1 
ATOM   15846 O  O     . ARG A 1 3544 ? 148.021 188.401 201.966 1.00 57.42  ? 3544 ARG A O     1 
ATOM   15847 C  CB    . ARG A 1 3544 ? 150.161 189.834 203.698 1.00 58.05  ? 3544 ARG A CB    1 
ATOM   15848 C  CG    . ARG A 1 3544 ? 150.798 190.674 204.786 1.00 67.04  ? 3544 ARG A CG    1 
ATOM   15849 C  CD    . ARG A 1 3544 ? 151.662 191.771 204.191 1.00 75.97  ? 3544 ARG A CD    1 
ATOM   15850 N  NE    . ARG A 1 3544 ? 152.340 191.326 202.981 1.00 77.05  ? 3544 ARG A NE    1 
ATOM   15851 C  CZ    . ARG A 1 3544 ? 153.588 190.880 202.940 1.00 82.83  ? 3544 ARG A CZ    1 
ATOM   15852 N  NH1   . ARG A 1 3544 ? 154.333 190.811 204.031 1.00 79.01  ? 3544 ARG A NH1   1 
ATOM   15853 N  NH2   . ARG A 1 3544 ? 154.102 190.493 201.776 1.00 79.59  ? 3544 ARG A NH2   1 
ATOM   15854 N  N     . THR A 1 3545 ? 146.911 190.148 202.865 1.00 68.97  ? 3545 THR A N     1 
ATOM   15855 C  CA    . THR A 1 3545 ? 145.929 190.180 201.787 1.00 68.33  ? 3545 THR A CA    1 
ATOM   15856 C  C     . THR A 1 3545 ? 146.595 190.438 200.443 1.00 68.87  ? 3545 THR A C     1 
ATOM   15857 O  O     . THR A 1 3545 ? 146.195 189.866 199.422 1.00 66.44  ? 3545 THR A O     1 
ATOM   15858 C  CB    . THR A 1 3545 ? 144.870 191.242 202.071 1.00 77.43  ? 3545 THR A CB    1 
ATOM   15859 O  OG1   . THR A 1 3545 ? 145.492 192.532 202.142 1.00 75.15  ? 3545 THR A OG1   1 
ATOM   15860 C  CG2   . THR A 1 3545 ? 144.169 190.950 203.387 1.00 78.31  ? 3545 THR A CG2   1 
ATOM   15861 N  N     . ASP A 1 3546 ? 147.612 191.294 200.422 1.00 68.94  ? 3546 ASP A N     1 
ATOM   15862 C  CA    . ASP A 1 3546 ? 148.346 191.617 199.200 1.00 66.00  ? 3546 ASP A CA    1 
ATOM   15863 C  C     . ASP A 1 3546 ? 149.733 190.974 199.232 1.00 64.05  ? 3546 ASP A C     1 
ATOM   15864 O  O     . ASP A 1 3546 ? 150.738 191.609 199.549 1.00 67.23  ? 3546 ASP A O     1 
ATOM   15865 C  CB    . ASP A 1 3546 ? 148.379 193.132 199.002 1.00 74.71  ? 3546 ASP A CB    1 
ATOM   15866 C  CG    . ASP A 1 3546 ? 149.075 193.873 200.136 1.00 82.99  ? 3546 ASP A CG    1 
ATOM   15867 O  OD1   . ASP A 1 3546 ? 149.501 193.238 201.123 1.00 74.53  ? 3546 ASP A OD1   1 
ATOM   15868 O  OD2   . ASP A 1 3546 ? 149.185 195.113 200.040 1.00 88.35  ? 3546 ASP A OD2   1 
ATOM   15869 N  N     . ILE A 1 3547 ? 149.785 189.701 198.852 1.00 65.11  ? 3547 ILE A N     1 
ATOM   15870 C  CA    . ILE A 1 3547 ? 151.044 188.976 198.721 1.00 60.60  ? 3547 ILE A CA    1 
ATOM   15871 C  C     . ILE A 1 3547 ? 151.674 189.361 197.390 1.00 58.15  ? 3547 ILE A C     1 
ATOM   15872 O  O     . ILE A 1 3547 ? 151.179 188.986 196.324 1.00 57.98  ? 3547 ILE A O     1 
ATOM   15873 C  CB    . ILE A 1 3547 ? 150.842 187.459 198.811 1.00 63.69  ? 3547 ILE A CB    1 
ATOM   15874 C  CG1   . ILE A 1 3547 ? 150.222 187.059 200.145 1.00 64.54  ? 3547 ILE A CG1   1 
ATOM   15875 C  CG2   . ILE A 1 3547 ? 152.168 186.743 198.647 1.00 59.55  ? 3547 ILE A CG2   1 
ATOM   15876 C  CD1   . ILE A 1 3547 ? 151.087 187.417 201.323 1.00 60.59  ? 3547 ILE A CD1   1 
ATOM   15877 N  N     . ALA A 1 3548 ? 152.770 190.109 197.449 1.00 54.70  ? 3548 ALA A N     1 
ATOM   15878 C  CA    . ALA A 1 3548 ? 153.593 190.369 196.273 1.00 49.84  ? 3548 ALA A CA    1 
ATOM   15879 C  C     . ALA A 1 3548 ? 154.624 189.251 196.197 1.00 51.24  ? 3548 ALA A C     1 
ATOM   15880 O  O     . ALA A 1 3548 ? 155.633 189.274 196.905 1.00 56.25  ? 3548 ALA A O     1 
ATOM   15881 C  CB    . ALA A 1 3548 ? 154.244 191.744 196.360 1.00 54.42  ? 3548 ALA A CB    1 
ATOM   15882 N  N     . ARG A 1 3549 ? 154.365 188.262 195.338 1.00 50.51  ? 3549 ARG A N     1 
ATOM   15883 C  CA    . ARG A 1 3549 ? 155.203 187.067 195.310 1.00 50.75  ? 3549 ARG A CA    1 
ATOM   15884 C  C     . ARG A 1 3549 ? 156.638 187.398 194.920 1.00 52.43  ? 3549 ARG A C     1 
ATOM   15885 O  O     . ARG A 1 3549 ? 157.585 186.836 195.480 1.00 53.85  ? 3549 ARG A O     1 
ATOM   15886 C  CB    . ARG A 1 3549 ? 154.619 186.034 194.348 1.00 51.67  ? 3549 ARG A CB    1 
ATOM   15887 C  CG    . ARG A 1 3549 ? 153.111 185.899 194.412 1.00 46.71  ? 3549 ARG A CG    1 
ATOM   15888 C  CD    . ARG A 1 3549 ? 152.630 184.810 193.472 1.00 45.75  ? 3549 ARG A CD    1 
ATOM   15889 N  NE    . ARG A 1 3549 ? 152.353 185.308 192.131 1.00 45.36  ? 3549 ARG A NE    1 
ATOM   15890 C  CZ    . ARG A 1 3549 ? 151.145 185.613 191.678 1.00 51.02  ? 3549 ARG A CZ    1 
ATOM   15891 N  NH1   . ARG A 1 3549 ? 150.072 185.499 192.443 1.00 48.37  ? 3549 ARG A NH1   1 
ATOM   15892 N  NH2   . ARG A 1 3549 ? 151.010 186.038 190.426 1.00 55.21  ? 3549 ARG A NH2   1 
ATOM   15893 N  N     . THR A 1 3550 ? 156.818 188.299 193.954 1.00 50.38  ? 3550 THR A N     1 
ATOM   15894 C  CA    . THR A 1 3550 ? 158.164 188.634 193.501 1.00 48.91  ? 3550 THR A CA    1 
ATOM   15895 C  C     . THR A 1 3550 ? 158.977 189.289 194.612 1.00 54.05  ? 3550 THR A C     1 
ATOM   15896 O  O     . THR A 1 3550 ? 160.153 188.960 194.807 1.00 57.34  ? 3550 THR A O     1 
ATOM   15897 C  CB    . THR A 1 3550 ? 158.091 189.545 192.277 1.00 57.15  ? 3550 THR A CB    1 
ATOM   15898 O  OG1   . THR A 1 3550 ? 157.385 188.873 191.227 1.00 62.90  ? 3550 THR A OG1   1 
ATOM   15899 C  CG2   . THR A 1 3550 ? 159.486 189.892 191.790 1.00 59.12  ? 3550 THR A CG2   1 
ATOM   15900 N  N     . GLU A 1 3551 ? 158.368 190.215 195.351 1.00 52.40  ? 3551 GLU A N     1 
ATOM   15901 C  CA    . GLU A 1 3551 ? 159.053 190.892 196.445 1.00 52.38  ? 3551 GLU A CA    1 
ATOM   15902 C  C     . GLU A 1 3551 ? 159.110 190.071 197.724 1.00 49.23  ? 3551 GLU A C     1 
ATOM   15903 O  O     . GLU A 1 3551 ? 159.963 190.341 198.576 1.00 52.63  ? 3551 GLU A O     1 
ATOM   15904 C  CB    . GLU A 1 3551 ? 158.386 192.241 196.718 1.00 54.76  ? 3551 GLU A CB    1 
ATOM   15905 C  CG    . GLU A 1 3551 ? 158.580 193.242 195.597 1.00 60.24  ? 3551 GLU A CG    1 
ATOM   15906 C  CD    . GLU A 1 3551 ? 157.613 193.060 194.452 1.00 69.69  ? 3551 GLU A CD    1 
ATOM   15907 O  OE1   . GLU A 1 3551 ? 156.730 192.186 194.544 1.00 73.11  ? 3551 GLU A OE1   1 
ATOM   15908 O  OE2   . GLU A 1 3551 ? 157.758 193.779 193.445 1.00 74.05  ? 3551 GLU A OE2   1 
ATOM   15909 N  N     . TYR A 1 3552 ? 158.230 189.085 197.887 1.00 47.01  ? 3552 TYR A N     1 
ATOM   15910 C  CA    . TYR A 1 3552 ? 158.325 188.221 199.058 1.00 45.41  ? 3552 TYR A CA    1 
ATOM   15911 C  C     . TYR A 1 3552 ? 159.449 187.205 198.912 1.00 46.40  ? 3552 TYR A C     1 
ATOM   15912 O  O     . TYR A 1 3552 ? 160.111 186.862 199.897 1.00 53.64  ? 3552 TYR A O     1 
ATOM   15913 C  CB    . TYR A 1 3552 ? 157.000 187.503 199.301 1.00 43.92  ? 3552 TYR A CB    1 
ATOM   15914 C  CG    . TYR A 1 3552 ? 156.884 186.932 200.692 1.00 43.77  ? 3552 TYR A CG    1 
ATOM   15915 C  CD1   . TYR A 1 3552 ? 157.204 187.696 201.803 1.00 46.60  ? 3552 TYR A CD1   1 
ATOM   15916 C  CD2   . TYR A 1 3552 ? 156.480 185.622 200.894 1.00 38.60  ? 3552 TYR A CD2   1 
ATOM   15917 C  CE1   . TYR A 1 3552 ? 157.106 187.178 203.076 1.00 47.89  ? 3552 TYR A CE1   1 
ATOM   15918 C  CE2   . TYR A 1 3552 ? 156.383 185.094 202.162 1.00 37.26  ? 3552 TYR A CE2   1 
ATOM   15919 C  CZ    . TYR A 1 3552 ? 156.696 185.877 203.250 1.00 44.94  ? 3552 TYR A CZ    1 
ATOM   15920 O  OH    . TYR A 1 3552 ? 156.600 185.358 204.519 1.00 50.90  ? 3552 TYR A OH    1 
ATOM   15921 N  N     . LEU A 1 3553 ? 159.678 186.716 197.696 1.00 45.20  ? 3553 LEU A N     1 
ATOM   15922 C  CA    . LEU A 1 3553 ? 160.627 185.643 197.445 1.00 42.70  ? 3553 LEU A CA    1 
ATOM   15923 C  C     . LEU A 1 3553 ? 161.951 186.140 196.883 1.00 45.54  ? 3553 LEU A C     1 
ATOM   15924 O  O     . LEU A 1 3553 ? 162.765 185.327 196.437 1.00 50.31  ? 3553 LEU A O     1 
ATOM   15925 C  CB    . LEU A 1 3553 ? 160.008 184.621 196.494 1.00 40.85  ? 3553 LEU A CB    1 
ATOM   15926 C  CG    . LEU A 1 3553 ? 158.742 183.940 197.012 1.00 36.02  ? 3553 LEU A CG    1 
ATOM   15927 C  CD1   . LEU A 1 3553 ? 158.142 183.049 195.946 1.00 32.08  ? 3553 LEU A CD1   1 
ATOM   15928 C  CD2   . LEU A 1 3553 ? 159.056 183.147 198.259 1.00 35.32  ? 3553 LEU A CD2   1 
ATOM   15929 N  N     . SER A 1 3554 ? 162.183 187.449 196.887 1.00 47.75  ? 3554 SER A N     1 
ATOM   15930 C  CA    . SER A 1 3554 ? 163.420 188.008 196.359 1.00 51.63  ? 3554 SER A CA    1 
ATOM   15931 C  C     . SER A 1 3554 ? 163.633 189.382 196.975 1.00 58.76  ? 3554 SER A C     1 
ATOM   15932 O  O     . SER A 1 3554 ? 162.725 189.967 197.566 1.00 60.97  ? 3554 SER A O     1 
ATOM   15933 C  CB    . SER A 1 3554 ? 163.387 188.088 194.830 1.00 51.21  ? 3554 SER A CB    1 
ATOM   15934 O  OG    . SER A 1 3554 ? 162.460 189.064 194.394 1.00 52.80  ? 3554 SER A OG    1 
ATOM   15935 N  N     . ASN A 1 3555 ? 164.855 189.888 196.831 1.00 59.97  ? 3555 ASN A N     1 
ATOM   15936 C  CA    . ASN A 1 3555 ? 165.210 191.215 197.306 1.00 60.06  ? 3555 ASN A CA    1 
ATOM   15937 C  C     . ASN A 1 3555 ? 165.697 192.054 196.134 1.00 60.31  ? 3555 ASN A C     1 
ATOM   15938 O  O     . ASN A 1 3555 ? 165.877 191.560 195.018 1.00 59.59  ? 3555 ASN A O     1 
ATOM   15939 C  CB    . ASN A 1 3555 ? 166.274 191.156 198.411 1.00 61.39  ? 3555 ASN A CB    1 
ATOM   15940 C  CG    . ASN A 1 3555 ? 167.444 190.268 198.048 1.00 64.64  ? 3555 ASN A CG    1 
ATOM   15941 O  OD1   . ASN A 1 3555 ? 167.281 189.072 197.814 1.00 62.78  ? 3555 ASN A OD1   1 
ATOM   15942 N  ND2   . ASN A 1 3555 ? 168.636 190.848 198.011 1.00 68.48  ? 3555 ASN A ND2   1 
ATOM   15943 N  N     . ALA A 1 3556 ? 165.903 193.346 196.402 1.00 64.41  ? 3556 ALA A N     1 
ATOM   15944 C  CA    . ALA A 1 3556 ? 166.254 194.281 195.338 1.00 61.22  ? 3556 ALA A CA    1 
ATOM   15945 C  C     . ALA A 1 3556 ? 167.603 193.945 194.717 1.00 64.41  ? 3556 ALA A C     1 
ATOM   15946 O  O     . ALA A 1 3556 ? 167.804 194.141 193.513 1.00 71.02  ? 3556 ALA A O     1 
ATOM   15947 C  CB    . ALA A 1 3556 ? 166.256 195.710 195.876 1.00 63.37  ? 3556 ALA A CB    1 
ATOM   15948 N  N     . ASP A 1 3557 ? 168.545 193.452 195.522 1.00 63.67  ? 3557 ASP A N     1 
ATOM   15949 C  CA    . ASP A 1 3557 ? 169.877 193.145 195.009 1.00 63.62  ? 3557 ASP A CA    1 
ATOM   15950 C  C     . ASP A 1 3557 ? 169.823 192.047 193.953 1.00 66.31  ? 3557 ASP A C     1 
ATOM   15951 O  O     . ASP A 1 3557 ? 170.414 192.174 192.874 1.00 74.81  ? 3557 ASP A O     1 
ATOM   15952 C  CB    . ASP A 1 3557 ? 170.795 192.739 196.160 1.00 65.58  ? 3557 ASP A CB    1 
ATOM   15953 C  CG    . ASP A 1 3557 ? 170.752 193.722 197.310 1.00 79.45  ? 3557 ASP A CG    1 
ATOM   15954 O  OD1   . ASP A 1 3557 ? 170.698 194.942 197.048 1.00 79.42  ? 3557 ASP A OD1   1 
ATOM   15955 O  OD2   . ASP A 1 3557 ? 170.772 193.276 198.476 1.00 84.05  ? 3557 ASP A OD2   1 
ATOM   15956 N  N     . GLU A 1 3558 ? 169.110 190.958 194.246 1.00 62.44  ? 3558 GLU A N     1 
ATOM   15957 C  CA    . GLU A 1 3558 ? 169.019 189.857 193.295 1.00 59.68  ? 3558 GLU A CA    1 
ATOM   15958 C  C     . GLU A 1 3558 ? 168.265 190.269 192.039 1.00 59.37  ? 3558 GLU A C     1 
ATOM   15959 O  O     . GLU A 1 3558 ? 168.626 189.858 190.932 1.00 67.42  ? 3558 GLU A O     1 
ATOM   15960 C  CB    . GLU A 1 3558 ? 168.355 188.649 193.953 1.00 65.75  ? 3558 GLU A CB    1 
ATOM   15961 C  CG    . GLU A 1 3558 ? 169.193 188.027 195.055 1.00 82.03  ? 3558 GLU A CG    1 
ATOM   15962 C  CD    . GLU A 1 3558 ? 168.514 186.844 195.709 1.00 88.10  ? 3558 GLU A CD    1 
ATOM   15963 O  OE1   . GLU A 1 3558 ? 167.336 186.585 195.391 1.00 83.35  ? 3558 GLU A OE1   1 
ATOM   15964 O  OE2   . GLU A 1 3558 ? 169.162 186.170 196.537 1.00 80.61  ? 3558 GLU A OE2   1 
ATOM   15965 N  N     . ARG A 1 3559 ? 167.212 191.075 192.187 1.00 58.61  ? 3559 ARG A N     1 
ATOM   15966 C  CA    . ARG A 1 3559 ? 166.477 191.543 191.016 1.00 59.00  ? 3559 ARG A CA    1 
ATOM   15967 C  C     . ARG A 1 3559 ? 167.339 192.446 190.143 1.00 63.94  ? 3559 ARG A C     1 
ATOM   15968 O  O     . ARG A 1 3559 ? 167.297 192.353 188.911 1.00 65.69  ? 3559 ARG A O     1 
ATOM   15969 C  CB    . ARG A 1 3559 ? 165.207 192.269 191.451 1.00 58.83  ? 3559 ARG A CB    1 
ATOM   15970 C  CG    . ARG A 1 3559 ? 164.013 191.361 191.654 1.00 51.87  ? 3559 ARG A CG    1 
ATOM   15971 C  CD    . ARG A 1 3559 ? 162.893 192.123 192.320 1.00 48.28  ? 3559 ARG A CD    1 
ATOM   15972 N  NE    . ARG A 1 3559 ? 163.155 192.331 193.737 1.00 54.45  ? 3559 ARG A NE    1 
ATOM   15973 C  CZ    . ARG A 1 3559 ? 162.379 193.042 194.539 1.00 61.65  ? 3559 ARG A CZ    1 
ATOM   15974 N  NH1   . ARG A 1 3559 ? 161.314 193.676 194.082 1.00 65.79  ? 3559 ARG A NH1   1 
ATOM   15975 N  NH2   . ARG A 1 3559 ? 162.687 193.132 195.830 1.00 60.02  ? 3559 ARG A NH2   1 
ATOM   15976 N  N     . LEU A 1 3560 ? 168.124 193.330 190.762 1.00 64.28  ? 3560 LEU A N     1 
ATOM   15977 C  CA    . LEU A 1 3560 ? 169.040 194.169 189.995 1.00 65.51  ? 3560 LEU A CA    1 
ATOM   15978 C  C     . LEU A 1 3560 ? 170.096 193.328 189.291 1.00 69.30  ? 3560 LEU A C     1 
ATOM   15979 O  O     . LEU A 1 3560 ? 170.463 193.615 188.146 1.00 70.55  ? 3560 LEU A O     1 
ATOM   15980 C  CB    . LEU A 1 3560 ? 169.701 195.203 190.905 1.00 61.89  ? 3560 LEU A CB    1 
ATOM   15981 C  CG    . LEU A 1 3560 ? 168.913 196.488 191.162 1.00 69.23  ? 3560 LEU A CG    1 
ATOM   15982 C  CD1   . LEU A 1 3560 ? 169.251 197.057 192.530 1.00 65.96  ? 3560 LEU A CD1   1 
ATOM   15983 C  CD2   . LEU A 1 3560 ? 169.188 197.507 190.069 1.00 72.28  ? 3560 LEU A CD2   1 
ATOM   15984 N  N     . ARG A 1 3561 ? 170.602 192.293 189.963 1.00 67.30  ? 3561 ARG A N     1 
ATOM   15985 C  CA    . ARG A 1 3561 ? 171.569 191.403 189.328 1.00 62.31  ? 3561 ARG A CA    1 
ATOM   15986 C  C     . ARG A 1 3561 ? 170.947 190.670 188.146 1.00 63.01  ? 3561 ARG A C     1 
ATOM   15987 O  O     . ARG A 1 3561 ? 171.597 190.480 187.112 1.00 68.93  ? 3561 ARG A O     1 
ATOM   15988 C  CB    . ARG A 1 3561 ? 172.118 190.414 190.355 1.00 60.90  ? 3561 ARG A CB    1 
ATOM   15989 C  CG    . ARG A 1 3561 ? 173.036 189.356 189.776 1.00 65.28  ? 3561 ARG A CG    1 
ATOM   15990 C  CD    . ARG A 1 3561 ? 173.838 188.675 190.872 1.00 70.65  ? 3561 ARG A CD    1 
ATOM   15991 N  NE    . ARG A 1 3561 ? 172.993 188.157 191.941 1.00 72.61  ? 3561 ARG A NE    1 
ATOM   15992 C  CZ    . ARG A 1 3561 ? 172.200 187.100 191.830 1.00 69.80  ? 3561 ARG A CZ    1 
ATOM   15993 N  NH1   . ARG A 1 3561 ? 172.122 186.408 190.706 1.00 62.29  ? 3561 ARG A NH1   1 
ATOM   15994 N  NH2   . ARG A 1 3561 ? 171.470 186.725 192.876 1.00 70.39  ? 3561 ARG A NH2   1 
ATOM   15995 N  N     . TRP A 1 3562 ? 169.689 190.246 188.283 1.00 61.18  ? 3562 TRP A N     1 
ATOM   15996 C  CA    . TRP A 1 3562 ? 168.992 189.615 187.167 1.00 61.58  ? 3562 TRP A CA    1 
ATOM   15997 C  C     . TRP A 1 3562 ? 168.824 190.582 186.003 1.00 65.15  ? 3562 TRP A C     1 
ATOM   15998 O  O     . TRP A 1 3562 ? 169.020 190.207 184.842 1.00 66.12  ? 3562 TRP A O     1 
ATOM   15999 C  CB    . TRP A 1 3562 ? 167.627 189.101 187.621 1.00 57.66  ? 3562 TRP A CB    1 
ATOM   16000 C  CG    . TRP A 1 3562 ? 167.680 188.051 188.676 1.00 58.29  ? 3562 TRP A CG    1 
ATOM   16001 C  CD1   . TRP A 1 3562 ? 168.752 187.286 189.020 1.00 58.20  ? 3562 TRP A CD1   1 
ATOM   16002 C  CD2   . TRP A 1 3562 ? 166.607 187.650 189.534 1.00 60.68  ? 3562 TRP A CD2   1 
ATOM   16003 N  NE1   . TRP A 1 3562 ? 168.414 186.430 190.039 1.00 60.40  ? 3562 TRP A NE1   1 
ATOM   16004 C  CE2   . TRP A 1 3562 ? 167.101 186.635 190.373 1.00 59.52  ? 3562 TRP A CE2   1 
ATOM   16005 C  CE3   . TRP A 1 3562 ? 165.275 188.051 189.673 1.00 53.64  ? 3562 TRP A CE3   1 
ATOM   16006 C  CZ2   . TRP A 1 3562 ? 166.313 186.016 191.336 1.00 56.74  ? 3562 TRP A CZ2   1 
ATOM   16007 C  CZ3   . TRP A 1 3562 ? 164.495 187.436 190.630 1.00 46.50  ? 3562 TRP A CZ3   1 
ATOM   16008 C  CH2   . TRP A 1 3562 ? 165.015 186.430 191.449 1.00 50.91  ? 3562 TRP A CH2   1 
ATOM   16009 N  N     . GLN A 1 3563 ? 168.448 191.830 186.294 1.00 64.94  ? 3563 GLN A N     1 
ATOM   16010 C  CA    . GLN A 1 3563 ? 168.313 192.824 185.234 1.00 66.34  ? 3563 GLN A CA    1 
ATOM   16011 C  C     . GLN A 1 3563 ? 169.654 193.130 184.582 1.00 68.41  ? 3563 GLN A C     1 
ATOM   16012 O  O     . GLN A 1 3563 ? 169.698 193.486 183.399 1.00 72.02  ? 3563 GLN A O     1 
ATOM   16013 C  CB    . GLN A 1 3563 ? 167.681 194.105 185.778 1.00 71.07  ? 3563 GLN A CB    1 
ATOM   16014 C  CG    . GLN A 1 3563 ? 166.291 193.921 186.369 1.00 70.98  ? 3563 GLN A CG    1 
ATOM   16015 C  CD    . GLN A 1 3563 ? 165.359 193.146 185.459 1.00 73.03  ? 3563 GLN A CD    1 
ATOM   16016 O  OE1   . GLN A 1 3563 ? 165.300 193.391 184.255 1.00 75.40  ? 3563 GLN A OE1   1 
ATOM   16017 N  NE2   . GLN A 1 3563 ? 164.622 192.203 186.034 1.00 68.32  ? 3563 GLN A NE2   1 
ATOM   16018 N  N     . ALA A 1 3564 ? 170.751 193.010 185.334 1.00 62.39  ? 3564 ALA A N     1 
ATOM   16019 C  CA    . ALA A 1 3564 ? 172.075 193.098 184.727 1.00 60.00  ? 3564 ALA A CA    1 
ATOM   16020 C  C     . ALA A 1 3564 ? 172.282 191.970 183.726 1.00 64.21  ? 3564 ALA A C     1 
ATOM   16021 O  O     . ALA A 1 3564 ? 172.848 192.181 182.647 1.00 64.65  ? 3564 ALA A O     1 
ATOM   16022 C  CB    . ALA A 1 3564 ? 173.155 193.068 185.806 1.00 57.88  ? 3564 ALA A CB    1 
ATOM   16023 N  N     . SER A 1 3565 ? 171.830 190.766 184.067 1.00 65.13  ? 3565 SER A N     1 
ATOM   16024 C  CA    . SER A 1 3565 ? 171.765 189.680 183.105 1.00 62.68  ? 3565 SER A CA    1 
ATOM   16025 C  C     . SER A 1 3565 ? 170.626 189.939 182.120 1.00 66.19  ? 3565 SER A C     1 
ATOM   16026 O  O     . SER A 1 3565 ? 169.934 190.959 182.177 1.00 69.76  ? 3565 SER A O     1 
ATOM   16027 C  CB    . SER A 1 3565 ? 171.583 188.346 183.824 1.00 57.59  ? 3565 SER A CB    1 
ATOM   16028 O  OG    . SER A 1 3565 ? 172.534 188.193 184.862 1.00 54.61  ? 3565 SER A OG    1 
ATOM   16029 N  N     . SER A 1 3566 ? 170.419 189.000 181.203 1.00 59.55  ? 3566 SER A N     1 
ATOM   16030 C  CA    . SER A 1 3566 ? 169.417 189.175 180.153 1.00 64.38  ? 3566 SER A CA    1 
ATOM   16031 C  C     . SER A 1 3566 ? 168.060 188.622 180.593 1.00 60.03  ? 3566 SER A C     1 
ATOM   16032 O  O     . SER A 1 3566 ? 167.462 187.764 179.945 1.00 63.04  ? 3566 SER A O     1 
ATOM   16033 C  CB    . SER A 1 3566 ? 169.889 188.520 178.862 1.00 74.60  ? 3566 SER A CB    1 
ATOM   16034 O  OG    . SER A 1 3566 ? 171.153 189.023 178.467 1.00 77.62  ? 3566 SER A OG    1 
ATOM   16035 N  N     . LEU A 1 3567 ? 167.575 189.138 181.719 1.00 57.92  ? 3567 LEU A N     1 
ATOM   16036 C  CA    . LEU A 1 3567 ? 166.245 188.787 182.203 1.00 57.19  ? 3567 LEU A CA    1 
ATOM   16037 C  C     . LEU A 1 3567 ? 165.293 189.944 181.941 1.00 60.07  ? 3567 LEU A C     1 
ATOM   16038 O  O     . LEU A 1 3567 ? 165.462 191.022 182.532 1.00 61.24  ? 3567 LEU A O     1 
ATOM   16039 C  CB    . LEU A 1 3567 ? 166.266 188.446 183.693 1.00 52.02  ? 3567 LEU A CB    1 
ATOM   16040 C  CG    . LEU A 1 3567 ? 164.915 187.952 184.216 1.00 49.51  ? 3567 LEU A CG    1 
ATOM   16041 C  CD1   . LEU A 1 3567 ? 164.675 186.508 183.811 1.00 44.54  ? 3567 LEU A CD1   1 
ATOM   16042 C  CD2   . LEU A 1 3567 ? 164.809 188.110 185.719 1.00 49.59  ? 3567 LEU A CD2   1 
ATOM   16043 N  N     . PRO A 1 3568 ? 164.303 189.780 181.065 1.00 59.18  ? 3568 PRO A N     1 
ATOM   16044 C  CA    . PRO A 1 3568 ? 163.353 190.870 180.812 1.00 58.24  ? 3568 PRO A CA    1 
ATOM   16045 C  C     . PRO A 1 3568 ? 162.612 191.272 182.079 1.00 58.33  ? 3568 PRO A C     1 
ATOM   16046 O  O     . PRO A 1 3568 ? 162.307 190.439 182.935 1.00 62.41  ? 3568 PRO A O     1 
ATOM   16047 C  CB    . PRO A 1 3568 ? 162.399 190.282 179.765 1.00 55.92  ? 3568 PRO A CB    1 
ATOM   16048 C  CG    . PRO A 1 3568 ? 162.740 188.830 179.655 1.00 55.15  ? 3568 PRO A CG    1 
ATOM   16049 C  CD    . PRO A 1 3568 ? 164.130 188.654 180.136 1.00 54.64  ? 3568 PRO A CD    1 
ATOM   16050 N  N     . ALA A 1 3569 ? 162.328 192.570 182.192 1.00 58.41  ? 3569 ALA A N     1 
ATOM   16051 C  CA    . ALA A 1 3569 ? 161.687 193.129 183.382 1.00 60.51  ? 3569 ALA A CA    1 
ATOM   16052 C  C     . ALA A 1 3569 ? 160.168 192.990 183.266 1.00 62.12  ? 3569 ALA A C     1 
ATOM   16053 O  O     . ALA A 1 3569 ? 159.426 193.953 183.066 1.00 64.75  ? 3569 ALA A O     1 
ATOM   16054 C  CB    . ALA A 1 3569 ? 162.103 194.580 183.578 1.00 55.03  ? 3569 ALA A CB    1 
ATOM   16055 N  N     . ASP A 1 3570 ? 159.710 191.749 183.401 1.00 61.19  ? 3570 ASP A N     1 
ATOM   16056 C  CA    . ASP A 1 3570 ? 158.292 191.428 183.379 1.00 58.42  ? 3570 ASP A CA    1 
ATOM   16057 C  C     . ASP A 1 3570 ? 157.945 190.615 184.617 1.00 57.09  ? 3570 ASP A C     1 
ATOM   16058 O  O     . ASP A 1 3570 ? 158.799 189.948 185.204 1.00 62.37  ? 3570 ASP A O     1 
ATOM   16059 C  CB    . ASP A 1 3570 ? 157.904 190.651 182.114 1.00 54.33  ? 3570 ASP A CB    1 
ATOM   16060 C  CG    . ASP A 1 3570 ? 158.551 191.212 180.865 1.00 63.30  ? 3570 ASP A CG    1 
ATOM   16061 O  OD1   . ASP A 1 3570 ? 158.419 192.429 180.620 1.00 67.55  ? 3570 ASP A OD1   1 
ATOM   16062 O  OD2   . ASP A 1 3570 ? 159.186 190.435 180.122 1.00 61.24  ? 3570 ASP A OD2   1 
ATOM   16063 N  N     . ASP A 1 3571 ? 156.672 190.683 185.013 1.00 52.98  ? 3571 ASP A N     1 
ATOM   16064 C  CA    . ASP A 1 3571 ? 156.228 189.939 186.188 1.00 51.18  ? 3571 ASP A CA    1 
ATOM   16065 C  C     . ASP A 1 3571 ? 156.397 188.440 185.984 1.00 47.03  ? 3571 ASP A C     1 
ATOM   16066 O  O     . ASP A 1 3571 ? 156.867 187.729 186.882 1.00 50.45  ? 3571 ASP A O     1 
ATOM   16067 C  CB    . ASP A 1 3571 ? 154.770 190.276 186.497 1.00 61.68  ? 3571 ASP A CB    1 
ATOM   16068 C  CG    . ASP A 1 3571 ? 154.529 191.768 186.618 1.00 72.04  ? 3571 ASP A CG    1 
ATOM   16069 O  OD1   . ASP A 1 3571 ? 155.501 192.542 186.489 1.00 73.89  ? 3571 ASP A OD1   1 
ATOM   16070 O  OD2   . ASP A 1 3571 ? 153.367 192.169 186.836 1.00 69.79  ? 3571 ASP A OD2   1 
ATOM   16071 N  N     . LEU A 1 3572 ? 156.030 187.944 184.800 1.00 43.66  ? 3572 LEU A N     1 
ATOM   16072 C  CA    . LEU A 1 3572 ? 156.202 186.527 184.501 1.00 39.90  ? 3572 LEU A CA    1 
ATOM   16073 C  C     . LEU A 1 3572 ? 157.668 186.128 184.558 1.00 43.78  ? 3572 LEU A C     1 
ATOM   16074 O  O     . LEU A 1 3572 ? 158.013 185.082 185.117 1.00 47.49  ? 3572 LEU A O     1 
ATOM   16075 C  CB    . LEU A 1 3572 ? 155.617 186.211 183.125 1.00 43.23  ? 3572 LEU A CB    1 
ATOM   16076 C  CG    . LEU A 1 3572 ? 155.695 184.761 182.652 1.00 36.24  ? 3572 LEU A CG    1 
ATOM   16077 C  CD1   . LEU A 1 3572 ? 154.495 183.975 183.144 1.00 40.86  ? 3572 LEU A CD1   1 
ATOM   16078 C  CD2   . LEU A 1 3572 ? 155.795 184.701 181.139 1.00 38.41  ? 3572 LEU A CD2   1 
ATOM   16079 N  N     . CYS A 1 3573 ? 158.549 186.956 183.994 1.00 47.55  ? 3573 CYS A N     1 
ATOM   16080 C  CA    . CYS A 1 3573 ? 159.968 186.621 183.975 1.00 39.50  ? 3573 CYS A CA    1 
ATOM   16081 C  C     . CYS A 1 3573 ? 160.579 186.689 185.369 1.00 40.61  ? 3573 CYS A C     1 
ATOM   16082 O  O     . CYS A 1 3573 ? 161.434 185.867 185.711 1.00 48.78  ? 3573 CYS A O     1 
ATOM   16083 C  CB    . CYS A 1 3573 ? 160.707 187.541 183.009 1.00 45.75  ? 3573 CYS A CB    1 
ATOM   16084 S  SG    . CYS A 1 3573 ? 159.966 187.580 181.365 1.00 75.14  ? 3573 CYS A SG    1 
ATOM   16085 N  N     . THR A 1 3574 ? 160.160 187.655 186.189 1.00 42.81  ? 3574 THR A N     1 
ATOM   16086 C  CA    . THR A 1 3574 ? 160.657 187.706 187.562 1.00 42.03  ? 3574 THR A CA    1 
ATOM   16087 C  C     . THR A 1 3574 ? 160.195 186.495 188.364 1.00 41.77  ? 3574 THR A C     1 
ATOM   16088 O  O     . THR A 1 3574 ? 160.982 185.906 189.116 1.00 46.57  ? 3574 THR A O     1 
ATOM   16089 C  CB    . THR A 1 3574 ? 160.216 188.999 188.245 1.00 41.42  ? 3574 THR A CB    1 
ATOM   16090 O  OG1   . THR A 1 3574 ? 158.793 189.130 188.157 1.00 48.43  ? 3574 THR A OG1   1 
ATOM   16091 C  CG2   . THR A 1 3574 ? 160.880 190.201 187.593 1.00 48.33  ? 3574 THR A CG2   1 
ATOM   16092 N  N     . GLU A 1 3575 ? 158.928 186.101 188.214 1.00 39.60  ? 3575 GLU A N     1 
ATOM   16093 C  CA    . GLU A 1 3575 ? 158.450 184.904 188.899 1.00 37.46  ? 3575 GLU A CA    1 
ATOM   16094 C  C     . GLU A 1 3575 ? 159.198 183.665 188.425 1.00 40.99  ? 3575 GLU A C     1 
ATOM   16095 O  O     . GLU A 1 3575 ? 159.566 182.801 189.231 1.00 46.96  ? 3575 GLU A O     1 
ATOM   16096 C  CB    . GLU A 1 3575 ? 156.948 184.739 188.677 1.00 36.51  ? 3575 GLU A CB    1 
ATOM   16097 C  CG    . GLU A 1 3575 ? 156.099 185.761 189.405 1.00 44.84  ? 3575 GLU A CG    1 
ATOM   16098 C  CD    . GLU A 1 3575 ? 154.637 185.678 189.017 1.00 59.06  ? 3575 GLU A CD    1 
ATOM   16099 O  OE1   . GLU A 1 3575 ? 154.299 184.855 188.140 1.00 54.93  ? 3575 GLU A OE1   1 
ATOM   16100 O  OE2   . GLU A 1 3575 ? 153.827 186.435 189.588 1.00 56.51  ? 3575 GLU A OE2   1 
ATOM   16101 N  N     . ASN A 1 3576 ? 159.440 183.565 187.118 1.00 34.52  ? 3576 ASN A N     1 
ATOM   16102 C  CA    . ASN A 1 3576 ? 160.173 182.429 186.576 1.00 28.43  ? 3576 ASN A CA    1 
ATOM   16103 C  C     . ASN A 1 3576 ? 161.608 182.396 187.087 1.00 29.63  ? 3576 ASN A C     1 
ATOM   16104 O  O     . ASN A 1 3576 ? 162.146 181.321 187.366 1.00 36.49  ? 3576 ASN A O     1 
ATOM   16105 C  CB    . ASN A 1 3576 ? 160.138 182.479 185.053 1.00 29.44  ? 3576 ASN A CB    1 
ATOM   16106 C  CG    . ASN A 1 3576 ? 158.768 182.170 184.495 1.00 35.42  ? 3576 ASN A CG    1 
ATOM   16107 O  OD1   . ASN A 1 3576 ? 157.836 181.877 185.240 1.00 41.84  ? 3576 ASN A OD1   1 
ATOM   16108 N  ND2   . ASN A 1 3576 ? 158.637 182.238 183.177 1.00 34.07  ? 3576 ASN A ND2   1 
ATOM   16109 N  N     . ALA A 1 3577 ? 162.248 183.560 187.209 1.00 29.28  ? 3577 ALA A N     1 
ATOM   16110 C  CA    . ALA A 1 3577 ? 163.590 183.610 187.779 1.00 31.43  ? 3577 ALA A CA    1 
ATOM   16111 C  C     . ALA A 1 3577 ? 163.581 183.191 189.242 1.00 35.08  ? 3577 ALA A C     1 
ATOM   16112 O  O     . ALA A 1 3577 ? 164.513 182.527 189.711 1.00 42.06  ? 3577 ALA A O     1 
ATOM   16113 C  CB    . ALA A 1 3577 ? 164.175 185.012 187.625 1.00 38.55  ? 3577 ALA A CB    1 
ATOM   16114 N  N     . ILE A 1 3578 ? 162.538 183.574 189.979 1.00 33.13  ? 3578 ILE A N     1 
ATOM   16115 C  CA    . ILE A 1 3578 ? 162.411 183.139 191.367 1.00 33.44  ? 3578 ILE A CA    1 
ATOM   16116 C  C     . ILE A 1 3578 ? 162.308 181.622 191.441 1.00 33.39  ? 3578 ILE A C     1 
ATOM   16117 O  O     . ILE A 1 3578 ? 162.931 180.982 192.296 1.00 40.87  ? 3578 ILE A O     1 
ATOM   16118 C  CB    . ILE A 1 3578 ? 161.203 183.823 192.029 1.00 32.86  ? 3578 ILE A CB    1 
ATOM   16119 C  CG1   . ILE A 1 3578 ? 161.526 185.287 192.313 1.00 40.57  ? 3578 ILE A CG1   1 
ATOM   16120 C  CG2   . ILE A 1 3578 ? 160.806 183.099 193.300 1.00 32.85  ? 3578 ILE A CG2   1 
ATOM   16121 C  CD1   . ILE A 1 3578 ? 160.471 185.987 193.100 1.00 42.76  ? 3578 ILE A CD1   1 
ATOM   16122 N  N     . MET A 1 3579 ? 161.519 181.022 190.548 1.00 30.82  ? 3579 MET A N     1 
ATOM   16123 C  CA    . MET A 1 3579 ? 161.440 179.563 190.505 1.00 26.70  ? 3579 MET A CA    1 
ATOM   16124 C  C     . MET A 1 3579 ? 162.783 178.948 190.131 1.00 32.11  ? 3579 MET A C     1 
ATOM   16125 O  O     . MET A 1 3579 ? 163.168 177.905 190.671 1.00 37.89  ? 3579 MET A O     1 
ATOM   16126 C  CB    . MET A 1 3579 ? 160.359 179.116 189.525 1.00 28.87  ? 3579 MET A CB    1 
ATOM   16127 C  CG    . MET A 1 3579 ? 159.038 179.820 189.710 1.00 29.89  ? 3579 MET A CG    1 
ATOM   16128 S  SD    . MET A 1 3579 ? 157.677 178.948 188.935 1.00 44.06  ? 3579 MET A SD    1 
ATOM   16129 C  CE    . MET A 1 3579 ? 156.292 179.759 189.718 1.00 39.48  ? 3579 MET A CE    1 
ATOM   16130 N  N     . LEU A 1 3580 ? 163.506 179.573 189.199 1.00 33.04  ? 3580 LEU A N     1 
ATOM   16131 C  CA    . LEU A 1 3580 ? 164.841 179.121 188.825 1.00 30.19  ? 3580 LEU A CA    1 
ATOM   16132 C  C     . LEU A 1 3580 ? 165.860 179.307 189.938 1.00 31.17  ? 3580 LEU A C     1 
ATOM   16133 O  O     . LEU A 1 3580 ? 166.954 178.741 189.852 1.00 34.72  ? 3580 LEU A O     1 
ATOM   16134 C  CB    . LEU A 1 3580 ? 165.325 179.863 187.578 1.00 27.92  ? 3580 LEU A CB    1 
ATOM   16135 C  CG    . LEU A 1 3580 ? 164.650 179.567 186.241 1.00 28.79  ? 3580 LEU A CG    1 
ATOM   16136 C  CD1   . LEU A 1 3580 ? 165.205 180.479 185.166 1.00 27.04  ? 3580 LEU A CD1   1 
ATOM   16137 C  CD2   . LEU A 1 3580 ? 164.849 178.117 185.859 1.00 31.52  ? 3580 LEU A CD2   1 
ATOM   16138 N  N     . LYS A 1 3581 ? 165.544 180.102 190.958 1.00 29.76  ? 3581 LYS A N     1 
ATOM   16139 C  CA    . LYS A 1 3581 ? 166.421 180.279 192.110 1.00 31.62  ? 3581 LYS A CA    1 
ATOM   16140 C  C     . LYS A 1 3581 ? 166.093 179.300 193.233 1.00 36.63  ? 3581 LYS A C     1 
ATOM   16141 O  O     . LYS A 1 3581 ? 166.961 178.543 193.674 1.00 42.90  ? 3581 LYS A O     1 
ATOM   16142 C  CB    . LYS A 1 3581 ? 166.334 181.723 192.618 1.00 32.10  ? 3581 LYS A CB    1 
ATOM   16143 C  CG    . LYS A 1 3581 ? 166.898 181.921 194.011 1.00 36.15  ? 3581 LYS A CG    1 
ATOM   16144 C  CD    . LYS A 1 3581 ? 167.041 183.393 194.336 1.00 47.58  ? 3581 LYS A CD    1 
ATOM   16145 C  CE    . LYS A 1 3581 ? 165.720 184.118 194.183 1.00 49.59  ? 3581 LYS A CE    1 
ATOM   16146 N  NZ    . LYS A 1 3581 ? 164.771 183.800 195.274 1.00 50.47  ? 3581 LYS A NZ    1 
ATOM   16147 N  N     . ARG A 1 3582 ? 164.850 179.305 193.706 1.00 34.13  ? 3582 ARG A N     1 
ATOM   16148 C  CA    . ARG A 1 3582 ? 164.443 178.458 194.824 1.00 31.47  ? 3582 ARG A CA    1 
ATOM   16149 C  C     . ARG A 1 3582 ? 163.776 177.188 194.301 1.00 36.78  ? 3582 ARG A C     1 
ATOM   16150 O  O     . ARG A 1 3582 ? 162.582 176.954 194.477 1.00 46.90  ? 3582 ARG A O     1 
ATOM   16151 C  CB    . ARG A 1 3582 ? 163.514 179.227 195.759 1.00 35.07  ? 3582 ARG A CB    1 
ATOM   16152 C  CG    . ARG A 1 3582 ? 163.705 180.728 195.732 1.00 37.23  ? 3582 ARG A CG    1 
ATOM   16153 C  CD    . ARG A 1 3582 ? 162.543 181.436 196.397 1.00 32.54  ? 3582 ARG A CD    1 
ATOM   16154 N  NE    . ARG A 1 3582 ? 162.636 181.396 197.850 1.00 35.66  ? 3582 ARG A NE    1 
ATOM   16155 C  CZ    . ARG A 1 3582 ? 163.441 182.160 198.575 1.00 39.30  ? 3582 ARG A CZ    1 
ATOM   16156 N  NH1   . ARG A 1 3582 ? 164.232 183.059 198.015 1.00 37.58  ? 3582 ARG A NH1   1 
ATOM   16157 N  NH2   . ARG A 1 3582 ? 163.450 182.022 199.897 1.00 41.38  ? 3582 ARG A NH2   1 
ATOM   16158 N  N     . PHE A 1 3583 ? 164.578 176.355 193.650 1.00 35.10  ? 3583 PHE A N     1 
ATOM   16159 C  CA    . PHE A 1 3583 ? 164.105 175.085 193.121 1.00 36.16  ? 3583 PHE A CA    1 
ATOM   16160 C  C     . PHE A 1 3583 ? 164.764 173.933 193.867 1.00 44.03  ? 3583 PHE A C     1 
ATOM   16161 O  O     . PHE A 1 3583 ? 165.953 173.990 194.194 1.00 49.13  ? 3583 PHE A O     1 
ATOM   16162 C  CB    . PHE A 1 3583 ? 164.371 174.974 191.613 1.00 33.29  ? 3583 PHE A CB    1 
ATOM   16163 C  CG    . PHE A 1 3583 ? 165.825 174.829 191.248 1.00 36.09  ? 3583 PHE A CG    1 
ATOM   16164 C  CD1   . PHE A 1 3583 ? 166.424 173.583 191.184 1.00 40.91  ? 3583 PHE A CD1   1 
ATOM   16165 C  CD2   . PHE A 1 3583 ? 166.588 175.941 190.959 1.00 40.22  ? 3583 PHE A CD2   1 
ATOM   16166 C  CE1   . PHE A 1 3583 ? 167.752 173.454 190.848 1.00 41.84  ? 3583 PHE A CE1   1 
ATOM   16167 C  CE2   . PHE A 1 3583 ? 167.919 175.817 190.621 1.00 41.97  ? 3583 PHE A CE2   1 
ATOM   16168 C  CZ    . PHE A 1 3583 ? 168.500 174.572 190.566 1.00 42.90  ? 3583 PHE A CZ    1 
ATOM   16169 N  N     . ASN A 1 3584 ? 163.976 172.900 194.155 1.00 46.23  ? 3584 ASN A N     1 
ATOM   16170 C  CA    . ASN A 1 3584 ? 164.502 171.657 194.701 1.00 47.55  ? 3584 ASN A CA    1 
ATOM   16171 C  C     . ASN A 1 3584 ? 164.677 170.583 193.641 1.00 46.61  ? 3584 ASN A C     1 
ATOM   16172 O  O     . ASN A 1 3584 ? 165.477 169.662 193.832 1.00 56.63  ? 3584 ASN A O     1 
ATOM   16173 C  CB    . ASN A 1 3584 ? 163.583 171.124 195.805 1.00 47.62  ? 3584 ASN A CB    1 
ATOM   16174 C  CG    . ASN A 1 3584 ? 163.595 171.991 197.045 1.00 50.68  ? 3584 ASN A CG    1 
ATOM   16175 O  OD1   . ASN A 1 3584 ? 162.545 172.355 197.569 1.00 50.09  ? 3584 ASN A OD1   1 
ATOM   16176 N  ND2   . ASN A 1 3584 ? 164.787 172.329 197.521 1.00 51.51  ? 3584 ASN A ND2   1 
ATOM   16177 N  N     . ARG A 1 3585 ? 163.947 170.684 192.536 1.00 38.25  ? 3585 ARG A N     1 
ATOM   16178 C  CA    . ARG A 1 3585 ? 164.084 169.792 191.398 1.00 36.94  ? 3585 ARG A CA    1 
ATOM   16179 C  C     . ARG A 1 3585 ? 164.637 170.570 190.213 1.00 38.71  ? 3585 ARG A C     1 
ATOM   16180 O  O     . ARG A 1 3585 ? 164.297 171.737 190.007 1.00 43.15  ? 3585 ARG A O     1 
ATOM   16181 C  CB    . ARG A 1 3585 ? 162.741 169.160 191.030 1.00 40.70  ? 3585 ARG A CB    1 
ATOM   16182 C  CG    . ARG A 1 3585 ? 162.131 168.324 192.136 1.00 45.88  ? 3585 ARG A CG    1 
ATOM   16183 C  CD    . ARG A 1 3585 ? 160.808 167.734 191.702 1.00 37.75  ? 3585 ARG A CD    1 
ATOM   16184 N  NE    . ARG A 1 3585 ? 159.853 168.777 191.352 1.00 34.37  ? 3585 ARG A NE    1 
ATOM   16185 C  CZ    . ARG A 1 3585 ? 158.658 168.553 190.829 1.00 38.83  ? 3585 ARG A CZ    1 
ATOM   16186 N  NH1   . ARG A 1 3585 ? 158.238 167.327 190.567 1.00 42.83  ? 3585 ARG A NH1   1 
ATOM   16187 N  NH2   . ARG A 1 3585 ? 157.864 169.584 190.560 1.00 38.33  ? 3585 ARG A NH2   1 
ATOM   16188 N  N     . TYR A 1 3586 ? 165.491 169.915 189.439 1.00 39.63  ? 3586 TYR A N     1 
ATOM   16189 C  CA    . TYR A 1 3586 ? 166.180 170.579 188.342 1.00 33.49  ? 3586 TYR A CA    1 
ATOM   16190 C  C     . TYR A 1 3586 ? 165.173 171.102 187.325 1.00 31.25  ? 3586 TYR A C     1 
ATOM   16191 O  O     . TYR A 1 3586 ? 164.351 170.323 186.823 1.00 33.81  ? 3586 TYR A O     1 
ATOM   16192 C  CB    . TYR A 1 3586 ? 167.165 169.620 187.684 1.00 34.13  ? 3586 TYR A CB    1 
ATOM   16193 C  CG    . TYR A 1 3586 ? 168.259 169.161 188.621 1.00 36.65  ? 3586 TYR A CG    1 
ATOM   16194 C  CD1   . TYR A 1 3586 ? 169.035 170.081 189.310 1.00 36.08  ? 3586 TYR A CD1   1 
ATOM   16195 C  CD2   . TYR A 1 3586 ? 168.511 167.813 188.821 1.00 39.43  ? 3586 TYR A CD2   1 
ATOM   16196 C  CE1   . TYR A 1 3586 ? 170.031 169.672 190.167 1.00 39.46  ? 3586 TYR A CE1   1 
ATOM   16197 C  CE2   . TYR A 1 3586 ? 169.506 167.395 189.677 1.00 42.17  ? 3586 TYR A CE2   1 
ATOM   16198 C  CZ    . TYR A 1 3586 ? 170.263 168.329 190.347 1.00 43.00  ? 3586 TYR A CZ    1 
ATOM   16199 O  OH    . TYR A 1 3586 ? 171.258 167.918 191.202 1.00 49.59  ? 3586 TYR A OH    1 
ATOM   16200 N  N     . PRO A 1 3587 ? 165.199 172.389 186.995 1.00 29.26  ? 3587 PRO A N     1 
ATOM   16201 C  CA    . PRO A 1 3587 ? 164.111 172.979 186.215 1.00 27.05  ? 3587 PRO A CA    1 
ATOM   16202 C  C     . PRO A 1 3587 ? 164.176 172.638 184.737 1.00 23.18  ? 3587 PRO A C     1 
ATOM   16203 O  O     . PRO A 1 3587 ? 165.232 172.334 184.181 1.00 29.66  ? 3587 PRO A O     1 
ATOM   16204 C  CB    . PRO A 1 3587 ? 164.300 174.483 186.438 1.00 23.30  ? 3587 PRO A CB    1 
ATOM   16205 C  CG    . PRO A 1 3587 ? 165.744 174.637 186.686 1.00 28.86  ? 3587 PRO A CG    1 
ATOM   16206 C  CD    . PRO A 1 3587 ? 166.219 173.384 187.364 1.00 29.54  ? 3587 PRO A CD    1 
ATOM   16207 N  N     . LEU A 1 3588 ? 163.007 172.695 184.104 1.00 22.00  ? 3588 LEU A N     1 
ATOM   16208 C  CA    . LEU A 1 3588 ? 162.864 172.534 182.661 1.00 21.80  ? 3588 LEU A CA    1 
ATOM   16209 C  C     . LEU A 1 3588 ? 162.315 173.842 182.110 1.00 30.09  ? 3588 LEU A C     1 
ATOM   16210 O  O     . LEU A 1 3588 ? 161.155 174.185 182.355 1.00 40.05  ? 3588 LEU A O     1 
ATOM   16211 C  CB    . LEU A 1 3588 ? 161.946 171.360 182.325 1.00 24.73  ? 3588 LEU A CB    1 
ATOM   16212 C  CG    . LEU A 1 3588 ? 161.969 170.839 180.887 1.00 27.74  ? 3588 LEU A CG    1 
ATOM   16213 C  CD1   . LEU A 1 3588 ? 161.729 169.344 180.872 1.00 34.98  ? 3588 LEU A CD1   1 
ATOM   16214 C  CD2   . LEU A 1 3588 ? 160.938 171.545 180.028 1.00 31.23  ? 3588 LEU A CD2   1 
ATOM   16215 N  N     . ILE A 1 3589 ? 163.142 174.565 181.376 1.00 30.41  ? 3589 ILE A N     1 
ATOM   16216 C  CA    . ILE A 1 3589 ? 162.784 175.874 180.846 1.00 30.22  ? 3589 ILE A CA    1 
ATOM   16217 C  C     . ILE A 1 3589 ? 162.114 175.699 179.491 1.00 39.90  ? 3589 ILE A C     1 
ATOM   16218 O  O     . ILE A 1 3589 ? 162.584 174.931 178.645 1.00 46.16  ? 3589 ILE A O     1 
ATOM   16219 C  CB    . ILE A 1 3589 ? 164.029 176.772 180.748 1.00 29.34  ? 3589 ILE A CB    1 
ATOM   16220 C  CG1   . ILE A 1 3589 ? 164.785 176.759 182.075 1.00 22.41  ? 3589 ILE A CG1   1 
ATOM   16221 C  CG2   . ILE A 1 3589 ? 163.633 178.181 180.391 1.00 38.75  ? 3589 ILE A CG2   1 
ATOM   16222 C  CD1   . ILE A 1 3589 ? 166.089 177.509 182.038 1.00 30.77  ? 3589 ILE A CD1   1 
ATOM   16223 N  N     . ILE A 1 3590 ? 161.006 176.410 179.282 1.00 36.69  ? 3590 ILE A N     1 
ATOM   16224 C  CA    . ILE A 1 3590 ? 160.195 176.234 178.081 1.00 42.19  ? 3590 ILE A CA    1 
ATOM   16225 C  C     . ILE A 1 3590 ? 160.100 177.554 177.322 1.00 46.89  ? 3590 ILE A C     1 
ATOM   16226 O  O     . ILE A 1 3590 ? 159.068 177.862 176.718 1.00 51.90  ? 3590 ILE A O     1 
ATOM   16227 C  CB    . ILE A 1 3590 ? 158.799 175.683 178.430 1.00 43.60  ? 3590 ILE A CB    1 
ATOM   16228 C  CG1   . ILE A 1 3590 ? 158.907 174.594 179.494 1.00 40.67  ? 3590 ILE A CG1   1 
ATOM   16229 C  CG2   . ILE A 1 3590 ? 158.136 175.067 177.208 1.00 47.59  ? 3590 ILE A CG2   1 
ATOM   16230 C  CD1   . ILE A 1 3590 ? 157.575 174.153 180.049 1.00 39.49  ? 3590 ILE A CD1   1 
ATOM   16231 N  N     . ASP A 1 3591 ? 161.160 178.355 177.368 1.00 47.26  ? 3591 ASP A N     1 
ATOM   16232 C  CA    . ASP A 1 3591 ? 161.154 179.619 176.644 1.00 50.33  ? 3591 ASP A CA    1 
ATOM   16233 C  C     . ASP A 1 3591 ? 161.102 179.364 175.138 1.00 60.14  ? 3591 ASP A C     1 
ATOM   16234 O  O     . ASP A 1 3591 ? 161.806 178.486 174.631 1.00 60.71  ? 3591 ASP A O     1 
ATOM   16235 C  CB    . ASP A 1 3591 ? 162.385 180.459 177.006 1.00 54.40  ? 3591 ASP A CB    1 
ATOM   16236 C  CG    . ASP A 1 3591 ? 163.706 179.727 176.780 1.00 64.19  ? 3591 ASP A CG    1 
ATOM   16237 O  OD1   . ASP A 1 3591 ? 163.983 179.266 175.656 1.00 63.12  ? 3591 ASP A OD1   1 
ATOM   16238 O  OD2   . ASP A 1 3591 ? 164.484 179.608 177.743 1.00 67.19  ? 3591 ASP A OD2   1 
ATOM   16239 N  N     . PRO A 1 3592 ? 160.244 180.067 174.402 1.00 60.00  ? 3592 PRO A N     1 
ATOM   16240 C  CA    . PRO A 1 3592 ? 160.269 179.980 172.937 1.00 57.57  ? 3592 PRO A CA    1 
ATOM   16241 C  C     . PRO A 1 3592 ? 161.287 180.889 172.265 1.00 63.53  ? 3592 PRO A C     1 
ATOM   16242 O  O     . PRO A 1 3592 ? 161.534 180.723 171.065 1.00 65.08  ? 3592 PRO A O     1 
ATOM   16243 C  CB    . PRO A 1 3592 ? 158.846 180.410 172.551 1.00 54.01  ? 3592 PRO A CB    1 
ATOM   16244 C  CG    . PRO A 1 3592 ? 158.024 180.153 173.746 1.00 52.62  ? 3592 PRO A CG    1 
ATOM   16245 C  CD    . PRO A 1 3592 ? 158.918 180.459 174.903 1.00 52.97  ? 3592 PRO A CD    1 
ATOM   16246 N  N     . SER A 1 3593 ? 161.882 181.829 172.994 1.00 63.24  ? 3593 SER A N     1 
ATOM   16247 C  CA    . SER A 1 3593 ? 162.753 182.843 172.412 1.00 61.06  ? 3593 SER A CA    1 
ATOM   16248 C  C     . SER A 1 3593 ? 164.225 182.639 172.726 1.00 71.52  ? 3593 SER A C     1 
ATOM   16249 O  O     . SER A 1 3593 ? 165.074 182.933 171.883 1.00 81.26  ? 3593 SER A O     1 
ATOM   16250 C  CB    . SER A 1 3593 ? 162.330 184.235 172.891 1.00 62.62  ? 3593 SER A CB    1 
ATOM   16251 O  OG    . SER A 1 3593 ? 162.561 184.386 174.280 1.00 72.04  ? 3593 SER A OG    1 
ATOM   16252 N  N     . GLY A 1 3594 ? 164.554 182.144 173.915 1.00 69.40  ? 3594 GLY A N     1 
ATOM   16253 C  CA    . GLY A 1 3594 ? 165.929 181.924 174.312 1.00 64.36  ? 3594 GLY A CA    1 
ATOM   16254 C  C     . GLY A 1 3594 ? 166.487 182.961 175.259 1.00 66.88  ? 3594 GLY A C     1 
ATOM   16255 O  O     . GLY A 1 3594 ? 167.671 182.878 175.609 1.00 71.90  ? 3594 GLY A O     1 
ATOM   16256 N  N     . GLN A 1 3595 ? 165.683 183.940 175.680 1.00 67.99  ? 3595 GLN A N     1 
ATOM   16257 C  CA    . GLN A 1 3595 ? 166.155 184.908 176.665 1.00 71.38  ? 3595 GLN A CA    1 
ATOM   16258 C  C     . GLN A 1 3595 ? 166.444 184.238 178.001 1.00 66.37  ? 3595 GLN A C     1 
ATOM   16259 O  O     . GLN A 1 3595 ? 167.393 184.612 178.698 1.00 67.03  ? 3595 GLN A O     1 
ATOM   16260 C  CB    . GLN A 1 3595 ? 165.131 186.028 176.840 1.00 79.85  ? 3595 GLN A CB    1 
ATOM   16261 C  CG    . GLN A 1 3595 ? 164.982 186.933 175.632 1.00 82.81  ? 3595 GLN A CG    1 
ATOM   16262 C  CD    . GLN A 1 3595 ? 166.319 187.373 175.072 1.00 91.13  ? 3595 GLN A CD    1 
ATOM   16263 O  OE1   . GLN A 1 3595 ? 167.036 188.158 175.692 1.00 87.38  ? 3595 GLN A OE1   1 
ATOM   16264 N  NE2   . GLN A 1 3595 ? 166.661 186.869 173.891 1.00 88.45  ? 3595 GLN A NE2   1 
ATOM   16265 N  N     . ALA A 1 3596 ? 165.629 183.252 178.380 1.00 62.58  ? 3596 ALA A N     1 
ATOM   16266 C  CA    . ALA A 1 3596 ? 165.828 182.577 179.658 1.00 56.81  ? 3596 ALA A CA    1 
ATOM   16267 C  C     . ALA A 1 3596 ? 167.097 181.734 179.656 1.00 56.92  ? 3596 ALA A C     1 
ATOM   16268 O  O     . ALA A 1 3596 ? 167.802 181.665 180.669 1.00 55.69  ? 3596 ALA A O     1 
ATOM   16269 C  CB    . ALA A 1 3596 ? 164.616 181.717 179.988 1.00 51.25  ? 3596 ALA A CB    1 
ATOM   16270 N  N     . THR A 1 3597 ? 167.401 181.075 178.536 1.00 58.94  ? 3597 THR A N     1 
ATOM   16271 C  CA    . THR A 1 3597 ? 168.641 180.310 178.451 1.00 58.97  ? 3597 THR A CA    1 
ATOM   16272 C  C     . THR A 1 3597 ? 169.856 181.219 178.573 1.00 56.74  ? 3597 THR A C     1 
ATOM   16273 O  O     . THR A 1 3597 ? 170.820 180.891 179.273 1.00 59.01  ? 3597 THR A O     1 
ATOM   16274 C  CB    . THR A 1 3597 ? 168.691 179.526 177.142 1.00 62.26  ? 3597 THR A CB    1 
ATOM   16275 O  OG1   . THR A 1 3597 ? 168.672 180.438 176.037 1.00 70.63  ? 3597 THR A OG1   1 
ATOM   16276 C  CG2   . THR A 1 3597 ? 167.501 178.595 177.038 1.00 59.23  ? 3597 THR A CG2   1 
ATOM   16277 N  N     . GLU A 1 3598 ? 169.828 182.369 177.898 1.00 57.94  ? 3598 GLU A N     1 
ATOM   16278 C  CA    . GLU A 1 3598 ? 170.924 183.325 178.012 1.00 58.39  ? 3598 GLU A CA    1 
ATOM   16279 C  C     . GLU A 1 3598 ? 171.016 183.896 179.422 1.00 56.39  ? 3598 GLU A C     1 
ATOM   16280 O  O     . GLU A 1 3598 ? 172.121 184.138 179.922 1.00 59.45  ? 3598 GLU A O     1 
ATOM   16281 C  CB    . GLU A 1 3598 ? 170.747 184.433 176.974 1.00 61.78  ? 3598 GLU A CB    1 
ATOM   16282 C  CG    . GLU A 1 3598 ? 171.516 185.706 177.253 1.00 69.51  ? 3598 GLU A CG    1 
ATOM   16283 C  CD    . GLU A 1 3598 ? 171.182 186.809 176.268 1.00 82.88  ? 3598 GLU A CD    1 
ATOM   16284 O  OE1   . GLU A 1 3598 ? 170.268 186.612 175.441 1.00 83.24  ? 3598 GLU A OE1   1 
ATOM   16285 O  OE2   . GLU A 1 3598 ? 171.833 187.873 176.323 1.00 86.08  ? 3598 GLU A OE2   1 
ATOM   16286 N  N     . PHE A 1 3599 ? 169.873 184.097 180.080 1.00 54.84  ? 3599 PHE A N     1 
ATOM   16287 C  CA    . PHE A 1 3599 ? 169.869 184.503 181.482 1.00 49.18  ? 3599 PHE A CA    1 
ATOM   16288 C  C     . PHE A 1 3599 ? 170.544 183.456 182.359 1.00 51.37  ? 3599 PHE A C     1 
ATOM   16289 O  O     . PHE A 1 3599 ? 171.316 183.794 183.264 1.00 53.71  ? 3599 PHE A O     1 
ATOM   16290 C  CB    . PHE A 1 3599 ? 168.431 184.742 181.940 1.00 43.86  ? 3599 PHE A CB    1 
ATOM   16291 C  CG    . PHE A 1 3599 ? 168.271 184.851 183.427 1.00 43.04  ? 3599 PHE A CG    1 
ATOM   16292 C  CD1   . PHE A 1 3599 ? 168.808 185.919 184.120 1.00 48.17  ? 3599 PHE A CD1   1 
ATOM   16293 C  CD2   . PHE A 1 3599 ? 167.579 183.883 184.132 1.00 43.51  ? 3599 PHE A CD2   1 
ATOM   16294 C  CE1   . PHE A 1 3599 ? 168.654 186.020 185.486 1.00 47.48  ? 3599 PHE A CE1   1 
ATOM   16295 C  CE2   . PHE A 1 3599 ? 167.427 183.978 185.499 1.00 40.29  ? 3599 PHE A CE2   1 
ATOM   16296 C  CZ    . PHE A 1 3599 ? 167.966 185.047 186.176 1.00 43.96  ? 3599 PHE A CZ    1 
ATOM   16297 N  N     . ILE A 1 3600 ? 170.256 182.179 182.108 1.00 51.44  ? 3600 ILE A N     1 
ATOM   16298 C  CA    . ILE A 1 3600 ? 170.867 181.103 182.884 1.00 45.36  ? 3600 ILE A CA    1 
ATOM   16299 C  C     . ILE A 1 3600 ? 172.372 181.063 182.651 1.00 49.86  ? 3600 ILE A C     1 
ATOM   16300 O  O     . ILE A 1 3600 ? 173.156 180.893 183.593 1.00 55.27  ? 3600 ILE A O     1 
ATOM   16301 C  CB    . ILE A 1 3600 ? 170.198 179.758 182.545 1.00 40.39  ? 3600 ILE A CB    1 
ATOM   16302 C  CG1   . ILE A 1 3600 ? 168.824 179.676 183.204 1.00 38.21  ? 3600 ILE A CG1   1 
ATOM   16303 C  CG2   . ILE A 1 3600 ? 171.057 178.599 182.999 1.00 44.90  ? 3600 ILE A CG2   1 
ATOM   16304 C  CD1   . ILE A 1 3600 ? 168.878 179.745 184.709 1.00 37.78  ? 3600 ILE A CD1   1 
ATOM   16305 N  N     . MET A 1 3601 ? 172.801 181.217 181.396 1.00 47.85  ? 3601 MET A N     1 
ATOM   16306 C  CA    . MET A 1 3601 ? 174.233 181.243 181.109 1.00 50.15  ? 3601 MET A CA    1 
ATOM   16307 C  C     . MET A 1 3601 ? 174.920 182.418 181.794 1.00 53.88  ? 3601 MET A C     1 
ATOM   16308 O  O     . MET A 1 3601 ? 176.020 182.269 182.338 1.00 57.91  ? 3601 MET A O     1 
ATOM   16309 C  CB    . MET A 1 3601 ? 174.480 181.286 179.601 1.00 50.93  ? 3601 MET A CB    1 
ATOM   16310 C  CG    . MET A 1 3601 ? 173.755 180.215 178.814 1.00 59.51  ? 3601 MET A CG    1 
ATOM   16311 S  SD    . MET A 1 3601 ? 174.476 178.579 179.031 1.00 69.60  ? 3601 MET A SD    1 
ATOM   16312 C  CE    . MET A 1 3601 ? 176.221 178.969 178.996 1.00 62.13  ? 3601 MET A CE    1 
ATOM   16313 N  N     . ASN A 1 3602 ? 174.295 183.596 181.773 1.00 50.92  ? 3602 ASN A N     1 
ATOM   16314 C  CA    . ASN A 1 3602 ? 174.893 184.757 182.426 1.00 47.75  ? 3602 ASN A CA    1 
ATOM   16315 C  C     . ASN A 1 3602 ? 174.962 184.574 183.937 1.00 53.70  ? 3602 ASN A C     1 
ATOM   16316 O  O     . ASN A 1 3602 ? 175.950 184.965 184.568 1.00 64.14  ? 3602 ASN A O     1 
ATOM   16317 C  CB    . ASN A 1 3602 ? 174.111 186.020 182.075 1.00 48.22  ? 3602 ASN A CB    1 
ATOM   16318 C  CG    . ASN A 1 3602 ? 174.206 186.372 180.609 1.00 56.27  ? 3602 ASN A CG    1 
ATOM   16319 O  OD1   . ASN A 1 3602 ? 175.295 186.408 180.038 1.00 61.78  ? 3602 ASN A OD1   1 
ATOM   16320 N  ND2   . ASN A 1 3602 ? 173.065 186.639 179.990 1.00 60.61  ? 3602 ASN A ND2   1 
ATOM   16321 N  N     . GLU A 1 3603 ? 173.920 183.993 184.536 1.00 52.71  ? 3603 GLU A N     1 
ATOM   16322 C  CA    . GLU A 1 3603 ? 173.904 183.815 185.985 1.00 55.05  ? 3603 GLU A CA    1 
ATOM   16323 C  C     . GLU A 1 3603 ? 175.006 182.872 186.448 1.00 60.92  ? 3603 GLU A C     1 
ATOM   16324 O  O     . GLU A 1 3603 ? 175.662 183.127 187.464 1.00 61.91  ? 3603 GLU A O     1 
ATOM   16325 C  CB    . GLU A 1 3603 ? 172.541 183.296 186.436 1.00 47.66  ? 3603 GLU A CB    1 
ATOM   16326 C  CG    . GLU A 1 3603 ? 171.482 184.366 186.529 1.00 52.42  ? 3603 GLU A CG    1 
ATOM   16327 C  CD    . GLU A 1 3603 ? 171.731 185.329 187.671 1.00 60.60  ? 3603 GLU A CD    1 
ATOM   16328 O  OE1   . GLU A 1 3603 ? 171.715 184.887 188.838 1.00 60.21  ? 3603 GLU A OE1   1 
ATOM   16329 O  OE2   . GLU A 1 3603 ? 171.948 186.529 187.402 1.00 65.52  ? 3603 GLU A OE2   1 
ATOM   16330 N  N     . TYR A 1 3604 ? 175.225 181.780 185.718 1.00 55.64  ? 3604 TYR A N     1 
ATOM   16331 C  CA    . TYR A 1 3604 ? 176.178 180.755 186.116 1.00 52.45  ? 3604 TYR A CA    1 
ATOM   16332 C  C     . TYR A 1 3604 ? 177.478 180.835 185.328 1.00 59.05  ? 3604 TYR A C     1 
ATOM   16333 O  O     . TYR A 1 3604 ? 178.216 179.847 185.258 1.00 61.35  ? 3604 TYR A O     1 
ATOM   16334 C  CB    . TYR A 1 3604 ? 175.545 179.371 185.976 1.00 50.70  ? 3604 TYR A CB    1 
ATOM   16335 C  CG    . TYR A 1 3604 ? 174.444 179.115 186.979 1.00 54.78  ? 3604 TYR A CG    1 
ATOM   16336 C  CD1   . TYR A 1 3604 ? 173.185 179.675 186.814 1.00 54.56  ? 3604 TYR A CD1   1 
ATOM   16337 C  CD2   . TYR A 1 3604 ? 174.668 178.332 188.101 1.00 58.16  ? 3604 TYR A CD2   1 
ATOM   16338 C  CE1   . TYR A 1 3604 ? 172.179 179.453 187.729 1.00 51.38  ? 3604 TYR A CE1   1 
ATOM   16339 C  CE2   . TYR A 1 3604 ? 173.667 178.105 189.023 1.00 58.43  ? 3604 TYR A CE2   1 
ATOM   16340 C  CZ    . TYR A 1 3604 ? 172.425 178.668 188.832 1.00 54.28  ? 3604 TYR A CZ    1 
ATOM   16341 O  OH    . TYR A 1 3604 ? 171.424 178.443 189.748 1.00 54.07  ? 3604 TYR A OH    1 
ATOM   16342 N  N     . LYS A 1 3605 ? 177.772 181.993 184.733 1.00 61.87  ? 3605 LYS A N     1 
ATOM   16343 C  CA    . LYS A 1 3605 ? 179.023 182.162 184.003 1.00 58.98  ? 3605 LYS A CA    1 
ATOM   16344 C  C     . LYS A 1 3605 ? 180.224 182.050 184.934 1.00 61.52  ? 3605 LYS A C     1 
ATOM   16345 O  O     . LYS A 1 3605 ? 181.253 181.473 184.565 1.00 64.82  ? 3605 LYS A O     1 
ATOM   16346 C  CB    . LYS A 1 3605 ? 179.027 183.507 183.279 1.00 57.15  ? 3605 LYS A CB    1 
ATOM   16347 C  CG    . LYS A 1 3605 ? 180.187 183.697 182.322 1.00 59.44  ? 3605 LYS A CG    1 
ATOM   16348 C  CD    . LYS A 1 3605 ? 179.948 184.879 181.400 1.00 65.18  ? 3605 LYS A CD    1 
ATOM   16349 C  CE    . LYS A 1 3605 ? 178.637 184.732 180.645 1.00 66.46  ? 3605 LYS A CE    1 
ATOM   16350 N  NZ    . LYS A 1 3605 ? 178.385 185.883 179.736 1.00 64.21  ? 3605 LYS A NZ    1 
ATOM   16351 N  N     . ASP A 1 3606 ? 180.114 182.603 186.143 1.00 60.63  ? 3606 ASP A N     1 
ATOM   16352 C  CA    . ASP A 1 3606 ? 181.198 182.503 187.111 1.00 61.40  ? 3606 ASP A CA    1 
ATOM   16353 C  C     . ASP A 1 3606 ? 181.394 181.080 187.615 1.00 61.81  ? 3606 ASP A C     1 
ATOM   16354 O  O     . ASP A 1 3606 ? 182.477 180.756 188.113 1.00 63.22  ? 3606 ASP A O     1 
ATOM   16355 C  CB    . ASP A 1 3606 ? 180.938 183.439 188.291 1.00 66.86  ? 3606 ASP A CB    1 
ATOM   16356 C  CG    . ASP A 1 3606 ? 179.597 183.187 188.949 1.00 74.66  ? 3606 ASP A CG    1 
ATOM   16357 O  OD1   . ASP A 1 3606 ? 178.565 183.283 188.253 1.00 73.29  ? 3606 ASP A OD1   1 
ATOM   16358 O  OD2   . ASP A 1 3606 ? 179.573 182.894 190.163 1.00 71.33  ? 3606 ASP A OD2   1 
ATOM   16359 N  N     . ARG A 1 3607 ? 180.377 180.229 187.500 1.00 58.75  ? 3607 ARG A N     1 
ATOM   16360 C  CA    . ARG A 1 3607 ? 180.472 178.831 187.894 1.00 57.79  ? 3607 ARG A CA    1 
ATOM   16361 C  C     . ARG A 1 3607 ? 180.845 177.925 186.729 1.00 59.12  ? 3607 ARG A C     1 
ATOM   16362 O  O     . ARG A 1 3607 ? 180.840 176.701 186.885 1.00 62.90  ? 3607 ARG A O     1 
ATOM   16363 C  CB    . ARG A 1 3607 ? 179.155 178.367 188.520 1.00 57.36  ? 3607 ARG A CB    1 
ATOM   16364 C  CG    . ARG A 1 3607 ? 178.799 179.077 189.814 1.00 61.73  ? 3607 ARG A CG    1 
ATOM   16365 C  CD    . ARG A 1 3607 ? 177.773 178.294 190.617 1.00 62.25  ? 3607 ARG A CD    1 
ATOM   16366 N  NE    . ARG A 1 3607 ? 177.904 176.856 190.422 1.00 68.52  ? 3607 ARG A NE    1 
ATOM   16367 C  CZ    . ARG A 1 3607 ? 177.028 175.957 190.851 1.00 68.33  ? 3607 ARG A CZ    1 
ATOM   16368 N  NH1   . ARG A 1 3607 ? 175.939 176.314 191.511 1.00 68.85  ? 3607 ARG A NH1   1 
ATOM   16369 N  NH2   . ARG A 1 3607 ? 177.251 174.668 190.611 1.00 61.04  ? 3607 ARG A NH2   1 
ATOM   16370 N  N     . LYS A 1 3608 ? 181.169 178.503 185.570 1.00 56.86  ? 3608 LYS A N     1 
ATOM   16371 C  CA    . LYS A 1 3608 ? 181.588 177.760 184.381 1.00 51.60  ? 3608 LYS A CA    1 
ATOM   16372 C  C     . LYS A 1 3608 ? 180.493 176.798 183.918 1.00 50.25  ? 3608 LYS A C     1 
ATOM   16373 O  O     . LYS A 1 3608 ? 180.672 175.580 183.869 1.00 57.89  ? 3608 LYS A O     1 
ATOM   16374 C  CB    . LYS A 1 3608 ? 182.907 177.018 184.628 1.00 60.91  ? 3608 LYS A CB    1 
ATOM   16375 C  CG    . LYS A 1 3608 ? 183.941 177.805 185.417 1.00 63.78  ? 3608 LYS A CG    1 
ATOM   16376 C  CD    . LYS A 1 3608 ? 184.315 179.096 184.715 1.00 63.77  ? 3608 LYS A CD    1 
ATOM   16377 C  CE    . LYS A 1 3608 ? 185.108 180.001 185.638 1.00 70.04  ? 3608 LYS A CE    1 
ATOM   16378 N  NZ    . LYS A 1 3608 ? 186.221 179.265 186.295 1.00 72.58  ? 3608 LYS A NZ    1 
ATOM   16379 N  N     . ILE A 1 3609 ? 179.347 177.371 183.572 1.00 49.20  ? 3609 ILE A N     1 
ATOM   16380 C  CA    . ILE A 1 3609 ? 178.227 176.588 183.066 1.00 49.10  ? 3609 ILE A CA    1 
ATOM   16381 C  C     . ILE A 1 3609 ? 178.496 176.205 181.618 1.00 51.33  ? 3609 ILE A C     1 
ATOM   16382 O  O     . ILE A 1 3609 ? 179.029 177.000 180.835 1.00 57.14  ? 3609 ILE A O     1 
ATOM   16383 C  CB    . ILE A 1 3609 ? 176.909 177.372 183.210 1.00 49.84  ? 3609 ILE A CB    1 
ATOM   16384 C  CG1   . ILE A 1 3609 ? 175.732 176.552 182.681 1.00 48.09  ? 3609 ILE A CG1   1 
ATOM   16385 C  CG2   . ILE A 1 3609 ? 176.999 178.712 182.504 1.00 52.44  ? 3609 ILE A CG2   1 
ATOM   16386 C  CD1   . ILE A 1 3609 ? 174.393 177.177 182.944 1.00 48.41  ? 3609 ILE A CD1   1 
ATOM   16387 N  N     . THR A 1 3610 ? 178.141 174.975 181.259 1.00 52.30  ? 3610 THR A N     1 
ATOM   16388 C  CA    . THR A 1 3610 ? 178.369 174.452 179.921 1.00 53.37  ? 3610 THR A CA    1 
ATOM   16389 C  C     . THR A 1 3610 ? 177.037 174.205 179.227 1.00 49.71  ? 3610 THR A C     1 
ATOM   16390 O  O     . THR A 1 3610 ? 176.135 173.586 179.798 1.00 56.40  ? 3610 THR A O     1 
ATOM   16391 C  CB    . THR A 1 3610 ? 179.180 173.155 179.970 1.00 61.92  ? 3610 THR A CB    1 
ATOM   16392 O  OG1   . THR A 1 3610 ? 180.448 173.407 180.587 1.00 66.24  ? 3610 THR A OG1   1 
ATOM   16393 C  CG2   . THR A 1 3610 ? 179.409 172.612 178.568 1.00 59.80  ? 3610 THR A CG2   1 
ATOM   16394 N  N     . ARG A 1 3611 ? 176.916 174.694 177.996 1.00 45.95  ? 3611 ARG A N     1 
ATOM   16395 C  CA    . ARG A 1 3611 ? 175.697 174.534 177.211 1.00 49.39  ? 3611 ARG A CA    1 
ATOM   16396 C  C     . ARG A 1 3611 ? 175.847 173.312 176.312 1.00 53.22  ? 3611 ARG A C     1 
ATOM   16397 O  O     . ARG A 1 3611 ? 176.795 173.222 175.525 1.00 64.95  ? 3611 ARG A O     1 
ATOM   16398 C  CB    . ARG A 1 3611 ? 175.412 175.788 176.390 1.00 53.84  ? 3611 ARG A CB    1 
ATOM   16399 C  CG    . ARG A 1 3611 ? 174.078 175.754 175.668 1.00 58.34  ? 3611 ARG A CG    1 
ATOM   16400 C  CD    . ARG A 1 3611 ? 174.005 176.797 174.566 1.00 63.33  ? 3611 ARG A CD    1 
ATOM   16401 N  NE    . ARG A 1 3611 ? 174.244 178.148 175.055 1.00 65.96  ? 3611 ARG A NE    1 
ATOM   16402 C  CZ    . ARG A 1 3611 ? 173.353 179.129 175.004 1.00 72.93  ? 3611 ARG A CZ    1 
ATOM   16403 N  NH1   . ARG A 1 3611 ? 172.142 178.937 174.506 1.00 68.65  ? 3611 ARG A NH1   1 
ATOM   16404 N  NH2   . ARG A 1 3611 ? 173.684 180.332 175.463 1.00 71.73  ? 3611 ARG A NH2   1 
ATOM   16405 N  N     . THR A 1 3612 ? 174.913 172.376 176.429 1.00 44.76  ? 3612 THR A N     1 
ATOM   16406 C  CA    . THR A 1 3612 ? 174.881 171.151 175.647 1.00 45.97  ? 3612 THR A CA    1 
ATOM   16407 C  C     . THR A 1 3612 ? 173.466 170.964 175.110 1.00 50.71  ? 3612 THR A C     1 
ATOM   16408 O  O     . THR A 1 3612 ? 172.528 171.640 175.532 1.00 59.23  ? 3612 THR A O     1 
ATOM   16409 C  CB    . THR A 1 3612 ? 175.318 169.951 176.502 1.00 50.97  ? 3612 THR A CB    1 
ATOM   16410 O  OG1   . THR A 1 3612 ? 176.506 170.295 177.223 1.00 60.56  ? 3612 THR A OG1   1 
ATOM   16411 C  CG2   . THR A 1 3612 ? 175.632 168.740 175.639 1.00 59.02  ? 3612 THR A CG2   1 
ATOM   16412 N  N     . SER A 1 3613 ? 173.312 170.052 174.155 1.00 52.95  ? 3613 SER A N     1 
ATOM   16413 C  CA    . SER A 1 3613 ? 172.009 169.728 173.597 1.00 50.58  ? 3613 SER A CA    1 
ATOM   16414 C  C     . SER A 1 3613 ? 171.801 168.222 173.634 1.00 53.94  ? 3613 SER A C     1 
ATOM   16415 O  O     . SER A 1 3613 ? 172.760 167.448 173.599 1.00 60.60  ? 3613 SER A O     1 
ATOM   16416 C  CB    . SER A 1 3613 ? 171.875 170.241 172.158 1.00 54.98  ? 3613 SER A CB    1 
ATOM   16417 O  OG    . SER A 1 3613 ? 170.620 169.890 171.605 1.00 59.63  ? 3613 SER A OG    1 
ATOM   16418 N  N     . PHE A 1 3614 ? 170.533 167.811 173.719 1.00 54.03  ? 3614 PHE A N     1 
ATOM   16419 C  CA    . PHE A 1 3614 ? 170.222 166.388 173.638 1.00 58.19  ? 3614 PHE A CA    1 
ATOM   16420 C  C     . PHE A 1 3614 ? 170.519 165.829 172.254 1.00 65.36  ? 3614 PHE A C     1 
ATOM   16421 O  O     . PHE A 1 3614 ? 170.830 164.640 172.121 1.00 68.50  ? 3614 PHE A O     1 
ATOM   16422 C  CB    . PHE A 1 3614 ? 168.759 166.134 174.002 1.00 54.95  ? 3614 PHE A CB    1 
ATOM   16423 C  CG    . PHE A 1 3614 ? 168.502 166.065 175.478 1.00 54.54  ? 3614 PHE A CG    1 
ATOM   16424 C  CD1   . PHE A 1 3614 ? 168.844 164.936 176.199 1.00 58.61  ? 3614 PHE A CD1   1 
ATOM   16425 C  CD2   . PHE A 1 3614 ? 167.902 167.117 176.142 1.00 55.39  ? 3614 PHE A CD2   1 
ATOM   16426 C  CE1   . PHE A 1 3614 ? 168.606 164.865 177.555 1.00 59.61  ? 3614 PHE A CE1   1 
ATOM   16427 C  CE2   . PHE A 1 3614 ? 167.659 167.050 177.498 1.00 55.73  ? 3614 PHE A CE2   1 
ATOM   16428 C  CZ    . PHE A 1 3614 ? 168.013 165.923 178.204 1.00 53.99  ? 3614 PHE A CZ    1 
ATOM   16429 N  N     . LEU A 1 3615 ? 170.424 166.662 171.215 1.00 65.92  ? 3615 LEU A N     1 
ATOM   16430 C  CA    . LEU A 1 3615 ? 170.736 166.200 169.867 1.00 64.24  ? 3615 LEU A CA    1 
ATOM   16431 C  C     . LEU A 1 3615 ? 172.228 165.964 169.681 1.00 68.85  ? 3615 LEU A C     1 
ATOM   16432 O  O     . LEU A 1 3615 ? 172.623 165.184 168.807 1.00 76.51  ? 3615 LEU A O     1 
ATOM   16433 C  CB    . LEU A 1 3615 ? 170.226 167.200 168.827 1.00 64.09  ? 3615 LEU A CB    1 
ATOM   16434 C  CG    . LEU A 1 3615 ? 168.759 167.134 168.387 1.00 70.81  ? 3615 LEU A CG    1 
ATOM   16435 C  CD1   . LEU A 1 3615 ? 168.473 165.813 167.688 1.00 71.89  ? 3615 LEU A CD1   1 
ATOM   16436 C  CD2   . LEU A 1 3615 ? 167.794 167.350 169.538 1.00 69.73  ? 3615 LEU A CD2   1 
ATOM   16437 N  N     . ASP A 1 3616 ? 173.068 166.628 170.473 1.00 64.87  ? 3616 ASP A N     1 
ATOM   16438 C  CA    . ASP A 1 3616 ? 174.507 166.426 170.365 1.00 67.13  ? 3616 ASP A CA    1 
ATOM   16439 C  C     . ASP A 1 3616 ? 174.870 164.992 170.721 1.00 75.21  ? 3616 ASP A C     1 
ATOM   16440 O  O     . ASP A 1 3616 ? 174.379 164.439 171.709 1.00 75.51  ? 3616 ASP A O     1 
ATOM   16441 C  CB    . ASP A 1 3616 ? 175.255 167.400 171.276 1.00 62.56  ? 3616 ASP A CB    1 
ATOM   16442 C  CG    . ASP A 1 3616 ? 175.230 168.822 170.756 1.00 70.72  ? 3616 ASP A CG    1 
ATOM   16443 O  OD1   . ASP A 1 3616 ? 175.052 169.006 169.534 1.00 75.95  ? 3616 ASP A OD1   1 
ATOM   16444 O  OD2   . ASP A 1 3616 ? 175.403 169.756 171.566 1.00 71.33  ? 3616 ASP A OD2   1 
ATOM   16445 N  N     . ASP A 1 3617 ? 175.734 164.385 169.904 1.00 82.05  ? 3617 ASP A N     1 
ATOM   16446 C  CA    . ASP A 1 3617 ? 176.194 163.033 170.195 1.00 84.18  ? 3617 ASP A CA    1 
ATOM   16447 C  C     . ASP A 1 3617 ? 177.117 163.007 171.404 1.00 81.47  ? 3617 ASP A C     1 
ATOM   16448 O  O     . ASP A 1 3617 ? 177.177 161.998 172.116 1.00 80.71  ? 3617 ASP A O     1 
ATOM   16449 C  CB    . ASP A 1 3617 ? 176.896 162.442 168.974 1.00 85.76  ? 3617 ASP A CB    1 
ATOM   16450 C  CG    . ASP A 1 3617 ? 175.994 162.379 167.758 1.00 101.23 ? 3617 ASP A CG    1 
ATOM   16451 O  OD1   . ASP A 1 3617 ? 176.302 163.051 166.751 1.00 109.34 ? 3617 ASP A OD1   1 
ATOM   16452 O  OD2   . ASP A 1 3617 ? 174.976 161.658 167.809 1.00 105.45 ? 3617 ASP A OD2   1 
ATOM   16453 N  N     . ALA A 1 3618 ? 177.838 164.098 171.652 1.00 76.25  ? 3618 ALA A N     1 
ATOM   16454 C  CA    . ALA A 1 3618 ? 178.715 164.209 172.808 1.00 73.05  ? 3618 ALA A CA    1 
ATOM   16455 C  C     . ALA A 1 3618 ? 177.987 164.672 174.058 1.00 71.72  ? 3618 ALA A C     1 
ATOM   16456 O  O     . ALA A 1 3618 ? 178.644 165.081 175.021 1.00 70.04  ? 3618 ALA A O     1 
ATOM   16457 C  CB    . ALA A 1 3618 ? 179.876 165.158 172.500 1.00 73.79  ? 3618 ALA A CB    1 
ATOM   16458 N  N     . PHE A 1 3619 ? 176.652 164.613 174.064 1.00 72.65  ? 3619 PHE A N     1 
ATOM   16459 C  CA    . PHE A 1 3619 ? 175.892 165.052 175.230 1.00 68.84  ? 3619 PHE A CA    1 
ATOM   16460 C  C     . PHE A 1 3619 ? 176.276 164.262 176.472 1.00 65.10  ? 3619 PHE A C     1 
ATOM   16461 O  O     . PHE A 1 3619 ? 176.763 164.839 177.454 1.00 63.60  ? 3619 PHE A O     1 
ATOM   16462 C  CB    . PHE A 1 3619 ? 174.393 164.923 174.954 1.00 66.01  ? 3619 PHE A CB    1 
ATOM   16463 C  CG    . PHE A 1 3619 ? 173.553 164.792 176.194 1.00 62.33  ? 3619 PHE A CG    1 
ATOM   16464 C  CD1   . PHE A 1 3619 ? 173.481 165.822 177.117 1.00 61.37  ? 3619 PHE A CD1   1 
ATOM   16465 C  CD2   . PHE A 1 3619 ? 172.836 163.633 176.437 1.00 63.06  ? 3619 PHE A CD2   1 
ATOM   16466 C  CE1   . PHE A 1 3619 ? 172.712 165.696 178.256 1.00 60.82  ? 3619 PHE A CE1   1 
ATOM   16467 C  CE2   . PHE A 1 3619 ? 172.066 163.502 177.574 1.00 63.99  ? 3619 PHE A CE2   1 
ATOM   16468 C  CZ    . PHE A 1 3619 ? 172.003 164.535 178.484 1.00 57.98  ? 3619 PHE A CZ    1 
ATOM   16469 N  N     . ARG A 1 3620 ? 176.095 162.937 176.433 1.00 65.10  ? 3620 ARG A N     1 
ATOM   16470 C  CA    . ARG A 1 3620 ? 176.326 162.109 177.612 1.00 59.35  ? 3620 ARG A CA    1 
ATOM   16471 C  C     . ARG A 1 3620 ? 177.692 162.381 178.223 1.00 60.28  ? 3620 ARG A C     1 
ATOM   16472 O  O     . ARG A 1 3620 ? 177.795 162.641 179.428 1.00 65.22  ? 3620 ARG A O     1 
ATOM   16473 C  CB    . ARG A 1 3620 ? 176.193 160.631 177.250 1.00 62.31  ? 3620 ARG A CB    1 
ATOM   16474 C  CG    . ARG A 1 3620 ? 175.640 159.764 178.365 1.00 72.80  ? 3620 ARG A CG    1 
ATOM   16475 C  CD    . ARG A 1 3620 ? 175.122 158.439 177.831 1.00 79.02  ? 3620 ARG A CD    1 
ATOM   16476 N  NE    . ARG A 1 3620 ? 173.895 158.590 177.059 1.00 87.42  ? 3620 ARG A NE    1 
ATOM   16477 C  CZ    . ARG A 1 3620 ? 173.029 157.612 176.831 1.00 92.05  ? 3620 ARG A CZ    1 
ATOM   16478 N  NH1   . ARG A 1 3620 ? 173.224 156.392 177.304 1.00 96.48  ? 3620 ARG A NH1   1 
ATOM   16479 N  NH2   . ARG A 1 3620 ? 171.941 157.863 176.109 1.00 90.34  ? 3620 ARG A NH2   1 
ATOM   16480 N  N     . LYS A 1 3621 ? 178.741 162.379 177.396 1.00 62.24  ? 3621 LYS A N     1 
ATOM   16481 C  CA    . LYS A 1 3621 ? 180.083 162.650 177.896 1.00 64.88  ? 3621 LYS A CA    1 
ATOM   16482 C  C     . LYS A 1 3621 ? 180.128 163.955 178.677 1.00 59.38  ? 3621 LYS A C     1 
ATOM   16483 O  O     . LYS A 1 3621 ? 180.555 163.968 179.839 1.00 62.27  ? 3621 LYS A O     1 
ATOM   16484 C  CB    . LYS A 1 3621 ? 181.077 162.683 176.736 1.00 67.43  ? 3621 LYS A CB    1 
ATOM   16485 C  CG    . LYS A 1 3621 ? 181.220 161.363 175.998 1.00 65.71  ? 3621 LYS A CG    1 
ATOM   16486 C  CD    . LYS A 1 3621 ? 181.498 160.224 176.962 1.00 71.22  ? 3621 LYS A CD    1 
ATOM   16487 C  CE    . LYS A 1 3621 ? 181.475 158.882 176.254 1.00 75.37  ? 3621 LYS A CE    1 
ATOM   16488 N  NZ    . LYS A 1 3621 ? 181.683 157.756 177.204 1.00 75.16  ? 3621 LYS A NZ    1 
ATOM   16489 N  N     . ASN A 1 3622 ? 179.639 165.049 178.082 1.00 55.67  ? 3622 ASN A N     1 
ATOM   16490 C  CA    . ASN A 1 3622 ? 179.626 166.318 178.803 1.00 54.21  ? 3622 ASN A CA    1 
ATOM   16491 C  C     . ASN A 1 3622 ? 178.863 166.182 180.109 1.00 54.32  ? 3622 ASN A C     1 
ATOM   16492 O  O     . ASN A 1 3622 ? 179.338 166.621 181.164 1.00 56.04  ? 3622 ASN A O     1 
ATOM   16493 C  CB    . ASN A 1 3622 ? 179.017 167.429 177.946 1.00 57.80  ? 3622 ASN A CB    1 
ATOM   16494 C  CG    . ASN A 1 3622 ? 179.747 167.626 176.634 1.00 66.30  ? 3622 ASN A CG    1 
ATOM   16495 O  OD1   . ASN A 1 3622 ? 179.134 167.658 175.569 1.00 60.32  ? 3622 ASN A OD1   1 
ATOM   16496 N  ND2   . ASN A 1 3622 ? 181.065 167.760 176.706 1.00 69.98  ? 3622 ASN A ND2   1 
ATOM   16497 N  N     . LEU A 1 3623 ? 177.702 165.524 180.064 1.00 53.24  ? 3623 LEU A N     1 
ATOM   16498 C  CA    . LEU A 1 3623 ? 176.929 165.315 181.279 1.00 50.69  ? 3623 LEU A CA    1 
ATOM   16499 C  C     . LEU A 1 3623 ? 177.770 164.620 182.339 1.00 50.84  ? 3623 LEU A C     1 
ATOM   16500 O  O     . LEU A 1 3623 ? 177.816 165.067 183.492 1.00 51.45  ? 3623 LEU A O     1 
ATOM   16501 C  CB    . LEU A 1 3623 ? 175.669 164.513 180.963 1.00 51.77  ? 3623 LEU A CB    1 
ATOM   16502 C  CG    . LEU A 1 3623 ? 174.868 163.946 182.131 1.00 52.70  ? 3623 LEU A CG    1 
ATOM   16503 C  CD1   . LEU A 1 3623 ? 174.287 165.060 182.982 1.00 46.78  ? 3623 LEU A CD1   1 
ATOM   16504 C  CD2   . LEU A 1 3623 ? 173.767 163.056 181.596 1.00 52.23  ? 3623 LEU A CD2   1 
ATOM   16505 N  N     . GLU A 1 3624 ? 178.497 163.565 181.949 1.00 53.56  ? 3624 GLU A N     1 
ATOM   16506 C  CA    . GLU A 1 3624 ? 179.360 162.883 182.907 1.00 48.73  ? 3624 GLU A CA    1 
ATOM   16507 C  C     . GLU A 1 3624 ? 180.318 163.866 183.557 1.00 50.08  ? 3624 GLU A C     1 
ATOM   16508 O  O     . GLU A 1 3624 ? 180.434 163.909 184.788 1.00 56.50  ? 3624 GLU A O     1 
ATOM   16509 C  CB    . GLU A 1 3624 ? 180.137 161.756 182.227 1.00 54.45  ? 3624 GLU A CB    1 
ATOM   16510 C  CG    . GLU A 1 3624 ? 179.281 160.764 181.467 1.00 68.47  ? 3624 GLU A CG    1 
ATOM   16511 C  CD    . GLU A 1 3624 ? 180.073 159.571 180.974 1.00 84.21  ? 3624 GLU A CD    1 
ATOM   16512 O  OE1   . GLU A 1 3624 ? 181.239 159.415 181.397 1.00 84.12  ? 3624 GLU A OE1   1 
ATOM   16513 O  OE2   . GLU A 1 3624 ? 179.532 158.788 180.165 1.00 88.23  ? 3624 GLU A OE2   1 
ATOM   16514 N  N     . SER A 1 3625 ? 180.968 164.706 182.746 1.00 48.81  ? 3625 SER A N     1 
ATOM   16515 C  CA    . SER A 1 3625 ? 181.877 165.697 183.304 1.00 47.68  ? 3625 SER A CA    1 
ATOM   16516 C  C     . SER A 1 3625 ? 181.154 166.583 184.306 1.00 53.11  ? 3625 SER A C     1 
ATOM   16517 O  O     . SER A 1 3625 ? 181.630 166.778 185.431 1.00 55.22  ? 3625 SER A O     1 
ATOM   16518 C  CB    . SER A 1 3625 ? 182.494 166.533 182.184 1.00 49.11  ? 3625 SER A CB    1 
ATOM   16519 O  OG    . SER A 1 3625 ? 181.512 167.319 181.535 1.00 62.13  ? 3625 SER A OG    1 
ATOM   16520 N  N     . ALA A 1 3626 ? 179.966 167.069 183.938 1.00 51.07  ? 3626 ALA A N     1 
ATOM   16521 C  CA    . ALA A 1 3626 ? 179.205 167.915 184.848 1.00 47.47  ? 3626 ALA A CA    1 
ATOM   16522 C  C     . ALA A 1 3626 ? 178.890 167.168 186.134 1.00 51.71  ? 3626 ALA A C     1 
ATOM   16523 O  O     . ALA A 1 3626 ? 178.939 167.741 187.228 1.00 55.56  ? 3626 ALA A O     1 
ATOM   16524 C  CB    . ALA A 1 3626 ? 177.925 168.398 184.170 1.00 43.15  ? 3626 ALA A CB    1 
ATOM   16525 N  N     . LEU A 1 3627 ? 178.583 165.874 186.023 1.00 47.61  ? 3627 LEU A N     1 
ATOM   16526 C  CA    . LEU A 1 3627 ? 178.281 165.093 187.216 1.00 40.16  ? 3627 LEU A CA    1 
ATOM   16527 C  C     . LEU A 1 3627 ? 179.528 164.877 188.059 1.00 48.09  ? 3627 LEU A C     1 
ATOM   16528 O  O     . LEU A 1 3627 ? 179.448 164.801 189.290 1.00 53.00  ? 3627 LEU A O     1 
ATOM   16529 C  CB    . LEU A 1 3627 ? 177.660 163.754 186.825 1.00 41.10  ? 3627 LEU A CB    1 
ATOM   16530 C  CG    . LEU A 1 3627 ? 176.155 163.749 186.568 1.00 38.58  ? 3627 LEU A CG    1 
ATOM   16531 C  CD1   . LEU A 1 3627 ? 175.743 162.476 185.859 1.00 46.84  ? 3627 LEU A CD1   1 
ATOM   16532 C  CD2   . LEU A 1 3627 ? 175.405 163.893 187.876 1.00 39.52  ? 3627 LEU A CD2   1 
ATOM   16533 N  N     . ARG A 1 3628 ? 180.693 164.788 187.417 1.00 50.94  ? 3628 ARG A N     1 
ATOM   16534 C  CA    . ARG A 1 3628 ? 181.885 164.361 188.139 1.00 50.20  ? 3628 ARG A CA    1 
ATOM   16535 C  C     . ARG A 1 3628 ? 182.683 165.546 188.666 1.00 53.74  ? 3628 ARG A C     1 
ATOM   16536 O  O     . ARG A 1 3628 ? 183.188 165.504 189.793 1.00 57.78  ? 3628 ARG A O     1 
ATOM   16537 C  CB    . ARG A 1 3628 ? 182.753 163.488 187.236 1.00 48.76  ? 3628 ARG A CB    1 
ATOM   16538 C  CG    . ARG A 1 3628 ? 183.874 162.772 187.959 1.00 63.35  ? 3628 ARG A CG    1 
ATOM   16539 C  CD    . ARG A 1 3628 ? 184.255 161.494 187.238 1.00 65.33  ? 3628 ARG A CD    1 
ATOM   16540 N  NE    . ARG A 1 3628 ? 184.250 161.666 185.791 1.00 59.77  ? 3628 ARG A NE    1 
ATOM   16541 C  CZ    . ARG A 1 3628 ? 183.967 160.703 184.926 1.00 65.91  ? 3628 ARG A CZ    1 
ATOM   16542 N  NH1   . ARG A 1 3628 ? 183.666 159.480 185.329 1.00 67.93  ? 3628 ARG A NH1   1 
ATOM   16543 N  NH2   . ARG A 1 3628 ? 183.988 160.974 183.624 1.00 65.30  ? 3628 ARG A NH2   1 
ATOM   16544 N  N     . PHE A 1 3629 ? 182.806 166.604 187.872 1.00 50.88  ? 3629 PHE A N     1 
ATOM   16545 C  CA    . PHE A 1 3629 ? 183.629 167.750 188.223 1.00 50.46  ? 3629 PHE A CA    1 
ATOM   16546 C  C     . PHE A 1 3629 ? 182.837 168.882 188.863 1.00 56.59  ? 3629 PHE A C     1 
ATOM   16547 O  O     . PHE A 1 3629 ? 183.438 169.868 189.299 1.00 63.04  ? 3629 PHE A O     1 
ATOM   16548 C  CB    . PHE A 1 3629 ? 184.363 168.255 186.979 1.00 53.23  ? 3629 PHE A CB    1 
ATOM   16549 C  CG    . PHE A 1 3629 ? 184.997 167.158 186.171 1.00 57.19  ? 3629 PHE A CG    1 
ATOM   16550 C  CD1   . PHE A 1 3629 ? 185.746 166.172 186.786 1.00 53.44  ? 3629 PHE A CD1   1 
ATOM   16551 C  CD2   . PHE A 1 3629 ? 184.828 167.100 184.802 1.00 59.33  ? 3629 PHE A CD2   1 
ATOM   16552 C  CE1   . PHE A 1 3629 ? 186.326 165.161 186.054 1.00 49.93  ? 3629 PHE A CE1   1 
ATOM   16553 C  CE2   . PHE A 1 3629 ? 185.405 166.087 184.064 1.00 58.79  ? 3629 PHE A CE2   1 
ATOM   16554 C  CZ    . PHE A 1 3629 ? 186.154 165.118 184.691 1.00 56.36  ? 3629 PHE A CZ    1 
ATOM   16555 N  N     . GLY A 1 3630 ? 181.515 168.765 188.938 1.00 54.71  ? 3630 GLY A N     1 
ATOM   16556 C  CA    . GLY A 1 3630 ? 180.703 169.763 189.605 1.00 54.09  ? 3630 GLY A CA    1 
ATOM   16557 C  C     . GLY A 1 3630 ? 180.622 171.091 188.882 1.00 54.25  ? 3630 GLY A C     1 
ATOM   16558 O  O     . GLY A 1 3630 ? 181.120 172.105 189.378 1.00 55.22  ? 3630 GLY A O     1 
ATOM   16559 N  N     . ASN A 1 3631 ? 179.996 171.100 187.708 1.00 50.24  ? 3631 ASN A N     1 
ATOM   16560 C  CA    . ASN A 1 3631 ? 179.794 172.324 186.955 1.00 48.65  ? 3631 ASN A CA    1 
ATOM   16561 C  C     . ASN A 1 3631 ? 178.342 172.420 186.512 1.00 48.75  ? 3631 ASN A C     1 
ATOM   16562 O  O     . ASN A 1 3631 ? 177.734 171.405 186.152 1.00 51.19  ? 3631 ASN A O     1 
ATOM   16563 C  CB    . ASN A 1 3631 ? 180.710 172.378 185.723 1.00 54.13  ? 3631 ASN A CB    1 
ATOM   16564 C  CG    . ASN A 1 3631 ? 182.169 172.533 186.088 1.00 59.94  ? 3631 ASN A CG    1 
ATOM   16565 O  OD1   . ASN A 1 3631 ? 183.007 171.722 185.699 1.00 62.45  ? 3631 ASN A OD1   1 
ATOM   16566 N  ND2   . ASN A 1 3631 ? 182.481 173.582 186.838 1.00 56.42  ? 3631 ASN A ND2   1 
ATOM   16567 N  N     . PRO A 1 3632 ? 177.756 173.615 186.539 1.00 45.01  ? 3632 PRO A N     1 
ATOM   16568 C  CA    . PRO A 1 3632 ? 176.401 173.778 186.005 1.00 41.91  ? 3632 PRO A CA    1 
ATOM   16569 C  C     . PRO A 1 3632 ? 176.344 173.435 184.525 1.00 44.17  ? 3632 PRO A C     1 
ATOM   16570 O  O     . PRO A 1 3632 ? 177.262 173.730 183.756 1.00 51.92  ? 3632 PRO A O     1 
ATOM   16571 C  CB    . PRO A 1 3632 ? 176.093 175.259 186.255 1.00 44.31  ? 3632 PRO A CB    1 
ATOM   16572 C  CG    . PRO A 1 3632 ? 177.410 175.894 186.545 1.00 46.14  ? 3632 PRO A CG    1 
ATOM   16573 C  CD    . PRO A 1 3632 ? 178.240 174.841 187.188 1.00 48.87  ? 3632 PRO A CD    1 
ATOM   16574 N  N     . LEU A 1 3633 ? 175.242 172.805 184.131 1.00 37.80  ? 3633 LEU A N     1 
ATOM   16575 C  CA    . LEU A 1 3633 ? 175.065 172.334 182.766 1.00 37.10  ? 3633 LEU A CA    1 
ATOM   16576 C  C     . LEU A 1 3633 ? 173.666 172.697 182.298 1.00 38.36  ? 3633 LEU A C     1 
ATOM   16577 O  O     . LEU A 1 3633 ? 172.689 172.429 183.000 1.00 42.87  ? 3633 LEU A O     1 
ATOM   16578 C  CB    . LEU A 1 3633 ? 175.288 170.819 182.685 1.00 35.87  ? 3633 LEU A CB    1 
ATOM   16579 C  CG    . LEU A 1 3633 ? 175.025 170.096 181.366 1.00 37.89  ? 3633 LEU A CG    1 
ATOM   16580 C  CD1   . LEU A 1 3633 ? 176.143 170.376 180.387 1.00 42.91  ? 3633 LEU A CD1   1 
ATOM   16581 C  CD2   . LEU A 1 3633 ? 174.885 168.606 181.600 1.00 38.56  ? 3633 LEU A CD2   1 
ATOM   16582 N  N     . LEU A 1 3634 ? 173.570 173.308 181.122 1.00 36.48  ? 3634 LEU A N     1 
ATOM   16583 C  CA    . LEU A 1 3634 ? 172.292 173.674 180.522 1.00 35.71  ? 3634 LEU A CA    1 
ATOM   16584 C  C     . LEU A 1 3634 ? 172.095 172.821 179.278 1.00 38.79  ? 3634 LEU A C     1 
ATOM   16585 O  O     . LEU A 1 3634 ? 172.799 173.003 178.281 1.00 48.18  ? 3634 LEU A O     1 
ATOM   16586 C  CB    . LEU A 1 3634 ? 172.247 175.161 180.178 1.00 38.33  ? 3634 LEU A CB    1 
ATOM   16587 C  CG    . LEU A 1 3634 ? 171.082 175.609 179.290 1.00 40.59  ? 3634 LEU A CG    1 
ATOM   16588 C  CD1   . LEU A 1 3634 ? 169.797 175.726 180.086 1.00 40.24  ? 3634 LEU A CD1   1 
ATOM   16589 C  CD2   . LEU A 1 3634 ? 171.399 176.920 178.603 1.00 50.81  ? 3634 LEU A CD2   1 
ATOM   16590 N  N     . VAL A 1 3635 ? 171.138 171.900 179.331 1.00 33.35  ? 3635 VAL A N     1 
ATOM   16591 C  CA    . VAL A 1 3635 ? 170.872 170.979 178.232 1.00 35.35  ? 3635 VAL A CA    1 
ATOM   16592 C  C     . VAL A 1 3635 ? 169.609 171.441 177.523 1.00 38.44  ? 3635 VAL A C     1 
ATOM   16593 O  O     . VAL A 1 3635 ? 168.530 171.492 178.126 1.00 47.80  ? 3635 VAL A O     1 
ATOM   16594 C  CB    . VAL A 1 3635 ? 170.732 169.532 178.722 1.00 38.19  ? 3635 VAL A CB    1 
ATOM   16595 C  CG1   . VAL A 1 3635 ? 170.771 168.583 177.547 1.00 44.83  ? 3635 VAL A CG1   1 
ATOM   16596 C  CG2   . VAL A 1 3635 ? 171.832 169.200 179.704 1.00 44.94  ? 3635 VAL A CG2   1 
ATOM   16597 N  N     . GLN A 1 3636 ? 169.744 171.768 176.245 1.00 41.26  ? 3636 GLN A N     1 
ATOM   16598 C  CA    . GLN A 1 3636 ? 168.648 172.252 175.426 1.00 45.74  ? 3636 GLN A CA    1 
ATOM   16599 C  C     . GLN A 1 3636 ? 168.019 171.089 174.665 1.00 50.79  ? 3636 GLN A C     1 
ATOM   16600 O  O     . GLN A 1 3636 ? 168.454 169.940 174.764 1.00 54.11  ? 3636 GLN A O     1 
ATOM   16601 C  CB    . GLN A 1 3636 ? 169.145 173.334 174.468 1.00 47.29  ? 3636 GLN A CB    1 
ATOM   16602 C  CG    . GLN A 1 3636 ? 170.022 174.377 175.132 1.00 53.63  ? 3636 GLN A CG    1 
ATOM   16603 C  CD    . GLN A 1 3636 ? 170.792 175.210 174.132 1.00 64.93  ? 3636 GLN A CD    1 
ATOM   16604 O  OE1   . GLN A 1 3636 ? 170.666 176.433 174.098 1.00 70.94  ? 3636 GLN A OE1   1 
ATOM   16605 N  NE2   . GLN A 1 3636 ? 171.597 174.550 173.309 1.00 64.10  ? 3636 GLN A NE2   1 
ATOM   16606 N  N     . ASP A 1 3637 ? 166.979 171.402 173.891 1.00 51.24  ? 3637 ASP A N     1 
ATOM   16607 C  CA    . ASP A 1 3637 ? 166.271 170.415 173.074 1.00 54.56  ? 3637 ASP A CA    1 
ATOM   16608 C  C     . ASP A 1 3637 ? 165.763 169.251 173.924 1.00 57.74  ? 3637 ASP A C     1 
ATOM   16609 O  O     . ASP A 1 3637 ? 165.940 168.080 173.583 1.00 62.05  ? 3637 ASP A O     1 
ATOM   16610 C  CB    . ASP A 1 3637 ? 167.160 169.912 171.934 1.00 56.49  ? 3637 ASP A CB    1 
ATOM   16611 C  CG    . ASP A 1 3637 ? 167.463 170.987 170.909 1.00 69.91  ? 3637 ASP A CG    1 
ATOM   16612 O  OD1   . ASP A 1 3637 ? 166.573 171.301 170.092 1.00 79.27  ? 3637 ASP A OD1   1 
ATOM   16613 O  OD2   . ASP A 1 3637 ? 168.595 171.515 170.916 1.00 70.81  ? 3637 ASP A OD2   1 
ATOM   16614 N  N     . VAL A 1 3638 ? 165.121 169.582 175.047 1.00 55.81  ? 3638 VAL A N     1 
ATOM   16615 C  CA    . VAL A 1 3638 ? 164.646 168.553 175.965 1.00 50.98  ? 3638 VAL A CA    1 
ATOM   16616 C  C     . VAL A 1 3638 ? 163.408 167.838 175.445 1.00 55.52  ? 3638 VAL A C     1 
ATOM   16617 O  O     . VAL A 1 3638 ? 162.988 166.839 176.036 1.00 57.87  ? 3638 VAL A O     1 
ATOM   16618 C  CB    . VAL A 1 3638 ? 164.364 169.152 177.360 1.00 45.12  ? 3638 VAL A CB    1 
ATOM   16619 C  CG1   . VAL A 1 3638 ? 163.056 169.913 177.364 1.00 48.06  ? 3638 VAL A CG1   1 
ATOM   16620 C  CG2   . VAL A 1 3638 ? 164.385 168.077 178.439 1.00 45.09  ? 3638 VAL A CG2   1 
ATOM   16621 N  N     . GLU A 1 3639 ? 162.810 168.318 174.351 1.00 57.83  ? 3639 GLU A N     1 
ATOM   16622 C  CA    . GLU A 1 3639 ? 161.698 167.585 173.755 1.00 61.91  ? 3639 GLU A CA    1 
ATOM   16623 C  C     . GLU A 1 3639 ? 162.132 166.198 173.303 1.00 67.96  ? 3639 GLU A C     1 
ATOM   16624 O  O     . GLU A 1 3639 ? 161.330 165.257 173.327 1.00 69.23  ? 3639 GLU A O     1 
ATOM   16625 C  CB    . GLU A 1 3639 ? 161.098 168.374 172.589 1.00 63.52  ? 3639 GLU A CB    1 
ATOM   16626 C  CG    . GLU A 1 3639 ? 162.025 168.571 171.404 1.00 69.76  ? 3639 GLU A CG    1 
ATOM   16627 C  CD    . GLU A 1 3639 ? 162.782 169.881 171.469 1.00 77.15  ? 3639 GLU A CD    1 
ATOM   16628 O  OE1   . GLU A 1 3639 ? 162.782 170.515 172.544 1.00 74.06  ? 3639 GLU A OE1   1 
ATOM   16629 O  OE2   . GLU A 1 3639 ? 163.375 170.278 170.445 1.00 80.46  ? 3639 GLU A OE2   1 
ATOM   16630 N  N     . SER A 1 3640 ? 163.387 166.052 172.889 1.00 67.81  ? 3640 SER A N     1 
ATOM   16631 C  CA    . SER A 1 3640 ? 163.995 164.741 172.666 1.00 68.30  ? 3640 SER A CA    1 
ATOM   16632 C  C     . SER A 1 3640 ? 164.740 164.271 173.911 1.00 64.02  ? 3640 SER A C     1 
ATOM   16633 O  O     . SER A 1 3640 ? 165.927 163.952 173.871 1.00 61.72  ? 3640 SER A O     1 
ATOM   16634 C  CB    . SER A 1 3640 ? 164.920 164.795 171.457 1.00 68.77  ? 3640 SER A CB    1 
ATOM   16635 O  OG    . SER A 1 3640 ? 165.955 165.740 171.655 1.00 72.60  ? 3640 SER A OG    1 
ATOM   16636 N  N     . TYR A 1 3641 ? 164.029 164.241 175.036 1.00 61.52  ? 3641 TYR A N     1 
ATOM   16637 C  CA    . TYR A 1 3641 ? 164.638 163.884 176.311 1.00 59.20  ? 3641 TYR A CA    1 
ATOM   16638 C  C     . TYR A 1 3641 ? 165.144 162.449 176.282 1.00 62.96  ? 3641 TYR A C     1 
ATOM   16639 O  O     . TYR A 1 3641 ? 164.457 161.538 175.814 1.00 63.48  ? 3641 TYR A O     1 
ATOM   16640 C  CB    . TYR A 1 3641 ? 163.622 164.064 177.439 1.00 54.73  ? 3641 TYR A CB    1 
ATOM   16641 C  CG    . TYR A 1 3641 ? 164.060 163.514 178.776 1.00 55.28  ? 3641 TYR A CG    1 
ATOM   16642 C  CD1   . TYR A 1 3641 ? 165.124 164.076 179.465 1.00 55.44  ? 3641 TYR A CD1   1 
ATOM   16643 C  CD2   . TYR A 1 3641 ? 163.403 162.437 179.352 1.00 56.47  ? 3641 TYR A CD2   1 
ATOM   16644 C  CE1   . TYR A 1 3641 ? 165.523 163.579 180.687 1.00 52.33  ? 3641 TYR A CE1   1 
ATOM   16645 C  CE2   . TYR A 1 3641 ? 163.796 161.932 180.573 1.00 54.05  ? 3641 TYR A CE2   1 
ATOM   16646 C  CZ    . TYR A 1 3641 ? 164.856 162.507 181.235 1.00 50.47  ? 3641 TYR A CZ    1 
ATOM   16647 O  OH    . TYR A 1 3641 ? 165.249 162.007 182.453 1.00 50.21  ? 3641 TYR A OH    1 
ATOM   16648 N  N     . ASP A 1 3642 ? 166.361 162.250 176.788 1.00 63.63  ? 3642 ASP A N     1 
ATOM   16649 C  CA    . ASP A 1 3642 ? 166.961 160.926 176.829 1.00 66.07  ? 3642 ASP A CA    1 
ATOM   16650 C  C     . ASP A 1 3642 ? 166.745 160.326 178.207 1.00 61.23  ? 3642 ASP A C     1 
ATOM   16651 O  O     . ASP A 1 3642 ? 167.276 160.862 179.192 1.00 61.96  ? 3642 ASP A O     1 
ATOM   16652 C  CB    . ASP A 1 3642 ? 168.449 160.999 176.508 1.00 70.33  ? 3642 ASP A CB    1 
ATOM   16653 C  CG    . ASP A 1 3642 ? 168.961 159.742 175.833 1.00 77.82  ? 3642 ASP A CG    1 
ATOM   16654 O  OD1   . ASP A 1 3642 ? 168.377 159.338 174.806 1.00 79.14  ? 3642 ASP A OD1   1 
ATOM   16655 O  OD2   . ASP A 1 3642 ? 169.951 159.161 176.319 1.00 80.73  ? 3642 ASP A OD2   1 
ATOM   16656 N  N     . PRO A 1 3643 ? 165.982 159.235 178.329 1.00 59.77  ? 3643 PRO A N     1 
ATOM   16657 C  CA    . PRO A 1 3643 ? 165.659 158.695 179.661 1.00 58.05  ? 3643 PRO A CA    1 
ATOM   16658 C  C     . PRO A 1 3643 ? 166.869 158.337 180.513 1.00 59.37  ? 3643 PRO A C     1 
ATOM   16659 O  O     . PRO A 1 3643 ? 166.696 158.091 181.714 1.00 58.66  ? 3643 PRO A O     1 
ATOM   16660 C  CB    . PRO A 1 3643 ? 164.825 157.443 179.352 1.00 58.90  ? 3643 PRO A CB    1 
ATOM   16661 C  CG    . PRO A 1 3643 ? 164.578 157.438 177.879 1.00 66.71  ? 3643 PRO A CG    1 
ATOM   16662 C  CD    . PRO A 1 3643 ? 165.114 158.689 177.275 1.00 63.95  ? 3643 PRO A CD    1 
ATOM   16663 N  N     . VAL A 1 3644 ? 168.078 158.302 179.945 1.00 61.36  ? 3644 VAL A N     1 
ATOM   16664 C  CA    . VAL A 1 3644 ? 169.262 157.983 180.733 1.00 63.63  ? 3644 VAL A CA    1 
ATOM   16665 C  C     . VAL A 1 3644 ? 169.476 159.004 181.842 1.00 56.56  ? 3644 VAL A C     1 
ATOM   16666 O  O     . VAL A 1 3644 ? 170.172 158.721 182.823 1.00 58.77  ? 3644 VAL A O     1 
ATOM   16667 C  CB    . VAL A 1 3644 ? 170.504 157.896 179.825 1.00 70.76  ? 3644 VAL A CB    1 
ATOM   16668 C  CG1   . VAL A 1 3644 ? 170.889 159.273 179.307 1.00 67.59  ? 3644 VAL A CG1   1 
ATOM   16669 C  CG2   . VAL A 1 3644 ? 171.660 157.226 180.544 1.00 75.22  ? 3644 VAL A CG2   1 
ATOM   16670 N  N     . LEU A 1 3645 ? 168.879 160.185 181.715 1.00 53.57  ? 3645 LEU A N     1 
ATOM   16671 C  CA    . LEU A 1 3645 ? 168.985 161.244 182.707 1.00 50.85  ? 3645 LEU A CA    1 
ATOM   16672 C  C     . LEU A 1 3645 ? 168.045 161.040 183.889 1.00 47.37  ? 3645 LEU A C     1 
ATOM   16673 O  O     . LEU A 1 3645 ? 168.089 161.833 184.835 1.00 47.31  ? 3645 LEU A O     1 
ATOM   16674 C  CB    . LEU A 1 3645 ? 168.711 162.594 182.035 1.00 49.91  ? 3645 LEU A CB    1 
ATOM   16675 C  CG    . LEU A 1 3645 ? 169.136 163.896 182.712 1.00 47.69  ? 3645 LEU A CG    1 
ATOM   16676 C  CD1   . LEU A 1 3645 ? 170.606 163.865 183.059 1.00 42.61  ? 3645 LEU A CD1   1 
ATOM   16677 C  CD2   . LEU A 1 3645 ? 168.835 165.070 181.804 1.00 44.31  ? 3645 LEU A CD2   1 
ATOM   16678 N  N     . ASN A 1 3646 ? 167.205 160.001 183.862 1.00 45.69  ? 3646 ASN A N     1 
ATOM   16679 C  CA    . ASN A 1 3646 ? 166.258 159.782 184.955 1.00 43.19  ? 3646 ASN A CA    1 
ATOM   16680 C  C     . ASN A 1 3646 ? 166.928 159.640 186.316 1.00 44.71  ? 3646 ASN A C     1 
ATOM   16681 O  O     . ASN A 1 3646 ? 166.475 160.298 187.268 1.00 50.16  ? 3646 ASN A O     1 
ATOM   16682 C  CB    . ASN A 1 3646 ? 165.378 158.565 184.649 1.00 49.14  ? 3646 ASN A CB    1 
ATOM   16683 C  CG    . ASN A 1 3646 ? 164.375 158.828 183.550 1.00 56.71  ? 3646 ASN A CG    1 
ATOM   16684 O  OD1   . ASN A 1 3646 ? 163.617 159.796 183.601 1.00 56.43  ? 3646 ASN A OD1   1 
ATOM   16685 N  ND2   . ASN A 1 3646 ? 164.345 157.949 182.560 1.00 63.32  ? 3646 ASN A ND2   1 
ATOM   16686 N  N     . PRO A 1 3647 ? 167.968 158.815 186.500 1.00 44.85  ? 3647 PRO A N     1 
ATOM   16687 C  CA    . PRO A 1 3647 ? 168.611 158.770 187.825 1.00 49.37  ? 3647 PRO A CA    1 
ATOM   16688 C  C     . PRO A 1 3647 ? 169.196 160.102 188.257 1.00 52.84  ? 3647 PRO A C     1 
ATOM   16689 O  O     . PRO A 1 3647 ? 169.195 160.413 189.454 1.00 57.90  ? 3647 PRO A O     1 
ATOM   16690 C  CB    . PRO A 1 3647 ? 169.699 157.703 187.648 1.00 50.66  ? 3647 PRO A CB    1 
ATOM   16691 C  CG    . PRO A 1 3647 ? 169.220 156.859 186.533 1.00 48.45  ? 3647 PRO A CG    1 
ATOM   16692 C  CD    . PRO A 1 3647 ? 168.536 157.798 185.596 1.00 47.76  ? 3647 PRO A CD    1 
ATOM   16693 N  N     . VAL A 1 3648 ? 169.701 160.898 187.314 1.00 52.48  ? 3648 VAL A N     1 
ATOM   16694 C  CA    . VAL A 1 3648 ? 170.310 162.177 187.665 1.00 47.11  ? 3648 VAL A CA    1 
ATOM   16695 C  C     . VAL A 1 3648 ? 169.251 163.158 188.151 1.00 48.50  ? 3648 VAL A C     1 
ATOM   16696 O  O     . VAL A 1 3648 ? 169.425 163.831 189.174 1.00 51.67  ? 3648 VAL A O     1 
ATOM   16697 C  CB    . VAL A 1 3648 ? 171.095 162.742 186.470 1.00 47.58  ? 3648 VAL A CB    1 
ATOM   16698 C  CG1   . VAL A 1 3648 ? 171.761 164.051 186.849 1.00 42.14  ? 3648 VAL A CG1   1 
ATOM   16699 C  CG2   . VAL A 1 3648 ? 172.118 161.729 185.985 1.00 50.72  ? 3648 VAL A CG2   1 
ATOM   16700 N  N     . LEU A 1 3649 ? 168.139 163.256 187.423 1.00 44.19  ? 3649 LEU A N     1 
ATOM   16701 C  CA    . LEU A 1 3649 ? 167.087 164.192 187.800 1.00 38.88  ? 3649 LEU A CA    1 
ATOM   16702 C  C     . LEU A 1 3649 ? 166.411 163.772 189.098 1.00 44.97  ? 3649 LEU A C     1 
ATOM   16703 O  O     . LEU A 1 3649 ? 165.999 164.623 189.894 1.00 51.93  ? 3649 LEU A O     1 
ATOM   16704 C  CB    . LEU A 1 3649 ? 166.067 164.306 186.671 1.00 36.29  ? 3649 LEU A CB    1 
ATOM   16705 C  CG    . LEU A 1 3649 ? 166.625 164.833 185.351 1.00 33.08  ? 3649 LEU A CG    1 
ATOM   16706 C  CD1   . LEU A 1 3649 ? 165.534 164.908 184.302 1.00 35.16  ? 3649 LEU A CD1   1 
ATOM   16707 C  CD2   . LEU A 1 3649 ? 167.277 166.187 185.552 1.00 33.54  ? 3649 LEU A CD2   1 
ATOM   16708 N  N     . ASN A 1 3650 ? 166.286 162.467 189.327 1.00 44.27  ? 3650 ASN A N     1 
ATOM   16709 C  CA    . ASN A 1 3650 ? 165.654 161.948 190.532 1.00 43.04  ? 3650 ASN A CA    1 
ATOM   16710 C  C     . ASN A 1 3650 ? 166.611 161.881 191.717 1.00 47.68  ? 3650 ASN A C     1 
ATOM   16711 O  O     . ASN A 1 3650 ? 166.174 161.553 192.825 1.00 48.34  ? 3650 ASN A O     1 
ATOM   16712 C  CB    . ASN A 1 3650 ? 165.071 160.562 190.252 1.00 43.11  ? 3650 ASN A CB    1 
ATOM   16713 C  CG    . ASN A 1 3650 ? 163.980 160.179 191.226 1.00 50.46  ? 3650 ASN A CG    1 
ATOM   16714 O  OD1   . ASN A 1 3650 ? 163.583 160.973 192.076 1.00 54.62  ? 3650 ASN A OD1   1 
ATOM   16715 N  ND2   . ASN A 1 3650 ? 163.486 158.953 191.107 1.00 56.12  ? 3650 ASN A ND2   1 
ATOM   16716 N  N     . ARG A 1 3651 ? 167.892 162.186 191.508 1.00 49.57  ? 3651 ARG A N     1 
ATOM   16717 C  CA    . ARG A 1 3651 ? 168.901 162.177 192.570 1.00 52.67  ? 3651 ARG A CA    1 
ATOM   16718 C  C     . ARG A 1 3651 ? 168.982 160.819 193.262 1.00 60.03  ? 3651 ARG A C     1 
ATOM   16719 O  O     . ARG A 1 3651 ? 169.128 160.728 194.483 1.00 59.65  ? 3651 ARG A O     1 
ATOM   16720 C  CB    . ARG A 1 3651 ? 168.642 163.285 193.592 1.00 54.51  ? 3651 ARG A CB    1 
ATOM   16721 C  CG    . ARG A 1 3651 ? 168.840 164.692 193.066 1.00 52.68  ? 3651 ARG A CG    1 
ATOM   16722 C  CD    . ARG A 1 3651 ? 168.559 165.707 194.158 1.00 55.27  ? 3651 ARG A CD    1 
ATOM   16723 N  NE    . ARG A 1 3651 ? 168.763 167.077 193.707 1.00 58.00  ? 3651 ARG A NE    1 
ATOM   16724 C  CZ    . ARG A 1 3651 ? 167.817 167.834 193.170 1.00 56.33  ? 3651 ARG A CZ    1 
ATOM   16725 N  NH1   . ARG A 1 3651 ? 166.589 167.379 192.986 1.00 52.15  ? 3651 ARG A NH1   1 
ATOM   16726 N  NH2   . ARG A 1 3651 ? 168.110 169.081 192.810 1.00 55.86  ? 3651 ARG A NH2   1 
ATOM   16727 N  N     . GLU A 1 3652 ? 168.888 159.750 192.476 1.00 60.04  ? 3652 GLU A N     1 
ATOM   16728 C  CA    . GLU A 1 3652 ? 169.044 158.399 193.005 1.00 58.92  ? 3652 GLU A CA    1 
ATOM   16729 C  C     . GLU A 1 3652 ? 170.531 158.078 193.084 1.00 63.20  ? 3652 GLU A C     1 
ATOM   16730 O  O     . GLU A 1 3652 ? 171.161 157.765 192.069 1.00 61.01  ? 3652 GLU A O     1 
ATOM   16731 C  CB    . GLU A 1 3652 ? 168.308 157.388 192.132 1.00 56.43  ? 3652 GLU A CB    1 
ATOM   16732 C  CG    . GLU A 1 3652 ? 166.851 157.726 191.878 1.00 61.20  ? 3652 GLU A CG    1 
ATOM   16733 C  CD    . GLU A 1 3652 ? 166.200 156.786 190.883 1.00 69.69  ? 3652 GLU A CD    1 
ATOM   16734 O  OE1   . GLU A 1 3652 ? 166.886 155.864 190.397 1.00 73.81  ? 3652 GLU A OE1   1 
ATOM   16735 O  OE2   . GLU A 1 3652 ? 165.001 156.971 190.585 1.00 65.21  ? 3652 GLU A OE2   1 
ATOM   16736 N  N     . VAL A 1 3653 ? 171.094 158.147 194.288 1.00 62.78  ? 3653 VAL A N     1 
ATOM   16737 C  CA    . VAL A 1 3653 ? 172.520 157.947 194.506 1.00 62.61  ? 3653 VAL A CA    1 
ATOM   16738 C  C     . VAL A 1 3653 ? 172.718 156.734 195.402 1.00 68.17  ? 3653 VAL A C     1 
ATOM   16739 O  O     . VAL A 1 3653 ? 171.884 156.441 196.266 1.00 72.96  ? 3653 VAL A O     1 
ATOM   16740 C  CB    . VAL A 1 3653 ? 173.187 159.195 195.121 1.00 59.13  ? 3653 VAL A CB    1 
ATOM   16741 C  CG1   . VAL A 1 3653 ? 173.061 160.376 194.180 1.00 61.70  ? 3653 VAL A CG1   1 
ATOM   16742 C  CG2   . VAL A 1 3653 ? 172.575 159.520 196.472 1.00 52.81  ? 3653 VAL A CG2   1 
ATOM   16743 N  N     . ARG A 1 3654 ? 173.820 156.023 195.183 1.00 71.29  ? 3654 ARG A N     1 
ATOM   16744 C  CA    . ARG A 1 3654 ? 174.206 154.877 195.994 1.00 71.79  ? 3654 ARG A CA    1 
ATOM   16745 C  C     . ARG A 1 3654 ? 175.583 155.142 196.591 1.00 75.39  ? 3654 ARG A C     1 
ATOM   16746 O  O     . ARG A 1 3654 ? 176.542 155.419 195.862 1.00 81.07  ? 3654 ARG A O     1 
ATOM   16747 C  CB    . ARG A 1 3654 ? 174.162 153.591 195.162 1.00 76.03  ? 3654 ARG A CB    1 
ATOM   16748 C  CG    . ARG A 1 3654 ? 175.152 153.511 194.009 1.00 87.59  ? 3654 ARG A CG    1 
ATOM   16749 C  CD    . ARG A 1 3654 ? 174.985 152.216 193.226 1.00 90.33  ? 3654 ARG A CD    1 
ATOM   16750 N  NE    . ARG A 1 3654 ? 175.336 151.038 194.007 1.00 95.70  ? 3654 ARG A NE    1 
ATOM   16751 C  CZ    . ARG A 1 3654 ? 176.569 150.571 194.137 1.00 99.14  ? 3654 ARG A CZ    1 
ATOM   16752 N  NH1   . ARG A 1 3654 ? 177.594 151.149 193.532 1.00 93.01  ? 3654 ARG A NH1   1 
ATOM   16753 N  NH2   . ARG A 1 3654 ? 176.780 149.494 194.889 1.00 97.83  ? 3654 ARG A NH2   1 
ATOM   16754 N  N     . ARG A 1 3655 ? 175.667 155.097 197.919 1.00 82.87  ? 3655 ARG A N     1 
ATOM   16755 C  CA    . ARG A 1 3655 ? 176.872 155.506 198.640 1.00 90.75  ? 3655 ARG A CA    1 
ATOM   16756 C  C     . ARG A 1 3655 ? 177.732 154.287 198.992 1.00 97.67  ? 3655 ARG A C     1 
ATOM   16757 O  O     . ARG A 1 3655 ? 177.926 153.930 200.154 1.00 98.79  ? 3655 ARG A O     1 
ATOM   16758 C  CB    . ARG A 1 3655 ? 176.490 156.306 199.882 1.00 90.06  ? 3655 ARG A CB    1 
ATOM   16759 C  CG    . ARG A 1 3655 ? 177.665 156.895 200.650 1.00 98.28  ? 3655 ARG A CG    1 
ATOM   16760 C  CD    . ARG A 1 3655 ? 177.195 157.681 201.864 1.00 108.74 ? 3655 ARG A CD    1 
ATOM   16761 N  NE    . ARG A 1 3655 ? 176.592 156.817 202.871 1.00 117.48 ? 3655 ARG A NE    1 
ATOM   16762 C  CZ    . ARG A 1 3655 ? 175.950 157.252 203.947 1.00 113.20 ? 3655 ARG A CZ    1 
ATOM   16763 N  NH1   . ARG A 1 3655 ? 175.796 158.544 204.185 1.00 114.67 ? 3655 ARG A NH1   1 
ATOM   16764 N  NH2   . ARG A 1 3655 ? 175.452 156.368 204.807 1.00 105.35 ? 3655 ARG A NH2   1 
ATOM   16765 N  N     . THR A 1 3656 ? 178.231 153.624 197.953 1.00 93.17  ? 3656 THR A N     1 
ATOM   16766 C  CA    . THR A 1 3656 ? 179.129 152.499 198.165 1.00 96.45  ? 3656 THR A CA    1 
ATOM   16767 C  C     . THR A 1 3656 ? 180.533 152.990 198.506 1.00 100.41 ? 3656 THR A C     1 
ATOM   16768 O  O     . THR A 1 3656 ? 181.019 153.984 197.962 1.00 102.47 ? 3656 THR A O     1 
ATOM   16769 C  CB    . THR A 1 3656 ? 179.160 151.590 196.933 1.00 96.96  ? 3656 THR A CB    1 
ATOM   16770 O  OG1   . THR A 1 3656 ? 179.915 150.409 197.227 1.00 102.74 ? 3656 THR A OG1   1 
ATOM   16771 C  CG2   . THR A 1 3656 ? 179.775 152.300 195.739 1.00 92.73  ? 3656 THR A CG2   1 
ATOM   16772 N  N     . GLY A 1 3657 ? 181.180 152.286 199.429 1.00 96.08  ? 3657 GLY A N     1 
ATOM   16773 C  CA    . GLY A 1 3657 ? 182.493 152.716 199.884 1.00 94.33  ? 3657 GLY A CA    1 
ATOM   16774 C  C     . GLY A 1 3657 ? 182.431 154.099 200.497 1.00 100.09 ? 3657 GLY A C     1 
ATOM   16775 O  O     . GLY A 1 3657 ? 181.576 154.393 201.342 1.00 101.57 ? 3657 GLY A O     1 
ATOM   16776 N  N     . GLY A 1 3658 ? 183.352 154.963 200.079 1.00 98.24  ? 3658 GLY A N     1 
ATOM   16777 C  CA    . GLY A 1 3658 ? 183.337 156.354 200.485 1.00 98.24  ? 3658 GLY A CA    1 
ATOM   16778 C  C     . GLY A 1 3658 ? 183.026 157.273 199.324 1.00 97.66  ? 3658 GLY A C     1 
ATOM   16779 O  O     . GLY A 1 3658 ? 183.241 158.486 199.394 1.00 100.35 ? 3658 GLY A O     1 
ATOM   16780 N  N     . ARG A 1 3659 ? 182.511 156.692 198.247 1.00 93.18  ? 3659 ARG A N     1 
ATOM   16781 C  CA    . ARG A 1 3659 ? 182.234 157.398 197.005 1.00 93.75  ? 3659 ARG A CA    1 
ATOM   16782 C  C     . ARG A 1 3659 ? 180.742 157.344 196.704 1.00 89.30  ? 3659 ARG A C     1 
ATOM   16783 O  O     . ARG A 1 3659 ? 180.112 156.290 196.840 1.00 87.67  ? 3659 ARG A O     1 
ATOM   16784 C  CB    . ARG A 1 3659 ? 183.067 156.802 195.861 1.00 90.76  ? 3659 ARG A CB    1 
ATOM   16785 C  CG    . ARG A 1 3659 ? 182.757 155.344 195.573 1.00 90.11  ? 3659 ARG A CG    1 
ATOM   16786 C  CD    . ARG A 1 3659 ? 183.589 154.751 194.446 1.00 87.45  ? 3659 ARG A CD    1 
ATOM   16787 N  NE    . ARG A 1 3659 ? 183.258 155.341 193.153 1.00 88.58  ? 3659 ARG A NE    1 
ATOM   16788 C  CZ    . ARG A 1 3659 ? 183.997 155.218 192.059 1.00 84.27  ? 3659 ARG A CZ    1 
ATOM   16789 N  NH1   . ARG A 1 3659 ? 185.127 154.532 192.062 1.00 81.95  ? 3659 ARG A NH1   1 
ATOM   16790 N  NH2   . ARG A 1 3659 ? 183.590 155.797 190.933 1.00 85.10  ? 3659 ARG A NH2   1 
ATOM   16791 N  N     . VAL A 1 3660 ? 180.177 158.486 196.324 1.00 84.54  ? 3660 VAL A N     1 
ATOM   16792 C  CA    . VAL A 1 3660 ? 178.752 158.584 196.021 1.00 73.39  ? 3660 VAL A CA    1 
ATOM   16793 C  C     . VAL A 1 3660 ? 178.571 158.423 194.519 1.00 72.12  ? 3660 VAL A C     1 
ATOM   16794 O  O     . VAL A 1 3660 ? 179.172 159.159 193.731 1.00 77.44  ? 3660 VAL A O     1 
ATOM   16795 C  CB    . VAL A 1 3660 ? 178.173 159.920 196.507 1.00 70.29  ? 3660 VAL A CB    1 
ATOM   16796 C  CG1   . VAL A 1 3660 ? 176.725 160.061 196.069 1.00 70.69  ? 3660 VAL A CG1   1 
ATOM   16797 C  CG2   . VAL A 1 3660 ? 178.293 160.035 198.017 1.00 71.03  ? 3660 VAL A CG2   1 
ATOM   16798 N  N     . LEU A 1 3661 ? 177.738 157.469 194.119 1.00 69.58  ? 3661 LEU A N     1 
ATOM   16799 C  CA    . LEU A 1 3661 ? 177.623 157.092 192.719 1.00 69.73  ? 3661 LEU A CA    1 
ATOM   16800 C  C     . LEU A 1 3661 ? 176.248 157.447 192.184 1.00 64.76  ? 3661 LEU A C     1 
ATOM   16801 O  O     . LEU A 1 3661 ? 175.277 157.557 192.936 1.00 69.70  ? 3661 LEU A O     1 
ATOM   16802 C  CB    . LEU A 1 3661 ? 177.851 155.591 192.498 1.00 74.26  ? 3661 LEU A CB    1 
ATOM   16803 C  CG    . LEU A 1 3661 ? 179.291 155.086 192.449 1.00 73.51  ? 3661 LEU A CG    1 
ATOM   16804 C  CD1   . LEU A 1 3661 ? 180.068 155.733 191.321 1.00 73.69  ? 3661 LEU A CD1   1 
ATOM   16805 C  CD2   . LEU A 1 3661 ? 179.963 155.309 193.762 1.00 76.69  ? 3661 LEU A CD2   1 
ATOM   16806 N  N     . ILE A 1 3662 ? 176.181 157.630 190.871 1.00 63.03  ? 3662 ILE A N     1 
ATOM   16807 C  CA    . ILE A 1 3662 ? 174.920 157.732 190.155 1.00 67.29  ? 3662 ILE A CA    1 
ATOM   16808 C  C     . ILE A 1 3662 ? 175.071 156.971 188.844 1.00 69.80  ? 3662 ILE A C     1 
ATOM   16809 O  O     . ILE A 1 3662 ? 176.109 157.054 188.180 1.00 73.51  ? 3662 ILE A O     1 
ATOM   16810 C  CB    . ILE A 1 3662 ? 174.509 159.207 189.938 1.00 65.48  ? 3662 ILE A CB    1 
ATOM   16811 C  CG1   . ILE A 1 3662 ? 173.017 159.310 189.636 1.00 65.87  ? 3662 ILE A CG1   1 
ATOM   16812 C  CG2   . ILE A 1 3662 ? 175.339 159.876 188.851 1.00 59.22  ? 3662 ILE A CG2   1 
ATOM   16813 C  CD1   . ILE A 1 3662 ? 172.451 160.660 189.960 1.00 56.65  ? 3662 ILE A CD1   1 
ATOM   16814 N  N     . THR A 1 3663 ? 174.055 156.189 188.495 1.00 69.12  ? 3663 THR A N     1 
ATOM   16815 C  CA    . THR A 1 3663 ? 174.149 155.277 187.357 1.00 73.30  ? 3663 THR A CA    1 
ATOM   16816 C  C     . THR A 1 3663 ? 173.777 156.029 186.088 1.00 77.39  ? 3663 THR A C     1 
ATOM   16817 O  O     . THR A 1 3663 ? 172.599 156.276 185.822 1.00 80.04  ? 3663 THR A O     1 
ATOM   16818 C  CB    . THR A 1 3663 ? 173.245 154.068 187.562 1.00 78.85  ? 3663 THR A CB    1 
ATOM   16819 O  OG1   . THR A 1 3663 ? 173.641 153.366 188.746 1.00 83.45  ? 3663 THR A OG1   1 
ATOM   16820 C  CG2   . THR A 1 3663 ? 173.338 153.128 186.371 1.00 81.15  ? 3663 THR A CG2   1 
ATOM   16821 N  N     . LEU A 1 3664 ? 174.780 156.401 185.295 1.00 77.35  ? 3664 LEU A N     1 
ATOM   16822 C  CA    . LEU A 1 3664 ? 174.563 157.071 184.018 1.00 77.22  ? 3664 LEU A CA    1 
ATOM   16823 C  C     . LEU A 1 3664 ? 175.012 156.103 182.929 1.00 84.88  ? 3664 LEU A C     1 
ATOM   16824 O  O     . LEU A 1 3664 ? 176.190 155.735 182.856 1.00 89.17  ? 3664 LEU A O     1 
ATOM   16825 C  CB    . LEU A 1 3664 ? 175.322 158.392 183.963 1.00 72.91  ? 3664 LEU A CB    1 
ATOM   16826 C  CG    . LEU A 1 3664 ? 175.213 159.190 182.667 1.00 72.31  ? 3664 LEU A CG    1 
ATOM   16827 C  CD1   . LEU A 1 3664 ? 173.765 159.506 182.361 1.00 67.60  ? 3664 LEU A CD1   1 
ATOM   16828 C  CD2   . LEU A 1 3664 ? 176.016 160.464 182.785 1.00 65.53  ? 3664 LEU A CD2   1 
ATOM   16829 N  N     . GLY A 1 3665 ? 174.073 155.692 182.088 1.00 85.37  ? 3665 GLY A N     1 
ATOM   16830 C  CA    . GLY A 1 3665 ? 174.373 154.682 181.086 1.00 96.42  ? 3665 GLY A CA    1 
ATOM   16831 C  C     . GLY A 1 3665 ? 174.818 153.405 181.754 1.00 101.42 ? 3665 GLY A C     1 
ATOM   16832 O  O     . GLY A 1 3665 ? 174.158 152.906 182.668 1.00 98.51  ? 3665 GLY A O     1 
ATOM   16833 N  N     . ASP A 1 3666 ? 175.944 152.864 181.299 1.00 104.20 ? 3666 ASP A N     1 
ATOM   16834 C  CA    . ASP A 1 3666 ? 176.548 151.694 181.916 1.00 106.02 ? 3666 ASP A CA    1 
ATOM   16835 C  C     . ASP A 1 3666 ? 177.600 152.049 182.955 1.00 101.99 ? 3666 ASP A C     1 
ATOM   16836 O  O     . ASP A 1 3666 ? 178.187 151.144 183.553 1.00 102.04 ? 3666 ASP A O     1 
ATOM   16837 C  CB    . ASP A 1 3666 ? 177.179 150.795 180.851 1.00 110.91 ? 3666 ASP A CB    1 
ATOM   16838 C  CG    . ASP A 1 3666 ? 178.228 151.517 180.022 1.00 110.40 ? 3666 ASP A CG    1 
ATOM   16839 O  OD1   . ASP A 1 3666 ? 178.348 152.754 180.151 1.00 104.08 ? 3666 ASP A OD1   1 
ATOM   16840 O  OD2   . ASP A 1 3666 ? 178.934 150.845 179.241 1.00 116.34 ? 3666 ASP A OD2   1 
ATOM   16841 N  N     . GLN A 1 3667 ? 177.858 153.332 183.182 1.00 96.25  ? 3667 GLN A N     1 
ATOM   16842 C  CA    . GLN A 1 3667 ? 178.965 153.756 184.024 1.00 91.24  ? 3667 GLN A CA    1 
ATOM   16843 C  C     . GLN A 1 3667 ? 178.425 154.456 185.263 1.00 88.96  ? 3667 GLN A C     1 
ATOM   16844 O  O     . GLN A 1 3667 ? 177.437 155.195 185.188 1.00 86.72  ? 3667 GLN A O     1 
ATOM   16845 C  CB    . GLN A 1 3667 ? 179.917 154.671 183.249 1.00 87.51  ? 3667 GLN A CB    1 
ATOM   16846 C  CG    . GLN A 1 3667 ? 181.159 155.086 184.021 1.00 94.76  ? 3667 GLN A CG    1 
ATOM   16847 C  CD    . GLN A 1 3667 ? 182.042 156.035 183.235 1.00 95.62  ? 3667 GLN A CD    1 
ATOM   16848 O  OE1   . GLN A 1 3667 ? 181.728 156.399 182.102 1.00 95.27  ? 3667 GLN A OE1   1 
ATOM   16849 N  NE2   . GLN A 1 3667 ? 183.157 156.437 183.833 1.00 92.16  ? 3667 GLN A NE2   1 
ATOM   16850 N  N     . ASP A 1 3668 ? 179.066 154.212 186.398 1.00 85.40  ? 3668 ASP A N     1 
ATOM   16851 C  CA    . ASP A 1 3668 ? 178.673 154.827 187.658 1.00 79.11  ? 3668 ASP A CA    1 
ATOM   16852 C  C     . ASP A 1 3668 ? 179.547 156.057 187.882 1.00 74.64  ? 3668 ASP A C     1 
ATOM   16853 O  O     . ASP A 1 3668 ? 180.742 155.936 188.172 1.00 75.50  ? 3668 ASP A O     1 
ATOM   16854 C  CB    . ASP A 1 3668 ? 178.797 153.822 188.798 1.00 83.20  ? 3668 ASP A CB    1 
ATOM   16855 C  CG    . ASP A 1 3668 ? 177.908 152.610 188.605 1.00 89.47  ? 3668 ASP A CG    1 
ATOM   16856 O  OD1   . ASP A 1 3668 ? 176.677 152.784 188.499 1.00 91.89  ? 3668 ASP A OD1   1 
ATOM   16857 O  OD2   . ASP A 1 3668 ? 178.441 151.482 188.559 1.00 89.97  ? 3668 ASP A OD2   1 
ATOM   16858 N  N     . ILE A 1 3669 ? 178.952 157.236 187.738 1.00 72.90  ? 3669 ILE A N     1 
ATOM   16859 C  CA    . ILE A 1 3669 ? 179.674 158.500 187.829 1.00 67.19  ? 3669 ILE A CA    1 
ATOM   16860 C  C     . ILE A 1 3669 ? 179.633 158.994 189.267 1.00 67.87  ? 3669 ILE A C     1 
ATOM   16861 O  O     . ILE A 1 3669 ? 178.589 158.935 189.925 1.00 74.85  ? 3669 ILE A O     1 
ATOM   16862 C  CB    . ILE A 1 3669 ? 179.072 159.546 186.876 1.00 60.22  ? 3669 ILE A CB    1 
ATOM   16863 C  CG1   . ILE A 1 3669 ? 178.900 158.961 185.476 1.00 67.63  ? 3669 ILE A CG1   1 
ATOM   16864 C  CG2   . ILE A 1 3669 ? 179.948 160.785 186.825 1.00 58.96  ? 3669 ILE A CG2   1 
ATOM   16865 C  CD1   . ILE A 1 3669 ? 180.190 158.492 184.854 1.00 72.42  ? 3669 ILE A CD1   1 
ATOM   16866 N  N     . ASP A 1 3670 ? 180.771 159.480 189.755 1.00 64.42  ? 3670 ASP A N     1 
ATOM   16867 C  CA    . ASP A 1 3670 ? 180.838 160.070 191.084 1.00 65.28  ? 3670 ASP A CA    1 
ATOM   16868 C  C     . ASP A 1 3670 ? 180.139 161.422 191.095 1.00 66.98  ? 3670 ASP A C     1 
ATOM   16869 O  O     . ASP A 1 3670 ? 180.653 162.394 190.535 1.00 71.76  ? 3670 ASP A O     1 
ATOM   16870 C  CB    . ASP A 1 3670 ? 182.292 160.228 191.522 1.00 69.57  ? 3670 ASP A CB    1 
ATOM   16871 C  CG    . ASP A 1 3670 ? 183.016 158.909 191.613 1.00 82.11  ? 3670 ASP A CG    1 
ATOM   16872 O  OD1   . ASP A 1 3670 ? 182.378 157.902 191.980 1.00 81.43  ? 3670 ASP A OD1   1 
ATOM   16873 O  OD2   . ASP A 1 3670 ? 184.223 158.877 191.301 1.00 89.48  ? 3670 ASP A OD2   1 
ATOM   16874 N  N     . LEU A 1 3671 ? 178.970 161.497 191.724 1.00 63.89  ? 3671 LEU A N     1 
ATOM   16875 C  CA    . LEU A 1 3671 ? 178.230 162.750 191.767 1.00 59.28  ? 3671 LEU A CA    1 
ATOM   16876 C  C     . LEU A 1 3671 ? 178.967 163.755 192.644 1.00 59.51  ? 3671 LEU A C     1 
ATOM   16877 O  O     . LEU A 1 3671 ? 179.456 163.412 193.724 1.00 62.19  ? 3671 LEU A O     1 
ATOM   16878 C  CB    . LEU A 1 3671 ? 176.810 162.507 192.283 1.00 59.48  ? 3671 LEU A CB    1 
ATOM   16879 C  CG    . LEU A 1 3671 ? 175.786 163.647 192.249 1.00 57.52  ? 3671 LEU A CG    1 
ATOM   16880 C  CD1   . LEU A 1 3671 ? 174.389 163.074 192.149 1.00 52.88  ? 3671 LEU A CD1   1 
ATOM   16881 C  CD2   . LEU A 1 3671 ? 175.881 164.528 193.482 1.00 57.94  ? 3671 LEU A CD2   1 
ATOM   16882 N  N     . SER A 1 3672 ? 179.051 165.005 192.168 1.00 54.69  ? 3672 SER A N     1 
ATOM   16883 C  CA    . SER A 1 3672 ? 179.725 166.087 192.865 1.00 54.55  ? 3672 SER A CA    1 
ATOM   16884 C  C     . SER A 1 3672 ? 178.710 167.014 193.525 1.00 60.08  ? 3672 SER A C     1 
ATOM   16885 O  O     . SER A 1 3672 ? 177.617 167.227 192.994 1.00 64.26  ? 3672 SER A O     1 
ATOM   16886 C  CB    . SER A 1 3672 ? 180.595 166.888 191.893 1.00 52.23  ? 3672 SER A CB    1 
ATOM   16887 O  OG    . SER A 1 3672 ? 181.197 167.996 192.533 1.00 62.46  ? 3672 SER A OG    1 
ATOM   16888 N  N     . PRO A 1 3673 ? 179.043 167.572 194.692 1.00 54.45  ? 3673 PRO A N     1 
ATOM   16889 C  CA    . PRO A 1 3673 ? 178.085 168.446 195.388 1.00 55.60  ? 3673 PRO A CA    1 
ATOM   16890 C  C     . PRO A 1 3673 ? 177.707 169.695 194.613 1.00 61.07  ? 3673 PRO A C     1 
ATOM   16891 O  O     . PRO A 1 3673 ? 176.600 170.211 194.807 1.00 61.03  ? 3673 PRO A O     1 
ATOM   16892 C  CB    . PRO A 1 3673 ? 178.815 168.800 196.691 1.00 61.59  ? 3673 PRO A CB    1 
ATOM   16893 C  CG    . PRO A 1 3673 ? 179.839 167.734 196.860 1.00 62.38  ? 3673 PRO A CG    1 
ATOM   16894 C  CD    . PRO A 1 3673 ? 180.268 167.365 195.479 1.00 60.28  ? 3673 PRO A CD    1 
ATOM   16895 N  N     . SER A 1 3674 ? 178.583 170.202 193.744 1.00 56.34  ? 3674 SER A N     1 
ATOM   16896 C  CA    . SER A 1 3674 ? 178.354 171.457 193.041 1.00 50.74  ? 3674 SER A CA    1 
ATOM   16897 C  C     . SER A 1 3674 ? 177.740 171.250 191.661 1.00 50.51  ? 3674 SER A C     1 
ATOM   16898 O  O     . SER A 1 3674 ? 177.958 172.062 190.757 1.00 57.45  ? 3674 SER A O     1 
ATOM   16899 C  CB    . SER A 1 3674 ? 179.659 172.243 192.928 1.00 56.21  ? 3674 SER A CB    1 
ATOM   16900 O  OG    . SER A 1 3674 ? 180.255 172.424 194.199 1.00 61.99  ? 3674 SER A OG    1 
ATOM   16901 N  N     . PHE A 1 3675 ? 176.971 170.181 191.483 1.00 49.29  ? 3675 PHE A N     1 
ATOM   16902 C  CA    . PHE A 1 3675 ? 176.336 169.896 190.206 1.00 44.13  ? 3675 PHE A CA    1 
ATOM   16903 C  C     . PHE A 1 3675 ? 174.918 170.447 190.171 1.00 47.79  ? 3675 PHE A C     1 
ATOM   16904 O  O     . PHE A 1 3675 ? 174.159 170.311 191.135 1.00 57.43  ? 3675 PHE A O     1 
ATOM   16905 C  CB    . PHE A 1 3675 ? 176.309 168.392 189.938 1.00 39.23  ? 3675 PHE A CB    1 
ATOM   16906 C  CG    . PHE A 1 3675 ? 175.481 168.006 188.748 1.00 37.06  ? 3675 PHE A CG    1 
ATOM   16907 C  CD1   . PHE A 1 3675 ? 175.907 168.300 187.467 1.00 40.59  ? 3675 PHE A CD1   1 
ATOM   16908 C  CD2   . PHE A 1 3675 ? 174.274 167.355 188.912 1.00 34.84  ? 3675 PHE A CD2   1 
ATOM   16909 C  CE1   . PHE A 1 3675 ? 175.147 167.948 186.372 1.00 37.40  ? 3675 PHE A CE1   1 
ATOM   16910 C  CE2   . PHE A 1 3675 ? 173.511 167.003 187.821 1.00 34.12  ? 3675 PHE A CE2   1 
ATOM   16911 C  CZ    . PHE A 1 3675 ? 173.948 167.299 186.550 1.00 34.63  ? 3675 PHE A CZ    1 
ATOM   16912 N  N     . VAL A 1 3676 ? 174.569 171.071 189.051 1.00 40.77  ? 3676 VAL A N     1 
ATOM   16913 C  CA    . VAL A 1 3676 ? 173.208 171.528 188.795 1.00 37.47  ? 3676 VAL A CA    1 
ATOM   16914 C  C     . VAL A 1 3676 ? 172.985 171.508 187.290 1.00 36.69  ? 3676 VAL A C     1 
ATOM   16915 O  O     . VAL A 1 3676 ? 173.871 171.876 186.515 1.00 41.30  ? 3676 VAL A O     1 
ATOM   16916 C  CB    . VAL A 1 3676 ? 172.955 172.925 189.404 1.00 39.96  ? 3676 VAL A CB    1 
ATOM   16917 C  CG1   . VAL A 1 3676 ? 173.938 173.941 188.857 1.00 47.06  ? 3676 VAL A CG1   1 
ATOM   16918 C  CG2   . VAL A 1 3676 ? 171.528 173.369 189.146 1.00 39.15  ? 3676 VAL A CG2   1 
ATOM   16919 N  N     . ILE A 1 3677 ? 171.808 171.051 186.875 1.00 32.33  ? 3677 ILE A N     1 
ATOM   16920 C  CA    . ILE A 1 3677 ? 171.481 170.908 185.463 1.00 32.28  ? 3677 ILE A CA    1 
ATOM   16921 C  C     . ILE A 1 3677 ? 170.175 171.638 185.182 1.00 32.31  ? 3677 ILE A C     1 
ATOM   16922 O  O     . ILE A 1 3677 ? 169.223 171.558 185.965 1.00 35.16  ? 3677 ILE A O     1 
ATOM   16923 C  CB    . ILE A 1 3677 ? 171.397 169.424 185.041 1.00 30.33  ? 3677 ILE A CB    1 
ATOM   16924 C  CG1   . ILE A 1 3677 ? 171.043 169.301 183.560 1.00 29.73  ? 3677 ILE A CG1   1 
ATOM   16925 C  CG2   . ILE A 1 3677 ? 170.405 168.662 185.901 1.00 34.67  ? 3677 ILE A CG2   1 
ATOM   16926 C  CD1   . ILE A 1 3677 ? 170.977 167.879 183.072 1.00 31.98  ? 3677 ILE A CD1   1 
ATOM   16927 N  N     . PHE A 1 3678 ? 170.144 172.375 184.074 1.00 30.93  ? 3678 PHE A N     1 
ATOM   16928 C  CA    . PHE A 1 3678 ? 168.969 173.124 183.642 1.00 26.82  ? 3678 PHE A CA    1 
ATOM   16929 C  C     . PHE A 1 3678 ? 168.508 172.559 182.307 1.00 30.21  ? 3678 PHE A C     1 
ATOM   16930 O  O     . PHE A 1 3678 ? 169.158 172.779 181.280 1.00 37.74  ? 3678 PHE A O     1 
ATOM   16931 C  CB    . PHE A 1 3678 ? 169.279 174.615 183.513 1.00 27.26  ? 3678 PHE A CB    1 
ATOM   16932 C  CG    . PHE A 1 3678 ? 169.715 175.260 184.793 1.00 29.87  ? 3678 PHE A CG    1 
ATOM   16933 C  CD1   . PHE A 1 3678 ? 171.049 175.272 185.158 1.00 33.52  ? 3678 PHE A CD1   1 
ATOM   16934 C  CD2   . PHE A 1 3678 ? 168.793 175.867 185.624 1.00 27.91  ? 3678 PHE A CD2   1 
ATOM   16935 C  CE1   . PHE A 1 3678 ? 171.451 175.866 186.332 1.00 38.26  ? 3678 PHE A CE1   1 
ATOM   16936 C  CE2   . PHE A 1 3678 ? 169.189 176.463 186.798 1.00 32.38  ? 3678 PHE A CE2   1 
ATOM   16937 C  CZ    . PHE A 1 3678 ? 170.519 176.463 187.153 1.00 40.03  ? 3678 PHE A CZ    1 
ATOM   16938 N  N     . LEU A 1 3679 ? 167.400 171.828 182.317 1.00 27.69  ? 3679 LEU A N     1 
ATOM   16939 C  CA    . LEU A 1 3679 ? 166.804 171.387 181.067 1.00 28.37  ? 3679 LEU A CA    1 
ATOM   16940 C  C     . LEU A 1 3679 ? 166.097 172.553 180.389 1.00 32.72  ? 3679 LEU A C     1 
ATOM   16941 O  O     . LEU A 1 3679 ? 165.571 173.453 181.046 1.00 39.37  ? 3679 LEU A O     1 
ATOM   16942 C  CB    . LEU A 1 3679 ? 165.827 170.240 181.313 1.00 30.98  ? 3679 LEU A CB    1 
ATOM   16943 C  CG    . LEU A 1 3679 ? 166.412 169.001 181.989 1.00 28.29  ? 3679 LEU A CG    1 
ATOM   16944 C  CD1   . LEU A 1 3679 ? 165.392 167.883 182.012 1.00 35.30  ? 3679 LEU A CD1   1 
ATOM   16945 C  CD2   . LEU A 1 3679 ? 167.676 168.555 181.282 1.00 34.58  ? 3679 LEU A CD2   1 
ATOM   16946 N  N     . SER A 1 3680 ? 166.093 172.539 179.059 1.00 33.61  ? 3680 SER A N     1 
ATOM   16947 C  CA    . SER A 1 3680 ? 165.542 173.656 178.309 1.00 34.30  ? 3680 SER A CA    1 
ATOM   16948 C  C     . SER A 1 3680 ? 164.947 173.162 177.001 1.00 40.32  ? 3680 SER A C     1 
ATOM   16949 O  O     . SER A 1 3680 ? 165.357 172.132 176.463 1.00 51.83  ? 3680 SER A O     1 
ATOM   16950 C  CB    . SER A 1 3680 ? 166.609 174.719 178.029 1.00 40.18  ? 3680 SER A CB    1 
ATOM   16951 O  OG    . SER A 1 3680 ? 166.121 175.697 177.130 1.00 51.70  ? 3680 SER A OG    1 
ATOM   16952 N  N     . THR A 1 3681 ? 163.972 173.915 176.495 1.00 39.02  ? 3681 THR A N     1 
ATOM   16953 C  CA    . THR A 1 3681 ? 163.382 173.650 175.192 1.00 47.80  ? 3681 THR A CA    1 
ATOM   16954 C  C     . THR A 1 3681 ? 162.858 174.956 174.618 1.00 55.69  ? 3681 THR A C     1 
ATOM   16955 O  O     . THR A 1 3681 ? 162.552 175.896 175.356 1.00 54.85  ? 3681 THR A O     1 
ATOM   16956 C  CB    . THR A 1 3681 ? 162.250 172.618 175.266 1.00 49.89  ? 3681 THR A CB    1 
ATOM   16957 O  OG1   . THR A 1 3681 ? 161.798 172.303 173.944 1.00 58.39  ? 3681 THR A OG1   1 
ATOM   16958 C  CG2   . THR A 1 3681 ? 161.087 173.154 176.077 1.00 51.08  ? 3681 THR A CG2   1 
ATOM   16959 N  N     . ARG A 1 3682 ? 162.764 175.008 173.291 1.00 60.08  ? 3682 ARG A N     1 
ATOM   16960 C  CA    . ARG A 1 3682 ? 162.235 176.170 172.591 1.00 55.75  ? 3682 ARG A CA    1 
ATOM   16961 C  C     . ARG A 1 3682 ? 160.864 175.908 171.988 1.00 61.08  ? 3682 ARG A C     1 
ATOM   16962 O  O     . ARG A 1 3682 ? 160.347 176.755 171.253 1.00 68.54  ? 3682 ARG A O     1 
ATOM   16963 C  CB    . ARG A 1 3682 ? 163.211 176.626 171.505 1.00 61.67  ? 3682 ARG A CB    1 
ATOM   16964 C  CG    . ARG A 1 3682 ? 164.320 177.528 172.015 1.00 67.02  ? 3682 ARG A CG    1 
ATOM   16965 C  CD    . ARG A 1 3682 ? 165.359 177.787 170.940 1.00 64.84  ? 3682 ARG A CD    1 
ATOM   16966 N  NE    . ARG A 1 3682 ? 166.066 179.044 171.156 1.00 65.52  ? 3682 ARG A NE    1 
ATOM   16967 C  CZ    . ARG A 1 3682 ? 165.769 180.184 170.548 1.00 72.93  ? 3682 ARG A CZ    1 
ATOM   16968 N  NH1   . ARG A 1 3682 ? 164.774 180.266 169.681 1.00 72.72  ? 3682 ARG A NH1   1 
ATOM   16969 N  NH2   . ARG A 1 3682 ? 166.488 181.269 170.818 1.00 78.75  ? 3682 ARG A NH2   1 
ATOM   16970 N  N     . ASP A 1 3683 ? 160.261 174.758 172.283 1.00 62.38  ? 3683 ASP A N     1 
ATOM   16971 C  CA    . ASP A 1 3683 ? 158.968 174.398 171.727 1.00 63.33  ? 3683 ASP A CA    1 
ATOM   16972 C  C     . ASP A 1 3683 ? 157.891 174.634 172.772 1.00 65.80  ? 3683 ASP A C     1 
ATOM   16973 O  O     . ASP A 1 3683 ? 157.867 173.926 173.790 1.00 69.72  ? 3683 ASP A O     1 
ATOM   16974 C  CB    . ASP A 1 3683 ? 158.969 172.937 171.283 1.00 66.80  ? 3683 ASP A CB    1 
ATOM   16975 C  CG    . ASP A 1 3683 ? 158.114 172.699 170.057 1.00 76.93  ? 3683 ASP A CG    1 
ATOM   16976 O  OD1   . ASP A 1 3683 ? 157.151 173.464 169.843 1.00 77.17  ? 3683 ASP A OD1   1 
ATOM   16977 O  OD2   . ASP A 1 3683 ? 158.406 171.745 169.307 1.00 83.87  ? 3683 ASP A OD2   1 
ATOM   16978 N  N     . PRO A 1 3684 ? 156.994 175.606 172.585 1.00 69.93  ? 3684 PRO A N     1 
ATOM   16979 C  CA    . PRO A 1 3684 ? 155.927 175.797 173.580 1.00 71.45  ? 3684 PRO A CA    1 
ATOM   16980 C  C     . PRO A 1 3684 ? 154.928 174.656 173.608 1.00 73.61  ? 3684 PRO A C     1 
ATOM   16981 O  O     . PRO A 1 3684 ? 154.455 174.278 174.687 1.00 71.53  ? 3684 PRO A O     1 
ATOM   16982 C  CB    . PRO A 1 3684 ? 155.278 177.117 173.142 1.00 69.73  ? 3684 PRO A CB    1 
ATOM   16983 C  CG    . PRO A 1 3684 ? 155.566 177.207 171.684 1.00 68.58  ? 3684 PRO A CG    1 
ATOM   16984 C  CD    . PRO A 1 3684 ? 156.918 176.588 171.491 1.00 71.04  ? 3684 PRO A CD    1 
ATOM   16985 N  N     . THR A 1 3685 ? 154.590 174.094 172.447 1.00 74.26  ? 3685 THR A N     1 
ATOM   16986 C  CA    . THR A 1 3685 ? 153.600 173.021 172.355 1.00 71.72  ? 3685 THR A CA    1 
ATOM   16987 C  C     . THR A 1 3685 ? 154.330 171.682 172.355 1.00 77.23  ? 3685 THR A C     1 
ATOM   16988 O  O     . THR A 1 3685 ? 154.533 171.042 171.322 1.00 80.13  ? 3685 THR A O     1 
ATOM   16989 C  CB    . THR A 1 3685 ? 152.738 173.191 171.111 1.00 73.71  ? 3685 THR A CB    1 
ATOM   16990 O  OG1   . THR A 1 3685 ? 153.578 173.257 169.953 1.00 77.73  ? 3685 THR A OG1   1 
ATOM   16991 C  CG2   . THR A 1 3685 ? 151.917 174.467 171.205 1.00 76.05  ? 3685 THR A CG2   1 
ATOM   16992 N  N     . VAL A 1 3686 ? 154.731 171.256 173.549 1.00 76.33  ? 3686 VAL A N     1 
ATOM   16993 C  CA    . VAL A 1 3686 ? 155.440 169.996 173.733 1.00 72.04  ? 3686 VAL A CA    1 
ATOM   16994 C  C     . VAL A 1 3686 ? 154.824 169.260 174.915 1.00 73.12  ? 3686 VAL A C     1 
ATOM   16995 O  O     . VAL A 1 3686 ? 154.464 169.873 175.926 1.00 77.67  ? 3686 VAL A O     1 
ATOM   16996 C  CB    . VAL A 1 3686 ? 156.956 170.221 173.935 1.00 66.98  ? 3686 VAL A CB    1 
ATOM   16997 C  CG1   . VAL A 1 3686 ? 157.222 171.055 175.177 1.00 65.34  ? 3686 VAL A CG1   1 
ATOM   16998 C  CG2   . VAL A 1 3686 ? 157.690 168.893 174.006 1.00 64.09  ? 3686 VAL A CG2   1 
ATOM   16999 N  N     . GLU A 1 3687 ? 154.677 167.947 174.773 1.00 74.30  ? 3687 GLU A N     1 
ATOM   17000 C  CA    . GLU A 1 3687 ? 154.138 167.092 175.820 1.00 68.31  ? 3687 GLU A CA    1 
ATOM   17001 C  C     . GLU A 1 3687 ? 155.248 166.207 176.364 1.00 65.63  ? 3687 GLU A C     1 
ATOM   17002 O  O     . GLU A 1 3687 ? 156.001 165.603 175.593 1.00 66.06  ? 3687 GLU A O     1 
ATOM   17003 C  CB    . GLU A 1 3687 ? 152.987 166.233 175.293 1.00 73.53  ? 3687 GLU A CB    1 
ATOM   17004 C  CG    . GLU A 1 3687 ? 151.620 166.879 175.424 1.00 86.23  ? 3687 GLU A CG    1 
ATOM   17005 C  CD    . GLU A 1 3687 ? 150.687 166.502 174.290 1.00 95.75  ? 3687 GLU A CD    1 
ATOM   17006 O  OE1   . GLU A 1 3687 ? 151.119 165.755 173.387 1.00 97.61  ? 3687 GLU A OE1   1 
ATOM   17007 O  OE2   . GLU A 1 3687 ? 149.522 166.950 174.304 1.00 92.64  ? 3687 GLU A OE2   1 
ATOM   17008 N  N     . PHE A 1 3688 ? 155.347 166.135 177.684 1.00 66.90  ? 3688 PHE A N     1 
ATOM   17009 C  CA    . PHE A 1 3688 ? 156.368 165.340 178.336 1.00 59.84  ? 3688 PHE A CA    1 
ATOM   17010 C  C     . PHE A 1 3688 ? 155.734 164.189 179.108 1.00 58.49  ? 3688 PHE A C     1 
ATOM   17011 O  O     . PHE A 1 3688 ? 154.607 164.309 179.598 1.00 59.69  ? 3688 PHE A O     1 
ATOM   17012 C  CB    . PHE A 1 3688 ? 157.201 166.200 179.294 1.00 51.35  ? 3688 PHE A CB    1 
ATOM   17013 C  CG    . PHE A 1 3688 ? 157.982 167.281 178.609 1.00 52.31  ? 3688 PHE A CG    1 
ATOM   17014 C  CD1   . PHE A 1 3688 ? 158.964 166.966 177.687 1.00 50.78  ? 3688 PHE A CD1   1 
ATOM   17015 C  CD2   . PHE A 1 3688 ? 157.726 168.613 178.876 1.00 53.71  ? 3688 PHE A CD2   1 
ATOM   17016 C  CE1   . PHE A 1 3688 ? 159.682 167.958 177.054 1.00 53.16  ? 3688 PHE A CE1   1 
ATOM   17017 C  CE2   . PHE A 1 3688 ? 158.439 169.609 178.244 1.00 50.73  ? 3688 PHE A CE2   1 
ATOM   17018 C  CZ    . PHE A 1 3688 ? 159.419 169.281 177.333 1.00 50.92  ? 3688 PHE A CZ    1 
ATOM   17019 N  N     . PRO A 1 3689 ? 156.428 163.054 179.225 1.00 55.63  ? 3689 PRO A N     1 
ATOM   17020 C  CA    . PRO A 1 3689 ? 155.868 161.938 179.981 1.00 56.07  ? 3689 PRO A CA    1 
ATOM   17021 C  C     . PRO A 1 3689 ? 155.723 162.303 181.445 1.00 56.64  ? 3689 PRO A C     1 
ATOM   17022 O  O     . PRO A 1 3689 ? 156.482 163.136 181.969 1.00 60.55  ? 3689 PRO A O     1 
ATOM   17023 C  CB    . PRO A 1 3689 ? 156.908 160.820 179.783 1.00 56.36  ? 3689 PRO A CB    1 
ATOM   17024 C  CG    . PRO A 1 3689 ? 157.676 161.218 178.572 1.00 59.56  ? 3689 PRO A CG    1 
ATOM   17025 C  CD    . PRO A 1 3689 ? 157.715 162.709 178.602 1.00 52.98  ? 3689 PRO A CD    1 
ATOM   17026 N  N     . PRO A 1 3690 ? 154.755 161.711 182.150 1.00 54.54  ? 3690 PRO A N     1 
ATOM   17027 C  CA    . PRO A 1 3690 ? 154.609 162.012 183.583 1.00 50.26  ? 3690 PRO A CA    1 
ATOM   17028 C  C     . PRO A 1 3690 ? 155.852 161.691 184.388 1.00 48.95  ? 3690 PRO A C     1 
ATOM   17029 O  O     . PRO A 1 3690 ? 156.064 162.286 185.452 1.00 50.34  ? 3690 PRO A O     1 
ATOM   17030 C  CB    . PRO A 1 3690 ? 153.420 161.139 184.002 1.00 51.29  ? 3690 PRO A CB    1 
ATOM   17031 C  CG    . PRO A 1 3690 ? 152.648 160.933 182.743 1.00 58.60  ? 3690 PRO A CG    1 
ATOM   17032 C  CD    . PRO A 1 3690 ? 153.672 160.848 181.652 1.00 53.34  ? 3690 PRO A CD    1 
ATOM   17033 N  N     . ASP A 1 3691 ? 156.683 160.764 183.909 1.00 48.19  ? 3691 ASP A N     1 
ATOM   17034 C  CA    . ASP A 1 3691 ? 157.964 160.500 184.555 1.00 48.04  ? 3691 ASP A CA    1 
ATOM   17035 C  C     . ASP A 1 3691 ? 158.831 161.754 184.582 1.00 49.31  ? 3691 ASP A C     1 
ATOM   17036 O  O     . ASP A 1 3691 ? 159.268 162.204 185.650 1.00 50.71  ? 3691 ASP A O     1 
ATOM   17037 C  CB    . ASP A 1 3691 ? 158.673 159.362 183.819 1.00 52.17  ? 3691 ASP A CB    1 
ATOM   17038 C  CG    . ASP A 1 3691 ? 159.881 158.844 184.563 1.00 63.68  ? 3691 ASP A CG    1 
ATOM   17039 O  OD1   . ASP A 1 3691 ? 160.855 159.607 184.724 1.00 67.34  ? 3691 ASP A OD1   1 
ATOM   17040 O  OD2   . ASP A 1 3691 ? 159.862 157.665 184.976 1.00 62.78  ? 3691 ASP A OD2   1 
ATOM   17041 N  N     . LEU A 1 3692 ? 159.061 162.355 183.413 1.00 49.34  ? 3692 LEU A N     1 
ATOM   17042 C  CA    . LEU A 1 3692 ? 159.863 163.571 183.363 1.00 41.27  ? 3692 LEU A CA    1 
ATOM   17043 C  C     . LEU A 1 3692 ? 159.185 164.703 184.120 1.00 41.63  ? 3692 LEU A C     1 
ATOM   17044 O  O     . LEU A 1 3692 ? 159.851 165.482 184.810 1.00 48.10  ? 3692 LEU A O     1 
ATOM   17045 C  CB    . LEU A 1 3692 ? 160.129 163.971 181.913 1.00 41.88  ? 3692 LEU A CB    1 
ATOM   17046 C  CG    . LEU A 1 3692 ? 160.902 165.275 181.735 1.00 40.75  ? 3692 LEU A CG    1 
ATOM   17047 C  CD1   . LEU A 1 3692 ? 162.300 165.131 182.294 1.00 38.06  ? 3692 LEU A CD1   1 
ATOM   17048 C  CD2   . LEU A 1 3692 ? 160.955 165.668 180.275 1.00 48.05  ? 3692 LEU A CD2   1 
ATOM   17049 N  N     . CYS A 1 3693 ? 157.857 164.804 184.013 1.00 37.73  ? 3693 CYS A N     1 
ATOM   17050 C  CA    . CYS A 1 3693 ? 157.129 165.809 184.779 1.00 39.47  ? 3693 CYS A CA    1 
ATOM   17051 C  C     . CYS A 1 3693 ? 157.376 165.660 186.273 1.00 41.13  ? 3693 CYS A C     1 
ATOM   17052 O  O     . CYS A 1 3693 ? 157.422 166.660 186.997 1.00 43.98  ? 3693 CYS A O     1 
ATOM   17053 C  CB    . CYS A 1 3693 ? 155.633 165.717 184.482 1.00 43.38  ? 3693 CYS A CB    1 
ATOM   17054 S  SG    . CYS A 1 3693 ? 155.198 165.912 182.743 1.00 59.21  ? 3693 CYS A SG    1 
ATOM   17055 N  N     . SER A 1 3694 ? 157.535 164.427 186.753 1.00 39.52  ? 3694 SER A N     1 
ATOM   17056 C  CA    . SER A 1 3694 ? 157.828 164.218 188.166 1.00 36.93  ? 3694 SER A CA    1 
ATOM   17057 C  C     . SER A 1 3694 ? 159.278 164.551 188.498 1.00 39.45  ? 3694 SER A C     1 
ATOM   17058 O  O     . SER A 1 3694 ? 159.562 165.058 189.588 1.00 41.36  ? 3694 SER A O     1 
ATOM   17059 C  CB    . SER A 1 3694 ? 157.506 162.778 188.562 1.00 37.00  ? 3694 SER A CB    1 
ATOM   17060 O  OG    . SER A 1 3694 ? 158.424 161.868 187.989 1.00 44.72  ? 3694 SER A OG    1 
ATOM   17061 N  N     . ARG A 1 3695 ? 160.209 164.276 187.582 1.00 40.90  ? 3695 ARG A N     1 
ATOM   17062 C  CA    . ARG A 1 3695 ? 161.617 164.531 187.875 1.00 34.31  ? 3695 ARG A CA    1 
ATOM   17063 C  C     . ARG A 1 3695 ? 162.053 165.982 187.688 1.00 39.03  ? 3695 ARG A C     1 
ATOM   17064 O  O     . ARG A 1 3695 ? 163.133 166.340 188.171 1.00 42.14  ? 3695 ARG A O     1 
ATOM   17065 C  CB    . ARG A 1 3695 ? 162.519 163.617 187.038 1.00 36.11  ? 3695 ARG A CB    1 
ATOM   17066 C  CG    . ARG A 1 3695 ? 162.713 162.224 187.625 1.00 43.28  ? 3695 ARG A CG    1 
ATOM   17067 C  CD    . ARG A 1 3695 ? 161.509 161.329 187.478 1.00 47.95  ? 3695 ARG A CD    1 
ATOM   17068 N  NE    . ARG A 1 3695 ? 161.754 160.005 188.034 1.00 44.43  ? 3695 ARG A NE    1 
ATOM   17069 C  CZ    . ARG A 1 3695 ? 162.284 158.999 187.357 1.00 44.88  ? 3695 ARG A CZ    1 
ATOM   17070 N  NH1   . ARG A 1 3695 ? 162.613 159.124 186.085 1.00 50.62  ? 3695 ARG A NH1   1 
ATOM   17071 N  NH2   . ARG A 1 3695 ? 162.484 157.838 187.972 1.00 53.42  ? 3695 ARG A NH2   1 
ATOM   17072 N  N     . VAL A 1 3696 ? 161.270 166.832 187.022 1.00 40.84  ? 3696 VAL A N     1 
ATOM   17073 C  CA    . VAL A 1 3696 ? 161.673 168.217 186.807 1.00 35.43  ? 3696 VAL A CA    1 
ATOM   17074 C  C     . VAL A 1 3696 ? 160.548 169.153 187.220 1.00 37.08  ? 3696 VAL A C     1 
ATOM   17075 O  O     . VAL A 1 3696 ? 159.380 168.769 187.302 1.00 43.78  ? 3696 VAL A O     1 
ATOM   17076 C  CB    . VAL A 1 3696 ? 162.072 168.508 185.344 1.00 30.96  ? 3696 VAL A CB    1 
ATOM   17077 C  CG1   . VAL A 1 3696 ? 163.192 167.591 184.899 1.00 31.90  ? 3696 VAL A CG1   1 
ATOM   17078 C  CG2   . VAL A 1 3696 ? 160.868 168.406 184.426 1.00 32.44  ? 3696 VAL A CG2   1 
ATOM   17079 N  N     . THR A 1 3697 ? 160.922 170.402 187.480 1.00 32.64  ? 3697 THR A N     1 
ATOM   17080 C  CA    . THR A 1 3697 ? 159.969 171.477 187.709 1.00 39.61  ? 3697 THR A CA    1 
ATOM   17081 C  C     . THR A 1 3697 ? 159.922 172.365 186.471 1.00 37.81  ? 3697 THR A C     1 
ATOM   17082 O  O     . THR A 1 3697 ? 160.964 172.751 185.933 1.00 37.41  ? 3697 THR A O     1 
ATOM   17083 C  CB    . THR A 1 3697 ? 160.322 172.285 188.965 1.00 41.05  ? 3697 THR A CB    1 
ATOM   17084 O  OG1   . THR A 1 3697 ? 159.277 173.223 189.245 1.00 59.40  ? 3697 THR A OG1   1 
ATOM   17085 C  CG2   . THR A 1 3697 ? 161.638 173.024 188.822 1.00 27.63  ? 3697 THR A CG2   1 
ATOM   17086 N  N     . PHE A 1 3698 ? 158.716 172.642 185.991 1.00 36.83  ? 3698 PHE A N     1 
ATOM   17087 C  CA    . PHE A 1 3698 ? 158.555 173.392 184.757 1.00 30.05  ? 3698 PHE A CA    1 
ATOM   17088 C  C     . PHE A 1 3698 ? 158.569 174.887 185.031 1.00 38.20  ? 3698 PHE A C     1 
ATOM   17089 O  O     . PHE A 1 3698 ? 157.960 175.365 185.990 1.00 49.73  ? 3698 PHE A O     1 
ATOM   17090 C  CB    . PHE A 1 3698 ? 157.258 172.996 184.058 1.00 29.85  ? 3698 PHE A CB    1 
ATOM   17091 C  CG    . PHE A 1 3698 ? 157.240 171.575 183.590 1.00 37.40  ? 3698 PHE A CG    1 
ATOM   17092 C  CD1   . PHE A 1 3698 ? 158.024 171.176 182.525 1.00 39.04  ? 3698 PHE A CD1   1 
ATOM   17093 C  CD2   . PHE A 1 3698 ? 156.450 170.635 184.223 1.00 41.90  ? 3698 PHE A CD2   1 
ATOM   17094 C  CE1   . PHE A 1 3698 ? 158.015 169.869 182.095 1.00 40.27  ? 3698 PHE A CE1   1 
ATOM   17095 C  CE2   . PHE A 1 3698 ? 156.436 169.326 183.797 1.00 45.40  ? 3698 PHE A CE2   1 
ATOM   17096 C  CZ    . PHE A 1 3698 ? 157.221 168.943 182.731 1.00 44.88  ? 3698 PHE A CZ    1 
ATOM   17097 N  N     . VAL A 1 3699 ? 159.282 175.621 184.183 1.00 34.55  ? 3699 VAL A N     1 
ATOM   17098 C  CA    . VAL A 1 3699 ? 159.372 177.073 184.267 1.00 30.25  ? 3699 VAL A CA    1 
ATOM   17099 C  C     . VAL A 1 3699 ? 159.050 177.593 182.872 1.00 29.42  ? 3699 VAL A C     1 
ATOM   17100 O  O     . VAL A 1 3699 ? 159.896 177.542 181.973 1.00 33.70  ? 3699 VAL A O     1 
ATOM   17101 C  CB    . VAL A 1 3699 ? 160.751 177.547 184.737 1.00 24.48  ? 3699 VAL A CB    1 
ATOM   17102 C  CG1   . VAL A 1 3699 ? 160.782 179.044 184.825 1.00 27.46  ? 3699 VAL A CG1   1 
ATOM   17103 C  CG2   . VAL A 1 3699 ? 161.090 176.939 186.083 1.00 26.76  ? 3699 VAL A CG2   1 
ATOM   17104 N  N     . ASN A 1 3700 ? 157.832 178.092 182.685 1.00 29.51  ? 3700 ASN A N     1 
ATOM   17105 C  CA    . ASN A 1 3700 ? 157.325 178.471 181.372 1.00 32.01  ? 3700 ASN A CA    1 
ATOM   17106 C  C     . ASN A 1 3700 ? 157.549 179.961 181.145 1.00 36.36  ? 3700 ASN A C     1 
ATOM   17107 O  O     . ASN A 1 3700 ? 157.046 180.792 181.906 1.00 37.80  ? 3700 ASN A O     1 
ATOM   17108 C  CB    . ASN A 1 3700 ? 155.841 178.130 181.251 1.00 32.04  ? 3700 ASN A CB    1 
ATOM   17109 C  CG    . ASN A 1 3700 ? 155.454 177.696 179.856 1.00 35.73  ? 3700 ASN A CG    1 
ATOM   17110 O  OD1   . ASN A 1 3700 ? 156.273 177.703 178.942 1.00 41.51  ? 3700 ASN A OD1   1 
ATOM   17111 N  ND2   . ASN A 1 3700 ? 154.197 177.309 179.686 1.00 34.45  ? 3700 ASN A ND2   1 
ATOM   17112 N  N     . PHE A 1 3701 ? 158.301 180.291 180.098 1.00 38.08  ? 3701 PHE A N     1 
ATOM   17113 C  CA    . PHE A 1 3701 ? 158.515 181.670 179.686 1.00 34.45  ? 3701 PHE A CA    1 
ATOM   17114 C  C     . PHE A 1 3701 ? 157.669 182.059 178.484 1.00 41.88  ? 3701 PHE A C     1 
ATOM   17115 O  O     . PHE A 1 3701 ? 157.874 183.140 177.925 1.00 49.22  ? 3701 PHE A O     1 
ATOM   17116 C  CB    . PHE A 1 3701 ? 159.991 181.908 179.355 1.00 35.35  ? 3701 PHE A CB    1 
ATOM   17117 C  CG    . PHE A 1 3701 ? 160.892 181.952 180.555 1.00 34.82  ? 3701 PHE A CG    1 
ATOM   17118 C  CD1   . PHE A 1 3701 ? 161.333 180.784 181.149 1.00 33.41  ? 3701 PHE A CD1   1 
ATOM   17119 C  CD2   . PHE A 1 3701 ? 161.310 183.161 181.080 1.00 38.23  ? 3701 PHE A CD2   1 
ATOM   17120 C  CE1   . PHE A 1 3701 ? 162.167 180.823 182.246 1.00 31.48  ? 3701 PHE A CE1   1 
ATOM   17121 C  CE2   . PHE A 1 3701 ? 162.144 183.203 182.178 1.00 35.39  ? 3701 PHE A CE2   1 
ATOM   17122 C  CZ    . PHE A 1 3701 ? 162.574 182.032 182.760 1.00 31.94  ? 3701 PHE A CZ    1 
ATOM   17123 N  N     . THR A 1 3702 ? 156.738 181.203 178.067 1.00 40.01  ? 3702 THR A N     1 
ATOM   17124 C  CA    . THR A 1 3702 ? 155.960 181.462 176.863 1.00 35.34  ? 3702 THR A CA    1 
ATOM   17125 C  C     . THR A 1 3702 ? 155.102 182.708 177.031 1.00 45.99  ? 3702 THR A C     1 
ATOM   17126 O  O     . THR A 1 3702 ? 154.452 182.897 178.062 1.00 51.85  ? 3702 THR A O     1 
ATOM   17127 C  CB    . THR A 1 3702 ? 155.078 180.258 176.539 1.00 35.10  ? 3702 THR A CB    1 
ATOM   17128 O  OG1   . THR A 1 3702 ? 155.884 179.075 176.499 1.00 42.66  ? 3702 THR A OG1   1 
ATOM   17129 C  CG2   . THR A 1 3702 ? 154.399 180.440 175.196 1.00 41.83  ? 3702 THR A CG2   1 
ATOM   17130 N  N     . VAL A 1 3703 ? 155.106 183.558 176.009 1.00 47.29  ? 3703 VAL A N     1 
ATOM   17131 C  CA    . VAL A 1 3703 ? 154.285 184.763 176.008 1.00 43.59  ? 3703 VAL A CA    1 
ATOM   17132 C  C     . VAL A 1 3703 ? 152.888 184.404 175.528 1.00 40.76  ? 3703 VAL A C     1 
ATOM   17133 O  O     . VAL A 1 3703 ? 152.704 183.956 174.391 1.00 45.43  ? 3703 VAL A O     1 
ATOM   17134 C  CB    . VAL A 1 3703 ? 154.914 185.851 175.125 1.00 44.11  ? 3703 VAL A CB    1 
ATOM   17135 C  CG1   . VAL A 1 3703 ? 153.997 187.057 175.034 1.00 44.97  ? 3703 VAL A CG1   1 
ATOM   17136 C  CG2   . VAL A 1 3703 ? 156.273 186.255 175.671 1.00 52.51  ? 3703 VAL A CG2   1 
ATOM   17137 N  N     . THR A 1 3704 ? 151.902 184.599 176.392 1.00 40.03  ? 3704 THR A N     1 
ATOM   17138 C  CA    . THR A 1 3704 ? 150.507 184.331 176.085 1.00 41.16  ? 3704 THR A CA    1 
ATOM   17139 C  C     . THR A 1 3704 ? 149.761 185.653 175.942 1.00 39.21  ? 3704 THR A C     1 
ATOM   17140 O  O     . THR A 1 3704 ? 150.350 186.733 176.001 1.00 41.06  ? 3704 THR A O     1 
ATOM   17141 C  CB    . THR A 1 3704 ? 149.868 183.451 177.163 1.00 49.95  ? 3704 THR A CB    1 
ATOM   17142 O  OG1   . THR A 1 3704 ? 149.855 184.153 178.412 1.00 53.20  ? 3704 THR A OG1   1 
ATOM   17143 C  CG2   . THR A 1 3704 ? 150.650 182.159 177.325 1.00 49.52  ? 3704 THR A CG2   1 
ATOM   17144 N  N     . ARG A 1 3705 ? 148.447 185.557 175.740 1.00 36.61  ? 3705 ARG A N     1 
ATOM   17145 C  CA    . ARG A 1 3705 ? 147.633 186.758 175.587 1.00 37.24  ? 3705 ARG A CA    1 
ATOM   17146 C  C     . ARG A 1 3705 ? 147.698 187.621 176.838 1.00 37.67  ? 3705 ARG A C     1 
ATOM   17147 O  O     . ARG A 1 3705 ? 147.850 188.845 176.759 1.00 42.89  ? 3705 ARG A O     1 
ATOM   17148 C  CB    . ARG A 1 3705 ? 146.190 186.369 175.266 1.00 45.05  ? 3705 ARG A CB    1 
ATOM   17149 C  CG    . ARG A 1 3705 ? 145.220 187.536 175.212 1.00 54.36  ? 3705 ARG A CG    1 
ATOM   17150 C  CD    . ARG A 1 3705 ? 144.058 187.251 174.273 1.00 66.11  ? 3705 ARG A CD    1 
ATOM   17151 N  NE    . ARG A 1 3705 ? 144.434 187.329 172.866 1.00 62.02  ? 3705 ARG A NE    1 
ATOM   17152 C  CZ    . ARG A 1 3705 ? 144.507 186.286 172.052 1.00 72.37  ? 3705 ARG A CZ    1 
ATOM   17153 N  NH1   . ARG A 1 3705 ? 144.282 185.056 172.481 1.00 81.15  ? 3705 ARG A NH1   1 
ATOM   17154 N  NH2   . ARG A 1 3705 ? 144.815 186.482 170.773 1.00 69.89  ? 3705 ARG A NH2   1 
ATOM   17155 N  N     . SER A 1 3706 ? 147.617 186.990 178.009 1.00 41.11  ? 3706 SER A N     1 
ATOM   17156 C  CA    . SER A 1 3706 ? 147.584 187.738 179.260 1.00 42.37  ? 3706 SER A CA    1 
ATOM   17157 C  C     . SER A 1 3706 ? 148.952 188.300 179.621 1.00 44.41  ? 3706 SER A C     1 
ATOM   17158 O  O     . SER A 1 3706 ? 149.048 189.418 180.138 1.00 45.50  ? 3706 SER A O     1 
ATOM   17159 C  CB    . SER A 1 3706 ? 147.067 186.845 180.377 1.00 47.80  ? 3706 SER A CB    1 
ATOM   17160 O  OG    . SER A 1 3706 ? 147.946 185.760 180.610 1.00 55.20  ? 3706 SER A OG    1 
ATOM   17161 N  N     . SER A 1 3707 ? 150.018 187.537 179.380 1.00 43.47  ? 3707 SER A N     1 
ATOM   17162 C  CA    . SER A 1 3707 ? 151.360 188.028 179.678 1.00 39.71  ? 3707 SER A CA    1 
ATOM   17163 C  C     . SER A 1 3707 ? 151.683 189.268 178.853 1.00 40.95  ? 3707 SER A C     1 
ATOM   17164 O  O     . SER A 1 3707 ? 152.155 190.282 179.384 1.00 46.03  ? 3707 SER A O     1 
ATOM   17165 C  CB    . SER A 1 3707 ? 152.385 186.925 179.424 1.00 44.64  ? 3707 SER A CB    1 
ATOM   17166 O  OG    . SER A 1 3707 ? 153.706 187.409 179.580 1.00 54.94  ? 3707 SER A OG    1 
ATOM   17167 N  N     . LEU A 1 3708 ? 151.415 189.211 177.548 1.00 35.27  ? 3708 LEU A N     1 
ATOM   17168 C  CA    . LEU A 1 3708 ? 151.653 190.370 176.699 1.00 31.60  ? 3708 LEU A CA    1 
ATOM   17169 C  C     . LEU A 1 3708 ? 150.697 191.508 177.021 1.00 32.74  ? 3708 LEU A C     1 
ATOM   17170 O  O     . LEU A 1 3708 ? 151.079 192.678 176.926 1.00 37.75  ? 3708 LEU A O     1 
ATOM   17171 C  CB    . LEU A 1 3708 ? 151.536 189.978 175.230 1.00 30.14  ? 3708 LEU A CB    1 
ATOM   17172 C  CG    . LEU A 1 3708 ? 151.823 191.118 174.259 1.00 34.83  ? 3708 LEU A CG    1 
ATOM   17173 C  CD1   . LEU A 1 3708 ? 153.307 191.413 174.202 1.00 40.33  ? 3708 LEU A CD1   1 
ATOM   17174 C  CD2   . LEU A 1 3708 ? 151.296 190.770 172.898 1.00 36.16  ? 3708 LEU A CD2   1 
ATOM   17175 N  N     . GLN A 1 3709 ? 149.459 191.193 177.404 1.00 32.85  ? 3709 GLN A N     1 
ATOM   17176 C  CA    . GLN A 1 3709 ? 148.532 192.238 177.821 1.00 33.08  ? 3709 GLN A CA    1 
ATOM   17177 C  C     . GLN A 1 3709 ? 149.054 192.980 179.046 1.00 38.66  ? 3709 GLN A C     1 
ATOM   17178 O  O     . GLN A 1 3709 ? 148.989 194.213 179.110 1.00 43.06  ? 3709 GLN A O     1 
ATOM   17179 C  CB    . GLN A 1 3709 ? 147.162 191.624 178.098 1.00 33.17  ? 3709 GLN A CB    1 
ATOM   17180 C  CG    . GLN A 1 3709 ? 146.212 192.506 178.871 1.00 38.07  ? 3709 GLN A CG    1 
ATOM   17181 C  CD    . GLN A 1 3709 ? 144.832 191.899 178.962 1.00 52.69  ? 3709 GLN A CD    1 
ATOM   17182 O  OE1   . GLN A 1 3709 ? 143.972 192.390 179.689 1.00 54.72  ? 3709 GLN A OE1   1 
ATOM   17183 N  NE2   . GLN A 1 3709 ? 144.611 190.822 178.218 1.00 52.08  ? 3709 GLN A NE2   1 
ATOM   17184 N  N     . SER A 1 3710 ? 149.586 192.243 180.023 1.00 38.00  ? 3710 SER A N     1 
ATOM   17185 C  CA    . SER A 1 3710 ? 150.162 192.874 181.206 1.00 35.77  ? 3710 SER A CA    1 
ATOM   17186 C  C     . SER A 1 3710 ? 151.396 193.693 180.852 1.00 39.12  ? 3710 SER A C     1 
ATOM   17187 O  O     . SER A 1 3710 ? 151.591 194.793 181.381 1.00 45.41  ? 3710 SER A O     1 
ATOM   17188 C  CB    . SER A 1 3710 ? 150.504 191.813 182.249 1.00 43.91  ? 3710 SER A CB    1 
ATOM   17189 O  OG    . SER A 1 3710 ? 149.332 191.325 182.877 1.00 55.79  ? 3710 SER A OG    1 
ATOM   17190 N  N     . GLN A 1 3711 ? 152.247 193.169 179.965 1.00 38.24  ? 3711 GLN A N     1 
ATOM   17191 C  CA    . GLN A 1 3711 ? 153.417 193.926 179.527 1.00 38.16  ? 3711 GLN A CA    1 
ATOM   17192 C  C     . GLN A 1 3711 ? 153.003 195.247 178.891 1.00 42.33  ? 3711 GLN A C     1 
ATOM   17193 O  O     . GLN A 1 3711 ? 153.558 196.309 179.204 1.00 44.03  ? 3711 GLN A O     1 
ATOM   17194 C  CB    . GLN A 1 3711 ? 154.236 193.101 178.535 1.00 33.48  ? 3711 GLN A CB    1 
ATOM   17195 C  CG    . GLN A 1 3711 ? 155.089 192.017 179.154 1.00 41.06  ? 3711 GLN A CG    1 
ATOM   17196 C  CD    . GLN A 1 3711 ? 155.867 191.243 178.111 1.00 50.57  ? 3711 GLN A CD    1 
ATOM   17197 O  OE1   . GLN A 1 3711 ? 156.454 191.826 177.200 1.00 53.55  ? 3711 GLN A OE1   1 
ATOM   17198 N  NE2   . GLN A 1 3711 ? 155.874 189.922 178.236 1.00 57.94  ? 3711 GLN A NE2   1 
ATOM   17199 N  N     . CYS A 1 3712 ? 152.017 195.196 177.996 1.00 38.26  ? 3712 CYS A N     1 
ATOM   17200 C  CA    . CYS A 1 3712 ? 151.571 196.396 177.303 1.00 32.19  ? 3712 CYS A CA    1 
ATOM   17201 C  C     . CYS A 1 3712 ? 150.912 197.378 178.262 1.00 39.16  ? 3712 CYS A C     1 
ATOM   17202 O  O     . CYS A 1 3712 ? 151.089 198.593 178.127 1.00 45.83  ? 3712 CYS A O     1 
ATOM   17203 C  CB    . CYS A 1 3712 ? 150.622 196.015 176.171 1.00 34.43  ? 3712 CYS A CB    1 
ATOM   17204 S  SG    . CYS A 1 3712 ? 151.416 195.071 174.852 1.00 46.00  ? 3712 CYS A SG    1 
ATOM   17205 N  N     . LEU A 1 3713 ? 150.145 196.877 179.234 1.00 39.31  ? 3713 LEU A N     1 
ATOM   17206 C  CA    . LEU A 1 3713 ? 149.544 197.766 180.222 1.00 38.64  ? 3713 LEU A CA    1 
ATOM   17207 C  C     . LEU A 1 3713 ? 150.609 198.458 181.058 1.00 44.80  ? 3713 LEU A C     1 
ATOM   17208 O  O     . LEU A 1 3713 ? 150.523 199.665 181.316 1.00 49.50  ? 3713 LEU A O     1 
ATOM   17209 C  CB    . LEU A 1 3713 ? 148.583 196.985 181.116 1.00 38.10  ? 3713 LEU A CB    1 
ATOM   17210 C  CG    . LEU A 1 3713 ? 147.933 197.777 182.247 1.00 44.23  ? 3713 LEU A CG    1 
ATOM   17211 C  CD1   . LEU A 1 3713 ? 147.022 198.839 181.672 1.00 44.69  ? 3713 LEU A CD1   1 
ATOM   17212 C  CD2   . LEU A 1 3713 ? 147.158 196.855 183.167 1.00 55.57  ? 3713 LEU A CD2   1 
ATOM   17213 N  N     . ASN A 1 3714 ? 151.630 197.711 181.483 1.00 44.13  ? 3714 ASN A N     1 
ATOM   17214 C  CA    . ASN A 1 3714 ? 152.708 198.315 182.254 1.00 42.63  ? 3714 ASN A CA    1 
ATOM   17215 C  C     . ASN A 1 3714 ? 153.445 199.364 181.435 1.00 44.44  ? 3714 ASN A C     1 
ATOM   17216 O  O     . ASN A 1 3714 ? 153.818 200.419 181.958 1.00 49.76  ? 3714 ASN A O     1 
ATOM   17217 C  CB    . ASN A 1 3714 ? 153.672 197.236 182.744 1.00 46.63  ? 3714 ASN A CB    1 
ATOM   17218 C  CG    . ASN A 1 3714 ? 153.045 196.324 183.777 1.00 52.30  ? 3714 ASN A CG    1 
ATOM   17219 O  OD1   . ASN A 1 3714 ? 151.923 196.557 184.226 1.00 51.31  ? 3714 ASN A OD1   1 
ATOM   17220 N  ND2   . ASN A 1 3714 ? 153.765 195.277 184.157 1.00 56.33  ? 3714 ASN A ND2   1 
ATOM   17221 N  N     . GLU A 1 3715 ? 153.653 199.101 180.143 1.00 44.27  ? 3715 GLU A N     1 
ATOM   17222 C  CA    . GLU A 1 3715 ? 154.365 200.072 179.318 1.00 46.25  ? 3715 GLU A CA    1 
ATOM   17223 C  C     . GLU A 1 3715 ? 153.515 201.314 179.053 1.00 47.41  ? 3715 GLU A C     1 
ATOM   17224 O  O     . GLU A 1 3715 ? 154.041 202.432 179.020 1.00 54.70  ? 3715 GLU A O     1 
ATOM   17225 C  CB    . GLU A 1 3715 ? 154.834 199.417 178.019 1.00 43.17  ? 3715 GLU A CB    1 
ATOM   17226 C  CG    . GLU A 1 3715 ? 155.907 198.359 178.271 1.00 59.23  ? 3715 GLU A CG    1 
ATOM   17227 C  CD    . GLU A 1 3715 ? 156.415 197.682 177.012 1.00 65.59  ? 3715 GLU A CD    1 
ATOM   17228 O  OE1   . GLU A 1 3715 ? 155.870 197.943 175.925 1.00 57.31  ? 3715 GLU A OE1   1 
ATOM   17229 O  OE2   . GLU A 1 3715 ? 157.362 196.875 177.113 1.00 69.57  ? 3715 GLU A OE2   1 
ATOM   17230 N  N     . VAL A 1 3716 ? 152.197 201.149 178.898 1.00 44.98  ? 3716 VAL A N     1 
ATOM   17231 C  CA    . VAL A 1 3716 ? 151.321 202.317 178.790 1.00 39.17  ? 3716 VAL A CA    1 
ATOM   17232 C  C     . VAL A 1 3716 ? 151.378 203.147 180.063 1.00 45.46  ? 3716 VAL A C     1 
ATOM   17233 O  O     . VAL A 1 3716 ? 151.467 204.379 180.013 1.00 54.86  ? 3716 VAL A O     1 
ATOM   17234 C  CB    . VAL A 1 3716 ? 149.872 201.905 178.474 1.00 41.50  ? 3716 VAL A CB    1 
ATOM   17235 C  CG1   . VAL A 1 3716 ? 148.988 203.122 178.502 1.00 45.71  ? 3716 VAL A CG1   1 
ATOM   17236 C  CG2   . VAL A 1 3716 ? 149.770 201.296 177.119 1.00 39.14  ? 3716 VAL A CG2   1 
ATOM   17237 N  N     . LEU A 1 3717 ? 151.306 202.493 181.223 1.00 44.21  ? 3717 LEU A N     1 
ATOM   17238 C  CA    . LEU A 1 3717 ? 151.366 203.233 182.480 1.00 48.14  ? 3717 LEU A CA    1 
ATOM   17239 C  C     . LEU A 1 3717 ? 152.702 203.946 182.641 1.00 54.41  ? 3717 LEU A C     1 
ATOM   17240 O  O     . LEU A 1 3717 ? 152.753 205.079 183.130 1.00 58.15  ? 3717 LEU A O     1 
ATOM   17241 C  CB    . LEU A 1 3717 ? 151.105 202.301 183.663 1.00 53.64  ? 3717 LEU A CB    1 
ATOM   17242 C  CG    . LEU A 1 3717 ? 149.650 202.126 184.101 1.00 51.14  ? 3717 LEU A CG    1 
ATOM   17243 C  CD1   . LEU A 1 3717 ? 149.135 203.446 184.620 1.00 57.64  ? 3717 LEU A CD1   1 
ATOM   17244 C  CD2   . LEU A 1 3717 ? 148.764 201.639 182.979 1.00 47.69  ? 3717 LEU A CD2   1 
ATOM   17245 N  N     . LYS A 1 3718 ? 153.794 203.300 182.235 1.00 53.17  ? 3718 LYS A N     1 
ATOM   17246 C  CA    . LYS A 1 3718 ? 155.103 203.933 182.341 1.00 51.42  ? 3718 LYS A CA    1 
ATOM   17247 C  C     . LYS A 1 3718 ? 155.226 205.118 181.390 1.00 54.03  ? 3718 LYS A C     1 
ATOM   17248 O  O     . LYS A 1 3718 ? 155.875 206.118 181.718 1.00 60.13  ? 3718 LYS A O     1 
ATOM   17249 C  CB    . LYS A 1 3718 ? 156.200 202.904 182.071 1.00 58.13  ? 3718 LYS A CB    1 
ATOM   17250 C  CG    . LYS A 1 3718 ? 157.613 203.454 182.141 1.00 68.13  ? 3718 LYS A CG    1 
ATOM   17251 C  CD    . LYS A 1 3718 ? 158.641 202.335 182.083 1.00 74.93  ? 3718 LYS A CD    1 
ATOM   17252 C  CE    . LYS A 1 3718 ? 158.421 201.442 180.872 1.00 72.49  ? 3718 LYS A CE    1 
ATOM   17253 N  NZ    . LYS A 1 3718 ? 158.478 202.207 179.595 1.00 64.58  ? 3718 LYS A NZ    1 
ATOM   17254 N  N     . ALA A 1 3719 ? 154.605 205.032 180.211 1.00 53.53  ? 3719 ALA A N     1 
ATOM   17255 C  CA    . ALA A 1 3719 ? 154.782 206.073 179.204 1.00 50.13  ? 3719 ALA A CA    1 
ATOM   17256 C  C     . ALA A 1 3719 ? 153.862 207.266 179.439 1.00 52.39  ? 3719 ALA A C     1 
ATOM   17257 O  O     . ALA A 1 3719 ? 154.316 208.415 179.437 1.00 54.05  ? 3719 ALA A O     1 
ATOM   17258 C  CB    . ALA A 1 3719 ? 154.550 205.490 177.809 1.00 46.78  ? 3719 ALA A CB    1 
ATOM   17259 N  N     . GLU A 1 3720 ? 152.568 207.019 179.642 1.00 51.93  ? 3720 GLU A N     1 
ATOM   17260 C  CA    . GLU A 1 3720 ? 151.579 208.089 179.640 1.00 54.00  ? 3720 GLU A CA    1 
ATOM   17261 C  C     . GLU A 1 3720 ? 151.145 208.542 181.027 1.00 60.22  ? 3720 GLU A C     1 
ATOM   17262 O  O     . GLU A 1 3720 ? 150.645 209.664 181.161 1.00 66.15  ? 3720 GLU A O     1 
ATOM   17263 C  CB    . GLU A 1 3720 ? 150.342 207.660 178.843 1.00 52.19  ? 3720 GLU A CB    1 
ATOM   17264 C  CG    . GLU A 1 3720 ? 150.650 207.308 177.401 1.00 60.76  ? 3720 GLU A CG    1 
ATOM   17265 C  CD    . GLU A 1 3720 ? 151.145 208.500 176.602 1.00 68.12  ? 3720 GLU A CD    1 
ATOM   17266 O  OE1   . GLU A 1 3720 ? 150.806 209.647 176.963 1.00 67.29  ? 3720 GLU A OE1   1 
ATOM   17267 O  OE2   . GLU A 1 3720 ? 151.889 208.293 175.620 1.00 64.13  ? 3720 GLU A OE2   1 
ATOM   17268 N  N     . ARG A 1 3721 ? 151.316 207.715 182.054 1.00 60.11  ? 3721 ARG A N     1 
ATOM   17269 C  CA    . ARG A 1 3721 ? 150.989 208.084 183.431 1.00 64.13  ? 3721 ARG A CA    1 
ATOM   17270 C  C     . ARG A 1 3721 ? 152.183 207.778 184.323 1.00 65.01  ? 3721 ARG A C     1 
ATOM   17271 O  O     . ARG A 1 3721 ? 152.138 206.860 185.150 1.00 68.57  ? 3721 ARG A O     1 
ATOM   17272 C  CB    . ARG A 1 3721 ? 149.739 207.349 183.917 1.00 61.32  ? 3721 ARG A CB    1 
ATOM   17273 C  CG    . ARG A 1 3721 ? 148.466 207.762 183.210 1.00 62.43  ? 3721 ARG A CG    1 
ATOM   17274 C  CD    . ARG A 1 3721 ? 148.236 209.260 183.314 1.00 68.44  ? 3721 ARG A CD    1 
ATOM   17275 N  NE    . ARG A 1 3721 ? 148.145 209.715 184.696 1.00 72.30  ? 3721 ARG A NE    1 
ATOM   17276 C  CZ    . ARG A 1 3721 ? 147.093 209.524 185.481 1.00 72.02  ? 3721 ARG A CZ    1 
ATOM   17277 N  NH1   . ARG A 1 3721 ? 146.011 208.897 185.048 1.00 66.00  ? 3721 ARG A NH1   1 
ATOM   17278 N  NH2   . ARG A 1 3721 ? 147.124 209.980 186.729 1.00 69.19  ? 3721 ARG A NH2   1 
ATOM   17279 N  N     . PRO A 1 3722 ? 153.275 208.534 184.181 1.00 64.57  ? 3722 PRO A N     1 
ATOM   17280 C  CA    . PRO A 1 3722 ? 154.466 208.246 184.994 1.00 67.67  ? 3722 PRO A CA    1 
ATOM   17281 C  C     . PRO A 1 3722 ? 154.219 208.350 186.487 1.00 72.45  ? 3722 PRO A C     1 
ATOM   17282 O  O     . PRO A 1 3722 ? 154.837 207.605 187.255 1.00 74.87  ? 3722 PRO A O     1 
ATOM   17283 C  CB    . PRO A 1 3722 ? 155.480 209.293 184.511 1.00 70.85  ? 3722 PRO A CB    1 
ATOM   17284 C  CG    . PRO A 1 3722 ? 154.654 210.385 183.933 1.00 69.14  ? 3722 PRO A CG    1 
ATOM   17285 C  CD    . PRO A 1 3722 ? 153.463 209.717 183.325 1.00 66.57  ? 3722 PRO A CD    1 
ATOM   17286 N  N     . ASP A 1 3723 ? 153.334 209.248 186.926 1.00 73.16  ? 3723 ASP A N     1 
ATOM   17287 C  CA    . ASP A 1 3723 ? 153.044 209.356 188.353 1.00 68.77  ? 3723 ASP A CA    1 
ATOM   17288 C  C     . ASP A 1 3723 ? 152.379 208.090 188.882 1.00 66.90  ? 3723 ASP A C     1 
ATOM   17289 O  O     . ASP A 1 3723 ? 152.733 207.599 189.961 1.00 72.70  ? 3723 ASP A O     1 
ATOM   17290 C  CB    . ASP A 1 3723 ? 152.169 210.580 188.623 1.00 74.70  ? 3723 ASP A CB    1 
ATOM   17291 C  CG    . ASP A 1 3723 ? 150.867 210.552 187.847 1.00 79.73  ? 3723 ASP A CG    1 
ATOM   17292 O  OD1   . ASP A 1 3723 ? 150.915 210.579 186.600 1.00 80.78  ? 3723 ASP A OD1   1 
ATOM   17293 O  OD2   . ASP A 1 3723 ? 149.795 210.501 188.486 1.00 78.31  ? 3723 ASP A OD2   1 
ATOM   17294 N  N     . VAL A 1 3724 ? 151.419 207.541 188.136 1.00 62.94  ? 3724 VAL A N     1 
ATOM   17295 C  CA    . VAL A 1 3724 ? 150.746 206.325 188.580 1.00 63.15  ? 3724 VAL A CA    1 
ATOM   17296 C  C     . VAL A 1 3724 ? 151.705 205.141 188.542 1.00 60.75  ? 3724 VAL A C     1 
ATOM   17297 O  O     . VAL A 1 3724 ? 151.655 204.257 189.404 1.00 65.47  ? 3724 VAL A O     1 
ATOM   17298 C  CB    . VAL A 1 3724 ? 149.484 206.073 187.735 1.00 63.62  ? 3724 VAL A CB    1 
ATOM   17299 C  CG1   . VAL A 1 3724 ? 148.935 204.682 187.992 1.00 55.49  ? 3724 VAL A CG1   1 
ATOM   17300 C  CG2   . VAL A 1 3724 ? 148.432 207.123 188.041 1.00 70.65  ? 3724 VAL A CG2   1 
ATOM   17301 N  N     . ASP A 1 3725 ? 152.595 205.105 187.548 1.00 58.37  ? 3725 ASP A N     1 
ATOM   17302 C  CA    . ASP A 1 3725 ? 153.609 204.057 187.507 1.00 57.63  ? 3725 ASP A CA    1 
ATOM   17303 C  C     . ASP A 1 3725 ? 154.543 204.146 188.708 1.00 63.40  ? 3725 ASP A C     1 
ATOM   17304 O  O     . ASP A 1 3725 ? 154.896 203.123 189.307 1.00 66.77  ? 3725 ASP A O     1 
ATOM   17305 C  CB    . ASP A 1 3725 ? 154.400 204.145 186.203 1.00 63.03  ? 3725 ASP A CB    1 
ATOM   17306 C  CG    . ASP A 1 3725 ? 155.309 202.953 185.993 1.00 76.24  ? 3725 ASP A CG    1 
ATOM   17307 O  OD1   . ASP A 1 3725 ? 154.800 201.813 185.954 1.00 79.55  ? 3725 ASP A OD1   1 
ATOM   17308 O  OD2   . ASP A 1 3725 ? 156.534 203.155 185.865 1.00 82.38  ? 3725 ASP A OD2   1 
ATOM   17309 N  N     . GLU A 1 3726 ? 154.956 205.362 189.076 1.00 65.21  ? 3726 GLU A N     1 
ATOM   17310 C  CA    . GLU A 1 3726 ? 155.790 205.533 190.261 1.00 60.83  ? 3726 GLU A CA    1 
ATOM   17311 C  C     . GLU A 1 3726 ? 155.053 205.100 191.520 1.00 60.19  ? 3726 GLU A C     1 
ATOM   17312 O  O     . GLU A 1 3726 ? 155.640 204.465 192.402 1.00 68.41  ? 3726 GLU A O     1 
ATOM   17313 C  CB    . GLU A 1 3726 ? 156.245 206.987 190.390 1.00 68.07  ? 3726 GLU A CB    1 
ATOM   17314 C  CG    . GLU A 1 3726 ? 157.203 207.450 189.310 1.00 80.77  ? 3726 GLU A CG    1 
ATOM   17315 C  CD    . GLU A 1 3726 ? 157.230 208.961 189.172 1.00 88.73  ? 3726 GLU A CD    1 
ATOM   17316 O  OE1   . GLU A 1 3726 ? 157.528 209.645 190.174 1.00 92.36  ? 3726 GLU A OE1   1 
ATOM   17317 O  OE2   . GLU A 1 3726 ? 156.954 209.464 188.063 1.00 82.76  ? 3726 GLU A OE2   1 
ATOM   17318 N  N     . LYS A 1 3727 ? 153.767 205.437 191.628 1.00 55.35  ? 3727 LYS A N     1 
ATOM   17319 C  CA    . LYS A 1 3727 ? 153.003 205.017 192.798 1.00 52.08  ? 3727 LYS A CA    1 
ATOM   17320 C  C     . LYS A 1 3727 ? 152.856 203.501 192.865 1.00 53.53  ? 3727 LYS A C     1 
ATOM   17321 O  O     . LYS A 1 3727 ? 152.971 202.919 193.948 1.00 63.16  ? 3727 LYS A O     1 
ATOM   17322 C  CB    . LYS A 1 3727 ? 151.637 205.700 192.807 1.00 55.34  ? 3727 LYS A CB    1 
ATOM   17323 C  CG    . LYS A 1 3727 ? 151.725 207.212 192.952 1.00 64.35  ? 3727 LYS A CG    1 
ATOM   17324 C  CD    . LYS A 1 3727 ? 150.464 207.807 193.552 1.00 59.28  ? 3727 LYS A CD    1 
ATOM   17325 C  CE    . LYS A 1 3727 ? 149.240 207.460 192.730 1.00 65.55  ? 3727 LYS A CE    1 
ATOM   17326 N  NZ    . LYS A 1 3727 ? 148.005 208.035 193.326 1.00 68.09  ? 3727 LYS A NZ    1 
ATOM   17327 N  N     . ARG A 1 3728 ? 152.613 202.843 191.731 1.00 51.14  ? 3728 ARG A N     1 
ATOM   17328 C  CA    . ARG A 1 3728 ? 152.541 201.385 191.727 1.00 52.59  ? 3728 ARG A CA    1 
ATOM   17329 C  C     . ARG A 1 3728 ? 153.880 200.766 192.114 1.00 57.92  ? 3728 ARG A C     1 
ATOM   17330 O  O     . ARG A 1 3728 ? 153.929 199.805 192.895 1.00 60.37  ? 3728 ARG A O     1 
ATOM   17331 C  CB    . ARG A 1 3728 ? 152.087 200.890 190.354 1.00 52.92  ? 3728 ARG A CB    1 
ATOM   17332 C  CG    . ARG A 1 3728 ? 152.088 199.382 190.198 1.00 57.73  ? 3728 ARG A CG    1 
ATOM   17333 C  CD    . ARG A 1 3728 ? 151.984 198.981 188.734 1.00 62.46  ? 3728 ARG A CD    1 
ATOM   17334 N  NE    . ARG A 1 3728 ? 153.086 199.499 187.932 1.00 73.46  ? 3728 ARG A NE    1 
ATOM   17335 C  CZ    . ARG A 1 3728 ? 154.333 199.051 187.986 1.00 79.01  ? 3728 ARG A CZ    1 
ATOM   17336 N  NH1   . ARG A 1 3728 ? 154.677 198.054 188.786 1.00 76.41  ? 3728 ARG A NH1   1 
ATOM   17337 N  NH2   . ARG A 1 3728 ? 155.258 199.613 187.214 1.00 78.64  ? 3728 ARG A NH2   1 
ATOM   17338 N  N     . SER A 1 3729 ? 154.979 201.309 191.587 1.00 60.34  ? 3729 SER A N     1 
ATOM   17339 C  CA    . SER A 1 3729 ? 156.296 200.845 192.001 1.00 53.13  ? 3729 SER A CA    1 
ATOM   17340 C  C     . SER A 1 3729 ? 156.503 201.054 193.495 1.00 54.18  ? 3729 SER A C     1 
ATOM   17341 O  O     . SER A 1 3729 ? 157.157 200.242 194.153 1.00 61.10  ? 3729 SER A O     1 
ATOM   17342 C  CB    . SER A 1 3729 ? 157.384 201.559 191.201 1.00 57.32  ? 3729 SER A CB    1 
ATOM   17343 O  OG    . SER A 1 3729 ? 157.229 201.329 189.812 1.00 63.76  ? 3729 SER A OG    1 
ATOM   17344 N  N     . ASP A 1 3730 ? 155.950 202.135 194.047 1.00 52.14  ? 3730 ASP A N     1 
ATOM   17345 C  CA    . ASP A 1 3730 ? 156.031 202.352 195.488 1.00 50.32  ? 3730 ASP A CA    1 
ATOM   17346 C  C     . ASP A 1 3730 ? 155.239 201.306 196.259 1.00 52.36  ? 3730 ASP A C     1 
ATOM   17347 O  O     . ASP A 1 3730 ? 155.671 200.871 197.329 1.00 65.16  ? 3730 ASP A O     1 
ATOM   17348 C  CB    . ASP A 1 3730 ? 155.544 203.757 195.838 1.00 59.60  ? 3730 ASP A CB    1 
ATOM   17349 C  CG    . ASP A 1 3730 ? 156.506 204.836 195.384 1.00 73.09  ? 3730 ASP A CG    1 
ATOM   17350 O  OD1   . ASP A 1 3730 ? 157.528 204.494 194.754 1.00 69.65  ? 3730 ASP A OD1   1 
ATOM   17351 O  OD2   . ASP A 1 3730 ? 156.244 206.025 195.660 1.00 79.38  ? 3730 ASP A OD2   1 
ATOM   17352 N  N     . LEU A 1 3731 ? 154.079 200.899 195.742 1.00 52.79  ? 3731 LEU A N     1 
ATOM   17353 C  CA    . LEU A 1 3731 ? 153.362 199.777 196.350 1.00 57.75  ? 3731 LEU A CA    1 
ATOM   17354 C  C     . LEU A 1 3731 ? 154.209 198.513 196.365 1.00 56.69  ? 3731 LEU A C     1 
ATOM   17355 O  O     . LEU A 1 3731 ? 154.291 197.825 197.389 1.00 58.65  ? 3731 LEU A O     1 
ATOM   17356 C  CB    . LEU A 1 3731 ? 152.045 199.509 195.626 1.00 55.87  ? 3731 LEU A CB    1 
ATOM   17357 C  CG    . LEU A 1 3731 ? 150.782 200.263 196.028 1.00 47.51  ? 3731 LEU A CG    1 
ATOM   17358 C  CD1   . LEU A 1 3731 ? 150.845 201.706 195.670 1.00 53.32  ? 3731 LEU A CD1   1 
ATOM   17359 C  CD2   . LEU A 1 3731 ? 149.619 199.612 195.320 1.00 56.31  ? 3731 LEU A CD2   1 
ATOM   17360 N  N     . LEU A 1 3732 ? 154.834 198.180 195.236 1.00 54.40  ? 3732 LEU A N     1 
ATOM   17361 C  CA    . LEU A 1 3732 ? 155.681 196.987 195.203 1.00 52.96  ? 3732 LEU A CA    1 
ATOM   17362 C  C     . LEU A 1 3732 ? 156.883 197.118 196.136 1.00 55.20  ? 3732 LEU A C     1 
ATOM   17363 O  O     . LEU A 1 3732 ? 157.299 196.137 196.762 1.00 55.56  ? 3732 LEU A O     1 
ATOM   17364 C  CB    . LEU A 1 3732 ? 156.124 196.673 193.772 1.00 53.19  ? 3732 LEU A CB    1 
ATOM   17365 C  CG    . LEU A 1 3732 ? 155.122 195.971 192.842 1.00 59.19  ? 3732 LEU A CG    1 
ATOM   17366 C  CD1   . LEU A 1 3732 ? 153.969 196.846 192.406 1.00 67.42  ? 3732 LEU A CD1   1 
ATOM   17367 C  CD2   . LEU A 1 3732 ? 155.847 195.436 191.616 1.00 59.89  ? 3732 LEU A CD2   1 
ATOM   17368 N  N     . LYS A 1 3733 ? 157.455 198.319 196.244 1.00 58.09  ? 3733 LYS A N     1 
ATOM   17369 C  CA    . LYS A 1 3733 ? 158.595 198.531 197.132 1.00 57.55  ? 3733 LYS A CA    1 
ATOM   17370 C  C     . LYS A 1 3733 ? 158.198 198.546 198.601 1.00 59.24  ? 3733 LYS A C     1 
ATOM   17371 O  O     . LYS A 1 3733 ? 159.046 198.293 199.462 1.00 70.30  ? 3733 LYS A O     1 
ATOM   17372 C  CB    . LYS A 1 3733 ? 159.302 199.841 196.782 1.00 56.67  ? 3733 LYS A CB    1 
ATOM   17373 C  CG    . LYS A 1 3733 ? 159.974 199.848 195.422 1.00 58.75  ? 3733 LYS A CG    1 
ATOM   17374 C  CD    . LYS A 1 3733 ? 160.652 201.178 195.153 1.00 68.28  ? 3733 LYS A CD    1 
ATOM   17375 C  CE    . LYS A 1 3733 ? 161.288 201.202 193.774 1.00 77.65  ? 3733 LYS A CE    1 
ATOM   17376 N  NZ    . LYS A 1 3733 ? 161.928 202.513 193.480 1.00 79.52  ? 3733 LYS A NZ    1 
ATOM   17377 N  N     . LEU A 1 3734 ? 156.939 198.845 198.907 1.00 55.73  ? 3734 LEU A N     1 
ATOM   17378 C  CA    . LEU A 1 3734 ? 156.480 198.904 200.287 1.00 64.49  ? 3734 LEU A CA    1 
ATOM   17379 C  C     . LEU A 1 3734 ? 156.377 197.526 200.928 1.00 66.16  ? 3734 LEU A C     1 
ATOM   17380 O  O     . LEU A 1 3734 ? 156.209 197.435 202.149 1.00 67.62  ? 3734 LEU A O     1 
ATOM   17381 C  CB    . LEU A 1 3734 ? 155.129 199.626 200.337 1.00 62.99  ? 3734 LEU A CB    1 
ATOM   17382 C  CG    . LEU A 1 3734 ? 154.443 199.896 201.675 1.00 70.70  ? 3734 LEU A CG    1 
ATOM   17383 C  CD1   . LEU A 1 3734 ? 155.303 200.811 202.526 1.00 75.79  ? 3734 LEU A CD1   1 
ATOM   17384 C  CD2   . LEU A 1 3734 ? 153.073 200.503 201.450 1.00 73.13  ? 3734 LEU A CD2   1 
ATOM   17385 N  N     . GLN A 1 3735 ? 156.505 196.457 200.144 1.00 61.91  ? 3735 GLN A N     1 
ATOM   17386 C  CA    . GLN A 1 3735 ? 156.441 195.094 200.650 1.00 60.05  ? 3735 GLN A CA    1 
ATOM   17387 C  C     . GLN A 1 3735 ? 157.755 194.631 201.267 1.00 69.24  ? 3735 GLN A C     1 
ATOM   17388 O  O     . GLN A 1 3735 ? 157.971 193.421 201.402 1.00 76.86  ? 3735 GLN A O     1 
ATOM   17389 C  CB    . GLN A 1 3735 ? 156.029 194.136 199.530 1.00 58.71  ? 3735 GLN A CB    1 
ATOM   17390 C  CG    . GLN A 1 3735 ? 154.678 194.441 198.910 1.00 59.73  ? 3735 GLN A CG    1 
ATOM   17391 C  CD    . GLN A 1 3735 ? 153.525 193.858 199.699 1.00 65.51  ? 3735 GLN A CD    1 
ATOM   17392 O  OE1   . GLN A 1 3735 ? 153.727 193.163 200.693 1.00 71.10  ? 3735 GLN A OE1   1 
ATOM   17393 N  NE2   . GLN A 1 3735 ? 152.307 194.137 199.257 1.00 65.37  ? 3735 GLN A NE2   1 
ATOM   17394 N  N     . GLY A 1 3736 ? 158.635 195.557 201.640 1.00 67.48  ? 3736 GLY A N     1 
ATOM   17395 C  CA    . GLY A 1 3736 ? 159.876 195.195 202.293 1.00 70.26  ? 3736 GLY A CA    1 
ATOM   17396 C  C     . GLY A 1 3736 ? 161.076 196.030 201.897 1.00 79.73  ? 3736 GLY A C     1 
ATOM   17397 O  O     . GLY A 1 3736 ? 162.015 196.166 202.685 1.00 89.24  ? 3736 GLY A O     1 
ATOM   17398 N  N     . GLU A 1 3737 ? 161.063 196.602 200.691 1.00 70.81  ? 3737 GLU A N     1 
ATOM   17399 C  CA    . GLU A 1 3737 ? 162.211 197.379 200.230 1.00 70.04  ? 3737 GLU A CA    1 
ATOM   17400 C  C     . GLU A 1 3737 ? 162.364 198.669 201.029 1.00 77.91  ? 3737 GLU A C     1 
ATOM   17401 O  O     . GLU A 1 3737 ? 163.469 199.012 201.472 1.00 85.63  ? 3737 GLU A O     1 
ATOM   17402 C  CB    . GLU A 1 3737 ? 162.075 197.682 198.740 1.00 63.84  ? 3737 GLU A CB    1 
ATOM   17403 C  CG    . GLU A 1 3737 ? 163.316 198.287 198.115 1.00 69.36  ? 3737 GLU A CG    1 
ATOM   17404 C  CD    . GLU A 1 3737 ? 163.439 197.955 196.643 1.00 74.60  ? 3737 GLU A CD    1 
ATOM   17405 O  OE1   . GLU A 1 3737 ? 163.236 196.778 196.282 1.00 70.96  ? 3737 GLU A OE1   1 
ATOM   17406 O  OE2   . GLU A 1 3737 ? 163.739 198.869 195.847 1.00 73.88  ? 3737 GLU A OE2   1 
ATOM   17407 N  N     . PHE A 1 3738 ? 161.264 199.403 201.217 1.00 73.31  ? 3738 PHE A N     1 
ATOM   17408 C  CA    . PHE A 1 3738 ? 161.320 200.612 202.032 1.00 77.82  ? 3738 PHE A CA    1 
ATOM   17409 C  C     . PHE A 1 3738 ? 161.733 200.285 203.459 1.00 82.47  ? 3738 PHE A C     1 
ATOM   17410 O  O     . PHE A 1 3738 ? 162.578 200.973 204.041 1.00 88.15  ? 3738 PHE A O     1 
ATOM   17411 C  CB    . PHE A 1 3738 ? 159.969 201.327 202.021 1.00 80.08  ? 3738 PHE A CB    1 
ATOM   17412 C  CG    . PHE A 1 3738 ? 159.679 202.058 200.743 1.00 78.80  ? 3738 PHE A CG    1 
ATOM   17413 C  CD1   . PHE A 1 3738 ? 160.662 202.805 200.118 1.00 79.11  ? 3738 PHE A CD1   1 
ATOM   17414 C  CD2   . PHE A 1 3738 ? 158.420 202.009 200.173 1.00 71.20  ? 3738 PHE A CD2   1 
ATOM   17415 C  CE1   . PHE A 1 3738 ? 160.396 203.480 198.944 1.00 73.63  ? 3738 PHE A CE1   1 
ATOM   17416 C  CE2   . PHE A 1 3738 ? 158.150 202.683 199.000 1.00 69.63  ? 3738 PHE A CE2   1 
ATOM   17417 C  CZ    . PHE A 1 3738 ? 159.139 203.418 198.385 1.00 70.13  ? 3738 PHE A CZ    1 
ATOM   17418 N  N     . GLN A 1 3739 ? 161.156 199.228 204.035 1.00 77.27  ? 3739 GLN A N     1 
ATOM   17419 C  CA    . GLN A 1 3739 ? 161.554 198.808 205.374 1.00 80.75  ? 3739 GLN A CA    1 
ATOM   17420 C  C     . GLN A 1 3739 ? 162.994 198.312 205.393 1.00 85.37  ? 3739 GLN A C     1 
ATOM   17421 O  O     . GLN A 1 3739 ? 163.701 198.485 206.392 1.00 92.79  ? 3739 GLN A O     1 
ATOM   17422 C  CB    . GLN A 1 3739 ? 160.602 197.731 205.894 1.00 79.72  ? 3739 GLN A CB    1 
ATOM   17423 C  CG    . GLN A 1 3739 ? 159.163 198.199 206.072 1.00 79.81  ? 3739 GLN A CG    1 
ATOM   17424 C  CD    . GLN A 1 3739 ? 158.357 198.138 204.788 1.00 78.88  ? 3739 GLN A CD    1 
ATOM   17425 O  OE1   . GLN A 1 3739 ? 158.909 197.964 203.703 1.00 76.19  ? 3739 GLN A OE1   1 
ATOM   17426 N  NE2   . GLN A 1 3739 ? 157.043 198.284 204.908 1.00 69.88  ? 3739 GLN A NE2   1 
ATOM   17427 N  N     . LEU A 1 3740 ? 163.452 197.697 204.298 1.00 82.09  ? 3740 LEU A N     1 
ATOM   17428 C  CA    . LEU A 1 3740 ? 164.845 197.266 204.227 1.00 84.77  ? 3740 LEU A CA    1 
ATOM   17429 C  C     . LEU A 1 3740 ? 165.794 198.453 204.309 1.00 91.79  ? 3740 LEU A C     1 
ATOM   17430 O  O     . LEU A 1 3740 ? 166.750 198.442 205.093 1.00 94.58  ? 3740 LEU A O     1 
ATOM   17431 C  CB    . LEU A 1 3740 ? 165.090 196.478 202.941 1.00 83.96  ? 3740 LEU A CB    1 
ATOM   17432 C  CG    . LEU A 1 3740 ? 166.242 195.475 202.967 1.00 92.65  ? 3740 LEU A CG    1 
ATOM   17433 C  CD1   . LEU A 1 3740 ? 165.851 194.238 203.759 1.00 92.97  ? 3740 LEU A CD1   1 
ATOM   17434 C  CD2   . LEU A 1 3740 ? 166.658 195.102 201.553 1.00 87.96  ? 3740 LEU A CD2   1 
ATOM   17435 N  N     . ARG A 1 3741 ? 165.540 199.497 203.516 1.00 92.88  ? 3741 ARG A N     1 
ATOM   17436 C  CA    . ARG A 1 3741 ? 166.403 200.673 203.574 1.00 91.59  ? 3741 ARG A CA    1 
ATOM   17437 C  C     . ARG A 1 3741 ? 166.247 201.408 204.900 1.00 91.93  ? 3741 ARG A C     1 
ATOM   17438 O  O     . ARG A 1 3741 ? 167.211 201.991 205.414 1.00 100.00 ? 3741 ARG A O     1 
ATOM   17439 C  CB    . ARG A 1 3741 ? 166.114 201.599 202.393 1.00 91.13  ? 3741 ARG A CB    1 
ATOM   17440 C  CG    . ARG A 1 3741 ? 166.709 201.102 201.081 1.00 92.96  ? 3741 ARG A CG    1 
ATOM   17441 C  CD    . ARG A 1 3741 ? 165.746 201.254 199.915 1.00 93.60  ? 3741 ARG A CD    1 
ATOM   17442 N  NE    . ARG A 1 3741 ? 165.287 202.628 199.756 1.00 100.52 ? 3741 ARG A NE    1 
ATOM   17443 C  CZ    . ARG A 1 3741 ? 164.438 203.030 198.819 1.00 94.43  ? 3741 ARG A CZ    1 
ATOM   17444 N  NH1   . ARG A 1 3741 ? 163.937 202.186 197.932 1.00 82.16  ? 3741 ARG A NH1   1 
ATOM   17445 N  NH2   . ARG A 1 3741 ? 164.085 204.311 198.770 1.00 89.68  ? 3741 ARG A NH2   1 
ATOM   17446 N  N     . LEU A 1 3742 ? 165.046 201.375 205.483 1.00 86.70  ? 3742 LEU A N     1 
ATOM   17447 C  CA    . LEU A 1 3742 ? 164.842 201.987 206.791 1.00 89.73  ? 3742 LEU A CA    1 
ATOM   17448 C  C     . LEU A 1 3742 ? 165.680 201.297 207.860 1.00 99.21  ? 3742 LEU A C     1 
ATOM   17449 O  O     . LEU A 1 3742 ? 166.321 201.962 208.682 1.00 106.76 ? 3742 LEU A O     1 
ATOM   17450 C  CB    . LEU A 1 3742 ? 163.360 201.945 207.160 1.00 85.98  ? 3742 LEU A CB    1 
ATOM   17451 C  CG    . LEU A 1 3742 ? 162.882 202.947 208.211 1.00 93.23  ? 3742 LEU A CG    1 
ATOM   17452 C  CD1   . LEU A 1 3742 ? 163.277 204.362 207.822 1.00 99.00  ? 3742 LEU A CD1   1 
ATOM   17453 C  CD2   . LEU A 1 3742 ? 161.379 202.839 208.404 1.00 93.76  ? 3742 LEU A CD2   1 
ATOM   17454 N  N     . ARG A 1 3743 ? 165.705 199.963 207.859 1.00 97.95  ? 3743 ARG A N     1 
ATOM   17455 C  CA    . ARG A 1 3743 ? 166.510 199.259 208.852 1.00 99.81  ? 3743 ARG A CA    1 
ATOM   17456 C  C     . ARG A 1 3743 ? 167.998 199.364 208.541 1.00 104.75 ? 3743 ARG A C     1 
ATOM   17457 O  O     . ARG A 1 3743 ? 168.823 199.304 209.458 1.00 111.86 ? 3743 ARG A O     1 
ATOM   17458 C  CB    . ARG A 1 3743 ? 166.076 197.796 208.961 1.00 96.54  ? 3743 ARG A CB    1 
ATOM   17459 C  CG    . ARG A 1 3743 ? 166.478 196.915 207.796 1.00 100.34 ? 3743 ARG A CG    1 
ATOM   17460 C  CD    . ARG A 1 3743 ? 165.728 195.593 207.834 1.00 106.45 ? 3743 ARG A CD    1 
ATOM   17461 N  NE    . ARG A 1 3743 ? 164.295 195.769 207.627 1.00 108.06 ? 3743 ARG A NE    1 
ATOM   17462 C  CZ    . ARG A 1 3743 ? 163.364 195.450 208.515 1.00 99.89  ? 3743 ARG A CZ    1 
ATOM   17463 N  NH1   . ARG A 1 3743 ? 163.679 194.944 209.696 1.00 100.13 ? 3743 ARG A NH1   1 
ATOM   17464 N  NH2   . ARG A 1 3743 ? 162.084 195.643 208.210 1.00 89.62  ? 3743 ARG A NH2   1 
ATOM   17465 N  N     . GLN A 1 3744 ? 168.365 199.538 207.269 1.00 100.58 ? 3744 GLN A N     1 
ATOM   17466 C  CA    . GLN A 1 3744 ? 169.764 199.821 206.955 1.00 99.18  ? 3744 GLN A CA    1 
ATOM   17467 C  C     . GLN A 1 3744 ? 170.197 201.164 207.532 1.00 104.51 ? 3744 GLN A C     1 
ATOM   17468 O  O     . GLN A 1 3744 ? 171.291 201.282 208.099 1.00 109.75 ? 3744 GLN A O     1 
ATOM   17469 C  CB    . GLN A 1 3744 ? 169.985 199.784 205.445 1.00 96.44  ? 3744 GLN A CB    1 
ATOM   17470 C  CG    . GLN A 1 3744 ? 169.915 198.389 204.852 1.00 98.73  ? 3744 GLN A CG    1 
ATOM   17471 C  CD    . GLN A 1 3744 ? 170.893 198.189 203.716 1.00 100.59 ? 3744 GLN A CD    1 
ATOM   17472 O  OE1   . GLN A 1 3744 ? 171.219 199.128 202.990 1.00 103.25 ? 3744 GLN A OE1   1 
ATOM   17473 N  NE2   . GLN A 1 3744 ? 171.367 196.960 203.554 1.00 94.73  ? 3744 GLN A NE2   1 
ATOM   17474 N  N     . LEU A 1 3745 ? 169.348 202.188 207.407 1.00 108.02 ? 3745 LEU A N     1 
ATOM   17475 C  CA    . LEU A 1 3745 ? 169.653 203.464 208.048 1.00 113.67 ? 3745 LEU A CA    1 
ATOM   17476 C  C     . LEU A 1 3745 ? 169.632 203.346 209.566 1.00 114.84 ? 3745 LEU A C     1 
ATOM   17477 O  O     . LEU A 1 3745 ? 170.384 204.045 210.250 1.00 119.21 ? 3745 LEU A O     1 
ATOM   17478 C  CB    . LEU A 1 3745 ? 168.679 204.546 207.587 1.00 110.55 ? 3745 LEU A CB    1 
ATOM   17479 C  CG    . LEU A 1 3745 ? 168.732 204.903 206.103 1.00 112.49 ? 3745 LEU A CG    1 
ATOM   17480 C  CD1   . LEU A 1 3745 ? 167.940 206.167 205.848 1.00 114.03 ? 3745 LEU A CD1   1 
ATOM   17481 C  CD2   . LEU A 1 3745 ? 170.170 205.062 205.634 1.00 110.82 ? 3745 LEU A CD2   1 
ATOM   17482 N  N     . GLU A 1 3746 ? 168.780 202.475 210.107 1.00 111.03 ? 3746 GLU A N     1 
ATOM   17483 C  CA    . GLU A 1 3746 ? 168.802 202.200 211.541 1.00 115.06 ? 3746 GLU A CA    1 
ATOM   17484 C  C     . GLU A 1 3746 ? 170.148 201.620 211.966 1.00 118.30 ? 3746 GLU A C     1 
ATOM   17485 O  O     . GLU A 1 3746 ? 170.716 202.013 212.992 1.00 120.96 ? 3746 GLU A O     1 
ATOM   17486 C  CB    . GLU A 1 3746 ? 167.659 201.246 211.893 1.00 115.92 ? 3746 GLU A CB    1 
ATOM   17487 C  CG    . GLU A 1 3746 ? 167.355 201.121 213.373 1.00 119.30 ? 3746 GLU A CG    1 
ATOM   17488 C  CD    . GLU A 1 3746 ? 168.224 200.089 214.066 1.00 122.52 ? 3746 GLU A CD    1 
ATOM   17489 O  OE1   . GLU A 1 3746 ? 168.792 199.222 213.370 1.00 119.70 ? 3746 GLU A OE1   1 
ATOM   17490 O  OE2   . GLU A 1 3746 ? 168.333 200.139 215.308 1.00 119.32 ? 3746 GLU A OE2   1 
ATOM   17491 N  N     . LYS A 1 3747 ? 170.670 200.677 211.181 1.00 115.64 ? 3747 LYS A N     1 
ATOM   17492 C  CA    . LYS A 1 3747 ? 171.979 200.101 211.469 1.00 118.42 ? 3747 LYS A CA    1 
ATOM   17493 C  C     . LYS A 1 3747 ? 173.076 201.153 211.369 1.00 121.75 ? 3747 LYS A C     1 
ATOM   17494 O  O     . LYS A 1 3747 ? 174.003 201.176 212.188 1.00 124.48 ? 3747 LYS A O     1 
ATOM   17495 C  CB    . LYS A 1 3747 ? 172.260 198.941 210.515 1.00 112.97 ? 3747 LYS A CB    1 
ATOM   17496 C  CG    . LYS A 1 3747 ? 173.291 197.949 211.023 1.00 113.02 ? 3747 LYS A CG    1 
ATOM   17497 C  CD    . LYS A 1 3747 ? 173.601 196.893 209.974 1.00 109.00 ? 3747 LYS A CD    1 
ATOM   17498 C  CE    . LYS A 1 3747 ? 172.330 196.324 209.365 1.00 102.19 ? 3747 LYS A CE    1 
ATOM   17499 N  NZ    . LYS A 1 3747 ? 172.592 195.639 208.069 1.00 96.36  ? 3747 LYS A NZ    1 
ATOM   17500 N  N     . SER A 1 3748 ? 172.991 202.028 210.365 1.00 119.29 ? 3748 SER A N     1 
ATOM   17501 C  CA    . SER A 1 3748 ? 173.973 203.102 210.237 1.00 118.23 ? 3748 SER A CA    1 
ATOM   17502 C  C     . SER A 1 3748 ? 173.916 204.049 211.431 1.00 119.54 ? 3748 SER A C     1 
ATOM   17503 O  O     . SER A 1 3748 ? 174.956 204.494 211.932 1.00 122.17 ? 3748 SER A O     1 
ATOM   17504 C  CB    . SER A 1 3748 ? 173.749 203.867 208.933 1.00 116.66 ? 3748 SER A CB    1 
ATOM   17505 O  OG    . SER A 1 3748 ? 173.850 203.005 207.813 1.00 118.40 ? 3748 SER A OG    1 
ATOM   17506 N  N     . LEU A 1 3749 ? 172.707 204.371 211.898 1.00 117.98 ? 3749 LEU A N     1 
ATOM   17507 C  CA    . LEU A 1 3749 ? 172.568 205.224 213.073 1.00 120.65 ? 3749 LEU A CA    1 
ATOM   17508 C  C     . LEU A 1 3749 ? 173.139 204.548 214.311 1.00 127.37 ? 3749 LEU A C     1 
ATOM   17509 O  O     . LEU A 1 3749 ? 173.774 205.205 215.140 1.00 131.26 ? 3749 LEU A O     1 
ATOM   17510 C  CB    . LEU A 1 3749 ? 171.099 205.601 213.283 1.00 118.65 ? 3749 LEU A CB    1 
ATOM   17511 C  CG    . LEU A 1 3749 ? 170.757 206.638 214.362 1.00 121.01 ? 3749 LEU A CG    1 
ATOM   17512 C  CD1   . LEU A 1 3749 ? 169.471 207.354 214.002 1.00 127.49 ? 3749 LEU A CD1   1 
ATOM   17513 C  CD2   . LEU A 1 3749 ? 170.616 206.012 215.741 1.00 120.19 ? 3749 LEU A CD2   1 
ATOM   17514 N  N     . LEU A 1 3750 ? 172.912 203.242 214.464 1.00 126.05 ? 3750 LEU A N     1 
ATOM   17515 C  CA    . LEU A 1 3750 ? 173.502 202.526 215.593 1.00 128.97 ? 3750 LEU A CA    1 
ATOM   17516 C  C     . LEU A 1 3750 ? 175.024 202.544 215.521 1.00 132.38 ? 3750 LEU A C     1 
ATOM   17517 O  O     . LEU A 1 3750 ? 175.701 202.729 216.540 1.00 133.72 ? 3750 LEU A O     1 
ATOM   17518 C  CB    . LEU A 1 3750 ? 172.988 201.088 215.639 1.00 125.39 ? 3750 LEU A CB    1 
ATOM   17519 C  CG    . LEU A 1 3750 ? 171.612 200.864 216.266 1.00 125.26 ? 3750 LEU A CG    1 
ATOM   17520 C  CD1   . LEU A 1 3750 ? 171.345 199.377 216.420 1.00 120.54 ? 3750 LEU A CD1   1 
ATOM   17521 C  CD2   . LEU A 1 3750 ? 171.505 201.575 217.605 1.00 122.28 ? 3750 LEU A CD2   1 
ATOM   17522 N  N     . GLN A 1 3751 ? 175.579 202.351 214.322 1.00 128.09 ? 3751 GLN A N     1 
ATOM   17523 C  CA    . GLN A 1 3751 ? 177.028 202.399 214.159 1.00 126.10 ? 3751 GLN A CA    1 
ATOM   17524 C  C     . GLN A 1 3751 ? 177.577 203.774 214.520 1.00 129.57 ? 3751 GLN A C     1 
ATOM   17525 O  O     . GLN A 1 3751 ? 178.606 203.882 215.198 1.00 131.67 ? 3751 GLN A O     1 
ATOM   17526 C  CB    . GLN A 1 3751 ? 177.403 202.021 212.724 1.00 120.91 ? 3751 GLN A CB    1 
ATOM   17527 C  CG    . GLN A 1 3751 ? 178.889 202.120 212.402 1.00 125.56 ? 3751 GLN A CG    1 
ATOM   17528 C  CD    . GLN A 1 3751 ? 179.302 203.508 211.949 1.00 127.56 ? 3751 GLN A CD    1 
ATOM   17529 O  OE1   . GLN A 1 3751 ? 178.774 204.037 210.972 1.00 128.41 ? 3751 GLN A OE1   1 
ATOM   17530 N  NE2   . GLN A 1 3751 ? 180.246 204.107 212.665 1.00 124.36 ? 3751 GLN A NE2   1 
ATOM   17531 N  N     . ALA A 1 3752 ? 176.904 204.838 214.075 1.00 127.68 ? 3752 ALA A N     1 
ATOM   17532 C  CA    . ALA A 1 3752 ? 177.339 206.186 214.425 1.00 126.55 ? 3752 ALA A CA    1 
ATOM   17533 C  C     . ALA A 1 3752 ? 177.197 206.450 215.918 1.00 131.26 ? 3752 ALA A C     1 
ATOM   17534 O  O     . ALA A 1 3752 ? 178.029 207.150 216.507 1.00 135.40 ? 3752 ALA A O     1 
ATOM   17535 C  CB    . ALA A 1 3752 ? 176.550 207.221 213.625 1.00 121.93 ? 3752 ALA A CB    1 
ATOM   17536 N  N     . LEU A 1 3753 ? 176.154 205.904 216.542 1.00 128.59 ? 3753 LEU A N     1 
ATOM   17537 C  CA    . LEU A 1 3753 ? 175.928 206.040 217.972 1.00 130.94 ? 3753 LEU A CA    1 
ATOM   17538 C  C     . LEU A 1 3753 ? 176.887 205.197 218.799 1.00 137.23 ? 3753 LEU A C     1 
ATOM   17539 O  O     . LEU A 1 3753 ? 176.980 205.405 220.012 1.00 137.36 ? 3753 LEU A O     1 
ATOM   17540 C  CB    . LEU A 1 3753 ? 174.481 205.656 218.297 1.00 131.25 ? 3753 LEU A CB    1 
ATOM   17541 C  CG    . LEU A 1 3753 ? 173.865 206.111 219.620 1.00 139.50 ? 3753 LEU A CG    1 
ATOM   17542 C  CD1   . LEU A 1 3753 ? 173.510 207.587 219.563 1.00 135.24 ? 3753 LEU A CD1   1 
ATOM   17543 C  CD2   . LEU A 1 3753 ? 172.635 205.276 219.934 1.00 136.95 ? 3753 LEU A CD2   1 
ATOM   17544 N  N     . ASN A 1 3754 ? 177.582 204.241 218.180 1.00 138.02 ? 3754 ASN A N     1 
ATOM   17545 C  CA    . ASN A 1 3754 ? 178.608 203.496 218.904 1.00 138.68 ? 3754 ASN A CA    1 
ATOM   17546 C  C     . ASN A 1 3754 ? 179.787 204.390 219.265 1.00 142.46 ? 3754 ASN A C     1 
ATOM   17547 O  O     . ASN A 1 3754 ? 180.334 204.291 220.370 1.00 142.37 ? 3754 ASN A O     1 
ATOM   17548 C  CB    . ASN A 1 3754 ? 179.073 202.300 218.075 1.00 134.23 ? 3754 ASN A CB    1 
ATOM   17549 C  CG    . ASN A 1 3754 ? 180.209 201.545 218.733 1.00 136.00 ? 3754 ASN A CG    1 
ATOM   17550 O  OD1   . ASN A 1 3754 ? 181.290 201.406 218.161 1.00 134.77 ? 3754 ASN A OD1   1 
ATOM   17551 N  ND2   . ASN A 1 3754 ? 179.971 201.056 219.944 1.00 137.19 ? 3754 ASN A ND2   1 
ATOM   17552 N  N     . GLU A 1 3755 ? 180.190 205.270 218.348 1.00 142.30 ? 3755 GLU A N     1 
ATOM   17553 C  CA    . GLU A 1 3755 ? 181.319 206.173 218.568 1.00 143.20 ? 3755 GLU A CA    1 
ATOM   17554 C  C     . GLU A 1 3755 ? 180.797 207.461 219.201 1.00 144.80 ? 3755 GLU A C     1 
ATOM   17555 O  O     . GLU A 1 3755 ? 180.601 208.487 218.546 1.00 142.26 ? 3755 GLU A O     1 
ATOM   17556 C  CB    . GLU A 1 3755 ? 182.049 206.437 217.257 1.00 142.18 ? 3755 GLU A CB    1 
ATOM   17557 C  CG    . GLU A 1 3755 ? 183.393 207.128 217.414 1.00 147.57 ? 3755 GLU A CG    1 
ATOM   17558 C  CD    . GLU A 1 3755 ? 183.325 208.611 217.110 1.00 148.92 ? 3755 GLU A CD    1 
ATOM   17559 O  OE1   . GLU A 1 3755 ? 182.510 209.008 216.251 1.00 145.82 ? 3755 GLU A OE1   1 
ATOM   17560 O  OE2   . GLU A 1 3755 ? 184.088 209.380 217.731 1.00 148.65 ? 3755 GLU A OE2   1 
ATOM   17561 N  N     . VAL A 1 3756 ? 180.566 207.397 220.512 1.00 147.39 ? 3756 VAL A N     1 
ATOM   17562 C  CA    . VAL A 1 3756 ? 180.044 208.527 221.283 1.00 147.56 ? 3756 VAL A CA    1 
ATOM   17563 C  C     . VAL A 1 3756 ? 180.978 208.735 222.474 1.00 145.82 ? 3756 VAL A C     1 
ATOM   17564 O  O     . VAL A 1 3756 ? 180.869 208.061 223.503 1.00 145.33 ? 3756 VAL A O     1 
ATOM   17565 C  CB    . VAL A 1 3756 ? 178.594 208.320 221.733 1.00 148.29 ? 3756 VAL A CB    1 
ATOM   17566 C  CG1   . VAL A 1 3756 ? 177.652 208.522 220.560 1.00 144.23 ? 3756 VAL A CG1   1 
ATOM   17567 C  CG2   . VAL A 1 3756 ? 178.396 206.925 222.317 1.00 144.60 ? 3756 VAL A CG2   1 
ATOM   17568 N  N     . LYS A 1 3757 ? 181.915 209.674 222.336 1.00 146.45 ? 3757 LYS A N     1 
ATOM   17569 C  CA    . LYS A 1 3757 ? 182.791 210.041 223.447 1.00 149.17 ? 3757 LYS A CA    1 
ATOM   17570 C  C     . LYS A 1 3757 ? 183.267 211.469 223.186 1.00 149.87 ? 3757 LYS A C     1 
ATOM   17571 O  O     . LYS A 1 3757 ? 184.189 211.679 222.393 1.00 149.24 ? 3757 LYS A O     1 
ATOM   17572 C  CB    . LYS A 1 3757 ? 183.957 209.075 223.578 1.00 150.33 ? 3757 LYS A CB    1 
ATOM   17573 C  CG    . LYS A 1 3757 ? 184.941 209.445 224.674 1.00 146.02 ? 3757 LYS A CG    1 
ATOM   17574 C  CD    . LYS A 1 3757 ? 184.243 209.572 226.017 1.00 140.45 ? 3757 LYS A CD    1 
ATOM   17575 C  CE    . LYS A 1 3757 ? 185.191 210.097 227.080 1.00 138.93 ? 3757 LYS A CE    1 
ATOM   17576 N  NZ    . LYS A 1 3757 ? 185.741 211.430 226.711 1.00 139.60 ? 3757 LYS A NZ    1 
ATOM   17577 N  N     . GLY A 1 3758 ? 182.634 212.429 223.845 1.00 149.54 ? 3758 GLY A N     1 
ATOM   17578 C  CA    . GLY A 1 3758 ? 182.952 213.836 223.606 1.00 150.58 ? 3758 GLY A CA    1 
ATOM   17579 C  C     . GLY A 1 3758 ? 182.397 214.387 222.313 1.00 152.52 ? 3758 GLY A C     1 
ATOM   17580 O  O     . GLY A 1 3758 ? 181.803 215.469 222.303 1.00 152.51 ? 3758 GLY A O     1 
ATOM   17581 N  N     . ARG A 1 3759 ? 182.575 213.659 221.209 1.00 154.20 ? 3759 ARG A N     1 
ATOM   17582 C  CA    . ARG A 1 3759 ? 182.066 214.085 219.912 1.00 154.58 ? 3759 ARG A CA    1 
ATOM   17583 C  C     . ARG A 1 3759 ? 180.547 214.027 219.824 1.00 155.23 ? 3759 ARG A C     1 
ATOM   17584 O  O     . ARG A 1 3759 ? 179.983 214.526 218.845 1.00 154.45 ? 3759 ARG A O     1 
ATOM   17585 C  CB    . ARG A 1 3759 ? 182.685 213.228 218.806 1.00 150.64 ? 3759 ARG A CB    1 
ATOM   17586 C  CG    . ARG A 1 3759 ? 184.183 213.421 218.650 1.00 145.46 ? 3759 ARG A CG    1 
ATOM   17587 C  CD    . ARG A 1 3759 ? 184.754 212.511 217.579 1.00 144.16 ? 3759 ARG A CD    1 
ATOM   17588 N  NE    . ARG A 1 3759 ? 186.194 212.682 217.432 1.00 144.61 ? 3759 ARG A NE    1 
ATOM   17589 C  CZ    . ARG A 1 3759 ? 186.953 211.975 216.607 1.00 143.30 ? 3759 ARG A CZ    1 
ATOM   17590 N  NH1   . ARG A 1 3759 ? 186.441 211.031 215.835 1.00 144.55 ? 3759 ARG A NH1   1 
ATOM   17591 N  NH2   . ARG A 1 3759 ? 188.259 212.220 216.555 1.00 142.92 ? 3759 ARG A NH2   1 
ATOM   17592 N  N     . ILE A 1 3760 ? 179.876 213.417 220.802 1.00 154.46 ? 3760 ILE A N     1 
ATOM   17593 C  CA    . ILE A 1 3760 ? 178.417 213.442 220.820 1.00 154.26 ? 3760 ILE A CA    1 
ATOM   17594 C  C     . ILE A 1 3760 ? 177.907 214.857 221.068 1.00 156.24 ? 3760 ILE A C     1 
ATOM   17595 O  O     . ILE A 1 3760 ? 176.873 215.262 220.523 1.00 156.49 ? 3760 ILE A O     1 
ATOM   17596 C  CB    . ILE A 1 3760 ? 177.870 212.438 221.854 1.00 149.09 ? 3760 ILE A CB    1 
ATOM   17597 C  CG1   . ILE A 1 3760 ? 176.352 212.302 221.711 1.00 146.19 ? 3760 ILE A CG1   1 
ATOM   17598 C  CG2   . ILE A 1 3760 ? 178.264 212.832 223.274 1.00 146.93 ? 3760 ILE A CG2   1 
ATOM   17599 C  CD1   . ILE A 1 3760 ? 175.912 211.709 220.393 1.00 144.43 ? 3760 ILE A CD1   1 
ATOM   17600 N  N     . LEU A 1 3761 ? 178.621 215.635 221.885 1.00 154.20 ? 3761 LEU A N     1 
ATOM   17601 C  CA    . LEU A 1 3761 ? 178.236 217.011 222.180 1.00 151.42 ? 3761 LEU A CA    1 
ATOM   17602 C  C     . LEU A 1 3761 ? 179.301 218.017 221.754 1.00 153.86 ? 3761 LEU A C     1 
ATOM   17603 O  O     . LEU A 1 3761 ? 179.315 219.143 222.260 1.00 153.15 ? 3761 LEU A O     1 
ATOM   17604 C  CB    . LEU A 1 3761 ? 177.922 217.182 223.668 1.00 149.87 ? 3761 LEU A CB    1 
ATOM   17605 C  CG    . LEU A 1 3761 ? 176.908 216.250 224.335 1.00 147.54 ? 3761 LEU A CG    1 
ATOM   17606 C  CD1   . LEU A 1 3761 ? 176.478 216.827 225.674 1.00 140.51 ? 3761 LEU A CD1   1 
ATOM   17607 C  CD2   . LEU A 1 3761 ? 175.698 216.015 223.448 1.00 147.43 ? 3761 LEU A CD2   1 
ATOM   17608 N  N     . ASP A 1 3762 ? 180.202 217.636 220.844 1.00 157.59 ? 3762 ASP A N     1 
ATOM   17609 C  CA    . ASP A 1 3762 ? 181.154 218.609 220.315 1.00 159.98 ? 3762 ASP A CA    1 
ATOM   17610 C  C     . ASP A 1 3762 ? 180.428 219.720 219.570 1.00 161.49 ? 3762 ASP A C     1 
ATOM   17611 O  O     . ASP A 1 3762 ? 180.755 220.903 219.722 1.00 160.71 ? 3762 ASP A O     1 
ATOM   17612 C  CB    . ASP A 1 3762 ? 182.174 217.917 219.407 1.00 157.74 ? 3762 ASP A CB    1 
ATOM   17613 C  CG    . ASP A 1 3762 ? 181.528 217.193 218.238 1.00 158.40 ? 3762 ASP A CG    1 
ATOM   17614 O  OD1   . ASP A 1 3762 ? 180.281 217.158 218.166 1.00 156.82 ? 3762 ASP A OD1   1 
ATOM   17615 O  OD2   . ASP A 1 3762 ? 182.270 216.659 217.387 1.00 156.39 ? 3762 ASP A OD2   1 
ATOM   17616 N  N     . ASP A 1 3763 ? 179.434 219.353 218.759 1.00 159.69 ? 3763 ASP A N     1 
ATOM   17617 C  CA    . ASP A 1 3763 ? 178.491 220.299 218.186 1.00 158.67 ? 3763 ASP A CA    1 
ATOM   17618 C  C     . ASP A 1 3763 ? 177.075 220.099 218.698 1.00 156.33 ? 3763 ASP A C     1 
ATOM   17619 O  O     . ASP A 1 3763 ? 176.263 221.024 218.595 1.00 154.46 ? 3763 ASP A O     1 
ATOM   17620 C  CB    . ASP A 1 3763 ? 178.486 220.191 216.654 1.00 157.58 ? 3763 ASP A CB    1 
ATOM   17621 C  CG    . ASP A 1 3763 ? 179.879 220.036 216.075 1.00 156.35 ? 3763 ASP A CG    1 
ATOM   17622 O  OD1   . ASP A 1 3763 ? 180.705 220.955 216.256 1.00 157.18 ? 3763 ASP A OD1   1 
ATOM   17623 O  OD2   . ASP A 1 3763 ? 180.148 218.994 215.440 1.00 153.38 ? 3763 ASP A OD2   1 
ATOM   17624 N  N     . ASP A 1 3764 ? 176.768 218.920 219.247 1.00 155.59 ? 3764 ASP A N     1 
ATOM   17625 C  CA    . ASP A 1 3764 ? 175.435 218.586 219.752 1.00 155.98 ? 3764 ASP A CA    1 
ATOM   17626 C  C     . ASP A 1 3764 ? 174.373 218.758 218.671 1.00 155.73 ? 3764 ASP A C     1 
ATOM   17627 O  O     . ASP A 1 3764 ? 173.221 219.097 218.955 1.00 153.09 ? 3764 ASP A O     1 
ATOM   17628 C  CB    . ASP A 1 3764 ? 175.090 219.409 220.996 1.00 152.05 ? 3764 ASP A CB    1 
ATOM   17629 C  CG    . ASP A 1 3764 ? 174.108 218.701 221.909 1.00 151.50 ? 3764 ASP A CG    1 
ATOM   17630 O  OD1   . ASP A 1 3764 ? 173.489 217.710 221.468 1.00 152.07 ? 3764 ASP A OD1   1 
ATOM   17631 O  OD2   . ASP A 1 3764 ? 173.954 219.136 223.069 1.00 150.07 ? 3764 ASP A OD2   1 
ATOM   17632 N  N     . THR A 1 3765 ? 174.760 218.524 217.417 1.00 154.48 ? 3765 THR A N     1 
ATOM   17633 C  CA    . THR A 1 3765 ? 173.855 218.606 216.279 1.00 148.81 ? 3765 THR A CA    1 
ATOM   17634 C  C     . THR A 1 3765 ? 173.751 217.281 215.532 1.00 146.87 ? 3765 THR A C     1 
ATOM   17635 O  O     . THR A 1 3765 ? 173.344 217.259 214.366 1.00 145.45 ? 3765 THR A O     1 
ATOM   17636 C  CB    . THR A 1 3765 ? 174.296 219.717 215.325 1.00 149.85 ? 3765 THR A CB    1 
ATOM   17637 O  OG1   . THR A 1 3765 ? 175.645 219.482 214.904 1.00 150.42 ? 3765 THR A OG1   1 
ATOM   17638 C  CG2   . THR A 1 3765 ? 174.211 221.073 216.011 1.00 147.21 ? 3765 THR A CG2   1 
ATOM   17639 N  N     . ILE A 1 3766 ? 174.116 216.174 216.182 1.00 148.70 ? 3766 ILE A N     1 
ATOM   17640 C  CA    . ILE A 1 3766 ? 173.997 214.856 215.577 1.00 149.23 ? 3766 ILE A CA    1 
ATOM   17641 C  C     . ILE A 1 3766 ? 172.551 214.496 215.272 1.00 146.00 ? 3766 ILE A C     1 
ATOM   17642 O  O     . ILE A 1 3766 ? 172.295 213.713 214.346 1.00 141.68 ? 3766 ILE A O     1 
ATOM   17643 C  CB    . ILE A 1 3766 ? 174.649 213.792 216.492 1.00 145.36 ? 3766 ILE A CB    1 
ATOM   17644 C  CG1   . ILE A 1 3766 ? 174.851 212.476 215.737 1.00 138.02 ? 3766 ILE A CG1   1 
ATOM   17645 C  CG2   . ILE A 1 3766 ? 173.821 213.578 217.754 1.00 138.81 ? 3766 ILE A CG2   1 
ATOM   17646 C  CD1   . ILE A 1 3766 ? 175.679 212.616 214.478 1.00 130.77 ? 3766 ILE A CD1   1 
ATOM   17647 N  N     . ILE A 1 3767 ? 171.597 215.091 215.995 1.00 147.07 ? 3767 ILE A N     1 
ATOM   17648 C  CA    . ILE A 1 3767 ? 170.180 214.802 215.831 1.00 143.06 ? 3767 ILE A CA    1 
ATOM   17649 C  C     . ILE A 1 3767 ? 169.746 214.823 214.377 1.00 139.64 ? 3767 ILE A C     1 
ATOM   17650 O  O     . ILE A 1 3767 ? 168.765 214.158 214.025 1.00 138.61 ? 3767 ILE A O     1 
ATOM   17651 C  CB    . ILE A 1 3767 ? 169.332 215.803 216.646 1.00 144.30 ? 3767 ILE A CB    1 
ATOM   17652 C  CG1   . ILE A 1 3767 ? 169.302 217.172 215.964 1.00 144.78 ? 3767 ILE A CG1   1 
ATOM   17653 C  CG2   . ILE A 1 3767 ? 169.907 215.966 218.031 1.00 142.09 ? 3767 ILE A CG2   1 
ATOM   17654 C  CD1   . ILE A 1 3767 ? 168.280 218.122 216.546 1.00 141.69 ? 3767 ILE A CD1   1 
ATOM   17655 N  N     . THR A 1 3768 ? 170.481 215.541 213.521 1.00 139.93 ? 3768 THR A N     1 
ATOM   17656 C  CA    . THR A 1 3768 ? 170.141 215.609 212.106 1.00 143.65 ? 3768 THR A CA    1 
ATOM   17657 C  C     . THR A 1 3768 ? 169.943 214.220 211.523 1.00 141.24 ? 3768 THR A C     1 
ATOM   17658 O  O     . THR A 1 3768 ? 168.901 213.942 210.913 1.00 138.12 ? 3768 THR A O     1 
ATOM   17659 C  CB    . THR A 1 3768 ? 171.233 216.357 211.339 1.00 145.43 ? 3768 THR A CB    1 
ATOM   17660 O  OG1   . THR A 1 3768 ? 171.413 217.660 211.907 1.00 146.89 ? 3768 THR A OG1   1 
ATOM   17661 C  CG2   . THR A 1 3768 ? 170.858 216.492 209.870 1.00 144.92 ? 3768 THR A CG2   1 
ATOM   17662 N  N     . THR A 1 3769 ? 170.901 213.313 211.749 1.00 138.77 ? 3769 THR A N     1 
ATOM   17663 C  CA    . THR A 1 3769 ? 170.747 211.973 211.192 1.00 133.89 ? 3769 THR A CA    1 
ATOM   17664 C  C     . THR A 1 3769 ? 169.468 211.322 211.703 1.00 133.96 ? 3769 THR A C     1 
ATOM   17665 O  O     . THR A 1 3769 ? 168.684 210.786 210.908 1.00 130.82 ? 3769 THR A O     1 
ATOM   17666 C  CB    . THR A 1 3769 ? 171.979 211.107 211.491 1.00 130.32 ? 3769 THR A CB    1 
ATOM   17667 O  OG1   . THR A 1 3769 ? 171.817 209.818 210.885 1.00 126.45 ? 3769 THR A OG1   1 
ATOM   17668 C  CG2   . THR A 1 3769 ? 172.216 210.933 212.986 1.00 130.66 ? 3769 THR A CG2   1 
ATOM   17669 N  N     . LEU A 1 3770 ? 169.197 211.435 213.008 1.00 135.50 ? 3770 LEU A N     1 
ATOM   17670 C  CA    . LEU A 1 3770 ? 167.936 210.935 213.541 1.00 131.88 ? 3770 LEU A CA    1 
ATOM   17671 C  C     . LEU A 1 3770 ? 166.761 211.546 212.796 1.00 130.93 ? 3770 LEU A C     1 
ATOM   17672 O  O     . LEU A 1 3770 ? 165.893 210.819 212.292 1.00 130.41 ? 3770 LEU A O     1 
ATOM   17673 C  CB    . LEU A 1 3770 ? 167.835 211.232 215.038 1.00 131.57 ? 3770 LEU A CB    1 
ATOM   17674 C  CG    . LEU A 1 3770 ? 168.745 210.436 215.974 1.00 129.37 ? 3770 LEU A CG    1 
ATOM   17675 C  CD1   . LEU A 1 3770 ? 170.051 211.168 216.229 1.00 132.46 ? 3770 LEU A CD1   1 
ATOM   17676 C  CD2   . LEU A 1 3770 ? 168.026 210.150 217.280 1.00 131.02 ? 3770 LEU A CD2   1 
ATOM   17677 N  N     . GLU A 1 3771 ? 166.757 212.878 212.658 1.00 133.06 ? 3771 GLU A N     1 
ATOM   17678 C  CA    . GLU A 1 3771 ? 165.696 213.535 211.904 1.00 133.32 ? 3771 GLU A CA    1 
ATOM   17679 C  C     . GLU A 1 3771 ? 165.534 212.888 210.540 1.00 129.41 ? 3771 GLU A C     1 
ATOM   17680 O  O     . GLU A 1 3771 ? 164.417 212.518 210.151 1.00 125.01 ? 3771 GLU A O     1 
ATOM   17681 C  CB    . GLU A 1 3771 ? 165.994 215.029 211.756 1.00 137.42 ? 3771 GLU A CB    1 
ATOM   17682 C  CG    . GLU A 1 3771 ? 166.262 215.765 213.062 1.00 141.61 ? 3771 GLU A CG    1 
ATOM   17683 C  CD    . GLU A 1 3771 ? 165.026 215.909 213.932 1.00 144.22 ? 3771 GLU A CD    1 
ATOM   17684 O  OE1   . GLU A 1 3771 ? 163.908 215.646 213.441 1.00 141.87 ? 3771 GLU A OE1   1 
ATOM   17685 O  OE2   . GLU A 1 3771 ? 165.173 216.288 215.113 1.00 144.07 ? 3771 GLU A OE2   1 
ATOM   17686 N  N     . ASN A 1 3772 ? 166.651 212.670 209.837 1.00 129.35 ? 3772 ASN A N     1 
ATOM   17687 C  CA    . ASN A 1 3772 ? 166.581 212.056 208.518 1.00 126.91 ? 3772 ASN A CA    1 
ATOM   17688 C  C     . ASN A 1 3772 ? 165.810 210.748 208.583 1.00 124.23 ? 3772 ASN A C     1 
ATOM   17689 O  O     . ASN A 1 3772 ? 164.798 210.578 207.890 1.00 121.97 ? 3772 ASN A O     1 
ATOM   17690 C  CB    . ASN A 1 3772 ? 167.994 211.839 207.968 1.00 127.41 ? 3772 ASN A CB    1 
ATOM   17691 C  CG    . ASN A 1 3772 ? 168.008 211.050 206.669 1.00 123.29 ? 3772 ASN A CG    1 
ATOM   17692 O  OD1   . ASN A 1 3772 ? 167.793 209.838 206.657 1.00 121.68 ? 3772 ASN A OD1   1 
ATOM   17693 N  ND2   . ASN A 1 3772 ? 168.265 211.740 205.564 1.00 116.72 ? 3772 ASN A ND2   1 
ATOM   17694 N  N     . LEU A 1 3773 ? 166.217 209.848 209.486 1.00 123.67 ? 3773 LEU A N     1 
ATOM   17695 C  CA    . LEU A 1 3773 ? 165.493 208.591 209.619 1.00 122.05 ? 3773 LEU A CA    1 
ATOM   17696 C  C     . LEU A 1 3773 ? 164.028 208.854 209.915 1.00 120.38 ? 3773 LEU A C     1 
ATOM   17697 O  O     . LEU A 1 3773 ? 163.146 208.351 209.206 1.00 121.43 ? 3773 LEU A O     1 
ATOM   17698 C  CB    . LEU A 1 3773 ? 166.115 207.716 210.708 1.00 121.56 ? 3773 LEU A CB    1 
ATOM   17699 C  CG    . LEU A 1 3773 ? 167.329 206.862 210.329 1.00 121.42 ? 3773 LEU A CG    1 
ATOM   17700 C  CD1   . LEU A 1 3773 ? 168.585 207.698 210.138 1.00 123.58 ? 3773 LEU A CD1   1 
ATOM   17701 C  CD2   . LEU A 1 3773 ? 167.554 205.770 211.362 1.00 118.53 ? 3773 LEU A CD2   1 
ATOM   17702 N  N     . LYS A 1 3774 ? 163.756 209.710 210.906 1.00 118.64 ? 3774 LYS A N     1 
ATOM   17703 C  CA    . LYS A 1 3774 ? 162.373 210.032 211.229 1.00 118.51 ? 3774 LYS A CA    1 
ATOM   17704 C  C     . LYS A 1 3774 ? 161.632 210.486 209.985 1.00 120.28 ? 3774 LYS A C     1 
ATOM   17705 O  O     . LYS A 1 3774 ? 160.554 209.962 209.672 1.00 116.66 ? 3774 LYS A O     1 
ATOM   17706 C  CB    . LYS A 1 3774 ? 162.317 211.106 212.315 1.00 119.82 ? 3774 LYS A CB    1 
ATOM   17707 C  CG    . LYS A 1 3774 ? 160.905 211.442 212.776 1.00 118.10 ? 3774 LYS A CG    1 
ATOM   17708 C  CD    . LYS A 1 3774 ? 160.898 212.183 214.107 1.00 115.98 ? 3774 LYS A CD    1 
ATOM   17709 C  CE    . LYS A 1 3774 ? 162.095 213.111 214.251 1.00 122.44 ? 3774 LYS A CE    1 
ATOM   17710 N  NZ    . LYS A 1 3774 ? 162.063 214.224 213.260 1.00 124.37 ? 3774 LYS A NZ    1 
ATOM   17711 N  N     . ARG A 1 3775 ? 162.242 211.393 209.215 1.00 122.10 ? 3775 ARG A N     1 
ATOM   17712 C  CA    . ARG A 1 3775 ? 161.595 211.870 208.001 1.00 117.18 ? 3775 ARG A CA    1 
ATOM   17713 C  C     . ARG A 1 3775 ? 161.227 210.700 207.105 1.00 115.39 ? 3775 ARG A C     1 
ATOM   17714 O  O     . ARG A 1 3775 ? 160.048 210.499 206.782 1.00 114.09 ? 3775 ARG A O     1 
ATOM   17715 C  CB    . ARG A 1 3775 ? 162.513 212.849 207.270 1.00 118.04 ? 3775 ARG A CB    1 
ATOM   17716 C  CG    . ARG A 1 3775 ? 161.982 213.322 205.929 1.00 120.52 ? 3775 ARG A CG    1 
ATOM   17717 C  CD    . ARG A 1 3775 ? 163.005 214.189 205.208 1.00 122.81 ? 3775 ARG A CD    1 
ATOM   17718 N  NE    . ARG A 1 3775 ? 164.256 213.485 204.942 1.00 124.90 ? 3775 ARG A NE    1 
ATOM   17719 C  CZ    . ARG A 1 3775 ? 164.385 212.447 204.126 1.00 125.89 ? 3775 ARG A CZ    1 
ATOM   17720 N  NH1   . ARG A 1 3775 ? 163.359 211.972 203.439 1.00 122.51 ? 3775 ARG A NH1   1 
ATOM   17721 N  NH2   . ARG A 1 3775 ? 165.578 211.877 203.986 1.00 123.24 ? 3775 ARG A NH2   1 
ATOM   17722 N  N     . GLU A 1 3776 ? 162.208 209.848 206.789 1.00 115.00 ? 3776 GLU A N     1 
ATOM   17723 C  CA    . GLU A 1 3776 ? 161.902 208.713 205.932 1.00 111.36 ? 3776 GLU A CA    1 
ATOM   17724 C  C     . GLU A 1 3776 ? 160.893 207.797 206.596 1.00 109.32 ? 3776 GLU A C     1 
ATOM   17725 O  O     . GLU A 1 3776 ? 159.968 207.314 205.930 1.00 108.86 ? 3776 GLU A O     1 
ATOM   17726 C  CB    . GLU A 1 3776 ? 163.170 207.945 205.566 1.00 110.24 ? 3776 GLU A CB    1 
ATOM   17727 C  CG    . GLU A 1 3776 ? 164.121 208.727 204.681 1.00 118.29 ? 3776 GLU A CG    1 
ATOM   17728 C  CD    . GLU A 1 3776 ? 165.210 207.856 204.095 1.00 122.88 ? 3776 GLU A CD    1 
ATOM   17729 O  OE1   . GLU A 1 3776 ? 165.226 206.647 204.404 1.00 121.68 ? 3776 GLU A OE1   1 
ATOM   17730 O  OE2   . GLU A 1 3776 ? 166.047 208.377 203.328 1.00 125.90 ? 3776 GLU A OE2   1 
ATOM   17731 N  N     . ALA A 1 3777 ? 161.021 207.592 207.911 1.00 109.74 ? 3777 ALA A N     1 
ATOM   17732 C  CA    . ALA A 1 3777 ? 160.009 206.823 208.618 1.00 104.62 ? 3777 ALA A CA    1 
ATOM   17733 C  C     . ALA A 1 3777 ? 158.632 207.407 208.363 1.00 103.69 ? 3777 ALA A C     1 
ATOM   17734 O  O     . ALA A 1 3777 ? 157.738 206.708 207.866 1.00 102.62 ? 3777 ALA A O     1 
ATOM   17735 C  CB    . ALA A 1 3777 ? 160.318 206.791 210.113 1.00 106.47 ? 3777 ALA A CB    1 
ATOM   17736 N  N     . ALA A 1 3778 ? 158.474 208.714 208.600 1.00 106.05 ? 3778 ALA A N     1 
ATOM   17737 C  CA    . ALA A 1 3778 ? 157.195 209.348 208.319 1.00 104.23 ? 3778 ALA A CA    1 
ATOM   17738 C  C     . ALA A 1 3778 ? 156.769 209.057 206.892 1.00 103.84 ? 3778 ALA A C     1 
ATOM   17739 O  O     . ALA A 1 3778 ? 155.643 208.600 206.653 1.00 103.18 ? 3778 ALA A O     1 
ATOM   17740 C  CB    . ALA A 1 3778 ? 157.282 210.854 208.565 1.00 105.65 ? 3778 ALA A CB    1 
ATOM   17741 N  N     . GLU A 1 3779 ? 157.696 209.220 205.944 1.00 104.04 ? 3779 GLU A N     1 
ATOM   17742 C  CA    . GLU A 1 3779 ? 157.375 208.967 204.548 1.00 102.69 ? 3779 GLU A CA    1 
ATOM   17743 C  C     . GLU A 1 3779 ? 156.810 207.567 204.374 1.00 101.80 ? 3779 GLU A C     1 
ATOM   17744 O  O     . GLU A 1 3779 ? 155.685 207.399 203.886 1.00 102.67 ? 3779 GLU A O     1 
ATOM   17745 C  CB    . GLU A 1 3779 ? 158.620 209.162 203.683 1.00 103.92 ? 3779 GLU A CB    1 
ATOM   17746 C  CG    . GLU A 1 3779 ? 158.372 209.022 202.193 1.00 107.63 ? 3779 GLU A CG    1 
ATOM   17747 C  CD    . GLU A 1 3779 ? 159.430 209.717 201.362 1.00 115.27 ? 3779 GLU A CD    1 
ATOM   17748 O  OE1   . GLU A 1 3779 ? 160.593 209.783 201.813 1.00 118.65 ? 3779 GLU A OE1   1 
ATOM   17749 O  OE2   . GLU A 1 3779 ? 159.100 210.202 200.260 1.00 117.10 ? 3779 GLU A OE2   1 
ATOM   17750 N  N     . VAL A 1 3780 ? 157.534 206.551 204.855 1.00 100.85 ? 3780 VAL A N     1 
ATOM   17751 C  CA    . VAL A 1 3780 ? 157.036 205.201 204.634 1.00 93.13  ? 3780 VAL A CA    1 
ATOM   17752 C  C     . VAL A 1 3780 ? 155.750 205.005 205.416 1.00 93.95  ? 3780 VAL A C     1 
ATOM   17753 O  O     . VAL A 1 3780 ? 154.805 204.379 204.918 1.00 98.53  ? 3780 VAL A O     1 
ATOM   17754 C  CB    . VAL A 1 3780 ? 158.100 204.134 204.969 1.00 91.84  ? 3780 VAL A CB    1 
ATOM   17755 C  CG1   . VAL A 1 3780 ? 159.349 204.351 204.128 1.00 90.14  ? 3780 VAL A CG1   1 
ATOM   17756 C  CG2   . VAL A 1 3780 ? 158.440 204.114 206.446 1.00 100.27 ? 3780 VAL A CG2   1 
ATOM   17757 N  N     . THR A 1 3781 ? 155.654 205.607 206.606 1.00 93.70  ? 3781 THR A N     1 
ATOM   17758 C  CA    . THR A 1 3781 ? 154.410 205.524 207.358 1.00 94.82  ? 3781 THR A CA    1 
ATOM   17759 C  C     . THR A 1 3781 ? 153.263 206.091 206.541 1.00 97.14  ? 3781 THR A C     1 
ATOM   17760 O  O     . THR A 1 3781 ? 152.197 205.469 206.439 1.00 98.27  ? 3781 THR A O     1 
ATOM   17761 C  CB    . THR A 1 3781 ? 154.541 206.262 208.689 1.00 102.99 ? 3781 THR A CB    1 
ATOM   17762 O  OG1   . THR A 1 3781 ? 155.665 205.747 209.413 1.00 106.54 ? 3781 THR A OG1   1 
ATOM   17763 C  CG2   . THR A 1 3781 ? 153.282 206.079 209.522 1.00 103.84 ? 3781 THR A CG2   1 
ATOM   17764 N  N     . ARG A 1 3782 ? 153.488 207.237 205.894 1.00 99.05  ? 3782 ARG A N     1 
ATOM   17765 C  CA    . ARG A 1 3782 ? 152.454 207.803 205.041 1.00 97.97  ? 3782 ARG A CA    1 
ATOM   17766 C  C     . ARG A 1 3782 ? 152.095 206.834 203.925 1.00 95.03  ? 3782 ARG A C     1 
ATOM   17767 O  O     . ARG A 1 3782 ? 150.911 206.598 203.653 1.00 94.83  ? 3782 ARG A O     1 
ATOM   17768 C  CB    . ARG A 1 3782 ? 152.919 209.144 204.476 1.00 97.49  ? 3782 ARG A CB    1 
ATOM   17769 C  CG    . ARG A 1 3782 ? 151.794 210.074 204.063 1.00 98.69  ? 3782 ARG A CG    1 
ATOM   17770 C  CD    . ARG A 1 3782 ? 152.326 211.276 203.301 1.00 102.17 ? 3782 ARG A CD    1 
ATOM   17771 N  NE    . ARG A 1 3782 ? 153.516 210.955 202.522 1.00 105.23 ? 3782 ARG A NE    1 
ATOM   17772 C  CZ    . ARG A 1 3782 ? 153.497 210.421 201.308 1.00 102.20 ? 3782 ARG A CZ    1 
ATOM   17773 N  NH1   . ARG A 1 3782 ? 152.359 210.139 200.696 1.00 97.12  ? 3782 ARG A NH1   1 
ATOM   17774 N  NH2   . ARG A 1 3782 ? 154.648 210.168 200.692 1.00 96.27  ? 3782 ARG A NH2   1 
ATOM   17775 N  N     . LYS A 1 3783 ? 153.106 206.215 203.309 1.00 90.09  ? 3783 LYS A N     1 
ATOM   17776 C  CA    . LYS A 1 3783 ? 152.833 205.271 202.233 1.00 84.84  ? 3783 LYS A CA    1 
ATOM   17777 C  C     . LYS A 1 3783 ? 152.093 204.049 202.757 1.00 88.92  ? 3783 LYS A C     1 
ATOM   17778 O  O     . LYS A 1 3783 ? 151.372 203.381 202.006 1.00 92.43  ? 3783 LYS A O     1 
ATOM   17779 C  CB    . LYS A 1 3783 ? 154.136 204.874 201.544 1.00 84.98  ? 3783 LYS A CB    1 
ATOM   17780 C  CG    . LYS A 1 3783 ? 154.820 206.036 200.844 1.00 89.56  ? 3783 LYS A CG    1 
ATOM   17781 C  CD    . LYS A 1 3783 ? 156.198 205.658 200.337 1.00 89.98  ? 3783 LYS A CD    1 
ATOM   17782 C  CE    . LYS A 1 3783 ? 156.840 206.818 199.597 1.00 88.27  ? 3783 LYS A CE    1 
ATOM   17783 N  NZ    . LYS A 1 3783 ? 158.251 206.528 199.223 1.00 86.08  ? 3783 LYS A NZ    1 
ATOM   17784 N  N     . VAL A 1 3784 ? 152.258 203.736 204.044 1.00 90.86  ? 3784 VAL A N     1 
ATOM   17785 C  CA    . VAL A 1 3784 ? 151.468 202.663 204.638 1.00 90.47  ? 3784 VAL A CA    1 
ATOM   17786 C  C     . VAL A 1 3784 ? 150.031 203.122 204.850 1.00 91.16  ? 3784 VAL A C     1 
ATOM   17787 O  O     . VAL A 1 3784 ? 149.081 202.362 204.630 1.00 90.79  ? 3784 VAL A O     1 
ATOM   17788 C  CB    . VAL A 1 3784 ? 152.114 202.180 205.950 1.00 89.18  ? 3784 VAL A CB    1 
ATOM   17789 C  CG1   . VAL A 1 3784 ? 151.228 201.152 206.633 1.00 89.74  ? 3784 VAL A CG1   1 
ATOM   17790 C  CG2   . VAL A 1 3784 ? 153.484 201.589 205.674 1.00 85.16  ? 3784 VAL A CG2   1 
ATOM   17791 N  N     . GLU A 1 3785 ? 149.848 204.378 205.267 1.00 93.13  ? 3785 GLU A N     1 
ATOM   17792 C  CA    . GLU A 1 3785 ? 148.510 204.845 205.612 1.00 96.42  ? 3785 GLU A CA    1 
ATOM   17793 C  C     . GLU A 1 3785 ? 147.661 205.102 204.375 1.00 98.88  ? 3785 GLU A C     1 
ATOM   17794 O  O     . GLU A 1 3785 ? 146.435 204.947 204.423 1.00 99.63  ? 3785 GLU A O     1 
ATOM   17795 C  CB    . GLU A 1 3785 ? 148.600 206.107 206.468 1.00 97.19  ? 3785 GLU A CB    1 
ATOM   17796 C  CG    . GLU A 1 3785 ? 149.248 205.887 207.824 1.00 100.18 ? 3785 GLU A CG    1 
ATOM   17797 C  CD    . GLU A 1 3785 ? 148.376 205.078 208.763 1.00 105.41 ? 3785 GLU A CD    1 
ATOM   17798 O  OE1   . GLU A 1 3785 ? 147.632 205.689 209.558 1.00 110.89 ? 3785 GLU A OE1   1 
ATOM   17799 O  OE2   . GLU A 1 3785 ? 148.438 203.831 208.711 1.00 104.31 ? 3785 GLU A OE2   1 
ATOM   17800 N  N     . GLU A 1 3786 ? 148.285 205.490 203.267 1.00 97.53  ? 3786 GLU A N     1 
ATOM   17801 C  CA    . GLU A 1 3786 ? 147.578 205.808 202.036 1.00 91.77  ? 3786 GLU A CA    1 
ATOM   17802 C  C     . GLU A 1 3786 ? 147.545 204.643 201.057 1.00 88.62  ? 3786 GLU A C     1 
ATOM   17803 O  O     . GLU A 1 3786 ? 147.219 204.848 199.885 1.00 90.14  ? 3786 GLU A O     1 
ATOM   17804 C  CB    . GLU A 1 3786 ? 148.217 207.025 201.363 1.00 87.54  ? 3786 GLU A CB    1 
ATOM   17805 C  CG    . GLU A 1 3786 ? 148.172 208.292 202.198 1.00 97.64  ? 3786 GLU A CG    1 
ATOM   17806 C  CD    . GLU A 1 3786 ? 149.049 209.391 201.632 1.00 106.31 ? 3786 GLU A CD    1 
ATOM   17807 O  OE1   . GLU A 1 3786 ? 149.758 209.131 200.638 1.00 107.97 ? 3786 GLU A OE1   1 
ATOM   17808 O  OE2   . GLU A 1 3786 ? 149.027 210.513 202.179 1.00 104.04 ? 3786 GLU A OE2   1 
ATOM   17809 N  N     . THR A 1 3787 ? 147.870 203.430 201.511 1.00 89.84  ? 3787 THR A N     1 
ATOM   17810 C  CA    . THR A 1 3787 ? 148.035 202.312 200.587 1.00 88.65  ? 3787 THR A CA    1 
ATOM   17811 C  C     . THR A 1 3787 ? 146.737 201.987 199.856 1.00 85.92  ? 3787 THR A C     1 
ATOM   17812 O  O     . THR A 1 3787 ? 146.744 201.776 198.640 1.00 89.25  ? 3787 THR A O     1 
ATOM   17813 C  CB    . THR A 1 3787 ? 148.547 201.083 201.340 1.00 88.45  ? 3787 THR A CB    1 
ATOM   17814 O  OG1   . THR A 1 3787 ? 149.939 201.248 201.633 1.00 84.15  ? 3787 THR A OG1   1 
ATOM   17815 C  CG2   . THR A 1 3787 ? 148.365 199.826 200.506 1.00 82.71  ? 3787 THR A CG2   1 
ATOM   17816 N  N     . ASP A 1 3788 ? 145.612 201.962 200.573 1.00 87.08  ? 3788 ASP A N     1 
ATOM   17817 C  CA    . ASP A 1 3788 ? 144.346 201.587 199.947 1.00 90.59  ? 3788 ASP A CA    1 
ATOM   17818 C  C     . ASP A 1 3788 ? 143.915 202.611 198.903 1.00 84.86  ? 3788 ASP A C     1 
ATOM   17819 O  O     . ASP A 1 3788 ? 143.426 202.248 197.824 1.00 82.67  ? 3788 ASP A O     1 
ATOM   17820 C  CB    . ASP A 1 3788 ? 143.266 201.421 201.016 1.00 97.10  ? 3788 ASP A CB    1 
ATOM   17821 C  CG    . ASP A 1 3788 ? 143.630 200.376 202.052 1.00 104.06 ? 3788 ASP A CG    1 
ATOM   17822 O  OD1   . ASP A 1 3788 ? 144.570 200.620 202.837 1.00 101.58 ? 3788 ASP A OD1   1 
ATOM   17823 O  OD2   . ASP A 1 3788 ? 142.979 199.311 202.081 1.00 108.70 ? 3788 ASP A OD2   1 
ATOM   17824 N  N     . ILE A 1 3789 ? 144.091 203.899 199.207 1.00 80.81  ? 3789 ILE A N     1 
ATOM   17825 C  CA    . ILE A 1 3789 ? 143.716 204.949 198.265 1.00 77.95  ? 3789 ILE A CA    1 
ATOM   17826 C  C     . ILE A 1 3789 ? 144.545 204.843 196.993 1.00 79.67  ? 3789 ILE A C     1 
ATOM   17827 O  O     . ILE A 1 3789 ? 144.018 204.957 195.878 1.00 81.29  ? 3789 ILE A O     1 
ATOM   17828 C  CB    . ILE A 1 3789 ? 143.866 206.332 198.924 1.00 73.53  ? 3789 ILE A CB    1 
ATOM   17829 C  CG1   . ILE A 1 3789 ? 142.971 206.433 200.158 1.00 80.71  ? 3789 ILE A CG1   1 
ATOM   17830 C  CG2   . ILE A 1 3789 ? 143.539 207.435 197.934 1.00 72.79  ? 3789 ILE A CG2   1 
ATOM   17831 C  CD1   . ILE A 1 3789 ? 141.497 206.292 199.854 1.00 82.09  ? 3789 ILE A CD1   1 
ATOM   17832 N  N     . VAL A 1 3790 ? 145.852 204.622 197.135 1.00 75.10  ? 3790 VAL A N     1 
ATOM   17833 C  CA    . VAL A 1 3790 ? 146.709 204.526 195.959 1.00 66.79  ? 3790 VAL A CA    1 
ATOM   17834 C  C     . VAL A 1 3790 ? 146.402 203.255 195.175 1.00 67.35  ? 3790 VAL A C     1 
ATOM   17835 O  O     . VAL A 1 3790 ? 146.477 203.244 193.943 1.00 77.17  ? 3790 VAL A O     1 
ATOM   17836 C  CB    . VAL A 1 3790 ? 148.191 204.611 196.358 1.00 65.21  ? 3790 VAL A CB    1 
ATOM   17837 C  CG1   . VAL A 1 3790 ? 149.058 204.612 195.119 1.00 65.04  ? 3790 VAL A CG1   1 
ATOM   17838 C  CG2   . VAL A 1 3790 ? 148.446 205.865 197.173 1.00 74.88  ? 3790 VAL A CG2   1 
ATOM   17839 N  N     . MET A 1 3791 ? 146.059 202.165 195.867 1.00 65.23  ? 3791 MET A N     1 
ATOM   17840 C  CA    . MET A 1 3791 ? 145.624 200.961 195.164 1.00 66.75  ? 3791 MET A CA    1 
ATOM   17841 C  C     . MET A 1 3791 ? 144.397 201.244 194.311 1.00 76.17  ? 3791 MET A C     1 
ATOM   17842 O  O     . MET A 1 3791 ? 144.343 200.868 193.135 1.00 80.21  ? 3791 MET A O     1 
ATOM   17843 C  CB    . MET A 1 3791 ? 145.324 199.832 196.151 1.00 71.78  ? 3791 MET A CB    1 
ATOM   17844 C  CG    . MET A 1 3791 ? 146.521 199.287 196.896 1.00 80.87  ? 3791 MET A CG    1 
ATOM   17845 S  SD    . MET A 1 3791 ? 146.054 198.022 198.089 1.00 112.05 ? 3791 MET A SD    1 
ATOM   17846 C  CE    . MET A 1 3791 ? 145.598 196.685 196.990 1.00 95.82  ? 3791 MET A CE    1 
ATOM   17847 N  N     . GLN A 1 3792 ? 143.398 201.915 194.888 1.00 75.68  ? 3792 GLN A N     1 
ATOM   17848 C  CA    . GLN A 1 3792 ? 142.199 202.244 194.123 1.00 75.40  ? 3792 GLN A CA    1 
ATOM   17849 C  C     . GLN A 1 3792 ? 142.535 203.140 192.936 1.00 74.53  ? 3792 GLN A C     1 
ATOM   17850 O  O     . GLN A 1 3792 ? 142.029 202.934 191.824 1.00 76.04  ? 3792 GLN A O     1 
ATOM   17851 C  CB    . GLN A 1 3792 ? 141.165 202.912 195.031 1.00 79.97  ? 3792 GLN A CB    1 
ATOM   17852 C  CG    . GLN A 1 3792 ? 140.055 203.666 194.303 1.00 87.84  ? 3792 GLN A CG    1 
ATOM   17853 C  CD    . GLN A 1 3792 ? 139.007 202.752 193.684 1.00 95.16  ? 3792 GLN A CD    1 
ATOM   17854 O  OE1   . GLN A 1 3792 ? 139.325 201.704 193.122 1.00 89.35  ? 3792 GLN A OE1   1 
ATOM   17855 N  NE2   . GLN A 1 3792 ? 137.745 203.151 193.790 1.00 96.78  ? 3792 GLN A NE2   1 
ATOM   17856 N  N     . GLU A 1 3793 ? 143.402 204.131 193.153 1.00 70.49  ? 3793 GLU A N     1 
ATOM   17857 C  CA    . GLU A 1 3793 ? 143.773 205.052 192.084 1.00 65.82  ? 3793 GLU A CA    1 
ATOM   17858 C  C     . GLU A 1 3793 ? 144.465 204.321 190.938 1.00 63.52  ? 3793 GLU A C     1 
ATOM   17859 O  O     . GLU A 1 3793 ? 144.117 204.507 189.764 1.00 69.50  ? 3793 GLU A O     1 
ATOM   17860 C  CB    . GLU A 1 3793 ? 144.671 206.154 192.648 1.00 66.65  ? 3793 GLU A CB    1 
ATOM   17861 C  CG    . GLU A 1 3793 ? 144.760 207.406 191.797 1.00 73.90  ? 3793 GLU A CG    1 
ATOM   17862 C  CD    . GLU A 1 3793 ? 145.993 207.426 190.918 1.00 78.91  ? 3793 GLU A CD    1 
ATOM   17863 O  OE1   . GLU A 1 3793 ? 146.736 206.423 190.912 1.00 77.61  ? 3793 GLU A OE1   1 
ATOM   17864 O  OE2   . GLU A 1 3793 ? 146.224 208.448 190.240 1.00 78.11  ? 3793 GLU A OE2   1 
ATOM   17865 N  N     . VAL A 1 3794 ? 145.444 203.471 191.261 1.00 63.24  ? 3794 VAL A N     1 
ATOM   17866 C  CA    . VAL A 1 3794 ? 146.177 202.778 190.209 1.00 60.69  ? 3794 VAL A CA    1 
ATOM   17867 C  C     . VAL A 1 3794 ? 145.288 201.756 189.517 1.00 64.63  ? 3794 VAL A C     1 
ATOM   17868 O  O     . VAL A 1 3794 ? 145.442 201.516 188.317 1.00 67.71  ? 3794 VAL A O     1 
ATOM   17869 C  CB    . VAL A 1 3794 ? 147.471 202.135 190.749 1.00 56.25  ? 3794 VAL A CB    1 
ATOM   17870 C  CG1   . VAL A 1 3794 ? 148.359 203.186 191.396 1.00 63.55  ? 3794 VAL A CG1   1 
ATOM   17871 C  CG2   . VAL A 1 3794 ? 147.168 201.008 191.717 1.00 60.63  ? 3794 VAL A CG2   1 
ATOM   17872 N  N     . GLU A 1 3795 ? 144.335 201.151 190.233 1.00 65.93  ? 3795 GLU A N     1 
ATOM   17873 C  CA    . GLU A 1 3795 ? 143.424 200.223 189.568 1.00 66.42  ? 3795 GLU A CA    1 
ATOM   17874 C  C     . GLU A 1 3795 ? 142.497 200.947 188.600 1.00 70.68  ? 3795 GLU A C     1 
ATOM   17875 O  O     . GLU A 1 3795 ? 142.241 200.451 187.498 1.00 74.78  ? 3795 GLU A O     1 
ATOM   17876 C  CB    . GLU A 1 3795 ? 142.620 199.424 190.594 1.00 71.42  ? 3795 GLU A CB    1 
ATOM   17877 C  CG    . GLU A 1 3795 ? 143.457 198.473 191.442 1.00 82.02  ? 3795 GLU A CG    1 
ATOM   17878 C  CD    . GLU A 1 3795 ? 144.126 197.373 190.632 1.00 90.51  ? 3795 GLU A CD    1 
ATOM   17879 O  OE1   . GLU A 1 3795 ? 143.721 197.138 189.474 1.00 91.23  ? 3795 GLU A OE1   1 
ATOM   17880 O  OE2   . GLU A 1 3795 ? 145.069 196.744 191.158 1.00 90.49  ? 3795 GLU A OE2   1 
ATOM   17881 N  N     . THR A 1 3796 ? 141.986 202.120 188.982 1.00 68.54  ? 3796 THR A N     1 
ATOM   17882 C  CA    . THR A 1 3796 ? 141.163 202.885 188.046 1.00 61.99  ? 3796 THR A CA    1 
ATOM   17883 C  C     . THR A 1 3796 ? 141.971 203.315 186.826 1.00 61.66  ? 3796 THR A C     1 
ATOM   17884 O  O     . THR A 1 3796 ? 141.498 203.211 185.684 1.00 66.49  ? 3796 THR A O     1 
ATOM   17885 C  CB    . THR A 1 3796 ? 140.552 204.102 188.739 1.00 64.37  ? 3796 THR A CB    1 
ATOM   17886 O  OG1   . THR A 1 3796 ? 141.594 204.931 189.267 1.00 72.29  ? 3796 THR A OG1   1 
ATOM   17887 C  CG2   . THR A 1 3796 ? 139.625 203.669 189.864 1.00 67.55  ? 3796 THR A CG2   1 
ATOM   17888 N  N     . VAL A 1 3797 ? 143.201 203.786 187.041 1.00 61.20  ? 3797 VAL A N     1 
ATOM   17889 C  CA    . VAL A 1 3797 ? 144.022 204.208 185.911 1.00 57.94  ? 3797 VAL A CA    1 
ATOM   17890 C  C     . VAL A 1 3797 ? 144.365 203.016 185.021 1.00 56.67  ? 3797 VAL A C     1 
ATOM   17891 O  O     . VAL A 1 3797 ? 144.431 203.142 183.793 1.00 57.41  ? 3797 VAL A O     1 
ATOM   17892 C  CB    . VAL A 1 3797 ? 145.281 204.940 186.408 1.00 60.56  ? 3797 VAL A CB    1 
ATOM   17893 C  CG1   . VAL A 1 3797 ? 146.165 205.324 185.242 1.00 61.70  ? 3797 VAL A CG1   1 
ATOM   17894 C  CG2   . VAL A 1 3797 ? 144.888 206.180 187.191 1.00 60.48  ? 3797 VAL A CG2   1 
ATOM   17895 N  N     . SER A 1 3798 ? 144.575 201.840 185.617 1.00 56.95  ? 3798 SER A N     1 
ATOM   17896 C  CA    . SER A 1 3798 ? 144.836 200.641 184.829 1.00 54.90  ? 3798 SER A CA    1 
ATOM   17897 C  C     . SER A 1 3798 ? 143.610 200.230 184.024 1.00 57.26  ? 3798 SER A C     1 
ATOM   17898 O  O     . SER A 1 3798 ? 143.737 199.772 182.884 1.00 64.32  ? 3798 SER A O     1 
ATOM   17899 C  CB    . SER A 1 3798 ? 145.284 199.502 185.743 1.00 56.51  ? 3798 SER A CB    1 
ATOM   17900 O  OG    . SER A 1 3798 ? 146.434 199.864 186.484 1.00 60.19  ? 3798 SER A OG    1 
ATOM   17901 N  N     . GLN A 1 3799 ? 142.418 200.361 184.609 1.00 59.88  ? 3799 GLN A N     1 
ATOM   17902 C  CA    . GLN A 1 3799 ? 141.199 200.090 183.856 1.00 62.51  ? 3799 GLN A CA    1 
ATOM   17903 C  C     . GLN A 1 3799 ? 141.028 201.070 182.706 1.00 59.46  ? 3799 GLN A C     1 
ATOM   17904 O  O     . GLN A 1 3799 ? 140.408 200.733 181.691 1.00 59.10  ? 3799 GLN A O     1 
ATOM   17905 C  CB    . GLN A 1 3799 ? 139.978 200.138 184.775 1.00 59.45  ? 3799 GLN A CB    1 
ATOM   17906 C  CG    . GLN A 1 3799 ? 139.950 199.052 185.831 1.00 65.76  ? 3799 GLN A CG    1 
ATOM   17907 C  CD    . GLN A 1 3799 ? 139.883 197.664 185.231 1.00 77.91  ? 3799 GLN A CD    1 
ATOM   17908 O  OE1   . GLN A 1 3799 ? 140.849 196.904 185.285 1.00 79.03  ? 3799 GLN A OE1   1 
ATOM   17909 N  NE2   . GLN A 1 3799 ? 138.738 197.327 184.650 1.00 84.48  ? 3799 GLN A NE2   1 
ATOM   17910 N  N     . GLN A 1 3800 ? 141.557 202.286 182.850 1.00 57.36  ? 3800 GLN A N     1 
ATOM   17911 C  CA    . GLN A 1 3800 ? 141.477 203.247 181.752 1.00 54.66  ? 3800 GLN A CA    1 
ATOM   17912 C  C     . GLN A 1 3800 ? 142.223 202.753 180.513 1.00 51.27  ? 3800 GLN A C     1 
ATOM   17913 O  O     . GLN A 1 3800 ? 141.731 202.899 179.388 1.00 51.30  ? 3800 GLN A O     1 
ATOM   17914 C  CB    . GLN A 1 3800 ? 142.019 204.606 182.190 1.00 55.49  ? 3800 GLN A CB    1 
ATOM   17915 C  CG    . GLN A 1 3800 ? 141.887 205.678 181.121 1.00 58.32  ? 3800 GLN A CG    1 
ATOM   17916 C  CD    . GLN A 1 3800 ? 142.374 207.036 181.582 1.00 72.53  ? 3800 GLN A CD    1 
ATOM   17917 O  OE1   . GLN A 1 3800 ? 142.854 207.189 182.704 1.00 74.88  ? 3800 GLN A OE1   1 
ATOM   17918 N  NE2   . GLN A 1 3800 ? 142.259 208.031 180.711 1.00 69.91  ? 3800 GLN A NE2   1 
ATOM   17919 N  N     . TYR A 1 3801 ? 143.409 202.172 180.694 1.00 50.18  ? 3801 TYR A N     1 
ATOM   17920 C  CA    . TYR A 1 3801 ? 144.244 201.725 179.584 1.00 44.68  ? 3801 TYR A CA    1 
ATOM   17921 C  C     . TYR A 1 3801 ? 144.157 200.225 179.324 1.00 49.10  ? 3801 TYR A C     1 
ATOM   17922 O  O     . TYR A 1 3801 ? 144.907 199.711 178.489 1.00 48.92  ? 3801 TYR A O     1 
ATOM   17923 C  CB    . TYR A 1 3801 ? 145.702 202.124 179.823 1.00 38.59  ? 3801 TYR A CB    1 
ATOM   17924 C  CG    . TYR A 1 3801 ? 145.900 203.598 180.085 1.00 43.28  ? 3801 TYR A CG    1 
ATOM   17925 C  CD1   . TYR A 1 3801 ? 145.942 204.504 179.038 1.00 44.35  ? 3801 TYR A CD1   1 
ATOM   17926 C  CD2   . TYR A 1 3801 ? 146.037 204.085 181.373 1.00 50.46  ? 3801 TYR A CD2   1 
ATOM   17927 C  CE1   . TYR A 1 3801 ? 146.122 205.848 179.265 1.00 47.66  ? 3801 TYR A CE1   1 
ATOM   17928 C  CE2   . TYR A 1 3801 ? 146.213 205.431 181.610 1.00 52.38  ? 3801 TYR A CE2   1 
ATOM   17929 C  CZ    . TYR A 1 3801 ? 146.255 206.307 180.551 1.00 51.09  ? 3801 TYR A CZ    1 
ATOM   17930 O  OH    . TYR A 1 3801 ? 146.430 207.651 180.774 1.00 64.60  ? 3801 TYR A OH    1 
ATOM   17931 N  N     . LEU A 1 3802 ? 143.284 199.513 180.031 1.00 50.74  ? 3802 LEU A N     1 
ATOM   17932 C  CA    . LEU A 1 3802 ? 143.099 198.090 179.755 1.00 48.21  ? 3802 LEU A CA    1 
ATOM   17933 C  C     . LEU A 1 3802 ? 142.658 197.783 178.323 1.00 48.98  ? 3802 LEU A C     1 
ATOM   17934 O  O     . LEU A 1 3802 ? 143.218 196.843 177.727 1.00 47.07  ? 3802 LEU A O     1 
ATOM   17935 C  CB    . LEU A 1 3802 ? 142.102 197.507 180.765 1.00 56.30  ? 3802 LEU A CB    1 
ATOM   17936 C  CG    . LEU A 1 3802 ? 141.817 196.010 180.682 1.00 65.90  ? 3802 LEU A CG    1 
ATOM   17937 C  CD1   . LEU A 1 3802 ? 143.118 195.235 180.678 1.00 58.47  ? 3802 LEU A CD1   1 
ATOM   17938 C  CD2   . LEU A 1 3802 ? 140.928 195.571 181.833 1.00 65.30  ? 3802 LEU A CD2   1 
ATOM   17939 N  N     . PRO A 1 3803 ? 141.675 198.479 177.729 1.00 51.37  ? 3803 PRO A N     1 
ATOM   17940 C  CA    . PRO A 1 3803 ? 141.291 198.139 176.347 1.00 49.07  ? 3803 PRO A CA    1 
ATOM   17941 C  C     . PRO A 1 3803 ? 142.428 198.264 175.350 1.00 45.63  ? 3803 PRO A C     1 
ATOM   17942 O  O     . PRO A 1 3803 ? 142.526 197.448 174.426 1.00 46.43  ? 3803 PRO A O     1 
ATOM   17943 C  CB    . PRO A 1 3803 ? 140.156 199.131 176.046 1.00 48.32  ? 3803 PRO A CB    1 
ATOM   17944 C  CG    . PRO A 1 3803 ? 140.307 200.215 177.052 1.00 47.77  ? 3803 PRO A CG    1 
ATOM   17945 C  CD    . PRO A 1 3803 ? 140.804 199.533 178.277 1.00 48.95  ? 3803 PRO A CD    1 
ATOM   17946 N  N     . LEU A 1 3804 ? 143.302 199.258 175.517 1.00 40.65  ? 3804 LEU A N     1 
ATOM   17947 C  CA    . LEU A 1 3804 ? 144.451 199.380 174.626 1.00 40.27  ? 3804 LEU A CA    1 
ATOM   17948 C  C     . LEU A 1 3804 ? 145.378 198.179 174.763 1.00 42.39  ? 3804 LEU A C     1 
ATOM   17949 O  O     . LEU A 1 3804 ? 145.921 197.688 173.769 1.00 41.65  ? 3804 LEU A O     1 
ATOM   17950 C  CB    . LEU A 1 3804 ? 145.202 200.680 174.910 1.00 37.56  ? 3804 LEU A CB    1 
ATOM   17951 C  CG    . LEU A 1 3804 ? 146.563 200.850 174.232 1.00 35.69  ? 3804 LEU A CG    1 
ATOM   17952 C  CD1   . LEU A 1 3804 ? 146.414 200.851 172.725 1.00 41.74  ? 3804 LEU A CD1   1 
ATOM   17953 C  CD2   . LEU A 1 3804 ? 147.226 202.129 174.695 1.00 31.65  ? 3804 LEU A CD2   1 
ATOM   17954 N  N     . SER A 1 3805 ? 145.568 197.691 175.990 1.00 41.43  ? 3805 SER A N     1 
ATOM   17955 C  CA    . SER A 1 3805 ? 146.423 196.529 176.207 1.00 34.27  ? 3805 SER A CA    1 
ATOM   17956 C  C     . SER A 1 3805 ? 145.833 195.279 175.572 1.00 38.50  ? 3805 SER A C     1 
ATOM   17957 O  O     . SER A 1 3805 ? 146.556 194.477 174.961 1.00 44.13  ? 3805 SER A O     1 
ATOM   17958 C  CB    . SER A 1 3805 ? 146.623 196.324 177.701 1.00 42.58  ? 3805 SER A CB    1 
ATOM   17959 O  OG    . SER A 1 3805 ? 147.303 197.433 178.242 1.00 55.13  ? 3805 SER A OG    1 
ATOM   17960 N  N     . THR A 1 3806 ? 144.519 195.088 175.712 1.00 37.94  ? 3806 THR A N     1 
ATOM   17961 C  CA    . THR A 1 3806 ? 143.875 193.958 175.049 1.00 35.66  ? 3806 THR A CA    1 
ATOM   17962 C  C     . THR A 1 3806 ? 144.001 194.075 173.536 1.00 37.16  ? 3806 THR A C     1 
ATOM   17963 O  O     . THR A 1 3806 ? 144.221 193.074 172.842 1.00 39.86  ? 3806 THR A O     1 
ATOM   17964 C  CB    . THR A 1 3806 ? 142.406 193.865 175.457 1.00 40.23  ? 3806 THR A CB    1 
ATOM   17965 O  OG1   . THR A 1 3806 ? 141.715 195.045 175.030 1.00 50.89  ? 3806 THR A OG1   1 
ATOM   17966 C  CG2   . THR A 1 3806 ? 142.281 193.729 176.962 1.00 40.88  ? 3806 THR A CG2   1 
ATOM   17967 N  N     . ALA A 1 3807 ? 143.872 195.296 173.009 1.00 38.19  ? 3807 ALA A N     1 
ATOM   17968 C  CA    . ALA A 1 3807 ? 144.057 195.511 171.579 1.00 33.85  ? 3807 ALA A CA    1 
ATOM   17969 C  C     . ALA A 1 3807 ? 145.467 195.143 171.142 1.00 33.62  ? 3807 ALA A C     1 
ATOM   17970 O  O     . ALA A 1 3807 ? 145.651 194.513 170.098 1.00 35.34  ? 3807 ALA A O     1 
ATOM   17971 C  CB    . ALA A 1 3807 ? 143.749 196.964 171.222 1.00 31.66  ? 3807 ALA A CB    1 
ATOM   17972 N  N     . CYS A 1 3808 ? 146.477 195.533 171.924 1.00 34.95  ? 3808 CYS A N     1 
ATOM   17973 C  CA    . CYS A 1 3808 ? 147.854 195.192 171.577 1.00 31.59  ? 3808 CYS A CA    1 
ATOM   17974 C  C     . CYS A 1 3808 ? 148.068 193.686 171.573 1.00 33.37  ? 3808 CYS A C     1 
ATOM   17975 O  O     . CYS A 1 3808 ? 148.713 193.143 170.666 1.00 40.11  ? 3808 CYS A O     1 
ATOM   17976 C  CB    . CYS A 1 3808 ? 148.832 195.856 172.545 1.00 26.24  ? 3808 CYS A CB    1 
ATOM   17977 S  SG    . CYS A 1 3808 ? 148.717 197.642 172.649 1.00 55.11  ? 3808 CYS A SG    1 
ATOM   17978 N  N     . SER A 1 3809 ? 147.542 192.992 172.583 1.00 30.90  ? 3809 SER A N     1 
ATOM   17979 C  CA    . SER A 1 3809 ? 147.691 191.540 172.626 1.00 28.97  ? 3809 SER A CA    1 
ATOM   17980 C  C     . SER A 1 3809 ? 147.025 190.886 171.420 1.00 36.75  ? 3809 SER A C     1 
ATOM   17981 O  O     . SER A 1 3809 ? 147.610 190.008 170.768 1.00 38.74  ? 3809 SER A O     1 
ATOM   17982 C  CB    . SER A 1 3809 ? 147.109 190.995 173.928 1.00 33.43  ? 3809 SER A CB    1 
ATOM   17983 O  OG    . SER A 1 3809 ? 147.373 189.612 174.052 1.00 45.47  ? 3809 SER A OG    1 
ATOM   17984 N  N     . SER A 1 3810 ? 145.803 191.319 171.096 1.00 37.60  ? 3810 SER A N     1 
ATOM   17985 C  CA    . SER A 1 3810 ? 145.097 190.756 169.950 1.00 30.83  ? 3810 SER A CA    1 
ATOM   17986 C  C     . SER A 1 3810 ? 145.840 191.036 168.652 1.00 30.07  ? 3810 SER A C     1 
ATOM   17987 O  O     . SER A 1 3810 ? 145.932 190.162 167.781 1.00 36.90  ? 3810 SER A O     1 
ATOM   17988 C  CB    . SER A 1 3810 ? 143.677 191.314 169.886 1.00 34.30  ? 3810 SER A CB    1 
ATOM   17989 O  OG    . SER A 1 3810 ? 142.985 191.090 171.100 1.00 45.21  ? 3810 SER A OG    1 
ATOM   17990 N  N     . ILE A 1 3811 ? 146.376 192.249 168.504 1.00 28.87  ? 3811 ILE A N     1 
ATOM   17991 C  CA    . ILE A 1 3811 ? 147.111 192.602 167.293 1.00 28.12  ? 3811 ILE A CA    1 
ATOM   17992 C  C     . ILE A 1 3811 ? 148.337 191.717 167.142 1.00 29.79  ? 3811 ILE A C     1 
ATOM   17993 O  O     . ILE A 1 3811 ? 148.601 191.175 166.063 1.00 35.28  ? 3811 ILE A O     1 
ATOM   17994 C  CB    . ILE A 1 3811 ? 147.496 194.091 167.309 1.00 25.20  ? 3811 ILE A CB    1 
ATOM   17995 C  CG1   . ILE A 1 3811 ? 146.270 194.968 167.077 1.00 25.83  ? 3811 ILE A CG1   1 
ATOM   17996 C  CG2   . ILE A 1 3811 ? 148.546 194.379 166.255 1.00 26.58  ? 3811 ILE A CG2   1 
ATOM   17997 C  CD1   . ILE A 1 3811 ? 146.582 196.435 167.098 1.00 28.50  ? 3811 ILE A CD1   1 
ATOM   17998 N  N     . TYR A 1 3812 ? 149.102 191.548 168.224 1.00 30.40  ? 3812 TYR A N     1 
ATOM   17999 C  CA    . TYR A 1 3812 ? 150.304 190.729 168.122 1.00 28.24  ? 3812 TYR A CA    1 
ATOM   18000 C  C     . TYR A 1 3812 ? 149.962 189.288 167.789 1.00 32.53  ? 3812 TYR A C     1 
ATOM   18001 O  O     . TYR A 1 3812 ? 150.677 188.638 167.022 1.00 38.35  ? 3812 TYR A O     1 
ATOM   18002 C  CB    . TYR A 1 3812 ? 151.125 190.765 169.405 1.00 26.06  ? 3812 TYR A CB    1 
ATOM   18003 C  CG    . TYR A 1 3812 ? 152.132 189.635 169.432 1.00 28.37  ? 3812 TYR A CG    1 
ATOM   18004 C  CD1   . TYR A 1 3812 ? 153.168 189.584 168.509 1.00 34.28  ? 3812 TYR A CD1   1 
ATOM   18005 C  CD2   . TYR A 1 3812 ? 152.016 188.593 170.340 1.00 34.56  ? 3812 TYR A CD2   1 
ATOM   18006 C  CE1   . TYR A 1 3812 ? 154.073 188.546 168.511 1.00 37.02  ? 3812 TYR A CE1   1 
ATOM   18007 C  CE2   . TYR A 1 3812 ? 152.920 187.552 170.349 1.00 36.38  ? 3812 TYR A CE2   1 
ATOM   18008 C  CZ    . TYR A 1 3812 ? 153.945 187.534 169.433 1.00 37.47  ? 3812 TYR A CZ    1 
ATOM   18009 O  OH    . TYR A 1 3812 ? 154.848 186.498 169.440 1.00 44.77  ? 3812 TYR A OH    1 
ATOM   18010 N  N     . PHE A 1 3813 ? 148.892 188.754 168.373 1.00 35.80  ? 3813 PHE A N     1 
ATOM   18011 C  CA    . PHE A 1 3813 ? 148.602 187.349 168.113 1.00 35.99  ? 3813 PHE A CA    1 
ATOM   18012 C  C     . PHE A 1 3813 ? 148.008 187.141 166.726 1.00 44.40  ? 3813 PHE A C     1 
ATOM   18013 O  O     . PHE A 1 3813 ? 148.239 186.094 166.111 1.00 52.03  ? 3813 PHE A O     1 
ATOM   18014 C  CB    . PHE A 1 3813 ? 147.715 186.795 169.220 1.00 37.98  ? 3813 PHE A CB    1 
ATOM   18015 C  CG    . PHE A 1 3813 ? 148.495 186.391 170.430 1.00 39.75  ? 3813 PHE A CG    1 
ATOM   18016 C  CD1   . PHE A 1 3813 ? 149.236 185.224 170.426 1.00 43.26  ? 3813 PHE A CD1   1 
ATOM   18017 C  CD2   . PHE A 1 3813 ? 148.560 187.212 171.535 1.00 34.50  ? 3813 PHE A CD2   1 
ATOM   18018 C  CE1   . PHE A 1 3813 ? 149.980 184.860 171.521 1.00 40.36  ? 3813 PHE A CE1   1 
ATOM   18019 C  CE2   . PHE A 1 3813 ? 149.309 186.854 172.629 1.00 35.96  ? 3813 PHE A CE2   1 
ATOM   18020 C  CZ    . PHE A 1 3813 ? 150.017 185.676 172.623 1.00 40.05  ? 3813 PHE A CZ    1 
ATOM   18021 N  N     . THR A 1 3814 ? 147.296 188.136 166.191 1.00 43.51  ? 3814 THR A N     1 
ATOM   18022 C  CA    . THR A 1 3814 ? 146.944 188.106 164.775 1.00 38.16  ? 3814 THR A CA    1 
ATOM   18023 C  C     . THR A 1 3814 ? 148.195 188.103 163.904 1.00 37.40  ? 3814 THR A C     1 
ATOM   18024 O  O     . THR A 1 3814 ? 148.299 187.327 162.946 1.00 46.76  ? 3814 THR A O     1 
ATOM   18025 C  CB    . THR A 1 3814 ? 146.062 189.305 164.433 1.00 34.86  ? 3814 THR A CB    1 
ATOM   18026 O  OG1   . THR A 1 3814 ? 144.884 189.283 165.247 1.00 43.50  ? 3814 THR A OG1   1 
ATOM   18027 C  CG2   . THR A 1 3814 ? 145.661 189.271 162.976 1.00 39.78  ? 3814 THR A CG2   1 
ATOM   18028 N  N     . MET A 1 3815 ? 149.162 188.961 164.238 1.00 35.34  ? 3815 MET A N     1 
ATOM   18029 C  CA    . MET A 1 3815 ? 150.431 188.999 163.518 1.00 31.45  ? 3815 MET A CA    1 
ATOM   18030 C  C     . MET A 1 3815 ? 151.131 187.646 163.554 1.00 37.23  ? 3815 MET A C     1 
ATOM   18031 O  O     . MET A 1 3815 ? 151.651 187.177 162.537 1.00 42.15  ? 3815 MET A O     1 
ATOM   18032 C  CB    . MET A 1 3815 ? 151.324 190.074 164.134 1.00 30.64  ? 3815 MET A CB    1 
ATOM   18033 C  CG    . MET A 1 3815 ? 150.820 191.489 163.946 1.00 30.35  ? 3815 MET A CG    1 
ATOM   18034 S  SD    . MET A 1 3815 ? 151.857 192.690 164.795 1.00 37.07  ? 3815 MET A SD    1 
ATOM   18035 C  CE    . MET A 1 3815 ? 153.328 192.624 163.798 1.00 39.32  ? 3815 MET A CE    1 
ATOM   18036 N  N     . GLU A 1 3816 ? 151.163 187.015 164.727 1.00 40.90  ? 3816 GLU A N     1 
ATOM   18037 C  CA    . GLU A 1 3816 ? 151.811 185.716 164.866 1.00 46.12  ? 3816 GLU A CA    1 
ATOM   18038 C  C     . GLU A 1 3816 ? 151.089 184.648 164.057 1.00 47.47  ? 3816 GLU A C     1 
ATOM   18039 O  O     . GLU A 1 3816 ? 151.727 183.813 163.407 1.00 50.31  ? 3816 GLU A O     1 
ATOM   18040 C  CB    . GLU A 1 3816 ? 151.874 185.320 166.340 1.00 44.72  ? 3816 GLU A CB    1 
ATOM   18041 C  CG    . GLU A 1 3816 ? 152.383 183.912 166.582 1.00 54.36  ? 3816 GLU A CG    1 
ATOM   18042 C  CD    . GLU A 1 3816 ? 152.264 183.491 168.032 1.00 63.95  ? 3816 GLU A CD    1 
ATOM   18043 O  OE1   . GLU A 1 3816 ? 151.764 184.294 168.844 1.00 58.69  ? 3816 GLU A OE1   1 
ATOM   18044 O  OE2   . GLU A 1 3816 ? 152.669 182.356 168.359 1.00 67.32  ? 3816 GLU A OE2   1 
ATOM   18045 N  N     . SER A 1 3817 ? 149.755 184.656 164.084 1.00 45.31  ? 3817 SER A N     1 
ATOM   18046 C  CA    . SER A 1 3817 ? 148.984 183.676 163.335 1.00 43.82  ? 3817 SER A CA    1 
ATOM   18047 C  C     . SER A 1 3817 ? 149.011 183.926 161.835 1.00 42.29  ? 3817 SER A C     1 
ATOM   18048 O  O     . SER A 1 3817 ? 148.610 183.042 161.072 1.00 44.79  ? 3817 SER A O     1 
ATOM   18049 C  CB    . SER A 1 3817 ? 147.540 183.666 163.830 1.00 53.91  ? 3817 SER A CB    1 
ATOM   18050 O  OG    . SER A 1 3817 ? 147.476 183.283 165.190 1.00 70.86  ? 3817 SER A OG    1 
ATOM   18051 N  N     . LEU A 1 3818 ? 149.465 185.104 161.397 1.00 40.51  ? 3818 LEU A N     1 
ATOM   18052 C  CA    . LEU A 1 3818 ? 149.506 185.403 159.969 1.00 33.58  ? 3818 LEU A CA    1 
ATOM   18053 C  C     . LEU A 1 3818 ? 150.396 184.447 159.185 1.00 38.32  ? 3818 LEU A C     1 
ATOM   18054 O  O     . LEU A 1 3818 ? 150.273 184.380 157.958 1.00 37.62  ? 3818 LEU A O     1 
ATOM   18055 C  CB    . LEU A 1 3818 ? 149.988 186.835 159.739 1.00 30.62  ? 3818 LEU A CB    1 
ATOM   18056 C  CG    . LEU A 1 3818 ? 148.963 187.962 159.831 1.00 25.81  ? 3818 LEU A CG    1 
ATOM   18057 C  CD1   . LEU A 1 3818 ? 149.657 189.304 159.738 1.00 25.65  ? 3818 LEU A CD1   1 
ATOM   18058 C  CD2   . LEU A 1 3818 ? 147.917 187.823 158.746 1.00 29.58  ? 3818 LEU A CD2   1 
ATOM   18059 N  N     . LYS A 1 3819 ? 151.294 183.716 159.851 1.00 42.30  ? 3819 LYS A N     1 
ATOM   18060 C  CA    . LYS A 1 3819 ? 152.183 182.805 159.137 1.00 37.93  ? 3819 LYS A CA    1 
ATOM   18061 C  C     . LYS A 1 3819 ? 151.426 181.683 158.441 1.00 43.14  ? 3819 LYS A C     1 
ATOM   18062 O  O     . LYS A 1 3819 ? 151.979 181.041 157.542 1.00 49.51  ? 3819 LYS A O     1 
ATOM   18063 C  CB    . LYS A 1 3819 ? 153.213 182.200 160.089 1.00 37.47  ? 3819 LYS A CB    1 
ATOM   18064 C  CG    . LYS A 1 3819 ? 152.621 181.273 161.133 1.00 44.85  ? 3819 LYS A CG    1 
ATOM   18065 C  CD    . LYS A 1 3819 ? 153.703 180.650 161.992 1.00 50.01  ? 3819 LYS A CD    1 
ATOM   18066 C  CE    . LYS A 1 3819 ? 154.305 181.661 162.944 1.00 56.59  ? 3819 LYS A CE    1 
ATOM   18067 N  NZ    . LYS A 1 3819 ? 153.315 182.110 163.956 1.00 58.03  ? 3819 LYS A NZ    1 
ATOM   18068 N  N     . GLN A 1 3820 ? 150.181 181.423 158.842 1.00 45.75  ? 3820 GLN A N     1 
ATOM   18069 C  CA    . GLN A 1 3820 ? 149.396 180.378 158.196 1.00 46.30  ? 3820 GLN A CA    1 
ATOM   18070 C  C     . GLN A 1 3820 ? 148.912 180.808 156.818 1.00 43.63  ? 3820 GLN A C     1 
ATOM   18071 O  O     . GLN A 1 3820 ? 148.768 179.967 155.923 1.00 49.25  ? 3820 GLN A O     1 
ATOM   18072 C  CB    . GLN A 1 3820 ? 148.218 179.994 159.087 1.00 46.84  ? 3820 GLN A CB    1 
ATOM   18073 C  CG    . GLN A 1 3820 ? 148.627 179.592 160.491 1.00 53.45  ? 3820 GLN A CG    1 
ATOM   18074 C  CD    . GLN A 1 3820 ? 147.516 179.786 161.498 1.00 67.74  ? 3820 GLN A CD    1 
ATOM   18075 O  OE1   . GLN A 1 3820 ? 147.743 179.730 162.706 1.00 78.46  ? 3820 GLN A OE1   1 
ATOM   18076 N  NE2   . GLN A 1 3820 ? 146.307 180.019 161.007 1.00 62.90  ? 3820 GLN A NE2   1 
ATOM   18077 N  N     . ILE A 1 3821 ? 148.650 182.102 156.631 1.00 41.13  ? 3821 ILE A N     1 
ATOM   18078 C  CA    . ILE A 1 3821 ? 148.241 182.604 155.324 1.00 41.35  ? 3821 ILE A CA    1 
ATOM   18079 C  C     . ILE A 1 3821 ? 149.358 182.430 154.304 1.00 41.67  ? 3821 ILE A C     1 
ATOM   18080 O  O     . ILE A 1 3821 ? 149.120 181.996 153.171 1.00 48.02  ? 3821 ILE A O     1 
ATOM   18081 C  CB    . ILE A 1 3821 ? 147.804 184.075 155.437 1.00 39.16  ? 3821 ILE A CB    1 
ATOM   18082 C  CG1   . ILE A 1 3821 ? 146.715 184.216 156.494 1.00 39.89  ? 3821 ILE A CG1   1 
ATOM   18083 C  CG2   . ILE A 1 3821 ? 147.333 184.600 154.102 1.00 43.94  ? 3821 ILE A CG2   1 
ATOM   18084 C  CD1   . ILE A 1 3821 ? 145.588 183.231 156.318 1.00 46.16  ? 3821 ILE A CD1   1 
ATOM   18085 N  N     . HIS A 1 3822 ? 150.588 182.762 154.684 1.00 38.52  ? 3822 HIS A N     1 
ATOM   18086 C  CA    . HIS A 1 3822 ? 151.715 182.710 153.770 1.00 36.38  ? 3822 HIS A CA    1 
ATOM   18087 C  C     . HIS A 1 3822 ? 152.982 182.522 154.588 1.00 41.38  ? 3822 HIS A C     1 
ATOM   18088 O  O     . HIS A 1 3822 ? 153.052 182.933 155.748 1.00 42.33  ? 3822 HIS A O     1 
ATOM   18089 C  CB    . HIS A 1 3822 ? 151.788 183.984 152.922 1.00 36.98  ? 3822 HIS A CB    1 
ATOM   18090 C  CG    . HIS A 1 3822 ? 152.699 183.883 151.741 1.00 37.71  ? 3822 HIS A CG    1 
ATOM   18091 N  ND1   . HIS A 1 3822 ? 153.792 184.704 151.572 1.00 44.86  ? 3822 HIS A ND1   1 
ATOM   18092 C  CD2   . HIS A 1 3822 ? 152.668 183.071 150.658 1.00 41.17  ? 3822 HIS A CD2   1 
ATOM   18093 C  CE1   . HIS A 1 3822 ? 154.402 184.396 150.442 1.00 46.24  ? 3822 HIS A CE1   1 
ATOM   18094 N  NE2   . HIS A 1 3822 ? 153.739 183.408 149.868 1.00 49.45  ? 3822 HIS A NE2   1 
ATOM   18095 N  N     . PHE A 1 3823 ? 153.988 181.895 153.976 1.00 46.44  ? 3823 PHE A N     1 
ATOM   18096 C  CA    . PHE A 1 3823 ? 155.207 181.581 154.711 1.00 42.88  ? 3823 PHE A CA    1 
ATOM   18097 C  C     . PHE A 1 3823 ? 156.064 182.810 154.981 1.00 42.09  ? 3823 PHE A C     1 
ATOM   18098 O  O     . PHE A 1 3823 ? 156.914 182.767 155.876 1.00 49.24  ? 3823 PHE A O     1 
ATOM   18099 C  CB    . PHE A 1 3823 ? 156.018 180.518 153.964 1.00 47.05  ? 3823 PHE A CB    1 
ATOM   18100 C  CG    . PHE A 1 3823 ? 156.320 180.868 152.535 1.00 49.16  ? 3823 PHE A CG    1 
ATOM   18101 C  CD1   . PHE A 1 3823 ? 157.353 181.732 152.219 1.00 51.94  ? 3823 PHE A CD1   1 
ATOM   18102 C  CD2   . PHE A 1 3823 ? 155.573 180.324 151.507 1.00 46.74  ? 3823 PHE A CD2   1 
ATOM   18103 C  CE1   . PHE A 1 3823 ? 157.629 182.051 150.907 1.00 53.48  ? 3823 PHE A CE1   1 
ATOM   18104 C  CE2   . PHE A 1 3823 ? 155.846 180.639 150.194 1.00 47.61  ? 3823 PHE A CE2   1 
ATOM   18105 C  CZ    . PHE A 1 3823 ? 156.875 181.503 149.895 1.00 52.48  ? 3823 PHE A CZ    1 
ATOM   18106 N  N     . LEU A 1 3824 ? 155.871 183.899 154.235 1.00 39.83  ? 3824 LEU A N     1 
ATOM   18107 C  CA    . LEU A 1 3824 ? 156.636 185.115 154.481 1.00 38.49  ? 3824 LEU A CA    1 
ATOM   18108 C  C     . LEU A 1 3824 ? 156.149 185.891 155.693 1.00 42.55  ? 3824 LEU A C     1 
ATOM   18109 O  O     . LEU A 1 3824 ? 156.837 186.821 156.125 1.00 43.93  ? 3824 LEU A O     1 
ATOM   18110 C  CB    . LEU A 1 3824 ? 156.586 186.044 153.269 1.00 36.67  ? 3824 LEU A CB    1 
ATOM   18111 C  CG    . LEU A 1 3824 ? 157.435 185.743 152.040 1.00 50.02  ? 3824 LEU A CG    1 
ATOM   18112 C  CD1   . LEU A 1 3824 ? 157.204 186.834 151.019 1.00 54.16  ? 3824 LEU A CD1   1 
ATOM   18113 C  CD2   . LEU A 1 3824 ? 158.901 185.652 152.405 1.00 51.37  ? 3824 LEU A CD2   1 
ATOM   18114 N  N     . TYR A 1 3825 ? 154.992 185.545 156.248 1.00 40.44  ? 3825 TYR A N     1 
ATOM   18115 C  CA    . TYR A 1 3825 ? 154.364 186.369 157.279 1.00 34.99  ? 3825 TYR A CA    1 
ATOM   18116 C  C     . TYR A 1 3825 ? 154.862 185.957 158.664 1.00 38.45  ? 3825 TYR A C     1 
ATOM   18117 O  O     . TYR A 1 3825 ? 154.099 185.609 159.564 1.00 42.39  ? 3825 TYR A O     1 
ATOM   18118 C  CB    . TYR A 1 3825 ? 152.846 186.278 157.176 1.00 34.83  ? 3825 TYR A CB    1 
ATOM   18119 C  CG    . TYR A 1 3825 ? 152.272 186.691 155.834 1.00 32.55  ? 3825 TYR A CG    1 
ATOM   18120 C  CD1   . TYR A 1 3825 ? 153.070 187.262 154.851 1.00 33.44  ? 3825 TYR A CD1   1 
ATOM   18121 C  CD2   . TYR A 1 3825 ? 150.930 186.505 155.552 1.00 32.77  ? 3825 TYR A CD2   1 
ATOM   18122 C  CE1   . TYR A 1 3825 ? 152.551 187.626 153.632 1.00 31.86  ? 3825 TYR A CE1   1 
ATOM   18123 C  CE2   . TYR A 1 3825 ? 150.401 186.874 154.337 1.00 34.05  ? 3825 TYR A CE2   1 
ATOM   18124 C  CZ    . TYR A 1 3825 ? 151.216 187.432 153.380 1.00 31.73  ? 3825 TYR A CZ    1 
ATOM   18125 O  OH    . TYR A 1 3825 ? 150.693 187.801 152.165 1.00 36.59  ? 3825 TYR A OH    1 
ATOM   18126 N  N     . GLN A 1 3826 ? 156.182 186.006 158.819 1.00 38.28  ? 3826 GLN A N     1 
ATOM   18127 C  CA    . GLN A 1 3826 ? 156.846 185.668 160.074 1.00 42.02  ? 3826 GLN A CA    1 
ATOM   18128 C  C     . GLN A 1 3826 ? 157.168 186.971 160.794 1.00 41.20  ? 3826 GLN A C     1 
ATOM   18129 O  O     . GLN A 1 3826 ? 158.085 187.698 160.405 1.00 44.19  ? 3826 GLN A O     1 
ATOM   18130 C  CB    . GLN A 1 3826 ? 158.099 184.840 159.817 1.00 41.67  ? 3826 GLN A CB    1 
ATOM   18131 C  CG    . GLN A 1 3826 ? 157.926 183.803 158.728 1.00 39.13  ? 3826 GLN A CG    1 
ATOM   18132 C  CD    . GLN A 1 3826 ? 157.331 182.514 159.244 1.00 45.98  ? 3826 GLN A CD    1 
ATOM   18133 O  OE1   . GLN A 1 3826 ? 157.203 182.317 160.450 1.00 48.98  ? 3826 GLN A OE1   1 
ATOM   18134 N  NE2   . GLN A 1 3826 ? 156.953 181.630 158.331 1.00 47.39  ? 3826 GLN A NE2   1 
ATOM   18135 N  N     . TYR A 1 3827 ? 156.407 187.268 161.842 1.00 38.14  ? 3827 TYR A N     1 
ATOM   18136 C  CA    . TYR A 1 3827 ? 156.564 188.494 162.609 1.00 39.18  ? 3827 TYR A CA    1 
ATOM   18137 C  C     . TYR A 1 3827 ? 156.850 188.137 164.059 1.00 47.25  ? 3827 TYR A C     1 
ATOM   18138 O  O     . TYR A 1 3827 ? 156.038 187.475 164.712 1.00 58.96  ? 3827 TYR A O     1 
ATOM   18139 C  CB    . TYR A 1 3827 ? 155.311 189.367 162.501 1.00 35.40  ? 3827 TYR A CB    1 
ATOM   18140 C  CG    . TYR A 1 3827 ? 154.938 189.683 161.072 1.00 34.15  ? 3827 TYR A CG    1 
ATOM   18141 C  CD1   . TYR A 1 3827 ? 155.742 190.496 160.289 1.00 36.79  ? 3827 TYR A CD1   1 
ATOM   18142 C  CD2   . TYR A 1 3827 ? 153.793 189.151 160.500 1.00 34.78  ? 3827 TYR A CD2   1 
ATOM   18143 C  CE1   . TYR A 1 3827 ? 155.412 190.778 158.981 1.00 36.97  ? 3827 TYR A CE1   1 
ATOM   18144 C  CE2   . TYR A 1 3827 ? 153.454 189.429 159.193 1.00 36.17  ? 3827 TYR A CE2   1 
ATOM   18145 C  CZ    . TYR A 1 3827 ? 154.268 190.242 158.438 1.00 37.65  ? 3827 TYR A CZ    1 
ATOM   18146 O  OH    . TYR A 1 3827 ? 153.937 190.523 157.135 1.00 41.34  ? 3827 TYR A OH    1 
ATOM   18147 N  N     . SER A 1 3828 ? 157.999 188.579 164.556 1.00 42.11  ? 3828 SER A N     1 
ATOM   18148 C  CA    . SER A 1 3828 ? 158.446 188.271 165.904 1.00 42.70  ? 3828 SER A CA    1 
ATOM   18149 C  C     . SER A 1 3828 ? 157.774 189.187 166.917 1.00 42.25  ? 3828 SER A C     1 
ATOM   18150 O  O     . SER A 1 3828 ? 157.157 190.195 166.568 1.00 45.55  ? 3828 SER A O     1 
ATOM   18151 C  CB    . SER A 1 3828 ? 159.966 188.401 166.012 1.00 44.37  ? 3828 SER A CB    1 
ATOM   18152 O  OG    . SER A 1 3828 ? 160.380 189.736 165.786 1.00 50.41  ? 3828 SER A OG    1 
ATOM   18153 N  N     . LEU A 1 3829 ? 157.897 188.813 168.192 1.00 37.53  ? 3829 LEU A N     1 
ATOM   18154 C  CA    . LEU A 1 3829 ? 157.364 189.653 169.259 1.00 36.26  ? 3829 LEU A CA    1 
ATOM   18155 C  C     . LEU A 1 3829 ? 158.114 190.974 169.340 1.00 39.79  ? 3829 LEU A C     1 
ATOM   18156 O  O     . LEU A 1 3829 ? 157.522 192.013 169.651 1.00 44.36  ? 3829 LEU A O     1 
ATOM   18157 C  CB    . LEU A 1 3829 ? 157.428 188.916 170.595 1.00 35.81  ? 3829 LEU A CB    1 
ATOM   18158 C  CG    . LEU A 1 3829 ? 156.851 189.671 171.794 1.00 34.63  ? 3829 LEU A CG    1 
ATOM   18159 C  CD1   . LEU A 1 3829 ? 155.376 189.941 171.597 1.00 32.74  ? 3829 LEU A CD1   1 
ATOM   18160 C  CD2   . LEU A 1 3829 ? 157.084 188.893 173.073 1.00 42.40  ? 3829 LEU A CD2   1 
ATOM   18161 N  N     . GLN A 1 3830 ? 159.420 190.955 169.070 1.00 39.54  ? 3830 GLN A N     1 
ATOM   18162 C  CA    . GLN A 1 3830 ? 160.194 192.191 169.092 1.00 40.22  ? 3830 GLN A CA    1 
ATOM   18163 C  C     . GLN A 1 3830 ? 159.736 193.146 167.998 1.00 42.17  ? 3830 GLN A C     1 
ATOM   18164 O  O     . GLN A 1 3830 ? 159.800 194.367 168.166 1.00 50.14  ? 3830 GLN A O     1 
ATOM   18165 C  CB    . GLN A 1 3830 ? 161.683 191.881 168.951 1.00 47.15  ? 3830 GLN A CB    1 
ATOM   18166 C  CG    . GLN A 1 3830 ? 162.588 193.095 169.089 1.00 52.75  ? 3830 GLN A CG    1 
ATOM   18167 C  CD    . GLN A 1 3830 ? 162.225 193.962 170.278 1.00 55.96  ? 3830 GLN A CD    1 
ATOM   18168 O  OE1   . GLN A 1 3830 ? 162.182 193.491 171.414 1.00 61.38  ? 3830 GLN A OE1   1 
ATOM   18169 N  NE2   . GLN A 1 3830 ? 161.965 195.238 170.022 1.00 49.38  ? 3830 GLN A NE2   1 
ATOM   18170 N  N     . PHE A 1 3831 ? 159.265 192.611 166.870 1.00 37.80  ? 3831 PHE A N     1 
ATOM   18171 C  CA    . PHE A 1 3831 ? 158.750 193.465 165.804 1.00 35.24  ? 3831 PHE A CA    1 
ATOM   18172 C  C     . PHE A 1 3831 ? 157.490 194.196 166.255 1.00 38.95  ? 3831 PHE A C     1 
ATOM   18173 O  O     . PHE A 1 3831 ? 157.345 195.409 166.045 1.00 46.41  ? 3831 PHE A O     1 
ATOM   18174 C  CB    . PHE A 1 3831 ? 158.485 192.619 164.558 1.00 37.00  ? 3831 PHE A CB    1 
ATOM   18175 C  CG    . PHE A 1 3831 ? 157.863 193.377 163.423 1.00 39.14  ? 3831 PHE A CG    1 
ATOM   18176 C  CD1   . PHE A 1 3831 ? 158.540 194.418 162.815 1.00 46.36  ? 3831 PHE A CD1   1 
ATOM   18177 C  CD2   . PHE A 1 3831 ? 156.614 193.032 162.947 1.00 35.69  ? 3831 PHE A CD2   1 
ATOM   18178 C  CE1   . PHE A 1 3831 ? 157.974 195.110 161.766 1.00 47.16  ? 3831 PHE A CE1   1 
ATOM   18179 C  CE2   . PHE A 1 3831 ? 156.044 193.722 161.898 1.00 37.73  ? 3831 PHE A CE2   1 
ATOM   18180 C  CZ    . PHE A 1 3831 ? 156.724 194.761 161.308 1.00 43.15  ? 3831 PHE A CZ    1 
ATOM   18181 N  N     . PHE A 1 3832 ? 156.573 193.474 166.904 1.00 39.52  ? 3832 PHE A N     1 
ATOM   18182 C  CA    . PHE A 1 3832 ? 155.388 194.121 167.455 1.00 35.44  ? 3832 PHE A CA    1 
ATOM   18183 C  C     . PHE A 1 3832 ? 155.756 195.120 168.540 1.00 35.73  ? 3832 PHE A C     1 
ATOM   18184 O  O     . PHE A 1 3832 ? 155.142 196.185 168.642 1.00 41.37  ? 3832 PHE A O     1 
ATOM   18185 C  CB    . PHE A 1 3832 ? 154.413 193.092 168.014 1.00 28.54  ? 3832 PHE A CB    1 
ATOM   18186 C  CG    . PHE A 1 3832 ? 153.254 193.713 168.730 1.00 30.37  ? 3832 PHE A CG    1 
ATOM   18187 C  CD1   . PHE A 1 3832 ? 152.320 194.462 168.037 1.00 33.26  ? 3832 PHE A CD1   1 
ATOM   18188 C  CD2   . PHE A 1 3832 ? 153.122 193.590 170.099 1.00 34.00  ? 3832 PHE A CD2   1 
ATOM   18189 C  CE1   . PHE A 1 3832 ? 151.263 195.050 168.690 1.00 29.71  ? 3832 PHE A CE1   1 
ATOM   18190 C  CE2   . PHE A 1 3832 ? 152.065 194.178 170.758 1.00 37.32  ? 3832 PHE A CE2   1 
ATOM   18191 C  CZ    . PHE A 1 3832 ? 151.136 194.909 170.051 1.00 33.88  ? 3832 PHE A CZ    1 
ATOM   18192 N  N     . LEU A 1 3833 ? 156.733 194.783 169.383 1.00 36.82  ? 3833 LEU A N     1 
ATOM   18193 C  CA    . LEU A 1 3833 ? 157.156 195.719 170.418 1.00 35.41  ? 3833 LEU A CA    1 
ATOM   18194 C  C     . LEU A 1 3833 ? 157.764 196.978 169.817 1.00 42.69  ? 3833 LEU A C     1 
ATOM   18195 O  O     . LEU A 1 3833 ? 157.576 198.069 170.357 1.00 46.64  ? 3833 LEU A O     1 
ATOM   18196 C  CB    . LEU A 1 3833 ? 158.142 195.047 171.370 1.00 39.66  ? 3833 LEU A CB    1 
ATOM   18197 C  CG    . LEU A 1 3833 ? 157.565 193.932 172.243 1.00 41.15  ? 3833 LEU A CG    1 
ATOM   18198 C  CD1   . LEU A 1 3833 ? 158.583 193.477 173.272 1.00 45.28  ? 3833 LEU A CD1   1 
ATOM   18199 C  CD2   . LEU A 1 3833 ? 156.285 194.392 172.920 1.00 40.66  ? 3833 LEU A CD2   1 
ATOM   18200 N  N     . ASP A 1 3834 ? 158.497 196.849 168.710 1.00 46.66  ? 3834 ASP A N     1 
ATOM   18201 C  CA    . ASP A 1 3834 ? 159.001 198.027 168.012 1.00 43.51  ? 3834 ASP A CA    1 
ATOM   18202 C  C     . ASP A 1 3834 ? 157.856 198.875 167.475 1.00 43.19  ? 3834 ASP A C     1 
ATOM   18203 O  O     . ASP A 1 3834 ? 157.868 200.105 167.610 1.00 45.00  ? 3834 ASP A O     1 
ATOM   18204 C  CB    . ASP A 1 3834 ? 159.936 197.600 166.880 1.00 48.24  ? 3834 ASP A CB    1 
ATOM   18205 C  CG    . ASP A 1 3834 ? 160.608 198.777 166.202 1.00 79.36  ? 3834 ASP A CG    1 
ATOM   18206 O  OD1   . ASP A 1 3834 ? 161.531 199.365 166.805 1.00 93.75  ? 3834 ASP A OD1   1 
ATOM   18207 O  OD2   . ASP A 1 3834 ? 160.216 199.115 165.065 1.00 81.61  ? 3834 ASP A OD2   1 
ATOM   18208 N  N     . ILE A 1 3835 ? 156.850 198.231 166.874 1.00 39.96  ? 3835 ILE A N     1 
ATOM   18209 C  CA    . ILE A 1 3835 ? 155.654 198.949 166.430 1.00 38.06  ? 3835 ILE A CA    1 
ATOM   18210 C  C     . ILE A 1 3835 ? 155.022 199.700 167.594 1.00 40.12  ? 3835 ILE A C     1 
ATOM   18211 O  O     . ILE A 1 3835 ? 154.640 200.872 167.478 1.00 45.26  ? 3835 ILE A O     1 
ATOM   18212 C  CB    . ILE A 1 3835 ? 154.649 197.965 165.800 1.00 31.51  ? 3835 ILE A CB    1 
ATOM   18213 C  CG1   . ILE A 1 3835 ? 155.205 197.360 164.513 1.00 37.12  ? 3835 ILE A CG1   1 
ATOM   18214 C  CG2   . ILE A 1 3835 ? 153.319 198.647 165.551 1.00 26.55  ? 3835 ILE A CG2   1 
ATOM   18215 C  CD1   . ILE A 1 3835 ? 154.274 196.360 163.874 1.00 35.12  ? 3835 ILE A CD1   1 
ATOM   18216 N  N     . TYR A 1 3836 ? 154.915 199.031 168.736 1.00 40.28  ? 3836 TYR A N     1 
ATOM   18217 C  CA    . TYR A 1 3836 ? 154.211 199.565 169.893 1.00 35.10  ? 3836 TYR A CA    1 
ATOM   18218 C  C     . TYR A 1 3836 ? 154.975 200.717 170.539 1.00 42.80  ? 3836 TYR A C     1 
ATOM   18219 O  O     . TYR A 1 3836 ? 154.372 201.711 170.963 1.00 48.23  ? 3836 TYR A O     1 
ATOM   18220 C  CB    . TYR A 1 3836 ? 153.971 198.410 170.858 1.00 33.66  ? 3836 TYR A CB    1 
ATOM   18221 C  CG    . TYR A 1 3836 ? 153.336 198.739 172.171 1.00 40.11  ? 3836 TYR A CG    1 
ATOM   18222 C  CD1   . TYR A 1 3836 ? 152.009 199.129 172.254 1.00 38.93  ? 3836 TYR A CD1   1 
ATOM   18223 C  CD2   . TYR A 1 3836 ? 154.045 198.576 173.345 1.00 45.25  ? 3836 TYR A CD2   1 
ATOM   18224 C  CE1   . TYR A 1 3836 ? 151.433 199.403 173.470 1.00 35.46  ? 3836 TYR A CE1   1 
ATOM   18225 C  CE2   . TYR A 1 3836 ? 153.477 198.840 174.551 1.00 45.32  ? 3836 TYR A CE2   1 
ATOM   18226 C  CZ    . TYR A 1 3836 ? 152.178 199.249 174.612 1.00 44.57  ? 3836 TYR A CZ    1 
ATOM   18227 O  OH    . TYR A 1 3836 ? 151.645 199.498 175.841 1.00 49.73  ? 3836 TYR A OH    1 
ATOM   18228 N  N     . HIS A 1 3837 ? 156.304 200.615 170.608 1.00 44.89  ? 3837 HIS A N     1 
ATOM   18229 C  CA    . HIS A 1 3837 ? 157.104 201.728 171.105 1.00 43.77  ? 3837 HIS A CA    1 
ATOM   18230 C  C     . HIS A 1 3837 ? 157.078 202.902 170.135 1.00 48.47  ? 3837 HIS A C     1 
ATOM   18231 O  O     . HIS A 1 3837 ? 157.119 204.062 170.559 1.00 54.63  ? 3837 HIS A O     1 
ATOM   18232 C  CB    . HIS A 1 3837 ? 158.541 201.280 171.370 1.00 49.30  ? 3837 HIS A CB    1 
ATOM   18233 C  CG    . HIS A 1 3837 ? 158.676 200.325 172.516 1.00 55.32  ? 3837 HIS A CG    1 
ATOM   18234 N  ND1   . HIS A 1 3837 ? 158.292 200.647 173.799 1.00 58.83  ? 3837 HIS A ND1   1 
ATOM   18235 C  CD2   . HIS A 1 3837 ? 159.173 199.068 172.577 1.00 48.64  ? 3837 HIS A CD2   1 
ATOM   18236 C  CE1   . HIS A 1 3837 ? 158.530 199.622 174.598 1.00 57.40  ? 3837 HIS A CE1   1 
ATOM   18237 N  NE2   . HIS A 1 3837 ? 159.065 198.651 173.881 1.00 50.45  ? 3837 HIS A NE2   1 
ATOM   18238 N  N     . ASN A 1 3838 ? 157.022 202.625 168.828 1.00 45.90  ? 3838 ASN A N     1 
ATOM   18239 C  CA    . ASN A 1 3838 ? 156.832 203.700 167.860 1.00 43.26  ? 3838 ASN A CA    1 
ATOM   18240 C  C     . ASN A 1 3838 ? 155.517 204.423 168.109 1.00 45.55  ? 3838 ASN A C     1 
ATOM   18241 O  O     . ASN A 1 3838 ? 155.461 205.658 168.085 1.00 51.64  ? 3838 ASN A O     1 
ATOM   18242 C  CB    . ASN A 1 3838 ? 156.871 203.134 166.439 1.00 43.39  ? 3838 ASN A CB    1 
ATOM   18243 C  CG    . ASN A 1 3838 ? 156.760 204.210 165.373 1.00 53.57  ? 3838 ASN A CG    1 
ATOM   18244 O  OD1   . ASN A 1 3838 ? 156.816 205.403 165.663 1.00 55.93  ? 3838 ASN A OD1   1 
ATOM   18245 N  ND2   . ASN A 1 3838 ? 156.594 203.786 164.127 1.00 53.05  ? 3838 ASN A ND2   1 
ATOM   18246 N  N     . VAL A 1 3839 ? 154.451 203.666 168.359 1.00 43.16  ? 3839 VAL A N     1 
ATOM   18247 C  CA    . VAL A 1 3839 ? 153.152 204.271 168.629 1.00 40.99  ? 3839 VAL A CA    1 
ATOM   18248 C  C     . VAL A 1 3839 ? 153.190 205.078 169.922 1.00 44.96  ? 3839 VAL A C     1 
ATOM   18249 O  O     . VAL A 1 3839 ? 152.549 206.129 170.033 1.00 47.30  ? 3839 VAL A O     1 
ATOM   18250 C  CB    . VAL A 1 3839 ? 152.065 203.184 168.666 1.00 37.26  ? 3839 VAL A CB    1 
ATOM   18251 C  CG1   . VAL A 1 3839 ? 150.743 203.763 169.122 1.00 40.10  ? 3839 VAL A CG1   1 
ATOM   18252 C  CG2   . VAL A 1 3839 ? 151.925 202.550 167.299 1.00 40.14  ? 3839 VAL A CG2   1 
ATOM   18253 N  N     . LEU A 1 3840 ? 153.946 204.609 170.916 1.00 47.49  ? 3840 LEU A N     1 
ATOM   18254 C  CA    . LEU A 1 3840 ? 153.942 205.265 172.221 1.00 45.06  ? 3840 LEU A CA    1 
ATOM   18255 C  C     . LEU A 1 3840 ? 154.837 206.500 172.247 1.00 45.23  ? 3840 LEU A C     1 
ATOM   18256 O  O     . LEU A 1 3840 ? 154.372 207.609 172.527 1.00 48.38  ? 3840 LEU A O     1 
ATOM   18257 C  CB    . LEU A 1 3840 ? 154.372 204.277 173.306 1.00 42.59  ? 3840 LEU A CB    1 
ATOM   18258 C  CG    . LEU A 1 3840 ? 153.301 203.330 173.840 1.00 35.04  ? 3840 LEU A CG    1 
ATOM   18259 C  CD1   . LEU A 1 3840 ? 153.913 202.368 174.835 1.00 41.95  ? 3840 LEU A CD1   1 
ATOM   18260 C  CD2   . LEU A 1 3840 ? 152.173 204.113 174.475 1.00 40.22  ? 3840 LEU A CD2   1 
ATOM   18261 N  N     . TYR A 1 3841 ? 156.129 206.329 171.967 1.00 47.60  ? 3841 TYR A N     1 
ATOM   18262 C  CA    . TYR A 1 3841 ? 157.104 207.382 172.240 1.00 49.63  ? 3841 TYR A CA    1 
ATOM   18263 C  C     . TYR A 1 3841 ? 157.326 208.310 171.047 1.00 56.95  ? 3841 TYR A C     1 
ATOM   18264 O  O     . TYR A 1 3841 ? 157.074 209.515 171.140 1.00 62.70  ? 3841 TYR A O     1 
ATOM   18265 C  CB    . TYR A 1 3841 ? 158.425 206.753 172.689 1.00 48.41  ? 3841 TYR A CB    1 
ATOM   18266 C  CG    . TYR A 1 3841 ? 158.275 205.883 173.913 1.00 47.94  ? 3841 TYR A CG    1 
ATOM   18267 C  CD1   . TYR A 1 3841 ? 157.894 206.428 175.130 1.00 43.15  ? 3841 TYR A CD1   1 
ATOM   18268 C  CD2   . TYR A 1 3841 ? 158.501 204.516 173.850 1.00 46.05  ? 3841 TYR A CD2   1 
ATOM   18269 C  CE1   . TYR A 1 3841 ? 157.750 205.640 176.250 1.00 46.90  ? 3841 TYR A CE1   1 
ATOM   18270 C  CE2   . TYR A 1 3841 ? 158.359 203.719 174.966 1.00 48.02  ? 3841 TYR A CE2   1 
ATOM   18271 C  CZ    . TYR A 1 3841 ? 157.982 204.286 176.163 1.00 53.55  ? 3841 TYR A CZ    1 
ATOM   18272 O  OH    . TYR A 1 3841 ? 157.839 203.496 177.280 1.00 59.90  ? 3841 TYR A OH    1 
ATOM   18273 N  N     . GLU A 1 3842 ? 157.799 207.771 169.925 1.00 53.94  ? 3842 GLU A N     1 
ATOM   18274 C  CA    . GLU A 1 3842 ? 158.070 208.593 168.745 1.00 57.39  ? 3842 GLU A CA    1 
ATOM   18275 C  C     . GLU A 1 3842 ? 156.850 208.643 167.819 1.00 61.90  ? 3842 GLU A C     1 
ATOM   18276 O  O     . GLU A 1 3842 ? 156.885 208.288 166.642 1.00 65.53  ? 3842 GLU A O     1 
ATOM   18277 C  CB    . GLU A 1 3842 ? 159.329 208.104 168.030 1.00 55.31  ? 3842 GLU A CB    1 
ATOM   18278 C  CG    . GLU A 1 3842 ? 159.283 206.701 167.443 1.00 58.37  ? 3842 GLU A CG    1 
ATOM   18279 C  CD    . GLU A 1 3842 ? 159.691 205.640 168.442 1.00 63.93  ? 3842 GLU A CD    1 
ATOM   18280 O  OE1   . GLU A 1 3842 ? 159.715 205.939 169.654 1.00 64.79  ? 3842 GLU A OE1   1 
ATOM   18281 O  OE2   . GLU A 1 3842 ? 160.002 204.509 168.014 1.00 61.24  ? 3842 GLU A OE2   1 
ATOM   18282 N  N     . ASN A 1 3843 ? 155.751 209.128 168.389 1.00 61.38  ? 3843 ASN A N     1 
ATOM   18283 C  CA    . ASN A 1 3843 ? 154.519 209.358 167.646 1.00 61.91  ? 3843 ASN A CA    1 
ATOM   18284 C  C     . ASN A 1 3843 ? 154.340 210.855 167.443 1.00 71.59  ? 3843 ASN A C     1 
ATOM   18285 O  O     . ASN A 1 3843 ? 154.028 211.570 168.409 1.00 75.09  ? 3843 ASN A O     1 
ATOM   18286 C  CB    . ASN A 1 3843 ? 153.322 208.774 168.396 1.00 58.19  ? 3843 ASN A CB    1 
ATOM   18287 C  CG    . ASN A 1 3843 ? 152.068 208.725 167.549 1.00 61.27  ? 3843 ASN A CG    1 
ATOM   18288 O  OD1   . ASN A 1 3843 ? 152.078 209.107 166.380 1.00 67.41  ? 3843 ASN A OD1   1 
ATOM   18289 N  ND2   . ASN A 1 3843 ? 150.976 208.252 168.137 1.00 56.80  ? 3843 ASN A ND2   1 
ATOM   18290 N  N     . PRO A 1 3844 ? 154.529 211.379 166.230 1.00 76.03  ? 3844 PRO A N     1 
ATOM   18291 C  CA    . PRO A 1 3844 ? 154.383 212.830 166.027 1.00 77.05  ? 3844 PRO A CA    1 
ATOM   18292 C  C     . PRO A 1 3844 ? 152.981 213.347 166.294 1.00 74.93  ? 3844 PRO A C     1 
ATOM   18293 O  O     . PRO A 1 3844 ? 152.818 214.547 166.544 1.00 78.57  ? 3844 PRO A O     1 
ATOM   18294 C  CB    . PRO A 1 3844 ? 154.783 213.021 164.558 1.00 77.26  ? 3844 PRO A CB    1 
ATOM   18295 C  CG    . PRO A 1 3844 ? 154.559 211.687 163.927 1.00 78.70  ? 3844 PRO A CG    1 
ATOM   18296 C  CD    . PRO A 1 3844 ? 154.888 210.679 164.986 1.00 75.27  ? 3844 PRO A CD    1 
ATOM   18297 N  N     . ASN A 1 3845 ? 151.963 212.486 166.245 1.00 67.81  ? 3845 ASN A N     1 
ATOM   18298 C  CA    . ASN A 1 3845 ? 150.607 212.934 166.538 1.00 69.12  ? 3845 ASN A CA    1 
ATOM   18299 C  C     . ASN A 1 3845 ? 150.449 213.331 168.000 1.00 75.83  ? 3845 ASN A C     1 
ATOM   18300 O  O     . ASN A 1 3845 ? 149.643 214.212 168.318 1.00 77.73  ? 3845 ASN A O     1 
ATOM   18301 C  CB    . ASN A 1 3845 ? 149.604 211.840 166.176 1.00 67.84  ? 3845 ASN A CB    1 
ATOM   18302 C  CG    . ASN A 1 3845 ? 149.265 211.826 164.702 1.00 74.75  ? 3845 ASN A CG    1 
ATOM   18303 O  OD1   . ASN A 1 3845 ? 150.136 211.636 163.855 1.00 78.91  ? 3845 ASN A OD1   1 
ATOM   18304 N  ND2   . ASN A 1 3845 ? 147.991 212.028 164.388 1.00 72.70  ? 3845 ASN A ND2   1 
ATOM   18305 N  N     . LEU A 1 3846 ? 151.203 212.693 168.898 1.00 75.42  ? 3846 LEU A N     1 
ATOM   18306 C  CA    . LEU A 1 3846 ? 151.083 212.978 170.323 1.00 68.92  ? 3846 LEU A CA    1 
ATOM   18307 C  C     . LEU A 1 3846 ? 151.712 214.309 170.710 1.00 72.05  ? 3846 LEU A C     1 
ATOM   18308 O  O     . LEU A 1 3846 ? 151.447 214.806 171.809 1.00 75.61  ? 3846 LEU A O     1 
ATOM   18309 C  CB    . LEU A 1 3846 ? 151.720 211.855 171.139 1.00 64.47  ? 3846 LEU A CB    1 
ATOM   18310 C  CG    . LEU A 1 3846 ? 150.979 210.521 171.167 1.00 55.10  ? 3846 LEU A CG    1 
ATOM   18311 C  CD1   . LEU A 1 3846 ? 151.762 209.509 171.976 1.00 55.30  ? 3846 LEU A CD1   1 
ATOM   18312 C  CD2   . LEU A 1 3846 ? 149.588 210.702 171.738 1.00 56.65  ? 3846 LEU A CD2   1 
ATOM   18313 N  N     . LYS A 1 3847 ? 152.550 214.886 169.853 1.00 72.65  ? 3847 LYS A N     1 
ATOM   18314 C  CA    . LYS A 1 3847 ? 153.181 216.156 170.185 1.00 78.95  ? 3847 LYS A CA    1 
ATOM   18315 C  C     . LYS A 1 3847 ? 152.148 217.274 170.198 1.00 82.89  ? 3847 LYS A C     1 
ATOM   18316 O  O     . LYS A 1 3847 ? 151.409 217.467 169.228 1.00 83.45  ? 3847 LYS A O     1 
ATOM   18317 C  CB    . LYS A 1 3847 ? 154.295 216.469 169.187 1.00 83.07  ? 3847 LYS A CB    1 
ATOM   18318 C  CG    . LYS A 1 3847 ? 155.477 215.517 169.269 1.00 89.68  ? 3847 LYS A CG    1 
ATOM   18319 C  CD    . LYS A 1 3847 ? 156.577 215.906 168.296 1.00 97.48  ? 3847 LYS A CD    1 
ATOM   18320 C  CE    . LYS A 1 3847 ? 157.717 214.901 168.328 1.00 102.88 ? 3847 LYS A CE    1 
ATOM   18321 N  NZ    . LYS A 1 3847 ? 158.449 214.928 169.624 1.00 99.89  ? 3847 LYS A NZ    1 
ATOM   18322 N  N     . GLY A 1 3848 ? 152.104 218.017 171.303 1.00 83.16  ? 3848 GLY A N     1 
ATOM   18323 C  CA    . GLY A 1 3848 ? 151.182 219.114 171.476 1.00 82.55  ? 3848 GLY A CA    1 
ATOM   18324 C  C     . GLY A 1 3848 ? 149.957 218.793 172.309 1.00 82.97  ? 3848 GLY A C     1 
ATOM   18325 O  O     . GLY A 1 3848 ? 149.521 219.637 173.098 1.00 84.58  ? 3848 GLY A O     1 
ATOM   18326 N  N     . VAL A 1 3849 ? 149.393 217.599 172.160 1.00 79.13  ? 3849 VAL A N     1 
ATOM   18327 C  CA    . VAL A 1 3849 ? 148.200 217.225 172.913 1.00 76.57  ? 3849 VAL A CA    1 
ATOM   18328 C  C     . VAL A 1 3849 ? 148.610 216.802 174.317 1.00 73.09  ? 3849 VAL A C     1 
ATOM   18329 O  O     . VAL A 1 3849 ? 149.560 216.030 174.498 1.00 71.04  ? 3849 VAL A O     1 
ATOM   18330 C  CB    . VAL A 1 3849 ? 147.419 216.117 172.187 1.00 71.43  ? 3849 VAL A CB    1 
ATOM   18331 C  CG1   . VAL A 1 3849 ? 148.301 214.912 171.913 1.00 71.06  ? 3849 VAL A CG1   1 
ATOM   18332 C  CG2   . VAL A 1 3849 ? 146.196 215.715 172.992 1.00 69.17  ? 3849 VAL A CG2   1 
ATOM   18333 N  N     . THR A 1 3850 ? 147.909 217.328 175.321 1.00 74.78  ? 3850 THR A N     1 
ATOM   18334 C  CA    . THR A 1 3850 ? 148.253 217.095 176.717 1.00 75.52  ? 3850 THR A CA    1 
ATOM   18335 C  C     . THR A 1 3850 ? 147.216 216.295 177.488 1.00 73.41  ? 3850 THR A C     1 
ATOM   18336 O  O     . THR A 1 3850 ? 147.583 215.587 178.427 1.00 75.86  ? 3850 THR A O     1 
ATOM   18337 C  CB    . THR A 1 3850 ? 148.478 218.428 177.440 1.00 79.23  ? 3850 THR A CB    1 
ATOM   18338 O  OG1   . THR A 1 3850 ? 147.316 219.255 177.295 1.00 79.58  ? 3850 THR A OG1   1 
ATOM   18339 C  CG2   . THR A 1 3850 ? 149.685 219.150 176.865 1.00 78.04  ? 3850 THR A CG2   1 
ATOM   18340 N  N     . ASP A 1 3851 ? 145.938 216.393 177.127 1.00 71.23  ? 3851 ASP A N     1 
ATOM   18341 C  CA    . ASP A 1 3851 ? 144.900 215.670 177.849 1.00 74.18  ? 3851 ASP A CA    1 
ATOM   18342 C  C     . ASP A 1 3851 ? 145.112 214.166 177.720 1.00 72.55  ? 3851 ASP A C     1 
ATOM   18343 O  O     . ASP A 1 3851 ? 145.442 213.659 176.645 1.00 73.80  ? 3851 ASP A O     1 
ATOM   18344 C  CB    . ASP A 1 3851 ? 143.518 216.060 177.327 1.00 77.33  ? 3851 ASP A CB    1 
ATOM   18345 C  CG    . ASP A 1 3851 ? 142.405 215.251 177.963 1.00 83.38  ? 3851 ASP A CG    1 
ATOM   18346 O  OD1   . ASP A 1 3851 ? 142.301 215.258 179.207 1.00 86.32  ? 3851 ASP A OD1   1 
ATOM   18347 O  OD2   . ASP A 1 3851 ? 141.630 214.614 177.219 1.00 81.82  ? 3851 ASP A OD2   1 
ATOM   18348 N  N     . HIS A 1 3852 ? 144.922 213.452 178.831 1.00 71.44  ? 3852 HIS A N     1 
ATOM   18349 C  CA    . HIS A 1 3852 ? 145.251 212.031 178.862 1.00 71.37  ? 3852 HIS A CA    1 
ATOM   18350 C  C     . HIS A 1 3852 ? 144.305 211.213 177.992 1.00 69.00  ? 3852 HIS A C     1 
ATOM   18351 O  O     . HIS A 1 3852 ? 144.738 210.273 177.315 1.00 70.51  ? 3852 HIS A O     1 
ATOM   18352 C  CB    . HIS A 1 3852 ? 145.235 211.522 180.303 1.00 75.05  ? 3852 HIS A CB    1 
ATOM   18353 C  CG    . HIS A 1 3852 ? 146.377 212.025 181.129 1.00 76.50  ? 3852 HIS A CG    1 
ATOM   18354 N  ND1   . HIS A 1 3852 ? 146.197 212.731 182.299 1.00 74.14  ? 3852 HIS A ND1   1 
ATOM   18355 C  CD2   . HIS A 1 3852 ? 147.716 211.936 180.946 1.00 72.02  ? 3852 HIS A CD2   1 
ATOM   18356 C  CE1   . HIS A 1 3852 ? 147.375 213.049 182.805 1.00 75.98  ? 3852 HIS A CE1   1 
ATOM   18357 N  NE2   . HIS A 1 3852 ? 148.313 212.579 182.003 1.00 75.68  ? 3852 HIS A NE2   1 
ATOM   18358 N  N     . THR A 1 3853 ? 143.012 211.545 178.000 1.00 68.73  ? 3853 THR A N     1 
ATOM   18359 C  CA    . THR A 1 3853 ? 142.057 210.797 177.187 1.00 72.44  ? 3853 THR A CA    1 
ATOM   18360 C  C     . THR A 1 3853 ? 142.335 210.977 175.699 1.00 67.30  ? 3853 THR A C     1 
ATOM   18361 O  O     . THR A 1 3853 ? 142.286 210.010 174.928 1.00 65.30  ? 3853 THR A O     1 
ATOM   18362 C  CB    . THR A 1 3853 ? 140.629 211.228 177.522 1.00 79.62  ? 3853 THR A CB    1 
ATOM   18363 O  OG1   . THR A 1 3853 ? 140.398 211.068 178.926 1.00 84.50  ? 3853 THR A OG1   1 
ATOM   18364 C  CG2   . THR A 1 3853 ? 139.627 210.381 176.756 1.00 74.41  ? 3853 THR A CG2   1 
ATOM   18365 N  N     . GLN A 1 3854 ? 142.627 212.210 175.277 1.00 68.89  ? 3854 GLN A N     1 
ATOM   18366 C  CA    . GLN A 1 3854 ? 142.943 212.453 173.874 1.00 65.15  ? 3854 GLN A CA    1 
ATOM   18367 C  C     . GLN A 1 3854 ? 144.215 211.726 173.463 1.00 58.61  ? 3854 GLN A C     1 
ATOM   18368 O  O     . GLN A 1 3854 ? 144.281 211.145 172.373 1.00 61.34  ? 3854 GLN A O     1 
ATOM   18369 C  CB    . GLN A 1 3854 ? 143.075 213.952 173.613 1.00 66.57  ? 3854 GLN A CB    1 
ATOM   18370 C  CG    . GLN A 1 3854 ? 141.800 214.739 173.856 1.00 77.77  ? 3854 GLN A CG    1 
ATOM   18371 C  CD    . GLN A 1 3854 ? 142.004 216.234 173.713 1.00 87.37  ? 3854 GLN A CD    1 
ATOM   18372 O  OE1   . GLN A 1 3854 ? 143.105 216.697 173.419 1.00 88.04  ? 3854 GLN A OE1   1 
ATOM   18373 N  NE2   . GLN A 1 3854 ? 140.938 216.998 173.922 1.00 89.68  ? 3854 GLN A NE2   1 
ATOM   18374 N  N     . ARG A 1 3855 ? 145.239 211.750 174.319 1.00 54.65  ? 3855 ARG A N     1 
ATOM   18375 C  CA    . ARG A 1 3855 ? 146.474 211.037 174.011 1.00 49.25  ? 3855 ARG A CA    1 
ATOM   18376 C  C     . ARG A 1 3855 ? 146.236 209.537 173.914 1.00 46.22  ? 3855 ARG A C     1 
ATOM   18377 O  O     . ARG A 1 3855 ? 146.801 208.868 173.044 1.00 49.18  ? 3855 ARG A O     1 
ATOM   18378 C  CB    . ARG A 1 3855 ? 147.540 211.343 175.061 1.00 52.76  ? 3855 ARG A CB    1 
ATOM   18379 C  CG    . ARG A 1 3855 ? 148.055 212.768 175.033 1.00 55.71  ? 3855 ARG A CG    1 
ATOM   18380 C  CD    . ARG A 1 3855 ? 148.983 213.027 176.204 1.00 56.56  ? 3855 ARG A CD    1 
ATOM   18381 N  NE    . ARG A 1 3855 ? 150.144 212.144 176.197 1.00 56.00  ? 3855 ARG A NE    1 
ATOM   18382 C  CZ    . ARG A 1 3855 ? 151.185 212.279 175.388 1.00 55.54  ? 3855 ARG A CZ    1 
ATOM   18383 N  NH1   . ARG A 1 3855 ? 151.257 213.267 174.512 1.00 55.87  ? 3855 ARG A NH1   1 
ATOM   18384 N  NH2   . ARG A 1 3855 ? 152.183 211.404 175.465 1.00 59.35  ? 3855 ARG A NH2   1 
ATOM   18385 N  N     . LEU A 1 3856 ? 145.405 208.987 174.802 1.00 44.72  ? 3856 LEU A N     1 
ATOM   18386 C  CA    . LEU A 1 3856 ? 145.105 207.560 174.738 1.00 43.93  ? 3856 LEU A CA    1 
ATOM   18387 C  C     . LEU A 1 3856 ? 144.354 207.210 173.458 1.00 47.88  ? 3856 LEU A C     1 
ATOM   18388 O  O     . LEU A 1 3856 ? 144.629 206.181 172.831 1.00 47.62  ? 3856 LEU A O     1 
ATOM   18389 C  CB    . LEU A 1 3856 ? 144.307 207.135 175.969 1.00 44.33  ? 3856 LEU A CB    1 
ATOM   18390 C  CG    . LEU A 1 3856 ? 143.690 205.736 175.936 1.00 40.14  ? 3856 LEU A CG    1 
ATOM   18391 C  CD1   . LEU A 1 3856 ? 144.763 204.676 175.764 1.00 28.25  ? 3856 LEU A CD1   1 
ATOM   18392 C  CD2   . LEU A 1 3856 ? 142.882 205.483 177.194 1.00 44.12  ? 3856 LEU A CD2   1 
ATOM   18393 N  N     . SER A 1 3857 ? 143.400 208.053 173.053 1.00 48.93  ? 3857 SER A N     1 
ATOM   18394 C  CA    . SER A 1 3857 ? 142.686 207.810 171.802 1.00 47.78  ? 3857 SER A CA    1 
ATOM   18395 C  C     . SER A 1 3857 ? 143.628 207.878 170.605 1.00 48.48  ? 3857 SER A C     1 
ATOM   18396 O  O     . SER A 1 3857 ? 143.543 207.051 169.686 1.00 49.51  ? 3857 SER A O     1 
ATOM   18397 C  CB    . SER A 1 3857 ? 141.547 208.816 171.645 1.00 50.89  ? 3857 SER A CB    1 
ATOM   18398 O  OG    . SER A 1 3857 ? 140.579 208.652 172.665 1.00 65.27  ? 3857 SER A OG    1 
ATOM   18399 N  N     . ILE A 1 3858 ? 144.533 208.859 170.600 1.00 47.66  ? 3858 ILE A N     1 
ATOM   18400 C  CA    . ILE A 1 3858 ? 145.507 208.981 169.518 1.00 40.70  ? 3858 ILE A CA    1 
ATOM   18401 C  C     . ILE A 1 3858 ? 146.406 207.753 169.469 1.00 41.75  ? 3858 ILE A C     1 
ATOM   18402 O  O     . ILE A 1 3858 ? 146.697 207.222 168.390 1.00 48.65  ? 3858 ILE A O     1 
ATOM   18403 C  CB    . ILE A 1 3858 ? 146.323 210.275 169.685 1.00 42.75  ? 3858 ILE A CB    1 
ATOM   18404 C  CG1   . ILE A 1 3858 ? 145.432 211.499 169.480 1.00 48.40  ? 3858 ILE A CG1   1 
ATOM   18405 C  CG2   . ILE A 1 3858 ? 147.486 210.302 168.721 1.00 50.42  ? 3858 ILE A CG2   1 
ATOM   18406 C  CD1   . ILE A 1 3858 ? 146.179 212.810 169.550 1.00 57.52  ? 3858 ILE A CD1   1 
ATOM   18407 N  N     . ILE A 1 3859 ? 146.861 207.286 170.633 1.00 42.06  ? 3859 ILE A N     1 
ATOM   18408 C  CA    . ILE A 1 3859 ? 147.695 206.089 170.687 1.00 41.47  ? 3859 ILE A CA    1 
ATOM   18409 C  C     . ILE A 1 3859 ? 146.930 204.883 170.163 1.00 44.31  ? 3859 ILE A C     1 
ATOM   18410 O  O     . ILE A 1 3859 ? 147.478 204.057 169.428 1.00 48.57  ? 3859 ILE A O     1 
ATOM   18411 C  CB    . ILE A 1 3859 ? 148.203 205.853 172.121 1.00 41.48  ? 3859 ILE A CB    1 
ATOM   18412 C  CG1   . ILE A 1 3859 ? 149.248 206.898 172.496 1.00 45.56  ? 3859 ILE A CG1   1 
ATOM   18413 C  CG2   . ILE A 1 3859 ? 148.787 204.460 172.264 1.00 36.53  ? 3859 ILE A CG2   1 
ATOM   18414 C  CD1   . ILE A 1 3859 ? 149.491 206.982 173.972 1.00 41.16  ? 3859 ILE A CD1   1 
ATOM   18415 N  N     . THR A 1 3860 ? 145.657 204.754 170.539 1.00 43.54  ? 3860 THR A N     1 
ATOM   18416 C  CA    . THR A 1 3860 ? 144.871 203.608 170.095 1.00 41.50  ? 3860 THR A CA    1 
ATOM   18417 C  C     . THR A 1 3860 ? 144.686 203.612 168.582 1.00 43.94  ? 3860 THR A C     1 
ATOM   18418 O  O     . THR A 1 3860 ? 144.792 202.564 167.936 1.00 45.16  ? 3860 THR A O     1 
ATOM   18419 C  CB    . THR A 1 3860 ? 143.518 203.591 170.801 1.00 45.68  ? 3860 THR A CB    1 
ATOM   18420 O  OG1   . THR A 1 3860 ? 143.708 203.837 172.199 1.00 42.07  ? 3860 THR A OG1   1 
ATOM   18421 C  CG2   . THR A 1 3860 ? 142.852 202.240 170.624 1.00 48.55  ? 3860 THR A CG2   1 
ATOM   18422 N  N     . LYS A 1 3861 ? 144.403 204.779 167.998 1.00 42.17  ? 3861 LYS A N     1 
ATOM   18423 C  CA    . LYS A 1 3861 ? 144.285 204.859 166.543 1.00 39.23  ? 3861 LYS A CA    1 
ATOM   18424 C  C     . LYS A 1 3861 ? 145.611 204.533 165.866 1.00 45.09  ? 3861 LYS A C     1 
ATOM   18425 O  O     . LYS A 1 3861 ? 145.673 203.706 164.941 1.00 49.34  ? 3861 LYS A O     1 
ATOM   18426 C  CB    . LYS A 1 3861 ? 143.807 206.249 166.124 1.00 37.66  ? 3861 LYS A CB    1 
ATOM   18427 C  CG    . LYS A 1 3861 ? 142.483 206.674 166.722 1.00 50.51  ? 3861 LYS A CG    1 
ATOM   18428 C  CD    . LYS A 1 3861 ? 142.244 208.159 166.499 1.00 56.50  ? 3861 LYS A CD    1 
ATOM   18429 C  CE    . LYS A 1 3861 ? 140.952 208.620 167.153 1.00 64.63  ? 3861 LYS A CE    1 
ATOM   18430 N  NZ    . LYS A 1 3861 ? 140.770 210.093 167.036 1.00 59.72  ? 3861 LYS A NZ    1 
ATOM   18431 N  N     . ASP A 1 3862 ? 146.690 205.173 166.321 1.00 42.94  ? 3862 ASP A N     1 
ATOM   18432 C  CA    . ASP A 1 3862 ? 147.985 204.980 165.690 1.00 36.37  ? 3862 ASP A CA    1 
ATOM   18433 C  C     . ASP A 1 3862 ? 148.519 203.573 165.883 1.00 34.04  ? 3862 ASP A C     1 
ATOM   18434 O  O     . ASP A 1 3862 ? 149.325 203.126 165.071 1.00 36.70  ? 3862 ASP A O     1 
ATOM   18435 C  CB    . ASP A 1 3862 ? 148.991 205.998 166.220 1.00 41.07  ? 3862 ASP A CB    1 
ATOM   18436 C  CG    . ASP A 1 3862 ? 148.704 207.402 165.734 1.00 58.39  ? 3862 ASP A CG    1 
ATOM   18437 O  OD1   . ASP A 1 3862 ? 148.495 207.581 164.516 1.00 61.58  ? 3862 ASP A OD1   1 
ATOM   18438 O  OD2   . ASP A 1 3862 ? 148.697 208.331 166.567 1.00 58.58  ? 3862 ASP A OD2   1 
ATOM   18439 N  N     . LEU A 1 3863 ? 148.078 202.855 166.915 1.00 33.15  ? 3863 LEU A N     1 
ATOM   18440 C  CA    . LEU A 1 3863 ? 148.510 201.473 167.079 1.00 30.99  ? 3863 LEU A CA    1 
ATOM   18441 C  C     . LEU A 1 3863 ? 148.055 200.624 165.903 1.00 30.43  ? 3863 LEU A C     1 
ATOM   18442 O  O     . LEU A 1 3863 ? 148.865 199.953 165.255 1.00 31.94  ? 3863 LEU A O     1 
ATOM   18443 C  CB    . LEU A 1 3863 ? 147.969 200.910 168.391 1.00 36.35  ? 3863 LEU A CB    1 
ATOM   18444 C  CG    . LEU A 1 3863 ? 148.154 199.408 168.598 1.00 30.59  ? 3863 LEU A CG    1 
ATOM   18445 C  CD1   . LEU A 1 3863 ? 149.612 199.067 168.852 1.00 29.97  ? 3863 LEU A CD1   1 
ATOM   18446 C  CD2   . LEU A 1 3863 ? 147.272 198.923 169.726 1.00 30.75  ? 3863 LEU A CD2   1 
ATOM   18447 N  N     . PHE A 1 3864 ? 146.757 200.671 165.594 1.00 30.81  ? 3864 PHE A N     1 
ATOM   18448 C  CA    . PHE A 1 3864 ? 146.237 199.939 164.446 1.00 28.57  ? 3864 PHE A CA    1 
ATOM   18449 C  C     . PHE A 1 3864 ? 146.846 200.449 163.149 1.00 29.90  ? 3864 PHE A C     1 
ATOM   18450 O  O     . PHE A 1 3864 ? 147.231 199.655 162.280 1.00 34.11  ? 3864 PHE A O     1 
ATOM   18451 C  CB    . PHE A 1 3864 ? 144.715 200.059 164.403 1.00 28.26  ? 3864 PHE A CB    1 
ATOM   18452 C  CG    . PHE A 1 3864 ? 144.014 199.273 165.469 1.00 28.13  ? 3864 PHE A CG    1 
ATOM   18453 C  CD1   . PHE A 1 3864 ? 143.830 197.911 165.338 1.00 28.17  ? 3864 PHE A CD1   1 
ATOM   18454 C  CD2   . PHE A 1 3864 ? 143.549 199.898 166.610 1.00 29.80  ? 3864 PHE A CD2   1 
ATOM   18455 C  CE1   . PHE A 1 3864 ? 143.187 197.189 166.319 1.00 30.57  ? 3864 PHE A CE1   1 
ATOM   18456 C  CE2   . PHE A 1 3864 ? 142.908 199.181 167.595 1.00 30.79  ? 3864 PHE A CE2   1 
ATOM   18457 C  CZ    . PHE A 1 3864 ? 142.727 197.825 167.450 1.00 33.55  ? 3864 PHE A CZ    1 
ATOM   18458 N  N     . GLN A 1 3865 ? 146.955 201.774 163.004 1.00 31.97  ? 3865 GLN A N     1 
ATOM   18459 C  CA    . GLN A 1 3865 ? 147.484 202.326 161.760 1.00 31.15  ? 3865 GLN A CA    1 
ATOM   18460 C  C     . GLN A 1 3865 ? 148.920 201.874 161.516 1.00 30.11  ? 3865 GLN A C     1 
ATOM   18461 O  O     . GLN A 1 3865 ? 149.258 201.411 160.422 1.00 32.62  ? 3865 GLN A O     1 
ATOM   18462 C  CB    . GLN A 1 3865 ? 147.395 203.851 161.781 1.00 36.88  ? 3865 GLN A CB    1 
ATOM   18463 C  CG    . GLN A 1 3865 ? 147.881 204.494 160.500 1.00 42.59  ? 3865 GLN A CG    1 
ATOM   18464 C  CD    . GLN A 1 3865 ? 146.999 204.160 159.318 1.00 49.83  ? 3865 GLN A CD    1 
ATOM   18465 O  OE1   . GLN A 1 3865 ? 145.824 204.522 159.285 1.00 54.58  ? 3865 GLN A OE1   1 
ATOM   18466 N  NE2   . GLN A 1 3865 ? 147.558 203.457 158.343 1.00 48.58  ? 3865 GLN A NE2   1 
ATOM   18467 N  N     . VAL A 1 3866 ? 149.779 201.993 162.531 1.00 28.26  ? 3866 VAL A N     1 
ATOM   18468 C  CA    . VAL A 1 3866 ? 151.182 201.629 162.383 1.00 25.05  ? 3866 VAL A CA    1 
ATOM   18469 C  C     . VAL A 1 3866 ? 151.336 200.122 162.237 1.00 26.39  ? 3866 VAL A C     1 
ATOM   18470 O  O     . VAL A 1 3866 ? 152.196 199.651 161.488 1.00 30.78  ? 3866 VAL A O     1 
ATOM   18471 C  CB    . VAL A 1 3866 ? 152.002 202.179 163.564 1.00 27.79  ? 3866 VAL A CB    1 
ATOM   18472 C  CG1   . VAL A 1 3866 ? 153.425 201.660 163.516 1.00 29.95  ? 3866 VAL A CG1   1 
ATOM   18473 C  CG2   . VAL A 1 3866 ? 152.002 203.695 163.539 1.00 31.63  ? 3866 VAL A CG2   1 
ATOM   18474 N  N     . ALA A 1 3867 ? 150.518 199.336 162.942 1.00 26.23  ? 3867 ALA A N     1 
ATOM   18475 C  CA    . ALA A 1 3867 ? 150.580 197.889 162.773 1.00 24.08  ? 3867 ALA A CA    1 
ATOM   18476 C  C     . ALA A 1 3867 ? 150.280 197.501 161.333 1.00 29.38  ? 3867 ALA A C     1 
ATOM   18477 O  O     . ALA A 1 3867 ? 151.012 196.709 160.724 1.00 33.39  ? 3867 ALA A O     1 
ATOM   18478 C  CB    . ALA A 1 3867 ? 149.608 197.205 163.733 1.00 20.85  ? 3867 ALA A CB    1 
ATOM   18479 N  N     . PHE A 1 3868 ? 149.219 198.075 160.758 1.00 27.67  ? 3868 PHE A N     1 
ATOM   18480 C  CA    . PHE A 1 3868 ? 148.908 197.793 159.361 1.00 23.56  ? 3868 PHE A CA    1 
ATOM   18481 C  C     . PHE A 1 3868 ? 150.017 198.274 158.436 1.00 27.44  ? 3868 PHE A C     1 
ATOM   18482 O  O     . PHE A 1 3868 ? 150.421 197.553 157.520 1.00 38.79  ? 3868 PHE A O     1 
ATOM   18483 C  CB    . PHE A 1 3868 ? 147.578 198.431 158.970 1.00 28.45  ? 3868 PHE A CB    1 
ATOM   18484 C  CG    . PHE A 1 3868 ? 147.162 198.131 157.560 1.00 33.49  ? 3868 PHE A CG    1 
ATOM   18485 C  CD1   . PHE A 1 3868 ? 146.752 196.860 157.203 1.00 30.27  ? 3868 PHE A CD1   1 
ATOM   18486 C  CD2   . PHE A 1 3868 ? 147.195 199.114 156.589 1.00 34.05  ? 3868 PHE A CD2   1 
ATOM   18487 C  CE1   . PHE A 1 3868 ? 146.377 196.579 155.909 1.00 28.42  ? 3868 PHE A CE1   1 
ATOM   18488 C  CE2   . PHE A 1 3868 ? 146.822 198.835 155.294 1.00 32.15  ? 3868 PHE A CE2   1 
ATOM   18489 C  CZ    . PHE A 1 3868 ? 146.412 197.567 154.955 1.00 30.54  ? 3868 PHE A CZ    1 
ATOM   18490 N  N     . ASN A 1 3869 ? 150.534 199.482 158.665 1.00 24.95  ? 3869 ASN A N     1 
ATOM   18491 C  CA    . ASN A 1 3869 ? 151.571 200.015 157.786 1.00 24.76  ? 3869 ASN A CA    1 
ATOM   18492 C  C     . ASN A 1 3869 ? 152.823 199.148 157.811 1.00 30.56  ? 3869 ASN A C     1 
ATOM   18493 O  O     . ASN A 1 3869 ? 153.443 198.911 156.768 1.00 37.62  ? 3869 ASN A O     1 
ATOM   18494 C  CB    . ASN A 1 3869 ? 151.908 201.451 158.183 1.00 27.44  ? 3869 ASN A CB    1 
ATOM   18495 C  CG    . ASN A 1 3869 ? 150.805 202.424 157.836 1.00 39.27  ? 3869 ASN A CG    1 
ATOM   18496 O  OD1   . ASN A 1 3869 ? 149.812 202.056 157.213 1.00 44.42  ? 3869 ASN A OD1   1 
ATOM   18497 N  ND2   . ASN A 1 3869 ? 150.975 203.677 158.238 1.00 41.65  ? 3869 ASN A ND2   1 
ATOM   18498 N  N     . ARG A 1 3870 ? 153.214 198.667 158.992 1.00 27.31  ? 3870 ARG A N     1 
ATOM   18499 C  CA    . ARG A 1 3870 ? 154.417 197.851 159.098 1.00 26.24  ? 3870 ARG A CA    1 
ATOM   18500 C  C     . ARG A 1 3870 ? 154.203 196.460 158.516 1.00 30.41  ? 3870 ARG A C     1 
ATOM   18501 O  O     . ARG A 1 3870 ? 155.106 195.907 157.880 1.00 40.72  ? 3870 ARG A O     1 
ATOM   18502 C  CB    . ARG A 1 3870 ? 154.861 197.748 160.557 1.00 31.40  ? 3870 ARG A CB    1 
ATOM   18503 C  CG    . ARG A 1 3870 ? 155.197 199.069 161.223 1.00 33.96  ? 3870 ARG A CG    1 
ATOM   18504 C  CD    . ARG A 1 3870 ? 156.512 199.639 160.737 1.00 42.52  ? 3870 ARG A CD    1 
ATOM   18505 N  NE    . ARG A 1 3870 ? 157.067 200.603 161.680 1.00 52.98  ? 3870 ARG A NE    1 
ATOM   18506 C  CZ    . ARG A 1 3870 ? 157.632 200.284 162.836 1.00 51.01  ? 3870 ARG A CZ    1 
ATOM   18507 N  NH1   . ARG A 1 3870 ? 157.757 199.025 163.221 1.00 44.99  ? 3870 ARG A NH1   1 
ATOM   18508 N  NH2   . ARG A 1 3870 ? 158.092 201.252 163.622 1.00 44.75  ? 3870 ARG A NH2   1 
ATOM   18509 N  N     . VAL A 1 3871 ? 153.023 195.872 158.722 1.00 29.33  ? 3871 VAL A N     1 
ATOM   18510 C  CA    . VAL A 1 3871 ? 152.829 194.484 158.315 1.00 29.97  ? 3871 VAL A CA    1 
ATOM   18511 C  C     . VAL A 1 3871 ? 152.481 194.390 156.835 1.00 33.60  ? 3871 VAL A C     1 
ATOM   18512 O  O     . VAL A 1 3871 ? 153.106 193.630 156.087 1.00 41.43  ? 3871 VAL A O     1 
ATOM   18513 C  CB    . VAL A 1 3871 ? 151.756 193.815 159.190 1.00 27.01  ? 3871 VAL A CB    1 
ATOM   18514 C  CG1   . VAL A 1 3871 ? 151.427 192.439 158.655 1.00 25.43  ? 3871 VAL A CG1   1 
ATOM   18515 C  CG2   . VAL A 1 3871 ? 152.233 193.726 160.618 1.00 30.33  ? 3871 VAL A CG2   1 
ATOM   18516 N  N     . ALA A 1 3872 ? 151.482 195.154 156.386 1.00 31.15  ? 3872 ALA A N     1 
ATOM   18517 C  CA    . ALA A 1 3872 ? 151.014 195.058 155.010 1.00 29.21  ? 3872 ALA A CA    1 
ATOM   18518 C  C     . ALA A 1 3872 ? 152.079 195.448 153.996 1.00 36.56  ? 3872 ALA A C     1 
ATOM   18519 O  O     . ALA A 1 3872 ? 151.963 195.074 152.825 1.00 47.04  ? 3872 ALA A O     1 
ATOM   18520 C  CB    . ALA A 1 3872 ? 149.771 195.923 154.824 1.00 30.42  ? 3872 ALA A CB    1 
ATOM   18521 N  N     . ARG A 1 3873 ? 153.105 196.193 154.408 1.00 37.60  ? 3873 ARG A N     1 
ATOM   18522 C  CA    . ARG A 1 3873 ? 154.246 196.412 153.530 1.00 36.55  ? 3873 ARG A CA    1 
ATOM   18523 C  C     . ARG A 1 3873 ? 155.016 195.126 153.276 1.00 34.33  ? 3873 ARG A C     1 
ATOM   18524 O  O     . ARG A 1 3873 ? 155.746 195.039 152.284 1.00 41.19  ? 3873 ARG A O     1 
ATOM   18525 C  CB    . ARG A 1 3873 ? 155.172 197.473 154.122 1.00 39.48  ? 3873 ARG A CB    1 
ATOM   18526 C  CG    . ARG A 1 3873 ? 154.788 198.890 153.749 1.00 50.27  ? 3873 ARG A CG    1 
ATOM   18527 C  CD    . ARG A 1 3873 ? 155.028 199.143 152.273 1.00 59.75  ? 3873 ARG A CD    1 
ATOM   18528 N  NE    . ARG A 1 3873 ? 154.648 200.493 151.876 1.00 70.24  ? 3873 ARG A NE    1 
ATOM   18529 C  CZ    . ARG A 1 3873 ? 153.825 200.773 150.876 1.00 72.50  ? 3873 ARG A CZ    1 
ATOM   18530 N  NH1   . ARG A 1 3873 ? 153.283 199.817 150.139 1.00 66.61  ? 3873 ARG A NH1   1 
ATOM   18531 N  NH2   . ARG A 1 3873 ? 153.540 202.044 150.605 1.00 73.97  ? 3873 ARG A NH2   1 
ATOM   18532 N  N     . GLY A 1 3874 ? 154.870 194.131 154.149 1.00 32.36  ? 3874 GLY A N     1 
ATOM   18533 C  CA    . GLY A 1 3874 ? 155.473 192.831 153.957 1.00 32.02  ? 3874 GLY A CA    1 
ATOM   18534 C  C     . GLY A 1 3874 ? 154.533 191.732 153.519 1.00 33.74  ? 3874 GLY A C     1 
ATOM   18535 O  O     . GLY A 1 3874 ? 154.929 190.559 153.545 1.00 40.76  ? 3874 GLY A O     1 
ATOM   18536 N  N     . MET A 1 3875 ? 153.301 192.050 153.128 1.00 35.30  ? 3875 MET A N     1 
ATOM   18537 C  CA    . MET A 1 3875 ? 152.370 191.056 152.620 1.00 37.12  ? 3875 MET A CA    1 
ATOM   18538 C  C     . MET A 1 3875 ? 152.050 191.336 151.159 1.00 38.76  ? 3875 MET A C     1 
ATOM   18539 O  O     . MET A 1 3875 ? 152.256 192.443 150.654 1.00 37.84  ? 3875 MET A O     1 
ATOM   18540 C  CB    . MET A 1 3875 ? 151.056 191.022 153.412 1.00 35.13  ? 3875 MET A CB    1 
ATOM   18541 C  CG    . MET A 1 3875 ? 151.170 190.560 154.848 1.00 37.03  ? 3875 MET A CG    1 
ATOM   18542 S  SD    . MET A 1 3875 ? 149.552 190.473 155.633 1.00 38.94  ? 3875 MET A SD    1 
ATOM   18543 C  CE    . MET A 1 3875 ? 149.190 192.201 155.862 1.00 34.24  ? 3875 MET A CE    1 
ATOM   18544 N  N     . LEU A 1 3876 ? 151.539 190.310 150.487 1.00 39.82  ? 3876 LEU A N     1 
ATOM   18545 C  CA    . LEU A 1 3876 ? 151.043 190.475 149.131 1.00 42.12  ? 3876 LEU A CA    1 
ATOM   18546 C  C     . LEU A 1 3876 ? 149.811 191.371 149.136 1.00 44.95  ? 3876 LEU A C     1 
ATOM   18547 O  O     . LEU A 1 3876 ? 149.064 191.427 150.115 1.00 49.50  ? 3876 LEU A O     1 
ATOM   18548 C  CB    . LEU A 1 3876 ? 150.702 189.116 148.521 1.00 45.96  ? 3876 LEU A CB    1 
ATOM   18549 C  CG    . LEU A 1 3876 ? 151.827 188.082 148.474 1.00 40.99  ? 3876 LEU A CG    1 
ATOM   18550 C  CD1   . LEU A 1 3876 ? 151.272 186.717 148.121 1.00 46.95  ? 3876 LEU A CD1   1 
ATOM   18551 C  CD2   . LEU A 1 3876 ? 152.893 188.492 147.482 1.00 38.94  ? 3876 LEU A CD2   1 
ATOM   18552 N  N     . HIS A 1 3877 ? 149.604 192.083 148.025 1.00 44.00  ? 3877 HIS A N     1 
ATOM   18553 C  CA    . HIS A 1 3877 ? 148.498 193.031 147.949 1.00 43.55  ? 3877 HIS A CA    1 
ATOM   18554 C  C     . HIS A 1 3877 ? 147.147 192.365 148.157 1.00 43.89  ? 3877 HIS A C     1 
ATOM   18555 O  O     . HIS A 1 3877 ? 146.206 193.024 148.612 1.00 44.82  ? 3877 HIS A O     1 
ATOM   18556 C  CB    . HIS A 1 3877 ? 148.510 193.756 146.605 1.00 44.64  ? 3877 HIS A CB    1 
ATOM   18557 C  CG    . HIS A 1 3877 ? 147.511 194.866 146.512 1.00 49.53  ? 3877 HIS A CG    1 
ATOM   18558 N  ND1   . HIS A 1 3877 ? 147.577 195.994 147.300 1.00 50.36  ? 3877 HIS A ND1   1 
ATOM   18559 C  CD2   . HIS A 1 3877 ? 146.415 195.015 145.732 1.00 52.85  ? 3877 HIS A CD2   1 
ATOM   18560 C  CE1   . HIS A 1 3877 ? 146.568 196.794 147.005 1.00 55.97  ? 3877 HIS A CE1   1 
ATOM   18561 N  NE2   . HIS A 1 3877 ? 145.848 196.224 146.057 1.00 56.70  ? 3877 HIS A NE2   1 
ATOM   18562 N  N     . GLN A 1 3878 ? 147.026 191.079 147.833 1.00 46.40  ? 3878 GLN A N     1 
ATOM   18563 C  CA    . GLN A 1 3878 ? 145.781 190.360 148.056 1.00 47.14  ? 3878 GLN A CA    1 
ATOM   18564 C  C     . GLN A 1 3878 ? 145.507 190.097 149.530 1.00 45.64  ? 3878 GLN A C     1 
ATOM   18565 O  O     . GLN A 1 3878 ? 144.346 189.899 149.903 1.00 49.60  ? 3878 GLN A O     1 
ATOM   18566 C  CB    . GLN A 1 3878 ? 145.800 189.038 147.287 1.00 47.80  ? 3878 GLN A CB    1 
ATOM   18567 C  CG    . GLN A 1 3878 ? 146.858 188.067 147.771 1.00 53.04  ? 3878 GLN A CG    1 
ATOM   18568 C  CD    . GLN A 1 3878 ? 146.899 186.792 146.960 1.00 67.50  ? 3878 GLN A CD    1 
ATOM   18569 O  OE1   . GLN A 1 3878 ? 146.095 186.596 146.049 1.00 78.69  ? 3878 GLN A OE1   1 
ATOM   18570 N  NE2   . GLN A 1 3878 ? 147.839 185.915 147.286 1.00 67.14  ? 3878 GLN A NE2   1 
ATOM   18571 N  N     . ASP A 1 3879 ? 146.540 190.090 150.372 1.00 42.58  ? 3879 ASP A N     1 
ATOM   18572 C  CA    . ASP A 1 3879 ? 146.386 189.802 151.791 1.00 38.24  ? 3879 ASP A CA    1 
ATOM   18573 C  C     . ASP A 1 3879 ? 146.258 191.047 152.657 1.00 40.95  ? 3879 ASP A C     1 
ATOM   18574 O  O     . ASP A 1 3879 ? 146.087 190.915 153.873 1.00 47.93  ? 3879 ASP A O     1 
ATOM   18575 C  CB    . ASP A 1 3879 ? 147.564 188.957 152.287 1.00 37.82  ? 3879 ASP A CB    1 
ATOM   18576 C  CG    . ASP A 1 3879 ? 147.633 187.605 151.609 1.00 46.75  ? 3879 ASP A CG    1 
ATOM   18577 O  OD1   . ASP A 1 3879 ? 146.735 187.305 150.799 1.00 56.48  ? 3879 ASP A OD1   1 
ATOM   18578 O  OD2   . ASP A 1 3879 ? 148.586 186.846 151.872 1.00 46.14  ? 3879 ASP A OD2   1 
ATOM   18579 N  N     . HIS A 1 3880 ? 146.343 192.245 152.075 1.00 36.78  ? 3880 HIS A N     1 
ATOM   18580 C  CA    . HIS A 1 3880 ? 146.132 193.458 152.860 1.00 33.42  ? 3880 HIS A CA    1 
ATOM   18581 C  C     . HIS A 1 3880 ? 144.714 193.517 153.409 1.00 36.55  ? 3880 HIS A C     1 
ATOM   18582 O  O     . HIS A 1 3880 ? 144.501 193.909 154.563 1.00 37.34  ? 3880 HIS A O     1 
ATOM   18583 C  CB    . HIS A 1 3880 ? 146.418 194.698 152.015 1.00 29.80  ? 3880 HIS A CB    1 
ATOM   18584 C  CG    . HIS A 1 3880 ? 147.847 194.833 151.597 1.00 30.82  ? 3880 HIS A CG    1 
ATOM   18585 N  ND1   . HIS A 1 3880 ? 148.309 195.913 150.878 1.00 34.78  ? 3880 HIS A ND1   1 
ATOM   18586 C  CD2   . HIS A 1 3880 ? 148.916 194.030 151.800 1.00 33.67  ? 3880 HIS A CD2   1 
ATOM   18587 C  CE1   . HIS A 1 3880 ? 149.602 195.767 150.653 1.00 36.45  ? 3880 HIS A CE1   1 
ATOM   18588 N  NE2   . HIS A 1 3880 ? 149.995 194.633 151.202 1.00 34.75  ? 3880 HIS A NE2   1 
ATOM   18589 N  N     . ILE A 1 3881 ? 143.731 193.138 152.592 1.00 38.50  ? 3881 ILE A N     1 
ATOM   18590 C  CA    . ILE A 1 3881 ? 142.338 193.252 153.005 1.00 36.76  ? 3881 ILE A CA    1 
ATOM   18591 C  C     . ILE A 1 3881 ? 142.038 192.299 154.155 1.00 37.57  ? 3881 ILE A C     1 
ATOM   18592 O  O     . ILE A 1 3881 ? 141.265 192.630 155.058 1.00 43.77  ? 3881 ILE A O     1 
ATOM   18593 C  CB    . ILE A 1 3881 ? 141.403 193.020 151.802 1.00 41.38  ? 3881 ILE A CB    1 
ATOM   18594 C  CG1   . ILE A 1 3881 ? 139.937 193.111 152.231 1.00 35.91  ? 3881 ILE A CG1   1 
ATOM   18595 C  CG2   . ILE A 1 3881 ? 141.701 191.689 151.129 1.00 41.72  ? 3881 ILE A CG2   1 
ATOM   18596 C  CD1   . ILE A 1 3881 ? 139.581 194.415 152.904 1.00 36.23  ? 3881 ILE A CD1   1 
ATOM   18597 N  N     . THR A 1 3882 ? 142.649 191.113 154.155 1.00 34.97  ? 3882 THR A N     1 
ATOM   18598 C  CA    . THR A 1 3882 ? 142.420 190.165 155.242 1.00 34.44  ? 3882 THR A CA    1 
ATOM   18599 C  C     . THR A 1 3882 ? 142.922 190.719 156.571 1.00 39.25  ? 3882 THR A C     1 
ATOM   18600 O  O     . THR A 1 3882 ? 142.217 190.674 157.587 1.00 48.33  ? 3882 THR A O     1 
ATOM   18601 C  CB    . THR A 1 3882 ? 143.099 188.832 154.927 1.00 33.85  ? 3882 THR A CB    1 
ATOM   18602 O  OG1   . THR A 1 3882 ? 142.631 188.342 153.665 1.00 43.55  ? 3882 THR A OG1   1 
ATOM   18603 C  CG2   . THR A 1 3882 ? 142.788 187.810 156.003 1.00 35.17  ? 3882 THR A CG2   1 
ATOM   18604 N  N     . PHE A 1 3883 ? 144.143 191.256 156.579 1.00 35.34  ? 3883 PHE A N     1 
ATOM   18605 C  CA    . PHE A 1 3883 ? 144.696 191.818 157.805 1.00 33.11  ? 3883 PHE A CA    1 
ATOM   18606 C  C     . PHE A 1 3883 ? 143.916 193.046 158.254 1.00 32.15  ? 3883 PHE A C     1 
ATOM   18607 O  O     . PHE A 1 3883 ? 143.694 193.241 159.454 1.00 37.07  ? 3883 PHE A O     1 
ATOM   18608 C  CB    . PHE A 1 3883 ? 146.170 192.159 157.607 1.00 29.62  ? 3883 PHE A CB    1 
ATOM   18609 C  CG    . PHE A 1 3883 ? 146.898 192.468 158.881 1.00 26.57  ? 3883 PHE A CG    1 
ATOM   18610 C  CD1   . PHE A 1 3883 ? 146.813 191.615 159.967 1.00 27.12  ? 3883 PHE A CD1   1 
ATOM   18611 C  CD2   . PHE A 1 3883 ? 147.675 193.605 158.991 1.00 26.86  ? 3883 PHE A CD2   1 
ATOM   18612 C  CE1   . PHE A 1 3883 ? 147.483 191.896 161.137 1.00 28.55  ? 3883 PHE A CE1   1 
ATOM   18613 C  CE2   . PHE A 1 3883 ? 148.346 193.888 160.158 1.00 27.54  ? 3883 PHE A CE2   1 
ATOM   18614 C  CZ    . PHE A 1 3883 ? 148.251 193.033 161.232 1.00 27.57  ? 3883 PHE A CZ    1 
ATOM   18615 N  N     . ALA A 1 3884 ? 143.499 193.893 157.310 1.00 28.06  ? 3884 ALA A N     1 
ATOM   18616 C  CA    . ALA A 1 3884 ? 142.697 195.054 157.679 1.00 25.97  ? 3884 ALA A CA    1 
ATOM   18617 C  C     . ALA A 1 3884 ? 141.350 194.631 158.247 1.00 31.74  ? 3884 ALA A C     1 
ATOM   18618 O  O     . ALA A 1 3884 ? 140.840 195.256 159.182 1.00 37.35  ? 3884 ALA A O     1 
ATOM   18619 C  CB    . ALA A 1 3884 ? 142.508 195.969 156.471 1.00 32.87  ? 3884 ALA A CB    1 
ATOM   18620 N  N     . MET A 1 3885 ? 140.763 193.564 157.700 1.00 36.14  ? 3885 MET A N     1 
ATOM   18621 C  CA    . MET A 1 3885 ? 139.511 193.036 158.228 1.00 35.29  ? 3885 MET A CA    1 
ATOM   18622 C  C     . MET A 1 3885 ? 139.693 192.532 159.652 1.00 38.13  ? 3885 MET A C     1 
ATOM   18623 O  O     . MET A 1 3885 ? 138.855 192.786 160.525 1.00 43.83  ? 3885 MET A O     1 
ATOM   18624 C  CB    . MET A 1 3885 ? 139.015 191.908 157.323 1.00 33.33  ? 3885 MET A CB    1 
ATOM   18625 C  CG    . MET A 1 3885 ? 138.102 192.350 156.193 1.00 40.21  ? 3885 MET A CG    1 
ATOM   18626 S  SD    . MET A 1 3885 ? 136.492 192.930 156.738 1.00 57.56  ? 3885 MET A SD    1 
ATOM   18627 C  CE    . MET A 1 3885 ? 135.556 191.407 156.702 1.00 51.73  ? 3885 MET A CE    1 
ATOM   18628 N  N     . LEU A 1 3886 ? 140.791 191.816 159.902 1.00 36.96  ? 3886 LEU A N     1 
ATOM   18629 C  CA    . LEU A 1 3886 ? 141.071 191.326 161.249 1.00 33.40  ? 3886 LEU A CA    1 
ATOM   18630 C  C     . LEU A 1 3886 ? 141.289 192.477 162.226 1.00 33.22  ? 3886 LEU A C     1 
ATOM   18631 O  O     . LEU A 1 3886 ? 140.800 192.440 163.361 1.00 38.36  ? 3886 LEU A O     1 
ATOM   18632 C  CB    . LEU A 1 3886 ? 142.285 190.402 161.219 1.00 33.62  ? 3886 LEU A CB    1 
ATOM   18633 C  CG    . LEU A 1 3886 ? 142.097 189.132 160.390 1.00 40.42  ? 3886 LEU A CG    1 
ATOM   18634 C  CD1   . LEU A 1 3886 ? 143.366 188.311 160.377 1.00 44.41  ? 3886 LEU A CD1   1 
ATOM   18635 C  CD2   . LEU A 1 3886 ? 140.936 188.314 160.923 1.00 46.41  ? 3886 LEU A CD2   1 
ATOM   18636 N  N     . LEU A 1 3887 ? 142.022 193.509 161.804 1.00 30.57  ? 3887 LEU A N     1 
ATOM   18637 C  CA    . LEU A 1 3887 ? 142.237 194.672 162.660 1.00 28.71  ? 3887 LEU A CA    1 
ATOM   18638 C  C     . LEU A 1 3887 ? 140.928 195.397 162.950 1.00 36.52  ? 3887 LEU A C     1 
ATOM   18639 O  O     . LEU A 1 3887 ? 140.699 195.855 164.077 1.00 45.51  ? 3887 LEU A O     1 
ATOM   18640 C  CB    . LEU A 1 3887 ? 143.240 195.624 162.010 1.00 27.81  ? 3887 LEU A CB    1 
ATOM   18641 C  CG    . LEU A 1 3887 ? 144.696 195.169 161.937 1.00 25.57  ? 3887 LEU A CG    1 
ATOM   18642 C  CD1   . LEU A 1 3887 ? 145.591 196.336 161.583 1.00 26.95  ? 3887 LEU A CD1   1 
ATOM   18643 C  CD2   . LEU A 1 3887 ? 145.132 194.543 163.246 1.00 31.58  ? 3887 LEU A CD2   1 
ATOM   18644 N  N     . ALA A 1 3888 ? 140.064 195.526 161.942 1.00 34.82  ? 3888 ALA A N     1 
ATOM   18645 C  CA    . ALA A 1 3888 ? 138.764 196.148 162.154 1.00 35.58  ? 3888 ALA A CA    1 
ATOM   18646 C  C     . ALA A 1 3888 ? 137.926 195.338 163.130 1.00 38.93  ? 3888 ALA A C     1 
ATOM   18647 O  O     . ALA A 1 3888 ? 137.225 195.903 163.975 1.00 47.96  ? 3888 ALA A O     1 
ATOM   18648 C  CB    . ALA A 1 3888 ? 138.034 196.307 160.822 1.00 35.74  ? 3888 ALA A CB    1 
ATOM   18649 N  N     . ARG A 1 3889 ? 137.984 194.009 163.029 1.00 34.87  ? 3889 ARG A N     1 
ATOM   18650 C  CA    . ARG A 1 3889 ? 137.261 193.168 163.975 1.00 37.70  ? 3889 ARG A CA    1 
ATOM   18651 C  C     . ARG A 1 3889 ? 137.813 193.324 165.388 1.00 39.34  ? 3889 ARG A C     1 
ATOM   18652 O  O     . ARG A 1 3889 ? 137.051 193.326 166.361 1.00 44.85  ? 3889 ARG A O     1 
ATOM   18653 C  CB    . ARG A 1 3889 ? 137.317 191.710 163.526 1.00 41.44  ? 3889 ARG A CB    1 
ATOM   18654 C  CG    . ARG A 1 3889 ? 136.131 190.882 163.977 1.00 48.12  ? 3889 ARG A CG    1 
ATOM   18655 C  CD    . ARG A 1 3889 ? 136.162 189.498 163.362 1.00 55.73  ? 3889 ARG A CD    1 
ATOM   18656 N  NE    . ARG A 1 3889 ? 135.162 188.621 163.958 1.00 62.60  ? 3889 ARG A NE    1 
ATOM   18657 C  CZ    . ARG A 1 3889 ? 135.004 187.344 163.640 1.00 69.27  ? 3889 ARG A CZ    1 
ATOM   18658 N  NH1   . ARG A 1 3889 ? 135.766 186.759 162.732 1.00 72.99  ? 3889 ARG A NH1   1 
ATOM   18659 N  NH2   . ARG A 1 3889 ? 134.058 186.635 164.250 1.00 68.22  ? 3889 ARG A NH2   1 
ATOM   18660 N  N     . ILE A 1 3890 ? 139.134 193.462 165.521 1.00 36.73  ? 3890 ILE A N     1 
ATOM   18661 C  CA    . ILE A 1 3890 ? 139.735 193.684 166.837 1.00 35.37  ? 3890 ILE A CA    1 
ATOM   18662 C  C     . ILE A 1 3890 ? 139.251 195.003 167.429 1.00 43.36  ? 3890 ILE A C     1 
ATOM   18663 O  O     . ILE A 1 3890 ? 138.877 195.077 168.607 1.00 52.73  ? 3890 ILE A O     1 
ATOM   18664 C  CB    . ILE A 1 3890 ? 141.270 193.641 166.745 1.00 30.51  ? 3890 ILE A CB    1 
ATOM   18665 C  CG1   . ILE A 1 3890 ? 141.752 192.232 166.403 1.00 36.32  ? 3890 ILE A CG1   1 
ATOM   18666 C  CG2   . ILE A 1 3890 ? 141.896 194.107 168.043 1.00 30.62  ? 3890 ILE A CG2   1 
ATOM   18667 C  CD1   . ILE A 1 3890 ? 143.234 192.149 166.148 1.00 29.07  ? 3890 ILE A CD1   1 
ATOM   18668 N  N     . LYS A 1 3891 ? 139.251 196.066 166.622 1.00 42.02  ? 3891 LYS A N     1 
ATOM   18669 C  CA    . LYS A 1 3891 ? 138.770 197.355 167.115 1.00 45.22  ? 3891 LYS A CA    1 
ATOM   18670 C  C     . LYS A 1 3891 ? 137.290 197.294 167.474 1.00 54.28  ? 3891 LYS A C     1 
ATOM   18671 O  O     . LYS A 1 3891 ? 136.862 197.894 168.467 1.00 65.15  ? 3891 LYS A O     1 
ATOM   18672 C  CB    . LYS A 1 3891 ? 139.022 198.457 166.088 1.00 40.31  ? 3891 LYS A CB    1 
ATOM   18673 C  CG    . LYS A 1 3891 ? 138.524 199.820 166.550 1.00 40.56  ? 3891 LYS A CG    1 
ATOM   18674 C  CD    . LYS A 1 3891 ? 138.926 200.936 165.606 1.00 42.22  ? 3891 LYS A CD    1 
ATOM   18675 C  CE    . LYS A 1 3891 ? 140.350 201.394 165.864 1.00 43.29  ? 3891 LYS A CE    1 
ATOM   18676 N  NZ    . LYS A 1 3891 ? 140.482 202.090 167.173 1.00 40.45  ? 3891 LYS A NZ    1 
ATOM   18677 N  N     . LEU A 1 3892 ? 136.494 196.579 166.678 1.00 50.97  ? 3892 LEU A N     1 
ATOM   18678 C  CA    . LEU A 1 3892 ? 135.076 196.426 166.985 1.00 52.64  ? 3892 LEU A CA    1 
ATOM   18679 C  C     . LEU A 1 3892 ? 134.874 195.667 168.289 1.00 53.46  ? 3892 LEU A C     1 
ATOM   18680 O  O     . LEU A 1 3892 ? 133.949 195.967 169.052 1.00 64.40  ? 3892 LEU A O     1 
ATOM   18681 C  CB    . LEU A 1 3892 ? 134.369 195.718 165.830 1.00 53.18  ? 3892 LEU A CB    1 
ATOM   18682 C  CG    . LEU A 1 3892 ? 132.854 195.571 165.936 1.00 58.26  ? 3892 LEU A CG    1 
ATOM   18683 C  CD1   . LEU A 1 3892 ? 132.190 196.933 166.020 1.00 64.95  ? 3892 LEU A CD1   1 
ATOM   18684 C  CD2   . LEU A 1 3892 ? 132.327 194.793 164.749 1.00 58.21  ? 3892 LEU A CD2   1 
ATOM   18685 N  N     . LYS A 1 3893 ? 135.717 194.668 168.553 1.00 48.52  ? 3893 LYS A N     1 
ATOM   18686 C  CA    . LYS A 1 3893 ? 135.675 193.992 169.845 1.00 52.01  ? 3893 LYS A CA    1 
ATOM   18687 C  C     . LYS A 1 3893 ? 136.024 194.950 170.974 1.00 61.66  ? 3893 LYS A C     1 
ATOM   18688 O  O     . LYS A 1 3893 ? 135.395 194.927 172.038 1.00 70.22  ? 3893 LYS A O     1 
ATOM   18689 C  CB    . LYS A 1 3893 ? 136.628 192.798 169.846 1.00 47.93  ? 3893 LYS A CB    1 
ATOM   18690 C  CG    . LYS A 1 3893 ? 136.025 191.511 169.309 1.00 53.50  ? 3893 LYS A CG    1 
ATOM   18691 C  CD    . LYS A 1 3893 ? 137.099 190.546 168.818 1.00 57.39  ? 3893 LYS A CD    1 
ATOM   18692 C  CE    . LYS A 1 3893 ? 138.394 190.687 169.606 1.00 59.87  ? 3893 LYS A CE    1 
ATOM   18693 N  NZ    . LYS A 1 3893 ? 139.402 189.661 169.220 1.00 55.38  ? 3893 LYS A NZ    1 
ATOM   18694 N  N     . GLY A 1 3894 ? 137.026 195.807 170.760 1.00 62.27  ? 3894 GLY A N     1 
ATOM   18695 C  CA    . GLY A 1 3894 ? 137.488 196.685 171.820 1.00 68.96  ? 3894 GLY A CA    1 
ATOM   18696 C  C     . GLY A 1 3894 ? 136.687 197.956 172.005 1.00 69.37  ? 3894 GLY A C     1 
ATOM   18697 O  O     . GLY A 1 3894 ? 136.845 198.624 173.031 1.00 74.78  ? 3894 GLY A O     1 
ATOM   18698 N  N     . THR A 1 3895 ? 135.836 198.309 171.047 1.00 67.66  ? 3895 THR A N     1 
ATOM   18699 C  CA    . THR A 1 3895 ? 135.114 199.569 171.136 1.00 75.00  ? 3895 THR A CA    1 
ATOM   18700 C  C     . THR A 1 3895 ? 133.954 199.461 172.124 1.00 84.98  ? 3895 THR A C     1 
ATOM   18701 O  O     . THR A 1 3895 ? 133.522 198.371 172.505 1.00 83.30  ? 3895 THR A O     1 
ATOM   18702 C  CB    . THR A 1 3895 ? 134.594 200.000 169.764 1.00 74.42  ? 3895 THR A CB    1 
ATOM   18703 O  OG1   . THR A 1 3895 ? 134.098 201.342 169.841 1.00 77.29  ? 3895 THR A OG1   1 
ATOM   18704 C  CG2   . THR A 1 3895 ? 133.471 199.089 169.314 1.00 74.43  ? 3895 THR A CG2   1 
ATOM   18705 N  N     . VAL A 1 3896 ? 133.451 200.622 172.537 1.00 92.48  ? 3896 VAL A N     1 
ATOM   18706 C  CA    . VAL A 1 3896 ? 132.374 200.727 173.515 1.00 95.04  ? 3896 VAL A CA    1 
ATOM   18707 C  C     . VAL A 1 3896 ? 131.145 201.296 172.821 1.00 95.56  ? 3896 VAL A C     1 
ATOM   18708 O  O     . VAL A 1 3896 ? 131.233 202.311 172.120 1.00 91.68  ? 3896 VAL A O     1 
ATOM   18709 C  CB    . VAL A 1 3896 ? 132.783 201.602 174.712 1.00 97.19  ? 3896 VAL A CB    1 
ATOM   18710 C  CG1   . VAL A 1 3896 ? 131.638 201.713 175.706 1.00 94.03  ? 3896 VAL A CG1   1 
ATOM   18711 C  CG2   . VAL A 1 3896 ? 134.022 201.034 175.384 1.00 96.16  ? 3896 VAL A CG2   1 
ATOM   18712 N  N     . GLY A 1 3897 ? 130.003 200.646 173.020 1.00 98.27  ? 3897 GLY A N     1 
ATOM   18713 C  CA    . GLY A 1 3897 ? 128.758 201.083 172.428 1.00 97.12  ? 3897 GLY A CA    1 
ATOM   18714 C  C     . GLY A 1 3897 ? 128.315 200.323 171.200 1.00 99.25  ? 3897 GLY A C     1 
ATOM   18715 O  O     . GLY A 1 3897 ? 127.331 200.726 170.568 1.00 102.10 ? 3897 GLY A O     1 
ATOM   18716 N  N     . GLU A 1 3898 ? 129.002 199.240 170.841 1.00 94.82  ? 3898 GLU A N     1 
ATOM   18717 C  CA    . GLU A 1 3898 ? 128.643 198.454 169.677 1.00 93.05  ? 3898 GLU A CA    1 
ATOM   18718 C  C     . GLU A 1 3898 ? 128.383 197.007 170.075 1.00 88.86  ? 3898 GLU A C     1 
ATOM   18719 O  O     . GLU A 1 3898 ? 129.078 196.470 170.944 1.00 93.50  ? 3898 GLU A O     1 
ATOM   18720 C  CB    . GLU A 1 3898 ? 129.754 198.500 168.617 1.00 93.59  ? 3898 GLU A CB    1 
ATOM   18721 C  CG    . GLU A 1 3898 ? 130.128 199.903 168.156 1.00 94.76  ? 3898 GLU A CG    1 
ATOM   18722 C  CD    . GLU A 1 3898 ? 129.090 200.522 167.240 1.00 98.46  ? 3898 GLU A CD    1 
ATOM   18723 O  OE1   . GLU A 1 3898 ? 128.117 199.827 166.880 1.00 99.14  ? 3898 GLU A OE1   1 
ATOM   18724 O  OE2   . GLU A 1 3898 ? 129.249 201.706 166.877 1.00 94.95  ? 3898 GLU A OE2   1 
ATOM   18725 N  N     . PRO A 1 3899 ? 127.395 196.356 169.468 1.00 84.33  ? 3899 PRO A N     1 
ATOM   18726 C  CA    . PRO A 1 3899 ? 127.118 194.954 169.799 1.00 82.17  ? 3899 PRO A CA    1 
ATOM   18727 C  C     . PRO A 1 3899 ? 128.264 194.050 169.371 1.00 83.77  ? 3899 PRO A C     1 
ATOM   18728 O  O     . PRO A 1 3899 ? 129.143 194.423 168.593 1.00 83.09  ? 3899 PRO A O     1 
ATOM   18729 C  CB    . PRO A 1 3899 ? 125.839 194.645 169.016 1.00 81.14  ? 3899 PRO A CB    1 
ATOM   18730 C  CG    . PRO A 1 3899 ? 125.215 195.982 168.765 1.00 84.29  ? 3899 PRO A CG    1 
ATOM   18731 C  CD    . PRO A 1 3899 ? 126.365 196.927 168.586 1.00 85.34  ? 3899 PRO A CD    1 
ATOM   18732 N  N     . THR A 1 3900 ? 128.245 192.832 169.916 1.00 85.74  ? 3900 THR A N     1 
ATOM   18733 C  CA    . THR A 1 3900 ? 129.300 191.870 169.614 1.00 86.10  ? 3900 THR A CA    1 
ATOM   18734 C  C     . THR A 1 3900 ? 129.276 191.459 168.148 1.00 86.08  ? 3900 THR A C     1 
ATOM   18735 O  O     . THR A 1 3900 ? 130.333 191.234 167.546 1.00 85.88  ? 3900 THR A O     1 
ATOM   18736 C  CB    . THR A 1 3900 ? 129.164 190.644 170.515 1.00 85.08  ? 3900 THR A CB    1 
ATOM   18737 O  OG1   . THR A 1 3900 ? 127.903 190.009 170.273 1.00 85.93  ? 3900 THR A OG1   1 
ATOM   18738 C  CG2   . THR A 1 3900 ? 129.250 191.047 171.977 1.00 89.42  ? 3900 THR A CG2   1 
ATOM   18739 N  N     . TYR A 1 3901 ? 128.082 191.350 167.561 1.00 85.15  ? 3901 TYR A N     1 
ATOM   18740 C  CA    . TYR A 1 3901 ? 127.905 190.899 166.179 1.00 77.08  ? 3901 TYR A CA    1 
ATOM   18741 C  C     . TYR A 1 3901 ? 128.531 189.527 165.954 1.00 76.51  ? 3901 TYR A C     1 
ATOM   18742 O  O     . TYR A 1 3901 ? 128.985 189.213 164.852 1.00 76.63  ? 3901 TYR A O     1 
ATOM   18743 C  CB    . TYR A 1 3901 ? 128.470 191.910 165.176 1.00 69.97  ? 3901 TYR A CB    1 
ATOM   18744 C  CG    . TYR A 1 3901 ? 127.785 193.255 165.206 1.00 75.19  ? 3901 TYR A CG    1 
ATOM   18745 C  CD1   . TYR A 1 3901 ? 126.442 193.379 164.886 1.00 77.65  ? 3901 TYR A CD1   1 
ATOM   18746 C  CD2   . TYR A 1 3901 ? 128.486 194.402 165.546 1.00 75.85  ? 3901 TYR A CD2   1 
ATOM   18747 C  CE1   . TYR A 1 3901 ? 125.815 194.608 164.912 1.00 78.57  ? 3901 TYR A CE1   1 
ATOM   18748 C  CE2   . TYR A 1 3901 ? 127.868 195.634 165.574 1.00 76.09  ? 3901 TYR A CE2   1 
ATOM   18749 C  CZ    . TYR A 1 3901 ? 126.533 195.732 165.256 1.00 79.94  ? 3901 TYR A CZ    1 
ATOM   18750 O  OH    . TYR A 1 3901 ? 125.915 196.959 165.284 1.00 81.26  ? 3901 TYR A OH    1 
ATOM   18751 N  N     . ASP A 1 3902 ? 128.565 188.703 167.003 1.00 78.75  ? 3902 ASP A N     1 
ATOM   18752 C  CA    . ASP A 1 3902 ? 129.160 187.377 166.880 1.00 75.56  ? 3902 ASP A CA    1 
ATOM   18753 C  C     . ASP A 1 3902 ? 128.372 186.503 165.915 1.00 75.87  ? 3902 ASP A C     1 
ATOM   18754 O  O     . ASP A 1 3902 ? 128.959 185.746 165.138 1.00 77.47  ? 3902 ASP A O     1 
ATOM   18755 C  CB    . ASP A 1 3902 ? 129.261 186.713 168.253 1.00 82.78  ? 3902 ASP A CB    1 
ATOM   18756 C  CG    . ASP A 1 3902 ? 130.400 187.268 169.085 1.00 95.88  ? 3902 ASP A CG    1 
ATOM   18757 O  OD1   . ASP A 1 3902 ? 130.804 188.425 168.844 1.00 95.67  ? 3902 ASP A OD1   1 
ATOM   18758 O  OD2   . ASP A 1 3902 ? 130.896 186.545 169.975 1.00 103.34 ? 3902 ASP A OD2   1 
ATOM   18759 N  N     . ALA A 1 3903 ? 127.040 186.585 165.956 1.00 80.53  ? 3903 ALA A N     1 
ATOM   18760 C  CA    . ALA A 1 3903 ? 126.227 185.790 165.040 1.00 79.31  ? 3903 ALA A CA    1 
ATOM   18761 C  C     . ALA A 1 3903 ? 126.420 186.234 163.596 1.00 75.87  ? 3903 ALA A C     1 
ATOM   18762 O  O     . ALA A 1 3903 ? 126.559 185.398 162.695 1.00 75.76  ? 3903 ALA A O     1 
ATOM   18763 C  CB    . ALA A 1 3903 ? 124.753 185.878 165.434 1.00 81.65  ? 3903 ALA A CB    1 
ATOM   18764 N  N     . GLU A 1 3904 ? 126.434 187.546 163.356 1.00 75.47  ? 3904 GLU A N     1 
ATOM   18765 C  CA    . GLU A 1 3904 ? 126.563 188.045 161.991 1.00 68.01  ? 3904 GLU A CA    1 
ATOM   18766 C  C     . GLU A 1 3904 ? 127.924 187.698 161.397 1.00 65.06  ? 3904 GLU A C     1 
ATOM   18767 O  O     . GLU A 1 3904 ? 128.009 187.238 160.254 1.00 67.42  ? 3904 GLU A O     1 
ATOM   18768 C  CB    . GLU A 1 3904 ? 126.322 189.554 161.963 1.00 64.69  ? 3904 GLU A CB    1 
ATOM   18769 C  CG    . GLU A 1 3904 ? 124.872 189.962 162.195 1.00 70.77  ? 3904 GLU A CG    1 
ATOM   18770 C  CD    . GLU A 1 3904 ? 124.475 189.937 163.666 1.00 86.36  ? 3904 GLU A CD    1 
ATOM   18771 O  OE1   . GLU A 1 3904 ? 125.315 189.568 164.513 1.00 83.89  ? 3904 GLU A OE1   1 
ATOM   18772 O  OE2   . GLU A 1 3904 ? 123.319 190.291 163.978 1.00 89.94  ? 3904 GLU A OE2   1 
ATOM   18773 N  N     . PHE A 1 3905 ? 129.002 187.893 162.163 1.00 64.14  ? 3905 PHE A N     1 
ATOM   18774 C  CA    . PHE A 1 3905 ? 130.330 187.520 161.679 1.00 60.78  ? 3905 PHE A CA    1 
ATOM   18775 C  C     . PHE A 1 3905 ? 130.462 186.010 161.544 1.00 64.02  ? 3905 PHE A C     1 
ATOM   18776 O  O     . PHE A 1 3905 ? 131.124 185.514 160.623 1.00 68.05  ? 3905 PHE A O     1 
ATOM   18777 C  CB    . PHE A 1 3905 ? 131.408 188.056 162.618 1.00 63.62  ? 3905 PHE A CB    1 
ATOM   18778 C  CG    . PHE A 1 3905 ? 131.805 189.472 162.343 1.00 61.56  ? 3905 PHE A CG    1 
ATOM   18779 C  CD1   . PHE A 1 3905 ? 132.310 189.831 161.107 1.00 61.59  ? 3905 PHE A CD1   1 
ATOM   18780 C  CD2   . PHE A 1 3905 ? 131.691 190.440 163.322 1.00 60.66  ? 3905 PHE A CD2   1 
ATOM   18781 C  CE1   . PHE A 1 3905 ? 132.683 191.129 160.851 1.00 61.69  ? 3905 PHE A CE1   1 
ATOM   18782 C  CE2   . PHE A 1 3905 ? 132.065 191.740 163.070 1.00 59.96  ? 3905 PHE A CE2   1 
ATOM   18783 C  CZ    . PHE A 1 3905 ? 132.560 192.085 161.834 1.00 60.60  ? 3905 PHE A CZ    1 
ATOM   18784 N  N     . GLN A 1 3906 ? 129.843 185.267 162.463 1.00 68.21  ? 3906 GLN A N     1 
ATOM   18785 C  CA    . GLN A 1 3906 ? 129.887 183.812 162.423 1.00 67.13  ? 3906 GLN A CA    1 
ATOM   18786 C  C     . GLN A 1 3906 ? 129.260 183.302 161.135 1.00 66.35  ? 3906 GLN A C     1 
ATOM   18787 O  O     . GLN A 1 3906 ? 129.807 182.415 160.465 1.00 65.51  ? 3906 GLN A O     1 
ATOM   18788 C  CB    . GLN A 1 3906 ? 129.138 183.270 163.644 1.00 75.01  ? 3906 GLN A CB    1 
ATOM   18789 C  CG    . GLN A 1 3906 ? 129.153 181.768 163.862 1.00 84.15  ? 3906 GLN A CG    1 
ATOM   18790 C  CD    . GLN A 1 3906 ? 130.539 181.263 164.211 1.00 88.96  ? 3906 GLN A CD    1 
ATOM   18791 O  OE1   . GLN A 1 3906 ? 130.963 180.212 163.736 1.00 88.43  ? 3906 GLN A OE1   1 
ATOM   18792 N  NE2   . GLN A 1 3906 ? 131.264 182.027 165.013 1.00 88.07  ? 3906 GLN A NE2   1 
ATOM   18793 N  N     . HIS A 1 3907 ? 128.116 183.884 160.767 1.00 69.01  ? 3907 HIS A N     1 
ATOM   18794 C  CA    . HIS A 1 3907 ? 127.493 183.593 159.483 1.00 67.96  ? 3907 HIS A CA    1 
ATOM   18795 C  C     . HIS A 1 3907 ? 128.382 184.024 158.325 1.00 66.29  ? 3907 HIS A C     1 
ATOM   18796 O  O     . HIS A 1 3907 ? 128.596 183.252 157.388 1.00 67.44  ? 3907 HIS A O     1 
ATOM   18797 C  CB    . HIS A 1 3907 ? 126.136 184.287 159.400 1.00 69.29  ? 3907 HIS A CB    1 
ATOM   18798 C  CG    . HIS A 1 3907 ? 125.272 183.792 158.285 1.00 73.93  ? 3907 HIS A CG    1 
ATOM   18799 N  ND1   . HIS A 1 3907 ? 125.595 183.972 156.958 1.00 74.89  ? 3907 HIS A ND1   1 
ATOM   18800 C  CD2   . HIS A 1 3907 ? 124.097 183.122 158.300 1.00 82.38  ? 3907 HIS A CD2   1 
ATOM   18801 C  CE1   . HIS A 1 3907 ? 124.655 183.434 156.202 1.00 79.28  ? 3907 HIS A CE1   1 
ATOM   18802 N  NE2   . HIS A 1 3907 ? 123.735 182.912 156.992 1.00 85.91  ? 3907 HIS A NE2   1 
ATOM   18803 N  N     . PHE A 1 3908 ? 128.925 185.241 158.384 1.00 62.48  ? 3908 PHE A N     1 
ATOM   18804 C  CA    . PHE A 1 3908 ? 129.784 185.726 157.308 1.00 56.03  ? 3908 PHE A CA    1 
ATOM   18805 C  C     . PHE A 1 3908 ? 130.934 184.764 157.043 1.00 59.14  ? 3908 PHE A C     1 
ATOM   18806 O  O     . PHE A 1 3908 ? 131.383 184.616 155.901 1.00 56.72  ? 3908 PHE A O     1 
ATOM   18807 C  CB    . PHE A 1 3908 ? 130.317 187.115 157.657 1.00 54.91  ? 3908 PHE A CB    1 
ATOM   18808 C  CG    . PHE A 1 3908 ? 131.314 187.645 156.674 1.00 56.78  ? 3908 PHE A CG    1 
ATOM   18809 C  CD1   . PHE A 1 3908 ? 130.941 187.930 155.375 1.00 57.00  ? 3908 PHE A CD1   1 
ATOM   18810 C  CD2   . PHE A 1 3908 ? 132.630 187.852 157.049 1.00 55.54  ? 3908 PHE A CD2   1 
ATOM   18811 C  CE1   . PHE A 1 3908 ? 131.859 188.415 154.470 1.00 54.25  ? 3908 PHE A CE1   1 
ATOM   18812 C  CE2   . PHE A 1 3908 ? 133.552 188.336 156.147 1.00 55.40  ? 3908 PHE A CE2   1 
ATOM   18813 C  CZ    . PHE A 1 3908 ? 133.166 188.618 154.857 1.00 51.80  ? 3908 PHE A CZ    1 
ATOM   18814 N  N     . LEU A 1 3909 ? 131.416 184.093 158.087 1.00 64.50  ? 3909 LEU A N     1 
ATOM   18815 C  CA    . LEU A 1 3909 ? 132.533 183.170 157.923 1.00 61.16  ? 3909 LEU A CA    1 
ATOM   18816 C  C     . LEU A 1 3909 ? 132.078 181.800 157.427 1.00 63.01  ? 3909 LEU A C     1 
ATOM   18817 O  O     . LEU A 1 3909 ? 132.631 181.267 156.459 1.00 59.72  ? 3909 LEU A O     1 
ATOM   18818 C  CB    . LEU A 1 3909 ? 133.300 183.047 159.241 1.00 59.24  ? 3909 LEU A CB    1 
ATOM   18819 C  CG    . LEU A 1 3909 ? 133.999 184.328 159.694 1.00 57.86  ? 3909 LEU A CG    1 
ATOM   18820 C  CD1   . LEU A 1 3909 ? 134.794 184.084 160.960 1.00 65.40  ? 3909 LEU A CD1   1 
ATOM   18821 C  CD2   . LEU A 1 3909 ? 134.896 184.857 158.591 1.00 52.20  ? 3909 LEU A CD2   1 
ATOM   18822 N  N     . ARG A 1 3910 ? 131.071 181.208 158.073 1.00 72.03  ? 3910 ARG A N     1 
ATOM   18823 C  CA    . ARG A 1 3910 ? 130.676 179.831 157.779 1.00 74.91  ? 3910 ARG A CA    1 
ATOM   18824 C  C     . ARG A 1 3910 ? 129.193 179.670 157.436 1.00 78.97  ? 3910 ARG A C     1 
ATOM   18825 O  O     . ARG A 1 3910 ? 128.528 178.745 157.906 1.00 83.33  ? 3910 ARG A O     1 
ATOM   18826 C  CB    . ARG A 1 3910 ? 131.063 178.910 158.933 1.00 71.46  ? 3910 ARG A CB    1 
ATOM   18827 C  CG    . ARG A 1 3910 ? 130.320 179.153 160.230 1.00 78.97  ? 3910 ARG A CG    1 
ATOM   18828 C  CD    . ARG A 1 3910 ? 130.784 178.173 161.281 1.00 85.09  ? 3910 ARG A CD    1 
ATOM   18829 N  NE    . ARG A 1 3910 ? 132.185 178.348 161.631 1.00 86.68  ? 3910 ARG A NE    1 
ATOM   18830 C  CZ    . ARG A 1 3910 ? 133.146 177.501 161.291 1.00 84.17  ? 3910 ARG A CZ    1 
ATOM   18831 N  NH1   . ARG A 1 3910 ? 132.890 176.414 160.581 1.00 90.32  ? 3910 ARG A NH1   1 
ATOM   18832 N  NH2   . ARG A 1 3910 ? 134.393 177.740 161.687 1.00 73.89  ? 3910 ARG A NH2   1 
ATOM   18833 N  N     . GLY A 1 3911 ? 128.662 180.541 156.577 1.00 80.41  ? 3911 GLY A N     1 
ATOM   18834 C  CA    . GLY A 1 3911 ? 127.299 180.366 156.111 1.00 81.76  ? 3911 GLY A CA    1 
ATOM   18835 C  C     . GLY A 1 3911 ? 127.118 179.215 155.149 1.00 91.54  ? 3911 GLY A C     1 
ATOM   18836 O  O     . GLY A 1 3911 ? 125.990 178.748 154.964 1.00 99.37  ? 3911 GLY A O     1 
ATOM   18837 N  N     . ASN A 1 3912 ? 128.199 178.760 154.513 1.00 90.20  ? 3912 ASN A N     1 
ATOM   18838 C  CA    . ASN A 1 3912 ? 128.127 177.545 153.714 1.00 95.25  ? 3912 ASN A CA    1 
ATOM   18839 C  C     . ASN A 1 3912 ? 127.794 176.328 154.566 1.00 95.52  ? 3912 ASN A C     1 
ATOM   18840 O  O     . ASN A 1 3912 ? 127.203 175.370 154.055 1.00 98.92  ? 3912 ASN A O     1 
ATOM   18841 C  CB    . ASN A 1 3912 ? 129.446 177.322 152.975 1.00 96.85  ? 3912 ASN A CB    1 
ATOM   18842 C  CG    . ASN A 1 3912 ? 129.748 178.421 151.978 1.00 105.97 ? 3912 ASN A CG    1 
ATOM   18843 O  OD1   . ASN A 1 3912 ? 129.034 178.591 150.991 1.00 110.78 ? 3912 ASN A OD1   1 
ATOM   18844 N  ND2   . ASN A 1 3912 ? 130.812 179.172 152.230 1.00 105.13 ? 3912 ASN A ND2   1 
ATOM   18845 N  N     . GLU A 1 3913 ? 128.163 176.346 155.849 1.00 90.98  ? 3913 GLU A N     1 
ATOM   18846 C  CA    . GLU A 1 3913 ? 127.822 175.259 156.758 1.00 93.20  ? 3913 GLU A CA    1 
ATOM   18847 C  C     . GLU A 1 3913 ? 126.319 175.123 156.960 1.00 99.45  ? 3913 GLU A C     1 
ATOM   18848 O  O     . GLU A 1 3913 ? 125.843 174.019 157.249 1.00 102.44 ? 3913 GLU A O     1 
ATOM   18849 C  CB    . GLU A 1 3913 ? 128.523 175.469 158.103 1.00 91.94  ? 3913 GLU A CB    1 
ATOM   18850 C  CG    . GLU A 1 3913 ? 128.275 174.375 159.129 1.00 99.69  ? 3913 GLU A CG    1 
ATOM   18851 C  CD    . GLU A 1 3913 ? 128.844 173.036 158.709 1.00 101.10 ? 3913 GLU A CD    1 
ATOM   18852 O  OE1   . GLU A 1 3913 ? 129.811 173.018 157.919 1.00 101.73 ? 3913 GLU A OE1   1 
ATOM   18853 O  OE2   . GLU A 1 3913 ? 128.324 171.998 159.169 1.00 99.00  ? 3913 GLU A OE2   1 
ATOM   18854 N  N     . ILE A 1 3914 ? 125.565 176.212 156.810 1.00 101.28 ? 3914 ILE A N     1 
ATOM   18855 C  CA    . ILE A 1 3914 ? 124.115 176.142 156.948 1.00 103.29 ? 3914 ILE A CA    1 
ATOM   18856 C  C     . ILE A 1 3914 ? 123.566 175.229 155.863 1.00 111.31 ? 3914 ILE A C     1 
ATOM   18857 O  O     . ILE A 1 3914 ? 123.638 175.543 154.669 1.00 110.72 ? 3914 ILE A O     1 
ATOM   18858 C  CB    . ILE A 1 3914 ? 123.497 177.540 156.876 1.00 100.51 ? 3914 ILE A CB    1 
ATOM   18859 C  CG1   . ILE A 1 3914 ? 123.916 178.371 158.090 1.00 100.96 ? 3914 ILE A CG1   1 
ATOM   18860 C  CG2   . ILE A 1 3914 ? 121.984 177.447 156.792 1.00 101.84 ? 3914 ILE A CG2   1 
ATOM   18861 C  CD1   . ILE A 1 3914 ? 123.499 177.769 159.415 1.00 103.88 ? 3914 ILE A CD1   1 
ATOM   18862 N  N     . VAL A 1 3915 ? 123.022 174.090 156.274 1.00 116.50 ? 3915 VAL A N     1 
ATOM   18863 C  CA    . VAL A 1 3915 ? 122.567 173.079 155.328 1.00 120.28 ? 3915 VAL A CA    1 
ATOM   18864 C  C     . VAL A 1 3915 ? 121.168 173.428 154.841 1.00 123.96 ? 3915 VAL A C     1 
ATOM   18865 O  O     . VAL A 1 3915 ? 120.305 173.847 155.623 1.00 122.12 ? 3915 VAL A O     1 
ATOM   18866 C  CB    . VAL A 1 3915 ? 122.606 171.679 155.962 1.00 118.54 ? 3915 VAL A CB    1 
ATOM   18867 C  CG1   . VAL A 1 3915 ? 121.750 171.628 157.220 1.00 120.79 ? 3915 VAL A CG1   1 
ATOM   18868 C  CG2   . VAL A 1 3915 ? 122.146 170.639 154.955 1.00 115.70 ? 3915 VAL A CG2   1 
ATOM   18869 N  N     . LEU A 1 3916 ? 120.951 173.281 153.537 1.00 123.70 ? 3916 LEU A N     1 
ATOM   18870 C  CA    . LEU A 1 3916 ? 119.635 173.417 152.927 1.00 126.31 ? 3916 LEU A CA    1 
ATOM   18871 C  C     . LEU A 1 3916 ? 119.379 172.176 152.088 1.00 131.11 ? 3916 LEU A C     1 
ATOM   18872 O  O     . LEU A 1 3916 ? 120.206 171.816 151.244 1.00 130.47 ? 3916 LEU A O     1 
ATOM   18873 C  CB    . LEU A 1 3916 ? 119.551 174.678 152.067 1.00 120.84 ? 3916 LEU A CB    1 
ATOM   18874 C  CG    . LEU A 1 3916 ? 119.665 176.007 152.812 1.00 113.91 ? 3916 LEU A CG    1 
ATOM   18875 C  CD1   . LEU A 1 3916 ? 119.442 177.148 151.850 1.00 109.02 ? 3916 LEU A CD1   1 
ATOM   18876 C  CD2   . LEU A 1 3916 ? 118.665 176.072 153.956 1.00 113.68 ? 3916 LEU A CD2   1 
ATOM   18877 N  N     . SER A 1 3917 ? 118.242 171.526 152.320 1.00 133.45 ? 3917 SER A N     1 
ATOM   18878 C  CA    . SER A 1 3917 ? 117.917 170.310 151.591 1.00 136.43 ? 3917 SER A CA    1 
ATOM   18879 C  C     . SER A 1 3917 ? 117.687 170.610 150.114 1.00 136.58 ? 3917 SER A C     1 
ATOM   18880 O  O     . SER A 1 3917 ? 117.264 171.706 149.737 1.00 136.51 ? 3917 SER A O     1 
ATOM   18881 C  CB    . SER A 1 3917 ? 116.677 169.646 152.190 1.00 133.87 ? 3917 SER A CB    1 
ATOM   18882 O  OG    . SER A 1 3917 ? 116.903 169.273 153.538 1.00 137.50 ? 3917 SER A OG    1 
ATOM   18883 N  N     . ALA A 1 3918 ? 117.983 169.621 149.274 1.00 135.89 ? 3918 ALA A N     1 
ATOM   18884 C  CA    . ALA A 1 3918 ? 117.751 169.757 147.841 1.00 132.78 ? 3918 ALA A CA    1 
ATOM   18885 C  C     . ALA A 1 3918 ? 116.256 169.889 147.578 1.00 133.29 ? 3918 ALA A C     1 
ATOM   18886 O  O     . ALA A 1 3918 ? 115.475 168.999 147.928 1.00 133.79 ? 3918 ALA A O     1 
ATOM   18887 C  CB    . ALA A 1 3918 ? 118.328 168.558 147.094 1.00 125.16 ? 3918 ALA A CB    1 
ATOM   18888 N  N     . GLY A 1 3919 ? 115.859 171.001 146.963 1.00 128.77 ? 3919 GLY A N     1 
ATOM   18889 C  CA    . GLY A 1 3919 ? 114.467 171.311 146.745 1.00 125.72 ? 3919 GLY A CA    1 
ATOM   18890 C  C     . GLY A 1 3919 ? 113.829 172.152 147.830 1.00 131.41 ? 3919 GLY A C     1 
ATOM   18891 O  O     . GLY A 1 3919 ? 112.759 172.727 147.600 1.00 130.97 ? 3919 GLY A O     1 
ATOM   18892 N  N     . SER A 1 3920 ? 114.453 172.239 149.007 1.00 135.14 ? 3920 SER A N     1 
ATOM   18893 C  CA    . SER A 1 3920 ? 113.926 173.096 150.063 1.00 132.50 ? 3920 SER A CA    1 
ATOM   18894 C  C     . SER A 1 3920 ? 114.055 174.568 149.692 1.00 128.75 ? 3920 SER A C     1 
ATOM   18895 O  O     . SER A 1 3920 ? 113.218 175.389 150.085 1.00 123.92 ? 3920 SER A O     1 
ATOM   18896 C  CB    . SER A 1 3920 ? 114.644 172.809 151.382 1.00 130.96 ? 3920 SER A CB    1 
ATOM   18897 O  OG    . SER A 1 3920 ? 115.966 173.318 151.365 1.00 125.59 ? 3920 SER A OG    1 
ATOM   18898 N  N     . THR A 1 3921 ? 115.093 174.917 148.946 1.00 130.30 ? 3921 THR A N     1 
ATOM   18899 C  CA    . THR A 1 3921 ? 115.295 176.300 148.529 1.00 124.54 ? 3921 THR A CA    1 
ATOM   18900 C  C     . THR A 1 3921 ? 114.263 176.685 147.477 1.00 123.81 ? 3921 THR A C     1 
ATOM   18901 O  O     . THR A 1 3921 ? 114.202 176.045 146.419 1.00 120.70 ? 3921 THR A O     1 
ATOM   18902 C  CB    . THR A 1 3921 ? 116.705 176.488 147.976 1.00 116.18 ? 3921 THR A CB    1 
ATOM   18903 O  OG1   . THR A 1 3921 ? 117.657 176.382 149.041 1.00 114.94 ? 3921 THR A OG1   1 
ATOM   18904 C  CG2   . THR A 1 3921 ? 116.840 177.849 147.312 1.00 109.56 ? 3921 THR A CG2   1 
ATOM   18905 N  N     . PRO A 1 3922 ? 113.442 177.701 147.715 1.00 121.45 ? 3922 PRO A N     1 
ATOM   18906 C  CA    . PRO A 1 3922 ? 112.481 178.138 146.701 1.00 119.00 ? 3922 PRO A CA    1 
ATOM   18907 C  C     . PRO A 1 3922 ? 113.172 178.914 145.587 1.00 115.73 ? 3922 PRO A C     1 
ATOM   18908 O  O     . PRO A 1 3922 ? 114.300 179.389 145.723 1.00 112.74 ? 3922 PRO A O     1 
ATOM   18909 C  CB    . PRO A 1 3922 ? 111.522 179.034 147.490 1.00 117.55 ? 3922 PRO A CB    1 
ATOM   18910 C  CG    . PRO A 1 3922 ? 112.364 179.579 148.591 1.00 117.95 ? 3922 PRO A CG    1 
ATOM   18911 C  CD    . PRO A 1 3922 ? 113.323 178.478 148.962 1.00 117.42 ? 3922 PRO A CD    1 
ATOM   18912 N  N     . ARG A 1 3923 ? 112.465 179.035 144.469 1.00 116.48 ? 3923 ARG A N     1 
ATOM   18913 C  CA    . ARG A 1 3923 ? 112.940 179.793 143.320 1.00 112.07 ? 3923 ARG A CA    1 
ATOM   18914 C  C     . ARG A 1 3923 ? 112.379 181.206 143.398 1.00 110.32 ? 3923 ARG A C     1 
ATOM   18915 O  O     . ARG A 1 3923 ? 111.164 181.390 143.529 1.00 108.00 ? 3923 ARG A O     1 
ATOM   18916 C  CB    . ARG A 1 3923 ? 112.534 179.117 142.011 1.00 112.62 ? 3923 ARG A CB    1 
ATOM   18917 C  CG    . ARG A 1 3923 ? 113.210 177.777 141.776 1.00 120.72 ? 3923 ARG A CG    1 
ATOM   18918 C  CD    . ARG A 1 3923 ? 112.882 177.217 140.402 1.00 129.48 ? 3923 ARG A CD    1 
ATOM   18919 N  NE    . ARG A 1 3923 ? 113.539 175.937 140.168 1.00 137.00 ? 3923 ARG A NE    1 
ATOM   18920 C  CZ    . ARG A 1 3923 ? 113.420 175.223 139.057 1.00 133.43 ? 3923 ARG A CZ    1 
ATOM   18921 N  NH1   . ARG A 1 3923 ? 112.672 175.636 138.047 1.00 133.09 ? 3923 ARG A NH1   1 
ATOM   18922 N  NH2   . ARG A 1 3923 ? 114.068 174.066 138.957 1.00 126.81 ? 3923 ARG A NH2   1 
ATOM   18923 N  N     . ILE A 1 3924 ? 113.263 182.197 143.322 1.00 110.80 ? 3924 ILE A N     1 
ATOM   18924 C  CA    . ILE A 1 3924 ? 112.896 183.605 143.416 1.00 105.80 ? 3924 ILE A CA    1 
ATOM   18925 C  C     . ILE A 1 3924 ? 113.060 184.234 142.042 1.00 100.30 ? 3924 ILE A C     1 
ATOM   18926 O  O     . ILE A 1 3924 ? 114.068 184.004 141.362 1.00 94.23  ? 3924 ILE A O     1 
ATOM   18927 C  CB    . ILE A 1 3924 ? 113.746 184.341 144.466 1.00 101.45 ? 3924 ILE A CB    1 
ATOM   18928 C  CG1   . ILE A 1 3924 ? 113.972 183.451 145.689 1.00 102.25 ? 3924 ILE A CG1   1 
ATOM   18929 C  CG2   . ILE A 1 3924 ? 113.081 185.648 144.868 1.00 98.74  ? 3924 ILE A CG2   1 
ATOM   18930 C  CD1   . ILE A 1 3924 ? 112.717 183.181 146.489 1.00 105.92 ? 3924 ILE A CD1   1 
ATOM   18931 N  N     . GLN A 1 3925 ? 112.067 185.020 141.631 1.00 102.60 ? 3925 GLN A N     1 
ATOM   18932 C  CA    . GLN A 1 3925 ? 112.108 185.652 140.320 1.00 105.49 ? 3925 GLN A CA    1 
ATOM   18933 C  C     . GLN A 1 3925 ? 113.249 186.659 140.249 1.00 98.66  ? 3925 GLN A C     1 
ATOM   18934 O  O     . GLN A 1 3925 ? 113.410 187.500 141.138 1.00 93.88  ? 3925 GLN A O     1 
ATOM   18935 C  CB    . GLN A 1 3925 ? 110.775 186.339 140.026 1.00 105.16 ? 3925 GLN A CB    1 
ATOM   18936 C  CG    . GLN A 1 3925 ? 110.715 187.020 138.671 1.00 102.40 ? 3925 GLN A CG    1 
ATOM   18937 C  CD    . GLN A 1 3925 ? 111.020 186.067 137.532 1.00 105.19 ? 3925 GLN A CD    1 
ATOM   18938 O  OE1   . GLN A 1 3925 ? 110.326 185.069 137.341 1.00 104.58 ? 3925 GLN A OE1   1 
ATOM   18939 N  NE2   . GLN A 1 3925 ? 112.064 186.371 136.770 1.00 100.71 ? 3925 GLN A NE2   1 
ATOM   18940 N  N     . GLY A 1 3926 ? 114.039 186.573 139.181 1.00 98.60  ? 3926 GLY A N     1 
ATOM   18941 C  CA    . GLY A 1 3926 ? 115.163 187.461 138.986 1.00 95.06  ? 3926 GLY A CA    1 
ATOM   18942 C  C     . GLY A 1 3926 ? 116.422 187.089 139.736 1.00 91.90  ? 3926 GLY A C     1 
ATOM   18943 O  O     . GLY A 1 3926 ? 117.396 187.852 139.690 1.00 88.67  ? 3926 GLY A O     1 
ATOM   18944 N  N     . LEU A 1 3927 ? 116.443 185.949 140.421 1.00 93.14  ? 3927 LEU A N     1 
ATOM   18945 C  CA    . LEU A 1 3927 ? 117.592 185.520 141.203 1.00 90.41  ? 3927 LEU A CA    1 
ATOM   18946 C  C     . LEU A 1 3927 ? 118.117 184.192 140.679 1.00 89.71  ? 3927 LEU A C     1 
ATOM   18947 O  O     . LEU A 1 3927 ? 117.342 183.283 140.368 1.00 96.45  ? 3927 LEU A O     1 
ATOM   18948 C  CB    . LEU A 1 3927 ? 117.235 185.388 142.687 1.00 89.43  ? 3927 LEU A CB    1 
ATOM   18949 C  CG    . LEU A 1 3927 ? 117.493 186.614 143.564 1.00 83.82  ? 3927 LEU A CG    1 
ATOM   18950 C  CD1   . LEU A 1 3927 ? 116.474 187.706 143.285 1.00 90.56  ? 3927 LEU A CD1   1 
ATOM   18951 C  CD2   . LEU A 1 3927 ? 117.477 186.228 145.030 1.00 85.82  ? 3927 LEU A CD2   1 
ATOM   18952 N  N     . THR A 1 3928 ? 119.440 184.090 140.584 1.00 86.40  ? 3928 THR A N     1 
ATOM   18953 C  CA    . THR A 1 3928 ? 120.085 182.863 140.148 1.00 90.37  ? 3928 THR A CA    1 
ATOM   18954 C  C     . THR A 1 3928 ? 119.994 181.814 141.260 1.00 90.88  ? 3928 THR A C     1 
ATOM   18955 O  O     . THR A 1 3928 ? 119.769 182.135 142.431 1.00 89.76  ? 3928 THR A O     1 
ATOM   18956 C  CB    . THR A 1 3928 ? 121.538 183.159 139.758 1.00 92.56  ? 3928 THR A CB    1 
ATOM   18957 O  OG1   . THR A 1 3928 ? 121.550 184.156 138.730 1.00 94.51  ? 3928 THR A OG1   1 
ATOM   18958 C  CG2   . THR A 1 3928 ? 122.226 181.932 139.195 1.00 94.04  ? 3928 THR A CG2   1 
ATOM   18959 N  N     . VAL A 1 3929 ? 120.150 180.542 140.880 1.00 94.01  ? 3929 VAL A N     1 
ATOM   18960 C  CA    . VAL A 1 3929 ? 119.932 179.442 141.819 1.00 98.15  ? 3929 VAL A CA    1 
ATOM   18961 C  C     . VAL A 1 3929 ? 120.890 179.538 143.003 1.00 98.70  ? 3929 VAL A C     1 
ATOM   18962 O  O     . VAL A 1 3929 ? 120.490 179.359 144.160 1.00 92.31  ? 3929 VAL A O     1 
ATOM   18963 C  CB    . VAL A 1 3929 ? 120.050 178.086 141.097 1.00 100.28 ? 3929 VAL A CB    1 
ATOM   18964 C  CG1   . VAL A 1 3929 ? 118.850 177.867 140.190 1.00 100.41 ? 3929 VAL A CG1   1 
ATOM   18965 C  CG2   . VAL A 1 3929 ? 121.336 178.011 140.290 1.00 101.08 ? 3929 VAL A CG2   1 
ATOM   18966 N  N     . GLU A 1 3930 ? 122.170 179.817 142.737 1.00 100.77 ? 3930 GLU A N     1 
ATOM   18967 C  CA    . GLU A 1 3930 ? 123.116 179.986 143.837 1.00 98.56  ? 3930 GLU A CA    1 
ATOM   18968 C  C     . GLU A 1 3930 ? 122.790 181.227 144.657 1.00 95.08  ? 3930 GLU A C     1 
ATOM   18969 O  O     . GLU A 1 3930 ? 122.950 181.227 145.885 1.00 93.24  ? 3930 GLU A O     1 
ATOM   18970 C  CB    . GLU A 1 3930 ? 124.551 180.048 143.311 1.00 96.93  ? 3930 GLU A CB    1 
ATOM   18971 C  CG    . GLU A 1 3930 ? 124.957 178.863 142.447 1.00 99.44  ? 3930 GLU A CG    1 
ATOM   18972 C  CD    . GLU A 1 3930 ? 124.795 179.133 140.967 1.00 107.52 ? 3930 GLU A CD    1 
ATOM   18973 O  OE1   . GLU A 1 3930 ? 124.430 180.269 140.610 1.00 107.79 ? 3930 GLU A OE1   1 
ATOM   18974 O  OE2   . GLU A 1 3930 ? 125.036 178.210 140.161 1.00 108.37 ? 3930 GLU A OE2   1 
ATOM   18975 N  N     . GLN A 1 3931 ? 122.328 182.293 144.000 1.00 90.27  ? 3931 GLN A N     1 
ATOM   18976 C  CA    . GLN A 1 3931 ? 121.903 183.475 144.740 1.00 83.78  ? 3931 GLN A CA    1 
ATOM   18977 C  C     . GLN A 1 3931 ? 120.751 183.149 145.678 1.00 91.49  ? 3931 GLN A C     1 
ATOM   18978 O  O     . GLN A 1 3931 ? 120.763 183.556 146.842 1.00 92.91  ? 3931 GLN A O     1 
ATOM   18979 C  CB    . GLN A 1 3931 ? 121.512 184.600 143.783 1.00 76.68  ? 3931 GLN A CB    1 
ATOM   18980 C  CG    . GLN A 1 3931 ? 122.691 185.329 143.167 1.00 75.09  ? 3931 GLN A CG    1 
ATOM   18981 C  CD    . GLN A 1 3931 ? 122.260 186.426 142.219 1.00 77.10  ? 3931 GLN A CD    1 
ATOM   18982 O  OE1   . GLN A 1 3931 ? 121.074 186.592 141.943 1.00 82.26  ? 3931 GLN A OE1   1 
ATOM   18983 N  NE2   . GLN A 1 3931 ? 123.225 187.186 141.716 1.00 71.36  ? 3931 GLN A NE2   1 
ATOM   18984 N  N     . ALA A 1 3932 ? 119.754 182.399 145.199 1.00 92.46  ? 3932 ALA A N     1 
ATOM   18985 C  CA    . ALA A 1 3932 ? 118.626 182.036 146.053 1.00 91.46  ? 3932 ALA A CA    1 
ATOM   18986 C  C     . ALA A 1 3932 ? 119.060 181.109 147.183 1.00 92.55  ? 3932 ALA A C     1 
ATOM   18987 O  O     . ALA A 1 3932 ? 118.548 181.204 148.305 1.00 91.97  ? 3932 ALA A O     1 
ATOM   18988 C  CB    . ALA A 1 3932 ? 117.522 181.389 145.219 1.00 93.49  ? 3932 ALA A CB    1 
ATOM   18989 N  N     . GLU A 1 3933 ? 119.993 180.197 146.899 1.00 94.85  ? 3933 GLU A N     1 
ATOM   18990 C  CA    . GLU A 1 3933 ? 120.569 179.364 147.950 1.00 95.77  ? 3933 GLU A CA    1 
ATOM   18991 C  C     . GLU A 1 3933 ? 121.193 180.221 149.044 1.00 95.58  ? 3933 GLU A C     1 
ATOM   18992 O  O     . GLU A 1 3933 ? 120.939 180.009 150.238 1.00 97.48  ? 3933 GLU A O     1 
ATOM   18993 C  CB    . GLU A 1 3933 ? 121.609 178.425 147.338 1.00 96.17  ? 3933 GLU A CB    1 
ATOM   18994 C  CG    . GLU A 1 3933 ? 122.278 177.454 148.298 1.00 101.51 ? 3933 GLU A CG    1 
ATOM   18995 C  CD    . GLU A 1 3933 ? 121.319 176.439 148.880 1.00 110.03 ? 3933 GLU A CD    1 
ATOM   18996 O  OE1   . GLU A 1 3933 ? 120.291 176.147 148.235 1.00 114.52 ? 3933 GLU A OE1   1 
ATOM   18997 O  OE2   . GLU A 1 3933 ? 121.612 175.910 149.971 1.00 112.29 ? 3933 GLU A OE2   1 
ATOM   18998 N  N     . ALA A 1 3934 ? 121.996 181.212 148.648 1.00 92.68  ? 3934 ALA A N     1 
ATOM   18999 C  CA    . ALA A 1 3934 ? 122.615 182.106 149.622 1.00 86.64  ? 3934 ALA A CA    1 
ATOM   19000 C  C     . ALA A 1 3934 ? 121.568 182.926 150.365 1.00 87.79  ? 3934 ALA A C     1 
ATOM   19001 O  O     . ALA A 1 3934 ? 121.728 183.213 151.555 1.00 91.50  ? 3934 ALA A O     1 
ATOM   19002 C  CB    . ALA A 1 3934 ? 123.621 183.021 148.926 1.00 83.04  ? 3934 ALA A CB    1 
ATOM   19003 N  N     . VAL A 1 3935 ? 120.492 183.315 149.679 1.00 86.58  ? 3935 VAL A N     1 
ATOM   19004 C  CA    . VAL A 1 3935 ? 119.426 184.082 150.322 1.00 87.88  ? 3935 VAL A CA    1 
ATOM   19005 C  C     . VAL A 1 3935 ? 118.764 183.260 151.419 1.00 90.12  ? 3935 VAL A C     1 
ATOM   19006 O  O     . VAL A 1 3935 ? 118.525 183.748 152.529 1.00 88.45  ? 3935 VAL A O     1 
ATOM   19007 C  CB    . VAL A 1 3935 ? 118.395 184.550 149.280 1.00 86.32  ? 3935 VAL A CB    1 
ATOM   19008 C  CG1   . VAL A 1 3935 ? 117.242 185.240 149.961 1.00 89.57  ? 3935 VAL A CG1   1 
ATOM   19009 C  CG2   . VAL A 1 3935 ? 119.031 185.498 148.306 1.00 82.75  ? 3935 VAL A CG2   1 
ATOM   19010 N  N     . VAL A 1 3936 ? 118.444 182.001 151.119 1.00 93.00  ? 3936 VAL A N     1 
ATOM   19011 C  CA    . VAL A 1 3936 ? 117.791 181.161 152.118 1.00 92.54  ? 3936 VAL A CA    1 
ATOM   19012 C  C     . VAL A 1 3936 ? 118.747 180.855 153.266 1.00 94.18  ? 3936 VAL A C     1 
ATOM   19013 O  O     . VAL A 1 3936 ? 118.331 180.765 154.428 1.00 97.01  ? 3936 VAL A O     1 
ATOM   19014 C  CB    . VAL A 1 3936 ? 117.235 179.881 151.470 1.00 96.40  ? 3936 VAL A CB    1 
ATOM   19015 C  CG1   . VAL A 1 3936 ? 116.511 179.035 152.505 1.00 101.75 ? 3936 VAL A CG1   1 
ATOM   19016 C  CG2   . VAL A 1 3936 ? 116.296 180.234 150.332 1.00 100.23 ? 3936 VAL A CG2   1 
ATOM   19017 N  N     . ARG A 1 3937 ? 120.040 180.693 152.968 1.00 93.15  ? 3937 ARG A N     1 
ATOM   19018 C  CA    . ARG A 1 3937 ? 121.023 180.523 154.037 1.00 91.45  ? 3937 ARG A CA    1 
ATOM   19019 C  C     . ARG A 1 3937 ? 121.098 181.761 154.925 1.00 88.46  ? 3937 ARG A C     1 
ATOM   19020 O  O     . ARG A 1 3937 ? 121.210 181.651 156.151 1.00 88.62  ? 3937 ARG A O     1 
ATOM   19021 C  CB    . ARG A 1 3937 ? 122.396 180.204 153.448 1.00 89.29  ? 3937 ARG A CB    1 
ATOM   19022 C  CG    . ARG A 1 3937 ? 122.479 178.850 152.774 1.00 94.82  ? 3937 ARG A CG    1 
ATOM   19023 C  CD    . ARG A 1 3937 ? 123.861 178.594 152.204 1.00 95.71  ? 3937 ARG A CD    1 
ATOM   19024 N  NE    . ARG A 1 3937 ? 123.936 177.300 151.537 1.00 100.67 ? 3937 ARG A NE    1 
ATOM   19025 C  CZ    . ARG A 1 3937 ? 125.006 176.846 150.900 1.00 101.21 ? 3937 ARG A CZ    1 
ATOM   19026 N  NH1   . ARG A 1 3937 ? 126.110 177.566 150.804 1.00 98.75  ? 3937 ARG A NH1   1 
ATOM   19027 N  NH2   . ARG A 1 3937 ? 124.964 175.641 150.339 1.00 101.01 ? 3937 ARG A NH2   1 
ATOM   19028 N  N     . LEU A 1 3938 ? 121.046 182.949 154.321 1.00 85.39  ? 3938 LEU A N     1 
ATOM   19029 C  CA    . LEU A 1 3938 ? 121.098 184.190 155.086 1.00 84.39  ? 3938 LEU A CA    1 
ATOM   19030 C  C     . LEU A 1 3938 ? 119.828 184.405 155.896 1.00 90.88  ? 3938 LEU A C     1 
ATOM   19031 O  O     . LEU A 1 3938 ? 119.869 185.039 156.956 1.00 91.19  ? 3938 LEU A O     1 
ATOM   19032 C  CB    . LEU A 1 3938 ? 121.330 185.368 154.140 1.00 80.94  ? 3938 LEU A CB    1 
ATOM   19033 C  CG    . LEU A 1 3938 ? 121.572 186.748 154.747 1.00 78.72  ? 3938 LEU A CG    1 
ATOM   19034 C  CD1   . LEU A 1 3938 ? 122.781 186.728 155.666 1.00 80.72  ? 3938 LEU A CD1   1 
ATOM   19035 C  CD2   . LEU A 1 3938 ? 121.745 187.781 153.647 1.00 70.49  ? 3938 LEU A CD2   1 
ATOM   19036 N  N     . SER A 1 3939 ? 118.696 183.886 155.417 1.00 95.36  ? 3939 SER A N     1 
ATOM   19037 C  CA    . SER A 1 3939 ? 117.425 184.066 156.105 1.00 94.55  ? 3939 SER A CA    1 
ATOM   19038 C  C     . SER A 1 3939 ? 117.380 183.379 157.463 1.00 95.43  ? 3939 SER A C     1 
ATOM   19039 O  O     . SER A 1 3939 ? 116.467 183.660 158.247 1.00 95.57  ? 3939 SER A O     1 
ATOM   19040 C  CB    . SER A 1 3939 ? 116.281 183.551 155.232 1.00 93.61  ? 3939 SER A CB    1 
ATOM   19041 O  OG    . SER A 1 3939 ? 116.300 182.137 155.154 1.00 97.27  ? 3939 SER A OG    1 
ATOM   19042 N  N     . CYS A 1 3940 ? 118.330 182.488 157.758 1.00 96.12  ? 3940 CYS A N     1 
ATOM   19043 C  CA    . CYS A 1 3940 ? 118.367 181.855 159.071 1.00 98.98  ? 3940 CYS A CA    1 
ATOM   19044 C  C     . CYS A 1 3940 ? 118.649 182.867 160.174 1.00 98.60  ? 3940 CYS A C     1 
ATOM   19045 O  O     . CYS A 1 3940 ? 118.240 182.662 161.323 1.00 97.47  ? 3940 CYS A O     1 
ATOM   19046 C  CB    . CYS A 1 3940 ? 119.413 180.742 159.087 1.00 98.62  ? 3940 CYS A CB    1 
ATOM   19047 S  SG    . CYS A 1 3940 ? 119.147 179.462 157.841 1.00 100.63 ? 3940 CYS A SG    1 
ATOM   19048 N  N     . LEU A 1 3941 ? 119.346 183.952 159.852 1.00 97.75  ? 3941 LEU A N     1 
ATOM   19049 C  CA    . LEU A 1 3941 ? 119.563 185.006 160.830 1.00 98.45  ? 3941 LEU A CA    1 
ATOM   19050 C  C     . LEU A 1 3941 ? 118.242 185.708 161.139 1.00 100.45 ? 3941 LEU A C     1 
ATOM   19051 O  O     . LEU A 1 3941 ? 117.427 185.924 160.237 1.00 102.43 ? 3941 LEU A O     1 
ATOM   19052 C  CB    . LEU A 1 3941 ? 120.582 186.020 160.313 1.00 96.62  ? 3941 LEU A CB    1 
ATOM   19053 C  CG    . LEU A 1 3941 ? 122.011 185.528 160.080 1.00 92.12  ? 3941 LEU A CG    1 
ATOM   19054 C  CD1   . LEU A 1 3941 ? 122.955 186.708 159.929 1.00 84.63  ? 3941 LEU A CD1   1 
ATOM   19055 C  CD2   . LEU A 1 3941 ? 122.463 184.620 161.211 1.00 88.42  ? 3941 LEU A CD2   1 
ATOM   19056 N  N     . PRO A 1 3942 ? 117.999 186.069 162.402 1.00 100.98 ? 3942 PRO A N     1 
ATOM   19057 C  CA    . PRO A 1 3942 ? 116.738 186.753 162.736 1.00 104.38 ? 3942 PRO A CA    1 
ATOM   19058 C  C     . PRO A 1 3942 ? 116.553 188.076 162.014 1.00 106.60 ? 3942 PRO A C     1 
ATOM   19059 O  O     . PRO A 1 3942 ? 115.412 188.466 161.741 1.00 108.02 ? 3942 PRO A O     1 
ATOM   19060 C  CB    . PRO A 1 3942 ? 116.837 186.948 164.256 1.00 103.60 ? 3942 PRO A CB    1 
ATOM   19061 C  CG    . PRO A 1 3942 ? 118.294 186.823 164.572 1.00 100.98 ? 3942 PRO A CG    1 
ATOM   19062 C  CD    . PRO A 1 3942 ? 118.838 185.839 163.588 1.00 99.92  ? 3942 PRO A CD    1 
ATOM   19063 N  N     . ALA A 1 3943 ? 117.641 188.782 161.699 1.00 104.01 ? 3943 ALA A N     1 
ATOM   19064 C  CA    . ALA A 1 3943 ? 117.516 190.074 161.032 1.00 101.91 ? 3943 ALA A CA    1 
ATOM   19065 C  C     . ALA A 1 3943 ? 117.019 189.929 159.600 1.00 101.15 ? 3943 ALA A C     1 
ATOM   19066 O  O     . ALA A 1 3943 ? 116.381 190.847 159.073 1.00 100.36 ? 3943 ALA A O     1 
ATOM   19067 C  CB    . ALA A 1 3943 ? 118.855 190.810 161.055 1.00 93.75  ? 3943 ALA A CB    1 
ATOM   19068 N  N     . PHE A 1 3944 ? 117.297 188.796 158.957 1.00 100.43 ? 3944 PHE A N     1 
ATOM   19069 C  CA    . PHE A 1 3944 ? 116.935 188.572 157.563 1.00 99.79  ? 3944 PHE A CA    1 
ATOM   19070 C  C     . PHE A 1 3944 ? 115.819 187.540 157.418 1.00 107.39 ? 3944 PHE A C     1 
ATOM   19071 O  O     . PHE A 1 3944 ? 115.757 186.823 156.417 1.00 105.86 ? 3944 PHE A O     1 
ATOM   19072 C  CB    . PHE A 1 3944 ? 118.162 188.144 156.759 1.00 91.34  ? 3944 PHE A CB    1 
ATOM   19073 C  CG    . PHE A 1 3944 ? 119.238 189.189 156.693 1.00 88.11  ? 3944 PHE A CG    1 
ATOM   19074 C  CD1   . PHE A 1 3944 ? 119.046 190.356 155.976 1.00 83.07  ? 3944 PHE A CD1   1 
ATOM   19075 C  CD2   . PHE A 1 3944 ? 120.442 189.002 157.349 1.00 86.09  ? 3944 PHE A CD2   1 
ATOM   19076 C  CE1   . PHE A 1 3944 ? 120.035 191.317 155.916 1.00 78.95  ? 3944 PHE A CE1   1 
ATOM   19077 C  CE2   . PHE A 1 3944 ? 121.434 189.960 157.291 1.00 76.13  ? 3944 PHE A CE2   1 
ATOM   19078 C  CZ    . PHE A 1 3944 ? 121.230 191.118 156.574 1.00 76.33  ? 3944 PHE A CZ    1 
ATOM   19079 N  N     . LYS A 1 3945 ? 114.932 187.454 158.412 1.00 112.71 ? 3945 LYS A N     1 
ATOM   19080 C  CA    . LYS A 1 3945 ? 113.856 186.468 158.360 1.00 113.35 ? 3945 LYS A CA    1 
ATOM   19081 C  C     . LYS A 1 3945 ? 112.886 186.758 157.219 1.00 114.08 ? 3945 LYS A C     1 
ATOM   19082 O  O     . LYS A 1 3945 ? 112.416 185.831 156.548 1.00 109.74 ? 3945 LYS A O     1 
ATOM   19083 C  CB    . LYS A 1 3945 ? 113.124 186.420 159.702 1.00 108.97 ? 3945 LYS A CB    1 
ATOM   19084 C  CG    . LYS A 1 3945 ? 112.568 187.753 160.169 1.00 111.56 ? 3945 LYS A CG    1 
ATOM   19085 C  CD    . LYS A 1 3945 ? 111.933 187.631 161.544 1.00 120.86 ? 3945 LYS A CD    1 
ATOM   19086 C  CE    . LYS A 1 3945 ? 111.453 188.980 162.053 1.00 119.91 ? 3945 LYS A CE    1 
ATOM   19087 N  NZ    . LYS A 1 3945 ? 110.848 188.878 163.409 1.00 115.00 ? 3945 LYS A NZ    1 
ATOM   19088 N  N     . ASP A 1 3946 ? 112.576 188.033 156.980 1.00 112.88 ? 3946 ASP A N     1 
ATOM   19089 C  CA    . ASP A 1 3946 ? 111.693 188.439 155.893 1.00 111.92 ? 3946 ASP A CA    1 
ATOM   19090 C  C     . ASP A 1 3946 ? 112.469 188.882 154.659 1.00 110.84 ? 3946 ASP A C     1 
ATOM   19091 O  O     . ASP A 1 3946 ? 112.021 189.771 153.926 1.00 107.90 ? 3946 ASP A O     1 
ATOM   19092 C  CB    . ASP A 1 3946 ? 110.755 189.552 156.360 1.00 114.21 ? 3946 ASP A CB    1 
ATOM   19093 C  CG    . ASP A 1 3946 ? 111.498 190.729 156.961 1.00 116.72 ? 3946 ASP A CG    1 
ATOM   19094 O  OD1   . ASP A 1 3946 ? 112.733 190.638 157.124 1.00 113.35 ? 3946 ASP A OD1   1 
ATOM   19095 O  OD2   . ASP A 1 3946 ? 110.848 191.750 157.268 1.00 116.38 ? 3946 ASP A OD2   1 
ATOM   19096 N  N     . LEU A 1 3947 ? 113.635 188.280 154.420 1.00 110.32 ? 3947 LEU A N     1 
ATOM   19097 C  CA    . LEU A 1 3947 ? 114.466 188.696 153.295 1.00 106.79 ? 3947 LEU A CA    1 
ATOM   19098 C  C     . LEU A 1 3947 ? 113.814 188.340 151.964 1.00 106.57 ? 3947 LEU A C     1 
ATOM   19099 O  O     . LEU A 1 3947 ? 113.919 189.098 150.994 1.00 105.25 ? 3947 LEU A O     1 
ATOM   19100 C  CB    . LEU A 1 3947 ? 115.855 188.068 153.424 1.00 100.52 ? 3947 LEU A CB    1 
ATOM   19101 C  CG    . LEU A 1 3947 ? 116.839 188.155 152.261 1.00 95.25  ? 3947 LEU A CG    1 
ATOM   19102 C  CD1   . LEU A 1 3947 ? 117.177 189.599 151.976 1.00 86.73  ? 3947 LEU A CD1   1 
ATOM   19103 C  CD2   . LEU A 1 3947 ? 118.098 187.391 152.618 1.00 88.43  ? 3947 LEU A CD2   1 
ATOM   19104 N  N     . ILE A 1 3948 ? 113.124 187.198 151.901 1.00 107.13 ? 3948 ILE A N     1 
ATOM   19105 C  CA    . ILE A 1 3948 ? 112.390 186.832 150.691 1.00 107.35 ? 3948 ILE A CA    1 
ATOM   19106 C  C     . ILE A 1 3948 ? 111.303 187.858 150.394 1.00 109.89 ? 3948 ILE A C     1 
ATOM   19107 O  O     . ILE A 1 3948 ? 111.140 188.303 149.249 1.00 110.21 ? 3948 ILE A O     1 
ATOM   19108 C  CB    . ILE A 1 3948 ? 111.795 185.419 150.833 1.00 107.25 ? 3948 ILE A CB    1 
ATOM   19109 C  CG1   . ILE A 1 3948 ? 112.892 184.384 151.076 1.00 103.40 ? 3948 ILE A CG1   1 
ATOM   19110 C  CG2   . ILE A 1 3948 ? 110.997 185.052 149.594 1.00 109.97 ? 3948 ILE A CG2   1 
ATOM   19111 C  CD1   . ILE A 1 3948 ? 113.881 184.290 149.952 1.00 99.73  ? 3948 ILE A CD1   1 
ATOM   19112 N  N     . ALA A 1 3949 ? 110.537 188.239 151.419 1.00 110.17 ? 3949 ALA A N     1 
ATOM   19113 C  CA    . ALA A 1 3949 ? 109.445 189.185 151.221 1.00 108.55 ? 3949 ALA A CA    1 
ATOM   19114 C  C     . ALA A 1 3949 ? 109.963 190.542 150.767 1.00 111.05 ? 3949 ALA A C     1 
ATOM   19115 O  O     . ALA A 1 3949 ? 109.373 191.174 149.884 1.00 110.39 ? 3949 ALA A O     1 
ATOM   19116 C  CB    . ALA A 1 3949 ? 108.631 189.323 152.507 1.00 107.55 ? 3949 ALA A CB    1 
ATOM   19117 N  N     . LYS A 1 3950 ? 111.064 191.009 151.359 1.00 111.90 ? 3950 LYS A N     1 
ATOM   19118 C  CA    . LYS A 1 3950 ? 111.614 192.302 150.964 1.00 110.60 ? 3950 LYS A CA    1 
ATOM   19119 C  C     . LYS A 1 3950 ? 112.236 192.240 149.574 1.00 110.91 ? 3950 LYS A C     1 
ATOM   19120 O  O     . LYS A 1 3950 ? 112.201 193.226 148.830 1.00 114.23 ? 3950 LYS A O     1 
ATOM   19121 C  CB    . LYS A 1 3950 ? 112.635 192.777 151.995 1.00 100.58 ? 3950 LYS A CB    1 
ATOM   19122 C  CG    . LYS A 1 3950 ? 112.022 193.142 153.337 1.00 103.34 ? 3950 LYS A CG    1 
ATOM   19123 C  CD    . LYS A 1 3950 ? 113.048 193.766 154.265 1.00 103.87 ? 3950 LYS A CD    1 
ATOM   19124 C  CE    . LYS A 1 3950 ? 112.415 194.190 155.579 1.00 103.94 ? 3950 LYS A CE    1 
ATOM   19125 N  NZ    . LYS A 1 3950 ? 113.365 194.959 156.427 1.00 102.07 ? 3950 LYS A NZ    1 
ATOM   19126 N  N     . VAL A 1 3951 ? 112.817 191.094 149.208 1.00 107.84 ? 3951 VAL A N     1 
ATOM   19127 C  CA    . VAL A 1 3951 ? 113.356 190.934 147.860 1.00 108.26 ? 3951 VAL A CA    1 
ATOM   19128 C  C     . VAL A 1 3951 ? 112.236 191.009 146.830 1.00 113.50 ? 3951 VAL A C     1 
ATOM   19129 O  O     . VAL A 1 3951 ? 112.347 191.702 145.812 1.00 111.49 ? 3951 VAL A O     1 
ATOM   19130 C  CB    . VAL A 1 3951 ? 114.143 189.616 147.747 1.00 104.25 ? 3951 VAL A CB    1 
ATOM   19131 C  CG1   . VAL A 1 3951 ? 114.246 189.178 146.296 1.00 102.18 ? 3951 VAL A CG1   1 
ATOM   19132 C  CG2   . VAL A 1 3951 ? 115.530 189.778 148.342 1.00 98.21  ? 3951 VAL A CG2   1 
ATOM   19133 N  N     . GLN A 1 3952 ? 111.133 190.299 147.084 1.00 114.51 ? 3952 GLN A N     1 
ATOM   19134 C  CA    . GLN A 1 3952 ? 110.024 190.308 146.133 1.00 113.00 ? 3952 GLN A CA    1 
ATOM   19135 C  C     . GLN A 1 3952 ? 109.331 191.666 146.092 1.00 114.44 ? 3952 GLN A C     1 
ATOM   19136 O  O     . GLN A 1 3952 ? 108.937 192.135 145.018 1.00 112.71 ? 3952 GLN A O     1 
ATOM   19137 C  CB    . GLN A 1 3952 ? 109.022 189.207 146.475 1.00 112.83 ? 3952 GLN A CB    1 
ATOM   19138 C  CG    . GLN A 1 3952 ? 109.610 187.808 146.466 1.00 116.10 ? 3952 GLN A CG    1 
ATOM   19139 C  CD    . GLN A 1 3952 ? 108.803 186.835 147.301 1.00 119.21 ? 3952 GLN A CD    1 
ATOM   19140 O  OE1   . GLN A 1 3952 ? 108.647 187.018 148.508 1.00 119.16 ? 3952 GLN A OE1   1 
ATOM   19141 N  NE2   . GLN A 1 3952 ? 108.288 185.791 146.662 1.00 118.62 ? 3952 GLN A NE2   1 
ATOM   19142 N  N     . ALA A 1 3953 ? 109.174 192.313 147.249 1.00 116.09 ? 3953 ALA A N     1 
ATOM   19143 C  CA    . ALA A 1 3953 ? 108.437 193.571 147.306 1.00 118.90 ? 3953 ALA A CA    1 
ATOM   19144 C  C     . ALA A 1 3953 ? 109.223 194.725 146.698 1.00 123.44 ? 3953 ALA A C     1 
ATOM   19145 O  O     . ALA A 1 3953 ? 108.626 195.639 146.119 1.00 120.89 ? 3953 ALA A O     1 
ATOM   19146 C  CB    . ALA A 1 3953 ? 108.062 193.892 148.752 1.00 111.91 ? 3953 ALA A CB    1 
ATOM   19147 N  N     . ASP A 1 3954 ? 110.547 194.710 146.826 1.00 124.37 ? 3954 ASP A N     1 
ATOM   19148 C  CA    . ASP A 1 3954 ? 111.362 195.793 146.293 1.00 124.06 ? 3954 ASP A CA    1 
ATOM   19149 C  C     . ASP A 1 3954 ? 111.280 195.825 144.772 1.00 122.95 ? 3954 ASP A C     1 
ATOM   19150 O  O     . ASP A 1 3954 ? 111.306 194.786 144.107 1.00 119.27 ? 3954 ASP A O     1 
ATOM   19151 C  CB    . ASP A 1 3954 ? 112.814 195.634 146.741 1.00 120.39 ? 3954 ASP A CB    1 
ATOM   19152 C  CG    . ASP A 1 3954 ? 113.658 196.857 146.439 1.00 122.50 ? 3954 ASP A CG    1 
ATOM   19153 O  OD1   . ASP A 1 3954 ? 113.100 197.871 145.968 1.00 122.64 ? 3954 ASP A OD1   1 
ATOM   19154 O  OD2   . ASP A 1 3954 ? 114.884 196.805 146.673 1.00 118.68 ? 3954 ASP A OD2   1 
ATOM   19155 N  N     . GLU A 1 3955 ? 111.180 197.035 144.222 1.00 124.17 ? 3955 GLU A N     1 
ATOM   19156 C  CA    . GLU A 1 3955 ? 111.077 197.240 142.782 1.00 124.75 ? 3955 GLU A CA    1 
ATOM   19157 C  C     . GLU A 1 3955 ? 112.423 197.509 142.124 1.00 119.94 ? 3955 GLU A C     1 
ATOM   19158 O  O     . GLU A 1 3955 ? 112.651 197.076 140.991 1.00 116.01 ? 3955 GLU A O     1 
ATOM   19159 C  CB    . GLU A 1 3955 ? 110.122 198.400 142.483 1.00 125.74 ? 3955 GLU A CB    1 
ATOM   19160 C  CG    . GLU A 1 3955 ? 109.821 198.597 141.006 1.00 130.38 ? 3955 GLU A CG    1 
ATOM   19161 C  CD    . GLU A 1 3955 ? 109.025 197.448 140.415 1.00 132.85 ? 3955 GLU A CD    1 
ATOM   19162 O  OE1   . GLU A 1 3955 ? 108.273 196.795 141.168 1.00 130.66 ? 3955 GLU A OE1   1 
ATOM   19163 O  OE2   . GLU A 1 3955 ? 109.155 197.197 139.198 1.00 130.44 ? 3955 GLU A OE2   1 
ATOM   19164 N  N     . GLN A 1 3956 ? 113.322 198.209 142.812 1.00 121.07 ? 3956 GLN A N     1 
ATOM   19165 C  CA    . GLN A 1 3956 ? 114.645 198.516 142.287 1.00 116.67 ? 3956 GLN A CA    1 
ATOM   19166 C  C     . GLN A 1 3956 ? 115.675 197.444 142.623 1.00 109.64 ? 3956 GLN A C     1 
ATOM   19167 O  O     . GLN A 1 3956 ? 116.875 197.683 142.460 1.00 104.94 ? 3956 GLN A O     1 
ATOM   19168 C  CB    . GLN A 1 3956 ? 115.119 199.876 142.810 1.00 120.64 ? 3956 GLN A CB    1 
ATOM   19169 C  CG    . GLN A 1 3956 ? 114.089 200.990 142.684 1.00 126.90 ? 3956 GLN A CG    1 
ATOM   19170 C  CD    . GLN A 1 3956 ? 113.208 201.120 143.913 1.00 133.53 ? 3956 GLN A CD    1 
ATOM   19171 O  OE1   . GLN A 1 3956 ? 112.506 200.182 144.292 1.00 131.47 ? 3956 GLN A OE1   1 
ATOM   19172 N  NE2   . GLN A 1 3956 ? 113.239 202.290 144.540 1.00 133.92 ? 3956 GLN A NE2   1 
ATOM   19173 N  N     . PHE A 1 3957 ? 115.234 196.277 143.097 1.00 106.31 ? 3957 PHE A N     1 
ATOM   19174 C  CA    . PHE A 1 3957 ? 116.168 195.187 143.363 1.00 98.96  ? 3957 PHE A CA    1 
ATOM   19175 C  C     . PHE A 1 3957 ? 116.825 194.696 142.081 1.00 92.29  ? 3957 PHE A C     1 
ATOM   19176 O  O     . PHE A 1 3957 ? 118.014 194.359 142.074 1.00 91.72  ? 3957 PHE A O     1 
ATOM   19177 C  CB    . PHE A 1 3957 ? 115.448 194.037 144.065 1.00 100.34 ? 3957 PHE A CB    1 
ATOM   19178 C  CG    . PHE A 1 3957 ? 116.374 193.071 144.742 1.00 97.24  ? 3957 PHE A CG    1 
ATOM   19179 C  CD1   . PHE A 1 3957 ? 117.149 193.470 145.817 1.00 93.14  ? 3957 PHE A CD1   1 
ATOM   19180 C  CD2   . PHE A 1 3957 ? 116.474 191.764 144.299 1.00 94.77  ? 3957 PHE A CD2   1 
ATOM   19181 C  CE1   . PHE A 1 3957 ? 118.001 192.582 146.440 1.00 86.03  ? 3957 PHE A CE1   1 
ATOM   19182 C  CE2   . PHE A 1 3957 ? 117.325 190.871 144.918 1.00 90.01  ? 3957 PHE A CE2   1 
ATOM   19183 C  CZ    . PHE A 1 3957 ? 118.089 191.281 145.989 1.00 85.29  ? 3957 PHE A CZ    1 
ATOM   19184 N  N     . GLY A 1 3958 ? 116.064 194.637 140.988 1.00 90.60  ? 3958 GLY A N     1 
ATOM   19185 C  CA    . GLY A 1 3958 ? 116.624 194.153 139.736 1.00 87.35  ? 3958 GLY A CA    1 
ATOM   19186 C  C     . GLY A 1 3958 ? 117.723 195.051 139.203 1.00 86.50  ? 3958 GLY A C     1 
ATOM   19187 O  O     . GLY A 1 3958 ? 118.754 194.575 138.723 1.00 86.50  ? 3958 GLY A O     1 
ATOM   19188 N  N     . ILE A 1 3959 ? 117.513 196.367 139.273 1.00 87.59  ? 3959 ILE A N     1 
ATOM   19189 C  CA    . ILE A 1 3959 ? 118.523 197.294 138.774 1.00 87.48  ? 3959 ILE A CA    1 
ATOM   19190 C  C     . ILE A 1 3959 ? 119.735 197.321 139.697 1.00 86.05  ? 3959 ILE A C     1 
ATOM   19191 O  O     . ILE A 1 3959 ? 120.863 197.551 139.242 1.00 90.94  ? 3959 ILE A O     1 
ATOM   19192 C  CB    . ILE A 1 3959 ? 117.918 198.698 138.573 1.00 89.27  ? 3959 ILE A CB    1 
ATOM   19193 C  CG1   . ILE A 1 3959 ? 118.792 199.526 137.631 1.00 86.65  ? 3959 ILE A CG1   1 
ATOM   19194 C  CG2   . ILE A 1 3959 ? 117.741 199.422 139.899 1.00 90.79  ? 3959 ILE A CG2   1 
ATOM   19195 C  CD1   . ILE A 1 3959 ? 118.110 200.770 137.111 1.00 90.48  ? 3959 ILE A CD1   1 
ATOM   19196 N  N     . TRP A 1 3960 ? 119.536 197.092 140.997 1.00 81.27  ? 3960 TRP A N     1 
ATOM   19197 C  CA    . TRP A 1 3960 ? 120.665 197.072 141.921 1.00 76.60  ? 3960 TRP A CA    1 
ATOM   19198 C  C     . TRP A 1 3960 ? 121.510 195.819 141.729 1.00 73.28  ? 3960 TRP A C     1 
ATOM   19199 O  O     . TRP A 1 3960 ? 122.744 195.888 141.704 1.00 71.99  ? 3960 TRP A O     1 
ATOM   19200 C  CB    . TRP A 1 3960 ? 120.173 197.157 143.365 1.00 76.59  ? 3960 TRP A CB    1 
ATOM   19201 C  CG    . TRP A 1 3960 ? 121.286 196.999 144.350 1.00 72.48  ? 3960 TRP A CG    1 
ATOM   19202 C  CD1   . TRP A 1 3960 ? 122.234 197.924 144.670 1.00 70.51  ? 3960 TRP A CD1   1 
ATOM   19203 C  CD2   . TRP A 1 3960 ? 121.601 195.825 145.104 1.00 65.78  ? 3960 TRP A CD2   1 
ATOM   19204 N  NE1   . TRP A 1 3960 ? 123.103 197.409 145.599 1.00 66.22  ? 3960 TRP A NE1   1 
ATOM   19205 C  CE2   . TRP A 1 3960 ? 122.738 196.119 145.879 1.00 62.60  ? 3960 TRP A CE2   1 
ATOM   19206 C  CE3   . TRP A 1 3960 ? 121.025 194.558 145.208 1.00 69.46  ? 3960 TRP A CE3   1 
ATOM   19207 C  CZ2   . TRP A 1 3960 ? 123.309 195.194 146.745 1.00 62.83  ? 3960 TRP A CZ2   1 
ATOM   19208 C  CZ3   . TRP A 1 3960 ? 121.593 193.642 146.066 1.00 68.67  ? 3960 TRP A CZ3   1 
ATOM   19209 C  CH2   . TRP A 1 3960 ? 122.723 193.963 146.824 1.00 62.96  ? 3960 TRP A CH2   1 
ATOM   19210 N  N     . LEU A 1 3961 ? 120.859 194.661 141.598 1.00 72.91  ? 3961 LEU A N     1 
ATOM   19211 C  CA    . LEU A 1 3961 ? 121.592 193.406 141.473 1.00 68.79  ? 3961 LEU A CA    1 
ATOM   19212 C  C     . LEU A 1 3961 ? 122.399 193.352 140.183 1.00 71.55  ? 3961 LEU A C     1 
ATOM   19213 O  O     . LEU A 1 3961 ? 123.368 192.591 140.089 1.00 71.05  ? 3961 LEU A O     1 
ATOM   19214 C  CB    . LEU A 1 3961 ? 120.619 192.230 141.552 1.00 67.27  ? 3961 LEU A CB    1 
ATOM   19215 C  CG    . LEU A 1 3961 ? 121.207 190.828 141.710 1.00 68.67  ? 3961 LEU A CG    1 
ATOM   19216 C  CD1   . LEU A 1 3961 ? 121.943 190.711 143.031 1.00 69.44  ? 3961 LEU A CD1   1 
ATOM   19217 C  CD2   . LEU A 1 3961 ? 120.113 189.780 141.614 1.00 73.74  ? 3961 LEU A CD2   1 
ATOM   19218 N  N     . ASP A 1 3962 ? 122.020 194.146 139.184 1.00 74.40  ? 3962 ASP A N     1 
ATOM   19219 C  CA    . ASP A 1 3962 ? 122.743 194.233 137.924 1.00 75.33  ? 3962 ASP A CA    1 
ATOM   19220 C  C     . ASP A 1 3962 ? 123.669 195.442 137.863 1.00 76.40  ? 3962 ASP A C     1 
ATOM   19221 O  O     . ASP A 1 3962 ? 124.275 195.692 136.817 1.00 78.73  ? 3962 ASP A O     1 
ATOM   19222 C  CB    . ASP A 1 3962 ? 121.757 194.275 136.756 1.00 81.75  ? 3962 ASP A CB    1 
ATOM   19223 C  CG    . ASP A 1 3962 ? 121.187 192.911 136.424 1.00 89.25  ? 3962 ASP A CG    1 
ATOM   19224 O  OD1   . ASP A 1 3962 ? 121.107 192.061 137.335 1.00 87.64  ? 3962 ASP A OD1   1 
ATOM   19225 O  OD2   . ASP A 1 3962 ? 120.816 192.689 135.252 1.00 91.48  ? 3962 ASP A OD2   1 
ATOM   19226 N  N     . SER A 1 3963 ? 123.791 196.193 138.954 1.00 75.84  ? 3963 SER A N     1 
ATOM   19227 C  CA    . SER A 1 3963 ? 124.579 197.414 138.951 1.00 70.77  ? 3963 SER A CA    1 
ATOM   19228 C  C     . SER A 1 3963 ? 126.071 197.102 138.907 1.00 69.65  ? 3963 SER A C     1 
ATOM   19229 O  O     . SER A 1 3963 ? 126.520 196.010 139.265 1.00 67.92  ? 3963 SER A O     1 
ATOM   19230 C  CB    . SER A 1 3963 ? 124.259 198.263 140.181 1.00 66.79  ? 3963 SER A CB    1 
ATOM   19231 O  OG    . SER A 1 3963 ? 125.011 199.464 140.177 1.00 72.08  ? 3963 SER A OG    1 
ATOM   19232 N  N     . SER A 1 3964 ? 126.844 198.091 138.451 1.00 68.21  ? 3964 SER A N     1 
ATOM   19233 C  CA    . SER A 1 3964 ? 128.290 197.919 138.356 1.00 68.23  ? 3964 SER A CA    1 
ATOM   19234 C  C     . SER A 1 3964 ? 128.940 197.883 139.734 1.00 73.01  ? 3964 SER A C     1 
ATOM   19235 O  O     . SER A 1 3964 ? 129.845 197.077 139.978 1.00 75.60  ? 3964 SER A O     1 
ATOM   19236 C  CB    . SER A 1 3964 ? 128.895 199.038 137.509 1.00 69.01  ? 3964 SER A CB    1 
ATOM   19237 O  OG    . SER A 1 3964 ? 128.666 200.304 138.102 1.00 68.15  ? 3964 SER A OG    1 
ATOM   19238 N  N     . SER A 1 3965 ? 128.496 198.748 140.646 1.00 74.41  ? 3965 SER A N     1 
ATOM   19239 C  CA    . SER A 1 3965 ? 129.036 198.829 142.003 1.00 67.40  ? 3965 SER A CA    1 
ATOM   19240 C  C     . SER A 1 3965 ? 127.879 198.774 142.989 1.00 63.81  ? 3965 SER A C     1 
ATOM   19241 O  O     . SER A 1 3965 ? 127.487 199.798 143.563 1.00 66.80  ? 3965 SER A O     1 
ATOM   19242 C  CB    . SER A 1 3965 ? 129.859 200.102 142.197 1.00 68.46  ? 3965 SER A CB    1 
ATOM   19243 O  OG    . SER A 1 3965 ? 129.037 201.252 142.108 1.00 70.42  ? 3965 SER A OG    1 
ATOM   19244 N  N     . PRO A 1 3966 ? 127.298 197.590 143.202 1.00 63.61  ? 3966 PRO A N     1 
ATOM   19245 C  CA    . PRO A 1 3966 ? 126.171 197.487 144.140 1.00 65.07  ? 3966 PRO A CA    1 
ATOM   19246 C  C     . PRO A 1 3966 ? 126.547 197.751 145.585 1.00 69.94  ? 3966 PRO A C     1 
ATOM   19247 O  O     . PRO A 1 3966 ? 125.658 198.057 146.387 1.00 75.43  ? 3966 PRO A O     1 
ATOM   19248 C  CB    . PRO A 1 3966 ? 125.691 196.044 143.949 1.00 64.59  ? 3966 PRO A CB    1 
ATOM   19249 C  CG    . PRO A 1 3966 ? 126.905 195.319 143.509 1.00 63.98  ? 3966 PRO A CG    1 
ATOM   19250 C  CD    . PRO A 1 3966 ? 127.656 196.282 142.634 1.00 65.20  ? 3966 PRO A CD    1 
ATOM   19251 N  N     . GLU A 1 3967 ? 127.828 197.640 145.947 1.00 70.24  ? 3967 GLU A N     1 
ATOM   19252 C  CA    . GLU A 1 3967 ? 128.218 197.809 147.343 1.00 60.88  ? 3967 GLU A CA    1 
ATOM   19253 C  C     . GLU A 1 3967 ? 128.020 199.242 147.817 1.00 63.83  ? 3967 GLU A C     1 
ATOM   19254 O  O     . GLU A 1 3967 ? 127.828 199.474 149.015 1.00 66.21  ? 3967 GLU A O     1 
ATOM   19255 C  CB    . GLU A 1 3967 ? 129.671 197.377 147.542 1.00 52.58  ? 3967 GLU A CB    1 
ATOM   19256 C  CG    . GLU A 1 3967 ? 130.698 198.357 147.006 1.00 58.46  ? 3967 GLU A CG    1 
ATOM   19257 C  CD    . GLU A 1 3967 ? 131.170 198.008 145.613 1.00 65.64  ? 3967 GLU A CD    1 
ATOM   19258 O  OE1   . GLU A 1 3967 ? 130.846 196.903 145.133 1.00 64.71  ? 3967 GLU A OE1   1 
ATOM   19259 O  OE2   . GLU A 1 3967 ? 131.870 198.838 144.997 1.00 74.11  ? 3967 GLU A OE2   1 
ATOM   19260 N  N     . GLN A 1 3968 ? 128.060 200.212 146.904 1.00 65.53  ? 3968 GLN A N     1 
ATOM   19261 C  CA    . GLN A 1 3968 ? 127.877 201.607 147.277 1.00 69.77  ? 3968 GLN A CA    1 
ATOM   19262 C  C     . GLN A 1 3968 ? 126.413 202.004 147.389 1.00 72.01  ? 3968 GLN A C     1 
ATOM   19263 O  O     . GLN A 1 3968 ? 126.123 203.103 147.875 1.00 76.09  ? 3968 GLN A O     1 
ATOM   19264 C  CB    . GLN A 1 3968 ? 128.575 202.517 146.265 1.00 70.20  ? 3968 GLN A CB    1 
ATOM   19265 C  CG    . GLN A 1 3968 ? 129.975 202.066 145.892 1.00 74.52  ? 3968 GLN A CG    1 
ATOM   19266 C  CD    . GLN A 1 3968 ? 130.837 203.205 145.389 1.00 86.13  ? 3968 GLN A CD    1 
ATOM   19267 O  OE1   . GLN A 1 3968 ? 131.816 203.587 146.028 1.00 94.38  ? 3968 GLN A OE1   1 
ATOM   19268 N  NE2   . GLN A 1 3968 ? 130.476 203.755 144.235 1.00 90.44  ? 3968 GLN A NE2   1 
ATOM   19269 N  N     . THR A 1 3969 ? 125.488 201.148 146.954 1.00 71.18  ? 3969 THR A N     1 
ATOM   19270 C  CA    . THR A 1 3969 ? 124.061 201.447 146.980 1.00 72.36  ? 3969 THR A CA    1 
ATOM   19271 C  C     . THR A 1 3969 ? 123.259 200.269 147.520 1.00 70.93  ? 3969 THR A C     1 
ATOM   19272 O  O     . THR A 1 3969 ? 122.187 199.955 146.999 1.00 73.84  ? 3969 THR A O     1 
ATOM   19273 C  CB    . THR A 1 3969 ? 123.551 201.831 145.590 1.00 76.14  ? 3969 THR A CB    1 
ATOM   19274 O  OG1   . THR A 1 3969 ? 123.746 200.734 144.688 1.00 74.00  ? 3969 THR A OG1   1 
ATOM   19275 C  CG2   . THR A 1 3969 ? 124.279 203.060 145.059 1.00 70.87  ? 3969 THR A CG2   1 
ATOM   19276 N  N     . VAL A 1 3970 ? 123.762 199.605 148.556 1.00 67.25  ? 3970 VAL A N     1 
ATOM   19277 C  CA    . VAL A 1 3970 ? 123.040 198.446 149.093 1.00 64.54  ? 3970 VAL A CA    1 
ATOM   19278 C  C     . VAL A 1 3970 ? 121.738 198.918 149.727 1.00 71.20  ? 3970 VAL A C     1 
ATOM   19279 O  O     . VAL A 1 3970 ? 121.761 199.807 150.602 1.00 75.43  ? 3970 VAL A O     1 
ATOM   19280 C  CB    . VAL A 1 3970 ? 123.904 197.690 150.114 1.00 60.86  ? 3970 VAL A CB    1 
ATOM   19281 C  CG1   . VAL A 1 3970 ? 123.244 196.374 150.489 1.00 59.47  ? 3970 VAL A CG1   1 
ATOM   19282 C  CG2   . VAL A 1 3970 ? 125.292 197.450 149.561 1.00 60.24  ? 3970 VAL A CG2   1 
ATOM   19283 N  N     . PRO A 1 3971 ? 120.593 198.379 149.337 1.00 71.98  ? 3971 PRO A N     1 
ATOM   19284 C  CA    . PRO A 1 3971 ? 119.319 198.814 149.911 1.00 74.71  ? 3971 PRO A CA    1 
ATOM   19285 C  C     . PRO A 1 3971 ? 119.062 198.142 151.258 1.00 84.42  ? 3971 PRO A C     1 
ATOM   19286 O  O     . PRO A 1 3971 ? 119.830 197.304 151.726 1.00 82.92  ? 3971 PRO A O     1 
ATOM   19287 C  CB    . PRO A 1 3971 ? 118.304 198.387 148.850 1.00 75.54  ? 3971 PRO A CB    1 
ATOM   19288 C  CG    . PRO A 1 3971 ? 118.921 197.194 148.216 1.00 74.89  ? 3971 PRO A CG    1 
ATOM   19289 C  CD    . PRO A 1 3971 ? 120.410 197.394 148.258 1.00 73.25  ? 3971 PRO A CD    1 
ATOM   19290 N  N     . TYR A 1 3972 ? 117.950 198.533 151.876 1.00 89.12  ? 3972 TYR A N     1 
ATOM   19291 C  CA    . TYR A 1 3972 ? 117.598 198.131 153.234 1.00 88.70  ? 3972 TYR A CA    1 
ATOM   19292 C  C     . TYR A 1 3972 ? 116.742 196.870 153.176 1.00 85.95  ? 3972 TYR A C     1 
ATOM   19293 O  O     . TYR A 1 3972 ? 115.581 196.919 152.758 1.00 89.00  ? 3972 TYR A O     1 
ATOM   19294 C  CB    . TYR A 1 3972 ? 116.864 199.271 153.935 1.00 92.76  ? 3972 TYR A CB    1 
ATOM   19295 C  CG    . TYR A 1 3972 ? 116.437 198.982 155.353 1.00 98.21  ? 3972 TYR A CG    1 
ATOM   19296 C  CD1   . TYR A 1 3972 ? 117.355 198.988 156.393 1.00 93.60  ? 3972 TYR A CD1   1 
ATOM   19297 C  CD2   . TYR A 1 3972 ? 115.107 198.721 155.653 1.00 103.28 ? 3972 TYR A CD2   1 
ATOM   19298 C  CE1   . TYR A 1 3972 ? 116.960 198.731 157.691 1.00 98.76  ? 3972 TYR A CE1   1 
ATOM   19299 C  CE2   . TYR A 1 3972 ? 114.704 198.463 156.944 1.00 103.03 ? 3972 TYR A CE2   1 
ATOM   19300 C  CZ    . TYR A 1 3972 ? 115.633 198.471 157.960 1.00 104.18 ? 3972 TYR A CZ    1 
ATOM   19301 O  OH    . TYR A 1 3972 ? 115.229 198.212 159.247 1.00 106.36 ? 3972 TYR A OH    1 
ATOM   19302 N  N     . LEU A 1 3973 ? 117.317 195.738 153.596 1.00 82.21  ? 3973 LEU A N     1 
ATOM   19303 C  CA    . LEU A 1 3973 ? 116.626 194.454 153.553 1.00 88.22  ? 3973 LEU A CA    1 
ATOM   19304 C  C     . LEU A 1 3973 ? 116.696 193.682 154.866 1.00 92.94  ? 3973 LEU A C     1 
ATOM   19305 O  O     . LEU A 1 3973 ? 116.484 192.464 154.862 1.00 96.73  ? 3973 LEU A O     1 
ATOM   19306 C  CB    . LEU A 1 3973 ? 117.175 193.572 152.422 1.00 81.35  ? 3973 LEU A CB    1 
ATOM   19307 C  CG    . LEU A 1 3973 ? 116.707 193.820 150.986 1.00 85.44  ? 3973 LEU A CG    1 
ATOM   19308 C  CD1   . LEU A 1 3973 ? 117.287 195.090 150.418 1.00 84.18  ? 3973 LEU A CD1   1 
ATOM   19309 C  CD2   . LEU A 1 3973 ? 117.072 192.643 150.103 1.00 87.64  ? 3973 LEU A CD2   1 
ATOM   19310 N  N     . TRP A 1 3974 ? 116.985 194.343 155.983 1.00 92.78  ? 3974 TRP A N     1 
ATOM   19311 C  CA    . TRP A 1 3974 ? 117.037 193.685 157.279 1.00 96.40  ? 3974 TRP A CA    1 
ATOM   19312 C  C     . TRP A 1 3974 ? 116.042 194.333 158.233 1.00 105.13 ? 3974 TRP A C     1 
ATOM   19313 O  O     . TRP A 1 3974 ? 115.817 195.545 158.191 1.00 104.50 ? 3974 TRP A O     1 
ATOM   19314 C  CB    . TRP A 1 3974 ? 118.451 193.733 157.878 1.00 91.01  ? 3974 TRP A CB    1 
ATOM   19315 C  CG    . TRP A 1 3974 ? 119.022 195.110 158.008 1.00 88.35  ? 3974 TRP A CG    1 
ATOM   19316 C  CD1   . TRP A 1 3974 ? 118.853 195.972 159.051 1.00 92.49  ? 3974 TRP A CD1   1 
ATOM   19317 C  CD2   . TRP A 1 3974 ? 119.866 195.782 157.066 1.00 85.88  ? 3974 TRP A CD2   1 
ATOM   19318 N  NE1   . TRP A 1 3974 ? 119.534 197.140 158.815 1.00 89.17  ? 3974 TRP A NE1   1 
ATOM   19319 C  CE2   . TRP A 1 3974 ? 120.164 197.049 157.602 1.00 86.95  ? 3974 TRP A CE2   1 
ATOM   19320 C  CE3   . TRP A 1 3974 ? 120.396 195.436 155.820 1.00 81.93  ? 3974 TRP A CE3   1 
ATOM   19321 C  CZ2   . TRP A 1 3974 ? 120.967 197.970 156.936 1.00 85.60  ? 3974 TRP A CZ2   1 
ATOM   19322 C  CZ3   . TRP A 1 3974 ? 121.193 196.352 155.161 1.00 76.33  ? 3974 TRP A CZ3   1 
ATOM   19323 C  CH2   . TRP A 1 3974 ? 121.470 197.604 155.719 1.00 77.53  ? 3974 TRP A CH2   1 
ATOM   19324 N  N     . SER A 1 3975 ? 115.443 193.510 159.089 1.00 107.71 ? 3975 SER A N     1 
ATOM   19325 C  CA    . SER A 1 3975 ? 114.470 193.962 160.074 1.00 108.38 ? 3975 SER A CA    1 
ATOM   19326 C  C     . SER A 1 3975 ? 115.106 193.931 161.456 1.00 113.96 ? 3975 SER A C     1 
ATOM   19327 O  O     . SER A 1 3975 ? 115.757 192.948 161.823 1.00 111.41 ? 3975 SER A O     1 
ATOM   19328 C  CB    . SER A 1 3975 ? 113.214 193.089 160.050 1.00 111.24 ? 3975 SER A CB    1 
ATOM   19329 O  OG    . SER A 1 3975 ? 113.386 191.925 160.839 1.00 113.51 ? 3975 SER A OG    1 
ATOM   19330 N  N     . GLU A 1 3976 ? 114.916 195.007 162.218 1.00 119.66 ? 3976 GLU A N     1 
ATOM   19331 C  CA    . GLU A 1 3976 ? 115.541 195.147 163.523 1.00 120.43 ? 3976 GLU A CA    1 
ATOM   19332 C  C     . GLU A 1 3976 ? 114.640 195.967 164.436 1.00 124.21 ? 3976 GLU A C     1 
ATOM   19333 O  O     . GLU A 1 3976 ? 113.805 196.752 163.980 1.00 120.93 ? 3976 GLU A O     1 
ATOM   19334 C  CB    . GLU A 1 3976 ? 116.927 195.797 163.404 1.00 117.98 ? 3976 GLU A CB    1 
ATOM   19335 C  CG    . GLU A 1 3976 ? 116.903 197.312 163.276 1.00 121.35 ? 3976 GLU A CG    1 
ATOM   19336 C  CD    . GLU A 1 3976 ? 116.135 197.803 162.065 1.00 118.25 ? 3976 GLU A CD    1 
ATOM   19337 O  OE1   . GLU A 1 3976 ? 116.048 197.059 161.065 1.00 114.04 ? 3976 GLU A OE1   1 
ATOM   19338 O  OE2   . GLU A 1 3976 ? 115.612 198.936 162.115 1.00 119.93 ? 3976 GLU A OE2   1 
ATOM   19339 N  N     . GLU A 1 3977 ? 114.816 195.766 165.745 1.00 127.09 ? 3977 GLU A N     1 
ATOM   19340 C  CA    . GLU A 1 3977 ? 113.993 196.473 166.722 1.00 128.48 ? 3977 GLU A CA    1 
ATOM   19341 C  C     . GLU A 1 3977 ? 114.391 197.941 166.827 1.00 127.66 ? 3977 GLU A C     1 
ATOM   19342 O  O     . GLU A 1 3977 ? 113.530 198.828 166.854 1.00 127.01 ? 3977 GLU A O     1 
ATOM   19343 C  CB    . GLU A 1 3977 ? 114.094 195.787 168.085 1.00 132.27 ? 3977 GLU A CB    1 
ATOM   19344 C  CG    . GLU A 1 3977 ? 113.269 196.453 169.177 1.00 137.23 ? 3977 GLU A CG    1 
ATOM   19345 C  CD    . GLU A 1 3977 ? 113.229 195.642 170.459 1.00 139.31 ? 3977 GLU A CD    1 
ATOM   19346 O  OE1   . GLU A 1 3977 ? 112.743 194.492 170.421 1.00 141.01 ? 3977 GLU A OE1   1 
ATOM   19347 O  OE2   . GLU A 1 3977 ? 113.682 196.155 171.504 1.00 138.41 ? 3977 GLU A OE2   1 
ATOM   19348 N  N     . THR A 1 3978 ? 115.693 198.218 166.886 1.00 127.91 ? 3978 THR A N     1 
ATOM   19349 C  CA    . THR A 1 3978 ? 116.197 199.577 167.010 1.00 129.34 ? 3978 THR A CA    1 
ATOM   19350 C  C     . THR A 1 3978 ? 117.233 199.839 165.925 1.00 129.34 ? 3978 THR A C     1 
ATOM   19351 O  O     . THR A 1 3978 ? 118.012 198.941 165.584 1.00 127.88 ? 3978 THR A O     1 
ATOM   19352 C  CB    . THR A 1 3978 ? 116.810 199.813 168.404 1.00 126.39 ? 3978 THR A CB    1 
ATOM   19353 O  OG1   . THR A 1 3978 ? 117.304 201.155 168.499 1.00 123.25 ? 3978 THR A OG1   1 
ATOM   19354 C  CG2   . THR A 1 3978 ? 117.939 198.828 168.683 1.00 123.06 ? 3978 THR A CG2   1 
ATOM   19355 N  N     . PRO A 1 3979 ? 117.268 201.052 165.369 1.00 128.04 ? 3979 PRO A N     1 
ATOM   19356 C  CA    . PRO A 1 3979 ? 118.136 201.308 164.211 1.00 123.30 ? 3979 PRO A CA    1 
ATOM   19357 C  C     . PRO A 1 3979 ? 119.593 200.988 164.505 1.00 120.37 ? 3979 PRO A C     1 
ATOM   19358 O  O     . PRO A 1 3979 ? 120.103 201.254 165.595 1.00 117.49 ? 3979 PRO A O     1 
ATOM   19359 C  CB    . PRO A 1 3979 ? 117.932 202.803 163.942 1.00 123.71 ? 3979 PRO A CB    1 
ATOM   19360 C  CG    . PRO A 1 3979 ? 116.571 203.091 164.470 1.00 123.59 ? 3979 PRO A CG    1 
ATOM   19361 C  CD    . PRO A 1 3979 ? 116.394 202.200 165.669 1.00 125.48 ? 3979 PRO A CD    1 
ATOM   19362 N  N     . ALA A 1 3980 ? 120.259 200.406 163.512 1.00 117.98 ? 3980 ALA A N     1 
ATOM   19363 C  CA    . ALA A 1 3980 ? 121.618 199.920 163.683 1.00 109.50 ? 3980 ALA A CA    1 
ATOM   19364 C  C     . ALA A 1 3980 ? 122.629 201.055 163.587 1.00 102.05 ? 3980 ALA A C     1 
ATOM   19365 O  O     . ALA A 1 3980 ? 122.411 202.061 162.906 1.00 95.81  ? 3980 ALA A O     1 
ATOM   19366 C  CB    . ALA A 1 3980 ? 121.940 198.851 162.639 1.00 96.58  ? 3980 ALA A CB    1 
ATOM   19367 N  N     . THR A 1 3981 ? 123.746 200.877 164.284 1.00 99.30  ? 3981 THR A N     1 
ATOM   19368 C  CA    . THR A 1 3981 ? 124.856 201.805 164.200 1.00 92.62  ? 3981 THR A CA    1 
ATOM   19369 C  C     . THR A 1 3981 ? 125.537 201.670 162.839 1.00 85.01  ? 3981 THR A C     1 
ATOM   19370 O  O     . THR A 1 3981 ? 125.328 200.684 162.130 1.00 82.46  ? 3981 THR A O     1 
ATOM   19371 C  CB    . THR A 1 3981 ? 125.847 201.538 165.330 1.00 92.33  ? 3981 THR A CB    1 
ATOM   19372 O  OG1   . THR A 1 3981 ? 126.687 200.431 164.982 1.00 89.43  ? 3981 THR A OG1   1 
ATOM   19373 C  CG2   . THR A 1 3981 ? 125.106 201.218 166.619 1.00 95.15  ? 3981 THR A CG2   1 
ATOM   19374 N  N     . PRO A 1 3982 ? 126.341 202.664 162.440 1.00 79.80  ? 3982 PRO A N     1 
ATOM   19375 C  CA    . PRO A 1 3982 ? 127.002 202.578 161.126 1.00 73.28  ? 3982 PRO A CA    1 
ATOM   19376 C  C     . PRO A 1 3982 ? 127.786 201.294 160.909 1.00 70.86  ? 3982 PRO A C     1 
ATOM   19377 O  O     . PRO A 1 3982 ? 127.788 200.765 159.792 1.00 73.69  ? 3982 PRO A O     1 
ATOM   19378 C  CB    . PRO A 1 3982 ? 127.915 203.809 161.127 1.00 71.20  ? 3982 PRO A CB    1 
ATOM   19379 C  CG    . PRO A 1 3982 ? 127.189 204.793 161.962 1.00 72.76  ? 3982 PRO A CG    1 
ATOM   19380 C  CD    . PRO A 1 3982 ? 126.496 204.002 163.040 1.00 79.95  ? 3982 PRO A CD    1 
ATOM   19381 N  N     . ILE A 1 3983 ? 128.447 200.769 161.943 1.00 68.92  ? 3983 ILE A N     1 
ATOM   19382 C  CA    . ILE A 1 3983 ? 129.135 199.492 161.780 1.00 67.67  ? 3983 ILE A CA    1 
ATOM   19383 C  C     . ILE A 1 3983 ? 128.131 198.350 161.651 1.00 70.98  ? 3983 ILE A C     1 
ATOM   19384 O  O     . ILE A 1 3983 ? 128.394 197.361 160.955 1.00 73.76  ? 3983 ILE A O     1 
ATOM   19385 C  CB    . ILE A 1 3983 ? 130.136 199.265 162.931 1.00 66.81  ? 3983 ILE A CB    1 
ATOM   19386 C  CG1   . ILE A 1 3983 ? 131.243 198.313 162.484 1.00 65.07  ? 3983 ILE A CG1   1 
ATOM   19387 C  CG2   . ILE A 1 3983 ? 129.448 198.726 164.171 1.00 73.62  ? 3983 ILE A CG2   1 
ATOM   19388 C  CD1   . ILE A 1 3983 ? 132.020 198.812 161.291 1.00 65.18  ? 3983 ILE A CD1   1 
ATOM   19389 N  N     . GLY A 1 3984 ? 126.967 198.464 162.294 1.00 68.91  ? 3984 GLY A N     1 
ATOM   19390 C  CA    . GLY A 1 3984 ? 125.936 197.455 162.114 1.00 69.77  ? 3984 GLY A CA    1 
ATOM   19391 C  C     . GLY A 1 3984 ? 125.375 197.445 160.706 1.00 71.65  ? 3984 GLY A C     1 
ATOM   19392 O  O     . GLY A 1 3984 ? 125.180 196.382 160.109 1.00 73.29  ? 3984 GLY A O     1 
ATOM   19393 N  N     . GLN A 1 3985 ? 125.113 198.629 160.151 1.00 71.96  ? 3985 GLN A N     1 
ATOM   19394 C  CA    . GLN A 1 3985 ? 124.702 198.704 158.755 1.00 68.58  ? 3985 GLN A CA    1 
ATOM   19395 C  C     . GLN A 1 3985 ? 125.802 198.189 157.839 1.00 63.08  ? 3985 GLN A C     1 
ATOM   19396 O  O     . GLN A 1 3985 ? 125.522 197.532 156.833 1.00 65.48  ? 3985 GLN A O     1 
ATOM   19397 C  CB    . GLN A 1 3985 ? 124.324 200.139 158.391 1.00 69.84  ? 3985 GLN A CB    1 
ATOM   19398 C  CG    . GLN A 1 3985 ? 123.115 200.666 159.140 1.00 79.67  ? 3985 GLN A CG    1 
ATOM   19399 C  CD    . GLN A 1 3985 ? 122.895 202.147 158.916 1.00 91.21  ? 3985 GLN A CD    1 
ATOM   19400 O  OE1   . GLN A 1 3985 ? 123.674 202.804 158.227 1.00 88.46  ? 3985 GLN A OE1   1 
ATOM   19401 N  NE2   . GLN A 1 3985 ? 121.827 202.681 159.497 1.00 96.03  ? 3985 GLN A NE2   1 
ATOM   19402 N  N     . ALA A 1 3986 ? 127.063 198.470 158.177 1.00 61.74  ? 3986 ALA A N     1 
ATOM   19403 C  CA    . ALA A 1 3986 ? 128.172 197.987 157.362 1.00 54.06  ? 3986 ALA A CA    1 
ATOM   19404 C  C     . ALA A 1 3986 ? 128.232 196.466 157.346 1.00 52.98  ? 3986 ALA A C     1 
ATOM   19405 O  O     . ALA A 1 3986 ? 128.420 195.860 156.287 1.00 61.77  ? 3986 ALA A O     1 
ATOM   19406 C  CB    . ALA A 1 3986 ? 129.490 198.571 157.868 1.00 55.16  ? 3986 ALA A CB    1 
ATOM   19407 N  N     . ILE A 1 3987 ? 128.064 195.826 158.505 1.00 54.65  ? 3987 ILE A N     1 
ATOM   19408 C  CA    . ILE A 1 3987 ? 128.132 194.367 158.543 1.00 59.30  ? 3987 ILE A CA    1 
ATOM   19409 C  C     . ILE A 1 3987 ? 126.903 193.750 157.879 1.00 62.97  ? 3987 ILE A C     1 
ATOM   19410 O  O     . ILE A 1 3987 ? 126.998 192.709 157.215 1.00 67.11  ? 3987 ILE A O     1 
ATOM   19411 C  CB    . ILE A 1 3987 ? 128.331 193.861 159.985 1.00 57.00  ? 3987 ILE A CB    1 
ATOM   19412 C  CG1   . ILE A 1 3987 ? 128.589 192.355 159.986 1.00 58.93  ? 3987 ILE A CG1   1 
ATOM   19413 C  CG2   . ILE A 1 3987 ? 127.143 194.177 160.864 1.00 62.56  ? 3987 ILE A CG2   1 
ATOM   19414 C  CD1   . ILE A 1 3987 ? 129.008 191.825 161.329 1.00 70.04  ? 3987 ILE A CD1   1 
ATOM   19415 N  N     . HIS A 1 3988 ? 125.734 194.379 158.029 1.00 60.61  ? 3988 HIS A N     1 
ATOM   19416 C  CA    . HIS A 1 3988 ? 124.546 193.870 157.349 1.00 59.93  ? 3988 HIS A CA    1 
ATOM   19417 C  C     . HIS A 1 3988 ? 124.688 193.975 155.835 1.00 58.62  ? 3988 HIS A C     1 
ATOM   19418 O  O     . HIS A 1 3988 ? 124.322 193.047 155.104 1.00 62.09  ? 3988 HIS A O     1 
ATOM   19419 C  CB    . HIS A 1 3988 ? 123.304 194.614 157.834 1.00 70.14  ? 3988 HIS A CB    1 
ATOM   19420 C  CG    . HIS A 1 3988 ? 122.776 194.110 159.141 1.00 75.52  ? 3988 HIS A CG    1 
ATOM   19421 N  ND1   . HIS A 1 3988 ? 121.740 194.722 159.812 1.00 82.21  ? 3988 HIS A ND1   1 
ATOM   19422 C  CD2   . HIS A 1 3988 ? 123.139 193.048 159.897 1.00 72.07  ? 3988 HIS A CD2   1 
ATOM   19423 C  CE1   . HIS A 1 3988 ? 121.490 194.060 160.927 1.00 87.18  ? 3988 HIS A CE1   1 
ATOM   19424 N  NE2   . HIS A 1 3988 ? 122.324 193.040 161.002 1.00 79.14  ? 3988 HIS A NE2   1 
ATOM   19425 N  N     . ARG A 1 3989 ? 125.228 195.092 155.345 1.00 58.26  ? 3989 ARG A N     1 
ATOM   19426 C  CA    . ARG A 1 3989 ? 125.481 195.226 153.916 1.00 52.38  ? 3989 ARG A CA    1 
ATOM   19427 C  C     . ARG A 1 3989 ? 126.565 194.267 153.448 1.00 48.86  ? 3989 ARG A C     1 
ATOM   19428 O  O     . ARG A 1 3989 ? 126.516 193.794 152.311 1.00 54.62  ? 3989 ARG A O     1 
ATOM   19429 C  CB    . ARG A 1 3989 ? 125.864 196.664 153.579 1.00 45.47  ? 3989 ARG A CB    1 
ATOM   19430 C  CG    . ARG A 1 3989 ? 124.743 197.661 153.786 1.00 52.11  ? 3989 ARG A CG    1 
ATOM   19431 C  CD    . ARG A 1 3989 ? 125.197 199.070 153.470 1.00 53.92  ? 3989 ARG A CD    1 
ATOM   19432 N  NE    . ARG A 1 3989 ? 124.099 200.024 153.564 1.00 63.33  ? 3989 ARG A NE    1 
ATOM   19433 C  CZ    . ARG A 1 3989 ? 124.223 201.328 153.364 1.00 69.83  ? 3989 ARG A CZ    1 
ATOM   19434 N  NH1   . ARG A 1 3989 ? 125.388 201.872 153.054 1.00 78.10  ? 3989 ARG A NH1   1 
ATOM   19435 N  NH2   . ARG A 1 3989 ? 123.151 202.106 153.477 1.00 66.85  ? 3989 ARG A NH2   1 
ATOM   19436 N  N     . LEU A 1 3990 ? 127.548 193.973 154.300 1.00 48.07  ? 3990 LEU A N     1 
ATOM   19437 C  CA    . LEU A 1 3990 ? 128.550 192.973 153.953 1.00 49.02  ? 3990 LEU A CA    1 
ATOM   19438 C  C     . LEU A 1 3990 ? 127.909 191.604 153.768 1.00 52.87  ? 3990 LEU A C     1 
ATOM   19439 O  O     . LEU A 1 3990 ? 128.210 190.894 152.801 1.00 56.96  ? 3990 LEU A O     1 
ATOM   19440 C  CB    . LEU A 1 3990 ? 129.630 192.930 155.034 1.00 52.11  ? 3990 LEU A CB    1 
ATOM   19441 C  CG    . LEU A 1 3990 ? 130.872 192.073 154.796 1.00 55.41  ? 3990 LEU A CG    1 
ATOM   19442 C  CD1   . LEU A 1 3990 ? 131.820 192.767 153.841 1.00 51.42  ? 3990 LEU A CD1   1 
ATOM   19443 C  CD2   . LEU A 1 3990 ? 131.565 191.782 156.111 1.00 54.87  ? 3990 LEU A CD2   1 
ATOM   19444 N  N     . LEU A 1 3991 ? 127.006 191.228 154.675 1.00 55.84  ? 3991 LEU A N     1 
ATOM   19445 C  CA    . LEU A 1 3991 ? 126.283 189.966 154.526 1.00 53.65  ? 3991 LEU A CA    1 
ATOM   19446 C  C     . LEU A 1 3991 ? 125.422 189.965 153.268 1.00 54.75  ? 3991 LEU A C     1 
ATOM   19447 O  O     . LEU A 1 3991 ? 125.378 188.968 152.534 1.00 55.54  ? 3991 LEU A O     1 
ATOM   19448 C  CB    . LEU A 1 3991 ? 125.420 189.707 155.760 1.00 55.38  ? 3991 LEU A CB    1 
ATOM   19449 C  CG    . LEU A 1 3991 ? 126.147 189.431 157.074 1.00 53.15  ? 3991 LEU A CG    1 
ATOM   19450 C  CD1   . LEU A 1 3991 ? 125.152 189.303 158.206 1.00 63.62  ? 3991 LEU A CD1   1 
ATOM   19451 C  CD2   . LEU A 1 3991 ? 126.972 188.171 156.954 1.00 55.03  ? 3991 LEU A CD2   1 
ATOM   19452 N  N     . LEU A 1 3992 ? 124.727 191.075 153.005 1.00 52.54  ? 3992 LEU A N     1 
ATOM   19453 C  CA    . LEU A 1 3992 ? 123.878 191.159 151.820 1.00 51.78  ? 3992 LEU A CA    1 
ATOM   19454 C  C     . LEU A 1 3992 ? 124.695 191.035 150.541 1.00 50.49  ? 3992 LEU A C     1 
ATOM   19455 O  O     . LEU A 1 3992 ? 124.280 190.356 149.597 1.00 52.19  ? 3992 LEU A O     1 
ATOM   19456 C  CB    . LEU A 1 3992 ? 123.096 192.471 151.825 1.00 51.18  ? 3992 LEU A CB    1 
ATOM   19457 C  CG    . LEU A 1 3992 ? 121.893 192.543 152.762 1.00 54.07  ? 3992 LEU A CG    1 
ATOM   19458 C  CD1   . LEU A 1 3992 ? 121.143 193.845 152.556 1.00 62.50  ? 3992 LEU A CD1   1 
ATOM   19459 C  CD2   . LEU A 1 3992 ? 120.980 191.353 152.534 1.00 57.65  ? 3992 LEU A CD2   1 
ATOM   19460 N  N     . ILE A 1 3993 ? 125.850 191.698 150.486 1.00 50.38  ? 3993 ILE A N     1 
ATOM   19461 C  CA    . ILE A 1 3993 ? 126.714 191.605 149.315 1.00 44.92  ? 3993 ILE A CA    1 
ATOM   19462 C  C     . ILE A 1 3993 ? 127.250 190.190 149.159 1.00 47.84  ? 3993 ILE A C     1 
ATOM   19463 O  O     . ILE A 1 3993 ? 127.290 189.648 148.049 1.00 53.58  ? 3993 ILE A O     1 
ATOM   19464 C  CB    . ILE A 1 3993 ? 127.848 192.640 149.410 1.00 44.22  ? 3993 ILE A CB    1 
ATOM   19465 C  CG1   . ILE A 1 3993 ? 127.322 194.033 149.065 1.00 50.61  ? 3993 ILE A CG1   1 
ATOM   19466 C  CG2   . ILE A 1 3993 ? 128.993 192.268 148.493 1.00 45.18  ? 3993 ILE A CG2   1 
ATOM   19467 C  CD1   . ILE A 1 3993 ? 126.978 194.206 147.609 1.00 56.77  ? 3993 ILE A CD1   1 
ATOM   19468 N  N     . GLN A 1 3994 ? 127.661 189.562 150.262 1.00 49.10  ? 3994 GLN A N     1 
ATOM   19469 C  CA    . GLN A 1 3994 ? 128.153 188.190 150.186 1.00 48.98  ? 3994 GLN A CA    1 
ATOM   19470 C  C     . GLN A 1 3994 ? 127.080 187.248 149.656 1.00 52.85  ? 3994 GLN A C     1 
ATOM   19471 O  O     . GLN A 1 3994 ? 127.380 186.314 148.904 1.00 51.92  ? 3994 GLN A O     1 
ATOM   19472 C  CB    . GLN A 1 3994 ? 128.637 187.732 151.559 1.00 49.56  ? 3994 GLN A CB    1 
ATOM   19473 C  CG    . GLN A 1 3994 ? 129.340 186.392 151.551 1.00 53.56  ? 3994 GLN A CG    1 
ATOM   19474 C  CD    . GLN A 1 3994 ? 129.292 185.711 152.899 1.00 60.29  ? 3994 GLN A CD    1 
ATOM   19475 O  OE1   . GLN A 1 3994 ? 128.638 186.191 153.823 1.00 65.88  ? 3994 GLN A OE1   1 
ATOM   19476 N  NE2   . GLN A 1 3994 ? 129.977 184.583 153.018 1.00 65.09  ? 3994 GLN A NE2   1 
ATOM   19477 N  N     . ALA A 1 3995 ? 125.822 187.472 150.042 1.00 57.52  ? 3995 ALA A N     1 
ATOM   19478 C  CA    . ALA A 1 3995 ? 124.740 186.616 149.565 1.00 57.58  ? 3995 ALA A CA    1 
ATOM   19479 C  C     . ALA A 1 3995 ? 124.380 186.900 148.109 1.00 54.61  ? 3995 ALA A C     1 
ATOM   19480 O  O     . ALA A 1 3995 ? 124.153 185.968 147.332 1.00 56.95  ? 3995 ALA A O     1 
ATOM   19481 C  CB    . ALA A 1 3995 ? 123.509 186.783 150.455 1.00 52.82  ? 3995 ALA A CB    1 
ATOM   19482 N  N     . PHE A 1 3996 ? 124.328 188.175 147.724 1.00 53.20  ? 3996 PHE A N     1 
ATOM   19483 C  CA    . PHE A 1 3996 ? 123.838 188.595 146.414 1.00 50.07  ? 3996 PHE A CA    1 
ATOM   19484 C  C     . PHE A 1 3996 ? 124.952 188.694 145.378 1.00 52.24  ? 3996 PHE A C     1 
ATOM   19485 O  O     . PHE A 1 3996 ? 124.901 188.031 144.338 1.00 60.26  ? 3996 PHE A O     1 
ATOM   19486 C  CB    . PHE A 1 3996 ? 123.128 189.948 146.541 1.00 52.67  ? 3996 PHE A CB    1 
ATOM   19487 C  CG    . PHE A 1 3996 ? 121.841 189.893 147.309 1.00 60.49  ? 3996 PHE A CG    1 
ATOM   19488 C  CD1   . PHE A 1 3996 ? 121.090 188.736 147.350 1.00 58.54  ? 3996 PHE A CD1   1 
ATOM   19489 C  CD2   . PHE A 1 3996 ? 121.397 190.997 148.015 1.00 68.83  ? 3996 PHE A CD2   1 
ATOM   19490 C  CE1   . PHE A 1 3996 ? 119.910 188.692 148.061 1.00 62.99  ? 3996 PHE A CE1   1 
ATOM   19491 C  CE2   . PHE A 1 3996 ? 120.220 190.955 148.729 1.00 72.79  ? 3996 PHE A CE2   1 
ATOM   19492 C  CZ    . PHE A 1 3996 ? 119.476 189.799 148.754 1.00 72.01  ? 3996 PHE A CZ    1 
ATOM   19493 N  N     . ARG A 1 3997 ? 125.965 189.519 145.648 1.00 50.90  ? 3997 ARG A N     1 
ATOM   19494 C  CA    . ARG A 1 3997 ? 127.028 189.843 144.698 1.00 44.90  ? 3997 ARG A CA    1 
ATOM   19495 C  C     . ARG A 1 3997 ? 128.371 189.547 145.351 1.00 46.77  ? 3997 ARG A C     1 
ATOM   19496 O  O     . ARG A 1 3997 ? 129.066 190.467 145.806 1.00 53.88  ? 3997 ARG A O     1 
ATOM   19497 C  CB    . ARG A 1 3997 ? 126.951 191.304 144.263 1.00 45.77  ? 3997 ARG A CB    1 
ATOM   19498 C  CG    . ARG A 1 3997 ? 125.731 191.655 143.438 1.00 49.83  ? 3997 ARG A CG    1 
ATOM   19499 C  CD    . ARG A 1 3997 ? 125.855 191.085 142.040 1.00 56.44  ? 3997 ARG A CD    1 
ATOM   19500 N  NE    . ARG A 1 3997 ? 126.956 191.702 141.310 1.00 59.25  ? 3997 ARG A NE    1 
ATOM   19501 C  CZ    . ARG A 1 3997 ? 126.929 192.928 140.807 1.00 64.12  ? 3997 ARG A CZ    1 
ATOM   19502 N  NH1   . ARG A 1 3997 ? 125.853 193.691 140.902 1.00 64.94  ? 3997 ARG A NH1   1 
ATOM   19503 N  NH2   . ARG A 1 3997 ? 128.007 193.399 140.187 1.00 60.82  ? 3997 ARG A NH2   1 
ATOM   19504 N  N     . PRO A 1 3998 ? 128.768 188.275 145.423 1.00 43.02  ? 3998 PRO A N     1 
ATOM   19505 C  CA    . PRO A 1 3998 ? 130.045 187.943 146.074 1.00 43.32  ? 3998 PRO A CA    1 
ATOM   19506 C  C     . PRO A 1 3998 ? 131.254 188.576 145.410 1.00 47.48  ? 3998 PRO A C     1 
ATOM   19507 O  O     . PRO A 1 3998 ? 132.258 188.814 146.093 1.00 54.55  ? 3998 PRO A O     1 
ATOM   19508 C  CB    . PRO A 1 3998 ? 130.093 186.412 145.991 1.00 42.67  ? 3998 PRO A CB    1 
ATOM   19509 C  CG    . PRO A 1 3998 ? 129.214 186.071 144.842 1.00 42.40  ? 3998 PRO A CG    1 
ATOM   19510 C  CD    . PRO A 1 3998 ? 128.110 187.085 144.862 1.00 44.59  ? 3998 PRO A CD    1 
ATOM   19511 N  N     . ASP A 1 3999 ? 131.192 188.864 144.107 1.00 43.25  ? 3999 ASP A N     1 
ATOM   19512 C  CA    . ASP A 1 3999 ? 132.334 189.471 143.430 1.00 42.33  ? 3999 ASP A CA    1 
ATOM   19513 C  C     . ASP A 1 3999 ? 132.674 190.832 144.023 1.00 46.62  ? 3999 ASP A C     1 
ATOM   19514 O  O     . ASP A 1 3999 ? 133.843 191.231 144.045 1.00 55.54  ? 3999 ASP A O     1 
ATOM   19515 C  CB    . ASP A 1 3999 ? 132.054 189.592 141.933 1.00 44.44  ? 3999 ASP A CB    1 
ATOM   19516 C  CG    . ASP A 1 3999 ? 130.800 190.385 141.636 1.00 53.54  ? 3999 ASP A CG    1 
ATOM   19517 O  OD1   . ASP A 1 3999 ? 129.712 189.961 142.075 1.00 53.64  ? 3999 ASP A OD1   1 
ATOM   19518 O  OD2   . ASP A 1 3999 ? 130.900 191.432 140.964 1.00 55.66  ? 3999 ASP A OD2   1 
ATOM   19519 N  N     . ARG A 1 4000 ? 131.672 191.554 144.513 1.00 43.04  ? 4000 ARG A N     1 
ATOM   19520 C  CA    . ARG A 1 4000 ? 131.887 192.852 145.136 1.00 42.41  ? 4000 ARG A CA    1 
ATOM   19521 C  C     . ARG A 1 4000 ? 132.277 192.749 146.602 1.00 41.73  ? 4000 ARG A C     1 
ATOM   19522 O  O     . ARG A 1 4000 ? 132.560 193.783 147.220 1.00 45.63  ? 4000 ARG A O     1 
ATOM   19523 C  CB    . ARG A 1 4000 ? 130.634 193.714 144.991 1.00 41.27  ? 4000 ARG A CB    1 
ATOM   19524 C  CG    . ARG A 1 4000 ? 130.177 193.875 143.561 1.00 48.66  ? 4000 ARG A CG    1 
ATOM   19525 C  CD    . ARG A 1 4000 ? 131.297 194.422 142.699 1.00 56.24  ? 4000 ARG A CD    1 
ATOM   19526 N  NE    . ARG A 1 4000 ? 131.772 195.714 143.177 1.00 55.21  ? 4000 ARG A NE    1 
ATOM   19527 C  CZ    . ARG A 1 4000 ? 132.800 196.369 142.658 1.00 56.71  ? 4000 ARG A CZ    1 
ATOM   19528 N  NH1   . ARG A 1 4000 ? 133.491 195.879 141.643 1.00 53.99  ? 4000 ARG A NH1   1 
ATOM   19529 N  NH2   . ARG A 1 4000 ? 133.145 197.547 143.171 1.00 63.18  ? 4000 ARG A NH2   1 
ATOM   19530 N  N     . LEU A 1 4001 ? 132.316 191.533 147.156 1.00 40.05  ? 4001 LEU A N     1 
ATOM   19531 C  CA    . LEU A 1 4001 ? 132.598 191.363 148.577 1.00 39.62  ? 4001 LEU A CA    1 
ATOM   19532 C  C     . LEU A 1 4001 ? 133.861 192.099 148.998 1.00 41.77  ? 4001 LEU A C     1 
ATOM   19533 O  O     . LEU A 1 4001 ? 133.824 192.877 149.959 1.00 51.51  ? 4001 LEU A O     1 
ATOM   19534 C  CB    . LEU A 1 4001 ? 132.715 189.879 148.916 1.00 41.03  ? 4001 LEU A CB    1 
ATOM   19535 C  CG    . LEU A 1 4001 ? 132.890 189.548 150.397 1.00 41.67  ? 4001 LEU A CG    1 
ATOM   19536 C  CD1   . LEU A 1 4001 ? 131.653 189.941 151.178 1.00 45.73  ? 4001 LEU A CD1   1 
ATOM   19537 C  CD2   . LEU A 1 4001 ? 133.190 188.072 150.575 1.00 46.60  ? 4001 LEU A CD2   1 
ATOM   19538 N  N     . LEU A 1 4002 ? 134.966 191.901 148.272 1.00 38.73  ? 4002 LEU A N     1 
ATOM   19539 C  CA    . LEU A 1 4002 ? 136.201 192.608 148.597 1.00 36.28  ? 4002 LEU A CA    1 
ATOM   19540 C  C     . LEU A 1 4002 ? 135.959 194.104 148.712 1.00 35.50  ? 4002 LEU A C     1 
ATOM   19541 O  O     . LEU A 1 4002 ? 136.300 194.716 149.732 1.00 38.67  ? 4002 LEU A O     1 
ATOM   19542 C  CB    . LEU A 1 4002 ? 137.266 192.332 147.538 1.00 33.32  ? 4002 LEU A CB    1 
ATOM   19543 C  CG    . LEU A 1 4002 ? 137.965 190.977 147.538 1.00 34.03  ? 4002 LEU A CG    1 
ATOM   19544 C  CD1   . LEU A 1 4002 ? 139.117 191.012 146.558 1.00 38.01  ? 4002 LEU A CD1   1 
ATOM   19545 C  CD2   . LEU A 1 4002 ? 138.454 190.626 148.928 1.00 36.86  ? 4002 LEU A CD2   1 
ATOM   19546 N  N     . ALA A 1 4003 ? 135.320 194.700 147.702 1.00 33.89  ? 4003 ALA A N     1 
ATOM   19547 C  CA    . ALA A 1 4003 ? 135.026 196.125 147.772 1.00 36.28  ? 4003 ALA A CA    1 
ATOM   19548 C  C     . ALA A 1 4003 ? 134.185 196.438 148.998 1.00 39.81  ? 4003 ALA A C     1 
ATOM   19549 O  O     . ALA A 1 4003 ? 134.523 197.340 149.775 1.00 44.07  ? 4003 ALA A O     1 
ATOM   19550 C  CB    . ALA A 1 4003 ? 134.319 196.581 146.498 1.00 40.08  ? 4003 ALA A CB    1 
ATOM   19551 N  N     . MET A 1 4004 ? 133.128 195.655 149.227 1.00 40.75  ? 4004 MET A N     1 
ATOM   19552 C  CA    . MET A 1 4004 ? 132.321 195.855 150.422 1.00 38.54  ? 4004 MET A CA    1 
ATOM   19553 C  C     . MET A 1 4004 ? 133.168 195.685 151.672 1.00 39.05  ? 4004 MET A C     1 
ATOM   19554 O  O     . MET A 1 4004 ? 133.050 196.471 152.620 1.00 45.76  ? 4004 MET A O     1 
ATOM   19555 C  CB    . MET A 1 4004 ? 131.141 194.886 150.434 1.00 39.49  ? 4004 MET A CB    1 
ATOM   19556 C  CG    . MET A 1 4004 ? 130.096 195.202 151.484 1.00 45.98  ? 4004 MET A CG    1 
ATOM   19557 S  SD    . MET A 1 4004 ? 129.544 196.915 151.425 1.00 66.60  ? 4004 MET A SD    1 
ATOM   19558 C  CE    . MET A 1 4004 ? 129.560 197.337 153.165 1.00 42.08  ? 4004 MET A CE    1 
ATOM   19559 N  N     . ALA A 1 4005 ? 134.061 194.690 151.670 1.00 35.40  ? 4005 ALA A N     1 
ATOM   19560 C  CA    . ALA A 1 4005 ? 134.970 194.522 152.795 1.00 33.24  ? 4005 ALA A CA    1 
ATOM   19561 C  C     . ALA A 1 4005 ? 135.734 195.807 153.063 1.00 36.09  ? 4005 ALA A C     1 
ATOM   19562 O  O     . ALA A 1 4005 ? 135.796 196.269 154.209 1.00 40.63  ? 4005 ALA A O     1 
ATOM   19563 C  CB    . ALA A 1 4005 ? 135.930 193.365 152.530 1.00 34.67  ? 4005 ALA A CB    1 
ATOM   19564 N  N     . HIS A 1 4006 ? 136.269 196.432 152.009 1.00 37.00  ? 4006 HIS A N     1 
ATOM   19565 C  CA    . HIS A 1 4006 ? 136.970 197.696 152.194 1.00 34.39  ? 4006 HIS A CA    1 
ATOM   19566 C  C     . HIS A 1 4006 ? 136.072 198.710 152.882 1.00 37.25  ? 4006 HIS A C     1 
ATOM   19567 O  O     . HIS A 1 4006 ? 136.477 199.340 153.867 1.00 46.24  ? 4006 HIS A O     1 
ATOM   19568 C  CB    . HIS A 1 4006 ? 137.460 198.235 150.851 1.00 33.77  ? 4006 HIS A CB    1 
ATOM   19569 C  CG    . HIS A 1 4006 ? 138.714 197.584 150.360 1.00 42.05  ? 4006 HIS A CG    1 
ATOM   19570 N  ND1   . HIS A 1 4006 ? 138.782 196.245 150.040 1.00 41.61  ? 4006 HIS A ND1   1 
ATOM   19571 C  CD2   . HIS A 1 4006 ? 139.951 198.086 150.139 1.00 47.16  ? 4006 HIS A CD2   1 
ATOM   19572 C  CE1   . HIS A 1 4006 ? 140.005 195.952 149.639 1.00 36.43  ? 4006 HIS A CE1   1 
ATOM   19573 N  NE2   . HIS A 1 4006 ? 140.735 197.051 149.690 1.00 46.22  ? 4006 HIS A NE2   1 
ATOM   19574 N  N     . MET A 1 4007 ? 134.825 198.831 152.418 1.00 37.37  ? 4007 MET A N     1 
ATOM   19575 C  CA    . MET A 1 4007 ? 133.905 199.771 153.043 1.00 38.23  ? 4007 MET A CA    1 
ATOM   19576 C  C     . MET A 1 4007 ? 133.744 199.465 154.522 1.00 38.06  ? 4007 MET A C     1 
ATOM   19577 O  O     . MET A 1 4007 ? 133.771 200.378 155.356 1.00 43.80  ? 4007 MET A O     1 
ATOM   19578 C  CB    . MET A 1 4007 ? 132.551 199.744 152.336 1.00 39.42  ? 4007 MET A CB    1 
ATOM   19579 C  CG    . MET A 1 4007 ? 132.588 200.266 150.913 1.00 44.20  ? 4007 MET A CG    1 
ATOM   19580 S  SD    . MET A 1 4007 ? 130.987 200.140 150.099 1.00 85.62  ? 4007 MET A SD    1 
ATOM   19581 C  CE    . MET A 1 4007 ? 130.061 201.393 150.978 1.00 59.05  ? 4007 MET A CE    1 
ATOM   19582 N  N     . PHE A 1 4008 ? 133.626 198.182 154.871 1.00 35.44  ? 4008 PHE A N     1 
ATOM   19583 C  CA    . PHE A 1 4008 ? 133.526 197.818 156.278 1.00 35.20  ? 4008 PHE A CA    1 
ATOM   19584 C  C     . PHE A 1 4008 ? 134.724 198.352 157.047 1.00 43.09  ? 4008 PHE A C     1 
ATOM   19585 O  O     . PHE A 1 4008 ? 134.571 199.018 158.078 1.00 51.46  ? 4008 PHE A O     1 
ATOM   19586 C  CB    . PHE A 1 4008 ? 133.420 196.302 156.425 1.00 37.01  ? 4008 PHE A CB    1 
ATOM   19587 C  CG    . PHE A 1 4008 ? 133.496 195.827 157.844 1.00 41.40  ? 4008 PHE A CG    1 
ATOM   19588 C  CD1   . PHE A 1 4008 ? 132.431 196.009 158.705 1.00 50.69  ? 4008 PHE A CD1   1 
ATOM   19589 C  CD2   . PHE A 1 4008 ? 134.634 195.208 158.320 1.00 43.89  ? 4008 PHE A CD2   1 
ATOM   19590 C  CE1   . PHE A 1 4008 ? 132.499 195.573 160.012 1.00 53.25  ? 4008 PHE A CE1   1 
ATOM   19591 C  CE2   . PHE A 1 4008 ? 134.709 194.770 159.625 1.00 45.46  ? 4008 PHE A CE2   1 
ATOM   19592 C  CZ    . PHE A 1 4008 ? 133.641 194.956 160.472 1.00 48.84  ? 4008 PHE A CZ    1 
ATOM   19593 N  N     . VAL A 1 4009 ? 135.928 198.121 156.518 1.00 42.02  ? 4009 VAL A N     1 
ATOM   19594 C  CA    . VAL A 1 4009 ? 137.123 198.657 157.154 1.00 35.13  ? 4009 VAL A CA    1 
ATOM   19595 C  C     . VAL A 1 4009 ? 137.049 200.173 157.215 1.00 37.58  ? 4009 VAL A C     1 
ATOM   19596 O  O     . VAL A 1 4009 ? 137.374 200.777 158.244 1.00 44.14  ? 4009 VAL A O     1 
ATOM   19597 C  CB    . VAL A 1 4009 ? 138.382 198.177 156.412 1.00 34.86  ? 4009 VAL A CB    1 
ATOM   19598 C  CG1   . VAL A 1 4009 ? 139.624 198.733 157.068 1.00 40.68  ? 4009 VAL A CG1   1 
ATOM   19599 C  CG2   . VAL A 1 4009 ? 138.428 196.662 156.382 1.00 31.74  ? 4009 VAL A CG2   1 
ATOM   19600 N  N     . SER A 1 4010 ? 136.585 200.810 156.138 1.00 39.09  ? 4010 SER A N     1 
ATOM   19601 C  CA    . SER A 1 4010 ? 136.478 202.263 156.134 1.00 45.20  ? 4010 SER A CA    1 
ATOM   19602 C  C     . SER A 1 4010 ? 135.489 202.745 157.185 1.00 50.45  ? 4010 SER A C     1 
ATOM   19603 O  O     . SER A 1 4010 ? 135.620 203.858 157.707 1.00 58.35  ? 4010 SER A O     1 
ATOM   19604 C  CB    . SER A 1 4010 ? 136.071 202.755 154.746 1.00 49.43  ? 4010 SER A CB    1 
ATOM   19605 O  OG    . SER A 1 4010 ? 137.054 202.426 153.782 1.00 57.63  ? 4010 SER A OG    1 
ATOM   19606 N  N     . THR A 1 4011 ? 134.490 201.922 157.514 1.00 47.24  ? 4011 THR A N     1 
ATOM   19607 C  CA    . THR A 1 4011 ? 133.526 202.335 158.527 1.00 49.77  ? 4011 THR A CA    1 
ATOM   19608 C  C     . THR A 1 4011 ? 134.029 202.044 159.932 1.00 53.41  ? 4011 THR A C     1 
ATOM   19609 O  O     . THR A 1 4011 ? 133.412 202.479 160.911 1.00 63.24  ? 4011 THR A O     1 
ATOM   19610 C  CB    . THR A 1 4011 ? 132.181 201.648 158.297 1.00 53.11  ? 4011 THR A CB    1 
ATOM   19611 O  OG1   . THR A 1 4011 ? 132.359 200.227 158.306 1.00 54.90  ? 4011 THR A OG1   1 
ATOM   19612 C  CG2   . THR A 1 4011 ? 131.582 202.078 156.967 1.00 52.62  ? 4011 THR A CG2   1 
ATOM   19613 N  N     . ASN A 1 4012 ? 135.139 201.319 160.057 1.00 51.40  ? 4012 ASN A N     1 
ATOM   19614 C  CA    . ASN A 1 4012 ? 135.603 200.908 161.375 1.00 48.67  ? 4012 ASN A CA    1 
ATOM   19615 C  C     . ASN A 1 4012 ? 136.951 201.529 161.728 1.00 45.38  ? 4012 ASN A C     1 
ATOM   19616 O  O     . ASN A 1 4012 ? 137.136 202.021 162.845 1.00 47.61  ? 4012 ASN A O     1 
ATOM   19617 C  CB    . ASN A 1 4012 ? 135.678 199.380 161.441 1.00 41.31  ? 4012 ASN A CB    1 
ATOM   19618 C  CG    . ASN A 1 4012 ? 135.661 198.860 162.859 1.00 49.56  ? 4012 ASN A CG    1 
ATOM   19619 O  OD1   . ASN A 1 4012 ? 135.625 199.634 163.814 1.00 61.20  ? 4012 ASN A OD1   1 
ATOM   19620 N  ND2   . ASN A 1 4012 ? 135.672 197.543 163.005 1.00 50.32  ? 4012 ASN A ND2   1 
ATOM   19621 N  N     . LEU A 1 4013 ? 137.898 201.517 160.792 1.00 45.25  ? 4013 LEU A N     1 
ATOM   19622 C  CA    . LEU A 1 4013 ? 139.232 202.055 161.019 1.00 41.77  ? 4013 LEU A CA    1 
ATOM   19623 C  C     . LEU A 1 4013 ? 139.474 203.369 160.286 1.00 48.41  ? 4013 LEU A C     1 
ATOM   19624 O  O     . LEU A 1 4013 ? 140.618 203.830 160.226 1.00 53.26  ? 4013 LEU A O     1 
ATOM   19625 C  CB    . LEU A 1 4013 ? 140.288 201.026 160.613 1.00 39.20  ? 4013 LEU A CB    1 
ATOM   19626 C  CG    . LEU A 1 4013 ? 140.103 199.617 161.174 1.00 37.36  ? 4013 LEU A CG    1 
ATOM   19627 C  CD1   . LEU A 1 4013 ? 140.970 198.625 160.432 1.00 37.75  ? 4013 LEU A CD1   1 
ATOM   19628 C  CD2   . LEU A 1 4013 ? 140.434 199.597 162.649 1.00 38.43  ? 4013 LEU A CD2   1 
ATOM   19629 N  N     . GLY A 1 4014 ? 138.440 203.979 159.735 1.00 52.62  ? 4014 GLY A N     1 
ATOM   19630 C  CA    . GLY A 1 4014 ? 138.603 205.236 159.035 1.00 52.53  ? 4014 GLY A CA    1 
ATOM   19631 C  C     . GLY A 1 4014 ? 138.723 205.048 157.535 1.00 53.91  ? 4014 GLY A C     1 
ATOM   19632 O  O     . GLY A 1 4014 ? 139.130 203.992 157.040 1.00 56.56  ? 4014 GLY A O     1 
ATOM   19633 N  N     . GLU A 1 4015 ? 138.368 206.098 156.793 1.00 54.64  ? 4015 GLU A N     1 
ATOM   19634 C  CA    . GLU A 1 4015 ? 138.379 206.042 155.336 1.00 61.55  ? 4015 GLU A CA    1 
ATOM   19635 C  C     . GLU A 1 4015 ? 139.783 206.007 154.748 1.00 62.43  ? 4015 GLU A C     1 
ATOM   19636 O  O     . GLU A 1 4015 ? 139.926 205.716 153.556 1.00 62.27  ? 4015 GLU A O     1 
ATOM   19637 C  CB    . GLU A 1 4015 ? 137.618 207.239 154.760 1.00 65.10  ? 4015 GLU A CB    1 
ATOM   19638 C  CG    . GLU A 1 4015 ? 136.127 207.244 155.060 1.00 68.28  ? 4015 GLU A CG    1 
ATOM   19639 C  CD    . GLU A 1 4015 ? 135.386 206.111 154.377 1.00 71.68  ? 4015 GLU A CD    1 
ATOM   19640 O  OE1   . GLU A 1 4015 ? 135.802 205.705 153.273 1.00 70.95  ? 4015 GLU A OE1   1 
ATOM   19641 O  OE2   . GLU A 1 4015 ? 134.385 205.627 154.946 1.00 70.94  ? 4015 GLU A OE2   1 
ATOM   19642 N  N     . SER A 1 4016 ? 140.814 206.292 155.541 1.00 60.25  ? 4016 SER A N     1 
ATOM   19643 C  CA    . SER A 1 4016 ? 142.184 206.376 155.052 1.00 60.69  ? 4016 SER A CA    1 
ATOM   19644 C  C     . SER A 1 4016 ? 143.098 205.352 155.719 1.00 59.80  ? 4016 SER A C     1 
ATOM   19645 O  O     . SER A 1 4016 ? 144.288 205.609 155.912 1.00 62.99  ? 4016 SER A O     1 
ATOM   19646 C  CB    . SER A 1 4016 ? 142.730 207.787 155.254 1.00 68.04  ? 4016 SER A CB    1 
ATOM   19647 O  OG    . SER A 1 4016 ? 142.612 208.183 156.609 1.00 66.49  ? 4016 SER A OG    1 
ATOM   19648 N  N     . PHE A 1 4017 ? 142.555 204.191 156.083 1.00 53.46  ? 4017 PHE A N     1 
ATOM   19649 C  CA    . PHE A 1 4017 ? 143.370 203.169 156.730 1.00 49.87  ? 4017 PHE A CA    1 
ATOM   19650 C  C     . PHE A 1 4017 ? 144.351 202.540 155.748 1.00 56.53  ? 4017 PHE A C     1 
ATOM   19651 O  O     . PHE A 1 4017 ? 145.541 202.396 156.050 1.00 61.88  ? 4017 PHE A O     1 
ATOM   19652 C  CB    . PHE A 1 4017 ? 142.472 202.103 157.355 1.00 43.58  ? 4017 PHE A CB    1 
ATOM   19653 C  CG    . PHE A 1 4017 ? 143.182 201.209 158.327 1.00 42.63  ? 4017 PHE A CG    1 
ATOM   19654 C  CD1   . PHE A 1 4017 ? 143.587 201.688 159.558 1.00 42.00  ? 4017 PHE A CD1   1 
ATOM   19655 C  CD2   . PHE A 1 4017 ? 143.442 199.888 158.012 1.00 40.85  ? 4017 PHE A CD2   1 
ATOM   19656 C  CE1   . PHE A 1 4017 ? 144.237 200.869 160.454 1.00 38.97  ? 4017 PHE A CE1   1 
ATOM   19657 C  CE2   . PHE A 1 4017 ? 144.093 199.065 158.904 1.00 36.31  ? 4017 PHE A CE2   1 
ATOM   19658 C  CZ    . PHE A 1 4017 ? 144.488 199.556 160.127 1.00 32.74  ? 4017 PHE A CZ    1 
ATOM   19659 N  N     . MET A 1 4018 ? 143.873 202.163 154.564 1.00 52.12  ? 4018 MET A N     1 
ATOM   19660 C  CA    . MET A 1 4018 ? 144.713 201.535 153.554 1.00 51.35  ? 4018 MET A CA    1 
ATOM   19661 C  C     . MET A 1 4018 ? 145.363 202.536 152.611 1.00 62.26  ? 4018 MET A C     1 
ATOM   19662 O  O     . MET A 1 4018 ? 146.181 202.133 151.781 1.00 68.25  ? 4018 MET A O     1 
ATOM   19663 C  CB    . MET A 1 4018 ? 143.901 200.530 152.729 1.00 53.08  ? 4018 MET A CB    1 
ATOM   19664 C  CG    . MET A 1 4018 ? 143.618 199.205 153.416 1.00 47.17  ? 4018 MET A CG    1 
ATOM   19665 S  SD    . MET A 1 4018 ? 142.376 199.332 154.709 1.00 71.10  ? 4018 MET A SD    1 
ATOM   19666 C  CE    . MET A 1 4018 ? 140.892 199.501 153.724 1.00 54.21  ? 4018 MET A CE    1 
ATOM   19667 N  N     . SER A 1 4019 ? 145.039 203.828 152.731 1.00 67.01  ? 4019 SER A N     1 
ATOM   19668 C  CA    . SER A 1 4019 ? 145.437 204.802 151.717 1.00 73.29  ? 4019 SER A CA    1 
ATOM   19669 C  C     . SER A 1 4019 ? 146.950 204.923 151.587 1.00 72.62  ? 4019 SER A C     1 
ATOM   19670 O  O     . SER A 1 4019 ? 147.446 205.379 150.551 1.00 76.32  ? 4019 SER A O     1 
ATOM   19671 C  CB    . SER A 1 4019 ? 144.825 206.166 152.034 1.00 77.33  ? 4019 SER A CB    1 
ATOM   19672 O  OG    . SER A 1 4019 ? 145.257 206.641 153.296 1.00 74.85  ? 4019 SER A OG    1 
ATOM   19673 N  N     . ILE A 1 4020 ? 147.699 204.535 152.619 1.00 68.84  ? 4020 ILE A N     1 
ATOM   19674 C  CA    . ILE A 1 4020 ? 149.155 204.598 152.541 1.00 75.66  ? 4020 ILE A CA    1 
ATOM   19675 C  C     . ILE A 1 4020 ? 149.686 203.572 151.545 1.00 74.43  ? 4020 ILE A C     1 
ATOM   19676 O  O     . ILE A 1 4020 ? 150.675 203.821 150.844 1.00 78.16  ? 4020 ILE A O     1 
ATOM   19677 C  CB    . ILE A 1 4020 ? 149.777 204.417 153.940 1.00 75.47  ? 4020 ILE A CB    1 
ATOM   19678 C  CG1   . ILE A 1 4020 ? 149.403 205.587 154.856 1.00 75.40  ? 4020 ILE A CG1   1 
ATOM   19679 C  CG2   . ILE A 1 4020 ? 151.291 204.287 153.850 1.00 65.69  ? 4020 ILE A CG2   1 
ATOM   19680 C  CD1   . ILE A 1 4020 ? 148.128 205.386 155.648 1.00 66.20  ? 4020 ILE A CD1   1 
ATOM   19681 N  N     . MET A 1 4021 ? 149.036 202.409 151.457 1.00 70.73  ? 4021 MET A N     1 
ATOM   19682 C  CA    . MET A 1 4021 ? 149.573 201.321 150.644 1.00 75.36  ? 4021 MET A CA    1 
ATOM   19683 C  C     . MET A 1 4021 ? 149.552 201.653 149.155 1.00 80.89  ? 4021 MET A C     1 
ATOM   19684 O  O     . MET A 1 4021 ? 150.473 201.278 148.421 1.00 82.39  ? 4021 MET A O     1 
ATOM   19685 C  CB    . MET A 1 4021 ? 148.803 200.032 150.922 1.00 65.91  ? 4021 MET A CB    1 
ATOM   19686 C  CG    . MET A 1 4021 ? 148.692 199.653 152.398 1.00 60.35  ? 4021 MET A CG    1 
ATOM   19687 S  SD    . MET A 1 4021 ? 150.178 198.958 153.164 1.00 55.06  ? 4021 MET A SD    1 
ATOM   19688 C  CE    . MET A 1 4021 ? 151.167 200.404 153.534 1.00 56.74  ? 4021 MET A CE    1 
ATOM   19689 N  N     . GLU A 1 4022 ? 148.508 202.341 148.683 1.00 80.82  ? 4022 GLU A N     1 
ATOM   19690 C  CA    . GLU A 1 4022 ? 148.478 202.723 147.273 1.00 83.09  ? 4022 GLU A CA    1 
ATOM   19691 C  C     . GLU A 1 4022 ? 149.592 203.704 146.934 1.00 83.10  ? 4022 GLU A C     1 
ATOM   19692 O  O     . GLU A 1 4022 ? 150.090 203.707 145.802 1.00 85.30  ? 4022 GLU A O     1 
ATOM   19693 C  CB    . GLU A 1 4022 ? 147.118 203.315 146.896 1.00 86.58  ? 4022 GLU A CB    1 
ATOM   19694 C  CG    . GLU A 1 4022 ? 145.963 202.323 146.932 1.00 88.99  ? 4022 GLU A CG    1 
ATOM   19695 C  CD    . GLU A 1 4022 ? 145.400 202.134 148.320 1.00 86.31  ? 4022 GLU A CD    1 
ATOM   19696 O  OE1   . GLU A 1 4022 ? 145.871 202.828 149.238 1.00 85.00  ? 4022 GLU A OE1   1 
ATOM   19697 O  OE2   . GLU A 1 4022 ? 144.493 201.293 148.493 1.00 85.17  ? 4022 GLU A OE2   1 
ATOM   19698 N  N     . GLN A 1 4023 ? 149.993 204.538 147.888 1.00 83.15  ? 4023 GLN A N     1 
ATOM   19699 C  CA    . GLN A 1 4023 ? 151.127 205.418 147.673 1.00 88.39  ? 4023 GLN A CA    1 
ATOM   19700 C  C     . GLN A 1 4023 ? 152.404 204.595 147.508 1.00 96.15  ? 4023 GLN A C     1 
ATOM   19701 O  O     . GLN A 1 4023 ? 152.542 203.524 148.105 1.00 94.13  ? 4023 GLN A O     1 
ATOM   19702 C  CB    . GLN A 1 4023 ? 151.281 206.389 148.840 1.00 88.33  ? 4023 GLN A CB    1 
ATOM   19703 C  CG    . GLN A 1 4023 ? 150.143 207.382 148.976 1.00 94.16  ? 4023 GLN A CG    1 
ATOM   19704 C  CD    . GLN A 1 4023 ? 150.001 207.909 150.389 1.00 92.32  ? 4023 GLN A CD    1 
ATOM   19705 O  OE1   . GLN A 1 4023 ? 150.981 208.315 151.014 1.00 85.70  ? 4023 GLN A OE1   1 
ATOM   19706 N  NE2   . GLN A 1 4023 ? 148.776 207.906 150.901 1.00 86.70  ? 4023 GLN A NE2   1 
ATOM   19707 N  N     . PRO A 1 4024 ? 153.348 205.067 146.694 1.00 99.02  ? 4024 PRO A N     1 
ATOM   19708 C  CA    . PRO A 1 4024 ? 154.598 204.321 146.517 1.00 93.45  ? 4024 PRO A CA    1 
ATOM   19709 C  C     . PRO A 1 4024 ? 155.382 204.241 147.817 1.00 95.53  ? 4024 PRO A C     1 
ATOM   19710 O  O     . PRO A 1 4024 ? 155.347 205.150 148.649 1.00 95.49  ? 4024 PRO A O     1 
ATOM   19711 C  CB    . PRO A 1 4024 ? 155.347 205.132 145.455 1.00 94.58  ? 4024 PRO A CB    1 
ATOM   19712 C  CG    . PRO A 1 4024 ? 154.819 206.515 145.606 1.00 94.84  ? 4024 PRO A CG    1 
ATOM   19713 C  CD    . PRO A 1 4024 ? 153.373 206.362 145.991 1.00 94.24  ? 4024 PRO A CD    1 
ATOM   19714 N  N     . LEU A 1 4025 ? 156.090 203.127 147.987 1.00 91.12  ? 4025 LEU A N     1 
ATOM   19715 C  CA    . LEU A 1 4025 ? 156.836 202.893 149.215 1.00 89.14  ? 4025 LEU A CA    1 
ATOM   19716 C  C     . LEU A 1 4025 ? 157.984 203.887 149.336 1.00 91.44  ? 4025 LEU A C     1 
ATOM   19717 O  O     . LEU A 1 4025 ? 158.752 204.085 148.390 1.00 94.38  ? 4025 LEU A O     1 
ATOM   19718 C  CB    . LEU A 1 4025 ? 157.366 201.460 149.243 1.00 80.41  ? 4025 LEU A CB    1 
ATOM   19719 C  CG    . LEU A 1 4025 ? 158.539 201.171 150.179 1.00 78.28  ? 4025 LEU A CG    1 
ATOM   19720 C  CD1   . LEU A 1 4025 ? 158.087 201.203 151.625 1.00 72.95  ? 4025 LEU A CD1   1 
ATOM   19721 C  CD2   . LEU A 1 4025 ? 159.165 199.830 149.847 1.00 73.97  ? 4025 LEU A CD2   1 
ATOM   19722 N  N     . ASP A 1 4026 ? 158.095 204.516 150.504 1.00 84.86  ? 4026 ASP A N     1 
ATOM   19723 C  CA    . ASP A 1 4026 ? 159.148 205.493 150.779 1.00 85.63  ? 4026 ASP A CA    1 
ATOM   19724 C  C     . ASP A 1 4026 ? 160.162 204.829 151.702 1.00 86.98  ? 4026 ASP A C     1 
ATOM   19725 O  O     . ASP A 1 4026 ? 160.045 204.878 152.927 1.00 87.89  ? 4026 ASP A O     1 
ATOM   19726 C  CB    . ASP A 1 4026 ? 158.568 206.762 151.391 1.00 93.88  ? 4026 ASP A CB    1 
ATOM   19727 C  CG    . ASP A 1 4026 ? 159.376 207.997 151.044 1.00 109.84 ? 4026 ASP A CG    1 
ATOM   19728 O  OD1   . ASP A 1 4026 ? 160.616 207.889 150.947 1.00 106.86 ? 4026 ASP A OD1   1 
ATOM   19729 O  OD2   . ASP A 1 4026 ? 158.770 209.074 150.868 1.00 118.94 ? 4026 ASP A OD2   1 
ATOM   19730 N  N     . LEU A 1 4027 ? 161.173 204.201 151.100 1.00 85.09  ? 4027 LEU A N     1 
ATOM   19731 C  CA    . LEU A 1 4027 ? 162.192 203.506 151.875 1.00 77.58  ? 4027 LEU A CA    1 
ATOM   19732 C  C     . LEU A 1 4027 ? 163.083 204.458 152.660 1.00 80.62  ? 4027 LEU A C     1 
ATOM   19733 O  O     . LEU A 1 4027 ? 163.773 204.013 153.581 1.00 84.26  ? 4027 LEU A O     1 
ATOM   19734 C  CB    . LEU A 1 4027 ? 163.050 202.639 150.955 1.00 75.74  ? 4027 LEU A CB    1 
ATOM   19735 C  CG    . LEU A 1 4027 ? 162.549 201.221 150.691 1.00 72.59  ? 4027 LEU A CG    1 
ATOM   19736 C  CD1   . LEU A 1 4027 ? 163.491 200.493 149.753 1.00 80.56  ? 4027 LEU A CD1   1 
ATOM   19737 C  CD2   . LEU A 1 4027 ? 162.406 200.463 151.997 1.00 69.18  ? 4027 LEU A CD2   1 
ATOM   19738 N  N     . THR A 1 4028 ? 163.079 205.749 152.324 1.00 86.51  ? 4028 THR A N     1 
ATOM   19739 C  CA    . THR A 1 4028 ? 163.987 206.695 152.968 1.00 92.66  ? 4028 THR A CA    1 
ATOM   19740 C  C     . THR A 1 4028 ? 163.802 206.699 154.481 1.00 94.06  ? 4028 THR A C     1 
ATOM   19741 O  O     . THR A 1 4028 ? 164.713 206.332 155.233 1.00 94.31  ? 4028 THR A O     1 
ATOM   19742 C  CB    . THR A 1 4028 ? 163.769 208.098 152.396 1.00 99.54  ? 4028 THR A CB    1 
ATOM   19743 O  OG1   . THR A 1 4028 ? 163.844 208.050 150.967 1.00 101.84 ? 4028 THR A OG1   1 
ATOM   19744 C  CG2   . THR A 1 4028 ? 164.827 209.054 152.920 1.00 98.82  ? 4028 THR A CG2   1 
ATOM   19745 N  N     . HIS A 1 4029 ? 162.615 207.097 154.942 1.00 92.37  ? 4029 HIS A N     1 
ATOM   19746 C  CA    . HIS A 1 4029 ? 162.376 207.209 156.377 1.00 90.93  ? 4029 HIS A CA    1 
ATOM   19747 C  C     . HIS A 1 4029 ? 162.421 205.845 157.053 1.00 87.80  ? 4029 HIS A C     1 
ATOM   19748 O  O     . HIS A 1 4029 ? 162.903 205.722 158.185 1.00 87.54  ? 4029 HIS A O     1 
ATOM   19749 C  CB    . HIS A 1 4029 ? 161.031 207.895 156.626 1.00 92.31  ? 4029 HIS A CB    1 
ATOM   19750 C  CG    . HIS A 1 4029 ? 160.831 208.354 158.037 1.00 98.75  ? 4029 HIS A CG    1 
ATOM   19751 N  ND1   . HIS A 1 4029 ? 161.164 207.583 159.130 1.00 98.22  ? 4029 HIS A ND1   1 
ATOM   19752 C  CD2   . HIS A 1 4029 ? 160.331 209.511 158.533 1.00 99.52  ? 4029 HIS A CD2   1 
ATOM   19753 C  CE1   . HIS A 1 4029 ? 160.878 208.244 160.238 1.00 99.42  ? 4029 HIS A CE1   1 
ATOM   19754 N  NE2   . HIS A 1 4029 ? 160.371 209.417 159.903 1.00 101.99 ? 4029 HIS A NE2   1 
ATOM   19755 N  N     . ILE A 1 4030 ? 161.919 204.809 156.377 1.00 81.14  ? 4030 ILE A N     1 
ATOM   19756 C  CA    . ILE A 1 4030 ? 161.858 203.481 156.983 1.00 75.36  ? 4030 ILE A CA    1 
ATOM   19757 C  C     . ILE A 1 4030 ? 163.261 202.962 157.276 1.00 81.09  ? 4030 ILE A C     1 
ATOM   19758 O  O     . ILE A 1 4030 ? 163.541 202.464 158.372 1.00 85.69  ? 4030 ILE A O     1 
ATOM   19759 C  CB    . ILE A 1 4030 ? 161.077 202.515 156.076 1.00 69.96  ? 4030 ILE A CB    1 
ATOM   19760 C  CG1   . ILE A 1 4030 ? 159.649 203.020 155.873 1.00 68.38  ? 4030 ILE A CG1   1 
ATOM   19761 C  CG2   . ILE A 1 4030 ? 161.074 201.120 156.672 1.00 68.49  ? 4030 ILE A CG2   1 
ATOM   19762 C  CD1   . ILE A 1 4030 ? 158.753 202.046 155.151 1.00 68.04  ? 4030 ILE A CD1   1 
ATOM   19763 N  N     . VAL A 1 4031 ? 164.164 203.067 156.299 1.00 82.90  ? 4031 VAL A N     1 
ATOM   19764 C  CA    . VAL A 1 4031 ? 165.540 202.640 156.526 1.00 77.54  ? 4031 VAL A CA    1 
ATOM   19765 C  C     . VAL A 1 4031 ? 166.252 203.577 157.494 1.00 81.39  ? 4031 VAL A C     1 
ATOM   19766 O  O     . VAL A 1 4031 ? 167.062 203.128 158.315 1.00 83.21  ? 4031 VAL A O     1 
ATOM   19767 C  CB    . VAL A 1 4031 ? 166.295 202.518 155.190 1.00 74.87  ? 4031 VAL A CB    1 
ATOM   19768 C  CG1   . VAL A 1 4031 ? 167.690 201.978 155.419 1.00 77.43  ? 4031 VAL A CG1   1 
ATOM   19769 C  CG2   . VAL A 1 4031 ? 165.547 201.588 154.255 1.00 77.71  ? 4031 VAL A CG2   1 
ATOM   19770 N  N     . GLY A 1 4032 ? 165.970 204.880 157.428 1.00 81.52  ? 4032 GLY A N     1 
ATOM   19771 C  CA    . GLY A 1 4032 ? 166.669 205.816 158.292 1.00 88.09  ? 4032 GLY A CA    1 
ATOM   19772 C  C     . GLY A 1 4032 ? 166.345 205.637 159.763 1.00 89.81  ? 4032 GLY A C     1 
ATOM   19773 O  O     . GLY A 1 4032 ? 167.233 205.720 160.616 1.00 93.87  ? 4032 GLY A O     1 
ATOM   19774 N  N     . THR A 1 4033 ? 165.077 205.390 160.085 1.00 84.86  ? 4033 THR A N     1 
ATOM   19775 C  CA    . THR A 1 4033 ? 164.625 205.362 161.470 1.00 87.03  ? 4033 THR A CA    1 
ATOM   19776 C  C     . THR A 1 4033 ? 164.148 203.993 161.929 1.00 81.10  ? 4033 THR A C     1 
ATOM   19777 O  O     . THR A 1 4033 ? 164.634 203.479 162.941 1.00 77.47  ? 4033 THR A O     1 
ATOM   19778 C  CB    . THR A 1 4033 ? 163.500 206.388 161.670 1.00 92.86  ? 4033 THR A CB    1 
ATOM   19779 O  OG1   . THR A 1 4033 ? 163.979 207.697 161.336 1.00 94.88  ? 4033 THR A OG1   1 
ATOM   19780 C  CG2   . THR A 1 4033 ? 163.021 206.380 163.114 1.00 89.04  ? 4033 THR A CG2   1 
ATOM   19781 N  N     . GLU A 1 4034 ? 163.199 203.387 161.213 1.00 79.19  ? 4034 GLU A N     1 
ATOM   19782 C  CA    . GLU A 1 4034 ? 162.538 202.188 161.721 1.00 74.14  ? 4034 GLU A CA    1 
ATOM   19783 C  C     . GLU A 1 4034 ? 163.489 201.000 161.801 1.00 77.69  ? 4034 GLU A C     1 
ATOM   19784 O  O     . GLU A 1 4034 ? 163.466 200.248 162.781 1.00 80.72  ? 4034 GLU A O     1 
ATOM   19785 C  CB    . GLU A 1 4034 ? 161.329 201.851 160.851 1.00 68.77  ? 4034 GLU A CB    1 
ATOM   19786 C  CG    . GLU A 1 4034 ? 160.340 202.993 160.716 1.00 73.62  ? 4034 GLU A CG    1 
ATOM   19787 C  CD    . GLU A 1 4034 ? 159.115 202.611 159.916 1.00 77.25  ? 4034 GLU A CD    1 
ATOM   19788 O  OE1   . GLU A 1 4034 ? 159.033 201.446 159.474 1.00 74.40  ? 4034 GLU A OE1   1 
ATOM   19789 O  OE2   . GLU A 1 4034 ? 158.233 203.475 159.730 1.00 72.61  ? 4034 GLU A OE2   1 
ATOM   19790 N  N     . VAL A 1 4035 ? 164.329 200.812 160.790 1.00 76.66  ? 4035 VAL A N     1 
ATOM   19791 C  CA    . VAL A 1 4035 ? 165.172 199.624 160.717 1.00 75.98  ? 4035 VAL A CA    1 
ATOM   19792 C  C     . VAL A 1 4035 ? 166.426 199.834 161.554 1.00 79.85  ? 4035 VAL A C     1 
ATOM   19793 O  O     . VAL A 1 4035 ? 167.129 200.841 161.404 1.00 83.13  ? 4035 VAL A O     1 
ATOM   19794 C  CB    . VAL A 1 4035 ? 165.527 199.299 159.258 1.00 72.00  ? 4035 VAL A CB    1 
ATOM   19795 C  CG1   . VAL A 1 4035 ? 166.391 198.055 159.193 1.00 71.33  ? 4035 VAL A CG1   1 
ATOM   19796 C  CG2   . VAL A 1 4035 ? 164.263 199.118 158.436 1.00 63.89  ? 4035 VAL A CG2   1 
ATOM   19797 N  N     . LYS A 1 4036 ? 166.706 198.884 162.443 1.00 77.66  ? 4036 LYS A N     1 
ATOM   19798 C  CA    . LYS A 1 4036 ? 167.926 198.901 163.232 1.00 79.34  ? 4036 LYS A CA    1 
ATOM   19799 C  C     . LYS A 1 4036 ? 169.118 198.474 162.381 1.00 81.14  ? 4036 LYS A C     1 
ATOM   19800 O  O     . LYS A 1 4036 ? 168.954 197.818 161.350 1.00 82.29  ? 4036 LYS A O     1 
ATOM   19801 C  CB    . LYS A 1 4036 ? 167.786 197.978 164.438 1.00 79.91  ? 4036 LYS A CB    1 
ATOM   19802 C  CG    . LYS A 1 4036 ? 166.666 198.357 165.388 1.00 86.26  ? 4036 LYS A CG    1 
ATOM   19803 C  CD    . LYS A 1 4036 ? 166.639 197.436 166.598 1.00 91.92  ? 4036 LYS A CD    1 
ATOM   19804 C  CE    . LYS A 1 4036 ? 166.672 195.972 166.185 1.00 89.12  ? 4036 LYS A CE    1 
ATOM   19805 N  NZ    . LYS A 1 4036 ? 165.533 195.612 165.296 1.00 96.68  ? 4036 LYS A NZ    1 
ATOM   19806 N  N     . PRO A 1 4037 ? 170.336 198.849 162.784 1.00 82.12  ? 4037 PRO A N     1 
ATOM   19807 C  CA    . PRO A 1 4037 ? 171.519 198.427 162.016 1.00 79.74  ? 4037 PRO A CA    1 
ATOM   19808 C  C     . PRO A 1 4037 ? 171.683 196.921 161.914 1.00 79.99  ? 4037 PRO A C     1 
ATOM   19809 O  O     . PRO A 1 4037 ? 172.173 196.432 160.888 1.00 81.31  ? 4037 PRO A O     1 
ATOM   19810 C  CB    . PRO A 1 4037 ? 172.678 199.068 162.789 1.00 83.08  ? 4037 PRO A CB    1 
ATOM   19811 C  CG    . PRO A 1 4037 ? 172.068 200.239 163.468 1.00 87.81  ? 4037 PRO A CG    1 
ATOM   19812 C  CD    . PRO A 1 4037 ? 170.686 199.806 163.847 1.00 87.05  ? 4037 PRO A CD    1 
ATOM   19813 N  N     . ASN A 1 4038 ? 171.295 196.168 162.939 1.00 80.94  ? 4038 ASN A N     1 
ATOM   19814 C  CA    . ASN A 1 4038 ? 171.456 194.720 162.934 1.00 81.80  ? 4038 ASN A CA    1 
ATOM   19815 C  C     . ASN A 1 4038 ? 170.244 193.981 162.379 1.00 79.08  ? 4038 ASN A C     1 
ATOM   19816 O  O     . ASN A 1 4038 ? 170.228 192.746 162.401 1.00 75.82  ? 4038 ASN A O     1 
ATOM   19817 C  CB    . ASN A 1 4038 ? 171.779 194.218 164.348 1.00 79.98  ? 4038 ASN A CB    1 
ATOM   19818 C  CG    . ASN A 1 4038 ? 170.657 194.476 165.343 1.00 86.11  ? 4038 ASN A CG    1 
ATOM   19819 O  OD1   . ASN A 1 4038 ? 169.570 194.926 164.983 1.00 87.00  ? 4038 ASN A OD1   1 
ATOM   19820 N  ND2   . ASN A 1 4038 ? 170.924 194.187 166.611 1.00 91.84  ? 4038 ASN A ND2   1 
ATOM   19821 N  N     . THR A 1 4039 ? 169.234 194.699 161.891 1.00 77.61  ? 4039 THR A N     1 
ATOM   19822 C  CA    . THR A 1 4039 ? 168.061 194.071 161.306 1.00 67.17  ? 4039 THR A CA    1 
ATOM   19823 C  C     . THR A 1 4039 ? 168.172 194.129 159.792 1.00 65.57  ? 4039 THR A C     1 
ATOM   19824 O  O     . THR A 1 4039 ? 168.115 195.228 159.220 1.00 71.18  ? 4039 THR A O     1 
ATOM   19825 C  CB    . THR A 1 4039 ? 166.784 194.768 161.772 1.00 68.99  ? 4039 THR A CB    1 
ATOM   19826 O  OG1   . THR A 1 4039 ? 166.616 194.570 163.180 1.00 79.84  ? 4039 THR A OG1   1 
ATOM   19827 C  CG2   . THR A 1 4039 ? 165.577 194.211 161.043 1.00 60.83  ? 4039 THR A CG2   1 
ATOM   19828 N  N     . PRO A 1 4040 ? 168.344 193.002 159.105 1.00 59.65  ? 4040 PRO A N     1 
ATOM   19829 C  CA    . PRO A 1 4040 ? 168.419 193.040 157.642 1.00 55.70  ? 4040 PRO A CA    1 
ATOM   19830 C  C     . PRO A 1 4040 ? 167.090 193.439 157.025 1.00 52.47  ? 4040 PRO A C     1 
ATOM   19831 O  O     . PRO A 1 4040 ? 166.015 193.116 157.535 1.00 56.66  ? 4040 PRO A O     1 
ATOM   19832 C  CB    . PRO A 1 4040 ? 168.796 191.603 157.269 1.00 53.63  ? 4040 PRO A CB    1 
ATOM   19833 C  CG    . PRO A 1 4040 ? 168.302 190.782 158.403 1.00 53.23  ? 4040 PRO A CG    1 
ATOM   19834 C  CD    . PRO A 1 4040 ? 168.448 191.631 159.631 1.00 57.43  ? 4040 PRO A CD    1 
ATOM   19835 N  N     . VAL A 1 4041 ? 167.176 194.153 155.908 1.00 48.85  ? 4041 VAL A N     1 
ATOM   19836 C  CA    . VAL A 1 4041 ? 166.011 194.557 155.135 1.00 50.39  ? 4041 VAL A CA    1 
ATOM   19837 C  C     . VAL A 1 4041 ? 165.827 193.502 154.052 1.00 53.64  ? 4041 VAL A C     1 
ATOM   19838 O  O     . VAL A 1 4041 ? 166.586 193.447 153.079 1.00 57.18  ? 4041 VAL A O     1 
ATOM   19839 C  CB    . VAL A 1 4041 ? 166.179 195.959 154.545 1.00 51.72  ? 4041 VAL A CB    1 
ATOM   19840 C  CG1   . VAL A 1 4041 ? 164.979 196.321 153.692 1.00 54.53  ? 4041 VAL A CG1   1 
ATOM   19841 C  CG2   . VAL A 1 4041 ? 166.376 196.978 155.652 1.00 46.90  ? 4041 VAL A CG2   1 
ATOM   19842 N  N     . LEU A 1 4042 ? 164.829 192.643 154.232 1.00 51.46  ? 4042 LEU A N     1 
ATOM   19843 C  CA    . LEU A 1 4042 ? 164.526 191.610 153.253 1.00 47.91  ? 4042 LEU A CA    1 
ATOM   19844 C  C     . LEU A 1 4042 ? 163.587 192.186 152.203 1.00 48.71  ? 4042 LEU A C     1 
ATOM   19845 O  O     . LEU A 1 4042 ? 162.545 192.756 152.538 1.00 53.25  ? 4042 LEU A O     1 
ATOM   19846 C  CB    . LEU A 1 4042 ? 163.914 190.389 153.932 1.00 47.49  ? 4042 LEU A CB    1 
ATOM   19847 C  CG    . LEU A 1 4042 ? 164.648 189.913 155.186 1.00 48.22  ? 4042 LEU A CG    1 
ATOM   19848 C  CD1   . LEU A 1 4042 ? 164.037 188.634 155.709 1.00 47.58  ? 4042 LEU A CD1   1 
ATOM   19849 C  CD2   . LEU A 1 4042 ? 166.122 189.712 154.891 1.00 57.39  ? 4042 LEU A CD2   1 
ATOM   19850 N  N     . MET A 1 4043 ? 163.962 192.042 150.938 1.00 50.13  ? 4043 MET A N     1 
ATOM   19851 C  CA    . MET A 1 4043 ? 163.279 192.671 149.815 1.00 47.52  ? 4043 MET A CA    1 
ATOM   19852 C  C     . MET A 1 4043 ? 162.821 191.533 148.914 1.00 54.00  ? 4043 MET A C     1 
ATOM   19853 O  O     . MET A 1 4043 ? 163.578 191.049 148.069 1.00 61.75  ? 4043 MET A O     1 
ATOM   19854 C  CB    . MET A 1 4043 ? 164.211 193.614 149.101 1.00 50.10  ? 4043 MET A CB    1 
ATOM   19855 C  CG    . MET A 1 4043 ? 164.899 194.581 150.038 1.00 59.93  ? 4043 MET A CG    1 
ATOM   19856 S  SD    . MET A 1 4043 ? 165.138 196.215 149.354 1.00 84.29  ? 4043 MET A SD    1 
ATOM   19857 C  CE    . MET A 1 4043 ? 163.471 196.842 149.372 1.00 65.96  ? 4043 MET A CE    1 
ATOM   19858 N  N     . CYS A 1 4044 ? 161.587 191.090 149.109 1.00 56.48  ? 4044 CYS A N     1 
ATOM   19859 C  CA    . CYS A 1 4044 ? 161.082 189.914 148.422 1.00 54.48  ? 4044 CYS A CA    1 
ATOM   19860 C  C     . CYS A 1 4044 ? 160.204 190.335 147.252 1.00 57.09  ? 4044 CYS A C     1 
ATOM   19861 O  O     . CYS A 1 4044 ? 159.241 191.085 147.428 1.00 61.23  ? 4044 CYS A O     1 
ATOM   19862 C  CB    . CYS A 1 4044 ? 160.300 189.032 149.393 1.00 51.10  ? 4044 CYS A CB    1 
ATOM   19863 S  SG    . CYS A 1 4044 ? 161.129 188.768 150.976 1.00 59.64  ? 4044 CYS A SG    1 
ATOM   19864 N  N     . SER A 1 4045 ? 160.543 189.855 146.062 1.00 55.49  ? 4045 SER A N     1 
ATOM   19865 C  CA    . SER A 1 4045 ? 159.774 190.117 144.860 1.00 59.86  ? 4045 SER A CA    1 
ATOM   19866 C  C     . SER A 1 4045 ? 159.095 188.832 144.414 1.00 63.41  ? 4045 SER A C     1 
ATOM   19867 O  O     . SER A 1 4045 ? 159.472 187.736 144.829 1.00 62.47  ? 4045 SER A O     1 
ATOM   19868 C  CB    . SER A 1 4045 ? 160.665 190.655 143.736 1.00 69.43  ? 4045 SER A CB    1 
ATOM   19869 O  OG    . SER A 1 4045 ? 161.370 191.809 144.154 1.00 76.85  ? 4045 SER A OG    1 
ATOM   19870 N  N     . VAL A 1 4046 ? 158.077 188.967 143.574 1.00 67.74  ? 4046 VAL A N     1 
ATOM   19871 C  CA    . VAL A 1 4046 ? 157.475 187.787 142.963 1.00 65.90  ? 4046 VAL A CA    1 
ATOM   19872 C  C     . VAL A 1 4046 ? 158.504 187.221 141.992 1.00 73.39  ? 4046 VAL A C     1 
ATOM   19873 O  O     . VAL A 1 4046 ? 159.351 187.975 141.490 1.00 79.70  ? 4046 VAL A O     1 
ATOM   19874 C  CB    . VAL A 1 4046 ? 156.148 188.119 142.266 1.00 63.17  ? 4046 VAL A CB    1 
ATOM   19875 C  CG1   . VAL A 1 4046 ? 155.186 188.764 143.248 1.00 60.33  ? 4046 VAL A CG1   1 
ATOM   19876 C  CG2   . VAL A 1 4046 ? 156.391 189.019 141.075 1.00 67.18  ? 4046 VAL A CG2   1 
ATOM   19877 N  N     . PRO A 1 4047 ? 158.500 185.912 141.727 1.00 74.66  ? 4047 PRO A N     1 
ATOM   19878 C  CA    . PRO A 1 4047 ? 159.469 185.351 140.776 1.00 76.65  ? 4047 PRO A CA    1 
ATOM   19879 C  C     . PRO A 1 4047 ? 159.451 186.062 139.433 1.00 79.68  ? 4047 PRO A C     1 
ATOM   19880 O  O     . PRO A 1 4047 ? 158.401 186.173 138.792 1.00 81.83  ? 4047 PRO A O     1 
ATOM   19881 C  CB    . PRO A 1 4047 ? 159.022 183.892 140.648 1.00 81.39  ? 4047 PRO A CB    1 
ATOM   19882 C  CG    . PRO A 1 4047 ? 158.388 183.591 141.962 1.00 75.22  ? 4047 PRO A CG    1 
ATOM   19883 C  CD    . PRO A 1 4047 ? 157.717 184.863 142.403 1.00 69.78  ? 4047 PRO A CD    1 
ATOM   19884 N  N     . GLY A 1 4048 ? 160.612 186.553 139.003 1.00 75.55  ? 4048 GLY A N     1 
ATOM   19885 C  CA    . GLY A 1 4048 ? 160.733 187.308 137.776 1.00 80.89  ? 4048 GLY A CA    1 
ATOM   19886 C  C     . GLY A 1 4048 ? 160.843 188.806 137.959 1.00 86.60  ? 4048 GLY A C     1 
ATOM   19887 O  O     . GLY A 1 4048 ? 161.152 189.510 136.989 1.00 95.84  ? 4048 GLY A O     1 
ATOM   19888 N  N     . TYR A 1 4049 ? 160.605 189.312 139.165 1.00 82.83  ? 4049 TYR A N     1 
ATOM   19889 C  CA    . TYR A 1 4049 ? 160.660 190.736 139.457 1.00 82.85  ? 4049 TYR A CA    1 
ATOM   19890 C  C     . TYR A 1 4049 ? 161.914 191.053 140.263 1.00 88.12  ? 4049 TYR A C     1 
ATOM   19891 O  O     . TYR A 1 4049 ? 162.442 190.198 140.980 1.00 88.90  ? 4049 TYR A O     1 
ATOM   19892 C  CB    . TYR A 1 4049 ? 159.409 191.179 140.223 1.00 78.30  ? 4049 TYR A CB    1 
ATOM   19893 C  CG    . TYR A 1 4049 ? 159.167 192.672 140.229 1.00 81.81  ? 4049 TYR A CG    1 
ATOM   19894 C  CD1   . TYR A 1 4049 ? 158.500 193.290 139.181 1.00 79.96  ? 4049 TYR A CD1   1 
ATOM   19895 C  CD2   . TYR A 1 4049 ? 159.587 193.459 141.292 1.00 81.34  ? 4049 TYR A CD2   1 
ATOM   19896 C  CE1   . TYR A 1 4049 ? 158.272 194.652 139.184 1.00 75.50  ? 4049 TYR A CE1   1 
ATOM   19897 C  CE2   . TYR A 1 4049 ? 159.361 194.822 141.304 1.00 80.62  ? 4049 TYR A CE2   1 
ATOM   19898 C  CZ    . TYR A 1 4049 ? 158.703 195.412 140.248 1.00 79.03  ? 4049 TYR A CZ    1 
ATOM   19899 O  OH    . TYR A 1 4049 ? 158.477 196.769 140.255 1.00 80.27  ? 4049 TYR A OH    1 
ATOM   19900 N  N     . ASP A 1 4050 ? 162.391 192.288 140.134 1.00 91.43  ? 4050 ASP A N     1 
ATOM   19901 C  CA    . ASP A 1 4050 ? 163.600 192.740 140.808 1.00 94.70  ? 4050 ASP A CA    1 
ATOM   19902 C  C     . ASP A 1 4050 ? 163.285 193.926 141.707 1.00 97.45  ? 4050 ASP A C     1 
ATOM   19903 O  O     . ASP A 1 4050 ? 162.490 194.800 141.345 1.00 92.85  ? 4050 ASP A O     1 
ATOM   19904 C  CB    . ASP A 1 4050 ? 164.686 193.127 139.799 1.00 95.90  ? 4050 ASP A CB    1 
ATOM   19905 C  CG    . ASP A 1 4050 ? 164.323 194.361 138.997 1.00 103.76 ? 4050 ASP A CG    1 
ATOM   19906 O  OD1   . ASP A 1 4050 ? 163.293 194.331 138.291 1.00 99.52  ? 4050 ASP A OD1   1 
ATOM   19907 O  OD2   . ASP A 1 4050 ? 165.066 195.362 139.076 1.00 104.86 ? 4050 ASP A OD2   1 
ATOM   19908 N  N     . ALA A 1 4051 ? 163.913 193.952 142.884 1.00 96.46  ? 4051 ALA A N     1 
ATOM   19909 C  CA    . ALA A 1 4051 ? 163.711 195.027 143.843 1.00 93.61  ? 4051 ALA A CA    1 
ATOM   19910 C  C     . ALA A 1 4051 ? 165.002 195.710 144.272 1.00 95.14  ? 4051 ALA A C     1 
ATOM   19911 O  O     . ALA A 1 4051 ? 164.954 196.592 145.136 1.00 96.16  ? 4051 ALA A O     1 
ATOM   19912 C  CB    . ALA A 1 4051 ? 162.982 194.504 145.089 1.00 82.03  ? 4051 ALA A CB    1 
ATOM   19913 N  N     . SER A 1 4052 ? 166.148 195.331 143.702 1.00 93.01  ? 4052 SER A N     1 
ATOM   19914 C  CA    . SER A 1 4052 ? 167.410 195.950 144.093 1.00 95.71  ? 4052 SER A CA    1 
ATOM   19915 C  C     . SER A 1 4052 ? 167.514 197.387 143.600 1.00 97.68  ? 4052 SER A C     1 
ATOM   19916 O  O     . SER A 1 4052 ? 168.206 198.205 144.218 1.00 103.01 ? 4052 SER A O     1 
ATOM   19917 C  CB    . SER A 1 4052 ? 168.581 195.123 143.568 1.00 94.40  ? 4052 SER A CB    1 
ATOM   19918 O  OG    . SER A 1 4052 ? 168.540 195.024 142.155 1.00 94.77  ? 4052 SER A OG    1 
ATOM   19919 N  N     . GLY A 1 4053 ? 166.837 197.711 142.496 1.00 92.45  ? 4053 GLY A N     1 
ATOM   19920 C  CA    . GLY A 1 4053 ? 166.880 199.068 141.982 1.00 94.31  ? 4053 GLY A CA    1 
ATOM   19921 C  C     . GLY A 1 4053 ? 166.322 200.088 142.952 1.00 99.03  ? 4053 GLY A C     1 
ATOM   19922 O  O     . GLY A 1 4053 ? 166.764 201.241 142.969 1.00 101.26 ? 4053 GLY A O     1 
ATOM   19923 N  N     . HIS A 1 4054 ? 165.356 199.680 143.778 1.00 97.84  ? 4054 HIS A N     1 
ATOM   19924 C  CA    . HIS A 1 4054 ? 164.786 200.593 144.762 1.00 96.67  ? 4054 HIS A CA    1 
ATOM   19925 C  C     . HIS A 1 4054 ? 165.852 201.090 145.731 1.00 103.49 ? 4054 HIS A C     1 
ATOM   19926 O  O     . HIS A 1 4054 ? 165.989 202.296 145.956 1.00 105.50 ? 4054 HIS A O     1 
ATOM   19927 C  CB    . HIS A 1 4054 ? 163.650 199.903 145.517 1.00 89.70  ? 4054 HIS A CB    1 
ATOM   19928 C  CG    . HIS A 1 4054 ? 162.369 199.834 144.746 1.00 90.29  ? 4054 HIS A CG    1 
ATOM   19929 N  ND1   . HIS A 1 4054 ? 162.156 198.918 143.739 1.00 91.99  ? 4054 HIS A ND1   1 
ATOM   19930 C  CD2   . HIS A 1 4054 ? 161.237 200.571 144.829 1.00 85.97  ? 4054 HIS A CD2   1 
ATOM   19931 C  CE1   . HIS A 1 4054 ? 160.947 199.091 143.237 1.00 84.40  ? 4054 HIS A CE1   1 
ATOM   19932 N  NE2   . HIS A 1 4054 ? 160.368 200.088 143.881 1.00 86.51  ? 4054 HIS A NE2   1 
ATOM   19933 N  N     . VAL A 1 4055 ? 166.644 200.174 146.291 1.00 101.95 ? 4055 VAL A N     1 
ATOM   19934 C  CA    . VAL A 1 4055 ? 167.676 200.595 147.233 1.00 102.98 ? 4055 VAL A CA    1 
ATOM   19935 C  C     . VAL A 1 4055 ? 168.876 201.187 146.504 1.00 101.45 ? 4055 VAL A C     1 
ATOM   19936 O  O     . VAL A 1 4055 ? 169.595 202.020 147.065 1.00 103.00 ? 4055 VAL A O     1 
ATOM   19937 C  CB    . VAL A 1 4055 ? 168.072 199.427 148.152 1.00 96.91  ? 4055 VAL A CB    1 
ATOM   19938 C  CG1   . VAL A 1 4055 ? 169.233 199.809 149.054 1.00 96.29  ? 4055 VAL A CG1   1 
ATOM   19939 C  CG2   . VAL A 1 4055 ? 166.898 199.041 149.002 1.00 93.61  ? 4055 VAL A CG2   1 
ATOM   19940 N  N     . GLU A 1 4056 ? 169.109 200.802 145.248 1.00 101.48 ? 4056 GLU A N     1 
ATOM   19941 C  CA    . GLU A 1 4056 ? 170.130 201.497 144.470 1.00 105.40 ? 4056 GLU A CA    1 
ATOM   19942 C  C     . GLU A 1 4056 ? 169.798 202.981 144.351 1.00 109.37 ? 4056 GLU A C     1 
ATOM   19943 O  O     . GLU A 1 4056 ? 170.643 203.845 144.620 1.00 111.29 ? 4056 GLU A O     1 
ATOM   19944 C  CB    . GLU A 1 4056 ? 170.275 200.857 143.087 1.00 101.74 ? 4056 GLU A CB    1 
ATOM   19945 C  CG    . GLU A 1 4056 ? 170.887 199.452 143.076 1.00 106.31 ? 4056 GLU A CG    1 
ATOM   19946 C  CD    . GLU A 1 4056 ? 172.147 199.308 143.922 1.00 107.06 ? 4056 GLU A CD    1 
ATOM   19947 O  OE1   . GLU A 1 4056 ? 172.462 198.164 144.313 1.00 107.06 ? 4056 GLU A OE1   1 
ATOM   19948 O  OE2   . GLU A 1 4056 ? 172.855 200.311 144.156 1.00 105.54 ? 4056 GLU A OE2   1 
ATOM   19949 N  N     . ASP A 1 4057 ? 168.552 203.296 143.988 1.00 106.48 ? 4057 ASP A N     1 
ATOM   19950 C  CA    . ASP A 1 4057 ? 168.127 204.691 143.930 1.00 108.45 ? 4057 ASP A CA    1 
ATOM   19951 C  C     . ASP A 1 4057 ? 168.091 205.328 145.315 1.00 109.55 ? 4057 ASP A C     1 
ATOM   19952 O  O     . ASP A 1 4057 ? 168.380 206.522 145.455 1.00 113.93 ? 4057 ASP A O     1 
ATOM   19953 C  CB    . ASP A 1 4057 ? 166.757 204.794 143.263 1.00 112.94 ? 4057 ASP A CB    1 
ATOM   19954 C  CG    . ASP A 1 4057 ? 166.803 204.459 141.785 1.00 117.56 ? 4057 ASP A CG    1 
ATOM   19955 O  OD1   . ASP A 1 4057 ? 167.858 204.684 141.155 1.00 114.04 ? 4057 ASP A OD1   1 
ATOM   19956 O  OD2   . ASP A 1 4057 ? 165.786 203.969 141.252 1.00 119.56 ? 4057 ASP A OD2   1 
ATOM   19957 N  N     . LEU A 1 4058 ? 167.739 204.551 146.342 1.00 106.33 ? 4058 LEU A N     1 
ATOM   19958 C  CA    . LEU A 1 4058 ? 167.727 205.067 147.707 1.00 105.85 ? 4058 LEU A CA    1 
ATOM   19959 C  C     . LEU A 1 4058 ? 169.116 205.524 148.135 1.00 109.37 ? 4058 LEU A C     1 
ATOM   19960 O  O     . LEU A 1 4058 ? 169.281 206.608 148.703 1.00 109.84 ? 4058 LEU A O     1 
ATOM   19961 C  CB    . LEU A 1 4058 ? 167.198 203.992 148.656 1.00 97.85  ? 4058 LEU A CB    1 
ATOM   19962 C  CG    . LEU A 1 4058 ? 167.085 204.352 150.136 1.00 93.26  ? 4058 LEU A CG    1 
ATOM   19963 C  CD1   . LEU A 1 4058 ? 166.044 205.431 150.328 1.00 94.70  ? 4058 LEU A CD1   1 
ATOM   19964 C  CD2   . LEU A 1 4058 ? 166.752 203.122 150.963 1.00 89.26  ? 4058 LEU A CD2   1 
ATOM   19965 N  N     . ALA A 1 4059 ? 170.132 204.703 147.865 1.00 109.47 ? 4059 ALA A N     1 
ATOM   19966 C  CA    . ALA A 1 4059 ? 171.501 205.073 148.200 1.00 107.47 ? 4059 ALA A CA    1 
ATOM   19967 C  C     . ALA A 1 4059 ? 172.016 206.183 147.296 1.00 110.42 ? 4059 ALA A C     1 
ATOM   19968 O  O     . ALA A 1 4059 ? 172.843 206.995 147.726 1.00 110.95 ? 4059 ALA A O     1 
ATOM   19969 C  CB    . ALA A 1 4059 ? 172.412 203.850 148.116 1.00 99.93  ? 4059 ALA A CB    1 
ATOM   19970 N  N     . ALA A 1 4060 ? 171.553 206.230 146.044 1.00 109.44 ? 4060 ALA A N     1 
ATOM   19971 C  CA    . ALA A 1 4060 ? 171.938 207.325 145.161 1.00 110.46 ? 4060 ALA A CA    1 
ATOM   19972 C  C     . ALA A 1 4060 ? 171.435 208.663 145.688 1.00 113.85 ? 4060 ALA A C     1 
ATOM   19973 O  O     . ALA A 1 4060 ? 172.177 209.652 145.701 1.00 117.21 ? 4060 ALA A O     1 
ATOM   19974 C  CB    . ALA A 1 4060 ? 171.411 207.071 143.749 1.00 107.49 ? 4060 ALA A CB    1 
ATOM   19975 N  N     . GLU A 1 4061 ? 170.176 208.715 146.128 1.00 112.73 ? 4061 GLU A N     1 
ATOM   19976 C  CA    . GLU A 1 4061 ? 169.629 209.968 146.640 1.00 111.88 ? 4061 GLU A CA    1 
ATOM   19977 C  C     . GLU A 1 4061 ? 170.118 210.273 148.052 1.00 112.53 ? 4061 GLU A C     1 
ATOM   19978 O  O     . GLU A 1 4061 ? 170.183 211.445 148.439 1.00 112.56 ? 4061 GLU A O     1 
ATOM   19979 C  CB    . GLU A 1 4061 ? 168.098 209.941 146.596 1.00 108.10 ? 4061 GLU A CB    1 
ATOM   19980 C  CG    . GLU A 1 4061 ? 167.443 208.859 147.441 1.00 111.75 ? 4061 GLU A CG    1 
ATOM   19981 C  CD    . GLU A 1 4061 ? 167.232 209.287 148.882 1.00 111.49 ? 4061 GLU A CD    1 
ATOM   19982 O  OE1   . GLU A 1 4061 ? 167.237 210.507 149.150 1.00 113.15 ? 4061 GLU A OE1   1 
ATOM   19983 O  OE2   . GLU A 1 4061 ? 167.067 208.404 149.747 1.00 109.50 ? 4061 GLU A OE2   1 
ATOM   19984 N  N     . GLN A 1 4062 ? 170.456 209.245 148.831 1.00 112.03 ? 4062 GLN A N     1 
ATOM   19985 C  CA    . GLN A 1 4062 ? 170.966 209.439 150.182 1.00 114.54 ? 4062 GLN A CA    1 
ATOM   19986 C  C     . GLN A 1 4062 ? 172.458 209.737 150.215 1.00 117.10 ? 4062 GLN A C     1 
ATOM   19987 O  O     . GLN A 1 4062 ? 172.980 210.070 151.285 1.00 117.50 ? 4062 GLN A O     1 
ATOM   19988 C  CB    . GLN A 1 4062 ? 170.677 208.200 151.035 1.00 112.32 ? 4062 GLN A CB    1 
ATOM   19989 C  CG    . GLN A 1 4062 ? 170.421 208.494 152.506 1.00 112.73 ? 4062 GLN A CG    1 
ATOM   19990 C  CD    . GLN A 1 4062 ? 168.971 208.834 152.792 1.00 113.11 ? 4062 GLN A CD    1 
ATOM   19991 O  OE1   . GLN A 1 4062 ? 168.061 208.111 152.389 1.00 107.18 ? 4062 GLN A OE1   1 
ATOM   19992 N  NE2   . GLN A 1 4062 ? 168.750 209.939 153.494 1.00 113.46 ? 4062 GLN A NE2   1 
ATOM   19993 N  N     . ASN A 1 4063 ? 173.147 209.631 149.076 1.00 117.38 ? 4063 ASN A N     1 
ATOM   19994 C  CA    . ASN A 1 4063 ? 174.594 209.837 148.996 1.00 119.27 ? 4063 ASN A CA    1 
ATOM   19995 C  C     . ASN A 1 4063 ? 175.335 208.929 149.976 1.00 117.97 ? 4063 ASN A C     1 
ATOM   19996 O  O     . ASN A 1 4063 ? 176.287 209.342 150.641 1.00 115.76 ? 4063 ASN A O     1 
ATOM   19997 C  CB    . ASN A 1 4063 ? 174.960 211.307 149.223 1.00 122.80 ? 4063 ASN A CB    1 
ATOM   19998 C  CG    . ASN A 1 4063 ? 176.356 211.644 148.732 1.00 125.56 ? 4063 ASN A CG    1 
ATOM   19999 O  OD1   . ASN A 1 4063 ? 177.050 210.796 148.171 1.00 124.53 ? 4063 ASN A OD1   1 
ATOM   20000 N  ND2   . ASN A 1 4063 ? 176.773 212.887 148.941 1.00 123.31 ? 4063 ASN A ND2   1 
ATOM   20001 N  N     . THR A 1 4064 ? 174.886 207.682 150.073 1.00 116.27 ? 4064 THR A N     1 
ATOM   20002 C  CA    . THR A 1 4064 ? 175.517 206.675 150.913 1.00 111.14 ? 4064 THR A CA    1 
ATOM   20003 C  C     . THR A 1 4064 ? 176.116 205.595 150.025 1.00 109.14 ? 4064 THR A C     1 
ATOM   20004 O  O     . THR A 1 4064 ? 175.422 205.032 149.172 1.00 109.59 ? 4064 THR A O     1 
ATOM   20005 C  CB    . THR A 1 4064 ? 174.513 206.057 151.889 1.00 106.29 ? 4064 THR A CB    1 
ATOM   20006 O  OG1   . THR A 1 4064 ? 173.929 207.087 152.695 1.00 111.46 ? 4064 THR A OG1   1 
ATOM   20007 C  CG2   . THR A 1 4064 ? 175.203 205.045 152.790 1.00 96.87  ? 4064 THR A CG2   1 
ATOM   20008 N  N     . GLN A 1 4065 ? 177.403 205.318 150.220 1.00 108.74 ? 4065 GLN A N     1 
ATOM   20009 C  CA    . GLN A 1 4065 ? 178.066 204.286 149.436 1.00 109.11 ? 4065 GLN A CA    1 
ATOM   20010 C  C     . GLN A 1 4065 ? 177.440 202.926 149.713 1.00 103.68 ? 4065 GLN A C     1 
ATOM   20011 O  O     . GLN A 1 4065 ? 177.224 202.544 150.866 1.00 101.89 ? 4065 GLN A O     1 
ATOM   20012 C  CB    . GLN A 1 4065 ? 179.560 204.257 149.760 1.00 114.72 ? 4065 GLN A CB    1 
ATOM   20013 C  CG    . GLN A 1 4065 ? 180.285 203.020 149.254 1.00 119.33 ? 4065 GLN A CG    1 
ATOM   20014 C  CD    . GLN A 1 4065 ? 181.791 203.151 149.346 1.00 123.30 ? 4065 GLN A CD    1 
ATOM   20015 O  OE1   . GLN A 1 4065 ? 182.502 202.977 148.356 1.00 122.54 ? 4065 GLN A OE1   1 
ATOM   20016 N  NE2   . GLN A 1 4065 ? 182.287 203.459 150.538 1.00 124.31 ? 4065 GLN A NE2   1 
ATOM   20017 N  N     . ILE A 1 4066 ? 177.144 202.193 148.643 1.00 99.88  ? 4066 ILE A N     1 
ATOM   20018 C  CA    . ILE A 1 4066 ? 176.561 200.861 148.741 1.00 98.79  ? 4066 ILE A CA    1 
ATOM   20019 C  C     . ILE A 1 4066 ? 177.350 199.921 147.842 1.00 99.60  ? 4066 ILE A C     1 
ATOM   20020 O  O     . ILE A 1 4066 ? 177.739 200.287 146.727 1.00 102.38 ? 4066 ILE A O     1 
ATOM   20021 C  CB    . ILE A 1 4066 ? 175.060 200.865 148.374 1.00 98.96  ? 4066 ILE A CB    1 
ATOM   20022 C  CG1   . ILE A 1 4066 ? 174.450 199.478 148.589 1.00 92.60  ? 4066 ILE A CG1   1 
ATOM   20023 C  CG2   . ILE A 1 4066 ? 174.844 201.344 146.946 1.00 98.24  ? 4066 ILE A CG2   1 
ATOM   20024 C  CD1   . ILE A 1 4066 ? 172.943 199.462 148.539 1.00 86.09  ? 4066 ILE A CD1   1 
ATOM   20025 N  N     . THR A 1 4067 ? 177.611 198.717 148.339 1.00 94.43  ? 4067 THR A N     1 
ATOM   20026 C  CA    . THR A 1 4067 ? 178.296 197.682 147.574 1.00 90.79  ? 4067 THR A CA    1 
ATOM   20027 C  C     . THR A 1 4067 ? 177.309 196.565 147.268 1.00 85.75  ? 4067 THR A C     1 
ATOM   20028 O  O     . THR A 1 4067 ? 176.781 195.934 148.187 1.00 87.34  ? 4067 THR A O     1 
ATOM   20029 C  CB    . THR A 1 4067 ? 179.503 197.137 148.337 1.00 97.83  ? 4067 THR A CB    1 
ATOM   20030 O  OG1   . THR A 1 4067 ? 179.067 196.545 149.566 1.00 94.16  ? 4067 THR A OG1   1 
ATOM   20031 C  CG2   . THR A 1 4067 ? 180.486 198.255 148.635 1.00 100.12 ? 4067 THR A CG2   1 
ATOM   20032 N  N     . SER A 1 4068 ? 177.066 196.326 145.982 1.00 87.80  ? 4068 SER A N     1 
ATOM   20033 C  CA    . SER A 1 4068 ? 176.111 195.316 145.544 1.00 88.33  ? 4068 SER A CA    1 
ATOM   20034 C  C     . SER A 1 4068 ? 176.850 194.045 145.147 1.00 87.13  ? 4068 SER A C     1 
ATOM   20035 O  O     . SER A 1 4068 ? 177.819 194.096 144.384 1.00 91.55  ? 4068 SER A O     1 
ATOM   20036 C  CB    . SER A 1 4068 ? 175.280 195.835 144.371 1.00 88.36  ? 4068 SER A CB    1 
ATOM   20037 O  OG    . SER A 1 4068 ? 174.484 196.941 144.759 1.00 91.25  ? 4068 SER A OG    1 
ATOM   20038 N  N     . ILE A 1 4069 ? 176.388 192.908 145.664 1.00 78.82  ? 4069 ILE A N     1 
ATOM   20039 C  CA    . ILE A 1 4069 ? 177.059 191.627 145.492 1.00 78.61  ? 4069 ILE A CA    1 
ATOM   20040 C  C     . ILE A 1 4069 ? 176.024 190.589 145.087 1.00 79.88  ? 4069 ILE A C     1 
ATOM   20041 O  O     . ILE A 1 4069 ? 175.005 190.427 145.767 1.00 83.30  ? 4069 ILE A O     1 
ATOM   20042 C  CB    . ILE A 1 4069 ? 177.776 191.199 146.785 1.00 80.55  ? 4069 ILE A CB    1 
ATOM   20043 C  CG1   . ILE A 1 4069 ? 178.814 192.250 147.174 1.00 88.05  ? 4069 ILE A CG1   1 
ATOM   20044 C  CG2   . ILE A 1 4069 ? 178.416 189.832 146.615 1.00 83.83  ? 4069 ILE A CG2   1 
ATOM   20045 C  CD1   . ILE A 1 4069 ? 179.606 191.900 148.389 1.00 92.20  ? 4069 ILE A CD1   1 
ATOM   20046 N  N     . ALA A 1 4070 ? 176.291 189.880 143.994 1.00 80.15  ? 4070 ALA A N     1 
ATOM   20047 C  CA    . ALA A 1 4070 ? 175.402 188.832 143.511 1.00 76.32  ? 4070 ALA A CA    1 
ATOM   20048 C  C     . ALA A 1 4070 ? 175.773 187.514 144.181 1.00 78.99  ? 4070 ALA A C     1 
ATOM   20049 O  O     . ALA A 1 4070 ? 176.904 187.038 144.043 1.00 87.44  ? 4070 ALA A O     1 
ATOM   20050 C  CB    . ALA A 1 4070 ? 175.483 188.711 141.991 1.00 78.57  ? 4070 ALA A CB    1 
ATOM   20051 N  N     . ILE A 1 4071 ? 174.823 186.931 144.898 1.00 75.56  ? 4071 ILE A N     1 
ATOM   20052 C  CA    . ILE A 1 4071 ? 175.069 185.722 145.674 1.00 82.15  ? 4071 ILE A CA    1 
ATOM   20053 C  C     . ILE A 1 4071 ? 174.784 184.494 144.819 1.00 84.77  ? 4071 ILE A C     1 
ATOM   20054 O  O     . ILE A 1 4071 ? 173.979 184.533 143.882 1.00 82.55  ? 4071 ILE A O     1 
ATOM   20055 C  CB    . ILE A 1 4071 ? 174.214 185.746 146.957 1.00 74.91  ? 4071 ILE A CB    1 
ATOM   20056 C  CG1   . ILE A 1 4071 ? 174.397 187.082 147.674 1.00 73.17  ? 4071 ILE A CG1   1 
ATOM   20057 C  CG2   . ILE A 1 4071 ? 174.583 184.610 147.894 1.00 82.35  ? 4071 ILE A CG2   1 
ATOM   20058 C  CD1   . ILE A 1 4071 ? 175.826 187.367 148.069 1.00 79.77  ? 4071 ILE A CD1   1 
ATOM   20059 N  N     . GLY A 1 4072 ? 175.455 183.389 145.140 1.00 89.07  ? 4072 GLY A N     1 
ATOM   20060 C  CA    . GLY A 1 4072 ? 175.270 182.149 144.413 1.00 93.31  ? 4072 GLY A CA    1 
ATOM   20061 C  C     . GLY A 1 4072 ? 176.540 181.345 144.218 1.00 106.69 ? 4072 GLY A C     1 
ATOM   20062 O  O     . GLY A 1 4072 ? 176.483 180.124 144.040 1.00 109.00 ? 4072 GLY A O     1 
ATOM   20063 N  N     . SER A 1 4073 ? 177.690 182.009 144.250 1.00 111.09 ? 4073 SER A N     1 
ATOM   20064 C  CA    . SER A 1 4073 ? 178.980 181.361 144.067 1.00 111.92 ? 4073 SER A CA    1 
ATOM   20065 C  C     . SER A 1 4073 ? 179.850 181.559 145.302 1.00 117.22 ? 4073 SER A C     1 
ATOM   20066 O  O     . SER A 1 4073 ? 179.666 182.503 146.073 1.00 120.15 ? 4073 SER A O     1 
ATOM   20067 C  CB    . SER A 1 4073 ? 179.695 181.906 142.827 1.00 111.82 ? 4073 SER A CB    1 
ATOM   20068 O  OG    . SER A 1 4073 ? 179.955 183.292 142.956 1.00 113.36 ? 4073 SER A OG    1 
ATOM   20069 N  N     . ALA A 1 4074 ? 180.813 180.648 145.479 1.00 118.82 ? 4074 ALA A N     1 
ATOM   20070 C  CA    . ALA A 1 4074 ? 181.686 180.708 146.649 1.00 117.69 ? 4074 ALA A CA    1 
ATOM   20071 C  C     . ALA A 1 4074 ? 182.490 182.002 146.676 1.00 115.38 ? 4074 ALA A C     1 
ATOM   20072 O  O     . ALA A 1 4074 ? 182.667 182.612 147.739 1.00 112.74 ? 4074 ALA A O     1 
ATOM   20073 C  CB    . ALA A 1 4074 ? 182.615 179.495 146.672 1.00 115.71 ? 4074 ALA A CB    1 
ATOM   20074 N  N     . GLU A 1 4075 ? 182.994 182.432 145.516 1.00 118.48 ? 4075 GLU A N     1 
ATOM   20075 C  CA    . GLU A 1 4075 ? 183.619 183.747 145.431 1.00 118.90 ? 4075 GLU A CA    1 
ATOM   20076 C  C     . GLU A 1 4075 ? 182.625 184.838 145.804 1.00 117.42 ? 4075 GLU A C     1 
ATOM   20077 O  O     . GLU A 1 4075 ? 182.989 185.830 146.447 1.00 114.39 ? 4075 GLU A O     1 
ATOM   20078 C  CB    . GLU A 1 4075 ? 184.173 183.981 144.024 1.00 125.05 ? 4075 GLU A CB    1 
ATOM   20079 C  CG    . GLU A 1 4075 ? 185.274 183.014 143.608 1.00 130.31 ? 4075 GLU A CG    1 
ATOM   20080 C  CD    . GLU A 1 4075 ? 184.734 181.686 143.112 1.00 128.89 ? 4075 GLU A CD    1 
ATOM   20081 O  OE1   . GLU A 1 4075 ? 183.498 181.550 142.998 1.00 122.29 ? 4075 GLU A OE1   1 
ATOM   20082 O  OE2   . GLU A 1 4075 ? 185.547 180.779 142.837 1.00 128.32 ? 4075 GLU A OE2   1 
ATOM   20083 N  N     . GLY A 1 4076 ? 181.361 184.665 145.412 1.00 119.27 ? 4076 GLY A N     1 
ATOM   20084 C  CA    . GLY A 1 4076 ? 180.327 185.584 145.853 1.00 110.68 ? 4076 GLY A CA    1 
ATOM   20085 C  C     . GLY A 1 4076 ? 180.155 185.587 147.359 1.00 108.08 ? 4076 GLY A C     1 
ATOM   20086 O  O     . GLY A 1 4076 ? 179.967 186.641 147.965 1.00 108.89 ? 4076 GLY A O     1 
ATOM   20087 N  N     . PHE A 1 4077 ? 180.220 184.408 147.984 1.00 107.04 ? 4077 PHE A N     1 
ATOM   20088 C  CA    . PHE A 1 4077 ? 180.111 184.330 149.441 1.00 107.61 ? 4077 PHE A CA    1 
ATOM   20089 C  C     . PHE A 1 4077 ? 181.264 185.058 150.122 1.00 109.62 ? 4077 PHE A C     1 
ATOM   20090 O  O     . PHE A 1 4077 ? 181.066 185.778 151.110 1.00 107.42 ? 4077 PHE A O     1 
ATOM   20091 C  CB    . PHE A 1 4077 ? 180.066 182.867 149.898 1.00 102.07 ? 4077 PHE A CB    1 
ATOM   20092 C  CG    . PHE A 1 4077 ? 178.855 182.095 149.430 1.00 101.55 ? 4077 PHE A CG    1 
ATOM   20093 C  CD1   . PHE A 1 4077 ? 177.945 182.639 148.538 1.00 100.96 ? 4077 PHE A CD1   1 
ATOM   20094 C  CD2   . PHE A 1 4077 ? 178.638 180.806 149.886 1.00 102.85 ? 4077 PHE A CD2   1 
ATOM   20095 C  CE1   . PHE A 1 4077 ? 176.848 181.917 148.118 1.00 100.75 ? 4077 PHE A CE1   1 
ATOM   20096 C  CE2   . PHE A 1 4077 ? 177.541 180.079 149.469 1.00 101.17 ? 4077 PHE A CE2   1 
ATOM   20097 C  CZ    . PHE A 1 4077 ? 176.645 180.636 148.584 1.00 100.00 ? 4077 PHE A CZ    1 
ATOM   20098 N  N     . ASN A 1 4078 ? 182.486 184.864 149.617 1.00 110.54 ? 4078 ASN A N     1 
ATOM   20099 C  CA    . ASN A 1 4078 ? 183.639 185.538 150.208 1.00 107.12 ? 4078 ASN A CA    1 
ATOM   20100 C  C     . ASN A 1 4078 ? 183.551 187.047 150.022 1.00 106.03 ? 4078 ASN A C     1 
ATOM   20101 O  O     . ASN A 1 4078 ? 183.822 187.817 150.953 1.00 107.29 ? 4078 ASN A O     1 
ATOM   20102 C  CB    . ASN A 1 4078 ? 184.932 184.994 149.602 1.00 109.30 ? 4078 ASN A CB    1 
ATOM   20103 C  CG    . ASN A 1 4078 ? 185.355 183.679 150.223 1.00 110.54 ? 4078 ASN A CG    1 
ATOM   20104 O  OD1   . ASN A 1 4078 ? 184.655 182.673 150.112 1.00 111.80 ? 4078 ASN A OD1   1 
ATOM   20105 N  ND2   . ASN A 1 4078 ? 186.507 183.681 150.884 1.00 109.80 ? 4078 ASN A ND2   1 
ATOM   20106 N  N     . GLN A 1 4079 ? 183.163 187.492 148.827 1.00 105.27 ? 4079 GLN A N     1 
ATOM   20107 C  CA    . GLN A 1 4079 ? 182.973 188.920 148.612 1.00 103.85 ? 4079 GLN A CA    1 
ATOM   20108 C  C     . GLN A 1 4079 ? 181.905 189.462 149.552 1.00 105.37 ? 4079 GLN A C     1 
ATOM   20109 O  O     . GLN A 1 4079 ? 182.074 190.533 150.149 1.00 104.51 ? 4079 GLN A O     1 
ATOM   20110 C  CB    . GLN A 1 4079 ? 182.606 189.178 147.151 1.00 100.47 ? 4079 GLN A CB    1 
ATOM   20111 C  CG    . GLN A 1 4079 ? 182.496 190.641 146.777 1.00 100.56 ? 4079 GLN A CG    1 
ATOM   20112 C  CD    . GLN A 1 4079 ? 182.189 190.838 145.308 1.00 98.45  ? 4079 GLN A CD    1 
ATOM   20113 O  OE1   . GLN A 1 4079 ? 182.022 189.873 144.563 1.00 100.65 ? 4079 GLN A OE1   1 
ATOM   20114 N  NE2   . GLN A 1 4079 ? 182.108 192.092 144.882 1.00 91.75  ? 4079 GLN A NE2   1 
ATOM   20115 N  N     . ALA A 1 4080 ? 180.821 188.704 149.734 1.00 105.47 ? 4080 ALA A N     1 
ATOM   20116 C  CA    . ALA A 1 4080 ? 179.733 189.138 150.599 1.00 103.19 ? 4080 ALA A CA    1 
ATOM   20117 C  C     . ALA A 1 4080 ? 180.193 189.302 152.039 1.00 107.73 ? 4080 ALA A C     1 
ATOM   20118 O  O     . ALA A 1 4080 ? 179.916 190.329 152.664 1.00 108.57 ? 4080 ALA A O     1 
ATOM   20119 C  CB    . ALA A 1 4080 ? 178.573 188.147 150.519 1.00 97.77  ? 4080 ALA A CB    1 
ATOM   20120 N  N     . ASP A 1 4081 ? 180.903 188.313 152.588 1.00 106.48 ? 4081 ASP A N     1 
ATOM   20121 C  CA    . ASP A 1 4081 ? 181.219 188.397 154.012 1.00 107.56 ? 4081 ASP A CA    1 
ATOM   20122 C  C     . ASP A 1 4081 ? 182.319 189.424 154.266 1.00 106.09 ? 4081 ASP A C     1 
ATOM   20123 O  O     . ASP A 1 4081 ? 182.293 190.135 155.279 1.00 106.18 ? 4081 ASP A O     1 
ATOM   20124 C  CB    . ASP A 1 4081 ? 181.570 187.018 154.597 1.00 112.50 ? 4081 ASP A CB    1 
ATOM   20125 C  CG    . ASP A 1 4081 ? 182.895 186.458 154.106 1.00 115.98 ? 4081 ASP A CG    1 
ATOM   20126 O  OD1   . ASP A 1 4081 ? 183.592 187.108 153.317 1.00 117.96 ? 4081 ASP A OD1   1 
ATOM   20127 O  OD2   . ASP A 1 4081 ? 183.242 185.334 154.527 1.00 114.00 ? 4081 ASP A OD2   1 
ATOM   20128 N  N     . LYS A 1 4082 ? 183.279 189.555 153.338 1.00 106.85 ? 4082 LYS A N     1 
ATOM   20129 C  CA    . LYS A 1 4082 ? 184.293 190.590 153.527 1.00 105.29 ? 4082 LYS A CA    1 
ATOM   20130 C  C     . LYS A 1 4082 ? 183.681 191.983 153.413 1.00 105.47 ? 4082 LYS A C     1 
ATOM   20131 O  O     . LYS A 1 4082 ? 184.039 192.889 154.177 1.00 105.18 ? 4082 LYS A O     1 
ATOM   20132 C  CB    . LYS A 1 4082 ? 185.453 190.423 152.540 1.00 104.95 ? 4082 LYS A CB    1 
ATOM   20133 C  CG    . LYS A 1 4082 ? 185.137 190.683 151.078 1.00 109.67 ? 4082 LYS A CG    1 
ATOM   20134 C  CD    . LYS A 1 4082 ? 186.373 190.466 150.215 1.00 108.98 ? 4082 LYS A CD    1 
ATOM   20135 C  CE    . LYS A 1 4082 ? 186.077 190.684 148.741 1.00 104.07 ? 4082 LYS A CE    1 
ATOM   20136 N  NZ    . LYS A 1 4082 ? 185.749 192.106 148.447 1.00 97.29  ? 4082 LYS A NZ    1 
ATOM   20137 N  N     . ALA A 1 4083 ? 182.737 192.174 152.484 1.00 105.14 ? 4083 ALA A N     1 
ATOM   20138 C  CA    . ALA A 1 4083 ? 182.084 193.472 152.369 1.00 104.81 ? 4083 ALA A CA    1 
ATOM   20139 C  C     . ALA A 1 4083 ? 181.196 193.750 153.573 1.00 102.62 ? 4083 ALA A C     1 
ATOM   20140 O  O     . ALA A 1 4083 ? 181.079 194.900 154.010 1.00 103.54 ? 4083 ALA A O     1 
ATOM   20141 C  CB    . ALA A 1 4083 ? 181.276 193.545 151.076 1.00 101.49 ? 4083 ALA A CB    1 
ATOM   20142 N  N     . ILE A 1 4084 ? 180.562 192.713 154.125 1.00 98.89  ? 4084 ILE A N     1 
ATOM   20143 C  CA    . ILE A 1 4084 ? 179.763 192.890 155.334 1.00 97.26  ? 4084 ILE A CA    1 
ATOM   20144 C  C     . ILE A 1 4084 ? 180.648 193.329 156.491 1.00 99.57  ? 4084 ILE A C     1 
ATOM   20145 O  O     . ILE A 1 4084 ? 180.285 194.226 157.259 1.00 99.27  ? 4084 ILE A O     1 
ATOM   20146 C  CB    . ILE A 1 4084 ? 178.991 191.599 155.664 1.00 100.17 ? 4084 ILE A CB    1 
ATOM   20147 C  CG1   . ILE A 1 4084 ? 177.797 191.434 154.723 1.00 98.12  ? 4084 ILE A CG1   1 
ATOM   20148 C  CG2   . ILE A 1 4084 ? 178.520 191.606 157.111 1.00 96.38  ? 4084 ILE A CG2   1 
ATOM   20149 C  CD1   . ILE A 1 4084 ? 176.995 190.179 154.973 1.00 91.64  ? 4084 ILE A CD1   1 
ATOM   20150 N  N     . ASN A 1 4085 ? 181.822 192.709 156.635 1.00 102.55 ? 4085 ASN A N     1 
ATOM   20151 C  CA    . ASN A 1 4085 ? 182.747 193.119 157.689 1.00 101.13 ? 4085 ASN A CA    1 
ATOM   20152 C  C     . ASN A 1 4085 ? 183.215 194.558 157.484 1.00 98.97  ? 4085 ASN A C     1 
ATOM   20153 O  O     . ASN A 1 4085 ? 183.247 195.358 158.430 1.00 98.40  ? 4085 ASN A O     1 
ATOM   20154 C  CB    . ASN A 1 4085 ? 183.937 192.162 157.740 1.00 102.74 ? 4085 ASN A CB    1 
ATOM   20155 C  CG    . ASN A 1 4085 ? 183.532 190.754 158.121 1.00 103.26 ? 4085 ASN A CG    1 
ATOM   20156 O  OD1   . ASN A 1 4085 ? 182.358 190.479 158.364 1.00 100.54 ? 4085 ASN A OD1   1 
ATOM   20157 N  ND2   . ASN A 1 4085 ? 184.504 189.852 158.176 1.00 104.30 ? 4085 ASN A ND2   1 
ATOM   20158 N  N     . THR A 1 4086 ? 183.568 194.910 156.246 1.00 99.54  ? 4086 THR A N     1 
ATOM   20159 C  CA    . THR A 1 4086 ? 184.014 196.272 155.970 1.00 99.89  ? 4086 THR A CA    1 
ATOM   20160 C  C     . THR A 1 4086 ? 182.919 197.285 156.283 1.00 102.24 ? 4086 THR A C     1 
ATOM   20161 O  O     . THR A 1 4086 ? 183.184 198.337 156.876 1.00 101.99 ? 4086 THR A O     1 
ATOM   20162 C  CB    . THR A 1 4086 ? 184.457 196.394 154.513 1.00 101.68 ? 4086 THR A CB    1 
ATOM   20163 O  OG1   . THR A 1 4086 ? 185.488 195.435 154.244 1.00 103.25 ? 4086 THR A OG1   1 
ATOM   20164 C  CG2   . THR A 1 4086 ? 184.988 197.791 154.231 1.00 100.88 ? 4086 THR A CG2   1 
ATOM   20165 N  N     . ALA A 1 4087 ? 181.677 196.978 155.905 1.00 102.49 ? 4087 ALA A N     1 
ATOM   20166 C  CA    . ALA A 1 4087 ? 180.579 197.907 156.136 1.00 98.72  ? 4087 ALA A CA    1 
ATOM   20167 C  C     . ALA A 1 4087 ? 180.207 198.001 157.609 1.00 97.17  ? 4087 ALA A C     1 
ATOM   20168 O  O     . ALA A 1 4087 ? 179.871 199.089 158.089 1.00 96.67  ? 4087 ALA A O     1 
ATOM   20169 C  CB    . ALA A 1 4087 ? 179.367 197.492 155.311 1.00 92.96  ? 4087 ALA A CB    1 
ATOM   20170 N  N     . VAL A 1 4088 ? 180.242 196.884 158.340 1.00 95.74  ? 4088 VAL A N     1 
ATOM   20171 C  CA    . VAL A 1 4088 ? 179.919 196.941 159.760 1.00 95.15  ? 4088 VAL A CA    1 
ATOM   20172 C  C     . VAL A 1 4088 ? 180.983 197.727 160.512 1.00 101.09 ? 4088 VAL A C     1 
ATOM   20173 O  O     . VAL A 1 4088 ? 180.671 198.437 161.476 1.00 103.00 ? 4088 VAL A O     1 
ATOM   20174 C  CB    . VAL A 1 4088 ? 179.721 195.527 160.346 1.00 92.08  ? 4088 VAL A CB    1 
ATOM   20175 C  CG1   . VAL A 1 4088 ? 180.996 194.727 160.317 1.00 97.92  ? 4088 VAL A CG1   1 
ATOM   20176 C  CG2   . VAL A 1 4088 ? 179.228 195.615 161.762 1.00 94.83  ? 4088 VAL A CG2   1 
ATOM   20177 N  N     . LYS A 1 4089 ? 182.247 197.635 160.091 1.00 101.56 ? 4089 LYS A N     1 
ATOM   20178 C  CA    . LYS A 1 4089 ? 183.268 198.448 160.739 1.00 99.44  ? 4089 LYS A CA    1 
ATOM   20179 C  C     . LYS A 1 4089 ? 183.357 199.862 160.175 1.00 100.42 ? 4089 LYS A C     1 
ATOM   20180 O  O     . LYS A 1 4089 ? 184.061 200.694 160.756 1.00 105.37 ? 4089 LYS A O     1 
ATOM   20181 C  CB    . LYS A 1 4089 ? 184.637 197.770 160.636 1.00 100.97 ? 4089 LYS A CB    1 
ATOM   20182 C  CG    . LYS A 1 4089 ? 185.228 197.761 159.241 1.00 106.67 ? 4089 LYS A CG    1 
ATOM   20183 C  CD    . LYS A 1 4089 ? 186.675 197.303 159.260 1.00 107.23 ? 4089 LYS A CD    1 
ATOM   20184 C  CE    . LYS A 1 4089 ? 187.482 197.986 158.170 1.00 106.23 ? 4089 LYS A CE    1 
ATOM   20185 N  NZ    . LYS A 1 4089 ? 187.251 197.362 156.839 1.00 105.61 ? 4089 LYS A NZ    1 
ATOM   20186 N  N     . SER A 1 4090 ? 182.665 200.162 159.073 1.00 97.92  ? 4090 SER A N     1 
ATOM   20187 C  CA    . SER A 1 4090 ? 182.765 201.473 158.441 1.00 99.98  ? 4090 SER A CA    1 
ATOM   20188 C  C     . SER A 1 4090 ? 181.414 202.125 158.158 1.00 101.36 ? 4090 SER A C     1 
ATOM   20189 O  O     . SER A 1 4090 ? 181.380 203.205 157.557 1.00 97.72  ? 4090 SER A O     1 
ATOM   20190 C  CB    . SER A 1 4090 ? 183.569 201.370 157.141 1.00 103.03 ? 4090 SER A CB    1 
ATOM   20191 O  OG    . SER A 1 4090 ? 182.944 200.491 156.223 1.00 105.00 ? 4090 SER A OG    1 
ATOM   20192 N  N     . GLY A 1 4091 ? 180.307 201.512 158.574 1.00 102.28 ? 4091 GLY A N     1 
ATOM   20193 C  CA    . GLY A 1 4091 ? 178.998 202.113 158.384 1.00 100.57 ? 4091 GLY A CA    1 
ATOM   20194 C  C     . GLY A 1 4091 ? 178.574 202.274 156.937 1.00 100.53 ? 4091 GLY A C     1 
ATOM   20195 O  O     . GLY A 1 4091 ? 178.094 203.339 156.539 1.00 98.21  ? 4091 GLY A O     1 
ATOM   20196 N  N     . ARG A 1 4092 ? 178.745 201.222 156.142 1.00 99.97  ? 4092 ARG A N     1 
ATOM   20197 C  CA    . ARG A 1 4092 ? 178.444 201.235 154.719 1.00 96.85  ? 4092 ARG A CA    1 
ATOM   20198 C  C     . ARG A 1 4092 ? 177.264 200.311 154.436 1.00 94.32  ? 4092 ARG A C     1 
ATOM   20199 O  O     . ARG A 1 4092 ? 176.924 199.443 155.243 1.00 95.65  ? 4092 ARG A O     1 
ATOM   20200 C  CB    . ARG A 1 4092 ? 179.682 200.814 153.912 1.00 99.79  ? 4092 ARG A CB    1 
ATOM   20201 C  CG    . ARG A 1 4092 ? 179.593 200.992 152.408 1.00 103.05 ? 4092 ARG A CG    1 
ATOM   20202 C  CD    . ARG A 1 4092 ? 180.739 200.260 151.734 1.00 108.35 ? 4092 ARG A CD    1 
ATOM   20203 N  NE    . ARG A 1 4092 ? 180.794 198.862 152.142 1.00 111.68 ? 4092 ARG A NE    1 
ATOM   20204 C  CZ    . ARG A 1 4092 ? 181.775 198.026 151.833 1.00 112.58 ? 4092 ARG A CZ    1 
ATOM   20205 N  NH1   . ARG A 1 4092 ? 182.815 198.416 151.114 1.00 115.14 ? 4092 ARG A NH1   1 
ATOM   20206 N  NH2   . ARG A 1 4092 ? 181.713 196.767 152.257 1.00 105.71 ? 4092 ARG A NH2   1 
ATOM   20207 N  N     . TRP A 1 4093 ? 176.622 200.515 153.288 1.00 93.81  ? 4093 TRP A N     1 
ATOM   20208 C  CA    . TRP A 1 4093 ? 175.470 199.717 152.894 1.00 85.21  ? 4093 TRP A CA    1 
ATOM   20209 C  C     . TRP A 1 4093 ? 175.890 198.535 152.029 1.00 84.83  ? 4093 TRP A C     1 
ATOM   20210 O  O     . TRP A 1 4093 ? 176.730 198.657 151.133 1.00 90.56  ? 4093 TRP A O     1 
ATOM   20211 C  CB    . TRP A 1 4093 ? 174.440 200.558 152.137 1.00 85.34  ? 4093 TRP A CB    1 
ATOM   20212 C  CG    . TRP A 1 4093 ? 173.681 201.513 152.998 1.00 84.34  ? 4093 TRP A CG    1 
ATOM   20213 C  CD1   . TRP A 1 4093 ? 173.923 201.810 154.305 1.00 87.15  ? 4093 TRP A CD1   1 
ATOM   20214 C  CD2   . TRP A 1 4093 ? 172.528 202.273 152.621 1.00 81.64  ? 4093 TRP A CD2   1 
ATOM   20215 N  NE1   . TRP A 1 4093 ? 173.005 202.723 154.761 1.00 89.04  ? 4093 TRP A NE1   1 
ATOM   20216 C  CE2   . TRP A 1 4093 ? 172.136 203.022 153.745 1.00 83.67  ? 4093 TRP A CE2   1 
ATOM   20217 C  CE3   . TRP A 1 4093 ? 171.795 202.399 151.438 1.00 84.71  ? 4093 TRP A CE3   1 
ATOM   20218 C  CZ2   . TRP A 1 4093 ? 171.044 203.884 153.724 1.00 86.23  ? 4093 TRP A CZ2   1 
ATOM   20219 C  CZ3   . TRP A 1 4093 ? 170.711 203.255 151.418 1.00 86.68  ? 4093 TRP A CZ3   1 
ATOM   20220 C  CH2   . TRP A 1 4093 ? 170.345 203.987 152.553 1.00 88.91  ? 4093 TRP A CH2   1 
ATOM   20221 N  N     . VAL A 1 4094 ? 175.278 197.385 152.300 1.00 77.40  ? 4094 VAL A N     1 
ATOM   20222 C  CA    . VAL A 1 4094 ? 175.540 196.161 151.556 1.00 74.96  ? 4094 VAL A CA    1 
ATOM   20223 C  C     . VAL A 1 4094 ? 174.251 195.701 150.892 1.00 77.27  ? 4094 VAL A C     1 
ATOM   20224 O  O     . VAL A 1 4094 ? 173.192 195.667 151.528 1.00 81.03  ? 4094 VAL A O     1 
ATOM   20225 C  CB    . VAL A 1 4094 ? 176.104 195.046 152.459 1.00 71.60  ? 4094 VAL A CB    1 
ATOM   20226 C  CG1   . VAL A 1 4094 ? 176.643 193.901 151.618 1.00 77.30  ? 4094 VAL A CG1   1 
ATOM   20227 C  CG2   . VAL A 1 4094 ? 177.180 195.590 153.361 1.00 84.34  ? 4094 VAL A CG2   1 
ATOM   20228 N  N     . MET A 1 4095 ? 174.341 195.382 149.606 1.00 78.13  ? 4095 MET A N     1 
ATOM   20229 C  CA    . MET A 1 4095 ? 173.290 194.708 148.858 1.00 74.95  ? 4095 MET A CA    1 
ATOM   20230 C  C     . MET A 1 4095 ? 173.717 193.278 148.580 1.00 72.29  ? 4095 MET A C     1 
ATOM   20231 O  O     . MET A 1 4095 ? 174.819 193.047 148.077 1.00 80.83  ? 4095 MET A O     1 
ATOM   20232 C  CB    . MET A 1 4095 ? 173.005 195.420 147.536 1.00 81.65  ? 4095 MET A CB    1 
ATOM   20233 C  CG    . MET A 1 4095 ? 171.856 194.812 146.757 1.00 81.13  ? 4095 MET A CG    1 
ATOM   20234 S  SD    . MET A 1 4095 ? 170.282 194.926 147.600 1.00 92.49  ? 4095 MET A SD    1 
ATOM   20235 C  CE    . MET A 1 4095 ? 169.982 196.667 147.400 1.00 91.07  ? 4095 MET A CE    1 
ATOM   20236 N  N     . LEU A 1 4096 ? 172.841 192.328 148.884 1.00 64.07  ? 4096 LEU A N     1 
ATOM   20237 C  CA    . LEU A 1 4096 ? 173.070 190.918 148.587 1.00 66.00  ? 4096 LEU A CA    1 
ATOM   20238 C  C     . LEU A 1 4096 ? 171.908 190.450 147.718 1.00 69.75  ? 4096 LEU A C     1 
ATOM   20239 O  O     . LEU A 1 4096 ? 170.781 190.283 148.201 1.00 75.58  ? 4096 LEU A O     1 
ATOM   20240 C  CB    . LEU A 1 4096 ? 173.206 190.107 149.870 1.00 60.89  ? 4096 LEU A CB    1 
ATOM   20241 C  CG    . LEU A 1 4096 ? 174.343 190.547 150.794 1.00 61.69  ? 4096 LEU A CG    1 
ATOM   20242 C  CD1   . LEU A 1 4096 ? 174.509 189.582 151.945 1.00 63.38  ? 4096 LEU A CD1   1 
ATOM   20243 C  CD2   . LEU A 1 4096 ? 175.640 190.660 150.020 1.00 69.52  ? 4096 LEU A CD2   1 
ATOM   20244 N  N     . LYS A 1 4097 ? 172.190 190.247 146.434 1.00 69.39  ? 4097 LYS A N     1 
ATOM   20245 C  CA    . LYS A 1 4097 ? 171.152 189.962 145.458 1.00 67.01  ? 4097 LYS A CA    1 
ATOM   20246 C  C     . LYS A 1 4097 ? 170.902 188.466 145.343 1.00 68.23  ? 4097 LYS A C     1 
ATOM   20247 O  O     . LYS A 1 4097 ? 171.835 187.660 145.375 1.00 77.67  ? 4097 LYS A O     1 
ATOM   20248 C  CB    . LYS A 1 4097 ? 171.541 190.524 144.092 1.00 71.03  ? 4097 LYS A CB    1 
ATOM   20249 C  CG    . LYS A 1 4097 ? 171.903 191.997 144.095 1.00 77.37  ? 4097 LYS A CG    1 
ATOM   20250 C  CD    . LYS A 1 4097 ? 171.892 192.553 142.682 1.00 85.06  ? 4097 LYS A CD    1 
ATOM   20251 C  CE    . LYS A 1 4097 ? 171.915 194.070 142.674 1.00 89.36  ? 4097 LYS A CE    1 
ATOM   20252 N  NZ    . LYS A 1 4097 ? 173.203 194.595 142.148 1.00 93.00  ? 4097 LYS A NZ    1 
ATOM   20253 N  N     . ASN A 1 4098 ? 169.627 188.105 145.203 1.00 62.97  ? 4098 ASN A N     1 
ATOM   20254 C  CA    . ASN A 1 4098 ? 169.207 186.730 144.941 1.00 62.95  ? 4098 ASN A CA    1 
ATOM   20255 C  C     . ASN A 1 4098 ? 169.756 185.767 145.990 1.00 65.48  ? 4098 ASN A C     1 
ATOM   20256 O  O     . ASN A 1 4098 ? 170.267 184.690 145.679 1.00 68.45  ? 4098 ASN A O     1 
ATOM   20257 C  CB    . ASN A 1 4098 ? 169.618 186.302 143.533 1.00 67.86  ? 4098 ASN A CB    1 
ATOM   20258 C  CG    . ASN A 1 4098 ? 169.330 187.368 142.496 1.00 74.56  ? 4098 ASN A CG    1 
ATOM   20259 O  OD1   . ASN A 1 4098 ? 168.418 188.178 142.661 1.00 71.13  ? 4098 ASN A OD1   1 
ATOM   20260 N  ND2   . ASN A 1 4098 ? 170.110 187.377 141.423 1.00 80.07  ? 4098 ASN A ND2   1 
ATOM   20261 N  N     . VAL A 1 4099 ? 169.639 186.162 147.260 1.00 63.48  ? 4099 VAL A N     1 
ATOM   20262 C  CA    . VAL A 1 4099 ? 170.117 185.316 148.347 1.00 68.26  ? 4099 VAL A CA    1 
ATOM   20263 C  C     . VAL A 1 4099 ? 169.208 184.129 148.616 1.00 66.40  ? 4099 VAL A C     1 
ATOM   20264 O  O     . VAL A 1 4099 ? 169.518 183.313 149.489 1.00 76.32  ? 4099 VAL A O     1 
ATOM   20265 C  CB    . VAL A 1 4099 ? 170.302 186.129 149.644 1.00 67.55  ? 4099 VAL A CB    1 
ATOM   20266 C  CG1   . VAL A 1 4099 ? 171.341 187.198 149.445 1.00 66.28  ? 4099 VAL A CG1   1 
ATOM   20267 C  CG2   . VAL A 1 4099 ? 169.001 186.745 150.079 1.00 63.26  ? 4099 VAL A CG2   1 
ATOM   20268 N  N     . HIS A 1 4100 ? 168.095 184.006 147.892 1.00 60.87  ? 4100 HIS A N     1 
ATOM   20269 C  CA    . HIS A 1 4100 ? 167.278 182.804 147.991 1.00 66.66  ? 4100 HIS A CA    1 
ATOM   20270 C  C     . HIS A 1 4100 ? 167.982 181.580 147.426 1.00 76.27  ? 4100 HIS A C     1 
ATOM   20271 O  O     . HIS A 1 4100 ? 167.513 180.457 147.645 1.00 79.26  ? 4100 HIS A O     1 
ATOM   20272 C  CB    . HIS A 1 4100 ? 165.944 183.005 147.271 1.00 65.03  ? 4100 HIS A CB    1 
ATOM   20273 C  CG    . HIS A 1 4100 ? 166.083 183.337 145.817 1.00 63.22  ? 4100 HIS A CG    1 
ATOM   20274 N  ND1   . HIS A 1 4100 ? 166.612 184.528 145.370 1.00 68.41  ? 4100 HIS A ND1   1 
ATOM   20275 C  CD2   . HIS A 1 4100 ? 165.767 182.627 144.709 1.00 64.29  ? 4100 HIS A CD2   1 
ATOM   20276 C  CE1   . HIS A 1 4100 ? 166.610 184.541 144.050 1.00 64.58  ? 4100 HIS A CE1   1 
ATOM   20277 N  NE2   . HIS A 1 4100 ? 166.103 183.399 143.623 1.00 64.04  ? 4100 HIS A NE2   1 
ATOM   20278 N  N     . LEU A 1 4101 ? 169.087 181.771 146.707 1.00 70.83  ? 4101 LEU A N     1 
ATOM   20279 C  CA    . LEU A 1 4101 ? 169.844 180.679 146.115 1.00 68.93  ? 4101 LEU A CA    1 
ATOM   20280 C  C     . LEU A 1 4101 ? 170.695 179.926 147.129 1.00 74.94  ? 4101 LEU A C     1 
ATOM   20281 O  O     . LEU A 1 4101 ? 171.129 178.807 146.835 1.00 78.32  ? 4101 LEU A O     1 
ATOM   20282 C  CB    . LEU A 1 4101 ? 170.737 181.223 144.997 1.00 67.78  ? 4101 LEU A CB    1 
ATOM   20283 C  CG    . LEU A 1 4101 ? 170.022 181.948 143.854 1.00 64.35  ? 4101 LEU A CG    1 
ATOM   20284 C  CD1   . LEU A 1 4101 ? 170.965 182.197 142.692 1.00 59.35  ? 4101 LEU A CD1   1 
ATOM   20285 C  CD2   . LEU A 1 4101 ? 168.811 181.162 143.396 1.00 62.40  ? 4101 LEU A CD2   1 
ATOM   20286 N  N     . ALA A 1 4102 ? 170.946 180.505 148.303 1.00 76.87  ? 4102 ALA A N     1 
ATOM   20287 C  CA    . ALA A 1 4102 ? 171.794 179.901 149.331 1.00 77.41  ? 4102 ALA A CA    1 
ATOM   20288 C  C     . ALA A 1 4102 ? 171.076 179.954 150.673 1.00 78.81  ? 4102 ALA A C     1 
ATOM   20289 O  O     . ALA A 1 4102 ? 171.298 180.871 151.473 1.00 85.49  ? 4102 ALA A O     1 
ATOM   20290 C  CB    . ALA A 1 4102 ? 173.150 180.604 149.404 1.00 76.78  ? 4102 ALA A CB    1 
ATOM   20291 N  N     . PRO A 1 4103 ? 170.200 178.983 150.951 1.00 76.06  ? 4103 PRO A N     1 
ATOM   20292 C  CA    . PRO A 1 4103 ? 169.468 179.014 152.231 1.00 83.00  ? 4103 PRO A CA    1 
ATOM   20293 C  C     . PRO A 1 4103 ? 170.351 178.794 153.449 1.00 90.29  ? 4103 PRO A C     1 
ATOM   20294 O  O     . PRO A 1 4103 ? 170.204 179.510 154.450 1.00 91.89  ? 4103 PRO A O     1 
ATOM   20295 C  CB    . PRO A 1 4103 ? 168.435 177.889 152.066 1.00 81.38  ? 4103 PRO A CB    1 
ATOM   20296 C  CG    . PRO A 1 4103 ? 168.336 177.666 150.586 1.00 79.21  ? 4103 PRO A CG    1 
ATOM   20297 C  CD    . PRO A 1 4103 ? 169.709 177.922 150.059 1.00 77.47  ? 4103 PRO A CD    1 
ATOM   20298 N  N     . GLY A 1 4104 ? 171.250 177.808 153.408 1.00 86.21  ? 4104 GLY A N     1 
ATOM   20299 C  CA    . GLY A 1 4104 ? 172.126 177.577 154.546 1.00 86.10  ? 4104 GLY A CA    1 
ATOM   20300 C  C     . GLY A 1 4104 ? 173.041 178.754 154.819 1.00 86.20  ? 4104 GLY A C     1 
ATOM   20301 O  O     . GLY A 1 4104 ? 173.299 179.104 155.976 1.00 87.65  ? 4104 GLY A O     1 
ATOM   20302 N  N     . TRP A 1 4105 ? 173.546 179.382 153.756 1.00 81.35  ? 4105 TRP A N     1 
ATOM   20303 C  CA    . TRP A 1 4105 ? 174.329 180.596 153.929 1.00 81.11  ? 4105 TRP A CA    1 
ATOM   20304 C  C     . TRP A 1 4105 ? 173.481 181.711 154.524 1.00 85.19  ? 4105 TRP A C     1 
ATOM   20305 O  O     . TRP A 1 4105 ? 173.995 182.547 155.271 1.00 87.70  ? 4105 TRP A O     1 
ATOM   20306 C  CB    . TRP A 1 4105 ? 174.933 181.020 152.591 1.00 84.53  ? 4105 TRP A CB    1 
ATOM   20307 C  CG    . TRP A 1 4105 ? 175.831 182.210 152.679 1.00 88.99  ? 4105 TRP A CG    1 
ATOM   20308 C  CD1   . TRP A 1 4105 ? 177.187 182.198 152.816 1.00 93.45  ? 4105 TRP A CD1   1 
ATOM   20309 C  CD2   . TRP A 1 4105 ? 175.445 183.586 152.622 1.00 93.81  ? 4105 TRP A CD2   1 
ATOM   20310 N  NE1   . TRP A 1 4105 ? 177.670 183.482 152.857 1.00 97.30  ? 4105 TRP A NE1   1 
ATOM   20311 C  CE2   . TRP A 1 4105 ? 176.621 184.353 152.738 1.00 96.93  ? 4105 TRP A CE2   1 
ATOM   20312 C  CE3   . TRP A 1 4105 ? 174.221 184.246 152.487 1.00 93.50  ? 4105 TRP A CE3   1 
ATOM   20313 C  CZ2   . TRP A 1 4105 ? 176.607 185.743 152.724 1.00 96.52  ? 4105 TRP A CZ2   1 
ATOM   20314 C  CZ3   . TRP A 1 4105 ? 174.210 185.625 152.474 1.00 90.49  ? 4105 TRP A CZ3   1 
ATOM   20315 C  CH2   . TRP A 1 4105 ? 175.395 186.358 152.593 1.00 92.92  ? 4105 TRP A CH2   1 
ATOM   20316 N  N     . LEU A 1 4106 ? 172.179 181.729 154.222 1.00 86.18  ? 4106 LEU A N     1 
ATOM   20317 C  CA    . LEU A 1 4106 ? 171.282 182.690 154.859 1.00 82.74  ? 4106 LEU A CA    1 
ATOM   20318 C  C     . LEU A 1 4106 ? 171.142 182.419 156.351 1.00 87.14  ? 4106 LEU A C     1 
ATOM   20319 O  O     . LEU A 1 4106 ? 171.110 183.357 157.155 1.00 93.47  ? 4106 LEU A O     1 
ATOM   20320 C  CB    . LEU A 1 4106 ? 169.912 182.665 154.182 1.00 75.48  ? 4106 LEU A CB    1 
ATOM   20321 C  CG    . LEU A 1 4106 ? 169.814 183.395 152.846 1.00 72.35  ? 4106 LEU A CG    1 
ATOM   20322 C  CD1   . LEU A 1 4106 ? 168.363 183.596 152.458 1.00 72.14  ? 4106 LEU A CD1   1 
ATOM   20323 C  CD2   . LEU A 1 4106 ? 170.535 184.725 152.938 1.00 74.57  ? 4106 LEU A CD2   1 
ATOM   20324 N  N     . MET A 1 4107 ? 171.041 181.146 156.742 1.00 86.05  ? 4107 MET A N     1 
ATOM   20325 C  CA    . MET A 1 4107 ? 171.005 180.824 158.167 1.00 88.60  ? 4107 MET A CA    1 
ATOM   20326 C  C     . MET A 1 4107 ? 172.288 181.270 158.858 1.00 92.28  ? 4107 MET A C     1 
ATOM   20327 O  O     . MET A 1 4107 ? 172.252 181.841 159.958 1.00 93.74  ? 4107 MET A O     1 
ATOM   20328 C  CB    . MET A 1 4107 ? 170.790 179.325 158.367 1.00 87.39  ? 4107 MET A CB    1 
ATOM   20329 C  CG    . MET A 1 4107 ? 169.430 178.820 157.931 1.00 89.71  ? 4107 MET A CG    1 
ATOM   20330 S  SD    . MET A 1 4107 ? 169.238 177.046 158.183 1.00 98.55  ? 4107 MET A SD    1 
ATOM   20331 C  CE    . MET A 1 4107 ? 167.609 176.781 157.490 1.00 91.02  ? 4107 MET A CE    1 
ATOM   20332 N  N     . GLN A 1 4108 ? 173.433 181.017 158.222 1.00 93.28  ? 4108 GLN A N     1 
ATOM   20333 C  CA    . GLN A 1 4108 ? 174.706 181.446 158.793 1.00 93.26  ? 4108 GLN A CA    1 
ATOM   20334 C  C     . GLN A 1 4108 ? 174.780 182.965 158.896 1.00 94.24  ? 4108 GLN A C     1 
ATOM   20335 O  O     . GLN A 1 4108 ? 175.300 183.503 159.880 1.00 96.82  ? 4108 GLN A O     1 
ATOM   20336 C  CB    . GLN A 1 4108 ? 175.865 180.902 157.961 1.00 90.45  ? 4108 GLN A CB    1 
ATOM   20337 C  CG    . GLN A 1 4108 ? 175.950 179.387 157.959 1.00 93.14  ? 4108 GLN A CG    1 
ATOM   20338 C  CD    . GLN A 1 4108 ? 176.281 178.823 159.327 1.00 99.99  ? 4108 GLN A CD    1 
ATOM   20339 O  OE1   . GLN A 1 4108 ? 177.089 179.387 160.065 1.00 99.08  ? 4108 GLN A OE1   1 
ATOM   20340 N  NE2   . GLN A 1 4108 ? 175.654 177.705 159.674 1.00 100.26 ? 4108 GLN A NE2   1 
ATOM   20341 N  N     . LEU A 1 4109 ? 174.264 183.672 157.889 1.00 89.83  ? 4109 LEU A N     1 
ATOM   20342 C  CA    . LEU A 1 4109 ? 174.240 185.130 157.937 1.00 86.13  ? 4109 LEU A CA    1 
ATOM   20343 C  C     . LEU A 1 4109 ? 173.355 185.632 159.069 1.00 89.77  ? 4109 LEU A C     1 
ATOM   20344 O  O     . LEU A 1 4109 ? 173.697 186.606 159.745 1.00 96.38  ? 4109 LEU A O     1 
ATOM   20345 C  CB    . LEU A 1 4109 ? 173.764 185.693 156.599 1.00 83.93  ? 4109 LEU A CB    1 
ATOM   20346 C  CG    . LEU A 1 4109 ? 173.542 187.206 156.557 1.00 80.21  ? 4109 LEU A CG    1 
ATOM   20347 C  CD1   . LEU A 1 4109 ? 174.816 187.945 156.926 1.00 81.41  ? 4109 LEU A CD1   1 
ATOM   20348 C  CD2   . LEU A 1 4109 ? 173.046 187.640 155.190 1.00 81.58  ? 4109 LEU A CD2   1 
ATOM   20349 N  N     . GLU A 1 4110 ? 172.204 184.991 159.279 1.00 87.53  ? 4110 GLU A N     1 
ATOM   20350 C  CA    . GLU A 1 4110 ? 171.335 185.392 160.381 1.00 89.19  ? 4110 GLU A CA    1 
ATOM   20351 C  C     . GLU A 1 4110 ? 172.027 185.188 161.723 1.00 95.07  ? 4110 GLU A C     1 
ATOM   20352 O  O     . GLU A 1 4110 ? 171.965 186.056 162.605 1.00 95.93  ? 4110 GLU A O     1 
ATOM   20353 C  CB    . GLU A 1 4110 ? 170.021 184.611 160.321 1.00 83.27  ? 4110 GLU A CB    1 
ATOM   20354 C  CG    . GLU A 1 4110 ? 168.895 185.198 161.160 1.00 83.30  ? 4110 GLU A CG    1 
ATOM   20355 C  CD    . GLU A 1 4110 ? 169.002 184.840 162.628 1.00 89.61  ? 4110 GLU A CD    1 
ATOM   20356 O  OE1   . GLU A 1 4110 ? 168.963 183.635 162.953 1.00 86.21  ? 4110 GLU A OE1   1 
ATOM   20357 O  OE2   . GLU A 1 4110 ? 169.125 185.765 163.458 1.00 95.51  ? 4110 GLU A OE2   1 
ATOM   20358 N  N     . LYS A 1 4111 ? 172.701 184.047 161.890 1.00 95.54  ? 4111 LYS A N     1 
ATOM   20359 C  CA    . LYS A 1 4111 ? 173.435 183.803 163.129 1.00 93.40  ? 4111 LYS A CA    1 
ATOM   20360 C  C     . LYS A 1 4111 ? 174.553 184.822 163.318 1.00 94.17  ? 4111 LYS A C     1 
ATOM   20361 O  O     . LYS A 1 4111 ? 174.800 185.283 164.438 1.00 96.82  ? 4111 LYS A O     1 
ATOM   20362 C  CB    . LYS A 1 4111 ? 173.995 182.381 163.139 1.00 94.67  ? 4111 LYS A CB    1 
ATOM   20363 C  CG    . LYS A 1 4111 ? 172.933 181.297 163.119 1.00 102.19 ? 4111 LYS A CG    1 
ATOM   20364 C  CD    . LYS A 1 4111 ? 172.483 180.944 164.527 1.00 103.85 ? 4111 LYS A CD    1 
ATOM   20365 C  CE    . LYS A 1 4111 ? 172.101 179.476 164.634 1.00 106.64 ? 4111 LYS A CE    1 
ATOM   20366 N  NZ    . LYS A 1 4111 ? 171.408 178.992 163.409 1.00 107.92 ? 4111 LYS A NZ    1 
ATOM   20367 N  N     . LYS A 1 4112 ? 175.245 185.179 162.235 1.00 93.81  ? 4112 LYS A N     1 
ATOM   20368 C  CA    . LYS A 1 4112 ? 176.304 186.179 162.322 1.00 91.53  ? 4112 LYS A CA    1 
ATOM   20369 C  C     . LYS A 1 4112 ? 175.747 187.544 162.708 1.00 92.93  ? 4112 LYS A C     1 
ATOM   20370 O  O     . LYS A 1 4112 ? 176.337 188.254 163.530 1.00 99.39  ? 4112 LYS A O     1 
ATOM   20371 C  CB    . LYS A 1 4112 ? 177.052 186.259 160.992 1.00 90.17  ? 4112 LYS A CB    1 
ATOM   20372 C  CG    . LYS A 1 4112 ? 178.236 187.209 160.989 1.00 93.58  ? 4112 LYS A CG    1 
ATOM   20373 C  CD    . LYS A 1 4112 ? 178.283 188.019 159.705 1.00 95.73  ? 4112 LYS A CD    1 
ATOM   20374 C  CE    . LYS A 1 4112 ? 179.601 188.762 159.566 1.00 98.92  ? 4112 LYS A CE    1 
ATOM   20375 N  NZ    . LYS A 1 4112 ? 179.862 189.660 160.724 1.00 99.89  ? 4112 LYS A NZ    1 
ATOM   20376 N  N     . LEU A 1 4113 ? 174.611 187.928 162.122 1.00 92.79  ? 4113 LEU A N     1 
ATOM   20377 C  CA    . LEU A 1 4113 ? 174.019 189.229 162.418 1.00 94.60  ? 4113 LEU A CA    1 
ATOM   20378 C  C     . LEU A 1 4113 ? 173.477 189.298 163.838 1.00 97.61  ? 4113 LEU A C     1 
ATOM   20379 O  O     . LEU A 1 4113 ? 173.466 190.378 164.440 1.00 95.07  ? 4113 LEU A O     1 
ATOM   20380 C  CB    . LEU A 1 4113 ? 172.901 189.543 161.425 1.00 89.36  ? 4113 LEU A CB    1 
ATOM   20381 C  CG    . LEU A 1 4113 ? 173.278 189.752 159.961 1.00 89.03  ? 4113 LEU A CG    1 
ATOM   20382 C  CD1   . LEU A 1 4113 ? 172.021 189.908 159.129 1.00 81.08  ? 4113 LEU A CD1   1 
ATOM   20383 C  CD2   . LEU A 1 4113 ? 174.180 190.964 159.808 1.00 90.53  ? 4113 LEU A CD2   1 
ATOM   20384 N  N     . HIS A 1 4114 ? 173.009 188.172 164.383 1.00 99.77  ? 4114 HIS A N     1 
ATOM   20385 C  CA    . HIS A 1 4114 ? 172.443 188.191 165.728 1.00 101.35 ? 4114 HIS A CA    1 
ATOM   20386 C  C     . HIS A 1 4114 ? 173.469 188.651 166.758 1.00 104.94 ? 4114 HIS A C     1 
ATOM   20387 O  O     . HIS A 1 4114 ? 173.163 189.466 167.636 1.00 105.06 ? 4114 HIS A O     1 
ATOM   20388 C  CB    . HIS A 1 4114 ? 171.900 186.810 166.090 1.00 100.59 ? 4114 HIS A CB    1 
ATOM   20389 C  CG    . HIS A 1 4114 ? 171.269 186.751 167.445 1.00 106.22 ? 4114 HIS A CG    1 
ATOM   20390 N  ND1   . HIS A 1 4114 ? 170.036 187.304 167.717 1.00 107.34 ? 4114 HIS A ND1   1 
ATOM   20391 C  CD2   . HIS A 1 4114 ? 171.702 186.207 168.608 1.00 108.16 ? 4114 HIS A CD2   1 
ATOM   20392 C  CE1   . HIS A 1 4114 ? 169.736 187.103 168.987 1.00 105.54 ? 4114 HIS A CE1   1 
ATOM   20393 N  NE2   . HIS A 1 4114 ? 170.730 186.439 169.550 1.00 112.16 ? 4114 HIS A NE2   1 
ATOM   20394 N  N     . SER A 1 4115 ? 174.698 188.138 166.668 1.00 104.35 ? 4115 SER A N     1 
ATOM   20395 C  CA    . SER A 1 4115 ? 175.728 188.501 167.636 1.00 103.17 ? 4115 SER A CA    1 
ATOM   20396 C  C     . SER A 1 4115 ? 176.440 189.796 167.267 1.00 99.75  ? 4115 SER A C     1 
ATOM   20397 O  O     . SER A 1 4115 ? 176.964 190.482 168.151 1.00 98.87  ? 4115 SER A O     1 
ATOM   20398 C  CB    . SER A 1 4115 ? 176.744 187.366 167.768 1.00 102.52 ? 4115 SER A CB    1 
ATOM   20399 O  OG    . SER A 1 4115 ? 177.376 187.101 166.528 1.00 99.37  ? 4115 SER A OG    1 
ATOM   20400 N  N     . LEU A 1 4116 ? 176.472 190.139 165.983 1.00 99.94  ? 4116 LEU A N     1 
ATOM   20401 C  CA    . LEU A 1 4116 ? 177.201 191.313 165.524 1.00 99.69  ? 4116 LEU A CA    1 
ATOM   20402 C  C     . LEU A 1 4116 ? 176.572 192.594 166.061 1.00 102.51 ? 4116 LEU A C     1 
ATOM   20403 O  O     . LEU A 1 4116 ? 175.354 192.682 166.237 1.00 106.80 ? 4116 LEU A O     1 
ATOM   20404 C  CB    . LEU A 1 4116 ? 177.228 191.335 163.996 1.00 100.94 ? 4116 LEU A CB    1 
ATOM   20405 C  CG    . LEU A 1 4116 ? 178.195 192.265 163.266 1.00 102.94 ? 4116 LEU A CG    1 
ATOM   20406 C  CD1   . LEU A 1 4116 ? 179.623 191.766 163.398 1.00 97.54  ? 4116 LEU A CD1   1 
ATOM   20407 C  CD2   . LEU A 1 4116 ? 177.794 192.355 161.804 1.00 99.48  ? 4116 LEU A CD2   1 
ATOM   20408 N  N     . GLN A 1 4117 ? 177.414 193.592 166.324 1.00 99.85  ? 4117 GLN A N     1 
ATOM   20409 C  CA    . GLN A 1 4117 ? 176.966 194.906 166.789 1.00 98.98  ? 4117 GLN A CA    1 
ATOM   20410 C  C     . GLN A 1 4117 ? 177.357 195.954 165.758 1.00 97.75  ? 4117 GLN A C     1 
ATOM   20411 O  O     . GLN A 1 4117 ? 178.477 196.494 165.808 1.00 97.40  ? 4117 GLN A O     1 
ATOM   20412 C  CB    . GLN A 1 4117 ? 177.564 195.241 168.153 1.00 101.00 ? 4117 GLN A CB    1 
ATOM   20413 C  CG    . GLN A 1 4117 ? 177.087 194.338 169.277 1.00 105.32 ? 4117 GLN A CG    1 
ATOM   20414 C  CD    . GLN A 1 4117 ? 177.748 194.660 170.602 1.00 112.73 ? 4117 GLN A CD    1 
ATOM   20415 O  OE1   . GLN A 1 4117 ? 178.631 195.514 170.676 1.00 111.06 ? 4117 GLN A OE1   1 
ATOM   20416 N  NE2   . GLN A 1 4117 ? 177.319 193.979 171.658 1.00 113.16 ? 4117 GLN A NE2   1 
ATOM   20417 N  N     . PRO A 1 4118 ? 176.480 196.275 164.815 1.00 95.51  ? 4118 PRO A N     1 
ATOM   20418 C  CA    . PRO A 1 4118 ? 176.858 197.148 163.701 1.00 93.98  ? 4118 PRO A CA    1 
ATOM   20419 C  C     . PRO A 1 4118 ? 176.994 198.609 164.111 1.00 96.61  ? 4118 PRO A C     1 
ATOM   20420 O  O     . PRO A 1 4118 ? 176.575 199.037 165.186 1.00 95.90  ? 4118 PRO A O     1 
ATOM   20421 C  CB    . PRO A 1 4118 ? 175.703 196.970 162.713 1.00 93.63  ? 4118 PRO A CB    1 
ATOM   20422 C  CG    . PRO A 1 4118 ? 175.124 195.640 163.040 1.00 96.52  ? 4118 PRO A CG    1 
ATOM   20423 C  CD    . PRO A 1 4118 ? 175.247 195.523 164.529 1.00 95.76  ? 4118 PRO A CD    1 
ATOM   20424 N  N     . HIS A 1 4119 ? 177.603 199.373 163.208 1.00 95.42  ? 4119 HIS A N     1 
ATOM   20425 C  CA    . HIS A 1 4119 ? 177.622 200.821 163.313 1.00 94.54  ? 4119 HIS A CA    1 
ATOM   20426 C  C     . HIS A 1 4119 ? 176.226 201.375 163.042 1.00 96.26  ? 4119 HIS A C     1 
ATOM   20427 O  O     . HIS A 1 4119 ? 175.390 200.733 162.401 1.00 101.68 ? 4119 HIS A O     1 
ATOM   20428 C  CB    . HIS A 1 4119 ? 178.638 201.410 162.331 1.00 94.59  ? 4119 HIS A CB    1 
ATOM   20429 C  CG    . HIS A 1 4119 ? 178.710 202.905 162.349 1.00 101.53 ? 4119 HIS A CG    1 
ATOM   20430 N  ND1   . HIS A 1 4119 ? 178.334 203.681 161.274 1.00 103.93 ? 4119 HIS A ND1   1 
ATOM   20431 C  CD2   . HIS A 1 4119 ? 179.121 203.767 163.309 1.00 104.86 ? 4119 HIS A CD2   1 
ATOM   20432 C  CE1   . HIS A 1 4119 ? 178.505 204.956 161.572 1.00 103.05 ? 4119 HIS A CE1   1 
ATOM   20433 N  NE2   . HIS A 1 4119 ? 178.982 205.036 162.801 1.00 104.86 ? 4119 HIS A NE2   1 
ATOM   20434 N  N     . ALA A 1 4120 ? 175.976 202.587 163.544 1.00 93.66  ? 4120 ALA A N     1 
ATOM   20435 C  CA    . ALA A 1 4120 ? 174.644 203.175 163.449 1.00 95.95  ? 4120 ALA A CA    1 
ATOM   20436 C  C     . ALA A 1 4120 ? 174.181 203.367 162.011 1.00 97.10  ? 4120 ALA A C     1 
ATOM   20437 O  O     . ALA A 1 4120 ? 172.971 203.425 161.768 1.00 93.94  ? 4120 ALA A O     1 
ATOM   20438 C  CB    . ALA A 1 4120 ? 174.611 204.515 164.185 1.00 98.39  ? 4120 ALA A CB    1 
ATOM   20439 N  N     . CYS A 1 4121 ? 175.102 203.468 161.055 1.00 97.59  ? 4121 CYS A N     1 
ATOM   20440 C  CA    . CYS A 1 4121 ? 174.749 203.687 159.659 1.00 95.15  ? 4121 CYS A CA    1 
ATOM   20441 C  C     . CYS A 1 4121 ? 174.824 202.424 158.809 1.00 91.93  ? 4121 CYS A C     1 
ATOM   20442 O  O     . CYS A 1 4121 ? 174.636 202.506 157.592 1.00 89.55  ? 4121 CYS A O     1 
ATOM   20443 C  CB    . CYS A 1 4121 ? 175.648 204.768 159.051 1.00 100.41 ? 4121 CYS A CB    1 
ATOM   20444 S  SG    . CYS A 1 4121 ? 175.319 206.438 159.657 1.00 120.19 ? 4121 CYS A SG    1 
ATOM   20445 N  N     . PHE A 1 4122 ? 175.095 201.268 159.408 1.00 91.20  ? 4122 PHE A N     1 
ATOM   20446 C  CA    . PHE A 1 4122 ? 175.165 200.032 158.639 1.00 83.85  ? 4122 PHE A CA    1 
ATOM   20447 C  C     . PHE A 1 4122 ? 173.770 199.589 158.222 1.00 86.08  ? 4122 PHE A C     1 
ATOM   20448 O  O     . PHE A 1 4122 ? 172.838 199.592 159.032 1.00 89.68  ? 4122 PHE A O     1 
ATOM   20449 C  CB    . PHE A 1 4122 ? 175.838 198.930 159.452 1.00 83.84  ? 4122 PHE A CB    1 
ATOM   20450 C  CG    . PHE A 1 4122 ? 175.811 197.586 158.782 1.00 82.18  ? 4122 PHE A CG    1 
ATOM   20451 C  CD1   . PHE A 1 4122 ? 176.432 197.393 157.562 1.00 83.34  ? 4122 PHE A CD1   1 
ATOM   20452 C  CD2   . PHE A 1 4122 ? 175.155 196.517 159.367 1.00 79.93  ? 4122 PHE A CD2   1 
ATOM   20453 C  CE1   . PHE A 1 4122 ? 176.407 196.160 156.944 1.00 76.28  ? 4122 PHE A CE1   1 
ATOM   20454 C  CE2   . PHE A 1 4122 ? 175.128 195.282 158.754 1.00 74.04  ? 4122 PHE A CE2   1 
ATOM   20455 C  CZ    . PHE A 1 4122 ? 175.754 195.104 157.541 1.00 70.77  ? 4122 PHE A CZ    1 
ATOM   20456 N  N     . ARG A 1 4123 ? 173.627 199.203 156.955 1.00 84.35  ? 4123 ARG A N     1 
ATOM   20457 C  CA    . ARG A 1 4123 ? 172.368 198.680 156.441 1.00 77.96  ? 4123 ARG A CA    1 
ATOM   20458 C  C     . ARG A 1 4123 ? 172.654 197.532 155.487 1.00 72.56  ? 4123 ARG A C     1 
ATOM   20459 O  O     . ARG A 1 4123 ? 173.383 197.701 154.505 1.00 75.05  ? 4123 ARG A O     1 
ATOM   20460 C  CB    . ARG A 1 4123 ? 171.557 199.768 155.728 1.00 76.99  ? 4123 ARG A CB    1 
ATOM   20461 C  CG    . ARG A 1 4123 ? 170.968 200.818 156.654 1.00 79.80  ? 4123 ARG A CG    1 
ATOM   20462 C  CD    . ARG A 1 4123 ? 169.991 200.203 157.644 1.00 83.65  ? 4123 ARG A CD    1 
ATOM   20463 N  NE    . ARG A 1 4123 ? 169.446 201.191 158.567 1.00 85.96  ? 4123 ARG A NE    1 
ATOM   20464 C  CZ    . ARG A 1 4123 ? 170.131 201.766 159.547 1.00 86.05  ? 4123 ARG A CZ    1 
ATOM   20465 N  NH1   . ARG A 1 4123 ? 171.395 201.457 159.781 1.00 87.66  ? 4123 ARG A NH1   1 
ATOM   20466 N  NH2   . ARG A 1 4123 ? 169.529 202.669 160.316 1.00 82.31  ? 4123 ARG A NH2   1 
ATOM   20467 N  N     . LEU A 1 4124 ? 172.067 196.375 155.778 1.00 64.45  ? 4124 LEU A N     1 
ATOM   20468 C  CA    . LEU A 1 4124 ? 172.190 195.180 154.955 1.00 59.54  ? 4124 LEU A CA    1 
ATOM   20469 C  C     . LEU A 1 4124 ? 170.845 194.900 154.301 1.00 63.12  ? 4124 LEU A C     1 
ATOM   20470 O  O     . LEU A 1 4124 ? 169.840 194.744 154.999 1.00 68.02  ? 4124 LEU A O     1 
ATOM   20471 C  CB    . LEU A 1 4124 ? 172.632 193.985 155.799 1.00 57.65  ? 4124 LEU A CB    1 
ATOM   20472 C  CG    . LEU A 1 4124 ? 172.856 192.659 155.073 1.00 56.09  ? 4124 LEU A CG    1 
ATOM   20473 C  CD1   . LEU A 1 4124 ? 174.081 192.715 154.188 1.00 62.91  ? 4124 LEU A CD1   1 
ATOM   20474 C  CD2   . LEU A 1 4124 ? 172.968 191.521 156.066 1.00 61.54  ? 4124 LEU A CD2   1 
ATOM   20475 N  N     . PHE A 1 4125 ? 170.831 194.834 152.972 1.00 60.62  ? 4125 PHE A N     1 
ATOM   20476 C  CA    . PHE A 1 4125 ? 169.637 194.519 152.201 1.00 57.76  ? 4125 PHE A CA    1 
ATOM   20477 C  C     . PHE A 1 4125 ? 169.840 193.177 151.515 1.00 60.65  ? 4125 PHE A C     1 
ATOM   20478 O  O     . PHE A 1 4125 ? 170.901 192.932 150.934 1.00 68.26  ? 4125 PHE A O     1 
ATOM   20479 C  CB    . PHE A 1 4125 ? 169.344 195.601 151.159 1.00 63.97  ? 4125 PHE A CB    1 
ATOM   20480 C  CG    . PHE A 1 4125 ? 169.384 196.999 151.702 1.00 65.16  ? 4125 PHE A CG    1 
ATOM   20481 C  CD1   . PHE A 1 4125 ? 170.577 197.696 151.776 1.00 69.81  ? 4125 PHE A CD1   1 
ATOM   20482 C  CD2   . PHE A 1 4125 ? 168.224 197.625 152.119 1.00 67.86  ? 4125 PHE A CD2   1 
ATOM   20483 C  CE1   . PHE A 1 4125 ? 170.613 198.982 152.269 1.00 75.12  ? 4125 PHE A CE1   1 
ATOM   20484 C  CE2   . PHE A 1 4125 ? 168.255 198.912 152.613 1.00 71.15  ? 4125 PHE A CE2   1 
ATOM   20485 C  CZ    . PHE A 1 4125 ? 169.451 199.591 152.688 1.00 77.44  ? 4125 PHE A CZ    1 
ATOM   20486 N  N     . LEU A 1 4126 ? 168.834 192.311 151.596 1.00 55.33  ? 4126 LEU A N     1 
ATOM   20487 C  CA    . LEU A 1 4126 ? 168.874 190.987 150.985 1.00 51.67  ? 4126 LEU A CA    1 
ATOM   20488 C  C     . LEU A 1 4126 ? 167.669 190.844 150.071 1.00 55.32  ? 4126 LEU A C     1 
ATOM   20489 O  O     . LEU A 1 4126 ? 166.532 190.848 150.549 1.00 64.41  ? 4126 LEU A O     1 
ATOM   20490 C  CB    . LEU A 1 4126 ? 168.855 189.886 152.049 1.00 57.83  ? 4126 LEU A CB    1 
ATOM   20491 C  CG    . LEU A 1 4126 ? 169.724 190.022 153.297 1.00 55.53  ? 4126 LEU A CG    1 
ATOM   20492 C  CD1   . LEU A 1 4126 ? 169.672 188.741 154.105 1.00 48.40  ? 4126 LEU A CD1   1 
ATOM   20493 C  CD2   . LEU A 1 4126 ? 171.145 190.337 152.913 1.00 61.54  ? 4126 LEU A CD2   1 
ATOM   20494 N  N     . THR A 1 4127 ? 167.908 190.696 148.771 1.00 55.15  ? 4127 THR A N     1 
ATOM   20495 C  CA    . THR A 1 4127 ? 166.822 190.601 147.800 1.00 57.19  ? 4127 THR A CA    1 
ATOM   20496 C  C     . THR A 1 4127 ? 166.548 189.140 147.467 1.00 59.10  ? 4127 THR A C     1 
ATOM   20497 O  O     . THR A 1 4127 ? 167.481 188.352 147.292 1.00 66.31  ? 4127 THR A O     1 
ATOM   20498 C  CB    . THR A 1 4127 ? 167.136 191.384 146.525 1.00 58.85  ? 4127 THR A CB    1 
ATOM   20499 O  OG1   . THR A 1 4127 ? 168.181 190.729 145.802 1.00 65.02  ? 4127 THR A OG1   1 
ATOM   20500 C  CG2   . THR A 1 4127 ? 167.563 192.798 146.865 1.00 61.48  ? 4127 THR A CG2   1 
ATOM   20501 N  N     . MET A 1 4128 ? 165.266 188.788 147.392 1.00 57.16  ? 4128 MET A N     1 
ATOM   20502 C  CA    . MET A 1 4128 ? 164.827 187.409 147.199 1.00 57.04  ? 4128 MET A CA    1 
ATOM   20503 C  C     . MET A 1 4128 ? 163.645 187.407 146.237 1.00 64.44  ? 4128 MET A C     1 
ATOM   20504 O  O     . MET A 1 4128 ? 163.081 188.457 145.915 1.00 70.56  ? 4128 MET A O     1 
ATOM   20505 C  CB    . MET A 1 4128 ? 164.462 186.776 148.547 1.00 60.78  ? 4128 MET A CB    1 
ATOM   20506 C  CG    . MET A 1 4128 ? 165.638 186.602 149.469 1.00 70.61  ? 4128 MET A CG    1 
ATOM   20507 S  SD    . MET A 1 4128 ? 165.225 185.816 151.029 1.00 94.77  ? 4128 MET A SD    1 
ATOM   20508 C  CE    . MET A 1 4128 ? 164.379 187.161 151.850 1.00 69.09  ? 4128 MET A CE    1 
ATOM   20509 N  N     . GLU A 1 4129 ? 163.237 186.214 145.796 1.00 64.27  ? 4129 GLU A N     1 
ATOM   20510 C  CA    . GLU A 1 4129 ? 162.079 186.086 144.917 1.00 67.07  ? 4129 GLU A CA    1 
ATOM   20511 C  C     . GLU A 1 4129 ? 160.959 185.286 145.577 1.00 69.75  ? 4129 GLU A C     1 
ATOM   20512 O  O     . GLU A 1 4129 ? 160.153 184.656 144.886 1.00 80.76  ? 4129 GLU A O     1 
ATOM   20513 C  CB    . GLU A 1 4129 ? 162.461 185.464 143.572 1.00 64.91  ? 4129 GLU A CB    1 
ATOM   20514 C  CG    . GLU A 1 4129 ? 162.815 183.988 143.615 1.00 73.59  ? 4129 GLU A CG    1 
ATOM   20515 C  CD    . GLU A 1 4129 ? 163.010 183.402 142.231 1.00 81.69  ? 4129 GLU A CD    1 
ATOM   20516 O  OE1   . GLU A 1 4129 ? 162.869 184.154 141.243 1.00 83.43  ? 4129 GLU A OE1   1 
ATOM   20517 O  OE2   . GLU A 1 4129 ? 163.297 182.191 142.128 1.00 77.39  ? 4129 GLU A OE2   1 
ATOM   20518 N  N     . ILE A 1 4130 ? 160.880 185.325 146.908 1.00 59.05  ? 4130 ILE A N     1 
ATOM   20519 C  CA    . ILE A 1 4130 ? 159.836 184.641 147.669 1.00 58.38  ? 4130 ILE A CA    1 
ATOM   20520 C  C     . ILE A 1 4130 ? 159.887 183.142 147.401 1.00 65.26  ? 4130 ILE A C     1 
ATOM   20521 O  O     . ILE A 1 4130 ? 159.170 182.628 146.536 1.00 73.74  ? 4130 ILE A O     1 
ATOM   20522 C  CB    . ILE A 1 4130 ? 158.435 185.204 147.359 1.00 56.66  ? 4130 ILE A CB    1 
ATOM   20523 C  CG1   . ILE A 1 4130 ? 158.401 186.716 147.566 1.00 56.22  ? 4130 ILE A CG1   1 
ATOM   20524 C  CG2   . ILE A 1 4130 ? 157.385 184.542 148.230 1.00 48.24  ? 4130 ILE A CG2   1 
ATOM   20525 C  CD1   . ILE A 1 4130 ? 157.029 187.324 147.393 1.00 50.69  ? 4130 ILE A CD1   1 
ATOM   20526 N  N     . ASN A 1 4131 ? 160.744 182.436 148.131 1.00 65.64  ? 4131 ASN A N     1 
ATOM   20527 C  CA    . ASN A 1 4131 ? 160.814 180.989 148.045 1.00 64.17  ? 4131 ASN A CA    1 
ATOM   20528 C  C     . ASN A 1 4131 ? 160.566 180.370 149.415 1.00 64.97  ? 4131 ASN A C     1 
ATOM   20529 O  O     . ASN A 1 4131 ? 160.901 180.968 150.441 1.00 73.22  ? 4131 ASN A O     1 
ATOM   20530 C  CB    . ASN A 1 4131 ? 162.179 180.524 147.523 1.00 67.88  ? 4131 ASN A CB    1 
ATOM   20531 C  CG    . ASN A 1 4131 ? 162.363 180.800 146.046 1.00 75.35  ? 4131 ASN A CG    1 
ATOM   20532 O  OD1   . ASN A 1 4131 ? 161.449 181.272 145.372 1.00 78.58  ? 4131 ASN A OD1   1 
ATOM   20533 N  ND2   . ASN A 1 4131 ? 163.551 180.505 145.535 1.00 76.32  ? 4131 ASN A ND2   1 
ATOM   20534 N  N     . PRO A 1 4132 ? 159.967 179.179 149.465 1.00 59.66  ? 4132 PRO A N     1 
ATOM   20535 C  CA    . PRO A 1 4132 ? 159.855 178.475 150.752 1.00 60.55  ? 4132 PRO A CA    1 
ATOM   20536 C  C     . PRO A 1 4132 ? 161.198 178.078 151.335 1.00 67.67  ? 4132 PRO A C     1 
ATOM   20537 O  O     . PRO A 1 4132 ? 161.278 177.805 152.539 1.00 67.65  ? 4132 PRO A O     1 
ATOM   20538 C  CB    . PRO A 1 4132 ? 159.003 177.244 150.409 1.00 59.61  ? 4132 PRO A CB    1 
ATOM   20539 C  CG    . PRO A 1 4132 ? 158.305 177.600 149.134 1.00 59.66  ? 4132 PRO A CG    1 
ATOM   20540 C  CD    . PRO A 1 4132 ? 159.255 178.479 148.386 1.00 56.25  ? 4132 PRO A CD    1 
ATOM   20541 N  N     . LYS A 1 4133 ? 162.254 178.035 150.518 1.00 69.95  ? 4133 LYS A N     1 
ATOM   20542 C  CA    . LYS A 1 4133 ? 163.583 177.694 151.011 1.00 70.91  ? 4133 LYS A CA    1 
ATOM   20543 C  C     . LYS A 1 4133 ? 164.128 178.732 151.981 1.00 69.84  ? 4133 LYS A C     1 
ATOM   20544 O  O     . LYS A 1 4133 ? 165.037 178.417 152.756 1.00 74.74  ? 4133 LYS A O     1 
ATOM   20545 C  CB    . LYS A 1 4133 ? 164.554 177.536 149.841 1.00 75.81  ? 4133 LYS A CB    1 
ATOM   20546 C  CG    . LYS A 1 4133 ? 164.197 176.432 148.864 1.00 82.14  ? 4133 LYS A CG    1 
ATOM   20547 C  CD    . LYS A 1 4133 ? 165.269 176.304 147.794 1.00 89.17  ? 4133 LYS A CD    1 
ATOM   20548 C  CE    . LYS A 1 4133 ? 165.272 177.518 146.878 1.00 83.92  ? 4133 LYS A CE    1 
ATOM   20549 N  NZ    . LYS A 1 4133 ? 166.259 177.385 145.772 1.00 77.88  ? 4133 LYS A NZ    1 
ATOM   20550 N  N     . VAL A 1 4134 ? 163.602 179.953 151.949 1.00 65.94  ? 4134 VAL A N     1 
ATOM   20551 C  CA    . VAL A 1 4134 ? 164.110 181.019 152.819 1.00 67.36  ? 4134 VAL A CA    1 
ATOM   20552 C  C     . VAL A 1 4134 ? 163.913 180.621 154.275 1.00 68.95  ? 4134 VAL A C     1 
ATOM   20553 O  O     . VAL A 1 4134 ? 162.812 180.175 154.653 1.00 68.36  ? 4134 VAL A O     1 
ATOM   20554 C  CB    . VAL A 1 4134 ? 163.400 182.346 152.512 1.00 63.96  ? 4134 VAL A CB    1 
ATOM   20555 C  CG1   . VAL A 1 4134 ? 163.965 183.458 153.370 1.00 66.52  ? 4134 VAL A CG1   1 
ATOM   20556 C  CG2   . VAL A 1 4134 ? 163.546 182.686 151.043 1.00 63.38  ? 4134 VAL A CG2   1 
ATOM   20557 N  N     . PRO A 1 4135 ? 164.934 180.740 155.123 1.00 67.85  ? 4135 PRO A N     1 
ATOM   20558 C  CA    . PRO A 1 4135 ? 164.789 180.313 156.519 1.00 66.08  ? 4135 PRO A CA    1 
ATOM   20559 C  C     . PRO A 1 4135 ? 163.718 181.110 157.247 1.00 64.12  ? 4135 PRO A C     1 
ATOM   20560 O  O     . PRO A 1 4135 ? 163.525 182.302 156.999 1.00 65.78  ? 4135 PRO A O     1 
ATOM   20561 C  CB    . PRO A 1 4135 ? 166.179 180.570 157.111 1.00 74.15  ? 4135 PRO A CB    1 
ATOM   20562 C  CG    . PRO A 1 4135 ? 167.097 180.594 155.934 1.00 78.61  ? 4135 PRO A CG    1 
ATOM   20563 C  CD    . PRO A 1 4135 ? 166.304 181.178 154.816 1.00 72.10  ? 4135 PRO A CD    1 
ATOM   20564 N  N     . VAL A 1 4136 ? 163.015 180.431 158.154 1.00 64.59  ? 4136 VAL A N     1 
ATOM   20565 C  CA    . VAL A 1 4136 ? 162.002 181.099 158.966 1.00 57.64  ? 4136 VAL A CA    1 
ATOM   20566 C  C     . VAL A 1 4136 ? 162.656 182.078 159.931 1.00 53.82  ? 4136 VAL A C     1 
ATOM   20567 O  O     . VAL A 1 4136 ? 162.125 183.164 160.190 1.00 54.99  ? 4136 VAL A O     1 
ATOM   20568 C  CB    . VAL A 1 4136 ? 161.143 180.058 159.706 1.00 61.17  ? 4136 VAL A CB    1 
ATOM   20569 C  CG1   . VAL A 1 4136 ? 160.156 180.742 160.635 1.00 57.00  ? 4136 VAL A CG1   1 
ATOM   20570 C  CG2   . VAL A 1 4136 ? 160.413 179.174 158.711 1.00 65.41  ? 4136 VAL A CG2   1 
ATOM   20571 N  N     . ASN A 1 4137 ? 163.817 181.713 160.478 1.00 58.32  ? 4137 ASN A N     1 
ATOM   20572 C  CA    . ASN A 1 4137 ? 164.481 182.578 161.448 1.00 59.14  ? 4137 ASN A CA    1 
ATOM   20573 C  C     . ASN A 1 4137 ? 164.998 183.858 160.800 1.00 58.26  ? 4137 ASN A C     1 
ATOM   20574 O  O     . ASN A 1 4137 ? 165.037 184.913 161.443 1.00 58.77  ? 4137 ASN A O     1 
ATOM   20575 C  CB    . ASN A 1 4137 ? 165.609 181.814 162.148 1.00 67.50  ? 4137 ASN A CB    1 
ATOM   20576 C  CG    . ASN A 1 4137 ? 166.715 181.380 161.197 1.00 77.08  ? 4137 ASN A CG    1 
ATOM   20577 O  OD1   . ASN A 1 4137 ? 166.727 181.738 160.021 1.00 77.94  ? 4137 ASN A OD1   1 
ATOM   20578 N  ND2   . ASN A 1 4137 ? 167.655 180.597 161.713 1.00 80.48  ? 4137 ASN A ND2   1 
ATOM   20579 N  N     . LEU A 1 4138 ? 165.412 183.785 159.533 1.00 58.38  ? 4138 LEU A N     1 
ATOM   20580 C  CA    . LEU A 1 4138 ? 165.856 184.991 158.839 1.00 58.39  ? 4138 LEU A CA    1 
ATOM   20581 C  C     . LEU A 1 4138 ? 164.690 185.930 158.562 1.00 57.75  ? 4138 LEU A C     1 
ATOM   20582 O  O     . LEU A 1 4138 ? 164.810 187.149 158.734 1.00 58.43  ? 4138 LEU A O     1 
ATOM   20583 C  CB    . LEU A 1 4138 ? 166.561 184.627 157.535 1.00 56.77  ? 4138 LEU A CB    1 
ATOM   20584 C  CG    . LEU A 1 4138 ? 167.036 185.840 156.733 1.00 56.32  ? 4138 LEU A CG    1 
ATOM   20585 C  CD1   . LEU A 1 4138 ? 168.335 186.393 157.299 1.00 57.96  ? 4138 LEU A CD1   1 
ATOM   20586 C  CD2   . LEU A 1 4138 ? 167.184 185.499 155.264 1.00 65.48  ? 4138 LEU A CD2   1 
ATOM   20587 N  N     . LEU A 1 4139 ? 163.555 185.383 158.119 1.00 54.28  ? 4139 LEU A N     1 
ATOM   20588 C  CA    . LEU A 1 4139 ? 162.369 186.205 157.902 1.00 44.49  ? 4139 LEU A CA    1 
ATOM   20589 C  C     . LEU A 1 4139 ? 161.884 186.818 159.207 1.00 43.02  ? 4139 LEU A C     1 
ATOM   20590 O  O     . LEU A 1 4139 ? 161.479 187.986 159.243 1.00 46.82  ? 4139 LEU A O     1 
ATOM   20591 C  CB    . LEU A 1 4139 ? 161.261 185.368 157.265 1.00 46.06  ? 4139 LEU A CB    1 
ATOM   20592 C  CG    . LEU A 1 4139 ? 161.497 184.825 155.857 1.00 44.59  ? 4139 LEU A CG    1 
ATOM   20593 C  CD1   . LEU A 1 4139 ? 160.334 183.951 155.432 1.00 44.13  ? 4139 LEU A CD1   1 
ATOM   20594 C  CD2   . LEU A 1 4139 ? 161.694 185.963 154.874 1.00 43.33  ? 4139 LEU A CD2   1 
ATOM   20595 N  N     . ARG A 1 4140 ? 161.918 186.040 160.288 1.00 44.38  ? 4140 ARG A N     1 
ATOM   20596 C  CA    . ARG A 1 4140 ? 161.442 186.515 161.581 1.00 46.42  ? 4140 ARG A CA    1 
ATOM   20597 C  C     . ARG A 1 4140 ? 162.349 187.595 162.156 1.00 51.20  ? 4140 ARG A C     1 
ATOM   20598 O  O     . ARG A 1 4140 ? 161.875 188.485 162.871 1.00 50.17  ? 4140 ARG A O     1 
ATOM   20599 C  CB    . ARG A 1 4140 ? 161.326 185.332 162.540 1.00 44.59  ? 4140 ARG A CB    1 
ATOM   20600 C  CG    . ARG A 1 4140 ? 160.906 185.687 163.945 1.00 51.96  ? 4140 ARG A CG    1 
ATOM   20601 C  CD    . ARG A 1 4140 ? 160.442 184.455 164.692 1.00 53.06  ? 4140 ARG A CD    1 
ATOM   20602 N  NE    . ARG A 1 4140 ? 159.486 183.689 163.904 1.00 60.73  ? 4140 ARG A NE    1 
ATOM   20603 C  CZ    . ARG A 1 4140 ? 158.177 183.686 164.111 1.00 61.25  ? 4140 ARG A CZ    1 
ATOM   20604 N  NH1   . ARG A 1 4140 ? 157.630 184.395 165.085 1.00 57.16  ? 4140 ARG A NH1   1 
ATOM   20605 N  NH2   . ARG A 1 4140 ? 157.396 182.955 163.320 1.00 57.73  ? 4140 ARG A NH2   1 
ATOM   20606 N  N     . ALA A 1 4141 ? 163.644 187.545 161.852 1.00 51.07  ? 4141 ALA A N     1 
ATOM   20607 C  CA    . ALA A 1 4141 ? 164.623 188.491 162.384 1.00 49.97  ? 4141 ALA A CA    1 
ATOM   20608 C  C     . ALA A 1 4141 ? 165.048 189.522 161.348 1.00 48.42  ? 4141 ALA A C     1 
ATOM   20609 O  O     . ALA A 1 4141 ? 166.214 189.921 161.304 1.00 57.21  ? 4141 ALA A O     1 
ATOM   20610 C  CB    . ALA A 1 4141 ? 165.838 187.743 162.922 1.00 61.50  ? 4141 ALA A CB    1 
ATOM   20611 N  N     . GLY A 1 4142 ? 164.129 189.968 160.500 1.00 49.70  ? 4142 GLY A N     1 
ATOM   20612 C  CA    . GLY A 1 4142 ? 164.456 190.964 159.499 1.00 49.89  ? 4142 GLY A CA    1 
ATOM   20613 C  C     . GLY A 1 4142 ? 163.210 191.620 158.958 1.00 45.51  ? 4142 GLY A C     1 
ATOM   20614 O  O     . GLY A 1 4142 ? 162.156 190.988 158.842 1.00 49.13  ? 4142 GLY A O     1 
ATOM   20615 N  N     . ARG A 1 4143 ? 163.331 192.904 158.630 1.00 42.38  ? 4143 ARG A N     1 
ATOM   20616 C  CA    . ARG A 1 4143 ? 162.221 193.636 158.036 1.00 38.38  ? 4143 ARG A CA    1 
ATOM   20617 C  C     . ARG A 1 4143 ? 161.962 193.127 156.625 1.00 44.71  ? 4143 ARG A C     1 
ATOM   20618 O  O     . ARG A 1 4143 ? 162.884 193.032 155.810 1.00 54.35  ? 4143 ARG A O     1 
ATOM   20619 C  CB    . ARG A 1 4143 ? 162.529 195.131 158.017 1.00 39.70  ? 4143 ARG A CB    1 
ATOM   20620 C  CG    . ARG A 1 4143 ? 161.348 196.018 157.677 1.00 48.65  ? 4143 ARG A CG    1 
ATOM   20621 C  CD    . ARG A 1 4143 ? 160.471 196.277 158.892 1.00 48.16  ? 4143 ARG A CD    1 
ATOM   20622 N  NE    . ARG A 1 4143 ? 159.717 197.519 158.766 1.00 48.53  ? 4143 ARG A NE    1 
ATOM   20623 C  CZ    . ARG A 1 4143 ? 158.688 197.697 157.949 1.00 52.08  ? 4143 ARG A CZ    1 
ATOM   20624 N  NH1   . ARG A 1 4143 ? 158.230 196.718 157.187 1.00 47.54  ? 4143 ARG A NH1   1 
ATOM   20625 N  NH2   . ARG A 1 4143 ? 158.100 198.889 157.898 1.00 52.27  ? 4143 ARG A NH2   1 
ATOM   20626 N  N     . ILE A 1 4144 ? 160.705 192.807 156.331 1.00 40.69  ? 4144 ILE A N     1 
ATOM   20627 C  CA    . ILE A 1 4144 ? 160.319 192.182 155.072 1.00 36.22  ? 4144 ILE A CA    1 
ATOM   20628 C  C     . ILE A 1 4144 ? 159.554 193.194 154.236 1.00 38.71  ? 4144 ILE A C     1 
ATOM   20629 O  O     . ILE A 1 4144 ? 158.625 193.845 154.730 1.00 45.02  ? 4144 ILE A O     1 
ATOM   20630 C  CB    . ILE A 1 4144 ? 159.475 190.918 155.306 1.00 33.21  ? 4144 ILE A CB    1 
ATOM   20631 C  CG1   . ILE A 1 4144 ? 160.227 189.935 156.200 1.00 41.96  ? 4144 ILE A CG1   1 
ATOM   20632 C  CG2   . ILE A 1 4144 ? 159.130 190.260 153.986 1.00 37.21  ? 4144 ILE A CG2   1 
ATOM   20633 C  CD1   . ILE A 1 4144 ? 159.450 188.684 156.506 1.00 41.38  ? 4144 ILE A CD1   1 
ATOM   20634 N  N     . PHE A 1 4145 ? 159.950 193.331 152.973 1.00 42.56  ? 4145 PHE A N     1 
ATOM   20635 C  CA    . PHE A 1 4145 ? 159.249 194.164 152.004 1.00 41.17  ? 4145 PHE A CA    1 
ATOM   20636 C  C     . PHE A 1 4145 ? 158.909 193.301 150.802 1.00 45.98  ? 4145 PHE A C     1 
ATOM   20637 O  O     . PHE A 1 4145 ? 159.797 192.669 150.222 1.00 55.98  ? 4145 PHE A O     1 
ATOM   20638 C  CB    . PHE A 1 4145 ? 160.103 195.362 151.584 1.00 43.57  ? 4145 PHE A CB    1 
ATOM   20639 C  CG    . PHE A 1 4145 ? 160.252 196.400 152.653 1.00 46.51  ? 4145 PHE A CG    1 
ATOM   20640 C  CD1   . PHE A 1 4145 ? 159.193 197.220 152.993 1.00 49.90  ? 4145 PHE A CD1   1 
ATOM   20641 C  CD2   . PHE A 1 4145 ? 161.448 196.547 153.330 1.00 46.76  ? 4145 PHE A CD2   1 
ATOM   20642 C  CE1   . PHE A 1 4145 ? 159.329 198.174 153.977 1.00 49.24  ? 4145 PHE A CE1   1 
ATOM   20643 C  CE2   . PHE A 1 4145 ? 161.588 197.497 154.316 1.00 46.22  ? 4145 PHE A CE2   1 
ATOM   20644 C  CZ    . PHE A 1 4145 ? 160.527 198.311 154.639 1.00 47.26  ? 4145 PHE A CZ    1 
ATOM   20645 N  N     . VAL A 1 4146 ? 157.634 193.270 150.432 1.00 46.09  ? 4146 VAL A N     1 
ATOM   20646 C  CA    . VAL A 1 4146 ? 157.159 192.456 149.320 1.00 46.49  ? 4146 VAL A CA    1 
ATOM   20647 C  C     . VAL A 1 4146 ? 156.869 193.366 148.138 1.00 52.36  ? 4146 VAL A C     1 
ATOM   20648 O  O     . VAL A 1 4146 ? 156.119 194.342 148.264 1.00 53.36  ? 4146 VAL A O     1 
ATOM   20649 C  CB    . VAL A 1 4146 ? 155.914 191.644 149.711 1.00 38.91  ? 4146 VAL A CB    1 
ATOM   20650 C  CG1   . VAL A 1 4146 ? 155.229 191.109 148.473 1.00 39.71  ? 4146 VAL A CG1   1 
ATOM   20651 C  CG2   . VAL A 1 4146 ? 156.302 190.503 150.629 1.00 40.67  ? 4146 VAL A CG2   1 
ATOM   20652 N  N     . PHE A 1 4147 ? 157.462 193.051 146.990 1.00 53.59  ? 4147 PHE A N     1 
ATOM   20653 C  CA    . PHE A 1 4147 ? 157.292 193.829 145.772 1.00 54.71  ? 4147 PHE A CA    1 
ATOM   20654 C  C     . PHE A 1 4147 ? 156.584 192.993 144.719 1.00 63.07  ? 4147 PHE A C     1 
ATOM   20655 O  O     . PHE A 1 4147 ? 156.992 191.861 144.439 1.00 64.58  ? 4147 PHE A O     1 
ATOM   20656 C  CB    . PHE A 1 4147 ? 158.638 194.319 145.238 1.00 56.33  ? 4147 PHE A CB    1 
ATOM   20657 C  CG    . PHE A 1 4147 ? 159.272 195.374 146.087 1.00 61.43  ? 4147 PHE A CG    1 
ATOM   20658 C  CD1   . PHE A 1 4147 ? 159.928 195.037 147.254 1.00 55.41  ? 4147 PHE A CD1   1 
ATOM   20659 C  CD2   . PHE A 1 4147 ? 159.205 196.706 145.722 1.00 70.77  ? 4147 PHE A CD2   1 
ATOM   20660 C  CE1   . PHE A 1 4147 ? 160.503 196.003 148.038 1.00 58.31  ? 4147 PHE A CE1   1 
ATOM   20661 C  CE2   . PHE A 1 4147 ? 159.784 197.679 146.505 1.00 73.90  ? 4147 PHE A CE2   1 
ATOM   20662 C  CZ    . PHE A 1 4147 ? 160.434 197.326 147.664 1.00 69.77  ? 4147 PHE A CZ    1 
ATOM   20663 N  N     . GLU A 1 4148 ? 155.527 193.555 144.142 1.00 65.48  ? 4148 GLU A N     1 
ATOM   20664 C  CA    . GLU A 1 4148 ? 154.784 192.933 143.065 1.00 64.96  ? 4148 GLU A CA    1 
ATOM   20665 C  C     . GLU A 1 4148 ? 154.686 193.913 141.905 1.00 69.09  ? 4148 GLU A C     1 
ATOM   20666 O  O     . GLU A 1 4148 ? 154.563 195.124 142.125 1.00 70.11  ? 4148 GLU A O     1 
ATOM   20667 C  CB    . GLU A 1 4148 ? 153.379 192.530 143.530 1.00 63.69  ? 4148 GLU A CB    1 
ATOM   20668 C  CG    . GLU A 1 4148 ? 153.358 191.676 144.783 1.00 60.06  ? 4148 GLU A CG    1 
ATOM   20669 C  CD    . GLU A 1 4148 ? 152.019 191.718 145.485 1.00 64.21  ? 4148 GLU A CD    1 
ATOM   20670 O  OE1   . GLU A 1 4148 ? 151.636 192.804 145.966 1.00 64.16  ? 4148 GLU A OE1   1 
ATOM   20671 O  OE2   . GLU A 1 4148 ? 151.345 190.669 145.549 1.00 68.42  ? 4148 GLU A OE2   1 
ATOM   20672 N  N     . PRO A 1 4149 ? 154.744 193.428 140.663 1.00 66.60  ? 4149 PRO A N     1 
ATOM   20673 C  CA    . PRO A 1 4149 ? 154.671 194.339 139.528 1.00 68.84  ? 4149 PRO A CA    1 
ATOM   20674 C  C     . PRO A 1 4149 ? 153.285 194.945 139.415 1.00 66.49  ? 4149 PRO A C     1 
ATOM   20675 O  O     . PRO A 1 4149 ? 152.280 194.299 139.758 1.00 62.88  ? 4149 PRO A O     1 
ATOM   20676 C  CB    . PRO A 1 4149 ? 154.988 193.432 138.327 1.00 63.76  ? 4149 PRO A CB    1 
ATOM   20677 C  CG    . PRO A 1 4149 ? 154.535 192.089 138.759 1.00 60.67  ? 4149 PRO A CG    1 
ATOM   20678 C  CD    . PRO A 1 4149 ? 154.787 192.018 140.241 1.00 60.71  ? 4149 PRO A CD    1 
ATOM   20679 N  N     . PRO A 1 4150 ? 153.179 196.182 138.945 1.00 63.68  ? 4150 PRO A N     1 
ATOM   20680 C  CA    . PRO A 1 4150 ? 151.862 196.775 138.712 1.00 62.02  ? 4150 PRO A CA    1 
ATOM   20681 C  C     . PRO A 1 4150 ? 151.141 196.048 137.593 1.00 65.29  ? 4150 PRO A C     1 
ATOM   20682 O  O     . PRO A 1 4150 ? 151.603 196.047 136.442 1.00 65.37  ? 4150 PRO A O     1 
ATOM   20683 C  CB    . PRO A 1 4150 ? 152.188 198.225 138.324 1.00 66.55  ? 4150 PRO A CB    1 
ATOM   20684 C  CG    . PRO A 1 4150 ? 153.602 198.191 137.857 1.00 69.37  ? 4150 PRO A CG    1 
ATOM   20685 C  CD    . PRO A 1 4150 ? 154.275 197.122 138.656 1.00 64.23  ? 4150 PRO A CD    1 
ATOM   20686 N  N     . PRO A 1 4151 ? 150.014 195.407 137.891 1.00 65.64  ? 4151 PRO A N     1 
ATOM   20687 C  CA    . PRO A 1 4151 ? 149.322 194.624 136.865 1.00 60.78  ? 4151 PRO A CA    1 
ATOM   20688 C  C     . PRO A 1 4151 ? 148.780 195.506 135.752 1.00 59.74  ? 4151 PRO A C     1 
ATOM   20689 O  O     . PRO A 1 4151 ? 148.423 196.667 135.962 1.00 66.55  ? 4151 PRO A O     1 
ATOM   20690 C  CB    . PRO A 1 4151 ? 148.187 193.950 137.642 1.00 57.08  ? 4151 PRO A CB    1 
ATOM   20691 C  CG    . PRO A 1 4151 ? 147.931 194.866 138.785 1.00 58.70  ? 4151 PRO A CG    1 
ATOM   20692 C  CD    . PRO A 1 4151 ? 149.271 195.433 139.162 1.00 62.43  ? 4151 PRO A CD    1 
ATOM   20693 N  N     . GLY A 1 4152 ? 148.729 194.938 134.558 1.00 51.04  ? 4152 GLY A N     1 
ATOM   20694 C  CA    . GLY A 1 4152 ? 148.187 195.622 133.398 1.00 49.17  ? 4152 GLY A CA    1 
ATOM   20695 C  C     . GLY A 1 4152 ? 149.028 195.422 132.154 1.00 46.91  ? 4152 GLY A C     1 
ATOM   20696 O  O     . GLY A 1 4152 ? 150.230 195.165 132.215 1.00 50.72  ? 4152 GLY A O     1 
ATOM   20697 N  N     . VAL A 1 4153 ? 148.378 195.533 130.995 1.00 47.69  ? 4153 VAL A N     1 
ATOM   20698 C  CA    . VAL A 1 4153 ? 149.093 195.446 129.726 1.00 40.24  ? 4153 VAL A CA    1 
ATOM   20699 C  C     . VAL A 1 4153 ? 150.041 196.627 129.569 1.00 42.39  ? 4153 VAL A C     1 
ATOM   20700 O  O     . VAL A 1 4153 ? 151.174 196.475 129.099 1.00 45.36  ? 4153 VAL A O     1 
ATOM   20701 C  CB    . VAL A 1 4153 ? 148.093 195.358 128.558 1.00 34.79  ? 4153 VAL A CB    1 
ATOM   20702 C  CG1   . VAL A 1 4153 ? 148.807 195.502 127.230 1.00 39.13  ? 4153 VAL A CG1   1 
ATOM   20703 C  CG2   . VAL A 1 4153 ? 147.337 194.047 128.614 1.00 37.99  ? 4153 VAL A CG2   1 
ATOM   20704 N  N     . LYS A 1 4154 ? 149.593 197.820 129.962 1.00 44.31  ? 4154 LYS A N     1 
ATOM   20705 C  CA    . LYS A 1 4154 ? 150.409 199.020 129.802 1.00 41.87  ? 4154 LYS A CA    1 
ATOM   20706 C  C     . LYS A 1 4154 ? 151.699 198.922 130.607 1.00 45.74  ? 4154 LYS A C     1 
ATOM   20707 O  O     . LYS A 1 4154 ? 152.793 199.163 130.083 1.00 52.67  ? 4154 LYS A O     1 
ATOM   20708 C  CB    . LYS A 1 4154 ? 149.601 200.247 130.222 1.00 44.05  ? 4154 LYS A CB    1 
ATOM   20709 C  CG    . LYS A 1 4154 ? 150.308 201.573 130.027 1.00 50.41  ? 4154 LYS A CG    1 
ATOM   20710 C  CD    . LYS A 1 4154 ? 149.361 202.724 130.315 1.00 57.71  ? 4154 LYS A CD    1 
ATOM   20711 C  CE    . LYS A 1 4154 ? 150.080 204.057 130.284 1.00 58.19  ? 4154 LYS A CE    1 
ATOM   20712 N  NZ    . LYS A 1 4154 ? 149.140 205.192 130.490 1.00 57.11  ? 4154 LYS A NZ    1 
ATOM   20713 N  N     . ALA A 1 4155 ? 151.587 198.560 131.887 1.00 46.21  ? 4155 ALA A N     1 
ATOM   20714 C  CA    . ALA A 1 4155 ? 152.771 198.440 132.731 1.00 45.49  ? 4155 ALA A CA    1 
ATOM   20715 C  C     . ALA A 1 4155 ? 153.685 197.322 132.248 1.00 49.49  ? 4155 ALA A C     1 
ATOM   20716 O  O     . ALA A 1 4155 ? 154.913 197.469 132.260 1.00 54.75  ? 4155 ALA A O     1 
ATOM   20717 C  CB    . ALA A 1 4155 ? 152.359 198.207 134.182 1.00 46.18  ? 4155 ALA A CB    1 
ATOM   20718 N  N     . ASN A 1 4156 ? 153.106 196.195 131.827 1.00 46.72  ? 4156 ASN A N     1 
ATOM   20719 C  CA    . ASN A 1 4156 ? 153.914 195.087 131.330 1.00 40.70  ? 4156 ASN A CA    1 
ATOM   20720 C  C     . ASN A 1 4156 ? 154.700 195.490 130.090 1.00 41.01  ? 4156 ASN A C     1 
ATOM   20721 O  O     . ASN A 1 4156 ? 155.890 195.178 129.971 1.00 45.95  ? 4156 ASN A O     1 
ATOM   20722 C  CB    . ASN A 1 4156 ? 153.022 193.884 131.031 1.00 39.17  ? 4156 ASN A CB    1 
ATOM   20723 C  CG    . ASN A 1 4156 ? 153.750 192.567 131.184 1.00 46.35  ? 4156 ASN A CG    1 
ATOM   20724 O  OD1   . ASN A 1 4156 ? 154.759 192.322 130.525 1.00 50.47  ? 4156 ASN A OD1   1 
ATOM   20725 N  ND2   . ASN A 1 4156 ? 153.238 191.706 132.053 1.00 49.97  ? 4156 ASN A ND2   1 
ATOM   20726 N  N     . MET A 1 4157 ? 154.055 196.194 129.160 1.00 40.56  ? 4157 MET A N     1 
ATOM   20727 C  CA    . MET A 1 4157 ? 154.749 196.609 127.946 1.00 41.53  ? 4157 MET A CA    1 
ATOM   20728 C  C     . MET A 1 4157 ? 155.796 197.672 128.245 1.00 45.32  ? 4157 MET A C     1 
ATOM   20729 O  O     . MET A 1 4157 ? 156.857 197.698 127.612 1.00 48.44  ? 4157 MET A O     1 
ATOM   20730 C  CB    . MET A 1 4157 ? 153.747 197.113 126.913 1.00 37.65  ? 4157 MET A CB    1 
ATOM   20731 C  CG    . MET A 1 4157 ? 152.825 196.035 126.392 1.00 36.43  ? 4157 MET A CG    1 
ATOM   20732 S  SD    . MET A 1 4157 ? 151.614 196.683 125.240 1.00 52.82  ? 4157 MET A SD    1 
ATOM   20733 C  CE    . MET A 1 4157 ? 152.670 197.045 123.846 1.00 46.13  ? 4157 MET A CE    1 
ATOM   20734 N  N     . LEU A 1 4158 ? 155.519 198.561 129.202 1.00 44.97  ? 4158 LEU A N     1 
ATOM   20735 C  CA    . LEU A 1 4158 ? 156.525 199.539 129.600 1.00 41.36  ? 4158 LEU A CA    1 
ATOM   20736 C  C     . LEU A 1 4158 ? 157.747 198.855 130.201 1.00 46.13  ? 4158 LEU A C     1 
ATOM   20737 O  O     . LEU A 1 4158 ? 158.887 199.224 129.896 1.00 48.71  ? 4158 LEU A O     1 
ATOM   20738 C  CB    . LEU A 1 4158 ? 155.924 200.540 130.583 1.00 40.85  ? 4158 LEU A CB    1 
ATOM   20739 C  CG    . LEU A 1 4158 ? 155.063 201.633 129.950 1.00 46.89  ? 4158 LEU A CG    1 
ATOM   20740 C  CD1   . LEU A 1 4158 ? 154.571 202.608 131.005 1.00 54.93  ? 4158 LEU A CD1   1 
ATOM   20741 C  CD2   . LEU A 1 4158 ? 155.836 202.358 128.862 1.00 45.58  ? 4158 LEU A CD2   1 
ATOM   20742 N  N     . ARG A 1 4159 ? 157.529 197.846 131.048 1.00 45.00  ? 4159 ARG A N     1 
ATOM   20743 C  CA    . ARG A 1 4159 ? 158.647 197.085 131.597 1.00 42.86  ? 4159 ARG A CA    1 
ATOM   20744 C  C     . ARG A 1 4159 ? 159.414 196.364 130.497 1.00 50.11  ? 4159 ARG A C     1 
ATOM   20745 O  O     . ARG A 1 4159 ? 160.650 196.317 130.519 1.00 57.04  ? 4159 ARG A O     1 
ATOM   20746 C  CB    . ARG A 1 4159 ? 158.145 196.084 132.637 1.00 41.88  ? 4159 ARG A CB    1 
ATOM   20747 C  CG    . ARG A 1 4159 ? 157.671 196.712 133.931 1.00 51.95  ? 4159 ARG A CG    1 
ATOM   20748 C  CD    . ARG A 1 4159 ? 157.272 195.650 134.940 1.00 55.23  ? 4159 ARG A CD    1 
ATOM   20749 N  NE    . ARG A 1 4159 ? 155.825 195.516 135.048 1.00 54.72  ? 4159 ARG A NE    1 
ATOM   20750 C  CZ    . ARG A 1 4159 ? 155.169 194.370 134.933 1.00 59.18  ? 4159 ARG A CZ    1 
ATOM   20751 N  NH1   . ARG A 1 4159 ? 155.802 193.233 134.694 1.00 59.40  ? 4159 ARG A NH1   1 
ATOM   20752 N  NH2   . ARG A 1 4159 ? 153.846 194.364 135.061 1.00 60.80  ? 4159 ARG A NH2   1 
ATOM   20753 N  N     . THR A 1 4160 ? 158.697 195.787 129.531 1.00 50.14  ? 4160 THR A N     1 
ATOM   20754 C  CA    . THR A 1 4160 ? 159.352 195.092 128.427 1.00 44.32  ? 4160 THR A CA    1 
ATOM   20755 C  C     . THR A 1 4160 ? 160.224 196.046 127.620 1.00 44.66  ? 4160 THR A C     1 
ATOM   20756 O  O     . THR A 1 4160 ? 161.371 195.729 127.288 1.00 48.12  ? 4160 THR A O     1 
ATOM   20757 C  CB    . THR A 1 4160 ? 158.305 194.431 127.531 1.00 44.46  ? 4160 THR A CB    1 
ATOM   20758 O  OG1   . THR A 1 4160 ? 157.736 193.303 128.207 1.00 43.92  ? 4160 THR A OG1   1 
ATOM   20759 C  CG2   . THR A 1 4160 ? 158.931 193.969 126.229 1.00 44.03  ? 4160 THR A CG2   1 
ATOM   20760 N  N     . PHE A 1 4161 ? 159.698 197.231 127.306 1.00 47.53  ? 4161 PHE A N     1 
ATOM   20761 C  CA    . PHE A 1 4161 ? 160.469 198.199 126.534 1.00 49.36  ? 4161 PHE A CA    1 
ATOM   20762 C  C     . PHE A 1 4161 ? 161.638 198.757 127.335 1.00 52.66  ? 4161 PHE A C     1 
ATOM   20763 O  O     . PHE A 1 4161 ? 162.676 199.096 126.756 1.00 58.53  ? 4161 PHE A O     1 
ATOM   20764 C  CB    . PHE A 1 4161 ? 159.563 199.329 126.049 1.00 51.92  ? 4161 PHE A CB    1 
ATOM   20765 C  CG    . PHE A 1 4161 ? 158.712 198.957 124.870 1.00 48.53  ? 4161 PHE A CG    1 
ATOM   20766 C  CD1   . PHE A 1 4161 ? 159.289 198.455 123.717 1.00 51.09  ? 4161 PHE A CD1   1 
ATOM   20767 C  CD2   . PHE A 1 4161 ? 157.338 199.105 124.915 1.00 46.35  ? 4161 PHE A CD2   1 
ATOM   20768 C  CE1   . PHE A 1 4161 ? 158.512 198.111 122.631 1.00 51.91  ? 4161 PHE A CE1   1 
ATOM   20769 C  CE2   . PHE A 1 4161 ? 156.556 198.761 123.831 1.00 48.80  ? 4161 PHE A CE2   1 
ATOM   20770 C  CZ    . PHE A 1 4161 ? 157.144 198.264 122.689 1.00 50.75  ? 4161 PHE A CZ    1 
ATOM   20771 N  N     . SER A 1 4162 ? 161.491 198.869 128.657 1.00 49.99  ? 4162 SER A N     1 
ATOM   20772 C  CA    . SER A 1 4162 ? 162.606 199.321 129.483 1.00 53.61  ? 4162 SER A CA    1 
ATOM   20773 C  C     . SER A 1 4162 ? 163.717 198.280 129.534 1.00 54.63  ? 4162 SER A C     1 
ATOM   20774 O  O     . SER A 1 4162 ? 164.901 198.626 129.451 1.00 56.48  ? 4162 SER A O     1 
ATOM   20775 C  CB    . SER A 1 4162 ? 162.115 199.649 130.892 1.00 52.60  ? 4162 SER A CB    1 
ATOM   20776 O  OG    . SER A 1 4162 ? 161.146 200.681 130.865 1.00 61.14  ? 4162 SER A OG    1 
ATOM   20777 N  N     . SER A 1 4163 ? 163.357 197.002 129.676 1.00 52.55  ? 4163 SER A N     1 
ATOM   20778 C  CA    . SER A 1 4163 ? 164.370 195.956 129.784 1.00 49.15  ? 4163 SER A CA    1 
ATOM   20779 C  C     . SER A 1 4163 ? 165.178 195.824 128.499 1.00 48.15  ? 4163 SER A C     1 
ATOM   20780 O  O     . SER A 1 4163 ? 166.402 195.656 128.544 1.00 50.02  ? 4163 SER A O     1 
ATOM   20781 C  CB    . SER A 1 4163 ? 163.713 194.624 130.142 1.00 55.21  ? 4163 SER A CB    1 
ATOM   20782 O  OG    . SER A 1 4163 ? 162.865 194.177 129.100 1.00 57.75  ? 4163 SER A OG    1 
ATOM   20783 N  N     . ILE A 1 4164 ? 164.518 195.894 127.352 1.00 48.72  ? 4164 ILE A N     1 
ATOM   20784 C  CA    . ILE A 1 4164 ? 165.205 195.748 126.067 1.00 49.32  ? 4164 ILE A CA    1 
ATOM   20785 C  C     . ILE A 1 4164 ? 165.939 197.048 125.749 1.00 57.18  ? 4164 ILE A C     1 
ATOM   20786 O  O     . ILE A 1 4164 ? 165.329 198.126 125.823 1.00 60.71  ? 4164 ILE A O     1 
ATOM   20787 C  CB    . ILE A 1 4164 ? 164.214 195.393 124.966 1.00 45.11  ? 4164 ILE A CB    1 
ATOM   20788 C  CG1   . ILE A 1 4164 ? 163.400 194.163 125.364 1.00 48.99  ? 4164 ILE A CG1   1 
ATOM   20789 C  CG2   . ILE A 1 4164 ? 164.943 195.123 123.668 1.00 50.05  ? 4164 ILE A CG2   1 
ATOM   20790 C  CD1   . ILE A 1 4164 ? 162.339 193.790 124.362 1.00 51.89  ? 4164 ILE A CD1   1 
ATOM   20791 N  N     . PRO A 1 4165 ? 167.227 196.995 125.411 1.00 62.15  ? 4165 PRO A N     1 
ATOM   20792 C  CA    . PRO A 1 4165 ? 167.958 198.227 125.094 1.00 60.64  ? 4165 PRO A CA    1 
ATOM   20793 C  C     . PRO A 1 4165 ? 167.397 198.919 123.861 1.00 62.98  ? 4165 PRO A C     1 
ATOM   20794 O  O     . PRO A 1 4165 ? 166.843 198.287 122.960 1.00 68.14  ? 4165 PRO A O     1 
ATOM   20795 C  CB    . PRO A 1 4165 ? 169.391 197.737 124.854 1.00 60.27  ? 4165 PRO A CB    1 
ATOM   20796 C  CG    . PRO A 1 4165 ? 169.471 196.435 125.577 1.00 61.35  ? 4165 PRO A CG    1 
ATOM   20797 C  CD    . PRO A 1 4165 ? 168.113 195.821 125.439 1.00 62.73  ? 4165 PRO A CD    1 
ATOM   20798 N  N     . VAL A 1 4166 ? 167.543 200.246 123.838 1.00 64.76  ? 4166 VAL A N     1 
ATOM   20799 C  CA    . VAL A 1 4166 ? 167.070 201.036 122.703 1.00 68.92  ? 4166 VAL A CA    1 
ATOM   20800 C  C     . VAL A 1 4166 ? 167.854 200.682 121.446 1.00 69.04  ? 4166 VAL A C     1 
ATOM   20801 O  O     . VAL A 1 4166 ? 167.293 200.584 120.348 1.00 69.88  ? 4166 VAL A O     1 
ATOM   20802 C  CB    . VAL A 1 4166 ? 167.167 202.539 123.021 1.00 75.52  ? 4166 VAL A CB    1 
ATOM   20803 C  CG1   . VAL A 1 4166 ? 166.658 203.366 121.852 1.00 72.62  ? 4166 VAL A CG1   1 
ATOM   20804 C  CG2   . VAL A 1 4166 ? 166.394 202.864 124.289 1.00 77.08  ? 4166 VAL A CG2   1 
ATOM   20805 N  N     . SER A 1 4167 ? 169.168 200.492 121.590 1.00 73.27  ? 4167 SER A N     1 
ATOM   20806 C  CA    . SER A 1 4167 ? 170.005 200.182 120.436 1.00 73.13  ? 4167 SER A CA    1 
ATOM   20807 C  C     . SER A 1 4167 ? 169.604 198.857 119.800 1.00 71.15  ? 4167 SER A C     1 
ATOM   20808 O  O     . SER A 1 4167 ? 169.645 198.714 118.574 1.00 72.73  ? 4167 SER A O     1 
ATOM   20809 C  CB    . SER A 1 4167 ? 171.476 200.155 120.847 1.00 73.45  ? 4167 SER A CB    1 
ATOM   20810 O  OG    . SER A 1 4167 ? 171.697 199.220 121.887 1.00 71.13  ? 4167 SER A OG    1 
ATOM   20811 N  N     . ARG A 1 4168 ? 169.220 197.876 120.620 1.00 68.16  ? 4168 ARG A N     1 
ATOM   20812 C  CA    . ARG A 1 4168 ? 168.791 196.587 120.086 1.00 65.77  ? 4168 ARG A CA    1 
ATOM   20813 C  C     . ARG A 1 4168 ? 167.549 196.731 119.217 1.00 64.85  ? 4168 ARG A C     1 
ATOM   20814 O  O     . ARG A 1 4168 ? 167.457 196.122 118.145 1.00 67.49  ? 4168 ARG A O     1 
ATOM   20815 C  CB    . ARG A 1 4168 ? 168.527 195.609 121.230 1.00 62.47  ? 4168 ARG A CB    1 
ATOM   20816 C  CG    . ARG A 1 4168 ? 168.204 194.202 120.773 1.00 63.88  ? 4168 ARG A CG    1 
ATOM   20817 C  CD    . ARG A 1 4168 ? 168.068 193.261 121.954 1.00 63.43  ? 4168 ARG A CD    1 
ATOM   20818 N  NE    . ARG A 1 4168 ? 168.062 191.866 121.536 1.00 59.63  ? 4168 ARG A NE    1 
ATOM   20819 C  CZ    . ARG A 1 4168 ? 167.875 190.841 122.356 1.00 62.16  ? 4168 ARG A CZ    1 
ATOM   20820 N  NH1   . ARG A 1 4168 ? 167.655 191.021 123.648 1.00 66.96  ? 4168 ARG A NH1   1 
ATOM   20821 N  NH2   . ARG A 1 4168 ? 167.907 189.606 121.867 1.00 63.22  ? 4168 ARG A NH2   1 
ATOM   20822 N  N     . ILE A 1 4169 ? 166.577 197.526 119.666 1.00 60.89  ? 4169 ILE A N     1 
ATOM   20823 C  CA    . ILE A 1 4169 ? 165.357 197.716 118.891 1.00 56.98  ? 4169 ILE A CA    1 
ATOM   20824 C  C     . ILE A 1 4169 ? 165.612 198.615 117.687 1.00 65.89  ? 4169 ILE A C     1 
ATOM   20825 O  O     . ILE A 1 4169 ? 164.877 198.559 116.694 1.00 66.77  ? 4169 ILE A O     1 
ATOM   20826 C  CB    . ILE A 1 4169 ? 164.245 198.275 119.796 1.00 56.41  ? 4169 ILE A CB    1 
ATOM   20827 C  CG1   . ILE A 1 4169 ? 164.183 197.489 121.104 1.00 62.04  ? 4169 ILE A CG1   1 
ATOM   20828 C  CG2   . ILE A 1 4169 ? 162.904 198.206 119.110 1.00 52.04  ? 4169 ILE A CG2   1 
ATOM   20829 C  CD1   . ILE A 1 4169 ? 163.015 197.861 121.986 1.00 62.95  ? 4169 ILE A CD1   1 
ATOM   20830 N  N     . CYS A 1 4170 ? 166.651 199.442 117.742 1.00 72.94  ? 4170 CYS A N     1 
ATOM   20831 C  CA    . CYS A 1 4170 ? 166.926 200.427 116.704 1.00 72.83  ? 4170 CYS A CA    1 
ATOM   20832 C  C     . CYS A 1 4170 ? 167.677 199.847 115.508 1.00 74.84  ? 4170 CYS A C     1 
ATOM   20833 O  O     . CYS A 1 4170 ? 167.769 200.513 114.471 1.00 79.66  ? 4170 CYS A O     1 
ATOM   20834 C  CB    . CYS A 1 4170 ? 167.709 201.600 117.315 1.00 78.68  ? 4170 CYS A CB    1 
ATOM   20835 S  SG    . CYS A 1 4170 ? 168.438 202.803 116.172 1.00 99.62  ? 4170 CYS A SG    1 
ATOM   20836 N  N     . LYS A 1 4171 ? 168.175 198.615 115.604 1.00 74.22  ? 4171 LYS A N     1 
ATOM   20837 C  CA    . LYS A 1 4171 ? 168.977 198.046 114.527 1.00 73.72  ? 4171 LYS A CA    1 
ATOM   20838 C  C     . LYS A 1 4171 ? 168.159 197.901 113.249 1.00 76.81  ? 4171 LYS A C     1 
ATOM   20839 O  O     . LYS A 1 4171 ? 166.943 197.697 113.279 1.00 73.91  ? 4171 LYS A O     1 
ATOM   20840 C  CB    . LYS A 1 4171 ? 169.535 196.682 114.933 1.00 70.33  ? 4171 LYS A CB    1 
ATOM   20841 C  CG    . LYS A 1 4171 ? 170.071 196.613 116.346 1.00 73.86  ? 4171 LYS A CG    1 
ATOM   20842 C  CD    . LYS A 1 4171 ? 170.884 195.349 116.567 1.00 75.68  ? 4171 LYS A CD    1 
ATOM   20843 C  CE    . LYS A 1 4171 ? 170.080 194.300 117.316 1.00 76.97  ? 4171 LYS A CE    1 
ATOM   20844 N  NZ    . LYS A 1 4171 ? 170.813 193.009 117.424 1.00 73.77  ? 4171 LYS A NZ    1 
ATOM   20845 N  N     . SER A 1 4172 ? 168.847 198.015 112.116 1.00 78.55  ? 4172 SER A N     1 
ATOM   20846 C  CA    . SER A 1 4172 ? 168.205 197.827 110.826 1.00 81.10  ? 4172 SER A CA    1 
ATOM   20847 C  C     . SER A 1 4172 ? 167.779 196.369 110.655 1.00 80.99  ? 4172 SER A C     1 
ATOM   20848 O  O     . SER A 1 4172 ? 168.441 195.457 111.158 1.00 79.61  ? 4172 SER A O     1 
ATOM   20849 C  CB    . SER A 1 4172 ? 169.151 198.228 109.698 1.00 84.43  ? 4172 SER A CB    1 
ATOM   20850 O  OG    . SER A 1 4172 ? 169.589 199.566 109.854 1.00 88.54  ? 4172 SER A OG    1 
ATOM   20851 N  N     . PRO A 1 4173 ? 166.672 196.117 109.942 1.00 76.85  ? 4173 PRO A N     1 
ATOM   20852 C  CA    . PRO A 1 4173 ? 165.799 197.074 109.246 1.00 78.28  ? 4173 PRO A CA    1 
ATOM   20853 C  C     . PRO A 1 4173 ? 164.874 197.840 110.188 1.00 79.66  ? 4173 PRO A C     1 
ATOM   20854 O  O     . PRO A 1 4173 ? 164.749 197.499 111.359 1.00 76.86  ? 4173 PRO A O     1 
ATOM   20855 C  CB    . PRO A 1 4173 ? 165.017 196.173 108.285 1.00 76.99  ? 4173 PRO A CB    1 
ATOM   20856 C  CG    . PRO A 1 4173 ? 164.895 194.879 109.023 1.00 69.51  ? 4173 PRO A CG    1 
ATOM   20857 C  CD    . PRO A 1 4173 ? 166.182 194.733 109.800 1.00 66.17  ? 4173 PRO A CD    1 
ATOM   20858 N  N     . ASN A 1 4174 ? 164.220 198.894 109.692 1.00 84.55  ? 4174 ASN A N     1 
ATOM   20859 C  CA    . ASN A 1 4174 ? 163.345 199.701 110.534 1.00 86.25  ? 4174 ASN A CA    1 
ATOM   20860 C  C     . ASN A 1 4174 ? 162.116 198.935 111.004 1.00 81.07  ? 4174 ASN A C     1 
ATOM   20861 O  O     . ASN A 1 4174 ? 161.513 199.317 112.013 1.00 76.96  ? 4174 ASN A O     1 
ATOM   20862 C  CB    . ASN A 1 4174 ? 162.914 200.963 109.787 1.00 86.29  ? 4174 ASN A CB    1 
ATOM   20863 C  CG    . ASN A 1 4174 ? 164.087 201.722 109.203 1.00 93.45  ? 4174 ASN A CG    1 
ATOM   20864 O  OD1   . ASN A 1 4174 ? 165.200 201.664 109.725 1.00 87.80  ? 4174 ASN A OD1   1 
ATOM   20865 N  ND2   . ASN A 1 4174 ? 163.843 202.444 108.116 1.00 101.19 ? 4174 ASN A ND2   1 
ATOM   20866 N  N     . GLU A 1 4175 ? 161.732 197.870 110.300 1.00 75.90  ? 4175 GLU A N     1 
ATOM   20867 C  CA    . GLU A 1 4175 ? 160.611 197.044 110.726 1.00 67.59  ? 4175 GLU A CA    1 
ATOM   20868 C  C     . GLU A 1 4175 ? 160.886 196.321 112.036 1.00 62.02  ? 4175 GLU A C     1 
ATOM   20869 O  O     . GLU A 1 4175 ? 159.930 195.952 112.731 1.00 59.46  ? 4175 GLU A O     1 
ATOM   20870 C  CB    . GLU A 1 4175 ? 160.270 196.032 109.629 1.00 68.36  ? 4175 GLU A CB    1 
ATOM   20871 C  CG    . GLU A 1 4175 ? 159.566 196.634 108.414 1.00 77.42  ? 4175 GLU A CG    1 
ATOM   20872 C  CD    . GLU A 1 4175 ? 160.489 197.423 107.497 1.00 89.76  ? 4175 GLU A CD    1 
ATOM   20873 O  OE1   . GLU A 1 4175 ? 161.595 197.814 107.927 1.00 91.21  ? 4175 GLU A OE1   1 
ATOM   20874 O  OE2   . GLU A 1 4175 ? 160.095 197.670 106.339 1.00 86.35  ? 4175 GLU A OE2   1 
ATOM   20875 N  N     . ARG A 1 4176 ? 162.163 196.149 112.398 1.00 59.69  ? 4176 ARG A N     1 
ATOM   20876 C  CA    . ARG A 1 4176 ? 162.522 195.417 113.608 1.00 52.14  ? 4176 ARG A CA    1 
ATOM   20877 C  C     . ARG A 1 4176 ? 161.756 195.928 114.817 1.00 51.89  ? 4176 ARG A C     1 
ATOM   20878 O  O     . ARG A 1 4176 ? 161.146 195.139 115.550 1.00 52.98  ? 4176 ARG A O     1 
ATOM   20879 C  CB    . ARG A 1 4176 ? 164.028 195.524 113.849 1.00 54.90  ? 4176 ARG A CB    1 
ATOM   20880 C  CG    . ARG A 1 4176 ? 164.467 195.047 115.217 1.00 55.92  ? 4176 ARG A CG    1 
ATOM   20881 C  CD    . ARG A 1 4176 ? 165.960 194.779 115.282 1.00 59.82  ? 4176 ARG A CD    1 
ATOM   20882 N  NE    . ARG A 1 4176 ? 166.321 193.503 114.680 1.00 66.94  ? 4176 ARG A NE    1 
ATOM   20883 C  CZ    . ARG A 1 4176 ? 167.174 193.362 113.675 1.00 69.49  ? 4176 ARG A CZ    1 
ATOM   20884 N  NH1   . ARG A 1 4176 ? 167.778 194.404 113.132 1.00 74.31  ? 4176 ARG A NH1   1 
ATOM   20885 N  NH2   . ARG A 1 4176 ? 167.430 192.145 113.207 1.00 67.82  ? 4176 ARG A NH2   1 
ATOM   20886 N  N     . ALA A 1 4177 ? 161.747 197.249 115.019 1.00 57.50  ? 4177 ALA A N     1 
ATOM   20887 C  CA    . ALA A 1 4177 ? 161.039 197.822 116.157 1.00 53.37  ? 4177 ALA A CA    1 
ATOM   20888 C  C     . ALA A 1 4177 ? 159.603 197.330 116.214 1.00 49.40  ? 4177 ALA A C     1 
ATOM   20889 O  O     . ALA A 1 4177 ? 159.152 196.831 117.254 1.00 49.21  ? 4177 ALA A O     1 
ATOM   20890 C  CB    . ALA A 1 4177 ? 161.081 199.348 116.087 1.00 54.18  ? 4177 ALA A CB    1 
ATOM   20891 N  N     . ARG A 1 4178 ? 158.888 197.402 115.087 1.00 48.90  ? 4178 ARG A N     1 
ATOM   20892 C  CA    . ARG A 1 4178 ? 157.502 196.953 115.078 1.00 47.55  ? 4178 ARG A CA    1 
ATOM   20893 C  C     . ARG A 1 4178 ? 157.384 195.511 115.538 1.00 47.11  ? 4178 ARG A C     1 
ATOM   20894 O  O     . ARG A 1 4178 ? 156.511 195.199 116.358 1.00 47.85  ? 4178 ARG A O     1 
ATOM   20895 C  CB    . ARG A 1 4178 ? 156.893 197.120 113.689 1.00 48.46  ? 4178 ARG A CB    1 
ATOM   20896 C  CG    . ARG A 1 4178 ? 155.432 196.735 113.641 1.00 49.37  ? 4178 ARG A CG    1 
ATOM   20897 C  CD    . ARG A 1 4178 ? 154.741 197.229 112.388 1.00 59.93  ? 4178 ARG A CD    1 
ATOM   20898 N  NE    . ARG A 1 4178 ? 154.740 198.683 112.299 1.00 62.04  ? 4178 ARG A NE    1 
ATOM   20899 C  CZ    . ARG A 1 4178 ? 153.645 199.423 112.199 1.00 64.23  ? 4178 ARG A CZ    1 
ATOM   20900 N  NH1   . ARG A 1 4178 ? 152.441 198.876 112.187 1.00 59.93  ? 4178 ARG A NH1   1 
ATOM   20901 N  NH2   . ARG A 1 4178 ? 153.760 200.744 112.114 1.00 73.28  ? 4178 ARG A NH2   1 
ATOM   20902 N  N     . LEU A 1 4179 ? 158.276 194.635 115.064 1.00 45.01  ? 4179 LEU A N     1 
ATOM   20903 C  CA    . LEU A 1 4179 ? 158.258 193.251 115.521 1.00 39.08  ? 4179 LEU A CA    1 
ATOM   20904 C  C     . LEU A 1 4179 ? 158.309 193.191 117.038 1.00 41.44  ? 4179 LEU A C     1 
ATOM   20905 O  O     . LEU A 1 4179 ? 157.436 192.587 117.676 1.00 48.69  ? 4179 LEU A O     1 
ATOM   20906 C  CB    . LEU A 1 4179 ? 159.426 192.478 114.910 1.00 38.37  ? 4179 LEU A CB    1 
ATOM   20907 C  CG    . LEU A 1 4179 ? 159.365 192.244 113.403 1.00 42.57  ? 4179 LEU A CG    1 
ATOM   20908 C  CD1   . LEU A 1 4179 ? 160.386 191.205 112.985 1.00 39.84  ? 4179 LEU A CD1   1 
ATOM   20909 C  CD2   . LEU A 1 4179 ? 157.973 191.813 113.003 1.00 47.86  ? 4179 LEU A CD2   1 
ATOM   20910 N  N     . TYR A 1 4180 ? 159.285 193.882 117.637 1.00 38.85  ? 4180 TYR A N     1 
ATOM   20911 C  CA    . TYR A 1 4180 ? 159.372 193.903 119.091 1.00 40.41  ? 4180 TYR A CA    1 
ATOM   20912 C  C     . TYR A 1 4180 ? 158.069 194.368 119.710 1.00 40.56  ? 4180 TYR A C     1 
ATOM   20913 O  O     . TYR A 1 4180 ? 157.573 193.735 120.651 1.00 42.18  ? 4180 TYR A O     1 
ATOM   20914 C  CB    . TYR A 1 4180 ? 160.527 194.790 119.545 1.00 45.48  ? 4180 TYR A CB    1 
ATOM   20915 C  CG    . TYR A 1 4180 ? 161.874 194.122 119.445 1.00 46.78  ? 4180 TYR A CG    1 
ATOM   20916 C  CD1   . TYR A 1 4180 ? 162.554 194.058 118.241 1.00 42.68  ? 4180 TYR A CD1   1 
ATOM   20917 C  CD2   . TYR A 1 4180 ? 162.465 193.553 120.562 1.00 48.08  ? 4180 TYR A CD2   1 
ATOM   20918 C  CE1   . TYR A 1 4180 ? 163.783 193.445 118.154 1.00 42.70  ? 4180 TYR A CE1   1 
ATOM   20919 C  CE2   . TYR A 1 4180 ? 163.692 192.942 120.483 1.00 49.38  ? 4180 TYR A CE2   1 
ATOM   20920 C  CZ    . TYR A 1 4180 ? 164.346 192.891 119.278 1.00 50.50  ? 4180 TYR A CZ    1 
ATOM   20921 O  OH    . TYR A 1 4180 ? 165.571 192.281 119.199 1.00 61.63  ? 4180 TYR A OH    1 
ATOM   20922 N  N     . PHE A 1 4181 ? 157.466 195.425 119.155 1.00 39.17  ? 4181 PHE A N     1 
ATOM   20923 C  CA    . PHE A 1 4181 ? 156.188 195.882 119.680 1.00 38.75  ? 4181 PHE A CA    1 
ATOM   20924 C  C     . PHE A 1 4181 ? 155.194 194.737 119.736 1.00 39.98  ? 4181 PHE A C     1 
ATOM   20925 O  O     . PHE A 1 4181 ? 154.671 194.416 120.812 1.00 44.06  ? 4181 PHE A O     1 
ATOM   20926 C  CB    . PHE A 1 4181 ? 155.641 197.022 118.826 1.00 43.51  ? 4181 PHE A CB    1 
ATOM   20927 C  CG    . PHE A 1 4181 ? 154.289 197.499 119.259 1.00 50.45  ? 4181 PHE A CG    1 
ATOM   20928 C  CD1   . PHE A 1 4181 ? 154.143 198.271 120.397 1.00 57.39  ? 4181 PHE A CD1   1 
ATOM   20929 C  CD2   . PHE A 1 4181 ? 153.161 197.167 118.532 1.00 49.33  ? 4181 PHE A CD2   1 
ATOM   20930 C  CE1   . PHE A 1 4181 ? 152.899 198.706 120.795 1.00 60.54  ? 4181 PHE A CE1   1 
ATOM   20931 C  CE2   . PHE A 1 4181 ? 151.917 197.598 118.928 1.00 51.25  ? 4181 PHE A CE2   1 
ATOM   20932 C  CZ    . PHE A 1 4181 ? 151.786 198.367 120.061 1.00 58.26  ? 4181 PHE A CZ    1 
ATOM   20933 N  N     . LEU A 1 4182 ? 155.000 194.045 118.609 1.00 39.25  ? 4182 LEU A N     1 
ATOM   20934 C  CA    . LEU A 1 4182 ? 154.101 192.899 118.608 1.00 33.84  ? 4182 LEU A CA    1 
ATOM   20935 C  C     . LEU A 1 4182 ? 154.510 191.911 119.680 1.00 34.64  ? 4182 LEU A C     1 
ATOM   20936 O  O     . LEU A 1 4182 ? 153.700 191.547 120.543 1.00 36.72  ? 4182 LEU A O     1 
ATOM   20937 C  CB    . LEU A 1 4182 ? 154.096 192.230 117.237 1.00 32.50  ? 4182 LEU A CB    1 
ATOM   20938 C  CG    . LEU A 1 4182 ? 153.420 193.005 116.113 1.00 39.25  ? 4182 LEU A CG    1 
ATOM   20939 C  CD1   . LEU A 1 4182 ? 153.511 192.226 114.820 1.00 41.45  ? 4182 LEU A CD1   1 
ATOM   20940 C  CD2   . LEU A 1 4182 ? 151.974 193.261 116.481 1.00 40.43  ? 4182 LEU A CD2   1 
ATOM   20941 N  N     . LEU A 1 4183 ? 155.792 191.539 119.694 1.00 35.84  ? 4183 LEU A N     1 
ATOM   20942 C  CA    . LEU A 1 4183 ? 156.275 190.619 120.710 1.00 35.02  ? 4183 LEU A CA    1 
ATOM   20943 C  C     . LEU A 1 4183 ? 155.954 191.147 122.097 1.00 36.03  ? 4183 LEU A C     1 
ATOM   20944 O  O     . LEU A 1 4183 ? 155.333 190.445 122.906 1.00 37.74  ? 4183 LEU A O     1 
ATOM   20945 C  CB    . LEU A 1 4183 ? 157.775 190.399 120.538 1.00 33.99  ? 4183 LEU A CB    1 
ATOM   20946 C  CG    . LEU A 1 4183 ? 158.437 189.450 121.529 1.00 42.01  ? 4183 LEU A CG    1 
ATOM   20947 C  CD1   . LEU A 1 4183 ? 157.725 188.115 121.514 1.00 39.78  ? 4183 LEU A CD1   1 
ATOM   20948 C  CD2   . LEU A 1 4183 ? 159.896 189.287 121.171 1.00 44.52  ? 4183 LEU A CD2   1 
ATOM   20949 N  N     . ALA A 1 4184 ? 156.286 192.418 122.353 1.00 38.08  ? 4184 ALA A N     1 
ATOM   20950 C  CA    . ALA A 1 4184 ? 155.962 193.011 123.643 1.00 33.96  ? 4184 ALA A CA    1 
ATOM   20951 C  C     . ALA A 1 4184 ? 154.482 192.856 123.940 1.00 34.39  ? 4184 ALA A C     1 
ATOM   20952 O  O     . ALA A 1 4184 ? 154.106 192.289 124.975 1.00 37.31  ? 4184 ALA A O     1 
ATOM   20953 C  CB    . ALA A 1 4184 ? 156.365 194.484 123.663 1.00 37.48  ? 4184 ALA A CB    1 
ATOM   20954 N  N     . TRP A 1 4185 ? 153.630 193.269 122.996 1.00 33.68  ? 4185 TRP A N     1 
ATOM   20955 C  CA    . TRP A 1 4185 ? 152.195 193.125 123.195 1.00 32.36  ? 4185 TRP A CA    1 
ATOM   20956 C  C     . TRP A 1 4185 ? 151.851 191.683 123.517 1.00 31.82  ? 4185 TRP A C     1 
ATOM   20957 O  O     . TRP A 1 4185 ? 151.220 191.404 124.546 1.00 35.33  ? 4185 TRP A O     1 
ATOM   20958 C  CB    . TRP A 1 4185 ? 151.442 193.605 121.955 1.00 32.09  ? 4185 TRP A CB    1 
ATOM   20959 C  CG    . TRP A 1 4185 ? 149.960 193.409 122.026 1.00 37.75  ? 4185 TRP A CG    1 
ATOM   20960 C  CD1   . TRP A 1 4185 ? 149.249 192.357 121.534 1.00 41.50  ? 4185 TRP A CD1   1 
ATOM   20961 C  CD2   . TRP A 1 4185 ? 149.004 194.295 122.621 1.00 45.82  ? 4185 TRP A CD2   1 
ATOM   20962 N  NE1   . TRP A 1 4185 ? 147.911 192.529 121.784 1.00 47.83  ? 4185 TRP A NE1   1 
ATOM   20963 C  CE2   . TRP A 1 4185 ? 147.734 193.712 122.453 1.00 50.57  ? 4185 TRP A CE2   1 
ATOM   20964 C  CE3   . TRP A 1 4185 ? 149.098 195.524 123.279 1.00 44.75  ? 4185 TRP A CE3   1 
ATOM   20965 C  CZ2   . TRP A 1 4185 ? 146.569 194.314 122.920 1.00 52.65  ? 4185 TRP A CZ2   1 
ATOM   20966 C  CZ3   . TRP A 1 4185 ? 147.942 196.119 123.741 1.00 45.50  ? 4185 TRP A CZ3   1 
ATOM   20967 C  CH2   . TRP A 1 4185 ? 146.694 195.515 123.560 1.00 48.85  ? 4185 TRP A CH2   1 
ATOM   20968 N  N     . PHE A 1 4186 ? 152.352 190.748 122.703 1.00 31.61  ? 4186 PHE A N     1 
ATOM   20969 C  CA    . PHE A 1 4186 ? 152.059 189.342 122.939 1.00 27.86  ? 4186 PHE A CA    1 
ATOM   20970 C  C     . PHE A 1 4186 ? 152.428 188.957 124.360 1.00 29.13  ? 4186 PHE A C     1 
ATOM   20971 O  O     . PHE A 1 4186 ? 151.597 188.411 125.097 1.00 31.41  ? 4186 PHE A O     1 
ATOM   20972 C  CB    . PHE A 1 4186 ? 152.805 188.473 121.927 1.00 30.74  ? 4186 PHE A CB    1 
ATOM   20973 C  CG    . PHE A 1 4186 ? 152.608 186.999 122.129 1.00 33.51  ? 4186 PHE A CG    1 
ATOM   20974 C  CD1   . PHE A 1 4186 ? 151.360 186.426 121.964 1.00 39.44  ? 4186 PHE A CD1   1 
ATOM   20975 C  CD2   . PHE A 1 4186 ? 153.668 186.187 122.484 1.00 34.16  ? 4186 PHE A CD2   1 
ATOM   20976 C  CE1   . PHE A 1 4186 ? 151.176 185.072 122.150 1.00 37.65  ? 4186 PHE A CE1   1 
ATOM   20977 C  CE2   . PHE A 1 4186 ? 153.488 184.834 122.671 1.00 35.24  ? 4186 PHE A CE2   1 
ATOM   20978 C  CZ    . PHE A 1 4186 ? 152.241 184.277 122.504 1.00 34.26  ? 4186 PHE A CZ    1 
ATOM   20979 N  N     . HIS A 1 4187 ? 153.639 189.323 124.791 1.00 30.19  ? 4187 HIS A N     1 
ATOM   20980 C  CA    . HIS A 1 4187 ? 154.064 188.983 126.141 1.00 27.76  ? 4187 HIS A CA    1 
ATOM   20981 C  C     . HIS A 1 4187 ? 153.067 189.508 127.158 1.00 34.32  ? 4187 HIS A C     1 
ATOM   20982 O  O     . HIS A 1 4187 ? 152.526 188.737 127.963 1.00 40.17  ? 4187 HIS A O     1 
ATOM   20983 C  CB    . HIS A 1 4187 ? 155.461 189.542 126.407 1.00 29.62  ? 4187 HIS A CB    1 
ATOM   20984 C  CG    . HIS A 1 4187 ? 156.173 188.877 127.542 1.00 37.17  ? 4187 HIS A CG    1 
ATOM   20985 N  ND1   . HIS A 1 4187 ? 156.550 187.552 127.510 1.00 39.08  ? 4187 HIS A ND1   1 
ATOM   20986 C  CD2   . HIS A 1 4187 ? 156.582 189.355 128.740 1.00 39.30  ? 4187 HIS A CD2   1 
ATOM   20987 C  CE1   . HIS A 1 4187 ? 157.158 187.242 128.640 1.00 40.52  ? 4187 HIS A CE1   1 
ATOM   20988 N  NE2   . HIS A 1 4187 ? 157.190 188.319 129.404 1.00 39.06  ? 4187 HIS A NE2   1 
ATOM   20989 N  N     . ALA A 1 4188 ? 152.735 190.798 127.074 1.00 32.49  ? 4188 ALA A N     1 
ATOM   20990 C  CA    . ALA A 1 4188 ? 151.766 191.350 128.009 1.00 26.11  ? 4188 ALA A CA    1 
ATOM   20991 C  C     . ALA A 1 4188 ? 150.480 190.546 127.970 1.00 31.92  ? 4188 ALA A C     1 
ATOM   20992 O  O     . ALA A 1 4188 ? 150.011 190.057 129.007 1.00 35.94  ? 4188 ALA A O     1 
ATOM   20993 C  CB    . ALA A 1 4188 ? 151.497 192.818 127.688 1.00 28.40  ? 4188 ALA A CB    1 
ATOM   20994 N  N     . ILE A 1 4189 ? 149.968 190.296 126.763 1.00 34.48  ? 4189 ILE A N     1 
ATOM   20995 C  CA    . ILE A 1 4189 ? 148.652 189.684 126.621 1.00 30.24  ? 4189 ILE A CA    1 
ATOM   20996 C  C     . ILE A 1 4189 ? 148.630 188.318 127.288 1.00 30.67  ? 4189 ILE A C     1 
ATOM   20997 O  O     . ILE A 1 4189 ? 147.597 187.882 127.806 1.00 38.33  ? 4189 ILE A O     1 
ATOM   20998 C  CB    . ILE A 1 4189 ? 148.255 189.608 125.136 1.00 31.74  ? 4189 ILE A CB    1 
ATOM   20999 C  CG1   . ILE A 1 4189 ? 147.954 191.009 124.614 1.00 36.86  ? 4189 ILE A CG1   1 
ATOM   21000 C  CG2   . ILE A 1 4189 ? 147.042 188.720 124.936 1.00 34.19  ? 4189 ILE A CG2   1 
ATOM   21001 C  CD1   . ILE A 1 4189 ? 146.858 191.712 125.373 1.00 37.39  ? 4189 ILE A CD1   1 
ATOM   21002 N  N     . ILE A 1 4190 ? 149.775 187.633 127.325 1.00 28.82  ? 4190 ILE A N     1 
ATOM   21003 C  CA    . ILE A 1 4190 ? 149.751 186.325 127.966 1.00 31.17  ? 4190 ILE A CA    1 
ATOM   21004 C  C     . ILE A 1 4190 ? 149.976 186.467 129.465 1.00 37.74  ? 4190 ILE A C     1 
ATOM   21005 O  O     . ILE A 1 4190 ? 149.267 185.846 130.268 1.00 43.89  ? 4190 ILE A O     1 
ATOM   21006 C  CB    . ILE A 1 4190 ? 150.751 185.356 127.303 1.00 33.53  ? 4190 ILE A CB    1 
ATOM   21007 C  CG1   . ILE A 1 4190 ? 152.198 185.772 127.536 1.00 31.65  ? 4190 ILE A CG1   1 
ATOM   21008 C  CG2   . ILE A 1 4190 ? 150.478 185.258 125.814 1.00 37.68  ? 4190 ILE A CG2   1 
ATOM   21009 C  CD1   . ILE A 1 4190 ? 153.182 184.693 127.219 1.00 35.56  ? 4190 ILE A CD1   1 
ATOM   21010 N  N     . GLN A 1 4191 ? 150.910 187.331 129.875 1.00 38.35  ? 4191 GLN A N     1 
ATOM   21011 C  CA    . GLN A 1 4191 ? 151.236 187.406 131.296 1.00 33.29  ? 4191 GLN A CA    1 
ATOM   21012 C  C     . GLN A 1 4191 ? 150.056 187.926 132.101 1.00 37.06  ? 4191 GLN A C     1 
ATOM   21013 O  O     . GLN A 1 4191 ? 149.683 187.333 133.120 1.00 36.72  ? 4191 GLN A O     1 
ATOM   21014 C  CB    . GLN A 1 4191 ? 152.470 188.275 131.519 1.00 34.06  ? 4191 GLN A CB    1 
ATOM   21015 C  CG    . GLN A 1 4191 ? 153.776 187.566 131.224 1.00 39.87  ? 4191 GLN A CG    1 
ATOM   21016 C  CD    . GLN A 1 4191 ? 154.968 188.274 131.826 1.00 43.75  ? 4191 GLN A CD    1 
ATOM   21017 O  OE1   . GLN A 1 4191 ? 155.240 189.432 131.513 1.00 48.94  ? 4191 GLN A OE1   1 
ATOM   21018 N  NE2   . GLN A 1 4191 ? 155.683 187.584 132.705 1.00 40.41  ? 4191 GLN A NE2   1 
ATOM   21019 N  N     . GLU A 1 4192 ? 149.437 189.015 131.643 1.00 37.32  ? 4192 GLU A N     1 
ATOM   21020 C  CA    . GLU A 1 4192 ? 148.206 189.477 132.264 1.00 36.89  ? 4192 GLU A CA    1 
ATOM   21021 C  C     . GLU A 1 4192 ? 147.130 188.406 132.233 1.00 36.23  ? 4192 GLU A C     1 
ATOM   21022 O  O     . GLU A 1 4192 ? 146.384 188.264 133.207 1.00 46.98  ? 4192 GLU A O     1 
ATOM   21023 C  CB    . GLU A 1 4192 ? 147.709 190.742 131.568 1.00 37.78  ? 4192 GLU A CB    1 
ATOM   21024 C  CG    . GLU A 1 4192 ? 148.719 191.872 131.574 1.00 46.66  ? 4192 GLU A CG    1 
ATOM   21025 C  CD    . GLU A 1 4192 ? 149.345 192.083 132.938 1.00 59.03  ? 4192 GLU A CD    1 
ATOM   21026 O  OE1   . GLU A 1 4192 ? 148.603 192.405 133.889 1.00 64.31  ? 4192 GLU A OE1   1 
ATOM   21027 O  OE2   . GLU A 1 4192 ? 150.578 191.924 133.061 1.00 52.32  ? 4192 GLU A OE2   1 
ATOM   21028 N  N     . ARG A 1 4193 ? 147.060 187.626 131.152 1.00 31.16  ? 4193 ARG A N     1 
ATOM   21029 C  CA    . ARG A 1 4193 ? 146.073 186.559 131.085 1.00 30.79  ? 4193 ARG A CA    1 
ATOM   21030 C  C     . ARG A 1 4193 ? 146.321 185.518 132.165 1.00 32.86  ? 4193 ARG A C     1 
ATOM   21031 O  O     . ARG A 1 4193 ? 145.375 184.880 132.644 1.00 36.79  ? 4193 ARG A O     1 
ATOM   21032 C  CB    . ARG A 1 4193 ? 146.098 185.927 129.697 1.00 30.88  ? 4193 ARG A CB    1 
ATOM   21033 C  CG    . ARG A 1 4193 ? 144.954 185.000 129.413 1.00 36.23  ? 4193 ARG A CG    1 
ATOM   21034 C  CD    . ARG A 1 4193 ? 144.859 184.693 127.936 1.00 34.34  ? 4193 ARG A CD    1 
ATOM   21035 N  NE    . ARG A 1 4193 ? 143.911 183.616 127.693 1.00 30.88  ? 4193 ARG A NE    1 
ATOM   21036 C  CZ    . ARG A 1 4193 ? 142.764 183.762 127.049 1.00 30.06  ? 4193 ARG A CZ    1 
ATOM   21037 N  NH1   . ARG A 1 4193 ? 142.399 184.929 126.546 1.00 29.92  ? 4193 ARG A NH1   1 
ATOM   21038 N  NH2   . ARG A 1 4193 ? 141.962 182.713 126.907 1.00 35.94  ? 4193 ARG A NH2   1 
ATOM   21039 N  N     . LEU A 1 4194 ? 147.578 185.364 132.587 1.00 33.68  ? 4194 LEU A N     1 
ATOM   21040 C  CA    . LEU A 1 4194 ? 147.896 184.421 133.651 1.00 34.85  ? 4194 LEU A CA    1 
ATOM   21041 C  C     . LEU A 1 4194 ? 147.217 184.806 134.956 1.00 38.07  ? 4194 LEU A C     1 
ATOM   21042 O  O     . LEU A 1 4194 ? 147.022 183.952 135.828 1.00 42.28  ? 4194 LEU A O     1 
ATOM   21043 C  CB    . LEU A 1 4194 ? 149.409 184.347 133.844 1.00 35.20  ? 4194 LEU A CB    1 
ATOM   21044 C  CG    . LEU A 1 4194 ? 150.143 183.310 132.998 1.00 36.30  ? 4194 LEU A CG    1 
ATOM   21045 C  CD1   . LEU A 1 4194 ? 151.641 183.471 133.151 1.00 38.21  ? 4194 LEU A CD1   1 
ATOM   21046 C  CD2   . LEU A 1 4194 ? 149.706 181.912 133.378 1.00 38.47  ? 4194 LEU A CD2   1 
ATOM   21047 N  N     . ARG A 1 4195 ? 146.855 186.082 135.113 1.00 35.97  ? 4195 ARG A N     1 
ATOM   21048 C  CA    . ARG A 1 4195 ? 146.143 186.496 136.316 1.00 33.32  ? 4195 ARG A CA    1 
ATOM   21049 C  C     . ARG A 1 4195 ? 144.763 185.861 136.386 1.00 37.62  ? 4195 ARG A C     1 
ATOM   21050 O  O     . ARG A 1 4195 ? 144.240 185.618 137.479 1.00 40.14  ? 4195 ARG A O     1 
ATOM   21051 C  CB    . ARG A 1 4195 ? 146.028 188.017 136.368 1.00 33.83  ? 4195 ARG A CB    1 
ATOM   21052 C  CG    . ARG A 1 4195 ? 147.354 188.748 136.404 1.00 39.95  ? 4195 ARG A CG    1 
ATOM   21053 C  CD    . ARG A 1 4195 ? 147.188 190.162 135.889 1.00 39.41  ? 4195 ARG A CD    1 
ATOM   21054 N  NE    . ARG A 1 4195 ? 145.948 190.757 136.370 1.00 46.64  ? 4195 ARG A NE    1 
ATOM   21055 C  CZ    . ARG A 1 4195 ? 145.480 191.934 135.981 1.00 59.75  ? 4195 ARG A CZ    1 
ATOM   21056 N  NH1   . ARG A 1 4195 ? 146.120 192.671 135.089 1.00 55.16  ? 4195 ARG A NH1   1 
ATOM   21057 N  NH2   . ARG A 1 4195 ? 144.340 192.383 136.498 1.00 63.79  ? 4195 ARG A NH2   1 
ATOM   21058 N  N     . TYR A 1 4196 ? 144.157 185.582 135.232 1.00 38.87  ? 4196 TYR A N     1 
ATOM   21059 C  CA    . TYR A 1 4196 ? 142.786 185.099 135.175 1.00 33.67  ? 4196 TYR A CA    1 
ATOM   21060 C  C     . TYR A 1 4196 ? 142.696 183.586 135.041 1.00 37.90  ? 4196 TYR A C     1 
ATOM   21061 O  O     . TYR A 1 4196 ? 141.684 183.077 134.549 1.00 42.70  ? 4196 TYR A O     1 
ATOM   21062 C  CB    . TYR A 1 4196 ? 142.044 185.781 134.028 1.00 32.02  ? 4196 TYR A CB    1 
ATOM   21063 C  CG    . TYR A 1 4196 ? 141.923 187.274 134.208 1.00 34.52  ? 4196 TYR A CG    1 
ATOM   21064 C  CD1   . TYR A 1 4196 ? 141.042 187.810 135.134 1.00 37.07  ? 4196 TYR A CD1   1 
ATOM   21065 C  CD2   . TYR A 1 4196 ? 142.706 188.146 133.469 1.00 32.76  ? 4196 TYR A CD2   1 
ATOM   21066 C  CE1   . TYR A 1 4196 ? 140.933 189.171 135.306 1.00 38.59  ? 4196 TYR A CE1   1 
ATOM   21067 C  CE2   . TYR A 1 4196 ? 142.605 189.509 133.636 1.00 37.19  ? 4196 TYR A CE2   1 
ATOM   21068 C  CZ    . TYR A 1 4196 ? 141.717 190.017 134.555 1.00 39.81  ? 4196 TYR A CZ    1 
ATOM   21069 O  OH    . TYR A 1 4196 ? 141.613 191.378 134.725 1.00 43.30  ? 4196 TYR A OH    1 
ATOM   21070 N  N     . ALA A 1 4197 ? 143.727 182.860 135.463 1.00 40.75  ? 4197 ALA A N     1 
ATOM   21071 C  CA    . ALA A 1 4197 ? 143.661 181.410 135.468 1.00 38.69  ? 4197 ALA A CA    1 
ATOM   21072 C  C     . ALA A 1 4197 ? 142.596 180.949 136.462 1.00 46.32  ? 4197 ALA A C     1 
ATOM   21073 O  O     . ALA A 1 4197 ? 142.362 181.606 137.480 1.00 51.94  ? 4197 ALA A O     1 
ATOM   21074 C  CB    . ALA A 1 4197 ? 145.020 180.816 135.829 1.00 35.07  ? 4197 ALA A CB    1 
ATOM   21075 N  N     . PRO A 1 4198 ? 141.932 179.816 136.197 1.00 42.75  ? 4198 PRO A N     1 
ATOM   21076 C  CA    . PRO A 1 4198 ? 142.144 178.874 135.094 1.00 38.75  ? 4198 PRO A CA    1 
ATOM   21077 C  C     . PRO A 1 4198 ? 141.390 179.247 133.825 1.00 37.99  ? 4198 PRO A C     1 
ATOM   21078 O  O     . PRO A 1 4198 ? 141.448 178.524 132.837 1.00 38.44  ? 4198 PRO A O     1 
ATOM   21079 C  CB    . PRO A 1 4198 ? 141.633 177.560 135.686 1.00 40.80  ? 4198 PRO A CB    1 
ATOM   21080 C  CG    . PRO A 1 4198 ? 140.485 177.991 136.554 1.00 45.30  ? 4198 PRO A CG    1 
ATOM   21081 C  CD    . PRO A 1 4198 ? 140.844 179.366 137.083 1.00 45.57  ? 4198 PRO A CD    1 
ATOM   21082 N  N     . LEU A 1 4199 ? 140.670 180.368 133.816 1.00 38.37  ? 4199 LEU A N     1 
ATOM   21083 C  CA    . LEU A 1 4199 ? 139.940 180.752 132.615 1.00 35.27  ? 4199 LEU A CA    1 
ATOM   21084 C  C     . LEU A 1 4199 ? 140.873 181.309 131.546 1.00 39.75  ? 4199 LEU A C     1 
ATOM   21085 O  O     . LEU A 1 4199 ? 140.694 181.029 130.356 1.00 45.80  ? 4199 LEU A O     1 
ATOM   21086 C  CB    . LEU A 1 4199 ? 138.851 181.764 132.965 1.00 31.67  ? 4199 LEU A CB    1 
ATOM   21087 C  CG    . LEU A 1 4199 ? 138.014 182.275 131.796 1.00 36.80  ? 4199 LEU A CG    1 
ATOM   21088 C  CD1   . LEU A 1 4199 ? 137.085 181.186 131.302 1.00 46.49  ? 4199 LEU A CD1   1 
ATOM   21089 C  CD2   . LEU A 1 4199 ? 137.220 183.493 132.208 1.00 41.23  ? 4199 LEU A CD2   1 
ATOM   21090 N  N     . GLY A 1 4200 ? 141.873 182.089 131.948 1.00 43.69  ? 4200 GLY A N     1 
ATOM   21091 C  CA    . GLY A 1 4200 ? 142.846 182.614 131.010 1.00 35.95  ? 4200 GLY A CA    1 
ATOM   21092 C  C     . GLY A 1 4200 ? 143.772 181.539 130.484 1.00 36.78  ? 4200 GLY A C     1 
ATOM   21093 O  O     . GLY A 1 4200 ? 143.794 181.259 129.282 1.00 40.92  ? 4200 GLY A O     1 
ATOM   21094 N  N     . TRP A 1 4201 ? 144.548 180.935 131.379 1.00 33.79  ? 4201 TRP A N     1 
ATOM   21095 C  CA    . TRP A 1 4201 ? 145.358 179.764 131.080 1.00 31.55  ? 4201 TRP A CA    1 
ATOM   21096 C  C     . TRP A 1 4201 ? 144.926 178.640 132.007 1.00 34.74  ? 4201 TRP A C     1 
ATOM   21097 O  O     . TRP A 1 4201 ? 144.612 178.884 133.175 1.00 44.24  ? 4201 TRP A O     1 
ATOM   21098 C  CB    . TRP A 1 4201 ? 146.853 180.051 131.264 1.00 30.24  ? 4201 TRP A CB    1 
ATOM   21099 C  CG    . TRP A 1 4201 ? 147.418 181.005 130.263 1.00 32.64  ? 4201 TRP A CG    1 
ATOM   21100 C  CD1   . TRP A 1 4201 ? 147.720 182.317 130.465 1.00 34.74  ? 4201 TRP A CD1   1 
ATOM   21101 C  CD2   . TRP A 1 4201 ? 147.754 180.722 128.901 1.00 31.75  ? 4201 TRP A CD2   1 
ATOM   21102 N  NE1   . TRP A 1 4201 ? 148.220 182.872 129.315 1.00 31.70  ? 4201 TRP A NE1   1 
ATOM   21103 C  CE2   . TRP A 1 4201 ? 148.251 181.912 128.339 1.00 31.82  ? 4201 TRP A CE2   1 
ATOM   21104 C  CE3   . TRP A 1 4201 ? 147.682 179.579 128.103 1.00 33.08  ? 4201 TRP A CE3   1 
ATOM   21105 C  CZ2   . TRP A 1 4201 ? 148.673 181.991 127.016 1.00 32.07  ? 4201 TRP A CZ2   1 
ATOM   21106 C  CZ3   . TRP A 1 4201 ? 148.103 179.660 126.793 1.00 34.07  ? 4201 TRP A CZ3   1 
ATOM   21107 C  CH2   . TRP A 1 4201 ? 148.592 180.857 126.262 1.00 33.77  ? 4201 TRP A CH2   1 
ATOM   21108 N  N     . SER A 1 4202 ? 144.909 177.408 131.491 1.00 31.74  ? 4202 SER A N     1 
ATOM   21109 C  CA    . SER A 1 4202 ? 144.419 176.288 132.289 1.00 33.86  ? 4202 SER A CA    1 
ATOM   21110 C  C     . SER A 1 4202 ? 145.237 176.098 133.560 1.00 36.22  ? 4202 SER A C     1 
ATOM   21111 O  O     . SER A 1 4202 ? 144.724 175.576 134.556 1.00 41.62  ? 4202 SER A O     1 
ATOM   21112 C  CB    . SER A 1 4202 ? 144.420 175.006 131.459 1.00 37.22  ? 4202 SER A CB    1 
ATOM   21113 O  OG    . SER A 1 4202 ? 145.725 174.467 131.357 1.00 44.49  ? 4202 SER A OG    1 
ATOM   21114 N  N     . LYS A 1 4203 ? 146.501 176.511 133.548 1.00 34.77  ? 4203 LYS A N     1 
ATOM   21115 C  CA    . LYS A 1 4203 ? 147.316 176.529 134.752 1.00 37.16  ? 4203 LYS A CA    1 
ATOM   21116 C  C     . LYS A 1 4203 ? 148.282 177.699 134.658 1.00 35.18  ? 4203 LYS A C     1 
ATOM   21117 O  O     . LYS A 1 4203 ? 148.505 178.259 133.583 1.00 35.05  ? 4203 LYS A O     1 
ATOM   21118 C  CB    . LYS A 1 4203 ? 148.073 175.212 134.957 1.00 34.82  ? 4203 LYS A CB    1 
ATOM   21119 C  CG    . LYS A 1 4203 ? 149.018 174.852 133.834 1.00 37.03  ? 4203 LYS A CG    1 
ATOM   21120 C  CD    . LYS A 1 4203 ? 149.297 173.360 133.806 1.00 44.63  ? 4203 LYS A CD    1 
ATOM   21121 C  CE    . LYS A 1 4203 ? 148.050 172.572 133.449 1.00 51.84  ? 4203 LYS A CE    1 
ATOM   21122 N  NZ    . LYS A 1 4203 ? 148.326 171.113 133.347 1.00 54.96  ? 4203 LYS A NZ    1 
ATOM   21123 N  N     . LYS A 1 4204 ? 148.846 178.072 135.803 1.00 36.32  ? 4204 LYS A N     1 
ATOM   21124 C  CA    . LYS A 1 4204 ? 149.732 179.231 135.881 1.00 37.76  ? 4204 LYS A CA    1 
ATOM   21125 C  C     . LYS A 1 4204 ? 151.115 178.823 135.393 1.00 37.80  ? 4204 LYS A C     1 
ATOM   21126 O  O     . LYS A 1 4204 ? 151.937 178.294 136.141 1.00 40.42  ? 4204 LYS A O     1 
ATOM   21127 C  CB    . LYS A 1 4204 ? 149.778 179.780 137.301 1.00 41.11  ? 4204 LYS A CB    1 
ATOM   21128 C  CG    . LYS A 1 4204 ? 148.450 180.333 137.787 1.00 48.07  ? 4204 LYS A CG    1 
ATOM   21129 C  CD    . LYS A 1 4204 ? 148.642 181.601 138.598 1.00 51.63  ? 4204 LYS A CD    1 
ATOM   21130 C  CE    . LYS A 1 4204 ? 147.311 182.260 138.913 1.00 52.90  ? 4204 LYS A CE    1 
ATOM   21131 N  NZ    . LYS A 1 4204 ? 147.490 183.548 139.635 1.00 51.30  ? 4204 LYS A NZ    1 
ATOM   21132 N  N     . TYR A 1 4205 ? 151.371 179.072 134.112 1.00 35.60  ? 4205 TYR A N     1 
ATOM   21133 C  CA    . TYR A 1 4205 ? 152.681 178.812 133.543 1.00 33.00  ? 4205 TYR A CA    1 
ATOM   21134 C  C     . TYR A 1 4205 ? 153.661 179.905 133.952 1.00 42.38  ? 4205 TYR A C     1 
ATOM   21135 O  O     . TYR A 1 4205 ? 153.277 181.005 134.354 1.00 50.93  ? 4205 TYR A O     1 
ATOM   21136 C  CB    . TYR A 1 4205 ? 152.601 178.732 132.021 1.00 33.29  ? 4205 TYR A CB    1 
ATOM   21137 C  CG    . TYR A 1 4205 ? 151.678 177.655 131.513 1.00 30.86  ? 4205 TYR A CG    1 
ATOM   21138 C  CD1   . TYR A 1 4205 ? 152.009 176.316 131.637 1.00 32.16  ? 4205 TYR A CD1   1 
ATOM   21139 C  CD2   . TYR A 1 4205 ? 150.475 177.979 130.912 1.00 31.09  ? 4205 TYR A CD2   1 
ATOM   21140 C  CE1   . TYR A 1 4205 ? 151.168 175.332 131.174 1.00 34.20  ? 4205 TYR A CE1   1 
ATOM   21141 C  CE2   . TYR A 1 4205 ? 149.629 177.003 130.447 1.00 30.29  ? 4205 TYR A CE2   1 
ATOM   21142 C  CZ    . TYR A 1 4205 ? 149.978 175.681 130.581 1.00 31.39  ? 4205 TYR A CZ    1 
ATOM   21143 O  OH    . TYR A 1 4205 ? 149.131 174.703 130.117 1.00 35.85  ? 4205 TYR A OH    1 
ATOM   21144 N  N     . GLU A 1 4206 ? 154.946 179.586 133.853 1.00 44.05  ? 4206 GLU A N     1 
ATOM   21145 C  CA    . GLU A 1 4206 ? 155.995 180.538 134.206 1.00 46.17  ? 4206 GLU A CA    1 
ATOM   21146 C  C     . GLU A 1 4206 ? 156.481 181.323 132.992 1.00 46.34  ? 4206 GLU A C     1 
ATOM   21147 O  O     . GLU A 1 4206 ? 157.674 181.371 132.701 1.00 54.29  ? 4206 GLU A O     1 
ATOM   21148 C  CB    . GLU A 1 4206 ? 157.148 179.810 134.885 1.00 50.18  ? 4206 GLU A CB    1 
ATOM   21149 C  CG    . GLU A 1 4206 ? 156.750 179.070 136.148 1.00 59.62  ? 4206 GLU A CG    1 
ATOM   21150 C  CD    . GLU A 1 4206 ? 157.937 178.453 136.860 1.00 76.30  ? 4206 GLU A CD    1 
ATOM   21151 O  OE1   . GLU A 1 4206 ? 157.950 178.457 138.109 1.00 78.06  ? 4206 GLU A OE1   1 
ATOM   21152 O  OE2   . GLU A 1 4206 ? 158.857 177.963 136.171 1.00 73.04  ? 4206 GLU A OE2   1 
ATOM   21153 N  N     . PHE A 1 4207 ? 155.554 181.947 132.268 1.00 40.58  ? 4207 PHE A N     1 
ATOM   21154 C  CA    . PHE A 1 4207 ? 155.945 182.868 131.211 1.00 41.93  ? 4207 PHE A CA    1 
ATOM   21155 C  C     . PHE A 1 4207 ? 156.610 184.086 131.834 1.00 47.98  ? 4207 PHE A C     1 
ATOM   21156 O  O     . PHE A 1 4207 ? 155.985 184.818 132.606 1.00 53.52  ? 4207 PHE A O     1 
ATOM   21157 C  CB    . PHE A 1 4207 ? 154.734 183.293 130.383 1.00 40.94  ? 4207 PHE A CB    1 
ATOM   21158 C  CG    . PHE A 1 4207 ? 153.981 182.148 129.769 1.00 39.92  ? 4207 PHE A CG    1 
ATOM   21159 C  CD1   . PHE A 1 4207 ? 154.638 181.191 129.019 1.00 40.47  ? 4207 PHE A CD1   1 
ATOM   21160 C  CD2   . PHE A 1 4207 ? 152.611 182.039 129.930 1.00 33.60  ? 4207 PHE A CD2   1 
ATOM   21161 C  CE1   . PHE A 1 4207 ? 153.945 180.141 128.452 1.00 35.38  ? 4207 PHE A CE1   1 
ATOM   21162 C  CE2   . PHE A 1 4207 ? 151.916 180.993 129.364 1.00 30.41  ? 4207 PHE A CE2   1 
ATOM   21163 C  CZ    . PHE A 1 4207 ? 152.583 180.044 128.624 1.00 26.86  ? 4207 PHE A CZ    1 
ATOM   21164 N  N     . GLY A 1 4208 ? 157.870 184.306 131.502 1.00 48.35  ? 4208 GLY A N     1 
ATOM   21165 C  CA    . GLY A 1 4208 ? 158.623 185.351 132.149 1.00 48.70  ? 4208 GLY A CA    1 
ATOM   21166 C  C     . GLY A 1 4208 ? 159.670 185.956 131.252 1.00 46.87  ? 4208 GLY A C     1 
ATOM   21167 O  O     . GLY A 1 4208 ? 159.556 185.930 130.026 1.00 44.94  ? 4208 GLY A O     1 
ATOM   21168 N  N     . GLU A 1 4209 ? 160.703 186.511 131.889 1.00 50.36  ? 4209 GLU A N     1 
ATOM   21169 C  CA    . GLU A 1 4209 ? 161.741 187.223 131.153 1.00 48.16  ? 4209 GLU A CA    1 
ATOM   21170 C  C     . GLU A 1 4209 ? 162.538 186.294 130.250 1.00 49.91  ? 4209 GLU A C     1 
ATOM   21171 O  O     . GLU A 1 4209 ? 163.000 186.719 129.187 1.00 50.06  ? 4209 GLU A O     1 
ATOM   21172 C  CB    . GLU A 1 4209 ? 162.672 187.944 132.128 1.00 53.25  ? 4209 GLU A CB    1 
ATOM   21173 C  CG    . GLU A 1 4209 ? 163.775 188.756 131.463 1.00 64.57  ? 4209 GLU A CG    1 
ATOM   21174 C  CD    . GLU A 1 4209 ? 163.244 189.921 130.648 1.00 72.35  ? 4209 GLU A CD    1 
ATOM   21175 O  OE1   . GLU A 1 4209 ? 162.138 190.413 130.955 1.00 78.02  ? 4209 GLU A OE1   1 
ATOM   21176 O  OE2   . GLU A 1 4209 ? 163.938 190.347 129.700 1.00 67.69  ? 4209 GLU A OE2   1 
ATOM   21177 N  N     . SER A 1 4210 ? 162.721 185.035 130.651 1.00 48.50  ? 4210 SER A N     1 
ATOM   21178 C  CA    . SER A 1 4210 ? 163.507 184.110 129.839 1.00 50.58  ? 4210 SER A CA    1 
ATOM   21179 C  C     . SER A 1 4210 ? 162.859 183.886 128.478 1.00 48.49  ? 4210 SER A C     1 
ATOM   21180 O  O     . SER A 1 4210 ? 163.537 183.894 127.443 1.00 47.85  ? 4210 SER A O     1 
ATOM   21181 C  CB    . SER A 1 4210 ? 163.684 182.786 130.580 1.00 51.71  ? 4210 SER A CB    1 
ATOM   21182 O  OG    . SER A 1 4210 ? 162.429 182.216 130.904 1.00 55.63  ? 4210 SER A OG    1 
ATOM   21183 N  N     . ASP A 1 4211 ? 161.537 183.696 128.461 1.00 45.78  ? 4211 ASP A N     1 
ATOM   21184 C  CA    . ASP A 1 4211 ? 160.832 183.521 127.196 1.00 38.78  ? 4211 ASP A CA    1 
ATOM   21185 C  C     . ASP A 1 4211 ? 160.902 184.781 126.346 1.00 41.15  ? 4211 ASP A C     1 
ATOM   21186 O  O     . ASP A 1 4211 ? 161.044 184.704 125.122 1.00 48.63  ? 4211 ASP A O     1 
ATOM   21187 C  CB    . ASP A 1 4211 ? 159.380 183.125 127.450 1.00 40.53  ? 4211 ASP A CB    1 
ATOM   21188 C  CG    . ASP A 1 4211 ? 159.258 181.876 128.291 1.00 51.00  ? 4211 ASP A CG    1 
ATOM   21189 O  OD1   . ASP A 1 4211 ? 159.842 180.842 127.908 1.00 55.25  ? 4211 ASP A OD1   1 
ATOM   21190 O  OD2   . ASP A 1 4211 ? 158.575 181.922 129.333 1.00 53.56  ? 4211 ASP A OD2   1 
ATOM   21191 N  N     . LEU A 1 4212 ? 160.800 185.953 126.975 1.00 38.51  ? 4212 LEU A N     1 
ATOM   21192 C  CA    . LEU A 1 4212 ? 160.886 187.202 126.227 1.00 35.30  ? 4212 LEU A CA    1 
ATOM   21193 C  C     . LEU A 1 4212 ? 162.262 187.370 125.595 1.00 40.78  ? 4212 LEU A C     1 
ATOM   21194 O  O     . LEU A 1 4212 ? 162.378 187.783 124.436 1.00 47.08  ? 4212 LEU A O     1 
ATOM   21195 C  CB    . LEU A 1 4212 ? 160.564 188.381 127.141 1.00 42.83  ? 4212 LEU A CB    1 
ATOM   21196 C  CG    . LEU A 1 4212 ? 160.553 189.761 126.486 1.00 44.32  ? 4212 LEU A CG    1 
ATOM   21197 C  CD1   . LEU A 1 4212 ? 159.513 189.827 125.383 1.00 35.40  ? 4212 LEU A CD1   1 
ATOM   21198 C  CD2   . LEU A 1 4212 ? 160.300 190.829 127.531 1.00 48.08  ? 4212 LEU A CD2   1 
ATOM   21199 N  N     . ARG A 1 4213 ? 163.321 187.055 126.344 1.00 39.68  ? 4213 ARG A N     1 
ATOM   21200 C  CA    . ARG A 1 4213 ? 164.669 187.143 125.792 1.00 40.15  ? 4213 ARG A CA    1 
ATOM   21201 C  C     . ARG A 1 4213 ? 164.868 186.147 124.658 1.00 45.59  ? 4213 ARG A C     1 
ATOM   21202 O  O     . ARG A 1 4213 ? 165.476 186.478 123.634 1.00 48.94  ? 4213 ARG A O     1 
ATOM   21203 C  CB    . ARG A 1 4213 ? 165.711 186.917 126.887 1.00 45.98  ? 4213 ARG A CB    1 
ATOM   21204 C  CG    . ARG A 1 4213 ? 165.629 187.892 128.048 1.00 57.34  ? 4213 ARG A CG    1 
ATOM   21205 C  CD    . ARG A 1 4213 ? 166.941 187.946 128.815 1.00 71.67  ? 4213 ARG A CD    1 
ATOM   21206 N  NE    . ARG A 1 4213 ? 168.094 187.995 127.924 1.00 81.01  ? 4213 ARG A NE    1 
ATOM   21207 C  CZ    . ARG A 1 4213 ? 168.775 189.096 127.640 1.00 76.17  ? 4213 ARG A CZ    1 
ATOM   21208 N  NH1   . ARG A 1 4213 ? 168.449 190.266 128.165 1.00 71.22  ? 4213 ARG A NH1   1 
ATOM   21209 N  NH2   . ARG A 1 4213 ? 169.810 189.023 126.807 1.00 66.63  ? 4213 ARG A NH2   1 
ATOM   21210 N  N     . SER A 1 4214 ? 164.365 184.921 124.821 1.00 43.63  ? 4214 SER A N     1 
ATOM   21211 C  CA    . SER A 1 4214 ? 164.492 183.930 123.757 1.00 33.74  ? 4214 SER A CA    1 
ATOM   21212 C  C     . SER A 1 4214 ? 163.743 184.366 122.505 1.00 35.49  ? 4214 SER A C     1 
ATOM   21213 O  O     . SER A 1 4214 ? 164.241 184.202 121.386 1.00 41.61  ? 4214 SER A O     1 
ATOM   21214 C  CB    . SER A 1 4214 ? 163.988 182.572 124.241 1.00 30.23  ? 4214 SER A CB    1 
ATOM   21215 O  OG    . SER A 1 4214 ? 164.673 182.165 125.411 1.00 39.90  ? 4214 SER A OG    1 
ATOM   21216 N  N     . ALA A 1 4215 ? 162.545 184.929 122.674 1.00 33.03  ? 4215 ALA A N     1 
ATOM   21217 C  CA    . ALA A 1 4215 ? 161.773 185.391 121.527 1.00 30.51  ? 4215 ALA A CA    1 
ATOM   21218 C  C     . ALA A 1 4215 ? 162.445 186.575 120.845 1.00 36.87  ? 4215 ALA A C     1 
ATOM   21219 O  O     . ALA A 1 4215 ? 162.448 186.666 119.613 1.00 43.92  ? 4215 ALA A O     1 
ATOM   21220 C  CB    . ALA A 1 4215 ? 160.358 185.750 121.967 1.00 28.19  ? 4215 ALA A CB    1 
ATOM   21221 N  N     . CYS A 1 4216 ? 163.015 187.494 121.627 1.00 40.52  ? 4216 CYS A N     1 
ATOM   21222 C  CA    . CYS A 1 4216 ? 163.750 188.609 121.040 1.00 42.16  ? 4216 CYS A CA    1 
ATOM   21223 C  C     . CYS A 1 4216 ? 164.963 188.116 120.264 1.00 47.05  ? 4216 CYS A C     1 
ATOM   21224 O  O     . CYS A 1 4216 ? 165.260 188.620 119.175 1.00 48.71  ? 4216 CYS A O     1 
ATOM   21225 C  CB    . CYS A 1 4216 ? 164.176 189.591 122.130 1.00 45.69  ? 4216 CYS A CB    1 
ATOM   21226 S  SG    . CYS A 1 4216 ? 162.820 190.513 122.883 1.00 65.88  ? 4216 CYS A SG    1 
ATOM   21227 N  N     . ASP A 1 4217 ? 165.677 187.129 120.809 1.00 46.72  ? 4217 ASP A N     1 
ATOM   21228 C  CA    . ASP A 1 4217 ? 166.817 186.558 120.102 1.00 45.23  ? 4217 ASP A CA    1 
ATOM   21229 C  C     . ASP A 1 4217 ? 166.382 185.887 118.806 1.00 47.16  ? 4217 ASP A C     1 
ATOM   21230 O  O     . ASP A 1 4217 ? 167.056 186.014 117.777 1.00 52.04  ? 4217 ASP A O     1 
ATOM   21231 C  CB    . ASP A 1 4217 ? 167.540 185.561 121.005 1.00 46.33  ? 4217 ASP A CB    1 
ATOM   21232 C  CG    . ASP A 1 4217 ? 168.238 186.231 122.170 1.00 59.76  ? 4217 ASP A CG    1 
ATOM   21233 O  OD1   . ASP A 1 4217 ? 168.649 187.401 122.028 1.00 64.97  ? 4217 ASP A OD1   1 
ATOM   21234 O  OD2   . ASP A 1 4217 ? 168.374 185.589 123.232 1.00 62.95  ? 4217 ASP A OD2   1 
ATOM   21235 N  N     . THR A 1 4218 ? 165.264 185.160 118.842 1.00 42.53  ? 4218 THR A N     1 
ATOM   21236 C  CA    . THR A 1 4218 ? 164.741 184.525 117.635 1.00 40.66  ? 4218 THR A CA    1 
ATOM   21237 C  C     . THR A 1 4218 ? 164.385 185.564 116.580 1.00 42.25  ? 4218 THR A C     1 
ATOM   21238 O  O     . THR A 1 4218 ? 164.708 185.404 115.395 1.00 51.05  ? 4218 THR A O     1 
ATOM   21239 C  CB    . THR A 1 4218 ? 163.519 183.677 117.985 1.00 38.95  ? 4218 THR A CB    1 
ATOM   21240 O  OG1   . THR A 1 4218 ? 163.913 182.593 118.835 1.00 35.37  ? 4218 THR A OG1   1 
ATOM   21241 C  CG2   . THR A 1 4218 ? 162.868 183.128 116.730 1.00 40.21  ? 4218 THR A CG2   1 
ATOM   21242 N  N     . VAL A 1 4219 ? 163.716 186.640 116.997 1.00 42.63  ? 4219 VAL A N     1 
ATOM   21243 C  CA    . VAL A 1 4219 ? 163.359 187.707 116.066 1.00 41.87  ? 4219 VAL A CA    1 
ATOM   21244 C  C     . VAL A 1 4219 ? 164.615 188.316 115.461 1.00 45.45  ? 4219 VAL A C     1 
ATOM   21245 O  O     . VAL A 1 4219 ? 164.702 188.521 114.246 1.00 51.43  ? 4219 VAL A O     1 
ATOM   21246 C  CB    . VAL A 1 4219 ? 162.496 188.770 116.768 1.00 38.13  ? 4219 VAL A CB    1 
ATOM   21247 C  CG1   . VAL A 1 4219 ? 162.368 190.008 115.900 1.00 38.41  ? 4219 VAL A CG1   1 
ATOM   21248 C  CG2   . VAL A 1 4219 ? 161.125 188.207 117.091 1.00 36.99  ? 4219 VAL A CG2   1 
ATOM   21249 N  N     . ASP A 1 4220 ? 165.619 188.591 116.299 1.00 45.65  ? 4220 ASP A N     1 
ATOM   21250 C  CA    . ASP A 1 4220 ? 166.870 189.153 115.800 1.00 51.21  ? 4220 ASP A CA    1 
ATOM   21251 C  C     . ASP A 1 4220 ? 167.504 188.243 114.759 1.00 55.61  ? 4220 ASP A C     1 
ATOM   21252 O  O     . ASP A 1 4220 ? 167.845 188.688 113.658 1.00 59.96  ? 4220 ASP A O     1 
ATOM   21253 C  CB    . ASP A 1 4220 ? 167.842 189.392 116.954 1.00 56.60  ? 4220 ASP A CB    1 
ATOM   21254 C  CG    . ASP A 1 4220 ? 167.504 190.628 117.754 1.00 68.50  ? 4220 ASP A CG    1 
ATOM   21255 O  OD1   . ASP A 1 4220 ? 167.384 191.714 117.150 1.00 70.57  ? 4220 ASP A OD1   1 
ATOM   21256 O  OD2   . ASP A 1 4220 ? 167.367 190.520 118.991 1.00 68.31  ? 4220 ASP A OD2   1 
ATOM   21257 N  N     . THR A 1 4221 ? 167.656 186.957 115.085 1.00 54.49  ? 4221 THR A N     1 
ATOM   21258 C  CA    . THR A 1 4221 ? 168.343 186.041 114.180 1.00 53.04  ? 4221 THR A CA    1 
ATOM   21259 C  C     . THR A 1 4221 ? 167.601 185.910 112.857 1.00 51.99  ? 4221 THR A C     1 
ATOM   21260 O  O     . THR A 1 4221 ? 168.200 186.036 111.781 1.00 60.91  ? 4221 THR A O     1 
ATOM   21261 C  CB    . THR A 1 4221 ? 168.509 184.669 114.834 1.00 45.39  ? 4221 THR A CB    1 
ATOM   21262 O  OG1   . THR A 1 4221 ? 167.228 184.169 115.231 1.00 45.49  ? 4221 THR A OG1   1 
ATOM   21263 C  CG2   . THR A 1 4221 ? 169.415 184.760 116.049 1.00 48.74  ? 4221 THR A CG2   1 
ATOM   21264 N  N     . TRP A 1 4222 ? 166.289 185.675 112.911 1.00 47.87  ? 4222 TRP A N     1 
ATOM   21265 C  CA    . TRP A 1 4222 ? 165.554 185.429 111.676 1.00 47.87  ? 4222 TRP A CA    1 
ATOM   21266 C  C     . TRP A 1 4222 ? 165.416 186.695 110.840 1.00 54.22  ? 4222 TRP A C     1 
ATOM   21267 O  O     . TRP A 1 4222 ? 165.500 186.639 109.608 1.00 62.90  ? 4222 TRP A O     1 
ATOM   21268 C  CB    . TRP A 1 4222 ? 164.193 184.816 111.991 1.00 39.06  ? 4222 TRP A CB    1 
ATOM   21269 C  CG    . TRP A 1 4222 ? 164.321 183.377 112.357 1.00 40.31  ? 4222 TRP A CG    1 
ATOM   21270 C  CD1   . TRP A 1 4222 ? 164.397 182.856 113.612 1.00 36.10  ? 4222 TRP A CD1   1 
ATOM   21271 C  CD2   . TRP A 1 4222 ? 164.419 182.270 111.456 1.00 40.66  ? 4222 TRP A CD2   1 
ATOM   21272 N  NE1   . TRP A 1 4222 ? 164.529 181.493 113.550 1.00 34.02  ? 4222 TRP A NE1   1 
ATOM   21273 C  CE2   . TRP A 1 4222 ? 164.542 181.107 112.236 1.00 34.31  ? 4222 TRP A CE2   1 
ATOM   21274 C  CE3   . TRP A 1 4222 ? 164.408 182.149 110.064 1.00 42.97  ? 4222 TRP A CE3   1 
ATOM   21275 C  CZ2   . TRP A 1 4222 ? 164.652 179.841 111.674 1.00 32.87  ? 4222 TRP A CZ2   1 
ATOM   21276 C  CZ3   . TRP A 1 4222 ? 164.518 180.892 109.508 1.00 36.79  ? 4222 TRP A CZ3   1 
ATOM   21277 C  CH2   . TRP A 1 4222 ? 164.638 179.754 110.311 1.00 35.06  ? 4222 TRP A CH2   1 
ATOM   21278 N  N     . LEU A 1 4223 ? 165.232 187.850 111.482 1.00 53.23  ? 4223 LEU A N     1 
ATOM   21279 C  CA    . LEU A 1 4223 ? 165.126 189.089 110.725 1.00 57.19  ? 4223 LEU A CA    1 
ATOM   21280 C  C     . LEU A 1 4223 ? 166.469 189.483 110.124 1.00 63.08  ? 4223 LEU A C     1 
ATOM   21281 O  O     . LEU A 1 4223 ? 166.518 190.065 109.036 1.00 67.73  ? 4223 LEU A O     1 
ATOM   21282 C  CB    . LEU A 1 4223 ? 164.580 190.199 111.619 1.00 51.99  ? 4223 LEU A CB    1 
ATOM   21283 C  CG    . LEU A 1 4223 ? 164.109 191.454 110.893 1.00 55.63  ? 4223 LEU A CG    1 
ATOM   21284 C  CD1   . LEU A 1 4223 ? 162.920 191.128 110.014 1.00 56.86  ? 4223 LEU A CD1   1 
ATOM   21285 C  CD2   . LEU A 1 4223 ? 163.747 192.518 111.895 1.00 56.53  ? 4223 LEU A CD2   1 
ATOM   21286 N  N     . ASP A 1 4224 ? 167.572 189.176 110.814 1.00 59.39  ? 4224 ASP A N     1 
ATOM   21287 C  CA    . ASP A 1 4224 ? 168.890 189.408 110.234 1.00 63.81  ? 4224 ASP A CA    1 
ATOM   21288 C  C     . ASP A 1 4224 ? 169.135 188.489 109.046 1.00 71.41  ? 4224 ASP A C     1 
ATOM   21289 O  O     . ASP A 1 4224 ? 169.715 188.907 108.037 1.00 77.17  ? 4224 ASP A O     1 
ATOM   21290 C  CB    . ASP A 1 4224 ? 169.971 189.212 111.295 1.00 66.60  ? 4224 ASP A CB    1 
ATOM   21291 C  CG    . ASP A 1 4224 ? 170.030 190.356 112.283 1.00 73.86  ? 4224 ASP A CG    1 
ATOM   21292 O  OD1   . ASP A 1 4224 ? 169.282 191.338 112.098 1.00 76.51  ? 4224 ASP A OD1   1 
ATOM   21293 O  OD2   . ASP A 1 4224 ? 170.820 190.272 113.246 1.00 68.96  ? 4224 ASP A OD2   1 
ATOM   21294 N  N     . ASP A 1 4225 ? 168.711 187.227 109.152 1.00 70.76  ? 4225 ASP A N     1 
ATOM   21295 C  CA    . ASP A 1 4225 ? 168.851 186.307 108.028 1.00 74.53  ? 4225 ASP A CA    1 
ATOM   21296 C  C     . ASP A 1 4225 ? 168.030 186.768 106.831 1.00 77.53  ? 4225 ASP A C     1 
ATOM   21297 O  O     . ASP A 1 4225 ? 168.490 186.689 105.686 1.00 81.81  ? 4225 ASP A O     1 
ATOM   21298 C  CB    . ASP A 1 4225 ? 168.439 184.896 108.447 1.00 74.46  ? 4225 ASP A CB    1 
ATOM   21299 C  CG    . ASP A 1 4225 ? 169.296 184.349 109.569 1.00 82.36  ? 4225 ASP A CG    1 
ATOM   21300 O  OD1   . ASP A 1 4225 ? 170.240 185.049 109.992 1.00 83.38  ? 4225 ASP A OD1   1 
ATOM   21301 O  OD2   . ASP A 1 4225 ? 169.026 183.220 110.030 1.00 75.34  ? 4225 ASP A OD2   1 
ATOM   21302 N  N     . THR A 1 4226 ? 166.808 187.245 107.073 1.00 72.07  ? 4226 THR A N     1 
ATOM   21303 C  CA    . THR A 1 4226 ? 165.945 187.655 105.969 1.00 72.87  ? 4226 THR A CA    1 
ATOM   21304 C  C     . THR A 1 4226 ? 166.420 188.961 105.339 1.00 83.21  ? 4226 THR A C     1 
ATOM   21305 O  O     . THR A 1 4226 ? 166.505 189.073 104.111 1.00 91.75  ? 4226 THR A O     1 
ATOM   21306 C  CB    . THR A 1 4226 ? 164.503 187.789 106.457 1.00 71.73  ? 4226 THR A CB    1 
ATOM   21307 O  OG1   . THR A 1 4226 ? 163.999 186.496 106.813 1.00 67.83  ? 4226 THR A OG1   1 
ATOM   21308 C  CG2   . THR A 1 4226 ? 163.629 188.386 105.371 1.00 73.61  ? 4226 THR A CG2   1 
ATOM   21309 N  N     . ALA A 1 4227 ? 166.739 189.961 106.165 1.00 80.90  ? 4227 ALA A N     1 
ATOM   21310 C  CA    . ALA A 1 4227 ? 167.083 191.278 105.640 1.00 82.23  ? 4227 ALA A CA    1 
ATOM   21311 C  C     . ALA A 1 4227 ? 168.429 191.258 104.928 1.00 90.87  ? 4227 ALA A C     1 
ATOM   21312 O  O     . ALA A 1 4227 ? 168.571 191.818 103.834 1.00 95.07  ? 4227 ALA A O     1 
ATOM   21313 C  CB    . ALA A 1 4227 ? 167.087 192.306 106.770 1.00 80.09  ? 4227 ALA A CB    1 
ATOM   21314 N  N     . LYS A 1 4228 ? 169.428 190.615 105.534 1.00 91.67  ? 4228 LYS A N     1 
ATOM   21315 C  CA    . LYS A 1 4228 ? 170.774 190.516 104.966 1.00 97.39  ? 4228 LYS A CA    1 
ATOM   21316 C  C     . LYS A 1 4228 ? 171.372 191.895 104.694 1.00 98.56  ? 4228 LYS A C     1 
ATOM   21317 O  O     . LYS A 1 4228 ? 172.038 192.115 103.680 1.00 98.49  ? 4228 LYS A O     1 
ATOM   21318 C  CB    . LYS A 1 4228 ? 170.778 189.661 103.695 1.00 95.36  ? 4228 LYS A CB    1 
ATOM   21319 C  CG    . LYS A 1 4228 ? 170.832 188.163 103.951 1.00 92.56  ? 4228 LYS A CG    1 
ATOM   21320 C  CD    . LYS A 1 4228 ? 171.721 187.833 105.140 1.00 95.08  ? 4228 LYS A CD    1 
ATOM   21321 C  CE    . LYS A 1 4228 ? 171.945 186.337 105.265 1.00 93.87  ? 4228 LYS A CE    1 
ATOM   21322 N  NZ    . LYS A 1 4228 ? 170.665 185.581 105.205 1.00 90.45  ? 4228 LYS A NZ    1 
ATOM   21323 N  N     . GLY A 1 4229 ? 171.133 192.834 105.608 1.00 93.91  ? 4229 GLY A N     1 
ATOM   21324 C  CA    . GLY A 1 4229 ? 171.709 194.158 105.528 1.00 95.78  ? 4229 GLY A CA    1 
ATOM   21325 C  C     . GLY A 1 4229 ? 170.819 195.218 104.912 1.00 97.45  ? 4229 GLY A C     1 
ATOM   21326 O  O     . GLY A 1 4229 ? 171.181 196.401 104.954 1.00 97.38  ? 4229 GLY A O     1 
ATOM   21327 N  N     . ARG A 1 4230 ? 169.680 194.839 104.340 1.00 99.22  ? 4230 ARG A N     1 
ATOM   21328 C  CA    . ARG A 1 4230 ? 168.787 195.823 103.743 1.00 100.16 ? 4230 ARG A CA    1 
ATOM   21329 C  C     . ARG A 1 4230 ? 168.185 196.724 104.814 1.00 100.68 ? 4230 ARG A C     1 
ATOM   21330 O  O     . ARG A 1 4230 ? 167.855 196.275 105.915 1.00 99.14  ? 4230 ARG A O     1 
ATOM   21331 C  CB    . ARG A 1 4230 ? 167.676 195.131 102.955 1.00 99.46  ? 4230 ARG A CB    1 
ATOM   21332 C  CG    . ARG A 1 4230 ? 168.153 194.422 101.701 1.00 96.72  ? 4230 ARG A CG    1 
ATOM   21333 C  CD    . ARG A 1 4230 ? 166.979 193.939 100.868 1.00 98.33  ? 4230 ARG A CD    1 
ATOM   21334 N  NE    . ARG A 1 4230 ? 166.185 192.936 101.566 1.00 100.29 ? 4230 ARG A NE    1 
ATOM   21335 C  CZ    . ARG A 1 4230 ? 166.426 191.633 101.528 1.00 104.86 ? 4230 ARG A CZ    1 
ATOM   21336 N  NH1   . ARG A 1 4230 ? 167.435 191.137 100.832 1.00 104.90 ? 4230 ARG A NH1   1 
ATOM   21337 N  NH2   . ARG A 1 4230 ? 165.634 190.807 102.206 1.00 102.93 ? 4230 ARG A NH2   1 
ATOM   21338 N  N     . GLN A 1 4231 ? 168.049 198.010 104.484 1.00 103.97 ? 4231 GLN A N     1 
ATOM   21339 C  CA    . GLN A 1 4231 ? 167.494 198.964 105.438 1.00 103.46 ? 4231 GLN A CA    1 
ATOM   21340 C  C     . GLN A 1 4231 ? 165.995 198.767 105.627 1.00 100.45 ? 4231 GLN A C     1 
ATOM   21341 O  O     . GLN A 1 4231 ? 165.474 199.009 106.721 1.00 98.51  ? 4231 GLN A O     1 
ATOM   21342 C  CB    . GLN A 1 4231 ? 167.792 200.394 104.983 1.00 103.34 ? 4231 GLN A CB    1 
ATOM   21343 C  CG    . GLN A 1 4231 ? 167.412 201.463 105.995 1.00 101.57 ? 4231 GLN A CG    1 
ATOM   21344 C  CD    . GLN A 1 4231 ? 168.425 201.590 107.117 1.00 108.00 ? 4231 GLN A CD    1 
ATOM   21345 O  OE1   . GLN A 1 4231 ? 169.484 200.963 107.087 1.00 111.41 ? 4231 GLN A OE1   1 
ATOM   21346 N  NE2   . GLN A 1 4231 ? 168.102 202.403 108.116 1.00 107.84 ? 4231 GLN A NE2   1 
ATOM   21347 N  N     . ASN A 1 4232 ? 165.288 198.343 104.584 1.00 98.34  ? 4232 ASN A N     1 
ATOM   21348 C  CA    . ASN A 1 4232 ? 163.859 198.076 104.661 1.00 96.16  ? 4232 ASN A CA    1 
ATOM   21349 C  C     . ASN A 1 4232 ? 163.540 196.785 103.926 1.00 96.08  ? 4232 ASN A C     1 
ATOM   21350 O  O     . ASN A 1 4232 ? 164.079 196.525 102.846 1.00 101.64 ? 4232 ASN A O     1 
ATOM   21351 C  CB    . ASN A 1 4232 ? 163.037 199.224 104.065 1.00 98.43  ? 4232 ASN A CB    1 
ATOM   21352 C  CG    . ASN A 1 4232 ? 163.203 200.518 104.830 1.00 104.62 ? 4232 ASN A CG    1 
ATOM   21353 O  OD1   . ASN A 1 4232 ? 163.738 201.497 104.310 1.00 110.63 ? 4232 ASN A OD1   1 
ATOM   21354 N  ND2   . ASN A 1 4232 ? 162.738 200.534 106.073 1.00 99.77  ? 4232 ASN A ND2   1 
ATOM   21355 N  N     . ILE A 1 4233 ? 162.662 195.978 104.516 1.00 90.32  ? 4233 ILE A N     1 
ATOM   21356 C  CA    . ILE A 1 4233 ? 162.168 194.763 103.884 1.00 88.09  ? 4233 ILE A CA    1 
ATOM   21357 C  C     . ILE A 1 4233 ? 160.648 194.799 103.902 1.00 83.49  ? 4233 ILE A C     1 
ATOM   21358 O  O     . ILE A 1 4233 ? 160.030 195.385 104.795 1.00 83.82  ? 4233 ILE A O     1 
ATOM   21359 C  CB    . ILE A 1 4233 ? 162.697 193.483 104.571 1.00 82.20  ? 4233 ILE A CB    1 
ATOM   21360 C  CG1   . ILE A 1 4233 ? 162.047 193.288 105.940 1.00 78.37  ? 4233 ILE A CG1   1 
ATOM   21361 C  CG2   . ILE A 1 4233 ? 164.208 193.529 104.705 1.00 89.85  ? 4233 ILE A CG2   1 
ATOM   21362 C  CD1   . ILE A 1 4233 ? 162.300 191.926 106.532 1.00 74.36  ? 4233 ILE A CD1   1 
ATOM   21363 N  N     . SER A 1 4234 ? 160.045 194.177 102.894 1.00 77.54  ? 4234 SER A N     1 
ATOM   21364 C  CA    . SER A 1 4234 ? 158.598 194.164 102.795 1.00 72.40  ? 4234 SER A CA    1 
ATOM   21365 C  C     . SER A 1 4234 ? 157.997 193.359 103.946 1.00 72.30  ? 4234 SER A C     1 
ATOM   21366 O  O     . SER A 1 4234 ? 158.617 192.416 104.443 1.00 76.18  ? 4234 SER A O     1 
ATOM   21367 C  CB    . SER A 1 4234 ? 158.161 193.570 101.459 1.00 80.73  ? 4234 SER A CB    1 
ATOM   21368 O  OG    . SER A 1 4234 ? 156.768 193.313 101.440 1.00 80.50  ? 4234 SER A OG    1 
ATOM   21369 N  N     . PRO A 1 4235 ? 156.796 193.725 104.400 1.00 71.79  ? 4235 PRO A N     1 
ATOM   21370 C  CA    . PRO A 1 4235 ? 156.141 192.924 105.446 1.00 69.81  ? 4235 PRO A CA    1 
ATOM   21371 C  C     . PRO A 1 4235 ? 155.899 191.486 105.030 1.00 71.41  ? 4235 PRO A C     1 
ATOM   21372 O  O     . PRO A 1 4235 ? 155.794 190.607 105.894 1.00 71.57  ? 4235 PRO A O     1 
ATOM   21373 C  CB    . PRO A 1 4235 ? 154.824 193.674 105.686 1.00 67.20  ? 4235 PRO A CB    1 
ATOM   21374 C  CG    . PRO A 1 4235 ? 155.103 195.070 105.256 1.00 67.56  ? 4235 PRO A CG    1 
ATOM   21375 C  CD    . PRO A 1 4235 ? 156.050 194.958 104.099 1.00 72.73  ? 4235 PRO A CD    1 
ATOM   21376 N  N     . ASP A 1 4236 ? 155.799 191.220 103.726 1.00 70.15  ? 4236 ASP A N     1 
ATOM   21377 C  CA    . ASP A 1 4236 ? 155.643 189.849 103.255 1.00 72.32  ? 4236 ASP A CA    1 
ATOM   21378 C  C     . ASP A 1 4236 ? 156.923 189.043 103.433 1.00 69.06  ? 4236 ASP A C     1 
ATOM   21379 O  O     . ASP A 1 4236 ? 156.862 187.828 103.650 1.00 69.05  ? 4236 ASP A O     1 
ATOM   21380 C  CB    . ASP A 1 4236 ? 155.220 189.846 101.787 1.00 79.04  ? 4236 ASP A CB    1 
ATOM   21381 C  CG    . ASP A 1 4236 ? 153.814 190.371 101.586 1.00 85.32  ? 4236 ASP A CG    1 
ATOM   21382 O  OD1   . ASP A 1 4236 ? 152.985 190.221 102.507 1.00 83.92  ? 4236 ASP A OD1   1 
ATOM   21383 O  OD2   . ASP A 1 4236 ? 153.539 190.936 100.507 1.00 88.73  ? 4236 ASP A OD2   1 
ATOM   21384 N  N     . LYS A 1 4237 ? 158.084 189.695 103.344 1.00 66.98  ? 4237 LYS A N     1 
ATOM   21385 C  CA    . LYS A 1 4237 ? 159.352 188.977 103.408 1.00 66.91  ? 4237 LYS A CA    1 
ATOM   21386 C  C     . LYS A 1 4237 ? 159.704 188.528 104.819 1.00 63.50  ? 4237 LYS A C     1 
ATOM   21387 O  O     . LYS A 1 4237 ? 160.552 187.643 104.976 1.00 68.11  ? 4237 LYS A O     1 
ATOM   21388 C  CB    . LYS A 1 4237 ? 160.482 189.846 102.852 1.00 69.22  ? 4237 LYS A CB    1 
ATOM   21389 C  CG    . LYS A 1 4237 ? 160.380 190.156 101.364 1.00 72.42  ? 4237 LYS A CG    1 
ATOM   21390 C  CD    . LYS A 1 4237 ? 159.672 189.054 100.594 1.00 72.23  ? 4237 LYS A CD    1 
ATOM   21391 C  CE    . LYS A 1 4237 ? 159.620 189.373 99.111  1.00 71.24  ? 4237 LYS A CE    1 
ATOM   21392 N  NZ    . LYS A 1 4237 ? 159.217 190.786 98.866  1.00 75.09  ? 4237 LYS A NZ    1 
ATOM   21393 N  N     . ILE A 1 4238 ? 159.086 189.112 105.841 1.00 59.10  ? 4238 ILE A N     1 
ATOM   21394 C  CA    . ILE A 1 4238 ? 159.427 188.740 107.219 1.00 56.98  ? 4238 ILE A CA    1 
ATOM   21395 C  C     . ILE A 1 4238 ? 159.051 187.282 107.454 1.00 56.02  ? 4238 ILE A C     1 
ATOM   21396 O  O     . ILE A 1 4238 ? 157.932 186.866 107.095 1.00 54.61  ? 4238 ILE A O     1 
ATOM   21397 C  CB    . ILE A 1 4238 ? 158.712 189.662 108.220 1.00 53.83  ? 4238 ILE A CB    1 
ATOM   21398 C  CG1   . ILE A 1 4238 ? 158.922 191.126 107.837 1.00 58.53  ? 4238 ILE A CG1   1 
ATOM   21399 C  CG2   . ILE A 1 4238 ? 159.211 189.410 109.633 1.00 52.54  ? 4238 ILE A CG2   1 
ATOM   21400 C  CD1   . ILE A 1 4238 ? 158.365 192.103 108.841 1.00 57.87  ? 4238 ILE A CD1   1 
ATOM   21401 N  N     . PRO A 1 4239 ? 159.929 186.464 108.037 1.00 52.92  ? 4239 PRO A N     1 
ATOM   21402 C  CA    . PRO A 1 4239 ? 159.587 185.053 108.258 1.00 46.96  ? 4239 PRO A CA    1 
ATOM   21403 C  C     . PRO A 1 4239 ? 158.539 184.882 109.343 1.00 41.34  ? 4239 PRO A C     1 
ATOM   21404 O  O     . PRO A 1 4239 ? 158.857 184.495 110.470 1.00 41.59  ? 4239 PRO A O     1 
ATOM   21405 C  CB    . PRO A 1 4239 ? 160.926 184.428 108.664 1.00 50.40  ? 4239 PRO A CB    1 
ATOM   21406 C  CG    . PRO A 1 4239 ? 161.700 185.554 109.247 1.00 53.44  ? 4239 PRO A CG    1 
ATOM   21407 C  CD    . PRO A 1 4239 ? 161.301 186.776 108.474 1.00 50.80  ? 4239 PRO A CD    1 
ATOM   21408 N  N     . TRP A 1 4240 ? 157.283 185.178 109.006 1.00 40.74  ? 4240 TRP A N     1 
ATOM   21409 C  CA    . TRP A 1 4240 ? 156.204 185.068 109.981 1.00 35.07  ? 4240 TRP A CA    1 
ATOM   21410 C  C     . TRP A 1 4240 ? 156.009 183.629 110.434 1.00 33.42  ? 4240 TRP A C     1 
ATOM   21411 O  O     . TRP A 1 4240 ? 155.778 183.370 111.621 1.00 35.56  ? 4240 TRP A O     1 
ATOM   21412 C  CB    . TRP A 1 4240 ? 154.915 185.625 109.388 1.00 37.46  ? 4240 TRP A CB    1 
ATOM   21413 C  CG    . TRP A 1 4240 ? 154.979 187.088 109.134 1.00 45.74  ? 4240 TRP A CG    1 
ATOM   21414 C  CD1   . TRP A 1 4240 ? 154.987 187.710 107.923 1.00 50.82  ? 4240 TRP A CD1   1 
ATOM   21415 C  CD2   . TRP A 1 4240 ? 155.037 188.122 110.119 1.00 45.59  ? 4240 TRP A CD2   1 
ATOM   21416 N  NE1   . TRP A 1 4240 ? 155.051 189.071 108.092 1.00 53.70  ? 4240 TRP A NE1   1 
ATOM   21417 C  CE2   . TRP A 1 4240 ? 155.082 189.349 109.433 1.00 50.19  ? 4240 TRP A CE2   1 
ATOM   21418 C  CE3   . TRP A 1 4240 ? 155.056 188.130 111.516 1.00 41.50  ? 4240 TRP A CE3   1 
ATOM   21419 C  CZ2   . TRP A 1 4240 ? 155.143 190.569 110.093 1.00 51.41  ? 4240 TRP A CZ2   1 
ATOM   21420 C  CZ3   . TRP A 1 4240 ? 155.118 189.341 112.169 1.00 46.06  ? 4240 TRP A CZ3   1 
ATOM   21421 C  CH2   . TRP A 1 4240 ? 155.159 190.544 111.459 1.00 49.60  ? 4240 TRP A CH2   1 
ATOM   21422 N  N     . SER A 1 4241 ? 156.090 182.679 109.501 1.00 34.36  ? 4241 SER A N     1 
ATOM   21423 C  CA    . SER A 1 4241 ? 155.939 181.274 109.859 1.00 31.96  ? 4241 SER A CA    1 
ATOM   21424 C  C     . SER A 1 4241 ? 157.027 180.834 110.827 1.00 29.58  ? 4241 SER A C     1 
ATOM   21425 O  O     . SER A 1 4241 ? 156.752 180.119 111.797 1.00 27.55  ? 4241 SER A O     1 
ATOM   21426 C  CB    . SER A 1 4241 ? 155.956 180.410 108.600 1.00 35.92  ? 4241 SER A CB    1 
ATOM   21427 O  OG    . SER A 1 4241 ? 157.031 180.772 107.752 1.00 34.78  ? 4241 SER A OG    1 
ATOM   21428 N  N     . ALA A 1 4242 ? 158.268 181.261 110.586 1.00 30.72  ? 4242 ALA A N     1 
ATOM   21429 C  CA    . ALA A 1 4242 ? 159.370 180.895 111.469 1.00 28.38  ? 4242 ALA A CA    1 
ATOM   21430 C  C     . ALA A 1 4242 ? 159.143 181.421 112.879 1.00 27.48  ? 4242 ALA A C     1 
ATOM   21431 O  O     . ALA A 1 4242 ? 159.275 180.680 113.860 1.00 31.98  ? 4242 ALA A O     1 
ATOM   21432 C  CB    . ALA A 1 4242 ? 160.687 181.426 110.906 1.00 32.23  ? 4242 ALA A CB    1 
ATOM   21433 N  N     . LEU A 1 4243 ? 158.789 182.702 112.997 1.00 29.25  ? 4243 LEU A N     1 
ATOM   21434 C  CA    . LEU A 1 4243 ? 158.564 183.297 114.310 1.00 28.97  ? 4243 LEU A CA    1 
ATOM   21435 C  C     . LEU A 1 4243 ? 157.405 182.619 115.028 1.00 27.89  ? 4243 LEU A C     1 
ATOM   21436 O  O     . LEU A 1 4243 ? 157.512 182.263 116.207 1.00 29.38  ? 4243 LEU A O     1 
ATOM   21437 C  CB    . LEU A 1 4243 ? 158.302 184.795 114.165 1.00 33.01  ? 4243 LEU A CB    1 
ATOM   21438 C  CG    . LEU A 1 4243 ? 159.382 185.626 113.471 1.00 37.50  ? 4243 LEU A CG    1 
ATOM   21439 C  CD1   . LEU A 1 4243 ? 159.025 187.100 113.503 1.00 37.62  ? 4243 LEU A CD1   1 
ATOM   21440 C  CD2   . LEU A 1 4243 ? 160.735 185.389 114.113 1.00 40.76  ? 4243 LEU A CD2   1 
ATOM   21441 N  N     . LYS A 1 4244 ? 156.287 182.420 114.323 1.00 26.53  ? 4244 LYS A N     1 
ATOM   21442 C  CA    . LYS A 1 4244 ? 155.117 181.811 114.946 1.00 23.65  ? 4244 LYS A CA    1 
ATOM   21443 C  C     . LYS A 1 4244 ? 155.418 180.396 115.415 1.00 30.72  ? 4244 LYS A C     1 
ATOM   21444 O  O     . LYS A 1 4244 ? 155.073 180.018 116.538 1.00 34.48  ? 4244 LYS A O     1 
ATOM   21445 C  CB    . LYS A 1 4244 ? 153.938 181.809 113.975 1.00 23.21  ? 4244 LYS A CB    1 
ATOM   21446 C  CG    . LYS A 1 4244 ? 153.312 183.165 113.752 1.00 30.25  ? 4244 LYS A CG    1 
ATOM   21447 C  CD    . LYS A 1 4244 ? 152.076 183.058 112.880 1.00 32.16  ? 4244 LYS A CD    1 
ATOM   21448 C  CE    . LYS A 1 4244 ? 152.421 182.587 111.483 1.00 36.98  ? 4244 LYS A CE    1 
ATOM   21449 N  NZ    . LYS A 1 4244 ? 151.226 182.580 110.598 1.00 47.19  ? 4244 LYS A NZ    1 
ATOM   21450 N  N     . THR A 1 4245 ? 156.072 179.597 114.568 1.00 29.03  ? 4245 THR A N     1 
ATOM   21451 C  CA    . THR A 1 4245 ? 156.367 178.219 114.937 1.00 23.42  ? 4245 THR A CA    1 
ATOM   21452 C  C     . THR A 1 4245 ? 157.347 178.151 116.099 1.00 24.73  ? 4245 THR A C     1 
ATOM   21453 O  O     . THR A 1 4245 ? 157.145 177.378 117.042 1.00 32.53  ? 4245 THR A O     1 
ATOM   21454 C  CB    . THR A 1 4245 ? 156.913 177.460 113.732 1.00 23.52  ? 4245 THR A CB    1 
ATOM   21455 O  OG1   . THR A 1 4245 ? 155.991 177.571 112.642 1.00 30.69  ? 4245 THR A OG1   1 
ATOM   21456 C  CG2   . THR A 1 4245 ? 157.108 175.996 114.072 1.00 27.71  ? 4245 THR A CG2   1 
ATOM   21457 N  N     . LEU A 1 4246 ? 158.410 178.957 116.062 1.00 23.37  ? 4246 LEU A N     1 
ATOM   21458 C  CA    . LEU A 1 4246 ? 159.399 178.895 117.130 1.00 23.30  ? 4246 LEU A CA    1 
ATOM   21459 C  C     . LEU A 1 4246 ? 158.821 179.384 118.451 1.00 27.34  ? 4246 LEU A C     1 
ATOM   21460 O  O     . LEU A 1 4246 ? 159.165 178.855 119.513 1.00 34.74  ? 4246 LEU A O     1 
ATOM   21461 C  CB    . LEU A 1 4246 ? 160.640 179.693 116.741 1.00 22.42  ? 4246 LEU A CB    1 
ATOM   21462 C  CG    . LEU A 1 4246 ? 161.494 179.026 115.662 1.00 20.03  ? 4246 LEU A CG    1 
ATOM   21463 C  CD1   . LEU A 1 4246 ? 162.835 179.698 115.564 1.00 23.54  ? 4246 LEU A CD1   1 
ATOM   21464 C  CD2   . LEU A 1 4246 ? 161.669 177.548 115.952 1.00 24.62  ? 4246 LEU A CD2   1 
ATOM   21465 N  N     . MET A 1 4247 ? 157.936 180.382 118.414 1.00 27.79  ? 4247 MET A N     1 
ATOM   21466 C  CA    . MET A 1 4247 ? 157.318 180.848 119.649 1.00 26.57  ? 4247 MET A CA    1 
ATOM   21467 C  C     . MET A 1 4247 ? 156.226 179.913 120.150 1.00 28.11  ? 4247 MET A C     1 
ATOM   21468 O  O     . MET A 1 4247 ? 155.997 179.849 121.361 1.00 34.90  ? 4247 MET A O     1 
ATOM   21469 C  CB    . MET A 1 4247 ? 156.759 182.255 119.455 1.00 24.75  ? 4247 MET A CB    1 
ATOM   21470 C  CG    . MET A 1 4247 ? 157.800 183.342 119.627 1.00 26.96  ? 4247 MET A CG    1 
ATOM   21471 S  SD    . MET A 1 4247 ? 157.104 184.999 119.624 1.00 48.87  ? 4247 MET A SD    1 
ATOM   21472 C  CE    . MET A 1 4247 ? 157.837 185.647 118.126 1.00 44.41  ? 4247 MET A CE    1 
ATOM   21473 N  N     . ALA A 1 4248 ? 155.550 179.189 119.258 1.00 28.30  ? 4248 ALA A N     1 
ATOM   21474 C  CA    . ALA A 1 4248 ? 154.469 178.305 119.668 1.00 29.09  ? 4248 ALA A CA    1 
ATOM   21475 C  C     . ALA A 1 4248 ? 154.953 176.939 120.123 1.00 34.47  ? 4248 ALA A C     1 
ATOM   21476 O  O     . ALA A 1 4248 ? 154.289 176.304 120.948 1.00 39.70  ? 4248 ALA A O     1 
ATOM   21477 C  CB    . ALA A 1 4248 ? 153.471 178.126 118.522 1.00 31.02  ? 4248 ALA A CB    1 
ATOM   21478 N  N     . GLN A 1 4249 ? 156.082 176.463 119.602 1.00 35.02  ? 4249 GLN A N     1 
ATOM   21479 C  CA    . GLN A 1 4249 ? 156.581 175.142 119.958 1.00 35.82  ? 4249 GLN A CA    1 
ATOM   21480 C  C     . GLN A 1 4249 ? 157.837 175.164 120.812 1.00 34.97  ? 4249 GLN A C     1 
ATOM   21481 O  O     . GLN A 1 4249 ? 158.063 174.218 121.568 1.00 35.55  ? 4249 GLN A O     1 
ATOM   21482 C  CB    . GLN A 1 4249 ? 156.858 174.316 118.695 1.00 31.48  ? 4249 GLN A CB    1 
ATOM   21483 C  CG    . GLN A 1 4249 ? 155.918 174.605 117.538 1.00 33.89  ? 4249 GLN A CG    1 
ATOM   21484 C  CD    . GLN A 1 4249 ? 154.598 173.873 117.651 1.00 43.54  ? 4249 GLN A CD    1 
ATOM   21485 O  OE1   . GLN A 1 4249 ? 154.494 172.859 118.337 1.00 46.30  ? 4249 GLN A OE1   1 
ATOM   21486 N  NE2   . GLN A 1 4249 ? 153.579 174.387 116.974 1.00 46.34  ? 4249 GLN A NE2   1 
ATOM   21487 N  N     . SER A 1 4250 ? 158.657 176.209 120.721 1.00 31.02  ? 4250 SER A N     1 
ATOM   21488 C  CA    . SER A 1 4250 ? 159.937 176.246 121.416 1.00 27.67  ? 4250 SER A CA    1 
ATOM   21489 C  C     . SER A 1 4250 ? 160.009 177.309 122.502 1.00 32.21  ? 4250 SER A C     1 
ATOM   21490 O  O     . SER A 1 4250 ? 160.302 176.988 123.657 1.00 38.88  ? 4250 SER A O     1 
ATOM   21491 C  CB    . SER A 1 4250 ? 161.071 176.466 120.407 1.00 31.21  ? 4250 SER A CB    1 
ATOM   21492 O  OG    . SER A 1 4250 ? 160.953 175.579 119.311 1.00 39.73  ? 4250 SER A OG    1 
ATOM   21493 N  N     . ILE A 1 4251 ? 159.751 178.573 122.165 1.00 32.70  ? 4251 ILE A N     1 
ATOM   21494 C  CA    . ILE A 1 4251 ? 159.980 179.655 123.120 1.00 30.83  ? 4251 ILE A CA    1 
ATOM   21495 C  C     . ILE A 1 4251 ? 158.935 179.623 124.229 1.00 34.67  ? 4251 ILE A C     1 
ATOM   21496 O  O     . ILE A 1 4251 ? 159.260 179.426 125.405 1.00 39.62  ? 4251 ILE A O     1 
ATOM   21497 C  CB    . ILE A 1 4251 ? 159.994 181.016 122.404 1.00 27.00  ? 4251 ILE A CB    1 
ATOM   21498 C  CG1   . ILE A 1 4251 ? 160.871 180.961 121.153 1.00 25.84  ? 4251 ILE A CG1   1 
ATOM   21499 C  CG2   . ILE A 1 4251 ? 160.473 182.097 123.342 1.00 30.61  ? 4251 ILE A CG2   1 
ATOM   21500 C  CD1   . ILE A 1 4251 ? 162.312 180.638 121.433 1.00 33.32  ? 4251 ILE A CD1   1 
ATOM   21501 N  N     . TYR A 1 4252 ? 157.666 179.809 123.873 1.00 31.44  ? 4252 TYR A N     1 
ATOM   21502 C  CA    . TYR A 1 4252 ? 156.597 179.835 124.863 1.00 30.53  ? 4252 TYR A CA    1 
ATOM   21503 C  C     . TYR A 1 4252 ? 155.867 178.510 125.000 1.00 36.02  ? 4252 TYR A C     1 
ATOM   21504 O  O     . TYR A 1 4252 ? 155.350 178.212 126.079 1.00 44.69  ? 4252 TYR A O     1 
ATOM   21505 C  CB    . TYR A 1 4252 ? 155.572 180.923 124.527 1.00 26.14  ? 4252 TYR A CB    1 
ATOM   21506 C  CG    . TYR A 1 4252 ? 156.100 182.334 124.616 1.00 30.48  ? 4252 TYR A CG    1 
ATOM   21507 C  CD1   . TYR A 1 4252 ? 156.800 182.903 123.564 1.00 33.58  ? 4252 TYR A CD1   1 
ATOM   21508 C  CD2   . TYR A 1 4252 ? 155.903 183.095 125.757 1.00 32.76  ? 4252 TYR A CD2   1 
ATOM   21509 C  CE1   . TYR A 1 4252 ? 157.280 184.193 123.644 1.00 34.37  ? 4252 TYR A CE1   1 
ATOM   21510 C  CE2   . TYR A 1 4252 ? 156.381 184.384 125.845 1.00 31.52  ? 4252 TYR A CE2   1 
ATOM   21511 C  CZ    . TYR A 1 4252 ? 157.067 184.928 124.787 1.00 33.78  ? 4252 TYR A CZ    1 
ATOM   21512 O  OH    . TYR A 1 4252 ? 157.544 186.212 124.874 1.00 43.94  ? 4252 TYR A OH    1 
ATOM   21513 N  N     . GLY A 1 4253 ? 155.808 177.712 123.937 1.00 33.55  ? 4253 GLY A N     1 
ATOM   21514 C  CA    . GLY A 1 4253 ? 155.074 176.465 123.982 1.00 30.11  ? 4253 GLY A CA    1 
ATOM   21515 C  C     . GLY A 1 4253 ? 155.770 175.327 124.687 1.00 39.01  ? 4253 GLY A C     1 
ATOM   21516 O  O     . GLY A 1 4253 ? 155.162 174.269 124.864 1.00 52.45  ? 4253 GLY A O     1 
ATOM   21517 N  N     . GLY A 1 4254 ? 157.030 175.509 125.082 1.00 34.88  ? 4254 GLY A N     1 
ATOM   21518 C  CA    . GLY A 1 4254 ? 157.720 174.456 125.808 1.00 29.32  ? 4254 GLY A CA    1 
ATOM   21519 C  C     . GLY A 1 4254 ? 157.081 174.159 127.150 1.00 30.97  ? 4254 GLY A C     1 
ATOM   21520 O  O     . GLY A 1 4254 ? 156.894 172.997 127.516 1.00 39.01  ? 4254 GLY A O     1 
ATOM   21521 N  N     . ARG A 1 4255 ? 156.733 175.205 127.899 1.00 30.25  ? 4255 ARG A N     1 
ATOM   21522 C  CA    . ARG A 1 4255 ? 156.091 175.010 129.193 1.00 34.61  ? 4255 ARG A CA    1 
ATOM   21523 C  C     . ARG A 1 4255 ? 154.676 174.469 129.048 1.00 36.38  ? 4255 ARG A C     1 
ATOM   21524 O  O     . ARG A 1 4255 ? 154.196 173.749 129.930 1.00 37.07  ? 4255 ARG A O     1 
ATOM   21525 C  CB    . ARG A 1 4255 ? 156.070 176.323 129.971 1.00 38.49  ? 4255 ARG A CB    1 
ATOM   21526 C  CG    . ARG A 1 4255 ? 157.326 177.153 129.815 1.00 44.08  ? 4255 ARG A CG    1 
ATOM   21527 C  CD    . ARG A 1 4255 ? 157.124 178.557 130.352 1.00 43.85  ? 4255 ARG A CD    1 
ATOM   21528 N  NE    . ARG A 1 4255 ? 158.350 179.343 130.306 1.00 51.81  ? 4255 ARG A NE    1 
ATOM   21529 C  CZ    . ARG A 1 4255 ? 159.396 179.152 131.099 1.00 55.65  ? 4255 ARG A CZ    1 
ATOM   21530 N  NH1   . ARG A 1 4255 ? 159.396 178.213 132.031 1.00 54.27  ? 4255 ARG A NH1   1 
ATOM   21531 N  NH2   . ARG A 1 4255 ? 160.468 179.925 130.956 1.00 54.65  ? 4255 ARG A NH2   1 
ATOM   21532 N  N     . VAL A 1 4256 ? 153.995 174.807 127.956 1.00 35.29  ? 4256 VAL A N     1 
ATOM   21533 C  CA    . VAL A 1 4256 ? 152.602 174.417 127.778 1.00 33.54  ? 4256 VAL A CA    1 
ATOM   21534 C  C     . VAL A 1 4256 ? 152.528 172.917 127.529 1.00 38.77  ? 4256 VAL A C     1 
ATOM   21535 O  O     . VAL A 1 4256 ? 153.099 172.403 126.560 1.00 41.03  ? 4256 VAL A O     1 
ATOM   21536 C  CB    . VAL A 1 4256 ? 151.958 175.201 126.629 1.00 30.69  ? 4256 VAL A CB    1 
ATOM   21537 C  CG1   . VAL A 1 4256 ? 150.578 174.662 126.337 1.00 35.14  ? 4256 VAL A CG1   1 
ATOM   21538 C  CG2   . VAL A 1 4256 ? 151.892 176.677 126.968 1.00 30.03  ? 4256 VAL A CG2   1 
ATOM   21539 N  N     . ASP A 1 4257 ? 151.814 172.206 128.404 1.00 41.37  ? 4257 ASP A N     1 
ATOM   21540 C  CA    . ASP A 1 4257 ? 151.588 170.778 128.242 1.00 45.70  ? 4257 ASP A CA    1 
ATOM   21541 C  C     . ASP A 1 4257 ? 150.154 170.427 127.874 1.00 48.54  ? 4257 ASP A C     1 
ATOM   21542 O  O     . ASP A 1 4257 ? 149.930 169.369 127.279 1.00 50.93  ? 4257 ASP A O     1 
ATOM   21543 C  CB    . ASP A 1 4257 ? 151.972 170.027 129.525 1.00 44.48  ? 4257 ASP A CB    1 
ATOM   21544 C  CG    . ASP A 1 4257 ? 151.447 170.700 130.773 1.00 53.88  ? 4257 ASP A CG    1 
ATOM   21545 O  OD1   . ASP A 1 4257 ? 150.732 171.715 130.646 1.00 54.59  ? 4257 ASP A OD1   1 
ATOM   21546 O  OD2   . ASP A 1 4257 ? 151.755 170.218 131.883 1.00 61.35  ? 4257 ASP A OD2   1 
ATOM   21547 N  N     . ASN A 1 4258 ? 149.188 171.279 128.208 1.00 44.49  ? 4258 ASN A N     1 
ATOM   21548 C  CA    . ASN A 1 4258 ? 147.810 171.075 127.786 1.00 39.60  ? 4258 ASN A CA    1 
ATOM   21549 C  C     . ASN A 1 4258 ? 147.690 171.350 126.294 1.00 36.21  ? 4258 ASN A C     1 
ATOM   21550 O  O     . ASN A 1 4258 ? 148.334 172.264 125.771 1.00 39.67  ? 4258 ASN A O     1 
ATOM   21551 C  CB    . ASN A 1 4258 ? 146.873 171.990 128.573 1.00 38.20  ? 4258 ASN A CB    1 
ATOM   21552 C  CG    . ASN A 1 4258 ? 145.484 171.412 128.724 1.00 46.15  ? 4258 ASN A CG    1 
ATOM   21553 O  OD1   . ASN A 1 4258 ? 145.315 170.203 128.879 1.00 55.16  ? 4258 ASN A OD1   1 
ATOM   21554 N  ND2   . ASN A 1 4258 ? 144.477 172.274 128.683 1.00 43.02  ? 4258 ASN A ND2   1 
ATOM   21555 N  N     . GLU A 1 4259 ? 146.872 170.553 125.604 1.00 38.23  ? 4259 GLU A N     1 
ATOM   21556 C  CA    . GLU A 1 4259 ? 146.682 170.778 124.175 1.00 41.44  ? 4259 GLU A CA    1 
ATOM   21557 C  C     . GLU A 1 4259 ? 145.780 171.974 123.909 1.00 36.45  ? 4259 GLU A C     1 
ATOM   21558 O  O     . GLU A 1 4259 ? 145.911 172.627 122.869 1.00 37.71  ? 4259 GLU A O     1 
ATOM   21559 C  CB    . GLU A 1 4259 ? 146.119 169.524 123.506 1.00 46.83  ? 4259 GLU A CB    1 
ATOM   21560 C  CG    . GLU A 1 4259 ? 144.722 169.136 123.950 1.00 51.86  ? 4259 GLU A CG    1 
ATOM   21561 C  CD    . GLU A 1 4259 ? 144.244 167.853 123.298 1.00 67.03  ? 4259 GLU A CD    1 
ATOM   21562 O  OE1   . GLU A 1 4259 ? 145.017 167.260 122.517 1.00 78.27  ? 4259 GLU A OE1   1 
ATOM   21563 O  OE2   . GLU A 1 4259 ? 143.097 167.438 123.563 1.00 70.20  ? 4259 GLU A OE2   1 
ATOM   21564 N  N     . PHE A 1 4260 ? 144.868 172.285 124.832 1.00 35.91  ? 4260 PHE A N     1 
ATOM   21565 C  CA    . PHE A 1 4260 ? 143.990 173.434 124.640 1.00 34.57  ? 4260 PHE A CA    1 
ATOM   21566 C  C     . PHE A 1 4260 ? 144.720 174.741 124.921 1.00 35.61  ? 4260 PHE A C     1 
ATOM   21567 O  O     . PHE A 1 4260 ? 144.477 175.751 124.251 1.00 39.55  ? 4260 PHE A O     1 
ATOM   21568 C  CB    . PHE A 1 4260 ? 142.750 173.293 125.519 1.00 38.08  ? 4260 PHE A CB    1 
ATOM   21569 C  CG    . PHE A 1 4260 ? 141.996 172.017 125.287 1.00 39.51  ? 4260 PHE A CG    1 
ATOM   21570 C  CD1   . PHE A 1 4260 ? 142.281 170.884 126.025 1.00 37.51  ? 4260 PHE A CD1   1 
ATOM   21571 C  CD2   . PHE A 1 4260 ? 141.024 171.943 124.308 1.00 36.79  ? 4260 PHE A CD2   1 
ATOM   21572 C  CE1   . PHE A 1 4260 ? 141.598 169.710 125.803 1.00 38.22  ? 4260 PHE A CE1   1 
ATOM   21573 C  CE2   . PHE A 1 4260 ? 140.339 170.772 124.082 1.00 34.61  ? 4260 PHE A CE2   1 
ATOM   21574 C  CZ    . PHE A 1 4260 ? 140.626 169.654 124.830 1.00 37.18  ? 4260 PHE A CZ    1 
ATOM   21575 N  N     . ASP A 1 4261 ? 145.631 174.740 125.896 1.00 36.41  ? 4261 ASP A N     1 
ATOM   21576 C  CA    . ASP A 1 4261 ? 146.490 175.901 126.098 1.00 30.82  ? 4261 ASP A CA    1 
ATOM   21577 C  C     . ASP A 1 4261 ? 147.401 176.120 124.898 1.00 29.44  ? 4261 ASP A C     1 
ATOM   21578 O  O     . ASP A 1 4261 ? 147.645 177.262 124.491 1.00 33.98  ? 4261 ASP A O     1 
ATOM   21579 C  CB    . ASP A 1 4261 ? 147.310 175.730 127.372 1.00 31.19  ? 4261 ASP A CB    1 
ATOM   21580 C  CG    . ASP A 1 4261 ? 146.476 175.871 128.622 1.00 38.95  ? 4261 ASP A CG    1 
ATOM   21581 O  OD1   . ASP A 1 4261 ? 145.287 176.234 128.507 1.00 44.94  ? 4261 ASP A OD1   1 
ATOM   21582 O  OD2   . ASP A 1 4261 ? 147.005 175.610 129.719 1.00 43.11  ? 4261 ASP A OD2   1 
ATOM   21583 N  N     . GLN A 1 4262 ? 147.917 175.035 124.318 1.00 27.16  ? 4262 GLN A N     1 
ATOM   21584 C  CA    . GLN A 1 4262 ? 148.713 175.155 123.103 1.00 27.01  ? 4262 GLN A CA    1 
ATOM   21585 C  C     . GLN A 1 4262 ? 147.874 175.692 121.951 1.00 31.07  ? 4262 GLN A C     1 
ATOM   21586 O  O     . GLN A 1 4262 ? 148.352 176.502 121.150 1.00 34.90  ? 4262 GLN A O     1 
ATOM   21587 C  CB    . GLN A 1 4262 ? 149.322 173.803 122.740 1.00 30.21  ? 4262 GLN A CB    1 
ATOM   21588 C  CG    . GLN A 1 4262 ? 150.239 173.839 121.534 1.00 39.25  ? 4262 GLN A CG    1 
ATOM   21589 C  CD    . GLN A 1 4262 ? 151.506 174.622 121.791 1.00 39.08  ? 4262 GLN A CD    1 
ATOM   21590 O  OE1   . GLN A 1 4262 ? 152.301 174.267 122.659 1.00 38.45  ? 4262 GLN A OE1   1 
ATOM   21591 N  NE2   . GLN A 1 4262 ? 151.704 175.693 121.036 1.00 35.55  ? 4262 GLN A NE2   1 
ATOM   21592 N  N     . ARG A 1 4263 ? 146.620 175.249 121.852 1.00 33.90  ? 4263 ARG A N     1 
ATOM   21593 C  CA    . ARG A 1 4263 ? 145.716 175.774 120.834 1.00 30.83  ? 4263 ARG A CA    1 
ATOM   21594 C  C     . ARG A 1 4263 ? 145.486 177.268 121.020 1.00 33.31  ? 4263 ARG A C     1 
ATOM   21595 O  O     . ARG A 1 4263 ? 145.482 178.031 120.047 1.00 37.22  ? 4263 ARG A O     1 
ATOM   21596 C  CB    . ARG A 1 4263 ? 144.393 175.014 120.889 1.00 34.05  ? 4263 ARG A CB    1 
ATOM   21597 C  CG    . ARG A 1 4263 ? 143.403 175.371 119.805 1.00 46.67  ? 4263 ARG A CG    1 
ATOM   21598 C  CD    . ARG A 1 4263 ? 142.148 174.530 119.944 1.00 54.39  ? 4263 ARG A CD    1 
ATOM   21599 N  NE    . ARG A 1 4263 ? 141.464 174.785 121.206 1.00 52.16  ? 4263 ARG A NE    1 
ATOM   21600 C  CZ    . ARG A 1 4263 ? 140.353 174.174 121.593 1.00 48.07  ? 4263 ARG A CZ    1 
ATOM   21601 N  NH1   . ARG A 1 4263 ? 139.774 173.253 120.842 1.00 46.66  ? 4263 ARG A NH1   1 
ATOM   21602 N  NH2   . ARG A 1 4263 ? 139.808 174.498 122.761 1.00 46.78  ? 4263 ARG A NH2   1 
ATOM   21603 N  N     . LEU A 1 4264 ? 145.291 177.701 122.266 1.00 35.54  ? 4264 LEU A N     1 
ATOM   21604 C  CA    . LEU A 1 4264 ? 145.110 179.122 122.551 1.00 33.43  ? 4264 LEU A CA    1 
ATOM   21605 C  C     . LEU A 1 4264 ? 146.353 179.927 122.188 1.00 34.08  ? 4264 LEU A C     1 
ATOM   21606 O  O     . LEU A 1 4264 ? 146.254 181.015 121.603 1.00 36.16  ? 4264 LEU A O     1 
ATOM   21607 C  CB    . LEU A 1 4264 ? 144.759 179.302 124.026 1.00 29.95  ? 4264 LEU A CB    1 
ATOM   21608 C  CG    . LEU A 1 4264 ? 144.730 180.725 124.567 1.00 32.52  ? 4264 LEU A CG    1 
ATOM   21609 C  CD1   . LEU A 1 4264 ? 143.572 181.473 123.959 1.00 37.08  ? 4264 LEU A CD1   1 
ATOM   21610 C  CD2   . LEU A 1 4264 ? 144.617 180.697 126.078 1.00 29.60  ? 4264 LEU A CD2   1 
ATOM   21611 N  N     . LEU A 1 4265 ? 147.533 179.410 122.533 1.00 32.50  ? 4265 LEU A N     1 
ATOM   21612 C  CA    . LEU A 1 4265 ? 148.776 180.089 122.186 1.00 29.77  ? 4265 LEU A CA    1 
ATOM   21613 C  C     . LEU A 1 4265 ? 148.943 180.190 120.675 1.00 30.80  ? 4265 LEU A C     1 
ATOM   21614 O  O     . LEU A 1 4265 ? 149.365 181.231 120.154 1.00 36.23  ? 4265 LEU A O     1 
ATOM   21615 C  CB    . LEU A 1 4265 ? 149.956 179.351 122.815 1.00 26.46  ? 4265 LEU A CB    1 
ATOM   21616 C  CG    . LEU A 1 4265 ? 151.323 180.029 122.806 1.00 31.56  ? 4265 LEU A CG    1 
ATOM   21617 C  CD1   . LEU A 1 4265 ? 151.402 181.077 123.896 1.00 39.42  ? 4265 LEU A CD1   1 
ATOM   21618 C  CD2   . LEU A 1 4265 ? 152.410 178.993 122.987 1.00 34.90  ? 4265 LEU A CD2   1 
ATOM   21619 N  N     . ASN A 1 4266 ? 148.611 179.117 119.954 1.00 30.86  ? 4266 ASN A N     1 
ATOM   21620 C  CA    . ASN A 1 4266 ? 148.686 179.145 118.499 1.00 31.25  ? 4266 ASN A CA    1 
ATOM   21621 C  C     . ASN A 1 4266 ? 147.720 180.167 117.916 1.00 37.25  ? 4266 ASN A C     1 
ATOM   21622 O  O     . ASN A 1 4266 ? 148.059 180.869 116.959 1.00 40.24  ? 4266 ASN A O     1 
ATOM   21623 C  CB    . ASN A 1 4266 ? 148.402 177.757 117.928 1.00 35.96  ? 4266 ASN A CB    1 
ATOM   21624 C  CG    . ASN A 1 4266 ? 149.429 176.732 118.353 1.00 40.94  ? 4266 ASN A CG    1 
ATOM   21625 O  OD1   . ASN A 1 4266 ? 150.368 177.045 119.081 1.00 40.65  ? 4266 ASN A OD1   1 
ATOM   21626 N  ND2   . ASN A 1 4266 ? 149.255 175.497 117.902 1.00 41.29  ? 4266 ASN A ND2   1 
ATOM   21627 N  N     . THR A 1 4267 ? 146.507 180.255 118.467 1.00 35.85  ? 4267 THR A N     1 
ATOM   21628 C  CA    . THR A 1 4267 ? 145.553 181.245 117.971 1.00 36.13  ? 4267 THR A CA    1 
ATOM   21629 C  C     . THR A 1 4267 ? 146.059 182.662 118.200 1.00 38.70  ? 4267 THR A C     1 
ATOM   21630 O  O     . THR A 1 4267 ? 145.962 183.513 117.308 1.00 45.11  ? 4267 THR A O     1 
ATOM   21631 C  CB    . THR A 1 4267 ? 144.188 181.057 118.631 1.00 38.20  ? 4267 THR A CB    1 
ATOM   21632 O  OG1   . THR A 1 4267 ? 144.333 181.081 120.055 1.00 41.41  ? 4267 THR A OG1   1 
ATOM   21633 C  CG2   . THR A 1 4267 ? 143.567 179.740 118.203 1.00 46.83  ? 4267 THR A CG2   1 
ATOM   21634 N  N     . PHE A 1 4268 ? 146.615 182.932 119.384 1.00 37.58  ? 4268 PHE A N     1 
ATOM   21635 C  CA    . PHE A 1 4268 ? 147.166 184.259 119.646 1.00 36.43  ? 4268 PHE A CA    1 
ATOM   21636 C  C     . PHE A 1 4268 ? 148.296 184.590 118.680 1.00 37.23  ? 4268 PHE A C     1 
ATOM   21637 O  O     . PHE A 1 4268 ? 148.350 185.696 118.127 1.00 40.82  ? 4268 PHE A O     1 
ATOM   21638 C  CB    . PHE A 1 4268 ? 147.660 184.353 121.089 1.00 34.92  ? 4268 PHE A CB    1 
ATOM   21639 C  CG    . PHE A 1 4268 ? 146.600 184.757 122.067 1.00 43.45  ? 4268 PHE A CG    1 
ATOM   21640 C  CD1   . PHE A 1 4268 ? 145.798 185.857 121.822 1.00 51.06  ? 4268 PHE A CD1   1 
ATOM   21641 C  CD2   . PHE A 1 4268 ? 146.410 184.044 123.236 1.00 40.22  ? 4268 PHE A CD2   1 
ATOM   21642 C  CE1   . PHE A 1 4268 ? 144.823 186.234 122.721 1.00 44.22  ? 4268 PHE A CE1   1 
ATOM   21643 C  CE2   . PHE A 1 4268 ? 145.438 184.418 124.137 1.00 44.16  ? 4268 PHE A CE2   1 
ATOM   21644 C  CZ    . PHE A 1 4268 ? 144.642 185.513 123.878 1.00 44.69  ? 4268 PHE A CZ    1 
ATOM   21645 N  N     . LEU A 1 4269 ? 149.205 183.639 118.458 1.00 38.36  ? 4269 LEU A N     1 
ATOM   21646 C  CA    . LEU A 1 4269 ? 150.341 183.893 117.578 1.00 32.67  ? 4269 LEU A CA    1 
ATOM   21647 C  C     . LEU A 1 4269 ? 149.900 184.081 116.131 1.00 36.87  ? 4269 LEU A C     1 
ATOM   21648 O  O     . LEU A 1 4269 ? 150.431 184.945 115.425 1.00 42.38  ? 4269 LEU A O     1 
ATOM   21649 C  CB    . LEU A 1 4269 ? 151.352 182.757 117.696 1.00 28.32  ? 4269 LEU A CB    1 
ATOM   21650 C  CG    . LEU A 1 4269 ? 152.253 182.871 118.922 1.00 29.97  ? 4269 LEU A CG    1 
ATOM   21651 C  CD1   . LEU A 1 4269 ? 153.137 181.661 119.041 1.00 28.00  ? 4269 LEU A CD1   1 
ATOM   21652 C  CD2   . LEU A 1 4269 ? 153.091 184.127 118.830 1.00 35.10  ? 4269 LEU A CD2   1 
ATOM   21653 N  N     . GLU A 1 4270 ? 148.938 183.282 115.666 1.00 36.56  ? 4270 GLU A N     1 
ATOM   21654 C  CA    . GLU A 1 4270 ? 148.441 183.442 114.304 1.00 39.89  ? 4270 GLU A CA    1 
ATOM   21655 C  C     . GLU A 1 4270 ? 147.667 184.740 114.139 1.00 40.47  ? 4270 GLU A C     1 
ATOM   21656 O  O     . GLU A 1 4270 ? 147.626 185.297 113.038 1.00 46.46  ? 4270 GLU A O     1 
ATOM   21657 C  CB    . GLU A 1 4270 ? 147.562 182.255 113.915 1.00 49.46  ? 4270 GLU A CB    1 
ATOM   21658 C  CG    . GLU A 1 4270 ? 148.307 180.938 113.793 1.00 62.24  ? 4270 GLU A CG    1 
ATOM   21659 C  CD    . GLU A 1 4270 ? 147.396 179.785 113.426 1.00 79.52  ? 4270 GLU A CD    1 
ATOM   21660 O  OE1   . GLU A 1 4270 ? 146.163 179.987 113.389 1.00 76.45  ? 4270 GLU A OE1   1 
ATOM   21661 O  OE2   . GLU A 1 4270 ? 147.911 178.674 113.179 1.00 77.16  ? 4270 GLU A OE2   1 
ATOM   21662 N  N     . ARG A 1 4271 ? 147.035 185.229 115.206 1.00 41.44  ? 4271 ARG A N     1 
ATOM   21663 C  CA    . ARG A 1 4271 ? 146.326 186.498 115.113 1.00 42.72  ? 4271 ARG A CA    1 
ATOM   21664 C  C     . ARG A 1 4271 ? 147.295 187.673 115.084 1.00 44.05  ? 4271 ARG A C     1 
ATOM   21665 O  O     . ARG A 1 4271 ? 147.100 188.625 114.319 1.00 48.26  ? 4271 ARG A O     1 
ATOM   21666 C  CB    . ARG A 1 4271 ? 145.349 186.635 116.278 1.00 47.49  ? 4271 ARG A CB    1 
ATOM   21667 C  CG    . ARG A 1 4271 ? 144.514 187.897 116.240 1.00 52.98  ? 4271 ARG A CG    1 
ATOM   21668 C  CD    . ARG A 1 4271 ? 143.568 187.954 117.422 1.00 62.62  ? 4271 ARG A CD    1 
ATOM   21669 N  NE    . ARG A 1 4271 ? 144.292 188.008 118.685 1.00 59.25  ? 4271 ARG A NE    1 
ATOM   21670 C  CZ    . ARG A 1 4271 ? 144.786 189.118 119.214 1.00 67.91  ? 4271 ARG A CZ    1 
ATOM   21671 N  NH1   . ARG A 1 4271 ? 144.664 190.287 118.607 1.00 66.79  ? 4271 ARG A NH1   1 
ATOM   21672 N  NH2   . ARG A 1 4271 ? 145.423 189.053 120.380 1.00 67.27  ? 4271 ARG A NH2   1 
ATOM   21673 N  N     . LEU A 1 4272 ? 148.349 187.625 115.900 1.00 41.64  ? 4272 LEU A N     1 
ATOM   21674 C  CA    . LEU A 1 4272 ? 149.237 188.777 116.026 1.00 36.03  ? 4272 LEU A CA    1 
ATOM   21675 C  C     . LEU A 1 4272 ? 150.287 188.814 114.919 1.00 40.02  ? 4272 LEU A C     1 
ATOM   21676 O  O     . LEU A 1 4272 ? 150.438 189.826 114.227 1.00 41.05  ? 4272 LEU A O     1 
ATOM   21677 C  CB    . LEU A 1 4272 ? 149.909 188.771 117.401 1.00 35.40  ? 4272 LEU A CB    1 
ATOM   21678 C  CG    . LEU A 1 4272 ? 148.992 189.099 118.578 1.00 43.85  ? 4272 LEU A CG    1 
ATOM   21679 C  CD1   . LEU A 1 4272 ? 149.753 189.030 119.886 1.00 44.22  ? 4272 LEU A CD1   1 
ATOM   21680 C  CD2   . LEU A 1 4272 ? 148.370 190.470 118.391 1.00 46.60  ? 4272 LEU A CD2   1 
ATOM   21681 N  N     . PHE A 1 4273 ? 151.028 187.723 114.741 1.00 41.24  ? 4273 PHE A N     1 
ATOM   21682 C  CA    . PHE A 1 4273 ? 152.189 187.714 113.852 1.00 36.11  ? 4273 PHE A CA    1 
ATOM   21683 C  C     . PHE A 1 4273 ? 151.755 187.351 112.437 1.00 43.06  ? 4273 PHE A C     1 
ATOM   21684 O  O     . PHE A 1 4273 ? 151.856 186.203 112.004 1.00 44.42  ? 4273 PHE A O     1 
ATOM   21685 C  CB    . PHE A 1 4273 ? 153.256 186.757 114.369 1.00 31.95  ? 4273 PHE A CB    1 
ATOM   21686 C  CG    . PHE A 1 4273 ? 153.916 187.216 115.638 1.00 41.00  ? 4273 PHE A CG    1 
ATOM   21687 C  CD1   . PHE A 1 4273 ? 153.252 187.142 116.850 1.00 44.96  ? 4273 PHE A CD1   1 
ATOM   21688 C  CD2   . PHE A 1 4273 ? 155.195 187.742 115.614 1.00 45.18  ? 4273 PHE A CD2   1 
ATOM   21689 C  CE1   . PHE A 1 4273 ? 153.855 187.570 118.013 1.00 38.93  ? 4273 PHE A CE1   1 
ATOM   21690 C  CE2   . PHE A 1 4273 ? 155.803 188.174 116.775 1.00 41.05  ? 4273 PHE A CE2   1 
ATOM   21691 C  CZ    . PHE A 1 4273 ? 155.132 188.086 117.975 1.00 39.38  ? 4273 PHE A CZ    1 
ATOM   21692 N  N     . THR A 1 4274 ? 151.268 188.351 111.706 1.00 46.50  ? 4274 THR A N     1 
ATOM   21693 C  CA    . THR A 1 4274 ? 150.971 188.218 110.286 1.00 46.02  ? 4274 THR A CA    1 
ATOM   21694 C  C     . THR A 1 4274 ? 151.433 189.482 109.579 1.00 52.48  ? 4274 THR A C     1 
ATOM   21695 O  O     . THR A 1 4274 ? 151.852 190.454 110.210 1.00 54.68  ? 4274 THR A O     1 
ATOM   21696 C  CB    . THR A 1 4274 ? 149.479 187.980 110.024 1.00 51.36  ? 4274 THR A CB    1 
ATOM   21697 O  OG1   . THR A 1 4274 ? 148.713 189.063 110.566 1.00 58.23  ? 4274 THR A OG1   1 
ATOM   21698 C  CG2   . THR A 1 4274 ? 149.013 186.666 110.620 1.00 49.95  ? 4274 THR A CG2   1 
ATOM   21699 N  N     . THR A 1 4275 ? 151.358 189.453 108.246 1.00 58.24  ? 4275 THR A N     1 
ATOM   21700 C  CA    . THR A 1 4275 ? 151.637 190.655 107.468 1.00 58.45  ? 4275 THR A CA    1 
ATOM   21701 C  C     . THR A 1 4275 ? 150.601 191.736 107.734 1.00 61.27  ? 4275 THR A C     1 
ATOM   21702 O  O     . THR A 1 4275 ? 150.916 192.930 107.663 1.00 66.47  ? 4275 THR A O     1 
ATOM   21703 C  CB    . THR A 1 4275 ? 151.676 190.325 105.976 1.00 67.54  ? 4275 THR A CB    1 
ATOM   21704 O  OG1   . THR A 1 4275 ? 150.392 189.847 105.558 1.00 74.41  ? 4275 THR A OG1   1 
ATOM   21705 C  CG2   . THR A 1 4275 ? 152.719 189.257 105.693 1.00 62.86  ? 4275 THR A CG2   1 
ATOM   21706 N  N     . ARG A 1 4276 ? 149.367 191.337 108.054 1.00 63.22  ? 4276 ARG A N     1 
ATOM   21707 C  CA    . ARG A 1 4276 ? 148.296 192.291 108.309 1.00 65.06  ? 4276 ARG A CA    1 
ATOM   21708 C  C     . ARG A 1 4276 ? 148.601 193.199 109.490 1.00 64.95  ? 4276 ARG A C     1 
ATOM   21709 O  O     . ARG A 1 4276 ? 147.995 194.269 109.606 1.00 70.15  ? 4276 ARG A O     1 
ATOM   21710 C  CB    . ARG A 1 4276 ? 146.979 191.551 108.557 1.00 62.54  ? 4276 ARG A CB    1 
ATOM   21711 C  CG    . ARG A 1 4276 ? 146.728 190.352 107.645 1.00 69.25  ? 4276 ARG A CG    1 
ATOM   21712 C  CD    . ARG A 1 4276 ? 146.790 190.687 106.156 1.00 80.45  ? 4276 ARG A CD    1 
ATOM   21713 N  NE    . ARG A 1 4276 ? 146.282 192.018 105.843 1.00 83.37  ? 4276 ARG A NE    1 
ATOM   21714 C  CZ    . ARG A 1 4276 ? 146.700 192.757 104.824 1.00 85.15  ? 4276 ARG A CZ    1 
ATOM   21715 N  NH1   . ARG A 1 4276 ? 147.644 192.329 104.002 1.00 85.00  ? 4276 ARG A NH1   1 
ATOM   21716 N  NH2   . ARG A 1 4276 ? 146.154 193.952 104.623 1.00 81.79  ? 4276 ARG A NH2   1 
ATOM   21717 N  N     . SER A 1 4277 ? 149.524 192.800 110.366 1.00 59.40  ? 4277 SER A N     1 
ATOM   21718 C  CA    . SER A 1 4277 ? 149.923 193.641 111.485 1.00 55.51  ? 4277 SER A CA    1 
ATOM   21719 C  C     . SER A 1 4277 ? 150.725 194.858 111.049 1.00 59.71  ? 4277 SER A C     1 
ATOM   21720 O  O     . SER A 1 4277 ? 150.975 195.739 111.876 1.00 62.63  ? 4277 SER A O     1 
ATOM   21721 C  CB    . SER A 1 4277 ? 150.731 192.826 112.494 1.00 50.55  ? 4277 SER A CB    1 
ATOM   21722 O  OG    . SER A 1 4277 ? 151.971 192.428 111.943 1.00 58.46  ? 4277 SER A OG    1 
ATOM   21723 N  N     . PHE A 1 4278 ? 151.138 194.929 109.787 1.00 63.37  ? 4278 PHE A N     1 
ATOM   21724 C  CA    . PHE A 1 4278 ? 151.845 196.093 109.274 1.00 65.01  ? 4278 PHE A CA    1 
ATOM   21725 C  C     . PHE A 1 4278 ? 150.928 197.047 108.523 1.00 69.66  ? 4278 PHE A C     1 
ATOM   21726 O  O     . PHE A 1 4278 ? 151.414 197.974 107.869 1.00 68.77  ? 4278 PHE A O     1 
ATOM   21727 C  CB    . PHE A 1 4278 ? 153.009 195.655 108.384 1.00 60.10  ? 4278 PHE A CB    1 
ATOM   21728 C  CG    . PHE A 1 4278 ? 154.246 195.299 109.153 1.00 58.35  ? 4278 PHE A CG    1 
ATOM   21729 C  CD1   . PHE A 1 4278 ? 154.248 194.233 110.034 1.00 59.74  ? 4278 PHE A CD1   1 
ATOM   21730 C  CD2   . PHE A 1 4278 ? 155.401 196.044 109.010 1.00 60.39  ? 4278 PHE A CD2   1 
ATOM   21731 C  CE1   . PHE A 1 4278 ? 155.381 193.912 110.749 1.00 55.39  ? 4278 PHE A CE1   1 
ATOM   21732 C  CE2   . PHE A 1 4278 ? 156.536 195.724 109.722 1.00 59.14  ? 4278 PHE A CE2   1 
ATOM   21733 C  CZ    . PHE A 1 4278 ? 156.527 194.657 110.592 1.00 55.62  ? 4278 PHE A CZ    1 
ATOM   21734 N  N     . ASP A 1 4279 ? 149.618 196.838 108.603 1.00 73.18  ? 4279 ASP A N     1 
ATOM   21735 C  CA    . ASP A 1 4279 ? 148.659 197.765 108.029 1.00 82.53  ? 4279 ASP A CA    1 
ATOM   21736 C  C     . ASP A 1 4279 ? 148.382 198.912 108.995 1.00 85.60  ? 4279 ASP A C     1 
ATOM   21737 O  O     . ASP A 1 4279 ? 148.754 198.877 110.171 1.00 85.66  ? 4279 ASP A O     1 
ATOM   21738 C  CB    . ASP A 1 4279 ? 147.355 197.047 107.685 1.00 81.85  ? 4279 ASP A CB    1 
ATOM   21739 C  CG    . ASP A 1 4279 ? 147.403 196.373 106.332 1.00 87.93  ? 4279 ASP A CG    1 
ATOM   21740 O  OD1   . ASP A 1 4279 ? 148.485 196.365 105.709 1.00 85.72  ? 4279 ASP A OD1   1 
ATOM   21741 O  OD2   . ASP A 1 4279 ? 146.357 195.855 105.890 1.00 91.39  ? 4279 ASP A OD2   1 
ATOM   21742 N  N     . SER A 1 4280 ? 147.718 199.945 108.478 1.00 83.00  ? 4280 SER A N     1 
ATOM   21743 C  CA    . SER A 1 4280 ? 147.346 201.090 109.297 1.00 89.58  ? 4280 SER A CA    1 
ATOM   21744 C  C     . SER A 1 4280 ? 146.067 200.861 110.090 1.00 94.94  ? 4280 SER A C     1 
ATOM   21745 O  O     . SER A 1 4280 ? 145.757 201.663 110.977 1.00 95.08  ? 4280 SER A O     1 
ATOM   21746 C  CB    . SER A 1 4280 ? 147.189 202.334 108.419 1.00 89.89  ? 4280 SER A CB    1 
ATOM   21747 O  OG    . SER A 1 4280 ? 146.116 202.182 107.508 1.00 93.68  ? 4280 SER A OG    1 
ATOM   21748 N  N     . GLU A 1 4281 ? 145.324 199.790 109.801 1.00 91.76  ? 4281 GLU A N     1 
ATOM   21749 C  CA    . GLU A 1 4281 ? 144.052 199.519 110.462 1.00 85.06  ? 4281 GLU A CA    1 
ATOM   21750 C  C     . GLU A 1 4281 ? 144.062 198.197 111.222 1.00 83.41  ? 4281 GLU A C     1 
ATOM   21751 O  O     . GLU A 1 4281 ? 142.994 197.668 111.547 1.00 86.21  ? 4281 GLU A O     1 
ATOM   21752 C  CB    . GLU A 1 4281 ? 142.909 199.537 109.444 1.00 88.39  ? 4281 GLU A CB    1 
ATOM   21753 C  CG    . GLU A 1 4281 ? 142.940 198.386 108.446 1.00 97.38  ? 4281 GLU A CG    1 
ATOM   21754 C  CD    . GLU A 1 4281 ? 143.826 198.666 107.245 1.00 100.24 ? 4281 GLU A CD    1 
ATOM   21755 O  OE1   . GLU A 1 4281 ? 144.642 199.609 107.306 1.00 95.66  ? 4281 GLU A OE1   1 
ATOM   21756 O  OE2   . GLU A 1 4281 ? 143.709 197.937 106.238 1.00 104.01 ? 4281 GLU A OE2   1 
ATOM   21757 N  N     . PHE A 1 4282 ? 145.240 197.652 111.513 1.00 81.35  ? 4282 PHE A N     1 
ATOM   21758 C  CA    . PHE A 1 4282 ? 145.315 196.410 112.269 1.00 69.80  ? 4282 PHE A CA    1 
ATOM   21759 C  C     . PHE A 1 4282 ? 144.776 196.606 113.679 1.00 65.89  ? 4282 PHE A C     1 
ATOM   21760 O  O     . PHE A 1 4282 ? 145.073 197.601 114.345 1.00 72.54  ? 4282 PHE A O     1 
ATOM   21761 C  CB    . PHE A 1 4282 ? 146.751 195.899 112.328 1.00 64.15  ? 4282 PHE A CB    1 
ATOM   21762 C  CG    . PHE A 1 4282 ? 146.874 194.530 112.927 1.00 60.27  ? 4282 PHE A CG    1 
ATOM   21763 C  CD1   . PHE A 1 4282 ? 146.323 193.431 112.295 1.00 61.04  ? 4282 PHE A CD1   1 
ATOM   21764 C  CD2   . PHE A 1 4282 ? 147.535 194.345 114.128 1.00 57.62  ? 4282 PHE A CD2   1 
ATOM   21765 C  CE1   . PHE A 1 4282 ? 146.427 192.174 112.851 1.00 54.19  ? 4282 PHE A CE1   1 
ATOM   21766 C  CE2   . PHE A 1 4282 ? 147.643 193.091 114.685 1.00 52.61  ? 4282 PHE A CE2   1 
ATOM   21767 C  CZ    . PHE A 1 4282 ? 147.088 192.005 114.045 1.00 53.91  ? 4282 PHE A CZ    1 
ATOM   21768 N  N     . LYS A 1 4283 ? 143.981 195.644 114.132 1.00 59.89  ? 4283 LYS A N     1 
ATOM   21769 C  CA    . LYS A 1 4283 ? 143.303 195.721 115.420 1.00 63.18  ? 4283 LYS A CA    1 
ATOM   21770 C  C     . LYS A 1 4283 ? 143.994 194.773 116.394 1.00 62.27  ? 4283 LYS A C     1 
ATOM   21771 O  O     . LYS A 1 4283 ? 143.877 193.549 116.267 1.00 69.25  ? 4283 LYS A O     1 
ATOM   21772 C  CB    . LYS A 1 4283 ? 141.825 195.379 115.263 1.00 69.48  ? 4283 LYS A CB    1 
ATOM   21773 C  CG    . LYS A 1 4283 ? 141.095 196.318 114.305 1.00 77.03  ? 4283 LYS A CG    1 
ATOM   21774 C  CD    . LYS A 1 4283 ? 141.037 197.746 114.836 1.00 78.90  ? 4283 LYS A CD    1 
ATOM   21775 C  CE    . LYS A 1 4283 ? 140.167 198.616 113.947 1.00 85.31  ? 4283 LYS A CE    1 
ATOM   21776 N  NZ    . LYS A 1 4283 ? 140.811 198.839 112.621 1.00 88.14  ? 4283 LYS A NZ    1 
ATOM   21777 N  N     . LEU A 1 4284 ? 144.709 195.340 117.370 1.00 57.66  ? 4284 LEU A N     1 
ATOM   21778 C  CA    . LEU A 1 4284 ? 145.401 194.509 118.349 1.00 54.60  ? 4284 LEU A CA    1 
ATOM   21779 C  C     . LEU A 1 4284 ? 144.415 193.690 119.170 1.00 60.79  ? 4284 LEU A C     1 
ATOM   21780 O  O     . LEU A 1 4284 ? 144.657 192.512 119.451 1.00 66.65  ? 4284 LEU A O     1 
ATOM   21781 C  CB    . LEU A 1 4284 ? 146.267 195.381 119.259 1.00 48.81  ? 4284 LEU A CB    1 
ATOM   21782 C  CG    . LEU A 1 4284 ? 147.567 195.899 118.646 1.00 50.08  ? 4284 LEU A CG    1 
ATOM   21783 C  CD1   . LEU A 1 4284 ? 148.262 196.856 119.593 1.00 48.97  ? 4284 LEU A CD1   1 
ATOM   21784 C  CD2   . LEU A 1 4284 ? 148.474 194.744 118.288 1.00 56.06  ? 4284 LEU A CD2   1 
ATOM   21785 N  N     . ALA A 1 4285 ? 143.299 194.296 119.566 1.00 59.57  ? 4285 ALA A N     1 
ATOM   21786 C  CA    . ALA A 1 4285 ? 142.262 193.596 120.309 1.00 65.08  ? 4285 ALA A CA    1 
ATOM   21787 C  C     . ALA A 1 4285 ? 140.904 194.090 119.841 1.00 76.25  ? 4285 ALA A C     1 
ATOM   21788 O  O     . ALA A 1 4285 ? 140.665 195.299 119.790 1.00 76.41  ? 4285 ALA A O     1 
ATOM   21789 C  CB    . ALA A 1 4285 ? 142.414 193.809 121.818 1.00 58.87  ? 4285 ALA A CB    1 
ATOM   21790 N  N     . CYS A 1 4286 ? 140.024 193.156 119.501 1.00 85.92  ? 4286 CYS A N     1 
ATOM   21791 C  CA    . CYS A 1 4286 ? 138.692 193.473 119.011 1.00 86.36  ? 4286 CYS A CA    1 
ATOM   21792 C  C     . CYS A 1 4286 ? 137.671 193.373 120.138 1.00 86.48  ? 4286 CYS A C     1 
ATOM   21793 O  O     . CYS A 1 4286 ? 137.947 192.846 121.218 1.00 82.57  ? 4286 CYS A O     1 
ATOM   21794 C  CB    . CYS A 1 4286 ? 138.312 192.543 117.855 1.00 85.32  ? 4286 CYS A CB    1 
ATOM   21795 S  SG    . CYS A 1 4286 ? 139.326 192.749 116.375 1.00 98.54  ? 4286 CYS A SG    1 
ATOM   21796 N  N     . LYS A 1 4287 ? 136.473 193.897 119.859 1.00 87.71  ? 4287 LYS A N     1 
ATOM   21797 C  CA    . LYS A 1 4287 ? 135.341 193.952 120.782 1.00 91.29  ? 4287 LYS A CA    1 
ATOM   21798 C  C     . LYS A 1 4287 ? 135.761 194.334 122.199 1.00 93.09  ? 4287 LYS A C     1 
ATOM   21799 O  O     . LYS A 1 4287 ? 135.252 193.785 123.182 1.00 93.80  ? 4287 LYS A O     1 
ATOM   21800 C  CB    . LYS A 1 4287 ? 134.566 192.623 120.763 1.00 93.98  ? 4287 LYS A CB    1 
ATOM   21801 C  CG    . LYS A 1 4287 ? 135.266 191.401 121.351 1.00 94.77  ? 4287 LYS A CG    1 
ATOM   21802 C  CD    . LYS A 1 4287 ? 134.479 190.129 121.075 1.00 96.13  ? 4287 LYS A CD    1 
ATOM   21803 C  CE    . LYS A 1 4287 ? 134.316 189.888 119.581 1.00 94.02  ? 4287 LYS A CE    1 
ATOM   21804 N  NZ    . LYS A 1 4287 ? 135.626 189.814 118.876 1.00 90.20  ? 4287 LYS A NZ    1 
ATOM   21805 N  N     . VAL A 1 4288 ? 136.669 195.304 122.311 1.00 92.26  ? 4288 VAL A N     1 
ATOM   21806 C  CA    . VAL A 1 4288 ? 137.137 195.749 123.617 1.00 86.04  ? 4288 VAL A CA    1 
ATOM   21807 C  C     . VAL A 1 4288 ? 136.015 196.487 124.333 1.00 92.90  ? 4288 VAL A C     1 
ATOM   21808 O  O     . VAL A 1 4288 ? 135.451 197.453 123.805 1.00 101.15 ? 4288 VAL A O     1 
ATOM   21809 C  CB    . VAL A 1 4288 ? 138.382 196.635 123.465 1.00 83.06  ? 4288 VAL A CB    1 
ATOM   21810 C  CG1   . VAL A 1 4288 ? 138.746 197.263 124.789 1.00 74.82  ? 4288 VAL A CG1   1 
ATOM   21811 C  CG2   . VAL A 1 4288 ? 139.545 195.822 122.930 1.00 75.15  ? 4288 VAL A CG2   1 
ATOM   21812 N  N     . ASP A 1 4289 ? 135.681 196.026 125.541 1.00 88.55  ? 4289 ASP A N     1 
ATOM   21813 C  CA    . ASP A 1 4289 ? 134.605 196.579 126.366 1.00 96.67  ? 4289 ASP A CA    1 
ATOM   21814 C  C     . ASP A 1 4289 ? 133.246 196.532 125.673 1.00 103.90 ? 4289 ASP A C     1 
ATOM   21815 O  O     . ASP A 1 4289 ? 132.302 197.199 126.110 1.00 102.25 ? 4289 ASP A O     1 
ATOM   21816 C  CB    . ASP A 1 4289 ? 134.910 198.017 126.809 1.00 99.82  ? 4289 ASP A CB    1 
ATOM   21817 C  CG    . ASP A 1 4289 ? 136.347 198.204 127.247 1.00 98.52  ? 4289 ASP A CG    1 
ATOM   21818 O  OD1   . ASP A 1 4289 ? 136.808 197.441 128.121 1.00 88.57  ? 4289 ASP A OD1   1 
ATOM   21819 O  OD2   . ASP A 1 4289 ? 137.010 199.127 126.731 1.00 100.03 ? 4289 ASP A OD2   1 
ATOM   21820 N  N     . GLY A 1 4290 ? 133.125 195.759 124.594 1.00 104.61 ? 4290 GLY A N     1 
ATOM   21821 C  CA    . GLY A 1 4290 ? 131.895 195.675 123.840 1.00 105.66 ? 4290 GLY A CA    1 
ATOM   21822 C  C     . GLY A 1 4290 ? 131.711 196.755 122.795 1.00 112.87 ? 4290 GLY A C     1 
ATOM   21823 O  O     . GLY A 1 4290 ? 130.825 196.623 121.943 1.00 113.40 ? 4290 GLY A O     1 
ATOM   21824 N  N     . HIS A 1 4291 ? 132.521 197.810 122.827 1.00 116.70 ? 4291 HIS A N     1 
ATOM   21825 C  CA    . HIS A 1 4291 ? 132.462 198.856 121.816 1.00 120.50 ? 4291 HIS A CA    1 
ATOM   21826 C  C     . HIS A 1 4291 ? 133.826 199.525 121.732 1.00 121.92 ? 4291 HIS A C     1 
ATOM   21827 O  O     . HIS A 1 4291 ? 134.458 199.778 122.759 1.00 118.29 ? 4291 HIS A O     1 
ATOM   21828 C  CB    . HIS A 1 4291 ? 131.375 199.889 122.135 1.00 124.90 ? 4291 HIS A CB    1 
ATOM   21829 C  CG    . HIS A 1 4291 ? 131.556 201.194 121.425 1.00 130.45 ? 4291 HIS A CG    1 
ATOM   21830 N  ND1   . HIS A 1 4291 ? 131.699 202.391 122.094 1.00 132.98 ? 4291 HIS A ND1   1 
ATOM   21831 C  CD2   . HIS A 1 4291 ? 131.624 201.490 120.106 1.00 128.69 ? 4291 HIS A CD2   1 
ATOM   21832 C  CE1   . HIS A 1 4291 ? 131.843 203.369 121.217 1.00 131.45 ? 4291 HIS A CE1   1 
ATOM   21833 N  NE2   . HIS A 1 4291 ? 131.802 202.849 120.003 1.00 130.67 ? 4291 HIS A NE2   1 
ATOM   21834 N  N     . LYS A 1 4292 ? 134.264 199.798 120.499 1.00 117.88 ? 4292 LYS A N     1 
ATOM   21835 C  CA    . LYS A 1 4292 ? 135.578 200.356 120.179 1.00 111.83 ? 4292 LYS A CA    1 
ATOM   21836 C  C     . LYS A 1 4292 ? 136.662 199.308 120.413 1.00 105.93 ? 4292 LYS A C     1 
ATOM   21837 O  O     . LYS A 1 4292 ? 136.610 198.554 121.390 1.00 103.18 ? 4292 LYS A O     1 
ATOM   21838 C  CB    . LYS A 1 4292 ? 135.849 201.643 120.977 1.00 112.73 ? 4292 LYS A CB    1 
ATOM   21839 C  CG    . LYS A 1 4292 ? 137.119 202.389 120.574 1.00 108.86 ? 4292 LYS A CG    1 
ATOM   21840 C  CD    . LYS A 1 4292 ? 138.343 201.976 121.384 1.00 109.08 ? 4292 LYS A CD    1 
ATOM   21841 C  CE    . LYS A 1 4292 ? 139.563 202.798 120.985 1.00 104.48 ? 4292 LYS A CE    1 
ATOM   21842 N  NZ    . LYS A 1 4292 ? 140.778 202.390 121.741 1.00 90.99  ? 4292 LYS A NZ    1 
ATOM   21843 N  N     . ASP A 1 4293 ? 137.648 199.255 119.520 1.00 100.23 ? 4293 ASP A N     1 
ATOM   21844 C  CA    . ASP A 1 4293 ? 138.677 198.227 119.542 1.00 87.64  ? 4293 ASP A CA    1 
ATOM   21845 C  C     . ASP A 1 4293 ? 140.058 198.859 119.413 1.00 81.27  ? 4293 ASP A C     1 
ATOM   21846 O  O     . ASP A 1 4293 ? 140.230 199.894 118.762 1.00 85.92  ? 4293 ASP A O     1 
ATOM   21847 C  CB    . ASP A 1 4293 ? 138.444 197.190 118.429 1.00 88.71  ? 4293 ASP A CB    1 
ATOM   21848 C  CG    . ASP A 1 4293 ? 138.262 197.824 117.064 1.00 95.67  ? 4293 ASP A CG    1 
ATOM   21849 O  OD1   . ASP A 1 4293 ? 138.088 199.059 117.003 1.00 97.23  ? 4293 ASP A OD1   1 
ATOM   21850 O  OD2   . ASP A 1 4293 ? 138.289 197.082 116.056 1.00 94.91  ? 4293 ASP A OD2   1 
ATOM   21851 N  N     . ILE A 1 4294 ? 141.044 198.219 120.043 1.00 72.55  ? 4294 ILE A N     1 
ATOM   21852 C  CA    . ILE A 1 4294 ? 142.396 198.765 120.090 1.00 65.63  ? 4294 ILE A CA    1 
ATOM   21853 C  C     . ILE A 1 4294 ? 143.025 198.706 118.707 1.00 67.24  ? 4294 ILE A C     1 
ATOM   21854 O  O     . ILE A 1 4294 ? 143.017 197.660 118.045 1.00 74.64  ? 4294 ILE A O     1 
ATOM   21855 C  CB    . ILE A 1 4294 ? 143.249 198.009 121.119 1.00 59.16  ? 4294 ILE A CB    1 
ATOM   21856 C  CG1   . ILE A 1 4294 ? 142.570 198.034 122.485 1.00 63.59  ? 4294 ILE A CG1   1 
ATOM   21857 C  CG2   . ILE A 1 4294 ? 144.622 198.635 121.230 1.00 53.30  ? 4294 ILE A CG2   1 
ATOM   21858 C  CD1   . ILE A 1 4294 ? 143.260 197.203 123.537 1.00 60.23  ? 4294 ILE A CD1   1 
ATOM   21859 N  N     . GLN A 1 4295 ? 143.578 199.832 118.265 1.00 66.99  ? 4295 GLN A N     1 
ATOM   21860 C  CA    . GLN A 1 4295 ? 144.261 199.927 116.986 1.00 66.03  ? 4295 GLN A CA    1 
ATOM   21861 C  C     . GLN A 1 4295 ? 145.766 199.987 117.203 1.00 60.10  ? 4295 GLN A C     1 
ATOM   21862 O  O     . GLN A 1 4295 ? 146.254 200.641 118.129 1.00 68.11  ? 4295 GLN A O     1 
ATOM   21863 C  CB    . GLN A 1 4295 ? 143.804 201.154 116.189 1.00 70.66  ? 4295 GLN A CB    1 
ATOM   21864 C  CG    . GLN A 1 4295 ? 142.415 201.031 115.596 1.00 79.90  ? 4295 GLN A CG    1 
ATOM   21865 C  CD    . GLN A 1 4295 ? 142.279 201.790 114.293 1.00 87.37  ? 4295 GLN A CD    1 
ATOM   21866 O  OE1   . GLN A 1 4295 ? 141.922 201.220 113.263 1.00 88.22  ? 4295 GLN A OE1   1 
ATOM   21867 N  NE2   . GLN A 1 4295 ? 142.569 203.083 114.331 1.00 88.62  ? 4295 GLN A NE2   1 
ATOM   21868 N  N     . MET A 1 4296 ? 146.492 199.291 116.342 1.00 57.12  ? 4296 MET A N     1 
ATOM   21869 C  CA    . MET A 1 4296 ? 147.938 199.253 116.452 1.00 62.51  ? 4296 MET A CA    1 
ATOM   21870 C  C     . MET A 1 4296 ? 148.533 200.572 115.961 1.00 63.84  ? 4296 MET A C     1 
ATOM   21871 O  O     . MET A 1 4296 ? 148.079 201.118 114.950 1.00 68.69  ? 4296 MET A O     1 
ATOM   21872 C  CB    . MET A 1 4296 ? 148.487 198.078 115.647 1.00 58.91  ? 4296 MET A CB    1 
ATOM   21873 C  CG    . MET A 1 4296 ? 149.977 197.880 115.750 1.00 55.73  ? 4296 MET A CG    1 
ATOM   21874 S  SD    . MET A 1 4296 ? 150.522 196.425 114.858 1.00 73.21  ? 4296 MET A SD    1 
ATOM   21875 C  CE    . MET A 1 4296 ? 152.285 196.556 115.097 1.00 61.67  ? 4296 MET A CE    1 
ATOM   21876 N  N     . PRO A 1 4297 ? 149.537 201.112 116.655 1.00 59.08  ? 4297 PRO A N     1 
ATOM   21877 C  CA    . PRO A 1 4297 ? 150.082 202.419 116.269 1.00 60.95  ? 4297 PRO A CA    1 
ATOM   21878 C  C     . PRO A 1 4297 ? 150.663 202.415 114.864 1.00 69.04  ? 4297 PRO A C     1 
ATOM   21879 O  O     . PRO A 1 4297 ? 151.235 201.425 114.405 1.00 73.53  ? 4297 PRO A O     1 
ATOM   21880 C  CB    . PRO A 1 4297 ? 151.164 202.678 117.324 1.00 59.86  ? 4297 PRO A CB    1 
ATOM   21881 C  CG    . PRO A 1 4297 ? 151.471 201.343 117.902 1.00 56.96  ? 4297 PRO A CG    1 
ATOM   21882 C  CD    . PRO A 1 4297 ? 150.188 200.585 117.864 1.00 57.46  ? 4297 PRO A CD    1 
ATOM   21883 N  N     . ASP A 1 4298 ? 150.508 203.551 114.184 1.00 71.91  ? 4298 ASP A N     1 
ATOM   21884 C  CA    . ASP A 1 4298 ? 150.944 203.695 112.802 1.00 77.26  ? 4298 ASP A CA    1 
ATOM   21885 C  C     . ASP A 1 4298 ? 152.450 203.918 112.700 1.00 78.67  ? 4298 ASP A C     1 
ATOM   21886 O  O     . ASP A 1 4298 ? 153.032 203.687 111.636 1.00 84.09  ? 4298 ASP A O     1 
ATOM   21887 C  CB    . ASP A 1 4298 ? 150.174 204.860 112.162 1.00 87.20  ? 4298 ASP A CB    1 
ATOM   21888 C  CG    . ASP A 1 4298 ? 150.362 204.960 110.651 1.00 96.06  ? 4298 ASP A CG    1 
ATOM   21889 O  OD1   . ASP A 1 4298 ? 151.100 204.152 110.054 1.00 96.61  ? 4298 ASP A OD1   1 
ATOM   21890 O  OD2   . ASP A 1 4298 ? 149.762 205.877 110.051 1.00 98.39  ? 4298 ASP A OD2   1 
ATOM   21891 N  N     . GLY A 1 4299 ? 153.100 204.324 113.790 1.00 75.05  ? 4299 GLY A N     1 
ATOM   21892 C  CA    . GLY A 1 4299 ? 154.501 204.685 113.724 1.00 78.63  ? 4299 GLY A CA    1 
ATOM   21893 C  C     . GLY A 1 4299 ? 155.399 203.512 113.381 1.00 77.43  ? 4299 GLY A C     1 
ATOM   21894 O  O     . GLY A 1 4299 ? 155.028 202.345 113.492 1.00 75.37  ? 4299 GLY A O     1 
ATOM   21895 N  N     . ILE A 1 4300 ? 156.613 203.842 112.942 1.00 79.68  ? 4300 ILE A N     1 
ATOM   21896 C  CA    . ILE A 1 4300 ? 157.600 202.855 112.524 1.00 81.17  ? 4300 ILE A CA    1 
ATOM   21897 C  C     . ILE A 1 4300 ? 158.910 203.010 113.296 1.00 81.74  ? 4300 ILE A C     1 
ATOM   21898 O  O     . ILE A 1 4300 ? 159.950 202.535 112.858 1.00 84.02  ? 4300 ILE A O     1 
ATOM   21899 C  CB    . ILE A 1 4300 ? 157.840 202.922 111.003 1.00 80.47  ? 4300 ILE A CB    1 
ATOM   21900 C  CG1   . ILE A 1 4300 ? 158.399 204.288 110.610 1.00 77.65  ? 4300 ILE A CG1   1 
ATOM   21901 C  CG2   . ILE A 1 4300 ? 156.554 202.637 110.242 1.00 81.48  ? 4300 ILE A CG2   1 
ATOM   21902 C  CD1   . ILE A 1 4300 ? 158.877 204.361 109.179 1.00 77.67  ? 4300 ILE A CD1   1 
ATOM   21903 N  N     . ARG A 1 4301 ? 158.864 203.672 114.449 1.00 80.12  ? 4301 ARG A N     1 
ATOM   21904 C  CA    . ARG A 1 4301 ? 160.035 203.908 115.279 1.00 74.59  ? 4301 ARG A CA    1 
ATOM   21905 C  C     . ARG A 1 4301 ? 159.743 203.448 116.697 1.00 68.72  ? 4301 ARG A C     1 
ATOM   21906 O  O     . ARG A 1 4301 ? 158.586 203.400 117.121 1.00 72.97  ? 4301 ARG A O     1 
ATOM   21907 C  CB    . ARG A 1 4301 ? 160.434 205.388 115.298 1.00 76.69  ? 4301 ARG A CB    1 
ATOM   21908 C  CG    . ARG A 1 4301 ? 161.291 205.840 114.131 1.00 80.53  ? 4301 ARG A CG    1 
ATOM   21909 C  CD    . ARG A 1 4301 ? 160.425 206.164 112.935 1.00 88.36  ? 4301 ARG A CD    1 
ATOM   21910 N  NE    . ARG A 1 4301 ? 159.374 207.113 113.282 1.00 93.74  ? 4301 ARG A NE    1 
ATOM   21911 C  CZ    . ARG A 1 4301 ? 159.526 208.429 113.298 1.00 100.72 ? 4301 ARG A CZ    1 
ATOM   21912 N  NH1   . ARG A 1 4301 ? 160.677 208.996 112.974 1.00 100.32 ? 4301 ARG A NH1   1 
ATOM   21913 N  NH2   . ARG A 1 4301 ? 158.500 209.195 113.655 1.00 101.08 ? 4301 ARG A NH2   1 
ATOM   21914 N  N     . ARG A 1 4302 ? 160.805 203.115 117.431 1.00 60.69  ? 4302 ARG A N     1 
ATOM   21915 C  CA    . ARG A 1 4302 ? 160.634 202.640 118.801 1.00 60.41  ? 4302 ARG A CA    1 
ATOM   21916 C  C     . ARG A 1 4302 ? 159.963 203.689 119.681 1.00 69.14  ? 4302 ARG A C     1 
ATOM   21917 O  O     . ARG A 1 4302 ? 159.072 203.361 120.476 1.00 74.99  ? 4302 ARG A O     1 
ATOM   21918 C  CB    . ARG A 1 4302 ? 161.987 202.238 119.385 1.00 64.64  ? 4302 ARG A CB    1 
ATOM   21919 C  CG    . ARG A 1 4302 ? 161.950 201.887 120.857 1.00 62.97  ? 4302 ARG A CG    1 
ATOM   21920 C  CD    . ARG A 1 4302 ? 163.348 201.889 121.444 1.00 68.38  ? 4302 ARG A CD    1 
ATOM   21921 N  NE    . ARG A 1 4302 ? 163.362 201.496 122.847 1.00 70.44  ? 4302 ARG A NE    1 
ATOM   21922 C  CZ    . ARG A 1 4302 ? 162.867 202.221 123.841 1.00 69.07  ? 4302 ARG A CZ    1 
ATOM   21923 N  NH1   . ARG A 1 4302 ? 162.328 203.410 123.629 1.00 70.49  ? 4302 ARG A NH1   1 
ATOM   21924 N  NH2   . ARG A 1 4302 ? 162.926 201.745 125.081 1.00 64.49  ? 4302 ARG A NH2   1 
ATOM   21925 N  N     . GLU A 1 4303 ? 160.368 204.957 119.552 1.00 73.68  ? 4303 GLU A N     1 
ATOM   21926 C  CA    . GLU A 1 4303 ? 159.789 205.996 120.399 1.00 73.12  ? 4303 GLU A CA    1 
ATOM   21927 C  C     . GLU A 1 4303 ? 158.296 206.152 120.140 1.00 68.88  ? 4303 GLU A C     1 
ATOM   21928 O  O     . GLU A 1 4303 ? 157.527 206.419 121.068 1.00 65.96  ? 4303 GLU A O     1 
ATOM   21929 C  CB    . GLU A 1 4303 ? 160.518 207.331 120.216 1.00 75.62  ? 4303 GLU A CB    1 
ATOM   21930 C  CG    . GLU A 1 4303 ? 160.336 208.022 118.873 1.00 81.74  ? 4303 GLU A CG    1 
ATOM   21931 C  CD    . GLU A 1 4303 ? 161.309 207.532 117.819 1.00 91.46  ? 4303 GLU A CD    1 
ATOM   21932 O  OE1   . GLU A 1 4303 ? 161.927 206.464 118.016 1.00 89.95  ? 4303 GLU A OE1   1 
ATOM   21933 O  OE2   . GLU A 1 4303 ? 161.465 208.226 116.792 1.00 93.56  ? 4303 GLU A OE2   1 
ATOM   21934 N  N     . GLU A 1 4304 ? 157.863 205.981 118.889 1.00 69.04  ? 4304 GLU A N     1 
ATOM   21935 C  CA    . GLU A 1 4304 ? 156.434 206.035 118.595 1.00 68.23  ? 4304 GLU A CA    1 
ATOM   21936 C  C     . GLU A 1 4304 ? 155.676 204.924 119.312 1.00 64.04  ? 4304 GLU A C     1 
ATOM   21937 O  O     . GLU A 1 4304 ? 154.590 205.154 119.856 1.00 64.67  ? 4304 GLU A O     1 
ATOM   21938 C  CB    . GLU A 1 4304 ? 156.200 205.955 117.088 1.00 70.15  ? 4304 GLU A CB    1 
ATOM   21939 C  CG    . GLU A 1 4304 ? 156.864 207.062 116.297 1.00 82.25  ? 4304 GLU A CG    1 
ATOM   21940 C  CD    . GLU A 1 4304 ? 156.028 207.502 115.113 1.00 87.44  ? 4304 GLU A CD    1 
ATOM   21941 O  OE1   . GLU A 1 4304 ? 154.872 207.926 115.325 1.00 87.72  ? 4304 GLU A OE1   1 
ATOM   21942 O  OE2   . GLU A 1 4304 ? 156.525 207.424 113.972 1.00 88.44  ? 4304 GLU A OE2   1 
ATOM   21943 N  N     . PHE A 1 4305 ? 156.233 203.711 119.326 1.00 61.49  ? 4305 PHE A N     1 
ATOM   21944 C  CA    . PHE A 1 4305 ? 155.566 202.608 120.011 1.00 57.08  ? 4305 PHE A CA    1 
ATOM   21945 C  C     . PHE A 1 4305 ? 155.523 202.833 121.518 1.00 57.00  ? 4305 PHE A C     1 
ATOM   21946 O  O     . PHE A 1 4305 ? 154.502 202.559 122.160 1.00 60.55  ? 4305 PHE A O     1 
ATOM   21947 C  CB    . PHE A 1 4305 ? 156.256 201.287 119.677 1.00 54.53  ? 4305 PHE A CB    1 
ATOM   21948 C  CG    . PHE A 1 4305 ? 156.159 200.909 118.230 1.00 55.95  ? 4305 PHE A CG    1 
ATOM   21949 C  CD1   . PHE A 1 4305 ? 154.926 200.785 117.618 1.00 56.68  ? 4305 PHE A CD1   1 
ATOM   21950 C  CD2   . PHE A 1 4305 ? 157.295 200.673 117.484 1.00 59.02  ? 4305 PHE A CD2   1 
ATOM   21951 C  CE1   . PHE A 1 4305 ? 154.829 200.440 116.288 1.00 57.34  ? 4305 PHE A CE1   1 
ATOM   21952 C  CE2   . PHE A 1 4305 ? 157.204 200.330 116.153 1.00 59.25  ? 4305 PHE A CE2   1 
ATOM   21953 C  CZ    . PHE A 1 4305 ? 155.969 200.211 115.555 1.00 59.00  ? 4305 PHE A CZ    1 
ATOM   21954 N  N     . VAL A 1 4306 ? 156.613 203.336 122.101 1.00 58.08  ? 4306 VAL A N     1 
ATOM   21955 C  CA    . VAL A 1 4306 ? 156.603 203.615 123.535 1.00 58.06  ? 4306 VAL A CA    1 
ATOM   21956 C  C     . VAL A 1 4306 ? 155.614 204.729 123.861 1.00 61.83  ? 4306 VAL A C     1 
ATOM   21957 O  O     . VAL A 1 4306 ? 154.942 204.692 124.898 1.00 61.52  ? 4306 VAL A O     1 
ATOM   21958 C  CB    . VAL A 1 4306 ? 158.019 203.944 124.038 1.00 59.07  ? 4306 VAL A CB    1 
ATOM   21959 C  CG1   . VAL A 1 4306 ? 158.037 203.975 125.555 1.00 62.21  ? 4306 VAL A CG1   1 
ATOM   21960 C  CG2   . VAL A 1 4306 ? 159.003 202.909 123.537 1.00 56.01  ? 4306 VAL A CG2   1 
ATOM   21961 N  N     . GLN A 1 4307 ? 155.509 205.739 122.993 1.00 62.52  ? 4307 GLN A N     1 
ATOM   21962 C  CA    . GLN A 1 4307 ? 154.508 206.782 123.196 1.00 61.20  ? 4307 GLN A CA    1 
ATOM   21963 C  C     . GLN A 1 4307 ? 153.099 206.211 123.137 1.00 60.34  ? 4307 GLN A C     1 
ATOM   21964 O  O     . GLN A 1 4307 ? 152.247 206.561 123.960 1.00 65.23  ? 4307 GLN A O     1 
ATOM   21965 C  CB    . GLN A 1 4307 ? 154.674 207.891 122.158 1.00 62.55  ? 4307 GLN A CB    1 
ATOM   21966 C  CG    . GLN A 1 4307 ? 155.918 208.739 122.339 1.00 72.54  ? 4307 GLN A CG    1 
ATOM   21967 C  CD    . GLN A 1 4307 ? 156.154 209.670 121.170 1.00 77.61  ? 4307 GLN A CD    1 
ATOM   21968 O  OE1   . GLN A 1 4307 ? 155.486 209.574 120.140 1.00 71.97  ? 4307 GLN A OE1   1 
ATOM   21969 N  NE2   . GLN A 1 4307 ? 157.110 210.579 121.320 1.00 80.12  ? 4307 GLN A NE2   1 
ATOM   21970 N  N     . TRP A 1 4308 ? 152.835 205.329 122.172 1.00 59.20  ? 4308 TRP A N     1 
ATOM   21971 C  CA    . TRP A 1 4308 ? 151.514 204.716 122.085 1.00 56.46  ? 4308 TRP A CA    1 
ATOM   21972 C  C     . TRP A 1 4308 ? 151.210 203.898 123.332 1.00 53.31  ? 4308 TRP A C     1 
ATOM   21973 O  O     . TRP A 1 4308 ? 150.069 203.876 123.806 1.00 55.25  ? 4308 TRP A O     1 
ATOM   21974 C  CB    . TRP A 1 4308 ? 151.412 203.849 120.831 1.00 54.13  ? 4308 TRP A CB    1 
ATOM   21975 C  CG    . TRP A 1 4308 ? 150.091 203.152 120.683 1.00 55.25  ? 4308 TRP A CG    1 
ATOM   21976 C  CD1   . TRP A 1 4308 ? 149.006 203.598 119.987 1.00 55.42  ? 4308 TRP A CD1   1 
ATOM   21977 C  CD2   . TRP A 1 4308 ? 149.720 201.878 121.227 1.00 55.70  ? 4308 TRP A CD2   1 
ATOM   21978 N  NE1   . TRP A 1 4308 ? 147.981 202.689 120.072 1.00 59.04  ? 4308 TRP A NE1   1 
ATOM   21979 C  CE2   . TRP A 1 4308 ? 148.395 201.624 120.826 1.00 54.60  ? 4308 TRP A CE2   1 
ATOM   21980 C  CE3   . TRP A 1 4308 ? 150.378 200.931 122.016 1.00 55.33  ? 4308 TRP A CE3   1 
ATOM   21981 C  CZ2   . TRP A 1 4308 ? 147.716 200.464 121.188 1.00 48.38  ? 4308 TRP A CZ2   1 
ATOM   21982 C  CZ3   . TRP A 1 4308 ? 149.702 199.781 122.374 1.00 53.76  ? 4308 TRP A CZ3   1 
ATOM   21983 C  CH2   . TRP A 1 4308 ? 148.386 199.557 121.960 1.00 50.13  ? 4308 TRP A CH2   1 
ATOM   21984 N  N     . VAL A 1 4309 ? 152.219 203.215 123.876 1.00 53.90  ? 4309 VAL A N     1 
ATOM   21985 C  CA    . VAL A 1 4309 ? 152.022 202.464 125.113 1.00 52.92  ? 4309 VAL A CA    1 
ATOM   21986 C  C     . VAL A 1 4309 ? 151.729 203.410 126.272 1.00 60.25  ? 4309 VAL A C     1 
ATOM   21987 O  O     . VAL A 1 4309 ? 150.871 203.132 127.118 1.00 66.55  ? 4309 VAL A O     1 
ATOM   21988 C  CB    . VAL A 1 4309 ? 153.244 201.574 125.405 1.00 51.00  ? 4309 VAL A CB    1 
ATOM   21989 C  CG1   . VAL A 1 4309 ? 153.105 200.910 126.762 1.00 49.30  ? 4309 VAL A CG1   1 
ATOM   21990 C  CG2   . VAL A 1 4309 ? 153.403 200.530 124.326 1.00 51.27  ? 4309 VAL A CG2   1 
ATOM   21991 N  N     . GLU A 1 4310 ? 152.435 204.541 126.333 1.00 61.95  ? 4310 GLU A N     1 
ATOM   21992 C  CA    . GLU A 1 4310 ? 152.259 205.468 127.445 1.00 61.26  ? 4310 GLU A CA    1 
ATOM   21993 C  C     . GLU A 1 4310 ? 150.926 206.203 127.397 1.00 62.52  ? 4310 GLU A C     1 
ATOM   21994 O  O     . GLU A 1 4310 ? 150.465 206.686 128.436 1.00 69.99  ? 4310 GLU A O     1 
ATOM   21995 C  CB    . GLU A 1 4310 ? 153.405 206.479 127.480 1.00 65.03  ? 4310 GLU A CB    1 
ATOM   21996 C  CG    . GLU A 1 4310 ? 154.734 205.887 127.912 1.00 68.84  ? 4310 GLU A CG    1 
ATOM   21997 C  CD    . GLU A 1 4310 ? 155.852 206.908 127.919 1.00 84.02  ? 4310 GLU A CD    1 
ATOM   21998 O  OE1   . GLU A 1 4310 ? 155.616 208.053 127.480 1.00 86.84  ? 4310 GLU A OE1   1 
ATOM   21999 O  OE2   . GLU A 1 4310 ? 156.967 206.567 128.364 1.00 87.28  ? 4310 GLU A OE2   1 
ATOM   22000 N  N     . LEU A 1 4311 ? 150.300 206.303 126.228 1.00 59.90  ? 4311 LEU A N     1 
ATOM   22001 C  CA    . LEU A 1 4311 ? 148.999 206.945 126.103 1.00 60.73  ? 4311 LEU A CA    1 
ATOM   22002 C  C     . LEU A 1 4311 ? 147.845 205.951 126.120 1.00 66.48  ? 4311 LEU A C     1 
ATOM   22003 O  O     . LEU A 1 4311 ? 146.716 206.329 125.792 1.00 73.98  ? 4311 LEU A O     1 
ATOM   22004 C  CB    . LEU A 1 4311 ? 148.937 207.789 124.827 1.00 61.94  ? 4311 LEU A CB    1 
ATOM   22005 C  CG    . LEU A 1 4311 ? 150.099 208.747 124.573 1.00 66.53  ? 4311 LEU A CG    1 
ATOM   22006 C  CD1   . LEU A 1 4311 ? 149.925 209.454 123.241 1.00 65.73  ? 4311 LEU A CD1   1 
ATOM   22007 C  CD2   . LEU A 1 4311 ? 150.218 209.751 125.705 1.00 70.83  ? 4311 LEU A CD2   1 
ATOM   22008 N  N     . LEU A 1 4312 ? 148.101 204.699 126.481 1.00 65.00  ? 4312 LEU A N     1 
ATOM   22009 C  CA    . LEU A 1 4312 ? 147.022 203.734 126.615 1.00 65.52  ? 4312 LEU A CA    1 
ATOM   22010 C  C     . LEU A 1 4312 ? 146.068 204.166 127.725 1.00 70.04  ? 4312 LEU A C     1 
ATOM   22011 O  O     . LEU A 1 4312 ? 146.511 204.577 128.802 1.00 69.01  ? 4312 LEU A O     1 
ATOM   22012 C  CB    . LEU A 1 4312 ? 147.574 202.342 126.919 1.00 63.59  ? 4312 LEU A CB    1 
ATOM   22013 C  CG    . LEU A 1 4312 ? 148.331 201.639 125.795 1.00 58.16  ? 4312 LEU A CG    1 
ATOM   22014 C  CD1   . LEU A 1 4312 ? 148.443 200.151 126.075 1.00 49.38  ? 4312 LEU A CD1   1 
ATOM   22015 C  CD2   . LEU A 1 4312 ? 147.624 201.882 124.479 1.00 60.34  ? 4312 LEU A CD2   1 
ATOM   22016 N  N     . PRO A 1 4313 ? 144.759 204.101 127.490 1.00 73.47  ? 4313 PRO A N     1 
ATOM   22017 C  CA    . PRO A 1 4313 ? 143.805 204.438 128.549 1.00 74.48  ? 4313 PRO A CA    1 
ATOM   22018 C  C     . PRO A 1 4313 ? 143.963 203.513 129.744 1.00 77.66  ? 4313 PRO A C     1 
ATOM   22019 O  O     . PRO A 1 4313 ? 144.242 202.321 129.603 1.00 80.61  ? 4313 PRO A O     1 
ATOM   22020 C  CB    . PRO A 1 4313 ? 142.442 204.251 127.873 1.00 76.24  ? 4313 PRO A CB    1 
ATOM   22021 C  CG    . PRO A 1 4313 ? 142.724 204.374 126.410 1.00 79.67  ? 4313 PRO A CG    1 
ATOM   22022 C  CD    . PRO A 1 4313 ? 144.088 203.792 126.217 1.00 76.50  ? 4313 PRO A CD    1 
ATOM   22023 N  N     . ASP A 1 4314 ? 143.786 204.078 130.933 1.00 78.44  ? 4314 ASP A N     1 
ATOM   22024 C  CA    . ASP A 1 4314 ? 143.879 203.307 132.171 1.00 82.33  ? 4314 ASP A CA    1 
ATOM   22025 C  C     . ASP A 1 4314 ? 142.530 202.676 132.511 1.00 86.99  ? 4314 ASP A C     1 
ATOM   22026 O  O     . ASP A 1 4314 ? 141.997 202.821 133.609 1.00 91.75  ? 4314 ASP A O     1 
ATOM   22027 C  CB    . ASP A 1 4314 ? 144.379 204.202 133.300 1.00 87.03  ? 4314 ASP A CB    1 
ATOM   22028 C  CG    . ASP A 1 4314 ? 144.715 203.429 134.566 1.00 101.09 ? 4314 ASP A CG    1 
ATOM   22029 O  OD1   . ASP A 1 4314 ? 144.537 202.193 134.589 1.00 101.83 ? 4314 ASP A OD1   1 
ATOM   22030 O  OD2   . ASP A 1 4314 ? 145.159 204.065 135.544 1.00 103.44 ? 4314 ASP A OD2   1 
ATOM   22031 N  N     . THR A 1 4315 ? 141.961 201.975 131.535 1.00 82.43  ? 4315 THR A N     1 
ATOM   22032 C  CA    . THR A 1 4315 ? 140.668 201.309 131.659 1.00 80.00  ? 4315 THR A CA    1 
ATOM   22033 C  C     . THR A 1 4315 ? 140.751 199.896 131.102 1.00 74.66  ? 4315 THR A C     1 
ATOM   22034 O  O     . THR A 1 4315 ? 139.891 199.449 130.341 1.00 78.78  ? 4315 THR A O     1 
ATOM   22035 C  CB    . THR A 1 4315 ? 139.567 202.087 130.944 1.00 81.27  ? 4315 THR A CB    1 
ATOM   22036 O  OG1   . THR A 1 4315 ? 139.897 202.217 129.555 1.00 83.93  ? 4315 THR A OG1   1 
ATOM   22037 C  CG2   . THR A 1 4315 ? 139.395 203.471 131.556 1.00 80.13  ? 4315 THR A CG2   1 
ATOM   22038 N  N     . GLN A 1 4316 ? 141.806 199.175 131.470 1.00 64.96  ? 4316 GLN A N     1 
ATOM   22039 C  CA    . GLN A 1 4316 ? 141.992 197.826 130.959 1.00 59.47  ? 4316 GLN A CA    1 
ATOM   22040 C  C     . GLN A 1 4316 ? 140.930 196.886 131.511 1.00 59.59  ? 4316 GLN A C     1 
ATOM   22041 O  O     . GLN A 1 4316 ? 140.609 196.911 132.702 1.00 61.39  ? 4316 GLN A O     1 
ATOM   22042 C  CB    . GLN A 1 4316 ? 143.381 197.301 131.315 1.00 58.94  ? 4316 GLN A CB    1 
ATOM   22043 C  CG    . GLN A 1 4316 ? 143.574 195.830 130.986 1.00 52.48  ? 4316 GLN A CG    1 
ATOM   22044 C  CD    . GLN A 1 4316 ? 144.886 195.285 131.491 1.00 50.04  ? 4316 GLN A CD    1 
ATOM   22045 O  OE1   . GLN A 1 4316 ? 145.952 195.777 131.132 1.00 54.87  ? 4316 GLN A OE1   1 
ATOM   22046 N  NE2   . GLN A 1 4316 ? 144.817 194.257 132.327 1.00 47.90  ? 4316 GLN A NE2   1 
ATOM   22047 N  N     . THR A 1 4317 ? 140.390 196.055 130.635 1.00 55.15  ? 4317 THR A N     1 
ATOM   22048 C  CA    . THR A 1 4317 ? 139.415 195.028 130.955 1.00 53.19  ? 4317 THR A CA    1 
ATOM   22049 C  C     . THR A 1 4317 ? 139.889 193.720 130.347 1.00 53.26  ? 4317 THR A C     1 
ATOM   22050 O  O     . THR A 1 4317 ? 140.754 193.718 129.465 1.00 55.32  ? 4317 THR A O     1 
ATOM   22051 C  CB    . THR A 1 4317 ? 138.023 195.393 130.416 1.00 56.94  ? 4317 THR A CB    1 
ATOM   22052 O  OG1   . THR A 1 4317 ? 138.122 195.751 129.033 1.00 59.54  ? 4317 THR A OG1   1 
ATOM   22053 C  CG2   . THR A 1 4317 ? 137.439 196.558 131.197 1.00 64.30  ? 4317 THR A CG2   1 
ATOM   22054 N  N     . PRO A 1 4318 ? 139.362 192.582 130.810 1.00 49.99  ? 4318 PRO A N     1 
ATOM   22055 C  CA    . PRO A 1 4318 ? 139.762 191.301 130.207 1.00 40.57  ? 4318 PRO A CA    1 
ATOM   22056 C  C     . PRO A 1 4318 ? 139.488 191.212 128.715 1.00 39.05  ? 4318 PRO A C     1 
ATOM   22057 O  O     . PRO A 1 4318 ? 140.054 190.334 128.054 1.00 41.98  ? 4318 PRO A O     1 
ATOM   22058 C  CB    . PRO A 1 4318 ? 138.938 190.276 130.993 1.00 39.28  ? 4318 PRO A CB    1 
ATOM   22059 C  CG    . PRO A 1 4318 ? 138.730 190.913 132.309 1.00 41.65  ? 4318 PRO A CG    1 
ATOM   22060 C  CD    . PRO A 1 4318 ? 138.569 192.381 132.034 1.00 50.97  ? 4318 PRO A CD    1 
ATOM   22061 N  N     . SER A 1 4319 ? 138.641 192.083 128.162 1.00 40.49  ? 4319 SER A N     1 
ATOM   22062 C  CA    . SER A 1 4319 ? 138.454 192.118 126.717 1.00 44.06  ? 4319 SER A CA    1 
ATOM   22063 C  C     . SER A 1 4319 ? 139.731 192.505 125.982 1.00 44.80  ? 4319 SER A C     1 
ATOM   22064 O  O     . SER A 1 4319 ? 139.868 192.191 124.795 1.00 52.18  ? 4319 SER A O     1 
ATOM   22065 C  CB    . SER A 1 4319 ? 137.332 193.087 126.352 1.00 60.93  ? 4319 SER A CB    1 
ATOM   22066 O  OG    . SER A 1 4319 ? 137.746 194.430 126.524 1.00 72.82  ? 4319 SER A OG    1 
ATOM   22067 N  N     . TRP A 1 4320 ? 140.659 193.190 126.653 1.00 43.63  ? 4320 TRP A N     1 
ATOM   22068 C  CA    . TRP A 1 4320 ? 141.967 193.443 126.058 1.00 42.67  ? 4320 TRP A CA    1 
ATOM   22069 C  C     . TRP A 1 4320 ? 142.710 192.140 125.801 1.00 41.54  ? 4320 TRP A C     1 
ATOM   22070 O  O     . TRP A 1 4320 ? 143.396 191.995 124.783 1.00 46.53  ? 4320 TRP A O     1 
ATOM   22071 C  CB    . TRP A 1 4320 ? 142.796 194.353 126.966 1.00 43.60  ? 4320 TRP A CB    1 
ATOM   22072 C  CG    . TRP A 1 4320 ? 142.311 195.764 127.045 1.00 52.50  ? 4320 TRP A CG    1 
ATOM   22073 C  CD1   . TRP A 1 4320 ? 141.021 196.187 127.158 1.00 57.45  ? 4320 TRP A CD1   1 
ATOM   22074 C  CD2   . TRP A 1 4320 ? 143.120 196.945 127.031 1.00 54.73  ? 4320 TRP A CD2   1 
ATOM   22075 N  NE1   . TRP A 1 4320 ? 140.974 197.558 127.206 1.00 60.84  ? 4320 TRP A NE1   1 
ATOM   22076 C  CE2   . TRP A 1 4320 ? 142.251 198.047 127.130 1.00 60.46  ? 4320 TRP A CE2   1 
ATOM   22077 C  CE3   . TRP A 1 4320 ? 144.495 197.177 126.941 1.00 55.87  ? 4320 TRP A CE3   1 
ATOM   22078 C  CZ2   . TRP A 1 4320 ? 142.711 199.361 127.142 1.00 69.36  ? 4320 TRP A CZ2   1 
ATOM   22079 C  CZ3   . TRP A 1 4320 ? 144.949 198.481 126.953 1.00 59.22  ? 4320 TRP A CZ3   1 
ATOM   22080 C  CH2   . TRP A 1 4320 ? 144.061 199.556 127.052 1.00 66.42  ? 4320 TRP A CH2   1 
ATOM   22081 N  N     . LEU A 1 4321 ? 142.586 191.183 126.717 1.00 37.87  ? 4321 LEU A N     1 
ATOM   22082 C  CA    . LEU A 1 4321 ? 143.281 189.909 126.622 1.00 34.81  ? 4321 LEU A CA    1 
ATOM   22083 C  C     . LEU A 1 4321 ? 142.528 188.881 125.790 1.00 42.40  ? 4321 LEU A C     1 
ATOM   22084 O  O     . LEU A 1 4321 ? 143.011 187.755 125.643 1.00 52.23  ? 4321 LEU A O     1 
ATOM   22085 C  CB    . LEU A 1 4321 ? 143.523 189.351 128.025 1.00 33.14  ? 4321 LEU A CB    1 
ATOM   22086 C  CG    . LEU A 1 4321 ? 143.893 190.378 129.096 1.00 35.49  ? 4321 LEU A CG    1 
ATOM   22087 C  CD1   . LEU A 1 4321 ? 144.064 189.701 130.437 1.00 34.98  ? 4321 LEU A CD1   1 
ATOM   22088 C  CD2   . LEU A 1 4321 ? 145.157 191.123 128.714 1.00 37.42  ? 4321 LEU A CD2   1 
ATOM   22089 N  N     . GLY A 1 4322 ? 141.362 189.233 125.255 1.00 36.27  ? 4322 GLY A N     1 
ATOM   22090 C  CA    . GLY A 1 4322 ? 140.506 188.293 124.569 1.00 34.05  ? 4322 GLY A CA    1 
ATOM   22091 C  C     . GLY A 1 4322 ? 139.505 187.603 125.467 1.00 38.79  ? 4322 GLY A C     1 
ATOM   22092 O  O     . GLY A 1 4322 ? 138.581 186.957 124.960 1.00 50.12  ? 4322 GLY A O     1 
ATOM   22093 N  N     . LEU A 1 4323 ? 139.661 187.730 126.780 1.00 33.12  ? 4323 LEU A N     1 
ATOM   22094 C  CA    . LEU A 1 4323 ? 138.747 187.127 127.727 1.00 32.61  ? 4323 LEU A CA    1 
ATOM   22095 C  C     . LEU A 1 4323 ? 137.428 187.895 127.756 1.00 37.14  ? 4323 LEU A C     1 
ATOM   22096 O  O     . LEU A 1 4323 ? 137.365 189.055 127.343 1.00 39.88  ? 4323 LEU A O     1 
ATOM   22097 C  CB    . LEU A 1 4323 ? 139.377 187.119 129.116 1.00 31.81  ? 4323 LEU A CB    1 
ATOM   22098 C  CG    . LEU A 1 4323 ? 140.377 186.004 129.402 1.00 32.49  ? 4323 LEU A CG    1 
ATOM   22099 C  CD1   . LEU A 1 4323 ? 141.224 186.365 130.599 1.00 27.50  ? 4323 LEU A CD1   1 
ATOM   22100 C  CD2   . LEU A 1 4323 ? 139.653 184.699 129.635 1.00 36.71  ? 4323 LEU A CD2   1 
ATOM   22101 N  N     . PRO A 1 4324 ? 136.355 187.265 128.226 1.00 36.60  ? 4324 PRO A N     1 
ATOM   22102 C  CA    . PRO A 1 4324 ? 135.116 188.012 128.453 1.00 36.69  ? 4324 PRO A CA    1 
ATOM   22103 C  C     . PRO A 1 4324 ? 135.270 188.981 129.614 1.00 43.32  ? 4324 PRO A C     1 
ATOM   22104 O  O     . PRO A 1 4324 ? 136.064 188.765 130.532 1.00 48.40  ? 4324 PRO A O     1 
ATOM   22105 C  CB    . PRO A 1 4324 ? 134.096 186.915 128.769 1.00 40.50  ? 4324 PRO A CB    1 
ATOM   22106 C  CG    . PRO A 1 4324 ? 134.910 185.803 129.319 1.00 37.55  ? 4324 PRO A CG    1 
ATOM   22107 C  CD    . PRO A 1 4324 ? 136.205 185.840 128.566 1.00 37.47  ? 4324 PRO A CD    1 
ATOM   22108 N  N     . ASN A 1 4325 ? 134.493 190.065 129.567 1.00 47.55  ? 4325 ASN A N     1 
ATOM   22109 C  CA    . ASN A 1 4325 ? 134.599 191.093 130.597 1.00 48.39  ? 4325 ASN A CA    1 
ATOM   22110 C  C     . ASN A 1 4325 ? 134.145 190.604 131.965 1.00 47.97  ? 4325 ASN A C     1 
ATOM   22111 O  O     . ASN A 1 4325 ? 134.518 191.207 132.976 1.00 48.73  ? 4325 ASN A O     1 
ATOM   22112 C  CB    . ASN A 1 4325 ? 133.795 192.330 130.197 1.00 56.80  ? 4325 ASN A CB    1 
ATOM   22113 C  CG    . ASN A 1 4325 ? 134.482 193.146 129.124 1.00 62.76  ? 4325 ASN A CG    1 
ATOM   22114 O  OD1   . ASN A 1 4325 ? 135.698 193.325 129.151 1.00 52.86  ? 4325 ASN A OD1   1 
ATOM   22115 N  ND2   . ASN A 1 4325 ? 133.705 193.650 128.174 1.00 75.94  ? 4325 ASN A ND2   1 
ATOM   22116 N  N     . ASN A 1 4326 ? 133.354 189.536 132.025 1.00 48.38  ? 4326 ASN A N     1 
ATOM   22117 C  CA    . ASN A 1 4326 ? 132.954 188.966 133.304 1.00 46.32  ? 4326 ASN A CA    1 
ATOM   22118 C  C     . ASN A 1 4326 ? 134.072 188.186 133.980 1.00 46.12  ? 4326 ASN A C     1 
ATOM   22119 O  O     . ASN A 1 4326 ? 133.950 187.873 135.169 1.00 52.01  ? 4326 ASN A O     1 
ATOM   22120 C  CB    . ASN A 1 4326 ? 131.730 188.064 133.125 1.00 55.82  ? 4326 ASN A CB    1 
ATOM   22121 C  CG    . ASN A 1 4326 ? 131.946 186.987 132.083 1.00 62.26  ? 4326 ASN A CG    1 
ATOM   22122 O  OD1   . ASN A 1 4326 ? 131.832 187.240 130.886 1.00 68.47  ? 4326 ASN A OD1   1 
ATOM   22123 N  ND2   . ASN A 1 4326 ? 132.266 185.781 132.532 1.00 60.76  ? 4326 ASN A ND2   1 
ATOM   22124 N  N     . ALA A 1 4327 ? 135.156 187.883 133.259 1.00 47.83  ? 4327 ALA A N     1 
ATOM   22125 C  CA    . ALA A 1 4327 ? 136.271 187.155 133.855 1.00 43.73  ? 4327 ALA A CA    1 
ATOM   22126 C  C     . ALA A 1 4327 ? 136.782 187.861 135.101 1.00 46.82  ? 4327 ALA A C     1 
ATOM   22127 O  O     . ALA A 1 4327 ? 137.004 187.222 136.137 1.00 48.71  ? 4327 ALA A O     1 
ATOM   22128 C  CB    . ALA A 1 4327 ? 137.398 186.994 132.838 1.00 38.82  ? 4327 ALA A CB    1 
ATOM   22129 N  N     . GLU A 1 4328 ? 136.948 189.184 135.023 1.00 46.89  ? 4328 GLU A N     1 
ATOM   22130 C  CA    . GLU A 1 4328 ? 137.343 189.957 136.195 1.00 44.27  ? 4328 GLU A CA    1 
ATOM   22131 C  C     . GLU A 1 4328 ? 136.440 189.648 137.377 1.00 40.35  ? 4328 GLU A C     1 
ATOM   22132 O  O     . GLU A 1 4328 ? 136.925 189.323 138.468 1.00 41.64  ? 4328 GLU A O     1 
ATOM   22133 C  CB    . GLU A 1 4328 ? 137.309 191.450 135.872 1.00 40.57  ? 4328 GLU A CB    1 
ATOM   22134 C  CG    . GLU A 1 4328 ? 137.891 192.338 136.956 1.00 47.37  ? 4328 GLU A CG    1 
ATOM   22135 C  CD    . GLU A 1 4328 ? 139.302 191.944 137.345 1.00 54.69  ? 4328 GLU A CD    1 
ATOM   22136 O  OE1   . GLU A 1 4328 ? 140.199 192.014 136.479 1.00 55.09  ? 4328 GLU A OE1   1 
ATOM   22137 O  OE2   . GLU A 1 4328 ? 139.514 191.565 138.516 1.00 52.22  ? 4328 GLU A OE2   1 
ATOM   22138 N  N     . ARG A 1 4329 ? 135.120 189.689 137.162 1.00 39.61  ? 4329 ARG A N     1 
ATOM   22139 C  CA    . ARG A 1 4329 ? 134.187 189.368 138.235 1.00 36.26  ? 4329 ARG A CA    1 
ATOM   22140 C  C     . ARG A 1 4329 ? 134.512 188.016 138.846 1.00 34.21  ? 4329 ARG A C     1 
ATOM   22141 O  O     . ARG A 1 4329 ? 134.626 187.895 140.072 1.00 42.79  ? 4329 ARG A O     1 
ATOM   22142 C  CB    . ARG A 1 4329 ? 132.752 189.389 137.713 1.00 40.03  ? 4329 ARG A CB    1 
ATOM   22143 C  CG    . ARG A 1 4329 ? 132.269 190.759 137.277 1.00 49.21  ? 4329 ARG A CG    1 
ATOM   22144 C  CD    . ARG A 1 4329 ? 130.833 190.699 136.789 1.00 54.14  ? 4329 ARG A CD    1 
ATOM   22145 N  NE    . ARG A 1 4329 ? 130.082 189.636 137.447 1.00 61.06  ? 4329 ARG A NE    1 
ATOM   22146 C  CZ    . ARG A 1 4329 ? 128.780 189.678 137.688 1.00 70.25  ? 4329 ARG A CZ    1 
ATOM   22147 N  NH1   . ARG A 1 4329 ? 128.044 190.718 137.333 1.00 64.45  ? 4329 ARG A NH1   1 
ATOM   22148 N  NH2   . ARG A 1 4329 ? 128.200 188.649 138.300 1.00 70.38  ? 4329 ARG A NH2   1 
ATOM   22149 N  N     . VAL A 1 4330 ? 134.731 187.002 138.004 1.00 34.89  ? 4330 VAL A N     1 
ATOM   22150 C  CA    . VAL A 1 4330 ? 135.083 185.685 138.523 1.00 38.29  ? 4330 VAL A CA    1 
ATOM   22151 C  C     . VAL A 1 4330 ? 136.320 185.788 139.396 1.00 44.64  ? 4330 VAL A C     1 
ATOM   22152 O  O     . VAL A 1 4330 ? 136.312 185.369 140.561 1.00 50.13  ? 4330 VAL A O     1 
ATOM   22153 C  CB    . VAL A 1 4330 ? 135.290 184.685 137.371 1.00 35.85  ? 4330 VAL A CB    1 
ATOM   22154 C  CG1   . VAL A 1 4330 ? 135.718 183.336 137.919 1.00 33.30  ? 4330 VAL A CG1   1 
ATOM   22155 C  CG2   . VAL A 1 4330 ? 134.027 184.553 136.549 1.00 44.51  ? 4330 VAL A CG2   1 
ATOM   22156 N  N     . LEU A 1 4331 ? 137.375 186.423 138.878 1.00 42.60  ? 4331 LEU A N     1 
ATOM   22157 C  CA    . LEU A 1 4331 ? 138.566 186.621 139.690 1.00 39.80  ? 4331 LEU A CA    1 
ATOM   22158 C  C     . LEU A 1 4331 ? 138.192 187.249 141.020 1.00 41.96  ? 4331 LEU A C     1 
ATOM   22159 O  O     . LEU A 1 4331 ? 138.481 186.683 142.084 1.00 44.36  ? 4331 LEU A O     1 
ATOM   22160 C  CB    . LEU A 1 4331 ? 139.575 187.492 138.942 1.00 39.53  ? 4331 LEU A CB    1 
ATOM   22161 C  CG    . LEU A 1 4331 ? 140.953 187.666 139.578 1.00 38.75  ? 4331 LEU A CG    1 
ATOM   22162 C  CD1   . LEU A 1 4331 ? 141.733 186.366 139.524 1.00 36.68  ? 4331 LEU A CD1   1 
ATOM   22163 C  CD2   . LEU A 1 4331 ? 141.720 188.781 138.889 1.00 40.42  ? 4331 LEU A CD2   1 
ATOM   22164 N  N     . LEU A 1 4332 ? 137.432 188.348 140.973 1.00 41.20  ? 4332 LEU A N     1 
ATOM   22165 C  CA    . LEU A 1 4332 ? 137.036 189.019 142.201 1.00 35.67  ? 4332 LEU A CA    1 
ATOM   22166 C  C     . LEU A 1 4332 ? 136.357 188.049 143.152 1.00 40.83  ? 4332 LEU A C     1 
ATOM   22167 O  O     . LEU A 1 4332 ? 136.787 187.906 144.304 1.00 45.03  ? 4332 LEU A O     1 
ATOM   22168 C  CB    . LEU A 1 4332 ? 136.115 190.196 141.889 1.00 31.88  ? 4332 LEU A CB    1 
ATOM   22169 C  CG    . LEU A 1 4332 ? 136.743 191.370 141.141 1.00 34.84  ? 4332 LEU A CG    1 
ATOM   22170 C  CD1   . LEU A 1 4332 ? 135.744 192.504 141.006 1.00 41.85  ? 4332 LEU A CD1   1 
ATOM   22171 C  CD2   . LEU A 1 4332 ? 137.996 191.838 141.852 1.00 42.29  ? 4332 LEU A CD2   1 
ATOM   22172 N  N     . THR A 1 4333 ? 135.348 187.314 142.670 1.00 41.20  ? 4333 THR A N     1 
ATOM   22173 C  CA    . THR A 1 4333 ? 134.624 186.463 143.603 1.00 43.44  ? 4333 THR A CA    1 
ATOM   22174 C  C     . THR A 1 4333 ? 135.546 185.400 144.175 1.00 46.41  ? 4333 THR A C     1 
ATOM   22175 O  O     . THR A 1 4333 ? 135.509 185.146 145.386 1.00 50.58  ? 4333 THR A O     1 
ATOM   22176 C  CB    . THR A 1 4333 ? 133.371 185.853 142.956 1.00 40.97  ? 4333 THR A CB    1 
ATOM   22177 O  OG1   . THR A 1 4333 ? 132.570 185.233 143.969 1.00 54.22  ? 4333 THR A OG1   1 
ATOM   22178 C  CG2   . THR A 1 4333 ? 133.702 184.820 141.906 1.00 42.34  ? 4333 THR A CG2   1 
ATOM   22179 N  N     . THR A 1 4334 ? 136.446 184.851 143.351 1.00 44.33  ? 4334 THR A N     1 
ATOM   22180 C  CA    . THR A 1 4334 ? 137.414 183.902 143.882 1.00 47.17  ? 4334 THR A CA    1 
ATOM   22181 C  C     . THR A 1 4334 ? 138.191 184.537 145.020 1.00 42.20  ? 4334 THR A C     1 
ATOM   22182 O  O     . THR A 1 4334 ? 138.192 184.020 146.147 1.00 44.47  ? 4334 THR A O     1 
ATOM   22183 C  CB    . THR A 1 4334 ? 138.361 183.433 142.779 1.00 51.51  ? 4334 THR A CB    1 
ATOM   22184 O  OG1   . THR A 1 4334 ? 137.600 182.883 141.696 1.00 55.05  ? 4334 THR A OG1   1 
ATOM   22185 C  CG2   . THR A 1 4334 ? 139.310 182.374 143.310 1.00 49.50  ? 4334 THR A CG2   1 
ATOM   22186 N  N     . GLN A 1 4335 ? 138.762 185.718 144.768 1.00 40.49  ? 4335 GLN A N     1 
ATOM   22187 C  CA    . GLN A 1 4335 ? 139.491 186.419 145.813 1.00 41.02  ? 4335 GLN A CA    1 
ATOM   22188 C  C     . GLN A 1 4335 ? 138.615 186.605 147.039 1.00 43.39  ? 4335 GLN A C     1 
ATOM   22189 O  O     . GLN A 1 4335 ? 139.045 186.312 148.162 1.00 50.30  ? 4335 GLN A O     1 
ATOM   22190 C  CB    . GLN A 1 4335 ? 139.988 187.764 145.290 1.00 39.05  ? 4335 GLN A CB    1 
ATOM   22191 C  CG    . GLN A 1 4335 ? 141.115 187.654 144.282 1.00 39.92  ? 4335 GLN A CG    1 
ATOM   22192 C  CD    . GLN A 1 4335 ? 141.413 188.972 143.602 1.00 48.39  ? 4335 GLN A CD    1 
ATOM   22193 O  OE1   . GLN A 1 4335 ? 140.727 189.968 143.828 1.00 47.15  ? 4335 GLN A OE1   1 
ATOM   22194 N  NE2   . GLN A 1 4335 ? 142.439 188.986 142.762 1.00 52.28  ? 4335 GLN A NE2   1 
ATOM   22195 N  N     . GLY A 1 4336 ? 137.360 187.015 146.834 1.00 42.37  ? 4336 GLY A N     1 
ATOM   22196 C  CA    . GLY A 1 4336 ? 136.469 187.187 147.965 1.00 39.85  ? 4336 GLY A CA    1 
ATOM   22197 C  C     . GLY A 1 4336 ? 136.367 185.921 148.787 1.00 38.56  ? 4336 GLY A C     1 
ATOM   22198 O  O     . GLY A 1 4336 ? 136.647 185.931 149.991 1.00 38.15  ? 4336 GLY A O     1 
ATOM   22199 N  N     . VAL A 1 4337 ? 136.068 184.797 148.131 1.00 43.13  ? 4337 VAL A N     1 
ATOM   22200 C  CA    . VAL A 1 4337 ? 135.993 183.533 148.853 1.00 40.59  ? 4337 VAL A CA    1 
ATOM   22201 C  C     . VAL A 1 4337 ? 137.322 183.257 149.529 1.00 43.23  ? 4337 VAL A C     1 
ATOM   22202 O  O     . VAL A 1 4337 ? 137.376 182.921 150.720 1.00 48.25  ? 4337 VAL A O     1 
ATOM   22203 C  CB    . VAL A 1 4337 ? 135.593 182.391 147.902 1.00 45.92  ? 4337 VAL A CB    1 
ATOM   22204 C  CG1   . VAL A 1 4337 ? 135.686 181.054 148.614 1.00 47.62  ? 4337 VAL A CG1   1 
ATOM   22205 C  CG2   . VAL A 1 4337 ? 134.192 182.617 147.365 1.00 45.99  ? 4337 VAL A CG2   1 
ATOM   22206 N  N     . ASP A 1 4338 ? 138.417 183.472 148.797 1.00 43.51  ? 4338 ASP A N     1 
ATOM   22207 C  CA    . ASP A 1 4338 ? 139.740 183.261 149.362 1.00 39.18  ? 4338 ASP A CA    1 
ATOM   22208 C  C     . ASP A 1 4338 ? 139.907 184.055 150.646 1.00 41.28  ? 4338 ASP A C     1 
ATOM   22209 O  O     . ASP A 1 4338 ? 140.317 183.501 151.675 1.00 44.81  ? 4338 ASP A O     1 
ATOM   22210 C  CB    . ASP A 1 4338 ? 140.802 183.642 148.332 1.00 42.47  ? 4338 ASP A CB    1 
ATOM   22211 C  CG    . ASP A 1 4338 ? 142.199 183.319 148.791 1.00 59.33  ? 4338 ASP A CG    1 
ATOM   22212 O  OD1   . ASP A 1 4338 ? 142.566 182.125 148.799 1.00 60.89  ? 4338 ASP A OD1   1 
ATOM   22213 O  OD2   . ASP A 1 4338 ? 142.939 184.264 149.126 1.00 71.81  ? 4338 ASP A OD2   1 
ATOM   22214 N  N     . MET A 1 4339 ? 139.517 185.335 150.628 1.00 42.49  ? 4339 MET A N     1 
ATOM   22215 C  CA    . MET A 1 4339 ? 139.627 186.147 151.834 1.00 37.81  ? 4339 MET A CA    1 
ATOM   22216 C  C     . MET A 1 4339 ? 138.920 185.475 152.999 1.00 40.05  ? 4339 MET A C     1 
ATOM   22217 O  O     . MET A 1 4339 ? 139.517 185.276 154.065 1.00 43.78  ? 4339 MET A O     1 
ATOM   22218 C  CB    . MET A 1 4339 ? 139.052 187.541 151.593 1.00 36.50  ? 4339 MET A CB    1 
ATOM   22219 C  CG    . MET A 1 4339 ? 138.714 188.287 152.873 1.00 38.69  ? 4339 MET A CG    1 
ATOM   22220 S  SD    . MET A 1 4339 ? 137.948 189.892 152.591 1.00 65.00  ? 4339 MET A SD    1 
ATOM   22221 C  CE    . MET A 1 4339 ? 136.217 189.440 152.551 1.00 48.61  ? 4339 MET A CE    1 
ATOM   22222 N  N     . ILE A 1 4340 ? 137.673 185.051 152.787 1.00 42.84  ? 4340 ILE A N     1 
ATOM   22223 C  CA    . ILE A 1 4340 ? 136.919 184.425 153.867 1.00 42.76  ? 4340 ILE A CA    1 
ATOM   22224 C  C     . ILE A 1 4340 ? 137.640 183.179 154.351 1.00 43.79  ? 4340 ILE A C     1 
ATOM   22225 O  O     . ILE A 1 4340 ? 137.766 182.949 155.561 1.00 49.55  ? 4340 ILE A O     1 
ATOM   22226 C  CB    . ILE A 1 4340 ? 135.482 184.120 153.412 1.00 44.61  ? 4340 ILE A CB    1 
ATOM   22227 C  CG1   . ILE A 1 4340 ? 134.658 185.406 153.388 1.00 49.10  ? 4340 ILE A CG1   1 
ATOM   22228 C  CG2   . ILE A 1 4340 ? 134.840 183.093 154.325 1.00 49.43  ? 4340 ILE A CG2   1 
ATOM   22229 C  CD1   . ILE A 1 4340 ? 133.186 185.180 153.176 1.00 56.53  ? 4340 ILE A CD1   1 
ATOM   22230 N  N     . SER A 1 4341 ? 138.171 182.383 153.419 1.00 41.07  ? 4341 SER A N     1 
ATOM   22231 C  CA    . SER A 1 4341 ? 138.916 181.199 153.827 1.00 41.95  ? 4341 SER A CA    1 
ATOM   22232 C  C     . SER A 1 4341 ? 140.086 181.589 154.715 1.00 45.07  ? 4341 SER A C     1 
ATOM   22233 O  O     . SER A 1 4341 ? 140.278 181.010 155.791 1.00 50.65  ? 4341 SER A O     1 
ATOM   22234 C  CB    . SER A 1 4341 ? 139.398 180.428 152.600 1.00 47.52  ? 4341 SER A CB    1 
ATOM   22235 O  OG    . SER A 1 4341 ? 140.373 181.163 151.885 1.00 54.43  ? 4341 SER A OG    1 
ATOM   22236 N  N     . LYS A 1 4342 ? 140.835 182.621 154.315 1.00 44.83  ? 4342 LYS A N     1 
ATOM   22237 C  CA    . LYS A 1 4342 ? 141.925 183.095 155.157 1.00 38.89  ? 4342 LYS A CA    1 
ATOM   22238 C  C     . LYS A 1 4342 ? 141.400 183.577 156.498 1.00 41.75  ? 4342 LYS A C     1 
ATOM   22239 O  O     . LYS A 1 4342 ? 142.013 183.321 157.539 1.00 53.05  ? 4342 LYS A O     1 
ATOM   22240 C  CB    . LYS A 1 4342 ? 142.702 184.201 154.448 1.00 39.83  ? 4342 LYS A CB    1 
ATOM   22241 C  CG    . LYS A 1 4342 ? 143.575 183.707 153.312 1.00 44.07  ? 4342 LYS A CG    1 
ATOM   22242 C  CD    . LYS A 1 4342 ? 144.075 184.855 152.460 1.00 43.88  ? 4342 LYS A CD    1 
ATOM   22243 C  CE    . LYS A 1 4342 ? 145.007 184.355 151.377 1.00 44.74  ? 4342 LYS A CE    1 
ATOM   22244 N  NZ    . LYS A 1 4342 ? 145.362 185.432 150.418 1.00 55.63  ? 4342 LYS A NZ    1 
ATOM   22245 N  N     . MET A 1 4343 ? 140.246 184.247 156.499 1.00 43.09  ? 4343 MET A N     1 
ATOM   22246 C  CA    . MET A 1 4343 ? 139.694 184.736 157.755 1.00 47.24  ? 4343 MET A CA    1 
ATOM   22247 C  C     . MET A 1 4343 ? 139.273 183.580 158.651 1.00 51.33  ? 4343 MET A C     1 
ATOM   22248 O  O     . MET A 1 4343 ? 139.205 183.728 159.877 1.00 54.40  ? 4343 MET A O     1 
ATOM   22249 C  CB    . MET A 1 4343 ? 138.522 185.677 157.479 1.00 49.25  ? 4343 MET A CB    1 
ATOM   22250 C  CG    . MET A 1 4343 ? 138.891 187.149 157.558 1.00 45.39  ? 4343 MET A CG    1 
ATOM   22251 S  SD    . MET A 1 4343 ? 137.460 188.242 157.553 1.00 64.81  ? 4343 MET A SD    1 
ATOM   22252 C  CE    . MET A 1 4343 ? 136.933 188.125 159.259 1.00 59.90  ? 4343 MET A CE    1 
ATOM   22253 N  N     . LEU A 1 4344 ? 138.988 182.415 158.060 1.00 50.97  ? 4344 LEU A N     1 
ATOM   22254 C  CA    . LEU A 1 4344 ? 138.728 181.231 158.872 1.00 54.71  ? 4344 LEU A CA    1 
ATOM   22255 C  C     . LEU A 1 4344 ? 140.010 180.700 159.494 1.00 55.94  ? 4344 LEU A C     1 
ATOM   22256 O  O     . LEU A 1 4344 ? 139.995 180.165 160.608 1.00 63.48  ? 4344 LEU A O     1 
ATOM   22257 C  CB    . LEU A 1 4344 ? 138.056 180.145 158.033 1.00 57.32  ? 4344 LEU A CB    1 
ATOM   22258 C  CG    . LEU A 1 4344 ? 136.629 180.430 157.582 1.00 58.34  ? 4344 LEU A CG    1 
ATOM   22259 C  CD1   . LEU A 1 4344 ? 136.141 179.346 156.639 1.00 58.89  ? 4344 LEU A CD1   1 
ATOM   22260 C  CD2   . LEU A 1 4344 ? 135.745 180.507 158.805 1.00 59.60  ? 4344 LEU A CD2   1 
ATOM   22261 N  N     . LYS A 1 4345 ? 141.129 180.835 158.786 1.00 53.06  ? 4345 LYS A N     1 
ATOM   22262 C  CA    . LYS A 1 4345 ? 142.381 180.281 159.282 1.00 53.57  ? 4345 LYS A CA    1 
ATOM   22263 C  C     . LYS A 1 4345 ? 142.958 181.139 160.403 1.00 59.77  ? 4345 LYS A C     1 
ATOM   22264 O  O     . LYS A 1 4345 ? 143.798 180.666 161.177 1.00 65.92  ? 4345 LYS A O     1 
ATOM   22265 C  CB    . LYS A 1 4345 ? 143.357 180.135 158.116 1.00 48.69  ? 4345 LYS A CB    1 
ATOM   22266 C  CG    . LYS A 1 4345 ? 144.525 179.214 158.367 1.00 60.60  ? 4345 LYS A CG    1 
ATOM   22267 C  CD    . LYS A 1 4345 ? 145.390 179.129 157.124 1.00 59.46  ? 4345 LYS A CD    1 
ATOM   22268 C  CE    . LYS A 1 4345 ? 144.690 178.351 156.025 1.00 52.75  ? 4345 LYS A CE    1 
ATOM   22269 N  NZ    . LYS A 1 4345 ? 145.551 178.186 154.823 1.00 58.48  ? 4345 LYS A NZ    1 
ATOM   22270 N  N     . MET A 1 4346 ? 142.523 182.393 160.502 1.00 60.30  ? 4346 MET A N     1 
ATOM   22271 C  CA    . MET A 1 4346 ? 142.812 183.268 161.640 1.00 63.41  ? 4346 MET A CA    1 
ATOM   22272 C  C     . MET A 1 4346 ? 141.698 183.225 162.680 1.00 78.15  ? 4346 MET A C     1 
ATOM   22273 O  O     . MET A 1 4346 ? 141.166 184.260 163.079 1.00 83.92  ? 4346 MET A O     1 
ATOM   22274 C  CB    . MET A 1 4346 ? 143.028 184.696 161.152 1.00 65.99  ? 4346 MET A CB    1 
ATOM   22275 C  CG    . MET A 1 4346 ? 143.559 184.798 159.746 1.00 55.34  ? 4346 MET A CG    1 
ATOM   22276 S  SD    . MET A 1 4346 ? 145.187 184.063 159.652 1.00 54.10  ? 4346 MET A SD    1 
ATOM   22277 C  CE    . MET A 1 4346 ? 145.983 184.999 160.946 1.00 52.80  ? 4346 MET A CE    1 
ATOM   22278 N  N     . GLN A 1 4347 ? 141.324 182.031 163.130 1.00 82.52  ? 4347 GLN A N     1 
ATOM   22279 C  CA    . GLN A 1 4347 ? 140.258 181.903 164.116 1.00 87.32  ? 4347 GLN A CA    1 
ATOM   22280 C  C     . GLN A 1 4347 ? 140.735 181.289 165.420 1.00 97.94  ? 4347 GLN A C     1 
ATOM   22281 O  O     . GLN A 1 4347 ? 140.535 181.882 166.487 1.00 99.06  ? 4347 GLN A O     1 
ATOM   22282 C  CB    . GLN A 1 4347 ? 139.098 181.076 163.537 1.00 78.96  ? 4347 GLN A CB    1 
ATOM   22283 C  CG    . GLN A 1 4347 ? 137.744 181.410 164.138 1.00 81.32  ? 4347 GLN A CG    1 
ATOM   22284 C  CD    . GLN A 1 4347 ? 137.158 182.693 163.580 1.00 82.62  ? 4347 GLN A CD    1 
ATOM   22285 O  OE1   . GLN A 1 4347 ? 137.706 183.289 162.653 1.00 79.49  ? 4347 GLN A OE1   1 
ATOM   22286 N  NE2   . GLN A 1 4347 ? 136.039 183.128 164.147 1.00 80.39  ? 4347 GLN A NE2   1 
ATOM   22287 N  N     . MET A 1 4348 ? 141.371 180.118 165.370 1.00 100.43 ? 4348 MET A N     1 
ATOM   22288 C  CA    . MET A 1 4348 ? 141.833 179.477 166.596 1.00 105.79 ? 4348 MET A CA    1 
ATOM   22289 C  C     . MET A 1 4348 ? 143.076 180.163 167.146 1.00 102.56 ? 4348 MET A C     1 
ATOM   22290 O  O     . MET A 1 4348 ? 143.059 180.714 168.251 1.00 100.30 ? 4348 MET A O     1 
ATOM   22291 C  CB    . MET A 1 4348 ? 142.100 177.992 166.346 1.00 110.02 ? 4348 MET A CB    1 
ATOM   22292 C  CG    . MET A 1 4348 ? 142.448 177.221 167.606 1.00 109.36 ? 4348 MET A CG    1 
ATOM   22293 S  SD    . MET A 1 4348 ? 141.094 177.134 168.786 1.00 121.73 ? 4348 MET A SD    1 
ATOM   22294 C  CE    . MET A 1 4348 ? 142.009 176.865 170.301 1.00 112.50 ? 4348 MET A CE    1 
ATOM   22295 N  N     . LEU A 1 4349 ? 144.169 180.143 166.381 1.00 104.18 ? 4349 LEU A N     1 
ATOM   22296 C  CA    . LEU A 1 4349 ? 145.424 180.703 166.874 1.00 104.98 ? 4349 LEU A CA    1 
ATOM   22297 C  C     . LEU A 1 4349 ? 145.347 182.216 167.036 1.00 99.71  ? 4349 LEU A C     1 
ATOM   22298 O  O     . LEU A 1 4349 ? 146.045 182.781 167.885 1.00 90.14  ? 4349 LEU A O     1 
ATOM   22299 C  CB    . LEU A 1 4349 ? 146.574 180.322 165.940 1.00 99.17  ? 4349 LEU A CB    1 
ATOM   22300 C  CG    . LEU A 1 4349 ? 147.299 178.993 166.190 1.00 105.46 ? 4349 LEU A CG    1 
ATOM   22301 C  CD1   . LEU A 1 4349 ? 148.031 179.030 167.523 1.00 104.14 ? 4349 LEU A CD1   1 
ATOM   22302 C  CD2   . LEU A 1 4349 ? 146.354 177.802 166.133 1.00 104.18 ? 4349 LEU A CD2   1 
ATOM   22303 N  N     . GLU A 1 4350 ? 144.518 182.887 166.233 1.00 96.07  ? 4350 GLU A N     1 
ATOM   22304 C  CA    . GLU A 1 4350 ? 144.380 184.334 166.362 1.00 91.18  ? 4350 GLU A CA    1 
ATOM   22305 C  C     . GLU A 1 4350 ? 143.771 184.714 167.706 1.00 97.70  ? 4350 GLU A C     1 
ATOM   22306 O  O     . GLU A 1 4350 ? 144.201 185.687 168.335 1.00 88.16  ? 4350 GLU A O     1 
ATOM   22307 C  CB    . GLU A 1 4350 ? 143.536 184.884 165.212 1.00 86.96  ? 4350 GLU A CB    1 
ATOM   22308 C  CG    . GLU A 1 4350 ? 143.594 186.395 165.064 1.00 81.34  ? 4350 GLU A CG    1 
ATOM   22309 C  CD    . GLU A 1 4350 ? 142.487 187.107 165.817 1.00 92.31  ? 4350 GLU A CD    1 
ATOM   22310 O  OE1   . GLU A 1 4350 ? 141.593 186.422 166.356 1.00 100.55 ? 4350 GLU A OE1   1 
ATOM   22311 O  OE2   . GLU A 1 4350 ? 142.515 188.355 165.874 1.00 81.93  ? 4350 GLU A OE2   1 
ATOM   22312 N  N     . ASP A 1 4351 ? 142.770 183.961 168.160 1.00 105.18 ? 4351 ASP A N     1 
ATOM   22313 C  CA    . ASP A 1 4351 ? 142.115 184.216 169.442 1.00 107.54 ? 4351 ASP A CA    1 
ATOM   22314 C  C     . ASP A 1 4351 ? 141.853 182.879 170.119 1.00 108.08 ? 4351 ASP A C     1 
ATOM   22315 O  O     . ASP A 1 4351 ? 141.030 182.091 169.643 1.00 105.61 ? 4351 ASP A O     1 
ATOM   22316 C  CB    . ASP A 1 4351 ? 140.815 184.998 169.255 1.00 102.76 ? 4351 ASP A CB    1 
ATOM   22317 C  CG    . ASP A 1 4351 ? 140.251 185.518 170.565 1.00 103.52 ? 4351 ASP A CG    1 
ATOM   22318 O  OD1   . ASP A 1 4351 ? 140.885 185.302 171.619 1.00 100.49 ? 4351 ASP A OD1   1 
ATOM   22319 O  OD2   . ASP A 1 4351 ? 139.172 186.146 170.540 1.00 108.28 ? 4351 ASP A OD2   1 
ATOM   22320 N  N     . GLU A 1 4352 ? 142.544 182.628 171.227 1.00 111.20 ? 4352 GLU A N     1 
ATOM   22321 C  CA    . GLU A 1 4352 ? 142.379 181.409 172.008 1.00 114.39 ? 4352 GLU A CA    1 
ATOM   22322 C  C     . GLU A 1 4352 ? 141.670 181.742 173.312 1.00 116.01 ? 4352 GLU A C     1 
ATOM   22323 O  O     . GLU A 1 4352 ? 142.080 182.660 174.030 1.00 115.19 ? 4352 GLU A O     1 
ATOM   22324 C  CB    . GLU A 1 4352 ? 143.729 180.749 172.297 1.00 115.79 ? 4352 GLU A CB    1 
ATOM   22325 C  CG    . GLU A 1 4352 ? 144.489 180.312 171.059 1.00 119.64 ? 4352 GLU A CG    1 
ATOM   22326 C  CD    . GLU A 1 4352 ? 145.797 179.626 171.392 1.00 123.67 ? 4352 GLU A CD    1 
ATOM   22327 O  OE1   . GLU A 1 4352 ? 146.118 179.506 172.592 1.00 132.27 ? 4352 GLU A OE1   1 
ATOM   22328 O  OE2   . GLU A 1 4352 ? 146.503 179.205 170.452 1.00 111.41 ? 4352 GLU A OE2   1 
ATOM   22329 N  N     . ASP A 1 4353 ? 140.614 180.995 173.615 1.00 118.99 ? 4353 ASP A N     1 
ATOM   22330 C  CA    . ASP A 1 4353 ? 139.849 181.216 174.835 1.00 118.67 ? 4353 ASP A CA    1 
ATOM   22331 C  C     . ASP A 1 4353 ? 139.503 179.888 175.501 1.00 114.43 ? 4353 ASP A C     1 
ATOM   22332 O  O     . ASP A 1 4353 ? 139.736 179.702 176.695 1.00 109.47 ? 4353 ASP A O     1 
ATOM   22333 C  CB    . ASP A 1 4353 ? 138.575 182.009 174.532 1.00 111.44 ? 4353 ASP A CB    1 
ATOM   22334 C  CG    . ASP A 1 4353 ? 137.936 182.589 175.779 1.00 116.79 ? 4353 ASP A CG    1 
ATOM   22335 O  OD1   . ASP A 1 4353 ? 137.492 181.808 176.646 1.00 116.97 ? 4353 ASP A OD1   1 
ATOM   22336 O  OD2   . ASP A 1 4353 ? 137.879 183.832 175.893 1.00 115.04 ? 4353 ASP A OD2   1 
ATOM   22337 N  N     . ALA A 1 4375 ? 134.412 178.333 173.212 1.00 87.80  ? 4375 ALA A N     1 
ATOM   22338 C  CA    . ALA A 1 4375 ? 133.549 178.777 172.125 1.00 87.21  ? 4375 ALA A CA    1 
ATOM   22339 C  C     . ALA A 1 4375 ? 133.820 177.978 170.857 1.00 85.54  ? 4375 ALA A C     1 
ATOM   22340 O  O     . ALA A 1 4375 ? 132.900 177.640 170.115 1.00 86.25  ? 4375 ALA A O     1 
ATOM   22341 C  CB    . ALA A 1 4375 ? 133.740 180.261 171.867 1.00 85.98  ? 4375 ALA A CB    1 
ATOM   22342 N  N     . TRP A 1 4376 ? 135.097 177.684 170.611 1.00 87.57  ? 4376 TRP A N     1 
ATOM   22343 C  CA    . TRP A 1 4376 ? 135.457 176.898 169.436 1.00 89.85  ? 4376 TRP A CA    1 
ATOM   22344 C  C     . TRP A 1 4376 ? 135.024 175.446 169.594 1.00 88.34  ? 4376 TRP A C     1 
ATOM   22345 O  O     . TRP A 1 4376 ? 134.638 174.797 168.615 1.00 87.07  ? 4376 TRP A O     1 
ATOM   22346 C  CB    . TRP A 1 4376 ? 136.963 177.017 169.179 1.00 88.51  ? 4376 TRP A CB    1 
ATOM   22347 C  CG    . TRP A 1 4376 ? 137.844 176.174 170.063 1.00 89.42  ? 4376 TRP A CG    1 
ATOM   22348 C  CD1   . TRP A 1 4376 ? 138.622 176.616 171.093 1.00 90.96  ? 4376 TRP A CD1   1 
ATOM   22349 C  CD2   . TRP A 1 4376 ? 138.108 174.769 169.940 1.00 94.56  ? 4376 TRP A CD2   1 
ATOM   22350 N  NE1   . TRP A 1 4376 ? 139.310 175.568 171.652 1.00 93.87  ? 4376 TRP A NE1   1 
ATOM   22351 C  CE2   . TRP A 1 4376 ? 139.017 174.425 170.958 1.00 94.15  ? 4376 TRP A CE2   1 
ATOM   22352 C  CE3   . TRP A 1 4376 ? 137.647 173.766 169.082 1.00 94.60  ? 4376 TRP A CE3   1 
ATOM   22353 C  CZ2   . TRP A 1 4376 ? 139.474 173.123 171.141 1.00 91.76  ? 4376 TRP A CZ2   1 
ATOM   22354 C  CZ3   . TRP A 1 4376 ? 138.097 172.476 169.270 1.00 94.60  ? 4376 TRP A CZ3   1 
ATOM   22355 C  CH2   . TRP A 1 4376 ? 139.004 172.166 170.288 1.00 91.12  ? 4376 TRP A CH2   1 
ATOM   22356 N  N     . MET A 1 4377 ? 135.078 174.922 170.821 1.00 92.43  ? 4377 MET A N     1 
ATOM   22357 C  CA    . MET A 1 4377 ? 134.707 173.530 171.056 1.00 88.08  ? 4377 MET A CA    1 
ATOM   22358 C  C     . MET A 1 4377 ? 133.229 173.297 170.770 1.00 88.77  ? 4377 MET A C     1 
ATOM   22359 O  O     . MET A 1 4377 ? 132.861 172.321 170.108 1.00 92.77  ? 4377 MET A O     1 
ATOM   22360 C  CB    . MET A 1 4377 ? 135.043 173.135 172.493 1.00 89.91  ? 4377 MET A CB    1 
ATOM   22361 C  CG    . MET A 1 4377 ? 135.162 171.640 172.716 1.00 91.18  ? 4377 MET A CG    1 
ATOM   22362 S  SD    . MET A 1 4377 ? 136.183 171.247 174.146 1.00 97.14  ? 4377 MET A SD    1 
ATOM   22363 C  CE    . MET A 1 4377 ? 137.739 170.858 173.351 1.00 81.15  ? 4377 MET A CE    1 
ATOM   22364 N  N     . ARG A 1 4378 ? 132.365 174.185 171.267 1.00 87.75  ? 4378 ARG A N     1 
ATOM   22365 C  CA    . ARG A 1 4378 ? 130.930 174.020 171.052 1.00 91.48  ? 4378 ARG A CA    1 
ATOM   22366 C  C     . ARG A 1 4378 ? 130.573 174.153 169.576 1.00 93.05  ? 4378 ARG A C     1 
ATOM   22367 O  O     . ARG A 1 4378 ? 129.765 173.374 169.052 1.00 95.99  ? 4378 ARG A O     1 
ATOM   22368 C  CB    . ARG A 1 4378 ? 130.157 175.041 171.885 1.00 91.25  ? 4378 ARG A CB    1 
ATOM   22369 C  CG    . ARG A 1 4378 ? 130.073 174.714 173.371 1.00 97.07  ? 4378 ARG A CG    1 
ATOM   22370 C  CD    . ARG A 1 4378 ? 129.157 173.531 173.654 1.00 103.40 ? 4378 ARG A CD    1 
ATOM   22371 N  NE    . ARG A 1 4378 ? 129.867 172.258 173.607 1.00 99.90  ? 4378 ARG A NE    1 
ATOM   22372 C  CZ    . ARG A 1 4378 ? 130.631 171.788 174.584 1.00 95.84  ? 4378 ARG A CZ    1 
ATOM   22373 N  NH1   . ARG A 1 4378 ? 130.814 172.465 175.705 1.00 98.07  ? 4378 ARG A NH1   1 
ATOM   22374 N  NH2   . ARG A 1 4378 ? 131.228 170.610 174.431 1.00 89.29  ? 4378 ARG A NH2   1 
ATOM   22375 N  N     . THR A 1 4379 ? 131.165 175.135 168.892 1.00 90.43  ? 4379 THR A N     1 
ATOM   22376 C  CA    . THR A 1 4379 ? 130.896 175.316 167.469 1.00 85.26  ? 4379 THR A CA    1 
ATOM   22377 C  C     . THR A 1 4379 ? 131.366 174.113 166.661 1.00 90.07  ? 4379 THR A C     1 
ATOM   22378 O  O     . THR A 1 4379 ? 130.656 173.645 165.764 1.00 95.22  ? 4379 THR A O     1 
ATOM   22379 C  CB    . THR A 1 4379 ? 131.566 176.594 166.966 1.00 85.88  ? 4379 THR A CB    1 
ATOM   22380 O  OG1   . THR A 1 4379 ? 131.086 177.715 167.718 1.00 84.35  ? 4379 THR A OG1   1 
ATOM   22381 C  CG2   . THR A 1 4379 ? 131.258 176.813 165.493 1.00 85.69  ? 4379 THR A CG2   1 
ATOM   22382 N  N     . LEU A 1 4380 ? 132.559 173.597 166.966 1.00 90.90  ? 4380 LEU A N     1 
ATOM   22383 C  CA    . LEU A 1 4380 ? 133.052 172.420 166.257 1.00 86.09  ? 4380 LEU A CA    1 
ATOM   22384 C  C     . LEU A 1 4380 ? 132.188 171.200 166.545 1.00 83.03  ? 4380 LEU A C     1 
ATOM   22385 O  O     . LEU A 1 4380 ? 131.940 170.386 165.650 1.00 87.53  ? 4380 LEU A O     1 
ATOM   22386 C  CB    . LEU A 1 4380 ? 134.510 172.151 166.626 1.00 87.42  ? 4380 LEU A CB    1 
ATOM   22387 C  CG    . LEU A 1 4380 ? 135.177 170.976 165.906 1.00 84.33  ? 4380 LEU A CG    1 
ATOM   22388 C  CD1   . LEU A 1 4380 ? 135.229 171.222 164.409 1.00 85.50  ? 4380 LEU A CD1   1 
ATOM   22389 C  CD2   . LEU A 1 4380 ? 136.571 170.741 166.451 1.00 84.06  ? 4380 LEU A CD2   1 
ATOM   22390 N  N     . HIS A 1 4381 ? 131.723 171.052 167.788 1.00 81.03  ? 4381 HIS A N     1 
ATOM   22391 C  CA    . HIS A 1 4381 ? 130.836 169.944 168.125 1.00 88.04  ? 4381 HIS A CA    1 
ATOM   22392 C  C     . HIS A 1 4381 ? 129.545 170.018 167.321 1.00 93.86  ? 4381 HIS A C     1 
ATOM   22393 O  O     . HIS A 1 4381 ? 129.095 169.016 166.753 1.00 97.97  ? 4381 HIS A O     1 
ATOM   22394 C  CB    . HIS A 1 4381 ? 130.547 169.956 169.627 1.00 92.72  ? 4381 HIS A CB    1 
ATOM   22395 C  CG    . HIS A 1 4381 ? 129.694 168.818 170.096 1.00 99.98  ? 4381 HIS A CG    1 
ATOM   22396 N  ND1   . HIS A 1 4381 ? 128.358 168.704 169.777 1.00 104.00 ? 4381 HIS A ND1   1 
ATOM   22397 C  CD2   . HIS A 1 4381 ? 129.988 167.744 170.866 1.00 103.44 ? 4381 HIS A CD2   1 
ATOM   22398 C  CE1   . HIS A 1 4381 ? 127.867 167.609 170.328 1.00 105.82 ? 4381 HIS A CE1   1 
ATOM   22399 N  NE2   . HIS A 1 4381 ? 128.835 167.008 170.994 1.00 108.12 ? 4381 HIS A NE2   1 
ATOM   22400 N  N     . THR A 1 4382 ? 128.940 171.206 167.254 1.00 92.41  ? 4382 THR A N     1 
ATOM   22401 C  CA    . THR A 1 4382 ? 127.708 171.364 166.486 1.00 92.68  ? 4382 THR A CA    1 
ATOM   22402 C  C     . THR A 1 4382 ? 127.944 171.100 165.003 1.00 93.24  ? 4382 THR A C     1 
ATOM   22403 O  O     . THR A 1 4382 ? 127.140 170.424 164.348 1.00 96.37  ? 4382 THR A O     1 
ATOM   22404 C  CB    . THR A 1 4382 ? 127.134 172.764 166.694 1.00 95.28  ? 4382 THR A CB    1 
ATOM   22405 O  OG1   . THR A 1 4382 ? 126.985 173.017 168.097 1.00 94.35  ? 4382 THR A OG1   1 
ATOM   22406 C  CG2   . THR A 1 4382 ? 125.778 172.889 166.018 1.00 97.58  ? 4382 THR A CG2   1 
ATOM   22407 N  N     . THR A 1 4383 ? 129.047 171.620 164.460 1.00 92.30  ? 4383 THR A N     1 
ATOM   22408 C  CA    . THR A 1 4383 ? 129.347 171.424 163.046 1.00 90.86  ? 4383 THR A CA    1 
ATOM   22409 C  C     . THR A 1 4383 ? 129.563 169.951 162.723 1.00 90.74  ? 4383 THR A C     1 
ATOM   22410 O  O     . THR A 1 4383 ? 129.047 169.445 161.720 1.00 94.54  ? 4383 THR A O     1 
ATOM   22411 C  CB    . THR A 1 4383 ? 130.577 172.247 162.662 1.00 89.99  ? 4383 THR A CB    1 
ATOM   22412 O  OG1   . THR A 1 4383 ? 130.269 173.643 162.760 1.00 93.71  ? 4383 THR A OG1   1 
ATOM   22413 C  CG2   . THR A 1 4383 ? 131.010 171.934 161.248 1.00 87.73  ? 4383 THR A CG2   1 
ATOM   22414 N  N     . ALA A 1 4384 ? 130.313 169.241 163.569 1.00 87.00  ? 4384 ALA A N     1 
ATOM   22415 C  CA    . ALA A 1 4384 ? 130.567 167.827 163.324 1.00 82.51  ? 4384 ALA A CA    1 
ATOM   22416 C  C     . ALA A 1 4384 ? 129.302 166.998 163.497 1.00 86.74  ? 4384 ALA A C     1 
ATOM   22417 O  O     . ALA A 1 4384 ? 129.096 166.019 162.773 1.00 93.50  ? 4384 ALA A O     1 
ATOM   22418 C  CB    . ALA A 1 4384 ? 131.676 167.329 164.248 1.00 84.64  ? 4384 ALA A CB    1 
ATOM   22419 N  N     . SER A 1 4385 ? 128.441 167.369 164.449 1.00 89.93  ? 4385 SER A N     1 
ATOM   22420 C  CA    . SER A 1 4385 ? 127.164 166.676 164.594 1.00 94.43  ? 4385 SER A CA    1 
ATOM   22421 C  C     . SER A 1 4385 ? 126.297 166.862 163.355 1.00 96.30  ? 4385 SER A C     1 
ATOM   22422 O  O     . SER A 1 4385 ? 125.689 165.903 162.860 1.00 98.70  ? 4385 SER A O     1 
ATOM   22423 C  CB    . SER A 1 4385 ? 126.436 167.176 165.840 1.00 94.47  ? 4385 SER A CB    1 
ATOM   22424 O  OG    . SER A 1 4385 ? 127.252 167.047 166.990 1.00 95.65  ? 4385 SER A OG    1 
ATOM   22425 N  N     . ASN A 1 4386 ? 126.238 168.089 162.832 1.00 94.53  ? 4386 ASN A N     1 
ATOM   22426 C  CA    . ASN A 1 4386 ? 125.496 168.325 161.598 1.00 94.85  ? 4386 ASN A CA    1 
ATOM   22427 C  C     . ASN A 1 4386 ? 126.082 167.525 160.442 1.00 96.82  ? 4386 ASN A C     1 
ATOM   22428 O  O     . ASN A 1 4386 ? 125.340 166.924 159.659 1.00 99.90  ? 4386 ASN A O     1 
ATOM   22429 C  CB    . ASN A 1 4386 ? 125.484 169.817 161.268 1.00 99.91  ? 4386 ASN A CB    1 
ATOM   22430 C  CG    . ASN A 1 4386 ? 124.836 170.649 162.353 1.00 103.55 ? 4386 ASN A CG    1 
ATOM   22431 O  OD1   . ASN A 1 4386 ? 124.355 170.118 163.354 1.00 105.18 ? 4386 ASN A OD1   1 
ATOM   22432 N  ND2   . ASN A 1 4386 ? 124.817 171.963 162.161 1.00 99.24  ? 4386 ASN A ND2   1 
ATOM   22433 N  N     . TRP A 1 4387 ? 127.412 167.494 160.330 1.00 93.31  ? 4387 TRP A N     1 
ATOM   22434 C  CA    . TRP A 1 4387 ? 128.054 166.736 159.259 1.00 89.70  ? 4387 TRP A CA    1 
ATOM   22435 C  C     . TRP A 1 4387 ? 127.737 165.250 159.366 1.00 91.20  ? 4387 TRP A C     1 
ATOM   22436 O  O     . TRP A 1 4387 ? 127.479 164.588 158.355 1.00 93.16  ? 4387 TRP A O     1 
ATOM   22437 C  CB    . TRP A 1 4387 ? 129.562 166.966 159.293 1.00 85.83  ? 4387 TRP A CB    1 
ATOM   22438 C  CG    . TRP A 1 4387 ? 129.968 168.287 158.741 1.00 87.15  ? 4387 TRP A CG    1 
ATOM   22439 C  CD1   . TRP A 1 4387 ? 129.191 169.150 158.030 1.00 88.61  ? 4387 TRP A CD1   1 
ATOM   22440 C  CD2   . TRP A 1 4387 ? 131.243 168.920 158.886 1.00 90.03  ? 4387 TRP A CD2   1 
ATOM   22441 N  NE1   . TRP A 1 4387 ? 129.908 170.274 157.704 1.00 95.52  ? 4387 TRP A NE1   1 
ATOM   22442 C  CE2   . TRP A 1 4387 ? 131.171 170.158 158.220 1.00 94.19  ? 4387 TRP A CE2   1 
ATOM   22443 C  CE3   . TRP A 1 4387 ? 132.440 168.556 159.508 1.00 85.01  ? 4387 TRP A CE3   1 
ATOM   22444 C  CZ2   . TRP A 1 4387 ? 132.251 171.033 158.156 1.00 91.45  ? 4387 TRP A CZ2   1 
ATOM   22445 C  CZ3   . TRP A 1 4387 ? 133.509 169.427 159.445 1.00 84.03  ? 4387 TRP A CZ3   1 
ATOM   22446 C  CH2   . TRP A 1 4387 ? 133.405 170.654 158.780 1.00 86.24  ? 4387 TRP A CH2   1 
ATOM   22447 N  N     . LEU A 1 4388 ? 127.756 164.707 160.585 1.00 94.13  ? 4388 LEU A N     1 
ATOM   22448 C  CA    . LEU A 1 4388 ? 127.367 163.316 160.784 1.00 92.69  ? 4388 LEU A CA    1 
ATOM   22449 C  C     . LEU A 1 4388 ? 125.916 163.093 160.382 1.00 95.89  ? 4388 LEU A C     1 
ATOM   22450 O  O     . LEU A 1 4388 ? 125.569 162.041 159.833 1.00 95.10  ? 4388 LEU A O     1 
ATOM   22451 C  CB    . LEU A 1 4388 ? 127.587 162.910 162.242 1.00 92.57  ? 4388 LEU A CB    1 
ATOM   22452 C  CG    . LEU A 1 4388 ? 129.025 162.643 162.685 1.00 89.61  ? 4388 LEU A CG    1 
ATOM   22453 C  CD1   . LEU A 1 4388 ? 129.044 162.008 164.062 1.00 80.58  ? 4388 LEU A CD1   1 
ATOM   22454 C  CD2   . LEU A 1 4388 ? 129.728 161.752 161.679 1.00 93.51  ? 4388 LEU A CD2   1 
ATOM   22455 N  N     . HIS A 1 4389 ? 125.052 164.072 160.659 1.00 97.68  ? 4389 HIS A N     1 
ATOM   22456 C  CA    . HIS A 1 4389 ? 123.652 163.953 160.265 1.00 101.77 ? 4389 HIS A CA    1 
ATOM   22457 C  C     . HIS A 1 4389 ? 123.503 163.908 158.747 1.00 105.23 ? 4389 HIS A C     1 
ATOM   22458 O  O     . HIS A 1 4389 ? 122.769 163.070 158.210 1.00 106.87 ? 4389 HIS A O     1 
ATOM   22459 C  CB    . HIS A 1 4389 ? 122.842 165.108 160.851 1.00 103.74 ? 4389 HIS A CB    1 
ATOM   22460 C  CG    . HIS A 1 4389 ? 121.372 165.007 160.588 1.00 109.75 ? 4389 HIS A CG    1 
ATOM   22461 N  ND1   . HIS A 1 4389 ? 120.644 163.871 160.870 1.00 110.03 ? 4389 HIS A ND1   1 
ATOM   22462 C  CD2   . HIS A 1 4389 ? 120.495 165.898 160.069 1.00 112.29 ? 4389 HIS A CD2   1 
ATOM   22463 C  CE1   . HIS A 1 4389 ? 119.381 164.067 160.535 1.00 111.30 ? 4389 HIS A CE1   1 
ATOM   22464 N  NE2   . HIS A 1 4389 ? 119.264 165.289 160.047 1.00 115.61 ? 4389 HIS A NE2   1 
ATOM   22465 N  N     . LEU A 1 4390 ? 124.191 164.806 158.036 1.00 104.01 ? 4390 LEU A N     1 
ATOM   22466 C  CA    . LEU A 1 4390 ? 124.056 164.856 156.581 1.00 100.66 ? 4390 LEU A CA    1 
ATOM   22467 C  C     . LEU A 1 4390 ? 124.690 163.638 155.922 1.00 99.57  ? 4390 LEU A C     1 
ATOM   22468 O  O     . LEU A 1 4390 ? 124.086 163.006 155.049 1.00 98.57  ? 4390 LEU A O     1 
ATOM   22469 C  CB    . LEU A 1 4390 ? 124.675 166.140 156.029 1.00 97.55  ? 4390 LEU A CB    1 
ATOM   22470 C  CG    . LEU A 1 4390 ? 124.441 167.427 156.817 1.00 103.36 ? 4390 LEU A CG    1 
ATOM   22471 C  CD1   . LEU A 1 4390 ? 125.305 168.563 156.282 1.00 105.54 ? 4390 LEU A CD1   1 
ATOM   22472 C  CD2   . LEU A 1 4390 ? 122.967 167.797 156.832 1.00 105.47 ? 4390 LEU A CD2   1 
ATOM   22473 N  N     . ILE A 1 4391 ? 125.912 163.300 156.323 1.00 100.42 ? 4391 ILE A N     1 
ATOM   22474 C  CA    . ILE A 1 4391 ? 126.638 162.201 155.679 1.00 97.34  ? 4391 ILE A CA    1 
ATOM   22475 C  C     . ILE A 1 4391 ? 125.934 160.883 155.977 1.00 99.71  ? 4391 ILE A C     1 
ATOM   22476 O  O     . ILE A 1 4391 ? 125.691 160.564 157.157 1.00 105.21 ? 4391 ILE A O     1 
ATOM   22477 C  CB    . ILE A 1 4391 ? 128.097 162.167 156.163 1.00 95.32  ? 4391 ILE A CB    1 
ATOM   22478 C  CG1   . ILE A 1 4391 ? 128.835 163.440 155.743 1.00 99.00  ? 4391 ILE A CG1   1 
ATOM   22479 C  CG2   . ILE A 1 4391 ? 128.803 160.938 155.642 1.00 87.66  ? 4391 ILE A CG2   1 
ATOM   22480 C  CD1   . ILE A 1 4391 ? 128.899 163.650 154.250 1.00 98.81  ? 4391 ILE A CD1   1 
ATOM   22481 N  N     . PRO A 1 4392 ? 125.570 160.097 154.964 1.00 97.07  ? 4392 PRO A N     1 
ATOM   22482 C  CA    . PRO A 1 4392 ? 124.928 158.803 155.225 1.00 98.20  ? 4392 PRO A CA    1 
ATOM   22483 C  C     . PRO A 1 4392 ? 125.817 157.892 156.059 1.00 99.98  ? 4392 PRO A C     1 
ATOM   22484 O  O     . PRO A 1 4392 ? 127.042 157.899 155.931 1.00 103.52 ? 4392 PRO A O     1 
ATOM   22485 C  CB    . PRO A 1 4392 ? 124.698 158.224 153.826 1.00 99.58  ? 4392 PRO A CB    1 
ATOM   22486 C  CG    . PRO A 1 4392 ? 125.063 159.291 152.848 1.00 100.79 ? 4392 PRO A CG    1 
ATOM   22487 C  CD    . PRO A 1 4392 ? 125.391 160.543 153.575 1.00 100.65 ? 4392 PRO A CD    1 
ATOM   22488 N  N     . GLN A 1 4393 ? 125.176 157.101 156.921 1.00 98.90  ? 4393 GLN A N     1 
ATOM   22489 C  CA    . GLN A 1 4393 ? 125.914 156.279 157.875 1.00 99.22  ? 4393 GLN A CA    1 
ATOM   22490 C  C     . GLN A 1 4393 ? 126.709 155.183 157.174 1.00 101.46 ? 4393 GLN A C     1 
ATOM   22491 O  O     . GLN A 1 4393 ? 127.885 154.961 157.487 1.00 91.81  ? 4393 GLN A O     1 
ATOM   22492 C  CB    . GLN A 1 4393 ? 124.944 155.677 158.892 1.00 101.30 ? 4393 GLN A CB    1 
ATOM   22493 C  CG    . GLN A 1 4393 ? 123.837 156.629 159.317 1.00 103.27 ? 4393 GLN A CG    1 
ATOM   22494 C  CD    . GLN A 1 4393 ? 123.254 156.281 160.671 1.00 110.44 ? 4393 GLN A CD    1 
ATOM   22495 O  OE1   . GLN A 1 4393 ? 123.761 156.712 161.707 1.00 108.71 ? 4393 GLN A OE1   1 
ATOM   22496 N  NE2   . GLN A 1 4393 ? 122.181 155.499 160.670 1.00 109.67 ? 4393 GLN A NE2   1 
ATOM   22497 N  N     . THR A 1 4394 ? 126.087 154.485 156.225 1.00 111.24 ? 4394 THR A N     1 
ATOM   22498 C  CA    . THR A 1 4394 ? 126.713 153.356 155.552 1.00 113.87 ? 4394 THR A CA    1 
ATOM   22499 C  C     . THR A 1 4394 ? 126.465 153.427 154.052 1.00 111.76 ? 4394 THR A C     1 
ATOM   22500 O  O     . THR A 1 4394 ? 125.448 153.957 153.597 1.00 107.83 ? 4394 THR A O     1 
ATOM   22501 C  CB    . THR A 1 4394 ? 126.186 152.014 156.084 1.00 111.04 ? 4394 THR A CB    1 
ATOM   22502 O  OG1   . THR A 1 4394 ? 124.754 152.002 156.016 1.00 104.37 ? 4394 THR A OG1   1 
ATOM   22503 C  CG2   . THR A 1 4394 ? 126.624 151.794 157.525 1.00 109.41 ? 4394 THR A CG2   1 
ATOM   22504 N  N     . LEU A 1 4395 ? 127.409 152.878 153.290 1.00 109.08 ? 4395 LEU A N     1 
ATOM   22505 C  CA    . LEU A 1 4395 ? 127.279 152.725 151.847 1.00 111.36 ? 4395 LEU A CA    1 
ATOM   22506 C  C     . LEU A 1 4395 ? 127.304 151.242 151.509 1.00 112.46 ? 4395 LEU A C     1 
ATOM   22507 O  O     . LEU A 1 4395 ? 128.220 150.523 151.921 1.00 111.62 ? 4395 LEU A O     1 
ATOM   22508 C  CB    . LEU A 1 4395 ? 128.399 153.460 151.104 1.00 109.80 ? 4395 LEU A CB    1 
ATOM   22509 C  CG    . LEU A 1 4395 ? 128.256 153.536 149.581 1.00 108.50 ? 4395 LEU A CG    1 
ATOM   22510 C  CD1   . LEU A 1 4395 ? 127.140 154.487 149.198 1.00 103.44 ? 4395 LEU A CD1   1 
ATOM   22511 C  CD2   . LEU A 1 4395 ? 129.557 153.958 148.926 1.00 103.59 ? 4395 LEU A CD2   1 
ATOM   22512 N  N     . SER A 1 4396 ? 126.301 150.787 150.763 1.00 110.18 ? 4396 SER A N     1 
ATOM   22513 C  CA    . SER A 1 4396 ? 126.191 149.377 150.422 1.00 106.56 ? 4396 SER A CA    1 
ATOM   22514 C  C     . SER A 1 4396 ? 127.062 149.042 149.220 1.00 110.32 ? 4396 SER A C     1 
ATOM   22515 O  O     . SER A 1 4396 ? 127.104 149.786 148.236 1.00 109.25 ? 4396 SER A O     1 
ATOM   22516 C  CB    . SER A 1 4396 ? 124.737 149.010 150.130 1.00 110.44 ? 4396 SER A CB    1 
ATOM   22517 O  OG    . SER A 1 4396 ? 124.248 149.719 149.006 1.00 110.49 ? 4396 SER A OG    1 
ATOM   22518 N  N     . HIS A 1 4397 ? 127.760 147.913 149.306 1.00 110.85 ? 4397 HIS A N     1 
ATOM   22519 C  CA    . HIS A 1 4397 ? 128.595 147.447 148.210 1.00 107.17 ? 4397 HIS A CA    1 
ATOM   22520 C  C     . HIS A 1 4397 ? 127.760 146.700 147.178 1.00 108.67 ? 4397 HIS A C     1 
ATOM   22521 O  O     . HIS A 1 4397 ? 126.765 146.047 147.503 1.00 107.28 ? 4397 HIS A O     1 
ATOM   22522 C  CB    . HIS A 1 4397 ? 129.711 146.541 148.729 1.00 99.71  ? 4397 HIS A CB    1 
ATOM   22523 C  CG    . HIS A 1 4397 ? 130.923 147.283 149.197 1.00 105.99 ? 4397 HIS A CG    1 
ATOM   22524 N  ND1   . HIS A 1 4397 ? 132.140 146.668 149.399 1.00 106.94 ? 4397 HIS A ND1   1 
ATOM   22525 C  CD2   . HIS A 1 4397 ? 131.107 148.589 149.501 1.00 106.66 ? 4397 HIS A CD2   1 
ATOM   22526 C  CE1   . HIS A 1 4397 ? 133.021 147.563 149.808 1.00 104.97 ? 4397 HIS A CE1   1 
ATOM   22527 N  NE2   . HIS A 1 4397 ? 132.420 148.737 149.878 1.00 105.64 ? 4397 HIS A NE2   1 
ATOM   22528 N  N     . LEU A 1 4398 ? 128.174 146.809 145.919 1.00 110.54 ? 4398 LEU A N     1 
ATOM   22529 C  CA    . LEU A 1 4398 ? 127.475 146.127 144.841 1.00 108.65 ? 4398 LEU A CA    1 
ATOM   22530 C  C     . LEU A 1 4398 ? 127.746 144.630 144.896 1.00 109.68 ? 4398 LEU A C     1 
ATOM   22531 O  O     . LEU A 1 4398 ? 128.862 144.194 145.191 1.00 110.71 ? 4398 LEU A O     1 
ATOM   22532 C  CB    . LEU A 1 4398 ? 127.903 146.691 143.488 1.00 108.45 ? 4398 LEU A CB    1 
ATOM   22533 C  CG    . LEU A 1 4398 ? 127.599 148.172 143.268 1.00 100.29 ? 4398 LEU A CG    1 
ATOM   22534 C  CD1   . LEU A 1 4398 ? 127.924 148.592 141.848 1.00 101.58 ? 4398 LEU A CD1   1 
ATOM   22535 C  CD2   . LEU A 1 4398 ? 126.150 148.440 143.581 1.00 106.53 ? 4398 LEU A CD2   1 
ATOM   22536 N  N     . LYS A 1 4399 ? 126.714 143.841 144.610 1.00 109.59 ? 4399 LYS A N     1 
ATOM   22537 C  CA    . LYS A 1 4399 ? 126.808 142.383 144.654 1.00 111.71 ? 4399 LYS A CA    1 
ATOM   22538 C  C     . LYS A 1 4399 ? 127.294 141.892 143.296 1.00 112.29 ? 4399 LYS A C     1 
ATOM   22539 O  O     . LYS A 1 4399 ? 126.541 141.879 142.320 1.00 113.65 ? 4399 LYS A O     1 
ATOM   22540 C  CB    . LYS A 1 4399 ? 125.464 141.770 145.029 1.00 115.51 ? 4399 LYS A CB    1 
ATOM   22541 C  CG    . LYS A 1 4399 ? 124.906 142.278 146.348 1.00 120.72 ? 4399 LYS A CG    1 
ATOM   22542 C  CD    . LYS A 1 4399 ? 123.526 141.709 146.626 1.00 126.76 ? 4399 LYS A CD    1 
ATOM   22543 C  CE    . LYS A 1 4399 ? 122.949 142.278 147.912 1.00 127.48 ? 4399 LYS A CE    1 
ATOM   22544 N  NZ    . LYS A 1 4399 ? 121.585 141.752 148.193 1.00 134.78 ? 4399 LYS A NZ    1 
ATOM   22545 N  N     . ARG A 1 4400 ? 128.559 141.485 143.236 1.00 110.82 ? 4400 ARG A N     1 
ATOM   22546 C  CA    . ARG A 1 4400 ? 129.139 140.976 142.001 1.00 112.74 ? 4400 ARG A CA    1 
ATOM   22547 C  C     . ARG A 1 4400 ? 128.635 139.566 141.724 1.00 113.05 ? 4400 ARG A C     1 
ATOM   22548 O  O     . ARG A 1 4400 ? 128.695 138.693 142.596 1.00 116.74 ? 4400 ARG A O     1 
ATOM   22549 C  CB    . ARG A 1 4400 ? 130.665 140.986 142.089 1.00 108.89 ? 4400 ARG A CB    1 
ATOM   22550 C  CG    . ARG A 1 4400 ? 131.352 140.217 140.975 1.00 111.79 ? 4400 ARG A CG    1 
ATOM   22551 C  CD    . ARG A 1 4400 ? 132.864 140.290 141.102 1.00 115.76 ? 4400 ARG A CD    1 
ATOM   22552 N  NE    . ARG A 1 4400 ? 133.531 139.443 140.120 1.00 121.01 ? 4400 ARG A NE    1 
ATOM   22553 C  CZ    . ARG A 1 4400 ? 134.846 139.350 139.980 1.00 121.53 ? 4400 ARG A CZ    1 
ATOM   22554 N  NH1   . ARG A 1 4400 ? 135.673 140.051 140.738 1.00 121.98 ? 4400 ARG A NH1   1 
ATOM   22555 N  NH2   . ARG A 1 4400 ? 135.344 138.535 139.055 1.00 117.84 ? 4400 ARG A NH2   1 
ATOM   22556 N  N     . THR A 1 4401 ? 128.137 139.345 140.508 1.00 109.63 ? 4401 THR A N     1 
ATOM   22557 C  CA    . THR A 1 4401 ? 127.650 138.030 140.108 1.00 110.43 ? 4401 THR A CA    1 
ATOM   22558 C  C     . THR A 1 4401 ? 128.326 137.578 138.821 1.00 112.57 ? 4401 THR A C     1 
ATOM   22559 O  O     . THR A 1 4401 ? 129.277 138.214 138.356 1.00 113.65 ? 4401 THR A O     1 
ATOM   22560 C  CB    . THR A 1 4401 ? 126.129 138.037 139.927 1.00 108.58 ? 4401 THR A CB    1 
ATOM   22561 O  OG1   . THR A 1 4401 ? 125.790 138.753 138.733 1.00 108.98 ? 4401 THR A OG1   1 
ATOM   22562 C  CG2   . THR A 1 4401 ? 125.443 138.687 141.122 1.00 108.10 ? 4401 THR A CG2   1 
ATOM   22563 N  N     . VAL A 1 4402 ? 127.848 136.473 138.246 1.00 114.35 ? 4402 VAL A N     1 
ATOM   22564 C  CA    . VAL A 1 4402 ? 128.439 135.961 137.014 1.00 115.40 ? 4402 VAL A CA    1 
ATOM   22565 C  C     . VAL A 1 4402 ? 128.157 136.902 135.849 1.00 115.57 ? 4402 VAL A C     1 
ATOM   22566 O  O     . VAL A 1 4402 ? 129.056 137.230 135.066 1.00 115.43 ? 4402 VAL A O     1 
ATOM   22567 C  CB    . VAL A 1 4402 ? 127.926 134.538 136.731 1.00 115.06 ? 4402 VAL A CB    1 
ATOM   22568 C  CG1   . VAL A 1 4402 ? 128.446 134.039 135.391 1.00 110.24 ? 4402 VAL A CG1   1 
ATOM   22569 C  CG2   . VAL A 1 4402 ? 128.332 133.595 137.853 1.00 112.04 ? 4402 VAL A CG2   1 
ATOM   22570 N  N     . GLU A 1 4403 ? 126.909 137.350 135.714 1.00 114.07 ? 4403 GLU A N     1 
ATOM   22571 C  CA    . GLU A 1 4403 ? 126.527 138.223 134.611 1.00 111.42 ? 4403 GLU A CA    1 
ATOM   22572 C  C     . GLU A 1 4403 ? 126.930 139.675 134.830 1.00 108.64 ? 4403 GLU A C     1 
ATOM   22573 O  O     . GLU A 1 4403 ? 127.212 140.382 133.856 1.00 106.81 ? 4403 GLU A O     1 
ATOM   22574 C  CB    . GLU A 1 4403 ? 125.015 138.146 134.380 1.00 109.00 ? 4403 GLU A CB    1 
ATOM   22575 C  CG    . GLU A 1 4403 ? 124.550 136.857 133.721 1.00 112.00 ? 4403 GLU A CG    1 
ATOM   22576 C  CD    . GLU A 1 4403 ? 125.028 136.728 132.287 1.00 115.09 ? 4403 GLU A CD    1 
ATOM   22577 O  OE1   . GLU A 1 4403 ? 124.323 137.213 131.377 1.00 109.69 ? 4403 GLU A OE1   1 
ATOM   22578 O  OE2   . GLU A 1 4403 ? 126.107 136.138 132.069 1.00 116.21 ? 4403 GLU A OE2   1 
ATOM   22579 N  N     . ASN A 1 4404 ? 126.962 140.136 136.082 1.00 110.49 ? 4404 ASN A N     1 
ATOM   22580 C  CA    . ASN A 1 4404 ? 127.248 141.543 136.346 1.00 106.33 ? 4404 ASN A CA    1 
ATOM   22581 C  C     . ASN A 1 4404 ? 128.713 141.884 136.113 1.00 103.37 ? 4404 ASN A C     1 
ATOM   22582 O  O     . ASN A 1 4404 ? 129.030 143.025 135.760 1.00 104.49 ? 4404 ASN A O     1 
ATOM   22583 C  CB    . ASN A 1 4404 ? 126.844 141.903 137.776 1.00 108.47 ? 4404 ASN A CB    1 
ATOM   22584 C  CG    . ASN A 1 4404 ? 125.353 141.765 138.012 1.00 113.61 ? 4404 ASN A CG    1 
ATOM   22585 O  OD1   . ASN A 1 4404 ? 124.911 140.923 138.793 1.00 115.40 ? 4404 ASN A OD1   1 
ATOM   22586 N  ND2   . ASN A 1 4404 ? 124.568 142.595 137.337 1.00 111.60 ? 4404 ASN A ND2   1 
ATOM   22587 N  N     . ILE A 1 4405 ? 129.619 140.923 136.309 1.00 104.76 ? 4405 ILE A N     1 
ATOM   22588 C  CA    . ILE A 1 4405 ? 131.040 141.208 136.129 1.00 107.20 ? 4405 ILE A CA    1 
ATOM   22589 C  C     . ILE A 1 4405 ? 131.362 141.457 134.660 1.00 111.08 ? 4405 ILE A C     1 
ATOM   22590 O  O     . ILE A 1 4405 ? 132.312 142.181 134.340 1.00 108.31 ? 4405 ILE A O     1 
ATOM   22591 C  CB    . ILE A 1 4405 ? 131.895 140.071 136.721 1.00 107.78 ? 4405 ILE A CB    1 
ATOM   22592 C  CG1   . ILE A 1 4405 ? 133.363 140.492 136.804 1.00 111.08 ? 4405 ILE A CG1   1 
ATOM   22593 C  CG2   . ILE A 1 4405 ? 131.749 138.797 135.905 1.00 106.40 ? 4405 ILE A CG2   1 
ATOM   22594 C  CD1   . ILE A 1 4405 ? 133.590 141.754 137.608 1.00 108.29 ? 4405 ILE A CD1   1 
ATOM   22595 N  N     . LYS A 1 4406 ? 130.582 140.877 133.745 1.00 109.36 ? 4406 LYS A N     1 
ATOM   22596 C  CA    . LYS A 1 4406 ? 130.785 141.113 132.321 1.00 105.83 ? 4406 LYS A CA    1 
ATOM   22597 C  C     . LYS A 1 4406 ? 130.340 142.503 131.885 1.00 102.47 ? 4406 LYS A C     1 
ATOM   22598 O  O     . LYS A 1 4406 ? 130.596 142.885 130.738 1.00 96.61  ? 4406 LYS A O     1 
ATOM   22599 C  CB    . LYS A 1 4406 ? 130.045 140.054 131.505 1.00 102.14 ? 4406 LYS A CB    1 
ATOM   22600 C  CG    . LYS A 1 4406 ? 130.262 138.636 132.001 1.00 106.84 ? 4406 LYS A CG    1 
ATOM   22601 C  CD    . LYS A 1 4406 ? 129.472 137.633 131.177 1.00 110.83 ? 4406 LYS A CD    1 
ATOM   22602 C  CE    . LYS A 1 4406 ? 129.369 136.293 131.889 1.00 111.80 ? 4406 LYS A CE    1 
ATOM   22603 N  NZ    . LYS A 1 4406 ? 130.462 136.097 132.882 1.00 113.90 ? 4406 LYS A NZ    1 
ATOM   22604 N  N     . ASP A 1 4407 ? 129.682 143.257 132.761 1.00 103.64 ? 4407 ASP A N     1 
ATOM   22605 C  CA    . ASP A 1 4407 ? 129.218 144.597 132.432 1.00 95.32  ? 4407 ASP A CA    1 
ATOM   22606 C  C     . ASP A 1 4407 ? 130.307 145.608 132.762 1.00 93.16  ? 4407 ASP A C     1 
ATOM   22607 O  O     . ASP A 1 4407 ? 130.691 145.723 133.934 1.00 92.38  ? 4407 ASP A O     1 
ATOM   22608 C  CB    . ASP A 1 4407 ? 127.952 144.924 133.207 1.00 95.28  ? 4407 ASP A CB    1 
ATOM   22609 C  CG    . ASP A 1 4407 ? 127.190 146.090 132.617 1.00 98.61  ? 4407 ASP A CG    1 
ATOM   22610 O  OD1   . ASP A 1 4407 ? 127.746 147.204 132.572 1.00 91.95  ? 4407 ASP A OD1   1 
ATOM   22611 O  OD2   . ASP A 1 4407 ? 126.029 145.892 132.201 1.00 106.12 ? 4407 ASP A OD2   1 
ATOM   22612 N  N     . PRO A 1 4408 ? 130.843 146.339 131.778 1.00 88.24  ? 4408 PRO A N     1 
ATOM   22613 C  CA    . PRO A 1 4408 ? 131.855 147.361 132.103 1.00 84.91  ? 4408 PRO A CA    1 
ATOM   22614 C  C     . PRO A 1 4408 ? 131.327 148.446 133.023 1.00 88.65  ? 4408 PRO A C     1 
ATOM   22615 O  O     . PRO A 1 4408 ? 132.046 148.914 133.920 1.00 86.74  ? 4408 PRO A O     1 
ATOM   22616 C  CB    . PRO A 1 4408 ? 132.239 147.921 130.724 1.00 72.31  ? 4408 PRO A CB    1 
ATOM   22617 C  CG    . PRO A 1 4408 ? 131.726 146.918 129.729 1.00 75.50  ? 4408 PRO A CG    1 
ATOM   22618 C  CD    . PRO A 1 4408 ? 130.511 146.324 130.346 1.00 77.54  ? 4408 PRO A CD    1 
ATOM   22619 N  N     . LEU A 1 4409 ? 130.068 148.846 132.830 1.00 87.30  ? 4409 LEU A N     1 
ATOM   22620 C  CA    . LEU A 1 4409 ? 129.465 149.840 133.707 1.00 85.01  ? 4409 LEU A CA    1 
ATOM   22621 C  C     . LEU A 1 4409 ? 129.380 149.324 135.134 1.00 87.04  ? 4409 LEU A C     1 
ATOM   22622 O  O     . LEU A 1 4409 ? 129.643 150.068 136.085 1.00 88.60  ? 4409 LEU A O     1 
ATOM   22623 C  CB    . LEU A 1 4409 ? 128.080 150.229 133.189 1.00 86.51  ? 4409 LEU A CB    1 
ATOM   22624 C  CG    . LEU A 1 4409 ? 128.015 150.791 131.769 1.00 79.89  ? 4409 LEU A CG    1 
ATOM   22625 C  CD1   . LEU A 1 4409 ? 126.576 151.024 131.349 1.00 78.66  ? 4409 LEU A CD1   1 
ATOM   22626 C  CD2   . LEU A 1 4409 ? 128.809 152.079 131.682 1.00 76.08  ? 4409 LEU A CD2   1 
ATOM   22627 N  N     . PHE A 1 4410 ? 128.996 148.053 135.285 1.00 90.72  ? 4410 PHE A N     1 
ATOM   22628 C  CA    . PHE A 1 4410 ? 128.892 147.449 136.641 1.00 92.76  ? 4410 PHE A CA    1 
ATOM   22629 C  C     . PHE A 1 4410 ? 130.267 147.486 137.301 1.00 90.07  ? 4410 PHE A C     1 
ATOM   22630 O  O     . PHE A 1 4410 ? 130.372 147.917 138.471 1.00 93.04  ? 4410 PHE A O     1 
ATOM   22631 C  CB    . PHE A 1 4410 ? 128.362 146.014 136.577 1.00 100.79 ? 4410 PHE A CB    1 
ATOM   22632 C  CG    . PHE A 1 4410 ? 128.372 145.291 137.917 1.00 106.28 ? 4410 PHE A CG    1 
ATOM   22633 C  CD1   . PHE A 1 4410 ? 129.472 144.542 138.318 1.00 106.74 ? 4410 PHE A CD1   1 
ATOM   22634 C  CD2   . PHE A 1 4410 ? 127.284 145.373 138.780 1.00 101.98 ? 4410 PHE A CD2   1 
ATOM   22635 C  CE1   . PHE A 1 4410 ? 129.479 143.889 139.540 1.00 105.31 ? 4410 PHE A CE1   1 
ATOM   22636 C  CE2   . PHE A 1 4410 ? 127.297 144.718 140.001 1.00 100.29 ? 4410 PHE A CE2   1 
ATOM   22637 C  CZ    . PHE A 1 4410 ? 128.393 143.979 140.379 1.00 105.26 ? 4410 PHE A CZ    1 
ATOM   22638 N  N     . ARG A 1 4411 ? 131.297 147.051 136.570 1.00 85.96  ? 4411 ARG A N     1 
ATOM   22639 C  CA    . ARG A 1 4411 ? 132.672 147.014 137.132 1.00 89.85  ? 4411 ARG A CA    1 
ATOM   22640 C  C     . ARG A 1 4411 ? 133.068 148.427 137.588 1.00 91.32  ? 4411 ARG A C     1 
ATOM   22641 O  O     . ARG A 1 4411 ? 133.599 148.561 138.713 1.00 92.16  ? 4411 ARG A O     1 
ATOM   22642 C  CB    . ARG A 1 4411 ? 133.645 146.472 136.080 1.00 85.69  ? 4411 ARG A CB    1 
ATOM   22643 C  CG    . ARG A 1 4411 ? 133.292 145.076 135.588 1.00 85.16  ? 4411 ARG A CG    1 
ATOM   22644 C  CD    . ARG A 1 4411 ? 134.258 144.577 134.525 1.00 84.40  ? 4411 ARG A CD    1 
ATOM   22645 N  NE    . ARG A 1 4411 ? 134.237 145.402 133.312 1.00 88.46  ? 4411 ARG A NE    1 
ATOM   22646 C  CZ    . ARG A 1 4411 ? 134.979 145.174 132.236 1.00 79.94  ? 4411 ARG A CZ    1 
ATOM   22647 N  NH1   . ARG A 1 4411 ? 135.754 144.105 132.182 1.00 71.58  ? 4411 ARG A NH1   1 
ATOM   22648 N  NH2   . ARG A 1 4411 ? 134.945 146.014 131.217 1.00 75.56  ? 4411 ARG A NH2   1 
ATOM   22649 N  N     . PHE A 1 4412 ? 132.807 149.435 136.751 1.00 88.11  ? 4412 PHE A N     1 
ATOM   22650 C  CA    . PHE A 1 4412 ? 133.145 150.840 137.105 1.00 87.32  ? 4412 PHE A CA    1 
ATOM   22651 C  C     . PHE A 1 4412 ? 132.402 151.228 138.380 1.00 91.52  ? 4412 PHE A C     1 
ATOM   22652 O  O     . PHE A 1 4412 ? 133.049 151.695 139.343 1.00 91.49  ? 4412 PHE A O     1 
ATOM   22653 C  CB    . PHE A 1 4412 ? 132.790 151.770 135.940 1.00 76.21  ? 4412 PHE A CB    1 
ATOM   22654 C  CG    . PHE A 1 4412 ? 132.715 153.244 136.315 1.00 73.49  ? 4412 PHE A CG    1 
ATOM   22655 C  CD1   . PHE A 1 4412 ? 133.854 154.040 136.307 1.00 77.08  ? 4412 PHE A CD1   1 
ATOM   22656 C  CD2   . PHE A 1 4412 ? 131.505 153.830 136.668 1.00 74.77  ? 4412 PHE A CD2   1 
ATOM   22657 C  CE1   . PHE A 1 4412 ? 133.783 155.381 136.650 1.00 76.53  ? 4412 PHE A CE1   1 
ATOM   22658 C  CE2   . PHE A 1 4412 ? 131.441 155.172 137.008 1.00 76.11  ? 4412 PHE A CE2   1 
ATOM   22659 C  CZ    . PHE A 1 4412 ? 132.579 155.944 136.998 1.00 76.96  ? 4412 PHE A CZ    1 
ATOM   22660 N  N     . PHE A 1 4413 ? 131.080 151.038 138.394 1.00 92.08  ? 4413 PHE A N     1 
ATOM   22661 C  CA    . PHE A 1 4413 ? 130.281 151.427 139.551 1.00 85.13  ? 4413 PHE A CA    1 
ATOM   22662 C  C     . PHE A 1 4413 ? 130.728 150.686 140.804 1.00 91.66  ? 4413 PHE A C     1 
ATOM   22663 O  O     . PHE A 1 4413 ? 130.704 151.250 141.904 1.00 95.66  ? 4413 PHE A O     1 
ATOM   22664 C  CB    . PHE A 1 4413 ? 128.797 151.178 139.278 1.00 85.53  ? 4413 PHE A CB    1 
ATOM   22665 C  CG    . PHE A 1 4413 ? 128.203 152.102 138.251 1.00 86.36  ? 4413 PHE A CG    1 
ATOM   22666 C  CD1   . PHE A 1 4413 ? 128.419 153.467 138.320 1.00 83.41  ? 4413 PHE A CD1   1 
ATOM   22667 C  CD2   . PHE A 1 4413 ? 127.409 151.608 137.230 1.00 84.25  ? 4413 PHE A CD2   1 
ATOM   22668 C  CE1   . PHE A 1 4413 ? 127.871 154.317 137.380 1.00 79.78  ? 4413 PHE A CE1   1 
ATOM   22669 C  CE2   . PHE A 1 4413 ? 126.861 152.453 136.287 1.00 80.30  ? 4413 PHE A CE2   1 
ATOM   22670 C  CZ    . PHE A 1 4413 ? 127.090 153.809 136.363 1.00 76.72  ? 4413 PHE A CZ    1 
ATOM   22671 N  N     . GLU A 1 4414 ? 131.124 149.420 140.663 1.00 93.98  ? 4414 GLU A N     1 
ATOM   22672 C  CA    . GLU A 1 4414 ? 131.627 148.661 141.801 1.00 98.17  ? 4414 GLU A CA    1 
ATOM   22673 C  C     . GLU A 1 4414 ? 132.900 149.288 142.350 1.00 102.35 ? 4414 GLU A C     1 
ATOM   22674 O  O     . GLU A 1 4414 ? 133.053 149.442 143.566 1.00 106.35 ? 4414 GLU A O     1 
ATOM   22675 C  CB    . GLU A 1 4414 ? 131.866 147.206 141.392 1.00 93.87  ? 4414 GLU A CB    1 
ATOM   22676 C  CG    . GLU A 1 4414 ? 132.665 146.365 142.389 1.00 104.45 ? 4414 GLU A CG    1 
ATOM   22677 C  CD    . GLU A 1 4414 ? 132.213 146.529 143.832 1.00 110.62 ? 4414 GLU A CD    1 
ATOM   22678 O  OE1   . GLU A 1 4414 ? 130.992 146.605 144.078 1.00 110.47 ? 4414 GLU A OE1   1 
ATOM   22679 O  OE2   . GLU A 1 4414 ? 133.086 146.586 144.723 1.00 109.73 ? 4414 GLU A OE2   1 
ATOM   22680 N  N     . ARG A 1 4415 ? 133.823 149.672 141.465 1.00 98.05  ? 4415 ARG A N     1 
ATOM   22681 C  CA    . ARG A 1 4415 ? 135.032 150.344 141.935 1.00 99.27  ? 4415 ARG A CA    1 
ATOM   22682 C  C     . ARG A 1 4415 ? 134.696 151.676 142.599 1.00 98.55  ? 4415 ARG A C     1 
ATOM   22683 O  O     . ARG A 1 4415 ? 135.272 152.028 143.640 1.00 95.74  ? 4415 ARG A O     1 
ATOM   22684 C  CB    . ARG A 1 4415 ? 136.009 150.539 140.775 1.00 101.42 ? 4415 ARG A CB    1 
ATOM   22685 C  CG    . ARG A 1 4415 ? 137.178 151.455 141.093 1.00 107.75 ? 4415 ARG A CG    1 
ATOM   22686 C  CD    . ARG A 1 4415 ? 138.065 151.666 139.878 1.00 108.56 ? 4415 ARG A CD    1 
ATOM   22687 N  NE    . ARG A 1 4415 ? 137.311 152.107 138.711 1.00 106.44 ? 4415 ARG A NE    1 
ATOM   22688 C  CZ    . ARG A 1 4415 ? 137.260 151.447 137.562 1.00 103.16 ? 4415 ARG A CZ    1 
ATOM   22689 N  NH1   . ARG A 1 4415 ? 137.909 150.307 137.390 1.00 99.49  ? 4415 ARG A NH1   1 
ATOM   22690 N  NH2   . ARG A 1 4415 ? 136.541 151.945 136.560 1.00 94.76  ? 4415 ARG A NH2   1 
ATOM   22691 N  N     . GLU A 1 4416 ? 133.752 152.422 142.018 1.00 98.68  ? 4416 GLU A N     1 
ATOM   22692 C  CA    . GLU A 1 4416 ? 133.357 153.709 142.585 1.00 98.05  ? 4416 GLU A CA    1 
ATOM   22693 C  C     . GLU A 1 4416 ? 132.794 153.548 143.991 1.00 100.92 ? 4416 GLU A C     1 
ATOM   22694 O  O     . GLU A 1 4416 ? 133.187 154.268 144.915 1.00 103.91 ? 4416 GLU A O     1 
ATOM   22695 C  CB    . GLU A 1 4416 ? 132.331 154.386 141.678 1.00 94.13  ? 4416 GLU A CB    1 
ATOM   22696 C  CG    . GLU A 1 4416 ? 132.925 155.048 140.458 1.00 93.74  ? 4416 GLU A CG    1 
ATOM   22697 C  CD    . GLU A 1 4416 ? 133.602 156.359 140.785 1.00 92.30  ? 4416 GLU A CD    1 
ATOM   22698 O  OE1   . GLU A 1 4416 ? 132.932 157.248 141.347 1.00 94.47  ? 4416 GLU A OE1   1 
ATOM   22699 O  OE2   . GLU A 1 4416 ? 134.803 156.502 140.481 1.00 89.88  ? 4416 GLU A OE2   1 
ATOM   22700 N  N     . VAL A 1 4417 ? 131.864 152.608 144.171 1.00 99.71  ? 4417 VAL A N     1 
ATOM   22701 C  CA    . VAL A 1 4417 ? 131.260 152.425 145.486 1.00 100.24 ? 4417 VAL A CA    1 
ATOM   22702 C  C     . VAL A 1 4417 ? 132.267 151.838 146.465 1.00 99.94  ? 4417 VAL A C     1 
ATOM   22703 O  O     . VAL A 1 4417 ? 132.211 152.128 147.664 1.00 100.29 ? 4417 VAL A O     1 
ATOM   22704 C  CB    . VAL A 1 4417 ? 129.984 151.564 145.394 1.00 100.82 ? 4417 VAL A CB    1 
ATOM   22705 C  CG1   . VAL A 1 4417 ? 128.952 152.241 144.504 1.00 99.53  ? 4417 VAL A CG1   1 
ATOM   22706 C  CG2   . VAL A 1 4417 ? 130.299 150.164 144.896 1.00 96.89  ? 4417 VAL A CG2   1 
ATOM   22707 N  N     . LYS A 1 4418 ? 133.208 151.021 145.982 1.00 98.85  ? 4418 LYS A N     1 
ATOM   22708 C  CA    . LYS A 1 4418 ? 134.246 150.491 146.857 1.00 99.27  ? 4418 LYS A CA    1 
ATOM   22709 C  C     . LYS A 1 4418 ? 135.122 151.608 147.408 1.00 102.34 ? 4418 LYS A C     1 
ATOM   22710 O  O     . LYS A 1 4418 ? 135.482 151.600 148.591 1.00 105.14 ? 4418 LYS A O     1 
ATOM   22711 C  CB    . LYS A 1 4418 ? 135.086 149.464 146.098 1.00 100.69 ? 4418 LYS A CB    1 
ATOM   22712 C  CG    . LYS A 1 4418 ? 136.180 148.812 146.921 1.00 108.73 ? 4418 LYS A CG    1 
ATOM   22713 C  CD    . LYS A 1 4418 ? 136.943 147.788 146.094 1.00 106.31 ? 4418 LYS A CD    1 
ATOM   22714 C  CE    . LYS A 1 4418 ? 138.025 147.108 146.916 1.00 110.96 ? 4418 LYS A CE    1 
ATOM   22715 N  NZ    . LYS A 1 4418 ? 138.761 146.085 146.123 1.00 112.93 ? 4418 LYS A NZ    1 
ATOM   22716 N  N     . MET A 1 4419 ? 135.482 152.577 146.563 1.00 102.60 ? 4419 MET A N     1 
ATOM   22717 C  CA    . MET A 1 4419 ? 136.222 153.737 147.057 1.00 105.15 ? 4419 MET A CA    1 
ATOM   22718 C  C     . MET A 1 4419 ? 135.363 154.589 147.988 1.00 100.99 ? 4419 MET A C     1 
ATOM   22719 O  O     . MET A 1 4419 ? 135.829 155.043 149.046 1.00 98.30  ? 4419 MET A O     1 
ATOM   22720 C  CB    . MET A 1 4419 ? 136.722 154.576 145.881 1.00 104.49 ? 4419 MET A CB    1 
ATOM   22721 C  CG    . MET A 1 4419 ? 137.768 153.890 145.021 1.00 110.03 ? 4419 MET A CG    1 
ATOM   22722 S  SD    . MET A 1 4419 ? 138.254 154.892 143.602 1.00 129.75 ? 4419 MET A SD    1 
ATOM   22723 C  CE    . MET A 1 4419 ? 139.176 156.201 144.404 1.00 123.49 ? 4419 MET A CE    1 
ATOM   22724 N  N     . GLY A 1 4420 ? 134.104 154.811 147.605 1.00 98.85  ? 4420 GLY A N     1 
ATOM   22725 C  CA    . GLY A 1 4420 ? 133.252 155.713 148.359 1.00 98.02  ? 4420 GLY A CA    1 
ATOM   22726 C  C     . GLY A 1 4420 ? 132.928 155.202 149.747 1.00 101.42 ? 4420 GLY A C     1 
ATOM   22727 O  O     . GLY A 1 4420 ? 132.872 155.979 150.699 1.00 101.93 ? 4420 GLY A O     1 
ATOM   22728 N  N     . ALA A 1 4421 ? 132.704 153.894 149.883 1.00 106.24 ? 4421 ALA A N     1 
ATOM   22729 C  CA    . ALA A 1 4421 ? 132.406 153.328 151.195 1.00 98.43  ? 4421 ALA A CA    1 
ATOM   22730 C  C     . ALA A 1 4421 ? 133.592 153.468 152.139 1.00 95.72  ? 4421 ALA A C     1 
ATOM   22731 O  O     . ALA A 1 4421 ? 133.418 153.804 153.316 1.00 95.70  ? 4421 ALA A O     1 
ATOM   22732 C  CB    . ALA A 1 4421 ? 132.000 151.862 151.054 1.00 99.15  ? 4421 ALA A CB    1 
ATOM   22733 N  N     . LYS A 1 4422 ? 134.804 153.209 151.643 1.00 98.40  ? 4422 LYS A N     1 
ATOM   22734 C  CA    . LYS A 1 4422 ? 135.991 153.355 152.478 1.00 104.87 ? 4422 LYS A CA    1 
ATOM   22735 C  C     . LYS A 1 4422 ? 136.182 154.804 152.909 1.00 103.05 ? 4422 LYS A C     1 
ATOM   22736 O  O     . LYS A 1 4422 ? 136.464 155.085 154.084 1.00 102.05 ? 4422 LYS A O     1 
ATOM   22737 C  CB    . LYS A 1 4422 ? 137.222 152.845 151.729 1.00 104.52 ? 4422 LYS A CB    1 
ATOM   22738 C  CG    . LYS A 1 4422 ? 138.541 153.171 152.404 1.00 108.16 ? 4422 LYS A CG    1 
ATOM   22739 C  CD    . LYS A 1 4422 ? 139.714 152.707 151.562 1.00 114.80 ? 4422 LYS A CD    1 
ATOM   22740 C  CE    . LYS A 1 4422 ? 139.629 151.218 151.275 1.00 116.92 ? 4422 LYS A CE    1 
ATOM   22741 N  NZ    . LYS A 1 4422 ? 139.632 150.413 152.527 1.00 111.84 ? 4422 LYS A NZ    1 
ATOM   22742 N  N     . LEU A 1 4423 ? 136.024 155.744 151.971 1.00 99.30  ? 4423 LEU A N     1 
ATOM   22743 C  CA    . LEU A 1 4423 ? 136.140 157.153 152.337 1.00 98.20  ? 4423 LEU A CA    1 
ATOM   22744 C  C     . LEU A 1 4423 ? 135.053 157.552 153.329 1.00 90.88  ? 4423 LEU A C     1 
ATOM   22745 O  O     . LEU A 1 4423 ? 135.299 158.338 154.253 1.00 94.69  ? 4423 LEU A O     1 
ATOM   22746 C  CB    . LEU A 1 4423 ? 136.083 158.032 151.089 1.00 100.32 ? 4423 LEU A CB    1 
ATOM   22747 C  CG    . LEU A 1 4423 ? 136.296 159.532 151.309 1.00 100.34 ? 4423 LEU A CG    1 
ATOM   22748 C  CD1   . LEU A 1 4423 ? 137.481 159.791 152.227 1.00 97.04  ? 4423 LEU A CD1   1 
ATOM   22749 C  CD2   . LEU A 1 4423 ? 136.483 160.240 149.985 1.00 96.56  ? 4423 LEU A CD2   1 
ATOM   22750 N  N     . LEU A 1 4424 ? 133.845 157.015 153.151 1.00 92.49  ? 4424 LEU A N     1 
ATOM   22751 C  CA    . LEU A 1 4424 ? 132.747 157.278 154.073 1.00 92.81  ? 4424 LEU A CA    1 
ATOM   22752 C  C     . LEU A 1 4424 ? 133.099 156.826 155.480 1.00 91.92  ? 4424 LEU A C     1 
ATOM   22753 O  O     . LEU A 1 4424 ? 132.923 157.574 156.447 1.00 87.80  ? 4424 LEU A O     1 
ATOM   22754 C  CB    . LEU A 1 4424 ? 131.489 156.560 153.583 1.00 96.38  ? 4424 LEU A CB    1 
ATOM   22755 C  CG    . LEU A 1 4424 ? 130.123 157.060 154.044 1.00 92.55  ? 4424 LEU A CG    1 
ATOM   22756 C  CD1   . LEU A 1 4424 ? 129.866 158.432 153.475 1.00 91.35  ? 4424 LEU A CD1   1 
ATOM   22757 C  CD2   . LEU A 1 4424 ? 129.033 156.092 153.624 1.00 95.88  ? 4424 LEU A CD2   1 
ATOM   22758 N  N     . GLN A 1 4425 ? 133.596 155.594 155.611 1.00 96.82  ? 4425 GLN A N     1 
ATOM   22759 C  CA    . GLN A 1 4425 ? 133.961 155.086 156.929 1.00 94.10  ? 4425 GLN A CA    1 
ATOM   22760 C  C     . GLN A 1 4425 ? 135.060 155.931 157.555 1.00 93.75  ? 4425 GLN A C     1 
ATOM   22761 O  O     . GLN A 1 4425 ? 134.983 156.279 158.738 1.00 99.72  ? 4425 GLN A O     1 
ATOM   22762 C  CB    . GLN A 1 4425 ? 134.400 153.623 156.841 1.00 98.16  ? 4425 GLN A CB    1 
ATOM   22763 C  CG    . GLN A 1 4425 ? 133.396 152.686 156.189 1.00 98.25  ? 4425 GLN A CG    1 
ATOM   22764 C  CD    . GLN A 1 4425 ? 131.961 153.011 156.552 1.00 105.46 ? 4425 GLN A CD    1 
ATOM   22765 O  OE1   . GLN A 1 4425 ? 131.600 153.065 157.728 1.00 109.01 ? 4425 GLN A OE1   1 
ATOM   22766 N  NE2   . GLN A 1 4425 ? 131.130 153.223 155.538 1.00 107.80 ? 4425 GLN A NE2   1 
ATOM   22767 N  N     . ASP A 1 4426 ? 136.080 156.287 156.771 1.00 93.95  ? 4426 ASP A N     1 
ATOM   22768 C  CA    . ASP A 1 4426 ? 137.185 157.075 157.313 1.00 96.04  ? 4426 ASP A CA    1 
ATOM   22769 C  C     . ASP A 1 4426 ? 136.698 158.427 157.824 1.00 91.70  ? 4426 ASP A C     1 
ATOM   22770 O  O     . ASP A 1 4426 ? 136.979 158.813 158.968 1.00 91.79  ? 4426 ASP A O     1 
ATOM   22771 C  CB    . ASP A 1 4426 ? 138.266 157.254 156.246 1.00 98.36  ? 4426 ASP A CB    1 
ATOM   22772 C  CG    . ASP A 1 4426 ? 139.525 157.902 156.789 1.00 102.65 ? 4426 ASP A CG    1 
ATOM   22773 O  OD1   . ASP A 1 4426 ? 139.644 158.044 158.024 1.00 100.15 ? 4426 ASP A OD1   1 
ATOM   22774 O  OD2   . ASP A 1 4426 ? 140.399 158.273 155.977 1.00 108.00 ? 4426 ASP A OD2   1 
ATOM   22775 N  N     . VAL A 1 4427 ? 135.951 159.156 156.991 1.00 91.47  ? 4427 VAL A N     1 
ATOM   22776 C  CA    . VAL A 1 4427 ? 135.498 160.490 157.371 1.00 84.38  ? 4427 VAL A CA    1 
ATOM   22777 C  C     . VAL A 1 4427 ? 134.532 160.420 158.547 1.00 88.10  ? 4427 VAL A C     1 
ATOM   22778 O  O     . VAL A 1 4427 ? 134.599 161.242 159.469 1.00 92.33  ? 4427 VAL A O     1 
ATOM   22779 C  CB    . VAL A 1 4427 ? 134.871 161.204 156.160 1.00 82.17  ? 4427 VAL A CB    1 
ATOM   22780 C  CG1   . VAL A 1 4427 ? 134.231 162.513 156.583 1.00 76.86  ? 4427 VAL A CG1   1 
ATOM   22781 C  CG2   . VAL A 1 4427 ? 135.925 161.451 155.101 1.00 86.35  ? 4427 VAL A CG2   1 
ATOM   22782 N  N     . ARG A 1 4428 ? 133.616 159.447 158.539 1.00 89.99  ? 4428 ARG A N     1 
ATOM   22783 C  CA    . ARG A 1 4428 ? 132.650 159.338 159.626 1.00 85.99  ? 4428 ARG A CA    1 
ATOM   22784 C  C     . ARG A 1 4428 ? 133.333 158.990 160.942 1.00 87.87  ? 4428 ARG A C     1 
ATOM   22785 O  O     . ARG A 1 4428 ? 132.971 159.533 161.991 1.00 89.22  ? 4428 ARG A O     1 
ATOM   22786 C  CB    . ARG A 1 4428 ? 131.580 158.304 159.273 1.00 94.87  ? 4428 ARG A CB    1 
ATOM   22787 C  CG    . ARG A 1 4428 ? 130.843 157.731 160.469 1.00 98.21  ? 4428 ARG A CG    1 
ATOM   22788 C  CD    . ARG A 1 4428 ? 129.447 157.275 160.083 1.00 99.82  ? 4428 ARG A CD    1 
ATOM   22789 N  NE    . ARG A 1 4428 ? 128.639 158.375 159.567 1.00 94.64  ? 4428 ARG A NE    1 
ATOM   22790 C  CZ    . ARG A 1 4428 ? 127.614 158.916 160.211 1.00 92.85  ? 4428 ARG A CZ    1 
ATOM   22791 N  NH1   . ARG A 1 4428 ? 127.243 158.486 161.405 1.00 91.38  ? 4428 ARG A NH1   1 
ATOM   22792 N  NH2   . ARG A 1 4428 ? 126.946 159.915 159.642 1.00 89.41  ? 4428 ARG A NH2   1 
ATOM   22793 N  N     . GLN A 1 4429 ? 134.325 158.095 160.914 1.00 90.58  ? 4429 GLN A N     1 
ATOM   22794 C  CA    . GLN A 1 4429 ? 135.056 157.779 162.137 1.00 90.45  ? 4429 GLN A CA    1 
ATOM   22795 C  C     . GLN A 1 4429 ? 135.835 158.985 162.646 1.00 93.33  ? 4429 GLN A C     1 
ATOM   22796 O  O     . GLN A 1 4429 ? 135.871 159.240 163.856 1.00 95.52  ? 4429 GLN A O     1 
ATOM   22797 C  CB    . GLN A 1 4429 ? 135.990 156.594 161.902 1.00 89.66  ? 4429 GLN A CB    1 
ATOM   22798 C  CG    . GLN A 1 4429 ? 136.756 156.163 163.144 1.00 102.50 ? 4429 GLN A CG    1 
ATOM   22799 C  CD    . GLN A 1 4429 ? 135.841 155.776 164.293 1.00 106.69 ? 4429 GLN A CD    1 
ATOM   22800 O  OE1   . GLN A 1 4429 ? 135.008 154.879 164.164 1.00 105.89 ? 4429 GLN A OE1   1 
ATOM   22801 N  NE2   . GLN A 1 4429 ? 135.994 156.452 165.426 1.00 99.02  ? 4429 GLN A NE2   1 
ATOM   22802 N  N     . ASP A 1 4430 ? 136.463 159.742 161.740 1.00 95.25  ? 4430 ASP A N     1 
ATOM   22803 C  CA    . ASP A 1 4430 ? 137.179 160.942 162.168 1.00 89.34  ? 4430 ASP A CA    1 
ATOM   22804 C  C     . ASP A 1 4430 ? 136.230 161.960 162.792 1.00 87.40  ? 4430 ASP A C     1 
ATOM   22805 O  O     . ASP A 1 4430 ? 136.543 162.562 163.828 1.00 92.38  ? 4430 ASP A O     1 
ATOM   22806 C  CB    . ASP A 1 4430 ? 137.926 161.556 160.985 1.00 88.24  ? 4430 ASP A CB    1 
ATOM   22807 C  CG    . ASP A 1 4430 ? 139.067 160.684 160.505 1.00 94.58  ? 4430 ASP A CG    1 
ATOM   22808 O  OD1   . ASP A 1 4430 ? 139.281 159.606 161.096 1.00 95.65  ? 4430 ASP A OD1   1 
ATOM   22809 O  OD2   . ASP A 1 4430 ? 139.752 161.077 159.537 1.00 95.39  ? 4430 ASP A OD2   1 
ATOM   22810 N  N     . LEU A 1 4431 ? 135.060 162.158 162.184 1.00 87.89  ? 4431 LEU A N     1 
ATOM   22811 C  CA    . LEU A 1 4431 ? 134.093 163.103 162.732 1.00 88.46  ? 4431 LEU A CA    1 
ATOM   22812 C  C     . LEU A 1 4431 ? 133.539 162.618 164.066 1.00 88.14  ? 4431 LEU A C     1 
ATOM   22813 O  O     . LEU A 1 4431 ? 133.276 163.424 164.964 1.00 91.91  ? 4431 LEU A O     1 
ATOM   22814 C  CB    . LEU A 1 4431 ? 132.965 163.339 161.730 1.00 89.75  ? 4431 LEU A CB    1 
ATOM   22815 C  CG    . LEU A 1 4431 ? 133.325 164.201 160.519 1.00 88.59  ? 4431 LEU A CG    1 
ATOM   22816 C  CD1   . LEU A 1 4431 ? 132.109 164.428 159.641 1.00 86.14  ? 4431 LEU A CD1   1 
ATOM   22817 C  CD2   . LEU A 1 4431 ? 133.923 165.525 160.963 1.00 84.11  ? 4431 LEU A CD2   1 
ATOM   22818 N  N     . ALA A 1 4432 ? 133.352 161.304 164.216 1.00 88.39  ? 4432 ALA A N     1 
ATOM   22819 C  CA    . ALA A 1 4432 ? 132.907 160.762 165.494 1.00 91.88  ? 4432 ALA A CA    1 
ATOM   22820 C  C     . ALA A 1 4432 ? 133.951 160.991 166.578 1.00 90.88  ? 4432 ALA A C     1 
ATOM   22821 O  O     . ALA A 1 4432 ? 133.610 161.326 167.718 1.00 92.54  ? 4432 ALA A O     1 
ATOM   22822 C  CB    . ALA A 1 4432 ? 132.594 159.273 165.354 1.00 95.24  ? 4432 ALA A CB    1 
ATOM   22823 N  N     . ASP A 1 4433 ? 135.230 160.815 166.240 1.00 91.16  ? 4433 ASP A N     1 
ATOM   22824 C  CA    . ASP A 1 4433 ? 136.292 161.109 167.197 1.00 94.62  ? 4433 ASP A CA    1 
ATOM   22825 C  C     . ASP A 1 4433 ? 136.303 162.588 167.570 1.00 93.62  ? 4433 ASP A C     1 
ATOM   22826 O  O     . ASP A 1 4433 ? 136.502 162.942 168.739 1.00 92.72  ? 4433 ASP A O     1 
ATOM   22827 C  CB    . ASP A 1 4433 ? 137.644 160.688 166.624 1.00 95.20  ? 4433 ASP A CB    1 
ATOM   22828 C  CG    . ASP A 1 4433 ? 137.714 159.201 166.335 1.00 101.97 ? 4433 ASP A CG    1 
ATOM   22829 O  OD1   . ASP A 1 4433 ? 136.732 158.490 166.635 1.00 97.60  ? 4433 ASP A OD1   1 
ATOM   22830 O  OD2   . ASP A 1 4433 ? 138.751 158.744 165.809 1.00 107.84 ? 4433 ASP A OD2   1 
ATOM   22831 N  N     . VAL A 1 4434 ? 136.091 163.465 166.586 1.00 90.04  ? 4434 VAL A N     1 
ATOM   22832 C  CA    . VAL A 1 4434 ? 136.026 164.899 166.864 1.00 81.12  ? 4434 VAL A CA    1 
ATOM   22833 C  C     . VAL A 1 4434 ? 134.868 165.211 167.806 1.00 87.92  ? 4434 VAL A C     1 
ATOM   22834 O  O     . VAL A 1 4434 ? 135.006 166.008 168.741 1.00 95.24  ? 4434 VAL A O     1 
ATOM   22835 C  CB    . VAL A 1 4434 ? 135.919 165.695 165.550 1.00 76.28  ? 4434 VAL A CB    1 
ATOM   22836 C  CG1   . VAL A 1 4434 ? 135.565 167.143 165.830 1.00 81.08  ? 4434 VAL A CG1   1 
ATOM   22837 C  CG2   . VAL A 1 4434 ? 137.222 165.611 164.781 1.00 80.34  ? 4434 VAL A CG2   1 
ATOM   22838 N  N     . VAL A 1 4435 ? 133.708 164.591 167.572 1.00 89.81  ? 4435 VAL A N     1 
ATOM   22839 C  CA    . VAL A 1 4435 ? 132.556 164.798 168.447 1.00 92.25  ? 4435 VAL A CA    1 
ATOM   22840 C  C     . VAL A 1 4435 ? 132.862 164.311 169.857 1.00 95.37  ? 4435 VAL A C     1 
ATOM   22841 O  O     . VAL A 1 4435 ? 132.524 164.974 170.846 1.00 95.42  ? 4435 VAL A O     1 
ATOM   22842 C  CB    . VAL A 1 4435 ? 131.309 164.103 167.870 1.00 95.35  ? 4435 VAL A CB    1 
ATOM   22843 C  CG1   . VAL A 1 4435 ? 130.183 164.090 168.891 1.00 94.02  ? 4435 VAL A CG1   1 
ATOM   22844 C  CG2   . VAL A 1 4435 ? 130.856 164.797 166.605 1.00 93.97  ? 4435 VAL A CG2   1 
ATOM   22845 N  N     . GLN A 1 4436 ? 133.501 163.144 169.974 1.00 94.28  ? 4436 GLN A N     1 
ATOM   22846 C  CA    . GLN A 1 4436 ? 133.843 162.616 171.292 1.00 90.83  ? 4436 GLN A CA    1 
ATOM   22847 C  C     . GLN A 1 4436 ? 134.786 163.554 172.033 1.00 94.57  ? 4436 GLN A C     1 
ATOM   22848 O  O     . GLN A 1 4436 ? 134.618 163.789 173.235 1.00 98.42  ? 4436 GLN A O     1 
ATOM   22849 C  CB    . GLN A 1 4436 ? 134.467 161.227 171.163 1.00 91.72  ? 4436 GLN A CB    1 
ATOM   22850 C  CG    . GLN A 1 4436 ? 133.512 160.156 170.665 1.00 100.43 ? 4436 GLN A CG    1 
ATOM   22851 C  CD    . GLN A 1 4436 ? 134.174 158.798 170.543 1.00 102.52 ? 4436 GLN A CD    1 
ATOM   22852 O  OE1   . GLN A 1 4436 ? 135.375 158.658 170.773 1.00 98.84  ? 4436 GLN A OE1   1 
ATOM   22853 N  NE2   . GLN A 1 4436 ? 133.393 157.789 170.175 1.00 97.50  ? 4436 GLN A NE2   1 
ATOM   22854 N  N     . VAL A 1 4437 ? 135.786 164.095 171.335 1.00 93.99  ? 4437 VAL A N     1 
ATOM   22855 C  CA    . VAL A 1 4437 ? 136.710 165.030 171.973 1.00 91.71  ? 4437 VAL A CA    1 
ATOM   22856 C  C     . VAL A 1 4437 ? 135.979 166.297 172.402 1.00 89.04  ? 4437 VAL A C     1 
ATOM   22857 O  O     . VAL A 1 4437 ? 136.140 166.773 173.531 1.00 95.28  ? 4437 VAL A O     1 
ATOM   22858 C  CB    . VAL A 1 4437 ? 137.887 165.355 171.039 1.00 89.25  ? 4437 VAL A CB    1 
ATOM   22859 C  CG1   . VAL A 1 4437 ? 138.766 166.404 171.674 1.00 90.79  ? 4437 VAL A CG1   1 
ATOM   22860 C  CG2   . VAL A 1 4437 ? 138.695 164.106 170.748 1.00 95.49  ? 4437 VAL A CG2   1 
ATOM   22861 N  N     . CYS A 1 4438 ? 135.164 166.861 171.509 1.00 89.44  ? 4438 CYS A N     1 
ATOM   22862 C  CA    . CYS A 1 4438 ? 134.432 168.078 171.837 1.00 90.01  ? 4438 CYS A CA    1 
ATOM   22863 C  C     . CYS A 1 4438 ? 133.387 167.851 172.919 1.00 97.05  ? 4438 CYS A C     1 
ATOM   22864 O  O     . CYS A 1 4438 ? 132.999 168.807 173.599 1.00 99.05  ? 4438 CYS A O     1 
ATOM   22865 C  CB    . CYS A 1 4438 ? 133.773 168.649 170.583 1.00 90.23  ? 4438 CYS A CB    1 
ATOM   22866 S  SG    . CYS A 1 4438 ? 134.934 169.327 169.380 1.00 87.92  ? 4438 CYS A SG    1 
ATOM   22867 N  N     . GLU A 1 4439 ? 132.917 166.616 173.091 1.00 101.07 ? 4439 GLU A N     1 
ATOM   22868 C  CA    . GLU A 1 4439 ? 132.023 166.293 174.194 1.00 103.04 ? 4439 GLU A CA    1 
ATOM   22869 C  C     . GLU A 1 4439 ? 132.764 166.141 175.516 1.00 101.81 ? 4439 GLU A C     1 
ATOM   22870 O  O     . GLU A 1 4439 ? 132.133 166.221 176.575 1.00 104.53 ? 4439 GLU A O     1 
ATOM   22871 C  CB    . GLU A 1 4439 ? 131.245 165.011 173.877 1.00 102.70 ? 4439 GLU A CB    1 
ATOM   22872 C  CG    . GLU A 1 4439 ? 129.961 164.834 174.676 1.00 104.15 ? 4439 GLU A CG    1 
ATOM   22873 C  CD    . GLU A 1 4439 ? 130.156 163.995 175.924 1.00 107.75 ? 4439 GLU A CD    1 
ATOM   22874 O  OE1   . GLU A 1 4439 ? 131.042 163.116 175.921 1.00 101.61 ? 4439 GLU A OE1   1 
ATOM   22875 O  OE2   . GLU A 1 4439 ? 129.421 164.216 176.910 1.00 110.64 ? 4439 GLU A OE2   1 
ATOM   22876 N  N     . GLY A 1 4440 ? 134.078 165.941 175.479 1.00 97.56  ? 4440 GLY A N     1 
ATOM   22877 C  CA    . GLY A 1 4440 ? 134.880 165.868 176.680 1.00 93.86  ? 4440 GLY A CA    1 
ATOM   22878 C  C     . GLY A 1 4440 ? 135.230 164.477 177.158 1.00 99.02  ? 4440 GLY A C     1 
ATOM   22879 O  O     . GLY A 1 4440 ? 135.810 164.346 178.243 1.00 99.06  ? 4440 GLY A O     1 
ATOM   22880 N  N     . LYS A 1 4441 ? 134.905 163.434 176.393 1.00 98.23  ? 4441 LYS A N     1 
ATOM   22881 C  CA    . LYS A 1 4441 ? 135.185 162.072 176.825 1.00 101.50 ? 4441 LYS A CA    1 
ATOM   22882 C  C     . LYS A 1 4441 ? 136.342 161.418 176.081 1.00 97.85  ? 4441 LYS A C     1 
ATOM   22883 O  O     . LYS A 1 4441 ? 136.599 160.230 176.299 1.00 94.09  ? 4441 LYS A O     1 
ATOM   22884 C  CB    . LYS A 1 4441 ? 133.938 161.191 176.673 1.00 100.05 ? 4441 LYS A CB    1 
ATOM   22885 C  CG    . LYS A 1 4441 ? 133.471 160.997 175.243 1.00 101.64 ? 4441 LYS A CG    1 
ATOM   22886 C  CD    . LYS A 1 4441 ? 132.202 160.161 175.197 1.00 103.40 ? 4441 LYS A CD    1 
ATOM   22887 C  CE    . LYS A 1 4441 ? 131.739 159.935 173.769 1.00 105.99 ? 4441 LYS A CE    1 
ATOM   22888 N  NZ    . LYS A 1 4441 ? 131.287 161.197 173.122 1.00 104.25 ? 4441 LYS A NZ    1 
ATOM   22889 N  N     . LYS A 1 4442 ? 137.038 162.147 175.214 1.00 94.76  ? 4442 LYS A N     1 
ATOM   22890 C  CA    . LYS A 1 4442 ? 138.176 161.609 174.483 1.00 94.70  ? 4442 LYS A CA    1 
ATOM   22891 C  C     . LYS A 1 4442 ? 139.359 162.561 174.590 1.00 99.56  ? 4442 LYS A C     1 
ATOM   22892 O  O     . LYS A 1 4442 ? 139.200 163.781 174.478 1.00 98.93  ? 4442 LYS A O     1 
ATOM   22893 C  CB    . LYS A 1 4442 ? 137.828 161.365 173.013 1.00 98.76  ? 4442 LYS A CB    1 
ATOM   22894 C  CG    . LYS A 1 4442 ? 138.869 160.550 172.264 1.00 98.93  ? 4442 LYS A CG    1 
ATOM   22895 C  CD    . LYS A 1 4442 ? 138.309 159.994 170.968 1.00 94.90  ? 4442 LYS A CD    1 
ATOM   22896 C  CE    . LYS A 1 4442 ? 139.262 158.987 170.348 1.00 95.15  ? 4442 LYS A CE    1 
ATOM   22897 N  NZ    . LYS A 1 4442 ? 138.644 158.267 169.204 1.00 95.44  ? 4442 LYS A NZ    1 
ATOM   22898 N  N     . LYS A 1 4443 ? 140.543 161.994 174.806 1.00 103.91 ? 4443 LYS A N     1 
ATOM   22899 C  CA    . LYS A 1 4443 ? 141.759 162.785 174.926 1.00 108.33 ? 4443 LYS A CA    1 
ATOM   22900 C  C     . LYS A 1 4443 ? 142.287 163.160 173.546 1.00 110.34 ? 4443 LYS A C     1 
ATOM   22901 O  O     . LYS A 1 4443 ? 142.215 162.369 172.601 1.00 109.29 ? 4443 LYS A O     1 
ATOM   22902 C  CB    . LYS A 1 4443 ? 142.822 162.009 175.705 1.00 107.48 ? 4443 LYS A CB    1 
ATOM   22903 C  CG    . LYS A 1 4443 ? 144.163 162.717 175.821 1.00 108.08 ? 4443 LYS A CG    1 
ATOM   22904 C  CD    . LYS A 1 4443 ? 145.198 161.838 176.503 1.00 113.22 ? 4443 LYS A CD    1 
ATOM   22905 C  CE    . LYS A 1 4443 ? 145.464 160.579 175.696 1.00 111.47 ? 4443 LYS A CE    1 
ATOM   22906 N  NZ    . LYS A 1 4443 ? 146.249 160.869 174.465 1.00 106.90 ? 4443 LYS A NZ    1 
ATOM   22907 N  N     . GLN A 1 4444 ? 142.818 164.375 173.436 1.00 107.28 ? 4444 GLN A N     1 
ATOM   22908 C  CA    . GLN A 1 4444 ? 143.336 164.886 172.169 1.00 106.22 ? 4444 GLN A CA    1 
ATOM   22909 C  C     . GLN A 1 4444 ? 144.676 164.227 171.873 1.00 110.72 ? 4444 GLN A C     1 
ATOM   22910 O  O     . GLN A 1 4444 ? 145.705 164.599 172.441 1.00 111.04 ? 4444 GLN A O     1 
ATOM   22911 C  CB    . GLN A 1 4444 ? 143.478 166.403 172.219 1.00 99.73  ? 4444 GLN A CB    1 
ATOM   22912 C  CG    . GLN A 1 4444 ? 142.175 167.158 172.074 1.00 96.59  ? 4444 GLN A CG    1 
ATOM   22913 C  CD    . GLN A 1 4444 ? 142.335 168.453 171.307 1.00 97.71  ? 4444 GLN A CD    1 
ATOM   22914 O  OE1   . GLN A 1 4444 ? 142.391 168.456 170.078 1.00 97.08  ? 4444 GLN A OE1   1 
ATOM   22915 N  NE2   . GLN A 1 4444 ? 142.407 169.565 172.029 1.00 97.87  ? 4444 GLN A NE2   1 
ATOM   22916 N  N     . THR A 1 4445 ? 144.670 163.244 170.976 1.00 110.17 ? 4445 THR A N     1 
ATOM   22917 C  CA    . THR A 1 4445 ? 145.916 162.707 170.456 1.00 107.64 ? 4445 THR A CA    1 
ATOM   22918 C  C     . THR A 1 4445 ? 146.484 163.668 169.414 1.00 109.19 ? 4445 THR A C     1 
ATOM   22919 O  O     . THR A 1 4445 ? 145.852 164.655 169.030 1.00 109.55 ? 4445 THR A O     1 
ATOM   22920 C  CB    . THR A 1 4445 ? 145.696 161.317 169.864 1.00 105.68 ? 4445 THR A CB    1 
ATOM   22921 O  OG1   . THR A 1 4445 ? 145.133 161.437 168.552 1.00 103.67 ? 4445 THR A OG1   1 
ATOM   22922 C  CG2   . THR A 1 4445 ? 144.752 160.509 170.741 1.00 107.63 ? 4445 THR A CG2   1 
ATOM   22923 N  N     . ASN A 1 4446 ? 147.702 163.379 168.951 1.00 110.25 ? 4446 ASN A N     1 
ATOM   22924 C  CA    . ASN A 1 4446 ? 148.348 164.264 167.985 1.00 111.59 ? 4446 ASN A CA    1 
ATOM   22925 C  C     . ASN A 1 4446 ? 147.557 164.332 166.684 1.00 108.98 ? 4446 ASN A C     1 
ATOM   22926 O  O     . ASN A 1 4446 ? 147.307 165.423 166.154 1.00 111.36 ? 4446 ASN A O     1 
ATOM   22927 C  CB    . ASN A 1 4446 ? 149.780 163.798 167.726 1.00 115.03 ? 4446 ASN A CB    1 
ATOM   22928 C  CG    . ASN A 1 4446 ? 150.641 163.852 168.971 1.00 118.55 ? 4446 ASN A CG    1 
ATOM   22929 O  OD1   . ASN A 1 4446 ? 150.835 164.916 169.559 1.00 114.87 ? 4446 ASN A OD1   1 
ATOM   22930 N  ND2   . ASN A 1 4446 ? 151.161 162.701 169.383 1.00 121.68 ? 4446 ASN A ND2   1 
ATOM   22931 N  N     . TYR A 1 4447 ? 147.143 163.176 166.161 1.00 104.87 ? 4447 TYR A N     1 
ATOM   22932 C  CA    . TYR A 1 4447 ? 146.304 163.174 164.967 1.00 103.85 ? 4447 TYR A CA    1 
ATOM   22933 C  C     . TYR A 1 4447 ? 144.966 163.845 165.239 1.00 99.82  ? 4447 TYR A C     1 
ATOM   22934 O  O     . TYR A 1 4447 ? 144.475 164.623 164.414 1.00 99.31  ? 4447 TYR A O     1 
ATOM   22935 C  CB    . TYR A 1 4447 ? 146.088 161.748 164.465 1.00 105.90 ? 4447 TYR A CB    1 
ATOM   22936 C  CG    . TYR A 1 4447 ? 145.005 161.656 163.417 1.00 102.86 ? 4447 TYR A CG    1 
ATOM   22937 C  CD1   . TYR A 1 4447 ? 145.131 162.317 162.203 1.00 99.44  ? 4447 TYR A CD1   1 
ATOM   22938 C  CD2   . TYR A 1 4447 ? 143.847 160.926 163.647 1.00 97.67  ? 4447 TYR A CD2   1 
ATOM   22939 C  CE1   . TYR A 1 4447 ? 144.142 162.245 161.244 1.00 95.63  ? 4447 TYR A CE1   1 
ATOM   22940 C  CE2   . TYR A 1 4447 ? 142.851 160.848 162.693 1.00 92.92  ? 4447 TYR A CE2   1 
ATOM   22941 C  CZ    . TYR A 1 4447 ? 143.005 161.509 161.495 1.00 91.78  ? 4447 TYR A CZ    1 
ATOM   22942 O  OH    . TYR A 1 4447 ? 142.018 161.435 160.541 1.00 89.80  ? 4447 TYR A OH    1 
ATOM   22943 N  N     . LEU A 1 4448 ? 144.358 163.554 166.390 1.00 99.68  ? 4448 LEU A N     1 
ATOM   22944 C  CA    . LEU A 1 4448 ? 143.100 164.205 166.738 1.00 100.70 ? 4448 LEU A CA    1 
ATOM   22945 C  C     . LEU A 1 4448 ? 143.284 165.708 166.891 1.00 99.41  ? 4448 LEU A C     1 
ATOM   22946 O  O     . LEU A 1 4448 ? 142.431 166.491 166.459 1.00 101.53 ? 4448 LEU A O     1 
ATOM   22947 C  CB    . LEU A 1 4448 ? 142.531 163.601 168.020 1.00 105.51 ? 4448 LEU A CB    1 
ATOM   22948 C  CG    . LEU A 1 4448 ? 141.965 162.187 167.906 1.00 107.45 ? 4448 LEU A CG    1 
ATOM   22949 C  CD1   . LEU A 1 4448 ? 141.176 161.837 169.154 1.00 107.10 ? 4448 LEU A CD1   1 
ATOM   22950 C  CD2   . LEU A 1 4448 ? 141.099 162.056 166.663 1.00 102.24 ? 4448 LEU A CD2   1 
ATOM   22951 N  N     . ARG A 1 4449 ? 144.395 166.130 167.498 1.00 99.04  ? 4449 ARG A N     1 
ATOM   22952 C  CA    . ARG A 1 4449 ? 144.635 167.558 167.676 1.00 98.16  ? 4449 ARG A CA    1 
ATOM   22953 C  C     . ARG A 1 4449 ? 144.799 168.266 166.338 1.00 95.77  ? 4449 ARG A C     1 
ATOM   22954 O  O     . ARG A 1 4449 ? 144.211 169.331 166.117 1.00 96.60  ? 4449 ARG A O     1 
ATOM   22955 C  CB    . ARG A 1 4449 ? 145.863 167.780 168.558 1.00 99.28  ? 4449 ARG A CB    1 
ATOM   22956 C  CG    . ARG A 1 4449 ? 146.013 169.208 169.050 1.00 101.25 ? 4449 ARG A CG    1 
ATOM   22957 C  CD    . ARG A 1 4449 ? 147.194 169.346 169.990 1.00 98.27  ? 4449 ARG A CD    1 
ATOM   22958 N  NE    . ARG A 1 4449 ? 146.870 168.880 171.332 1.00 94.20  ? 4449 ARG A NE    1 
ATOM   22959 C  CZ    . ARG A 1 4449 ? 146.356 169.644 172.286 1.00 89.10  ? 4449 ARG A CZ    1 
ATOM   22960 N  NH1   . ARG A 1 4449 ? 146.093 170.924 172.079 1.00 88.95  ? 4449 ARG A NH1   1 
ATOM   22961 N  NH2   . ARG A 1 4449 ? 146.099 169.111 173.476 1.00 83.79  ? 4449 ARG A NH2   1 
ATOM   22962 N  N     . THR A 1 4450 ? 145.582 167.687 165.421 1.00 97.91  ? 4450 THR A N     1 
ATOM   22963 C  CA    . THR A 1 4450 ? 145.773 168.341 164.130 1.00 96.38  ? 4450 THR A CA    1 
ATOM   22964 C  C     . THR A 1 4450 ? 144.494 168.308 163.298 1.00 93.24  ? 4450 THR A C     1 
ATOM   22965 O  O     . THR A 1 4450 ? 144.188 169.269 162.582 1.00 93.64  ? 4450 THR A O     1 
ATOM   22966 C  CB    . THR A 1 4450 ? 146.950 167.716 163.372 1.00 97.25  ? 4450 THR A CB    1 
ATOM   22967 O  OG1   . THR A 1 4450 ? 147.219 168.483 162.191 1.00 102.48 ? 4450 THR A OG1   1 
ATOM   22968 C  CG2   . THR A 1 4450 ? 146.672 166.278 162.979 1.00 93.10  ? 4450 THR A CG2   1 
ATOM   22969 N  N     . LEU A 1 4451 ? 143.716 167.225 163.399 1.00 91.59  ? 4451 LEU A N     1 
ATOM   22970 C  CA    . LEU A 1 4451 ? 142.438 167.169 162.700 1.00 88.31  ? 4451 LEU A CA    1 
ATOM   22971 C  C     . LEU A 1 4451 ? 141.484 168.236 163.217 1.00 85.50  ? 4451 LEU A C     1 
ATOM   22972 O  O     . LEU A 1 4451 ? 140.825 168.925 162.431 1.00 85.64  ? 4451 LEU A O     1 
ATOM   22973 C  CB    . LEU A 1 4451 ? 141.824 165.777 162.854 1.00 87.41  ? 4451 LEU A CB    1 
ATOM   22974 C  CG    . LEU A 1 4451 ? 140.509 165.497 162.128 1.00 85.47  ? 4451 LEU A CG    1 
ATOM   22975 C  CD1   . LEU A 1 4451 ? 140.738 165.393 160.632 1.00 86.29  ? 4451 LEU A CD1   1 
ATOM   22976 C  CD2   . LEU A 1 4451 ? 139.880 164.226 162.662 1.00 91.08  ? 4451 LEU A CD2   1 
ATOM   22977 N  N     . ILE A 1 4452 ? 141.405 168.393 164.539 1.00 87.41  ? 4452 ILE A N     1 
ATOM   22978 C  CA    . ILE A 1 4452 ? 140.549 169.420 165.121 1.00 86.61  ? 4452 ILE A CA    1 
ATOM   22979 C  C     . ILE A 1 4452 ? 141.013 170.805 164.697 1.00 92.81  ? 4452 ILE A C     1 
ATOM   22980 O  O     . ILE A 1 4452 ? 140.197 171.681 164.386 1.00 95.65  ? 4452 ILE A O     1 
ATOM   22981 C  CB    . ILE A 1 4452 ? 140.514 169.270 166.652 1.00 90.79  ? 4452 ILE A CB    1 
ATOM   22982 C  CG1   . ILE A 1 4452 ? 139.531 168.171 167.054 1.00 89.67  ? 4452 ILE A CG1   1 
ATOM   22983 C  CG2   . ILE A 1 4452 ? 140.176 170.588 167.318 1.00 91.63  ? 4452 ILE A CG2   1 
ATOM   22984 C  CD1   . ILE A 1 4452 ? 139.468 167.934 168.536 1.00 90.17  ? 4452 ILE A CD1   1 
ATOM   22985 N  N     . ASN A 1 4453 ? 142.330 171.027 164.675 1.00 95.12  ? 4453 ASN A N     1 
ATOM   22986 C  CA    . ASN A 1 4453 ? 142.852 172.318 164.242 1.00 89.20  ? 4453 ASN A CA    1 
ATOM   22987 C  C     . ASN A 1 4453 ? 142.460 172.616 162.800 1.00 87.11  ? 4453 ASN A C     1 
ATOM   22988 O  O     . ASN A 1 4453 ? 142.031 173.733 162.484 1.00 89.17  ? 4453 ASN A O     1 
ATOM   22989 C  CB    . ASN A 1 4453 ? 144.371 172.345 164.402 1.00 89.04  ? 4453 ASN A CB    1 
ATOM   22990 C  CG    . ASN A 1 4453 ? 144.970 173.688 164.050 1.00 91.96  ? 4453 ASN A CG    1 
ATOM   22991 O  OD1   . ASN A 1 4453 ? 144.682 174.695 164.695 1.00 93.33  ? 4453 ASN A OD1   1 
ATOM   22992 N  ND2   . ASN A 1 4453 ? 145.810 173.712 163.022 1.00 92.87  ? 4453 ASN A ND2   1 
ATOM   22993 N  N     . GLU A 1 4454 ? 142.590 171.627 161.912 1.00 83.76  ? 4454 GLU A N     1 
ATOM   22994 C  CA    . GLU A 1 4454 ? 142.236 171.848 160.512 1.00 79.23  ? 4454 GLU A CA    1 
ATOM   22995 C  C     . GLU A 1 4454 ? 140.739 172.082 160.340 1.00 79.53  ? 4454 GLU A C     1 
ATOM   22996 O  O     . GLU A 1 4454 ? 140.331 172.946 159.554 1.00 84.06  ? 4454 GLU A O     1 
ATOM   22997 C  CB    . GLU A 1 4454 ? 142.703 170.673 159.655 1.00 84.46  ? 4454 GLU A CB    1 
ATOM   22998 C  CG    . GLU A 1 4454 ? 144.203 170.440 159.700 1.00 89.07  ? 4454 GLU A CG    1 
ATOM   22999 C  CD    . GLU A 1 4454 ? 144.744 169.846 158.417 1.00 96.04  ? 4454 GLU A CD    1 
ATOM   23000 O  OE1   . GLU A 1 4454 ? 144.007 169.833 157.410 1.00 98.08  ? 4454 GLU A OE1   1 
ATOM   23001 O  OE2   . GLU A 1 4454 ? 145.906 169.389 158.415 1.00 98.74  ? 4454 GLU A OE2   1 
ATOM   23002 N  N     . LEU A 1 4455 ? 139.903 171.324 161.053 1.00 78.89  ? 4455 LEU A N     1 
ATOM   23003 C  CA    . LEU A 1 4455 ? 138.461 171.541 160.956 1.00 78.69  ? 4455 LEU A CA    1 
ATOM   23004 C  C     . LEU A 1 4455 ? 138.057 172.912 161.487 1.00 80.36  ? 4455 LEU A C     1 
ATOM   23005 O  O     . LEU A 1 4455 ? 137.190 173.573 160.905 1.00 83.81  ? 4455 LEU A O     1 
ATOM   23006 C  CB    . LEU A 1 4455 ? 137.693 170.434 161.682 1.00 82.48  ? 4455 LEU A CB    1 
ATOM   23007 C  CG    . LEU A 1 4455 ? 137.333 169.164 160.898 1.00 83.61  ? 4455 LEU A CG    1 
ATOM   23008 C  CD1   . LEU A 1 4455 ? 138.528 168.301 160.563 1.00 86.38  ? 4455 LEU A CD1   1 
ATOM   23009 C  CD2   . LEU A 1 4455 ? 136.300 168.356 161.668 1.00 72.98  ? 4455 LEU A CD2   1 
ATOM   23010 N  N     . VAL A 1 4456 ? 138.659 173.355 162.593 1.00 84.93  ? 4456 VAL A N     1 
ATOM   23011 C  CA    . VAL A 1 4456 ? 138.333 174.675 163.124 1.00 87.64  ? 4456 VAL A CA    1 
ATOM   23012 C  C     . VAL A 1 4456 ? 138.789 175.765 162.161 1.00 83.92  ? 4456 VAL A C     1 
ATOM   23013 O  O     . VAL A 1 4456 ? 138.056 176.726 161.898 1.00 81.58  ? 4456 VAL A O     1 
ATOM   23014 C  CB    . VAL A 1 4456 ? 138.946 174.858 164.524 1.00 87.02  ? 4456 VAL A CB    1 
ATOM   23015 C  CG1   . VAL A 1 4456 ? 138.868 176.315 164.952 1.00 86.11  ? 4456 VAL A CG1   1 
ATOM   23016 C  CG2   . VAL A 1 4456 ? 138.233 173.973 165.531 1.00 82.05  ? 4456 VAL A CG2   1 
ATOM   23017 N  N     . LYS A 1 4457 ? 139.996 175.631 161.612 1.00 82.03  ? 4457 LYS A N     1 
ATOM   23018 C  CA    . LYS A 1 4457 ? 140.503 176.602 160.653 1.00 74.99  ? 4457 LYS A CA    1 
ATOM   23019 C  C     . LYS A 1 4457 ? 139.895 176.447 159.266 1.00 74.00  ? 4457 LYS A C     1 
ATOM   23020 O  O     . LYS A 1 4457 ? 140.109 177.316 158.415 1.00 75.34  ? 4457 LYS A O     1 
ATOM   23021 C  CB    . LYS A 1 4457 ? 142.025 176.495 160.548 1.00 72.04  ? 4457 LYS A CB    1 
ATOM   23022 C  CG    . LYS A 1 4457 ? 142.776 177.006 161.759 1.00 72.52  ? 4457 LYS A CG    1 
ATOM   23023 C  CD    . LYS A 1 4457 ? 144.272 176.983 161.509 1.00 72.52  ? 4457 LYS A CD    1 
ATOM   23024 C  CE    . LYS A 1 4457 ? 145.046 177.284 162.776 1.00 83.36  ? 4457 LYS A CE    1 
ATOM   23025 N  NZ    . LYS A 1 4457 ? 144.653 178.593 163.363 1.00 83.06  ? 4457 LYS A NZ    1 
ATOM   23026 N  N     . GLY A 1 4458 ? 139.153 175.372 159.015 1.00 79.10  ? 4458 GLY A N     1 
ATOM   23027 C  CA    . GLY A 1 4458 ? 138.570 175.136 157.714 1.00 80.70  ? 4458 GLY A CA    1 
ATOM   23028 C  C     . GLY A 1 4458 ? 139.492 174.495 156.701 1.00 88.86  ? 4458 GLY A C     1 
ATOM   23029 O  O     . GLY A 1 4458 ? 139.079 174.298 155.551 1.00 94.29  ? 4458 GLY A O     1 
ATOM   23030 N  N     . ILE A 1 4459 ? 140.728 174.171 157.081 1.00 88.20  ? 4459 ILE A N     1 
ATOM   23031 C  CA    . ILE A 1 4459 ? 141.649 173.520 156.159 1.00 82.88  ? 4459 ILE A CA    1 
ATOM   23032 C  C     . ILE A 1 4459 ? 141.208 172.082 155.937 1.00 84.04  ? 4459 ILE A C     1 
ATOM   23033 O  O     . ILE A 1 4459 ? 140.941 171.342 156.893 1.00 87.40  ? 4459 ILE A O     1 
ATOM   23034 C  CB    . ILE A 1 4459 ? 143.088 173.581 156.693 1.00 84.51  ? 4459 ILE A CB    1 
ATOM   23035 C  CG1   . ILE A 1 4459 ? 143.467 175.015 157.058 1.00 78.35  ? 4459 ILE A CG1   1 
ATOM   23036 C  CG2   . ILE A 1 4459 ? 144.060 173.015 155.671 1.00 84.49  ? 4459 ILE A CG2   1 
ATOM   23037 C  CD1   . ILE A 1 4459 ? 144.391 175.107 158.248 1.00 75.71  ? 4459 ILE A CD1   1 
ATOM   23038 N  N     . LEU A 1 4460 ? 141.133 171.681 154.678 1.00 90.05  ? 4460 LEU A N     1 
ATOM   23039 C  CA    . LEU A 1 4460 ? 140.730 170.324 154.335 1.00 95.37  ? 4460 LEU A CA    1 
ATOM   23040 C  C     . LEU A 1 4460 ? 141.767 169.332 154.843 1.00 96.82  ? 4460 LEU A C     1 
ATOM   23041 O  O     . LEU A 1 4460 ? 142.948 169.454 154.494 1.00 100.15 ? 4460 LEU A O     1 
ATOM   23042 C  CB    . LEU A 1 4460 ? 140.561 170.203 152.825 1.00 97.10  ? 4460 LEU A CB    1 
ATOM   23043 C  CG    . LEU A 1 4460 ? 140.209 168.839 152.236 1.00 98.13  ? 4460 LEU A CG    1 
ATOM   23044 C  CD1   . LEU A 1 4460 ? 138.892 168.332 152.794 1.00 100.43 ? 4460 LEU A CD1   1 
ATOM   23045 C  CD2   . LEU A 1 4460 ? 140.144 168.951 150.725 1.00 98.98  ? 4460 LEU A CD2   1 
ATOM   23046 N  N     . PRO A 1 4461 ? 141.387 168.361 155.672 1.00 92.76  ? 4461 PRO A N     1 
ATOM   23047 C  CA    . PRO A 1 4461 ? 142.368 167.384 156.159 1.00 97.39  ? 4461 PRO A CA    1 
ATOM   23048 C  C     . PRO A 1 4461 ? 142.980 166.594 155.013 1.00 102.57 ? 4461 PRO A C     1 
ATOM   23049 O  O     . PRO A 1 4461 ? 142.295 166.197 154.069 1.00 103.72 ? 4461 PRO A O     1 
ATOM   23050 C  CB    . PRO A 1 4461 ? 141.542 166.487 157.088 1.00 97.04  ? 4461 PRO A CB    1 
ATOM   23051 C  CG    . PRO A 1 4461 ? 140.389 167.338 157.504 1.00 90.77  ? 4461 PRO A CG    1 
ATOM   23052 C  CD    . PRO A 1 4461 ? 140.074 168.197 156.317 1.00 91.06  ? 4461 PRO A CD    1 
ATOM   23053 N  N     . ARG A 1 4462 ? 144.292 166.363 155.110 1.00 103.50 ? 4462 ARG A N     1 
ATOM   23054 C  CA    . ARG A 1 4462 ? 144.987 165.633 154.056 1.00 109.29 ? 4462 ARG A CA    1 
ATOM   23055 C  C     . ARG A 1 4462 ? 144.638 164.151 154.080 1.00 111.22 ? 4462 ARG A C     1 
ATOM   23056 O  O     . ARG A 1 4462 ? 144.667 163.492 153.034 1.00 113.80 ? 4462 ARG A O     1 
ATOM   23057 C  CB    . ARG A 1 4462 ? 146.497 165.831 154.188 1.00 114.66 ? 4462 ARG A CB    1 
ATOM   23058 C  CG    . ARG A 1 4462 ? 147.299 165.267 153.027 1.00 115.03 ? 4462 ARG A CG    1 
ATOM   23059 C  CD    . ARG A 1 4462 ? 146.811 165.839 151.702 1.00 121.20 ? 4462 ARG A CD    1 
ATOM   23060 N  NE    . ARG A 1 4462 ? 147.375 165.145 150.549 1.00 128.46 ? 4462 ARG A NE    1 
ATOM   23061 C  CZ    . ARG A 1 4462 ? 147.054 163.912 150.180 1.00 124.81 ? 4462 ARG A CZ    1 
ATOM   23062 N  NH1   . ARG A 1 4462 ? 146.157 163.201 150.843 1.00 123.16 ? 4462 ARG A NH1   1 
ATOM   23063 N  NH2   . ARG A 1 4462 ? 147.644 163.381 149.112 1.00 121.31 ? 4462 ARG A NH2   1 
ATOM   23064 N  N     . SER A 1 4463 ? 144.307 163.612 155.256 1.00 108.37 ? 4463 SER A N     1 
ATOM   23065 C  CA    . SER A 1 4463 ? 143.866 162.224 155.336 1.00 102.68 ? 4463 SER A CA    1 
ATOM   23066 C  C     . SER A 1 4463 ? 142.575 162.007 154.562 1.00 94.45  ? 4463 SER A C     1 
ATOM   23067 O  O     . SER A 1 4463 ? 142.346 160.917 154.026 1.00 92.01  ? 4463 SER A O     1 
ATOM   23068 C  CB    . SER A 1 4463 ? 143.689 161.812 156.797 1.00 99.99  ? 4463 SER A CB    1 
ATOM   23069 O  OG    . SER A 1 4463 ? 142.711 162.613 157.436 1.00 100.17 ? 4463 SER A OG    1 
ATOM   23070 N  N     . TRP A 1 4464 ? 141.723 163.026 154.492 1.00 94.56  ? 4464 TRP A N     1 
ATOM   23071 C  CA    . TRP A 1 4464 ? 140.531 162.969 153.663 1.00 100.28 ? 4464 TRP A CA    1 
ATOM   23072 C  C     . TRP A 1 4464 ? 140.908 163.225 152.205 1.00 105.91 ? 4464 TRP A C     1 
ATOM   23073 O  O     . TRP A 1 4464 ? 142.082 163.379 151.857 1.00 111.03 ? 4464 TRP A O     1 
ATOM   23074 C  CB    . TRP A 1 4464 ? 139.491 163.979 154.145 1.00 95.22  ? 4464 TRP A CB    1 
ATOM   23075 C  CG    . TRP A 1 4464 ? 139.058 163.804 155.574 1.00 90.25  ? 4464 TRP A CG    1 
ATOM   23076 C  CD1   . TRP A 1 4464 ? 139.512 162.878 156.466 1.00 89.73  ? 4464 TRP A CD1   1 
ATOM   23077 C  CD2   . TRP A 1 4464 ? 138.075 164.580 156.269 1.00 87.49  ? 4464 TRP A CD2   1 
ATOM   23078 N  NE1   . TRP A 1 4464 ? 138.877 163.031 157.673 1.00 89.19  ? 4464 TRP A NE1   1 
ATOM   23079 C  CE2   . TRP A 1 4464 ? 137.989 164.069 157.578 1.00 87.68  ? 4464 TRP A CE2   1 
ATOM   23080 C  CE3   . TRP A 1 4464 ? 137.260 165.658 155.912 1.00 86.43  ? 4464 TRP A CE3   1 
ATOM   23081 C  CZ2   . TRP A 1 4464 ? 137.121 164.598 158.530 1.00 84.52  ? 4464 TRP A CZ2   1 
ATOM   23082 C  CZ3   . TRP A 1 4464 ? 136.399 166.181 156.858 1.00 85.22  ? 4464 TRP A CZ3   1 
ATOM   23083 C  CH2   . TRP A 1 4464 ? 136.337 165.651 158.151 1.00 84.20  ? 4464 TRP A CH2   1 
ATOM   23084 N  N     . SER A 1 4465 ? 139.894 163.274 151.342 1.00 102.40 ? 4465 SER A N     1 
ATOM   23085 C  CA    . SER A 1 4465 ? 140.073 163.552 149.917 1.00 102.51 ? 4465 SER A CA    1 
ATOM   23086 C  C     . SER A 1 4465 ? 141.009 162.531 149.267 1.00 98.95  ? 4465 SER A C     1 
ATOM   23087 O  O     . SER A 1 4465 ? 142.093 162.857 148.781 1.00 98.88  ? 4465 SER A O     1 
ATOM   23088 C  CB    . SER A 1 4465 ? 140.582 164.980 149.697 1.00 106.03 ? 4465 SER A CB    1 
ATOM   23089 O  OG    . SER A 1 4465 ? 139.604 165.924 150.082 1.00 109.39 ? 4465 SER A OG    1 
ATOM   23090 N  N     . HIS A 1 4466 ? 140.566 161.274 149.271 1.00 98.48  ? 4466 HIS A N     1 
ATOM   23091 C  CA    . HIS A 1 4466 ? 141.325 160.229 148.598 1.00 100.68 ? 4466 HIS A CA    1 
ATOM   23092 C  C     . HIS A 1 4466 ? 141.102 160.241 147.092 1.00 105.25 ? 4466 HIS A C     1 
ATOM   23093 O  O     . HIS A 1 4466 ? 141.789 159.510 146.371 1.00 103.98 ? 4466 HIS A O     1 
ATOM   23094 C  CB    . HIS A 1 4466 ? 140.964 158.860 149.175 1.00 100.35 ? 4466 HIS A CB    1 
ATOM   23095 C  CG    . HIS A 1 4466 ? 141.197 158.748 150.650 1.00 104.00 ? 4466 HIS A CG    1 
ATOM   23096 N  ND1   . HIS A 1 4466 ? 140.255 158.238 151.516 1.00 103.33 ? 4466 HIS A ND1   1 
ATOM   23097 C  CD2   . HIS A 1 4466 ? 142.262 159.090 151.412 1.00 106.29 ? 4466 HIS A CD2   1 
ATOM   23098 C  CE1   . HIS A 1 4466 ? 140.731 158.265 152.748 1.00 103.81 ? 4466 HIS A CE1   1 
ATOM   23099 N  NE2   . HIS A 1 4466 ? 141.948 158.778 152.712 1.00 105.54 ? 4466 HIS A NE2   1 
ATOM   23100 N  N     . TYR A 1 4467 ? 140.165 161.050 146.605 1.00 106.18 ? 4467 TYR A N     1 
ATOM   23101 C  CA    . TYR A 1 4467 ? 139.903 161.193 145.183 1.00 100.76 ? 4467 TYR A CA    1 
ATOM   23102 C  C     . TYR A 1 4467 ? 140.323 162.586 144.719 1.00 98.05  ? 4467 TYR A C     1 
ATOM   23103 O  O     . TYR A 1 4467 ? 140.842 163.398 145.488 1.00 98.95  ? 4467 TYR A O     1 
ATOM   23104 C  CB    . TYR A 1 4467 ? 138.428 160.920 144.884 1.00 98.49  ? 4467 TYR A CB    1 
ATOM   23105 C  CG    . TYR A 1 4467 ? 137.464 161.897 145.522 1.00 100.31 ? 4467 TYR A CG    1 
ATOM   23106 C  CD1   . TYR A 1 4467 ? 136.978 161.685 146.804 1.00 101.26 ? 4467 TYR A CD1   1 
ATOM   23107 C  CD2   . TYR A 1 4467 ? 137.013 163.012 144.830 1.00 97.98  ? 4467 TYR A CD2   1 
ATOM   23108 C  CE1   . TYR A 1 4467 ? 136.091 162.567 147.388 1.00 98.66  ? 4467 TYR A CE1   1 
ATOM   23109 C  CE2   . TYR A 1 4467 ? 136.123 163.898 145.405 1.00 97.07  ? 4467 TYR A CE2   1 
ATOM   23110 C  CZ    . TYR A 1 4467 ? 135.667 163.671 146.685 1.00 97.27  ? 4467 TYR A CZ    1 
ATOM   23111 O  OH    . TYR A 1 4467 ? 134.781 164.549 147.266 1.00 100.83 ? 4467 TYR A OH    1 
ATOM   23112 N  N     . THR A 1 4468 ? 140.096 162.865 143.438 1.00 98.56  ? 4468 THR A N     1 
ATOM   23113 C  CA    . THR A 1 4468 ? 140.521 164.134 142.862 1.00 96.67  ? 4468 THR A CA    1 
ATOM   23114 C  C     . THR A 1 4468 ? 139.557 165.240 143.275 1.00 92.22  ? 4468 THR A C     1 
ATOM   23115 O  O     . THR A 1 4468 ? 138.354 165.158 143.009 1.00 90.91  ? 4468 THR A O     1 
ATOM   23116 C  CB    . THR A 1 4468 ? 140.597 164.030 141.341 1.00 95.63  ? 4468 THR A CB    1 
ATOM   23117 O  OG1   . THR A 1 4468 ? 141.401 162.901 140.978 1.00 96.10  ? 4468 THR A OG1   1 
ATOM   23118 C  CG2   . THR A 1 4468 ? 141.225 165.286 140.763 1.00 93.51  ? 4468 THR A CG2   1 
ATOM   23119 N  N     . VAL A 1 4469 ? 140.087 166.277 143.916 1.00 93.09  ? 4469 VAL A N     1 
ATOM   23120 C  CA    . VAL A 1 4469 ? 139.268 167.374 144.427 1.00 90.32  ? 4469 VAL A CA    1 
ATOM   23121 C  C     . VAL A 1 4469 ? 139.856 168.688 143.933 1.00 89.84  ? 4469 VAL A C     1 
ATOM   23122 O  O     . VAL A 1 4469 ? 141.054 168.774 143.618 1.00 91.96  ? 4469 VAL A O     1 
ATOM   23123 C  CB    . VAL A 1 4469 ? 139.189 167.359 145.972 1.00 94.64  ? 4469 VAL A CB    1 
ATOM   23124 C  CG1   . VAL A 1 4469 ? 138.567 166.069 146.465 1.00 96.49  ? 4469 VAL A CG1   1 
ATOM   23125 C  CG2   . VAL A 1 4469 ? 140.570 167.556 146.580 1.00 94.17  ? 4469 VAL A CG2   1 
ATOM   23126 N  N     . PRO A 1 4470 ? 139.032 169.730 143.836 1.00 83.24  ? 4470 PRO A N     1 
ATOM   23127 C  CA    . PRO A 1 4470 ? 139.565 171.061 143.527 1.00 78.63  ? 4470 PRO A CA    1 
ATOM   23128 C  C     . PRO A 1 4470 ? 140.583 171.505 144.567 1.00 81.88  ? 4470 PRO A C     1 
ATOM   23129 O  O     . PRO A 1 4470 ? 140.460 171.203 145.755 1.00 88.80  ? 4470 PRO A O     1 
ATOM   23130 C  CB    . PRO A 1 4470 ? 138.319 171.950 143.541 1.00 77.51  ? 4470 PRO A CB    1 
ATOM   23131 C  CG    . PRO A 1 4470 ? 137.212 171.029 143.175 1.00 78.84  ? 4470 PRO A CG    1 
ATOM   23132 C  CD    . PRO A 1 4470 ? 137.561 169.696 143.774 1.00 80.50  ? 4470 PRO A CD    1 
ATOM   23133 N  N     . ALA A 1 4471 ? 141.604 172.220 144.103 1.00 84.54  ? 4471 ALA A N     1 
ATOM   23134 C  CA    . ALA A 1 4471 ? 142.673 172.668 144.986 1.00 91.37  ? 4471 ALA A CA    1 
ATOM   23135 C  C     . ALA A 1 4471 ? 142.204 173.829 145.854 1.00 97.77  ? 4471 ALA A C     1 
ATOM   23136 O  O     . ALA A 1 4471 ? 141.460 174.701 145.396 1.00 100.68 ? 4471 ALA A O     1 
ATOM   23137 C  CB    . ALA A 1 4471 ? 143.895 173.079 144.168 1.00 90.92  ? 4471 ALA A CB    1 
ATOM   23138 N  N     . GLY A 1 4472 ? 142.641 173.836 147.112 1.00 102.03 ? 4472 GLY A N     1 
ATOM   23139 C  CA    . GLY A 1 4472 ? 142.348 174.932 148.013 1.00 101.16 ? 4472 GLY A CA    1 
ATOM   23140 C  C     . GLY A 1 4472 ? 140.925 174.996 148.515 1.00 104.05 ? 4472 GLY A C     1 
ATOM   23141 O  O     . GLY A 1 4472 ? 140.537 176.013 149.100 1.00 103.82 ? 4472 GLY A O     1 
ATOM   23142 N  N     . MET A 1 4473 ? 140.135 173.948 148.309 1.00 102.31 ? 4473 MET A N     1 
ATOM   23143 C  CA    . MET A 1 4473 ? 138.732 173.982 148.693 1.00 99.17  ? 4473 MET A CA    1 
ATOM   23144 C  C     . MET A 1 4473 ? 138.583 173.726 150.189 1.00 105.75 ? 4473 MET A C     1 
ATOM   23145 O  O     . MET A 1 4473 ? 139.352 172.968 150.787 1.00 105.70 ? 4473 MET A O     1 
ATOM   23146 C  CB    . MET A 1 4473 ? 137.949 172.951 147.884 1.00 93.18  ? 4473 MET A CB    1 
ATOM   23147 C  CG    . MET A 1 4473 ? 138.331 171.513 148.162 1.00 94.11  ? 4473 MET A CG    1 
ATOM   23148 S  SD    . MET A 1 4473 ? 137.361 170.380 147.159 1.00 108.54 ? 4473 MET A SD    1 
ATOM   23149 C  CE    . MET A 1 4473 ? 135.763 170.523 147.932 1.00 98.17  ? 4473 MET A CE    1 
ATOM   23150 N  N     . THR A 1 4474 ? 137.591 174.371 150.794 1.00 106.75 ? 4474 THR A N     1 
ATOM   23151 C  CA    . THR A 1 4474 ? 137.387 174.297 152.232 1.00 99.77  ? 4474 THR A CA    1 
ATOM   23152 C  C     . THR A 1 4474 ? 136.700 172.990 152.622 1.00 95.63  ? 4474 THR A C     1 
ATOM   23153 O  O     . THR A 1 4474 ? 136.297 172.187 151.778 1.00 95.75  ? 4474 THR A O     1 
ATOM   23154 C  CB    . THR A 1 4474 ? 136.571 175.494 152.720 1.00 97.78  ? 4474 THR A CB    1 
ATOM   23155 O  OG1   . THR A 1 4474 ? 135.283 175.488 152.094 1.00 106.81 ? 4474 THR A OG1   1 
ATOM   23156 C  CG2   . THR A 1 4474 ? 137.286 176.794 152.390 1.00 88.68  ? 4474 THR A CG2   1 
ATOM   23157 N  N     . VAL A 1 4475 ? 136.576 172.782 153.934 1.00 96.19  ? 4475 VAL A N     1 
ATOM   23158 C  CA    . VAL A 1 4475 ? 136.013 171.534 154.439 1.00 99.51  ? 4475 VAL A CA    1 
ATOM   23159 C  C     . VAL A 1 4475 ? 134.509 171.485 154.197 1.00 103.03 ? 4475 VAL A C     1 
ATOM   23160 O  O     . VAL A 1 4475 ? 133.947 170.417 153.931 1.00 104.77 ? 4475 VAL A O     1 
ATOM   23161 C  CB    . VAL A 1 4475 ? 136.349 171.359 155.931 1.00 96.90  ? 4475 VAL A CB    1 
ATOM   23162 C  CG1   . VAL A 1 4475 ? 135.745 170.074 156.462 1.00 97.19  ? 4475 VAL A CG1   1 
ATOM   23163 C  CG2   . VAL A 1 4475 ? 137.840 171.372 156.148 1.00 94.46  ? 4475 VAL A CG2   1 
ATOM   23164 N  N     . ILE A 1 4476 ? 133.830 172.629 154.307 1.00 99.39  ? 4476 ILE A N     1 
ATOM   23165 C  CA    . ILE A 1 4476 ? 132.374 172.651 154.176 1.00 98.84  ? 4476 ILE A CA    1 
ATOM   23166 C  C     . ILE A 1 4476 ? 131.957 172.268 152.760 1.00 102.31 ? 4476 ILE A C     1 
ATOM   23167 O  O     . ILE A 1 4476 ? 131.044 171.454 152.556 1.00 106.50 ? 4476 ILE A O     1 
ATOM   23168 C  CB    . ILE A 1 4476 ? 131.823 174.031 154.570 1.00 99.38  ? 4476 ILE A CB    1 
ATOM   23169 C  CG1   . ILE A 1 4476 ? 132.110 174.326 156.044 1.00 95.18  ? 4476 ILE A CG1   1 
ATOM   23170 C  CG2   . ILE A 1 4476 ? 130.336 174.092 154.302 1.00 102.15 ? 4476 ILE A CG2   1 
ATOM   23171 C  CD1   . ILE A 1 4476 ? 133.318 175.213 156.270 1.00 90.82  ? 4476 ILE A CD1   1 
ATOM   23172 N  N     . GLN A 1 4477 ? 132.615 172.856 151.759 1.00 97.13  ? 4477 GLN A N     1 
ATOM   23173 C  CA    . GLN A 1 4477 ? 132.344 172.473 150.379 1.00 96.53  ? 4477 GLN A CA    1 
ATOM   23174 C  C     . GLN A 1 4477 ? 132.626 170.994 150.166 1.00 96.92  ? 4477 GLN A C     1 
ATOM   23175 O  O     . GLN A 1 4477 ? 131.871 170.301 149.472 1.00 100.20 ? 4477 GLN A O     1 
ATOM   23176 C  CB    . GLN A 1 4477 ? 133.187 173.321 149.427 1.00 97.90  ? 4477 GLN A CB    1 
ATOM   23177 C  CG    . GLN A 1 4477 ? 132.826 174.794 149.422 1.00 109.75 ? 4477 GLN A CG    1 
ATOM   23178 C  CD    . GLN A 1 4477 ? 133.705 175.604 148.490 1.00 112.62 ? 4477 GLN A CD    1 
ATOM   23179 O  OE1   . GLN A 1 4477 ? 134.636 175.076 147.882 1.00 109.36 ? 4477 GLN A OE1   1 
ATOM   23180 N  NE2   . GLN A 1 4477 ? 133.413 176.894 148.373 1.00 109.31 ? 4477 GLN A NE2   1 
ATOM   23181 N  N     . TRP A 1 4478 ? 133.703 170.492 150.772 1.00 95.55  ? 4478 TRP A N     1 
ATOM   23182 C  CA    . TRP A 1 4478 ? 134.069 169.095 150.588 1.00 94.08  ? 4478 TRP A CA    1 
ATOM   23183 C  C     . TRP A 1 4478 ? 133.024 168.167 151.184 1.00 92.51  ? 4478 TRP A C     1 
ATOM   23184 O  O     . TRP A 1 4478 ? 132.681 167.151 150.577 1.00 91.38  ? 4478 TRP A O     1 
ATOM   23185 C  CB    . TRP A 1 4478 ? 135.447 168.827 151.193 1.00 95.90  ? 4478 TRP A CB    1 
ATOM   23186 C  CG    . TRP A 1 4478 ? 135.992 167.465 150.877 1.00 98.90  ? 4478 TRP A CG    1 
ATOM   23187 C  CD1   . TRP A 1 4478 ? 136.941 167.169 149.947 1.00 102.55 ? 4478 TRP A CD1   1 
ATOM   23188 C  CD2   . TRP A 1 4478 ? 135.654 166.223 151.513 1.00 99.73  ? 4478 TRP A CD2   1 
ATOM   23189 N  NE1   . TRP A 1 4478 ? 137.201 165.822 149.944 1.00 103.61 ? 4478 TRP A NE1   1 
ATOM   23190 C  CE2   . TRP A 1 4478 ? 136.426 165.219 150.899 1.00 98.85  ? 4478 TRP A CE2   1 
ATOM   23191 C  CE3   . TRP A 1 4478 ? 134.772 165.863 152.535 1.00 102.30 ? 4478 TRP A CE3   1 
ATOM   23192 C  CZ2   . TRP A 1 4478 ? 136.340 163.881 151.270 1.00 96.82  ? 4478 TRP A CZ2   1 
ATOM   23193 C  CZ3   . TRP A 1 4478 ? 134.687 164.535 152.900 1.00 100.27 ? 4478 TRP A CZ3   1 
ATOM   23194 C  CH2   . TRP A 1 4478 ? 135.467 163.560 152.270 1.00 97.09  ? 4478 TRP A CH2   1 
ATOM   23195 N  N     . VAL A 1 4479 ? 132.503 168.494 152.366 1.00 93.61  ? 4479 VAL A N     1 
ATOM   23196 C  CA    . VAL A 1 4479 ? 131.525 167.612 152.994 1.00 97.01  ? 4479 VAL A CA    1 
ATOM   23197 C  C     . VAL A 1 4479 ? 130.190 167.683 152.261 1.00 97.25  ? 4479 VAL A C     1 
ATOM   23198 O  O     . VAL A 1 4479 ? 129.488 166.673 152.135 1.00 96.27  ? 4479 VAL A O     1 
ATOM   23199 C  CB    . VAL A 1 4479 ? 131.386 167.924 154.496 1.00 93.52  ? 4479 VAL A CB    1 
ATOM   23200 C  CG1   . VAL A 1 4479 ? 132.714 167.701 155.203 1.00 88.06  ? 4479 VAL A CG1   1 
ATOM   23201 C  CG2   . VAL A 1 4479 ? 130.890 169.332 154.725 1.00 91.62  ? 4479 VAL A CG2   1 
ATOM   23202 N  N     . SER A 1 4480 ? 129.826 168.861 151.743 1.00 96.73  ? 4480 SER A N     1 
ATOM   23203 C  CA    . SER A 1 4480 ? 128.616 168.951 150.927 1.00 97.92  ? 4480 SER A CA    1 
ATOM   23204 C  C     . SER A 1 4480 ? 128.738 168.094 149.669 1.00 98.24  ? 4480 SER A C     1 
ATOM   23205 O  O     . SER A 1 4480 ? 127.839 167.300 149.345 1.00 97.54  ? 4480 SER A O     1 
ATOM   23206 C  CB    . SER A 1 4480 ? 128.342 170.410 150.562 1.00 96.44  ? 4480 SER A CB    1 
ATOM   23207 O  OG    . SER A 1 4480 ? 128.089 171.187 151.719 1.00 100.98 ? 4480 SER A OG    1 
ATOM   23208 N  N     . ASP A 1 4481 ? 129.859 168.233 148.955 1.00 97.95  ? 4481 ASP A N     1 
ATOM   23209 C  CA    . ASP A 1 4481 ? 130.076 167.439 147.751 1.00 93.75  ? 4481 ASP A CA    1 
ATOM   23210 C  C     . ASP A 1 4481 ? 130.136 165.954 148.079 1.00 91.91  ? 4481 ASP A C     1 
ATOM   23211 O  O     . ASP A 1 4481 ? 129.634 165.124 147.316 1.00 91.93  ? 4481 ASP A O     1 
ATOM   23212 C  CB    . ASP A 1 4481 ? 131.360 167.887 147.053 1.00 95.25  ? 4481 ASP A CB    1 
ATOM   23213 C  CG    . ASP A 1 4481 ? 131.246 169.277 146.461 1.00 102.54 ? 4481 ASP A CG    1 
ATOM   23214 O  OD1   . ASP A 1 4481 ? 130.123 169.676 146.086 1.00 104.93 ? 4481 ASP A OD1   1 
ATOM   23215 O  OD2   . ASP A 1 4481 ? 132.279 169.972 146.372 1.00 103.80 ? 4481 ASP A OD2   1 
ATOM   23216 N  N     . PHE A 1 4482 ? 130.754 165.602 149.207 1.00 93.62  ? 4482 PHE A N     1 
ATOM   23217 C  CA    . PHE A 1 4482 ? 130.830 164.209 149.625 1.00 95.32  ? 4482 PHE A CA    1 
ATOM   23218 C  C     . PHE A 1 4482 ? 129.447 163.638 149.895 1.00 95.53  ? 4482 PHE A C     1 
ATOM   23219 O  O     . PHE A 1 4482 ? 129.148 162.505 149.502 1.00 93.45  ? 4482 PHE A O     1 
ATOM   23220 C  CB    . PHE A 1 4482 ? 131.711 164.095 150.868 1.00 93.90  ? 4482 PHE A CB    1 
ATOM   23221 C  CG    . PHE A 1 4482 ? 132.099 162.689 151.210 1.00 95.70  ? 4482 PHE A CG    1 
ATOM   23222 C  CD1   . PHE A 1 4482 ? 132.022 162.237 152.515 1.00 92.43  ? 4482 PHE A CD1   1 
ATOM   23223 C  CD2   . PHE A 1 4482 ? 132.538 161.819 150.229 1.00 97.73  ? 4482 PHE A CD2   1 
ATOM   23224 C  CE1   . PHE A 1 4482 ? 132.377 160.946 152.834 1.00 94.98  ? 4482 PHE A CE1   1 
ATOM   23225 C  CE2   . PHE A 1 4482 ? 132.893 160.526 150.543 1.00 95.58  ? 4482 PHE A CE2   1 
ATOM   23226 C  CZ    . PHE A 1 4482 ? 132.813 160.089 151.847 1.00 96.74  ? 4482 PHE A CZ    1 
ATOM   23227 N  N     . SER A 1 4483 ? 128.589 164.407 150.570 1.00 92.36  ? 4483 SER A N     1 
ATOM   23228 C  CA    . SER A 1 4483 ? 127.227 163.950 150.813 1.00 94.81  ? 4483 SER A CA    1 
ATOM   23229 C  C     . SER A 1 4483 ? 126.487 163.720 149.503 1.00 101.83 ? 4483 SER A C     1 
ATOM   23230 O  O     . SER A 1 4483 ? 125.815 162.694 149.333 1.00 102.45 ? 4483 SER A O     1 
ATOM   23231 C  CB    . SER A 1 4483 ? 126.483 164.964 151.680 1.00 94.98  ? 4483 SER A CB    1 
ATOM   23232 O  OG    . SER A 1 4483 ? 126.399 166.221 151.032 1.00 89.79  ? 4483 SER A OG    1 
ATOM   23233 N  N     . GLU A 1 4484 ? 126.613 164.655 148.556 1.00 101.39 ? 4484 GLU A N     1 
ATOM   23234 C  CA    . GLU A 1 4484 ? 125.948 164.474 147.266 1.00 91.17  ? 4484 GLU A CA    1 
ATOM   23235 C  C     . GLU A 1 4484 ? 126.481 163.247 146.531 1.00 92.28  ? 4484 GLU A C     1 
ATOM   23236 O  O     . GLU A 1 4484 ? 125.705 162.462 145.968 1.00 94.23  ? 4484 GLU A O     1 
ATOM   23237 C  CB    . GLU A 1 4484 ? 126.107 165.728 146.407 1.00 93.97  ? 4484 GLU A CB    1 
ATOM   23238 C  CG    . GLU A 1 4484 ? 125.536 166.988 147.038 1.00 100.55 ? 4484 GLU A CG    1 
ATOM   23239 C  CD    . GLU A 1 4484 ? 126.164 168.255 146.489 1.00 103.61 ? 4484 GLU A CD    1 
ATOM   23240 O  OE1   . GLU A 1 4484 ? 127.345 168.210 146.086 1.00 101.19 ? 4484 GLU A OE1   1 
ATOM   23241 O  OE2   . GLU A 1 4484 ? 125.476 169.297 146.463 1.00 106.51 ? 4484 GLU A OE2   1 
ATOM   23242 N  N     . ARG A 1 4485 ? 127.805 163.059 146.536 1.00 95.26  ? 4485 ARG A N     1 
ATOM   23243 C  CA    . ARG A 1 4485 ? 128.404 161.917 145.852 1.00 95.13  ? 4485 ARG A CA    1 
ATOM   23244 C  C     . ARG A 1 4485 ? 127.942 160.602 146.463 1.00 98.09  ? 4485 ARG A C     1 
ATOM   23245 O  O     . ARG A 1 4485 ? 127.632 159.650 145.739 1.00 95.16  ? 4485 ARG A O     1 
ATOM   23246 C  CB    . ARG A 1 4485 ? 129.929 162.008 145.904 1.00 91.22  ? 4485 ARG A CB    1 
ATOM   23247 C  CG    . ARG A 1 4485 ? 130.536 163.146 145.107 1.00 92.02  ? 4485 ARG A CG    1 
ATOM   23248 C  CD    . ARG A 1 4485 ? 131.928 163.476 145.631 1.00 94.93  ? 4485 ARG A CD    1 
ATOM   23249 N  NE    . ARG A 1 4485 ? 132.640 164.423 144.783 1.00 92.12  ? 4485 ARG A NE    1 
ATOM   23250 C  CZ    . ARG A 1 4485 ? 133.163 164.129 143.601 1.00 85.29  ? 4485 ARG A CZ    1 
ATOM   23251 N  NH1   . ARG A 1 4485 ? 133.083 162.910 143.093 1.00 85.90  ? 4485 ARG A NH1   1 
ATOM   23252 N  NH2   . ARG A 1 4485 ? 133.789 165.080 142.914 1.00 83.69  ? 4485 ARG A NH2   1 
ATOM   23253 N  N     . ILE A 1 4486 ? 127.900 160.523 147.795 1.00 97.72  ? 4486 ILE A N     1 
ATOM   23254 C  CA    . ILE A 1 4486 ? 127.498 159.279 148.442 1.00 98.51  ? 4486 ILE A CA    1 
ATOM   23255 C  C     . ILE A 1 4486 ? 126.010 159.018 148.236 1.00 102.08 ? 4486 ILE A C     1 
ATOM   23256 O  O     . ILE A 1 4486 ? 125.590 157.861 148.121 1.00 101.07 ? 4486 ILE A O     1 
ATOM   23257 C  CB    . ILE A 1 4486 ? 127.881 159.297 149.932 1.00 99.05  ? 4486 ILE A CB    1 
ATOM   23258 C  CG1   . ILE A 1 4486 ? 129.390 159.485 150.087 1.00 95.24  ? 4486 ILE A CG1   1 
ATOM   23259 C  CG2   . ILE A 1 4486 ? 127.484 157.993 150.596 1.00 104.37 ? 4486 ILE A CG2   1 
ATOM   23260 C  CD1   . ILE A 1 4486 ? 130.213 158.385 149.462 1.00 95.05  ? 4486 ILE A CD1   1 
ATOM   23261 N  N     . LYS A 1 4487 ? 125.186 160.070 148.186 1.00 101.30 ? 4487 LYS A N     1 
ATOM   23262 C  CA    . LYS A 1 4487 ? 123.780 159.873 147.841 1.00 98.51  ? 4487 LYS A CA    1 
ATOM   23263 C  C     . LYS A 1 4487 ? 123.637 159.318 146.427 1.00 102.47 ? 4487 LYS A C     1 
ATOM   23264 O  O     . LYS A 1 4487 ? 122.831 158.409 146.183 1.00 102.34 ? 4487 LYS A O     1 
ATOM   23265 C  CB    . LYS A 1 4487 ? 123.014 161.187 147.986 1.00 93.03  ? 4487 LYS A CB    1 
ATOM   23266 C  CG    . LYS A 1 4487 ? 122.401 161.398 149.359 1.00 97.86  ? 4487 LYS A CG    1 
ATOM   23267 C  CD    . LYS A 1 4487 ? 121.653 162.720 149.437 1.00 95.15  ? 4487 LYS A CD    1 
ATOM   23268 C  CE    . LYS A 1 4487 ? 122.553 163.837 149.940 1.00 91.01  ? 4487 LYS A CE    1 
ATOM   23269 N  NZ    . LYS A 1 4487 ? 122.104 165.175 149.463 1.00 91.20  ? 4487 LYS A NZ    1 
ATOM   23270 N  N     . GLN A 1 4488 ? 124.421 159.847 145.484 1.00 101.51 ? 4488 GLN A N     1 
ATOM   23271 C  CA    . GLN A 1 4488 ? 124.414 159.303 144.129 1.00 97.94  ? 4488 GLN A CA    1 
ATOM   23272 C  C     . GLN A 1 4488 ? 124.873 157.850 144.119 1.00 98.78  ? 4488 GLN A C     1 
ATOM   23273 O  O     . GLN A 1 4488 ? 124.338 157.024 143.369 1.00 101.82 ? 4488 GLN A O     1 
ATOM   23274 C  CB    . GLN A 1 4488 ? 125.302 160.151 143.220 1.00 94.23  ? 4488 GLN A CB    1 
ATOM   23275 C  CG    . GLN A 1 4488 ? 125.587 159.523 141.867 1.00 96.32  ? 4488 GLN A CG    1 
ATOM   23276 C  CD    . GLN A 1 4488 ? 126.640 160.280 141.087 1.00 91.42  ? 4488 GLN A CD    1 
ATOM   23277 O  OE1   . GLN A 1 4488 ? 126.487 161.468 140.810 1.00 92.51  ? 4488 GLN A OE1   1 
ATOM   23278 N  NE2   . GLN A 1 4488 ? 127.717 159.594 140.725 1.00 85.91  ? 4488 GLN A NE2   1 
ATOM   23279 N  N     . LEU A 1 4489 ? 125.874 157.525 144.938 1.00 97.53  ? 4489 LEU A N     1 
ATOM   23280 C  CA    . LEU A 1 4489 ? 126.359 156.151 145.011 1.00 101.66 ? 4489 LEU A CA    1 
ATOM   23281 C  C     . LEU A 1 4489 ? 125.301 155.218 145.586 1.00 108.39 ? 4489 LEU A C     1 
ATOM   23282 O  O     . LEU A 1 4489 ? 125.169 154.077 145.138 1.00 110.34 ? 4489 LEU A O     1 
ATOM   23283 C  CB    . LEU A 1 4489 ? 127.646 156.086 145.832 1.00 104.47 ? 4489 LEU A CB    1 
ATOM   23284 C  CG    . LEU A 1 4489 ? 128.883 156.742 145.214 1.00 97.09  ? 4489 LEU A CG    1 
ATOM   23285 C  CD1   . LEU A 1 4489 ? 130.131 156.397 146.008 1.00 93.44  ? 4489 LEU A CD1   1 
ATOM   23286 C  CD2   . LEU A 1 4489 ? 129.041 156.330 143.761 1.00 95.54  ? 4489 LEU A CD2   1 
ATOM   23287 N  N     . GLN A 1 4490 ? 124.541 155.674 146.584 1.00 108.56 ? 4490 GLN A N     1 
ATOM   23288 C  CA    . GLN A 1 4490 ? 123.434 154.861 147.082 1.00 108.87 ? 4490 GLN A CA    1 
ATOM   23289 C  C     . GLN A 1 4490 ? 122.366 154.667 146.015 1.00 107.97 ? 4490 GLN A C     1 
ATOM   23290 O  O     . GLN A 1 4490 ? 121.794 153.577 145.892 1.00 107.15 ? 4490 GLN A O     1 
ATOM   23291 C  CB    . GLN A 1 4490 ? 122.818 155.476 148.336 1.00 104.29 ? 4490 GLN A CB    1 
ATOM   23292 C  CG    . GLN A 1 4490 ? 123.703 155.414 149.556 1.00 110.02 ? 4490 GLN A CG    1 
ATOM   23293 C  CD    . GLN A 1 4490 ? 123.151 156.213 150.712 1.00 109.17 ? 4490 GLN A CD    1 
ATOM   23294 O  OE1   . GLN A 1 4490 ? 123.720 156.216 151.799 1.00 106.23 ? 4490 GLN A OE1   1 
ATOM   23295 N  NE2   . GLN A 1 4490 ? 122.033 156.893 150.486 1.00 101.47 ? 4490 GLN A NE2   1 
ATOM   23296 N  N     . ASN A 1 4491 ? 122.069 155.716 145.246 1.00 109.58 ? 4491 ASN A N     1 
ATOM   23297 C  CA    . ASN A 1 4491 ? 121.096 155.568 144.167 1.00 110.52 ? 4491 ASN A CA    1 
ATOM   23298 C  C     . ASN A 1 4491 ? 121.565 154.543 143.141 1.00 107.54 ? 4491 ASN A C     1 
ATOM   23299 O  O     . ASN A 1 4491 ? 120.788 153.680 142.714 1.00 106.58 ? 4491 ASN A O     1 
ATOM   23300 C  CB    . ASN A 1 4491 ? 120.836 156.920 143.503 1.00 108.44 ? 4491 ASN A CB    1 
ATOM   23301 C  CG    . ASN A 1 4491 ? 119.958 157.821 144.346 1.00 107.19 ? 4491 ASN A CG    1 
ATOM   23302 O  OD1   . ASN A 1 4491 ? 118.961 157.379 144.917 1.00 108.03 ? 4491 ASN A OD1   1 
ATOM   23303 N  ND2   . ASN A 1 4491 ? 120.325 159.094 144.430 1.00 102.34 ? 4491 ASN A ND2   1 
ATOM   23304 N  N     . ILE A 1 4492 ? 122.842 154.606 142.752 1.00 108.71 ? 4492 ILE A N     1 
ATOM   23305 C  CA    . ILE A 1 4492 ? 123.360 153.648 141.779 1.00 114.07 ? 4492 ILE A CA    1 
ATOM   23306 C  C     . ILE A 1 4492 ? 123.421 152.245 142.377 1.00 118.20 ? 4492 ILE A C     1 
ATOM   23307 O  O     . ILE A 1 4492 ? 123.219 151.254 141.666 1.00 121.72 ? 4492 ILE A O     1 
ATOM   23308 C  CB    . ILE A 1 4492 ? 124.727 154.105 141.226 1.00 106.37 ? 4492 ILE A CB    1 
ATOM   23309 C  CG1   . ILE A 1 4492 ? 124.988 153.469 139.861 1.00 99.66  ? 4492 ILE A CG1   1 
ATOM   23310 C  CG2   . ILE A 1 4492 ? 125.864 153.754 142.166 1.00 104.43 ? 4492 ILE A CG2   1 
ATOM   23311 C  CD1   . ILE A 1 4492 ? 124.059 153.946 138.781 1.00 99.89  ? 4492 ILE A CD1   1 
ATOM   23312 N  N     . SER A 1 4493 ? 123.678 152.130 143.683 1.00 110.97 ? 4493 SER A N     1 
ATOM   23313 C  CA    . SER A 1 4493 ? 123.687 150.819 144.322 1.00 112.66 ? 4493 SER A CA    1 
ATOM   23314 C  C     . SER A 1 4493 ? 122.295 150.203 144.337 1.00 119.47 ? 4493 SER A C     1 
ATOM   23315 O  O     . SER A 1 4493 ? 122.135 149.008 144.064 1.00 121.77 ? 4493 SER A O     1 
ATOM   23316 C  CB    . SER A 1 4493 ? 124.242 150.931 145.741 1.00 112.47 ? 4493 SER A CB    1 
ATOM   23317 O  OG    . SER A 1 4493 ? 124.396 149.652 146.330 1.00 116.71 ? 4493 SER A OG    1 
ATOM   23318 N  N     . LEU A 1 4494 ? 121.278 151.006 144.653 1.00 117.83 ? 4494 LEU A N     1 
ATOM   23319 C  CA    . LEU A 1 4494 ? 119.905 150.516 144.602 1.00 120.47 ? 4494 LEU A CA    1 
ATOM   23320 C  C     . LEU A 1 4494 ? 119.520 150.132 143.179 1.00 121.75 ? 4494 LEU A C     1 
ATOM   23321 O  O     . LEU A 1 4494 ? 118.840 149.122 142.963 1.00 123.37 ? 4494 LEU A O     1 
ATOM   23322 C  CB    . LEU A 1 4494 ? 118.953 151.572 145.168 1.00 120.18 ? 4494 LEU A CB    1 
ATOM   23323 C  CG    . LEU A 1 4494 ? 117.485 151.205 145.412 1.00 125.66 ? 4494 LEU A CG    1 
ATOM   23324 C  CD1   . LEU A 1 4494 ? 116.934 152.030 146.562 1.00 121.35 ? 4494 LEU A CD1   1 
ATOM   23325 C  CD2   . LEU A 1 4494 ? 116.636 151.420 144.167 1.00 122.30 ? 4494 LEU A CD2   1 
ATOM   23326 N  N     . ALA A 1 4495 ? 119.946 150.928 142.196 1.00 120.00 ? 4495 ALA A N     1 
ATOM   23327 C  CA    . ALA A 1 4495 ? 119.660 150.612 140.801 1.00 121.92 ? 4495 ALA A CA    1 
ATOM   23328 C  C     . ALA A 1 4495 ? 120.306 149.293 140.393 1.00 124.97 ? 4495 ALA A C     1 
ATOM   23329 O  O     . ALA A 1 4495 ? 119.705 148.482 139.679 1.00 129.62 ? 4495 ALA A O     1 
ATOM   23330 C  CB    . ALA A 1 4495 ? 120.139 151.752 139.900 1.00 118.14 ? 4495 ALA A CB    1 
ATOM   23331 N  N     . ALA A 1 4496 ? 121.544 149.063 140.835 1.00 121.56 ? 4496 ALA A N     1 
ATOM   23332 C  CA    . ALA A 1 4496 ? 122.233 147.822 140.506 1.00 126.00 ? 4496 ALA A CA    1 
ATOM   23333 C  C     . ALA A 1 4496 ? 121.636 146.621 141.224 1.00 131.60 ? 4496 ALA A C     1 
ATOM   23334 O  O     . ALA A 1 4496 ? 121.615 145.522 140.659 1.00 132.64 ? 4496 ALA A O     1 
ATOM   23335 C  CB    . ALA A 1 4496 ? 123.720 147.940 140.841 1.00 117.03 ? 4496 ALA A CB    1 
ATOM   23336 N  N     . ALA A 1 4497 ? 121.149 146.802 142.452 1.00 132.07 ? 4497 ALA A N     1 
ATOM   23337 C  CA    . ALA A 1 4497 ? 120.632 145.672 143.216 1.00 133.00 ? 4497 ALA A CA    1 
ATOM   23338 C  C     . ALA A 1 4497 ? 119.217 145.300 142.787 1.00 134.11 ? 4497 ALA A C     1 
ATOM   23339 O  O     . ALA A 1 4497 ? 118.942 144.137 142.475 1.00 131.92 ? 4497 ALA A O     1 
ATOM   23340 C  CB    . ALA A 1 4497 ? 120.672 145.988 144.712 1.00 131.03 ? 4497 ALA A CB    1 
ATOM   23341 N  N     . SER A 1 4498 ? 118.308 146.274 142.760 1.00 134.80 ? 4498 SER A N     1 
ATOM   23342 C  CA    . SER A 1 4498 ? 116.899 146.016 142.484 1.00 135.55 ? 4498 SER A CA    1 
ATOM   23343 C  C     . SER A 1 4498 ? 116.523 146.257 141.026 1.00 136.06 ? 4498 SER A C     1 
ATOM   23344 O  O     . SER A 1 4498 ? 115.729 145.501 140.459 1.00 130.58 ? 4498 SER A O     1 
ATOM   23345 C  CB    . SER A 1 4498 ? 116.023 146.881 143.398 1.00 126.88 ? 4498 SER A CB    1 
ATOM   23346 O  OG    . SER A 1 4498 ? 116.291 148.258 143.205 1.00 124.95 ? 4498 SER A OG    1 
ATOM   23347 N  N     . GLY A 1 4499 ? 117.076 147.295 140.406 1.00 135.67 ? 4499 GLY A N     1 
ATOM   23348 C  CA    . GLY A 1 4499 ? 116.731 147.624 139.039 1.00 135.50 ? 4499 GLY A CA    1 
ATOM   23349 C  C     . GLY A 1 4499 ? 117.355 146.755 137.974 1.00 142.51 ? 4499 GLY A C     1 
ATOM   23350 O  O     . GLY A 1 4499 ? 116.952 146.838 136.810 1.00 145.45 ? 4499 GLY A O     1 
ATOM   23351 N  N     . GLY A 1 4500 ? 118.322 145.918 138.328 1.00 139.47 ? 4500 GLY A N     1 
ATOM   23352 C  CA    . GLY A 1 4500 ? 118.976 145.058 137.367 1.00 136.83 ? 4500 GLY A CA    1 
ATOM   23353 C  C     . GLY A 1 4500 ? 120.184 145.722 136.725 1.00 131.56 ? 4500 GLY A C     1 
ATOM   23354 O  O     . GLY A 1 4500 ? 120.412 146.929 136.844 1.00 125.62 ? 4500 GLY A O     1 
ATOM   23355 N  N     . ALA A 1 4501 ? 120.979 144.902 136.033 1.00 131.96 ? 4501 ALA A N     1 
ATOM   23356 C  CA    . ALA A 1 4501 ? 122.187 145.408 135.390 1.00 126.31 ? 4501 ALA A CA    1 
ATOM   23357 C  C     . ALA A 1 4501 ? 121.856 146.355 134.243 1.00 124.18 ? 4501 ALA A C     1 
ATOM   23358 O  O     . ALA A 1 4501 ? 122.481 147.414 134.107 1.00 120.22 ? 4501 ALA A O     1 
ATOM   23359 C  CB    . ALA A 1 4501 ? 123.043 144.244 134.893 1.00 120.09 ? 4501 ALA A CB    1 
ATOM   23360 N  N     . LYS A 1 4502 ? 120.874 145.995 133.413 1.00 121.82 ? 4502 LYS A N     1 
ATOM   23361 C  CA    . LYS A 1 4502 ? 120.529 146.815 132.257 1.00 118.22 ? 4502 LYS A CA    1 
ATOM   23362 C  C     . LYS A 1 4502 ? 120.039 148.201 132.654 1.00 113.66 ? 4502 LYS A C     1 
ATOM   23363 O  O     . LYS A 1 4502 ? 120.191 149.145 131.870 1.00 107.19 ? 4502 LYS A O     1 
ATOM   23364 C  CB    . LYS A 1 4502 ? 119.471 146.108 131.410 1.00 117.32 ? 4502 LYS A CB    1 
ATOM   23365 C  CG    . LYS A 1 4502 ? 119.969 144.837 130.740 1.00 114.96 ? 4502 LYS A CG    1 
ATOM   23366 C  CD    . LYS A 1 4502 ? 118.857 144.144 129.972 1.00 110.02 ? 4502 LYS A CD    1 
ATOM   23367 C  CE    . LYS A 1 4502 ? 117.739 143.708 130.902 1.00 109.25 ? 4502 LYS A CE    1 
ATOM   23368 N  NZ    . LYS A 1 4502 ? 118.229 142.783 131.960 1.00 109.24 ? 4502 LYS A NZ    1 
ATOM   23369 N  N     . GLU A 1 4503 ? 119.464 148.345 133.851 1.00 115.79 ? 4503 GLU A N     1 
ATOM   23370 C  CA    . GLU A 1 4503 ? 119.070 149.662 134.334 1.00 113.91 ? 4503 GLU A CA    1 
ATOM   23371 C  C     . GLU A 1 4503 ? 120.256 150.609 134.440 1.00 108.58 ? 4503 GLU A C     1 
ATOM   23372 O  O     . GLU A 1 4503 ? 120.081 151.822 134.280 1.00 109.55 ? 4503 GLU A O     1 
ATOM   23373 C  CB    . GLU A 1 4503 ? 118.372 149.539 135.690 1.00 119.55 ? 4503 GLU A CB    1 
ATOM   23374 C  CG    . GLU A 1 4503 ? 117.745 150.830 136.196 1.00 124.67 ? 4503 GLU A CG    1 
ATOM   23375 C  CD    . GLU A 1 4503 ? 116.603 151.312 135.320 1.00 123.44 ? 4503 GLU A CD    1 
ATOM   23376 O  OE1   . GLU A 1 4503 ? 115.952 150.469 134.668 1.00 123.76 ? 4503 GLU A OE1   1 
ATOM   23377 O  OE2   . GLU A 1 4503 ? 116.358 152.536 135.281 1.00 115.43 ? 4503 GLU A OE2   1 
ATOM   23378 N  N     . LEU A 1 4504 ? 121.460 150.082 134.686 1.00 105.99 ? 4504 LEU A N     1 
ATOM   23379 C  CA    . LEU A 1 4504 ? 122.649 150.924 134.708 1.00 102.26 ? 4504 LEU A CA    1 
ATOM   23380 C  C     . LEU A 1 4504 ? 122.875 151.621 133.375 1.00 101.14 ? 4504 LEU A C     1 
ATOM   23381 O  O     . LEU A 1 4504 ? 123.540 152.662 133.336 1.00 103.05 ? 4504 LEU A O     1 
ATOM   23382 C  CB    . LEU A 1 4504 ? 123.878 150.094 135.078 1.00 99.22  ? 4504 LEU A CB    1 
ATOM   23383 C  CG    . LEU A 1 4504 ? 123.860 149.423 136.452 1.00 103.43 ? 4504 LEU A CG    1 
ATOM   23384 C  CD1   . LEU A 1 4504 ? 124.953 148.372 136.549 1.00 102.96 ? 4504 LEU A CD1   1 
ATOM   23385 C  CD2   . LEU A 1 4504 ? 124.004 150.452 137.560 1.00 99.99  ? 4504 LEU A CD2   1 
ATOM   23386 N  N     . LYS A 1 4505 ? 122.341 151.070 132.284 1.00 96.25  ? 4505 LYS A N     1 
ATOM   23387 C  CA    . LYS A 1 4505 ? 122.421 151.746 130.996 1.00 89.49  ? 4505 LYS A CA    1 
ATOM   23388 C  C     . LYS A 1 4505 ? 121.425 152.896 130.912 1.00 96.50  ? 4505 LYS A C     1 
ATOM   23389 O  O     . LYS A 1 4505 ? 121.721 153.934 130.311 1.00 99.28  ? 4505 LYS A O     1 
ATOM   23390 C  CB    . LYS A 1 4505 ? 122.184 150.742 129.866 1.00 86.71  ? 4505 LYS A CB    1 
ATOM   23391 C  CG    . LYS A 1 4505 ? 122.311 151.318 128.464 1.00 80.62  ? 4505 LYS A CG    1 
ATOM   23392 C  CD    . LYS A 1 4505 ? 120.965 151.688 127.866 1.00 89.75  ? 4505 LYS A CD    1 
ATOM   23393 C  CE    . LYS A 1 4505 ? 121.126 152.310 126.490 1.00 84.41  ? 4505 LYS A CE    1 
ATOM   23394 N  NZ    . LYS A 1 4505 ? 119.829 152.775 125.928 1.00 90.04  ? 4505 LYS A NZ    1 
ATOM   23395 N  N     . ASN A 1 4506 ? 120.245 152.731 131.510 1.00 99.46  ? 4506 ASN A N     1 
ATOM   23396 C  CA    . ASN A 1 4506 ? 119.181 153.720 131.407 1.00 94.00  ? 4506 ASN A CA    1 
ATOM   23397 C  C     . ASN A 1 4506 ? 119.219 154.773 132.506 1.00 92.38  ? 4506 ASN A C     1 
ATOM   23398 O  O     . ASN A 1 4506 ? 118.410 155.705 132.471 1.00 97.01  ? 4506 ASN A O     1 
ATOM   23399 C  CB    . ASN A 1 4506 ? 117.813 153.031 131.422 1.00 94.51  ? 4506 ASN A CB    1 
ATOM   23400 C  CG    . ASN A 1 4506 ? 117.771 151.801 130.542 1.00 99.24  ? 4506 ASN A CG    1 
ATOM   23401 O  OD1   . ASN A 1 4506 ? 117.549 150.688 131.019 1.00 104.20 ? 4506 ASN A OD1   1 
ATOM   23402 N  ND2   . ASN A 1 4506 ? 117.975 151.996 129.245 1.00 94.03  ? 4506 ASN A ND2   1 
ATOM   23403 N  N     . ILE A 1 4507 ? 120.119 154.652 133.473 1.00 86.97  ? 4507 ILE A N     1 
ATOM   23404 C  CA    . ILE A 1 4507 ? 120.202 155.635 134.546 1.00 90.64  ? 4507 ILE A CA    1 
ATOM   23405 C  C     . ILE A 1 4507 ? 121.077 156.798 134.099 1.00 92.13  ? 4507 ILE A C     1 
ATOM   23406 O  O     . ILE A 1 4507 ? 122.081 156.614 133.399 1.00 92.89  ? 4507 ILE A O     1 
ATOM   23407 C  CB    . ILE A 1 4507 ? 120.727 154.988 135.841 1.00 90.75  ? 4507 ILE A CB    1 
ATOM   23408 C  CG1   . ILE A 1 4507 ? 120.574 155.956 137.017 1.00 94.91  ? 4507 ILE A CG1   1 
ATOM   23409 C  CG2   . ILE A 1 4507 ? 122.172 154.542 135.687 1.00 87.64  ? 4507 ILE A CG2   1 
ATOM   23410 C  CD1   . ILE A 1 4507 ? 120.753 155.311 138.368 1.00 100.19 ? 4507 ILE A CD1   1 
ATOM   23411 N  N     . HIS A 1 4508 ? 120.681 158.008 134.483 1.00 84.99  ? 4508 HIS A N     1 
ATOM   23412 C  CA    . HIS A 1 4508 ? 121.439 159.208 134.164 1.00 74.92  ? 4508 HIS A CA    1 
ATOM   23413 C  C     . HIS A 1 4508 ? 122.463 159.456 135.263 1.00 75.52  ? 4508 HIS A C     1 
ATOM   23414 O  O     . HIS A 1 4508 ? 122.108 159.548 136.442 1.00 84.49  ? 4508 HIS A O     1 
ATOM   23415 C  CB    . HIS A 1 4508 ? 120.509 160.409 134.013 1.00 74.10  ? 4508 HIS A CB    1 
ATOM   23416 C  CG    . HIS A 1 4508 ? 119.373 160.172 133.068 1.00 78.60  ? 4508 HIS A CG    1 
ATOM   23417 N  ND1   . HIS A 1 4508 ? 119.556 159.681 131.794 1.00 76.42  ? 4508 HIS A ND1   1 
ATOM   23418 C  CD2   . HIS A 1 4508 ? 118.040 160.363 133.210 1.00 85.17  ? 4508 HIS A CD2   1 
ATOM   23419 C  CE1   . HIS A 1 4508 ? 118.385 159.575 131.193 1.00 83.55  ? 4508 HIS A CE1   1 
ATOM   23420 N  NE2   . HIS A 1 4508 ? 117.449 159.983 132.030 1.00 90.87  ? 4508 HIS A NE2   1 
ATOM   23421 N  N     . VAL A 1 4509 ? 123.728 159.567 134.872 1.00 69.22  ? 4509 VAL A N     1 
ATOM   23422 C  CA    . VAL A 1 4509 ? 124.846 159.615 135.805 1.00 71.07  ? 4509 VAL A CA    1 
ATOM   23423 C  C     . VAL A 1 4509 ? 125.415 161.025 135.814 1.00 68.38  ? 4509 VAL A C     1 
ATOM   23424 O  O     . VAL A 1 4509 ? 125.682 161.601 134.752 1.00 73.84  ? 4509 VAL A O     1 
ATOM   23425 C  CB    . VAL A 1 4509 ? 125.931 158.592 135.428 1.00 71.24  ? 4509 VAL A CB    1 
ATOM   23426 C  CG1   . VAL A 1 4509 ? 127.083 158.662 136.409 1.00 71.83  ? 4509 VAL A CG1   1 
ATOM   23427 C  CG2   . VAL A 1 4509 ? 125.346 157.192 135.375 1.00 73.86  ? 4509 VAL A CG2   1 
ATOM   23428 N  N     . CYS A 1 4510 ? 125.600 161.580 137.007 1.00 66.81  ? 4510 CYS A N     1 
ATOM   23429 C  CA    . CYS A 1 4510 ? 126.244 162.876 137.169 1.00 72.43  ? 4510 CYS A CA    1 
ATOM   23430 C  C     . CYS A 1 4510 ? 127.754 162.674 137.200 1.00 76.27  ? 4510 CYS A C     1 
ATOM   23431 O  O     . CYS A 1 4510 ? 128.286 162.092 138.152 1.00 79.64  ? 4510 CYS A O     1 
ATOM   23432 C  CB    . CYS A 1 4510 ? 125.762 163.565 138.445 1.00 74.87  ? 4510 CYS A CB    1 
ATOM   23433 S  SG    . CYS A 1 4510 ? 126.370 165.251 138.663 1.00 92.90  ? 4510 CYS A SG    1 
ATOM   23434 N  N     . LEU A 1 4511 ? 128.441 163.151 136.158 1.00 68.95  ? 4511 LEU A N     1 
ATOM   23435 C  CA    . LEU A 1 4511 ? 129.883 162.948 136.062 1.00 67.31  ? 4511 LEU A CA    1 
ATOM   23436 C  C     . LEU A 1 4511 ? 130.626 163.601 137.218 1.00 73.71  ? 4511 LEU A C     1 
ATOM   23437 O  O     . LEU A 1 4511 ? 131.705 163.137 137.601 1.00 75.28  ? 4511 LEU A O     1 
ATOM   23438 C  CB    . LEU A 1 4511 ? 130.405 163.486 134.730 1.00 66.17  ? 4511 LEU A CB    1 
ATOM   23439 C  CG    . LEU A 1 4511 ? 130.105 162.666 133.475 1.00 61.48  ? 4511 LEU A CG    1 
ATOM   23440 C  CD1   . LEU A 1 4511 ? 131.073 163.024 132.363 1.00 58.38  ? 4511 LEU A CD1   1 
ATOM   23441 C  CD2   . LEU A 1 4511 ? 130.168 161.185 133.777 1.00 57.91  ? 4511 LEU A CD2   1 
ATOM   23442 N  N     . GLY A 1 4512 ? 130.078 164.681 137.778 1.00 76.33  ? 4512 GLY A N     1 
ATOM   23443 C  CA    . GLY A 1 4512 ? 130.724 165.319 138.912 1.00 74.37  ? 4512 GLY A CA    1 
ATOM   23444 C  C     . GLY A 1 4512 ? 130.779 164.423 140.133 1.00 84.80  ? 4512 GLY A C     1 
ATOM   23445 O  O     . GLY A 1 4512 ? 131.761 164.430 140.877 1.00 89.52  ? 4512 GLY A O     1 
ATOM   23446 N  N     . GLY A 1 4513 ? 129.722 163.640 140.357 1.00 84.15  ? 4513 GLY A N     1 
ATOM   23447 C  CA    . GLY A 1 4513 ? 129.697 162.758 141.512 1.00 87.54  ? 4513 GLY A CA    1 
ATOM   23448 C  C     . GLY A 1 4513 ? 130.727 161.648 141.432 1.00 89.61  ? 4513 GLY A C     1 
ATOM   23449 O  O     . GLY A 1 4513 ? 131.311 161.257 142.447 1.00 94.17  ? 4513 GLY A O     1 
ATOM   23450 N  N     . LEU A 1 4514 ? 130.962 161.123 140.231 1.00 81.94  ? 4514 LEU A N     1 
ATOM   23451 C  CA    . LEU A 1 4514 ? 131.903 160.025 140.062 1.00 81.24  ? 4514 LEU A CA    1 
ATOM   23452 C  C     . LEU A 1 4514 ? 133.315 160.458 140.435 1.00 82.60  ? 4514 LEU A C     1 
ATOM   23453 O  O     . LEU A 1 4514 ? 133.709 161.606 140.216 1.00 84.03  ? 4514 LEU A O     1 
ATOM   23454 C  CB    . LEU A 1 4514 ? 131.878 159.526 138.619 1.00 75.67  ? 4514 LEU A CB    1 
ATOM   23455 C  CG    . LEU A 1 4514 ? 130.519 159.132 138.046 1.00 75.09  ? 4514 LEU A CG    1 
ATOM   23456 C  CD1   . LEU A 1 4514 ? 130.646 158.855 136.563 1.00 67.64  ? 4514 LEU A CD1   1 
ATOM   23457 C  CD2   . LEU A 1 4514 ? 129.954 157.927 138.772 1.00 78.79  ? 4514 LEU A CD2   1 
ATOM   23458 N  N     . PHE A 1 4515 ? 134.077 159.527 141.012 1.00 82.16  ? 4515 PHE A N     1 
ATOM   23459 C  CA    . PHE A 1 4515 ? 135.478 159.798 141.313 1.00 85.70  ? 4515 PHE A CA    1 
ATOM   23460 C  C     . PHE A 1 4515 ? 136.347 159.765 140.061 1.00 83.46  ? 4515 PHE A C     1 
ATOM   23461 O  O     . PHE A 1 4515 ? 137.281 160.565 139.942 1.00 82.46  ? 4515 PHE A O     1 
ATOM   23462 C  CB    . PHE A 1 4515 ? 136.000 158.796 142.345 1.00 92.56  ? 4515 PHE A CB    1 
ATOM   23463 C  CG    . PHE A 1 4515 ? 135.195 158.754 143.614 1.00 96.71  ? 4515 PHE A CG    1 
ATOM   23464 C  CD1   . PHE A 1 4515 ? 135.079 159.877 144.414 1.00 92.88  ? 4515 PHE A CD1   1 
ATOM   23465 C  CD2   . PHE A 1 4515 ? 134.554 157.590 144.005 1.00 96.59  ? 4515 PHE A CD2   1 
ATOM   23466 C  CE1   . PHE A 1 4515 ? 134.340 159.841 145.581 1.00 91.46  ? 4515 PHE A CE1   1 
ATOM   23467 C  CE2   . PHE A 1 4515 ? 133.813 157.549 145.169 1.00 96.25  ? 4515 PHE A CE2   1 
ATOM   23468 C  CZ    . PHE A 1 4515 ? 133.706 158.676 145.958 1.00 95.62  ? 4515 PHE A CZ    1 
ATOM   23469 N  N     . VAL A 1 4516 ? 136.064 158.859 139.129 1.00 81.78  ? 4516 VAL A N     1 
ATOM   23470 C  CA    . VAL A 1 4516 ? 136.802 158.767 137.869 1.00 76.92  ? 4516 VAL A CA    1 
ATOM   23471 C  C     . VAL A 1 4516 ? 135.827 158.754 136.692 1.00 69.53  ? 4516 VAL A C     1 
ATOM   23472 O  O     . VAL A 1 4516 ? 135.551 157.695 136.111 1.00 69.87  ? 4516 VAL A O     1 
ATOM   23473 C  CB    . VAL A 1 4516 ? 137.752 157.554 137.873 1.00 75.29  ? 4516 VAL A CB    1 
ATOM   23474 C  CG1   . VAL A 1 4516 ? 138.815 157.735 138.937 1.00 80.52  ? 4516 VAL A CG1   1 
ATOM   23475 C  CG2   . VAL A 1 4516 ? 137.003 156.263 138.180 1.00 78.51  ? 4516 VAL A CG2   1 
ATOM   23476 N  N     . PRO A 1 4517 ? 135.285 159.911 136.304 1.00 58.97  ? 4517 PRO A N     1 
ATOM   23477 C  CA    . PRO A 1 4517 ? 134.327 159.932 135.185 1.00 56.36  ? 4517 PRO A CA    1 
ATOM   23478 C  C     . PRO A 1 4517 ? 134.918 159.497 133.854 1.00 63.58  ? 4517 PRO A C     1 
ATOM   23479 O  O     . PRO A 1 4517 ? 134.179 159.005 132.991 1.00 64.85  ? 4517 PRO A O     1 
ATOM   23480 C  CB    . PRO A 1 4517 ? 133.868 161.396 135.150 1.00 59.34  ? 4517 PRO A CB    1 
ATOM   23481 C  CG    . PRO A 1 4517 ? 134.970 162.153 135.799 1.00 61.92  ? 4517 PRO A CG    1 
ATOM   23482 C  CD    . PRO A 1 4517 ? 135.534 161.254 136.850 1.00 59.24  ? 4517 PRO A CD    1 
ATOM   23483 N  N     . GLU A 1 4518 ? 136.226 159.672 133.650 1.00 65.24  ? 4518 GLU A N     1 
ATOM   23484 C  CA    . GLU A 1 4518 ? 136.843 159.207 132.412 1.00 61.94  ? 4518 GLU A CA    1 
ATOM   23485 C  C     . GLU A 1 4518 ? 136.740 157.692 132.285 1.00 61.96  ? 4518 GLU A C     1 
ATOM   23486 O  O     . GLU A 1 4518 ? 136.536 157.161 131.184 1.00 62.09  ? 4518 GLU A O     1 
ATOM   23487 C  CB    . GLU A 1 4518 ? 138.296 159.681 132.346 1.00 65.78  ? 4518 GLU A CB    1 
ATOM   23488 C  CG    . GLU A 1 4518 ? 139.209 159.099 133.409 1.00 79.37  ? 4518 GLU A CG    1 
ATOM   23489 C  CD    . GLU A 1 4518 ? 140.617 159.658 133.336 1.00 100.53 ? 4518 GLU A CD    1 
ATOM   23490 O  OE1   . GLU A 1 4518 ? 140.874 160.518 132.467 1.00 92.64  ? 4518 GLU A OE1   1 
ATOM   23491 O  OE2   . GLU A 1 4518 ? 141.466 159.239 134.151 1.00 110.90 ? 4518 GLU A OE2   1 
ATOM   23492 N  N     . ALA A 1 4519 ? 136.853 156.978 133.408 1.00 65.62  ? 4519 ALA A N     1 
ATOM   23493 C  CA    . ALA A 1 4519 ? 136.586 155.546 133.398 1.00 62.32  ? 4519 ALA A CA    1 
ATOM   23494 C  C     . ALA A 1 4519 ? 135.140 155.258 133.024 1.00 59.87  ? 4519 ALA A C     1 
ATOM   23495 O  O     . ALA A 1 4519 ? 134.862 154.256 132.357 1.00 57.24  ? 4519 ALA A O     1 
ATOM   23496 C  CB    . ALA A 1 4519 ? 136.918 154.937 134.758 1.00 66.02  ? 4519 ALA A CB    1 
ATOM   23497 N  N     . TYR A 1 4520 ? 134.208 156.124 133.430 1.00 58.91  ? 4520 TYR A N     1 
ATOM   23498 C  CA    . TYR A 1 4520 ? 132.819 155.950 133.016 1.00 59.81  ? 4520 TYR A CA    1 
ATOM   23499 C  C     . TYR A 1 4520 ? 132.674 156.098 131.510 1.00 58.04  ? 4520 TYR A C     1 
ATOM   23500 O  O     . TYR A 1 4520 ? 131.961 155.322 130.868 1.00 59.81  ? 4520 TYR A O     1 
ATOM   23501 C  CB    . TYR A 1 4520 ? 131.908 156.947 133.727 1.00 60.36  ? 4520 TYR A CB    1 
ATOM   23502 C  CG    . TYR A 1 4520 ? 130.487 156.895 133.213 1.00 62.17  ? 4520 TYR A CG    1 
ATOM   23503 C  CD1   . TYR A 1 4520 ? 129.694 155.777 133.425 1.00 67.46  ? 4520 TYR A CD1   1 
ATOM   23504 C  CD2   . TYR A 1 4520 ? 129.949 157.950 132.491 1.00 61.38  ? 4520 TYR A CD2   1 
ATOM   23505 C  CE1   . TYR A 1 4520 ? 128.401 155.718 132.949 1.00 69.15  ? 4520 TYR A CE1   1 
ATOM   23506 C  CE2   . TYR A 1 4520 ? 128.656 157.900 132.010 1.00 62.71  ? 4520 TYR A CE2   1 
ATOM   23507 C  CZ    . TYR A 1 4520 ? 127.887 156.782 132.242 1.00 67.27  ? 4520 TYR A CZ    1 
ATOM   23508 O  OH    . TYR A 1 4520 ? 126.598 156.727 131.766 1.00 72.11  ? 4520 TYR A OH    1 
ATOM   23509 N  N     . ILE A 1 4521 ? 133.335 157.115 130.950 1.00 58.49  ? 4521 ILE A N     1 
ATOM   23510 C  CA    . ILE A 1 4521 ? 133.260 157.357 129.477 1.00 53.95  ? 4521 ILE A CA    1 
ATOM   23511 C  C     . ILE A 1 4521 ? 133.874 156.146 128.758 1.00 53.36  ? 4521 ILE A C     1 
ATOM   23512 O  O     . ILE A 1 4521 ? 133.332 155.742 127.706 1.00 53.37  ? 4521 ILE A O     1 
ATOM   23513 C  CB    . ILE A 1 4521 ? 133.976 158.667 129.101 1.00 55.52  ? 4521 ILE A CB    1 
ATOM   23514 C  CG1   . ILE A 1 4521 ? 133.574 159.816 130.026 1.00 54.20  ? 4521 ILE A CG1   1 
ATOM   23515 C  CG2   . ILE A 1 4521 ? 133.744 159.015 127.630 1.00 54.24  ? 4521 ILE A CG2   1 
ATOM   23516 C  CD1   . ILE A 1 4521 ? 132.082 160.091 130.059 1.00 56.66  ? 4521 ILE A CD1   1 
ATOM   23517 N  N     . THR A 1 4522 ? 134.962 155.597 129.305 1.00 54.88  ? 4522 THR A N     1 
ATOM   23518 C  CA    . THR A 1 4522 ? 135.600 154.408 128.702 1.00 51.30  ? 4522 THR A CA    1 
ATOM   23519 C  C     . THR A 1 4522 ? 134.624 153.253 128.756 1.00 56.12  ? 4522 THR A C     1 
ATOM   23520 O  O     . THR A 1 4522 ? 134.444 152.580 127.718 1.00 55.92  ? 4522 THR A O     1 
ATOM   23521 C  CB    . THR A 1 4522 ? 136.890 154.091 129.456 1.00 51.63  ? 4522 THR A CB    1 
ATOM   23522 O  OG1   . THR A 1 4522 ? 137.681 155.271 129.356 1.00 52.75  ? 4522 THR A OG1   1 
ATOM   23523 C  CG2   . THR A 1 4522 ? 137.634 152.908 128.862 1.00 54.10  ? 4522 THR A CG2   1 
ATOM   23524 N  N     . ALA A 1 4523 ? 134.002 153.036 129.918 1.00 58.17  ? 4523 ALA A N     1 
ATOM   23525 C  CA    . ALA A 1 4523 ? 133.028 151.930 130.080 1.00 56.38  ? 4523 ALA A CA    1 
ATOM   23526 C  C     . ALA A 1 4523 ? 131.916 152.075 129.040 1.00 55.85  ? 4523 ALA A C     1 
ATOM   23527 O  O     . ALA A 1 4523 ? 131.630 151.092 128.322 1.00 58.38  ? 4523 ALA A O     1 
ATOM   23528 C  CB    . ALA A 1 4523 ? 132.474 151.936 131.487 1.00 60.23  ? 4523 ALA A CB    1 
ATOM   23529 N  N     . THR A 1 4524 ? 131.314 153.265 128.957 1.00 54.79  ? 4524 THR A N     1 
ATOM   23530 C  CA    . THR A 1 4524 ? 130.226 153.490 128.008 1.00 50.39  ? 4524 THR A CA    1 
ATOM   23531 C  C     . THR A 1 4524 ? 130.642 153.110 126.593 1.00 53.40  ? 4524 THR A C     1 
ATOM   23532 O  O     . THR A 1 4524 ? 129.875 152.471 125.856 1.00 58.28  ? 4524 THR A O     1 
ATOM   23533 C  CB    . THR A 1 4524 ? 129.790 154.952 128.055 1.00 49.10  ? 4524 THR A CB    1 
ATOM   23534 O  OG1   . THR A 1 4524 ? 130.889 155.796 127.694 1.00 53.63  ? 4524 THR A OG1   1 
ATOM   23535 C  CG2   . THR A 1 4524 ? 129.305 155.320 129.444 1.00 59.12  ? 4524 THR A CG2   1 
ATOM   23536 N  N     . ARG A 1 4525 ? 131.856 153.507 126.203 1.00 53.20  ? 4525 ARG A N     1 
ATOM   23537 C  CA    . ARG A 1 4525 ? 132.337 153.212 124.828 1.00 48.71  ? 4525 ARG A CA    1 
ATOM   23538 C  C     . ARG A 1 4525 ? 132.382 151.689 124.632 1.00 54.48  ? 4525 ARG A C     1 
ATOM   23539 O  O     . ARG A 1 4525 ? 131.840 151.206 123.613 1.00 57.31  ? 4525 ARG A O     1 
ATOM   23540 C  CB    . ARG A 1 4525 ? 133.717 153.831 124.583 1.00 49.11  ? 4525 ARG A CB    1 
ATOM   23541 C  CG    . ARG A 1 4525 ? 134.135 153.784 123.121 1.00 50.83  ? 4525 ARG A CG    1 
ATOM   23542 C  CD    . ARG A 1 4525 ? 135.506 154.402 122.905 1.00 50.81  ? 4525 ARG A CD    1 
ATOM   23543 N  NE    . ARG A 1 4525 ? 135.885 154.431 121.489 1.00 54.83  ? 4525 ARG A NE    1 
ATOM   23544 C  CZ    . ARG A 1 4525 ? 137.031 154.917 121.032 1.00 58.15  ? 4525 ARG A CZ    1 
ATOM   23545 N  NH1   . ARG A 1 4525 ? 137.913 155.429 121.872 1.00 64.93  ? 4525 ARG A NH1   1 
ATOM   23546 N  NH2   . ARG A 1 4525 ? 137.293 154.887 119.738 1.00 58.89  ? 4525 ARG A NH2   1 
ATOM   23547 N  N     . GLN A 1 4526 ? 132.997 150.969 125.575 1.00 59.71  ? 4526 GLN A N     1 
ATOM   23548 C  CA    . GLN A 1 4526 ? 133.110 149.491 125.468 1.00 59.39  ? 4526 GLN A CA    1 
ATOM   23549 C  C     . GLN A 1 4526 ? 131.701 148.880 125.444 1.00 63.85  ? 4526 GLN A C     1 
ATOM   23550 O  O     . GLN A 1 4526 ? 131.452 148.003 124.589 1.00 67.63  ? 4526 GLN A O     1 
ATOM   23551 C  CB    . GLN A 1 4526 ? 133.938 148.955 126.636 1.00 53.91  ? 4526 GLN A CB    1 
ATOM   23552 C  CG    . GLN A 1 4526 ? 135.318 149.593 126.750 1.00 54.40  ? 4526 GLN A CG    1 
ATOM   23553 C  CD    . GLN A 1 4526 ? 136.091 149.133 127.966 1.00 56.54  ? 4526 GLN A CD    1 
ATOM   23554 O  OE1   . GLN A 1 4526 ? 136.446 149.929 128.842 1.00 58.24  ? 4526 GLN A OE1   1 
ATOM   23555 N  NE2   . GLN A 1 4526 ? 136.356 147.837 128.032 1.00 60.65  ? 4526 GLN A NE2   1 
ATOM   23556 N  N     . TYR A 1 4527 ? 130.820 149.331 126.341 1.00 61.86  ? 4527 TYR A N     1 
ATOM   23557 C  CA    . TYR A 1 4527 ? 129.417 148.836 126.354 1.00 63.61  ? 4527 TYR A CA    1 
ATOM   23558 C  C     . TYR A 1 4527 ? 128.870 148.896 124.934 1.00 64.28  ? 4527 TYR A C     1 
ATOM   23559 O  O     . TYR A 1 4527 ? 128.476 147.845 124.384 1.00 67.89  ? 4527 TYR A O     1 
ATOM   23560 C  CB    . TYR A 1 4527 ? 128.588 149.695 127.312 1.00 65.11  ? 4527 TYR A CB    1 
ATOM   23561 C  CG    . TYR A 1 4527 ? 127.121 149.303 127.413 1.00 72.47  ? 4527 TYR A CG    1 
ATOM   23562 C  CD1   . TYR A 1 4527 ? 126.678 148.423 128.393 1.00 84.93  ? 4527 TYR A CD1   1 
ATOM   23563 C  CD2   . TYR A 1 4527 ? 126.181 149.805 126.521 1.00 70.60  ? 4527 TYR A CD2   1 
ATOM   23564 C  CE1   . TYR A 1 4527 ? 125.345 148.062 128.488 1.00 85.53  ? 4527 TYR A CE1   1 
ATOM   23565 C  CE2   . TYR A 1 4527 ? 124.845 149.452 126.606 1.00 74.93  ? 4527 TYR A CE2   1 
ATOM   23566 C  CZ    . TYR A 1 4527 ? 124.426 148.577 127.592 1.00 83.57  ? 4527 TYR A CZ    1 
ATOM   23567 O  OH    . TYR A 1 4527 ? 123.110 148.225 127.679 1.00 86.05  ? 4527 TYR A OH    1 
ATOM   23568 N  N     . VAL A 1 4528 ? 128.847 150.097 124.349 1.00 63.45  ? 4528 VAL A N     1 
ATOM   23569 C  CA    . VAL A 1 4528 ? 128.344 150.269 122.989 1.00 61.50  ? 4528 VAL A CA    1 
ATOM   23570 C  C     . VAL A 1 4528 ? 129.038 149.301 122.038 1.00 68.21  ? 4528 VAL A C     1 
ATOM   23571 O  O     . VAL A 1 4528 ? 128.389 148.644 121.212 1.00 76.12  ? 4528 VAL A O     1 
ATOM   23572 C  CB    . VAL A 1 4528 ? 128.512 151.729 122.532 1.00 55.38  ? 4528 VAL A CB    1 
ATOM   23573 C  CG1   . VAL A 1 4528 ? 128.110 151.872 121.077 1.00 54.99  ? 4528 VAL A CG1   1 
ATOM   23574 C  CG2   . VAL A 1 4528 ? 127.693 152.656 123.409 1.00 57.20  ? 4528 VAL A CG2   1 
ATOM   23575 N  N     . ALA A 1 4529 ? 130.365 149.181 122.154 1.00 63.52  ? 4529 ALA A N     1 
ATOM   23576 C  CA    . ALA A 1 4529 ? 131.111 148.300 121.260 1.00 64.78  ? 4529 ALA A CA    1 
ATOM   23577 C  C     . ALA A 1 4529 ? 130.687 146.846 121.425 1.00 73.65  ? 4529 ALA A C     1 
ATOM   23578 O  O     . ALA A 1 4529 ? 130.518 146.125 120.436 1.00 71.63  ? 4529 ALA A O     1 
ATOM   23579 C  CB    . ALA A 1 4529 ? 132.610 148.453 121.514 1.00 63.44  ? 4529 ALA A CB    1 
ATOM   23580 N  N     . GLN A 1 4530 ? 130.515 146.398 122.670 1.00 79.70  ? 4530 GLN A N     1 
ATOM   23581 C  CA    . GLN A 1 4530 ? 130.121 145.018 122.928 1.00 81.01  ? 4530 GLN A CA    1 
ATOM   23582 C  C     . GLN A 1 4530 ? 128.700 144.747 122.454 1.00 81.69  ? 4530 GLN A C     1 
ATOM   23583 O  O     . GLN A 1 4530 ? 128.436 143.715 121.827 1.00 83.15  ? 4530 GLN A O     1 
ATOM   23584 C  CB    . GLN A 1 4530 ? 130.258 144.713 124.419 1.00 78.66  ? 4530 GLN A CB    1 
ATOM   23585 C  CG    . GLN A 1 4530 ? 129.551 143.449 124.872 1.00 88.92  ? 4530 GLN A CG    1 
ATOM   23586 C  CD    . GLN A 1 4530 ? 129.840 143.113 126.321 1.00 104.30 ? 4530 GLN A CD    1 
ATOM   23587 O  OE1   . GLN A 1 4530 ? 130.343 143.945 127.076 1.00 102.08 ? 4530 GLN A OE1   1 
ATOM   23588 N  NE2   . GLN A 1 4530 ? 129.522 141.886 126.718 1.00 109.90 ? 4530 GLN A NE2   1 
ATOM   23589 N  N     . ALA A 1 4531 ? 127.769 145.661 122.744 1.00 78.60  ? 4531 ALA A N     1 
ATOM   23590 C  CA    . ALA A 1 4531 ? 126.382 145.456 122.348 1.00 74.29  ? 4531 ALA A CA    1 
ATOM   23591 C  C     . ALA A 1 4531 ? 126.233 145.430 120.833 1.00 74.57  ? 4531 ALA A C     1 
ATOM   23592 O  O     . ALA A 1 4531 ? 125.483 144.608 120.294 1.00 78.82  ? 4531 ALA A O     1 
ATOM   23593 C  CB    . ALA A 1 4531 ? 125.499 146.542 122.958 1.00 72.78  ? 4531 ALA A CB    1 
ATOM   23594 N  N     . ASN A 1 4532 ? 126.936 146.313 120.127 1.00 75.92  ? 4532 ASN A N     1 
ATOM   23595 C  CA    . ASN A 1 4532 ? 126.815 146.402 118.679 1.00 81.93  ? 4532 ASN A CA    1 
ATOM   23596 C  C     . ASN A 1 4532 ? 127.857 145.567 117.945 1.00 82.21  ? 4532 ASN A C     1 
ATOM   23597 O  O     . ASN A 1 4532 ? 127.912 145.613 116.712 1.00 78.34  ? 4532 ASN A O     1 
ATOM   23598 C  CB    . ASN A 1 4532 ? 126.900 147.862 118.236 1.00 83.18  ? 4532 ASN A CB    1 
ATOM   23599 C  CG    . ASN A 1 4532 ? 125.763 148.700 118.781 1.00 86.66  ? 4532 ASN A CG    1 
ATOM   23600 O  OD1   . ASN A 1 4532 ? 125.405 148.590 119.953 1.00 86.44  ? 4532 ASN A OD1   1 
ATOM   23601 N  ND2   . ASN A 1 4532 ? 125.185 149.539 117.932 1.00 89.95  ? 4532 ASN A ND2   1 
ATOM   23602 N  N     . SER A 1 4533 ? 128.674 144.803 118.674 1.00 80.74  ? 4533 SER A N     1 
ATOM   23603 C  CA    . SER A 1 4533 ? 129.732 143.976 118.086 1.00 82.73  ? 4533 SER A CA    1 
ATOM   23604 C  C     . SER A 1 4533 ? 130.687 144.816 117.242 1.00 84.06  ? 4533 SER A C     1 
ATOM   23605 O  O     . SER A 1 4533 ? 131.161 144.384 116.190 1.00 79.98  ? 4533 SER A O     1 
ATOM   23606 C  CB    . SER A 1 4533 ? 129.151 142.826 117.261 1.00 83.62  ? 4533 SER A CB    1 
ATOM   23607 O  OG    . SER A 1 4533 ? 128.552 143.305 116.069 1.00 87.15  ? 4533 SER A OG    1 
ATOM   23608 N  N     . TRP A 1 4534 ? 130.971 146.026 117.711 1.00 83.06  ? 4534 TRP A N     1 
ATOM   23609 C  CA    . TRP A 1 4534 ? 131.852 146.956 117.023 1.00 72.28  ? 4534 TRP A CA    1 
ATOM   23610 C  C     . TRP A 1 4534 ? 133.210 146.996 117.710 1.00 69.19  ? 4534 TRP A C     1 
ATOM   23611 O  O     . TRP A 1 4534 ? 133.319 146.794 118.921 1.00 76.63  ? 4534 TRP A O     1 
ATOM   23612 C  CB    . TRP A 1 4534 ? 131.250 148.364 116.995 1.00 74.20  ? 4534 TRP A CB    1 
ATOM   23613 C  CG    . TRP A 1 4534 ? 130.070 148.513 116.083 1.00 83.55  ? 4534 TRP A CG    1 
ATOM   23614 C  CD1   . TRP A 1 4534 ? 129.740 147.714 115.029 1.00 81.32  ? 4534 TRP A CD1   1 
ATOM   23615 C  CD2   . TRP A 1 4534 ? 129.063 149.532 116.143 1.00 85.39  ? 4534 TRP A CD2   1 
ATOM   23616 N  NE1   . TRP A 1 4534 ? 128.591 148.169 114.431 1.00 81.96  ? 4534 TRP A NE1   1 
ATOM   23617 C  CE2   . TRP A 1 4534 ? 128.155 149.284 115.096 1.00 84.84  ? 4534 TRP A CE2   1 
ATOM   23618 C  CE3   . TRP A 1 4534 ? 128.839 150.627 116.983 1.00 77.60  ? 4534 TRP A CE3   1 
ATOM   23619 C  CZ2   . TRP A 1 4534 ? 127.043 150.091 114.866 1.00 84.63  ? 4534 TRP A CZ2   1 
ATOM   23620 C  CZ3   . TRP A 1 4534 ? 127.736 151.427 116.752 1.00 81.49  ? 4534 TRP A CZ3   1 
ATOM   23621 C  CH2   . TRP A 1 4534 ? 126.852 151.155 115.702 1.00 87.51  ? 4534 TRP A CH2   1 
ATOM   23622 N  N     . SER A 1 4535 ? 134.249 147.247 116.922 1.00 66.01  ? 4535 SER A N     1 
ATOM   23623 C  CA    . SER A 1 4535 ? 135.575 147.413 117.496 1.00 61.28  ? 4535 SER A CA    1 
ATOM   23624 C  C     . SER A 1 4535 ? 135.660 148.752 118.218 1.00 56.09  ? 4535 SER A C     1 
ATOM   23625 O  O     . SER A 1 4535 ? 135.070 149.746 117.789 1.00 62.06  ? 4535 SER A O     1 
ATOM   23626 C  CB    . SER A 1 4535 ? 136.645 147.315 116.415 1.00 61.14  ? 4535 SER A CB    1 
ATOM   23627 O  OG    . SER A 1 4535 ? 137.934 147.405 116.988 1.00 63.55  ? 4535 SER A OG    1 
ATOM   23628 N  N     . LEU A 1 4536 ? 136.407 148.771 119.323 1.00 50.95  ? 4536 LEU A N     1 
ATOM   23629 C  CA    . LEU A 1 4536 ? 136.341 149.895 120.252 1.00 49.15  ? 4536 LEU A CA    1 
ATOM   23630 C  C     . LEU A 1 4536 ? 136.838 151.197 119.633 1.00 58.01  ? 4536 LEU A C     1 
ATOM   23631 O  O     . LEU A 1 4536 ? 136.304 152.269 119.939 1.00 62.29  ? 4536 LEU A O     1 
ATOM   23632 C  CB    . LEU A 1 4536 ? 137.149 149.579 121.508 1.00 52.21  ? 4536 LEU A CB    1 
ATOM   23633 C  CG    . LEU A 1 4536 ? 137.052 150.622 122.618 1.00 50.85  ? 4536 LEU A CG    1 
ATOM   23634 C  CD1   . LEU A 1 4536 ? 135.640 150.659 123.156 1.00 55.76  ? 4536 LEU A CD1   1 
ATOM   23635 C  CD2   . LEU A 1 4536 ? 138.044 150.352 123.723 1.00 45.82  ? 4536 LEU A CD2   1 
ATOM   23636 N  N     . GLU A 1 4537 ? 137.851 151.134 118.769 1.00 61.01  ? 4537 GLU A N     1 
ATOM   23637 C  CA    . GLU A 1 4537 ? 138.502 152.328 118.238 1.00 64.41  ? 4537 GLU A CA    1 
ATOM   23638 C  C     . GLU A 1 4537 ? 137.739 152.965 117.086 1.00 67.52  ? 4537 GLU A C     1 
ATOM   23639 O  O     . GLU A 1 4537 ? 138.109 154.062 116.651 1.00 77.06  ? 4537 GLU A O     1 
ATOM   23640 C  CB    . GLU A 1 4537 ? 139.904 151.979 117.745 1.00 56.70  ? 4537 GLU A CB    1 
ATOM   23641 C  CG    . GLU A 1 4537 ? 139.845 151.123 116.500 1.00 58.19  ? 4537 GLU A CG    1 
ATOM   23642 C  CD    . GLU A 1 4537 ? 139.681 149.664 116.814 1.00 66.01  ? 4537 GLU A CD    1 
ATOM   23643 O  OE1   . GLU A 1 4537 ? 139.335 149.341 117.968 1.00 71.40  ? 4537 GLU A OE1   1 
ATOM   23644 O  OE2   . GLU A 1 4537 ? 139.815 148.842 115.891 1.00 64.76  ? 4537 GLU A OE2   1 
ATOM   23645 N  N     . GLU A 1 4538 ? 136.702 152.310 116.572 1.00 59.77  ? 4538 GLU A N     1 
ATOM   23646 C  CA    . GLU A 1 4538 ? 135.877 152.873 115.515 1.00 61.12  ? 4538 GLU A CA    1 
ATOM   23647 C  C     . GLU A 1 4538 ? 134.703 153.658 116.069 1.00 68.61  ? 4538 GLU A C     1 
ATOM   23648 O  O     . GLU A 1 4538 ? 133.807 154.039 115.311 1.00 80.54  ? 4538 GLU A O     1 
ATOM   23649 C  CB    . GLU A 1 4538 ? 135.371 151.774 114.580 1.00 66.16  ? 4538 GLU A CB    1 
ATOM   23650 C  CG    . GLU A 1 4538 ? 136.458 151.030 113.837 1.00 74.31  ? 4538 GLU A CG    1 
ATOM   23651 C  CD    . GLU A 1 4538 ? 136.149 149.559 113.686 1.00 77.21  ? 4538 GLU A CD    1 
ATOM   23652 O  OE1   . GLU A 1 4538 ? 134.954 149.209 113.595 1.00 75.60  ? 4538 GLU A OE1   1 
ATOM   23653 O  OE2   . GLU A 1 4538 ? 137.101 148.754 113.640 1.00 79.07  ? 4538 GLU A OE2   1 
ATOM   23654 N  N     . LEU A 1 4539 ? 134.691 153.909 117.372 1.00 62.84  ? 4539 LEU A N     1 
ATOM   23655 C  CA    . LEU A 1 4539 ? 133.629 154.648 118.031 1.00 56.25  ? 4539 LEU A CA    1 
ATOM   23656 C  C     . LEU A 1 4539 ? 134.123 156.047 118.360 1.00 60.88  ? 4539 LEU A C     1 
ATOM   23657 O  O     . LEU A 1 4539 ? 135.203 156.210 118.938 1.00 65.78  ? 4539 LEU A O     1 
ATOM   23658 C  CB    . LEU A 1 4539 ? 133.180 153.937 119.309 1.00 50.97  ? 4539 LEU A CB    1 
ATOM   23659 C  CG    . LEU A 1 4539 ? 132.563 152.547 119.172 1.00 49.09  ? 4539 LEU A CG    1 
ATOM   23660 C  CD1   . LEU A 1 4539 ? 131.811 152.197 120.435 1.00 51.08  ? 4539 LEU A CD1   1 
ATOM   23661 C  CD2   . LEU A 1 4539 ? 131.644 152.487 117.972 1.00 52.84  ? 4539 LEU A CD2   1 
ATOM   23662 N  N     . CYS A 1 4540 ? 133.337 157.049 117.989 1.00 60.95  ? 4540 CYS A N     1 
ATOM   23663 C  CA    . CYS A 1 4540 ? 133.602 158.429 118.355 1.00 59.62  ? 4540 CYS A CA    1 
ATOM   23664 C  C     . CYS A 1 4540 ? 132.369 159.006 119.032 1.00 53.38  ? 4540 CYS A C     1 
ATOM   23665 O  O     . CYS A 1 4540 ? 131.239 158.581 118.772 1.00 55.59  ? 4540 CYS A O     1 
ATOM   23666 C  CB    . CYS A 1 4540 ? 133.998 159.273 117.137 1.00 69.78  ? 4540 CYS A CB    1 
ATOM   23667 S  SG    . CYS A 1 4540 ? 132.707 159.492 115.902 1.00 81.43  ? 4540 CYS A SG    1 
ATOM   23668 N  N     . LEU A 1 4541 ? 132.598 159.977 119.908 1.00 48.31  ? 4541 LEU A N     1 
ATOM   23669 C  CA    . LEU A 1 4541 ? 131.547 160.478 120.781 1.00 47.21  ? 4541 LEU A CA    1 
ATOM   23670 C  C     . LEU A 1 4541 ? 130.837 161.654 120.125 1.00 50.04  ? 4541 LEU A C     1 
ATOM   23671 O  O     . LEU A 1 4541 ? 131.482 162.617 119.695 1.00 58.81  ? 4541 LEU A O     1 
ATOM   23672 C  CB    . LEU A 1 4541 ? 132.139 160.886 122.127 1.00 46.84  ? 4541 LEU A CB    1 
ATOM   23673 C  CG    . LEU A 1 4541 ? 131.143 161.224 123.230 1.00 45.12  ? 4541 LEU A CG    1 
ATOM   23674 C  CD1   . LEU A 1 4541 ? 130.325 160.001 123.574 1.00 46.92  ? 4541 LEU A CD1   1 
ATOM   23675 C  CD2   . LEU A 1 4541 ? 131.874 161.734 124.453 1.00 47.41  ? 4541 LEU A CD2   1 
ATOM   23676 N  N     . GLU A 1 4542 ? 129.513 161.576 120.049 1.00 46.78  ? 4542 GLU A N     1 
ATOM   23677 C  CA    . GLU A 1 4542 ? 128.670 162.656 119.562 1.00 51.36  ? 4542 GLU A CA    1 
ATOM   23678 C  C     . GLU A 1 4542 ? 127.818 163.137 120.727 1.00 58.30  ? 4542 GLU A C     1 
ATOM   23679 O  O     . GLU A 1 4542 ? 127.198 162.327 121.424 1.00 63.24  ? 4542 GLU A O     1 
ATOM   23680 C  CB    . GLU A 1 4542 ? 127.799 162.182 118.399 1.00 46.60  ? 4542 GLU A CB    1 
ATOM   23681 C  CG    . GLU A 1 4542 ? 126.948 163.266 117.772 1.00 60.39  ? 4542 GLU A CG    1 
ATOM   23682 C  CD    . GLU A 1 4542 ? 126.137 162.756 116.599 1.00 76.86  ? 4542 GLU A CD    1 
ATOM   23683 O  OE1   . GLU A 1 4542 ? 126.225 161.548 116.296 1.00 75.96  ? 4542 GLU A OE1   1 
ATOM   23684 O  OE2   . GLU A 1 4542 ? 125.414 163.563 115.979 1.00 78.36  ? 4542 GLU A OE2   1 
ATOM   23685 N  N     . VAL A 1 4543 ? 127.795 164.443 120.949 1.00 59.58  ? 4543 VAL A N     1 
ATOM   23686 C  CA    . VAL A 1 4543 ? 127.144 165.022 122.116 1.00 55.80  ? 4543 VAL A CA    1 
ATOM   23687 C  C     . VAL A 1 4543 ? 125.865 165.712 121.674 1.00 66.88  ? 4543 VAL A C     1 
ATOM   23688 O  O     . VAL A 1 4543 ? 125.880 166.532 120.747 1.00 77.76  ? 4543 VAL A O     1 
ATOM   23689 C  CB    . VAL A 1 4543 ? 128.081 165.998 122.841 1.00 54.72  ? 4543 VAL A CB    1 
ATOM   23690 C  CG1   . VAL A 1 4543 ? 127.315 166.804 123.866 1.00 58.58  ? 4543 VAL A CG1   1 
ATOM   23691 C  CG2   . VAL A 1 4543 ? 129.206 165.230 123.492 1.00 57.39  ? 4543 VAL A CG2   1 
ATOM   23692 N  N     . ASN A 1 4544 ? 124.755 165.379 122.332 1.00 62.18  ? 4544 ASN A N     1 
ATOM   23693 C  CA    . ASN A 1 4544 ? 123.451 165.945 122.004 1.00 60.99  ? 4544 ASN A CA    1 
ATOM   23694 C  C     . ASN A 1 4544 ? 122.835 166.497 123.282 1.00 66.80  ? 4544 ASN A C     1 
ATOM   23695 O  O     . ASN A 1 4544 ? 122.427 165.731 124.156 1.00 74.45  ? 4544 ASN A O     1 
ATOM   23696 C  CB    . ASN A 1 4544 ? 122.545 164.889 121.369 1.00 63.01  ? 4544 ASN A CB    1 
ATOM   23697 C  CG    . ASN A 1 4544 ? 121.233 165.462 120.880 1.00 76.92  ? 4544 ASN A CG    1 
ATOM   23698 O  OD1   . ASN A 1 4544 ? 121.212 166.401 120.086 1.00 86.70  ? 4544 ASN A OD1   1 
ATOM   23699 N  ND2   . ASN A 1 4544 ? 120.129 164.903 121.357 1.00 74.74  ? 4544 ASN A ND2   1 
ATOM   23700 N  N     . VAL A 1 4545 ? 122.775 167.818 123.402 1.00 70.80  ? 4545 VAL A N     1 
ATOM   23701 C  CA    . VAL A 1 4545 ? 122.194 168.434 124.591 1.00 70.40  ? 4545 VAL A CA    1 
ATOM   23702 C  C     . VAL A 1 4545 ? 120.684 168.507 124.412 1.00 77.47  ? 4545 VAL A C     1 
ATOM   23703 O  O     . VAL A 1 4545 ? 120.188 169.153 123.483 1.00 82.15  ? 4545 VAL A O     1 
ATOM   23704 C  CB    . VAL A 1 4545 ? 122.791 169.823 124.846 1.00 63.65  ? 4545 VAL A CB    1 
ATOM   23705 C  CG1   . VAL A 1 4545 ? 122.122 170.467 126.044 1.00 63.89  ? 4545 VAL A CG1   1 
ATOM   23706 C  CG2   . VAL A 1 4545 ? 124.289 169.716 125.068 1.00 60.41  ? 4545 VAL A CG2   1 
ATOM   23707 N  N     . THR A 1 4546 ? 119.951 167.842 125.301 1.00 76.88  ? 4546 THR A N     1 
ATOM   23708 C  CA    . THR A 1 4546 ? 118.496 167.753 125.226 1.00 84.29  ? 4546 THR A CA    1 
ATOM   23709 C  C     . THR A 1 4546 ? 117.900 168.519 126.397 1.00 91.36  ? 4546 THR A C     1 
ATOM   23710 O  O     . THR A 1 4546 ? 118.121 168.158 127.558 1.00 85.57  ? 4546 THR A O     1 
ATOM   23711 C  CB    . THR A 1 4546 ? 118.035 166.297 125.241 1.00 85.68  ? 4546 THR A CB    1 
ATOM   23712 O  OG1   . THR A 1 4546 ? 118.563 165.641 126.400 1.00 82.30  ? 4546 THR A OG1   1 
ATOM   23713 C  CG2   . THR A 1 4546 ? 118.516 165.573 123.996 1.00 80.76  ? 4546 THR A CG2   1 
ATOM   23714 N  N     . THR A 1 4547 ? 117.143 169.576 126.094 1.00 102.43 ? 4547 THR A N     1 
ATOM   23715 C  CA    . THR A 1 4547 ? 116.444 170.313 127.138 1.00 108.65 ? 4547 THR A CA    1 
ATOM   23716 C  C     . THR A 1 4547 ? 115.183 169.597 127.600 1.00 113.99 ? 4547 THR A C     1 
ATOM   23717 O  O     . THR A 1 4547 ? 114.656 169.923 128.669 1.00 116.71 ? 4547 THR A O     1 
ATOM   23718 C  CB    . THR A 1 4547 ? 116.086 171.718 126.651 1.00 108.40 ? 4547 THR A CB    1 
ATOM   23719 O  OG1   . THR A 1 4547 ? 115.065 171.633 125.650 1.00 108.44 ? 4547 THR A OG1   1 
ATOM   23720 C  CG2   . THR A 1 4547 ? 117.310 172.405 126.063 1.00 105.83 ? 4547 THR A CG2   1 
ATOM   23721 N  N     . SER A 1 4548 ? 114.690 168.638 126.821 1.00 116.91 ? 4548 SER A N     1 
ATOM   23722 C  CA    . SER A 1 4548 ? 113.483 167.913 127.191 1.00 120.86 ? 4548 SER A CA    1 
ATOM   23723 C  C     . SER A 1 4548 ? 113.728 167.050 128.422 1.00 122.12 ? 4548 SER A C     1 
ATOM   23724 O  O     . SER A 1 4548 ? 114.782 166.424 128.564 1.00 118.40 ? 4548 SER A O     1 
ATOM   23725 C  CB    . SER A 1 4548 ? 113.007 167.046 126.026 1.00 119.41 ? 4548 SER A CB    1 
ATOM   23726 O  OG    . SER A 1 4548 ? 114.058 166.234 125.531 1.00 109.17 ? 4548 SER A OG    1 
ATOM   23727 N  N     . GLN A 1 4549 ? 112.745 167.025 129.318 1.00 122.41 ? 4549 GLN A N     1 
ATOM   23728 C  CA    . GLN A 1 4549 ? 112.851 166.218 130.525 1.00 122.26 ? 4549 GLN A CA    1 
ATOM   23729 C  C     . GLN A 1 4549 ? 112.633 164.748 130.193 1.00 126.33 ? 4549 GLN A C     1 
ATOM   23730 O  O     . GLN A 1 4549 ? 111.678 164.393 129.495 1.00 122.25 ? 4549 GLN A O     1 
ATOM   23731 C  CB    . GLN A 1 4549 ? 111.833 166.686 131.563 1.00 118.78 ? 4549 GLN A CB    1 
ATOM   23732 C  CG    . GLN A 1 4549 ? 111.889 168.176 131.850 1.00 120.33 ? 4549 GLN A CG    1 
ATOM   23733 C  CD    . GLN A 1 4549 ? 110.761 168.640 132.748 1.00 123.51 ? 4549 GLN A CD    1 
ATOM   23734 O  OE1   . GLN A 1 4549 ? 109.923 167.845 133.173 1.00 124.44 ? 4549 GLN A OE1   1 
ATOM   23735 N  NE2   . GLN A 1 4549 ? 110.732 169.935 133.041 1.00 125.67 ? 4549 GLN A NE2   1 
ATOM   23736 N  N     . GLY A 1 4550 ? 113.516 163.893 130.698 1.00 127.56 ? 4550 GLY A N     1 
ATOM   23737 C  CA    . GLY A 1 4550 ? 113.405 162.468 130.428 1.00 125.78 ? 4550 GLY A CA    1 
ATOM   23738 C  C     . GLY A 1 4550 ? 113.507 162.122 128.959 1.00 129.60 ? 4550 GLY A C     1 
ATOM   23739 O  O     . GLY A 1 4550 ? 112.706 161.326 128.453 1.00 128.37 ? 4550 GLY A O     1 
ATOM   23740 N  N     . ALA A 1 4551 ? 114.473 162.712 128.257 1.00 125.78 ? 4551 ALA A N     1 
ATOM   23741 C  CA    . ALA A 1 4551 ? 114.628 162.456 126.833 1.00 119.19 ? 4551 ALA A CA    1 
ATOM   23742 C  C     . ALA A 1 4551 ? 114.957 160.989 126.586 1.00 119.23 ? 4551 ALA A C     1 
ATOM   23743 O  O     . ALA A 1 4551 ? 115.663 160.345 127.368 1.00 115.16 ? 4551 ALA A O     1 
ATOM   23744 C  CB    . ALA A 1 4551 ? 115.722 163.349 126.248 1.00 107.88 ? 4551 ALA A CB    1 
ATOM   23745 N  N     . THR A 1 4552 ? 114.425 160.460 125.486 1.00 120.00 ? 4552 THR A N     1 
ATOM   23746 C  CA    . THR A 1 4552 ? 114.619 159.054 125.162 1.00 113.49 ? 4552 THR A CA    1 
ATOM   23747 C  C     . THR A 1 4552 ? 116.091 158.758 124.912 1.00 107.15 ? 4552 THR A C     1 
ATOM   23748 O  O     . THR A 1 4552 ? 116.783 159.500 124.210 1.00 108.65 ? 4552 THR A O     1 
ATOM   23749 C  CB    . THR A 1 4552 ? 113.792 158.674 123.934 1.00 115.78 ? 4552 THR A CB    1 
ATOM   23750 O  OG1   . THR A 1 4552 ? 114.300 159.362 122.784 1.00 115.49 ? 4552 THR A OG1   1 
ATOM   23751 C  CG2   . THR A 1 4552 ? 112.332 159.050 124.139 1.00 116.02 ? 4552 THR A CG2   1 
ATOM   23752 N  N     . LEU A 1 4553 ? 116.569 157.662 125.492 1.00 101.02 ? 4553 LEU A N     1 
ATOM   23753 C  CA    . LEU A 1 4553 ? 117.953 157.233 125.344 1.00 95.21  ? 4553 LEU A CA    1 
ATOM   23754 C  C     . LEU A 1 4553 ? 118.016 156.109 124.320 1.00 93.84  ? 4553 LEU A C     1 
ATOM   23755 O  O     . LEU A 1 4553 ? 117.355 155.077 124.481 1.00 95.30  ? 4553 LEU A O     1 
ATOM   23756 C  CB    . LEU A 1 4553 ? 118.530 156.775 126.683 1.00 92.64  ? 4553 LEU A CB    1 
ATOM   23757 C  CG    . LEU A 1 4553 ? 118.790 157.859 127.731 1.00 89.70  ? 4553 LEU A CG    1 
ATOM   23758 C  CD1   . LEU A 1 4553 ? 119.684 157.324 128.837 1.00 81.61  ? 4553 LEU A CD1   1 
ATOM   23759 C  CD2   . LEU A 1 4553 ? 119.405 159.095 127.092 1.00 84.37  ? 4553 LEU A CD2   1 
ATOM   23760 N  N     . ASP A 1 4554 ? 118.809 156.310 123.271 1.00 88.13  ? 4554 ASP A N     1 
ATOM   23761 C  CA    . ASP A 1 4554 ? 119.006 155.285 122.260 1.00 85.60  ? 4554 ASP A CA    1 
ATOM   23762 C  C     . ASP A 1 4554 ? 119.881 154.170 122.839 1.00 88.27  ? 4554 ASP A C     1 
ATOM   23763 O  O     . ASP A 1 4554 ? 120.359 154.243 123.975 1.00 87.00  ? 4554 ASP A O     1 
ATOM   23764 C  CB    . ASP A 1 4554 ? 119.613 155.913 121.004 1.00 88.70  ? 4554 ASP A CB    1 
ATOM   23765 C  CG    . ASP A 1 4554 ? 119.709 154.943 119.842 1.00 100.21 ? 4554 ASP A CG    1 
ATOM   23766 O  OD1   . ASP A 1 4554 ? 118.660 154.637 119.236 1.00 102.31 ? 4554 ASP A OD1   1 
ATOM   23767 O  OD2   . ASP A 1 4554 ? 120.831 154.489 119.533 1.00 98.59  ? 4554 ASP A OD2   1 
ATOM   23768 N  N     . ALA A 1 4555 ? 120.087 153.112 122.051 1.00 88.12  ? 4555 ALA A N     1 
ATOM   23769 C  CA    . ALA A 1 4555 ? 120.907 151.996 122.511 1.00 85.08  ? 4555 ALA A CA    1 
ATOM   23770 C  C     . ALA A 1 4555 ? 122.333 152.443 122.808 1.00 83.05  ? 4555 ALA A C     1 
ATOM   23771 O  O     . ALA A 1 4555 ? 122.939 152.004 123.792 1.00 79.03  ? 4555 ALA A O     1 
ATOM   23772 C  CB    . ALA A 1 4555 ? 120.900 150.876 121.472 1.00 81.59  ? 4555 ALA A CB    1 
ATOM   23773 N  N     . CYS A 1 4556 ? 122.888 153.310 121.966 1.00 82.09  ? 4556 CYS A N     1 
ATOM   23774 C  CA    . CYS A 1 4556 ? 124.229 153.836 122.172 1.00 76.27  ? 4556 CYS A CA    1 
ATOM   23775 C  C     . CYS A 1 4556 ? 124.244 155.236 122.774 1.00 75.01  ? 4556 CYS A C     1 
ATOM   23776 O  O     . CYS A 1 4556 ? 125.321 155.828 122.888 1.00 73.36  ? 4556 CYS A O     1 
ATOM   23777 C  CB    . CYS A 1 4556 ? 125.002 153.831 120.849 1.00 70.49  ? 4556 CYS A CB    1 
ATOM   23778 S  SG    . CYS A 1 4556 ? 124.311 154.892 119.570 1.00 77.33  ? 4556 CYS A SG    1 
ATOM   23779 N  N     . SER A 1 4557 ? 123.090 155.774 123.163 1.00 77.98  ? 4557 SER A N     1 
ATOM   23780 C  CA    . SER A 1 4557 ? 122.998 157.104 123.755 1.00 72.15  ? 4557 SER A CA    1 
ATOM   23781 C  C     . SER A 1 4557 ? 122.826 156.970 125.262 1.00 67.49  ? 4557 SER A C     1 
ATOM   23782 O  O     . SER A 1 4557 ? 121.922 156.268 125.726 1.00 76.18  ? 4557 SER A O     1 
ATOM   23783 C  CB    . SER A 1 4557 ? 121.834 157.890 123.154 1.00 75.12  ? 4557 SER A CB    1 
ATOM   23784 O  OG    . SER A 1 4557 ? 121.984 158.036 121.754 1.00 75.06  ? 4557 SER A OG    1 
ATOM   23785 N  N     . PHE A 1 4558 ? 123.686 157.644 126.018 1.00 57.32  ? 4558 PHE A N     1 
ATOM   23786 C  CA    . PHE A 1 4558 ? 123.688 157.574 127.472 1.00 63.49  ? 4558 PHE A CA    1 
ATOM   23787 C  C     . PHE A 1 4558 ? 123.478 158.965 128.052 1.00 66.47  ? 4558 PHE A C     1 
ATOM   23788 O  O     . PHE A 1 4558 ? 124.009 159.949 127.531 1.00 73.51  ? 4558 PHE A O     1 
ATOM   23789 C  CB    . PHE A 1 4558 ? 125.001 156.988 127.990 1.00 63.21  ? 4558 PHE A CB    1 
ATOM   23790 C  CG    . PHE A 1 4558 ? 125.203 155.545 127.633 1.00 73.97  ? 4558 PHE A CG    1 
ATOM   23791 C  CD1   . PHE A 1 4558 ? 124.155 154.767 127.187 1.00 84.71  ? 4558 PHE A CD1   1 
ATOM   23792 C  CD2   . PHE A 1 4558 ? 126.447 154.970 127.730 1.00 67.90  ? 4558 PHE A CD2   1 
ATOM   23793 C  CE1   . PHE A 1 4558 ? 124.354 153.449 126.850 1.00 81.38  ? 4558 PHE A CE1   1 
ATOM   23794 C  CE2   . PHE A 1 4558 ? 126.646 153.651 127.401 1.00 63.05  ? 4558 PHE A CE2   1 
ATOM   23795 C  CZ    . PHE A 1 4558 ? 125.600 152.892 126.961 1.00 69.29  ? 4558 PHE A CZ    1 
ATOM   23796 N  N     . GLY A 1 4559 ? 122.707 159.046 129.133 1.00 62.98  ? 4559 GLY A N     1 
ATOM   23797 C  CA    . GLY A 1 4559 ? 122.406 160.335 129.730 1.00 58.43  ? 4559 GLY A CA    1 
ATOM   23798 C  C     . GLY A 1 4559 ? 123.430 160.730 130.783 1.00 53.25  ? 4559 GLY A C     1 
ATOM   23799 O  O     . GLY A 1 4559 ? 123.873 159.916 131.591 1.00 67.58  ? 4559 GLY A O     1 
ATOM   23800 N  N     . VAL A 1 4560 ? 123.807 162.006 130.760 1.00 49.36  ? 4560 VAL A N     1 
ATOM   23801 C  CA    . VAL A 1 4560 ? 124.730 162.581 131.730 1.00 53.59  ? 4560 VAL A CA    1 
ATOM   23802 C  C     . VAL A 1 4560 ? 124.191 163.941 132.144 1.00 60.97  ? 4560 VAL A C     1 
ATOM   23803 O  O     . VAL A 1 4560 ? 123.863 164.769 131.289 1.00 67.29  ? 4560 VAL A O     1 
ATOM   23804 C  CB    . VAL A 1 4560 ? 126.155 162.712 131.157 1.00 50.49  ? 4560 VAL A CB    1 
ATOM   23805 C  CG1   . VAL A 1 4560 ? 126.955 163.736 131.942 1.00 53.06  ? 4560 VAL A CG1   1 
ATOM   23806 C  CG2   . VAL A 1 4560 ? 126.857 161.366 131.166 1.00 56.43  ? 4560 VAL A CG2   1 
ATOM   23807 N  N     . THR A 1 4561 ? 124.098 164.172 133.448 1.00 60.41  ? 4561 THR A N     1 
ATOM   23808 C  CA    . THR A 1 4561 ? 123.603 165.426 133.993 1.00 60.92  ? 4561 THR A CA    1 
ATOM   23809 C  C     . THR A 1 4561 ? 124.716 166.147 134.743 1.00 65.02  ? 4561 THR A C     1 
ATOM   23810 O  O     . THR A 1 4561 ? 125.785 165.592 135.008 1.00 64.63  ? 4561 THR A O     1 
ATOM   23811 C  CB    . THR A 1 4561 ? 122.407 165.187 134.922 1.00 65.14  ? 4561 THR A CB    1 
ATOM   23812 O  OG1   . THR A 1 4561 ? 122.810 164.365 136.024 1.00 72.55  ? 4561 THR A OG1   1 
ATOM   23813 C  CG2   . THR A 1 4561 ? 121.282 164.498 134.174 1.00 65.20  ? 4561 THR A CG2   1 
ATOM   23814 N  N     . GLY A 1 4562 ? 124.449 167.405 135.082 1.00 67.45  ? 4562 GLY A N     1 
ATOM   23815 C  CA    . GLY A 1 4562 ? 125.380 168.205 135.847 1.00 70.16  ? 4562 GLY A CA    1 
ATOM   23816 C  C     . GLY A 1 4562 ? 126.432 168.930 135.039 1.00 64.44  ? 4562 GLY A C     1 
ATOM   23817 O  O     . GLY A 1 4562 ? 127.235 169.667 135.625 1.00 63.64  ? 4562 GLY A O     1 
ATOM   23818 N  N     . LEU A 1 4563 ? 126.460 168.749 133.722 1.00 59.66  ? 4563 LEU A N     1 
ATOM   23819 C  CA    . LEU A 1 4563 ? 127.460 169.412 132.897 1.00 57.52  ? 4563 LEU A CA    1 
ATOM   23820 C  C     . LEU A 1 4563 ? 127.199 170.912 132.855 1.00 59.73  ? 4563 LEU A C     1 
ATOM   23821 O  O     . LEU A 1 4563 ? 126.067 171.351 132.629 1.00 62.72  ? 4563 LEU A O     1 
ATOM   23822 C  CB    . LEU A 1 4563 ? 127.447 168.830 131.485 1.00 58.80  ? 4563 LEU A CB    1 
ATOM   23823 C  CG    . LEU A 1 4563 ? 127.928 167.387 131.321 1.00 54.48  ? 4563 LEU A CG    1 
ATOM   23824 C  CD1   . LEU A 1 4563 ? 128.324 167.118 129.883 1.00 51.61  ? 4563 LEU A CD1   1 
ATOM   23825 C  CD2   . LEU A 1 4563 ? 129.087 167.092 132.255 1.00 54.99  ? 4563 LEU A CD2   1 
ATOM   23826 N  N     . LYS A 1 4564 ? 128.248 171.698 133.070 1.00 56.48  ? 4564 LYS A N     1 
ATOM   23827 C  CA    . LYS A 1 4564 ? 128.171 173.152 133.039 1.00 52.85  ? 4564 LYS A CA    1 
ATOM   23828 C  C     . LYS A 1 4564 ? 128.945 173.665 131.834 1.00 50.60  ? 4564 LYS A C     1 
ATOM   23829 O  O     . LYS A 1 4564 ? 130.058 173.206 131.571 1.00 57.51  ? 4564 LYS A O     1 
ATOM   23830 C  CB    . LYS A 1 4564 ? 128.740 173.761 134.323 1.00 54.37  ? 4564 LYS A CB    1 
ATOM   23831 C  CG    . LYS A 1 4564 ? 128.078 173.278 135.601 1.00 66.09  ? 4564 LYS A CG    1 
ATOM   23832 C  CD    . LYS A 1 4564 ? 126.656 173.791 135.726 1.00 74.92  ? 4564 LYS A CD    1 
ATOM   23833 C  CE    . LYS A 1 4564 ? 126.044 173.374 137.053 1.00 85.00  ? 4564 LYS A CE    1 
ATOM   23834 N  NZ    . LYS A 1 4564 ? 124.634 173.830 137.188 1.00 89.09  ? 4564 LYS A NZ    1 
ATOM   23835 N  N     . LEU A 1 4565 ? 128.361 174.609 131.107 1.00 45.74  ? 4565 LEU A N     1 
ATOM   23836 C  CA    . LEU A 1 4565 ? 129.011 175.220 129.956 1.00 41.34  ? 4565 LEU A CA    1 
ATOM   23837 C  C     . LEU A 1 4565 ? 129.504 176.605 130.350 1.00 47.81  ? 4565 LEU A C     1 
ATOM   23838 O  O     . LEU A 1 4565 ? 128.706 177.460 130.746 1.00 57.26  ? 4565 LEU A O     1 
ATOM   23839 C  CB    . LEU A 1 4565 ? 128.048 175.302 128.773 1.00 40.21  ? 4565 LEU A CB    1 
ATOM   23840 C  CG    . LEU A 1 4565 ? 128.644 175.705 127.427 1.00 41.48  ? 4565 LEU A CG    1 
ATOM   23841 C  CD1   . LEU A 1 4565 ? 129.792 174.789 127.052 1.00 38.02  ? 4565 LEU A CD1   1 
ATOM   23842 C  CD2   . LEU A 1 4565 ? 127.566 175.670 126.365 1.00 49.96  ? 4565 LEU A CD2   1 
ATOM   23843 N  N     . GLN A 1 4566 ? 130.811 176.828 130.238 1.00 39.96  ? 4566 GLN A N     1 
ATOM   23844 C  CA    . GLN A 1 4566 ? 131.435 178.065 130.687 1.00 39.48  ? 4566 GLN A CA    1 
ATOM   23845 C  C     . GLN A 1 4566 ? 131.492 179.059 129.537 1.00 43.73  ? 4566 GLN A C     1 
ATOM   23846 O  O     . GLN A 1 4566 ? 132.190 178.828 128.545 1.00 48.47  ? 4566 GLN A O     1 
ATOM   23847 C  CB    . GLN A 1 4566 ? 132.837 177.796 131.228 1.00 39.22  ? 4566 GLN A CB    1 
ATOM   23848 C  CG    . GLN A 1 4566 ? 132.898 176.688 132.256 1.00 46.16  ? 4566 GLN A CG    1 
ATOM   23849 C  CD    . GLN A 1 4566 ? 132.133 177.030 133.516 1.00 61.72  ? 4566 GLN A CD    1 
ATOM   23850 O  OE1   . GLN A 1 4566 ? 131.189 176.336 133.891 1.00 62.69  ? 4566 GLN A OE1   1 
ATOM   23851 N  NE2   . GLN A 1 4566 ? 132.539 178.105 134.179 1.00 66.75  ? 4566 GLN A NE2   1 
ATOM   23852 N  N     . GLY A 1 4567 ? 130.769 180.167 129.676 1.00 45.83  ? 4567 GLY A N     1 
ATOM   23853 C  CA    . GLY A 1 4567 ? 130.848 181.232 128.699 1.00 48.28  ? 4567 GLY A CA    1 
ATOM   23854 C  C     . GLY A 1 4567 ? 130.175 180.951 127.379 1.00 50.62  ? 4567 GLY A C     1 
ATOM   23855 O  O     . GLY A 1 4567 ? 130.529 181.570 126.374 1.00 57.37  ? 4567 GLY A O     1 
ATOM   23856 N  N     . ALA A 1 4568 ? 129.213 180.034 127.345 1.00 46.59  ? 4568 ALA A N     1 
ATOM   23857 C  CA    . ALA A 1 4568 ? 128.484 179.757 126.118 1.00 45.51  ? 4568 ALA A CA    1 
ATOM   23858 C  C     . ALA A 1 4568 ? 127.113 179.203 126.470 1.00 49.62  ? 4568 ALA A C     1 
ATOM   23859 O  O     . ALA A 1 4568 ? 126.899 178.668 127.560 1.00 54.46  ? 4568 ALA A O     1 
ATOM   23860 C  CB    . ALA A 1 4568 ? 129.246 178.781 125.217 1.00 42.13  ? 4568 ALA A CB    1 
ATOM   23861 N  N     . THR A 1 4569 ? 126.186 179.346 125.528 1.00 48.24  ? 4569 THR A N     1 
ATOM   23862 C  CA    . THR A 1 4569 ? 124.831 178.832 125.660 1.00 48.53  ? 4569 THR A CA    1 
ATOM   23863 C  C     . THR A 1 4569 ? 124.577 177.831 124.546 1.00 55.98  ? 4569 THR A C     1 
ATOM   23864 O  O     . THR A 1 4569 ? 124.869 178.110 123.379 1.00 61.11  ? 4569 THR A O     1 
ATOM   23865 C  CB    . THR A 1 4569 ? 123.795 179.957 125.598 1.00 56.30  ? 4569 THR A CB    1 
ATOM   23866 O  OG1   . THR A 1 4569 ? 124.085 180.815 124.489 1.00 60.12  ? 4569 THR A OG1   1 
ATOM   23867 C  CG2   . THR A 1 4569 ? 123.815 180.771 126.880 1.00 59.38  ? 4569 THR A CG2   1 
ATOM   23868 N  N     . CYS A 1 4570 ? 124.035 176.671 124.905 1.00 64.45  ? 4570 CYS A N     1 
ATOM   23869 C  CA    . CYS A 1 4570 ? 123.763 175.601 123.950 1.00 63.24  ? 4570 CYS A CA    1 
ATOM   23870 C  C     . CYS A 1 4570 ? 122.266 175.581 123.667 1.00 67.00  ? 4570 CYS A C     1 
ATOM   23871 O  O     . CYS A 1 4570 ? 121.474 175.101 124.481 1.00 72.77  ? 4570 CYS A O     1 
ATOM   23872 C  CB    . CYS A 1 4570 ? 124.249 174.260 124.487 1.00 61.18  ? 4570 CYS A CB    1 
ATOM   23873 S  SG    . CYS A 1 4570 ? 124.000 172.881 123.353 1.00 74.51  ? 4570 CYS A SG    1 
ATOM   23874 N  N     . ASN A 1 4571 ? 121.883 176.102 122.506 1.00 66.64  ? 4571 ASN A N     1 
ATOM   23875 C  CA    . ASN A 1 4571 ? 120.503 176.086 122.044 1.00 74.66  ? 4571 ASN A CA    1 
ATOM   23876 C  C     . ASN A 1 4571 ? 120.425 175.271 120.762 1.00 74.51  ? 4571 ASN A C     1 
ATOM   23877 O  O     . ASN A 1 4571 ? 121.199 175.505 119.827 1.00 75.15  ? 4571 ASN A O     1 
ATOM   23878 C  CB    . ASN A 1 4571 ? 119.981 177.507 121.811 1.00 81.45  ? 4571 ASN A CB    1 
ATOM   23879 C  CG    . ASN A 1 4571 ? 120.173 178.403 123.021 1.00 84.94  ? 4571 ASN A CG    1 
ATOM   23880 O  OD1   . ASN A 1 4571 ? 119.666 178.119 124.105 1.00 84.23  ? 4571 ASN A OD1   1 
ATOM   23881 N  ND2   . ASN A 1 4571 ? 120.908 179.494 122.839 1.00 84.00  ? 4571 ASN A ND2   1 
ATOM   23882 N  N     . ASN A 1 4572 ? 119.496 174.313 120.727 1.00 76.10  ? 4572 ASN A N     1 
ATOM   23883 C  CA    . ASN A 1 4572 ? 119.339 173.403 119.591 1.00 75.55  ? 4572 ASN A CA    1 
ATOM   23884 C  C     . ASN A 1 4572 ? 120.655 172.702 119.267 1.00 75.73  ? 4572 ASN A C     1 
ATOM   23885 O  O     . ASN A 1 4572 ? 121.008 172.499 118.103 1.00 76.63  ? 4572 ASN A O     1 
ATOM   23886 C  CB    . ASN A 1 4572 ? 118.792 174.134 118.364 1.00 78.05  ? 4572 ASN A CB    1 
ATOM   23887 C  CG    . ASN A 1 4572 ? 117.399 174.683 118.588 1.00 89.10  ? 4572 ASN A CG    1 
ATOM   23888 O  OD1   . ASN A 1 4572 ? 117.190 175.895 118.596 1.00 92.81  ? 4572 ASN A OD1   1 
ATOM   23889 N  ND2   . ASN A 1 4572 ? 116.436 173.789 118.773 1.00 89.53  ? 4572 ASN A ND2   1 
ATOM   23890 N  N     . ASN A 1 4573 ? 121.387 172.333 120.319 1.00 74.70  ? 4573 ASN A N     1 
ATOM   23891 C  CA    . ASN A 1 4573 ? 122.684 171.666 120.206 1.00 72.00  ? 4573 ASN A CA    1 
ATOM   23892 C  C     . ASN A 1 4573 ? 123.664 172.516 119.392 1.00 67.54  ? 4573 ASN A C     1 
ATOM   23893 O  O     . ASN A 1 4573 ? 124.477 172.000 118.624 1.00 66.83  ? 4573 ASN A O     1 
ATOM   23894 C  CB    . ASN A 1 4573 ? 122.524 170.262 119.609 1.00 72.35  ? 4573 ASN A CB    1 
ATOM   23895 C  CG    . ASN A 1 4573 ? 123.794 169.430 119.688 1.00 78.62  ? 4573 ASN A CG    1 
ATOM   23896 O  OD1   . ASN A 1 4573 ? 124.830 169.887 120.172 1.00 77.51  ? 4573 ASN A OD1   1 
ATOM   23897 N  ND2   . ASN A 1 4573 ? 123.716 168.196 119.206 1.00 81.43  ? 4573 ASN A ND2   1 
ATOM   23898 N  N     . LYS A 1 4574 ? 123.566 173.836 119.530 1.00 64.22  ? 4574 LYS A N     1 
ATOM   23899 C  CA    . LYS A 1 4574 ? 124.482 174.772 118.895 1.00 53.75  ? 4574 LYS A CA    1 
ATOM   23900 C  C     . LYS A 1 4574 ? 124.953 175.778 119.931 1.00 55.69  ? 4574 LYS A C     1 
ATOM   23901 O  O     . LYS A 1 4574 ? 124.155 176.272 120.731 1.00 65.34  ? 4574 LYS A O     1 
ATOM   23902 C  CB    . LYS A 1 4574 ? 123.817 175.503 117.727 1.00 61.44  ? 4574 LYS A CB    1 
ATOM   23903 C  CG    . LYS A 1 4574 ? 123.702 174.690 116.453 1.00 60.02  ? 4574 LYS A CG    1 
ATOM   23904 C  CD    . LYS A 1 4574 ? 123.333 175.587 115.287 1.00 62.29  ? 4574 LYS A CD    1 
ATOM   23905 C  CE    . LYS A 1 4574 ? 123.314 174.825 113.977 1.00 66.77  ? 4574 LYS A CE    1 
ATOM   23906 N  NZ    . LYS A 1 4574 ? 123.010 175.725 112.830 1.00 74.66  ? 4574 LYS A NZ    1 
ATOM   23907 N  N     . LEU A 1 4575 ? 126.245 176.089 119.912 1.00 53.15  ? 4575 LEU A N     1 
ATOM   23908 C  CA    . LEU A 1 4575 ? 126.839 176.981 120.897 1.00 50.79  ? 4575 LEU A CA    1 
ATOM   23909 C  C     . LEU A 1 4575 ? 126.846 178.419 120.405 1.00 55.32  ? 4575 LEU A C     1 
ATOM   23910 O  O     . LEU A 1 4575 ? 127.178 178.693 119.248 1.00 64.06  ? 4575 LEU A O     1 
ATOM   23911 C  CB    . LEU A 1 4575 ? 128.269 176.563 121.234 1.00 44.99  ? 4575 LEU A CB    1 
ATOM   23912 C  CG    . LEU A 1 4575 ? 128.486 175.162 121.789 1.00 46.92  ? 4575 LEU A CG    1 
ATOM   23913 C  CD1   . LEU A 1 4575 ? 129.875 175.076 122.370 1.00 50.40  ? 4575 LEU A CD1   1 
ATOM   23914 C  CD2   . LEU A 1 4575 ? 127.445 174.830 122.832 1.00 49.61  ? 4575 LEU A CD2   1 
ATOM   23915 N  N     . SER A 1 4576 ? 126.486 179.334 121.298 1.00 50.80  ? 4576 SER A N     1 
ATOM   23916 C  CA    . SER A 1 4576 ? 126.606 180.764 121.062 1.00 54.74  ? 4576 SER A CA    1 
ATOM   23917 C  C     . SER A 1 4576 ? 127.377 181.382 122.216 1.00 55.38  ? 4576 SER A C     1 
ATOM   23918 O  O     . SER A 1 4576 ? 127.181 181.004 123.373 1.00 60.60  ? 4576 SER A O     1 
ATOM   23919 C  CB    . SER A 1 4576 ? 125.233 181.430 120.927 1.00 59.08  ? 4576 SER A CB    1 
ATOM   23920 O  OG    . SER A 1 4576 ? 124.377 180.669 120.093 1.00 69.05  ? 4576 SER A OG    1 
ATOM   23921 N  N     . LEU A 1 4577 ? 128.261 182.324 121.898 1.00 56.92  ? 4577 LEU A N     1 
ATOM   23922 C  CA    . LEU A 1 4577 ? 129.037 182.993 122.933 1.00 58.35  ? 4577 LEU A CA    1 
ATOM   23923 C  C     . LEU A 1 4577 ? 128.113 183.733 123.889 1.00 63.25  ? 4577 LEU A C     1 
ATOM   23924 O  O     . LEU A 1 4577 ? 127.165 184.399 123.465 1.00 70.22  ? 4577 LEU A O     1 
ATOM   23925 C  CB    . LEU A 1 4577 ? 130.036 183.959 122.302 1.00 54.13  ? 4577 LEU A CB    1 
ATOM   23926 C  CG    . LEU A 1 4577 ? 131.309 183.325 121.746 1.00 47.10  ? 4577 LEU A CG    1 
ATOM   23927 C  CD1   . LEU A 1 4577 ? 132.226 184.398 121.202 1.00 45.46  ? 4577 LEU A CD1   1 
ATOM   23928 C  CD2   . LEU A 1 4577 ? 132.011 182.512 122.816 1.00 40.02  ? 4577 LEU A CD2   1 
ATOM   23929 N  N     . SER A 1 4578 ? 128.388 183.610 125.183 1.00 57.07  ? 4578 SER A N     1 
ATOM   23930 C  CA    . SER A 1 4578 ? 127.550 184.198 126.216 1.00 61.46  ? 4578 SER A CA    1 
ATOM   23931 C  C     . SER A 1 4578 ? 128.408 184.973 127.202 1.00 71.52  ? 4578 SER A C     1 
ATOM   23932 O  O     . SER A 1 4578 ? 129.520 184.553 127.537 1.00 67.94  ? 4578 SER A O     1 
ATOM   23933 C  CB    . SER A 1 4578 ? 126.750 183.123 126.957 1.00 58.33  ? 4578 SER A CB    1 
ATOM   23934 O  OG    . SER A 1 4578 ? 125.979 183.689 128.001 1.00 70.17  ? 4578 SER A OG    1 
ATOM   23935 N  N     . ASN A 1 4579 ? 127.884 186.104 127.666 1.00 76.02  ? 4579 ASN A N     1 
ATOM   23936 C  CA    . ASN A 1 4579 ? 128.538 186.878 128.712 1.00 77.28  ? 4579 ASN A CA    1 
ATOM   23937 C  C     . ASN A 1 4579 ? 128.194 186.381 130.108 1.00 76.53  ? 4579 ASN A C     1 
ATOM   23938 O  O     . ASN A 1 4579 ? 128.697 186.938 131.089 1.00 77.38  ? 4579 ASN A O     1 
ATOM   23939 C  CB    . ASN A 1 4579 ? 128.172 188.358 128.581 1.00 81.77  ? 4579 ASN A CB    1 
ATOM   23940 C  CG    . ASN A 1 4579 ? 128.688 188.973 127.296 1.00 90.76  ? 4579 ASN A CG    1 
ATOM   23941 O  OD1   . ASN A 1 4579 ? 129.889 188.972 127.032 1.00 88.81  ? 4579 ASN A OD1   1 
ATOM   23942 N  ND2   . ASN A 1 4579 ? 127.780 189.507 126.489 1.00 91.78  ? 4579 ASN A ND2   1 
ATOM   23943 N  N     . ALA A 1 4580 ? 127.350 185.359 130.220 1.00 73.33  ? 4580 ALA A N     1 
ATOM   23944 C  CA    . ALA A 1 4580 ? 127.044 184.769 131.511 1.00 72.59  ? 4580 ALA A CA    1 
ATOM   23945 C  C     . ALA A 1 4580 ? 128.247 183.994 132.039 1.00 72.57  ? 4580 ALA A C     1 
ATOM   23946 O  O     . ALA A 1 4580 ? 129.114 183.545 131.284 1.00 69.88  ? 4580 ALA A O     1 
ATOM   23947 C  CB    . ALA A 1 4580 ? 125.829 183.849 131.407 1.00 65.57  ? 4580 ALA A CB    1 
ATOM   23948 N  N     . ILE A 1 4581 ? 128.294 183.847 133.364 1.00 72.23  ? 4581 ILE A N     1 
ATOM   23949 C  CA    . ILE A 1 4581 ? 129.429 183.184 134.000 1.00 70.69  ? 4581 ILE A CA    1 
ATOM   23950 C  C     . ILE A 1 4581 ? 129.490 181.720 133.586 1.00 70.31  ? 4581 ILE A C     1 
ATOM   23951 O  O     . ILE A 1 4581 ? 130.545 181.208 133.194 1.00 63.98  ? 4581 ILE A O     1 
ATOM   23952 C  CB    . ILE A 1 4581 ? 129.344 183.330 135.530 1.00 74.95  ? 4581 ILE A CB    1 
ATOM   23953 C  CG1   . ILE A 1 4581 ? 129.492 184.796 135.938 1.00 74.67  ? 4581 ILE A CG1   1 
ATOM   23954 C  CG2   . ILE A 1 4581 ? 130.408 182.479 136.204 1.00 72.89  ? 4581 ILE A CG2   1 
ATOM   23955 C  CD1   . ILE A 1 4581 ? 130.755 185.444 135.447 1.00 65.64  ? 4581 ILE A CD1   1 
ATOM   23956 N  N     . SER A 1 4582 ? 128.354 181.029 133.656 1.00 71.22  ? 4582 SER A N     1 
ATOM   23957 C  CA    . SER A 1 4582 ? 128.293 179.604 133.367 1.00 61.57  ? 4582 SER A CA    1 
ATOM   23958 C  C     . SER A 1 4582 ? 126.839 179.201 133.181 1.00 62.37  ? 4582 SER A C     1 
ATOM   23959 O  O     . SER A 1 4582 ? 125.963 179.671 133.911 1.00 75.12  ? 4582 SER A O     1 
ATOM   23960 C  CB    . SER A 1 4582 ? 128.930 178.781 134.493 1.00 62.91  ? 4582 SER A CB    1 
ATOM   23961 O  OG    . SER A 1 4582 ? 128.736 177.395 134.284 1.00 66.64  ? 4582 SER A OG    1 
ATOM   23962 N  N     . THR A 1 4583 ? 126.591 178.330 132.208 1.00 53.85  ? 4583 THR A N     1 
ATOM   23963 C  CA    . THR A 1 4583 ? 125.261 177.807 131.945 1.00 54.27  ? 4583 THR A CA    1 
ATOM   23964 C  C     . THR A 1 4583 ? 125.252 176.304 132.180 1.00 55.64  ? 4583 THR A C     1 
ATOM   23965 O  O     . THR A 1 4583 ? 126.265 175.625 131.995 1.00 64.79  ? 4583 THR A O     1 
ATOM   23966 C  CB    . THR A 1 4583 ? 124.806 178.112 130.513 1.00 54.82  ? 4583 THR A CB    1 
ATOM   23967 O  OG1   . THR A 1 4583 ? 125.563 177.321 129.590 1.00 54.31  ? 4583 THR A OG1   1 
ATOM   23968 C  CG2   . THR A 1 4583 ? 125.012 179.583 130.194 1.00 55.37  ? 4583 THR A CG2   1 
ATOM   23969 N  N     . ALA A 1 4584 ? 124.098 175.788 132.590 1.00 52.82  ? 4584 ALA A N     1 
ATOM   23970 C  CA    . ALA A 1 4584 ? 123.947 174.380 132.928 1.00 57.79  ? 4584 ALA A CA    1 
ATOM   23971 C  C     . ALA A 1 4584 ? 123.282 173.638 131.778 1.00 60.91  ? 4584 ALA A C     1 
ATOM   23972 O  O     . ALA A 1 4584 ? 122.207 174.034 131.315 1.00 64.65  ? 4584 ALA A O     1 
ATOM   23973 C  CB    . ALA A 1 4584 ? 123.126 174.212 134.206 1.00 59.44  ? 4584 ALA A CB    1 
ATOM   23974 N  N     . LEU A 1 4585 ? 123.923 172.568 131.322 1.00 58.48  ? 4585 LEU A N     1 
ATOM   23975 C  CA    . LEU A 1 4585 ? 123.350 171.732 130.276 1.00 61.87  ? 4585 LEU A CA    1 
ATOM   23976 C  C     . LEU A 1 4585 ? 122.306 170.804 130.886 1.00 70.71  ? 4585 LEU A C     1 
ATOM   23977 O  O     . LEU A 1 4585 ? 122.636 170.034 131.796 1.00 74.72  ? 4585 LEU A O     1 
ATOM   23978 C  CB    . LEU A 1 4585 ? 124.441 170.926 129.586 1.00 59.41  ? 4585 LEU A CB    1 
ATOM   23979 C  CG    . LEU A 1 4585 ? 125.582 171.746 128.980 1.00 53.82  ? 4585 LEU A CG    1 
ATOM   23980 C  CD1   . LEU A 1 4585 ? 126.532 170.861 128.195 1.00 48.43  ? 4585 LEU A CD1   1 
ATOM   23981 C  CD2   . LEU A 1 4585 ? 125.031 172.853 128.099 1.00 57.13  ? 4585 LEU A CD2   1 
ATOM   23982 N  N     . PRO A 1 4586 ? 121.049 170.848 130.431 1.00 66.56  ? 4586 PRO A N     1 
ATOM   23983 C  CA    . PRO A 1 4586 ? 119.990 170.066 131.087 1.00 70.33  ? 4586 PRO A CA    1 
ATOM   23984 C  C     . PRO A 1 4586 ? 120.265 168.571 131.115 1.00 69.73  ? 4586 PRO A C     1 
ATOM   23985 O  O     . PRO A 1 4586 ? 120.327 167.962 132.187 1.00 66.63  ? 4586 PRO A O     1 
ATOM   23986 C  CB    . PRO A 1 4586 ? 118.752 170.382 130.240 1.00 79.50  ? 4586 PRO A CB    1 
ATOM   23987 C  CG    . PRO A 1 4586 ? 119.043 171.705 129.623 1.00 72.99  ? 4586 PRO A CG    1 
ATOM   23988 C  CD    . PRO A 1 4586 ? 120.520 171.727 129.375 1.00 64.01  ? 4586 PRO A CD    1 
ATOM   23989 N  N     . LEU A 1 4587 ? 120.437 167.974 129.939 1.00 69.77  ? 4587 LEU A N     1 
ATOM   23990 C  CA    . LEU A 1 4587 ? 120.726 166.548 129.830 1.00 66.22  ? 4587 LEU A CA    1 
ATOM   23991 C  C     . LEU A 1 4587 ? 121.585 166.336 128.597 1.00 68.84  ? 4587 LEU A C     1 
ATOM   23992 O  O     . LEU A 1 4587 ? 121.177 166.695 127.489 1.00 74.02  ? 4587 LEU A O     1 
ATOM   23993 C  CB    . LEU A 1 4587 ? 119.442 165.721 129.741 1.00 69.08  ? 4587 LEU A CB    1 
ATOM   23994 C  CG    . LEU A 1 4587 ? 119.624 164.209 129.586 1.00 63.39  ? 4587 LEU A CG    1 
ATOM   23995 C  CD1   . LEU A 1 4587 ? 120.015 163.575 130.905 1.00 59.49  ? 4587 LEU A CD1   1 
ATOM   23996 C  CD2   . LEU A 1 4587 ? 118.359 163.569 129.042 1.00 78.83  ? 4587 LEU A CD2   1 
ATOM   23997 N  N     . THR A 1 4588 ? 122.762 165.755 128.790 1.00 61.29  ? 4588 THR A N     1 
ATOM   23998 C  CA    . THR A 1 4588 ? 123.708 165.519 127.710 1.00 56.90  ? 4588 THR A CA    1 
ATOM   23999 C  C     . THR A 1 4588 ? 123.647 164.051 127.309 1.00 54.06  ? 4588 THR A C     1 
ATOM   24000 O  O     . THR A 1 4588 ? 123.911 163.169 128.131 1.00 63.41  ? 4588 THR A O     1 
ATOM   24001 C  CB    . THR A 1 4588 ? 125.122 165.900 128.142 1.00 60.57  ? 4588 THR A CB    1 
ATOM   24002 O  OG1   . THR A 1 4588 ? 125.158 167.290 128.489 1.00 61.48  ? 4588 THR A OG1   1 
ATOM   24003 C  CG2   . THR A 1 4588 ? 126.112 165.634 127.024 1.00 63.60  ? 4588 THR A CG2   1 
ATOM   24004 N  N     . GLN A 1 4589 ? 123.297 163.790 126.055 1.00 50.04  ? 4589 GLN A N     1 
ATOM   24005 C  CA    . GLN A 1 4589 ? 123.273 162.439 125.509 1.00 56.38  ? 4589 GLN A CA    1 
ATOM   24006 C  C     . GLN A 1 4589 ? 124.618 162.210 124.830 1.00 58.54  ? 4589 GLN A C     1 
ATOM   24007 O  O     . GLN A 1 4589 ? 124.942 162.832 123.815 1.00 67.76  ? 4589 GLN A O     1 
ATOM   24008 C  CB    . GLN A 1 4589 ? 122.110 162.262 124.543 1.00 67.16  ? 4589 GLN A CB    1 
ATOM   24009 C  CG    . GLN A 1 4589 ? 120.754 162.191 125.217 1.00 74.74  ? 4589 GLN A CG    1 
ATOM   24010 C  CD    . GLN A 1 4589 ? 119.679 161.666 124.292 1.00 87.24  ? 4589 GLN A CD    1 
ATOM   24011 O  OE1   . GLN A 1 4589 ? 119.933 161.391 123.120 1.00 86.34  ? 4589 GLN A OE1   1 
ATOM   24012 N  NE2   . GLN A 1 4589 ? 118.466 161.529 124.812 1.00 95.16  ? 4589 GLN A NE2   1 
ATOM   24013 N  N     . LEU A 1 4590 ? 125.416 161.334 125.430 1.00 51.96  ? 4590 LEU A N     1 
ATOM   24014 C  CA    . LEU A 1 4590 ? 126.673 160.871 124.854 1.00 51.70  ? 4590 LEU A CA    1 
ATOM   24015 C  C     . LEU A 1 4590 ? 126.358 159.670 123.978 1.00 54.29  ? 4590 LEU A C     1 
ATOM   24016 O  O     . LEU A 1 4590 ? 125.920 158.631 124.471 1.00 62.70  ? 4590 LEU A O     1 
ATOM   24017 C  CB    . LEU A 1 4590 ? 127.653 160.503 125.961 1.00 47.97  ? 4590 LEU A CB    1 
ATOM   24018 C  CG    . LEU A 1 4590 ? 128.055 161.610 126.935 1.00 51.33  ? 4590 LEU A CG    1 
ATOM   24019 C  CD1   . LEU A 1 4590 ? 129.157 161.126 127.858 1.00 53.13  ? 4590 LEU A CD1   1 
ATOM   24020 C  CD2   . LEU A 1 4590 ? 128.488 162.859 126.190 1.00 56.48  ? 4590 LEU A CD2   1 
ATOM   24021 N  N     . ARG A 1 4591 ? 126.553 159.804 122.672 1.00 47.24  ? 4591 ARG A N     1 
ATOM   24022 C  CA    . ARG A 1 4591 ? 126.161 158.780 121.717 1.00 49.12  ? 4591 ARG A CA    1 
ATOM   24023 C  C     . ARG A 1 4591 ? 127.402 158.304 120.978 1.00 52.34  ? 4591 ARG A C     1 
ATOM   24024 O  O     . ARG A 1 4591 ? 128.083 159.097 120.325 1.00 62.05  ? 4591 ARG A O     1 
ATOM   24025 C  CB    . ARG A 1 4591 ? 125.103 159.337 120.759 1.00 57.62  ? 4591 ARG A CB    1 
ATOM   24026 C  CG    . ARG A 1 4591 ? 124.514 158.350 119.774 1.00 64.91  ? 4591 ARG A CG    1 
ATOM   24027 C  CD    . ARG A 1 4591 ? 123.369 158.997 118.998 1.00 72.37  ? 4591 ARG A CD    1 
ATOM   24028 N  NE    . ARG A 1 4591 ? 122.702 158.067 118.094 1.00 90.94  ? 4591 ARG A NE    1 
ATOM   24029 C  CZ    . ARG A 1 4591 ? 123.016 157.892 116.818 1.00 95.11  ? 4591 ARG A CZ    1 
ATOM   24030 N  NH1   . ARG A 1 4591 ? 123.928 158.640 116.222 1.00 90.38  ? 4591 ARG A NH1   1 
ATOM   24031 N  NH2   . ARG A 1 4591 ? 122.379 156.960 116.115 1.00 95.20  ? 4591 ARG A NH2   1 
ATOM   24032 N  N     . TRP A 1 4592 ? 127.703 157.015 121.098 1.00 51.68  ? 4592 TRP A N     1 
ATOM   24033 C  CA    . TRP A 1 4592 ? 128.940 156.450 120.564 1.00 45.48  ? 4592 TRP A CA    1 
ATOM   24034 C  C     . TRP A 1 4592 ? 128.643 155.966 119.150 1.00 48.15  ? 4592 TRP A C     1 
ATOM   24035 O  O     . TRP A 1 4592 ? 128.055 154.905 118.947 1.00 60.03  ? 4592 TRP A O     1 
ATOM   24036 C  CB    . TRP A 1 4592 ? 129.448 155.329 121.460 1.00 40.41  ? 4592 TRP A CB    1 
ATOM   24037 C  CG    . TRP A 1 4592 ? 130.156 155.829 122.671 1.00 42.36  ? 4592 TRP A CG    1 
ATOM   24038 C  CD1   . TRP A 1 4592 ? 129.690 155.821 123.949 1.00 45.79  ? 4592 TRP A CD1   1 
ATOM   24039 C  CD2   . TRP A 1 4592 ? 131.457 156.423 122.721 1.00 43.54  ? 4592 TRP A CD2   1 
ATOM   24040 N  NE1   . TRP A 1 4592 ? 130.619 156.369 124.796 1.00 45.31  ? 4592 TRP A NE1   1 
ATOM   24041 C  CE2   . TRP A 1 4592 ? 131.714 156.747 124.066 1.00 44.82  ? 4592 TRP A CE2   1 
ATOM   24042 C  CE3   . TRP A 1 4592 ? 132.429 156.710 121.761 1.00 46.15  ? 4592 TRP A CE3   1 
ATOM   24043 C  CZ2   . TRP A 1 4592 ? 132.902 157.342 124.474 1.00 42.26  ? 4592 TRP A CZ2   1 
ATOM   24044 C  CZ3   . TRP A 1 4592 ? 133.607 157.301 122.169 1.00 46.53  ? 4592 TRP A CZ3   1 
ATOM   24045 C  CH2   . TRP A 1 4592 ? 133.834 157.611 123.513 1.00 44.75  ? 4592 TRP A CH2   1 
ATOM   24046 N  N     . VAL A 1 4593 ? 129.046 156.753 118.171 1.00 46.66  ? 4593 VAL A N     1 
ATOM   24047 C  CA    . VAL A 1 4593 ? 128.704 156.479 116.782 1.00 55.82  ? 4593 VAL A CA    1 
ATOM   24048 C  C     . VAL A 1 4593 ? 129.912 155.892 116.072 1.00 64.50  ? 4593 VAL A C     1 
ATOM   24049 O  O     . VAL A 1 4593 ? 131.061 156.099 116.474 1.00 64.11  ? 4593 VAL A O     1 
ATOM   24050 C  CB    . VAL A 1 4593 ? 128.205 157.758 116.079 1.00 59.55  ? 4593 VAL A CB    1 
ATOM   24051 C  CG1   . VAL A 1 4593 ? 126.980 158.283 116.779 1.00 65.39  ? 4593 VAL A CG1   1 
ATOM   24052 C  CG2   . VAL A 1 4593 ? 129.289 158.811 116.058 1.00 59.95  ? 4593 VAL A CG2   1 
ATOM   24053 N  N     . LYS A 1 4594 ? 129.652 155.140 115.008 1.00 68.53  ? 4594 LYS A N     1 
ATOM   24054 C  CA    . LYS A 1 4594 ? 130.739 154.630 114.187 1.00 70.98  ? 4594 LYS A CA    1 
ATOM   24055 C  C     . LYS A 1 4594 ? 131.491 155.788 113.546 1.00 77.01  ? 4594 LYS A C     1 
ATOM   24056 O  O     . LYS A 1 4594 ? 130.889 156.705 112.982 1.00 83.75  ? 4594 LYS A O     1 
ATOM   24057 C  CB    . LYS A 1 4594 ? 130.202 153.687 113.113 1.00 75.26  ? 4594 LYS A CB    1 
ATOM   24058 C  CG    . LYS A 1 4594 ? 131.270 152.822 112.466 1.00 83.23  ? 4594 LYS A CG    1 
ATOM   24059 C  CD    . LYS A 1 4594 ? 130.675 151.557 111.875 1.00 81.16  ? 4594 LYS A CD    1 
ATOM   24060 C  CE    . LYS A 1 4594 ? 130.813 150.385 112.830 1.00 82.38  ? 4594 LYS A CE    1 
ATOM   24061 N  NZ    . LYS A 1 4594 ? 130.364 149.113 112.204 1.00 82.43  ? 4594 LYS A NZ    1 
ATOM   24062 N  N     . GLN A 1 4595 ? 132.816 155.744 113.641 1.00 82.34  ? 4595 GLN A N     1 
ATOM   24063 C  CA    . GLN A 1 4595 ? 133.636 156.831 113.129 1.00 87.47  ? 4595 GLN A CA    1 
ATOM   24064 C  C     . GLN A 1 4595 ? 133.521 156.921 111.613 1.00 98.94  ? 4595 GLN A C     1 
ATOM   24065 O  O     . GLN A 1 4595 ? 133.548 155.908 110.908 1.00 99.55  ? 4595 GLN A O     1 
ATOM   24066 C  CB    . GLN A 1 4595 ? 135.094 156.631 113.537 1.00 88.22  ? 4595 GLN A CB    1 
ATOM   24067 C  CG    . GLN A 1 4595 ? 135.962 157.864 113.372 1.00 95.79  ? 4595 GLN A CG    1 
ATOM   24068 C  CD    . GLN A 1 4595 ? 137.173 157.845 114.283 1.00 101.61 ? 4595 GLN A CD    1 
ATOM   24069 O  OE1   . GLN A 1 4595 ? 137.655 156.781 114.670 1.00 93.97  ? 4595 GLN A OE1   1 
ATOM   24070 N  NE2   . GLN A 1 4595 ? 137.670 159.026 114.631 1.00 102.12 ? 4595 GLN A NE2   1 
ATOM   24071 N  N     . THR A 1 4596 ? 133.388 158.146 111.113 1.00 109.77 ? 4596 THR A N     1 
ATOM   24072 C  CA    . THR A 1 4596 ? 133.294 158.407 109.686 1.00 116.31 ? 4596 THR A CA    1 
ATOM   24073 C  C     . THR A 1 4596 ? 134.403 159.363 109.275 1.00 123.44 ? 4596 THR A C     1 
ATOM   24074 O  O     . THR A 1 4596 ? 134.801 160.244 110.041 1.00 125.61 ? 4596 THR A O     1 
ATOM   24075 C  CB    . THR A 1 4596 ? 131.931 159.000 109.302 1.00 115.95 ? 4596 THR A CB    1 
ATOM   24076 O  OG1   . THR A 1 4596 ? 131.790 160.300 109.889 1.00 125.26 ? 4596 THR A OG1   1 
ATOM   24077 C  CG2   . THR A 1 4596 ? 130.800 158.104 109.784 1.00 105.91 ? 4596 THR A CG2   1 
ATOM   24078 N  N     . ASN A 1 4597 ? 134.895 159.182 108.053 1.00 126.79 ? 4597 ASN A N     1 
ATOM   24079 C  CA    . ASN A 1 4597 ? 135.981 159.997 107.525 1.00 133.28 ? 4597 ASN A CA    1 
ATOM   24080 C  C     . ASN A 1 4597 ? 135.512 161.351 107.006 1.00 135.98 ? 4597 ASN A C     1 
ATOM   24081 O  O     . ASN A 1 4597 ? 136.265 162.014 106.285 1.00 135.46 ? 4597 ASN A O     1 
ATOM   24082 C  CB    . ASN A 1 4597 ? 136.713 159.239 106.415 1.00 137.58 ? 4597 ASN A CB    1 
ATOM   24083 C  CG    . ASN A 1 4597 ? 137.394 157.982 106.921 1.00 143.92 ? 4597 ASN A CG    1 
ATOM   24084 O  OD1   . ASN A 1 4597 ? 137.346 157.672 108.112 1.00 140.52 ? 4597 ASN A OD1   1 
ATOM   24085 N  ND2   . ASN A 1 4597 ? 138.032 157.249 106.016 1.00 144.81 ? 4597 ASN A ND2   1 
ATOM   24086 N  N     . THR A 1 4598 ? 134.293 161.767 107.344 1.00 138.30 ? 4598 THR A N     1 
ATOM   24087 C  CA    . THR A 1 4598 ? 133.812 163.083 106.946 1.00 139.33 ? 4598 THR A CA    1 
ATOM   24088 C  C     . THR A 1 4598 ? 134.670 164.170 107.583 1.00 138.40 ? 4598 THR A C     1 
ATOM   24089 O  O     . THR A 1 4598 ? 134.983 164.111 108.776 1.00 134.94 ? 4598 THR A O     1 
ATOM   24090 C  CB    . THR A 1 4598 ? 132.348 163.255 107.354 1.00 136.15 ? 4598 THR A CB    1 
ATOM   24091 O  OG1   . THR A 1 4598 ? 131.555 162.229 106.742 1.00 130.78 ? 4598 THR A OG1   1 
ATOM   24092 C  CG2   . THR A 1 4598 ? 131.825 164.617 106.919 1.00 129.19 ? 4598 THR A CG2   1 
ATOM   24093 N  N     . GLU A 1 4599 ? 135.056 165.159 106.781 1.00 139.60 ? 4599 GLU A N     1 
ATOM   24094 C  CA    . GLU A 1 4599 ? 135.905 166.234 107.275 1.00 136.28 ? 4599 GLU A CA    1 
ATOM   24095 C  C     . GLU A 1 4599 ? 135.159 167.082 108.297 1.00 130.65 ? 4599 GLU A C     1 
ATOM   24096 O  O     . GLU A 1 4599 ? 133.975 167.390 108.131 1.00 127.31 ? 4599 GLU A O     1 
ATOM   24097 C  CB    . GLU A 1 4599 ? 136.387 167.110 106.119 1.00 133.79 ? 4599 GLU A CB    1 
ATOM   24098 C  CG    . GLU A 1 4599 ? 137.634 166.594 105.413 1.00 141.04 ? 4599 GLU A CG    1 
ATOM   24099 C  CD    . GLU A 1 4599 ? 137.500 165.155 104.955 1.00 151.25 ? 4599 GLU A CD    1 
ATOM   24100 O  OE1   . GLU A 1 4599 ? 136.582 164.867 104.158 1.00 149.59 ? 4599 GLU A OE1   1 
ATOM   24101 O  OE2   . GLU A 1 4599 ? 138.311 164.312 105.394 1.00 155.64 ? 4599 GLU A OE2   1 
ATOM   24102 N  N     . LYS A 1 4600 ? 135.862 167.455 109.363 1.00 123.83 ? 4600 LYS A N     1 
ATOM   24103 C  CA    . LYS A 1 4600 ? 135.271 168.288 110.400 1.00 112.84 ? 4600 LYS A CA    1 
ATOM   24104 C  C     . LYS A 1 4600 ? 135.024 169.692 109.862 1.00 113.87 ? 4600 LYS A C     1 
ATOM   24105 O  O     . LYS A 1 4600 ? 135.908 170.298 109.249 1.00 114.08 ? 4600 LYS A O     1 
ATOM   24106 C  CB    . LYS A 1 4600 ? 136.186 168.330 111.624 1.00 103.16 ? 4600 LYS A CB    1 
ATOM   24107 C  CG    . LYS A 1 4600 ? 135.737 169.274 112.725 1.00 97.44  ? 4600 LYS A CG    1 
ATOM   24108 C  CD    . LYS A 1 4600 ? 136.480 168.981 114.021 1.00 87.72  ? 4600 LYS A CD    1 
ATOM   24109 C  CE    . LYS A 1 4600 ? 136.427 170.161 114.975 1.00 75.01  ? 4600 LYS A CE    1 
ATOM   24110 N  NZ    . LYS A 1 4600 ? 137.183 171.331 114.453 1.00 75.95  ? 4600 LYS A NZ    1 
ATOM   24111 N  N     . LYS A 1 4601 ? 133.819 170.206 110.089 1.00 107.92 ? 4601 LYS A N     1 
ATOM   24112 C  CA    . LYS A 1 4601 ? 133.436 171.496 109.540 1.00 103.61 ? 4601 LYS A CA    1 
ATOM   24113 C  C     . LYS A 1 4601 ? 134.210 172.626 110.213 1.00 97.00  ? 4601 LYS A C     1 
ATOM   24114 O  O     . LYS A 1 4601 ? 134.753 172.482 111.311 1.00 93.24  ? 4601 LYS A O     1 
ATOM   24115 C  CB    . LYS A 1 4601 ? 131.936 171.732 109.711 1.00 96.68  ? 4601 LYS A CB    1 
ATOM   24116 C  CG    . LYS A 1 4601 ? 131.065 170.535 109.385 1.00 99.34  ? 4601 LYS A CG    1 
ATOM   24117 C  CD    . LYS A 1 4601 ? 129.613 170.819 109.735 1.00 98.65  ? 4601 LYS A CD    1 
ATOM   24118 C  CE    . LYS A 1 4601 ? 128.733 169.604 109.507 1.00 101.69 ? 4601 LYS A CE    1 
ATOM   24119 N  NZ    . LYS A 1 4601 ? 127.315 169.882 109.862 1.00 96.54  ? 4601 LYS A NZ    1 
ATOM   24120 N  N     . ALA A 1 4602 ? 134.259 173.769 109.525 1.00 95.74  ? 4602 ALA A N     1 
ATOM   24121 C  CA    . ALA A 1 4602 ? 134.848 174.965 110.113 1.00 93.59  ? 4602 ALA A CA    1 
ATOM   24122 C  C     . ALA A 1 4602 ? 133.977 175.550 111.215 1.00 92.44  ? 4602 ALA A C     1 
ATOM   24123 O  O     . ALA A 1 4602 ? 134.469 176.349 112.019 1.00 86.82  ? 4602 ALA A O     1 
ATOM   24124 C  CB    . ALA A 1 4602 ? 135.097 176.018 109.032 1.00 93.00  ? 4602 ALA A CB    1 
ATOM   24125 N  N     . SER A 1 4603 ? 132.699 175.174 111.268 1.00 90.29  ? 4603 SER A N     1 
ATOM   24126 C  CA    . SER A 1 4603 ? 131.778 175.636 112.297 1.00 80.54  ? 4603 SER A CA    1 
ATOM   24127 C  C     . SER A 1 4603 ? 131.644 174.641 113.443 1.00 74.42  ? 4603 SER A C     1 
ATOM   24128 O  O     . SER A 1 4603 ? 130.610 174.618 114.118 1.00 71.67  ? 4603 SER A O     1 
ATOM   24129 C  CB    . SER A 1 4603 ? 130.407 175.924 111.686 1.00 73.28  ? 4603 SER A CB    1 
ATOM   24130 O  OG    . SER A 1 4603 ? 129.803 174.733 111.213 1.00 79.45  ? 4603 SER A OG    1 
ATOM   24131 N  N     . VAL A 1 4604 ? 132.662 173.815 113.669 1.00 72.31  ? 4604 VAL A N     1 
ATOM   24132 C  CA    . VAL A 1 4604 ? 132.674 172.841 114.752 1.00 66.90  ? 4604 VAL A CA    1 
ATOM   24133 C  C     . VAL A 1 4604 ? 133.839 173.170 115.673 1.00 65.46  ? 4604 VAL A C     1 
ATOM   24134 O  O     . VAL A 1 4604 ? 134.968 173.366 115.208 1.00 72.31  ? 4604 VAL A O     1 
ATOM   24135 C  CB    . VAL A 1 4604 ? 132.779 171.399 114.224 1.00 70.77  ? 4604 VAL A CB    1 
ATOM   24136 C  CG1   . VAL A 1 4604 ? 132.786 170.413 115.377 1.00 64.42  ? 4604 VAL A CG1   1 
ATOM   24137 C  CG2   . VAL A 1 4604 ? 131.631 171.102 113.282 1.00 77.19  ? 4604 VAL A CG2   1 
ATOM   24138 N  N     . VAL A 1 4605 ? 133.562 173.230 116.971 1.00 55.33  ? 4605 VAL A N     1 
ATOM   24139 C  CA    . VAL A 1 4605 ? 134.550 173.588 117.980 1.00 47.15  ? 4605 VAL A CA    1 
ATOM   24140 C  C     . VAL A 1 4605 ? 134.721 172.415 118.934 1.00 51.85  ? 4605 VAL A C     1 
ATOM   24141 O  O     . VAL A 1 4605 ? 133.749 171.737 119.287 1.00 60.00  ? 4605 VAL A O     1 
ATOM   24142 C  CB    . VAL A 1 4605 ? 134.147 174.872 118.738 1.00 40.92  ? 4605 VAL A CB    1 
ATOM   24143 C  CG1   . VAL A 1 4605 ? 132.895 174.646 119.569 1.00 48.85  ? 4605 VAL A CG1   1 
ATOM   24144 C  CG2   . VAL A 1 4605 ? 135.286 175.356 119.611 1.00 47.80  ? 4605 VAL A CG2   1 
ATOM   24145 N  N     . THR A 1 4606 ? 135.963 172.157 119.329 1.00 45.69  ? 4606 THR A N     1 
ATOM   24146 C  CA    . THR A 1 4606 ? 136.276 171.105 120.286 1.00 41.38  ? 4606 THR A CA    1 
ATOM   24147 C  C     . THR A 1 4606 ? 136.481 171.736 121.656 1.00 44.07  ? 4606 THR A C     1 
ATOM   24148 O  O     . THR A 1 4606 ? 137.396 172.546 121.841 1.00 51.92  ? 4606 THR A O     1 
ATOM   24149 C  CB    . THR A 1 4606 ? 137.519 170.326 119.860 1.00 43.03  ? 4606 THR A CB    1 
ATOM   24150 O  OG1   . THR A 1 4606 ? 137.347 169.849 118.520 1.00 53.15  ? 4606 THR A OG1   1 
ATOM   24151 C  CG2   . THR A 1 4606 ? 137.746 169.145 120.783 1.00 40.27  ? 4606 THR A CG2   1 
ATOM   24152 N  N     . LEU A 1 4607 ? 135.634 171.364 122.608 1.00 42.84  ? 4607 LEU A N     1 
ATOM   24153 C  CA    . LEU A 1 4607 ? 135.627 171.911 123.949 1.00 38.83  ? 4607 LEU A CA    1 
ATOM   24154 C  C     . LEU A 1 4607 ? 136.086 170.868 124.958 1.00 36.15  ? 4607 LEU A C     1 
ATOM   24155 O  O     . LEU A 1 4607 ? 135.624 169.723 124.921 1.00 40.77  ? 4607 LEU A O     1 
ATOM   24156 C  CB    . LEU A 1 4607 ? 134.227 172.395 124.341 1.00 36.26  ? 4607 LEU A CB    1 
ATOM   24157 C  CG    . LEU A 1 4607 ? 133.688 173.654 123.669 1.00 37.59  ? 4607 LEU A CG    1 
ATOM   24158 C  CD1   . LEU A 1 4607 ? 132.552 174.204 124.496 1.00 44.96  ? 4607 LEU A CD1   1 
ATOM   24159 C  CD2   . LEU A 1 4607 ? 134.779 174.691 123.493 1.00 38.33  ? 4607 LEU A CD2   1 
ATOM   24160 N  N     . PRO A 1 4608 ? 136.993 171.233 125.862 1.00 32.59  ? 4608 PRO A N     1 
ATOM   24161 C  CA    . PRO A 1 4608 ? 137.421 170.297 126.909 1.00 33.24  ? 4608 PRO A CA    1 
ATOM   24162 C  C     . PRO A 1 4608 ? 136.348 170.156 127.978 1.00 40.95  ? 4608 PRO A C     1 
ATOM   24163 O  O     . PRO A 1 4608 ? 135.711 171.137 128.367 1.00 48.75  ? 4608 PRO A O     1 
ATOM   24164 C  CB    . PRO A 1 4608 ? 138.684 170.954 127.473 1.00 38.36  ? 4608 PRO A CB    1 
ATOM   24165 C  CG    . PRO A 1 4608 ? 138.488 172.404 127.215 1.00 38.98  ? 4608 PRO A CG    1 
ATOM   24166 C  CD    . PRO A 1 4608 ? 137.695 172.524 125.948 1.00 37.90  ? 4608 PRO A CD    1 
ATOM   24167 N  N     . VAL A 1 4609 ? 136.150 168.932 128.456 1.00 37.96  ? 4609 VAL A N     1 
ATOM   24168 C  CA    . VAL A 1 4609 ? 135.248 168.664 129.570 1.00 34.58  ? 4609 VAL A CA    1 
ATOM   24169 C  C     . VAL A 1 4609 ? 136.141 168.466 130.788 1.00 41.71  ? 4609 VAL A C     1 
ATOM   24170 O  O     . VAL A 1 4609 ? 136.605 167.364 131.079 1.00 51.47  ? 4609 VAL A O     1 
ATOM   24171 C  CB    . VAL A 1 4609 ? 134.350 167.461 129.303 1.00 40.19  ? 4609 VAL A CB    1 
ATOM   24172 C  CG1   . VAL A 1 4609 ? 133.440 167.206 130.491 1.00 45.19  ? 4609 VAL A CG1   1 
ATOM   24173 C  CG2   . VAL A 1 4609 ? 133.534 167.692 128.052 1.00 36.80  ? 4609 VAL A CG2   1 
ATOM   24174 N  N     . TYR A 1 4610 ? 136.398 169.555 131.503 1.00 39.83  ? 4610 TYR A N     1 
ATOM   24175 C  CA    . TYR A 1 4610 ? 137.238 169.497 132.686 1.00 43.79  ? 4610 TYR A CA    1 
ATOM   24176 C  C     . TYR A 1 4610 ? 136.468 168.896 133.853 1.00 52.16  ? 4610 TYR A C     1 
ATOM   24177 O  O     . TYR A 1 4610 ? 135.237 168.956 133.911 1.00 58.91  ? 4610 TYR A O     1 
ATOM   24178 C  CB    . TYR A 1 4610 ? 137.744 170.890 133.049 1.00 45.68  ? 4610 TYR A CB    1 
ATOM   24179 C  CG    . TYR A 1 4610 ? 138.771 171.431 132.085 1.00 49.12  ? 4610 TYR A CG    1 
ATOM   24180 C  CD1   . TYR A 1 4610 ? 139.990 170.794 131.909 1.00 52.15  ? 4610 TYR A CD1   1 
ATOM   24181 C  CD2   . TYR A 1 4610 ? 138.519 172.574 131.345 1.00 46.52  ? 4610 TYR A CD2   1 
ATOM   24182 C  CE1   . TYR A 1 4610 ? 140.931 171.286 131.028 1.00 50.50  ? 4610 TYR A CE1   1 
ATOM   24183 C  CE2   . TYR A 1 4610 ? 139.452 173.072 130.463 1.00 48.45  ? 4610 TYR A CE2   1 
ATOM   24184 C  CZ    . TYR A 1 4610 ? 140.655 172.425 130.307 1.00 49.98  ? 4610 TYR A CZ    1 
ATOM   24185 O  OH    . TYR A 1 4610 ? 141.584 172.925 129.427 1.00 48.62  ? 4610 TYR A OH    1 
ATOM   24186 N  N     . LEU A 1 4611 ? 137.210 168.299 134.786 1.00 53.71  ? 4611 LEU A N     1 
ATOM   24187 C  CA    . LEU A 1 4611 ? 136.572 167.644 135.923 1.00 55.92  ? 4611 LEU A CA    1 
ATOM   24188 C  C     . LEU A 1 4611 ? 135.878 168.651 136.832 1.00 59.74  ? 4611 LEU A C     1 
ATOM   24189 O  O     . LEU A 1 4611 ? 134.755 168.410 137.286 1.00 67.60  ? 4611 LEU A O     1 
ATOM   24190 C  CB    . LEU A 1 4611 ? 137.602 166.833 136.705 1.00 61.20  ? 4611 LEU A CB    1 
ATOM   24191 C  CG    . LEU A 1 4611 ? 137.082 166.160 137.973 1.00 62.88  ? 4611 LEU A CG    1 
ATOM   24192 C  CD1   . LEU A 1 4611 ? 136.070 165.087 137.626 1.00 63.25  ? 4611 LEU A CD1   1 
ATOM   24193 C  CD2   . LEU A 1 4611 ? 138.231 165.574 138.764 1.00 70.34  ? 4611 LEU A CD2   1 
ATOM   24194 N  N     . ASN A 1 4612 ? 136.523 169.781 137.106 1.00 57.41  ? 4612 ASN A N     1 
ATOM   24195 C  CA    . ASN A 1 4612 ? 135.955 170.787 137.992 1.00 56.43  ? 4612 ASN A CA    1 
ATOM   24196 C  C     . ASN A 1 4612 ? 136.392 172.164 137.504 1.00 57.60  ? 4612 ASN A C     1 
ATOM   24197 O  O     . ASN A 1 4612 ? 137.005 172.301 136.442 1.00 62.97  ? 4612 ASN A O     1 
ATOM   24198 C  CB    . ASN A 1 4612 ? 136.364 170.524 139.447 1.00 64.00  ? 4612 ASN A CB    1 
ATOM   24199 C  CG    . ASN A 1 4612 ? 137.851 170.279 139.602 1.00 68.18  ? 4612 ASN A CG    1 
ATOM   24200 O  OD1   . ASN A 1 4612 ? 138.669 171.152 139.319 1.00 65.77  ? 4612 ASN A OD1   1 
ATOM   24201 N  ND2   . ASN A 1 4612 ? 138.209 169.086 140.059 1.00 70.45  ? 4612 ASN A ND2   1 
ATOM   24202 N  N     . PHE A 1 4613 ? 136.073 173.193 138.293 1.00 59.75  ? 4613 PHE A N     1 
ATOM   24203 C  CA    . PHE A 1 4613 ? 136.335 174.566 137.879 1.00 58.65  ? 4613 PHE A CA    1 
ATOM   24204 C  C     . PHE A 1 4613 ? 137.819 174.901 137.842 1.00 60.63  ? 4613 PHE A C     1 
ATOM   24205 O  O     . PHE A 1 4613 ? 138.200 175.878 137.192 1.00 59.50  ? 4613 PHE A O     1 
ATOM   24206 C  CB    . PHE A 1 4613 ? 135.593 175.537 138.801 1.00 67.11  ? 4613 PHE A CB    1 
ATOM   24207 C  CG    . PHE A 1 4613 ? 136.141 175.593 140.201 1.00 74.19  ? 4613 PHE A CG    1 
ATOM   24208 C  CD1   . PHE A 1 4613 ? 135.620 174.778 141.191 1.00 73.61  ? 4613 PHE A CD1   1 
ATOM   24209 C  CD2   . PHE A 1 4613 ? 137.154 176.478 140.535 1.00 72.81  ? 4613 PHE A CD2   1 
ATOM   24210 C  CE1   . PHE A 1 4613 ? 136.113 174.827 142.478 1.00 77.07  ? 4613 PHE A CE1   1 
ATOM   24211 C  CE2   . PHE A 1 4613 ? 137.650 176.530 141.821 1.00 72.84  ? 4613 PHE A CE2   1 
ATOM   24212 C  CZ    . PHE A 1 4613 ? 137.127 175.705 142.794 1.00 74.56  ? 4613 PHE A CZ    1 
ATOM   24213 N  N     . THR A 1 4614 ? 138.663 174.126 138.525 1.00 63.92  ? 4614 THR A N     1 
ATOM   24214 C  CA    . THR A 1 4614 ? 140.094 174.399 138.512 1.00 60.60  ? 4614 THR A CA    1 
ATOM   24215 C  C     . THR A 1 4614 ? 140.751 174.041 137.188 1.00 55.65  ? 4614 THR A C     1 
ATOM   24216 O  O     . THR A 1 4614 ? 141.895 174.448 136.960 1.00 58.32  ? 4614 THR A O     1 
ATOM   24217 C  CB    . THR A 1 4614 ? 140.792 173.647 139.648 1.00 64.54  ? 4614 THR A CB    1 
ATOM   24218 O  OG1   . THR A 1 4614 ? 140.885 172.257 139.318 1.00 62.69  ? 4614 THR A OG1   1 
ATOM   24219 C  CG2   . THR A 1 4614 ? 140.021 173.809 140.944 1.00 69.13  ? 4614 THR A CG2   1 
ATOM   24220 N  N     . ARG A 1 4615 ? 140.060 173.299 136.320 1.00 52.95  ? 4615 ARG A N     1 
ATOM   24221 C  CA    . ARG A 1 4615 ? 140.572 172.935 134.999 1.00 48.44  ? 4615 ARG A CA    1 
ATOM   24222 C  C     . ARG A 1 4615 ? 141.908 172.205 135.103 1.00 54.84  ? 4615 ARG A C     1 
ATOM   24223 O  O     . ARG A 1 4615 ? 142.826 172.434 134.314 1.00 56.63  ? 4615 ARG A O     1 
ATOM   24224 C  CB    . ARG A 1 4615 ? 140.693 174.165 134.098 1.00 44.92  ? 4615 ARG A CB    1 
ATOM   24225 C  CG    . ARG A 1 4615 ? 139.400 174.944 133.950 1.00 43.48  ? 4615 ARG A CG    1 
ATOM   24226 C  CD    . ARG A 1 4615 ? 139.418 175.822 132.717 1.00 41.60  ? 4615 ARG A CD    1 
ATOM   24227 N  NE    . ARG A 1 4615 ? 138.162 176.542 132.547 1.00 41.08  ? 4615 ARG A NE    1 
ATOM   24228 C  CZ    . ARG A 1 4615 ? 137.833 177.225 131.460 1.00 40.37  ? 4615 ARG A CZ    1 
ATOM   24229 N  NH1   . ARG A 1 4615 ? 138.641 177.292 130.415 1.00 38.43  ? 4615 ARG A NH1   1 
ATOM   24230 N  NH2   . ARG A 1 4615 ? 136.664 177.855 131.419 1.00 39.50  ? 4615 ARG A NH2   1 
ATOM   24231 N  N     . ALA A 1 4616 ? 142.019 171.316 136.087 1.00 60.76  ? 4616 ALA A N     1 
ATOM   24232 C  CA    . ALA A 1 4616 ? 143.249 170.572 136.318 1.00 59.51  ? 4616 ALA A CA    1 
ATOM   24233 C  C     . ALA A 1 4616 ? 143.215 169.161 135.754 1.00 64.93  ? 4616 ALA A C     1 
ATOM   24234 O  O     . ALA A 1 4616 ? 144.268 168.628 135.391 1.00 68.50  ? 4616 ALA A O     1 
ATOM   24235 C  CB    . ALA A 1 4616 ? 143.555 170.505 137.818 1.00 59.28  ? 4616 ALA A CB    1 
ATOM   24236 N  N     . ASP A 1 4617 ? 142.040 168.544 135.671 1.00 62.06  ? 4617 ASP A N     1 
ATOM   24237 C  CA    . ASP A 1 4617 ? 141.890 167.199 135.137 1.00 61.47  ? 4617 ASP A CA    1 
ATOM   24238 C  C     . ASP A 1 4617 ? 140.982 167.251 133.918 1.00 60.36  ? 4617 ASP A C     1 
ATOM   24239 O  O     . ASP A 1 4617 ? 139.871 167.784 133.990 1.00 63.88  ? 4617 ASP A O     1 
ATOM   24240 C  CB    . ASP A 1 4617 ? 141.316 166.249 136.193 1.00 66.75  ? 4617 ASP A CB    1 
ATOM   24241 C  CG    . ASP A 1 4617 ? 141.342 164.794 135.754 1.00 77.55  ? 4617 ASP A CG    1 
ATOM   24242 O  OD1   . ASP A 1 4617 ? 141.777 164.513 134.618 1.00 77.76  ? 4617 ASP A OD1   1 
ATOM   24243 O  OD2   . ASP A 1 4617 ? 140.925 163.927 136.549 1.00 83.65  ? 4617 ASP A OD2   1 
ATOM   24244 N  N     . LEU A 1 4618 ? 141.455 166.696 132.806 1.00 60.06  ? 4618 LEU A N     1 
ATOM   24245 C  CA    . LEU A 1 4618 ? 140.702 166.655 131.558 1.00 55.31  ? 4618 LEU A CA    1 
ATOM   24246 C  C     . LEU A 1 4618 ? 140.038 165.288 131.442 1.00 58.59  ? 4618 LEU A C     1 
ATOM   24247 O  O     . LEU A 1 4618 ? 140.714 164.256 131.492 1.00 67.78  ? 4618 LEU A O     1 
ATOM   24248 C  CB    . LEU A 1 4618 ? 141.614 166.926 130.365 1.00 53.27  ? 4618 LEU A CB    1 
ATOM   24249 C  CG    . LEU A 1 4618 ? 140.970 166.778 128.988 1.00 51.74  ? 4618 LEU A CG    1 
ATOM   24250 C  CD1   . LEU A 1 4618 ? 139.994 167.905 128.744 1.00 48.12  ? 4618 LEU A CD1   1 
ATOM   24251 C  CD2   . LEU A 1 4618 ? 142.024 166.739 127.897 1.00 56.14  ? 4618 LEU A CD2   1 
ATOM   24252 N  N     . ILE A 1 4619 ? 138.714 165.281 131.285 1.00 48.59  ? 4619 ILE A N     1 
ATOM   24253 C  CA    . ILE A 1 4619 ? 137.988 164.019 131.199 1.00 52.40  ? 4619 ILE A CA    1 
ATOM   24254 C  C     . ILE A 1 4619 ? 137.891 163.551 129.752 1.00 55.69  ? 4619 ILE A C     1 
ATOM   24255 O  O     . ILE A 1 4619 ? 138.262 162.418 129.427 1.00 64.51  ? 4619 ILE A O     1 
ATOM   24256 C  CB    . ILE A 1 4619 ? 136.599 164.156 131.848 1.00 51.42  ? 4619 ILE A CB    1 
ATOM   24257 C  CG1   . ILE A 1 4619 ? 136.721 164.736 133.257 1.00 56.87  ? 4619 ILE A CG1   1 
ATOM   24258 C  CG2   . ILE A 1 4619 ? 135.911 162.808 131.916 1.00 50.29  ? 4619 ILE A CG2   1 
ATOM   24259 C  CD1   . ILE A 1 4619 ? 137.730 164.023 134.131 1.00 62.07  ? 4619 ILE A CD1   1 
ATOM   24260 N  N     . PHE A 1 4620 ? 137.403 164.412 128.864 1.00 48.01  ? 4620 PHE A N     1 
ATOM   24261 C  CA    . PHE A 1 4620 ? 137.316 164.112 127.437 1.00 45.59  ? 4620 PHE A CA    1 
ATOM   24262 C  C     . PHE A 1 4620 ? 137.060 165.423 126.700 1.00 45.45  ? 4620 PHE A C     1 
ATOM   24263 O  O     . PHE A 1 4620 ? 137.167 166.510 127.275 1.00 47.53  ? 4620 PHE A O     1 
ATOM   24264 C  CB    . PHE A 1 4620 ? 136.246 163.056 127.141 1.00 42.84  ? 4620 PHE A CB    1 
ATOM   24265 C  CG    . PHE A 1 4620 ? 134.851 163.462 127.527 1.00 47.37  ? 4620 PHE A CG    1 
ATOM   24266 C  CD1   . PHE A 1 4620 ? 134.452 163.448 128.851 1.00 49.70  ? 4620 PHE A CD1   1 
ATOM   24267 C  CD2   . PHE A 1 4620 ? 133.928 163.816 126.563 1.00 48.52  ? 4620 PHE A CD2   1 
ATOM   24268 C  CE1   . PHE A 1 4620 ? 133.171 163.810 129.208 1.00 47.54  ? 4620 PHE A CE1   1 
ATOM   24269 C  CE2   . PHE A 1 4620 ? 132.644 164.174 126.917 1.00 45.83  ? 4620 PHE A CE2   1 
ATOM   24270 C  CZ    . PHE A 1 4620 ? 132.266 164.172 128.239 1.00 41.22  ? 4620 PHE A CZ    1 
ATOM   24271 N  N     . THR A 1 4621 ? 136.760 165.317 125.409 1.00 43.21  ? 4621 THR A N     1 
ATOM   24272 C  CA    . THR A 1 4621 ? 136.485 166.476 124.574 1.00 40.82  ? 4621 THR A CA    1 
ATOM   24273 C  C     . THR A 1 4621 ? 135.160 166.288 123.848 1.00 44.49  ? 4621 THR A C     1 
ATOM   24274 O  O     . THR A 1 4621 ? 134.763 165.164 123.529 1.00 53.94  ? 4621 THR A O     1 
ATOM   24275 C  CB    . THR A 1 4621 ? 137.600 166.718 123.547 1.00 41.29  ? 4621 THR A CB    1 
ATOM   24276 O  OG1   . THR A 1 4621 ? 137.469 165.787 122.466 1.00 56.10  ? 4621 THR A OG1   1 
ATOM   24277 C  CG2   . THR A 1 4621 ? 138.970 166.562 124.185 1.00 34.19  ? 4621 THR A CG2   1 
ATOM   24278 N  N     . VAL A 1 4622 ? 134.480 167.401 123.587 1.00 42.02  ? 4622 VAL A N     1 
ATOM   24279 C  CA    . VAL A 1 4622 ? 133.178 167.395 122.933 1.00 46.74  ? 4622 VAL A CA    1 
ATOM   24280 C  C     . VAL A 1 4622 ? 133.243 168.265 121.686 1.00 50.41  ? 4622 VAL A C     1 
ATOM   24281 O  O     . VAL A 1 4622 ? 133.761 169.385 121.724 1.00 53.20  ? 4622 VAL A O     1 
ATOM   24282 C  CB    . VAL A 1 4622 ? 132.061 167.881 123.881 1.00 45.22  ? 4622 VAL A CB    1 
ATOM   24283 C  CG1   . VAL A 1 4622 ? 131.869 166.893 125.001 1.00 46.14  ? 4622 VAL A CG1   1 
ATOM   24284 C  CG2   . VAL A 1 4622 ? 132.389 169.247 124.452 1.00 46.91  ? 4622 VAL A CG2   1 
ATOM   24285 N  N     . ASP A 1 4623 ? 132.728 167.746 120.578 1.00 50.79  ? 4623 ASP A N     1 
ATOM   24286 C  CA    . ASP A 1 4623 ? 132.619 168.509 119.343 1.00 49.75  ? 4623 ASP A CA    1 
ATOM   24287 C  C     . ASP A 1 4623 ? 131.225 169.118 119.272 1.00 55.78  ? 4623 ASP A C     1 
ATOM   24288 O  O     . ASP A 1 4623 ? 130.228 168.391 119.213 1.00 64.03  ? 4623 ASP A O     1 
ATOM   24289 C  CB    . ASP A 1 4623 ? 132.890 167.630 118.124 1.00 61.73  ? 4623 ASP A CB    1 
ATOM   24290 C  CG    . ASP A 1 4623 ? 134.307 167.103 118.092 1.00 67.53  ? 4623 ASP A CG    1 
ATOM   24291 O  OD1   . ASP A 1 4623 ? 134.971 167.123 119.149 1.00 64.91  ? 4623 ASP A OD1   1 
ATOM   24292 O  OD2   . ASP A 1 4623 ? 134.759 166.670 117.011 1.00 68.66  ? 4623 ASP A OD2   1 
ATOM   24293 N  N     . PHE A 1 4624 ? 131.161 170.443 119.281 1.00 52.66  ? 4624 PHE A N     1 
ATOM   24294 C  CA    . PHE A 1 4624 ? 129.911 171.183 119.247 1.00 52.40  ? 4624 PHE A CA    1 
ATOM   24295 C  C     . PHE A 1 4624 ? 129.847 172.004 117.968 1.00 53.72  ? 4624 PHE A C     1 
ATOM   24296 O  O     . PHE A 1 4624 ? 130.860 172.257 117.314 1.00 59.14  ? 4624 PHE A O     1 
ATOM   24297 C  CB    . PHE A 1 4624 ? 129.779 172.094 120.470 1.00 51.85  ? 4624 PHE A CB    1 
ATOM   24298 C  CG    . PHE A 1 4624 ? 129.081 171.455 121.632 1.00 51.32  ? 4624 PHE A CG    1 
ATOM   24299 C  CD1   . PHE A 1 4624 ? 127.771 171.025 121.521 1.00 54.56  ? 4624 PHE A CD1   1 
ATOM   24300 C  CD2   . PHE A 1 4624 ? 129.735 171.290 122.840 1.00 45.51  ? 4624 PHE A CD2   1 
ATOM   24301 C  CE1   . PHE A 1 4624 ? 127.130 170.438 122.591 1.00 54.61  ? 4624 PHE A CE1   1 
ATOM   24302 C  CE2   . PHE A 1 4624 ? 129.099 170.705 123.913 1.00 48.71  ? 4624 PHE A CE2   1 
ATOM   24303 C  CZ    . PHE A 1 4624 ? 127.795 170.280 123.789 1.00 54.17  ? 4624 PHE A CZ    1 
ATOM   24304 N  N     . GLU A 1 4625 ? 128.640 172.432 117.617 1.00 50.46  ? 4625 GLU A N     1 
ATOM   24305 C  CA    . GLU A 1 4625 ? 128.405 173.167 116.383 1.00 52.56  ? 4625 GLU A CA    1 
ATOM   24306 C  C     . GLU A 1 4625 ? 128.251 174.650 116.688 1.00 59.12  ? 4625 GLU A C     1 
ATOM   24307 O  O     . GLU A 1 4625 ? 127.470 175.032 117.565 1.00 67.15  ? 4625 GLU A O     1 
ATOM   24308 C  CB    . GLU A 1 4625 ? 127.163 172.638 115.664 1.00 59.62  ? 4625 GLU A CB    1 
ATOM   24309 C  CG    . GLU A 1 4625 ? 126.664 173.538 114.548 1.00 72.48  ? 4625 GLU A CG    1 
ATOM   24310 C  CD    . GLU A 1 4625 ? 127.313 173.226 113.214 1.00 82.61  ? 4625 GLU A CD    1 
ATOM   24311 O  OE1   . GLU A 1 4625 ? 127.237 174.075 112.301 1.00 82.02  ? 4625 GLU A OE1   1 
ATOM   24312 O  OE2   . GLU A 1 4625 ? 127.898 172.131 113.078 1.00 85.29  ? 4625 GLU A OE2   1 
ATOM   24313 N  N     . ILE A 1 4626 ? 129.000 175.480 115.964 1.00 63.49  ? 4626 ILE A N     1 
ATOM   24314 C  CA    . ILE A 1 4626 ? 128.947 176.922 116.167 1.00 61.02  ? 4626 ILE A CA    1 
ATOM   24315 C  C     . ILE A 1 4626 ? 127.649 177.472 115.596 1.00 63.82  ? 4626 ILE A C     1 
ATOM   24316 O  O     . ILE A 1 4626 ? 127.272 177.166 114.457 1.00 68.37  ? 4626 ILE A O     1 
ATOM   24317 C  CB    . ILE A 1 4626 ? 130.164 177.600 115.523 1.00 64.63  ? 4626 ILE A CB    1 
ATOM   24318 C  CG1   . ILE A 1 4626 ? 131.459 177.058 116.123 1.00 59.26  ? 4626 ILE A CG1   1 
ATOM   24319 C  CG2   . ILE A 1 4626 ? 130.093 179.100 115.703 1.00 67.02  ? 4626 ILE A CG2   1 
ATOM   24320 C  CD1   . ILE A 1 4626 ? 131.576 177.308 117.596 1.00 56.35  ? 4626 ILE A CD1   1 
ATOM   24321 N  N     . ALA A 1 4627 ? 126.960 178.290 116.383 1.00 62.33  ? 4627 ALA A N     1 
ATOM   24322 C  CA    . ALA A 1 4627 ? 125.748 178.962 115.943 1.00 66.34  ? 4627 ALA A CA    1 
ATOM   24323 C  C     . ALA A 1 4627 ? 126.072 180.381 115.495 1.00 73.72  ? 4627 ALA A C     1 
ATOM   24324 O  O     . ALA A 1 4627 ? 126.962 181.036 116.043 1.00 77.51  ? 4627 ALA A O     1 
ATOM   24325 C  CB    . ALA A 1 4627 ? 124.701 178.995 117.056 1.00 66.30  ? 4627 ALA A CB    1 
ATOM   24326 N  N     . THR A 1 4628 ? 125.335 180.846 114.484 1.00 79.65  ? 4628 THR A N     1 
ATOM   24327 C  CA    . THR A 1 4628 ? 125.510 182.174 113.901 1.00 89.69  ? 4628 THR A CA    1 
ATOM   24328 C  C     . THR A 1 4628 ? 126.935 182.387 113.404 1.00 86.68  ? 4628 THR A C     1 
ATOM   24329 O  O     . THR A 1 4628 ? 127.697 181.427 113.243 1.00 80.22  ? 4628 THR A O     1 
ATOM   24330 C  CB    . THR A 1 4628 ? 125.131 183.270 114.905 1.00 91.77  ? 4628 THR A CB    1 
ATOM   24331 O  OG1   . THR A 1 4628 ? 126.164 183.404 115.890 1.00 87.49  ? 4628 THR A OG1   1 
ATOM   24332 C  CG2   . THR A 1 4628 ? 123.810 182.941 115.592 1.00 83.01  ? 4628 THR A CG2   1 
ATOM   24333 N  N     . LYS A 1 4629 ? 127.300 183.643 113.146 1.00 85.31  ? 4629 LYS A N     1 
ATOM   24334 C  CA    . LYS A 1 4629 ? 128.623 183.978 112.619 1.00 86.01  ? 4629 LYS A CA    1 
ATOM   24335 C  C     . LYS A 1 4629 ? 129.577 184.218 113.786 1.00 84.41  ? 4629 LYS A C     1 
ATOM   24336 O  O     . LYS A 1 4629 ? 129.884 185.349 114.167 1.00 89.49  ? 4629 LYS A O     1 
ATOM   24337 C  CB    . LYS A 1 4629 ? 128.538 185.184 111.691 1.00 95.45  ? 4629 LYS A CB    1 
ATOM   24338 C  CG    . LYS A 1 4629 ? 127.623 186.294 112.190 1.00 99.33  ? 4629 LYS A CG    1 
ATOM   24339 C  CD    . LYS A 1 4629 ? 127.644 187.495 111.258 1.00 102.85 ? 4629 LYS A CD    1 
ATOM   24340 C  CE    . LYS A 1 4629 ? 127.193 187.117 109.857 1.00 101.28 ? 4629 LYS A CE    1 
ATOM   24341 N  NZ    . LYS A 1 4629 ? 127.222 188.282 108.929 1.00 101.59 ? 4629 LYS A NZ    1 
ATOM   24342 N  N     . GLU A 1 4630 ? 130.057 183.118 114.361 1.00 77.21  ? 4630 GLU A N     1 
ATOM   24343 C  CA    . GLU A 1 4630 ? 131.000 183.155 115.470 1.00 72.28  ? 4630 GLU A CA    1 
ATOM   24344 C  C     . GLU A 1 4630 ? 132.261 182.396 115.088 1.00 70.13  ? 4630 GLU A C     1 
ATOM   24345 O  O     . GLU A 1 4630 ? 132.186 181.266 114.596 1.00 74.14  ? 4630 GLU A O     1 
ATOM   24346 C  CB    . GLU A 1 4630 ? 130.386 182.557 116.736 1.00 67.89  ? 4630 GLU A CB    1 
ATOM   24347 C  CG    . GLU A 1 4630 ? 129.291 183.404 117.351 1.00 71.83  ? 4630 GLU A CG    1 
ATOM   24348 C  CD    . GLU A 1 4630 ? 128.522 182.660 118.418 1.00 72.22  ? 4630 GLU A CD    1 
ATOM   24349 O  OE1   . GLU A 1 4630 ? 128.831 181.474 118.650 1.00 70.70  ? 4630 GLU A OE1   1 
ATOM   24350 O  OE2   . GLU A 1 4630 ? 127.611 183.260 119.023 1.00 76.08  ? 4630 GLU A OE2   1 
ATOM   24351 N  N     . ASP A 1 4631 ? 133.408 183.018 115.310 1.00 63.36  ? 4631 ASP A N     1 
ATOM   24352 C  CA    . ASP A 1 4631 ? 134.685 182.383 115.023 1.00 63.39  ? 4631 ASP A CA    1 
ATOM   24353 C  C     . ASP A 1 4631 ? 135.048 181.403 116.137 1.00 60.44  ? 4631 ASP A C     1 
ATOM   24354 O  O     . ASP A 1 4631 ? 134.897 181.724 117.318 1.00 61.23  ? 4631 ASP A O     1 
ATOM   24355 C  CB    . ASP A 1 4631 ? 135.783 183.435 114.882 1.00 68.78  ? 4631 ASP A CB    1 
ATOM   24356 C  CG    . ASP A 1 4631 ? 136.820 183.062 113.842 1.00 76.99  ? 4631 ASP A CG    1 
ATOM   24357 O  OD1   . ASP A 1 4631 ? 136.534 182.186 112.999 1.00 76.42  ? 4631 ASP A OD1   1 
ATOM   24358 O  OD2   . ASP A 1 4631 ? 137.924 183.647 113.868 1.00 78.17  ? 4631 ASP A OD2   1 
ATOM   24359 N  N     . PRO A 1 4632 ? 135.512 180.199 115.793 1.00 56.55  ? 4632 PRO A N     1 
ATOM   24360 C  CA    . PRO A 1 4632 ? 136.010 179.288 116.836 1.00 53.15  ? 4632 PRO A CA    1 
ATOM   24361 C  C     . PRO A 1 4632 ? 137.180 179.858 117.616 1.00 56.71  ? 4632 PRO A C     1 
ATOM   24362 O  O     . PRO A 1 4632 ? 137.391 179.476 118.775 1.00 59.44  ? 4632 PRO A O     1 
ATOM   24363 C  CB    . PRO A 1 4632 ? 136.413 178.038 116.042 1.00 53.13  ? 4632 PRO A CB    1 
ATOM   24364 C  CG    . PRO A 1 4632 ? 135.575 178.091 114.815 1.00 64.74  ? 4632 PRO A CG    1 
ATOM   24365 C  CD    . PRO A 1 4632 ? 135.445 179.546 114.476 1.00 62.88  ? 4632 PRO A CD    1 
ATOM   24366 N  N     . ARG A 1 4633 ? 137.955 180.759 117.009 1.00 56.80  ? 4633 ARG A N     1 
ATOM   24367 C  CA    . ARG A 1 4633 ? 139.037 181.412 117.736 1.00 52.03  ? 4633 ARG A CA    1 
ATOM   24368 C  C     . ARG A 1 4633 ? 138.504 182.224 118.906 1.00 48.67  ? 4633 ARG A C     1 
ATOM   24369 O  O     . ARG A 1 4633 ? 139.184 182.356 119.928 1.00 50.80  ? 4633 ARG A O     1 
ATOM   24370 C  CB    . ARG A 1 4633 ? 139.849 182.302 116.795 1.00 59.29  ? 4633 ARG A CB    1 
ATOM   24371 C  CG    . ARG A 1 4633 ? 140.853 181.559 115.920 1.00 70.63  ? 4633 ARG A CG    1 
ATOM   24372 C  CD    . ARG A 1 4633 ? 140.180 180.810 114.783 1.00 79.75  ? 4633 ARG A CD    1 
ATOM   24373 N  NE    . ARG A 1 4633 ? 141.144 180.146 113.915 1.00 95.04  ? 4633 ARG A NE    1 
ATOM   24374 C  CZ    . ARG A 1 4633 ? 141.725 180.718 112.869 1.00 98.56  ? 4633 ARG A CZ    1 
ATOM   24375 N  NH1   . ARG A 1 4633 ? 141.459 181.969 112.530 1.00 91.63  ? 4633 ARG A NH1   1 
ATOM   24376 N  NH2   . ARG A 1 4633 ? 142.591 180.016 112.143 1.00 98.32  ? 4633 ARG A NH2   1 
ATOM   24377 N  N     . SER A 1 4634 ? 137.294 182.772 118.780 1.00 49.11  ? 4634 SER A N     1 
ATOM   24378 C  CA    . SER A 1 4634 ? 136.667 183.440 119.914 1.00 45.77  ? 4634 SER A CA    1 
ATOM   24379 C  C     . SER A 1 4634 ? 136.400 182.458 121.047 1.00 44.62  ? 4634 SER A C     1 
ATOM   24380 O  O     . SER A 1 4634 ? 136.605 182.784 122.222 1.00 46.97  ? 4634 SER A O     1 
ATOM   24381 C  CB    . SER A 1 4634 ? 135.371 184.118 119.473 1.00 48.93  ? 4634 SER A CB    1 
ATOM   24382 O  OG    . SER A 1 4634 ? 135.606 185.018 118.406 1.00 59.25  ? 4634 SER A OG    1 
ATOM   24383 N  N     . PHE A 1 4635 ? 135.943 181.249 120.714 1.00 43.30  ? 4635 PHE A N     1 
ATOM   24384 C  CA    . PHE A 1 4635 ? 135.736 180.230 121.737 1.00 38.77  ? 4635 PHE A CA    1 
ATOM   24385 C  C     . PHE A 1 4635 ? 137.053 179.832 122.386 1.00 43.30  ? 4635 PHE A C     1 
ATOM   24386 O  O     . PHE A 1 4635 ? 137.104 179.558 123.590 1.00 48.84  ? 4635 PHE A O     1 
ATOM   24387 C  CB    . PHE A 1 4635 ? 135.046 179.004 121.138 1.00 35.19  ? 4635 PHE A CB    1 
ATOM   24388 C  CG    . PHE A 1 4635 ? 133.590 179.209 120.838 1.00 40.05  ? 4635 PHE A CG    1 
ATOM   24389 C  CD1   . PHE A 1 4635 ? 133.188 180.065 119.830 1.00 45.13  ? 4635 PHE A CD1   1 
ATOM   24390 C  CD2   . PHE A 1 4635 ? 132.623 178.550 121.573 1.00 39.44  ? 4635 PHE A CD2   1 
ATOM   24391 C  CE1   . PHE A 1 4635 ? 131.852 180.255 119.559 1.00 44.63  ? 4635 PHE A CE1   1 
ATOM   24392 C  CE2   . PHE A 1 4635 ? 131.286 178.738 121.305 1.00 42.70  ? 4635 PHE A CE2   1 
ATOM   24393 C  CZ    . PHE A 1 4635 ? 130.901 179.591 120.297 1.00 46.57  ? 4635 PHE A CZ    1 
ATOM   24394 N  N     . TYR A 1 4636 ? 138.128 179.778 121.599 1.00 42.94  ? 4636 TYR A N     1 
ATOM   24395 C  CA    . TYR A 1 4636 ? 139.429 179.424 122.159 1.00 38.83  ? 4636 TYR A CA    1 
ATOM   24396 C  C     . TYR A 1 4636 ? 139.946 180.517 123.087 1.00 39.43  ? 4636 TYR A C     1 
ATOM   24397 O  O     . TYR A 1 4636 ? 140.471 180.227 124.168 1.00 40.29  ? 4636 TYR A O     1 
ATOM   24398 C  CB    . TYR A 1 4636 ? 140.432 179.157 121.035 1.00 41.48  ? 4636 TYR A CB    1 
ATOM   24399 C  CG    . TYR A 1 4636 ? 140.016 178.074 120.061 1.00 47.20  ? 4636 TYR A CG    1 
ATOM   24400 C  CD1   . TYR A 1 4636 ? 139.054 177.133 120.401 1.00 50.62  ? 4636 TYR A CD1   1 
ATOM   24401 C  CD2   . TYR A 1 4636 ? 140.581 178.000 118.797 1.00 48.87  ? 4636 TYR A CD2   1 
ATOM   24402 C  CE1   . TYR A 1 4636 ? 138.671 176.152 119.512 1.00 48.95  ? 4636 TYR A CE1   1 
ATOM   24403 C  CE2   . TYR A 1 4636 ? 140.204 177.021 117.902 1.00 49.91  ? 4636 TYR A CE2   1 
ATOM   24404 C  CZ    . TYR A 1 4636 ? 139.248 176.099 118.265 1.00 53.09  ? 4636 TYR A CZ    1 
ATOM   24405 O  OH    . TYR A 1 4636 ? 138.867 175.118 117.379 1.00 62.09  ? 4636 TYR A OH    1 
ATOM   24406 N  N     . GLU A 1 4637 ? 139.804 181.781 122.683 1.00 40.67  ? 4637 GLU A N     1 
ATOM   24407 C  CA    . GLU A 1 4637 ? 140.338 182.886 123.474 1.00 35.02  ? 4637 GLU A CA    1 
ATOM   24408 C  C     . GLU A 1 4637 ? 139.525 183.109 124.742 1.00 38.02  ? 4637 GLU A C     1 
ATOM   24409 O  O     . GLU A 1 4637 ? 140.089 183.334 125.818 1.00 41.97  ? 4637 GLU A O     1 
ATOM   24410 C  CB    . GLU A 1 4637 ? 140.383 184.162 122.634 1.00 40.15  ? 4637 GLU A CB    1 
ATOM   24411 C  CG    . GLU A 1 4637 ? 141.384 184.119 121.496 1.00 53.87  ? 4637 GLU A CG    1 
ATOM   24412 C  CD    . GLU A 1 4637 ? 141.427 185.415 120.712 1.00 68.67  ? 4637 GLU A CD    1 
ATOM   24413 O  OE1   . GLU A 1 4637 ? 140.369 185.836 120.199 1.00 69.46  ? 4637 GLU A OE1   1 
ATOM   24414 O  OE2   . GLU A 1 4637 ? 142.518 186.011 120.605 1.00 69.31  ? 4637 GLU A OE2   1 
ATOM   24415 N  N     . ARG A 1 4638 ? 138.198 183.057 124.641 1.00 37.97  ? 4638 ARG A N     1 
ATOM   24416 C  CA    . ARG A 1 4638 ? 137.363 183.327 125.804 1.00 35.97  ? 4638 ARG A CA    1 
ATOM   24417 C  C     . ARG A 1 4638 ? 137.371 182.192 126.818 1.00 38.00  ? 4638 ARG A C     1 
ATOM   24418 O  O     . ARG A 1 4638 ? 136.764 182.336 127.883 1.00 43.64  ? 4638 ARG A O     1 
ATOM   24419 C  CB    . ARG A 1 4638 ? 135.934 183.627 125.359 1.00 35.85  ? 4638 ARG A CB    1 
ATOM   24420 C  CG    . ARG A 1 4638 ? 135.798 184.949 124.629 1.00 38.51  ? 4638 ARG A CG    1 
ATOM   24421 C  CD    . ARG A 1 4638 ? 134.439 185.083 123.984 1.00 46.11  ? 4638 ARG A CD    1 
ATOM   24422 N  NE    . ARG A 1 4638 ? 133.368 185.155 124.969 1.00 46.26  ? 4638 ARG A NE    1 
ATOM   24423 C  CZ    . ARG A 1 4638 ? 132.826 186.283 125.403 1.00 54.28  ? 4638 ARG A CZ    1 
ATOM   24424 N  NH1   . ARG A 1 4638 ? 133.231 187.460 124.957 1.00 55.24  ? 4638 ARG A NH1   1 
ATOM   24425 N  NH2   . ARG A 1 4638 ? 131.849 186.229 126.303 1.00 60.54  ? 4638 ARG A NH2   1 
ATOM   24426 N  N     . GLY A 1 4639 ? 138.035 181.081 126.521 1.00 39.66  ? 4639 GLY A N     1 
ATOM   24427 C  CA    . GLY A 1 4639 ? 138.125 179.986 127.466 1.00 36.64  ? 4639 GLY A CA    1 
ATOM   24428 C  C     . GLY A 1 4639 ? 136.843 179.213 127.657 1.00 41.17  ? 4639 GLY A C     1 
ATOM   24429 O  O     . GLY A 1 4639 ? 136.532 178.805 128.783 1.00 42.48  ? 4639 GLY A O     1 
ATOM   24430 N  N     . VAL A 1 4640 ? 136.080 179.000 126.584 1.00 38.32  ? 4640 VAL A N     1 
ATOM   24431 C  CA    . VAL A 1 4640 ? 134.859 178.212 126.681 1.00 33.11  ? 4640 VAL A CA    1 
ATOM   24432 C  C     . VAL A 1 4640 ? 135.219 176.756 126.924 1.00 39.06  ? 4640 VAL A C     1 
ATOM   24433 O  O     . VAL A 1 4640 ? 136.113 176.202 126.273 1.00 49.12  ? 4640 VAL A O     1 
ATOM   24434 C  CB    . VAL A 1 4640 ? 134.014 178.381 125.412 1.00 31.86  ? 4640 VAL A CB    1 
ATOM   24435 C  CG1   . VAL A 1 4640 ? 132.683 177.680 125.569 1.00 34.97  ? 4640 VAL A CG1   1 
ATOM   24436 C  CG2   . VAL A 1 4640 ? 133.809 179.852 125.110 1.00 37.91  ? 4640 VAL A CG2   1 
ATOM   24437 N  N     . ALA A 1 4641 ? 134.526 176.129 127.869 1.00 37.34  ? 4641 ALA A N     1 
ATOM   24438 C  CA    . ALA A 1 4641 ? 134.802 174.745 128.224 1.00 36.35  ? 4641 ALA A CA    1 
ATOM   24439 C  C     . ALA A 1 4641 ? 133.560 174.147 128.865 1.00 39.32  ? 4641 ALA A C     1 
ATOM   24440 O  O     . ALA A 1 4641 ? 132.536 174.813 129.034 1.00 47.54  ? 4641 ALA A O     1 
ATOM   24441 C  CB    . ALA A 1 4641 ? 136.007 174.637 129.161 1.00 31.52  ? 4641 ALA A CB    1 
ATOM   24442 N  N     . VAL A 1 4642 ? 133.664 172.868 129.210 1.00 34.07  ? 4642 VAL A N     1 
ATOM   24443 C  CA    . VAL A 1 4642 ? 132.607 172.138 129.898 1.00 34.84  ? 4642 VAL A CA    1 
ATOM   24444 C  C     . VAL A 1 4642 ? 133.180 171.609 131.205 1.00 43.07  ? 4642 VAL A C     1 
ATOM   24445 O  O     . VAL A 1 4642 ? 134.316 171.124 131.242 1.00 52.37  ? 4642 VAL A O     1 
ATOM   24446 C  CB    . VAL A 1 4642 ? 132.050 170.996 129.031 1.00 37.56  ? 4642 VAL A CB    1 
ATOM   24447 C  CG1   . VAL A 1 4642 ? 130.928 170.276 129.757 1.00 43.59  ? 4642 VAL A CG1   1 
ATOM   24448 C  CG2   . VAL A 1 4642 ? 131.562 171.533 127.699 1.00 33.67  ? 4642 VAL A CG2   1 
ATOM   24449 N  N     . LEU A 1 4643 ? 132.407 171.728 132.276 1.00 42.76  ? 4643 LEU A N     1 
ATOM   24450 C  CA    . LEU A 1 4643 ? 132.811 171.282 133.600 1.00 46.03  ? 4643 LEU A CA    1 
ATOM   24451 C  C     . LEU A 1 4643 ? 131.871 170.180 134.064 1.00 54.08  ? 4643 LEU A C     1 
ATOM   24452 O  O     . LEU A 1 4643 ? 130.648 170.333 133.994 1.00 59.99  ? 4643 LEU A O     1 
ATOM   24453 C  CB    . LEU A 1 4643 ? 132.789 172.443 134.595 1.00 49.19  ? 4643 LEU A CB    1 
ATOM   24454 C  CG    . LEU A 1 4643 ? 133.650 173.660 134.261 1.00 44.12  ? 4643 LEU A CG    1 
ATOM   24455 C  CD1   . LEU A 1 4643 ? 133.674 174.618 135.434 1.00 52.71  ? 4643 LEU A CD1   1 
ATOM   24456 C  CD2   . LEU A 1 4643 ? 135.057 173.245 133.883 1.00 45.63  ? 4643 LEU A CD2   1 
ATOM   24457 N  N     . CYS A 1 4644 ? 132.445 169.067 134.527 1.00 55.82  ? 4644 CYS A N     1 
ATOM   24458 C  CA    . CYS A 1 4644 ? 131.623 168.003 135.094 1.00 59.56  ? 4644 CYS A CA    1 
ATOM   24459 C  C     . CYS A 1 4644 ? 130.906 168.479 136.350 1.00 62.63  ? 4644 CYS A C     1 
ATOM   24460 O  O     . CYS A 1 4644 ? 129.728 168.169 136.557 1.00 69.25  ? 4644 CYS A O     1 
ATOM   24461 C  CB    . CYS A 1 4644 ? 132.484 166.777 135.394 1.00 63.13  ? 4644 CYS A CB    1 
ATOM   24462 S  SG    . CYS A 1 4644 ? 133.059 165.896 133.925 1.00 73.87  ? 4644 CYS A SG    1 
ATOM   24463 N  N     . THR A 1 4645 ? 131.601 169.233 137.198 1.00 61.52  ? 4645 THR A N     1 
ATOM   24464 C  CA    . THR A 1 4645 ? 131.004 169.835 138.379 1.00 68.66  ? 4645 THR A CA    1 
ATOM   24465 C  C     . THR A 1 4645 ? 131.461 171.282 138.481 1.00 71.87  ? 4645 THR A C     1 
ATOM   24466 O  O     . THR A 1 4645 ? 132.561 171.635 138.048 1.00 72.02  ? 4645 THR A O     1 
ATOM   24467 C  CB    . THR A 1 4645 ? 131.371 169.070 139.661 1.00 74.44  ? 4645 THR A CB    1 
ATOM   24468 O  OG1   . THR A 1 4645 ? 130.728 169.680 140.787 1.00 71.51  ? 4645 THR A OG1   1 
ATOM   24469 C  CG2   . THR A 1 4645 ? 132.874 169.069 139.881 1.00 67.14  ? 4645 THR A CG2   1 
ATOM   24470 N  N     . GLU A 1 4646 ? 130.600 172.120 139.047 1.00 74.47  ? 4646 GLU A N     1 
ATOM   24471 C  CA    . GLU A 1 4646 ? 130.906 173.538 139.192 1.00 81.78  ? 4646 GLU A CA    1 
ATOM   24472 C  C     . GLU A 1 4646 ? 131.299 173.869 140.627 1.00 89.94  ? 4646 GLU A C     1 
ATOM   24473 O  O     . GLU A 1 4646 ? 131.111 173.063 141.538 1.00 88.24  ? 4646 GLU A O     1 
ATOM   24474 C  CB    . GLU A 1 4646 ? 129.711 174.390 138.761 1.00 85.78  ? 4646 GLU A CB    1 
ATOM   24475 C  CG    . GLU A 1 4646 ? 130.085 175.776 138.263 1.00 89.44  ? 4646 GLU A CG    1 
ATOM   24476 C  CD    . GLU A 1 4646 ? 128.905 176.727 138.241 1.00 95.28  ? 4646 GLU A CD    1 
ATOM   24477 O  OE1   . GLU A 1 4646 ? 127.799 176.316 138.651 1.00 92.78  ? 4646 GLU A OE1   1 
ATOM   24478 O  OE2   . GLU A 1 4646 ? 129.083 177.887 137.813 1.00 101.71 ? 4646 GLU A OE2   1 
ATOM   24479 O  OXT   . GLU A 1 4646 ? 131.815 174.950 140.911 1.00 95.08  ? 4646 GLU A OXT   1 
HETATM 24480 P  PB    . ADP B 2 .    ? 161.443 158.408 130.053 1.00 41.16  ? 4701 ADP A PB    1 
HETATM 24481 O  O1B   . ADP B 2 .    ? 160.415 158.488 128.956 1.00 39.31  ? 4701 ADP A O1B   1 
HETATM 24482 O  O2B   . ADP B 2 .    ? 162.620 159.329 129.872 1.00 43.61  ? 4701 ADP A O2B   1 
HETATM 24483 O  O3B   . ADP B 2 .    ? 160.869 158.409 131.446 1.00 47.27  ? 4701 ADP A O3B   1 
HETATM 24484 P  PA    . ADP B 2 .    ? 162.696 156.452 128.493 1.00 51.21  ? 4701 ADP A PA    1 
HETATM 24485 O  O1A   . ADP B 2 .    ? 164.022 155.793 128.780 1.00 52.99  ? 4701 ADP A O1A   1 
HETATM 24486 O  O2A   . ADP B 2 .    ? 162.652 157.604 127.528 1.00 31.24  ? 4701 ADP A O2A   1 
HETATM 24487 O  O3A   . ADP B 2 .    ? 162.076 156.938 129.895 1.00 49.86  ? 4701 ADP A O3A   1 
HETATM 24488 O  "O5'" . ADP B 2 .    ? 161.701 155.300 127.975 1.00 49.84  ? 4701 ADP A "O5'" 1 
HETATM 24489 C  "C5'" . ADP B 2 .    ? 160.499 155.601 127.275 1.00 41.05  ? 4701 ADP A "C5'" 1 
HETATM 24490 C  "C4'" . ADP B 2 .    ? 160.191 154.434 126.348 1.00 35.35  ? 4701 ADP A "C4'" 1 
HETATM 24491 O  "O4'" . ADP B 2 .    ? 159.361 154.877 125.275 1.00 34.87  ? 4701 ADP A "O4'" 1 
HETATM 24492 C  "C3'" . ADP B 2 .    ? 161.469 153.896 125.733 1.00 38.45  ? 4701 ADP A "C3'" 1 
HETATM 24493 O  "O3'" . ADP B 2 .    ? 161.591 152.504 126.020 1.00 46.32  ? 4701 ADP A "O3'" 1 
HETATM 24494 C  "C2'" . ADP B 2 .    ? 161.332 154.078 124.241 1.00 37.73  ? 4701 ADP A "C2'" 1 
HETATM 24495 O  "O2'" . ADP B 2 .    ? 161.648 152.852 123.580 1.00 43.92  ? 4701 ADP A "O2'" 1 
HETATM 24496 C  "C1'" . ADP B 2 .    ? 159.877 154.442 124.017 1.00 33.89  ? 4701 ADP A "C1'" 1 
HETATM 24497 N  N9    . ADP B 2 .    ? 159.769 155.543 123.031 1.00 30.28  ? 4701 ADP A N9    1 
HETATM 24498 C  C8    . ADP B 2 .    ? 159.558 156.836 123.325 1.00 31.38  ? 4701 ADP A C8    1 
HETATM 24499 N  N7    . ADP B 2 .    ? 159.504 157.590 122.200 1.00 33.21  ? 4701 ADP A N7    1 
HETATM 24500 C  C5    . ADP B 2 .    ? 159.680 156.765 121.155 1.00 28.85  ? 4701 ADP A C5    1 
HETATM 24501 C  C6    . ADP B 2 .    ? 159.735 156.906 119.684 1.00 31.47  ? 4701 ADP A C6    1 
HETATM 24502 N  N6    . ADP B 2 .    ? 159.586 158.113 119.091 1.00 31.68  ? 4701 ADP A N6    1 
HETATM 24503 N  N1    . ADP B 2 .    ? 159.939 155.790 118.954 1.00 35.27  ? 4701 ADP A N1    1 
HETATM 24504 C  C2    . ADP B 2 .    ? 160.087 154.585 119.530 1.00 34.13  ? 4701 ADP A C2    1 
HETATM 24505 N  N3    . ADP B 2 .    ? 160.050 154.386 120.857 1.00 32.81  ? 4701 ADP A N3    1 
HETATM 24506 C  C4    . ADP B 2 .    ? 159.853 155.417 121.708 1.00 30.03  ? 4701 ADP A C4    1 
HETATM 24507 P  PG    . ATP C 3 .    ? 154.699 126.994 148.673 1.00 48.38  ? 4702 ATP A PG    1 
HETATM 24508 O  O1G   . ATP C 3 .    ? 154.175 126.543 149.991 1.00 47.55  ? 4702 ATP A O1G   1 
HETATM 24509 O  O2G   . ATP C 3 .    ? 156.125 126.528 148.388 1.00 54.98  ? 4702 ATP A O2G   1 
HETATM 24510 O  O3G   . ATP C 3 .    ? 154.623 128.504 148.464 1.00 40.62  ? 4702 ATP A O3G   1 
HETATM 24511 P  PB    . ATP C 3 .    ? 154.030 125.813 146.024 1.00 36.16  ? 4702 ATP A PB    1 
HETATM 24512 O  O1B   . ATP C 3 .    ? 155.456 125.600 145.725 1.00 45.38  ? 4702 ATP A O1B   1 
HETATM 24513 O  O2B   . ATP C 3 .    ? 153.269 126.733 145.078 1.00 37.50  ? 4702 ATP A O2B   1 
HETATM 24514 O  O3B   . ATP C 3 .    ? 153.835 126.381 147.484 1.00 34.69  ? 4702 ATP A O3B   1 
HETATM 24515 P  PA    . ATP C 3 .    ? 153.451 122.955 145.579 1.00 38.48  ? 4702 ATP A PA    1 
HETATM 24516 O  O1A   . ATP C 3 .    ? 153.922 122.921 144.181 1.00 42.48  ? 4702 ATP A O1A   1 
HETATM 24517 O  O2A   . ATP C 3 .    ? 154.363 122.263 146.586 1.00 42.82  ? 4702 ATP A O2A   1 
HETATM 24518 O  O3A   . ATP C 3 .    ? 153.232 124.438 146.087 1.00 27.27  ? 4702 ATP A O3A   1 
HETATM 24519 O  "O5'" . ATP C 3 .    ? 152.010 122.323 145.691 1.00 35.54  ? 4702 ATP A "O5'" 1 
HETATM 24520 C  "C5'" . ATP C 3 .    ? 151.316 122.266 146.954 1.00 32.62  ? 4702 ATP A "C5'" 1 
HETATM 24521 C  "C4'" . ATP C 3 .    ? 150.725 120.891 147.119 1.00 28.87  ? 4702 ATP A "C4'" 1 
HETATM 24522 O  "O4'" . ATP C 3 .    ? 149.579 120.753 146.253 1.00 29.22  ? 4702 ATP A "O4'" 1 
HETATM 24523 C  "C3'" . ATP C 3 .    ? 151.647 119.741 146.738 1.00 32.03  ? 4702 ATP A "C3'" 1 
HETATM 24524 O  "O3'" . ATP C 3 .    ? 152.478 119.365 147.830 1.00 38.44  ? 4702 ATP A "O3'" 1 
HETATM 24525 C  "C2'" . ATP C 3 .    ? 150.652 118.637 146.379 1.00 31.67  ? 4702 ATP A "C2'" 1 
HETATM 24526 O  "O2'" . ATP C 3 .    ? 150.175 117.961 147.535 1.00 43.17  ? 4702 ATP A "O2'" 1 
HETATM 24527 C  "C1'" . ATP C 3 .    ? 149.518 119.437 145.729 1.00 28.33  ? 4702 ATP A "C1'" 1 
HETATM 24528 N  N9    . ATP C 3 .    ? 149.599 119.514 144.275 1.00 30.62  ? 4702 ATP A N9    1 
HETATM 24529 C  C8    . ATP C 3 .    ? 150.392 120.348 143.530 1.00 34.20  ? 4702 ATP A C8    1 
HETATM 24530 N  N7    . ATP C 3 .    ? 150.258 120.199 142.235 1.00 31.02  ? 4702 ATP A N7    1 
HETATM 24531 C  C5    . ATP C 3 .    ? 149.309 119.195 142.118 1.00 27.21  ? 4702 ATP A C5    1 
HETATM 24532 C  C6    . ATP C 3 .    ? 148.722 118.567 141.004 1.00 31.10  ? 4702 ATP A C6    1 
HETATM 24533 N  N6    . ATP C 3 .    ? 149.017 118.873 139.736 1.00 32.35  ? 4702 ATP A N6    1 
HETATM 24534 N  N1    . ATP C 3 .    ? 147.806 117.603 141.236 1.00 36.60  ? 4702 ATP A N1    1 
HETATM 24535 C  C2    . ATP C 3 .    ? 147.506 117.292 142.498 1.00 34.28  ? 4702 ATP A C2    1 
HETATM 24536 N  N3    . ATP C 3 .    ? 147.993 117.813 143.626 1.00 30.97  ? 4702 ATP A N3    1 
HETATM 24537 C  C4    . ATP C 3 .    ? 148.894 118.764 143.367 1.00 28.34  ? 4702 ATP A C4    1 
HETATM 24538 P  PG    . ANP D 4 .    ? 153.361 131.360 177.899 1.00 44.72  ? 4703 ANP A PG    1 
HETATM 24539 O  O1G   . ANP D 4 .    ? 153.542 132.425 178.979 1.00 44.32  ? 4703 ANP A O1G   1 
HETATM 24540 O  O2G   . ANP D 4 .    ? 152.623 131.850 176.655 1.00 47.76  ? 4703 ANP A O2G   1 
HETATM 24541 O  O3G   . ANP D 4 .    ? 154.620 130.551 177.602 1.00 51.28  ? 4703 ANP A O3G   1 
HETATM 24542 P  PB    . ANP D 4 .    ? 152.223 128.525 178.426 1.00 32.22  ? 4703 ANP A PB    1 
HETATM 24543 O  O1B   . ANP D 4 .    ? 153.596 128.048 178.068 1.00 34.26  ? 4703 ANP A O1B   1 
HETATM 24544 O  O2B   . ANP D 4 .    ? 151.018 127.980 177.709 1.00 42.18  ? 4703 ANP A O2B   1 
HETATM 24545 N  N3B   . ANP D 4 .    ? 152.178 130.184 178.555 1.00 34.00  ? 4703 ANP A N3B   1 
HETATM 24546 P  PA    . ANP D 4 .    ? 153.074 127.105 180.857 1.00 40.57  ? 4703 ANP A PA    1 
HETATM 24547 O  O1A   . ANP D 4 .    ? 154.426 127.722 180.975 1.00 45.76  ? 4703 ANP A O1A   1 
HETATM 24548 O  O2A   . ANP D 4 .    ? 152.927 125.659 180.434 1.00 37.74  ? 4703 ANP A O2A   1 
HETATM 24549 O  O3A   . ANP D 4 .    ? 152.036 128.018 180.033 1.00 27.57  ? 4703 ANP A O3A   1 
HETATM 24550 O  "O5'" . ANP D 4 .    ? 152.376 127.278 182.342 1.00 38.46  ? 4703 ANP A "O5'" 1 
HETATM 24551 C  "C5'" . ANP D 4 .    ? 150.998 127.044 182.505 1.00 35.62  ? 4703 ANP A "C5'" 1 
HETATM 24552 C  "C4'" . ANP D 4 .    ? 150.537 127.307 183.921 1.00 31.17  ? 4703 ANP A "C4'" 1 
HETATM 24553 O  "O4'" . ANP D 4 .    ? 149.256 126.725 184.165 1.00 31.32  ? 4703 ANP A "O4'" 1 
HETATM 24554 C  "C3'" . ANP D 4 .    ? 151.437 126.740 185.019 1.00 32.40  ? 4703 ANP A "C3'" 1 
HETATM 24555 O  "O3'" . ANP D 4 .    ? 151.508 127.506 186.170 1.00 39.94  ? 4703 ANP A "O3'" 1 
HETATM 24556 C  "C2'" . ANP D 4 .    ? 150.869 125.343 185.193 1.00 38.63  ? 4703 ANP A "C2'" 1 
HETATM 24557 O  "O2'" . ANP D 4 .    ? 151.121 124.897 186.495 1.00 43.30  ? 4703 ANP A "O2'" 1 
HETATM 24558 C  "C1'" . ANP D 4 .    ? 149.367 125.587 184.959 1.00 35.79  ? 4703 ANP A "C1'" 1 
HETATM 24559 N  N9    . ANP D 4 .    ? 148.729 124.484 184.247 1.00 37.63  ? 4703 ANP A N9    1 
HETATM 24560 C  C8    . ANP D 4 .    ? 147.995 124.555 183.096 1.00 36.36  ? 4703 ANP A C8    1 
HETATM 24561 N  N7    . ANP D 4 .    ? 147.550 123.402 182.695 1.00 41.12  ? 4703 ANP A N7    1 
HETATM 24562 C  C5    . ANP D 4 .    ? 148.013 122.516 183.629 1.00 42.34  ? 4703 ANP A C5    1 
HETATM 24563 C  C6    . ANP D 4 .    ? 147.883 121.126 183.773 1.00 45.65  ? 4703 ANP A C6    1 
HETATM 24564 N  N6    . ANP D 4 .    ? 147.198 120.371 182.904 1.00 47.04  ? 4703 ANP A N6    1 
HETATM 24565 N  N1    . ANP D 4 .    ? 148.467 120.542 184.820 1.00 44.94  ? 4703 ANP A N1    1 
HETATM 24566 C  C2    . ANP D 4 .    ? 149.145 121.291 185.682 1.00 42.65  ? 4703 ANP A C2    1 
HETATM 24567 N  N3    . ANP D 4 .    ? 149.335 122.596 185.656 1.00 39.41  ? 4703 ANP A N3    1 
HETATM 24568 C  C4    . ANP D 4 .    ? 148.749 123.167 184.605 1.00 39.21  ? 4703 ANP A C4    1 
HETATM 24569 P  PG    . ANP E 4 .    ? 159.260 156.664 188.367 1.00 53.12  ? 4704 ANP A PG    1 
HETATM 24570 O  O1G   . ANP E 4 .    ? 160.508 155.783 188.318 1.00 51.11  ? 4704 ANP A O1G   1 
HETATM 24571 O  O2G   . ANP E 4 .    ? 157.972 155.945 187.972 1.00 47.15  ? 4704 ANP A O2G   1 
HETATM 24572 O  O3G   . ANP E 4 .    ? 159.437 158.039 187.730 1.00 52.20  ? 4704 ANP A O3G   1 
HETATM 24573 P  PB    . ANP E 4 .    ? 158.914 155.839 191.302 1.00 34.74  ? 4704 ANP A PB    1 
HETATM 24574 O  O1B   . ANP E 4 .    ? 157.551 155.226 191.396 1.00 42.13  ? 4704 ANP A O1B   1 
HETATM 24575 O  O2B   . ANP E 4 .    ? 160.137 154.963 191.275 1.00 49.68  ? 4704 ANP A O2B   1 
HETATM 24576 N  N3B   . ANP E 4 .    ? 158.963 156.989 190.103 1.00 34.67  ? 4704 ANP A N3B   1 
HETATM 24577 P  PA    . ANP E 4 .    ? 160.393 157.138 193.492 1.00 39.35  ? 4704 ANP A PA    1 
HETATM 24578 O  O1A   . ANP E 4 .    ? 161.573 157.181 192.582 1.00 42.86  ? 4704 ANP A O1A   1 
HETATM 24579 O  O2A   . ANP E 4 .    ? 160.472 156.367 194.791 1.00 36.00  ? 4704 ANP A O2A   1 
HETATM 24580 O  O3A   . ANP E 4 .    ? 159.031 156.752 192.727 1.00 34.77  ? 4704 ANP A O3A   1 
HETATM 24581 O  "O5'" . ANP E 4 .    ? 160.032 158.713 193.838 1.00 54.18  ? 4704 ANP A "O5'" 1 
HETATM 24582 C  "C5'" . ANP E 4 .    ? 161.046 159.639 194.146 1.00 46.64  ? 4704 ANP A "C5'" 1 
HETATM 24583 C  "C4'" . ANP E 4 .    ? 160.860 160.307 195.494 1.00 42.40  ? 4704 ANP A "C4'" 1 
HETATM 24584 O  "O4'" . ANP E 4 .    ? 159.710 159.806 196.179 1.00 39.48  ? 4704 ANP A "O4'" 1 
HETATM 24585 C  "C3'" . ANP E 4 .    ? 162.028 160.148 196.481 1.00 50.02  ? 4704 ANP A "C3'" 1 
HETATM 24586 O  "O3'" . ANP E 4 .    ? 162.711 161.325 196.739 1.00 64.46  ? 4704 ANP A "O3'" 1 
HETATM 24587 C  "C2'" . ANP E 4 .    ? 161.414 159.481 197.705 1.00 45.76  ? 4704 ANP A "C2'" 1 
HETATM 24588 O  "O2'" . ANP E 4 .    ? 161.970 160.040 198.859 1.00 55.10  ? 4704 ANP A "O2'" 1 
HETATM 24589 C  "C1'" . ANP E 4 .    ? 159.946 159.902 197.541 1.00 39.47  ? 4704 ANP A "C1'" 1 
HETATM 24590 N  N9    . ANP E 4 .    ? 159.033 159.024 198.260 1.00 37.02  ? 4704 ANP A N9    1 
HETATM 24591 C  C8    . ANP E 4 .    ? 158.472 157.852 197.838 1.00 42.64  ? 4704 ANP A C8    1 
HETATM 24592 N  N7    . ANP E 4 .    ? 157.694 157.304 198.724 1.00 43.41  ? 4704 ANP A N7    1 
HETATM 24593 C  C5    . ANP E 4 .    ? 157.740 158.158 199.790 1.00 36.85  ? 4704 ANP A C5    1 
HETATM 24594 C  C6    . ANP E 4 .    ? 157.131 158.147 201.052 1.00 36.11  ? 4704 ANP A C6    1 
HETATM 24595 N  N6    . ANP E 4 .    ? 156.307 157.170 201.448 1.00 33.92  ? 4704 ANP A N6    1 
HETATM 24596 N  N1    . ANP E 4 .    ? 157.389 159.157 201.884 1.00 39.50  ? 4704 ANP A N1    1 
HETATM 24597 C  C2    . ANP E 4 .    ? 158.208 160.127 201.490 1.00 40.05  ? 4704 ANP A C2    1 
HETATM 24598 N  N3    . ANP E 4 .    ? 158.838 160.248 200.337 1.00 36.58  ? 4704 ANP A N3    1 
HETATM 24599 C  C4    . ANP E 4 .    ? 158.568 159.234 199.521 1.00 34.55  ? 4704 ANP A C4    1 
HETATM 24600 MG MG    . MG  F 5 .    ? 162.525 155.925 132.739 1.00 41.42  ? 4705 MG  A MG    1 
HETATM 24601 MG MG    . MG  G 5 .    ? 157.219 125.538 146.828 1.00 41.56  ? 4706 MG  A MG    1 
HETATM 24602 MG MG    . MG  H 5 .    ? 155.494 128.797 177.109 1.00 43.75  ? 4707 MG  A MG    1 
HETATM 24603 MG MG    . MG  I 5 .    ? 161.666 154.391 189.585 1.00 40.16  ? 4708 MG  A MG    1 
# 
