data_8YQZ
# 
_entry.id   8YQZ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8YQZ         pdb_00008yqz 10.2210/pdb8yqz/pdb 
WWPDB D_1300046210 ?            ?                   
EMDB  EMD-39511    ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YQZ 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-20 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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        'African swine fever virus RNA Polymerase--DNA complex' 
_pdbx_database_related.db_id          EMD-39511 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              1406630682@qq.com 
_pdbx_contact_author.name_first         xiaoying 
_pdbx_contact_author.name_last          Feng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0009-0004-4689-8853 
# 
_audit_author.name               'Feng, X.Y.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0009-0004-4689-8853 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Regulation of early transcription and late transcript processing enzymes packaging for African swine fever virus from endogenous vRNAP-M1249L supercomplex structures
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Feng, X.Y.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   0009-0004-4689-8853 
# 
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     nat 'DNA-directed RNA polymerase subunit'         163933.938 1 2.7.7.6 ? ? ? 
2  polymer     nat 'DNA-directed RNA polymerase subunit beta'    140056.453 1 2.7.7.6 ? ? ? 
3  polymer     nat 'DNA-directed RNA polymerase RPB3-11 homolog' 41418.137  1 ?       ? ? ? 
4  polymer     nat 'DNA-directed RNA polymerase RPB5 homolog'    23693.711  1 ?       ? ? ? 
5  polymer     nat C147L                                         16670.795  1 ?       ? ? ? 
6  polymer     nat D339L                                         38798.594  1 ?       ? ? ? 
7  polymer     nat C122R                                         11831.861  1 ?       ? ? ? 
8  polymer     nat 'DNA-directed RNA polymerase RPB10 homolog'   9040.790   1 ?       ? ? ? 
9  polymer     nat 
;DNA (5'-D(P*GP*CP*CP*GP*AP*GP*CP*A)-3')
;
2436.619   1 ?       ? ? ? 
10 polymer     nat 
;DNA (5'-D(P*TP*CP*GP*GP*CP*TP*C)-3')
;
2089.385   1 ?       ? ? ? 
11 non-polymer syn 'MAGNESIUM ION'                               24.305     1 ?       ? ? ? 
12 non-polymer syn 'ZINC ION'                                    65.409     4 ?       ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 vRPB1                               
2 vRPB2                               
3 vRPB3-11                            
4 vRPB5                               
5 'C147L protein,Protein C147L'       
6 'vRPB7,D339L protein,Protein D339L' 
7 'vRPB9,C122R protein,PC105R,PC122R' 
8 vRPB10                              
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1  'polypeptide(L)'        no no 
;MEAGYAEIAAVQFNIAGDNDHKRQGVMEVTISNLFEGTLPAEGGIYDARMGTTDHHYKCITCSHQRKQCMGHPGILQMHA
PVLQPLFIAEIRRWLRVICLNCGAPIVDLKRYEHLIRPKRLIEAASSQTEGKQCYVCKAVHPKIVKDSEDYFTFWADQQG
KIDKLYPQIIREIFSRVTYDTVVKLGRSKNSHPEKLVLKAIQIPPISIRPGIRLGIGSGPQSFHDINNVIQYLVRKNLLI
PKDLQIVRGQKIPLNIDRNLQTIQQLYYNFLLDSVSTTATQGGTGKRGIVMGARPAPSIMRRLPRKEGRIRKSLLGSQVW
SISRSTICGNSDLHLDEVGYPISFARTLQVAETVQHYNINRLMPYFLNGKRQYPGCSRVYKQITQSVHDIEGLKQDFRLE
VGDILYRDVVTGDVAFFNRQPSLERSSIGVHRIVVLENPKISTFQMNVSACAWYNADFDGDQMNLWVPWSVMSRVEAELL
CSVRNWFISTKSSGPVNGQVQDSTVGSFLLTRTNTPMGKNVMNKLHAMGLFQTTQTDPPCFANYSPTDLLDGKSVVSMLL
RQTPINYQRAPTWYSEVYAPYMHYNKQDISTQIRNGELIEGVLDKKAVGAGSSGGIYHLISRRYGPQQALKMIFATQQLA
LNYVRNAGFTVSTADMLLTPEAHQEVQEIINELLLESEEINNRLLHGDIMPPIGLTTHDFYEKLQLNALKFPDRILKPIM
NSINPETNGLFQMVATGAKGSNPNMIHIMAGIGQIEINTQRIQPQFSFGRTLVYYPRFALEAQAYGFICNSYIAGLTSPE
FIFGEMNGRFDLINKALSTSSTGYANRKAIFGLQSCIVDYYRRVSIDTRLVQQLYGEDGLDARQLETVRFETIMLSDQEL
EDKFKYTGIQSPLFEEEFSRLKKDRDKYRQIFLNVENFNFSQLLTDVRQVPVNVASIVKNILLSSTSGVLPFDEKSILQK
YAMVKTFCKNLPYVFINNIQERLQTPIPVYLKRAASLMRMLIRIELATVKTLNITCEQMSAILDLIRLQYTQSLINYGEA
VGILAAQSVSEPLTQYMLDSHHRSVAGGTNKSGIVRPQEIFSAKPVEAEQSSEMLLRLKNPEVETNKTYAQEIANSIELI
TFERLILQWHLLYETYSSTKKNVMYPDFASDVEWMTDFLENHPLLQPPEDIANWCIRLELNKTTMILKSISLESIINSLR
AKHPNTYIMHSVENTASGIPIIIRIYLRESAFRRSTNTRMATDEKIAVNVVDKLLNSTIRGIPGIKNANVVKLMRHRVDA
QGKLVRLDNIYAIKTNGTNIFGAMLDDNIDPYTIVSSSIGDTMELYGIEAARQKIISEIRTVMGDKGPNHRHLLMYADLM
TRTGQVTSLEKAGLNAREPSNVLLRMALSSPVQVLTDAAVDSAVNPIYGIAAPTLMGSVPRIGTMYSDIIMDEKYITENY
KSVDSLIDML
;
;MEAGYAEIAAVQFNIAGDNDHKRQGVMEVTISNLFEGTLPAEGGIYDARMGTTDHHYKCITCSHQRKQCMGHPGILQMHA
PVLQPLFIAEIRRWLRVICLNCGAPIVDLKRYEHLIRPKRLIEAASSQTEGKQCYVCKAVHPKIVKDSEDYFTFWADQQG
KIDKLYPQIIREIFSRVTYDTVVKLGRSKNSHPEKLVLKAIQIPPISIRPGIRLGIGSGPQSFHDINNVIQYLVRKNLLI
PKDLQIVRGQKIPLNIDRNLQTIQQLYYNFLLDSVSTTATQGGTGKRGIVMGARPAPSIMRRLPRKEGRIRKSLLGSQVW
SISRSTICGNSDLHLDEVGYPISFARTLQVAETVQHYNINRLMPYFLNGKRQYPGCSRVYKQITQSVHDIEGLKQDFRLE
VGDILYRDVVTGDVAFFNRQPSLERSSIGVHRIVVLENPKISTFQMNVSACAWYNADFDGDQMNLWVPWSVMSRVEAELL
CSVRNWFISTKSSGPVNGQVQDSTVGSFLLTRTNTPMGKNVMNKLHAMGLFQTTQTDPPCFANYSPTDLLDGKSVVSMLL
RQTPINYQRAPTWYSEVYAPYMHYNKQDISTQIRNGELIEGVLDKKAVGAGSSGGIYHLISRRYGPQQALKMIFATQQLA
LNYVRNAGFTVSTADMLLTPEAHQEVQEIINELLLESEEINNRLLHGDIMPPIGLTTHDFYEKLQLNALKFPDRILKPIM
NSINPETNGLFQMVATGAKGSNPNMIHIMAGIGQIEINTQRIQPQFSFGRTLVYYPRFALEAQAYGFICNSYIAGLTSPE
FIFGEMNGRFDLINKALSTSSTGYANRKAIFGLQSCIVDYYRRVSIDTRLVQQLYGEDGLDARQLETVRFETIMLSDQEL
EDKFKYTGIQSPLFEEEFSRLKKDRDKYRQIFLNVENFNFSQLLTDVRQVPVNVASIVKNILLSSTSGVLPFDEKSILQK
YAMVKTFCKNLPYVFINNIQERLQTPIPVYLKRAASLMRMLIRIELATVKTLNITCEQMSAILDLIRLQYTQSLINYGEA
VGILAAQSVSEPLTQYMLDSHHRSVAGGTNKSGIVRPQEIFSAKPVEAEQSSEMLLRLKNPEVETNKTYAQEIANSIELI
TFERLILQWHLLYETYSSTKKNVMYPDFASDVEWMTDFLENHPLLQPPEDIANWCIRLELNKTTMILKSISLESIINSLR
AKHPNTYIMHSVENTASGIPIIIRIYLRESAFRRSTNTRMATDEKIAVNVVDKLLNSTIRGIPGIKNANVVKLMRHRVDA
QGKLVRLDNIYAIKTNGTNIFGAMLDDNIDPYTIVSSSIGDTMELYGIEAARQKIISEIRTVMGDKGPNHRHLLMYADLM
TRTGQVTSLEKAGLNAREPSNVLLRMALSSPVQVLTDAAVDSAVNPIYGIAAPTLMGSVPRIGTMYSDIIMDEKYITENY
KSVDSLIDML
;
A ? 
2  'polypeptide(L)'        no no 
;MEPLRPQITYGPIETVDNEELTEADMLSFISAAVNSTGLIGYNIKSFDDLMDNGIPQIVKQMFNVDITYKDQRDHTEIDK
LRESVQIQFNFTDVNIERPQHRNYSQGNKINLLPNKARLCGLSYSGPVNLAAEVILTAHYSNGRQEVKRASIPPFQVSTF
PIMRGSNRCHTHHLSKTAKKEIGEDPNEPGGYFIARGGEWVVDLLENIRFNTLHIHYHTMQQGNNEIIRGEFISQPGGAF
ENSSQIIIRYMTTGAITIEINSTKFSKLRIPWYLIFRMFGMTGDDSIIEQVVFDLESNSLVNTFMIEILEKSIHVLDPIF
QPVQHELNREKIIQFLSEKVSKFVSNPSAYKSDENAVQYLNERQLTILDKILLPHMGQTADTRVRKLRFLGLLIHKILLV
IMNVFPPTDRDSYRTKRVHGSGVSLAKAFKAIFNTSVIAPIINGFKELLKQTAFEELTQRNIIEAFSAALSKNTASDLNR
SMEQSIISGNKTIMVRQRPIVNRVSTQSLERKNLLNTISALRTVNTHNTTNASKQTERADMMRRVHASYPGYICVAQSAD
TGEKVGMSKQLAITANVCTAGEVLSLKQRLLSDPAIQQLADVSNKDIVRKGLARVFINGEWIGCCTNAFELAQRYRMLRR
EGKVVHPHTTIYWDSMVDEVEFWLDVGRLTRPLLIVDNNIEKYNQACYKAAEARKKGDKDWEKHKIPFIQNTRFTPQMAK
DILAGTLTLEDLVAQGICEFITPEEAENCLVAFSIIELRKHKHDVTRRFTHVDVPQAILGLAALVSPYANCTQPARVTYE
TNQGRQTGGWYCFSWPYRVDMNRFFQFYNEMPLVKTIAHNYVIPNGLNTIVAYMIYGGYNQEDSVIVSQSFIDRGGFAGT
FYREEKVELESDIESFGKPDPLITKNLKPGANYEKLVDGFVPVGTVVKKGDIIIGKVAKIRGEKDELNKYIDRSVMYGFD
EPAVVDAVMRPHGPNDEIFGLMRLRYERNLNIGDKMSSRSGNKGIAALALPTSDMPFTEDGLQPDLIVNPHSHPSRMTNG
QMIETTVGLANALQGVVTDGTAFLPINVQLLSERLAQEGLRFNGCQKMFNGQTGEYFDAAIFIGPTYHQRLQKFVLDDRY
AVASYGPTDALTGQPLDGKRSHGGLRLGEMEHWVLTAQGAMQTIIEKSHDDSDGCISYICRNCGEPAIYNASHPIYKCMN
CDVQADIGMVDSRRSSIVFQHEMRAANVNITSVLSPRVFQPA
;
;MEPLRPQITYGPIETVDNEELTEADMLSFISAAVNSTGLIGYNIKSFDDLMDNGIPQIVKQMFNVDITYKDQRDHTEIDK
LRESVQIQFNFTDVNIERPQHRNYSQGNKINLLPNKARLCGLSYSGPVNLAAEVILTAHYSNGRQEVKRASIPPFQVSTF
PIMRGSNRCHTHHLSKTAKKEIGEDPNEPGGYFIARGGEWVVDLLENIRFNTLHIHYHTMQQGNNEIIRGEFISQPGGAF
ENSSQIIIRYMTTGAITIEINSTKFSKLRIPWYLIFRMFGMTGDDSIIEQVVFDLESNSLVNTFMIEILEKSIHVLDPIF
QPVQHELNREKIIQFLSEKVSKFVSNPSAYKSDENAVQYLNERQLTILDKILLPHMGQTADTRVRKLRFLGLLIHKILLV
IMNVFPPTDRDSYRTKRVHGSGVSLAKAFKAIFNTSVIAPIINGFKELLKQTAFEELTQRNIIEAFSAALSKNTASDLNR
SMEQSIISGNKTIMVRQRPIVNRVSTQSLERKNLLNTISALRTVNTHNTTNASKQTERADMMRRVHASYPGYICVAQSAD
TGEKVGMSKQLAITANVCTAGEVLSLKQRLLSDPAIQQLADVSNKDIVRKGLARVFINGEWIGCCTNAFELAQRYRMLRR
EGKVVHPHTTIYWDSMVDEVEFWLDVGRLTRPLLIVDNNIEKYNQACYKAAEARKKGDKDWEKHKIPFIQNTRFTPQMAK
DILAGTLTLEDLVAQGICEFITPEEAENCLVAFSIIELRKHKHDVTRRFTHVDVPQAILGLAALVSPYANCTQPARVTYE
TNQGRQTGGWYCFSWPYRVDMNRFFQFYNEMPLVKTIAHNYVIPNGLNTIVAYMIYGGYNQEDSVIVSQSFIDRGGFAGT
FYREEKVELESDIESFGKPDPLITKNLKPGANYEKLVDGFVPVGTVVKKGDIIIGKVAKIRGEKDELNKYIDRSVMYGFD
EPAVVDAVMRPHGPNDEIFGLMRLRYERNLNIGDKMSSRSGNKGIAALALPTSDMPFTEDGLQPDLIVNPHSHPSRMTNG
QMIETTVGLANALQGVVTDGTAFLPINVQLLSERLAQEGLRFNGCQKMFNGQTGEYFDAAIFIGPTYHQRLQKFVLDDRY
AVASYGPTDALTGQPLDGKRSHGGLRLGEMEHWVLTAQGAMQTIIEKSHDDSDGCISYICRNCGEPAIYNASHPIYKCMN
CDVQADIGMVDSRRSSIVFQHEMRAANVNITSVLSPRVFQPA
;
B ? 
3  'polypeptide(L)'        no no 
;MEKIFQNVEIKPFLIDFSNLFIKNAAKKLFQLEEQLPLVPVNVVMDFKGISRAAVHGLSRVLQDEIPNYMLDIKPGGYKI
EDSTDLFMTEQFIRNRINFIPIYAKNETLVFALRSLNNSCEVKTIYSRDLIQVAGPKLKYPIFNPTFEIGFLQPGKSLII
EDIYIKKGIGRKHAAFNLAVKTHFSHLDIEQYPTDKKEYMALSGYKQSSMTSDPRHHRLGLCFPAVPLPHINQAVRTYLK
NACRIIIGRIQSIQKIYENFEEPQPELVLFSMDEEKTKAIITIKDETHTIGNLLKTYIYEMIPDISFVGYQCVPHKQEMV
LTIIHKASQEDLITLLEKSIQNIIQTFQILEKNVDELIA
;
;MEKIFQNVEIKPFLIDFSNLFIKNAAKKLFQLEEQLPLVPVNVVMDFKGISRAAVHGLSRVLQDEIPNYMLDIKPGGYKI
EDSTDLFMTEQFIRNRINFIPIYAKNETLVFALRSLNNSCEVKTIYSRDLIQVAGPKLKYPIFNPTFEIGFLQPGKSLII
EDIYIKKGIGRKHAAFNLAVKTHFSHLDIEQYPTDKKEYMALSGYKQSSMTSDPRHHRLGLCFPAVPLPHINQAVRTYLK
NACRIIIGRIQSIQKIYENFEEPQPELVLFSMDEEKTKAIITIKDETHTIGNLLKTYIYEMIPDISFVGYQCVPHKQEMV
LTIIHKASQEDLITLLEKSIQNIIQTFQILEKNVDELIA
;
C ? 
4  'polypeptide(L)'        no no 
;MAMQKLFTYIYEFIEYRKMVLLEEKVPYDKFVQMVLNTGFFRINAETLNHGIVSVFIFGANGKYVHHGGDMRTLLTNTLN
EKKHYEELILIVDKPVLSKKNILDIIVEQRAANPTIVINIYPYHLFCINIPKVSAIPKHKLITQEEAQEFLGREYLQPQD
LMQISASDPPVVWLGGRPGDFVQIERPSETAMHAVVIRFITKSKI
;
;MAMQKLFTYIYEFIEYRKMVLLEEKVPYDKFVQMVLNTGFFRINAETLNHGIVSVFIFGANGKYVHHGGDMRTLLTNTLN
EKKHYEELILIVDKPVLSKKNILDIIVEQRAANPTIVINIYPYHLFCINIPKVSAIPKHKLITQEEAQEFLGREYLQPQD
LMQISASDPPVVWLGGRPGDFVQIERPSETAMHAVVIRFITKSKI
;
D ? 
5  'polypeptide(L)'        no no 
;MADNDNEDLIMDDLVEEYVETEEENLVDSEEESEDKDEIVESPSICEGFVQASSQTLVIIPDNERITSNVLTTFEATRLV
AVRAQQLAINGSTMLKKKYSSPIDIAKQELFNRKIPLLVMRCIKVTPEGQKIVEIWNPREMGIPLLD
;
;MADNDNEDLIMDDLVEEYVETEEENLVDSEEESEDKDEIVESPSICEGFVQASSQTLVIIPDNERITSNVLTTFEATRLV
AVRAQQLAINGSTMLKKKYSSPIDIAKQELFNRKIPLLVMRCIKVTPEGQKIVEIWNPREMGIPLLD
;
E ? 
6  'polypeptide(L)'        no no 
;MIDQKIFETTLNIDDPTNFCTNVEAHLLKELENIYVGKCFKNSFILNITGVIQRSPCFIMRTNNSGRGYMHVRFSAVVSY
LNAFDLIAAVKIIKNDSNIILGESLLTEPVTIVIPSSESQNNVAEVGQIVPVQLANSSVYYIPGRQQASATGSIFIPKHT
FSVYHVQEELTQEQALNLTKLVNIIEMLLESRSKKDFKQICFFEKLYYTYSISSDEILDLKIWKGPKGKEMSRLKPCNVL
SFLYDALKNKNSSLGFWARPPNLLKSSPLAYQQDQNSFNATELPIICSAEVMFVTLLKEIINYLQFINDLCDTFNNEQLI
KRHENIWMLIEQRKIGHDF
;
;MIDQKIFETTLNIDDPTNFCTNVEAHLLKELENIYVGKCFKNSFILNITGVIQRSPCFIMRTNNSGRGYMHVRFSAVVSY
LNAFDLIAAVKIIKNDSNIILGESLLTEPVTIVIPSSESQNNVAEVGQIVPVQLANSSVYYIPGRQQASATGSIFIPKHT
FSVYHVQEELTQEQALNLTKLVNIIEMLLESRSKKDFKQICFFEKLYYTYSISSDEILDLKIWKGPKGKEMSRLKPCNVL
SFLYDALKNKNSSLGFWARPPNLLKSSPLAYQQDQNSFNATELPIICSAEVMFVTLLKEIINYLQFINDLCDTFNNEQLI
KRHENIWMLIEQRKIGHDF
;
F ? 
7  'polypeptide(L)'        no no 
;MKICKACSSCMVRTYVDGNIIFRCSCGESVQGDSQNLLVSSKVYHTGEMEDKYKIFIKNAPFDPTNCQIKKDCPNCHLDY
LTQICIGSQKIIILVCRCGYMSNRG
;
;MKICKACSSCMVRTYVDGNIIFRCSCGESVQGDSQNLLVSSKVYHTGEMEDKYKIFIKNAPFDPTNCQIKKDCPNCHLDY
LTQICIGSQKIIILVCRCGYMSNRG
;
G ? 
8  'polypeptide(L)'        no no MLIPVVCFTCGFPIGTYAAIFDKARTEYIKTKMGGTLPQNIPLDASLQIELKDLITALGIPMRVCCRTHLITTLDYRKYY 
MLIPVVCFTCGFPIGTYAAIFDKARTEYIKTKMGGTLPQNIPLDASLQIELKDLITALGIPMRVCCRTHLITTLDYRKYY H ? 
9  polydeoxyribonucleotide no no '(DG)(DC)(DC)(DG)(DA)(DG)(DC)(DA)' GCCGAGCA X ? 
10 polydeoxyribonucleotide no no '(DT)(DC)(DG)(DG)(DC)(DT)(DC)' TCGGCTC Y ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
11 'MAGNESIUM ION' MG 
12 'ZINC ION'      ZN 
# 
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    GLU n 
1  3    ALA n 
1  4    GLY n 
1  5    TYR n 
1  6    ALA n 
1  7    GLU n 
1  8    ILE n 
1  9    ALA n 
1  10   ALA n 
1  11   VAL n 
1  12   GLN n 
1  13   PHE n 
1  14   ASN n 
1  15   ILE n 
1  16   ALA n 
1  17   GLY n 
1  18   ASP n 
1  19   ASN n 
1  20   ASP n 
1  21   HIS n 
1  22   LYS n 
1  23   ARG n 
1  24   GLN n 
1  25   GLY n 
1  26   VAL n 
1  27   MET n 
1  28   GLU n 
1  29   VAL n 
1  30   THR n 
1  31   ILE n 
1  32   SER n 
1  33   ASN n 
1  34   LEU n 
1  35   PHE n 
1  36   GLU n 
1  37   GLY n 
1  38   THR n 
1  39   LEU n 
1  40   PRO n 
1  41   ALA n 
1  42   GLU n 
1  43   GLY n 
1  44   GLY n 
1  45   ILE n 
1  46   TYR n 
1  47   ASP n 
1  48   ALA n 
1  49   ARG n 
1  50   MET n 
1  51   GLY n 
1  52   THR n 
1  53   THR n 
1  54   ASP n 
1  55   HIS n 
1  56   HIS n 
1  57   TYR n 
1  58   LYS n 
1  59   CYS n 
1  60   ILE n 
1  61   THR n 
1  62   CYS n 
1  63   SER n 
1  64   HIS n 
1  65   GLN n 
1  66   ARG n 
1  67   LYS n 
1  68   GLN n 
1  69   CYS n 
1  70   MET n 
1  71   GLY n 
1  72   HIS n 
1  73   PRO n 
1  74   GLY n 
1  75   ILE n 
1  76   LEU n 
1  77   GLN n 
1  78   MET n 
1  79   HIS n 
1  80   ALA n 
1  81   PRO n 
1  82   VAL n 
1  83   LEU n 
1  84   GLN n 
1  85   PRO n 
1  86   LEU n 
1  87   PHE n 
1  88   ILE n 
1  89   ALA n 
1  90   GLU n 
1  91   ILE n 
1  92   ARG n 
1  93   ARG n 
1  94   TRP n 
1  95   LEU n 
1  96   ARG n 
1  97   VAL n 
1  98   ILE n 
1  99   CYS n 
1  100  LEU n 
1  101  ASN n 
1  102  CYS n 
1  103  GLY n 
1  104  ALA n 
1  105  PRO n 
1  106  ILE n 
1  107  VAL n 
1  108  ASP n 
1  109  LEU n 
1  110  LYS n 
1  111  ARG n 
1  112  TYR n 
1  113  GLU n 
1  114  HIS n 
1  115  LEU n 
1  116  ILE n 
1  117  ARG n 
1  118  PRO n 
1  119  LYS n 
1  120  ARG n 
1  121  LEU n 
1  122  ILE n 
1  123  GLU n 
1  124  ALA n 
1  125  ALA n 
1  126  SER n 
1  127  SER n 
1  128  GLN n 
1  129  THR n 
1  130  GLU n 
1  131  GLY n 
1  132  LYS n 
1  133  GLN n 
1  134  CYS n 
1  135  TYR n 
1  136  VAL n 
1  137  CYS n 
1  138  LYS n 
1  139  ALA n 
1  140  VAL n 
1  141  HIS n 
1  142  PRO n 
1  143  LYS n 
1  144  ILE n 
1  145  VAL n 
1  146  LYS n 
1  147  ASP n 
1  148  SER n 
1  149  GLU n 
1  150  ASP n 
1  151  TYR n 
1  152  PHE n 
1  153  THR n 
1  154  PHE n 
1  155  TRP n 
1  156  ALA n 
1  157  ASP n 
1  158  GLN n 
1  159  GLN n 
1  160  GLY n 
1  161  LYS n 
1  162  ILE n 
1  163  ASP n 
1  164  LYS n 
1  165  LEU n 
1  166  TYR n 
1  167  PRO n 
1  168  GLN n 
1  169  ILE n 
1  170  ILE n 
1  171  ARG n 
1  172  GLU n 
1  173  ILE n 
1  174  PHE n 
1  175  SER n 
1  176  ARG n 
1  177  VAL n 
1  178  THR n 
1  179  TYR n 
1  180  ASP n 
1  181  THR n 
1  182  VAL n 
1  183  VAL n 
1  184  LYS n 
1  185  LEU n 
1  186  GLY n 
1  187  ARG n 
1  188  SER n 
1  189  LYS n 
1  190  ASN n 
1  191  SER n 
1  192  HIS n 
1  193  PRO n 
1  194  GLU n 
1  195  LYS n 
1  196  LEU n 
1  197  VAL n 
1  198  LEU n 
1  199  LYS n 
1  200  ALA n 
1  201  ILE n 
1  202  GLN n 
1  203  ILE n 
1  204  PRO n 
1  205  PRO n 
1  206  ILE n 
1  207  SER n 
1  208  ILE n 
1  209  ARG n 
1  210  PRO n 
1  211  GLY n 
1  212  ILE n 
1  213  ARG n 
1  214  LEU n 
1  215  GLY n 
1  216  ILE n 
1  217  GLY n 
1  218  SER n 
1  219  GLY n 
1  220  PRO n 
1  221  GLN n 
1  222  SER n 
1  223  PHE n 
1  224  HIS n 
1  225  ASP n 
1  226  ILE n 
1  227  ASN n 
1  228  ASN n 
1  229  VAL n 
1  230  ILE n 
1  231  GLN n 
1  232  TYR n 
1  233  LEU n 
1  234  VAL n 
1  235  ARG n 
1  236  LYS n 
1  237  ASN n 
1  238  LEU n 
1  239  LEU n 
1  240  ILE n 
1  241  PRO n 
1  242  LYS n 
1  243  ASP n 
1  244  LEU n 
1  245  GLN n 
1  246  ILE n 
1  247  VAL n 
1  248  ARG n 
1  249  GLY n 
1  250  GLN n 
1  251  LYS n 
1  252  ILE n 
1  253  PRO n 
1  254  LEU n 
1  255  ASN n 
1  256  ILE n 
1  257  ASP n 
1  258  ARG n 
1  259  ASN n 
1  260  LEU n 
1  261  GLN n 
1  262  THR n 
1  263  ILE n 
1  264  GLN n 
1  265  GLN n 
1  266  LEU n 
1  267  TYR n 
1  268  TYR n 
1  269  ASN n 
1  270  PHE n 
1  271  LEU n 
1  272  LEU n 
1  273  ASP n 
1  274  SER n 
1  275  VAL n 
1  276  SER n 
1  277  THR n 
1  278  THR n 
1  279  ALA n 
1  280  THR n 
1  281  GLN n 
1  282  GLY n 
1  283  GLY n 
1  284  THR n 
1  285  GLY n 
1  286  LYS n 
1  287  ARG n 
1  288  GLY n 
1  289  ILE n 
1  290  VAL n 
1  291  MET n 
1  292  GLY n 
1  293  ALA n 
1  294  ARG n 
1  295  PRO n 
1  296  ALA n 
1  297  PRO n 
1  298  SER n 
1  299  ILE n 
1  300  MET n 
1  301  ARG n 
1  302  ARG n 
1  303  LEU n 
1  304  PRO n 
1  305  ARG n 
1  306  LYS n 
1  307  GLU n 
1  308  GLY n 
1  309  ARG n 
1  310  ILE n 
1  311  ARG n 
1  312  LYS n 
1  313  SER n 
1  314  LEU n 
1  315  LEU n 
1  316  GLY n 
1  317  SER n 
1  318  GLN n 
1  319  VAL n 
1  320  TRP n 
1  321  SER n 
1  322  ILE n 
1  323  SER n 
1  324  ARG n 
1  325  SER n 
1  326  THR n 
1  327  ILE n 
1  328  CYS n 
1  329  GLY n 
1  330  ASN n 
1  331  SER n 
1  332  ASP n 
1  333  LEU n 
1  334  HIS n 
1  335  LEU n 
1  336  ASP n 
1  337  GLU n 
1  338  VAL n 
1  339  GLY n 
1  340  TYR n 
1  341  PRO n 
1  342  ILE n 
1  343  SER n 
1  344  PHE n 
1  345  ALA n 
1  346  ARG n 
1  347  THR n 
1  348  LEU n 
1  349  GLN n 
1  350  VAL n 
1  351  ALA n 
1  352  GLU n 
1  353  THR n 
1  354  VAL n 
1  355  GLN n 
1  356  HIS n 
1  357  TYR n 
1  358  ASN n 
1  359  ILE n 
1  360  ASN n 
1  361  ARG n 
1  362  LEU n 
1  363  MET n 
1  364  PRO n 
1  365  TYR n 
1  366  PHE n 
1  367  LEU n 
1  368  ASN n 
1  369  GLY n 
1  370  LYS n 
1  371  ARG n 
1  372  GLN n 
1  373  TYR n 
1  374  PRO n 
1  375  GLY n 
1  376  CYS n 
1  377  SER n 
1  378  ARG n 
1  379  VAL n 
1  380  TYR n 
1  381  LYS n 
1  382  GLN n 
1  383  ILE n 
1  384  THR n 
1  385  GLN n 
1  386  SER n 
1  387  VAL n 
1  388  HIS n 
1  389  ASP n 
1  390  ILE n 
1  391  GLU n 
1  392  GLY n 
1  393  LEU n 
1  394  LYS n 
1  395  GLN n 
1  396  ASP n 
1  397  PHE n 
1  398  ARG n 
1  399  LEU n 
1  400  GLU n 
1  401  VAL n 
1  402  GLY n 
1  403  ASP n 
1  404  ILE n 
1  405  LEU n 
1  406  TYR n 
1  407  ARG n 
1  408  ASP n 
1  409  VAL n 
1  410  VAL n 
1  411  THR n 
1  412  GLY n 
1  413  ASP n 
1  414  VAL n 
1  415  ALA n 
1  416  PHE n 
1  417  PHE n 
1  418  ASN n 
1  419  ARG n 
1  420  GLN n 
1  421  PRO n 
1  422  SER n 
1  423  LEU n 
1  424  GLU n 
1  425  ARG n 
1  426  SER n 
1  427  SER n 
1  428  ILE n 
1  429  GLY n 
1  430  VAL n 
1  431  HIS n 
1  432  ARG n 
1  433  ILE n 
1  434  VAL n 
1  435  VAL n 
1  436  LEU n 
1  437  GLU n 
1  438  ASN n 
1  439  PRO n 
1  440  LYS n 
1  441  ILE n 
1  442  SER n 
1  443  THR n 
1  444  PHE n 
1  445  GLN n 
1  446  MET n 
1  447  ASN n 
1  448  VAL n 
1  449  SER n 
1  450  ALA n 
1  451  CYS n 
1  452  ALA n 
1  453  TRP n 
1  454  TYR n 
1  455  ASN n 
1  456  ALA n 
1  457  ASP n 
1  458  PHE n 
1  459  ASP n 
1  460  GLY n 
1  461  ASP n 
1  462  GLN n 
1  463  MET n 
1  464  ASN n 
1  465  LEU n 
1  466  TRP n 
1  467  VAL n 
1  468  PRO n 
1  469  TRP n 
1  470  SER n 
1  471  VAL n 
1  472  MET n 
1  473  SER n 
1  474  ARG n 
1  475  VAL n 
1  476  GLU n 
1  477  ALA n 
1  478  GLU n 
1  479  LEU n 
1  480  LEU n 
1  481  CYS n 
1  482  SER n 
1  483  VAL n 
1  484  ARG n 
1  485  ASN n 
1  486  TRP n 
1  487  PHE n 
1  488  ILE n 
1  489  SER n 
1  490  THR n 
1  491  LYS n 
1  492  SER n 
1  493  SER n 
1  494  GLY n 
1  495  PRO n 
1  496  VAL n 
1  497  ASN n 
1  498  GLY n 
1  499  GLN n 
1  500  VAL n 
1  501  GLN n 
1  502  ASP n 
1  503  SER n 
1  504  THR n 
1  505  VAL n 
1  506  GLY n 
1  507  SER n 
1  508  PHE n 
1  509  LEU n 
1  510  LEU n 
1  511  THR n 
1  512  ARG n 
1  513  THR n 
1  514  ASN n 
1  515  THR n 
1  516  PRO n 
1  517  MET n 
1  518  GLY n 
1  519  LYS n 
1  520  ASN n 
1  521  VAL n 
1  522  MET n 
1  523  ASN n 
1  524  LYS n 
1  525  LEU n 
1  526  HIS n 
1  527  ALA n 
1  528  MET n 
1  529  GLY n 
1  530  LEU n 
1  531  PHE n 
1  532  GLN n 
1  533  THR n 
1  534  THR n 
1  535  GLN n 
1  536  THR n 
1  537  ASP n 
1  538  PRO n 
1  539  PRO n 
1  540  CYS n 
1  541  PHE n 
1  542  ALA n 
1  543  ASN n 
1  544  TYR n 
1  545  SER n 
1  546  PRO n 
1  547  THR n 
1  548  ASP n 
1  549  LEU n 
1  550  LEU n 
1  551  ASP n 
1  552  GLY n 
1  553  LYS n 
1  554  SER n 
1  555  VAL n 
1  556  VAL n 
1  557  SER n 
1  558  MET n 
1  559  LEU n 
1  560  LEU n 
1  561  ARG n 
1  562  GLN n 
1  563  THR n 
1  564  PRO n 
1  565  ILE n 
1  566  ASN n 
1  567  TYR n 
1  568  GLN n 
1  569  ARG n 
1  570  ALA n 
1  571  PRO n 
1  572  THR n 
1  573  TRP n 
1  574  TYR n 
1  575  SER n 
1  576  GLU n 
1  577  VAL n 
1  578  TYR n 
1  579  ALA n 
1  580  PRO n 
1  581  TYR n 
1  582  MET n 
1  583  HIS n 
1  584  TYR n 
1  585  ASN n 
1  586  LYS n 
1  587  GLN n 
1  588  ASP n 
1  589  ILE n 
1  590  SER n 
1  591  THR n 
1  592  GLN n 
1  593  ILE n 
1  594  ARG n 
1  595  ASN n 
1  596  GLY n 
1  597  GLU n 
1  598  LEU n 
1  599  ILE n 
1  600  GLU n 
1  601  GLY n 
1  602  VAL n 
1  603  LEU n 
1  604  ASP n 
1  605  LYS n 
1  606  LYS n 
1  607  ALA n 
1  608  VAL n 
1  609  GLY n 
1  610  ALA n 
1  611  GLY n 
1  612  SER n 
1  613  SER n 
1  614  GLY n 
1  615  GLY n 
1  616  ILE n 
1  617  TYR n 
1  618  HIS n 
1  619  LEU n 
1  620  ILE n 
1  621  SER n 
1  622  ARG n 
1  623  ARG n 
1  624  TYR n 
1  625  GLY n 
1  626  PRO n 
1  627  GLN n 
1  628  GLN n 
1  629  ALA n 
1  630  LEU n 
1  631  LYS n 
1  632  MET n 
1  633  ILE n 
1  634  PHE n 
1  635  ALA n 
1  636  THR n 
1  637  GLN n 
1  638  GLN n 
1  639  LEU n 
1  640  ALA n 
1  641  LEU n 
1  642  ASN n 
1  643  TYR n 
1  644  VAL n 
1  645  ARG n 
1  646  ASN n 
1  647  ALA n 
1  648  GLY n 
1  649  PHE n 
1  650  THR n 
1  651  VAL n 
1  652  SER n 
1  653  THR n 
1  654  ALA n 
1  655  ASP n 
1  656  MET n 
1  657  LEU n 
1  658  LEU n 
1  659  THR n 
1  660  PRO n 
1  661  GLU n 
1  662  ALA n 
1  663  HIS n 
1  664  GLN n 
1  665  GLU n 
1  666  VAL n 
1  667  GLN n 
1  668  GLU n 
1  669  ILE n 
1  670  ILE n 
1  671  ASN n 
1  672  GLU n 
1  673  LEU n 
1  674  LEU n 
1  675  LEU n 
1  676  GLU n 
1  677  SER n 
1  678  GLU n 
1  679  GLU n 
1  680  ILE n 
1  681  ASN n 
1  682  ASN n 
1  683  ARG n 
1  684  LEU n 
1  685  LEU n 
1  686  HIS n 
1  687  GLY n 
1  688  ASP n 
1  689  ILE n 
1  690  MET n 
1  691  PRO n 
1  692  PRO n 
1  693  ILE n 
1  694  GLY n 
1  695  LEU n 
1  696  THR n 
1  697  THR n 
1  698  HIS n 
1  699  ASP n 
1  700  PHE n 
1  701  TYR n 
1  702  GLU n 
1  703  LYS n 
1  704  LEU n 
1  705  GLN n 
1  706  LEU n 
1  707  ASN n 
1  708  ALA n 
1  709  LEU n 
1  710  LYS n 
1  711  PHE n 
1  712  PRO n 
1  713  ASP n 
1  714  ARG n 
1  715  ILE n 
1  716  LEU n 
1  717  LYS n 
1  718  PRO n 
1  719  ILE n 
1  720  MET n 
1  721  ASN n 
1  722  SER n 
1  723  ILE n 
1  724  ASN n 
1  725  PRO n 
1  726  GLU n 
1  727  THR n 
1  728  ASN n 
1  729  GLY n 
1  730  LEU n 
1  731  PHE n 
1  732  GLN n 
1  733  MET n 
1  734  VAL n 
1  735  ALA n 
1  736  THR n 
1  737  GLY n 
1  738  ALA n 
1  739  LYS n 
1  740  GLY n 
1  741  SER n 
1  742  ASN n 
1  743  PRO n 
1  744  ASN n 
1  745  MET n 
1  746  ILE n 
1  747  HIS n 
1  748  ILE n 
1  749  MET n 
1  750  ALA n 
1  751  GLY n 
1  752  ILE n 
1  753  GLY n 
1  754  GLN n 
1  755  ILE n 
1  756  GLU n 
1  757  ILE n 
1  758  ASN n 
1  759  THR n 
1  760  GLN n 
1  761  ARG n 
1  762  ILE n 
1  763  GLN n 
1  764  PRO n 
1  765  GLN n 
1  766  PHE n 
1  767  SER n 
1  768  PHE n 
1  769  GLY n 
1  770  ARG n 
1  771  THR n 
1  772  LEU n 
1  773  VAL n 
1  774  TYR n 
1  775  TYR n 
1  776  PRO n 
1  777  ARG n 
1  778  PHE n 
1  779  ALA n 
1  780  LEU n 
1  781  GLU n 
1  782  ALA n 
1  783  GLN n 
1  784  ALA n 
1  785  TYR n 
1  786  GLY n 
1  787  PHE n 
1  788  ILE n 
1  789  CYS n 
1  790  ASN n 
1  791  SER n 
1  792  TYR n 
1  793  ILE n 
1  794  ALA n 
1  795  GLY n 
1  796  LEU n 
1  797  THR n 
1  798  SER n 
1  799  PRO n 
1  800  GLU n 
1  801  PHE n 
1  802  ILE n 
1  803  PHE n 
1  804  GLY n 
1  805  GLU n 
1  806  MET n 
1  807  ASN n 
1  808  GLY n 
1  809  ARG n 
1  810  PHE n 
1  811  ASP n 
1  812  LEU n 
1  813  ILE n 
1  814  ASN n 
1  815  LYS n 
1  816  ALA n 
1  817  LEU n 
1  818  SER n 
1  819  THR n 
1  820  SER n 
1  821  SER n 
1  822  THR n 
1  823  GLY n 
1  824  TYR n 
1  825  ALA n 
1  826  ASN n 
1  827  ARG n 
1  828  LYS n 
1  829  ALA n 
1  830  ILE n 
1  831  PHE n 
1  832  GLY n 
1  833  LEU n 
1  834  GLN n 
1  835  SER n 
1  836  CYS n 
1  837  ILE n 
1  838  VAL n 
1  839  ASP n 
1  840  TYR n 
1  841  TYR n 
1  842  ARG n 
1  843  ARG n 
1  844  VAL n 
1  845  SER n 
1  846  ILE n 
1  847  ASP n 
1  848  THR n 
1  849  ARG n 
1  850  LEU n 
1  851  VAL n 
1  852  GLN n 
1  853  GLN n 
1  854  LEU n 
1  855  TYR n 
1  856  GLY n 
1  857  GLU n 
1  858  ASP n 
1  859  GLY n 
1  860  LEU n 
1  861  ASP n 
1  862  ALA n 
1  863  ARG n 
1  864  GLN n 
1  865  LEU n 
1  866  GLU n 
1  867  THR n 
1  868  VAL n 
1  869  ARG n 
1  870  PHE n 
1  871  GLU n 
1  872  THR n 
1  873  ILE n 
1  874  MET n 
1  875  LEU n 
1  876  SER n 
1  877  ASP n 
1  878  GLN n 
1  879  GLU n 
1  880  LEU n 
1  881  GLU n 
1  882  ASP n 
1  883  LYS n 
1  884  PHE n 
1  885  LYS n 
1  886  TYR n 
1  887  THR n 
1  888  GLY n 
1  889  ILE n 
1  890  GLN n 
1  891  SER n 
1  892  PRO n 
1  893  LEU n 
1  894  PHE n 
1  895  GLU n 
1  896  GLU n 
1  897  GLU n 
1  898  PHE n 
1  899  SER n 
1  900  ARG n 
1  901  LEU n 
1  902  LYS n 
1  903  LYS n 
1  904  ASP n 
1  905  ARG n 
1  906  ASP n 
1  907  LYS n 
1  908  TYR n 
1  909  ARG n 
1  910  GLN n 
1  911  ILE n 
1  912  PHE n 
1  913  LEU n 
1  914  ASN n 
1  915  VAL n 
1  916  GLU n 
1  917  ASN n 
1  918  PHE n 
1  919  ASN n 
1  920  PHE n 
1  921  SER n 
1  922  GLN n 
1  923  LEU n 
1  924  LEU n 
1  925  THR n 
1  926  ASP n 
1  927  VAL n 
1  928  ARG n 
1  929  GLN n 
1  930  VAL n 
1  931  PRO n 
1  932  VAL n 
1  933  ASN n 
1  934  VAL n 
1  935  ALA n 
1  936  SER n 
1  937  ILE n 
1  938  VAL n 
1  939  LYS n 
1  940  ASN n 
1  941  ILE n 
1  942  LEU n 
1  943  LEU n 
1  944  SER n 
1  945  SER n 
1  946  THR n 
1  947  SER n 
1  948  GLY n 
1  949  VAL n 
1  950  LEU n 
1  951  PRO n 
1  952  PHE n 
1  953  ASP n 
1  954  GLU n 
1  955  LYS n 
1  956  SER n 
1  957  ILE n 
1  958  LEU n 
1  959  GLN n 
1  960  LYS n 
1  961  TYR n 
1  962  ALA n 
1  963  MET n 
1  964  VAL n 
1  965  LYS n 
1  966  THR n 
1  967  PHE n 
1  968  CYS n 
1  969  LYS n 
1  970  ASN n 
1  971  LEU n 
1  972  PRO n 
1  973  TYR n 
1  974  VAL n 
1  975  PHE n 
1  976  ILE n 
1  977  ASN n 
1  978  ASN n 
1  979  ILE n 
1  980  GLN n 
1  981  GLU n 
1  982  ARG n 
1  983  LEU n 
1  984  GLN n 
1  985  THR n 
1  986  PRO n 
1  987  ILE n 
1  988  PRO n 
1  989  VAL n 
1  990  TYR n 
1  991  LEU n 
1  992  LYS n 
1  993  ARG n 
1  994  ALA n 
1  995  ALA n 
1  996  SER n 
1  997  LEU n 
1  998  MET n 
1  999  ARG n 
1  1000 MET n 
1  1001 LEU n 
1  1002 ILE n 
1  1003 ARG n 
1  1004 ILE n 
1  1005 GLU n 
1  1006 LEU n 
1  1007 ALA n 
1  1008 THR n 
1  1009 VAL n 
1  1010 LYS n 
1  1011 THR n 
1  1012 LEU n 
1  1013 ASN n 
1  1014 ILE n 
1  1015 THR n 
1  1016 CYS n 
1  1017 GLU n 
1  1018 GLN n 
1  1019 MET n 
1  1020 SER n 
1  1021 ALA n 
1  1022 ILE n 
1  1023 LEU n 
1  1024 ASP n 
1  1025 LEU n 
1  1026 ILE n 
1  1027 ARG n 
1  1028 LEU n 
1  1029 GLN n 
1  1030 TYR n 
1  1031 THR n 
1  1032 GLN n 
1  1033 SER n 
1  1034 LEU n 
1  1035 ILE n 
1  1036 ASN n 
1  1037 TYR n 
1  1038 GLY n 
1  1039 GLU n 
1  1040 ALA n 
1  1041 VAL n 
1  1042 GLY n 
1  1043 ILE n 
1  1044 LEU n 
1  1045 ALA n 
1  1046 ALA n 
1  1047 GLN n 
1  1048 SER n 
1  1049 VAL n 
1  1050 SER n 
1  1051 GLU n 
1  1052 PRO n 
1  1053 LEU n 
1  1054 THR n 
1  1055 GLN n 
1  1056 TYR n 
1  1057 MET n 
1  1058 LEU n 
1  1059 ASP n 
1  1060 SER n 
1  1061 HIS n 
1  1062 HIS n 
1  1063 ARG n 
1  1064 SER n 
1  1065 VAL n 
1  1066 ALA n 
1  1067 GLY n 
1  1068 GLY n 
1  1069 THR n 
1  1070 ASN n 
1  1071 LYS n 
1  1072 SER n 
1  1073 GLY n 
1  1074 ILE n 
1  1075 VAL n 
1  1076 ARG n 
1  1077 PRO n 
1  1078 GLN n 
1  1079 GLU n 
1  1080 ILE n 
1  1081 PHE n 
1  1082 SER n 
1  1083 ALA n 
1  1084 LYS n 
1  1085 PRO n 
1  1086 VAL n 
1  1087 GLU n 
1  1088 ALA n 
1  1089 GLU n 
1  1090 GLN n 
1  1091 SER n 
1  1092 SER n 
1  1093 GLU n 
1  1094 MET n 
1  1095 LEU n 
1  1096 LEU n 
1  1097 ARG n 
1  1098 LEU n 
1  1099 LYS n 
1  1100 ASN n 
1  1101 PRO n 
1  1102 GLU n 
1  1103 VAL n 
1  1104 GLU n 
1  1105 THR n 
1  1106 ASN n 
1  1107 LYS n 
1  1108 THR n 
1  1109 TYR n 
1  1110 ALA n 
1  1111 GLN n 
1  1112 GLU n 
1  1113 ILE n 
1  1114 ALA n 
1  1115 ASN n 
1  1116 SER n 
1  1117 ILE n 
1  1118 GLU n 
1  1119 LEU n 
1  1120 ILE n 
1  1121 THR n 
1  1122 PHE n 
1  1123 GLU n 
1  1124 ARG n 
1  1125 LEU n 
1  1126 ILE n 
1  1127 LEU n 
1  1128 GLN n 
1  1129 TRP n 
1  1130 HIS n 
1  1131 LEU n 
1  1132 LEU n 
1  1133 TYR n 
1  1134 GLU n 
1  1135 THR n 
1  1136 TYR n 
1  1137 SER n 
1  1138 SER n 
1  1139 THR n 
1  1140 LYS n 
1  1141 LYS n 
1  1142 ASN n 
1  1143 VAL n 
1  1144 MET n 
1  1145 TYR n 
1  1146 PRO n 
1  1147 ASP n 
1  1148 PHE n 
1  1149 ALA n 
1  1150 SER n 
1  1151 ASP n 
1  1152 VAL n 
1  1153 GLU n 
1  1154 TRP n 
1  1155 MET n 
1  1156 THR n 
1  1157 ASP n 
1  1158 PHE n 
1  1159 LEU n 
1  1160 GLU n 
1  1161 ASN n 
1  1162 HIS n 
1  1163 PRO n 
1  1164 LEU n 
1  1165 LEU n 
1  1166 GLN n 
1  1167 PRO n 
1  1168 PRO n 
1  1169 GLU n 
1  1170 ASP n 
1  1171 ILE n 
1  1172 ALA n 
1  1173 ASN n 
1  1174 TRP n 
1  1175 CYS n 
1  1176 ILE n 
1  1177 ARG n 
1  1178 LEU n 
1  1179 GLU n 
1  1180 LEU n 
1  1181 ASN n 
1  1182 LYS n 
1  1183 THR n 
1  1184 THR n 
1  1185 MET n 
1  1186 ILE n 
1  1187 LEU n 
1  1188 LYS n 
1  1189 SER n 
1  1190 ILE n 
1  1191 SER n 
1  1192 LEU n 
1  1193 GLU n 
1  1194 SER n 
1  1195 ILE n 
1  1196 ILE n 
1  1197 ASN n 
1  1198 SER n 
1  1199 LEU n 
1  1200 ARG n 
1  1201 ALA n 
1  1202 LYS n 
1  1203 HIS n 
1  1204 PRO n 
1  1205 ASN n 
1  1206 THR n 
1  1207 TYR n 
1  1208 ILE n 
1  1209 MET n 
1  1210 HIS n 
1  1211 SER n 
1  1212 VAL n 
1  1213 GLU n 
1  1214 ASN n 
1  1215 THR n 
1  1216 ALA n 
1  1217 SER n 
1  1218 GLY n 
1  1219 ILE n 
1  1220 PRO n 
1  1221 ILE n 
1  1222 ILE n 
1  1223 ILE n 
1  1224 ARG n 
1  1225 ILE n 
1  1226 TYR n 
1  1227 LEU n 
1  1228 ARG n 
1  1229 GLU n 
1  1230 SER n 
1  1231 ALA n 
1  1232 PHE n 
1  1233 ARG n 
1  1234 ARG n 
1  1235 SER n 
1  1236 THR n 
1  1237 ASN n 
1  1238 THR n 
1  1239 ARG n 
1  1240 MET n 
1  1241 ALA n 
1  1242 THR n 
1  1243 ASP n 
1  1244 GLU n 
1  1245 LYS n 
1  1246 ILE n 
1  1247 ALA n 
1  1248 VAL n 
1  1249 ASN n 
1  1250 VAL n 
1  1251 VAL n 
1  1252 ASP n 
1  1253 LYS n 
1  1254 LEU n 
1  1255 LEU n 
1  1256 ASN n 
1  1257 SER n 
1  1258 THR n 
1  1259 ILE n 
1  1260 ARG n 
1  1261 GLY n 
1  1262 ILE n 
1  1263 PRO n 
1  1264 GLY n 
1  1265 ILE n 
1  1266 LYS n 
1  1267 ASN n 
1  1268 ALA n 
1  1269 ASN n 
1  1270 VAL n 
1  1271 VAL n 
1  1272 LYS n 
1  1273 LEU n 
1  1274 MET n 
1  1275 ARG n 
1  1276 HIS n 
1  1277 ARG n 
1  1278 VAL n 
1  1279 ASP n 
1  1280 ALA n 
1  1281 GLN n 
1  1282 GLY n 
1  1283 LYS n 
1  1284 LEU n 
1  1285 VAL n 
1  1286 ARG n 
1  1287 LEU n 
1  1288 ASP n 
1  1289 ASN n 
1  1290 ILE n 
1  1291 TYR n 
1  1292 ALA n 
1  1293 ILE n 
1  1294 LYS n 
1  1295 THR n 
1  1296 ASN n 
1  1297 GLY n 
1  1298 THR n 
1  1299 ASN n 
1  1300 ILE n 
1  1301 PHE n 
1  1302 GLY n 
1  1303 ALA n 
1  1304 MET n 
1  1305 LEU n 
1  1306 ASP n 
1  1307 ASP n 
1  1308 ASN n 
1  1309 ILE n 
1  1310 ASP n 
1  1311 PRO n 
1  1312 TYR n 
1  1313 THR n 
1  1314 ILE n 
1  1315 VAL n 
1  1316 SER n 
1  1317 SER n 
1  1318 SER n 
1  1319 ILE n 
1  1320 GLY n 
1  1321 ASP n 
1  1322 THR n 
1  1323 MET n 
1  1324 GLU n 
1  1325 LEU n 
1  1326 TYR n 
1  1327 GLY n 
1  1328 ILE n 
1  1329 GLU n 
1  1330 ALA n 
1  1331 ALA n 
1  1332 ARG n 
1  1333 GLN n 
1  1334 LYS n 
1  1335 ILE n 
1  1336 ILE n 
1  1337 SER n 
1  1338 GLU n 
1  1339 ILE n 
1  1340 ARG n 
1  1341 THR n 
1  1342 VAL n 
1  1343 MET n 
1  1344 GLY n 
1  1345 ASP n 
1  1346 LYS n 
1  1347 GLY n 
1  1348 PRO n 
1  1349 ASN n 
1  1350 HIS n 
1  1351 ARG n 
1  1352 HIS n 
1  1353 LEU n 
1  1354 LEU n 
1  1355 MET n 
1  1356 TYR n 
1  1357 ALA n 
1  1358 ASP n 
1  1359 LEU n 
1  1360 MET n 
1  1361 THR n 
1  1362 ARG n 
1  1363 THR n 
1  1364 GLY n 
1  1365 GLN n 
1  1366 VAL n 
1  1367 THR n 
1  1368 SER n 
1  1369 LEU n 
1  1370 GLU n 
1  1371 LYS n 
1  1372 ALA n 
1  1373 GLY n 
1  1374 LEU n 
1  1375 ASN n 
1  1376 ALA n 
1  1377 ARG n 
1  1378 GLU n 
1  1379 PRO n 
1  1380 SER n 
1  1381 ASN n 
1  1382 VAL n 
1  1383 LEU n 
1  1384 LEU n 
1  1385 ARG n 
1  1386 MET n 
1  1387 ALA n 
1  1388 LEU n 
1  1389 SER n 
1  1390 SER n 
1  1391 PRO n 
1  1392 VAL n 
1  1393 GLN n 
1  1394 VAL n 
1  1395 LEU n 
1  1396 THR n 
1  1397 ASP n 
1  1398 ALA n 
1  1399 ALA n 
1  1400 VAL n 
1  1401 ASP n 
1  1402 SER n 
1  1403 ALA n 
1  1404 VAL n 
1  1405 ASN n 
1  1406 PRO n 
1  1407 ILE n 
1  1408 TYR n 
1  1409 GLY n 
1  1410 ILE n 
1  1411 ALA n 
1  1412 ALA n 
1  1413 PRO n 
1  1414 THR n 
1  1415 LEU n 
1  1416 MET n 
1  1417 GLY n 
1  1418 SER n 
1  1419 VAL n 
1  1420 PRO n 
1  1421 ARG n 
1  1422 ILE n 
1  1423 GLY n 
1  1424 THR n 
1  1425 MET n 
1  1426 TYR n 
1  1427 SER n 
1  1428 ASP n 
1  1429 ILE n 
1  1430 ILE n 
1  1431 MET n 
1  1432 ASP n 
1  1433 GLU n 
1  1434 LYS n 
1  1435 TYR n 
1  1436 ILE n 
1  1437 THR n 
1  1438 GLU n 
1  1439 ASN n 
1  1440 TYR n 
1  1441 LYS n 
1  1442 SER n 
1  1443 VAL n 
1  1444 ASP n 
1  1445 SER n 
1  1446 LEU n 
1  1447 ILE n 
1  1448 ASP n 
1  1449 MET n 
1  1450 LEU n 
2  1    MET n 
2  2    GLU n 
2  3    PRO n 
2  4    LEU n 
2  5    ARG n 
2  6    PRO n 
2  7    GLN n 
2  8    ILE n 
2  9    THR n 
2  10   TYR n 
2  11   GLY n 
2  12   PRO n 
2  13   ILE n 
2  14   GLU n 
2  15   THR n 
2  16   VAL n 
2  17   ASP n 
2  18   ASN n 
2  19   GLU n 
2  20   GLU n 
2  21   LEU n 
2  22   THR n 
2  23   GLU n 
2  24   ALA n 
2  25   ASP n 
2  26   MET n 
2  27   LEU n 
2  28   SER n 
2  29   PHE n 
2  30   ILE n 
2  31   SER n 
2  32   ALA n 
2  33   ALA n 
2  34   VAL n 
2  35   ASN n 
2  36   SER n 
2  37   THR n 
2  38   GLY n 
2  39   LEU n 
2  40   ILE n 
2  41   GLY n 
2  42   TYR n 
2  43   ASN n 
2  44   ILE n 
2  45   LYS n 
2  46   SER n 
2  47   PHE n 
2  48   ASP n 
2  49   ASP n 
2  50   LEU n 
2  51   MET n 
2  52   ASP n 
2  53   ASN n 
2  54   GLY n 
2  55   ILE n 
2  56   PRO n 
2  57   GLN n 
2  58   ILE n 
2  59   VAL n 
2  60   LYS n 
2  61   GLN n 
2  62   MET n 
2  63   PHE n 
2  64   ASN n 
2  65   VAL n 
2  66   ASP n 
2  67   ILE n 
2  68   THR n 
2  69   TYR n 
2  70   LYS n 
2  71   ASP n 
2  72   GLN n 
2  73   ARG n 
2  74   ASP n 
2  75   HIS n 
2  76   THR n 
2  77   GLU n 
2  78   ILE n 
2  79   ASP n 
2  80   LYS n 
2  81   LEU n 
2  82   ARG n 
2  83   GLU n 
2  84   SER n 
2  85   VAL n 
2  86   GLN n 
2  87   ILE n 
2  88   GLN n 
2  89   PHE n 
2  90   ASN n 
2  91   PHE n 
2  92   THR n 
2  93   ASP n 
2  94   VAL n 
2  95   ASN n 
2  96   ILE n 
2  97   GLU n 
2  98   ARG n 
2  99   PRO n 
2  100  GLN n 
2  101  HIS n 
2  102  ARG n 
2  103  ASN n 
2  104  TYR n 
2  105  SER n 
2  106  GLN n 
2  107  GLY n 
2  108  ASN n 
2  109  LYS n 
2  110  ILE n 
2  111  ASN n 
2  112  LEU n 
2  113  LEU n 
2  114  PRO n 
2  115  ASN n 
2  116  LYS n 
2  117  ALA n 
2  118  ARG n 
2  119  LEU n 
2  120  CYS n 
2  121  GLY n 
2  122  LEU n 
2  123  SER n 
2  124  TYR n 
2  125  SER n 
2  126  GLY n 
2  127  PRO n 
2  128  VAL n 
2  129  ASN n 
2  130  LEU n 
2  131  ALA n 
2  132  ALA n 
2  133  GLU n 
2  134  VAL n 
2  135  ILE n 
2  136  LEU n 
2  137  THR n 
2  138  ALA n 
2  139  HIS n 
2  140  TYR n 
2  141  SER n 
2  142  ASN n 
2  143  GLY n 
2  144  ARG n 
2  145  GLN n 
2  146  GLU n 
2  147  VAL n 
2  148  LYS n 
2  149  ARG n 
2  150  ALA n 
2  151  SER n 
2  152  ILE n 
2  153  PRO n 
2  154  PRO n 
2  155  PHE n 
2  156  GLN n 
2  157  VAL n 
2  158  SER n 
2  159  THR n 
2  160  PHE n 
2  161  PRO n 
2  162  ILE n 
2  163  MET n 
2  164  ARG n 
2  165  GLY n 
2  166  SER n 
2  167  ASN n 
2  168  ARG n 
2  169  CYS n 
2  170  HIS n 
2  171  THR n 
2  172  HIS n 
2  173  HIS n 
2  174  LEU n 
2  175  SER n 
2  176  LYS n 
2  177  THR n 
2  178  ALA n 
2  179  LYS n 
2  180  LYS n 
2  181  GLU n 
2  182  ILE n 
2  183  GLY n 
2  184  GLU n 
2  185  ASP n 
2  186  PRO n 
2  187  ASN n 
2  188  GLU n 
2  189  PRO n 
2  190  GLY n 
2  191  GLY n 
2  192  TYR n 
2  193  PHE n 
2  194  ILE n 
2  195  ALA n 
2  196  ARG n 
2  197  GLY n 
2  198  GLY n 
2  199  GLU n 
2  200  TRP n 
2  201  VAL n 
2  202  VAL n 
2  203  ASP n 
2  204  LEU n 
2  205  LEU n 
2  206  GLU n 
2  207  ASN n 
2  208  ILE n 
2  209  ARG n 
2  210  PHE n 
2  211  ASN n 
2  212  THR n 
2  213  LEU n 
2  214  HIS n 
2  215  ILE n 
2  216  HIS n 
2  217  TYR n 
2  218  HIS n 
2  219  THR n 
2  220  MET n 
2  221  GLN n 
2  222  GLN n 
2  223  GLY n 
2  224  ASN n 
2  225  ASN n 
2  226  GLU n 
2  227  ILE n 
2  228  ILE n 
2  229  ARG n 
2  230  GLY n 
2  231  GLU n 
2  232  PHE n 
2  233  ILE n 
2  234  SER n 
2  235  GLN n 
2  236  PRO n 
2  237  GLY n 
2  238  GLY n 
2  239  ALA n 
2  240  PHE n 
2  241  GLU n 
2  242  ASN n 
2  243  SER n 
2  244  SER n 
2  245  GLN n 
2  246  ILE n 
2  247  ILE n 
2  248  ILE n 
2  249  ARG n 
2  250  TYR n 
2  251  MET n 
2  252  THR n 
2  253  THR n 
2  254  GLY n 
2  255  ALA n 
2  256  ILE n 
2  257  THR n 
2  258  ILE n 
2  259  GLU n 
2  260  ILE n 
2  261  ASN n 
2  262  SER n 
2  263  THR n 
2  264  LYS n 
2  265  PHE n 
2  266  SER n 
2  267  LYS n 
2  268  LEU n 
2  269  ARG n 
2  270  ILE n 
2  271  PRO n 
2  272  TRP n 
2  273  TYR n 
2  274  LEU n 
2  275  ILE n 
2  276  PHE n 
2  277  ARG n 
2  278  MET n 
2  279  PHE n 
2  280  GLY n 
2  281  MET n 
2  282  THR n 
2  283  GLY n 
2  284  ASP n 
2  285  ASP n 
2  286  SER n 
2  287  ILE n 
2  288  ILE n 
2  289  GLU n 
2  290  GLN n 
2  291  VAL n 
2  292  VAL n 
2  293  PHE n 
2  294  ASP n 
2  295  LEU n 
2  296  GLU n 
2  297  SER n 
2  298  ASN n 
2  299  SER n 
2  300  LEU n 
2  301  VAL n 
2  302  ASN n 
2  303  THR n 
2  304  PHE n 
2  305  MET n 
2  306  ILE n 
2  307  GLU n 
2  308  ILE n 
2  309  LEU n 
2  310  GLU n 
2  311  LYS n 
2  312  SER n 
2  313  ILE n 
2  314  HIS n 
2  315  VAL n 
2  316  LEU n 
2  317  ASP n 
2  318  PRO n 
2  319  ILE n 
2  320  PHE n 
2  321  GLN n 
2  322  PRO n 
2  323  VAL n 
2  324  GLN n 
2  325  HIS n 
2  326  GLU n 
2  327  LEU n 
2  328  ASN n 
2  329  ARG n 
2  330  GLU n 
2  331  LYS n 
2  332  ILE n 
2  333  ILE n 
2  334  GLN n 
2  335  PHE n 
2  336  LEU n 
2  337  SER n 
2  338  GLU n 
2  339  LYS n 
2  340  VAL n 
2  341  SER n 
2  342  LYS n 
2  343  PHE n 
2  344  VAL n 
2  345  SER n 
2  346  ASN n 
2  347  PRO n 
2  348  SER n 
2  349  ALA n 
2  350  TYR n 
2  351  LYS n 
2  352  SER n 
2  353  ASP n 
2  354  GLU n 
2  355  ASN n 
2  356  ALA n 
2  357  VAL n 
2  358  GLN n 
2  359  TYR n 
2  360  LEU n 
2  361  ASN n 
2  362  GLU n 
2  363  ARG n 
2  364  GLN n 
2  365  LEU n 
2  366  THR n 
2  367  ILE n 
2  368  LEU n 
2  369  ASP n 
2  370  LYS n 
2  371  ILE n 
2  372  LEU n 
2  373  LEU n 
2  374  PRO n 
2  375  HIS n 
2  376  MET n 
2  377  GLY n 
2  378  GLN n 
2  379  THR n 
2  380  ALA n 
2  381  ASP n 
2  382  THR n 
2  383  ARG n 
2  384  VAL n 
2  385  ARG n 
2  386  LYS n 
2  387  LEU n 
2  388  ARG n 
2  389  PHE n 
2  390  LEU n 
2  391  GLY n 
2  392  LEU n 
2  393  LEU n 
2  394  ILE n 
2  395  HIS n 
2  396  LYS n 
2  397  ILE n 
2  398  LEU n 
2  399  LEU n 
2  400  VAL n 
2  401  ILE n 
2  402  MET n 
2  403  ASN n 
2  404  VAL n 
2  405  PHE n 
2  406  PRO n 
2  407  PRO n 
2  408  THR n 
2  409  ASP n 
2  410  ARG n 
2  411  ASP n 
2  412  SER n 
2  413  TYR n 
2  414  ARG n 
2  415  THR n 
2  416  LYS n 
2  417  ARG n 
2  418  VAL n 
2  419  HIS n 
2  420  GLY n 
2  421  SER n 
2  422  GLY n 
2  423  VAL n 
2  424  SER n 
2  425  LEU n 
2  426  ALA n 
2  427  LYS n 
2  428  ALA n 
2  429  PHE n 
2  430  LYS n 
2  431  ALA n 
2  432  ILE n 
2  433  PHE n 
2  434  ASN n 
2  435  THR n 
2  436  SER n 
2  437  VAL n 
2  438  ILE n 
2  439  ALA n 
2  440  PRO n 
2  441  ILE n 
2  442  ILE n 
2  443  ASN n 
2  444  GLY n 
2  445  PHE n 
2  446  LYS n 
2  447  GLU n 
2  448  LEU n 
2  449  LEU n 
2  450  LYS n 
2  451  GLN n 
2  452  THR n 
2  453  ALA n 
2  454  PHE n 
2  455  GLU n 
2  456  GLU n 
2  457  LEU n 
2  458  THR n 
2  459  GLN n 
2  460  ARG n 
2  461  ASN n 
2  462  ILE n 
2  463  ILE n 
2  464  GLU n 
2  465  ALA n 
2  466  PHE n 
2  467  SER n 
2  468  ALA n 
2  469  ALA n 
2  470  LEU n 
2  471  SER n 
2  472  LYS n 
2  473  ASN n 
2  474  THR n 
2  475  ALA n 
2  476  SER n 
2  477  ASP n 
2  478  LEU n 
2  479  ASN n 
2  480  ARG n 
2  481  SER n 
2  482  MET n 
2  483  GLU n 
2  484  GLN n 
2  485  SER n 
2  486  ILE n 
2  487  ILE n 
2  488  SER n 
2  489  GLY n 
2  490  ASN n 
2  491  LYS n 
2  492  THR n 
2  493  ILE n 
2  494  MET n 
2  495  VAL n 
2  496  ARG n 
2  497  GLN n 
2  498  ARG n 
2  499  PRO n 
2  500  ILE n 
2  501  VAL n 
2  502  ASN n 
2  503  ARG n 
2  504  VAL n 
2  505  SER n 
2  506  THR n 
2  507  GLN n 
2  508  SER n 
2  509  LEU n 
2  510  GLU n 
2  511  ARG n 
2  512  LYS n 
2  513  ASN n 
2  514  LEU n 
2  515  LEU n 
2  516  ASN n 
2  517  THR n 
2  518  ILE n 
2  519  SER n 
2  520  ALA n 
2  521  LEU n 
2  522  ARG n 
2  523  THR n 
2  524  VAL n 
2  525  ASN n 
2  526  THR n 
2  527  HIS n 
2  528  ASN n 
2  529  THR n 
2  530  THR n 
2  531  ASN n 
2  532  ALA n 
2  533  SER n 
2  534  LYS n 
2  535  GLN n 
2  536  THR n 
2  537  GLU n 
2  538  ARG n 
2  539  ALA n 
2  540  ASP n 
2  541  MET n 
2  542  MET n 
2  543  ARG n 
2  544  ARG n 
2  545  VAL n 
2  546  HIS n 
2  547  ALA n 
2  548  SER n 
2  549  TYR n 
2  550  PRO n 
2  551  GLY n 
2  552  TYR n 
2  553  ILE n 
2  554  CYS n 
2  555  VAL n 
2  556  ALA n 
2  557  GLN n 
2  558  SER n 
2  559  ALA n 
2  560  ASP n 
2  561  THR n 
2  562  GLY n 
2  563  GLU n 
2  564  LYS n 
2  565  VAL n 
2  566  GLY n 
2  567  MET n 
2  568  SER n 
2  569  LYS n 
2  570  GLN n 
2  571  LEU n 
2  572  ALA n 
2  573  ILE n 
2  574  THR n 
2  575  ALA n 
2  576  ASN n 
2  577  VAL n 
2  578  CYS n 
2  579  THR n 
2  580  ALA n 
2  581  GLY n 
2  582  GLU n 
2  583  VAL n 
2  584  LEU n 
2  585  SER n 
2  586  LEU n 
2  587  LYS n 
2  588  GLN n 
2  589  ARG n 
2  590  LEU n 
2  591  LEU n 
2  592  SER n 
2  593  ASP n 
2  594  PRO n 
2  595  ALA n 
2  596  ILE n 
2  597  GLN n 
2  598  GLN n 
2  599  LEU n 
2  600  ALA n 
2  601  ASP n 
2  602  VAL n 
2  603  SER n 
2  604  ASN n 
2  605  LYS n 
2  606  ASP n 
2  607  ILE n 
2  608  VAL n 
2  609  ARG n 
2  610  LYS n 
2  611  GLY n 
2  612  LEU n 
2  613  ALA n 
2  614  ARG n 
2  615  VAL n 
2  616  PHE n 
2  617  ILE n 
2  618  ASN n 
2  619  GLY n 
2  620  GLU n 
2  621  TRP n 
2  622  ILE n 
2  623  GLY n 
2  624  CYS n 
2  625  CYS n 
2  626  THR n 
2  627  ASN n 
2  628  ALA n 
2  629  PHE n 
2  630  GLU n 
2  631  LEU n 
2  632  ALA n 
2  633  GLN n 
2  634  ARG n 
2  635  TYR n 
2  636  ARG n 
2  637  MET n 
2  638  LEU n 
2  639  ARG n 
2  640  ARG n 
2  641  GLU n 
2  642  GLY n 
2  643  LYS n 
2  644  VAL n 
2  645  VAL n 
2  646  HIS n 
2  647  PRO n 
2  648  HIS n 
2  649  THR n 
2  650  THR n 
2  651  ILE n 
2  652  TYR n 
2  653  TRP n 
2  654  ASP n 
2  655  SER n 
2  656  MET n 
2  657  VAL n 
2  658  ASP n 
2  659  GLU n 
2  660  VAL n 
2  661  GLU n 
2  662  PHE n 
2  663  TRP n 
2  664  LEU n 
2  665  ASP n 
2  666  VAL n 
2  667  GLY n 
2  668  ARG n 
2  669  LEU n 
2  670  THR n 
2  671  ARG n 
2  672  PRO n 
2  673  LEU n 
2  674  LEU n 
2  675  ILE n 
2  676  VAL n 
2  677  ASP n 
2  678  ASN n 
2  679  ASN n 
2  680  ILE n 
2  681  GLU n 
2  682  LYS n 
2  683  TYR n 
2  684  ASN n 
2  685  GLN n 
2  686  ALA n 
2  687  CYS n 
2  688  TYR n 
2  689  LYS n 
2  690  ALA n 
2  691  ALA n 
2  692  GLU n 
2  693  ALA n 
2  694  ARG n 
2  695  LYS n 
2  696  LYS n 
2  697  GLY n 
2  698  ASP n 
2  699  LYS n 
2  700  ASP n 
2  701  TRP n 
2  702  GLU n 
2  703  LYS n 
2  704  HIS n 
2  705  LYS n 
2  706  ILE n 
2  707  PRO n 
2  708  PHE n 
2  709  ILE n 
2  710  GLN n 
2  711  ASN n 
2  712  THR n 
2  713  ARG n 
2  714  PHE n 
2  715  THR n 
2  716  PRO n 
2  717  GLN n 
2  718  MET n 
2  719  ALA n 
2  720  LYS n 
2  721  ASP n 
2  722  ILE n 
2  723  LEU n 
2  724  ALA n 
2  725  GLY n 
2  726  THR n 
2  727  LEU n 
2  728  THR n 
2  729  LEU n 
2  730  GLU n 
2  731  ASP n 
2  732  LEU n 
2  733  VAL n 
2  734  ALA n 
2  735  GLN n 
2  736  GLY n 
2  737  ILE n 
2  738  CYS n 
2  739  GLU n 
2  740  PHE n 
2  741  ILE n 
2  742  THR n 
2  743  PRO n 
2  744  GLU n 
2  745  GLU n 
2  746  ALA n 
2  747  GLU n 
2  748  ASN n 
2  749  CYS n 
2  750  LEU n 
2  751  VAL n 
2  752  ALA n 
2  753  PHE n 
2  754  SER n 
2  755  ILE n 
2  756  ILE n 
2  757  GLU n 
2  758  LEU n 
2  759  ARG n 
2  760  LYS n 
2  761  HIS n 
2  762  LYS n 
2  763  HIS n 
2  764  ASP n 
2  765  VAL n 
2  766  THR n 
2  767  ARG n 
2  768  ARG n 
2  769  PHE n 
2  770  THR n 
2  771  HIS n 
2  772  VAL n 
2  773  ASP n 
2  774  VAL n 
2  775  PRO n 
2  776  GLN n 
2  777  ALA n 
2  778  ILE n 
2  779  LEU n 
2  780  GLY n 
2  781  LEU n 
2  782  ALA n 
2  783  ALA n 
2  784  LEU n 
2  785  VAL n 
2  786  SER n 
2  787  PRO n 
2  788  TYR n 
2  789  ALA n 
2  790  ASN n 
2  791  CYS n 
2  792  THR n 
2  793  GLN n 
2  794  PRO n 
2  795  ALA n 
2  796  ARG n 
2  797  VAL n 
2  798  THR n 
2  799  TYR n 
2  800  GLU n 
2  801  THR n 
2  802  ASN n 
2  803  GLN n 
2  804  GLY n 
2  805  ARG n 
2  806  GLN n 
2  807  THR n 
2  808  GLY n 
2  809  GLY n 
2  810  TRP n 
2  811  TYR n 
2  812  CYS n 
2  813  PHE n 
2  814  SER n 
2  815  TRP n 
2  816  PRO n 
2  817  TYR n 
2  818  ARG n 
2  819  VAL n 
2  820  ASP n 
2  821  MET n 
2  822  ASN n 
2  823  ARG n 
2  824  PHE n 
2  825  PHE n 
2  826  GLN n 
2  827  PHE n 
2  828  TYR n 
2  829  ASN n 
2  830  GLU n 
2  831  MET n 
2  832  PRO n 
2  833  LEU n 
2  834  VAL n 
2  835  LYS n 
2  836  THR n 
2  837  ILE n 
2  838  ALA n 
2  839  HIS n 
2  840  ASN n 
2  841  TYR n 
2  842  VAL n 
2  843  ILE n 
2  844  PRO n 
2  845  ASN n 
2  846  GLY n 
2  847  LEU n 
2  848  ASN n 
2  849  THR n 
2  850  ILE n 
2  851  VAL n 
2  852  ALA n 
2  853  TYR n 
2  854  MET n 
2  855  ILE n 
2  856  TYR n 
2  857  GLY n 
2  858  GLY n 
2  859  TYR n 
2  860  ASN n 
2  861  GLN n 
2  862  GLU n 
2  863  ASP n 
2  864  SER n 
2  865  VAL n 
2  866  ILE n 
2  867  VAL n 
2  868  SER n 
2  869  GLN n 
2  870  SER n 
2  871  PHE n 
2  872  ILE n 
2  873  ASP n 
2  874  ARG n 
2  875  GLY n 
2  876  GLY n 
2  877  PHE n 
2  878  ALA n 
2  879  GLY n 
2  880  THR n 
2  881  PHE n 
2  882  TYR n 
2  883  ARG n 
2  884  GLU n 
2  885  GLU n 
2  886  LYS n 
2  887  VAL n 
2  888  GLU n 
2  889  LEU n 
2  890  GLU n 
2  891  SER n 
2  892  ASP n 
2  893  ILE n 
2  894  GLU n 
2  895  SER n 
2  896  PHE n 
2  897  GLY n 
2  898  LYS n 
2  899  PRO n 
2  900  ASP n 
2  901  PRO n 
2  902  LEU n 
2  903  ILE n 
2  904  THR n 
2  905  LYS n 
2  906  ASN n 
2  907  LEU n 
2  908  LYS n 
2  909  PRO n 
2  910  GLY n 
2  911  ALA n 
2  912  ASN n 
2  913  TYR n 
2  914  GLU n 
2  915  LYS n 
2  916  LEU n 
2  917  VAL n 
2  918  ASP n 
2  919  GLY n 
2  920  PHE n 
2  921  VAL n 
2  922  PRO n 
2  923  VAL n 
2  924  GLY n 
2  925  THR n 
2  926  VAL n 
2  927  VAL n 
2  928  LYS n 
2  929  LYS n 
2  930  GLY n 
2  931  ASP n 
2  932  ILE n 
2  933  ILE n 
2  934  ILE n 
2  935  GLY n 
2  936  LYS n 
2  937  VAL n 
2  938  ALA n 
2  939  LYS n 
2  940  ILE n 
2  941  ARG n 
2  942  GLY n 
2  943  GLU n 
2  944  LYS n 
2  945  ASP n 
2  946  GLU n 
2  947  LEU n 
2  948  ASN n 
2  949  LYS n 
2  950  TYR n 
2  951  ILE n 
2  952  ASP n 
2  953  ARG n 
2  954  SER n 
2  955  VAL n 
2  956  MET n 
2  957  TYR n 
2  958  GLY n 
2  959  PHE n 
2  960  ASP n 
2  961  GLU n 
2  962  PRO n 
2  963  ALA n 
2  964  VAL n 
2  965  VAL n 
2  966  ASP n 
2  967  ALA n 
2  968  VAL n 
2  969  MET n 
2  970  ARG n 
2  971  PRO n 
2  972  HIS n 
2  973  GLY n 
2  974  PRO n 
2  975  ASN n 
2  976  ASP n 
2  977  GLU n 
2  978  ILE n 
2  979  PHE n 
2  980  GLY n 
2  981  LEU n 
2  982  MET n 
2  983  ARG n 
2  984  LEU n 
2  985  ARG n 
2  986  TYR n 
2  987  GLU n 
2  988  ARG n 
2  989  ASN n 
2  990  LEU n 
2  991  ASN n 
2  992  ILE n 
2  993  GLY n 
2  994  ASP n 
2  995  LYS n 
2  996  MET n 
2  997  SER n 
2  998  SER n 
2  999  ARG n 
2  1000 SER n 
2  1001 GLY n 
2  1002 ASN n 
2  1003 LYS n 
2  1004 GLY n 
2  1005 ILE n 
2  1006 ALA n 
2  1007 ALA n 
2  1008 LEU n 
2  1009 ALA n 
2  1010 LEU n 
2  1011 PRO n 
2  1012 THR n 
2  1013 SER n 
2  1014 ASP n 
2  1015 MET n 
2  1016 PRO n 
2  1017 PHE n 
2  1018 THR n 
2  1019 GLU n 
2  1020 ASP n 
2  1021 GLY n 
2  1022 LEU n 
2  1023 GLN n 
2  1024 PRO n 
2  1025 ASP n 
2  1026 LEU n 
2  1027 ILE n 
2  1028 VAL n 
2  1029 ASN n 
2  1030 PRO n 
2  1031 HIS n 
2  1032 SER n 
2  1033 HIS n 
2  1034 PRO n 
2  1035 SER n 
2  1036 ARG n 
2  1037 MET n 
2  1038 THR n 
2  1039 ASN n 
2  1040 GLY n 
2  1041 GLN n 
2  1042 MET n 
2  1043 ILE n 
2  1044 GLU n 
2  1045 THR n 
2  1046 THR n 
2  1047 VAL n 
2  1048 GLY n 
2  1049 LEU n 
2  1050 ALA n 
2  1051 ASN n 
2  1052 ALA n 
2  1053 LEU n 
2  1054 GLN n 
2  1055 GLY n 
2  1056 VAL n 
2  1057 VAL n 
2  1058 THR n 
2  1059 ASP n 
2  1060 GLY n 
2  1061 THR n 
2  1062 ALA n 
2  1063 PHE n 
2  1064 LEU n 
2  1065 PRO n 
2  1066 ILE n 
2  1067 ASN n 
2  1068 VAL n 
2  1069 GLN n 
2  1070 LEU n 
2  1071 LEU n 
2  1072 SER n 
2  1073 GLU n 
2  1074 ARG n 
2  1075 LEU n 
2  1076 ALA n 
2  1077 GLN n 
2  1078 GLU n 
2  1079 GLY n 
2  1080 LEU n 
2  1081 ARG n 
2  1082 PHE n 
2  1083 ASN n 
2  1084 GLY n 
2  1085 CYS n 
2  1086 GLN n 
2  1087 LYS n 
2  1088 MET n 
2  1089 PHE n 
2  1090 ASN n 
2  1091 GLY n 
2  1092 GLN n 
2  1093 THR n 
2  1094 GLY n 
2  1095 GLU n 
2  1096 TYR n 
2  1097 PHE n 
2  1098 ASP n 
2  1099 ALA n 
2  1100 ALA n 
2  1101 ILE n 
2  1102 PHE n 
2  1103 ILE n 
2  1104 GLY n 
2  1105 PRO n 
2  1106 THR n 
2  1107 TYR n 
2  1108 HIS n 
2  1109 GLN n 
2  1110 ARG n 
2  1111 LEU n 
2  1112 GLN n 
2  1113 LYS n 
2  1114 PHE n 
2  1115 VAL n 
2  1116 LEU n 
2  1117 ASP n 
2  1118 ASP n 
2  1119 ARG n 
2  1120 TYR n 
2  1121 ALA n 
2  1122 VAL n 
2  1123 ALA n 
2  1124 SER n 
2  1125 TYR n 
2  1126 GLY n 
2  1127 PRO n 
2  1128 THR n 
2  1129 ASP n 
2  1130 ALA n 
2  1131 LEU n 
2  1132 THR n 
2  1133 GLY n 
2  1134 GLN n 
2  1135 PRO n 
2  1136 LEU n 
2  1137 ASP n 
2  1138 GLY n 
2  1139 LYS n 
2  1140 ARG n 
2  1141 SER n 
2  1142 HIS n 
2  1143 GLY n 
2  1144 GLY n 
2  1145 LEU n 
2  1146 ARG n 
2  1147 LEU n 
2  1148 GLY n 
2  1149 GLU n 
2  1150 MET n 
2  1151 GLU n 
2  1152 HIS n 
2  1153 TRP n 
2  1154 VAL n 
2  1155 LEU n 
2  1156 THR n 
2  1157 ALA n 
2  1158 GLN n 
2  1159 GLY n 
2  1160 ALA n 
2  1161 MET n 
2  1162 GLN n 
2  1163 THR n 
2  1164 ILE n 
2  1165 ILE n 
2  1166 GLU n 
2  1167 LYS n 
2  1168 SER n 
2  1169 HIS n 
2  1170 ASP n 
2  1171 ASP n 
2  1172 SER n 
2  1173 ASP n 
2  1174 GLY n 
2  1175 CYS n 
2  1176 ILE n 
2  1177 SER n 
2  1178 TYR n 
2  1179 ILE n 
2  1180 CYS n 
2  1181 ARG n 
2  1182 ASN n 
2  1183 CYS n 
2  1184 GLY n 
2  1185 GLU n 
2  1186 PRO n 
2  1187 ALA n 
2  1188 ILE n 
2  1189 TYR n 
2  1190 ASN n 
2  1191 ALA n 
2  1192 SER n 
2  1193 HIS n 
2  1194 PRO n 
2  1195 ILE n 
2  1196 TYR n 
2  1197 LYS n 
2  1198 CYS n 
2  1199 MET n 
2  1200 ASN n 
2  1201 CYS n 
2  1202 ASP n 
2  1203 VAL n 
2  1204 GLN n 
2  1205 ALA n 
2  1206 ASP n 
2  1207 ILE n 
2  1208 GLY n 
2  1209 MET n 
2  1210 VAL n 
2  1211 ASP n 
2  1212 SER n 
2  1213 ARG n 
2  1214 ARG n 
2  1215 SER n 
2  1216 SER n 
2  1217 ILE n 
2  1218 VAL n 
2  1219 PHE n 
2  1220 GLN n 
2  1221 HIS n 
2  1222 GLU n 
2  1223 MET n 
2  1224 ARG n 
2  1225 ALA n 
2  1226 ALA n 
2  1227 ASN n 
2  1228 VAL n 
2  1229 ASN n 
2  1230 ILE n 
2  1231 THR n 
2  1232 SER n 
2  1233 VAL n 
2  1234 LEU n 
2  1235 SER n 
2  1236 PRO n 
2  1237 ARG n 
2  1238 VAL n 
2  1239 PHE n 
2  1240 GLN n 
2  1241 PRO n 
2  1242 ALA n 
3  1    MET n 
3  2    GLU n 
3  3    LYS n 
3  4    ILE n 
3  5    PHE n 
3  6    GLN n 
3  7    ASN n 
3  8    VAL n 
3  9    GLU n 
3  10   ILE n 
3  11   LYS n 
3  12   PRO n 
3  13   PHE n 
3  14   LEU n 
3  15   ILE n 
3  16   ASP n 
3  17   PHE n 
3  18   SER n 
3  19   ASN n 
3  20   LEU n 
3  21   PHE n 
3  22   ILE n 
3  23   LYS n 
3  24   ASN n 
3  25   ALA n 
3  26   ALA n 
3  27   LYS n 
3  28   LYS n 
3  29   LEU n 
3  30   PHE n 
3  31   GLN n 
3  32   LEU n 
3  33   GLU n 
3  34   GLU n 
3  35   GLN n 
3  36   LEU n 
3  37   PRO n 
3  38   LEU n 
3  39   VAL n 
3  40   PRO n 
3  41   VAL n 
3  42   ASN n 
3  43   VAL n 
3  44   VAL n 
3  45   MET n 
3  46   ASP n 
3  47   PHE n 
3  48   LYS n 
3  49   GLY n 
3  50   ILE n 
3  51   SER n 
3  52   ARG n 
3  53   ALA n 
3  54   ALA n 
3  55   VAL n 
3  56   HIS n 
3  57   GLY n 
3  58   LEU n 
3  59   SER n 
3  60   ARG n 
3  61   VAL n 
3  62   LEU n 
3  63   GLN n 
3  64   ASP n 
3  65   GLU n 
3  66   ILE n 
3  67   PRO n 
3  68   ASN n 
3  69   TYR n 
3  70   MET n 
3  71   LEU n 
3  72   ASP n 
3  73   ILE n 
3  74   LYS n 
3  75   PRO n 
3  76   GLY n 
3  77   GLY n 
3  78   TYR n 
3  79   LYS n 
3  80   ILE n 
3  81   GLU n 
3  82   ASP n 
3  83   SER n 
3  84   THR n 
3  85   ASP n 
3  86   LEU n 
3  87   PHE n 
3  88   MET n 
3  89   THR n 
3  90   GLU n 
3  91   GLN n 
3  92   PHE n 
3  93   ILE n 
3  94   ARG n 
3  95   ASN n 
3  96   ARG n 
3  97   ILE n 
3  98   ASN n 
3  99   PHE n 
3  100  ILE n 
3  101  PRO n 
3  102  ILE n 
3  103  TYR n 
3  104  ALA n 
3  105  LYS n 
3  106  ASN n 
3  107  GLU n 
3  108  THR n 
3  109  LEU n 
3  110  VAL n 
3  111  PHE n 
3  112  ALA n 
3  113  LEU n 
3  114  ARG n 
3  115  SER n 
3  116  LEU n 
3  117  ASN n 
3  118  ASN n 
3  119  SER n 
3  120  CYS n 
3  121  GLU n 
3  122  VAL n 
3  123  LYS n 
3  124  THR n 
3  125  ILE n 
3  126  TYR n 
3  127  SER n 
3  128  ARG n 
3  129  ASP n 
3  130  LEU n 
3  131  ILE n 
3  132  GLN n 
3  133  VAL n 
3  134  ALA n 
3  135  GLY n 
3  136  PRO n 
3  137  LYS n 
3  138  LEU n 
3  139  LYS n 
3  140  TYR n 
3  141  PRO n 
3  142  ILE n 
3  143  PHE n 
3  144  ASN n 
3  145  PRO n 
3  146  THR n 
3  147  PHE n 
3  148  GLU n 
3  149  ILE n 
3  150  GLY n 
3  151  PHE n 
3  152  LEU n 
3  153  GLN n 
3  154  PRO n 
3  155  GLY n 
3  156  LYS n 
3  157  SER n 
3  158  LEU n 
3  159  ILE n 
3  160  ILE n 
3  161  GLU n 
3  162  ASP n 
3  163  ILE n 
3  164  TYR n 
3  165  ILE n 
3  166  LYS n 
3  167  LYS n 
3  168  GLY n 
3  169  ILE n 
3  170  GLY n 
3  171  ARG n 
3  172  LYS n 
3  173  HIS n 
3  174  ALA n 
3  175  ALA n 
3  176  PHE n 
3  177  ASN n 
3  178  LEU n 
3  179  ALA n 
3  180  VAL n 
3  181  LYS n 
3  182  THR n 
3  183  HIS n 
3  184  PHE n 
3  185  SER n 
3  186  HIS n 
3  187  LEU n 
3  188  ASP n 
3  189  ILE n 
3  190  GLU n 
3  191  GLN n 
3  192  TYR n 
3  193  PRO n 
3  194  THR n 
3  195  ASP n 
3  196  LYS n 
3  197  LYS n 
3  198  GLU n 
3  199  TYR n 
3  200  MET n 
3  201  ALA n 
3  202  LEU n 
3  203  SER n 
3  204  GLY n 
3  205  TYR n 
3  206  LYS n 
3  207  GLN n 
3  208  SER n 
3  209  SER n 
3  210  MET n 
3  211  THR n 
3  212  SER n 
3  213  ASP n 
3  214  PRO n 
3  215  ARG n 
3  216  HIS n 
3  217  HIS n 
3  218  ARG n 
3  219  LEU n 
3  220  GLY n 
3  221  LEU n 
3  222  CYS n 
3  223  PHE n 
3  224  PRO n 
3  225  ALA n 
3  226  VAL n 
3  227  PRO n 
3  228  LEU n 
3  229  PRO n 
3  230  HIS n 
3  231  ILE n 
3  232  ASN n 
3  233  GLN n 
3  234  ALA n 
3  235  VAL n 
3  236  ARG n 
3  237  THR n 
3  238  TYR n 
3  239  LEU n 
3  240  LYS n 
3  241  ASN n 
3  242  ALA n 
3  243  CYS n 
3  244  ARG n 
3  245  ILE n 
3  246  ILE n 
3  247  ILE n 
3  248  GLY n 
3  249  ARG n 
3  250  ILE n 
3  251  GLN n 
3  252  SER n 
3  253  ILE n 
3  254  GLN n 
3  255  LYS n 
3  256  ILE n 
3  257  TYR n 
3  258  GLU n 
3  259  ASN n 
3  260  PHE n 
3  261  GLU n 
3  262  GLU n 
3  263  PRO n 
3  264  GLN n 
3  265  PRO n 
3  266  GLU n 
3  267  LEU n 
3  268  VAL n 
3  269  LEU n 
3  270  PHE n 
3  271  SER n 
3  272  MET n 
3  273  ASP n 
3  274  GLU n 
3  275  GLU n 
3  276  LYS n 
3  277  THR n 
3  278  LYS n 
3  279  ALA n 
3  280  ILE n 
3  281  ILE n 
3  282  THR n 
3  283  ILE n 
3  284  LYS n 
3  285  ASP n 
3  286  GLU n 
3  287  THR n 
3  288  HIS n 
3  289  THR n 
3  290  ILE n 
3  291  GLY n 
3  292  ASN n 
3  293  LEU n 
3  294  LEU n 
3  295  LYS n 
3  296  THR n 
3  297  TYR n 
3  298  ILE n 
3  299  TYR n 
3  300  GLU n 
3  301  MET n 
3  302  ILE n 
3  303  PRO n 
3  304  ASP n 
3  305  ILE n 
3  306  SER n 
3  307  PHE n 
3  308  VAL n 
3  309  GLY n 
3  310  TYR n 
3  311  GLN n 
3  312  CYS n 
3  313  VAL n 
3  314  PRO n 
3  315  HIS n 
3  316  LYS n 
3  317  GLN n 
3  318  GLU n 
3  319  MET n 
3  320  VAL n 
3  321  LEU n 
3  322  THR n 
3  323  ILE n 
3  324  ILE n 
3  325  HIS n 
3  326  LYS n 
3  327  ALA n 
3  328  SER n 
3  329  GLN n 
3  330  GLU n 
3  331  ASP n 
3  332  LEU n 
3  333  ILE n 
3  334  THR n 
3  335  LEU n 
3  336  LEU n 
3  337  GLU n 
3  338  LYS n 
3  339  SER n 
3  340  ILE n 
3  341  GLN n 
3  342  ASN n 
3  343  ILE n 
3  344  ILE n 
3  345  GLN n 
3  346  THR n 
3  347  PHE n 
3  348  GLN n 
3  349  ILE n 
3  350  LEU n 
3  351  GLU n 
3  352  LYS n 
3  353  ASN n 
3  354  VAL n 
3  355  ASP n 
3  356  GLU n 
3  357  LEU n 
3  358  ILE n 
3  359  ALA n 
4  1    MET n 
4  2    ALA n 
4  3    MET n 
4  4    GLN n 
4  5    LYS n 
4  6    LEU n 
4  7    PHE n 
4  8    THR n 
4  9    TYR n 
4  10   ILE n 
4  11   TYR n 
4  12   GLU n 
4  13   PHE n 
4  14   ILE n 
4  15   GLU n 
4  16   TYR n 
4  17   ARG n 
4  18   LYS n 
4  19   MET n 
4  20   VAL n 
4  21   LEU n 
4  22   LEU n 
4  23   GLU n 
4  24   GLU n 
4  25   LYS n 
4  26   VAL n 
4  27   PRO n 
4  28   TYR n 
4  29   ASP n 
4  30   LYS n 
4  31   PHE n 
4  32   VAL n 
4  33   GLN n 
4  34   MET n 
4  35   VAL n 
4  36   LEU n 
4  37   ASN n 
4  38   THR n 
4  39   GLY n 
4  40   PHE n 
4  41   PHE n 
4  42   ARG n 
4  43   ILE n 
4  44   ASN n 
4  45   ALA n 
4  46   GLU n 
4  47   THR n 
4  48   LEU n 
4  49   ASN n 
4  50   HIS n 
4  51   GLY n 
4  52   ILE n 
4  53   VAL n 
4  54   SER n 
4  55   VAL n 
4  56   PHE n 
4  57   ILE n 
4  58   PHE n 
4  59   GLY n 
4  60   ALA n 
4  61   ASN n 
4  62   GLY n 
4  63   LYS n 
4  64   TYR n 
4  65   VAL n 
4  66   HIS n 
4  67   HIS n 
4  68   GLY n 
4  69   GLY n 
4  70   ASP n 
4  71   MET n 
4  72   ARG n 
4  73   THR n 
4  74   LEU n 
4  75   LEU n 
4  76   THR n 
4  77   ASN n 
4  78   THR n 
4  79   LEU n 
4  80   ASN n 
4  81   GLU n 
4  82   LYS n 
4  83   LYS n 
4  84   HIS n 
4  85   TYR n 
4  86   GLU n 
4  87   GLU n 
4  88   LEU n 
4  89   ILE n 
4  90   LEU n 
4  91   ILE n 
4  92   VAL n 
4  93   ASP n 
4  94   LYS n 
4  95   PRO n 
4  96   VAL n 
4  97   LEU n 
4  98   SER n 
4  99   LYS n 
4  100  LYS n 
4  101  ASN n 
4  102  ILE n 
4  103  LEU n 
4  104  ASP n 
4  105  ILE n 
4  106  ILE n 
4  107  VAL n 
4  108  GLU n 
4  109  GLN n 
4  110  ARG n 
4  111  ALA n 
4  112  ALA n 
4  113  ASN n 
4  114  PRO n 
4  115  THR n 
4  116  ILE n 
4  117  VAL n 
4  118  ILE n 
4  119  ASN n 
4  120  ILE n 
4  121  TYR n 
4  122  PRO n 
4  123  TYR n 
4  124  HIS n 
4  125  LEU n 
4  126  PHE n 
4  127  CYS n 
4  128  ILE n 
4  129  ASN n 
4  130  ILE n 
4  131  PRO n 
4  132  LYS n 
4  133  VAL n 
4  134  SER n 
4  135  ALA n 
4  136  ILE n 
4  137  PRO n 
4  138  LYS n 
4  139  HIS n 
4  140  LYS n 
4  141  LEU n 
4  142  ILE n 
4  143  THR n 
4  144  GLN n 
4  145  GLU n 
4  146  GLU n 
4  147  ALA n 
4  148  GLN n 
4  149  GLU n 
4  150  PHE n 
4  151  LEU n 
4  152  GLY n 
4  153  ARG n 
4  154  GLU n 
4  155  TYR n 
4  156  LEU n 
4  157  GLN n 
4  158  PRO n 
4  159  GLN n 
4  160  ASP n 
4  161  LEU n 
4  162  MET n 
4  163  GLN n 
4  164  ILE n 
4  165  SER n 
4  166  ALA n 
4  167  SER n 
4  168  ASP n 
4  169  PRO n 
4  170  PRO n 
4  171  VAL n 
4  172  VAL n 
4  173  TRP n 
4  174  LEU n 
4  175  GLY n 
4  176  GLY n 
4  177  ARG n 
4  178  PRO n 
4  179  GLY n 
4  180  ASP n 
4  181  PHE n 
4  182  VAL n 
4  183  GLN n 
4  184  ILE n 
4  185  GLU n 
4  186  ARG n 
4  187  PRO n 
4  188  SER n 
4  189  GLU n 
4  190  THR n 
4  191  ALA n 
4  192  MET n 
4  193  HIS n 
4  194  ALA n 
4  195  VAL n 
4  196  VAL n 
4  197  ILE n 
4  198  ARG n 
4  199  PHE n 
4  200  ILE n 
4  201  THR n 
4  202  LYS n 
4  203  SER n 
4  204  LYS n 
4  205  ILE n 
5  1    MET n 
5  2    ALA n 
5  3    ASP n 
5  4    ASN n 
5  5    ASP n 
5  6    ASN n 
5  7    GLU n 
5  8    ASP n 
5  9    LEU n 
5  10   ILE n 
5  11   MET n 
5  12   ASP n 
5  13   ASP n 
5  14   LEU n 
5  15   VAL n 
5  16   GLU n 
5  17   GLU n 
5  18   TYR n 
5  19   VAL n 
5  20   GLU n 
5  21   THR n 
5  22   GLU n 
5  23   GLU n 
5  24   GLU n 
5  25   ASN n 
5  26   LEU n 
5  27   VAL n 
5  28   ASP n 
5  29   SER n 
5  30   GLU n 
5  31   GLU n 
5  32   GLU n 
5  33   SER n 
5  34   GLU n 
5  35   ASP n 
5  36   LYS n 
5  37   ASP n 
5  38   GLU n 
5  39   ILE n 
5  40   VAL n 
5  41   GLU n 
5  42   SER n 
5  43   PRO n 
5  44   SER n 
5  45   ILE n 
5  46   CYS n 
5  47   GLU n 
5  48   GLY n 
5  49   PHE n 
5  50   VAL n 
5  51   GLN n 
5  52   ALA n 
5  53   SER n 
5  54   SER n 
5  55   GLN n 
5  56   THR n 
5  57   LEU n 
5  58   VAL n 
5  59   ILE n 
5  60   ILE n 
5  61   PRO n 
5  62   ASP n 
5  63   ASN n 
5  64   GLU n 
5  65   ARG n 
5  66   ILE n 
5  67   THR n 
5  68   SER n 
5  69   ASN n 
5  70   VAL n 
5  71   LEU n 
5  72   THR n 
5  73   THR n 
5  74   PHE n 
5  75   GLU n 
5  76   ALA n 
5  77   THR n 
5  78   ARG n 
5  79   LEU n 
5  80   VAL n 
5  81   ALA n 
5  82   VAL n 
5  83   ARG n 
5  84   ALA n 
5  85   GLN n 
5  86   GLN n 
5  87   LEU n 
5  88   ALA n 
5  89   ILE n 
5  90   ASN n 
5  91   GLY n 
5  92   SER n 
5  93   THR n 
5  94   MET n 
5  95   LEU n 
5  96   LYS n 
5  97   LYS n 
5  98   LYS n 
5  99   TYR n 
5  100  SER n 
5  101  SER n 
5  102  PRO n 
5  103  ILE n 
5  104  ASP n 
5  105  ILE n 
5  106  ALA n 
5  107  LYS n 
5  108  GLN n 
5  109  GLU n 
5  110  LEU n 
5  111  PHE n 
5  112  ASN n 
5  113  ARG n 
5  114  LYS n 
5  115  ILE n 
5  116  PRO n 
5  117  LEU n 
5  118  LEU n 
5  119  VAL n 
5  120  MET n 
5  121  ARG n 
5  122  CYS n 
5  123  ILE n 
5  124  LYS n 
5  125  VAL n 
5  126  THR n 
5  127  PRO n 
5  128  GLU n 
5  129  GLY n 
5  130  GLN n 
5  131  LYS n 
5  132  ILE n 
5  133  VAL n 
5  134  GLU n 
5  135  ILE n 
5  136  TRP n 
5  137  ASN n 
5  138  PRO n 
5  139  ARG n 
5  140  GLU n 
5  141  MET n 
5  142  GLY n 
5  143  ILE n 
5  144  PRO n 
5  145  LEU n 
5  146  LEU n 
5  147  ASP n 
6  1    MET n 
6  2    ILE n 
6  3    ASP n 
6  4    GLN n 
6  5    LYS n 
6  6    ILE n 
6  7    PHE n 
6  8    GLU n 
6  9    THR n 
6  10   THR n 
6  11   LEU n 
6  12   ASN n 
6  13   ILE n 
6  14   ASP n 
6  15   ASP n 
6  16   PRO n 
6  17   THR n 
6  18   ASN n 
6  19   PHE n 
6  20   CYS n 
6  21   THR n 
6  22   ASN n 
6  23   VAL n 
6  24   GLU n 
6  25   ALA n 
6  26   HIS n 
6  27   LEU n 
6  28   LEU n 
6  29   LYS n 
6  30   GLU n 
6  31   LEU n 
6  32   GLU n 
6  33   ASN n 
6  34   ILE n 
6  35   TYR n 
6  36   VAL n 
6  37   GLY n 
6  38   LYS n 
6  39   CYS n 
6  40   PHE n 
6  41   LYS n 
6  42   ASN n 
6  43   SER n 
6  44   PHE n 
6  45   ILE n 
6  46   LEU n 
6  47   ASN n 
6  48   ILE n 
6  49   THR n 
6  50   GLY n 
6  51   VAL n 
6  52   ILE n 
6  53   GLN n 
6  54   ARG n 
6  55   SER n 
6  56   PRO n 
6  57   CYS n 
6  58   PHE n 
6  59   ILE n 
6  60   MET n 
6  61   ARG n 
6  62   THR n 
6  63   ASN n 
6  64   ASN n 
6  65   SER n 
6  66   GLY n 
6  67   ARG n 
6  68   GLY n 
6  69   TYR n 
6  70   MET n 
6  71   HIS n 
6  72   VAL n 
6  73   ARG n 
6  74   PHE n 
6  75   SER n 
6  76   ALA n 
6  77   VAL n 
6  78   VAL n 
6  79   SER n 
6  80   TYR n 
6  81   LEU n 
6  82   ASN n 
6  83   ALA n 
6  84   PHE n 
6  85   ASP n 
6  86   LEU n 
6  87   ILE n 
6  88   ALA n 
6  89   ALA n 
6  90   VAL n 
6  91   LYS n 
6  92   ILE n 
6  93   ILE n 
6  94   LYS n 
6  95   ASN n 
6  96   ASP n 
6  97   SER n 
6  98   ASN n 
6  99   ILE n 
6  100  ILE n 
6  101  LEU n 
6  102  GLY n 
6  103  GLU n 
6  104  SER n 
6  105  LEU n 
6  106  LEU n 
6  107  THR n 
6  108  GLU n 
6  109  PRO n 
6  110  VAL n 
6  111  THR n 
6  112  ILE n 
6  113  VAL n 
6  114  ILE n 
6  115  PRO n 
6  116  SER n 
6  117  SER n 
6  118  GLU n 
6  119  SER n 
6  120  GLN n 
6  121  ASN n 
6  122  ASN n 
6  123  VAL n 
6  124  ALA n 
6  125  GLU n 
6  126  VAL n 
6  127  GLY n 
6  128  GLN n 
6  129  ILE n 
6  130  VAL n 
6  131  PRO n 
6  132  VAL n 
6  133  GLN n 
6  134  LEU n 
6  135  ALA n 
6  136  ASN n 
6  137  SER n 
6  138  SER n 
6  139  VAL n 
6  140  TYR n 
6  141  TYR n 
6  142  ILE n 
6  143  PRO n 
6  144  GLY n 
6  145  ARG n 
6  146  GLN n 
6  147  GLN n 
6  148  ALA n 
6  149  SER n 
6  150  ALA n 
6  151  THR n 
6  152  GLY n 
6  153  SER n 
6  154  ILE n 
6  155  PHE n 
6  156  ILE n 
6  157  PRO n 
6  158  LYS n 
6  159  HIS n 
6  160  THR n 
6  161  PHE n 
6  162  SER n 
6  163  VAL n 
6  164  TYR n 
6  165  HIS n 
6  166  VAL n 
6  167  GLN n 
6  168  GLU n 
6  169  GLU n 
6  170  LEU n 
6  171  THR n 
6  172  GLN n 
6  173  GLU n 
6  174  GLN n 
6  175  ALA n 
6  176  LEU n 
6  177  ASN n 
6  178  LEU n 
6  179  THR n 
6  180  LYS n 
6  181  LEU n 
6  182  VAL n 
6  183  ASN n 
6  184  ILE n 
6  185  ILE n 
6  186  GLU n 
6  187  MET n 
6  188  LEU n 
6  189  LEU n 
6  190  GLU n 
6  191  SER n 
6  192  ARG n 
6  193  SER n 
6  194  LYS n 
6  195  LYS n 
6  196  ASP n 
6  197  PHE n 
6  198  LYS n 
6  199  GLN n 
6  200  ILE n 
6  201  CYS n 
6  202  PHE n 
6  203  PHE n 
6  204  GLU n 
6  205  LYS n 
6  206  LEU n 
6  207  TYR n 
6  208  TYR n 
6  209  THR n 
6  210  TYR n 
6  211  SER n 
6  212  ILE n 
6  213  SER n 
6  214  SER n 
6  215  ASP n 
6  216  GLU n 
6  217  ILE n 
6  218  LEU n 
6  219  ASP n 
6  220  LEU n 
6  221  LYS n 
6  222  ILE n 
6  223  TRP n 
6  224  LYS n 
6  225  GLY n 
6  226  PRO n 
6  227  LYS n 
6  228  GLY n 
6  229  LYS n 
6  230  GLU n 
6  231  MET n 
6  232  SER n 
6  233  ARG n 
6  234  LEU n 
6  235  LYS n 
6  236  PRO n 
6  237  CYS n 
6  238  ASN n 
6  239  VAL n 
6  240  LEU n 
6  241  SER n 
6  242  PHE n 
6  243  LEU n 
6  244  TYR n 
6  245  ASP n 
6  246  ALA n 
6  247  LEU n 
6  248  LYS n 
6  249  ASN n 
6  250  LYS n 
6  251  ASN n 
6  252  SER n 
6  253  SER n 
6  254  LEU n 
6  255  GLY n 
6  256  PHE n 
6  257  TRP n 
6  258  ALA n 
6  259  ARG n 
6  260  PRO n 
6  261  PRO n 
6  262  ASN n 
6  263  LEU n 
6  264  LEU n 
6  265  LYS n 
6  266  SER n 
6  267  SER n 
6  268  PRO n 
6  269  LEU n 
6  270  ALA n 
6  271  TYR n 
6  272  GLN n 
6  273  GLN n 
6  274  ASP n 
6  275  GLN n 
6  276  ASN n 
6  277  SER n 
6  278  PHE n 
6  279  ASN n 
6  280  ALA n 
6  281  THR n 
6  282  GLU n 
6  283  LEU n 
6  284  PRO n 
6  285  ILE n 
6  286  ILE n 
6  287  CYS n 
6  288  SER n 
6  289  ALA n 
6  290  GLU n 
6  291  VAL n 
6  292  MET n 
6  293  PHE n 
6  294  VAL n 
6  295  THR n 
6  296  LEU n 
6  297  LEU n 
6  298  LYS n 
6  299  GLU n 
6  300  ILE n 
6  301  ILE n 
6  302  ASN n 
6  303  TYR n 
6  304  LEU n 
6  305  GLN n 
6  306  PHE n 
6  307  ILE n 
6  308  ASN n 
6  309  ASP n 
6  310  LEU n 
6  311  CYS n 
6  312  ASP n 
6  313  THR n 
6  314  PHE n 
6  315  ASN n 
6  316  ASN n 
6  317  GLU n 
6  318  GLN n 
6  319  LEU n 
6  320  ILE n 
6  321  LYS n 
6  322  ARG n 
6  323  HIS n 
6  324  GLU n 
6  325  ASN n 
6  326  ILE n 
6  327  TRP n 
6  328  MET n 
6  329  LEU n 
6  330  ILE n 
6  331  GLU n 
6  332  GLN n 
6  333  ARG n 
6  334  LYS n 
6  335  ILE n 
6  336  GLY n 
6  337  HIS n 
6  338  ASP n 
6  339  PHE n 
7  1    MET n 
7  2    LYS n 
7  3    ILE n 
7  4    CYS n 
7  5    LYS n 
7  6    ALA n 
7  7    CYS n 
7  8    SER n 
7  9    SER n 
7  10   CYS n 
7  11   MET n 
7  12   VAL n 
7  13   ARG n 
7  14   THR n 
7  15   TYR n 
7  16   VAL n 
7  17   ASP n 
7  18   GLY n 
7  19   ASN n 
7  20   ILE n 
7  21   ILE n 
7  22   PHE n 
7  23   ARG n 
7  24   CYS n 
7  25   SER n 
7  26   CYS n 
7  27   GLY n 
7  28   GLU n 
7  29   SER n 
7  30   VAL n 
7  31   GLN n 
7  32   GLY n 
7  33   ASP n 
7  34   SER n 
7  35   GLN n 
7  36   ASN n 
7  37   LEU n 
7  38   LEU n 
7  39   VAL n 
7  40   SER n 
7  41   SER n 
7  42   LYS n 
7  43   VAL n 
7  44   TYR n 
7  45   HIS n 
7  46   THR n 
7  47   GLY n 
7  48   GLU n 
7  49   MET n 
7  50   GLU n 
7  51   ASP n 
7  52   LYS n 
7  53   TYR n 
7  54   LYS n 
7  55   ILE n 
7  56   PHE n 
7  57   ILE n 
7  58   LYS n 
7  59   ASN n 
7  60   ALA n 
7  61   PRO n 
7  62   PHE n 
7  63   ASP n 
7  64   PRO n 
7  65   THR n 
7  66   ASN n 
7  67   CYS n 
7  68   GLN n 
7  69   ILE n 
7  70   LYS n 
7  71   LYS n 
7  72   ASP n 
7  73   CYS n 
7  74   PRO n 
7  75   ASN n 
7  76   CYS n 
7  77   HIS n 
7  78   LEU n 
7  79   ASP n 
7  80   TYR n 
7  81   LEU n 
7  82   THR n 
7  83   GLN n 
7  84   ILE n 
7  85   CYS n 
7  86   ILE n 
7  87   GLY n 
7  88   SER n 
7  89   GLN n 
7  90   LYS n 
7  91   ILE n 
7  92   ILE n 
7  93   ILE n 
7  94   LEU n 
7  95   VAL n 
7  96   CYS n 
7  97   ARG n 
7  98   CYS n 
7  99   GLY n 
7  100  TYR n 
7  101  MET n 
7  102  SER n 
7  103  ASN n 
7  104  ARG n 
7  105  GLY n 
8  1    MET n 
8  2    LEU n 
8  3    ILE n 
8  4    PRO n 
8  5    VAL n 
8  6    VAL n 
8  7    CYS n 
8  8    PHE n 
8  9    THR n 
8  10   CYS n 
8  11   GLY n 
8  12   PHE n 
8  13   PRO n 
8  14   ILE n 
8  15   GLY n 
8  16   THR n 
8  17   TYR n 
8  18   ALA n 
8  19   ALA n 
8  20   ILE n 
8  21   PHE n 
8  22   ASP n 
8  23   LYS n 
8  24   ALA n 
8  25   ARG n 
8  26   THR n 
8  27   GLU n 
8  28   TYR n 
8  29   ILE n 
8  30   LYS n 
8  31   THR n 
8  32   LYS n 
8  33   MET n 
8  34   GLY n 
8  35   GLY n 
8  36   THR n 
8  37   LEU n 
8  38   PRO n 
8  39   GLN n 
8  40   ASN n 
8  41   ILE n 
8  42   PRO n 
8  43   LEU n 
8  44   ASP n 
8  45   ALA n 
8  46   SER n 
8  47   LEU n 
8  48   GLN n 
8  49   ILE n 
8  50   GLU n 
8  51   LEU n 
8  52   LYS n 
8  53   ASP n 
8  54   LEU n 
8  55   ILE n 
8  56   THR n 
8  57   ALA n 
8  58   LEU n 
8  59   GLY n 
8  60   ILE n 
8  61   PRO n 
8  62   MET n 
8  63   ARG n 
8  64   VAL n 
8  65   CYS n 
8  66   CYS n 
8  67   ARG n 
8  68   THR n 
8  69   HIS n 
8  70   LEU n 
8  71   ILE n 
8  72   THR n 
8  73   THR n 
8  74   LEU n 
8  75   ASP n 
8  76   TYR n 
8  77   ARG n 
8  78   LYS n 
8  79   TYR n 
8  80   TYR n 
9  1    DG  n 
9  2    DC  n 
9  3    DC  n 
9  4    DG  n 
9  5    DA  n 
9  6    DG  n 
9  7    DC  n 
9  8    DA  n 
10 1    DT  n 
10 2    DC  n 
10 3    DG  n 
10 4    DG  n 
10 5    DC  n 
10 6    DT  n 
10 7    DC  n 
# 
loop_
_entity_src_nat.entity_id 
_entity_src_nat.pdbx_src_id 
_entity_src_nat.pdbx_alt_source_flag 
_entity_src_nat.pdbx_beg_seq_num 
_entity_src_nat.pdbx_end_seq_num 
_entity_src_nat.common_name 
_entity_src_nat.pdbx_organism_scientific 
_entity_src_nat.pdbx_ncbi_taxonomy_id 
_entity_src_nat.genus 
_entity_src_nat.species 
_entity_src_nat.strain 
_entity_src_nat.tissue 
_entity_src_nat.tissue_fraction 
_entity_src_nat.pdbx_secretion 
_entity_src_nat.pdbx_fragment 
_entity_src_nat.pdbx_variant 
_entity_src_nat.pdbx_cell_line 
_entity_src_nat.pdbx_atcc 
_entity_src_nat.pdbx_cellular_location 
_entity_src_nat.pdbx_organ 
_entity_src_nat.pdbx_organelle 
_entity_src_nat.pdbx_cell 
_entity_src_nat.pdbx_plasmid_name 
_entity_src_nat.pdbx_plasmid_details 
_entity_src_nat.details 
1  1 sample 1 1450 ? 'African swine fever virus' 10497 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2  1 sample 1 1242 ? 'African swine fever virus' 10497 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3  1 sample 1 359  ? 'African swine fever virus' 10497 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4  1 sample 1 205  ? 'African swine fever virus' 10497 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
5  1 sample 1 147  ? 'African swine fever virus' 10497 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
6  1 sample 1 339  ? 'African swine fever virus' 10497 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
7  1 sample 1 105  ? 'African swine fever virus' 10497 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
8  1 sample 1 80   ? 'African swine fever virus' 10497 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
9  1 sample 1 8    ? 'African swine fever virus' 10497 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
10 1 sample 1 7    ? 'African swine fever virus' 10497 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
ALA 'L-peptide linking' y ALANINE                              ? 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                             ? 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                           ? 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                      ? 'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE                             ? 'C3 H7 N O2 S'    121.158 
DA  'DNA linking'       y "2'-DEOXYADENOSINE-5'-MONOPHOSPHATE" ? 'C10 H14 N5 O6 P' 331.222 
DC  'DNA linking'       y "2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE"  ? 'C9 H14 N3 O7 P'  307.197 
DG  'DNA linking'       y "2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE" ? 'C10 H14 N5 O7 P' 347.221 
DT  'DNA linking'       y "THYMIDINE-5'-MONOPHOSPHATE"         ? 'C10 H15 N2 O8 P' 322.208 
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 
ZN  non-polymer         . 'ZINC ION'                           ? 'Zn 2'            65.409  
# 
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    GLU 2    2    2    GLU GLU A . n 
A 1  3    ALA 3    3    3    ALA ALA A . n 
A 1  4    GLY 4    4    4    GLY GLY A . n 
A 1  5    TYR 5    5    5    TYR TYR A . n 
A 1  6    ALA 6    6    6    ALA ALA A . n 
A 1  7    GLU 7    7    7    GLU GLU A . n 
A 1  8    ILE 8    8    8    ILE ILE A . n 
A 1  9    ALA 9    9    9    ALA ALA A . n 
A 1  10   ALA 10   10   10   ALA ALA A . n 
A 1  11   VAL 11   11   11   VAL VAL A . n 
A 1  12   GLN 12   12   12   GLN GLN A . n 
A 1  13   PHE 13   13   13   PHE PHE A . n 
A 1  14   ASN 14   14   14   ASN ASN A . n 
A 1  15   ILE 15   15   15   ILE ILE A . n 
A 1  16   ALA 16   16   16   ALA ALA A . n 
A 1  17   GLY 17   17   17   GLY GLY A . n 
A 1  18   ASP 18   18   18   ASP ASP A . n 
A 1  19   ASN 19   19   19   ASN ASN A . n 
A 1  20   ASP 20   20   20   ASP ASP A . n 
A 1  21   HIS 21   21   21   HIS HIS A . n 
A 1  22   LYS 22   22   22   LYS LYS A . n 
A 1  23   ARG 23   23   23   ARG ARG A . n 
A 1  24   GLN 24   24   24   GLN GLN A . n 
A 1  25   GLY 25   25   25   GLY GLY A . n 
A 1  26   VAL 26   26   26   VAL VAL A . n 
A 1  27   MET 27   27   27   MET MET A . n 
A 1  28   GLU 28   28   28   GLU GLU A . n 
A 1  29   VAL 29   29   29   VAL VAL A . n 
A 1  30   THR 30   30   30   THR THR A . n 
A 1  31   ILE 31   31   31   ILE ILE A . n 
A 1  32   SER 32   32   32   SER SER A . n 
A 1  33   ASN 33   33   33   ASN ASN A . n 
A 1  34   LEU 34   34   34   LEU LEU A . n 
A 1  35   PHE 35   35   35   PHE PHE A . n 
A 1  36   GLU 36   36   36   GLU GLU A . n 
A 1  37   GLY 37   37   37   GLY GLY A . n 
A 1  38   THR 38   38   38   THR THR A . n 
A 1  39   LEU 39   39   39   LEU LEU A . n 
A 1  40   PRO 40   40   40   PRO PRO A . n 
A 1  41   ALA 41   41   41   ALA ALA A . n 
A 1  42   GLU 42   42   42   GLU GLU A . n 
A 1  43   GLY 43   43   43   GLY GLY A . n 
A 1  44   GLY 44   44   44   GLY GLY A . n 
A 1  45   ILE 45   45   45   ILE ILE A . n 
A 1  46   TYR 46   46   46   TYR TYR A . n 
A 1  47   ASP 47   47   47   ASP ASP A . n 
A 1  48   ALA 48   48   48   ALA ALA A . n 
A 1  49   ARG 49   49   49   ARG ARG A . n 
A 1  50   MET 50   50   50   MET MET A . n 
A 1  51   GLY 51   51   51   GLY GLY A . n 
A 1  52   THR 52   52   52   THR THR A . n 
A 1  53   THR 53   53   53   THR THR A . n 
A 1  54   ASP 54   54   54   ASP ASP A . n 
A 1  55   HIS 55   55   55   HIS HIS A . n 
A 1  56   HIS 56   56   56   HIS HIS A . n 
A 1  57   TYR 57   57   57   TYR TYR A . n 
A 1  58   LYS 58   58   58   LYS LYS A . n 
A 1  59   CYS 59   59   59   CYS CYS A . n 
A 1  60   ILE 60   60   60   ILE ILE A . n 
A 1  61   THR 61   61   61   THR THR A . n 
A 1  62   CYS 62   62   62   CYS CYS A . n 
A 1  63   SER 63   63   63   SER SER A . n 
A 1  64   HIS 64   64   64   HIS HIS A . n 
A 1  65   GLN 65   65   65   GLN GLN A . n 
A 1  66   ARG 66   66   66   ARG ARG A . n 
A 1  67   LYS 67   67   67   LYS LYS A . n 
A 1  68   GLN 68   68   68   GLN GLN A . n 
A 1  69   CYS 69   69   69   CYS CYS A . n 
A 1  70   MET 70   70   70   MET MET A . n 
A 1  71   GLY 71   71   71   GLY GLY A . n 
A 1  72   HIS 72   72   72   HIS HIS A . n 
A 1  73   PRO 73   73   73   PRO PRO A . n 
A 1  74   GLY 74   74   74   GLY GLY A . n 
A 1  75   ILE 75   75   75   ILE ILE A . n 
A 1  76   LEU 76   76   76   LEU LEU A . n 
A 1  77   GLN 77   77   77   GLN GLN A . n 
A 1  78   MET 78   78   78   MET MET A . n 
A 1  79   HIS 79   79   79   HIS HIS A . n 
A 1  80   ALA 80   80   80   ALA ALA A . n 
A 1  81   PRO 81   81   81   PRO PRO A . n 
A 1  82   VAL 82   82   82   VAL VAL A . n 
A 1  83   LEU 83   83   83   LEU LEU A . n 
A 1  84   GLN 84   84   84   GLN GLN A . n 
A 1  85   PRO 85   85   85   PRO PRO A . n 
A 1  86   LEU 86   86   86   LEU LEU A . n 
A 1  87   PHE 87   87   87   PHE PHE A . n 
A 1  88   ILE 88   88   88   ILE ILE A . n 
A 1  89   ALA 89   89   89   ALA ALA A . n 
A 1  90   GLU 90   90   90   GLU GLU A . n 
A 1  91   ILE 91   91   91   ILE ILE A . n 
A 1  92   ARG 92   92   92   ARG ARG A . n 
A 1  93   ARG 93   93   93   ARG ARG A . n 
A 1  94   TRP 94   94   94   TRP TRP A . n 
A 1  95   LEU 95   95   95   LEU LEU A . n 
A 1  96   ARG 96   96   96   ARG ARG A . n 
A 1  97   VAL 97   97   97   VAL VAL A . n 
A 1  98   ILE 98   98   98   ILE ILE A . n 
A 1  99   CYS 99   99   99   CYS CYS A . n 
A 1  100  LEU 100  100  100  LEU LEU A . n 
A 1  101  ASN 101  101  101  ASN ASN A . n 
A 1  102  CYS 102  102  102  CYS CYS A . n 
A 1  103  GLY 103  103  103  GLY GLY A . n 
A 1  104  ALA 104  104  104  ALA ALA A . n 
A 1  105  PRO 105  105  105  PRO PRO A . n 
A 1  106  ILE 106  106  106  ILE ILE A . n 
A 1  107  VAL 107  107  107  VAL VAL A . n 
A 1  108  ASP 108  108  108  ASP ASP A . n 
A 1  109  LEU 109  109  109  LEU LEU A . n 
A 1  110  LYS 110  110  110  LYS LYS A . n 
A 1  111  ARG 111  111  111  ARG ARG A . n 
A 1  112  TYR 112  112  112  TYR TYR A . n 
A 1  113  GLU 113  113  113  GLU GLU A . n 
A 1  114  HIS 114  114  114  HIS HIS A . n 
A 1  115  LEU 115  115  115  LEU LEU A . n 
A 1  116  ILE 116  116  116  ILE ILE A . n 
A 1  117  ARG 117  117  117  ARG ARG A . n 
A 1  118  PRO 118  118  118  PRO PRO A . n 
A 1  119  LYS 119  119  119  LYS LYS A . n 
A 1  120  ARG 120  120  120  ARG ARG A . n 
A 1  121  LEU 121  121  121  LEU LEU A . n 
A 1  122  ILE 122  122  122  ILE ILE A . n 
A 1  123  GLU 123  123  123  GLU GLU A . n 
A 1  124  ALA 124  124  124  ALA ALA A . n 
A 1  125  ALA 125  125  125  ALA ALA A . n 
A 1  126  SER 126  126  126  SER SER A . n 
A 1  127  SER 127  127  127  SER SER A . n 
A 1  128  GLN 128  128  128  GLN GLN A . n 
A 1  129  THR 129  129  129  THR THR A . n 
A 1  130  GLU 130  130  130  GLU GLU A . n 
A 1  131  GLY 131  131  131  GLY GLY A . n 
A 1  132  LYS 132  132  132  LYS LYS A . n 
A 1  133  GLN 133  133  133  GLN GLN A . n 
A 1  134  CYS 134  134  134  CYS CYS A . n 
A 1  135  TYR 135  135  135  TYR TYR A . n 
A 1  136  VAL 136  136  136  VAL VAL A . n 
A 1  137  CYS 137  137  137  CYS CYS A . n 
A 1  138  LYS 138  138  138  LYS LYS A . n 
A 1  139  ALA 139  139  139  ALA ALA A . n 
A 1  140  VAL 140  140  140  VAL VAL A . n 
A 1  141  HIS 141  141  141  HIS HIS A . n 
A 1  142  PRO 142  142  142  PRO PRO A . n 
A 1  143  LYS 143  143  143  LYS LYS A . n 
A 1  144  ILE 144  144  144  ILE ILE A . n 
A 1  145  VAL 145  145  145  VAL VAL A . n 
A 1  146  LYS 146  146  146  LYS LYS A . n 
A 1  147  ASP 147  147  147  ASP ASP A . n 
A 1  148  SER 148  148  148  SER SER A . n 
A 1  149  GLU 149  149  149  GLU GLU A . n 
A 1  150  ASP 150  150  150  ASP ASP A . n 
A 1  151  TYR 151  151  151  TYR TYR A . n 
A 1  152  PHE 152  152  152  PHE PHE A . n 
A 1  153  THR 153  153  153  THR THR A . n 
A 1  154  PHE 154  154  154  PHE PHE A . n 
A 1  155  TRP 155  155  155  TRP TRP A . n 
A 1  156  ALA 156  156  156  ALA ALA A . n 
A 1  157  ASP 157  157  157  ASP ASP A . n 
A 1  158  GLN 158  158  158  GLN GLN A . n 
A 1  159  GLN 159  159  159  GLN GLN A . n 
A 1  160  GLY 160  160  160  GLY GLY A . n 
A 1  161  LYS 161  161  161  LYS LYS A . n 
A 1  162  ILE 162  162  162  ILE ILE A . n 
A 1  163  ASP 163  163  163  ASP ASP A . n 
A 1  164  LYS 164  164  164  LYS LYS A . n 
A 1  165  LEU 165  165  165  LEU LEU A . n 
A 1  166  TYR 166  166  166  TYR TYR A . n 
A 1  167  PRO 167  167  167  PRO PRO A . n 
A 1  168  GLN 168  168  168  GLN GLN A . n 
A 1  169  ILE 169  169  169  ILE ILE A . n 
A 1  170  ILE 170  170  170  ILE ILE A . n 
A 1  171  ARG 171  171  171  ARG ARG A . n 
A 1  172  GLU 172  172  172  GLU GLU A . n 
A 1  173  ILE 173  173  173  ILE ILE A . n 
A 1  174  PHE 174  174  174  PHE PHE A . n 
A 1  175  SER 175  175  175  SER SER A . n 
A 1  176  ARG 176  176  176  ARG ARG A . n 
A 1  177  VAL 177  177  177  VAL VAL A . n 
A 1  178  THR 178  178  178  THR THR A . n 
A 1  179  TYR 179  179  179  TYR TYR A . n 
A 1  180  ASP 180  180  180  ASP ASP A . n 
A 1  181  THR 181  181  181  THR THR A . n 
A 1  182  VAL 182  182  182  VAL VAL A . n 
A 1  183  VAL 183  183  183  VAL VAL A . n 
A 1  184  LYS 184  184  184  LYS LYS A . n 
A 1  185  LEU 185  185  185  LEU LEU A . n 
A 1  186  GLY 186  186  186  GLY GLY A . n 
A 1  187  ARG 187  187  187  ARG ARG A . n 
A 1  188  SER 188  188  188  SER SER A . n 
A 1  189  LYS 189  189  189  LYS LYS A . n 
A 1  190  ASN 190  190  190  ASN ASN A . n 
A 1  191  SER 191  191  191  SER SER A . n 
A 1  192  HIS 192  192  192  HIS HIS A . n 
A 1  193  PRO 193  193  193  PRO PRO A . n 
A 1  194  GLU 194  194  194  GLU GLU A . n 
A 1  195  LYS 195  195  195  LYS LYS A . n 
A 1  196  LEU 196  196  196  LEU LEU A . n 
A 1  197  VAL 197  197  197  VAL VAL A . n 
A 1  198  LEU 198  198  198  LEU LEU A . n 
A 1  199  LYS 199  199  199  LYS LYS A . n 
A 1  200  ALA 200  200  200  ALA ALA A . n 
A 1  201  ILE 201  201  201  ILE ILE A . n 
A 1  202  GLN 202  202  202  GLN GLN A . n 
A 1  203  ILE 203  203  203  ILE ILE A . n 
A 1  204  PRO 204  204  204  PRO PRO A . n 
A 1  205  PRO 205  205  205  PRO PRO A . n 
A 1  206  ILE 206  206  206  ILE ILE A . n 
A 1  207  SER 207  207  207  SER SER A . n 
A 1  208  ILE 208  208  208  ILE ILE A . n 
A 1  209  ARG 209  209  209  ARG ARG A . n 
A 1  210  PRO 210  210  210  PRO PRO A . n 
A 1  211  GLY 211  211  211  GLY GLY A . n 
A 1  212  ILE 212  212  212  ILE ILE A . n 
A 1  213  ARG 213  213  ?    ?   ?   A . n 
A 1  214  LEU 214  214  ?    ?   ?   A . n 
A 1  215  GLY 215  215  ?    ?   ?   A . n 
A 1  216  ILE 216  216  ?    ?   ?   A . n 
A 1  217  GLY 217  217  ?    ?   ?   A . n 
A 1  218  SER 218  218  ?    ?   ?   A . n 
A 1  219  GLY 219  219  ?    ?   ?   A . n 
A 1  220  PRO 220  220  ?    ?   ?   A . n 
A 1  221  GLN 221  221  ?    ?   ?   A . n 
A 1  222  SER 222  222  ?    ?   ?   A . n 
A 1  223  PHE 223  223  ?    ?   ?   A . n 
A 1  224  HIS 224  224  224  HIS HIS A . n 
A 1  225  ASP 225  225  225  ASP ASP A . n 
A 1  226  ILE 226  226  226  ILE ILE A . n 
A 1  227  ASN 227  227  227  ASN ASN A . n 
A 1  228  ASN 228  228  228  ASN ASN A . n 
A 1  229  VAL 229  229  229  VAL VAL A . n 
A 1  230  ILE 230  230  230  ILE ILE A . n 
A 1  231  GLN 231  231  231  GLN GLN A . n 
A 1  232  TYR 232  232  232  TYR TYR A . n 
A 1  233  LEU 233  233  233  LEU LEU A . n 
A 1  234  VAL 234  234  234  VAL VAL A . n 
A 1  235  ARG 235  235  235  ARG ARG A . n 
A 1  236  LYS 236  236  236  LYS LYS A . n 
A 1  237  ASN 237  237  237  ASN ASN A . n 
A 1  238  LEU 238  238  238  LEU LEU A . n 
A 1  239  LEU 239  239  239  LEU LEU A . n 
A 1  240  ILE 240  240  240  ILE ILE A . n 
A 1  241  PRO 241  241  241  PRO PRO A . n 
A 1  242  LYS 242  242  242  LYS LYS A . n 
A 1  243  ASP 243  243  243  ASP ASP A . n 
A 1  244  LEU 244  244  244  LEU LEU A . n 
A 1  245  GLN 245  245  245  GLN GLN A . n 
A 1  246  ILE 246  246  246  ILE ILE A . n 
A 1  247  VAL 247  247  247  VAL VAL A . n 
A 1  248  ARG 248  248  248  ARG ARG A . n 
A 1  249  GLY 249  249  249  GLY GLY A . n 
A 1  250  GLN 250  250  250  GLN GLN A . n 
A 1  251  LYS 251  251  251  LYS LYS A . n 
A 1  252  ILE 252  252  252  ILE ILE A . n 
A 1  253  PRO 253  253  253  PRO PRO A . n 
A 1  254  LEU 254  254  254  LEU LEU A . n 
A 1  255  ASN 255  255  255  ASN ASN A . n 
A 1  256  ILE 256  256  256  ILE ILE A . n 
A 1  257  ASP 257  257  257  ASP ASP A . n 
A 1  258  ARG 258  258  258  ARG ARG A . n 
A 1  259  ASN 259  259  259  ASN ASN A . n 
A 1  260  LEU 260  260  260  LEU LEU A . n 
A 1  261  GLN 261  261  261  GLN GLN A . n 
A 1  262  THR 262  262  262  THR THR A . n 
A 1  263  ILE 263  263  263  ILE ILE A . n 
A 1  264  GLN 264  264  264  GLN GLN A . n 
A 1  265  GLN 265  265  265  GLN GLN A . n 
A 1  266  LEU 266  266  266  LEU LEU A . n 
A 1  267  TYR 267  267  267  TYR TYR A . n 
A 1  268  TYR 268  268  268  TYR TYR A . n 
A 1  269  ASN 269  269  269  ASN ASN A . n 
A 1  270  PHE 270  270  270  PHE PHE A . n 
A 1  271  LEU 271  271  271  LEU LEU A . n 
A 1  272  LEU 272  272  272  LEU LEU A . n 
A 1  273  ASP 273  273  273  ASP ASP A . n 
A 1  274  SER 274  274  274  SER SER A . n 
A 1  275  VAL 275  275  275  VAL VAL A . n 
A 1  276  SER 276  276  ?    ?   ?   A . n 
A 1  277  THR 277  277  ?    ?   ?   A . n 
A 1  278  THR 278  278  ?    ?   ?   A . n 
A 1  279  ALA 279  279  ?    ?   ?   A . n 
A 1  280  THR 280  280  ?    ?   ?   A . n 
A 1  281  GLN 281  281  ?    ?   ?   A . n 
A 1  282  GLY 282  282  ?    ?   ?   A . n 
A 1  283  GLY 283  283  ?    ?   ?   A . n 
A 1  284  THR 284  284  ?    ?   ?   A . n 
A 1  285  GLY 285  285  ?    ?   ?   A . n 
A 1  286  LYS 286  286  ?    ?   ?   A . n 
A 1  287  ARG 287  287  ?    ?   ?   A . n 
A 1  288  GLY 288  288  ?    ?   ?   A . n 
A 1  289  ILE 289  289  ?    ?   ?   A . n 
A 1  290  VAL 290  290  ?    ?   ?   A . n 
A 1  291  MET 291  291  ?    ?   ?   A . n 
A 1  292  GLY 292  292  ?    ?   ?   A . n 
A 1  293  ALA 293  293  ?    ?   ?   A . n 
A 1  294  ARG 294  294  ?    ?   ?   A . n 
A 1  295  PRO 295  295  ?    ?   ?   A . n 
A 1  296  ALA 296  296  ?    ?   ?   A . n 
A 1  297  PRO 297  297  297  PRO PRO A . n 
A 1  298  SER 298  298  298  SER SER A . n 
A 1  299  ILE 299  299  299  ILE ILE A . n 
A 1  300  MET 300  300  300  MET MET A . n 
A 1  301  ARG 301  301  301  ARG ARG A . n 
A 1  302  ARG 302  302  302  ARG ARG A . n 
A 1  303  LEU 303  303  303  LEU LEU A . n 
A 1  304  PRO 304  304  304  PRO PRO A . n 
A 1  305  ARG 305  305  305  ARG ARG A . n 
A 1  306  LYS 306  306  306  LYS LYS A . n 
A 1  307  GLU 307  307  307  GLU GLU A . n 
A 1  308  GLY 308  308  308  GLY GLY A . n 
A 1  309  ARG 309  309  309  ARG ARG A . n 
A 1  310  ILE 310  310  310  ILE ILE A . n 
A 1  311  ARG 311  311  311  ARG ARG A . n 
A 1  312  LYS 312  312  312  LYS LYS A . n 
A 1  313  SER 313  313  313  SER SER A . n 
A 1  314  LEU 314  314  314  LEU LEU A . n 
A 1  315  LEU 315  315  315  LEU LEU A . n 
A 1  316  GLY 316  316  316  GLY GLY A . n 
A 1  317  SER 317  317  317  SER SER A . n 
A 1  318  GLN 318  318  318  GLN GLN A . n 
A 1  319  VAL 319  319  319  VAL VAL A . n 
A 1  320  TRP 320  320  320  TRP TRP A . n 
A 1  321  SER 321  321  321  SER SER A . n 
A 1  322  ILE 322  322  322  ILE ILE A . n 
A 1  323  SER 323  323  323  SER SER A . n 
A 1  324  ARG 324  324  324  ARG ARG A . n 
A 1  325  SER 325  325  325  SER SER A . n 
A 1  326  THR 326  326  326  THR THR A . n 
A 1  327  ILE 327  327  327  ILE ILE A . n 
A 1  328  CYS 328  328  328  CYS CYS A . n 
A 1  329  GLY 329  329  329  GLY GLY A . n 
A 1  330  ASN 330  330  330  ASN ASN A . n 
A 1  331  SER 331  331  331  SER SER A . n 
A 1  332  ASP 332  332  332  ASP ASP A . n 
A 1  333  LEU 333  333  333  LEU LEU A . n 
A 1  334  HIS 334  334  334  HIS HIS A . n 
A 1  335  LEU 335  335  335  LEU LEU A . n 
A 1  336  ASP 336  336  336  ASP ASP A . n 
A 1  337  GLU 337  337  337  GLU GLU A . n 
A 1  338  VAL 338  338  338  VAL VAL A . n 
A 1  339  GLY 339  339  339  GLY GLY A . n 
A 1  340  TYR 340  340  340  TYR TYR A . n 
A 1  341  PRO 341  341  341  PRO PRO A . n 
A 1  342  ILE 342  342  342  ILE ILE A . n 
A 1  343  SER 343  343  343  SER SER A . n 
A 1  344  PHE 344  344  344  PHE PHE A . n 
A 1  345  ALA 345  345  345  ALA ALA A . n 
A 1  346  ARG 346  346  346  ARG ARG A . n 
A 1  347  THR 347  347  347  THR THR A . n 
A 1  348  LEU 348  348  348  LEU LEU A . n 
A 1  349  GLN 349  349  349  GLN GLN A . n 
A 1  350  VAL 350  350  350  VAL VAL A . n 
A 1  351  ALA 351  351  351  ALA ALA A . n 
A 1  352  GLU 352  352  352  GLU GLU A . n 
A 1  353  THR 353  353  353  THR THR A . n 
A 1  354  VAL 354  354  354  VAL VAL A . n 
A 1  355  GLN 355  355  355  GLN GLN A . n 
A 1  356  HIS 356  356  356  HIS HIS A . n 
A 1  357  TYR 357  357  357  TYR TYR A . n 
A 1  358  ASN 358  358  358  ASN ASN A . n 
A 1  359  ILE 359  359  359  ILE ILE A . n 
A 1  360  ASN 360  360  360  ASN ASN A . n 
A 1  361  ARG 361  361  361  ARG ARG A . n 
A 1  362  LEU 362  362  362  LEU LEU A . n 
A 1  363  MET 363  363  363  MET MET A . n 
A 1  364  PRO 364  364  364  PRO PRO A . n 
A 1  365  TYR 365  365  365  TYR TYR A . n 
A 1  366  PHE 366  366  366  PHE PHE A . n 
A 1  367  LEU 367  367  367  LEU LEU A . n 
A 1  368  ASN 368  368  368  ASN ASN A . n 
A 1  369  GLY 369  369  369  GLY GLY A . n 
A 1  370  LYS 370  370  370  LYS LYS A . n 
A 1  371  ARG 371  371  371  ARG ARG A . n 
A 1  372  GLN 372  372  372  GLN GLN A . n 
A 1  373  TYR 373  373  373  TYR TYR A . n 
A 1  374  PRO 374  374  374  PRO PRO A . n 
A 1  375  GLY 375  375  375  GLY GLY A . n 
A 1  376  CYS 376  376  376  CYS CYS A . n 
A 1  377  SER 377  377  377  SER SER A . n 
A 1  378  ARG 378  378  378  ARG ARG A . n 
A 1  379  VAL 379  379  379  VAL VAL A . n 
A 1  380  TYR 380  380  380  TYR TYR A . n 
A 1  381  LYS 381  381  381  LYS LYS A . n 
A 1  382  GLN 382  382  382  GLN GLN A . n 
A 1  383  ILE 383  383  383  ILE ILE A . n 
A 1  384  THR 384  384  384  THR THR A . n 
A 1  385  GLN 385  385  385  GLN GLN A . n 
A 1  386  SER 386  386  386  SER SER A . n 
A 1  387  VAL 387  387  387  VAL VAL A . n 
A 1  388  HIS 388  388  388  HIS HIS A . n 
A 1  389  ASP 389  389  389  ASP ASP A . n 
A 1  390  ILE 390  390  390  ILE ILE A . n 
A 1  391  GLU 391  391  391  GLU GLU A . n 
A 1  392  GLY 392  392  392  GLY GLY A . n 
A 1  393  LEU 393  393  393  LEU LEU A . n 
A 1  394  LYS 394  394  394  LYS LYS A . n 
A 1  395  GLN 395  395  395  GLN GLN A . n 
A 1  396  ASP 396  396  396  ASP ASP A . n 
A 1  397  PHE 397  397  397  PHE PHE A . n 
A 1  398  ARG 398  398  398  ARG ARG A . n 
A 1  399  LEU 399  399  399  LEU LEU A . n 
A 1  400  GLU 400  400  400  GLU GLU A . n 
A 1  401  VAL 401  401  401  VAL VAL A . n 
A 1  402  GLY 402  402  402  GLY GLY A . n 
A 1  403  ASP 403  403  403  ASP ASP A . n 
A 1  404  ILE 404  404  404  ILE ILE A . n 
A 1  405  LEU 405  405  405  LEU LEU A . n 
A 1  406  TYR 406  406  406  TYR TYR A . n 
A 1  407  ARG 407  407  407  ARG ARG A . n 
A 1  408  ASP 408  408  408  ASP ASP A . n 
A 1  409  VAL 409  409  409  VAL VAL A . n 
A 1  410  VAL 410  410  410  VAL VAL A . n 
A 1  411  THR 411  411  411  THR THR A . n 
A 1  412  GLY 412  412  412  GLY GLY A . n 
A 1  413  ASP 413  413  413  ASP ASP A . n 
A 1  414  VAL 414  414  414  VAL VAL A . n 
A 1  415  ALA 415  415  415  ALA ALA A . n 
A 1  416  PHE 416  416  416  PHE PHE A . n 
A 1  417  PHE 417  417  417  PHE PHE A . n 
A 1  418  ASN 418  418  418  ASN ASN A . n 
A 1  419  ARG 419  419  419  ARG ARG A . n 
A 1  420  GLN 420  420  420  GLN GLN A . n 
A 1  421  PRO 421  421  421  PRO PRO A . n 
A 1  422  SER 422  422  422  SER SER A . n 
A 1  423  LEU 423  423  423  LEU LEU A . n 
A 1  424  GLU 424  424  424  GLU GLU A . n 
A 1  425  ARG 425  425  425  ARG ARG A . n 
A 1  426  SER 426  426  426  SER SER A . n 
A 1  427  SER 427  427  427  SER SER A . n 
A 1  428  ILE 428  428  428  ILE ILE A . n 
A 1  429  GLY 429  429  429  GLY GLY A . n 
A 1  430  VAL 430  430  430  VAL VAL A . n 
A 1  431  HIS 431  431  431  HIS HIS A . n 
A 1  432  ARG 432  432  432  ARG ARG A . n 
A 1  433  ILE 433  433  433  ILE ILE A . n 
A 1  434  VAL 434  434  434  VAL VAL A . n 
A 1  435  VAL 435  435  435  VAL VAL A . n 
A 1  436  LEU 436  436  436  LEU LEU A . n 
A 1  437  GLU 437  437  437  GLU GLU A . n 
A 1  438  ASN 438  438  438  ASN ASN A . n 
A 1  439  PRO 439  439  439  PRO PRO A . n 
A 1  440  LYS 440  440  440  LYS LYS A . n 
A 1  441  ILE 441  441  441  ILE ILE A . n 
A 1  442  SER 442  442  442  SER SER A . n 
A 1  443  THR 443  443  443  THR THR A . n 
A 1  444  PHE 444  444  444  PHE PHE A . n 
A 1  445  GLN 445  445  445  GLN GLN A . n 
A 1  446  MET 446  446  446  MET MET A . n 
A 1  447  ASN 447  447  447  ASN ASN A . n 
A 1  448  VAL 448  448  448  VAL VAL A . n 
A 1  449  SER 449  449  449  SER SER A . n 
A 1  450  ALA 450  450  450  ALA ALA A . n 
A 1  451  CYS 451  451  451  CYS CYS A . n 
A 1  452  ALA 452  452  452  ALA ALA A . n 
A 1  453  TRP 453  453  453  TRP TRP A . n 
A 1  454  TYR 454  454  454  TYR TYR A . n 
A 1  455  ASN 455  455  455  ASN ASN A . n 
A 1  456  ALA 456  456  456  ALA ALA A . n 
A 1  457  ASP 457  457  457  ASP ASP A . n 
A 1  458  PHE 458  458  458  PHE PHE A . n 
A 1  459  ASP 459  459  459  ASP ASP A . n 
A 1  460  GLY 460  460  460  GLY GLY A . n 
A 1  461  ASP 461  461  461  ASP ASP A . n 
A 1  462  GLN 462  462  462  GLN GLN A . n 
A 1  463  MET 463  463  463  MET MET A . n 
A 1  464  ASN 464  464  464  ASN ASN A . n 
A 1  465  LEU 465  465  465  LEU LEU A . n 
A 1  466  TRP 466  466  466  TRP TRP A . n 
A 1  467  VAL 467  467  467  VAL VAL A . n 
A 1  468  PRO 468  468  468  PRO PRO A . n 
A 1  469  TRP 469  469  469  TRP TRP A . n 
A 1  470  SER 470  470  470  SER SER A . n 
A 1  471  VAL 471  471  471  VAL VAL A . n 
A 1  472  MET 472  472  472  MET MET A . n 
A 1  473  SER 473  473  473  SER SER A . n 
A 1  474  ARG 474  474  474  ARG ARG A . n 
A 1  475  VAL 475  475  475  VAL VAL A . n 
A 1  476  GLU 476  476  476  GLU GLU A . n 
A 1  477  ALA 477  477  477  ALA ALA A . n 
A 1  478  GLU 478  478  478  GLU GLU A . n 
A 1  479  LEU 479  479  479  LEU LEU A . n 
A 1  480  LEU 480  480  480  LEU LEU A . n 
A 1  481  CYS 481  481  481  CYS CYS A . n 
A 1  482  SER 482  482  482  SER SER A . n 
A 1  483  VAL 483  483  483  VAL VAL A . n 
A 1  484  ARG 484  484  484  ARG ARG A . n 
A 1  485  ASN 485  485  485  ASN ASN A . n 
A 1  486  TRP 486  486  486  TRP TRP A . n 
A 1  487  PHE 487  487  487  PHE PHE A . n 
A 1  488  ILE 488  488  488  ILE ILE A . n 
A 1  489  SER 489  489  489  SER SER A . n 
A 1  490  THR 490  490  490  THR THR A . n 
A 1  491  LYS 491  491  491  LYS LYS A . n 
A 1  492  SER 492  492  492  SER SER A . n 
A 1  493  SER 493  493  493  SER SER A . n 
A 1  494  GLY 494  494  494  GLY GLY A . n 
A 1  495  PRO 495  495  495  PRO PRO A . n 
A 1  496  VAL 496  496  496  VAL VAL A . n 
A 1  497  ASN 497  497  497  ASN ASN A . n 
A 1  498  GLY 498  498  498  GLY GLY A . n 
A 1  499  GLN 499  499  499  GLN GLN A . n 
A 1  500  VAL 500  500  500  VAL VAL A . n 
A 1  501  GLN 501  501  501  GLN GLN A . n 
A 1  502  ASP 502  502  502  ASP ASP A . n 
A 1  503  SER 503  503  503  SER SER A . n 
A 1  504  THR 504  504  504  THR THR A . n 
A 1  505  VAL 505  505  505  VAL VAL A . n 
A 1  506  GLY 506  506  506  GLY GLY A . n 
A 1  507  SER 507  507  507  SER SER A . n 
A 1  508  PHE 508  508  508  PHE PHE A . n 
A 1  509  LEU 509  509  509  LEU LEU A . n 
A 1  510  LEU 510  510  510  LEU LEU A . n 
A 1  511  THR 511  511  511  THR THR A . n 
A 1  512  ARG 512  512  512  ARG ARG A . n 
A 1  513  THR 513  513  513  THR THR A . n 
A 1  514  ASN 514  514  514  ASN ASN A . n 
A 1  515  THR 515  515  515  THR THR A . n 
A 1  516  PRO 516  516  516  PRO PRO A . n 
A 1  517  MET 517  517  517  MET MET A . n 
A 1  518  GLY 518  518  518  GLY GLY A . n 
A 1  519  LYS 519  519  519  LYS LYS A . n 
A 1  520  ASN 520  520  520  ASN ASN A . n 
A 1  521  VAL 521  521  521  VAL VAL A . n 
A 1  522  MET 522  522  522  MET MET A . n 
A 1  523  ASN 523  523  523  ASN ASN A . n 
A 1  524  LYS 524  524  524  LYS LYS A . n 
A 1  525  LEU 525  525  525  LEU LEU A . n 
A 1  526  HIS 526  526  526  HIS HIS A . n 
A 1  527  ALA 527  527  527  ALA ALA A . n 
A 1  528  MET 528  528  528  MET MET A . n 
A 1  529  GLY 529  529  529  GLY GLY A . n 
A 1  530  LEU 530  530  530  LEU LEU A . n 
A 1  531  PHE 531  531  531  PHE PHE A . n 
A 1  532  GLN 532  532  532  GLN GLN A . n 
A 1  533  THR 533  533  533  THR THR A . n 
A 1  534  THR 534  534  534  THR THR A . n 
A 1  535  GLN 535  535  535  GLN GLN A . n 
A 1  536  THR 536  536  536  THR THR A . n 
A 1  537  ASP 537  537  537  ASP ASP A . n 
A 1  538  PRO 538  538  538  PRO PRO A . n 
A 1  539  PRO 539  539  539  PRO PRO A . n 
A 1  540  CYS 540  540  540  CYS CYS A . n 
A 1  541  PHE 541  541  541  PHE PHE A . n 
A 1  542  ALA 542  542  542  ALA ALA A . n 
A 1  543  ASN 543  543  543  ASN ASN A . n 
A 1  544  TYR 544  544  544  TYR TYR A . n 
A 1  545  SER 545  545  545  SER SER A . n 
A 1  546  PRO 546  546  546  PRO PRO A . n 
A 1  547  THR 547  547  547  THR THR A . n 
A 1  548  ASP 548  548  548  ASP ASP A . n 
A 1  549  LEU 549  549  549  LEU LEU A . n 
A 1  550  LEU 550  550  550  LEU LEU A . n 
A 1  551  ASP 551  551  551  ASP ASP A . n 
A 1  552  GLY 552  552  552  GLY GLY A . n 
A 1  553  LYS 553  553  553  LYS LYS A . n 
A 1  554  SER 554  554  554  SER SER A . n 
A 1  555  VAL 555  555  555  VAL VAL A . n 
A 1  556  VAL 556  556  556  VAL VAL A . n 
A 1  557  SER 557  557  557  SER SER A . n 
A 1  558  MET 558  558  558  MET MET A . n 
A 1  559  LEU 559  559  559  LEU LEU A . n 
A 1  560  LEU 560  560  560  LEU LEU A . n 
A 1  561  ARG 561  561  561  ARG ARG A . n 
A 1  562  GLN 562  562  562  GLN GLN A . n 
A 1  563  THR 563  563  563  THR THR A . n 
A 1  564  PRO 564  564  564  PRO PRO A . n 
A 1  565  ILE 565  565  565  ILE ILE A . n 
A 1  566  ASN 566  566  566  ASN ASN A . n 
A 1  567  TYR 567  567  567  TYR TYR A . n 
A 1  568  GLN 568  568  568  GLN GLN A . n 
A 1  569  ARG 569  569  569  ARG ARG A . n 
A 1  570  ALA 570  570  570  ALA ALA A . n 
A 1  571  PRO 571  571  571  PRO PRO A . n 
A 1  572  THR 572  572  572  THR THR A . n 
A 1  573  TRP 573  573  573  TRP TRP A . n 
A 1  574  TYR 574  574  574  TYR TYR A . n 
A 1  575  SER 575  575  575  SER SER A . n 
A 1  576  GLU 576  576  576  GLU GLU A . n 
A 1  577  VAL 577  577  577  VAL VAL A . n 
A 1  578  TYR 578  578  578  TYR TYR A . n 
A 1  579  ALA 579  579  579  ALA ALA A . n 
A 1  580  PRO 580  580  580  PRO PRO A . n 
A 1  581  TYR 581  581  581  TYR TYR A . n 
A 1  582  MET 582  582  582  MET MET A . n 
A 1  583  HIS 583  583  583  HIS HIS A . n 
A 1  584  TYR 584  584  584  TYR TYR A . n 
A 1  585  ASN 585  585  585  ASN ASN A . n 
A 1  586  LYS 586  586  586  LYS LYS A . n 
A 1  587  GLN 587  587  587  GLN GLN A . n 
A 1  588  ASP 588  588  588  ASP ASP A . n 
A 1  589  ILE 589  589  589  ILE ILE A . n 
A 1  590  SER 590  590  590  SER SER A . n 
A 1  591  THR 591  591  591  THR THR A . n 
A 1  592  GLN 592  592  592  GLN GLN A . n 
A 1  593  ILE 593  593  593  ILE ILE A . n 
A 1  594  ARG 594  594  594  ARG ARG A . n 
A 1  595  ASN 595  595  595  ASN ASN A . n 
A 1  596  GLY 596  596  596  GLY GLY A . n 
A 1  597  GLU 597  597  597  GLU GLU A . n 
A 1  598  LEU 598  598  598  LEU LEU A . n 
A 1  599  ILE 599  599  599  ILE ILE A . n 
A 1  600  GLU 600  600  600  GLU GLU A . n 
A 1  601  GLY 601  601  601  GLY GLY A . n 
A 1  602  VAL 602  602  602  VAL VAL A . n 
A 1  603  LEU 603  603  603  LEU LEU A . n 
A 1  604  ASP 604  604  604  ASP ASP A . n 
A 1  605  LYS 605  605  605  LYS LYS A . n 
A 1  606  LYS 606  606  606  LYS LYS A . n 
A 1  607  ALA 607  607  607  ALA ALA A . n 
A 1  608  VAL 608  608  608  VAL VAL A . n 
A 1  609  GLY 609  609  609  GLY GLY A . n 
A 1  610  ALA 610  610  610  ALA ALA A . n 
A 1  611  GLY 611  611  611  GLY GLY A . n 
A 1  612  SER 612  612  612  SER SER A . n 
A 1  613  SER 613  613  613  SER SER A . n 
A 1  614  GLY 614  614  614  GLY GLY A . n 
A 1  615  GLY 615  615  615  GLY GLY A . n 
A 1  616  ILE 616  616  616  ILE ILE A . n 
A 1  617  TYR 617  617  617  TYR TYR A . n 
A 1  618  HIS 618  618  618  HIS HIS A . n 
A 1  619  LEU 619  619  619  LEU LEU A . n 
A 1  620  ILE 620  620  620  ILE ILE A . n 
A 1  621  SER 621  621  621  SER SER A . n 
A 1  622  ARG 622  622  622  ARG ARG A . n 
A 1  623  ARG 623  623  623  ARG ARG A . n 
A 1  624  TYR 624  624  624  TYR TYR A . n 
A 1  625  GLY 625  625  625  GLY GLY A . n 
A 1  626  PRO 626  626  626  PRO PRO A . n 
A 1  627  GLN 627  627  627  GLN GLN A . n 
A 1  628  GLN 628  628  628  GLN GLN A . n 
A 1  629  ALA 629  629  629  ALA ALA A . n 
A 1  630  LEU 630  630  630  LEU LEU A . n 
A 1  631  LYS 631  631  631  LYS LYS A . n 
A 1  632  MET 632  632  632  MET MET A . n 
A 1  633  ILE 633  633  633  ILE ILE A . n 
A 1  634  PHE 634  634  634  PHE PHE A . n 
A 1  635  ALA 635  635  635  ALA ALA A . n 
A 1  636  THR 636  636  636  THR THR A . n 
A 1  637  GLN 637  637  637  GLN GLN A . n 
A 1  638  GLN 638  638  638  GLN GLN A . n 
A 1  639  LEU 639  639  639  LEU LEU A . n 
A 1  640  ALA 640  640  640  ALA ALA A . n 
A 1  641  LEU 641  641  641  LEU LEU A . n 
A 1  642  ASN 642  642  642  ASN ASN A . n 
A 1  643  TYR 643  643  643  TYR TYR A . n 
A 1  644  VAL 644  644  644  VAL VAL A . n 
A 1  645  ARG 645  645  645  ARG ARG A . n 
A 1  646  ASN 646  646  646  ASN ASN A . n 
A 1  647  ALA 647  647  647  ALA ALA A . n 
A 1  648  GLY 648  648  648  GLY GLY A . n 
A 1  649  PHE 649  649  649  PHE PHE A . n 
A 1  650  THR 650  650  650  THR THR A . n 
A 1  651  VAL 651  651  651  VAL VAL A . n 
A 1  652  SER 652  652  652  SER SER A . n 
A 1  653  THR 653  653  653  THR THR A . n 
A 1  654  ALA 654  654  654  ALA ALA A . n 
A 1  655  ASP 655  655  655  ASP ASP A . n 
A 1  656  MET 656  656  656  MET MET A . n 
A 1  657  LEU 657  657  657  LEU LEU A . n 
A 1  658  LEU 658  658  658  LEU LEU A . n 
A 1  659  THR 659  659  659  THR THR A . n 
A 1  660  PRO 660  660  660  PRO PRO A . n 
A 1  661  GLU 661  661  661  GLU GLU A . n 
A 1  662  ALA 662  662  662  ALA ALA A . n 
A 1  663  HIS 663  663  663  HIS HIS A . n 
A 1  664  GLN 664  664  664  GLN GLN A . n 
A 1  665  GLU 665  665  665  GLU GLU A . n 
A 1  666  VAL 666  666  666  VAL VAL A . n 
A 1  667  GLN 667  667  667  GLN GLN A . n 
A 1  668  GLU 668  668  668  GLU GLU A . n 
A 1  669  ILE 669  669  669  ILE ILE A . n 
A 1  670  ILE 670  670  670  ILE ILE A . n 
A 1  671  ASN 671  671  671  ASN ASN A . n 
A 1  672  GLU 672  672  672  GLU GLU A . n 
A 1  673  LEU 673  673  673  LEU LEU A . n 
A 1  674  LEU 674  674  674  LEU LEU A . n 
A 1  675  LEU 675  675  675  LEU LEU A . n 
A 1  676  GLU 676  676  676  GLU GLU A . n 
A 1  677  SER 677  677  677  SER SER A . n 
A 1  678  GLU 678  678  678  GLU GLU A . n 
A 1  679  GLU 679  679  679  GLU GLU A . n 
A 1  680  ILE 680  680  680  ILE ILE A . n 
A 1  681  ASN 681  681  681  ASN ASN A . n 
A 1  682  ASN 682  682  682  ASN ASN A . n 
A 1  683  ARG 683  683  683  ARG ARG A . n 
A 1  684  LEU 684  684  684  LEU LEU A . n 
A 1  685  LEU 685  685  685  LEU LEU A . n 
A 1  686  HIS 686  686  686  HIS HIS A . n 
A 1  687  GLY 687  687  687  GLY GLY A . n 
A 1  688  ASP 688  688  688  ASP ASP A . n 
A 1  689  ILE 689  689  689  ILE ILE A . n 
A 1  690  MET 690  690  690  MET MET A . n 
A 1  691  PRO 691  691  691  PRO PRO A . n 
A 1  692  PRO 692  692  692  PRO PRO A . n 
A 1  693  ILE 693  693  693  ILE ILE A . n 
A 1  694  GLY 694  694  694  GLY GLY A . n 
A 1  695  LEU 695  695  695  LEU LEU A . n 
A 1  696  THR 696  696  696  THR THR A . n 
A 1  697  THR 697  697  697  THR THR A . n 
A 1  698  HIS 698  698  698  HIS HIS A . n 
A 1  699  ASP 699  699  699  ASP ASP A . n 
A 1  700  PHE 700  700  700  PHE PHE A . n 
A 1  701  TYR 701  701  701  TYR TYR A . n 
A 1  702  GLU 702  702  702  GLU GLU A . n 
A 1  703  LYS 703  703  703  LYS LYS A . n 
A 1  704  LEU 704  704  704  LEU LEU A . n 
A 1  705  GLN 705  705  705  GLN GLN A . n 
A 1  706  LEU 706  706  706  LEU LEU A . n 
A 1  707  ASN 707  707  707  ASN ASN A . n 
A 1  708  ALA 708  708  708  ALA ALA A . n 
A 1  709  LEU 709  709  709  LEU LEU A . n 
A 1  710  LYS 710  710  710  LYS LYS A . n 
A 1  711  PHE 711  711  711  PHE PHE A . n 
A 1  712  PRO 712  712  712  PRO PRO A . n 
A 1  713  ASP 713  713  713  ASP ASP A . n 
A 1  714  ARG 714  714  714  ARG ARG A . n 
A 1  715  ILE 715  715  715  ILE ILE A . n 
A 1  716  LEU 716  716  716  LEU LEU A . n 
A 1  717  LYS 717  717  717  LYS LYS A . n 
A 1  718  PRO 718  718  718  PRO PRO A . n 
A 1  719  ILE 719  719  719  ILE ILE A . n 
A 1  720  MET 720  720  720  MET MET A . n 
A 1  721  ASN 721  721  721  ASN ASN A . n 
A 1  722  SER 722  722  722  SER SER A . n 
A 1  723  ILE 723  723  723  ILE ILE A . n 
A 1  724  ASN 724  724  724  ASN ASN A . n 
A 1  725  PRO 725  725  725  PRO PRO A . n 
A 1  726  GLU 726  726  726  GLU GLU A . n 
A 1  727  THR 727  727  727  THR THR A . n 
A 1  728  ASN 728  728  728  ASN ASN A . n 
A 1  729  GLY 729  729  729  GLY GLY A . n 
A 1  730  LEU 730  730  730  LEU LEU A . n 
A 1  731  PHE 731  731  731  PHE PHE A . n 
A 1  732  GLN 732  732  732  GLN GLN A . n 
A 1  733  MET 733  733  733  MET MET A . n 
A 1  734  VAL 734  734  734  VAL VAL A . n 
A 1  735  ALA 735  735  735  ALA ALA A . n 
A 1  736  THR 736  736  736  THR THR A . n 
A 1  737  GLY 737  737  737  GLY GLY A . n 
A 1  738  ALA 738  738  738  ALA ALA A . n 
A 1  739  LYS 739  739  739  LYS LYS A . n 
A 1  740  GLY 740  740  740  GLY GLY A . n 
A 1  741  SER 741  741  741  SER SER A . n 
A 1  742  ASN 742  742  742  ASN ASN A . n 
A 1  743  PRO 743  743  743  PRO PRO A . n 
A 1  744  ASN 744  744  744  ASN ASN A . n 
A 1  745  MET 745  745  745  MET MET A . n 
A 1  746  ILE 746  746  746  ILE ILE A . n 
A 1  747  HIS 747  747  747  HIS HIS A . n 
A 1  748  ILE 748  748  748  ILE ILE A . n 
A 1  749  MET 749  749  749  MET MET A . n 
A 1  750  ALA 750  750  750  ALA ALA A . n 
A 1  751  GLY 751  751  751  GLY GLY A . n 
A 1  752  ILE 752  752  752  ILE ILE A . n 
A 1  753  GLY 753  753  753  GLY GLY A . n 
A 1  754  GLN 754  754  754  GLN GLN A . n 
A 1  755  ILE 755  755  755  ILE ILE A . n 
A 1  756  GLU 756  756  756  GLU GLU A . n 
A 1  757  ILE 757  757  757  ILE ILE A . n 
A 1  758  ASN 758  758  758  ASN ASN A . n 
A 1  759  THR 759  759  759  THR THR A . n 
A 1  760  GLN 760  760  760  GLN GLN A . n 
A 1  761  ARG 761  761  761  ARG ARG A . n 
A 1  762  ILE 762  762  762  ILE ILE A . n 
A 1  763  GLN 763  763  763  GLN GLN A . n 
A 1  764  PRO 764  764  764  PRO PRO A . n 
A 1  765  GLN 765  765  765  GLN GLN A . n 
A 1  766  PHE 766  766  766  PHE PHE A . n 
A 1  767  SER 767  767  767  SER SER A . n 
A 1  768  PHE 768  768  768  PHE PHE A . n 
A 1  769  GLY 769  769  769  GLY GLY A . n 
A 1  770  ARG 770  770  770  ARG ARG A . n 
A 1  771  THR 771  771  771  THR THR A . n 
A 1  772  LEU 772  772  772  LEU LEU A . n 
A 1  773  VAL 773  773  773  VAL VAL A . n 
A 1  774  TYR 774  774  774  TYR TYR A . n 
A 1  775  TYR 775  775  775  TYR TYR A . n 
A 1  776  PRO 776  776  776  PRO PRO A . n 
A 1  777  ARG 777  777  777  ARG ARG A . n 
A 1  778  PHE 778  778  778  PHE PHE A . n 
A 1  779  ALA 779  779  779  ALA ALA A . n 
A 1  780  LEU 780  780  780  LEU LEU A . n 
A 1  781  GLU 781  781  781  GLU GLU A . n 
A 1  782  ALA 782  782  782  ALA ALA A . n 
A 1  783  GLN 783  783  783  GLN GLN A . n 
A 1  784  ALA 784  784  784  ALA ALA A . n 
A 1  785  TYR 785  785  785  TYR TYR A . n 
A 1  786  GLY 786  786  786  GLY GLY A . n 
A 1  787  PHE 787  787  787  PHE PHE A . n 
A 1  788  ILE 788  788  788  ILE ILE A . n 
A 1  789  CYS 789  789  789  CYS CYS A . n 
A 1  790  ASN 790  790  790  ASN ASN A . n 
A 1  791  SER 791  791  791  SER SER A . n 
A 1  792  TYR 792  792  792  TYR TYR A . n 
A 1  793  ILE 793  793  793  ILE ILE A . n 
A 1  794  ALA 794  794  794  ALA ALA A . n 
A 1  795  GLY 795  795  795  GLY GLY A . n 
A 1  796  LEU 796  796  796  LEU LEU A . n 
A 1  797  THR 797  797  797  THR THR A . n 
A 1  798  SER 798  798  798  SER SER A . n 
A 1  799  PRO 799  799  799  PRO PRO A . n 
A 1  800  GLU 800  800  800  GLU GLU A . n 
A 1  801  PHE 801  801  801  PHE PHE A . n 
A 1  802  ILE 802  802  802  ILE ILE A . n 
A 1  803  PHE 803  803  803  PHE PHE A . n 
A 1  804  GLY 804  804  804  GLY GLY A . n 
A 1  805  GLU 805  805  805  GLU GLU A . n 
A 1  806  MET 806  806  806  MET MET A . n 
A 1  807  ASN 807  807  807  ASN ASN A . n 
A 1  808  GLY 808  808  808  GLY GLY A . n 
A 1  809  ARG 809  809  809  ARG ARG A . n 
A 1  810  PHE 810  810  810  PHE PHE A . n 
A 1  811  ASP 811  811  811  ASP ASP A . n 
A 1  812  LEU 812  812  812  LEU LEU A . n 
A 1  813  ILE 813  813  813  ILE ILE A . n 
A 1  814  ASN 814  814  814  ASN ASN A . n 
A 1  815  LYS 815  815  815  LYS LYS A . n 
A 1  816  ALA 816  816  816  ALA ALA A . n 
A 1  817  LEU 817  817  817  LEU LEU A . n 
A 1  818  SER 818  818  818  SER SER A . n 
A 1  819  THR 819  819  819  THR THR A . n 
A 1  820  SER 820  820  820  SER SER A . n 
A 1  821  SER 821  821  821  SER SER A . n 
A 1  822  THR 822  822  822  THR THR A . n 
A 1  823  GLY 823  823  823  GLY GLY A . n 
A 1  824  TYR 824  824  824  TYR TYR A . n 
A 1  825  ALA 825  825  825  ALA ALA A . n 
A 1  826  ASN 826  826  826  ASN ASN A . n 
A 1  827  ARG 827  827  827  ARG ARG A . n 
A 1  828  LYS 828  828  828  LYS LYS A . n 
A 1  829  ALA 829  829  829  ALA ALA A . n 
A 1  830  ILE 830  830  830  ILE ILE A . n 
A 1  831  PHE 831  831  831  PHE PHE A . n 
A 1  832  GLY 832  832  832  GLY GLY A . n 
A 1  833  LEU 833  833  833  LEU LEU A . n 
A 1  834  GLN 834  834  834  GLN GLN A . n 
A 1  835  SER 835  835  835  SER SER A . n 
A 1  836  CYS 836  836  836  CYS CYS A . n 
A 1  837  ILE 837  837  837  ILE ILE A . n 
A 1  838  VAL 838  838  838  VAL VAL A . n 
A 1  839  ASP 839  839  839  ASP ASP A . n 
A 1  840  TYR 840  840  840  TYR TYR A . n 
A 1  841  TYR 841  841  841  TYR TYR A . n 
A 1  842  ARG 842  842  842  ARG ARG A . n 
A 1  843  ARG 843  843  843  ARG ARG A . n 
A 1  844  VAL 844  844  844  VAL VAL A . n 
A 1  845  SER 845  845  845  SER SER A . n 
A 1  846  ILE 846  846  846  ILE ILE A . n 
A 1  847  ASP 847  847  847  ASP ASP A . n 
A 1  848  THR 848  848  848  THR THR A . n 
A 1  849  ARG 849  849  849  ARG ARG A . n 
A 1  850  LEU 850  850  850  LEU LEU A . n 
A 1  851  VAL 851  851  851  VAL VAL A . n 
A 1  852  GLN 852  852  852  GLN GLN A . n 
A 1  853  GLN 853  853  853  GLN GLN A . n 
A 1  854  LEU 854  854  854  LEU LEU A . n 
A 1  855  TYR 855  855  855  TYR TYR A . n 
A 1  856  GLY 856  856  856  GLY GLY A . n 
A 1  857  GLU 857  857  857  GLU GLU A . n 
A 1  858  ASP 858  858  858  ASP ASP A . n 
A 1  859  GLY 859  859  859  GLY GLY A . n 
A 1  860  LEU 860  860  860  LEU LEU A . n 
A 1  861  ASP 861  861  861  ASP ASP A . n 
A 1  862  ALA 862  862  862  ALA ALA A . n 
A 1  863  ARG 863  863  863  ARG ARG A . n 
A 1  864  GLN 864  864  864  GLN GLN A . n 
A 1  865  LEU 865  865  865  LEU LEU A . n 
A 1  866  GLU 866  866  866  GLU GLU A . n 
A 1  867  THR 867  867  867  THR THR A . n 
A 1  868  VAL 868  868  868  VAL VAL A . n 
A 1  869  ARG 869  869  869  ARG ARG A . n 
A 1  870  PHE 870  870  870  PHE PHE A . n 
A 1  871  GLU 871  871  871  GLU GLU A . n 
A 1  872  THR 872  872  872  THR THR A . n 
A 1  873  ILE 873  873  873  ILE ILE A . n 
A 1  874  MET 874  874  874  MET MET A . n 
A 1  875  LEU 875  875  875  LEU LEU A . n 
A 1  876  SER 876  876  876  SER SER A . n 
A 1  877  ASP 877  877  877  ASP ASP A . n 
A 1  878  GLN 878  878  878  GLN GLN A . n 
A 1  879  GLU 879  879  879  GLU GLU A . n 
A 1  880  LEU 880  880  880  LEU LEU A . n 
A 1  881  GLU 881  881  881  GLU GLU A . n 
A 1  882  ASP 882  882  882  ASP ASP A . n 
A 1  883  LYS 883  883  883  LYS LYS A . n 
A 1  884  PHE 884  884  884  PHE PHE A . n 
A 1  885  LYS 885  885  885  LYS LYS A . n 
A 1  886  TYR 886  886  886  TYR TYR A . n 
A 1  887  THR 887  887  887  THR THR A . n 
A 1  888  GLY 888  888  888  GLY GLY A . n 
A 1  889  ILE 889  889  889  ILE ILE A . n 
A 1  890  GLN 890  890  890  GLN GLN A . n 
A 1  891  SER 891  891  891  SER SER A . n 
A 1  892  PRO 892  892  892  PRO PRO A . n 
A 1  893  LEU 893  893  893  LEU LEU A . n 
A 1  894  PHE 894  894  894  PHE PHE A . n 
A 1  895  GLU 895  895  895  GLU GLU A . n 
A 1  896  GLU 896  896  896  GLU GLU A . n 
A 1  897  GLU 897  897  897  GLU GLU A . n 
A 1  898  PHE 898  898  898  PHE PHE A . n 
A 1  899  SER 899  899  899  SER SER A . n 
A 1  900  ARG 900  900  900  ARG ARG A . n 
A 1  901  LEU 901  901  901  LEU LEU A . n 
A 1  902  LYS 902  902  902  LYS LYS A . n 
A 1  903  LYS 903  903  903  LYS LYS A . n 
A 1  904  ASP 904  904  904  ASP ASP A . n 
A 1  905  ARG 905  905  905  ARG ARG A . n 
A 1  906  ASP 906  906  906  ASP ASP A . n 
A 1  907  LYS 907  907  907  LYS LYS A . n 
A 1  908  TYR 908  908  908  TYR TYR A . n 
A 1  909  ARG 909  909  909  ARG ARG A . n 
A 1  910  GLN 910  910  910  GLN GLN A . n 
A 1  911  ILE 911  911  911  ILE ILE A . n 
A 1  912  PHE 912  912  912  PHE PHE A . n 
A 1  913  LEU 913  913  913  LEU LEU A . n 
A 1  914  ASN 914  914  914  ASN ASN A . n 
A 1  915  VAL 915  915  915  VAL VAL A . n 
A 1  916  GLU 916  916  916  GLU GLU A . n 
A 1  917  ASN 917  917  917  ASN ASN A . n 
A 1  918  PHE 918  918  918  PHE PHE A . n 
A 1  919  ASN 919  919  919  ASN ASN A . n 
A 1  920  PHE 920  920  920  PHE PHE A . n 
A 1  921  SER 921  921  921  SER SER A . n 
A 1  922  GLN 922  922  922  GLN GLN A . n 
A 1  923  LEU 923  923  923  LEU LEU A . n 
A 1  924  LEU 924  924  924  LEU LEU A . n 
A 1  925  THR 925  925  925  THR THR A . n 
A 1  926  ASP 926  926  926  ASP ASP A . n 
A 1  927  VAL 927  927  927  VAL VAL A . n 
A 1  928  ARG 928  928  928  ARG ARG A . n 
A 1  929  GLN 929  929  929  GLN GLN A . n 
A 1  930  VAL 930  930  930  VAL VAL A . n 
A 1  931  PRO 931  931  931  PRO PRO A . n 
A 1  932  VAL 932  932  932  VAL VAL A . n 
A 1  933  ASN 933  933  933  ASN ASN A . n 
A 1  934  VAL 934  934  934  VAL VAL A . n 
A 1  935  ALA 935  935  935  ALA ALA A . n 
A 1  936  SER 936  936  936  SER SER A . n 
A 1  937  ILE 937  937  937  ILE ILE A . n 
A 1  938  VAL 938  938  938  VAL VAL A . n 
A 1  939  LYS 939  939  939  LYS LYS A . n 
A 1  940  ASN 940  940  940  ASN ASN A . n 
A 1  941  ILE 941  941  941  ILE ILE A . n 
A 1  942  LEU 942  942  942  LEU LEU A . n 
A 1  943  LEU 943  943  943  LEU LEU A . n 
A 1  944  SER 944  944  944  SER SER A . n 
A 1  945  SER 945  945  945  SER SER A . n 
A 1  946  THR 946  946  946  THR THR A . n 
A 1  947  SER 947  947  947  SER SER A . n 
A 1  948  GLY 948  948  948  GLY GLY A . n 
A 1  949  VAL 949  949  949  VAL VAL A . n 
A 1  950  LEU 950  950  950  LEU LEU A . n 
A 1  951  PRO 951  951  951  PRO PRO A . n 
A 1  952  PHE 952  952  952  PHE PHE A . n 
A 1  953  ASP 953  953  953  ASP ASP A . n 
A 1  954  GLU 954  954  954  GLU GLU A . n 
A 1  955  LYS 955  955  955  LYS LYS A . n 
A 1  956  SER 956  956  956  SER SER A . n 
A 1  957  ILE 957  957  957  ILE ILE A . n 
A 1  958  LEU 958  958  958  LEU LEU A . n 
A 1  959  GLN 959  959  959  GLN GLN A . n 
A 1  960  LYS 960  960  960  LYS LYS A . n 
A 1  961  TYR 961  961  961  TYR TYR A . n 
A 1  962  ALA 962  962  962  ALA ALA A . n 
A 1  963  MET 963  963  963  MET MET A . n 
A 1  964  VAL 964  964  964  VAL VAL A . n 
A 1  965  LYS 965  965  965  LYS LYS A . n 
A 1  966  THR 966  966  966  THR THR A . n 
A 1  967  PHE 967  967  967  PHE PHE A . n 
A 1  968  CYS 968  968  968  CYS CYS A . n 
A 1  969  LYS 969  969  969  LYS LYS A . n 
A 1  970  ASN 970  970  970  ASN ASN A . n 
A 1  971  LEU 971  971  971  LEU LEU A . n 
A 1  972  PRO 972  972  972  PRO PRO A . n 
A 1  973  TYR 973  973  973  TYR TYR A . n 
A 1  974  VAL 974  974  974  VAL VAL A . n 
A 1  975  PHE 975  975  975  PHE PHE A . n 
A 1  976  ILE 976  976  976  ILE ILE A . n 
A 1  977  ASN 977  977  977  ASN ASN A . n 
A 1  978  ASN 978  978  978  ASN ASN A . n 
A 1  979  ILE 979  979  979  ILE ILE A . n 
A 1  980  GLN 980  980  980  GLN GLN A . n 
A 1  981  GLU 981  981  981  GLU GLU A . n 
A 1  982  ARG 982  982  982  ARG ARG A . n 
A 1  983  LEU 983  983  983  LEU LEU A . n 
A 1  984  GLN 984  984  984  GLN GLN A . n 
A 1  985  THR 985  985  985  THR THR A . n 
A 1  986  PRO 986  986  986  PRO PRO A . n 
A 1  987  ILE 987  987  987  ILE ILE A . n 
A 1  988  PRO 988  988  988  PRO PRO A . n 
A 1  989  VAL 989  989  989  VAL VAL A . n 
A 1  990  TYR 990  990  990  TYR TYR A . n 
A 1  991  LEU 991  991  991  LEU LEU A . n 
A 1  992  LYS 992  992  992  LYS LYS A . n 
A 1  993  ARG 993  993  993  ARG ARG A . n 
A 1  994  ALA 994  994  994  ALA ALA A . n 
A 1  995  ALA 995  995  995  ALA ALA A . n 
A 1  996  SER 996  996  996  SER SER A . n 
A 1  997  LEU 997  997  997  LEU LEU A . n 
A 1  998  MET 998  998  998  MET MET A . n 
A 1  999  ARG 999  999  999  ARG ARG A . n 
A 1  1000 MET 1000 1000 1000 MET MET A . n 
A 1  1001 LEU 1001 1001 1001 LEU LEU A . n 
A 1  1002 ILE 1002 1002 1002 ILE ILE A . n 
A 1  1003 ARG 1003 1003 1003 ARG ARG A . n 
A 1  1004 ILE 1004 1004 1004 ILE ILE A . n 
A 1  1005 GLU 1005 1005 1005 GLU GLU A . n 
A 1  1006 LEU 1006 1006 1006 LEU LEU A . n 
A 1  1007 ALA 1007 1007 1007 ALA ALA A . n 
A 1  1008 THR 1008 1008 1008 THR THR A . n 
A 1  1009 VAL 1009 1009 1009 VAL VAL A . n 
A 1  1010 LYS 1010 1010 1010 LYS LYS A . n 
A 1  1011 THR 1011 1011 1011 THR THR A . n 
A 1  1012 LEU 1012 1012 1012 LEU LEU A . n 
A 1  1013 ASN 1013 1013 1013 ASN ASN A . n 
A 1  1014 ILE 1014 1014 1014 ILE ILE A . n 
A 1  1015 THR 1015 1015 1015 THR THR A . n 
A 1  1016 CYS 1016 1016 1016 CYS CYS A . n 
A 1  1017 GLU 1017 1017 1017 GLU GLU A . n 
A 1  1018 GLN 1018 1018 1018 GLN GLN A . n 
A 1  1019 MET 1019 1019 1019 MET MET A . n 
A 1  1020 SER 1020 1020 1020 SER SER A . n 
A 1  1021 ALA 1021 1021 1021 ALA ALA A . n 
A 1  1022 ILE 1022 1022 1022 ILE ILE A . n 
A 1  1023 LEU 1023 1023 1023 LEU LEU A . n 
A 1  1024 ASP 1024 1024 1024 ASP ASP A . n 
A 1  1025 LEU 1025 1025 1025 LEU LEU A . n 
A 1  1026 ILE 1026 1026 1026 ILE ILE A . n 
A 1  1027 ARG 1027 1027 1027 ARG ARG A . n 
A 1  1028 LEU 1028 1028 1028 LEU LEU A . n 
A 1  1029 GLN 1029 1029 1029 GLN GLN A . n 
A 1  1030 TYR 1030 1030 1030 TYR TYR A . n 
A 1  1031 THR 1031 1031 1031 THR THR A . n 
A 1  1032 GLN 1032 1032 1032 GLN GLN A . n 
A 1  1033 SER 1033 1033 1033 SER SER A . n 
A 1  1034 LEU 1034 1034 1034 LEU LEU A . n 
A 1  1035 ILE 1035 1035 1035 ILE ILE A . n 
A 1  1036 ASN 1036 1036 1036 ASN ASN A . n 
A 1  1037 TYR 1037 1037 1037 TYR TYR A . n 
A 1  1038 GLY 1038 1038 1038 GLY GLY A . n 
A 1  1039 GLU 1039 1039 1039 GLU GLU A . n 
A 1  1040 ALA 1040 1040 1040 ALA ALA A . n 
A 1  1041 VAL 1041 1041 1041 VAL VAL A . n 
A 1  1042 GLY 1042 1042 1042 GLY GLY A . n 
A 1  1043 ILE 1043 1043 1043 ILE ILE A . n 
A 1  1044 LEU 1044 1044 1044 LEU LEU A . n 
A 1  1045 ALA 1045 1045 1045 ALA ALA A . n 
A 1  1046 ALA 1046 1046 1046 ALA ALA A . n 
A 1  1047 GLN 1047 1047 1047 GLN GLN A . n 
A 1  1048 SER 1048 1048 1048 SER SER A . n 
A 1  1049 VAL 1049 1049 1049 VAL VAL A . n 
A 1  1050 SER 1050 1050 1050 SER SER A . n 
A 1  1051 GLU 1051 1051 1051 GLU GLU A . n 
A 1  1052 PRO 1052 1052 1052 PRO PRO A . n 
A 1  1053 LEU 1053 1053 1053 LEU LEU A . n 
A 1  1054 THR 1054 1054 1054 THR THR A . n 
A 1  1055 GLN 1055 1055 1055 GLN GLN A . n 
A 1  1056 TYR 1056 1056 1056 TYR TYR A . n 
A 1  1057 MET 1057 1057 ?    ?   ?   A . n 
A 1  1058 LEU 1058 1058 ?    ?   ?   A . n 
A 1  1059 ASP 1059 1059 ?    ?   ?   A . n 
A 1  1060 SER 1060 1060 ?    ?   ?   A . n 
A 1  1061 HIS 1061 1061 ?    ?   ?   A . n 
A 1  1062 HIS 1062 1062 ?    ?   ?   A . n 
A 1  1063 ARG 1063 1063 ?    ?   ?   A . n 
A 1  1064 SER 1064 1064 ?    ?   ?   A . n 
A 1  1065 VAL 1065 1065 ?    ?   ?   A . n 
A 1  1066 ALA 1066 1066 ?    ?   ?   A . n 
A 1  1067 GLY 1067 1067 ?    ?   ?   A . n 
A 1  1068 GLY 1068 1068 ?    ?   ?   A . n 
A 1  1069 THR 1069 1069 ?    ?   ?   A . n 
A 1  1070 ASN 1070 1070 ?    ?   ?   A . n 
A 1  1071 LYS 1071 1071 ?    ?   ?   A . n 
A 1  1072 SER 1072 1072 ?    ?   ?   A . n 
A 1  1073 GLY 1073 1073 1073 GLY GLY A . n 
A 1  1074 ILE 1074 1074 1074 ILE ILE A . n 
A 1  1075 VAL 1075 1075 1075 VAL VAL A . n 
A 1  1076 ARG 1076 1076 1076 ARG ARG A . n 
A 1  1077 PRO 1077 1077 1077 PRO PRO A . n 
A 1  1078 GLN 1078 1078 1078 GLN GLN A . n 
A 1  1079 GLU 1079 1079 1079 GLU GLU A . n 
A 1  1080 ILE 1080 1080 1080 ILE ILE A . n 
A 1  1081 PHE 1081 1081 1081 PHE PHE A . n 
A 1  1082 SER 1082 1082 1082 SER SER A . n 
A 1  1083 ALA 1083 1083 1083 ALA ALA A . n 
A 1  1084 LYS 1084 1084 1084 LYS LYS A . n 
A 1  1085 PRO 1085 1085 1085 PRO PRO A . n 
A 1  1086 VAL 1086 1086 1086 VAL VAL A . n 
A 1  1087 GLU 1087 1087 1087 GLU GLU A . n 
A 1  1088 ALA 1088 1088 1088 ALA ALA A . n 
A 1  1089 GLU 1089 1089 1089 GLU GLU A . n 
A 1  1090 GLN 1090 1090 1090 GLN GLN A . n 
A 1  1091 SER 1091 1091 1091 SER SER A . n 
A 1  1092 SER 1092 1092 1092 SER SER A . n 
A 1  1093 GLU 1093 1093 1093 GLU GLU A . n 
A 1  1094 MET 1094 1094 1094 MET MET A . n 
A 1  1095 LEU 1095 1095 1095 LEU LEU A . n 
A 1  1096 LEU 1096 1096 1096 LEU LEU A . n 
A 1  1097 ARG 1097 1097 1097 ARG ARG A . n 
A 1  1098 LEU 1098 1098 1098 LEU LEU A . n 
A 1  1099 LYS 1099 1099 1099 LYS LYS A . n 
A 1  1100 ASN 1100 1100 1100 ASN ASN A . n 
A 1  1101 PRO 1101 1101 1101 PRO PRO A . n 
A 1  1102 GLU 1102 1102 1102 GLU GLU A . n 
A 1  1103 VAL 1103 1103 1103 VAL VAL A . n 
A 1  1104 GLU 1104 1104 1104 GLU GLU A . n 
A 1  1105 THR 1105 1105 1105 THR THR A . n 
A 1  1106 ASN 1106 1106 1106 ASN ASN A . n 
A 1  1107 LYS 1107 1107 1107 LYS LYS A . n 
A 1  1108 THR 1108 1108 1108 THR THR A . n 
A 1  1109 TYR 1109 1109 1109 TYR TYR A . n 
A 1  1110 ALA 1110 1110 1110 ALA ALA A . n 
A 1  1111 GLN 1111 1111 1111 GLN GLN A . n 
A 1  1112 GLU 1112 1112 1112 GLU GLU A . n 
A 1  1113 ILE 1113 1113 1113 ILE ILE A . n 
A 1  1114 ALA 1114 1114 1114 ALA ALA A . n 
A 1  1115 ASN 1115 1115 1115 ASN ASN A . n 
A 1  1116 SER 1116 1116 1116 SER SER A . n 
A 1  1117 ILE 1117 1117 1117 ILE ILE A . n 
A 1  1118 GLU 1118 1118 1118 GLU GLU A . n 
A 1  1119 LEU 1119 1119 1119 LEU LEU A . n 
A 1  1120 ILE 1120 1120 1120 ILE ILE A . n 
A 1  1121 THR 1121 1121 1121 THR THR A . n 
A 1  1122 PHE 1122 1122 1122 PHE PHE A . n 
A 1  1123 GLU 1123 1123 1123 GLU GLU A . n 
A 1  1124 ARG 1124 1124 1124 ARG ARG A . n 
A 1  1125 LEU 1125 1125 1125 LEU LEU A . n 
A 1  1126 ILE 1126 1126 1126 ILE ILE A . n 
A 1  1127 LEU 1127 1127 1127 LEU LEU A . n 
A 1  1128 GLN 1128 1128 1128 GLN GLN A . n 
A 1  1129 TRP 1129 1129 1129 TRP TRP A . n 
A 1  1130 HIS 1130 1130 1130 HIS HIS A . n 
A 1  1131 LEU 1131 1131 1131 LEU LEU A . n 
A 1  1132 LEU 1132 1132 1132 LEU LEU A . n 
A 1  1133 TYR 1133 1133 ?    ?   ?   A . n 
A 1  1134 GLU 1134 1134 ?    ?   ?   A . n 
A 1  1135 THR 1135 1135 ?    ?   ?   A . n 
A 1  1136 TYR 1136 1136 ?    ?   ?   A . n 
A 1  1137 SER 1137 1137 ?    ?   ?   A . n 
A 1  1138 SER 1138 1138 ?    ?   ?   A . n 
A 1  1139 THR 1139 1139 ?    ?   ?   A . n 
A 1  1140 LYS 1140 1140 ?    ?   ?   A . n 
A 1  1141 LYS 1141 1141 ?    ?   ?   A . n 
A 1  1142 ASN 1142 1142 ?    ?   ?   A . n 
A 1  1143 VAL 1143 1143 1143 VAL VAL A . n 
A 1  1144 MET 1144 1144 1144 MET MET A . n 
A 1  1145 TYR 1145 1145 1145 TYR TYR A . n 
A 1  1146 PRO 1146 1146 1146 PRO PRO A . n 
A 1  1147 ASP 1147 1147 1147 ASP ASP A . n 
A 1  1148 PHE 1148 1148 1148 PHE PHE A . n 
A 1  1149 ALA 1149 1149 1149 ALA ALA A . n 
A 1  1150 SER 1150 1150 1150 SER SER A . n 
A 1  1151 ASP 1151 1151 1151 ASP ASP A . n 
A 1  1152 VAL 1152 1152 1152 VAL VAL A . n 
A 1  1153 GLU 1153 1153 1153 GLU GLU A . n 
A 1  1154 TRP 1154 1154 1154 TRP TRP A . n 
A 1  1155 MET 1155 1155 1155 MET MET A . n 
A 1  1156 THR 1156 1156 1156 THR THR A . n 
A 1  1157 ASP 1157 1157 1157 ASP ASP A . n 
A 1  1158 PHE 1158 1158 1158 PHE PHE A . n 
A 1  1159 LEU 1159 1159 1159 LEU LEU A . n 
A 1  1160 GLU 1160 1160 1160 GLU GLU A . n 
A 1  1161 ASN 1161 1161 1161 ASN ASN A . n 
A 1  1162 HIS 1162 1162 1162 HIS HIS A . n 
A 1  1163 PRO 1163 1163 1163 PRO PRO A . n 
A 1  1164 LEU 1164 1164 1164 LEU LEU A . n 
A 1  1165 LEU 1165 1165 1165 LEU LEU A . n 
A 1  1166 GLN 1166 1166 1166 GLN GLN A . n 
A 1  1167 PRO 1167 1167 1167 PRO PRO A . n 
A 1  1168 PRO 1168 1168 1168 PRO PRO A . n 
A 1  1169 GLU 1169 1169 1169 GLU GLU A . n 
A 1  1170 ASP 1170 1170 1170 ASP ASP A . n 
A 1  1171 ILE 1171 1171 1171 ILE ILE A . n 
A 1  1172 ALA 1172 1172 1172 ALA ALA A . n 
A 1  1173 ASN 1173 1173 1173 ASN ASN A . n 
A 1  1174 TRP 1174 1174 1174 TRP TRP A . n 
A 1  1175 CYS 1175 1175 1175 CYS CYS A . n 
A 1  1176 ILE 1176 1176 1176 ILE ILE A . n 
A 1  1177 ARG 1177 1177 1177 ARG ARG A . n 
A 1  1178 LEU 1178 1178 1178 LEU LEU A . n 
A 1  1179 GLU 1179 1179 1179 GLU GLU A . n 
A 1  1180 LEU 1180 1180 1180 LEU LEU A . n 
A 1  1181 ASN 1181 1181 1181 ASN ASN A . n 
A 1  1182 LYS 1182 1182 1182 LYS LYS A . n 
A 1  1183 THR 1183 1183 1183 THR THR A . n 
A 1  1184 THR 1184 1184 1184 THR THR A . n 
A 1  1185 MET 1185 1185 1185 MET MET A . n 
A 1  1186 ILE 1186 1186 1186 ILE ILE A . n 
A 1  1187 LEU 1187 1187 1187 LEU LEU A . n 
A 1  1188 LYS 1188 1188 1188 LYS LYS A . n 
A 1  1189 SER 1189 1189 1189 SER SER A . n 
A 1  1190 ILE 1190 1190 1190 ILE ILE A . n 
A 1  1191 SER 1191 1191 1191 SER SER A . n 
A 1  1192 LEU 1192 1192 1192 LEU LEU A . n 
A 1  1193 GLU 1193 1193 1193 GLU GLU A . n 
A 1  1194 SER 1194 1194 1194 SER SER A . n 
A 1  1195 ILE 1195 1195 1195 ILE ILE A . n 
A 1  1196 ILE 1196 1196 1196 ILE ILE A . n 
A 1  1197 ASN 1197 1197 1197 ASN ASN A . n 
A 1  1198 SER 1198 1198 1198 SER SER A . n 
A 1  1199 LEU 1199 1199 1199 LEU LEU A . n 
A 1  1200 ARG 1200 1200 1200 ARG ARG A . n 
A 1  1201 ALA 1201 1201 1201 ALA ALA A . n 
A 1  1202 LYS 1202 1202 1202 LYS LYS A . n 
A 1  1203 HIS 1203 1203 1203 HIS HIS A . n 
A 1  1204 PRO 1204 1204 1204 PRO PRO A . n 
A 1  1205 ASN 1205 1205 1205 ASN ASN A . n 
A 1  1206 THR 1206 1206 1206 THR THR A . n 
A 1  1207 TYR 1207 1207 1207 TYR TYR A . n 
A 1  1208 ILE 1208 1208 1208 ILE ILE A . n 
A 1  1209 MET 1209 1209 1209 MET MET A . n 
A 1  1210 HIS 1210 1210 1210 HIS HIS A . n 
A 1  1211 SER 1211 1211 1211 SER SER A . n 
A 1  1212 VAL 1212 1212 1212 VAL VAL A . n 
A 1  1213 GLU 1213 1213 ?    ?   ?   A . n 
A 1  1214 ASN 1214 1214 ?    ?   ?   A . n 
A 1  1215 THR 1215 1215 ?    ?   ?   A . n 
A 1  1216 ALA 1216 1216 ?    ?   ?   A . n 
A 1  1217 SER 1217 1217 ?    ?   ?   A . n 
A 1  1218 GLY 1218 1218 ?    ?   ?   A . n 
A 1  1219 ILE 1219 1219 ?    ?   ?   A . n 
A 1  1220 PRO 1220 1220 ?    ?   ?   A . n 
A 1  1221 ILE 1221 1221 1221 ILE ILE A . n 
A 1  1222 ILE 1222 1222 1222 ILE ILE A . n 
A 1  1223 ILE 1223 1223 1223 ILE ILE A . n 
A 1  1224 ARG 1224 1224 1224 ARG ARG A . n 
A 1  1225 ILE 1225 1225 1225 ILE ILE A . n 
A 1  1226 TYR 1226 1226 1226 TYR TYR A . n 
A 1  1227 LEU 1227 1227 1227 LEU LEU A . n 
A 1  1228 ARG 1228 1228 1228 ARG ARG A . n 
A 1  1229 GLU 1229 1229 1229 GLU GLU A . n 
A 1  1230 SER 1230 1230 1230 SER SER A . n 
A 1  1231 ALA 1231 1231 1231 ALA ALA A . n 
A 1  1232 PHE 1232 1232 1232 PHE PHE A . n 
A 1  1233 ARG 1233 1233 1233 ARG ARG A . n 
A 1  1234 ARG 1234 1234 1234 ARG ARG A . n 
A 1  1235 SER 1235 1235 1235 SER SER A . n 
A 1  1236 THR 1236 1236 1236 THR THR A . n 
A 1  1237 ASN 1237 1237 1237 ASN ASN A . n 
A 1  1238 THR 1238 1238 1238 THR THR A . n 
A 1  1239 ARG 1239 1239 1239 ARG ARG A . n 
A 1  1240 MET 1240 1240 1240 MET MET A . n 
A 1  1241 ALA 1241 1241 1241 ALA ALA A . n 
A 1  1242 THR 1242 1242 1242 THR THR A . n 
A 1  1243 ASP 1243 1243 1243 ASP ASP A . n 
A 1  1244 GLU 1244 1244 1244 GLU GLU A . n 
A 1  1245 LYS 1245 1245 1245 LYS LYS A . n 
A 1  1246 ILE 1246 1246 1246 ILE ILE A . n 
A 1  1247 ALA 1247 1247 1247 ALA ALA A . n 
A 1  1248 VAL 1248 1248 1248 VAL VAL A . n 
A 1  1249 ASN 1249 1249 1249 ASN ASN A . n 
A 1  1250 VAL 1250 1250 1250 VAL VAL A . n 
A 1  1251 VAL 1251 1251 1251 VAL VAL A . n 
A 1  1252 ASP 1252 1252 1252 ASP ASP A . n 
A 1  1253 LYS 1253 1253 1253 LYS LYS A . n 
A 1  1254 LEU 1254 1254 1254 LEU LEU A . n 
A 1  1255 LEU 1255 1255 1255 LEU LEU A . n 
A 1  1256 ASN 1256 1256 1256 ASN ASN A . n 
A 1  1257 SER 1257 1257 1257 SER SER A . n 
A 1  1258 THR 1258 1258 1258 THR THR A . n 
A 1  1259 ILE 1259 1259 1259 ILE ILE A . n 
A 1  1260 ARG 1260 1260 1260 ARG ARG A . n 
A 1  1261 GLY 1261 1261 1261 GLY GLY A . n 
A 1  1262 ILE 1262 1262 1262 ILE ILE A . n 
A 1  1263 PRO 1263 1263 1263 PRO PRO A . n 
A 1  1264 GLY 1264 1264 1264 GLY GLY A . n 
A 1  1265 ILE 1265 1265 1265 ILE ILE A . n 
A 1  1266 LYS 1266 1266 1266 LYS LYS A . n 
A 1  1267 ASN 1267 1267 1267 ASN ASN A . n 
A 1  1268 ALA 1268 1268 1268 ALA ALA A . n 
A 1  1269 ASN 1269 1269 1269 ASN ASN A . n 
A 1  1270 VAL 1270 1270 1270 VAL VAL A . n 
A 1  1271 VAL 1271 1271 1271 VAL VAL A . n 
A 1  1272 LYS 1272 1272 1272 LYS LYS A . n 
A 1  1273 LEU 1273 1273 1273 LEU LEU A . n 
A 1  1274 MET 1274 1274 1274 MET MET A . n 
A 1  1275 ARG 1275 1275 1275 ARG ARG A . n 
A 1  1276 HIS 1276 1276 1276 HIS HIS A . n 
A 1  1277 ARG 1277 1277 1277 ARG ARG A . n 
A 1  1278 VAL 1278 1278 1278 VAL VAL A . n 
A 1  1279 ASP 1279 1279 1279 ASP ASP A . n 
A 1  1280 ALA 1280 1280 1280 ALA ALA A . n 
A 1  1281 GLN 1281 1281 1281 GLN GLN A . n 
A 1  1282 GLY 1282 1282 1282 GLY GLY A . n 
A 1  1283 LYS 1283 1283 1283 LYS LYS A . n 
A 1  1284 LEU 1284 1284 1284 LEU LEU A . n 
A 1  1285 VAL 1285 1285 1285 VAL VAL A . n 
A 1  1286 ARG 1286 1286 1286 ARG ARG A . n 
A 1  1287 LEU 1287 1287 1287 LEU LEU A . n 
A 1  1288 ASP 1288 1288 1288 ASP ASP A . n 
A 1  1289 ASN 1289 1289 1289 ASN ASN A . n 
A 1  1290 ILE 1290 1290 1290 ILE ILE A . n 
A 1  1291 TYR 1291 1291 1291 TYR TYR A . n 
A 1  1292 ALA 1292 1292 1292 ALA ALA A . n 
A 1  1293 ILE 1293 1293 1293 ILE ILE A . n 
A 1  1294 LYS 1294 1294 1294 LYS LYS A . n 
A 1  1295 THR 1295 1295 1295 THR THR A . n 
A 1  1296 ASN 1296 1296 1296 ASN ASN A . n 
A 1  1297 GLY 1297 1297 1297 GLY GLY A . n 
A 1  1298 THR 1298 1298 1298 THR THR A . n 
A 1  1299 ASN 1299 1299 1299 ASN ASN A . n 
A 1  1300 ILE 1300 1300 1300 ILE ILE A . n 
A 1  1301 PHE 1301 1301 1301 PHE PHE A . n 
A 1  1302 GLY 1302 1302 1302 GLY GLY A . n 
A 1  1303 ALA 1303 1303 1303 ALA ALA A . n 
A 1  1304 MET 1304 1304 1304 MET MET A . n 
A 1  1305 LEU 1305 1305 1305 LEU LEU A . n 
A 1  1306 ASP 1306 1306 1306 ASP ASP A . n 
A 1  1307 ASP 1307 1307 1307 ASP ASP A . n 
A 1  1308 ASN 1308 1308 1308 ASN ASN A . n 
A 1  1309 ILE 1309 1309 1309 ILE ILE A . n 
A 1  1310 ASP 1310 1310 1310 ASP ASP A . n 
A 1  1311 PRO 1311 1311 1311 PRO PRO A . n 
A 1  1312 TYR 1312 1312 1312 TYR TYR A . n 
A 1  1313 THR 1313 1313 1313 THR THR A . n 
A 1  1314 ILE 1314 1314 1314 ILE ILE A . n 
A 1  1315 VAL 1315 1315 1315 VAL VAL A . n 
A 1  1316 SER 1316 1316 1316 SER SER A . n 
A 1  1317 SER 1317 1317 1317 SER SER A . n 
A 1  1318 SER 1318 1318 1318 SER SER A . n 
A 1  1319 ILE 1319 1319 1319 ILE ILE A . n 
A 1  1320 GLY 1320 1320 1320 GLY GLY A . n 
A 1  1321 ASP 1321 1321 1321 ASP ASP A . n 
A 1  1322 THR 1322 1322 1322 THR THR A . n 
A 1  1323 MET 1323 1323 1323 MET MET A . n 
A 1  1324 GLU 1324 1324 1324 GLU GLU A . n 
A 1  1325 LEU 1325 1325 1325 LEU LEU A . n 
A 1  1326 TYR 1326 1326 1326 TYR TYR A . n 
A 1  1327 GLY 1327 1327 1327 GLY GLY A . n 
A 1  1328 ILE 1328 1328 1328 ILE ILE A . n 
A 1  1329 GLU 1329 1329 1329 GLU GLU A . n 
A 1  1330 ALA 1330 1330 1330 ALA ALA A . n 
A 1  1331 ALA 1331 1331 1331 ALA ALA A . n 
A 1  1332 ARG 1332 1332 1332 ARG ARG A . n 
A 1  1333 GLN 1333 1333 1333 GLN GLN A . n 
A 1  1334 LYS 1334 1334 1334 LYS LYS A . n 
A 1  1335 ILE 1335 1335 1335 ILE ILE A . n 
A 1  1336 ILE 1336 1336 1336 ILE ILE A . n 
A 1  1337 SER 1337 1337 1337 SER SER A . n 
A 1  1338 GLU 1338 1338 1338 GLU GLU A . n 
A 1  1339 ILE 1339 1339 1339 ILE ILE A . n 
A 1  1340 ARG 1340 1340 1340 ARG ARG A . n 
A 1  1341 THR 1341 1341 1341 THR THR A . n 
A 1  1342 VAL 1342 1342 1342 VAL VAL A . n 
A 1  1343 MET 1343 1343 1343 MET MET A . n 
A 1  1344 GLY 1344 1344 1344 GLY GLY A . n 
A 1  1345 ASP 1345 1345 1345 ASP ASP A . n 
A 1  1346 LYS 1346 1346 1346 LYS LYS A . n 
A 1  1347 GLY 1347 1347 1347 GLY GLY A . n 
A 1  1348 PRO 1348 1348 1348 PRO PRO A . n 
A 1  1349 ASN 1349 1349 1349 ASN ASN A . n 
A 1  1350 HIS 1350 1350 1350 HIS HIS A . n 
A 1  1351 ARG 1351 1351 1351 ARG ARG A . n 
A 1  1352 HIS 1352 1352 1352 HIS HIS A . n 
A 1  1353 LEU 1353 1353 1353 LEU LEU A . n 
A 1  1354 LEU 1354 1354 1354 LEU LEU A . n 
A 1  1355 MET 1355 1355 1355 MET MET A . n 
A 1  1356 TYR 1356 1356 1356 TYR TYR A . n 
A 1  1357 ALA 1357 1357 1357 ALA ALA A . n 
A 1  1358 ASP 1358 1358 1358 ASP ASP A . n 
A 1  1359 LEU 1359 1359 1359 LEU LEU A . n 
A 1  1360 MET 1360 1360 1360 MET MET A . n 
A 1  1361 THR 1361 1361 1361 THR THR A . n 
A 1  1362 ARG 1362 1362 1362 ARG ARG A . n 
A 1  1363 THR 1363 1363 1363 THR THR A . n 
A 1  1364 GLY 1364 1364 1364 GLY GLY A . n 
A 1  1365 GLN 1365 1365 1365 GLN GLN A . n 
A 1  1366 VAL 1366 1366 1366 VAL VAL A . n 
A 1  1367 THR 1367 1367 1367 THR THR A . n 
A 1  1368 SER 1368 1368 1368 SER SER A . n 
A 1  1369 LEU 1369 1369 1369 LEU LEU A . n 
A 1  1370 GLU 1370 1370 1370 GLU GLU A . n 
A 1  1371 LYS 1371 1371 1371 LYS LYS A . n 
A 1  1372 ALA 1372 1372 1372 ALA ALA A . n 
A 1  1373 GLY 1373 1373 1373 GLY GLY A . n 
A 1  1374 LEU 1374 1374 1374 LEU LEU A . n 
A 1  1375 ASN 1375 1375 1375 ASN ASN A . n 
A 1  1376 ALA 1376 1376 1376 ALA ALA A . n 
A 1  1377 ARG 1377 1377 1377 ARG ARG A . n 
A 1  1378 GLU 1378 1378 1378 GLU GLU A . n 
A 1  1379 PRO 1379 1379 1379 PRO PRO A . n 
A 1  1380 SER 1380 1380 1380 SER SER A . n 
A 1  1381 ASN 1381 1381 1381 ASN ASN A . n 
A 1  1382 VAL 1382 1382 1382 VAL VAL A . n 
A 1  1383 LEU 1383 1383 1383 LEU LEU A . n 
A 1  1384 LEU 1384 1384 1384 LEU LEU A . n 
A 1  1385 ARG 1385 1385 1385 ARG ARG A . n 
A 1  1386 MET 1386 1386 1386 MET MET A . n 
A 1  1387 ALA 1387 1387 1387 ALA ALA A . n 
A 1  1388 LEU 1388 1388 1388 LEU LEU A . n 
A 1  1389 SER 1389 1389 1389 SER SER A . n 
A 1  1390 SER 1390 1390 1390 SER SER A . n 
A 1  1391 PRO 1391 1391 1391 PRO PRO A . n 
A 1  1392 VAL 1392 1392 1392 VAL VAL A . n 
A 1  1393 GLN 1393 1393 1393 GLN GLN A . n 
A 1  1394 VAL 1394 1394 1394 VAL VAL A . n 
A 1  1395 LEU 1395 1395 1395 LEU LEU A . n 
A 1  1396 THR 1396 1396 1396 THR THR A . n 
A 1  1397 ASP 1397 1397 1397 ASP ASP A . n 
A 1  1398 ALA 1398 1398 1398 ALA ALA A . n 
A 1  1399 ALA 1399 1399 1399 ALA ALA A . n 
A 1  1400 VAL 1400 1400 1400 VAL VAL A . n 
A 1  1401 ASP 1401 1401 1401 ASP ASP A . n 
A 1  1402 SER 1402 1402 1402 SER SER A . n 
A 1  1403 ALA 1403 1403 1403 ALA ALA A . n 
A 1  1404 VAL 1404 1404 1404 VAL VAL A . n 
A 1  1405 ASN 1405 1405 1405 ASN ASN A . n 
A 1  1406 PRO 1406 1406 1406 PRO PRO A . n 
A 1  1407 ILE 1407 1407 1407 ILE ILE A . n 
A 1  1408 TYR 1408 1408 1408 TYR TYR A . n 
A 1  1409 GLY 1409 1409 1409 GLY GLY A . n 
A 1  1410 ILE 1410 1410 1410 ILE ILE A . n 
A 1  1411 ALA 1411 1411 1411 ALA ALA A . n 
A 1  1412 ALA 1412 1412 1412 ALA ALA A . n 
A 1  1413 PRO 1413 1413 1413 PRO PRO A . n 
A 1  1414 THR 1414 1414 1414 THR THR A . n 
A 1  1415 LEU 1415 1415 1415 LEU LEU A . n 
A 1  1416 MET 1416 1416 1416 MET MET A . n 
A 1  1417 GLY 1417 1417 1417 GLY GLY A . n 
A 1  1418 SER 1418 1418 1418 SER SER A . n 
A 1  1419 VAL 1419 1419 1419 VAL VAL A . n 
A 1  1420 PRO 1420 1420 1420 PRO PRO A . n 
A 1  1421 ARG 1421 1421 1421 ARG ARG A . n 
A 1  1422 ILE 1422 1422 1422 ILE ILE A . n 
A 1  1423 GLY 1423 1423 1423 GLY GLY A . n 
A 1  1424 THR 1424 1424 1424 THR THR A . n 
A 1  1425 MET 1425 1425 1425 MET MET A . n 
A 1  1426 TYR 1426 1426 1426 TYR TYR A . n 
A 1  1427 SER 1427 1427 1427 SER SER A . n 
A 1  1428 ASP 1428 1428 1428 ASP ASP A . n 
A 1  1429 ILE 1429 1429 1429 ILE ILE A . n 
A 1  1430 ILE 1430 1430 1430 ILE ILE A . n 
A 1  1431 MET 1431 1431 1431 MET MET A . n 
A 1  1432 ASP 1432 1432 1432 ASP ASP A . n 
A 1  1433 GLU 1433 1433 1433 GLU GLU A . n 
A 1  1434 LYS 1434 1434 1434 LYS LYS A . n 
A 1  1435 TYR 1435 1435 1435 TYR TYR A . n 
A 1  1436 ILE 1436 1436 1436 ILE ILE A . n 
A 1  1437 THR 1437 1437 1437 THR THR A . n 
A 1  1438 GLU 1438 1438 1438 GLU GLU A . n 
A 1  1439 ASN 1439 1439 1439 ASN ASN A . n 
A 1  1440 TYR 1440 1440 1440 TYR TYR A . n 
A 1  1441 LYS 1441 1441 1441 LYS LYS A . n 
A 1  1442 SER 1442 1442 1442 SER SER A . n 
A 1  1443 VAL 1443 1443 ?    ?   ?   A . n 
A 1  1444 ASP 1444 1444 ?    ?   ?   A . n 
A 1  1445 SER 1445 1445 ?    ?   ?   A . n 
A 1  1446 LEU 1446 1446 ?    ?   ?   A . n 
A 1  1447 ILE 1447 1447 ?    ?   ?   A . n 
A 1  1448 ASP 1448 1448 ?    ?   ?   A . n 
A 1  1449 MET 1449 1449 ?    ?   ?   A . n 
A 1  1450 LEU 1450 1450 ?    ?   ?   A . n 
B 2  1    MET 1    1    ?    ?   ?   B . n 
B 2  2    GLU 2    2    ?    ?   ?   B . n 
B 2  3    PRO 3    3    ?    ?   ?   B . n 
B 2  4    LEU 4    4    ?    ?   ?   B . n 
B 2  5    ARG 5    5    ?    ?   ?   B . n 
B 2  6    PRO 6    6    ?    ?   ?   B . n 
B 2  7    GLN 7    7    ?    ?   ?   B . n 
B 2  8    ILE 8    8    8    ILE ILE B . n 
B 2  9    THR 9    9    9    THR THR B . n 
B 2  10   TYR 10   10   10   TYR TYR B . n 
B 2  11   GLY 11   11   11   GLY GLY B . n 
B 2  12   PRO 12   12   12   PRO PRO B . n 
B 2  13   ILE 13   13   13   ILE ILE B . n 
B 2  14   GLU 14   14   14   GLU GLU B . n 
B 2  15   THR 15   15   15   THR THR B . n 
B 2  16   VAL 16   16   16   VAL VAL B . n 
B 2  17   ASP 17   17   17   ASP ASP B . n 
B 2  18   ASN 18   18   18   ASN ASN B . n 
B 2  19   GLU 19   19   19   GLU GLU B . n 
B 2  20   GLU 20   20   20   GLU GLU B . n 
B 2  21   LEU 21   21   21   LEU LEU B . n 
B 2  22   THR 22   22   22   THR THR B . n 
B 2  23   GLU 23   23   23   GLU GLU B . n 
B 2  24   ALA 24   24   24   ALA ALA B . n 
B 2  25   ASP 25   25   25   ASP ASP B . n 
B 2  26   MET 26   26   26   MET MET B . n 
B 2  27   LEU 27   27   27   LEU LEU B . n 
B 2  28   SER 28   28   28   SER SER B . n 
B 2  29   PHE 29   29   29   PHE PHE B . n 
B 2  30   ILE 30   30   30   ILE ILE B . n 
B 2  31   SER 31   31   31   SER SER B . n 
B 2  32   ALA 32   32   32   ALA ALA B . n 
B 2  33   ALA 33   33   33   ALA ALA B . n 
B 2  34   VAL 34   34   34   VAL VAL B . n 
B 2  35   ASN 35   35   35   ASN ASN B . n 
B 2  36   SER 36   36   36   SER SER B . n 
B 2  37   THR 37   37   37   THR THR B . n 
B 2  38   GLY 38   38   38   GLY GLY B . n 
B 2  39   LEU 39   39   39   LEU LEU B . n 
B 2  40   ILE 40   40   40   ILE ILE B . n 
B 2  41   GLY 41   41   41   GLY GLY B . n 
B 2  42   TYR 42   42   42   TYR TYR B . n 
B 2  43   ASN 43   43   43   ASN ASN B . n 
B 2  44   ILE 44   44   44   ILE ILE B . n 
B 2  45   LYS 45   45   45   LYS LYS B . n 
B 2  46   SER 46   46   46   SER SER B . n 
B 2  47   PHE 47   47   47   PHE PHE B . n 
B 2  48   ASP 48   48   48   ASP ASP B . n 
B 2  49   ASP 49   49   49   ASP ASP B . n 
B 2  50   LEU 50   50   50   LEU LEU B . n 
B 2  51   MET 51   51   51   MET MET B . n 
B 2  52   ASP 52   52   52   ASP ASP B . n 
B 2  53   ASN 53   53   53   ASN ASN B . n 
B 2  54   GLY 54   54   54   GLY GLY B . n 
B 2  55   ILE 55   55   55   ILE ILE B . n 
B 2  56   PRO 56   56   56   PRO PRO B . n 
B 2  57   GLN 57   57   57   GLN GLN B . n 
B 2  58   ILE 58   58   58   ILE ILE B . n 
B 2  59   VAL 59   59   59   VAL VAL B . n 
B 2  60   LYS 60   60   60   LYS LYS B . n 
B 2  61   GLN 61   61   61   GLN GLN B . n 
B 2  62   MET 62   62   62   MET MET B . n 
B 2  63   PHE 63   63   63   PHE PHE B . n 
B 2  64   ASN 64   64   64   ASN ASN B . n 
B 2  65   VAL 65   65   65   VAL VAL B . n 
B 2  66   ASP 66   66   66   ASP ASP B . n 
B 2  67   ILE 67   67   67   ILE ILE B . n 
B 2  68   THR 68   68   68   THR THR B . n 
B 2  69   TYR 69   69   69   TYR TYR B . n 
B 2  70   LYS 70   70   70   LYS LYS B . n 
B 2  71   ASP 71   71   71   ASP ASP B . n 
B 2  72   GLN 72   72   72   GLN GLN B . n 
B 2  73   ARG 73   73   73   ARG ARG B . n 
B 2  74   ASP 74   74   74   ASP ASP B . n 
B 2  75   HIS 75   75   75   HIS HIS B . n 
B 2  76   THR 76   76   76   THR THR B . n 
B 2  77   GLU 77   77   77   GLU GLU B . n 
B 2  78   ILE 78   78   78   ILE ILE B . n 
B 2  79   ASP 79   79   79   ASP ASP B . n 
B 2  80   LYS 80   80   80   LYS LYS B . n 
B 2  81   LEU 81   81   81   LEU LEU B . n 
B 2  82   ARG 82   82   82   ARG ARG B . n 
B 2  83   GLU 83   83   83   GLU GLU B . n 
B 2  84   SER 84   84   84   SER SER B . n 
B 2  85   VAL 85   85   85   VAL VAL B . n 
B 2  86   GLN 86   86   86   GLN GLN B . n 
B 2  87   ILE 87   87   87   ILE ILE B . n 
B 2  88   GLN 88   88   88   GLN GLN B . n 
B 2  89   PHE 89   89   89   PHE PHE B . n 
B 2  90   ASN 90   90   90   ASN ASN B . n 
B 2  91   PHE 91   91   91   PHE PHE B . n 
B 2  92   THR 92   92   92   THR THR B . n 
B 2  93   ASP 93   93   93   ASP ASP B . n 
B 2  94   VAL 94   94   94   VAL VAL B . n 
B 2  95   ASN 95   95   95   ASN ASN B . n 
B 2  96   ILE 96   96   96   ILE ILE B . n 
B 2  97   GLU 97   97   97   GLU GLU B . n 
B 2  98   ARG 98   98   98   ARG ARG B . n 
B 2  99   PRO 99   99   99   PRO PRO B . n 
B 2  100  GLN 100  100  100  GLN GLN B . n 
B 2  101  HIS 101  101  101  HIS HIS B . n 
B 2  102  ARG 102  102  102  ARG ARG B . n 
B 2  103  ASN 103  103  103  ASN ASN B . n 
B 2  104  TYR 104  104  104  TYR TYR B . n 
B 2  105  SER 105  105  105  SER SER B . n 
B 2  106  GLN 106  106  106  GLN GLN B . n 
B 2  107  GLY 107  107  107  GLY GLY B . n 
B 2  108  ASN 108  108  108  ASN ASN B . n 
B 2  109  LYS 109  109  109  LYS LYS B . n 
B 2  110  ILE 110  110  110  ILE ILE B . n 
B 2  111  ASN 111  111  111  ASN ASN B . n 
B 2  112  LEU 112  112  112  LEU LEU B . n 
B 2  113  LEU 113  113  113  LEU LEU B . n 
B 2  114  PRO 114  114  114  PRO PRO B . n 
B 2  115  ASN 115  115  115  ASN ASN B . n 
B 2  116  LYS 116  116  116  LYS LYS B . n 
B 2  117  ALA 117  117  117  ALA ALA B . n 
B 2  118  ARG 118  118  118  ARG ARG B . n 
B 2  119  LEU 119  119  119  LEU LEU B . n 
B 2  120  CYS 120  120  120  CYS CYS B . n 
B 2  121  GLY 121  121  121  GLY GLY B . n 
B 2  122  LEU 122  122  122  LEU LEU B . n 
B 2  123  SER 123  123  123  SER SER B . n 
B 2  124  TYR 124  124  124  TYR TYR B . n 
B 2  125  SER 125  125  125  SER SER B . n 
B 2  126  GLY 126  126  126  GLY GLY B . n 
B 2  127  PRO 127  127  127  PRO PRO B . n 
B 2  128  VAL 128  128  128  VAL VAL B . n 
B 2  129  ASN 129  129  129  ASN ASN B . n 
B 2  130  LEU 130  130  130  LEU LEU B . n 
B 2  131  ALA 131  131  131  ALA ALA B . n 
B 2  132  ALA 132  132  132  ALA ALA B . n 
B 2  133  GLU 133  133  133  GLU GLU B . n 
B 2  134  VAL 134  134  134  VAL VAL B . n 
B 2  135  ILE 135  135  135  ILE ILE B . n 
B 2  136  LEU 136  136  136  LEU LEU B . n 
B 2  137  THR 137  137  137  THR THR B . n 
B 2  138  ALA 138  138  138  ALA ALA B . n 
B 2  139  HIS 139  139  139  HIS HIS B . n 
B 2  140  TYR 140  140  140  TYR TYR B . n 
B 2  141  SER 141  141  141  SER SER B . n 
B 2  142  ASN 142  142  142  ASN ASN B . n 
B 2  143  GLY 143  143  143  GLY GLY B . n 
B 2  144  ARG 144  144  144  ARG ARG B . n 
B 2  145  GLN 145  145  145  GLN GLN B . n 
B 2  146  GLU 146  146  146  GLU GLU B . n 
B 2  147  VAL 147  147  147  VAL VAL B . n 
B 2  148  LYS 148  148  148  LYS LYS B . n 
B 2  149  ARG 149  149  149  ARG ARG B . n 
B 2  150  ALA 150  150  150  ALA ALA B . n 
B 2  151  SER 151  151  151  SER SER B . n 
B 2  152  ILE 152  152  152  ILE ILE B . n 
B 2  153  PRO 153  153  153  PRO PRO B . n 
B 2  154  PRO 154  154  154  PRO PRO B . n 
B 2  155  PHE 155  155  155  PHE PHE B . n 
B 2  156  GLN 156  156  156  GLN GLN B . n 
B 2  157  VAL 157  157  157  VAL VAL B . n 
B 2  158  SER 158  158  158  SER SER B . n 
B 2  159  THR 159  159  159  THR THR B . n 
B 2  160  PHE 160  160  160  PHE PHE B . n 
B 2  161  PRO 161  161  161  PRO PRO B . n 
B 2  162  ILE 162  162  162  ILE ILE B . n 
B 2  163  MET 163  163  163  MET MET B . n 
B 2  164  ARG 164  164  164  ARG ARG B . n 
B 2  165  GLY 165  165  165  GLY GLY B . n 
B 2  166  SER 166  166  166  SER SER B . n 
B 2  167  ASN 167  167  167  ASN ASN B . n 
B 2  168  ARG 168  168  168  ARG ARG B . n 
B 2  169  CYS 169  169  169  CYS CYS B . n 
B 2  170  HIS 170  170  170  HIS HIS B . n 
B 2  171  THR 171  171  171  THR THR B . n 
B 2  172  HIS 172  172  172  HIS HIS B . n 
B 2  173  HIS 173  173  173  HIS HIS B . n 
B 2  174  LEU 174  174  174  LEU LEU B . n 
B 2  175  SER 175  175  175  SER SER B . n 
B 2  176  LYS 176  176  176  LYS LYS B . n 
B 2  177  THR 177  177  177  THR THR B . n 
B 2  178  ALA 178  178  178  ALA ALA B . n 
B 2  179  LYS 179  179  179  LYS LYS B . n 
B 2  180  LYS 180  180  180  LYS LYS B . n 
B 2  181  GLU 181  181  181  GLU GLU B . n 
B 2  182  ILE 182  182  182  ILE ILE B . n 
B 2  183  GLY 183  183  183  GLY GLY B . n 
B 2  184  GLU 184  184  184  GLU GLU B . n 
B 2  185  ASP 185  185  185  ASP ASP B . n 
B 2  186  PRO 186  186  186  PRO PRO B . n 
B 2  187  ASN 187  187  187  ASN ASN B . n 
B 2  188  GLU 188  188  188  GLU GLU B . n 
B 2  189  PRO 189  189  189  PRO PRO B . n 
B 2  190  GLY 190  190  190  GLY GLY B . n 
B 2  191  GLY 191  191  191  GLY GLY B . n 
B 2  192  TYR 192  192  192  TYR TYR B . n 
B 2  193  PHE 193  193  193  PHE PHE B . n 
B 2  194  ILE 194  194  194  ILE ILE B . n 
B 2  195  ALA 195  195  195  ALA ALA B . n 
B 2  196  ARG 196  196  196  ARG ARG B . n 
B 2  197  GLY 197  197  197  GLY GLY B . n 
B 2  198  GLY 198  198  198  GLY GLY B . n 
B 2  199  GLU 199  199  199  GLU GLU B . n 
B 2  200  TRP 200  200  200  TRP TRP B . n 
B 2  201  VAL 201  201  201  VAL VAL B . n 
B 2  202  VAL 202  202  202  VAL VAL B . n 
B 2  203  ASP 203  203  203  ASP ASP B . n 
B 2  204  LEU 204  204  204  LEU LEU B . n 
B 2  205  LEU 205  205  205  LEU LEU B . n 
B 2  206  GLU 206  206  206  GLU GLU B . n 
B 2  207  ASN 207  207  207  ASN ASN B . n 
B 2  208  ILE 208  208  208  ILE ILE B . n 
B 2  209  ARG 209  209  209  ARG ARG B . n 
B 2  210  PHE 210  210  210  PHE PHE B . n 
B 2  211  ASN 211  211  211  ASN ASN B . n 
B 2  212  THR 212  212  212  THR THR B . n 
B 2  213  LEU 213  213  213  LEU LEU B . n 
B 2  214  HIS 214  214  214  HIS HIS B . n 
B 2  215  ILE 215  215  215  ILE ILE B . n 
B 2  216  HIS 216  216  216  HIS HIS B . n 
B 2  217  TYR 217  217  217  TYR TYR B . n 
B 2  218  HIS 218  218  ?    ?   ?   B . n 
B 2  219  THR 219  219  ?    ?   ?   B . n 
B 2  220  MET 220  220  ?    ?   ?   B . n 
B 2  221  GLN 221  221  ?    ?   ?   B . n 
B 2  222  GLN 222  222  ?    ?   ?   B . n 
B 2  223  GLY 223  223  ?    ?   ?   B . n 
B 2  224  ASN 224  224  ?    ?   ?   B . n 
B 2  225  ASN 225  225  225  ASN ASN B . n 
B 2  226  GLU 226  226  226  GLU GLU B . n 
B 2  227  ILE 227  227  227  ILE ILE B . n 
B 2  228  ILE 228  228  228  ILE ILE B . n 
B 2  229  ARG 229  229  229  ARG ARG B . n 
B 2  230  GLY 230  230  230  GLY GLY B . n 
B 2  231  GLU 231  231  231  GLU GLU B . n 
B 2  232  PHE 232  232  232  PHE PHE B . n 
B 2  233  ILE 233  233  233  ILE ILE B . n 
B 2  234  SER 234  234  234  SER SER B . n 
B 2  235  GLN 235  235  235  GLN GLN B . n 
B 2  236  PRO 236  236  236  PRO PRO B . n 
B 2  237  GLY 237  237  237  GLY GLY B . n 
B 2  238  GLY 238  238  238  GLY GLY B . n 
B 2  239  ALA 239  239  239  ALA ALA B . n 
B 2  240  PHE 240  240  240  PHE PHE B . n 
B 2  241  GLU 241  241  241  GLU GLU B . n 
B 2  242  ASN 242  242  242  ASN ASN B . n 
B 2  243  SER 243  243  243  SER SER B . n 
B 2  244  SER 244  244  244  SER SER B . n 
B 2  245  GLN 245  245  245  GLN GLN B . n 
B 2  246  ILE 246  246  246  ILE ILE B . n 
B 2  247  ILE 247  247  247  ILE ILE B . n 
B 2  248  ILE 248  248  248  ILE ILE B . n 
B 2  249  ARG 249  249  249  ARG ARG B . n 
B 2  250  TYR 250  250  250  TYR TYR B . n 
B 2  251  MET 251  251  251  MET MET B . n 
B 2  252  THR 252  252  252  THR THR B . n 
B 2  253  THR 253  253  253  THR THR B . n 
B 2  254  GLY 254  254  254  GLY GLY B . n 
B 2  255  ALA 255  255  255  ALA ALA B . n 
B 2  256  ILE 256  256  256  ILE ILE B . n 
B 2  257  THR 257  257  257  THR THR B . n 
B 2  258  ILE 258  258  258  ILE ILE B . n 
B 2  259  GLU 259  259  259  GLU GLU B . n 
B 2  260  ILE 260  260  260  ILE ILE B . n 
B 2  261  ASN 261  261  261  ASN ASN B . n 
B 2  262  SER 262  262  262  SER SER B . n 
B 2  263  THR 263  263  263  THR THR B . n 
B 2  264  LYS 264  264  264  LYS LYS B . n 
B 2  265  PHE 265  265  265  PHE PHE B . n 
B 2  266  SER 266  266  266  SER SER B . n 
B 2  267  LYS 267  267  267  LYS LYS B . n 
B 2  268  LEU 268  268  268  LEU LEU B . n 
B 2  269  ARG 269  269  269  ARG ARG B . n 
B 2  270  ILE 270  270  270  ILE ILE B . n 
B 2  271  PRO 271  271  271  PRO PRO B . n 
B 2  272  TRP 272  272  272  TRP TRP B . n 
B 2  273  TYR 273  273  273  TYR TYR B . n 
B 2  274  LEU 274  274  274  LEU LEU B . n 
B 2  275  ILE 275  275  275  ILE ILE B . n 
B 2  276  PHE 276  276  276  PHE PHE B . n 
B 2  277  ARG 277  277  277  ARG ARG B . n 
B 2  278  MET 278  278  278  MET MET B . n 
B 2  279  PHE 279  279  279  PHE PHE B . n 
B 2  280  GLY 280  280  280  GLY GLY B . n 
B 2  281  MET 281  281  281  MET MET B . n 
B 2  282  THR 282  282  282  THR THR B . n 
B 2  283  GLY 283  283  283  GLY GLY B . n 
B 2  284  ASP 284  284  284  ASP ASP B . n 
B 2  285  ASP 285  285  285  ASP ASP B . n 
B 2  286  SER 286  286  286  SER SER B . n 
B 2  287  ILE 287  287  287  ILE ILE B . n 
B 2  288  ILE 288  288  288  ILE ILE B . n 
B 2  289  GLU 289  289  289  GLU GLU B . n 
B 2  290  GLN 290  290  290  GLN GLN B . n 
B 2  291  VAL 291  291  291  VAL VAL B . n 
B 2  292  VAL 292  292  292  VAL VAL B . n 
B 2  293  PHE 293  293  293  PHE PHE B . n 
B 2  294  ASP 294  294  294  ASP ASP B . n 
B 2  295  LEU 295  295  295  LEU LEU B . n 
B 2  296  GLU 296  296  296  GLU GLU B . n 
B 2  297  SER 297  297  297  SER SER B . n 
B 2  298  ASN 298  298  298  ASN ASN B . n 
B 2  299  SER 299  299  299  SER SER B . n 
B 2  300  LEU 300  300  300  LEU LEU B . n 
B 2  301  VAL 301  301  301  VAL VAL B . n 
B 2  302  ASN 302  302  302  ASN ASN B . n 
B 2  303  THR 303  303  303  THR THR B . n 
B 2  304  PHE 304  304  304  PHE PHE B . n 
B 2  305  MET 305  305  305  MET MET B . n 
B 2  306  ILE 306  306  306  ILE ILE B . n 
B 2  307  GLU 307  307  307  GLU GLU B . n 
B 2  308  ILE 308  308  308  ILE ILE B . n 
B 2  309  LEU 309  309  309  LEU LEU B . n 
B 2  310  GLU 310  310  310  GLU GLU B . n 
B 2  311  LYS 311  311  311  LYS LYS B . n 
B 2  312  SER 312  312  312  SER SER B . n 
B 2  313  ILE 313  313  313  ILE ILE B . n 
B 2  314  HIS 314  314  314  HIS HIS B . n 
B 2  315  VAL 315  315  315  VAL VAL B . n 
B 2  316  LEU 316  316  316  LEU LEU B . n 
B 2  317  ASP 317  317  317  ASP ASP B . n 
B 2  318  PRO 318  318  318  PRO PRO B . n 
B 2  319  ILE 319  319  319  ILE ILE B . n 
B 2  320  PHE 320  320  320  PHE PHE B . n 
B 2  321  GLN 321  321  321  GLN GLN B . n 
B 2  322  PRO 322  322  322  PRO PRO B . n 
B 2  323  VAL 323  323  323  VAL VAL B . n 
B 2  324  GLN 324  324  324  GLN GLN B . n 
B 2  325  HIS 325  325  325  HIS HIS B . n 
B 2  326  GLU 326  326  326  GLU GLU B . n 
B 2  327  LEU 327  327  327  LEU LEU B . n 
B 2  328  ASN 328  328  328  ASN ASN B . n 
B 2  329  ARG 329  329  329  ARG ARG B . n 
B 2  330  GLU 330  330  330  GLU GLU B . n 
B 2  331  LYS 331  331  331  LYS LYS B . n 
B 2  332  ILE 332  332  332  ILE ILE B . n 
B 2  333  ILE 333  333  333  ILE ILE B . n 
B 2  334  GLN 334  334  334  GLN GLN B . n 
B 2  335  PHE 335  335  335  PHE PHE B . n 
B 2  336  LEU 336  336  336  LEU LEU B . n 
B 2  337  SER 337  337  337  SER SER B . n 
B 2  338  GLU 338  338  338  GLU GLU B . n 
B 2  339  LYS 339  339  339  LYS LYS B . n 
B 2  340  VAL 340  340  340  VAL VAL B . n 
B 2  341  SER 341  341  341  SER SER B . n 
B 2  342  LYS 342  342  342  LYS LYS B . n 
B 2  343  PHE 343  343  343  PHE PHE B . n 
B 2  344  VAL 344  344  344  VAL VAL B . n 
B 2  345  SER 345  345  345  SER SER B . n 
B 2  346  ASN 346  346  346  ASN ASN B . n 
B 2  347  PRO 347  347  347  PRO PRO B . n 
B 2  348  SER 348  348  348  SER SER B . n 
B 2  349  ALA 349  349  349  ALA ALA B . n 
B 2  350  TYR 350  350  350  TYR TYR B . n 
B 2  351  LYS 351  351  351  LYS LYS B . n 
B 2  352  SER 352  352  352  SER SER B . n 
B 2  353  ASP 353  353  353  ASP ASP B . n 
B 2  354  GLU 354  354  354  GLU GLU B . n 
B 2  355  ASN 355  355  355  ASN ASN B . n 
B 2  356  ALA 356  356  356  ALA ALA B . n 
B 2  357  VAL 357  357  357  VAL VAL B . n 
B 2  358  GLN 358  358  358  GLN GLN B . n 
B 2  359  TYR 359  359  359  TYR TYR B . n 
B 2  360  LEU 360  360  360  LEU LEU B . n 
B 2  361  ASN 361  361  361  ASN ASN B . n 
B 2  362  GLU 362  362  362  GLU GLU B . n 
B 2  363  ARG 363  363  363  ARG ARG B . n 
B 2  364  GLN 364  364  364  GLN GLN B . n 
B 2  365  LEU 365  365  365  LEU LEU B . n 
B 2  366  THR 366  366  366  THR THR B . n 
B 2  367  ILE 367  367  367  ILE ILE B . n 
B 2  368  LEU 368  368  368  LEU LEU B . n 
B 2  369  ASP 369  369  369  ASP ASP B . n 
B 2  370  LYS 370  370  370  LYS LYS B . n 
B 2  371  ILE 371  371  371  ILE ILE B . n 
B 2  372  LEU 372  372  372  LEU LEU B . n 
B 2  373  LEU 373  373  373  LEU LEU B . n 
B 2  374  PRO 374  374  374  PRO PRO B . n 
B 2  375  HIS 375  375  375  HIS HIS B . n 
B 2  376  MET 376  376  376  MET MET B . n 
B 2  377  GLY 377  377  377  GLY GLY B . n 
B 2  378  GLN 378  378  378  GLN GLN B . n 
B 2  379  THR 379  379  379  THR THR B . n 
B 2  380  ALA 380  380  380  ALA ALA B . n 
B 2  381  ASP 381  381  381  ASP ASP B . n 
B 2  382  THR 382  382  382  THR THR B . n 
B 2  383  ARG 383  383  383  ARG ARG B . n 
B 2  384  VAL 384  384  384  VAL VAL B . n 
B 2  385  ARG 385  385  385  ARG ARG B . n 
B 2  386  LYS 386  386  386  LYS LYS B . n 
B 2  387  LEU 387  387  387  LEU LEU B . n 
B 2  388  ARG 388  388  388  ARG ARG B . n 
B 2  389  PHE 389  389  389  PHE PHE B . n 
B 2  390  LEU 390  390  390  LEU LEU B . n 
B 2  391  GLY 391  391  391  GLY GLY B . n 
B 2  392  LEU 392  392  392  LEU LEU B . n 
B 2  393  LEU 393  393  393  LEU LEU B . n 
B 2  394  ILE 394  394  394  ILE ILE B . n 
B 2  395  HIS 395  395  395  HIS HIS B . n 
B 2  396  LYS 396  396  396  LYS LYS B . n 
B 2  397  ILE 397  397  397  ILE ILE B . n 
B 2  398  LEU 398  398  398  LEU LEU B . n 
B 2  399  LEU 399  399  399  LEU LEU B . n 
B 2  400  VAL 400  400  400  VAL VAL B . n 
B 2  401  ILE 401  401  401  ILE ILE B . n 
B 2  402  MET 402  402  402  MET MET B . n 
B 2  403  ASN 403  403  403  ASN ASN B . n 
B 2  404  VAL 404  404  404  VAL VAL B . n 
B 2  405  PHE 405  405  405  PHE PHE B . n 
B 2  406  PRO 406  406  406  PRO PRO B . n 
B 2  407  PRO 407  407  407  PRO PRO B . n 
B 2  408  THR 408  408  408  THR THR B . n 
B 2  409  ASP 409  409  409  ASP ASP B . n 
B 2  410  ARG 410  410  410  ARG ARG B . n 
B 2  411  ASP 411  411  411  ASP ASP B . n 
B 2  412  SER 412  412  412  SER SER B . n 
B 2  413  TYR 413  413  413  TYR TYR B . n 
B 2  414  ARG 414  414  414  ARG ARG B . n 
B 2  415  THR 415  415  415  THR THR B . n 
B 2  416  LYS 416  416  416  LYS LYS B . n 
B 2  417  ARG 417  417  417  ARG ARG B . n 
B 2  418  VAL 418  418  418  VAL VAL B . n 
B 2  419  HIS 419  419  419  HIS HIS B . n 
B 2  420  GLY 420  420  420  GLY GLY B . n 
B 2  421  SER 421  421  421  SER SER B . n 
B 2  422  GLY 422  422  422  GLY GLY B . n 
B 2  423  VAL 423  423  423  VAL VAL B . n 
B 2  424  SER 424  424  424  SER SER B . n 
B 2  425  LEU 425  425  425  LEU LEU B . n 
B 2  426  ALA 426  426  426  ALA ALA B . n 
B 2  427  LYS 427  427  427  LYS LYS B . n 
B 2  428  ALA 428  428  428  ALA ALA B . n 
B 2  429  PHE 429  429  429  PHE PHE B . n 
B 2  430  LYS 430  430  430  LYS LYS B . n 
B 2  431  ALA 431  431  431  ALA ALA B . n 
B 2  432  ILE 432  432  432  ILE ILE B . n 
B 2  433  PHE 433  433  433  PHE PHE B . n 
B 2  434  ASN 434  434  434  ASN ASN B . n 
B 2  435  THR 435  435  435  THR THR B . n 
B 2  436  SER 436  436  436  SER SER B . n 
B 2  437  VAL 437  437  437  VAL VAL B . n 
B 2  438  ILE 438  438  438  ILE ILE B . n 
B 2  439  ALA 439  439  439  ALA ALA B . n 
B 2  440  PRO 440  440  440  PRO PRO B . n 
B 2  441  ILE 441  441  441  ILE ILE B . n 
B 2  442  ILE 442  442  442  ILE ILE B . n 
B 2  443  ASN 443  443  443  ASN ASN B . n 
B 2  444  GLY 444  444  444  GLY GLY B . n 
B 2  445  PHE 445  445  445  PHE PHE B . n 
B 2  446  LYS 446  446  446  LYS LYS B . n 
B 2  447  GLU 447  447  447  GLU GLU B . n 
B 2  448  LEU 448  448  448  LEU LEU B . n 
B 2  449  LEU 449  449  449  LEU LEU B . n 
B 2  450  LYS 450  450  450  LYS LYS B . n 
B 2  451  GLN 451  451  451  GLN GLN B . n 
B 2  452  THR 452  452  452  THR THR B . n 
B 2  453  ALA 453  453  453  ALA ALA B . n 
B 2  454  PHE 454  454  454  PHE PHE B . n 
B 2  455  GLU 455  455  455  GLU GLU B . n 
B 2  456  GLU 456  456  456  GLU GLU B . n 
B 2  457  LEU 457  457  457  LEU LEU B . n 
B 2  458  THR 458  458  458  THR THR B . n 
B 2  459  GLN 459  459  459  GLN GLN B . n 
B 2  460  ARG 460  460  460  ARG ARG B . n 
B 2  461  ASN 461  461  461  ASN ASN B . n 
B 2  462  ILE 462  462  462  ILE ILE B . n 
B 2  463  ILE 463  463  463  ILE ILE B . n 
B 2  464  GLU 464  464  464  GLU GLU B . n 
B 2  465  ALA 465  465  465  ALA ALA B . n 
B 2  466  PHE 466  466  466  PHE PHE B . n 
B 2  467  SER 467  467  467  SER SER B . n 
B 2  468  ALA 468  468  468  ALA ALA B . n 
B 2  469  ALA 469  469  469  ALA ALA B . n 
B 2  470  LEU 470  470  470  LEU LEU B . n 
B 2  471  SER 471  471  471  SER SER B . n 
B 2  472  LYS 472  472  472  LYS LYS B . n 
B 2  473  ASN 473  473  473  ASN ASN B . n 
B 2  474  THR 474  474  474  THR THR B . n 
B 2  475  ALA 475  475  475  ALA ALA B . n 
B 2  476  SER 476  476  476  SER SER B . n 
B 2  477  ASP 477  477  477  ASP ASP B . n 
B 2  478  LEU 478  478  478  LEU LEU B . n 
B 2  479  ASN 479  479  479  ASN ASN B . n 
B 2  480  ARG 480  480  480  ARG ARG B . n 
B 2  481  SER 481  481  481  SER SER B . n 
B 2  482  MET 482  482  482  MET MET B . n 
B 2  483  GLU 483  483  483  GLU GLU B . n 
B 2  484  GLN 484  484  484  GLN GLN B . n 
B 2  485  SER 485  485  485  SER SER B . n 
B 2  486  ILE 486  486  486  ILE ILE B . n 
B 2  487  ILE 487  487  487  ILE ILE B . n 
B 2  488  SER 488  488  488  SER SER B . n 
B 2  489  GLY 489  489  489  GLY GLY B . n 
B 2  490  ASN 490  490  ?    ?   ?   B . n 
B 2  491  LYS 491  491  ?    ?   ?   B . n 
B 2  492  THR 492  492  ?    ?   ?   B . n 
B 2  493  ILE 493  493  ?    ?   ?   B . n 
B 2  494  MET 494  494  ?    ?   ?   B . n 
B 2  495  VAL 495  495  ?    ?   ?   B . n 
B 2  496  ARG 496  496  ?    ?   ?   B . n 
B 2  497  GLN 497  497  ?    ?   ?   B . n 
B 2  498  ARG 498  498  ?    ?   ?   B . n 
B 2  499  PRO 499  499  ?    ?   ?   B . n 
B 2  500  ILE 500  500  ?    ?   ?   B . n 
B 2  501  VAL 501  501  ?    ?   ?   B . n 
B 2  502  ASN 502  502  ?    ?   ?   B . n 
B 2  503  ARG 503  503  ?    ?   ?   B . n 
B 2  504  VAL 504  504  504  VAL VAL B . n 
B 2  505  SER 505  505  505  SER SER B . n 
B 2  506  THR 506  506  506  THR THR B . n 
B 2  507  GLN 507  507  507  GLN GLN B . n 
B 2  508  SER 508  508  508  SER SER B . n 
B 2  509  LEU 509  509  509  LEU LEU B . n 
B 2  510  GLU 510  510  510  GLU GLU B . n 
B 2  511  ARG 511  511  511  ARG ARG B . n 
B 2  512  LYS 512  512  512  LYS LYS B . n 
B 2  513  ASN 513  513  513  ASN ASN B . n 
B 2  514  LEU 514  514  514  LEU LEU B . n 
B 2  515  LEU 515  515  515  LEU LEU B . n 
B 2  516  ASN 516  516  516  ASN ASN B . n 
B 2  517  THR 517  517  517  THR THR B . n 
B 2  518  ILE 518  518  518  ILE ILE B . n 
B 2  519  SER 519  519  519  SER SER B . n 
B 2  520  ALA 520  520  520  ALA ALA B . n 
B 2  521  LEU 521  521  521  LEU LEU B . n 
B 2  522  ARG 522  522  522  ARG ARG B . n 
B 2  523  THR 523  523  523  THR THR B . n 
B 2  524  VAL 524  524  524  VAL VAL B . n 
B 2  525  ASN 525  525  525  ASN ASN B . n 
B 2  526  THR 526  526  526  THR THR B . n 
B 2  527  HIS 527  527  ?    ?   ?   B . n 
B 2  528  ASN 528  528  ?    ?   ?   B . n 
B 2  529  THR 529  529  ?    ?   ?   B . n 
B 2  530  THR 530  530  ?    ?   ?   B . n 
B 2  531  ASN 531  531  ?    ?   ?   B . n 
B 2  532  ALA 532  532  ?    ?   ?   B . n 
B 2  533  SER 533  533  ?    ?   ?   B . n 
B 2  534  LYS 534  534  ?    ?   ?   B . n 
B 2  535  GLN 535  535  ?    ?   ?   B . n 
B 2  536  THR 536  536  ?    ?   ?   B . n 
B 2  537  GLU 537  537  537  GLU GLU B . n 
B 2  538  ARG 538  538  538  ARG ARG B . n 
B 2  539  ALA 539  539  539  ALA ALA B . n 
B 2  540  ASP 540  540  540  ASP ASP B . n 
B 2  541  MET 541  541  541  MET MET B . n 
B 2  542  MET 542  542  542  MET MET B . n 
B 2  543  ARG 543  543  543  ARG ARG B . n 
B 2  544  ARG 544  544  544  ARG ARG B . n 
B 2  545  VAL 545  545  545  VAL VAL B . n 
B 2  546  HIS 546  546  546  HIS HIS B . n 
B 2  547  ALA 547  547  547  ALA ALA B . n 
B 2  548  SER 548  548  548  SER SER B . n 
B 2  549  TYR 549  549  549  TYR TYR B . n 
B 2  550  PRO 550  550  550  PRO PRO B . n 
B 2  551  GLY 551  551  551  GLY GLY B . n 
B 2  552  TYR 552  552  552  TYR TYR B . n 
B 2  553  ILE 553  553  553  ILE ILE B . n 
B 2  554  CYS 554  554  554  CYS CYS B . n 
B 2  555  VAL 555  555  555  VAL VAL B . n 
B 2  556  ALA 556  556  556  ALA ALA B . n 
B 2  557  GLN 557  557  557  GLN GLN B . n 
B 2  558  SER 558  558  558  SER SER B . n 
B 2  559  ALA 559  559  559  ALA ALA B . n 
B 2  560  ASP 560  560  560  ASP ASP B . n 
B 2  561  THR 561  561  561  THR THR B . n 
B 2  562  GLY 562  562  562  GLY GLY B . n 
B 2  563  GLU 563  563  563  GLU GLU B . n 
B 2  564  LYS 564  564  564  LYS LYS B . n 
B 2  565  VAL 565  565  565  VAL VAL B . n 
B 2  566  GLY 566  566  566  GLY GLY B . n 
B 2  567  MET 567  567  567  MET MET B . n 
B 2  568  SER 568  568  568  SER SER B . n 
B 2  569  LYS 569  569  569  LYS LYS B . n 
B 2  570  GLN 570  570  570  GLN GLN B . n 
B 2  571  LEU 571  571  571  LEU LEU B . n 
B 2  572  ALA 572  572  572  ALA ALA B . n 
B 2  573  ILE 573  573  573  ILE ILE B . n 
B 2  574  THR 574  574  574  THR THR B . n 
B 2  575  ALA 575  575  575  ALA ALA B . n 
B 2  576  ASN 576  576  576  ASN ASN B . n 
B 2  577  VAL 577  577  577  VAL VAL B . n 
B 2  578  CYS 578  578  578  CYS CYS B . n 
B 2  579  THR 579  579  579  THR THR B . n 
B 2  580  ALA 580  580  580  ALA ALA B . n 
B 2  581  GLY 581  581  581  GLY GLY B . n 
B 2  582  GLU 582  582  582  GLU GLU B . n 
B 2  583  VAL 583  583  583  VAL VAL B . n 
B 2  584  LEU 584  584  584  LEU LEU B . n 
B 2  585  SER 585  585  585  SER SER B . n 
B 2  586  LEU 586  586  586  LEU LEU B . n 
B 2  587  LYS 587  587  587  LYS LYS B . n 
B 2  588  GLN 588  588  588  GLN GLN B . n 
B 2  589  ARG 589  589  589  ARG ARG B . n 
B 2  590  LEU 590  590  590  LEU LEU B . n 
B 2  591  LEU 591  591  591  LEU LEU B . n 
B 2  592  SER 592  592  592  SER SER B . n 
B 2  593  ASP 593  593  593  ASP ASP B . n 
B 2  594  PRO 594  594  594  PRO PRO B . n 
B 2  595  ALA 595  595  595  ALA ALA B . n 
B 2  596  ILE 596  596  596  ILE ILE B . n 
B 2  597  GLN 597  597  597  GLN GLN B . n 
B 2  598  GLN 598  598  598  GLN GLN B . n 
B 2  599  LEU 599  599  599  LEU LEU B . n 
B 2  600  ALA 600  600  600  ALA ALA B . n 
B 2  601  ASP 601  601  601  ASP ASP B . n 
B 2  602  VAL 602  602  602  VAL VAL B . n 
B 2  603  SER 603  603  603  SER SER B . n 
B 2  604  ASN 604  604  604  ASN ASN B . n 
B 2  605  LYS 605  605  605  LYS LYS B . n 
B 2  606  ASP 606  606  606  ASP ASP B . n 
B 2  607  ILE 607  607  607  ILE ILE B . n 
B 2  608  VAL 608  608  608  VAL VAL B . n 
B 2  609  ARG 609  609  609  ARG ARG B . n 
B 2  610  LYS 610  610  610  LYS LYS B . n 
B 2  611  GLY 611  611  611  GLY GLY B . n 
B 2  612  LEU 612  612  612  LEU LEU B . n 
B 2  613  ALA 613  613  613  ALA ALA B . n 
B 2  614  ARG 614  614  614  ARG ARG B . n 
B 2  615  VAL 615  615  615  VAL VAL B . n 
B 2  616  PHE 616  616  616  PHE PHE B . n 
B 2  617  ILE 617  617  617  ILE ILE B . n 
B 2  618  ASN 618  618  618  ASN ASN B . n 
B 2  619  GLY 619  619  619  GLY GLY B . n 
B 2  620  GLU 620  620  620  GLU GLU B . n 
B 2  621  TRP 621  621  621  TRP TRP B . n 
B 2  622  ILE 622  622  622  ILE ILE B . n 
B 2  623  GLY 623  623  623  GLY GLY B . n 
B 2  624  CYS 624  624  624  CYS CYS B . n 
B 2  625  CYS 625  625  625  CYS CYS B . n 
B 2  626  THR 626  626  626  THR THR B . n 
B 2  627  ASN 627  627  627  ASN ASN B . n 
B 2  628  ALA 628  628  628  ALA ALA B . n 
B 2  629  PHE 629  629  629  PHE PHE B . n 
B 2  630  GLU 630  630  630  GLU GLU B . n 
B 2  631  LEU 631  631  631  LEU LEU B . n 
B 2  632  ALA 632  632  632  ALA ALA B . n 
B 2  633  GLN 633  633  633  GLN GLN B . n 
B 2  634  ARG 634  634  634  ARG ARG B . n 
B 2  635  TYR 635  635  635  TYR TYR B . n 
B 2  636  ARG 636  636  636  ARG ARG B . n 
B 2  637  MET 637  637  637  MET MET B . n 
B 2  638  LEU 638  638  638  LEU LEU B . n 
B 2  639  ARG 639  639  639  ARG ARG B . n 
B 2  640  ARG 640  640  640  ARG ARG B . n 
B 2  641  GLU 641  641  641  GLU GLU B . n 
B 2  642  GLY 642  642  642  GLY GLY B . n 
B 2  643  LYS 643  643  643  LYS LYS B . n 
B 2  644  VAL 644  644  644  VAL VAL B . n 
B 2  645  VAL 645  645  645  VAL VAL B . n 
B 2  646  HIS 646  646  646  HIS HIS B . n 
B 2  647  PRO 647  647  647  PRO PRO B . n 
B 2  648  HIS 648  648  648  HIS HIS B . n 
B 2  649  THR 649  649  649  THR THR B . n 
B 2  650  THR 650  650  650  THR THR B . n 
B 2  651  ILE 651  651  651  ILE ILE B . n 
B 2  652  TYR 652  652  652  TYR TYR B . n 
B 2  653  TRP 653  653  653  TRP TRP B . n 
B 2  654  ASP 654  654  654  ASP ASP B . n 
B 2  655  SER 655  655  655  SER SER B . n 
B 2  656  MET 656  656  656  MET MET B . n 
B 2  657  VAL 657  657  657  VAL VAL B . n 
B 2  658  ASP 658  658  658  ASP ASP B . n 
B 2  659  GLU 659  659  659  GLU GLU B . n 
B 2  660  VAL 660  660  660  VAL VAL B . n 
B 2  661  GLU 661  661  661  GLU GLU B . n 
B 2  662  PHE 662  662  662  PHE PHE B . n 
B 2  663  TRP 663  663  663  TRP TRP B . n 
B 2  664  LEU 664  664  664  LEU LEU B . n 
B 2  665  ASP 665  665  665  ASP ASP B . n 
B 2  666  VAL 666  666  666  VAL VAL B . n 
B 2  667  GLY 667  667  667  GLY GLY B . n 
B 2  668  ARG 668  668  668  ARG ARG B . n 
B 2  669  LEU 669  669  669  LEU LEU B . n 
B 2  670  THR 670  670  670  THR THR B . n 
B 2  671  ARG 671  671  671  ARG ARG B . n 
B 2  672  PRO 672  672  672  PRO PRO B . n 
B 2  673  LEU 673  673  673  LEU LEU B . n 
B 2  674  LEU 674  674  674  LEU LEU B . n 
B 2  675  ILE 675  675  675  ILE ILE B . n 
B 2  676  VAL 676  676  676  VAL VAL B . n 
B 2  677  ASP 677  677  677  ASP ASP B . n 
B 2  678  ASN 678  678  678  ASN ASN B . n 
B 2  679  ASN 679  679  679  ASN ASN B . n 
B 2  680  ILE 680  680  680  ILE ILE B . n 
B 2  681  GLU 681  681  681  GLU GLU B . n 
B 2  682  LYS 682  682  682  LYS LYS B . n 
B 2  683  TYR 683  683  683  TYR TYR B . n 
B 2  684  ASN 684  684  684  ASN ASN B . n 
B 2  685  GLN 685  685  685  GLN GLN B . n 
B 2  686  ALA 686  686  686  ALA ALA B . n 
B 2  687  CYS 687  687  687  CYS CYS B . n 
B 2  688  TYR 688  688  688  TYR TYR B . n 
B 2  689  LYS 689  689  689  LYS LYS B . n 
B 2  690  ALA 690  690  690  ALA ALA B . n 
B 2  691  ALA 691  691  691  ALA ALA B . n 
B 2  692  GLU 692  692  692  GLU GLU B . n 
B 2  693  ALA 693  693  693  ALA ALA B . n 
B 2  694  ARG 694  694  694  ARG ARG B . n 
B 2  695  LYS 695  695  695  LYS LYS B . n 
B 2  696  LYS 696  696  696  LYS LYS B . n 
B 2  697  GLY 697  697  697  GLY GLY B . n 
B 2  698  ASP 698  698  698  ASP ASP B . n 
B 2  699  LYS 699  699  699  LYS LYS B . n 
B 2  700  ASP 700  700  700  ASP ASP B . n 
B 2  701  TRP 701  701  701  TRP TRP B . n 
B 2  702  GLU 702  702  702  GLU GLU B . n 
B 2  703  LYS 703  703  703  LYS LYS B . n 
B 2  704  HIS 704  704  704  HIS HIS B . n 
B 2  705  LYS 705  705  705  LYS LYS B . n 
B 2  706  ILE 706  706  706  ILE ILE B . n 
B 2  707  PRO 707  707  707  PRO PRO B . n 
B 2  708  PHE 708  708  708  PHE PHE B . n 
B 2  709  ILE 709  709  709  ILE ILE B . n 
B 2  710  GLN 710  710  710  GLN GLN B . n 
B 2  711  ASN 711  711  711  ASN ASN B . n 
B 2  712  THR 712  712  712  THR THR B . n 
B 2  713  ARG 713  713  713  ARG ARG B . n 
B 2  714  PHE 714  714  714  PHE PHE B . n 
B 2  715  THR 715  715  715  THR THR B . n 
B 2  716  PRO 716  716  716  PRO PRO B . n 
B 2  717  GLN 717  717  717  GLN GLN B . n 
B 2  718  MET 718  718  718  MET MET B . n 
B 2  719  ALA 719  719  719  ALA ALA B . n 
B 2  720  LYS 720  720  720  LYS LYS B . n 
B 2  721  ASP 721  721  721  ASP ASP B . n 
B 2  722  ILE 722  722  722  ILE ILE B . n 
B 2  723  LEU 723  723  723  LEU LEU B . n 
B 2  724  ALA 724  724  724  ALA ALA B . n 
B 2  725  GLY 725  725  725  GLY GLY B . n 
B 2  726  THR 726  726  726  THR THR B . n 
B 2  727  LEU 727  727  727  LEU LEU B . n 
B 2  728  THR 728  728  728  THR THR B . n 
B 2  729  LEU 729  729  729  LEU LEU B . n 
B 2  730  GLU 730  730  730  GLU GLU B . n 
B 2  731  ASP 731  731  731  ASP ASP B . n 
B 2  732  LEU 732  732  732  LEU LEU B . n 
B 2  733  VAL 733  733  733  VAL VAL B . n 
B 2  734  ALA 734  734  734  ALA ALA B . n 
B 2  735  GLN 735  735  735  GLN GLN B . n 
B 2  736  GLY 736  736  736  GLY GLY B . n 
B 2  737  ILE 737  737  737  ILE ILE B . n 
B 2  738  CYS 738  738  738  CYS CYS B . n 
B 2  739  GLU 739  739  739  GLU GLU B . n 
B 2  740  PHE 740  740  740  PHE PHE B . n 
B 2  741  ILE 741  741  741  ILE ILE B . n 
B 2  742  THR 742  742  742  THR THR B . n 
B 2  743  PRO 743  743  743  PRO PRO B . n 
B 2  744  GLU 744  744  744  GLU GLU B . n 
B 2  745  GLU 745  745  745  GLU GLU B . n 
B 2  746  ALA 746  746  746  ALA ALA B . n 
B 2  747  GLU 747  747  747  GLU GLU B . n 
B 2  748  ASN 748  748  748  ASN ASN B . n 
B 2  749  CYS 749  749  749  CYS CYS B . n 
B 2  750  LEU 750  750  750  LEU LEU B . n 
B 2  751  VAL 751  751  751  VAL VAL B . n 
B 2  752  ALA 752  752  752  ALA ALA B . n 
B 2  753  PHE 753  753  753  PHE PHE B . n 
B 2  754  SER 754  754  754  SER SER B . n 
B 2  755  ILE 755  755  755  ILE ILE B . n 
B 2  756  ILE 756  756  756  ILE ILE B . n 
B 2  757  GLU 757  757  757  GLU GLU B . n 
B 2  758  LEU 758  758  758  LEU LEU B . n 
B 2  759  ARG 759  759  759  ARG ARG B . n 
B 2  760  LYS 760  760  760  LYS LYS B . n 
B 2  761  HIS 761  761  761  HIS HIS B . n 
B 2  762  LYS 762  762  762  LYS LYS B . n 
B 2  763  HIS 763  763  763  HIS HIS B . n 
B 2  764  ASP 764  764  764  ASP ASP B . n 
B 2  765  VAL 765  765  765  VAL VAL B . n 
B 2  766  THR 766  766  766  THR THR B . n 
B 2  767  ARG 767  767  767  ARG ARG B . n 
B 2  768  ARG 768  768  768  ARG ARG B . n 
B 2  769  PHE 769  769  769  PHE PHE B . n 
B 2  770  THR 770  770  770  THR THR B . n 
B 2  771  HIS 771  771  771  HIS HIS B . n 
B 2  772  VAL 772  772  772  VAL VAL B . n 
B 2  773  ASP 773  773  773  ASP ASP B . n 
B 2  774  VAL 774  774  774  VAL VAL B . n 
B 2  775  PRO 775  775  775  PRO PRO B . n 
B 2  776  GLN 776  776  776  GLN GLN B . n 
B 2  777  ALA 777  777  777  ALA ALA B . n 
B 2  778  ILE 778  778  778  ILE ILE B . n 
B 2  779  LEU 779  779  779  LEU LEU B . n 
B 2  780  GLY 780  780  780  GLY GLY B . n 
B 2  781  LEU 781  781  781  LEU LEU B . n 
B 2  782  ALA 782  782  782  ALA ALA B . n 
B 2  783  ALA 783  783  783  ALA ALA B . n 
B 2  784  LEU 784  784  784  LEU LEU B . n 
B 2  785  VAL 785  785  785  VAL VAL B . n 
B 2  786  SER 786  786  786  SER SER B . n 
B 2  787  PRO 787  787  787  PRO PRO B . n 
B 2  788  TYR 788  788  788  TYR TYR B . n 
B 2  789  ALA 789  789  789  ALA ALA B . n 
B 2  790  ASN 790  790  790  ASN ASN B . n 
B 2  791  CYS 791  791  791  CYS CYS B . n 
B 2  792  THR 792  792  792  THR THR B . n 
B 2  793  GLN 793  793  793  GLN GLN B . n 
B 2  794  PRO 794  794  794  PRO PRO B . n 
B 2  795  ALA 795  795  795  ALA ALA B . n 
B 2  796  ARG 796  796  796  ARG ARG B . n 
B 2  797  VAL 797  797  797  VAL VAL B . n 
B 2  798  THR 798  798  798  THR THR B . n 
B 2  799  TYR 799  799  799  TYR TYR B . n 
B 2  800  GLU 800  800  800  GLU GLU B . n 
B 2  801  THR 801  801  801  THR THR B . n 
B 2  802  ASN 802  802  802  ASN ASN B . n 
B 2  803  GLN 803  803  803  GLN GLN B . n 
B 2  804  GLY 804  804  804  GLY GLY B . n 
B 2  805  ARG 805  805  805  ARG ARG B . n 
B 2  806  GLN 806  806  806  GLN GLN B . n 
B 2  807  THR 807  807  807  THR THR B . n 
B 2  808  GLY 808  808  808  GLY GLY B . n 
B 2  809  GLY 809  809  809  GLY GLY B . n 
B 2  810  TRP 810  810  810  TRP TRP B . n 
B 2  811  TYR 811  811  811  TYR TYR B . n 
B 2  812  CYS 812  812  812  CYS CYS B . n 
B 2  813  PHE 813  813  813  PHE PHE B . n 
B 2  814  SER 814  814  814  SER SER B . n 
B 2  815  TRP 815  815  815  TRP TRP B . n 
B 2  816  PRO 816  816  816  PRO PRO B . n 
B 2  817  TYR 817  817  817  TYR TYR B . n 
B 2  818  ARG 818  818  818  ARG ARG B . n 
B 2  819  VAL 819  819  819  VAL VAL B . n 
B 2  820  ASP 820  820  820  ASP ASP B . n 
B 2  821  MET 821  821  821  MET MET B . n 
B 2  822  ASN 822  822  822  ASN ASN B . n 
B 2  823  ARG 823  823  823  ARG ARG B . n 
B 2  824  PHE 824  824  824  PHE PHE B . n 
B 2  825  PHE 825  825  825  PHE PHE B . n 
B 2  826  GLN 826  826  826  GLN GLN B . n 
B 2  827  PHE 827  827  827  PHE PHE B . n 
B 2  828  TYR 828  828  828  TYR TYR B . n 
B 2  829  ASN 829  829  829  ASN ASN B . n 
B 2  830  GLU 830  830  830  GLU GLU B . n 
B 2  831  MET 831  831  831  MET MET B . n 
B 2  832  PRO 832  832  832  PRO PRO B . n 
B 2  833  LEU 833  833  833  LEU LEU B . n 
B 2  834  VAL 834  834  834  VAL VAL B . n 
B 2  835  LYS 835  835  835  LYS LYS B . n 
B 2  836  THR 836  836  836  THR THR B . n 
B 2  837  ILE 837  837  837  ILE ILE B . n 
B 2  838  ALA 838  838  838  ALA ALA B . n 
B 2  839  HIS 839  839  839  HIS HIS B . n 
B 2  840  ASN 840  840  840  ASN ASN B . n 
B 2  841  TYR 841  841  841  TYR TYR B . n 
B 2  842  VAL 842  842  842  VAL VAL B . n 
B 2  843  ILE 843  843  843  ILE ILE B . n 
B 2  844  PRO 844  844  844  PRO PRO B . n 
B 2  845  ASN 845  845  845  ASN ASN B . n 
B 2  846  GLY 846  846  846  GLY GLY B . n 
B 2  847  LEU 847  847  847  LEU LEU B . n 
B 2  848  ASN 848  848  848  ASN ASN B . n 
B 2  849  THR 849  849  849  THR THR B . n 
B 2  850  ILE 850  850  850  ILE ILE B . n 
B 2  851  VAL 851  851  851  VAL VAL B . n 
B 2  852  ALA 852  852  852  ALA ALA B . n 
B 2  853  TYR 853  853  853  TYR TYR B . n 
B 2  854  MET 854  854  854  MET MET B . n 
B 2  855  ILE 855  855  855  ILE ILE B . n 
B 2  856  TYR 856  856  856  TYR TYR B . n 
B 2  857  GLY 857  857  857  GLY GLY B . n 
B 2  858  GLY 858  858  858  GLY GLY B . n 
B 2  859  TYR 859  859  859  TYR TYR B . n 
B 2  860  ASN 860  860  860  ASN ASN B . n 
B 2  861  GLN 861  861  861  GLN GLN B . n 
B 2  862  GLU 862  862  862  GLU GLU B . n 
B 2  863  ASP 863  863  863  ASP ASP B . n 
B 2  864  SER 864  864  864  SER SER B . n 
B 2  865  VAL 865  865  865  VAL VAL B . n 
B 2  866  ILE 866  866  866  ILE ILE B . n 
B 2  867  VAL 867  867  867  VAL VAL B . n 
B 2  868  SER 868  868  868  SER SER B . n 
B 2  869  GLN 869  869  869  GLN GLN B . n 
B 2  870  SER 870  870  870  SER SER B . n 
B 2  871  PHE 871  871  871  PHE PHE B . n 
B 2  872  ILE 872  872  872  ILE ILE B . n 
B 2  873  ASP 873  873  873  ASP ASP B . n 
B 2  874  ARG 874  874  874  ARG ARG B . n 
B 2  875  GLY 875  875  875  GLY GLY B . n 
B 2  876  GLY 876  876  876  GLY GLY B . n 
B 2  877  PHE 877  877  877  PHE PHE B . n 
B 2  878  ALA 878  878  878  ALA ALA B . n 
B 2  879  GLY 879  879  879  GLY GLY B . n 
B 2  880  THR 880  880  880  THR THR B . n 
B 2  881  PHE 881  881  881  PHE PHE B . n 
B 2  882  TYR 882  882  882  TYR TYR B . n 
B 2  883  ARG 883  883  883  ARG ARG B . n 
B 2  884  GLU 884  884  884  GLU GLU B . n 
B 2  885  GLU 885  885  885  GLU GLU B . n 
B 2  886  LYS 886  886  886  LYS LYS B . n 
B 2  887  VAL 887  887  887  VAL VAL B . n 
B 2  888  GLU 888  888  888  GLU GLU B . n 
B 2  889  LEU 889  889  889  LEU LEU B . n 
B 2  890  GLU 890  890  890  GLU GLU B . n 
B 2  891  SER 891  891  891  SER SER B . n 
B 2  892  ASP 892  892  892  ASP ASP B . n 
B 2  893  ILE 893  893  893  ILE ILE B . n 
B 2  894  GLU 894  894  894  GLU GLU B . n 
B 2  895  SER 895  895  895  SER SER B . n 
B 2  896  PHE 896  896  896  PHE PHE B . n 
B 2  897  GLY 897  897  897  GLY GLY B . n 
B 2  898  LYS 898  898  898  LYS LYS B . n 
B 2  899  PRO 899  899  899  PRO PRO B . n 
B 2  900  ASP 900  900  900  ASP ASP B . n 
B 2  901  PRO 901  901  901  PRO PRO B . n 
B 2  902  LEU 902  902  902  LEU LEU B . n 
B 2  903  ILE 903  903  903  ILE ILE B . n 
B 2  904  THR 904  904  904  THR THR B . n 
B 2  905  LYS 905  905  905  LYS LYS B . n 
B 2  906  ASN 906  906  906  ASN ASN B . n 
B 2  907  LEU 907  907  907  LEU LEU B . n 
B 2  908  LYS 908  908  908  LYS LYS B . n 
B 2  909  PRO 909  909  909  PRO PRO B . n 
B 2  910  GLY 910  910  910  GLY GLY B . n 
B 2  911  ALA 911  911  911  ALA ALA B . n 
B 2  912  ASN 912  912  912  ASN ASN B . n 
B 2  913  TYR 913  913  913  TYR TYR B . n 
B 2  914  GLU 914  914  914  GLU GLU B . n 
B 2  915  LYS 915  915  915  LYS LYS B . n 
B 2  916  LEU 916  916  916  LEU LEU B . n 
B 2  917  VAL 917  917  917  VAL VAL B . n 
B 2  918  ASP 918  918  918  ASP ASP B . n 
B 2  919  GLY 919  919  919  GLY GLY B . n 
B 2  920  PHE 920  920  920  PHE PHE B . n 
B 2  921  VAL 921  921  921  VAL VAL B . n 
B 2  922  PRO 922  922  922  PRO PRO B . n 
B 2  923  VAL 923  923  923  VAL VAL B . n 
B 2  924  GLY 924  924  924  GLY GLY B . n 
B 2  925  THR 925  925  925  THR THR B . n 
B 2  926  VAL 926  926  926  VAL VAL B . n 
B 2  927  VAL 927  927  927  VAL VAL B . n 
B 2  928  LYS 928  928  928  LYS LYS B . n 
B 2  929  LYS 929  929  929  LYS LYS B . n 
B 2  930  GLY 930  930  930  GLY GLY B . n 
B 2  931  ASP 931  931  931  ASP ASP B . n 
B 2  932  ILE 932  932  932  ILE ILE B . n 
B 2  933  ILE 933  933  933  ILE ILE B . n 
B 2  934  ILE 934  934  934  ILE ILE B . n 
B 2  935  GLY 935  935  935  GLY GLY B . n 
B 2  936  LYS 936  936  936  LYS LYS B . n 
B 2  937  VAL 937  937  937  VAL VAL B . n 
B 2  938  ALA 938  938  938  ALA ALA B . n 
B 2  939  LYS 939  939  939  LYS LYS B . n 
B 2  940  ILE 940  940  940  ILE ILE B . n 
B 2  941  ARG 941  941  ?    ?   ?   B . n 
B 2  942  GLY 942  942  ?    ?   ?   B . n 
B 2  943  GLU 943  943  ?    ?   ?   B . n 
B 2  944  LYS 944  944  ?    ?   ?   B . n 
B 2  945  ASP 945  945  ?    ?   ?   B . n 
B 2  946  GLU 946  946  ?    ?   ?   B . n 
B 2  947  LEU 947  947  ?    ?   ?   B . n 
B 2  948  ASN 948  948  ?    ?   ?   B . n 
B 2  949  LYS 949  949  949  LYS LYS B . n 
B 2  950  TYR 950  950  950  TYR TYR B . n 
B 2  951  ILE 951  951  951  ILE ILE B . n 
B 2  952  ASP 952  952  952  ASP ASP B . n 
B 2  953  ARG 953  953  953  ARG ARG B . n 
B 2  954  SER 954  954  954  SER SER B . n 
B 2  955  VAL 955  955  955  VAL VAL B . n 
B 2  956  MET 956  956  956  MET MET B . n 
B 2  957  TYR 957  957  957  TYR TYR B . n 
B 2  958  GLY 958  958  958  GLY GLY B . n 
B 2  959  PHE 959  959  959  PHE PHE B . n 
B 2  960  ASP 960  960  960  ASP ASP B . n 
B 2  961  GLU 961  961  961  GLU GLU B . n 
B 2  962  PRO 962  962  962  PRO PRO B . n 
B 2  963  ALA 963  963  963  ALA ALA B . n 
B 2  964  VAL 964  964  964  VAL VAL B . n 
B 2  965  VAL 965  965  965  VAL VAL B . n 
B 2  966  ASP 966  966  966  ASP ASP B . n 
B 2  967  ALA 967  967  967  ALA ALA B . n 
B 2  968  VAL 968  968  968  VAL VAL B . n 
B 2  969  MET 969  969  969  MET MET B . n 
B 2  970  ARG 970  970  970  ARG ARG B . n 
B 2  971  PRO 971  971  971  PRO PRO B . n 
B 2  972  HIS 972  972  972  HIS HIS B . n 
B 2  973  GLY 973  973  973  GLY GLY B . n 
B 2  974  PRO 974  974  974  PRO PRO B . n 
B 2  975  ASN 975  975  975  ASN ASN B . n 
B 2  976  ASP 976  976  976  ASP ASP B . n 
B 2  977  GLU 977  977  977  GLU GLU B . n 
B 2  978  ILE 978  978  978  ILE ILE B . n 
B 2  979  PHE 979  979  979  PHE PHE B . n 
B 2  980  GLY 980  980  980  GLY GLY B . n 
B 2  981  LEU 981  981  981  LEU LEU B . n 
B 2  982  MET 982  982  982  MET MET B . n 
B 2  983  ARG 983  983  983  ARG ARG B . n 
B 2  984  LEU 984  984  984  LEU LEU B . n 
B 2  985  ARG 985  985  985  ARG ARG B . n 
B 2  986  TYR 986  986  986  TYR TYR B . n 
B 2  987  GLU 987  987  987  GLU GLU B . n 
B 2  988  ARG 988  988  988  ARG ARG B . n 
B 2  989  ASN 989  989  989  ASN ASN B . n 
B 2  990  LEU 990  990  990  LEU LEU B . n 
B 2  991  ASN 991  991  991  ASN ASN B . n 
B 2  992  ILE 992  992  992  ILE ILE B . n 
B 2  993  GLY 993  993  993  GLY GLY B . n 
B 2  994  ASP 994  994  994  ASP ASP B . n 
B 2  995  LYS 995  995  995  LYS LYS B . n 
B 2  996  MET 996  996  996  MET MET B . n 
B 2  997  SER 997  997  997  SER SER B . n 
B 2  998  SER 998  998  998  SER SER B . n 
B 2  999  ARG 999  999  999  ARG ARG B . n 
B 2  1000 SER 1000 1000 1000 SER SER B . n 
B 2  1001 GLY 1001 1001 1001 GLY GLY B . n 
B 2  1002 ASN 1002 1002 1002 ASN ASN B . n 
B 2  1003 LYS 1003 1003 1003 LYS LYS B . n 
B 2  1004 GLY 1004 1004 1004 GLY GLY B . n 
B 2  1005 ILE 1005 1005 1005 ILE ILE B . n 
B 2  1006 ALA 1006 1006 1006 ALA ALA B . n 
B 2  1007 ALA 1007 1007 1007 ALA ALA B . n 
B 2  1008 LEU 1008 1008 1008 LEU LEU B . n 
B 2  1009 ALA 1009 1009 1009 ALA ALA B . n 
B 2  1010 LEU 1010 1010 1010 LEU LEU B . n 
B 2  1011 PRO 1011 1011 1011 PRO PRO B . n 
B 2  1012 THR 1012 1012 1012 THR THR B . n 
B 2  1013 SER 1013 1013 1013 SER SER B . n 
B 2  1014 ASP 1014 1014 1014 ASP ASP B . n 
B 2  1015 MET 1015 1015 1015 MET MET B . n 
B 2  1016 PRO 1016 1016 1016 PRO PRO B . n 
B 2  1017 PHE 1017 1017 1017 PHE PHE B . n 
B 2  1018 THR 1018 1018 1018 THR THR B . n 
B 2  1019 GLU 1019 1019 1019 GLU GLU B . n 
B 2  1020 ASP 1020 1020 1020 ASP ASP B . n 
B 2  1021 GLY 1021 1021 1021 GLY GLY B . n 
B 2  1022 LEU 1022 1022 1022 LEU LEU B . n 
B 2  1023 GLN 1023 1023 1023 GLN GLN B . n 
B 2  1024 PRO 1024 1024 1024 PRO PRO B . n 
B 2  1025 ASP 1025 1025 1025 ASP ASP B . n 
B 2  1026 LEU 1026 1026 1026 LEU LEU B . n 
B 2  1027 ILE 1027 1027 1027 ILE ILE B . n 
B 2  1028 VAL 1028 1028 1028 VAL VAL B . n 
B 2  1029 ASN 1029 1029 1029 ASN ASN B . n 
B 2  1030 PRO 1030 1030 1030 PRO PRO B . n 
B 2  1031 HIS 1031 1031 1031 HIS HIS B . n 
B 2  1032 SER 1032 1032 1032 SER SER B . n 
B 2  1033 HIS 1033 1033 1033 HIS HIS B . n 
B 2  1034 PRO 1034 1034 1034 PRO PRO B . n 
B 2  1035 SER 1035 1035 1035 SER SER B . n 
B 2  1036 ARG 1036 1036 1036 ARG ARG B . n 
B 2  1037 MET 1037 1037 1037 MET MET B . n 
B 2  1038 THR 1038 1038 1038 THR THR B . n 
B 2  1039 ASN 1039 1039 1039 ASN ASN B . n 
B 2  1040 GLY 1040 1040 1040 GLY GLY B . n 
B 2  1041 GLN 1041 1041 1041 GLN GLN B . n 
B 2  1042 MET 1042 1042 1042 MET MET B . n 
B 2  1043 ILE 1043 1043 1043 ILE ILE B . n 
B 2  1044 GLU 1044 1044 1044 GLU GLU B . n 
B 2  1045 THR 1045 1045 1045 THR THR B . n 
B 2  1046 THR 1046 1046 1046 THR THR B . n 
B 2  1047 VAL 1047 1047 1047 VAL VAL B . n 
B 2  1048 GLY 1048 1048 1048 GLY GLY B . n 
B 2  1049 LEU 1049 1049 1049 LEU LEU B . n 
B 2  1050 ALA 1050 1050 1050 ALA ALA B . n 
B 2  1051 ASN 1051 1051 1051 ASN ASN B . n 
B 2  1052 ALA 1052 1052 1052 ALA ALA B . n 
B 2  1053 LEU 1053 1053 1053 LEU LEU B . n 
B 2  1054 GLN 1054 1054 1054 GLN GLN B . n 
B 2  1055 GLY 1055 1055 1055 GLY GLY B . n 
B 2  1056 VAL 1056 1056 1056 VAL VAL B . n 
B 2  1057 VAL 1057 1057 1057 VAL VAL B . n 
B 2  1058 THR 1058 1058 1058 THR THR B . n 
B 2  1059 ASP 1059 1059 1059 ASP ASP B . n 
B 2  1060 GLY 1060 1060 1060 GLY GLY B . n 
B 2  1061 THR 1061 1061 1061 THR THR B . n 
B 2  1062 ALA 1062 1062 1062 ALA ALA B . n 
B 2  1063 PHE 1063 1063 1063 PHE PHE B . n 
B 2  1064 LEU 1064 1064 1064 LEU LEU B . n 
B 2  1065 PRO 1065 1065 1065 PRO PRO B . n 
B 2  1066 ILE 1066 1066 1066 ILE ILE B . n 
B 2  1067 ASN 1067 1067 1067 ASN ASN B . n 
B 2  1068 VAL 1068 1068 1068 VAL VAL B . n 
B 2  1069 GLN 1069 1069 1069 GLN GLN B . n 
B 2  1070 LEU 1070 1070 1070 LEU LEU B . n 
B 2  1071 LEU 1071 1071 1071 LEU LEU B . n 
B 2  1072 SER 1072 1072 1072 SER SER B . n 
B 2  1073 GLU 1073 1073 1073 GLU GLU B . n 
B 2  1074 ARG 1074 1074 1074 ARG ARG B . n 
B 2  1075 LEU 1075 1075 1075 LEU LEU B . n 
B 2  1076 ALA 1076 1076 1076 ALA ALA B . n 
B 2  1077 GLN 1077 1077 1077 GLN GLN B . n 
B 2  1078 GLU 1078 1078 1078 GLU GLU B . n 
B 2  1079 GLY 1079 1079 1079 GLY GLY B . n 
B 2  1080 LEU 1080 1080 1080 LEU LEU B . n 
B 2  1081 ARG 1081 1081 1081 ARG ARG B . n 
B 2  1082 PHE 1082 1082 1082 PHE PHE B . n 
B 2  1083 ASN 1083 1083 1083 ASN ASN B . n 
B 2  1084 GLY 1084 1084 1084 GLY GLY B . n 
B 2  1085 CYS 1085 1085 1085 CYS CYS B . n 
B 2  1086 GLN 1086 1086 1086 GLN GLN B . n 
B 2  1087 LYS 1087 1087 1087 LYS LYS B . n 
B 2  1088 MET 1088 1088 1088 MET MET B . n 
B 2  1089 PHE 1089 1089 1089 PHE PHE B . n 
B 2  1090 ASN 1090 1090 1090 ASN ASN B . n 
B 2  1091 GLY 1091 1091 1091 GLY GLY B . n 
B 2  1092 GLN 1092 1092 1092 GLN GLN B . n 
B 2  1093 THR 1093 1093 1093 THR THR B . n 
B 2  1094 GLY 1094 1094 1094 GLY GLY B . n 
B 2  1095 GLU 1095 1095 1095 GLU GLU B . n 
B 2  1096 TYR 1096 1096 1096 TYR TYR B . n 
B 2  1097 PHE 1097 1097 1097 PHE PHE B . n 
B 2  1098 ASP 1098 1098 1098 ASP ASP B . n 
B 2  1099 ALA 1099 1099 1099 ALA ALA B . n 
B 2  1100 ALA 1100 1100 1100 ALA ALA B . n 
B 2  1101 ILE 1101 1101 1101 ILE ILE B . n 
B 2  1102 PHE 1102 1102 1102 PHE PHE B . n 
B 2  1103 ILE 1103 1103 1103 ILE ILE B . n 
B 2  1104 GLY 1104 1104 1104 GLY GLY B . n 
B 2  1105 PRO 1105 1105 1105 PRO PRO B . n 
B 2  1106 THR 1106 1106 1106 THR THR B . n 
B 2  1107 TYR 1107 1107 1107 TYR TYR B . n 
B 2  1108 HIS 1108 1108 1108 HIS HIS B . n 
B 2  1109 GLN 1109 1109 1109 GLN GLN B . n 
B 2  1110 ARG 1110 1110 1110 ARG ARG B . n 
B 2  1111 LEU 1111 1111 1111 LEU LEU B . n 
B 2  1112 GLN 1112 1112 1112 GLN GLN B . n 
B 2  1113 LYS 1113 1113 1113 LYS LYS B . n 
B 2  1114 PHE 1114 1114 1114 PHE PHE B . n 
B 2  1115 VAL 1115 1115 1115 VAL VAL B . n 
B 2  1116 LEU 1116 1116 1116 LEU LEU B . n 
B 2  1117 ASP 1117 1117 1117 ASP ASP B . n 
B 2  1118 ASP 1118 1118 1118 ASP ASP B . n 
B 2  1119 ARG 1119 1119 1119 ARG ARG B . n 
B 2  1120 TYR 1120 1120 1120 TYR TYR B . n 
B 2  1121 ALA 1121 1121 1121 ALA ALA B . n 
B 2  1122 VAL 1122 1122 1122 VAL VAL B . n 
B 2  1123 ALA 1123 1123 1123 ALA ALA B . n 
B 2  1124 SER 1124 1124 1124 SER SER B . n 
B 2  1125 TYR 1125 1125 1125 TYR TYR B . n 
B 2  1126 GLY 1126 1126 1126 GLY GLY B . n 
B 2  1127 PRO 1127 1127 1127 PRO PRO B . n 
B 2  1128 THR 1128 1128 1128 THR THR B . n 
B 2  1129 ASP 1129 1129 1129 ASP ASP B . n 
B 2  1130 ALA 1130 1130 1130 ALA ALA B . n 
B 2  1131 LEU 1131 1131 1131 LEU LEU B . n 
B 2  1132 THR 1132 1132 1132 THR THR B . n 
B 2  1133 GLY 1133 1133 1133 GLY GLY B . n 
B 2  1134 GLN 1134 1134 1134 GLN GLN B . n 
B 2  1135 PRO 1135 1135 1135 PRO PRO B . n 
B 2  1136 LEU 1136 1136 1136 LEU LEU B . n 
B 2  1137 ASP 1137 1137 1137 ASP ASP B . n 
B 2  1138 GLY 1138 1138 1138 GLY GLY B . n 
B 2  1139 LYS 1139 1139 1139 LYS LYS B . n 
B 2  1140 ARG 1140 1140 1140 ARG ARG B . n 
B 2  1141 SER 1141 1141 1141 SER SER B . n 
B 2  1142 HIS 1142 1142 1142 HIS HIS B . n 
B 2  1143 GLY 1143 1143 1143 GLY GLY B . n 
B 2  1144 GLY 1144 1144 1144 GLY GLY B . n 
B 2  1145 LEU 1145 1145 1145 LEU LEU B . n 
B 2  1146 ARG 1146 1146 1146 ARG ARG B . n 
B 2  1147 LEU 1147 1147 1147 LEU LEU B . n 
B 2  1148 GLY 1148 1148 1148 GLY GLY B . n 
B 2  1149 GLU 1149 1149 1149 GLU GLU B . n 
B 2  1150 MET 1150 1150 1150 MET MET B . n 
B 2  1151 GLU 1151 1151 1151 GLU GLU B . n 
B 2  1152 HIS 1152 1152 1152 HIS HIS B . n 
B 2  1153 TRP 1153 1153 1153 TRP TRP B . n 
B 2  1154 VAL 1154 1154 1154 VAL VAL B . n 
B 2  1155 LEU 1155 1155 1155 LEU LEU B . n 
B 2  1156 THR 1156 1156 1156 THR THR B . n 
B 2  1157 ALA 1157 1157 1157 ALA ALA B . n 
B 2  1158 GLN 1158 1158 1158 GLN GLN B . n 
B 2  1159 GLY 1159 1159 1159 GLY GLY B . n 
B 2  1160 ALA 1160 1160 1160 ALA ALA B . n 
B 2  1161 MET 1161 1161 1161 MET MET B . n 
B 2  1162 GLN 1162 1162 1162 GLN GLN B . n 
B 2  1163 THR 1163 1163 1163 THR THR B . n 
B 2  1164 ILE 1164 1164 1164 ILE ILE B . n 
B 2  1165 ILE 1165 1165 1165 ILE ILE B . n 
B 2  1166 GLU 1166 1166 1166 GLU GLU B . n 
B 2  1167 LYS 1167 1167 1167 LYS LYS B . n 
B 2  1168 SER 1168 1168 1168 SER SER B . n 
B 2  1169 HIS 1169 1169 1169 HIS HIS B . n 
B 2  1170 ASP 1170 1170 1170 ASP ASP B . n 
B 2  1171 ASP 1171 1171 1171 ASP ASP B . n 
B 2  1172 SER 1172 1172 1172 SER SER B . n 
B 2  1173 ASP 1173 1173 1173 ASP ASP B . n 
B 2  1174 GLY 1174 1174 1174 GLY GLY B . n 
B 2  1175 CYS 1175 1175 1175 CYS CYS B . n 
B 2  1176 ILE 1176 1176 1176 ILE ILE B . n 
B 2  1177 SER 1177 1177 1177 SER SER B . n 
B 2  1178 TYR 1178 1178 1178 TYR TYR B . n 
B 2  1179 ILE 1179 1179 1179 ILE ILE B . n 
B 2  1180 CYS 1180 1180 1180 CYS CYS B . n 
B 2  1181 ARG 1181 1181 1181 ARG ARG B . n 
B 2  1182 ASN 1182 1182 1182 ASN ASN B . n 
B 2  1183 CYS 1183 1183 1183 CYS CYS B . n 
B 2  1184 GLY 1184 1184 1184 GLY GLY B . n 
B 2  1185 GLU 1185 1185 1185 GLU GLU B . n 
B 2  1186 PRO 1186 1186 1186 PRO PRO B . n 
B 2  1187 ALA 1187 1187 1187 ALA ALA B . n 
B 2  1188 ILE 1188 1188 1188 ILE ILE B . n 
B 2  1189 TYR 1189 1189 1189 TYR TYR B . n 
B 2  1190 ASN 1190 1190 1190 ASN ASN B . n 
B 2  1191 ALA 1191 1191 1191 ALA ALA B . n 
B 2  1192 SER 1192 1192 1192 SER SER B . n 
B 2  1193 HIS 1193 1193 1193 HIS HIS B . n 
B 2  1194 PRO 1194 1194 1194 PRO PRO B . n 
B 2  1195 ILE 1195 1195 1195 ILE ILE B . n 
B 2  1196 TYR 1196 1196 1196 TYR TYR B . n 
B 2  1197 LYS 1197 1197 1197 LYS LYS B . n 
B 2  1198 CYS 1198 1198 1198 CYS CYS B . n 
B 2  1199 MET 1199 1199 1199 MET MET B . n 
B 2  1200 ASN 1200 1200 1200 ASN ASN B . n 
B 2  1201 CYS 1201 1201 1201 CYS CYS B . n 
B 2  1202 ASP 1202 1202 1202 ASP ASP B . n 
B 2  1203 VAL 1203 1203 1203 VAL VAL B . n 
B 2  1204 GLN 1204 1204 1204 GLN GLN B . n 
B 2  1205 ALA 1205 1205 1205 ALA ALA B . n 
B 2  1206 ASP 1206 1206 1206 ASP ASP B . n 
B 2  1207 ILE 1207 1207 1207 ILE ILE B . n 
B 2  1208 GLY 1208 1208 1208 GLY GLY B . n 
B 2  1209 MET 1209 1209 1209 MET MET B . n 
B 2  1210 VAL 1210 1210 1210 VAL VAL B . n 
B 2  1211 ASP 1211 1211 1211 ASP ASP B . n 
B 2  1212 SER 1212 1212 1212 SER SER B . n 
B 2  1213 ARG 1213 1213 1213 ARG ARG B . n 
B 2  1214 ARG 1214 1214 1214 ARG ARG B . n 
B 2  1215 SER 1215 1215 1215 SER SER B . n 
B 2  1216 SER 1216 1216 1216 SER SER B . n 
B 2  1217 ILE 1217 1217 1217 ILE ILE B . n 
B 2  1218 VAL 1218 1218 1218 VAL VAL B . n 
B 2  1219 PHE 1219 1219 1219 PHE PHE B . n 
B 2  1220 GLN 1220 1220 1220 GLN GLN B . n 
B 2  1221 HIS 1221 1221 1221 HIS HIS B . n 
B 2  1222 GLU 1222 1222 1222 GLU GLU B . n 
B 2  1223 MET 1223 1223 1223 MET MET B . n 
B 2  1224 ARG 1224 1224 1224 ARG ARG B . n 
B 2  1225 ALA 1225 1225 1225 ALA ALA B . n 
B 2  1226 ALA 1226 1226 1226 ALA ALA B . n 
B 2  1227 ASN 1227 1227 1227 ASN ASN B . n 
B 2  1228 VAL 1228 1228 1228 VAL VAL B . n 
B 2  1229 ASN 1229 1229 1229 ASN ASN B . n 
B 2  1230 ILE 1230 1230 1230 ILE ILE B . n 
B 2  1231 THR 1231 1231 1231 THR THR B . n 
B 2  1232 SER 1232 1232 1232 SER SER B . n 
B 2  1233 VAL 1233 1233 1233 VAL VAL B . n 
B 2  1234 LEU 1234 1234 1234 LEU LEU B . n 
B 2  1235 SER 1235 1235 1235 SER SER B . n 
B 2  1236 PRO 1236 1236 1236 PRO PRO B . n 
B 2  1237 ARG 1237 1237 1237 ARG ARG B . n 
B 2  1238 VAL 1238 1238 1238 VAL VAL B . n 
B 2  1239 PHE 1239 1239 1239 PHE PHE B . n 
B 2  1240 GLN 1240 1240 1240 GLN GLN B . n 
B 2  1241 PRO 1241 1241 1241 PRO PRO B . n 
B 2  1242 ALA 1242 1242 1242 ALA ALA B . n 
C 3  1    MET 1    1    ?    ?   ?   C . n 
C 3  2    GLU 2    2    ?    ?   ?   C . n 
C 3  3    LYS 3    3    3    LYS LYS C . n 
C 3  4    ILE 4    4    4    ILE ILE C . n 
C 3  5    PHE 5    5    5    PHE PHE C . n 
C 3  6    GLN 6    6    6    GLN GLN C . n 
C 3  7    ASN 7    7    7    ASN ASN C . n 
C 3  8    VAL 8    8    8    VAL VAL C . n 
C 3  9    GLU 9    9    9    GLU GLU C . n 
C 3  10   ILE 10   10   10   ILE ILE C . n 
C 3  11   LYS 11   11   11   LYS LYS C . n 
C 3  12   PRO 12   12   12   PRO PRO C . n 
C 3  13   PHE 13   13   13   PHE PHE C . n 
C 3  14   LEU 14   14   14   LEU LEU C . n 
C 3  15   ILE 15   15   15   ILE ILE C . n 
C 3  16   ASP 16   16   16   ASP ASP C . n 
C 3  17   PHE 17   17   17   PHE PHE C . n 
C 3  18   SER 18   18   18   SER SER C . n 
C 3  19   ASN 19   19   19   ASN ASN C . n 
C 3  20   LEU 20   20   20   LEU LEU C . n 
C 3  21   PHE 21   21   21   PHE PHE C . n 
C 3  22   ILE 22   22   22   ILE ILE C . n 
C 3  23   LYS 23   23   23   LYS LYS C . n 
C 3  24   ASN 24   24   24   ASN ASN C . n 
C 3  25   ALA 25   25   25   ALA ALA C . n 
C 3  26   ALA 26   26   26   ALA ALA C . n 
C 3  27   LYS 27   27   27   LYS LYS C . n 
C 3  28   LYS 28   28   28   LYS LYS C . n 
C 3  29   LEU 29   29   29   LEU LEU C . n 
C 3  30   PHE 30   30   30   PHE PHE C . n 
C 3  31   GLN 31   31   31   GLN GLN C . n 
C 3  32   LEU 32   32   32   LEU LEU C . n 
C 3  33   GLU 33   33   33   GLU GLU C . n 
C 3  34   GLU 34   34   34   GLU GLU C . n 
C 3  35   GLN 35   35   35   GLN GLN C . n 
C 3  36   LEU 36   36   36   LEU LEU C . n 
C 3  37   PRO 37   37   37   PRO PRO C . n 
C 3  38   LEU 38   38   38   LEU LEU C . n 
C 3  39   VAL 39   39   39   VAL VAL C . n 
C 3  40   PRO 40   40   40   PRO PRO C . n 
C 3  41   VAL 41   41   41   VAL VAL C . n 
C 3  42   ASN 42   42   42   ASN ASN C . n 
C 3  43   VAL 43   43   43   VAL VAL C . n 
C 3  44   VAL 44   44   44   VAL VAL C . n 
C 3  45   MET 45   45   45   MET MET C . n 
C 3  46   ASP 46   46   46   ASP ASP C . n 
C 3  47   PHE 47   47   47   PHE PHE C . n 
C 3  48   LYS 48   48   48   LYS LYS C . n 
C 3  49   GLY 49   49   49   GLY GLY C . n 
C 3  50   ILE 50   50   50   ILE ILE C . n 
C 3  51   SER 51   51   51   SER SER C . n 
C 3  52   ARG 52   52   52   ARG ARG C . n 
C 3  53   ALA 53   53   53   ALA ALA C . n 
C 3  54   ALA 54   54   54   ALA ALA C . n 
C 3  55   VAL 55   55   55   VAL VAL C . n 
C 3  56   HIS 56   56   56   HIS HIS C . n 
C 3  57   GLY 57   57   57   GLY GLY C . n 
C 3  58   LEU 58   58   58   LEU LEU C . n 
C 3  59   SER 59   59   59   SER SER C . n 
C 3  60   ARG 60   60   60   ARG ARG C . n 
C 3  61   VAL 61   61   61   VAL VAL C . n 
C 3  62   LEU 62   62   62   LEU LEU C . n 
C 3  63   GLN 63   63   63   GLN GLN C . n 
C 3  64   ASP 64   64   64   ASP ASP C . n 
C 3  65   GLU 65   65   65   GLU GLU C . n 
C 3  66   ILE 66   66   66   ILE ILE C . n 
C 3  67   PRO 67   67   67   PRO PRO C . n 
C 3  68   ASN 68   68   68   ASN ASN C . n 
C 3  69   TYR 69   69   69   TYR TYR C . n 
C 3  70   MET 70   70   70   MET MET C . n 
C 3  71   LEU 71   71   71   LEU LEU C . n 
C 3  72   ASP 72   72   72   ASP ASP C . n 
C 3  73   ILE 73   73   73   ILE ILE C . n 
C 3  74   LYS 74   74   74   LYS LYS C . n 
C 3  75   PRO 75   75   75   PRO PRO C . n 
C 3  76   GLY 76   76   76   GLY GLY C . n 
C 3  77   GLY 77   77   77   GLY GLY C . n 
C 3  78   TYR 78   78   78   TYR TYR C . n 
C 3  79   LYS 79   79   79   LYS LYS C . n 
C 3  80   ILE 80   80   80   ILE ILE C . n 
C 3  81   GLU 81   81   81   GLU GLU C . n 
C 3  82   ASP 82   82   82   ASP ASP C . n 
C 3  83   SER 83   83   83   SER SER C . n 
C 3  84   THR 84   84   84   THR THR C . n 
C 3  85   ASP 85   85   85   ASP ASP C . n 
C 3  86   LEU 86   86   86   LEU LEU C . n 
C 3  87   PHE 87   87   87   PHE PHE C . n 
C 3  88   MET 88   88   88   MET MET C . n 
C 3  89   THR 89   89   89   THR THR C . n 
C 3  90   GLU 90   90   90   GLU GLU C . n 
C 3  91   GLN 91   91   91   GLN GLN C . n 
C 3  92   PHE 92   92   92   PHE PHE C . n 
C 3  93   ILE 93   93   93   ILE ILE C . n 
C 3  94   ARG 94   94   94   ARG ARG C . n 
C 3  95   ASN 95   95   95   ASN ASN C . n 
C 3  96   ARG 96   96   96   ARG ARG C . n 
C 3  97   ILE 97   97   97   ILE ILE C . n 
C 3  98   ASN 98   98   98   ASN ASN C . n 
C 3  99   PHE 99   99   99   PHE PHE C . n 
C 3  100  ILE 100  100  100  ILE ILE C . n 
C 3  101  PRO 101  101  101  PRO PRO C . n 
C 3  102  ILE 102  102  102  ILE ILE C . n 
C 3  103  TYR 103  103  103  TYR TYR C . n 
C 3  104  ALA 104  104  104  ALA ALA C . n 
C 3  105  LYS 105  105  105  LYS LYS C . n 
C 3  106  ASN 106  106  106  ASN ASN C . n 
C 3  107  GLU 107  107  107  GLU GLU C . n 
C 3  108  THR 108  108  108  THR THR C . n 
C 3  109  LEU 109  109  109  LEU LEU C . n 
C 3  110  VAL 110  110  110  VAL VAL C . n 
C 3  111  PHE 111  111  111  PHE PHE C . n 
C 3  112  ALA 112  112  112  ALA ALA C . n 
C 3  113  LEU 113  113  113  LEU LEU C . n 
C 3  114  ARG 114  114  114  ARG ARG C . n 
C 3  115  SER 115  115  115  SER SER C . n 
C 3  116  LEU 116  116  116  LEU LEU C . n 
C 3  117  ASN 117  117  117  ASN ASN C . n 
C 3  118  ASN 118  118  118  ASN ASN C . n 
C 3  119  SER 119  119  119  SER SER C . n 
C 3  120  CYS 120  120  120  CYS CYS C . n 
C 3  121  GLU 121  121  121  GLU GLU C . n 
C 3  122  VAL 122  122  122  VAL VAL C . n 
C 3  123  LYS 123  123  123  LYS LYS C . n 
C 3  124  THR 124  124  124  THR THR C . n 
C 3  125  ILE 125  125  125  ILE ILE C . n 
C 3  126  TYR 126  126  126  TYR TYR C . n 
C 3  127  SER 127  127  127  SER SER C . n 
C 3  128  ARG 128  128  128  ARG ARG C . n 
C 3  129  ASP 129  129  129  ASP ASP C . n 
C 3  130  LEU 130  130  130  LEU LEU C . n 
C 3  131  ILE 131  131  131  ILE ILE C . n 
C 3  132  GLN 132  132  132  GLN GLN C . n 
C 3  133  VAL 133  133  133  VAL VAL C . n 
C 3  134  ALA 134  134  134  ALA ALA C . n 
C 3  135  GLY 135  135  135  GLY GLY C . n 
C 3  136  PRO 136  136  136  PRO PRO C . n 
C 3  137  LYS 137  137  137  LYS LYS C . n 
C 3  138  LEU 138  138  138  LEU LEU C . n 
C 3  139  LYS 139  139  139  LYS LYS C . n 
C 3  140  TYR 140  140  140  TYR TYR C . n 
C 3  141  PRO 141  141  141  PRO PRO C . n 
C 3  142  ILE 142  142  142  ILE ILE C . n 
C 3  143  PHE 143  143  143  PHE PHE C . n 
C 3  144  ASN 144  144  144  ASN ASN C . n 
C 3  145  PRO 145  145  145  PRO PRO C . n 
C 3  146  THR 146  146  146  THR THR C . n 
C 3  147  PHE 147  147  147  PHE PHE C . n 
C 3  148  GLU 148  148  148  GLU GLU C . n 
C 3  149  ILE 149  149  149  ILE ILE C . n 
C 3  150  GLY 150  150  150  GLY GLY C . n 
C 3  151  PHE 151  151  151  PHE PHE C . n 
C 3  152  LEU 152  152  152  LEU LEU C . n 
C 3  153  GLN 153  153  153  GLN GLN C . n 
C 3  154  PRO 154  154  154  PRO PRO C . n 
C 3  155  GLY 155  155  155  GLY GLY C . n 
C 3  156  LYS 156  156  156  LYS LYS C . n 
C 3  157  SER 157  157  157  SER SER C . n 
C 3  158  LEU 158  158  158  LEU LEU C . n 
C 3  159  ILE 159  159  159  ILE ILE C . n 
C 3  160  ILE 160  160  160  ILE ILE C . n 
C 3  161  GLU 161  161  161  GLU GLU C . n 
C 3  162  ASP 162  162  162  ASP ASP C . n 
C 3  163  ILE 163  163  163  ILE ILE C . n 
C 3  164  TYR 164  164  164  TYR TYR C . n 
C 3  165  ILE 165  165  165  ILE ILE C . n 
C 3  166  LYS 166  166  166  LYS LYS C . n 
C 3  167  LYS 167  167  167  LYS LYS C . n 
C 3  168  GLY 168  168  168  GLY GLY C . n 
C 3  169  ILE 169  169  169  ILE ILE C . n 
C 3  170  GLY 170  170  170  GLY GLY C . n 
C 3  171  ARG 171  171  171  ARG ARG C . n 
C 3  172  LYS 172  172  172  LYS LYS C . n 
C 3  173  HIS 173  173  173  HIS HIS C . n 
C 3  174  ALA 174  174  174  ALA ALA C . n 
C 3  175  ALA 175  175  175  ALA ALA C . n 
C 3  176  PHE 176  176  176  PHE PHE C . n 
C 3  177  ASN 177  177  177  ASN ASN C . n 
C 3  178  LEU 178  178  178  LEU LEU C . n 
C 3  179  ALA 179  179  179  ALA ALA C . n 
C 3  180  VAL 180  180  180  VAL VAL C . n 
C 3  181  LYS 181  181  181  LYS LYS C . n 
C 3  182  THR 182  182  182  THR THR C . n 
C 3  183  HIS 183  183  183  HIS HIS C . n 
C 3  184  PHE 184  184  184  PHE PHE C . n 
C 3  185  SER 185  185  185  SER SER C . n 
C 3  186  HIS 186  186  186  HIS HIS C . n 
C 3  187  LEU 187  187  187  LEU LEU C . n 
C 3  188  ASP 188  188  188  ASP ASP C . n 
C 3  189  ILE 189  189  189  ILE ILE C . n 
C 3  190  GLU 190  190  190  GLU GLU C . n 
C 3  191  GLN 191  191  191  GLN GLN C . n 
C 3  192  TYR 192  192  192  TYR TYR C . n 
C 3  193  PRO 193  193  193  PRO PRO C . n 
C 3  194  THR 194  194  194  THR THR C . n 
C 3  195  ASP 195  195  195  ASP ASP C . n 
C 3  196  LYS 196  196  196  LYS LYS C . n 
C 3  197  LYS 197  197  197  LYS LYS C . n 
C 3  198  GLU 198  198  198  GLU GLU C . n 
C 3  199  TYR 199  199  199  TYR TYR C . n 
C 3  200  MET 200  200  200  MET MET C . n 
C 3  201  ALA 201  201  201  ALA ALA C . n 
C 3  202  LEU 202  202  202  LEU LEU C . n 
C 3  203  SER 203  203  203  SER SER C . n 
C 3  204  GLY 204  204  204  GLY GLY C . n 
C 3  205  TYR 205  205  205  TYR TYR C . n 
C 3  206  LYS 206  206  206  LYS LYS C . n 
C 3  207  GLN 207  207  207  GLN GLN C . n 
C 3  208  SER 208  208  208  SER SER C . n 
C 3  209  SER 209  209  209  SER SER C . n 
C 3  210  MET 210  210  210  MET MET C . n 
C 3  211  THR 211  211  211  THR THR C . n 
C 3  212  SER 212  212  212  SER SER C . n 
C 3  213  ASP 213  213  213  ASP ASP C . n 
C 3  214  PRO 214  214  214  PRO PRO C . n 
C 3  215  ARG 215  215  215  ARG ARG C . n 
C 3  216  HIS 216  216  216  HIS HIS C . n 
C 3  217  HIS 217  217  217  HIS HIS C . n 
C 3  218  ARG 218  218  218  ARG ARG C . n 
C 3  219  LEU 219  219  219  LEU LEU C . n 
C 3  220  GLY 220  220  220  GLY GLY C . n 
C 3  221  LEU 221  221  221  LEU LEU C . n 
C 3  222  CYS 222  222  222  CYS CYS C . n 
C 3  223  PHE 223  223  223  PHE PHE C . n 
C 3  224  PRO 224  224  224  PRO PRO C . n 
C 3  225  ALA 225  225  225  ALA ALA C . n 
C 3  226  VAL 226  226  226  VAL VAL C . n 
C 3  227  PRO 227  227  227  PRO PRO C . n 
C 3  228  LEU 228  228  228  LEU LEU C . n 
C 3  229  PRO 229  229  229  PRO PRO C . n 
C 3  230  HIS 230  230  230  HIS HIS C . n 
C 3  231  ILE 231  231  231  ILE ILE C . n 
C 3  232  ASN 232  232  232  ASN ASN C . n 
C 3  233  GLN 233  233  233  GLN GLN C . n 
C 3  234  ALA 234  234  234  ALA ALA C . n 
C 3  235  VAL 235  235  235  VAL VAL C . n 
C 3  236  ARG 236  236  236  ARG ARG C . n 
C 3  237  THR 237  237  237  THR THR C . n 
C 3  238  TYR 238  238  238  TYR TYR C . n 
C 3  239  LEU 239  239  239  LEU LEU C . n 
C 3  240  LYS 240  240  240  LYS LYS C . n 
C 3  241  ASN 241  241  241  ASN ASN C . n 
C 3  242  ALA 242  242  242  ALA ALA C . n 
C 3  243  CYS 243  243  243  CYS CYS C . n 
C 3  244  ARG 244  244  244  ARG ARG C . n 
C 3  245  ILE 245  245  245  ILE ILE C . n 
C 3  246  ILE 246  246  246  ILE ILE C . n 
C 3  247  ILE 247  247  247  ILE ILE C . n 
C 3  248  GLY 248  248  248  GLY GLY C . n 
C 3  249  ARG 249  249  249  ARG ARG C . n 
C 3  250  ILE 250  250  250  ILE ILE C . n 
C 3  251  GLN 251  251  251  GLN GLN C . n 
C 3  252  SER 252  252  252  SER SER C . n 
C 3  253  ILE 253  253  253  ILE ILE C . n 
C 3  254  GLN 254  254  254  GLN GLN C . n 
C 3  255  LYS 255  255  255  LYS LYS C . n 
C 3  256  ILE 256  256  256  ILE ILE C . n 
C 3  257  TYR 257  257  257  TYR TYR C . n 
C 3  258  GLU 258  258  258  GLU GLU C . n 
C 3  259  ASN 259  259  259  ASN ASN C . n 
C 3  260  PHE 260  260  260  PHE PHE C . n 
C 3  261  GLU 261  261  261  GLU GLU C . n 
C 3  262  GLU 262  262  262  GLU GLU C . n 
C 3  263  PRO 263  263  263  PRO PRO C . n 
C 3  264  GLN 264  264  264  GLN GLN C . n 
C 3  265  PRO 265  265  265  PRO PRO C . n 
C 3  266  GLU 266  266  266  GLU GLU C . n 
C 3  267  LEU 267  267  267  LEU LEU C . n 
C 3  268  VAL 268  268  268  VAL VAL C . n 
C 3  269  LEU 269  269  269  LEU LEU C . n 
C 3  270  PHE 270  270  270  PHE PHE C . n 
C 3  271  SER 271  271  271  SER SER C . n 
C 3  272  MET 272  272  272  MET MET C . n 
C 3  273  ASP 273  273  273  ASP ASP C . n 
C 3  274  GLU 274  274  274  GLU GLU C . n 
C 3  275  GLU 275  275  275  GLU GLU C . n 
C 3  276  LYS 276  276  276  LYS LYS C . n 
C 3  277  THR 277  277  277  THR THR C . n 
C 3  278  LYS 278  278  278  LYS LYS C . n 
C 3  279  ALA 279  279  279  ALA ALA C . n 
C 3  280  ILE 280  280  280  ILE ILE C . n 
C 3  281  ILE 281  281  281  ILE ILE C . n 
C 3  282  THR 282  282  282  THR THR C . n 
C 3  283  ILE 283  283  283  ILE ILE C . n 
C 3  284  LYS 284  284  284  LYS LYS C . n 
C 3  285  ASP 285  285  285  ASP ASP C . n 
C 3  286  GLU 286  286  286  GLU GLU C . n 
C 3  287  THR 287  287  287  THR THR C . n 
C 3  288  HIS 288  288  288  HIS HIS C . n 
C 3  289  THR 289  289  289  THR THR C . n 
C 3  290  ILE 290  290  290  ILE ILE C . n 
C 3  291  GLY 291  291  291  GLY GLY C . n 
C 3  292  ASN 292  292  292  ASN ASN C . n 
C 3  293  LEU 293  293  293  LEU LEU C . n 
C 3  294  LEU 294  294  294  LEU LEU C . n 
C 3  295  LYS 295  295  295  LYS LYS C . n 
C 3  296  THR 296  296  296  THR THR C . n 
C 3  297  TYR 297  297  297  TYR TYR C . n 
C 3  298  ILE 298  298  298  ILE ILE C . n 
C 3  299  TYR 299  299  299  TYR TYR C . n 
C 3  300  GLU 300  300  300  GLU GLU C . n 
C 3  301  MET 301  301  301  MET MET C . n 
C 3  302  ILE 302  302  302  ILE ILE C . n 
C 3  303  PRO 303  303  303  PRO PRO C . n 
C 3  304  ASP 304  304  304  ASP ASP C . n 
C 3  305  ILE 305  305  305  ILE ILE C . n 
C 3  306  SER 306  306  306  SER SER C . n 
C 3  307  PHE 307  307  307  PHE PHE C . n 
C 3  308  VAL 308  308  308  VAL VAL C . n 
C 3  309  GLY 309  309  309  GLY GLY C . n 
C 3  310  TYR 310  310  310  TYR TYR C . n 
C 3  311  GLN 311  311  311  GLN GLN C . n 
C 3  312  CYS 312  312  312  CYS CYS C . n 
C 3  313  VAL 313  313  313  VAL VAL C . n 
C 3  314  PRO 314  314  314  PRO PRO C . n 
C 3  315  HIS 315  315  315  HIS HIS C . n 
C 3  316  LYS 316  316  316  LYS LYS C . n 
C 3  317  GLN 317  317  317  GLN GLN C . n 
C 3  318  GLU 318  318  318  GLU GLU C . n 
C 3  319  MET 319  319  319  MET MET C . n 
C 3  320  VAL 320  320  320  VAL VAL C . n 
C 3  321  LEU 321  321  321  LEU LEU C . n 
C 3  322  THR 322  322  322  THR THR C . n 
C 3  323  ILE 323  323  323  ILE ILE C . n 
C 3  324  ILE 324  324  324  ILE ILE C . n 
C 3  325  HIS 325  325  325  HIS HIS C . n 
C 3  326  LYS 326  326  326  LYS LYS C . n 
C 3  327  ALA 327  327  327  ALA ALA C . n 
C 3  328  SER 328  328  328  SER SER C . n 
C 3  329  GLN 329  329  329  GLN GLN C . n 
C 3  330  GLU 330  330  330  GLU GLU C . n 
C 3  331  ASP 331  331  331  ASP ASP C . n 
C 3  332  LEU 332  332  332  LEU LEU C . n 
C 3  333  ILE 333  333  333  ILE ILE C . n 
C 3  334  THR 334  334  334  THR THR C . n 
C 3  335  LEU 335  335  335  LEU LEU C . n 
C 3  336  LEU 336  336  336  LEU LEU C . n 
C 3  337  GLU 337  337  337  GLU GLU C . n 
C 3  338  LYS 338  338  338  LYS LYS C . n 
C 3  339  SER 339  339  339  SER SER C . n 
C 3  340  ILE 340  340  340  ILE ILE C . n 
C 3  341  GLN 341  341  341  GLN GLN C . n 
C 3  342  ASN 342  342  342  ASN ASN C . n 
C 3  343  ILE 343  343  343  ILE ILE C . n 
C 3  344  ILE 344  344  344  ILE ILE C . n 
C 3  345  GLN 345  345  345  GLN GLN C . n 
C 3  346  THR 346  346  346  THR THR C . n 
C 3  347  PHE 347  347  347  PHE PHE C . n 
C 3  348  GLN 348  348  348  GLN GLN C . n 
C 3  349  ILE 349  349  349  ILE ILE C . n 
C 3  350  LEU 350  350  350  LEU LEU C . n 
C 3  351  GLU 351  351  351  GLU GLU C . n 
C 3  352  LYS 352  352  352  LYS LYS C . n 
C 3  353  ASN 353  353  353  ASN ASN C . n 
C 3  354  VAL 354  354  354  VAL VAL C . n 
C 3  355  ASP 355  355  355  ASP ASP C . n 
C 3  356  GLU 356  356  356  GLU GLU C . n 
C 3  357  LEU 357  357  357  LEU LEU C . n 
C 3  358  ILE 358  358  358  ILE ILE C . n 
C 3  359  ALA 359  359  359  ALA ALA C . n 
D 4  1    MET 1    1    1    MET MET D . n 
D 4  2    ALA 2    2    2    ALA ALA D . n 
D 4  3    MET 3    3    3    MET MET D . n 
D 4  4    GLN 4    4    4    GLN GLN D . n 
D 4  5    LYS 5    5    5    LYS LYS D . n 
D 4  6    LEU 6    6    6    LEU LEU D . n 
D 4  7    PHE 7    7    7    PHE PHE D . n 
D 4  8    THR 8    8    8    THR THR D . n 
D 4  9    TYR 9    9    9    TYR TYR D . n 
D 4  10   ILE 10   10   10   ILE ILE D . n 
D 4  11   TYR 11   11   11   TYR TYR D . n 
D 4  12   GLU 12   12   12   GLU GLU D . n 
D 4  13   PHE 13   13   13   PHE PHE D . n 
D 4  14   ILE 14   14   14   ILE ILE D . n 
D 4  15   GLU 15   15   15   GLU GLU D . n 
D 4  16   TYR 16   16   16   TYR TYR D . n 
D 4  17   ARG 17   17   17   ARG ARG D . n 
D 4  18   LYS 18   18   18   LYS LYS D . n 
D 4  19   MET 19   19   19   MET MET D . n 
D 4  20   VAL 20   20   20   VAL VAL D . n 
D 4  21   LEU 21   21   21   LEU LEU D . n 
D 4  22   LEU 22   22   22   LEU LEU D . n 
D 4  23   GLU 23   23   23   GLU GLU D . n 
D 4  24   GLU 24   24   24   GLU GLU D . n 
D 4  25   LYS 25   25   25   LYS LYS D . n 
D 4  26   VAL 26   26   26   VAL VAL D . n 
D 4  27   PRO 27   27   27   PRO PRO D . n 
D 4  28   TYR 28   28   28   TYR TYR D . n 
D 4  29   ASP 29   29   29   ASP ASP D . n 
D 4  30   LYS 30   30   30   LYS LYS D . n 
D 4  31   PHE 31   31   31   PHE PHE D . n 
D 4  32   VAL 32   32   32   VAL VAL D . n 
D 4  33   GLN 33   33   33   GLN GLN D . n 
D 4  34   MET 34   34   34   MET MET D . n 
D 4  35   VAL 35   35   35   VAL VAL D . n 
D 4  36   LEU 36   36   36   LEU LEU D . n 
D 4  37   ASN 37   37   37   ASN ASN D . n 
D 4  38   THR 38   38   38   THR THR D . n 
D 4  39   GLY 39   39   39   GLY GLY D . n 
D 4  40   PHE 40   40   40   PHE PHE D . n 
D 4  41   PHE 41   41   41   PHE PHE D . n 
D 4  42   ARG 42   42   42   ARG ARG D . n 
D 4  43   ILE 43   43   43   ILE ILE D . n 
D 4  44   ASN 44   44   44   ASN ASN D . n 
D 4  45   ALA 45   45   45   ALA ALA D . n 
D 4  46   GLU 46   46   46   GLU GLU D . n 
D 4  47   THR 47   47   47   THR THR D . n 
D 4  48   LEU 48   48   48   LEU LEU D . n 
D 4  49   ASN 49   49   49   ASN ASN D . n 
D 4  50   HIS 50   50   50   HIS HIS D . n 
D 4  51   GLY 51   51   51   GLY GLY D . n 
D 4  52   ILE 52   52   52   ILE ILE D . n 
D 4  53   VAL 53   53   53   VAL VAL D . n 
D 4  54   SER 54   54   54   SER SER D . n 
D 4  55   VAL 55   55   55   VAL VAL D . n 
D 4  56   PHE 56   56   56   PHE PHE D . n 
D 4  57   ILE 57   57   57   ILE ILE D . n 
D 4  58   PHE 58   58   58   PHE PHE D . n 
D 4  59   GLY 59   59   59   GLY GLY D . n 
D 4  60   ALA 60   60   60   ALA ALA D . n 
D 4  61   ASN 61   61   61   ASN ASN D . n 
D 4  62   GLY 62   62   62   GLY GLY D . n 
D 4  63   LYS 63   63   63   LYS LYS D . n 
D 4  64   TYR 64   64   64   TYR TYR D . n 
D 4  65   VAL 65   65   65   VAL VAL D . n 
D 4  66   HIS 66   66   66   HIS HIS D . n 
D 4  67   HIS 67   67   67   HIS HIS D . n 
D 4  68   GLY 68   68   68   GLY GLY D . n 
D 4  69   GLY 69   69   69   GLY GLY D . n 
D 4  70   ASP 70   70   70   ASP ASP D . n 
D 4  71   MET 71   71   71   MET MET D . n 
D 4  72   ARG 72   72   72   ARG ARG D . n 
D 4  73   THR 73   73   73   THR THR D . n 
D 4  74   LEU 74   74   74   LEU LEU D . n 
D 4  75   LEU 75   75   75   LEU LEU D . n 
D 4  76   THR 76   76   76   THR THR D . n 
D 4  77   ASN 77   77   77   ASN ASN D . n 
D 4  78   THR 78   78   78   THR THR D . n 
D 4  79   LEU 79   79   79   LEU LEU D . n 
D 4  80   ASN 80   80   80   ASN ASN D . n 
D 4  81   GLU 81   81   81   GLU GLU D . n 
D 4  82   LYS 82   82   82   LYS LYS D . n 
D 4  83   LYS 83   83   83   LYS LYS D . n 
D 4  84   HIS 84   84   84   HIS HIS D . n 
D 4  85   TYR 85   85   85   TYR TYR D . n 
D 4  86   GLU 86   86   86   GLU GLU D . n 
D 4  87   GLU 87   87   87   GLU GLU D . n 
D 4  88   LEU 88   88   88   LEU LEU D . n 
D 4  89   ILE 89   89   89   ILE ILE D . n 
D 4  90   LEU 90   90   90   LEU LEU D . n 
D 4  91   ILE 91   91   91   ILE ILE D . n 
D 4  92   VAL 92   92   92   VAL VAL D . n 
D 4  93   ASP 93   93   93   ASP ASP D . n 
D 4  94   LYS 94   94   94   LYS LYS D . n 
D 4  95   PRO 95   95   95   PRO PRO D . n 
D 4  96   VAL 96   96   96   VAL VAL D . n 
D 4  97   LEU 97   97   97   LEU LEU D . n 
D 4  98   SER 98   98   98   SER SER D . n 
D 4  99   LYS 99   99   99   LYS LYS D . n 
D 4  100  LYS 100  100  100  LYS LYS D . n 
D 4  101  ASN 101  101  101  ASN ASN D . n 
D 4  102  ILE 102  102  102  ILE ILE D . n 
D 4  103  LEU 103  103  103  LEU LEU D . n 
D 4  104  ASP 104  104  104  ASP ASP D . n 
D 4  105  ILE 105  105  105  ILE ILE D . n 
D 4  106  ILE 106  106  106  ILE ILE D . n 
D 4  107  VAL 107  107  107  VAL VAL D . n 
D 4  108  GLU 108  108  108  GLU GLU D . n 
D 4  109  GLN 109  109  109  GLN GLN D . n 
D 4  110  ARG 110  110  110  ARG ARG D . n 
D 4  111  ALA 111  111  111  ALA ALA D . n 
D 4  112  ALA 112  112  112  ALA ALA D . n 
D 4  113  ASN 113  113  113  ASN ASN D . n 
D 4  114  PRO 114  114  114  PRO PRO D . n 
D 4  115  THR 115  115  115  THR THR D . n 
D 4  116  ILE 116  116  116  ILE ILE D . n 
D 4  117  VAL 117  117  117  VAL VAL D . n 
D 4  118  ILE 118  118  118  ILE ILE D . n 
D 4  119  ASN 119  119  119  ASN ASN D . n 
D 4  120  ILE 120  120  120  ILE ILE D . n 
D 4  121  TYR 121  121  121  TYR TYR D . n 
D 4  122  PRO 122  122  122  PRO PRO D . n 
D 4  123  TYR 123  123  123  TYR TYR D . n 
D 4  124  HIS 124  124  124  HIS HIS D . n 
D 4  125  LEU 125  125  125  LEU LEU D . n 
D 4  126  PHE 126  126  126  PHE PHE D . n 
D 4  127  CYS 127  127  127  CYS CYS D . n 
D 4  128  ILE 128  128  128  ILE ILE D . n 
D 4  129  ASN 129  129  129  ASN ASN D . n 
D 4  130  ILE 130  130  130  ILE ILE D . n 
D 4  131  PRO 131  131  131  PRO PRO D . n 
D 4  132  LYS 132  132  132  LYS LYS D . n 
D 4  133  VAL 133  133  133  VAL VAL D . n 
D 4  134  SER 134  134  134  SER SER D . n 
D 4  135  ALA 135  135  135  ALA ALA D . n 
D 4  136  ILE 136  136  136  ILE ILE D . n 
D 4  137  PRO 137  137  137  PRO PRO D . n 
D 4  138  LYS 138  138  138  LYS LYS D . n 
D 4  139  HIS 139  139  139  HIS HIS D . n 
D 4  140  LYS 140  140  140  LYS LYS D . n 
D 4  141  LEU 141  141  141  LEU LEU D . n 
D 4  142  ILE 142  142  142  ILE ILE D . n 
D 4  143  THR 143  143  143  THR THR D . n 
D 4  144  GLN 144  144  144  GLN GLN D . n 
D 4  145  GLU 145  145  145  GLU GLU D . n 
D 4  146  GLU 146  146  146  GLU GLU D . n 
D 4  147  ALA 147  147  147  ALA ALA D . n 
D 4  148  GLN 148  148  148  GLN GLN D . n 
D 4  149  GLU 149  149  149  GLU GLU D . n 
D 4  150  PHE 150  150  150  PHE PHE D . n 
D 4  151  LEU 151  151  151  LEU LEU D . n 
D 4  152  GLY 152  152  152  GLY GLY D . n 
D 4  153  ARG 153  153  153  ARG ARG D . n 
D 4  154  GLU 154  154  154  GLU GLU D . n 
D 4  155  TYR 155  155  155  TYR TYR D . n 
D 4  156  LEU 156  156  156  LEU LEU D . n 
D 4  157  GLN 157  157  157  GLN GLN D . n 
D 4  158  PRO 158  158  158  PRO PRO D . n 
D 4  159  GLN 159  159  159  GLN GLN D . n 
D 4  160  ASP 160  160  160  ASP ASP D . n 
D 4  161  LEU 161  161  161  LEU LEU D . n 
D 4  162  MET 162  162  162  MET MET D . n 
D 4  163  GLN 163  163  163  GLN GLN D . n 
D 4  164  ILE 164  164  164  ILE ILE D . n 
D 4  165  SER 165  165  165  SER SER D . n 
D 4  166  ALA 166  166  166  ALA ALA D . n 
D 4  167  SER 167  167  167  SER SER D . n 
D 4  168  ASP 168  168  168  ASP ASP D . n 
D 4  169  PRO 169  169  169  PRO PRO D . n 
D 4  170  PRO 170  170  170  PRO PRO D . n 
D 4  171  VAL 171  171  171  VAL VAL D . n 
D 4  172  VAL 172  172  172  VAL VAL D . n 
D 4  173  TRP 173  173  173  TRP TRP D . n 
D 4  174  LEU 174  174  174  LEU LEU D . n 
D 4  175  GLY 175  175  175  GLY GLY D . n 
D 4  176  GLY 176  176  176  GLY GLY D . n 
D 4  177  ARG 177  177  177  ARG ARG D . n 
D 4  178  PRO 178  178  178  PRO PRO D . n 
D 4  179  GLY 179  179  179  GLY GLY D . n 
D 4  180  ASP 180  180  180  ASP ASP D . n 
D 4  181  PHE 181  181  181  PHE PHE D . n 
D 4  182  VAL 182  182  182  VAL VAL D . n 
D 4  183  GLN 183  183  183  GLN GLN D . n 
D 4  184  ILE 184  184  184  ILE ILE D . n 
D 4  185  GLU 185  185  185  GLU GLU D . n 
D 4  186  ARG 186  186  186  ARG ARG D . n 
D 4  187  PRO 187  187  187  PRO PRO D . n 
D 4  188  SER 188  188  188  SER SER D . n 
D 4  189  GLU 189  189  189  GLU GLU D . n 
D 4  190  THR 190  190  190  THR THR D . n 
D 4  191  ALA 191  191  191  ALA ALA D . n 
D 4  192  MET 192  192  192  MET MET D . n 
D 4  193  HIS 193  193  193  HIS HIS D . n 
D 4  194  ALA 194  194  194  ALA ALA D . n 
D 4  195  VAL 195  195  195  VAL VAL D . n 
D 4  196  VAL 196  196  196  VAL VAL D . n 
D 4  197  ILE 197  197  197  ILE ILE D . n 
D 4  198  ARG 198  198  198  ARG ARG D . n 
D 4  199  PHE 199  199  199  PHE PHE D . n 
D 4  200  ILE 200  200  200  ILE ILE D . n 
D 4  201  THR 201  201  201  THR THR D . n 
D 4  202  LYS 202  202  202  LYS LYS D . n 
D 4  203  SER 203  203  203  SER SER D . n 
D 4  204  LYS 204  204  204  LYS LYS D . n 
D 4  205  ILE 205  205  205  ILE ILE D . n 
E 5  1    MET 1    1    ?    ?   ?   E . n 
E 5  2    ALA 2    2    ?    ?   ?   E . n 
E 5  3    ASP 3    3    ?    ?   ?   E . n 
E 5  4    ASN 4    4    ?    ?   ?   E . n 
E 5  5    ASP 5    5    ?    ?   ?   E . n 
E 5  6    ASN 6    6    ?    ?   ?   E . n 
E 5  7    GLU 7    7    ?    ?   ?   E . n 
E 5  8    ASP 8    8    ?    ?   ?   E . n 
E 5  9    LEU 9    9    ?    ?   ?   E . n 
E 5  10   ILE 10   10   ?    ?   ?   E . n 
E 5  11   MET 11   11   ?    ?   ?   E . n 
E 5  12   ASP 12   12   ?    ?   ?   E . n 
E 5  13   ASP 13   13   ?    ?   ?   E . n 
E 5  14   LEU 14   14   ?    ?   ?   E . n 
E 5  15   VAL 15   15   ?    ?   ?   E . n 
E 5  16   GLU 16   16   ?    ?   ?   E . n 
E 5  17   GLU 17   17   ?    ?   ?   E . n 
E 5  18   TYR 18   18   ?    ?   ?   E . n 
E 5  19   VAL 19   19   ?    ?   ?   E . n 
E 5  20   GLU 20   20   ?    ?   ?   E . n 
E 5  21   THR 21   21   ?    ?   ?   E . n 
E 5  22   GLU 22   22   ?    ?   ?   E . n 
E 5  23   GLU 23   23   ?    ?   ?   E . n 
E 5  24   GLU 24   24   ?    ?   ?   E . n 
E 5  25   ASN 25   25   ?    ?   ?   E . n 
E 5  26   LEU 26   26   ?    ?   ?   E . n 
E 5  27   VAL 27   27   ?    ?   ?   E . n 
E 5  28   ASP 28   28   ?    ?   ?   E . n 
E 5  29   SER 29   29   ?    ?   ?   E . n 
E 5  30   GLU 30   30   ?    ?   ?   E . n 
E 5  31   GLU 31   31   ?    ?   ?   E . n 
E 5  32   GLU 32   32   ?    ?   ?   E . n 
E 5  33   SER 33   33   ?    ?   ?   E . n 
E 5  34   GLU 34   34   ?    ?   ?   E . n 
E 5  35   ASP 35   35   ?    ?   ?   E . n 
E 5  36   LYS 36   36   ?    ?   ?   E . n 
E 5  37   ASP 37   37   ?    ?   ?   E . n 
E 5  38   GLU 38   38   ?    ?   ?   E . n 
E 5  39   ILE 39   39   ?    ?   ?   E . n 
E 5  40   VAL 40   40   ?    ?   ?   E . n 
E 5  41   GLU 41   41   ?    ?   ?   E . n 
E 5  42   SER 42   42   42   SER SER E . n 
E 5  43   PRO 43   43   43   PRO PRO E . n 
E 5  44   SER 44   44   44   SER SER E . n 
E 5  45   ILE 45   45   45   ILE ILE E . n 
E 5  46   CYS 46   46   46   CYS CYS E . n 
E 5  47   GLU 47   47   47   GLU GLU E . n 
E 5  48   GLY 48   48   48   GLY GLY E . n 
E 5  49   PHE 49   49   49   PHE PHE E . n 
E 5  50   VAL 50   50   50   VAL VAL E . n 
E 5  51   GLN 51   51   51   GLN GLN E . n 
E 5  52   ALA 52   52   52   ALA ALA E . n 
E 5  53   SER 53   53   53   SER SER E . n 
E 5  54   SER 54   54   54   SER SER E . n 
E 5  55   GLN 55   55   55   GLN GLN E . n 
E 5  56   THR 56   56   56   THR THR E . n 
E 5  57   LEU 57   57   57   LEU LEU E . n 
E 5  58   VAL 58   58   58   VAL VAL E . n 
E 5  59   ILE 59   59   59   ILE ILE E . n 
E 5  60   ILE 60   60   60   ILE ILE E . n 
E 5  61   PRO 61   61   61   PRO PRO E . n 
E 5  62   ASP 62   62   62   ASP ASP E . n 
E 5  63   ASN 63   63   63   ASN ASN E . n 
E 5  64   GLU 64   64   64   GLU GLU E . n 
E 5  65   ARG 65   65   65   ARG ARG E . n 
E 5  66   ILE 66   66   66   ILE ILE E . n 
E 5  67   THR 67   67   67   THR THR E . n 
E 5  68   SER 68   68   68   SER SER E . n 
E 5  69   ASN 69   69   69   ASN ASN E . n 
E 5  70   VAL 70   70   70   VAL VAL E . n 
E 5  71   LEU 71   71   71   LEU LEU E . n 
E 5  72   THR 72   72   72   THR THR E . n 
E 5  73   THR 73   73   73   THR THR E . n 
E 5  74   PHE 74   74   74   PHE PHE E . n 
E 5  75   GLU 75   75   75   GLU GLU E . n 
E 5  76   ALA 76   76   76   ALA ALA E . n 
E 5  77   THR 77   77   77   THR THR E . n 
E 5  78   ARG 78   78   78   ARG ARG E . n 
E 5  79   LEU 79   79   79   LEU LEU E . n 
E 5  80   VAL 80   80   80   VAL VAL E . n 
E 5  81   ALA 81   81   81   ALA ALA E . n 
E 5  82   VAL 82   82   82   VAL VAL E . n 
E 5  83   ARG 83   83   83   ARG ARG E . n 
E 5  84   ALA 84   84   84   ALA ALA E . n 
E 5  85   GLN 85   85   85   GLN GLN E . n 
E 5  86   GLN 86   86   86   GLN GLN E . n 
E 5  87   LEU 87   87   87   LEU LEU E . n 
E 5  88   ALA 88   88   88   ALA ALA E . n 
E 5  89   ILE 89   89   89   ILE ILE E . n 
E 5  90   ASN 90   90   90   ASN ASN E . n 
E 5  91   GLY 91   91   91   GLY GLY E . n 
E 5  92   SER 92   92   92   SER SER E . n 
E 5  93   THR 93   93   93   THR THR E . n 
E 5  94   MET 94   94   94   MET MET E . n 
E 5  95   LEU 95   95   95   LEU LEU E . n 
E 5  96   LYS 96   96   96   LYS LYS E . n 
E 5  97   LYS 97   97   97   LYS LYS E . n 
E 5  98   LYS 98   98   98   LYS LYS E . n 
E 5  99   TYR 99   99   99   TYR TYR E . n 
E 5  100  SER 100  100  100  SER SER E . n 
E 5  101  SER 101  101  101  SER SER E . n 
E 5  102  PRO 102  102  102  PRO PRO E . n 
E 5  103  ILE 103  103  103  ILE ILE E . n 
E 5  104  ASP 104  104  104  ASP ASP E . n 
E 5  105  ILE 105  105  105  ILE ILE E . n 
E 5  106  ALA 106  106  106  ALA ALA E . n 
E 5  107  LYS 107  107  107  LYS LYS E . n 
E 5  108  GLN 108  108  108  GLN GLN E . n 
E 5  109  GLU 109  109  109  GLU GLU E . n 
E 5  110  LEU 110  110  110  LEU LEU E . n 
E 5  111  PHE 111  111  111  PHE PHE E . n 
E 5  112  ASN 112  112  112  ASN ASN E . n 
E 5  113  ARG 113  113  113  ARG ARG E . n 
E 5  114  LYS 114  114  114  LYS LYS E . n 
E 5  115  ILE 115  115  115  ILE ILE E . n 
E 5  116  PRO 116  116  116  PRO PRO E . n 
E 5  117  LEU 117  117  117  LEU LEU E . n 
E 5  118  LEU 118  118  118  LEU LEU E . n 
E 5  119  VAL 119  119  119  VAL VAL E . n 
E 5  120  MET 120  120  120  MET MET E . n 
E 5  121  ARG 121  121  121  ARG ARG E . n 
E 5  122  CYS 122  122  122  CYS CYS E . n 
E 5  123  ILE 123  123  123  ILE ILE E . n 
E 5  124  LYS 124  124  124  LYS LYS E . n 
E 5  125  VAL 125  125  125  VAL VAL E . n 
E 5  126  THR 126  126  126  THR THR E . n 
E 5  127  PRO 127  127  127  PRO PRO E . n 
E 5  128  GLU 128  128  128  GLU GLU E . n 
E 5  129  GLY 129  129  129  GLY GLY E . n 
E 5  130  GLN 130  130  130  GLN GLN E . n 
E 5  131  LYS 131  131  131  LYS LYS E . n 
E 5  132  ILE 132  132  132  ILE ILE E . n 
E 5  133  VAL 133  133  133  VAL VAL E . n 
E 5  134  GLU 134  134  134  GLU GLU E . n 
E 5  135  ILE 135  135  135  ILE ILE E . n 
E 5  136  TRP 136  136  136  TRP TRP E . n 
E 5  137  ASN 137  137  137  ASN ASN E . n 
E 5  138  PRO 138  138  138  PRO PRO E . n 
E 5  139  ARG 139  139  139  ARG ARG E . n 
E 5  140  GLU 140  140  140  GLU GLU E . n 
E 5  141  MET 141  141  141  MET MET E . n 
E 5  142  GLY 142  142  142  GLY GLY E . n 
E 5  143  ILE 143  143  143  ILE ILE E . n 
E 5  144  PRO 144  144  144  PRO PRO E . n 
E 5  145  LEU 145  145  145  LEU LEU E . n 
E 5  146  LEU 146  146  146  LEU LEU E . n 
E 5  147  ASP 147  147  147  ASP ASP E . n 
F 6  1    MET 1    1    1    MET MET F . n 
F 6  2    ILE 2    2    2    ILE ILE F . n 
F 6  3    ASP 3    3    3    ASP ASP F . n 
F 6  4    GLN 4    4    4    GLN GLN F . n 
F 6  5    LYS 5    5    5    LYS LYS F . n 
F 6  6    ILE 6    6    6    ILE ILE F . n 
F 6  7    PHE 7    7    7    PHE PHE F . n 
F 6  8    GLU 8    8    8    GLU GLU F . n 
F 6  9    THR 9    9    9    THR THR F . n 
F 6  10   THR 10   10   10   THR THR F . n 
F 6  11   LEU 11   11   11   LEU LEU F . n 
F 6  12   ASN 12   12   12   ASN ASN F . n 
F 6  13   ILE 13   13   13   ILE ILE F . n 
F 6  14   ASP 14   14   14   ASP ASP F . n 
F 6  15   ASP 15   15   15   ASP ASP F . n 
F 6  16   PRO 16   16   16   PRO PRO F . n 
F 6  17   THR 17   17   17   THR THR F . n 
F 6  18   ASN 18   18   18   ASN ASN F . n 
F 6  19   PHE 19   19   19   PHE PHE F . n 
F 6  20   CYS 20   20   20   CYS CYS F . n 
F 6  21   THR 21   21   21   THR THR F . n 
F 6  22   ASN 22   22   22   ASN ASN F . n 
F 6  23   VAL 23   23   23   VAL VAL F . n 
F 6  24   GLU 24   24   24   GLU GLU F . n 
F 6  25   ALA 25   25   25   ALA ALA F . n 
F 6  26   HIS 26   26   26   HIS HIS F . n 
F 6  27   LEU 27   27   27   LEU LEU F . n 
F 6  28   LEU 28   28   28   LEU LEU F . n 
F 6  29   LYS 29   29   29   LYS LYS F . n 
F 6  30   GLU 30   30   30   GLU GLU F . n 
F 6  31   LEU 31   31   31   LEU LEU F . n 
F 6  32   GLU 32   32   32   GLU GLU F . n 
F 6  33   ASN 33   33   33   ASN ASN F . n 
F 6  34   ILE 34   34   34   ILE ILE F . n 
F 6  35   TYR 35   35   35   TYR TYR F . n 
F 6  36   VAL 36   36   36   VAL VAL F . n 
F 6  37   GLY 37   37   37   GLY GLY F . n 
F 6  38   LYS 38   38   38   LYS LYS F . n 
F 6  39   CYS 39   39   39   CYS CYS F . n 
F 6  40   PHE 40   40   40   PHE PHE F . n 
F 6  41   LYS 41   41   41   LYS LYS F . n 
F 6  42   ASN 42   42   42   ASN ASN F . n 
F 6  43   SER 43   43   43   SER SER F . n 
F 6  44   PHE 44   44   44   PHE PHE F . n 
F 6  45   ILE 45   45   45   ILE ILE F . n 
F 6  46   LEU 46   46   46   LEU LEU F . n 
F 6  47   ASN 47   47   47   ASN ASN F . n 
F 6  48   ILE 48   48   48   ILE ILE F . n 
F 6  49   THR 49   49   49   THR THR F . n 
F 6  50   GLY 50   50   50   GLY GLY F . n 
F 6  51   VAL 51   51   51   VAL VAL F . n 
F 6  52   ILE 52   52   52   ILE ILE F . n 
F 6  53   GLN 53   53   53   GLN GLN F . n 
F 6  54   ARG 54   54   54   ARG ARG F . n 
F 6  55   SER 55   55   55   SER SER F . n 
F 6  56   PRO 56   56   56   PRO PRO F . n 
F 6  57   CYS 57   57   57   CYS CYS F . n 
F 6  58   PHE 58   58   58   PHE PHE F . n 
F 6  59   ILE 59   59   59   ILE ILE F . n 
F 6  60   MET 60   60   60   MET MET F . n 
F 6  61   ARG 61   61   61   ARG ARG F . n 
F 6  62   THR 62   62   62   THR THR F . n 
F 6  63   ASN 63   63   63   ASN ASN F . n 
F 6  64   ASN 64   64   64   ASN ASN F . n 
F 6  65   SER 65   65   65   SER SER F . n 
F 6  66   GLY 66   66   66   GLY GLY F . n 
F 6  67   ARG 67   67   67   ARG ARG F . n 
F 6  68   GLY 68   68   68   GLY GLY F . n 
F 6  69   TYR 69   69   69   TYR TYR F . n 
F 6  70   MET 70   70   70   MET MET F . n 
F 6  71   HIS 71   71   71   HIS HIS F . n 
F 6  72   VAL 72   72   72   VAL VAL F . n 
F 6  73   ARG 73   73   73   ARG ARG F . n 
F 6  74   PHE 74   74   74   PHE PHE F . n 
F 6  75   SER 75   75   75   SER SER F . n 
F 6  76   ALA 76   76   76   ALA ALA F . n 
F 6  77   VAL 77   77   77   VAL VAL F . n 
F 6  78   VAL 78   78   78   VAL VAL F . n 
F 6  79   SER 79   79   79   SER SER F . n 
F 6  80   TYR 80   80   80   TYR TYR F . n 
F 6  81   LEU 81   81   81   LEU LEU F . n 
F 6  82   ASN 82   82   82   ASN ASN F . n 
F 6  83   ALA 83   83   83   ALA ALA F . n 
F 6  84   PHE 84   84   84   PHE PHE F . n 
F 6  85   ASP 85   85   85   ASP ASP F . n 
F 6  86   LEU 86   86   86   LEU LEU F . n 
F 6  87   ILE 87   87   87   ILE ILE F . n 
F 6  88   ALA 88   88   88   ALA ALA F . n 
F 6  89   ALA 89   89   89   ALA ALA F . n 
F 6  90   VAL 90   90   90   VAL VAL F . n 
F 6  91   LYS 91   91   91   LYS LYS F . n 
F 6  92   ILE 92   92   92   ILE ILE F . n 
F 6  93   ILE 93   93   93   ILE ILE F . n 
F 6  94   LYS 94   94   94   LYS LYS F . n 
F 6  95   ASN 95   95   95   ASN ASN F . n 
F 6  96   ASP 96   96   96   ASP ASP F . n 
F 6  97   SER 97   97   97   SER SER F . n 
F 6  98   ASN 98   98   98   ASN ASN F . n 
F 6  99   ILE 99   99   99   ILE ILE F . n 
F 6  100  ILE 100  100  100  ILE ILE F . n 
F 6  101  LEU 101  101  101  LEU LEU F . n 
F 6  102  GLY 102  102  102  GLY GLY F . n 
F 6  103  GLU 103  103  103  GLU GLU F . n 
F 6  104  SER 104  104  104  SER SER F . n 
F 6  105  LEU 105  105  105  LEU LEU F . n 
F 6  106  LEU 106  106  106  LEU LEU F . n 
F 6  107  THR 107  107  107  THR THR F . n 
F 6  108  GLU 108  108  108  GLU GLU F . n 
F 6  109  PRO 109  109  109  PRO PRO F . n 
F 6  110  VAL 110  110  110  VAL VAL F . n 
F 6  111  THR 111  111  111  THR THR F . n 
F 6  112  ILE 112  112  112  ILE ILE F . n 
F 6  113  VAL 113  113  113  VAL VAL F . n 
F 6  114  ILE 114  114  114  ILE ILE F . n 
F 6  115  PRO 115  115  115  PRO PRO F . n 
F 6  116  SER 116  116  116  SER SER F . n 
F 6  117  SER 117  117  117  SER SER F . n 
F 6  118  GLU 118  118  118  GLU GLU F . n 
F 6  119  SER 119  119  119  SER SER F . n 
F 6  120  GLN 120  120  120  GLN GLN F . n 
F 6  121  ASN 121  121  121  ASN ASN F . n 
F 6  122  ASN 122  122  122  ASN ASN F . n 
F 6  123  VAL 123  123  123  VAL VAL F . n 
F 6  124  ALA 124  124  124  ALA ALA F . n 
F 6  125  GLU 125  125  125  GLU GLU F . n 
F 6  126  VAL 126  126  126  VAL VAL F . n 
F 6  127  GLY 127  127  127  GLY GLY F . n 
F 6  128  GLN 128  128  128  GLN GLN F . n 
F 6  129  ILE 129  129  129  ILE ILE F . n 
F 6  130  VAL 130  130  130  VAL VAL F . n 
F 6  131  PRO 131  131  131  PRO PRO F . n 
F 6  132  VAL 132  132  132  VAL VAL F . n 
F 6  133  GLN 133  133  133  GLN GLN F . n 
F 6  134  LEU 134  134  134  LEU LEU F . n 
F 6  135  ALA 135  135  135  ALA ALA F . n 
F 6  136  ASN 136  136  136  ASN ASN F . n 
F 6  137  SER 137  137  137  SER SER F . n 
F 6  138  SER 138  138  138  SER SER F . n 
F 6  139  VAL 139  139  139  VAL VAL F . n 
F 6  140  TYR 140  140  140  TYR TYR F . n 
F 6  141  TYR 141  141  141  TYR TYR F . n 
F 6  142  ILE 142  142  142  ILE ILE F . n 
F 6  143  PRO 143  143  143  PRO PRO F . n 
F 6  144  GLY 144  144  144  GLY GLY F . n 
F 6  145  ARG 145  145  145  ARG ARG F . n 
F 6  146  GLN 146  146  146  GLN GLN F . n 
F 6  147  GLN 147  147  147  GLN GLN F . n 
F 6  148  ALA 148  148  148  ALA ALA F . n 
F 6  149  SER 149  149  149  SER SER F . n 
F 6  150  ALA 150  150  150  ALA ALA F . n 
F 6  151  THR 151  151  151  THR THR F . n 
F 6  152  GLY 152  152  152  GLY GLY F . n 
F 6  153  SER 153  153  153  SER SER F . n 
F 6  154  ILE 154  154  154  ILE ILE F . n 
F 6  155  PHE 155  155  155  PHE PHE F . n 
F 6  156  ILE 156  156  156  ILE ILE F . n 
F 6  157  PRO 157  157  157  PRO PRO F . n 
F 6  158  LYS 158  158  158  LYS LYS F . n 
F 6  159  HIS 159  159  159  HIS HIS F . n 
F 6  160  THR 160  160  160  THR THR F . n 
F 6  161  PHE 161  161  161  PHE PHE F . n 
F 6  162  SER 162  162  162  SER SER F . n 
F 6  163  VAL 163  163  163  VAL VAL F . n 
F 6  164  TYR 164  164  164  TYR TYR F . n 
F 6  165  HIS 165  165  165  HIS HIS F . n 
F 6  166  VAL 166  166  166  VAL VAL F . n 
F 6  167  GLN 167  167  167  GLN GLN F . n 
F 6  168  GLU 168  168  168  GLU GLU F . n 
F 6  169  GLU 169  169  169  GLU GLU F . n 
F 6  170  LEU 170  170  170  LEU LEU F . n 
F 6  171  THR 171  171  171  THR THR F . n 
F 6  172  GLN 172  172  172  GLN GLN F . n 
F 6  173  GLU 173  173  173  GLU GLU F . n 
F 6  174  GLN 174  174  174  GLN GLN F . n 
F 6  175  ALA 175  175  175  ALA ALA F . n 
F 6  176  LEU 176  176  176  LEU LEU F . n 
F 6  177  ASN 177  177  177  ASN ASN F . n 
F 6  178  LEU 178  178  178  LEU LEU F . n 
F 6  179  THR 179  179  179  THR THR F . n 
F 6  180  LYS 180  180  180  LYS LYS F . n 
F 6  181  LEU 181  181  181  LEU LEU F . n 
F 6  182  VAL 182  182  182  VAL VAL F . n 
F 6  183  ASN 183  183  183  ASN ASN F . n 
F 6  184  ILE 184  184  184  ILE ILE F . n 
F 6  185  ILE 185  185  185  ILE ILE F . n 
F 6  186  GLU 186  186  186  GLU GLU F . n 
F 6  187  MET 187  187  187  MET MET F . n 
F 6  188  LEU 188  188  188  LEU LEU F . n 
F 6  189  LEU 189  189  189  LEU LEU F . n 
F 6  190  GLU 190  190  190  GLU GLU F . n 
F 6  191  SER 191  191  191  SER SER F . n 
F 6  192  ARG 192  192  192  ARG ARG F . n 
F 6  193  SER 193  193  193  SER SER F . n 
F 6  194  LYS 194  194  194  LYS LYS F . n 
F 6  195  LYS 195  195  195  LYS LYS F . n 
F 6  196  ASP 196  196  196  ASP ASP F . n 
F 6  197  PHE 197  197  197  PHE PHE F . n 
F 6  198  LYS 198  198  198  LYS LYS F . n 
F 6  199  GLN 199  199  199  GLN GLN F . n 
F 6  200  ILE 200  200  200  ILE ILE F . n 
F 6  201  CYS 201  201  201  CYS CYS F . n 
F 6  202  PHE 202  202  202  PHE PHE F . n 
F 6  203  PHE 203  203  203  PHE PHE F . n 
F 6  204  GLU 204  204  204  GLU GLU F . n 
F 6  205  LYS 205  205  205  LYS LYS F . n 
F 6  206  LEU 206  206  206  LEU LEU F . n 
F 6  207  TYR 207  207  207  TYR TYR F . n 
F 6  208  TYR 208  208  208  TYR TYR F . n 
F 6  209  THR 209  209  209  THR THR F . n 
F 6  210  TYR 210  210  210  TYR TYR F . n 
F 6  211  SER 211  211  211  SER SER F . n 
F 6  212  ILE 212  212  212  ILE ILE F . n 
F 6  213  SER 213  213  213  SER SER F . n 
F 6  214  SER 214  214  214  SER SER F . n 
F 6  215  ASP 215  215  215  ASP ASP F . n 
F 6  216  GLU 216  216  216  GLU GLU F . n 
F 6  217  ILE 217  217  217  ILE ILE F . n 
F 6  218  LEU 218  218  218  LEU LEU F . n 
F 6  219  ASP 219  219  219  ASP ASP F . n 
F 6  220  LEU 220  220  220  LEU LEU F . n 
F 6  221  LYS 221  221  221  LYS LYS F . n 
F 6  222  ILE 222  222  222  ILE ILE F . n 
F 6  223  TRP 223  223  223  TRP TRP F . n 
F 6  224  LYS 224  224  224  LYS LYS F . n 
F 6  225  GLY 225  225  225  GLY GLY F . n 
F 6  226  PRO 226  226  226  PRO PRO F . n 
F 6  227  LYS 227  227  227  LYS LYS F . n 
F 6  228  GLY 228  228  228  GLY GLY F . n 
F 6  229  LYS 229  229  229  LYS LYS F . n 
F 6  230  GLU 230  230  230  GLU GLU F . n 
F 6  231  MET 231  231  231  MET MET F . n 
F 6  232  SER 232  232  232  SER SER F . n 
F 6  233  ARG 233  233  233  ARG ARG F . n 
F 6  234  LEU 234  234  234  LEU LEU F . n 
F 6  235  LYS 235  235  235  LYS LYS F . n 
F 6  236  PRO 236  236  236  PRO PRO F . n 
F 6  237  CYS 237  237  237  CYS CYS F . n 
F 6  238  ASN 238  238  238  ASN ASN F . n 
F 6  239  VAL 239  239  239  VAL VAL F . n 
F 6  240  LEU 240  240  240  LEU LEU F . n 
F 6  241  SER 241  241  241  SER SER F . n 
F 6  242  PHE 242  242  242  PHE PHE F . n 
F 6  243  LEU 243  243  243  LEU LEU F . n 
F 6  244  TYR 244  244  244  TYR TYR F . n 
F 6  245  ASP 245  245  245  ASP ASP F . n 
F 6  246  ALA 246  246  246  ALA ALA F . n 
F 6  247  LEU 247  247  247  LEU LEU F . n 
F 6  248  LYS 248  248  248  LYS LYS F . n 
F 6  249  ASN 249  249  249  ASN ASN F . n 
F 6  250  LYS 250  250  250  LYS LYS F . n 
F 6  251  ASN 251  251  251  ASN ASN F . n 
F 6  252  SER 252  252  252  SER SER F . n 
F 6  253  SER 253  253  253  SER SER F . n 
F 6  254  LEU 254  254  254  LEU LEU F . n 
F 6  255  GLY 255  255  255  GLY GLY F . n 
F 6  256  PHE 256  256  256  PHE PHE F . n 
F 6  257  TRP 257  257  257  TRP TRP F . n 
F 6  258  ALA 258  258  258  ALA ALA F . n 
F 6  259  ARG 259  259  259  ARG ARG F . n 
F 6  260  PRO 260  260  260  PRO PRO F . n 
F 6  261  PRO 261  261  261  PRO PRO F . n 
F 6  262  ASN 262  262  262  ASN ASN F . n 
F 6  263  LEU 263  263  263  LEU LEU F . n 
F 6  264  LEU 264  264  264  LEU LEU F . n 
F 6  265  LYS 265  265  265  LYS LYS F . n 
F 6  266  SER 266  266  266  SER SER F . n 
F 6  267  SER 267  267  267  SER SER F . n 
F 6  268  PRO 268  268  268  PRO PRO F . n 
F 6  269  LEU 269  269  269  LEU LEU F . n 
F 6  270  ALA 270  270  270  ALA ALA F . n 
F 6  271  TYR 271  271  271  TYR TYR F . n 
F 6  272  GLN 272  272  272  GLN GLN F . n 
F 6  273  GLN 273  273  273  GLN GLN F . n 
F 6  274  ASP 274  274  274  ASP ASP F . n 
F 6  275  GLN 275  275  275  GLN GLN F . n 
F 6  276  ASN 276  276  276  ASN ASN F . n 
F 6  277  SER 277  277  277  SER SER F . n 
F 6  278  PHE 278  278  278  PHE PHE F . n 
F 6  279  ASN 279  279  279  ASN ASN F . n 
F 6  280  ALA 280  280  280  ALA ALA F . n 
F 6  281  THR 281  281  281  THR THR F . n 
F 6  282  GLU 282  282  282  GLU GLU F . n 
F 6  283  LEU 283  283  283  LEU LEU F . n 
F 6  284  PRO 284  284  284  PRO PRO F . n 
F 6  285  ILE 285  285  285  ILE ILE F . n 
F 6  286  ILE 286  286  286  ILE ILE F . n 
F 6  287  CYS 287  287  287  CYS CYS F . n 
F 6  288  SER 288  288  288  SER SER F . n 
F 6  289  ALA 289  289  289  ALA ALA F . n 
F 6  290  GLU 290  290  290  GLU GLU F . n 
F 6  291  VAL 291  291  291  VAL VAL F . n 
F 6  292  MET 292  292  292  MET MET F . n 
F 6  293  PHE 293  293  293  PHE PHE F . n 
F 6  294  VAL 294  294  294  VAL VAL F . n 
F 6  295  THR 295  295  295  THR THR F . n 
F 6  296  LEU 296  296  296  LEU LEU F . n 
F 6  297  LEU 297  297  297  LEU LEU F . n 
F 6  298  LYS 298  298  298  LYS LYS F . n 
F 6  299  GLU 299  299  299  GLU GLU F . n 
F 6  300  ILE 300  300  300  ILE ILE F . n 
F 6  301  ILE 301  301  301  ILE ILE F . n 
F 6  302  ASN 302  302  302  ASN ASN F . n 
F 6  303  TYR 303  303  303  TYR TYR F . n 
F 6  304  LEU 304  304  304  LEU LEU F . n 
F 6  305  GLN 305  305  305  GLN GLN F . n 
F 6  306  PHE 306  306  306  PHE PHE F . n 
F 6  307  ILE 307  307  307  ILE ILE F . n 
F 6  308  ASN 308  308  308  ASN ASN F . n 
F 6  309  ASP 309  309  309  ASP ASP F . n 
F 6  310  LEU 310  310  310  LEU LEU F . n 
F 6  311  CYS 311  311  311  CYS CYS F . n 
F 6  312  ASP 312  312  312  ASP ASP F . n 
F 6  313  THR 313  313  313  THR THR F . n 
F 6  314  PHE 314  314  314  PHE PHE F . n 
F 6  315  ASN 315  315  315  ASN ASN F . n 
F 6  316  ASN 316  316  316  ASN ASN F . n 
F 6  317  GLU 317  317  317  GLU GLU F . n 
F 6  318  GLN 318  318  318  GLN GLN F . n 
F 6  319  LEU 319  319  319  LEU LEU F . n 
F 6  320  ILE 320  320  320  ILE ILE F . n 
F 6  321  LYS 321  321  321  LYS LYS F . n 
F 6  322  ARG 322  322  322  ARG ARG F . n 
F 6  323  HIS 323  323  323  HIS HIS F . n 
F 6  324  GLU 324  324  324  GLU GLU F . n 
F 6  325  ASN 325  325  325  ASN ASN F . n 
F 6  326  ILE 326  326  326  ILE ILE F . n 
F 6  327  TRP 327  327  327  TRP TRP F . n 
F 6  328  MET 328  328  328  MET MET F . n 
F 6  329  LEU 329  329  329  LEU LEU F . n 
F 6  330  ILE 330  330  330  ILE ILE F . n 
F 6  331  GLU 331  331  331  GLU GLU F . n 
F 6  332  GLN 332  332  332  GLN GLN F . n 
F 6  333  ARG 333  333  333  ARG ARG F . n 
F 6  334  LYS 334  334  334  LYS LYS F . n 
F 6  335  ILE 335  335  335  ILE ILE F . n 
F 6  336  GLY 336  336  336  GLY GLY F . n 
F 6  337  HIS 337  337  337  HIS HIS F . n 
F 6  338  ASP 338  338  338  ASP ASP F . n 
F 6  339  PHE 339  339  339  PHE PHE F . n 
G 7  1    MET 1    1    ?    ?   ?   G . n 
G 7  2    LYS 2    2    ?    ?   ?   G . n 
G 7  3    ILE 3    3    ?    ?   ?   G . n 
G 7  4    CYS 4    4    ?    ?   ?   G . n 
G 7  5    LYS 5    5    ?    ?   ?   G . n 
G 7  6    ALA 6    6    ?    ?   ?   G . n 
G 7  7    CYS 7    7    ?    ?   ?   G . n 
G 7  8    SER 8    8    ?    ?   ?   G . n 
G 7  9    SER 9    9    ?    ?   ?   G . n 
G 7  10   CYS 10   10   ?    ?   ?   G . n 
G 7  11   MET 11   11   ?    ?   ?   G . n 
G 7  12   VAL 12   12   ?    ?   ?   G . n 
G 7  13   ARG 13   13   ?    ?   ?   G . n 
G 7  14   THR 14   14   ?    ?   ?   G . n 
G 7  15   TYR 15   15   ?    ?   ?   G . n 
G 7  16   VAL 16   16   ?    ?   ?   G . n 
G 7  17   ASP 17   17   ?    ?   ?   G . n 
G 7  18   GLY 18   18   ?    ?   ?   G . n 
G 7  19   ASN 19   19   ?    ?   ?   G . n 
G 7  20   ILE 20   20   ?    ?   ?   G . n 
G 7  21   ILE 21   21   ?    ?   ?   G . n 
G 7  22   PHE 22   22   ?    ?   ?   G . n 
G 7  23   ARG 23   23   ?    ?   ?   G . n 
G 7  24   CYS 24   24   ?    ?   ?   G . n 
G 7  25   SER 25   25   ?    ?   ?   G . n 
G 7  26   CYS 26   26   ?    ?   ?   G . n 
G 7  27   GLY 27   27   ?    ?   ?   G . n 
G 7  28   GLU 28   28   ?    ?   ?   G . n 
G 7  29   SER 29   29   ?    ?   ?   G . n 
G 7  30   VAL 30   30   ?    ?   ?   G . n 
G 7  31   GLN 31   31   ?    ?   ?   G . n 
G 7  32   GLY 32   32   ?    ?   ?   G . n 
G 7  33   ASP 33   33   ?    ?   ?   G . n 
G 7  34   SER 34   34   ?    ?   ?   G . n 
G 7  35   GLN 35   35   ?    ?   ?   G . n 
G 7  36   ASN 36   36   ?    ?   ?   G . n 
G 7  37   LEU 37   37   ?    ?   ?   G . n 
G 7  38   LEU 38   38   ?    ?   ?   G . n 
G 7  39   VAL 39   39   ?    ?   ?   G . n 
G 7  40   SER 40   40   ?    ?   ?   G . n 
G 7  41   SER 41   41   ?    ?   ?   G . n 
G 7  42   LYS 42   42   ?    ?   ?   G . n 
G 7  43   VAL 43   43   ?    ?   ?   G . n 
G 7  44   TYR 44   44   ?    ?   ?   G . n 
G 7  45   HIS 45   45   ?    ?   ?   G . n 
G 7  46   THR 46   46   ?    ?   ?   G . n 
G 7  47   GLY 47   47   47   GLY GLY G . n 
G 7  48   GLU 48   48   48   GLU GLU G . n 
G 7  49   MET 49   49   49   MET MET G . n 
G 7  50   GLU 50   50   50   GLU GLU G . n 
G 7  51   ASP 51   51   51   ASP ASP G . n 
G 7  52   LYS 52   52   52   LYS LYS G . n 
G 7  53   TYR 53   53   53   TYR TYR G . n 
G 7  54   LYS 54   54   54   LYS LYS G . n 
G 7  55   ILE 55   55   55   ILE ILE G . n 
G 7  56   PHE 56   56   56   PHE PHE G . n 
G 7  57   ILE 57   57   57   ILE ILE G . n 
G 7  58   LYS 58   58   58   LYS LYS G . n 
G 7  59   ASN 59   59   59   ASN ASN G . n 
G 7  60   ALA 60   60   60   ALA ALA G . n 
G 7  61   PRO 61   61   61   PRO PRO G . n 
G 7  62   PHE 62   62   62   PHE PHE G . n 
G 7  63   ASP 63   63   63   ASP ASP G . n 
G 7  64   PRO 64   64   64   PRO PRO G . n 
G 7  65   THR 65   65   65   THR THR G . n 
G 7  66   ASN 66   66   66   ASN ASN G . n 
G 7  67   CYS 67   67   67   CYS CYS G . n 
G 7  68   GLN 68   68   68   GLN GLN G . n 
G 7  69   ILE 69   69   69   ILE ILE G . n 
G 7  70   LYS 70   70   70   LYS LYS G . n 
G 7  71   LYS 71   71   71   LYS LYS G . n 
G 7  72   ASP 72   72   72   ASP ASP G . n 
G 7  73   CYS 73   73   73   CYS CYS G . n 
G 7  74   PRO 74   74   74   PRO PRO G . n 
G 7  75   ASN 75   75   75   ASN ASN G . n 
G 7  76   CYS 76   76   76   CYS CYS G . n 
G 7  77   HIS 77   77   77   HIS HIS G . n 
G 7  78   LEU 78   78   78   LEU LEU G . n 
G 7  79   ASP 79   79   79   ASP ASP G . n 
G 7  80   TYR 80   80   80   TYR TYR G . n 
G 7  81   LEU 81   81   81   LEU LEU G . n 
G 7  82   THR 82   82   82   THR THR G . n 
G 7  83   GLN 83   83   83   GLN GLN G . n 
G 7  84   ILE 84   84   84   ILE ILE G . n 
G 7  85   CYS 85   85   85   CYS CYS G . n 
G 7  86   ILE 86   86   86   ILE ILE G . n 
G 7  87   GLY 87   87   87   GLY GLY G . n 
G 7  88   SER 88   88   88   SER SER G . n 
G 7  89   GLN 89   89   89   GLN GLN G . n 
G 7  90   LYS 90   90   90   LYS LYS G . n 
G 7  91   ILE 91   91   91   ILE ILE G . n 
G 7  92   ILE 92   92   92   ILE ILE G . n 
G 7  93   ILE 93   93   93   ILE ILE G . n 
G 7  94   LEU 94   94   94   LEU LEU G . n 
G 7  95   VAL 95   95   95   VAL VAL G . n 
G 7  96   CYS 96   96   96   CYS CYS G . n 
G 7  97   ARG 97   97   97   ARG ARG G . n 
G 7  98   CYS 98   98   98   CYS CYS G . n 
G 7  99   GLY 99   99   99   GLY GLY G . n 
G 7  100  TYR 100  100  100  TYR TYR G . n 
G 7  101  MET 101  101  101  MET MET G . n 
G 7  102  SER 102  102  102  SER SER G . n 
G 7  103  ASN 103  103  103  ASN ASN G . n 
G 7  104  ARG 104  104  104  ARG ARG G . n 
G 7  105  GLY 105  105  105  GLY GLY G . n 
H 8  1    MET 1    1    1    MET MET H . n 
H 8  2    LEU 2    2    2    LEU LEU H . n 
H 8  3    ILE 3    3    3    ILE ILE H . n 
H 8  4    PRO 4    4    4    PRO PRO H . n 
H 8  5    VAL 5    5    5    VAL VAL H . n 
H 8  6    VAL 6    6    6    VAL VAL H . n 
H 8  7    CYS 7    7    7    CYS CYS H . n 
H 8  8    PHE 8    8    8    PHE PHE H . n 
H 8  9    THR 9    9    9    THR THR H . n 
H 8  10   CYS 10   10   10   CYS CYS H . n 
H 8  11   GLY 11   11   11   GLY GLY H . n 
H 8  12   PHE 12   12   12   PHE PHE H . n 
H 8  13   PRO 13   13   13   PRO PRO H . n 
H 8  14   ILE 14   14   14   ILE ILE H . n 
H 8  15   GLY 15   15   15   GLY GLY H . n 
H 8  16   THR 16   16   16   THR THR H . n 
H 8  17   TYR 17   17   17   TYR TYR H . n 
H 8  18   ALA 18   18   18   ALA ALA H . n 
H 8  19   ALA 19   19   19   ALA ALA H . n 
H 8  20   ILE 20   20   20   ILE ILE H . n 
H 8  21   PHE 21   21   21   PHE PHE H . n 
H 8  22   ASP 22   22   22   ASP ASP H . n 
H 8  23   LYS 23   23   23   LYS LYS H . n 
H 8  24   ALA 24   24   24   ALA ALA H . n 
H 8  25   ARG 25   25   25   ARG ARG H . n 
H 8  26   THR 26   26   26   THR THR H . n 
H 8  27   GLU 27   27   27   GLU GLU H . n 
H 8  28   TYR 28   28   28   TYR TYR H . n 
H 8  29   ILE 29   29   29   ILE ILE H . n 
H 8  30   LYS 30   30   30   LYS LYS H . n 
H 8  31   THR 31   31   31   THR THR H . n 
H 8  32   LYS 32   32   32   LYS LYS H . n 
H 8  33   MET 33   33   33   MET MET H . n 
H 8  34   GLY 34   34   34   GLY GLY H . n 
H 8  35   GLY 35   35   35   GLY GLY H . n 
H 8  36   THR 36   36   36   THR THR H . n 
H 8  37   LEU 37   37   37   LEU LEU H . n 
H 8  38   PRO 38   38   38   PRO PRO H . n 
H 8  39   GLN 39   39   39   GLN GLN H . n 
H 8  40   ASN 40   40   40   ASN ASN H . n 
H 8  41   ILE 41   41   41   ILE ILE H . n 
H 8  42   PRO 42   42   42   PRO PRO H . n 
H 8  43   LEU 43   43   43   LEU LEU H . n 
H 8  44   ASP 44   44   44   ASP ASP H . n 
H 8  45   ALA 45   45   45   ALA ALA H . n 
H 8  46   SER 46   46   46   SER SER H . n 
H 8  47   LEU 47   47   47   LEU LEU H . n 
H 8  48   GLN 48   48   48   GLN GLN H . n 
H 8  49   ILE 49   49   49   ILE ILE H . n 
H 8  50   GLU 50   50   50   GLU GLU H . n 
H 8  51   LEU 51   51   51   LEU LEU H . n 
H 8  52   LYS 52   52   52   LYS LYS H . n 
H 8  53   ASP 53   53   53   ASP ASP H . n 
H 8  54   LEU 54   54   54   LEU LEU H . n 
H 8  55   ILE 55   55   55   ILE ILE H . n 
H 8  56   THR 56   56   56   THR THR H . n 
H 8  57   ALA 57   57   57   ALA ALA H . n 
H 8  58   LEU 58   58   58   LEU LEU H . n 
H 8  59   GLY 59   59   59   GLY GLY H . n 
H 8  60   ILE 60   60   60   ILE ILE H . n 
H 8  61   PRO 61   61   61   PRO PRO H . n 
H 8  62   MET 62   62   62   MET MET H . n 
H 8  63   ARG 63   63   63   ARG ARG H . n 
H 8  64   VAL 64   64   64   VAL VAL H . n 
H 8  65   CYS 65   65   65   CYS CYS H . n 
H 8  66   CYS 66   66   66   CYS CYS H . n 
H 8  67   ARG 67   67   67   ARG ARG H . n 
H 8  68   THR 68   68   68   THR THR H . n 
H 8  69   HIS 69   69   69   HIS HIS H . n 
H 8  70   LEU 70   70   70   LEU LEU H . n 
H 8  71   ILE 71   71   71   ILE ILE H . n 
H 8  72   THR 72   72   72   THR THR H . n 
H 8  73   THR 73   73   73   THR THR H . n 
H 8  74   LEU 74   74   74   LEU LEU H . n 
H 8  75   ASP 75   75   75   ASP ASP H . n 
H 8  76   TYR 76   76   76   TYR TYR H . n 
H 8  77   ARG 77   77   77   ARG ARG H . n 
H 8  78   LYS 78   78   78   LYS LYS H . n 
H 8  79   TYR 79   79   79   TYR TYR H . n 
H 8  80   TYR 80   80   80   TYR TYR H . n 
I 9  1    DG  1    20   20   DG  DG  X . n 
I 9  2    DC  2    21   21   DC  DC  X . n 
I 9  3    DC  3    22   22   DC  DC  X . n 
I 9  4    DG  4    23   23   DG  DG  X . n 
I 9  5    DA  5    24   24   DA  DA  X . n 
I 9  6    DG  6    25   25   DG  DG  X . n 
I 9  7    DC  7    26   26   DC  DC  X . n 
I 9  8    DA  8    27   27   DA  DA  X . n 
J 10 1    DT  1    -24  -24  DT  DT  Y . n 
J 10 2    DC  2    -23  -23  DC  DC  Y . n 
J 10 3    DG  3    -22  -22  DG  DG  Y . n 
J 10 4    DG  4    -21  -21  DG  DG  Y . n 
J 10 5    DC  5    -20  -20  DC  DC  Y . n 
J 10 6    DT  6    -19  -19  DT  DT  Y . n 
J 10 7    DC  7    -18  -18  DC  DC  Y . n 
# 
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 
K 11 MG 1 1501 1501 MG MG A . 
L 12 ZN 1 1502 1502 ZN ZN A . 
M 12 ZN 1 1301 1301 ZN ZN B . 
N 12 ZN 1 201  201  ZN ZN G . 
O 12 ZN 1 101  101  ZN ZN H . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A TRP 1154 ? CG  ? A TRP 1154 CG  
2 1 Y 1 A TRP 1154 ? CD1 ? A TRP 1154 CD1 
3 1 Y 1 A TRP 1154 ? CD2 ? A TRP 1154 CD2 
4 1 Y 1 A TRP 1154 ? NE1 ? A TRP 1154 NE1 
5 1 Y 1 A TRP 1154 ? CE2 ? A TRP 1154 CE2 
6 1 Y 1 A TRP 1154 ? CE3 ? A TRP 1154 CE3 
7 1 Y 1 A TRP 1154 ? CZ2 ? A TRP 1154 CZ2 
8 1 Y 1 A TRP 1154 ? CZ3 ? A TRP 1154 CZ3 
9 1 Y 1 A TRP 1154 ? CH2 ? A TRP 1154 CH2 
# 
_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                     8YQZ 
_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                         8YQZ 
_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                   8YQZ 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     8YQZ 
_struct.title                        'African swine fever virus RNA Polymerase--DNA complex' 
_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        8YQZ 
_struct_keywords.text            'ASFV, RNA polymerase, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL 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 5  ? 
F N N 6  ? 
G N N 7  ? 
H N N 8  ? 
I N N 9  ? 
J N N 10 ? 
K N N 11 ? 
L N N 12 ? 
M N N 12 ? 
N N N 12 ? 
O N N 12 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1  UNP A0A3S7XUW7_ASF A0A3S7XUW7 ? 1  
;MEAGYAEIAAVQFNIAGDNDHKRQGVMEVTISNLFEGTLPAEGGIYDARMGTTDHHYKCITCSHQRKQCMGHPGILQMHA
PVLQPLFIAEIRRWLRVICLNCGAPIVDLKRYEHLIRPKRLIEAASSQTEGKQCYVCKAVHPKIVKDSEDYFTFWADQQG
KIDKLYPQIIREIFSRVTYDTVVKLGRSKNSHPEKLVLKAIQIPPISIRPGIRLGIGSGPQSFHDINNVIQYLVRKNLLI
PKDLQIVRGQKIPLNIDRNLQTIQQLYYNFLLDSVSTTATQGGTGKRGIVMGARPAPSIMRRLPRKEGRIRKSLLGSQVW
SISRSTICGNSDLHLDEVGYPISFARTLQVAETVQHYNINRLMPYFLNGKRQYPGCSRVYKQITQSVHDIEGLKQDFRLE
VGDILYRDVVTGDVAFFNRQPSLERSSIGVHRIVVLENPKISTFQMNVSACAWYNADFDGDQMNLWVPWSVMSRVEAELL
CSVRNWFISTKSSGPVNGQVQDSTVGSFLLTRTNTPMGKNVMNKLHAMGLFQTTQTDPPCFANYSPTDLLDGKSVVSMLL
RQTPINYQRAPTWYSEVYAPYMHYNKQDISTQIRNGELIEGVLDKKAVGAGSSGGIYHLISRRYGPQQALKMIFATQQLA
LNYVRNAGFTVSTADMLLTPEAHQEVQEIINELLLESEEINNRLLHGDIMPPIGLTTHDFYEKLQLNALKFPDRILKPIM
NSINPETNGLFQMVATGAKGSNPNMIHIMAGIGQIEINTQRIQPQFSFGRTLVYYPRFALEAQAYGFICNSYIAGLTSPE
FIFGEMNGRFDLINKALSTSSTGYANRKAIFGLQSCIVDYYRRVSIDTRLVQQLYGEDGLDARQLETVRFETIMLSDQEL
EDKFKYTGIQSPLFEEEFSRLKKDRDKYRQIFLNVENFNFSQLLTDVRQVPVNVASIVKNILLSSTSGVLPFDEKSILQK
YAMVKTFCKNLPYVFINNIQERLQTPIPVYLKRAASLMRMLIRIELATVKTLNITCEQMSAILDLIRLQYTQSLINYGEA
VGILAAQSVSEPLTQYMLDSHHRSVAGGTNKSGIVRPQEIFSAKPVEAEQSSEMLLRLKNPEVETNKTYAQEIANSIELI
TFERLILQWHLLYETYSSTKKNVMYPDFASDVEWMTDFLENHPLLQPPEDIANWCIRLELNKTTMILKSISLESIINSLR
AKHPNTYIMHSVENTASGIPIIIRIYLRESAFRRSTNTRMATDEKIAVNVVDKLLNSTIRGIPGIKNANVVKLMRHRVDA
QGKLVRLDNIYAIKTNGTNIFGAMLDDNIDPYTIVSSSIGDTMELYGIEAARQKIISEIRTVMGDKGPNHRHLLMYADLM
TRTGQVTSLEKAGLNAREPSNVLLRMALSSPVQVLTDAAVDSAVNPIYGIAAPTLMGSVPRIGTMYSDIIMDEKYITENY
KSVDSLIDML
;
1 
2  UNP A0A2X0RU95_ASF A0A2X0RU95 ? 2  
;MEPLRPQITYGPIETVDNEELTEADMLSFISAAVNSTGLIGYNIKSFDDLMDNGIPQIVKQMFNVDITYKDQRDHTEIDK
LRESVQIQFNFTDVNIERPQHRNYSQGNKINLLPNKARLCGLSYSGPVNLAAEVILTAHYSNGRQEVKRASIPPFQVSTF
PIMRGSNRCHTHHLSKTAKKEIGEDPNEPGGYFIARGGEWVVDLLENIRFNTLHIHYHTMQQGNNEIIRGEFISQPGGAF
ENSSQIIIRYMTTGAITIEINSTKFSKLRIPWYLIFRMFGMTGDDSIIEQVVFDLESNSLVNTFMIEILEKSIHVLDPIF
QPVQHELNREKIIQFLSEKVSKFVSNPSAYKSDENAVQYLNERQLTILDKILLPHMGQTADTRVRKLRFLGLLIHKILLV
IMNVFPPTDRDSYRTKRVHGSGVSLAKAFKAIFNTSVIAPIINGFKELLKQTAFEELTQRNIIEAFSAALSKNTASDLNR
SMEQSIISGNKTIMVRQRPIVNRVSTQSLERKNLLNTISALRTVNTHNTTNASKQTERADMMRRVHASYPGYICVAQSAD
TGEKVGMSKQLAITANVCTAGEVLSLKQRLLSDPAIQQLADVSNKDIVRKGLARVFINGEWIGCCTNAFELAQRYRMLRR
EGKVVHPHTTIYWDSMVDEVEFWLDVGRLTRPLLIVDNNIEKYNQACYKAAEARKKGDKDWEKHKIPFIQNTRFTPQMAK
DILAGTLTLEDLVAQGICEFITPEEAENCLVAFSIIELRKHKHDVTRRFTHVDVPQAILGLAALVSPYANCTQPARVTYE
TNQGRQTGGWYCFSWPYRVDMNRFFQFYNEMPLVKTIAHNYVIPNGLNTIVAYMIYGGYNQEDSVIVSQSFIDRGGFAGT
FYREEKVELESDIESFGKPDPLITKNLKPGANYEKLVDGFVPVGTVVKKGDIIIGKVAKIRGEKDELNKYIDRSVMYGFD
EPAVVDAVMRPHGPNDEIFGLMRLRYERNLNIGDKMSSRSGNKGIAALALPTSDMPFTEDGLQPDLIVNPHSHPSRMTNG
QMIETTVGLANALQGVVTDGTAFLPINVQLLSERLAQEGLRFNGCQKMFNGQTGEYFDAAIFIGPTYHQRLQKFVLDDRY
AVASYGPTDALTGQPLDGKRSHGGLRLGEMEHWVLTAQGAMQTIIEKSHDDSDGCISYICRNCGEPAIYNASHPIYKCMN
CDVQADIGMVDSRRSSIVFQHEMRAANVNITSVLSPRVFQPA
;
1 
3  UNP A0A2X0RUE7_ASF A0A2X0RUE7 ? 3  
;MEKIFQNVEIKPFLIDFSNLFIKNAAKKLFQLEEQLPLVPVNVVMDFKGISRAAVHGLSRVLQDEIPNYMLDIKPGGYKI
EDSTDLFMTEQFIRNRINFIPIYAKNETLVFALRSLNNSCEVKTIYSRDLIQVAGPKLKYPIFNPTFEIGFLQPGKSLII
EDIYIKKGIGRKHAAFNLAVKTHFSHLDIEQYPTDKKEYMALSGYKQSSMTSDPRHHRLGLCFPAVPLPHINQAVRTYLK
NACRIIIGRIQSIQKIYENFEEPQPELVLFSMDEEKTKAIITIKDETHTIGNLLKTYIYEMIPDISFVGYQCVPHKQEMV
LTIIHKASQEDLITLLEKSIQNIIQTFQILEKNVDELIA
;
1 
4  UNP A0A0A1E0C1_ASF A0A0A1E0C1 ? 4  
;MAMQKLFTYIYEFIEYRKMVLLEEKVPYDKFVQMVLNTGFFRINAETLNHGIVSVFIFGANGKYVHHGGDMRTLLTNTLN
EKKHYEELILIVDKPVLSKKNILDIIVEQRAANPTIVINIYPYHLFCINIPKVSAIPKHKLITQEEAQEFLGREYLQPQD
LMQISASDPPVVWLGGRPGDFVQIERPSETAMHAVVIRFITKSKI
;
1 
5  UNP A0A2X0RTW5_ASF A0A2X0RTW5 ? 5  
;MADNDNEDLIMDDLVEEYVETEEENLVDSEEESEDKDEIVESPSICEGFVQASSQTLVIIPDNERITSNVLTTFEATRLV
AVRAQQLAINGSTMLKKKYSSPIDIAKQELFNRKIPLLVMRCIKVTPEGQKIVEIWNPREMGIPLLD
;
1 
6  UNP A0A2X0RV08_ASF A0A2X0RV08 ? 6  
;MIDQKIFETTLNIDDPTNFCTNVEAHLLKELENIYVGKCFKNSFILNITGVIQRSPCFIMRTNNSGRGYMHVRFSAVVSY
LNAFDLIAAVKIIKNDSNIILGESLLTEPVTIVIPSSESQNNVAEVGQIVPVQLANSSVYYIPGRQQASATGSIFIPKHT
FSVYHVQEELTQEQALNLTKLVNIIEMLLESRSKKDFKQICFFEKLYYTYSISSDEILDLKIWKGPKGKEMSRLKPCNVL
SFLYDALKNKNSSLGFWARPPNLLKSSPLAYQQDQNSFNATELPIICSAEVMFVTLLKEIINYLQFINDLCDTFNNEQLI
KRHENIWMLIEQRKIGHDF
;
1 
7  UNP A0A0A1DYD1_ASF A0A0A1DYD1 ? 7  
;MKICKACSSCMVRTYVDGNIIFRCSCGESVQGDSQNLLVSSKVYHTGEMEDKYKIFIKNAPFDPTNCQIKKDCPNCHLDY
LTQICIGSQKIIILVCRCGYMSNRG
;
1 
8  UNP A0A0C5BCR6_ASF A0A0C5BCR6 ? 8  
;MLIPVVCFTCGFPIGTYAAIFDKARTEYIKTKMGGTLPQNIPLDASLQIELKDLITALGIPMRVCCRTHLITTLDYRKYY

;
1 
9  PDB 8YQZ           8YQZ       ? 9  ? 1 
10 PDB 8YQZ           8YQZ       ? 10 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1  1  8YQZ A 1 ? 1450 ? A0A3S7XUW7 1   ? 1450 ? 1   1450 
2  2  8YQZ B 1 ? 1242 ? A0A2X0RU95 1   ? 1242 ? 1   1242 
3  3  8YQZ C 1 ? 359  ? A0A2X0RUE7 1   ? 359  ? 1   359  
4  4  8YQZ D 1 ? 205  ? A0A0A1E0C1 1   ? 205  ? 1   205  
5  5  8YQZ E 1 ? 147  ? A0A2X0RTW5 1   ? 147  ? 1   147  
6  6  8YQZ F 1 ? 339  ? A0A2X0RV08 1   ? 339  ? 1   339  
7  7  8YQZ G 1 ? 105  ? A0A0A1DYD1 1   ? 105  ? 1   105  
8  8  8YQZ H 1 ? 80   ? A0A0C5BCR6 1   ? 80   ? 1   80   
9  9  8YQZ X 1 ? 8    ? 8YQZ       20  ? 27   ? 20  27   
10 10 8YQZ Y 1 ? 7    ? 8YQZ       -24 ? -18  ? -24 -18  
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   decameric 
_pdbx_struct_assembly.oligomeric_count     10 
# 
_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,J,K,L,M,N,O 
# 
_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 GLY A 17   ? GLY A 25   ? GLY A 17   GLY A 25   1 ? 9  
HELX_P HELX_P2   AA2 ASP A 47   ? GLY A 51   ? ASP A 47   GLY A 51   5 ? 5  
HELX_P HELX_P3   AA3 PHE A 87   ? ARG A 96   ? PHE A 87   ARG A 96   1 ? 10 
HELX_P HELX_P4   AA4 ASP A 108  ? TYR A 112  ? ASP A 108  TYR A 112  5 ? 5  
HELX_P HELX_P5   AA5 ILE A 116  ? SER A 127  ? ILE A 116  SER A 127  1 ? 12 
HELX_P HELX_P6   AA6 TYR A 166  ? SER A 175  ? TYR A 166  SER A 175  1 ? 10 
HELX_P HELX_P7   AA7 THR A 178  ? LEU A 185  ? THR A 178  LEU A 185  1 ? 8  
HELX_P HELX_P8   AA8 SER A 188  ? LYS A 195  ? SER A 188  LYS A 195  5 ? 8  
HELX_P HELX_P9   AA9 PRO A 205  ? ARG A 209  ? PRO A 205  ARG A 209  5 ? 5  
HELX_P HELX_P10  AB1 ASP A 225  ? LEU A 239  ? ASP A 225  LEU A 239  1 ? 15 
HELX_P HELX_P11  AB2 PRO A 253  ? ASP A 273  ? PRO A 253  ASP A 273  1 ? 21 
HELX_P HELX_P12  AB3 ILE A 299  ? LEU A 303  ? ILE A 299  LEU A 303  5 ? 5  
HELX_P HELX_P13  AB4 GLY A 308  ? SER A 313  ? GLY A 308  SER A 313  1 ? 6  
HELX_P HELX_P14  AB5 ILE A 342  ? ARG A 346  ? ILE A 342  ARG A 346  1 ? 5  
HELX_P HELX_P15  AB6 ASN A 358  ? GLY A 369  ? ASN A 358  GLY A 369  1 ? 12 
HELX_P HELX_P16  AB7 ASN A 447  ? SER A 449  ? ASN A 447  SER A 449  5 ? 3  
HELX_P HELX_P17  AB8 ALA A 450  ? ASN A 455  ? ALA A 450  ASN A 455  1 ? 6  
HELX_P HELX_P18  AB9 SER A 470  ? CYS A 481  ? SER A 470  CYS A 481  1 ? 12 
HELX_P HELX_P19  AC1 SER A 482  ? PHE A 487  ? SER A 482  PHE A 487  5 ? 6  
HELX_P HELX_P20  AC2 ASP A 502  ? ARG A 512  ? ASP A 502  ARG A 512  1 ? 11 
HELX_P HELX_P21  AC3 LYS A 524  ? LEU A 530  ? LYS A 524  LEU A 530  1 ? 7  
HELX_P HELX_P22  AC4 GLY A 552  ? ARG A 561  ? GLY A 552  ARG A 561  1 ? 10 
HELX_P HELX_P23  AC5 TYR A 578  ? MET A 582  ? TYR A 578  MET A 582  5 ? 5  
HELX_P HELX_P24  AC6 ASN A 585  ? ILE A 589  ? ASN A 585  ILE A 589  5 ? 5  
HELX_P HELX_P25  AC7 ASP A 604  ? GLY A 609  ? ASP A 604  GLY A 609  1 ? 6  
HELX_P HELX_P26  AC8 GLY A 615  ? GLY A 625  ? GLY A 615  GLY A 625  1 ? 11 
HELX_P HELX_P27  AC9 GLY A 625  ? GLY A 648  ? GLY A 625  GLY A 648  1 ? 24 
HELX_P HELX_P28  AD1 SER A 652  ? LEU A 657  ? SER A 652  LEU A 657  5 ? 6  
HELX_P HELX_P29  AD2 THR A 659  ? HIS A 686  ? THR A 659  HIS A 686  1 ? 28 
HELX_P HELX_P30  AD3 THR A 696  ? LEU A 709  ? THR A 696  LEU A 709  1 ? 14 
HELX_P HELX_P31  AD4 PRO A 712  ? ARG A 714  ? PRO A 712  ARG A 714  5 ? 3  
HELX_P HELX_P32  AD5 ILE A 715  ? ASN A 721  ? ILE A 715  ASN A 721  1 ? 7  
HELX_P HELX_P33  AD6 ASN A 728  ? THR A 736  ? ASN A 728  THR A 736  1 ? 9  
HELX_P HELX_P34  AD7 SER A 741  ? ALA A 750  ? SER A 741  ALA A 750  1 ? 10 
HELX_P HELX_P35  AD8 GLU A 781  ? TYR A 785  ? GLU A 781  TYR A 785  5 ? 5  
HELX_P HELX_P36  AD9 THR A 797  ? GLN A 834  ? THR A 797  GLN A 834  1 ? 38 
HELX_P HELX_P37  AE1 LEU A 854  ? ASP A 858  ? LEU A 854  ASP A 858  5 ? 5  
HELX_P HELX_P38  AE2 ASP A 861  ? LEU A 865  ? ASP A 861  LEU A 865  5 ? 5  
HELX_P HELX_P39  AE3 SER A 876  ? LYS A 885  ? SER A 876  LYS A 885  1 ? 10 
HELX_P HELX_P40  AE4 PRO A 892  ? PHE A 918  ? PRO A 892  PHE A 918  1 ? 27 
HELX_P HELX_P41  AE5 ASN A 933  ? SER A 944  ? ASN A 933  SER A 944  1 ? 12 
HELX_P HELX_P42  AE6 ASP A 953  ? ASN A 970  ? ASP A 953  ASN A 970  1 ? 18 
HELX_P HELX_P43  AE7 LEU A 971  ? ILE A 976  ? LEU A 971  ILE A 976  5 ? 6  
HELX_P HELX_P44  AE8 ASN A 977  ? GLN A 984  ? ASN A 977  GLN A 984  1 ? 8  
HELX_P HELX_P45  AE9 PRO A 988  ? ARG A 993  ? PRO A 988  ARG A 993  1 ? 6  
HELX_P HELX_P46  AF1 ALA A 995  ? LEU A 1006 ? ALA A 995  LEU A 1006 1 ? 12 
HELX_P HELX_P47  AF2 THR A 1015 ? GLN A 1032 ? THR A 1015 GLN A 1032 1 ? 18 
HELX_P HELX_P48  AF3 ALA A 1040 ? GLU A 1051 ? ALA A 1040 GLU A 1051 1 ? 12 
HELX_P HELX_P49  AF4 ILE A 1074 ? ALA A 1083 ? ILE A 1074 ALA A 1083 1 ? 10 
HELX_P HELX_P50  AF5 PRO A 1085 ? GLU A 1089 ? PRO A 1085 GLU A 1089 5 ? 5  
HELX_P HELX_P51  AF6 ASN A 1106 ? ILE A 1117 ? ASN A 1106 ILE A 1117 1 ? 12 
HELX_P HELX_P52  AF7 PHE A 1148 ? LEU A 1159 ? PHE A 1148 LEU A 1159 1 ? 12 
HELX_P HELX_P53  AF8 ASN A 1181 ? SER A 1189 ? ASN A 1181 SER A 1189 1 ? 9  
HELX_P HELX_P54  AF9 SER A 1191 ? ARG A 1200 ? SER A 1191 ARG A 1200 1 ? 10 
HELX_P HELX_P55  AG1 GLU A 1229 ? PHE A 1232 ? GLU A 1229 PHE A 1232 5 ? 4  
HELX_P HELX_P56  AG2 THR A 1242 ? ASN A 1256 ? THR A 1242 ASN A 1256 1 ? 15 
HELX_P HELX_P57  AG3 ASN A 1299 ? LEU A 1305 ? ASN A 1299 LEU A 1305 1 ? 7  
HELX_P HELX_P58  AG4 SER A 1318 ? GLY A 1327 ? SER A 1318 GLY A 1327 1 ? 10 
HELX_P HELX_P59  AG5 GLY A 1327 ? GLY A 1344 ? GLY A 1327 GLY A 1344 1 ? 18 
HELX_P HELX_P60  AG6 ASN A 1349 ? THR A 1361 ? ASN A 1349 THR A 1361 1 ? 13 
HELX_P HELX_P61  AG7 GLU A 1370 ? GLU A 1378 ? GLU A 1370 GLU A 1378 1 ? 9  
HELX_P HELX_P62  AG8 ASN A 1381 ? SER A 1389 ? ASN A 1381 SER A 1389 1 ? 9  
HELX_P HELX_P63  AG9 SER A 1390 ? SER A 1402 ? SER A 1390 SER A 1402 1 ? 13 
HELX_P HELX_P64  AH1 ILE A 1410 ? MET A 1416 ? ILE A 1410 MET A 1416 1 ? 7  
HELX_P HELX_P65  AH2 ILE A 1422 ? TYR A 1426 ? ILE A 1422 TYR A 1426 5 ? 5  
HELX_P HELX_P66  AH3 ASP A 1432 ? TYR A 1440 ? ASP A 1432 TYR A 1440 1 ? 9  
HELX_P HELX_P67  AH4 PRO B 12   ? VAL B 16   ? PRO B 12   VAL B 16   5 ? 5  
HELX_P HELX_P68  AH5 MET B 26   ? GLY B 38   ? MET B 26   GLY B 38   1 ? 13 
HELX_P HELX_P69  AH6 GLY B 41   ? ASN B 53   ? GLY B 41   ASN B 53   1 ? 13 
HELX_P HELX_P70  AH7 ASN B 53   ? GLN B 61   ? ASN B 53   GLN B 61   1 ? 9  
HELX_P HELX_P71  AH8 THR B 76   ? LEU B 81   ? THR B 76   LEU B 81   1 ? 6  
HELX_P HELX_P72  AH9 LEU B 113  ? GLY B 121  ? LEU B 113  GLY B 121  1 ? 9  
HELX_P HELX_P73  AI1 SER B 175  ? ILE B 182  ? SER B 175  ILE B 182  1 ? 8  
HELX_P HELX_P74  AI2 TRP B 272  ? PHE B 279  ? TRP B 272  PHE B 279  1 ? 8  
HELX_P HELX_P75  AI3 GLY B 283  ? VAL B 292  ? GLY B 283  VAL B 292  1 ? 10 
HELX_P HELX_P76  AI4 SER B 299  ? ILE B 313  ? SER B 299  ILE B 313  1 ? 15 
HELX_P HELX_P77  AI5 ARG B 329  ? SER B 341  ? ARG B 329  SER B 341  1 ? 13 
HELX_P HELX_P78  AI6 ALA B 349  ? ASP B 353  ? ALA B 349  ASP B 353  5 ? 5  
HELX_P HELX_P79  AI7 GLU B 354  ? LEU B 372  ? GLU B 354  LEU B 372  1 ? 19 
HELX_P HELX_P80  AI8 LEU B 373  ? GLY B 377  ? LEU B 373  GLY B 377  5 ? 5  
HELX_P HELX_P81  AI9 THR B 379  ? ASP B 381  ? THR B 379  ASP B 381  5 ? 3  
HELX_P HELX_P82  AJ1 THR B 382  ? MET B 402  ? THR B 382  MET B 402  1 ? 21 
HELX_P HELX_P83  AJ2 SER B 412  ? ARG B 414  ? SER B 412  ARG B 414  5 ? 3  
HELX_P HELX_P84  AJ3 GLY B 420  ? VAL B 437  ? GLY B 420  VAL B 437  1 ? 18 
HELX_P HELX_P85  AJ4 VAL B 437  ? LYS B 450  ? VAL B 437  LYS B 450  1 ? 14 
HELX_P HELX_P86  AJ5 THR B 458  ? ALA B 469  ? THR B 458  ALA B 469  1 ? 12 
HELX_P HELX_P87  AJ6 SER B 471  ? GLY B 489  ? SER B 471  GLY B 489  1 ? 19 
HELX_P HELX_P88  AJ7 ASN B 513  ? LEU B 521  ? ASN B 513  LEU B 521  1 ? 9  
HELX_P HELX_P89  AJ8 ARG B 538  ? MET B 542  ? ARG B 538  MET B 542  1 ? 5  
HELX_P HELX_P90  AJ9 GLU B 582  ? LEU B 591  ? GLU B 582  LEU B 591  1 ? 10 
HELX_P HELX_P91  AK1 GLN B 598  ? VAL B 602  ? GLN B 598  VAL B 602  5 ? 5  
HELX_P HELX_P92  AK2 SER B 603  ? LYS B 610  ? SER B 603  LYS B 610  1 ? 8  
HELX_P HELX_P93  AK3 ASN B 627  ? GLY B 642  ? ASN B 627  GLY B 642  1 ? 16 
HELX_P HELX_P94  AK4 ASN B 679  ? GLY B 697  ? ASN B 679  GLY B 697  1 ? 19 
HELX_P HELX_P95  AK5 ASP B 700  ? LYS B 705  ? ASP B 700  LYS B 705  5 ? 6  
HELX_P HELX_P96  AK6 THR B 715  ? ALA B 724  ? THR B 715  ALA B 724  1 ? 10 
HELX_P HELX_P97  AK7 THR B 728  ? GLN B 735  ? THR B 728  GLN B 735  1 ? 8  
HELX_P HELX_P98  AK8 GLU B 744  ? CYS B 749  ? GLU B 744  CYS B 749  5 ? 6  
HELX_P HELX_P99  AK9 SER B 754  ? HIS B 761  ? SER B 754  HIS B 761  1 ? 8  
HELX_P HELX_P100 AL1 VAL B 774  ? LEU B 779  ? VAL B 774  LEU B 779  5 ? 6  
HELX_P HELX_P101 AL2 TYR B 788  ? THR B 792  ? TYR B 788  THR B 792  5 ? 5  
HELX_P HELX_P102 AL3 GLN B 793  ? ARG B 805  ? GLN B 793  ARG B 805  1 ? 13 
HELX_P HELX_P103 AL4 SER B 814  ? ARG B 818  ? SER B 814  ARG B 818  5 ? 5  
HELX_P HELX_P104 AL5 THR B 836  ? TYR B 841  ? THR B 836  TYR B 841  5 ? 6  
HELX_P HELX_P105 AL6 GLN B 869  ? ARG B 874  ? GLN B 869  ARG B 874  1 ? 6  
HELX_P HELX_P106 AL7 PRO B 1011 ? MET B 1015 ? PRO B 1011 MET B 1015 5 ? 5  
HELX_P HELX_P107 AL8 PRO B 1030 ? HIS B 1033 ? PRO B 1030 HIS B 1033 5 ? 4  
HELX_P HELX_P108 AL9 THR B 1038 ? GLY B 1055 ? THR B 1038 GLY B 1055 1 ? 18 
HELX_P HELX_P109 AM1 ASN B 1067 ? GLU B 1078 ? ASN B 1067 GLU B 1078 1 ? 12 
HELX_P HELX_P110 AM2 PHE B 1114 ? ARG B 1119 ? PHE B 1114 ARG B 1119 1 ? 6  
HELX_P HELX_P111 AM3 GLY B 1148 ? GLY B 1159 ? GLY B 1148 GLY B 1159 1 ? 12 
HELX_P HELX_P112 AM4 ALA B 1160 ? HIS B 1169 ? ALA B 1160 HIS B 1169 1 ? 10 
HELX_P HELX_P113 AM5 ARG B 1214 ? ALA B 1226 ? ARG B 1214 ALA B 1226 1 ? 13 
HELX_P HELX_P114 AM6 ASN C 19   ? GLN C 31   ? ASN C 19   GLN C 31   1 ? 13 
HELX_P HELX_P115 AM7 SER C 51   ? GLU C 65   ? SER C 51   GLU C 65   1 ? 15 
HELX_P HELX_P116 AM8 THR C 89   ? PHE C 99   ? THR C 89   PHE C 99   1 ? 11 
HELX_P HELX_P117 AM9 HIS C 173  ? ASN C 177  ? HIS C 173  ASN C 177  5 ? 5  
HELX_P HELX_P118 AN1 HIS C 230  ? GLU C 258  ? HIS C 230  GLU C 258  1 ? 29 
HELX_P HELX_P119 AN2 THR C 287  ? ILE C 302  ? THR C 287  ILE C 302  1 ? 16 
HELX_P HELX_P120 AN3 SER C 328  ? ILE C 358  ? SER C 328  ILE C 358  1 ? 31 
HELX_P HELX_P121 AN4 ALA D 2    ? ARG D 17   ? ALA D 2    ARG D 17   1 ? 16 
HELX_P HELX_P122 AN5 PRO D 27   ? GLY D 39   ? PRO D 27   GLY D 39   1 ? 13 
HELX_P HELX_P123 AN6 GLY D 62   ? HIS D 67   ? GLY D 62   HIS D 67   1 ? 6  
HELX_P HELX_P124 AN7 HIS D 67   ? ASN D 80   ? HIS D 67   ASN D 80   1 ? 14 
HELX_P HELX_P125 AN8 ASP D 93   ? SER D 98   ? ASP D 93   SER D 98   5 ? 6  
HELX_P HELX_P126 AN9 LYS D 99   ? ASN D 113  ? LYS D 99   ASN D 113  1 ? 15 
HELX_P HELX_P127 AO1 TYR D 123  ? CYS D 127  ? TYR D 123  CYS D 127  5 ? 5  
HELX_P HELX_P128 AO2 ASN D 129  ? VAL D 133  ? ASN D 129  VAL D 133  5 ? 5  
HELX_P HELX_P129 AO3 THR D 143  ? TYR D 155  ? THR D 143  TYR D 155  1 ? 13 
HELX_P HELX_P130 AO4 GLN D 157  ? LEU D 161  ? GLN D 157  LEU D 161  5 ? 5  
HELX_P HELX_P131 AO5 ASP D 168  ? GLY D 175  ? ASP D 168  GLY D 175  1 ? 8  
HELX_P HELX_P132 AO6 SER E 44   ? PHE E 49   ? SER E 44   PHE E 49   1 ? 6  
HELX_P HELX_P133 AO7 PRO E 61   ? ARG E 65   ? PRO E 61   ARG E 65   5 ? 5  
HELX_P HELX_P134 AO8 THR E 72   ? ASN E 90   ? THR E 72   ASN E 90   1 ? 19 
HELX_P HELX_P135 AO9 SER E 101  ? ASN E 112  ? SER E 101  ASN E 112  1 ? 12 
HELX_P HELX_P136 AP1 ASN E 137  ? MET E 141  ? ASN E 137  MET E 141  5 ? 5  
HELX_P HELX_P137 AP2 ASP F 15   ? CYS F 20   ? ASP F 15   CYS F 20   1 ? 6  
HELX_P HELX_P138 AP3 ASN F 22   ? VAL F 36   ? ASN F 22   VAL F 36   1 ? 15 
HELX_P HELX_P139 AP4 THR F 171  ? LYS F 195  ? THR F 171  LYS F 195  1 ? 25 
HELX_P HELX_P140 AP5 ASP F 196  ? TYR F 208  ? ASP F 196  TYR F 208  1 ? 13 
HELX_P HELX_P141 AP6 VAL F 239  ? LYS F 248  ? VAL F 239  LYS F 248  1 ? 10 
HELX_P HELX_P142 AP7 SER F 288  ? PHE F 314  ? SER F 288  PHE F 314  1 ? 27 
HELX_P HELX_P143 AP8 ASN F 316  ? HIS F 323  ? ASN F 316  HIS F 323  1 ? 8  
HELX_P HELX_P144 AP9 HIS F 323  ? GLN F 332  ? HIS F 323  GLN F 332  1 ? 10 
HELX_P HELX_P145 AQ1 TYR G 53   ? ALA G 60   ? TYR G 53   ALA G 60   1 ? 8  
HELX_P HELX_P146 AQ2 PRO H 13   ? THR H 16   ? PRO H 13   THR H 16   5 ? 4  
HELX_P HELX_P147 AQ3 TYR H 17   ? GLY H 34   ? TYR H 17   GLY H 34   1 ? 18 
HELX_P HELX_P148 AQ4 PRO H 42   ? GLN H 48   ? PRO H 42   GLN H 48   1 ? 7  
HELX_P HELX_P149 AQ5 LEU H 51   ? GLY H 59   ? LEU H 51   GLY H 59   1 ? 9  
HELX_P HELX_P150 AQ6 ARG H 63   ? THR H 73   ? ARG H 63   THR H 73   1 ? 11 
HELX_P HELX_P151 AQ7 ASP H 75   ? TYR H 79   ? ASP H 75   TYR H 79   5 ? 5  
# 
_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 CYS 59   SG  ? ? ? 1_555 L ZN . ZN ? ? A CYS 59   A ZN 1502 1_555 ? ? ? ? ? ? ?                       2.482 
? ? 
metalc2  metalc ? ? A CYS 62   SG  ? ? ? 1_555 L ZN . ZN ? ? A CYS 62   A ZN 1502 1_555 ? ? ? ? ? ? ?                       2.282 
? ? 
metalc3  metalc ? ? A CYS 69   SG  ? ? ? 1_555 L ZN . ZN ? ? A CYS 69   A ZN 1502 1_555 ? ? ? ? ? ? ?                       2.294 
? ? 
metalc4  metalc ? ? A HIS 72   NE2 ? ? ? 1_555 L ZN . ZN ? ? A HIS 72   A ZN 1502 1_555 ? ? ? ? ? ? ?                       2.296 
? ? 
metalc5  metalc ? ? A ASP 457  OD1 ? ? ? 1_555 K MG . MG ? ? A ASP 457  A MG 1501 1_555 ? ? ? ? ? ? ?                       2.437 
? ? 
metalc6  metalc ? ? A ASP 459  OD1 ? ? ? 1_555 K MG . MG ? ? A ASP 459  A MG 1501 1_555 ? ? ? ? ? ? ?                       2.022 
? ? 
metalc7  metalc ? ? A ASP 461  OD1 ? ? ? 1_555 K MG . MG ? ? A ASP 461  A MG 1501 1_555 ? ? ? ? ? ? ?                       2.318 
? ? 
metalc8  metalc ? ? B CYS 1180 SG  ? ? ? 1_555 M ZN . ZN ? ? B CYS 1180 B ZN 1301 1_555 ? ? ? ? ? ? ?                       2.290 
? ? 
metalc9  metalc ? ? B CYS 1183 SG  ? ? ? 1_555 M ZN . ZN ? ? B CYS 1183 B ZN 1301 1_555 ? ? ? ? ? ? ?                       2.228 
? ? 
metalc10 metalc ? ? B CYS 1198 SG  ? ? ? 1_555 M ZN . ZN ? ? B CYS 1198 B ZN 1301 1_555 ? ? ? ? ? ? ?                       2.722 
? ? 
metalc11 metalc ? ? B CYS 1201 SG  ? ? ? 1_555 M ZN . ZN ? ? B CYS 1201 B ZN 1301 1_555 ? ? ? ? ? ? ?                       2.344 
? ? 
metalc12 metalc ? ? G CYS 73   SG  ? ? ? 1_555 N ZN . ZN ? ? G CYS 73   G ZN 201  1_555 ? ? ? ? ? ? ?                       2.594 
? ? 
metalc13 metalc ? ? G CYS 76   SG  ? ? ? 1_555 N ZN . ZN ? ? G CYS 76   G ZN 201  1_555 ? ? ? ? ? ? ?                       2.313 
? ? 
metalc14 metalc ? ? G CYS 96   SG  ? ? ? 1_555 N ZN . ZN ? ? G CYS 96   G ZN 201  1_555 ? ? ? ? ? ? ?                       2.305 
? ? 
metalc15 metalc ? ? G CYS 98   SG  ? ? ? 1_555 N ZN . ZN ? ? G CYS 98   G ZN 201  1_555 ? ? ? ? ? ? ?                       2.294 
? ? 
metalc16 metalc ? ? H CYS 7    SG  ? ? ? 1_555 O ZN . ZN ? ? H CYS 7    H ZN 101  1_555 ? ? ? ? ? ? ?                       2.324 
? ? 
metalc17 metalc ? ? H CYS 10   SG  ? ? ? 1_555 O ZN . ZN ? ? H CYS 10   H ZN 101  1_555 ? ? ? ? ? ? ?                       2.314 
? ? 
metalc18 metalc ? ? H CYS 65   SG  ? ? ? 1_555 O ZN . ZN ? ? H CYS 65   H ZN 101  1_555 ? ? ? ? ? ? ?                       2.343 
? ? 
metalc19 metalc ? ? H CYS 66   SG  ? ? ? 1_555 O ZN . ZN ? ? H CYS 66   H ZN 101  1_555 ? ? ? ? ? ? ?                       2.324 
? ? 
hydrog1  hydrog ? ? I DG  1    N2  ? ? ? 1_555 J DC 5 N3 ? ? X DG  20   Y DC -20  1_555 ? ? ? ? ? ? 'DG-DC PAIR'            ?     
? ? 
hydrog2  hydrog ? ? I DC  2    N3  ? ? ? 1_555 J DG 4 N2 ? ? X DC  21   Y DG -21  1_555 ? ? ? ? ? ? 'REVERSED WATSON-CRICK' ?     
? ? 
hydrog3  hydrog ? ? I DC  2    O2  ? ? ? 1_555 J DG 4 N1 ? ? X DC  21   Y DG -21  1_555 ? ? ? ? ? ? 'REVERSED WATSON-CRICK' ?     
? ? 
hydrog4  hydrog ? ? I DC  3    N3  ? ? ? 1_555 J DG 3 N1 ? ? X DC  22   Y DG -22  1_555 ? ? ? ? ? ? WATSON-CRICK            ?     
? ? 
hydrog5  hydrog ? ? I DC  3    N4  ? ? ? 1_555 J DG 3 O6 ? ? X DC  22   Y DG -22  1_555 ? ? ? ? ? ? WATSON-CRICK            ?     
? ? 
hydrog6  hydrog ? ? I DC  3    O2  ? ? ? 1_555 J DG 3 N2 ? ? X DC  22   Y DG -22  1_555 ? ? ? ? ? ? WATSON-CRICK            ?     
? ? 
hydrog7  hydrog ? ? I DG  4    N1  ? ? ? 1_555 J DC 2 N3 ? ? X DG  23   Y DC -23  1_555 ? ? ? ? ? ? WATSON-CRICK            ?     
? ? 
hydrog8  hydrog ? ? I DG  4    N2  ? ? ? 1_555 J DC 2 O2 ? ? X DG  23   Y DC -23  1_555 ? ? ? ? ? ? WATSON-CRICK            ?     
? ? 
hydrog9  hydrog ? ? I DG  4    O6  ? ? ? 1_555 J DC 2 N4 ? ? X DG  23   Y DC -23  1_555 ? ? ? ? ? ? WATSON-CRICK            ?     
? ? 
hydrog10 hydrog ? ? I DA  5    N1  ? ? ? 1_555 J DT 1 N3 ? ? X DA  24   Y DT -24  1_555 ? ? ? ? ? ? WATSON-CRICK            ?     
? ? 
hydrog11 hydrog ? ? I DA  5    N6  ? ? ? 1_555 J DT 1 O4 ? ? X DA  24   Y DT -24  1_555 ? ? ? ? ? ? WATSON-CRICK            ?     
? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
metalc ? ? 
hydrog ? ? 
# 
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  SG  ? A CYS 59   ? A CYS 59   ? 1_555 ZN ? L ZN . ? A ZN 1502 ? 1_555 SG  ? A CYS 62   ? A CYS 62   ? 1_555 103.0 ? 
2  SG  ? A CYS 59   ? A CYS 59   ? 1_555 ZN ? L ZN . ? A ZN 1502 ? 1_555 SG  ? A CYS 69   ? A CYS 69   ? 1_555 106.1 ? 
3  SG  ? A CYS 62   ? A CYS 62   ? 1_555 ZN ? L ZN . ? A ZN 1502 ? 1_555 SG  ? A CYS 69   ? A CYS 69   ? 1_555 111.2 ? 
4  SG  ? A CYS 59   ? A CYS 59   ? 1_555 ZN ? L ZN . ? A ZN 1502 ? 1_555 NE2 ? A HIS 72   ? A HIS 72   ? 1_555 102.6 ? 
5  SG  ? A CYS 62   ? A CYS 62   ? 1_555 ZN ? L ZN . ? A ZN 1502 ? 1_555 NE2 ? A HIS 72   ? A HIS 72   ? 1_555 103.5 ? 
6  SG  ? A CYS 69   ? A CYS 69   ? 1_555 ZN ? L ZN . ? A ZN 1502 ? 1_555 NE2 ? A HIS 72   ? A HIS 72   ? 1_555 127.7 ? 
7  OD1 ? A ASP 457  ? A ASP 457  ? 1_555 MG ? K MG . ? A MG 1501 ? 1_555 OD1 ? A ASP 459  ? A ASP 459  ? 1_555 88.9  ? 
8  OD1 ? A ASP 457  ? A ASP 457  ? 1_555 MG ? K MG . ? A MG 1501 ? 1_555 OD1 ? A ASP 461  ? A ASP 461  ? 1_555 103.3 ? 
9  OD1 ? A ASP 459  ? A ASP 459  ? 1_555 MG ? K MG . ? A MG 1501 ? 1_555 OD1 ? A ASP 461  ? A ASP 461  ? 1_555 89.2  ? 
10 SG  ? B CYS 1180 ? B CYS 1180 ? 1_555 ZN ? M ZN . ? B ZN 1301 ? 1_555 SG  ? B CYS 1183 ? B CYS 1183 ? 1_555 118.0 ? 
11 SG  ? B CYS 1180 ? B CYS 1180 ? 1_555 ZN ? M ZN . ? B ZN 1301 ? 1_555 SG  ? B CYS 1198 ? B CYS 1198 ? 1_555 109.0 ? 
12 SG  ? B CYS 1183 ? B CYS 1183 ? 1_555 ZN ? M ZN . ? B ZN 1301 ? 1_555 SG  ? B CYS 1198 ? B CYS 1198 ? 1_555 87.8  ? 
13 SG  ? B CYS 1180 ? B CYS 1180 ? 1_555 ZN ? M ZN . ? B ZN 1301 ? 1_555 SG  ? B CYS 1201 ? B CYS 1201 ? 1_555 125.2 ? 
14 SG  ? B CYS 1183 ? B CYS 1183 ? 1_555 ZN ? M ZN . ? B ZN 1301 ? 1_555 SG  ? B CYS 1201 ? B CYS 1201 ? 1_555 106.8 ? 
15 SG  ? B CYS 1198 ? B CYS 1198 ? 1_555 ZN ? M ZN . ? B ZN 1301 ? 1_555 SG  ? B CYS 1201 ? B CYS 1201 ? 1_555 102.4 ? 
16 SG  ? G CYS 73   ? G CYS 73   ? 1_555 ZN ? N ZN . ? G ZN 201  ? 1_555 SG  ? G CYS 76   ? G CYS 76   ? 1_555 114.2 ? 
17 SG  ? G CYS 73   ? G CYS 73   ? 1_555 ZN ? N ZN . ? G ZN 201  ? 1_555 SG  ? G CYS 96   ? G CYS 96   ? 1_555 103.5 ? 
18 SG  ? G CYS 76   ? G CYS 76   ? 1_555 ZN ? N ZN . ? G ZN 201  ? 1_555 SG  ? G CYS 96   ? G CYS 96   ? 1_555 104.0 ? 
19 SG  ? G CYS 73   ? G CYS 73   ? 1_555 ZN ? N ZN . ? G ZN 201  ? 1_555 SG  ? G CYS 98   ? G CYS 98   ? 1_555 121.7 ? 
20 SG  ? G CYS 76   ? G CYS 76   ? 1_555 ZN ? N ZN . ? G ZN 201  ? 1_555 SG  ? G CYS 98   ? G CYS 98   ? 1_555 108.6 ? 
21 SG  ? G CYS 96   ? G CYS 96   ? 1_555 ZN ? N ZN . ? G ZN 201  ? 1_555 SG  ? G CYS 98   ? G CYS 98   ? 1_555 102.3 ? 
22 SG  ? H CYS 7    ? H CYS 7    ? 1_555 ZN ? O ZN . ? H ZN 101  ? 1_555 SG  ? H CYS 10   ? H CYS 10   ? 1_555 111.5 ? 
23 SG  ? H CYS 7    ? H CYS 7    ? 1_555 ZN ? O ZN . ? H ZN 101  ? 1_555 SG  ? H CYS 65   ? H CYS 65   ? 1_555 107.3 ? 
24 SG  ? H CYS 10   ? H CYS 10   ? 1_555 ZN ? O ZN . ? H ZN 101  ? 1_555 SG  ? H CYS 65   ? H CYS 65   ? 1_555 116.1 ? 
25 SG  ? H CYS 7    ? H CYS 7    ? 1_555 ZN ? O ZN . ? H ZN 101  ? 1_555 SG  ? H CYS 66   ? H CYS 66   ? 1_555 112.4 ? 
26 SG  ? H CYS 10   ? H CYS 10   ? 1_555 ZN ? O ZN . ? H ZN 101  ? 1_555 SG  ? H CYS 66   ? H CYS 66   ? 1_555 98.1  ? 
27 SG  ? H CYS 65   ? H CYS 65   ? 1_555 ZN ? O ZN . ? H ZN 101  ? 1_555 SG  ? H CYS 66   ? H CYS 66   ? 1_555 111.4 ? 
# 
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 TYR 373 A . ? TYR 373 A PRO 374 A ? PRO 374 A 1 -3.24 
2 GLN 420 A . ? GLN 420 A PRO 421 A ? PRO 421 A 1 0.78  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 2 ? 
AA6 ? 8 ? 
AA7 ? 4 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 3 ? 
AB2 ? 2 ? 
AB3 ? 3 ? 
AB4 ? 2 ? 
AB5 ? 2 ? 
AB6 ? 2 ? 
AB7 ? 4 ? 
AB8 ? 2 ? 
AB9 ? 5 ? 
AC1 ? 4 ? 
AC2 ? 2 ? 
AC3 ? 3 ? 
AC4 ? 4 ? 
AC5 ? 5 ? 
AC6 ? 3 ? 
AC7 ? 4 ? 
AC8 ? 5 ? 
AC9 ? 5 ? 
AD1 ? 2 ? 
AD2 ? 8 ? 
AD3 ? 3 ? 
AD4 ? 2 ? 
AD5 ? 2 ? 
AD6 ? 2 ? 
AD7 ? 4 ? 
AD8 ? 4 ? 
AD9 ? 2 ? 
AE1 ? 4 ? 
AE2 ? 5 ? 
AE3 ? 4 ? 
AE4 ? 3 ? 
AE5 ? 3 ? 
AE6 ? 3 ? 
AE7 ? 4 ? 
AE8 ? 5 ? 
AE9 ? 3 ? 
# 
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 ? parallel      
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? parallel      
AA6 6 7 ? anti-parallel 
AA6 7 8 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
AB9 3 4 ? parallel      
AB9 4 5 ? parallel      
AC1 1 2 ? anti-parallel 
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC4 2 3 ? parallel      
AC4 3 4 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC5 2 3 ? anti-parallel 
AC5 3 4 ? anti-parallel 
AC5 4 5 ? anti-parallel 
AC6 1 2 ? anti-parallel 
AC6 2 3 ? anti-parallel 
AC7 1 2 ? anti-parallel 
AC7 2 3 ? anti-parallel 
AC7 3 4 ? parallel      
AC8 1 2 ? anti-parallel 
AC8 2 3 ? anti-parallel 
AC8 3 4 ? parallel      
AC8 4 5 ? anti-parallel 
AC9 1 2 ? anti-parallel 
AC9 2 3 ? anti-parallel 
AC9 3 4 ? anti-parallel 
AC9 4 5 ? anti-parallel 
AD1 1 2 ? parallel      
AD2 1 2 ? anti-parallel 
AD2 2 3 ? anti-parallel 
AD2 3 4 ? anti-parallel 
AD2 4 5 ? parallel      
AD2 5 6 ? anti-parallel 
AD2 6 7 ? parallel      
AD2 7 8 ? anti-parallel 
AD3 1 2 ? anti-parallel 
AD3 2 3 ? anti-parallel 
AD4 1 2 ? anti-parallel 
AD5 1 2 ? anti-parallel 
AD6 1 2 ? anti-parallel 
AD7 1 2 ? anti-parallel 
AD7 2 3 ? anti-parallel 
AD7 3 4 ? anti-parallel 
AD8 1 2 ? anti-parallel 
AD8 2 3 ? anti-parallel 
AD8 3 4 ? anti-parallel 
AD9 1 2 ? anti-parallel 
AE1 1 2 ? anti-parallel 
AE1 2 3 ? anti-parallel 
AE1 3 4 ? anti-parallel 
AE2 1 2 ? anti-parallel 
AE2 2 3 ? anti-parallel 
AE2 3 4 ? parallel      
AE2 4 5 ? parallel      
AE3 1 2 ? anti-parallel 
AE3 2 3 ? anti-parallel 
AE3 3 4 ? parallel      
AE4 1 2 ? anti-parallel 
AE4 2 3 ? anti-parallel 
AE5 1 2 ? anti-parallel 
AE5 2 3 ? anti-parallel 
AE6 1 2 ? anti-parallel 
AE6 2 3 ? anti-parallel 
AE7 1 2 ? anti-parallel 
AE7 2 3 ? anti-parallel 
AE7 3 4 ? parallel      
AE8 1 2 ? anti-parallel 
AE8 2 3 ? anti-parallel 
AE8 3 4 ? anti-parallel 
AE8 4 5 ? parallel      
AE9 1 2 ? anti-parallel 
AE9 2 3 ? 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 GLY A 4    ? TYR A 5    ? GLY A 4    TYR A 5    
AA1 2 ILE B 1207 ? ARG B 1213 ? ILE B 1207 ARG B 1213 
AA1 3 GLY B 1174 ? CYS B 1180 ? GLY B 1174 CYS B 1180 
AA2 1 VAL A 1404 ? PRO A 1406 ? VAL A 1404 PRO A 1406 
AA2 2 ILE A 8    ? ILE A 15   ? ILE A 8    ILE A 15   
AA2 3 VAL B 1228 ? LEU B 1234 ? VAL B 1228 LEU B 1234 
AA3 1 GLY A 74   ? LEU A 83   ? GLY A 74   LEU A 83   
AA3 2 VAL A 197  ? ILE A 203  ? VAL A 197  ILE A 203  
AA4 1 LYS A 143  ? LYS A 146  ? LYS A 143  LYS A 146  
AA4 2 PHE A 154  ? GLN A 158  ? PHE A 154  GLN A 158  
AA4 3 LYS A 161  ? LYS A 164  ? LYS A 161  LYS A 164  
AA5 1 SER A 317  ? VAL A 319  ? SER A 317  VAL A 319  
AA5 2 LEU B 1145 ? LEU B 1147 ? LEU B 1145 LEU B 1147 
AA6 1 TYR B 1120 ? ALA B 1121 ? TYR B 1120 ALA B 1121 
AA6 2 ILE A 322  ? GLY A 329  ? ILE A 322  GLY A 329  
AA6 3 GLN A 462  ? TRP A 466  ? GLN A 462  TRP A 466  
AA6 4 VAL A 414  ? ASN A 418  ? VAL A 414  ASN A 418  
AA6 5 ILE A 428  ? LEU A 436  ? ILE A 428  LEU A 436  
AA6 6 GLU A 337  ? PRO A 341  ? GLU A 337  PRO A 341  
AA6 7 PHE A 444  ? MET A 446  ? PHE A 444  MET A 446  
AA6 8 ILE A 322  ? GLY A 329  ? ILE A 322  GLY A 329  
AA7 1 GLN A 349  ? THR A 353  ? GLN A 349  THR A 353  
AA7 2 ILE A 404  ? ASP A 408  ? ILE A 404  ASP A 408  
AA7 3 CYS A 376  ? LYS A 381  ? CYS A 376  LYS A 381  
AA7 4 SER A 386  ? ASP A 389  ? SER A 386  ASP A 389  
AA8 1 ASN A 514  ? THR A 515  ? ASN A 514  THR A 515  
AA8 2 GLY A 518  ? LYS A 519  ? GLY A 518  LYS A 519  
AA9 1 VAL A 521  ? ASN A 523  ? VAL A 521  ASN A 523  
AA9 2 LEU A 549  ? ASP A 551  ? LEU A 549  ASP A 551  
AB1 1 ASN A 566  ? ARG A 569  ? ASN A 566  ARG A 569  
AB1 2 THR A 591  ? ARG A 594  ? THR A 591  ARG A 594  
AB1 3 GLU A 597  ? GLU A 600  ? GLU A 597  GLU A 600  
AB2 1 GLY A 753  ? GLN A 754  ? GLY A 753  GLN A 754  
AB2 2 PHE A 787  ? ILE A 788  ? PHE A 787  ILE A 788  
AB3 1 ILE A 837  ? VAL A 838  ? ILE A 837  VAL A 838  
AB3 2 VAL A 844  ? ILE A 846  ? VAL A 844  ILE A 846  
AB3 3 ARG A 849  ? GLN A 852  ? ARG A 849  GLN A 852  
AB4 1 GLU A 866  ? ARG A 869  ? GLU A 866  ARG A 869  
AB4 2 VAL A 927  ? VAL A 930  ? VAL A 927  VAL A 930  
AB5 1 MET A 1094 ? LEU A 1095 ? MET A 1094 LEU A 1095 
AB5 2 VAL A 1315 ? SER A 1316 ? VAL A 1315 SER A 1316 
AB6 1 ILE A 1120 ? THR A 1121 ? ILE A 1120 THR A 1121 
AB6 2 THR A 1258 ? ARG A 1260 ? THR A 1258 ARG A 1260 
AB7 1 ILE A 1126 ? TRP A 1129 ? ILE A 1126 TRP A 1129 
AB7 2 ILE A 1176 ? LEU A 1180 ? ILE A 1176 LEU A 1180 
AB7 3 ILE A 1222 ? LEU A 1227 ? ILE A 1222 LEU A 1227 
AB7 4 THR A 1206 ? TYR A 1207 ? THR A 1206 TYR A 1207 
AB8 1 ASN A 1267 ? VAL A 1278 ? ASN A 1267 VAL A 1278 
AB8 2 LEU A 1284 ? ASN A 1296 ? LEU A 1284 ASN A 1296 
AB9 1 ASP A 1428 ? MET A 1431 ? ASP A 1428 MET A 1431 
AB9 2 LEU E 117  ? THR E 126  ? LEU E 117  THR E 126  
AB9 3 GLN E 130  ? TRP E 136  ? GLN E 130  TRP E 136  
AB9 4 GLN E 55   ? ILE E 59   ? GLN E 55   ILE E 59   
AB9 5 VAL B 1238 ? PHE B 1239 ? VAL B 1238 PHE B 1239 
AC1 1 VAL B 65   ? LYS B 70   ? VAL B 65   LYS B 70   
AC1 2 ARG B 82   ? ILE B 96   ? ARG B 82   ILE B 96   
AC1 3 SER B 125  ? TYR B 140  ? SER B 125  TYR B 140  
AC1 4 GLN B 145  ? PRO B 161  ? GLN B 145  PRO B 161  
AC2 1 GLN B 100  ? HIS B 101  ? GLN B 100  HIS B 101  
AC2 2 ILE B 110  ? ASN B 111  ? ILE B 110  ASN B 111  
AC3 1 PHE B 193  ? ALA B 195  ? PHE B 193  ALA B 195  
AC3 2 GLY B 198  ? VAL B 202  ? GLY B 198  VAL B 202  
AC3 3 THR B 506  ? SER B 508  ? THR B 506  SER B 508  
AC4 1 LYS B 416  ? VAL B 418  ? LYS B 416  VAL B 418  
AC4 2 LEU B 204  ? ILE B 208  ? LEU B 204  ILE B 208  
AC4 3 THR B 523  ? ASN B 525  ? THR B 523  ASN B 525  
AC4 4 LYS B 569  ? GLN B 570  ? LYS B 569  GLN B 570  
AC5 1 LEU B 213  ? HIS B 216  ? LEU B 213  HIS B 216  
AC5 2 GLU B 226  ? SER B 234  ? GLU B 226  SER B 234  
AC5 3 SER B 244  ? MET B 251  ? SER B 244  MET B 251  
AC5 4 ILE B 256  ? ASN B 261  ? ILE B 256  ASN B 261  
AC5 5 ARG B 269  ? PRO B 271  ? ARG B 269  PRO B 271  
AC6 1 ASN B 576  ? VAL B 577  ? ASN B 576  VAL B 577  
AC6 2 LEU B 669  ? ASN B 678  ? LEU B 669  ASN B 678  
AC6 3 CYS B 738  ? ILE B 741  ? CYS B 738  ILE B 741  
AC7 1 GLN B 710  ? THR B 712  ? GLN B 710  THR B 712  
AC7 2 LEU B 669  ? ASN B 678  ? LEU B 669  ASN B 678  
AC7 3 HIS B 771  ? VAL B 772  ? HIS B 771  VAL B 772  
AC7 4 VAL B 751  ? ALA B 752  ? VAL B 751  ALA B 752  
AC8 1 ILE B 596  ? GLN B 597  ? ILE B 596  GLN B 597  
AC8 2 GLU B 620  ? CYS B 625  ? GLU B 620  CYS B 625  
AC8 3 ALA B 613  ? ILE B 617  ? ALA B 613  ILE B 617  
AC8 4 GLU B 659  ? TRP B 663  ? GLU B 659  TRP B 663  
AC8 5 THR B 650  ? ASP B 654  ? THR B 650  ASP B 654  
AC9 1 ARG B 823  ? GLN B 826  ? ARG B 823  GLN B 826  
AC9 2 GLY B 879  ? GLU B 888  ? GLY B 879  GLU B 888  
AC9 3 PHE B 979  ? ARG B 988  ? PHE B 979  ARG B 988  
AC9 4 ALA B 963  ? MET B 969  ? ALA B 963  MET B 969  
AC9 5 VAL B 926  ? VAL B 927  ? VAL B 926  VAL B 927  
AD1 1 VAL B 834  ? LYS B 835  ? VAL B 834  LYS B 835  
AD1 2 THR B 1058 ? ASP B 1059 ? THR B 1058 ASP B 1059 
AD2 1 CYS B 1085 ? GLN B 1086 ? CYS B 1085 GLN B 1086 
AD2 2 ILE B 1101 ? ARG B 1110 ? ILE B 1101 ARG B 1110 
AD2 3 LYS B 995  ? SER B 998  ? LYS B 995  SER B 998  
AD2 4 LYS B 1003 ? LEU B 1010 ? LYS B 1003 LEU B 1010 
AD2 5 SER B 864  ? SER B 868  ? SER B 864  SER B 868  
AD2 6 LEU B 1026 ? VAL B 1028 ? LEU B 1026 VAL B 1028 
AD2 7 LEU B 847  ? TYR B 853  ? LEU B 847  TYR B 853  
AD2 8 ILE B 1101 ? ARG B 1110 ? ILE B 1101 ARG B 1110 
AD3 1 GLU B 894  ? PHE B 896  ? GLU B 894  PHE B 896  
AD3 2 LYS B 936  ? ALA B 938  ? LYS B 936  ALA B 938  
AD3 3 ILE B 951  ? ASP B 952  ? ILE B 951  ASP B 952  
AD4 1 ILE B 932  ? ILE B 934  ? ILE B 932  ILE B 934  
AD4 2 VAL B 955  ? MET B 956  ? VAL B 955  MET B 956  
AD5 1 PHE B 1017 ? THR B 1018 ? PHE B 1017 THR B 1018 
AD5 2 MET B 1088 ? PHE B 1089 ? MET B 1088 PHE B 1089 
AD6 1 ILE B 1188 ? ASN B 1190 ? ILE B 1188 ASN B 1190 
AD6 2 ILE B 1195 ? LYS B 1197 ? ILE B 1195 LYS B 1197 
AD7 1 PHE C 5    ? PRO C 12   ? PHE C 5    PRO C 12   
AD7 2 LEU C 38   ? LYS C 48   ? LEU C 38   LYS C 48   
AD7 3 HIS C 216  ? PRO C 227  ? HIS C 216  PRO C 227  
AD7 4 VAL C 180  ? HIS C 186  ? VAL C 180  HIS C 186  
AD8 1 ASN C 68   ? ILE C 73   ? ASN C 68   ILE C 73   
AD8 2 SER C 157  ? GLY C 168  ? SER C 157  GLY C 168  
AD8 3 VAL C 110  ? LEU C 116  ? VAL C 110  LEU C 116  
AD8 4 LEU C 130  ? ALA C 134  ? LEU C 130  ALA C 134  
AD9 1 LYS C 123  ? TYR C 126  ? LYS C 123  TYR C 126  
AD9 2 GLU C 148  ? LEU C 152  ? GLU C 148  LEU C 152  
AE1 1 LEU C 267  ? SER C 271  ? LEU C 267  SER C 271  
AE1 2 THR C 277  ? LYS C 284  ? THR C 277  LYS C 284  
AE1 3 GLU C 318  ? HIS C 325  ? GLU C 318  HIS C 325  
AE1 4 PHE C 307  ? GLN C 311  ? PHE C 307  GLN C 311  
AE2 1 VAL D 20   ? LEU D 21   ? VAL D 20   LEU D 21   
AE2 2 PHE D 40   ? GLU D 46   ? PHE D 40   GLU D 46   
AE2 3 ILE D 52   ? PHE D 58   ? ILE D 52   PHE D 58   
AE2 4 TYR D 85   ? ILE D 91   ? TYR D 85   ILE D 91   
AE2 5 VAL D 117  ? TYR D 121  ? VAL D 117  TYR D 121  
AE3 1 LYS D 138  ? ILE D 142  ? LYS D 138  ILE D 142  
AE3 2 PHE D 181  ? SER D 188  ? PHE D 181  SER D 188  
AE3 3 MET D 192  ? THR D 201  ? MET D 192  THR D 201  
AE3 4 MET D 162  ? SER D 165  ? MET D 162  SER D 165  
AE4 1 ILE F 2    ? ILE F 13   ? ILE F 2    ILE F 13   
AE4 2 GLY F 68   ? SER F 79   ? GLY F 68   SER F 79   
AE4 3 ILE F 45   ? ARG F 54   ? ILE F 45   ARG F 54   
AE5 1 ILE F 2    ? ILE F 13   ? ILE F 2    ILE F 13   
AE5 2 GLY F 68   ? SER F 79   ? GLY F 68   SER F 79   
AE5 3 PHE F 58   ? ILE F 59   ? PHE F 58   ILE F 59   
AE6 1 LEU F 86   ? ILE F 87   ? LEU F 86   ILE F 87   
AE6 2 VAL F 132  ? LEU F 134  ? VAL F 132  LEU F 134  
AE6 3 GLY F 152  ? ILE F 154  ? GLY F 152  ILE F 154  
AE7 1 LYS F 91   ? ASN F 95   ? LYS F 91   ASN F 95   
AE7 2 ILE F 99   ? GLU F 103  ? ILE F 99   GLU F 103  
AE7 3 THR F 111  ? PRO F 115  ? THR F 111  PRO F 115  
AE7 4 SER F 149  ? ALA F 150  ? SER F 149  ALA F 150  
AE8 1 CYS F 237  ? ASN F 238  ? CYS F 237  ASN F 238  
AE8 2 LEU F 269  ? GLN F 273  ? LEU F 269  GLN F 273  
AE8 3 GLY F 255  ? ALA F 258  ? GLY F 255  ALA F 258  
AE8 4 VAL F 163  ? VAL F 166  ? VAL F 163  VAL F 166  
AE8 5 ILE F 285  ? CYS F 287  ? ILE F 285  CYS F 287  
AE9 1 GLN G 68   ? LYS G 70   ? GLN G 68   LYS G 70   
AE9 2 TYR G 80   ? ILE G 86   ? TYR G 80   ILE G 86   
AE9 3 ILE G 91   ? VAL G 95   ? ILE G 91   VAL G 95   
# 
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 GLY A 4    ? N GLY A 4    O MET B 1209 ? O MET B 1209 
AA1 2 3 O VAL B 1210 ? O VAL B 1210 N SER B 1177 ? N SER B 1177 
AA2 1 2 O ASN A 1405 ? O ASN A 1405 N VAL A 11   ? N VAL A 11   
AA2 2 3 N ALA A 9    ? N ALA A 9    O VAL B 1233 ? O VAL B 1233 
AA3 1 2 N GLY A 74   ? N GLY A 74   O ILE A 203  ? O ILE A 203  
AA4 1 2 N LYS A 143  ? N LYS A 143  O ASP A 157  ? O ASP A 157  
AA4 2 3 N GLN A 158  ? N GLN A 158  O LYS A 161  ? O LYS A 161  
AA5 1 2 N VAL A 319  ? N VAL A 319  O LEU B 1145 ? O LEU B 1145 
AA6 1 2 O TYR B 1120 ? O TYR B 1120 N ARG A 324  ? N ARG A 324  
AA6 2 3 N SER A 323  ? N SER A 323  O LEU A 465  ? O LEU A 465  
AA6 3 4 O ASN A 464  ? O ASN A 464  N ASN A 418  ? N ASN A 418  
AA6 4 5 N PHE A 417  ? N PHE A 417  O GLY A 429  ? O GLY A 429  
AA6 5 6 O LEU A 436  ? O LEU A 436  N TYR A 340  ? N TYR A 340  
AA6 6 7 N GLY A 339  ? N GLY A 339  O GLN A 445  ? O GLN A 445  
AA6 7 8 O PHE A 444  ? O PHE A 444  N THR A 326  ? N THR A 326  
AA7 1 2 N GLU A 352  ? N GLU A 352  O LEU A 405  ? O LEU A 405  
AA7 2 3 O ILE A 404  ? O ILE A 404  N TYR A 380  ? N TYR A 380  
AA7 3 4 N LYS A 381  ? N LYS A 381  O SER A 386  ? O SER A 386  
AA8 1 2 N THR A 515  ? N THR A 515  O GLY A 518  ? O GLY A 518  
AA9 1 2 N MET A 522  ? N MET A 522  O LEU A 550  ? O LEU A 550  
AB1 1 2 N TYR A 567  ? N TYR A 567  O ILE A 593  ? O ILE A 593  
AB1 2 3 N ARG A 594  ? N ARG A 594  O GLU A 597  ? O GLU A 597  
AB2 1 2 N GLY A 753  ? N GLY A 753  O ILE A 788  ? O ILE A 788  
AB3 1 2 N ILE A 837  ? N ILE A 837  O SER A 845  ? O SER A 845  
AB3 2 3 N VAL A 844  ? N VAL A 844  O VAL A 851  ? O VAL A 851  
AB4 1 2 N GLU A 866  ? N GLU A 866  O VAL A 930  ? O VAL A 930  
AB5 1 2 N LEU A 1095 ? N LEU A 1095 O VAL A 1315 ? O VAL A 1315 
AB6 1 2 N ILE A 1120 ? N ILE A 1120 O ARG A 1260 ? O ARG A 1260 
AB7 1 2 N GLN A 1128 ? N GLN A 1128 O GLU A 1179 ? O GLU A 1179 
AB7 2 3 N LEU A 1178 ? N LEU A 1178 O ILE A 1223 ? O ILE A 1223 
AB7 3 4 O TYR A 1226 ? O TYR A 1226 N TYR A 1207 ? N TYR A 1207 
AB8 1 2 N ARG A 1275 ? N ARG A 1275 O LEU A 1287 ? O LEU A 1287 
AB9 1 2 N ILE A 1430 ? N ILE A 1430 O LEU E 118  ? O LEU E 118  
AB9 2 3 N ARG E 121  ? N ARG E 121  O GLU E 134  ? O GLU E 134  
AB9 3 4 O VAL E 133  ? O VAL E 133  N VAL E 58   ? N VAL E 58   
AB9 4 5 O LEU E 57   ? O LEU E 57   N PHE B 1239 ? N PHE B 1239 
AC1 1 2 N TYR B 69   ? N TYR B 69   O VAL B 85   ? O VAL B 85   
AC1 2 3 N ASN B 95   ? N ASN B 95   O ASN B 129  ? O ASN B 129  
AC1 3 4 N ALA B 138  ? N ALA B 138  O GLU B 146  ? O GLU B 146  
AC2 1 2 N HIS B 101  ? N HIS B 101  O ILE B 110  ? O ILE B 110  
AC3 1 2 N PHE B 193  ? N PHE B 193  O TRP B 200  ? O TRP B 200  
AC3 2 3 N VAL B 201  ? N VAL B 201  O GLN B 507  ? O GLN B 507  
AC4 1 2 O ARG B 417  ? O ARG B 417  N ASN B 207  ? N ASN B 207  
AC4 2 3 N LEU B 204  ? N LEU B 204  O ASN B 525  ? O ASN B 525  
AC4 3 4 N VAL B 524  ? N VAL B 524  O LYS B 569  ? O LYS B 569  
AC5 1 2 N HIS B 216  ? N HIS B 216  O ARG B 229  ? O ARG B 229  
AC5 2 3 N GLY B 230  ? N GLY B 230  O ILE B 248  ? O ILE B 248  
AC5 3 4 N ILE B 247  ? N ILE B 247  O GLU B 259  ? O GLU B 259  
AC5 4 5 N ILE B 258  ? N ILE B 258  O ILE B 270  ? O ILE B 270  
AC6 1 2 N ASN B 576  ? N ASN B 576  O THR B 670  ? O THR B 670  
AC6 2 3 N ARG B 671  ? N ARG B 671  O ILE B 741  ? O ILE B 741  
AC7 1 2 O ASN B 711  ? O ASN B 711  N ASP B 677  ? N ASP B 677  
AC7 2 3 N LEU B 674  ? N LEU B 674  O VAL B 772  ? O VAL B 772  
AC7 3 4 O HIS B 771  ? O HIS B 771  N ALA B 752  ? N ALA B 752  
AC8 1 2 N GLN B 597  ? N GLN B 597  O CYS B 624  ? O CYS B 624  
AC8 2 3 O CYS B 625  ? O CYS B 625  N ALA B 613  ? N ALA B 613  
AC8 3 4 N PHE B 616  ? N PHE B 616  O VAL B 660  ? O VAL B 660  
AC8 4 5 O GLU B 661  ? O GLU B 661  N TYR B 652  ? N TYR B 652  
AC9 1 2 N PHE B 825  ? N PHE B 825  O THR B 880  ? O THR B 880  
AC9 2 3 N ARG B 883  ? N ARG B 883  O LEU B 984  ? O LEU B 984  
AC9 3 4 O ARG B 983  ? O ARG B 983  N ASP B 966  ? N ASP B 966  
AC9 4 5 O ALA B 963  ? O ALA B 963  N VAL B 927  ? N VAL B 927  
AD1 1 2 N LYS B 835  ? N LYS B 835  O THR B 1058 ? O THR B 1058 
AD2 1 2 N GLN B 1086 ? N GLN B 1086 O ILE B 1101 ? O ILE B 1101 
AD2 2 3 O GLN B 1109 ? O GLN B 1109 N SER B 997  ? N SER B 997  
AD2 3 4 N MET B 996  ? N MET B 996  O GLY B 1004 ? O GLY B 1004 
AD2 4 5 O LEU B 1008 ? O LEU B 1008 N VAL B 867  ? N VAL B 867  
AD2 5 6 N ILE B 866  ? N ILE B 866  O ILE B 1027 ? O ILE B 1027 
AD2 6 7 O LEU B 1026 ? O LEU B 1026 N ALA B 852  ? N ALA B 852  
AD2 7 8 N THR B 849  ? N THR B 849  O THR B 1106 ? O THR B 1106 
AD3 1 2 N SER B 895  ? N SER B 895  O VAL B 937  ? O VAL B 937  
AD3 2 3 N ALA B 938  ? N ALA B 938  O ILE B 951  ? O ILE B 951  
AD4 1 2 N ILE B 933  ? N ILE B 933  O VAL B 955  ? O VAL B 955  
AD5 1 2 N PHE B 1017 ? N PHE B 1017 O PHE B 1089 ? O PHE B 1089 
AD6 1 2 N ILE B 1188 ? N ILE B 1188 O LYS B 1197 ? O LYS B 1197 
AD7 1 2 N GLU C 9    ? N GLU C 9    O VAL C 44   ? O VAL C 44   
AD7 2 3 N MET C 45   ? N MET C 45   O LEU C 219  ? O LEU C 219  
AD7 3 4 O GLY C 220  ? O GLY C 220  N HIS C 183  ? N HIS C 183  
AD8 1 2 N MET C 70   ? N MET C 70   O LYS C 166  ? O LYS C 166  
AD8 2 3 O ILE C 160  ? O ILE C 160  N LEU C 113  ? N LEU C 113  
AD8 3 4 N ALA C 112  ? N ALA C 112  O ILE C 131  ? O ILE C 131  
AD9 1 2 N LYS C 123  ? N LYS C 123  O LEU C 152  ? O LEU C 152  
AE1 1 2 N PHE C 270  ? N PHE C 270  O LYS C 278  ? O LYS C 278  
AE1 2 3 N THR C 277  ? N THR C 277  O HIS C 325  ? O HIS C 325  
AE1 3 4 O THR C 322  ? O THR C 322  N GLY C 309  ? N GLY C 309  
AE2 1 2 N VAL D 20   ? N VAL D 20   O GLU D 46   ? O GLU D 46   
AE2 2 3 N ILE D 43   ? N ILE D 43   O VAL D 55   ? O VAL D 55   
AE2 3 4 N PHE D 56   ? N PHE D 56   O ILE D 91   ? O ILE D 91   
AE2 4 5 N LEU D 90   ? N LEU D 90   O ASN D 119  ? O ASN D 119  
AE3 1 2 N LYS D 140  ? N LYS D 140  O GLN D 183  ? O GLN D 183  
AE3 2 3 N VAL D 182  ? N VAL D 182  O ARG D 198  ? O ARG D 198  
AE3 3 4 O THR D 201  ? O THR D 201  N ILE D 164  ? N ILE D 164  
AE4 1 2 N THR F 9    ? N THR F 9    O VAL F 72   ? O VAL F 72   
AE4 2 3 O ARG F 73   ? O ARG F 73   N GLN F 53   ? N GLN F 53   
AE5 1 2 N THR F 9    ? N THR F 9    O VAL F 72   ? O VAL F 72   
AE5 2 3 O TYR F 69   ? O TYR F 69   N PHE F 58   ? N PHE F 58   
AE6 1 2 N ILE F 87   ? N ILE F 87   O VAL F 132  ? O VAL F 132  
AE6 2 3 N GLN F 133  ? N GLN F 133  O SER F 153  ? O SER F 153  
AE7 1 2 N LYS F 94   ? N LYS F 94   O LEU F 101  ? O LEU F 101  
AE7 2 3 N ILE F 100  ? N ILE F 100  O ILE F 114  ? O ILE F 114  
AE7 3 4 N VAL F 113  ? N VAL F 113  O ALA F 150  ? O ALA F 150  
AE8 1 2 N CYS F 237  ? N CYS F 237  O ALA F 270  ? O ALA F 270  
AE8 2 3 O GLN F 273  ? O GLN F 273  N PHE F 256  ? N PHE F 256  
AE8 3 4 O GLY F 255  ? O GLY F 255  N VAL F 166  ? N VAL F 166  
AE8 4 5 N HIS F 165  ? N HIS F 165  O ILE F 285  ? O ILE F 285  
AE9 1 2 N ILE G 69   ? N ILE G 69   O LEU G 81   ? O LEU G 81   
AE9 2 3 N THR G 82   ? N THR G 82   O VAL G 95   ? O VAL G 95   
# 
_pdbx_entry_details.entry_id                   8YQZ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OG1 B THR 807  ? ? ND2 B ASN 845  ? ? 1.99 
2  1 O   B ILE 486  ? ? OG1 B THR 506  ? ? 2.14 
3  1 OG1 E THR 67   ? ? OE1 E GLU 134  ? ? 2.14 
4  1 O   A ARG 49   ? ? OG1 A THR 61   ? ? 2.14 
5  1 OE1 A GLN 1078 ? ? NZ  A LYS 1084 ? ? 2.14 
6  1 OD2 B ASP 1059 ? ? OG1 B THR 1061 ? ? 2.15 
7  1 O   D PHE 58   ? ? OH  D TYR 123  ? ? 2.17 
8  1 OG1 B THR 379  ? ? OD1 B ASP 381  ? ? 2.17 
9  1 OG  A SER 493  ? ? O   A ALA 862  ? ? 2.17 
10 1 OD1 A ASN 681  ? ? OH  A TYR 701  ? ? 2.19 
11 1 O   F ASN 22   ? ? ND1 F HIS 26   ? ? 2.19 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             N 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_1              1101 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_2              1101 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_3              1101 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                91.07 
_pdbx_validate_rmsd_angle.angle_target_value         103.20 
_pdbx_validate_rmsd_angle.angle_deviation            -12.13 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 GLN A 501  ? ? 71.90   -24.60  
2  1 ASP A 502  ? ? -133.44 -31.52  
3  1 ASN A 543  ? ? -92.45  43.09   
4  1 ASP A 604  ? ? -150.32 -156.80 
5  1 ARG A 761  ? ? -69.80  -174.93 
6  1 SER A 767  ? ? 63.00   67.33   
7  1 PHE A 768  ? ? 59.28   71.04   
8  1 ASP A 847  ? ? 72.07   -36.42  
9  1 THR A 848  ? ? -154.21 -23.18  
10 1 GLU A 857  ? ? 64.07   -3.73   
11 1 SER A 921  ? ? -143.11 48.30   
12 1 SER A 944  ? ? -98.53  30.21   
13 1 ILE A 976  ? ? -117.39 -81.14  
14 1 ASN A 977  ? ? 176.29  176.46  
15 1 ALA A 1172 ? ? -98.06  -66.48  
16 1 PRO A 1204 ? ? -82.40  45.87   
17 1 SER A 1211 ? ? 59.01   -153.01 
18 1 SER A 1235 ? ? -99.05  36.08   
19 1 ALA A 1268 ? ? -162.47 101.21  
20 1 ASN A 1289 ? ? -102.35 63.53   
21 1 THR A 1313 ? ? -141.58 25.18   
22 1 LYS A 1346 ? ? -92.39  43.31   
23 1 LEU A 1369 ? ? -98.49  33.43   
24 1 SER A 1389 ? ? -122.53 -57.28  
25 1 SER A 1418 ? ? -106.82 -168.76 
26 1 THR B 92   ? ? -101.69 -61.07  
27 1 ASN B 103  ? ? 68.41   -3.42   
28 1 SER B 158  ? ? -166.42 -164.67 
29 1 PHE B 232  ? ? -163.32 107.19  
30 1 ASN B 328  ? ? -113.01 -169.12 
31 1 HIS B 419  ? ? -97.97  -63.47  
32 1 VAL B 437  ? ? -125.15 -61.78  
33 1 ASP B 658  ? ? 62.29   67.96   
34 1 LEU B 664  ? ? -144.80 25.76   
35 1 ASP B 892  ? ? 71.11   -4.89   
36 1 ARG B 953  ? ? -99.90  58.44   
37 1 ASP B 1098 ? ? -88.63  38.08   
38 1 ALA B 1123 ? ? -116.82 -165.88 
39 1 SER B 1172 ? ? -103.58 -80.95  
40 1 ASP B 1173 ? ? -150.27 31.13   
41 1 HIS B 1193 ? ? 57.00   73.64   
42 1 ASP B 1202 ? ? 73.57   -7.32   
43 1 ASN C 7    ? ? 54.20   72.67   
44 1 ASP C 64   ? ? -146.61 33.97   
45 1 ASN C 118  ? ? -96.22  38.44   
46 1 LYS C 197  ? ? -67.14  1.24    
47 1 ASP C 304  ? ? -106.55 40.41   
48 1 LYS C 326  ? ? -92.23  36.15   
49 1 PRO D 27   ? ? -46.12  161.15  
50 1 MET D 192  ? ? 73.59   -19.31  
51 1 ASN E 90   ? ? -97.72  -63.88  
52 1 ASP F 15   ? ? -151.21 77.12   
53 1 SER F 213  ? ? -91.06  46.63   
54 1 SER F 214  ? ? 68.63   147.46  
55 1 GLU F 216  ? ? -143.46 25.13   
56 1 LYS F 227  ? ? -89.30  48.59   
57 1 LYS F 229  ? ? 47.00   24.88   
58 1 HIS F 337  ? ? -90.90  53.83   
59 1 ASP F 338  ? ? -102.21 62.62   
60 1 MET G 49   ? ? 71.24   -7.53   
61 1 MET H 62   ? ? -88.47  32.96   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8YQZ 
_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                    8YQZ 
_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                  2.78 
_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               266388 
_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       ? 
_em_buffer.pH            7.5 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               NATURAL 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'African swine fever virus RNA polymerase complex' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       '1, 2, 3, 4, 5, 6, 7, 8, 9, 10' 
# 
_em_imaging.entry_id                        8YQZ 
_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           ? 
_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                      ? 
_em_imaging.nominal_defocus_min             1000 
_em_imaging.nominal_defocus_max             2500 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_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            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              8YQZ 
_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   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                8YQZ 
_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 ARG 213  ? A ARG 213  
3   1 Y 1 A LEU 214  ? A LEU 214  
4   1 Y 1 A GLY 215  ? A GLY 215  
5   1 Y 1 A ILE 216  ? A ILE 216  
6   1 Y 1 A GLY 217  ? A GLY 217  
7   1 Y 1 A SER 218  ? A SER 218  
8   1 Y 1 A GLY 219  ? A GLY 219  
9   1 Y 1 A PRO 220  ? A PRO 220  
10  1 Y 1 A GLN 221  ? A GLN 221  
11  1 Y 1 A SER 222  ? A SER 222  
12  1 Y 1 A PHE 223  ? A PHE 223  
13  1 Y 1 A SER 276  ? A SER 276  
14  1 Y 1 A THR 277  ? A THR 277  
15  1 Y 1 A THR 278  ? A THR 278  
16  1 Y 1 A ALA 279  ? A ALA 279  
17  1 Y 1 A THR 280  ? A THR 280  
18  1 Y 1 A GLN 281  ? A GLN 281  
19  1 Y 1 A GLY 282  ? A GLY 282  
20  1 Y 1 A GLY 283  ? A GLY 283  
21  1 Y 1 A THR 284  ? A THR 284  
22  1 Y 1 A GLY 285  ? A GLY 285  
23  1 Y 1 A LYS 286  ? A LYS 286  
24  1 Y 1 A ARG 287  ? A ARG 287  
25  1 Y 1 A GLY 288  ? A GLY 288  
26  1 Y 1 A ILE 289  ? A ILE 289  
27  1 Y 1 A VAL 290  ? A VAL 290  
28  1 Y 1 A MET 291  ? A MET 291  
29  1 Y 1 A GLY 292  ? A GLY 292  
30  1 Y 1 A ALA 293  ? A ALA 293  
31  1 Y 1 A ARG 294  ? A ARG 294  
32  1 Y 1 A PRO 295  ? A PRO 295  
33  1 Y 1 A ALA 296  ? A ALA 296  
34  1 Y 1 A MET 1057 ? A MET 1057 
35  1 Y 1 A LEU 1058 ? A LEU 1058 
36  1 Y 1 A ASP 1059 ? A ASP 1059 
37  1 Y 1 A SER 1060 ? A SER 1060 
38  1 Y 1 A HIS 1061 ? A HIS 1061 
39  1 Y 1 A HIS 1062 ? A HIS 1062 
40  1 Y 1 A ARG 1063 ? A ARG 1063 
41  1 Y 1 A SER 1064 ? A SER 1064 
42  1 Y 1 A VAL 1065 ? A VAL 1065 
43  1 Y 1 A ALA 1066 ? A ALA 1066 
44  1 Y 1 A GLY 1067 ? A GLY 1067 
45  1 Y 1 A GLY 1068 ? A GLY 1068 
46  1 Y 1 A THR 1069 ? A THR 1069 
47  1 Y 1 A ASN 1070 ? A ASN 1070 
48  1 Y 1 A LYS 1071 ? A LYS 1071 
49  1 Y 1 A SER 1072 ? A SER 1072 
50  1 Y 1 A TYR 1133 ? A TYR 1133 
51  1 Y 1 A GLU 1134 ? A GLU 1134 
52  1 Y 1 A THR 1135 ? A THR 1135 
53  1 Y 1 A TYR 1136 ? A TYR 1136 
54  1 Y 1 A SER 1137 ? A SER 1137 
55  1 Y 1 A SER 1138 ? A SER 1138 
56  1 Y 1 A THR 1139 ? A THR 1139 
57  1 Y 1 A LYS 1140 ? A LYS 1140 
58  1 Y 1 A LYS 1141 ? A LYS 1141 
59  1 Y 1 A ASN 1142 ? A ASN 1142 
60  1 Y 1 A GLU 1213 ? A GLU 1213 
61  1 Y 1 A ASN 1214 ? A ASN 1214 
62  1 Y 1 A THR 1215 ? A THR 1215 
63  1 Y 1 A ALA 1216 ? A ALA 1216 
64  1 Y 1 A SER 1217 ? A SER 1217 
65  1 Y 1 A GLY 1218 ? A GLY 1218 
66  1 Y 1 A ILE 1219 ? A ILE 1219 
67  1 Y 1 A PRO 1220 ? A PRO 1220 
68  1 Y 1 A VAL 1443 ? A VAL 1443 
69  1 Y 1 A ASP 1444 ? A ASP 1444 
70  1 Y 1 A SER 1445 ? A SER 1445 
71  1 Y 1 A LEU 1446 ? A LEU 1446 
72  1 Y 1 A ILE 1447 ? A ILE 1447 
73  1 Y 1 A ASP 1448 ? A ASP 1448 
74  1 Y 1 A MET 1449 ? A MET 1449 
75  1 Y 1 A LEU 1450 ? A LEU 1450 
76  1 Y 1 B MET 1    ? B MET 1    
77  1 Y 1 B GLU 2    ? B GLU 2    
78  1 Y 1 B PRO 3    ? B PRO 3    
79  1 Y 1 B LEU 4    ? B LEU 4    
80  1 Y 1 B ARG 5    ? B ARG 5    
81  1 Y 1 B PRO 6    ? B PRO 6    
82  1 Y 1 B GLN 7    ? B GLN 7    
83  1 Y 1 B HIS 218  ? B HIS 218  
84  1 Y 1 B THR 219  ? B THR 219  
85  1 Y 1 B MET 220  ? B MET 220  
86  1 Y 1 B GLN 221  ? B GLN 221  
87  1 Y 1 B GLN 222  ? B GLN 222  
88  1 Y 1 B GLY 223  ? B GLY 223  
89  1 Y 1 B ASN 224  ? B ASN 224  
90  1 Y 1 B ASN 490  ? B ASN 490  
91  1 Y 1 B LYS 491  ? B LYS 491  
92  1 Y 1 B THR 492  ? B THR 492  
93  1 Y 1 B ILE 493  ? B ILE 493  
94  1 Y 1 B MET 494  ? B MET 494  
95  1 Y 1 B VAL 495  ? B VAL 495  
96  1 Y 1 B ARG 496  ? B ARG 496  
97  1 Y 1 B GLN 497  ? B GLN 497  
98  1 Y 1 B ARG 498  ? B ARG 498  
99  1 Y 1 B PRO 499  ? B PRO 499  
100 1 Y 1 B ILE 500  ? B ILE 500  
101 1 Y 1 B VAL 501  ? B VAL 501  
102 1 Y 1 B ASN 502  ? B ASN 502  
103 1 Y 1 B ARG 503  ? B ARG 503  
104 1 Y 1 B HIS 527  ? B HIS 527  
105 1 Y 1 B ASN 528  ? B ASN 528  
106 1 Y 1 B THR 529  ? B THR 529  
107 1 Y 1 B THR 530  ? B THR 530  
108 1 Y 1 B ASN 531  ? B ASN 531  
109 1 Y 1 B ALA 532  ? B ALA 532  
110 1 Y 1 B SER 533  ? B SER 533  
111 1 Y 1 B LYS 534  ? B LYS 534  
112 1 Y 1 B GLN 535  ? B GLN 535  
113 1 Y 1 B THR 536  ? B THR 536  
114 1 Y 1 B ARG 941  ? B ARG 941  
115 1 Y 1 B GLY 942  ? B GLY 942  
116 1 Y 1 B GLU 943  ? B GLU 943  
117 1 Y 1 B LYS 944  ? B LYS 944  
118 1 Y 1 B ASP 945  ? B ASP 945  
119 1 Y 1 B GLU 946  ? B GLU 946  
120 1 Y 1 B LEU 947  ? B LEU 947  
121 1 Y 1 B ASN 948  ? B ASN 948  
122 1 Y 1 C MET 1    ? C MET 1    
123 1 Y 1 C GLU 2    ? C GLU 2    
124 1 Y 1 E MET 1    ? E MET 1    
125 1 Y 1 E ALA 2    ? E ALA 2    
126 1 Y 1 E ASP 3    ? E ASP 3    
127 1 Y 1 E ASN 4    ? E ASN 4    
128 1 Y 1 E ASP 5    ? E ASP 5    
129 1 Y 1 E ASN 6    ? E ASN 6    
130 1 Y 1 E GLU 7    ? E GLU 7    
131 1 Y 1 E ASP 8    ? E ASP 8    
132 1 Y 1 E LEU 9    ? E LEU 9    
133 1 Y 1 E ILE 10   ? E ILE 10   
134 1 Y 1 E MET 11   ? E MET 11   
135 1 Y 1 E ASP 12   ? E ASP 12   
136 1 Y 1 E ASP 13   ? E ASP 13   
137 1 Y 1 E LEU 14   ? E LEU 14   
138 1 Y 1 E VAL 15   ? E VAL 15   
139 1 Y 1 E GLU 16   ? E GLU 16   
140 1 Y 1 E GLU 17   ? E GLU 17   
141 1 Y 1 E TYR 18   ? E TYR 18   
142 1 Y 1 E VAL 19   ? E VAL 19   
143 1 Y 1 E GLU 20   ? E GLU 20   
144 1 Y 1 E THR 21   ? E THR 21   
145 1 Y 1 E GLU 22   ? E GLU 22   
146 1 Y 1 E GLU 23   ? E GLU 23   
147 1 Y 1 E GLU 24   ? E GLU 24   
148 1 Y 1 E ASN 25   ? E ASN 25   
149 1 Y 1 E LEU 26   ? E LEU 26   
150 1 Y 1 E VAL 27   ? E VAL 27   
151 1 Y 1 E ASP 28   ? E ASP 28   
152 1 Y 1 E SER 29   ? E SER 29   
153 1 Y 1 E GLU 30   ? E GLU 30   
154 1 Y 1 E GLU 31   ? E GLU 31   
155 1 Y 1 E GLU 32   ? E GLU 32   
156 1 Y 1 E SER 33   ? E SER 33   
157 1 Y 1 E GLU 34   ? E GLU 34   
158 1 Y 1 E ASP 35   ? E ASP 35   
159 1 Y 1 E LYS 36   ? E LYS 36   
160 1 Y 1 E ASP 37   ? E ASP 37   
161 1 Y 1 E GLU 38   ? E GLU 38   
162 1 Y 1 E ILE 39   ? E ILE 39   
163 1 Y 1 E VAL 40   ? E VAL 40   
164 1 Y 1 E GLU 41   ? E GLU 41   
165 1 Y 1 G MET 1    ? G MET 1    
166 1 Y 1 G LYS 2    ? G LYS 2    
167 1 Y 1 G ILE 3    ? G ILE 3    
168 1 Y 1 G CYS 4    ? G CYS 4    
169 1 Y 1 G LYS 5    ? G LYS 5    
170 1 Y 1 G ALA 6    ? G ALA 6    
171 1 Y 1 G CYS 7    ? G CYS 7    
172 1 Y 1 G SER 8    ? G SER 8    
173 1 Y 1 G SER 9    ? G SER 9    
174 1 Y 1 G CYS 10   ? G CYS 10   
175 1 Y 1 G MET 11   ? G MET 11   
176 1 Y 1 G VAL 12   ? G VAL 12   
177 1 Y 1 G ARG 13   ? G ARG 13   
178 1 Y 1 G THR 14   ? G THR 14   
179 1 Y 1 G TYR 15   ? G TYR 15   
180 1 Y 1 G VAL 16   ? G VAL 16   
181 1 Y 1 G ASP 17   ? G ASP 17   
182 1 Y 1 G GLY 18   ? G GLY 18   
183 1 Y 1 G ASN 19   ? G ASN 19   
184 1 Y 1 G ILE 20   ? G ILE 20   
185 1 Y 1 G ILE 21   ? G ILE 21   
186 1 Y 1 G PHE 22   ? G PHE 22   
187 1 Y 1 G ARG 23   ? G ARG 23   
188 1 Y 1 G CYS 24   ? G CYS 24   
189 1 Y 1 G SER 25   ? G SER 25   
190 1 Y 1 G CYS 26   ? G CYS 26   
191 1 Y 1 G GLY 27   ? G GLY 27   
192 1 Y 1 G GLU 28   ? G GLU 28   
193 1 Y 1 G SER 29   ? G SER 29   
194 1 Y 1 G VAL 30   ? G VAL 30   
195 1 Y 1 G GLN 31   ? G GLN 31   
196 1 Y 1 G GLY 32   ? G GLY 32   
197 1 Y 1 G ASP 33   ? G ASP 33   
198 1 Y 1 G SER 34   ? G SER 34   
199 1 Y 1 G GLN 35   ? G GLN 35   
200 1 Y 1 G ASN 36   ? G ASN 36   
201 1 Y 1 G LEU 37   ? G LEU 37   
202 1 Y 1 G LEU 38   ? G LEU 38   
203 1 Y 1 G VAL 39   ? G VAL 39   
204 1 Y 1 G SER 40   ? G SER 40   
205 1 Y 1 G SER 41   ? G SER 41   
206 1 Y 1 G LYS 42   ? G LYS 42   
207 1 Y 1 G VAL 43   ? G VAL 43   
208 1 Y 1 G TYR 44   ? G TYR 44   
209 1 Y 1 G HIS 45   ? G HIS 45   
210 1 Y 1 G THR 46   ? G THR 46   
# 
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 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CYS N      N  N N 74  
CYS CA     C  N R 75  
CYS C      C  N N 76  
CYS O      O  N N 77  
CYS CB     C  N N 78  
CYS SG     S  N N 79  
CYS OXT    O  N N 80  
CYS H      H  N N 81  
CYS H2     H  N N 82  
CYS HA     H  N N 83  
CYS HB2    H  N N 84  
CYS HB3    H  N N 85  
CYS HG     H  N N 86  
CYS HXT    H  N N 87  
DA  OP3    O  N N 88  
DA  P      P  N N 89  
DA  OP1    O  N N 90  
DA  OP2    O  N N 91  
DA  "O5'"  O  N N 92  
DA  "C5'"  C  N N 93  
DA  "C4'"  C  N R 94  
DA  "O4'"  O  N N 95  
DA  "C3'"  C  N S 96  
DA  "O3'"  O  N N 97  
DA  "C2'"  C  N N 98  
DA  "C1'"  C  N R 99  
DA  N9     N  Y N 100 
DA  C8     C  Y N 101 
DA  N7     N  Y N 102 
DA  C5     C  Y N 103 
DA  C6     C  Y N 104 
DA  N6     N  N N 105 
DA  N1     N  Y N 106 
DA  C2     C  Y N 107 
DA  N3     N  Y N 108 
DA  C4     C  Y N 109 
DA  HOP3   H  N N 110 
DA  HOP2   H  N N 111 
DA  "H5'"  H  N N 112 
DA  "H5''" H  N N 113 
DA  "H4'"  H  N N 114 
DA  "H3'"  H  N N 115 
DA  "HO3'" H  N N 116 
DA  "H2'"  H  N N 117 
DA  "H2''" H  N N 118 
DA  "H1'"  H  N N 119 
DA  H8     H  N N 120 
DA  H61    H  N N 121 
DA  H62    H  N N 122 
DA  H2     H  N N 123 
DC  OP3    O  N N 124 
DC  P      P  N N 125 
DC  OP1    O  N N 126 
DC  OP2    O  N N 127 
DC  "O5'"  O  N N 128 
DC  "C5'"  C  N N 129 
DC  "C4'"  C  N R 130 
DC  "O4'"  O  N N 131 
DC  "C3'"  C  N S 132 
DC  "O3'"  O  N N 133 
DC  "C2'"  C  N N 134 
DC  "C1'"  C  N R 135 
DC  N1     N  N N 136 
DC  C2     C  N N 137 
DC  O2     O  N N 138 
DC  N3     N  N N 139 
DC  C4     C  N N 140 
DC  N4     N  N N 141 
DC  C5     C  N N 142 
DC  C6     C  N N 143 
DC  HOP3   H  N N 144 
DC  HOP2   H  N N 145 
DC  "H5'"  H  N N 146 
DC  "H5''" H  N N 147 
DC  "H4'"  H  N N 148 
DC  "H3'"  H  N N 149 
DC  "HO3'" H  N N 150 
DC  "H2'"  H  N N 151 
DC  "H2''" H  N N 152 
DC  "H1'"  H  N N 153 
DC  H41    H  N N 154 
DC  H42    H  N N 155 
DC  H5     H  N N 156 
DC  H6     H  N N 157 
DG  OP3    O  N N 158 
DG  P      P  N N 159 
DG  OP1    O  N N 160 
DG  OP2    O  N N 161 
DG  "O5'"  O  N N 162 
DG  "C5'"  C  N N 163 
DG  "C4'"  C  N R 164 
DG  "O4'"  O  N N 165 
DG  "C3'"  C  N S 166 
DG  "O3'"  O  N N 167 
DG  "C2'"  C  N N 168 
DG  "C1'"  C  N R 169 
DG  N9     N  Y N 170 
DG  C8     C  Y N 171 
DG  N7     N  Y N 172 
DG  C5     C  Y N 173 
DG  C6     C  N N 174 
DG  O6     O  N N 175 
DG  N1     N  N N 176 
DG  C2     C  N N 177 
DG  N2     N  N N 178 
DG  N3     N  N N 179 
DG  C4     C  Y N 180 
DG  HOP3   H  N N 181 
DG  HOP2   H  N N 182 
DG  "H5'"  H  N N 183 
DG  "H5''" H  N N 184 
DG  "H4'"  H  N N 185 
DG  "H3'"  H  N N 186 
DG  "HO3'" H  N N 187 
DG  "H2'"  H  N N 188 
DG  "H2''" H  N N 189 
DG  "H1'"  H  N N 190 
DG  H8     H  N N 191 
DG  H1     H  N N 192 
DG  H21    H  N N 193 
DG  H22    H  N N 194 
DT  OP3    O  N N 195 
DT  P      P  N N 196 
DT  OP1    O  N N 197 
DT  OP2    O  N N 198 
DT  "O5'"  O  N N 199 
DT  "C5'"  C  N N 200 
DT  "C4'"  C  N R 201 
DT  "O4'"  O  N N 202 
DT  "C3'"  C  N S 203 
DT  "O3'"  O  N N 204 
DT  "C2'"  C  N N 205 
DT  "C1'"  C  N R 206 
DT  N1     N  N N 207 
DT  C2     C  N N 208 
DT  O2     O  N N 209 
DT  N3     N  N N 210 
DT  C4     C  N N 211 
DT  O4     O  N N 212 
DT  C5     C  N N 213 
DT  C7     C  N N 214 
DT  C6     C  N N 215 
DT  HOP3   H  N N 216 
DT  HOP2   H  N N 217 
DT  "H5'"  H  N N 218 
DT  "H5''" H  N N 219 
DT  "H4'"  H  N N 220 
DT  "H3'"  H  N N 221 
DT  "HO3'" H  N N 222 
DT  "H2'"  H  N N 223 
DT  "H2''" H  N N 224 
DT  "H1'"  H  N N 225 
DT  H3     H  N N 226 
DT  H71    H  N N 227 
DT  H72    H  N N 228 
DT  H73    H  N N 229 
DT  H6     H  N N 230 
GLN N      N  N N 231 
GLN CA     C  N S 232 
GLN C      C  N N 233 
GLN O      O  N N 234 
GLN CB     C  N N 235 
GLN CG     C  N N 236 
GLN CD     C  N N 237 
GLN OE1    O  N N 238 
GLN NE2    N  N N 239 
GLN OXT    O  N N 240 
GLN H      H  N N 241 
GLN H2     H  N N 242 
GLN HA     H  N N 243 
GLN HB2    H  N N 244 
GLN HB3    H  N N 245 
GLN HG2    H  N N 246 
GLN HG3    H  N N 247 
GLN HE21   H  N N 248 
GLN HE22   H  N N 249 
GLN HXT    H  N N 250 
GLU N      N  N N 251 
GLU CA     C  N S 252 
GLU C      C  N N 253 
GLU O      O  N N 254 
GLU CB     C  N N 255 
GLU CG     C  N N 256 
GLU CD     C  N N 257 
GLU OE1    O  N N 258 
GLU OE2    O  N N 259 
GLU OXT    O  N N 260 
GLU H      H  N N 261 
GLU H2     H  N N 262 
GLU HA     H  N N 263 
GLU HB2    H  N N 264 
GLU HB3    H  N N 265 
GLU HG2    H  N N 266 
GLU HG3    H  N N 267 
GLU HE2    H  N N 268 
GLU HXT    H  N N 269 
GLY N      N  N N 270 
GLY CA     C  N N 271 
GLY C      C  N N 272 
GLY O      O  N N 273 
GLY OXT    O  N N 274 
GLY H      H  N N 275 
GLY H2     H  N N 276 
GLY HA2    H  N N 277 
GLY HA3    H  N N 278 
GLY HXT    H  N N 279 
HIS N      N  N N 280 
HIS CA     C  N S 281 
HIS C      C  N N 282 
HIS O      O  N N 283 
HIS CB     C  N N 284 
HIS CG     C  Y N 285 
HIS ND1    N  Y N 286 
HIS CD2    C  Y N 287 
HIS CE1    C  Y N 288 
HIS NE2    N  Y N 289 
HIS OXT    O  N N 290 
HIS H      H  N N 291 
HIS H2     H  N N 292 
HIS HA     H  N N 293 
HIS HB2    H  N N 294 
HIS HB3    H  N N 295 
HIS HD1    H  N N 296 
HIS HD2    H  N N 297 
HIS HE1    H  N N 298 
HIS HE2    H  N N 299 
HIS HXT    H  N N 300 
ILE N      N  N N 301 
ILE CA     C  N S 302 
ILE C      C  N N 303 
ILE O      O  N N 304 
ILE CB     C  N S 305 
ILE CG1    C  N N 306 
ILE CG2    C  N N 307 
ILE CD1    C  N N 308 
ILE OXT    O  N N 309 
ILE H      H  N N 310 
ILE H2     H  N N 311 
ILE HA     H  N N 312 
ILE HB     H  N N 313 
ILE HG12   H  N N 314 
ILE HG13   H  N N 315 
ILE HG21   H  N N 316 
ILE HG22   H  N N 317 
ILE HG23   H  N N 318 
ILE HD11   H  N N 319 
ILE HD12   H  N N 320 
ILE HD13   H  N N 321 
ILE HXT    H  N N 322 
LEU N      N  N N 323 
LEU CA     C  N S 324 
LEU C      C  N N 325 
LEU O      O  N N 326 
LEU CB     C  N N 327 
LEU CG     C  N N 328 
LEU CD1    C  N N 329 
LEU CD2    C  N N 330 
LEU OXT    O  N N 331 
LEU H      H  N N 332 
LEU H2     H  N N 333 
LEU HA     H  N N 334 
LEU HB2    H  N N 335 
LEU HB3    H  N N 336 
LEU HG     H  N N 337 
LEU HD11   H  N N 338 
LEU HD12   H  N N 339 
LEU HD13   H  N N 340 
LEU HD21   H  N N 341 
LEU HD22   H  N N 342 
LEU HD23   H  N N 343 
LEU HXT    H  N N 344 
LYS N      N  N N 345 
LYS CA     C  N S 346 
LYS C      C  N N 347 
LYS O      O  N N 348 
LYS CB     C  N N 349 
LYS CG     C  N N 350 
LYS CD     C  N N 351 
LYS CE     C  N N 352 
LYS NZ     N  N N 353 
LYS OXT    O  N N 354 
LYS H      H  N N 355 
LYS H2     H  N N 356 
LYS HA     H  N N 357 
LYS HB2    H  N N 358 
LYS HB3    H  N N 359 
LYS HG2    H  N N 360 
LYS HG3    H  N N 361 
LYS HD2    H  N N 362 
LYS HD3    H  N N 363 
LYS HE2    H  N N 364 
LYS HE3    H  N N 365 
LYS HZ1    H  N N 366 
LYS HZ2    H  N N 367 
LYS HZ3    H  N N 368 
LYS HXT    H  N N 369 
MET N      N  N N 370 
MET CA     C  N S 371 
MET C      C  N N 372 
MET O      O  N N 373 
MET CB     C  N N 374 
MET CG     C  N N 375 
MET SD     S  N N 376 
MET CE     C  N N 377 
MET OXT    O  N N 378 
MET H      H  N N 379 
MET H2     H  N N 380 
MET HA     H  N N 381 
MET HB2    H  N N 382 
MET HB3    H  N N 383 
MET HG2    H  N N 384 
MET HG3    H  N N 385 
MET HE1    H  N N 386 
MET HE2    H  N N 387 
MET HE3    H  N N 388 
MET HXT    H  N N 389 
MG  MG     MG N N 390 
PHE N      N  N N 391 
PHE CA     C  N S 392 
PHE C      C  N N 393 
PHE O      O  N N 394 
PHE CB     C  N N 395 
PHE CG     C  Y N 396 
PHE CD1    C  Y N 397 
PHE CD2    C  Y N 398 
PHE CE1    C  Y N 399 
PHE CE2    C  Y N 400 
PHE CZ     C  Y N 401 
PHE OXT    O  N N 402 
PHE H      H  N N 403 
PHE H2     H  N N 404 
PHE HA     H  N N 405 
PHE HB2    H  N N 406 
PHE HB3    H  N N 407 
PHE HD1    H  N N 408 
PHE HD2    H  N N 409 
PHE HE1    H  N N 410 
PHE HE2    H  N N 411 
PHE HZ     H  N N 412 
PHE HXT    H  N N 413 
PRO N      N  N N 414 
PRO CA     C  N S 415 
PRO C      C  N N 416 
PRO O      O  N N 417 
PRO CB     C  N N 418 
PRO CG     C  N N 419 
PRO CD     C  N N 420 
PRO OXT    O  N N 421 
PRO H      H  N N 422 
PRO HA     H  N N 423 
PRO HB2    H  N N 424 
PRO HB3    H  N N 425 
PRO HG2    H  N N 426 
PRO HG3    H  N N 427 
PRO HD2    H  N N 428 
PRO HD3    H  N N 429 
PRO HXT    H  N N 430 
SER N      N  N N 431 
SER CA     C  N S 432 
SER C      C  N N 433 
SER O      O  N N 434 
SER CB     C  N N 435 
SER OG     O  N N 436 
SER OXT    O  N N 437 
SER H      H  N N 438 
SER H2     H  N N 439 
SER HA     H  N N 440 
SER HB2    H  N N 441 
SER HB3    H  N N 442 
SER HG     H  N N 443 
SER HXT    H  N N 444 
THR N      N  N N 445 
THR CA     C  N S 446 
THR C      C  N N 447 
THR O      O  N N 448 
THR CB     C  N R 449 
THR OG1    O  N N 450 
THR CG2    C  N N 451 
THR OXT    O  N N 452 
THR H      H  N N 453 
THR H2     H  N N 454 
THR HA     H  N N 455 
THR HB     H  N N 456 
THR HG1    H  N N 457 
THR HG21   H  N N 458 
THR HG22   H  N N 459 
THR HG23   H  N N 460 
THR HXT    H  N N 461 
TRP N      N  N N 462 
TRP CA     C  N S 463 
TRP C      C  N N 464 
TRP O      O  N N 465 
TRP CB     C  N N 466 
TRP CG     C  Y N 467 
TRP CD1    C  Y N 468 
TRP CD2    C  Y N 469 
TRP NE1    N  Y N 470 
TRP CE2    C  Y N 471 
TRP CE3    C  Y N 472 
TRP CZ2    C  Y N 473 
TRP CZ3    C  Y N 474 
TRP CH2    C  Y N 475 
TRP OXT    O  N N 476 
TRP H      H  N N 477 
TRP H2     H  N N 478 
TRP HA     H  N N 479 
TRP HB2    H  N N 480 
TRP HB3    H  N N 481 
TRP HD1    H  N N 482 
TRP HE1    H  N N 483 
TRP HE3    H  N N 484 
TRP HZ2    H  N N 485 
TRP HZ3    H  N N 486 
TRP HH2    H  N N 487 
TRP HXT    H  N N 488 
TYR N      N  N N 489 
TYR CA     C  N S 490 
TYR C      C  N N 491 
TYR O      O  N N 492 
TYR CB     C  N N 493 
TYR CG     C  Y N 494 
TYR CD1    C  Y N 495 
TYR CD2    C  Y N 496 
TYR CE1    C  Y N 497 
TYR CE2    C  Y N 498 
TYR CZ     C  Y N 499 
TYR OH     O  N N 500 
TYR OXT    O  N N 501 
TYR H      H  N N 502 
TYR H2     H  N N 503 
TYR HA     H  N N 504 
TYR HB2    H  N N 505 
TYR HB3    H  N N 506 
TYR HD1    H  N N 507 
TYR HD2    H  N N 508 
TYR HE1    H  N N 509 
TYR HE2    H  N N 510 
TYR HH     H  N N 511 
TYR HXT    H  N N 512 
VAL N      N  N N 513 
VAL CA     C  N S 514 
VAL C      C  N N 515 
VAL O      O  N N 516 
VAL CB     C  N N 517 
VAL CG1    C  N N 518 
VAL CG2    C  N N 519 
VAL OXT    O  N N 520 
VAL H      H  N N 521 
VAL H2     H  N N 522 
VAL HA     H  N N 523 
VAL HB     H  N N 524 
VAL HG11   H  N N 525 
VAL HG12   H  N N 526 
VAL HG13   H  N N 527 
VAL HG21   H  N N 528 
VAL HG22   H  N N 529 
VAL HG23   H  N N 530 
VAL HXT    H  N N 531 
ZN  ZN     ZN N N 532 
# 
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 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
DA  OP3   P      sing N N 83  
DA  OP3   HOP3   sing N N 84  
DA  P     OP1    doub N N 85  
DA  P     OP2    sing N N 86  
DA  P     "O5'"  sing N N 87  
DA  OP2   HOP2   sing N N 88  
DA  "O5'" "C5'"  sing N N 89  
DA  "C5'" "C4'"  sing N N 90  
DA  "C5'" "H5'"  sing N N 91  
DA  "C5'" "H5''" sing N N 92  
DA  "C4'" "O4'"  sing N N 93  
DA  "C4'" "C3'"  sing N N 94  
DA  "C4'" "H4'"  sing N N 95  
DA  "O4'" "C1'"  sing N N 96  
DA  "C3'" "O3'"  sing N N 97  
DA  "C3'" "C2'"  sing N N 98  
DA  "C3'" "H3'"  sing N N 99  
DA  "O3'" "HO3'" sing N N 100 
DA  "C2'" "C1'"  sing N N 101 
DA  "C2'" "H2'"  sing N N 102 
DA  "C2'" "H2''" sing N N 103 
DA  "C1'" N9     sing N N 104 
DA  "C1'" "H1'"  sing N N 105 
DA  N9    C8     sing Y N 106 
DA  N9    C4     sing Y N 107 
DA  C8    N7     doub Y N 108 
DA  C8    H8     sing N N 109 
DA  N7    C5     sing Y N 110 
DA  C5    C6     sing Y N 111 
DA  C5    C4     doub Y N 112 
DA  C6    N6     sing N N 113 
DA  C6    N1     doub Y N 114 
DA  N6    H61    sing N N 115 
DA  N6    H62    sing N N 116 
DA  N1    C2     sing Y N 117 
DA  C2    N3     doub Y N 118 
DA  C2    H2     sing N N 119 
DA  N3    C4     sing Y N 120 
DC  OP3   P      sing N N 121 
DC  OP3   HOP3   sing N N 122 
DC  P     OP1    doub N N 123 
DC  P     OP2    sing N N 124 
DC  P     "O5'"  sing N N 125 
DC  OP2   HOP2   sing N N 126 
DC  "O5'" "C5'"  sing N N 127 
DC  "C5'" "C4'"  sing N N 128 
DC  "C5'" "H5'"  sing N N 129 
DC  "C5'" "H5''" sing N N 130 
DC  "C4'" "O4'"  sing N N 131 
DC  "C4'" "C3'"  sing N N 132 
DC  "C4'" "H4'"  sing N N 133 
DC  "O4'" "C1'"  sing N N 134 
DC  "C3'" "O3'"  sing N N 135 
DC  "C3'" "C2'"  sing N N 136 
DC  "C3'" "H3'"  sing N N 137 
DC  "O3'" "HO3'" sing N N 138 
DC  "C2'" "C1'"  sing N N 139 
DC  "C2'" "H2'"  sing N N 140 
DC  "C2'" "H2''" sing N N 141 
DC  "C1'" N1     sing N N 142 
DC  "C1'" "H1'"  sing N N 143 
DC  N1    C2     sing N N 144 
DC  N1    C6     sing N N 145 
DC  C2    O2     doub N N 146 
DC  C2    N3     sing N N 147 
DC  N3    C4     doub N N 148 
DC  C4    N4     sing N N 149 
DC  C4    C5     sing N N 150 
DC  N4    H41    sing N N 151 
DC  N4    H42    sing N N 152 
DC  C5    C6     doub N N 153 
DC  C5    H5     sing N N 154 
DC  C6    H6     sing N N 155 
DG  OP3   P      sing N N 156 
DG  OP3   HOP3   sing N N 157 
DG  P     OP1    doub N N 158 
DG  P     OP2    sing N N 159 
DG  P     "O5'"  sing N N 160 
DG  OP2   HOP2   sing N N 161 
DG  "O5'" "C5'"  sing N N 162 
DG  "C5'" "C4'"  sing N N 163 
DG  "C5'" "H5'"  sing N N 164 
DG  "C5'" "H5''" sing N N 165 
DG  "C4'" "O4'"  sing N N 166 
DG  "C4'" "C3'"  sing N N 167 
DG  "C4'" "H4'"  sing N N 168 
DG  "O4'" "C1'"  sing N N 169 
DG  "C3'" "O3'"  sing N N 170 
DG  "C3'" "C2'"  sing N N 171 
DG  "C3'" "H3'"  sing N N 172 
DG  "O3'" "HO3'" sing N N 173 
DG  "C2'" "C1'"  sing N N 174 
DG  "C2'" "H2'"  sing N N 175 
DG  "C2'" "H2''" sing N N 176 
DG  "C1'" N9     sing N N 177 
DG  "C1'" "H1'"  sing N N 178 
DG  N9    C8     sing Y N 179 
DG  N9    C4     sing Y N 180 
DG  C8    N7     doub Y N 181 
DG  C8    H8     sing N N 182 
DG  N7    C5     sing Y N 183 
DG  C5    C6     sing N N 184 
DG  C5    C4     doub Y N 185 
DG  C6    O6     doub N N 186 
DG  C6    N1     sing N N 187 
DG  N1    C2     sing N N 188 
DG  N1    H1     sing N N 189 
DG  C2    N2     sing N N 190 
DG  C2    N3     doub N N 191 
DG  N2    H21    sing N N 192 
DG  N2    H22    sing N N 193 
DG  N3    C4     sing N N 194 
DT  OP3   P      sing N N 195 
DT  OP3   HOP3   sing N N 196 
DT  P     OP1    doub N N 197 
DT  P     OP2    sing N N 198 
DT  P     "O5'"  sing N N 199 
DT  OP2   HOP2   sing N N 200 
DT  "O5'" "C5'"  sing N N 201 
DT  "C5'" "C4'"  sing N N 202 
DT  "C5'" "H5'"  sing N N 203 
DT  "C5'" "H5''" sing N N 204 
DT  "C4'" "O4'"  sing N N 205 
DT  "C4'" "C3'"  sing N N 206 
DT  "C4'" "H4'"  sing N N 207 
DT  "O4'" "C1'"  sing N N 208 
DT  "C3'" "O3'"  sing N N 209 
DT  "C3'" "C2'"  sing N N 210 
DT  "C3'" "H3'"  sing N N 211 
DT  "O3'" "HO3'" sing N N 212 
DT  "C2'" "C1'"  sing N N 213 
DT  "C2'" "H2'"  sing N N 214 
DT  "C2'" "H2''" sing N N 215 
DT  "C1'" N1     sing N N 216 
DT  "C1'" "H1'"  sing N N 217 
DT  N1    C2     sing N N 218 
DT  N1    C6     sing N N 219 
DT  C2    O2     doub N N 220 
DT  C2    N3     sing N N 221 
DT  N3    C4     sing N N 222 
DT  N3    H3     sing N N 223 
DT  C4    O4     doub N N 224 
DT  C4    C5     sing N N 225 
DT  C5    C7     sing N N 226 
DT  C5    C6     doub N N 227 
DT  C7    H71    sing N N 228 
DT  C7    H72    sing N N 229 
DT  C7    H73    sing N N 230 
DT  C6    H6     sing N N 231 
GLN N     CA     sing N N 232 
GLN N     H      sing N N 233 
GLN N     H2     sing N N 234 
GLN CA    C      sing N N 235 
GLN CA    CB     sing N N 236 
GLN CA    HA     sing N N 237 
GLN C     O      doub N N 238 
GLN C     OXT    sing N N 239 
GLN CB    CG     sing N N 240 
GLN CB    HB2    sing N N 241 
GLN CB    HB3    sing N N 242 
GLN CG    CD     sing N N 243 
GLN CG    HG2    sing N N 244 
GLN CG    HG3    sing N N 245 
GLN CD    OE1    doub N N 246 
GLN CD    NE2    sing N N 247 
GLN NE2   HE21   sing N N 248 
GLN NE2   HE22   sing N N 249 
GLN OXT   HXT    sing N N 250 
GLU N     CA     sing N N 251 
GLU N     H      sing N N 252 
GLU N     H2     sing N N 253 
GLU CA    C      sing N N 254 
GLU CA    CB     sing N N 255 
GLU CA    HA     sing N N 256 
GLU C     O      doub N N 257 
GLU C     OXT    sing N N 258 
GLU CB    CG     sing N N 259 
GLU CB    HB2    sing N N 260 
GLU CB    HB3    sing N N 261 
GLU CG    CD     sing N N 262 
GLU CG    HG2    sing N N 263 
GLU CG    HG3    sing N N 264 
GLU CD    OE1    doub N N 265 
GLU CD    OE2    sing N N 266 
GLU OE2   HE2    sing N N 267 
GLU OXT   HXT    sing N N 268 
GLY N     CA     sing N N 269 
GLY N     H      sing N N 270 
GLY N     H2     sing N N 271 
GLY CA    C      sing N N 272 
GLY CA    HA2    sing N N 273 
GLY CA    HA3    sing N N 274 
GLY C     O      doub N N 275 
GLY C     OXT    sing N N 276 
GLY OXT   HXT    sing N N 277 
HIS N     CA     sing N N 278 
HIS N     H      sing N N 279 
HIS N     H2     sing N N 280 
HIS CA    C      sing N N 281 
HIS CA    CB     sing N N 282 
HIS CA    HA     sing N N 283 
HIS C     O      doub N N 284 
HIS C     OXT    sing N N 285 
HIS CB    CG     sing N N 286 
HIS CB    HB2    sing N N 287 
HIS CB    HB3    sing N N 288 
HIS CG    ND1    sing Y N 289 
HIS CG    CD2    doub Y N 290 
HIS ND1   CE1    doub Y N 291 
HIS ND1   HD1    sing N N 292 
HIS CD2   NE2    sing Y N 293 
HIS CD2   HD2    sing N N 294 
HIS CE1   NE2    sing Y N 295 
HIS CE1   HE1    sing N N 296 
HIS NE2   HE2    sing N N 297 
HIS OXT   HXT    sing N N 298 
ILE N     CA     sing N N 299 
ILE N     H      sing N N 300 
ILE N     H2     sing N N 301 
ILE CA    C      sing N N 302 
ILE CA    CB     sing N N 303 
ILE CA    HA     sing N N 304 
ILE C     O      doub N N 305 
ILE C     OXT    sing N N 306 
ILE CB    CG1    sing N N 307 
ILE CB    CG2    sing N N 308 
ILE CB    HB     sing N N 309 
ILE CG1   CD1    sing N N 310 
ILE CG1   HG12   sing N N 311 
ILE CG1   HG13   sing N N 312 
ILE CG2   HG21   sing N N 313 
ILE CG2   HG22   sing N N 314 
ILE CG2   HG23   sing N N 315 
ILE CD1   HD11   sing N N 316 
ILE CD1   HD12   sing N N 317 
ILE CD1   HD13   sing N N 318 
ILE OXT   HXT    sing N N 319 
LEU N     CA     sing N N 320 
LEU N     H      sing N N 321 
LEU N     H2     sing N N 322 
LEU CA    C      sing N N 323 
LEU CA    CB     sing N N 324 
LEU CA    HA     sing N N 325 
LEU C     O      doub N N 326 
LEU C     OXT    sing N N 327 
LEU CB    CG     sing N N 328 
LEU CB    HB2    sing N N 329 
LEU CB    HB3    sing N N 330 
LEU CG    CD1    sing N N 331 
LEU CG    CD2    sing N N 332 
LEU CG    HG     sing N N 333 
LEU CD1   HD11   sing N N 334 
LEU CD1   HD12   sing N N 335 
LEU CD1   HD13   sing N N 336 
LEU CD2   HD21   sing N N 337 
LEU CD2   HD22   sing N N 338 
LEU CD2   HD23   sing N N 339 
LEU OXT   HXT    sing N N 340 
LYS N     CA     sing N N 341 
LYS N     H      sing N N 342 
LYS N     H2     sing N N 343 
LYS CA    C      sing N N 344 
LYS CA    CB     sing N N 345 
LYS CA    HA     sing N N 346 
LYS C     O      doub N N 347 
LYS C     OXT    sing N N 348 
LYS CB    CG     sing N N 349 
LYS CB    HB2    sing N N 350 
LYS CB    HB3    sing N N 351 
LYS CG    CD     sing N N 352 
LYS CG    HG2    sing N N 353 
LYS CG    HG3    sing N N 354 
LYS CD    CE     sing N N 355 
LYS CD    HD2    sing N N 356 
LYS CD    HD3    sing N N 357 
LYS CE    NZ     sing N N 358 
LYS CE    HE2    sing N N 359 
LYS CE    HE3    sing N N 360 
LYS NZ    HZ1    sing N N 361 
LYS NZ    HZ2    sing N N 362 
LYS NZ    HZ3    sing N N 363 
LYS OXT   HXT    sing N N 364 
MET N     CA     sing N N 365 
MET N     H      sing N N 366 
MET N     H2     sing N N 367 
MET CA    C      sing N N 368 
MET CA    CB     sing N N 369 
MET CA    HA     sing N N 370 
MET C     O      doub N N 371 
MET C     OXT    sing N N 372 
MET CB    CG     sing N N 373 
MET CB    HB2    sing N N 374 
MET CB    HB3    sing N N 375 
MET CG    SD     sing N N 376 
MET CG    HG2    sing N N 377 
MET CG    HG3    sing N N 378 
MET SD    CE     sing N N 379 
MET CE    HE1    sing N N 380 
MET CE    HE2    sing N N 381 
MET CE    HE3    sing N N 382 
MET OXT   HXT    sing N N 383 
PHE N     CA     sing N N 384 
PHE N     H      sing N N 385 
PHE N     H2     sing N N 386 
PHE CA    C      sing N N 387 
PHE CA    CB     sing N N 388 
PHE CA    HA     sing N N 389 
PHE C     O      doub N N 390 
PHE C     OXT    sing N N 391 
PHE CB    CG     sing N N 392 
PHE CB    HB2    sing N N 393 
PHE CB    HB3    sing N N 394 
PHE CG    CD1    doub Y N 395 
PHE CG    CD2    sing Y N 396 
PHE CD1   CE1    sing Y N 397 
PHE CD1   HD1    sing N N 398 
PHE CD2   CE2    doub Y N 399 
PHE CD2   HD2    sing N N 400 
PHE CE1   CZ     doub Y N 401 
PHE CE1   HE1    sing N N 402 
PHE CE2   CZ     sing Y N 403 
PHE CE2   HE2    sing N N 404 
PHE CZ    HZ     sing N N 405 
PHE OXT   HXT    sing N N 406 
PRO N     CA     sing N N 407 
PRO N     CD     sing N N 408 
PRO N     H      sing N N 409 
PRO CA    C      sing N N 410 
PRO CA    CB     sing N N 411 
PRO CA    HA     sing N N 412 
PRO C     O      doub N N 413 
PRO C     OXT    sing N N 414 
PRO CB    CG     sing N N 415 
PRO CB    HB2    sing N N 416 
PRO CB    HB3    sing N N 417 
PRO CG    CD     sing N N 418 
PRO CG    HG2    sing N N 419 
PRO CG    HG3    sing N N 420 
PRO CD    HD2    sing N N 421 
PRO CD    HD3    sing N N 422 
PRO OXT   HXT    sing N N 423 
SER N     CA     sing N N 424 
SER N     H      sing N N 425 
SER N     H2     sing N N 426 
SER CA    C      sing N N 427 
SER CA    CB     sing N N 428 
SER CA    HA     sing N N 429 
SER C     O      doub N N 430 
SER C     OXT    sing N N 431 
SER CB    OG     sing N N 432 
SER CB    HB2    sing N N 433 
SER CB    HB3    sing N N 434 
SER OG    HG     sing N N 435 
SER OXT   HXT    sing N N 436 
THR N     CA     sing N N 437 
THR N     H      sing N N 438 
THR N     H2     sing N N 439 
THR CA    C      sing N N 440 
THR CA    CB     sing N N 441 
THR CA    HA     sing N N 442 
THR C     O      doub N N 443 
THR C     OXT    sing N N 444 
THR CB    OG1    sing N N 445 
THR CB    CG2    sing N N 446 
THR CB    HB     sing N N 447 
THR OG1   HG1    sing N N 448 
THR CG2   HG21   sing N N 449 
THR CG2   HG22   sing N N 450 
THR CG2   HG23   sing N N 451 
THR OXT   HXT    sing N N 452 
TRP N     CA     sing N N 453 
TRP N     H      sing N N 454 
TRP N     H2     sing N N 455 
TRP CA    C      sing N N 456 
TRP CA    CB     sing N N 457 
TRP CA    HA     sing N N 458 
TRP C     O      doub N N 459 
TRP C     OXT    sing N N 460 
TRP CB    CG     sing N N 461 
TRP CB    HB2    sing N N 462 
TRP CB    HB3    sing N N 463 
TRP CG    CD1    doub Y N 464 
TRP CG    CD2    sing Y N 465 
TRP CD1   NE1    sing Y N 466 
TRP CD1   HD1    sing N N 467 
TRP CD2   CE2    doub Y N 468 
TRP CD2   CE3    sing Y N 469 
TRP NE1   CE2    sing Y N 470 
TRP NE1   HE1    sing N N 471 
TRP CE2   CZ2    sing Y N 472 
TRP CE3   CZ3    doub Y N 473 
TRP CE3   HE3    sing N N 474 
TRP CZ2   CH2    doub Y N 475 
TRP CZ2   HZ2    sing N N 476 
TRP CZ3   CH2    sing Y N 477 
TRP CZ3   HZ3    sing N N 478 
TRP CH2   HH2    sing N N 479 
TRP OXT   HXT    sing N N 480 
TYR N     CA     sing N N 481 
TYR N     H      sing N N 482 
TYR N     H2     sing N N 483 
TYR CA    C      sing N N 484 
TYR CA    CB     sing N N 485 
TYR CA    HA     sing N N 486 
TYR C     O      doub N N 487 
TYR C     OXT    sing N N 488 
TYR CB    CG     sing N N 489 
TYR CB    HB2    sing N N 490 
TYR CB    HB3    sing N N 491 
TYR CG    CD1    doub Y N 492 
TYR CG    CD2    sing Y N 493 
TYR CD1   CE1    sing Y N 494 
TYR CD1   HD1    sing N N 495 
TYR CD2   CE2    doub Y N 496 
TYR CD2   HD2    sing N N 497 
TYR CE1   CZ     doub Y N 498 
TYR CE1   HE1    sing N N 499 
TYR CE2   CZ     sing Y N 500 
TYR CE2   HE2    sing N N 501 
TYR CZ    OH     sing N N 502 
TYR OH    HH     sing N N 503 
TYR OXT   HXT    sing N N 504 
VAL N     CA     sing N N 505 
VAL N     H      sing N N 506 
VAL N     H2     sing N N 507 
VAL CA    C      sing N N 508 
VAL CA    CB     sing N N 509 
VAL CA    HA     sing N N 510 
VAL C     O      doub N N 511 
VAL C     OXT    sing N N 512 
VAL CB    CG1    sing N N 513 
VAL CB    CG2    sing N N 514 
VAL CB    HB     sing N N 515 
VAL CG1   HG11   sing N N 516 
VAL CG1   HG12   sing N N 517 
VAL CG1   HG13   sing N N 518 
VAL CG2   HG21   sing N N 519 
VAL CG2   HG22   sing N N 520 
VAL CG2   HG23   sing N N 521 
VAL OXT   HXT    sing N N 522 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-03-20 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           8YQZ 
_em_admin.last_update        2024-11-06 
_em_admin.map_release_date   2024-11-06 
_em_admin.title              'African swine fever virus RNA Polymerase--DNA complex' 
# 
_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_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   1 
_em_entity_assembly_naturalsource.ncbi_tax_id          10497 
_em_entity_assembly_naturalsource.organism             'African swine fever virus' 
_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_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         1.25 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'FEI FALCON IV (4k 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 ? ? 
MASKING                         ? 3  ? ? ? ? ? 
'CTF CORRECTION'                ? 4  1 ? ? ? ? 
'LAYERLINE INDEXING'            ? 5  ? ? ? ? ? 
'DIFFRACTION INDEXING'          ? 6  ? ? ? ? ? 
'MODEL FITTING'                 ? 7  ? ? ? ? ? 
'MODEL REFINEMENT'              ? 8  ? ? ? ? ? 
OTHER                           ? 9  ? ? ? ? ? 
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? ? ? 
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? ? ? 
CLASSIFICATION                  ? 12 1 ? ? ? ? 
RECONSTRUCTION                  ? 13 1 ? ? ? ? 
'VOLUME SELECTION'              ? 14 1 1 1 ? ? 
'SERIES ALIGNMENT'              ? 15 1 1 1 ? ? 
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ? ? 
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ? ? 
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ? ? 
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 1 ? ? 
# 
_em_specimen.concentration           ? 
_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 
# 
_ndb_struct_conf_na.entry_id   8YQZ 
_ndb_struct_conf_na.feature    'b-form double helix' 
# 
loop_
_ndb_struct_na_base_pair.model_number 
_ndb_struct_na_base_pair.i_label_asym_id 
_ndb_struct_na_base_pair.i_label_comp_id 
_ndb_struct_na_base_pair.i_label_seq_id 
_ndb_struct_na_base_pair.i_symmetry 
_ndb_struct_na_base_pair.j_label_asym_id 
_ndb_struct_na_base_pair.j_label_comp_id 
_ndb_struct_na_base_pair.j_label_seq_id 
_ndb_struct_na_base_pair.j_symmetry 
_ndb_struct_na_base_pair.shear 
_ndb_struct_na_base_pair.stretch 
_ndb_struct_na_base_pair.stagger 
_ndb_struct_na_base_pair.buckle 
_ndb_struct_na_base_pair.propeller 
_ndb_struct_na_base_pair.opening 
_ndb_struct_na_base_pair.pair_number 
_ndb_struct_na_base_pair.pair_name 
_ndb_struct_na_base_pair.i_auth_asym_id 
_ndb_struct_na_base_pair.i_auth_seq_id 
_ndb_struct_na_base_pair.i_PDB_ins_code 
_ndb_struct_na_base_pair.j_auth_asym_id 
_ndb_struct_na_base_pair.j_auth_seq_id 
_ndb_struct_na_base_pair.j_PDB_ins_code 
_ndb_struct_na_base_pair.hbond_type_28 
_ndb_struct_na_base_pair.hbond_type_12 
1 I DG 1 1_555 J DC 5 1_555 2.272  0.429  -0.870 -20.512 -8.854  5.063   1 X_DG20:DC-20_Y X 20 ? Y -20 ? ?  1 
1 I DC 2 1_555 J DG 4 1_555 -0.001 -0.730 -0.039 5.817   -2.188  -3.279  2 X_DC21:DG-21_Y X 21 ? Y -21 ? 22 1 
1 I DC 3 1_555 J DG 3 1_555 0.913  -0.653 -0.267 12.848  -4.700  1.819   3 X_DC22:DG-22_Y X 22 ? Y -22 ? 19 1 
1 I DG 4 1_555 J DC 2 1_555 -0.015 -1.064 -1.131 9.232   9.751   -4.505  4 X_DG23:DC-23_Y X 23 ? Y -23 ? 19 1 
1 I DA 5 1_555 J DT 1 1_555 -0.764 -0.089 -0.288 4.331   -27.122 -10.077 5 X_DA24:DT-24_Y X 24 ? Y -24 ? 20 1 
# 
loop_
_ndb_struct_na_base_pair_step.model_number 
_ndb_struct_na_base_pair_step.i_label_asym_id_1 
_ndb_struct_na_base_pair_step.i_label_comp_id_1 
_ndb_struct_na_base_pair_step.i_label_seq_id_1 
_ndb_struct_na_base_pair_step.i_symmetry_1 
_ndb_struct_na_base_pair_step.j_label_asym_id_1 
_ndb_struct_na_base_pair_step.j_label_comp_id_1 
_ndb_struct_na_base_pair_step.j_label_seq_id_1 
_ndb_struct_na_base_pair_step.j_symmetry_1 
_ndb_struct_na_base_pair_step.i_label_asym_id_2 
_ndb_struct_na_base_pair_step.i_label_comp_id_2 
_ndb_struct_na_base_pair_step.i_label_seq_id_2 
_ndb_struct_na_base_pair_step.i_symmetry_2 
_ndb_struct_na_base_pair_step.j_label_asym_id_2 
_ndb_struct_na_base_pair_step.j_label_comp_id_2 
_ndb_struct_na_base_pair_step.j_label_seq_id_2 
_ndb_struct_na_base_pair_step.j_symmetry_2 
_ndb_struct_na_base_pair_step.shift 
_ndb_struct_na_base_pair_step.slide 
_ndb_struct_na_base_pair_step.rise 
_ndb_struct_na_base_pair_step.tilt 
_ndb_struct_na_base_pair_step.roll 
_ndb_struct_na_base_pair_step.twist 
_ndb_struct_na_base_pair_step.x_displacement 
_ndb_struct_na_base_pair_step.y_displacement 
_ndb_struct_na_base_pair_step.helical_rise 
_ndb_struct_na_base_pair_step.inclination 
_ndb_struct_na_base_pair_step.tip 
_ndb_struct_na_base_pair_step.helical_twist 
_ndb_struct_na_base_pair_step.step_number 
_ndb_struct_na_base_pair_step.step_name 
_ndb_struct_na_base_pair_step.i_auth_asym_id_1 
_ndb_struct_na_base_pair_step.i_auth_seq_id_1 
_ndb_struct_na_base_pair_step.i_PDB_ins_code_1 
_ndb_struct_na_base_pair_step.j_auth_asym_id_1 
_ndb_struct_na_base_pair_step.j_auth_seq_id_1 
_ndb_struct_na_base_pair_step.j_PDB_ins_code_1 
_ndb_struct_na_base_pair_step.i_auth_asym_id_2 
_ndb_struct_na_base_pair_step.i_auth_seq_id_2 
_ndb_struct_na_base_pair_step.i_PDB_ins_code_2 
_ndb_struct_na_base_pair_step.j_auth_asym_id_2 
_ndb_struct_na_base_pair_step.j_auth_seq_id_2 
_ndb_struct_na_base_pair_step.j_PDB_ins_code_2 
1 I DG 1 1_555 J DC 5 1_555 I DC 2 1_555 J DG 4 1_555 -0.301 -0.553 2.686 -6.930 7.502  25.898 -2.612 -0.724 2.432 15.970  14.753  
27.807 1 XX_DG20DC21:DG-21DC-20_YY X 20 ? Y -20 ? X 21 ? Y -21 ? 
1 I DC 2 1_555 J DG 4 1_555 I DC 3 1_555 J DG 3 1_555 -0.097 -0.832 3.277 -1.197 -7.546 40.319 -0.344 0.005  3.374 -10.830 1.718   
41.007 2 XX_DC21DC22:DG-22DG-21_YY X 21 ? Y -21 ? X 22 ? Y -22 ? 
1 I DC 3 1_555 J DG 3 1_555 I DG 4 1_555 J DC 2 1_555 -0.108 -0.149 3.469 6.319  10.793 28.758 -2.422 1.456  3.121 20.547  -12.030 
31.307 3 XX_DC22DG23:DC-23DG-22_YY X 22 ? Y -22 ? X 23 ? Y -23 ? 
1 I DG 4 1_555 J DC 2 1_555 I DA 5 1_555 J DT 1 1_555 -0.411 0.480  3.544 -3.571 -3.436 37.684 1.211  0.139  3.512 -5.291  5.499   
37.997 4 XX_DG23DA24:DT-24DC-23_YY X 23 ? Y -23 ? X 24 ? Y -24 ? 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    8YQZ 
_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  
ZN 
# 
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     . GLU A 1  2    ? 159.555 97.395  111.321 1.00 34.09  ? 2    GLU A N     1 
ATOM   2     C  CA    . GLU A 1  2    ? 159.722 96.154  112.063 1.00 35.48  ? 2    GLU A CA    1 
ATOM   3     C  C     . GLU A 1  2    ? 158.779 96.123  113.260 1.00 36.04  ? 2    GLU A C     1 
ATOM   4     O  O     . GLU A 1  2    ? 158.533 95.068  113.833 1.00 39.35  ? 2    GLU A O     1 
ATOM   5     C  CB    . GLU A 1  2    ? 161.183 95.988  112.506 1.00 33.60  ? 2    GLU A CB    1 
ATOM   6     C  CG    . GLU A 1  2    ? 161.563 94.578  112.931 1.00 35.01  ? 2    GLU A CG    1 
ATOM   7     C  CD    . GLU A 1  2    ? 163.056 94.414  113.152 1.00 41.40  ? 2    GLU A CD    1 
ATOM   8     O  OE1   . GLU A 1  2    ? 163.797 95.386  112.916 1.00 40.41  ? 2    GLU A OE1   1 
ATOM   9     O  OE2   . GLU A 1  2    ? 163.492 93.316  113.564 1.00 40.88  ? 2    GLU A OE2   1 
ATOM   10    N  N     . ALA A 1  3    ? 158.249 97.285  113.632 1.00 23.04  ? 3    ALA A N     1 
ATOM   11    C  CA    . ALA A 1  3    ? 157.222 97.381  114.664 1.00 16.91  ? 3    ALA A CA    1 
ATOM   12    C  C     . ALA A 1  3    ? 155.869 97.554  113.988 1.00 15.45  ? 3    ALA A C     1 
ATOM   13    O  O     . ALA A 1  3    ? 155.631 98.559  113.319 1.00 20.02  ? 3    ALA A O     1 
ATOM   14    C  CB    . ALA A 1  3    ? 157.517 98.540  115.609 1.00 12.73  ? 3    ALA A CB    1 
ATOM   15    N  N     . GLY A 1  4    ? 154.986 96.578  114.162 1.00 14.41  ? 4    GLY A N     1 
ATOM   16    C  CA    . GLY A 1  4    ? 153.697 96.619  113.509 1.00 8.19   ? 4    GLY A CA    1 
ATOM   17    C  C     . GLY A 1  4    ? 152.702 97.528  114.199 1.00 10.01  ? 4    GLY A C     1 
ATOM   18    O  O     . GLY A 1  4    ? 152.835 97.877  115.363 1.00 16.96  ? 4    GLY A O     1 
ATOM   19    N  N     . TYR A 1  5    ? 151.673 97.899  113.446 1.00 8.45   ? 5    TYR A N     1 
ATOM   20    C  CA    . TYR A 1  5    ? 150.646 98.814  113.925 1.00 5.90   ? 5    TYR A CA    1 
ATOM   21    C  C     . TYR A 1  5    ? 149.794 98.155  115.001 1.00 6.87   ? 5    TYR A C     1 
ATOM   22    O  O     . TYR A 1  5    ? 149.361 97.011  114.848 1.00 12.77  ? 5    TYR A O     1 
ATOM   23    C  CB    . TYR A 1  5    ? 149.778 99.250  112.749 1.00 2.38   ? 5    TYR A CB    1 
ATOM   24    C  CG    . TYR A 1  5    ? 148.559 100.057 113.100 1.00 6.06   ? 5    TYR A CG    1 
ATOM   25    C  CD1   . TYR A 1  5    ? 148.614 101.430 113.189 1.00 5.76   ? 5    TYR A CD1   1 
ATOM   26    C  CD2   . TYR A 1  5    ? 147.348 99.442  113.338 1.00 5.29   ? 5    TYR A CD2   1 
ATOM   27    C  CE1   . TYR A 1  5    ? 147.499 102.157 113.504 1.00 4.15   ? 5    TYR A CE1   1 
ATOM   28    C  CE2   . TYR A 1  5    ? 146.244 100.158 113.656 1.00 2.13   ? 5    TYR A CE2   1 
ATOM   29    C  CZ    . TYR A 1  5    ? 146.319 101.512 113.731 1.00 4.85   ? 5    TYR A CZ    1 
ATOM   30    O  OH    . TYR A 1  5    ? 145.198 102.222 114.048 1.00 4.78   ? 5    TYR A OH    1 
ATOM   31    N  N     . ALA A 1  6    ? 149.527 98.886  116.080 1.00 3.12   ? 6    ALA A N     1 
ATOM   32    C  CA    . ALA A 1  6    ? 148.761 98.353  117.194 1.00 1.27   ? 6    ALA A CA    1 
ATOM   33    C  C     . ALA A 1  6    ? 147.877 99.441  117.790 1.00 7.72   ? 6    ALA A C     1 
ATOM   34    O  O     . ALA A 1  6    ? 148.074 100.631 117.551 1.00 9.45   ? 6    ALA A O     1 
ATOM   35    C  CB    . ALA A 1  6    ? 149.682 97.763  118.263 1.00 2.14   ? 6    ALA A CB    1 
ATOM   36    N  N     . GLU A 1  7    ? 146.883 99.012  118.563 1.00 7.56   ? 7    GLU A N     1 
ATOM   37    C  CA    . GLU A 1  7    ? 146.020 99.912  119.316 1.00 14.51  ? 7    GLU A CA    1 
ATOM   38    C  C     . GLU A 1  7    ? 145.910 99.429  120.750 1.00 3.64   ? 7    GLU A C     1 
ATOM   39    O  O     . GLU A 1  7    ? 145.956 98.228  121.007 1.00 12.17  ? 7    GLU A O     1 
ATOM   40    C  CB    . GLU A 1  7    ? 144.623 100.003 118.707 1.00 7.98   ? 7    GLU A CB    1 
ATOM   41    C  CG    . GLU A 1  7    ? 144.516 100.910 117.510 1.00 6.38   ? 7    GLU A CG    1 
ATOM   42    C  CD    . GLU A 1  7    ? 143.522 100.406 116.494 1.00 13.71  ? 7    GLU A CD    1 
ATOM   43    O  OE1   . GLU A 1  7    ? 143.241 99.193  116.493 1.00 19.12  ? 7    GLU A OE1   1 
ATOM   44    O  OE2   . GLU A 1  7    ? 143.024 101.215 115.689 1.00 11.17  ? 7    GLU A OE2   1 
ATOM   45    N  N     . ILE A 1  8    ? 145.757 100.362 121.677 1.00 9.11   ? 8    ILE A N     1 
ATOM   46    C  CA    . ILE A 1  8    ? 145.605 100.025 123.087 1.00 10.60  ? 8    ILE A CA    1 
ATOM   47    C  C     . ILE A 1  8    ? 144.149 99.683  123.364 1.00 4.82   ? 8    ILE A C     1 
ATOM   48    O  O     . ILE A 1  8    ? 143.250 100.488 123.104 1.00 9.77   ? 8    ILE A O     1 
ATOM   49    C  CB    . ILE A 1  8    ? 146.079 101.183 123.975 1.00 0.28   ? 8    ILE A CB    1 
ATOM   50    C  CG1   . ILE A 1  8    ? 147.567 101.437 123.775 1.00 7.22   ? 8    ILE A CG1   1 
ATOM   51    C  CG2   . ILE A 1  8    ? 145.799 100.895 125.421 1.00 5.55   ? 8    ILE A CG2   1 
ATOM   52    C  CD1   . ILE A 1  8    ? 148.040 102.705 124.400 1.00 5.40   ? 8    ILE A CD1   1 
ATOM   53    N  N     . ALA A 1  9    ? 143.910 98.486  123.890 1.00 5.06   ? 9    ALA A N     1 
ATOM   54    C  CA    . ALA A 1  9    ? 142.563 98.035  124.205 1.00 7.02   ? 9    ALA A CA    1 
ATOM   55    C  C     . ALA A 1  9    ? 142.183 98.230  125.663 1.00 2.35   ? 9    ALA A C     1 
ATOM   56    O  O     . ALA A 1  9    ? 141.009 98.461  125.954 1.00 11.41  ? 9    ALA A O     1 
ATOM   57    C  CB    . ALA A 1  9    ? 142.398 96.561  123.838 1.00 3.63   ? 9    ALA A CB    1 
ATOM   58    N  N     . ALA A 1  10   ? 143.134 98.159  126.587 1.00 1.86   ? 10   ALA A N     1 
ATOM   59    C  CA    . ALA A 1  10   ? 142.830 98.378  127.989 1.00 3.10   ? 10   ALA A CA    1 
ATOM   60    C  C     . ALA A 1  10   ? 144.043 98.979  128.678 1.00 6.71   ? 10   ALA A C     1 
ATOM   61    O  O     . ALA A 1  10   ? 145.148 98.984  128.140 1.00 11.63  ? 10   ALA A O     1 
ATOM   62    C  CB    . ALA A 1  10   ? 142.399 97.086  128.685 1.00 2.67   ? 10   ALA A CB    1 
ATOM   63    N  N     . VAL A 1  11   ? 143.814 99.510  129.869 1.00 2.54   ? 11   VAL A N     1 
ATOM   64    C  CA    . VAL A 1  11   ? 144.865 100.025 130.734 1.00 6.88   ? 11   VAL A CA    1 
ATOM   65    C  C     . VAL A 1  11   ? 144.652 99.436  132.119 1.00 12.07  ? 11   VAL A C     1 
ATOM   66    O  O     . VAL A 1  11   ? 143.526 99.413  132.616 1.00 16.65  ? 11   VAL A O     1 
ATOM   67    C  CB    . VAL A 1  11   ? 144.866 101.565 130.787 1.00 7.62   ? 11   VAL A CB    1 
ATOM   68    C  CG1   . VAL A 1  11   ? 145.818 102.053 131.829 1.00 11.04  ? 11   VAL A CG1   1 
ATOM   69    C  CG2   . VAL A 1  11   ? 145.271 102.128 129.460 1.00 8.76   ? 11   VAL A CG2   1 
ATOM   70    N  N     . GLN A 1  12   ? 145.721 98.937  132.728 1.00 11.71  ? 12   GLN A N     1 
ATOM   71    C  CA    . GLN A 1  12   ? 145.664 98.387  134.074 1.00 8.38   ? 12   GLN A CA    1 
ATOM   72    C  C     . GLN A 1  12   ? 146.448 99.274  135.025 1.00 10.80  ? 12   GLN A C     1 
ATOM   73    O  O     . GLN A 1  12   ? 147.558 99.698  134.707 1.00 13.91  ? 12   GLN A O     1 
ATOM   74    C  CB    . GLN A 1  12   ? 146.219 96.971  134.103 1.00 9.84   ? 12   GLN A CB    1 
ATOM   75    C  CG    . GLN A 1  12   ? 145.604 96.073  133.071 1.00 17.68  ? 12   GLN A CG    1 
ATOM   76    C  CD    . GLN A 1  12   ? 145.889 94.627  133.347 1.00 22.51  ? 12   GLN A CD    1 
ATOM   77    O  OE1   . GLN A 1  12   ? 145.604 93.755  132.531 1.00 22.85  ? 12   GLN A OE1   1 
ATOM   78    N  NE2   . GLN A 1  12   ? 146.458 94.358  134.513 1.00 23.51  ? 12   GLN A NE2   1 
ATOM   79    N  N     . PHE A 1  13   ? 145.865 99.564  136.179 1.00 14.35  ? 13   PHE A N     1 
ATOM   80    C  CA    . PHE A 1  13   ? 146.497 100.378 137.205 1.00 13.03  ? 13   PHE A CA    1 
ATOM   81    C  C     . PHE A 1  13   ? 146.954 99.490  138.352 1.00 19.95  ? 13   PHE A C     1 
ATOM   82    O  O     . PHE A 1  13   ? 146.259 98.546  138.724 1.00 23.72  ? 13   PHE A O     1 
ATOM   83    C  CB    . PHE A 1  13   ? 145.540 101.449 137.721 1.00 12.29  ? 13   PHE A CB    1 
ATOM   84    C  CG    . PHE A 1  13   ? 145.099 102.417 136.680 1.00 16.21  ? 13   PHE A CG    1 
ATOM   85    C  CD1   . PHE A 1  13   ? 144.064 102.114 135.822 1.00 15.70  ? 13   PHE A CD1   1 
ATOM   86    C  CD2   . PHE A 1  13   ? 145.718 103.640 136.559 1.00 15.56  ? 13   PHE A CD2   1 
ATOM   87    C  CE1   . PHE A 1  13   ? 143.666 103.009 134.866 1.00 12.00  ? 13   PHE A CE1   1 
ATOM   88    C  CE2   . PHE A 1  13   ? 145.317 104.534 135.605 1.00 11.41  ? 13   PHE A CE2   1 
ATOM   89    C  CZ    . PHE A 1  13   ? 144.290 104.217 134.762 1.00 11.92  ? 13   PHE A CZ    1 
ATOM   90    N  N     . ASN A 1  14   ? 148.126 99.783  138.905 1.00 18.87  ? 14   ASN A N     1 
ATOM   91    C  CA    . ASN A 1  14   ? 148.718 98.935  139.928 1.00 17.60  ? 14   ASN A CA    1 
ATOM   92    C  C     . ASN A 1  14   ? 149.613 99.780  140.822 1.00 23.17  ? 14   ASN A C     1 
ATOM   93    O  O     . ASN A 1  14   ? 149.882 100.946 140.538 1.00 24.71  ? 14   ASN A O     1 
ATOM   94    C  CB    . ASN A 1  14   ? 149.504 97.785  139.300 1.00 20.49  ? 14   ASN A CB    1 
ATOM   95    C  CG    . ASN A 1  14   ? 148.666 96.551  139.102 1.00 24.54  ? 14   ASN A CG    1 
ATOM   96    O  OD1   . ASN A 1  14   ? 148.110 96.012  140.050 1.00 27.78  ? 14   ASN A OD1   1 
ATOM   97    N  ND2   . ASN A 1  14   ? 148.570 96.094  137.869 1.00 22.27  ? 14   ASN A ND2   1 
ATOM   98    N  N     . ILE A 1  15   ? 150.069 99.181  141.917 1.00 30.12  ? 15   ILE A N     1 
ATOM   99    C  CA    . ILE A 1  15   ? 151.022 99.808  142.825 1.00 25.64  ? 15   ILE A CA    1 
ATOM   100   C  C     . ILE A 1  15   ? 152.410 99.292  142.486 1.00 25.06  ? 15   ILE A C     1 
ATOM   101   O  O     . ILE A 1  15   ? 152.616 98.081  142.360 1.00 28.05  ? 15   ILE A O     1 
ATOM   102   C  CB    . ILE A 1  15   ? 150.671 99.528  144.296 1.00 26.18  ? 15   ILE A CB    1 
ATOM   103   C  CG1   . ILE A 1  15   ? 149.379 100.240 144.678 1.00 27.57  ? 15   ILE A CG1   1 
ATOM   104   C  CG2   . ILE A 1  15   ? 151.780 100.001 145.213 1.00 28.67  ? 15   ILE A CG2   1 
ATOM   105   C  CD1   . ILE A 1  15   ? 148.870 99.870  146.026 1.00 26.71  ? 15   ILE A CD1   1 
ATOM   106   N  N     . ALA A 1  16   ? 153.356 100.208 142.323 1.00 22.28  ? 16   ALA A N     1 
ATOM   107   C  CA    . ALA A 1  16   ? 154.717 99.858  141.949 1.00 26.70  ? 16   ALA A CA    1 
ATOM   108   C  C     . ALA A 1  16   ? 155.549 99.547  143.186 1.00 30.76  ? 16   ALA A C     1 
ATOM   109   O  O     . ALA A 1  16   ? 155.549 100.312 144.155 1.00 32.66  ? 16   ALA A O     1 
ATOM   110   C  CB    . ALA A 1  16   ? 155.362 100.991 141.155 1.00 29.63  ? 16   ALA A CB    1 
ATOM   111   N  N     . GLY A 1  17   ? 156.253 98.425  143.150 1.00 33.23  ? 17   GLY A N     1 
ATOM   112   C  CA    . GLY A 1  17   ? 157.153 98.035  144.204 1.00 34.15  ? 17   GLY A CA    1 
ATOM   113   C  C     . GLY A 1  17   ? 158.590 98.394  143.893 1.00 36.25  ? 17   GLY A C     1 
ATOM   114   O  O     . GLY A 1  17   ? 158.884 99.205  143.010 1.00 38.84  ? 17   GLY A O     1 
ATOM   115   N  N     . ASP A 1  18   ? 159.505 97.781  144.642 1.00 38.91  ? 18   ASP A N     1 
ATOM   116   C  CA    . ASP A 1  18   ? 160.924 98.013  144.403 1.00 35.29  ? 18   ASP A CA    1 
ATOM   117   C  C     . ASP A 1  18   ? 161.401 97.279  143.161 1.00 35.98  ? 18   ASP A C     1 
ATOM   118   O  O     . ASP A 1  18   ? 162.208 97.809  142.391 1.00 37.89  ? 18   ASP A O     1 
ATOM   119   C  CB    . ASP A 1  18   ? 161.731 97.575  145.618 1.00 37.51  ? 18   ASP A CB    1 
ATOM   120   C  CG    . ASP A 1  18   ? 161.934 98.689  146.605 1.00 41.73  ? 18   ASP A CG    1 
ATOM   121   O  OD1   . ASP A 1  18   ? 162.041 98.397  147.811 1.00 43.12  ? 18   ASP A OD1   1 
ATOM   122   O  OD2   . ASP A 1  18   ? 161.971 99.859  146.181 1.00 41.09  ? 18   ASP A OD2   1 
ATOM   123   N  N     . ASN A 1  19   ? 160.919 96.054  142.956 1.00 35.12  ? 19   ASN A N     1 
ATOM   124   C  CA    . ASN A 1  19   ? 161.388 95.245  141.838 1.00 33.71  ? 19   ASN A CA    1 
ATOM   125   C  C     . ASN A 1  19   ? 160.958 95.836  140.506 1.00 35.56  ? 19   ASN A C     1 
ATOM   126   O  O     . ASN A 1  19   ? 161.699 95.755  139.523 1.00 39.83  ? 19   ASN A O     1 
ATOM   127   C  CB    . ASN A 1  19   ? 160.880 93.817  141.982 1.00 35.04  ? 19   ASN A CB    1 
ATOM   128   C  CG    . ASN A 1  19   ? 160.890 93.350  143.414 1.00 39.69  ? 19   ASN A CG    1 
ATOM   129   O  OD1   . ASN A 1  19   ? 160.392 94.040  144.301 1.00 38.33  ? 19   ASN A OD1   1 
ATOM   130   N  ND2   . ASN A 1  19   ? 161.453 92.174  143.652 1.00 40.75  ? 19   ASN A ND2   1 
ATOM   131   N  N     . ASP A 1  20   ? 159.765 96.432  140.453 1.00 37.04  ? 20   ASP A N     1 
ATOM   132   C  CA    . ASP A 1  20   ? 159.336 97.118  139.239 1.00 31.90  ? 20   ASP A CA    1 
ATOM   133   C  C     . ASP A 1  20   ? 160.283 98.253  138.890 1.00 35.88  ? 20   ASP A C     1 
ATOM   134   O  O     . ASP A 1  20   ? 160.709 98.384  137.738 1.00 35.83  ? 20   ASP A O     1 
ATOM   135   C  CB    . ASP A 1  20   ? 157.922 97.662  139.411 1.00 32.93  ? 20   ASP A CB    1 
ATOM   136   C  CG    . ASP A 1  20   ? 156.862 96.621  139.156 1.00 39.41  ? 20   ASP A CG    1 
ATOM   137   O  OD1   . ASP A 1  20   ? 156.819 96.080  138.036 1.00 42.34  ? 20   ASP A OD1   1 
ATOM   138   O  OD2   . ASP A 1  20   ? 156.051 96.368  140.070 1.00 40.25  ? 20   ASP A OD2   1 
ATOM   139   N  N     . HIS A 1  21   ? 160.624 99.081  139.877 1.00 32.61  ? 21   HIS A N     1 
ATOM   140   C  CA    . HIS A 1  21   ? 161.541 100.188 139.649 1.00 28.39  ? 21   HIS A CA    1 
ATOM   141   C  C     . HIS A 1  21   ? 162.904 99.688  139.212 1.00 30.02  ? 21   HIS A C     1 
ATOM   142   O  O     . HIS A 1  21   ? 163.528 100.262 138.316 1.00 35.12  ? 21   HIS A O     1 
ATOM   143   C  CB    . HIS A 1  21   ? 161.666 101.017 140.919 1.00 28.59  ? 21   HIS A CB    1 
ATOM   144   C  CG    . HIS A 1  21   ? 160.419 101.753 141.277 1.00 31.73  ? 21   HIS A CG    1 
ATOM   145   N  ND1   . HIS A 1  21   ? 160.167 102.210 142.550 1.00 34.29  ? 21   HIS A ND1   1 
ATOM   146   C  CD2   . HIS A 1  21   ? 159.357 102.123 140.527 1.00 32.58  ? 21   HIS A CD2   1 
ATOM   147   C  CE1   . HIS A 1  21   ? 158.999 102.822 142.571 1.00 31.84  ? 21   HIS A CE1   1 
ATOM   148   N  NE2   . HIS A 1  21   ? 158.488 102.786 141.355 1.00 31.97  ? 21   HIS A NE2   1 
ATOM   149   N  N     . LYS A 1  22   ? 163.384 98.619  139.837 1.00 32.52  ? 22   LYS A N     1 
ATOM   150   C  CA    . LYS A 1  22   ? 164.693 98.091  139.498 1.00 33.82  ? 22   LYS A CA    1 
ATOM   151   C  C     . LYS A 1  22   ? 164.726 97.476  138.107 1.00 35.79  ? 22   LYS A C     1 
ATOM   152   O  O     . LYS A 1  22   ? 165.747 97.575  137.422 1.00 37.22  ? 22   LYS A O     1 
ATOM   153   C  CB    . LYS A 1  22   ? 165.112 97.070  140.550 1.00 34.17  ? 22   LYS A CB    1 
ATOM   154   C  CG    . LYS A 1  22   ? 166.024 97.648  141.606 1.00 35.44  ? 22   LYS A CG    1 
ATOM   155   C  CD    . LYS A 1  22   ? 166.825 96.567  142.285 1.00 37.41  ? 22   LYS A CD    1 
ATOM   156   C  CE    . LYS A 1  22   ? 165.913 95.622  143.029 1.00 36.52  ? 22   LYS A CE    1 
ATOM   157   N  NZ    . LYS A 1  22   ? 165.084 96.350  144.020 1.00 37.99  ? 22   LYS A NZ    1 
ATOM   158   N  N     . ARG A 1  23   ? 163.642 96.843  137.675 1.00 36.16  ? 23   ARG A N     1 
ATOM   159   C  CA    . ARG A 1  23   ? 163.582 96.265  136.342 1.00 36.50  ? 23   ARG A CA    1 
ATOM   160   C  C     . ARG A 1  23   ? 163.363 97.298  135.248 1.00 39.37  ? 23   ARG A C     1 
ATOM   161   O  O     . ARG A 1  23   ? 163.910 97.146  134.153 1.00 38.13  ? 23   ARG A O     1 
ATOM   162   C  CB    . ARG A 1  23   ? 162.471 95.218  136.276 1.00 37.18  ? 23   ARG A CB    1 
ATOM   163   C  CG    . ARG A 1  23   ? 162.717 94.144  135.249 1.00 40.81  ? 23   ARG A CG    1 
ATOM   164   C  CD    . ARG A 1  23   ? 161.740 93.005  135.417 1.00 42.83  ? 23   ARG A CD    1 
ATOM   165   N  NE    . ARG A 1  23   ? 162.313 91.743  134.970 1.00 43.43  ? 23   ARG A NE    1 
ATOM   166   C  CZ    . ARG A 1  23   ? 161.986 90.558  135.465 1.00 43.38  ? 23   ARG A CZ    1 
ATOM   167   N  NH1   . ARG A 1  23   ? 161.085 90.436  136.425 1.00 42.60  ? 23   ARG A NH1   1 
ATOM   168   N  NH2   . ARG A 1  23   ? 162.576 89.467  134.982 1.00 40.59  ? 23   ARG A NH2   1 
ATOM   169   N  N     . GLN A 1  24   ? 162.577 98.340  135.511 1.00 36.77  ? 24   GLN A N     1 
ATOM   170   C  CA    . GLN A 1  24   ? 162.309 99.345  134.494 1.00 35.77  ? 24   GLN A CA    1 
ATOM   171   C  C     . GLN A 1  24   ? 163.471 100.311 134.305 1.00 37.55  ? 24   GLN A C     1 
ATOM   172   O  O     . GLN A 1  24   ? 163.647 100.843 133.205 1.00 39.04  ? 24   GLN A O     1 
ATOM   173   C  CB    . GLN A 1  24   ? 161.044 100.119 134.853 1.00 33.60  ? 24   GLN A CB    1 
ATOM   174   C  CG    . GLN A 1  24   ? 159.781 99.296  134.748 1.00 35.93  ? 24   GLN A CG    1 
ATOM   175   C  CD    . GLN A 1  24   ? 158.616 99.936  135.457 1.00 38.59  ? 24   GLN A CD    1 
ATOM   176   O  OE1   . GLN A 1  24   ? 158.750 100.994 136.065 1.00 37.98  ? 24   GLN A OE1   1 
ATOM   177   N  NE2   . GLN A 1  24   ? 157.471 99.276  135.417 1.00 35.93  ? 24   GLN A NE2   1 
ATOM   178   N  N     . GLY A 1  25   ? 164.259 100.553 135.348 1.00 33.62  ? 25   GLY A N     1 
ATOM   179   C  CA    . GLY A 1  25   ? 165.284 101.582 135.278 1.00 29.17  ? 25   GLY A CA    1 
ATOM   180   C  C     . GLY A 1  25   ? 166.391 101.234 134.297 1.00 30.97  ? 25   GLY A C     1 
ATOM   181   O  O     . GLY A 1  25   ? 166.682 100.067 134.038 1.00 37.20  ? 25   GLY A O     1 
ATOM   182   N  N     . VAL A 1  26   ? 167.013 102.278 133.742 1.00 29.41  ? 26   VAL A N     1 
ATOM   183   C  CA    . VAL A 1  26   ? 168.118 102.119 132.797 1.00 27.68  ? 26   VAL A CA    1 
ATOM   184   C  C     . VAL A 1  26   ? 169.459 102.530 133.386 1.00 30.54  ? 26   VAL A C     1 
ATOM   185   O  O     . VAL A 1  26   ? 170.502 102.263 132.771 1.00 29.62  ? 26   VAL A O     1 
ATOM   186   C  CB    . VAL A 1  26   ? 167.875 102.940 131.514 1.00 25.12  ? 26   VAL A CB    1 
ATOM   187   C  CG1   . VAL A 1  26   ? 166.549 102.586 130.898 1.00 27.13  ? 26   VAL A CG1   1 
ATOM   188   C  CG2   . VAL A 1  26   ? 167.916 104.418 131.829 1.00 25.39  ? 26   VAL A CG2   1 
ATOM   189   N  N     . MET A 1  27   ? 169.466 103.175 134.547 1.00 32.40  ? 27   MET A N     1 
ATOM   190   C  CA    . MET A 1  27   ? 170.679 103.669 135.179 1.00 31.67  ? 27   MET A CA    1 
ATOM   191   C  C     . MET A 1  27   ? 170.408 103.833 136.664 1.00 33.34  ? 27   MET A C     1 
ATOM   192   O  O     . MET A 1  27   ? 169.257 103.878 137.100 1.00 33.48  ? 27   MET A O     1 
ATOM   193   C  CB    . MET A 1  27   ? 171.137 104.990 134.557 1.00 32.32  ? 27   MET A CB    1 
ATOM   194   C  CG    . MET A 1  27   ? 170.241 106.171 134.894 1.00 34.88  ? 27   MET A CG    1 
ATOM   195   S  SD    . MET A 1  27   ? 170.757 107.199 136.276 1.00 39.13  ? 27   MET A SD    1 
ATOM   196   C  CE    . MET A 1  27   ? 172.492 107.375 135.940 1.00 34.90  ? 27   MET A CE    1 
ATOM   197   N  N     . GLU A 1  28   ? 171.485 103.923 137.440 1.00 37.25  ? 28   GLU A N     1 
ATOM   198   C  CA    . GLU A 1  28   ? 171.402 104.158 138.875 1.00 36.21  ? 28   GLU A CA    1 
ATOM   199   C  C     . GLU A 1  28   ? 172.122 105.452 139.216 1.00 35.25  ? 28   GLU A C     1 
ATOM   200   O  O     . GLU A 1  28   ? 173.297 105.618 138.881 1.00 38.81  ? 28   GLU A O     1 
ATOM   201   C  CB    . GLU A 1  28   ? 172.002 102.998 139.670 1.00 35.77  ? 28   GLU A CB    1 
ATOM   202   C  CG    . GLU A 1  28   ? 171.240 102.697 140.944 1.00 37.61  ? 28   GLU A CG    1 
ATOM   203   C  CD    . GLU A 1  28   ? 171.905 103.280 142.174 1.00 39.68  ? 28   GLU A CD    1 
ATOM   204   O  OE1   . GLU A 1  28   ? 171.186 103.745 143.078 1.00 39.78  ? 28   GLU A OE1   1 
ATOM   205   O  OE2   . GLU A 1  28   ? 173.148 103.255 142.246 1.00 42.12  ? 28   GLU A OE2   1 
ATOM   206   N  N     . VAL A 1  29   ? 171.424 106.354 139.894 1.00 32.19  ? 29   VAL A N     1 
ATOM   207   C  CA    . VAL A 1  29   ? 171.992 107.644 140.265 1.00 33.08  ? 29   VAL A CA    1 
ATOM   208   C  C     . VAL A 1  29   ? 172.863 107.452 141.496 1.00 32.81  ? 29   VAL A C     1 
ATOM   209   O  O     . VAL A 1  29   ? 172.410 106.910 142.508 1.00 34.25  ? 29   VAL A O     1 
ATOM   210   C  CB    . VAL A 1  29   ? 170.889 108.678 140.526 1.00 35.09  ? 29   VAL A CB    1 
ATOM   211   C  CG1   . VAL A 1  29   ? 171.477 109.939 141.129 1.00 32.19  ? 29   VAL A CG1   1 
ATOM   212   C  CG2   . VAL A 1  29   ? 170.144 108.992 139.245 1.00 31.47  ? 29   VAL A CG2   1 
ATOM   213   N  N     . THR A 1  30   ? 174.113 107.888 141.414 1.00 34.74  ? 30   THR A N     1 
ATOM   214   C  CA    . THR A 1  30   ? 175.043 107.756 142.529 1.00 35.71  ? 30   THR A CA    1 
ATOM   215   C  C     . THR A 1  30   ? 175.595 109.081 143.021 1.00 35.44  ? 30   THR A C     1 
ATOM   216   O  O     . THR A 1  30   ? 175.619 109.318 144.230 1.00 33.91  ? 30   THR A O     1 
ATOM   217   C  CB    . THR A 1  30   ? 176.210 106.839 142.145 1.00 34.35  ? 30   THR A CB    1 
ATOM   218   O  OG1   . THR A 1  30   ? 176.629 107.118 140.805 1.00 35.20  ? 30   THR A OG1   1 
ATOM   219   C  CG2   . THR A 1  30   ? 175.792 105.389 142.247 1.00 30.42  ? 30   THR A CG2   1 
ATOM   220   N  N     . ILE A 1  31   ? 176.013 109.964 142.124 1.00 30.95  ? 31   ILE A N     1 
ATOM   221   C  CA    . ILE A 1  31   ? 176.671 111.202 142.502 1.00 32.79  ? 31   ILE A CA    1 
ATOM   222   C  C     . ILE A 1  31   ? 175.671 112.350 142.422 1.00 35.96  ? 31   ILE A C     1 
ATOM   223   O  O     . ILE A 1  31   ? 174.604 112.238 141.823 1.00 38.86  ? 31   ILE A O     1 
ATOM   224   C  CB    . ILE A 1  31   ? 177.904 111.485 141.631 1.00 36.03  ? 31   ILE A CB    1 
ATOM   225   C  CG1   . ILE A 1  31   ? 177.512 111.501 140.158 1.00 34.97  ? 31   ILE A CG1   1 
ATOM   226   C  CG2   . ILE A 1  31   ? 178.961 110.428 141.872 1.00 38.23  ? 31   ILE A CG2   1 
ATOM   227   C  CD1   . ILE A 1  31   ? 178.666 111.312 139.234 1.00 34.70  ? 31   ILE A CD1   1 
ATOM   228   N  N     . SER A 1  32   ? 176.035 113.471 143.041 1.00 34.55  ? 32   SER A N     1 
ATOM   229   C  CA    . SER A 1  32   ? 175.192 114.656 143.078 1.00 32.51  ? 32   SER A CA    1 
ATOM   230   C  C     . SER A 1  32   ? 175.652 115.738 142.113 1.00 34.93  ? 32   SER A C     1 
ATOM   231   O  O     . SER A 1  32   ? 175.052 116.815 142.076 1.00 35.51  ? 32   SER A O     1 
ATOM   232   C  CB    . SER A 1  32   ? 175.134 115.220 144.497 1.00 34.80  ? 32   SER A CB    1 
ATOM   233   O  OG    . SER A 1  32   ? 174.289 116.354 144.547 1.00 38.92  ? 32   SER A OG    1 
ATOM   234   N  N     . ASN A 1  33   ? 176.695 115.485 141.332 1.00 42.21  ? 33   ASN A N     1 
ATOM   235   C  CA    . ASN A 1  33   ? 177.185 116.488 140.398 1.00 42.32  ? 33   ASN A CA    1 
ATOM   236   C  C     . ASN A 1  33   ? 176.265 116.567 139.184 1.00 43.97  ? 33   ASN A C     1 
ATOM   237   O  O     . ASN A 1  33   ? 175.926 115.546 138.582 1.00 44.64  ? 33   ASN A O     1 
ATOM   238   C  CB    . ASN A 1  33   ? 178.613 116.166 139.963 1.00 41.41  ? 33   ASN A CB    1 
ATOM   239   C  CG    . ASN A 1  33   ? 179.349 117.388 139.464 1.00 45.46  ? 33   ASN A CG    1 
ATOM   240   O  OD1   . ASN A 1  33   ? 178.892 118.515 139.645 1.00 46.34  ? 33   ASN A OD1   1 
ATOM   241   N  ND2   . ASN A 1  33   ? 180.481 117.173 138.813 1.00 45.73  ? 33   ASN A ND2   1 
ATOM   242   N  N     . LEU A 1  34   ? 175.870 117.787 138.823 1.00 42.06  ? 34   LEU A N     1 
ATOM   243   C  CA    . LEU A 1  34   ? 174.945 118.013 137.721 1.00 39.20  ? 34   LEU A CA    1 
ATOM   244   C  C     . LEU A 1  34   ? 175.642 117.973 136.366 1.00 41.15  ? 34   LEU A C     1 
ATOM   245   O  O     . LEU A 1  34   ? 175.342 117.112 135.536 1.00 43.93  ? 34   LEU A O     1 
ATOM   246   C  CB    . LEU A 1  34   ? 174.242 119.359 137.900 1.00 40.30  ? 34   LEU A CB    1 
ATOM   247   C  CG    . LEU A 1  34   ? 173.372 119.566 139.137 1.00 43.27  ? 34   LEU A CG    1 
ATOM   248   C  CD1   . LEU A 1  34   ? 172.929 121.009 139.204 1.00 42.54  ? 34   LEU A CD1   1 
ATOM   249   C  CD2   . LEU A 1  34   ? 172.171 118.647 139.122 1.00 39.07  ? 34   LEU A CD2   1 
ATOM   250   N  N     . PHE A 1  35   ? 176.570 118.896 136.127 1.00 47.84  ? 35   PHE A N     1 
ATOM   251   C  CA    . PHE A 1  35   ? 177.240 119.000 134.837 1.00 48.77  ? 35   PHE A CA    1 
ATOM   252   C  C     . PHE A 1  35   ? 178.738 118.903 135.039 1.00 48.85  ? 35   PHE A C     1 
ATOM   253   O  O     . PHE A 1  35   ? 179.292 119.568 135.918 1.00 48.61  ? 35   PHE A O     1 
ATOM   254   C  CB    . PHE A 1  35   ? 176.888 120.304 134.123 1.00 46.69  ? 35   PHE A CB    1 
ATOM   255   C  CG    . PHE A 1  35   ? 175.667 120.203 133.278 1.00 47.54  ? 35   PHE A CG    1 
ATOM   256   C  CD1   . PHE A 1  35   ? 175.733 119.656 132.012 1.00 46.73  ? 35   PHE A CD1   1 
ATOM   257   C  CD2   . PHE A 1  35   ? 174.453 120.635 133.754 1.00 45.50  ? 35   PHE A CD2   1 
ATOM   258   C  CE1   . PHE A 1  35   ? 174.608 119.547 131.239 1.00 47.21  ? 35   PHE A CE1   1 
ATOM   259   C  CE2   . PHE A 1  35   ? 173.334 120.531 132.986 1.00 47.90  ? 35   PHE A CE2   1 
ATOM   260   C  CZ    . PHE A 1  35   ? 173.405 119.989 131.726 1.00 48.92  ? 35   PHE A CZ    1 
ATOM   261   N  N     . GLU A 1  36   ? 179.384 118.066 134.229 1.00 47.12  ? 36   GLU A N     1 
ATOM   262   C  CA    . GLU A 1  36   ? 180.838 117.981 134.261 1.00 50.30  ? 36   GLU A CA    1 
ATOM   263   C  C     . GLU A 1  36   ? 181.468 118.956 133.272 1.00 50.64  ? 36   GLU A C     1 
ATOM   264   O  O     . GLU A 1  36   ? 182.537 119.516 133.536 1.00 53.06  ? 36   GLU A O     1 
ATOM   265   C  CB    . GLU A 1  36   ? 181.271 116.547 133.973 1.00 51.93  ? 36   GLU A CB    1 
ATOM   266   C  CG    . GLU A 1  36   ? 180.845 116.026 132.618 1.00 50.11  ? 36   GLU A CG    1 
ATOM   267   C  CD    . GLU A 1  36   ? 180.969 114.526 132.526 1.00 52.75  ? 36   GLU A CD    1 
ATOM   268   O  OE1   . GLU A 1  36   ? 181.554 113.929 133.455 1.00 51.19  ? 36   GLU A OE1   1 
ATOM   269   O  OE2   . GLU A 1  36   ? 180.496 113.945 131.524 1.00 51.40  ? 36   GLU A OE2   1 
ATOM   270   N  N     . GLY A 1  37   ? 180.822 119.164 132.129 1.00 42.31  ? 37   GLY A N     1 
ATOM   271   C  CA    . GLY A 1  37   ? 181.271 120.087 131.107 1.00 41.56  ? 37   GLY A CA    1 
ATOM   272   C  C     . GLY A 1  37   ? 180.078 120.601 130.329 1.00 43.54  ? 37   GLY A C     1 
ATOM   273   O  O     . GLY A 1  37   ? 179.108 121.081 130.923 1.00 44.57  ? 37   GLY A O     1 
ATOM   274   N  N     . THR A 1  38   ? 180.143 120.535 128.998 1.00 42.74  ? 38   THR A N     1 
ATOM   275   C  CA    . THR A 1  38   ? 178.931 120.710 128.204 1.00 43.83  ? 38   THR A CA    1 
ATOM   276   C  C     . THR A 1  38   ? 177.974 119.540 128.402 1.00 43.17  ? 38   THR A C     1 
ATOM   277   O  O     . THR A 1  38   ? 176.758 119.732 128.510 1.00 42.80  ? 38   THR A O     1 
ATOM   278   C  CB    . THR A 1  38   ? 179.277 120.870 126.724 1.00 41.02  ? 38   THR A CB    1 
ATOM   279   O  OG1   . THR A 1  38   ? 180.053 119.747 126.290 1.00 39.96  ? 38   THR A OG1   1 
ATOM   280   C  CG2   . THR A 1  38   ? 180.062 122.146 126.492 1.00 40.62  ? 38   THR A CG2   1 
ATOM   281   N  N     . LEU A 1  39   ? 178.503 118.323 128.441 1.00 42.11  ? 39   LEU A N     1 
ATOM   282   C  CA    . LEU A 1  39   ? 177.693 117.131 128.609 1.00 41.82  ? 39   LEU A CA    1 
ATOM   283   C  C     . LEU A 1  39   ? 177.301 116.949 130.069 1.00 44.38  ? 39   LEU A C     1 
ATOM   284   O  O     . LEU A 1  39   ? 177.980 117.446 130.969 1.00 44.94  ? 39   LEU A O     1 
ATOM   285   C  CB    . LEU A 1  39   ? 178.452 115.907 128.114 1.00 42.09  ? 39   LEU A CB    1 
ATOM   286   C  CG    . LEU A 1  39   ? 178.848 115.898 126.643 1.00 42.61  ? 39   LEU A CG    1 
ATOM   287   C  CD1   . LEU A 1  39   ? 180.001 114.941 126.429 1.00 41.66  ? 39   LEU A CD1   1 
ATOM   288   C  CD2   . LEU A 1  39   ? 177.665 115.522 125.774 1.00 42.53  ? 39   LEU A CD2   1 
ATOM   289   N  N     . PRO A 1  40   ? 176.201 116.246 130.334 1.00 44.63  ? 40   PRO A N     1 
ATOM   290   C  CA    . PRO A 1  40   ? 175.784 116.038 131.722 1.00 42.83  ? 40   PRO A CA    1 
ATOM   291   C  C     . PRO A 1  40   ? 176.716 115.090 132.456 1.00 44.10  ? 40   PRO A C     1 
ATOM   292   O  O     . PRO A 1  40   ? 177.393 114.252 131.855 1.00 44.26  ? 40   PRO A O     1 
ATOM   293   C  CB    . PRO A 1  40   ? 174.377 115.443 131.584 1.00 41.68  ? 40   PRO A CB    1 
ATOM   294   C  CG    . PRO A 1  40   ? 174.053 115.507 130.103 1.00 41.52  ? 40   PRO A CG    1 
ATOM   295   C  CD    . PRO A 1  40   ? 175.354 115.469 129.417 1.00 41.21  ? 40   PRO A CD    1 
ATOM   296   N  N     . ALA A 1  41   ? 176.750 115.238 133.777 1.00 36.76  ? 41   ALA A N     1 
ATOM   297   C  CA    . ALA A 1  41   ? 177.606 114.396 134.596 1.00 37.29  ? 41   ALA A CA    1 
ATOM   298   C  C     . ALA A 1  41   ? 177.036 112.989 134.683 1.00 37.98  ? 41   ALA A C     1 
ATOM   299   O  O     . ALA A 1  41   ? 175.942 112.777 135.210 1.00 44.96  ? 41   ALA A O     1 
ATOM   300   C  CB    . ALA A 1  41   ? 177.750 114.985 135.995 1.00 38.76  ? 41   ALA A CB    1 
ATOM   301   N  N     . GLU A 1  42   ? 177.791 112.023 134.171 1.00 33.74  ? 42   GLU A N     1 
ATOM   302   C  CA    . GLU A 1  42   ? 177.340 110.641 134.153 1.00 34.80  ? 42   GLU A CA    1 
ATOM   303   C  C     . GLU A 1  42   ? 177.187 110.125 135.576 1.00 37.15  ? 42   GLU A C     1 
ATOM   304   O  O     . GLU A 1  42   ? 178.070 110.321 136.412 1.00 35.37  ? 42   GLU A O     1 
ATOM   305   C  CB    . GLU A 1  42   ? 178.322 109.772 133.372 1.00 32.85  ? 42   GLU A CB    1 
ATOM   306   C  CG    . GLU A 1  42   ? 178.491 108.380 133.929 1.00 35.23  ? 42   GLU A CG    1 
ATOM   307   C  CD    . GLU A 1  42   ? 179.131 107.440 132.938 1.00 38.99  ? 42   GLU A CD    1 
ATOM   308   O  OE1   . GLU A 1  42   ? 179.865 107.920 132.050 1.00 37.20  ? 42   GLU A OE1   1 
ATOM   309   O  OE2   . GLU A 1  42   ? 178.900 106.217 133.044 1.00 39.89  ? 42   GLU A OE2   1 
ATOM   310   N  N     . GLY A 1  43   ? 176.067 109.455 135.843 1.00 35.39  ? 43   GLY A N     1 
ATOM   311   C  CA    . GLY A 1  43   ? 175.728 109.004 137.173 1.00 34.66  ? 43   GLY A CA    1 
ATOM   312   C  C     . GLY A 1  43   ? 174.910 109.986 137.981 1.00 34.96  ? 43   GLY A C     1 
ATOM   313   O  O     . GLY A 1  43   ? 174.507 109.654 139.099 1.00 36.31  ? 43   GLY A O     1 
ATOM   314   N  N     . GLY A 1  44   ? 174.659 111.184 137.454 1.00 29.56  ? 44   GLY A N     1 
ATOM   315   C  CA    . GLY A 1  44   ? 173.846 112.166 138.136 1.00 27.26  ? 44   GLY A CA    1 
ATOM   316   C  C     . GLY A 1  44   ? 172.413 112.184 137.634 1.00 28.81  ? 44   GLY A C     1 
ATOM   317   O  O     . GLY A 1  44   ? 171.990 111.365 136.822 1.00 32.17  ? 44   GLY A O     1 
ATOM   318   N  N     . ILE A 1  45   ? 171.654 113.163 138.133 1.00 28.96  ? 45   ILE A N     1 
ATOM   319   C  CA    . ILE A 1  45   ? 170.237 113.263 137.794 1.00 27.01  ? 45   ILE A CA    1 
ATOM   320   C  C     . ILE A 1  45   ? 169.988 113.909 136.443 1.00 29.50  ? 45   ILE A C     1 
ATOM   321   O  O     . ILE A 1  45   ? 168.827 114.119 136.075 1.00 34.31  ? 45   ILE A O     1 
ATOM   322   C  CB    . ILE A 1  45   ? 169.473 114.041 138.877 1.00 28.09  ? 45   ILE A CB    1 
ATOM   323   C  CG1   . ILE A 1  45   ? 169.894 115.505 138.881 1.00 27.79  ? 45   ILE A CG1   1 
ATOM   324   C  CG2   . ILE A 1  45   ? 169.731 113.424 140.230 1.00 30.20  ? 45   ILE A CG2   1 
ATOM   325   C  CD1   . ILE A 1  45   ? 169.010 116.382 139.729 1.00 29.67  ? 45   ILE A CD1   1 
ATOM   326   N  N     . TYR A 1  46   ? 171.036 114.247 135.700 1.00 33.77  ? 46   TYR A N     1 
ATOM   327   C  CA    . TYR A 1  46   ? 170.909 114.736 134.336 1.00 30.48  ? 46   TYR A CA    1 
ATOM   328   C  C     . TYR A 1  46   ? 171.480 113.759 133.326 1.00 29.68  ? 46   TYR A C     1 
ATOM   329   O  O     . TYR A 1  46   ? 171.647 114.121 132.161 1.00 31.91  ? 46   TYR A O     1 
ATOM   330   C  CB    . TYR A 1  46   ? 171.604 116.087 134.188 1.00 31.06  ? 46   TYR A CB    1 
ATOM   331   C  CG    . TYR A 1  46   ? 170.895 117.225 134.866 1.00 32.21  ? 46   TYR A CG    1 
ATOM   332   C  CD1   . TYR A 1  46   ? 169.575 117.117 135.255 1.00 30.65  ? 46   TYR A CD1   1 
ATOM   333   C  CD2   . TYR A 1  46   ? 171.562 118.398 135.150 1.00 33.76  ? 46   TYR A CD2   1 
ATOM   334   C  CE1   . TYR A 1  46   ? 168.936 118.160 135.887 1.00 34.54  ? 46   TYR A CE1   1 
ATOM   335   C  CE2   . TYR A 1  46   ? 170.938 119.434 135.785 1.00 33.89  ? 46   TYR A CE2   1 
ATOM   336   C  CZ    . TYR A 1  46   ? 169.627 119.317 136.147 1.00 35.83  ? 46   TYR A CZ    1 
ATOM   337   O  OH    . TYR A 1  46   ? 169.011 120.369 136.775 1.00 36.80  ? 46   TYR A OH    1 
ATOM   338   N  N     . ASP A 1  47   ? 171.780 112.535 133.743 1.00 31.53  ? 47   ASP A N     1 
ATOM   339   C  CA    . ASP A 1  47   ? 172.483 111.599 132.879 1.00 31.53  ? 47   ASP A CA    1 
ATOM   340   C  C     . ASP A 1  47   ? 171.716 111.364 131.585 1.00 33.69  ? 47   ASP A C     1 
ATOM   341   O  O     . ASP A 1  47   ? 170.498 111.185 131.586 1.00 39.41  ? 47   ASP A O     1 
ATOM   342   C  CB    . ASP A 1  47   ? 172.703 110.277 133.607 1.00 28.70  ? 47   ASP A CB    1 
ATOM   343   C  CG    . ASP A 1  47   ? 173.644 109.367 132.871 1.00 33.74  ? 47   ASP A CG    1 
ATOM   344   O  OD1   . ASP A 1  47   ? 174.239 109.808 131.873 1.00 38.48  ? 47   ASP A OD1   1 
ATOM   345   O  OD2   . ASP A 1  47   ? 173.801 108.207 133.282 1.00 35.96  ? 47   ASP A OD2   1 
ATOM   346   N  N     . ALA A 1  48   ? 172.449 111.356 130.474 1.00 30.55  ? 48   ALA A N     1 
ATOM   347   C  CA    . ALA A 1  48   ? 171.844 111.250 129.158 1.00 29.75  ? 48   ALA A CA    1 
ATOM   348   C  C     . ALA A 1  48   ? 171.378 109.841 128.828 1.00 33.79  ? 48   ALA A C     1 
ATOM   349   O  O     . ALA A 1  48   ? 170.833 109.633 127.741 1.00 36.19  ? 48   ALA A O     1 
ATOM   350   C  CB    . ALA A 1  48   ? 172.824 111.736 128.093 1.00 29.93  ? 48   ALA A CB    1 
ATOM   351   N  N     . ARG A 1  49   ? 171.617 108.862 129.700 1.00 29.92  ? 49   ARG A N     1 
ATOM   352   C  CA    . ARG A 1  49   ? 170.983 107.565 129.511 1.00 29.29  ? 49   ARG A CA    1 
ATOM   353   C  C     . ARG A 1  49   ? 169.491 107.625 129.778 1.00 28.18  ? 49   ARG A C     1 
ATOM   354   O  O     . ARG A 1  49   ? 168.772 106.686 129.430 1.00 30.73  ? 49   ARG A O     1 
ATOM   355   C  CB    . ARG A 1  49   ? 171.615 106.508 130.411 1.00 31.78  ? 49   ARG A CB    1 
ATOM   356   C  CG    . ARG A 1  49   ? 172.666 105.666 129.730 1.00 30.20  ? 49   ARG A CG    1 
ATOM   357   C  CD    . ARG A 1  49   ? 173.424 104.837 130.730 1.00 32.23  ? 49   ARG A CD    1 
ATOM   358   N  NE    . ARG A 1  49   ? 173.947 105.657 131.814 1.00 32.66  ? 49   ARG A NE    1 
ATOM   359   C  CZ    . ARG A 1  49   ? 174.662 105.191 132.826 1.00 33.57  ? 49   ARG A CZ    1 
ATOM   360   N  NH1   . ARG A 1  49   ? 174.967 103.908 132.924 1.00 30.39  ? 49   ARG A NH1   1 
ATOM   361   N  NH2   . ARG A 1  49   ? 175.077 106.032 133.767 1.00 32.33  ? 49   ARG A NH2   1 
ATOM   362   N  N     . MET A 1  50   ? 169.019 108.702 130.394 1.00 27.03  ? 50   MET A N     1 
ATOM   363   C  CA    . MET A 1  50   ? 167.616 108.893 130.708 1.00 25.96  ? 50   MET A CA    1 
ATOM   364   C  C     . MET A 1  50   ? 166.937 109.886 129.774 1.00 30.81  ? 50   MET A C     1 
ATOM   365   O  O     . MET A 1  50   ? 165.925 110.483 130.149 1.00 34.65  ? 50   MET A O     1 
ATOM   366   C  CB    . MET A 1  50   ? 167.476 109.339 132.163 1.00 24.54  ? 50   MET A CB    1 
ATOM   367   C  CG    . MET A 1  50   ? 167.767 108.230 133.153 1.00 31.32  ? 50   MET A CG    1 
ATOM   368   S  SD    . MET A 1  50   ? 167.810 108.737 134.874 1.00 42.15  ? 50   MET A SD    1 
ATOM   369   C  CE    . MET A 1  50   ? 167.050 110.332 134.768 1.00 27.60  ? 50   MET A CE    1 
ATOM   370   N  N     . GLY A 1  51   ? 167.465 110.072 128.572 1.00 31.51  ? 51   GLY A N     1 
ATOM   371   C  CA    . GLY A 1  51   ? 166.906 111.001 127.615 1.00 28.78  ? 51   GLY A CA    1 
ATOM   372   C  C     . GLY A 1  51   ? 167.728 112.272 127.487 1.00 31.99  ? 51   GLY A C     1 
ATOM   373   O  O     . GLY A 1  51   ? 168.709 112.500 128.195 1.00 33.60  ? 51   GLY A O     1 
ATOM   374   N  N     . THR A 1  52   ? 167.304 113.114 126.549 1.00 35.12  ? 52   THR A N     1 
ATOM   375   C  CA    . THR A 1  52   ? 167.962 114.381 126.259 1.00 34.95  ? 52   THR A CA    1 
ATOM   376   C  C     . THR A 1  52   ? 166.919 115.480 126.153 1.00 37.96  ? 52   THR A C     1 
ATOM   377   O  O     . THR A 1  52   ? 165.905 115.316 125.468 1.00 41.90  ? 52   THR A O     1 
ATOM   378   C  CB    . THR A 1  52   ? 168.778 114.298 124.966 1.00 35.78  ? 52   THR A CB    1 
ATOM   379   O  OG1   . THR A 1  52   ? 169.220 115.608 124.597 1.00 39.12  ? 52   THR A OG1   1 
ATOM   380   C  CG2   . THR A 1  52   ? 167.961 113.704 123.835 1.00 33.21  ? 52   THR A CG2   1 
ATOM   381   N  N     . THR A 1  53   ? 167.159 116.591 126.843 1.00 37.36  ? 53   THR A N     1 
ATOM   382   C  CA    . THR A 1  53   ? 166.390 117.810 126.641 1.00 40.47  ? 53   THR A CA    1 
ATOM   383   C  C     . THR A 1  53   ? 167.197 118.897 125.953 1.00 42.52  ? 53   THR A C     1 
ATOM   384   O  O     . THR A 1  53   ? 166.795 120.063 125.978 1.00 42.74  ? 53   THR A O     1 
ATOM   385   C  CB    . THR A 1  53   ? 165.837 118.329 127.967 1.00 40.23  ? 53   THR A CB    1 
ATOM   386   O  OG1   . THR A 1  53   ? 166.904 118.485 128.910 1.00 39.22  ? 53   THR A OG1   1 
ATOM   387   C  CG2   . THR A 1  53   ? 164.782 117.383 128.509 1.00 39.06  ? 53   THR A CG2   1 
ATOM   388   N  N     . ASP A 1  54   ? 168.328 118.544 125.352 1.00 41.91  ? 54   ASP A N     1 
ATOM   389   C  CA    . ASP A 1  54   ? 169.149 119.484 124.610 1.00 44.29  ? 54   ASP A CA    1 
ATOM   390   C  C     . ASP A 1  54   ? 169.313 119.005 123.176 1.00 44.20  ? 54   ASP A C     1 
ATOM   391   O  O     . ASP A 1  54   ? 169.325 117.804 122.900 1.00 45.03  ? 54   ASP A O     1 
ATOM   392   C  CB    . ASP A 1  54   ? 170.516 119.672 125.266 1.00 46.56  ? 54   ASP A CB    1 
ATOM   393   C  CG    . ASP A 1  54   ? 171.264 120.861 124.709 1.00 47.47  ? 54   ASP A CG    1 
ATOM   394   O  OD1   . ASP A 1  54   ? 170.801 121.999 124.916 1.00 46.27  ? 54   ASP A OD1   1 
ATOM   395   O  OD2   . ASP A 1  54   ? 172.319 120.664 124.076 1.00 46.88  ? 54   ASP A OD2   1 
ATOM   396   N  N     . HIS A 1  55   ? 169.447 119.964 122.269 1.00 44.65  ? 55   HIS A N     1 
ATOM   397   C  CA    . HIS A 1  55   ? 169.440 119.707 120.839 1.00 45.97  ? 55   HIS A CA    1 
ATOM   398   C  C     . HIS A 1  55   ? 170.826 119.476 120.256 1.00 48.30  ? 55   HIS A C     1 
ATOM   399   O  O     . HIS A 1  55   ? 171.007 119.651 119.048 1.00 49.75  ? 55   HIS A O     1 
ATOM   400   C  CB    . HIS A 1  55   ? 168.754 120.868 120.118 1.00 46.14  ? 55   HIS A CB    1 
ATOM   401   C  CG    . HIS A 1  55   ? 167.272 120.907 120.331 1.00 50.69  ? 55   HIS A CG    1 
ATOM   402   N  ND1   . HIS A 1  55   ? 166.701 121.365 121.499 1.00 49.56  ? 55   HIS A ND1   1 
ATOM   403   C  CD2   . HIS A 1  55   ? 166.245 120.539 119.530 1.00 47.76  ? 55   HIS A CD2   1 
ATOM   404   C  CE1   . HIS A 1  55   ? 165.387 121.275 121.409 1.00 48.97  ? 55   HIS A CE1   1 
ATOM   405   N  NE2   . HIS A 1  55   ? 165.084 120.780 120.222 1.00 48.77  ? 55   HIS A NE2   1 
ATOM   406   N  N     . HIS A 1  56   ? 171.807 119.099 121.075 1.00 47.79  ? 56   HIS A N     1 
ATOM   407   C  CA    . HIS A 1  56   ? 173.143 118.821 120.566 1.00 47.15  ? 56   HIS A CA    1 
ATOM   408   C  C     . HIS A 1  56   ? 173.526 117.348 120.672 1.00 48.49  ? 56   HIS A C     1 
ATOM   409   O  O     . HIS A 1  56   ? 174.125 116.802 119.740 1.00 50.23  ? 56   HIS A O     1 
ATOM   410   C  CB    . HIS A 1  56   ? 174.175 119.693 121.288 1.00 48.19  ? 56   HIS A CB    1 
ATOM   411   C  CG    . HIS A 1  56   ? 173.842 121.155 121.276 1.00 51.81  ? 56   HIS A CG    1 
ATOM   412   N  ND1   . HIS A 1  56   ? 172.778 121.685 121.973 1.00 52.53  ? 56   HIS A ND1   1 
ATOM   413   C  CD2   . HIS A 1  56   ? 174.419 122.194 120.627 1.00 49.12  ? 56   HIS A CD2   1 
ATOM   414   C  CE1   . HIS A 1  56   ? 172.722 122.989 121.767 1.00 49.03  ? 56   HIS A CE1   1 
ATOM   415   N  NE2   . HIS A 1  56   ? 173.707 123.322 120.953 1.00 50.98  ? 56   HIS A NE2   1 
ATOM   416   N  N     . TYR A 1  57   ? 173.202 116.685 121.778 1.00 43.69  ? 57   TYR A N     1 
ATOM   417   C  CA    . TYR A 1  57   ? 173.567 115.290 121.972 1.00 40.85  ? 57   TYR A CA    1 
ATOM   418   C  C     . TYR A 1  57   ? 172.334 114.396 121.902 1.00 42.04  ? 57   TYR A C     1 
ATOM   419   O  O     . TYR A 1  57   ? 171.217 114.827 122.191 1.00 42.56  ? 57   TYR A O     1 
ATOM   420   C  CB    . TYR A 1  57   ? 174.283 115.079 123.309 1.00 37.00  ? 57   TYR A CB    1 
ATOM   421   C  CG    . TYR A 1  57   ? 173.525 115.558 124.522 1.00 41.50  ? 57   TYR A CG    1 
ATOM   422   C  CD1   . TYR A 1  57   ? 173.646 116.863 124.970 1.00 42.22  ? 57   TYR A CD1   1 
ATOM   423   C  CD2   . TYR A 1  57   ? 172.708 114.695 125.236 1.00 41.52  ? 57   TYR A CD2   1 
ATOM   424   C  CE1   . TYR A 1  57   ? 172.961 117.298 126.081 1.00 41.62  ? 57   TYR A CE1   1 
ATOM   425   C  CE2   . TYR A 1  57   ? 172.019 115.122 126.346 1.00 40.94  ? 57   TYR A CE2   1 
ATOM   426   C  CZ    . TYR A 1  57   ? 172.147 116.424 126.765 1.00 42.11  ? 57   TYR A CZ    1 
ATOM   427   O  OH    . TYR A 1  57   ? 171.461 116.853 127.876 1.00 40.10  ? 57   TYR A OH    1 
ATOM   428   N  N     . LYS A 1  58   ? 172.551 113.149 121.494 1.00 35.61  ? 58   LYS A N     1 
ATOM   429   C  CA    . LYS A 1  58   ? 171.495 112.154 121.432 1.00 33.11  ? 58   LYS A CA    1 
ATOM   430   C  C     . LYS A 1  58   ? 171.255 111.525 122.800 1.00 36.54  ? 58   LYS A C     1 
ATOM   431   O  O     . LYS A 1  58   ? 172.022 111.703 123.747 1.00 37.05  ? 58   LYS A O     1 
ATOM   432   C  CB    . LYS A 1  58   ? 171.839 111.052 120.436 1.00 30.85  ? 58   LYS A CB    1 
ATOM   433   C  CG    . LYS A 1  58   ? 171.651 111.400 118.981 1.00 36.24  ? 58   LYS A CG    1 
ATOM   434   C  CD    . LYS A 1  58   ? 171.925 110.180 118.127 1.00 35.43  ? 58   LYS A CD    1 
ATOM   435   C  CE    . LYS A 1  58   ? 171.805 110.480 116.652 1.00 34.96  ? 58   LYS A CE    1 
ATOM   436   N  NZ    . LYS A 1  58   ? 172.133 109.285 115.831 1.00 38.13  ? 58   LYS A NZ    1 
ATOM   437   N  N     . CYS A 1  59   ? 170.160 110.780 122.892 1.00 35.28  ? 59   CYS A N     1 
ATOM   438   C  CA    . CYS A 1  59   ? 169.934 109.918 124.040 1.00 29.36  ? 59   CYS A CA    1 
ATOM   439   C  C     . CYS A 1  59   ? 170.804 108.678 123.919 1.00 30.41  ? 59   CYS A C     1 
ATOM   440   O  O     . CYS A 1  59   ? 170.892 108.065 122.855 1.00 34.72  ? 59   CYS A O     1 
ATOM   441   C  CB    . CYS A 1  59   ? 168.462 109.529 124.127 1.00 27.12  ? 59   CYS A CB    1 
ATOM   442   S  SG    . CYS A 1  59   ? 168.056 108.340 125.412 1.00 32.48  ? 59   CYS A SG    1 
ATOM   443   N  N     . ILE A 1  60   ? 171.469 108.315 125.014 1.00 27.93  ? 60   ILE A N     1 
ATOM   444   C  CA    . ILE A 1  60   ? 172.340 107.148 124.980 1.00 32.47  ? 60   ILE A CA    1 
ATOM   445   C  C     . ILE A 1  60   ? 171.511 105.878 124.837 1.00 30.86  ? 60   ILE A C     1 
ATOM   446   O  O     . ILE A 1  60   ? 171.908 104.930 124.151 1.00 29.71  ? 60   ILE A O     1 
ATOM   447   C  CB    . ILE A 1  60   ? 173.228 107.118 126.235 1.00 32.51  ? 60   ILE A CB    1 
ATOM   448   C  CG1   . ILE A 1  60   ? 174.369 108.112 126.097 1.00 29.17  ? 60   ILE A CG1   1 
ATOM   449   C  CG2   . ILE A 1  60   ? 173.848 105.757 126.420 1.00 29.05  ? 60   ILE A CG2   1 
ATOM   450   C  CD1   . ILE A 1  60   ? 175.053 108.406 127.401 1.00 30.26  ? 60   ILE A CD1   1 
ATOM   451   N  N     . THR A 1  61   ? 170.340 105.847 125.472 1.00 32.23  ? 61   THR A N     1 
ATOM   452   C  CA    . THR A 1  61   ? 169.526 104.637 125.513 1.00 27.40  ? 61   THR A CA    1 
ATOM   453   C  C     . THR A 1  61   ? 168.934 104.295 124.149 1.00 26.71  ? 61   THR A C     1 
ATOM   454   O  O     . THR A 1  61   ? 169.067 103.164 123.673 1.00 30.17  ? 61   THR A O     1 
ATOM   455   C  CB    . THR A 1  61   ? 168.424 104.806 126.552 1.00 27.94  ? 61   THR A CB    1 
ATOM   456   O  OG1   . THR A 1  61   ? 168.973 105.415 127.723 1.00 30.79  ? 61   THR A OG1   1 
ATOM   457   C  CG2   . THR A 1  61   ? 167.841 103.473 126.921 1.00 25.55  ? 61   THR A CG2   1 
ATOM   458   N  N     . CYS A 1  62   ? 168.279 105.255 123.498 1.00 29.74  ? 62   CYS A N     1 
ATOM   459   C  CA    . CYS A 1  62   ? 167.559 104.973 122.261 1.00 28.84  ? 62   CYS A CA    1 
ATOM   460   C  C     . CYS A 1  62   ? 168.189 105.610 121.033 1.00 28.45  ? 62   CYS A C     1 
ATOM   461   O  O     . CYS A 1  62   ? 167.776 105.291 119.915 1.00 32.34  ? 62   CYS A O     1 
ATOM   462   C  CB    . CYS A 1  62   ? 166.094 105.415 122.370 1.00 27.03  ? 62   CYS A CB    1 
ATOM   463   S  SG    . CYS A 1  62   ? 165.817 107.157 122.672 1.00 33.87  ? 62   CYS A SG    1 
ATOM   464   N  N     . SER A 1  63   ? 169.177 106.487 121.211 1.00 27.72  ? 63   SER A N     1 
ATOM   465   C  CA    . SER A 1  63   ? 169.881 107.129 120.099 1.00 31.83  ? 63   SER A CA    1 
ATOM   466   C  C     . SER A 1  63   ? 168.926 107.934 119.226 1.00 35.23  ? 63   SER A C     1 
ATOM   467   O  O     . SER A 1  63   ? 168.951 107.845 117.999 1.00 36.27  ? 63   SER A O     1 
ATOM   468   C  CB    . SER A 1  63   ? 170.647 106.102 119.264 1.00 33.87  ? 63   SER A CB    1 
ATOM   469   O  OG    . SER A 1  63   ? 171.738 105.575 119.995 1.00 38.59  ? 63   SER A OG    1 
ATOM   470   N  N     . HIS A 1  64   ? 168.068 108.718 119.867 1.00 31.50  ? 64   HIS A N     1 
ATOM   471   C  CA    . HIS A 1  64   ? 167.147 109.610 119.187 1.00 31.16  ? 64   HIS A CA    1 
ATOM   472   C  C     . HIS A 1  64   ? 167.463 111.049 119.563 1.00 31.82  ? 64   HIS A C     1 
ATOM   473   O  O     . HIS A 1  64   ? 168.197 111.318 120.514 1.00 30.19  ? 64   HIS A O     1 
ATOM   474   C  CB    . HIS A 1  64   ? 165.694 109.293 119.548 1.00 28.29  ? 64   HIS A CB    1 
ATOM   475   C  CG    . HIS A 1  64   ? 165.071 108.231 118.699 1.00 28.16  ? 64   HIS A CG    1 
ATOM   476   N  ND1   . HIS A 1  64   ? 164.835 108.397 117.354 1.00 33.02  ? 64   HIS A ND1   1 
ATOM   477   C  CD2   . HIS A 1  64   ? 164.594 107.006 119.016 1.00 29.28  ? 64   HIS A CD2   1 
ATOM   478   C  CE1   . HIS A 1  64   ? 164.264 107.308 116.872 1.00 29.75  ? 64   HIS A CE1   1 
ATOM   479   N  NE2   . HIS A 1  64   ? 164.106 106.449 117.860 1.00 28.45  ? 64   HIS A NE2   1 
ATOM   480   N  N     . GLN A 1  65   ? 166.894 111.976 118.803 1.00 39.93  ? 65   GLN A N     1 
ATOM   481   C  CA    . GLN A 1  65   ? 167.011 113.394 119.110 1.00 38.61  ? 65   GLN A CA    1 
ATOM   482   C  C     . GLN A 1  65   ? 165.950 113.766 120.139 1.00 39.27  ? 65   GLN A C     1 
ATOM   483   O  O     . GLN A 1  65   ? 165.266 112.905 120.696 1.00 42.40  ? 65   GLN A O     1 
ATOM   484   C  CB    . GLN A 1  65   ? 166.897 114.224 117.837 1.00 39.42  ? 65   GLN A CB    1 
ATOM   485   C  CG    . GLN A 1  65   ? 167.950 113.905 116.785 1.00 39.35  ? 65   GLN A CG    1 
ATOM   486   C  CD    . GLN A 1  65   ? 169.360 114.170 117.266 1.00 41.15  ? 65   GLN A CD    1 
ATOM   487   O  OE1   . GLN A 1  65   ? 169.597 115.062 118.076 1.00 42.73  ? 65   GLN A OE1   1 
ATOM   488   N  NE2   . GLN A 1  65   ? 170.309 113.404 116.752 1.00 41.83  ? 65   GLN A NE2   1 
ATOM   489   N  N     . ARG A 1  66   ? 165.792 115.061 120.408 1.00 36.11  ? 66   ARG A N     1 
ATOM   490   C  CA    . ARG A 1  66   ? 164.841 115.477 121.432 1.00 35.99  ? 66   ARG A CA    1 
ATOM   491   C  C     . ARG A 1  66   ? 163.423 115.065 121.060 1.00 39.17  ? 66   ARG A C     1 
ATOM   492   O  O     . ARG A 1  66   ? 162.668 114.605 121.920 1.00 37.50  ? 66   ARG A O     1 
ATOM   493   C  CB    . ARG A 1  66   ? 164.953 116.995 121.663 1.00 33.21  ? 66   ARG A CB    1 
ATOM   494   C  CG    . ARG A 1  66   ? 163.833 117.689 122.498 1.00 39.10  ? 66   ARG A CG    1 
ATOM   495   C  CD    . ARG A 1  66   ? 162.461 117.867 121.817 1.00 38.73  ? 66   ARG A CD    1 
ATOM   496   N  NE    . ARG A 1  66   ? 161.609 118.848 122.482 1.00 41.24  ? 66   ARG A NE    1 
ATOM   497   C  CZ    . ARG A 1  66   ? 160.281 118.813 122.484 1.00 39.03  ? 66   ARG A CZ    1 
ATOM   498   N  NH1   . ARG A 1  66   ? 159.611 117.862 121.856 1.00 35.36  ? 66   ARG A NH1   1 
ATOM   499   N  NH2   . ARG A 1  66   ? 159.608 119.763 123.125 1.00 36.83  ? 66   ARG A NH2   1 
ATOM   500   N  N     . LYS A 1  67   ? 163.048 115.213 119.790 1.00 37.77  ? 67   LYS A N     1 
ATOM   501   C  CA    . LYS A 1  67   ? 161.653 115.042 119.402 1.00 36.66  ? 67   LYS A CA    1 
ATOM   502   C  C     . LYS A 1  67   ? 161.212 113.585 119.463 1.00 36.86  ? 67   LYS A C     1 
ATOM   503   O  O     . LYS A 1  67   ? 160.063 113.297 119.813 1.00 37.07  ? 67   LYS A O     1 
ATOM   504   C  CB    . LYS A 1  67   ? 161.425 115.607 118.002 1.00 36.16  ? 67   LYS A CB    1 
ATOM   505   C  CG    . LYS A 1  67   ? 160.635 116.902 117.993 1.00 37.94  ? 67   LYS A CG    1 
ATOM   506   C  CD    . LYS A 1  67   ? 159.740 116.992 116.777 1.00 38.69  ? 67   LYS A CD    1 
ATOM   507   C  CE    . LYS A 1  67   ? 160.549 116.985 115.498 1.00 37.00  ? 67   LYS A CE    1 
ATOM   508   N  NZ    . LYS A 1  67   ? 159.674 116.998 114.291 1.00 37.60  ? 67   LYS A NZ    1 
ATOM   509   N  N     . GLN A 1  68   ? 162.088 112.654 119.105 1.00 30.70  ? 68   GLN A N     1 
ATOM   510   C  CA    . GLN A 1  68   ? 161.704 111.253 119.057 1.00 30.68  ? 68   GLN A CA    1 
ATOM   511   C  C     . GLN A 1  68   ? 162.054 110.482 120.321 1.00 31.82  ? 68   GLN A C     1 
ATOM   512   O  O     . GLN A 1  68   ? 161.773 109.283 120.390 1.00 37.63  ? 68   GLN A O     1 
ATOM   513   C  CB    . GLN A 1  68   ? 162.346 110.574 117.851 1.00 30.18  ? 68   GLN A CB    1 
ATOM   514   C  CG    . GLN A 1  68   ? 161.593 110.782 116.559 1.00 30.61  ? 68   GLN A CG    1 
ATOM   515   C  CD    . GLN A 1  68   ? 161.863 112.142 115.954 1.00 34.69  ? 68   GLN A CD    1 
ATOM   516   O  OE1   . GLN A 1  68   ? 160.987 112.743 115.335 1.00 34.30  ? 68   GLN A OE1   1 
ATOM   517   N  NE2   . GLN A 1  68   ? 163.075 112.646 116.151 1.00 33.92  ? 68   GLN A NE2   1 
ATOM   518   N  N     . CYS A 1  69   ? 162.645 111.127 121.317 1.00 26.39  ? 69   CYS A N     1 
ATOM   519   C  CA    . CYS A 1  69   ? 162.990 110.465 122.565 1.00 31.00  ? 69   CYS A CA    1 
ATOM   520   C  C     . CYS A 1  69   ? 161.955 110.826 123.618 1.00 33.07  ? 69   CYS A C     1 
ATOM   521   O  O     . CYS A 1  69   ? 161.760 112.006 123.922 1.00 36.14  ? 69   CYS A O     1 
ATOM   522   C  CB    . CYS A 1  69   ? 164.386 110.867 123.035 1.00 29.32  ? 69   CYS A CB    1 
ATOM   523   S  SG    . CYS A 1  69   ? 164.814 110.210 124.654 1.00 32.53  ? 69   CYS A SG    1 
ATOM   524   N  N     . MET A 1  70   ? 161.301 109.814 124.180 1.00 26.34  ? 70   MET A N     1 
ATOM   525   C  CA    . MET A 1  70   ? 160.258 110.047 125.165 1.00 24.55  ? 70   MET A CA    1 
ATOM   526   C  C     . MET A 1  70   ? 160.771 110.015 126.599 1.00 29.43  ? 70   MET A C     1 
ATOM   527   O  O     . MET A 1  70   ? 160.057 110.456 127.505 1.00 29.91  ? 70   MET A O     1 
ATOM   528   C  CB    . MET A 1  70   ? 159.131 109.024 124.994 1.00 28.79  ? 70   MET A CB    1 
ATOM   529   C  CG    . MET A 1  70   ? 158.662 108.784 123.551 1.00 31.66  ? 70   MET A CG    1 
ATOM   530   S  SD    . MET A 1  70   ? 157.924 110.142 122.598 1.00 39.28  ? 70   MET A SD    1 
ATOM   531   C  CE    . MET A 1  70   ? 157.368 111.299 123.845 1.00 25.81  ? 70   MET A CE    1 
ATOM   532   N  N     . GLY A 1  71   ? 161.986 109.535 126.828 1.00 25.03  ? 71   GLY A N     1 
ATOM   533   C  CA    . GLY A 1  71   ? 162.575 109.537 128.148 1.00 24.28  ? 71   GLY A CA    1 
ATOM   534   C  C     . GLY A 1  71   ? 162.483 108.188 128.838 1.00 27.04  ? 71   GLY A C     1 
ATOM   535   O  O     . GLY A 1  71   ? 161.541 107.421 128.658 1.00 30.31  ? 71   GLY A O     1 
ATOM   536   N  N     . HIS A 1  72   ? 163.492 107.906 129.652 1.00 23.97  ? 72   HIS A N     1 
ATOM   537   C  CA    . HIS A 1  72   ? 163.617 106.634 130.341 1.00 19.25  ? 72   HIS A CA    1 
ATOM   538   C  C     . HIS A 1  72   ? 163.946 106.901 131.800 1.00 21.77  ? 72   HIS A C     1 
ATOM   539   O  O     . HIS A 1  72   ? 164.666 107.853 132.108 1.00 25.70  ? 72   HIS A O     1 
ATOM   540   C  CB    . HIS A 1  72   ? 164.710 105.780 129.689 1.00 24.26  ? 72   HIS A CB    1 
ATOM   541   C  CG    . HIS A 1  72   ? 164.710 105.853 128.193 1.00 22.33  ? 72   HIS A CG    1 
ATOM   542   N  ND1   . HIS A 1  72   ? 163.966 105.007 127.402 1.00 24.41  ? 72   HIS A ND1   1 
ATOM   543   C  CD2   . HIS A 1  72   ? 165.333 106.703 127.347 1.00 22.13  ? 72   HIS A CD2   1 
ATOM   544   C  CE1   . HIS A 1  72   ? 164.147 105.319 126.133 1.00 23.75  ? 72   HIS A CE1   1 
ATOM   545   N  NE2   . HIS A 1  72   ? 164.974 106.345 126.072 1.00 25.59  ? 72   HIS A NE2   1 
ATOM   546   N  N     . PRO A 1  73   ? 163.419 106.100 132.717 1.00 26.80  ? 73   PRO A N     1 
ATOM   547   C  CA    . PRO A 1  73   ? 163.603 106.388 134.141 1.00 20.31  ? 73   PRO A CA    1 
ATOM   548   C  C     . PRO A 1  73   ? 164.892 105.803 134.706 1.00 22.88  ? 73   PRO A C     1 
ATOM   549   O  O     . PRO A 1  73   ? 165.517 104.909 134.139 1.00 27.21  ? 73   PRO A O     1 
ATOM   550   C  CB    . PRO A 1  73   ? 162.376 105.736 134.781 1.00 18.79  ? 73   PRO A CB    1 
ATOM   551   C  CG    . PRO A 1  73   ? 162.073 104.595 133.890 1.00 18.99  ? 73   PRO A CG    1 
ATOM   552   C  CD    . PRO A 1  73   ? 162.453 105.011 132.498 1.00 22.97  ? 73   PRO A CD    1 
ATOM   553   N  N     . GLY A 1  74   ? 165.277 106.331 135.865 1.00 25.82  ? 74   GLY A N     1 
ATOM   554   C  CA    . GLY A 1  74   ? 166.442 105.848 136.566 1.00 25.53  ? 74   GLY A CA    1 
ATOM   555   C  C     . GLY A 1  74   ? 166.106 105.515 138.006 1.00 29.68  ? 74   GLY A C     1 
ATOM   556   O  O     . GLY A 1  74   ? 165.047 105.869 138.520 1.00 33.46  ? 74   GLY A O     1 
ATOM   557   N  N     . ILE A 1  75   ? 167.041 104.826 138.657 1.00 32.30  ? 75   ILE A N     1 
ATOM   558   C  CA    . ILE A 1  75   ? 166.838 104.281 139.994 1.00 31.54  ? 75   ILE A CA    1 
ATOM   559   C  C     . ILE A 1  75   ? 167.759 104.989 140.973 1.00 30.31  ? 75   ILE A C     1 
ATOM   560   O  O     . ILE A 1  75   ? 168.946 105.182 140.697 1.00 32.73  ? 75   ILE A O     1 
ATOM   561   C  CB    . ILE A 1  75   ? 167.089 102.763 140.037 1.00 31.83  ? 75   ILE A CB    1 
ATOM   562   C  CG1   . ILE A 1  75   ? 166.893 102.142 138.657 1.00 34.12  ? 75   ILE A CG1   1 
ATOM   563   C  CG2   . ILE A 1  75   ? 166.165 102.109 141.034 1.00 33.16  ? 75   ILE A CG2   1 
ATOM   564   C  CD1   . ILE A 1  75   ? 167.219 100.673 138.603 1.00 31.76  ? 75   ILE A CD1   1 
ATOM   565   N  N     . LEU A 1  76   ? 167.208 105.381 142.114 1.00 29.13  ? 76   LEU A N     1 
ATOM   566   C  CA    . LEU A 1  76   ? 167.989 105.818 143.265 1.00 31.13  ? 76   LEU A CA    1 
ATOM   567   C  C     . LEU A 1  76   ? 167.820 104.769 144.354 1.00 31.88  ? 76   LEU A C     1 
ATOM   568   O  O     . LEU A 1  76   ? 166.697 104.498 144.787 1.00 33.66  ? 76   LEU A O     1 
ATOM   569   C  CB    . LEU A 1  76   ? 167.539 107.193 143.753 1.00 30.04  ? 76   LEU A CB    1 
ATOM   570   C  CG    . LEU A 1  76   ? 168.136 107.673 145.071 1.00 28.83  ? 76   LEU A CG    1 
ATOM   571   C  CD1   . LEU A 1  76   ? 169.640 107.708 144.972 1.00 28.32  ? 76   LEU A CD1   1 
ATOM   572   C  CD2   . LEU A 1  76   ? 167.599 109.035 145.442 1.00 28.59  ? 76   LEU A CD2   1 
ATOM   573   N  N     . GLN A 1  77   ? 168.927 104.179 144.798 1.00 36.75  ? 77   GLN A N     1 
ATOM   574   C  CA    . GLN A 1  77   ? 168.886 103.203 145.884 1.00 32.55  ? 77   GLN A CA    1 
ATOM   575   C  C     . GLN A 1  77   ? 168.950 103.944 147.207 1.00 35.30  ? 77   GLN A C     1 
ATOM   576   O  O     . GLN A 1  77   ? 169.955 104.573 147.535 1.00 37.91  ? 77   GLN A O     1 
ATOM   577   C  CB    . GLN A 1  77   ? 170.018 102.193 145.760 1.00 31.86  ? 77   GLN A CB    1 
ATOM   578   C  CG    . GLN A 1  77   ? 169.899 101.306 144.551 1.00 35.07  ? 77   GLN A CG    1 
ATOM   579   C  CD    . GLN A 1  77   ? 169.242 99.988  144.874 1.00 39.99  ? 77   GLN A CD    1 
ATOM   580   O  OE1   . GLN A 1  77   ? 168.634 99.832  145.930 1.00 38.23  ? 77   GLN A OE1   1 
ATOM   581   N  NE2   . GLN A 1  77   ? 169.336 99.035  143.956 1.00 38.33  ? 77   GLN A NE2   1 
ATOM   582   N  N     . MET A 1  78   ? 167.858 103.892 147.960 1.00 36.01  ? 78   MET A N     1 
ATOM   583   C  CA    . MET A 1  78   ? 167.773 104.625 149.210 1.00 36.58  ? 78   MET A CA    1 
ATOM   584   C  C     . MET A 1  78   ? 168.567 103.919 150.300 1.00 40.59  ? 78   MET A C     1 
ATOM   585   O  O     . MET A 1  78   ? 168.650 102.691 150.337 1.00 41.83  ? 78   MET A O     1 
ATOM   586   C  CB    . MET A 1  78   ? 166.312 104.773 149.624 1.00 37.49  ? 78   MET A CB    1 
ATOM   587   C  CG    . MET A 1  78   ? 165.518 105.702 148.735 1.00 37.22  ? 78   MET A CG    1 
ATOM   588   S  SD    . MET A 1  78   ? 166.064 107.408 148.823 1.00 45.67  ? 78   MET A SD    1 
ATOM   589   C  CE    . MET A 1  78   ? 164.668 108.159 149.638 1.00 37.46  ? 78   MET A CE    1 
ATOM   590   N  N     . HIS A 1  79   ? 169.176 104.707 151.185 1.00 44.97  ? 79   HIS A N     1 
ATOM   591   C  CA    . HIS A 1  79   ? 169.904 104.121 152.304 1.00 43.05  ? 79   HIS A CA    1 
ATOM   592   C  C     . HIS A 1  79   ? 168.956 103.581 153.367 1.00 45.29  ? 79   HIS A C     1 
ATOM   593   O  O     . HIS A 1  79   ? 169.233 102.537 153.965 1.00 45.27  ? 79   HIS A O     1 
ATOM   594   C  CB    . HIS A 1  79   ? 170.853 105.155 152.900 1.00 44.57  ? 79   HIS A CB    1 
ATOM   595   C  CG    . HIS A 1  79   ? 172.098 105.358 152.096 1.00 46.70  ? 79   HIS A CG    1 
ATOM   596   N  ND1   . HIS A 1  79   ? 172.743 106.573 152.017 1.00 43.24  ? 79   HIS A ND1   1 
ATOM   597   C  CD2   . HIS A 1  79   ? 172.808 104.504 151.322 1.00 44.05  ? 79   HIS A CD2   1 
ATOM   598   C  CE1   . HIS A 1  79   ? 173.799 106.457 151.233 1.00 43.20  ? 79   HIS A CE1   1 
ATOM   599   N  NE2   . HIS A 1  79   ? 173.861 105.212 150.798 1.00 43.36  ? 79   HIS A NE2   1 
ATOM   600   N  N     . ALA A 1  80   ? 167.839 104.266 153.607 1.00 41.50  ? 80   ALA A N     1 
ATOM   601   C  CA    . ALA A 1  80   ? 166.811 103.819 154.531 1.00 39.67  ? 80   ALA A CA    1 
ATOM   602   C  C     . ALA A 1  80   ? 165.462 103.772 153.826 1.00 42.12  ? 80   ALA A C     1 
ATOM   603   O  O     . ALA A 1  80   ? 165.157 104.667 153.025 1.00 43.62  ? 80   ALA A O     1 
ATOM   604   C  CB    . ALA A 1  80   ? 166.729 104.743 155.747 1.00 40.04  ? 80   ALA A CB    1 
ATOM   605   N  N     . PRO A 1  81   ? 164.642 102.753 154.076 1.00 38.50  ? 81   PRO A N     1 
ATOM   606   C  CA    . PRO A 1  81   ? 163.342 102.660 153.402 1.00 34.46  ? 81   PRO A CA    1 
ATOM   607   C  C     . PRO A 1  81   ? 162.425 103.827 153.730 1.00 36.79  ? 81   PRO A C     1 
ATOM   608   O  O     . PRO A 1  81   ? 162.518 104.444 154.792 1.00 38.65  ? 81   PRO A O     1 
ATOM   609   C  CB    . PRO A 1  81   ? 162.758 101.343 153.925 1.00 35.00  ? 81   PRO A CB    1 
ATOM   610   C  CG    . PRO A 1  81   ? 163.844 100.652 154.654 1.00 36.93  ? 81   PRO A CG    1 
ATOM   611   C  CD    . PRO A 1  81   ? 165.088 101.458 154.608 1.00 38.26  ? 81   PRO A CD    1 
ATOM   612   N  N     . VAL A 1  82   ? 161.524 104.122 152.793 1.00 32.89  ? 82   VAL A N     1 
ATOM   613   C  CA    . VAL A 1  82   ? 160.523 105.172 152.943 1.00 31.24  ? 82   VAL A CA    1 
ATOM   614   C  C     . VAL A 1  82   ? 159.145 104.570 152.709 1.00 32.24  ? 82   VAL A C     1 
ATOM   615   O  O     . VAL A 1  82   ? 159.020 103.489 152.125 1.00 34.23  ? 82   VAL A O     1 
ATOM   616   C  CB    . VAL A 1  82   ? 160.768 106.344 151.970 1.00 27.77  ? 82   VAL A CB    1 
ATOM   617   C  CG1   . VAL A 1  82   ? 161.921 107.190 152.437 1.00 29.30  ? 82   VAL A CG1   1 
ATOM   618   C  CG2   . VAL A 1  82   ? 161.025 105.830 150.575 1.00 29.26  ? 82   VAL A CG2   1 
ATOM   619   N  N     . LEU A 1  83   ? 158.114 105.257 153.190 1.00 30.66  ? 83   LEU A N     1 
ATOM   620   C  CA    . LEU A 1  83   ? 156.745 104.869 152.884 1.00 29.81  ? 83   LEU A CA    1 
ATOM   621   C  C     . LEU A 1  83   ? 156.311 105.485 151.562 1.00 34.32  ? 83   LEU A C     1 
ATOM   622   O  O     . LEU A 1  83   ? 156.858 106.499 151.125 1.00 39.55  ? 83   LEU A O     1 
ATOM   623   C  CB    . LEU A 1  83   ? 155.797 105.315 153.997 1.00 30.15  ? 83   LEU A CB    1 
ATOM   624   C  CG    . LEU A 1  83   ? 156.020 104.803 155.418 1.00 32.34  ? 83   LEU A CG    1 
ATOM   625   C  CD1   . LEU A 1  83   ? 154.956 105.362 156.331 1.00 30.69  ? 83   LEU A CD1   1 
ATOM   626   C  CD2   . LEU A 1  83   ? 156.025 103.291 155.461 1.00 32.21  ? 83   LEU A CD2   1 
ATOM   627   N  N     . GLN A 1  84   ? 155.323 104.871 150.924 1.00 31.20  ? 84   GLN A N     1 
ATOM   628   C  CA    . GLN A 1  84   ? 154.773 105.427 149.693 1.00 29.17  ? 84   GLN A CA    1 
ATOM   629   C  C     . GLN A 1  84   ? 153.842 106.586 150.010 1.00 30.69  ? 84   GLN A C     1 
ATOM   630   O  O     . GLN A 1  84   ? 152.830 106.383 150.687 1.00 33.00  ? 84   GLN A O     1 
ATOM   631   C  CB    . GLN A 1  84   ? 154.024 104.365 148.909 1.00 30.83  ? 84   GLN A CB    1 
ATOM   632   C  CG    . GLN A 1  84   ? 154.841 103.168 148.547 1.00 30.78  ? 84   GLN A CG    1 
ATOM   633   C  CD    . GLN A 1  84   ? 154.602 102.769 147.130 1.00 28.28  ? 84   GLN A CD    1 
ATOM   634   O  OE1   . GLN A 1  84   ? 154.196 103.590 146.322 1.00 33.10  ? 84   GLN A OE1   1 
ATOM   635   N  NE2   . GLN A 1  84   ? 154.861 101.513 146.807 1.00 27.10  ? 84   GLN A NE2   1 
ATOM   636   N  N     . PRO A 1  85   ? 154.128 107.798 149.538 1.00 27.02  ? 85   PRO A N     1 
ATOM   637   C  CA    . PRO A 1  85   ? 153.300 108.950 149.917 1.00 27.84  ? 85   PRO A CA    1 
ATOM   638   C  C     . PRO A 1  85   ? 151.840 108.850 149.493 1.00 27.22  ? 85   PRO A C     1 
ATOM   639   O  O     . PRO A 1  85   ? 150.975 109.419 150.167 1.00 28.53  ? 85   PRO A O     1 
ATOM   640   C  CB    . PRO A 1  85   ? 154.017 110.119 149.227 1.00 26.49  ? 85   PRO A CB    1 
ATOM   641   C  CG    . PRO A 1  85   ? 155.400 109.654 149.039 1.00 26.77  ? 85   PRO A CG    1 
ATOM   642   C  CD    . PRO A 1  85   ? 155.303 108.201 148.756 1.00 27.62  ? 85   PRO A CD    1 
ATOM   643   N  N     . LEU A 1  86   ? 151.533 108.167 148.391 1.00 23.37  ? 86   LEU A N     1 
ATOM   644   C  CA    . LEU A 1  86   ? 150.150 108.126 147.921 1.00 25.23  ? 86   LEU A CA    1 
ATOM   645   C  C     . LEU A 1  86   ? 149.288 107.179 148.745 1.00 27.76  ? 86   LEU A C     1 
ATOM   646   O  O     . LEU A 1  86   ? 148.073 107.371 148.834 1.00 27.70  ? 86   LEU A O     1 
ATOM   647   C  CB    . LEU A 1  86   ? 150.104 107.722 146.449 1.00 25.57  ? 86   LEU A CB    1 
ATOM   648   C  CG    . LEU A 1  86   ? 149.668 108.775 145.434 1.00 24.99  ? 86   LEU A CG    1 
ATOM   649   C  CD1   . LEU A 1  86   ? 150.483 110.035 145.579 1.00 25.76  ? 86   LEU A CD1   1 
ATOM   650   C  CD2   . LEU A 1  86   ? 149.783 108.221 144.037 1.00 27.24  ? 86   LEU A CD2   1 
ATOM   651   N  N     . PHE A 1  87   ? 149.888 106.159 149.349 1.00 29.24  ? 87   PHE A N     1 
ATOM   652   C  CA    . PHE A 1  87   ? 149.154 105.081 149.994 1.00 29.91  ? 87   PHE A CA    1 
ATOM   653   C  C     . PHE A 1  87   ? 149.358 105.056 151.508 1.00 31.65  ? 87   PHE A C     1 
ATOM   654   O  O     . PHE A 1  87   ? 149.389 103.989 152.125 1.00 33.94  ? 87   PHE A O     1 
ATOM   655   C  CB    . PHE A 1  87   ? 149.547 103.756 149.347 1.00 30.36  ? 87   PHE A CB    1 
ATOM   656   C  CG    . PHE A 1  87   ? 149.530 103.805 147.846 1.00 31.79  ? 87   PHE A CG    1 
ATOM   657   C  CD1   . PHE A 1  87   ? 150.703 103.813 147.123 1.00 30.71  ? 87   PHE A CD1   1 
ATOM   658   C  CD2   . PHE A 1  87   ? 148.331 103.852 147.157 1.00 29.81  ? 87   PHE A CD2   1 
ATOM   659   C  CE1   . PHE A 1  87   ? 150.683 103.873 145.752 1.00 28.40  ? 87   PHE A CE1   1 
ATOM   660   C  CE2   . PHE A 1  87   ? 148.310 103.905 145.784 1.00 27.34  ? 87   PHE A CE2   1 
ATOM   661   C  CZ    . PHE A 1  87   ? 149.488 103.913 145.082 1.00 27.66  ? 87   PHE A CZ    1 
ATOM   662   N  N     . ILE A 1  88   ? 149.454 106.234 152.123 1.00 32.82  ? 88   ILE A N     1 
ATOM   663   C  CA    . ILE A 1  88   ? 149.597 106.313 153.574 1.00 34.92  ? 88   ILE A CA    1 
ATOM   664   C  C     . ILE A 1  88   ? 148.364 105.750 154.270 1.00 33.83  ? 88   ILE A C     1 
ATOM   665   O  O     . ILE A 1  88   ? 148.472 105.034 155.270 1.00 34.26  ? 88   ILE A O     1 
ATOM   666   C  CB    . ILE A 1  88   ? 149.885 107.761 154.007 1.00 33.93  ? 88   ILE A CB    1 
ATOM   667   C  CG1   . ILE A 1  88   ? 151.338 108.120 153.714 1.00 32.17  ? 88   ILE A CG1   1 
ATOM   668   C  CG2   . ILE A 1  88   ? 149.595 107.950 155.473 1.00 35.32  ? 88   ILE A CG2   1 
ATOM   669   C  CD1   . ILE A 1  88   ? 152.287 106.977 153.916 1.00 31.01  ? 88   ILE A CD1   1 
ATOM   670   N  N     . ALA A 1  89   ? 147.173 106.072 153.763 1.00 34.04  ? 89   ALA A N     1 
ATOM   671   C  CA    . ALA A 1  89   ? 145.953 105.563 154.379 1.00 32.89  ? 89   ALA A CA    1 
ATOM   672   C  C     . ALA A 1  89   ? 145.857 104.051 154.228 1.00 33.78  ? 89   ALA A C     1 
ATOM   673   O  O     . ALA A 1  89   ? 145.362 103.354 155.118 1.00 36.15  ? 89   ALA A O     1 
ATOM   674   C  CB    . ALA A 1  89   ? 144.733 106.252 153.778 1.00 30.65  ? 89   ALA A CB    1 
ATOM   675   N  N     . GLU A 1  90   ? 146.334 103.526 153.103 1.00 35.49  ? 90   GLU A N     1 
ATOM   676   C  CA    . GLU A 1  90   ? 146.356 102.083 152.905 1.00 33.08  ? 90   GLU A CA    1 
ATOM   677   C  C     . GLU A 1  90   ? 147.291 101.417 153.904 1.00 34.98  ? 90   GLU A C     1 
ATOM   678   O  O     . GLU A 1  90   ? 146.989 100.350 154.451 1.00 34.99  ? 90   GLU A O     1 
ATOM   679   C  CB    . GLU A 1  90   ? 146.769 101.780 151.465 1.00 29.70  ? 90   GLU A CB    1 
ATOM   680   C  CG    . GLU A 1  90   ? 146.766 100.325 151.077 1.00 32.02  ? 90   GLU A CG    1 
ATOM   681   C  CD    . GLU A 1  90   ? 145.376 99.750  150.944 1.00 34.44  ? 90   GLU A CD    1 
ATOM   682   O  OE1   . GLU A 1  90   ? 144.395 100.517 151.014 1.00 35.81  ? 90   GLU A OE1   1 
ATOM   683   O  OE2   . GLU A 1  90   ? 145.269 98.528  150.732 1.00 35.00  ? 90   GLU A OE2   1 
ATOM   684   N  N     . ILE A 1  91   ? 148.441 102.048 154.156 1.00 37.22  ? 91   ILE A N     1 
ATOM   685   C  CA    . ILE A 1  91   ? 149.371 101.547 155.167 1.00 33.76  ? 91   ILE A CA    1 
ATOM   686   C  C     . ILE A 1  91   ? 148.718 101.572 156.543 1.00 35.99  ? 91   ILE A C     1 
ATOM   687   O  O     . ILE A 1  91   ? 148.801 100.607 157.311 1.00 33.38  ? 91   ILE A O     1 
ATOM   688   C  CB    . ILE A 1  91   ? 150.667 102.374 155.151 1.00 31.71  ? 91   ILE A CB    1 
ATOM   689   C  CG1   . ILE A 1  91   ? 151.349 102.262 153.789 1.00 32.17  ? 91   ILE A CG1   1 
ATOM   690   C  CG2   . ILE A 1  91   ? 151.593 101.926 156.270 1.00 32.18  ? 91   ILE A CG2   1 
ATOM   691   C  CD1   . ILE A 1  91   ? 152.810 102.588 153.800 1.00 34.34  ? 91   ILE A CD1   1 
ATOM   692   N  N     . ARG A 1  92   ? 148.051 102.681 156.864 1.00 38.15  ? 92   ARG A N     1 
ATOM   693   C  CA    . ARG A 1  92   ? 147.415 102.834 158.167 1.00 36.42  ? 92   ARG A CA    1 
ATOM   694   C  C     . ARG A 1  92   ? 146.363 101.763 158.389 1.00 37.95  ? 92   ARG A C     1 
ATOM   695   O  O     . ARG A 1  92   ? 146.298 101.142 159.453 1.00 42.12  ? 92   ARG A O     1 
ATOM   696   C  CB    . ARG A 1  92   ? 146.791 104.225 158.278 1.00 36.19  ? 92   ARG A CB    1 
ATOM   697   C  CG    . ARG A 1  92   ? 146.208 104.535 159.639 1.00 37.04  ? 92   ARG A CG    1 
ATOM   698   C  CD    . ARG A 1  92   ? 144.696 104.649 159.602 1.00 37.92  ? 92   ARG A CD    1 
ATOM   699   N  NE    . ARG A 1  92   ? 144.229 105.850 158.916 1.00 42.23  ? 92   ARG A NE    1 
ATOM   700   C  CZ    . ARG A 1  92   ? 143.560 105.854 157.770 1.00 39.82  ? 92   ARG A CZ    1 
ATOM   701   N  NH1   . ARG A 1  92   ? 143.257 104.732 157.141 1.00 38.61  ? 92   ARG A NH1   1 
ATOM   702   N  NH2   . ARG A 1  92   ? 143.174 107.014 157.249 1.00 35.94  ? 92   ARG A NH2   1 
ATOM   703   N  N     . ARG A 1  93   ? 145.532 101.533 157.390 1.00 37.93  ? 93   ARG A N     1 
ATOM   704   C  CA    . ARG A 1  93   ? 144.449 100.576 157.502 1.00 37.07  ? 93   ARG A CA    1 
ATOM   705   C  C     . ARG A 1  93   ? 144.918 99.135  157.343 1.00 34.61  ? 93   ARG A C     1 
ATOM   706   O  O     . ARG A 1  93   ? 144.158 98.216  157.656 1.00 37.88  ? 93   ARG A O     1 
ATOM   707   C  CB    . ARG A 1  93   ? 143.369 100.950 156.482 1.00 35.13  ? 93   ARG A CB    1 
ATOM   708   C  CG    . ARG A 1  93   ? 143.347 100.136 155.229 1.00 34.77  ? 93   ARG A CG    1 
ATOM   709   C  CD    . ARG A 1  93   ? 142.016 100.297 154.530 1.00 37.49  ? 93   ARG A CD    1 
ATOM   710   N  NE    . ARG A 1  93   ? 141.704 101.688 154.244 1.00 38.09  ? 93   ARG A NE    1 
ATOM   711   C  CZ    . ARG A 1  93   ? 142.032 102.307 153.120 1.00 37.56  ? 93   ARG A CZ    1 
ATOM   712   N  NH1   . ARG A 1  93   ? 142.688 101.685 152.155 1.00 35.40  ? 93   ARG A NH1   1 
ATOM   713   N  NH2   . ARG A 1  93   ? 141.694 103.582 152.960 1.00 37.15  ? 93   ARG A NH2   1 
ATOM   714   N  N     . TRP A 1  94   ? 146.150 98.911  156.892 1.00 35.49  ? 94   TRP A N     1 
ATOM   715   C  CA    . TRP A 1  94   ? 146.723 97.571  156.901 1.00 37.44  ? 94   TRP A CA    1 
ATOM   716   C  C     . TRP A 1  94   ? 147.304 97.176  158.248 1.00 41.86  ? 94   TRP A C     1 
ATOM   717   O  O     . TRP A 1  94   ? 147.351 95.982  158.558 1.00 42.91  ? 94   TRP A O     1 
ATOM   718   C  CB    . TRP A 1  94   ? 147.831 97.447  155.853 1.00 38.43  ? 94   TRP A CB    1 
ATOM   719   C  CG    . TRP A 1  94   ? 147.397 96.820  154.587 1.00 37.57  ? 94   TRP A CG    1 
ATOM   720   C  CD1   . TRP A 1  94   ? 147.232 97.440  153.392 1.00 37.94  ? 94   TRP A CD1   1 
ATOM   721   C  CD2   . TRP A 1  94   ? 147.069 95.448  154.378 1.00 40.26  ? 94   TRP A CD2   1 
ATOM   722   N  NE1   . TRP A 1  94   ? 146.823 96.541  152.445 1.00 41.34  ? 94   TRP A NE1   1 
ATOM   723   C  CE2   . TRP A 1  94   ? 146.714 95.307  153.026 1.00 42.00  ? 94   TRP A CE2   1 
ATOM   724   C  CE3   . TRP A 1  94   ? 147.040 94.323  155.203 1.00 38.61  ? 94   TRP A CE3   1 
ATOM   725   C  CZ2   . TRP A 1  94   ? 146.335 94.088  152.477 1.00 37.63  ? 94   TRP A CZ2   1 
ATOM   726   C  CZ3   . TRP A 1  94   ? 146.662 93.112  154.656 1.00 41.49  ? 94   TRP A CZ3   1 
ATOM   727   C  CH2   . TRP A 1  94   ? 146.315 93.004  153.306 1.00 38.74  ? 94   TRP A CH2   1 
ATOM   728   N  N     . LEU A 1  95   ? 147.776 98.139  159.041 1.00 41.02  ? 95   LEU A N     1 
ATOM   729   C  CA    . LEU A 1  95   ? 148.343 97.830  160.345 1.00 39.07  ? 95   LEU A CA    1 
ATOM   730   C  C     . LEU A 1  95   ? 147.294 97.385  161.352 1.00 41.51  ? 95   LEU A C     1 
ATOM   731   O  O     . LEU A 1  95   ? 147.618 96.609  162.255 1.00 41.80  ? 95   LEU A O     1 
ATOM   732   C  CB    . LEU A 1  95   ? 149.087 99.047  160.905 1.00 36.80  ? 95   LEU A CB    1 
ATOM   733   C  CG    . LEU A 1  95   ? 150.435 99.454  160.304 1.00 38.67  ? 95   LEU A CG    1 
ATOM   734   C  CD1   . LEU A 1  95   ? 150.875 100.803 160.847 1.00 37.98  ? 95   LEU A CD1   1 
ATOM   735   C  CD2   . LEU A 1  95   ? 151.497 98.407  160.551 1.00 34.82  ? 95   LEU A CD2   1 
ATOM   736   N  N     . ARG A 1  96   ? 146.049 97.831  161.211 1.00 41.33  ? 96   ARG A N     1 
ATOM   737   C  CA    . ARG A 1  96   ? 145.031 97.543  162.208 1.00 41.97  ? 96   ARG A CA    1 
ATOM   738   C  C     . ARG A 1  96   ? 144.400 96.169  162.058 1.00 41.93  ? 96   ARG A C     1 
ATOM   739   O  O     . ARG A 1  96   ? 143.575 95.799  162.896 1.00 43.93  ? 96   ARG A O     1 
ATOM   740   C  CB    . ARG A 1  96   ? 143.913 98.590  162.163 1.00 42.22  ? 96   ARG A CB    1 
ATOM   741   C  CG    . ARG A 1  96   ? 144.358 100.033 162.140 1.00 39.81  ? 96   ARG A CG    1 
ATOM   742   C  CD    . ARG A 1  96   ? 143.134 100.931 162.225 1.00 41.73  ? 96   ARG A CD    1 
ATOM   743   N  NE    . ARG A 1  96   ? 143.318 102.046 163.145 1.00 42.92  ? 96   ARG A NE    1 
ATOM   744   C  CZ    . ARG A 1  96   ? 143.047 103.310 162.854 1.00 46.25  ? 96   ARG A CZ    1 
ATOM   745   N  NH1   . ARG A 1  96   ? 142.541 103.658 161.684 1.00 45.68  ? 96   ARG A NH1   1 
ATOM   746   N  NH2   . ARG A 1  96   ? 143.273 104.249 163.768 1.00 42.80  ? 96   ARG A NH2   1 
ATOM   747   N  N     . VAL A 1  97   ? 144.749 95.408  161.023 1.00 37.47  ? 97   VAL A N     1 
ATOM   748   C  CA    . VAL A 1  97   ? 144.084 94.142  160.748 1.00 41.20  ? 97   VAL A CA    1 
ATOM   749   C  C     . VAL A 1  97   ? 145.027 92.950  160.767 1.00 41.86  ? 97   VAL A C     1 
ATOM   750   O  O     . VAL A 1  97   ? 144.574 91.823  160.554 1.00 44.21  ? 97   VAL A O     1 
ATOM   751   C  CB    . VAL A 1  97   ? 143.315 94.186  159.411 1.00 43.46  ? 97   VAL A CB    1 
ATOM   752   C  CG1   . VAL A 1  97   ? 142.365 95.371  159.383 1.00 39.85  ? 97   VAL A CG1   1 
ATOM   753   C  CG2   . VAL A 1  97   ? 144.277 94.226  158.245 1.00 39.56  ? 97   VAL A CG2   1 
ATOM   754   N  N     . ILE A 1  98   ? 146.325 93.152  160.997 1.00 41.17  ? 98   ILE A N     1 
ATOM   755   C  CA    . ILE A 1  98   ? 147.267 92.043  161.068 1.00 43.37  ? 98   ILE A CA    1 
ATOM   756   C  C     . ILE A 1  98   ? 148.142 92.189  162.307 1.00 45.11  ? 98   ILE A C     1 
ATOM   757   O  O     . ILE A 1  98   ? 148.262 93.267  162.892 1.00 44.95  ? 98   ILE A O     1 
ATOM   758   C  CB    . ILE A 1  98   ? 148.136 91.920  159.795 1.00 44.36  ? 98   ILE A CB    1 
ATOM   759   C  CG1   . ILE A 1  98   ? 148.915 93.207  159.535 1.00 43.25  ? 98   ILE A CG1   1 
ATOM   760   C  CG2   . ILE A 1  98   ? 147.288 91.525  158.593 1.00 43.43  ? 98   ILE A CG2   1 
ATOM   761   C  CD1   . ILE A 1  98   ? 150.381 93.083  159.848 1.00 41.84  ? 98   ILE A CD1   1 
ATOM   762   N  N     . CYS A 1  99   ? 148.752 91.074  162.707 1.00 45.00  ? 99   CYS A N     1 
ATOM   763   C  CA    . CYS A 1  99   ? 149.526 91.021  163.940 1.00 43.44  ? 99   CYS A CA    1 
ATOM   764   C  C     . CYS A 1  99   ? 150.920 91.596  163.730 1.00 44.13  ? 99   CYS A C     1 
ATOM   765   O  O     . CYS A 1  99   ? 151.606 91.252  162.765 1.00 45.12  ? 99   CYS A O     1 
ATOM   766   C  CB    . CYS A 1  99   ? 149.624 89.581  164.440 1.00 45.67  ? 99   CYS A CB    1 
ATOM   767   S  SG    . CYS A 1  99   ? 150.337 89.388  166.089 1.00 52.58  ? 99   CYS A SG    1 
ATOM   768   N  N     . LEU A 1  100  ? 151.353 92.445  164.660 1.00 43.36  ? 100  LEU A N     1 
ATOM   769   C  CA    . LEU A 1  100  ? 152.656 93.087  164.551 1.00 43.16  ? 100  LEU A CA    1 
ATOM   770   C  C     . LEU A 1  100  ? 153.819 92.136  164.794 1.00 44.05  ? 100  LEU A C     1 
ATOM   771   O  O     . LEU A 1  100  ? 154.966 92.525  164.556 1.00 44.03  ? 100  LEU A O     1 
ATOM   772   C  CB    . LEU A 1  100  ? 152.752 94.256  165.529 1.00 40.22  ? 100  LEU A CB    1 
ATOM   773   C  CG    . LEU A 1  100  ? 152.180 95.605  165.104 1.00 41.53  ? 100  LEU A CG    1 
ATOM   774   C  CD1   . LEU A 1  100  ? 150.681 95.619  165.183 1.00 38.95  ? 100  LEU A CD1   1 
ATOM   775   C  CD2   . LEU A 1  100  ? 152.773 96.711  165.957 1.00 44.47  ? 100  LEU A CD2   1 
ATOM   776   N  N     . ASN A 1  101  ? 153.566 90.917  165.266 1.00 46.01  ? 101  ASN A N     1 
ATOM   777   C  CA    . ASN A 1  101  ? 154.639 89.977  165.564 1.00 45.13  ? 101  ASN A CA    1 
ATOM   778   C  C     . ASN A 1  101  ? 154.670 88.751  164.668 1.00 48.10  ? 101  ASN A C     1 
ATOM   779   O  O     . ASN A 1  101  ? 155.754 88.228  164.412 1.00 49.71  ? 101  ASN A O     1 
ATOM   780   C  CB    . ASN A 1  101  ? 154.555 89.517  167.026 1.00 42.45  ? 101  ASN A CB    1 
ATOM   781   C  CG    . ASN A 1  101  ? 155.296 90.447  167.969 1.00 47.13  ? 101  ASN A CG    1 
ATOM   782   O  OD1   . ASN A 1  101  ? 156.493 90.682  167.810 1.00 47.47  ? 101  ASN A OD1   1 
ATOM   783   N  ND2   . ASN A 1  101  ? 154.582 91.000  168.943 1.00 47.80  ? 101  ASN A ND2   1 
ATOM   784   N  N     . CYS A 1  102  ? 153.527 88.274  164.180 1.00 45.47  ? 102  CYS A N     1 
ATOM   785   C  CA    . CYS A 1  102  ? 153.546 87.041  163.401 1.00 43.88  ? 102  CYS A CA    1 
ATOM   786   C  C     . CYS A 1  102  ? 152.972 87.223  162.001 1.00 45.98  ? 102  CYS A C     1 
ATOM   787   O  O     . CYS A 1  102  ? 153.297 86.451  161.094 1.00 48.33  ? 102  CYS A O     1 
ATOM   788   C  CB    . CYS A 1  102  ? 152.803 85.931  164.147 1.00 44.46  ? 102  CYS A CB    1 
ATOM   789   S  SG    . CYS A 1  102  ? 151.136 86.333  164.686 1.00 47.72  ? 102  CYS A SG    1 
ATOM   790   N  N     . GLY A 1  103  ? 152.134 88.237  161.802 1.00 43.59  ? 103  GLY A N     1 
ATOM   791   C  CA    . GLY A 1  103  ? 151.596 88.543  160.499 1.00 43.29  ? 103  GLY A CA    1 
ATOM   792   C  C     . GLY A 1  103  ? 150.274 87.877  160.181 1.00 44.75  ? 103  GLY A C     1 
ATOM   793   O  O     . GLY A 1  103  ? 149.699 88.150  159.120 1.00 45.80  ? 103  GLY A O     1 
ATOM   794   N  N     . ALA A 1  104  ? 149.795 86.993  161.045 1.00 39.08  ? 104  ALA A N     1 
ATOM   795   C  CA    . ALA A 1  104  ? 148.455 86.458  160.886 1.00 37.93  ? 104  ALA A CA    1 
ATOM   796   C  C     . ALA A 1  104  ? 147.428 87.538  161.224 1.00 37.88  ? 104  ALA A C     1 
ATOM   797   O  O     . ALA A 1  104  ? 147.721 88.446  162.006 1.00 37.23  ? 104  ALA A O     1 
ATOM   798   C  CB    . ALA A 1  104  ? 148.265 85.239  161.785 1.00 40.13  ? 104  ALA A CB    1 
ATOM   799   N  N     . PRO A 1  105  ? 146.225 87.479  160.655 1.00 38.87  ? 105  PRO A N     1 
ATOM   800   C  CA    . PRO A 1  105  ? 145.232 88.510  160.959 1.00 38.39  ? 105  PRO A CA    1 
ATOM   801   C  C     . PRO A 1  105  ? 144.610 88.302  162.327 1.00 40.91  ? 105  PRO A C     1 
ATOM   802   O  O     . PRO A 1  105  ? 144.478 87.177  162.813 1.00 41.54  ? 105  PRO A O     1 
ATOM   803   C  CB    . PRO A 1  105  ? 144.193 88.344  159.846 1.00 36.18  ? 105  PRO A CB    1 
ATOM   804   C  CG    . PRO A 1  105  ? 144.413 86.968  159.292 1.00 36.29  ? 105  PRO A CG    1 
ATOM   805   C  CD    . PRO A 1  105  ? 145.618 86.353  159.930 1.00 37.70  ? 105  PRO A CD    1 
ATOM   806   N  N     . ILE A 1  106  ? 144.225 89.408  162.952 1.00 39.48  ? 106  ILE A N     1 
ATOM   807   C  CA    . ILE A 1  106  ? 143.575 89.335  164.253 1.00 40.21  ? 106  ILE A CA    1 
ATOM   808   C  C     . ILE A 1  106  ? 142.061 89.380  164.118 1.00 41.48  ? 106  ILE A C     1 
ATOM   809   O  O     . ILE A 1  106  ? 141.340 88.931  165.012 1.00 43.16  ? 106  ILE A O     1 
ATOM   810   C  CB    . ILE A 1  106  ? 144.091 90.456  165.172 1.00 40.07  ? 106  ILE A CB    1 
ATOM   811   C  CG1   . ILE A 1  106  ? 143.976 91.807  164.481 1.00 42.58  ? 106  ILE A CG1   1 
ATOM   812   C  CG2   . ILE A 1  106  ? 145.531 90.181  165.576 1.00 40.71  ? 106  ILE A CG2   1 
ATOM   813   C  CD1   . ILE A 1  106  ? 144.165 92.966  165.414 1.00 43.96  ? 106  ILE A CD1   1 
ATOM   814   N  N     . VAL A 1  107  ? 141.556 89.923  163.016 1.00 41.53  ? 107  VAL A N     1 
ATOM   815   C  CA    . VAL A 1  107  ? 140.119 89.974  162.782 1.00 41.17  ? 107  VAL A CA    1 
ATOM   816   C  C     . VAL A 1  107  ? 139.635 88.615  162.299 1.00 40.03  ? 107  VAL A C     1 
ATOM   817   O  O     . VAL A 1  107  ? 140.439 87.739  161.958 1.00 38.30  ? 107  VAL A O     1 
ATOM   818   C  CB    . VAL A 1  107  ? 139.760 91.079  161.776 1.00 42.77  ? 107  VAL A CB    1 
ATOM   819   C  CG1   . VAL A 1  107  ? 140.122 92.440  162.347 1.00 39.70  ? 107  VAL A CG1   1 
ATOM   820   C  CG2   . VAL A 1  107  ? 140.469 90.836  160.450 1.00 40.93  ? 107  VAL A CG2   1 
ATOM   821   N  N     . ASP A 1  108  ? 138.319 88.422  162.288 1.00 43.06  ? 108  ASP A N     1 
ATOM   822   C  CA    . ASP A 1  108  ? 137.735 87.195  161.768 1.00 45.24  ? 108  ASP A CA    1 
ATOM   823   C  C     . ASP A 1  108  ? 137.646 87.293  160.254 1.00 47.96  ? 108  ASP A C     1 
ATOM   824   O  O     . ASP A 1  108  ? 136.924 88.142  159.723 1.00 47.61  ? 108  ASP A O     1 
ATOM   825   C  CB    . ASP A 1  108  ? 136.357 86.953  162.377 1.00 45.23  ? 108  ASP A CB    1 
ATOM   826   C  CG    . ASP A 1  108  ? 135.967 85.488  162.376 1.00 48.31  ? 108  ASP A CG    1 
ATOM   827   O  OD1   . ASP A 1  108  ? 136.809 84.646  162.003 1.00 50.43  ? 108  ASP A OD1   1 
ATOM   828   O  OD2   . ASP A 1  108  ? 134.818 85.179  162.751 1.00 48.30  ? 108  ASP A OD2   1 
ATOM   829   N  N     . LEU A 1  109  ? 138.387 86.431  159.558 1.00 45.22  ? 109  LEU A N     1 
ATOM   830   C  CA    . LEU A 1  109  ? 138.403 86.496  158.103 1.00 42.91  ? 109  LEU A CA    1 
ATOM   831   C  C     . LEU A 1  109  ? 137.067 86.072  157.510 1.00 45.43  ? 109  LEU A C     1 
ATOM   832   O  O     . LEU A 1  109  ? 136.654 86.600  156.473 1.00 45.31  ? 109  LEU A O     1 
ATOM   833   C  CB    . LEU A 1  109  ? 139.531 85.629  157.549 1.00 38.50  ? 109  LEU A CB    1 
ATOM   834   C  CG    . LEU A 1  109  ? 140.946 86.113  157.854 1.00 43.11  ? 109  LEU A CG    1 
ATOM   835   C  CD1   . LEU A 1  109  ? 141.961 85.036  157.530 1.00 42.47  ? 109  LEU A CD1   1 
ATOM   836   C  CD2   . LEU A 1  109  ? 141.244 87.391  157.090 1.00 43.69  ? 109  LEU A CD2   1 
ATOM   837   N  N     . LYS A 1  110  ? 136.370 85.143  158.161 1.00 46.09  ? 110  LYS A N     1 
ATOM   838   C  CA    . LYS A 1  110  ? 135.104 84.626  157.664 1.00 47.23  ? 110  LYS A CA    1 
ATOM   839   C  C     . LYS A 1  110  ? 133.925 85.460  158.141 1.00 48.69  ? 110  LYS A C     1 
ATOM   840   O  O     . LYS A 1  110  ? 132.802 84.956  158.244 1.00 47.45  ? 110  LYS A O     1 
ATOM   841   C  CB    . LYS A 1  110  ? 134.936 83.166  158.079 1.00 46.33  ? 110  LYS A CB    1 
ATOM   842   C  CG    . LYS A 1  110  ? 135.885 82.230  157.360 1.00 47.29  ? 110  LYS A CG    1 
ATOM   843   C  CD    . LYS A 1  110  ? 135.571 80.781  157.666 1.00 47.60  ? 110  LYS A CD    1 
ATOM   844   C  CE    . LYS A 1  110  ? 136.494 79.849  156.897 1.00 48.73  ? 110  LYS A CE    1 
ATOM   845   N  NZ    . LYS A 1  110  ? 136.245 78.425  157.241 1.00 48.45  ? 110  LYS A NZ    1 
ATOM   846   N  N     . ARG A 1  111  ? 134.165 86.729  158.437 1.00 49.00  ? 111  ARG A N     1 
ATOM   847   C  CA    . ARG A 1  111  ? 133.125 87.674  158.814 1.00 46.97  ? 111  ARG A CA    1 
ATOM   848   C  C     . ARG A 1  111  ? 132.902 88.739  157.757 1.00 48.37  ? 111  ARG A C     1 
ATOM   849   O  O     . ARG A 1  111  ? 131.805 89.294  157.663 1.00 47.26  ? 111  ARG A O     1 
ATOM   850   C  CB    . ARG A 1  111  ? 133.479 88.335  160.158 1.00 45.86  ? 111  ARG A CB    1 
ATOM   851   C  CG    . ARG A 1  111  ? 132.462 89.357  160.635 1.00 48.41  ? 111  ARG A CG    1 
ATOM   852   C  CD    . ARG A 1  111  ? 132.778 89.894  162.019 1.00 48.46  ? 111  ARG A CD    1 
ATOM   853   N  NE    . ARG A 1  111  ? 131.835 90.940  162.395 1.00 50.72  ? 111  ARG A NE    1 
ATOM   854   C  CZ    . ARG A 1  111  ? 131.782 91.515  163.588 1.00 50.07  ? 111  ARG A CZ    1 
ATOM   855   N  NH1   . ARG A 1  111  ? 132.617 91.176  164.556 1.00 46.67  ? 111  ARG A NH1   1 
ATOM   856   N  NH2   . ARG A 1  111  ? 130.861 92.447  163.818 1.00 46.58  ? 111  ARG A NH2   1 
ATOM   857   N  N     . TYR A 1  112  ? 133.917 89.034  156.950 1.00 50.10  ? 112  TYR A N     1 
ATOM   858   C  CA    . TYR A 1  112  ? 133.820 90.050  155.915 1.00 48.49  ? 112  TYR A CA    1 
ATOM   859   C  C     . TYR A 1  112  ? 133.813 89.473  154.508 1.00 47.63  ? 112  TYR A C     1 
ATOM   860   O  O     . TYR A 1  112  ? 133.723 90.238  153.545 1.00 51.11  ? 112  TYR A O     1 
ATOM   861   C  CB    . TYR A 1  112  ? 134.975 91.047  156.046 1.00 47.29  ? 112  TYR A CB    1 
ATOM   862   C  CG    . TYR A 1  112  ? 135.044 91.724  157.392 1.00 46.49  ? 112  TYR A CG    1 
ATOM   863   C  CD1   . TYR A 1  112  ? 134.342 92.891  157.639 1.00 48.26  ? 112  TYR A CD1   1 
ATOM   864   C  CD2   . TYR A 1  112  ? 135.817 91.197  158.413 1.00 45.86  ? 112  TYR A CD2   1 
ATOM   865   C  CE1   . TYR A 1  112  ? 134.401 93.513  158.865 1.00 49.67  ? 112  TYR A CE1   1 
ATOM   866   C  CE2   . TYR A 1  112  ? 135.884 91.811  159.641 1.00 49.51  ? 112  TYR A CE2   1 
ATOM   867   C  CZ    . TYR A 1  112  ? 135.173 92.970  159.863 1.00 50.70  ? 112  TYR A CZ    1 
ATOM   868   O  OH    . TYR A 1  112  ? 135.236 93.588  161.089 1.00 49.61  ? 112  TYR A OH    1 
ATOM   869   N  N     . GLU A 1  113  ? 133.906 88.155  154.356 1.00 46.59  ? 113  GLU A N     1 
ATOM   870   C  CA    . GLU A 1  113  ? 133.974 87.572  153.023 1.00 47.70  ? 113  GLU A CA    1 
ATOM   871   C  C     . GLU A 1  113  ? 132.678 87.735  152.239 1.00 49.30  ? 113  GLU A C     1 
ATOM   872   O  O     . GLU A 1  113  ? 132.693 87.589  151.011 1.00 46.37  ? 113  GLU A O     1 
ATOM   873   C  CB    . GLU A 1  113  ? 134.322 86.087  153.110 1.00 47.27  ? 113  GLU A CB    1 
ATOM   874   C  CG    . GLU A 1  113  ? 133.127 85.159  152.944 1.00 47.73  ? 113  GLU A CG    1 
ATOM   875   C  CD    . GLU A 1  113  ? 132.338 84.967  154.222 1.00 51.60  ? 113  GLU A CD    1 
ATOM   876   O  OE1   . GLU A 1  113  ? 132.439 85.823  155.126 1.00 49.55  ? 113  GLU A OE1   1 
ATOM   877   O  OE2   . GLU A 1  113  ? 131.614 83.951  154.318 1.00 51.92  ? 113  GLU A OE2   1 
ATOM   878   N  N     . HIS A 1  114  ? 131.568 88.041  152.907 1.00 46.11  ? 114  HIS A N     1 
ATOM   879   C  CA    . HIS A 1  114  ? 130.286 88.143  152.228 1.00 46.32  ? 114  HIS A CA    1 
ATOM   880   C  C     . HIS A 1  114  ? 130.112 89.455  151.474 1.00 47.27  ? 114  HIS A C     1 
ATOM   881   O  O     . HIS A 1  114  ? 129.224 89.539  150.618 1.00 48.95  ? 114  HIS A O     1 
ATOM   882   C  CB    . HIS A 1  114  ? 129.146 87.981  153.232 1.00 46.57  ? 114  HIS A CB    1 
ATOM   883   C  CG    . HIS A 1  114  ? 128.944 89.173  154.112 1.00 48.73  ? 114  HIS A CG    1 
ATOM   884   N  ND1   . HIS A 1  114  ? 128.093 90.204  153.780 1.00 48.39  ? 114  HIS A ND1   1 
ATOM   885   C  CD2   . HIS A 1  114  ? 129.483 89.500  155.310 1.00 47.37  ? 114  HIS A CD2   1 
ATOM   886   C  CE1   . HIS A 1  114  ? 128.110 91.113  154.738 1.00 47.12  ? 114  HIS A CE1   1 
ATOM   887   N  NE2   . HIS A 1  114  ? 128.948 90.711  155.677 1.00 47.97  ? 114  HIS A NE2   1 
ATOM   888   N  N     . LEU A 1  115  ? 130.925 90.470  151.749 1.00 43.21  ? 115  LEU A N     1 
ATOM   889   C  CA    . LEU A 1  115  ? 130.816 91.730  151.034 1.00 43.38  ? 115  LEU A CA    1 
ATOM   890   C  C     . LEU A 1  115  ? 131.711 91.723  149.805 1.00 41.91  ? 115  LEU A C     1 
ATOM   891   O  O     . LEU A 1  115  ? 132.532 90.827  149.599 1.00 42.64  ? 115  LEU A O     1 
ATOM   892   C  CB    . LEU A 1  115  ? 131.159 92.923  151.931 1.00 41.80  ? 115  LEU A CB    1 
ATOM   893   C  CG    . LEU A 1  115  ? 130.630 92.902  153.361 1.00 44.06  ? 115  LEU A CG    1 
ATOM   894   C  CD1   . LEU A 1  115  ? 131.686 92.428  154.328 1.00 41.27  ? 115  LEU A CD1   1 
ATOM   895   C  CD2   . LEU A 1  115  ? 130.048 94.250  153.770 1.00 42.08  ? 115  LEU A CD2   1 
ATOM   896   N  N     . ILE A 1  116  ? 131.525 92.742  148.969 1.00 39.16  ? 116  ILE A N     1 
ATOM   897   C  CA    . ILE A 1  116  ? 132.330 92.868  147.767 1.00 39.79  ? 116  ILE A CA    1 
ATOM   898   C  C     . ILE A 1  116  ? 133.773 93.167  148.150 1.00 40.02  ? 116  ILE A C     1 
ATOM   899   O  O     . ILE A 1  116  ? 134.054 93.798  149.177 1.00 38.66  ? 116  ILE A O     1 
ATOM   900   C  CB    . ILE A 1  116  ? 131.753 93.949  146.839 1.00 35.45  ? 116  ILE A CB    1 
ATOM   901   C  CG1   . ILE A 1  116  ? 131.588 95.258  147.595 1.00 35.16  ? 116  ILE A CG1   1 
ATOM   902   C  CG2   . ILE A 1  116  ? 130.417 93.507  146.290 1.00 36.72  ? 116  ILE A CG2   1 
ATOM   903   C  CD1   . ILE A 1  116  ? 131.127 96.392  146.730 1.00 37.43  ? 116  ILE A CD1   1 
ATOM   904   N  N     . ARG A 1  117  ? 134.696 92.705  147.312 1.00 38.34  ? 117  ARG A N     1 
ATOM   905   C  CA    . ARG A 1  117  ? 136.112 92.720  147.671 1.00 37.73  ? 117  ARG A CA    1 
ATOM   906   C  C     . ARG A 1  117  ? 136.648 94.116  147.965 1.00 38.87  ? 117  ARG A C     1 
ATOM   907   O  O     . ARG A 1  117  ? 137.362 94.275  148.969 1.00 43.58  ? 117  ARG A O     1 
ATOM   908   C  CB    . ARG A 1  117  ? 136.904 92.017  146.565 1.00 36.81  ? 117  ARG A CB    1 
ATOM   909   C  CG    . ARG A 1  117  ? 136.332 90.659  146.223 1.00 37.99  ? 117  ARG A CG    1 
ATOM   910   C  CD    . ARG A 1  117  ? 136.933 90.068  144.960 1.00 39.30  ? 117  ARG A CD    1 
ATOM   911   N  NE    . ARG A 1  117  ? 138.289 89.570  145.146 1.00 40.27  ? 117  ARG A NE    1 
ATOM   912   C  CZ    . ARG A 1  117  ? 139.372 90.129  144.623 1.00 42.16  ? 117  ARG A CZ    1 
ATOM   913   N  NH1   . ARG A 1  117  ? 139.299 91.229  143.893 1.00 39.46  ? 117  ARG A NH1   1 
ATOM   914   N  NH2   . ARG A 1  117  ? 140.558 89.565  144.834 1.00 41.95  ? 117  ARG A NH2   1 
ATOM   915   N  N     . PRO A 1  118  ? 136.359 95.157  147.172 1.00 36.52  ? 118  PRO A N     1 
ATOM   916   C  CA    . PRO A 1  118  ? 136.942 96.475  147.469 1.00 34.62  ? 118  PRO A CA    1 
ATOM   917   C  C     . PRO A 1  118  ? 136.351 97.219  148.660 1.00 36.86  ? 118  PRO A C     1 
ATOM   918   O  O     . PRO A 1  118  ? 136.588 98.424  148.788 1.00 36.49  ? 118  PRO A O     1 
ATOM   919   C  CB    . PRO A 1  118  ? 136.710 97.255  146.166 1.00 34.68  ? 118  PRO A CB    1 
ATOM   920   C  CG    . PRO A 1  118  ? 136.504 96.216  145.132 1.00 34.28  ? 118  PRO A CG    1 
ATOM   921   C  CD    . PRO A 1  118  ? 135.762 95.141  145.827 1.00 35.16  ? 118  PRO A CD    1 
ATOM   922   N  N     . LYS A 1  119  ? 135.580 96.559  149.525 1.00 39.03  ? 119  LYS A N     1 
ATOM   923   C  CA    . LYS A 1  119  ? 135.100 97.202  150.747 1.00 36.35  ? 119  LYS A CA    1 
ATOM   924   C  C     . LYS A 1  119  ? 135.383 96.423  152.024 1.00 38.38  ? 119  LYS A C     1 
ATOM   925   O  O     . LYS A 1  119  ? 135.300 97.005  153.113 1.00 39.63  ? 119  LYS A O     1 
ATOM   926   C  CB    . LYS A 1  119  ? 133.589 97.477  150.662 1.00 32.53  ? 119  LYS A CB    1 
ATOM   927   C  CG    . LYS A 1  119  ? 133.125 97.887  149.277 1.00 36.85  ? 119  LYS A CG    1 
ATOM   928   C  CD    . LYS A 1  119  ? 131.980 98.901  149.286 1.00 37.16  ? 119  LYS A CD    1 
ATOM   929   C  CE    . LYS A 1  119  ? 130.900 98.557  150.297 1.00 37.19  ? 119  LYS A CE    1 
ATOM   930   N  NZ    . LYS A 1  119  ? 130.028 99.730  150.578 1.00 35.50  ? 119  LYS A NZ    1 
ATOM   931   N  N     . ARG A 1  120  ? 135.714 95.134  151.933 1.00 38.01  ? 120  ARG A N     1 
ATOM   932   C  CA    . ARG A 1  120  ? 135.813 94.335  153.148 1.00 40.46  ? 120  ARG A CA    1 
ATOM   933   C  C     . ARG A 1  120  ? 137.055 94.676  153.967 1.00 38.93  ? 120  ARG A C     1 
ATOM   934   O  O     . ARG A 1  120  ? 136.987 94.690  155.199 1.00 41.52  ? 120  ARG A O     1 
ATOM   935   C  CB    . ARG A 1  120  ? 135.742 92.845  152.803 1.00 38.49  ? 120  ARG A CB    1 
ATOM   936   C  CG    . ARG A 1  120  ? 136.920 92.287  152.066 1.00 36.42  ? 120  ARG A CG    1 
ATOM   937   C  CD    . ARG A 1  120  ? 136.737 90.807  151.772 1.00 34.44  ? 120  ARG A CD    1 
ATOM   938   N  NE    . ARG A 1  120  ? 135.832 90.568  150.657 1.00 38.03  ? 120  ARG A NE    1 
ATOM   939   C  CZ    . ARG A 1  120  ? 135.725 89.413  150.014 1.00 40.30  ? 120  ARG A CZ    1 
ATOM   940   N  NH1   . ARG A 1  120  ? 136.501 88.383  150.306 1.00 37.22  ? 120  ARG A NH1   1 
ATOM   941   N  NH2   . ARG A 1  120  ? 134.827 89.293  149.042 1.00 41.66  ? 120  ARG A NH2   1 
ATOM   942   N  N     . LEU A 1  121  ? 138.178 94.990  153.321 1.00 37.06  ? 121  LEU A N     1 
ATOM   943   C  CA    . LEU A 1  121  ? 139.354 95.450  154.059 1.00 37.89  ? 121  LEU A CA    1 
ATOM   944   C  C     . LEU A 1  121  ? 139.086 96.777  154.767 1.00 38.03  ? 121  LEU A C     1 
ATOM   945   O  O     . LEU A 1  121  ? 139.474 96.965  155.929 1.00 38.27  ? 121  LEU A O     1 
ATOM   946   C  CB    . LEU A 1  121  ? 140.549 95.534  153.107 1.00 36.04  ? 121  LEU A CB    1 
ATOM   947   C  CG    . LEU A 1  121  ? 142.000 95.656  153.586 1.00 36.77  ? 121  LEU A CG    1 
ATOM   948   C  CD1   . LEU A 1  121  ? 142.348 97.065  153.853 1.00 36.08  ? 121  LEU A CD1   1 
ATOM   949   C  CD2   . LEU A 1  121  ? 142.194 94.914  154.868 1.00 34.53  ? 121  LEU A CD2   1 
ATOM   950   N  N     . ILE A 1  122  ? 138.401 97.703  154.093 1.00 38.16  ? 122  ILE A N     1 
ATOM   951   C  CA    . ILE A 1  122  ? 138.071 98.984  154.715 1.00 37.91  ? 122  ILE A CA    1 
ATOM   952   C  C     . ILE A 1  122  ? 137.188 98.777  155.937 1.00 38.98  ? 122  ILE A C     1 
ATOM   953   O  O     . ILE A 1  122  ? 137.443 99.338  157.012 1.00 36.28  ? 122  ILE A O     1 
ATOM   954   C  CB    . ILE A 1  122  ? 137.395 99.917  153.692 1.00 35.44  ? 122  ILE A CB    1 
ATOM   955   C  CG1   . ILE A 1  122  ? 138.170 99.932  152.376 1.00 36.73  ? 122  ILE A CG1   1 
ATOM   956   C  CG2   . ILE A 1  122  ? 137.253 101.317 154.257 1.00 37.50  ? 122  ILE A CG2   1 
ATOM   957   C  CD1   . ILE A 1  122  ? 137.919 101.161 151.541 1.00 36.86  ? 122  ILE A CD1   1 
ATOM   958   N  N     . GLU A 1  123  ? 136.138 97.962  155.797 1.00 42.33  ? 123  GLU A N     1 
ATOM   959   C  CA    . GLU A 1  123  ? 135.239 97.730  156.923 1.00 43.39  ? 123  GLU A CA    1 
ATOM   960   C  C     . GLU A 1  123  ? 135.945 97.014  158.061 1.00 44.47  ? 123  GLU A C     1 
ATOM   961   O  O     . GLU A 1  123  ? 135.731 97.342  159.234 1.00 43.22  ? 123  GLU A O     1 
ATOM   962   C  CB    . GLU A 1  123  ? 134.022 96.933  156.478 1.00 42.18  ? 123  GLU A CB    1 
ATOM   963   C  CG    . GLU A 1  123  ? 133.155 97.647  155.480 1.00 44.92  ? 123  GLU A CG    1 
ATOM   964   C  CD    . GLU A 1  123  ? 132.436 96.676  154.591 1.00 46.40  ? 123  GLU A CD    1 
ATOM   965   O  OE1   . GLU A 1  123  ? 132.695 95.464  154.736 1.00 43.40  ? 123  GLU A OE1   1 
ATOM   966   O  OE2   . GLU A 1  123  ? 131.616 97.117  153.758 1.00 48.73  ? 123  GLU A OE2   1 
ATOM   967   N  N     . ALA A 1  124  ? 136.788 96.031  157.740 1.00 39.51  ? 124  ALA A N     1 
ATOM   968   C  CA    . ALA A 1  124  ? 137.517 95.328  158.784 1.00 37.40  ? 124  ALA A CA    1 
ATOM   969   C  C     . ALA A 1  124  ? 138.390 96.287  159.574 1.00 39.38  ? 124  ALA A C     1 
ATOM   970   O  O     . ALA A 1  124  ? 138.386 96.262  160.809 1.00 40.90  ? 124  ALA A O     1 
ATOM   971   C  CB    . ALA A 1  124  ? 138.359 94.210  158.176 1.00 37.85  ? 124  ALA A CB    1 
ATOM   972   N  N     . ALA A 1  125  ? 139.124 97.162  158.886 1.00 35.96  ? 125  ALA A N     1 
ATOM   973   C  CA    . ALA A 1  125  ? 139.945 98.127  159.606 1.00 35.88  ? 125  ALA A CA    1 
ATOM   974   C  C     . ALA A 1  125  ? 139.107 99.125  160.389 1.00 37.74  ? 125  ALA A C     1 
ATOM   975   O  O     . ALA A 1  125  ? 139.575 99.637  161.411 1.00 36.50  ? 125  ALA A O     1 
ATOM   976   C  CB    . ALA A 1  125  ? 140.868 98.869  158.641 1.00 34.71  ? 125  ALA A CB    1 
ATOM   977   N  N     . SER A 1  126  ? 137.883 99.410  159.940 1.00 39.41  ? 126  SER A N     1 
ATOM   978   C  CA    . SER A 1  126  ? 137.050 100.387 160.636 1.00 38.60  ? 126  SER A CA    1 
ATOM   979   C  C     . SER A 1  126  ? 136.715 99.935  162.053 1.00 40.67  ? 126  SER A C     1 
ATOM   980   O  O     . SER A 1  126  ? 136.653 100.760 162.972 1.00 38.57  ? 126  SER A O     1 
ATOM   981   C  CB    . SER A 1  126  ? 135.773 100.643 159.840 1.00 35.39  ? 126  SER A CB    1 
ATOM   982   O  OG    . SER A 1  126  ? 134.983 99.471  159.773 1.00 39.13  ? 126  SER A OG    1 
ATOM   983   N  N     . SER A 1  127  ? 136.483 98.638  162.247 1.00 42.30  ? 127  SER A N     1 
ATOM   984   C  CA    . SER A 1  127  ? 136.154 98.120  163.569 1.00 40.35  ? 127  SER A CA    1 
ATOM   985   C  C     . SER A 1  127  ? 137.339 98.260  164.515 1.00 43.26  ? 127  SER A C     1 
ATOM   986   O  O     . SER A 1  127  ? 138.491 98.047  164.130 1.00 39.54  ? 127  SER A O     1 
ATOM   987   C  CB    . SER A 1  127  ? 135.733 96.655  163.475 1.00 39.69  ? 127  SER A CB    1 
ATOM   988   O  OG    . SER A 1  127  ? 136.798 95.839  163.031 1.00 43.24  ? 127  SER A OG    1 
ATOM   989   N  N     . GLN A 1  128  ? 137.047 98.614  165.766 1.00 48.79  ? 128  GLN A N     1 
ATOM   990   C  CA    . GLN A 1  128  ? 138.095 98.807  166.759 1.00 49.04  ? 128  GLN A CA    1 
ATOM   991   C  C     . GLN A 1  128  ? 138.812 97.495  167.050 1.00 48.33  ? 128  GLN A C     1 
ATOM   992   O  O     . GLN A 1  128  ? 138.191 96.434  167.159 1.00 48.52  ? 128  GLN A O     1 
ATOM   993   C  CB    . GLN A 1  128  ? 137.510 99.393  168.046 1.00 46.99  ? 128  GLN A CB    1 
ATOM   994   C  CG    . GLN A 1  128  ? 136.399 98.562  168.665 1.00 47.57  ? 128  GLN A CG    1 
ATOM   995   C  CD    . GLN A 1  128  ? 135.941 99.095  170.008 1.00 50.62  ? 128  GLN A CD    1 
ATOM   996   O  OE1   . GLN A 1  128  ? 136.505 100.053 170.534 1.00 50.54  ? 128  GLN A OE1   1 
ATOM   997   N  NE2   . GLN A 1  128  ? 134.911 98.475  170.571 1.00 51.41  ? 128  GLN A NE2   1 
ATOM   998   N  N     . THR A 1  129  ? 140.137 97.573  167.167 1.00 47.60  ? 129  THR A N     1 
ATOM   999   C  CA    . THR A 1  129  ? 140.973 96.394  167.339 1.00 48.13  ? 129  THR A CA    1 
ATOM   1000  C  C     . THR A 1  129  ? 142.019 96.532  168.430 1.00 49.45  ? 129  THR A C     1 
ATOM   1001  O  O     . THR A 1  129  ? 142.602 95.518  168.823 1.00 49.91  ? 129  THR A O     1 
ATOM   1002  C  CB    . THR A 1  129  ? 141.694 96.041  166.027 1.00 47.70  ? 129  THR A CB    1 
ATOM   1003  O  OG1   . THR A 1  129  ? 142.294 97.221  165.476 1.00 46.94  ? 129  THR A OG1   1 
ATOM   1004  C  CG2   . THR A 1  129  ? 140.728 95.456  165.019 1.00 46.25  ? 129  THR A CG2   1 
ATOM   1005  N  N     . GLU A 1  130  ? 142.290 97.740  168.917 1.00 50.62  ? 130  GLU A N     1 
ATOM   1006  C  CA    . GLU A 1  130  ? 143.335 97.921  169.912 1.00 49.61  ? 130  GLU A CA    1 
ATOM   1007  C  C     . GLU A 1  130  ? 142.928 97.257  171.221 1.00 50.81  ? 130  GLU A C     1 
ATOM   1008  O  O     . GLU A 1  130  ? 141.791 97.399  171.678 1.00 49.63  ? 130  GLU A O     1 
ATOM   1009  C  CB    . GLU A 1  130  ? 143.620 99.406  170.122 1.00 47.40  ? 130  GLU A CB    1 
ATOM   1010  C  CG    . GLU A 1  130  ? 142.411 100.241 170.488 1.00 46.79  ? 130  GLU A CG    1 
ATOM   1011  C  CD    . GLU A 1  130  ? 142.387 100.596 171.959 1.00 51.30  ? 130  GLU A CD    1 
ATOM   1012  O  OE1   . GLU A 1  130  ? 143.471 100.629 172.580 1.00 49.80  ? 130  GLU A OE1   1 
ATOM   1013  O  OE2   . GLU A 1  130  ? 141.286 100.845 172.494 1.00 52.53  ? 130  GLU A OE2   1 
ATOM   1014  N  N     . GLY A 1  131  ? 143.860 96.524  171.818 1.00 46.29  ? 131  GLY A N     1 
ATOM   1015  C  CA    . GLY A 1  131  ? 143.594 95.737  172.994 1.00 46.16  ? 131  GLY A CA    1 
ATOM   1016  C  C     . GLY A 1  131  ? 143.313 94.276  172.720 1.00 47.61  ? 131  GLY A C     1 
ATOM   1017  O  O     . GLY A 1  131  ? 143.421 93.457  173.641 1.00 49.17  ? 131  GLY A O     1 
ATOM   1018  N  N     . LYS A 1  132  ? 142.967 93.925  171.484 1.00 47.02  ? 132  LYS A N     1 
ATOM   1019  C  CA    . LYS A 1  132  ? 142.761 92.528  171.146 1.00 47.00  ? 132  LYS A CA    1 
ATOM   1020  C  C     . LYS A 1  132  ? 144.075 91.769  171.269 1.00 49.05  ? 132  LYS A C     1 
ATOM   1021  O  O     . LYS A 1  132  ? 145.162 92.351  171.250 1.00 49.60  ? 132  LYS A O     1 
ATOM   1022  C  CB    . LYS A 1  132  ? 142.208 92.383  169.727 1.00 47.47  ? 132  LYS A CB    1 
ATOM   1023  C  CG    . LYS A 1  132  ? 140.767 92.838  169.556 1.00 50.01  ? 132  LYS A CG    1 
ATOM   1024  C  CD    . LYS A 1  132  ? 140.355 92.819  168.086 1.00 50.04  ? 132  LYS A CD    1 
ATOM   1025  C  CE    . LYS A 1  132  ? 138.921 93.299  167.909 1.00 48.98  ? 132  LYS A CE    1 
ATOM   1026  N  NZ    . LYS A 1  132  ? 138.561 93.538  166.483 1.00 45.94  ? 132  LYS A NZ    1 
ATOM   1027  N  N     . GLN A 1  133  ? 143.970 90.455  171.414 1.00 44.59  ? 133  GLN A N     1 
ATOM   1028  C  CA    . GLN A 1  133  ? 145.143 89.611  171.547 1.00 46.28  ? 133  GLN A CA    1 
ATOM   1029  C  C     . GLN A 1  133  ? 145.182 88.590  170.420 1.00 44.65  ? 133  GLN A C     1 
ATOM   1030  O  O     . GLN A 1  133  ? 144.146 88.074  169.990 1.00 43.84  ? 133  GLN A O     1 
ATOM   1031  C  CB    . GLN A 1  133  ? 145.170 88.897  172.901 1.00 46.31  ? 133  GLN A CB    1 
ATOM   1032  C  CG    . GLN A 1  133  ? 146.576 88.551  173.367 1.00 46.57  ? 133  GLN A CG    1 
ATOM   1033  C  CD    . GLN A 1  133  ? 146.597 87.823  174.691 1.00 48.89  ? 133  GLN A CD    1 
ATOM   1034  O  OE1   . GLN A 1  133  ? 145.580 87.299  175.144 1.00 48.65  ? 133  GLN A OE1   1 
ATOM   1035  N  NE2   . GLN A 1  133  ? 147.758 87.802  175.332 1.00 46.22  ? 133  GLN A NE2   1 
ATOM   1036  N  N     . CYS A 1  134  ? 146.392 88.302  169.949 1.00 44.72  ? 134  CYS A N     1 
ATOM   1037  C  CA    . CYS A 1  134  ? 146.564 87.404  168.821 1.00 45.59  ? 134  CYS A CA    1 
ATOM   1038  C  C     . CYS A 1  134  ? 146.254 85.966  169.225 1.00 46.71  ? 134  CYS A C     1 
ATOM   1039  O  O     . CYS A 1  134  ? 146.312 85.588  170.396 1.00 47.94  ? 134  CYS A O     1 
ATOM   1040  C  CB    . CYS A 1  134  ? 147.982 87.498  168.264 1.00 45.53  ? 134  CYS A CB    1 
ATOM   1041  S  SG    . CYS A 1  134  ? 148.268 86.408  166.857 1.00 52.88  ? 134  CYS A SG    1 
ATOM   1042  N  N     . TYR A 1  135  ? 145.942 85.153  168.220 1.00 51.42  ? 135  TYR A N     1 
ATOM   1043  C  CA    . TYR A 1  135  ? 145.495 83.785  168.426 1.00 52.88  ? 135  TYR A CA    1 
ATOM   1044  C  C     . TYR A 1  135  ? 146.563 82.743  168.157 1.00 52.94  ? 135  TYR A C     1 
ATOM   1045  O  O     . TYR A 1  135  ? 146.467 81.635  168.684 1.00 56.28  ? 135  TYR A O     1 
ATOM   1046  C  CB    . TYR A 1  135  ? 144.285 83.484  167.533 1.00 52.77  ? 135  TYR A CB    1 
ATOM   1047  C  CG    . TYR A 1  135  ? 143.041 84.251  167.912 1.00 53.04  ? 135  TYR A CG    1 
ATOM   1048  C  CD1   . TYR A 1  135  ? 142.876 84.757  169.191 1.00 51.83  ? 135  TYR A CD1   1 
ATOM   1049  C  CD2   . TYR A 1  135  ? 142.033 84.471  166.987 1.00 54.52  ? 135  TYR A CD2   1 
ATOM   1050  C  CE1   . TYR A 1  135  ? 141.733 85.459  169.540 1.00 54.96  ? 135  TYR A CE1   1 
ATOM   1051  C  CE2   . TYR A 1  135  ? 140.891 85.172  167.324 1.00 54.68  ? 135  TYR A CE2   1 
ATOM   1052  C  CZ    . TYR A 1  135  ? 140.746 85.663  168.599 1.00 55.76  ? 135  TYR A CZ    1 
ATOM   1053  O  OH    . TYR A 1  135  ? 139.611 86.362  168.934 1.00 54.74  ? 135  TYR A OH    1 
ATOM   1054  N  N     . VAL A 1  136  ? 147.564 83.059  167.342 1.00 44.32  ? 136  VAL A N     1 
ATOM   1055  C  CA    . VAL A 1  136  ? 148.608 82.089  167.039 1.00 47.12  ? 136  VAL A CA    1 
ATOM   1056  C  C     . VAL A 1  136  ? 149.886 82.357  167.830 1.00 46.16  ? 136  VAL A C     1 
ATOM   1057  O  O     . VAL A 1  136  ? 150.601 81.413  168.179 1.00 45.22  ? 136  VAL A O     1 
ATOM   1058  C  CB    . VAL A 1  136  ? 148.885 82.058  165.527 1.00 46.81  ? 136  VAL A CB    1 
ATOM   1059  C  CG1   . VAL A 1  136  ? 147.733 81.400  164.803 1.00 45.02  ? 136  VAL A CG1   1 
ATOM   1060  C  CG2   . VAL A 1  136  ? 149.092 83.461  164.997 1.00 44.61  ? 136  VAL A CG2   1 
ATOM   1061  N  N     . CYS A 1  137  ? 150.189 83.619  168.127 1.00 48.44  ? 137  CYS A N     1 
ATOM   1062  C  CA    . CYS A 1  137  ? 151.355 83.962  168.926 1.00 47.98  ? 137  CYS A CA    1 
ATOM   1063  C  C     . CYS A 1  137  ? 150.983 84.560  170.271 1.00 48.73  ? 137  CYS A C     1 
ATOM   1064  O  O     . CYS A 1  137  ? 151.868 84.741  171.115 1.00 47.88  ? 137  CYS A O     1 
ATOM   1065  C  CB    . CYS A 1  137  ? 152.266 84.941  168.171 1.00 47.52  ? 137  CYS A CB    1 
ATOM   1066  S  SG    . CYS A 1  137  ? 151.683 86.651  168.155 1.00 56.55  ? 137  CYS A SG    1 
ATOM   1067  N  N     . LYS A 1  138  ? 149.707 84.869  170.493 1.00 47.89  ? 138  LYS A N     1 
ATOM   1068  C  CA    . LYS A 1  138  ? 149.227 85.408  171.764 1.00 48.63  ? 138  LYS A CA    1 
ATOM   1069  C  C     . LYS A 1  138  ? 149.897 86.733  172.108 1.00 46.73  ? 138  LYS A C     1 
ATOM   1070  O  O     . LYS A 1  138  ? 150.502 86.878  173.170 1.00 48.66  ? 138  LYS A O     1 
ATOM   1071  C  CB    . LYS A 1  138  ? 149.406 84.400  172.905 1.00 48.14  ? 138  LYS A CB    1 
ATOM   1072  C  CG    . LYS A 1  138  ? 148.288 83.368  173.005 1.00 48.21  ? 138  LYS A CG    1 
ATOM   1073  C  CD    . LYS A 1  138  ? 148.422 82.279  171.949 1.00 47.52  ? 138  LYS A CD    1 
ATOM   1074  C  CE    . LYS A 1  138  ? 149.744 81.539  172.079 1.00 49.12  ? 138  LYS A CE    1 
ATOM   1075  N  NZ    . LYS A 1  138  ? 149.909 80.494  171.027 1.00 47.62  ? 138  LYS A NZ    1 
ATOM   1076  N  N     . ALA A 1  139  ? 149.807 87.701  171.203 1.00 43.32  ? 139  ALA A N     1 
ATOM   1077  C  CA    . ALA A 1  139  ? 150.301 89.051  171.433 1.00 45.96  ? 139  ALA A CA    1 
ATOM   1078  C  C     . ALA A 1  139  ? 149.124 90.018  171.406 1.00 46.94  ? 139  ALA A C     1 
ATOM   1079  O  O     . ALA A 1  139  ? 148.186 89.837  170.625 1.00 46.84  ? 139  ALA A O     1 
ATOM   1080  C  CB    . ALA A 1  139  ? 151.345 89.442  170.388 1.00 41.73  ? 139  ALA A CB    1 
ATOM   1081  N  N     . VAL A 1  140  ? 149.170 91.033  172.266 1.00 44.84  ? 140  VAL A N     1 
ATOM   1082  C  CA    . VAL A 1  140  ? 148.112 92.033  172.297 1.00 46.74  ? 140  VAL A CA    1 
ATOM   1083  C  C     . VAL A 1  140  ? 148.356 93.067  171.204 1.00 46.32  ? 140  VAL A C     1 
ATOM   1084  O  O     . VAL A 1  140  ? 149.459 93.614  171.078 1.00 44.80  ? 140  VAL A O     1 
ATOM   1085  C  CB    . VAL A 1  140  ? 148.036 92.687  173.684 1.00 47.79  ? 140  VAL A CB    1 
ATOM   1086  C  CG1   . VAL A 1  140  ? 149.426 93.070  174.162 1.00 42.89  ? 140  VAL A CG1   1 
ATOM   1087  C  CG2   . VAL A 1  140  ? 147.114 93.899  173.654 1.00 44.74  ? 140  VAL A CG2   1 
ATOM   1088  N  N     . HIS A 1  141  ? 147.327 93.341  170.410 1.00 43.57  ? 141  HIS A N     1 
ATOM   1089  C  CA    . HIS A 1  141  ? 147.445 94.315  169.331 1.00 43.62  ? 141  HIS A CA    1 
ATOM   1090  C  C     . HIS A 1  141  ? 147.422 95.732  169.895 1.00 46.58  ? 141  HIS A C     1 
ATOM   1091  O  O     . HIS A 1  141  ? 146.431 96.122  170.521 1.00 45.69  ? 141  HIS A O     1 
ATOM   1092  C  CB    . HIS A 1  141  ? 146.314 94.136  168.332 1.00 43.57  ? 141  HIS A CB    1 
ATOM   1093  C  CG    . HIS A 1  141  ? 146.454 94.980  167.105 1.00 47.38  ? 141  HIS A CG    1 
ATOM   1094  N  ND1   . HIS A 1  141  ? 147.521 94.865  166.241 1.00 46.96  ? 141  HIS A ND1   1 
ATOM   1095  C  CD2   . HIS A 1  141  ? 145.664 95.955  166.600 1.00 45.35  ? 141  HIS A CD2   1 
ATOM   1096  C  CE1   . HIS A 1  141  ? 147.378 95.730  165.254 1.00 43.26  ? 141  HIS A CE1   1 
ATOM   1097  N  NE2   . HIS A 1  141  ? 146.262 96.406  165.450 1.00 44.88  ? 141  HIS A NE2   1 
ATOM   1098  N  N     . PRO A 1  142  ? 148.460 96.532  169.681 1.00 38.87  ? 142  PRO A N     1 
ATOM   1099  C  CA    . PRO A 1  142  ? 148.500 97.876  170.262 1.00 37.39  ? 142  PRO A CA    1 
ATOM   1100  C  C     . PRO A 1  142  ? 147.611 98.854  169.507 1.00 41.17  ? 142  PRO A C     1 
ATOM   1101  O  O     . PRO A 1  142  ? 147.089 98.574  168.431 1.00 41.19  ? 142  PRO A O     1 
ATOM   1102  C  CB    . PRO A 1  142  ? 149.973 98.267  170.134 1.00 38.44  ? 142  PRO A CB    1 
ATOM   1103  C  CG    . PRO A 1  142  ? 150.454 97.513  168.962 1.00 40.39  ? 142  PRO A CG    1 
ATOM   1104  C  CD    . PRO A 1  142  ? 149.687 96.217  168.933 1.00 39.51  ? 142  PRO A CD    1 
ATOM   1105  N  N     . LYS A 1  143  ? 147.440 100.023 170.115 1.00 43.86  ? 143  LYS A N     1 
ATOM   1106  C  CA    . LYS A 1  143  ? 146.774 101.134 169.456 1.00 40.16  ? 143  LYS A CA    1 
ATOM   1107  C  C     . LYS A 1  143  ? 147.707 101.768 168.437 1.00 42.87  ? 143  LYS A C     1 
ATOM   1108  O  O     . LYS A 1  143  ? 148.863 102.073 168.738 1.00 43.47  ? 143  LYS A O     1 
ATOM   1109  C  CB    . LYS A 1  143  ? 146.338 102.178 170.482 1.00 41.13  ? 143  LYS A CB    1 
ATOM   1110  C  CG    . LYS A 1  143  ? 145.530 103.332 169.911 1.00 43.28  ? 143  LYS A CG    1 
ATOM   1111  C  CD    . LYS A 1  143  ? 145.000 104.225 171.024 1.00 45.22  ? 143  LYS A CD    1 
ATOM   1112  C  CE    . LYS A 1  143  ? 144.070 105.314 170.499 1.00 42.92  ? 143  LYS A CE    1 
ATOM   1113  N  NZ    . LYS A 1  143  ? 144.794 106.393 169.781 1.00 41.91  ? 143  LYS A NZ    1 
ATOM   1114  N  N     . ILE A 1  144  ? 147.199 101.967 167.227 1.00 40.42  ? 144  ILE A N     1 
ATOM   1115  C  CA    . ILE A 1  144  ? 147.931 102.631 166.157 1.00 36.57  ? 144  ILE A CA    1 
ATOM   1116  C  C     . ILE A 1  144  ? 147.417 104.058 166.100 1.00 37.25  ? 144  ILE A C     1 
ATOM   1117  O  O     . ILE A 1  144  ? 146.226 104.289 165.861 1.00 37.07  ? 144  ILE A O     1 
ATOM   1118  C  CB    . ILE A 1  144  ? 147.753 101.920 164.810 1.00 35.85  ? 144  ILE A CB    1 
ATOM   1119  C  CG1   . ILE A 1  144  ? 148.209 100.468 164.909 1.00 36.63  ? 144  ILE A CG1   1 
ATOM   1120  C  CG2   . ILE A 1  144  ? 148.533 102.637 163.734 1.00 37.06  ? 144  ILE A CG2   1 
ATOM   1121  C  CD1   . ILE A 1  144  ? 149.673 100.320 165.192 1.00 35.55  ? 144  ILE A CD1   1 
ATOM   1122  N  N     . VAL A 1  145  ? 148.296 105.020 166.350 1.00 41.44  ? 145  VAL A N     1 
ATOM   1123  C  CA    . VAL A 1  145  ? 147.919 106.425 166.377 1.00 44.61  ? 145  VAL A CA    1 
ATOM   1124  C  C     . VAL A 1  145  ? 148.738 107.168 165.333 1.00 43.50  ? 145  VAL A C     1 
ATOM   1125  O  O     . VAL A 1  145  ? 149.972 107.094 165.328 1.00 39.49  ? 145  VAL A O     1 
ATOM   1126  C  CB    . VAL A 1  145  ? 148.097 107.041 167.777 1.00 45.86  ? 145  VAL A CB    1 
ATOM   1127  C  CG1   . VAL A 1  145  ? 149.301 106.447 168.476 1.00 43.95  ? 145  VAL A CG1   1 
ATOM   1128  C  CG2   . VAL A 1  145  ? 148.218 108.554 167.684 1.00 41.79  ? 145  VAL A CG2   1 
ATOM   1129  N  N     . LYS A 1  146  ? 148.042 107.864 164.444 1.00 49.88  ? 146  LYS A N     1 
ATOM   1130  C  CA    . LYS A 1  146  ? 148.677 108.675 163.420 1.00 51.45  ? 146  LYS A CA    1 
ATOM   1131  C  C     . LYS A 1  146  ? 148.995 110.051 163.985 1.00 51.22  ? 146  LYS A C     1 
ATOM   1132  O  O     . LYS A 1  146  ? 148.153 110.670 164.643 1.00 50.37  ? 146  LYS A O     1 
ATOM   1133  C  CB    . LYS A 1  146  ? 147.756 108.784 162.204 1.00 49.22  ? 146  LYS A CB    1 
ATOM   1134  C  CG    . LYS A 1  146  ? 148.057 109.931 161.263 1.00 47.52  ? 146  LYS A CG    1 
ATOM   1135  C  CD    . LYS A 1  146  ? 149.343 109.729 160.496 1.00 47.81  ? 146  LYS A CD    1 
ATOM   1136  C  CE    . LYS A 1  146  ? 149.465 110.789 159.424 1.00 50.99  ? 146  LYS A CE    1 
ATOM   1137  N  NZ    . LYS A 1  146  ? 149.419 112.162 160.001 1.00 50.35  ? 146  LYS A NZ    1 
ATOM   1138  N  N     . ASP A 1  147  ? 150.212 110.521 163.734 1.00 47.16  ? 147  ASP A N     1 
ATOM   1139  C  CA    . ASP A 1  147  ? 150.618 111.840 164.193 1.00 46.70  ? 147  ASP A CA    1 
ATOM   1140  C  C     . ASP A 1  147  ? 149.765 112.922 163.544 1.00 48.08  ? 147  ASP A C     1 
ATOM   1141  O  O     . ASP A 1  147  ? 149.210 112.742 162.457 1.00 50.01  ? 147  ASP A O     1 
ATOM   1142  C  CB    . ASP A 1  147  ? 152.093 112.077 163.872 1.00 48.65  ? 147  ASP A CB    1 
ATOM   1143  C  CG    . ASP A 1  147  ? 152.635 113.349 164.494 1.00 49.24  ? 147  ASP A CG    1 
ATOM   1144  O  OD1   . ASP A 1  147  ? 151.872 114.062 165.171 1.00 47.11  ? 147  ASP A OD1   1 
ATOM   1145  O  OD2   . ASP A 1  147  ? 153.833 113.635 164.311 1.00 48.55  ? 147  ASP A OD2   1 
ATOM   1146  N  N     . SER A 1  148  ? 149.643 114.047 164.238 1.00 42.86  ? 148  SER A N     1 
ATOM   1147  C  CA    . SER A 1  148  ? 148.996 115.229 163.695 1.00 43.80  ? 148  SER A CA    1 
ATOM   1148  C  C     . SER A 1  148  ? 149.995 116.249 163.177 1.00 47.36  ? 148  SER A C     1 
ATOM   1149  O  O     . SER A 1  148  ? 149.587 117.261 162.597 1.00 49.46  ? 148  SER A O     1 
ATOM   1150  C  CB    . SER A 1  148  ? 148.114 115.884 164.759 1.00 44.37  ? 148  SER A CB    1 
ATOM   1151  O  OG    . SER A 1  148  ? 148.913 116.419 165.801 1.00 48.66  ? 148  SER A OG    1 
ATOM   1152  N  N     . GLU A 1  149  ? 151.286 116.012 163.375 1.00 48.82  ? 149  GLU A N     1 
ATOM   1153  C  CA    . GLU A 1  149  ? 152.328 116.968 163.040 1.00 49.73  ? 149  GLU A CA    1 
ATOM   1154  C  C     . GLU A 1  149  ? 152.834 116.826 161.613 1.00 50.09  ? 149  GLU A C     1 
ATOM   1155  O  O     . GLU A 1  149  ? 153.536 117.721 161.130 1.00 49.43  ? 149  GLU A O     1 
ATOM   1156  C  CB    . GLU A 1  149  ? 153.491 116.808 164.020 1.00 51.21  ? 149  GLU A CB    1 
ATOM   1157  C  CG    . GLU A 1  149  ? 153.118 117.119 165.455 1.00 49.10  ? 149  GLU A CG    1 
ATOM   1158  C  CD    . GLU A 1  149  ? 154.257 116.867 166.417 1.00 52.81  ? 149  GLU A CD    1 
ATOM   1159  O  OE1   . GLU A 1  149  ? 155.303 116.341 165.978 1.00 51.85  ? 149  GLU A OE1   1 
ATOM   1160  O  OE2   . GLU A 1  149  ? 154.105 117.190 167.615 1.00 53.52  ? 149  GLU A OE2   1 
ATOM   1161  N  N     . ASP A 1  150  ? 152.497 115.736 160.933 1.00 48.42  ? 150  ASP A N     1 
ATOM   1162  C  CA    . ASP A 1  150  ? 152.919 115.500 159.557 1.00 45.39  ? 150  ASP A CA    1 
ATOM   1163  C  C     . ASP A 1  150  ? 151.935 114.510 158.937 1.00 46.73  ? 150  ASP A C     1 
ATOM   1164  O  O     . ASP A 1  150  ? 150.847 114.284 159.479 1.00 45.93  ? 150  ASP A O     1 
ATOM   1165  C  CB    . ASP A 1  150  ? 154.374 115.010 159.512 1.00 44.36  ? 150  ASP A CB    1 
ATOM   1166  C  CG    . ASP A 1  150  ? 154.623 113.859 160.449 1.00 46.58  ? 150  ASP A CG    1 
ATOM   1167  O  OD1   . ASP A 1  150  ? 153.700 113.507 161.206 1.00 46.90  ? 150  ASP A OD1   1 
ATOM   1168  O  OD2   . ASP A 1  150  ? 155.736 113.301 160.428 1.00 46.61  ? 150  ASP A OD2   1 
ATOM   1169  N  N     . TYR A 1  151  ? 152.316 113.912 157.808 1.00 46.91  ? 151  TYR A N     1 
ATOM   1170  C  CA    . TYR A 1  151  ? 151.389 113.113 157.022 1.00 46.87  ? 151  TYR A CA    1 
ATOM   1171  C  C     . TYR A 1  151  ? 151.750 111.638 156.894 1.00 46.65  ? 151  TYR A C     1 
ATOM   1172  O  O     . TYR A 1  151  ? 151.003 110.905 156.239 1.00 44.97  ? 151  TYR A O     1 
ATOM   1173  C  CB    . TYR A 1  151  ? 151.249 113.711 155.614 1.00 43.98  ? 151  TYR A CB    1 
ATOM   1174  C  CG    . TYR A 1  151  ? 150.647 115.096 155.583 1.00 44.98  ? 151  TYR A CG    1 
ATOM   1175  C  CD1   . TYR A 1  151  ? 149.277 115.281 155.702 1.00 45.74  ? 151  TYR A CD1   1 
ATOM   1176  C  CD2   . TYR A 1  151  ? 151.444 116.216 155.419 1.00 44.54  ? 151  TYR A CD2   1 
ATOM   1177  C  CE1   . TYR A 1  151  ? 148.721 116.541 155.672 1.00 43.18  ? 151  TYR A CE1   1 
ATOM   1178  C  CE2   . TYR A 1  151  ? 150.896 117.480 155.387 1.00 44.51  ? 151  TYR A CE2   1 
ATOM   1179  C  CZ    . TYR A 1  151  ? 149.535 117.637 155.514 1.00 45.77  ? 151  TYR A CZ    1 
ATOM   1180  O  OH    . TYR A 1  151  ? 148.982 118.898 155.482 1.00 48.16  ? 151  TYR A OH    1 
ATOM   1181  N  N     . PHE A 1  152  ? 152.850 111.167 157.486 1.00 43.83  ? 152  PHE A N     1 
ATOM   1182  C  CA    . PHE A 1  152  ? 153.261 109.792 157.206 1.00 44.78  ? 152  PHE A CA    1 
ATOM   1183  C  C     . PHE A 1  152  ? 153.601 108.951 158.434 1.00 45.46  ? 152  PHE A C     1 
ATOM   1184  O  O     . PHE A 1  152  ? 153.540 107.719 158.366 1.00 47.35  ? 152  PHE A O     1 
ATOM   1185  C  CB    . PHE A 1  152  ? 154.455 109.789 156.251 1.00 42.75  ? 152  PHE A CB    1 
ATOM   1186  C  CG    . PHE A 1  152  ? 155.416 110.909 156.481 1.00 45.45  ? 152  PHE A CG    1 
ATOM   1187  C  CD1   . PHE A 1  152  ? 156.299 110.872 157.543 1.00 44.95  ? 152  PHE A CD1   1 
ATOM   1188  C  CD2   . PHE A 1  152  ? 155.424 112.008 155.647 1.00 44.47  ? 152  PHE A CD2   1 
ATOM   1189  C  CE1   . PHE A 1  152  ? 157.182 111.907 157.762 1.00 43.84  ? 152  PHE A CE1   1 
ATOM   1190  C  CE2   . PHE A 1  152  ? 156.300 113.039 155.860 1.00 44.00  ? 152  PHE A CE2   1 
ATOM   1191  C  CZ    . PHE A 1  152  ? 157.182 112.991 156.922 1.00 43.57  ? 152  PHE A CZ    1 
ATOM   1192  N  N     . THR A 1  153  ? 153.965 109.579 159.549 1.00 42.15  ? 153  THR A N     1 
ATOM   1193  C  CA    . THR A 1  153  ? 154.462 108.842 160.709 1.00 42.09  ? 153  THR A CA    1 
ATOM   1194  C  C     . THR A 1  153  ? 153.333 108.120 161.441 1.00 42.63  ? 153  THR A C     1 
ATOM   1195  O  O     . THR A 1  153  ? 152.200 108.606 161.490 1.00 44.08  ? 153  THR A O     1 
ATOM   1196  C  CB    . THR A 1  153  ? 155.178 109.785 161.672 1.00 42.47  ? 153  THR A CB    1 
ATOM   1197  O  OG1   . THR A 1  153  ? 154.390 110.963 161.864 1.00 42.41  ? 153  THR A OG1   1 
ATOM   1198  C  CG2   . THR A 1  153  ? 156.530 110.181 161.109 1.00 42.67  ? 153  THR A CG2   1 
ATOM   1199  N  N     . PHE A 1  154  ? 153.651 106.964 162.019 1.00 43.02  ? 154  PHE A N     1 
ATOM   1200  C  CA    . PHE A 1  154  ? 152.730 106.203 162.851 1.00 44.48  ? 154  PHE A CA    1 
ATOM   1201  C  C     . PHE A 1  154  ? 153.365 105.882 164.198 1.00 45.89  ? 154  PHE A C     1 
ATOM   1202  O  O     . PHE A 1  154  ? 154.552 105.553 164.281 1.00 45.87  ? 154  PHE A O     1 
ATOM   1203  C  CB    . PHE A 1  154  ? 152.310 104.895 162.174 1.00 42.33  ? 154  PHE A CB    1 
ATOM   1204  C  CG    . PHE A 1  154  ? 151.564 105.088 160.894 1.00 43.54  ? 154  PHE A CG    1 
ATOM   1205  C  CD1   . PHE A 1  154  ? 150.262 105.555 160.903 1.00 43.54  ? 154  PHE A CD1   1 
ATOM   1206  C  CD2   . PHE A 1  154  ? 152.162 104.810 159.679 1.00 43.87  ? 154  PHE A CD2   1 
ATOM   1207  C  CE1   . PHE A 1  154  ? 149.576 105.737 159.725 1.00 44.56  ? 154  PHE A CE1   1 
ATOM   1208  C  CE2   . PHE A 1  154  ? 151.477 104.994 158.502 1.00 41.95  ? 154  PHE A CE2   1 
ATOM   1209  C  CZ    . PHE A 1  154  ? 150.184 105.455 158.528 1.00 42.59  ? 154  PHE A CZ    1 
ATOM   1210  N  N     . TRP A 1  155  ? 152.557 105.958 165.255 1.00 47.86  ? 155  TRP A N     1 
ATOM   1211  C  CA    . TRP A 1  155  ? 152.982 105.600 166.600 1.00 46.65  ? 155  TRP A CA    1 
ATOM   1212  C  C     . TRP A 1  155  ? 152.213 104.372 167.064 1.00 49.99  ? 155  TRP A C     1 
ATOM   1213  O  O     . TRP A 1  155  ? 150.996 104.288 166.878 1.00 47.15  ? 155  TRP A O     1 
ATOM   1214  C  CB    . TRP A 1  155  ? 152.754 106.738 167.600 1.00 48.42  ? 155  TRP A CB    1 
ATOM   1215  C  CG    . TRP A 1  155  ? 153.467 108.019 167.297 1.00 50.26  ? 155  TRP A CG    1 
ATOM   1216  C  CD1   . TRP A 1  155  ? 152.996 109.056 166.549 1.00 49.81  ? 155  TRP A CD1   1 
ATOM   1217  C  CD2   . TRP A 1  155  ? 154.773 108.404 167.738 1.00 49.47  ? 155  TRP A CD2   1 
ATOM   1218  N  NE1   . TRP A 1  155  ? 153.923 110.063 166.496 1.00 50.05  ? 155  TRP A NE1   1 
ATOM   1219  C  CE2   . TRP A 1  155  ? 155.026 109.688 167.217 1.00 50.33  ? 155  TRP A CE2   1 
ATOM   1220  C  CE3   . TRP A 1  155  ? 155.754 107.788 168.520 1.00 47.95  ? 155  TRP A CE3   1 
ATOM   1221  C  CZ2   . TRP A 1  155  ? 156.220 110.369 167.455 1.00 48.34  ? 155  TRP A CZ2   1 
ATOM   1222  C  CZ3   . TRP A 1  155  ? 156.938 108.466 168.755 1.00 51.22  ? 155  TRP A CZ3   1 
ATOM   1223  C  CH2   . TRP A 1  155  ? 157.160 109.742 168.223 1.00 51.08  ? 155  TRP A CH2   1 
ATOM   1224  N  N     . ALA A 1  156  ? 152.919 103.420 167.670 1.00 47.57  ? 156  ALA A N     1 
ATOM   1225  C  CA    . ALA A 1  156  ? 152.287 102.222 168.211 1.00 46.80  ? 156  ALA A CA    1 
ATOM   1226  C  C     . ALA A 1  156  ? 152.174 102.338 169.726 1.00 46.13  ? 156  ALA A C     1 
ATOM   1227  O  O     . ALA A 1  156  ? 153.182 102.287 170.435 1.00 44.43  ? 156  ALA A O     1 
ATOM   1228  C  CB    . ALA A 1  156  ? 153.075 100.969 167.829 1.00 42.89  ? 156  ALA A CB    1 
ATOM   1229  N  N     . ASP A 1  157  ? 150.943 102.468 170.216 1.00 47.78  ? 157  ASP A N     1 
ATOM   1230  C  CA    . ASP A 1  157  ? 150.654 102.714 171.629 1.00 47.13  ? 157  ASP A CA    1 
ATOM   1231  C  C     . ASP A 1  157  ? 150.277 101.392 172.289 1.00 45.72  ? 157  ASP A C     1 
ATOM   1232  O  O     . ASP A 1  157  ? 149.175 100.878 172.078 1.00 45.67  ? 157  ASP A O     1 
ATOM   1233  C  CB    . ASP A 1  157  ? 149.539 103.745 171.779 1.00 48.03  ? 157  ASP A CB    1 
ATOM   1234  C  CG    . ASP A 1  157  ? 149.386 104.242 173.204 1.00 50.15  ? 157  ASP A CG    1 
ATOM   1235  O  OD1   . ASP A 1  157  ? 150.115 103.759 174.094 1.00 48.30  ? 157  ASP A OD1   1 
ATOM   1236  O  OD2   . ASP A 1  157  ? 148.531 105.121 173.436 1.00 49.23  ? 157  ASP A OD2   1 
ATOM   1237  N  N     . GLN A 1  158  ? 151.192 100.846 173.091 1.00 46.58  ? 158  GLN A N     1 
ATOM   1238  C  CA    . GLN A 1  158  ? 150.987 99.568  173.773 1.00 47.12  ? 158  GLN A CA    1 
ATOM   1239  C  C     . GLN A 1  158  ? 150.725 99.820  175.257 1.00 46.04  ? 158  GLN A C     1 
ATOM   1240  O  O     . GLN A 1  158  ? 151.621 99.730  176.097 1.00 45.14  ? 158  GLN A O     1 
ATOM   1241  C  CB    . GLN A 1  158  ? 152.191 98.660  173.559 1.00 45.15  ? 158  GLN A CB    1 
ATOM   1242  C  CG    . GLN A 1  158  ? 152.050 97.288  174.170 1.00 45.13  ? 158  GLN A CG    1 
ATOM   1243  C  CD    . GLN A 1  158  ? 151.143 96.388  173.379 1.00 46.79  ? 158  GLN A CD    1 
ATOM   1244  O  OE1   . GLN A 1  158  ? 149.950 96.284  173.664 1.00 45.77  ? 158  GLN A OE1   1 
ATOM   1245  N  NE2   . GLN A 1  158  ? 151.705 95.712  172.383 1.00 46.10  ? 158  GLN A NE2   1 
ATOM   1246  N  N     . GLN A 1  159  ? 149.464 100.123 175.578 1.00 47.48  ? 159  GLN A N     1 
ATOM   1247  C  CA    . GLN A 1  159  ? 149.042 100.392 176.957 1.00 47.77  ? 159  GLN A CA    1 
ATOM   1248  C  C     . GLN A 1  159  ? 149.978 101.381 177.645 1.00 47.84  ? 159  GLN A C     1 
ATOM   1249  O  O     . GLN A 1  159  ? 150.463 101.143 178.751 1.00 47.96  ? 159  GLN A O     1 
ATOM   1250  C  CB    . GLN A 1  159  ? 148.920 99.101  177.775 1.00 47.34  ? 159  GLN A CB    1 
ATOM   1251  C  CG    . GLN A 1  159  ? 147.830 98.148  177.300 1.00 48.42  ? 159  GLN A CG    1 
ATOM   1252  C  CD    . GLN A 1  159  ? 148.349 97.067  176.374 1.00 51.10  ? 159  GLN A CD    1 
ATOM   1253  O  OE1   . GLN A 1  159  ? 149.498 96.639  176.481 1.00 51.75  ? 159  GLN A OE1   1 
ATOM   1254  N  NE2   . GLN A 1  159  ? 147.502 96.621  175.455 1.00 47.47  ? 159  GLN A NE2   1 
ATOM   1255  N  N     . GLY A 1  160  ? 150.249 102.494 176.973 1.00 42.68  ? 160  GLY A N     1 
ATOM   1256  C  CA    . GLY A 1  160  ? 151.147 103.511 177.471 1.00 43.68  ? 160  GLY A CA    1 
ATOM   1257  C  C     . GLY A 1  160  ? 152.551 103.425 176.914 1.00 43.54  ? 160  GLY A C     1 
ATOM   1258  O  O     . GLY A 1  160  ? 153.313 104.392 177.040 1.00 42.55  ? 160  GLY A O     1 
ATOM   1259  N  N     . LYS A 1  161  ? 152.920 102.298 176.314 1.00 46.11  ? 161  LYS A N     1 
ATOM   1260  C  CA    . LYS A 1  161  ? 154.204 102.176 175.633 1.00 49.02  ? 161  LYS A CA    1 
ATOM   1261  C  C     . LYS A 1  161  ? 154.078 102.766 174.233 1.00 49.21  ? 161  LYS A C     1 
ATOM   1262  O  O     . LYS A 1  161  ? 153.344 102.239 173.393 1.00 48.28  ? 161  LYS A O     1 
ATOM   1263  C  CB    . LYS A 1  161  ? 154.648 100.717 175.588 1.00 46.20  ? 161  LYS A CB    1 
ATOM   1264  C  CG    . LYS A 1  161  ? 156.031 100.524 175.007 1.00 45.77  ? 161  LYS A CG    1 
ATOM   1265  C  CD    . LYS A 1  161  ? 157.045 101.259 175.855 1.00 45.59  ? 161  LYS A CD    1 
ATOM   1266  C  CE    . LYS A 1  161  ? 157.140 100.656 177.236 1.00 46.82  ? 161  LYS A CE    1 
ATOM   1267  N  NZ    . LYS A 1  161  ? 158.101 101.405 178.081 1.00 48.78  ? 161  LYS A NZ    1 
ATOM   1268  N  N     . ILE A 1  162  ? 154.791 103.861 173.986 1.00 46.44  ? 162  ILE A N     1 
ATOM   1269  C  CA    . ILE A 1  162  ? 154.673 104.633 172.755 1.00 45.46  ? 162  ILE A CA    1 
ATOM   1270  C  C     . ILE A 1  162  ? 155.916 104.390 171.914 1.00 46.68  ? 162  ILE A C     1 
ATOM   1271  O  O     . ILE A 1  162  ? 157.037 104.680 172.349 1.00 46.18  ? 162  ILE A O     1 
ATOM   1272  C  CB    . ILE A 1  162  ? 154.497 106.129 173.056 1.00 46.19  ? 162  ILE A CB    1 
ATOM   1273  C  CG1   . ILE A 1  162  ? 153.095 106.404 173.603 1.00 45.42  ? 162  ILE A CG1   1 
ATOM   1274  C  CG2   . ILE A 1  162  ? 154.770 106.962 171.818 1.00 44.40  ? 162  ILE A CG2   1 
ATOM   1275  C  CD1   . ILE A 1  162  ? 152.004 106.252 172.575 1.00 44.51  ? 162  ILE A CD1   1 
ATOM   1276  N  N     . ASP A 1  163  ? 155.722 103.874 170.704 1.00 51.77  ? 163  ASP A N     1 
ATOM   1277  C  CA    . ASP A 1  163  ? 156.809 103.589 169.783 1.00 50.96  ? 163  ASP A CA    1 
ATOM   1278  C  C     . ASP A 1  163  ? 156.572 104.327 168.476 1.00 52.66  ? 163  ASP A C     1 
ATOM   1279  O  O     . ASP A 1  163  ? 155.433 104.514 168.049 1.00 52.49  ? 163  ASP A O     1 
ATOM   1280  C  CB    . ASP A 1  163  ? 156.929 102.089 169.500 1.00 49.31  ? 163  ASP A CB    1 
ATOM   1281  C  CG    . ASP A 1  163  ? 157.255 101.293 170.733 1.00 53.50  ? 163  ASP A CG    1 
ATOM   1282  O  OD1   . ASP A 1  163  ? 157.816 101.876 171.686 1.00 53.33  ? 163  ASP A OD1   1 
ATOM   1283  O  OD2   . ASP A 1  163  ? 156.944 100.085 170.753 1.00 52.61  ? 163  ASP A OD2   1 
ATOM   1284  N  N     . LYS A 1  164  ? 157.663 104.738 167.836 1.00 49.24  ? 164  LYS A N     1 
ATOM   1285  C  CA    . LYS A 1  164  ? 157.607 105.322 166.502 1.00 48.24  ? 164  LYS A CA    1 
ATOM   1286  C  C     . LYS A 1  164  ? 157.923 104.221 165.499 1.00 48.63  ? 164  LYS A C     1 
ATOM   1287  O  O     . LYS A 1  164  ? 158.951 103.545 165.615 1.00 48.48  ? 164  LYS A O     1 
ATOM   1288  C  CB    . LYS A 1  164  ? 158.578 106.494 166.365 1.00 45.20  ? 164  LYS A CB    1 
ATOM   1289  C  CG    . LYS A 1  164  ? 159.274 106.597 165.020 1.00 44.07  ? 164  LYS A CG    1 
ATOM   1290  C  CD    . LYS A 1  164  ? 159.932 107.953 164.861 1.00 47.46  ? 164  LYS A CD    1 
ATOM   1291  C  CE    . LYS A 1  164  ? 158.951 109.084 165.114 1.00 47.15  ? 164  LYS A CE    1 
ATOM   1292  N  NZ    . LYS A 1  164  ? 159.629 110.408 165.127 1.00 45.30  ? 164  LYS A NZ    1 
ATOM   1293  N  N     . LEU A 1  165  ? 157.026 104.022 164.538 1.00 46.30  ? 165  LEU A N     1 
ATOM   1294  C  CA    . LEU A 1  165  ? 157.126 102.902 163.607 1.00 46.33  ? 165  LEU A CA    1 
ATOM   1295  C  C     . LEU A 1  165  ? 157.948 103.339 162.401 1.00 46.76  ? 165  LEU A C     1 
ATOM   1296  O  O     . LEU A 1  165  ? 157.446 103.947 161.455 1.00 44.51  ? 165  LEU A O     1 
ATOM   1297  C  CB    . LEU A 1  165  ? 155.738 102.421 163.207 1.00 46.18  ? 165  LEU A CB    1 
ATOM   1298  C  CG    . LEU A 1  165  ? 155.052 101.520 164.235 1.00 45.21  ? 165  LEU A CG    1 
ATOM   1299  C  CD1   . LEU A 1  165  ? 153.638 101.189 163.813 1.00 44.57  ? 165  LEU A CD1   1 
ATOM   1300  C  CD2   . LEU A 1  165  ? 155.850 100.257 164.425 1.00 44.73  ? 165  LEU A CD2   1 
ATOM   1301  N  N     . TYR A 1  166  ? 159.237 103.030 162.446 1.00 47.39  ? 166  TYR A N     1 
ATOM   1302  C  CA    . TYR A 1  166  ? 160.121 103.323 161.337 1.00 48.49  ? 166  TYR A CA    1 
ATOM   1303  C  C     . TYR A 1  166  ? 159.780 102.450 160.132 1.00 46.91  ? 166  TYR A C     1 
ATOM   1304  O  O     . TYR A 1  166  ? 159.317 101.319 160.288 1.00 42.71  ? 166  TYR A O     1 
ATOM   1305  C  CB    . TYR A 1  166  ? 161.568 103.106 161.762 1.00 46.58  ? 166  TYR A CB    1 
ATOM   1306  C  CG    . TYR A 1  166  ? 162.038 104.111 162.783 1.00 46.55  ? 166  TYR A CG    1 
ATOM   1307  C  CD1   . TYR A 1  166  ? 162.106 105.455 162.467 1.00 47.38  ? 166  TYR A CD1   1 
ATOM   1308  C  CD2   . TYR A 1  166  ? 162.337 103.729 164.081 1.00 46.66  ? 166  TYR A CD2   1 
ATOM   1309  C  CE1   . TYR A 1  166  ? 162.525 106.384 163.392 1.00 49.50  ? 166  TYR A CE1   1 
ATOM   1310  C  CE2   . TYR A 1  166  ? 162.748 104.655 165.021 1.00 48.72  ? 166  TYR A CE2   1 
ATOM   1311  C  CZ    . TYR A 1  166  ? 162.835 105.982 164.670 1.00 49.20  ? 166  TYR A CZ    1 
ATOM   1312  O  OH    . TYR A 1  166  ? 163.241 106.910 165.596 1.00 45.86  ? 166  TYR A OH    1 
ATOM   1313  N  N     . PRO A 1  167  ? 160.005 102.957 158.916 1.00 41.40  ? 167  PRO A N     1 
ATOM   1314  C  CA    . PRO A 1  167  ? 159.644 102.182 157.722 1.00 39.25  ? 167  PRO A CA    1 
ATOM   1315  C  C     . PRO A 1  167  ? 160.327 100.834 157.641 1.00 38.45  ? 167  PRO A C     1 
ATOM   1316  O  O     . PRO A 1  167  ? 159.781 99.912  157.029 1.00 39.68  ? 167  PRO A O     1 
ATOM   1317  C  CB    . PRO A 1  167  ? 160.067 103.104 156.572 1.00 37.64  ? 167  PRO A CB    1 
ATOM   1318  C  CG    . PRO A 1  167  ? 160.045 104.462 157.152 1.00 35.85  ? 167  PRO A CG    1 
ATOM   1319  C  CD    . PRO A 1  167  ? 160.486 104.304 158.569 1.00 40.17  ? 167  PRO A CD    1 
ATOM   1320  N  N     . GLN A 1  168  ? 161.509 100.683 158.232 1.00 39.64  ? 168  GLN A N     1 
ATOM   1321  C  CA    . GLN A 1  168  ? 162.108 99.359  158.326 1.00 40.29  ? 168  GLN A CA    1 
ATOM   1322  C  C     . GLN A 1  168  ? 161.230 98.435  159.158 1.00 43.37  ? 168  GLN A C     1 
ATOM   1323  O  O     . GLN A 1  168  ? 161.002 97.276  158.791 1.00 41.50  ? 168  GLN A O     1 
ATOM   1324  C  CB    . GLN A 1  168  ? 163.507 99.472  158.928 1.00 42.36  ? 168  GLN A CB    1 
ATOM   1325  C  CG    . GLN A 1  168  ? 164.372 98.229  158.854 1.00 43.31  ? 168  GLN A CG    1 
ATOM   1326  C  CD    . GLN A 1  168  ? 164.219 97.473  157.556 1.00 46.19  ? 168  GLN A CD    1 
ATOM   1327  O  OE1   . GLN A 1  168  ? 163.305 96.664  157.393 1.00 44.77  ? 168  GLN A OE1   1 
ATOM   1328  N  NE2   . GLN A 1  168  ? 165.110 97.746  156.610 1.00 42.85  ? 168  GLN A NE2   1 
ATOM   1329  N  N     . ILE A 1  169  ? 160.699 98.947  160.269 1.00 42.86  ? 169  ILE A N     1 
ATOM   1330  C  CA    . ILE A 1  169  ? 159.821 98.154  161.120 1.00 38.74  ? 169  ILE A CA    1 
ATOM   1331  C  C     . ILE A 1  169  ? 158.532 97.811  160.386 1.00 40.30  ? 169  ILE A C     1 
ATOM   1332  O  O     . ILE A 1  169  ? 158.045 96.678  160.458 1.00 41.60  ? 169  ILE A O     1 
ATOM   1333  C  CB    . ILE A 1  169  ? 159.540 98.896  162.442 1.00 40.86  ? 169  ILE A CB    1 
ATOM   1334  C  CG1   . ILE A 1  169  ? 160.827 99.143  163.239 1.00 40.90  ? 169  ILE A CG1   1 
ATOM   1335  C  CG2   . ILE A 1  169  ? 158.547 98.124  163.293 1.00 39.20  ? 169  ILE A CG2   1 
ATOM   1336  C  CD1   . ILE A 1  169  ? 161.942 98.151  162.991 1.00 39.72  ? 169  ILE A CD1   1 
ATOM   1337  N  N     . ILE A 1  170  ? 157.954 98.781  159.675 1.00 38.20  ? 170  ILE A N     1 
ATOM   1338  C  CA    . ILE A 1  170  ? 156.700 98.537  158.969 1.00 35.74  ? 170  ILE A CA    1 
ATOM   1339  C  C     . ILE A 1  170  ? 156.905 97.526  157.846 1.00 35.96  ? 170  ILE A C     1 
ATOM   1340  O  O     . ILE A 1  170  ? 156.074 96.635  157.634 1.00 35.28  ? 170  ILE A O     1 
ATOM   1341  C  CB    . ILE A 1  170  ? 156.118 99.860  158.449 1.00 32.51  ? 170  ILE A CB    1 
ATOM   1342  C  CG1   . ILE A 1  170  ? 155.578 100.692 159.604 1.00 36.13  ? 170  ILE A CG1   1 
ATOM   1343  C  CG2   . ILE A 1  170  ? 154.991 99.592  157.497 1.00 34.97  ? 170  ILE A CG2   1 
ATOM   1344  C  CD1   . ILE A 1  170  ? 155.248 102.107 159.222 1.00 35.92  ? 170  ILE A CD1   1 
ATOM   1345  N  N     . ARG A 1  171  ? 158.014 97.640  157.116 1.00 36.06  ? 171  ARG A N     1 
ATOM   1346  C  CA    . ARG A 1  171  ? 158.321 96.668  156.074 1.00 36.42  ? 171  ARG A CA    1 
ATOM   1347  C  C     . ARG A 1  171  ? 158.516 95.276  156.653 1.00 37.94  ? 171  ARG A C     1 
ATOM   1348  O  O     . ARG A 1  171  ? 158.027 94.289  156.092 1.00 37.28  ? 171  ARG A O     1 
ATOM   1349  C  CB    . ARG A 1  171  ? 159.567 97.104  155.309 1.00 36.75  ? 171  ARG A CB    1 
ATOM   1350  C  CG    . ARG A 1  171  ? 160.282 95.984  154.583 1.00 35.04  ? 171  ARG A CG    1 
ATOM   1351  C  CD    . ARG A 1  171  ? 161.457 96.520  153.792 1.00 38.24  ? 171  ARG A CD    1 
ATOM   1352  N  NE    . ARG A 1  171  ? 161.051 97.126  152.531 1.00 39.75  ? 171  ARG A NE    1 
ATOM   1353  C  CZ    . ARG A 1  171  ? 161.587 96.830  151.356 1.00 39.49  ? 171  ARG A CZ    1 
ATOM   1354  N  NH1   . ARG A 1  171  ? 162.565 95.947  151.247 1.00 37.78  ? 171  ARG A NH1   1 
ATOM   1355  N  NH2   . ARG A 1  171  ? 161.131 97.434  150.264 1.00 37.82  ? 171  ARG A NH2   1 
ATOM   1356  N  N     . GLU A 1  172  ? 159.240 95.173  157.772 1.00 39.85  ? 172  GLU A N     1 
ATOM   1357  C  CA    . GLU A 1  172  ? 159.451 93.874  158.403 1.00 40.44  ? 172  GLU A CA    1 
ATOM   1358  C  C     . GLU A 1  172  ? 158.138 93.277  158.892 1.00 37.41  ? 172  GLU A C     1 
ATOM   1359  O  O     . GLU A 1  172  ? 157.925 92.063  158.802 1.00 36.73  ? 172  GLU A O     1 
ATOM   1360  C  CB    . GLU A 1  172  ? 160.440 94.017  159.556 1.00 39.11  ? 172  GLU A CB    1 
ATOM   1361  C  CG    . GLU A 1  172  ? 161.886 93.826  159.156 1.00 40.25  ? 172  GLU A CG    1 
ATOM   1362  C  CD    . GLU A 1  172  ? 162.447 92.509  159.634 1.00 41.57  ? 172  GLU A CD    1 
ATOM   1363  O  OE1   . GLU A 1  172  ? 163.657 92.277  159.449 1.00 38.87  ? 172  GLU A OE1   1 
ATOM   1364  O  OE2   . GLU A 1  172  ? 161.677 91.706  160.202 1.00 42.47  ? 172  GLU A OE2   1 
ATOM   1365  N  N     . ILE A 1  173  ? 157.247 94.121  159.412 1.00 31.26  ? 173  ILE A N     1 
ATOM   1366  C  CA    . ILE A 1  173  ? 155.929 93.664  159.836 1.00 34.30  ? 173  ILE A CA    1 
ATOM   1367  C  C     . ILE A 1  173  ? 155.156 93.113  158.646 1.00 38.07  ? 173  ILE A C     1 
ATOM   1368  O  O     . ILE A 1  173  ? 154.598 92.012  158.699 1.00 37.59  ? 173  ILE A O     1 
ATOM   1369  C  CB    . ILE A 1  173  ? 155.165 94.821  160.503 1.00 34.07  ? 173  ILE A CB    1 
ATOM   1370  C  CG1   . ILE A 1  173  ? 155.451 94.879  161.992 1.00 35.07  ? 173  ILE A CG1   1 
ATOM   1371  C  CG2   . ILE A 1  173  ? 153.674 94.665  160.310 1.00 33.97  ? 173  ILE A CG2   1 
ATOM   1372  C  CD1   . ILE A 1  173  ? 154.717 95.998  162.671 1.00 34.68  ? 173  ILE A CD1   1 
ATOM   1373  N  N     . PHE A 1  174  ? 155.131 93.870  157.545 1.00 38.06  ? 174  PHE A N     1 
ATOM   1374  C  CA    . PHE A 1  174  ? 154.307 93.511  156.397 1.00 33.75  ? 174  PHE A CA    1 
ATOM   1375  C  C     . PHE A 1  174  ? 154.873 92.336  155.621 1.00 35.25  ? 174  PHE A C     1 
ATOM   1376  O  O     . PHE A 1  174  ? 154.122 91.664  154.910 1.00 37.26  ? 174  PHE A O     1 
ATOM   1377  C  CB    . PHE A 1  174  ? 154.156 94.715  155.472 1.00 32.89  ? 174  PHE A CB    1 
ATOM   1378  C  CG    . PHE A 1  174  ? 153.168 95.729  155.955 1.00 32.77  ? 174  PHE A CG    1 
ATOM   1379  C  CD1   . PHE A 1  174  ? 152.235 95.402  156.914 1.00 31.10  ? 174  PHE A CD1   1 
ATOM   1380  C  CD2   . PHE A 1  174  ? 153.192 97.017  155.467 1.00 33.47  ? 174  PHE A CD2   1 
ATOM   1381  C  CE1   . PHE A 1  174  ? 151.336 96.334  157.360 1.00 34.10  ? 174  PHE A CE1   1 
ATOM   1382  C  CE2   . PHE A 1  174  ? 152.296 97.951  155.913 1.00 33.84  ? 174  PHE A CE2   1 
ATOM   1383  C  CZ    . PHE A 1  174  ? 151.368 97.610  156.860 1.00 35.51  ? 174  PHE A CZ    1 
ATOM   1384  N  N     . SER A 1  175  ? 156.173 92.071  155.739 1.00 34.63  ? 175  SER A N     1 
ATOM   1385  C  CA    . SER A 1  175  ? 156.765 90.974  154.988 1.00 33.43  ? 175  SER A CA    1 
ATOM   1386  C  C     . SER A 1  175  ? 156.328 89.613  155.499 1.00 34.17  ? 175  SER A C     1 
ATOM   1387  O  O     . SER A 1  175  ? 156.536 88.612  154.808 1.00 35.76  ? 175  SER A O     1 
ATOM   1388  C  CB    . SER A 1  175  ? 158.284 91.063  155.032 1.00 35.97  ? 175  SER A CB    1 
ATOM   1389  O  OG    . SER A 1  175  ? 158.859 89.838  154.625 1.00 38.30  ? 175  SER A OG    1 
ATOM   1390  N  N     . ARG A 1  176  ? 155.736 89.548  156.684 1.00 38.89  ? 176  ARG A N     1 
ATOM   1391  C  CA    . ARG A 1  176  ? 155.344 88.280  157.276 1.00 40.85  ? 176  ARG A CA    1 
ATOM   1392  C  C     . ARG A 1  176  ? 153.920 87.878  156.927 1.00 42.64  ? 176  ARG A C     1 
ATOM   1393  O  O     . ARG A 1  176  ? 153.472 86.811  157.357 1.00 44.89  ? 176  ARG A O     1 
ATOM   1394  C  CB    . ARG A 1  176  ? 155.514 88.344  158.796 1.00 39.98  ? 176  ARG A CB    1 
ATOM   1395  C  CG    . ARG A 1  176  ? 156.961 88.277  159.260 1.00 40.43  ? 176  ARG A CG    1 
ATOM   1396  C  CD    . ARG A 1  176  ? 157.056 88.112  160.763 1.00 41.33  ? 176  ARG A CD    1 
ATOM   1397  N  NE    . ARG A 1  176  ? 156.540 89.269  161.486 1.00 42.06  ? 176  ARG A NE    1 
ATOM   1398  C  CZ    . ARG A 1  176  ? 157.292 90.251  161.964 1.00 41.76  ? 176  ARG A CZ    1 
ATOM   1399  N  NH1   . ARG A 1  176  ? 158.603 90.258  161.804 1.00 39.32  ? 176  ARG A NH1   1 
ATOM   1400  N  NH2   . ARG A 1  176  ? 156.714 91.247  162.627 1.00 42.47  ? 176  ARG A NH2   1 
ATOM   1401  N  N     . VAL A 1  177  ? 153.214 88.691  156.146 1.00 38.69  ? 177  VAL A N     1 
ATOM   1402  C  CA    . VAL A 1  177  ? 151.815 88.445  155.808 1.00 37.26  ? 177  VAL A CA    1 
ATOM   1403  C  C     . VAL A 1  177  ? 151.756 87.522  154.599 1.00 33.51  ? 177  VAL A C     1 
ATOM   1404  O  O     . VAL A 1  177  ? 152.433 87.758  153.596 1.00 35.45  ? 177  VAL A O     1 
ATOM   1405  C  CB    . VAL A 1  177  ? 151.081 89.765  155.537 1.00 35.20  ? 177  VAL A CB    1 
ATOM   1406  C  CG1   . VAL A 1  177  ? 149.813 89.526  154.739 1.00 34.32  ? 177  VAL A CG1   1 
ATOM   1407  C  CG2   . VAL A 1  177  ? 150.778 90.475  156.837 1.00 35.12  ? 177  VAL A CG2   1 
ATOM   1408  N  N     . THR A 1  178  ? 150.956 86.463  154.694 1.00 38.03  ? 178  THR A N     1 
ATOM   1409  C  CA    . THR A 1  178  ? 150.847 85.493  153.612 1.00 39.61  ? 178  THR A CA    1 
ATOM   1410  C  C     . THR A 1  178  ? 149.867 85.969  152.544 1.00 40.02  ? 178  THR A C     1 
ATOM   1411  O  O     . THR A 1  178  ? 149.026 86.839  152.775 1.00 40.93  ? 178  THR A O     1 
ATOM   1412  C  CB    . THR A 1  178  ? 150.401 84.132  154.141 1.00 38.02  ? 178  THR A CB    1 
ATOM   1413  O  OG1   . THR A 1  178  ? 149.154 84.275  154.829 1.00 38.60  ? 178  THR A OG1   1 
ATOM   1414  C  CG2   . THR A 1  178  ? 151.435 83.573  155.098 1.00 37.77  ? 178  THR A CG2   1 
ATOM   1415  N  N     . TYR A 1  179  ? 149.979 85.365  151.360 1.00 42.08  ? 179  TYR A N     1 
ATOM   1416  C  CA    . TYR A 1  179  ? 149.131 85.764  150.242 1.00 42.70  ? 179  TYR A CA    1 
ATOM   1417  C  C     . TYR A 1  179  ? 147.674 85.385  150.468 1.00 43.59  ? 179  TYR A C     1 
ATOM   1418  O  O     . TYR A 1  179  ? 146.780 86.003  149.883 1.00 41.21  ? 179  TYR A O     1 
ATOM   1419  C  CB    . TYR A 1  179  ? 149.640 85.139  148.945 1.00 40.82  ? 179  TYR A CB    1 
ATOM   1420  C  CG    . TYR A 1  179  ? 150.721 85.944  148.265 1.00 42.63  ? 179  TYR A CG    1 
ATOM   1421  C  CD1   . TYR A 1  179  ? 150.445 87.180  147.700 1.00 41.10  ? 179  TYR A CD1   1 
ATOM   1422  C  CD2   . TYR A 1  179  ? 152.016 85.461  148.176 1.00 41.35  ? 179  TYR A CD2   1 
ATOM   1423  C  CE1   . TYR A 1  179  ? 151.429 87.912  147.079 1.00 40.56  ? 179  TYR A CE1   1 
ATOM   1424  C  CE2   . TYR A 1  179  ? 153.004 86.184  147.553 1.00 39.85  ? 179  TYR A CE2   1 
ATOM   1425  C  CZ    . TYR A 1  179  ? 152.708 87.409  147.007 1.00 42.34  ? 179  TYR A CZ    1 
ATOM   1426  O  OH    . TYR A 1  179  ? 153.701 88.130  146.385 1.00 42.59  ? 179  TYR A OH    1 
ATOM   1427  N  N     . ASP A 1  180  ? 147.418 84.369  151.292 1.00 43.76  ? 180  ASP A N     1 
ATOM   1428  C  CA    . ASP A 1  180  ? 146.045 83.972  151.584 1.00 41.42  ? 180  ASP A CA    1 
ATOM   1429  C  C     . ASP A 1  180  ? 145.284 85.084  152.297 1.00 41.78  ? 180  ASP A C     1 
ATOM   1430  O  O     . ASP A 1  180  ? 144.131 85.376  151.956 1.00 44.32  ? 180  ASP A O     1 
ATOM   1431  C  CB    . ASP A 1  180  ? 146.051 82.698  152.421 1.00 41.82  ? 180  ASP A CB    1 
ATOM   1432  C  CG    . ASP A 1  180  ? 144.770 81.911  152.297 1.00 45.23  ? 180  ASP A CG    1 
ATOM   1433  O  OD1   . ASP A 1  180  ? 144.245 81.477  153.340 1.00 44.14  ? 180  ASP A OD1   1 
ATOM   1434  O  OD2   . ASP A 1  180  ? 144.286 81.728  151.161 1.00 46.50  ? 180  ASP A OD2   1 
ATOM   1435  N  N     . THR A 1  181  ? 145.921 85.723  153.280 1.00 36.21  ? 181  THR A N     1 
ATOM   1436  C  CA    . THR A 1  181  ? 145.294 86.840  153.976 1.00 36.10  ? 181  THR A CA    1 
ATOM   1437  C  C     . THR A 1  181  ? 144.989 87.982  153.020 1.00 40.44  ? 181  THR A C     1 
ATOM   1438  O  O     . THR A 1  181  ? 143.895 88.557  153.054 1.00 41.23  ? 181  THR A O     1 
ATOM   1439  C  CB    . THR A 1  181  ? 146.205 87.333  155.100 1.00 38.43  ? 181  THR A CB    1 
ATOM   1440  O  OG1   . THR A 1  181  ? 146.520 86.247  155.979 1.00 42.97  ? 181  THR A OG1   1 
ATOM   1441  C  CG2   . THR A 1  181  ? 145.532 88.434  155.888 1.00 38.08  ? 181  THR A CG2   1 
ATOM   1442  N  N     . VAL A 1  182  ? 145.945 88.314  152.148 1.00 38.45  ? 182  VAL A N     1 
ATOM   1443  C  CA    . VAL A 1  182  ? 145.749 89.402  151.198 1.00 36.95  ? 182  VAL A CA    1 
ATOM   1444  C  C     . VAL A 1  182  ? 144.601 89.086  150.251 1.00 36.86  ? 182  VAL A C     1 
ATOM   1445  O  O     . VAL A 1  182  ? 143.727 89.927  150.016 1.00 39.95  ? 182  VAL A O     1 
ATOM   1446  C  CB    . VAL A 1  182  ? 147.052 89.674  150.427 1.00 41.13  ? 182  VAL A CB    1 
ATOM   1447  C  CG1   . VAL A 1  182  ? 146.859 90.810  149.434 1.00 36.50  ? 182  VAL A CG1   1 
ATOM   1448  C  CG2   . VAL A 1  182  ? 148.174 89.993  151.384 1.00 41.38  ? 182  VAL A CG2   1 
ATOM   1449  N  N     . VAL A 1  183  ? 144.574 87.871  149.704 1.00 30.51  ? 183  VAL A N     1 
ATOM   1450  C  CA    . VAL A 1  183  ? 143.555 87.526  148.719 1.00 31.90  ? 183  VAL A CA    1 
ATOM   1451  C  C     . VAL A 1  183  ? 142.172 87.521  149.356 1.00 36.19  ? 183  VAL A C     1 
ATOM   1452  O  O     . VAL A 1  183  ? 141.226 88.116  148.828 1.00 38.30  ? 183  VAL A O     1 
ATOM   1453  C  CB    . VAL A 1  183  ? 143.876 86.174  148.061 1.00 33.30  ? 183  VAL A CB    1 
ATOM   1454  C  CG1   . VAL A 1  183  ? 142.672 85.664  147.305 1.00 29.94  ? 183  VAL A CG1   1 
ATOM   1455  C  CG2   . VAL A 1  183  ? 145.055 86.320  147.121 1.00 33.50  ? 183  VAL A CG2   1 
ATOM   1456  N  N     . LYS A 1  184  ? 142.034 86.872  150.506 1.00 35.64  ? 184  LYS A N     1 
ATOM   1457  C  CA    . LYS A 1  184  ? 140.726 86.708  151.116 1.00 36.62  ? 184  LYS A CA    1 
ATOM   1458  C  C     . LYS A 1  184  ? 140.299 87.911  151.941 1.00 38.01  ? 184  LYS A C     1 
ATOM   1459  O  O     . LYS A 1  184  ? 139.167 87.939  152.434 1.00 39.46  ? 184  LYS A O     1 
ATOM   1460  C  CB    . LYS A 1  184  ? 140.707 85.430  151.958 1.00 35.26  ? 184  LYS A CB    1 
ATOM   1461  C  CG    . LYS A 1  184  ? 140.849 85.615  153.453 1.00 35.45  ? 184  LYS A CG    1 
ATOM   1462  C  CD    . LYS A 1  184  ? 141.479 84.379  154.046 1.00 36.49  ? 184  LYS A CD    1 
ATOM   1463  C  CE    . LYS A 1  184  ? 140.635 83.158  153.740 1.00 38.00  ? 184  LYS A CE    1 
ATOM   1464  N  NZ    . LYS A 1  184  ? 141.417 81.901  153.848 1.00 39.76  ? 184  LYS A NZ    1 
ATOM   1465  N  N     . LEU A 1  185  ? 141.155 88.920  152.077 1.00 33.38  ? 185  LEU A N     1 
ATOM   1466  C  CA    . LEU A 1  185  ? 140.790 90.091  152.860 1.00 34.46  ? 185  LEU A CA    1 
ATOM   1467  C  C     . LEU A 1  185  ? 140.341 91.236  151.956 1.00 38.48  ? 185  LEU A C     1 
ATOM   1468  O  O     . LEU A 1  185  ? 140.081 92.346  152.431 1.00 39.23  ? 185  LEU A O     1 
ATOM   1469  C  CB    . LEU A 1  185  ? 141.956 90.504  153.760 1.00 35.37  ? 185  LEU A CB    1 
ATOM   1470  C  CG    . LEU A 1  185  ? 141.772 91.566  154.838 1.00 36.87  ? 185  LEU A CG    1 
ATOM   1471  C  CD1   . LEU A 1  185  ? 140.423 91.449  155.527 1.00 35.80  ? 185  LEU A CD1   1 
ATOM   1472  C  CD2   . LEU A 1  185  ? 142.890 91.449  155.853 1.00 36.02  ? 185  LEU A CD2   1 
ATOM   1473  N  N     . GLY A 1  186  ? 140.217 90.981  150.657 1.00 37.23  ? 186  GLY A N     1 
ATOM   1474  C  CA    . GLY A 1  186  ? 139.666 91.972  149.753 1.00 34.17  ? 186  GLY A CA    1 
ATOM   1475  C  C     . GLY A 1  186  ? 140.539 92.325  148.569 1.00 34.70  ? 186  GLY A C     1 
ATOM   1476  O  O     . GLY A 1  186  ? 140.037 92.527  147.462 1.00 34.21  ? 186  GLY A O     1 
ATOM   1477  N  N     . ARG A 1  187  ? 141.845 92.396  148.781 1.00 37.59  ? 187  ARG A N     1 
ATOM   1478  C  CA    . ARG A 1  187  ? 142.772 92.845  147.757 1.00 36.36  ? 187  ARG A CA    1 
ATOM   1479  C  C     . ARG A 1  187  ? 143.151 91.699  146.826 1.00 35.23  ? 187  ARG A C     1 
ATOM   1480  O  O     . ARG A 1  187  ? 142.743 90.552  147.004 1.00 36.34  ? 187  ARG A O     1 
ATOM   1481  C  CB    . ARG A 1  187  ? 144.013 93.442  148.405 1.00 34.74  ? 187  ARG A CB    1 
ATOM   1482  C  CG    . ARG A 1  187  ? 143.704 94.593  149.327 1.00 35.44  ? 187  ARG A CG    1 
ATOM   1483  C  CD    . ARG A 1  187  ? 143.570 95.881  148.565 1.00 34.25  ? 187  ARG A CD    1 
ATOM   1484  N  NE    . ARG A 1  187  ? 143.053 96.956  149.398 1.00 33.44  ? 187  ARG A NE    1 
ATOM   1485  C  CZ    . ARG A 1  187  ? 141.841 97.472  149.276 1.00 37.17  ? 187  ARG A CZ    1 
ATOM   1486  N  NH1   . ARG A 1  187  ? 140.998 97.042  148.352 1.00 35.09  ? 187  ARG A NH1   1 
ATOM   1487  N  NH2   . ARG A 1  187  ? 141.469 98.455  150.089 1.00 38.98  ? 187  ARG A NH2   1 
ATOM   1488  N  N     . SER A 1  188  ? 143.930 92.031  145.808 1.00 35.15  ? 188  SER A N     1 
ATOM   1489  C  CA    . SER A 1  188  ? 144.433 91.051  144.861 1.00 37.29  ? 188  SER A CA    1 
ATOM   1490  C  C     . SER A 1  188  ? 145.874 90.697  145.194 1.00 35.82  ? 188  SER A C     1 
ATOM   1491  O  O     . SER A 1  188  ? 146.476 91.232  146.124 1.00 38.55  ? 188  SER A O     1 
ATOM   1492  C  CB    . SER A 1  188  ? 144.332 91.575  143.426 1.00 36.87  ? 188  SER A CB    1 
ATOM   1493  O  OG    . SER A 1  188  ? 145.164 92.702  143.229 1.00 38.06  ? 188  SER A OG    1 
ATOM   1494  N  N     . LYS A 1  189  ? 146.428 89.780  144.407 1.00 40.22  ? 189  LYS A N     1 
ATOM   1495  C  CA    . LYS A 1  189  ? 147.800 89.350  144.622 1.00 41.73  ? 189  LYS A CA    1 
ATOM   1496  C  C     . LYS A 1  189  ? 148.800 90.477  144.411 1.00 41.93  ? 189  LYS A C     1 
ATOM   1497  O  O     . LYS A 1  189  ? 149.801 90.542  145.129 1.00 46.48  ? 189  LYS A O     1 
ATOM   1498  C  CB    . LYS A 1  189  ? 148.119 88.174  143.702 1.00 41.87  ? 189  LYS A CB    1 
ATOM   1499  C  CG    . LYS A 1  189  ? 149.580 87.790  143.663 1.00 42.20  ? 189  LYS A CG    1 
ATOM   1500  C  CD    . LYS A 1  189  ? 149.761 86.354  143.202 1.00 43.41  ? 189  LYS A CD    1 
ATOM   1501  C  CE    . LYS A 1  189  ? 150.891 85.674  143.955 1.00 43.57  ? 189  LYS A CE    1 
ATOM   1502  N  NZ    . LYS A 1  189  ? 152.155 85.707  143.177 1.00 42.43  ? 189  LYS A NZ    1 
ATOM   1503  N  N     . ASN A 1  190  ? 148.545 91.376  143.470 1.00 40.17  ? 190  ASN A N     1 
ATOM   1504  C  CA    . ASN A 1  190  ? 149.457 92.467  143.161 1.00 39.60  ? 190  ASN A CA    1 
ATOM   1505  C  C     . ASN A 1  190  ? 149.346 93.633  144.133 1.00 42.06  ? 190  ASN A C     1 
ATOM   1506  O  O     . ASN A 1  190  ? 150.135 94.576  144.037 1.00 43.69  ? 190  ASN A O     1 
ATOM   1507  C  CB    . ASN A 1  190  ? 149.210 92.966  141.737 1.00 41.32  ? 190  ASN A CB    1 
ATOM   1508  C  CG    . ASN A 1  190  ? 149.411 91.882  140.703 1.00 43.95  ? 190  ASN A CG    1 
ATOM   1509  O  OD1   . ASN A 1  190  ? 150.377 91.129  140.763 1.00 44.01  ? 190  ASN A OD1   1 
ATOM   1510  N  ND2   . ASN A 1  190  ? 148.495 91.794  139.749 1.00 44.29  ? 190  ASN A ND2   1 
ATOM   1511  N  N     . SER A 1  191  ? 148.394 93.599  145.061 1.00 36.98  ? 191  SER A N     1 
ATOM   1512  C  CA    . SER A 1  191  ? 148.226 94.663  146.041 1.00 38.91  ? 191  SER A CA    1 
ATOM   1513  C  C     . SER A 1  191  ? 148.768 94.266  147.409 1.00 39.00  ? 191  SER A C     1 
ATOM   1514  O  O     . SER A 1  191  ? 148.261 94.722  148.436 1.00 38.38  ? 191  SER A O     1 
ATOM   1515  C  CB    . SER A 1  191  ? 146.757 95.066  146.148 1.00 39.01  ? 191  SER A CB    1 
ATOM   1516  O  OG    . SER A 1  191  ? 146.476 96.217  145.369 1.00 39.75  ? 191  SER A OG    1 
ATOM   1517  N  N     . HIS A 1  192  ? 149.806 93.435  147.432 1.00 41.66  ? 192  HIS A N     1 
ATOM   1518  C  CA    . HIS A 1  192  ? 150.386 92.990  148.690 1.00 42.90  ? 192  HIS A CA    1 
ATOM   1519  C  C     . HIS A 1  192  ? 150.916 94.188  149.473 1.00 42.90  ? 192  HIS A C     1 
ATOM   1520  O  O     . HIS A 1  192  ? 151.530 95.086  148.889 1.00 44.18  ? 192  HIS A O     1 
ATOM   1521  C  CB    . HIS A 1  192  ? 151.518 91.998  148.433 1.00 40.40  ? 192  HIS A CB    1 
ATOM   1522  C  CG    . HIS A 1  192  ? 151.902 91.193  149.633 1.00 43.70  ? 192  HIS A CG    1 
ATOM   1523  N  ND1   . HIS A 1  192  ? 152.666 91.706  150.658 1.00 41.86  ? 192  HIS A ND1   1 
ATOM   1524  C  CD2   . HIS A 1  192  ? 151.658 89.902  149.958 1.00 45.41  ? 192  HIS A CD2   1 
ATOM   1525  C  CE1   . HIS A 1  192  ? 152.858 90.773  151.573 1.00 42.81  ? 192  HIS A CE1   1 
ATOM   1526  N  NE2   . HIS A 1  192  ? 152.260 89.667  151.170 1.00 46.29  ? 192  HIS A NE2   1 
ATOM   1527  N  N     . PRO A 1  193  ? 150.700 94.235  150.790 1.00 38.92  ? 193  PRO A N     1 
ATOM   1528  C  CA    . PRO A 1  193  ? 151.122 95.416  151.559 1.00 37.67  ? 193  PRO A CA    1 
ATOM   1529  C  C     . PRO A 1  193  ? 152.623 95.633  151.580 1.00 37.66  ? 193  PRO A C     1 
ATOM   1530  O  O     . PRO A 1  193  ? 153.073 96.742  151.887 1.00 36.91  ? 193  PRO A O     1 
ATOM   1531  C  CB    . PRO A 1  193  ? 150.581 95.128  152.965 1.00 36.64  ? 193  PRO A CB    1 
ATOM   1532  C  CG    . PRO A 1  193  ? 150.408 93.666  153.012 1.00 37.60  ? 193  PRO A CG    1 
ATOM   1533  C  CD    . PRO A 1  193  ? 150.004 93.256  151.637 1.00 38.61  ? 193  PRO A CD    1 
ATOM   1534  N  N     . GLU A 1  194  ? 153.418 94.612  151.268 1.00 38.11  ? 194  GLU A N     1 
ATOM   1535  C  CA    . GLU A 1  194  ? 154.863 94.761  151.361 1.00 36.32  ? 194  GLU A CA    1 
ATOM   1536  C  C     . GLU A 1  194  ? 155.425 95.698  150.302 1.00 40.32  ? 194  GLU A C     1 
ATOM   1537  O  O     . GLU A 1  194  ? 156.567 96.144  150.435 1.00 41.62  ? 194  GLU A O     1 
ATOM   1538  C  CB    . GLU A 1  194  ? 155.542 93.404  151.248 1.00 37.86  ? 194  GLU A CB    1 
ATOM   1539  C  CG    . GLU A 1  194  ? 155.693 92.920  149.831 1.00 38.70  ? 194  GLU A CG    1 
ATOM   1540  C  CD    . GLU A 1  194  ? 156.609 91.726  149.743 1.00 43.89  ? 194  GLU A CD    1 
ATOM   1541  O  OE1   . GLU A 1  194  ? 157.134 91.304  150.794 1.00 44.72  ? 194  GLU A OE1   1 
ATOM   1542  O  OE2   . GLU A 1  194  ? 156.811 91.212  148.628 1.00 44.68  ? 194  GLU A OE2   1 
ATOM   1543  N  N     . LYS A 1  195  ? 154.663 95.998  149.251 1.00 37.29  ? 195  LYS A N     1 
ATOM   1544  C  CA    . LYS A 1  195  ? 155.110 96.955  148.249 1.00 30.87  ? 195  LYS A CA    1 
ATOM   1545  C  C     . LYS A 1  195  ? 154.880 98.389  148.684 1.00 32.96  ? 195  LYS A C     1 
ATOM   1546  O  O     . LYS A 1  195  ? 155.239 99.306  147.944 1.00 39.84  ? 195  LYS A O     1 
ATOM   1547  C  CB    . LYS A 1  195  ? 154.404 96.704  146.920 1.00 32.68  ? 195  LYS A CB    1 
ATOM   1548  C  CG    . LYS A 1  195  ? 154.589 95.304  146.395 1.00 38.71  ? 195  LYS A CG    1 
ATOM   1549  C  CD    . LYS A 1  195  ? 153.721 95.031  145.183 1.00 35.71  ? 195  LYS A CD    1 
ATOM   1550  C  CE    . LYS A 1  195  ? 154.387 95.465  143.911 1.00 35.60  ? 195  LYS A CE    1 
ATOM   1551  N  NZ    . LYS A 1  195  ? 153.785 94.781  142.737 1.00 35.74  ? 195  LYS A NZ    1 
ATOM   1552  N  N     . LEU A 1  196  ? 154.286 98.601  149.854 1.00 32.30  ? 196  LEU A N     1 
ATOM   1553  C  CA    . LEU A 1  196  ? 154.007 99.940  150.346 1.00 31.06  ? 196  LEU A CA    1 
ATOM   1554  C  C     . LEU A 1  196  ? 155.204 100.569 151.044 1.00 34.81  ? 196  LEU A C     1 
ATOM   1555  O  O     . LEU A 1  196  ? 155.101 101.707 151.510 1.00 34.25  ? 196  LEU A O     1 
ATOM   1556  C  CB    . LEU A 1  196  ? 152.800 99.914  151.290 1.00 31.39  ? 196  LEU A CB    1 
ATOM   1557  C  CG    . LEU A 1  196  ? 151.365 99.707  150.767 1.00 34.13  ? 196  LEU A CG    1 
ATOM   1558  C  CD1   . LEU A 1  196  ? 151.247 98.665  149.674 1.00 32.50  ? 196  LEU A CD1   1 
ATOM   1559  C  CD2   . LEU A 1  196  ? 150.431 99.347  151.909 1.00 32.94  ? 196  LEU A CD2   1 
ATOM   1560  N  N     . VAL A 1  197  ? 156.328 99.862  151.124 1.00 33.36  ? 197  VAL A N     1 
ATOM   1561  C  CA    . VAL A 1  197  ? 157.576 100.392 151.658 1.00 31.02  ? 197  VAL A CA    1 
ATOM   1562  C  C     . VAL A 1  197  ? 158.629 100.298 150.565 1.00 31.30  ? 197  VAL A C     1 
ATOM   1563  O  O     . VAL A 1  197  ? 158.812 99.235  149.963 1.00 32.35  ? 197  VAL A O     1 
ATOM   1564  C  CB    . VAL A 1  197  ? 158.020 99.633  152.922 1.00 33.75  ? 197  VAL A CB    1 
ATOM   1565  C  CG1   . VAL A 1  197  ? 159.342 100.168 153.424 1.00 34.01  ? 197  VAL A CG1   1 
ATOM   1566  C  CG2   . VAL A 1  197  ? 156.961 99.749  154.003 1.00 30.72  ? 197  VAL A CG2   1 
ATOM   1567  N  N     . LEU A 1  198  ? 159.317 101.405 150.307 1.00 34.45  ? 198  LEU A N     1 
ATOM   1568  C  CA    . LEU A 1  198  ? 160.204 101.526 149.158 1.00 34.02  ? 198  LEU A CA    1 
ATOM   1569  C  C     . LEU A 1  198  ? 161.645 101.664 149.621 1.00 33.39  ? 198  LEU A C     1 
ATOM   1570  O  O     . LEU A 1  198  ? 161.956 102.532 150.441 1.00 33.20  ? 198  LEU A O     1 
ATOM   1571  C  CB    . LEU A 1  198  ? 159.823 102.738 148.304 1.00 35.79  ? 198  LEU A CB    1 
ATOM   1572  C  CG    . LEU A 1  198  ? 158.564 102.656 147.448 1.00 34.07  ? 198  LEU A CG    1 
ATOM   1573  C  CD1   . LEU A 1  198  ? 158.114 104.049 147.109 1.00 35.50  ? 198  LEU A CD1   1 
ATOM   1574  C  CD2   . LEU A 1  198  ? 158.809 101.852 146.193 1.00 35.32  ? 198  LEU A CD2   1 
ATOM   1575  N  N     . LYS A 1  199  ? 162.523 100.823 149.082 1.00 34.62  ? 199  LYS A N     1 
ATOM   1576  C  CA    . LYS A 1  199  ? 163.955 100.969 149.297 1.00 36.27  ? 199  LYS A CA    1 
ATOM   1577  C  C     . LYS A 1  199  ? 164.707 101.424 148.058 1.00 39.99  ? 199  LYS A C     1 
ATOM   1578  O  O     . LYS A 1  199  ? 165.900 101.725 148.149 1.00 40.63  ? 199  LYS A O     1 
ATOM   1579  C  CB    . LYS A 1  199  ? 164.567 99.659  149.798 1.00 37.17  ? 199  LYS A CB    1 
ATOM   1580  C  CG    . LYS A 1  199  ? 164.436 99.465  151.299 1.00 39.86  ? 199  LYS A CG    1 
ATOM   1581  C  CD    . LYS A 1  199  ? 165.348 98.359  151.793 1.00 39.54  ? 199  LYS A CD    1 
ATOM   1582  C  CE    . LYS A 1  199  ? 166.650 98.920  152.334 1.00 37.38  ? 199  LYS A CE    1 
ATOM   1583  N  NZ    . LYS A 1  199  ? 167.478 99.575  151.295 1.00 37.00  ? 199  LYS A NZ    1 
ATOM   1584  N  N     . ALA A 1  200  ? 164.050 101.455 146.902 1.00 35.59  ? 200  ALA A N     1 
ATOM   1585  C  CA    . ALA A 1  200  ? 164.618 101.989 145.671 1.00 31.41  ? 200  ALA A CA    1 
ATOM   1586  C  C     . ALA A 1  200  ? 163.539 102.805 144.977 1.00 34.18  ? 200  ALA A C     1 
ATOM   1587  O  O     . ALA A 1  200  ? 162.562 102.242 144.477 1.00 38.27  ? 200  ALA A O     1 
ATOM   1588  C  CB    . ALA A 1  200  ? 165.124 100.867 144.768 1.00 31.77  ? 200  ALA A CB    1 
ATOM   1589  N  N     . ILE A 1  201  ? 163.700 104.121 144.949 1.00 30.98  ? 201  ILE A N     1 
ATOM   1590  C  CA    . ILE A 1  201  ? 162.726 104.975 144.289 1.00 30.97  ? 201  ILE A CA    1 
ATOM   1591  C  C     . ILE A 1  201  ? 163.119 105.163 142.829 1.00 32.37  ? 201  ILE A C     1 
ATOM   1592  O  O     . ILE A 1  201  ? 164.218 104.815 142.397 1.00 29.97  ? 201  ILE A O     1 
ATOM   1593  C  CB    . ILE A 1  201  ? 162.554 106.333 144.995 1.00 27.91  ? 201  ILE A CB    1 
ATOM   1594  C  CG1   . ILE A 1  201  ? 163.791 107.202 144.834 1.00 26.98  ? 201  ILE A CG1   1 
ATOM   1595  C  CG2   . ILE A 1  201  ? 162.236 106.132 146.463 1.00 30.73  ? 201  ILE A CG2   1 
ATOM   1596  C  CD1   . ILE A 1  201  ? 163.648 108.538 145.500 1.00 26.81  ? 201  ILE A CD1   1 
ATOM   1597  N  N     . GLN A 1  202  ? 162.184 105.700 142.056 1.00 30.66  ? 202  GLN A N     1 
ATOM   1598  C  CA    . GLN A 1  202  ? 162.346 105.909 140.624 1.00 29.00  ? 202  GLN A CA    1 
ATOM   1599  C  C     . GLN A 1  202  ? 162.675 107.370 140.351 1.00 28.78  ? 202  GLN A C     1 
ATOM   1600  O  O     . GLN A 1  202  ? 162.030 108.266 140.904 1.00 31.67  ? 202  GLN A O     1 
ATOM   1601  C  CB    . GLN A 1  202  ? 161.074 105.499 139.889 1.00 23.89  ? 202  GLN A CB    1 
ATOM   1602  C  CG    . GLN A 1  202  ? 161.240 105.318 138.409 1.00 24.42  ? 202  GLN A CG    1 
ATOM   1603  C  CD    . GLN A 1  202  ? 159.968 105.602 137.664 1.00 26.45  ? 202  GLN A CD    1 
ATOM   1604  O  OE1   . GLN A 1  202  ? 159.513 106.738 137.607 1.00 28.76  ? 202  GLN A OE1   1 
ATOM   1605  N  NE2   . GLN A 1  202  ? 159.389 104.571 137.074 1.00 26.82  ? 202  GLN A NE2   1 
ATOM   1606  N  N     . ILE A 1  203  ? 163.677 107.608 139.513 1.00 23.81  ? 203  ILE A N     1 
ATOM   1607  C  CA    . ILE A 1  203  ? 163.998 108.963 139.073 1.00 25.33  ? 203  ILE A CA    1 
ATOM   1608  C  C     . ILE A 1  203  ? 163.307 109.209 137.737 1.00 27.24  ? 203  ILE A C     1 
ATOM   1609  O  O     . ILE A 1  203  ? 163.627 108.544 136.743 1.00 27.64  ? 203  ILE A O     1 
ATOM   1610  C  CB    . ILE A 1  203  ? 165.515 109.182 138.970 1.00 25.24  ? 203  ILE A CB    1 
ATOM   1611  C  CG1   . ILE A 1  203  ? 166.207 108.799 140.277 1.00 27.66  ? 203  ILE A CG1   1 
ATOM   1612  C  CG2   . ILE A 1  203  ? 165.814 110.629 138.659 1.00 27.13  ? 203  ILE A CG2   1 
ATOM   1613  C  CD1   . ILE A 1  203  ? 165.837 109.681 141.445 1.00 27.53  ? 203  ILE A CD1   1 
ATOM   1614  N  N     . PRO A 1  204  ? 162.370 110.145 137.661 1.00 28.50  ? 204  PRO A N     1 
ATOM   1615  C  CA    . PRO A 1  204  ? 161.597 110.326 136.432 1.00 23.24  ? 204  PRO A CA    1 
ATOM   1616  C  C     . PRO A 1  204  ? 162.482 110.788 135.290 1.00 24.18  ? 204  PRO A C     1 
ATOM   1617  O  O     . PRO A 1  204  ? 163.493 111.467 135.514 1.00 29.79  ? 204  PRO A O     1 
ATOM   1618  C  CB    . PRO A 1  204  ? 160.569 111.398 136.819 1.00 27.43  ? 204  PRO A CB    1 
ATOM   1619  C  CG    . PRO A 1  204  ? 161.171 112.109 137.967 1.00 26.35  ? 204  PRO A CG    1 
ATOM   1620  C  CD    . PRO A 1  204  ? 161.974 111.095 138.713 1.00 26.28  ? 204  PRO A CD    1 
ATOM   1621  N  N     . PRO A 1  205  ? 162.143 110.431 134.052 1.00 21.17  ? 205  PRO A N     1 
ATOM   1622  C  CA    . PRO A 1  205  ? 162.972 110.837 132.915 1.00 22.04  ? 205  PRO A CA    1 
ATOM   1623  C  C     . PRO A 1  205  ? 163.009 112.347 132.758 1.00 24.07  ? 205  PRO A C     1 
ATOM   1624  O  O     . PRO A 1  205  ? 162.117 113.062 133.213 1.00 26.96  ? 205  PRO A O     1 
ATOM   1625  C  CB    . PRO A 1  205  ? 162.290 110.163 131.721 1.00 21.63  ? 205  PRO A CB    1 
ATOM   1626  C  CG    . PRO A 1  205  ? 160.942 109.831 132.177 1.00 22.11  ? 205  PRO A CG    1 
ATOM   1627  C  CD    . PRO A 1  205  ? 161.033 109.564 133.631 1.00 21.47  ? 205  PRO A CD    1 
ATOM   1628  N  N     . ILE A 1  206  ? 164.078 112.832 132.125 1.00 23.76  ? 206  ILE A N     1 
ATOM   1629  C  CA    . ILE A 1  206  ? 164.289 114.268 131.998 1.00 24.46  ? 206  ILE A CA    1 
ATOM   1630  C  C     . ILE A 1  206  ? 163.224 114.922 131.128 1.00 27.10  ? 206  ILE A C     1 
ATOM   1631  O  O     . ILE A 1  206  ? 162.948 116.113 131.282 1.00 28.29  ? 206  ILE A O     1 
ATOM   1632  C  CB    . ILE A 1  206  ? 165.712 114.544 131.464 1.00 25.33  ? 206  ILE A CB    1 
ATOM   1633  C  CG1   . ILE A 1  206  ? 166.744 113.803 132.306 1.00 25.81  ? 206  ILE A CG1   1 
ATOM   1634  C  CG2   . ILE A 1  206  ? 166.040 116.009 131.532 1.00 24.03  ? 206  ILE A CG2   1 
ATOM   1635  C  CD1   . ILE A 1  206  ? 167.622 112.883 131.518 1.00 26.07  ? 206  ILE A CD1   1 
ATOM   1636  N  N     . SER A 1  207  ? 162.600 114.164 130.224 1.00 25.54  ? 207  SER A N     1 
ATOM   1637  C  CA    . SER A 1  207  ? 161.535 114.706 129.389 1.00 19.14  ? 207  SER A CA    1 
ATOM   1638  C  C     . SER A 1  207  ? 160.366 115.230 130.209 1.00 23.13  ? 207  SER A C     1 
ATOM   1639  O  O     . SER A 1  207  ? 159.591 116.051 129.712 1.00 27.17  ? 207  SER A O     1 
ATOM   1640  C  CB    . SER A 1  207  ? 161.049 113.634 128.421 1.00 23.00  ? 207  SER A CB    1 
ATOM   1641  O  OG    . SER A 1  207  ? 160.514 112.531 129.117 1.00 20.61  ? 207  SER A OG    1 
ATOM   1642  N  N     . ILE A 1  208  ? 160.215 114.759 131.443 1.00 18.28  ? 208  ILE A N     1 
ATOM   1643  C  CA    . ILE A 1  208  ? 159.191 115.257 132.351 1.00 19.20  ? 208  ILE A CA    1 
ATOM   1644  C  C     . ILE A 1  208  ? 159.683 116.430 133.189 1.00 21.07  ? 208  ILE A C     1 
ATOM   1645  O  O     . ILE A 1  208  ? 158.864 117.174 133.745 1.00 27.69  ? 208  ILE A O     1 
ATOM   1646  C  CB    . ILE A 1  208  ? 158.678 114.065 133.185 1.00 19.73  ? 208  ILE A CB    1 
ATOM   1647  C  CG1   . ILE A 1  208  ? 157.441 113.475 132.511 1.00 21.73  ? 208  ILE A CG1   1 
ATOM   1648  C  CG2   . ILE A 1  208  ? 158.423 114.408 134.644 1.00 16.00  ? 208  ILE A CG2   1 
ATOM   1649  C  CD1   . ILE A 1  208  ? 157.741 112.760 131.231 1.00 24.96  ? 208  ILE A CD1   1 
ATOM   1650  N  N     . ARG A 1  209  ? 160.991 116.648 133.255 1.00 21.53  ? 209  ARG A N     1 
ATOM   1651  C  CA    . ARG A 1  209  ? 161.568 117.801 133.943 1.00 24.20  ? 209  ARG A CA    1 
ATOM   1652  C  C     . ARG A 1  209  ? 162.618 118.466 133.060 1.00 29.60  ? 209  ARG A C     1 
ATOM   1653  O  O     . ARG A 1  209  ? 163.802 118.504 133.401 1.00 29.26  ? 209  ARG A O     1 
ATOM   1654  C  CB    . ARG A 1  209  ? 162.181 117.360 135.265 1.00 23.69  ? 209  ARG A CB    1 
ATOM   1655  C  CG    . ARG A 1  209  ? 162.918 116.064 135.117 1.00 23.79  ? 209  ARG A CG    1 
ATOM   1656  C  CD    . ARG A 1  209  ? 163.359 115.518 136.422 1.00 25.46  ? 209  ARG A CD    1 
ATOM   1657  N  NE    . ARG A 1  209  ? 164.017 114.237 136.234 1.00 25.16  ? 209  ARG A NE    1 
ATOM   1658  C  CZ    . ARG A 1  209  ? 165.328 114.090 136.127 1.00 25.26  ? 209  ARG A CZ    1 
ATOM   1659  N  NH1   . ARG A 1  209  ? 166.146 115.123 136.198 1.00 25.93  ? 209  ARG A NH1   1 
ATOM   1660  N  NH2   . ARG A 1  209  ? 165.829 112.878 135.950 1.00 23.37  ? 209  ARG A NH2   1 
ATOM   1661  N  N     . PRO A 1  210  ? 162.224 119.012 131.922 1.00 32.34  ? 210  PRO A N     1 
ATOM   1662  C  CA    . PRO A 1  210  ? 163.196 119.739 131.108 1.00 31.87  ? 210  PRO A CA    1 
ATOM   1663  C  C     . PRO A 1  210  ? 163.505 121.082 131.741 1.00 36.07  ? 210  PRO A C     1 
ATOM   1664  O  O     . PRO A 1  210  ? 163.070 121.353 132.864 1.00 37.83  ? 210  PRO A O     1 
ATOM   1665  C  CB    . PRO A 1  210  ? 162.482 119.882 129.764 1.00 27.59  ? 210  PRO A CB    1 
ATOM   1666  C  CG    . PRO A 1  210  ? 161.075 119.928 130.120 1.00 26.61  ? 210  PRO A CG    1 
ATOM   1667  C  CD    . PRO A 1  210  ? 160.884 119.055 131.314 1.00 27.48  ? 210  PRO A CD    1 
ATOM   1668  N  N     . GLY A 1  211  ? 164.258 121.929 131.058 1.00 36.00  ? 211  GLY A N     1 
ATOM   1669  C  CA    . GLY A 1  211  ? 164.549 123.225 131.630 1.00 38.60  ? 211  GLY A CA    1 
ATOM   1670  C  C     . GLY A 1  211  ? 165.625 123.125 132.684 1.00 39.31  ? 211  GLY A C     1 
ATOM   1671  O  O     . GLY A 1  211  ? 165.477 123.619 133.806 1.00 37.68  ? 211  GLY A O     1 
ATOM   1672  N  N     . ILE A 1  212  ? 166.707 122.450 132.325 1.00 40.96  ? 212  ILE A N     1 
ATOM   1673  C  CA    . ILE A 1  212  ? 167.883 122.361 133.166 1.00 41.22  ? 212  ILE A CA    1 
ATOM   1674  C  C     . ILE A 1  212  ? 168.501 123.741 133.373 1.00 42.64  ? 212  ILE A C     1 
ATOM   1675  O  O     . ILE A 1  212  ? 169.062 124.330 132.446 1.00 43.07  ? 212  ILE A O     1 
ATOM   1676  C  CB    . ILE A 1  212  ? 168.899 121.400 132.563 1.00 40.27  ? 212  ILE A CB    1 
ATOM   1677  C  CG1   . ILE A 1  212  ? 168.365 119.970 132.595 1.00 37.40  ? 212  ILE A CG1   1 
ATOM   1678  C  CG2   . ILE A 1  212  ? 170.208 121.531 133.278 1.00 42.71  ? 212  ILE A CG2   1 
ATOM   1679  C  CD1   . ILE A 1  212  ? 169.281 118.969 131.953 1.00 39.10  ? 212  ILE A CD1   1 
ATOM   1680  N  N     . HIS A 1  224  ? 163.182 123.476 135.402 1.00 48.37  ? 224  HIS A N     1 
ATOM   1681  C  CA    . HIS A 1  224  ? 162.094 123.369 136.366 1.00 50.38  ? 224  HIS A CA    1 
ATOM   1682  C  C     . HIS A 1  224  ? 162.624 123.357 137.798 1.00 50.37  ? 224  HIS A C     1 
ATOM   1683  O  O     . HIS A 1  224  ? 163.810 123.129 138.031 1.00 50.72  ? 224  HIS A O     1 
ATOM   1684  C  CB    . HIS A 1  224  ? 161.264 122.108 136.111 1.00 48.30  ? 224  HIS A CB    1 
ATOM   1685  C  CG    . HIS A 1  224  ? 160.537 122.112 134.804 1.00 49.57  ? 224  HIS A CG    1 
ATOM   1686  N  ND1   . HIS A 1  224  ? 159.747 121.062 134.391 1.00 46.90  ? 224  HIS A ND1   1 
ATOM   1687  C  CD2   . HIS A 1  224  ? 160.499 123.026 133.806 1.00 49.83  ? 224  HIS A CD2   1 
ATOM   1688  C  CE1   . HIS A 1  224  ? 159.237 121.337 133.204 1.00 48.50  ? 224  HIS A CE1   1 
ATOM   1689  N  NE2   . HIS A 1  224  ? 159.680 122.522 132.825 1.00 50.01  ? 224  HIS A NE2   1 
ATOM   1690  N  N     . ASP A 1  225  ? 161.738 123.614 138.758 1.00 43.61  ? 225  ASP A N     1 
ATOM   1691  C  CA    . ASP A 1  225  ? 162.106 123.576 140.165 1.00 42.74  ? 225  ASP A CA    1 
ATOM   1692  C  C     . ASP A 1  225  ? 161.949 122.199 140.788 1.00 43.34  ? 225  ASP A C     1 
ATOM   1693  O  O     . ASP A 1  225  ? 162.351 122.011 141.939 1.00 46.41  ? 225  ASP A O     1 
ATOM   1694  C  CB    . ASP A 1  225  ? 161.271 124.582 140.960 1.00 43.91  ? 225  ASP A CB    1 
ATOM   1695  C  CG    . ASP A 1  225  ? 161.779 125.997 140.821 1.00 45.96  ? 225  ASP A CG    1 
ATOM   1696  O  OD1   . ASP A 1  225  ? 163.011 126.189 140.821 1.00 43.96  ? 225  ASP A OD1   1 
ATOM   1697  O  OD2   . ASP A 1  225  ? 160.945 126.921 140.708 1.00 48.44  ? 225  ASP A OD2   1 
ATOM   1698  N  N     . ILE A 1  226  ? 161.358 121.242 140.069 1.00 36.73  ? 226  ILE A N     1 
ATOM   1699  C  CA    . ILE A 1  226  ? 161.299 119.871 140.564 1.00 35.24  ? 226  ILE A CA    1 
ATOM   1700  C  C     . ILE A 1  226  ? 162.678 119.237 140.519 1.00 38.32  ? 226  ILE A C     1 
ATOM   1701  O  O     . ILE A 1  226  ? 162.916 118.203 141.152 1.00 39.76  ? 226  ILE A O     1 
ATOM   1702  C  CB    . ILE A 1  226  ? 160.269 119.049 139.764 1.00 38.98  ? 226  ILE A CB    1 
ATOM   1703  C  CG1   . ILE A 1  226  ? 159.604 118.002 140.657 1.00 37.01  ? 226  ILE A CG1   1 
ATOM   1704  C  CG2   . ILE A 1  226  ? 160.913 118.382 138.560 1.00 36.79  ? 226  ILE A CG2   1 
ATOM   1705  C  CD1   . ILE A 1  226  ? 158.731 118.586 141.727 1.00 38.87  ? 226  ILE A CD1   1 
ATOM   1706  N  N     . ASN A 1  227  ? 163.600 119.825 139.756 1.00 36.43  ? 227  ASN A N     1 
ATOM   1707  C  CA    . ASN A 1  227  ? 164.977 119.355 139.763 1.00 36.42  ? 227  ASN A CA    1 
ATOM   1708  C  C     . ASN A 1  227  ? 165.693 119.699 141.060 1.00 37.69  ? 227  ASN A C     1 
ATOM   1709  O  O     . ASN A 1  227  ? 166.561 118.936 141.494 1.00 38.58  ? 227  ASN A O     1 
ATOM   1710  C  CB    . ASN A 1  227  ? 165.744 119.937 138.580 1.00 34.79  ? 227  ASN A CB    1 
ATOM   1711  C  CG    . ASN A 1  227  ? 165.422 119.244 137.285 1.00 33.55  ? 227  ASN A CG    1 
ATOM   1712  O  OD1   . ASN A 1  227  ? 165.467 118.021 137.197 1.00 33.56  ? 227  ASN A OD1   1 
ATOM   1713  N  ND2   . ASN A 1  227  ? 165.119 120.024 136.260 1.00 34.79  ? 227  ASN A ND2   1 
ATOM   1714  N  N     . ASN A 1  228  ? 165.364 120.834 141.682 1.00 35.86  ? 228  ASN A N     1 
ATOM   1715  C  CA    . ASN A 1  228  ? 165.961 121.157 142.972 1.00 36.13  ? 228  ASN A CA    1 
ATOM   1716  C  C     . ASN A 1  228  ? 165.595 120.117 144.019 1.00 38.37  ? 228  ASN A C     1 
ATOM   1717  O  O     . ASN A 1  228  ? 166.455 119.665 144.783 1.00 36.22  ? 228  ASN A O     1 
ATOM   1718  C  CB    . ASN A 1  228  ? 165.517 122.544 143.438 1.00 37.30  ? 228  ASN A CB    1 
ATOM   1719  C  CG    . ASN A 1  228  ? 165.875 123.639 142.458 1.00 42.21  ? 228  ASN A CG    1 
ATOM   1720  O  OD1   . ASN A 1  228  ? 165.288 124.722 142.482 1.00 41.35  ? 228  ASN A OD1   1 
ATOM   1721  N  ND2   . ASN A 1  228  ? 166.846 123.369 141.594 1.00 41.77  ? 228  ASN A ND2   1 
ATOM   1722  N  N     . VAL A 1  229  ? 164.326 119.714 144.052 1.00 39.74  ? 229  VAL A N     1 
ATOM   1723  C  CA    . VAL A 1  229  ? 163.857 118.792 145.078 1.00 36.00  ? 229  VAL A CA    1 
ATOM   1724  C  C     . VAL A 1  229  ? 164.557 117.448 144.955 1.00 34.97  ? 229  VAL A C     1 
ATOM   1725  O  O     . VAL A 1  229  ? 164.873 116.808 145.961 1.00 37.76  ? 229  VAL A O     1 
ATOM   1726  C  CB    . VAL A 1  229  ? 162.329 118.649 144.997 1.00 33.22  ? 229  VAL A CB    1 
ATOM   1727  C  CG1   . VAL A 1  229  ? 161.795 118.004 146.258 1.00 35.78  ? 229  VAL A CG1   1 
ATOM   1728  C  CG2   . VAL A 1  229  ? 161.696 120.006 144.788 1.00 34.73  ? 229  VAL A CG2   1 
ATOM   1729  N  N     . ILE A 1  230  ? 164.796 116.992 143.727 1.00 34.01  ? 230  ILE A N     1 
ATOM   1730  C  CA    . ILE A 1  230  ? 165.501 115.731 143.532 1.00 35.42  ? 230  ILE A CA    1 
ATOM   1731  C  C     . ILE A 1  230  ? 166.938 115.845 144.025 1.00 37.28  ? 230  ILE A C     1 
ATOM   1732  O  O     . ILE A 1  230  ? 167.452 114.945 144.698 1.00 38.39  ? 230  ILE A O     1 
ATOM   1733  C  CB    . ILE A 1  230  ? 165.442 115.316 142.053 1.00 34.90  ? 230  ILE A CB    1 
ATOM   1734  C  CG1   . ILE A 1  230  ? 164.118 114.632 141.739 1.00 36.47  ? 230  ILE A CG1   1 
ATOM   1735  C  CG2   . ILE A 1  230  ? 166.565 114.360 141.721 1.00 32.19  ? 230  ILE A CG2   1 
ATOM   1736  C  CD1   . ILE A 1  230  ? 163.794 114.610 140.261 1.00 35.98  ? 230  ILE A CD1   1 
ATOM   1737  N  N     . GLN A 1  231  ? 167.605 116.956 143.705 1.00 38.61  ? 231  GLN A N     1 
ATOM   1738  C  CA    . GLN A 1  231  ? 169.012 117.116 144.054 1.00 39.62  ? 231  GLN A CA    1 
ATOM   1739  C  C     . GLN A 1  231  ? 169.213 117.174 145.565 1.00 39.66  ? 231  GLN A C     1 
ATOM   1740  O  O     . GLN A 1  231  ? 170.162 116.584 146.090 1.00 38.73  ? 231  GLN A O     1 
ATOM   1741  C  CB    . GLN A 1  231  ? 169.567 118.368 143.383 1.00 41.66  ? 231  GLN A CB    1 
ATOM   1742  C  CG    . GLN A 1  231  ? 171.068 118.393 143.237 1.00 40.82  ? 231  GLN A CG    1 
ATOM   1743  C  CD    . GLN A 1  231  ? 171.574 119.756 142.833 1.00 44.47  ? 231  GLN A CD    1 
ATOM   1744  O  OE1   . GLN A 1  231  ? 172.688 120.147 143.176 1.00 45.09  ? 231  GLN A OE1   1 
ATOM   1745  N  NE2   . GLN A 1  231  ? 170.752 120.494 142.099 1.00 41.01  ? 231  GLN A NE2   1 
ATOM   1746  N  N     . TYR A 1  232  ? 168.335 117.883 146.281 1.00 39.59  ? 232  TYR A N     1 
ATOM   1747  C  CA    . TYR A 1  232  ? 168.379 117.839 147.739 1.00 40.61  ? 232  TYR A CA    1 
ATOM   1748  C  C     . TYR A 1  232  ? 168.188 116.419 148.240 1.00 41.31  ? 232  TYR A C     1 
ATOM   1749  O  O     . TYR A 1  232  ? 168.959 115.939 149.075 1.00 43.74  ? 232  TYR A O     1 
ATOM   1750  C  CB    . TYR A 1  232  ? 167.298 118.733 148.343 1.00 39.41  ? 232  TYR A CB    1 
ATOM   1751  C  CG    . TYR A 1  232  ? 167.387 120.193 147.986 1.00 41.50  ? 232  TYR A CG    1 
ATOM   1752  C  CD1   . TYR A 1  232  ? 168.578 120.762 147.578 1.00 43.94  ? 232  TYR A CD1   1 
ATOM   1753  C  CD2   . TYR A 1  232  ? 166.266 121.002 148.053 1.00 39.37  ? 232  TYR A CD2   1 
ATOM   1754  C  CE1   . TYR A 1  232  ? 168.651 122.099 147.248 1.00 44.19  ? 232  TYR A CE1   1 
ATOM   1755  C  CE2   . TYR A 1  232  ? 166.328 122.334 147.723 1.00 42.32  ? 232  TYR A CE2   1 
ATOM   1756  C  CZ    . TYR A 1  232  ? 167.522 122.879 147.323 1.00 44.95  ? 232  TYR A CZ    1 
ATOM   1757  O  OH    . TYR A 1  232  ? 167.583 124.212 146.999 1.00 45.41  ? 232  TYR A OH    1 
ATOM   1758  N  N     . LEU A 1  233  ? 167.179 115.723 147.716 1.00 38.95  ? 233  LEU A N     1 
ATOM   1759  C  CA    . LEU A 1  233  ? 166.856 114.383 148.192 1.00 36.73  ? 233  LEU A CA    1 
ATOM   1760  C  C     . LEU A 1  233  ? 168.022 113.428 147.985 1.00 38.28  ? 233  LEU A C     1 
ATOM   1761  O  O     . LEU A 1  233  ? 168.248 112.533 148.804 1.00 41.19  ? 233  LEU A O     1 
ATOM   1762  C  CB    . LEU A 1  233  ? 165.601 113.876 147.480 1.00 37.31  ? 233  LEU A CB    1 
ATOM   1763  C  CG    . LEU A 1  233  ? 165.259 112.385 147.495 1.00 39.78  ? 233  LEU A CG    1 
ATOM   1764  C  CD1   . LEU A 1  233  ? 164.421 112.022 148.707 1.00 38.02  ? 233  LEU A CD1   1 
ATOM   1765  C  CD2   . LEU A 1  233  ? 164.550 111.990 146.215 1.00 38.60  ? 233  LEU A CD2   1 
ATOM   1766  N  N     . VAL A 1  234  ? 168.767 113.596 146.894 1.00 35.44  ? 234  VAL A N     1 
ATOM   1767  C  CA    . VAL A 1  234  ? 169.921 112.740 146.640 1.00 36.94  ? 234  VAL A CA    1 
ATOM   1768  C  C     . VAL A 1  234  ? 171.058 113.070 147.597 1.00 38.84  ? 234  VAL A C     1 
ATOM   1769  O  O     . VAL A 1  234  ? 171.751 112.173 148.092 1.00 40.13  ? 234  VAL A O     1 
ATOM   1770  C  CB    . VAL A 1  234  ? 170.356 112.862 145.169 1.00 37.16  ? 234  VAL A CB    1 
ATOM   1771  C  CG1   . VAL A 1  234  ? 171.790 112.399 144.985 1.00 34.03  ? 234  VAL A CG1   1 
ATOM   1772  C  CG2   . VAL A 1  234  ? 169.422 112.066 144.274 1.00 37.93  ? 234  VAL A CG2   1 
ATOM   1773  N  N     . ARG A 1  235  ? 171.273 114.358 147.874 1.00 40.74  ? 235  ARG A N     1 
ATOM   1774  C  CA    . ARG A 1  235  ? 172.372 114.764 148.746 1.00 39.11  ? 235  ARG A CA    1 
ATOM   1775  C  C     . ARG A 1  235  ? 172.165 114.271 150.171 1.00 39.32  ? 235  ARG A C     1 
ATOM   1776  O  O     . ARG A 1  235  ? 173.059 113.654 150.759 1.00 40.98  ? 235  ARG A O     1 
ATOM   1777  C  CB    . ARG A 1  235  ? 172.518 116.284 148.726 1.00 39.71  ? 235  ARG A CB    1 
ATOM   1778  C  CG    . ARG A 1  235  ? 173.242 116.813 147.511 1.00 38.95  ? 235  ARG A CG    1 
ATOM   1779  C  CD    . ARG A 1  235  ? 174.061 118.036 147.841 1.00 39.08  ? 235  ARG A CD    1 
ATOM   1780  N  NE    . ARG A 1  235  ? 173.337 119.269 147.555 1.00 42.55  ? 235  ARG A NE    1 
ATOM   1781  C  CZ    . ARG A 1  235  ? 172.528 119.883 148.407 1.00 43.15  ? 235  ARG A CZ    1 
ATOM   1782  N  NH1   . ARG A 1  235  ? 172.309 119.404 149.620 1.00 41.24  ? 235  ARG A NH1   1 
ATOM   1783  N  NH2   . ARG A 1  235  ? 171.926 121.009 148.032 1.00 40.30  ? 235  ARG A NH2   1 
ATOM   1784  N  N     . LYS A 1  236  ? 170.990 114.533 150.743 1.00 36.87  ? 236  LYS A N     1 
ATOM   1785  C  CA    . LYS A 1  236  ? 170.728 114.122 152.116 1.00 35.59  ? 236  LYS A CA    1 
ATOM   1786  C  C     . LYS A 1  236  ? 170.587 112.614 152.246 1.00 36.55  ? 236  LYS A C     1 
ATOM   1787  O  O     . LYS A 1  236  ? 170.629 112.099 153.365 1.00 41.22  ? 236  LYS A O     1 
ATOM   1788  C  CB    . LYS A 1  236  ? 169.480 114.831 152.640 1.00 34.93  ? 236  LYS A CB    1 
ATOM   1789  C  CG    . LYS A 1  236  ? 169.344 116.238 152.092 1.00 38.05  ? 236  LYS A CG    1 
ATOM   1790  C  CD    . LYS A 1  236  ? 168.789 117.236 153.087 1.00 37.96  ? 236  LYS A CD    1 
ATOM   1791  C  CE    . LYS A 1  236  ? 168.413 118.534 152.373 1.00 38.87  ? 236  LYS A CE    1 
ATOM   1792  N  NZ    . LYS A 1  236  ? 168.056 119.636 153.308 1.00 37.52  ? 236  LYS A NZ    1 
ATOM   1793  N  N     . ASN A 1  237  ? 170.417 111.897 151.134 1.00 37.63  ? 237  ASN A N     1 
ATOM   1794  C  CA    . ASN A 1  237  ? 170.431 110.439 151.189 1.00 40.27  ? 237  ASN A CA    1 
ATOM   1795  C  C     . ASN A 1  237  ? 171.818 109.919 151.540 1.00 40.26  ? 237  ASN A C     1 
ATOM   1796  O  O     . ASN A 1  237  ? 171.954 108.892 152.213 1.00 38.89  ? 237  ASN A O     1 
ATOM   1797  C  CB    . ASN A 1  237  ? 169.982 109.844 149.855 1.00 39.45  ? 237  ASN A CB    1 
ATOM   1798  C  CG    . ASN A 1  237  ? 169.805 108.338 149.921 1.00 40.48  ? 237  ASN A CG    1 
ATOM   1799  O  OD1   . ASN A 1  237  ? 169.457 107.792 150.963 1.00 41.52  ? 237  ASN A OD1   1 
ATOM   1800  N  ND2   . ASN A 1  237  ? 170.100 107.657 148.826 1.00 37.62  ? 237  ASN A ND2   1 
ATOM   1801  N  N     . LEU A 1  238  ? 172.862 110.597 151.065 1.00 40.84  ? 238  LEU A N     1 
ATOM   1802  C  CA    . LEU A 1  238  ? 174.222 110.132 151.302 1.00 44.04  ? 238  LEU A CA    1 
ATOM   1803  C  C     . LEU A 1  238  ? 174.658 110.316 152.749 1.00 44.95  ? 238  LEU A C     1 
ATOM   1804  O  O     . LEU A 1  238  ? 175.625 109.681 153.178 1.00 44.54  ? 238  LEU A O     1 
ATOM   1805  C  CB    . LEU A 1  238  ? 175.189 110.854 150.367 1.00 41.14  ? 238  LEU A CB    1 
ATOM   1806  C  CG    . LEU A 1  238  ? 175.040 110.488 148.896 1.00 41.87  ? 238  LEU A CG    1 
ATOM   1807  C  CD1   . LEU A 1  238  ? 175.865 111.414 148.039 1.00 43.70  ? 238  LEU A CD1   1 
ATOM   1808  C  CD2   . LEU A 1  238  ? 175.437 109.043 148.666 1.00 42.57  ? 238  LEU A CD2   1 
ATOM   1809  N  N     . LEU A 1  239  ? 173.970 111.166 153.508 1.00 41.04  ? 239  LEU A N     1 
ATOM   1810  C  CA    . LEU A 1  239  ? 174.337 111.367 154.902 1.00 39.01  ? 239  LEU A CA    1 
ATOM   1811  C  C     . LEU A 1  239  ? 173.931 110.183 155.772 1.00 38.46  ? 239  LEU A C     1 
ATOM   1812  O  O     . LEU A 1  239  ? 174.516 109.975 156.838 1.00 41.80  ? 239  LEU A O     1 
ATOM   1813  C  CB    . LEU A 1  239  ? 173.718 112.662 155.423 1.00 38.94  ? 239  LEU A CB    1 
ATOM   1814  C  CG    . LEU A 1  239  ? 174.151 113.921 154.670 1.00 38.49  ? 239  LEU A CG    1 
ATOM   1815  C  CD1   . LEU A 1  239  ? 173.458 115.161 155.212 1.00 36.39  ? 239  LEU A CD1   1 
ATOM   1816  C  CD2   . LEU A 1  239  ? 175.655 114.075 154.718 1.00 38.33  ? 239  LEU A CD2   1 
ATOM   1817  N  N     . ILE A 1  240  ? 172.935 109.416 155.355 1.00 38.27  ? 240  ILE A N     1 
ATOM   1818  C  CA    . ILE A 1  240  ? 172.522 108.239 156.129 1.00 40.42  ? 240  ILE A CA    1 
ATOM   1819  C  C     . ILE A 1  240  ? 173.570 107.143 155.988 1.00 41.25  ? 240  ILE A C     1 
ATOM   1820  O  O     . ILE A 1  240  ? 174.107 106.945 154.883 1.00 41.74  ? 240  ILE A O     1 
ATOM   1821  C  CB    . ILE A 1  240  ? 171.148 107.755 155.668 1.00 39.17  ? 240  ILE A CB    1 
ATOM   1822  C  CG1   . ILE A 1  240  ? 170.225 108.950 155.477 1.00 38.02  ? 240  ILE A CG1   1 
ATOM   1823  C  CG2   . ILE A 1  240  ? 170.555 106.786 156.671 1.00 38.55  ? 240  ILE A CG2   1 
ATOM   1824  C  CD1   . ILE A 1  240  ? 169.866 109.622 156.777 1.00 37.30  ? 240  ILE A CD1   1 
ATOM   1825  N  N     . PRO A 1  241  ? 173.907 106.429 157.063 1.00 41.22  ? 241  PRO A N     1 
ATOM   1826  C  CA    . PRO A 1  241  ? 174.863 105.320 156.947 1.00 40.87  ? 241  PRO A CA    1 
ATOM   1827  C  C     . PRO A 1  241  ? 174.368 104.248 155.987 1.00 40.93  ? 241  PRO A C     1 
ATOM   1828  O  O     . PRO A 1  241  ? 173.175 103.955 155.915 1.00 40.41  ? 241  PRO A O     1 
ATOM   1829  C  CB    . PRO A 1  241  ? 174.961 104.784 158.382 1.00 39.99  ? 241  PRO A CB    1 
ATOM   1830  C  CG    . PRO A 1  241  ? 173.962 105.589 159.195 1.00 41.34  ? 241  PRO A CG    1 
ATOM   1831  C  CD    . PRO A 1  241  ? 173.754 106.858 158.458 1.00 37.94  ? 241  PRO A CD    1 
ATOM   1832  N  N     . LYS A 1  242  ? 175.312 103.652 155.253 1.00 45.99  ? 242  LYS A N     1 
ATOM   1833  C  CA    . LYS A 1  242  ? 174.958 102.686 154.214 1.00 46.16  ? 242  LYS A CA    1 
ATOM   1834  C  C     . LYS A 1  242  ? 174.249 101.468 154.790 1.00 48.01  ? 242  LYS A C     1 
ATOM   1835  O  O     . LYS A 1  242  ? 173.429 100.841 154.111 1.00 49.40  ? 242  LYS A O     1 
ATOM   1836  C  CB    . LYS A 1  242  ? 176.205 102.250 153.447 1.00 44.76  ? 242  LYS A CB    1 
ATOM   1837  C  CG    . LYS A 1  242  ? 176.449 102.988 152.141 1.00 46.72  ? 242  LYS A CG    1 
ATOM   1838  C  CD    . LYS A 1  242  ? 177.030 104.374 152.363 1.00 48.91  ? 242  LYS A CD    1 
ATOM   1839  C  CE    . LYS A 1  242  ? 177.430 105.014 151.037 1.00 46.95  ? 242  LYS A CE    1 
ATOM   1840  N  NZ    . LYS A 1  242  ? 177.831 106.439 151.190 1.00 48.01  ? 242  LYS A NZ    1 
ATOM   1841  N  N     . ASP A 1  243  ? 174.571 101.096 156.028 1.00 45.73  ? 243  ASP A N     1 
ATOM   1842  C  CA    . ASP A 1  243  ? 173.933 99.940  156.647 1.00 46.78  ? 243  ASP A CA    1 
ATOM   1843  C  C     . ASP A 1  243  ? 173.304 100.270 157.993 1.00 47.50  ? 243  ASP A C     1 
ATOM   1844  O  O     . ASP A 1  243  ? 173.466 99.513  158.955 1.00 48.12  ? 243  ASP A O     1 
ATOM   1845  C  CB    . ASP A 1  243  ? 174.932 98.792  156.809 1.00 46.99  ? 243  ASP A CB    1 
ATOM   1846  C  CG    . ASP A 1  243  ? 174.788 97.738  155.730 1.00 49.43  ? 243  ASP A CG    1 
ATOM   1847  O  OD1   . ASP A 1  243  ? 173.638 97.429  155.351 1.00 48.38  ? 243  ASP A OD1   1 
ATOM   1848  O  OD2   . ASP A 1  243  ? 175.821 97.213  155.263 1.00 49.51  ? 243  ASP A OD2   1 
ATOM   1849  N  N     . LEU A 1  244  ? 172.587 101.383 158.082 1.00 40.48  ? 244  LEU A N     1 
ATOM   1850  C  CA    . LEU A 1  244  ? 171.794 101.635 159.275 1.00 38.94  ? 244  LEU A CA    1 
ATOM   1851  C  C     . LEU A 1  244  ? 170.659 100.626 159.353 1.00 41.79  ? 244  LEU A C     1 
ATOM   1852  O  O     . LEU A 1  244  ? 169.915 100.434 158.387 1.00 41.62  ? 244  LEU A O     1 
ATOM   1853  C  CB    . LEU A 1  244  ? 171.238 103.057 159.264 1.00 36.66  ? 244  LEU A CB    1 
ATOM   1854  C  CG    . LEU A 1  244  ? 170.168 103.312 160.323 1.00 38.89  ? 244  LEU A CG    1 
ATOM   1855  C  CD1   . LEU A 1  244  ? 170.743 103.142 161.725 1.00 40.00  ? 244  LEU A CD1   1 
ATOM   1856  C  CD2   . LEU A 1  244  ? 169.563 104.690 160.159 1.00 39.63  ? 244  LEU A CD2   1 
ATOM   1857  N  N     . GLN A 1  245  ? 170.533 99.971  160.503 1.00 43.14  ? 245  GLN A N     1 
ATOM   1858  C  CA    . GLN A 1  245  ? 169.468 99.012  160.749 1.00 43.11  ? 245  GLN A CA    1 
ATOM   1859  C  C     . GLN A 1  245  ? 168.708 99.434  161.997 1.00 42.69  ? 245  GLN A C     1 
ATOM   1860  O  O     . GLN A 1  245  ? 169.314 99.827  162.995 1.00 43.84  ? 245  GLN A O     1 
ATOM   1861  C  CB    . GLN A 1  245  ? 170.028 97.601  160.926 1.00 41.00  ? 245  GLN A CB    1 
ATOM   1862  C  CG    . GLN A 1  245  ? 170.851 97.105  159.751 1.00 40.70  ? 245  GLN A CG    1 
ATOM   1863  C  CD    . GLN A 1  245  ? 170.035 96.898  158.499 1.00 42.67  ? 245  GLN A CD    1 
ATOM   1864  O  OE1   . GLN A 1  245  ? 168.918 96.386  158.550 1.00 44.28  ? 245  GLN A OE1   1 
ATOM   1865  N  NE2   . GLN A 1  245  ? 170.592 97.292  157.361 1.00 42.86  ? 245  GLN A NE2   1 
ATOM   1866  N  N     . ILE A 1  246  ? 167.382 99.347  161.942 1.00 42.70  ? 246  ILE A N     1 
ATOM   1867  C  CA    . ILE A 1  246  ? 166.516 99.781  163.031 1.00 42.30  ? 246  ILE A CA    1 
ATOM   1868  C  C     . ILE A 1  246  ? 165.734 98.581  163.541 1.00 43.11  ? 246  ILE A C     1 
ATOM   1869  O  O     . ILE A 1  246  ? 165.285 97.744  162.750 1.00 45.76  ? 246  ILE A O     1 
ATOM   1870  C  CB    . ILE A 1  246  ? 165.558 100.902 162.592 1.00 43.52  ? 246  ILE A CB    1 
ATOM   1871  C  CG1   . ILE A 1  246  ? 166.337 102.105 162.064 1.00 42.17  ? 246  ILE A CG1   1 
ATOM   1872  C  CG2   . ILE A 1  246  ? 164.710 101.343 163.763 1.00 41.28  ? 246  ILE A CG2   1 
ATOM   1873  C  CD1   . ILE A 1  246  ? 167.160 102.804 163.113 1.00 41.35  ? 246  ILE A CD1   1 
ATOM   1874  N  N     . VAL A 1  247  ? 165.583 98.494  164.861 1.00 46.28  ? 247  VAL A N     1 
ATOM   1875  C  CA    . VAL A 1  247  ? 164.799 97.458  165.515 1.00 46.33  ? 247  VAL A CA    1 
ATOM   1876  C  C     . VAL A 1  247  ? 163.654 98.140  166.254 1.00 46.78  ? 247  VAL A C     1 
ATOM   1877  O  O     . VAL A 1  247  ? 163.657 99.355  166.463 1.00 47.44  ? 247  VAL A O     1 
ATOM   1878  C  CB    . VAL A 1  247  ? 165.659 96.611  166.480 1.00 46.17  ? 247  VAL A CB    1 
ATOM   1879  C  CG1   . VAL A 1  247  ? 164.949 95.323  166.870 1.00 46.14  ? 247  VAL A CG1   1 
ATOM   1880  C  CG2   . VAL A 1  247  ? 167.018 96.314  165.865 1.00 43.31  ? 247  VAL A CG2   1 
ATOM   1881  N  N     . ARG A 1  248  ? 162.651 97.347  166.623 1.00 47.31  ? 248  ARG A N     1 
ATOM   1882  C  CA    . ARG A 1  248  ? 161.537 97.863  167.407 1.00 48.30  ? 248  ARG A CA    1 
ATOM   1883  C  C     . ARG A 1  248  ? 162.034 98.364  168.761 1.00 51.41  ? 248  ARG A C     1 
ATOM   1884  O  O     . ARG A 1  248  ? 162.717 97.641  169.491 1.00 49.93  ? 248  ARG A O     1 
ATOM   1885  C  CB    . ARG A 1  248  ? 160.485 96.768  167.593 1.00 47.13  ? 248  ARG A CB    1 
ATOM   1886  C  CG    . ARG A 1  248  ? 159.246 97.182  168.374 1.00 48.25  ? 248  ARG A CG    1 
ATOM   1887  C  CD    . ARG A 1  248  ? 158.229 97.847  167.467 1.00 48.54  ? 248  ARG A CD    1 
ATOM   1888  N  NE    . ARG A 1  248  ? 157.043 98.299  168.183 1.00 47.10  ? 248  ARG A NE    1 
ATOM   1889  C  CZ    . ARG A 1  248  ? 156.026 97.515  168.510 1.00 50.19  ? 248  ARG A CZ    1 
ATOM   1890  N  NH1   . ARG A 1  248  ? 156.031 96.223  168.225 1.00 49.72  ? 248  ARG A NH1   1 
ATOM   1891  N  NH2   . ARG A 1  248  ? 154.978 98.038  169.140 1.00 49.14  ? 248  ARG A NH2   1 
ATOM   1892  N  N     . GLY A 1  249  ? 161.688 99.609  169.093 1.00 50.64  ? 249  GLY A N     1 
ATOM   1893  C  CA    . GLY A 1  249  ? 162.076 100.195 170.365 1.00 48.64  ? 249  GLY A CA    1 
ATOM   1894  C  C     . GLY A 1  249  ? 163.523 100.621 170.487 1.00 49.29  ? 249  GLY A C     1 
ATOM   1895  O  O     . GLY A 1  249  ? 164.041 100.682 171.606 1.00 48.63  ? 249  GLY A O     1 
ATOM   1896  N  N     . GLN A 1  250  ? 164.194 100.924 169.378 1.00 50.03  ? 250  GLN A N     1 
ATOM   1897  C  CA    . GLN A 1  250  ? 165.629 101.173 169.408 1.00 49.23  ? 250  GLN A CA    1 
ATOM   1898  C  C     . GLN A 1  250  ? 165.935 102.672 169.397 1.00 49.75  ? 250  GLN A C     1 
ATOM   1899  O  O     . GLN A 1  250  ? 165.423 103.428 168.570 1.00 53.24  ? 250  GLN A O     1 
ATOM   1900  C  CB    . GLN A 1  250  ? 166.284 100.490 168.212 1.00 48.63  ? 250  GLN A CB    1 
ATOM   1901  C  CG    . GLN A 1  250  ? 167.731 100.127 168.380 1.00 49.67  ? 250  GLN A CG    1 
ATOM   1902  C  CD    . GLN A 1  250  ? 168.290 99.506  167.126 1.00 51.18  ? 250  GLN A CD    1 
ATOM   1903  O  OE1   . GLN A 1  250  ? 167.677 99.584  166.067 1.00 50.57  ? 250  GLN A OE1   1 
ATOM   1904  N  NE2   . GLN A 1  250  ? 169.444 98.865  167.238 1.00 50.03  ? 250  GLN A NE2   1 
ATOM   1905  N  N     . LYS A 1  251  ? 166.800 103.096 170.316 1.00 47.90  ? 251  LYS A N     1 
ATOM   1906  C  CA    . LYS A 1  251  ? 167.138 104.509 170.449 1.00 49.89  ? 251  LYS A CA    1 
ATOM   1907  C  C     . LYS A 1  251  ? 168.142 104.932 169.385 1.00 50.00  ? 251  LYS A C     1 
ATOM   1908  O  O     . LYS A 1  251  ? 169.156 104.265 169.165 1.00 50.60  ? 251  LYS A O     1 
ATOM   1909  C  CB    . LYS A 1  251  ? 167.714 104.786 171.840 1.00 50.31  ? 251  LYS A CB    1 
ATOM   1910  C  CG    . LYS A 1  251  ? 167.698 106.252 172.277 1.00 50.45  ? 251  LYS A CG    1 
ATOM   1911  C  CD    . LYS A 1  251  ? 169.002 106.970 171.943 1.00 50.26  ? 251  LYS A CD    1 
ATOM   1912  C  CE    . LYS A 1  251  ? 170.215 106.254 172.531 1.00 51.18  ? 251  LYS A CE    1 
ATOM   1913  N  NZ    . LYS A 1  251  ? 170.299 106.367 174.011 1.00 51.00  ? 251  LYS A NZ    1 
ATOM   1914  N  N     . ILE A 1  252  ? 167.871 106.063 168.737 1.00 45.09  ? 252  ILE A N     1 
ATOM   1915  C  CA    . ILE A 1  252  ? 168.754 106.559 167.679 1.00 44.93  ? 252  ILE A CA    1 
ATOM   1916  C  C     . ILE A 1  252  ? 169.076 108.017 167.932 1.00 44.81  ? 252  ILE A C     1 
ATOM   1917  O  O     . ILE A 1  252  ? 168.268 108.778 168.488 1.00 43.12  ? 252  ILE A O     1 
ATOM   1918  C  CB    . ILE A 1  252  ? 168.121 106.396 166.277 1.00 44.67  ? 252  ILE A CB    1 
ATOM   1919  C  CG1   . ILE A 1  252  ? 166.879 107.280 166.132 1.00 44.04  ? 252  ILE A CG1   1 
ATOM   1920  C  CG2   . ILE A 1  252  ? 167.765 104.939 166.019 1.00 42.31  ? 252  ILE A CG2   1 
ATOM   1921  C  CD1   . ILE A 1  252  ? 166.382 107.397 164.716 1.00 44.13  ? 252  ILE A CD1   1 
ATOM   1922  N  N     . PRO A 1  253  ? 170.277 108.442 167.543 1.00 45.97  ? 253  PRO A N     1 
ATOM   1923  C  CA    . PRO A 1  253  ? 170.696 109.822 167.817 1.00 44.70  ? 253  PRO A CA    1 
ATOM   1924  C  C     . PRO A 1  253  ? 169.831 110.829 167.076 1.00 42.04  ? 253  PRO A C     1 
ATOM   1925  O  O     . PRO A 1  253  ? 169.372 110.586 165.959 1.00 40.69  ? 253  PRO A O     1 
ATOM   1926  C  CB    . PRO A 1  253  ? 172.149 109.861 167.326 1.00 43.04  ? 253  PRO A CB    1 
ATOM   1927  C  CG    . PRO A 1  253  ? 172.584 108.430 167.287 1.00 41.34  ? 253  PRO A CG    1 
ATOM   1928  C  CD    . PRO A 1  253  ? 171.359 107.643 166.943 1.00 40.48  ? 253  PRO A CD    1 
ATOM   1929  N  N     . LEU A 1  254  ? 169.631 111.987 167.708 1.00 44.45  ? 254  LEU A N     1 
ATOM   1930  C  CA    . LEU A 1  254  ? 168.660 112.950 167.205 1.00 44.77  ? 254  LEU A CA    1 
ATOM   1931  C  C     . LEU A 1  254  ? 169.048 113.552 165.862 1.00 46.29  ? 254  LEU A C     1 
ATOM   1932  O  O     . LEU A 1  254  ? 168.180 114.111 165.186 1.00 47.06  ? 254  LEU A O     1 
ATOM   1933  C  CB    . LEU A 1  254  ? 168.429 114.062 168.226 1.00 44.51  ? 254  LEU A CB    1 
ATOM   1934  C  CG    . LEU A 1  254  ? 167.289 113.745 169.195 1.00 46.83  ? 254  LEU A CG    1 
ATOM   1935  C  CD1   . LEU A 1  254  ? 167.808 112.998 170.416 1.00 44.54  ? 254  LEU A CD1   1 
ATOM   1936  C  CD2   . LEU A 1  254  ? 166.527 114.996 169.588 1.00 45.74  ? 254  LEU A CD2   1 
ATOM   1937  N  N     . ASN A 1  255  ? 170.318 113.480 165.461 1.00 46.36  ? 255  ASN A N     1 
ATOM   1938  C  CA    . ASN A 1  255  ? 170.653 113.904 164.106 1.00 47.04  ? 255  ASN A CA    1 
ATOM   1939  C  C     . ASN A 1  255  ? 170.082 112.938 163.075 1.00 47.84  ? 255  ASN A C     1 
ATOM   1940  O  O     . ASN A 1  255  ? 169.560 113.364 162.038 1.00 46.09  ? 255  ASN A O     1 
ATOM   1941  C  CB    . ASN A 1  255  ? 172.167 114.040 163.929 1.00 44.68  ? 255  ASN A CB    1 
ATOM   1942  C  CG    . ASN A 1  255  ? 172.906 112.731 164.125 1.00 48.17  ? 255  ASN A CG    1 
ATOM   1943  O  OD1   . ASN A 1  255  ? 172.312 111.706 164.461 1.00 49.92  ? 255  ASN A OD1   1 
ATOM   1944  N  ND2   . ASN A 1  255  ? 174.209 112.751 163.878 1.00 47.31  ? 255  ASN A ND2   1 
ATOM   1945  N  N     . ILE A 1  256  ? 170.174 111.634 163.342 1.00 45.49  ? 256  ILE A N     1 
ATOM   1946  C  CA    . ILE A 1  256  ? 169.624 110.639 162.425 1.00 44.81  ? 256  ILE A CA    1 
ATOM   1947  C  C     . ILE A 1  256  ? 168.108 110.762 162.348 1.00 44.67  ? 256  ILE A C     1 
ATOM   1948  O  O     . ILE A 1  256  ? 167.523 110.724 161.259 1.00 46.77  ? 256  ILE A O     1 
ATOM   1949  C  CB    . ILE A 1  256  ? 170.063 109.225 162.847 1.00 44.38  ? 256  ILE A CB    1 
ATOM   1950  C  CG1   . ILE A 1  256  ? 171.488 108.952 162.377 1.00 43.27  ? 256  ILE A CG1   1 
ATOM   1951  C  CG2   . ILE A 1  256  ? 169.119 108.181 162.298 1.00 42.39  ? 256  ILE A CG2   1 
ATOM   1952  C  CD1   . ILE A 1  256  ? 172.018 107.609 162.805 1.00 43.38  ? 256  ILE A CD1   1 
ATOM   1953  N  N     . ASP A 1  257  ? 167.448 110.927 163.495 1.00 42.68  ? 257  ASP A N     1 
ATOM   1954  C  CA    . ASP A 1  257  ? 166.003 111.123 163.484 1.00 45.81  ? 257  ASP A CA    1 
ATOM   1955  C  C     . ASP A 1  257  ? 165.624 112.370 162.696 1.00 47.50  ? 257  ASP A C     1 
ATOM   1956  O  O     . ASP A 1  257  ? 164.606 112.382 161.997 1.00 49.00  ? 257  ASP A O     1 
ATOM   1957  C  CB    . ASP A 1  257  ? 165.467 111.208 164.912 1.00 45.48  ? 257  ASP A CB    1 
ATOM   1958  C  CG    . ASP A 1  257  ? 163.998 110.838 165.003 1.00 46.47  ? 257  ASP A CG    1 
ATOM   1959  O  OD1   . ASP A 1  257  ? 163.435 110.385 163.987 1.00 49.05  ? 257  ASP A OD1   1 
ATOM   1960  O  OD2   . ASP A 1  257  ? 163.400 111.015 166.083 1.00 45.43  ? 257  ASP A OD2   1 
ATOM   1961  N  N     . ARG A 1  258  ? 166.418 113.438 162.806 1.00 45.66  ? 258  ARG A N     1 
ATOM   1962  C  CA    . ARG A 1  258  ? 166.180 114.605 161.964 1.00 47.30  ? 258  ARG A CA    1 
ATOM   1963  C  C     . ARG A 1  258  ? 166.503 114.316 160.503 1.00 47.07  ? 258  ARG A C     1 
ATOM   1964  O  O     . ARG A 1  258  ? 165.803 114.796 159.605 1.00 48.28  ? 258  ARG A O     1 
ATOM   1965  C  CB    . ARG A 1  258  ? 166.984 115.810 162.454 1.00 45.66  ? 258  ARG A CB    1 
ATOM   1966  C  CG    . ARG A 1  258  ? 166.425 116.480 163.689 1.00 46.71  ? 258  ARG A CG    1 
ATOM   1967  C  CD    . ARG A 1  258  ? 166.896 117.927 163.771 1.00 47.42  ? 258  ARG A CD    1 
ATOM   1968  N  NE    . ARG A 1  258  ? 168.341 118.060 163.623 1.00 48.20  ? 258  ARG A NE    1 
ATOM   1969  C  CZ    . ARG A 1  258  ? 169.205 118.014 164.627 1.00 48.57  ? 258  ARG A CZ    1 
ATOM   1970  N  NH1   . ARG A 1  258  ? 168.803 117.855 165.878 1.00 47.11  ? 258  ARG A NH1   1 
ATOM   1971  N  NH2   . ARG A 1  258  ? 170.504 118.131 164.371 1.00 48.34  ? 258  ARG A NH2   1 
ATOM   1972  N  N     . ASN A 1  259  ? 167.565 113.552 160.242 1.00 43.72  ? 259  ASN A N     1 
ATOM   1973  C  CA    . ASN A 1  259  ? 167.909 113.230 158.860 1.00 43.99  ? 259  ASN A CA    1 
ATOM   1974  C  C     . ASN A 1  259  ? 166.849 112.356 158.207 1.00 43.07  ? 259  ASN A C     1 
ATOM   1975  O  O     . ASN A 1  259  ? 166.408 112.645 157.090 1.00 42.74  ? 259  ASN A O     1 
ATOM   1976  C  CB    . ASN A 1  259  ? 169.273 112.546 158.792 1.00 43.58  ? 259  ASN A CB    1 
ATOM   1977  C  CG    . ASN A 1  259  ? 170.416 113.533 158.700 1.00 46.24  ? 259  ASN A CG    1 
ATOM   1978  O  OD1   . ASN A 1  259  ? 170.294 114.583 158.071 1.00 46.71  ? 259  ASN A OD1   1 
ATOM   1979  N  ND2   . ASN A 1  259  ? 171.539 113.198 159.317 1.00 46.27  ? 259  ASN A ND2   1 
ATOM   1980  N  N     . LEU A 1  260  ? 166.417 111.294 158.889 1.00 41.52  ? 260  LEU A N     1 
ATOM   1981  C  CA    . LEU A 1  260  ? 165.450 110.381 158.290 1.00 41.89  ? 260  LEU A CA    1 
ATOM   1982  C  C     . LEU A 1  260  ? 164.137 111.086 157.991 1.00 43.23  ? 260  LEU A C     1 
ATOM   1983  O  O     . LEU A 1  260  ? 163.535 110.871 156.933 1.00 45.27  ? 260  LEU A O     1 
ATOM   1984  C  CB    . LEU A 1  260  ? 165.211 109.184 159.203 1.00 41.00  ? 260  LEU A CB    1 
ATOM   1985  C  CG    . LEU A 1  260  ? 166.398 108.255 159.427 1.00 42.45  ? 260  LEU A CG    1 
ATOM   1986  C  CD1   . LEU A 1  260  ? 166.059 107.257 160.516 1.00 44.81  ? 260  LEU A CD1   1 
ATOM   1987  C  CD2   . LEU A 1  260  ? 166.779 107.552 158.141 1.00 39.42  ? 260  LEU A CD2   1 
ATOM   1988  N  N     . GLN A 1  261  ? 163.674 111.931 158.907 1.00 39.72  ? 261  GLN A N     1 
ATOM   1989  C  CA    . GLN A 1  261  ? 162.470 112.703 158.647 1.00 41.65  ? 261  GLN A CA    1 
ATOM   1990  C  C     . GLN A 1  261  ? 162.632 113.636 157.458 1.00 43.89  ? 261  GLN A C     1 
ATOM   1991  O  O     . GLN A 1  261  ? 161.693 113.783 156.671 1.00 42.62  ? 261  GLN A O     1 
ATOM   1992  C  CB    . GLN A 1  261  ? 162.083 113.509 159.888 1.00 39.86  ? 261  GLN A CB    1 
ATOM   1993  C  CG    . GLN A 1  261  ? 160.707 114.135 159.828 1.00 39.73  ? 261  GLN A CG    1 
ATOM   1994  C  CD    . GLN A 1  261  ? 160.751 115.541 159.268 1.00 43.58  ? 261  GLN A CD    1 
ATOM   1995  O  OE1   . GLN A 1  261  ? 161.766 116.224 159.371 1.00 44.60  ? 261  GLN A OE1   1 
ATOM   1996  N  NE2   . GLN A 1  261  ? 159.649 115.985 158.681 1.00 43.78  ? 261  GLN A NE2   1 
ATOM   1997  N  N     . THR A 1  262  ? 163.799 114.262 157.306 1.00 41.84  ? 262  THR A N     1 
ATOM   1998  C  CA    . THR A 1  262  ? 164.010 115.184 156.198 1.00 38.87  ? 262  THR A CA    1 
ATOM   1999  C  C     . THR A 1  262  ? 163.863 114.483 154.854 1.00 37.77  ? 262  THR A C     1 
ATOM   2000  O  O     . THR A 1  262  ? 163.251 115.031 153.933 1.00 39.81  ? 262  THR A O     1 
ATOM   2001  C  CB    . THR A 1  262  ? 165.387 115.839 156.311 1.00 39.74  ? 262  THR A CB    1 
ATOM   2002  O  OG1   . THR A 1  262  ? 165.545 116.396 157.619 1.00 41.75  ? 262  THR A OG1   1 
ATOM   2003  C  CG2   . THR A 1  262  ? 165.544 116.950 155.282 1.00 39.78  ? 262  THR A CG2   1 
ATOM   2004  N  N     . ILE A 1  263  ? 164.411 113.274 154.723 1.00 36.39  ? 263  ILE A N     1 
ATOM   2005  C  CA    . ILE A 1  263  ? 164.310 112.555 153.458 1.00 38.09  ? 263  ILE A CA    1 
ATOM   2006  C  C     . ILE A 1  263  ? 162.871 112.148 153.178 1.00 42.06  ? 263  ILE A C     1 
ATOM   2007  O  O     . ILE A 1  263  ? 162.378 112.299 152.055 1.00 44.30  ? 263  ILE A O     1 
ATOM   2008  C  CB    . ILE A 1  263  ? 165.245 111.339 153.455 1.00 36.79  ? 263  ILE A CB    1 
ATOM   2009  C  CG1   . ILE A 1  263  ? 166.639 111.752 153.887 1.00 40.65  ? 263  ILE A CG1   1 
ATOM   2010  C  CG2   . ILE A 1  263  ? 165.313 110.721 152.088 1.00 36.69  ? 263  ILE A CG2   1 
ATOM   2011  C  CD1   . ILE A 1  263  ? 167.299 110.713 154.697 1.00 42.29  ? 263  ILE A CD1   1 
ATOM   2012  N  N     . GLN A 1  264  ? 162.173 111.627 154.184 1.00 35.97  ? 264  GLN A N     1 
ATOM   2013  C  CA    . GLN A 1  264  ? 160.788 111.227 153.974 1.00 34.68  ? 264  GLN A CA    1 
ATOM   2014  C  C     . GLN A 1  264  ? 159.905 112.437 153.703 1.00 37.66  ? 264  GLN A C     1 
ATOM   2015  O  O     . GLN A 1  264  ? 158.985 112.371 152.883 1.00 42.18  ? 264  GLN A O     1 
ATOM   2016  C  CB    . GLN A 1  264  ? 160.282 110.434 155.176 1.00 35.81  ? 264  GLN A CB    1 
ATOM   2017  C  CG    . GLN A 1  264  ? 158.802 110.146 155.152 1.00 37.05  ? 264  GLN A CG    1 
ATOM   2018  C  CD    . GLN A 1  264  ? 158.439 109.026 154.199 1.00 38.26  ? 264  GLN A CD    1 
ATOM   2019  O  OE1   . GLN A 1  264  ? 157.984 109.269 153.082 1.00 37.47  ? 264  GLN A OE1   1 
ATOM   2020  N  NE2   . GLN A 1  264  ? 158.644 107.792 154.631 1.00 36.84  ? 264  GLN A NE2   1 
ATOM   2021  N  N     . GLN A 1  265  ? 160.168 113.555 154.378 1.00 39.33  ? 265  GLN A N     1 
ATOM   2022  C  CA    . GLN A 1  265  ? 159.419 114.773 154.089 1.00 38.63  ? 265  GLN A CA    1 
ATOM   2023  C  C     . GLN A 1  265  ? 159.741 115.303 152.697 1.00 39.77  ? 265  GLN A C     1 
ATOM   2024  O  O     . GLN A 1  265  ? 158.887 115.917 152.050 1.00 41.18  ? 265  GLN A O     1 
ATOM   2025  C  CB    . GLN A 1  265  ? 159.702 115.831 155.153 1.00 38.66  ? 265  GLN A CB    1 
ATOM   2026  C  CG    . GLN A 1  265  ? 158.994 117.158 154.930 1.00 36.89  ? 265  GLN A CG    1 
ATOM   2027  C  CD    . GLN A 1  265  ? 157.537 117.127 155.331 1.00 41.58  ? 265  GLN A CD    1 
ATOM   2028  O  OE1   . GLN A 1  265  ? 156.803 118.086 155.105 1.00 46.07  ? 265  GLN A OE1   1 
ATOM   2029  N  NE2   . GLN A 1  265  ? 157.115 116.038 155.951 1.00 39.14  ? 265  GLN A NE2   1 
ATOM   2030  N  N     . LEU A 1  266  ? 160.974 115.101 152.225 1.00 35.42  ? 266  LEU A N     1 
ATOM   2031  C  CA    . LEU A 1  266  ? 161.314 115.515 150.867 1.00 34.96  ? 266  LEU A CA    1 
ATOM   2032  C  C     . LEU A 1  266  ? 160.615 114.644 149.829 1.00 37.91  ? 266  LEU A C     1 
ATOM   2033  O  O     . LEU A 1  266  ? 160.073 115.157 148.845 1.00 36.11  ? 266  LEU A O     1 
ATOM   2034  C  CB    . LEU A 1  266  ? 162.829 115.481 150.664 1.00 35.00  ? 266  LEU A CB    1 
ATOM   2035  C  CG    . LEU A 1  266  ? 163.607 116.687 151.195 1.00 36.18  ? 266  LEU A CG    1 
ATOM   2036  C  CD1   . LEU A 1  266  ? 165.101 116.481 151.024 1.00 35.43  ? 266  LEU A CD1   1 
ATOM   2037  C  CD2   . LEU A 1  266  ? 163.154 117.965 150.512 1.00 34.03  ? 266  LEU A CD2   1 
ATOM   2038  N  N     . TYR A 1  267  ? 160.612 113.326 150.032 1.00 35.74  ? 267  TYR A N     1 
ATOM   2039  C  CA    . TYR A 1  267  ? 159.911 112.440 149.111 1.00 32.09  ? 267  TYR A CA    1 
ATOM   2040  C  C     . TYR A 1  267  ? 158.412 112.694 149.124 1.00 33.04  ? 267  TYR A C     1 
ATOM   2041  O  O     . TYR A 1  267  ? 157.753 112.575 148.087 1.00 34.03  ? 267  TYR A O     1 
ATOM   2042  C  CB    . TYR A 1  267  ? 160.200 110.981 149.447 1.00 32.09  ? 267  TYR A CB    1 
ATOM   2043  C  CG    . TYR A 1  267  ? 159.912 110.037 148.304 1.00 33.34  ? 267  TYR A CG    1 
ATOM   2044  C  CD1   . TYR A 1  267  ? 160.304 110.343 147.016 1.00 30.03  ? 267  TYR A CD1   1 
ATOM   2045  C  CD2   . TYR A 1  267  ? 159.236 108.849 148.515 1.00 31.98  ? 267  TYR A CD2   1 
ATOM   2046  C  CE1   . TYR A 1  267  ? 160.038 109.494 145.972 1.00 32.74  ? 267  TYR A CE1   1 
ATOM   2047  C  CE2   . TYR A 1  267  ? 158.965 107.990 147.479 1.00 31.64  ? 267  TYR A CE2   1 
ATOM   2048  C  CZ    . TYR A 1  267  ? 159.370 108.315 146.207 1.00 35.76  ? 267  TYR A CZ    1 
ATOM   2049  O  OH    . TYR A 1  267  ? 159.110 107.462 145.163 1.00 32.17  ? 267  TYR A OH    1 
ATOM   2050  N  N     . TYR A 1  268  ? 157.847 113.014 150.288 1.00 30.91  ? 268  TYR A N     1 
ATOM   2051  C  CA    . TYR A 1  268  ? 156.424 113.322 150.338 1.00 31.58  ? 268  TYR A CA    1 
ATOM   2052  C  C     . TYR A 1  268  ? 156.104 114.592 149.566 1.00 32.03  ? 268  TYR A C     1 
ATOM   2053  O  O     . TYR A 1  268  ? 155.085 114.661 148.873 1.00 34.35  ? 268  TYR A O     1 
ATOM   2054  C  CB    . TYR A 1  268  ? 155.949 113.446 151.782 1.00 31.39  ? 268  TYR A CB    1 
ATOM   2055  C  CG    . TYR A 1  268  ? 154.450 113.578 151.900 1.00 33.50  ? 268  TYR A CG    1 
ATOM   2056  C  CD1   . TYR A 1  268  ? 153.836 114.821 151.841 1.00 34.01  ? 268  TYR A CD1   1 
ATOM   2057  C  CD2   . TYR A 1  268  ? 153.648 112.462 152.066 1.00 31.50  ? 268  TYR A CD2   1 
ATOM   2058  C  CE1   . TYR A 1  268  ? 152.475 114.945 151.938 1.00 33.03  ? 268  TYR A CE1   1 
ATOM   2059  C  CE2   . TYR A 1  268  ? 152.287 112.579 152.167 1.00 31.47  ? 268  TYR A CE2   1 
ATOM   2060  C  CZ    . TYR A 1  268  ? 151.705 113.823 152.103 1.00 33.71  ? 268  TYR A CZ    1 
ATOM   2061  O  OH    . TYR A 1  268  ? 150.342 113.946 152.201 1.00 34.65  ? 268  TYR A OH    1 
ATOM   2062  N  N     . ASN A 1  269  ? 156.947 115.619 149.686 1.00 33.24  ? 269  ASN A N     1 
ATOM   2063  C  CA    . ASN A 1  269  ? 156.686 116.873 148.989 1.00 35.02  ? 269  ASN A CA    1 
ATOM   2064  C  C     . ASN A 1  269  ? 157.095 116.818 147.526 1.00 34.73  ? 269  ASN A C     1 
ATOM   2065  O  O     . ASN A 1  269  ? 156.664 117.668 146.743 1.00 34.99  ? 269  ASN A O     1 
ATOM   2066  C  CB    . ASN A 1  269  ? 157.405 118.025 149.687 1.00 36.86  ? 269  ASN A CB    1 
ATOM   2067  C  CG    . ASN A 1  269  ? 156.792 118.366 151.027 1.00 37.33  ? 269  ASN A CG    1 
ATOM   2068  O  OD1   . ASN A 1  269  ? 157.494 118.482 152.026 1.00 36.20  ? 269  ASN A OD1   1 
ATOM   2069  N  ND2   . ASN A 1  269  ? 155.479 118.542 151.053 1.00 35.06  ? 269  ASN A ND2   1 
ATOM   2070  N  N     . PHE A 1  270  ? 157.919 115.843 147.144 1.00 32.64  ? 270  PHE A N     1 
ATOM   2071  C  CA    . PHE A 1  270  ? 158.227 115.631 145.737 1.00 30.78  ? 270  PHE A CA    1 
ATOM   2072  C  C     . PHE A 1  270  ? 156.997 115.193 144.959 1.00 34.04  ? 270  PHE A C     1 
ATOM   2073  O  O     . PHE A 1  270  ? 156.933 115.390 143.743 1.00 38.71  ? 270  PHE A O     1 
ATOM   2074  C  CB    . PHE A 1  270  ? 159.335 114.589 145.609 1.00 30.43  ? 270  PHE A CB    1 
ATOM   2075  C  CG    . PHE A 1  270  ? 159.679 114.230 144.199 1.00 31.18  ? 270  PHE A CG    1 
ATOM   2076  C  CD1   . PHE A 1  270  ? 160.072 115.196 143.298 1.00 31.74  ? 270  PHE A CD1   1 
ATOM   2077  C  CD2   . PHE A 1  270  ? 159.624 112.918 143.778 1.00 32.15  ? 270  PHE A CD2   1 
ATOM   2078  C  CE1   . PHE A 1  270  ? 160.393 114.855 142.005 1.00 32.21  ? 270  PHE A CE1   1 
ATOM   2079  C  CE2   . PHE A 1  270  ? 159.946 112.579 142.490 1.00 30.43  ? 270  PHE A CE2   1 
ATOM   2080  C  CZ    . PHE A 1  270  ? 160.329 113.548 141.602 1.00 30.53  ? 270  PHE A CZ    1 
ATOM   2081  N  N     . LEU A 1  271  ? 156.011 114.613 145.636 1.00 32.13  ? 271  LEU A N     1 
ATOM   2082  C  CA    . LEU A 1  271  ? 154.824 114.073 144.996 1.00 28.98  ? 271  LEU A CA    1 
ATOM   2083  C  C     . LEU A 1  271  ? 153.551 114.819 145.363 1.00 31.65  ? 271  LEU A C     1 
ATOM   2084  O  O     . LEU A 1  271  ? 152.762 115.137 144.476 1.00 37.58  ? 271  LEU A O     1 
ATOM   2085  C  CB    . LEU A 1  271  ? 154.678 112.585 145.339 1.00 30.21  ? 271  LEU A CB    1 
ATOM   2086  C  CG    . LEU A 1  271  ? 155.820 111.648 144.943 1.00 28.34  ? 271  LEU A CG    1 
ATOM   2087  C  CD1   . LEU A 1  271  ? 155.430 110.211 145.186 1.00 26.55  ? 271  LEU A CD1   1 
ATOM   2088  C  CD2   . LEU A 1  271  ? 156.199 111.846 143.507 1.00 28.54  ? 271  LEU A CD2   1 
ATOM   2089  N  N     . LEU A 1  272  ? 153.319 115.126 146.641 1.00 29.18  ? 272  LEU A N     1 
ATOM   2090  C  CA    . LEU A 1  272  ? 152.047 115.710 147.062 1.00 29.51  ? 272  LEU A CA    1 
ATOM   2091  C  C     . LEU A 1  272  ? 152.187 117.046 147.782 1.00 30.72  ? 272  LEU A C     1 
ATOM   2092  O  O     . LEU A 1  272  ? 151.505 117.268 148.782 1.00 33.66  ? 272  LEU A O     1 
ATOM   2093  C  CB    . LEU A 1  272  ? 151.278 114.745 147.960 1.00 28.26  ? 272  LEU A CB    1 
ATOM   2094  C  CG    . LEU A 1  272  ? 151.002 113.345 147.440 1.00 28.72  ? 272  LEU A CG    1 
ATOM   2095  C  CD1   . LEU A 1  272  ? 151.451 112.340 148.459 1.00 29.55  ? 272  LEU A CD1   1 
ATOM   2096  C  CD2   . LEU A 1  272  ? 149.530 113.187 147.134 1.00 28.81  ? 272  LEU A CD2   1 
ATOM   2097  N  N     . ASP A 1  273  ? 153.015 117.958 147.289 1.00 32.76  ? 273  ASP A N     1 
ATOM   2098  C  CA    . ASP A 1  273  ? 153.154 119.253 147.946 1.00 33.25  ? 273  ASP A CA    1 
ATOM   2099  C  C     . ASP A 1  273  ? 152.004 120.171 147.553 1.00 33.70  ? 273  ASP A C     1 
ATOM   2100  O  O     . ASP A 1  273  ? 151.993 120.730 146.452 1.00 31.77  ? 273  ASP A O     1 
ATOM   2101  C  CB    . ASP A 1  273  ? 154.489 119.887 147.579 1.00 34.55  ? 273  ASP A CB    1 
ATOM   2102  C  CG    . ASP A 1  273  ? 154.823 121.065 148.437 1.00 36.73  ? 273  ASP A CG    1 
ATOM   2103  O  OD1   . ASP A 1  273  ? 154.166 121.243 149.482 1.00 33.23  ? 273  ASP A OD1   1 
ATOM   2104  O  OD2   . ASP A 1  273  ? 155.730 121.826 148.050 1.00 36.93  ? 273  ASP A OD2   1 
ATOM   2105  N  N     . SER A 1  274  ? 151.046 120.335 148.463 1.00 38.51  ? 274  SER A N     1 
ATOM   2106  C  CA    . SER A 1  274  ? 149.900 121.225 148.284 1.00 37.69  ? 274  SER A CA    1 
ATOM   2107  C  C     . SER A 1  274  ? 149.102 120.863 147.031 1.00 38.57  ? 274  SER A C     1 
ATOM   2108  O  O     . SER A 1  274  ? 148.957 121.659 146.103 1.00 39.29  ? 274  SER A O     1 
ATOM   2109  C  CB    . SER A 1  274  ? 150.341 122.690 148.243 1.00 36.32  ? 274  SER A CB    1 
ATOM   2110  O  OG    . SER A 1  274  ? 149.221 123.545 148.075 1.00 38.22  ? 274  SER A OG    1 
ATOM   2111  N  N     . VAL A 1  275  ? 148.570 119.645 147.028 1.00 41.91  ? 275  VAL A N     1 
ATOM   2112  C  CA    . VAL A 1  275  ? 147.772 119.175 145.903 1.00 43.02  ? 275  VAL A CA    1 
ATOM   2113  C  C     . VAL A 1  275  ? 146.377 119.795 145.926 1.00 43.67  ? 275  VAL A C     1 
ATOM   2114  O  O     . VAL A 1  275  ? 146.180 120.903 146.423 1.00 42.06  ? 275  VAL A O     1 
ATOM   2115  C  CB    . VAL A 1  275  ? 147.676 117.638 145.885 1.00 42.67  ? 275  VAL A CB    1 
ATOM   2116  C  CG1   . VAL A 1  275  ? 146.672 117.192 144.837 1.00 40.93  ? 275  VAL A CG1   1 
ATOM   2117  C  CG2   . VAL A 1  275  ? 149.028 117.030 145.595 1.00 39.99  ? 275  VAL A CG2   1 
ATOM   2118  N  N     . PRO A 1  297  ? 156.533 122.904 144.137 1.00 42.63  ? 297  PRO A N     1 
ATOM   2119  C  CA    . PRO A 1  297  ? 156.523 122.011 142.977 1.00 41.55  ? 297  PRO A CA    1 
ATOM   2120  C  C     . PRO A 1  297  ? 156.264 120.557 143.355 1.00 42.94  ? 297  PRO A C     1 
ATOM   2121  O  O     . PRO A 1  297  ? 157.008 119.979 144.146 1.00 42.31  ? 297  PRO A O     1 
ATOM   2122  C  CB    . PRO A 1  297  ? 157.931 122.178 142.397 1.00 38.81  ? 297  PRO A CB    1 
ATOM   2123  C  CG    . PRO A 1  297  ? 158.390 123.483 142.891 1.00 37.70  ? 297  PRO A CG    1 
ATOM   2124  C  CD    . PRO A 1  297  ? 157.803 123.632 144.251 1.00 40.64  ? 297  PRO A CD    1 
ATOM   2125  N  N     . SER A 1  298  ? 155.217 119.977 142.780 1.00 38.71  ? 298  SER A N     1 
ATOM   2126  C  CA    . SER A 1  298  ? 154.876 118.578 142.977 1.00 32.09  ? 298  SER A CA    1 
ATOM   2127  C  C     . SER A 1  298  ? 154.718 117.886 141.639 1.00 33.91  ? 298  SER A C     1 
ATOM   2128  O  O     . SER A 1  298  ? 154.491 118.525 140.612 1.00 40.37  ? 298  SER A O     1 
ATOM   2129  C  CB    . SER A 1  298  ? 153.583 118.398 143.750 1.00 32.49  ? 298  SER A CB    1 
ATOM   2130  O  OG    . SER A 1  298  ? 153.826 118.400 145.126 1.00 37.56  ? 298  SER A OG    1 
ATOM   2131  N  N     . ILE A 1  299  ? 154.852 116.564 141.667 1.00 26.44  ? 299  ILE A N     1 
ATOM   2132  C  CA    . ILE A 1  299  ? 154.471 115.764 140.514 1.00 27.23  ? 299  ILE A CA    1 
ATOM   2133  C  C     . ILE A 1  299  ? 152.957 115.750 140.354 1.00 26.63  ? 299  ILE A C     1 
ATOM   2134  O  O     . ILE A 1  299  ? 152.438 115.839 139.238 1.00 28.20  ? 299  ILE A O     1 
ATOM   2135  C  CB    . ILE A 1  299  ? 155.047 114.347 140.646 1.00 27.21  ? 299  ILE A CB    1 
ATOM   2136  C  CG1   . ILE A 1  299  ? 156.571 114.406 140.622 1.00 27.64  ? 299  ILE A CG1   1 
ATOM   2137  C  CG2   . ILE A 1  299  ? 154.529 113.454 139.545 1.00 26.41  ? 299  ILE A CG2   1 
ATOM   2138  C  CD1   . ILE A 1  299  ? 157.125 114.954 139.338 1.00 27.32  ? 299  ILE A CD1   1 
ATOM   2139  N  N     . MET A 1  300  ? 152.224 115.656 141.460 1.00 25.76  ? 300  MET A N     1 
ATOM   2140  C  CA    . MET A 1  300  ? 150.782 115.470 141.404 1.00 25.82  ? 300  MET A CA    1 
ATOM   2141  C  C     . MET A 1  300  ? 149.991 116.768 141.386 1.00 29.80  ? 300  MET A C     1 
ATOM   2142  O  O     . MET A 1  300  ? 148.775 116.720 141.192 1.00 30.22  ? 300  MET A O     1 
ATOM   2143  C  CB    . MET A 1  300  ? 150.310 114.619 142.582 1.00 26.60  ? 300  MET A CB    1 
ATOM   2144  C  CG    . MET A 1  300  ? 150.792 113.190 142.545 1.00 30.33  ? 300  MET A CG    1 
ATOM   2145  S  SD    . MET A 1  300  ? 149.771 112.112 141.526 1.00 42.63  ? 300  MET A SD    1 
ATOM   2146  C  CE    . MET A 1  300  ? 150.721 112.066 140.014 1.00 28.18  ? 300  MET A CE    1 
ATOM   2147  N  N     . ARG A 1  301  ? 150.626 117.920 141.588 1.00 34.74  ? 301  ARG A N     1 
ATOM   2148  C  CA    . ARG A 1  301  ? 149.896 119.169 141.438 1.00 31.91  ? 301  ARG A CA    1 
ATOM   2149  C  C     . ARG A 1  301  ? 149.766 119.569 139.977 1.00 31.32  ? 301  ARG A C     1 
ATOM   2150  O  O     . ARG A 1  301  ? 149.005 120.488 139.661 1.00 30.94  ? 301  ARG A O     1 
ATOM   2151  C  CB    . ARG A 1  301  ? 150.572 120.299 142.225 1.00 34.04  ? 301  ARG A CB    1 
ATOM   2152  C  CG    . ARG A 1  301  ? 149.682 121.528 142.379 1.00 34.82  ? 301  ARG A CG    1 
ATOM   2153  C  CD    . ARG A 1  301  ? 150.420 122.850 142.381 1.00 35.27  ? 301  ARG A CD    1 
ATOM   2154  N  NE    . ARG A 1  301  ? 151.788 122.776 142.872 1.00 39.65  ? 301  ARG A NE    1 
ATOM   2155  C  CZ    . ARG A 1  301  ? 152.534 123.839 143.144 1.00 38.21  ? 301  ARG A CZ    1 
ATOM   2156  N  NH1   . ARG A 1  301  ? 152.082 125.068 142.956 1.00 33.24  ? 301  ARG A NH1   1 
ATOM   2157  N  NH2   . ARG A 1  301  ? 153.761 123.665 143.624 1.00 37.79  ? 301  ARG A NH2   1 
ATOM   2158  N  N     . ARG A 1  302  ? 150.479 118.888 139.081 1.00 22.56  ? 302  ARG A N     1 
ATOM   2159  C  CA    . ARG A 1  302  ? 150.384 119.170 137.658 1.00 18.29  ? 302  ARG A CA    1 
ATOM   2160  C  C     . ARG A 1  302  ? 149.071 118.703 137.048 1.00 23.89  ? 302  ARG A C     1 
ATOM   2161  O  O     . ARG A 1  302  ? 148.661 119.237 136.016 1.00 24.76  ? 302  ARG A O     1 
ATOM   2162  C  CB    . ARG A 1  302  ? 151.545 118.508 136.924 1.00 21.68  ? 302  ARG A CB    1 
ATOM   2163  C  CG    . ARG A 1  302  ? 152.914 118.884 137.429 1.00 21.60  ? 302  ARG A CG    1 
ATOM   2164  C  CD    . ARG A 1  302  ? 153.964 118.121 136.668 1.00 22.58  ? 302  ARG A CD    1 
ATOM   2165  N  NE    . ARG A 1  302  ? 155.301 118.658 136.867 1.00 24.45  ? 302  ARG A NE    1 
ATOM   2166  C  CZ    . ARG A 1  302  ? 156.371 118.250 136.201 1.00 21.88  ? 302  ARG A CZ    1 
ATOM   2167  N  NH1   . ARG A 1  302  ? 156.299 117.281 135.307 1.00 17.75  ? 302  ARG A NH1   1 
ATOM   2168  N  NH2   . ARG A 1  302  ? 157.541 118.832 136.435 1.00 25.64  ? 302  ARG A NH2   1 
ATOM   2169  N  N     . LEU A 1  303  ? 148.412 117.734 137.659 1.00 21.66  ? 303  LEU A N     1 
ATOM   2170  C  CA    . LEU A 1  303  ? 147.235 117.052 137.130 1.00 15.16  ? 303  LEU A CA    1 
ATOM   2171  C  C     . LEU A 1  303  ? 145.900 117.786 137.278 1.00 18.75  ? 303  LEU A C     1 
ATOM   2172  O  O     . LEU A 1  303  ? 145.139 117.849 136.307 1.00 18.58  ? 303  LEU A O     1 
ATOM   2173  C  CB    . LEU A 1  303  ? 147.128 115.678 137.788 1.00 17.36  ? 303  LEU A CB    1 
ATOM   2174  C  CG    . LEU A 1  303  ? 147.825 114.490 137.129 1.00 14.65  ? 303  LEU A CG    1 
ATOM   2175  C  CD1   . LEU A 1  303  ? 149.286 114.754 136.914 1.00 15.56  ? 303  LEU A CD1   1 
ATOM   2176  C  CD2   . LEU A 1  303  ? 147.647 113.262 137.988 1.00 16.73  ? 303  LEU A CD2   1 
ATOM   2177  N  N     . PRO A 1  304  ? 145.555 118.338 138.463 1.00 23.26  ? 304  PRO A N     1 
ATOM   2178  C  CA    . PRO A 1  304  ? 144.136 118.568 138.781 1.00 22.64  ? 304  PRO A CA    1 
ATOM   2179  C  C     . PRO A 1  304  ? 143.360 119.658 138.049 1.00 26.42  ? 304  PRO A C     1 
ATOM   2180  O  O     . PRO A 1  304  ? 142.292 119.366 137.507 1.00 32.72  ? 304  PRO A O     1 
ATOM   2181  C  CB    . PRO A 1  304  ? 144.179 118.886 140.280 1.00 22.44  ? 304  PRO A CB    1 
ATOM   2182  C  CG    . PRO A 1  304  ? 145.479 118.408 140.742 1.00 22.71  ? 304  PRO A CG    1 
ATOM   2183  C  CD    . PRO A 1  304  ? 146.393 118.648 139.626 1.00 22.10  ? 304  PRO A CD    1 
ATOM   2184  N  N     . ARG A 1  305  ? 143.826 120.899 138.038 1.00 30.55  ? 305  ARG A N     1 
ATOM   2185  C  CA    . ARG A 1  305  ? 142.921 122.022 137.804 1.00 32.03  ? 305  ARG A CA    1 
ATOM   2186  C  C     . ARG A 1  305  ? 142.546 122.160 136.326 1.00 35.02  ? 305  ARG A C     1 
ATOM   2187  O  O     . ARG A 1  305  ? 142.795 121.281 135.499 1.00 36.91  ? 305  ARG A O     1 
ATOM   2188  C  CB    . ARG A 1  305  ? 143.527 123.314 138.348 1.00 34.30  ? 305  ARG A CB    1 
ATOM   2189  C  CG    . ARG A 1  305  ? 144.077 123.211 139.765 1.00 36.32  ? 305  ARG A CG    1 
ATOM   2190  C  CD    . ARG A 1  305  ? 143.124 122.448 140.669 1.00 37.58  ? 305  ARG A CD    1 
ATOM   2191  N  NE    . ARG A 1  305  ? 143.765 121.981 141.892 1.00 38.92  ? 305  ARG A NE    1 
ATOM   2192  C  CZ    . ARG A 1  305  ? 143.124 121.389 142.890 1.00 41.76  ? 305  ARG A CZ    1 
ATOM   2193  N  NH1   . ARG A 1  305  ? 141.815 121.207 142.857 1.00 41.52  ? 305  ARG A NH1   1 
ATOM   2194  N  NH2   . ARG A 1  305  ? 143.813 120.970 143.947 1.00 37.53  ? 305  ARG A NH2   1 
ATOM   2195  N  N     . LYS A 1  306  ? 141.893 123.273 135.993 1.00 31.78  ? 306  LYS A N     1 
ATOM   2196  C  CA    . LYS A 1  306  ? 141.579 123.565 134.602 1.00 29.68  ? 306  LYS A CA    1 
ATOM   2197  C  C     . LYS A 1  306  ? 142.839 123.869 133.806 1.00 31.84  ? 306  LYS A C     1 
ATOM   2198  O  O     . LYS A 1  306  ? 142.869 123.673 132.588 1.00 38.89  ? 306  LYS A O     1 
ATOM   2199  C  CB    . LYS A 1  306  ? 140.581 124.721 134.533 1.00 31.53  ? 306  LYS A CB    1 
ATOM   2200  C  CG    . LYS A 1  306  ? 140.699 125.614 133.324 1.00 35.06  ? 306  LYS A CG    1 
ATOM   2201  C  CD    . LYS A 1  306  ? 139.579 126.636 133.289 1.00 37.83  ? 306  LYS A CD    1 
ATOM   2202  C  CE    . LYS A 1  306  ? 139.250 127.051 131.861 1.00 39.69  ? 306  LYS A CE    1 
ATOM   2203  N  NZ    . LYS A 1  306  ? 138.976 125.895 130.965 1.00 37.69  ? 306  LYS A NZ    1 
ATOM   2204  N  N     . GLU A 1  307  ? 143.884 124.343 134.473 1.00 31.26  ? 307  GLU A N     1 
ATOM   2205  C  CA    . GLU A 1  307  ? 145.188 124.552 133.864 1.00 29.63  ? 307  GLU A CA    1 
ATOM   2206  C  C     . GLU A 1  307  ? 146.125 123.372 134.060 1.00 30.49  ? 307  GLU A C     1 
ATOM   2207  O  O     . GLU A 1  307  ? 147.331 123.518 133.850 1.00 32.72  ? 307  GLU A O     1 
ATOM   2208  C  CB    . GLU A 1  307  ? 145.837 125.814 134.428 1.00 32.75  ? 307  GLU A CB    1 
ATOM   2209  C  CG    . GLU A 1  307  ? 145.228 127.097 133.921 1.00 35.62  ? 307  GLU A CG    1 
ATOM   2210  C  CD    . GLU A 1  307  ? 145.659 127.427 132.508 1.00 39.70  ? 307  GLU A CD    1 
ATOM   2211  O  OE1   . GLU A 1  307  ? 146.878 127.557 132.267 1.00 41.05  ? 307  GLU A OE1   1 
ATOM   2212  O  OE2   . GLU A 1  307  ? 144.778 127.558 131.635 1.00 38.87  ? 307  GLU A OE2   1 
ATOM   2213  N  N     . GLY A 1  308  ? 145.604 122.217 134.458 1.00 22.92  ? 308  GLY A N     1 
ATOM   2214  C  CA    . GLY A 1  308  ? 146.422 121.058 134.708 1.00 18.44  ? 308  GLY A CA    1 
ATOM   2215  C  C     . GLY A 1  308  ? 146.733 120.273 133.456 1.00 13.46  ? 308  GLY A C     1 
ATOM   2216  O  O     . GLY A 1  308  ? 146.398 120.654 132.340 1.00 16.80  ? 308  GLY A O     1 
ATOM   2217  N  N     . ARG A 1  309  ? 147.401 119.140 133.657 1.00 12.24  ? 309  ARG A N     1 
ATOM   2218  C  CA    . ARG A 1  309  ? 147.789 118.304 132.529 1.00 13.07  ? 309  ARG A CA    1 
ATOM   2219  C  C     . ARG A 1  309  ? 146.568 117.785 131.785 1.00 14.55  ? 309  ARG A C     1 
ATOM   2220  O  O     . ARG A 1  309  ? 146.535 117.790 130.552 1.00 20.26  ? 309  ARG A O     1 
ATOM   2221  C  CB    . ARG A 1  309  ? 148.646 117.136 133.016 1.00 13.01  ? 309  ARG A CB    1 
ATOM   2222  C  CG    . ARG A 1  309  ? 149.066 116.162 131.936 1.00 9.60   ? 309  ARG A CG    1 
ATOM   2223  C  CD    . ARG A 1  309  ? 150.170 116.752 131.097 1.00 11.79  ? 309  ARG A CD    1 
ATOM   2224  N  NE    . ARG A 1  309  ? 151.327 117.049 131.926 1.00 16.34  ? 309  ARG A NE    1 
ATOM   2225  C  CZ    . ARG A 1  309  ? 152.037 118.166 131.863 1.00 17.85  ? 309  ARG A CZ    1 
ATOM   2226  N  NH1   . ARG A 1  309  ? 151.737 119.129 131.011 1.00 12.91  ? 309  ARG A NH1   1 
ATOM   2227  N  NH2   . ARG A 1  309  ? 153.062 118.327 132.693 1.00 15.16  ? 309  ARG A NH2   1 
ATOM   2228  N  N     . ILE A 1  310  ? 145.549 117.345 132.517 1.00 8.87   ? 310  ILE A N     1 
ATOM   2229  C  CA    . ILE A 1  310  ? 144.432 116.646 131.895 1.00 7.93   ? 310  ILE A CA    1 
ATOM   2230  C  C     . ILE A 1  310  ? 143.568 117.606 131.091 1.00 6.18   ? 310  ILE A C     1 
ATOM   2231  O  O     . ILE A 1  310  ? 143.271 117.362 129.919 1.00 6.57   ? 310  ILE A O     1 
ATOM   2232  C  CB    . ILE A 1  310  ? 143.614 115.905 132.966 1.00 8.70   ? 310  ILE A CB    1 
ATOM   2233  C  CG1   . ILE A 1  310  ? 144.477 114.847 133.649 1.00 6.75   ? 310  ILE A CG1   1 
ATOM   2234  C  CG2   . ILE A 1  310  ? 142.378 115.283 132.357 1.00 8.68   ? 310  ILE A CG2   1 
ATOM   2235  C  CD1   . ILE A 1  310  ? 143.882 114.295 134.901 1.00 7.82   ? 310  ILE A CD1   1 
ATOM   2236  N  N     . ARG A 1  311  ? 143.151 118.709 131.699 1.00 7.02   ? 311  ARG A N     1 
ATOM   2237  C  CA    . ARG A 1  311  ? 142.168 119.569 131.053 1.00 3.29   ? 311  ARG A CA    1 
ATOM   2238  C  C     . ARG A 1  311  ? 142.802 120.553 130.085 1.00 9.77   ? 311  ARG A C     1 
ATOM   2239  O  O     . ARG A 1  311  ? 142.154 120.981 129.127 1.00 17.19  ? 311  ARG A O     1 
ATOM   2240  C  CB    . ARG A 1  311  ? 141.355 120.306 132.108 1.00 9.39   ? 311  ARG A CB    1 
ATOM   2241  C  CG    . ARG A 1  311  ? 140.338 119.433 132.788 1.00 13.66  ? 311  ARG A CG    1 
ATOM   2242  C  CD    . ARG A 1  311  ? 139.591 120.195 133.830 1.00 13.56  ? 311  ARG A CD    1 
ATOM   2243  N  NE    . ARG A 1  311  ? 138.880 121.329 133.262 1.00 8.30   ? 311  ARG A NE    1 
ATOM   2244  C  CZ    . ARG A 1  311  ? 138.091 122.130 133.959 1.00 10.99  ? 311  ARG A CZ    1 
ATOM   2245  N  NH1   . ARG A 1  311  ? 137.895 121.949 135.251 1.00 9.08   ? 311  ARG A NH1   1 
ATOM   2246  N  NH2   . ARG A 1  311  ? 137.479 123.131 133.342 1.00 13.36  ? 311  ARG A NH2   1 
ATOM   2247  N  N     . LYS A 1  312  ? 144.053 120.934 130.314 1.00 14.25  ? 312  LYS A N     1 
ATOM   2248  C  CA    . LYS A 1  312  ? 144.716 121.865 129.413 1.00 11.66  ? 312  LYS A CA    1 
ATOM   2249  C  C     . LYS A 1  312  ? 145.514 121.168 128.324 1.00 14.97  ? 312  LYS A C     1 
ATOM   2250  O  O     . LYS A 1  312  ? 145.384 121.513 127.149 1.00 19.20  ? 312  LYS A O     1 
ATOM   2251  C  CB    . LYS A 1  312  ? 145.634 122.793 130.198 1.00 11.97  ? 312  LYS A CB    1 
ATOM   2252  C  CG    . LYS A 1  312  ? 146.539 123.612 129.325 1.00 12.61  ? 312  LYS A CG    1 
ATOM   2253  C  CD    . LYS A 1  312  ? 146.116 125.046 129.263 1.00 16.96  ? 312  LYS A CD    1 
ATOM   2254  C  CE    . LYS A 1  312  ? 147.090 125.839 128.430 1.00 20.34  ? 312  LYS A CE    1 
ATOM   2255  N  NZ    . LYS A 1  312  ? 148.470 125.334 128.602 1.00 22.73  ? 312  LYS A NZ    1 
ATOM   2256  N  N     . SER A 1  313  ? 146.343 120.198 128.680 1.00 9.98   ? 313  SER A N     1 
ATOM   2257  C  CA    . SER A 1  313  ? 147.252 119.610 127.712 1.00 8.03   ? 313  SER A CA    1 
ATOM   2258  C  C     . SER A 1  313  ? 146.646 118.441 126.964 1.00 9.34   ? 313  SER A C     1 
ATOM   2259  O  O     . SER A 1  313  ? 147.018 118.199 125.814 1.00 12.72  ? 313  SER A O     1 
ATOM   2260  C  CB    . SER A 1  313  ? 148.534 119.156 128.410 1.00 14.53  ? 313  SER A CB    1 
ATOM   2261  O  OG    . SER A 1  313  ? 149.240 120.260 128.938 1.00 23.91  ? 313  SER A OG    1 
ATOM   2262  N  N     . LEU A 1  314  ? 145.728 117.712 127.584 1.00 5.32   ? 314  LEU A N     1 
ATOM   2263  C  CA    . LEU A 1  314  ? 145.196 116.485 127.015 1.00 5.79   ? 314  LEU A CA    1 
ATOM   2264  C  C     . LEU A 1  314  ? 143.814 116.656 126.410 1.00 8.19   ? 314  LEU A C     1 
ATOM   2265  O  O     . LEU A 1  314  ? 143.560 116.154 125.315 1.00 9.43   ? 314  LEU A O     1 
ATOM   2266  C  CB    . LEU A 1  314  ? 145.151 115.397 128.087 1.00 8.51   ? 314  LEU A CB    1 
ATOM   2267  C  CG    . LEU A 1  314  ? 146.458 114.674 128.389 1.00 6.17   ? 314  LEU A CG    1 
ATOM   2268  C  CD1   . LEU A 1  314  ? 146.330 113.883 129.661 1.00 4.24   ? 314  LEU A CD1   1 
ATOM   2269  C  CD2   . LEU A 1  314  ? 146.791 113.774 127.239 1.00 13.56  ? 314  LEU A CD2   1 
ATOM   2270  N  N     . LEU A 1  315  ? 142.910 117.344 127.099 1.00 6.37   ? 315  LEU A N     1 
ATOM   2271  C  CA    . LEU A 1  315  ? 141.565 117.535 126.583 1.00 0.37   ? 315  LEU A CA    1 
ATOM   2272  C  C     . LEU A 1  315  ? 141.470 118.710 125.623 1.00 8.28   ? 315  LEU A C     1 
ATOM   2273  O  O     . LEU A 1  315  ? 140.468 118.830 124.917 1.00 9.45   ? 315  LEU A O     1 
ATOM   2274  C  CB    . LEU A 1  315  ? 140.584 117.714 127.740 1.00 0.39   ? 315  LEU A CB    1 
ATOM   2275  C  CG    . LEU A 1  315  ? 140.403 116.517 128.679 1.00 1.09   ? 315  LEU A CG    1 
ATOM   2276  C  CD1   . LEU A 1  315  ? 139.513 116.875 129.844 1.00 2.72   ? 315  LEU A CD1   1 
ATOM   2277  C  CD2   . LEU A 1  315  ? 139.877 115.302 127.942 1.00 2.56   ? 315  LEU A CD2   1 
ATOM   2278  N  N     . GLY A 1  316  ? 142.491 119.558 125.569 1.00 10.86  ? 316  GLY A N     1 
ATOM   2279  C  CA    . GLY A 1  316  ? 142.568 120.637 124.608 1.00 1.54   ? 316  GLY A CA    1 
ATOM   2280  C  C     . GLY A 1  316  ? 143.858 120.594 123.824 1.00 4.22   ? 316  GLY A C     1 
ATOM   2281  O  O     . GLY A 1  316  ? 144.632 119.651 123.970 1.00 8.46   ? 316  GLY A O     1 
ATOM   2282  N  N     . SER A 1  317  ? 144.115 121.605 123.000 1.00 7.80   ? 317  SER A N     1 
ATOM   2283  C  CA    . SER A 1  317  ? 145.289 121.601 122.140 1.00 2.51   ? 317  SER A CA    1 
ATOM   2284  C  C     . SER A 1  317  ? 145.704 123.024 121.820 1.00 1.52   ? 317  SER A C     1 
ATOM   2285  O  O     . SER A 1  317  ? 144.893 123.943 121.865 1.00 5.85   ? 317  SER A O     1 
ATOM   2286  C  CB    . SER A 1  317  ? 145.023 120.848 120.834 1.00 4.34   ? 317  SER A CB    1 
ATOM   2287  O  OG    . SER A 1  317  ? 144.843 119.470 121.053 1.00 3.01   ? 317  SER A OG    1 
ATOM   2288  N  N     . GLN A 1  318  ? 146.982 123.188 121.509 1.00 6.04   ? 318  GLN A N     1 
ATOM   2289  C  CA    . GLN A 1  318  ? 147.482 124.315 120.738 1.00 3.03   ? 318  GLN A CA    1 
ATOM   2290  C  C     . GLN A 1  318  ? 147.842 123.792 119.364 1.00 5.07   ? 318  GLN A C     1 
ATOM   2291  O  O     . GLN A 1  318  ? 148.505 122.762 119.252 1.00 15.85  ? 318  GLN A O     1 
ATOM   2292  C  CB    . GLN A 1  318  ? 148.705 124.953 121.383 1.00 8.58   ? 318  GLN A CB    1 
ATOM   2293  C  CG    . GLN A 1  318  ? 148.405 125.781 122.578 1.00 9.42   ? 318  GLN A CG    1 
ATOM   2294  C  CD    . GLN A 1  318  ? 147.984 127.156 122.201 1.00 5.36   ? 318  GLN A CD    1 
ATOM   2295  O  OE1   . GLN A 1  318  ? 146.972 127.653 122.665 1.00 8.50   ? 318  GLN A OE1   1 
ATOM   2296  N  NE2   . GLN A 1  318  ? 148.754 127.784 121.342 1.00 12.28  ? 318  GLN A NE2   1 
ATOM   2297  N  N     . VAL A 1  319  ? 147.389 124.477 118.322 1.00 15.88  ? 319  VAL A N     1 
ATOM   2298  C  CA    . VAL A 1  319  ? 147.517 123.944 116.977 1.00 5.42   ? 319  VAL A CA    1 
ATOM   2299  C  C     . VAL A 1  319  ? 148.222 124.950 116.079 1.00 1.54   ? 319  VAL A C     1 
ATOM   2300  O  O     . VAL A 1  319  ? 148.272 126.146 116.355 1.00 6.30   ? 319  VAL A O     1 
ATOM   2301  C  CB    . VAL A 1  319  ? 146.147 123.534 116.384 1.00 6.08   ? 319  VAL A CB    1 
ATOM   2302  C  CG1   . VAL A 1  319  ? 145.552 122.426 117.190 1.00 1.86   ? 319  VAL A CG1   1 
ATOM   2303  C  CG2   . VAL A 1  319  ? 145.201 124.698 116.360 1.00 3.25   ? 319  VAL A CG2   1 
ATOM   2304  N  N     . TRP A 1  320  ? 148.801 124.430 115.009 1.00 1.89   ? 320  TRP A N     1 
ATOM   2305  C  CA    . TRP A 1  320  ? 149.377 125.226 113.946 1.00 0.78   ? 320  TRP A CA    1 
ATOM   2306  C  C     . TRP A 1  320  ? 148.352 125.410 112.834 1.00 3.01   ? 320  TRP A C     1 
ATOM   2307  O  O     . TRP A 1  320  ? 147.254 124.859 112.874 1.00 12.59  ? 320  TRP A O     1 
ATOM   2308  C  CB    . TRP A 1  320  ? 150.633 124.556 113.396 1.00 7.21   ? 320  TRP A CB    1 
ATOM   2309  C  CG    . TRP A 1  320  ? 151.766 124.458 114.349 1.00 9.98   ? 320  TRP A CG    1 
ATOM   2310  C  CD1   . TRP A 1  320  ? 152.391 123.326 114.746 1.00 9.54   ? 320  TRP A CD1   1 
ATOM   2311  C  CD2   . TRP A 1  320  ? 152.433 125.535 115.004 1.00 11.96  ? 320  TRP A CD2   1 
ATOM   2312  N  NE1   . TRP A 1  320  ? 153.395 123.622 115.622 1.00 12.06  ? 320  TRP A NE1   1 
ATOM   2313  C  CE2   . TRP A 1  320  ? 153.445 124.976 115.793 1.00 14.75  ? 320  TRP A CE2   1 
ATOM   2314  C  CE3   . TRP A 1  320  ? 152.269 126.919 115.003 1.00 8.25   ? 320  TRP A CE3   1 
ATOM   2315  C  CZ2   . TRP A 1  320  ? 154.282 125.748 116.577 1.00 11.49  ? 320  TRP A CZ2   1 
ATOM   2316  C  CZ3   . TRP A 1  320  ? 153.095 127.674 115.775 1.00 7.46   ? 320  TRP A CZ3   1 
ATOM   2317  C  CH2   . TRP A 1  320  ? 154.087 127.095 116.556 1.00 7.91   ? 320  TRP A CH2   1 
ATOM   2318  N  N     . SER A 1  321  ? 148.722 126.194 111.826 1.00 0.32   ? 321  SER A N     1 
ATOM   2319  C  CA    . SER A 1  321  ? 147.952 126.363 110.593 1.00 14.37  ? 321  SER A CA    1 
ATOM   2320  C  C     . SER A 1  321  ? 146.533 126.856 110.862 1.00 0.04   ? 321  SER A C     1 
ATOM   2321  O  O     . SER A 1  321  ? 145.558 126.337 110.326 1.00 10.14  ? 321  SER A O     1 
ATOM   2322  C  CB    . SER A 1  321  ? 147.918 125.068 109.786 1.00 1.28   ? 321  SER A CB    1 
ATOM   2323  O  OG    . SER A 1  321  ? 149.207 124.565 109.541 1.00 3.45   ? 321  SER A OG    1 
ATOM   2324  N  N     . ILE A 1  322  ? 146.420 127.890 111.683 1.00 13.57  ? 322  ILE A N     1 
ATOM   2325  C  CA    . ILE A 1  322  ? 145.130 128.450 112.048 1.00 7.25   ? 322  ILE A CA    1 
ATOM   2326  C  C     . ILE A 1  322  ? 145.233 129.971 112.028 1.00 4.40   ? 322  ILE A C     1 
ATOM   2327  O  O     . ILE A 1  322  ? 146.324 130.535 112.119 1.00 3.94   ? 322  ILE A O     1 
ATOM   2328  C  CB    . ILE A 1  322  ? 144.669 127.892 113.418 1.00 1.06   ? 322  ILE A CB    1 
ATOM   2329  C  CG1   . ILE A 1  322  ? 143.207 128.252 113.701 1.00 0.94   ? 322  ILE A CG1   1 
ATOM   2330  C  CG2   . ILE A 1  322  ? 145.627 128.305 114.521 1.00 11.75  ? 322  ILE A CG2   1 
ATOM   2331  C  CD1   . ILE A 1  322  ? 142.564 127.397 114.716 1.00 8.14   ? 322  ILE A CD1   1 
ATOM   2332  N  N     . SER A 1  323  ? 144.091 130.637 111.862 1.00 0.18   ? 323  SER A N     1 
ATOM   2333  C  CA    . SER A 1  323  ? 144.036 132.091 111.794 1.00 1.58   ? 323  SER A CA    1 
ATOM   2334  C  C     . SER A 1  323  ? 142.838 132.606 112.573 1.00 15.35  ? 323  SER A C     1 
ATOM   2335  O  O     . SER A 1  323  ? 141.907 131.872 112.886 1.00 2.96   ? 323  SER A O     1 
ATOM   2336  C  CB    . SER A 1  323  ? 143.989 132.591 110.351 1.00 9.68   ? 323  SER A CB    1 
ATOM   2337  O  OG    . SER A 1  323  ? 143.002 131.931 109.602 1.00 3.73   ? 323  SER A OG    1 
ATOM   2338  N  N     . ARG A 1  324  ? 142.877 133.895 112.884 1.00 0.30   ? 324  ARG A N     1 
ATOM   2339  C  CA    . ARG A 1  324  ? 141.852 134.554 113.676 1.00 1.40   ? 324  ARG A CA    1 
ATOM   2340  C  C     . ARG A 1  324  ? 141.744 135.997 113.209 1.00 1.51   ? 324  ARG A C     1 
ATOM   2341  O  O     . ARG A 1  324  ? 142.754 136.615 112.892 1.00 3.40   ? 324  ARG A O     1 
ATOM   2342  C  CB    . ARG A 1  324  ? 142.195 134.484 115.163 1.00 5.80   ? 324  ARG A CB    1 
ATOM   2343  C  CG    . ARG A 1  324  ? 141.164 135.077 116.079 1.00 2.89   ? 324  ARG A CG    1 
ATOM   2344  C  CD    . ARG A 1  324  ? 141.500 134.776 117.509 1.00 3.10   ? 324  ARG A CD    1 
ATOM   2345  N  NE    . ARG A 1  324  ? 140.620 135.469 118.439 1.00 10.05  ? 324  ARG A NE    1 
ATOM   2346  C  CZ    . ARG A 1  324  ? 139.495 134.973 118.936 1.00 10.60  ? 324  ARG A CZ    1 
ATOM   2347  N  NH1   . ARG A 1  324  ? 139.058 133.774 118.596 1.00 9.07   ? 324  ARG A NH1   1 
ATOM   2348  N  NH2   . ARG A 1  324  ? 138.792 135.700 119.797 1.00 4.56   ? 324  ARG A NH2   1 
ATOM   2349  N  N     . SER A 1  325  ? 140.525 136.524 113.150 1.00 13.19  ? 325  SER A N     1 
ATOM   2350  C  CA    . SER A 1  325  ? 140.310 137.900 112.721 1.00 2.01   ? 325  SER A CA    1 
ATOM   2351  C  C     . SER A 1  325  ? 138.898 138.324 113.094 1.00 4.46   ? 325  SER A C     1 
ATOM   2352  O  O     . SER A 1  325  ? 138.083 137.520 113.544 1.00 13.10  ? 325  SER A O     1 
ATOM   2353  C  CB    . SER A 1  325  ? 140.544 138.066 111.221 1.00 7.81   ? 325  SER A CB    1 
ATOM   2354  O  OG    . SER A 1  325  ? 140.667 139.419 110.863 1.00 10.62  ? 325  SER A OG    1 
ATOM   2355  N  N     . THR A 1  326  ? 138.636 139.617 112.923 1.00 7.20   ? 326  THR A N     1 
ATOM   2356  C  CA    . THR A 1  326  ? 137.316 140.197 113.131 1.00 6.33   ? 326  THR A CA    1 
ATOM   2357  C  C     . THR A 1  326  ? 136.409 139.902 111.947 1.00 5.88   ? 326  THR A C     1 
ATOM   2358  O  O     . THR A 1  326  ? 136.848 139.879 110.799 1.00 6.27   ? 326  THR A O     1 
ATOM   2359  C  CB    . THR A 1  326  ? 137.446 141.708 113.333 1.00 0.46   ? 326  THR A CB    1 
ATOM   2360  O  OG1   . THR A 1  326  ? 138.356 141.969 114.401 1.00 11.20  ? 326  THR A OG1   1 
ATOM   2361  C  CG2   . THR A 1  326  ? 136.128 142.363 113.643 1.00 4.29   ? 326  THR A CG2   1 
ATOM   2362  N  N     . ILE A 1  327  ? 135.137 139.698 112.223 1.00 7.50   ? 327  ILE A N     1 
ATOM   2363  C  CA    . ILE A 1  327  ? 134.180 139.349 111.186 1.00 7.52   ? 327  ILE A CA    1 
ATOM   2364  C  C     . ILE A 1  327  ? 133.352 140.568 110.814 1.00 8.11   ? 327  ILE A C     1 
ATOM   2365  O  O     . ILE A 1  327  ? 133.105 141.465 111.622 1.00 1.33   ? 327  ILE A O     1 
ATOM   2366  C  CB    . ILE A 1  327  ? 133.284 138.167 111.610 1.00 4.17   ? 327  ILE A CB    1 
ATOM   2367  C  CG1   . ILE A 1  327  ? 132.557 138.482 112.908 1.00 1.06   ? 327  ILE A CG1   1 
ATOM   2368  C  CG2   . ILE A 1  327  ? 134.114 136.909 111.746 1.00 14.27  ? 327  ILE A CG2   1 
ATOM   2369  C  CD1   . ILE A 1  327  ? 131.372 137.628 113.167 1.00 13.82  ? 327  ILE A CD1   1 
ATOM   2370  N  N     . CYS A 1  328  ? 132.914 140.588 109.565 1.00 13.40  ? 328  CYS A N     1 
ATOM   2371  C  CA    . CYS A 1  328  ? 132.174 141.696 108.993 1.00 5.02   ? 328  CYS A CA    1 
ATOM   2372  C  C     . CYS A 1  328  ? 131.230 141.126 107.949 1.00 8.45   ? 328  CYS A C     1 
ATOM   2373  O  O     . CYS A 1  328  ? 131.397 139.996 107.497 1.00 2.99   ? 328  CYS A O     1 
ATOM   2374  C  CB    . CYS A 1  328  ? 133.143 142.743 108.422 1.00 0.73   ? 328  CYS A CB    1 
ATOM   2375  S  SG    . CYS A 1  328  ? 132.908 143.240 106.743 1.00 17.23  ? 328  CYS A SG    1 
ATOM   2376  N  N     . GLY A 1  329  ? 130.221 141.904 107.587 1.00 0.26   ? 329  GLY A N     1 
ATOM   2377  C  CA    . GLY A 1  329  ? 129.206 141.439 106.669 1.00 11.52  ? 329  GLY A CA    1 
ATOM   2378  C  C     . GLY A 1  329  ? 129.529 141.699 105.210 1.00 1.15   ? 329  GLY A C     1 
ATOM   2379  O  O     . GLY A 1  329  ? 130.210 142.651 104.864 1.00 11.44  ? 329  GLY A O     1 
ATOM   2380  N  N     . ASN A 1  330  ? 129.013 140.829 104.354 1.00 10.02  ? 330  ASN A N     1 
ATOM   2381  C  CA    . ASN A 1  330  ? 129.202 140.936 102.912 1.00 5.62   ? 330  ASN A CA    1 
ATOM   2382  C  C     . ASN A 1  330  ? 128.020 140.245 102.251 1.00 2.20   ? 330  ASN A C     1 
ATOM   2383  O  O     . ASN A 1  330  ? 127.912 139.022 102.285 1.00 7.97   ? 330  ASN A O     1 
ATOM   2384  C  CB    . ASN A 1  330  ? 130.533 140.323 102.488 1.00 0.35   ? 330  ASN A CB    1 
ATOM   2385  C  CG    . ASN A 1  330  ? 130.871 140.577 101.037 1.00 0.96   ? 330  ASN A CG    1 
ATOM   2386  O  OD1   . ASN A 1  330  ? 130.010 140.851 100.229 1.00 0.07   ? 330  ASN A OD1   1 
ATOM   2387  N  ND2   . ASN A 1  330  ? 132.140 140.507 100.713 1.00 14.35  ? 330  ASN A ND2   1 
ATOM   2388  N  N     . SER A 1  331  ? 127.130 141.028 101.660 1.00 10.14  ? 331  SER A N     1 
ATOM   2389  C  CA    . SER A 1  331  ? 125.894 140.483 101.127 1.00 8.17   ? 331  SER A CA    1 
ATOM   2390  C  C     . SER A 1  331  ? 126.055 139.886 99.742  1.00 9.35   ? 331  SER A C     1 
ATOM   2391  O  O     . SER A 1  331  ? 125.096 139.330 99.216  1.00 17.91  ? 331  SER A O     1 
ATOM   2392  C  CB    . SER A 1  331  ? 124.810 141.561 101.129 1.00 7.60   ? 331  SER A CB    1 
ATOM   2393  O  OG    . SER A 1  331  ? 125.068 142.562 100.181 1.00 12.11  ? 331  SER A OG    1 
ATOM   2394  N  N     . ASP A 1  332  ? 127.235 139.967 99.151  1.00 7.75   ? 332  ASP A N     1 
ATOM   2395  C  CA    . ASP A 1  332  ? 127.521 139.313 97.886  1.00 3.49   ? 332  ASP A CA    1 
ATOM   2396  C  C     . ASP A 1  332  ? 128.098 137.921 98.061  1.00 14.47  ? 332  ASP A C     1 
ATOM   2397  O  O     . ASP A 1  332  ? 128.434 137.278 97.070  1.00 6.77   ? 332  ASP A O     1 
ATOM   2398  C  CB    . ASP A 1  332  ? 128.483 140.164 97.068  1.00 3.25   ? 332  ASP A CB    1 
ATOM   2399  C  CG    . ASP A 1  332  ? 127.811 141.358 96.454  1.00 12.95  ? 332  ASP A CG    1 
ATOM   2400  O  OD1   . ASP A 1  332  ? 126.741 141.194 95.838  1.00 18.83  ? 332  ASP A OD1   1 
ATOM   2401  O  OD2   . ASP A 1  332  ? 128.341 142.472 96.605  1.00 17.18  ? 332  ASP A OD2   1 
ATOM   2402  N  N     . LEU A 1  333  ? 128.218 137.447 99.291  1.00 1.09   ? 333  LEU A N     1 
ATOM   2403  C  CA    . LEU A 1  333  ? 128.666 136.098 99.572  1.00 13.08  ? 333  LEU A CA    1 
ATOM   2404  C  C     . LEU A 1  333  ? 127.475 135.177 99.768  1.00 4.01   ? 333  LEU A C     1 
ATOM   2405  O  O     . LEU A 1  333  ? 126.463 135.572 100.344 1.00 2.75   ? 333  LEU A O     1 
ATOM   2406  C  CB    . LEU A 1  333  ? 129.535 136.076 100.823 1.00 0.76   ? 333  LEU A CB    1 
ATOM   2407  C  CG    . LEU A 1  333  ? 130.928 136.674 100.775 1.00 10.59  ? 333  LEU A CG    1 
ATOM   2408  C  CD1   . LEU A 1  333  ? 131.518 136.610 102.141 1.00 1.64   ? 333  LEU A CD1   1 
ATOM   2409  C  CD2   . LEU A 1  333  ? 131.795 135.966 99.781  1.00 13.76  ? 333  LEU A CD2   1 
ATOM   2410  N  N     . HIS A 1  334  ? 127.599 133.946 99.287  1.00 2.17   ? 334  HIS A N     1 
ATOM   2411  C  CA    . HIS A 1  334  ? 126.599 132.941 99.587  1.00 2.50   ? 334  HIS A CA    1 
ATOM   2412  C  C     . HIS A 1  334  ? 126.674 132.554 101.057 1.00 12.47  ? 334  HIS A C     1 
ATOM   2413  O  O     . HIS A 1  334  ? 127.614 132.889 101.767 1.00 6.04   ? 334  HIS A O     1 
ATOM   2414  C  CB    . HIS A 1  334  ? 126.790 131.710 98.714  1.00 4.44   ? 334  HIS A CB    1 
ATOM   2415  C  CG    . HIS A 1  334  ? 126.412 131.921 97.288  1.00 11.62  ? 334  HIS A CG    1 
ATOM   2416  N  ND1   . HIS A 1  334  ? 125.285 131.368 96.728  1.00 5.22   ? 334  HIS A ND1   1 
ATOM   2417  C  CD2   . HIS A 1  334  ? 127.000 132.640 96.311  1.00 3.16   ? 334  HIS A CD2   1 
ATOM   2418  C  CE1   . HIS A 1  334  ? 125.205 131.723 95.461  1.00 1.52   ? 334  HIS A CE1   1 
ATOM   2419  N  NE2   . HIS A 1  334  ? 126.234 132.498 95.184  1.00 4.54   ? 334  HIS A NE2   1 
ATOM   2420  N  N     . LEU A 1  335  ? 125.646 131.852 101.520 1.00 1.06   ? 335  LEU A N     1 
ATOM   2421  C  CA    . LEU A 1  335  ? 125.571 131.512 102.935 1.00 1.03   ? 335  LEU A CA    1 
ATOM   2422  C  C     . LEU A 1  335  ? 126.649 130.524 103.346 1.00 4.40   ? 335  LEU A C     1 
ATOM   2423  O  O     . LEU A 1  335  ? 127.036 130.490 104.514 1.00 9.69   ? 335  LEU A O     1 
ATOM   2424  C  CB    . LEU A 1  335  ? 124.193 130.954 103.266 1.00 1.01   ? 335  LEU A CB    1 
ATOM   2425  C  CG    . LEU A 1  335  ? 123.179 131.954 103.807 1.00 15.80  ? 335  LEU A CG    1 
ATOM   2426  C  CD1   . LEU A 1  335  ? 122.705 132.876 102.720 1.00 6.84   ? 335  LEU A CD1   1 
ATOM   2427  C  CD2   . LEU A 1  335  ? 122.021 131.221 104.409 1.00 10.24  ? 335  LEU A CD2   1 
ATOM   2428  N  N     . ASP A 1  336  ? 127.144 129.714 102.417 1.00 14.41  ? 336  ASP A N     1 
ATOM   2429  C  CA    . ASP A 1  336  ? 128.200 128.759 102.702 1.00 8.66   ? 336  ASP A CA    1 
ATOM   2430  C  C     . ASP A 1  336  ? 129.544 129.207 102.166 1.00 9.81   ? 336  ASP A C     1 
ATOM   2431  O  O     . ASP A 1  336  ? 130.361 128.370 101.785 1.00 18.05  ? 336  ASP A O     1 
ATOM   2432  C  CB    . ASP A 1  336  ? 127.851 127.395 102.129 1.00 15.93  ? 336  ASP A CB    1 
ATOM   2433  C  CG    . ASP A 1  336  ? 127.382 127.475 100.722 1.00 20.22  ? 336  ASP A CG    1 
ATOM   2434  O  OD1   . ASP A 1  336  ? 126.792 128.496 100.360 1.00 24.61  ? 336  ASP A OD1   1 
ATOM   2435  O  OD2   . ASP A 1  336  ? 127.617 126.520 99.963  1.00 26.42  ? 336  ASP A OD2   1 
ATOM   2436  N  N     . GLU A 1  337  ? 129.782 130.503 102.112 1.00 3.25   ? 337  GLU A N     1 
ATOM   2437  C  CA    . GLU A 1  337  ? 131.044 131.057 101.675 1.00 1.84   ? 337  GLU A CA    1 
ATOM   2438  C  C     . GLU A 1  337  ? 131.590 131.960 102.764 1.00 13.62  ? 337  GLU A C     1 
ATOM   2439  O  O     . GLU A 1  337  ? 130.841 132.510 103.570 1.00 2.27   ? 337  GLU A O     1 
ATOM   2440  C  CB    . GLU A 1  337  ? 130.880 131.836 100.383 1.00 8.27   ? 337  GLU A CB    1 
ATOM   2441  C  CG    . GLU A 1  337  ? 130.827 130.983 99.155  1.00 1.36   ? 337  GLU A CG    1 
ATOM   2442  C  CD    . GLU A 1  337  ? 130.492 131.783 97.928  1.00 5.97   ? 337  GLU A CD    1 
ATOM   2443  O  OE1   . GLU A 1  337  ? 130.068 132.942 98.069  1.00 11.48  ? 337  GLU A OE1   1 
ATOM   2444  O  OE2   . GLU A 1  337  ? 130.652 131.267 96.812  1.00 13.68  ? 337  GLU A OE2   1 
ATOM   2445  N  N     . VAL A 1  338  ? 132.901 132.089 102.804 1.00 15.30  ? 338  VAL A N     1 
ATOM   2446  C  CA    . VAL A 1  338  ? 133.562 133.022 103.701 1.00 0.46   ? 338  VAL A CA    1 
ATOM   2447  C  C     . VAL A 1  338  ? 134.630 133.748 102.902 1.00 11.62  ? 338  VAL A C     1 
ATOM   2448  O  O     . VAL A 1  338  ? 135.350 133.136 102.112 1.00 15.28  ? 338  VAL A O     1 
ATOM   2449  C  CB    . VAL A 1  338  ? 134.140 132.307 104.949 1.00 15.31  ? 338  VAL A CB    1 
ATOM   2450  C  CG1   . VAL A 1  338  ? 135.157 131.257 104.562 1.00 0.71   ? 338  VAL A CG1   1 
ATOM   2451  C  CG2   . VAL A 1  338  ? 134.724 133.290 105.928 1.00 11.50  ? 338  VAL A CG2   1 
ATOM   2452  N  N     . GLY A 1  339  ? 134.702 135.065 103.073 1.00 2.55   ? 339  GLY A N     1 
ATOM   2453  C  CA    . GLY A 1  339  ? 135.719 135.861 102.424 1.00 3.98   ? 339  GLY A CA    1 
ATOM   2454  C  C     . GLY A 1  339  ? 137.003 135.818 103.218 1.00 6.02   ? 339  GLY A C     1 
ATOM   2455  O  O     . GLY A 1  339  ? 136.999 136.009 104.434 1.00 9.75   ? 339  GLY A O     1 
ATOM   2456  N  N     . TYR A 1  340  ? 138.106 135.569 102.522 1.00 7.90   ? 340  TYR A N     1 
ATOM   2457  C  CA    . TYR A 1  340  ? 139.403 135.343 103.142 1.00 3.51   ? 340  TYR A CA    1 
ATOM   2458  C  C     . TYR A 1  340  ? 140.403 136.376 102.654 1.00 0.85   ? 340  TYR A C     1 
ATOM   2459  O  O     . TYR A 1  340  ? 140.591 136.513 101.438 1.00 2.19   ? 340  TYR A O     1 
ATOM   2460  C  CB    . TYR A 1  340  ? 139.895 133.931 102.826 1.00 11.62  ? 340  TYR A CB    1 
ATOM   2461  C  CG    . TYR A 1  340  ? 140.819 133.342 103.862 1.00 6.62   ? 340  TYR A CG    1 
ATOM   2462  C  CD1   . TYR A 1  340  ? 140.633 133.590 105.204 1.00 4.72   ? 340  TYR A CD1   1 
ATOM   2463  C  CD2   . TYR A 1  340  ? 141.876 132.537 103.492 1.00 15.72  ? 340  TYR A CD2   1 
ATOM   2464  C  CE1   . TYR A 1  340  ? 141.469 133.068 106.135 1.00 3.69   ? 340  TYR A CE1   1 
ATOM   2465  C  CE2   . TYR A 1  340  ? 142.707 132.007 104.419 1.00 3.08   ? 340  TYR A CE2   1 
ATOM   2466  C  CZ    . TYR A 1  340  ? 142.506 132.277 105.737 1.00 6.68   ? 340  TYR A CZ    1 
ATOM   2467  O  OH    . TYR A 1  340  ? 143.344 131.739 106.671 1.00 4.09   ? 340  TYR A OH    1 
ATOM   2468  N  N     . PRO A 1  341  ? 141.058 137.123 103.537 1.00 6.51   ? 341  PRO A N     1 
ATOM   2469  C  CA    . PRO A 1  341  ? 142.096 138.059 103.090 1.00 1.49   ? 341  PRO A CA    1 
ATOM   2470  C  C     . PRO A 1  341  ? 143.231 137.348 102.365 1.00 9.48   ? 341  PRO A C     1 
ATOM   2471  O  O     . PRO A 1  341  ? 143.607 136.232 102.713 1.00 12.20  ? 341  PRO A O     1 
ATOM   2472  C  CB    . PRO A 1  341  ? 142.579 138.693 104.395 1.00 12.51  ? 341  PRO A CB    1 
ATOM   2473  C  CG    . PRO A 1  341  ? 141.483 138.496 105.335 1.00 8.00   ? 341  PRO A CG    1 
ATOM   2474  C  CD    . PRO A 1  341  ? 140.815 137.229 104.981 1.00 6.68   ? 341  PRO A CD    1 
ATOM   2475  N  N     . ILE A 1  342  ? 143.791 138.018 101.357 1.00 2.23   ? 342  ILE A N     1 
ATOM   2476  C  CA    . ILE A 1  342  ? 144.811 137.393 100.522 1.00 2.57   ? 342  ILE A CA    1 
ATOM   2477  C  C     . ILE A 1  342  ? 146.096 137.135 101.300 1.00 4.79   ? 342  ILE A C     1 
ATOM   2478  O  O     . ILE A 1  342  ? 146.793 136.155 101.036 1.00 7.10   ? 342  ILE A O     1 
ATOM   2479  C  CB    . ILE A 1  342  ? 145.078 138.230 99.258  1.00 10.54  ? 342  ILE A CB    1 
ATOM   2480  C  CG1   . ILE A 1  342  ? 146.055 137.492 98.345  1.00 0.17   ? 342  ILE A CG1   1 
ATOM   2481  C  CG2   . ILE A 1  342  ? 145.605 139.594 99.612  1.00 0.55   ? 342  ILE A CG2   1 
ATOM   2482  C  CD1   . ILE A 1  342  ? 146.055 137.964 96.953  1.00 6.11   ? 342  ILE A CD1   1 
ATOM   2483  N  N     . SER A 1  343  ? 146.439 137.994 102.255 1.00 1.59   ? 343  SER A N     1 
ATOM   2484  C  CA    . SER A 1  343  ? 147.648 137.771 103.038 1.00 4.26   ? 343  SER A CA    1 
ATOM   2485  C  C     . SER A 1  343  ? 147.554 136.494 103.862 1.00 4.20   ? 343  SER A C     1 
ATOM   2486  O  O     . SER A 1  343  ? 148.550 135.789 104.043 1.00 9.74   ? 343  SER A O     1 
ATOM   2487  C  CB    . SER A 1  343  ? 147.910 138.969 103.936 1.00 1.54   ? 343  SER A CB    1 
ATOM   2488  O  OG    . SER A 1  343  ? 146.800 139.201 104.773 1.00 8.24   ? 343  SER A OG    1 
ATOM   2489  N  N     . PHE A 1  344  ? 146.369 136.189 104.383 1.00 3.38   ? 344  PHE A N     1 
ATOM   2490  C  CA    . PHE A 1  344  ? 146.164 134.947 105.114 1.00 0.47   ? 344  PHE A CA    1 
ATOM   2491  C  C     . PHE A 1  344  ? 146.204 133.738 104.193 1.00 1.83   ? 344  PHE A C     1 
ATOM   2492  O  O     . PHE A 1  344  ? 146.551 132.640 104.632 1.00 1.65   ? 344  PHE A O     1 
ATOM   2493  C  CB    . PHE A 1  344  ? 144.828 134.992 105.845 1.00 0.12   ? 344  PHE A CB    1 
ATOM   2494  C  CG    . PHE A 1  344  ? 144.873 135.703 107.152 1.00 2.11   ? 344  PHE A CG    1 
ATOM   2495  C  CD1   . PHE A 1  344  ? 145.950 136.485 107.500 1.00 10.77  ? 344  PHE A CD1   1 
ATOM   2496  C  CD2   . PHE A 1  344  ? 143.838 135.587 108.039 1.00 0.31   ? 344  PHE A CD2   1 
ATOM   2497  C  CE1   . PHE A 1  344  ? 145.972 137.134 108.704 1.00 6.39   ? 344  PHE A CE1   1 
ATOM   2498  C  CE2   . PHE A 1  344  ? 143.865 136.228 109.234 1.00 0.25   ? 344  PHE A CE2   1 
ATOM   2499  C  CZ    . PHE A 1  344  ? 144.924 136.990 109.566 1.00 0.87   ? 344  PHE A CZ    1 
ATOM   2500  N  N     . ALA A 1  345  ? 145.817 133.909 102.930 1.00 11.55  ? 345  ALA A N     1 
ATOM   2501  C  CA    . ALA A 1  345  ? 145.789 132.795 101.992 1.00 3.25   ? 345  ALA A CA    1 
ATOM   2502  C  C     . ALA A 1  345  ? 147.184 132.410 101.520 1.00 5.78   ? 345  ALA A C     1 
ATOM   2503  O  O     . ALA A 1  345  ? 147.379 131.297 101.028 1.00 7.46   ? 345  ALA A O     1 
ATOM   2504  C  CB    . ALA A 1  345  ? 144.903 133.141 100.799 1.00 13.08  ? 345  ALA A CB    1 
ATOM   2505  N  N     . ARG A 1  346  ? 148.154 133.309 101.635 1.00 4.04   ? 346  ARG A N     1 
ATOM   2506  C  CA    . ARG A 1  346  ? 149.536 132.983 101.334 1.00 0.15   ? 346  ARG A CA    1 
ATOM   2507  C  C     . ARG A 1  346  ? 150.322 132.548 102.558 1.00 4.58   ? 346  ARG A C     1 
ATOM   2508  O  O     . ARG A 1  346  ? 151.502 132.226 102.429 1.00 11.59  ? 346  ARG A O     1 
ATOM   2509  C  CB    . ARG A 1  346  ? 150.230 134.175 100.673 1.00 6.34   ? 346  ARG A CB    1 
ATOM   2510  C  CG    . ARG A 1  346  ? 149.338 134.939 99.733  1.00 13.97  ? 346  ARG A CG    1 
ATOM   2511  C  CD    . ARG A 1  346  ? 150.089 135.588 98.601  1.00 7.04   ? 346  ARG A CD    1 
ATOM   2512  N  NE    . ARG A 1  346  ? 150.912 134.646 97.859  1.00 20.35  ? 346  ARG A NE    1 
ATOM   2513  C  CZ    . ARG A 1  346  ? 151.833 134.995 96.973  1.00 17.22  ? 346  ARG A CZ    1 
ATOM   2514  N  NH1   . ARG A 1  346  ? 152.066 136.261 96.685  1.00 16.65  ? 346  ARG A NH1   1 
ATOM   2515  N  NH2   . ARG A 1  346  ? 152.533 134.048 96.361  1.00 10.52  ? 346  ARG A NH2   1 
ATOM   2516  N  N     . THR A 1  347  ? 149.704 132.546 103.735 1.00 3.46   ? 347  THR A N     1 
ATOM   2517  C  CA    . THR A 1  347  ? 150.320 132.051 104.959 1.00 10.69  ? 347  THR A CA    1 
ATOM   2518  C  C     . THR A 1  347  ? 149.896 130.615 105.235 1.00 0.15   ? 347  THR A C     1 
ATOM   2519  O  O     . THR A 1  347  ? 150.722 129.772 105.585 1.00 9.59   ? 347  THR A O     1 
ATOM   2520  C  CB    . THR A 1  347  ? 149.946 132.955 106.137 1.00 1.02   ? 347  THR A CB    1 
ATOM   2521  O  OG1   . THR A 1  347  ? 150.440 134.276 105.903 1.00 11.97  ? 347  THR A OG1   1 
ATOM   2522  C  CG2   . THR A 1  347  ? 150.514 132.428 107.429 1.00 12.15  ? 347  THR A CG2   1 
ATOM   2523  N  N     . LEU A 1  348  ? 148.612 130.331 105.092 1.00 0.14   ? 348  LEU A N     1 
ATOM   2524  C  CA    . LEU A 1  348  ? 148.108 128.978 105.218 1.00 0.28   ? 348  LEU A CA    1 
ATOM   2525  C  C     . LEU A 1  348  ? 148.204 128.278 103.874 1.00 0.51   ? 348  LEU A C     1 
ATOM   2526  O  O     . LEU A 1  348  ? 148.065 128.898 102.821 1.00 10.38  ? 348  LEU A O     1 
ATOM   2527  C  CB    . LEU A 1  348  ? 146.666 128.992 105.731 1.00 1.09   ? 348  LEU A CB    1 
ATOM   2528  C  CG    . LEU A 1  348  ? 146.473 128.908 107.249 1.00 0.09   ? 348  LEU A CG    1 
ATOM   2529  C  CD1   . LEU A 1  348  ? 146.870 130.190 107.941 1.00 1.07   ? 348  LEU A CD1   1 
ATOM   2530  C  CD2   . LEU A 1  348  ? 145.048 128.534 107.608 1.00 9.20   ? 348  LEU A CD2   1 
ATOM   2531  N  N     . GLN A 1  349  ? 148.465 126.977 103.912 1.00 4.68   ? 349  GLN A N     1 
ATOM   2532  C  CA    . GLN A 1  349  ? 148.788 126.216 102.716 1.00 1.63   ? 349  GLN A CA    1 
ATOM   2533  C  C     . GLN A 1  349  ? 147.923 124.968 102.636 1.00 0.75   ? 349  GLN A C     1 
ATOM   2534  O  O     . GLN A 1  349  ? 147.289 124.556 103.605 1.00 12.49  ? 349  GLN A O     1 
ATOM   2535  C  CB    . GLN A 1  349  ? 150.277 125.844 102.689 1.00 0.37   ? 349  GLN A CB    1 
ATOM   2536  C  CG    . GLN A 1  349  ? 151.225 127.016 102.914 1.00 1.57   ? 349  GLN A CG    1 
ATOM   2537  C  CD    . GLN A 1  349  ? 151.472 127.833 101.664 1.00 8.48   ? 349  GLN A CD    1 
ATOM   2538  O  OE1   . GLN A 1  349  ? 151.852 127.298 100.637 1.00 12.28  ? 349  GLN A OE1   1 
ATOM   2539  N  NE2   . GLN A 1  349  ? 151.257 129.131 101.746 1.00 3.29   ? 349  GLN A NE2   1 
ATOM   2540  N  N     . VAL A 1  350  ? 147.884 124.377 101.449 1.00 0.89   ? 350  VAL A N     1 
ATOM   2541  C  CA    . VAL A 1  350  ? 147.245 123.088 101.210 1.00 3.94   ? 350  VAL A CA    1 
ATOM   2542  C  C     . VAL A 1  350  ? 148.300 122.173 100.608 1.00 7.05   ? 350  VAL A C     1 
ATOM   2543  O  O     . VAL A 1  350  ? 149.025 122.581 99.697  1.00 11.02  ? 350  VAL A O     1 
ATOM   2544  C  CB    . VAL A 1  350  ? 146.027 123.206 100.278 1.00 0.68   ? 350  VAL A CB    1 
ATOM   2545  C  CG1   . VAL A 1  350  ? 145.583 121.851 99.802  1.00 2.78   ? 350  VAL A CG1   1 
ATOM   2546  C  CG2   . VAL A 1  350  ? 144.891 123.904 100.965 1.00 0.30   ? 350  VAL A CG2   1 
ATOM   2547  N  N     . ALA A 1  351  ? 148.404 120.954 101.124 1.00 2.31   ? 351  ALA A N     1 
ATOM   2548  C  CA    . ALA A 1  351  ? 149.408 120.007 100.664 1.00 4.21   ? 351  ALA A CA    1 
ATOM   2549  C  C     . ALA A 1  351  ? 148.870 119.150 99.525  1.00 9.96   ? 351  ALA A C     1 
ATOM   2550  O  O     . ALA A 1  351  ? 147.855 118.471 99.678  1.00 14.04  ? 351  ALA A O     1 
ATOM   2551  C  CB    . ALA A 1  351  ? 149.850 119.122 101.821 1.00 1.88   ? 351  ALA A CB    1 
ATOM   2552  N  N     . GLU A 1  352  ? 149.560 119.167 98.387  1.00 7.83   ? 352  GLU A N     1 
ATOM   2553  C  CA    . GLU A 1  352  ? 149.136 118.431 97.200  1.00 3.74   ? 352  GLU A CA    1 
ATOM   2554  C  C     . GLU A 1  352  ? 150.232 117.465 96.784  1.00 7.84   ? 352  GLU A C     1 
ATOM   2555  O  O     . GLU A 1  352  ? 151.382 117.869 96.604  1.00 21.02  ? 352  GLU A O     1 
ATOM   2556  C  CB    . GLU A 1  352  ? 148.810 119.384 96.051  1.00 5.39   ? 352  GLU A CB    1 
ATOM   2557  C  CG    . GLU A 1  352  ? 147.659 120.319 96.325  1.00 11.77  ? 352  GLU A CG    1 
ATOM   2558  C  CD    . GLU A 1  352  ? 146.463 120.048 95.449  1.00 17.62  ? 352  GLU A CD    1 
ATOM   2559  O  OE1   . GLU A 1  352  ? 145.826 121.012 94.985  1.00 14.01  ? 352  GLU A OE1   1 
ATOM   2560  O  OE2   . GLU A 1  352  ? 146.151 118.866 95.228  1.00 17.57  ? 352  GLU A OE2   1 
ATOM   2561  N  N     . THR A 1  353  ? 149.882 116.197 96.626  1.00 10.88  ? 353  THR A N     1 
ATOM   2562  C  CA    . THR A 1  353  ? 150.851 115.190 96.223  1.00 13.07  ? 353  THR A CA    1 
ATOM   2563  C  C     . THR A 1  353  ? 150.890 115.095 94.707  1.00 13.66  ? 353  THR A C     1 
ATOM   2564  O  O     . THR A 1  353  ? 149.848 114.996 94.055  1.00 12.77  ? 353  THR A O     1 
ATOM   2565  C  CB    . THR A 1  353  ? 150.513 113.831 96.832  1.00 14.32  ? 353  THR A CB    1 
ATOM   2566  O  OG1   . THR A 1  353  ? 150.406 113.958 98.252  1.00 16.28  ? 353  THR A OG1   1 
ATOM   2567  C  CG2   . THR A 1  353  ? 151.593 112.829 96.523  1.00 13.59  ? 353  THR A CG2   1 
ATOM   2568  N  N     . VAL A 1  354  ? 152.098 115.128 94.149  1.00 20.22  ? 354  VAL A N     1 
ATOM   2569  C  CA    . VAL A 1  354  ? 152.259 115.178 92.704  1.00 18.77  ? 354  VAL A CA    1 
ATOM   2570  C  C     . VAL A 1  354  ? 152.028 113.794 92.119  1.00 19.03  ? 354  VAL A C     1 
ATOM   2571  O  O     . VAL A 1  354  ? 152.673 112.817 92.512  1.00 28.54  ? 354  VAL A O     1 
ATOM   2572  C  CB    . VAL A 1  354  ? 153.649 115.717 92.341  1.00 19.98  ? 354  VAL A CB    1 
ATOM   2573  C  CG1   . VAL A 1  354  ? 153.784 115.865 90.846  1.00 20.70  ? 354  VAL A CG1   1 
ATOM   2574  C  CG2   . VAL A 1  354  ? 153.894 117.038 93.032  1.00 19.76  ? 354  VAL A CG2   1 
ATOM   2575  N  N     . GLN A 1  355  ? 151.097 113.705 91.180  1.00 19.07  ? 355  GLN A N     1 
ATOM   2576  C  CA    . GLN A 1  355  ? 150.801 112.472 90.477  1.00 18.46  ? 355  GLN A CA    1 
ATOM   2577  C  C     . GLN A 1  355  ? 150.675 112.805 89.000  1.00 20.12  ? 355  GLN A C     1 
ATOM   2578  O  O     . GLN A 1  355  ? 150.840 113.953 88.589  1.00 23.71  ? 355  GLN A O     1 
ATOM   2579  C  CB    . GLN A 1  355  ? 149.523 111.815 91.009  1.00 20.10  ? 355  GLN A CB    1 
ATOM   2580  C  CG    . GLN A 1  355  ? 149.652 111.138 92.363  1.00 19.43  ? 355  GLN A CG    1 
ATOM   2581  C  CD    . GLN A 1  355  ? 150.393 109.825 92.306  1.00 22.31  ? 355  GLN A CD    1 
ATOM   2582  O  OE1   . GLN A 1  355  ? 151.360 109.612 93.030  1.00 24.16  ? 355  GLN A OE1   1 
ATOM   2583  N  NE2   . GLN A 1  355  ? 149.948 108.938 91.436  1.00 26.94  ? 355  GLN A NE2   1 
ATOM   2584  N  N     . HIS A 1  356  ? 150.371 111.796 88.192  1.00 24.80  ? 356  HIS A N     1 
ATOM   2585  C  CA    . HIS A 1  356  ? 150.227 112.027 86.763  1.00 24.43  ? 356  HIS A CA    1 
ATOM   2586  C  C     . HIS A 1  356  ? 148.969 112.810 86.427  1.00 26.15  ? 356  HIS A C     1 
ATOM   2587  O  O     . HIS A 1  356  ? 148.939 113.490 85.399  1.00 28.78  ? 356  HIS A O     1 
ATOM   2588  C  CB    . HIS A 1  356  ? 150.225 110.697 86.013  1.00 27.05  ? 356  HIS A CB    1 
ATOM   2589  C  CG    . HIS A 1  356  ? 149.019 109.853 86.288  1.00 33.37  ? 356  HIS A CG    1 
ATOM   2590  N  ND1   . HIS A 1  356  ? 148.877 109.109 87.439  1.00 34.75  ? 356  HIS A ND1   1 
ATOM   2591  C  CD2   . HIS A 1  356  ? 147.906 109.620 85.551  1.00 30.18  ? 356  HIS A CD2   1 
ATOM   2592  C  CE1   . HIS A 1  356  ? 147.724 108.467 87.407  1.00 32.54  ? 356  HIS A CE1   1 
ATOM   2593  N  NE2   . HIS A 1  356  ? 147.115 108.760 86.272  1.00 31.68  ? 356  HIS A NE2   1 
ATOM   2594  N  N     . TYR A 1  357  ? 147.933 112.733 87.258  1.00 25.31  ? 357  TYR A N     1 
ATOM   2595  C  CA    . TYR A 1  357  ? 146.657 113.341 86.918  1.00 20.77  ? 357  TYR A CA    1 
ATOM   2596  C  C     . TYR A 1  357  ? 146.555 114.802 87.324  1.00 21.63  ? 357  TYR A C     1 
ATOM   2597  O  O     . TYR A 1  357  ? 145.608 115.471 86.910  1.00 26.80  ? 357  TYR A O     1 
ATOM   2598  C  CB    . TYR A 1  357  ? 145.498 112.547 87.544  1.00 22.45  ? 357  TYR A CB    1 
ATOM   2599  C  CG    . TYR A 1  357  ? 145.660 112.224 89.012  1.00 24.39  ? 357  TYR A CG    1 
ATOM   2600  C  CD1   . TYR A 1  357  ? 145.425 113.182 89.981  1.00 22.80  ? 357  TYR A CD1   1 
ATOM   2601  C  CD2   . TYR A 1  357  ? 146.032 110.958 89.429  1.00 25.03  ? 357  TYR A CD2   1 
ATOM   2602  C  CE1   . TYR A 1  357  ? 145.576 112.903 91.305  1.00 22.17  ? 357  TYR A CE1   1 
ATOM   2603  C  CE2   . TYR A 1  357  ? 146.178 110.667 90.764  1.00 21.84  ? 357  TYR A CE2   1 
ATOM   2604  C  CZ    . TYR A 1  357  ? 145.948 111.648 91.699  1.00 24.37  ? 357  TYR A CZ    1 
ATOM   2605  O  OH    . TYR A 1  357  ? 146.092 111.379 93.036  1.00 24.27  ? 357  TYR A OH    1 
ATOM   2606  N  N     . ASN A 1  358  ? 147.511 115.325 88.091  1.00 19.89  ? 358  ASN A N     1 
ATOM   2607  C  CA    . ASN A 1  358  ? 147.426 116.691 88.595  1.00 14.95  ? 358  ASN A CA    1 
ATOM   2608  C  C     . ASN A 1  358  ? 148.697 117.487 88.332  1.00 22.15  ? 358  ASN A C     1 
ATOM   2609  O  O     . ASN A 1  358  ? 148.860 118.572 88.887  1.00 31.07  ? 358  ASN A O     1 
ATOM   2610  C  CB    . ASN A 1  358  ? 147.123 116.696 90.091  1.00 16.50  ? 358  ASN A CB    1 
ATOM   2611  C  CG    . ASN A 1  358  ? 148.149 115.937 90.886  1.00 22.15  ? 358  ASN A CG    1 
ATOM   2612  O  OD1   . ASN A 1  358  ? 149.021 115.297 90.322  1.00 29.79  ? 358  ASN A OD1   1 
ATOM   2613  N  ND2   . ASN A 1  358  ? 148.057 116.006 92.203  1.00 19.12  ? 358  ASN A ND2   1 
ATOM   2614  N  N     . ILE A 1  359  ? 149.600 116.974 87.498  1.00 25.82  ? 359  ILE A N     1 
ATOM   2615  C  CA    . ILE A 1  359  ? 150.887 117.631 87.306  1.00 22.95  ? 359  ILE A CA    1 
ATOM   2616  C  C     . ILE A 1  359  ? 150.722 118.936 86.535  1.00 28.58  ? 359  ILE A C     1 
ATOM   2617  O  O     . ILE A 1  359  ? 151.350 119.945 86.867  1.00 31.78  ? 359  ILE A O     1 
ATOM   2618  C  CB    . ILE A 1  359  ? 151.874 116.671 86.617  1.00 22.10  ? 359  ILE A CB    1 
ATOM   2619  C  CG1   . ILE A 1  359  ? 153.204 117.361 86.339  1.00 22.03  ? 359  ILE A CG1   1 
ATOM   2620  C  CG2   . ILE A 1  359  ? 151.286 116.114 85.346  1.00 27.13  ? 359  ILE A CG2   1 
ATOM   2621  C  CD1   . ILE A 1  359  ? 153.914 117.821 87.566  1.00 25.01  ? 359  ILE A CD1   1 
ATOM   2622  N  N     . ASN A 1  360  ? 149.873 118.946 85.506  1.00 29.71  ? 360  ASN A N     1 
ATOM   2623  C  CA    . ASN A 1  360  ? 149.689 120.159 84.716  1.00 26.49  ? 360  ASN A CA    1 
ATOM   2624  C  C     . ASN A 1  360  ? 148.977 121.239 85.518  1.00 28.69  ? 360  ASN A C     1 
ATOM   2625  O  O     . ASN A 1  360  ? 149.195 122.432 85.293  1.00 32.71  ? 360  ASN A O     1 
ATOM   2626  C  CB    . ASN A 1  360  ? 148.903 119.854 83.443  1.00 29.28  ? 360  ASN A CB    1 
ATOM   2627  C  CG    . ASN A 1  360  ? 149.659 118.960 82.489  1.00 35.57  ? 360  ASN A CG    1 
ATOM   2628  O  OD1   . ASN A 1  360  ? 150.882 119.035 82.382  1.00 35.35  ? 360  ASN A OD1   1 
ATOM   2629  N  ND2   . ASN A 1  360  ? 148.930 118.126 81.764  1.00 36.01  ? 360  ASN A ND2   1 
ATOM   2630  N  N     . ARG A 1  361  ? 148.102 120.838 86.437  1.00 25.83  ? 361  ARG A N     1 
ATOM   2631  C  CA    . ARG A 1  361  ? 147.370 121.798 87.251  1.00 20.05  ? 361  ARG A CA    1 
ATOM   2632  C  C     . ARG A 1  361  ? 148.248 122.391 88.344  1.00 17.95  ? 361  ARG A C     1 
ATOM   2633  O  O     . ARG A 1  361  ? 148.066 123.552 88.716  1.00 22.48  ? 361  ARG A O     1 
ATOM   2634  C  CB    . ARG A 1  361  ? 146.138 121.121 87.847  1.00 19.15  ? 361  ARG A CB    1 
ATOM   2635  C  CG    . ARG A 1  361  ? 145.281 122.018 88.695  1.00 22.89  ? 361  ARG A CG    1 
ATOM   2636  C  CD    . ARG A 1  361  ? 144.041 121.314 89.190  1.00 20.11  ? 361  ARG A CD    1 
ATOM   2637  N  NE    . ARG A 1  361  ? 144.347 120.131 89.983  1.00 21.29  ? 361  ARG A NE    1 
ATOM   2638  C  CZ    . ARG A 1  361  ? 144.704 120.152 91.259  1.00 18.67  ? 361  ARG A CZ    1 
ATOM   2639  N  NH1   . ARG A 1  361  ? 144.854 121.287 91.914  1.00 20.74  ? 361  ARG A NH1   1 
ATOM   2640  N  NH2   . ARG A 1  361  ? 144.915 119.005 91.892  1.00 16.23  ? 361  ARG A NH2   1 
ATOM   2641  N  N     . LEU A 1  362  ? 149.199 121.620 88.864  1.00 15.10  ? 362  LEU A N     1 
ATOM   2642  C  CA    . LEU A 1  362  ? 150.088 122.092 89.916  1.00 15.83  ? 362  LEU A CA    1 
ATOM   2643  C  C     . LEU A 1  362  ? 151.290 122.858 89.387  1.00 22.83  ? 362  LEU A C     1 
ATOM   2644  O  O     . LEU A 1  362  ? 151.963 123.530 90.171  1.00 26.65  ? 362  LEU A O     1 
ATOM   2645  C  CB    . LEU A 1  362  ? 150.576 120.912 90.758  1.00 20.26  ? 362  LEU A CB    1 
ATOM   2646  C  CG    . LEU A 1  362  ? 149.543 120.188 91.624  1.00 20.82  ? 362  LEU A CG    1 
ATOM   2647  C  CD1   . LEU A 1  362  ? 150.191 119.042 92.366  1.00 16.77  ? 362  LEU A CD1   1 
ATOM   2648  C  CD2   . LEU A 1  362  ? 148.883 121.140 92.590  1.00 21.54  ? 362  LEU A CD2   1 
ATOM   2649  N  N     . MET A 1  363  ? 151.582 122.769 88.092  1.00 26.72  ? 363  MET A N     1 
ATOM   2650  C  CA    . MET A 1  363  ? 152.719 123.492 87.525  1.00 24.27  ? 363  MET A CA    1 
ATOM   2651  C  C     . MET A 1  363  ? 152.605 125.007 87.643  1.00 20.12  ? 363  MET A C     1 
ATOM   2652  O  O     . MET A 1  363  ? 153.618 125.651 87.962  1.00 17.64  ? 363  MET A O     1 
ATOM   2653  C  CB    . MET A 1  363  ? 152.929 123.050 86.074  1.00 26.59  ? 363  MET A CB    1 
ATOM   2654  C  CG    . MET A 1  363  ? 154.103 122.111 85.899  1.00 26.70  ? 363  MET A CG    1 
ATOM   2655  S  SD    . MET A 1  363  ? 155.558 122.792 86.703  1.00 43.38  ? 363  MET A SD    1 
ATOM   2656  C  CE    . MET A 1  363  ? 156.597 121.347 86.826  1.00 27.45  ? 363  MET A CE    1 
ATOM   2657  N  N     . PRO A 1  364  ? 151.456 125.643 87.379  1.00 17.70  ? 364  PRO A N     1 
ATOM   2658  C  CA    . PRO A 1  364  ? 151.382 127.101 87.574  1.00 17.19  ? 364  PRO A CA    1 
ATOM   2659  C  C     . PRO A 1  364  ? 151.709 127.567 88.983  1.00 18.34  ? 364  PRO A C     1 
ATOM   2660  O  O     . PRO A 1  364  ? 152.320 128.626 89.143  1.00 14.93  ? 364  PRO A O     1 
ATOM   2661  C  CB    . PRO A 1  364  ? 149.933 127.419 87.197  1.00 17.07  ? 364  PRO A CB    1 
ATOM   2662  C  CG    . PRO A 1  364  ? 149.566 126.365 86.252  1.00 16.43  ? 364  PRO A CG    1 
ATOM   2663  C  CD    . PRO A 1  364  ? 150.237 125.133 86.730  1.00 19.19  ? 364  PRO A CD    1 
ATOM   2664  N  N     . TYR A 1  365  ? 151.307 126.821 90.013  1.00 17.61  ? 365  TYR A N     1 
ATOM   2665  C  CA    . TYR A 1  365  ? 151.634 127.212 91.380  1.00 15.71  ? 365  TYR A CA    1 
ATOM   2666  C  C     . TYR A 1  365  ? 153.135 127.183 91.614  1.00 15.31  ? 365  TYR A C     1 
ATOM   2667  O  O     . TYR A 1  365  ? 153.691 128.080 92.254  1.00 17.13  ? 365  TYR A O     1 
ATOM   2668  C  CB    . TYR A 1  365  ? 150.947 126.283 92.378  1.00 13.80  ? 365  TYR A CB    1 
ATOM   2669  C  CG    . TYR A 1  365  ? 149.443 126.289 92.370  1.00 14.14  ? 365  TYR A CG    1 
ATOM   2670  C  CD1   . TYR A 1  365  ? 148.728 127.231 93.084  1.00 12.76  ? 365  TYR A CD1   1 
ATOM   2671  C  CD2   . TYR A 1  365  ? 148.738 125.329 91.676  1.00 14.14  ? 365  TYR A CD2   1 
ATOM   2672  C  CE1   . TYR A 1  365  ? 147.354 127.224 93.090  1.00 13.23  ? 365  TYR A CE1   1 
ATOM   2673  C  CE2   . TYR A 1  365  ? 147.371 125.316 91.675  1.00 13.80  ? 365  TYR A CE2   1 
ATOM   2674  C  CZ    . TYR A 1  365  ? 146.683 126.263 92.384  1.00 11.48  ? 365  TYR A CZ    1 
ATOM   2675  O  OH    . TYR A 1  365  ? 145.315 126.240 92.378  1.00 17.69  ? 365  TYR A OH    1 
ATOM   2676  N  N     . PHE A 1  366  ? 153.800 126.140 91.116  1.00 18.75  ? 366  PHE A N     1 
ATOM   2677  C  CA    . PHE A 1  366  ? 155.231 125.958 91.324  1.00 14.98  ? 366  PHE A CA    1 
ATOM   2678  C  C     . PHE A 1  366  ? 156.037 127.063 90.656  1.00 20.08  ? 366  PHE A C     1 
ATOM   2679  O  O     . PHE A 1  366  ? 157.019 127.554 91.222  1.00 23.31  ? 366  PHE A O     1 
ATOM   2680  C  CB    . PHE A 1  366  ? 155.637 124.584 90.791  1.00 17.29  ? 366  PHE A CB    1 
ATOM   2681  C  CG    . PHE A 1  366  ? 157.077 124.245 91.003  1.00 21.33  ? 366  PHE A CG    1 
ATOM   2682  C  CD1   . PHE A 1  366  ? 157.535 123.867 92.246  1.00 21.25  ? 366  PHE A CD1   1 
ATOM   2683  C  CD2   . PHE A 1  366  ? 157.969 124.292 89.956  1.00 18.62  ? 366  PHE A CD2   1 
ATOM   2684  C  CE1   . PHE A 1  366  ? 158.850 123.552 92.438  1.00 18.69  ? 366  PHE A CE1   1 
ATOM   2685  C  CE2   . PHE A 1  366  ? 159.285 123.983 90.149  1.00 21.36  ? 366  PHE A CE2   1 
ATOM   2686  C  CZ    . PHE A 1  366  ? 159.724 123.609 91.390  1.00 19.25  ? 366  PHE A CZ    1 
ATOM   2687  N  N     . LEU A 1  367  ? 155.633 127.470 89.454  1.00 19.59  ? 367  LEU A N     1 
ATOM   2688  C  CA    . LEU A 1  367  ? 156.354 128.516 88.743  1.00 17.38  ? 367  LEU A CA    1 
ATOM   2689  C  C     . LEU A 1  367  ? 156.203 129.874 89.415  1.00 20.75  ? 367  LEU A C     1 
ATOM   2690  O  O     . LEU A 1  367  ? 157.138 130.678 89.384  1.00 27.62  ? 367  LEU A O     1 
ATOM   2691  C  CB    . LEU A 1  367  ? 155.876 128.581 87.297  1.00 17.03  ? 367  LEU A CB    1 
ATOM   2692  C  CG    . LEU A 1  367  ? 156.137 127.318 86.480  1.00 20.74  ? 367  LEU A CG    1 
ATOM   2693  C  CD1   . LEU A 1  367  ? 155.698 127.508 85.052  1.00 18.66  ? 367  LEU A CD1   1 
ATOM   2694  C  CD2   . LEU A 1  367  ? 157.595 126.907 86.550  1.00 20.28  ? 367  LEU A CD2   1 
ATOM   2695  N  N     . ASN A 1  368  ? 155.041 130.157 90.007  1.00 18.63  ? 368  ASN A N     1 
ATOM   2696  C  CA    . ASN A 1  368  ? 154.846 131.442 90.672  1.00 15.48  ? 368  ASN A CA    1 
ATOM   2697  C  C     . ASN A 1  368  ? 155.726 131.570 91.905  1.00 14.93  ? 368  ASN A C     1 
ATOM   2698  O  O     . ASN A 1  368  ? 156.238 132.655 92.195  1.00 20.34  ? 368  ASN A O     1 
ATOM   2699  C  CB    . ASN A 1  368  ? 153.381 131.635 91.052  1.00 15.47  ? 368  ASN A CB    1 
ATOM   2700  C  CG    . ASN A 1  368  ? 152.541 132.126 89.903  1.00 18.72  ? 368  ASN A CG    1 
ATOM   2701  O  OD1   . ASN A 1  368  ? 153.047 132.730 88.968  1.00 24.92  ? 368  ASN A OD1   1 
ATOM   2702  N  ND2   . ASN A 1  368  ? 151.244 131.885 89.976  1.00 18.50  ? 368  ASN A ND2   1 
ATOM   2703  N  N     . GLY A 1  369  ? 155.907 130.483 92.647  1.00 13.68  ? 369  GLY A N     1 
ATOM   2704  C  CA    . GLY A 1  369  ? 156.731 130.541 93.839  1.00 14.49  ? 369  GLY A CA    1 
ATOM   2705  C  C     . GLY A 1  369  ? 156.101 131.421 94.894  1.00 15.39  ? 369  GLY A C     1 
ATOM   2706  O  O     . GLY A 1  369  ? 154.896 131.371 95.137  1.00 22.93  ? 369  GLY A O     1 
ATOM   2707  N  N     . LYS A 1  370  ? 156.923 132.242 95.538  1.00 21.78  ? 370  LYS A N     1 
ATOM   2708  C  CA    . LYS A 1  370  ? 156.452 133.156 96.566  1.00 19.60  ? 370  LYS A CA    1 
ATOM   2709  C  C     . LYS A 1  370  ? 156.355 134.593 96.072  1.00 25.32  ? 370  LYS A C     1 
ATOM   2710  O  O     . LYS A 1  370  ? 156.234 135.509 96.887  1.00 29.27  ? 370  LYS A O     1 
ATOM   2711  C  CB    . LYS A 1  370  ? 157.361 133.081 97.792  1.00 20.66  ? 370  LYS A CB    1 
ATOM   2712  C  CG    . LYS A 1  370  ? 157.124 131.857 98.642  1.00 21.10  ? 370  LYS A CG    1 
ATOM   2713  C  CD    . LYS A 1  370  ? 158.063 131.778 99.820  1.00 20.32  ? 370  LYS A CD    1 
ATOM   2714  C  CE    . LYS A 1  370  ? 157.376 132.169 101.107 1.00 27.06  ? 370  LYS A CE    1 
ATOM   2715  N  NZ    . LYS A 1  370  ? 157.056 133.617 101.182 1.00 29.79  ? 370  LYS A NZ    1 
ATOM   2716  N  N     . ARG A 1  371  ? 156.412 134.816 94.761  1.00 26.14  ? 371  ARG A N     1 
ATOM   2717  C  CA    . ARG A 1  371  ? 156.415 136.172 94.235  1.00 26.62  ? 371  ARG A CA    1 
ATOM   2718  C  C     . ARG A 1  371  ? 155.152 136.551 93.481  1.00 26.90  ? 371  ARG A C     1 
ATOM   2719  O  O     . ARG A 1  371  ? 154.861 137.738 93.367  1.00 34.76  ? 371  ARG A O     1 
ATOM   2720  C  CB    . ARG A 1  371  ? 157.630 136.399 93.322  1.00 25.78  ? 371  ARG A CB    1 
ATOM   2721  C  CG    . ARG A 1  371  ? 157.560 135.692 91.993  1.00 28.34  ? 371  ARG A CG    1 
ATOM   2722  C  CD    . ARG A 1  371  ? 158.934 135.501 91.389  1.00 25.56  ? 371  ARG A CD    1 
ATOM   2723  N  NE    . ARG A 1  371  ? 159.070 134.160 90.836  1.00 25.69  ? 371  ARG A NE    1 
ATOM   2724  C  CZ    . ARG A 1  371  ? 159.493 133.109 91.522  1.00 28.85  ? 371  ARG A CZ    1 
ATOM   2725  N  NH1   . ARG A 1  371  ? 159.879 133.216 92.781  1.00 29.92  ? 371  ARG A NH1   1 
ATOM   2726  N  NH2   . ARG A 1  371  ? 159.512 131.917 90.935  1.00 28.20  ? 371  ARG A NH2   1 
ATOM   2727  N  N     . GLN A 1  372  ? 154.399 135.592 92.968  1.00 20.57  ? 372  GLN A N     1 
ATOM   2728  C  CA    . GLN A 1  372  ? 153.098 135.857 92.377  1.00 19.68  ? 372  GLN A CA    1 
ATOM   2729  C  C     . GLN A 1  372  ? 152.062 134.951 93.018  1.00 20.13  ? 372  GLN A C     1 
ATOM   2730  O  O     . GLN A 1  372  ? 152.388 133.857 93.479  1.00 23.11  ? 372  GLN A O     1 
ATOM   2731  C  CB    . GLN A 1  372  ? 153.110 135.647 90.866  1.00 20.44  ? 372  GLN A CB    1 
ATOM   2732  C  CG    . GLN A 1  372  ? 152.172 136.566 90.119  1.00 23.24  ? 372  GLN A CG    1 
ATOM   2733  C  CD    . GLN A 1  372  ? 151.817 136.047 88.746  1.00 29.17  ? 372  GLN A CD    1 
ATOM   2734  O  OE1   . GLN A 1  372  ? 150.645 135.856 88.423  1.00 25.07  ? 372  GLN A OE1   1 
ATOM   2735  N  NE2   . GLN A 1  372  ? 152.832 135.819 87.923  1.00 26.55  ? 372  GLN A NE2   1 
ATOM   2736  N  N     . TYR A 1  373  ? 150.822 135.419 93.063  1.00 14.92  ? 373  TYR A N     1 
ATOM   2737  C  CA    . TYR A 1  373  ? 149.687 134.682 93.592  1.00 10.69  ? 373  TYR A CA    1 
ATOM   2738  C  C     . TYR A 1  373  ? 148.840 134.138 92.454  1.00 9.94   ? 373  TYR A C     1 
ATOM   2739  O  O     . TYR A 1  373  ? 148.600 134.843 91.474  1.00 9.74   ? 373  TYR A O     1 
ATOM   2740  C  CB    . TYR A 1  373  ? 148.824 135.573 94.492  1.00 6.44   ? 373  TYR A CB    1 
ATOM   2741  C  CG    . TYR A 1  373  ? 147.545 134.919 94.960  1.00 12.40  ? 373  TYR A CG    1 
ATOM   2742  C  CD1   . TYR A 1  373  ? 147.512 134.155 96.114  1.00 12.97  ? 373  TYR A CD1   1 
ATOM   2743  C  CD2   . TYR A 1  373  ? 146.368 135.057 94.240  1.00 13.26  ? 373  TYR A CD2   1 
ATOM   2744  C  CE1   . TYR A 1  373  ? 146.348 133.549 96.526  1.00 4.43   ? 373  TYR A CE1   1 
ATOM   2745  C  CE2   . TYR A 1  373  ? 145.216 134.454 94.643  1.00 8.13   ? 373  TYR A CE2   1 
ATOM   2746  C  CZ    . TYR A 1  373  ? 145.207 133.707 95.780  1.00 5.21   ? 373  TYR A CZ    1 
ATOM   2747  O  OH    . TYR A 1  373  ? 144.038 133.121 96.164  1.00 6.31   ? 373  TYR A OH    1 
ATOM   2748  N  N     . PRO A 1  374  ? 148.348 132.897 92.543  1.00 15.23  ? 374  PRO A N     1 
ATOM   2749  C  CA    . PRO A 1  374  ? 148.571 131.911 93.610  1.00 9.78   ? 374  PRO A CA    1 
ATOM   2750  C  C     . PRO A 1  374  ? 149.853 131.107 93.432  1.00 9.49   ? 374  PRO A C     1 
ATOM   2751  O  O     . PRO A 1  374  ? 150.164 130.648 92.347  1.00 16.05  ? 374  PRO A O     1 
ATOM   2752  C  CB    . PRO A 1  374  ? 147.315 131.040 93.521  1.00 8.35   ? 374  PRO A CB    1 
ATOM   2753  C  CG    . PRO A 1  374  ? 146.930 131.092 92.092  1.00 6.98   ? 374  PRO A CG    1 
ATOM   2754  C  CD    . PRO A 1  374  ? 147.290 132.466 91.616  1.00 11.08  ? 374  PRO A CD    1 
ATOM   2755  N  N     . GLY A 1  375  ? 150.610 130.914 94.504  1.00 11.55  ? 375  GLY A N     1 
ATOM   2756  C  CA    . GLY A 1  375  ? 151.908 130.280 94.423  1.00 5.89   ? 375  GLY A CA    1 
ATOM   2757  C  C     . GLY A 1  375  ? 152.110 129.169 95.426  1.00 8.76   ? 375  GLY A C     1 
ATOM   2758  O  O     . GLY A 1  375  ? 151.186 128.408 95.701  1.00 17.68  ? 375  GLY A O     1 
ATOM   2759  N  N     . CYS A 1  376  ? 153.309 129.061 95.982  1.00 5.91   ? 376  CYS A N     1 
ATOM   2760  C  CA    . CYS A 1  376  ? 153.647 127.936 96.840  1.00 7.62   ? 376  CYS A CA    1 
ATOM   2761  C  C     . CYS A 1  376  ? 154.795 128.339 97.747  1.00 14.62  ? 376  CYS A C     1 
ATOM   2762  O  O     . CYS A 1  376  ? 155.417 129.382 97.565  1.00 24.87  ? 376  CYS A O     1 
ATOM   2763  C  CB    . CYS A 1  376  ? 154.001 126.692 96.021  1.00 7.80   ? 376  CYS A CB    1 
ATOM   2764  S  SG    . CYS A 1  376  ? 155.392 126.872 94.922  1.00 31.93  ? 376  CYS A SG    1 
ATOM   2765  N  N     . SER A 1  377  ? 155.061 127.511 98.727  1.00 15.19  ? 377  SER A N     1 
ATOM   2766  C  CA    . SER A 1  377  ? 156.101 127.837 99.693  1.00 19.35  ? 377  SER A CA    1 
ATOM   2767  C  C     . SER A 1  377  ? 157.143 126.743 99.856  1.00 21.42  ? 377  SER A C     1 
ATOM   2768  O  O     . SER A 1  377  ? 158.320 127.052 100.029 1.00 26.87  ? 377  SER A O     1 
ATOM   2769  C  CB    . SER A 1  377  ? 155.462 128.151 101.051 1.00 15.83  ? 377  SER A CB    1 
ATOM   2770  O  OG    . SER A 1  377  ? 154.677 127.065 101.503 1.00 16.73  ? 377  SER A OG    1 
ATOM   2771  N  N     . ARG A 1  378  ? 156.747 125.477 99.809  1.00 14.68  ? 378  ARG A N     1 
ATOM   2772  C  CA    . ARG A 1  378  ? 157.668 124.392 100.095 1.00 14.80  ? 378  ARG A CA    1 
ATOM   2773  C  C     . ARG A 1  378  ? 157.367 123.217 99.184  1.00 19.61  ? 378  ARG A C     1 
ATOM   2774  O  O     . ARG A 1  378  ? 156.258 123.070 98.673  1.00 17.62  ? 378  ARG A O     1 
ATOM   2775  C  CB    . ARG A 1  378  ? 157.586 123.940 101.555 1.00 13.58  ? 378  ARG A CB    1 
ATOM   2776  C  CG    . ARG A 1  378  ? 157.968 124.981 102.571 1.00 16.15  ? 378  ARG A CG    1 
ATOM   2777  C  CD    . ARG A 1  378  ? 157.856 124.424 103.969 1.00 20.58  ? 378  ARG A CD    1 
ATOM   2778  N  NE    . ARG A 1  378  ? 156.558 123.800 104.189 1.00 25.43  ? 378  ARG A NE    1 
ATOM   2779  C  CZ    . ARG A 1  378  ? 156.287 122.941 105.162 1.00 22.66  ? 378  ARG A CZ    1 
ATOM   2780  N  NH1   . ARG A 1  378  ? 157.205 122.580 106.041 1.00 21.55  ? 378  ARG A NH1   1 
ATOM   2781  N  NH2   . ARG A 1  378  ? 155.063 122.435 105.257 1.00 19.81  ? 378  ARG A NH2   1 
ATOM   2782  N  N     . VAL A 1  379  ? 158.383 122.384 98.982  1.00 21.18  ? 379  VAL A N     1 
ATOM   2783  C  CA    . VAL A 1  379  ? 158.234 121.097 98.320  1.00 18.67  ? 379  VAL A CA    1 
ATOM   2784  C  C     . VAL A 1  379  ? 158.902 120.050 99.194  1.00 21.06  ? 379  VAL A C     1 
ATOM   2785  O  O     . VAL A 1  379  ? 160.007 120.269 99.694  1.00 26.41  ? 379  VAL A O     1 
ATOM   2786  C  CB    . VAL A 1  379  ? 158.851 121.080 96.911  1.00 19.29  ? 379  VAL A CB    1 
ATOM   2787  C  CG1   . VAL A 1  379  ? 158.696 119.715 96.299  1.00 19.08  ? 379  VAL A CG1   1 
ATOM   2788  C  CG2   . VAL A 1  379  ? 158.216 122.116 96.033  1.00 19.88  ? 379  VAL A CG2   1 
ATOM   2789  N  N     . TYR A 1  380  ? 158.233 118.927 99.387  1.00 25.83  ? 380  TYR A N     1 
ATOM   2790  C  CA    . TYR A 1  380  ? 158.811 117.775 100.059 1.00 22.11  ? 380  TYR A CA    1 
ATOM   2791  C  C     . TYR A 1  380  ? 159.236 116.787 98.983  1.00 26.50  ? 380  TYR A C     1 
ATOM   2792  O  O     . TYR A 1  380  ? 158.420 116.379 98.156  1.00 32.76  ? 380  TYR A O     1 
ATOM   2793  C  CB    . TYR A 1  380  ? 157.810 117.148 101.025 1.00 23.73  ? 380  TYR A CB    1 
ATOM   2794  C  CG    . TYR A 1  380  ? 158.237 115.809 101.574 1.00 27.66  ? 380  TYR A CG    1 
ATOM   2795  C  CD1   . TYR A 1  380  ? 158.931 115.719 102.767 1.00 24.25  ? 380  TYR A CD1   1 
ATOM   2796  C  CD2   . TYR A 1  380  ? 157.939 114.635 100.898 1.00 24.96  ? 380  TYR A CD2   1 
ATOM   2797  C  CE1   . TYR A 1  380  ? 159.318 114.507 103.263 1.00 24.14  ? 380  TYR A CE1   1 
ATOM   2798  C  CE2   . TYR A 1  380  ? 158.326 113.425 101.384 1.00 25.06  ? 380  TYR A CE2   1 
ATOM   2799  C  CZ    . TYR A 1  380  ? 159.013 113.361 102.567 1.00 30.66  ? 380  TYR A CZ    1 
ATOM   2800  O  OH    . TYR A 1  380  ? 159.395 112.137 103.058 1.00 34.70  ? 380  TYR A OH    1 
ATOM   2801  N  N     . LYS A 1  381  ? 160.510 116.413 98.986  1.00 29.72  ? 381  LYS A N     1 
ATOM   2802  C  CA    . LYS A 1  381  ? 161.019 115.456 98.016  1.00 29.18  ? 381  LYS A CA    1 
ATOM   2803  C  C     . LYS A 1  381  ? 161.037 114.060 98.621  1.00 29.55  ? 381  LYS A C     1 
ATOM   2804  O  O     . LYS A 1  381  ? 161.671 113.833 99.654  1.00 29.03  ? 381  LYS A O     1 
ATOM   2805  C  CB    . LYS A 1  381  ? 162.418 115.853 97.558  1.00 31.60  ? 381  LYS A CB    1 
ATOM   2806  C  CG    . LYS A 1  381  ? 162.438 116.685 96.292  1.00 33.95  ? 381  LYS A CG    1 
ATOM   2807  C  CD    . LYS A 1  381  ? 162.907 115.847 95.113  1.00 33.67  ? 381  LYS A CD    1 
ATOM   2808  C  CE    . LYS A 1  381  ? 162.851 116.617 93.806  1.00 31.65  ? 381  LYS A CE    1 
ATOM   2809  N  NZ    . LYS A 1  381  ? 161.464 116.851 93.338  1.00 31.19  ? 381  LYS A NZ    1 
ATOM   2810  N  N     . GLN A 1  382  ? 160.335 113.124 97.981  1.00 27.43  ? 382  GLN A N     1 
ATOM   2811  C  CA    . GLN A 1  382  ? 160.206 111.787 98.546  1.00 31.62  ? 382  GLN A CA    1 
ATOM   2812  C  C     . GLN A 1  382  ? 161.432 110.924 98.293  1.00 38.37  ? 382  GLN A C     1 
ATOM   2813  O  O     . GLN A 1  382  ? 161.566 109.864 98.911  1.00 39.02  ? 382  GLN A O     1 
ATOM   2814  C  CB    . GLN A 1  382  ? 158.952 111.100 97.998  1.00 30.27  ? 382  GLN A CB    1 
ATOM   2815  C  CG    . GLN A 1  382  ? 159.179 110.126 96.855  1.00 31.06  ? 382  GLN A CG    1 
ATOM   2816  C  CD    . GLN A 1  382  ? 159.480 110.810 95.531  1.00 37.65  ? 382  GLN A CD    1 
ATOM   2817  O  OE1   . GLN A 1  382  ? 160.353 111.671 95.441  1.00 38.62  ? 382  GLN A OE1   1 
ATOM   2818  N  NE2   . GLN A 1  382  ? 158.743 110.432 94.497  1.00 33.60  ? 382  GLN A NE2   1 
ATOM   2819  N  N     . ILE A 1  383  ? 162.326 111.348 97.402  1.00 36.88  ? 383  ILE A N     1 
ATOM   2820  C  CA    . ILE A 1  383  ? 163.565 110.615 97.193  1.00 34.28  ? 383  ILE A CA    1 
ATOM   2821  C  C     . ILE A 1  383  ? 164.630 111.007 98.207  1.00 33.08  ? 383  ILE A C     1 
ATOM   2822  O  O     . ILE A 1  383  ? 165.635 110.302 98.346  1.00 37.54  ? 383  ILE A O     1 
ATOM   2823  C  CB    . ILE A 1  383  ? 164.072 110.830 95.759  1.00 35.42  ? 383  ILE A CB    1 
ATOM   2824  C  CG1   . ILE A 1  383  ? 164.941 109.654 95.325  1.00 38.29  ? 383  ILE A CG1   1 
ATOM   2825  C  CG2   . ILE A 1  383  ? 164.830 112.133 95.649  1.00 38.01  ? 383  ILE A CG2   1 
ATOM   2826  C  CD1   . ILE A 1  383  ? 164.200 108.341 95.293  1.00 37.47  ? 383  ILE A CD1   1 
ATOM   2827  N  N     . THR A 1  384  ? 164.432 112.104 98.932  1.00 32.97  ? 384  THR A N     1 
ATOM   2828  C  CA    . THR A 1  384  ? 165.394 112.583 99.910  1.00 32.11  ? 384  THR A CA    1 
ATOM   2829  C  C     . THR A 1  384  ? 164.791 112.753 101.299 1.00 34.60  ? 384  THR A C     1 
ATOM   2830  O  O     . THR A 1  384  ? 165.542 112.812 102.279 1.00 33.24  ? 384  THR A O     1 
ATOM   2831  C  CB    . THR A 1  384  ? 165.990 113.911 99.426  1.00 35.01  ? 384  THR A CB    1 
ATOM   2832  O  OG1   . THR A 1  384  ? 166.505 113.737 98.101  1.00 37.51  ? 384  THR A OG1   1 
ATOM   2833  C  CG2   . THR A 1  384  ? 167.131 114.363 100.323 1.00 34.87  ? 384  THR A CG2   1 
ATOM   2834  N  N     . GLN A 1  385  ? 163.461 112.800 101.410 1.00 33.28  ? 385  GLN A N     1 
ATOM   2835  C  CA    . GLN A 1  385  ? 162.751 112.977 102.678 1.00 29.46  ? 385  GLN A CA    1 
ATOM   2836  C  C     . GLN A 1  385  ? 163.098 114.319 103.322 1.00 31.88  ? 385  GLN A C     1 
ATOM   2837  O  O     . GLN A 1  385  ? 163.258 114.439 104.537 1.00 31.69  ? 385  GLN A O     1 
ATOM   2838  C  CB    . GLN A 1  385  ? 163.036 111.820 103.642 1.00 32.13  ? 385  GLN A CB    1 
ATOM   2839  C  CG    . GLN A 1  385  ? 162.130 110.610 103.503 1.00 32.34  ? 385  GLN A CG    1 
ATOM   2840  C  CD    . GLN A 1  385  ? 162.340 109.830 102.220 1.00 33.66  ? 385  GLN A CD    1 
ATOM   2841  O  OE1   . GLN A 1  385  ? 162.819 110.358 101.220 1.00 33.06  ? 385  GLN A OE1   1 
ATOM   2842  N  NE2   . GLN A 1  385  ? 161.971 108.559 102.246 1.00 33.85  ? 385  GLN A NE2   1 
ATOM   2843  N  N     . SER A 1  386  ? 163.188 115.342 102.480 1.00 31.54  ? 386  SER A N     1 
ATOM   2844  C  CA    . SER A 1  386  ? 163.576 116.658 102.953 1.00 31.61  ? 386  SER A CA    1 
ATOM   2845  C  C     . SER A 1  386  ? 162.657 117.704 102.347 1.00 31.49  ? 386  SER A C     1 
ATOM   2846  O  O     . SER A 1  386  ? 162.097 117.520 101.266 1.00 31.67  ? 386  SER A O     1 
ATOM   2847  C  CB    . SER A 1  386  ? 165.041 116.951 102.625 1.00 32.23  ? 386  SER A CB    1 
ATOM   2848  O  OG    . SER A 1  386  ? 165.232 117.093 101.235 1.00 35.53  ? 386  SER A OG    1 
ATOM   2849  N  N     . VAL A 1  387  ? 162.506 118.809 103.071 1.00 31.90  ? 387  VAL A N     1 
ATOM   2850  C  CA    . VAL A 1  387  ? 161.647 119.914 102.673 1.00 30.90  ? 387  VAL A CA    1 
ATOM   2851  C  C     . VAL A 1  387  ? 162.535 121.082 102.281 1.00 31.88  ? 387  VAL A C     1 
ATOM   2852  O  O     . VAL A 1  387  ? 163.442 121.458 103.031 1.00 34.36  ? 387  VAL A O     1 
ATOM   2853  C  CB    . VAL A 1  387  ? 160.680 120.311 103.801 1.00 28.00  ? 387  VAL A CB    1 
ATOM   2854  C  CG1   . VAL A 1  387  ? 159.498 121.056 103.238 1.00 29.82  ? 387  VAL A CG1   1 
ATOM   2855  C  CG2   . VAL A 1  387  ? 160.216 119.088 104.551 1.00 30.22  ? 387  VAL A CG2   1 
ATOM   2856  N  N     . HIS A 1  388  ? 162.285 121.645 101.105 1.00 29.76  ? 388  HIS A N     1 
ATOM   2857  C  CA    . HIS A 1  388  ? 163.036 122.783 100.598 1.00 30.38  ? 388  HIS A CA    1 
ATOM   2858  C  C     . HIS A 1  388  ? 162.097 123.953 100.362 1.00 33.28  ? 388  HIS A C     1 
ATOM   2859  O  O     . HIS A 1  388  ? 161.011 123.778 99.803  1.00 35.28  ? 388  HIS A O     1 
ATOM   2860  C  CB    . HIS A 1  388  ? 163.760 122.434 99.298  1.00 31.66  ? 388  HIS A CB    1 
ATOM   2861  C  CG    . HIS A 1  388  ? 164.539 121.158 99.359  1.00 36.56  ? 388  HIS A CG    1 
ATOM   2862  N  ND1   . HIS A 1  388  ? 164.106 119.995 98.764  1.00 39.09  ? 388  HIS A ND1   1 
ATOM   2863  C  CD2   . HIS A 1  388  ? 165.719 120.861 99.951  1.00 33.03  ? 388  HIS A CD2   1 
ATOM   2864  C  CE1   . HIS A 1  388  ? 164.989 119.039 98.978  1.00 34.76  ? 388  HIS A CE1   1 
ATOM   2865  N  NE2   . HIS A 1  388  ? 165.975 119.536 99.700  1.00 34.26  ? 388  HIS A NE2   1 
ATOM   2866  N  N     . ASP A 1  389  ? 162.518 125.142 100.783 1.00 32.28  ? 389  ASP A N     1 
ATOM   2867  C  CA    . ASP A 1  389  ? 161.781 126.350 100.452 1.00 29.71  ? 389  ASP A CA    1 
ATOM   2868  C  C     . ASP A 1  389  ? 161.857 126.616 98.956  1.00 34.29  ? 389  ASP A C     1 
ATOM   2869  O  O     . ASP A 1  389  ? 162.794 126.201 98.275  1.00 37.06  ? 389  ASP A O     1 
ATOM   2870  C  CB    . ASP A 1  389  ? 162.328 127.544 101.228 1.00 34.65  ? 389  ASP A CB    1 
ATOM   2871  C  CG    . ASP A 1  389  ? 162.363 127.299 102.723 1.00 41.91  ? 389  ASP A CG    1 
ATOM   2872  O  OD1   . ASP A 1  389  ? 161.959 126.202 103.154 1.00 39.21  ? 389  ASP A OD1   1 
ATOM   2873  O  OD2   . ASP A 1  389  ? 162.792 128.203 103.470 1.00 39.67  ? 389  ASP A OD2   1 
ATOM   2874  N  N     . ILE A 1  390  ? 160.845 127.309 98.442  1.00 31.17  ? 390  ILE A N     1 
ATOM   2875  C  CA    . ILE A 1  390  ? 160.731 127.491 97.002  1.00 27.75  ? 390  ILE A CA    1 
ATOM   2876  C  C     . ILE A 1  390  ? 161.678 128.567 96.488  1.00 32.32  ? 390  ILE A C     1 
ATOM   2877  O  O     . ILE A 1  390  ? 162.079 128.533 95.321  1.00 36.21  ? 390  ILE A O     1 
ATOM   2878  C  CB    . ILE A 1  390  ? 159.272 127.795 96.628  1.00 25.87  ? 390  ILE A CB    1 
ATOM   2879  C  CG1   . ILE A 1  390  ? 159.008 127.404 95.180  1.00 26.18  ? 390  ILE A CG1   1 
ATOM   2880  C  CG2   . ILE A 1  390  ? 158.937 129.244 96.862  1.00 27.32  ? 390  ILE A CG2   1 
ATOM   2881  C  CD1   . ILE A 1  390  ? 158.892 125.932 94.993  1.00 26.56  ? 390  ILE A CD1   1 
ATOM   2882  N  N     . GLU A 1  391  ? 162.048 129.539 97.318  1.00 33.27  ? 391  GLU A N     1 
ATOM   2883  C  CA    . GLU A 1  391  ? 162.941 130.593 96.859  1.00 31.89  ? 391  GLU A CA    1 
ATOM   2884  C  C     . GLU A 1  391  ? 164.401 130.179 96.991  1.00 34.46  ? 391  GLU A C     1 
ATOM   2885  O  O     . GLU A 1  391  ? 165.164 130.259 96.025  1.00 38.03  ? 391  GLU A O     1 
ATOM   2886  C  CB    . GLU A 1  391  ? 162.667 131.883 97.632  1.00 33.76  ? 391  GLU A CB    1 
ATOM   2887  C  CG    . GLU A 1  391  ? 161.413 132.627 97.181  1.00 35.05  ? 391  GLU A CG    1 
ATOM   2888  C  CD    . GLU A 1  391  ? 161.342 132.825 95.675  1.00 37.55  ? 391  GLU A CD    1 
ATOM   2889  O  OE1   . GLU A 1  391  ? 162.341 133.291 95.089  1.00 34.58  ? 391  GLU A OE1   1 
ATOM   2890  O  OE2   . GLU A 1  391  ? 160.289 132.516 95.077  1.00 32.42  ? 391  GLU A OE2   1 
ATOM   2891  N  N     . GLY A 1  392  ? 164.797 129.717 98.171  1.00 34.76  ? 392  GLY A N     1 
ATOM   2892  C  CA    . GLY A 1  392  ? 166.097 129.103 98.333  1.00 37.15  ? 392  GLY A CA    1 
ATOM   2893  C  C     . GLY A 1  392  ? 166.088 127.680 97.816  1.00 39.78  ? 392  GLY A C     1 
ATOM   2894  O  O     . GLY A 1  392  ? 166.143 126.728 98.601  1.00 39.01  ? 392  GLY A O     1 
ATOM   2895  N  N     . LEU A 1  393  ? 165.991 127.520 96.498  1.00 38.60  ? 393  LEU A N     1 
ATOM   2896  C  CA    . LEU A 1  393  ? 165.866 126.208 95.884  1.00 42.84  ? 393  LEU A CA    1 
ATOM   2897  C  C     . LEU A 1  393  ? 166.765 126.108 94.659  1.00 44.04  ? 393  LEU A C     1 
ATOM   2898  O  O     . LEU A 1  393  ? 167.044 127.102 93.984  1.00 44.05  ? 393  LEU A O     1 
ATOM   2899  C  CB    . LEU A 1  393  ? 164.407 125.923 95.501  1.00 40.44  ? 393  LEU A CB    1 
ATOM   2900  C  CG    . LEU A 1  393  ? 164.039 124.651 94.744  1.00 38.79  ? 393  LEU A CG    1 
ATOM   2901  C  CD1   . LEU A 1  393  ? 163.511 123.611 95.703  1.00 38.23  ? 393  LEU A CD1   1 
ATOM   2902  C  CD2   . LEU A 1  393  ? 163.007 124.973 93.681  1.00 39.02  ? 393  LEU A CD2   1 
ATOM   2903  N  N     . LYS A 1  394  ? 167.204 124.881 94.376  1.00 47.11  ? 394  LYS A N     1 
ATOM   2904  C  CA    . LYS A 1  394  ? 168.066 124.601 93.238  1.00 46.91  ? 394  LYS A CA    1 
ATOM   2905  C  C     . LYS A 1  394  ? 167.414 125.078 91.940  1.00 46.79  ? 394  LYS A C     1 
ATOM   2906  O  O     . LYS A 1  394  ? 166.199 125.266 91.849  1.00 46.50  ? 394  LYS A O     1 
ATOM   2907  C  CB    . LYS A 1  394  ? 168.349 123.101 93.136  1.00 47.22  ? 394  LYS A CB    1 
ATOM   2908  C  CG    . LYS A 1  394  ? 168.807 122.422 94.418  1.00 48.08  ? 394  LYS A CG    1 
ATOM   2909  C  CD    . LYS A 1  394  ? 170.329 122.433 94.582  1.00 46.69  ? 394  LYS A CD    1 
ATOM   2910  C  CE    . LYS A 1  394  ? 170.768 123.393 95.671  1.00 44.02  ? 394  LYS A CE    1 
ATOM   2911  N  NZ    . LYS A 1  394  ? 172.237 123.341 95.877  1.00 44.76  ? 394  LYS A NZ    1 
ATOM   2912  N  N     . GLN A 1  395  ? 168.245 125.269 90.916  1.00 48.71  ? 395  GLN A N     1 
ATOM   2913  C  CA    . GLN A 1  395  ? 167.735 125.609 89.596  1.00 49.86  ? 395  GLN A CA    1 
ATOM   2914  C  C     . GLN A 1  395  ? 167.500 124.389 88.720  1.00 50.46  ? 395  GLN A C     1 
ATOM   2915  O  O     . GLN A 1  395  ? 166.764 124.488 87.733  1.00 49.10  ? 395  GLN A O     1 
ATOM   2916  C  CB    . GLN A 1  395  ? 168.695 126.565 88.876  1.00 47.73  ? 395  GLN A CB    1 
ATOM   2917  C  CG    . GLN A 1  395  ? 168.849 127.914 89.555  1.00 50.13  ? 395  GLN A CG    1 
ATOM   2918  C  CD    . GLN A 1  395  ? 169.952 127.915 90.599  1.00 49.33  ? 395  GLN A CD    1 
ATOM   2919  O  OE1   . GLN A 1  395  ? 170.832 127.055 90.587  1.00 49.17  ? 395  GLN A OE1   1 
ATOM   2920  N  NE2   . GLN A 1  395  ? 169.902 128.877 91.515  1.00 47.17  ? 395  GLN A NE2   1 
ATOM   2921  N  N     . ASP A 1  396  ? 168.098 123.248 89.060  1.00 50.55  ? 396  ASP A N     1 
ATOM   2922  C  CA    . ASP A 1  396  ? 167.890 121.993 88.342  1.00 48.34  ? 396  ASP A CA    1 
ATOM   2923  C  C     . ASP A 1  396  ? 166.845 121.124 89.029  1.00 49.77  ? 396  ASP A C     1 
ATOM   2924  O  O     . ASP A 1  396  ? 166.873 119.896 88.926  1.00 52.90  ? 396  ASP A O     1 
ATOM   2925  C  CB    . ASP A 1  396  ? 169.210 121.241 88.199  1.00 49.20  ? 396  ASP A CB    1 
ATOM   2926  C  CG    . ASP A 1  396  ? 169.848 120.905 89.541  1.00 51.40  ? 396  ASP A CG    1 
ATOM   2927  O  OD1   . ASP A 1  396  ? 169.312 121.315 90.591  1.00 49.85  ? 396  ASP A OD1   1 
ATOM   2928  O  OD2   . ASP A 1  396  ? 170.901 120.235 89.544  1.00 52.53  ? 396  ASP A OD2   1 
ATOM   2929  N  N     . PHE A 1  397  ? 165.915 121.754 89.738  1.00 42.27  ? 397  PHE A N     1 
ATOM   2930  C  CA    . PHE A 1  397  ? 164.888 121.078 90.516  1.00 38.51  ? 397  PHE A CA    1 
ATOM   2931  C  C     . PHE A 1  397  ? 163.679 120.773 89.642  1.00 39.17  ? 397  PHE A C     1 
ATOM   2932  O  O     . PHE A 1  397  ? 163.361 121.528 88.720  1.00 40.48  ? 397  PHE A O     1 
ATOM   2933  C  CB    . PHE A 1  397  ? 164.475 121.951 91.701  1.00 38.21  ? 397  PHE A CB    1 
ATOM   2934  C  CG    . PHE A 1  397  ? 163.758 121.216 92.787  1.00 38.14  ? 397  PHE A CG    1 
ATOM   2935  C  CD1   . PHE A 1  397  ? 162.386 121.065 92.747  1.00 36.02  ? 397  PHE A CD1   1 
ATOM   2936  C  CD2   . PHE A 1  397  ? 164.450 120.701 93.860  1.00 40.13  ? 397  PHE A CD2   1 
ATOM   2937  C  CE1   . PHE A 1  397  ? 161.725 120.402 93.743  1.00 35.99  ? 397  PHE A CE1   1 
ATOM   2938  C  CE2   . PHE A 1  397  ? 163.793 120.037 94.864  1.00 38.87  ? 397  PHE A CE2   1 
ATOM   2939  C  CZ    . PHE A 1  397  ? 162.428 119.890 94.805  1.00 39.68  ? 397  PHE A CZ    1 
ATOM   2940  N  N     . ARG A 1  398  ? 163.013 119.660 89.934  1.00 37.88  ? 398  ARG A N     1 
ATOM   2941  C  CA    . ARG A 1  398  ? 161.833 119.250 89.191  1.00 36.34  ? 398  ARG A CA    1 
ATOM   2942  C  C     . ARG A 1  398  ? 160.816 118.628 90.136  1.00 39.42  ? 398  ARG A C     1 
ATOM   2943  O  O     . ARG A 1  398  ? 161.159 118.109 91.200  1.00 40.15  ? 398  ARG A O     1 
ATOM   2944  C  CB    . ARG A 1  398  ? 162.180 118.255 88.081  1.00 35.67  ? 398  ARG A CB    1 
ATOM   2945  C  CG    . ARG A 1  398  ? 162.341 118.882 86.719  1.00 37.70  ? 398  ARG A CG    1 
ATOM   2946  C  CD    . ARG A 1  398  ? 161.970 117.901 85.629  1.00 39.45  ? 398  ARG A CD    1 
ATOM   2947  N  NE    . ARG A 1  398  ? 162.325 116.534 85.988  1.00 42.40  ? 398  ARG A NE    1 
ATOM   2948  C  CZ    . ARG A 1  398  ? 161.680 115.456 85.566  1.00 41.97  ? 398  ARG A CZ    1 
ATOM   2949  N  NH1   . ARG A 1  398  ? 160.636 115.547 84.757  1.00 36.72  ? 398  ARG A NH1   1 
ATOM   2950  N  NH2   . ARG A 1  398  ? 162.097 114.255 85.959  1.00 38.74  ? 398  ARG A NH2   1 
ATOM   2951  N  N     . LEU A 1  399  ? 159.553 118.677 89.722  1.00 32.77  ? 399  LEU A N     1 
ATOM   2952  C  CA    . LEU A 1  399  ? 158.467 118.037 90.453  1.00 26.39  ? 399  LEU A CA    1 
ATOM   2953  C  C     . LEU A 1  399  ? 158.387 116.586 90.007  1.00 28.08  ? 399  LEU A C     1 
ATOM   2954  O  O     . LEU A 1  399  ? 158.050 116.299 88.855  1.00 31.70  ? 399  LEU A O     1 
ATOM   2955  C  CB    . LEU A 1  399  ? 157.141 118.747 90.207  1.00 27.84  ? 399  LEU A CB    1 
ATOM   2956  C  CG    . LEU A 1  399  ? 156.799 120.010 90.986  1.00 26.49  ? 399  LEU A CG    1 
ATOM   2957  C  CD1   . LEU A 1  399  ? 155.353 120.358 90.717  1.00 24.00  ? 399  LEU A CD1   1 
ATOM   2958  C  CD2   . LEU A 1  399  ? 157.056 119.844 92.459  1.00 28.11  ? 399  LEU A CD2   1 
ATOM   2959  N  N     . GLU A 1  400  ? 158.698 115.674 90.915  1.00 31.04  ? 400  GLU A N     1 
ATOM   2960  C  CA    . GLU A 1  400  ? 158.624 114.253 90.636  1.00 33.03  ? 400  GLU A CA    1 
ATOM   2961  C  C     . GLU A 1  400  ? 157.369 113.664 91.257  1.00 30.27  ? 400  GLU A C     1 
ATOM   2962  O  O     . GLU A 1  400  ? 156.873 114.146 92.275  1.00 31.00  ? 400  GLU A O     1 
ATOM   2963  C  CB    . GLU A 1  400  ? 159.856 113.532 91.179  1.00 31.89  ? 400  GLU A CB    1 
ATOM   2964  C  CG    . GLU A 1  400  ? 161.169 114.167 90.790  1.00 32.47  ? 400  GLU A CG    1 
ATOM   2965  C  CD    . GLU A 1  400  ? 161.639 113.723 89.426  1.00 37.89  ? 400  GLU A CD    1 
ATOM   2966  O  OE1   . GLU A 1  400  ? 162.361 112.709 89.346  1.00 38.11  ? 400  GLU A OE1   1 
ATOM   2967  O  OE2   . GLU A 1  400  ? 161.285 114.385 88.432  1.00 36.20  ? 400  GLU A OE2   1 
ATOM   2968  N  N     . VAL A 1  401  ? 156.864 112.602 90.635  1.00 26.55  ? 401  VAL A N     1 
ATOM   2969  C  CA    . VAL A 1  401  ? 155.686 111.920 91.153  1.00 23.58  ? 401  VAL A CA    1 
ATOM   2970  C  C     . VAL A 1  401  ? 155.998 111.391 92.544  1.00 24.71  ? 401  VAL A C     1 
ATOM   2971  O  O     . VAL A 1  401  ? 156.972 110.656 92.741  1.00 30.85  ? 401  VAL A O     1 
ATOM   2972  C  CB    . VAL A 1  401  ? 155.256 110.805 90.199  1.00 22.88  ? 401  VAL A CB    1 
ATOM   2973  C  CG1   . VAL A 1  401  ? 154.329 109.848 90.890  1.00 21.28  ? 401  VAL A CG1   1 
ATOM   2974  C  CG2   . VAL A 1  401  ? 154.584 111.400 88.984  1.00 21.52  ? 401  VAL A CG2   1 
ATOM   2975  N  N     . GLY A 1  402  ? 155.180 111.772 93.518  1.00 19.09  ? 402  GLY A N     1 
ATOM   2976  C  CA    . GLY A 1  402  ? 155.423 111.457 94.909  1.00 21.76  ? 402  GLY A CA    1 
ATOM   2977  C  C     . GLY A 1  402  ? 155.917 112.620 95.740  1.00 22.80  ? 402  GLY A C     1 
ATOM   2978  O  O     . GLY A 1  402  ? 155.922 112.517 96.971  1.00 18.25  ? 402  GLY A O     1 
ATOM   2979  N  N     . ASP A 1  403  ? 156.348 113.711 95.121  1.00 26.42  ? 403  ASP A N     1 
ATOM   2980  C  CA    . ASP A 1  403  ? 156.650 114.908 95.883  1.00 24.98  ? 403  ASP A CA    1 
ATOM   2981  C  C     . ASP A 1  403  ? 155.358 115.565 96.350  1.00 27.74  ? 403  ASP A C     1 
ATOM   2982  O  O     . ASP A 1  403  ? 154.287 115.368 95.776  1.00 24.07  ? 403  ASP A O     1 
ATOM   2983  C  CB    . ASP A 1  403  ? 157.465 115.905 95.061  1.00 23.34  ? 403  ASP A CB    1 
ATOM   2984  C  CG    . ASP A 1  403  ? 158.834 115.382 94.689  1.00 31.88  ? 403  ASP A CG    1 
ATOM   2985  O  OD1   . ASP A 1  403  ? 159.316 114.433 95.335  1.00 33.04  ? 403  ASP A OD1   1 
ATOM   2986  O  OD2   . ASP A 1  403  ? 159.444 115.944 93.760  1.00 31.08  ? 403  ASP A OD2   1 
ATOM   2987  N  N     . ILE A 1  404  ? 155.468 116.355 97.407  1.00 20.21  ? 404  ILE A N     1 
ATOM   2988  C  CA    . ILE A 1  404  ? 154.327 117.033 97.994  1.00 16.72  ? 404  ILE A CA    1 
ATOM   2989  C  C     . ILE A 1  404  ? 154.573 118.527 97.878  1.00 15.68  ? 404  ILE A C     1 
ATOM   2990  O  O     . ILE A 1  404  ? 155.565 119.044 98.400  1.00 18.60  ? 404  ILE A O     1 
ATOM   2991  C  CB    . ILE A 1  404  ? 154.094 116.612 99.451  1.00 19.10  ? 404  ILE A CB    1 
ATOM   2992  C  CG1   . ILE A 1  404  ? 153.784 115.116 99.514  1.00 18.95  ? 404  ILE A CG1   1 
ATOM   2993  C  CG2   . ILE A 1  404  ? 152.958 117.403 100.062 1.00 15.50  ? 404  ILE A CG2   1 
ATOM   2994  C  CD1   . ILE A 1  404  ? 153.802 114.541 100.884 1.00 19.26  ? 404  ILE A CD1   1 
ATOM   2995  N  N     . LEU A 1  405  ? 153.672 119.219 97.198  1.00 9.88   ? 405  LEU A N     1 
ATOM   2996  C  CA    . LEU A 1  405  ? 153.752 120.659 97.033  1.00 6.67   ? 405  LEU A CA    1 
ATOM   2997  C  C     . LEU A 1  405  ? 152.803 121.333 98.012  1.00 8.88   ? 405  LEU A C     1 
ATOM   2998  O  O     . LEU A 1  405  ? 151.656 120.913 98.159  1.00 9.84   ? 405  LEU A O     1 
ATOM   2999  C  CB    . LEU A 1  405  ? 153.404 121.043 95.597  1.00 9.76   ? 405  LEU A CB    1 
ATOM   3000  C  CG    . LEU A 1  405  ? 153.432 122.511 95.184  1.00 10.35  ? 405  LEU A CG    1 
ATOM   3001  C  CD1   . LEU A 1  405  ? 154.826 123.071 95.276  1.00 10.54  ? 405  LEU A CD1   1 
ATOM   3002  C  CD2   . LEU A 1  405  ? 152.897 122.653 93.781  1.00 12.88  ? 405  LEU A CD2   1 
ATOM   3003  N  N     . TYR A 1  406  ? 153.285 122.367 98.686  1.00 4.19   ? 406  TYR A N     1 
ATOM   3004  C  CA    . TYR A 1  406  ? 152.471 123.150 99.609  1.00 1.12   ? 406  TYR A CA    1 
ATOM   3005  C  C     . TYR A 1  406  ? 152.144 124.467 98.920  1.00 6.86   ? 406  TYR A C     1 
ATOM   3006  O  O     . TYR A 1  406  ? 152.963 125.379 98.871  1.00 14.97  ? 406  TYR A O     1 
ATOM   3007  C  CB    . TYR A 1  406  ? 153.205 123.359 100.921 1.00 6.25   ? 406  TYR A CB    1 
ATOM   3008  C  CG    . TYR A 1  406  ? 153.420 122.083 101.684 1.00 14.58  ? 406  TYR A CG    1 
ATOM   3009  C  CD1   . TYR A 1  406  ? 152.498 121.648 102.610 1.00 11.62  ? 406  TYR A CD1   1 
ATOM   3010  C  CD2   . TYR A 1  406  ? 154.538 121.301 101.461 1.00 14.58  ? 406  TYR A CD2   1 
ATOM   3011  C  CE1   . TYR A 1  406  ? 152.690 120.487 103.301 1.00 12.53  ? 406  TYR A CE1   1 
ATOM   3012  C  CE2   . TYR A 1  406  ? 154.735 120.139 102.147 1.00 9.19   ? 406  TYR A CE2   1 
ATOM   3013  C  CZ    . TYR A 1  406  ? 153.809 119.733 103.066 1.00 12.39  ? 406  TYR A CZ    1 
ATOM   3014  O  OH    . TYR A 1  406  ? 154.002 118.565 103.759 1.00 18.17  ? 406  TYR A OH    1 
ATOM   3015  N  N     . ARG A 1  407  ? 150.933 124.560 98.387  1.00 5.46   ? 407  ARG A N     1 
ATOM   3016  C  CA    . ARG A 1  407  ? 150.489 125.692 97.595  1.00 12.90  ? 407  ARG A CA    1 
ATOM   3017  C  C     . ARG A 1  407  ? 149.642 126.646 98.429  1.00 14.52  ? 407  ARG A C     1 
ATOM   3018  O  O     . ARG A 1  407  ? 149.355 126.406 99.596  1.00 6.68   ? 407  ARG A O     1 
ATOM   3019  C  CB    . ARG A 1  407  ? 149.700 125.208 96.384  1.00 2.65   ? 407  ARG A CB    1 
ATOM   3020  C  CG    . ARG A 1  407  ? 148.463 124.422 96.722  1.00 2.68   ? 407  ARG A CG    1 
ATOM   3021  C  CD    . ARG A 1  407  ? 147.550 124.351 95.541  1.00 2.43   ? 407  ARG A CD    1 
ATOM   3022  N  NE    . ARG A 1  407  ? 146.293 123.675 95.828  1.00 9.61   ? 407  ARG A NE    1 
ATOM   3023  C  CZ    . ARG A 1  407  ? 145.273 124.223 96.471  1.00 5.66   ? 407  ARG A CZ    1 
ATOM   3024  N  NH1   . ARG A 1  407  ? 145.330 125.458 96.932  1.00 4.64   ? 407  ARG A NH1   1 
ATOM   3025  N  NH2   . ARG A 1  407  ? 144.164 123.517 96.644  1.00 2.78   ? 407  ARG A NH2   1 
ATOM   3026  N  N     . ASP A 1  408  ? 149.232 127.745 97.806  1.00 4.99   ? 408  ASP A N     1 
ATOM   3027  C  CA    . ASP A 1  408  ? 148.421 128.751 98.473  1.00 1.74   ? 408  ASP A CA    1 
ATOM   3028  C  C     . ASP A 1  408  ? 146.948 128.346 98.483  1.00 3.84   ? 408  ASP A C     1 
ATOM   3029  O  O     . ASP A 1  408  ? 146.518 127.415 97.806  1.00 7.92   ? 408  ASP A O     1 
ATOM   3030  C  CB    . ASP A 1  408  ? 148.586 130.105 97.796  1.00 3.02   ? 408  ASP A CB    1 
ATOM   3031  C  CG    . ASP A 1  408  ? 149.899 130.755 98.110  1.00 11.88  ? 408  ASP A CG    1 
ATOM   3032  O  OD1   . ASP A 1  408  ? 150.546 130.353 99.088  1.00 20.20  ? 408  ASP A OD1   1 
ATOM   3033  O  OD2   . ASP A 1  408  ? 150.277 131.698 97.394  1.00 10.91  ? 408  ASP A OD2   1 
ATOM   3034  N  N     . VAL A 1  409  ? 146.164 129.074 99.261  1.00 7.33   ? 409  VAL A N     1 
ATOM   3035  C  CA    . VAL A 1  409  ? 144.729 128.847 99.374  1.00 2.65   ? 409  VAL A CA    1 
ATOM   3036  C  C     . VAL A 1  409  ? 144.032 129.649 98.287  1.00 13.13  ? 409  VAL A C     1 
ATOM   3037  O  O     . VAL A 1  409  ? 144.322 130.831 98.097  1.00 5.31   ? 409  VAL A O     1 
ATOM   3038  C  CB    . VAL A 1  409  ? 144.226 129.241 100.774 1.00 1.18   ? 409  VAL A CB    1 
ATOM   3039  C  CG1   . VAL A 1  409  ? 142.727 129.243 100.827 1.00 10.09  ? 409  VAL A CG1   1 
ATOM   3040  C  CG2   . VAL A 1  409  ? 144.797 128.309 101.815 1.00 1.64   ? 409  VAL A CG2   1 
ATOM   3041  N  N     . VAL A 1  410  ? 143.133 129.005 97.553  1.00 0.39   ? 410  VAL A N     1 
ATOM   3042  C  CA    . VAL A 1  410  ? 142.484 129.619 96.408  1.00 0.58   ? 410  VAL A CA    1 
ATOM   3043  C  C     . VAL A 1  410  ? 140.976 129.595 96.625  1.00 0.84   ? 410  VAL A C     1 
ATOM   3044  O  O     . VAL A 1  410  ? 140.478 129.068 97.613  1.00 6.87   ? 410  VAL A O     1 
ATOM   3045  C  CB    . VAL A 1  410  ? 142.868 128.933 95.082  1.00 8.30   ? 410  VAL A CB    1 
ATOM   3046  C  CG1   . VAL A 1  410  ? 144.340 129.076 94.831  1.00 3.15   ? 410  VAL A CG1   1 
ATOM   3047  C  CG2   . VAL A 1  410  ? 142.462 127.481 95.085  1.00 1.87   ? 410  VAL A CG2   1 
ATOM   3048  N  N     . THR A 1  411  ? 140.252 130.206 95.699  1.00 10.32  ? 411  THR A N     1 
ATOM   3049  C  CA    . THR A 1  411  ? 138.799 130.201 95.774  1.00 4.88   ? 411  THR A CA    1 
ATOM   3050  C  C     . THR A 1  411  ? 138.276 128.800 95.504  1.00 1.91   ? 411  THR A C     1 
ATOM   3051  O  O     . THR A 1  411  ? 138.679 128.151 94.539  1.00 10.84  ? 411  THR A O     1 
ATOM   3052  C  CB    . THR A 1  411  ? 138.210 131.206 94.783  1.00 0.98   ? 411  THR A CB    1 
ATOM   3053  O  OG1   . THR A 1  411  ? 138.560 132.529 95.188  1.00 10.02  ? 411  THR A OG1   1 
ATOM   3054  C  CG2   . THR A 1  411  ? 136.714 131.113 94.731  1.00 12.01  ? 411  THR A CG2   1 
ATOM   3055  N  N     . GLY A 1  412  ? 137.390 128.326 96.368  1.00 2.52   ? 412  GLY A N     1 
ATOM   3056  C  CA    . GLY A 1  412  ? 136.841 126.996 96.277  1.00 5.07   ? 412  GLY A CA    1 
ATOM   3057  C  C     . GLY A 1  412  ? 137.373 126.023 97.302  1.00 4.03   ? 412  GLY A C     1 
ATOM   3058  O  O     . GLY A 1  412  ? 136.817 124.929 97.433  1.00 18.86  ? 412  GLY A O     1 
ATOM   3059  N  N     . ASP A 1  413  ? 138.436 126.372 98.015  1.00 7.23   ? 413  ASP A N     1 
ATOM   3060  C  CA    . ASP A 1  413  ? 138.904 125.536 99.104  1.00 15.60  ? 413  ASP A CA    1 
ATOM   3061  C  C     . ASP A 1  413  ? 137.899 125.560 100.246 1.00 6.57   ? 413  ASP A C     1 
ATOM   3062  O  O     . ASP A 1  413  ? 137.176 126.532 100.440 1.00 12.22  ? 413  ASP A O     1 
ATOM   3063  C  CB    . ASP A 1  413  ? 140.269 126.009 99.598  1.00 1.23   ? 413  ASP A CB    1 
ATOM   3064  C  CG    . ASP A 1  413  ? 141.417 125.446 98.786  1.00 8.92   ? 413  ASP A CG    1 
ATOM   3065  O  OD1   . ASP A 1  413  ? 141.250 124.397 98.148  1.00 17.10  ? 413  ASP A OD1   1 
ATOM   3066  O  OD2   . ASP A 1  413  ? 142.502 126.045 98.790  1.00 7.16   ? 413  ASP A OD2   1 
ATOM   3067  N  N     . VAL A 1  414  ? 137.845 124.479 100.992 1.00 6.25   ? 414  VAL A N     1 
ATOM   3068  C  CA    . VAL A 1  414  ? 136.957 124.387 102.138 1.00 8.10   ? 414  VAL A CA    1 
ATOM   3069  C  C     . VAL A 1  414  ? 137.715 124.786 103.398 1.00 5.16   ? 414  VAL A C     1 
ATOM   3070  O  O     . VAL A 1  414  ? 138.913 124.559 103.527 1.00 10.59  ? 414  VAL A O     1 
ATOM   3071  C  CB    . VAL A 1  414  ? 136.347 122.975 102.265 1.00 4.48   ? 414  VAL A CB    1 
ATOM   3072  C  CG1   . VAL A 1  414  ? 135.419 122.713 101.120 1.00 0.20   ? 414  VAL A CG1   1 
ATOM   3073  C  CG2   . VAL A 1  414  ? 137.418 121.922 102.299 1.00 2.08   ? 414  VAL A CG2   1 
ATOM   3074  N  N     . ALA A 1  415  ? 137.009 125.399 104.341 1.00 6.58   ? 415  ALA A N     1 
ATOM   3075  C  CA    . ALA A 1  415  ? 137.633 125.853 105.575 1.00 2.66   ? 415  ALA A CA    1 
ATOM   3076  C  C     . ALA A 1  415  ? 136.675 125.701 106.745 1.00 15.90  ? 415  ALA A C     1 
ATOM   3077  O  O     . ALA A 1  415  ? 135.475 125.913 106.598 1.00 6.72   ? 415  ALA A O     1 
ATOM   3078  C  CB    . ALA A 1  415  ? 138.075 127.307 105.467 1.00 7.83   ? 415  ALA A CB    1 
ATOM   3079  N  N     . PHE A 1  416  ? 137.222 125.362 107.908 1.00 13.49  ? 416  PHE A N     1 
ATOM   3080  C  CA    . PHE A 1  416  ? 136.450 125.309 109.141 1.00 11.46  ? 416  PHE A CA    1 
ATOM   3081  C  C     . PHE A 1  416  ? 136.347 126.695 109.767 1.00 3.52   ? 416  PHE A C     1 
ATOM   3082  O  O     . PHE A 1  416  ? 137.355 127.369 109.967 1.00 3.77   ? 416  PHE A O     1 
ATOM   3083  C  CB    . PHE A 1  416  ? 137.091 124.345 110.130 1.00 2.02   ? 416  PHE A CB    1 
ATOM   3084  C  CG    . PHE A 1  416  ? 136.874 122.900 109.809 1.00 7.64   ? 416  PHE A CG    1 
ATOM   3085  C  CD1   . PHE A 1  416  ? 137.723 122.234 108.959 1.00 14.30  ? 416  PHE A CD1   1 
ATOM   3086  C  CD2   . PHE A 1  416  ? 135.828 122.203 110.371 1.00 5.51   ? 416  PHE A CD2   1 
ATOM   3087  C  CE1   . PHE A 1  416  ? 137.531 120.918 108.675 1.00 1.41   ? 416  PHE A CE1   1 
ATOM   3088  C  CE2   . PHE A 1  416  ? 135.640 120.882 110.082 1.00 0.15   ? 416  PHE A CE2   1 
ATOM   3089  C  CZ    . PHE A 1  416  ? 136.495 120.244 109.230 1.00 0.26   ? 416  PHE A CZ    1 
ATOM   3090  N  N     . PHE A 1  417  ? 135.126 127.105 110.090 1.00 9.21   ? 417  PHE A N     1 
ATOM   3091  C  CA    . PHE A 1  417  ? 134.816 128.417 110.641 1.00 1.98   ? 417  PHE A CA    1 
ATOM   3092  C  C     . PHE A 1  417  ? 134.247 128.236 112.041 1.00 3.27   ? 417  PHE A C     1 
ATOM   3093  O  O     . PHE A 1  417  ? 133.264 127.521 112.221 1.00 15.75  ? 417  PHE A O     1 
ATOM   3094  C  CB    . PHE A 1  417  ? 133.825 129.138 109.719 1.00 7.69   ? 417  PHE A CB    1 
ATOM   3095  C  CG    . PHE A 1  417  ? 133.919 130.635 109.739 1.00 6.34   ? 417  PHE A CG    1 
ATOM   3096  C  CD1   . PHE A 1  417  ? 135.112 131.276 109.986 1.00 5.35   ? 417  PHE A CD1   1 
ATOM   3097  C  CD2   . PHE A 1  417  ? 132.804 131.398 109.474 1.00 2.30   ? 417  PHE A CD2   1 
ATOM   3098  C  CE1   . PHE A 1  417  ? 135.183 132.637 109.999 1.00 14.43  ? 417  PHE A CE1   1 
ATOM   3099  C  CE2   . PHE A 1  417  ? 132.874 132.759 109.477 1.00 6.45   ? 417  PHE A CE2   1 
ATOM   3100  C  CZ    . PHE A 1  417  ? 134.068 133.381 109.733 1.00 4.58   ? 417  PHE A CZ    1 
ATOM   3101  N  N     . ASN A 1  418  ? 134.863 128.871 113.029 1.00 4.64   ? 418  ASN A N     1 
ATOM   3102  C  CA    . ASN A 1  418  ? 134.571 128.598 114.428 1.00 10.25  ? 418  ASN A CA    1 
ATOM   3103  C  C     . ASN A 1  418  ? 134.342 129.894 115.187 1.00 11.86  ? 418  ASN A C     1 
ATOM   3104  O  O     . ASN A 1  418  ? 135.129 130.828 115.065 1.00 23.50  ? 418  ASN A O     1 
ATOM   3105  C  CB    . ASN A 1  418  ? 135.726 127.828 115.062 1.00 15.45  ? 418  ASN A CB    1 
ATOM   3106  C  CG    . ASN A 1  418  ? 135.499 127.518 116.513 1.00 15.34  ? 418  ASN A CG    1 
ATOM   3107  O  OD1   . ASN A 1  418  ? 134.380 127.371 116.969 1.00 13.72  ? 418  ASN A OD1   1 
ATOM   3108  N  ND2   . ASN A 1  418  ? 136.573 127.459 117.257 1.00 22.22  ? 418  ASN A ND2   1 
ATOM   3109  N  N     . ARG A 1  419  ? 133.284 129.944 115.985 1.00 7.97   ? 419  ARG A N     1 
ATOM   3110  C  CA    . ARG A 1  419  ? 133.076 131.026 116.936 1.00 0.60   ? 419  ARG A CA    1 
ATOM   3111  C  C     . ARG A 1  419  ? 132.881 130.456 118.330 1.00 5.27   ? 419  ARG A C     1 
ATOM   3112  O  O     . ARG A 1  419  ? 132.124 129.503 118.514 1.00 6.95   ? 419  ARG A O     1 
ATOM   3113  C  CB    . ARG A 1  419  ? 131.877 131.887 116.568 1.00 5.91   ? 419  ARG A CB    1 
ATOM   3114  C  CG    . ARG A 1  419  ? 131.750 133.070 117.476 1.00 4.23   ? 419  ARG A CG    1 
ATOM   3115  C  CD    . ARG A 1  419  ? 130.469 133.779 117.304 1.00 6.64   ? 419  ARG A CD    1 
ATOM   3116  N  NE    . ARG A 1  419  ? 130.266 134.768 118.349 1.00 2.22   ? 419  ARG A NE    1 
ATOM   3117  C  CZ    . ARG A 1  419  ? 129.659 134.522 119.499 1.00 7.40   ? 419  ARG A CZ    1 
ATOM   3118  N  NH1   . ARG A 1  419  ? 129.196 133.320 119.790 1.00 7.45   ? 419  ARG A NH1   1 
ATOM   3119  N  NH2   . ARG A 1  419  ? 129.509 135.506 120.378 1.00 15.91  ? 419  ARG A NH2   1 
ATOM   3120  N  N     . GLN A 1  420  ? 133.534 131.058 119.303 1.00 7.46   ? 420  GLN A N     1 
ATOM   3121  C  CA    . GLN A 1  420  ? 133.541 130.644 120.693 1.00 1.22   ? 420  GLN A CA    1 
ATOM   3122  C  C     . GLN A 1  420  ? 132.680 131.560 121.546 1.00 1.44   ? 420  GLN A C     1 
ATOM   3123  O  O     . GLN A 1  420  ? 132.583 132.753 121.267 1.00 15.03  ? 420  GLN A O     1 
ATOM   3124  C  CB    . GLN A 1  420  ? 134.967 130.634 121.222 1.00 12.94  ? 420  GLN A CB    1 
ATOM   3125  C  CG    . GLN A 1  420  ? 135.813 129.646 120.484 1.00 0.55   ? 420  GLN A CG    1 
ATOM   3126  C  CD    . GLN A 1  420  ? 137.269 129.828 120.751 1.00 6.98   ? 420  GLN A CD    1 
ATOM   3127  O  OE1   . GLN A 1  420  ? 138.094 129.045 120.295 1.00 12.92  ? 420  GLN A OE1   1 
ATOM   3128  N  NE2   . GLN A 1  420  ? 137.605 130.880 121.475 1.00 6.92   ? 420  GLN A NE2   1 
ATOM   3129  N  N     . PRO A 1  421  ? 132.019 131.026 122.578 1.00 5.52   ? 421  PRO A N     1 
ATOM   3130  C  CA    . PRO A 1  421  ? 132.023 129.623 123.027 1.00 4.22   ? 421  PRO A CA    1 
ATOM   3131  C  C     . PRO A 1  421  ? 131.277 128.673 122.096 1.00 2.01   ? 421  PRO A C     1 
ATOM   3132  O  O     . PRO A 1  421  ? 130.268 129.029 121.514 1.00 5.52   ? 421  PRO A O     1 
ATOM   3133  C  CB    . PRO A 1  421  ? 131.365 129.715 124.405 1.00 6.26   ? 421  PRO A CB    1 
ATOM   3134  C  CG    . PRO A 1  421  ? 130.460 130.898 124.315 1.00 2.76   ? 421  PRO A CG    1 
ATOM   3135  C  CD    . PRO A 1  421  ? 131.176 131.876 123.438 1.00 3.27   ? 421  PRO A CD    1 
ATOM   3136  N  N     . SER A 1  422  ? 131.779 127.449 121.951 1.00 2.87   ? 422  SER A N     1 
ATOM   3137  C  CA    . SER A 1  422  ? 131.235 126.450 121.035 1.00 0.40   ? 422  SER A CA    1 
ATOM   3138  C  C     . SER A 1  422  ? 130.216 125.590 121.766 1.00 0.13   ? 422  SER A C     1 
ATOM   3139  O  O     . SER A 1  422  ? 130.535 124.541 122.310 1.00 8.71   ? 422  SER A O     1 
ATOM   3140  C  CB    . SER A 1  422  ? 132.356 125.601 120.456 1.00 0.99   ? 422  SER A CB    1 
ATOM   3141  O  OG    . SER A 1  422  ? 133.334 126.411 119.848 1.00 13.54  ? 422  SER A OG    1 
ATOM   3142  N  N     . LEU A 1  423  ? 128.959 126.019 121.729 1.00 2.33   ? 423  LEU A N     1 
ATOM   3143  C  CA    . LEU A 1  423  ? 127.909 125.438 122.547 1.00 2.73   ? 423  LEU A CA    1 
ATOM   3144  C  C     . LEU A 1  423  ? 127.041 124.419 121.820 1.00 4.82   ? 423  LEU A C     1 
ATOM   3145  O  O     . LEU A 1  423  ? 126.508 123.519 122.467 1.00 9.12   ? 423  LEU A O     1 
ATOM   3146  C  CB    . LEU A 1  423  ? 127.018 126.551 123.103 1.00 5.49   ? 423  LEU A CB    1 
ATOM   3147  C  CG    . LEU A 1  423  ? 127.693 127.513 124.073 1.00 2.04   ? 423  LEU A CG    1 
ATOM   3148  C  CD1   . LEU A 1  423  ? 126.824 128.711 124.322 1.00 3.27   ? 423  LEU A CD1   1 
ATOM   3149  C  CD2   . LEU A 1  423  ? 127.976 126.811 125.361 1.00 3.95   ? 423  LEU A CD2   1 
ATOM   3150  N  N     . GLU A 1  424  ? 126.880 124.539 120.510 1.00 6.98   ? 424  GLU A N     1 
ATOM   3151  C  CA    . GLU A 1  424  ? 126.064 123.628 119.725 1.00 12.83  ? 424  GLU A CA    1 
ATOM   3152  C  C     . GLU A 1  424  ? 126.918 123.095 118.592 1.00 3.33   ? 424  GLU A C     1 
ATOM   3153  O  O     . GLU A 1  424  ? 128.060 123.508 118.424 1.00 5.52   ? 424  GLU A O     1 
ATOM   3154  C  CB    . GLU A 1  424  ? 124.812 124.330 119.208 1.00 2.28   ? 424  GLU A CB    1 
ATOM   3155  C  CG    . GLU A 1  424  ? 125.093 125.535 118.364 1.00 4.80   ? 424  GLU A CG    1 
ATOM   3156  C  CD    . GLU A 1  424  ? 124.193 126.684 118.719 1.00 19.19  ? 424  GLU A CD    1 
ATOM   3157  O  OE1   . GLU A 1  424  ? 123.343 126.497 119.612 1.00 12.98  ? 424  GLU A OE1   1 
ATOM   3158  O  OE2   . GLU A 1  424  ? 124.327 127.774 118.114 1.00 17.47  ? 424  GLU A OE2   1 
ATOM   3159  N  N     . ARG A 1  425  ? 126.382 122.169 117.805 1.00 6.82   ? 425  ARG A N     1 
ATOM   3160  C  CA    . ARG A 1  425  ? 127.241 121.544 116.811 1.00 1.37   ? 425  ARG A CA    1 
ATOM   3161  C  C     . ARG A 1  425  ? 127.247 122.264 115.470 1.00 3.27   ? 425  ARG A C     1 
ATOM   3162  O  O     . ARG A 1  425  ? 127.906 121.802 114.542 1.00 10.22  ? 425  ARG A O     1 
ATOM   3163  C  CB    . ARG A 1  425  ? 126.893 120.060 116.631 1.00 8.68   ? 425  ARG A CB    1 
ATOM   3164  C  CG    . ARG A 1  425  ? 125.709 119.705 115.802 1.00 11.13  ? 425  ARG A CG    1 
ATOM   3165  C  CD    . ARG A 1  425  ? 125.892 118.284 115.323 1.00 5.10   ? 425  ARG A CD    1 
ATOM   3166  N  NE    . ARG A 1  425  ? 124.633 117.607 115.057 1.00 6.23   ? 425  ARG A NE    1 
ATOM   3167  C  CZ    . ARG A 1  425  ? 124.523 116.354 114.649 1.00 4.52   ? 425  ARG A CZ    1 
ATOM   3168  N  NH1   . ARG A 1  425  ? 125.581 115.613 114.397 1.00 6.47   ? 425  ARG A NH1   1 
ATOM   3169  N  NH2   . ARG A 1  425  ? 123.317 115.827 114.505 1.00 5.87   ? 425  ARG A NH2   1 
ATOM   3170  N  N     . SER A 1  426  ? 126.569 123.393 115.352 1.00 12.21  ? 426  SER A N     1 
ATOM   3171  C  CA    . SER A 1  426  ? 126.779 124.295 114.236 1.00 2.65   ? 426  SER A CA    1 
ATOM   3172  C  C     . SER A 1  426  ? 127.782 125.393 114.560 1.00 0.46   ? 426  SER A C     1 
ATOM   3173  O  O     . SER A 1  426  ? 128.003 126.273 113.728 1.00 3.71   ? 426  SER A O     1 
ATOM   3174  C  CB    . SER A 1  426  ? 125.451 124.897 113.786 1.00 14.57  ? 426  SER A CB    1 
ATOM   3175  O  OG    . SER A 1  426  ? 124.892 125.718 114.781 1.00 9.50   ? 426  SER A OG    1 
ATOM   3176  N  N     . SER A 1  427  ? 128.396 125.350 115.747 1.00 15.25  ? 427  SER A N     1 
ATOM   3177  C  CA    . SER A 1  427  ? 129.429 126.300 116.139 1.00 2.93   ? 427  SER A CA    1 
ATOM   3178  C  C     . SER A 1  427  ? 130.707 126.149 115.338 1.00 4.01   ? 427  SER A C     1 
ATOM   3179  O  O     . SER A 1  427  ? 131.533 127.062 115.341 1.00 10.34  ? 427  SER A O     1 
ATOM   3180  C  CB    . SER A 1  427  ? 129.761 126.153 117.616 1.00 13.33  ? 427  SER A CB    1 
ATOM   3181  O  OG    . SER A 1  427  ? 128.735 126.680 118.414 1.00 8.33   ? 427  SER A OG    1 
ATOM   3182  N  N     . ILE A 1  428  ? 130.909 125.012 114.695 1.00 8.05   ? 428  ILE A N     1 
ATOM   3183  C  CA    . ILE A 1  428  ? 131.967 124.830 113.721 1.00 3.96   ? 428  ILE A CA    1 
ATOM   3184  C  C     . ILE A 1  428  ? 131.298 124.369 112.444 1.00 0.56   ? 428  ILE A C     1 
ATOM   3185  O  O     . ILE A 1  428  ? 130.573 123.372 112.448 1.00 8.14   ? 428  ILE A O     1 
ATOM   3186  C  CB    . ILE A 1  428  ? 133.023 123.820 114.196 1.00 4.52   ? 428  ILE A CB    1 
ATOM   3187  C  CG1   . ILE A 1  428  ? 133.596 124.245 115.546 1.00 2.66   ? 428  ILE A CG1   1 
ATOM   3188  C  CG2   . ILE A 1  428  ? 134.123 123.677 113.170 1.00 14.04  ? 428  ILE A CG2   1 
ATOM   3189  C  CD1   . ILE A 1  428  ? 134.463 123.237 116.185 1.00 4.67   ? 428  ILE A CD1   1 
ATOM   3190  N  N     . GLY A 1  429  ? 131.512 125.101 111.360 1.00 7.36   ? 429  GLY A N     1 
ATOM   3191  C  CA    . GLY A 1  429  ? 130.956 124.724 110.083 1.00 7.29   ? 429  GLY A CA    1 
ATOM   3192  C  C     . GLY A 1  429  ? 131.997 124.894 109.002 1.00 5.83   ? 429  GLY A C     1 
ATOM   3193  O  O     . GLY A 1  429  ? 133.023 125.529 109.205 1.00 15.32  ? 429  GLY A O     1 
ATOM   3194  N  N     . VAL A 1  430  ? 131.718 124.310 107.848 1.00 1.43   ? 430  VAL A N     1 
ATOM   3195  C  CA    . VAL A 1  430  ? 132.648 124.326 106.727 1.00 2.46   ? 430  VAL A CA    1 
ATOM   3196  C  C     . VAL A 1  430  ? 132.071 125.203 105.628 1.00 0.28   ? 430  VAL A C     1 
ATOM   3197  O  O     . VAL A 1  430  ? 130.922 125.032 105.213 1.00 3.26   ? 430  VAL A O     1 
ATOM   3198  C  CB    . VAL A 1  430  ? 132.962 122.907 106.227 1.00 10.16  ? 430  VAL A CB    1 
ATOM   3199  C  CG1   . VAL A 1  430  ? 133.528 122.939 104.837 1.00 9.98   ? 430  VAL A CG1   1 
ATOM   3200  C  CG2   . VAL A 1  430  ? 133.932 122.243 107.156 1.00 4.58   ? 430  VAL A CG2   1 
ATOM   3201  N  N     . HIS A 1  431  ? 132.875 126.155 105.173 1.00 1.95   ? 431  HIS A N     1 
ATOM   3202  C  CA    . HIS A 1  431  ? 132.497 127.118 104.157 1.00 11.73  ? 431  HIS A CA    1 
ATOM   3203  C  C     . HIS A 1  431  ? 133.431 126.988 102.968 1.00 13.89  ? 431  HIS A C     1 
ATOM   3204  O  O     . HIS A 1  431  ? 134.549 126.501 103.098 1.00 6.77   ? 431  HIS A O     1 
ATOM   3205  C  CB    . HIS A 1  431  ? 132.550 128.537 104.708 1.00 8.37   ? 431  HIS A CB    1 
ATOM   3206  C  CG    . HIS A 1  431  ? 131.521 128.825 105.752 1.00 10.41  ? 431  HIS A CG    1 
ATOM   3207  N  ND1   . HIS A 1  431  ? 130.428 129.620 105.516 1.00 15.28  ? 431  HIS A ND1   1 
ATOM   3208  C  CD2   . HIS A 1  431  ? 131.416 128.421 107.036 1.00 7.26   ? 431  HIS A CD2   1 
ATOM   3209  C  CE1   . HIS A 1  431  ? 129.694 129.695 106.606 1.00 9.40   ? 431  HIS A CE1   1 
ATOM   3210  N  NE2   . HIS A 1  431  ? 130.268 128.969 107.542 1.00 2.51   ? 431  HIS A NE2   1 
ATOM   3211  N  N     . ARG A 1  432  ? 132.958 127.408 101.801 1.00 14.23  ? 432  ARG A N     1 
ATOM   3212  C  CA    . ARG A 1  432  ? 133.818 127.534 100.634 1.00 9.64   ? 432  ARG A CA    1 
ATOM   3213  C  C     . ARG A 1  432  ? 134.527 128.875 100.652 1.00 7.39   ? 432  ARG A C     1 
ATOM   3214  O  O     . ARG A 1  432  ? 133.899 129.913 100.842 1.00 16.40  ? 432  ARG A O     1 
ATOM   3215  C  CB    . ARG A 1  432  ? 133.014 127.389 99.353  1.00 15.32  ? 432  ARG A CB    1 
ATOM   3216  C  CG    . ARG A 1  432  ? 132.485 126.008 99.121  1.00 22.98  ? 432  ARG A CG    1 
ATOM   3217  C  CD    . ARG A 1  432  ? 131.612 125.965 97.905  1.00 24.81  ? 432  ARG A CD    1 
ATOM   3218  N  NE    . ARG A 1  432  ? 130.382 126.716 98.099  1.00 26.49  ? 432  ARG A NE    1 
ATOM   3219  C  CZ    . ARG A 1  432  ? 129.963 127.686 97.301  1.00 24.75  ? 432  ARG A CZ    1 
ATOM   3220  N  NH1   . ARG A 1  432  ? 130.648 128.046 96.233  1.00 20.39  ? 432  ARG A NH1   1 
ATOM   3221  N  NH2   . ARG A 1  432  ? 128.824 128.307 97.581  1.00 21.82  ? 432  ARG A NH2   1 
ATOM   3222  N  N     . ILE A 1  433  ? 135.834 128.854 100.451 1.00 1.24   ? 433  ILE A N     1 
ATOM   3223  C  CA    . ILE A 1  433  ? 136.645 130.056 100.586 1.00 0.61   ? 433  ILE A CA    1 
ATOM   3224  C  C     . ILE A 1  433  ? 136.531 130.901 99.325  1.00 4.20   ? 433  ILE A C     1 
ATOM   3225  O  O     . ILE A 1  433  ? 136.592 130.385 98.208  1.00 6.75   ? 433  ILE A O     1 
ATOM   3226  C  CB    . ILE A 1  433  ? 138.103 129.689 100.897 1.00 8.91   ? 433  ILE A CB    1 
ATOM   3227  C  CG1   . ILE A 1  433  ? 138.253 129.466 102.394 1.00 2.69   ? 433  ILE A CG1   1 
ATOM   3228  C  CG2   . ILE A 1  433  ? 139.045 130.779 100.454 1.00 12.56  ? 433  ILE A CG2   1 
ATOM   3229  C  CD1   . ILE A 1  433  ? 139.625 129.202 102.838 1.00 6.74   ? 433  ILE A CD1   1 
ATOM   3230  N  N     . VAL A 1  434  ? 136.315 132.201 99.512  1.00 10.85  ? 434  VAL A N     1 
ATOM   3231  C  CA    . VAL A 1  434  ? 136.445 133.217 98.470  1.00 6.55   ? 434  VAL A CA    1 
ATOM   3232  C  C     . VAL A 1  434  ? 137.567 134.152 98.891  1.00 4.79   ? 434  VAL A C     1 
ATOM   3233  O  O     . VAL A 1  434  ? 137.459 134.830 99.915  1.00 4.38   ? 434  VAL A O     1 
ATOM   3234  C  CB    . VAL A 1  434  ? 135.137 133.997 98.259  1.00 6.76   ? 434  VAL A CB    1 
ATOM   3235  C  CG1   . VAL A 1  434  ? 135.351 135.137 97.316  1.00 0.23   ? 434  VAL A CG1   1 
ATOM   3236  C  CG2   . VAL A 1  434  ? 134.058 133.092 97.738  1.00 0.80   ? 434  VAL A CG2   1 
ATOM   3237  N  N     . VAL A 1  435  ? 138.642 134.188 98.114  1.00 8.13   ? 435  VAL A N     1 
ATOM   3238  C  CA    . VAL A 1  435  ? 139.812 134.983 98.479  1.00 0.66   ? 435  VAL A CA    1 
ATOM   3239  C  C     . VAL A 1  435  ? 139.576 136.434 98.088  1.00 0.74   ? 435  VAL A C     1 
ATOM   3240  O  O     . VAL A 1  435  ? 139.189 136.729 96.955  1.00 8.71   ? 435  VAL A O     1 
ATOM   3241  C  CB    . VAL A 1  435  ? 141.090 134.435 97.830  1.00 1.71   ? 435  VAL A CB    1 
ATOM   3242  C  CG1   . VAL A 1  435  ? 142.249 135.340 98.123  1.00 2.11   ? 435  VAL A CG1   1 
ATOM   3243  C  CG2   . VAL A 1  435  ? 141.393 133.056 98.344  1.00 1.71   ? 435  VAL A CG2   1 
ATOM   3244  N  N     . LEU A 1  436  ? 139.787 137.339 99.035  1.00 9.74   ? 436  LEU A N     1 
ATOM   3245  C  CA    . LEU A 1  436  ? 139.635 138.771 98.808  1.00 1.81   ? 436  LEU A CA    1 
ATOM   3246  C  C     . LEU A 1  436  ? 140.988 139.326 98.399  1.00 3.45   ? 436  LEU A C     1 
ATOM   3247  O  O     . LEU A 1  436  ? 141.926 139.348 99.191  1.00 5.00   ? 436  LEU A O     1 
ATOM   3248  C  CB    . LEU A 1  436  ? 139.101 139.459 100.056 1.00 7.07   ? 436  LEU A CB    1 
ATOM   3249  C  CG    . LEU A 1  436  ? 137.838 138.915 100.711 1.00 0.09   ? 436  LEU A CG    1 
ATOM   3250  C  CD1   . LEU A 1  436  ? 137.598 139.608 102.021 1.00 11.81  ? 436  LEU A CD1   1 
ATOM   3251  C  CD2   . LEU A 1  436  ? 136.655 139.060 99.798  1.00 1.99   ? 436  LEU A CD2   1 
ATOM   3252  N  N     . GLU A 1  437  ? 141.093 139.787 97.160  1.00 6.81   ? 437  GLU A N     1 
ATOM   3253  C  CA    . GLU A 1  437  ? 142.380 140.189 96.620  1.00 4.83   ? 437  GLU A CA    1 
ATOM   3254  C  C     . GLU A 1  437  ? 142.688 141.668 96.823  1.00 10.99  ? 437  GLU A C     1 
ATOM   3255  O  O     . GLU A 1  437  ? 143.768 142.114 96.434  1.00 15.41  ? 437  GLU A O     1 
ATOM   3256  C  CB    . GLU A 1  437  ? 142.450 139.821 95.139  1.00 6.26   ? 437  GLU A CB    1 
ATOM   3257  C  CG    . GLU A 1  437  ? 143.111 138.477 94.900  1.00 10.80  ? 437  GLU A CG    1 
ATOM   3258  C  CD    . GLU A 1  437  ? 142.476 137.681 93.773  1.00 16.81  ? 437  GLU A CD    1 
ATOM   3259  O  OE1   . GLU A 1  437  ? 142.099 136.517 94.006  1.00 12.16  ? 437  GLU A OE1   1 
ATOM   3260  O  OE2   . GLU A 1  437  ? 142.371 138.208 92.648  1.00 25.72  ? 437  GLU A OE2   1 
ATOM   3261  N  N     . ASN A 1  438  ? 141.792 142.426 97.430  1.00 13.90  ? 438  ASN A N     1 
ATOM   3262  C  CA    . ASN A 1  438  ? 142.099 143.786 97.857  1.00 9.14   ? 438  ASN A CA    1 
ATOM   3263  C  C     . ASN A 1  438  ? 143.057 143.725 99.036  1.00 11.60  ? 438  ASN A C     1 
ATOM   3264  O  O     . ASN A 1  438  ? 142.711 143.143 100.068 1.00 14.39  ? 438  ASN A O     1 
ATOM   3265  C  CB    . ASN A 1  438  ? 140.819 144.515 98.246  1.00 8.74   ? 438  ASN A CB    1 
ATOM   3266  C  CG    . ASN A 1  438  ? 141.048 145.975 98.584  1.00 14.08  ? 438  ASN A CG    1 
ATOM   3267  O  OD1   . ASN A 1  438  ? 142.106 146.526 98.316  1.00 24.22  ? 438  ASN A OD1   1 
ATOM   3268  N  ND2   . ASN A 1  438  ? 140.053 146.603 99.185  1.00 11.25  ? 438  ASN A ND2   1 
ATOM   3269  N  N     . PRO A 1  439  ? 144.258 144.298 98.939  1.00 17.10  ? 439  PRO A N     1 
ATOM   3270  C  CA    . PRO A 1  439  ? 145.246 144.114 100.010 1.00 15.22  ? 439  PRO A CA    1 
ATOM   3271  C  C     . PRO A 1  439  ? 144.962 144.919 101.261 1.00 11.65  ? 439  PRO A C     1 
ATOM   3272  O  O     . PRO A 1  439  ? 145.691 144.768 102.244 1.00 15.34  ? 439  PRO A O     1 
ATOM   3273  C  CB    . PRO A 1  439  ? 146.556 144.553 99.351  1.00 12.90  ? 439  PRO A CB    1 
ATOM   3274  C  CG    . PRO A 1  439  ? 146.144 145.480 98.285  1.00 12.10  ? 439  PRO A CG    1 
ATOM   3275  C  CD    . PRO A 1  439  ? 144.834 144.989 97.774  1.00 13.16  ? 439  PRO A CD    1 
ATOM   3276  N  N     . LYS A 1  440  ? 143.936 145.756 101.266 1.00 12.77  ? 440  LYS A N     1 
ATOM   3277  C  CA    . LYS A 1  440  ? 143.642 146.614 102.402 1.00 10.38  ? 440  LYS A CA    1 
ATOM   3278  C  C     . LYS A 1  440  ? 142.591 146.043 103.333 1.00 14.04  ? 440  LYS A C     1 
ATOM   3279  O  O     . LYS A 1  440  ? 142.147 146.750 104.240 1.00 25.15  ? 440  LYS A O     1 
ATOM   3280  C  CB    . LYS A 1  440  ? 143.184 147.990 101.920 1.00 13.88  ? 440  LYS A CB    1 
ATOM   3281  C  CG    . LYS A 1  440  ? 144.317 148.941 101.591 1.00 16.47  ? 440  LYS A CG    1 
ATOM   3282  C  CD    . LYS A 1  440  ? 143.817 150.363 101.432 1.00 17.90  ? 440  LYS A CD    1 
ATOM   3283  C  CE    . LYS A 1  440  ? 142.476 150.418 100.723 1.00 21.66  ? 440  LYS A CE    1 
ATOM   3284  N  NZ    . LYS A 1  440  ? 142.332 151.643 99.891  1.00 15.07  ? 440  LYS A NZ    1 
ATOM   3285  N  N     . ILE A 1  441  ? 142.175 144.798 103.140 1.00 10.04  ? 441  ILE A N     1 
ATOM   3286  C  CA    . ILE A 1  441  ? 141.102 144.195 103.918 1.00 4.49   ? 441  ILE A CA    1 
ATOM   3287  C  C     . ILE A 1  441  ? 141.699 143.119 104.810 1.00 1.65   ? 441  ILE A C     1 
ATOM   3288  O  O     . ILE A 1  441  ? 142.495 142.297 104.352 1.00 12.95  ? 441  ILE A O     1 
ATOM   3289  C  CB    . ILE A 1  441  ? 139.998 143.637 103.008 1.00 5.48   ? 441  ILE A CB    1 
ATOM   3290  C  CG1   . ILE A 1  441  ? 139.244 144.791 102.352 1.00 0.83   ? 441  ILE A CG1   1 
ATOM   3291  C  CG2   . ILE A 1  441  ? 139.049 142.768 103.787 1.00 6.81   ? 441  ILE A CG2   1 
ATOM   3292  C  CD1   . ILE A 1  441  ? 138.349 144.368 101.274 1.00 7.02   ? 441  ILE A CD1   1 
ATOM   3293  N  N     . SER A 1  442  ? 141.333 143.138 106.088 1.00 0.90   ? 442  SER A N     1 
ATOM   3294  C  CA    . SER A 1  442  ? 141.883 142.218 107.074 1.00 1.09   ? 442  SER A CA    1 
ATOM   3295  C  C     . SER A 1  442  ? 140.810 141.423 107.798 1.00 1.94   ? 442  SER A C     1 
ATOM   3296  O  O     . SER A 1  442  ? 141.116 140.755 108.784 1.00 6.33   ? 442  SER A O     1 
ATOM   3297  C  CB    . SER A 1  442  ? 142.718 142.983 108.102 1.00 5.89   ? 442  SER A CB    1 
ATOM   3298  O  OG    . SER A 1  442  ? 143.779 143.680 107.487 1.00 14.74  ? 442  SER A OG    1 
ATOM   3299  N  N     . THR A 1  443  ? 139.572 141.470 107.341 1.00 4.77   ? 443  THR A N     1 
ATOM   3300  C  CA    . THR A 1  443  ? 138.460 140.874 108.058 1.00 4.53   ? 443  THR A CA    1 
ATOM   3301  C  C     . THR A 1  443  ? 138.043 139.559 107.419 1.00 5.54   ? 443  THR A C     1 
ATOM   3302  O  O     . THR A 1  443  ? 138.262 139.327 106.233 1.00 12.86  ? 443  THR A O     1 
ATOM   3303  C  CB    . THR A 1  443  ? 137.265 141.827 108.093 1.00 1.96   ? 443  THR A CB    1 
ATOM   3304  O  OG1   . THR A 1  443  ? 137.114 142.441 106.816 1.00 12.69  ? 443  THR A OG1   1 
ATOM   3305  C  CG2   . THR A 1  443  ? 137.447 142.902 109.130 1.00 7.11   ? 443  THR A CG2   1 
ATOM   3306  N  N     . PHE A 1  444  ? 137.450 138.692 108.234 1.00 3.13   ? 444  PHE A N     1 
ATOM   3307  C  CA    . PHE A 1  444  ? 136.723 137.529 107.741 1.00 4.65   ? 444  PHE A CA    1 
ATOM   3308  C  C     . PHE A 1  444  ? 135.310 137.980 107.399 1.00 2.48   ? 444  PHE A C     1 
ATOM   3309  O  O     . PHE A 1  444  ? 134.602 138.499 108.258 1.00 7.60   ? 444  PHE A O     1 
ATOM   3310  C  CB    . PHE A 1  444  ? 136.684 136.419 108.793 1.00 5.74   ? 444  PHE A CB    1 
ATOM   3311  C  CG    . PHE A 1  444  ? 138.014 135.789 109.090 1.00 3.91   ? 444  PHE A CG    1 
ATOM   3312  C  CD1   . PHE A 1  444  ? 139.084 135.930 108.231 1.00 7.54   ? 444  PHE A CD1   1 
ATOM   3313  C  CD2   . PHE A 1  444  ? 138.192 135.037 110.238 1.00 12.95  ? 444  PHE A CD2   1 
ATOM   3314  C  CE1   . PHE A 1  444  ? 140.291 135.351 108.518 1.00 0.21   ? 444  PHE A CE1   1 
ATOM   3315  C  CE2   . PHE A 1  444  ? 139.399 134.459 110.517 1.00 1.12   ? 444  PHE A CE2   1 
ATOM   3316  C  CZ    . PHE A 1  444  ? 140.447 134.620 109.657 1.00 3.45   ? 444  PHE A CZ    1 
ATOM   3317  N  N     . GLN A 1  445  ? 134.889 137.796 106.161 1.00 15.45  ? 445  GLN A N     1 
ATOM   3318  C  CA    . GLN A 1  445  ? 133.601 138.297 105.717 1.00 2.80   ? 445  GLN A CA    1 
ATOM   3319  C  C     . GLN A 1  445  ? 132.636 137.149 105.460 1.00 3.15   ? 445  GLN A C     1 
ATOM   3320  O  O     . GLN A 1  445  ? 133.037 136.083 104.999 1.00 2.65   ? 445  GLN A O     1 
ATOM   3321  C  CB    . GLN A 1  445  ? 133.773 139.157 104.476 1.00 13.85  ? 445  GLN A CB    1 
ATOM   3322  C  CG    . GLN A 1  445  ? 134.592 140.380 104.776 1.00 4.84   ? 445  GLN A CG    1 
ATOM   3323  C  CD    . GLN A 1  445  ? 134.701 141.325 103.630 1.00 0.01   ? 445  GLN A CD    1 
ATOM   3324  O  OE1   . GLN A 1  445  ? 134.148 141.095 102.571 1.00 1.41   ? 445  GLN A OE1   1 
ATOM   3325  N  NE2   . GLN A 1  445  ? 135.428 142.401 103.830 1.00 2.09   ? 445  GLN A NE2   1 
ATOM   3326  N  N     . MET A 1  446  ? 131.365 137.361 105.791 1.00 5.08   ? 446  MET A N     1 
ATOM   3327  C  CA    . MET A 1  446  ? 130.352 136.339 105.603 1.00 2.66   ? 446  MET A CA    1 
ATOM   3328  C  C     . MET A 1  446  ? 129.004 136.991 105.353 1.00 15.77  ? 446  MET A C     1 
ATOM   3329  O  O     . MET A 1  446  ? 128.828 138.190 105.535 1.00 5.76   ? 446  MET A O     1 
ATOM   3330  C  CB    . MET A 1  446  ? 130.253 135.390 106.800 1.00 1.84   ? 446  MET A CB    1 
ATOM   3331  C  CG    . MET A 1  446  ? 129.986 136.040 108.138 1.00 15.36  ? 446  MET A CG    1 
ATOM   3332  S  SD    . MET A 1  446  ? 129.145 134.879 109.226 1.00 18.85  ? 446  MET A SD    1 
ATOM   3333  C  CE    . MET A 1  446  ? 129.889 135.226 110.789 1.00 7.37   ? 446  MET A CE    1 
ATOM   3334  N  N     . ASN A 1  447  ? 128.062 136.178 104.900 1.00 15.01  ? 447  ASN A N     1 
ATOM   3335  C  CA    . ASN A 1  447  ? 126.690 136.614 104.720 1.00 4.62   ? 447  ASN A CA    1 
ATOM   3336  C  C     . ASN A 1  447  ? 125.981 136.744 106.061 1.00 2.30   ? 447  ASN A C     1 
ATOM   3337  O  O     . ASN A 1  447  ? 126.221 135.981 106.993 1.00 10.69  ? 447  ASN A O     1 
ATOM   3338  C  CB    . ASN A 1  447  ? 125.964 135.638 103.805 1.00 2.26   ? 447  ASN A CB    1 
ATOM   3339  C  CG    . ASN A 1  447  ? 124.796 136.255 103.103 1.00 5.80   ? 447  ASN A CG    1 
ATOM   3340  O  OD1   . ASN A 1  447  ? 123.926 136.829 103.725 1.00 3.51   ? 447  ASN A OD1   1 
ATOM   3341  N  ND2   . ASN A 1  447  ? 124.812 136.211 101.791 1.00 5.53   ? 447  ASN A ND2   1 
ATOM   3342  N  N     . VAL A 1  448  ? 125.105 137.744 106.152 1.00 2.56   ? 448  VAL A N     1 
ATOM   3343  C  CA    . VAL A 1  448  ? 124.418 138.042 107.403 1.00 13.35  ? 448  VAL A CA    1 
ATOM   3344  C  C     . VAL A 1  448  ? 123.483 136.910 107.810 1.00 4.78   ? 448  VAL A C     1 
ATOM   3345  O  O     . VAL A 1  448  ? 123.183 136.740 108.994 1.00 1.98   ? 448  VAL A O     1 
ATOM   3346  C  CB    . VAL A 1  448  ? 123.677 139.389 107.275 1.00 6.45   ? 448  VAL A CB    1 
ATOM   3347  C  CG1   . VAL A 1  448  ? 122.401 139.241 106.482 1.00 0.55   ? 448  VAL A CG1   1 
ATOM   3348  C  CG2   . VAL A 1  448  ? 123.411 139.983 108.624 1.00 0.53   ? 448  VAL A CG2   1 
ATOM   3349  N  N     . SER A 1  449  ? 122.998 136.127 106.853 1.00 4.40   ? 449  SER A N     1 
ATOM   3350  C  CA    . SER A 1  449  ? 122.121 135.016 107.170 1.00 5.86   ? 449  SER A CA    1 
ATOM   3351  C  C     . SER A 1  449  ? 122.868 133.798 107.686 1.00 9.75   ? 449  SER A C     1 
ATOM   3352  O  O     . SER A 1  449  ? 122.225 132.847 108.127 1.00 15.83  ? 449  SER A O     1 
ATOM   3353  C  CB    . SER A 1  449  ? 121.291 134.641 105.952 1.00 1.00   ? 449  SER A CB    1 
ATOM   3354  O  OG    . SER A 1  449  ? 120.384 135.669 105.629 1.00 11.92  ? 449  SER A OG    1 
ATOM   3355  N  N     . ALA A 1  450  ? 124.193 133.804 107.646 1.00 10.98  ? 450  ALA A N     1 
ATOM   3356  C  CA    . ALA A 1  450  ? 124.997 132.752 108.241 1.00 0.74   ? 450  ALA A CA    1 
ATOM   3357  C  C     . ALA A 1  450  ? 125.294 132.984 109.714 1.00 12.81  ? 450  ALA A C     1 
ATOM   3358  O  O     . ALA A 1  450  ? 125.823 132.088 110.366 1.00 10.57  ? 450  ALA A O     1 
ATOM   3359  C  CB    . ALA A 1  450  ? 126.309 132.605 107.479 1.00 9.38   ? 450  ALA A CB    1 
ATOM   3360  N  N     . CYS A 1  451  ? 124.963 134.150 110.259 1.00 5.30   ? 451  CYS A N     1 
ATOM   3361  C  CA    . CYS A 1  451  ? 125.270 134.462 111.647 1.00 0.71   ? 451  CYS A CA    1 
ATOM   3362  C  C     . CYS A 1  451  ? 124.454 133.654 112.638 1.00 14.01  ? 451  CYS A C     1 
ATOM   3363  O  O     . CYS A 1  451  ? 124.846 133.573 113.800 1.00 7.64   ? 451  CYS A O     1 
ATOM   3364  C  CB    . CYS A 1  451  ? 125.051 135.950 111.920 1.00 5.09   ? 451  CYS A CB    1 
ATOM   3365  S  SG    . CYS A 1  451  ? 126.127 137.077 111.058 1.00 5.16   ? 451  CYS A SG    1 
ATOM   3366  N  N     . ALA A 1  452  ? 123.335 133.070 112.215 1.00 5.01   ? 452  ALA A N     1 
ATOM   3367  C  CA    . ALA A 1  452  ? 122.513 132.267 113.113 1.00 13.90  ? 452  ALA A CA    1 
ATOM   3368  C  C     . ALA A 1  452  ? 123.187 130.955 113.491 1.00 7.70   ? 452  ALA A C     1 
ATOM   3369  O  O     . ALA A 1  452  ? 122.860 130.372 114.528 1.00 11.33  ? 452  ALA A O     1 
ATOM   3370  C  CB    . ALA A 1  452  ? 121.161 131.995 112.467 1.00 4.44   ? 452  ALA A CB    1 
ATOM   3371  N  N     . TRP A 1  453  ? 124.108 130.467 112.664 1.00 15.21  ? 453  TRP A N     1 
ATOM   3372  C  CA    . TRP A 1  453  ? 124.819 129.236 112.980 1.00 2.18   ? 453  TRP A CA    1 
ATOM   3373  C  C     . TRP A 1  453  ? 125.756 129.427 114.152 1.00 5.68   ? 453  TRP A C     1 
ATOM   3374  O  O     . TRP A 1  453  ? 125.972 128.507 114.944 1.00 13.48  ? 453  TRP A O     1 
ATOM   3375  C  CB    . TRP A 1  453  ? 125.599 128.762 111.764 1.00 12.25  ? 453  TRP A CB    1 
ATOM   3376  C  CG    . TRP A 1  453  ? 124.788 128.052 110.771 1.00 14.61  ? 453  TRP A CG    1 
ATOM   3377  C  CD1   . TRP A 1  453  ? 123.851 127.114 111.016 1.00 9.27   ? 453  TRP A CD1   1 
ATOM   3378  C  CD2   . TRP A 1  453  ? 124.837 128.213 109.357 1.00 16.20  ? 453  TRP A CD2   1 
ATOM   3379  N  NE1   . TRP A 1  453  ? 123.307 126.676 109.855 1.00 1.06   ? 453  TRP A NE1   1 
ATOM   3380  C  CE2   . TRP A 1  453  ? 123.898 127.333 108.812 1.00 12.68  ? 453  TRP A CE2   1 
ATOM   3381  C  CE3   . TRP A 1  453  ? 125.585 129.016 108.498 1.00 11.02  ? 453  TRP A CE3   1 
ATOM   3382  C  CZ2   . TRP A 1  453  ? 123.678 127.235 107.448 1.00 15.80  ? 453  TRP A CZ2   1 
ATOM   3383  C  CZ3   . TRP A 1  453  ? 125.363 128.919 107.157 1.00 9.71   ? 453  TRP A CZ3   1 
ATOM   3384  C  CH2   . TRP A 1  453  ? 124.420 128.040 106.640 1.00 17.55  ? 453  TRP A CH2   1 
ATOM   3385  N  N     . TYR A 1  454  ? 126.320 130.615 114.277 1.00 10.13  ? 454  TYR A N     1 
ATOM   3386  C  CA    . TYR A 1  454  ? 127.362 130.905 115.238 1.00 3.02   ? 454  TYR A CA    1 
ATOM   3387  C  C     . TYR A 1  454  ? 126.906 131.840 116.333 1.00 2.77   ? 454  TYR A C     1 
ATOM   3388  O  O     . TYR A 1  454  ? 127.672 132.094 117.259 1.00 9.24   ? 454  TYR A O     1 
ATOM   3389  C  CB    . TYR A 1  454  ? 128.569 131.497 114.517 1.00 2.64   ? 454  TYR A CB    1 
ATOM   3390  C  CG    . TYR A 1  454  ? 128.989 130.691 113.320 1.00 4.13   ? 454  TYR A CG    1 
ATOM   3391  C  CD1   . TYR A 1  454  ? 129.768 129.559 113.472 1.00 0.05   ? 454  TYR A CD1   1 
ATOM   3392  C  CD2   . TYR A 1  454  ? 128.601 131.047 112.043 1.00 0.86   ? 454  TYR A CD2   1 
ATOM   3393  C  CE1   . TYR A 1  454  ? 130.146 128.821 112.399 1.00 8.10   ? 454  TYR A CE1   1 
ATOM   3394  C  CE2   . TYR A 1  454  ? 128.984 130.305 110.967 1.00 1.20   ? 454  TYR A CE2   1 
ATOM   3395  C  CZ    . TYR A 1  454  ? 129.759 129.193 111.158 1.00 8.25   ? 454  TYR A CZ    1 
ATOM   3396  O  OH    . TYR A 1  454  ? 130.153 128.433 110.097 1.00 3.77   ? 454  TYR A OH    1 
ATOM   3397  N  N     . ASN A 1  455  ? 125.679 132.343 116.257 1.00 2.76   ? 455  ASN A N     1 
ATOM   3398  C  CA    . ASN A 1  455  ? 125.161 133.299 117.228 1.00 2.00   ? 455  ASN A CA    1 
ATOM   3399  C  C     . ASN A 1  455  ? 126.043 134.542 117.285 1.00 3.82   ? 455  ASN A C     1 
ATOM   3400  O  O     . ASN A 1  455  ? 126.469 134.983 118.350 1.00 10.55  ? 455  ASN A O     1 
ATOM   3401  C  CB    . ASN A 1  455  ? 125.026 132.652 118.601 1.00 4.86   ? 455  ASN A CB    1 
ATOM   3402  C  CG    . ASN A 1  455  ? 124.201 133.468 119.547 1.00 9.50   ? 455  ASN A CG    1 
ATOM   3403  O  OD1   . ASN A 1  455  ? 124.336 133.348 120.755 1.00 12.96  ? 455  ASN A OD1   1 
ATOM   3404  N  ND2   . ASN A 1  455  ? 123.325 134.296 119.006 1.00 15.90  ? 455  ASN A ND2   1 
ATOM   3405  N  N     . ALA A 1  456  ? 126.313 135.114 116.121 1.00 0.79   ? 456  ALA A N     1 
ATOM   3406  C  CA    . ALA A 1  456  ? 127.289 136.177 115.964 1.00 2.59   ? 456  ALA A CA    1 
ATOM   3407  C  C     . ALA A 1  456  ? 126.644 137.428 115.384 1.00 11.05  ? 456  ALA A C     1 
ATOM   3408  O  O     . ALA A 1  456  ? 125.511 137.405 114.903 1.00 20.67  ? 456  ALA A O     1 
ATOM   3409  C  CB    . ALA A 1  456  ? 128.435 135.720 115.063 1.00 6.11   ? 456  ALA A CB    1 
ATOM   3410  N  N     . ASP A 1  457  ? 127.373 138.538 115.472 1.00 4.21   ? 457  ASP A N     1 
ATOM   3411  C  CA    . ASP A 1  457  ? 127.013 139.766 114.783 1.00 5.29   ? 457  ASP A CA    1 
ATOM   3412  C  C     . ASP A 1  457  ? 128.286 140.555 114.525 1.00 9.99   ? 457  ASP A C     1 
ATOM   3413  O  O     . ASP A 1  457  ? 129.394 140.048 114.696 1.00 16.09  ? 457  ASP A O     1 
ATOM   3414  C  CB    . ASP A 1  457  ? 125.971 140.569 115.565 1.00 12.98  ? 457  ASP A CB    1 
ATOM   3415  C  CG    . ASP A 1  457  ? 126.454 141.007 116.917 1.00 16.51  ? 457  ASP A CG    1 
ATOM   3416  O  OD1   . ASP A 1  457  ? 127.285 140.312 117.525 1.00 13.43  ? 457  ASP A OD1   1 
ATOM   3417  O  OD2   . ASP A 1  457  ? 125.969 142.048 117.386 1.00 21.92  ? 457  ASP A OD2   1 
ATOM   3418  N  N     . PHE A 1  458  ? 128.135 141.800 114.098 1.00 12.61  ? 458  PHE A N     1 
ATOM   3419  C  CA    . PHE A 1  458  ? 129.244 142.570 113.556 1.00 6.06   ? 458  PHE A CA    1 
ATOM   3420  C  C     . PHE A 1  458  ? 129.562 143.808 114.384 1.00 12.11  ? 458  PHE A C     1 
ATOM   3421  O  O     . PHE A 1  458  ? 129.785 144.888 113.844 1.00 9.29   ? 458  PHE A O     1 
ATOM   3422  C  CB    . PHE A 1  458  ? 128.972 142.959 112.109 1.00 13.65  ? 458  PHE A CB    1 
ATOM   3423  C  CG    . PHE A 1  458  ? 128.532 141.819 111.248 1.00 4.20   ? 458  PHE A CG    1 
ATOM   3424  C  CD1   . PHE A 1  458  ? 129.214 140.618 111.264 1.00 2.18   ? 458  PHE A CD1   1 
ATOM   3425  C  CD2   . PHE A 1  458  ? 127.450 141.954 110.411 1.00 3.16   ? 458  PHE A CD2   1 
ATOM   3426  C  CE1   . PHE A 1  458  ? 128.814 139.579 110.471 1.00 1.18   ? 458  PHE A CE1   1 
ATOM   3427  C  CE2   . PHE A 1  458  ? 127.048 140.920 109.612 1.00 5.18   ? 458  PHE A CE2   1 
ATOM   3428  C  CZ    . PHE A 1  458  ? 127.731 139.729 109.639 1.00 3.57   ? 458  PHE A CZ    1 
ATOM   3429  N  N     . ASP A 1  459  ? 129.608 143.670 115.703 1.00 13.57  ? 459  ASP A N     1 
ATOM   3430  C  CA    . ASP A 1  459  ? 130.073 144.754 116.553 1.00 7.60   ? 459  ASP A CA    1 
ATOM   3431  C  C     . ASP A 1  459  ? 131.440 144.482 117.168 1.00 13.96  ? 459  ASP A C     1 
ATOM   3432  O  O     . ASP A 1  459  ? 131.789 145.110 118.165 1.00 24.28  ? 459  ASP A O     1 
ATOM   3433  C  CB    . ASP A 1  459  ? 129.058 145.051 117.654 1.00 13.08  ? 459  ASP A CB    1 
ATOM   3434  C  CG    . ASP A 1  459  ? 128.755 143.856 118.509 1.00 20.55  ? 459  ASP A CG    1 
ATOM   3435  O  OD1   . ASP A 1  459  ? 129.173 142.737 118.157 1.00 24.76  ? 459  ASP A OD1   1 
ATOM   3436  O  OD2   . ASP A 1  459  ? 128.104 144.039 119.552 1.00 20.50  ? 459  ASP A OD2   1 
ATOM   3437  N  N     . GLY A 1  460  ? 132.213 143.560 116.610 1.00 20.02  ? 460  GLY A N     1 
ATOM   3438  C  CA    . GLY A 1  460  ? 133.567 143.342 117.072 1.00 11.51  ? 460  GLY A CA    1 
ATOM   3439  C  C     . GLY A 1  460  ? 133.882 141.907 117.425 1.00 14.30  ? 460  GLY A C     1 
ATOM   3440  O  O     . GLY A 1  460  ? 134.882 141.639 118.090 1.00 18.12  ? 460  GLY A O     1 
ATOM   3441  N  N     . ASP A 1  461  ? 133.044 140.975 116.985 1.00 13.30  ? 461  ASP A N     1 
ATOM   3442  C  CA    . ASP A 1  461  ? 133.289 139.568 117.252 1.00 0.42   ? 461  ASP A CA    1 
ATOM   3443  C  C     . ASP A 1  461  ? 134.451 139.059 116.416 1.00 2.33   ? 461  ASP A C     1 
ATOM   3444  O  O     . ASP A 1  461  ? 134.730 139.561 115.329 1.00 5.27   ? 461  ASP A O     1 
ATOM   3445  C  CB    . ASP A 1  461  ? 132.052 138.730 116.952 1.00 1.92   ? 461  ASP A CB    1 
ATOM   3446  C  CG    . ASP A 1  461  ? 130.826 139.239 117.637 1.00 11.72  ? 461  ASP A CG    1 
ATOM   3447  O  OD1   . ASP A 1  461  ? 130.920 140.239 118.362 1.00 18.61  ? 461  ASP A OD1   1 
ATOM   3448  O  OD2   . ASP A 1  461  ? 129.760 138.624 117.471 1.00 16.10  ? 461  ASP A OD2   1 
ATOM   3449  N  N     . GLN A 1  462  ? 135.132 138.050 116.941 1.00 4.34   ? 462  GLN A N     1 
ATOM   3450  C  CA    . GLN A 1  462  ? 136.227 137.392 116.256 1.00 0.44   ? 462  GLN A CA    1 
ATOM   3451  C  C     . GLN A 1  462  ? 135.922 135.912 116.120 1.00 2.20   ? 462  GLN A C     1 
ATOM   3452  O  O     . GLN A 1  462  ? 135.365 135.293 117.024 1.00 10.78  ? 462  GLN A O     1 
ATOM   3453  C  CB    . GLN A 1  462  ? 137.536 137.576 117.002 1.00 1.82   ? 462  GLN A CB    1 
ATOM   3454  C  CG    . GLN A 1  462  ? 137.955 139.007 117.147 1.00 1.15   ? 462  GLN A CG    1 
ATOM   3455  C  CD    . GLN A 1  462  ? 139.406 139.142 117.459 1.00 4.09   ? 462  GLN A CD    1 
ATOM   3456  O  OE1   . GLN A 1  462  ? 140.252 139.062 116.579 1.00 6.75   ? 462  GLN A OE1   1 
ATOM   3457  N  NE2   . GLN A 1  462  ? 139.715 139.335 118.723 1.00 9.21   ? 462  GLN A NE2   1 
ATOM   3458  N  N     . MET A 1  463  ? 136.299 135.349 114.984 1.00 8.26   ? 463  MET A N     1 
ATOM   3459  C  CA    . MET A 1  463  ? 136.074 133.943 114.710 1.00 4.00   ? 463  MET A CA    1 
ATOM   3460  C  C     . MET A 1  463  ? 137.387 133.336 114.251 1.00 13.83  ? 463  MET A C     1 
ATOM   3461  O  O     . MET A 1  463  ? 138.249 134.029 113.717 1.00 0.92   ? 463  MET A O     1 
ATOM   3462  C  CB    . MET A 1  463  ? 134.969 133.761 113.659 1.00 1.77   ? 463  MET A CB    1 
ATOM   3463  C  CG    . MET A 1  463  ? 133.570 134.087 114.179 1.00 0.33   ? 463  MET A CG    1 
ATOM   3464  S  SD    . MET A 1  463  ? 132.209 133.695 113.080 1.00 15.56  ? 463  MET A SD    1 
ATOM   3465  C  CE    . MET A 1  463  ? 132.401 131.942 112.888 1.00 4.85   ? 463  MET A CE    1 
ATOM   3466  N  N     . ASN A 1  464  ? 137.543 132.043 114.492 1.00 12.54  ? 464  ASN A N     1 
ATOM   3467  C  CA    . ASN A 1  464  ? 138.711 131.296 114.059 1.00 10.48  ? 464  ASN A CA    1 
ATOM   3468  C  C     . ASN A 1  464  ? 138.467 130.660 112.707 1.00 8.24   ? 464  ASN A C     1 
ATOM   3469  O  O     . ASN A 1  464  ? 137.334 130.376 112.329 1.00 16.71  ? 464  ASN A O     1 
ATOM   3470  C  CB    . ASN A 1  464  ? 139.063 130.202 115.058 1.00 15.95  ? 464  ASN A CB    1 
ATOM   3471  C  CG    . ASN A 1  464  ? 139.632 130.739 116.323 1.00 16.17  ? 464  ASN A CG    1 
ATOM   3472  O  OD1   . ASN A 1  464  ? 140.611 131.462 116.321 1.00 20.89  ? 464  ASN A OD1   1 
ATOM   3473  N  ND2   . ASN A 1  464  ? 139.011 130.396 117.424 1.00 23.90  ? 464  ASN A ND2   1 
ATOM   3474  N  N     . LEU A 1  465  ? 139.550 130.404 111.991 1.00 2.78   ? 465  LEU A N     1 
ATOM   3475  C  CA    . LEU A 1  465  ? 139.453 129.770 110.689 1.00 1.57   ? 465  LEU A CA    1 
ATOM   3476  C  C     . LEU A 1  465  ? 140.714 128.966 110.431 1.00 11.55  ? 465  LEU A C     1 
ATOM   3477  O  O     . LEU A 1  465  ? 141.815 129.505 110.505 1.00 2.48   ? 465  LEU A O     1 
ATOM   3478  C  CB    . LEU A 1  465  ? 139.242 130.822 109.594 1.00 2.17   ? 465  LEU A CB    1 
ATOM   3479  C  CG    . LEU A 1  465  ? 138.648 130.397 108.259 1.00 10.71  ? 465  LEU A CG    1 
ATOM   3480  C  CD1   . LEU A 1  465  ? 137.842 131.526 107.727 1.00 2.85   ? 465  LEU A CD1   1 
ATOM   3481  C  CD2   . LEU A 1  465  ? 139.741 130.022 107.278 1.00 10.01  ? 465  LEU A CD2   1 
ATOM   3482  N  N     . TRP A 1  466  ? 140.559 127.692 110.121 1.00 15.22  ? 466  TRP A N     1 
ATOM   3483  C  CA    . TRP A 1  466  ? 141.678 126.894 109.655 1.00 4.10   ? 466  TRP A CA    1 
ATOM   3484  C  C     . TRP A 1  466  ? 141.276 126.164 108.390 1.00 7.26   ? 466  TRP A C     1 
ATOM   3485  O  O     . TRP A 1  466  ? 140.108 125.837 108.197 1.00 12.30  ? 466  TRP A O     1 
ATOM   3486  C  CB    . TRP A 1  466  ? 142.181 125.920 110.729 1.00 4.58   ? 466  TRP A CB    1 
ATOM   3487  C  CG    . TRP A 1  466  ? 141.361 124.705 111.006 1.00 9.50   ? 466  TRP A CG    1 
ATOM   3488  C  CD1   . TRP A 1  466  ? 141.447 123.511 110.379 1.00 3.06   ? 466  TRP A CD1   1 
ATOM   3489  C  CD2   . TRP A 1  466  ? 140.367 124.555 112.015 1.00 7.64   ? 466  TRP A CD2   1 
ATOM   3490  N  NE1   . TRP A 1  466  ? 140.564 122.631 110.913 1.00 3.97   ? 466  TRP A NE1   1 
ATOM   3491  C  CE2   . TRP A 1  466  ? 139.880 123.247 111.923 1.00 6.70   ? 466  TRP A CE2   1 
ATOM   3492  C  CE3   . TRP A 1  466  ? 139.826 125.409 112.975 1.00 5.44   ? 466  TRP A CE3   1 
ATOM   3493  C  CZ2   . TRP A 1  466  ? 138.888 122.761 112.763 1.00 1.82   ? 466  TRP A CZ2   1 
ATOM   3494  C  CZ3   . TRP A 1  466  ? 138.843 124.933 113.802 1.00 14.71  ? 466  TRP A CZ3   1 
ATOM   3495  C  CH2   . TRP A 1  466  ? 138.381 123.620 113.693 1.00 1.35   ? 466  TRP A CH2   1 
ATOM   3496  N  N     . VAL A 1  467  ? 142.240 125.971 107.504 1.00 13.58  ? 467  VAL A N     1 
ATOM   3497  C  CA    . VAL A 1  467  ? 142.018 125.357 106.200 1.00 11.87  ? 467  VAL A CA    1 
ATOM   3498  C  C     . VAL A 1  467  ? 142.589 123.945 106.247 1.00 12.79  ? 467  VAL A C     1 
ATOM   3499  O  O     . VAL A 1  467  ? 143.783 123.789 106.524 1.00 24.81  ? 467  VAL A O     1 
ATOM   3500  C  CB    . VAL A 1  467  ? 142.669 126.177 105.074 1.00 13.54  ? 467  VAL A CB    1 
ATOM   3501  C  CG1   . VAL A 1  467  ? 142.332 125.600 103.735 1.00 18.33  ? 467  VAL A CG1   1 
ATOM   3502  C  CG2   . VAL A 1  467  ? 142.242 127.619 105.136 1.00 9.33   ? 467  VAL A CG2   1 
ATOM   3503  N  N     . PRO A 1  468  ? 141.787 122.908 106.028 1.00 6.80   ? 468  PRO A N     1 
ATOM   3504  C  CA    . PRO A 1  468  ? 142.338 121.550 105.941 1.00 2.61   ? 468  PRO A CA    1 
ATOM   3505  C  C     . PRO A 1  468  ? 143.352 121.416 104.815 1.00 0.99   ? 468  PRO A C     1 
ATOM   3506  O  O     . PRO A 1  468  ? 143.101 121.814 103.681 1.00 7.16   ? 468  PRO A O     1 
ATOM   3507  C  CB    . PRO A 1  468  ? 141.099 120.689 105.684 1.00 5.66   ? 468  PRO A CB    1 
ATOM   3508  C  CG    . PRO A 1  468  ? 139.988 121.484 106.191 1.00 0.15   ? 468  PRO A CG    1 
ATOM   3509  C  CD    . PRO A 1  468  ? 140.320 122.907 105.992 1.00 0.95   ? 468  PRO A CD    1 
ATOM   3510  N  N     . TRP A 1  469  ? 144.503 120.834 105.135 1.00 2.58   ? 469  TRP A N     1 
ATOM   3511  C  CA    . TRP A 1  469  ? 145.537 120.583 104.143 1.00 11.90  ? 469  TRP A CA    1 
ATOM   3512  C  C     . TRP A 1  469  ? 145.644 119.121 103.761 1.00 8.39   ? 469  TRP A C     1 
ATOM   3513  O  O     . TRP A 1  469  ? 146.118 118.812 102.668 1.00 2.96   ? 469  TRP A O     1 
ATOM   3514  C  CB    . TRP A 1  469  ? 146.899 121.070 104.639 1.00 1.48   ? 469  TRP A CB    1 
ATOM   3515  C  CG    . TRP A 1  469  ? 147.240 120.688 106.034 1.00 6.36   ? 469  TRP A CG    1 
ATOM   3516  C  CD1   . TRP A 1  469  ? 147.029 121.417 107.152 1.00 10.93  ? 469  TRP A CD1   1 
ATOM   3517  C  CD2   . TRP A 1  469  ? 147.871 119.476 106.460 1.00 1.60   ? 469  TRP A CD2   1 
ATOM   3518  N  NE1   . TRP A 1  469  ? 147.473 120.740 108.251 1.00 15.29  ? 469  TRP A NE1   1 
ATOM   3519  C  CE2   . TRP A 1  469  ? 147.995 119.541 107.852 1.00 3.06   ? 469  TRP A CE2   1 
ATOM   3520  C  CE3   . TRP A 1  469  ? 148.330 118.339 105.796 1.00 13.68  ? 469  TRP A CE3   1 
ATOM   3521  C  CZ2   . TRP A 1  469  ? 148.558 118.516 108.594 1.00 1.00   ? 469  TRP A CZ2   1 
ATOM   3522  C  CZ3   . TRP A 1  469  ? 148.882 117.333 106.526 1.00 15.01  ? 469  TRP A CZ3   1 
ATOM   3523  C  CH2   . TRP A 1  469  ? 148.996 117.423 107.910 1.00 0.54   ? 469  TRP A CH2   1 
ATOM   3524  N  N     . SER A 1  470  ? 145.205 118.224 104.631 1.00 3.82   ? 470  SER A N     1 
ATOM   3525  C  CA    . SER A 1  470  ? 145.250 116.796 104.375 1.00 2.30   ? 470  SER A CA    1 
ATOM   3526  C  C     . SER A 1  470  ? 144.080 116.368 103.495 1.00 2.55   ? 470  SER A C     1 
ATOM   3527  O  O     . SER A 1  470  ? 143.007 116.964 103.529 1.00 1.92   ? 470  SER A O     1 
ATOM   3528  C  CB    . SER A 1  470  ? 145.230 116.051 105.706 1.00 3.18   ? 470  SER A CB    1 
ATOM   3529  O  OG    . SER A 1  470  ? 145.268 114.657 105.523 1.00 13.34  ? 470  SER A OG    1 
ATOM   3530  N  N     . VAL A 1  471  ? 144.295 115.321 102.698 1.00 1.18   ? 471  VAL A N     1 
ATOM   3531  C  CA    . VAL A 1  471  ? 143.242 114.821 101.816 1.00 0.32   ? 471  VAL A CA    1 
ATOM   3532  C  C     . VAL A 1  471  ? 142.104 114.208 102.618 1.00 1.65   ? 471  VAL A C     1 
ATOM   3533  O  O     . VAL A 1  471  ? 140.931 114.384 102.284 1.00 7.65   ? 471  VAL A O     1 
ATOM   3534  C  CB    . VAL A 1  471  ? 143.822 113.816 100.803 1.00 2.50   ? 471  VAL A CB    1 
ATOM   3535  C  CG1   . VAL A 1  471  ? 142.744 113.262 99.927  1.00 5.74   ? 471  VAL A CG1   1 
ATOM   3536  C  CG2   . VAL A 1  471  ? 144.843 114.482 99.941  1.00 3.16   ? 471  VAL A CG2   1 
ATOM   3537  N  N     . MET A 1  472  ? 142.429 113.457 103.670 1.00 8.86   ? 472  MET A N     1 
ATOM   3538  C  CA    . MET A 1  472  ? 141.401 112.830 104.491 1.00 7.10   ? 472  MET A CA    1 
ATOM   3539  C  C     . MET A 1  472  ? 140.593 113.858 105.264 1.00 13.49  ? 472  MET A C     1 
ATOM   3540  O  O     . MET A 1  472  ? 139.383 113.698 105.437 1.00 0.82   ? 472  MET A O     1 
ATOM   3541  C  CB    . MET A 1  472  ? 142.031 111.827 105.448 1.00 12.74  ? 472  MET A CB    1 
ATOM   3542  C  CG    . MET A 1  472  ? 142.329 110.502 104.821 1.00 13.64  ? 472  MET A CG    1 
ATOM   3543  S  SD    . MET A 1  472  ? 142.330 109.187 106.030 1.00 14.91  ? 472  MET A SD    1 
ATOM   3544  C  CE    . MET A 1  472  ? 143.114 107.897 105.111 1.00 4.29   ? 472  MET A CE    1 
ATOM   3545  N  N     . SER A 1  473  ? 141.242 114.905 105.759 1.00 0.63   ? 473  SER A N     1 
ATOM   3546  C  CA    . SER A 1  473  ? 140.516 115.934 106.486 1.00 12.00  ? 473  SER A CA    1 
ATOM   3547  C  C     . SER A 1  473  ? 139.721 116.825 105.545 1.00 9.00   ? 473  SER A C     1 
ATOM   3548  O  O     . SER A 1  473  ? 138.731 117.430 105.955 1.00 5.90   ? 473  SER A O     1 
ATOM   3549  C  CB    . SER A 1  473  ? 141.486 116.754 107.320 1.00 1.87   ? 473  SER A CB    1 
ATOM   3550  O  OG    . SER A 1  473  ? 140.796 117.723 108.077 1.00 6.76   ? 473  SER A OG    1 
ATOM   3551  N  N     . ARG A 1  474  ? 140.145 116.916 104.289 1.00 7.35   ? 474  ARG A N     1 
ATOM   3552  C  CA    . ARG A 1  474  ? 139.458 117.709 103.284 1.00 9.13   ? 474  ARG A CA    1 
ATOM   3553  C  C     . ARG A 1  474  ? 138.223 117.006 102.752 1.00 1.93   ? 474  ARG A C     1 
ATOM   3554  O  O     . ARG A 1  474  ? 137.242 117.665 102.406 1.00 4.42   ? 474  ARG A O     1 
ATOM   3555  C  CB    . ARG A 1  474  ? 140.409 118.001 102.133 1.00 3.40   ? 474  ARG A CB    1 
ATOM   3556  C  CG    . ARG A 1  474  ? 140.966 119.372 102.142 1.00 3.24   ? 474  ARG A CG    1 
ATOM   3557  C  CD    . ARG A 1  474  ? 142.328 119.414 101.514 1.00 2.51   ? 474  ARG A CD    1 
ATOM   3558  N  NE    . ARG A 1  474  ? 142.222 119.513 100.069 1.00 2.70   ? 474  ARG A NE    1 
ATOM   3559  C  CZ    . ARG A 1  474  ? 143.006 118.889 99.207  1.00 4.17   ? 474  ARG A CZ    1 
ATOM   3560  N  NH1   . ARG A 1  474  ? 144.001 118.118 99.608  1.00 2.54   ? 474  ARG A NH1   1 
ATOM   3561  N  NH2   . ARG A 1  474  ? 142.791 119.053 97.908  1.00 10.75  ? 474  ARG A NH2   1 
ATOM   3562  N  N     . VAL A 1  475  ? 138.270 115.682 102.635 1.00 2.85   ? 475  VAL A N     1 
ATOM   3563  C  CA    . VAL A 1  475  ? 137.109 114.934 102.174 1.00 1.91   ? 475  VAL A CA    1 
ATOM   3564  C  C     . VAL A 1  475  ? 135.979 115.038 103.183 1.00 14.82  ? 475  VAL A C     1 
ATOM   3565  O  O     . VAL A 1  475  ? 134.829 115.312 102.832 1.00 5.84   ? 475  VAL A O     1 
ATOM   3566  C  CB    . VAL A 1  475  ? 137.482 113.466 101.916 1.00 3.48   ? 475  VAL A CB    1 
ATOM   3567  C  CG1   . VAL A 1  475  ? 136.243 112.618 101.924 1.00 2.88   ? 475  VAL A CG1   1 
ATOM   3568  C  CG2   . VAL A 1  475  ? 138.205 113.321 100.613 1.00 11.18  ? 475  VAL A CG2   1 
ATOM   3569  N  N     . GLU A 1  476  ? 136.288 114.833 104.455 1.00 2.03   ? 476  GLU A N     1 
ATOM   3570  C  CA    . GLU A 1  476  ? 135.239 114.823 105.451 1.00 9.55   ? 476  GLU A CA    1 
ATOM   3571  C  C     . GLU A 1  476  ? 134.765 116.215 105.822 1.00 3.79   ? 476  GLU A C     1 
ATOM   3572  O  O     . GLU A 1  476  ? 133.662 116.352 106.344 1.00 6.72   ? 476  GLU A O     1 
ATOM   3573  C  CB    . GLU A 1  476  ? 135.708 114.070 106.682 1.00 3.28   ? 476  GLU A CB    1 
ATOM   3574  C  CG    . GLU A 1  476  ? 136.441 114.899 107.639 1.00 4.12   ? 476  GLU A CG    1 
ATOM   3575  C  CD    . GLU A 1  476  ? 136.398 114.321 109.009 1.00 3.63   ? 476  GLU A CD    1 
ATOM   3576  O  OE1   . GLU A 1  476  ? 135.790 113.259 109.185 1.00 7.89   ? 476  GLU A OE1   1 
ATOM   3577  O  OE2   . GLU A 1  476  ? 136.971 114.935 109.914 1.00 14.65  ? 476  GLU A OE2   1 
ATOM   3578  N  N     . ALA A 1  477  ? 135.554 117.251 105.558 1.00 3.30   ? 477  ALA A N     1 
ATOM   3579  C  CA    . ALA A 1  477  ? 135.050 118.609 105.710 1.00 15.32  ? 477  ALA A CA    1 
ATOM   3580  C  C     . ALA A 1  477  ? 133.925 118.883 104.728 1.00 0.52   ? 477  ALA A C     1 
ATOM   3581  O  O     . ALA A 1  477  ? 132.898 119.455 105.089 1.00 13.88  ? 477  ALA A O     1 
ATOM   3582  C  CB    . ALA A 1  477  ? 136.184 119.609 105.519 1.00 2.09   ? 477  ALA A CB    1 
ATOM   3583  N  N     . GLU A 1  478  ? 134.093 118.463 103.486 1.00 8.96   ? 478  GLU A N     1 
ATOM   3584  C  CA    . GLU A 1  478  ? 133.106 118.731 102.455 1.00 1.37   ? 478  GLU A CA    1 
ATOM   3585  C  C     . GLU A 1  478  ? 131.892 117.803 102.517 1.00 3.40   ? 478  GLU A C     1 
ATOM   3586  O  O     . GLU A 1  478  ? 130.777 118.247 102.242 1.00 8.25   ? 478  GLU A O     1 
ATOM   3587  C  CB    . GLU A 1  478  ? 133.796 118.659 101.104 1.00 0.43   ? 478  GLU A CB    1 
ATOM   3588  C  CG    . GLU A 1  478  ? 132.894 118.637 99.928  1.00 6.05   ? 478  GLU A CG    1 
ATOM   3589  C  CD    . GLU A 1  478  ? 133.529 117.928 98.768  1.00 17.55  ? 478  GLU A CD    1 
ATOM   3590  O  OE1   . GLU A 1  478  ? 134.386 117.060 99.013  1.00 21.35  ? 478  GLU A OE1   1 
ATOM   3591  O  OE2   . GLU A 1  478  ? 133.186 118.245 97.614  1.00 14.78  ? 478  GLU A OE2   1 
ATOM   3592  N  N     . LEU A 1  479  ? 132.060 116.536 102.892 1.00 0.15   ? 479  LEU A N     1 
ATOM   3593  C  CA    . LEU A 1  479  ? 130.935 115.605 102.876 1.00 0.90   ? 479  LEU A CA    1 
ATOM   3594  C  C     . LEU A 1  479  ? 130.178 115.563 104.193 1.00 4.71   ? 479  LEU A C     1 
ATOM   3595  O  O     . LEU A 1  479  ? 128.975 115.298 104.203 1.00 3.03   ? 479  LEU A O     1 
ATOM   3596  C  CB    . LEU A 1  479  ? 131.409 114.196 102.531 1.00 0.82   ? 479  LEU A CB    1 
ATOM   3597  C  CG    . LEU A 1  479  ? 131.981 113.925 101.145 1.00 3.14   ? 479  LEU A CG    1 
ATOM   3598  C  CD1   . LEU A 1  479  ? 132.155 112.447 100.960 1.00 4.82   ? 479  LEU A CD1   1 
ATOM   3599  C  CD2   . LEU A 1  479  ? 131.099 114.508 100.086 1.00 9.54   ? 479  LEU A CD2   1 
ATOM   3600  N  N     . LEU A 1  480  ? 130.852 115.822 105.306 1.00 11.79  ? 480  LEU A N     1 
ATOM   3601  C  CA    . LEU A 1  480  ? 130.263 115.696 106.629 1.00 10.83  ? 480  LEU A CA    1 
ATOM   3602  C  C     . LEU A 1  480  ? 129.928 117.020 107.297 1.00 7.86   ? 480  LEU A C     1 
ATOM   3603  O  O     . LEU A 1  480  ? 128.895 117.128 107.953 1.00 6.73   ? 480  LEU A O     1 
ATOM   3604  C  CB    . LEU A 1  480  ? 131.201 114.912 107.544 1.00 1.52   ? 480  LEU A CB    1 
ATOM   3605  C  CG    . LEU A 1  480  ? 130.573 114.077 108.644 1.00 1.25   ? 480  LEU A CG    1 
ATOM   3606  C  CD1   . LEU A 1  480  ? 129.853 112.888 108.094 1.00 7.58   ? 480  LEU A CD1   1 
ATOM   3607  C  CD2   . LEU A 1  480  ? 131.656 113.693 109.610 1.00 0.10   ? 480  LEU A CD2   1 
ATOM   3608  N  N     . CYS A 1  481  ? 130.797 118.014 107.192 1.00 5.67   ? 481  CYS A N     1 
ATOM   3609  C  CA    . CYS A 1  481  ? 130.736 119.162 108.077 1.00 10.29  ? 481  CYS A CA    1 
ATOM   3610  C  C     . CYS A 1  481  ? 130.341 120.449 107.380 1.00 10.01  ? 481  CYS A C     1 
ATOM   3611  O  O     . CYS A 1  481  ? 130.459 121.515 107.979 1.00 4.76   ? 481  CYS A O     1 
ATOM   3612  C  CB    . CYS A 1  481  ? 132.072 119.341 108.793 1.00 3.10   ? 481  CYS A CB    1 
ATOM   3613  S  SG    . CYS A 1  481  ? 132.676 117.880 109.609 1.00 0.45   ? 481  CYS A SG    1 
ATOM   3614  N  N     . SER A 1  482  ? 129.858 120.378 106.149 1.00 3.68   ? 482  SER A N     1 
ATOM   3615  C  CA    . SER A 1  482  ? 129.365 121.564 105.462 1.00 12.13  ? 482  SER A CA    1 
ATOM   3616  C  C     . SER A 1  482  ? 128.181 122.161 106.207 1.00 8.80   ? 482  SER A C     1 
ATOM   3617  O  O     . SER A 1  482  ? 127.482 121.470 106.943 1.00 6.41   ? 482  SER A O     1 
ATOM   3618  C  CB    . SER A 1  482  ? 128.964 121.205 104.043 1.00 6.93   ? 482  SER A CB    1 
ATOM   3619  O  OG    . SER A 1  482  ? 130.065 120.711 103.331 1.00 12.14  ? 482  SER A OG    1 
ATOM   3620  N  N     . VAL A 1  483  ? 127.954 123.461 106.018 1.00 13.67  ? 483  VAL A N     1 
ATOM   3621  C  CA    . VAL A 1  483  ? 126.944 124.137 106.818 1.00 15.63  ? 483  VAL A CA    1 
ATOM   3622  C  C     . VAL A 1  483  ? 125.526 123.833 106.350 1.00 10.66  ? 483  VAL A C     1 
ATOM   3623  O  O     . VAL A 1  483  ? 124.574 124.184 107.042 1.00 18.11  ? 483  VAL A O     1 
ATOM   3624  C  CB    . VAL A 1  483  ? 127.198 125.655 106.867 1.00 13.04  ? 483  VAL A CB    1 
ATOM   3625  C  CG1   . VAL A 1  483  ? 128.225 125.973 107.912 1.00 10.95  ? 483  VAL A CG1   1 
ATOM   3626  C  CG2   . VAL A 1  483  ? 127.606 126.191 105.526 1.00 12.67  ? 483  VAL A CG2   1 
ATOM   3627  N  N     . ARG A 1  484  ? 125.355 123.184 105.201 1.00 3.28   ? 484  ARG A N     1 
ATOM   3628  C  CA    . ARG A 1  484  ? 124.036 122.718 104.788 1.00 13.49  ? 484  ARG A CA    1 
ATOM   3629  C  C     . ARG A 1  484  ? 123.518 121.599 105.672 1.00 0.78   ? 484  ARG A C     1 
ATOM   3630  O  O     . ARG A 1  484  ? 122.324 121.297 105.643 1.00 7.96   ? 484  ARG A O     1 
ATOM   3631  C  CB    . ARG A 1  484  ? 124.072 122.227 103.351 1.00 11.60  ? 484  ARG A CB    1 
ATOM   3632  C  CG    . ARG A 1  484  ? 124.881 120.979 103.168 1.00 12.89  ? 484  ARG A CG    1 
ATOM   3633  C  CD    . ARG A 1  484  ? 124.804 120.494 101.757 1.00 13.04  ? 484  ARG A CD    1 
ATOM   3634  N  NE    . ARG A 1  484  ? 125.840 119.520 101.456 1.00 6.06   ? 484  ARG A NE    1 
ATOM   3635  C  CZ    . ARG A 1  484  ? 126.975 119.803 100.835 1.00 8.12   ? 484  ARG A CZ    1 
ATOM   3636  N  NH1   . ARG A 1  484  ? 127.253 121.027 100.430 1.00 7.85   ? 484  ARG A NH1   1 
ATOM   3637  N  NH2   . ARG A 1  484  ? 127.852 118.830 100.615 1.00 4.91   ? 484  ARG A NH2   1 
ATOM   3638  N  N     . ASN A 1  485  ? 124.396 120.961 106.434 1.00 7.36   ? 485  ASN A N     1 
ATOM   3639  C  CA    . ASN A 1  485  ? 124.000 119.922 107.366 1.00 0.57   ? 485  ASN A CA    1 
ATOM   3640  C  C     . ASN A 1  485  ? 123.469 120.492 108.667 1.00 0.12   ? 485  ASN A C     1 
ATOM   3641  O  O     . ASN A 1  485  ? 122.850 119.760 109.438 1.00 9.94   ? 485  ASN A O     1 
ATOM   3642  C  CB    . ASN A 1  485  ? 125.186 119.001 107.635 1.00 5.31   ? 485  ASN A CB    1 
ATOM   3643  C  CG    . ASN A 1  485  ? 125.608 118.239 106.415 1.00 6.61   ? 485  ASN A CG    1 
ATOM   3644  O  OD1   . ASN A 1  485  ? 124.802 117.577 105.783 1.00 1.61   ? 485  ASN A OD1   1 
ATOM   3645  N  ND2   . ASN A 1  485  ? 126.863 118.350 106.057 1.00 14.38  ? 485  ASN A ND2   1 
ATOM   3646  N  N     . TRP A 1  486  ? 123.684 121.777 108.925 1.00 13.41  ? 486  TRP A N     1 
ATOM   3647  C  CA    . TRP A 1  486  ? 123.152 122.423 110.110 1.00 12.14  ? 486  TRP A CA    1 
ATOM   3648  C  C     . TRP A 1  486  ? 122.050 123.416 109.781 1.00 10.07  ? 486  TRP A C     1 
ATOM   3649  O  O     . TRP A 1  486  ? 121.765 124.292 110.595 1.00 5.74   ? 486  TRP A O     1 
ATOM   3650  C  CB    . TRP A 1  486  ? 124.260 123.116 110.907 1.00 12.73  ? 486  TRP A CB    1 
ATOM   3651  C  CG    . TRP A 1  486  ? 125.623 122.515 110.793 1.00 0.85   ? 486  TRP A CG    1 
ATOM   3652  C  CD1   . TRP A 1  486  ? 126.758 123.157 110.429 1.00 4.74   ? 486  TRP A CD1   1 
ATOM   3653  C  CD2   . TRP A 1  486  ? 126.000 121.160 111.058 1.00 0.65   ? 486  TRP A CD2   1 
ATOM   3654  N  NE1   . TRP A 1  486  ? 127.813 122.294 110.431 1.00 1.95   ? 486  TRP A NE1   1 
ATOM   3655  C  CE2   . TRP A 1  486  ? 127.373 121.056 110.805 1.00 0.35   ? 486  TRP A CE2   1 
ATOM   3656  C  CE3   . TRP A 1  486  ? 125.305 120.020 111.467 1.00 13.73  ? 486  TRP A CE3   1 
ATOM   3657  C  CZ2   . TRP A 1  486  ? 128.064 119.868 110.953 1.00 3.49   ? 486  TRP A CZ2   1 
ATOM   3658  C  CZ3   . TRP A 1  486  ? 125.988 118.850 111.605 1.00 15.19  ? 486  TRP A CZ3   1 
ATOM   3659  C  CH2   . TRP A 1  486  ? 127.353 118.778 111.353 1.00 1.25   ? 486  TRP A CH2   1 
ATOM   3660  N  N     . PHE A 1  487  ? 121.430 123.305 108.605 1.00 7.60   ? 487  PHE A N     1 
ATOM   3661  C  CA    . PHE A 1  487  ? 120.297 124.165 108.291 1.00 9.28   ? 487  PHE A CA    1 
ATOM   3662  C  C     . PHE A 1  487  ? 119.101 123.851 109.184 1.00 1.84   ? 487  PHE A C     1 
ATOM   3663  O  O     . PHE A 1  487  ? 118.385 124.757 109.610 1.00 0.49   ? 487  PHE A O     1 
ATOM   3664  C  CB    . PHE A 1  487  ? 119.922 124.047 106.814 1.00 2.08   ? 487  PHE A CB    1 
ATOM   3665  C  CG    . PHE A 1  487  ? 118.654 124.761 106.463 1.00 7.34   ? 487  PHE A CG    1 
ATOM   3666  C  CD1   . PHE A 1  487  ? 118.579 126.134 106.535 1.00 14.07  ? 487  PHE A CD1   1 
ATOM   3667  C  CD2   . PHE A 1  487  ? 117.526 124.062 106.103 1.00 4.36   ? 487  PHE A CD2   1 
ATOM   3668  C  CE1   . PHE A 1  487  ? 117.421 126.788 106.248 1.00 0.62   ? 487  PHE A CE1   1 
ATOM   3669  C  CE2   . PHE A 1  487  ? 116.364 124.717 105.813 1.00 0.52   ? 487  PHE A CE2   1 
ATOM   3670  C  CZ    . PHE A 1  487  ? 116.316 126.079 105.884 1.00 2.17   ? 487  PHE A CZ    1 
ATOM   3671  N  N     . ILE A 1  488  ? 118.873 122.582 109.484 1.00 9.26   ? 488  ILE A N     1 
ATOM   3672  C  CA    . ILE A 1  488  ? 117.867 122.180 110.459 1.00 9.96   ? 488  ILE A CA    1 
ATOM   3673  C  C     . ILE A 1  488  ? 118.549 122.006 111.806 1.00 8.51   ? 488  ILE A C     1 
ATOM   3674  O  O     . ILE A 1  488  ? 119.598 121.365 111.903 1.00 1.69   ? 488  ILE A O     1 
ATOM   3675  C  CB    . ILE A 1  488  ? 117.157 120.887 110.027 1.00 8.77   ? 488  ILE A CB    1 
ATOM   3676  C  CG1   . ILE A 1  488  ? 116.455 121.068 108.683 1.00 11.85  ? 488  ILE A CG1   1 
ATOM   3677  C  CG2   . ILE A 1  488  ? 116.162 120.459 111.066 1.00 5.41   ? 488  ILE A CG2   1 
ATOM   3678  C  CD1   . ILE A 1  488  ? 115.342 122.051 108.696 1.00 13.88  ? 488  ILE A CD1   1 
ATOM   3679  N  N     . SER A 1  489  ? 117.969 122.596 112.843 1.00 9.83   ? 489  SER A N     1 
ATOM   3680  C  CA    . SER A 1  489  ? 118.536 122.499 114.179 1.00 2.16   ? 489  SER A CA    1 
ATOM   3681  C  C     . SER A 1  489  ? 118.473 121.068 114.700 1.00 0.87   ? 489  SER A C     1 
ATOM   3682  O  O     . SER A 1  489  ? 117.480 120.363 114.520 1.00 9.90   ? 489  SER A O     1 
ATOM   3683  C  CB    . SER A 1  489  ? 117.794 123.437 115.122 1.00 15.40  ? 489  SER A CB    1 
ATOM   3684  O  OG    . SER A 1  489  ? 118.475 123.605 116.339 1.00 8.69   ? 489  SER A OG    1 
ATOM   3685  N  N     . THR A 1  490  ? 119.556 120.632 115.337 1.00 8.72   ? 490  THR A N     1 
ATOM   3686  C  CA    . THR A 1  490  ? 119.538 119.368 116.059 1.00 0.74   ? 490  THR A CA    1 
ATOM   3687  C  C     . THR A 1  490  ? 118.775 119.500 117.365 1.00 4.02   ? 490  THR A C     1 
ATOM   3688  O  O     . THR A 1  490  ? 118.112 118.555 117.793 1.00 7.28   ? 490  THR A O     1 
ATOM   3689  C  CB    . THR A 1  490  ? 120.972 118.892 116.313 1.00 3.36   ? 490  THR A CB    1 
ATOM   3690  O  OG1   . THR A 1  490  ? 121.639 118.700 115.067 1.00 10.27  ? 490  THR A OG1   1 
ATOM   3691  C  CG2   . THR A 1  490  ? 121.008 117.600 117.091 1.00 10.65  ? 490  THR A CG2   1 
ATOM   3692  N  N     . LYS A 1  491  ? 118.828 120.679 117.977 1.00 5.64   ? 491  LYS A N     1 
ATOM   3693  C  CA    . LYS A 1  491  ? 118.168 120.905 119.253 1.00 3.04   ? 491  LYS A CA    1 
ATOM   3694  C  C     . LYS A 1  491  ? 116.654 120.911 119.112 1.00 1.07   ? 491  LYS A C     1 
ATOM   3695  O  O     . LYS A 1  491  ? 115.953 120.244 119.875 1.00 4.51   ? 491  LYS A O     1 
ATOM   3696  C  CB    . LYS A 1  491  ? 118.657 122.218 119.853 1.00 0.29   ? 491  LYS A CB    1 
ATOM   3697  C  CG    . LYS A 1  491  ? 117.876 122.701 121.039 1.00 5.28   ? 491  LYS A CG    1 
ATOM   3698  C  CD    . LYS A 1  491  ? 117.974 124.187 121.158 1.00 1.43   ? 491  LYS A CD    1 
ATOM   3699  C  CE    . LYS A 1  491  ? 116.727 124.756 121.789 1.00 17.57  ? 491  LYS A CE    1 
ATOM   3700  N  NZ    . LYS A 1  491  ? 115.492 124.388 121.043 1.00 20.15  ? 491  LYS A NZ    1 
ATOM   3701  N  N     . SER A 1  492  ? 116.126 121.647 118.142 1.00 12.26  ? 492  SER A N     1 
ATOM   3702  C  CA    . SER A 1  492  ? 114.697 121.891 118.073 1.00 2.30   ? 492  SER A CA    1 
ATOM   3703  C  C     . SER A 1  492  ? 114.009 121.254 116.882 1.00 3.91   ? 492  SER A C     1 
ATOM   3704  O  O     . SER A 1  492  ? 112.780 121.163 116.887 1.00 16.35  ? 492  SER A O     1 
ATOM   3705  C  CB    . SER A 1  492  ? 114.419 123.395 118.047 1.00 9.06   ? 492  SER A CB    1 
ATOM   3706  O  OG    . SER A 1  492  ? 114.795 123.966 116.810 1.00 8.77   ? 492  SER A OG    1 
ATOM   3707  N  N     . SER A 1  493  ? 114.757 120.815 115.874 1.00 10.36  ? 493  SER A N     1 
ATOM   3708  C  CA    . SER A 1  493  ? 114.288 120.164 114.657 1.00 10.32  ? 493  SER A CA    1 
ATOM   3709  C  C     . SER A 1  493  ? 113.653 121.122 113.661 1.00 0.97   ? 493  SER A C     1 
ATOM   3710  O  O     . SER A 1  493  ? 113.039 120.666 112.701 1.00 2.81   ? 493  SER A O     1 
ATOM   3711  C  CB    . SER A 1  493  ? 113.301 119.027 114.948 1.00 2.62   ? 493  SER A CB    1 
ATOM   3712  O  OG    . SER A 1  493  ? 113.467 117.978 114.021 1.00 10.77  ? 493  SER A OG    1 
ATOM   3713  N  N     . GLY A 1  494  ? 113.793 122.427 113.840 1.00 2.71   ? 494  GLY A N     1 
ATOM   3714  C  CA    . GLY A 1  494  ? 113.308 123.378 112.875 1.00 10.23  ? 494  GLY A CA    1 
ATOM   3715  C  C     . GLY A 1  494  ? 114.436 124.095 112.171 1.00 3.22   ? 494  GLY A C     1 
ATOM   3716  O  O     . GLY A 1  494  ? 115.606 123.943 112.521 1.00 6.66   ? 494  GLY A O     1 
ATOM   3717  N  N     . PRO A 1  495  ? 114.098 124.908 111.173 1.00 2.28   ? 495  PRO A N     1 
ATOM   3718  C  CA    . PRO A 1  495  ? 115.126 125.596 110.386 1.00 10.43  ? 495  PRO A CA    1 
ATOM   3719  C  C     . PRO A 1  495  ? 115.839 126.670 111.192 1.00 11.47  ? 495  PRO A C     1 
ATOM   3720  O  O     . PRO A 1  495  ? 115.338 127.179 112.194 1.00 13.43  ? 495  PRO A O     1 
ATOM   3721  C  CB    . PRO A 1  495  ? 114.327 126.208 109.238 1.00 4.96   ? 495  PRO A CB    1 
ATOM   3722  C  CG    . PRO A 1  495  ? 112.997 126.397 109.793 1.00 13.81  ? 495  PRO A CG    1 
ATOM   3723  C  CD    . PRO A 1  495  ? 112.746 125.306 110.767 1.00 7.49   ? 495  PRO A CD    1 
ATOM   3724  N  N     . VAL A 1  496  ? 117.039 127.010 110.742 1.00 5.78   ? 496  VAL A N     1 
ATOM   3725  C  CA    . VAL A 1  496  ? 117.887 127.958 111.439 1.00 7.05   ? 496  VAL A CA    1 
ATOM   3726  C  C     . VAL A 1  496  ? 118.006 129.274 110.683 1.00 2.09   ? 496  VAL A C     1 
ATOM   3727  O  O     . VAL A 1  496  ? 117.961 130.341 111.292 1.00 5.45   ? 496  VAL A O     1 
ATOM   3728  C  CB    . VAL A 1  496  ? 119.281 127.351 111.724 1.00 0.92   ? 496  VAL A CB    1 
ATOM   3729  C  CG1   . VAL A 1  496  ? 120.224 128.383 112.301 1.00 3.33   ? 496  VAL A CG1   1 
ATOM   3730  C  CG2   . VAL A 1  496  ? 119.164 126.187 112.671 1.00 13.94  ? 496  VAL A CG2   1 
ATOM   3731  N  N     . ASN A 1  497  ? 118.149 129.225 109.368 1.00 4.62   ? 497  ASN A N     1 
ATOM   3732  C  CA    . ASN A 1  497  ? 118.473 130.401 108.581 1.00 7.16   ? 497  ASN A CA    1 
ATOM   3733  C  C     . ASN A 1  497  ? 117.253 130.922 107.838 1.00 7.53   ? 497  ASN A C     1 
ATOM   3734  O  O     . ASN A 1  497  ? 116.226 130.255 107.720 1.00 5.32   ? 497  ASN A O     1 
ATOM   3735  C  CB    . ASN A 1  497  ? 119.587 130.100 107.579 1.00 2.96   ? 497  ASN A CB    1 
ATOM   3736  C  CG    . ASN A 1  497  ? 120.730 129.348 108.192 1.00 9.06   ? 497  ASN A CG    1 
ATOM   3737  O  OD1   . ASN A 1  497  ? 120.724 128.132 108.195 1.00 10.69  ? 497  ASN A OD1   1 
ATOM   3738  N  ND2   . ASN A 1  497  ? 121.715 130.062 108.703 1.00 3.41   ? 497  ASN A ND2   1 
ATOM   3739  N  N     . GLY A 1  498  ? 117.401 132.135 107.323 1.00 0.77   ? 498  GLY A N     1 
ATOM   3740  C  CA    . GLY A 1  498  ? 116.313 132.835 106.674 1.00 4.90   ? 498  GLY A CA    1 
ATOM   3741  C  C     . GLY A 1  498  ? 116.712 134.278 106.483 1.00 14.30  ? 498  GLY A C     1 
ATOM   3742  O  O     . GLY A 1  498  ? 117.889 134.603 106.526 1.00 8.47   ? 498  GLY A O     1 
ATOM   3743  N  N     . GLN A 1  499  ? 115.720 135.138 106.297 1.00 1.81   ? 499  GLN A N     1 
ATOM   3744  C  CA    . GLN A 1  499  ? 115.980 136.560 106.133 1.00 14.80  ? 499  GLN A CA    1 
ATOM   3745  C  C     . GLN A 1  499  ? 116.062 137.262 107.474 1.00 3.24   ? 499  GLN A C     1 
ATOM   3746  O  O     . GLN A 1  499  ? 115.407 136.868 108.437 1.00 1.20   ? 499  GLN A O     1 
ATOM   3747  C  CB    . GLN A 1  499  ? 114.903 137.229 105.282 1.00 9.15   ? 499  GLN A CB    1 
ATOM   3748  C  CG    . GLN A 1  499  ? 114.601 136.584 103.950 1.00 3.21   ? 499  GLN A CG    1 
ATOM   3749  C  CD    . GLN A 1  499  ? 115.822 136.261 103.111 1.00 11.83  ? 499  GLN A CD    1 
ATOM   3750  O  OE1   . GLN A 1  499  ? 116.865 136.873 103.232 1.00 4.26   ? 499  GLN A OE1   1 
ATOM   3751  N  NE2   . GLN A 1  499  ? 115.675 135.296 102.236 1.00 0.04   ? 499  GLN A NE2   1 
ATOM   3752  N  N     . VAL A 1  500  ? 116.879 138.312 107.531 1.00 2.91   ? 500  VAL A N     1 
ATOM   3753  C  CA    . VAL A 1  500  ? 116.971 139.173 108.703 1.00 1.97   ? 500  VAL A CA    1 
ATOM   3754  C  C     . VAL A 1  500  ? 117.040 140.612 108.226 1.00 1.54   ? 500  VAL A C     1 
ATOM   3755  O  O     . VAL A 1  500  ? 117.866 140.948 107.374 1.00 16.05  ? 500  VAL A O     1 
ATOM   3756  C  CB    . VAL A 1  500  ? 118.182 138.853 109.597 1.00 0.02   ? 500  VAL A CB    1 
ATOM   3757  C  CG1   . VAL A 1  500  ? 117.893 137.647 110.455 1.00 11.87  ? 500  VAL A CG1   1 
ATOM   3758  C  CG2   . VAL A 1  500  ? 119.435 138.649 108.778 1.00 2.96   ? 500  VAL A CG2   1 
ATOM   3759  N  N     . GLN A 1  501  ? 116.111 141.427 108.699 1.00 7.38   ? 501  GLN A N     1 
ATOM   3760  C  CA    . GLN A 1  501  ? 116.191 142.876 108.839 1.00 4.44   ? 501  GLN A CA    1 
ATOM   3761  C  C     . GLN A 1  501  ? 116.141 143.722 107.580 1.00 9.56   ? 501  GLN A C     1 
ATOM   3762  O  O     . GLN A 1  501  ? 115.677 144.852 107.641 1.00 20.57  ? 501  GLN A O     1 
ATOM   3763  C  CB    . GLN A 1  501  ? 117.505 143.251 109.511 1.00 15.12  ? 501  GLN A CB    1 
ATOM   3764  C  CG    . GLN A 1  501  ? 117.701 142.803 110.907 1.00 2.77   ? 501  GLN A CG    1 
ATOM   3765  C  CD    . GLN A 1  501  ? 119.033 143.256 111.431 1.00 7.92   ? 501  GLN A CD    1 
ATOM   3766  O  OE1   . GLN A 1  501  ? 119.721 144.037 110.791 1.00 6.22   ? 501  GLN A OE1   1 
ATOM   3767  N  NE2   . GLN A 1  501  ? 119.420 142.749 112.582 1.00 7.55   ? 501  GLN A NE2   1 
ATOM   3768  N  N     . ASP A 1  502  ? 116.508 143.210 106.427 1.00 4.38   ? 502  ASP A N     1 
ATOM   3769  C  CA    . ASP A 1  502  ? 116.559 144.095 105.270 1.00 4.88   ? 502  ASP A CA    1 
ATOM   3770  C  C     . ASP A 1  502  ? 115.870 143.358 104.163 1.00 6.65   ? 502  ASP A C     1 
ATOM   3771  O  O     . ASP A 1  502  ? 115.270 143.945 103.263 1.00 13.08  ? 502  ASP A O     1 
ATOM   3772  C  CB    . ASP A 1  502  ? 117.986 144.426 104.847 1.00 2.85   ? 502  ASP A CB    1 
ATOM   3773  C  CG    . ASP A 1  502  ? 118.554 145.595 105.573 1.00 6.66   ? 502  ASP A CG    1 
ATOM   3774  O  OD1   . ASP A 1  502  ? 118.108 145.861 106.695 1.00 15.32  ? 502  ASP A OD1   1 
ATOM   3775  O  OD2   . ASP A 1  502  ? 119.481 146.227 105.043 1.00 6.27   ? 502  ASP A OD2   1 
ATOM   3776  N  N     . SER A 1  503  ? 116.006 142.049 104.234 1.00 4.72   ? 503  SER A N     1 
ATOM   3777  C  CA    . SER A 1  503  ? 115.281 141.139 103.393 1.00 10.31  ? 503  SER A CA    1 
ATOM   3778  C  C     . SER A 1  503  ? 113.962 140.739 104.016 1.00 3.75   ? 503  SER A C     1 
ATOM   3779  O  O     . SER A 1  503  ? 113.082 140.268 103.301 1.00 18.23  ? 503  SER A O     1 
ATOM   3780  C  CB    . SER A 1  503  ? 116.153 139.925 103.118 1.00 8.44   ? 503  SER A CB    1 
ATOM   3781  O  OG    . SER A 1  503  ? 117.500 140.326 103.019 1.00 1.02   ? 503  SER A OG    1 
ATOM   3782  N  N     . THR A 1  504  ? 113.796 140.932 105.320 1.00 14.05  ? 504  THR A N     1 
ATOM   3783  C  CA    . THR A 1  504  ? 112.474 140.804 105.914 1.00 3.23   ? 504  THR A CA    1 
ATOM   3784  C  C     . THR A 1  504  ? 111.590 141.984 105.543 1.00 15.58  ? 504  THR A C     1 
ATOM   3785  O  O     . THR A 1  504  ? 110.436 141.802 105.150 1.00 9.82   ? 504  THR A O     1 
ATOM   3786  C  CB    . THR A 1  504  ? 112.570 140.680 107.431 1.00 13.52  ? 504  THR A CB    1 
ATOM   3787  O  OG1   . THR A 1  504  ? 113.185 139.442 107.770 1.00 6.57   ? 504  THR A OG1   1 
ATOM   3788  C  CG2   . THR A 1  504  ? 111.190 140.700 108.036 1.00 11.59  ? 504  THR A CG2   1 
ATOM   3789  N  N     . VAL A 1  505  ? 112.113 143.203 105.668 1.00 10.02  ? 505  VAL A N     1 
ATOM   3790  C  CA    . VAL A 1  505  ? 111.326 144.379 105.339 1.00 2.31   ? 505  VAL A CA    1 
ATOM   3791  C  C     . VAL A 1  505  ? 111.390 144.682 103.852 1.00 13.72  ? 505  VAL A C     1 
ATOM   3792  O  O     . VAL A 1  505  ? 110.484 145.326 103.324 1.00 5.95   ? 505  VAL A O     1 
ATOM   3793  C  CB    . VAL A 1  505  ? 111.767 145.586 106.194 1.00 4.02   ? 505  VAL A CB    1 
ATOM   3794  C  CG1   . VAL A 1  505  ? 112.886 146.358 105.549 1.00 13.37  ? 505  VAL A CG1   1 
ATOM   3795  C  CG2   . VAL A 1  505  ? 110.598 146.508 106.453 1.00 5.99   ? 505  VAL A CG2   1 
ATOM   3796  N  N     . GLY A 1  506  ? 112.413 144.195 103.152 1.00 2.76   ? 506  GLY A N     1 
ATOM   3797  C  CA    . GLY A 1  506  ? 112.469 144.361 101.716 1.00 4.60   ? 506  GLY A CA    1 
ATOM   3798  C  C     . GLY A 1  506  ? 111.639 143.364 100.947 1.00 7.35   ? 506  GLY A C     1 
ATOM   3799  O  O     . GLY A 1  506  ? 111.244 143.637 99.815  1.00 11.91  ? 506  GLY A O     1 
ATOM   3800  N  N     . SER A 1  507  ? 111.383 142.193 101.526 1.00 6.38   ? 507  SER A N     1 
ATOM   3801  C  CA    . SER A 1  507  ? 110.438 141.261 100.927 1.00 11.70  ? 507  SER A CA    1 
ATOM   3802  C  C     . SER A 1  507  ? 109.010 141.739 101.101 1.00 0.19   ? 507  SER A C     1 
ATOM   3803  O  O     . SER A 1  507  ? 108.172 141.509 100.229 1.00 6.71   ? 507  SER A O     1 
ATOM   3804  C  CB    . SER A 1  507  ? 110.589 139.874 101.537 1.00 14.77  ? 507  SER A CB    1 
ATOM   3805  O  OG    . SER A 1  507  ? 111.930 139.459 101.547 1.00 3.19   ? 507  SER A OG    1 
ATOM   3806  N  N     . PHE A 1  508  ? 108.716 142.386 102.225 1.00 7.32   ? 508  PHE A N     1 
ATOM   3807  C  CA    . PHE A 1  508  ? 107.408 142.992 102.421 1.00 3.36   ? 508  PHE A CA    1 
ATOM   3808  C  C     . PHE A 1  508  ? 107.166 144.114 101.422 1.00 7.61   ? 508  PHE A C     1 
ATOM   3809  O  O     . PHE A 1  508  ? 106.096 144.196 100.817 1.00 0.12   ? 508  PHE A O     1 
ATOM   3810  C  CB    . PHE A 1  508  ? 107.285 143.513 103.848 1.00 5.08   ? 508  PHE A CB    1 
ATOM   3811  C  CG    . PHE A 1  508  ? 106.135 144.441 104.049 1.00 4.94   ? 508  PHE A CG    1 
ATOM   3812  C  CD1   . PHE A 1  508  ? 104.848 143.961 104.118 1.00 0.91   ? 508  PHE A CD1   1 
ATOM   3813  C  CD2   . PHE A 1  508  ? 106.340 145.803 104.159 1.00 0.68   ? 508  PHE A CD2   1 
ATOM   3814  C  CE1   . PHE A 1  508  ? 103.807 144.812 104.290 1.00 15.32  ? 508  PHE A CE1   1 
ATOM   3815  C  CE2   . PHE A 1  508  ? 105.294 146.646 104.332 1.00 8.57   ? 508  PHE A CE2   1 
ATOM   3816  C  CZ    . PHE A 1  508  ? 104.029 146.153 104.398 1.00 14.65  ? 508  PHE A CZ    1 
ATOM   3817  N  N     . LEU A 1  509  ? 108.156 144.986 101.228 1.00 12.12  ? 509  LEU A N     1 
ATOM   3818  C  CA    . LEU A 1  509  ? 107.980 146.113 100.320 1.00 2.18   ? 509  LEU A CA    1 
ATOM   3819  C  C     . LEU A 1  509  ? 107.857 145.649 98.880  1.00 5.76   ? 509  LEU A C     1 
ATOM   3820  O  O     . LEU A 1  509  ? 107.160 146.277 98.079  1.00 9.22   ? 509  LEU A O     1 
ATOM   3821  C  CB    . LEU A 1  509  ? 109.134 147.104 100.462 1.00 15.22  ? 509  LEU A CB    1 
ATOM   3822  C  CG    . LEU A 1  509  ? 109.375 147.835 101.782 1.00 9.86   ? 509  LEU A CG    1 
ATOM   3823  C  CD1   . LEU A 1  509  ? 110.608 148.692 101.684 1.00 7.54   ? 509  LEU A CD1   1 
ATOM   3824  C  CD2   . LEU A 1  509  ? 108.186 148.660 102.203 1.00 6.10   ? 509  LEU A CD2   1 
ATOM   3825  N  N     . LEU A 1  510  ? 108.527 144.554 98.531  1.00 10.20  ? 510  LEU A N     1 
ATOM   3826  C  CA    . LEU A 1  510  ? 108.476 144.043 97.170  1.00 2.63   ? 510  LEU A CA    1 
ATOM   3827  C  C     . LEU A 1  510  ? 107.123 143.423 96.842  1.00 3.83   ? 510  LEU A C     1 
ATOM   3828  O  O     . LEU A 1  510  ? 106.573 143.662 95.764  1.00 6.19   ? 510  LEU A O     1 
ATOM   3829  C  CB    . LEU A 1  510  ? 109.600 143.037 96.965  1.00 1.45   ? 510  LEU A CB    1 
ATOM   3830  C  CG    . LEU A 1  510  ? 109.630 142.174 95.706  1.00 3.33   ? 510  LEU A CG    1 
ATOM   3831  C  CD1   . LEU A 1  510  ? 109.685 142.995 94.448  1.00 4.63   ? 510  LEU A CD1   1 
ATOM   3832  C  CD2   . LEU A 1  510  ? 110.811 141.270 95.783  1.00 1.28   ? 510  LEU A CD2   1 
ATOM   3833  N  N     . THR A 1  511  ? 106.572 142.622 97.747  1.00 6.25   ? 511  THR A N     1 
ATOM   3834  C  CA    . THR A 1  511  ? 105.332 141.901 97.502  1.00 0.92   ? 511  THR A CA    1 
ATOM   3835  C  C     . THR A 1  511  ? 104.105 142.648 97.988  1.00 1.91   ? 511  THR A C     1 
ATOM   3836  O  O     . THR A 1  511  ? 102.992 142.153 97.829  1.00 12.14  ? 511  THR A O     1 
ATOM   3837  C  CB    . THR A 1  511  ? 105.389 140.523 98.155  1.00 1.95   ? 511  THR A CB    1 
ATOM   3838  O  OG1   . THR A 1  511  ? 105.645 140.670 99.550  1.00 2.15   ? 511  THR A OG1   1 
ATOM   3839  C  CG2   . THR A 1  511  ? 106.476 139.700 97.532  1.00 7.50   ? 511  THR A CG2   1 
ATOM   3840  N  N     . ARG A 1  512  ? 104.295 143.820 98.562  1.00 8.37   ? 512  ARG A N     1 
ATOM   3841  C  CA    . ARG A 1  512  ? 103.208 144.704 98.945  1.00 6.59   ? 512  ARG A CA    1 
ATOM   3842  C  C     . ARG A 1  512  ? 102.350 145.041 97.732  1.00 0.05   ? 512  ARG A C     1 
ATOM   3843  O  O     . ARG A 1  512  ? 102.865 145.272 96.641  1.00 15.94  ? 512  ARG A O     1 
ATOM   3844  C  CB    . ARG A 1  512  ? 103.834 145.959 99.531  1.00 0.24   ? 512  ARG A CB    1 
ATOM   3845  C  CG    . ARG A 1  512  ? 102.950 146.925 100.144 1.00 5.24   ? 512  ARG A CG    1 
ATOM   3846  C  CD    . ARG A 1  512  ? 103.792 148.032 100.677 1.00 6.48   ? 512  ARG A CD    1 
ATOM   3847  N  NE    . ARG A 1  512  ? 104.859 148.370 99.752  1.00 5.00   ? 512  ARG A NE    1 
ATOM   3848  C  CZ    . ARG A 1  512  ? 105.537 149.505 99.788  1.00 5.89   ? 512  ARG A CZ    1 
ATOM   3849  N  NH1   . ARG A 1  512  ? 105.253 150.448 100.664 1.00 4.36   ? 512  ARG A NH1   1 
ATOM   3850  N  NH2   . ARG A 1  512  ? 106.511 149.706 98.909  1.00 0.12   ? 512  ARG A NH2   1 
ATOM   3851  N  N     . THR A 1  513  ? 101.032 145.053 97.911  1.00 1.56   ? 513  THR A N     1 
ATOM   3852  C  CA    . THR A 1  513  ? 100.139 145.244 96.769  1.00 5.86   ? 513  THR A CA    1 
ATOM   3853  C  C     . THR A 1  513  ? 100.124 146.689 96.292  1.00 8.46   ? 513  THR A C     1 
ATOM   3854  O  O     . THR A 1  513  ? 100.149 146.949 95.086  1.00 10.06  ? 513  THR A O     1 
ATOM   3855  C  CB    . THR A 1  513  ? 98.719  144.800 97.123  1.00 11.16  ? 513  THR A CB    1 
ATOM   3856  O  OG1   . THR A 1  513  ? 98.738  143.437 97.541  1.00 15.52  ? 513  THR A OG1   1 
ATOM   3857  C  CG2   . THR A 1  513  ? 97.814  144.916 95.927  1.00 5.43   ? 513  THR A CG2   1 
ATOM   3858  N  N     . ASN A 1  514  ? 100.056 147.643 97.214  1.00 6.45   ? 514  ASN A N     1 
ATOM   3859  C  CA    . ASN A 1  514  ? 99.983  149.056 96.881  1.00 3.21   ? 514  ASN A CA    1 
ATOM   3860  C  C     . ASN A 1  514  ? 101.121 149.799 97.559  1.00 11.28  ? 514  ASN A C     1 
ATOM   3861  O  O     . ASN A 1  514  ? 101.470 149.499 98.702  1.00 17.39  ? 514  ASN A O     1 
ATOM   3862  C  CB    . ASN A 1  514  ? 98.649  149.671 97.307  1.00 8.27   ? 514  ASN A CB    1 
ATOM   3863  C  CG    . ASN A 1  514  ? 97.527  149.364 96.348  1.00 11.70  ? 514  ASN A CG    1 
ATOM   3864  O  OD1   . ASN A 1  514  ? 97.540  149.773 95.196  1.00 14.14  ? 514  ASN A OD1   1 
ATOM   3865  N  ND2   . ASN A 1  514  ? 96.532  148.649 96.833  1.00 17.91  ? 514  ASN A ND2   1 
ATOM   3866  N  N     . THR A 1  515  ? 101.671 150.754 96.865  1.00 8.09   ? 515  THR A N     1 
ATOM   3867  C  CA    . THR A 1  515  ? 102.696 151.725 97.204  1.00 6.05   ? 515  THR A CA    1 
ATOM   3868  C  C     . THR A 1  515  ? 102.049 153.100 97.314  1.00 11.73  ? 515  THR A C     1 
ATOM   3869  O  O     . THR A 1  515  ? 100.989 153.332 96.734  1.00 19.06  ? 515  THR A O     1 
ATOM   3870  C  CB    . THR A 1  515  ? 103.783 151.692 96.121  1.00 13.94  ? 515  THR A CB    1 
ATOM   3871  O  OG1   . THR A 1  515  ? 104.595 150.528 96.295  1.00 16.00  ? 515  THR A OG1   1 
ATOM   3872  C  CG2   . THR A 1  515  ? 104.669 152.908 96.117  1.00 15.59  ? 515  THR A CG2   1 
ATOM   3873  N  N     . PRO A 1  516  ? 102.612 154.034 98.089  1.00 16.27  ? 516  PRO A N     1 
ATOM   3874  C  CA    . PRO A 1  516  ? 102.079 155.405 98.072  1.00 19.21  ? 516  PRO A CA    1 
ATOM   3875  C  C     . PRO A 1  516  ? 101.996 156.030 96.681  1.00 17.44  ? 516  PRO A C     1 
ATOM   3876  O  O     . PRO A 1  516  ? 101.338 157.062 96.531  1.00 19.73  ? 516  PRO A O     1 
ATOM   3877  C  CB    . PRO A 1  516  ? 103.051 156.176 98.972  1.00 10.82  ? 516  PRO A CB    1 
ATOM   3878  C  CG    . PRO A 1  516  ? 103.727 155.178 99.791  1.00 10.89  ? 516  PRO A CG    1 
ATOM   3879  C  CD    . PRO A 1  516  ? 103.536 153.820 99.215  1.00 16.59  ? 516  PRO A CD    1 
ATOM   3880  N  N     . MET A 1  517  ? 102.616 155.437 95.665  1.00 18.65  ? 517  MET A N     1 
ATOM   3881  C  CA    . MET A 1  517  ? 102.575 155.945 94.303  1.00 14.08  ? 517  MET A CA    1 
ATOM   3882  C  C     . MET A 1  517  ? 101.495 155.287 93.456  1.00 17.01  ? 517  MET A C     1 
ATOM   3883  O  O     . MET A 1  517  ? 101.379 155.603 92.272  1.00 22.28  ? 517  MET A O     1 
ATOM   3884  C  CB    . MET A 1  517  ? 103.937 155.755 93.626  1.00 19.03  ? 517  MET A CB    1 
ATOM   3885  C  CG    . MET A 1  517  ? 105.020 156.742 94.041  1.00 13.97  ? 517  MET A CG    1 
ATOM   3886  S  SD    . MET A 1  517  ? 104.762 158.404 93.424  1.00 25.17  ? 517  MET A SD    1 
ATOM   3887  C  CE    . MET A 1  517  ? 104.022 159.163 94.858  1.00 17.21  ? 517  MET A CE    1 
ATOM   3888  N  N     . GLY A 1  518  ? 100.705 154.387 94.027  1.00 11.28  ? 518  GLY A N     1 
ATOM   3889  C  CA    . GLY A 1  518  ? 99.756  153.612 93.254  1.00 9.65   ? 518  GLY A CA    1 
ATOM   3890  C  C     . GLY A 1  518  ? 100.009 152.128 93.369  1.00 9.19   ? 518  GLY A C     1 
ATOM   3891  O  O     . GLY A 1  518  ? 100.400 151.651 94.433  1.00 14.98  ? 518  GLY A O     1 
ATOM   3892  N  N     . LYS A 1  519  ? 99.800  151.385 92.288  1.00 12.66  ? 519  LYS A N     1 
ATOM   3893  C  CA    . LYS A 1  519  ? 100.108 149.963 92.296  1.00 8.18   ? 519  LYS A CA    1 
ATOM   3894  C  C     . LYS A 1  519  ? 101.608 149.733 92.362  1.00 11.42  ? 519  LYS A C     1 
ATOM   3895  O  O     . LYS A 1  519  ? 102.398 150.515 91.835  1.00 14.36  ? 519  LYS A O     1 
ATOM   3896  C  CB    . LYS A 1  519  ? 99.554  149.281 91.055  1.00 10.85  ? 519  LYS A CB    1 
ATOM   3897  C  CG    . LYS A 1  519  ? 98.131  148.821 91.180  1.00 17.47  ? 519  LYS A CG    1 
ATOM   3898  C  CD    . LYS A 1  519  ? 97.828  147.719 90.189  1.00 19.74  ? 519  LYS A CD    1 
ATOM   3899  C  CE    . LYS A 1  519  ? 99.042  146.840 89.949  1.00 19.89  ? 519  LYS A CE    1 
ATOM   3900  N  NZ    . LYS A 1  519  ? 98.696  145.398 89.797  1.00 21.61  ? 519  LYS A NZ    1 
ATOM   3901  N  N     . ASN A 1  520  ? 101.995 148.637 92.996  1.00 9.19   ? 520  ASN A N     1 
ATOM   3902  C  CA    . ASN A 1  520  ? 103.392 148.264 93.172  1.00 2.75   ? 520  ASN A CA    1 
ATOM   3903  C  C     . ASN A 1  520  ? 103.855 147.526 91.922  1.00 6.45   ? 520  ASN A C     1 
ATOM   3904  O  O     . ASN A 1  520  ? 103.885 146.301 91.880  1.00 16.35  ? 520  ASN A O     1 
ATOM   3905  C  CB    . ASN A 1  520  ? 103.530 147.412 94.424  1.00 3.15   ? 520  ASN A CB    1 
ATOM   3906  C  CG    . ASN A 1  520  ? 104.944 147.259 94.883  1.00 3.65   ? 520  ASN A CG    1 
ATOM   3907  O  OD1   . ASN A 1  520  ? 105.856 147.876 94.348  1.00 11.51  ? 520  ASN A OD1   1 
ATOM   3908  N  ND2   . ASN A 1  520  ? 105.142 146.426 95.884  1.00 1.32   ? 520  ASN A ND2   1 
ATOM   3909  N  N     . VAL A 1  521  ? 104.230 148.281 90.888  1.00 6.98   ? 521  VAL A N     1 
ATOM   3910  C  CA    . VAL A 1  521  ? 104.662 147.723 89.614  1.00 9.16   ? 521  VAL A CA    1 
ATOM   3911  C  C     . VAL A 1  521  ? 105.986 148.355 89.202  1.00 5.99   ? 521  VAL A C     1 
ATOM   3912  O  O     . VAL A 1  521  ? 106.340 149.450 89.638  1.00 5.12   ? 521  VAL A O     1 
ATOM   3913  C  CB    . VAL A 1  521  ? 103.612 147.930 88.497  1.00 10.09  ? 521  VAL A CB    1 
ATOM   3914  C  CG1   . VAL A 1  521  ? 102.413 147.050 88.726  1.00 3.69   ? 521  VAL A CG1   1 
ATOM   3915  C  CG2   . VAL A 1  521  ? 103.201 149.377 88.399  1.00 9.65   ? 521  VAL A CG2   1 
ATOM   3916  N  N     . MET A 1  522  ? 106.718 147.644 88.344  1.00 4.17   ? 522  MET A N     1 
ATOM   3917  C  CA    . MET A 1  522  ? 107.933 148.149 87.720  1.00 11.58  ? 522  MET A CA    1 
ATOM   3918  C  C     . MET A 1  522  ? 107.912 147.793 86.246  1.00 0.71   ? 522  MET A C     1 
ATOM   3919  O  O     . MET A 1  522  ? 107.184 146.896 85.832  1.00 11.47  ? 522  MET A O     1 
ATOM   3920  C  CB    . MET A 1  522  ? 109.214 147.585 88.348  1.00 1.67   ? 522  MET A CB    1 
ATOM   3921  C  CG    . MET A 1  522  ? 109.262 146.083 88.489  1.00 6.24   ? 522  MET A CG    1 
ATOM   3922  S  SD    . MET A 1  522  ? 110.246 145.558 89.897  1.00 13.62  ? 522  MET A SD    1 
ATOM   3923  C  CE    . MET A 1  522  ? 108.993 144.764 90.869  1.00 3.49   ? 522  MET A CE    1 
ATOM   3924  N  N     . ASN A 1  523  ? 108.709 148.505 85.454  1.00 7.65   ? 523  ASN A N     1 
ATOM   3925  C  CA    . ASN A 1  523  ? 108.789 148.227 84.030  1.00 5.97   ? 523  ASN A CA    1 
ATOM   3926  C  C     . ASN A 1  523  ? 109.801 147.112 83.762  1.00 2.63   ? 523  ASN A C     1 
ATOM   3927  O  O     . ASN A 1  523  ? 110.421 146.568 84.672  1.00 6.16   ? 523  ASN A O     1 
ATOM   3928  C  CB    . ASN A 1  523  ? 109.106 149.502 83.247  1.00 11.64  ? 523  ASN A CB    1 
ATOM   3929  C  CG    . ASN A 1  523  ? 110.406 150.155 83.657  1.00 0.50   ? 523  ASN A CG    1 
ATOM   3930  O  OD1   . ASN A 1  523  ? 111.179 149.608 84.420  1.00 1.35   ? 523  ASN A OD1   1 
ATOM   3931  N  ND2   . ASN A 1  523  ? 110.639 151.349 83.156  1.00 5.93   ? 523  ASN A ND2   1 
ATOM   3932  N  N     . LYS A 1  524  ? 109.966 146.758 82.490  1.00 1.72   ? 524  LYS A N     1 
ATOM   3933  C  CA    . LYS A 1  524  ? 110.784 145.603 82.143  1.00 1.95   ? 524  LYS A CA    1 
ATOM   3934  C  C     . LYS A 1  524  ? 112.244 145.805 82.526  1.00 5.22   ? 524  LYS A C     1 
ATOM   3935  O  O     . LYS A 1  524  ? 112.926 144.853 82.912  1.00 7.48   ? 524  LYS A O     1 
ATOM   3936  C  CB    . LYS A 1  524  ? 110.660 145.305 80.651  1.00 3.87   ? 524  LYS A CB    1 
ATOM   3937  C  CG    . LYS A 1  524  ? 111.537 144.183 80.178  1.00 3.27   ? 524  LYS A CG    1 
ATOM   3938  C  CD    . LYS A 1  524  ? 111.496 144.042 78.690  1.00 6.31   ? 524  LYS A CD    1 
ATOM   3939  C  CE    . LYS A 1  524  ? 112.481 143.013 78.209  1.00 2.46   ? 524  LYS A CE    1 
ATOM   3940  N  NZ    . LYS A 1  524  ? 112.302 142.756 76.773  1.00 3.73   ? 524  LYS A NZ    1 
ATOM   3941  N  N     . LEU A 1  525  ? 112.750 147.029 82.404  1.00 0.99   ? 525  LEU A N     1 
ATOM   3942  C  CA    . LEU A 1  525  ? 114.146 147.288 82.722  1.00 7.63   ? 525  LEU A CA    1 
ATOM   3943  C  C     . LEU A 1  525  ? 114.435 147.079 84.200  1.00 0.74   ? 525  LEU A C     1 
ATOM   3944  O  O     . LEU A 1  525  ? 115.478 146.528 84.565  1.00 5.99   ? 525  LEU A O     1 
ATOM   3945  C  CB    . LEU A 1  525  ? 114.511 148.705 82.304  1.00 2.31   ? 525  LEU A CB    1 
ATOM   3946  C  CG    . LEU A 1  525  ? 115.937 149.162 82.579  1.00 1.72   ? 525  LEU A CG    1 
ATOM   3947  C  CD1   . LEU A 1  525  ? 116.924 148.381 81.759  1.00 2.25   ? 525  LEU A CD1   1 
ATOM   3948  C  CD2   . LEU A 1  525  ? 116.042 150.621 82.281  1.00 4.19   ? 525  LEU A CD2   1 
ATOM   3949  N  N     . HIS A 1  526  ? 113.534 147.531 85.067  1.00 7.53   ? 526  HIS A N     1 
ATOM   3950  C  CA    . HIS A 1  526  ? 113.731 147.396 86.501  1.00 3.76   ? 526  HIS A CA    1 
ATOM   3951  C  C     . HIS A 1  526  ? 113.429 146.000 87.007  1.00 7.86   ? 526  HIS A C     1 
ATOM   3952  O  O     . HIS A 1  526  ? 114.020 145.574 88.000  1.00 4.83   ? 526  HIS A O     1 
ATOM   3953  C  CB    . HIS A 1  526  ? 112.885 148.419 87.241  1.00 2.67   ? 526  HIS A CB    1 
ATOM   3954  C  CG    . HIS A 1  526  ? 113.408 149.810 87.119  1.00 8.17   ? 526  HIS A CG    1 
ATOM   3955  N  ND1   . HIS A 1  526  ? 113.142 150.611 86.033  1.00 0.33   ? 526  HIS A ND1   1 
ATOM   3956  C  CD2   . HIS A 1  526  ? 114.235 150.520 87.915  1.00 3.75   ? 526  HIS A CD2   1 
ATOM   3957  C  CE1   . HIS A 1  526  ? 113.753 151.769 86.183  1.00 4.68   ? 526  HIS A CE1   1 
ATOM   3958  N  NE2   . HIS A 1  526  ? 114.426 151.738 87.316  1.00 3.38   ? 526  HIS A NE2   1 
ATOM   3959  N  N     . ALA A 1  527  ? 112.505 145.287 86.365  1.00 7.84   ? 527  ALA A N     1 
ATOM   3960  C  CA    . ALA A 1  527  ? 112.284 143.888 86.701  1.00 12.15  ? 527  ALA A CA    1 
ATOM   3961  C  C     . ALA A 1  527  ? 113.486 143.036 86.326  1.00 1.81   ? 527  ALA A C     1 
ATOM   3962  O  O     . ALA A 1  527  ? 113.858 142.121 87.064  1.00 11.69  ? 527  ALA A O     1 
ATOM   3963  C  CB    . ALA A 1  527  ? 111.026 143.377 86.012  1.00 0.21   ? 527  ALA A CB    1 
ATOM   3964  N  N     . MET A 1  528  ? 114.102 143.319 85.182  1.00 9.63   ? 528  MET A N     1 
ATOM   3965  C  CA    . MET A 1  528  ? 115.329 142.633 84.799  1.00 1.09   ? 528  MET A CA    1 
ATOM   3966  C  C     . MET A 1  528  ? 116.462 142.950 85.763  1.00 13.43  ? 528  MET A C     1 
ATOM   3967  O  O     . MET A 1  528  ? 117.322 142.104 86.019  1.00 8.35   ? 528  MET A O     1 
ATOM   3968  C  CB    . MET A 1  528  ? 115.709 143.025 83.374  1.00 2.94   ? 528  MET A CB    1 
ATOM   3969  C  CG    . MET A 1  528  ? 115.311 142.037 82.325  1.00 1.20   ? 528  MET A CG    1 
ATOM   3970  S  SD    . MET A 1  528  ? 115.987 142.339 80.696  1.00 19.47  ? 528  MET A SD    1 
ATOM   3971  C  CE    . MET A 1  528  ? 116.065 144.115 80.687  1.00 12.62  ? 528  MET A CE    1 
ATOM   3972  N  N     . GLY A 1  529  ? 116.486 144.169 86.301  1.00 2.39   ? 529  GLY A N     1 
ATOM   3973  C  CA    . GLY A 1  529  ? 117.550 144.588 87.188  1.00 12.97  ? 529  GLY A CA    1 
ATOM   3974  C  C     . GLY A 1  529  ? 117.529 143.936 88.549  1.00 13.19  ? 529  GLY A C     1 
ATOM   3975  O  O     . GLY A 1  529  ? 118.568 143.870 89.201  1.00 13.73  ? 529  GLY A O     1 
ATOM   3976  N  N     . LEU A 1  530  ? 116.372 143.462 88.999  1.00 7.89   ? 530  LEU A N     1 
ATOM   3977  C  CA    . LEU A 1  530  ? 116.297 142.746 90.265  1.00 2.32   ? 530  LEU A CA    1 
ATOM   3978  C  C     . LEU A 1  530  ? 117.053 141.431 90.236  1.00 2.25   ? 530  LEU A C     1 
ATOM   3979  O  O     . LEU A 1  530  ? 117.460 140.943 91.290  1.00 6.73   ? 530  LEU A O     1 
ATOM   3980  C  CB    . LEU A 1  530  ? 114.840 142.489 90.637  1.00 14.99  ? 530  LEU A CB    1 
ATOM   3981  C  CG    . LEU A 1  530  ? 114.135 143.400 91.638  1.00 2.42   ? 530  LEU A CG    1 
ATOM   3982  C  CD1   . LEU A 1  530  ? 114.449 144.847 91.434  1.00 8.49   ? 530  LEU A CD1   1 
ATOM   3983  C  CD2   . LEU A 1  530  ? 112.669 143.164 91.558  1.00 8.78   ? 530  LEU A CD2   1 
ATOM   3984  N  N     . PHE A 1  531  ? 117.259 140.857 89.059  1.00 6.26   ? 531  PHE A N     1 
ATOM   3985  C  CA    . PHE A 1  531  ? 117.904 139.567 88.911  1.00 5.21   ? 531  PHE A CA    1 
ATOM   3986  C  C     . PHE A 1  531  ? 119.367 139.658 88.512  1.00 1.83   ? 531  PHE A C     1 
ATOM   3987  O  O     . PHE A 1  531  ? 120.004 138.619 88.345  1.00 9.14   ? 531  PHE A O     1 
ATOM   3988  C  CB    . PHE A 1  531  ? 117.167 138.734 87.863  1.00 11.28  ? 531  PHE A CB    1 
ATOM   3989  C  CG    . PHE A 1  531  ? 115.870 138.178 88.329  1.00 3.86   ? 531  PHE A CG    1 
ATOM   3990  C  CD1   . PHE A 1  531  ? 115.820 136.985 89.012  1.00 2.38   ? 531  PHE A CD1   1 
ATOM   3991  C  CD2   . PHE A 1  531  ? 114.694 138.844 88.073  1.00 7.56   ? 531  PHE A CD2   1 
ATOM   3992  C  CE1   . PHE A 1  531  ? 114.628 136.479 89.424  1.00 9.76   ? 531  PHE A CE1   1 
ATOM   3993  C  CE2   . PHE A 1  531  ? 113.513 138.341 88.484  1.00 9.01   ? 531  PHE A CE2   1 
ATOM   3994  C  CZ    . PHE A 1  531  ? 113.479 137.160 89.164  1.00 1.47   ? 531  PHE A CZ    1 
ATOM   3995  N  N     . GLN A 1  532  ? 119.918 140.849 88.343  1.00 0.94   ? 532  GLN A N     1 
ATOM   3996  C  CA    . GLN A 1  532  ? 121.272 140.927 87.820  1.00 15.11  ? 532  GLN A CA    1 
ATOM   3997  C  C     . GLN A 1  532  ? 122.321 140.696 88.884  1.00 1.39   ? 532  GLN A C     1 
ATOM   3998  O  O     . GLN A 1  532  ? 123.501 140.939 88.640  1.00 4.57   ? 532  GLN A O     1 
ATOM   3999  C  CB    . GLN A 1  532  ? 121.508 142.259 87.108  1.00 0.64   ? 532  GLN A CB    1 
ATOM   4000  C  CG    . GLN A 1  532  ? 121.476 143.479 87.951  1.00 2.34   ? 532  GLN A CG    1 
ATOM   4001  C  CD    . GLN A 1  532  ? 121.528 144.730 87.112  1.00 0.74   ? 532  GLN A CD    1 
ATOM   4002  O  OE1   . GLN A 1  532  ? 121.593 144.661 85.899  1.00 6.23   ? 532  GLN A OE1   1 
ATOM   4003  N  NE2   . GLN A 1  532  ? 121.466 145.877 87.752  1.00 1.57   ? 532  GLN A NE2   1 
ATOM   4004  N  N     . THR A 1  533  ? 121.916 140.188 90.035  1.00 15.52  ? 533  THR A N     1 
ATOM   4005  C  CA    . THR A 1  533  ? 122.816 139.920 91.139  1.00 5.84   ? 533  THR A CA    1 
ATOM   4006  C  C     . THR A 1  533  ? 122.562 138.571 91.802  1.00 2.22   ? 533  THR A C     1 
ATOM   4007  O  O     . THR A 1  533  ? 123.446 138.068 92.500  1.00 5.42   ? 533  THR A O     1 
ATOM   4008  C  CB    . THR A 1  533  ? 122.716 141.077 92.152  1.00 3.82   ? 533  THR A CB    1 
ATOM   4009  O  OG1   . THR A 1  533  ? 123.516 142.171 91.691  1.00 9.95   ? 533  THR A OG1   1 
ATOM   4010  C  CG2   . THR A 1  533  ? 123.184 140.715 93.513  1.00 4.24   ? 533  THR A CG2   1 
ATOM   4011  N  N     . THR A 1  534  ? 121.436 137.919 91.511  1.00 6.06   ? 534  THR A N     1 
ATOM   4012  C  CA    . THR A 1  534  ? 121.006 136.727 92.231  1.00 2.94   ? 534  THR A CA    1 
ATOM   4013  C  C     . THR A 1  534  ? 121.930 135.542 92.034  1.00 7.73   ? 534  THR A C     1 
ATOM   4014  O  O     . THR A 1  534  ? 121.803 134.556 92.761  1.00 15.59  ? 534  THR A O     1 
ATOM   4015  C  CB    . THR A 1  534  ? 119.608 136.326 91.789  1.00 5.39   ? 534  THR A CB    1 
ATOM   4016  O  OG1   . THR A 1  534  ? 119.615 136.082 90.384  1.00 3.71   ? 534  THR A OG1   1 
ATOM   4017  C  CG2   . THR A 1  534  ? 118.646 137.422 92.077  1.00 1.95   ? 534  THR A CG2   1 
ATOM   4018  N  N     . GLN A 1  535  ? 122.828 135.601 91.058  1.00 10.35  ? 535  GLN A N     1 
ATOM   4019  C  CA    . GLN A 1  535  ? 123.789 134.543 90.759  1.00 9.36   ? 535  GLN A CA    1 
ATOM   4020  C  C     . GLN A 1  535  ? 123.116 133.231 90.393  1.00 13.66  ? 535  GLN A C     1 
ATOM   4021  O  O     . GLN A 1  535  ? 123.710 132.165 90.532  1.00 23.23  ? 535  GLN A O     1 
ATOM   4022  C  CB    . GLN A 1  535  ? 124.776 134.336 91.906  1.00 4.29   ? 535  GLN A CB    1 
ATOM   4023  C  CG    . GLN A 1  535  ? 126.093 135.036 91.664  1.00 8.70   ? 535  GLN A CG    1 
ATOM   4024  C  CD    . GLN A 1  535  ? 126.785 135.451 92.932  1.00 18.62  ? 535  GLN A CD    1 
ATOM   4025  O  OE1   . GLN A 1  535  ? 127.174 134.613 93.737  1.00 17.63  ? 535  GLN A OE1   1 
ATOM   4026  N  NE2   . GLN A 1  535  ? 126.961 136.749 93.112  1.00 20.81  ? 535  GLN A NE2   1 
ATOM   4027  N  N     . THR A 1  536  ? 121.884 133.295 89.921  1.00 15.86  ? 536  THR A N     1 
ATOM   4028  C  CA    . THR A 1  536  ? 121.185 132.165 89.348  1.00 16.04  ? 536  THR A CA    1 
ATOM   4029  C  C     . THR A 1  536  ? 121.176 132.319 87.830  1.00 19.73  ? 536  THR A C     1 
ATOM   4030  O  O     . THR A 1  536  ? 121.825 133.205 87.271  1.00 21.77  ? 536  THR A O     1 
ATOM   4031  C  CB    . THR A 1  536  ? 119.771 132.062 89.938  1.00 20.27  ? 536  THR A CB    1 
ATOM   4032  O  OG1   . THR A 1  536  ? 119.064 133.292 89.744  1.00 23.61  ? 536  THR A OG1   1 
ATOM   4033  C  CG2   . THR A 1  536  ? 119.813 131.735 91.419  1.00 14.67  ? 536  THR A CG2   1 
ATOM   4034  N  N     . ASP A 1  537  ? 120.472 131.441 87.152  1.00 24.54  ? 537  ASP A N     1 
ATOM   4035  C  CA    . ASP A 1  537  ? 120.210 131.640 85.732  1.00 22.19  ? 537  ASP A CA    1 
ATOM   4036  C  C     . ASP A 1  537  ? 119.119 132.689 85.557  1.00 22.28  ? 537  ASP A C     1 
ATOM   4037  O  O     . ASP A 1  537  ? 118.087 132.614 86.228  1.00 25.76  ? 537  ASP A O     1 
ATOM   4038  C  CB    . ASP A 1  537  ? 119.786 130.341 85.072  1.00 25.44  ? 537  ASP A CB    1 
ATOM   4039  C  CG    . ASP A 1  537  ? 120.945 129.599 84.464  1.00 29.85  ? 537  ASP A CG    1 
ATOM   4040  O  OD1   . ASP A 1  537  ? 121.586 130.148 83.544  1.00 26.95  ? 537  ASP A OD1   1 
ATOM   4041  O  OD2   . ASP A 1  537  ? 121.220 128.466 84.907  1.00 30.95  ? 537  ASP A OD2   1 
ATOM   4042  N  N     . PRO A 1  538  ? 119.313 133.680 84.696  1.00 20.06  ? 538  PRO A N     1 
ATOM   4043  C  CA    . PRO A 1  538  ? 118.314 134.730 84.532  1.00 12.49  ? 538  PRO A CA    1 
ATOM   4044  C  C     . PRO A 1  538  ? 117.025 134.181 83.951  1.00 11.46  ? 538  PRO A C     1 
ATOM   4045  O  O     . PRO A 1  538  ? 117.041 133.217 83.175  1.00 15.90  ? 538  PRO A O     1 
ATOM   4046  C  CB    . PRO A 1  538  ? 118.988 135.705 83.561  1.00 8.83   ? 538  PRO A CB    1 
ATOM   4047  C  CG    . PRO A 1  538  ? 120.408 135.378 83.602  1.00 11.20  ? 538  PRO A CG    1 
ATOM   4048  C  CD    . PRO A 1  538  ? 120.496 133.925 83.864  1.00 16.14  ? 538  PRO A CD    1 
ATOM   4049  N  N     . PRO A 1  539  ? 115.891 134.757 84.307  1.00 7.65   ? 539  PRO A N     1 
ATOM   4050  C  CA    . PRO A 1  539  ? 114.638 134.400 83.634  1.00 5.63   ? 539  PRO A CA    1 
ATOM   4051  C  C     . PRO A 1  539  ? 114.562 134.977 82.233  1.00 10.06  ? 539  PRO A C     1 
ATOM   4052  O  O     . PRO A 1  539  ? 115.474 135.683 81.800  1.00 15.27  ? 539  PRO A O     1 
ATOM   4053  C  CB    . PRO A 1  539  ? 113.567 135.004 84.549  1.00 7.50   ? 539  PRO A CB    1 
ATOM   4054  C  CG    . PRO A 1  539  ? 114.261 135.276 85.837  1.00 7.14   ? 539  PRO A CG    1 
ATOM   4055  C  CD    . PRO A 1  539  ? 115.655 135.606 85.480  1.00 10.61  ? 539  PRO A CD    1 
ATOM   4056  N  N     . CYS A 1  540  ? 113.485 134.692 81.514  1.00 9.23   ? 540  CYS A N     1 
ATOM   4057  C  CA    . CYS A 1  540  ? 113.295 135.186 80.160  1.00 8.36   ? 540  CYS A CA    1 
ATOM   4058  C  C     . CYS A 1  540  ? 112.245 136.287 80.174  1.00 10.18  ? 540  CYS A C     1 
ATOM   4059  O  O     . CYS A 1  540  ? 111.141 136.090 80.685  1.00 21.47  ? 540  CYS A O     1 
ATOM   4060  C  CB    . CYS A 1  540  ? 112.880 134.053 79.226  1.00 10.11  ? 540  CYS A CB    1 
ATOM   4061  S  SG    . CYS A 1  540  ? 112.853 134.468 77.476  1.00 29.12  ? 540  CYS A SG    1 
ATOM   4062  N  N     . PHE A 1  541  ? 112.597 137.448 79.629  1.00 4.93   ? 541  PHE A N     1 
ATOM   4063  C  CA    . PHE A 1  541  ? 111.686 138.578 79.535  1.00 7.34   ? 541  PHE A CA    1 
ATOM   4064  C  C     . PHE A 1  541  ? 111.337 138.897 78.090  1.00 8.12   ? 541  PHE A C     1 
ATOM   4065  O  O     . PHE A 1  541  ? 110.885 140.001 77.798  1.00 12.34  ? 541  PHE A O     1 
ATOM   4066  C  CB    . PHE A 1  541  ? 112.286 139.813 80.210  1.00 9.07   ? 541  PHE A CB    1 
ATOM   4067  C  CG    . PHE A 1  541  ? 112.452 139.687 81.697  1.00 9.11   ? 541  PHE A CG    1 
ATOM   4068  C  CD1   . PHE A 1  541  ? 113.557 139.060 82.232  1.00 11.54  ? 541  PHE A CD1   1 
ATOM   4069  C  CD2   . PHE A 1  541  ? 111.524 140.219 82.560  1.00 6.65   ? 541  PHE A CD2   1 
ATOM   4070  C  CE1   . PHE A 1  541  ? 113.720 138.957 83.587  1.00 4.19   ? 541  PHE A CE1   1 
ATOM   4071  C  CE2   . PHE A 1  541  ? 111.690 140.106 83.918  1.00 1.33   ? 541  PHE A CE2   1 
ATOM   4072  C  CZ    . PHE A 1  541  ? 112.785 139.476 84.425  1.00 1.14   ? 541  PHE A CZ    1 
ATOM   4073  N  N     . ALA A 1  542  ? 111.548 137.952 77.178  1.00 9.58   ? 542  ALA A N     1 
ATOM   4074  C  CA    . ALA A 1  542  ? 111.396 138.233 75.756  1.00 10.12  ? 542  ALA A CA    1 
ATOM   4075  C  C     . ALA A 1  542  ? 109.946 138.471 75.364  1.00 13.95  ? 542  ALA A C     1 
ATOM   4076  O  O     . ALA A 1  542  ? 109.685 139.091 74.330  1.00 17.45  ? 542  ALA A O     1 
ATOM   4077  C  CB    . ALA A 1  542  ? 111.988 137.095 74.936  1.00 9.44   ? 542  ALA A CB    1 
ATOM   4078  N  N     . ASN A 1  543  ? 108.995 137.978 76.149  1.00 16.26  ? 543  ASN A N     1 
ATOM   4079  C  CA    . ASN A 1  543  ? 107.579 138.261 75.919  1.00 11.11  ? 543  ASN A CA    1 
ATOM   4080  C  C     . ASN A 1  543  ? 107.123 139.478 76.712  1.00 14.74  ? 543  ASN A C     1 
ATOM   4081  O  O     . ASN A 1  543  ? 106.040 139.501 77.286  1.00 22.70  ? 543  ASN A O     1 
ATOM   4082  C  CB    . ASN A 1  543  ? 106.743 137.040 76.275  1.00 15.14  ? 543  ASN A CB    1 
ATOM   4083  C  CG    . ASN A 1  543  ? 107.034 135.849 75.386  1.00 22.20  ? 543  ASN A CG    1 
ATOM   4084  O  OD1   . ASN A 1  543  ? 107.162 135.980 74.171  1.00 21.81  ? 543  ASN A OD1   1 
ATOM   4085  N  ND2   . ASN A 1  543  ? 107.147 134.675 75.994  1.00 21.09  ? 543  ASN A ND2   1 
ATOM   4086  N  N     . TYR A 1  544  ? 107.947 140.519 76.716  1.00 15.43  ? 544  TYR A N     1 
ATOM   4087  C  CA    . TYR A 1  544  ? 107.685 141.722 77.491  1.00 12.56  ? 544  TYR A CA    1 
ATOM   4088  C  C     . TYR A 1  544  ? 108.234 142.907 76.724  1.00 13.44  ? 544  TYR A C     1 
ATOM   4089  O  O     . TYR A 1  544  ? 109.313 142.821 76.136  1.00 14.78  ? 544  TYR A O     1 
ATOM   4090  C  CB    . TYR A 1  544  ? 108.332 141.662 78.874  1.00 10.84  ? 544  TYR A CB    1 
ATOM   4091  C  CG    . TYR A 1  544  ? 107.565 140.880 79.902  1.00 14.62  ? 544  TYR A CG    1 
ATOM   4092  C  CD1   . TYR A 1  544  ? 106.372 141.351 80.412  1.00 12.07  ? 544  TYR A CD1   1 
ATOM   4093  C  CD2   . TYR A 1  544  ? 108.046 139.678 80.377  1.00 12.51  ? 544  TYR A CD2   1 
ATOM   4094  C  CE1   . TYR A 1  544  ? 105.683 140.644 81.348  1.00 10.60  ? 544  TYR A CE1   1 
ATOM   4095  C  CE2   . TYR A 1  544  ? 107.365 138.968 81.314  1.00 12.29  ? 544  TYR A CE2   1 
ATOM   4096  C  CZ    . TYR A 1  544  ? 106.185 139.452 81.800  1.00 14.32  ? 544  TYR A CZ    1 
ATOM   4097  O  OH    . TYR A 1  544  ? 105.499 138.733 82.747  1.00 15.63  ? 544  TYR A OH    1 
ATOM   4098  N  N     . SER A 1  545  ? 107.488 143.988 76.717  1.00 16.15  ? 545  SER A N     1 
ATOM   4099  C  CA    . SER A 1  545  ? 107.897 145.200 76.044  1.00 12.51  ? 545  SER A CA    1 
ATOM   4100  C  C     . SER A 1  545  ? 108.408 146.210 77.064  1.00 19.31  ? 545  SER A C     1 
ATOM   4101  O  O     . SER A 1  545  ? 108.135 146.087 78.257  1.00 25.35  ? 545  SER A O     1 
ATOM   4102  C  CB    . SER A 1  545  ? 106.726 145.764 75.256  1.00 15.19  ? 545  SER A CB    1 
ATOM   4103  O  OG    . SER A 1  545  ? 106.757 145.285 73.928  1.00 26.78  ? 545  SER A OG    1 
ATOM   4104  N  N     . PRO A 1  546  ? 109.159 147.221 76.623  1.00 16.12  ? 546  PRO A N     1 
ATOM   4105  C  CA    . PRO A 1  546  ? 109.729 148.177 77.583  1.00 13.77  ? 546  PRO A CA    1 
ATOM   4106  C  C     . PRO A 1  546  ? 108.708 148.880 78.454  1.00 18.99  ? 546  PRO A C     1 
ATOM   4107  O  O     . PRO A 1  546  ? 109.042 149.258 79.580  1.00 26.57  ? 546  PRO A O     1 
ATOM   4108  C  CB    . PRO A 1  546  ? 110.470 149.167 76.682  1.00 10.38  ? 546  PRO A CB    1 
ATOM   4109  C  CG    . PRO A 1  546  ? 110.822 148.373 75.498  1.00 14.91  ? 546  PRO A CG    1 
ATOM   4110  C  CD    . PRO A 1  546  ? 109.687 147.438 75.268  1.00 14.30  ? 546  PRO A CD    1 
ATOM   4111  N  N     . THR A 1  547  ? 107.482 149.071 77.984  1.00 17.31  ? 547  THR A N     1 
ATOM   4112  C  CA    . THR A 1  547  ? 106.463 149.775 78.746  1.00 15.09  ? 547  THR A CA    1 
ATOM   4113  C  C     . THR A 1  547  ? 105.522 148.844 79.500  1.00 18.11  ? 547  THR A C     1 
ATOM   4114  O  O     . THR A 1  547  ? 104.605 149.325 80.166  1.00 21.02  ? 547  THR A O     1 
ATOM   4115  C  CB    . THR A 1  547  ? 105.663 150.689 77.823  1.00 21.37  ? 547  THR A CB    1 
ATOM   4116  O  OG1   . THR A 1  547  ? 105.278 149.964 76.650  1.00 20.73  ? 547  THR A OG1   1 
ATOM   4117  C  CG2   . THR A 1  547  ? 106.499 151.884 77.414  1.00 21.60  ? 547  THR A CG2   1 
ATOM   4118  N  N     . ASP A 1  548  ? 105.722 147.532 79.413  1.00 18.45  ? 548  ASP A N     1 
ATOM   4119  C  CA    . ASP A 1  548  ? 104.909 146.586 80.163  1.00 11.69  ? 548  ASP A CA    1 
ATOM   4120  C  C     . ASP A 1  548  ? 105.236 146.695 81.644  1.00 14.66  ? 548  ASP A C     1 
ATOM   4121  O  O     . ASP A 1  548  ? 106.380 146.965 82.013  1.00 17.71  ? 548  ASP A O     1 
ATOM   4122  C  CB    . ASP A 1  548  ? 105.150 145.159 79.682  1.00 12.97  ? 548  ASP A CB    1 
ATOM   4123  C  CG    . ASP A 1  548  ? 104.435 144.847 78.390  1.00 23.64  ? 548  ASP A CG    1 
ATOM   4124  O  OD1   . ASP A 1  548  ? 103.535 145.609 77.996  1.00 29.55  ? 548  ASP A OD1   1 
ATOM   4125  O  OD2   . ASP A 1  548  ? 104.768 143.826 77.763  1.00 23.62  ? 548  ASP A OD2   1 
ATOM   4126  N  N     . LEU A 1  549  ? 104.234 146.486 82.488  1.00 9.83   ? 549  LEU A N     1 
ATOM   4127  C  CA    . LEU A 1  549  ? 104.387 146.610 83.929  1.00 7.01   ? 549  LEU A CA    1 
ATOM   4128  C  C     . LEU A 1  549  ? 104.243 145.252 84.595  1.00 14.02  ? 549  LEU A C     1 
ATOM   4129  O  O     . LEU A 1  549  ? 103.380 144.455 84.223  1.00 16.02  ? 549  LEU A O     1 
ATOM   4130  C  CB    . LEU A 1  549  ? 103.360 147.579 84.501  1.00 10.18  ? 549  LEU A CB    1 
ATOM   4131  C  CG    . LEU A 1  549  ? 103.348 148.969 83.880  1.00 9.44   ? 549  LEU A CG    1 
ATOM   4132  C  CD1   . LEU A 1  549  ? 102.163 149.742 84.393  1.00 12.90  ? 549  LEU A CD1   1 
ATOM   4133  C  CD2   . LEU A 1  549  ? 104.631 149.695 84.188  1.00 5.58   ? 549  LEU A CD2   1 
ATOM   4134  N  N     . LEU A 1  550  ? 105.098 144.992 85.578  1.00 13.55  ? 550  LEU A N     1 
ATOM   4135  C  CA    . LEU A 1  550  ? 105.134 143.726 86.292  1.00 7.44   ? 550  LEU A CA    1 
ATOM   4136  C  C     . LEU A 1  550  ? 104.940 143.981 87.775  1.00 10.39  ? 550  LEU A C     1 
ATOM   4137  O  O     . LEU A 1  550  ? 105.597 144.849 88.345  1.00 16.10  ? 550  LEU A O     1 
ATOM   4138  C  CB    . LEU A 1  550  ? 106.460 143.010 86.064  1.00 7.80   ? 550  LEU A CB    1 
ATOM   4139  C  CG    . LEU A 1  550  ? 106.733 142.367 84.713  1.00 8.84   ? 550  LEU A CG    1 
ATOM   4140  C  CD1   . LEU A 1  550  ? 107.469 143.328 83.809  1.00 6.91   ? 550  LEU A CD1   1 
ATOM   4141  C  CD2   . LEU A 1  550  ? 107.537 141.120 84.916  1.00 12.99  ? 550  LEU A CD2   1 
ATOM   4142  N  N     . ASP A 1  551  ? 104.046 143.229 88.399  1.00 11.74  ? 551  ASP A N     1 
ATOM   4143  C  CA    . ASP A 1  551  ? 103.860 143.361 89.831  1.00 2.79   ? 551  ASP A CA    1 
ATOM   4144  C  C     . ASP A 1  551  ? 104.978 142.641 90.574  1.00 10.19  ? 551  ASP A C     1 
ATOM   4145  O  O     . ASP A 1  551  ? 105.688 141.806 90.022  1.00 14.74  ? 551  ASP A O     1 
ATOM   4146  C  CB    . ASP A 1  551  ? 102.500 142.814 90.246  1.00 7.17   ? 551  ASP A CB    1 
ATOM   4147  C  CG    . ASP A 1  551  ? 102.136 141.552 89.505  1.00 23.10  ? 551  ASP A CG    1 
ATOM   4148  O  OD1   . ASP A 1  551  ? 102.161 141.565 88.252  1.00 27.20  ? 551  ASP A OD1   1 
ATOM   4149  O  OD2   . ASP A 1  551  ? 101.825 140.540 90.169  1.00 25.72  ? 551  ASP A OD2   1 
ATOM   4150  N  N     . GLY A 1  552  ? 105.138 142.994 91.846  1.00 8.23   ? 552  GLY A N     1 
ATOM   4151  C  CA    . GLY A 1  552  ? 106.203 142.405 92.637  1.00 4.82   ? 552  GLY A CA    1 
ATOM   4152  C  C     . GLY A 1  552  ? 106.021 140.922 92.867  1.00 8.15   ? 552  GLY A C     1 
ATOM   4153  O  O     . GLY A 1  552  ? 106.994 140.178 92.955  1.00 11.75  ? 552  GLY A O     1 
ATOM   4154  N  N     . LYS A 1  553  ? 104.772 140.477 92.991  1.00 12.08  ? 553  LYS A N     1 
ATOM   4155  C  CA    . LYS A 1  553  ? 104.489 139.053 93.120  1.00 6.77   ? 553  LYS A CA    1 
ATOM   4156  C  C     . LYS A 1  553  ? 104.802 138.293 91.841  1.00 10.15  ? 553  LYS A C     1 
ATOM   4157  O  O     . LYS A 1  553  ? 105.113 137.102 91.895  1.00 14.60  ? 553  LYS A O     1 
ATOM   4158  C  CB    . LYS A 1  553  ? 103.029 138.844 93.504  1.00 13.87  ? 553  LYS A CB    1 
ATOM   4159  C  CG    . LYS A 1  553  ? 102.602 139.563 94.764  1.00 17.19  ? 553  LYS A CG    1 
ATOM   4160  C  CD    . LYS A 1  553  ? 101.247 139.061 95.228  1.00 19.51  ? 553  LYS A CD    1 
ATOM   4161  C  CE    . LYS A 1  553  ? 100.729 139.837 96.427  1.00 15.90  ? 553  LYS A CE    1 
ATOM   4162  N  NZ    . LYS A 1  553  ? 100.041 141.093 96.054  1.00 15.83  ? 553  LYS A NZ    1 
ATOM   4163  N  N     . SER A 1  554  ? 104.704 138.952 90.687  1.00 10.57  ? 554  SER A N     1 
ATOM   4164  C  CA    . SER A 1  554  ? 105.113 138.333 89.431  1.00 12.74  ? 554  SER A CA    1 
ATOM   4165  C  C     . SER A 1  554  ? 106.611 138.072 89.396  1.00 9.74   ? 554  SER A C     1 
ATOM   4166  O  O     . SER A 1  554  ? 107.059 137.045 88.883  1.00 15.08  ? 554  SER A O     1 
ATOM   4167  C  CB    . SER A 1  554  ? 104.709 139.226 88.264  1.00 15.68  ? 554  SER A CB    1 
ATOM   4168  O  OG    . SER A 1  554  ? 104.677 138.508 87.052  1.00 18.80  ? 554  SER A OG    1 
ATOM   4169  N  N     . VAL A 1  555  ? 107.401 139.008 89.912  1.00 13.06  ? 555  VAL A N     1 
ATOM   4170  C  CA    . VAL A 1  555  ? 108.851 138.889 89.867  1.00 8.49   ? 555  VAL A CA    1 
ATOM   4171  C  C     . VAL A 1  555  ? 109.334 137.814 90.830  1.00 8.57   ? 555  VAL A C     1 
ATOM   4172  O  O     . VAL A 1  555  ? 110.286 137.085 90.540  1.00 12.49  ? 555  VAL A O     1 
ATOM   4173  C  CB    . VAL A 1  555  ? 109.488 140.261 90.153  1.00 5.00   ? 555  VAL A CB    1 
ATOM   4174  C  CG1   . VAL A 1  555  ? 110.967 140.139 90.365  1.00 6.35   ? 555  VAL A CG1   1 
ATOM   4175  C  CG2   . VAL A 1  555  ? 109.202 141.210 89.017  1.00 4.24   ? 555  VAL A CG2   1 
ATOM   4176  N  N     . VAL A 1  556  ? 108.693 137.703 91.991  1.00 4.53   ? 556  VAL A N     1 
ATOM   4177  C  CA    . VAL A 1  556  ? 109.080 136.690 92.964  1.00 4.64   ? 556  VAL A CA    1 
ATOM   4178  C  C     . VAL A 1  556  ? 108.794 135.297 92.427  1.00 10.43  ? 556  VAL A C     1 
ATOM   4179  O  O     . VAL A 1  556  ? 109.568 134.363 92.651  1.00 19.29  ? 556  VAL A O     1 
ATOM   4180  C  CB    . VAL A 1  556  ? 108.372 136.944 94.307  1.00 2.12   ? 556  VAL A CB    1 
ATOM   4181  C  CG1   . VAL A 1  556  ? 108.679 135.852 95.284  1.00 2.67   ? 556  VAL A CG1   1 
ATOM   4182  C  CG2   . VAL A 1  556  ? 108.796 138.258 94.883  1.00 7.40   ? 556  VAL A CG2   1 
ATOM   4183  N  N     . SER A 1  557  ? 107.693 135.137 91.693  1.00 8.75   ? 557  SER A N     1 
ATOM   4184  C  CA    . SER A 1  557  ? 107.343 133.839 91.129  1.00 0.76   ? 557  SER A CA    1 
ATOM   4185  C  C     . SER A 1  557  ? 108.366 133.361 90.114  1.00 5.50   ? 557  SER A C     1 
ATOM   4186  O  O     . SER A 1  557  ? 108.543 132.155 89.945  1.00 14.74  ? 557  SER A O     1 
ATOM   4187  C  CB    . SER A 1  557  ? 105.970 133.914 90.485  1.00 4.59   ? 557  SER A CB    1 
ATOM   4188  O  OG    . SER A 1  557  ? 105.029 134.416 91.399  1.00 10.83  ? 557  SER A OG    1 
ATOM   4189  N  N     . MET A 1  558  ? 109.042 134.279 89.426  1.00 6.37   ? 558  MET A N     1 
ATOM   4190  C  CA    . MET A 1  558  ? 110.071 133.879 88.474  1.00 2.38   ? 558  MET A CA    1 
ATOM   4191  C  C     . MET A 1  558  ? 111.230 133.186 89.163  1.00 2.35   ? 558  MET A C     1 
ATOM   4192  O  O     . MET A 1  558  ? 112.027 132.513 88.510  1.00 6.28   ? 558  MET A O     1 
ATOM   4193  C  CB    . MET A 1  558  ? 110.586 135.091 87.706  1.00 3.01   ? 558  MET A CB    1 
ATOM   4194  C  CG    . MET A 1  558  ? 109.621 135.653 86.709  1.00 7.51   ? 558  MET A CG    1 
ATOM   4195  S  SD    . MET A 1  558  ? 110.286 137.093 85.890  1.00 11.18  ? 558  MET A SD    1 
ATOM   4196  C  CE    . MET A 1  558  ? 108.813 137.707 85.113  1.00 7.39   ? 558  MET A CE    1 
ATOM   4197  N  N     . LEU A 1  559  ? 111.354 133.357 90.471  1.00 9.63   ? 559  LEU A N     1 
ATOM   4198  C  CA    . LEU A 1  559  ? 112.426 132.754 91.242  1.00 3.57   ? 559  LEU A CA    1 
ATOM   4199  C  C     . LEU A 1  559  ? 111.979 131.490 91.957  1.00 4.97   ? 559  LEU A C     1 
ATOM   4200  O  O     . LEU A 1  559  ? 112.755 130.543 92.077  1.00 12.23  ? 559  LEU A O     1 
ATOM   4201  C  CB    . LEU A 1  559  ? 112.953 133.757 92.261  1.00 0.97   ? 559  LEU A CB    1 
ATOM   4202  C  CG    . LEU A 1  559  ? 114.309 133.462 92.875  1.00 6.59   ? 559  LEU A CG    1 
ATOM   4203  C  CD1   . LEU A 1  559  ? 115.383 133.619 91.836  1.00 9.95   ? 559  LEU A CD1   1 
ATOM   4204  C  CD2   . LEU A 1  559  ? 114.538 134.387 94.021  1.00 0.45   ? 559  LEU A CD2   1 
ATOM   4205  N  N     . LEU A 1  560  ? 110.739 131.458 92.439  1.00 4.61   ? 560  LEU A N     1 
ATOM   4206  C  CA    . LEU A 1  560  ? 110.235 130.300 93.157  1.00 8.53   ? 560  LEU A CA    1 
ATOM   4207  C  C     . LEU A 1  560  ? 109.770 129.184 92.235  1.00 8.79   ? 560  LEU A C     1 
ATOM   4208  O  O     . LEU A 1  560  ? 109.447 128.103 92.726  1.00 18.83  ? 560  LEU A O     1 
ATOM   4209  C  CB    . LEU A 1  560  ? 109.086 130.711 94.066  1.00 8.13   ? 560  LEU A CB    1 
ATOM   4210  C  CG    . LEU A 1  560  ? 109.356 131.699 95.191  1.00 12.69  ? 560  LEU A CG    1 
ATOM   4211  C  CD1   . LEU A 1  560  ? 108.046 132.047 95.860  1.00 6.30   ? 560  LEU A CD1   1 
ATOM   4212  C  CD2   . LEU A 1  560  ? 110.342 131.137 96.184  1.00 8.03   ? 560  LEU A CD2   1 
ATOM   4213  N  N     . ARG A 1  561  ? 109.719 129.414 90.926  1.00 7.70   ? 561  ARG A N     1 
ATOM   4214  C  CA    . ARG A 1  561  ? 109.401 128.354 89.981  1.00 9.89   ? 561  ARG A CA    1 
ATOM   4215  C  C     . ARG A 1  561  ? 110.456 127.263 89.938  1.00 18.23  ? 561  ARG A C     1 
ATOM   4216  O  O     . ARG A 1  561  ? 110.136 126.132 89.570  1.00 22.73  ? 561  ARG A O     1 
ATOM   4217  C  CB    . ARG A 1  561  ? 109.245 128.927 88.577  1.00 13.61  ? 561  ARG A CB    1 
ATOM   4218  C  CG    . ARG A 1  561  ? 107.831 129.125 88.137  1.00 15.65  ? 561  ARG A CG    1 
ATOM   4219  C  CD    . ARG A 1  561  ? 107.767 129.878 86.831  1.00 16.57  ? 561  ARG A CD    1 
ATOM   4220  N  NE    . ARG A 1  561  ? 106.840 130.997 86.921  1.00 15.95  ? 561  ARG A NE    1 
ATOM   4221  C  CZ    . ARG A 1  561  ? 107.084 132.206 86.443  1.00 19.06  ? 561  ARG A CZ    1 
ATOM   4222  N  NH1   . ARG A 1  561  ? 108.200 132.478 85.790  1.00 16.81  ? 561  ARG A NH1   1 
ATOM   4223  N  NH2   . ARG A 1  561  ? 106.190 133.170 86.633  1.00 16.93  ? 561  ARG A NH2   1 
ATOM   4224  N  N     . GLN A 1  562  ? 111.710 127.582 90.250  1.00 13.63  ? 562  GLN A N     1 
ATOM   4225  C  CA    . GLN A 1  562  ? 112.761 126.574 90.194  1.00 13.60  ? 562  GLN A CA    1 
ATOM   4226  C  C     . GLN A 1  562  ? 112.539 125.483 91.230  1.00 22.10  ? 562  GLN A C     1 
ATOM   4227  O  O     . GLN A 1  562  ? 112.789 124.302 90.961  1.00 23.99  ? 562  GLN A O     1 
ATOM   4228  C  CB    . GLN A 1  562  ? 114.123 127.222 90.404  1.00 18.97  ? 562  GLN A CB    1 
ATOM   4229  C  CG    . GLN A 1  562  ? 114.203 128.699 90.060  1.00 23.39  ? 562  GLN A CG    1 
ATOM   4230  C  CD    . GLN A 1  562  ? 114.170 128.988 88.577  1.00 26.54  ? 562  GLN A CD    1 
ATOM   4231  O  OE1   . GLN A 1  562  ? 113.872 128.116 87.763  1.00 28.07  ? 562  GLN A OE1   1 
ATOM   4232  N  NE2   . GLN A 1  562  ? 114.503 130.219 88.214  1.00 22.89  ? 562  GLN A NE2   1 
ATOM   4233  N  N     . THR A 1  563  ? 112.081 125.859 92.421  1.00 15.31  ? 563  THR A N     1 
ATOM   4234  C  CA    . THR A 1  563  ? 111.799 124.928 93.511  1.00 6.70   ? 563  THR A CA    1 
ATOM   4235  C  C     . THR A 1  563  ? 110.364 125.152 93.956  1.00 6.06   ? 563  THR A C     1 
ATOM   4236  O  O     . THR A 1  563  ? 110.116 125.805 94.976  1.00 10.15  ? 563  THR A O     1 
ATOM   4237  C  CB    . THR A 1  563  ? 112.758 125.127 94.683  1.00 7.96   ? 563  THR A CB    1 
ATOM   4238  O  OG1   . THR A 1  563  ? 112.579 126.439 95.220  1.00 15.17  ? 563  THR A OG1   1 
ATOM   4239  C  CG2   . THR A 1  563  ? 114.184 124.954 94.257  1.00 5.01   ? 563  THR A CG2   1 
ATOM   4240  N  N     . PRO A 1  564  ? 109.392 124.628 93.211  1.00 2.56   ? 564  PRO A N     1 
ATOM   4241  C  CA    . PRO A 1  564  ? 107.979 124.892 93.523  1.00 8.29   ? 564  PRO A CA    1 
ATOM   4242  C  C     . PRO A 1  564  ? 107.536 124.239 94.826  1.00 6.05   ? 564  PRO A C     1 
ATOM   4243  O  O     . PRO A 1  564  ? 107.777 123.056 95.054  1.00 8.20   ? 564  PRO A O     1 
ATOM   4244  C  CB    . PRO A 1  564  ? 107.241 124.309 92.315  1.00 8.17   ? 564  PRO A CB    1 
ATOM   4245  C  CG    . PRO A 1  564  ? 108.183 123.388 91.692  1.00 3.87   ? 564  PRO A CG    1 
ATOM   4246  C  CD    . PRO A 1  564  ? 109.542 123.906 91.942  1.00 3.18   ? 564  PRO A CD    1 
ATOM   4247  N  N     . ILE A 1  565  ? 106.873 125.020 95.674  1.00 0.56   ? 565  ILE A N     1 
ATOM   4248  C  CA    . ILE A 1  565  ? 106.342 124.556 96.943  1.00 9.32   ? 565  ILE A CA    1 
ATOM   4249  C  C     . ILE A 1  565  ? 104.914 125.061 97.085  1.00 1.22   ? 565  ILE A C     1 
ATOM   4250  O  O     . ILE A 1  565  ? 104.436 125.870 96.299  1.00 8.39   ? 565  ILE A O     1 
ATOM   4251  C  CB    . ILE A 1  565  ? 107.183 125.019 98.148  1.00 5.41   ? 565  ILE A CB    1 
ATOM   4252  C  CG1   . ILE A 1  565  ? 107.300 126.543 98.143  1.00 2.04   ? 565  ILE A CG1   1 
ATOM   4253  C  CG2   . ILE A 1  565  ? 108.538 124.335 98.160  1.00 6.76   ? 565  ILE A CG2   1 
ATOM   4254  C  CD1   . ILE A 1  565  ? 107.475 127.130 99.479  1.00 2.55   ? 565  ILE A CD1   1 
ATOM   4255  N  N     . ASN A 1  566  ? 104.243 124.578 98.123  1.00 2.54   ? 566  ASN A N     1 
ATOM   4256  C  CA    . ASN A 1  566  ? 102.895 124.995 98.484  1.00 12.02  ? 566  ASN A CA    1 
ATOM   4257  C  C     . ASN A 1  566  ? 102.942 125.625 99.866  1.00 3.68   ? 566  ASN A C     1 
ATOM   4258  O  O     . ASN A 1  566  ? 103.530 125.056 100.785 1.00 6.00   ? 566  ASN A O     1 
ATOM   4259  C  CB    . ASN A 1  566  ? 101.942 123.803 98.473  1.00 11.84  ? 566  ASN A CB    1 
ATOM   4260  C  CG    . ASN A 1  566  ? 101.653 123.300 97.085  1.00 5.09   ? 566  ASN A CG    1 
ATOM   4261  O  OD1   . ASN A 1  566  ? 101.247 124.051 96.214  1.00 18.02  ? 566  ASN A OD1   1 
ATOM   4262  N  ND2   . ASN A 1  566  ? 101.899 122.027 96.863  1.00 4.43   ? 566  ASN A ND2   1 
ATOM   4263  N  N     . TYR A 1  567  ? 102.316 126.786 100.017 1.00 3.69   ? 567  TYR A N     1 
ATOM   4264  C  CA    . TYR A 1  567  ? 102.350 127.527 101.268 1.00 10.21  ? 567  TYR A CA    1 
ATOM   4265  C  C     . TYR A 1  567  ? 101.077 128.343 101.420 1.00 7.13   ? 567  TYR A C     1 
ATOM   4266  O  O     . TYR A 1  567  ? 100.612 128.951 100.459 1.00 4.64   ? 567  TYR A O     1 
ATOM   4267  C  CB    . TYR A 1  567  ? 103.574 128.443 101.314 1.00 2.93   ? 567  TYR A CB    1 
ATOM   4268  C  CG    . TYR A 1  567  ? 103.682 129.289 102.549 1.00 1.03   ? 567  TYR A CG    1 
ATOM   4269  C  CD1   . TYR A 1  567  ? 104.361 128.842 103.659 1.00 0.71   ? 567  TYR A CD1   1 
ATOM   4270  C  CD2   . TYR A 1  567  ? 103.098 130.538 102.603 1.00 0.61   ? 567  TYR A CD2   1 
ATOM   4271  C  CE1   . TYR A 1  567  ? 104.456 129.614 104.774 1.00 3.31   ? 567  TYR A CE1   1 
ATOM   4272  C  CE2   . TYR A 1  567  ? 103.182 131.303 103.714 1.00 12.97  ? 567  TYR A CE2   1 
ATOM   4273  C  CZ    . TYR A 1  567  ? 103.864 130.842 104.794 1.00 15.42  ? 567  TYR A CZ    1 
ATOM   4274  O  OH    . TYR A 1  567  ? 103.946 131.625 105.907 1.00 9.05   ? 567  TYR A OH    1 
ATOM   4275  N  N     . GLN A 1  568  ? 100.517 128.361 102.631 1.00 8.88   ? 568  GLN A N     1 
ATOM   4276  C  CA    . GLN A 1  568  ? 99.313  129.148 102.889 1.00 9.30   ? 568  GLN A CA    1 
ATOM   4277  C  C     . GLN A 1  568  ? 99.217  129.441 104.388 1.00 1.42   ? 568  GLN A C     1 
ATOM   4278  O  O     . GLN A 1  568  ? 98.858  128.558 105.165 1.00 8.15   ? 568  GLN A O     1 
ATOM   4279  C  CB    . GLN A 1  568  ? 98.087  128.415 102.372 1.00 4.81   ? 568  GLN A CB    1 
ATOM   4280  C  CG    . GLN A 1  568  ? 96.777  128.887 102.918 1.00 9.07   ? 568  GLN A CG    1 
ATOM   4281  C  CD    . GLN A 1  568  ? 96.091  129.861 102.015 1.00 16.01  ? 568  GLN A CD    1 
ATOM   4282  O  OE1   . GLN A 1  568  ? 95.340  129.474 101.127 1.00 19.46  ? 568  GLN A OE1   1 
ATOM   4283  N  NE2   . GLN A 1  568  ? 96.325  131.144 102.248 1.00 16.61  ? 568  GLN A NE2   1 
ATOM   4284  N  N     . ARG A 1  569  ? 99.552  130.672 104.775 1.00 1.52   ? 569  ARG A N     1 
ATOM   4285  C  CA    . ARG A 1  569  ? 99.401  131.164 106.140 1.00 1.46   ? 569  ARG A CA    1 
ATOM   4286  C  C     . ARG A 1  569  ? 99.090  132.652 106.091 1.00 3.25   ? 569  ARG A C     1 
ATOM   4287  O  O     . ARG A 1  569  ? 99.037  133.260 105.025 1.00 11.83  ? 569  ARG A O     1 
ATOM   4288  C  CB    . ARG A 1  569  ? 100.654 130.940 106.992 1.00 14.03  ? 569  ARG A CB    1 
ATOM   4289  C  CG    . ARG A 1  569  ? 101.026 129.517 107.193 1.00 0.76   ? 569  ARG A CG    1 
ATOM   4290  C  CD    . ARG A 1  569  ? 101.917 129.297 108.388 1.00 5.55   ? 569  ARG A CD    1 
ATOM   4291  N  NE    . ARG A 1  569  ? 103.246 129.868 108.236 1.00 6.91   ? 569  ARG A NE    1 
ATOM   4292  C  CZ    . ARG A 1  569  ? 104.311 129.435 108.890 1.00 7.77   ? 569  ARG A CZ    1 
ATOM   4293  N  NH1   . ARG A 1  569  ? 104.247 128.397 109.693 1.00 1.39   ? 569  ARG A NH1   1 
ATOM   4294  N  NH2   . ARG A 1  569  ? 105.468 130.060 108.731 1.00 2.65   ? 569  ARG A NH2   1 
ATOM   4295  N  N     . ALA A 1  570  ? 98.900  133.213 107.200 1.00 2.97   ? 570  ALA A N     1 
ATOM   4296  C  CA    . ALA A 1  570  ? 98.752  134.657 107.264 1.00 3.85   ? 570  ALA A CA    1 
ATOM   4297  C  C     . ALA A 1  570  ? 100.069 135.308 107.670 1.00 7.85   ? 570  ALA A C     1 
ATOM   4298  O  O     . ALA A 1  570  ? 100.815 134.756 108.480 1.00 10.36  ? 570  ALA A O     1 
ATOM   4299  C  CB    . ALA A 1  570  ? 97.669  135.039 108.261 1.00 5.92   ? 570  ALA A CB    1 
ATOM   4300  N  N     . PRO A 1  571  ? 100.382 136.481 107.132 1.00 6.11   ? 571  PRO A N     1 
ATOM   4301  C  CA    . PRO A 1  571  ? 101.664 137.120 107.429 1.00 3.44   ? 571  PRO A CA    1 
ATOM   4302  C  C     . PRO A 1  571  ? 101.725 137.726 108.823 1.00 2.63   ? 571  PRO A C     1 
ATOM   4303  O  O     . PRO A 1  571  ? 100.720 137.884 109.511 1.00 11.83  ? 571  PRO A O     1 
ATOM   4304  C  CB    . PRO A 1  571  ? 101.752 138.207 106.357 1.00 4.29   ? 571  PRO A CB    1 
ATOM   4305  C  CG    . PRO A 1  571  ? 100.378 138.505 106.028 1.00 1.70   ? 571  PRO A CG    1 
ATOM   4306  C  CD    . PRO A 1  571  ? 99.627  137.233 106.124 1.00 13.41  ? 571  PRO A CD    1 
ATOM   4307  N  N     . THR A 1  572  ? 102.948 138.058 109.240 1.00 1.35   ? 572  THR A N     1 
ATOM   4308  C  CA    . THR A 1  572  ? 103.134 138.855 110.446 1.00 0.30   ? 572  THR A CA    1 
ATOM   4309  C  C     . THR A 1  572  ? 102.468 140.215 110.327 1.00 3.00   ? 572  THR A C     1 
ATOM   4310  O  O     . THR A 1  572  ? 102.048 140.782 111.337 1.00 2.38   ? 572  THR A O     1 
ATOM   4311  C  CB    . THR A 1  572  ? 104.630 139.035 110.742 1.00 4.13   ? 572  THR A CB    1 
ATOM   4312  O  OG1   . THR A 1  572  ? 105.273 137.765 110.767 1.00 1.78   ? 572  THR A OG1   1 
ATOM   4313  C  CG2   . THR A 1  572  ? 104.848 139.689 112.067 1.00 3.21   ? 572  THR A CG2   1 
ATOM   4314  N  N     . TRP A 1  573  ? 102.346 140.729 109.103 1.00 3.70   ? 573  TRP A N     1 
ATOM   4315  C  CA    . TRP A 1  573  ? 101.786 142.051 108.863 1.00 6.85   ? 573  TRP A CA    1 
ATOM   4316  C  C     . TRP A 1  573  ? 100.369 142.169 109.403 1.00 3.64   ? 573  TRP A C     1 
ATOM   4317  O  O     . TRP A 1  573  ? 100.007 143.189 109.998 1.00 4.52   ? 573  TRP A O     1 
ATOM   4318  C  CB    . TRP A 1  573  ? 101.835 142.330 107.364 1.00 3.29   ? 573  TRP A CB    1 
ATOM   4319  C  CG    . TRP A 1  573  ? 101.260 143.619 106.888 1.00 1.41   ? 573  TRP A CG    1 
ATOM   4320  C  CD1   . TRP A 1  573  ? 100.192 143.765 106.069 1.00 12.50  ? 573  TRP A CD1   1 
ATOM   4321  C  CD2   . TRP A 1  573  ? 101.737 144.938 107.165 1.00 4.28   ? 573  TRP A CD2   1 
ATOM   4322  N  NE1   . TRP A 1  573  ? 99.961  145.085 105.825 1.00 13.91  ? 573  TRP A NE1   1 
ATOM   4323  C  CE2   . TRP A 1  573  ? 100.896 145.830 106.487 1.00 1.11   ? 573  TRP A CE2   1 
ATOM   4324  C  CE3   . TRP A 1  573  ? 102.793 145.450 107.923 1.00 0.52   ? 573  TRP A CE3   1 
ATOM   4325  C  CZ2   . TRP A 1  573  ? 101.072 147.202 106.542 1.00 0.57   ? 573  TRP A CZ2   1 
ATOM   4326  C  CZ3   . TRP A 1  573  ? 102.968 146.807 107.973 1.00 0.11   ? 573  TRP A CZ3   1 
ATOM   4327  C  CH2   . TRP A 1  573  ? 102.108 147.671 107.287 1.00 0.62   ? 573  TRP A CH2   1 
ATOM   4328  N  N     . TYR A 1  574  ? 99.553  141.143 109.210 1.00 5.24   ? 574  TYR A N     1 
ATOM   4329  C  CA    . TYR A 1  574  ? 98.171  141.186 109.660 1.00 3.89   ? 574  TYR A CA    1 
ATOM   4330  C  C     . TYR A 1  574  ? 98.118  140.846 111.141 1.00 8.64   ? 574  TYR A C     1 
ATOM   4331  O  O     . TYR A 1  574  ? 98.412  139.718 111.540 1.00 12.79  ? 574  TYR A O     1 
ATOM   4332  C  CB    . TYR A 1  574  ? 97.303  140.233 108.851 1.00 10.59  ? 574  TYR A CB    1 
ATOM   4333  C  CG    . TYR A 1  574  ? 95.887  140.251 109.329 1.00 13.11  ? 574  TYR A CG    1 
ATOM   4334  C  CD1   . TYR A 1  574  ? 95.221  141.450 109.491 1.00 11.14  ? 574  TYR A CD1   1 
ATOM   4335  C  CD2   . TYR A 1  574  ? 95.223  139.085 109.651 1.00 13.03  ? 574  TYR A CD2   1 
ATOM   4336  C  CE1   . TYR A 1  574  ? 93.935  141.491 109.941 1.00 11.63  ? 574  TYR A CE1   1 
ATOM   4337  C  CE2   . TYR A 1  574  ? 93.928  139.119 110.107 1.00 15.07  ? 574  TYR A CE2   1 
ATOM   4338  C  CZ    . TYR A 1  574  ? 93.291  140.327 110.251 1.00 13.51  ? 574  TYR A CZ    1 
ATOM   4339  O  OH    . TYR A 1  574  ? 92.000  140.384 110.705 1.00 16.03  ? 574  TYR A OH    1 
ATOM   4340  N  N     . SER A 1  575  ? 97.729  141.818 111.956 1.00 13.31  ? 575  SER A N     1 
ATOM   4341  C  CA    . SER A 1  575  ? 97.656  141.657 113.397 1.00 10.72  ? 575  SER A CA    1 
ATOM   4342  C  C     . SER A 1  575  ? 96.293  142.118 113.882 1.00 19.97  ? 575  SER A C     1 
ATOM   4343  O  O     . SER A 1  575  ? 95.788  143.148 113.433 1.00 22.00  ? 575  SER A O     1 
ATOM   4344  C  CB    . SER A 1  575  ? 98.760  142.449 114.089 1.00 13.52  ? 575  SER A CB    1 
ATOM   4345  O  OG    . SER A 1  575  ? 98.726  142.266 115.484 1.00 16.31  ? 575  SER A OG    1 
ATOM   4346  N  N     . GLU A 1  576  ? 95.697  141.347 114.791 1.00 25.06  ? 576  GLU A N     1 
ATOM   4347  C  CA    . GLU A 1  576  ? 94.445  141.753 115.413 1.00 21.54  ? 576  GLU A CA    1 
ATOM   4348  C  C     . GLU A 1  576  ? 94.609  142.994 116.266 1.00 21.87  ? 576  GLU A C     1 
ATOM   4349  O  O     . GLU A 1  576  ? 93.634  143.716 116.486 1.00 28.68  ? 576  GLU A O     1 
ATOM   4350  C  CB    . GLU A 1  576  ? 93.893  140.618 116.267 1.00 24.84  ? 576  GLU A CB    1 
ATOM   4351  C  CG    . GLU A 1  576  ? 92.427  140.373 116.050 1.00 29.92  ? 576  GLU A CG    1 
ATOM   4352  C  CD    . GLU A 1  576  ? 92.129  139.904 114.650 1.00 35.77  ? 576  GLU A CD    1 
ATOM   4353  O  OE1   . GLU A 1  576  ? 91.591  140.705 113.859 1.00 35.33  ? 576  GLU A OE1   1 
ATOM   4354  O  OE2   . GLU A 1  576  ? 92.440  138.737 114.339 1.00 33.72  ? 576  GLU A OE2   1 
ATOM   4355  N  N     . VAL A 1  577  ? 95.819  143.243 116.755 1.00 11.26  ? 577  VAL A N     1 
ATOM   4356  C  CA    . VAL A 1  577  ? 96.100  144.430 117.550 1.00 9.13   ? 577  VAL A CA    1 
ATOM   4357  C  C     . VAL A 1  577  ? 95.920  145.693 116.718 1.00 10.77  ? 577  VAL A C     1 
ATOM   4358  O  O     . VAL A 1  577  ? 95.313  146.666 117.170 1.00 20.42  ? 577  VAL A O     1 
ATOM   4359  C  CB    . VAL A 1  577  ? 97.519  144.322 118.130 1.00 16.34  ? 577  VAL A CB    1 
ATOM   4360  C  CG1   . VAL A 1  577  ? 97.862  145.531 118.942 1.00 12.98  ? 577  VAL A CG1   1 
ATOM   4361  C  CG2   . VAL A 1  577  ? 97.634  143.075 118.964 1.00 12.50  ? 577  VAL A CG2   1 
ATOM   4362  N  N     . TYR A 1  578  ? 96.441  145.703 115.493 1.00 15.09  ? 578  TYR A N     1 
ATOM   4363  C  CA    . TYR A 1  578  ? 96.371  146.879 114.637 1.00 10.33  ? 578  TYR A CA    1 
ATOM   4364  C  C     . TYR A 1  578  ? 95.078  146.983 113.846 1.00 13.25  ? 578  TYR A C     1 
ATOM   4365  O  O     . TYR A 1  578  ? 94.787  148.056 113.317 1.00 11.80  ? 578  TYR A O     1 
ATOM   4366  C  CB    . TYR A 1  578  ? 97.530  146.890 113.638 1.00 9.15   ? 578  TYR A CB    1 
ATOM   4367  C  CG    . TYR A 1  578  ? 98.891  146.733 114.241 1.00 9.83   ? 578  TYR A CG    1 
ATOM   4368  C  CD1   . TYR A 1  578  ? 99.272  147.462 115.352 1.00 9.55   ? 578  TYR A CD1   1 
ATOM   4369  C  CD2   . TYR A 1  578  ? 99.796  145.845 113.702 1.00 9.38   ? 578  TYR A CD2   1 
ATOM   4370  C  CE1   . TYR A 1  578  ? 100.517 147.308 115.902 1.00 8.27   ? 578  TYR A CE1   1 
ATOM   4371  C  CE2   . TYR A 1  578  ? 101.036 145.685 114.246 1.00 11.29  ? 578  TYR A CE2   1 
ATOM   4372  C  CZ    . TYR A 1  578  ? 101.394 146.418 115.338 1.00 12.79  ? 578  TYR A CZ    1 
ATOM   4373  O  OH    . TYR A 1  578  ? 102.645 146.249 115.869 1.00 13.49  ? 578  TYR A OH    1 
ATOM   4374  N  N     . ALA A 1  579  ? 94.309  145.903 113.748 1.00 13.39  ? 579  ALA A N     1 
ATOM   4375  C  CA    . ALA A 1  579  ? 93.137  145.894 112.876 1.00 11.54  ? 579  ALA A CA    1 
ATOM   4376  C  C     . ALA A 1  579  ? 92.096  146.961 113.196 1.00 16.79  ? 579  ALA A C     1 
ATOM   4377  O  O     . ALA A 1  579  ? 91.555  147.545 112.241 1.00 14.85  ? 579  ALA A O     1 
ATOM   4378  C  CB    . ALA A 1  579  ? 92.500  144.502 112.888 1.00 14.68  ? 579  ALA A CB    1 
ATOM   4379  N  N     . PRO A 1  580  ? 91.740  147.244 114.455 1.00 11.39  ? 580  PRO A N     1 
ATOM   4380  C  CA    . PRO A 1  580  ? 90.717  148.274 114.695 1.00 5.15   ? 580  PRO A CA    1 
ATOM   4381  C  C     . PRO A 1  580  ? 91.074  149.646 114.158 1.00 15.85  ? 580  PRO A C     1 
ATOM   4382  O  O     . PRO A 1  580  ? 90.175  150.395 113.760 1.00 15.68  ? 580  PRO A O     1 
ATOM   4383  C  CB    . PRO A 1  580  ? 90.598  148.295 116.222 1.00 7.60   ? 580  PRO A CB    1 
ATOM   4384  C  CG    . PRO A 1  580  ? 91.087  147.007 116.656 1.00 10.66  ? 580  PRO A CG    1 
ATOM   4385  C  CD    . PRO A 1  580  ? 92.155  146.614 115.718 1.00 8.57   ? 580  PRO A CD    1 
ATOM   4386  N  N     . TYR A 1  581  ? 92.354  150.008 114.137 1.00 19.79  ? 581  TYR A N     1 
ATOM   4387  C  CA    . TYR A 1  581  ? 92.771  151.371 113.851 1.00 7.45   ? 581  TYR A CA    1 
ATOM   4388  C  C     . TYR A 1  581  ? 93.488  151.507 112.519 1.00 12.58  ? 581  TYR A C     1 
ATOM   4389  O  O     . TYR A 1  581  ? 94.189  152.496 112.302 1.00 19.18  ? 581  TYR A O     1 
ATOM   4390  C  CB    . TYR A 1  581  ? 93.667  151.890 114.971 1.00 7.79   ? 581  TYR A CB    1 
ATOM   4391  C  CG    . TYR A 1  581  ? 93.308  151.361 116.332 1.00 11.91  ? 581  TYR A CG    1 
ATOM   4392  C  CD1   . TYR A 1  581  ? 92.227  151.865 117.026 1.00 10.16  ? 581  TYR A CD1   1 
ATOM   4393  C  CD2   . TYR A 1  581  ? 94.045  150.350 116.916 1.00 10.73  ? 581  TYR A CD2   1 
ATOM   4394  C  CE1   . TYR A 1  581  ? 91.896  151.383 118.264 1.00 12.24  ? 581  TYR A CE1   1 
ATOM   4395  C  CE2   . TYR A 1  581  ? 93.719  149.865 118.149 1.00 9.74   ? 581  TYR A CE2   1 
ATOM   4396  C  CZ    . TYR A 1  581  ? 92.644  150.385 118.822 1.00 14.79  ? 581  TYR A CZ    1 
ATOM   4397  O  OH    . TYR A 1  581  ? 92.312  149.895 120.061 1.00 15.71  ? 581  TYR A OH    1 
ATOM   4398  N  N     . MET A 1  582  ? 93.325  150.550 111.616 1.00 11.99  ? 582  MET A N     1 
ATOM   4399  C  CA    . MET A 1  582  ? 94.161  150.529 110.428 1.00 7.87   ? 582  MET A CA    1 
ATOM   4400  C  C     . MET A 1  582  ? 93.409  149.846 109.300 1.00 14.07  ? 582  MET A C     1 
ATOM   4401  O  O     . MET A 1  582  ? 92.671  148.889 109.535 1.00 26.89  ? 582  MET A O     1 
ATOM   4402  C  CB    . MET A 1  582  ? 95.468  149.796 110.732 1.00 11.27  ? 582  MET A CB    1 
ATOM   4403  C  CG    . MET A 1  582  ? 96.517  149.862 109.680 1.00 9.76   ? 582  MET A CG    1 
ATOM   4404  S  SD    . MET A 1  582  ? 97.884  148.807 110.130 1.00 8.14   ? 582  MET A SD    1 
ATOM   4405  C  CE    . MET A 1  582  ? 98.161  148.010 108.574 1.00 10.04  ? 582  MET A CE    1 
ATOM   4406  N  N     . HIS A 1  583  ? 93.602  150.337 108.084 1.00 9.93   ? 583  HIS A N     1 
ATOM   4407  C  CA    . HIS A 1  583  ? 93.028  149.712 106.902 1.00 12.02  ? 583  HIS A CA    1 
ATOM   4408  C  C     . HIS A 1  583  ? 93.995  148.667 106.365 1.00 16.95  ? 583  HIS A C     1 
ATOM   4409  O  O     . HIS A 1  583  ? 95.183  148.944 106.191 1.00 22.84  ? 583  HIS A O     1 
ATOM   4410  C  CB    . HIS A 1  583  ? 92.716  150.747 105.825 1.00 13.88  ? 583  HIS A CB    1 
ATOM   4411  C  CG    . HIS A 1  583  ? 92.048  150.171 104.617 1.00 20.73  ? 583  HIS A CG    1 
ATOM   4412  N  ND1   . HIS A 1  583  ? 92.685  150.047 103.402 1.00 22.82  ? 583  HIS A ND1   1 
ATOM   4413  C  CD2   . HIS A 1  583  ? 90.804  149.665 104.442 1.00 18.51  ? 583  HIS A CD2   1 
ATOM   4414  C  CE1   . HIS A 1  583  ? 91.861  149.494 102.530 1.00 17.75  ? 583  HIS A CE1   1 
ATOM   4415  N  NE2   . HIS A 1  583  ? 90.714  149.252 103.136 1.00 20.70  ? 583  HIS A NE2   1 
ATOM   4416  N  N     . TYR A 1  584  ? 93.488  147.470 106.116 1.00 14.87  ? 584  TYR A N     1 
ATOM   4417  C  CA    . TYR A 1  584  ? 94.262  146.400 105.515 1.00 8.19   ? 584  TYR A CA    1 
ATOM   4418  C  C     . TYR A 1  584  ? 93.764  146.136 104.107 1.00 12.63  ? 584  TYR A C     1 
ATOM   4419  O  O     . TYR A 1  584  ? 92.559  146.061 103.871 1.00 23.52  ? 584  TYR A O     1 
ATOM   4420  C  CB    . TYR A 1  584  ? 94.158  145.118 106.337 1.00 8.54   ? 584  TYR A CB    1 
ATOM   4421  C  CG    . TYR A 1  584  ? 95.153  145.013 107.460 1.00 11.06  ? 584  TYR A CG    1 
ATOM   4422  C  CD1   . TYR A 1  584  ? 96.482  144.768 107.207 1.00 9.86   ? 584  TYR A CD1   1 
ATOM   4423  C  CD2   . TYR A 1  584  ? 94.757  145.138 108.774 1.00 13.22  ? 584  TYR A CD2   1 
ATOM   4424  C  CE1   . TYR A 1  584  ? 97.386  144.666 108.223 1.00 11.75  ? 584  TYR A CE1   1 
ATOM   4425  C  CE2   . TYR A 1  584  ? 95.657  145.033 109.799 1.00 8.92   ? 584  TYR A CE2   1 
ATOM   4426  C  CZ    . TYR A 1  584  ? 96.970  144.791 109.517 1.00 10.48  ? 584  TYR A CZ    1 
ATOM   4427  O  OH    . TYR A 1  584  ? 97.879  144.694 110.531 1.00 10.03  ? 584  TYR A OH    1 
ATOM   4428  N  N     . ASN A 1  585  ? 94.690  145.998 103.171 1.00 16.43  ? 585  ASN A N     1 
ATOM   4429  C  CA    . ASN A 1  585  ? 94.340  145.532 101.841 1.00 13.33  ? 585  ASN A CA    1 
ATOM   4430  C  C     . ASN A 1  585  ? 94.065  144.038 101.899 1.00 13.86  ? 585  ASN A C     1 
ATOM   4431  O  O     . ASN A 1  585  ? 94.835  143.283 102.493 1.00 19.95  ? 585  ASN A O     1 
ATOM   4432  C  CB    . ASN A 1  585  ? 95.461  145.835 100.855 1.00 9.56   ? 585  ASN A CB    1 
ATOM   4433  C  CG    . ASN A 1  585  ? 95.013  145.731 99.422  1.00 19.46  ? 585  ASN A CG    1 
ATOM   4434  O  OD1   . ASN A 1  585  ? 93.874  145.384 99.141  1.00 25.96  ? 585  ASN A OD1   1 
ATOM   4435  N  ND2   . ASN A 1  585  ? 95.906  146.045 98.503  1.00 19.55  ? 585  ASN A ND2   1 
ATOM   4436  N  N     . LYS A 1  586  ? 92.961  143.609 101.288 1.00 14.69  ? 586  LYS A N     1 
ATOM   4437  C  CA    . LYS A 1  586  ? 92.557  142.215 101.412 1.00 14.31  ? 586  LYS A CA    1 
ATOM   4438  C  C     . LYS A 1  586  ? 93.484  141.283 100.652 1.00 17.13  ? 586  LYS A C     1 
ATOM   4439  O  O     . LYS A 1  586  ? 93.599  140.107 101.007 1.00 19.71  ? 586  LYS A O     1 
ATOM   4440  C  CB    . LYS A 1  586  ? 91.117  142.035 100.937 1.00 16.80  ? 586  LYS A CB    1 
ATOM   4441  C  CG    . LYS A 1  586  ? 90.075  142.505 101.938 1.00 21.22  ? 586  LYS A CG    1 
ATOM   4442  C  CD    . LYS A 1  586  ? 90.440  142.115 103.369 1.00 24.79  ? 586  LYS A CD    1 
ATOM   4443  C  CE    . LYS A 1  586  ? 89.874  143.102 104.384 1.00 25.10  ? 586  LYS A CE    1 
ATOM   4444  N  NZ    . LYS A 1  586  ? 90.641  143.149 105.660 1.00 22.83  ? 586  LYS A NZ    1 
ATOM   4445  N  N     . GLN A 1  587  ? 94.158  141.780 99.619  1.00 19.65  ? 587  GLN A N     1 
ATOM   4446  C  CA    . GLN A 1  587  ? 95.106  140.984 98.856  1.00 15.94  ? 587  GLN A CA    1 
ATOM   4447  C  C     . GLN A 1  587  ? 96.494  140.990 99.466  1.00 15.19  ? 587  GLN A C     1 
ATOM   4448  O  O     . GLN A 1  587  ? 97.450  140.590 98.803  1.00 21.88  ? 587  GLN A O     1 
ATOM   4449  C  CB    . GLN A 1  587  ? 95.170  141.471 97.411  1.00 12.66  ? 587  GLN A CB    1 
ATOM   4450  C  CG    . GLN A 1  587  ? 93.900  142.129 96.941  1.00 19.22  ? 587  GLN A CG    1 
ATOM   4451  C  CD    . GLN A 1  587  ? 94.129  143.085 95.793  1.00 27.24  ? 587  GLN A CD    1 
ATOM   4452  O  OE1   . GLN A 1  587  ? 94.929  142.814 94.898  1.00 30.60  ? 587  GLN A OE1   1 
ATOM   4453  N  NE2   . GLN A 1  587  ? 93.442  144.221 95.820  1.00 18.84  ? 587  GLN A NE2   1 
ATOM   4454  N  N     . ASP A 1  588  ? 96.622  141.426 100.715 1.00 12.79  ? 588  ASP A N     1 
ATOM   4455  C  CA    . ASP A 1  588  ? 97.891  141.450 101.418 1.00 8.77   ? 588  ASP A CA    1 
ATOM   4456  C  C     . ASP A 1  588  ? 97.922  140.576 102.655 1.00 10.23  ? 588  ASP A C     1 
ATOM   4457  O  O     . ASP A 1  588  ? 99.007  140.353 103.193 1.00 11.30  ? 588  ASP A O     1 
ATOM   4458  C  CB    . ASP A 1  588  ? 98.246  142.880 101.852 1.00 12.98  ? 588  ASP A CB    1 
ATOM   4459  C  CG    . ASP A 1  588  ? 98.948  143.662 100.772 1.00 18.34  ? 588  ASP A CG    1 
ATOM   4460  O  OD1   . ASP A 1  588  ? 99.421  143.042 99.802  1.00 16.79  ? 588  ASP A OD1   1 
ATOM   4461  O  OD2   . ASP A 1  588  ? 99.036  144.898 100.898 1.00 16.12  ? 588  ASP A OD2   1 
ATOM   4462  N  N     . ILE A 1  589  ? 96.786  140.068 103.114 1.00 13.72  ? 589  ILE A N     1 
ATOM   4463  C  CA    . ILE A 1  589  ? 96.682  139.519 104.453 1.00 12.50  ? 589  ILE A CA    1 
ATOM   4464  C  C     . ILE A 1  589  ? 96.506  138.000 104.441 1.00 15.03  ? 589  ILE A C     1 
ATOM   4465  O  O     . ILE A 1  589  ? 96.230  137.409 105.476 1.00 17.80  ? 589  ILE A O     1 
ATOM   4466  C  CB    . ILE A 1  589  ? 95.562  140.198 105.246 1.00 13.17  ? 589  ILE A CB    1 
ATOM   4467  C  CG1   . ILE A 1  589  ? 94.219  139.939 104.581 1.00 13.62  ? 589  ILE A CG1   1 
ATOM   4468  C  CG2   . ILE A 1  589  ? 95.822  141.678 105.346 1.00 12.40  ? 589  ILE A CG2   1 
ATOM   4469  C  CD1   . ILE A 1  589  ? 93.068  140.442 105.362 1.00 12.70  ? 589  ILE A CD1   1 
ATOM   4470  N  N     . SER A 1  590  ? 96.670  137.357 103.292 1.00 9.69   ? 590  SER A N     1 
ATOM   4471  C  CA    . SER A 1  590  ? 96.628  135.896 103.259 1.00 6.54   ? 590  SER A CA    1 
ATOM   4472  C  C     . SER A 1  590  ? 97.626  135.432 102.202 1.00 7.57   ? 590  SER A C     1 
ATOM   4473  O  O     . SER A 1  590  ? 97.299  135.361 101.020 1.00 15.32  ? 590  SER A O     1 
ATOM   4474  C  CB    . SER A 1  590  ? 95.229  135.383 102.968 1.00 19.57  ? 590  SER A CB    1 
ATOM   4475  O  OG    . SER A 1  590  ? 94.795  135.788 101.681 1.00 23.07  ? 590  SER A OG    1 
ATOM   4476  N  N     . THR A 1  591  ? 98.835  135.106 102.647 1.00 7.82   ? 591  THR A N     1 
ATOM   4477  C  CA    . THR A 1  591  ? 99.889  134.700 101.730 1.00 6.85   ? 591  THR A CA    1 
ATOM   4478  C  C     . THR A 1  591  ? 99.616  133.294 101.222 1.00 5.47   ? 591  THR A C     1 
ATOM   4479  O  O     . THR A 1  591  ? 99.319  132.391 102.003 1.00 4.77   ? 591  THR A O     1 
ATOM   4480  C  CB    . THR A 1  591  ? 101.249 134.764 102.425 1.00 4.74   ? 591  THR A CB    1 
ATOM   4481  O  OG1   . THR A 1  591  ? 101.385 136.016 103.088 1.00 6.98   ? 591  THR A OG1   1 
ATOM   4482  C  CG2   . THR A 1  591  ? 102.371 134.630 101.432 1.00 2.16   ? 591  THR A CG2   1 
ATOM   4483  N  N     . GLN A 1  592  ? 99.709  133.107 99.913  1.00 5.54   ? 592  GLN A N     1 
ATOM   4484  C  CA    . GLN A 1  592  ? 99.431  131.820 99.301  1.00 4.77   ? 592  GLN A CA    1 
ATOM   4485  C  C     . GLN A 1  592  ? 100.397 131.579 98.155  1.00 6.62   ? 592  GLN A C     1 
ATOM   4486  O  O     . GLN A 1  592  ? 100.540 132.421 97.269  1.00 11.00  ? 592  GLN A O     1 
ATOM   4487  C  CB    . GLN A 1  592  ? 97.999  131.756 98.792  1.00 5.66   ? 592  GLN A CB    1 
ATOM   4488  C  CG    . GLN A 1  592  ? 97.650  130.467 98.115  1.00 6.19   ? 592  GLN A CG    1 
ATOM   4489  C  CD    . GLN A 1  592  ? 96.260  130.492 97.536  1.00 17.36  ? 592  GLN A CD    1 
ATOM   4490  O  OE1   . GLN A 1  592  ? 95.575  131.507 97.587  1.00 21.05  ? 592  GLN A OE1   1 
ATOM   4491  N  NE2   . GLN A 1  592  ? 95.828  129.372 96.991  1.00 18.00  ? 592  GLN A NE2   1 
ATOM   4492  N  N     . ILE A 1  593  ? 101.050 130.424 98.172  1.00 5.52   ? 593  ILE A N     1 
ATOM   4493  C  CA    . ILE A 1  593  ? 101.985 130.025 97.131  1.00 6.06   ? 593  ILE A CA    1 
ATOM   4494  C  C     . ILE A 1  593  ? 101.539 128.672 96.597  1.00 8.58   ? 593  ILE A C     1 
ATOM   4495  O  O     . ILE A 1  593  ? 101.340 127.734 97.372  1.00 13.90  ? 593  ILE A O     1 
ATOM   4496  C  CB    . ILE A 1  593  ? 103.430 129.974 97.664  1.00 0.67   ? 593  ILE A CB    1 
ATOM   4497  C  CG1   . ILE A 1  593  ? 103.857 131.370 98.105  1.00 6.97   ? 593  ILE A CG1   1 
ATOM   4498  C  CG2   . ILE A 1  593  ? 104.376 129.460 96.619  1.00 3.53   ? 593  ILE A CG2   1 
ATOM   4499  C  CD1   . ILE A 1  593  ? 105.156 131.431 98.808  1.00 2.56   ? 593  ILE A CD1   1 
ATOM   4500  N  N     . ARG A 1  594  ? 101.367 128.576 95.283  1.00 1.96   ? 594  ARG A N     1 
ATOM   4501  C  CA    . ARG A 1  594  ? 100.894 127.367 94.614  1.00 5.53   ? 594  ARG A CA    1 
ATOM   4502  C  C     . ARG A 1  594  ? 101.886 126.973 93.534  1.00 10.80  ? 594  ARG A C     1 
ATOM   4503  O  O     . ARG A 1  594  ? 101.931 127.609 92.479  1.00 21.58  ? 594  ARG A O     1 
ATOM   4504  C  CB    . ARG A 1  594  ? 99.520  127.582 93.996  1.00 8.49   ? 594  ARG A CB    1 
ATOM   4505  C  CG    . ARG A 1  594  ? 98.417  126.779 94.614  1.00 17.97  ? 594  ARG A CG    1 
ATOM   4506  C  CD    . ARG A 1  594  ? 97.157  127.596 94.713  1.00 14.78  ? 594  ARG A CD    1 
ATOM   4507  N  NE    . ARG A 1  594  ? 96.780  128.154 93.422  1.00 20.88  ? 594  ARG A NE    1 
ATOM   4508  C  CZ    . ARG A 1  594  ? 95.725  128.929 93.218  1.00 21.11  ? 594  ARG A CZ    1 
ATOM   4509  N  NH1   . ARG A 1  594  ? 94.887  129.228 94.195  1.00 16.11  ? 594  ARG A NH1   1 
ATOM   4510  N  NH2   . ARG A 1  594  ? 95.513  129.426 92.005  1.00 17.29  ? 594  ARG A NH2   1 
ATOM   4511  N  N     . ASN A 1  595  ? 102.650 125.909 93.776  1.00 6.78   ? 595  ASN A N     1 
ATOM   4512  C  CA    . ASN A 1  595  ? 103.678 125.449 92.842  1.00 4.81   ? 595  ASN A CA    1 
ATOM   4513  C  C     . ASN A 1  595  ? 104.696 126.543 92.544  1.00 7.39   ? 595  ASN A C     1 
ATOM   4514  O  O     . ASN A 1  595  ? 105.172 126.681 91.420  1.00 14.14  ? 595  ASN A O     1 
ATOM   4515  C  CB    . ASN A 1  595  ? 103.065 124.934 91.539  1.00 7.97   ? 595  ASN A CB    1 
ATOM   4516  C  CG    . ASN A 1  595  ? 102.336 123.634 91.708  1.00 15.01  ? 595  ASN A CG    1 
ATOM   4517  O  OD1   . ASN A 1  595  ? 101.129 123.561 91.515  1.00 18.51  ? 595  ASN A OD1   1 
ATOM   4518  N  ND2   . ASN A 1  595  ? 103.072 122.586 92.033  1.00 18.17  ? 595  ASN A ND2   1 
ATOM   4519  N  N     . GLY A 1  596  ? 105.039 127.324 93.555  1.00 3.87   ? 596  GLY A N     1 
ATOM   4520  C  CA    . GLY A 1  596  ? 106.016 128.368 93.396  1.00 7.46   ? 596  GLY A CA    1 
ATOM   4521  C  C     . GLY A 1  596  ? 105.484 129.678 92.868  1.00 11.24  ? 596  GLY A C     1 
ATOM   4522  O  O     . GLY A 1  596  ? 106.263 130.617 92.704  1.00 17.95  ? 596  GLY A O     1 
ATOM   4523  N  N     . GLU A 1  597  ? 104.193 129.775 92.589  1.00 7.52   ? 597  GLU A N     1 
ATOM   4524  C  CA    . GLU A 1  597  ? 103.587 131.028 92.172  1.00 2.90   ? 597  GLU A CA    1 
ATOM   4525  C  C     . GLU A 1  597  ? 102.991 131.713 93.388  1.00 11.62  ? 597  GLU A C     1 
ATOM   4526  O  O     . GLU A 1  597  ? 102.123 131.150 94.055  1.00 17.07  ? 597  GLU A O     1 
ATOM   4527  C  CB    . GLU A 1  597  ? 102.511 130.794 91.119  1.00 3.14   ? 597  GLU A CB    1 
ATOM   4528  C  CG    . GLU A 1  597  ? 102.955 129.937 89.976  1.00 13.19  ? 597  GLU A CG    1 
ATOM   4529  C  CD    . GLU A 1  597  ? 104.046 130.579 89.160  1.00 23.83  ? 597  GLU A CD    1 
ATOM   4530  O  OE1   . GLU A 1  597  ? 103.778 131.596 88.492  1.00 24.16  ? 597  GLU A OE1   1 
ATOM   4531  O  OE2   . GLU A 1  597  ? 105.176 130.064 89.173  1.00 16.35  ? 597  GLU A OE2   1 
ATOM   4532  N  N     . LEU A 1  598  ? 103.456 132.919 93.678  1.00 9.85   ? 598  LEU A N     1 
ATOM   4533  C  CA    . LEU A 1  598  ? 102.912 133.705 94.776  1.00 8.38   ? 598  LEU A CA    1 
ATOM   4534  C  C     . LEU A 1  598  ? 101.594 134.297 94.311  1.00 12.02  ? 598  LEU A C     1 
ATOM   4535  O  O     . LEU A 1  598  ? 101.567 135.292 93.590  1.00 18.07  ? 598  LEU A O     1 
ATOM   4536  C  CB    . LEU A 1  598  ? 103.902 134.776 95.202  1.00 6.91   ? 598  LEU A CB    1 
ATOM   4537  C  CG    . LEU A 1  598  ? 103.510 135.730 96.320  1.00 10.87  ? 598  LEU A CG    1 
ATOM   4538  C  CD1   . LEU A 1  598  ? 103.125 134.981 97.576  1.00 7.83   ? 598  LEU A CD1   1 
ATOM   4539  C  CD2   . LEU A 1  598  ? 104.672 136.638 96.584  1.00 9.64   ? 598  LEU A CD2   1 
ATOM   4540  N  N     . ILE A 1  599  ? 100.489 133.667 94.708  1.00 9.73   ? 599  ILE A N     1 
ATOM   4541  C  CA    . ILE A 1  599  ? 99.172  134.104 94.260  1.00 11.25  ? 599  ILE A CA    1 
ATOM   4542  C  C     . ILE A 1  599  ? 98.797  135.431 94.901  1.00 14.23  ? 599  ILE A C     1 
ATOM   4543  O  O     . ILE A 1  599  ? 98.279  136.331 94.235  1.00 15.30  ? 599  ILE A O     1 
ATOM   4544  C  CB    . ILE A 1  599  ? 98.121  133.018 94.556  1.00 19.25  ? 599  ILE A CB    1 
ATOM   4545  C  CG1   . ILE A 1  599  ? 98.558  131.677 93.977  1.00 16.10  ? 599  ILE A CG1   1 
ATOM   4546  C  CG2   . ILE A 1  599  ? 96.772  133.412 94.023  1.00 16.52  ? 599  ILE A CG2   1 
ATOM   4547  C  CD1   . ILE A 1  599  ? 98.752  131.698 92.509  1.00 13.92  ? 599  ILE A CD1   1 
ATOM   4548  N  N     . GLU A 1  600  ? 99.043  135.572 96.199  1.00 13.05  ? 600  GLU A N     1 
ATOM   4549  C  CA    . GLU A 1  600  ? 98.645  136.762 96.933  1.00 7.85   ? 600  GLU A CA    1 
ATOM   4550  C  C     . GLU A 1  600  ? 99.394  136.810 98.252  1.00 14.02  ? 600  GLU A C     1 
ATOM   4551  O  O     . GLU A 1  600  ? 100.055 135.854 98.646  1.00 18.45  ? 600  GLU A O     1 
ATOM   4552  C  CB    . GLU A 1  600  ? 97.145  136.776 97.176  1.00 6.91   ? 600  GLU A CB    1 
ATOM   4553  C  CG    . GLU A 1  600  ? 96.622  135.453 97.644  1.00 12.85  ? 600  GLU A CG    1 
ATOM   4554  C  CD    . GLU A 1  600  ? 95.202  135.544 98.109  1.00 25.42  ? 600  GLU A CD    1 
ATOM   4555  O  OE1   . GLU A 1  600  ? 94.661  136.667 98.112  1.00 27.85  ? 600  GLU A OE1   1 
ATOM   4556  O  OE2   . GLU A 1  600  ? 94.620  134.496 98.451  1.00 23.51  ? 600  GLU A OE2   1 
ATOM   4557  N  N     . GLY A 1  601  ? 99.279  137.944 98.929  1.00 10.82  ? 601  GLY A N     1 
ATOM   4558  C  CA    . GLY A 1  601  ? 99.843  138.126 100.249 1.00 4.08   ? 601  GLY A CA    1 
ATOM   4559  C  C     . GLY A 1  601  ? 101.267 138.651 100.225 1.00 1.30   ? 601  GLY A C     1 
ATOM   4560  O  O     . GLY A 1  601  ? 101.942 138.672 99.202  1.00 9.76   ? 601  GLY A O     1 
ATOM   4561  N  N     . VAL A 1  602  ? 101.727 139.059 101.387 1.00 8.31   ? 602  VAL A N     1 
ATOM   4562  C  CA    . VAL A 1  602  ? 103.058 139.621 101.524 1.00 3.72   ? 602  VAL A CA    1 
ATOM   4563  C  C     . VAL A 1  602  ? 103.988 138.595 102.161 1.00 6.47   ? 602  VAL A C     1 
ATOM   4564  O  O     . VAL A 1  602  ? 103.576 137.730 102.930 1.00 8.09   ? 602  VAL A O     1 
ATOM   4565  C  CB    . VAL A 1  602  ? 103.039 140.931 102.338 1.00 2.03   ? 602  VAL A CB    1 
ATOM   4566  C  CG1   . VAL A 1  602  ? 102.274 142.002 101.604 1.00 11.99  ? 602  VAL A CG1   1 
ATOM   4567  C  CG2   . VAL A 1  602  ? 102.449 140.697 103.703 1.00 2.62   ? 602  VAL A CG2   1 
ATOM   4568  N  N     . LEU A 1  603  ? 105.269 138.710 101.839 1.00 6.89   ? 603  LEU A N     1 
ATOM   4569  C  CA    . LEU A 1  603  ? 106.315 137.878 102.409 1.00 7.02   ? 603  LEU A CA    1 
ATOM   4570  C  C     . LEU A 1  603  ? 106.997 138.665 103.512 1.00 4.51   ? 603  LEU A C     1 
ATOM   4571  O  O     . LEU A 1  603  ? 107.538 139.739 103.260 1.00 7.97   ? 603  LEU A O     1 
ATOM   4572  C  CB    . LEU A 1  603  ? 107.334 137.474 101.348 1.00 0.67   ? 603  LEU A CB    1 
ATOM   4573  C  CG    . LEU A 1  603  ? 106.891 136.645 100.148 1.00 3.27   ? 603  LEU A CG    1 
ATOM   4574  C  CD1   . LEU A 1  603  ? 108.041 136.553 99.186  1.00 6.51   ? 603  LEU A CD1   1 
ATOM   4575  C  CD2   . LEU A 1  603  ? 106.420 135.275 100.565 1.00 10.51  ? 603  LEU A CD2   1 
ATOM   4576  N  N     . ASP A 1  604  ? 106.963 138.144 104.728 1.00 1.21   ? 604  ASP A N     1 
ATOM   4577  C  CA    . ASP A 1  604  ? 107.663 138.766 105.842 1.00 0.64   ? 604  ASP A CA    1 
ATOM   4578  C  C     . ASP A 1  604  ? 108.057 137.658 106.807 1.00 0.82   ? 604  ASP A C     1 
ATOM   4579  O  O     . ASP A 1  604  ? 108.195 136.502 106.406 1.00 9.39   ? 604  ASP A O     1 
ATOM   4580  C  CB    . ASP A 1  604  ? 106.829 139.889 106.480 1.00 0.93   ? 604  ASP A CB    1 
ATOM   4581  C  CG    . ASP A 1  604  ? 105.454 139.455 106.866 1.00 2.00   ? 604  ASP A CG    1 
ATOM   4582  O  OD1   . ASP A 1  604  ? 105.110 138.285 106.666 1.00 12.31  ? 604  ASP A OD1   1 
ATOM   4583  O  OD2   . ASP A 1  604  ? 104.702 140.297 107.368 1.00 5.33   ? 604  ASP A OD2   1 
ATOM   4584  N  N     . LYS A 1  605  ? 108.267 138.015 108.072 1.00 2.87   ? 605  LYS A N     1 
ATOM   4585  C  CA    . LYS A 1  605  ? 108.907 137.118 109.025 1.00 13.84  ? 605  LYS A CA    1 
ATOM   4586  C  C     . LYS A 1  605  ? 108.254 135.746 109.090 1.00 5.74   ? 605  LYS A C     1 
ATOM   4587  O  O     . LYS A 1  605  ? 108.941 134.747 109.303 1.00 5.83   ? 605  LYS A O     1 
ATOM   4588  C  CB    . LYS A 1  605  ? 108.898 137.752 110.405 1.00 8.98   ? 605  LYS A CB    1 
ATOM   4589  C  CG    . LYS A 1  605  ? 109.636 136.980 111.448 1.00 5.81   ? 605  LYS A CG    1 
ATOM   4590  C  CD    . LYS A 1  605  ? 109.273 137.463 112.817 1.00 2.27   ? 605  LYS A CD    1 
ATOM   4591  C  CE    . LYS A 1  605  ? 110.231 136.957 113.857 1.00 0.06   ? 605  LYS A CE    1 
ATOM   4592  N  NZ    . LYS A 1  605  ? 110.061 135.526 114.094 1.00 10.77  ? 605  LYS A NZ    1 
ATOM   4593  N  N     . LYS A 1  606  ? 106.938 135.673 108.917 1.00 3.42   ? 606  LYS A N     1 
ATOM   4594  C  CA    . LYS A 1  606  ? 106.246 134.396 109.029 1.00 9.13   ? 606  LYS A CA    1 
ATOM   4595  C  C     . LYS A 1  606  ? 106.650 133.437 107.916 1.00 1.39   ? 606  LYS A C     1 
ATOM   4596  O  O     . LYS A 1  606  ? 106.678 132.221 108.121 1.00 11.14  ? 606  LYS A O     1 
ATOM   4597  C  CB    . LYS A 1  606  ? 104.742 134.631 109.029 1.00 1.91   ? 606  LYS A CB    1 
ATOM   4598  C  CG    . LYS A 1  606  ? 103.923 133.457 109.487 1.00 0.24   ? 606  LYS A CG    1 
ATOM   4599  C  CD    . LYS A 1  606  ? 104.137 133.210 110.938 1.00 2.65   ? 606  LYS A CD    1 
ATOM   4600  C  CE    . LYS A 1  606  ? 103.465 131.945 111.375 1.00 4.11   ? 606  LYS A CE    1 
ATOM   4601  N  NZ    . LYS A 1  606  ? 103.852 131.584 112.759 1.00 8.49   ? 606  LYS A NZ    1 
ATOM   4602  N  N     . ALA A 1  607  ? 106.976 133.959 106.740 1.00 2.95   ? 607  ALA A N     1 
ATOM   4603  C  CA    . ALA A 1  607  ? 107.291 133.133 105.585 1.00 11.50  ? 607  ALA A CA    1 
ATOM   4604  C  C     . ALA A 1  607  ? 108.789 133.033 105.333 1.00 0.92   ? 607  ALA A C     1 
ATOM   4605  O  O     . ALA A 1  607  ? 109.304 131.941 105.094 1.00 3.92   ? 607  ALA A O     1 
ATOM   4606  C  CB    . ALA A 1  607  ? 106.584 133.680 104.347 1.00 11.79  ? 607  ALA A CB    1 
ATOM   4607  N  N     . VAL A 1  608  ? 109.508 134.154 105.388 1.00 7.42   ? 608  VAL A N     1 
ATOM   4608  C  CA    . VAL A 1  608  ? 110.907 134.185 104.986 1.00 1.64   ? 608  VAL A CA    1 
ATOM   4609  C  C     . VAL A 1  608  ? 111.858 134.351 106.156 1.00 2.68   ? 608  VAL A C     1 
ATOM   4610  O  O     . VAL A 1  608  ? 113.066 134.193 105.974 1.00 7.43   ? 608  VAL A O     1 
ATOM   4611  C  CB    . VAL A 1  608  ? 111.166 135.290 103.938 1.00 13.08  ? 608  VAL A CB    1 
ATOM   4612  C  CG1   . VAL A 1  608  ? 110.331 135.069 102.716 1.00 11.31  ? 608  VAL A CG1   1 
ATOM   4613  C  CG2   . VAL A 1  608  ? 110.903 136.660 104.507 1.00 11.97  ? 608  VAL A CG2   1 
ATOM   4614  N  N     . GLY A 1  609  ? 111.361 134.630 107.348 1.00 4.44   ? 609  GLY A N     1 
ATOM   4615  C  CA    . GLY A 1  609  ? 112.229 134.937 108.462 1.00 10.73  ? 609  GLY A CA    1 
ATOM   4616  C  C     . GLY A 1  609  ? 113.073 133.759 108.912 1.00 2.93   ? 609  GLY A C     1 
ATOM   4617  O  O     . GLY A 1  609  ? 112.792 132.598 108.641 1.00 13.66  ? 609  GLY A O     1 
ATOM   4618  N  N     . ALA A 1  610  ? 114.144 134.080 109.627 1.00 4.23   ? 610  ALA A N     1 
ATOM   4619  C  CA    . ALA A 1  610  ? 115.087 133.087 110.117 1.00 0.91   ? 610  ALA A CA    1 
ATOM   4620  C  C     . ALA A 1  610  ? 114.500 132.345 111.307 1.00 4.77   ? 610  ALA A C     1 
ATOM   4621  O  O     . ALA A 1  610  ? 114.038 132.966 112.267 1.00 14.36  ? 610  ALA A O     1 
ATOM   4622  C  CB    . ALA A 1  610  ? 116.403 133.747 110.511 1.00 13.32  ? 610  ALA A CB    1 
ATOM   4623  N  N     . GLY A 1  611  ? 114.538 131.020 111.253 1.00 1.52   ? 611  GLY A N     1 
ATOM   4624  C  CA    . GLY A 1  611  ? 113.969 130.216 112.307 1.00 8.89   ? 611  GLY A CA    1 
ATOM   4625  C  C     . GLY A 1  611  ? 112.473 130.044 112.248 1.00 2.57   ? 611  GLY A C     1 
ATOM   4626  O  O     . GLY A 1  611  ? 111.860 129.746 113.274 1.00 11.68  ? 611  GLY A O     1 
ATOM   4627  N  N     . SER A 1  612  ? 111.868 130.214 111.083 1.00 0.39   ? 612  SER A N     1 
ATOM   4628  C  CA    . SER A 1  612  ? 110.425 130.129 110.917 1.00 1.34   ? 612  SER A CA    1 
ATOM   4629  C  C     . SER A 1  612  ? 110.062 128.703 110.532 1.00 8.81   ? 612  SER A C     1 
ATOM   4630  O  O     . SER A 1  612  ? 110.428 128.234 109.453 1.00 3.24   ? 612  SER A O     1 
ATOM   4631  C  CB    . SER A 1  612  ? 109.963 131.131 109.863 1.00 2.36   ? 612  SER A CB    1 
ATOM   4632  O  OG    . SER A 1  612  ? 108.573 131.056 109.642 1.00 9.69   ? 612  SER A OG    1 
ATOM   4633  N  N     . SER A 1  613  ? 109.348 128.011 111.414 1.00 2.45   ? 613  SER A N     1 
ATOM   4634  C  CA    . SER A 1  613  ? 108.952 126.634 111.150 1.00 8.52   ? 613  SER A CA    1 
ATOM   4635  C  C     . SER A 1  613  ? 107.792 126.594 110.173 1.00 3.37   ? 613  SER A C     1 
ATOM   4636  O  O     . SER A 1  613  ? 106.811 127.323 110.328 1.00 10.88  ? 613  SER A O     1 
ATOM   4637  C  CB    . SER A 1  613  ? 108.563 125.929 112.441 1.00 1.91   ? 613  SER A CB    1 
ATOM   4638  O  OG    . SER A 1  613  ? 109.693 125.655 113.232 1.00 5.17   ? 613  SER A OG    1 
ATOM   4639  N  N     . GLY A 1  614  ? 107.896 125.731 109.175 1.00 12.68  ? 614  GLY A N     1 
ATOM   4640  C  CA    . GLY A 1  614  ? 106.880 125.640 108.162 1.00 12.03  ? 614  GLY A CA    1 
ATOM   4641  C  C     . GLY A 1  614  ? 106.897 126.749 107.143 1.00 4.53   ? 614  GLY A C     1 
ATOM   4642  O  O     . GLY A 1  614  ? 105.950 126.852 106.360 1.00 5.22   ? 614  GLY A O     1 
ATOM   4643  N  N     . GLY A 1  615  ? 107.937 127.577 107.125 1.00 3.01   ? 615  GLY A N     1 
ATOM   4644  C  CA    . GLY A 1  615  ? 108.068 128.648 106.168 1.00 9.78   ? 615  GLY A CA    1 
ATOM   4645  C  C     . GLY A 1  615  ? 108.636 128.179 104.846 1.00 1.66   ? 615  GLY A C     1 
ATOM   4646  O  O     . GLY A 1  615  ? 108.790 126.989 104.583 1.00 3.23   ? 615  GLY A O     1 
ATOM   4647  N  N     . ILE A 1  616  ? 108.975 129.157 104.007 1.00 1.58   ? 616  ILE A N     1 
ATOM   4648  C  CA    . ILE A 1  616  ? 109.314 128.900 102.607 1.00 0.25   ? 616  ILE A CA    1 
ATOM   4649  C  C     . ILE A 1  616  ? 110.537 128.003 102.493 1.00 1.58   ? 616  ILE A C     1 
ATOM   4650  O  O     . ILE A 1  616  ? 110.557 127.048 101.714 1.00 6.68   ? 616  ILE A O     1 
ATOM   4651  C  CB    . ILE A 1  616  ? 109.527 130.237 101.870 1.00 4.54   ? 616  ILE A CB    1 
ATOM   4652  C  CG1   . ILE A 1  616  ? 108.219 131.010 101.802 1.00 4.13   ? 616  ILE A CG1   1 
ATOM   4653  C  CG2   . ILE A 1  616  ? 110.103 130.047 100.499 1.00 1.07   ? 616  ILE A CG2   1 
ATOM   4654  C  CD1   . ILE A 1  616  ? 107.078 130.161 101.475 1.00 0.54   ? 616  ILE A CD1   1 
ATOM   4655  N  N     . TYR A 1  617  ? 111.581 128.310 103.250 1.00 4.88   ? 617  TYR A N     1 
ATOM   4656  C  CA    . TYR A 1  617  ? 112.849 127.609 103.119 1.00 2.95   ? 617  TYR A CA    1 
ATOM   4657  C  C     . TYR A 1  617  ? 112.841 126.268 103.822 1.00 7.04   ? 617  TYR A C     1 
ATOM   4658  O  O     . TYR A 1  617  ? 113.550 125.353 103.405 1.00 8.07   ? 617  TYR A O     1 
ATOM   4659  C  CB    . TYR A 1  617  ? 113.971 128.489 103.657 1.00 15.94  ? 617  TYR A CB    1 
ATOM   4660  C  CG    . TYR A 1  617  ? 113.949 129.870 103.071 1.00 6.07   ? 617  TYR A CG    1 
ATOM   4661  C  CD1   . TYR A 1  617  ? 114.069 130.060 101.708 1.00 10.72  ? 617  TYR A CD1   1 
ATOM   4662  C  CD2   . TYR A 1  617  ? 113.775 130.985 103.872 1.00 15.75  ? 617  TYR A CD2   1 
ATOM   4663  C  CE1   . TYR A 1  617  ? 114.040 131.313 101.167 1.00 2.45   ? 617  TYR A CE1   1 
ATOM   4664  C  CE2   . TYR A 1  617  ? 113.748 132.242 103.334 1.00 8.08   ? 617  TYR A CE2   1 
ATOM   4665  C  CZ    . TYR A 1  617  ? 113.882 132.397 101.980 1.00 9.59   ? 617  TYR A CZ    1 
ATOM   4666  O  OH    . TYR A 1  617  ? 113.857 133.646 101.432 1.00 1.63   ? 617  TYR A OH    1 
ATOM   4667  N  N     . HIS A 1  618  ? 112.063 126.139 104.890 1.00 7.74   ? 618  HIS A N     1 
ATOM   4668  C  CA    . HIS A 1  618  ? 111.844 124.839 105.504 1.00 1.21   ? 618  HIS A CA    1 
ATOM   4669  C  C     . HIS A 1  618  ? 111.165 123.884 104.533 1.00 7.48   ? 618  HIS A C     1 
ATOM   4670  O  O     . HIS A 1  618  ? 111.510 122.703 104.472 1.00 4.65   ? 618  HIS A O     1 
ATOM   4671  C  CB    . HIS A 1  618  ? 111.015 125.015 106.771 1.00 5.16   ? 618  HIS A CB    1 
ATOM   4672  C  CG    . HIS A 1  618  ? 111.056 123.842 107.696 1.00 1.18   ? 618  HIS A CG    1 
ATOM   4673  N  ND1   . HIS A 1  618  ? 110.198 123.714 108.761 1.00 5.21   ? 618  HIS A ND1   1 
ATOM   4674  C  CD2   . HIS A 1  618  ? 111.848 122.747 107.719 1.00 14.27  ? 618  HIS A CD2   1 
ATOM   4675  C  CE1   . HIS A 1  618  ? 110.457 122.591 109.401 1.00 13.05  ? 618  HIS A CE1   1 
ATOM   4676  N  NE2   . HIS A 1  618  ? 111.454 121.984 108.787 1.00 11.35  ? 618  HIS A NE2   1 
ATOM   4677  N  N     . LEU A 1  619  ? 110.198 124.377 103.763 1.00 14.84  ? 619  LEU A N     1 
ATOM   4678  C  CA    . LEU A 1  619  ? 109.528 123.550 102.765 1.00 0.36   ? 619  LEU A CA    1 
ATOM   4679  C  C     . LEU A 1  619  ? 110.430 123.206 101.592 1.00 12.14  ? 619  LEU A C     1 
ATOM   4680  O  O     . LEU A 1  619  ? 110.332 122.105 101.050 1.00 11.53  ? 619  LEU A O     1 
ATOM   4681  C  CB    . LEU A 1  619  ? 108.274 124.255 102.260 1.00 0.64   ? 619  LEU A CB    1 
ATOM   4682  C  CG    . LEU A 1  619  ? 107.194 124.516 103.299 1.00 1.87   ? 619  LEU A CG    1 
ATOM   4683  C  CD1   . LEU A 1  619  ? 106.191 125.496 102.772 1.00 3.14   ? 619  LEU A CD1   1 
ATOM   4684  C  CD2   . LEU A 1  619  ? 106.533 123.239 103.691 1.00 1.23   ? 619  LEU A CD2   1 
ATOM   4685  N  N     . ILE A 1  620  ? 111.276 124.136 101.155 1.00 2.57   ? 620  ILE A N     1 
ATOM   4686  C  CA    . ILE A 1  620  ? 112.209 123.839 100.077 1.00 7.02   ? 620  ILE A CA    1 
ATOM   4687  C  C     . ILE A 1  620  ? 113.204 122.781 100.522 1.00 6.94   ? 620  ILE A C     1 
ATOM   4688  O  O     . ILE A 1  620  ? 113.589 121.904 99.748  1.00 4.81   ? 620  ILE A O     1 
ATOM   4689  C  CB    . ILE A 1  620  ? 112.917 125.127 99.612  1.00 1.90   ? 620  ILE A CB    1 
ATOM   4690  C  CG1   . ILE A 1  620  ? 111.929 126.077 98.949  1.00 14.57  ? 620  ILE A CG1   1 
ATOM   4691  C  CG2   . ILE A 1  620  ? 114.041 124.820 98.651  1.00 15.50  ? 620  ILE A CG2   1 
ATOM   4692  C  CD1   . ILE A 1  620  ? 112.456 127.465 98.775  1.00 13.75  ? 620  ILE A CD1   1 
ATOM   4693  N  N     . SER A 1  621  ? 113.637 122.848 101.774 1.00 4.65   ? 621  SER A N     1 
ATOM   4694  C  CA    . SER A 1  621  ? 114.586 121.873 102.283 1.00 7.25   ? 621  SER A CA    1 
ATOM   4695  C  C     . SER A 1  621  ? 113.985 120.476 102.316 1.00 4.30   ? 621  SER A C     1 
ATOM   4696  O  O     . SER A 1  621  ? 114.679 119.490 102.063 1.00 8.24   ? 621  SER A O     1 
ATOM   4697  C  CB    . SER A 1  621  ? 115.055 122.295 103.665 1.00 15.02  ? 621  SER A CB    1 
ATOM   4698  O  OG    . SER A 1  621  ? 115.853 121.299 104.246 1.00 8.55   ? 621  SER A OG    1 
ATOM   4699  N  N     . ARG A 1  622  ? 112.698 120.366 102.638 1.00 9.78   ? 622  ARG A N     1 
ATOM   4700  C  CA    . ARG A 1  622  ? 112.066 119.060 102.721 1.00 15.67  ? 622  ARG A CA    1 
ATOM   4701  C  C     . ARG A 1  622  ? 111.893 118.405 101.359 1.00 0.96   ? 622  ARG A C     1 
ATOM   4702  O  O     . ARG A 1  622  ? 111.988 117.182 101.267 1.00 8.21   ? 622  ARG A O     1 
ATOM   4703  C  CB    . ARG A 1  622  ? 110.715 119.173 103.414 1.00 1.42   ? 622  ARG A CB    1 
ATOM   4704  C  CG    . ARG A 1  622  ? 110.769 119.637 104.850 1.00 3.01   ? 622  ARG A CG    1 
ATOM   4705  C  CD    . ARG A 1  622  ? 111.359 118.611 105.781 1.00 2.56   ? 622  ARG A CD    1 
ATOM   4706  N  NE    . ARG A 1  622  ? 110.596 117.373 105.797 1.00 2.78   ? 622  ARG A NE    1 
ATOM   4707  C  CZ    . ARG A 1  622  ? 111.012 116.242 106.345 1.00 2.85   ? 622  ARG A CZ    1 
ATOM   4708  N  NH1   . ARG A 1  622  ? 112.186 116.155 106.937 1.00 5.01   ? 622  ARG A NH1   1 
ATOM   4709  N  NH2   . ARG A 1  622  ? 110.228 115.174 106.298 1.00 4.19   ? 622  ARG A NH2   1 
ATOM   4710  N  N     . ARG A 1  623  ? 111.654 119.175 100.301 1.00 3.58   ? 623  ARG A N     1 
ATOM   4711  C  CA    . ARG A 1  623  ? 111.451 118.606 98.977  1.00 0.41   ? 623  ARG A CA    1 
ATOM   4712  C  C     . ARG A 1  623  ? 112.717 118.508 98.150  1.00 1.27   ? 623  ARG A C     1 
ATOM   4713  O  O     . ARG A 1  623  ? 112.836 117.585 97.343  1.00 8.26   ? 623  ARG A O     1 
ATOM   4714  C  CB    . ARG A 1  623  ? 110.426 119.423 98.191  1.00 0.86   ? 623  ARG A CB    1 
ATOM   4715  C  CG    . ARG A 1  623  ? 109.010 119.103 98.532  1.00 6.51   ? 623  ARG A CG    1 
ATOM   4716  C  CD    . ARG A 1  623  ? 108.029 119.767 97.602  1.00 5.66   ? 623  ARG A CD    1 
ATOM   4717  N  NE    . ARG A 1  623  ? 108.027 119.214 96.256  1.00 5.05   ? 623  ARG A NE    1 
ATOM   4718  C  CZ    . ARG A 1  623  ? 107.161 119.568 95.317  1.00 11.39  ? 623  ARG A CZ    1 
ATOM   4719  N  NH1   . ARG A 1  623  ? 106.214 120.457 95.555  1.00 4.05   ? 623  ARG A NH1   1 
ATOM   4720  N  NH2   . ARG A 1  623  ? 107.245 119.016 94.114  1.00 12.45  ? 623  ARG A NH2   1 
ATOM   4721  N  N     . TYR A 1  624  ? 113.661 119.427 98.314  1.00 2.58   ? 624  TYR A N     1 
ATOM   4722  C  CA    . TYR A 1  624  ? 114.811 119.490 97.431  1.00 7.02   ? 624  TYR A CA    1 
ATOM   4723  C  C     . TYR A 1  624  ? 116.156 119.428 98.128  1.00 2.63   ? 624  TYR A C     1 
ATOM   4724  O  O     . TYR A 1  624  ? 117.173 119.360 97.435  1.00 6.94   ? 624  TYR A O     1 
ATOM   4725  C  CB    . TYR A 1  624  ? 114.756 120.762 96.574  1.00 15.32  ? 624  TYR A CB    1 
ATOM   4726  C  CG    . TYR A 1  624  ? 113.437 120.936 95.875  1.00 13.81  ? 624  TYR A CG    1 
ATOM   4727  C  CD1   . TYR A 1  624  ? 113.149 120.228 94.725  1.00 0.26   ? 624  TYR A CD1   1 
ATOM   4728  C  CD2   . TYR A 1  624  ? 112.470 121.785 96.375  1.00 3.49   ? 624  TYR A CD2   1 
ATOM   4729  C  CE1   . TYR A 1  624  ? 111.953 120.367 94.094  1.00 1.40   ? 624  TYR A CE1   1 
ATOM   4730  C  CE2   . TYR A 1  624  ? 111.267 121.921 95.750  1.00 0.63   ? 624  TYR A CE2   1 
ATOM   4731  C  CZ    . TYR A 1  624  ? 111.016 121.212 94.611  1.00 5.58   ? 624  TYR A CZ    1 
ATOM   4732  O  OH    . TYR A 1  624  ? 109.817 121.352 93.974  1.00 10.48  ? 624  TYR A OH    1 
ATOM   4733  N  N     . GLY A 1  625  ? 116.207 119.445 99.452  1.00 15.72  ? 625  GLY A N     1 
ATOM   4734  C  CA    . GLY A 1  625  ? 117.464 119.389 100.155 1.00 0.98   ? 625  GLY A CA    1 
ATOM   4735  C  C     . GLY A 1  625  ? 117.915 120.719 100.713 1.00 15.00  ? 625  GLY A C     1 
ATOM   4736  O  O     . GLY A 1  625  ? 117.527 121.783 100.239 1.00 3.52   ? 625  GLY A O     1 
ATOM   4737  N  N     . PRO A 1  626  ? 118.760 120.672 101.741 1.00 1.08   ? 626  PRO A N     1 
ATOM   4738  C  CA    . PRO A 1  626  ? 119.180 121.910 102.409 1.00 0.52   ? 626  PRO A CA    1 
ATOM   4739  C  C     . PRO A 1  626  ? 120.132 122.793 101.617 1.00 6.65   ? 626  PRO A C     1 
ATOM   4740  O  O     . PRO A 1  626  ? 120.196 123.988 101.904 1.00 6.83   ? 626  PRO A O     1 
ATOM   4741  C  CB    . PRO A 1  626  ? 119.835 121.392 103.691 1.00 9.73   ? 626  PRO A CB    1 
ATOM   4742  C  CG    . PRO A 1  626  ? 120.234 120.038 103.384 1.00 1.31   ? 626  PRO A CG    1 
ATOM   4743  C  CD    . PRO A 1  626  ? 119.218 119.485 102.466 1.00 3.03   ? 626  PRO A CD    1 
ATOM   4744  N  N     . GLN A 1  627  ? 120.900 122.262 100.665 1.00 9.09   ? 627  GLN A N     1 
ATOM   4745  C  CA    . GLN A 1  627  ? 121.732 123.130 99.840  1.00 1.88   ? 627  GLN A CA    1 
ATOM   4746  C  C     . GLN A 1  627  ? 120.877 123.982 98.923  1.00 7.95   ? 627  GLN A C     1 
ATOM   4747  O  O     . GLN A 1  627  ? 121.212 125.132 98.638  1.00 4.02   ? 627  GLN A O     1 
ATOM   4748  C  CB    . GLN A 1  627  ? 122.726 122.311 99.022  1.00 0.40   ? 627  GLN A CB    1 
ATOM   4749  C  CG    . GLN A 1  627  ? 123.697 123.132 98.185  1.00 4.21   ? 627  GLN A CG    1 
ATOM   4750  C  CD    . GLN A 1  627  ? 124.603 124.022 99.014  1.00 3.98   ? 627  GLN A CD    1 
ATOM   4751  O  OE1   . GLN A 1  627  ? 125.114 123.617 100.048 1.00 13.92  ? 627  GLN A OE1   1 
ATOM   4752  N  NE2   . GLN A 1  627  ? 124.800 125.244 98.563  1.00 0.29   ? 627  GLN A NE2   1 
ATOM   4753  N  N     . GLN A 1  628  ? 119.777 123.421 98.439  1.00 5.29   ? 628  GLN A N     1 
ATOM   4754  C  CA    . GLN A 1  628  ? 118.852 124.156 97.596  1.00 2.81   ? 628  GLN A CA    1 
ATOM   4755  C  C     . GLN A 1  628  ? 118.145 125.260 98.366  1.00 13.66  ? 628  GLN A C     1 
ATOM   4756  O  O     . GLN A 1  628  ? 117.789 126.284 97.784  1.00 6.49   ? 628  GLN A O     1 
ATOM   4757  C  CB    . GLN A 1  628  ? 117.839 123.184 97.008  1.00 7.80   ? 628  GLN A CB    1 
ATOM   4758  C  CG    . GLN A 1  628  ? 117.251 123.631 95.717  1.00 5.11   ? 628  GLN A CG    1 
ATOM   4759  C  CD    . GLN A 1  628  ? 118.267 123.632 94.617  1.00 12.63  ? 628  GLN A CD    1 
ATOM   4760  O  OE1   . GLN A 1  628  ? 118.911 122.621 94.361  1.00 17.19  ? 628  GLN A OE1   1 
ATOM   4761  N  NE2   . GLN A 1  628  ? 118.435 124.774 93.964  1.00 11.45  ? 628  GLN A NE2   1 
ATOM   4762  N  N     . ALA A 1  629  ? 117.909 125.057 99.660  1.00 9.08   ? 629  ALA A N     1 
ATOM   4763  C  CA    . ALA A 1  629  ? 117.276 126.077 100.485 1.00 10.82  ? 629  ALA A CA    1 
ATOM   4764  C  C     . ALA A 1  629  ? 118.219 127.238 100.757 1.00 9.70   ? 629  ALA A C     1 
ATOM   4765  O  O     . ALA A 1  629  ? 117.791 128.393 100.785 1.00 1.55   ? 629  ALA A O     1 
ATOM   4766  C  CB    . ALA A 1  629  ? 116.796 125.463 101.794 1.00 6.88   ? 629  ALA A CB    1 
ATOM   4767  N  N     . LEU A 1  630  ? 119.500 126.948 100.981 1.00 0.65   ? 630  LEU A N     1 
ATOM   4768  C  CA    . LEU A 1  630  ? 120.486 127.997 101.200 1.00 0.37   ? 630  LEU A CA    1 
ATOM   4769  C  C     . LEU A 1  630  ? 120.679 128.840 99.954  1.00 3.38   ? 630  LEU A C     1 
ATOM   4770  O  O     . LEU A 1  630  ? 120.951 130.040 100.044 1.00 13.75  ? 630  LEU A O     1 
ATOM   4771  C  CB    . LEU A 1  630  ? 121.817 127.390 101.617 1.00 6.79   ? 630  LEU A CB    1 
ATOM   4772  C  CG    . LEU A 1  630  ? 121.924 126.633 102.930 1.00 3.47   ? 630  LEU A CG    1 
ATOM   4773  C  CD1   . LEU A 1  630  ? 123.359 126.245 103.137 1.00 9.44   ? 630  LEU A CD1   1 
ATOM   4774  C  CD2   . LEU A 1  630  ? 121.405 127.460 104.076 1.00 11.04  ? 630  LEU A CD2   1 
ATOM   4775  N  N     . LYS A 1  631  ? 120.587 128.216 98.787  1.00 1.50   ? 631  LYS A N     1 
ATOM   4776  C  CA    . LYS A 1  631  ? 120.694 128.932 97.531  1.00 14.02  ? 631  LYS A CA    1 
ATOM   4777  C  C     . LYS A 1  631  ? 119.483 129.822 97.290  1.00 2.93   ? 631  LYS A C     1 
ATOM   4778  O  O     . LYS A 1  631  ? 119.598 130.860 96.634  1.00 4.24   ? 631  LYS A O     1 
ATOM   4779  C  CB    . LYS A 1  631  ? 120.886 127.922 96.405  1.00 3.34   ? 631  LYS A CB    1 
ATOM   4780  C  CG    . LYS A 1  631  ? 120.845 128.490 95.014  1.00 8.98   ? 631  LYS A CG    1 
ATOM   4781  C  CD    . LYS A 1  631  ? 122.237 128.759 94.487  1.00 10.32  ? 631  LYS A CD    1 
ATOM   4782  C  CE    . LYS A 1  631  ? 122.272 129.948 93.534  1.00 8.52   ? 631  LYS A CE    1 
ATOM   4783  N  NZ    . LYS A 1  631  ? 122.304 131.265 94.212  1.00 6.68   ? 631  LYS A NZ    1 
ATOM   4784  N  N     . MET A 1  632  ? 118.323 129.438 97.808  1.00 6.39   ? 632  MET A N     1 
ATOM   4785  C  CA    . MET A 1  632  ? 117.120 130.248 97.696  1.00 7.37   ? 632  MET A CA    1 
ATOM   4786  C  C     . MET A 1  632  ? 117.108 131.413 98.667  1.00 13.62  ? 632  MET A C     1 
ATOM   4787  O  O     . MET A 1  632  ? 116.543 132.459 98.353  1.00 9.98   ? 632  MET A O     1 
ATOM   4788  C  CB    . MET A 1  632  ? 115.892 129.380 97.930  1.00 9.04   ? 632  MET A CB    1 
ATOM   4789  C  CG    . MET A 1  632  ? 115.284 128.830 96.687  1.00 1.02   ? 632  MET A CG    1 
ATOM   4790  S  SD    . MET A 1  632  ? 114.441 130.070 95.707  1.00 16.21  ? 632  MET A SD    1 
ATOM   4791  C  CE    . MET A 1  632  ? 115.438 130.011 94.242  1.00 2.96   ? 632  MET A CE    1 
ATOM   4792  N  N     . ILE A 1  633  ? 117.692 131.247 99.852  1.00 9.75   ? 633  ILE A N     1 
ATOM   4793  C  CA    . ILE A 1  633  ? 117.791 132.355 100.792 1.00 14.99  ? 633  ILE A CA    1 
ATOM   4794  C  C     . ILE A 1  633  ? 118.640 133.467 100.202 1.00 2.79   ? 633  ILE A C     1 
ATOM   4795  O  O     . ILE A 1  633  ? 118.320 134.649 100.337 1.00 3.29   ? 633  ILE A O     1 
ATOM   4796  C  CB    . ILE A 1  633  ? 118.351 131.872 102.142 1.00 6.60   ? 633  ILE A CB    1 
ATOM   4797  C  CG1   . ILE A 1  633  ? 117.405 130.874 102.793 1.00 12.31  ? 633  ILE A CG1   1 
ATOM   4798  C  CG2   . ILE A 1  633  ? 118.575 133.038 103.071 1.00 12.22  ? 633  ILE A CG2   1 
ATOM   4799  C  CD1   . ILE A 1  633  ? 117.970 130.159 103.967 1.00 2.40   ? 633  ILE A CD1   1 
ATOM   4800  N  N     . PHE A 1  634  ? 119.735 133.106 99.543  1.00 10.56  ? 634  PHE A N     1 
ATOM   4801  C  CA    . PHE A 1  634  ? 120.589 134.092 98.899  1.00 2.31   ? 634  PHE A CA    1 
ATOM   4802  C  C     . PHE A 1  634  ? 119.879 134.788 97.749  1.00 5.27   ? 634  PHE A C     1 
ATOM   4803  O  O     . PHE A 1  634  ? 119.992 136.002 97.592  1.00 3.69   ? 634  PHE A O     1 
ATOM   4804  C  CB    . PHE A 1  634  ? 121.867 133.417 98.408  1.00 15.39  ? 634  PHE A CB    1 
ATOM   4805  C  CG    . PHE A 1  634  ? 122.783 134.329 97.671  1.00 9.54   ? 634  PHE A CG    1 
ATOM   4806  C  CD1   . PHE A 1  634  ? 123.648 135.146 98.349  1.00 13.73  ? 634  PHE A CD1   1 
ATOM   4807  C  CD2   . PHE A 1  634  ? 122.767 134.383 96.297  1.00 14.90  ? 634  PHE A CD2   1 
ATOM   4808  C  CE1   . PHE A 1  634  ? 124.472 135.990 97.675  1.00 14.17  ? 634  PHE A CE1   1 
ATOM   4809  C  CE2   . PHE A 1  634  ? 123.587 135.225 95.633  1.00 2.48   ? 634  PHE A CE2   1 
ATOM   4810  C  CZ    . PHE A 1  634  ? 124.444 136.026 96.321  1.00 14.66  ? 634  PHE A CZ    1 
ATOM   4811  N  N     . ALA A 1  635  ? 119.157 134.035 96.926  1.00 10.25  ? 635  ALA A N     1 
ATOM   4812  C  CA    . ALA A 1  635  ? 118.534 134.607 95.742  1.00 7.71   ? 635  ALA A CA    1 
ATOM   4813  C  C     . ALA A 1  635  ? 117.380 135.534 96.099  1.00 6.93   ? 635  ALA A C     1 
ATOM   4814  O  O     . ALA A 1  635  ? 117.226 136.594 95.492  1.00 17.06  ? 635  ALA A O     1 
ATOM   4815  C  CB    . ALA A 1  635  ? 118.066 133.491 94.819  1.00 12.78  ? 635  ALA A CB    1 
ATOM   4816  N  N     . THR A 1  636  ? 116.538 135.147 97.056  1.00 6.79   ? 636  THR A N     1 
ATOM   4817  C  CA    . THR A 1  636  ? 115.449 136.016 97.475  1.00 11.96  ? 636  THR A CA    1 
ATOM   4818  C  C     . THR A 1  636  ? 115.937 137.203 98.282  1.00 0.26   ? 636  THR A C     1 
ATOM   4819  O  O     . THR A 1  636  ? 115.211 138.184 98.419  1.00 5.26   ? 636  THR A O     1 
ATOM   4820  C  CB    . THR A 1  636  ? 114.423 135.240 98.298  1.00 0.41   ? 636  THR A CB    1 
ATOM   4821  O  OG1   . THR A 1  636  ? 115.090 134.515 99.327  1.00 3.25   ? 636  THR A OG1   1 
ATOM   4822  C  CG2   . THR A 1  636  ? 113.666 134.275 97.448  1.00 3.70   ? 636  THR A CG2   1 
ATOM   4823  N  N     . GLN A 1  637  ? 117.138 137.120 98.834  1.00 11.25  ? 637  GLN A N     1 
ATOM   4824  C  CA    . GLN A 1  637  ? 117.732 138.235 99.552  1.00 14.69  ? 637  GLN A CA    1 
ATOM   4825  C  C     . GLN A 1  637  ? 118.280 139.286 98.600  1.00 6.09   ? 637  GLN A C     1 
ATOM   4826  O  O     . GLN A 1  637  ? 118.297 140.473 98.926  1.00 5.61   ? 637  GLN A O     1 
ATOM   4827  C  CB    . GLN A 1  637  ? 118.818 137.698 100.463 1.00 8.96   ? 637  GLN A CB    1 
ATOM   4828  C  CG    . GLN A 1  637  ? 119.834 138.672 100.880 1.00 2.33   ? 637  GLN A CG    1 
ATOM   4829  C  CD    . GLN A 1  637  ? 120.825 138.060 101.799 1.00 1.06   ? 637  GLN A CD    1 
ATOM   4830  O  OE1   . GLN A 1  637  ? 120.606 136.981 102.328 1.00 1.96   ? 637  GLN A OE1   1 
ATOM   4831  N  NE2   . GLN A 1  637  ? 121.943 138.726 101.979 1.00 5.97   ? 637  GLN A NE2   1 
ATOM   4832  N  N     . GLN A 1  638  ? 118.742 138.873 97.426  1.00 5.48   ? 638  GLN A N     1 
ATOM   4833  C  CA    . GLN A 1  638  ? 119.202 139.817 96.419  1.00 12.68  ? 638  GLN A CA    1 
ATOM   4834  C  C     . GLN A 1  638  ? 118.042 140.489 95.706  1.00 9.37   ? 638  GLN A C     1 
ATOM   4835  O  O     . GLN A 1  638  ? 118.148 141.653 95.324  1.00 13.27  ? 638  GLN A O     1 
ATOM   4836  C  CB    . GLN A 1  638  ? 120.107 139.113 95.404  1.00 11.66  ? 638  GLN A CB    1 
ATOM   4837  C  CG    . GLN A 1  638  ? 121.295 138.384 95.982  1.00 8.69   ? 638  GLN A CG    1 
ATOM   4838  C  CD    . GLN A 1  638  ? 122.188 139.271 96.811  1.00 4.23   ? 638  GLN A CD    1 
ATOM   4839  O  OE1   . GLN A 1  638  ? 122.507 140.378 96.423  1.00 1.08   ? 638  GLN A OE1   1 
ATOM   4840  N  NE2   . GLN A 1  638  ? 122.595 138.784 97.963  1.00 4.29   ? 638  GLN A NE2   1 
ATOM   4841  N  N     . LEU A 1  639  ? 116.935 139.777 95.505  1.00 0.19   ? 639  LEU A N     1 
ATOM   4842  C  CA    . LEU A 1  639  ? 115.727 140.415 94.996  1.00 9.72   ? 639  LEU A CA    1 
ATOM   4843  C  C     . LEU A 1  639  ? 115.228 141.495 95.937  1.00 2.96   ? 639  LEU A C     1 
ATOM   4844  O  O     . LEU A 1  639  ? 114.809 142.565 95.496  1.00 10.49  ? 639  LEU A O     1 
ATOM   4845  C  CB    . LEU A 1  639  ? 114.624 139.386 94.775  1.00 10.43  ? 639  LEU A CB    1 
ATOM   4846  C  CG    . LEU A 1  639  ? 114.236 138.948 93.367  1.00 0.95   ? 639  LEU A CG    1 
ATOM   4847  C  CD1   . LEU A 1  639  ? 115.401 138.544 92.553  1.00 0.26   ? 639  LEU A CD1   1 
ATOM   4848  C  CD2   . LEU A 1  639  ? 113.238 137.817 93.464  1.00 4.01   ? 639  LEU A CD2   1 
ATOM   4849  N  N     . ALA A 1  640  ? 115.226 141.218 97.235  1.00 9.87   ? 640  ALA A N     1 
ATOM   4850  C  CA    . ALA A 1  640  ? 114.712 142.181 98.195  1.00 2.67   ? 640  ALA A CA    1 
ATOM   4851  C  C     . ALA A 1  640  ? 115.630 143.382 98.318  1.00 5.92   ? 640  ALA A C     1 
ATOM   4852  O  O     . ALA A 1  640  ? 115.163 144.508 98.482  1.00 15.74  ? 640  ALA A O     1 
ATOM   4853  C  CB    . ALA A 1  640  ? 114.520 141.514 99.550  1.00 9.75   ? 640  ALA A CB    1 
ATOM   4854  N  N     . LEU A 1  641  ? 116.939 143.163 98.256  1.00 7.81   ? 641  LEU A N     1 
ATOM   4855  C  CA    . LEU A 1  641  ? 117.877 144.265 98.397  1.00 9.88   ? 641  LEU A CA    1 
ATOM   4856  C  C     . LEU A 1  641  ? 117.904 145.142 97.164  1.00 15.63  ? 641  LEU A C     1 
ATOM   4857  O  O     . LEU A 1  641  ? 118.067 146.356 97.280  1.00 8.02   ? 641  LEU A O     1 
ATOM   4858  C  CB    . LEU A 1  641  ? 119.277 143.740 98.692  1.00 1.07   ? 641  LEU A CB    1 
ATOM   4859  C  CG    . LEU A 1  641  ? 119.513 143.152 100.078 1.00 2.96   ? 641  LEU A CG    1 
ATOM   4860  C  CD1   . LEU A 1  641  ? 120.883 142.517 100.151 1.00 1.50   ? 641  LEU A CD1   1 
ATOM   4861  C  CD2   . LEU A 1  641  ? 119.340 144.195 101.140 1.00 13.28  ? 641  LEU A CD2   1 
ATOM   4862  N  N     . ASN A 1  642  ? 117.789 144.553 95.982  1.00 0.27   ? 642  ASN A N     1 
ATOM   4863  C  CA    . ASN A 1  642  ? 117.773 145.339 94.762  1.00 3.25   ? 642  ASN A CA    1 
ATOM   4864  C  C     . ASN A 1  642  ? 116.480 146.107 94.587  1.00 1.39   ? 642  ASN A C     1 
ATOM   4865  O  O     . ASN A 1  642  ? 116.470 147.114 93.881  1.00 9.35   ? 642  ASN A O     1 
ATOM   4866  C  CB    . ASN A 1  642  ? 118.001 144.451 93.545  1.00 9.56   ? 642  ASN A CB    1 
ATOM   4867  C  CG    . ASN A 1  642  ? 119.389 143.893 93.487  1.00 0.85   ? 642  ASN A CG    1 
ATOM   4868  O  OD1   . ASN A 1  642  ? 120.318 144.472 94.018  1.00 15.21  ? 642  ASN A OD1   1 
ATOM   4869  N  ND2   . ASN A 1  642  ? 119.546 142.774 92.807  1.00 0.86   ? 642  ASN A ND2   1 
ATOM   4870  N  N     . TYR A 1  643  ? 115.392 145.650 95.193  1.00 13.15  ? 643  TYR A N     1 
ATOM   4871  C  CA    . TYR A 1  643  ? 114.157 146.421 95.187  1.00 4.04   ? 643  TYR A CA    1 
ATOM   4872  C  C     . TYR A 1  643  ? 114.291 147.690 96.015  1.00 12.07  ? 643  TYR A C     1 
ATOM   4873  O  O     . TYR A 1  643  ? 113.821 148.755 95.612  1.00 2.80   ? 643  TYR A O     1 
ATOM   4874  C  CB    . TYR A 1  643  ? 113.000 145.566 95.705  1.00 6.20   ? 643  TYR A CB    1 
ATOM   4875  C  CG    . TYR A 1  643  ? 111.687 146.299 95.702  1.00 7.88   ? 643  TYR A CG    1 
ATOM   4876  C  CD1   . TYR A 1  643  ? 110.906 146.362 94.569  1.00 1.35   ? 643  TYR A CD1   1 
ATOM   4877  C  CD2   . TYR A 1  643  ? 111.248 146.955 96.828  1.00 7.87   ? 643  TYR A CD2   1 
ATOM   4878  C  CE1   . TYR A 1  643  ? 109.734 147.043 94.573  1.00 1.45   ? 643  TYR A CE1   1 
ATOM   4879  C  CE2   . TYR A 1  643  ? 110.091 147.636 96.827  1.00 7.51   ? 643  TYR A CE2   1 
ATOM   4880  C  CZ    . TYR A 1  643  ? 109.335 147.678 95.702  1.00 9.76   ? 643  TYR A CZ    1 
ATOM   4881  O  OH    . TYR A 1  643  ? 108.157 148.364 95.710  1.00 9.08   ? 643  TYR A OH    1 
ATOM   4882  N  N     . VAL A 1  644  ? 114.917 147.591 97.186  1.00 0.40   ? 644  VAL A N     1 
ATOM   4883  C  CA    . VAL A 1  644  ? 115.037 148.728 98.088  1.00 9.02   ? 644  VAL A CA    1 
ATOM   4884  C  C     . VAL A 1  644  ? 116.092 149.707 97.596  1.00 3.23   ? 644  VAL A C     1 
ATOM   4885  O  O     . VAL A 1  644  ? 116.154 150.850 98.060  1.00 3.28   ? 644  VAL A O     1 
ATOM   4886  C  CB    . VAL A 1  644  ? 115.328 148.227 99.514  1.00 1.99   ? 644  VAL A CB    1 
ATOM   4887  C  CG1   . VAL A 1  644  ? 115.336 149.357 100.503 1.00 10.17  ? 644  VAL A CG1   1 
ATOM   4888  C  CG2   . VAL A 1  644  ? 114.292 147.239 99.918  1.00 4.16   ? 644  VAL A CG2   1 
ATOM   4889  N  N     . ARG A 1  645  ? 116.932 149.300 96.659  1.00 11.58  ? 645  ARG A N     1 
ATOM   4890  C  CA    . ARG A 1  645  ? 117.860 150.277 96.126  1.00 14.49  ? 645  ARG A CA    1 
ATOM   4891  C  C     . ARG A 1  645  ? 117.215 151.158 95.083  1.00 12.48  ? 645  ARG A C     1 
ATOM   4892  O  O     . ARG A 1  645  ? 117.892 151.982 94.475  1.00 23.31  ? 645  ARG A O     1 
ATOM   4893  C  CB    . ARG A 1  645  ? 119.107 149.582 95.587  1.00 17.90  ? 645  ARG A CB    1 
ATOM   4894  C  CG    . ARG A 1  645  ? 119.053 149.104 94.178  1.00 16.70  ? 645  ARG A CG    1 
ATOM   4895  C  CD    . ARG A 1  645  ? 120.432 148.656 93.776  1.00 20.87  ? 645  ARG A CD    1 
ATOM   4896  N  NE    . ARG A 1  645  ? 120.812 147.454 94.504  1.00 25.06  ? 645  ARG A NE    1 
ATOM   4897  C  CZ    . ARG A 1  645  ? 121.686 147.400 95.499  1.00 30.00  ? 645  ARG A CZ    1 
ATOM   4898  N  NH1   . ARG A 1  645  ? 122.341 148.476 95.908  1.00 26.19  ? 645  ARG A NH1   1 
ATOM   4899  N  NH2   . ARG A 1  645  ? 121.910 146.234 96.097  1.00 22.38  ? 645  ARG A NH2   1 
ATOM   4900  N  N     . ASN A 1  646  ? 115.916 151.012 94.888  1.00 14.38  ? 646  ASN A N     1 
ATOM   4901  C  CA    . ASN A 1  646  ? 115.119 151.936 94.117  1.00 10.64  ? 646  ASN A CA    1 
ATOM   4902  C  C     . ASN A 1  646  ? 113.998 152.550 94.927  1.00 1.11   ? 646  ASN A C     1 
ATOM   4903  O  O     . ASN A 1  646  ? 113.483 153.597 94.541  1.00 2.52   ? 646  ASN A O     1 
ATOM   4904  C  CB    . ASN A 1  646  ? 114.524 151.219 92.901  1.00 6.36   ? 646  ASN A CB    1 
ATOM   4905  C  CG    . ASN A 1  646  ? 114.780 151.948 91.625  1.00 4.29   ? 646  ASN A CG    1 
ATOM   4906  O  OD1   . ASN A 1  646  ? 114.523 153.133 91.510  1.00 13.01  ? 646  ASN A OD1   1 
ATOM   4907  N  ND2   . ASN A 1  646  ? 115.354 151.253 90.671  1.00 4.86   ? 646  ASN A ND2   1 
ATOM   4908  N  N     . ALA A 1  647  ? 113.625 151.945 96.045  1.00 1.12   ? 647  ALA A N     1 
ATOM   4909  C  CA    . ALA A 1  647  ? 112.482 152.358 96.838  1.00 7.71   ? 647  ALA A CA    1 
ATOM   4910  C  C     . ALA A 1  647  ? 112.861 153.156 98.070  1.00 2.42   ? 647  ALA A C     1 
ATOM   4911  O  O     . ALA A 1  647  ? 112.127 154.067 98.443  1.00 8.01   ? 647  ALA A O     1 
ATOM   4912  C  CB    . ALA A 1  647  ? 111.677 151.131 97.269  1.00 15.23  ? 647  ALA A CB    1 
ATOM   4913  N  N     . GLY A 1  648  ? 113.970 152.836 98.716  1.00 4.17   ? 648  GLY A N     1 
ATOM   4914  C  CA    . GLY A 1  648  ? 114.390 153.564 99.888  1.00 6.41   ? 648  GLY A CA    1 
ATOM   4915  C  C     . GLY A 1  648  ? 113.759 153.069 101.166 1.00 10.84  ? 648  GLY A C     1 
ATOM   4916  O  O     . GLY A 1  648  ? 112.672 152.501 101.153 1.00 24.44  ? 648  GLY A O     1 
ATOM   4917  N  N     . PHE A 1  649  ? 114.442 153.273 102.281 1.00 1.13   ? 649  PHE A N     1 
ATOM   4918  C  CA    . PHE A 1  649  ? 113.875 152.962 103.580 1.00 2.77   ? 649  PHE A CA    1 
ATOM   4919  C  C     . PHE A 1  649  ? 114.680 153.710 104.625 1.00 1.17   ? 649  PHE A C     1 
ATOM   4920  O  O     . PHE A 1  649  ? 115.891 153.536 104.705 1.00 3.24   ? 649  PHE A O     1 
ATOM   4921  C  CB    . PHE A 1  649  ? 113.887 151.458 103.850 1.00 14.35  ? 649  PHE A CB    1 
ATOM   4922  C  CG    . PHE A 1  649  ? 113.095 151.063 105.040 1.00 2.35   ? 649  PHE A CG    1 
ATOM   4923  C  CD1   . PHE A 1  649  ? 111.731 150.951 104.962 1.00 1.11   ? 649  PHE A CD1   1 
ATOM   4924  C  CD2   . PHE A 1  649  ? 113.713 150.808 106.240 1.00 15.44  ? 649  PHE A CD2   1 
ATOM   4925  C  CE1   . PHE A 1  649  ? 111.006 150.600 106.052 1.00 7.55   ? 649  PHE A CE1   1 
ATOM   4926  C  CE2   . PHE A 1  649  ? 112.994 150.462 107.323 1.00 1.44   ? 649  PHE A CE2   1 
ATOM   4927  C  CZ    . PHE A 1  649  ? 111.638 150.355 107.235 1.00 1.53   ? 649  PHE A CZ    1 
ATOM   4928  N  N     . THR A 1  650  ? 114.008 154.535 105.418 1.00 7.93   ? 650  THR A N     1 
ATOM   4929  C  CA    . THR A 1  650  ? 114.685 155.371 106.392 1.00 10.96  ? 650  THR A CA    1 
ATOM   4930  C  C     . THR A 1  650  ? 113.871 155.376 107.677 1.00 5.25   ? 650  THR A C     1 
ATOM   4931  O  O     . THR A 1  650  ? 112.796 154.784 107.749 1.00 7.99   ? 650  THR A O     1 
ATOM   4932  C  CB    . THR A 1  650  ? 114.899 156.788 105.838 1.00 8.35   ? 650  THR A CB    1 
ATOM   4933  O  OG1   . THR A 1  650  ? 116.031 157.381 106.466 1.00 0.55   ? 650  THR A OG1   1 
ATOM   4934  C  CG2   . THR A 1  650  ? 113.697 157.660 106.070 1.00 10.37  ? 650  THR A CG2   1 
ATOM   4935  N  N     . VAL A 1  651  ? 114.426 155.993 108.713 1.00 13.10  ? 651  VAL A N     1 
ATOM   4936  C  CA    . VAL A 1  651  ? 113.683 156.312 109.924 1.00 13.80  ? 651  VAL A CA    1 
ATOM   4937  C  C     . VAL A 1  651  ? 114.138 157.681 110.408 1.00 1.58   ? 651  VAL A C     1 
ATOM   4938  O  O     . VAL A 1  651  ? 115.324 158.011 110.324 1.00 2.01   ? 651  VAL A O     1 
ATOM   4939  C  CB    . VAL A 1  651  ? 113.853 155.225 111.010 1.00 1.60   ? 651  VAL A CB    1 
ATOM   4940  C  CG1   . VAL A 1  651  ? 115.278 155.150 111.513 1.00 3.16   ? 651  VAL A CG1   1 
ATOM   4941  C  CG2   . VAL A 1  651  ? 112.900 155.445 112.142 1.00 3.42   ? 651  VAL A CG2   1 
ATOM   4942  N  N     . SER A 1  652  ? 113.198 158.488 110.880 1.00 7.67   ? 652  SER A N     1 
ATOM   4943  C  CA    . SER A 1  652  ? 113.458 159.855 111.305 1.00 1.58   ? 652  SER A CA    1 
ATOM   4944  C  C     . SER A 1  652  ? 112.916 160.100 112.708 1.00 1.44   ? 652  SER A C     1 
ATOM   4945  O  O     . SER A 1  652  ? 112.215 159.275 113.286 1.00 6.40   ? 652  SER A O     1 
ATOM   4946  C  CB    . SER A 1  652  ? 112.864 160.853 110.312 1.00 2.09   ? 652  SER A CB    1 
ATOM   4947  O  OG    . SER A 1  652  ? 111.503 160.582 110.045 1.00 9.55   ? 652  SER A OG    1 
ATOM   4948  N  N     . THR A 1  653  ? 113.275 161.261 113.260 1.00 5.46   ? 653  THR A N     1 
ATOM   4949  C  CA    . THR A 1  653  ? 112.761 161.673 114.563 1.00 2.08   ? 653  THR A CA    1 
ATOM   4950  C  C     . THR A 1  653  ? 111.270 161.962 114.505 1.00 3.24   ? 653  THR A C     1 
ATOM   4951  O  O     . THR A 1  653  ? 110.566 161.789 115.501 1.00 10.74  ? 653  THR A O     1 
ATOM   4952  C  CB    . THR A 1  653  ? 113.504 162.913 115.057 1.00 1.07   ? 653  THR A CB    1 
ATOM   4953  O  OG1   . THR A 1  653  ? 114.880 162.814 114.703 1.00 4.26   ? 653  THR A OG1   1 
ATOM   4954  C  CG2   . THR A 1  653  ? 113.399 163.040 116.550 1.00 1.86   ? 653  THR A CG2   1 
ATOM   4955  N  N     . ALA A 1  654  ? 110.782 162.412 113.353 1.00 2.74   ? 654  ALA A N     1 
ATOM   4956  C  CA    . ALA A 1  654  ? 109.371 162.681 113.156 1.00 11.11  ? 654  ALA A CA    1 
ATOM   4957  C  C     . ALA A 1  654  ? 108.530 161.417 113.067 1.00 8.58   ? 654  ALA A C     1 
ATOM   4958  O  O     . ALA A 1  654  ? 107.303 161.518 113.091 1.00 19.40  ? 654  ALA A O     1 
ATOM   4959  C  CB    . ALA A 1  654  ? 109.180 163.513 111.898 1.00 2.64   ? 654  ALA A CB    1 
ATOM   4960  N  N     . ASP A 1  655  ? 109.146 160.243 112.940 1.00 8.60   ? 655  ASP A N     1 
ATOM   4961  C  CA    . ASP A 1  655  ? 108.412 158.985 112.941 1.00 5.10   ? 655  ASP A CA    1 
ATOM   4962  C  C     . ASP A 1  655  ? 107.927 158.578 114.321 1.00 5.41   ? 655  ASP A C     1 
ATOM   4963  O  O     . ASP A 1  655  ? 107.049 157.722 114.419 1.00 11.24  ? 655  ASP A O     1 
ATOM   4964  C  CB    . ASP A 1  655  ? 109.277 157.858 112.380 1.00 4.27   ? 655  ASP A CB    1 
ATOM   4965  C  CG    . ASP A 1  655  ? 109.242 157.793 110.883 1.00 11.95  ? 655  ASP A CG    1 
ATOM   4966  O  OD1   . ASP A 1  655  ? 108.384 158.461 110.283 1.00 12.87  ? 655  ASP A OD1   1 
ATOM   4967  O  OD2   . ASP A 1  655  ? 110.050 157.055 110.303 1.00 13.93  ? 655  ASP A OD2   1 
ATOM   4968  N  N     . MET A 1  656  ? 108.479 159.156 115.379 1.00 7.31   ? 656  MET A N     1 
ATOM   4969  C  CA    . MET A 1  656  ? 108.189 158.768 116.749 1.00 4.14   ? 656  MET A CA    1 
ATOM   4970  C  C     . MET A 1  656  ? 107.438 159.850 117.505 1.00 6.09   ? 656  MET A C     1 
ATOM   4971  O  O     . MET A 1  656  ? 107.411 159.838 118.733 1.00 13.16  ? 656  MET A O     1 
ATOM   4972  C  CB    . MET A 1  656  ? 109.493 158.415 117.458 1.00 1.95   ? 656  MET A CB    1 
ATOM   4973  C  CG    . MET A 1  656  ? 110.552 157.902 116.515 1.00 5.30   ? 656  MET A CG    1 
ATOM   4974  S  SD    . MET A 1  656  ? 112.067 157.311 117.274 1.00 21.15  ? 656  MET A SD    1 
ATOM   4975  C  CE    . MET A 1  656  ? 112.882 158.840 117.691 1.00 11.36  ? 656  MET A CE    1 
ATOM   4976  N  N     . LEU A 1  657  ? 106.802 160.765 116.791 1.00 0.71   ? 657  LEU A N     1 
ATOM   4977  C  CA    . LEU A 1  657  ? 106.215 161.961 117.365 1.00 0.86   ? 657  LEU A CA    1 
ATOM   4978  C  C     . LEU A 1  657  ? 104.698 161.903 117.283 1.00 5.39   ? 657  LEU A C     1 
ATOM   4979  O  O     . LEU A 1  657  ? 104.138 161.790 116.192 1.00 12.79  ? 657  LEU A O     1 
ATOM   4980  C  CB    . LEU A 1  657  ? 106.745 163.186 116.635 1.00 7.76   ? 657  LEU A CB    1 
ATOM   4981  C  CG    . LEU A 1  657  ? 106.558 164.556 117.250 1.00 6.17   ? 657  LEU A CG    1 
ATOM   4982  C  CD1   . LEU A 1  657  ? 107.219 164.603 118.591 1.00 5.69   ? 657  LEU A CD1   1 
ATOM   4983  C  CD2   . LEU A 1  657  ? 107.173 165.560 116.316 1.00 3.62   ? 657  LEU A CD2   1 
ATOM   4984  N  N     . LEU A 1  658  ? 104.040 162.000 118.434 1.00 9.40   ? 658  LEU A N     1 
ATOM   4985  C  CA    . LEU A 1  658  ? 102.590 161.996 118.503 1.00 5.57   ? 658  LEU A CA    1 
ATOM   4986  C  C     . LEU A 1  658  ? 102.031 163.337 118.065 1.00 8.45   ? 658  LEU A C     1 
ATOM   4987  O  O     . LEU A 1  658  ? 102.652 164.384 118.243 1.00 19.06  ? 658  LEU A O     1 
ATOM   4988  C  CB    . LEU A 1  658  ? 102.087 161.692 119.913 1.00 6.01   ? 658  LEU A CB    1 
ATOM   4989  C  CG    . LEU A 1  658  ? 102.130 160.265 120.449 1.00 2.17   ? 658  LEU A CG    1 
ATOM   4990  C  CD1   . LEU A 1  658  ? 101.449 160.223 121.784 1.00 6.03   ? 658  LEU A CD1   1 
ATOM   4991  C  CD2   . LEU A 1  658  ? 101.519 159.278 119.504 1.00 7.42   ? 658  LEU A CD2   1 
ATOM   4992  N  N     . THR A 1  659  ? 100.845 163.287 117.489 1.00 10.17  ? 659  THR A N     1 
ATOM   4993  C  CA    . THR A 1  659  ? 100.137 164.488 117.102 1.00 11.05  ? 659  THR A CA    1 
ATOM   4994  C  C     . THR A 1  659  ? 99.664  165.233 118.356 1.00 17.50  ? 659  THR A C     1 
ATOM   4995  O  O     . THR A 1  659  ? 99.419  164.614 119.392 1.00 23.12  ? 659  THR A O     1 
ATOM   4996  C  CB    . THR A 1  659  ? 98.978  164.092 116.190 1.00 13.78  ? 659  THR A CB    1 
ATOM   4997  O  OG1   . THR A 1  659  ? 99.457  163.943 114.852 1.00 24.26  ? 659  THR A OG1   1 
ATOM   4998  C  CG2   . THR A 1  659  ? 97.916  165.092 116.185 1.00 16.11  ? 659  THR A CG2   1 
ATOM   4999  N  N     . PRO A 1  660  ? 99.582  166.567 118.311 1.00 24.89  ? 660  PRO A N     1 
ATOM   5000  C  CA    . PRO A 1  660  ? 99.177  167.312 119.515 1.00 21.22  ? 660  PRO A CA    1 
ATOM   5001  C  C     . PRO A 1  660  ? 97.862  166.868 120.141 1.00 25.60  ? 660  PRO A C     1 
ATOM   5002  O  O     . PRO A 1  660  ? 97.768  166.845 121.371 1.00 29.29  ? 660  PRO A O     1 
ATOM   5003  C  CB    . PRO A 1  660  ? 99.092  168.752 119.004 1.00 21.18  ? 660  PRO A CB    1 
ATOM   5004  C  CG    . PRO A 1  660  ? 100.088 168.806 117.926 1.00 24.14  ? 660  PRO A CG    1 
ATOM   5005  C  CD    . PRO A 1  660  ? 100.105 167.467 117.269 1.00 24.30  ? 660  PRO A CD    1 
ATOM   5006  N  N     . GLU A 1  661  ? 96.841  166.528 119.353 1.00 22.35  ? 661  GLU A N     1 
ATOM   5007  C  CA    . GLU A 1  661  ? 95.604  166.037 119.950 1.00 18.91  ? 661  GLU A CA    1 
ATOM   5008  C  C     . GLU A 1  661  ? 95.744  164.595 120.426 1.00 21.03  ? 661  GLU A C     1 
ATOM   5009  O  O     . GLU A 1  661  ? 95.117  164.200 121.413 1.00 23.78  ? 661  GLU A O     1 
ATOM   5010  C  CB    . GLU A 1  661  ? 94.435  166.176 118.975 1.00 18.49  ? 661  GLU A CB    1 
ATOM   5011  C  CG    . GLU A 1  661  ? 94.722  165.850 117.525 1.00 27.01  ? 661  GLU A CG    1 
ATOM   5012  C  CD    . GLU A 1  661  ? 95.419  166.975 116.770 1.00 29.37  ? 661  GLU A CD    1 
ATOM   5013  O  OE1   . GLU A 1  661  ? 95.415  166.940 115.522 1.00 28.85  ? 661  GLU A OE1   1 
ATOM   5014  O  OE2   . GLU A 1  661  ? 95.983  167.880 117.416 1.00 28.85  ? 661  GLU A OE2   1 
ATOM   5015  N  N     . ALA A 1  662  ? 96.560  163.796 119.744 1.00 19.54  ? 662  ALA A N     1 
ATOM   5016  C  CA    . ALA A 1  662  ? 96.819  162.432 120.179 1.00 15.10  ? 662  ALA A CA    1 
ATOM   5017  C  C     . ALA A 1  662  ? 97.676  162.369 121.428 1.00 19.95  ? 662  ALA A C     1 
ATOM   5018  O  O     . ALA A 1  662  ? 97.672  161.347 122.114 1.00 25.62  ? 662  ALA A O     1 
ATOM   5019  C  CB    . ALA A 1  662  ? 97.493  161.644 119.063 1.00 11.99  ? 662  ALA A CB    1 
ATOM   5020  N  N     . HIS A 1  663  ? 98.430  163.425 121.719 1.00 17.67  ? 663  HIS A N     1 
ATOM   5021  C  CA    . HIS A 1  663  ? 99.167  163.506 122.973 1.00 15.43  ? 663  HIS A CA    1 
ATOM   5022  C  C     . HIS A 1  663  ? 98.230  163.674 124.164 1.00 23.00  ? 663  HIS A C     1 
ATOM   5023  O  O     . HIS A 1  663  ? 98.459  163.093 125.227 1.00 24.47  ? 663  HIS A O     1 
ATOM   5024  C  CB    . HIS A 1  663  ? 100.167 164.657 122.892 1.00 15.77  ? 663  HIS A CB    1 
ATOM   5025  C  CG    . HIS A 1  663  ? 100.893 164.917 124.169 1.00 25.29  ? 663  HIS A CG    1 
ATOM   5026  N  ND1   . HIS A 1  663  ? 101.900 164.102 124.634 1.00 24.84  ? 663  HIS A ND1   1 
ATOM   5027  C  CD2   . HIS A 1  663  ? 100.749 165.900 125.088 1.00 27.51  ? 663  HIS A CD2   1 
ATOM   5028  C  CE1   . HIS A 1  663  ? 102.345 164.569 125.785 1.00 21.53  ? 663  HIS A CE1   1 
ATOM   5029  N  NE2   . HIS A 1  663  ? 101.663 165.660 126.083 1.00 25.23  ? 663  HIS A NE2   1 
ATOM   5030  N  N     . GLN A 1  664  ? 97.169  164.466 124.005 1.00 26.90  ? 664  GLN A N     1 
ATOM   5031  C  CA    . GLN A 1  664  ? 96.207  164.667 125.082 1.00 19.27  ? 664  GLN A CA    1 
ATOM   5032  C  C     . GLN A 1  664  ? 95.403  163.409 125.372 1.00 19.95  ? 664  GLN A C     1 
ATOM   5033  O  O     . GLN A 1  664  ? 94.936  163.226 126.498 1.00 30.18  ? 664  GLN A O     1 
ATOM   5034  C  CB    . GLN A 1  664  ? 95.273  165.821 124.733 1.00 24.63  ? 664  GLN A CB    1 
ATOM   5035  C  CG    . GLN A 1  664  ? 95.495  167.088 125.536 1.00 27.71  ? 664  GLN A CG    1 
ATOM   5036  C  CD    . GLN A 1  664  ? 95.020  166.967 126.974 1.00 31.79  ? 664  GLN A CD    1 
ATOM   5037  O  OE1   . GLN A 1  664  ? 93.821  166.949 127.241 1.00 29.92  ? 664  GLN A OE1   1 
ATOM   5038  N  NE2   . GLN A 1  664  ? 95.961  166.883 127.907 1.00 29.73  ? 664  GLN A NE2   1 
ATOM   5039  N  N     . GLU A 1  665  ? 95.208  162.546 124.376 1.00 19.28  ? 665  GLU A N     1 
ATOM   5040  C  CA    . GLU A 1  665  ? 94.529  161.281 124.618 1.00 15.83  ? 665  GLU A CA    1 
ATOM   5041  C  C     . GLU A 1  665  ? 95.373  160.330 125.447 1.00 20.58  ? 665  GLU A C     1 
ATOM   5042  O  O     . GLU A 1  665  ? 94.828  159.552 126.230 1.00 29.82  ? 665  GLU A O     1 
ATOM   5043  C  CB    . GLU A 1  665  ? 94.147  160.629 123.300 1.00 19.49  ? 665  GLU A CB    1 
ATOM   5044  C  CG    . GLU A 1  665  ? 93.104  161.401 122.539 1.00 25.30  ? 665  GLU A CG    1 
ATOM   5045  C  CD    . GLU A 1  665  ? 92.705  160.730 121.251 1.00 31.90  ? 665  GLU A CD    1 
ATOM   5046  O  OE1   . GLU A 1  665  ? 93.333  159.716 120.883 1.00 29.55  ? 665  GLU A OE1   1 
ATOM   5047  O  OE2   . GLU A 1  665  ? 91.753  161.215 120.609 1.00 33.86  ? 665  GLU A OE2   1 
ATOM   5048  N  N     . VAL A 1  666  ? 96.691  160.347 125.275 1.00 18.30  ? 666  VAL A N     1 
ATOM   5049  C  CA    . VAL A 1  666  ? 97.542  159.509 126.107 1.00 17.94  ? 666  VAL A CA    1 
ATOM   5050  C  C     . VAL A 1  666  ? 97.517  159.995 127.547 1.00 14.72  ? 666  VAL A C     1 
ATOM   5051  O  O     . VAL A 1  666  ? 97.504  159.193 128.486 1.00 22.24  ? 666  VAL A O     1 
ATOM   5052  C  CB    . VAL A 1  666  ? 98.973  159.468 125.543 1.00 18.10  ? 666  VAL A CB    1 
ATOM   5053  C  CG1   . VAL A 1  666  ? 99.888  158.720 126.482 1.00 15.41  ? 666  VAL A CG1   1 
ATOM   5054  C  CG2   . VAL A 1  666  ? 98.978  158.811 124.191 1.00 15.36  ? 666  VAL A CG2   1 
ATOM   5055  N  N     . GLN A 1  667  ? 97.504  161.313 127.748 1.00 11.41  ? 667  GLN A N     1 
ATOM   5056  C  CA    . GLN A 1  667  ? 97.455  161.855 129.100 1.00 15.47  ? 667  GLN A CA    1 
ATOM   5057  C  C     . GLN A 1  667  ? 96.165  161.469 129.806 1.00 19.08  ? 667  GLN A C     1 
ATOM   5058  O  O     . GLN A 1  667  ? 96.177  161.146 130.996 1.00 23.25  ? 667  GLN A O     1 
ATOM   5059  C  CB    . GLN A 1  667  ? 97.621  163.369 129.062 1.00 16.43  ? 667  GLN A CB    1 
ATOM   5060  C  CG    . GLN A 1  667  ? 98.976  163.847 129.531 1.00 17.04  ? 667  GLN A CG    1 
ATOM   5061  C  CD    . GLN A 1  667  ? 100.115 163.071 128.911 1.00 25.90  ? 667  GLN A CD    1 
ATOM   5062  O  OE1   . GLN A 1  667  ? 100.811 162.318 129.588 1.00 26.83  ? 667  GLN A OE1   1 
ATOM   5063  N  NE2   . GLN A 1  667  ? 100.316 163.255 127.617 1.00 22.90  ? 667  GLN A NE2   1 
ATOM   5064  N  N     . GLU A 1  668  ? 95.044  161.485 129.087 1.00 19.39  ? 668  GLU A N     1 
ATOM   5065  C  CA    . GLU A 1  668  ? 93.777  161.069 129.675 1.00 19.05  ? 668  GLU A CA    1 
ATOM   5066  C  C     . GLU A 1  668  ? 93.799  159.601 130.083 1.00 19.86  ? 668  GLU A C     1 
ATOM   5067  O  O     . GLU A 1  668  ? 93.249  159.238 131.126 1.00 25.93  ? 668  GLU A O     1 
ATOM   5068  C  CB    . GLU A 1  668  ? 92.635  161.344 128.703 1.00 18.17  ? 668  GLU A CB    1 
ATOM   5069  C  CG    . GLU A 1  668  ? 92.389  162.815 128.461 1.00 20.19  ? 668  GLU A CG    1 
ATOM   5070  C  CD    . GLU A 1  668  ? 91.613  163.081 127.192 1.00 24.87  ? 668  GLU A CD    1 
ATOM   5071  O  OE1   . GLU A 1  668  ? 91.616  164.236 126.720 1.00 22.18  ? 668  GLU A OE1   1 
ATOM   5072  O  OE2   . GLU A 1  668  ? 91.010  162.130 126.654 1.00 30.03  ? 668  GLU A OE2   1 
ATOM   5073  N  N     . ILE A 1  669  ? 94.407  158.738 129.270 1.00 14.25  ? 669  ILE A N     1 
ATOM   5074  C  CA    . ILE A 1  669  ? 94.537  157.333 129.646 1.00 14.71  ? 669  ILE A CA    1 
ATOM   5075  C  C     . ILE A 1  669  ? 95.407  157.190 130.887 1.00 18.23  ? 669  ILE A C     1 
ATOM   5076  O  O     . ILE A 1  669  ? 95.147  156.346 131.749 1.00 16.60  ? 669  ILE A O     1 
ATOM   5077  C  CB    . ILE A 1  669  ? 95.095  156.510 128.471 1.00 15.45  ? 669  ILE A CB    1 
ATOM   5078  C  CG1   . ILE A 1  669  ? 94.070  156.398 127.351 1.00 16.65  ? 669  ILE A CG1   1 
ATOM   5079  C  CG2   . ILE A 1  669  ? 95.512  155.132 128.919 1.00 16.74  ? 669  ILE A CG2   1 
ATOM   5080  C  CD1   . ILE A 1  669  ? 94.602  155.706 126.139 1.00 20.90  ? 669  ILE A CD1   1 
ATOM   5081  N  N     . ILE A 1  670  ? 96.461  158.000 130.990 1.00 23.70  ? 670  ILE A N     1 
ATOM   5082  C  CA    . ILE A 1  670  ? 97.370  157.912 132.130 1.00 18.08  ? 670  ILE A CA    1 
ATOM   5083  C  C     . ILE A 1  670  ? 96.695  158.408 133.403 1.00 17.93  ? 670  ILE A C     1 
ATOM   5084  O  O     . ILE A 1  670  ? 96.872  157.828 134.478 1.00 21.83  ? 670  ILE A O     1 
ATOM   5085  C  CB    . ILE A 1  670  ? 98.674  158.673 131.831 1.00 14.89  ? 670  ILE A CB    1 
ATOM   5086  C  CG1   . ILE A 1  670  ? 99.569  157.837 130.923 1.00 14.57  ? 670  ILE A CG1   1 
ATOM   5087  C  CG2   . ILE A 1  670  ? 99.422  158.995 133.095 1.00 18.54  ? 670  ILE A CG2   1 
ATOM   5088  C  CD1   . ILE A 1  670  ? 100.811 158.543 130.486 1.00 22.55  ? 670  ILE A CD1   1 
ATOM   5089  N  N     . ASN A 1  671  ? 95.910  159.480 133.309 1.00 18.32  ? 671  ASN A N     1 
ATOM   5090  C  CA    . ASN A 1  671  ? 95.212  159.977 134.487 1.00 15.59  ? 671  ASN A CA    1 
ATOM   5091  C  C     . ASN A 1  671  ? 94.211  158.963 135.022 1.00 20.50  ? 671  ASN A C     1 
ATOM   5092  O  O     . ASN A 1  671  ? 94.019  158.868 136.235 1.00 24.98  ? 671  ASN A O     1 
ATOM   5093  C  CB    . ASN A 1  671  ? 94.510  161.292 134.172 1.00 17.78  ? 671  ASN A CB    1 
ATOM   5094  C  CG    . ASN A 1  671  ? 95.475  162.435 133.997 1.00 27.37  ? 671  ASN A CG    1 
ATOM   5095  O  OD1   . ASN A 1  671  ? 96.589  162.403 134.514 1.00 25.10  ? 671  ASN A OD1   1 
ATOM   5096  N  ND2   . ASN A 1  671  ? 95.044  163.469 133.290 1.00 23.56  ? 671  ASN A ND2   1 
ATOM   5097  N  N     . GLU A 1  672  ? 93.569  158.199 134.141 1.00 23.15  ? 672  GLU A N     1 
ATOM   5098  C  CA    . GLU A 1  672  ? 92.642  157.169 134.593 1.00 19.31  ? 672  GLU A CA    1 
ATOM   5099  C  C     . GLU A 1  672  ? 93.353  156.109 135.419 1.00 20.15  ? 672  GLU A C     1 
ATOM   5100  O  O     . GLU A 1  672  ? 92.785  155.580 136.378 1.00 26.65  ? 672  GLU A O     1 
ATOM   5101  C  CB    . GLU A 1  672  ? 91.945  156.531 133.398 1.00 17.32  ? 672  GLU A CB    1 
ATOM   5102  C  CG    . GLU A 1  672  ? 90.922  157.415 132.739 1.00 22.56  ? 672  GLU A CG    1 
ATOM   5103  C  CD    . GLU A 1  672  ? 90.404  156.822 131.452 1.00 30.93  ? 672  GLU A CD    1 
ATOM   5104  O  OE1   . GLU A 1  672  ? 90.936  155.777 131.025 1.00 30.93  ? 672  GLU A OE1   1 
ATOM   5105  O  OE2   . GLU A 1  672  ? 89.462  157.394 130.870 1.00 31.06  ? 672  GLU A OE2   1 
ATOM   5106  N  N     . LEU A 1  673  ? 94.584  155.764 135.047 1.00 20.85  ? 673  LEU A N     1 
ATOM   5107  C  CA    . LEU A 1  673  ? 95.360  154.818 135.842 1.00 21.99  ? 673  LEU A CA    1 
ATOM   5108  C  C     . LEU A 1  673  ? 95.711  155.391 137.209 1.00 20.33  ? 673  LEU A C     1 
ATOM   5109  O  O     . LEU A 1  673  ? 95.685  154.677 138.213 1.00 23.35  ? 673  LEU A O     1 
ATOM   5110  C  CB    . LEU A 1  673  ? 96.631  154.424 135.097 1.00 24.27  ? 673  LEU A CB    1 
ATOM   5111  C  CG    . LEU A 1  673  ? 96.494  153.839 133.697 1.00 21.85  ? 673  LEU A CG    1 
ATOM   5112  C  CD1   . LEU A 1  673  ? 97.765  153.125 133.334 1.00 19.73  ? 673  LEU A CD1   1 
ATOM   5113  C  CD2   . LEU A 1  673  ? 95.324  152.900 133.637 1.00 23.48  ? 673  LEU A CD2   1 
ATOM   5114  N  N     . LEU A 1  674  ? 96.077  156.667 137.262 1.00 19.69  ? 674  LEU A N     1 
ATOM   5115  C  CA    . LEU A 1  674  ? 96.437  157.285 138.529 1.00 22.15  ? 674  LEU A CA    1 
ATOM   5116  C  C     . LEU A 1  674  ? 95.211  157.614 139.367 1.00 26.79  ? 674  LEU A C     1 
ATOM   5117  O  O     . LEU A 1  674  ? 95.333  157.861 140.570 1.00 28.00  ? 674  LEU A O     1 
ATOM   5118  C  CB    . LEU A 1  674  ? 97.263  158.545 138.280 1.00 18.57  ? 674  LEU A CB    1 
ATOM   5119  C  CG    . LEU A 1  674  ? 98.635  158.313 137.663 1.00 20.06  ? 674  LEU A CG    1 
ATOM   5120  C  CD1   . LEU A 1  674  ? 99.307  159.631 137.423 1.00 20.34  ? 674  LEU A CD1   1 
ATOM   5121  C  CD2   . LEU A 1  674  ? 99.480  157.433 138.552 1.00 19.55  ? 674  LEU A CD2   1 
ATOM   5122  N  N     . LEU A 1  675  ? 94.036  157.664 138.743 1.00 29.73  ? 675  LEU A N     1 
ATOM   5123  C  CA    . LEU A 1  675  ? 92.798  157.817 139.493 1.00 24.08  ? 675  LEU A CA    1 
ATOM   5124  C  C     . LEU A 1  675  ? 92.379  156.499 140.132 1.00 28.75  ? 675  LEU A C     1 
ATOM   5125  O  O     . LEU A 1  675  ? 91.896  156.477 141.266 1.00 32.36  ? 675  LEU A O     1 
ATOM   5126  C  CB    . LEU A 1  675  ? 91.702  158.330 138.572 1.00 24.47  ? 675  LEU A CB    1 
ATOM   5127  C  CG    . LEU A 1  675  ? 90.922  159.529 139.079 1.00 28.71  ? 675  LEU A CG    1 
ATOM   5128  C  CD1   . LEU A 1  675  ? 91.880  160.675 139.311 1.00 29.80  ? 675  LEU A CD1   1 
ATOM   5129  C  CD2   . LEU A 1  675  ? 89.855  159.908 138.084 1.00 26.66  ? 675  LEU A CD2   1 
ATOM   5130  N  N     . GLU A 1  676  ? 92.533  155.395 139.404 1.00 29.07  ? 676  GLU A N     1 
ATOM   5131  C  CA    . GLU A 1  676  ? 92.226  154.087 139.959 1.00 26.73  ? 676  GLU A CA    1 
ATOM   5132  C  C     . GLU A 1  676  ? 93.266  153.665 140.984 1.00 29.39  ? 676  GLU A C     1 
ATOM   5133  O  O     . GLU A 1  676  ? 92.941  152.962 141.944 1.00 35.41  ? 676  GLU A O     1 
ATOM   5134  C  CB    . GLU A 1  676  ? 92.112  153.064 138.832 1.00 28.12  ? 676  GLU A CB    1 
ATOM   5135  C  CG    . GLU A 1  676  ? 92.392  151.635 139.228 1.00 32.49  ? 676  GLU A CG    1 
ATOM   5136  C  CD    . GLU A 1  676  ? 91.644  150.628 138.365 1.00 36.20  ? 676  GLU A CD    1 
ATOM   5137  O  OE1   . GLU A 1  676  ? 92.296  149.739 137.777 1.00 33.80  ? 676  GLU A OE1   1 
ATOM   5138  O  OE2   . GLU A 1  676  ? 90.402  150.724 138.276 1.00 34.86  ? 676  GLU A OE2   1 
ATOM   5139  N  N     . SER A 1  677  ? 94.516  154.086 140.801 1.00 30.58  ? 677  SER A N     1 
ATOM   5140  C  CA    . SER A 1  677  ? 95.548  153.829 141.799 1.00 29.09  ? 677  SER A CA    1 
ATOM   5141  C  C     . SER A 1  677  ? 95.266  154.563 143.099 1.00 31.90  ? 677  SER A C     1 
ATOM   5142  O  O     . SER A 1  677  ? 95.563  154.045 144.179 1.00 32.92  ? 677  SER A O     1 
ATOM   5143  C  CB    . SER A 1  677  ? 96.917  154.235 141.254 1.00 27.27  ? 677  SER A CB    1 
ATOM   5144  O  OG    . SER A 1  677  ? 97.913  154.172 142.254 1.00 28.31  ? 677  SER A OG    1 
ATOM   5145  N  N     . GLU A 1  678  ? 94.718  155.772 143.017 1.00 30.41  ? 678  GLU A N     1 
ATOM   5146  C  CA    . GLU A 1  678  ? 94.458  156.554 144.217 1.00 27.01  ? 678  GLU A CA    1 
ATOM   5147  C  C     . GLU A 1  678  ? 93.171  156.128 144.904 1.00 33.56  ? 678  GLU A C     1 
ATOM   5148  O  O     . GLU A 1  678  ? 92.913  156.539 146.039 1.00 38.75  ? 678  GLU A O     1 
ATOM   5149  C  CB    . GLU A 1  678  ? 94.421  158.038 143.870 1.00 31.49  ? 678  GLU A CB    1 
ATOM   5150  C  CG    . GLU A 1  678  ? 94.837  158.955 145.002 1.00 34.93  ? 678  GLU A CG    1 
ATOM   5151  C  CD    . GLU A 1  678  ? 96.344  159.003 145.229 1.00 39.76  ? 678  GLU A CD    1 
ATOM   5152  O  OE1   . GLU A 1  678  ? 96.811  159.971 145.863 1.00 38.04  ? 678  GLU A OE1   1 
ATOM   5153  O  OE2   . GLU A 1  678  ? 97.063  158.081 144.793 1.00 39.75  ? 678  GLU A OE2   1 
ATOM   5154  N  N     . GLU A 1  679  ? 92.337  155.335 144.231 1.00 33.81  ? 679  GLU A N     1 
ATOM   5155  C  CA    . GLU A 1  679  ? 91.186  154.749 144.905 1.00 30.43  ? 679  GLU A CA    1 
ATOM   5156  C  C     . GLU A 1  679  ? 91.610  153.609 145.818 1.00 31.71  ? 679  GLU A C     1 
ATOM   5157  O  O     . GLU A 1  679  ? 91.069  153.451 146.915 1.00 40.58  ? 679  GLU A O     1 
ATOM   5158  C  CB    . GLU A 1  679  ? 90.163  154.268 143.882 1.00 29.54  ? 679  GLU A CB    1 
ATOM   5159  C  CG    . GLU A 1  679  ? 89.343  155.380 143.263 1.00 35.93  ? 679  GLU A CG    1 
ATOM   5160  C  CD    . GLU A 1  679  ? 89.355  156.655 144.085 1.00 40.76  ? 679  GLU A CD    1 
ATOM   5161  O  OE1   . GLU A 1  679  ? 89.927  157.660 143.617 1.00 38.51  ? 679  GLU A OE1   1 
ATOM   5162  O  OE2   . GLU A 1  679  ? 88.769  156.667 145.186 1.00 39.00  ? 679  GLU A OE2   1 
ATOM   5163  N  N     . ILE A 1  680  ? 92.579  152.807 145.386 1.00 21.01  ? 680  ILE A N     1 
ATOM   5164  C  CA    . ILE A 1  680  ? 93.102  151.753 146.246 1.00 22.91  ? 680  ILE A CA    1 
ATOM   5165  C  C     . ILE A 1  680  ? 93.775  152.357 147.469 1.00 26.75  ? 680  ILE A C     1 
ATOM   5166  O  O     . ILE A 1  680  ? 93.710  151.799 148.567 1.00 31.84  ? 680  ILE A O     1 
ATOM   5167  C  CB    . ILE A 1  680  ? 94.057  150.846 145.451 1.00 26.26  ? 680  ILE A CB    1 
ATOM   5168  C  CG1   . ILE A 1  680  ? 93.326  150.248 144.256 1.00 27.97  ? 680  ILE A CG1   1 
ATOM   5169  C  CG2   . ILE A 1  680  ? 94.609  149.746 146.321 1.00 25.30  ? 680  ILE A CG2   1 
ATOM   5170  C  CD1   . ILE A 1  680  ? 94.229  149.584 143.265 1.00 26.03  ? 680  ILE A CD1   1 
ATOM   5171  N  N     . ASN A 1  681  ? 94.434  153.505 147.301 1.00 33.04  ? 681  ASN A N     1 
ATOM   5172  C  CA    . ASN A 1  681  ? 95.020  154.195 148.446 1.00 32.32  ? 681  ASN A CA    1 
ATOM   5173  C  C     . ASN A 1  681  ? 93.945  154.690 149.399 1.00 30.96  ? 681  ASN A C     1 
ATOM   5174  O  O     . ASN A 1  681  ? 94.098  154.603 150.619 1.00 31.53  ? 681  ASN A O     1 
ATOM   5175  C  CB    . ASN A 1  681  ? 95.881  155.367 147.980 1.00 27.69  ? 681  ASN A CB    1 
ATOM   5176  C  CG    . ASN A 1  681  ? 97.210  154.928 147.430 1.00 28.58  ? 681  ASN A CG    1 
ATOM   5177  O  OD1   . ASN A 1  681  ? 97.712  153.864 147.769 1.00 29.24  ? 681  ASN A OD1   1 
ATOM   5178  N  ND2   . ASN A 1  681  ? 97.796  155.756 146.586 1.00 30.22  ? 681  ASN A ND2   1 
ATOM   5179  N  N     . ASN A 1  682  ? 92.853  155.224 148.857 1.00 33.62  ? 682  ASN A N     1 
ATOM   5180  C  CA    . ASN A 1  682  ? 91.783  155.754 149.693 1.00 33.75  ? 682  ASN A CA    1 
ATOM   5181  C  C     . ASN A 1  682  ? 91.122  154.658 150.514 1.00 33.22  ? 682  ASN A C     1 
ATOM   5182  O  O     . ASN A 1  682  ? 90.773  154.880 151.676 1.00 33.25  ? 682  ASN A O     1 
ATOM   5183  C  CB    . ASN A 1  682  ? 90.753  156.463 148.821 1.00 31.89  ? 682  ASN A CB    1 
ATOM   5184  C  CG    . ASN A 1  682  ? 90.860  157.958 148.911 1.00 36.74  ? 682  ASN A CG    1 
ATOM   5185  O  OD1   . ASN A 1  682  ? 91.548  158.486 149.782 1.00 37.51  ? 682  ASN A OD1   1 
ATOM   5186  N  ND2   . ASN A 1  682  ? 90.199  158.655 148.001 1.00 37.47  ? 682  ASN A ND2   1 
ATOM   5187  N  N     . ARG A 1  683  ? 90.943  153.478 149.927 1.00 33.27  ? 683  ARG A N     1 
ATOM   5188  C  CA    . ARG A 1  683  ? 90.430  152.343 150.677 1.00 32.19  ? 683  ARG A CA    1 
ATOM   5189  C  C     . ARG A 1  683  ? 91.367  151.958 151.812 1.00 34.95  ? 683  ARG A C     1 
ATOM   5190  O  O     . ARG A 1  683  ? 90.906  151.613 152.904 1.00 37.11  ? 683  ARG A O     1 
ATOM   5191  C  CB    . ARG A 1  683  ? 90.226  151.158 149.741 1.00 28.55  ? 683  ARG A CB    1 
ATOM   5192  C  CG    . ARG A 1  683  ? 88.807  150.965 149.285 1.00 31.05  ? 683  ARG A CG    1 
ATOM   5193  C  CD    . ARG A 1  683  ? 88.775  150.268 147.944 1.00 31.22  ? 683  ARG A CD    1 
ATOM   5194  N  NE    . ARG A 1  683  ? 88.844  148.823 148.103 1.00 32.79  ? 683  ARG A NE    1 
ATOM   5195  C  CZ    . ARG A 1  683  ? 89.086  147.972 147.118 1.00 35.17  ? 683  ARG A CZ    1 
ATOM   5196  N  NH1   . ARG A 1  683  ? 89.264  148.386 145.874 1.00 35.91  ? 683  ARG A NH1   1 
ATOM   5197  N  NH2   . ARG A 1  683  ? 89.160  146.672 147.389 1.00 33.47  ? 683  ARG A NH2   1 
ATOM   5198  N  N     . LEU A 1  684  ? 92.677  152.003 151.574 1.00 31.01  ? 684  LEU A N     1 
ATOM   5199  C  CA    . LEU A 1  684  ? 93.640  151.689 152.621 1.00 29.44  ? 684  LEU A CA    1 
ATOM   5200  C  C     . LEU A 1  684  ? 93.552  152.679 153.777 1.00 31.20  ? 684  LEU A C     1 
ATOM   5201  O  O     . LEU A 1  684  ? 93.702  152.295 154.942 1.00 33.37  ? 684  LEU A O     1 
ATOM   5202  C  CB    . LEU A 1  684  ? 95.049  151.678 152.039 1.00 28.84  ? 684  LEU A CB    1 
ATOM   5203  C  CG    . LEU A 1  684  ? 96.188  151.262 152.962 1.00 30.78  ? 684  LEU A CG    1 
ATOM   5204  C  CD1   . LEU A 1  684  ? 96.348  149.758 152.952 1.00 30.11  ? 684  LEU A CD1   1 
ATOM   5205  C  CD2   . LEU A 1  684  ? 97.469  151.956 152.552 1.00 26.89  ? 684  LEU A CD2   1 
ATOM   5206  N  N     . LEU A 1  685  ? 93.327  153.958 153.477 1.00 27.65  ? 685  LEU A N     1 
ATOM   5207  C  CA    . LEU A 1  685  ? 93.242  154.960 154.534 1.00 30.23  ? 685  LEU A CA    1 
ATOM   5208  C  C     . LEU A 1  685  ? 92.038  154.720 155.432 1.00 32.90  ? 685  LEU A C     1 
ATOM   5209  O  O     . LEU A 1  685  ? 91.977  155.239 156.551 1.00 35.99  ? 685  LEU A O     1 
ATOM   5210  C  CB    . LEU A 1  685  ? 93.185  156.365 153.933 1.00 30.80  ? 685  LEU A CB    1 
ATOM   5211  C  CG    . LEU A 1  685  ? 94.502  157.120 153.749 1.00 32.79  ? 685  LEU A CG    1 
ATOM   5212  C  CD1   . LEU A 1  685  ? 95.530  156.270 153.037 1.00 32.59  ? 685  LEU A CD1   1 
ATOM   5213  C  CD2   . LEU A 1  685  ? 94.275  158.416 152.998 1.00 31.61  ? 685  LEU A CD2   1 
ATOM   5214  N  N     . HIS A 1  686  ? 91.058  153.961 154.951 1.00 33.03  ? 686  HIS A N     1 
ATOM   5215  C  CA    . HIS A 1  686  ? 89.871  153.618 155.721 1.00 31.92  ? 686  HIS A CA    1 
ATOM   5216  C  C     . HIS A 1  686  ? 89.894  152.186 156.236 1.00 34.15  ? 686  HIS A C     1 
ATOM   5217  O  O     . HIS A 1  686  ? 88.896  151.726 156.793 1.00 38.50  ? 686  HIS A O     1 
ATOM   5218  C  CB    . HIS A 1  686  ? 88.617  153.835 154.875 1.00 31.88  ? 686  HIS A CB    1 
ATOM   5219  C  CG    . HIS A 1  686  ? 88.388  155.263 154.496 1.00 34.43  ? 686  HIS A CG    1 
ATOM   5220  N  ND1   . HIS A 1  686  ? 87.630  155.630 153.405 1.00 35.27  ? 686  HIS A ND1   1 
ATOM   5221  C  CD2   . HIS A 1  686  ? 88.831  156.415 155.051 1.00 35.48  ? 686  HIS A CD2   1 
ATOM   5222  C  CE1   . HIS A 1  686  ? 87.609  156.947 153.310 1.00 36.25  ? 686  HIS A CE1   1 
ATOM   5223  N  NE2   . HIS A 1  686  ? 88.329  157.448 154.297 1.00 37.81  ? 686  HIS A NE2   1 
ATOM   5224  N  N     . GLY A 1  687  ? 90.995  151.468 156.050 1.00 34.71  ? 687  GLY A N     1 
ATOM   5225  C  CA    . GLY A 1  687  ? 91.061  150.079 156.476 1.00 34.44  ? 687  GLY A CA    1 
ATOM   5226  C  C     . GLY A 1  687  ? 90.072  149.170 155.779 1.00 36.32  ? 687  GLY A C     1 
ATOM   5227  O  O     . GLY A 1  687  ? 89.520  148.260 156.410 1.00 38.48  ? 687  GLY A O     1 
ATOM   5228  N  N     . ASP A 1  688  ? 89.841  149.385 154.487 1.00 35.85  ? 688  ASP A N     1 
ATOM   5229  C  CA    . ASP A 1  688  ? 88.882  148.592 153.731 1.00 36.33  ? 688  ASP A CA    1 
ATOM   5230  C  C     . ASP A 1  688  ? 89.540  147.511 152.888 1.00 35.50  ? 688  ASP A C     1 
ATOM   5231  O  O     . ASP A 1  688  ? 88.847  146.828 152.132 1.00 37.33  ? 688  ASP A O     1 
ATOM   5232  C  CB    . ASP A 1  688  ? 88.036  149.492 152.835 1.00 36.96  ? 688  ASP A CB    1 
ATOM   5233  C  CG    . ASP A 1  688  ? 87.409  150.628 153.590 1.00 38.77  ? 688  ASP A CG    1 
ATOM   5234  O  OD1   . ASP A 1  688  ? 87.309  150.529 154.828 1.00 36.75  ? 688  ASP A OD1   1 
ATOM   5235  O  OD2   . ASP A 1  688  ? 86.997  151.612 152.946 1.00 39.40  ? 688  ASP A OD2   1 
ATOM   5236  N  N     . ILE A 1  689  ? 90.849  147.341 152.995 1.00 35.22  ? 689  ILE A N     1 
ATOM   5237  C  CA    . ILE A 1  689  ? 91.571  146.333 152.232 1.00 37.76  ? 689  ILE A CA    1 
ATOM   5238  C  C     . ILE A 1  689  ? 91.543  145.047 153.041 1.00 40.10  ? 689  ILE A C     1 
ATOM   5239  O  O     . ILE A 1  689  ? 92.187  144.946 154.089 1.00 41.42  ? 689  ILE A O     1 
ATOM   5240  C  CB    . ILE A 1  689  ? 93.010  146.767 151.924 1.00 36.07  ? 689  ILE A CB    1 
ATOM   5241  C  CG1   . ILE A 1  689  ? 93.024  148.093 151.168 1.00 37.08  ? 689  ILE A CG1   1 
ATOM   5242  C  CG2   . ILE A 1  689  ? 93.718  145.696 151.112 1.00 35.45  ? 689  ILE A CG2   1 
ATOM   5243  C  CD1   . ILE A 1  689  ? 92.102  148.124 149.985 1.00 38.05  ? 689  ILE A CD1   1 
ATOM   5244  N  N     . MET A 1  690  ? 90.789  144.063 152.564 1.00 39.17  ? 690  MET A N     1 
ATOM   5245  C  CA    . MET A 1  690  ? 90.721  142.771 153.223 1.00 37.76  ? 690  MET A CA    1 
ATOM   5246  C  C     . MET A 1  690  ? 91.302  141.707 152.310 1.00 37.39  ? 690  MET A C     1 
ATOM   5247  O  O     . MET A 1  690  ? 90.696  141.380 151.280 1.00 35.93  ? 690  MET A O     1 
ATOM   5248  C  CB    . MET A 1  690  ? 89.284  142.431 153.603 1.00 39.51  ? 690  MET A CB    1 
ATOM   5249  C  CG    . MET A 1  690  ? 88.778  143.257 154.772 1.00 42.46  ? 690  MET A CG    1 
ATOM   5250  S  SD    . MET A 1  690  ? 89.925  143.219 156.168 1.00 56.06  ? 690  MET A SD    1 
ATOM   5251  C  CE    . MET A 1  690  ? 89.497  141.661 156.936 1.00 38.14  ? 690  MET A CE    1 
ATOM   5252  N  N     . PRO A 1  691  ? 92.463  141.157 152.639 1.00 35.27  ? 691  PRO A N     1 
ATOM   5253  C  CA    . PRO A 1  691  ? 93.098  140.182 151.765 1.00 37.51  ? 691  PRO A CA    1 
ATOM   5254  C  C     . PRO A 1  691  ? 92.356  138.860 151.776 1.00 39.20  ? 691  PRO A C     1 
ATOM   5255  O  O     . PRO A 1  691  ? 91.617  138.556 152.724 1.00 36.77  ? 691  PRO A O     1 
ATOM   5256  C  CB    . PRO A 1  691  ? 94.501  140.038 152.368 1.00 34.69  ? 691  PRO A CB    1 
ATOM   5257  C  CG    . PRO A 1  691  ? 94.323  140.368 153.794 1.00 33.49  ? 691  PRO A CG    1 
ATOM   5258  C  CD    . PRO A 1  691  ? 93.253  141.418 153.852 1.00 32.56  ? 691  PRO A CD    1 
ATOM   5259  N  N     . PRO A 1  692  ? 92.522  138.047 150.734 1.00 41.20  ? 692  PRO A N     1 
ATOM   5260  C  CA    . PRO A 1  692  ? 92.009  136.673 150.782 1.00 41.08  ? 692  PRO A CA    1 
ATOM   5261  C  C     . PRO A 1  692  ? 92.834  135.799 151.713 1.00 41.53  ? 692  PRO A C     1 
ATOM   5262  O  O     . PRO A 1  692  ? 93.805  136.265 152.314 1.00 38.71  ? 692  PRO A O     1 
ATOM   5263  C  CB    . PRO A 1  692  ? 92.121  136.209 149.326 1.00 40.31  ? 692  PRO A CB    1 
ATOM   5264  C  CG    . PRO A 1  692  ? 93.217  137.033 148.762 1.00 39.56  ? 692  PRO A CG    1 
ATOM   5265  C  CD    . PRO A 1  692  ? 93.115  138.367 149.427 1.00 38.55  ? 692  PRO A CD    1 
ATOM   5266  N  N     . ILE A 1  693  ? 92.464  134.527 151.833 1.00 46.29  ? 693  ILE A N     1 
ATOM   5267  C  CA    . ILE A 1  693  ? 93.142  133.609 152.747 1.00 45.46  ? 693  ILE A CA    1 
ATOM   5268  C  C     . ILE A 1  693  ? 94.483  133.242 152.120 1.00 47.28  ? 693  ILE A C     1 
ATOM   5269  O  O     . ILE A 1  693  ? 94.539  132.702 151.015 1.00 46.85  ? 693  ILE A O     1 
ATOM   5270  C  CB    . ILE A 1  693  ? 92.298  132.370 153.042 1.00 42.92  ? 693  ILE A CB    1 
ATOM   5271  C  CG1   . ILE A 1  693  ? 90.958  132.781 153.654 1.00 44.04  ? 693  ILE A CG1   1 
ATOM   5272  C  CG2   . ILE A 1  693  ? 93.042  131.456 153.994 1.00 42.28  ? 693  ILE A CG2   1 
ATOM   5273  C  CD1   . ILE A 1  693  ? 89.983  131.639 153.816 1.00 44.70  ? 693  ILE A CD1   1 
ATOM   5274  N  N     . GLY A 1  694  ? 95.572  133.547 152.822 1.00 41.71  ? 694  GLY A N     1 
ATOM   5275  C  CA    . GLY A 1  694  ? 96.893  133.224 152.323 1.00 39.24  ? 694  GLY A CA    1 
ATOM   5276  C  C     . GLY A 1  694  ? 97.729  134.447 152.014 1.00 39.41  ? 694  GLY A C     1 
ATOM   5277  O  O     . GLY A 1  694  ? 98.917  134.331 151.703 1.00 39.81  ? 694  GLY A O     1 
ATOM   5278  N  N     . LEU A 1  695  ? 97.116  135.624 152.080 1.00 40.26  ? 695  LEU A N     1 
ATOM   5279  C  CA    . LEU A 1  695  ? 97.787  136.872 151.750 1.00 39.61  ? 695  LEU A CA    1 
ATOM   5280  C  C     . LEU A 1  695  ? 97.681  137.865 152.898 1.00 39.08  ? 695  LEU A C     1 
ATOM   5281  O  O     . LEU A 1  695  ? 96.669  137.931 153.599 1.00 39.01  ? 695  LEU A O     1 
ATOM   5282  C  CB    . LEU A 1  695  ? 97.194  137.492 150.486 1.00 36.10  ? 695  LEU A CB    1 
ATOM   5283  C  CG    . LEU A 1  695  ? 97.462  136.742 149.185 1.00 37.30  ? 695  LEU A CG    1 
ATOM   5284  C  CD1   . LEU A 1  695  ? 96.757  137.437 148.050 1.00 39.06  ? 695  LEU A CD1   1 
ATOM   5285  C  CD2   . LEU A 1  695  ? 98.944  136.632 148.914 1.00 34.40  ? 695  LEU A CD2   1 
ATOM   5286  N  N     . THR A 1  696  ? 98.742  138.640 153.082 1.00 34.75  ? 696  THR A N     1 
ATOM   5287  C  CA    . THR A 1  696  ? 98.726  139.715 154.055 1.00 34.56  ? 696  THR A CA    1 
ATOM   5288  C  C     . THR A 1  696  ? 98.185  140.991 153.424 1.00 32.43  ? 696  THR A C     1 
ATOM   5289  O  O     . THR A 1  696  ? 97.965  141.074 152.217 1.00 32.23  ? 696  THR A O     1 
ATOM   5290  C  CB    . THR A 1  696  ? 100.122 139.947 154.620 1.00 34.59  ? 696  THR A CB    1 
ATOM   5291  O  OG1   . THR A 1  696  ? 100.129 141.155 155.383 1.00 37.28  ? 696  THR A OG1   1 
ATOM   5292  C  CG2   . THR A 1  696  ? 101.130 140.047 153.513 1.00 34.01  ? 696  THR A CG2   1 
ATOM   5293  N  N     . THR A 1  697  ? 97.956  141.998 154.263 1.00 30.98  ? 697  THR A N     1 
ATOM   5294  C  CA    . THR A 1  697  ? 97.442  143.261 153.750 1.00 32.66  ? 697  THR A CA    1 
ATOM   5295  C  C     . THR A 1  697  ? 98.486  143.982 152.907 1.00 32.38  ? 697  THR A C     1 
ATOM   5296  O  O     . THR A 1  697  ? 98.135  144.695 151.964 1.00 32.92  ? 697  THR A O     1 
ATOM   5297  C  CB    . THR A 1  697  ? 96.965  144.139 154.903 1.00 30.54  ? 697  THR A CB    1 
ATOM   5298  O  OG1   . THR A 1  697  ? 95.992  143.418 155.662 1.00 37.63  ? 697  THR A OG1   1 
ATOM   5299  C  CG2   . THR A 1  697  ? 96.316  145.403 154.384 1.00 29.47  ? 697  THR A CG2   1 
ATOM   5300  N  N     . HIS A 1  698  ? 99.767  143.815 153.227 1.00 34.11  ? 698  HIS A N     1 
ATOM   5301  C  CA    . HIS A 1  698  ? 100.805 144.409 152.395 1.00 33.50  ? 698  HIS A CA    1 
ATOM   5302  C  C     . HIS A 1  698  ? 100.860 143.750 151.024 1.00 35.22  ? 698  HIS A C     1 
ATOM   5303  O  O     . HIS A 1  698  ? 100.803 144.432 149.998 1.00 40.78  ? 698  HIS A O     1 
ATOM   5304  C  CB    . HIS A 1  698  ? 102.163 144.307 153.084 1.00 34.38  ? 698  HIS A CB    1 
ATOM   5305  C  CG    . HIS A 1  698  ? 103.299 144.773 152.230 1.00 36.19  ? 698  HIS A CG    1 
ATOM   5306  N  ND1   . HIS A 1  698  ? 103.670 146.096 152.143 1.00 37.39  ? 698  HIS A ND1   1 
ATOM   5307  C  CD2   . HIS A 1  698  ? 104.122 144.095 151.397 1.00 35.53  ? 698  HIS A CD2   1 
ATOM   5308  C  CE1   . HIS A 1  698  ? 104.686 146.210 151.309 1.00 37.14  ? 698  HIS A CE1   1 
ATOM   5309  N  NE2   . HIS A 1  698  ? 104.978 145.011 150.841 1.00 36.85  ? 698  HIS A NE2   1 
ATOM   5310  N  N     . ASP A 1  699  ? 100.955 142.422 150.982 1.00 34.13  ? 699  ASP A N     1 
ATOM   5311  C  CA    . ASP A 1  699  ? 101.072 141.735 149.701 1.00 34.08  ? 699  ASP A CA    1 
ATOM   5312  C  C     . ASP A 1  699  ? 99.791  141.782 148.883 1.00 33.96  ? 699  ASP A C     1 
ATOM   5313  O  O     . ASP A 1  699  ? 99.858  141.663 147.658 1.00 36.11  ? 699  ASP A O     1 
ATOM   5314  C  CB    . ASP A 1  699  ? 101.499 140.280 149.902 1.00 35.57  ? 699  ASP A CB    1 
ATOM   5315  C  CG    . ASP A 1  699  ? 102.869 140.161 150.537 1.00 41.08  ? 699  ASP A CG    1 
ATOM   5316  O  OD1   . ASP A 1  699  ? 103.348 141.160 151.108 1.00 41.53  ? 699  ASP A OD1   1 
ATOM   5317  O  OD2   . ASP A 1  699  ? 103.472 139.072 150.465 1.00 40.63  ? 699  ASP A OD2   1 
ATOM   5318  N  N     . PHE A 1  700  ? 98.634  141.936 149.518 1.00 29.13  ? 700  PHE A N     1 
ATOM   5319  C  CA    . PHE A 1  700  ? 97.412  142.125 148.749 1.00 28.53  ? 700  PHE A CA    1 
ATOM   5320  C  C     . PHE A 1  700  ? 97.316  143.534 148.187 1.00 26.47  ? 700  PHE A C     1 
ATOM   5321  O  O     . PHE A 1  700  ? 96.793  143.723 147.086 1.00 28.12  ? 700  PHE A O     1 
ATOM   5322  C  CB    . PHE A 1  700  ? 96.188  141.816 149.613 1.00 30.26  ? 700  PHE A CB    1 
ATOM   5323  C  CG    . PHE A 1  700  ? 94.891  141.883 148.870 1.00 27.98  ? 700  PHE A CG    1 
ATOM   5324  C  CD1   . PHE A 1  700  ? 94.673  141.084 147.770 1.00 28.33  ? 700  PHE A CD1   1 
ATOM   5325  C  CD2   . PHE A 1  700  ? 93.893  142.746 149.268 1.00 26.81  ? 700  PHE A CD2   1 
ATOM   5326  C  CE1   . PHE A 1  700  ? 93.488  141.147 147.083 1.00 28.67  ? 700  PHE A CE1   1 
ATOM   5327  C  CE2   . PHE A 1  700  ? 92.711  142.813 148.587 1.00 24.82  ? 700  PHE A CE2   1 
ATOM   5328  C  CZ    . PHE A 1  700  ? 92.506  142.013 147.494 1.00 26.14  ? 700  PHE A CZ    1 
ATOM   5329  N  N     . TYR A 1  701  ? 97.802  144.526 148.930 1.00 26.26  ? 701  TYR A N     1 
ATOM   5330  C  CA    . TYR A 1  701  ? 97.774  145.907 148.462 1.00 26.57  ? 701  TYR A CA    1 
ATOM   5331  C  C     . TYR A 1  701  ? 98.703  146.105 147.273 1.00 27.49  ? 701  TYR A C     1 
ATOM   5332  O  O     . TYR A 1  701  ? 98.350  146.790 146.310 1.00 27.02  ? 701  TYR A O     1 
ATOM   5333  C  CB    . TYR A 1  701  ? 98.153  146.832 149.613 1.00 23.43  ? 701  TYR A CB    1 
ATOM   5334  C  CG    . TYR A 1  701  ? 98.392  148.277 149.259 1.00 26.38  ? 701  TYR A CG    1 
ATOM   5335  C  CD1   . TYR A 1  701  ? 97.341  149.170 149.175 1.00 26.14  ? 701  TYR A CD1   1 
ATOM   5336  C  CD2   . TYR A 1  701  ? 99.670  148.755 149.046 1.00 24.75  ? 701  TYR A CD2   1 
ATOM   5337  C  CE1   . TYR A 1  701  ? 97.557  150.490 148.876 1.00 25.83  ? 701  TYR A CE1   1 
ATOM   5338  C  CE2   . TYR A 1  701  ? 99.891  150.065 148.745 1.00 24.29  ? 701  TYR A CE2   1 
ATOM   5339  C  CZ    . TYR A 1  701  ? 98.835  150.930 148.665 1.00 25.98  ? 701  TYR A CZ    1 
ATOM   5340  O  OH    . TYR A 1  701  ? 99.059  152.247 148.362 1.00 29.15  ? 701  TYR A OH    1 
ATOM   5341  N  N     . GLU A 1  702  ? 99.891  145.505 147.320 1.00 27.83  ? 702  GLU A N     1 
ATOM   5342  C  CA    . GLU A 1  702  ? 100.833 145.628 146.215 1.00 24.85  ? 702  GLU A CA    1 
ATOM   5343  C  C     . GLU A 1  702  ? 100.350 144.902 144.970 1.00 27.83  ? 702  GLU A C     1 
ATOM   5344  O  O     . GLU A 1  702  ? 100.639 145.338 143.853 1.00 33.55  ? 702  GLU A O     1 
ATOM   5345  C  CB    . GLU A 1  702  ? 102.205 145.112 146.639 1.00 24.72  ? 702  GLU A CB    1 
ATOM   5346  C  CG    . GLU A 1  702  ? 103.004 146.111 147.451 1.00 24.42  ? 702  GLU A CG    1 
ATOM   5347  C  CD    . GLU A 1  702  ? 103.538 147.244 146.603 1.00 30.17  ? 702  GLU A CD    1 
ATOM   5348  O  OE1   . GLU A 1  702  ? 103.887 146.991 145.435 1.00 34.16  ? 702  GLU A OE1   1 
ATOM   5349  O  OE2   . GLU A 1  702  ? 103.604 148.387 147.094 1.00 30.34  ? 702  GLU A OE2   1 
ATOM   5350  N  N     . LYS A 1  703  ? 99.635  143.790 145.133 1.00 29.67  ? 703  LYS A N     1 
ATOM   5351  C  CA    . LYS A 1  703  ? 99.036  143.126 143.983 1.00 26.91  ? 703  LYS A CA    1 
ATOM   5352  C  C     . LYS A 1  703  ? 97.912  143.962 143.384 1.00 25.00  ? 703  LYS A C     1 
ATOM   5353  O  O     . LYS A 1  703  ? 97.744  144.003 142.163 1.00 23.76  ? 703  LYS A O     1 
ATOM   5354  C  CB    . LYS A 1  703  ? 98.530  141.742 144.387 1.00 30.24  ? 703  LYS A CB    1 
ATOM   5355  C  CG    . LYS A 1  703  ? 97.801  141.013 143.278 1.00 33.07  ? 703  LYS A CG    1 
ATOM   5356  C  CD    . LYS A 1  703  ? 97.135  139.747 143.771 1.00 32.96  ? 703  LYS A CD    1 
ATOM   5357  C  CE    . LYS A 1  703  ? 98.152  138.658 144.044 1.00 31.08  ? 703  LYS A CE    1 
ATOM   5358  N  NZ    . LYS A 1  703  ? 97.566  137.552 144.844 1.00 28.21  ? 703  LYS A NZ    1 
ATOM   5359  N  N     . LEU A 1  704  ? 97.119  144.623 144.228 1.00 24.07  ? 704  LEU A N     1 
ATOM   5360  C  CA    . LEU A 1  704  ? 96.049  145.475 143.721 1.00 24.97  ? 704  LEU A CA    1 
ATOM   5361  C  C     . LEU A 1  704  ? 96.599  146.628 142.901 1.00 29.73  ? 704  LEU A C     1 
ATOM   5362  O  O     . LEU A 1  704  ? 96.052  146.962 141.845 1.00 31.61  ? 704  LEU A O     1 
ATOM   5363  C  CB    . LEU A 1  704  ? 95.216  146.028 144.870 1.00 24.73  ? 704  LEU A CB    1 
ATOM   5364  C  CG    . LEU A 1  704  ? 94.191  145.154 145.570 1.00 23.42  ? 704  LEU A CG    1 
ATOM   5365  C  CD1   . LEU A 1  704  ? 93.509  145.989 146.619 1.00 28.88  ? 704  LEU A CD1   1 
ATOM   5366  C  CD2   . LEU A 1  704  ? 93.184  144.633 144.576 1.00 26.84  ? 704  LEU A CD2   1 
ATOM   5367  N  N     . GLN A 1  705  ? 97.662  147.268 143.389 1.00 29.61  ? 705  GLN A N     1 
ATOM   5368  C  CA    . GLN A 1  705  ? 98.260  148.395 142.683 1.00 22.38  ? 705  GLN A CA    1 
ATOM   5369  C  C     . GLN A 1  705  ? 98.852  147.965 141.350 1.00 22.33  ? 705  GLN A C     1 
ATOM   5370  O  O     . GLN A 1  705  ? 98.686  148.657 140.343 1.00 24.44  ? 705  GLN A O     1 
ATOM   5371  C  CB    . GLN A 1  705  ? 99.340  149.038 143.547 1.00 19.10  ? 705  GLN A CB    1 
ATOM   5372  C  CG    . GLN A 1  705  ? 98.856  149.741 144.788 1.00 19.07  ? 705  GLN A CG    1 
ATOM   5373  C  CD    . GLN A 1  705  ? 98.108  151.007 144.487 1.00 22.47  ? 705  GLN A CD    1 
ATOM   5374  O  OE1   . GLN A 1  705  ? 98.155  151.516 143.376 1.00 27.12  ? 705  GLN A OE1   1 
ATOM   5375  N  NE2   . GLN A 1  705  ? 97.432  151.542 145.484 1.00 22.33  ? 705  GLN A NE2   1 
ATOM   5376  N  N     . LEU A 1  706  ? 99.535  146.820 141.321 1.00 21.77  ? 706  LEU A N     1 
ATOM   5377  C  CA    . LEU A 1  706  ? 100.210 146.386 140.103 1.00 20.12  ? 706  LEU A CA    1 
ATOM   5378  C  C     . LEU A 1  706  ? 99.232  146.217 138.950 1.00 24.46  ? 706  LEU A C     1 
ATOM   5379  O  O     . LEU A 1  706  ? 99.536  146.587 137.812 1.00 30.12  ? 706  LEU A O     1 
ATOM   5380  C  CB    . LEU A 1  706  ? 100.959 145.081 140.354 1.00 21.71  ? 706  LEU A CB    1 
ATOM   5381  C  CG    . LEU A 1  706  ? 102.431 145.209 140.733 1.00 24.82  ? 706  LEU A CG    1 
ATOM   5382  C  CD1   . LEU A 1  706  ? 102.974 143.879 141.207 1.00 23.70  ? 706  LEU A CD1   1 
ATOM   5383  C  CD2   . LEU A 1  706  ? 103.239 145.727 139.571 1.00 24.07  ? 706  LEU A CD2   1 
ATOM   5384  N  N     . ASN A 1  707  ? 98.060  145.645 139.214 1.00 27.47  ? 707  ASN A N     1 
ATOM   5385  C  CA    . ASN A 1  707  ? 97.071  145.482 138.159 1.00 25.43  ? 707  ASN A CA    1 
ATOM   5386  C  C     . ASN A 1  707  ? 96.361  146.785 137.829 1.00 26.60  ? 707  ASN A C     1 
ATOM   5387  O  O     . ASN A 1  707  ? 95.797  146.913 136.740 1.00 31.06  ? 707  ASN A O     1 
ATOM   5388  C  CB    . ASN A 1  707  ? 96.046  144.420 138.554 1.00 30.13  ? 707  ASN A CB    1 
ATOM   5389  C  CG    . ASN A 1  707  ? 96.689  143.147 139.063 1.00 34.69  ? 707  ASN A CG    1 
ATOM   5390  O  OD1   . ASN A 1  707  ? 96.416  142.706 140.176 1.00 39.54  ? 707  ASN A OD1   1 
ATOM   5391  N  ND2   . ASN A 1  707  ? 97.548  142.550 138.250 1.00 32.14  ? 707  ASN A ND2   1 
ATOM   5392  N  N     . ALA A 1  708  ? 96.362  147.752 138.742 1.00 20.00  ? 708  ALA A N     1 
ATOM   5393  C  CA    . ALA A 1  708  ? 95.689  149.016 138.481 1.00 19.71  ? 708  ALA A CA    1 
ATOM   5394  C  C     . ALA A 1  708  ? 96.528  149.974 137.655 1.00 24.00  ? 708  ALA A C     1 
ATOM   5395  O  O     . ALA A 1  708  ? 95.996  150.973 137.163 1.00 23.34  ? 708  ALA A O     1 
ATOM   5396  C  CB    . ALA A 1  708  ? 95.304  149.694 139.789 1.00 22.30  ? 708  ALA A CB    1 
ATOM   5397  N  N     . LEU A 1  709  ? 97.812  149.689 137.488 1.00 22.21  ? 709  LEU A N     1 
ATOM   5398  C  CA    . LEU A 1  709  ? 98.743  150.553 136.782 1.00 14.52  ? 709  LEU A CA    1 
ATOM   5399  C  C     . LEU A 1  709  ? 99.273  149.871 135.527 1.00 19.19  ? 709  LEU A C     1 
ATOM   5400  O  O     . LEU A 1  709  ? 100.441 150.003 135.170 1.00 24.88  ? 709  LEU A O     1 
ATOM   5401  C  CB    . LEU A 1  709  ? 99.886  150.962 137.702 1.00 16.22  ? 709  LEU A CB    1 
ATOM   5402  C  CG    . LEU A 1  709  ? 99.514  151.850 138.887 1.00 13.57  ? 709  LEU A CG    1 
ATOM   5403  C  CD1   . LEU A 1  709  ? 100.614 151.813 139.898 1.00 14.98  ? 709  LEU A CD1   1 
ATOM   5404  C  CD2   . LEU A 1  709  ? 99.233  153.271 138.456 1.00 10.50  ? 709  LEU A CD2   1 
ATOM   5405  N  N     . LYS A 1  710  ? 98.414  149.124 134.849 1.00 22.61  ? 710  LYS A N     1 
ATOM   5406  C  CA    . LYS A 1  710  ? 98.740  148.501 133.579 1.00 19.58  ? 710  LYS A CA    1 
ATOM   5407  C  C     . LYS A 1  710  ? 98.064  149.274 132.460 1.00 18.63  ? 710  LYS A C     1 
ATOM   5408  O  O     . LYS A 1  710  ? 96.913  149.696 132.594 1.00 23.15  ? 710  LYS A O     1 
ATOM   5409  C  CB    . LYS A 1  710  ? 98.300  147.041 133.550 1.00 19.12  ? 710  LYS A CB    1 
ATOM   5410  C  CG    . LYS A 1  710  ? 99.327  146.089 134.108 1.00 22.00  ? 710  LYS A CG    1 
ATOM   5411  C  CD    . LYS A 1  710  ? 98.780  144.678 134.200 1.00 21.95  ? 710  LYS A CD    1 
ATOM   5412  C  CE    . LYS A 1  710  ? 99.897  143.653 134.148 1.00 22.64  ? 710  LYS A CE    1 
ATOM   5413  N  NZ    . LYS A 1  710  ? 101.236 144.293 134.059 1.00 21.82  ? 710  LYS A NZ    1 
ATOM   5414  N  N     . PHE A 1  711  ? 98.791  149.471 131.373 1.00 16.74  ? 711  PHE A N     1 
ATOM   5415  C  CA    . PHE A 1  711  ? 98.254  150.189 130.232 1.00 14.58  ? 711  PHE A CA    1 
ATOM   5416  C  C     . PHE A 1  711  ? 97.119  149.388 129.609 1.00 17.52  ? 711  PHE A C     1 
ATOM   5417  O  O     . PHE A 1  711  ? 97.238  148.169 129.466 1.00 23.28  ? 711  PHE A O     1 
ATOM   5418  C  CB    . PHE A 1  711  ? 99.349  150.427 129.203 1.00 19.52  ? 711  PHE A CB    1 
ATOM   5419  C  CG    . PHE A 1  711  ? 100.148 151.668 129.434 1.00 17.00  ? 711  PHE A CG    1 
ATOM   5420  C  CD1   . PHE A 1  711  ? 99.534  152.852 129.775 1.00 19.18  ? 711  PHE A CD1   1 
ATOM   5421  C  CD2   . PHE A 1  711  ? 101.520 151.649 129.301 1.00 14.61  ? 711  PHE A CD2   1 
ATOM   5422  C  CE1   . PHE A 1  711  ? 100.278 153.989 129.982 1.00 17.81  ? 711  PHE A CE1   1 
ATOM   5423  C  CE2   . PHE A 1  711  ? 102.258 152.777 129.506 1.00 14.87  ? 711  PHE A CE2   1 
ATOM   5424  C  CZ    . PHE A 1  711  ? 101.640 153.948 129.849 1.00 18.03  ? 711  PHE A CZ    1 
ATOM   5425  N  N     . PRO A 1  712  ? 96.009  150.019 129.243 1.00 20.19  ? 712  PRO A N     1 
ATOM   5426  C  CA    . PRO A 1  712  ? 94.974  149.306 128.499 1.00 17.89  ? 712  PRO A CA    1 
ATOM   5427  C  C     . PRO A 1  712  ? 95.433  149.023 127.082 1.00 24.49  ? 712  PRO A C     1 
ATOM   5428  O  O     . PRO A 1  712  ? 96.439  149.550 126.609 1.00 31.13  ? 712  PRO A O     1 
ATOM   5429  C  CB    . PRO A 1  712  ? 93.793  150.275 128.518 1.00 21.79  ? 712  PRO A CB    1 
ATOM   5430  C  CG    . PRO A 1  712  ? 94.405  151.596 128.671 1.00 19.12  ? 712  PRO A CG    1 
ATOM   5431  C  CD    . PRO A 1  712  ? 95.621  151.411 129.518 1.00 23.29  ? 712  PRO A CD    1 
ATOM   5432  N  N     . ASP A 1  713  ? 94.682  148.162 126.399 1.00 31.86  ? 713  ASP A N     1 
ATOM   5433  C  CA    . ASP A 1  713  ? 95.008  147.853 125.014 1.00 29.21  ? 713  ASP A CA    1 
ATOM   5434  C  C     . ASP A 1  713  ? 94.724  149.019 124.079 1.00 29.35  ? 713  ASP A C     1 
ATOM   5435  O  O     . ASP A 1  713  ? 95.199  149.013 122.942 1.00 31.18  ? 713  ASP A O     1 
ATOM   5436  C  CB    . ASP A 1  713  ? 94.237  146.617 124.562 1.00 26.50  ? 713  ASP A CB    1 
ATOM   5437  C  CG    . ASP A 1  713  ? 94.797  145.341 125.152 1.00 36.40  ? 713  ASP A CG    1 
ATOM   5438  O  OD1   . ASP A 1  713  ? 94.880  144.328 124.428 1.00 39.26  ? 713  ASP A OD1   1 
ATOM   5439  O  OD2   . ASP A 1  713  ? 95.160  145.351 126.347 1.00 36.74  ? 713  ASP A OD2   1 
ATOM   5440  N  N     . ARG A 1  714  ? 93.967  150.017 124.528 1.00 24.19  ? 714  ARG A N     1 
ATOM   5441  C  CA    . ARG A 1  714  ? 93.609  151.152 123.691 1.00 22.34  ? 714  ARG A CA    1 
ATOM   5442  C  C     . ARG A 1  714  ? 94.654  152.251 123.697 1.00 24.23  ? 714  ARG A C     1 
ATOM   5443  O  O     . ARG A 1  714  ? 94.432  153.284 123.058 1.00 23.42  ? 714  ARG A O     1 
ATOM   5444  C  CB    . ARG A 1  714  ? 92.270  151.732 124.131 1.00 25.35  ? 714  ARG A CB    1 
ATOM   5445  C  CG    . ARG A 1  714  ? 92.132  151.852 125.619 1.00 26.80  ? 714  ARG A CG    1 
ATOM   5446  C  CD    . ARG A 1  714  ? 90.741  152.277 125.992 1.00 27.77  ? 714  ARG A CD    1 
ATOM   5447  N  NE    . ARG A 1  714  ? 90.594  153.723 125.941 1.00 26.99  ? 714  ARG A NE    1 
ATOM   5448  C  CZ    . ARG A 1  714  ? 90.508  154.497 127.013 1.00 27.64  ? 714  ARG A CZ    1 
ATOM   5449  N  NH1   . ARG A 1  714  ? 90.533  153.990 128.232 1.00 25.35  ? 714  ARG A NH1   1 
ATOM   5450  N  NH2   . ARG A 1  714  ? 90.387  155.811 126.856 1.00 27.35  ? 714  ARG A NH2   1 
ATOM   5451  N  N     . ILE A 1  715  ? 95.770  152.069 124.404 1.00 20.35  ? 715  ILE A N     1 
ATOM   5452  C  CA    . ILE A 1  715  ? 96.868  153.017 124.310 1.00 19.45  ? 715  ILE A CA    1 
ATOM   5453  C  C     . ILE A 1  715  ? 97.412  153.063 122.896 1.00 20.77  ? 715  ILE A C     1 
ATOM   5454  O  O     . ILE A 1  715  ? 98.064  154.039 122.514 1.00 24.01  ? 715  ILE A O     1 
ATOM   5455  C  CB    . ILE A 1  715  ? 97.974  152.670 125.328 1.00 21.04  ? 715  ILE A CB    1 
ATOM   5456  C  CG1   . ILE A 1  715  ? 98.994  153.801 125.426 1.00 19.93  ? 715  ILE A CG1   1 
ATOM   5457  C  CG2   . ILE A 1  715  ? 98.655  151.372 124.965 1.00 17.77  ? 715  ILE A CG2   1 
ATOM   5458  C  CD1   . ILE A 1  715  ? 98.447  155.059 126.024 1.00 17.30  ? 715  ILE A CD1   1 
ATOM   5459  N  N     . LEU A 1  716  ? 97.151  152.030 122.097 1.00 18.92  ? 716  LEU A N     1 
ATOM   5460  C  CA    . LEU A 1  716  ? 97.556  152.009 120.702 1.00 13.76  ? 716  LEU A CA    1 
ATOM   5461  C  C     . LEU A 1  716  ? 96.629  152.794 119.791 1.00 12.61  ? 716  LEU A C     1 
ATOM   5462  O  O     . LEU A 1  716  ? 96.975  153.002 118.630 1.00 20.90  ? 716  LEU A O     1 
ATOM   5463  C  CB    . LEU A 1  716  ? 97.651  150.571 120.204 1.00 12.11  ? 716  LEU A CB    1 
ATOM   5464  C  CG    . LEU A 1  716  ? 99.064  150.004 120.208 1.00 18.53  ? 716  LEU A CG    1 
ATOM   5465  C  CD1   . LEU A 1  716  ? 99.014  148.519 120.280 1.00 14.65  ? 716  LEU A CD1   1 
ATOM   5466  C  CD2   . LEU A 1  716  ? 99.798  150.431 118.971 1.00 18.78  ? 716  LEU A CD2   1 
ATOM   5467  N  N     . LYS A 1  717  ? 95.463  153.214 120.257 1.00 12.60  ? 717  LYS A N     1 
ATOM   5468  C  CA    . LYS A 1  717  ? 94.641  154.080 119.417 1.00 12.90  ? 717  LYS A CA    1 
ATOM   5469  C  C     . LYS A 1  717  ? 95.293  155.428 119.155 1.00 18.13  ? 717  LYS A C     1 
ATOM   5470  O  O     . LYS A 1  717  ? 95.344  155.839 117.985 1.00 22.87  ? 717  LYS A O     1 
ATOM   5471  C  CB    . LYS A 1  717  ? 93.247  154.257 120.021 1.00 15.80  ? 717  LYS A CB    1 
ATOM   5472  C  CG    . LYS A 1  717  ? 92.412  155.230 119.224 1.00 13.77  ? 717  LYS A CG    1 
ATOM   5473  C  CD    . LYS A 1  717  ? 91.113  155.552 119.894 1.00 18.00  ? 717  LYS A CD    1 
ATOM   5474  C  CE    . LYS A 1  717  ? 90.251  156.429 119.009 1.00 19.69  ? 717  LYS A CE    1 
ATOM   5475  N  NZ    . LYS A 1  717  ? 90.852  157.760 118.753 1.00 21.69  ? 717  LYS A NZ    1 
ATOM   5476  N  N     . PRO A 1  718  ? 95.785  156.171 120.152 1.00 19.84  ? 718  PRO A N     1 
ATOM   5477  C  CA    . PRO A 1  718  ? 96.467  157.428 119.825 1.00 17.00  ? 718  PRO A CA    1 
ATOM   5478  C  C     . PRO A 1  718  ? 97.780  157.236 119.088 1.00 15.79  ? 718  PRO A C     1 
ATOM   5479  O  O     . PRO A 1  718  ? 98.199  158.143 118.366 1.00 15.42  ? 718  PRO A O     1 
ATOM   5480  C  CB    . PRO A 1  718  ? 96.668  158.081 121.196 1.00 13.45  ? 718  PRO A CB    1 
ATOM   5481  C  CG    . PRO A 1  718  ? 96.647  156.982 122.130 1.00 16.53  ? 718  PRO A CG    1 
ATOM   5482  C  CD    . PRO A 1  718  ? 95.680  156.002 121.608 1.00 21.70  ? 718  PRO A CD    1 
ATOM   5483  N  N     . ILE A 1  719  ? 98.447  156.095 119.251 1.00 18.45  ? 719  ILE A N     1 
ATOM   5484  C  CA    . ILE A 1  719  ? 99.673  155.834 118.506 1.00 15.15  ? 719  ILE A CA    1 
ATOM   5485  C  C     . ILE A 1  719  ? 99.370  155.638 117.028 1.00 14.05  ? 719  ILE A C     1 
ATOM   5486  O  O     . ILE A 1  719  ? 100.031 156.214 116.160 1.00 14.56  ? 719  ILE A O     1 
ATOM   5487  C  CB    . ILE A 1  719  ? 100.407 154.615 119.088 1.00 11.51  ? 719  ILE A CB    1 
ATOM   5488  C  CG1   . ILE A 1  719  ? 101.038 154.959 120.433 1.00 13.00  ? 719  ILE A CG1   1 
ATOM   5489  C  CG2   . ILE A 1  719  ? 101.457 154.116 118.126 1.00 9.08   ? 719  ILE A CG2   1 
ATOM   5490  C  CD1   . ILE A 1  719  ? 101.683 153.786 121.107 1.00 15.53  ? 719  ILE A CD1   1 
ATOM   5491  N  N     . MET A 1  720  ? 98.366  154.825 116.718 1.00 14.18  ? 720  MET A N     1 
ATOM   5492  C  CA    . MET A 1  720  ? 98.069  154.494 115.335 1.00 10.16  ? 720  MET A CA    1 
ATOM   5493  C  C     . MET A 1  720  ? 97.339  155.606 114.612 1.00 11.22  ? 720  MET A C     1 
ATOM   5494  O  O     . MET A 1  720  ? 97.235  155.562 113.385 1.00 17.42  ? 720  MET A O     1 
ATOM   5495  C  CB    . MET A 1  720  ? 97.254  153.205 115.266 1.00 12.46  ? 720  MET A CB    1 
ATOM   5496  C  CG    . MET A 1  720  ? 97.997  151.993 115.786 1.00 11.56  ? 720  MET A CG    1 
ATOM   5497  S  SD    . MET A 1  720  ? 99.199  151.343 114.625 1.00 32.98  ? 720  MET A SD    1 
ATOM   5498  C  CE    . MET A 1  720  ? 98.251  151.358 113.115 1.00 13.89  ? 720  MET A CE    1 
ATOM   5499  N  N     . ASN A 1  721  ? 96.827  156.594 115.339 1.00 15.78  ? 721  ASN A N     1 
ATOM   5500  C  CA    . ASN A 1  721  ? 96.223  157.759 114.710 1.00 17.25  ? 721  ASN A CA    1 
ATOM   5501  C  C     . ASN A 1  721  ? 97.263  158.796 114.328 1.00 17.51  ? 721  ASN A C     1 
ATOM   5502  O  O     . ASN A 1  721  ? 96.953  159.730 113.584 1.00 21.68  ? 721  ASN A O     1 
ATOM   5503  C  CB    . ASN A 1  721  ? 95.197  158.393 115.645 1.00 17.44  ? 721  ASN A CB    1 
ATOM   5504  C  CG    . ASN A 1  721  ? 94.037  157.471 115.954 1.00 21.09  ? 721  ASN A CG    1 
ATOM   5505  O  OD1   . ASN A 1  721  ? 93.683  156.604 115.161 1.00 23.23  ? 721  ASN A OD1   1 
ATOM   5506  N  ND2   . ASN A 1  721  ? 93.436  157.660 117.111 1.00 20.45  ? 721  ASN A ND2   1 
ATOM   5507  N  N     . SER A 1  722  ? 98.490  158.651 114.822 1.00 12.52  ? 722  SER A N     1 
ATOM   5508  C  CA    . SER A 1  722  ? 99.548  159.611 114.555 1.00 10.28  ? 722  SER A CA    1 
ATOM   5509  C  C     . SER A 1  722  ? 100.459 159.187 113.416 1.00 14.49  ? 722  SER A C     1 
ATOM   5510  O  O     . SER A 1  722  ? 101.199 160.023 112.892 1.00 18.99  ? 722  SER A O     1 
ATOM   5511  C  CB    . SER A 1  722  ? 100.395 159.820 115.809 1.00 14.50  ? 722  SER A CB    1 
ATOM   5512  O  OG    . SER A 1  722  ? 99.647  160.410 116.843 1.00 20.25  ? 722  SER A OG    1 
ATOM   5513  N  N     . ILE A 1  723  ? 100.441 157.923 113.027 1.00 11.97  ? 723  ILE A N     1 
ATOM   5514  C  CA    . ILE A 1  723  ? 101.371 157.412 112.036 1.00 9.92   ? 723  ILE A CA    1 
ATOM   5515  C  C     . ILE A 1  723  ? 100.614 157.047 110.771 1.00 10.89  ? 723  ILE A C     1 
ATOM   5516  O  O     . ILE A 1  723  ? 99.399  156.841 110.781 1.00 18.10  ? 723  ILE A O     1 
ATOM   5517  C  CB    . ILE A 1  723  ? 102.157 156.197 112.559 1.00 8.01   ? 723  ILE A CB    1 
ATOM   5518  C  CG1   . ILE A 1  723  ? 101.306 154.946 112.481 1.00 6.64   ? 723  ILE A CG1   1 
ATOM   5519  C  CG2   . ILE A 1  723  ? 102.606 156.420 113.972 1.00 6.46   ? 723  ILE A CG2   1 
ATOM   5520  C  CD1   . ILE A 1  723  ? 102.009 153.760 112.953 1.00 7.21   ? 723  ILE A CD1   1 
ATOM   5521  N  N     . ASN A 1  724  ? 101.351 156.984 109.670 1.00 11.59  ? 724  ASN A N     1 
ATOM   5522  C  CA    . ASN A 1  724  ? 100.852 156.435 108.425 1.00 5.83   ? 724  ASN A CA    1 
ATOM   5523  C  C     . ASN A 1  724  ? 101.503 155.079 108.223 1.00 8.75   ? 724  ASN A C     1 
ATOM   5524  O  O     . ASN A 1  724  ? 102.710 155.022 107.959 1.00 15.31  ? 724  ASN A O     1 
ATOM   5525  C  CB    . ASN A 1  724  ? 101.180 157.368 107.265 1.00 6.63   ? 724  ASN A CB    1 
ATOM   5526  C  CG    . ASN A 1  724  ? 100.503 156.972 105.985 1.00 10.14  ? 724  ASN A CG    1 
ATOM   5527  O  OD1   . ASN A 1  724  ? 99.799  155.974 105.923 1.00 18.30  ? 724  ASN A OD1   1 
ATOM   5528  N  ND2   . ASN A 1  724  ? 100.687 157.769 104.959 1.00 18.80  ? 724  ASN A ND2   1 
ATOM   5529  N  N     . PRO A 1  725  ? 100.773 153.971 108.349 1.00 11.13  ? 725  PRO A N     1 
ATOM   5530  C  CA    . PRO A 1  725  ? 101.413 152.654 108.234 1.00 10.33  ? 725  PRO A CA    1 
ATOM   5531  C  C     . PRO A 1  725  ? 102.039 152.390 106.884 1.00 12.21  ? 725  PRO A C     1 
ATOM   5532  O  O     . PRO A 1  725  ? 102.858 151.476 106.770 1.00 15.26  ? 725  PRO A O     1 
ATOM   5533  C  CB    . PRO A 1  725  ? 100.260 151.686 108.520 1.00 2.95   ? 725  PRO A CB    1 
ATOM   5534  C  CG    . PRO A 1  725  ? 99.320  152.466 109.314 1.00 7.88   ? 725  PRO A CG    1 
ATOM   5535  C  CD    . PRO A 1  725  ? 99.376  153.851 108.778 1.00 10.16  ? 725  PRO A CD    1 
ATOM   5536  N  N     . GLU A 1  726  ? 101.675 153.150 105.858 1.00 12.55  ? 726  GLU A N     1 
ATOM   5537  C  CA    . GLU A 1  726  ? 102.259 152.986 104.539 1.00 8.13   ? 726  GLU A CA    1 
ATOM   5538  C  C     . GLU A 1  726  ? 103.663 153.561 104.422 1.00 9.90   ? 726  GLU A C     1 
ATOM   5539  O  O     . GLU A 1  726  ? 104.464 153.032 103.650 1.00 14.35  ? 726  GLU A O     1 
ATOM   5540  C  CB    . GLU A 1  726  ? 101.358 153.634 103.495 1.00 9.42   ? 726  GLU A CB    1 
ATOM   5541  C  CG    . GLU A 1  726  ? 101.277 152.860 102.207 1.00 19.76  ? 726  GLU A CG    1 
ATOM   5542  C  CD    . GLU A 1  726  ? 100.162 153.332 101.309 1.00 29.18  ? 726  GLU A CD    1 
ATOM   5543  O  OE1   . GLU A 1  726  ? 99.741  154.498 101.443 1.00 31.68  ? 726  GLU A OE1   1 
ATOM   5544  O  OE2   . GLU A 1  726  ? 99.693  152.529 100.475 1.00 26.40  ? 726  GLU A OE2   1 
ATOM   5545  N  N     . THR A 1  727  ? 103.986 154.617 105.162 1.00 11.02  ? 727  THR A N     1 
ATOM   5546  C  CA    . THR A 1  727  ? 105.278 155.276 105.034 1.00 2.38   ? 727  THR A CA    1 
ATOM   5547  C  C     . THR A 1  727  ? 106.106 155.300 106.306 1.00 2.28   ? 727  THR A C     1 
ATOM   5548  O  O     . THR A 1  727  ? 107.269 155.699 106.241 1.00 10.87  ? 727  THR A O     1 
ATOM   5549  C  CB    . THR A 1  727  ? 105.105 156.720 104.544 1.00 6.42   ? 727  THR A CB    1 
ATOM   5550  O  OG1   . THR A 1  727  ? 104.330 157.465 105.485 1.00 13.92  ? 727  THR A OG1   1 
ATOM   5551  C  CG2   . THR A 1  727  ? 104.411 156.754 103.208 1.00 7.41   ? 727  THR A CG2   1 
ATOM   5552  N  N     . ASN A 1  728  ? 105.570 154.886 107.445 1.00 4.52   ? 728  ASN A N     1 
ATOM   5553  C  CA    . ASN A 1  728  ? 106.304 154.966 108.700 1.00 1.59   ? 728  ASN A CA    1 
ATOM   5554  C  C     . ASN A 1  728  ? 107.308 153.825 108.792 1.00 5.59   ? 728  ASN A C     1 
ATOM   5555  O  O     . ASN A 1  728  ? 106.926 152.653 108.816 1.00 14.24  ? 728  ASN A O     1 
ATOM   5556  C  CB    . ASN A 1  728  ? 105.323 154.928 109.867 1.00 2.27   ? 728  ASN A CB    1 
ATOM   5557  C  CG    . ASN A 1  728  ? 105.880 155.533 111.122 1.00 3.68   ? 728  ASN A CG    1 
ATOM   5558  O  OD1   . ASN A 1  728  ? 105.521 156.634 111.502 1.00 8.55   ? 728  ASN A OD1   1 
ATOM   5559  N  ND2   . ASN A 1  728  ? 106.736 154.802 111.792 1.00 5.42   ? 728  ASN A ND2   1 
ATOM   5560  N  N     . GLY A 1  729  ? 108.594 154.165 108.841 1.00 2.13   ? 729  GLY A N     1 
ATOM   5561  C  CA    . GLY A 1  729  ? 109.623 153.148 108.885 1.00 14.54  ? 729  GLY A CA    1 
ATOM   5562  C  C     . GLY A 1  729  ? 109.760 152.448 110.215 1.00 0.59   ? 729  GLY A C     1 
ATOM   5563  O  O     . GLY A 1  729  ? 110.051 151.253 110.251 1.00 8.67   ? 729  GLY A O     1 
ATOM   5564  N  N     . LEU A 1  730  ? 109.585 153.170 111.321 1.00 1.08   ? 730  LEU A N     1 
ATOM   5565  C  CA    . LEU A 1  730  ? 109.608 152.527 112.629 1.00 8.71   ? 730  LEU A CA    1 
ATOM   5566  C  C     . LEU A 1  730  ? 108.458 151.543 112.779 1.00 4.60   ? 730  LEU A C     1 
ATOM   5567  O  O     . LEU A 1  730  ? 108.626 150.470 113.360 1.00 3.81   ? 730  LEU A O     1 
ATOM   5568  C  CB    . LEU A 1  730  ? 109.561 153.575 113.734 1.00 2.65   ? 730  LEU A CB    1 
ATOM   5569  C  CG    . LEU A 1  730  ? 109.469 153.039 115.167 1.00 3.66   ? 730  LEU A CG    1 
ATOM   5570  C  CD1   . LEU A 1  730  ? 110.752 152.363 115.572 1.00 3.14   ? 730  LEU A CD1   1 
ATOM   5571  C  CD2   . LEU A 1  730  ? 109.107 154.134 116.144 1.00 6.01   ? 730  LEU A CD2   1 
ATOM   5572  N  N     . PHE A 1  731  ? 107.284 151.892 112.263 1.00 4.63   ? 731  PHE A N     1 
ATOM   5573  C  CA    . PHE A 1  731  ? 106.145 150.989 112.336 1.00 5.00   ? 731  PHE A CA    1 
ATOM   5574  C  C     . PHE A 1  731  ? 106.342 149.760 111.459 1.00 2.63   ? 731  PHE A C     1 
ATOM   5575  O  O     . PHE A 1  731  ? 105.986 148.649 111.857 1.00 4.35   ? 731  PHE A O     1 
ATOM   5576  C  CB    . PHE A 1  731  ? 104.869 151.728 111.946 1.00 15.44  ? 731  PHE A CB    1 
ATOM   5577  C  CG    . PHE A 1  731  ? 103.652 150.860 111.946 1.00 1.09   ? 731  PHE A CG    1 
ATOM   5578  C  CD1   . PHE A 1  731  ? 103.090 150.443 113.134 1.00 1.70   ? 731  PHE A CD1   1 
ATOM   5579  C  CD2   . PHE A 1  731  ? 103.084 150.442 110.764 1.00 0.46   ? 731  PHE A CD2   1 
ATOM   5580  C  CE1   . PHE A 1  731  ? 101.996 149.642 113.139 1.00 12.30  ? 731  PHE A CE1   1 
ATOM   5581  C  CE2   . PHE A 1  731  ? 101.992 149.637 110.774 1.00 4.80   ? 731  PHE A CE2   1 
ATOM   5582  C  CZ    . PHE A 1  731  ? 101.446 149.236 111.963 1.00 0.65   ? 731  PHE A CZ    1 
ATOM   5583  N  N     . GLN A 1  732  ? 106.907 149.934 110.265 1.00 6.14   ? 732  GLN A N     1 
ATOM   5584  C  CA    . GLN A 1  732  ? 107.065 148.818 109.339 1.00 2.73   ? 732  GLN A CA    1 
ATOM   5585  C  C     . GLN A 1  732  ? 108.112 147.812 109.800 1.00 9.12   ? 732  GLN A C     1 
ATOM   5586  O  O     . GLN A 1  732  ? 107.945 146.618 109.566 1.00 2.11   ? 732  GLN A O     1 
ATOM   5587  C  CB    . GLN A 1  732  ? 107.389 149.343 107.946 1.00 8.07   ? 732  GLN A CB    1 
ATOM   5588  C  CG    . GLN A 1  732  ? 106.163 149.729 107.169 1.00 9.71   ? 732  GLN A CG    1 
ATOM   5589  C  CD    . GLN A 1  732  ? 106.463 150.512 105.920 1.00 4.50   ? 732  GLN A CD    1 
ATOM   5590  O  OE1   . GLN A 1  732  ? 107.572 150.968 105.710 1.00 6.86   ? 732  GLN A OE1   1 
ATOM   5591  N  NE2   . GLN A 1  732  ? 105.469 150.663 105.074 1.00 4.73   ? 732  GLN A NE2   1 
ATOM   5592  N  N     . MET A 1  733  ? 109.188 148.249 110.450 1.00 0.64   ? 733  MET A N     1 
ATOM   5593  C  CA    . MET A 1  733  ? 110.123 147.287 111.024 1.00 2.36   ? 733  MET A CA    1 
ATOM   5594  C  C     . MET A 1  733  ? 109.466 146.443 112.102 1.00 9.22   ? 733  MET A C     1 
ATOM   5595  O  O     . MET A 1  733  ? 109.709 145.239 112.185 1.00 2.07   ? 733  MET A O     1 
ATOM   5596  C  CB    . MET A 1  733  ? 111.358 147.989 111.584 1.00 10.81  ? 733  MET A CB    1 
ATOM   5597  C  CG    . MET A 1  733  ? 112.135 148.818 110.596 1.00 12.61  ? 733  MET A CG    1 
ATOM   5598  S  SD    . MET A 1  733  ? 113.698 149.393 111.247 1.00 12.61  ? 733  MET A SD    1 
ATOM   5599  C  CE    . MET A 1  733  ? 113.188 150.904 112.035 1.00 5.98   ? 733  MET A CE    1 
ATOM   5600  N  N     . VAL A 1  734  ? 108.648 147.055 112.948 1.00 2.06   ? 734  VAL A N     1 
ATOM   5601  C  CA    . VAL A 1  734  ? 107.975 146.315 114.006 1.00 5.59   ? 734  VAL A CA    1 
ATOM   5602  C  C     . VAL A 1  734  ? 106.886 145.417 113.434 1.00 3.56   ? 734  VAL A C     1 
ATOM   5603  O  O     . VAL A 1  734  ? 106.779 144.242 113.794 1.00 6.53   ? 734  VAL A O     1 
ATOM   5604  C  CB    . VAL A 1  734  ? 107.414 147.289 115.057 1.00 2.16   ? 734  VAL A CB    1 
ATOM   5605  C  CG1   . VAL A 1  734  ? 106.603 146.553 116.091 1.00 2.84   ? 734  VAL A CG1   1 
ATOM   5606  C  CG2   . VAL A 1  734  ? 108.535 148.058 115.716 1.00 3.22   ? 734  VAL A CG2   1 
ATOM   5607  N  N     . ALA A 1  735  ? 106.076 145.947 112.518 1.00 3.12   ? 735  ALA A N     1 
ATOM   5608  C  CA    . ALA A 1  735  ? 104.890 145.235 112.067 1.00 14.48  ? 735  ALA A CA    1 
ATOM   5609  C  C     . ALA A 1  735  ? 105.224 144.038 111.191 1.00 3.30   ? 735  ALA A C     1 
ATOM   5610  O  O     . ALA A 1  735  ? 104.436 143.096 111.126 1.00 10.73  ? 735  ALA A O     1 
ATOM   5611  C  CB    . ALA A 1  735  ? 103.962 146.186 111.328 1.00 7.06   ? 735  ALA A CB    1 
ATOM   5612  N  N     . THR A 1  736  ? 106.352 144.053 110.493 1.00 0.59   ? 736  THR A N     1 
ATOM   5613  C  CA    . THR A 1  736  ? 106.736 142.923 109.660 1.00 2.41   ? 736  THR A CA    1 
ATOM   5614  C  C     . THR A 1  736  ? 107.588 141.902 110.394 1.00 1.25   ? 736  THR A C     1 
ATOM   5615  O  O     . THR A 1  736  ? 107.890 140.855 109.829 1.00 2.40   ? 736  THR A O     1 
ATOM   5616  C  CB    . THR A 1  736  ? 107.489 143.401 108.413 1.00 0.14   ? 736  THR A CB    1 
ATOM   5617  O  OG1   . THR A 1  736  ? 108.740 143.970 108.795 1.00 7.63   ? 736  THR A OG1   1 
ATOM   5618  C  CG2   . THR A 1  736  ? 106.691 144.428 107.670 1.00 1.83   ? 736  THR A CG2   1 
ATOM   5619  N  N     . GLY A 1  737  ? 107.972 142.165 111.633 1.00 14.69  ? 737  GLY A N     1 
ATOM   5620  C  CA    . GLY A 1  737  ? 108.854 141.273 112.341 1.00 10.47  ? 737  GLY A CA    1 
ATOM   5621  C  C     . GLY A 1  737  ? 110.319 141.456 112.043 1.00 5.42   ? 737  GLY A C     1 
ATOM   5622  O  O     . GLY A 1  737  ? 111.110 140.560 112.340 1.00 9.00   ? 737  GLY A O     1 
ATOM   5623  N  N     . ALA A 1  738  ? 110.706 142.575 111.437 1.00 5.61   ? 738  ALA A N     1 
ATOM   5624  C  CA    . ALA A 1  738  ? 112.110 142.794 111.130 1.00 15.88  ? 738  ALA A CA    1 
ATOM   5625  C  C     . ALA A 1  738  ? 112.899 143.148 112.381 1.00 2.47   ? 738  ALA A C     1 
ATOM   5626  O  O     . ALA A 1  738  ? 114.011 142.651 112.576 1.00 7.25   ? 738  ALA A O     1 
ATOM   5627  C  CB    . ALA A 1  738  ? 112.253 143.875 110.069 1.00 11.33  ? 738  ALA A CB    1 
ATOM   5628  N  N     . LYS A 1  739  ? 112.335 143.986 113.248 1.00 2.19   ? 739  LYS A N     1 
ATOM   5629  C  CA    . LYS A 1  739  ? 113.013 144.424 114.458 1.00 3.79   ? 739  LYS A CA    1 
ATOM   5630  C  C     . LYS A 1  739  ? 112.021 145.147 115.346 1.00 7.33   ? 739  LYS A C     1 
ATOM   5631  O  O     . LYS A 1  739  ? 111.228 145.942 114.856 1.00 16.56  ? 739  LYS A O     1 
ATOM   5632  C  CB    . LYS A 1  739  ? 114.192 145.348 114.124 1.00 15.88  ? 739  LYS A CB    1 
ATOM   5633  C  CG    . LYS A 1  739  ? 115.060 145.705 115.304 1.00 5.86   ? 739  LYS A CG    1 
ATOM   5634  C  CD    . LYS A 1  739  ? 115.747 144.494 115.873 1.00 6.44   ? 739  LYS A CD    1 
ATOM   5635  C  CE    . LYS A 1  739  ? 116.851 144.010 115.000 1.00 5.76   ? 739  LYS A CE    1 
ATOM   5636  N  NZ    . LYS A 1  739  ? 117.531 142.873 115.643 1.00 14.05  ? 739  LYS A NZ    1 
ATOM   5637  N  N     . GLY A 1  740  ? 112.071 144.874 116.644 1.00 5.30   ? 740  GLY A N     1 
ATOM   5638  C  CA    . GLY A 1  740  ? 111.273 145.600 117.614 1.00 6.80   ? 740  GLY A CA    1 
ATOM   5639  C  C     . GLY A 1  740  ? 109.966 144.907 117.939 1.00 8.11   ? 740  GLY A C     1 
ATOM   5640  O  O     . GLY A 1  740  ? 109.565 143.917 117.324 1.00 14.93  ? 740  GLY A O     1 
ATOM   5641  N  N     . SER A 1  741  ? 109.287 145.467 118.935 1.00 6.58   ? 741  SER A N     1 
ATOM   5642  C  CA    . SER A 1  741  ? 108.023 144.935 119.420 1.00 0.90   ? 741  SER A CA    1 
ATOM   5643  C  C     . SER A 1  741  ? 107.094 146.095 119.725 1.00 0.64   ? 741  SER A C     1 
ATOM   5644  O  O     . SER A 1  741  ? 107.491 147.257 119.688 1.00 6.14   ? 741  SER A O     1 
ATOM   5645  C  CB    . SER A 1  741  ? 108.220 144.058 120.653 1.00 8.31   ? 741  SER A CB    1 
ATOM   5646  O  OG    . SER A 1  741  ? 108.793 144.784 121.719 1.00 10.11  ? 741  SER A OG    1 
ATOM   5647  N  N     . ASN A 1  742  ? 105.836 145.767 119.999 1.00 9.10   ? 742  ASN A N     1 
ATOM   5648  C  CA    . ASN A 1  742  ? 104.872 146.797 120.374 1.00 7.00   ? 742  ASN A CA    1 
ATOM   5649  C  C     . ASN A 1  742  ? 105.203 147.488 121.688 1.00 6.97   ? 742  ASN A C     1 
ATOM   5650  O  O     . ASN A 1  742  ? 105.059 148.719 121.751 1.00 11.91  ? 742  ASN A O     1 
ATOM   5651  C  CB    . ASN A 1  742  ? 103.461 146.205 120.424 1.00 10.74  ? 742  ASN A CB    1 
ATOM   5652  C  CG    . ASN A 1  742  ? 102.784 146.234 119.097 1.00 13.12  ? 742  ASN A CG    1 
ATOM   5653  O  OD1   . ASN A 1  742  ? 102.919 147.191 118.345 1.00 11.45  ? 742  ASN A OD1   1 
ATOM   5654  N  ND2   . ASN A 1  742  ? 102.046 145.185 118.791 1.00 15.75  ? 742  ASN A ND2   1 
ATOM   5655  N  N     . PRO A 1  743  ? 105.595 146.795 122.762 1.00 9.59   ? 743  PRO A N     1 
ATOM   5656  C  CA    . PRO A 1  743  ? 106.053 147.520 123.954 1.00 4.12   ? 743  PRO A CA    1 
ATOM   5657  C  C     . PRO A 1  743  ? 107.234 148.437 123.702 1.00 8.22   ? 743  PRO A C     1 
ATOM   5658  O  O     . PRO A 1  743  ? 107.367 149.443 124.400 1.00 13.81  ? 743  PRO A O     1 
ATOM   5659  C  CB    . PRO A 1  743  ? 106.403 146.392 124.931 1.00 7.14   ? 743  PRO A CB    1 
ATOM   5660  C  CG    . PRO A 1  743  ? 106.461 145.171 124.124 1.00 9.43   ? 743  PRO A CG    1 
ATOM   5661  C  CD    . PRO A 1  743  ? 105.493 145.356 123.039 1.00 7.06   ? 743  PRO A CD    1 
ATOM   5662  N  N     . ASN A 1  744  ? 108.102 148.129 122.736 1.00 6.11   ? 744  ASN A N     1 
ATOM   5663  C  CA    . ASN A 1  744  ? 109.142 149.080 122.359 1.00 0.30   ? 744  ASN A CA    1 
ATOM   5664  C  C     . ASN A 1  744  ? 108.537 150.366 121.830 1.00 1.50   ? 744  ASN A C     1 
ATOM   5665  O  O     . ASN A 1  744  ? 108.982 151.460 122.181 1.00 9.02   ? 744  ASN A O     1 
ATOM   5666  C  CB    . ASN A 1  744  ? 110.069 148.484 121.303 1.00 7.36   ? 744  ASN A CB    1 
ATOM   5667  C  CG    . ASN A 1  744  ? 111.079 147.525 121.878 1.00 11.08  ? 744  ASN A CG    1 
ATOM   5668  O  OD1   . ASN A 1  744  ? 111.423 147.597 123.050 1.00 16.62  ? 744  ASN A OD1   1 
ATOM   5669  N  ND2   . ASN A 1  744  ? 111.575 146.628 121.044 1.00 9.09   ? 744  ASN A ND2   1 
ATOM   5670  N  N     . MET A 1  745  ? 107.521 150.249 120.981 1.00 4.63   ? 745  MET A N     1 
ATOM   5671  C  CA    . MET A 1  745  ? 106.925 151.413 120.341 1.00 1.32   ? 745  MET A CA    1 
ATOM   5672  C  C     . MET A 1  745  ? 106.095 152.229 121.323 1.00 8.34   ? 745  MET A C     1 
ATOM   5673  O  O     . MET A 1  745  ? 106.029 153.455 121.214 1.00 13.11  ? 745  MET A O     1 
ATOM   5674  C  CB    . MET A 1  745  ? 106.072 150.956 119.166 1.00 2.16   ? 745  MET A CB    1 
ATOM   5675  C  CG    . MET A 1  745  ? 105.728 152.026 118.174 1.00 8.77   ? 745  MET A CG    1 
ATOM   5676  S  SD    . MET A 1  745  ? 105.520 151.334 116.533 1.00 22.95  ? 745  MET A SD    1 
ATOM   5677  C  CE    . MET A 1  745  ? 103.973 150.481 116.774 1.00 9.28   ? 745  MET A CE    1 
ATOM   5678  N  N     . ILE A 1  746  ? 105.436 151.566 122.273 1.00 8.09   ? 746  ILE A N     1 
ATOM   5679  C  CA    . ILE A 1  746  ? 104.660 152.277 123.285 1.00 4.76   ? 746  ILE A CA    1 
ATOM   5680  C  C     . ILE A 1  746  ? 105.578 153.092 124.185 1.00 7.23   ? 746  ILE A C     1 
ATOM   5681  O  O     . ILE A 1  746  ? 105.270 154.233 124.539 1.00 9.05   ? 746  ILE A O     1 
ATOM   5682  C  CB    . ILE A 1  746  ? 103.800 151.280 124.086 1.00 5.30   ? 746  ILE A CB    1 
ATOM   5683  C  CG1   . ILE A 1  746  ? 102.738 150.657 123.186 1.00 7.85   ? 746  ILE A CG1   1 
ATOM   5684  C  CG2   . ILE A 1  746  ? 103.116 151.949 125.255 1.00 9.52   ? 746  ILE A CG2   1 
ATOM   5685  C  CD1   . ILE A 1  746  ? 102.223 149.340 123.669 1.00 12.06  ? 746  ILE A CD1   1 
ATOM   5686  N  N     . HIS A 1  747  ? 106.723 152.525 124.559 1.00 4.26   ? 747  HIS A N     1 
ATOM   5687  C  CA    . HIS A 1  747  ? 107.662 153.224 125.425 1.00 2.33   ? 747  HIS A CA    1 
ATOM   5688  C  C     . HIS A 1  747  ? 108.217 154.472 124.756 1.00 7.09   ? 747  HIS A C     1 
ATOM   5689  O  O     . HIS A 1  747  ? 108.361 155.514 125.398 1.00 14.36  ? 747  HIS A O     1 
ATOM   5690  C  CB    . HIS A 1  747  ? 108.788 152.279 125.819 1.00 5.66   ? 747  HIS A CB    1 
ATOM   5691  C  CG    . HIS A 1  747  ? 108.396 151.264 126.846 1.00 9.46   ? 747  HIS A CG    1 
ATOM   5692  N  ND1   . HIS A 1  747  ? 107.107 150.803 126.979 1.00 8.91   ? 747  HIS A ND1   1 
ATOM   5693  C  CD2   . HIS A 1  747  ? 109.133 150.582 127.751 1.00 7.27   ? 747  HIS A CD2   1 
ATOM   5694  C  CE1   . HIS A 1  747  ? 107.060 149.905 127.943 1.00 5.52   ? 747  HIS A CE1   1 
ATOM   5695  N  NE2   . HIS A 1  747  ? 108.277 149.750 128.425 1.00 4.56   ? 747  HIS A NE2   1 
ATOM   5696  N  N     . ILE A 1  748  ? 108.541 154.383 123.467 1.00 5.40   ? 748  ILE A N     1 
ATOM   5697  C  CA    . ILE A 1  748  ? 109.100 155.520 122.746 1.00 0.45   ? 748  ILE A CA    1 
ATOM   5698  C  C     . ILE A 1  748  ? 108.072 156.634 122.608 1.00 3.23   ? 748  ILE A C     1 
ATOM   5699  O  O     . ILE A 1  748  ? 108.389 157.810 122.795 1.00 12.20  ? 748  ILE A O     1 
ATOM   5700  C  CB    . ILE A 1  748  ? 109.622 155.065 121.370 1.00 4.32   ? 748  ILE A CB    1 
ATOM   5701  C  CG1   . ILE A 1  748  ? 110.767 154.072 121.522 1.00 7.26   ? 748  ILE A CG1   1 
ATOM   5702  C  CG2   . ILE A 1  748  ? 110.083 156.245 120.534 1.00 6.10   ? 748  ILE A CG2   1 
ATOM   5703  C  CD1   . ILE A 1  748  ? 111.112 153.366 120.247 1.00 3.63   ? 748  ILE A CD1   1 
ATOM   5704  N  N     . MET A 1  749  ? 106.833 156.290 122.272 1.00 4.14   ? 749  MET A N     1 
ATOM   5705  C  CA    . MET A 1  749  ? 105.862 157.264 121.791 1.00 1.56   ? 749  MET A CA    1 
ATOM   5706  C  C     . MET A 1  749  ? 104.852 157.714 122.839 1.00 6.53   ? 749  MET A C     1 
ATOM   5707  O  O     . MET A 1  749  ? 104.450 158.876 122.827 1.00 8.07   ? 749  MET A O     1 
ATOM   5708  C  CB    . MET A 1  749  ? 105.123 156.690 120.583 1.00 3.07   ? 749  MET A CB    1 
ATOM   5709  C  CG    . MET A 1  749  ? 106.056 156.155 119.513 1.00 5.49   ? 749  MET A CG    1 
ATOM   5710  S  SD    . MET A 1  749  ? 105.461 156.132 117.824 1.00 9.02   ? 749  MET A SD    1 
ATOM   5711  C  CE    . MET A 1  749  ? 104.347 157.512 117.825 1.00 7.72   ? 749  MET A CE    1 
ATOM   5712  N  N     . ALA A 1  750  ? 104.425 156.837 123.747 1.00 11.11  ? 750  ALA A N     1 
ATOM   5713  C  CA    . ALA A 1  750  ? 103.321 157.137 124.653 1.00 3.40   ? 750  ALA A CA    1 
ATOM   5714  C  C     . ALA A 1  750  ? 103.733 157.179 126.120 1.00 10.42  ? 750  ALA A C     1 
ATOM   5715  O  O     . ALA A 1  750  ? 103.540 158.198 126.781 1.00 16.47  ? 750  ALA A O     1 
ATOM   5716  C  CB    . ALA A 1  750  ? 102.199 156.120 124.439 1.00 4.14   ? 750  ALA A CB    1 
ATOM   5717  N  N     . GLY A 1  751  ? 104.290 156.105 126.657 1.00 6.81   ? 751  GLY A N     1 
ATOM   5718  C  CA    . GLY A 1  751  ? 104.699 156.102 128.048 1.00 5.57   ? 751  GLY A CA    1 
ATOM   5719  C  C     . GLY A 1  751  ? 105.343 154.784 128.411 1.00 7.61   ? 751  GLY A C     1 
ATOM   5720  O  O     . GLY A 1  751  ? 105.120 153.759 127.765 1.00 18.05  ? 751  GLY A O     1 
ATOM   5721  N  N     . ILE A 1  752  ? 106.140 154.830 129.469 1.00 6.15   ? 752  ILE A N     1 
ATOM   5722  C  CA    . ILE A 1  752  ? 106.871 153.650 129.917 1.00 1.72   ? 752  ILE A CA    1 
ATOM   5723  C  C     . ILE A 1  752  ? 106.069 152.844 130.931 1.00 7.93   ? 752  ILE A C     1 
ATOM   5724  O  O     . ILE A 1  752  ? 106.074 151.614 130.890 1.00 13.99  ? 752  ILE A O     1 
ATOM   5725  C  CB    . ILE A 1  752  ? 108.246 154.068 130.472 1.00 2.91   ? 752  ILE A CB    1 
ATOM   5726  C  CG1   . ILE A 1  752  ? 109.087 154.690 129.358 1.00 8.37   ? 752  ILE A CG1   1 
ATOM   5727  C  CG2   . ILE A 1  752  ? 108.969 152.890 131.049 1.00 1.35   ? 752  ILE A CG2   1 
ATOM   5728  C  CD1   . ILE A 1  752  ? 110.364 155.283 129.813 1.00 5.74   ? 752  ILE A CD1   1 
ATOM   5729  N  N     . GLY A 1  753  ? 105.361 153.505 131.845 1.00 8.22   ? 753  GLY A N     1 
ATOM   5730  C  CA    . GLY A 1  753  ? 104.507 152.793 132.777 1.00 3.72   ? 753  GLY A CA    1 
ATOM   5731  C  C     . GLY A 1  753  ? 105.236 152.361 134.039 1.00 8.59   ? 753  GLY A C     1 
ATOM   5732  O  O     . GLY A 1  753  ? 106.132 153.040 134.529 1.00 21.73  ? 753  GLY A O     1 
ATOM   5733  N  N     . GLN A 1  754  ? 104.849 151.202 134.559 1.00 3.60   ? 754  GLN A N     1 
ATOM   5734  C  CA    . GLN A 1  754  ? 105.344 150.734 135.843 1.00 11.26  ? 754  GLN A CA    1 
ATOM   5735  C  C     . GLN A 1  754  ? 106.579 149.860 135.668 1.00 14.70  ? 754  GLN A C     1 
ATOM   5736  O  O     . GLN A 1  754  ? 106.605 148.973 134.813 1.00 19.55  ? 754  GLN A O     1 
ATOM   5737  C  CB    . GLN A 1  754  ? 104.250 149.973 136.590 1.00 12.52  ? 754  GLN A CB    1 
ATOM   5738  C  CG    . GLN A 1  754  ? 104.704 149.254 137.842 1.00 11.56  ? 754  GLN A CG    1 
ATOM   5739  C  CD    . GLN A 1  754  ? 105.102 150.185 138.960 1.00 13.97  ? 754  GLN A CD    1 
ATOM   5740  O  OE1   . GLN A 1  754  ? 104.371 151.100 139.314 1.00 15.15  ? 754  GLN A OE1   1 
ATOM   5741  N  NE2   . GLN A 1  754  ? 106.263 149.940 139.538 1.00 12.44  ? 754  GLN A NE2   1 
ATOM   5742  N  N     . ILE A 1  755  ? 107.600 150.127 136.477 1.00 12.63  ? 755  ILE A N     1 
ATOM   5743  C  CA    . ILE A 1  755  ? 108.822 149.333 136.500 1.00 16.44  ? 755  ILE A CA    1 
ATOM   5744  C  C     . ILE A 1  755  ? 108.606 148.133 137.411 1.00 17.75  ? 755  ILE A C     1 
ATOM   5745  O  O     . ILE A 1  755  ? 108.275 148.287 138.589 1.00 23.47  ? 755  ILE A O     1 
ATOM   5746  C  CB    . ILE A 1  755  ? 110.016 150.174 136.976 1.00 16.63  ? 755  ILE A CB    1 
ATOM   5747  C  CG1   . ILE A 1  755  ? 110.352 151.266 135.965 1.00 8.42   ? 755  ILE A CG1   1 
ATOM   5748  C  CG2   . ILE A 1  755  ? 111.221 149.296 137.257 1.00 14.34  ? 755  ILE A CG2   1 
ATOM   5749  C  CD1   . ILE A 1  755  ? 110.940 150.756 134.703 1.00 14.72  ? 755  ILE A CD1   1 
ATOM   5750  N  N     . GLU A 1  756  ? 108.795 146.936 136.869 1.00 22.18  ? 756  GLU A N     1 
ATOM   5751  C  CA    . GLU A 1  756  ? 108.670 145.698 137.622 1.00 19.76  ? 756  GLU A CA    1 
ATOM   5752  C  C     . GLU A 1  756  ? 110.028 145.026 137.722 1.00 22.26  ? 756  GLU A C     1 
ATOM   5753  O  O     . GLU A 1  756  ? 110.650 144.724 136.703 1.00 24.65  ? 756  GLU A O     1 
ATOM   5754  C  CB    . GLU A 1  756  ? 107.673 144.747 136.958 1.00 23.06  ? 756  GLU A CB    1 
ATOM   5755  C  CG    . GLU A 1  756  ? 106.221 145.137 137.131 1.00 22.97  ? 756  GLU A CG    1 
ATOM   5756  C  CD    . GLU A 1  756  ? 105.551 145.505 135.818 1.00 30.72  ? 756  GLU A CD    1 
ATOM   5757  O  OE1   . GLU A 1  756  ? 104.326 145.733 135.814 1.00 28.96  ? 756  GLU A OE1   1 
ATOM   5758  O  OE2   . GLU A 1  756  ? 106.248 145.563 134.786 1.00 30.63  ? 756  GLU A OE2   1 
ATOM   5759  N  N     . ILE A 1  757  ? 110.479 144.789 138.947 1.00 26.80  ? 757  ILE A N     1 
ATOM   5760  C  CA    . ILE A 1  757  ? 111.680 144.013 139.218 1.00 25.85  ? 757  ILE A CA    1 
ATOM   5761  C  C     . ILE A 1  757  ? 111.248 142.798 140.019 1.00 31.05  ? 757  ILE A C     1 
ATOM   5762  O  O     . ILE A 1  757  ? 110.659 142.944 141.097 1.00 35.28  ? 757  ILE A O     1 
ATOM   5763  C  CB    . ILE A 1  757  ? 112.734 144.830 139.980 1.00 26.06  ? 757  ILE A CB    1 
ATOM   5764  C  CG1   . ILE A 1  757  ? 113.353 145.894 139.072 1.00 24.41  ? 757  ILE A CG1   1 
ATOM   5765  C  CG2   . ILE A 1  757  ? 113.801 143.920 140.548 1.00 27.14  ? 757  ILE A CG2   1 
ATOM   5766  C  CD1   . ILE A 1  757  ? 114.211 146.894 139.795 1.00 22.99  ? 757  ILE A CD1   1 
ATOM   5767  N  N     . ASN A 1  758  ? 111.540 141.606 139.498 1.00 30.24  ? 758  ASN A N     1 
ATOM   5768  C  CA    . ASN A 1  758  ? 111.051 140.347 140.062 1.00 31.84  ? 758  ASN A CA    1 
ATOM   5769  C  C     . ASN A 1  758  ? 109.532 140.370 140.197 1.00 29.64  ? 758  ASN A C     1 
ATOM   5770  O  O     . ASN A 1  758  ? 108.969 140.004 141.229 1.00 27.03  ? 758  ASN A O     1 
ATOM   5771  C  CB    . ASN A 1  758  ? 111.713 140.046 141.406 1.00 30.74  ? 758  ASN A CB    1 
ATOM   5772  C  CG    . ASN A 1  758  ? 113.157 139.633 141.264 1.00 34.89  ? 758  ASN A CG    1 
ATOM   5773  O  OD1   . ASN A 1  758  ? 113.739 139.056 142.179 1.00 35.80  ? 758  ASN A OD1   1 
ATOM   5774  N  ND2   . ASN A 1  758  ? 113.743 139.915 140.110 1.00 35.58  ? 758  ASN A ND2   1 
ATOM   5775  N  N     . THR A 1  759  ? 108.875 140.822 139.127 1.00 33.77  ? 759  THR A N     1 
ATOM   5776  C  CA    . THR A 1  759  ? 107.431 141.040 139.032 1.00 36.20  ? 759  THR A CA    1 
ATOM   5777  C  C     . THR A 1  759  ? 106.891 141.737 140.278 1.00 33.14  ? 759  THR A C     1 
ATOM   5778  O  O     . THR A 1  759  ? 105.752 141.515 140.695 1.00 36.03  ? 759  THR A O     1 
ATOM   5779  C  CB    . THR A 1  759  ? 106.686 139.722 138.721 1.00 37.11  ? 759  THR A CB    1 
ATOM   5780  O  OG1   . THR A 1  759  ? 105.345 140.017 138.307 1.00 41.49  ? 759  THR A OG1   1 
ATOM   5781  C  CG2   . THR A 1  759  ? 106.643 138.743 139.898 1.00 32.68  ? 759  THR A CG2   1 
ATOM   5782  N  N     . GLN A 1  760  ? 107.695 142.633 140.840 1.00 26.21  ? 760  GLN A N     1 
ATOM   5783  C  CA    . GLN A 1  760  ? 107.328 143.405 142.014 1.00 25.90  ? 760  GLN A CA    1 
ATOM   5784  C  C     . GLN A 1  760  ? 107.710 144.857 141.767 1.00 26.39  ? 760  GLN A C     1 
ATOM   5785  O  O     . GLN A 1  760  ? 108.622 145.145 140.993 1.00 28.16  ? 760  GLN A O     1 
ATOM   5786  C  CB    . GLN A 1  760  ? 108.033 142.859 143.259 1.00 28.11  ? 760  GLN A CB    1 
ATOM   5787  C  CG    . GLN A 1  760  ? 107.274 143.026 144.552 1.00 29.47  ? 760  GLN A CG    1 
ATOM   5788  C  CD    . GLN A 1  760  ? 107.963 142.328 145.709 1.00 32.21  ? 760  GLN A CD    1 
ATOM   5789  O  OE1   . GLN A 1  760  ? 109.073 141.816 145.566 1.00 31.50  ? 760  GLN A OE1   1 
ATOM   5790  N  NE2   . GLN A 1  760  ? 107.316 142.323 146.870 1.00 29.42  ? 760  GLN A NE2   1 
ATOM   5791  N  N     . ARG A 1  761  ? 107.016 145.773 142.433 1.00 22.95  ? 761  ARG A N     1 
ATOM   5792  C  CA    . ARG A 1  761  ? 107.328 147.194 142.317 1.00 19.73  ? 761  ARG A CA    1 
ATOM   5793  C  C     . ARG A 1  761  ? 108.664 147.475 142.999 1.00 22.31  ? 761  ARG A C     1 
ATOM   5794  O  O     . ARG A 1  761  ? 109.371 146.571 143.450 1.00 20.85  ? 761  ARG A O     1 
ATOM   5795  C  CB    . ARG A 1  761  ? 106.209 148.049 142.902 1.00 12.98  ? 761  ARG A CB    1 
ATOM   5796  C  CG    . ARG A 1  761  ? 104.856 147.815 142.291 1.00 15.43  ? 761  ARG A CG    1 
ATOM   5797  C  CD    . ARG A 1  761  ? 103.923 148.978 142.532 1.00 17.35  ? 761  ARG A CD    1 
ATOM   5798  N  NE    . ARG A 1  761  ? 103.719 149.212 143.953 1.00 18.55  ? 761  ARG A NE    1 
ATOM   5799  C  CZ    . ARG A 1  761  ? 103.037 150.227 144.461 1.00 20.26  ? 761  ARG A CZ    1 
ATOM   5800  N  NH1   . ARG A 1  761  ? 102.455 151.126 143.690 1.00 19.67  ? 761  ARG A NH1   1 
ATOM   5801  N  NH2   . ARG A 1  761  ? 102.936 150.343 145.780 1.00 22.30  ? 761  ARG A NH2   1 
ATOM   5802  N  N     . ILE A 1  762  ? 109.034 148.749 143.067 1.00 21.16  ? 762  ILE A N     1 
ATOM   5803  C  CA    . ILE A 1  762  ? 110.292 149.156 143.681 1.00 15.81  ? 762  ILE A CA    1 
ATOM   5804  C  C     . ILE A 1  762  ? 110.123 149.057 145.192 1.00 19.04  ? 762  ILE A C     1 
ATOM   5805  O  O     . ILE A 1  762  ? 109.278 149.735 145.777 1.00 23.43  ? 762  ILE A O     1 
ATOM   5806  C  CB    . ILE A 1  762  ? 110.701 150.569 143.251 1.00 16.62  ? 762  ILE A CB    1 
ATOM   5807  C  CG1   . ILE A 1  762  ? 110.965 150.615 141.748 1.00 17.96  ? 762  ILE A CG1   1 
ATOM   5808  C  CG2   . ILE A 1  762  ? 111.947 151.007 143.969 1.00 18.49  ? 762  ILE A CG2   1 
ATOM   5809  C  CD1   . ILE A 1  762  ? 112.134 149.798 141.315 1.00 19.41  ? 762  ILE A CD1   1 
ATOM   5810  N  N     . GLN A 1  763  ? 110.902 148.191 145.817 1.00 25.56  ? 763  GLN A N     1 
ATOM   5811  C  CA    . GLN A 1  763  ? 110.834 147.983 147.259 1.00 24.39  ? 763  GLN A CA    1 
ATOM   5812  C  C     . GLN A 1  763  ? 111.558 149.106 147.987 1.00 25.49  ? 763  GLN A C     1 
ATOM   5813  O  O     . GLN A 1  763  ? 112.638 149.513 147.559 1.00 33.11  ? 763  GLN A O     1 
ATOM   5814  C  CB    . GLN A 1  763  ? 111.445 146.641 147.622 1.00 24.57  ? 763  GLN A CB    1 
ATOM   5815  C  CG    . GLN A 1  763  ? 110.579 145.465 147.241 1.00 22.99  ? 763  GLN A CG    1 
ATOM   5816  C  CD    . GLN A 1  763  ? 109.102 145.794 147.296 1.00 31.16  ? 763  GLN A CD    1 
ATOM   5817  O  OE1   . GLN A 1  763  ? 108.410 145.772 146.280 1.00 30.27  ? 763  GLN A OE1   1 
ATOM   5818  N  NE2   . GLN A 1  763  ? 108.601 146.071 148.493 1.00 33.36  ? 763  GLN A NE2   1 
ATOM   5819  N  N     . PRO A 1  764  ? 111.009 149.625 149.078 1.00 17.33  ? 764  PRO A N     1 
ATOM   5820  C  CA    . PRO A 1  764  ? 111.673 150.737 149.762 1.00 20.05  ? 764  PRO A CA    1 
ATOM   5821  C  C     . PRO A 1  764  ? 112.920 150.303 150.511 1.00 23.66  ? 764  PRO A C     1 
ATOM   5822  O  O     . PRO A 1  764  ? 112.840 149.717 151.591 1.00 28.66  ? 764  PRO A O     1 
ATOM   5823  C  CB    . PRO A 1  764  ? 110.590 151.263 150.710 1.00 15.72  ? 764  PRO A CB    1 
ATOM   5824  C  CG    . PRO A 1  764  ? 109.681 150.149 150.899 1.00 21.18  ? 764  PRO A CG    1 
ATOM   5825  C  CD    . PRO A 1  764  ? 109.681 149.351 149.640 1.00 23.62  ? 764  PRO A CD    1 
ATOM   5826  N  N     . GLN A 1  765  ? 114.083 150.604 149.935 1.00 24.52  ? 765  GLN A N     1 
ATOM   5827  C  CA    . GLN A 1  765  ? 115.376 150.280 150.521 1.00 21.58  ? 765  GLN A CA    1 
ATOM   5828  C  C     . GLN A 1  765  ? 116.188 151.519 150.869 1.00 26.40  ? 765  GLN A C     1 
ATOM   5829  O  O     . GLN A 1  765  ? 117.387 151.407 151.135 1.00 34.57  ? 765  GLN A O     1 
ATOM   5830  C  CB    . GLN A 1  765  ? 116.177 149.384 149.576 1.00 24.87  ? 765  GLN A CB    1 
ATOM   5831  C  CG    . GLN A 1  765  ? 115.495 148.067 149.264 1.00 27.95  ? 765  GLN A CG    1 
ATOM   5832  C  CD    . GLN A 1  765  ? 116.479 146.952 148.976 1.00 34.44  ? 765  GLN A CD    1 
ATOM   5833  O  OE1   . GLN A 1  765  ? 117.685 147.176 148.896 1.00 31.38  ? 765  GLN A OE1   1 
ATOM   5834  N  NE2   . GLN A 1  765  ? 115.965 145.741 148.812 1.00 32.93  ? 765  GLN A NE2   1 
ATOM   5835  N  N     . PHE A 1  766  ? 115.579 152.697 150.850 1.00 19.88  ? 766  PHE A N     1 
ATOM   5836  C  CA    . PHE A 1  766  ? 116.219 153.915 151.336 1.00 16.24  ? 766  PHE A CA    1 
ATOM   5837  C  C     . PHE A 1  766  ? 115.617 154.291 152.689 1.00 21.51  ? 766  PHE A C     1 
ATOM   5838  O  O     . PHE A 1  766  ? 114.704 155.104 152.792 1.00 29.71  ? 766  PHE A O     1 
ATOM   5839  C  CB    . PHE A 1  766  ? 116.047 155.038 150.319 1.00 11.20  ? 766  PHE A CB    1 
ATOM   5840  C  CG    . PHE A 1  766  ? 116.806 156.293 150.639 1.00 12.44  ? 766  PHE A CG    1 
ATOM   5841  C  CD1   . PHE A 1  766  ? 118.109 156.453 150.234 1.00 15.31  ? 766  PHE A CD1   1 
ATOM   5842  C  CD2   . PHE A 1  766  ? 116.204 157.321 151.330 1.00 14.11  ? 766  PHE A CD2   1 
ATOM   5843  C  CE1   . PHE A 1  766  ? 118.790 157.605 150.512 1.00 11.25  ? 766  PHE A CE1   1 
ATOM   5844  C  CE2   . PHE A 1  766  ? 116.891 158.473 151.612 1.00 13.62  ? 766  PHE A CE2   1 
ATOM   5845  C  CZ    . PHE A 1  766  ? 118.180 158.612 151.202 1.00 9.51   ? 766  PHE A CZ    1 
ATOM   5846  N  N     . SER A 1  767  ? 116.145 153.668 153.740 1.00 12.55  ? 767  SER A N     1 
ATOM   5847  C  CA    . SER A 1  767  ? 115.869 154.063 155.120 1.00 17.56  ? 767  SER A CA    1 
ATOM   5848  C  C     . SER A 1  767  ? 114.391 153.908 155.498 1.00 18.08  ? 767  SER A C     1 
ATOM   5849  O  O     . SER A 1  767  ? 113.687 154.881 155.771 1.00 20.72  ? 767  SER A O     1 
ATOM   5850  C  CB    . SER A 1  767  ? 116.321 155.505 155.364 1.00 17.90  ? 767  SER A CB    1 
ATOM   5851  O  OG    . SER A 1  767  ? 115.349 156.420 154.908 1.00 20.15  ? 767  SER A OG    1 
ATOM   5852  N  N     . PHE A 1  768  ? 113.948 152.651 155.547 1.00 23.01  ? 768  PHE A N     1 
ATOM   5853  C  CA    . PHE A 1  768  ? 112.720 152.270 156.257 1.00 24.95  ? 768  PHE A CA    1 
ATOM   5854  C  C     . PHE A 1  768  ? 111.490 153.001 155.710 1.00 21.94  ? 768  PHE A C     1 
ATOM   5855  O  O     . PHE A 1  768  ? 110.938 153.907 156.325 1.00 19.31  ? 768  PHE A O     1 
ATOM   5856  C  CB    . PHE A 1  768  ? 112.843 152.500 157.769 1.00 18.70  ? 768  PHE A CB    1 
ATOM   5857  C  CG    . PHE A 1  768  ? 111.570 152.221 158.522 1.00 21.02  ? 768  PHE A CG    1 
ATOM   5858  C  CD1   . PHE A 1  768  ? 111.005 150.962 158.514 1.00 24.19  ? 768  PHE A CD1   1 
ATOM   5859  C  CD2   . PHE A 1  768  ? 110.921 153.230 159.208 1.00 22.97  ? 768  PHE A CD2   1 
ATOM   5860  C  CE1   . PHE A 1  768  ? 109.832 150.714 159.178 1.00 22.34  ? 768  PHE A CE1   1 
ATOM   5861  C  CE2   . PHE A 1  768  ? 109.747 152.983 159.875 1.00 21.44  ? 768  PHE A CE2   1 
ATOM   5862  C  CZ    . PHE A 1  768  ? 109.206 151.726 159.861 1.00 21.60  ? 768  PHE A CZ    1 
ATOM   5863  N  N     . GLY A 1  769  ? 111.098 152.611 154.508 1.00 19.66  ? 769  GLY A N     1 
ATOM   5864  C  CA    . GLY A 1  769  ? 109.848 153.074 153.955 1.00 18.87  ? 769  GLY A CA    1 
ATOM   5865  C  C     . GLY A 1  769  ? 109.956 154.182 152.947 1.00 23.38  ? 769  GLY A C     1 
ATOM   5866  O  O     . GLY A 1  769  ? 108.921 154.708 152.528 1.00 23.69  ? 769  GLY A O     1 
ATOM   5867  N  N     . ARG A 1  770  ? 111.167 154.566 152.558 1.00 23.39  ? 770  ARG A N     1 
ATOM   5868  C  CA    . ARG A 1  770  ? 111.402 155.438 151.420 1.00 16.88  ? 770  ARG A CA    1 
ATOM   5869  C  C     . ARG A 1  770  ? 112.081 154.637 150.324 1.00 14.02  ? 770  ARG A C     1 
ATOM   5870  O  O     . ARG A 1  770  ? 112.896 153.757 150.605 1.00 8.85   ? 770  ARG A O     1 
ATOM   5871  C  CB    . ARG A 1  770  ? 112.273 156.626 151.788 1.00 11.37  ? 770  ARG A CB    1 
ATOM   5872  C  CG    . ARG A 1  770  ? 112.029 157.173 153.152 1.00 15.59  ? 770  ARG A CG    1 
ATOM   5873  C  CD    . ARG A 1  770  ? 113.050 158.215 153.472 1.00 17.46  ? 770  ARG A CD    1 
ATOM   5874  N  NE    . ARG A 1  770  ? 112.821 159.453 152.746 1.00 11.97  ? 770  ARG A NE    1 
ATOM   5875  C  CZ    . ARG A 1  770  ? 113.704 160.433 152.659 1.00 9.64   ? 770  ARG A CZ    1 
ATOM   5876  N  NH1   . ARG A 1  770  ? 114.893 160.339 153.218 1.00 11.75  ? 770  ARG A NH1   1 
ATOM   5877  N  NH2   . ARG A 1  770  ? 113.387 161.532 151.990 1.00 11.20  ? 770  ARG A NH2   1 
ATOM   5878  N  N     . THR A 1  771  ? 111.729 154.929 149.077 1.00 12.03  ? 771  THR A N     1 
ATOM   5879  C  CA    . THR A 1  771  ? 112.447 154.357 147.948 1.00 11.46  ? 771  THR A CA    1 
ATOM   5880  C  C     . THR A 1  771  ? 113.639 155.200 147.530 1.00 12.50  ? 771  THR A C     1 
ATOM   5881  O  O     . THR A 1  771  ? 114.696 154.650 147.220 1.00 18.35  ? 771  THR A O     1 
ATOM   5882  C  CB    . THR A 1  771  ? 111.509 154.176 146.756 1.00 13.57  ? 771  THR A CB    1 
ATOM   5883  O  OG1   . THR A 1  771  ? 110.789 155.390 146.531 1.00 22.55  ? 771  THR A OG1   1 
ATOM   5884  C  CG2   . THR A 1  771  ? 110.531 153.052 147.010 1.00 9.32   ? 771  THR A CG2   1 
ATOM   5885  N  N     . LEU A 1  772  ? 113.500 156.520 147.545 1.00 6.33   ? 772  LEU A N     1 
ATOM   5886  C  CA    . LEU A 1  772  ? 114.566 157.432 147.174 1.00 2.25   ? 772  LEU A CA    1 
ATOM   5887  C  C     . LEU A 1  772  ? 114.520 158.623 148.112 1.00 0.63   ? 772  LEU A C     1 
ATOM   5888  O  O     . LEU A 1  772  ? 113.571 158.800 148.871 1.00 8.25   ? 772  LEU A O     1 
ATOM   5889  C  CB    . LEU A 1  772  ? 114.440 157.900 145.720 1.00 5.40   ? 772  LEU A CB    1 
ATOM   5890  C  CG    . LEU A 1  772  ? 114.719 156.916 144.592 1.00 4.54   ? 772  LEU A CG    1 
ATOM   5891  C  CD1   . LEU A 1  772  ? 114.418 157.562 143.271 1.00 5.57   ? 772  LEU A CD1   1 
ATOM   5892  C  CD2   . LEU A 1  772  ? 116.151 156.430 144.640 1.00 0.87   ? 772  LEU A CD2   1 
ATOM   5893  N  N     . VAL A 1  773  ? 115.570 159.442 148.060 1.00 0.49   ? 773  VAL A N     1 
ATOM   5894  C  CA    . VAL A 1  773  ? 115.625 160.659 148.854 1.00 13.78  ? 773  VAL A CA    1 
ATOM   5895  C  C     . VAL A 1  773  ? 114.626 161.704 148.390 1.00 2.30   ? 773  VAL A C     1 
ATOM   5896  O  O     . VAL A 1  773  ? 114.378 162.671 149.109 1.00 9.61   ? 773  VAL A O     1 
ATOM   5897  C  CB    . VAL A 1  773  ? 117.065 161.212 148.834 1.00 6.86   ? 773  VAL A CB    1 
ATOM   5898  C  CG1   . VAL A 1  773  ? 117.377 161.882 147.512 1.00 3.78   ? 773  VAL A CG1   1 
ATOM   5899  C  CG2   . VAL A 1  773  ? 117.306 162.158 149.989 1.00 9.72   ? 773  VAL A CG2   1 
ATOM   5900  N  N     . TYR A 1  774  ? 114.041 161.532 147.208 1.00 7.37   ? 774  TYR A N     1 
ATOM   5901  C  CA    . TYR A 1  774  ? 113.084 162.493 146.679 1.00 2.87   ? 774  TYR A CA    1 
ATOM   5902  C  C     . TYR A 1  774  ? 111.668 162.246 147.159 1.00 6.71   ? 774  TYR A C     1 
ATOM   5903  O  O     . TYR A 1  774  ? 110.810 163.107 146.970 1.00 9.87   ? 774  TYR A O     1 
ATOM   5904  C  CB    . TYR A 1  774  ? 113.107 162.468 145.153 1.00 3.14   ? 774  TYR A CB    1 
ATOM   5905  C  CG    . TYR A 1  774  ? 114.462 162.762 144.577 1.00 3.68   ? 774  TYR A CG    1 
ATOM   5906  C  CD1   . TYR A 1  774  ? 115.075 163.977 144.804 1.00 5.55   ? 774  TYR A CD1   1 
ATOM   5907  C  CD2   . TYR A 1  774  ? 115.128 161.828 143.813 1.00 0.81   ? 774  TYR A CD2   1 
ATOM   5908  C  CE1   . TYR A 1  774  ? 116.299 164.255 144.293 1.00 1.71   ? 774  TYR A CE1   1 
ATOM   5909  C  CE2   . TYR A 1  774  ? 116.359 162.102 143.291 1.00 3.11   ? 774  TYR A CE2   1 
ATOM   5910  C  CZ    . TYR A 1  774  ? 116.939 163.318 143.539 1.00 3.64   ? 774  TYR A CZ    1 
ATOM   5911  O  OH    . TYR A 1  774  ? 118.173 163.602 143.030 1.00 12.78  ? 774  TYR A OH    1 
ATOM   5912  N  N     . TYR A 1  775  ? 111.407 161.123 147.762 1.00 5.61   ? 775  TYR A N     1 
ATOM   5913  C  CA    . TYR A 1  775  ? 110.057 160.840 148.190 1.00 2.85   ? 775  TYR A CA    1 
ATOM   5914  C  C     . TYR A 1  775  ? 109.979 160.715 149.702 1.00 7.07   ? 775  TYR A C     1 
ATOM   5915  O  O     . TYR A 1  775  ? 110.955 160.318 150.342 1.00 7.35   ? 775  TYR A O     1 
ATOM   5916  C  CB    . TYR A 1  775  ? 109.542 159.559 147.531 1.00 7.03   ? 775  TYR A CB    1 
ATOM   5917  C  CG    . TYR A 1  775  ? 109.454 159.711 146.040 1.00 7.16   ? 775  TYR A CG    1 
ATOM   5918  C  CD1   . TYR A 1  775  ? 108.547 160.592 145.486 1.00 2.63   ? 775  TYR A CD1   1 
ATOM   5919  C  CD2   . TYR A 1  775  ? 110.286 159.005 145.189 1.00 5.52   ? 775  TYR A CD2   1 
ATOM   5920  C  CE1   . TYR A 1  775  ? 108.462 160.763 144.143 1.00 0.08   ? 775  TYR A CE1   1 
ATOM   5921  C  CE2   . TYR A 1  775  ? 110.202 159.172 143.836 1.00 2.04   ? 775  TYR A CE2   1 
ATOM   5922  C  CZ    . TYR A 1  775  ? 109.285 160.054 143.322 1.00 4.37   ? 775  TYR A CZ    1 
ATOM   5923  O  OH    . TYR A 1  775  ? 109.179 160.241 141.973 1.00 8.22   ? 775  TYR A OH    1 
ATOM   5924  N  N     . PRO A 1  776  ? 108.850 161.080 150.300 1.00 13.62  ? 776  PRO A N     1 
ATOM   5925  C  CA    . PRO A 1  776  ? 108.709 160.960 151.753 1.00 9.32   ? 776  PRO A CA    1 
ATOM   5926  C  C     . PRO A 1  776  ? 108.555 159.512 152.184 1.00 9.15   ? 776  PRO A C     1 
ATOM   5927  O  O     . PRO A 1  776  ? 108.356 158.601 151.384 1.00 14.58  ? 776  PRO A O     1 
ATOM   5928  C  CB    . PRO A 1  776  ? 107.453 161.775 152.055 1.00 7.84   ? 776  PRO A CB    1 
ATOM   5929  C  CG    . PRO A 1  776  ? 106.703 161.779 150.809 1.00 7.49   ? 776  PRO A CG    1 
ATOM   5930  C  CD    . PRO A 1  776  ? 107.694 161.756 149.697 1.00 8.90   ? 776  PRO A CD    1 
ATOM   5931  N  N     . ARG A 1  777  ? 108.681 159.308 153.486 1.00 15.99  ? 777  ARG A N     1 
ATOM   5932  C  CA    . ARG A 1  777  ? 108.472 157.991 154.066 1.00 16.34  ? 777  ARG A CA    1 
ATOM   5933  C  C     . ARG A 1  777  ? 106.993 157.632 154.053 1.00 19.70  ? 777  ARG A C     1 
ATOM   5934  O  O     . ARG A 1  777  ? 106.133 158.479 154.303 1.00 24.49  ? 777  ARG A O     1 
ATOM   5935  C  CB    . ARG A 1  777  ? 109.011 157.965 155.489 1.00 17.70  ? 777  ARG A CB    1 
ATOM   5936  C  CG    . ARG A 1  777  ? 109.600 156.646 155.902 1.00 21.62  ? 777  ARG A CG    1 
ATOM   5937  C  CD    . ARG A 1  777  ? 109.683 156.537 157.412 1.00 19.62  ? 777  ARG A CD    1 
ATOM   5938  N  NE    . ARG A 1  777  ? 110.563 157.543 157.990 1.00 15.59  ? 777  ARG A NE    1 
ATOM   5939  C  CZ    . ARG A 1  777  ? 111.884 157.531 157.895 1.00 21.04  ? 777  ARG A CZ    1 
ATOM   5940  N  NH1   . ARG A 1  777  ? 112.525 156.574 157.246 1.00 17.36  ? 777  ARG A NH1   1 
ATOM   5941  N  NH2   . ARG A 1  777  ? 112.582 158.507 158.465 1.00 22.40  ? 777  ARG A NH2   1 
ATOM   5942  N  N     . PHE A 1  778  ? 106.702 156.362 153.774 1.00 14.86  ? 778  PHE A N     1 
ATOM   5943  C  CA    . PHE A 1  778  ? 105.328 155.862 153.662 1.00 16.16  ? 778  PHE A CA    1 
ATOM   5944  C  C     . PHE A 1  778  ? 104.534 156.658 152.635 1.00 20.97  ? 778  PHE A C     1 
ATOM   5945  O  O     . PHE A 1  778  ? 103.378 157.017 152.857 1.00 25.82  ? 778  PHE A O     1 
ATOM   5946  C  CB    . PHE A 1  778  ? 104.611 155.866 155.014 1.00 17.62  ? 778  PHE A CB    1 
ATOM   5947  C  CG    . PHE A 1  778  ? 105.404 155.254 156.110 1.00 17.36  ? 778  PHE A CG    1 
ATOM   5948  C  CD1   . PHE A 1  778  ? 105.885 153.972 155.993 1.00 16.15  ? 778  PHE A CD1   1 
ATOM   5949  C  CD2   . PHE A 1  778  ? 105.694 155.971 157.243 1.00 13.97  ? 778  PHE A CD2   1 
ATOM   5950  C  CE1   . PHE A 1  778  ? 106.627 153.420 156.985 1.00 20.24  ? 778  PHE A CE1   1 
ATOM   5951  C  CE2   . PHE A 1  778  ? 106.435 155.421 158.232 1.00 15.34  ? 778  PHE A CE2   1 
ATOM   5952  C  CZ    . PHE A 1  778  ? 106.901 154.145 158.107 1.00 21.39  ? 778  PHE A CZ    1 
ATOM   5953  N  N     . ALA A 1  779  ? 105.164 156.949 151.504 1.00 20.85  ? 779  ALA A N     1 
ATOM   5954  C  CA    . ALA A 1  779  ? 104.490 157.677 150.441 1.00 19.75  ? 779  ALA A CA    1 
ATOM   5955  C  C     . ALA A 1  779  ? 103.462 156.784 149.766 1.00 20.56  ? 779  ALA A C     1 
ATOM   5956  O  O     . ALA A 1  779  ? 103.644 155.569 149.665 1.00 18.58  ? 779  ALA A O     1 
ATOM   5957  C  CB    . ALA A 1  779  ? 105.504 158.185 149.422 1.00 18.72  ? 779  ALA A CB    1 
ATOM   5958  N  N     . LEU A 1  780  ? 102.370 157.392 149.306 1.00 23.44  ? 780  LEU A N     1 
ATOM   5959  C  CA    . LEU A 1  780  ? 101.280 156.641 148.699 1.00 25.25  ? 780  LEU A CA    1 
ATOM   5960  C  C     . LEU A 1  780  ? 101.220 156.760 147.187 1.00 24.77  ? 780  LEU A C     1 
ATOM   5961  O  O     . LEU A 1  780  ? 100.647 155.879 146.545 1.00 26.56  ? 780  LEU A O     1 
ATOM   5962  C  CB    . LEU A 1  780  ? 99.935  157.087 149.279 1.00 27.79  ? 780  LEU A CB    1 
ATOM   5963  C  CG    . LEU A 1  780  ? 99.780  157.017 150.792 1.00 29.94  ? 780  LEU A CG    1 
ATOM   5964  C  CD1   . LEU A 1  780  ? 98.949  158.181 151.285 1.00 26.58  ? 780  LEU A CD1   1 
ATOM   5965  C  CD2   . LEU A 1  780  ? 99.165  155.694 151.195 1.00 23.00  ? 780  LEU A CD2   1 
ATOM   5966  N  N     . GLU A 1  781  ? 101.807 157.803 146.608 1.00 22.56  ? 781  GLU A N     1 
ATOM   5967  C  CA    . GLU A 1  781  ? 101.722 158.024 145.172 1.00 21.26  ? 781  GLU A CA    1 
ATOM   5968  C  C     . GLU A 1  781  ? 102.388 156.893 144.402 1.00 20.24  ? 781  GLU A C     1 
ATOM   5969  O  O     . GLU A 1  781  ? 103.352 156.283 144.862 1.00 23.82  ? 781  GLU A O     1 
ATOM   5970  C  CB    . GLU A 1  781  ? 102.373 159.352 144.807 1.00 22.41  ? 781  GLU A CB    1 
ATOM   5971  C  CG    . GLU A 1  781  ? 101.815 160.533 145.570 1.00 25.63  ? 781  GLU A CG    1 
ATOM   5972  C  CD    . GLU A 1  781  ? 100.888 161.390 144.724 1.00 31.59  ? 781  GLU A CD    1 
ATOM   5973  O  OE1   . GLU A 1  781  ? 99.657  161.171 144.777 1.00 26.91  ? 781  GLU A OE1   1 
ATOM   5974  O  OE2   . GLU A 1  781  ? 101.388 162.283 144.006 1.00 30.19  ? 781  GLU A OE2   1 
ATOM   5975  N  N     . ALA A 1  782  ? 101.853 156.606 143.214 1.00 14.94  ? 782  ALA A N     1 
ATOM   5976  C  CA    . ALA A 1  782  ? 102.402 155.534 142.392 1.00 10.63  ? 782  ALA A CA    1 
ATOM   5977  C  C     . ALA A 1  782  ? 103.759 155.902 141.818 1.00 14.59  ? 782  ALA A C     1 
ATOM   5978  O  O     . ALA A 1  782  ? 104.563 155.016 141.516 1.00 12.70  ? 782  ALA A O     1 
ATOM   5979  C  CB    . ALA A 1  782  ? 101.436 155.189 141.267 1.00 11.64  ? 782  ALA A CB    1 
ATOM   5980  N  N     . GLN A 1  783  ? 104.031 157.195 141.659 1.00 15.65  ? 783  GLN A N     1 
ATOM   5981  C  CA    . GLN A 1  783  ? 105.320 157.627 141.143 1.00 7.41   ? 783  GLN A CA    1 
ATOM   5982  C  C     . GLN A 1  783  ? 106.459 157.227 142.065 1.00 8.80   ? 783  GLN A C     1 
ATOM   5983  O  O     . GLN A 1  783  ? 107.591 157.056 141.610 1.00 14.62  ? 783  GLN A O     1 
ATOM   5984  C  CB    . GLN A 1  783  ? 105.318 159.138 140.944 1.00 10.43  ? 783  GLN A CB    1 
ATOM   5985  C  CG    . GLN A 1  783  ? 104.534 159.617 139.748 1.00 14.10  ? 783  GLN A CG    1 
ATOM   5986  C  CD    . GLN A 1  783  ? 103.067 159.798 140.037 1.00 16.09  ? 783  GLN A CD    1 
ATOM   5987  O  OE1   . GLN A 1  783  ? 102.598 159.509 141.130 1.00 17.36  ? 783  GLN A OE1   1 
ATOM   5988  N  NE2   . GLN A 1  783  ? 102.336 160.315 139.066 1.00 15.77  ? 783  GLN A NE2   1 
ATOM   5989  N  N     . ALA A 1  784  ? 106.180 157.062 143.356 1.00 9.62   ? 784  ALA A N     1 
ATOM   5990  C  CA    . ALA A 1  784  ? 107.215 156.782 144.339 1.00 6.36   ? 784  ALA A CA    1 
ATOM   5991  C  C     . ALA A 1  784  ? 107.731 155.356 144.280 1.00 6.58   ? 784  ALA A C     1 
ATOM   5992  O  O     . ALA A 1  784  ? 108.755 155.069 144.900 1.00 6.14   ? 784  ALA A O     1 
ATOM   5993  C  CB    . ALA A 1  784  ? 106.693 157.075 145.739 1.00 7.87   ? 784  ALA A CB    1 
ATOM   5994  N  N     . TYR A 1  785  ? 107.067 154.464 143.551 1.00 14.89  ? 785  TYR A N     1 
ATOM   5995  C  CA    . TYR A 1  785  ? 107.437 153.055 143.523 1.00 12.27  ? 785  TYR A CA    1 
ATOM   5996  C  C     . TYR A 1  785  ? 107.766 152.566 142.121 1.00 11.70  ? 785  TYR A C     1 
ATOM   5997  O  O     . TYR A 1  785  ? 107.844 151.359 141.902 1.00 18.89  ? 785  TYR A O     1 
ATOM   5998  C  CB    . TYR A 1  785  ? 106.322 152.204 144.125 1.00 13.00  ? 785  TYR A CB    1 
ATOM   5999  C  CG    . TYR A 1  785  ? 105.992 152.615 145.526 1.00 11.43  ? 785  TYR A CG    1 
ATOM   6000  C  CD1   . TYR A 1  785  ? 104.998 153.540 145.770 1.00 10.52  ? 785  TYR A CD1   1 
ATOM   6001  C  CD2   . TYR A 1  785  ? 106.684 152.100 146.600 1.00 12.14  ? 785  TYR A CD2   1 
ATOM   6002  C  CE1   . TYR A 1  785  ? 104.704 153.937 147.029 1.00 9.82   ? 785  TYR A CE1   1 
ATOM   6003  C  CE2   . TYR A 1  785  ? 106.392 152.493 147.873 1.00 13.09  ? 785  TYR A CE2   1 
ATOM   6004  C  CZ    . TYR A 1  785  ? 105.401 153.412 148.080 1.00 14.78  ? 785  TYR A CZ    1 
ATOM   6005  O  OH    . TYR A 1  785  ? 105.090 153.814 149.355 1.00 26.81  ? 785  TYR A OH    1 
ATOM   6006  N  N     . GLY A 1  786  ? 107.951 153.465 141.171 1.00 7.17   ? 786  GLY A N     1 
ATOM   6007  C  CA    . GLY A 1  786  ? 108.423 153.107 139.859 1.00 4.89   ? 786  GLY A CA    1 
ATOM   6008  C  C     . GLY A 1  786  ? 107.471 153.276 138.705 1.00 8.47   ? 786  GLY A C     1 
ATOM   6009  O  O     . GLY A 1  786  ? 107.667 152.627 137.681 1.00 17.02  ? 786  GLY A O     1 
ATOM   6010  N  N     . PHE A 1  787  ? 106.459 154.123 138.825 1.00 4.33   ? 787  PHE A N     1 
ATOM   6011  C  CA    . PHE A 1  787  ? 105.558 154.404 137.718 1.00 0.74   ? 787  PHE A CA    1 
ATOM   6012  C  C     . PHE A 1  787  ? 106.084 155.609 136.952 1.00 10.05  ? 787  PHE A C     1 
ATOM   6013  O  O     . PHE A 1  787  ? 106.271 156.683 137.527 1.00 15.92  ? 787  PHE A O     1 
ATOM   6014  C  CB    . PHE A 1  787  ? 104.136 154.659 138.208 1.00 6.08   ? 787  PHE A CB    1 
ATOM   6015  C  CG    . PHE A 1  787  ? 103.133 154.749 137.104 1.00 7.78   ? 787  PHE A CG    1 
ATOM   6016  C  CD1   . PHE A 1  787  ? 102.688 153.615 136.462 1.00 10.57  ? 787  PHE A CD1   1 
ATOM   6017  C  CD2   . PHE A 1  787  ? 102.667 155.971 136.680 1.00 9.36   ? 787  PHE A CD2   1 
ATOM   6018  C  CE1   . PHE A 1  787  ? 101.791 153.700 135.440 1.00 9.84   ? 787  PHE A CE1   1 
ATOM   6019  C  CE2   . PHE A 1  787  ? 101.768 156.053 135.655 1.00 7.47   ? 787  PHE A CE2   1 
ATOM   6020  C  CZ    . PHE A 1  787  ? 101.333 154.915 135.034 1.00 6.80   ? 787  PHE A CZ    1 
ATOM   6021  N  N     . ILE A 1  788  ? 106.325 155.428 135.660 1.00 8.51   ? 788  ILE A N     1 
ATOM   6022  C  CA    . ILE A 1  788  ? 106.925 156.451 134.819 1.00 4.82   ? 788  ILE A CA    1 
ATOM   6023  C  C     . ILE A 1  788  ? 105.856 156.951 133.857 1.00 8.05   ? 788  ILE A C     1 
ATOM   6024  O  O     . ILE A 1  788  ? 105.405 156.218 132.977 1.00 9.70   ? 788  ILE A O     1 
ATOM   6025  C  CB    . ILE A 1  788  ? 108.153 155.906 134.082 1.00 4.36   ? 788  ILE A CB    1 
ATOM   6026  C  CG1   . ILE A 1  788  ? 109.169 155.385 135.094 1.00 5.42   ? 788  ILE A CG1   1 
ATOM   6027  C  CG2   . ILE A 1  788  ? 108.778 156.967 133.213 1.00 5.63   ? 788  ILE A CG2   1 
ATOM   6028  C  CD1   . ILE A 1  788  ? 110.277 154.602 134.489 1.00 9.28   ? 788  ILE A CD1   1 
ATOM   6029  N  N     . CYS A 1  789  ? 105.449 158.202 134.019 1.00 8.70   ? 789  CYS A N     1 
ATOM   6030  C  CA    . CYS A 1  789  ? 104.384 158.777 133.213 1.00 7.34   ? 789  CYS A CA    1 
ATOM   6031  C  C     . CYS A 1  789  ? 104.871 159.335 131.887 1.00 17.50  ? 789  CYS A C     1 
ATOM   6032  O  O     . CYS A 1  789  ? 104.045 159.732 131.063 1.00 20.42  ? 789  CYS A O     1 
ATOM   6033  C  CB    . CYS A 1  789  ? 103.681 159.894 133.984 1.00 12.72  ? 789  CYS A CB    1 
ATOM   6034  S  SG    . CYS A 1  789  ? 103.150 159.454 135.645 1.00 41.73  ? 789  CYS A SG    1 
ATOM   6035  N  N     . ASN A 1  790  ? 106.177 159.379 131.666 1.00 17.22  ? 790  ASN A N     1 
ATOM   6036  C  CA    . ASN A 1  790  ? 106.765 159.945 130.466 1.00 7.07   ? 790  ASN A CA    1 
ATOM   6037  C  C     . ASN A 1  790  ? 107.102 158.862 129.455 1.00 2.31   ? 790  ASN A C     1 
ATOM   6038  O  O     . ASN A 1  790  ? 107.269 157.694 129.802 1.00 7.89   ? 790  ASN A O     1 
ATOM   6039  C  CB    . ASN A 1  790  ? 108.032 160.728 130.801 1.00 7.26   ? 790  ASN A CB    1 
ATOM   6040  C  CG    . ASN A 1  790  ? 107.742 162.098 131.321 1.00 11.68  ? 790  ASN A CG    1 
ATOM   6041  O  OD1   . ASN A 1  790  ? 107.010 162.859 130.704 1.00 15.46  ? 790  ASN A OD1   1 
ATOM   6042  N  ND2   . ASN A 1  790  ? 108.312 162.430 132.464 1.00 12.91  ? 790  ASN A ND2   1 
ATOM   6043  N  N     . SER A 1  791  ? 107.189 159.270 128.194 1.00 0.89   ? 791  SER A N     1 
ATOM   6044  C  CA    . SER A 1  791  ? 107.770 158.439 127.158 1.00 0.27   ? 791  SER A CA    1 
ATOM   6045  C  C     . SER A 1  791  ? 109.248 158.767 127.000 1.00 2.43   ? 791  SER A C     1 
ATOM   6046  O  O     . SER A 1  791  ? 109.767 159.711 127.591 1.00 10.37  ? 791  SER A O     1 
ATOM   6047  C  CB    . SER A 1  791  ? 107.045 158.635 125.836 1.00 2.00   ? 791  SER A CB    1 
ATOM   6048  O  OG    . SER A 1  791  ? 107.048 159.984 125.436 1.00 6.36   ? 791  SER A OG    1 
ATOM   6049  N  N     . TYR A 1  792  ? 109.937 157.961 126.203 1.00 5.15   ? 792  TYR A N     1 
ATOM   6050  C  CA    . TYR A 1  792  ? 111.319 158.275 125.875 1.00 2.65   ? 792  TYR A CA    1 
ATOM   6051  C  C     . TYR A 1  792  ? 111.421 159.531 125.025 1.00 4.25   ? 792  TYR A C     1 
ATOM   6052  O  O     . TYR A 1  792  ? 112.342 160.327 125.203 1.00 12.32  ? 792  TYR A O     1 
ATOM   6053  C  CB    . TYR A 1  792  ? 111.972 157.103 125.161 1.00 3.05   ? 792  TYR A CB    1 
ATOM   6054  C  CG    . TYR A 1  792  ? 112.400 156.002 126.079 1.00 2.14   ? 792  TYR A CG    1 
ATOM   6055  C  CD1   . TYR A 1  792  ? 113.224 156.257 127.154 1.00 2.98   ? 792  TYR A CD1   1 
ATOM   6056  C  CD2   . TYR A 1  792  ? 112.001 154.704 125.858 1.00 4.40   ? 792  TYR A CD2   1 
ATOM   6057  C  CE1   . TYR A 1  792  ? 113.622 155.257 127.985 1.00 9.50   ? 792  TYR A CE1   1 
ATOM   6058  C  CE2   . TYR A 1  792  ? 112.392 153.700 126.682 1.00 7.29   ? 792  TYR A CE2   1 
ATOM   6059  C  CZ    . TYR A 1  792  ? 113.203 153.978 127.744 1.00 8.52   ? 792  TYR A CZ    1 
ATOM   6060  O  OH    . TYR A 1  792  ? 113.595 152.960 128.569 1.00 12.85  ? 792  TYR A OH    1 
ATOM   6061  N  N     . ILE A 1  793  ? 110.494 159.728 124.087 1.00 5.09   ? 793  ILE A N     1 
ATOM   6062  C  CA    . ILE A 1  793  ? 110.585 160.882 123.206 1.00 0.11   ? 793  ILE A CA    1 
ATOM   6063  C  C     . ILE A 1  793  ? 110.315 162.175 123.954 1.00 4.36   ? 793  ILE A C     1 
ATOM   6064  O  O     . ILE A 1  793  ? 110.729 163.244 123.505 1.00 12.81  ? 793  ILE A O     1 
ATOM   6065  C  CB    . ILE A 1  793  ? 109.639 160.717 121.996 1.00 2.94   ? 793  ILE A CB    1 
ATOM   6066  C  CG1   . ILE A 1  793  ? 110.249 161.346 120.751 1.00 3.85   ? 793  ILE A CG1   1 
ATOM   6067  C  CG2   . ILE A 1  793  ? 108.335 161.408 122.229 1.00 11.27  ? 793  ILE A CG2   1 
ATOM   6068  C  CD1   . ILE A 1  793  ? 111.523 160.715 120.334 1.00 6.07   ? 793  ILE A CD1   1 
ATOM   6069  N  N     . ALA A 1  794  ? 109.638 162.110 125.098 1.00 3.66   ? 794  ALA A N     1 
ATOM   6070  C  CA    . ALA A 1  794  ? 109.408 163.291 125.917 1.00 0.96   ? 794  ALA A CA    1 
ATOM   6071  C  C     . ALA A 1  794  ? 110.571 163.606 126.836 1.00 7.86   ? 794  ALA A C     1 
ATOM   6072  O  O     . ALA A 1  794  ? 110.845 164.781 127.091 1.00 11.36  ? 794  ALA A O     1 
ATOM   6073  C  CB    . ALA A 1  794  ? 108.146 163.118 126.754 1.00 8.20   ? 794  ALA A CB    1 
ATOM   6074  N  N     . GLY A 1  795  ? 111.258 162.590 127.343 1.00 4.36   ? 795  GLY A N     1 
ATOM   6075  C  CA    . GLY A 1  795  ? 112.355 162.786 128.261 1.00 4.01   ? 795  GLY A CA    1 
ATOM   6076  C  C     . GLY A 1  795  ? 111.952 162.529 129.692 1.00 3.06   ? 795  GLY A C     1 
ATOM   6077  O  O     . GLY A 1  795  ? 110.998 163.128 130.184 1.00 4.38   ? 795  GLY A O     1 
ATOM   6078  N  N     . LEU A 1  796  ? 112.667 161.641 130.371 1.00 8.40   ? 796  LEU A N     1 
ATOM   6079  C  CA    . LEU A 1  796  ? 112.355 161.296 131.745 1.00 2.85   ? 796  LEU A CA    1 
ATOM   6080  C  C     . LEU A 1  796  ? 112.872 162.361 132.705 1.00 0.50   ? 796  LEU A C     1 
ATOM   6081  O  O     . LEU A 1  796  ? 113.762 163.144 132.383 1.00 4.23   ? 796  LEU A O     1 
ATOM   6082  C  CB    . LEU A 1  796  ? 112.956 159.943 132.115 1.00 1.18   ? 796  LEU A CB    1 
ATOM   6083  C  CG    . LEU A 1  796  ? 112.779 158.744 131.190 1.00 8.84   ? 796  LEU A CG    1 
ATOM   6084  C  CD1   . LEU A 1  796  ? 113.094 157.466 131.928 1.00 13.55  ? 796  LEU A CD1   1 
ATOM   6085  C  CD2   . LEU A 1  796  ? 111.400 158.692 130.599 1.00 1.95   ? 796  LEU A CD2   1 
ATOM   6086  N  N     . THR A 1  797  ? 112.287 162.390 133.895 1.00 3.12   ? 797  THR A N     1 
ATOM   6087  C  CA    . THR A 1  797  ? 112.790 163.206 134.985 1.00 2.65   ? 797  THR A CA    1 
ATOM   6088  C  C     . THR A 1  797  ? 113.819 162.397 135.765 1.00 2.58   ? 797  THR A C     1 
ATOM   6089  O  O     . THR A 1  797  ? 114.021 161.210 135.522 1.00 7.77   ? 797  THR A O     1 
ATOM   6090  C  CB    . THR A 1  797  ? 111.650 163.689 135.886 1.00 3.96   ? 797  THR A CB    1 
ATOM   6091  O  OG1   . THR A 1  797  ? 110.987 162.573 136.480 1.00 8.38   ? 797  THR A OG1   1 
ATOM   6092  C  CG2   . THR A 1  797  ? 110.642 164.461 135.090 1.00 14.72  ? 797  THR A CG2   1 
ATOM   6093  N  N     . SER A 1  798  ? 114.494 163.050 136.699 1.00 4.81   ? 798  SER A N     1 
ATOM   6094  C  CA    . SER A 1  798  ? 115.569 162.384 137.433 1.00 2.13   ? 798  SER A CA    1 
ATOM   6095  C  C     . SER A 1  798  ? 115.105 161.169 138.226 1.00 2.13   ? 798  SER A C     1 
ATOM   6096  O  O     . SER A 1  798  ? 115.780 160.131 138.158 1.00 5.01   ? 798  SER A O     1 
ATOM   6097  C  CB    . SER A 1  798  ? 116.276 163.396 138.335 1.00 1.93   ? 798  SER A CB    1 
ATOM   6098  O  OG    . SER A 1  798  ? 116.979 164.328 137.556 1.00 12.51  ? 798  SER A OG    1 
ATOM   6099  N  N     . PRO A 1  799  ? 114.022 161.219 139.012 1.00 4.02   ? 799  PRO A N     1 
ATOM   6100  C  CA    . PRO A 1  799  ? 113.565 159.985 139.663 1.00 1.88   ? 799  PRO A CA    1 
ATOM   6101  C  C     . PRO A 1  799  ? 113.148 158.902 138.687 1.00 4.36   ? 799  PRO A C     1 
ATOM   6102  O  O     . PRO A 1  799  ? 113.421 157.725 138.929 1.00 5.15   ? 799  PRO A O     1 
ATOM   6103  C  CB    . PRO A 1  799  ? 112.390 160.471 140.514 1.00 0.04   ? 799  PRO A CB    1 
ATOM   6104  C  CG    . PRO A 1  799  ? 112.628 161.881 140.701 1.00 15.79  ? 799  PRO A CG    1 
ATOM   6105  C  CD    . PRO A 1  799  ? 113.213 162.363 139.448 1.00 2.47   ? 799  PRO A CD    1 
ATOM   6106  N  N     . GLU A 1  800  ? 112.501 159.274 137.581 1.00 5.99   ? 800  GLU A N     1 
ATOM   6107  C  CA    . GLU A 1  800  ? 112.125 158.300 136.564 1.00 9.16   ? 800  GLU A CA    1 
ATOM   6108  C  C     . GLU A 1  800  ? 113.349 157.652 135.937 1.00 2.07   ? 800  GLU A C     1 
ATOM   6109  O  O     . GLU A 1  800  ? 113.353 156.447 135.677 1.00 3.00   ? 800  GLU A O     1 
ATOM   6110  C  CB    . GLU A 1  800  ? 111.280 158.966 135.487 1.00 1.09   ? 800  GLU A CB    1 
ATOM   6111  C  CG    . GLU A 1  800  ? 109.835 159.133 135.829 1.00 3.36   ? 800  GLU A CG    1 
ATOM   6112  C  CD    . GLU A 1  800  ? 109.167 160.232 135.038 1.00 9.55   ? 800  GLU A CD    1 
ATOM   6113  O  OE1   . GLU A 1  800  ? 109.780 160.741 134.087 1.00 6.63   ? 800  GLU A OE1   1 
ATOM   6114  O  OE2   . GLU A 1  800  ? 108.006 160.563 135.338 1.00 14.12  ? 800  GLU A OE2   1 
ATOM   6115  N  N     . PHE A 1  801  ? 114.394 158.438 135.688 1.00 2.65   ? 801  PHE A N     1 
ATOM   6116  C  CA    . PHE A 1  801  ? 115.620 157.905 135.110 1.00 11.32  ? 801  PHE A CA    1 
ATOM   6117  C  C     . PHE A 1  801  ? 116.296 156.913 136.048 1.00 4.31   ? 801  PHE A C     1 
ATOM   6118  O  O     . PHE A 1  801  ? 116.844 155.902 135.600 1.00 11.84  ? 801  PHE A O     1 
ATOM   6119  C  CB    . PHE A 1  801  ? 116.559 159.060 134.761 1.00 0.31   ? 801  PHE A CB    1 
ATOM   6120  C  CG    . PHE A 1  801  ? 117.757 158.655 133.959 1.00 7.36   ? 801  PHE A CG    1 
ATOM   6121  C  CD1   . PHE A 1  801  ? 117.665 158.455 132.598 1.00 8.65   ? 801  PHE A CD1   1 
ATOM   6122  C  CD2   . PHE A 1  801  ? 118.978 158.476 134.569 1.00 6.97   ? 801  PHE A CD2   1 
ATOM   6123  C  CE1   . PHE A 1  801  ? 118.764 158.078 131.871 1.00 3.78   ? 801  PHE A CE1   1 
ATOM   6124  C  CE2   . PHE A 1  801  ? 120.075 158.095 133.845 1.00 6.76   ? 801  PHE A CE2   1 
ATOM   6125  C  CZ    . PHE A 1  801  ? 119.970 157.900 132.495 1.00 4.55   ? 801  PHE A CZ    1 
ATOM   6126  N  N     . ILE A 1  802  ? 116.286 157.192 137.351 1.00 6.85   ? 802  ILE A N     1 
ATOM   6127  C  CA    . ILE A 1  802  ? 116.916 156.304 138.326 1.00 3.27   ? 802  ILE A CA    1 
ATOM   6128  C  C     . ILE A 1  802  ? 116.185 154.970 138.395 1.00 4.03   ? 802  ILE A C     1 
ATOM   6129  O  O     . ILE A 1  802  ? 116.811 153.909 138.461 1.00 8.60   ? 802  ILE A O     1 
ATOM   6130  C  CB    . ILE A 1  802  ? 116.974 156.986 139.704 1.00 5.92   ? 802  ILE A CB    1 
ATOM   6131  C  CG1   . ILE A 1  802  ? 117.937 158.162 139.686 1.00 0.94   ? 802  ILE A CG1   1 
ATOM   6132  C  CG2   . ILE A 1  802  ? 117.401 156.012 140.765 1.00 7.04   ? 802  ILE A CG2   1 
ATOM   6133  C  CD1   . ILE A 1  802  ? 117.684 159.161 140.761 1.00 1.16   ? 802  ILE A CD1   1 
ATOM   6134  N  N     . PHE A 1  803  ? 114.853 155.001 138.391 1.00 7.05   ? 803  PHE A N     1 
ATOM   6135  C  CA    . PHE A 1  803  ? 114.078 153.768 138.399 1.00 4.02   ? 803  PHE A CA    1 
ATOM   6136  C  C     . PHE A 1  803  ? 114.360 152.935 137.161 1.00 12.58  ? 803  PHE A C     1 
ATOM   6137  O  O     . PHE A 1  803  ? 114.493 151.711 137.247 1.00 17.00  ? 803  PHE A O     1 
ATOM   6138  C  CB    . PHE A 1  803  ? 112.588 154.085 138.496 1.00 0.99   ? 803  PHE A CB    1 
ATOM   6139  C  CG    . PHE A 1  803  ? 112.161 154.583 139.840 1.00 8.21   ? 803  PHE A CG    1 
ATOM   6140  C  CD1   . PHE A 1  803  ? 112.716 154.070 140.988 1.00 9.16   ? 803  PHE A CD1   1 
ATOM   6141  C  CD2   . PHE A 1  803  ? 111.206 155.566 139.955 1.00 5.10   ? 803  PHE A CD2   1 
ATOM   6142  C  CE1   . PHE A 1  803  ? 112.325 154.528 142.216 1.00 3.14   ? 803  PHE A CE1   1 
ATOM   6143  C  CE2   . PHE A 1  803  ? 110.819 156.022 141.184 1.00 7.16   ? 803  PHE A CE2   1 
ATOM   6144  C  CZ    . PHE A 1  803  ? 111.376 155.501 142.311 1.00 3.91   ? 803  PHE A CZ    1 
ATOM   6145  N  N     . GLY A 1  804  ? 114.449 153.578 136.000 1.00 7.70   ? 804  GLY A N     1 
ATOM   6146  C  CA    . GLY A 1  804  ? 114.799 152.863 134.788 1.00 1.93   ? 804  GLY A CA    1 
ATOM   6147  C  C     . GLY A 1  804  ? 116.218 152.339 134.784 1.00 9.76   ? 804  GLY A C     1 
ATOM   6148  O  O     . GLY A 1  804  ? 116.506 151.330 134.147 1.00 20.07  ? 804  GLY A O     1 
ATOM   6149  N  N     . GLU A 1  805  ? 117.131 153.034 135.458 1.00 12.30  ? 805  GLU A N     1 
ATOM   6150  C  CA    . GLU A 1  805  ? 118.508 152.564 135.552 1.00 9.17   ? 805  GLU A CA    1 
ATOM   6151  C  C     . GLU A 1  805  ? 118.610 151.336 136.445 1.00 15.54  ? 805  GLU A C     1 
ATOM   6152  O  O     . GLU A 1  805  ? 119.425 150.445 136.191 1.00 20.06  ? 805  GLU A O     1 
ATOM   6153  C  CB    . GLU A 1  805  ? 119.409 153.679 136.079 1.00 11.05  ? 805  GLU A CB    1 
ATOM   6154  C  CG    . GLU A 1  805  ? 120.330 154.339 135.061 1.00 10.77  ? 805  GLU A CG    1 
ATOM   6155  C  CD    . GLU A 1  805  ? 121.262 153.377 134.351 1.00 23.56  ? 805  GLU A CD    1 
ATOM   6156  O  OE1   . GLU A 1  805  ? 121.580 152.309 134.903 1.00 27.31  ? 805  GLU A OE1   1 
ATOM   6157  O  OE2   . GLU A 1  805  ? 121.712 153.707 133.239 1.00 22.50  ? 805  GLU A OE2   1 
ATOM   6158  N  N     . MET A 1  806  ? 117.809 151.282 137.515 1.00 17.86  ? 806  MET A N     1 
ATOM   6159  C  CA    . MET A 1  806  ? 117.769 150.082 138.344 1.00 14.04  ? 806  MET A CA    1 
ATOM   6160  C  C     . MET A 1  806  ? 117.263 148.893 137.553 1.00 18.07  ? 806  MET A C     1 
ATOM   6161  O  O     . MET A 1  806  ? 117.787 147.783 137.683 1.00 19.50  ? 806  MET A O     1 
ATOM   6162  C  CB    . MET A 1  806  ? 116.887 150.289 139.573 1.00 11.97  ? 806  MET A CB    1 
ATOM   6163  C  CG    . MET A 1  806  ? 117.379 151.298 140.569 1.00 15.56  ? 806  MET A CG    1 
ATOM   6164  S  SD    . MET A 1  806  ? 116.052 151.936 141.590 1.00 17.39  ? 806  MET A SD    1 
ATOM   6165  C  CE    . MET A 1  806  ? 116.991 152.865 142.777 1.00 14.53  ? 806  MET A CE    1 
ATOM   6166  N  N     . ASN A 1  807  ? 116.229 149.103 136.743 1.00 22.29  ? 807  ASN A N     1 
ATOM   6167  C  CA    . ASN A 1  807  ? 115.717 148.033 135.901 1.00 18.85  ? 807  ASN A CA    1 
ATOM   6168  C  C     . ASN A 1  807  ? 116.779 147.551 134.923 1.00 21.57  ? 807  ASN A C     1 
ATOM   6169  O  O     . ASN A 1  807  ? 116.973 146.344 134.752 1.00 25.90  ? 807  ASN A O     1 
ATOM   6170  C  CB    . ASN A 1  807  ? 114.476 148.525 135.165 1.00 15.58  ? 807  ASN A CB    1 
ATOM   6171  C  CG    . ASN A 1  807  ? 113.804 147.443 134.372 1.00 24.15  ? 807  ASN A CG    1 
ATOM   6172  O  OD1   . ASN A 1  807  ? 113.430 146.407 134.908 1.00 26.63  ? 807  ASN A OD1   1 
ATOM   6173  N  ND2   . ASN A 1  807  ? 113.656 147.669 133.081 1.00 24.62  ? 807  ASN A ND2   1 
ATOM   6174  N  N     . GLY A 1  808  ? 117.489 148.481 134.286 1.00 22.02  ? 808  GLY A N     1 
ATOM   6175  C  CA    . GLY A 1  808  ? 118.487 148.100 133.304 1.00 19.05  ? 808  GLY A CA    1 
ATOM   6176  C  C     . GLY A 1  808  ? 119.686 147.389 133.900 1.00 22.42  ? 808  GLY A C     1 
ATOM   6177  O  O     . GLY A 1  808  ? 120.227 146.464 133.294 1.00 25.77  ? 808  GLY A O     1 
ATOM   6178  N  N     . ARG A 1  809  ? 120.134 147.825 135.081 1.00 29.32  ? 809  ARG A N     1 
ATOM   6179  C  CA    . ARG A 1  809  ? 121.266 147.173 135.731 1.00 29.95  ? 809  ARG A CA    1 
ATOM   6180  C  C     . ARG A 1  809  ? 120.956 145.727 136.078 1.00 31.34  ? 809  ARG A C     1 
ATOM   6181  O  O     . ARG A 1  809  ? 121.830 144.863 135.965 1.00 35.74  ? 809  ARG A O     1 
ATOM   6182  C  CB    . ARG A 1  809  ? 121.670 147.935 136.989 1.00 27.92  ? 809  ARG A CB    1 
ATOM   6183  C  CG    . ARG A 1  809  ? 122.856 147.326 137.723 1.00 27.89  ? 809  ARG A CG    1 
ATOM   6184  C  CD    . ARG A 1  809  ? 124.134 147.339 136.901 1.00 31.55  ? 809  ARG A CD    1 
ATOM   6185  N  NE    . ARG A 1  809  ? 124.545 148.697 136.575 1.00 34.93  ? 809  ARG A NE    1 
ATOM   6186  C  CZ    . ARG A 1  809  ? 125.232 149.481 137.392 1.00 35.59  ? 809  ARG A CZ    1 
ATOM   6187  N  NH1   . ARG A 1  809  ? 125.634 149.057 138.576 1.00 35.11  ? 809  ARG A NH1   1 
ATOM   6188  N  NH2   . ARG A 1  809  ? 125.519 150.722 137.015 1.00 33.78  ? 809  ARG A NH2   1 
ATOM   6189  N  N     . PHE A 1  810  ? 119.722 145.445 136.490 1.00 31.44  ? 810  PHE A N     1 
ATOM   6190  C  CA    . PHE A 1  810  ? 119.324 144.074 136.776 1.00 30.86  ? 810  PHE A CA    1 
ATOM   6191  C  C     . PHE A 1  810  ? 119.525 143.166 135.572 1.00 32.79  ? 810  PHE A C     1 
ATOM   6192  O  O     . PHE A 1  810  ? 120.031 142.047 135.709 1.00 33.49  ? 810  PHE A O     1 
ATOM   6193  C  CB    . PHE A 1  810  ? 117.867 144.045 137.219 1.00 31.11  ? 810  PHE A CB    1 
ATOM   6194  C  CG    . PHE A 1  810  ? 117.521 142.864 138.051 1.00 34.53  ? 810  PHE A CG    1 
ATOM   6195  C  CD1   . PHE A 1  810  ? 116.904 141.771 137.481 1.00 33.42  ? 810  PHE A CD1   1 
ATOM   6196  C  CD2   . PHE A 1  810  ? 117.830 142.829 139.393 1.00 33.06  ? 810  PHE A CD2   1 
ATOM   6197  C  CE1   . PHE A 1  810  ? 116.590 140.671 138.234 1.00 32.97  ? 810  PHE A CE1   1 
ATOM   6198  C  CE2   . PHE A 1  810  ? 117.520 141.730 140.150 1.00 35.42  ? 810  PHE A CE2   1 
ATOM   6199  C  CZ    . PHE A 1  810  ? 116.899 140.648 139.572 1.00 33.86  ? 810  PHE A CZ    1 
ATOM   6200  N  N     . ASP A 1  811  ? 119.135 143.626 134.386 1.00 34.86  ? 811  ASP A N     1 
ATOM   6201  C  CA    . ASP A 1  811  ? 119.233 142.783 133.203 1.00 35.26  ? 811  ASP A CA    1 
ATOM   6202  C  C     . ASP A 1  811  ? 120.684 142.521 132.813 1.00 36.54  ? 811  ASP A C     1 
ATOM   6203  O  O     . ASP A 1  811  ? 121.029 141.401 132.427 1.00 39.09  ? 811  ASP A O     1 
ATOM   6204  C  CB    . ASP A 1  811  ? 118.460 143.415 132.050 1.00 33.45  ? 811  ASP A CB    1 
ATOM   6205  C  CG    . ASP A 1  811  ? 117.015 143.706 132.408 1.00 39.47  ? 811  ASP A CG    1 
ATOM   6206  O  OD1   . ASP A 1  811  ? 116.506 143.117 133.383 1.00 36.90  ? 811  ASP A OD1   1 
ATOM   6207  O  OD2   . ASP A 1  811  ? 116.383 144.522 131.709 1.00 41.24  ? 811  ASP A OD2   1 
ATOM   6208  N  N     . LEU A 1  812  ? 121.549 143.533 132.908 1.00 31.95  ? 812  LEU A N     1 
ATOM   6209  C  CA    . LEU A 1  812  ? 122.962 143.327 132.597 1.00 33.58  ? 812  LEU A CA    1 
ATOM   6210  C  C     . LEU A 1  812  ? 123.604 142.334 133.556 1.00 37.28  ? 812  LEU A C     1 
ATOM   6211  O  O     . LEU A 1  812  ? 124.552 141.632 133.192 1.00 36.96  ? 812  LEU A O     1 
ATOM   6212  C  CB    . LEU A 1  812  ? 123.718 144.654 132.644 1.00 33.70  ? 812  LEU A CB    1 
ATOM   6213  C  CG    . LEU A 1  812  ? 123.473 145.694 131.555 1.00 37.93  ? 812  LEU A CG    1 
ATOM   6214  C  CD1   . LEU A 1  812  ? 124.477 146.817 131.675 1.00 33.13  ? 812  LEU A CD1   1 
ATOM   6215  C  CD2   . LEU A 1  812  ? 123.543 145.063 130.178 1.00 39.45  ? 812  LEU A CD2   1 
ATOM   6216  N  N     . ILE A 1  813  ? 123.131 142.294 134.801 1.00 36.62  ? 813  ILE A N     1 
ATOM   6217  C  CA    . ILE A 1  813  ? 123.686 141.363 135.777 1.00 33.22  ? 813  ILE A CA    1 
ATOM   6218  C  C     . ILE A 1  813  ? 123.231 139.936 135.486 1.00 39.23  ? 813  ILE A C     1 
ATOM   6219  O  O     . ILE A 1  813  ? 124.029 138.996 135.555 1.00 40.71  ? 813  ILE A O     1 
ATOM   6220  C  CB    . ILE A 1  813  ? 123.318 141.813 137.203 1.00 31.89  ? 813  ILE A CB    1 
ATOM   6221  C  CG1   . ILE A 1  813  ? 124.103 143.063 137.577 1.00 35.02  ? 813  ILE A CG1   1 
ATOM   6222  C  CG2   . ILE A 1  813  ? 123.583 140.720 138.217 1.00 33.51  ? 813  ILE A CG2   1 
ATOM   6223  C  CD1   . ILE A 1  813  ? 123.516 143.810 138.741 1.00 36.82  ? 813  ILE A CD1   1 
ATOM   6224  N  N     . ASN A 1  814  ? 121.947 139.747 135.160 1.00 36.32  ? 814  ASN A N     1 
ATOM   6225  C  CA    . ASN A 1  814  ? 121.455 138.406 134.853 1.00 33.80  ? 814  ASN A CA    1 
ATOM   6226  C  C     . ASN A 1  814  ? 122.148 137.838 133.624 1.00 37.26  ? 814  ASN A C     1 
ATOM   6227  O  O     . ASN A 1  814  ? 122.397 136.631 133.546 1.00 36.94  ? 814  ASN A O     1 
ATOM   6228  C  CB    . ASN A 1  814  ? 119.942 138.416 134.635 1.00 35.22  ? 814  ASN A CB    1 
ATOM   6229  C  CG    . ASN A 1  814  ? 119.166 138.597 135.913 1.00 37.94  ? 814  ASN A CG    1 
ATOM   6230  O  OD1   . ASN A 1  814  ? 119.632 138.244 136.991 1.00 38.56  ? 814  ASN A OD1   1 
ATOM   6231  N  ND2   . ASN A 1  814  ? 117.954 139.119 135.796 1.00 36.12  ? 814  ASN A ND2   1 
ATOM   6232  N  N     . LYS A 1  815  ? 122.455 138.692 132.647 1.00 35.45  ? 815  LYS A N     1 
ATOM   6233  C  CA    . LYS A 1  815  ? 123.181 138.247 131.467 1.00 36.69  ? 815  LYS A CA    1 
ATOM   6234  C  C     . LYS A 1  815  ? 124.547 137.673 131.810 1.00 40.91  ? 815  LYS A C     1 
ATOM   6235  O  O     . LYS A 1  815  ? 124.941 136.659 131.226 1.00 42.44  ? 815  LYS A O     1 
ATOM   6236  C  CB    . LYS A 1  815  ? 123.359 139.403 130.487 1.00 38.29  ? 815  LYS A CB    1 
ATOM   6237  C  CG    . LYS A 1  815  ? 122.096 139.818 129.766 1.00 41.41  ? 815  LYS A CG    1 
ATOM   6238  C  CD    . LYS A 1  815  ? 122.304 141.124 129.012 1.00 39.45  ? 815  LYS A CD    1 
ATOM   6239  C  CE    . LYS A 1  815  ? 121.000 141.633 128.419 1.00 41.31  ? 815  LYS A CE    1 
ATOM   6240  N  NZ    . LYS A 1  815  ? 119.977 141.927 129.463 1.00 39.24  ? 815  LYS A NZ    1 
ATOM   6241  N  N     . ALA A 1  816  ? 125.275 138.296 132.738 1.00 38.67  ? 816  ALA A N     1 
ATOM   6242  C  CA    . ALA A 1  816  ? 126.609 137.822 133.081 1.00 39.43  ? 816  ALA A CA    1 
ATOM   6243  C  C     . ALA A 1  816  ? 126.573 136.459 133.748 1.00 37.60  ? 816  ALA A C     1 
ATOM   6244  O  O     . ALA A 1  816  ? 127.509 135.671 133.586 1.00 38.08  ? 816  ALA A O     1 
ATOM   6245  C  CB    . ALA A 1  816  ? 127.311 138.830 133.989 1.00 36.07  ? 816  ALA A CB    1 
ATOM   6246  N  N     . LEU A 1  817  ? 125.514 136.165 134.496 1.00 33.91  ? 817  LEU A N     1 
ATOM   6247  C  CA    . LEU A 1  817  ? 125.388 134.881 135.167 1.00 35.63  ? 817  LEU A CA    1 
ATOM   6248  C  C     . LEU A 1  817  ? 125.174 133.731 134.197 1.00 40.38  ? 817  LEU A C     1 
ATOM   6249  O  O     . LEU A 1  817  ? 125.376 132.574 134.578 1.00 38.07  ? 817  LEU A O     1 
ATOM   6250  C  CB    . LEU A 1  817  ? 124.230 134.935 136.159 1.00 36.73  ? 817  LEU A CB    1 
ATOM   6251  C  CG    . LEU A 1  817  ? 124.339 136.103 137.134 1.00 37.26  ? 817  LEU A CG    1 
ATOM   6252  C  CD1   . LEU A 1  817  ? 123.115 136.163 138.029 1.00 35.81  ? 817  LEU A CD1   1 
ATOM   6253  C  CD2   . LEU A 1  817  ? 125.616 135.995 137.942 1.00 35.08  ? 817  LEU A CD2   1 
ATOM   6254  N  N     . SER A 1  818  ? 124.770 134.025 132.961 1.00 39.92  ? 818  SER A N     1 
ATOM   6255  C  CA    . SER A 1  818  ? 124.575 132.983 131.964 1.00 39.93  ? 818  SER A CA    1 
ATOM   6256  C  C     . SER A 1  818  ? 125.882 132.258 131.673 1.00 38.62  ? 818  SER A C     1 
ATOM   6257  O  O     . SER A 1  818  ? 125.904 131.037 131.486 1.00 38.52  ? 818  SER A O     1 
ATOM   6258  C  CB    . SER A 1  818  ? 123.990 133.597 130.691 1.00 42.12  ? 818  SER A CB    1 
ATOM   6259  O  OG    . SER A 1  818  ? 124.295 132.821 129.547 1.00 43.44  ? 818  SER A OG    1 
ATOM   6260  N  N     . THR A 1  819  ? 126.988 132.999 131.635 1.00 33.98  ? 819  THR A N     1 
ATOM   6261  C  CA    . THR A 1  819  ? 128.279 132.381 131.353 1.00 38.92  ? 819  THR A CA    1 
ATOM   6262  C  C     . THR A 1  819  ? 128.675 131.401 132.451 1.00 38.98  ? 819  THR A C     1 
ATOM   6263  O  O     . THR A 1  819  ? 129.157 130.297 132.169 1.00 42.15  ? 819  THR A O     1 
ATOM   6264  C  CB    . THR A 1  819  ? 129.352 133.456 131.197 1.00 41.82  ? 819  THR A CB    1 
ATOM   6265  O  OG1   . THR A 1  819  ? 128.967 134.380 130.174 1.00 43.55  ? 819  THR A OG1   1 
ATOM   6266  C  CG2   . THR A 1  819  ? 130.672 132.815 130.814 1.00 38.82  ? 819  THR A CG2   1 
ATOM   6267  N  N     . SER A 1  820  ? 128.472 131.786 133.712 1.00 38.36  ? 820  SER A N     1 
ATOM   6268  C  CA    . SER A 1  820  ? 129.014 131.013 134.825 1.00 39.85  ? 820  SER A CA    1 
ATOM   6269  C  C     . SER A 1  820  ? 128.062 129.906 135.261 1.00 37.64  ? 820  SER A C     1 
ATOM   6270  O  O     . SER A 1  820  ? 128.495 128.797 135.592 1.00 38.30  ? 820  SER A O     1 
ATOM   6271  C  CB    . SER A 1  820  ? 129.326 131.940 135.997 1.00 39.36  ? 820  SER A CB    1 
ATOM   6272  O  OG    . SER A 1  820  ? 128.141 132.498 136.538 1.00 40.71  ? 820  SER A OG    1 
ATOM   6273  N  N     . SER A 1  821  ? 126.761 130.192 135.293 1.00 35.87  ? 821  SER A N     1 
ATOM   6274  C  CA    . SER A 1  821  ? 125.816 129.236 135.860 1.00 37.49  ? 821  SER A CA    1 
ATOM   6275  C  C     . SER A 1  821  ? 125.661 128.007 134.976 1.00 40.63  ? 821  SER A C     1 
ATOM   6276  O  O     . SER A 1  821  ? 125.675 126.873 135.467 1.00 42.55  ? 821  SER A O     1 
ATOM   6277  C  CB    . SER A 1  821  ? 124.462 129.903 136.083 1.00 38.66  ? 821  SER A CB    1 
ATOM   6278  O  OG    . SER A 1  821  ? 123.532 128.965 136.590 1.00 37.08  ? 821  SER A OG    1 
ATOM   6279  N  N     . THR A 1  822  ? 125.489 128.209 133.669 1.00 36.19  ? 822  THR A N     1 
ATOM   6280  C  CA    . THR A 1  822  ? 125.214 127.085 132.784 1.00 34.85  ? 822  THR A CA    1 
ATOM   6281  C  C     . THR A 1  822  ? 126.481 126.431 132.251 1.00 33.77  ? 822  THR A C     1 
ATOM   6282  O  O     . THR A 1  822  ? 126.416 125.301 131.763 1.00 32.67  ? 822  THR A O     1 
ATOM   6283  C  CB    . THR A 1  822  ? 124.338 127.531 131.617 1.00 35.52  ? 822  THR A CB    1 
ATOM   6284  O  OG1   . THR A 1  822  ? 125.061 128.459 130.804 1.00 39.09  ? 822  THR A OG1   1 
ATOM   6285  C  CG2   . THR A 1  822  ? 123.080 128.199 132.135 1.00 33.40  ? 822  THR A CG2   1 
ATOM   6286  N  N     . GLY A 1  823  ? 127.620 127.119 132.304 1.00 28.88  ? 823  GLY A N     1 
ATOM   6287  C  CA    . GLY A 1  823  ? 128.856 126.513 131.841 1.00 28.24  ? 823  GLY A CA    1 
ATOM   6288  C  C     . GLY A 1  823  ? 129.319 125.378 132.730 1.00 28.64  ? 823  GLY A C     1 
ATOM   6289  O  O     . GLY A 1  823  ? 129.867 124.385 132.249 1.00 28.90  ? 823  GLY A O     1 
ATOM   6290  N  N     . TYR A 1  824  ? 129.134 125.524 134.042 1.00 34.50  ? 824  TYR A N     1 
ATOM   6291  C  CA    . TYR A 1  824  ? 129.522 124.473 134.975 1.00 32.36  ? 824  TYR A CA    1 
ATOM   6292  C  C     . TYR A 1  824  ? 128.578 123.284 134.885 1.00 28.60  ? 824  TYR A C     1 
ATOM   6293  O  O     . TYR A 1  824  ? 129.013 122.131 134.975 1.00 28.38  ? 824  TYR A O     1 
ATOM   6294  C  CB    . TYR A 1  824  ? 129.562 125.033 136.397 1.00 33.63  ? 824  TYR A CB    1 
ATOM   6295  C  CG    . TYR A 1  824  ? 129.969 124.025 137.454 1.00 33.43  ? 824  TYR A CG    1 
ATOM   6296  C  CD1   . TYR A 1  824  ? 131.215 123.417 137.418 1.00 32.01  ? 824  TYR A CD1   1 
ATOM   6297  C  CD2   . TYR A 1  824  ? 129.111 123.695 138.492 1.00 32.55  ? 824  TYR A CD2   1 
ATOM   6298  C  CE1   . TYR A 1  824  ? 131.589 122.501 138.376 1.00 34.91  ? 824  TYR A CE1   1 
ATOM   6299  C  CE2   . TYR A 1  824  ? 129.476 122.785 139.457 1.00 33.38  ? 824  TYR A CE2   1 
ATOM   6300  C  CZ    . TYR A 1  824  ? 130.717 122.189 139.394 1.00 35.47  ? 824  TYR A CZ    1 
ATOM   6301  O  OH    . TYR A 1  824  ? 131.084 121.277 140.358 1.00 33.21  ? 824  TYR A OH    1 
ATOM   6302  N  N     . ALA A 1  825  ? 127.284 123.546 134.706 1.00 27.14  ? 825  ALA A N     1 
ATOM   6303  C  CA    . ALA A 1  825  ? 126.324 122.466 134.527 1.00 24.69  ? 825  ALA A CA    1 
ATOM   6304  C  C     . ALA A 1  825  ? 126.481 121.797 133.171 1.00 27.40  ? 825  ALA A C     1 
ATOM   6305  O  O     . ALA A 1  825  ? 126.087 120.639 133.007 1.00 21.70  ? 825  ALA A O     1 
ATOM   6306  C  CB    . ALA A 1  825  ? 124.902 122.998 134.694 1.00 21.16  ? 825  ALA A CB    1 
ATOM   6307  N  N     . ASN A 1  826  ? 127.031 122.511 132.190 1.00 22.01  ? 826  ASN A N     1 
ATOM   6308  C  CA    . ASN A 1  826  ? 127.256 121.930 130.874 1.00 12.42  ? 826  ASN A CA    1 
ATOM   6309  C  C     . ASN A 1  826  ? 128.357 120.882 130.904 1.00 8.26   ? 826  ASN A C     1 
ATOM   6310  O  O     . ASN A 1  826  ? 128.273 119.872 130.203 1.00 14.82  ? 826  ASN A O     1 
ATOM   6311  C  CB    . ASN A 1  826  ? 127.586 123.030 129.870 1.00 14.36  ? 826  ASN A CB    1 
ATOM   6312  C  CG    . ASN A 1  826  ? 127.614 122.531 128.442 1.00 21.61  ? 826  ASN A CG    1 
ATOM   6313  O  OD1   . ASN A 1  826  ? 126.816 121.686 128.039 1.00 16.46  ? 826  ASN A OD1   1 
ATOM   6314  N  ND2   . ASN A 1  826  ? 128.544 123.058 127.665 1.00 22.05  ? 826  ASN A ND2   1 
ATOM   6315  N  N     . ARG A 1  827  ? 129.400 121.100 131.698 1.00 2.88   ? 827  ARG A N     1 
ATOM   6316  C  CA    . ARG A 1  827  ? 130.514 120.163 131.697 1.00 6.01   ? 827  ARG A CA    1 
ATOM   6317  C  C     . ARG A 1  827  ? 130.169 118.869 132.414 1.00 5.94   ? 827  ARG A C     1 
ATOM   6318  O  O     . ARG A 1  827  ? 130.691 117.811 132.059 1.00 9.00   ? 827  ARG A O     1 
ATOM   6319  C  CB    . ARG A 1  827  ? 131.746 120.805 132.323 1.00 10.99  ? 827  ARG A CB    1 
ATOM   6320  C  CG    . ARG A 1  827  ? 133.001 120.025 132.067 1.00 3.45   ? 827  ARG A CG    1 
ATOM   6321  C  CD    . ARG A 1  827  ? 134.239 120.746 132.520 1.00 3.41   ? 827  ARG A CD    1 
ATOM   6322  N  NE    . ARG A 1  827  ? 135.430 119.979 132.183 1.00 10.59  ? 827  ARG A NE    1 
ATOM   6323  C  CZ    . ARG A 1  827  ? 135.958 119.033 132.945 1.00 10.65  ? 827  ARG A CZ    1 
ATOM   6324  N  NH1   . ARG A 1  827  ? 135.471 118.753 134.137 1.00 4.97   ? 827  ARG A NH1   1 
ATOM   6325  N  NH2   . ARG A 1  827  ? 137.006 118.355 132.498 1.00 4.32   ? 827  ARG A NH2   1 
ATOM   6326  N  N     . LYS A 1  828  ? 129.317 118.931 133.430 1.00 12.78  ? 828  LYS A N     1 
ATOM   6327  C  CA    . LYS A 1  828  ? 128.903 117.728 134.133 1.00 8.93   ? 828  LYS A CA    1 
ATOM   6328  C  C     . LYS A 1  828  ? 127.865 116.942 133.354 1.00 2.82   ? 828  LYS A C     1 
ATOM   6329  O  O     . LYS A 1  828  ? 127.810 115.719 133.468 1.00 8.34   ? 828  LYS A O     1 
ATOM   6330  C  CB    . LYS A 1  828  ? 128.381 118.098 135.514 1.00 11.25  ? 828  LYS A CB    1 
ATOM   6331  C  CG    . LYS A 1  828  ? 129.464 118.612 136.424 1.00 13.29  ? 828  LYS A CG    1 
ATOM   6332  C  CD    . LYS A 1  828  ? 128.892 119.409 137.561 1.00 20.06  ? 828  LYS A CD    1 
ATOM   6333  C  CE    . LYS A 1  828  ? 128.545 118.527 138.730 1.00 21.84  ? 828  LYS A CE    1 
ATOM   6334  N  NZ    . LYS A 1  828  ? 128.208 119.336 139.925 1.00 19.72  ? 828  LYS A NZ    1 
ATOM   6335  N  N     . ALA A 1  829  ? 127.032 117.621 132.573 1.00 8.32   ? 829  ALA A N     1 
ATOM   6336  C  CA    . ALA A 1  829  ? 126.154 116.920 131.648 1.00 3.93   ? 829  ALA A CA    1 
ATOM   6337  C  C     . ALA A 1  829  ? 126.952 116.211 130.566 1.00 4.56   ? 829  ALA A C     1 
ATOM   6338  O  O     . ALA A 1  829  ? 126.619 115.091 130.178 1.00 8.12   ? 829  ALA A O     1 
ATOM   6339  C  CB    . ALA A 1  829  ? 125.168 117.900 131.024 1.00 0.97   ? 829  ALA A CB    1 
ATOM   6340  N  N     . ILE A 1  830  ? 128.006 116.850 130.064 1.00 3.56   ? 830  ILE A N     1 
ATOM   6341  C  CA    . ILE A 1  830  ? 128.764 116.273 128.963 1.00 13.19  ? 830  ILE A CA    1 
ATOM   6342  C  C     . ILE A 1  830  ? 129.514 115.031 129.412 1.00 0.48   ? 830  ILE A C     1 
ATOM   6343  O  O     . ILE A 1  830  ? 129.568 114.035 128.693 1.00 7.04   ? 830  ILE A O     1 
ATOM   6344  C  CB    . ILE A 1  830  ? 129.700 117.326 128.340 1.00 1.46   ? 830  ILE A CB    1 
ATOM   6345  C  CG1   . ILE A 1  830  ? 128.889 118.210 127.386 1.00 1.41   ? 830  ILE A CG1   1 
ATOM   6346  C  CG2   . ILE A 1  830  ? 130.881 116.675 127.665 1.00 11.37  ? 830  ILE A CG2   1 
ATOM   6347  C  CD1   . ILE A 1  830  ? 129.321 118.210 125.974 1.00 0.39   ? 830  ILE A CD1   1 
ATOM   6348  N  N     . PHE A 1  831  ? 130.089 115.055 130.606 1.00 2.26   ? 831  PHE A N     1 
ATOM   6349  C  CA    . PHE A 1  831  ? 130.845 113.904 131.074 1.00 1.72   ? 831  PHE A CA    1 
ATOM   6350  C  C     . PHE A 1  831  ? 129.957 112.742 131.485 1.00 6.54   ? 831  PHE A C     1 
ATOM   6351  O  O     . PHE A 1  831  ? 130.371 111.589 131.347 1.00 3.99   ? 831  PHE A O     1 
ATOM   6352  C  CB    . PHE A 1  831  ? 131.758 114.321 132.217 1.00 15.32  ? 831  PHE A CB    1 
ATOM   6353  C  CG    . PHE A 1  831  ? 133.108 114.747 131.755 1.00 1.64   ? 831  PHE A CG    1 
ATOM   6354  C  CD1   . PHE A 1  831  ? 133.338 116.042 131.363 1.00 1.77   ? 831  PHE A CD1   1 
ATOM   6355  C  CD2   . PHE A 1  831  ? 134.134 113.842 131.674 1.00 4.25   ? 831  PHE A CD2   1 
ATOM   6356  C  CE1   . PHE A 1  831  ? 134.558 116.417 130.917 1.00 2.48   ? 831  PHE A CE1   1 
ATOM   6357  C  CE2   . PHE A 1  831  ? 135.352 114.220 131.233 1.00 5.42   ? 831  PHE A CE2   1 
ATOM   6358  C  CZ    . PHE A 1  831  ? 135.569 115.507 130.858 1.00 6.16   ? 831  PHE A CZ    1 
ATOM   6359  N  N     . GLY A 1  832  ? 128.742 113.013 131.962 1.00 3.78   ? 832  GLY A N     1 
ATOM   6360  C  CA    . GLY A 1  832  ? 127.825 111.946 132.302 1.00 1.35   ? 832  GLY A CA    1 
ATOM   6361  C  C     . GLY A 1  832  ? 127.190 111.261 131.120 1.00 12.70  ? 832  GLY A C     1 
ATOM   6362  O  O     . GLY A 1  832  ? 126.761 110.115 131.244 1.00 4.31   ? 832  GLY A O     1 
ATOM   6363  N  N     . LEU A 1  833  ? 127.152 111.920 129.967 1.00 4.66   ? 833  LEU A N     1 
ATOM   6364  C  CA    . LEU A 1  833  ? 126.407 111.437 128.819 1.00 4.95   ? 833  LEU A CA    1 
ATOM   6365  C  C     . LEU A 1  833  ? 127.265 111.073 127.619 1.00 9.92   ? 833  LEU A C     1 
ATOM   6366  O  O     . LEU A 1  833  ? 126.753 110.455 126.689 1.00 2.41   ? 833  LEU A O     1 
ATOM   6367  C  CB    . LEU A 1  833  ? 125.385 112.496 128.387 1.00 8.90   ? 833  LEU A CB    1 
ATOM   6368  C  CG    . LEU A 1  833  ? 124.025 112.494 129.077 1.00 1.54   ? 833  LEU A CG    1 
ATOM   6369  C  CD1   . LEU A 1  833  ? 123.440 113.864 129.033 1.00 9.18   ? 833  LEU A CD1   1 
ATOM   6370  C  CD2   . LEU A 1  833  ? 123.107 111.527 128.400 1.00 0.58   ? 833  LEU A CD2   1 
ATOM   6371  N  N     . GLN A 1  834  ? 128.552 111.402 127.630 1.00 8.18   ? 834  GLN A N     1 
ATOM   6372  C  CA    . GLN A 1  834  ? 129.368 111.303 126.430 1.00 15.12  ? 834  GLN A CA    1 
ATOM   6373  C  C     . GLN A 1  834  ? 129.664 109.874 126.000 1.00 4.36   ? 834  GLN A C     1 
ATOM   6374  O  O     . GLN A 1  834  ? 130.060 109.664 124.854 1.00 6.49   ? 834  GLN A O     1 
ATOM   6375  C  CB    . GLN A 1  834  ? 130.680 112.032 126.635 1.00 12.18  ? 834  GLN A CB    1 
ATOM   6376  C  CG    . GLN A 1  834  ? 131.611 111.279 127.505 1.00 2.00   ? 834  GLN A CG    1 
ATOM   6377  C  CD    . GLN A 1  834  ? 132.945 111.921 127.611 1.00 11.09  ? 834  GLN A CD    1 
ATOM   6378  O  OE1   . GLN A 1  834  ? 133.081 113.132 127.524 1.00 7.21   ? 834  GLN A OE1   1 
ATOM   6379  N  NE2   . GLN A 1  834  ? 133.957 111.104 127.761 1.00 3.58   ? 834  GLN A NE2   1 
ATOM   6380  N  N     . SER A 1  835  ? 129.499 108.890 126.871 1.00 10.40  ? 835  SER A N     1 
ATOM   6381  C  CA    . SER A 1  835  ? 129.793 107.519 126.485 1.00 15.11  ? 835  SER A CA    1 
ATOM   6382  C  C     . SER A 1  835  ? 128.641 106.829 125.777 1.00 11.99  ? 835  SER A C     1 
ATOM   6383  O  O     . SER A 1  835  ? 128.806 105.686 125.352 1.00 8.75   ? 835  SER A O     1 
ATOM   6384  C  CB    . SER A 1  835  ? 130.206 106.695 127.704 1.00 4.18   ? 835  SER A CB    1 
ATOM   6385  O  OG    . SER A 1  835  ? 131.430 107.158 128.228 1.00 15.97  ? 835  SER A OG    1 
ATOM   6386  N  N     . CYS A 1  836  ? 127.499 107.486 125.622 1.00 6.58   ? 836  CYS A N     1 
ATOM   6387  C  CA    . CYS A 1  836  ? 126.358 106.902 124.933 1.00 4.44   ? 836  CYS A CA    1 
ATOM   6388  C  C     . CYS A 1  836  ? 126.526 107.061 123.427 1.00 10.47  ? 836  CYS A C     1 
ATOM   6389  O  O     . CYS A 1  836  ? 126.639 108.179 122.925 1.00 15.67  ? 836  CYS A O     1 
ATOM   6390  C  CB    . CYS A 1  836  ? 125.064 107.557 125.407 1.00 5.21   ? 836  CYS A CB    1 
ATOM   6391  S  SG    . CYS A 1  836  ? 124.741 107.454 127.170 1.00 2.53   ? 836  CYS A SG    1 
ATOM   6392  N  N     . ILE A 1  837  ? 126.524 105.943 122.708 1.00 1.39   ? 837  ILE A N     1 
ATOM   6393  C  CA    . ILE A 1  837  ? 126.814 105.905 121.282 1.00 1.98   ? 837  ILE A CA    1 
ATOM   6394  C  C     . ILE A 1  837  ? 125.872 104.905 120.623 1.00 10.15  ? 837  ILE A C     1 
ATOM   6395  O  O     . ILE A 1  837  ? 125.522 103.882 121.209 1.00 5.77   ? 837  ILE A O     1 
ATOM   6396  C  CB    . ILE A 1  837  ? 128.311 105.569 121.045 1.00 7.77   ? 837  ILE A CB    1 
ATOM   6397  C  CG1   . ILE A 1  837  ? 129.175 106.733 121.522 1.00 5.15   ? 837  ILE A CG1   1 
ATOM   6398  C  CG2   . ILE A 1  837  ? 128.611 105.297 119.600 1.00 9.50   ? 837  ILE A CG2   1 
ATOM   6399  C  CD1   . ILE A 1  837  ? 130.423 106.334 122.194 1.00 2.23   ? 837  ILE A CD1   1 
ATOM   6400  N  N     . VAL A 1  838  ? 125.428 105.230 119.410 1.00 0.82   ? 838  VAL A N     1 
ATOM   6401  C  CA    . VAL A 1  838  ? 124.486 104.399 118.665 1.00 1.70   ? 838  VAL A CA    1 
ATOM   6402  C  C     . VAL A 1  838  ? 125.194 103.157 118.131 1.00 0.90   ? 838  VAL A C     1 
ATOM   6403  O  O     . VAL A 1  838  ? 126.272 103.250 117.539 1.00 6.96   ? 838  VAL A O     1 
ATOM   6404  C  CB    . VAL A 1  838  ? 123.836 105.208 117.530 1.00 1.01   ? 838  VAL A CB    1 
ATOM   6405  C  CG1   . VAL A 1  838  ? 122.909 104.349 116.698 1.00 9.41   ? 838  VAL A CG1   1 
ATOM   6406  C  CG2   . VAL A 1  838  ? 123.074 106.367 118.090 1.00 6.28   ? 838  VAL A CG2   1 
ATOM   6407  N  N     . ASP A 1  839  ? 124.577 101.992 118.330 1.00 9.41   ? 839  ASP A N     1 
ATOM   6408  C  CA    . ASP A 1  839  ? 125.102 100.689 117.933 1.00 10.60  ? 839  ASP A CA    1 
ATOM   6409  C  C     . ASP A 1  839  ? 124.809 100.387 116.472 1.00 10.05  ? 839  ASP A C     1 
ATOM   6410  O  O     . ASP A 1  839  ? 124.331 101.231 115.719 1.00 18.04  ? 839  ASP A O     1 
ATOM   6411  C  CB    . ASP A 1  839  ? 124.473 99.575  118.759 1.00 14.57  ? 839  ASP A CB    1 
ATOM   6412  C  CG    . ASP A 1  839  ? 124.907 99.589  120.160 1.00 22.49  ? 839  ASP A CG    1 
ATOM   6413  O  OD1   . ASP A 1  839  ? 125.887 100.289 120.463 1.00 32.74  ? 839  ASP A OD1   1 
ATOM   6414  O  OD2   . ASP A 1  839  ? 124.280 98.889  120.966 1.00 19.80  ? 839  ASP A OD2   1 
ATOM   6415  N  N     . TYR A 1  840  ? 125.052 99.135  116.081 1.00 2.69   ? 840  TYR A N     1 
ATOM   6416  C  CA    . TYR A 1  840  ? 124.632 98.594  114.797 1.00 0.78   ? 840  TYR A CA    1 
ATOM   6417  C  C     . TYR A 1  840  ? 123.197 98.106  114.804 1.00 1.53   ? 840  TYR A C     1 
ATOM   6418  O  O     . TYR A 1  840  ? 122.703 97.664  113.768 1.00 7.25   ? 840  TYR A O     1 
ATOM   6419  C  CB    . TYR A 1  840  ? 125.539 97.443  114.384 1.00 4.35   ? 840  TYR A CB    1 
ATOM   6420  C  CG    . TYR A 1  840  ? 126.859 97.906  113.857 1.00 3.90   ? 840  TYR A CG    1 
ATOM   6421  C  CD1   . TYR A 1  840  ? 126.930 98.745  112.772 1.00 9.45   ? 840  TYR A CD1   1 
ATOM   6422  C  CD2   . TYR A 1  840  ? 128.036 97.513  114.459 1.00 0.84   ? 840  TYR A CD2   1 
ATOM   6423  C  CE1   . TYR A 1  840  ? 128.128 99.178  112.304 1.00 15.10  ? 840  TYR A CE1   1 
ATOM   6424  C  CE2   . TYR A 1  840  ? 129.237 97.945  113.998 1.00 1.81   ? 840  TYR A CE2   1 
ATOM   6425  C  CZ    . TYR A 1  840  ? 129.282 98.774  112.919 1.00 0.90   ? 840  TYR A CZ    1 
ATOM   6426  O  OH    . TYR A 1  840  ? 130.491 99.201  112.454 1.00 2.55   ? 840  TYR A OH    1 
ATOM   6427  N  N     . TYR A 1  841  ? 122.534 98.129  115.949 1.00 2.79   ? 841  TYR A N     1 
ATOM   6428  C  CA    . TYR A 1  841  ? 121.122 97.810  116.044 1.00 5.81   ? 841  TYR A CA    1 
ATOM   6429  C  C     . TYR A 1  841  ? 120.265 99.047  116.210 1.00 1.93   ? 841  TYR A C     1 
ATOM   6430  O  O     . TYR A 1  841  ? 119.047 98.922  116.323 1.00 12.45  ? 841  TYR A O     1 
ATOM   6431  C  CB    . TYR A 1  841  ? 120.872 96.865  117.214 1.00 2.68   ? 841  TYR A CB    1 
ATOM   6432  C  CG    . TYR A 1  841  ? 121.346 95.456  117.014 1.00 2.69   ? 841  TYR A CG    1 
ATOM   6433  C  CD1   . TYR A 1  841  ? 122.680 95.131  117.141 1.00 3.92   ? 841  TYR A CD1   1 
ATOM   6434  C  CD2   . TYR A 1  841  ? 120.453 94.440  116.744 1.00 2.24   ? 841  TYR A CD2   1 
ATOM   6435  C  CE1   . TYR A 1  841  ? 123.115 93.847  116.972 1.00 15.71  ? 841  TYR A CE1   1 
ATOM   6436  C  CE2   . TYR A 1  841  ? 120.880 93.151  116.577 1.00 6.16   ? 841  TYR A CE2   1 
ATOM   6437  C  CZ    . TYR A 1  841  ? 122.209 92.862  116.693 1.00 4.63   ? 841  TYR A CZ    1 
ATOM   6438  O  OH    . TYR A 1  841  ? 122.634 91.576  116.525 1.00 14.60  ? 841  TYR A OH    1 
ATOM   6439  N  N     . ARG A 1  842  ? 120.878 100.229 116.214 1.00 12.32  ? 842  ARG A N     1 
ATOM   6440  C  CA    . ARG A 1  842  ? 120.292 101.514 116.579 1.00 1.01   ? 842  ARG A CA    1 
ATOM   6441  C  C     . ARG A 1  842  ? 119.981 101.620 118.062 1.00 6.00   ? 842  ARG A C     1 
ATOM   6442  O  O     . ARG A 1  842  ? 119.262 102.529 118.467 1.00 1.14   ? 842  ARG A O     1 
ATOM   6443  C  CB    . ARG A 1  842  ? 119.031 101.837 115.773 1.00 7.02   ? 842  ARG A CB    1 
ATOM   6444  C  CG    . ARG A 1  842  ? 119.214 102.778 114.615 1.00 3.20   ? 842  ARG A CG    1 
ATOM   6445  C  CD    . ARG A 1  842  ? 119.866 102.064 113.507 1.00 0.17   ? 842  ARG A CD    1 
ATOM   6446  N  NE    . ARG A 1  842  ? 119.925 102.824 112.269 1.00 7.64   ? 842  ARG A NE    1 
ATOM   6447  C  CZ    . ARG A 1  842  ? 119.536 102.363 111.090 1.00 3.75   ? 842  ARG A CZ    1 
ATOM   6448  N  NH1   . ARG A 1  842  ? 118.922 101.203 110.969 1.00 13.61  ? 842  ARG A NH1   1 
ATOM   6449  N  NH2   . ARG A 1  842  ? 119.805 103.068 110.003 1.00 0.64   ? 842  ARG A NH2   1 
ATOM   6450  N  N     . ARG A 1  843  ? 120.502 100.722 118.886 1.00 13.45  ? 843  ARG A N     1 
ATOM   6451  C  CA    . ARG A 1  843  ? 120.408 100.882 120.326 1.00 15.85  ? 843  ARG A CA    1 
ATOM   6452  C  C     . ARG A 1  843  ? 121.440 101.892 120.801 1.00 4.68   ? 843  ARG A C     1 
ATOM   6453  O  O     . ARG A 1  843  ? 122.370 102.249 120.085 1.00 6.96   ? 843  ARG A O     1 
ATOM   6454  C  CB    . ARG A 1  843  ? 120.648 99.554  121.038 1.00 1.11   ? 843  ARG A CB    1 
ATOM   6455  C  CG    . ARG A 1  843  ? 119.963 98.370  120.429 1.00 9.23   ? 843  ARG A CG    1 
ATOM   6456  C  CD    . ARG A 1  843  ? 120.245 97.138  121.222 1.00 1.54   ? 843  ARG A CD    1 
ATOM   6457  N  NE    . ARG A 1  843  ? 121.672 96.882  121.327 1.00 1.95   ? 843  ARG A NE    1 
ATOM   6458  C  CZ    . ARG A 1  843  ? 122.272 95.764  120.957 1.00 5.02   ? 843  ARG A CZ    1 
ATOM   6459  N  NH1   . ARG A 1  843  ? 121.593 94.738  120.494 1.00 7.01   ? 843  ARG A NH1   1 
ATOM   6460  N  NH2   . ARG A 1  843  ? 123.589 95.678  121.055 1.00 1.85   ? 843  ARG A NH2   1 
ATOM   6461  N  N     . VAL A 1  844  ? 121.280 102.345 122.032 1.00 4.69   ? 844  VAL A N     1 
ATOM   6462  C  CA    . VAL A 1  844  ? 122.255 103.206 122.685 1.00 12.66  ? 844  VAL A CA    1 
ATOM   6463  C  C     . VAL A 1  844  ? 122.823 102.444 123.870 1.00 3.78   ? 844  VAL A C     1 
ATOM   6464  O  O     . VAL A 1  844  ? 122.072 101.935 124.702 1.00 2.97   ? 844  VAL A O     1 
ATOM   6465  C  CB    . VAL A 1  844  ? 121.628 104.535 123.132 1.00 8.77   ? 844  VAL A CB    1 
ATOM   6466  C  CG1   . VAL A 1  844  ? 122.666 105.411 123.756 1.00 3.07   ? 844  VAL A CG1   1 
ATOM   6467  C  CG2   . VAL A 1  844  ? 120.988 105.222 121.964 1.00 2.73   ? 844  VAL A CG2   1 
ATOM   6468  N  N     . SER A 1  845  ? 124.141 102.355 123.943 1.00 13.87  ? 845  SER A N     1 
ATOM   6469  C  CA    . SER A 1  845  ? 124.787 101.595 124.996 1.00 6.60   ? 845  SER A CA    1 
ATOM   6470  C  C     . SER A 1  845  ? 125.986 102.363 125.525 1.00 4.14   ? 845  SER A C     1 
ATOM   6471  O  O     . SER A 1  845  ? 126.460 103.313 124.909 1.00 14.57  ? 845  SER A O     1 
ATOM   6472  C  CB    . SER A 1  845  ? 125.203 100.206 124.500 1.00 1.92   ? 845  SER A CB    1 
ATOM   6473  O  OG    . SER A 1  845  ? 125.996 100.280 123.341 1.00 7.42   ? 845  SER A OG    1 
ATOM   6474  N  N     . ILE A 1  846  ? 126.443 101.965 126.707 1.00 15.09  ? 846  ILE A N     1 
ATOM   6475  C  CA    . ILE A 1  846  ? 127.734 102.419 127.206 1.00 10.26  ? 846  ILE A CA    1 
ATOM   6476  C  C     . ILE A 1  846  ? 128.677 101.230 127.227 1.00 2.74   ? 846  ILE A C     1 
ATOM   6477  O  O     . ILE A 1  846  ? 128.758 100.484 128.205 1.00 13.05  ? 846  ILE A O     1 
ATOM   6478  C  CB    . ILE A 1  846  ? 127.618 103.095 128.578 1.00 4.03   ? 846  ILE A CB    1 
ATOM   6479  C  CG1   . ILE A 1  846  ? 126.772 104.350 128.452 1.00 2.80   ? 846  ILE A CG1   1 
ATOM   6480  C  CG2   . ILE A 1  846  ? 128.968 103.457 129.104 1.00 7.70   ? 846  ILE A CG2   1 
ATOM   6481  C  CD1   . ILE A 1  846  ? 126.499 105.009 129.735 1.00 2.77   ? 846  ILE A CD1   1 
ATOM   6482  N  N     . ASP A 1  847  ? 129.355 101.050 126.104 1.00 4.35   ? 847  ASP A N     1 
ATOM   6483  C  CA    . ASP A 1  847  ? 130.344 100.043 125.760 1.00 3.42   ? 847  ASP A CA    1 
ATOM   6484  C  C     . ASP A 1  847  ? 129.794 98.643  125.543 1.00 1.74   ? 847  ASP A C     1 
ATOM   6485  O  O     . ASP A 1  847  ? 130.228 97.962  124.614 1.00 14.44  ? 847  ASP A O     1 
ATOM   6486  C  CB    . ASP A 1  847  ? 131.385 99.991  126.882 1.00 4.05   ? 847  ASP A CB    1 
ATOM   6487  C  CG    . ASP A 1  847  ? 132.283 98.792  126.802 1.00 8.83   ? 847  ASP A CG    1 
ATOM   6488  O  OD1   . ASP A 1  847  ? 132.710 98.423  125.697 1.00 18.37  ? 847  ASP A OD1   1 
ATOM   6489  O  OD2   . ASP A 1  847  ? 132.558 98.204  127.862 1.00 5.59   ? 847  ASP A OD2   1 
ATOM   6490  N  N     . THR A 1  848  ? 128.793 98.224  126.300 1.00 3.44   ? 848  THR A N     1 
ATOM   6491  C  CA    . THR A 1  848  ? 128.023 97.039  125.954 1.00 2.95   ? 848  THR A CA    1 
ATOM   6492  C  C     . THR A 1  848  ? 126.646 97.166  126.566 1.00 4.78   ? 848  THR A C     1 
ATOM   6493  O  O     . THR A 1  848  ? 125.687 96.538  126.118 1.00 13.97  ? 848  THR A O     1 
ATOM   6494  C  CB    . THR A 1  848  ? 128.712 95.757  126.415 1.00 11.98  ? 848  THR A CB    1 
ATOM   6495  O  OG1   . THR A 1  848  ? 129.657 96.059  127.448 1.00 17.64  ? 848  THR A OG1   1 
ATOM   6496  C  CG2   . THR A 1  848  ? 129.405 95.079  125.249 1.00 2.02   ? 848  THR A CG2   1 
ATOM   6497  N  N     . ARG A 1  849  ? 126.571 97.977  127.610 1.00 3.06   ? 849  ARG A N     1 
ATOM   6498  C  CA    . ARG A 1  849  ? 125.435 98.019  128.508 1.00 9.55   ? 849  ARG A CA    1 
ATOM   6499  C  C     . ARG A 1  849  ? 124.373 98.943  127.934 1.00 6.29   ? 849  ARG A C     1 
ATOM   6500  O  O     . ARG A 1  849  ? 124.621 100.132 127.743 1.00 7.06   ? 849  ARG A O     1 
ATOM   6501  C  CB    . ARG A 1  849  ? 125.885 98.494  129.885 1.00 2.72   ? 849  ARG A CB    1 
ATOM   6502  C  CG    . ARG A 1  849  ? 126.566 97.441  130.733 1.00 3.46   ? 849  ARG A CG    1 
ATOM   6503  C  CD    . ARG A 1  849  ? 127.306 98.085  131.886 1.00 2.55   ? 849  ARG A CD    1 
ATOM   6504  N  NE    . ARG A 1  849  ? 128.618 98.594  131.508 1.00 8.94   ? 849  ARG A NE    1 
ATOM   6505  C  CZ    . ARG A 1  849  ? 129.210 99.635  132.073 1.00 3.18   ? 849  ARG A CZ    1 
ATOM   6506  N  NH1   . ARG A 1  849  ? 128.615 100.339 133.016 1.00 9.41   ? 849  ARG A NH1   1 
ATOM   6507  N  NH2   . ARG A 1  849  ? 130.427 99.982  131.677 1.00 5.14   ? 849  ARG A NH2   1 
ATOM   6508  N  N     . LEU A 1  850  ? 123.192 98.393  127.678 1.00 7.31   ? 850  LEU A N     1 
ATOM   6509  C  CA    . LEU A 1  850  ? 122.118 99.126  127.031 1.00 11.12  ? 850  LEU A CA    1 
ATOM   6510  C  C     . LEU A 1  850  ? 121.678 100.322 127.856 1.00 10.74  ? 850  LEU A C     1 
ATOM   6511  O  O     . LEU A 1  850  ? 121.440 100.206 129.057 1.00 4.05   ? 850  LEU A O     1 
ATOM   6512  C  CB    . LEU A 1  850  ? 120.930 98.203  126.805 1.00 5.26   ? 850  LEU A CB    1 
ATOM   6513  C  CG    . LEU A 1  850  ? 120.690 97.699  125.397 1.00 2.41   ? 850  LEU A CG    1 
ATOM   6514  C  CD1   . LEU A 1  850  ? 121.953 97.073  124.877 1.00 4.90   ? 850  LEU A CD1   1 
ATOM   6515  C  CD2   . LEU A 1  850  ? 119.561 96.716  125.407 1.00 9.76   ? 850  LEU A CD2   1 
ATOM   6516  N  N     . VAL A 1  851  ? 121.545 101.468 127.203 1.00 4.74   ? 851  VAL A N     1 
ATOM   6517  C  CA    . VAL A 1  851  ? 120.895 102.625 127.787 1.00 15.63  ? 851  VAL A CA    1 
ATOM   6518  C  C     . VAL A 1  851  ? 119.507 102.830 127.199 1.00 2.78   ? 851  VAL A C     1 
ATOM   6519  O  O     . VAL A 1  851  ? 118.562 103.123 127.924 1.00 7.57   ? 851  VAL A O     1 
ATOM   6520  C  CB    . VAL A 1  851  ? 121.777 103.878 127.608 1.00 13.31  ? 851  VAL A CB    1 
ATOM   6521  C  CG1   . VAL A 1  851  ? 121.073 105.105 128.102 1.00 1.67   ? 851  VAL A CG1   1 
ATOM   6522  C  CG2   . VAL A 1  851  ? 123.075 103.700 128.333 1.00 2.12   ? 851  VAL A CG2   1 
ATOM   6523  N  N     . GLN A 1  852  ? 119.367 102.638 125.895 1.00 13.90  ? 852  GLN A N     1 
ATOM   6524  C  CA    . GLN A 1  852  ? 118.088 102.652 125.204 1.00 13.49  ? 852  GLN A CA    1 
ATOM   6525  C  C     . GLN A 1  852  ? 118.033 101.452 124.282 1.00 8.36   ? 852  GLN A C     1 
ATOM   6526  O  O     . GLN A 1  852  ? 119.049 101.057 123.718 1.00 18.04  ? 852  GLN A O     1 
ATOM   6527  C  CB    . GLN A 1  852  ? 117.896 103.927 124.397 1.00 10.81  ? 852  GLN A CB    1 
ATOM   6528  C  CG    . GLN A 1  852  ? 117.716 105.139 125.248 1.00 16.69  ? 852  GLN A CG    1 
ATOM   6529  C  CD    . GLN A 1  852  ? 117.416 106.358 124.452 1.00 12.41  ? 852  GLN A CD    1 
ATOM   6530  O  OE1   . GLN A 1  852  ? 117.560 106.365 123.247 1.00 22.77  ? 852  GLN A OE1   1 
ATOM   6531  N  NE2   . GLN A 1  852  ? 116.974 107.398 125.117 1.00 16.57  ? 852  GLN A NE2   1 
ATOM   6532  N  N     . GLN A 1  853  ? 116.850 100.858 124.146 1.00 0.85   ? 853  GLN A N     1 
ATOM   6533  C  CA    . GLN A 1  853  ? 116.684 99.754  123.211 1.00 2.78   ? 853  GLN A CA    1 
ATOM   6534  C  C     . GLN A 1  853  ? 116.613 100.241 121.769 1.00 4.34   ? 853  GLN A C     1 
ATOM   6535  O  O     . GLN A 1  853  ? 116.973 99.507  120.850 1.00 6.51   ? 853  GLN A O     1 
ATOM   6536  C  CB    . GLN A 1  853  ? 115.445 98.944  123.584 1.00 0.85   ? 853  GLN A CB    1 
ATOM   6537  C  CG    . GLN A 1  853  ? 115.083 97.866  122.601 1.00 2.21   ? 853  GLN A CG    1 
ATOM   6538  C  CD    . GLN A 1  853  ? 115.901 96.617  122.766 1.00 7.37   ? 853  GLN A CD    1 
ATOM   6539  O  OE1   . GLN A 1  853  ? 116.803 96.340  121.985 1.00 1.76   ? 853  GLN A OE1   1 
ATOM   6540  N  NE2   . GLN A 1  853  ? 115.581 95.842  123.784 1.00 10.88  ? 853  GLN A NE2   1 
ATOM   6541  N  N     . LEU A 1  854  ? 116.153 101.462 121.553 1.00 4.71   ? 854  LEU A N     1 
ATOM   6542  C  CA    . LEU A 1  854  ? 116.148 102.106 120.251 1.00 4.44   ? 854  LEU A CA    1 
ATOM   6543  C  C     . LEU A 1  854  ? 116.275 103.596 120.483 1.00 2.88   ? 854  LEU A C     1 
ATOM   6544  O  O     . LEU A 1  854  ? 115.556 104.149 121.310 1.00 2.25   ? 854  LEU A O     1 
ATOM   6545  C  CB    . LEU A 1  854  ? 114.870 101.795 119.476 1.00 2.98   ? 854  LEU A CB    1 
ATOM   6546  C  CG    . LEU A 1  854  ? 114.770 102.175 118.003 1.00 0.39   ? 854  LEU A CG    1 
ATOM   6547  C  CD1   . LEU A 1  854  ? 115.733 101.389 117.152 1.00 3.11   ? 854  LEU A CD1   1 
ATOM   6548  C  CD2   . LEU A 1  854  ? 113.372 101.946 117.538 1.00 0.17   ? 854  LEU A CD2   1 
ATOM   6549  N  N     . TYR A 1  855  ? 117.182 104.241 119.765 1.00 7.35   ? 855  TYR A N     1 
ATOM   6550  C  CA    . TYR A 1  855  ? 117.442 105.656 119.995 1.00 15.93  ? 855  TYR A CA    1 
ATOM   6551  C  C     . TYR A 1  855  ? 116.175 106.471 119.792 1.00 3.09   ? 855  TYR A C     1 
ATOM   6552  O  O     . TYR A 1  855  ? 115.526 106.373 118.752 1.00 6.63   ? 855  TYR A O     1 
ATOM   6553  C  CB    . TYR A 1  855  ? 118.543 106.154 119.063 1.00 3.77   ? 855  TYR A CB    1 
ATOM   6554  C  CG    . TYR A 1  855  ? 118.729 107.644 119.128 1.00 3.20   ? 855  TYR A CG    1 
ATOM   6555  C  CD1   . TYR A 1  855  ? 119.201 108.245 120.277 1.00 7.66   ? 855  TYR A CD1   1 
ATOM   6556  C  CD2   . TYR A 1  855  ? 118.415 108.453 118.057 1.00 2.75   ? 855  TYR A CD2   1 
ATOM   6557  C  CE1   . TYR A 1  855  ? 119.356 109.587 120.354 1.00 4.31   ? 855  TYR A CE1   1 
ATOM   6558  C  CE2   . TYR A 1  855  ? 118.574 109.797 118.131 1.00 4.82   ? 855  TYR A CE2   1 
ATOM   6559  C  CZ    . TYR A 1  855  ? 119.044 110.359 119.282 1.00 4.29   ? 855  TYR A CZ    1 
ATOM   6560  O  OH    . TYR A 1  855  ? 119.219 111.713 119.370 1.00 9.09   ? 855  TYR A OH    1 
ATOM   6561  N  N     . GLY A 1  856  ? 115.814 107.261 120.797 1.00 0.92   ? 856  GLY A N     1 
ATOM   6562  C  CA    . GLY A 1  856  ? 114.621 108.076 120.745 1.00 1.11   ? 856  GLY A CA    1 
ATOM   6563  C  C     . GLY A 1  856  ? 113.327 107.306 120.687 1.00 3.87   ? 856  GLY A C     1 
ATOM   6564  O  O     . GLY A 1  856  ? 112.281 107.905 120.440 1.00 7.76   ? 856  GLY A O     1 
ATOM   6565  N  N     . GLU A 1  857  ? 113.378 105.992 120.894 1.00 9.60   ? 857  GLU A N     1 
ATOM   6566  C  CA    . GLU A 1  857  ? 112.263 105.058 120.786 1.00 5.26   ? 857  GLU A CA    1 
ATOM   6567  C  C     . GLU A 1  857  ? 111.705 104.955 119.382 1.00 8.49   ? 857  GLU A C     1 
ATOM   6568  O  O     . GLU A 1  857  ? 110.826 104.133 119.131 1.00 10.37  ? 857  GLU A O     1 
ATOM   6569  C  CB    . GLU A 1  857  ? 111.155 105.420 121.761 1.00 1.96   ? 857  GLU A CB    1 
ATOM   6570  C  CG    . GLU A 1  857  ? 111.492 105.044 123.163 1.00 4.33   ? 857  GLU A CG    1 
ATOM   6571  C  CD    . GLU A 1  857  ? 110.925 105.988 124.161 1.00 9.96   ? 857  GLU A CD    1 
ATOM   6572  O  OE1   . GLU A 1  857  ? 110.378 107.026 123.746 1.00 6.77   ? 857  GLU A OE1   1 
ATOM   6573  O  OE2   . GLU A 1  857  ? 111.031 105.696 125.365 1.00 15.13  ? 857  GLU A OE2   1 
ATOM   6574  N  N     . ASP A 1  858  ? 112.217 105.751 118.453 1.00 11.35  ? 858  ASP A N     1 
ATOM   6575  C  CA    . ASP A 1  858  ? 111.832 105.625 117.059 1.00 4.55   ? 858  ASP A CA    1 
ATOM   6576  C  C     . ASP A 1  858  ? 113.010 105.522 116.107 1.00 3.41   ? 858  ASP A C     1 
ATOM   6577  O  O     . ASP A 1  858  ? 112.793 105.235 114.931 1.00 5.59   ? 858  ASP A O     1 
ATOM   6578  C  CB    . ASP A 1  858  ? 110.918 106.786 116.633 1.00 9.57   ? 858  ASP A CB    1 
ATOM   6579  C  CG    . ASP A 1  858  ? 111.490 108.159 116.943 1.00 11.04  ? 858  ASP A CG    1 
ATOM   6580  O  OD1   . ASP A 1  858  ? 112.687 108.294 117.250 1.00 8.26   ? 858  ASP A OD1   1 
ATOM   6581  O  OD2   . ASP A 1  858  ? 110.725 109.133 116.868 1.00 13.80  ? 858  ASP A OD2   1 
ATOM   6582  N  N     . GLY A 1  859  ? 114.239 105.712 116.576 1.00 15.15  ? 859  GLY A N     1 
ATOM   6583  C  CA    . GLY A 1  859  ? 115.414 105.500 115.759 1.00 1.34   ? 859  GLY A CA    1 
ATOM   6584  C  C     . GLY A 1  859  ? 115.682 106.537 114.700 1.00 12.39  ? 859  GLY A C     1 
ATOM   6585  O  O     . GLY A 1  859  ? 116.276 106.209 113.678 1.00 5.35   ? 859  GLY A O     1 
ATOM   6586  N  N     . LEU A 1  860  ? 115.299 107.785 114.927 1.00 10.16  ? 860  LEU A N     1 
ATOM   6587  C  CA    . LEU A 1  860  ? 115.347 108.828 113.919 1.00 7.34   ? 860  LEU A CA    1 
ATOM   6588  C  C     . LEU A 1  860  ? 116.333 109.924 114.295 1.00 5.29   ? 860  LEU A C     1 
ATOM   6589  O  O     . LEU A 1  860  ? 116.645 110.141 115.462 1.00 10.84  ? 860  LEU A O     1 
ATOM   6590  C  CB    . LEU A 1  860  ? 113.965 109.444 113.701 1.00 3.75   ? 860  LEU A CB    1 
ATOM   6591  C  CG    . LEU A 1  860  ? 112.835 108.501 113.318 1.00 3.84   ? 860  LEU A CG    1 
ATOM   6592  C  CD1   . LEU A 1  860  ? 111.529 109.220 113.383 1.00 2.42   ? 860  LEU A CD1   1 
ATOM   6593  C  CD2   . LEU A 1  860  ? 113.052 107.927 111.953 1.00 8.53   ? 860  LEU A CD2   1 
ATOM   6594  N  N     . ASP A 1  861  ? 116.829 110.599 113.267 1.00 10.13  ? 861  ASP A N     1 
ATOM   6595  C  CA    . ASP A 1  861  ? 117.613 111.813 113.422 1.00 2.41   ? 861  ASP A CA    1 
ATOM   6596  C  C     . ASP A 1  861  ? 116.685 113.011 113.611 1.00 5.36   ? 861  ASP A C     1 
ATOM   6597  O  O     . ASP A 1  861  ? 115.681 113.147 112.912 1.00 6.65   ? 861  ASP A O     1 
ATOM   6598  C  CB    . ASP A 1  861  ? 118.493 112.010 112.189 1.00 15.35  ? 861  ASP A CB    1 
ATOM   6599  C  CG    . ASP A 1  861  ? 119.518 113.098 112.361 1.00 1.35   ? 861  ASP A CG    1 
ATOM   6600  O  OD1   . ASP A 1  861  ? 119.675 113.633 113.467 1.00 7.96   ? 861  ASP A OD1   1 
ATOM   6601  O  OD2   . ASP A 1  861  ? 120.163 113.451 111.364 1.00 4.71   ? 861  ASP A OD2   1 
ATOM   6602  N  N     . ALA A 1  862  ? 117.023 113.880 114.566 1.00 3.68   ? 862  ALA A N     1 
ATOM   6603  C  CA    . ALA A 1  862  ? 116.183 115.035 114.870 1.00 0.11   ? 862  ALA A CA    1 
ATOM   6604  C  C     . ALA A 1  862  ? 116.226 116.106 113.791 1.00 4.13   ? 862  ALA A C     1 
ATOM   6605  O  O     . ALA A 1  862  ? 115.411 117.026 113.827 1.00 16.06  ? 862  ALA A O     1 
ATOM   6606  C  CB    . ALA A 1  862  ? 116.582 115.658 116.204 1.00 1.26   ? 862  ALA A CB    1 
ATOM   6607  N  N     . ARG A 1  863  ? 117.147 116.024 112.847 1.00 5.79   ? 863  ARG A N     1 
ATOM   6608  C  CA    . ARG A 1  863  ? 117.166 116.931 111.715 1.00 4.20   ? 863  ARG A CA    1 
ATOM   6609  C  C     . ARG A 1  863  ? 116.255 116.476 110.593 1.00 2.67   ? 863  ARG A C     1 
ATOM   6610  O  O     . ARG A 1  863  ? 116.183 117.146 109.563 1.00 7.99   ? 863  ARG A O     1 
ATOM   6611  C  CB    . ARG A 1  863  ? 118.589 117.082 111.184 1.00 11.06  ? 863  ARG A CB    1 
ATOM   6612  C  CG    . ARG A 1  863  ? 119.527 117.781 112.120 1.00 2.32   ? 863  ARG A CG    1 
ATOM   6613  C  CD    . ARG A 1  863  ? 120.942 117.742 111.610 1.00 2.15   ? 863  ARG A CD    1 
ATOM   6614  N  NE    . ARG A 1  863  ? 121.450 116.382 111.513 1.00 0.38   ? 863  ARG A NE    1 
ATOM   6615  C  CZ    . ARG A 1  863  ? 122.641 116.051 111.041 1.00 3.01   ? 863  ARG A CZ    1 
ATOM   6616  N  NH1   . ARG A 1  863  ? 123.493 116.959 110.619 1.00 15.62  ? 863  ARG A NH1   1 
ATOM   6617  N  NH2   . ARG A 1  863  ? 122.987 114.773 110.999 1.00 6.26   ? 863  ARG A NH2   1 
ATOM   6618  N  N     . GLN A 1  864  ? 115.556 115.364 110.766 1.00 1.88   ? 864  GLN A N     1 
ATOM   6619  C  CA    . GLN A 1  864  ? 114.802 114.740 109.691 1.00 5.34   ? 864  GLN A CA    1 
ATOM   6620  C  C     . GLN A 1  864  ? 113.341 114.534 110.067 1.00 3.82   ? 864  GLN A C     1 
ATOM   6621  O  O     . GLN A 1  864  ? 112.710 113.593 109.601 1.00 11.88  ? 864  GLN A O     1 
ATOM   6622  C  CB    . GLN A 1  864  ? 115.439 113.414 109.298 1.00 0.57   ? 864  GLN A CB    1 
ATOM   6623  C  CG    . GLN A 1  864  ? 116.855 113.495 108.821 1.00 0.97   ? 864  GLN A CG    1 
ATOM   6624  C  CD    . GLN A 1  864  ? 116.962 114.046 107.426 1.00 3.07   ? 864  GLN A CD    1 
ATOM   6625  O  OE1   . GLN A 1  864  ? 116.099 113.817 106.592 1.00 7.46   ? 864  GLN A OE1   1 
ATOM   6626  N  NE2   . GLN A 1  864  ? 118.034 114.764 107.158 1.00 4.36   ? 864  GLN A NE2   1 
ATOM   6627  N  N     . LEU A 1  865  ? 112.785 115.410 110.890 1.00 6.05   ? 865  LEU A N     1 
ATOM   6628  C  CA    . LEU A 1  865  ? 111.407 115.304 111.337 1.00 0.14   ? 865  LEU A CA    1 
ATOM   6629  C  C     . LEU A 1  865  ? 110.567 116.436 110.768 1.00 3.58   ? 865  LEU A C     1 
ATOM   6630  O  O     . LEU A 1  865  ? 111.036 117.564 110.621 1.00 14.09  ? 865  LEU A O     1 
ATOM   6631  C  CB    . LEU A 1  865  ? 111.317 115.339 112.862 1.00 13.41  ? 865  LEU A CB    1 
ATOM   6632  C  CG    . LEU A 1  865  ? 112.096 114.298 113.647 1.00 1.08   ? 865  LEU A CG    1 
ATOM   6633  C  CD1   . LEU A 1  865  ? 112.228 114.748 115.071 1.00 8.06   ? 865  LEU A CD1   1 
ATOM   6634  C  CD2   . LEU A 1  865  ? 111.394 112.982 113.567 1.00 1.28   ? 865  LEU A CD2   1 
ATOM   6635  N  N     . GLU A 1  866  ? 109.315 116.125 110.453 1.00 8.03   ? 866  GLU A N     1 
ATOM   6636  C  CA    . GLU A 1  866  ? 108.334 117.119 110.045 1.00 3.67   ? 866  GLU A CA    1 
ATOM   6637  C  C     . GLU A 1  866  ? 107.099 116.984 110.918 1.00 6.53   ? 866  GLU A C     1 
ATOM   6638  O  O     . GLU A 1  866  ? 106.703 115.877 111.274 1.00 10.48  ? 866  GLU A O     1 
ATOM   6639  C  CB    . GLU A 1  866  ? 107.955 116.961 108.575 1.00 4.83   ? 866  GLU A CB    1 
ATOM   6640  C  CG    . GLU A 1  866  ? 107.231 118.162 108.001 1.00 8.75   ? 866  GLU A CG    1 
ATOM   6641  C  CD    . GLU A 1  866  ? 107.110 118.128 106.490 1.00 16.58  ? 866  GLU A CD    1 
ATOM   6642  O  OE1   . GLU A 1  866  ? 107.652 117.199 105.860 1.00 20.44  ? 866  GLU A OE1   1 
ATOM   6643  O  OE2   . GLU A 1  866  ? 106.460 119.036 105.930 1.00 14.01  ? 866  GLU A OE2   1 
ATOM   6644  N  N     . THR A 1  867  ? 106.499 118.115 111.265 1.00 16.04  ? 867  THR A N     1 
ATOM   6645  C  CA    . THR A 1  867  ? 105.273 118.146 112.059 1.00 9.71   ? 867  THR A CA    1 
ATOM   6646  C  C     . THR A 1  867  ? 104.058 117.979 111.153 1.00 12.65  ? 867  THR A C     1 
ATOM   6647  O  O     . THR A 1  867  ? 103.898 118.719 110.180 1.00 19.35  ? 867  THR A O     1 
ATOM   6648  C  CB    . THR A 1  867  ? 105.191 119.453 112.837 1.00 12.83  ? 867  THR A CB    1 
ATOM   6649  O  OG1   . THR A 1  867  ? 106.009 119.375 114.007 1.00 20.21  ? 867  THR A OG1   1 
ATOM   6650  C  CG2   . THR A 1  867  ? 103.797 119.743 113.232 1.00 14.89  ? 867  THR A CG2   1 
ATOM   6651  N  N     . VAL A 1  868  ? 103.217 117.000 111.466 1.00 10.04  ? 868  VAL A N     1 
ATOM   6652  C  CA    . VAL A 1  868  ? 102.088 116.594 110.642 1.00 8.11   ? 868  VAL A CA    1 
ATOM   6653  C  C     . VAL A 1  868  ? 100.881 116.388 111.548 1.00 15.44  ? 868  VAL A C     1 
ATOM   6654  O  O     . VAL A 1  868  ? 101.022 116.132 112.746 1.00 24.65  ? 868  VAL A O     1 
ATOM   6655  C  CB    . VAL A 1  868  ? 102.434 115.319 109.839 1.00 14.44  ? 868  VAL A CB    1 
ATOM   6656  C  CG1   . VAL A 1  868  ? 101.250 114.768 109.111 1.00 18.90  ? 868  VAL A CG1   1 
ATOM   6657  C  CG2   . VAL A 1  868  ? 103.507 115.628 108.837 1.00 16.82  ? 868  VAL A CG2   1 
ATOM   6658  N  N     . ARG A 1  869  ? 99.688  116.539 110.984 1.00 18.44  ? 869  ARG A N     1 
ATOM   6659  C  CA    . ARG A 1  869  ? 98.453  116.424 111.744 1.00 23.86  ? 869  ARG A CA    1 
ATOM   6660  C  C     . ARG A 1  869  ? 97.757  115.101 111.445 1.00 25.48  ? 869  ARG A C     1 
ATOM   6661  O  O     . ARG A 1  869  ? 97.665  114.687 110.288 1.00 22.56  ? 869  ARG A O     1 
ATOM   6662  C  CB    . ARG A 1  869  ? 97.523  117.589 111.420 1.00 25.62  ? 869  ARG A CB    1 
ATOM   6663  C  CG    . ARG A 1  869  ? 96.142  117.432 111.999 1.00 25.62  ? 869  ARG A CG    1 
ATOM   6664  C  CD    . ARG A 1  869  ? 95.412  118.751 112.069 1.00 23.91  ? 869  ARG A CD    1 
ATOM   6665  N  NE    . ARG A 1  869  ? 94.090  118.588 112.656 1.00 28.38  ? 869  ARG A NE    1 
ATOM   6666  C  CZ    . ARG A 1  869  ? 93.027  118.133 112.009 1.00 27.53  ? 869  ARG A CZ    1 
ATOM   6667  N  NH1   . ARG A 1  869  ? 93.086  117.797 110.732 1.00 25.08  ? 869  ARG A NH1   1 
ATOM   6668  N  NH2   . ARG A 1  869  ? 91.875  118.013 112.661 1.00 22.70  ? 869  ARG A NH2   1 
ATOM   6669  N  N     . PHE A 1  870  ? 97.278  114.438 112.496 1.00 22.97  ? 870  PHE A N     1 
ATOM   6670  C  CA    . PHE A 1  870  ? 96.508  113.203 112.384 1.00 19.04  ? 870  PHE A CA    1 
ATOM   6671  C  C     . PHE A 1  870  ? 95.034  113.573 112.495 1.00 24.91  ? 870  PHE A C     1 
ATOM   6672  O  O     . PHE A 1  870  ? 94.561  113.936 113.574 1.00 27.34  ? 870  PHE A O     1 
ATOM   6673  C  CB    . PHE A 1  870  ? 96.906  112.216 113.478 1.00 21.03  ? 870  PHE A CB    1 
ATOM   6674  C  CG    . PHE A 1  870  ? 98.238  111.571 113.260 1.00 21.75  ? 870  PHE A CG    1 
ATOM   6675  C  CD1   . PHE A 1  870  ? 99.403  112.294 113.419 1.00 21.99  ? 870  PHE A CD1   1 
ATOM   6676  C  CD2   . PHE A 1  870  ? 98.331  110.241 112.924 1.00 19.16  ? 870  PHE A CD2   1 
ATOM   6677  C  CE1   . PHE A 1  870  ? 100.624 111.709 113.219 1.00 18.81  ? 870  PHE A CE1   1 
ATOM   6678  C  CE2   . PHE A 1  870  ? 99.555  109.654 112.738 1.00 18.61  ? 870  PHE A CE2   1 
ATOM   6679  C  CZ    . PHE A 1  870  ? 100.700 110.388 112.886 1.00 17.35  ? 870  PHE A CZ    1 
ATOM   6680  N  N     . GLU A 1  871  ? 94.306  113.470 111.388 1.00 32.23  ? 871  GLU A N     1 
ATOM   6681  C  CA    . GLU A 1  871  ? 92.995  114.089 111.279 1.00 33.39  ? 871  GLU A CA    1 
ATOM   6682  C  C     . GLU A 1  871  ? 91.855  113.172 111.696 1.00 30.84  ? 871  GLU A C     1 
ATOM   6683  O  O     . GLU A 1  871  ? 90.692  113.523 111.493 1.00 38.59  ? 871  GLU A O     1 
ATOM   6684  C  CB    . GLU A 1  871  ? 92.769  114.596 109.855 1.00 34.04  ? 871  GLU A CB    1 
ATOM   6685  C  CG    . GLU A 1  871  ? 92.934  113.558 108.779 1.00 33.36  ? 871  GLU A CG    1 
ATOM   6686  C  CD    . GLU A 1  871  ? 91.931  113.741 107.663 1.00 39.63  ? 871  GLU A CD    1 
ATOM   6687  O  OE1   . GLU A 1  871  ? 92.349  113.861 106.492 1.00 36.11  ? 871  GLU A OE1   1 
ATOM   6688  O  OE2   . GLU A 1  871  ? 90.718  113.771 107.958 1.00 41.04  ? 871  GLU A OE2   1 
ATOM   6689  N  N     . THR A 1  872  ? 92.156  112.018 112.278 1.00 20.88  ? 872  THR A N     1 
ATOM   6690  C  CA    . THR A 1  872  ? 91.142  111.103 112.779 1.00 20.87  ? 872  THR A CA    1 
ATOM   6691  C  C     . THR A 1  872  ? 90.914  111.225 114.283 1.00 20.20  ? 872  THR A C     1 
ATOM   6692  O  O     . THR A 1  872  ? 89.862  110.812 114.771 1.00 25.09  ? 872  THR A O     1 
ATOM   6693  C  CB    . THR A 1  872  ? 91.535  109.667 112.409 1.00 20.11  ? 872  THR A CB    1 
ATOM   6694  O  OG1   . THR A 1  872  ? 91.697  109.575 110.992 1.00 23.68  ? 872  THR A OG1   1 
ATOM   6695  C  CG2   . THR A 1  872  ? 90.494  108.688 112.810 1.00 22.32  ? 872  THR A CG2   1 
ATOM   6696  N  N     . ILE A 1  873  ? 91.840  111.837 115.014 1.00 17.40  ? 873  ILE A N     1 
ATOM   6697  C  CA    . ILE A 1  873  ? 91.825  111.752 116.472 1.00 16.64  ? 873  ILE A CA    1 
ATOM   6698  C  C     . ILE A 1  873  ? 90.575  112.402 117.048 1.00 19.81  ? 873  ILE A C     1 
ATOM   6699  O  O     . ILE A 1  873  ? 89.919  111.844 117.931 1.00 26.99  ? 873  ILE A O     1 
ATOM   6700  C  CB    . ILE A 1  873  ? 93.105  112.374 117.055 1.00 18.77  ? 873  ILE A CB    1 
ATOM   6701  C  CG1   . ILE A 1  873  ? 94.335  111.767 116.380 1.00 19.64  ? 873  ILE A CG1   1 
ATOM   6702  C  CG2   . ILE A 1  873  ? 93.160  112.191 118.554 1.00 13.08  ? 873  ILE A CG2   1 
ATOM   6703  C  CD1   . ILE A 1  873  ? 94.328  110.273 116.352 1.00 14.00  ? 873  ILE A CD1   1 
ATOM   6704  N  N     . MET A 1  874  ? 90.226  113.588 116.565 1.00 25.29  ? 874  MET A N     1 
ATOM   6705  C  CA    . MET A 1  874  ? 89.174  114.379 117.188 1.00 22.55  ? 874  MET A CA    1 
ATOM   6706  C  C     . MET A 1  874  ? 87.779  114.070 116.669 1.00 22.63  ? 874  MET A C     1 
ATOM   6707  O  O     . MET A 1  874  ? 86.803  114.551 117.248 1.00 26.27  ? 874  MET A O     1 
ATOM   6708  C  CB    . MET A 1  874  ? 89.469  115.865 117.004 1.00 22.83  ? 874  MET A CB    1 
ATOM   6709  C  CG    . MET A 1  874  ? 90.797  116.282 117.572 1.00 21.18  ? 874  MET A CG    1 
ATOM   6710  S  SD    . MET A 1  874  ? 90.837  116.122 119.356 1.00 31.79  ? 874  MET A SD    1 
ATOM   6711  C  CE    . MET A 1  874  ? 92.391  116.921 119.720 1.00 26.07  ? 874  MET A CE    1 
ATOM   6712  N  N     . LEU A 1  875  ? 87.657  113.274 115.617 1.00 20.10  ? 875  LEU A N     1 
ATOM   6713  C  CA    . LEU A 1  875  ? 86.360  112.998 115.030 1.00 22.56  ? 875  LEU A CA    1 
ATOM   6714  C  C     . LEU A 1  875  ? 85.522  112.113 115.946 1.00 26.24  ? 875  LEU A C     1 
ATOM   6715  O  O     . LEU A 1  875  ? 86.035  111.415 116.820 1.00 33.08  ? 875  LEU A O     1 
ATOM   6716  C  CB    . LEU A 1  875  ? 86.531  112.326 113.670 1.00 23.41  ? 875  LEU A CB    1 
ATOM   6717  C  CG    . LEU A 1  875  ? 87.290  113.159 112.642 1.00 23.80  ? 875  LEU A CG    1 
ATOM   6718  C  CD1   . LEU A 1  875  ? 87.268  112.490 111.285 1.00 23.28  ? 875  LEU A CD1   1 
ATOM   6719  C  CD2   . LEU A 1  875  ? 86.719  114.555 112.569 1.00 26.78  ? 875  LEU A CD2   1 
ATOM   6720  N  N     . SER A 1  876  ? 84.208  112.166 115.745 1.00 29.62  ? 876  SER A N     1 
ATOM   6721  C  CA    . SER A 1  876  ? 83.282  111.240 116.375 1.00 28.63  ? 876  SER A CA    1 
ATOM   6722  C  C     . SER A 1  876  ? 83.028  110.069 115.430 1.00 31.67  ? 876  SER A C     1 
ATOM   6723  O  O     . SER A 1  876  ? 83.486  110.061 114.287 1.00 33.39  ? 876  SER A O     1 
ATOM   6724  C  CB    . SER A 1  876  ? 81.991  111.957 116.753 1.00 29.00  ? 876  SER A CB    1 
ATOM   6725  O  OG    . SER A 1  876  ? 81.258  112.303 115.599 1.00 36.21  ? 876  SER A OG    1 
ATOM   6726  N  N     . ASP A 1  877  ? 82.303  109.053 115.900 1.00 30.78  ? 877  ASP A N     1 
ATOM   6727  C  CA    . ASP A 1  877  ? 82.144  107.863 115.072 1.00 30.85  ? 877  ASP A CA    1 
ATOM   6728  C  C     . ASP A 1  877  ? 81.193  108.095 113.912 1.00 36.65  ? 877  ASP A C     1 
ATOM   6729  O  O     . ASP A 1  877  ? 81.155  107.284 112.984 1.00 39.79  ? 877  ASP A O     1 
ATOM   6730  C  CB    . ASP A 1  877  ? 81.673  106.671 115.894 1.00 33.07  ? 877  ASP A CB    1 
ATOM   6731  C  CG    . ASP A 1  877  ? 82.303  106.623 117.253 1.00 38.53  ? 877  ASP A CG    1 
ATOM   6732  O  OD1   . ASP A 1  877  ? 81.833  107.356 118.133 1.00 38.58  ? 877  ASP A OD1   1 
ATOM   6733  O  OD2   . ASP A 1  877  ? 83.277  105.864 117.441 1.00 36.39  ? 877  ASP A OD2   1 
ATOM   6734  N  N     . GLN A 1  878  ? 80.406  109.169 113.946 1.00 38.58  ? 878  GLN A N     1 
ATOM   6735  C  CA    . GLN A 1  878  ? 79.580  109.483 112.787 1.00 34.03  ? 878  GLN A CA    1 
ATOM   6736  C  C     . GLN A 1  878  ? 80.349  110.326 111.777 1.00 34.46  ? 878  GLN A C     1 
ATOM   6737  O  O     . GLN A 1  878  ? 80.197  110.145 110.566 1.00 34.37  ? 878  GLN A O     1 
ATOM   6738  C  CB    . GLN A 1  878  ? 78.295  110.183 113.225 1.00 35.11  ? 878  GLN A CB    1 
ATOM   6739  C  CG    . GLN A 1  878  ? 77.184  110.090 112.203 1.00 36.95  ? 878  GLN A CG    1 
ATOM   6740  C  CD    . GLN A 1  878  ? 76.986  108.680 111.697 1.00 38.88  ? 878  GLN A CD    1 
ATOM   6741  O  OE1   . GLN A 1  878  ? 77.320  108.365 110.555 1.00 38.85  ? 878  GLN A OE1   1 
ATOM   6742  N  NE2   . GLN A 1  878  ? 76.446  107.817 112.546 1.00 36.37  ? 878  GLN A NE2   1 
ATOM   6743  N  N     . GLU A 1  879  ? 81.181  111.253 112.253 1.00 30.01  ? 879  GLU A N     1 
ATOM   6744  C  CA    . GLU A 1  879  ? 82.082  111.957 111.347 1.00 31.54  ? 879  GLU A CA    1 
ATOM   6745  C  C     . GLU A 1  879  ? 83.096  111.003 110.735 1.00 29.74  ? 879  GLU A C     1 
ATOM   6746  O  O     . GLU A 1  879  ? 83.393  111.081 109.539 1.00 30.77  ? 879  GLU A O     1 
ATOM   6747  C  CB    . GLU A 1  879  ? 82.798  113.087 112.082 1.00 31.34  ? 879  GLU A CB    1 
ATOM   6748  C  CG    . GLU A 1  879  ? 81.873  114.033 112.806 1.00 31.72  ? 879  GLU A CG    1 
ATOM   6749  C  CD    . GLU A 1  879  ? 82.618  115.022 113.671 1.00 35.05  ? 879  GLU A CD    1 
ATOM   6750  O  OE1   . GLU A 1  879  ? 83.078  116.049 113.136 1.00 34.50  ? 879  GLU A OE1   1 
ATOM   6751  O  OE2   . GLU A 1  879  ? 82.758  114.770 114.883 1.00 34.63  ? 879  GLU A OE2   1 
ATOM   6752  N  N     . LEU A 1  880  ? 83.645  110.098 111.545 1.00 28.42  ? 880  LEU A N     1 
ATOM   6753  C  CA    . LEU A 1  880  ? 84.587  109.116 111.029 1.00 27.82  ? 880  LEU A CA    1 
ATOM   6754  C  C     . LEU A 1  880  ? 83.900  108.149 110.082 1.00 30.45  ? 880  LEU A C     1 
ATOM   6755  O  O     . LEU A 1  880  ? 84.498  107.699 109.100 1.00 31.05  ? 880  LEU A O     1 
ATOM   6756  C  CB    . LEU A 1  880  ? 85.239  108.360 112.184 1.00 32.18  ? 880  LEU A CB    1 
ATOM   6757  C  CG    . LEU A 1  880  ? 86.251  107.275 111.814 1.00 30.86  ? 880  LEU A CG    1 
ATOM   6758  C  CD1   . LEU A 1  880  ? 87.491  107.897 111.226 1.00 30.24  ? 880  LEU A CD1   1 
ATOM   6759  C  CD2   . LEU A 1  880  ? 86.594  106.425 113.010 1.00 30.34  ? 880  LEU A CD2   1 
ATOM   6760  N  N     . GLU A 1  881  ? 82.643  107.810 110.364 1.00 35.56  ? 881  GLU A N     1 
ATOM   6761  C  CA    . GLU A 1  881  ? 81.901  106.920 109.482 1.00 32.59  ? 881  GLU A CA    1 
ATOM   6762  C  C     . GLU A 1  881  ? 81.760  107.535 108.100 1.00 37.07  ? 881  GLU A C     1 
ATOM   6763  O  O     . GLU A 1  881  ? 81.867  106.840 107.085 1.00 41.41  ? 881  GLU A O     1 
ATOM   6764  C  CB    . GLU A 1  881  ? 80.522  106.637 110.075 1.00 35.31  ? 881  GLU A CB    1 
ATOM   6765  C  CG    . GLU A 1  881  ? 79.624  105.577 109.411 1.00 37.01  ? 881  GLU A CG    1 
ATOM   6766  C  CD    . GLU A 1  881  ? 80.324  104.282 109.022 1.00 40.32  ? 881  GLU A CD    1 
ATOM   6767  O  OE1   . GLU A 1  881  ? 81.319  104.304 108.284 1.00 37.85  ? 881  GLU A OE1   1 
ATOM   6768  O  OE2   . GLU A 1  881  ? 79.863  103.214 109.468 1.00 41.11  ? 881  GLU A OE2   1 
ATOM   6769  N  N     . ASP A 1  882  ? 81.516  108.845 108.046 1.00 34.84  ? 882  ASP A N     1 
ATOM   6770  C  CA    . ASP A 1  882  ? 81.283  109.518 106.775 1.00 30.69  ? 882  ASP A CA    1 
ATOM   6771  C  C     . ASP A 1  882  ? 82.575  109.737 106.006 1.00 34.85  ? 882  ASP A C     1 
ATOM   6772  O  O     . ASP A 1  882  ? 82.642  109.460 104.805 1.00 33.22  ? 882  ASP A O     1 
ATOM   6773  C  CB    . ASP A 1  882  ? 80.595  110.852 107.026 1.00 32.30  ? 882  ASP A CB    1 
ATOM   6774  C  CG    . ASP A 1  882  ? 79.106  110.719 107.121 1.00 38.50  ? 882  ASP A CG    1 
ATOM   6775  O  OD1   . ASP A 1  882  ? 78.621  109.575 107.229 1.00 38.82  ? 882  ASP A OD1   1 
ATOM   6776  O  OD2   . ASP A 1  882  ? 78.421  111.759 107.083 1.00 38.93  ? 882  ASP A OD2   1 
ATOM   6777  N  N     . LYS A 1  883  ? 83.612  110.229 106.683 1.00 34.34  ? 883  LYS A N     1 
ATOM   6778  C  CA    . LYS A 1  883  ? 84.805  110.703 105.996 1.00 29.71  ? 883  LYS A CA    1 
ATOM   6779  C  C     . LYS A 1  883  ? 85.663  109.566 105.461 1.00 33.33  ? 883  LYS A C     1 
ATOM   6780  O  O     . LYS A 1  883  ? 86.199  109.667 104.355 1.00 32.25  ? 883  LYS A O     1 
ATOM   6781  C  CB    . LYS A 1  883  ? 85.631  111.573 106.935 1.00 26.05  ? 883  LYS A CB    1 
ATOM   6782  C  CG    . LYS A 1  883  ? 85.074  112.955 107.126 1.00 30.14  ? 883  LYS A CG    1 
ATOM   6783  C  CD    . LYS A 1  883  ? 86.038  113.828 107.888 1.00 34.54  ? 883  LYS A CD    1 
ATOM   6784  C  CE    . LYS A 1  883  ? 85.296  114.844 108.727 1.00 35.17  ? 883  LYS A CE    1 
ATOM   6785  N  NZ    . LYS A 1  883  ? 83.850  114.525 108.834 1.00 33.87  ? 883  LYS A NZ    1 
ATOM   6786  N  N     . PHE A 1  884  ? 85.824  108.487 106.220 1.00 28.94  ? 884  PHE A N     1 
ATOM   6787  C  CA    . PHE A 1  884  ? 86.853  107.514 105.901 1.00 28.15  ? 884  PHE A CA    1 
ATOM   6788  C  C     . PHE A 1  884  ? 86.332  106.145 105.506 1.00 29.93  ? 884  PHE A C     1 
ATOM   6789  O  O     . PHE A 1  884  ? 87.136  105.291 105.123 1.00 31.97  ? 884  PHE A O     1 
ATOM   6790  C  CB    . PHE A 1  884  ? 87.818  107.366 107.082 1.00 27.34  ? 884  PHE A CB    1 
ATOM   6791  C  CG    . PHE A 1  884  ? 88.786  108.493 107.192 1.00 24.24  ? 884  PHE A CG    1 
ATOM   6792  C  CD1   . PHE A 1  884  ? 89.922  108.523 106.417 1.00 26.21  ? 884  PHE A CD1   1 
ATOM   6793  C  CD2   . PHE A 1  884  ? 88.541  109.538 108.049 1.00 23.30  ? 884  PHE A CD2   1 
ATOM   6794  C  CE1   . PHE A 1  884  ? 90.797  109.563 106.508 1.00 25.17  ? 884  PHE A CE1   1 
ATOM   6795  C  CE2   . PHE A 1  884  ? 89.415  110.578 108.141 1.00 27.01  ? 884  PHE A CE2   1 
ATOM   6796  C  CZ    . PHE A 1  884  ? 90.544  110.590 107.370 1.00 25.79  ? 884  PHE A CZ    1 
ATOM   6797  N  N     . LYS A 1  885  ? 85.032  105.909 105.569 1.00 29.74  ? 885  LYS A N     1 
ATOM   6798  C  CA    . LYS A 1  885  ? 84.496  104.610 105.203 1.00 33.13  ? 885  LYS A CA    1 
ATOM   6799  C  C     . LYS A 1  885  ? 83.982  104.645 103.773 1.00 33.70  ? 885  LYS A C     1 
ATOM   6800  O  O     . LYS A 1  885  ? 83.166  105.497 103.415 1.00 35.67  ? 885  LYS A O     1 
ATOM   6801  C  CB    . LYS A 1  885  ? 83.386  104.205 106.165 1.00 30.74  ? 885  LYS A CB    1 
ATOM   6802  C  CG    . LYS A 1  885  ? 82.415  103.175 105.626 1.00 30.63  ? 885  LYS A CG    1 
ATOM   6803  C  CD    . LYS A 1  885  ? 83.046  101.810 105.498 1.00 30.96  ? 885  LYS A CD    1 
ATOM   6804  C  CE    . LYS A 1  885  ? 81.999  100.715 105.564 1.00 35.17  ? 885  LYS A CE    1 
ATOM   6805  N  NZ    . LYS A 1  885  ? 81.210  100.763 106.821 1.00 33.88  ? 885  LYS A NZ    1 
ATOM   6806  N  N     . TYR A 1  886  ? 84.447  103.703 102.967 1.00 29.81  ? 886  TYR A N     1 
ATOM   6807  C  CA    . TYR A 1  886  ? 84.183  103.679 101.539 1.00 28.12  ? 886  TYR A CA    1 
ATOM   6808  C  C     . TYR A 1  886  ? 82.970  102.799 101.265 1.00 37.26  ? 886  TYR A C     1 
ATOM   6809  O  O     . TYR A 1  886  ? 82.876  101.684 101.789 1.00 39.44  ? 886  TYR A O     1 
ATOM   6810  C  CB    . TYR A 1  886  ? 85.412  103.169 100.791 1.00 28.33  ? 886  TYR A CB    1 
ATOM   6811  C  CG    . TYR A 1  886  ? 85.278  103.177 99.297  1.00 33.06  ? 886  TYR A CG    1 
ATOM   6812  C  CD1   . TYR A 1  886  ? 85.071  104.357 98.609  1.00 34.22  ? 886  TYR A CD1   1 
ATOM   6813  C  CD2   . TYR A 1  886  ? 85.397  102.008 98.569  1.00 32.91  ? 886  TYR A CD2   1 
ATOM   6814  C  CE1   . TYR A 1  886  ? 84.960  104.367 97.245  1.00 32.49  ? 886  TYR A CE1   1 
ATOM   6815  C  CE2   . TYR A 1  886  ? 85.292  102.014 97.207  1.00 32.67  ? 886  TYR A CE2   1 
ATOM   6816  C  CZ    . TYR A 1  886  ? 85.074  103.194 96.552  1.00 33.29  ? 886  TYR A CZ    1 
ATOM   6817  O  OH    . TYR A 1  886  ? 84.968  103.203 95.188  1.00 36.71  ? 886  TYR A OH    1 
ATOM   6818  N  N     . THR A 1  887  ? 82.038  103.309 100.461 1.00 39.14  ? 887  THR A N     1 
ATOM   6819  C  CA    . THR A 1  887  ? 80.823  102.587 100.108 1.00 36.14  ? 887  THR A CA    1 
ATOM   6820  C  C     . THR A 1  887  ? 80.727  102.296 98.619  1.00 36.69  ? 887  THR A C     1 
ATOM   6821  O  O     . THR A 1  887  ? 79.683  101.828 98.156  1.00 38.84  ? 887  THR A O     1 
ATOM   6822  C  CB    . THR A 1  887  ? 79.592  103.372 100.560 1.00 34.24  ? 887  THR A CB    1 
ATOM   6823  O  OG1   . THR A 1  887  ? 79.551  104.627 99.874  1.00 34.39  ? 887  THR A OG1   1 
ATOM   6824  C  CG2   . THR A 1  887  ? 79.643  103.622 102.055 1.00 32.60  ? 887  THR A CG2   1 
ATOM   6825  N  N     . GLY A 1  888  ? 81.787  102.568 97.857  1.00 36.87  ? 888  GLY A N     1 
ATOM   6826  C  CA    . GLY A 1  888  ? 81.731  102.356 96.421  1.00 37.72  ? 888  GLY A CA    1 
ATOM   6827  C  C     . GLY A 1  888  ? 81.608  100.896 96.036  1.00 39.05  ? 888  GLY A C     1 
ATOM   6828  O  O     . GLY A 1  888  ? 80.820  100.544 95.155  1.00 44.30  ? 888  GLY A O     1 
ATOM   6829  N  N     . ILE A 1  889  ? 82.377  100.028 96.683  1.00 35.50  ? 889  ILE A N     1 
ATOM   6830  C  CA    . ILE A 1  889  ? 82.376  98.600  96.394  1.00 39.72  ? 889  ILE A CA    1 
ATOM   6831  C  C     . ILE A 1  889  ? 81.987  97.850  97.657  1.00 43.47  ? 889  ILE A C     1 
ATOM   6832  O  O     . ILE A 1  889  ? 82.538  98.101  98.734  1.00 46.80  ? 889  ILE A O     1 
ATOM   6833  C  CB    . ILE A 1  889  ? 83.745  98.118  95.873  1.00 41.50  ? 889  ILE A CB    1 
ATOM   6834  C  CG1   . ILE A 1  889  ? 84.146  98.902  94.625  1.00 42.41  ? 889  ILE A CG1   1 
ATOM   6835  C  CG2   . ILE A 1  889  ? 83.724  96.627  95.604  1.00 38.86  ? 889  ILE A CG2   1 
ATOM   6836  C  CD1   . ILE A 1  889  ? 85.496  99.561  94.725  1.00 40.67  ? 889  ILE A CD1   1 
ATOM   6837  N  N     . GLN A 1  890  ? 81.037  96.929  97.523  1.00 46.65  ? 890  GLN A N     1 
ATOM   6838  C  CA    . GLN A 1  890  ? 80.526  96.148  98.648  1.00 46.21  ? 890  GLN A CA    1 
ATOM   6839  C  C     . GLN A 1  890  ? 81.339  94.864  98.759  1.00 48.84  ? 890  GLN A C     1 
ATOM   6840  O  O     . GLN A 1  890  ? 81.030  93.852  98.131  1.00 50.57  ? 890  GLN A O     1 
ATOM   6841  C  CB    . GLN A 1  890  ? 79.043  95.871  98.471  1.00 48.24  ? 890  GLN A CB    1 
ATOM   6842  C  CG    . GLN A 1  890  ? 78.193  97.120  98.532  1.00 49.50  ? 890  GLN A CG    1 
ATOM   6843  C  CD    . GLN A 1  890  ? 78.406  97.882  99.820  1.00 52.20  ? 890  GLN A CD    1 
ATOM   6844  O  OE1   . GLN A 1  890  ? 78.428  97.294  100.900 1.00 51.57  ? 890  GLN A OE1   1 
ATOM   6845  N  NE2   . GLN A 1  890  ? 78.565  99.194  99.717  1.00 49.81  ? 890  GLN A NE2   1 
ATOM   6846  N  N     . SER A 1  891  ? 82.397  94.918  99.560  1.00 43.19  ? 891  SER A N     1 
ATOM   6847  C  CA    . SER A 1  891  ? 83.286  93.797  99.809  1.00 40.66  ? 891  SER A CA    1 
ATOM   6848  C  C     . SER A 1  891  ? 83.733  93.839  101.262 1.00 41.56  ? 891  SER A C     1 
ATOM   6849  O  O     . SER A 1  891  ? 83.800  94.919  101.859 1.00 43.19  ? 891  SER A O     1 
ATOM   6850  C  CB    . SER A 1  891  ? 84.513  93.838  98.884  1.00 41.48  ? 891  SER A CB    1 
ATOM   6851  O  OG    . SER A 1  891  ? 85.258  92.636  98.956  1.00 42.50  ? 891  SER A OG    1 
ATOM   6852  N  N     . PRO A 1  892  ? 84.026  92.684  101.861 1.00 37.18  ? 892  PRO A N     1 
ATOM   6853  C  CA    . PRO A 1  892  ? 84.500  92.686  103.253 1.00 37.02  ? 892  PRO A CA    1 
ATOM   6854  C  C     . PRO A 1  892  ? 85.857  93.341  103.454 1.00 38.41  ? 892  PRO A C     1 
ATOM   6855  O  O     . PRO A 1  892  ? 86.176  93.712  104.590 1.00 40.23  ? 892  PRO A O     1 
ATOM   6856  C  CB    . PRO A 1  892  ? 84.541  91.194  103.610 1.00 37.66  ? 892  PRO A CB    1 
ATOM   6857  C  CG    . PRO A 1  892  ? 84.602  90.484  102.299 1.00 39.50  ? 892  PRO A CG    1 
ATOM   6858  C  CD    . PRO A 1  892  ? 83.794  91.319  101.364 1.00 37.68  ? 892  PRO A CD    1 
ATOM   6859  N  N     . LEU A 1  893  ? 86.675  93.489  102.407 1.00 34.17  ? 893  LEU A N     1 
ATOM   6860  C  CA    . LEU A 1  893  ? 87.983  94.111  102.592 1.00 32.42  ? 893  LEU A CA    1 
ATOM   6861  C  C     . LEU A 1  893  ? 87.865  95.579  102.964 1.00 32.46  ? 893  LEU A C     1 
ATOM   6862  O  O     . LEU A 1  893  ? 88.733  96.108  103.662 1.00 33.94  ? 893  LEU A O     1 
ATOM   6863  C  CB    . LEU A 1  893  ? 88.845  93.964  101.339 1.00 32.26  ? 893  LEU A CB    1 
ATOM   6864  C  CG    . LEU A 1  893  ? 89.088  92.557  100.807 1.00 35.49  ? 893  LEU A CG    1 
ATOM   6865  C  CD1   . LEU A 1  893  ? 89.994  92.608  99.602  1.00 31.98  ? 893  LEU A CD1   1 
ATOM   6866  C  CD2   . LEU A 1  893  ? 89.694  91.688  101.883 1.00 33.50  ? 893  LEU A CD2   1 
ATOM   6867  N  N     . PHE A 1  894  ? 86.819  96.255  102.510 1.00 31.41  ? 894  PHE A N     1 
ATOM   6868  C  CA    . PHE A 1  894  ? 86.633  97.646  102.880 1.00 31.70  ? 894  PHE A CA    1 
ATOM   6869  C  C     . PHE A 1  894  ? 85.970  97.818  104.233 1.00 30.32  ? 894  PHE A C     1 
ATOM   6870  O  O     . PHE A 1  894  ? 85.892  98.946  104.725 1.00 31.74  ? 894  PHE A O     1 
ATOM   6871  C  CB    . PHE A 1  894  ? 85.833  98.373  101.803 1.00 34.23  ? 894  PHE A CB    1 
ATOM   6872  C  CG    . PHE A 1  894  ? 86.545  98.453  100.488 1.00 35.50  ? 894  PHE A CG    1 
ATOM   6873  C  CD1   . PHE A 1  894  ? 87.851  98.897  100.429 1.00 30.77  ? 894  PHE A CD1   1 
ATOM   6874  C  CD2   . PHE A 1  894  ? 85.919  98.084  99.319  1.00 34.89  ? 894  PHE A CD2   1 
ATOM   6875  C  CE1   . PHE A 1  894  ? 88.512  98.975  99.237  1.00 30.20  ? 894  PHE A CE1   1 
ATOM   6876  C  CE2   . PHE A 1  894  ? 86.582  98.161  98.120  1.00 35.19  ? 894  PHE A CE2   1 
ATOM   6877  C  CZ    . PHE A 1  894  ? 87.880  98.607  98.080  1.00 33.07  ? 894  PHE A CZ    1 
ATOM   6878  N  N     . GLU A 1  895  ? 85.486  96.735  104.841 1.00 36.17  ? 895  GLU A N     1 
ATOM   6879  C  CA    . GLU A 1  895  ? 85.070  96.800  106.236 1.00 36.13  ? 895  GLU A CA    1 
ATOM   6880  C  C     . GLU A 1  895  ? 86.266  96.630  107.158 1.00 35.49  ? 895  GLU A C     1 
ATOM   6881  O  O     . GLU A 1  895  ? 86.346  97.267  108.213 1.00 35.35  ? 895  GLU A O     1 
ATOM   6882  C  CB    . GLU A 1  895  ? 84.018  95.730  106.524 1.00 34.20  ? 895  GLU A CB    1 
ATOM   6883  C  CG    . GLU A 1  895  ? 82.618  96.050  106.021 1.00 37.10  ? 895  GLU A CG    1 
ATOM   6884  C  CD    . GLU A 1  895  ? 81.875  97.050  106.887 1.00 40.30  ? 895  GLU A CD    1 
ATOM   6885  O  OE1   . GLU A 1  895  ? 82.526  97.853  107.587 1.00 39.18  ? 895  GLU A OE1   1 
ATOM   6886  O  OE2   . GLU A 1  895  ? 80.625  97.024  106.874 1.00 39.56  ? 895  GLU A OE2   1 
ATOM   6887  N  N     . GLU A 1  896  ? 87.205  95.771  106.769 1.00 33.22  ? 896  GLU A N     1 
ATOM   6888  C  CA    . GLU A 1  896  ? 88.433  95.593  107.530 1.00 30.08  ? 896  GLU A CA    1 
ATOM   6889  C  C     . GLU A 1  896  ? 89.277  96.856  107.519 1.00 31.84  ? 896  GLU A C     1 
ATOM   6890  O  O     . GLU A 1  896  ? 89.904  97.198  108.527 1.00 37.12  ? 896  GLU A O     1 
ATOM   6891  C  CB    . GLU A 1  896  ? 89.218  94.417  106.959 1.00 31.56  ? 896  GLU A CB    1 
ATOM   6892  C  CG    . GLU A 1  896  ? 90.608  94.242  107.519 1.00 33.63  ? 896  GLU A CG    1 
ATOM   6893  C  CD    . GLU A 1  896  ? 91.345  93.105  106.850 1.00 38.32  ? 896  GLU A CD    1 
ATOM   6894  O  OE1   . GLU A 1  896  ? 90.736  92.427  105.998 1.00 38.47  ? 896  GLU A OE1   1 
ATOM   6895  O  OE2   . GLU A 1  896  ? 92.530  92.883  107.176 1.00 39.29  ? 896  GLU A OE2   1 
ATOM   6896  N  N     . GLU A 1  897  ? 89.317  97.556  106.385 1.00 33.83  ? 897  GLU A N     1 
ATOM   6897  C  CA    . GLU A 1  897  ? 90.107  98.779  106.302 1.00 30.57  ? 897  GLU A CA    1 
ATOM   6898  C  C     . GLU A 1  897  ? 89.592  99.836  107.265 1.00 28.97  ? 897  GLU A C     1 
ATOM   6899  O  O     . GLU A 1  897  ? 90.380  100.523 107.920 1.00 35.18  ? 897  GLU A O     1 
ATOM   6900  C  CB    . GLU A 1  897  ? 90.099  99.315  104.873 1.00 28.69  ? 897  GLU A CB    1 
ATOM   6901  C  CG    . GLU A 1  897  ? 90.865  100.608 104.704 1.00 31.08  ? 897  GLU A CG    1 
ATOM   6902  C  CD    . GLU A 1  897  ? 90.239  101.544 103.695 1.00 35.40  ? 897  GLU A CD    1 
ATOM   6903  O  OE1   . GLU A 1  897  ? 89.076  101.948 103.886 1.00 36.37  ? 897  GLU A OE1   1 
ATOM   6904  O  OE2   . GLU A 1  897  ? 90.917  101.887 102.707 1.00 33.13  ? 897  GLU A OE2   1 
ATOM   6905  N  N     . PHE A 1  898  ? 88.274  99.988  107.361 1.00 27.90  ? 898  PHE A N     1 
ATOM   6906  C  CA    . PHE A 1  898  ? 87.718  101.000 108.250 1.00 27.61  ? 898  PHE A CA    1 
ATOM   6907  C  C     . PHE A 1  898  ? 87.876  100.623 109.716 1.00 28.48  ? 898  PHE A C     1 
ATOM   6908  O  O     . PHE A 1  898  ? 88.010  101.507 110.568 1.00 29.25  ? 898  PHE A O     1 
ATOM   6909  C  CB    . PHE A 1  898  ? 86.249  101.244 107.919 1.00 28.99  ? 898  PHE A CB    1 
ATOM   6910  C  CG    . PHE A 1  898  ? 85.602  102.264 108.794 1.00 29.54  ? 898  PHE A CG    1 
ATOM   6911  C  CD1   . PHE A 1  898  ? 86.053  103.564 108.808 1.00 28.98  ? 898  PHE A CD1   1 
ATOM   6912  C  CD2   . PHE A 1  898  ? 84.548  101.920 109.611 1.00 30.19  ? 898  PHE A CD2   1 
ATOM   6913  C  CE1   . PHE A 1  898  ? 85.470  104.494 109.613 1.00 28.61  ? 898  PHE A CE1   1 
ATOM   6914  C  CE2   . PHE A 1  898  ? 83.964  102.849 110.418 1.00 30.21  ? 898  PHE A CE2   1 
ATOM   6915  C  CZ    . PHE A 1  898  ? 84.424  104.138 110.420 1.00 28.65  ? 898  PHE A CZ    1 
ATOM   6916  N  N     . SER A 1  899  ? 87.865  99.327  110.032 1.00 29.74  ? 899  SER A N     1 
ATOM   6917  C  CA    . SER A 1  899  ? 88.019  98.906  111.420 1.00 29.93  ? 899  SER A CA    1 
ATOM   6918  C  C     . SER A 1  899  ? 89.394  99.266  111.962 1.00 31.27  ? 899  SER A C     1 
ATOM   6919  O  O     . SER A 1  899  ? 89.528  99.621  113.137 1.00 29.67  ? 899  SER A O     1 
ATOM   6920  C  CB    . SER A 1  899  ? 87.768  97.406  111.551 1.00 30.29  ? 899  SER A CB    1 
ATOM   6921  O  OG    . SER A 1  899  ? 86.413  97.102  111.292 1.00 37.70  ? 899  SER A OG    1 
ATOM   6922  N  N     . ARG A 1  900  ? 90.432  99.163  111.131 1.00 26.02  ? 900  ARG A N     1 
ATOM   6923  C  CA    . ARG A 1  900  ? 91.760  99.576  111.566 1.00 26.27  ? 900  ARG A CA    1 
ATOM   6924  C  C     . ARG A 1  900  ? 91.837  101.075 111.811 1.00 25.91  ? 900  ARG A C     1 
ATOM   6925  O  O     . ARG A 1  900  ? 92.522  101.510 112.738 1.00 28.35  ? 900  ARG A O     1 
ATOM   6926  C  CB    . ARG A 1  900  ? 92.811  99.166  110.543 1.00 20.76  ? 900  ARG A CB    1 
ATOM   6927  C  CG    . ARG A 1  900  ? 92.803  97.705  110.220 1.00 26.30  ? 900  ARG A CG    1 
ATOM   6928  C  CD    . ARG A 1  900  ? 94.198  97.165  110.246 1.00 25.93  ? 900  ARG A CD    1 
ATOM   6929  N  NE    . ARG A 1  900  ? 94.898  97.606  111.442 1.00 30.88  ? 900  ARG A NE    1 
ATOM   6930  C  CZ    . ARG A 1  900  ? 95.982  97.021  111.931 1.00 32.69  ? 900  ARG A CZ    1 
ATOM   6931  N  NH1   . ARG A 1  900  ? 96.538  95.983  111.329 1.00 29.16  ? 900  ARG A NH1   1 
ATOM   6932  N  NH2   . ARG A 1  900  ? 96.522  97.490  113.053 1.00 28.09  ? 900  ARG A NH2   1 
ATOM   6933  N  N     . LEU A 1  901  ? 91.159  101.877 110.996 1.00 20.10  ? 901  LEU A N     1 
ATOM   6934  C  CA    . LEU A 1  901  ? 91.145  103.316 111.226 1.00 19.81  ? 901  LEU A CA    1 
ATOM   6935  C  C     . LEU A 1  901  ? 90.512  103.650 112.569 1.00 25.46  ? 901  LEU A C     1 
ATOM   6936  O  O     . LEU A 1  901  ? 90.906  104.619 113.225 1.00 24.15  ? 901  LEU A O     1 
ATOM   6937  C  CB    . LEU A 1  901  ? 90.403  104.017 110.091 1.00 22.79  ? 901  LEU A CB    1 
ATOM   6938  C  CG    . LEU A 1  901  ? 91.137  104.127 108.759 1.00 23.40  ? 901  LEU A CG    1 
ATOM   6939  C  CD1   . LEU A 1  901  ? 90.149  104.307 107.632 1.00 28.54  ? 901  LEU A CD1   1 
ATOM   6940  C  CD2   . LEU A 1  901  ? 92.104  105.279 108.793 1.00 21.07  ? 901  LEU A CD2   1 
ATOM   6941  N  N     . LYS A 1  902  ? 89.514  102.867 112.985 1.00 24.27  ? 902  LYS A N     1 
ATOM   6942  C  CA    . LYS A 1  902  ? 88.936  103.036 114.313 1.00 22.66  ? 902  LYS A CA    1 
ATOM   6943  C  C     . LYS A 1  902  ? 89.892  102.565 115.397 1.00 26.10  ? 902  LYS A C     1 
ATOM   6944  O  O     . LYS A 1  902  ? 90.039  103.223 116.432 1.00 24.83  ? 902  LYS A O     1 
ATOM   6945  C  CB    . LYS A 1  902  ? 87.631  102.260 114.422 1.00 20.72  ? 902  LYS A CB    1 
ATOM   6946  C  CG    . LYS A 1  902  ? 86.460  102.877 113.722 1.00 26.58  ? 902  LYS A CG    1 
ATOM   6947  C  CD    . LYS A 1  902  ? 85.187  102.178 114.136 1.00 28.51  ? 902  LYS A CD    1 
ATOM   6948  C  CE    . LYS A 1  902  ? 84.456  102.962 115.205 1.00 30.08  ? 902  LYS A CE    1 
ATOM   6949  N  NZ    . LYS A 1  902  ? 85.181  102.959 116.493 1.00 29.61  ? 902  LYS A NZ    1 
ATOM   6950  N  N     . LYS A 1  903  ? 90.523  101.409 115.192 1.00 24.40  ? 903  LYS A N     1 
ATOM   6951  C  CA    . LYS A 1  903  ? 91.410  100.856 116.206 1.00 20.24  ? 903  LYS A CA    1 
ATOM   6952  C  C     . LYS A 1  903  ? 92.621  101.743 116.430 1.00 25.08  ? 903  LYS A C     1 
ATOM   6953  O  O     . LYS A 1  903  ? 93.031  101.962 117.574 1.00 28.34  ? 903  LYS A O     1 
ATOM   6954  C  CB    . LYS A 1  903  ? 91.848  99.453  115.807 1.00 22.67  ? 903  LYS A CB    1 
ATOM   6955  C  CG    . LYS A 1  903  ? 90.834  98.394  116.126 1.00 27.47  ? 903  LYS A CG    1 
ATOM   6956  C  CD    . LYS A 1  903  ? 91.398  97.019  115.868 1.00 29.26  ? 903  LYS A CD    1 
ATOM   6957  C  CE    . LYS A 1  903  ? 91.338  96.679  114.391 1.00 29.80  ? 903  LYS A CE    1 
ATOM   6958  N  NZ    . LYS A 1  903  ? 91.838  95.317  114.099 1.00 28.72  ? 903  LYS A NZ    1 
ATOM   6959  N  N     . ASP A 1  904  ? 93.214  102.255 115.352 1.00 21.51  ? 904  ASP A N     1 
ATOM   6960  C  CA    . ASP A 1  904  ? 94.331  103.176 115.500 1.00 12.05  ? 904  ASP A CA    1 
ATOM   6961  C  C     . ASP A 1  904  ? 93.911  104.431 116.234 1.00 17.26  ? 904  ASP A C     1 
ATOM   6962  O  O     . ASP A 1  904  ? 94.671  104.954 117.052 1.00 22.41  ? 904  ASP A O     1 
ATOM   6963  C  CB    . ASP A 1  904  ? 94.900  103.554 114.140 1.00 16.57  ? 904  ASP A CB    1 
ATOM   6964  C  CG    . ASP A 1  904  ? 95.527  102.392 113.430 1.00 24.16  ? 904  ASP A CG    1 
ATOM   6965  O  OD1   . ASP A 1  904  ? 95.793  101.369 114.082 1.00 31.54  ? 904  ASP A OD1   1 
ATOM   6966  O  OD2   . ASP A 1  904  ? 95.773  102.508 112.216 1.00 25.24  ? 904  ASP A OD2   1 
ATOM   6967  N  N     . ARG A 1  905  ? 92.712  104.931 115.949 1.00 17.19  ? 905  ARG A N     1 
ATOM   6968  C  CA    . ARG A 1  905  ? 92.220  106.132 116.609 1.00 16.74  ? 905  ARG A CA    1 
ATOM   6969  C  C     . ARG A 1  905  ? 92.060  105.906 118.106 1.00 18.06  ? 905  ARG A C     1 
ATOM   6970  O  O     . ARG A 1  905  ? 92.434  106.756 118.915 1.00 21.02  ? 905  ARG A O     1 
ATOM   6971  C  CB    . ARG A 1  905  ? 90.897  106.554 115.972 1.00 21.00  ? 905  ARG A CB    1 
ATOM   6972  C  CG    . ARG A 1  905  ? 90.461  107.971 116.266 1.00 20.42  ? 905  ARG A CG    1 
ATOM   6973  C  CD    . ARG A 1  905  ? 89.389  108.004 117.315 1.00 22.34  ? 905  ARG A CD    1 
ATOM   6974  N  NE    . ARG A 1  905  ? 88.226  107.195 116.974 1.00 28.79  ? 905  ARG A NE    1 
ATOM   6975  C  CZ    . ARG A 1  905  ? 87.084  107.677 116.509 1.00 29.08  ? 905  ARG A CZ    1 
ATOM   6976  N  NH1   . ARG A 1  905  ? 86.910  108.970 116.313 1.00 30.12  ? 905  ARG A NH1   1 
ATOM   6977  N  NH2   . ARG A 1  905  ? 86.085  106.841 116.251 1.00 24.60  ? 905  ARG A NH2   1 
ATOM   6978  N  N     . ASP A 1  906  ? 91.507  104.757 118.492 1.00 20.16  ? 906  ASP A N     1 
ATOM   6979  C  CA    . ASP A 1  906  ? 91.255  104.491 119.904 1.00 18.87  ? 906  ASP A CA    1 
ATOM   6980  C  C     . ASP A 1  906  ? 92.545  104.231 120.667 1.00 22.51  ? 906  ASP A C     1 
ATOM   6981  O  O     . ASP A 1  906  ? 92.696  104.680 121.807 1.00 21.77  ? 906  ASP A O     1 
ATOM   6982  C  CB    . ASP A 1  906  ? 90.298  103.314 120.048 1.00 17.99  ? 906  ASP A CB    1 
ATOM   6983  C  CG    . ASP A 1  906  ? 88.931  103.605 119.473 1.00 26.35  ? 906  ASP A CG    1 
ATOM   6984  O  OD1   . ASP A 1  906  ? 88.547  104.791 119.428 1.00 25.34  ? 906  ASP A OD1   1 
ATOM   6985  O  OD2   . ASP A 1  906  ? 88.228  102.650 119.084 1.00 25.28  ? 906  ASP A OD2   1 
ATOM   6986  N  N     . LYS A 1  907  ? 93.484  103.505 120.058 1.00 18.34  ? 907  LYS A N     1 
ATOM   6987  C  CA    . LYS A 1  907  ? 94.779  103.280 120.694 1.00 11.66  ? 907  LYS A CA    1 
ATOM   6988  C  C     . LYS A 1  907  ? 95.524  104.591 120.916 1.00 15.91  ? 907  LYS A C     1 
ATOM   6989  O  O     . LYS A 1  907  ? 96.121  104.797 121.975 1.00 19.05  ? 907  LYS A O     1 
ATOM   6990  C  CB    . LYS A 1  907  ? 95.610  102.326 119.845 1.00 12.34  ? 907  LYS A CB    1 
ATOM   6991  C  CG    . LYS A 1  907  ? 96.857  101.813 120.520 1.00 16.34  ? 907  LYS A CG    1 
ATOM   6992  C  CD    . LYS A 1  907  ? 96.533  100.788 121.572 1.00 20.02  ? 907  LYS A CD    1 
ATOM   6993  C  CE    . LYS A 1  907  ? 97.787  100.233 122.197 1.00 19.25  ? 907  LYS A CE    1 
ATOM   6994  N  NZ    . LYS A 1  907  ? 97.468  99.339  123.335 1.00 23.38  ? 907  LYS A NZ    1 
ATOM   6995  N  N     . TYR A 1  908  ? 95.495  105.488 119.928 1.00 13.69  ? 908  TYR A N     1 
ATOM   6996  C  CA    . TYR A 1  908  ? 96.066  106.820 120.096 1.00 11.53  ? 908  TYR A CA    1 
ATOM   6997  C  C     . TYR A 1  908  ? 95.399  107.572 121.238 1.00 16.37  ? 908  TYR A C     1 
ATOM   6998  O  O     . TYR A 1  908  ? 96.080  108.198 122.056 1.00 13.17  ? 908  TYR A O     1 
ATOM   6999  C  CB    . TYR A 1  908  ? 95.928  107.604 118.790 1.00 15.27  ? 908  TYR A CB    1 
ATOM   7000  C  CG    . TYR A 1  908  ? 96.666  108.927 118.733 1.00 16.03  ? 908  TYR A CG    1 
ATOM   7001  C  CD1   . TYR A 1  908  ? 96.239  110.010 119.475 1.00 16.17  ? 908  TYR A CD1   1 
ATOM   7002  C  CD2   . TYR A 1  908  ? 97.760  109.104 117.910 1.00 14.92  ? 908  TYR A CD2   1 
ATOM   7003  C  CE1   . TYR A 1  908  ? 96.890  111.211 119.431 1.00 16.17  ? 908  TYR A CE1   1 
ATOM   7004  C  CE2   . TYR A 1  908  ? 98.413  110.313 117.854 1.00 16.40  ? 908  TYR A CE2   1 
ATOM   7005  C  CZ    . TYR A 1  908  ? 97.969  111.362 118.619 1.00 14.57  ? 908  TYR A CZ    1 
ATOM   7006  O  OH    . TYR A 1  908  ? 98.600  112.577 118.591 1.00 12.83  ? 908  TYR A OH    1 
ATOM   7007  N  N     . ARG A 1  909  ? 94.064  107.540 121.297 1.00 17.55  ? 909  ARG A N     1 
ATOM   7008  C  CA    . ARG A 1  909  ? 93.336  108.235 122.353 1.00 16.07  ? 909  ARG A CA    1 
ATOM   7009  C  C     . ARG A 1  909  ? 93.719  107.698 123.721 1.00 16.01  ? 909  ARG A C     1 
ATOM   7010  O  O     . ARG A 1  909  ? 93.997  108.459 124.650 1.00 18.07  ? 909  ARG A O     1 
ATOM   7011  C  CB    . ARG A 1  909  ? 91.830  108.072 122.139 1.00 19.28  ? 909  ARG A CB    1 
ATOM   7012  C  CG    . ARG A 1  909  ? 91.260  108.740 120.917 1.00 15.79  ? 909  ARG A CG    1 
ATOM   7013  C  CD    . ARG A 1  909  ? 90.405  109.904 121.290 1.00 19.55  ? 909  ARG A CD    1 
ATOM   7014  N  NE    . ARG A 1  909  ? 89.476  110.285 120.233 1.00 23.13  ? 909  ARG A NE    1 
ATOM   7015  C  CZ    . ARG A 1  909  ? 88.291  109.730 120.029 1.00 21.09  ? 909  ARG A CZ    1 
ATOM   7016  N  NH1   . ARG A 1  909  ? 87.851  108.740 120.782 1.00 24.19  ? 909  ARG A NH1   1 
ATOM   7017  N  NH2   . ARG A 1  909  ? 87.522  110.189 119.052 1.00 14.79  ? 909  ARG A NH2   1 
ATOM   7018  N  N     . GLN A 1  910  ? 93.739  106.375 123.851 1.00 15.34  ? 910  GLN A N     1 
ATOM   7019  C  CA    . GLN A 1  910  ? 94.002  105.731 125.130 1.00 9.51   ? 910  GLN A CA    1 
ATOM   7020  C  C     . GLN A 1  910  ? 95.394  106.052 125.647 1.00 13.10  ? 910  GLN A C     1 
ATOM   7021  O  O     . GLN A 1  910  ? 95.577  106.301 126.841 1.00 21.26  ? 910  GLN A O     1 
ATOM   7022  C  CB    . GLN A 1  910  ? 93.808  104.229 124.960 1.00 12.84  ? 910  GLN A CB    1 
ATOM   7023  C  CG    . GLN A 1  910  ? 94.067  103.394 126.168 1.00 19.08  ? 910  GLN A CG    1 
ATOM   7024  C  CD    . GLN A 1  910  ? 94.941  102.211 125.842 1.00 25.08  ? 910  GLN A CD    1 
ATOM   7025  O  OE1   . GLN A 1  910  ? 94.640  101.439 124.934 1.00 24.17  ? 910  GLN A OE1   1 
ATOM   7026  N  NE2   . GLN A 1  910  ? 96.029  102.054 126.585 1.00 22.95  ? 910  GLN A NE2   1 
ATOM   7027  N  N     . ILE A 1  911  ? 96.390  106.043 124.765 1.00 13.33  ? 911  ILE A N     1 
ATOM   7028  C  CA    . ILE A 1  911  ? 97.765  106.263 125.192 1.00 11.27  ? 911  ILE A CA    1 
ATOM   7029  C  C     . ILE A 1  911  ? 97.966  107.698 125.654 1.00 15.16  ? 911  ILE A C     1 
ATOM   7030  O  O     . ILE A 1  911  ? 98.527  107.947 126.725 1.00 17.78  ? 911  ILE A O     1 
ATOM   7031  C  CB    . ILE A 1  911  ? 98.739  105.887 124.062 1.00 11.44  ? 911  ILE A CB    1 
ATOM   7032  C  CG1   . ILE A 1  911  ? 99.006  104.385 124.085 1.00 7.91   ? 911  ILE A CG1   1 
ATOM   7033  C  CG2   . ILE A 1  911  ? 100.029 106.657 124.184 1.00 8.94   ? 911  ILE A CG2   1 
ATOM   7034  C  CD1   . ILE A 1  911  ? 99.617  103.868 122.835 1.00 7.64   ? 911  ILE A CD1   1 
ATOM   7035  N  N     . PHE A 1  912  ? 97.504  108.662 124.867 1.00 9.36   ? 912  PHE A N     1 
ATOM   7036  C  CA    . PHE A 1  912  ? 97.793  110.056 125.163 1.00 7.94   ? 912  PHE A CA    1 
ATOM   7037  C  C     . PHE A 1  912  ? 96.806  110.680 126.135 1.00 17.32  ? 912  PHE A C     1 
ATOM   7038  O  O     . PHE A 1  912  ? 97.085  111.757 126.667 1.00 19.41  ? 912  PHE A O     1 
ATOM   7039  C  CB    . PHE A 1  912  ? 97.860  110.859 123.866 1.00 9.59   ? 912  PHE A CB    1 
ATOM   7040  C  CG    . PHE A 1  912  ? 99.094  110.588 123.064 1.00 14.35  ? 912  PHE A CG    1 
ATOM   7041  C  CD1   . PHE A 1  912  ? 100.322 111.028 123.501 1.00 15.02  ? 912  PHE A CD1   1 
ATOM   7042  C  CD2   . PHE A 1  912  ? 99.028  109.876 121.888 1.00 13.66  ? 912  PHE A CD2   1 
ATOM   7043  C  CE1   . PHE A 1  912  ? 101.447 110.771 122.779 1.00 10.86  ? 912  PHE A CE1   1 
ATOM   7044  C  CE2   . PHE A 1  912  ? 100.151 109.614 121.166 1.00 6.95   ? 912  PHE A CE2   1 
ATOM   7045  C  CZ    . PHE A 1  912  ? 101.360 110.067 121.606 1.00 7.35   ? 912  PHE A CZ    1 
ATOM   7046  N  N     . LEU A 1  913  ? 95.677  110.023 126.395 1.00 17.60  ? 913  LEU A N     1 
ATOM   7047  C  CA    . LEU A 1  913  ? 94.843  110.380 127.537 1.00 11.88  ? 913  LEU A CA    1 
ATOM   7048  C  C     . LEU A 1  913  ? 95.511  109.980 128.845 1.00 13.12  ? 913  LEU A C     1 
ATOM   7049  O  O     . LEU A 1  913  ? 95.424  110.700 129.840 1.00 14.22  ? 913  LEU A O     1 
ATOM   7050  C  CB    . LEU A 1  913  ? 93.482  109.702 127.412 1.00 12.28  ? 913  LEU A CB    1 
ATOM   7051  C  CG    . LEU A 1  913  ? 92.422  110.459 126.619 1.00 15.79  ? 913  LEU A CG    1 
ATOM   7052  C  CD1   . LEU A 1  913  ? 91.078  109.812 126.792 1.00 13.69  ? 913  LEU A CD1   1 
ATOM   7053  C  CD2   . LEU A 1  913  ? 92.382  111.895 127.051 1.00 18.79  ? 913  LEU A CD2   1 
ATOM   7054  N  N     . ASN A 1  914  ? 96.179  108.829 128.850 1.00 17.30  ? 914  ASN A N     1 
ATOM   7055  C  CA    . ASN A 1  914  ? 96.938  108.395 130.014 1.00 11.01  ? 914  ASN A CA    1 
ATOM   7056  C  C     . ASN A 1  914  ? 98.091  109.338 130.313 1.00 15.14  ? 914  ASN A C     1 
ATOM   7057  O  O     . ASN A 1  914  ? 98.385  109.615 131.478 1.00 20.30  ? 914  ASN A O     1 
ATOM   7058  C  CB    . ASN A 1  914  ? 97.461  106.984 129.778 1.00 13.49  ? 914  ASN A CB    1 
ATOM   7059  C  CG    . ASN A 1  914  ? 98.205  106.436 130.961 1.00 20.22  ? 914  ASN A CG    1 
ATOM   7060  O  OD1   . ASN A 1  914  ? 97.969  106.836 132.092 1.00 18.94  ? 914  ASN A OD1   1 
ATOM   7061  N  ND2   . ASN A 1  914  ? 99.142  105.541 130.702 1.00 22.15  ? 914  ASN A ND2   1 
ATOM   7062  N  N     . VAL A 1  915  ? 98.775  109.819 129.275 1.00 12.36  ? 915  VAL A N     1 
ATOM   7063  C  CA    . VAL A 1  915  ? 99.900  110.725 129.469 1.00 8.63   ? 915  VAL A CA    1 
ATOM   7064  C  C     . VAL A 1  915  ? 99.443  112.001 130.152 1.00 15.07  ? 915  VAL A C     1 
ATOM   7065  O  O     . VAL A 1  915  ? 100.184 112.601 130.936 1.00 14.90  ? 915  VAL A O     1 
ATOM   7066  C  CB    . VAL A 1  915  ? 100.579 111.002 128.115 1.00 13.28  ? 915  VAL A CB    1 
ATOM   7067  C  CG1   . VAL A 1  915  ? 101.599 112.096 128.232 1.00 12.92  ? 915  VAL A CG1   1 
ATOM   7068  C  CG2   . VAL A 1  915  ? 101.223 109.748 127.600 1.00 11.10  ? 915  VAL A CG2   1 
ATOM   7069  N  N     . GLU A 1  916  ? 98.215  112.428 129.876 1.00 19.32  ? 916  GLU A N     1 
ATOM   7070  C  CA    . GLU A 1  916  ? 97.628  113.578 130.550 1.00 17.22  ? 916  GLU A CA    1 
ATOM   7071  C  C     . GLU A 1  916  ? 97.410  113.324 132.036 1.00 17.80  ? 916  GLU A C     1 
ATOM   7072  O  O     . GLU A 1  916  ? 97.344  114.270 132.821 1.00 21.01  ? 916  GLU A O     1 
ATOM   7073  C  CB    . GLU A 1  916  ? 96.308  113.915 129.886 1.00 17.19  ? 916  GLU A CB    1 
ATOM   7074  C  CG    . GLU A 1  916  ? 95.987  115.364 129.834 1.00 24.06  ? 916  GLU A CG    1 
ATOM   7075  C  CD    . GLU A 1  916  ? 94.888  115.642 128.854 1.00 28.80  ? 916  GLU A CD    1 
ATOM   7076  O  OE1   . GLU A 1  916  ? 94.213  114.685 128.434 1.00 25.58  ? 916  GLU A OE1   1 
ATOM   7077  O  OE2   . GLU A 1  916  ? 94.697  116.813 128.505 1.00 27.11  ? 916  GLU A OE2   1 
ATOM   7078  N  N     . ASN A 1  917  ? 97.287  112.059 132.436 1.00 18.31  ? 917  ASN A N     1 
ATOM   7079  C  CA    . ASN A 1  917  ? 96.935  111.736 133.812 1.00 13.32  ? 917  ASN A CA    1 
ATOM   7080  C  C     . ASN A 1  917  ? 98.147  111.756 134.733 1.00 14.66  ? 917  ASN A C     1 
ATOM   7081  O  O     . ASN A 1  917  ? 98.013  112.025 135.930 1.00 21.66  ? 917  ASN A O     1 
ATOM   7082  C  CB    . ASN A 1  917  ? 96.246  110.378 133.876 1.00 17.23  ? 917  ASN A CB    1 
ATOM   7083  C  CG    . ASN A 1  917  ? 94.752  110.483 133.745 1.00 18.44  ? 917  ASN A CG    1 
ATOM   7084  O  OD1   . ASN A 1  917  ? 94.155  111.476 134.146 1.00 15.65  ? 917  ASN A OD1   1 
ATOM   7085  N  ND2   . ASN A 1  917  ? 94.134  109.453 133.187 1.00 16.36  ? 917  ASN A ND2   1 
ATOM   7086  N  N     . PHE A 1  918  ? 99.333  111.428 134.226 1.00 12.37  ? 918  PHE A N     1 
ATOM   7087  C  CA    . PHE A 1  918  ? 100.509 111.518 135.080 1.00 14.52  ? 918  PHE A CA    1 
ATOM   7088  C  C     . PHE A 1  918  ? 101.314 112.785 134.841 1.00 14.37  ? 918  PHE A C     1 
ATOM   7089  O  O     . PHE A 1  918  ? 102.470 112.861 135.258 1.00 18.85  ? 918  PHE A O     1 
ATOM   7090  C  CB    . PHE A 1  918  ? 101.386 110.256 134.976 1.00 13.12  ? 918  PHE A CB    1 
ATOM   7091  C  CG    . PHE A 1  918  ? 101.871 109.905 133.593 1.00 8.63   ? 918  PHE A CG    1 
ATOM   7092  C  CD1   . PHE A 1  918  ? 102.911 110.598 133.001 1.00 10.88  ? 918  PHE A CD1   1 
ATOM   7093  C  CD2   . PHE A 1  918  ? 101.342 108.817 132.924 1.00 11.92  ? 918  PHE A CD2   1 
ATOM   7094  C  CE1   . PHE A 1  918  ? 103.369 110.250 131.751 1.00 13.60  ? 918  PHE A CE1   1 
ATOM   7095  C  CE2   . PHE A 1  918  ? 101.801 108.464 131.678 1.00 11.77  ? 918  PHE A CE2   1 
ATOM   7096  C  CZ    . PHE A 1  918  ? 102.816 109.180 131.091 1.00 10.28  ? 918  PHE A CZ    1 
ATOM   7097  N  N     . ASN A 1  919  ? 100.713 113.794 134.226 1.00 13.71  ? 919  ASN A N     1 
ATOM   7098  C  CA    . ASN A 1  919  ? 101.332 115.097 134.069 1.00 15.94  ? 919  ASN A CA    1 
ATOM   7099  C  C     . ASN A 1  919  ? 100.484 116.166 134.739 1.00 20.06  ? 919  ASN A C     1 
ATOM   7100  O  O     . ASN A 1  919  ? 99.286  115.991 134.962 1.00 19.78  ? 919  ASN A O     1 
ATOM   7101  C  CB    . ASN A 1  919  ? 101.527 115.453 132.594 1.00 16.59  ? 919  ASN A CB    1 
ATOM   7102  C  CG    . ASN A 1  919  ? 102.729 114.782 131.992 1.00 13.65  ? 919  ASN A CG    1 
ATOM   7103  O  OD1   . ASN A 1  919  ? 102.609 113.952 131.102 1.00 18.97  ? 919  ASN A OD1   1 
ATOM   7104  N  ND2   . ASN A 1  919  ? 103.899 115.126 132.489 1.00 12.34  ? 919  ASN A ND2   1 
ATOM   7105  N  N     . PHE A 1  920  ? 101.125 117.289 135.053 1.00 24.18  ? 920  PHE A N     1 
ATOM   7106  C  CA    . PHE A 1  920  ? 100.397 118.431 135.591 1.00 21.58  ? 920  PHE A CA    1 
ATOM   7107  C  C     . PHE A 1  920  ? 99.494  119.046 134.528 1.00 25.10  ? 920  PHE A C     1 
ATOM   7108  O  O     . PHE A 1  920  ? 98.274  119.121 134.701 1.00 29.57  ? 920  PHE A O     1 
ATOM   7109  C  CB    . PHE A 1  920  ? 101.375 119.473 136.132 1.00 20.37  ? 920  PHE A CB    1 
ATOM   7110  C  CG    . PHE A 1  920  ? 101.830 119.214 137.532 1.00 20.16  ? 920  PHE A CG    1 
ATOM   7111  C  CD1   . PHE A 1  920  ? 103.042 118.609 137.777 1.00 24.57  ? 920  PHE A CD1   1 
ATOM   7112  C  CD2   . PHE A 1  920  ? 101.061 119.590 138.605 1.00 25.79  ? 920  PHE A CD2   1 
ATOM   7113  C  CE1   . PHE A 1  920  ? 103.467 118.376 139.063 1.00 22.63  ? 920  PHE A CE1   1 
ATOM   7114  C  CE2   . PHE A 1  920  ? 101.489 119.359 139.889 1.00 25.40  ? 920  PHE A CE2   1 
ATOM   7115  C  CZ    . PHE A 1  920  ? 102.686 118.749 140.117 1.00 19.74  ? 920  PHE A CZ    1 
ATOM   7116  N  N     . SER A 1  921  ? 100.071 119.480 133.411 1.00 26.38  ? 921  SER A N     1 
ATOM   7117  C  CA    . SER A 1  921  ? 99.331  120.249 132.417 1.00 28.50  ? 921  SER A CA    1 
ATOM   7118  C  C     . SER A 1  921  ? 99.757  119.891 130.992 1.00 30.38  ? 921  SER A C     1 
ATOM   7119  O  O     . SER A 1  921  ? 100.017 120.763 130.164 1.00 29.00  ? 921  SER A O     1 
ATOM   7120  C  CB    . SER A 1  921  ? 99.516  121.740 132.685 1.00 25.04  ? 921  SER A CB    1 
ATOM   7121  O  OG    . SER A 1  921  ? 98.953  122.526 131.654 1.00 30.78  ? 921  SER A OG    1 
ATOM   7122  N  N     . GLN A 1  922  ? 99.829  118.604 130.671 1.00 21.88  ? 922  GLN A N     1 
ATOM   7123  C  CA    . GLN A 1  922  ? 100.318 118.172 129.364 1.00 17.88  ? 922  GLN A CA    1 
ATOM   7124  C  C     . GLN A 1  922  ? 99.140  117.690 128.523 1.00 16.04  ? 922  GLN A C     1 
ATOM   7125  O  O     . GLN A 1  922  ? 98.807  116.504 128.532 1.00 17.61  ? 922  GLN A O     1 
ATOM   7126  C  CB    . GLN A 1  922  ? 101.380 117.086 129.512 1.00 18.16  ? 922  GLN A CB    1 
ATOM   7127  C  CG    . GLN A 1  922  ? 102.660 117.391 128.752 1.00 17.94  ? 922  GLN A CG    1 
ATOM   7128  C  CD    . GLN A 1  922  ? 102.652 116.869 127.342 1.00 22.64  ? 922  GLN A CD    1 
ATOM   7129  O  OE1   . GLN A 1  922  ? 101.973 115.895 127.031 1.00 22.07  ? 922  GLN A OE1   1 
ATOM   7130  N  NE2   . GLN A 1  922  ? 103.397 117.527 126.469 1.00 22.95  ? 922  GLN A NE2   1 
ATOM   7131  N  N     . LEU A 1  923  ? 98.557  118.602 127.760 1.00 21.13  ? 923  LEU A N     1 
ATOM   7132  C  CA    . LEU A 1  923  ? 97.311  118.405 127.037 1.00 21.17  ? 923  LEU A CA    1 
ATOM   7133  C  C     . LEU A 1  923  ? 97.527  117.562 125.784 1.00 20.03  ? 923  LEU A C     1 
ATOM   7134  O  O     . LEU A 1  923  ? 98.561  117.641 125.124 1.00 22.92  ? 923  LEU A O     1 
ATOM   7135  C  CB    . LEU A 1  923  ? 96.721  119.766 126.659 1.00 22.67  ? 923  LEU A CB    1 
ATOM   7136  C  CG    . LEU A 1  923  ? 95.510  120.349 127.392 1.00 26.32  ? 923  LEU A CG    1 
ATOM   7137  C  CD1   . LEU A 1  923  ? 94.294  119.483 127.234 1.00 26.04  ? 923  LEU A CD1   1 
ATOM   7138  C  CD2   . LEU A 1  923  ? 95.819  120.550 128.867 1.00 21.87  ? 923  LEU A CD2   1 
ATOM   7139  N  N     . LEU A 1  924  ? 96.522  116.760 125.455 1.00 17.45  ? 924  LEU A N     1 
ATOM   7140  C  CA    . LEU A 1  924  ? 96.572  115.933 124.261 1.00 18.20  ? 924  LEU A CA    1 
ATOM   7141  C  C     . LEU A 1  924  ? 96.588  116.792 123.002 1.00 20.69  ? 924  LEU A C     1 
ATOM   7142  O  O     . LEU A 1  924  ? 95.969  117.856 122.939 1.00 24.62  ? 924  LEU A O     1 
ATOM   7143  C  CB    . LEU A 1  924  ? 95.374  114.984 124.236 1.00 22.85  ? 924  LEU A CB    1 
ATOM   7144  C  CG    . LEU A 1  924  ? 95.246  113.973 123.104 1.00 22.88  ? 924  LEU A CG    1 
ATOM   7145  C  CD1   . LEU A 1  924  ? 94.677  112.685 123.616 1.00 20.09  ? 924  LEU A CD1   1 
ATOM   7146  C  CD2   . LEU A 1  924  ? 94.353  114.521 122.016 1.00 21.29  ? 924  LEU A CD2   1 
ATOM   7147  N  N     . THR A 1  925  ? 97.304  116.313 121.987 1.00 18.54  ? 925  THR A N     1 
ATOM   7148  C  CA    . THR A 1  925  ? 97.405  116.994 120.706 1.00 17.46  ? 925  THR A CA    1 
ATOM   7149  C  C     . THR A 1  925  ? 97.214  115.976 119.597 1.00 22.93  ? 925  THR A C     1 
ATOM   7150  O  O     . THR A 1  925  ? 97.512  114.795 119.768 1.00 27.25  ? 925  THR A O     1 
ATOM   7151  C  CB    . THR A 1  925  ? 98.762  117.690 120.533 1.00 20.81  ? 925  THR A CB    1 
ATOM   7152  O  OG1   . THR A 1  925  ? 99.216  118.182 121.794 1.00 25.00  ? 925  THR A OG1   1 
ATOM   7153  C  CG2   . THR A 1  925  ? 98.640  118.859 119.584 1.00 21.18  ? 925  THR A CG2   1 
ATOM   7154  N  N     . ASP A 1  926  ? 96.707  116.435 118.458 1.00 24.77  ? 926  ASP A N     1 
ATOM   7155  C  CA    . ASP A 1  926  ? 96.582  115.599 117.273 1.00 21.55  ? 926  ASP A CA    1 
ATOM   7156  C  C     . ASP A 1  926  ? 97.721  115.824 116.293 1.00 21.90  ? 926  ASP A C     1 
ATOM   7157  O  O     . ASP A 1  926  ? 97.629  115.399 115.140 1.00 19.52  ? 926  ASP A O     1 
ATOM   7158  C  CB    . ASP A 1  926  ? 95.246  115.849 116.581 1.00 22.33  ? 926  ASP A CB    1 
ATOM   7159  C  CG    . ASP A 1  926  ? 94.959  117.314 116.395 1.00 28.15  ? 926  ASP A CG    1 
ATOM   7160  O  OD1   . ASP A 1  926  ? 94.937  118.052 117.401 1.00 28.02  ? 926  ASP A OD1   1 
ATOM   7161  O  OD2   . ASP A 1  926  ? 94.764  117.733 115.237 1.00 28.73  ? 926  ASP A OD2   1 
ATOM   7162  N  N     . VAL A 1  927  ? 98.786  116.484 116.728 1.00 22.02  ? 927  VAL A N     1 
ATOM   7163  C  CA    . VAL A 1  927  ? 99.904  116.867 115.878 1.00 18.56  ? 927  VAL A CA    1 
ATOM   7164  C  C     . VAL A 1  927  ? 101.150 116.139 116.372 1.00 19.35  ? 927  VAL A C     1 
ATOM   7165  O  O     . VAL A 1  927  ? 101.505 116.234 117.553 1.00 15.64  ? 927  VAL A O     1 
ATOM   7166  C  CB    . VAL A 1  927  ? 100.096 118.389 115.883 1.00 15.22  ? 927  VAL A CB    1 
ATOM   7167  C  CG1   . VAL A 1  927  ? 101.498 118.741 115.532 1.00 18.95  ? 927  VAL A CG1   1 
ATOM   7168  C  CG2   . VAL A 1  927  ? 99.124  119.046 114.917 1.00 21.07  ? 927  VAL A CG2   1 
ATOM   7169  N  N     . ARG A 1  928  ? 101.811 115.415 115.468 1.00 15.13  ? 928  ARG A N     1 
ATOM   7170  C  CA    . ARG A 1  928  ? 102.971 114.590 115.778 1.00 10.36  ? 928  ARG A CA    1 
ATOM   7171  C  C     . ARG A 1  928  ? 104.113 114.899 114.818 1.00 6.75   ? 928  ARG A C     1 
ATOM   7172  O  O     . ARG A 1  928  ? 103.895 115.343 113.694 1.00 10.91  ? 928  ARG A O     1 
ATOM   7173  C  CB    . ARG A 1  928  ? 102.637 113.098 115.681 1.00 13.27  ? 928  ARG A CB    1 
ATOM   7174  C  CG    . ARG A 1  928  ? 101.621 112.582 116.665 1.00 14.23  ? 928  ARG A CG    1 
ATOM   7175  C  CD    . ARG A 1  928  ? 102.265 112.269 117.981 1.00 14.41  ? 928  ARG A CD    1 
ATOM   7176  N  NE    . ARG A 1  928  ? 101.634 113.007 119.061 1.00 13.29  ? 928  ARG A NE    1 
ATOM   7177  C  CZ    . ARG A 1  928  ? 102.229 113.317 120.198 1.00 14.82  ? 928  ARG A CZ    1 
ATOM   7178  N  NH1   . ARG A 1  928  ? 103.490 113.006 120.421 1.00 8.48   ? 928  ARG A NH1   1 
ATOM   7179  N  NH2   . ARG A 1  928  ? 101.545 113.967 121.129 1.00 20.47  ? 928  ARG A NH2   1 
ATOM   7180  N  N     . GLN A 1  929  ? 105.337 114.627 115.268 1.00 12.43  ? 929  GLN A N     1 
ATOM   7181  C  CA    . GLN A 1  929  ? 106.542 114.775 114.454 1.00 6.31   ? 929  GLN A CA    1 
ATOM   7182  C  C     . GLN A 1  929  ? 106.926 113.435 113.842 1.00 4.97   ? 929  GLN A C     1 
ATOM   7183  O  O     . GLN A 1  929  ? 107.164 112.469 114.564 1.00 15.18  ? 929  GLN A O     1 
ATOM   7184  C  CB    . GLN A 1  929  ? 107.693 115.313 115.293 1.00 3.53   ? 929  GLN A CB    1 
ATOM   7185  C  CG    . GLN A 1  929  ? 107.848 116.793 115.242 1.00 6.35   ? 929  GLN A CG    1 
ATOM   7186  C  CD    . GLN A 1  929  ? 108.711 117.306 116.347 1.00 14.51  ? 929  GLN A CD    1 
ATOM   7187  O  OE1   . GLN A 1  929  ? 108.795 116.700 117.408 1.00 14.50  ? 929  GLN A OE1   1 
ATOM   7188  N  NE2   . GLN A 1  929  ? 109.376 118.425 116.107 1.00 12.95  ? 929  GLN A NE2   1 
ATOM   7189  N  N     . VAL A 1  930  ? 107.007 113.385 112.518 1.00 4.50   ? 930  VAL A N     1 
ATOM   7190  C  CA    . VAL A 1  930  ? 107.124 112.118 111.800 1.00 5.71   ? 930  VAL A CA    1 
ATOM   7191  C  C     . VAL A 1  930  ? 108.277 112.223 110.813 1.00 4.38   ? 930  VAL A C     1 
ATOM   7192  O  O     . VAL A 1  930  ? 108.684 113.326 110.424 1.00 9.19   ? 930  VAL A O     1 
ATOM   7193  C  CB    . VAL A 1  930  ? 105.810 111.754 111.068 1.00 11.58  ? 930  VAL A CB    1 
ATOM   7194  C  CG1   . VAL A 1  930  ? 104.728 111.371 112.060 1.00 6.74   ? 930  VAL A CG1   1 
ATOM   7195  C  CG2   . VAL A 1  930  ? 105.370 112.883 110.178 1.00 5.92   ? 930  VAL A CG2   1 
ATOM   7196  N  N     . PRO A 1  931  ? 108.849 111.089 110.409 1.00 1.83   ? 931  PRO A N     1 
ATOM   7197  C  CA    . PRO A 1  931  ? 109.877 111.137 109.365 1.00 2.30   ? 931  PRO A CA    1 
ATOM   7198  C  C     . PRO A 1  931  ? 109.375 111.596 108.009 1.00 6.41   ? 931  PRO A C     1 
ATOM   7199  O  O     . PRO A 1  931  ? 110.120 112.268 107.289 1.00 9.64   ? 931  PRO A O     1 
ATOM   7200  C  CB    . PRO A 1  931  ? 110.383 109.690 109.318 1.00 0.82   ? 931  PRO A CB    1 
ATOM   7201  C  CG    . PRO A 1  931  ? 109.309 108.898 109.883 1.00 0.82   ? 931  PRO A CG    1 
ATOM   7202  C  CD    . PRO A 1  931  ? 108.701 109.731 110.945 1.00 3.82   ? 931  PRO A CD    1 
ATOM   7203  N  N     . VAL A 1  932  ? 108.146 111.250 107.627 1.00 9.28   ? 932  VAL A N     1 
ATOM   7204  C  CA    . VAL A 1  932  ? 107.637 111.470 106.278 1.00 5.10   ? 932  VAL A CA    1 
ATOM   7205  C  C     . VAL A 1  932  ? 106.263 112.117 106.361 1.00 7.69   ? 932  VAL A C     1 
ATOM   7206  O  O     . VAL A 1  932  ? 105.414 111.681 107.142 1.00 13.92  ? 932  VAL A O     1 
ATOM   7207  C  CB    . VAL A 1  932  ? 107.557 110.158 105.479 1.00 6.07   ? 932  VAL A CB    1 
ATOM   7208  C  CG1   . VAL A 1  932  ? 107.121 110.430 104.068 1.00 10.24  ? 932  VAL A CG1   1 
ATOM   7209  C  CG2   . VAL A 1  932  ? 108.874 109.442 105.492 1.00 4.62   ? 932  VAL A CG2   1 
ATOM   7210  N  N     . ASN A 1  933  ? 106.042 113.150 105.551 1.00 16.49  ? 933  ASN A N     1 
ATOM   7211  C  CA    . ASN A 1  933  ? 104.736 113.796 105.416 1.00 15.57  ? 933  ASN A CA    1 
ATOM   7212  C  C     . ASN A 1  933  ? 104.026 113.163 104.226 1.00 18.54  ? 933  ASN A C     1 
ATOM   7213  O  O     . ASN A 1  933  ? 104.312 113.490 103.076 1.00 25.42  ? 933  ASN A O     1 
ATOM   7214  C  CB    . ASN A 1  933  ? 104.906 115.299 105.240 1.00 10.78  ? 933  ASN A CB    1 
ATOM   7215  C  CG    . ASN A 1  933  ? 103.618 116.063 105.423 1.00 17.29  ? 933  ASN A CG    1 
ATOM   7216  O  OD1   . ASN A 1  933  ? 102.548 115.482 105.503 1.00 25.11  ? 933  ASN A OD1   1 
ATOM   7217  N  ND2   . ASN A 1  933  ? 103.723 117.372 105.522 1.00 18.98  ? 933  ASN A ND2   1 
ATOM   7218  N  N     . VAL A 1  934  ? 103.103 112.243 104.503 1.00 10.53  ? 934  VAL A N     1 
ATOM   7219  C  CA    . VAL A 1  934  ? 102.475 111.478 103.433 1.00 13.12  ? 934  VAL A CA    1 
ATOM   7220  C  C     . VAL A 1  934  ? 101.402 112.293 102.726 1.00 19.93  ? 934  VAL A C     1 
ATOM   7221  O  O     . VAL A 1  934  ? 101.120 112.060 101.549 1.00 21.22  ? 934  VAL A O     1 
ATOM   7222  C  CB    . VAL A 1  934  ? 101.916 110.159 103.989 1.00 15.46  ? 934  VAL A CB    1 
ATOM   7223  C  CG1   . VAL A 1  934  ? 101.421 109.276 102.871 1.00 17.66  ? 934  VAL A CG1   1 
ATOM   7224  C  CG2   . VAL A 1  934  ? 102.976 109.433 104.771 1.00 18.08  ? 934  VAL A CG2   1 
ATOM   7225  N  N     . ALA A 1  935  ? 100.790 113.254 103.415 1.00 20.55  ? 935  ALA A N     1 
ATOM   7226  C  CA    . ALA A 1  935  ? 99.797  114.107 102.774 1.00 18.77  ? 935  ALA A CA    1 
ATOM   7227  C  C     . ALA A 1  935  ? 100.420 114.929 101.651 1.00 26.41  ? 935  ALA A C     1 
ATOM   7228  O  O     . ALA A 1  935  ? 99.830  115.078 100.576 1.00 31.20  ? 935  ALA A O     1 
ATOM   7229  C  CB    . ALA A 1  935  ? 99.144  115.014 103.813 1.00 18.77  ? 935  ALA A CB    1 
ATOM   7230  N  N     . SER A 1  936  ? 101.621 115.467 101.880 1.00 19.68  ? 936  SER A N     1 
ATOM   7231  C  CA    . SER A 1  936  ? 102.286 116.261 100.853 1.00 17.12  ? 936  SER A CA    1 
ATOM   7232  C  C     . SER A 1  936  ? 102.801 115.408 99.710  1.00 20.54  ? 936  SER A C     1 
ATOM   7233  O  O     . SER A 1  936  ? 102.880 115.886 98.579  1.00 30.51  ? 936  SER A O     1 
ATOM   7234  C  CB    . SER A 1  936  ? 103.438 117.059 101.448 1.00 23.19  ? 936  SER A CB    1 
ATOM   7235  O  OG    . SER A 1  936  ? 103.080 117.618 102.692 1.00 28.91  ? 936  SER A OG    1 
ATOM   7236  N  N     . ILE A 1  937  ? 103.185 114.164 99.973  1.00 19.10  ? 937  ILE A N     1 
ATOM   7237  C  CA    . ILE A 1  937  ? 103.680 113.320 98.892  1.00 20.55  ? 937  ILE A CA    1 
ATOM   7238  C  C     . ILE A 1  937  ? 102.561 113.007 97.914  1.00 24.85  ? 937  ILE A C     1 
ATOM   7239  O  O     . ILE A 1  937  ? 102.767 112.983 96.696  1.00 27.81  ? 937  ILE A O     1 
ATOM   7240  C  CB    . ILE A 1  937  ? 104.318 112.041 99.459  1.00 17.57  ? 937  ILE A CB    1 
ATOM   7241  C  CG1   . ILE A 1  937  ? 105.669 112.364 100.083 1.00 19.24  ? 937  ILE A CG1   1 
ATOM   7242  C  CG2   . ILE A 1  937  ? 104.497 111.007 98.379  1.00 19.60  ? 937  ILE A CG2   1 
ATOM   7243  C  CD1   . ILE A 1  937  ? 106.375 111.174 100.624 1.00 24.21  ? 937  ILE A CD1   1 
ATOM   7244  N  N     . VAL A 1  938  ? 101.357 112.769 98.428  1.00 25.60  ? 938  VAL A N     1 
ATOM   7245  C  CA    . VAL A 1  938  ? 100.246 112.381 97.567  1.00 24.67  ? 938  VAL A CA    1 
ATOM   7246  C  C     . VAL A 1  938  ? 99.794  113.556 96.709  1.00 27.85  ? 938  VAL A C     1 
ATOM   7247  O  O     . VAL A 1  938  ? 99.592  113.414 95.499  1.00 28.26  ? 938  VAL A O     1 
ATOM   7248  C  CB    . VAL A 1  938  ? 99.094  111.811 98.410  1.00 24.59  ? 938  VAL A CB    1 
ATOM   7249  C  CG1   . VAL A 1  938  ? 97.768  111.988 97.703  1.00 23.51  ? 938  VAL A CG1   1 
ATOM   7250  C  CG2   . VAL A 1  938  ? 99.350  110.359 98.692  1.00 23.27  ? 938  VAL A CG2   1 
ATOM   7251  N  N     . LYS A 1  939  ? 99.644  114.737 97.311  1.00 29.21  ? 939  LYS A N     1 
ATOM   7252  C  CA    . LYS A 1  939  ? 99.117  115.861 96.546  1.00 31.97  ? 939  LYS A CA    1 
ATOM   7253  C  C     . LYS A 1  939  ? 100.107 116.352 95.496  1.00 31.20  ? 939  LYS A C     1 
ATOM   7254  O  O     . LYS A 1  939  ? 99.695  116.722 94.393  1.00 31.17  ? 939  LYS A O     1 
ATOM   7255  C  CB    . LYS A 1  939  ? 98.702  116.998 97.478  1.00 26.96  ? 939  LYS A CB    1 
ATOM   7256  C  CG    . LYS A 1  939  ? 99.826  117.793 98.057  1.00 27.04  ? 939  LYS A CG    1 
ATOM   7257  C  CD    . LYS A 1  939  ? 99.298  119.014 98.779  1.00 29.47  ? 939  LYS A CD    1 
ATOM   7258  C  CE    . LYS A 1  939  ? 98.785  120.053 97.807  1.00 31.09  ? 939  LYS A CE    1 
ATOM   7259  N  NZ    . LYS A 1  939  ? 98.406  121.303 98.510  1.00 31.55  ? 939  LYS A NZ    1 
ATOM   7260  N  N     . ASN A 1  940  ? 101.405 116.328 95.790  1.00 24.10  ? 940  ASN A N     1 
ATOM   7261  C  CA    . ASN A 1  940  ? 102.378 116.729 94.786  1.00 25.00  ? 940  ASN A CA    1 
ATOM   7262  C  C     . ASN A 1  940  ? 102.390 115.794 93.588  1.00 28.22  ? 940  ASN A C     1 
ATOM   7263  O  O     . ASN A 1  940  ? 102.950 116.153 92.550  1.00 32.26  ? 940  ASN A O     1 
ATOM   7264  C  CB    . ASN A 1  940  ? 103.778 116.810 95.398  1.00 23.30  ? 940  ASN A CB    1 
ATOM   7265  C  CG    . ASN A 1  940  ? 103.863 117.818 96.523  1.00 24.37  ? 940  ASN A CG    1 
ATOM   7266  O  OD1   . ASN A 1  940  ? 103.022 118.698 96.640  1.00 26.83  ? 940  ASN A OD1   1 
ATOM   7267  N  ND2   . ASN A 1  940  ? 104.881 117.693 97.355  1.00 23.26  ? 940  ASN A ND2   1 
ATOM   7268  N  N     . ILE A 1  941  ? 101.794 114.611 93.707  1.00 29.16  ? 941  ILE A N     1 
ATOM   7269  C  CA    . ILE A 1  941  ? 101.624 113.713 92.571  1.00 27.10  ? 941  ILE A CA    1 
ATOM   7270  C  C     . ILE A 1  941  ? 100.282 113.915 91.876  1.00 32.65  ? 941  ILE A C     1 
ATOM   7271  O  O     . ILE A 1  941  ? 100.197 113.730 90.652  1.00 32.84  ? 941  ILE A O     1 
ATOM   7272  C  CB    . ILE A 1  941  ? 101.807 112.246 93.013  1.00 25.46  ? 941  ILE A CB    1 
ATOM   7273  C  CG1   . ILE A 1  941  ? 103.283 111.867 92.943  1.00 29.75  ? 941  ILE A CG1   1 
ATOM   7274  C  CG2   . ILE A 1  941  ? 100.975 111.296 92.187  1.00 29.33  ? 941  ILE A CG2   1 
ATOM   7275  C  CD1   . ILE A 1  941  ? 103.548 110.398 93.059  1.00 27.42  ? 941  ILE A CD1   1 
ATOM   7276  N  N     . LEU A 1  942  ? 99.245  114.327 92.606  1.00 37.31  ? 942  LEU A N     1 
ATOM   7277  C  CA    . LEU A 1  942  ? 97.977  114.637 91.960  1.00 37.57  ? 942  LEU A CA    1 
ATOM   7278  C  C     . LEU A 1  942  ? 98.109  115.815 91.004  1.00 41.50  ? 942  LEU A C     1 
ATOM   7279  O  O     . LEU A 1  942  ? 97.511  115.803 89.924  1.00 39.80  ? 942  LEU A O     1 
ATOM   7280  C  CB    . LEU A 1  942  ? 96.906  114.928 93.008  1.00 37.06  ? 942  LEU A CB    1 
ATOM   7281  C  CG    . LEU A 1  942  ? 96.251  113.668 93.573  1.00 37.72  ? 942  LEU A CG    1 
ATOM   7282  C  CD1   . LEU A 1  942  ? 95.302  114.006 94.713  1.00 32.91  ? 942  LEU A CD1   1 
ATOM   7283  C  CD2   . LEU A 1  942  ? 95.562  112.882 92.474  1.00 39.54  ? 942  LEU A CD2   1 
ATOM   7284  N  N     . LEU A 1  943  ? 98.884  116.831 91.379  1.00 40.11  ? 943  LEU A N     1 
ATOM   7285  C  CA    . LEU A 1  943  ? 99.071  118.007 90.538  1.00 36.30  ? 943  LEU A CA    1 
ATOM   7286  C  C     . LEU A 1  943  ? 99.931  117.733 89.313  1.00 38.42  ? 943  LEU A C     1 
ATOM   7287  O  O     . LEU A 1  943  ? 99.669  118.298 88.245  1.00 40.77  ? 943  LEU A O     1 
ATOM   7288  C  CB    . LEU A 1  943  ? 99.689  119.149 91.352  1.00 33.80  ? 943  LEU A CB    1 
ATOM   7289  C  CG    . LEU A 1  943  ? 98.726  120.098 92.075  1.00 36.47  ? 943  LEU A CG    1 
ATOM   7290  C  CD1   . LEU A 1  943  ? 97.481  119.378 92.567  1.00 35.11  ? 943  LEU A CD1   1 
ATOM   7291  C  CD2   . LEU A 1  943  ? 99.403  120.824 93.234  1.00 35.29  ? 943  LEU A CD2   1 
ATOM   7292  N  N     . SER A 1  944  ? 100.945 116.881 89.432  1.00 34.65  ? 944  SER A N     1 
ATOM   7293  C  CA    . SER A 1  944  ? 101.893 116.649 88.355  1.00 37.04  ? 944  SER A CA    1 
ATOM   7294  C  C     . SER A 1  944  ? 101.580 115.399 87.552  1.00 39.54  ? 944  SER A C     1 
ATOM   7295  O  O     . SER A 1  944  ? 102.503 114.761 87.034  1.00 38.64  ? 944  SER A O     1 
ATOM   7296  C  CB    . SER A 1  944  ? 103.313 116.569 88.914  1.00 38.47  ? 944  SER A CB    1 
ATOM   7297  O  OG    . SER A 1  944  ? 103.525 115.331 89.568  1.00 41.10  ? 944  SER A OG    1 
ATOM   7298  N  N     . SER A 1  945  ? 100.310 115.031 87.448  1.00 43.07  ? 945  SER A N     1 
ATOM   7299  C  CA    . SER A 1  945  ? 99.876  113.888 86.663  1.00 44.83  ? 945  SER A CA    1 
ATOM   7300  C  C     . SER A 1  945  ? 99.217  114.364 85.378  1.00 46.44  ? 945  SER A C     1 
ATOM   7301  O  O     . SER A 1  945  ? 98.662  115.463 85.310  1.00 44.97  ? 945  SER A O     1 
ATOM   7302  C  CB    . SER A 1  945  ? 98.889  113.021 87.444  1.00 40.70  ? 945  SER A CB    1 
ATOM   7303  O  OG    . SER A 1  945  ? 97.678  113.723 87.668  1.00 43.81  ? 945  SER A OG    1 
ATOM   7304  N  N     . THR A 1  946  ? 99.282  113.517 84.354  1.00 48.96  ? 946  THR A N     1 
ATOM   7305  C  CA    . THR A 1  946  ? 98.640  113.799 83.080  1.00 46.60  ? 946  THR A CA    1 
ATOM   7306  C  C     . THR A 1  946  ? 97.189  113.336 83.028  1.00 45.94  ? 946  THR A C     1 
ATOM   7307  O  O     . THR A 1  946  ? 96.559  113.444 81.971  1.00 48.37  ? 946  THR A O     1 
ATOM   7308  C  CB    . THR A 1  946  ? 99.432  113.148 81.946  1.00 47.65  ? 946  THR A CB    1 
ATOM   7309  O  OG1   . THR A 1  946  ? 98.777  113.396 80.697  1.00 50.02  ? 946  THR A OG1   1 
ATOM   7310  C  CG2   . THR A 1  946  ? 99.547  111.653 82.170  1.00 46.16  ? 946  THR A CG2   1 
ATOM   7311  N  N     . SER A 1  947  ? 96.656  112.808 84.122  1.00 40.72  ? 947  SER A N     1 
ATOM   7312  C  CA    . SER A 1  947  ? 95.303  112.279 84.159  1.00 40.21  ? 947  SER A CA    1 
ATOM   7313  C  C     . SER A 1  947  ? 94.410  113.163 85.020  1.00 42.04  ? 947  SER A C     1 
ATOM   7314  O  O     . SER A 1  947  ? 94.887  113.951 85.839  1.00 43.66  ? 947  SER A O     1 
ATOM   7315  C  CB    . SER A 1  947  ? 95.302  110.847 84.694  1.00 40.45  ? 947  SER A CB    1 
ATOM   7316  O  OG    . SER A 1  947  ? 96.079  110.000 83.864  1.00 44.05  ? 947  SER A OG    1 
ATOM   7317  N  N     . GLY A 1  948  ? 93.103  113.039 84.812  1.00 38.96  ? 948  GLY A N     1 
ATOM   7318  C  CA    . GLY A 1  948  ? 92.152  113.807 85.588  1.00 37.70  ? 948  GLY A CA    1 
ATOM   7319  C  C     . GLY A 1  948  ? 91.423  112.972 86.616  1.00 38.93  ? 948  GLY A C     1 
ATOM   7320  O  O     . GLY A 1  948  ? 92.045  112.374 87.497  1.00 41.32  ? 948  GLY A O     1 
ATOM   7321  N  N     . VAL A 1  949  ? 90.097  112.931 86.517  1.00 36.83  ? 949  VAL A N     1 
ATOM   7322  C  CA    . VAL A 1  949  ? 89.289  112.067 87.371  1.00 36.96  ? 949  VAL A CA    1 
ATOM   7323  C  C     . VAL A 1  949  ? 89.211  110.695 86.708  1.00 40.88  ? 949  VAL A C     1 
ATOM   7324  O  O     . VAL A 1  949  ? 88.545  110.532 85.682  1.00 41.31  ? 949  VAL A O     1 
ATOM   7325  C  CB    . VAL A 1  949  ? 87.895  112.655 87.602  1.00 34.77  ? 949  VAL A CB    1 
ATOM   7326  C  CG1   . VAL A 1  949  ? 87.025  111.673 88.356  1.00 34.82  ? 949  VAL A CG1   1 
ATOM   7327  C  CG2   . VAL A 1  949  ? 87.998  113.963 88.352  1.00 34.81  ? 949  VAL A CG2   1 
ATOM   7328  N  N     . LEU A 1  950  ? 89.888  109.706 87.287  1.00 40.92  ? 950  LEU A N     1 
ATOM   7329  C  CA    . LEU A 1  950  ? 89.938  108.387 86.677  1.00 38.94  ? 950  LEU A CA    1 
ATOM   7330  C  C     . LEU A 1  950  ? 88.544  107.767 86.620  1.00 40.42  ? 950  LEU A C     1 
ATOM   7331  O  O     . LEU A 1  950  ? 87.703  108.023 87.485  1.00 44.22  ? 950  LEU A O     1 
ATOM   7332  C  CB    . LEU A 1  950  ? 90.869  107.461 87.455  1.00 38.63  ? 950  LEU A CB    1 
ATOM   7333  C  CG    . LEU A 1  950  ? 92.353  107.388 87.097  1.00 40.40  ? 950  LEU A CG    1 
ATOM   7334  C  CD1   . LEU A 1  950  ? 92.977  106.166 87.744  1.00 39.17  ? 950  LEU A CD1   1 
ATOM   7335  C  CD2   . LEU A 1  950  ? 92.558  107.350 85.600  1.00 40.04  ? 950  LEU A CD2   1 
ATOM   7336  N  N     . PRO A 1  951  ? 88.265  106.970 85.595  1.00 41.90  ? 951  PRO A N     1 
ATOM   7337  C  CA    . PRO A 1  951  ? 87.020  106.204 85.581  1.00 40.84  ? 951  PRO A CA    1 
ATOM   7338  C  C     . PRO A 1  951  ? 87.054  105.111 86.635  1.00 43.41  ? 951  PRO A C     1 
ATOM   7339  O  O     . PRO A 1  951  ? 88.113  104.631 87.040  1.00 43.99  ? 951  PRO A O     1 
ATOM   7340  C  CB    . PRO A 1  951  ? 86.985  105.612 84.172  1.00 40.52  ? 951  PRO A CB    1 
ATOM   7341  C  CG    . PRO A 1  951  ? 88.416  105.511 83.788  1.00 40.52  ? 951  PRO A CG    1 
ATOM   7342  C  CD    . PRO A 1  951  ? 89.089  106.702 84.405  1.00 42.22  ? 951  PRO A CD    1 
ATOM   7343  N  N     . PHE A 1  952  ? 85.866  104.718 87.081  1.00 40.78  ? 952  PHE A N     1 
ATOM   7344  C  CA    . PHE A 1  952  ? 85.769  103.674 88.087  1.00 39.30  ? 952  PHE A CA    1 
ATOM   7345  C  C     . PHE A 1  952  ? 86.324  102.366 87.540  1.00 43.77  ? 952  PHE A C     1 
ATOM   7346  O  O     . PHE A 1  952  ? 85.978  101.940 86.437  1.00 45.13  ? 952  PHE A O     1 
ATOM   7347  C  CB    . PHE A 1  952  ? 84.308  103.530 88.543  1.00 39.54  ? 952  PHE A CB    1 
ATOM   7348  C  CG    . PHE A 1  952  ? 84.046  102.368 89.479  1.00 43.49  ? 952  PHE A CG    1 
ATOM   7349  C  CD1   . PHE A 1  952  ? 83.569  102.602 90.756  1.00 43.51  ? 952  PHE A CD1   1 
ATOM   7350  C  CD2   . PHE A 1  952  ? 84.155  101.055 89.052  1.00 42.88  ? 952  PHE A CD2   1 
ATOM   7351  C  CE1   . PHE A 1  952  ? 83.306  101.555 91.612  1.00 43.06  ? 952  PHE A CE1   1 
ATOM   7352  C  CE2   . PHE A 1  952  ? 83.887  100.009 89.898  1.00 42.00  ? 952  PHE A CE2   1 
ATOM   7353  C  CZ    . PHE A 1  952  ? 83.456  100.258 91.179  1.00 42.97  ? 952  PHE A CZ    1 
ATOM   7354  N  N     . ASP A 1  953  ? 87.187  101.729 88.329  1.00 42.03  ? 953  ASP A N     1 
ATOM   7355  C  CA    . ASP A 1  953  ? 87.684  100.393 88.023  1.00 41.84  ? 953  ASP A CA    1 
ATOM   7356  C  C     . ASP A 1  953  ? 87.885  99.680  89.350  1.00 42.70  ? 953  ASP A C     1 
ATOM   7357  O  O     . ASP A 1  953  ? 88.786  100.042 90.110  1.00 47.47  ? 953  ASP A O     1 
ATOM   7358  C  CB    . ASP A 1  953  ? 88.984  100.444 87.232  1.00 43.25  ? 953  ASP A CB    1 
ATOM   7359  C  CG    . ASP A 1  953  ? 89.393  99.088  86.707  1.00 45.61  ? 953  ASP A CG    1 
ATOM   7360  O  OD1   . ASP A 1  953  ? 88.764  98.604  85.742  1.00 46.02  ? 953  ASP A OD1   1 
ATOM   7361  O  OD2   . ASP A 1  953  ? 90.333  98.492  87.265  1.00 45.81  ? 953  ASP A OD2   1 
ATOM   7362  N  N     . GLU A 1  954  ? 87.048  98.685  89.640  1.00 40.24  ? 954  GLU A N     1 
ATOM   7363  C  CA    . GLU A 1  954  ? 87.137  98.039  90.942  1.00 42.60  ? 954  GLU A CA    1 
ATOM   7364  C  C     . GLU A 1  954  ? 88.391  97.182  91.052  1.00 42.74  ? 954  GLU A C     1 
ATOM   7365  O  O     . GLU A 1  954  ? 88.943  97.032  92.146  1.00 44.26  ? 954  GLU A O     1 
ATOM   7366  C  CB    . GLU A 1  954  ? 85.879  97.217  91.231  1.00 42.70  ? 954  GLU A CB    1 
ATOM   7367  C  CG    . GLU A 1  954  ? 85.778  95.889  90.511  1.00 43.03  ? 954  GLU A CG    1 
ATOM   7368  C  CD    . GLU A 1  954  ? 85.105  96.004  89.164  1.00 47.97  ? 954  GLU A CD    1 
ATOM   7369  O  OE1   . GLU A 1  954  ? 84.979  97.138  88.650  1.00 48.42  ? 954  GLU A OE1   1 
ATOM   7370  O  OE2   . GLU A 1  954  ? 84.694  94.957  88.621  1.00 45.65  ? 954  GLU A OE2   1 
ATOM   7371  N  N     . LYS A 1  955  ? 88.866  96.616  89.940  1.00 39.80  ? 955  LYS A N     1 
ATOM   7372  C  CA    . LYS A 1  955  ? 90.117  95.865  90.000  1.00 41.00  ? 955  LYS A CA    1 
ATOM   7373  C  C     . LYS A 1  955  ? 91.273  96.771  90.394  1.00 44.75  ? 955  LYS A C     1 
ATOM   7374  O  O     . LYS A 1  955  ? 92.141  96.379  91.182  1.00 46.69  ? 955  LYS A O     1 
ATOM   7375  C  CB    . LYS A 1  955  ? 90.415  95.189  88.663  1.00 38.20  ? 955  LYS A CB    1 
ATOM   7376  C  CG    . LYS A 1  955  ? 91.727  94.414  88.685  1.00 40.33  ? 955  LYS A CG    1 
ATOM   7377  C  CD    . LYS A 1  955  ? 92.204  94.023  87.304  1.00 41.86  ? 955  LYS A CD    1 
ATOM   7378  C  CE    . LYS A 1  955  ? 92.336  92.518  87.172  1.00 41.37  ? 955  LYS A CE    1 
ATOM   7379  N  NZ    . LYS A 1  955  ? 92.422  92.077  85.752  1.00 41.38  ? 955  LYS A NZ    1 
ATOM   7380  N  N     . SER A 1  956  ? 91.298  97.989  89.854  1.00 39.79  ? 956  SER A N     1 
ATOM   7381  C  CA    . SER A 1  956  ? 92.325  98.952  90.227  1.00 36.57  ? 956  SER A CA    1 
ATOM   7382  C  C     . SER A 1  956  ? 92.255  99.286  91.709  1.00 37.19  ? 956  SER A C     1 
ATOM   7383  O  O     . SER A 1  956  ? 93.283  99.330  92.390  1.00 37.91  ? 956  SER A O     1 
ATOM   7384  C  CB    . SER A 1  956  ? 92.170  100.216 89.382  1.00 38.98  ? 956  SER A CB    1 
ATOM   7385  O  OG    . SER A 1  956  ? 92.632  101.364 90.064  1.00 42.40  ? 956  SER A OG    1 
ATOM   7386  N  N     . ILE A 1  957  ? 91.049  99.506  92.229  1.00 35.92  ? 957  ILE A N     1 
ATOM   7387  C  CA    . ILE A 1  957  ? 90.904  99.874  93.633  1.00 36.79  ? 957  ILE A CA    1 
ATOM   7388  C  C     . ILE A 1  957  ? 91.255  98.699  94.536  1.00 34.18  ? 957  ILE A C     1 
ATOM   7389  O  O     . ILE A 1  957  ? 91.744  98.883  95.656  1.00 36.80  ? 957  ILE A O     1 
ATOM   7390  C  CB    . ILE A 1  957  ? 89.484  100.399 93.896  1.00 34.20  ? 957  ILE A CB    1 
ATOM   7391  C  CG1   . ILE A 1  957  ? 89.185  101.562 92.955  1.00 35.36  ? 957  ILE A CG1   1 
ATOM   7392  C  CG2   . ILE A 1  957  ? 89.349  100.865 95.326  1.00 32.49  ? 957  ILE A CG2   1 
ATOM   7393  C  CD1   . ILE A 1  957  ? 87.766  102.045 93.016  1.00 35.33  ? 957  ILE A CD1   1 
ATOM   7394  N  N     . LEU A 1  958  ? 90.996  97.475  94.081  1.00 33.50  ? 958  LEU A N     1 
ATOM   7395  C  CA    . LEU A 1  958  ? 91.356  96.315  94.886  1.00 35.79  ? 958  LEU A CA    1 
ATOM   7396  C  C     . LEU A 1  958  ? 92.866  96.097  94.915  1.00 36.98  ? 958  LEU A C     1 
ATOM   7397  O  O     . LEU A 1  958  ? 93.411  95.668  95.936  1.00 37.97  ? 958  LEU A O     1 
ATOM   7398  C  CB    . LEU A 1  958  ? 90.629  95.074  94.376  1.00 35.41  ? 958  LEU A CB    1 
ATOM   7399  C  CG    . LEU A 1  958  ? 89.128  95.018  94.684  1.00 36.58  ? 958  LEU A CG    1 
ATOM   7400  C  CD1   . LEU A 1  958  ? 88.682  93.592  94.871  1.00 35.59  ? 958  LEU A CD1   1 
ATOM   7401  C  CD2   . LEU A 1  958  ? 88.772  95.841  95.910  1.00 35.76  ? 958  LEU A CD2   1 
ATOM   7402  N  N     . GLN A 1  959  ? 93.560  96.366  93.806  1.00 32.46  ? 959  GLN A N     1 
ATOM   7403  C  CA    . GLN A 1  959  ? 95.018  96.260  93.816  1.00 33.14  ? 959  GLN A CA    1 
ATOM   7404  C  C     . GLN A 1  959  ? 95.653  97.339  94.679  1.00 33.36  ? 959  GLN A C     1 
ATOM   7405  O  O     . GLN A 1  959  ? 96.634  97.078  95.380  1.00 35.97  ? 959  GLN A O     1 
ATOM   7406  C  CB    . GLN A 1  959  ? 95.584  96.329  92.399  1.00 33.80  ? 959  GLN A CB    1 
ATOM   7407  C  CG    . GLN A 1  959  ? 95.859  94.982  91.773  1.00 37.02  ? 959  GLN A CG    1 
ATOM   7408  C  CD    . GLN A 1  959  ? 97.174  94.953  91.013  1.00 36.33  ? 959  GLN A CD    1 
ATOM   7409  O  OE1   . GLN A 1  959  ? 98.229  95.238  91.572  1.00 35.93  ? 959  GLN A OE1   1 
ATOM   7410  N  NE2   . GLN A 1  959  ? 97.115  94.602  89.735  1.00 36.65  ? 959  GLN A NE2   1 
ATOM   7411  N  N     . LYS A 1  960  ? 95.123  98.559  94.631  1.00 28.34  ? 960  LYS A N     1 
ATOM   7412  C  CA    . LYS A 1  960  ? 95.696  99.625  95.441  1.00 28.65  ? 960  LYS A CA    1 
ATOM   7413  C  C     . LYS A 1  960  ? 95.519  99.350  96.926  1.00 33.12  ? 960  LYS A C     1 
ATOM   7414  O  O     . LYS A 1  960  ? 96.367  99.735  97.736  1.00 33.91  ? 960  LYS A O     1 
ATOM   7415  C  CB    . LYS A 1  960  ? 95.080  100.967 95.066  1.00 30.73  ? 960  LYS A CB    1 
ATOM   7416  C  CG    . LYS A 1  960  ? 95.675  101.588 93.826  1.00 33.52  ? 960  LYS A CG    1 
ATOM   7417  C  CD    . LYS A 1  960  ? 95.181  102.998 93.662  1.00 32.31  ? 960  LYS A CD    1 
ATOM   7418  C  CE    . LYS A 1  960  ? 93.730  103.018 93.241  1.00 29.95  ? 960  LYS A CE    1 
ATOM   7419  N  NZ    . LYS A 1  960  ? 93.242  104.412 93.129  1.00 30.99  ? 960  LYS A NZ    1 
ATOM   7420  N  N     . TYR A 1  961  ? 94.416  98.709  97.308  1.00 32.90  ? 961  TYR A N     1 
ATOM   7421  C  CA    . TYR A 1  961  ? 94.225  98.358  98.709  1.00 27.66  ? 961  TYR A CA    1 
ATOM   7422  C  C     . TYR A 1  961  ? 95.267  97.348  99.168  1.00 30.78  ? 961  TYR A C     1 
ATOM   7423  O  O     . TYR A 1  961  ? 95.789  97.447  100.283 1.00 31.12  ? 961  TYR A O     1 
ATOM   7424  C  CB    . TYR A 1  961  ? 92.821  97.801  98.932  1.00 29.42  ? 961  TYR A CB    1 
ATOM   7425  C  CG    . TYR A 1  961  ? 92.615  97.286  100.332 1.00 30.51  ? 961  TYR A CG    1 
ATOM   7426  C  CD1   . TYR A 1  961  ? 92.435  98.158  101.392 1.00 29.96  ? 961  TYR A CD1   1 
ATOM   7427  C  CD2   . TYR A 1  961  ? 92.654  95.931  100.603 1.00 30.21  ? 961  TYR A CD2   1 
ATOM   7428  C  CE1   . TYR A 1  961  ? 92.268  97.691  102.668 1.00 30.79  ? 961  TYR A CE1   1 
ATOM   7429  C  CE2   . TYR A 1  961  ? 92.494  95.459  101.879 1.00 29.64  ? 961  TYR A CE2   1 
ATOM   7430  C  CZ    . TYR A 1  961  ? 92.301  96.342  102.906 1.00 33.39  ? 961  TYR A CZ    1 
ATOM   7431  O  OH    . TYR A 1  961  ? 92.136  95.864  104.181 1.00 34.69  ? 961  TYR A OH    1 
ATOM   7432  N  N     . ALA A 1  962  ? 95.573  96.361  98.326  1.00 24.79  ? 962  ALA A N     1 
ATOM   7433  C  CA    . ALA A 1  962  ? 96.490  95.302  98.730  1.00 24.54  ? 962  ALA A CA    1 
ATOM   7434  C  C     . ALA A 1  962  ? 97.922  95.807  98.833  1.00 27.87  ? 962  ALA A C     1 
ATOM   7435  O  O     . ALA A 1  962  ? 98.682  95.349  99.691  1.00 31.48  ? 962  ALA A O     1 
ATOM   7436  C  CB    . ALA A 1  962  ? 96.401  94.135  97.753  1.00 26.25  ? 962  ALA A CB    1 
ATOM   7437  N  N     . MET A 1  963  ? 98.320  96.729  97.956  1.00 31.98  ? 963  MET A N     1 
ATOM   7438  C  CA    . MET A 1  963  ? 99.672  97.273  98.024  1.00 24.55  ? 963  MET A CA    1 
ATOM   7439  C  C     . MET A 1  963  ? 99.883  98.096  99.288  1.00 25.61  ? 963  MET A C     1 
ATOM   7440  O  O     . MET A 1  963  ? 100.948 98.022  99.906  1.00 28.92  ? 963  MET A O     1 
ATOM   7441  C  CB    . MET A 1  963  ? 99.976  98.097  96.772  1.00 23.43  ? 963  MET A CB    1 
ATOM   7442  C  CG    . MET A 1  963  ? 99.907  97.286  95.493  1.00 29.28  ? 963  MET A CG    1 
ATOM   7443  S  SD    . MET A 1  963  ? 99.927  98.212  93.943  1.00 48.54  ? 963  MET A SD    1 
ATOM   7444  C  CE    . MET A 1  963  ? 99.929  99.888  94.535  1.00 31.44  ? 963  MET A CE    1 
ATOM   7445  N  N     . VAL A 1  964  ? 98.890  98.885  99.689  1.00 19.41  ? 964  VAL A N     1 
ATOM   7446  C  CA    . VAL A 1  964  ? 99.020  99.656  100.917 1.00 17.31  ? 964  VAL A CA    1 
ATOM   7447  C  C     . VAL A 1  964  ? 99.011  98.736  102.131 1.00 25.94  ? 964  VAL A C     1 
ATOM   7448  O  O     . VAL A 1  964  ? 99.716  98.982  103.115 1.00 27.05  ? 964  VAL A O     1 
ATOM   7449  C  CB    . VAL A 1  964  ? 97.918  100.723 100.993 1.00 19.16  ? 964  VAL A CB    1 
ATOM   7450  C  CG1   . VAL A 1  964  ? 98.007  101.493 102.291 1.00 19.32  ? 964  VAL A CG1   1 
ATOM   7451  C  CG2   . VAL A 1  964  ? 98.034  101.664 99.824  1.00 20.99  ? 964  VAL A CG2   1 
ATOM   7452  N  N     . LYS A 1  965  ? 98.210  97.670  102.090 1.00 27.09  ? 965  LYS A N     1 
ATOM   7453  C  CA    . LYS A 1  965  ? 98.182  96.717  103.196 1.00 22.03  ? 965  LYS A CA    1 
ATOM   7454  C  C     . LYS A 1  965  ? 99.501  95.964  103.319 1.00 22.93  ? 965  LYS A C     1 
ATOM   7455  O  O     . LYS A 1  965  ? 99.977  95.708  104.429 1.00 29.21  ? 965  LYS A O     1 
ATOM   7456  C  CB    . LYS A 1  965  ? 97.028  95.735  103.015 1.00 21.78  ? 965  LYS A CB    1 
ATOM   7457  C  CG    . LYS A 1  965  ? 96.555  95.097  104.301 1.00 23.96  ? 965  LYS A CG    1 
ATOM   7458  C  CD    . LYS A 1  965  ? 95.650  93.913  104.041 1.00 27.48  ? 965  LYS A CD    1 
ATOM   7459  C  CE    . LYS A 1  965  ? 96.109  93.112  102.834 1.00 29.85  ? 965  LYS A CE    1 
ATOM   7460  N  NZ    . LYS A 1  965  ? 97.343  92.321  103.083 1.00 26.65  ? 965  LYS A NZ    1 
ATOM   7461  N  N     . THR A 1  966  ? 100.093 95.580  102.193 1.00 12.75  ? 966  THR A N     1 
ATOM   7462  C  CA    . THR A 1  966  ? 101.371 94.884  102.235 1.00 11.70  ? 966  THR A CA    1 
ATOM   7463  C  C     . THR A 1  966  ? 102.512 95.829  102.578 1.00 18.05  ? 966  THR A C     1 
ATOM   7464  O  O     . THR A 1  966  ? 103.516 95.402  103.150 1.00 23.09  ? 966  THR A O     1 
ATOM   7465  C  CB    . THR A 1  966  ? 101.633 94.193  100.898 1.00 15.26  ? 966  THR A CB    1 
ATOM   7466  O  OG1   . THR A 1  966  ? 100.476 93.441  100.519 1.00 21.05  ? 966  THR A OG1   1 
ATOM   7467  C  CG2   . THR A 1  966  ? 102.807 93.257  100.997 1.00 14.24  ? 966  THR A CG2   1 
ATOM   7468  N  N     . PHE A 1  967  ? 102.387 97.107  102.222 1.00 20.45  ? 967  PHE A N     1 
ATOM   7469  C  CA    . PHE A 1  967  ? 103.420 98.074  102.569 1.00 10.44  ? 967  PHE A CA    1 
ATOM   7470  C  C     . PHE A 1  967  ? 103.474 98.299  104.070 1.00 13.35  ? 967  PHE A C     1 
ATOM   7471  O  O     . PHE A 1  967  ? 104.557 98.387  104.652 1.00 21.57  ? 967  PHE A O     1 
ATOM   7472  C  CB    . PHE A 1  967  ? 103.172 99.390  101.835 1.00 9.20   ? 967  PHE A CB    1 
ATOM   7473  C  CG    . PHE A 1  967  ? 104.265 100.398 102.009 1.00 14.38  ? 967  PHE A CG    1 
ATOM   7474  C  CD1   . PHE A 1  967  ? 105.431 100.295 101.287 1.00 14.59  ? 967  PHE A CD1   1 
ATOM   7475  C  CD2   . PHE A 1  967  ? 104.125 101.449 102.888 1.00 14.80  ? 967  PHE A CD2   1 
ATOM   7476  C  CE1   . PHE A 1  967  ? 106.431 101.214 101.439 1.00 11.42  ? 967  PHE A CE1   1 
ATOM   7477  C  CE2   . PHE A 1  967  ? 105.126 102.366 103.042 1.00 8.66   ? 967  PHE A CE2   1 
ATOM   7478  C  CZ    . PHE A 1  967  ? 106.279 102.249 102.315 1.00 10.30  ? 967  PHE A CZ    1 
ATOM   7479  N  N     . CYS A 1  968  ? 102.315 98.398  104.716 1.00 13.49  ? 968  CYS A N     1 
ATOM   7480  C  CA    . CYS A 1  968  ? 102.292 98.581  106.159 1.00 8.47   ? 968  CYS A CA    1 
ATOM   7481  C  C     . CYS A 1  968  ? 102.781 97.343  106.890 1.00 15.89  ? 968  CYS A C     1 
ATOM   7482  O  O     . CYS A 1  968  ? 103.377 97.456  107.963 1.00 21.51  ? 968  CYS A O     1 
ATOM   7483  C  CB    . CYS A 1  968  ? 100.885 98.946  106.620 1.00 12.79  ? 968  CYS A CB    1 
ATOM   7484  S  SG    . CYS A 1  968  ? 100.389 100.629 106.260 1.00 27.41  ? 968  CYS A SG    1 
ATOM   7485  N  N     . LYS A 1  969  ? 102.538 96.160  106.336 1.00 16.06  ? 969  LYS A N     1 
ATOM   7486  C  CA    . LYS A 1  969  ? 102.941 94.934  107.009 1.00 10.92  ? 969  LYS A CA    1 
ATOM   7487  C  C     . LYS A 1  969  ? 104.452 94.773  107.000 1.00 13.88  ? 969  LYS A C     1 
ATOM   7488  O  O     . LYS A 1  969  ? 105.022 94.193  107.926 1.00 25.19  ? 969  LYS A O     1 
ATOM   7489  C  CB    . LYS A 1  969  ? 102.263 93.738  106.347 1.00 17.52  ? 969  LYS A CB    1 
ATOM   7490  C  CG    . LYS A 1  969  ? 102.449 92.428  107.069 1.00 22.46  ? 969  LYS A CG    1 
ATOM   7491  C  CD    . LYS A 1  969  ? 103.414 91.521  106.332 1.00 22.01  ? 969  LYS A CD    1 
ATOM   7492  C  CE    . LYS A 1  969  ? 102.863 91.101  104.985 1.00 23.30  ? 969  LYS A CE    1 
ATOM   7493  N  NZ    . LYS A 1  969  ? 103.815 90.235  104.243 1.00 20.01  ? 969  LYS A NZ    1 
ATOM   7494  N  N     . ASN A 1  970  ? 105.116 95.272  105.962 1.00 12.13  ? 970  ASN A N     1 
ATOM   7495  C  CA    . ASN A 1  970  ? 106.560 95.153  105.816 1.00 9.97   ? 970  ASN A CA    1 
ATOM   7496  C  C     . ASN A 1  970  ? 107.315 96.389  106.268 1.00 9.25   ? 970  ASN A C     1 
ATOM   7497  O  O     . ASN A 1  970  ? 108.534 96.440  106.105 1.00 13.11  ? 970  ASN A O     1 
ATOM   7498  C  CB    . ASN A 1  970  ? 106.924 94.863  104.364 1.00 12.31  ? 970  ASN A CB    1 
ATOM   7499  C  CG    . ASN A 1  970  ? 106.537 93.484  103.934 1.00 16.98  ? 970  ASN A CG    1 
ATOM   7500  O  OD1   . ASN A 1  970  ? 106.743 92.518  104.654 1.00 17.58  ? 970  ASN A OD1   1 
ATOM   7501  N  ND2   . ASN A 1  970  ? 105.962 93.382  102.757 1.00 15.84  ? 970  ASN A ND2   1 
ATOM   7502  N  N     . LEU A 1  971  ? 106.627 97.384  106.813 1.00 9.49   ? 971  LEU A N     1 
ATOM   7503  C  CA    . LEU A 1  971  ? 107.291 98.629  107.180 1.00 2.57   ? 971  LEU A CA    1 
ATOM   7504  C  C     . LEU A 1  971  ? 108.418 98.464  108.194 1.00 9.62   ? 971  LEU A C     1 
ATOM   7505  O  O     . LEU A 1  971  ? 109.441 99.150  108.039 1.00 10.00  ? 971  LEU A O     1 
ATOM   7506  C  CB    . LEU A 1  971  ? 106.252 99.636  107.677 1.00 5.41   ? 971  LEU A CB    1 
ATOM   7507  C  CG    . LEU A 1  971  ? 106.728 101.085 107.652 1.00 8.64   ? 971  LEU A CG    1 
ATOM   7508  C  CD1   . LEU A 1  971  ? 107.002 101.527 106.245 1.00 6.22   ? 971  LEU A CD1   1 
ATOM   7509  C  CD2   . LEU A 1  971  ? 105.731 101.995 108.314 1.00 10.25  ? 971  LEU A CD2   1 
ATOM   7510  N  N     . PRO A 1  972  ? 108.316 97.632  109.236 1.00 7.64   ? 972  PRO A N     1 
ATOM   7511  C  CA    . PRO A 1  972  ? 109.415 97.555  110.208 1.00 1.01   ? 972  PRO A CA    1 
ATOM   7512  C  C     . PRO A 1  972  ? 110.739 97.077  109.632 1.00 4.03   ? 972  PRO A C     1 
ATOM   7513  O  O     . PRO A 1  972  ? 111.758 97.209  110.311 1.00 16.70  ? 972  PRO A O     1 
ATOM   7514  C  CB    . PRO A 1  972  ? 108.881 96.578  111.258 1.00 0.05   ? 972  PRO A CB    1 
ATOM   7515  C  CG    . PRO A 1  972  ? 107.446 96.680  111.146 1.00 2.36   ? 972  PRO A CG    1 
ATOM   7516  C  CD    . PRO A 1  972  ? 107.162 96.848  109.706 1.00 5.89   ? 972  PRO A CD    1 
ATOM   7517  N  N     . TYR A 1  973  ? 110.764 96.524  108.423 1.00 15.85  ? 973  TYR A N     1 
ATOM   7518  C  CA    . TYR A 1  973  ? 112.016 96.104  107.811 1.00 9.56   ? 973  TYR A CA    1 
ATOM   7519  C  C     . TYR A 1  973  ? 112.877 97.277  107.382 1.00 2.72   ? 973  TYR A C     1 
ATOM   7520  O  O     . TYR A 1  973  ? 114.023 97.067  106.986 1.00 7.36   ? 973  TYR A O     1 
ATOM   7521  C  CB    . TYR A 1  973  ? 111.744 95.215  106.606 1.00 3.50   ? 973  TYR A CB    1 
ATOM   7522  C  CG    . TYR A 1  973  ? 111.283 93.825  106.950 1.00 11.49  ? 973  TYR A CG    1 
ATOM   7523  C  CD1   . TYR A 1  973  ? 112.086 92.967  107.665 1.00 6.38   ? 973  TYR A CD1   1 
ATOM   7524  C  CD2   . TYR A 1  973  ? 110.050 93.366  106.534 1.00 9.13   ? 973  TYR A CD2   1 
ATOM   7525  C  CE1   . TYR A 1  973  ? 111.668 91.704  107.972 1.00 3.19   ? 973  TYR A CE1   1 
ATOM   7526  C  CE2   . TYR A 1  973  ? 109.623 92.103  106.835 1.00 8.00   ? 973  TYR A CE2   1 
ATOM   7527  C  CZ    . TYR A 1  973  ? 110.437 91.275  107.552 1.00 7.93   ? 973  TYR A CZ    1 
ATOM   7528  O  OH    . TYR A 1  973  ? 110.021 90.008  107.861 1.00 11.83  ? 973  TYR A OH    1 
ATOM   7529  N  N     . VAL A 1  974  ? 112.349 98.500  107.432 1.00 3.97   ? 974  VAL A N     1 
ATOM   7530  C  CA    . VAL A 1  974  ? 113.176 99.681  107.227 1.00 2.30   ? 974  VAL A CA    1 
ATOM   7531  C  C     . VAL A 1  974  ? 114.238 99.760  108.307 1.00 1.43   ? 974  VAL A C     1 
ATOM   7532  O  O     . VAL A 1  974  ? 115.268 100.418 108.136 1.00 5.58   ? 974  VAL A O     1 
ATOM   7533  C  CB    . VAL A 1  974  ? 112.292 100.943 107.192 1.00 0.59   ? 974  VAL A CB    1 
ATOM   7534  C  CG1   . VAL A 1  974  ? 112.061 101.487 108.590 1.00 1.30   ? 974  VAL A CG1   1 
ATOM   7535  C  CG2   . VAL A 1  974  ? 112.891 101.993 106.303 1.00 4.85   ? 974  VAL A CG2   1 
ATOM   7536  N  N     . PHE A 1  975  ? 114.017 99.077  109.424 1.00 1.89   ? 975  PHE A N     1 
ATOM   7537  C  CA    . PHE A 1  975  ? 114.963 99.022  110.523 1.00 0.79   ? 975  PHE A CA    1 
ATOM   7538  C  C     . PHE A 1  975  ? 115.917 97.846  110.430 1.00 2.15   ? 975  PHE A C     1 
ATOM   7539  O  O     . PHE A 1  975  ? 116.792 97.729  111.288 1.00 9.86   ? 975  PHE A O     1 
ATOM   7540  C  CB    . PHE A 1  975  ? 114.222 98.944  111.856 1.00 4.69   ? 975  PHE A CB    1 
ATOM   7541  C  CG    . PHE A 1  975  ? 113.434 100.163 112.184 1.00 1.94   ? 975  PHE A CG    1 
ATOM   7542  C  CD1   . PHE A 1  975  ? 114.063 101.321 112.582 1.00 2.27   ? 975  PHE A CD1   1 
ATOM   7543  C  CD2   . PHE A 1  975  ? 112.059 100.151 112.107 1.00 2.29   ? 975  PHE A CD2   1 
ATOM   7544  C  CE1   . PHE A 1  975  ? 113.335 102.435 112.882 1.00 12.64  ? 975  PHE A CE1   1 
ATOM   7545  C  CE2   . PHE A 1  975  ? 111.334 101.265 112.408 1.00 0.51   ? 975  PHE A CE2   1 
ATOM   7546  C  CZ    . PHE A 1  975  ? 111.971 102.404 112.795 1.00 10.03  ? 975  PHE A CZ    1 
ATOM   7547  N  N     . ILE A 1  976  ? 115.773 96.963  109.444 1.00 3.24   ? 976  ILE A N     1 
ATOM   7548  C  CA    . ILE A 1  976  ? 116.717 95.859  109.346 1.00 0.68   ? 976  ILE A CA    1 
ATOM   7549  C  C     . ILE A 1  976  ? 117.504 95.922  108.043 1.00 4.06   ? 976  ILE A C     1 
ATOM   7550  O  O     . ILE A 1  976  ? 118.591 96.501  108.013 1.00 10.40  ? 976  ILE A O     1 
ATOM   7551  C  CB    . ILE A 1  976  ? 115.960 94.523  109.478 1.00 1.84   ? 976  ILE A CB    1 
ATOM   7552  C  CG1   . ILE A 1  976  ? 115.078 94.556  110.726 1.00 4.08   ? 976  ILE A CG1   1 
ATOM   7553  C  CG2   . ILE A 1  976  ? 116.918 93.357  109.521 1.00 2.47   ? 976  ILE A CG2   1 
ATOM   7554  C  CD1   . ILE A 1  976  ? 113.931 93.621  110.713 1.00 10.98  ? 976  ILE A CD1   1 
ATOM   7555  N  N     . ASN A 1  977  ? 116.918 95.448  106.944 1.00 0.46   ? 977  ASN A N     1 
ATOM   7556  C  CA    . ASN A 1  977  ? 117.479 95.553  105.597 1.00 6.18   ? 977  ASN A CA    1 
ATOM   7557  C  C     . ASN A 1  977  ? 116.589 94.826  104.605 1.00 0.80   ? 977  ASN A C     1 
ATOM   7558  O  O     . ASN A 1  977  ? 115.598 94.209  104.995 1.00 6.53   ? 977  ASN A O     1 
ATOM   7559  C  CB    . ASN A 1  977  ? 118.927 95.046  105.491 1.00 2.96   ? 977  ASN A CB    1 
ATOM   7560  C  CG    . ASN A 1  977  ? 119.112 93.616  105.924 1.00 6.57   ? 977  ASN A CG    1 
ATOM   7561  O  OD1   . ASN A 1  977  ? 118.303 92.752  105.642 1.00 18.55  ? 977  ASN A OD1   1 
ATOM   7562  N  ND2   . ASN A 1  977  ? 120.226 93.352  106.562 1.00 5.76   ? 977  ASN A ND2   1 
ATOM   7563  N  N     . ASN A 1  978  ? 116.931 94.894  103.320 1.00 10.08  ? 978  ASN A N     1 
ATOM   7564  C  CA    . ASN A 1  978  ? 116.139 94.260  102.275 1.00 6.96   ? 978  ASN A CA    1 
ATOM   7565  C  C     . ASN A 1  978  ? 116.413 92.769  102.130 1.00 11.55  ? 978  ASN A C     1 
ATOM   7566  O  O     . ASN A 1  978  ? 115.638 92.082  101.463 1.00 13.87  ? 978  ASN A O     1 
ATOM   7567  C  CB    . ASN A 1  978  ? 116.372 94.965  100.935 1.00 2.98   ? 978  ASN A CB    1 
ATOM   7568  C  CG    . ASN A 1  978  ? 117.767 94.743  100.371 1.00 11.33  ? 978  ASN A CG    1 
ATOM   7569  O  OD1   . ASN A 1  978  ? 118.667 94.271  101.053 1.00 13.73  ? 978  ASN A OD1   1 
ATOM   7570  N  ND2   . ASN A 1  978  ? 117.948 95.101  99.114  1.00 12.12  ? 978  ASN A ND2   1 
ATOM   7571  N  N     . ILE A 1  979  ? 117.491 92.255  102.722 1.00 11.16  ? 979  ILE A N     1 
ATOM   7572  C  CA    . ILE A 1  979  ? 117.740 90.818  102.696 1.00 9.27   ? 979  ILE A CA    1 
ATOM   7573  C  C     . ILE A 1  979  ? 116.728 90.090  103.566 1.00 13.19  ? 979  ILE A C     1 
ATOM   7574  O  O     . ILE A 1  979  ? 116.175 89.060  103.172 1.00 20.12  ? 979  ILE A O     1 
ATOM   7575  C  CB    . ILE A 1  979  ? 119.176 90.509  103.150 1.00 11.90  ? 979  ILE A CB    1 
ATOM   7576  C  CG1   . ILE A 1  979  ? 120.199 91.298  102.344 1.00 8.81   ? 979  ILE A CG1   1 
ATOM   7577  C  CG2   . ILE A 1  979  ? 119.453 89.027  103.072 1.00 11.00  ? 979  ILE A CG2   1 
ATOM   7578  C  CD1   . ILE A 1  979  ? 121.530 91.361  103.020 1.00 11.13  ? 979  ILE A CD1   1 
ATOM   7579  N  N     . GLN A 1  980  ? 116.480 90.607  104.770 1.00 11.18  ? 980  GLN A N     1 
ATOM   7580  C  CA    . GLN A 1  980  ? 115.540 89.965  105.675 1.00 8.49   ? 980  GLN A CA    1 
ATOM   7581  C  C     . GLN A 1  980  ? 114.096 90.195  105.271 1.00 9.64   ? 980  GLN A C     1 
ATOM   7582  O  O     . GLN A 1  980  ? 113.238 89.382  105.610 1.00 13.25  ? 980  GLN A O     1 
ATOM   7583  C  CB    . GLN A 1  980  ? 115.754 90.456  107.101 1.00 4.85   ? 980  GLN A CB    1 
ATOM   7584  C  CG    . GLN A 1  980  ? 117.165 90.322  107.606 1.00 10.14  ? 980  GLN A CG    1 
ATOM   7585  C  CD    . GLN A 1  980  ? 117.673 88.904  107.588 1.00 11.55  ? 980  GLN A CD    1 
ATOM   7586  O  OE1   . GLN A 1  980  ? 116.974 87.981  107.965 1.00 14.78  ? 980  GLN A OE1   1 
ATOM   7587  N  NE2   . GLN A 1  980  ? 118.905 88.728  107.156 1.00 10.18  ? 980  GLN A NE2   1 
ATOM   7588  N  N     . GLU A 1  981  ? 113.803 91.290  104.579 1.00 11.42  ? 981  GLU A N     1 
ATOM   7589  C  CA    . GLU A 1  981  ? 112.446 91.517  104.104 1.00 11.39  ? 981  GLU A CA    1 
ATOM   7590  C  C     . GLU A 1  981  ? 112.074 90.531  103.012 1.00 14.73  ? 981  GLU A C     1 
ATOM   7591  O  O     . GLU A 1  981  ? 110.926 90.087  102.935 1.00 18.98  ? 981  GLU A O     1 
ATOM   7592  C  CB    . GLU A 1  981  ? 112.300 92.943  103.601 1.00 8.79   ? 981  GLU A CB    1 
ATOM   7593  C  CG    . GLU A 1  981  ? 110.946 93.242  103.048 1.00 9.76   ? 981  GLU A CG    1 
ATOM   7594  C  CD    . GLU A 1  981  ? 110.793 94.686  102.695 1.00 16.96  ? 981  GLU A CD    1 
ATOM   7595  O  OE1   . GLU A 1  981  ? 111.741 95.451  102.942 1.00 12.39  ? 981  GLU A OE1   1 
ATOM   7596  O  OE2   . GLU A 1  981  ? 109.726 95.062  102.182 1.00 19.54  ? 981  GLU A OE2   1 
ATOM   7597  N  N     . ARG A 1  982  ? 113.032 90.190  102.151 1.00 18.53  ? 982  ARG A N     1 
ATOM   7598  C  CA    . ARG A 1  982  ? 112.790 89.201  101.110 1.00 13.17  ? 982  ARG A CA    1 
ATOM   7599  C  C     . ARG A 1  982  ? 112.531 87.827  101.705 1.00 16.08  ? 982  ARG A C     1 
ATOM   7600  O  O     . ARG A 1  982  ? 111.669 87.086  101.225 1.00 20.43  ? 982  ARG A O     1 
ATOM   7601  C  CB    . ARG A 1  982  ? 113.980 89.154  100.158 1.00 10.26  ? 982  ARG A CB    1 
ATOM   7602  C  CG    . ARG A 1  982  ? 113.804 88.197  99.006  1.00 16.70  ? 982  ARG A CG    1 
ATOM   7603  C  CD    . ARG A 1  982  ? 115.053 88.101  98.159  1.00 18.08  ? 982  ARG A CD    1 
ATOM   7604  N  NE    . ARG A 1  982  ? 116.120 87.381  98.839  1.00 14.44  ? 982  ARG A NE    1 
ATOM   7605  C  CZ    . ARG A 1  982  ? 117.298 87.901  99.146  1.00 18.38  ? 982  ARG A CZ    1 
ATOM   7606  N  NH1   . ARG A 1  982  ? 117.603 89.151  98.843  1.00 19.95  ? 982  ARG A NH1   1 
ATOM   7607  N  NH2   . ARG A 1  982  ? 118.193 87.147  99.773  1.00 20.89  ? 982  ARG A NH2   1 
ATOM   7608  N  N     . LEU A 1  983  ? 113.271 87.464  102.748 1.00 12.94  ? 983  LEU A N     1 
ATOM   7609  C  CA    . LEU A 1  983  ? 113.118 86.162  103.377 1.00 13.30  ? 983  LEU A CA    1 
ATOM   7610  C  C     . LEU A 1  983  ? 111.977 86.111  104.377 1.00 15.30  ? 983  LEU A C     1 
ATOM   7611  O  O     . LEU A 1  983  ? 111.646 85.019  104.845 1.00 18.72  ? 983  LEU A O     1 
ATOM   7612  C  CB    . LEU A 1  983  ? 114.414 85.761  104.069 1.00 13.22  ? 983  LEU A CB    1 
ATOM   7613  C  CG    . LEU A 1  983  ? 115.612 85.693  103.139 1.00 16.70  ? 983  LEU A CG    1 
ATOM   7614  C  CD1   . LEU A 1  983  ? 116.843 85.299  103.915 1.00 16.72  ? 983  LEU A CD1   1 
ATOM   7615  C  CD2   . LEU A 1  983  ? 115.339 84.727  102.015 1.00 17.54  ? 983  LEU A CD2   1 
ATOM   7616  N  N     . GLN A 1  984  ? 111.385 87.256  104.709 1.00 15.67  ? 984  GLN A N     1 
ATOM   7617  C  CA    . GLN A 1  984  ? 110.245 87.356  105.620 1.00 13.47  ? 984  GLN A CA    1 
ATOM   7618  C  C     . GLN A 1  984  ? 110.525 86.674  106.953 1.00 13.88  ? 984  GLN A C     1 
ATOM   7619  O  O     . GLN A 1  984  ? 109.725 85.891  107.462 1.00 15.39  ? 984  GLN A O     1 
ATOM   7620  C  CB    . GLN A 1  984  ? 108.979 86.808  104.976 1.00 12.06  ? 984  GLN A CB    1 
ATOM   7621  C  CG    . GLN A 1  984  ? 108.589 87.554  103.730 1.00 17.51  ? 984  GLN A CG    1 
ATOM   7622  C  CD    . GLN A 1  984  ? 107.853 88.838  104.034 1.00 15.98  ? 984  GLN A CD    1 
ATOM   7623  O  OE1   . GLN A 1  984  ? 106.761 88.824  104.588 1.00 18.73  ? 984  GLN A OE1   1 
ATOM   7624  N  NE2   . GLN A 1  984  ? 108.456 89.959  103.678 1.00 13.06  ? 984  GLN A NE2   1 
ATOM   7625  N  N     . THR A 1  985  ? 111.684 86.985  107.518 1.00 12.09  ? 985  THR A N     1 
ATOM   7626  C  CA    . THR A 1  985  ? 112.046 86.497  108.830 1.00 11.85  ? 985  THR A CA    1 
ATOM   7627  C  C     . THR A 1  985  ? 111.274 87.262  109.905 1.00 12.58  ? 985  THR A C     1 
ATOM   7628  O  O     . THR A 1  985  ? 110.750 88.346  109.647 1.00 16.70  ? 985  THR A O     1 
ATOM   7629  C  CB    . THR A 1  985  ? 113.548 86.643  109.040 1.00 12.96  ? 985  THR A CB    1 
ATOM   7630  O  OG1   . THR A 1  985  ? 113.901 88.023  108.956 1.00 15.30  ? 985  THR A OG1   1 
ATOM   7631  C  CG2   . THR A 1  985  ? 114.306 85.880  107.984 1.00 8.79   ? 985  THR A CG2   1 
ATOM   7632  N  N     . PRO A 1  986  ? 111.169 86.707  111.112 1.00 11.05  ? 986  PRO A N     1 
ATOM   7633  C  CA    . PRO A 1  986  ? 110.407 87.383  112.168 1.00 13.39  ? 986  PRO A CA    1 
ATOM   7634  C  C     . PRO A 1  986  ? 111.009 88.718  112.589 1.00 10.00  ? 986  PRO A C     1 
ATOM   7635  O  O     . PRO A 1  986  ? 112.221 88.929  112.534 1.00 8.38   ? 986  PRO A O     1 
ATOM   7636  C  CB    . PRO A 1  986  ? 110.426 86.370  113.317 1.00 9.47   ? 986  PRO A CB    1 
ATOM   7637  C  CG    . PRO A 1  986  ? 111.487 85.414  112.984 1.00 8.82   ? 986  PRO A CG    1 
ATOM   7638  C  CD    . PRO A 1  986  ? 111.527 85.339  111.511 1.00 10.36  ? 986  PRO A CD    1 
ATOM   7639  N  N     . ILE A 1  987  ? 110.136 89.620  113.019 1.00 8.32   ? 987  ILE A N     1 
ATOM   7640  C  CA    . ILE A 1  987  ? 110.511 90.965  113.436 1.00 5.13   ? 987  ILE A CA    1 
ATOM   7641  C  C     . ILE A 1  987  ? 110.430 91.060  114.954 1.00 6.45   ? 987  ILE A C     1 
ATOM   7642  O  O     . ILE A 1  987  ? 109.454 90.591  115.547 1.00 15.47  ? 987  ILE A O     1 
ATOM   7643  C  CB    . ILE A 1  987  ? 109.613 92.016  112.767 1.00 6.35   ? 987  ILE A CB    1 
ATOM   7644  C  CG1   . ILE A 1  987  ? 109.585 91.796  111.260 1.00 7.94   ? 987  ILE A CG1   1 
ATOM   7645  C  CG2   . ILE A 1  987  ? 110.094 93.417  113.075 1.00 6.11   ? 987  ILE A CG2   1 
ATOM   7646  C  CD1   . ILE A 1  987  ? 108.603 92.669  110.539 1.00 7.03   ? 987  ILE A CD1   1 
ATOM   7647  N  N     . PRO A 1  988  ? 111.422 91.642  115.622 1.00 2.24   ? 988  PRO A N     1 
ATOM   7648  C  CA    . PRO A 1  988  ? 111.309 91.852  117.065 1.00 4.45   ? 988  PRO A CA    1 
ATOM   7649  C  C     . PRO A 1  988  ? 110.147 92.772  117.409 1.00 6.13   ? 988  PRO A C     1 
ATOM   7650  O  O     . PRO A 1  988  ? 109.761 93.639  116.629 1.00 13.99  ? 988  PRO A O     1 
ATOM   7651  C  CB    . PRO A 1  988  ? 112.651 92.486  117.434 1.00 0.32   ? 988  PRO A CB    1 
ATOM   7652  C  CG    . PRO A 1  988  ? 113.547 92.126  116.356 1.00 1.87   ? 988  PRO A CG    1 
ATOM   7653  C  CD    . PRO A 1  988  ? 112.746 92.032  115.120 1.00 3.35   ? 988  PRO A CD    1 
ATOM   7654  N  N     . VAL A 1  989  ? 109.585 92.565  118.598 1.00 3.38   ? 989  VAL A N     1 
ATOM   7655  C  CA    . VAL A 1  989  ? 108.396 93.310  119.003 1.00 2.93   ? 989  VAL A CA    1 
ATOM   7656  C  C     . VAL A 1  989  ? 108.711 94.791  119.161 1.00 1.87   ? 989  VAL A C     1 
ATOM   7657  O  O     . VAL A 1  989  ? 107.881 95.649  118.854 1.00 2.96   ? 989  VAL A O     1 
ATOM   7658  C  CB    . VAL A 1  989  ? 107.805 92.706  120.291 1.00 2.70   ? 989  VAL A CB    1 
ATOM   7659  C  CG1   . VAL A 1  989  ? 106.791 93.631  120.905 1.00 0.66   ? 989  VAL A CG1   1 
ATOM   7660  C  CG2   . VAL A 1  989  ? 107.163 91.390  119.990 1.00 2.80   ? 989  VAL A CG2   1 
ATOM   7661  N  N     . TYR A 1  990  ? 109.909 95.119  119.635 1.00 1.03   ? 990  TYR A N     1 
ATOM   7662  C  CA    . TYR A 1  990  ? 110.258 96.521  119.815 1.00 5.01   ? 990  TYR A CA    1 
ATOM   7663  C  C     . TYR A 1  990  ? 110.430 97.253  118.491 1.00 3.13   ? 990  TYR A C     1 
ATOM   7664  O  O     . TYR A 1  990  ? 110.432 98.484  118.482 1.00 9.38   ? 990  TYR A O     1 
ATOM   7665  C  CB    . TYR A 1  990  ? 111.520 96.651  120.672 1.00 3.95   ? 990  TYR A CB    1 
ATOM   7666  C  CG    . TYR A 1  990  ? 112.820 96.370  119.956 1.00 0.32   ? 990  TYR A CG    1 
ATOM   7667  C  CD1   . TYR A 1  990  ? 113.291 95.081  119.814 1.00 3.74   ? 990  TYR A CD1   1 
ATOM   7668  C  CD2   . TYR A 1  990  ? 113.575 97.399  119.422 1.00 0.26   ? 990  TYR A CD2   1 
ATOM   7669  C  CE1   . TYR A 1  990  ? 114.463 94.828  119.167 1.00 1.23   ? 990  TYR A CE1   1 
ATOM   7670  C  CE2   . TYR A 1  990  ? 114.744 97.148  118.764 1.00 3.64   ? 990  TYR A CE2   1 
ATOM   7671  C  CZ    . TYR A 1  990  ? 115.185 95.861  118.640 1.00 2.64   ? 990  TYR A CZ    1 
ATOM   7672  O  OH    . TYR A 1  990  ? 116.362 95.598  117.990 1.00 4.10   ? 990  TYR A OH    1 
ATOM   7673  N  N     . LEU A 1  991  ? 110.572 96.533  117.379 1.00 5.03   ? 991  LEU A N     1 
ATOM   7674  C  CA    . LEU A 1  991  ? 110.636 97.178  116.073 1.00 0.51   ? 991  LEU A CA    1 
ATOM   7675  C  C     . LEU A 1  991  ? 109.268 97.263  115.414 1.00 4.35   ? 991  LEU A C     1 
ATOM   7676  O  O     . LEU A 1  991  ? 109.062 98.100  114.536 1.00 14.81  ? 991  LEU A O     1 
ATOM   7677  C  CB    . LEU A 1  991  ? 111.606 96.439  115.155 1.00 2.29   ? 991  LEU A CB    1 
ATOM   7678  C  CG    . LEU A 1  991  ? 113.100 96.573  115.420 1.00 13.14  ? 991  LEU A CG    1 
ATOM   7679  C  CD1   . LEU A 1  991  ? 113.875 95.824  114.376 1.00 15.04  ? 991  LEU A CD1   1 
ATOM   7680  C  CD2   . LEU A 1  991  ? 113.522 98.023  115.461 1.00 0.73   ? 991  LEU A CD2   1 
ATOM   7681  N  N     . LYS A 1  992  ? 108.338 96.391  115.800 1.00 4.22   ? 992  LYS A N     1 
ATOM   7682  C  CA    . LYS A 1  992  ? 106.947 96.560  115.408 1.00 15.70  ? 992  LYS A CA    1 
ATOM   7683  C  C     . LYS A 1  992  ? 106.341 97.793  116.057 1.00 6.39   ? 992  LYS A C     1 
ATOM   7684  O  O     . LYS A 1  992  ? 105.512 98.476  115.452 1.00 12.87  ? 992  LYS A O     1 
ATOM   7685  C  CB    . LYS A 1  992  ? 106.137 95.331  115.793 1.00 2.14   ? 992  LYS A CB    1 
ATOM   7686  C  CG    . LYS A 1  992  ? 106.503 94.076  115.071 1.00 5.77   ? 992  LYS A CG    1 
ATOM   7687  C  CD    . LYS A 1  992  ? 105.765 92.904  115.672 1.00 6.68   ? 992  LYS A CD    1 
ATOM   7688  C  CE    . LYS A 1  992  ? 106.161 91.616  115.000 1.00 7.96   ? 992  LYS A CE    1 
ATOM   7689  N  NZ    . LYS A 1  992  ? 105.537 90.433  115.638 1.00 11.17  ? 992  LYS A NZ    1 
ATOM   7690  N  N     . ARG A 1  993  ? 106.712 98.076  117.304 1.00 3.29   ? 993  ARG A N     1 
ATOM   7691  C  CA    . ARG A 1  993  ? 106.208 99.269  117.965 1.00 4.82   ? 993  ARG A CA    1 
ATOM   7692  C  C     . ARG A 1  993  ? 106.780 100.534 117.356 1.00 4.79   ? 993  ARG A C     1 
ATOM   7693  O  O     . ARG A 1  993  ? 106.146 101.587 117.422 1.00 11.70  ? 993  ARG A O     1 
ATOM   7694  C  CB    . ARG A 1  993  ? 106.521 99.239  119.459 1.00 0.29   ? 993  ARG A CB    1 
ATOM   7695  C  CG    . ARG A 1  993  ? 106.033 98.030  120.175 1.00 11.12  ? 993  ARG A CG    1 
ATOM   7696  C  CD    . ARG A 1  993  ? 104.537 98.025  120.255 1.00 7.26   ? 993  ARG A CD    1 
ATOM   7697  N  NE    . ARG A 1  993  ? 104.052 96.959  121.115 1.00 5.90   ? 993  ARG A NE    1 
ATOM   7698  C  CZ    . ARG A 1  993  ? 103.690 95.763  120.681 1.00 9.97   ? 993  ARG A CZ    1 
ATOM   7699  N  NH1   . ARG A 1  993  ? 103.702 95.463  119.396 1.00 7.01   ? 993  ARG A NH1   1 
ATOM   7700  N  NH2   . ARG A 1  993  ? 103.309 94.844  121.558 1.00 13.07  ? 993  ARG A NH2   1 
ATOM   7701  N  N     . ALA A 1  994  ? 107.974 100.461 116.777 1.00 3.64   ? 994  ALA A N     1 
ATOM   7702  C  CA    . ALA A 1  994  ? 108.620 101.667 116.285 1.00 0.69   ? 994  ALA A CA    1 
ATOM   7703  C  C     . ALA A 1  994  ? 107.976 102.168 115.005 1.00 5.56   ? 994  ALA A C     1 
ATOM   7704  O  O     . ALA A 1  994  ? 108.118 103.343 114.663 1.00 14.59  ? 994  ALA A O     1 
ATOM   7705  C  CB    . ALA A 1  994  ? 110.106 101.414 116.076 1.00 12.40  ? 994  ALA A CB    1 
ATOM   7706  N  N     . ALA A 1  995  ? 107.259 101.305 114.296 1.00 4.60   ? 995  ALA A N     1 
ATOM   7707  C  CA    . ALA A 1  995  ? 106.600 101.660 113.052 1.00 3.10   ? 995  ALA A CA    1 
ATOM   7708  C  C     . ALA A 1  995  ? 105.134 102.012 113.248 1.00 9.72   ? 995  ALA A C     1 
ATOM   7709  O  O     . ALA A 1  995  ? 104.386 102.077 112.274 1.00 15.32  ? 995  ALA A O     1 
ATOM   7710  C  CB    . ALA A 1  995  ? 106.741 100.518 112.048 1.00 1.61   ? 995  ALA A CB    1 
ATOM   7711  N  N     . SER A 1  996  ? 104.712 102.249 114.485 1.00 7.88   ? 996  SER A N     1 
ATOM   7712  C  CA    . SER A 1  996  ? 103.294 102.406 114.776 1.00 6.71   ? 996  SER A CA    1 
ATOM   7713  C  C     . SER A 1  996  ? 102.746 103.738 114.285 1.00 10.78  ? 996  SER A C     1 
ATOM   7714  O  O     . SER A 1  996  ? 101.657 103.783 113.708 1.00 15.29  ? 996  SER A O     1 
ATOM   7715  C  CB    . SER A 1  996  ? 103.060 102.249 116.271 1.00 5.37   ? 996  SER A CB    1 
ATOM   7716  O  OG    . SER A 1  996  ? 103.005 100.883 116.604 1.00 14.53  ? 996  SER A OG    1 
ATOM   7717  N  N     . LEU A 1  997  ? 103.470 104.834 114.513 1.00 9.38   ? 997  LEU A N     1 
ATOM   7718  C  CA    . LEU A 1  997  ? 102.978 106.136 114.077 1.00 4.76   ? 997  LEU A CA    1 
ATOM   7719  C  C     . LEU A 1  997  ? 102.953 106.249 112.561 1.00 7.48   ? 997  LEU A C     1 
ATOM   7720  O  O     . LEU A 1  997  ? 102.056 106.879 111.999 1.00 18.89  ? 997  LEU A O     1 
ATOM   7721  C  CB    . LEU A 1  997  ? 103.825 107.261 114.659 1.00 5.23   ? 997  LEU A CB    1 
ATOM   7722  C  CG    . LEU A 1  997  ? 103.415 107.857 115.996 1.00 8.54   ? 997  LEU A CG    1 
ATOM   7723  C  CD1   . LEU A 1  997  ? 104.141 109.156 116.168 1.00 9.01   ? 997  LEU A CD1   1 
ATOM   7724  C  CD2   . LEU A 1  997  ? 101.925 108.043 116.094 1.00 9.34   ? 997  LEU A CD2   1 
ATOM   7725  N  N     . MET A 1  998  ? 103.944 105.679 111.881 1.00 4.53   ? 998  MET A N     1 
ATOM   7726  C  CA    . MET A 1  998  ? 103.983 105.780 110.430 1.00 3.11   ? 998  MET A CA    1 
ATOM   7727  C  C     . MET A 1  998  ? 102.967 104.863 109.773 1.00 7.61   ? 998  MET A C     1 
ATOM   7728  O  O     . MET A 1  998  ? 102.411 105.212 108.732 1.00 17.13  ? 998  MET A O     1 
ATOM   7729  C  CB    . MET A 1  998  ? 105.384 105.477 109.910 1.00 8.34   ? 998  MET A CB    1 
ATOM   7730  C  CG    . MET A 1  998  ? 106.326 106.675 109.870 1.00 13.20  ? 998  MET A CG    1 
ATOM   7731  S  SD    . MET A 1  998  ? 105.534 108.224 109.417 1.00 26.02  ? 998  MET A SD    1 
ATOM   7732  C  CE    . MET A 1  998  ? 105.358 107.976 107.664 1.00 4.54   ? 998  MET A CE    1 
ATOM   7733  N  N     . ARG A 1  999  ? 102.716 103.689 110.350 1.00 8.41   ? 999  ARG A N     1 
ATOM   7734  C  CA    . ARG A 1  999  ? 101.644 102.837 109.851 1.00 6.72   ? 999  ARG A CA    1 
ATOM   7735  C  C     . ARG A 1  999  ? 100.301 103.519 110.005 1.00 6.23   ? 999  ARG A C     1 
ATOM   7736  O  O     . ARG A 1  999  ? 99.436  103.407 109.135 1.00 14.18  ? 999  ARG A O     1 
ATOM   7737  C  CB    . ARG A 1  999  ? 101.632 101.510 110.595 1.00 8.34   ? 999  ARG A CB    1 
ATOM   7738  C  CG    . ARG A 1  999  ? 102.510 100.439 110.040 1.00 8.04   ? 999  ARG A CG    1 
ATOM   7739  C  CD    . ARG A 1  999  ? 102.695 99.396  111.099 1.00 6.82   ? 999  ARG A CD    1 
ATOM   7740  N  NE    . ARG A 1  999  ? 103.141 98.111  110.589 1.00 4.65   ? 999  ARG A NE    1 
ATOM   7741  C  CZ    . ARG A 1  999  ? 103.543 97.121  111.368 1.00 13.39  ? 999  ARG A CZ    1 
ATOM   7742  N  NH1   . ARG A 1  999  ? 103.612 97.265  112.676 1.00 12.96  ? 999  ARG A NH1   1 
ATOM   7743  N  NH2   . ARG A 1  999  ? 103.886 95.961  110.821 1.00 12.28  ? 999  ARG A NH2   1 
ATOM   7744  N  N     . MET A 1  1000 ? 100.104 104.207 111.127 1.00 3.29   ? 1000 MET A N     1 
ATOM   7745  C  CA    . MET A 1  1000 ? 98.869  104.937 111.367 1.00 2.15   ? 1000 MET A CA    1 
ATOM   7746  C  C     . MET A 1  1000 ? 98.675  106.055 110.357 1.00 12.27  ? 1000 MET A C     1 
ATOM   7747  O  O     . MET A 1  1000 ? 97.590  106.205 109.790 1.00 20.92  ? 1000 MET A O     1 
ATOM   7748  C  CB    . MET A 1  1000 ? 98.886  105.500 112.781 1.00 7.36   ? 1000 MET A CB    1 
ATOM   7749  C  CG    . MET A 1  1000 ? 97.684  106.310 113.140 1.00 10.80  ? 1000 MET A CG    1 
ATOM   7750  S  SD    . MET A 1  1000 ? 97.409  106.335 114.903 1.00 19.24  ? 1000 MET A SD    1 
ATOM   7751  C  CE    . MET A 1  1000 ? 96.071  107.500 114.984 1.00 7.64   ? 1000 MET A CE    1 
ATOM   7752  N  N     . LEU A 1  1001 ? 99.716  106.851 110.119 1.00 12.74  ? 1001 LEU A N     1 
ATOM   7753  C  CA    . LEU A 1  1001 ? 99.621  107.952 109.170 1.00 5.05   ? 1001 LEU A CA    1 
ATOM   7754  C  C     . LEU A 1  1001 ? 99.409  107.451 107.749 1.00 4.93   ? 1001 LEU A C     1 
ATOM   7755  O  O     . LEU A 1  1001 ? 98.664  108.062 106.981 1.00 16.10  ? 1001 LEU A O     1 
ATOM   7756  C  CB    . LEU A 1  1001 ? 100.877 108.814 109.248 1.00 9.44   ? 1001 LEU A CB    1 
ATOM   7757  C  CG    . LEU A 1  1001 ? 100.883 110.088 108.405 1.00 8.69   ? 1001 LEU A CG    1 
ATOM   7758  C  CD1   . LEU A 1  1001 ? 99.820  111.042 108.884 1.00 11.89  ? 1001 LEU A CD1   1 
ATOM   7759  C  CD2   . LEU A 1  1001 ? 102.237 110.735 108.425 1.00 7.72   ? 1001 LEU A CD2   1 
ATOM   7760  N  N     . ILE A 1  1002 ? 100.070 106.361 107.370 1.00 6.83   ? 1002 ILE A N     1 
ATOM   7761  C  CA    . ILE A 1  1002 ? 99.926  105.842 106.013 1.00 10.63  ? 1002 ILE A CA    1 
ATOM   7762  C  C     . ILE A 1  1002 ? 98.508  105.344 105.776 1.00 13.94  ? 1002 ILE A C     1 
ATOM   7763  O  O     . ILE A 1  1002 ? 97.948  105.517 104.693 1.00 15.39  ? 1002 ILE A O     1 
ATOM   7764  C  CB    . ILE A 1  1002 ? 100.972 104.747 105.744 1.00 5.72   ? 1002 ILE A CB    1 
ATOM   7765  C  CG1   . ILE A 1  1002 ? 102.338 105.379 105.503 1.00 10.42  ? 1002 ILE A CG1   1 
ATOM   7766  C  CG2   . ILE A 1  1002 ? 100.586 103.905 104.563 1.00 6.17   ? 1002 ILE A CG2   1 
ATOM   7767  C  CD1   . ILE A 1  1002 ? 103.476 104.432 105.656 1.00 11.01  ? 1002 ILE A CD1   1 
ATOM   7768  N  N     . ARG A 1  1003 ? 97.902  104.720 106.781 1.00 17.80  ? 1003 ARG A N     1 
ATOM   7769  C  CA    . ARG A 1  1003 ? 96.542  104.225 106.615 1.00 15.00  ? 1003 ARG A CA    1 
ATOM   7770  C  C     . ARG A 1  1003 ? 95.518  105.351 106.588 1.00 13.95  ? 1003 ARG A C     1 
ATOM   7771  O  O     . ARG A 1  1003 ? 94.428  105.171 106.042 1.00 20.19  ? 1003 ARG A O     1 
ATOM   7772  C  CB    . ARG A 1  1003 ? 96.210  103.231 107.720 1.00 16.02  ? 1003 ARG A CB    1 
ATOM   7773  C  CG    . ARG A 1  1003 ? 96.686  101.835 107.435 1.00 16.32  ? 1003 ARG A CG    1 
ATOM   7774  C  CD    . ARG A 1  1003 ? 96.063  100.865 108.395 1.00 15.93  ? 1003 ARG A CD    1 
ATOM   7775  N  NE    . ARG A 1  1003 ? 96.571  101.051 109.745 1.00 16.41  ? 1003 ARG A NE    1 
ATOM   7776  C  CZ    . ARG A 1  1003 ? 97.487  100.280 110.306 1.00 19.28  ? 1003 ARG A CZ    1 
ATOM   7777  N  NH1   . ARG A 1  1003 ? 97.991  99.237  109.671 1.00 20.96  ? 1003 ARG A NH1   1 
ATOM   7778  N  NH2   . ARG A 1  1003 ? 97.904  100.558 111.535 1.00 13.51  ? 1003 ARG A NH2   1 
ATOM   7779  N  N     . ILE A 1  1004 ? 95.834  106.506 107.173 1.00 13.45  ? 1004 ILE A N     1 
ATOM   7780  C  CA    . ILE A 1  1004 ? 94.924  107.647 107.113 1.00 14.52  ? 1004 ILE A CA    1 
ATOM   7781  C  C     . ILE A 1  1004 ? 95.034  108.339 105.763 1.00 20.27  ? 1004 ILE A C     1 
ATOM   7782  O  O     . ILE A 1  1004 ? 94.048  108.482 105.035 1.00 26.40  ? 1004 ILE A O     1 
ATOM   7783  C  CB    . ILE A 1  1004 ? 95.215  108.642 108.248 1.00 15.45  ? 1004 ILE A CB    1 
ATOM   7784  C  CG1   . ILE A 1  1004 ? 94.887  108.056 109.612 1.00 16.00  ? 1004 ILE A CG1   1 
ATOM   7785  C  CG2   . ILE A 1  1004 ? 94.429  109.905 108.035 1.00 17.76  ? 1004 ILE A CG2   1 
ATOM   7786  C  CD1   . ILE A 1  1004 ? 95.281  108.963 110.754 1.00 13.17  ? 1004 ILE A CD1   1 
ATOM   7787  N  N     . GLU A 1  1005 ? 96.240  108.774 105.407 1.00 17.96  ? 1005 GLU A N     1 
ATOM   7788  C  CA    . GLU A 1  1005 ? 96.434  109.591 104.220 1.00 17.15  ? 1005 GLU A CA    1 
ATOM   7789  C  C     . GLU A 1  1005 ? 96.419  108.791 102.931 1.00 18.74  ? 1005 GLU A C     1 
ATOM   7790  O  O     . GLU A 1  1005 ? 96.431  109.391 101.854 1.00 25.46  ? 1005 GLU A O     1 
ATOM   7791  C  CB    . GLU A 1  1005 ? 97.747  110.368 104.316 1.00 13.49  ? 1005 GLU A CB    1 
ATOM   7792  C  CG    . GLU A 1  1005 ? 97.852  111.270 105.516 1.00 17.91  ? 1005 GLU A CG    1 
ATOM   7793  C  CD    . GLU A 1  1005 ? 96.806  112.368 105.520 1.00 27.04  ? 1005 GLU A CD    1 
ATOM   7794  O  OE1   . GLU A 1  1005 ? 96.306  112.729 104.437 1.00 26.81  ? 1005 GLU A OE1   1 
ATOM   7795  O  OE2   . GLU A 1  1005 ? 96.497  112.896 106.607 1.00 26.63  ? 1005 GLU A OE2   1 
ATOM   7796  N  N     . LEU A 1  1006 ? 96.416  107.466 103.004 1.00 18.67  ? 1006 LEU A N     1 
ATOM   7797  C  CA    . LEU A 1  1006 ? 96.277  106.624 101.825 1.00 18.25  ? 1006 LEU A CA    1 
ATOM   7798  C  C     . LEU A 1  1006 ? 95.017  105.773 101.885 1.00 19.21  ? 1006 LEU A C     1 
ATOM   7799  O  O     . LEU A 1  1006 ? 94.986  104.662 101.356 1.00 21.36  ? 1006 LEU A O     1 
ATOM   7800  C  CB    . LEU A 1  1006 ? 97.505  105.740 101.641 1.00 16.56  ? 1006 LEU A CB    1 
ATOM   7801  C  CG    . LEU A 1  1006 ? 98.515  106.167 100.586 1.00 19.13  ? 1006 LEU A CG    1 
ATOM   7802  C  CD1   . LEU A 1  1006 ? 98.945  107.567 100.832 1.00 18.81  ? 1006 LEU A CD1   1 
ATOM   7803  C  CD2   . LEU A 1  1006 ? 99.712  105.257 100.625 1.00 17.57  ? 1006 LEU A CD2   1 
ATOM   7804  N  N     . ALA A 1  1007 ? 93.972  106.280 102.531 1.00 21.32  ? 1007 ALA A N     1 
ATOM   7805  C  CA    . ALA A 1  1007 ? 92.704  105.576 102.545 1.00 24.68  ? 1007 ALA A CA    1 
ATOM   7806  C  C     . ALA A 1  1007 ? 92.077  105.608 101.158 1.00 29.54  ? 1007 ALA A C     1 
ATOM   7807  O  O     . ALA A 1  1007 ? 92.423  106.434 100.314 1.00 32.60  ? 1007 ALA A O     1 
ATOM   7808  C  CB    . ALA A 1  1007 ? 91.759  106.192 103.572 1.00 22.18  ? 1007 ALA A CB    1 
ATOM   7809  N  N     . THR A 1  1008 ? 91.146  104.683 100.923 1.00 27.55  ? 1008 THR A N     1 
ATOM   7810  C  CA    . THR A 1  1008 ? 90.509  104.591 99.613  1.00 26.84  ? 1008 THR A CA    1 
ATOM   7811  C  C     . THR A 1  1008 ? 89.749  105.860 99.264  1.00 27.17  ? 1008 THR A C     1 
ATOM   7812  O  O     . THR A 1  1008 ? 89.706  106.255 98.096  1.00 28.57  ? 1008 THR A O     1 
ATOM   7813  C  CB    . THR A 1  1008 ? 89.578  103.382 99.566  1.00 28.90  ? 1008 THR A CB    1 
ATOM   7814  O  OG1   . THR A 1  1008 ? 90.329  102.199 99.856  1.00 33.24  ? 1008 THR A OG1   1 
ATOM   7815  C  CG2   . THR A 1  1008 ? 88.949  103.243 98.199  1.00 27.02  ? 1008 THR A CG2   1 
ATOM   7816  N  N     . VAL A 1  1009 ? 89.162  106.525 100.259 1.00 22.34  ? 1009 VAL A N     1 
ATOM   7817  C  CA    . VAL A 1  1009 ? 88.450  107.771 100.014 1.00 22.41  ? 1009 VAL A CA    1 
ATOM   7818  C  C     . VAL A 1  1009 ? 89.366  108.888 99.548  1.00 28.30  ? 1009 VAL A C     1 
ATOM   7819  O  O     . VAL A 1  1009 ? 88.880  109.907 99.044  1.00 29.81  ? 1009 VAL A O     1 
ATOM   7820  C  CB    . VAL A 1  1009 ? 87.704  108.221 101.284 1.00 25.20  ? 1009 VAL A CB    1 
ATOM   7821  C  CG1   . VAL A 1  1009 ? 86.731  107.158 101.729 1.00 23.28  ? 1009 VAL A CG1   1 
ATOM   7822  C  CG2   . VAL A 1  1009 ? 88.688  108.543 102.383 1.00 27.05  ? 1009 VAL A CG2   1 
ATOM   7823  N  N     . LYS A 1  1010 ? 90.678  108.729 99.707  1.00 25.30  ? 1010 LYS A N     1 
ATOM   7824  C  CA    . LYS A 1  1010 ? 91.645  109.741 99.320  1.00 22.48  ? 1010 LYS A CA    1 
ATOM   7825  C  C     . LYS A 1  1010 ? 92.443  109.371 98.081  1.00 25.62  ? 1010 LYS A C     1 
ATOM   7826  O  O     . LYS A 1  1010 ? 92.982  110.265 97.424  1.00 30.66  ? 1010 LYS A O     1 
ATOM   7827  C  CB    . LYS A 1  1010 ? 92.619  110.004 100.473 1.00 20.01  ? 1010 LYS A CB    1 
ATOM   7828  C  CG    . LYS A 1  1010 ? 91.984  110.593 101.704 1.00 21.22  ? 1010 LYS A CG    1 
ATOM   7829  C  CD    . LYS A 1  1010 ? 93.025  111.204 102.599 1.00 18.55  ? 1010 LYS A CD    1 
ATOM   7830  C  CE    . LYS A 1  1010 ? 92.443  111.578 103.933 1.00 23.23  ? 1010 LYS A CE    1 
ATOM   7831  N  NZ    . LYS A 1  1010 ? 91.650  112.821 103.864 1.00 27.68  ? 1010 LYS A NZ    1 
ATOM   7832  N  N     . THR A 1  1011 ? 92.534  108.095 97.748  1.00 26.46  ? 1011 THR A N     1 
ATOM   7833  C  CA    . THR A 1  1011 ? 93.385  107.611 96.673  1.00 26.10  ? 1011 THR A CA    1 
ATOM   7834  C  C     . THR A 1  1011 ? 92.554  107.101 95.507  1.00 30.92  ? 1011 THR A C     1 
ATOM   7835  O  O     . THR A 1  1011 ? 92.910  106.128 94.843  1.00 31.38  ? 1011 THR A O     1 
ATOM   7836  C  CB    . THR A 1  1011 ? 94.319  106.520 97.183  1.00 29.80  ? 1011 THR A CB    1 
ATOM   7837  O  OG1   . THR A 1  1011 ? 93.546  105.479 97.787  1.00 33.41  ? 1011 THR A OG1   1 
ATOM   7838  C  CG2   . THR A 1  1011 ? 95.265  107.080 98.214  1.00 27.19  ? 1011 THR A CG2   1 
ATOM   7839  N  N     . LEU A 1  1012 ? 91.429  107.763 95.242  1.00 34.49  ? 1012 LEU A N     1 
ATOM   7840  C  CA    . LEU A 1  1012 ? 90.506  107.279 94.222  1.00 31.99  ? 1012 LEU A CA    1 
ATOM   7841  C  C     . LEU A 1  1012 ? 91.010  107.589 92.816  1.00 31.51  ? 1012 LEU A C     1 
ATOM   7842  O  O     . LEU A 1  1012 ? 90.814  106.791 91.893  1.00 31.32  ? 1012 LEU A O     1 
ATOM   7843  C  CB    . LEU A 1  1012 ? 89.122  107.877 94.466  1.00 31.52  ? 1012 LEU A CB    1 
ATOM   7844  C  CG    . LEU A 1  1012 ? 87.930  106.930 94.339  1.00 33.25  ? 1012 LEU A CG    1 
ATOM   7845  C  CD1   . LEU A 1  1012 ? 88.341  105.487 94.572  1.00 32.18  ? 1012 LEU A CD1   1 
ATOM   7846  C  CD2   . LEU A 1  1012 ? 86.877  107.331 95.355  1.00 30.49  ? 1012 LEU A CD2   1 
ATOM   7847  N  N     . ASN A 1  1013 ? 91.669  108.735 92.634  1.00 36.71  ? 1013 ASN A N     1 
ATOM   7848  C  CA    . ASN A 1  1013 ? 92.178  109.137 91.327  1.00 38.01  ? 1013 ASN A CA    1 
ATOM   7849  C  C     . ASN A 1  1013 ? 93.628  108.731 91.079  1.00 39.23  ? 1013 ASN A C     1 
ATOM   7850  O  O     . ASN A 1  1013 ? 94.154  109.028 90.004  1.00 41.88  ? 1013 ASN A O     1 
ATOM   7851  C  CB    . ASN A 1  1013 ? 92.040  110.650 91.160  1.00 39.49  ? 1013 ASN A CB    1 
ATOM   7852  C  CG    . ASN A 1  1013 ? 90.602  111.114 91.247  1.00 42.09  ? 1013 ASN A CG    1 
ATOM   7853  O  OD1   . ASN A 1  1013 ? 89.709  110.496 90.679  1.00 43.44  ? 1013 ASN A OD1   1 
ATOM   7854  N  ND2   . ASN A 1  1013 ? 90.371  112.206 91.964  1.00 39.33  ? 1013 ASN A ND2   1 
ATOM   7855  N  N     . ILE A 1  1014 ? 94.286  108.076 92.030  1.00 33.87  ? 1014 ILE A N     1 
ATOM   7856  C  CA    . ILE A 1  1014 ? 95.677  107.660 91.868  1.00 32.89  ? 1014 ILE A CA    1 
ATOM   7857  C  C     . ILE A 1  1014 ? 95.706  106.322 91.145  1.00 30.16  ? 1014 ILE A C     1 
ATOM   7858  O  O     . ILE A 1  1014 ? 94.953  105.407 91.483  1.00 35.39  ? 1014 ILE A O     1 
ATOM   7859  C  CB    . ILE A 1  1014 ? 96.388  107.567 93.233  1.00 34.97  ? 1014 ILE A CB    1 
ATOM   7860  C  CG1   . ILE A 1  1014 ? 96.773  108.943 93.773  1.00 30.87  ? 1014 ILE A CG1   1 
ATOM   7861  C  CG2   . ILE A 1  1014 ? 97.628  106.701 93.149  1.00 32.85  ? 1014 ILE A CG2   1 
ATOM   7862  C  CD1   . ILE A 1  1014 ? 95.629  109.754 94.268  1.00 33.96  ? 1014 ILE A CD1   1 
ATOM   7863  N  N     . THR A 1  1015 ? 96.576  106.199 90.151  1.00 30.68  ? 1015 THR A N     1 
ATOM   7864  C  CA    . THR A 1  1015 ? 96.658  104.970 89.381  1.00 34.24  ? 1015 THR A CA    1 
ATOM   7865  C  C     . THR A 1  1015 ? 97.519  103.942 90.111  1.00 32.73  ? 1015 THR A C     1 
ATOM   7866  O  O     . THR A 1  1015 ? 98.146  104.232 91.129  1.00 34.88  ? 1015 THR A O     1 
ATOM   7867  C  CB    . THR A 1  1015 ? 97.237  105.249 87.997  1.00 36.90  ? 1015 THR A CB    1 
ATOM   7868  O  OG1   . THR A 1  1015 ? 96.811  106.545 87.566  1.00 38.56  ? 1015 THR A OG1   1 
ATOM   7869  C  CG2   . THR A 1  1015 ? 96.719  104.236 86.997  1.00 35.76  ? 1015 THR A CG2   1 
ATOM   7870  N  N     . CYS A 1  1016 ? 97.535  102.716 89.584  1.00 37.05  ? 1016 CYS A N     1 
ATOM   7871  C  CA    . CYS A 1  1016 ? 98.325  101.663 90.212  1.00 38.88  ? 1016 CYS A CA    1 
ATOM   7872  C  C     . CYS A 1  1016 ? 99.822  101.883 90.045  1.00 40.80  ? 1016 CYS A C     1 
ATOM   7873  O  O     . CYS A 1  1016 ? 100.586 101.613 90.974  1.00 45.50  ? 1016 CYS A O     1 
ATOM   7874  C  CB    . CYS A 1  1016 ? 97.927  100.293 89.672  1.00 37.94  ? 1016 CYS A CB    1 
ATOM   7875  S  SG    . CYS A 1  1016 ? 96.401  99.654  90.380  1.00 48.35  ? 1016 CYS A SG    1 
ATOM   7876  N  N     . GLU A 1  1017 ? 100.276 102.344 88.878  1.00 37.66  ? 1017 GLU A N     1 
ATOM   7877  C  CA    . GLU A 1  1017 ? 101.708 102.588 88.752  1.00 37.98  ? 1017 GLU A CA    1 
ATOM   7878  C  C     . GLU A 1  1017 ? 102.091 103.924 89.368  1.00 38.71  ? 1017 GLU A C     1 
ATOM   7879  O  O     . GLU A 1  1017 ? 103.277 104.182 89.594  1.00 42.18  ? 1017 GLU A O     1 
ATOM   7880  C  CB    . GLU A 1  1017 ? 102.177 102.519 87.294  1.00 39.10  ? 1017 GLU A CB    1 
ATOM   7881  C  CG    . GLU A 1  1017 ? 101.623 103.532 86.298  1.00 40.92  ? 1017 GLU A CG    1 
ATOM   7882  C  CD    . GLU A 1  1017 ? 100.121 103.567 86.198  1.00 44.34  ? 1017 GLU A CD    1 
ATOM   7883  O  OE1   . GLU A 1  1017 ? 99.585  104.672 85.978  1.00 41.66  ? 1017 GLU A OE1   1 
ATOM   7884  O  OE2   . GLU A 1  1017 ? 99.480  102.505 86.343  1.00 42.80  ? 1017 GLU A OE2   1 
ATOM   7885  N  N     . GLN A 1  1018 ? 101.112 104.787 89.639  1.00 28.53  ? 1018 GLN A N     1 
ATOM   7886  C  CA    . GLN A 1  1018 ? 101.367 105.971 90.444  1.00 28.88  ? 1018 GLN A CA    1 
ATOM   7887  C  C     . GLN A 1  1018 ? 101.480 105.658 91.923  1.00 30.78  ? 1018 GLN A C     1 
ATOM   7888  O  O     . GLN A 1  1018 ? 102.282 106.288 92.613  1.00 36.14  ? 1018 GLN A O     1 
ATOM   7889  C  CB    . GLN A 1  1018 ? 100.264 107.008 90.267  1.00 33.36  ? 1018 GLN A CB    1 
ATOM   7890  C  CG    . GLN A 1  1018 ? 100.270 107.736 88.955  1.00 33.27  ? 1018 GLN A CG    1 
ATOM   7891  C  CD    . GLN A 1  1018 ? 99.088  108.665 88.830  1.00 35.88  ? 1018 GLN A CD    1 
ATOM   7892  O  OE1   . GLN A 1  1018 ? 98.003  108.253 88.431  1.00 35.13  ? 1018 GLN A OE1   1 
ATOM   7893  N  NE2   . GLN A 1  1018 ? 99.289  109.927 89.181  1.00 33.51  ? 1018 GLN A NE2   1 
ATOM   7894  N  N     . MET A 1  1019 ? 100.676 104.726 92.434  1.00 32.89  ? 1019 MET A N     1 
ATOM   7895  C  CA    . MET A 1  1019 ? 100.731 104.420 93.857  1.00 29.42  ? 1019 MET A CA    1 
ATOM   7896  C  C     . MET A 1  1019 ? 102.018 103.689 94.203  1.00 30.22  ? 1019 MET A C     1 
ATOM   7897  O  O     . MET A 1  1019 ? 102.542 103.838 95.311  1.00 33.80  ? 1019 MET A O     1 
ATOM   7898  C  CB    . MET A 1  1019 ? 99.504  103.612 94.278  1.00 27.73  ? 1019 MET A CB    1 
ATOM   7899  C  CG    . MET A 1  1019 ? 99.543  103.118 95.716  1.00 27.60  ? 1019 MET A CG    1 
ATOM   7900  S  SD    . MET A 1  1019 ? 98.981  104.320 96.922  1.00 36.96  ? 1019 MET A SD    1 
ATOM   7901  C  CE    . MET A 1  1019 ? 97.230  104.335 96.597  1.00 31.42  ? 1019 MET A CE    1 
ATOM   7902  N  N     . SER A 1  1020 ? 102.549 102.906 93.264  1.00 25.51  ? 1020 SER A N     1 
ATOM   7903  C  CA    . SER A 1  1020 ? 103.870 102.324 93.465  1.00 26.41  ? 1020 SER A CA    1 
ATOM   7904  C  C     . SER A 1  1020 ? 104.931 103.403 93.584  1.00 28.91  ? 1020 SER A C     1 
ATOM   7905  O  O     . SER A 1  1020 ? 105.879 103.258 94.358  1.00 32.49  ? 1020 SER A O     1 
ATOM   7906  C  CB    . SER A 1  1020 ? 104.212 101.378 92.322  1.00 28.44  ? 1020 SER A CB    1 
ATOM   7907  O  OG    . SER A 1  1020 ? 103.499 100.167 92.448  1.00 33.27  ? 1020 SER A OG    1 
ATOM   7908  N  N     . ALA A 1  1021 ? 104.793 104.486 92.822  1.00 27.54  ? 1021 ALA A N     1 
ATOM   7909  C  CA    . ALA A 1  1021 ? 105.714 105.605 92.951  1.00 23.60  ? 1021 ALA A CA    1 
ATOM   7910  C  C     . ALA A 1  1021 ? 105.598 106.264 94.317  1.00 21.61  ? 1021 ALA A C     1 
ATOM   7911  O  O     . ALA A 1  1021 ? 106.607 106.676 94.894  1.00 27.88  ? 1021 ALA A O     1 
ATOM   7912  C  CB    . ALA A 1  1021 ? 105.462 106.621 91.839  1.00 22.27  ? 1021 ALA A CB    1 
ATOM   7913  N  N     . ILE A 1  1022 ? 104.378 106.390 94.842  1.00 19.56  ? 1022 ILE A N     1 
ATOM   7914  C  CA    . ILE A 1  1022 ? 104.188 106.989 96.160  1.00 19.80  ? 1022 ILE A CA    1 
ATOM   7915  C  C     . ILE A 1  1022 ? 104.829 106.131 97.242  1.00 18.48  ? 1022 ILE A C     1 
ATOM   7916  O  O     . ILE A 1  1022 ? 105.478 106.648 98.156  1.00 17.64  ? 1022 ILE A O     1 
ATOM   7917  C  CB    . ILE A 1  1022 ? 102.692 107.210 96.439  1.00 22.96  ? 1022 ILE A CB    1 
ATOM   7918  C  CG1   . ILE A 1  1022 ? 102.103 108.206 95.446  1.00 26.30  ? 1022 ILE A CG1   1 
ATOM   7919  C  CG2   . ILE A 1  1022 ? 102.479 107.716 97.849  1.00 15.21  ? 1022 ILE A CG2   1 
ATOM   7920  C  CD1   . ILE A 1  1022 ? 100.606 108.246 95.437  1.00 22.94  ? 1022 ILE A CD1   1 
ATOM   7921  N  N     . LEU A 1  1023 ? 104.649 104.813 97.168  1.00 14.85  ? 1023 LEU A N     1 
ATOM   7922  C  CA    . LEU A 1  1023 ? 105.172 103.944 98.216  1.00 13.26  ? 1023 LEU A CA    1 
ATOM   7923  C  C     . LEU A 1  1023 ? 106.688 103.877 98.180  1.00 18.34  ? 1023 LEU A C     1 
ATOM   7924  O  O     . LEU A 1  1023 ? 107.335 103.826 99.228  1.00 30.40  ? 1023 LEU A O     1 
ATOM   7925  C  CB    . LEU A 1  1023 ? 104.570 102.548 98.103  1.00 15.54  ? 1023 LEU A CB    1 
ATOM   7926  C  CG    . LEU A 1  1023 ? 103.062 102.451 98.311  1.00 17.59  ? 1023 LEU A CG    1 
ATOM   7927  C  CD1   . LEU A 1  1023 ? 102.619 101.011 98.238  1.00 12.35  ? 1023 LEU A CD1   1 
ATOM   7928  C  CD2   . LEU A 1  1023 ? 102.658 103.070 99.623  1.00 16.02  ? 1023 LEU A CD2   1 
ATOM   7929  N  N     . ASP A 1  1024 ? 107.277 103.872 96.987  1.00 19.88  ? 1024 ASP A N     1 
ATOM   7930  C  CA    . ASP A 1  1024 ? 108.731 103.829 96.890  1.00 10.41  ? 1024 ASP A CA    1 
ATOM   7931  C  C     . ASP A 1  1024 ? 109.356 105.140 97.342  1.00 12.31  ? 1024 ASP A C     1 
ATOM   7932  O  O     . ASP A 1  1024 ? 110.544 105.189 97.669  1.00 20.59  ? 1024 ASP A O     1 
ATOM   7933  C  CB    . ASP A 1  1024 ? 109.150 103.493 95.465  1.00 17.37  ? 1024 ASP A CB    1 
ATOM   7934  C  CG    . ASP A 1  1024 ? 109.524 102.043 95.311  1.00 27.04  ? 1024 ASP A CG    1 
ATOM   7935  O  OD1   . ASP A 1  1024 ? 109.603 101.350 96.345  1.00 27.42  ? 1024 ASP A OD1   1 
ATOM   7936  O  OD2   . ASP A 1  1024 ? 109.746 101.592 94.168  1.00 28.54  ? 1024 ASP A OD2   1 
ATOM   7937  N  N     . LEU A 1  1025 ? 108.581 106.216 97.341  1.00 10.96  ? 1025 LEU A N     1 
ATOM   7938  C  CA    . LEU A 1  1025 ? 109.066 107.471 97.891  1.00 11.73  ? 1025 LEU A CA    1 
ATOM   7939  C  C     . LEU A 1  1025 ? 108.968 107.519 99.407  1.00 18.88  ? 1025 LEU A C     1 
ATOM   7940  O  O     . LEU A 1  1025 ? 109.811 108.145 100.052 1.00 23.38  ? 1025 LEU A O     1 
ATOM   7941  C  CB    . LEU A 1  1025 ? 108.297 108.642 97.293  1.00 15.16  ? 1025 LEU A CB    1 
ATOM   7942  C  CG    . LEU A 1  1025 ? 109.177 109.865 97.067  1.00 19.93  ? 1025 LEU A CG    1 
ATOM   7943  C  CD1   . LEU A 1  1025 ? 110.067 109.643 95.871  1.00 22.88  ? 1025 LEU A CD1   1 
ATOM   7944  C  CD2   . LEU A 1  1025 ? 108.332 111.097 96.892  1.00 16.37  ? 1025 LEU A CD2   1 
ATOM   7945  N  N     . ILE A 1  1026 ? 107.945 106.899 99.989  1.00 16.06  ? 1026 ILE A N     1 
ATOM   7946  C  CA    . ILE A 1  1026 ? 107.822 106.900 101.439 1.00 13.46  ? 1026 ILE A CA    1 
ATOM   7947  C  C     . ILE A 1  1026 ? 108.930 106.065 102.061 1.00 15.17  ? 1026 ILE A C     1 
ATOM   7948  O  O     . ILE A 1  1026 ? 109.488 106.426 103.101 1.00 13.05  ? 1026 ILE A O     1 
ATOM   7949  C  CB    . ILE A 1  1026 ? 106.434 106.398 101.868 1.00 13.94  ? 1026 ILE A CB    1 
ATOM   7950  C  CG1   . ILE A 1  1026 ? 105.338 107.317 101.344 1.00 14.18  ? 1026 ILE A CG1   1 
ATOM   7951  C  CG2   . ILE A 1  1026 ? 106.338 106.346 103.372 1.00 10.98  ? 1026 ILE A CG2   1 
ATOM   7952  C  CD1   . ILE A 1  1026 ? 103.956 106.778 101.575 1.00 10.02  ? 1026 ILE A CD1   1 
ATOM   7953  N  N     . ARG A 1  1027 ? 109.262 104.934 101.445 1.00 8.66   ? 1027 ARG A N     1 
ATOM   7954  C  CA    . ARG A 1  1027 ? 110.299 104.087 102.011 1.00 7.56   ? 1027 ARG A CA    1 
ATOM   7955  C  C     . ARG A 1  1027 ? 111.678 104.703 101.842 1.00 12.05  ? 1027 ARG A C     1 
ATOM   7956  O  O     . ARG A 1  1027 ? 112.552 104.497 102.687 1.00 18.64  ? 1027 ARG A O     1 
ATOM   7957  C  CB    . ARG A 1  1027 ? 110.241 102.700 101.387 1.00 8.28   ? 1027 ARG A CB    1 
ATOM   7958  C  CG    . ARG A 1  1027 ? 111.252 101.735 101.955 1.00 12.66  ? 1027 ARG A CG    1 
ATOM   7959  C  CD    . ARG A 1  1027 ? 110.941 100.322 101.555 1.00 14.55  ? 1027 ARG A CD    1 
ATOM   7960  N  NE    . ARG A 1  1027 ? 110.379 99.563  102.664 1.00 19.43  ? 1027 ARG A NE    1 
ATOM   7961  C  CZ    . ARG A 1  1027 ? 111.065 98.721  103.423 1.00 16.00  ? 1027 ARG A CZ    1 
ATOM   7962  N  NH1   . ARG A 1  1027 ? 112.353 98.497  103.219 1.00 17.40  ? 1027 ARG A NH1   1 
ATOM   7963  N  NH2   . ARG A 1  1027 ? 110.440 98.077  104.403 1.00 7.46   ? 1027 ARG A NH2   1 
ATOM   7964  N  N     . LEU A 1  1028 ? 111.898 105.452 100.765 1.00 8.88   ? 1028 LEU A N     1 
ATOM   7965  C  CA    . LEU A 1  1028 ? 113.179 106.121 100.579 1.00 8.74   ? 1028 LEU A CA    1 
ATOM   7966  C  C     . LEU A 1  1028 ? 113.398 107.205 101.624 1.00 4.21   ? 1028 LEU A C     1 
ATOM   7967  O  O     . LEU A 1  1028 ? 114.488 107.328 102.181 1.00 4.67   ? 1028 LEU A O     1 
ATOM   7968  C  CB    . LEU A 1  1028 ? 113.260 106.709 99.177  1.00 11.50  ? 1028 LEU A CB    1 
ATOM   7969  C  CG    . LEU A 1  1028 ? 114.607 107.307 98.791  1.00 7.00   ? 1028 LEU A CG    1 
ATOM   7970  C  CD1   . LEU A 1  1028 ? 115.624 106.214 98.600  1.00 11.03  ? 1028 LEU A CD1   1 
ATOM   7971  C  CD2   . LEU A 1  1028 ? 114.469 108.134 97.550  1.00 8.69   ? 1028 LEU A CD2   1 
ATOM   7972  N  N     . GLN A 1  1029 ? 112.374 108.005 101.901 1.00 1.98   ? 1029 GLN A N     1 
ATOM   7973  C  CA    . GLN A 1  1029 ? 112.527 109.098 102.851 1.00 1.92   ? 1029 GLN A CA    1 
ATOM   7974  C  C     . GLN A 1  1029 ? 112.630 108.600 104.281 1.00 9.13   ? 1029 GLN A C     1 
ATOM   7975  O  O     . GLN A 1  1029 ? 113.224 109.271 105.126 1.00 14.08  ? 1029 GLN A O     1 
ATOM   7976  C  CB    . GLN A 1  1029 ? 111.355 110.060 102.741 1.00 3.87   ? 1029 GLN A CB    1 
ATOM   7977  C  CG    . GLN A 1  1029 ? 111.218 110.740 101.419 1.00 8.08   ? 1029 GLN A CG    1 
ATOM   7978  C  CD    . GLN A 1  1029 ? 110.433 112.014 101.546 1.00 14.85  ? 1029 GLN A CD    1 
ATOM   7979  O  OE1   . GLN A 1  1029 ? 110.117 112.446 102.651 1.00 19.60  ? 1029 GLN A OE1   1 
ATOM   7980  N  NE2   . GLN A 1  1029 ? 110.108 112.626 100.420 1.00 14.96  ? 1029 GLN A NE2   1 
ATOM   7981  N  N     . TYR A 1  1030 ? 112.016 107.458 104.575 1.00 13.11  ? 1030 TYR A N     1 
ATOM   7982  C  CA    . TYR A 1  1030 ? 112.100 106.838 105.889 1.00 7.09   ? 1030 TYR A CA    1 
ATOM   7983  C  C     . TYR A 1  1030 ? 113.499 106.307 106.161 1.00 1.20   ? 1030 TYR A C     1 
ATOM   7984  O  O     . TYR A 1  1030 ? 113.990 106.392 107.289 1.00 5.76   ? 1030 TYR A O     1 
ATOM   7985  C  CB    . TYR A 1  1030 ? 111.056 105.730 105.973 1.00 0.19   ? 1030 TYR A CB    1 
ATOM   7986  C  CG    . TYR A 1  1030 ? 110.574 105.368 107.349 1.00 2.65   ? 1030 TYR A CG    1 
ATOM   7987  C  CD1   . TYR A 1  1030 ? 111.191 105.855 108.484 1.00 3.29   ? 1030 TYR A CD1   1 
ATOM   7988  C  CD2   . TYR A 1  1030 ? 109.475 104.557 107.508 1.00 6.67   ? 1030 TYR A CD2   1 
ATOM   7989  C  CE1   . TYR A 1  1030 ? 110.744 105.518 109.730 1.00 1.33   ? 1030 TYR A CE1   1 
ATOM   7990  C  CE2   . TYR A 1  1030 ? 109.020 104.220 108.755 1.00 5.94   ? 1030 TYR A CE2   1 
ATOM   7991  C  CZ    . TYR A 1  1030 ? 109.657 104.704 109.859 1.00 2.65   ? 1030 TYR A CZ    1 
ATOM   7992  O  OH    . TYR A 1  1030 ? 109.201 104.365 111.101 1.00 3.60   ? 1030 TYR A OH    1 
ATOM   7993  N  N     . THR A 1  1031 ? 114.145 105.749 105.141 1.00 11.48  ? 1031 THR A N     1 
ATOM   7994  C  CA    . THR A 1  1031 ? 115.526 105.303 105.267 1.00 2.34   ? 1031 THR A CA    1 
ATOM   7995  C  C     . THR A 1  1031 ? 116.470 106.472 105.514 1.00 3.07   ? 1031 THR A C     1 
ATOM   7996  O  O     . THR A 1  1031 ? 117.445 106.348 106.262 1.00 8.56   ? 1031 THR A O     1 
ATOM   7997  C  CB    . THR A 1  1031 ? 115.922 104.537 104.005 1.00 2.23   ? 1031 THR A CB    1 
ATOM   7998  O  OG1   . THR A 1  1031 ? 115.309 103.246 104.015 1.00 4.49   ? 1031 THR A OG1   1 
ATOM   7999  C  CG2   . THR A 1  1031 ? 117.414 104.382 103.888 1.00 0.84   ? 1031 THR A CG2   1 
ATOM   8000  N  N     . GLN A 1  1032 ? 116.202 107.615 104.886 1.00 2.56   ? 1032 GLN A N     1 
ATOM   8001  C  CA    . GLN A 1  1032 ? 117.077 108.773 104.988 1.00 1.54   ? 1032 GLN A CA    1 
ATOM   8002  C  C     . GLN A 1  1032 ? 116.962 109.504 106.311 1.00 5.64   ? 1032 GLN A C     1 
ATOM   8003  O  O     . GLN A 1  1032 ? 117.751 110.416 106.561 1.00 10.63  ? 1032 GLN A O     1 
ATOM   8004  C  CB    . GLN A 1  1032 ? 116.787 109.735 103.849 1.00 1.77   ? 1032 GLN A CB    1 
ATOM   8005  C  CG    . GLN A 1  1032 ? 117.214 109.203 102.528 1.00 3.80   ? 1032 GLN A CG    1 
ATOM   8006  C  CD    . GLN A 1  1032 ? 116.711 110.015 101.378 1.00 14.16  ? 1032 GLN A CD    1 
ATOM   8007  O  OE1   . GLN A 1  1032 ? 115.879 110.900 101.540 1.00 13.56  ? 1032 GLN A OE1   1 
ATOM   8008  N  NE2   . GLN A 1  1032 ? 117.216 109.718 100.193 1.00 11.22  ? 1032 GLN A NE2   1 
ATOM   8009  N  N     . SER A 1  1033 ? 116.010 109.143 107.153 1.00 1.32   ? 1033 SER A N     1 
ATOM   8010  C  CA    . SER A 1  1033 ? 115.805 109.818 108.418 1.00 4.78   ? 1033 SER A CA    1 
ATOM   8011  C  C     . SER A 1  1033 ? 116.238 109.000 109.626 1.00 14.80  ? 1033 SER A C     1 
ATOM   8012  O  O     . SER A 1  1033 ? 116.066 109.461 110.750 1.00 4.39   ? 1033 SER A O     1 
ATOM   8013  C  CB    . SER A 1  1033 ? 114.340 110.235 108.539 1.00 1.11   ? 1033 SER A CB    1 
ATOM   8014  O  OG    . SER A 1  1033 ? 113.481 109.170 108.233 1.00 2.18   ? 1033 SER A OG    1 
ATOM   8015  N  N     . LEU A 1  1034 ? 116.828 107.828 109.427 1.00 6.57   ? 1034 LEU A N     1 
ATOM   8016  C  CA    . LEU A 1  1034 ? 117.279 106.996 110.530 1.00 4.27   ? 1034 LEU A CA    1 
ATOM   8017  C  C     . LEU A 1  1034 ? 118.628 107.470 111.058 1.00 0.67   ? 1034 LEU A C     1 
ATOM   8018  O  O     . LEU A 1  1034 ? 119.427 108.055 110.330 1.00 6.15   ? 1034 LEU A O     1 
ATOM   8019  C  CB    . LEU A 1  1034 ? 117.370 105.540 110.087 1.00 12.79  ? 1034 LEU A CB    1 
ATOM   8020  C  CG    . LEU A 1  1034 ? 116.078 104.874 109.630 1.00 13.33  ? 1034 LEU A CG    1 
ATOM   8021  C  CD1   . LEU A 1  1034 ? 116.314 103.471 109.179 1.00 10.98  ? 1034 LEU A CD1   1 
ATOM   8022  C  CD2   . LEU A 1  1034 ? 115.062 104.901 110.728 1.00 15.14  ? 1034 LEU A CD2   1 
ATOM   8023  N  N     . ILE A 1  1035 ? 118.880 107.210 112.340 1.00 6.01   ? 1035 ILE A N     1 
ATOM   8024  C  CA    . ILE A 1  1035 ? 120.109 107.673 112.975 1.00 5.91   ? 1035 ILE A CA    1 
ATOM   8025  C  C     . ILE A 1  1035 ? 121.283 106.786 112.553 1.00 4.90   ? 1035 ILE A C     1 
ATOM   8026  O  O     . ILE A 1  1035 ? 121.137 105.580 112.340 1.00 8.41   ? 1035 ILE A O     1 
ATOM   8027  C  CB    . ILE A 1  1035 ? 119.926 107.715 114.507 1.00 1.27   ? 1035 ILE A CB    1 
ATOM   8028  C  CG1   . ILE A 1  1035 ? 121.066 108.455 115.198 1.00 13.42  ? 1035 ILE A CG1   1 
ATOM   8029  C  CG2   . ILE A 1  1035 ? 119.782 106.338 115.090 1.00 3.26   ? 1035 ILE A CG2   1 
ATOM   8030  C  CD1   . ILE A 1  1035 ? 120.945 109.923 115.182 1.00 8.72   ? 1035 ILE A CD1   1 
ATOM   8031  N  N     . ASN A 1  1036 ? 122.458 107.392 112.409 1.00 12.75  ? 1036 ASN A N     1 
ATOM   8032  C  CA    . ASN A 1  1036 ? 123.630 106.688 111.912 1.00 10.83  ? 1036 ASN A CA    1 
ATOM   8033  C  C     . ASN A 1  1036 ? 124.292 105.874 113.013 1.00 12.69  ? 1036 ASN A C     1 
ATOM   8034  O  O     . ASN A 1  1036 ? 124.338 106.285 114.171 1.00 20.18  ? 1036 ASN A O     1 
ATOM   8035  C  CB    . ASN A 1  1036 ? 124.673 107.660 111.361 1.00 14.71  ? 1036 ASN A CB    1 
ATOM   8036  C  CG    . ASN A 1  1036 ? 124.325 108.198 110.005 1.00 16.06  ? 1036 ASN A CG    1 
ATOM   8037  O  OD1   . ASN A 1  1036 ? 123.418 107.722 109.340 1.00 15.63  ? 1036 ASN A OD1   1 
ATOM   8038  N  ND2   . ASN A 1  1036 ? 125.080 109.179 109.570 1.00 22.10  ? 1036 ASN A ND2   1 
ATOM   8039  N  N     . TYR A 1  1037 ? 124.838 104.726 112.630 1.00 3.49   ? 1037 TYR A N     1 
ATOM   8040  C  CA    . TYR A 1  1037 ? 125.635 103.928 113.546 1.00 8.09   ? 1037 TYR A CA    1 
ATOM   8041  C  C     . TYR A 1  1037 ? 126.857 104.715 113.987 1.00 4.07   ? 1037 TYR A C     1 
ATOM   8042  O  O     . TYR A 1  1037 ? 127.561 105.295 113.161 1.00 11.75  ? 1037 TYR A O     1 
ATOM   8043  C  CB    . TYR A 1  1037 ? 126.097 102.647 112.867 1.00 10.86  ? 1037 TYR A CB    1 
ATOM   8044  C  CG    . TYR A 1  1037 ? 125.048 101.796 112.206 1.00 9.19   ? 1037 TYR A CG    1 
ATOM   8045  C  CD1   . TYR A 1  1037 ? 123.869 101.471 112.841 1.00 5.23   ? 1037 TYR A CD1   1 
ATOM   8046  C  CD2   . TYR A 1  1037 ? 125.249 101.318 110.927 1.00 4.48   ? 1037 TYR A CD2   1 
ATOM   8047  C  CE1   . TYR A 1  1037 ? 122.938 100.682 112.228 1.00 3.19   ? 1037 TYR A CE1   1 
ATOM   8048  C  CE2   . TYR A 1  1037 ? 124.319 100.541 110.310 1.00 9.80   ? 1037 TYR A CE2   1 
ATOM   8049  C  CZ    . TYR A 1  1037 ? 123.171 100.224 110.964 1.00 11.13  ? 1037 TYR A CZ    1 
ATOM   8050  O  OH    . TYR A 1  1037 ? 122.245 99.443  110.339 1.00 0.57   ? 1037 TYR A OH    1 
ATOM   8051  N  N     . GLY A 1  1038 ? 127.138 104.704 115.281 1.00 3.94   ? 1038 GLY A N     1 
ATOM   8052  C  CA    . GLY A 1  1038 ? 128.336 105.349 115.765 1.00 1.78   ? 1038 GLY A CA    1 
ATOM   8053  C  C     . GLY A 1  1038 ? 128.205 106.815 116.043 1.00 2.11   ? 1038 GLY A C     1 
ATOM   8054  O  O     . GLY A 1  1038 ? 129.214 107.503 116.156 1.00 9.93   ? 1038 GLY A O     1 
ATOM   8055  N  N     . GLU A 1  1039 ? 126.991 107.313 116.164 1.00 6.76   ? 1039 GLU A N     1 
ATOM   8056  C  CA    . GLU A 1  1039 ? 126.734 108.703 116.473 1.00 4.31   ? 1039 GLU A CA    1 
ATOM   8057  C  C     . GLU A 1  1039 ? 126.788 108.936 117.976 1.00 0.48   ? 1039 GLU A C     1 
ATOM   8058  O  O     . GLU A 1  1039 ? 126.261 108.143 118.754 1.00 4.10   ? 1039 GLU A O     1 
ATOM   8059  C  CB    . GLU A 1  1039 ? 125.376 109.100 115.914 1.00 9.55   ? 1039 GLU A CB    1 
ATOM   8060  C  CG    . GLU A 1  1039 ? 125.011 110.513 116.162 1.00 13.97  ? 1039 GLU A CG    1 
ATOM   8061  C  CD    . GLU A 1  1039 ? 124.711 111.237 114.890 1.00 8.92   ? 1039 GLU A CD    1 
ATOM   8062  O  OE1   . GLU A 1  1039 ? 124.181 110.608 113.959 1.00 16.47  ? 1039 GLU A OE1   1 
ATOM   8063  O  OE2   . GLU A 1  1039 ? 125.008 112.440 114.809 1.00 14.02  ? 1039 GLU A OE2   1 
ATOM   8064  N  N     . ALA A 1  1040 ? 127.436 110.026 118.374 1.00 19.53  ? 1040 ALA A N     1 
ATOM   8065  C  CA    . ALA A 1  1040 ? 127.558 110.416 119.773 1.00 15.03  ? 1040 ALA A CA    1 
ATOM   8066  C  C     . ALA A 1  1040 ? 126.312 111.194 120.181 1.00 11.67  ? 1040 ALA A C     1 
ATOM   8067  O  O     . ALA A 1  1040 ? 126.294 112.420 120.250 1.00 14.84  ? 1040 ALA A O     1 
ATOM   8068  C  CB    . ALA A 1  1040 ? 128.826 111.227 119.990 1.00 15.20  ? 1040 ALA A CB    1 
ATOM   8069  N  N     . VAL A 1  1041 ? 125.244 110.450 120.466 1.00 2.91   ? 1041 VAL A N     1 
ATOM   8070  C  CA    . VAL A 1  1041 ? 123.951 111.058 120.761 1.00 1.94   ? 1041 VAL A CA    1 
ATOM   8071  C  C     . VAL A 1  1041 ? 123.821 111.521 122.198 1.00 1.54   ? 1041 VAL A C     1 
ATOM   8072  O  O     . VAL A 1  1041 ? 122.896 112.273 122.508 1.00 4.10   ? 1041 VAL A O     1 
ATOM   8073  C  CB    . VAL A 1  1041 ? 122.813 110.082 120.419 1.00 9.82   ? 1041 VAL A CB    1 
ATOM   8074  C  CG1   . VAL A 1  1041 ? 122.698 109.937 118.928 1.00 6.42   ? 1041 VAL A CG1   1 
ATOM   8075  C  CG2   . VAL A 1  1041 ? 123.042 108.746 121.065 1.00 15.35  ? 1041 VAL A CG2   1 
ATOM   8076  N  N     . GLY A 1  1042 ? 124.713 111.087 123.084 1.00 11.17  ? 1042 GLY A N     1 
ATOM   8077  C  CA    . GLY A 1  1042 ? 124.757 111.650 124.415 1.00 7.10   ? 1042 GLY A CA    1 
ATOM   8078  C  C     . GLY A 1  1042 ? 125.367 113.032 124.461 1.00 5.35   ? 1042 GLY A C     1 
ATOM   8079  O  O     . GLY A 1  1042 ? 124.978 113.850 125.291 1.00 10.86  ? 1042 GLY A O     1 
ATOM   8080  N  N     . ILE A 1  1043 ? 126.346 113.308 123.598 1.00 4.34   ? 1043 ILE A N     1 
ATOM   8081  C  CA    . ILE A 1  1043 ? 126.861 114.669 123.484 1.00 4.99   ? 1043 ILE A CA    1 
ATOM   8082  C  C     . ILE A 1  1043 ? 125.823 115.580 122.846 1.00 4.88   ? 1043 ILE A C     1 
ATOM   8083  O  O     . ILE A 1  1043 ? 125.665 116.734 123.249 1.00 2.72   ? 1043 ILE A O     1 
ATOM   8084  C  CB    . ILE A 1  1043 ? 128.188 114.696 122.701 1.00 1.92   ? 1043 ILE A CB    1 
ATOM   8085  C  CG1   . ILE A 1  1043 ? 129.295 114.020 123.489 1.00 1.52   ? 1043 ILE A CG1   1 
ATOM   8086  C  CG2   . ILE A 1  1043 ? 128.617 116.112 122.425 1.00 6.27   ? 1043 ILE A CG2   1 
ATOM   8087  C  CD1   . ILE A 1  1043 ? 130.587 113.949 122.745 1.00 1.65   ? 1043 ILE A CD1   1 
ATOM   8088  N  N     . LEU A 1  1044 ? 125.098 115.078 121.847 1.00 5.51   ? 1044 LEU A N     1 
ATOM   8089  C  CA    . LEU A 1  1044 ? 124.053 115.869 121.210 1.00 3.51   ? 1044 LEU A CA    1 
ATOM   8090  C  C     . LEU A 1  1044 ? 122.969 116.264 122.199 1.00 6.03   ? 1044 LEU A C     1 
ATOM   8091  O  O     . LEU A 1  1044 ? 122.403 117.354 122.101 1.00 1.99   ? 1044 LEU A O     1 
ATOM   8092  C  CB    . LEU A 1  1044 ? 123.442 115.099 120.046 1.00 0.06   ? 1044 LEU A CB    1 
ATOM   8093  C  CG    . LEU A 1  1044 ? 124.330 114.814 118.841 1.00 11.91  ? 1044 LEU A CG    1 
ATOM   8094  C  CD1   . LEU A 1  1044 ? 123.568 114.003 117.837 1.00 13.03  ? 1044 LEU A CD1   1 
ATOM   8095  C  CD2   . LEU A 1  1044 ? 124.816 116.096 118.246 1.00 4.73   ? 1044 LEU A CD2   1 
ATOM   8096  N  N     . ALA A 1  1045 ? 122.645 115.376 123.138 1.00 1.20   ? 1045 ALA A N     1 
ATOM   8097  C  CA    . ALA A 1  1045 ? 121.620 115.661 124.133 1.00 1.22   ? 1045 ALA A CA    1 
ATOM   8098  C  C     . ALA A 1  1045 ? 122.099 116.670 125.164 1.00 2.86   ? 1045 ALA A C     1 
ATOM   8099  O  O     . ALA A 1  1045 ? 121.341 117.547 125.577 1.00 2.66   ? 1045 ALA A O     1 
ATOM   8100  C  CB    . ALA A 1  1045 ? 121.193 114.373 124.817 1.00 3.07   ? 1045 ALA A CB    1 
ATOM   8101  N  N     . ALA A 1  1046 ? 123.347 116.549 125.604 1.00 0.83   ? 1046 ALA A N     1 
ATOM   8102  C  CA    . ALA A 1  1046 ? 123.895 117.489 126.570 1.00 11.44  ? 1046 ALA A CA    1 
ATOM   8103  C  C     . ALA A 1  1046 ? 123.964 118.896 125.998 1.00 1.29   ? 1046 ALA A C     1 
ATOM   8104  O  O     . ALA A 1  1046 ? 123.718 119.873 126.709 1.00 12.50  ? 1046 ALA A O     1 
ATOM   8105  C  CB    . ALA A 1  1046 ? 125.269 117.021 127.023 1.00 9.61   ? 1046 ALA A CB    1 
ATOM   8106  N  N     . GLN A 1  1047 ? 124.309 119.023 124.720 1.00 7.24   ? 1047 GLN A N     1 
ATOM   8107  C  CA    . GLN A 1  1047 ? 124.318 120.330 124.076 1.00 2.98   ? 1047 GLN A CA    1 
ATOM   8108  C  C     . GLN A 1  1047 ? 122.918 120.904 123.952 1.00 5.78   ? 1047 GLN A C     1 
ATOM   8109  O  O     . GLN A 1  1047 ? 122.718 122.105 124.142 1.00 11.14  ? 1047 GLN A O     1 
ATOM   8110  C  CB    . GLN A 1  1047 ? 124.955 120.231 122.700 1.00 11.15  ? 1047 GLN A CB    1 
ATOM   8111  C  CG    . GLN A 1  1047 ? 126.444 120.159 122.714 1.00 1.33   ? 1047 GLN A CG    1 
ATOM   8112  C  CD    . GLN A 1  1047 ? 126.997 119.844 121.356 1.00 3.29   ? 1047 GLN A CD    1 
ATOM   8113  O  OE1   . GLN A 1  1047 ? 126.282 119.361 120.486 1.00 1.50   ? 1047 GLN A OE1   1 
ATOM   8114  N  NE2   . GLN A 1  1047 ? 128.275 120.126 121.158 1.00 15.19  ? 1047 GLN A NE2   1 
ATOM   8115  N  N     . SER A 1  1048 ? 121.941 120.066 123.621 1.00 3.85   ? 1048 SER A N     1 
ATOM   8116  C  CA    . SER A 1  1048 ? 120.607 120.546 123.291 1.00 1.49   ? 1048 SER A CA    1 
ATOM   8117  C  C     . SER A 1  1048 ? 119.790 120.908 124.513 1.00 11.33  ? 1048 SER A C     1 
ATOM   8118  O  O     . SER A 1  1048 ? 118.793 121.618 124.388 1.00 14.06  ? 1048 SER A O     1 
ATOM   8119  C  CB    . SER A 1  1048 ? 119.870 119.499 122.472 1.00 11.76  ? 1048 SER A CB    1 
ATOM   8120  O  OG    . SER A 1  1048 ? 120.612 119.157 121.328 1.00 1.72   ? 1048 SER A OG    1 
ATOM   8121  N  N     . VAL A 1  1049 ? 120.170 120.427 125.688 1.00 4.86   ? 1049 VAL A N     1 
ATOM   8122  C  CA    . VAL A 1  1049 ? 119.408 120.714 126.891 1.00 2.40   ? 1049 VAL A CA    1 
ATOM   8123  C  C     . VAL A 1  1049 ? 120.063 121.814 127.716 1.00 7.31   ? 1049 VAL A C     1 
ATOM   8124  O  O     . VAL A 1  1049 ? 119.370 122.586 128.379 1.00 19.25  ? 1049 VAL A O     1 
ATOM   8125  C  CB    . VAL A 1  1049 ? 119.212 119.419 127.699 1.00 2.12   ? 1049 VAL A CB    1 
ATOM   8126  C  CG1   . VAL A 1  1049 ? 118.792 119.696 129.118 1.00 5.06   ? 1049 VAL A CG1   1 
ATOM   8127  C  CG2   . VAL A 1  1049 ? 118.175 118.541 127.025 1.00 9.10   ? 1049 VAL A CG2   1 
ATOM   8128  N  N     . SER A 1  1050 ? 121.383 121.931 127.662 1.00 11.59  ? 1050 SER A N     1 
ATOM   8129  C  CA    . SER A 1  1050 ? 122.058 123.023 128.344 1.00 12.86  ? 1050 SER A CA    1 
ATOM   8130  C  C     . SER A 1  1050 ? 121.830 124.370 127.680 1.00 16.09  ? 1050 SER A C     1 
ATOM   8131  O  O     . SER A 1  1050 ? 122.068 125.398 128.316 1.00 21.71  ? 1050 SER A O     1 
ATOM   8132  C  CB    . SER A 1  1050 ? 123.549 122.734 128.429 1.00 12.23  ? 1050 SER A CB    1 
ATOM   8133  O  OG    . SER A 1  1050 ? 123.782 121.582 129.214 1.00 20.07  ? 1050 SER A OG    1 
ATOM   8134  N  N     . GLU A 1  1051 ? 121.370 124.398 126.440 1.00 21.51  ? 1051 GLU A N     1 
ATOM   8135  C  CA    . GLU A 1  1051 ? 121.096 125.669 125.787 1.00 22.61  ? 1051 GLU A CA    1 
ATOM   8136  C  C     . GLU A 1  1051 ? 119.835 126.324 126.353 1.00 25.20  ? 1051 GLU A C     1 
ATOM   8137  O  O     . GLU A 1  1051 ? 119.883 127.505 126.713 1.00 28.29  ? 1051 GLU A O     1 
ATOM   8138  C  CB    . GLU A 1  1051 ? 120.995 125.485 124.272 1.00 21.01  ? 1051 GLU A CB    1 
ATOM   8139  C  CG    . GLU A 1  1051 ? 121.387 126.719 123.477 1.00 24.76  ? 1051 GLU A CG    1 
ATOM   8140  C  CD    . GLU A 1  1051 ? 122.844 126.694 123.040 1.00 29.89  ? 1051 GLU A CD    1 
ATOM   8141  O  OE1   . GLU A 1  1051 ? 123.235 127.551 122.217 1.00 29.46  ? 1051 GLU A OE1   1 
ATOM   8142  O  OE2   . GLU A 1  1051 ? 123.596 125.816 123.518 1.00 26.65  ? 1051 GLU A OE2   1 
ATOM   8143  N  N     . PRO A 1  1052 ? 118.695 125.626 126.453 1.00 21.64  ? 1052 PRO A N     1 
ATOM   8144  C  CA    . PRO A 1  1052 ? 117.530 126.232 127.115 1.00 21.47  ? 1052 PRO A CA    1 
ATOM   8145  C  C     . PRO A 1  1052 ? 117.725 126.533 128.594 1.00 23.33  ? 1052 PRO A C     1 
ATOM   8146  O  O     . PRO A 1  1052 ? 116.915 127.276 129.155 1.00 30.81  ? 1052 PRO A O     1 
ATOM   8147  C  CB    . PRO A 1  1052 ? 116.429 125.186 126.909 1.00 24.66  ? 1052 PRO A CB    1 
ATOM   8148  C  CG    . PRO A 1  1052 ? 116.849 124.442 125.721 1.00 21.83  ? 1052 PRO A CG    1 
ATOM   8149  C  CD    . PRO A 1  1052 ? 118.322 124.346 125.828 1.00 19.98  ? 1052 PRO A CD    1 
ATOM   8150  N  N     . LEU A 1  1053 ? 118.736 125.970 129.255 1.00 21.59  ? 1053 LEU A N     1 
ATOM   8151  C  CA    . LEU A 1  1053 ? 118.975 126.328 130.647 1.00 24.46  ? 1053 LEU A CA    1 
ATOM   8152  C  C     . LEU A 1  1053 ? 119.539 127.730 130.802 1.00 29.80  ? 1053 LEU A C     1 
ATOM   8153  O  O     . LEU A 1  1053 ? 119.494 128.281 131.903 1.00 33.50  ? 1053 LEU A O     1 
ATOM   8154  C  CB    . LEU A 1  1053 ? 119.924 125.341 131.314 1.00 24.35  ? 1053 LEU A CB    1 
ATOM   8155  C  CG    . LEU A 1  1053 ? 119.310 124.039 131.786 1.00 23.87  ? 1053 LEU A CG    1 
ATOM   8156  C  CD1   . LEU A 1  1053 ? 120.376 123.185 132.411 1.00 27.08  ? 1053 LEU A CD1   1 
ATOM   8157  C  CD2   . LEU A 1  1053 ? 118.227 124.341 132.771 1.00 27.78  ? 1053 LEU A CD2   1 
ATOM   8158  N  N     . THR A 1  1054 ? 120.095 128.309 129.741 1.00 38.68  ? 1054 THR A N     1 
ATOM   8159  C  CA    . THR A 1  1054 ? 120.592 129.676 129.831 1.00 38.83  ? 1054 THR A CA    1 
ATOM   8160  C  C     . THR A 1  1054 ? 119.454 130.653 130.080 1.00 39.25  ? 1054 THR A C     1 
ATOM   8161  O  O     . THR A 1  1054 ? 119.552 131.528 130.945 1.00 41.74  ? 1054 THR A O     1 
ATOM   8162  C  CB    . THR A 1  1054 ? 121.358 130.037 128.562 1.00 39.61  ? 1054 THR A CB    1 
ATOM   8163  O  OG1   . THR A 1  1054 ? 122.674 129.477 128.633 1.00 38.31  ? 1054 THR A OG1   1 
ATOM   8164  C  CG2   . THR A 1  1054 ? 121.448 131.542 128.393 1.00 37.27  ? 1054 THR A CG2   1 
ATOM   8165  N  N     . GLN A 1  1055 ? 118.351 130.494 129.358 1.00 38.07  ? 1055 GLN A N     1 
ATOM   8166  C  CA    . GLN A 1  1055 ? 117.188 131.353 129.518 1.00 36.10  ? 1055 GLN A CA    1 
ATOM   8167  C  C     . GLN A 1  1055 ? 116.324 130.952 130.697 1.00 37.11  ? 1055 GLN A C     1 
ATOM   8168  O  O     . GLN A 1  1055 ? 115.116 131.198 130.681 1.00 42.30  ? 1055 GLN A O     1 
ATOM   8169  C  CB    . GLN A 1  1055 ? 116.365 131.369 128.227 1.00 38.68  ? 1055 GLN A CB    1 
ATOM   8170  C  CG    . GLN A 1  1055 ? 115.962 129.999 127.717 1.00 41.63  ? 1055 GLN A CG    1 
ATOM   8171  C  CD    . GLN A 1  1055 ? 114.556 129.605 128.133 1.00 44.80  ? 1055 GLN A CD    1 
ATOM   8172  O  OE1   . GLN A 1  1055 ? 113.636 130.423 128.104 1.00 46.80  ? 1055 GLN A OE1   1 
ATOM   8173  N  NE2   . GLN A 1  1055 ? 114.386 128.350 128.533 1.00 41.17  ? 1055 GLN A NE2   1 
ATOM   8174  N  N     . TYR A 1  1056 ? 116.915 130.332 131.711 1.00 37.23  ? 1056 TYR A N     1 
ATOM   8175  C  CA    . TYR A 1  1056 ? 116.192 129.921 132.902 1.00 40.28  ? 1056 TYR A CA    1 
ATOM   8176  C  C     . TYR A 1  1056 ? 116.974 130.268 134.163 1.00 38.03  ? 1056 TYR A C     1 
ATOM   8177  O  O     . TYR A 1  1056 ? 117.688 131.267 134.209 1.00 35.79  ? 1056 TYR A O     1 
ATOM   8178  C  CB    . TYR A 1  1056 ? 115.913 128.424 132.858 1.00 37.59  ? 1056 TYR A CB    1 
ATOM   8179  C  CG    . TYR A 1  1056 ? 114.886 127.962 133.856 1.00 38.30  ? 1056 TYR A CG    1 
ATOM   8180  C  CD1   . TYR A 1  1056 ? 115.272 127.397 135.058 1.00 36.27  ? 1056 TYR A CD1   1 
ATOM   8181  C  CD2   . TYR A 1  1056 ? 113.531 128.074 133.592 1.00 37.22  ? 1056 TYR A CD2   1 
ATOM   8182  C  CE1   . TYR A 1  1056 ? 114.345 126.968 135.972 1.00 34.36  ? 1056 TYR A CE1   1 
ATOM   8183  C  CE2   . TYR A 1  1056 ? 112.595 127.641 134.501 1.00 37.70  ? 1056 TYR A CE2   1 
ATOM   8184  C  CZ    . TYR A 1  1056 ? 113.011 127.090 135.691 1.00 36.79  ? 1056 TYR A CZ    1 
ATOM   8185  O  OH    . TYR A 1  1056 ? 112.088 126.659 136.608 1.00 36.50  ? 1056 TYR A OH    1 
ATOM   8186  N  N     . GLY A 1  1073 ? 120.186 128.410 135.697 1.00 29.13  ? 1073 GLY A N     1 
ATOM   8187  C  CA    . GLY A 1  1073 ? 120.777 127.436 136.597 1.00 29.71  ? 1073 GLY A CA    1 
ATOM   8188  C  C     . GLY A 1  1073 ? 120.305 127.592 138.026 1.00 35.59  ? 1073 GLY A C     1 
ATOM   8189  O  O     . GLY A 1  1073 ? 121.094 127.526 138.967 1.00 36.52  ? 1073 GLY A O     1 
ATOM   8190  N  N     . ILE A 1  1074 ? 119.002 127.802 138.183 1.00 39.78  ? 1074 ILE A N     1 
ATOM   8191  C  CA    . ILE A 1  1074 ? 118.377 127.996 139.486 1.00 38.73  ? 1074 ILE A CA    1 
ATOM   8192  C  C     . ILE A 1  1074 ? 118.311 126.671 140.237 1.00 36.31  ? 1074 ILE A C     1 
ATOM   8193  O  O     . ILE A 1  1074 ? 118.739 125.633 139.726 1.00 35.76  ? 1074 ILE A O     1 
ATOM   8194  C  CB    . ILE A 1  1074 ? 116.991 128.655 139.344 1.00 36.49  ? 1074 ILE A CB    1 
ATOM   8195  C  CG1   . ILE A 1  1074 ? 116.744 129.610 140.514 1.00 35.55  ? 1074 ILE A CG1   1 
ATOM   8196  C  CG2   . ILE A 1  1074 ? 115.879 127.610 139.206 1.00 36.59  ? 1074 ILE A CG2   1 
ATOM   8197  C  CD1   . ILE A 1  1074 ? 115.673 130.629 140.248 1.00 36.28  ? 1074 ILE A CD1   1 
ATOM   8198  N  N     . VAL A 1  1075 ? 117.843 126.719 141.482 1.00 28.13  ? 1075 VAL A N     1 
ATOM   8199  C  CA    . VAL A 1  1075 ? 117.856 125.590 142.407 1.00 29.17  ? 1075 VAL A CA    1 
ATOM   8200  C  C     . VAL A 1  1075 ? 117.129 124.357 141.874 1.00 29.39  ? 1075 VAL A C     1 
ATOM   8201  O  O     . VAL A 1  1075 ? 117.504 123.227 142.202 1.00 26.91  ? 1075 VAL A O     1 
ATOM   8202  C  CB    . VAL A 1  1075 ? 117.264 126.026 143.758 1.00 29.24  ? 1075 VAL A CB    1 
ATOM   8203  C  CG1   . VAL A 1  1075 ? 117.651 125.054 144.847 1.00 28.03  ? 1075 VAL A CG1   1 
ATOM   8204  C  CG2   . VAL A 1  1075 ? 117.742 127.417 144.097 1.00 30.13  ? 1075 VAL A CG2   1 
ATOM   8205  N  N     . ARG A 1  1076 ? 116.068 124.549 141.089 1.00 26.37  ? 1076 ARG A N     1 
ATOM   8206  C  CA    . ARG A 1  1076 ? 115.306 123.394 140.611 1.00 25.12  ? 1076 ARG A CA    1 
ATOM   8207  C  C     . ARG A 1  1076 ? 116.094 122.503 139.654 1.00 26.44  ? 1076 ARG A C     1 
ATOM   8208  O  O     . ARG A 1  1076 ? 116.110 121.279 139.872 1.00 24.49  ? 1076 ARG A O     1 
ATOM   8209  C  CB    . ARG A 1  1076 ? 113.980 123.857 139.995 1.00 23.22  ? 1076 ARG A CB    1 
ATOM   8210  C  CG    . ARG A 1  1076 ? 113.096 122.728 139.503 1.00 18.48  ? 1076 ARG A CG    1 
ATOM   8211  C  CD    . ARG A 1  1076 ? 112.937 121.668 140.552 1.00 21.93  ? 1076 ARG A CD    1 
ATOM   8212  N  NE    . ARG A 1  1076 ? 111.930 120.680 140.198 1.00 22.62  ? 1076 ARG A NE    1 
ATOM   8213  C  CZ    . ARG A 1  1076 ? 111.883 119.454 140.696 1.00 23.45  ? 1076 ARG A CZ    1 
ATOM   8214  N  NH1   . ARG A 1  1076 ? 112.783 119.025 141.562 1.00 21.89  ? 1076 ARG A NH1   1 
ATOM   8215  N  NH2   . ARG A 1  1076 ? 110.902 118.642 140.325 1.00 16.30  ? 1076 ARG A NH2   1 
ATOM   8216  N  N     . PRO A 1  1077 ? 116.746 123.011 138.595 1.00 27.84  ? 1077 PRO A N     1 
ATOM   8217  C  CA    . PRO A 1  1077 ? 117.529 122.102 137.740 1.00 24.63  ? 1077 PRO A CA    1 
ATOM   8218  C  C     . PRO A 1  1077 ? 118.577 121.307 138.493 1.00 22.69  ? 1077 PRO A C     1 
ATOM   8219  O  O     . PRO A 1  1077 ? 118.768 120.123 138.207 1.00 25.35  ? 1077 PRO A O     1 
ATOM   8220  C  CB    . PRO A 1  1077 ? 118.170 123.054 136.726 1.00 25.40  ? 1077 PRO A CB    1 
ATOM   8221  C  CG    . PRO A 1  1077 ? 117.234 124.162 136.627 1.00 24.95  ? 1077 PRO A CG    1 
ATOM   8222  C  CD    . PRO A 1  1077 ? 116.603 124.334 137.967 1.00 28.61  ? 1077 PRO A CD    1 
ATOM   8223  N  N     . GLN A 1  1078 ? 119.251 121.922 139.461 1.00 25.27  ? 1078 GLN A N     1 
ATOM   8224  C  CA    . GLN A 1  1078 ? 120.262 121.229 140.243 1.00 25.89  ? 1078 GLN A CA    1 
ATOM   8225  C  C     . GLN A 1  1078 ? 119.671 120.149 141.129 1.00 28.50  ? 1078 GLN A C     1 
ATOM   8226  O  O     . GLN A 1  1078 ? 120.388 119.227 141.517 1.00 24.03  ? 1078 GLN A O     1 
ATOM   8227  C  CB    . GLN A 1  1078 ? 121.038 122.245 141.077 1.00 25.45  ? 1078 GLN A CB    1 
ATOM   8228  C  CG    . GLN A 1  1078 ? 122.464 121.843 141.396 1.00 31.44  ? 1078 GLN A CG    1 
ATOM   8229  C  CD    . GLN A 1  1078 ? 122.802 121.971 142.871 1.00 35.17  ? 1078 GLN A CD    1 
ATOM   8230  O  OE1   . GLN A 1  1078 ? 121.940 121.833 143.737 1.00 33.89  ? 1078 GLN A OE1   1 
ATOM   8231  N  NE2   . GLN A 1  1078 ? 124.067 122.251 143.161 1.00 33.37  ? 1078 GLN A NE2   1 
ATOM   8232  N  N     . GLU A 1  1079 ? 118.390 120.243 141.458 1.00 31.25  ? 1079 GLU A N     1 
ATOM   8233  C  CA    . GLU A 1  1079 ? 117.677 119.183 142.149 1.00 28.07  ? 1079 GLU A CA    1 
ATOM   8234  C  C     . GLU A 1  1079 ? 117.455 117.969 141.273 1.00 27.82  ? 1079 GLU A C     1 
ATOM   8235  O  O     . GLU A 1  1079 ? 117.609 116.838 141.740 1.00 29.83  ? 1079 GLU A O     1 
ATOM   8236  C  CB    . GLU A 1  1079 ? 116.320 119.700 142.614 1.00 32.87  ? 1079 GLU A CB    1 
ATOM   8237  C  CG    . GLU A 1  1079 ? 116.271 120.199 144.022 1.00 32.10  ? 1079 GLU A CG    1 
ATOM   8238  C  CD    . GLU A 1  1079 ? 114.889 120.665 144.383 1.00 35.79  ? 1079 GLU A CD    1 
ATOM   8239  O  OE1   . GLU A 1  1079 ? 114.190 119.921 145.081 1.00 37.85  ? 1079 GLU A OE1   1 
ATOM   8240  O  OE2   . GLU A 1  1079 ? 114.502 121.779 143.977 1.00 34.74  ? 1079 GLU A OE2   1 
ATOM   8241  N  N     . ILE A 1  1080 ? 117.076 118.193 140.017 1.00 23.24  ? 1080 ILE A N     1 
ATOM   8242  C  CA    . ILE A 1  1080 ? 116.825 117.099 139.089 1.00 19.25  ? 1080 ILE A CA    1 
ATOM   8243  C  C     . ILE A 1  1080 ? 118.123 116.400 138.715 1.00 16.99  ? 1080 ILE A C     1 
ATOM   8244  O  O     . ILE A 1  1080 ? 118.211 115.170 138.737 1.00 17.84  ? 1080 ILE A O     1 
ATOM   8245  C  CB    . ILE A 1  1080 ? 116.096 117.629 137.845 1.00 17.17  ? 1080 ILE A CB    1 
ATOM   8246  C  CG1   . ILE A 1  1080 ? 114.768 118.266 138.245 1.00 15.91  ? 1080 ILE A CG1   1 
ATOM   8247  C  CG2   . ILE A 1  1080 ? 115.906 116.523 136.828 1.00 19.06  ? 1080 ILE A CG2   1 
ATOM   8248  C  CD1   . ILE A 1  1080 ? 114.169 119.138 137.187 1.00 16.64  ? 1080 ILE A CD1   1 
ATOM   8249  N  N     . PHE A 1  1081 ? 119.152 117.172 138.370 1.00 18.57  ? 1081 PHE A N     1 
ATOM   8250  C  CA    . PHE A 1  1081 ? 120.372 116.594 137.824 1.00 12.12  ? 1081 PHE A CA    1 
ATOM   8251  C  C     . PHE A 1  1081 ? 121.319 116.058 138.887 1.00 17.78  ? 1081 PHE A C     1 
ATOM   8252  O  O     . PHE A 1  1081 ? 122.208 115.273 138.553 1.00 20.99  ? 1081 PHE A O     1 
ATOM   8253  C  CB    . PHE A 1  1081 ? 121.087 117.619 136.947 1.00 11.77  ? 1081 PHE A CB    1 
ATOM   8254  C  CG    . PHE A 1  1081 ? 120.297 118.036 135.745 1.00 15.15  ? 1081 PHE A CG    1 
ATOM   8255  C  CD1   . PHE A 1  1081 ? 119.572 117.108 135.029 1.00 12.13  ? 1081 PHE A CD1   1 
ATOM   8256  C  CD2   . PHE A 1  1081 ? 120.282 119.348 135.327 1.00 15.37  ? 1081 PHE A CD2   1 
ATOM   8257  C  CE1   . PHE A 1  1081 ? 118.846 117.483 133.934 1.00 10.30  ? 1081 PHE A CE1   1 
ATOM   8258  C  CE2   . PHE A 1  1081 ? 119.555 119.724 134.228 1.00 11.78  ? 1081 PHE A CE2   1 
ATOM   8259  C  CZ    . PHE A 1  1081 ? 118.836 118.789 133.532 1.00 10.64  ? 1081 PHE A CZ    1 
ATOM   8260  N  N     . SER A 1  1082 ? 121.151 116.441 140.150 1.00 17.49  ? 1082 SER A N     1 
ATOM   8261  C  CA    . SER A 1  1082 ? 121.916 115.849 141.236 1.00 17.53  ? 1082 SER A CA    1 
ATOM   8262  C  C     . SER A 1  1082 ? 121.179 114.712 141.922 1.00 21.36  ? 1082 SER A C     1 
ATOM   8263  O  O     . SER A 1  1082 ? 121.768 114.041 142.773 1.00 18.98  ? 1082 SER A O     1 
ATOM   8264  C  CB    . SER A 1  1082 ? 122.285 116.905 142.280 1.00 23.85  ? 1082 SER A CB    1 
ATOM   8265  O  OG    . SER A 1  1082 ? 123.047 117.950 141.717 1.00 25.36  ? 1082 SER A OG    1 
ATOM   8266  N  N     . ALA A 1  1083 ? 119.911 114.489 141.578 1.00 23.71  ? 1083 ALA A N     1 
ATOM   8267  C  CA    . ALA A 1  1083 ? 119.094 113.437 142.180 1.00 24.61  ? 1083 ALA A CA    1 
ATOM   8268  C  C     . ALA A 1  1083 ? 119.047 113.571 143.704 1.00 32.37  ? 1083 ALA A C     1 
ATOM   8269  O  O     . ALA A 1  1083 ? 119.411 112.660 144.448 1.00 35.82  ? 1083 ALA A O     1 
ATOM   8270  C  CB    . ALA A 1  1083 ? 119.593 112.056 141.762 1.00 23.78  ? 1083 ALA A CB    1 
ATOM   8271  N  N     . LYS A 1  1084 ? 118.594 114.731 144.166 1.00 32.52  ? 1084 LYS A N     1 
ATOM   8272  C  CA    . LYS A 1  1084 ? 118.545 114.998 145.598 1.00 30.97  ? 1084 LYS A CA    1 
ATOM   8273  C  C     . LYS A 1  1084 ? 117.327 114.330 146.236 1.00 35.36  ? 1084 LYS A C     1 
ATOM   8274  O  O     . LYS A 1  1084 ? 116.273 114.218 145.603 1.00 35.22  ? 1084 LYS A O     1 
ATOM   8275  C  CB    . LYS A 1  1084 ? 118.515 116.499 145.846 1.00 28.03  ? 1084 LYS A CB    1 
ATOM   8276  C  CG    . LYS A 1  1084 ? 119.838 117.146 145.569 1.00 30.81  ? 1084 LYS A CG    1 
ATOM   8277  C  CD    . LYS A 1  1084 ? 119.781 118.641 145.706 1.00 33.88  ? 1084 LYS A CD    1 
ATOM   8278  C  CE    . LYS A 1  1084 ? 121.111 119.246 145.316 1.00 30.39  ? 1084 LYS A CE    1 
ATOM   8279  N  NZ    . LYS A 1  1084 ? 121.087 120.729 145.365 1.00 30.79  ? 1084 LYS A NZ    1 
ATOM   8280  N  N     . PRO A 1  1085 ? 117.436 113.889 147.495 1.00 35.24  ? 1085 PRO A N     1 
ATOM   8281  C  CA    . PRO A 1  1085 ? 116.301 113.227 148.155 1.00 35.12  ? 1085 PRO A CA    1 
ATOM   8282  C  C     . PRO A 1  1085 ? 115.154 114.168 148.494 1.00 35.85  ? 1085 PRO A C     1 
ATOM   8283  O  O     . PRO A 1  1085 ? 115.263 115.388 148.332 1.00 33.27  ? 1085 PRO A O     1 
ATOM   8284  C  CB    . PRO A 1  1085 ? 116.931 112.640 149.420 1.00 32.68  ? 1085 PRO A CB    1 
ATOM   8285  C  CG    . PRO A 1  1085 ? 118.117 113.485 149.676 1.00 31.73  ? 1085 PRO A CG    1 
ATOM   8286  C  CD    . PRO A 1  1085 ? 118.641 113.888 148.337 1.00 32.05  ? 1085 PRO A CD    1 
ATOM   8287  N  N     . VAL A 1  1086 ? 114.053 113.595 148.986 1.00 36.64  ? 1086 VAL A N     1 
ATOM   8288  C  CA    . VAL A 1  1086 ? 112.795 114.329 149.106 1.00 34.47  ? 1086 VAL A CA    1 
ATOM   8289  C  C     . VAL A 1  1086 ? 112.903 115.435 150.147 1.00 38.51  ? 1086 VAL A C     1 
ATOM   8290  O  O     . VAL A 1  1086 ? 112.293 116.501 150.006 1.00 39.77  ? 1086 VAL A O     1 
ATOM   8291  C  CB    . VAL A 1  1086 ? 111.645 113.360 149.438 1.00 32.29  ? 1086 VAL A CB    1 
ATOM   8292  C  CG1   . VAL A 1  1086 ? 110.312 113.956 149.037 1.00 34.14  ? 1086 VAL A CG1   1 
ATOM   8293  C  CG2   . VAL A 1  1086 ? 111.871 112.018 148.770 1.00 35.44  ? 1086 VAL A CG2   1 
ATOM   8294  N  N     . GLU A 1  1087 ? 113.660 115.195 151.220 1.00 32.32  ? 1087 GLU A N     1 
ATOM   8295  C  CA    . GLU A 1  1087 ? 113.750 116.174 152.296 1.00 28.57  ? 1087 GLU A CA    1 
ATOM   8296  C  C     . GLU A 1  1087 ? 114.461 117.453 151.880 1.00 35.98  ? 1087 GLU A C     1 
ATOM   8297  O  O     . GLU A 1  1087 ? 114.280 118.484 152.535 1.00 39.35  ? 1087 GLU A O     1 
ATOM   8298  C  CB    . GLU A 1  1087 ? 114.460 115.567 153.500 1.00 32.65  ? 1087 GLU A CB    1 
ATOM   8299  C  CG    . GLU A 1  1087 ? 115.853 115.066 153.207 1.00 37.01  ? 1087 GLU A CG    1 
ATOM   8300  C  CD    . GLU A 1  1087 ? 115.887 113.572 152.980 1.00 39.67  ? 1087 GLU A CD    1 
ATOM   8301  O  OE1   . GLU A 1  1087 ? 114.805 112.972 152.822 1.00 36.15  ? 1087 GLU A OE1   1 
ATOM   8302  O  OE2   . GLU A 1  1087 ? 116.993 112.996 152.966 1.00 37.68  ? 1087 GLU A OE2   1 
ATOM   8303  N  N     . ALA A 1  1088 ? 115.258 117.419 150.817 1.00 37.83  ? 1088 ALA A N     1 
ATOM   8304  C  CA    . ALA A 1  1088 ? 115.982 118.595 150.357 1.00 32.77  ? 1088 ALA A CA    1 
ATOM   8305  C  C     . ALA A 1  1088 ? 115.242 119.366 149.276 1.00 32.44  ? 1088 ALA A C     1 
ATOM   8306  O  O     . ALA A 1  1088 ? 115.807 120.308 148.715 1.00 36.84  ? 1088 ALA A O     1 
ATOM   8307  C  CB    . ALA A 1  1088 ? 117.369 118.200 149.842 1.00 31.37  ? 1088 ALA A CB    1 
ATOM   8308  N  N     . GLU A 1  1089 ? 114.008 118.992 148.960 1.00 36.17  ? 1089 GLU A N     1 
ATOM   8309  C  CA    . GLU A 1  1089 ? 113.271 119.713 147.937 1.00 41.80  ? 1089 GLU A CA    1 
ATOM   8310  C  C     . GLU A 1  1089 ? 112.690 121.011 148.491 1.00 43.55  ? 1089 GLU A C     1 
ATOM   8311  O  O     . GLU A 1  1089 ? 112.191 121.073 149.616 1.00 45.58  ? 1089 GLU A O     1 
ATOM   8312  C  CB    . GLU A 1  1089 ? 112.154 118.848 147.357 1.00 41.48  ? 1089 GLU A CB    1 
ATOM   8313  C  CG    . GLU A 1  1089 ? 112.623 117.541 146.753 1.00 37.64  ? 1089 GLU A CG    1 
ATOM   8314  C  CD    . GLU A 1  1089 ? 111.496 116.779 146.101 1.00 39.34  ? 1089 GLU A CD    1 
ATOM   8315  O  OE1   . GLU A 1  1089 ? 110.370 117.313 146.052 1.00 39.29  ? 1089 GLU A OE1   1 
ATOM   8316  O  OE2   . GLU A 1  1089 ? 111.729 115.643 145.639 1.00 43.61  ? 1089 GLU A OE2   1 
ATOM   8317  N  N     . GLN A 1  1090 ? 112.745 122.055 147.666 1.00 41.34  ? 1090 GLN A N     1 
ATOM   8318  C  CA    . GLN A 1  1090 ? 112.330 123.387 148.074 1.00 41.72  ? 1090 GLN A CA    1 
ATOM   8319  C  C     . GLN A 1  1090 ? 111.002 123.824 147.490 1.00 41.04  ? 1090 GLN A C     1 
ATOM   8320  O  O     . GLN A 1  1090 ? 110.352 124.692 148.080 1.00 45.30  ? 1090 GLN A O     1 
ATOM   8321  C  CB    . GLN A 1  1090 ? 113.392 124.426 147.682 1.00 43.07  ? 1090 GLN A CB    1 
ATOM   8322  C  CG    . GLN A 1  1090 ? 114.786 124.022 148.066 1.00 44.17  ? 1090 GLN A CG    1 
ATOM   8323  C  CD    . GLN A 1  1090 ? 115.093 124.351 149.497 1.00 46.72  ? 1090 GLN A CD    1 
ATOM   8324  O  OE1   . GLN A 1  1090 ? 115.040 123.484 150.367 1.00 45.78  ? 1090 GLN A OE1   1 
ATOM   8325  N  NE2   . GLN A 1  1090 ? 115.434 125.607 149.755 1.00 46.03  ? 1090 GLN A NE2   1 
ATOM   8326  N  N     . SER A 1  1091 ? 110.586 123.268 146.357 1.00 29.98  ? 1091 SER A N     1 
ATOM   8327  C  CA    . SER A 1  1091 ? 109.318 123.617 145.733 1.00 31.32  ? 1091 SER A CA    1 
ATOM   8328  C  C     . SER A 1  1091 ? 108.529 122.364 145.399 1.00 30.73  ? 1091 SER A C     1 
ATOM   8329  O  O     . SER A 1  1091 ? 107.975 122.230 144.305 1.00 28.41  ? 1091 SER A O     1 
ATOM   8330  C  CB    . SER A 1  1091 ? 109.528 124.465 144.483 1.00 31.18  ? 1091 SER A CB    1 
ATOM   8331  O  OG    . SER A 1  1091 ? 108.289 124.742 143.852 1.00 33.23  ? 1091 SER A OG    1 
ATOM   8332  N  N     . SER A 1  1092 ? 108.462 121.432 146.340 1.00 30.70  ? 1092 SER A N     1 
ATOM   8333  C  CA    . SER A 1  1092 ? 107.705 120.209 146.129 1.00 26.74  ? 1092 SER A CA    1 
ATOM   8334  C  C     . SER A 1  1092 ? 106.214 120.507 146.048 1.00 27.04  ? 1092 SER A C     1 
ATOM   8335  O  O     . SER A 1  1092 ? 105.700 121.376 146.750 1.00 33.82  ? 1092 SER A O     1 
ATOM   8336  C  CB    . SER A 1  1092 ? 107.987 119.226 147.254 1.00 25.14  ? 1092 SER A CB    1 
ATOM   8337  O  OG    . SER A 1  1092 ? 107.200 118.073 147.102 1.00 27.86  ? 1092 SER A OG    1 
ATOM   8338  N  N     . GLU A 1  1093 ? 105.516 119.781 145.182 1.00 26.81  ? 1093 GLU A N     1 
ATOM   8339  C  CA    . GLU A 1  1093 ? 104.110 120.029 144.909 1.00 25.61  ? 1093 GLU A CA    1 
ATOM   8340  C  C     . GLU A 1  1093 ? 103.390 118.701 144.757 1.00 25.21  ? 1093 GLU A C     1 
ATOM   8341  O  O     . GLU A 1  1093 ? 103.994 117.632 144.834 1.00 27.96  ? 1093 GLU A O     1 
ATOM   8342  C  CB    . GLU A 1  1093 ? 103.920 120.871 143.645 1.00 21.91  ? 1093 GLU A CB    1 
ATOM   8343  C  CG    . GLU A 1  1093 ? 104.417 122.291 143.747 1.00 26.53  ? 1093 GLU A CG    1 
ATOM   8344  C  CD    . GLU A 1  1093 ? 103.585 123.246 142.920 1.00 36.31  ? 1093 GLU A CD    1 
ATOM   8345  O  OE1   . GLU A 1  1093 ? 102.355 123.044 142.843 1.00 35.05  ? 1093 GLU A OE1   1 
ATOM   8346  O  OE2   . GLU A 1  1093 ? 104.152 124.202 142.350 1.00 35.31  ? 1093 GLU A OE2   1 
ATOM   8347  N  N     . MET A 1  1094 ? 102.083 118.785 144.538 1.00 26.03  ? 1094 MET A N     1 
ATOM   8348  C  CA    . MET A 1  1094 ? 101.242 117.637 144.242 1.00 18.95  ? 1094 MET A CA    1 
ATOM   8349  C  C     . MET A 1  1094 ? 100.007 118.162 143.536 1.00 17.34  ? 1094 MET A C     1 
ATOM   8350  O  O     . MET A 1  1094 ? 99.722  119.356 143.573 1.00 24.97  ? 1094 MET A O     1 
ATOM   8351  C  CB    . MET A 1  1094 ? 100.877 116.869 145.506 1.00 20.68  ? 1094 MET A CB    1 
ATOM   8352  C  CG    . MET A 1  1094 ? 101.603 115.569 145.672 1.00 23.72  ? 1094 MET A CG    1 
ATOM   8353  S  SD    . MET A 1  1094 ? 101.433 114.865 147.315 1.00 33.11  ? 1094 MET A SD    1 
ATOM   8354  C  CE    . MET A 1  1094 ? 99.692  114.506 147.356 1.00 22.46  ? 1094 MET A CE    1 
ATOM   8355  N  N     . LEU A 1  1095 ? 99.299  117.269 142.857 1.00 13.87  ? 1095 LEU A N     1 
ATOM   8356  C  CA    . LEU A 1  1095 ? 98.104  117.645 142.101 1.00 17.34  ? 1095 LEU A CA    1 
ATOM   8357  C  C     . LEU A 1  1095 ? 97.111  116.500 142.244 1.00 22.79  ? 1095 LEU A C     1 
ATOM   8358  O  O     . LEU A 1  1095 ? 97.304  115.430 141.664 1.00 25.35  ? 1095 LEU A O     1 
ATOM   8359  C  CB    . LEU A 1  1095 ? 98.432  117.927 140.641 1.00 18.15  ? 1095 LEU A CB    1 
ATOM   8360  C  CG    . LEU A 1  1095 ? 97.402  118.608 139.739 1.00 21.37  ? 1095 LEU A CG    1 
ATOM   8361  C  CD1   . LEU A 1  1095 ? 96.524  117.600 139.032 1.00 21.46  ? 1095 LEU A CD1   1 
ATOM   8362  C  CD2   . LEU A 1  1095 ? 96.562  119.578 140.534 1.00 24.41  ? 1095 LEU A CD2   1 
ATOM   8363  N  N     . LEU A 1  1096 ? 96.049  116.736 143.009 1.00 21.77  ? 1096 LEU A N     1 
ATOM   8364  C  CA    . LEU A 1  1096 ? 95.109  115.690 143.388 1.00 20.99  ? 1096 LEU A CA    1 
ATOM   8365  C  C     . LEU A 1  1096 ? 93.792  115.875 142.648 1.00 20.14  ? 1096 LEU A C     1 
ATOM   8366  O  O     . LEU A 1  1096 ? 93.320  117.000 142.479 1.00 23.16  ? 1096 LEU A O     1 
ATOM   8367  C  CB    . LEU A 1  1096 ? 94.888  115.703 144.896 1.00 19.76  ? 1096 LEU A CB    1 
ATOM   8368  C  CG    . LEU A 1  1096 ? 96.174  115.462 145.677 1.00 23.33  ? 1096 LEU A CG    1 
ATOM   8369  C  CD1   . LEU A 1  1096 ? 96.140  116.135 147.024 1.00 21.10  ? 1096 LEU A CD1   1 
ATOM   8370  C  CD2   . LEU A 1  1096 ? 96.417  113.978 145.824 1.00 23.53  ? 1096 LEU A CD2   1 
ATOM   8371  N  N     . ARG A 1  1097 ? 93.216  114.773 142.188 1.00 18.34  ? 1097 ARG A N     1 
ATOM   8372  C  CA    . ARG A 1  1097 ? 91.925  114.824 141.530 1.00 23.78  ? 1097 ARG A CA    1 
ATOM   8373  C  C     . ARG A 1  1097 ? 90.833  114.388 142.497 1.00 26.18  ? 1097 ARG A C     1 
ATOM   8374  O  O     . ARG A 1  1097 ? 91.085  113.695 143.484 1.00 29.53  ? 1097 ARG A O     1 
ATOM   8375  C  CB    . ARG A 1  1097 ? 91.915  113.941 140.281 1.00 25.68  ? 1097 ARG A CB    1 
ATOM   8376  C  CG    . ARG A 1  1097 ? 92.892  114.372 139.210 1.00 23.59  ? 1097 ARG A CG    1 
ATOM   8377  C  CD    . ARG A 1  1097 ? 92.423  115.591 138.465 1.00 19.33  ? 1097 ARG A CD    1 
ATOM   8378  N  NE    . ARG A 1  1097 ? 91.151  115.355 137.800 1.00 26.26  ? 1097 ARG A NE    1 
ATOM   8379  C  CZ    . ARG A 1  1097 ? 91.018  114.857 136.580 1.00 23.36  ? 1097 ARG A CZ    1 
ATOM   8380  N  NH1   . ARG A 1  1097 ? 92.067  114.532 135.849 1.00 25.63  ? 1097 ARG A NH1   1 
ATOM   8381  N  NH2   . ARG A 1  1097 ? 89.800  114.681 136.081 1.00 22.86  ? 1097 ARG A NH2   1 
ATOM   8382  N  N     . LEU A 1  1098 ? 89.609  114.813 142.210 1.00 31.35  ? 1098 LEU A N     1 
ATOM   8383  C  CA    . LEU A 1  1098 ? 88.488  114.492 143.076 1.00 32.55  ? 1098 LEU A CA    1 
ATOM   8384  C  C     . LEU A 1  1098 ? 87.938  113.112 142.737 1.00 34.18  ? 1098 LEU A C     1 
ATOM   8385  O  O     . LEU A 1  1098 ? 88.025  112.641 141.603 1.00 35.89  ? 1098 LEU A O     1 
ATOM   8386  C  CB    . LEU A 1  1098 ? 87.393  115.549 142.949 1.00 33.25  ? 1098 LEU A CB    1 
ATOM   8387  C  CG    . LEU A 1  1098 ? 87.775  116.938 143.459 1.00 31.23  ? 1098 LEU A CG    1 
ATOM   8388  C  CD1   . LEU A 1  1098 ? 86.640  117.917 143.251 1.00 33.32  ? 1098 LEU A CD1   1 
ATOM   8389  C  CD2   . LEU A 1  1098 ? 88.184  116.878 144.914 1.00 28.74  ? 1098 LEU A CD2   1 
ATOM   8390  N  N     . LYS A 1  1099 ? 87.335  112.475 143.737 1.00 34.37  ? 1099 LYS A N     1 
ATOM   8391  C  CA    . LYS A 1  1099 ? 87.003  111.059 143.660 1.00 34.63  ? 1099 LYS A CA    1 
ATOM   8392  C  C     . LYS A 1  1099 ? 85.963  110.727 142.599 1.00 37.02  ? 1099 LYS A C     1 
ATOM   8393  O  O     . LYS A 1  1099 ? 85.791  109.546 142.281 1.00 39.95  ? 1099 LYS A O     1 
ATOM   8394  C  CB    . LYS A 1  1099 ? 86.527  110.572 145.025 1.00 38.52  ? 1099 LYS A CB    1 
ATOM   8395  C  CG    . LYS A 1  1099 ? 86.710  109.089 145.283 1.00 39.52  ? 1099 LYS A CG    1 
ATOM   8396  C  CD    . LYS A 1  1099 ? 87.903  108.512 144.548 1.00 39.40  ? 1099 LYS A CD    1 
ATOM   8397  C  CE    . LYS A 1  1099 ? 88.171  107.087 144.984 1.00 37.75  ? 1099 LYS A CE    1 
ATOM   8398  N  NZ    . LYS A 1  1099 ? 88.419  107.001 146.442 1.00 34.15  ? 1099 LYS A NZ    1 
ATOM   8399  N  N     . ASN A 1  1100 ? 85.275  111.718 142.041 1.00 39.07  ? 1100 ASN A N     1 
ATOM   8400  C  CA    . ASN A 1  1100 ? 84.164  111.420 141.158 1.00 38.34  ? 1100 ASN A CA    1 
ATOM   8401  C  C     . ASN A 1  1100 ? 84.128  112.469 140.051 1.00 39.53  ? 1100 ASN A C     1 
ATOM   8402  O  O     . ASN A 1  1100 ? 84.313  113.663 140.353 1.00 42.30  ? 1100 ASN A O     1 
ATOM   8403  C  CB    . ASN A 1  1100 ? 82.856  111.437 141.963 1.00 39.69  ? 1100 ASN A CB    1 
ATOM   8404  C  CG    . ASN A 1  1100 ? 81.830  110.453 141.457 1.00 42.05  ? 1100 ASN A CG    1 
ATOM   8405  O  OD1   . ASN A 1  1100 ? 81.751  110.152 140.271 1.00 42.41  ? 1100 ASN A OD1   1 
ATOM   8406  N  ND2   . ASN A 1  1100 ? 81.051  109.900 142.376 1.00 40.93  ? 1100 ASN A ND2   1 
ATOM   8407  N  N     . PRO A 1  1101 ? 83.941  112.086 138.786 1.00 43.87  ? 1101 PRO A N     1 
ATOM   8408  C  CA    . PRO A 1  1101 ? 83.767  113.099 137.733 1.00 43.33  ? 1101 PRO A CA    1 
ATOM   8409  C  C     . PRO A 1  1101 ? 82.420  113.790 137.746 1.00 45.07  ? 1101 PRO A C     1 
ATOM   8410  O  O     . PRO A 1  1101 ? 82.118  114.535 136.808 1.00 45.60  ? 1101 PRO A O     1 
ATOM   8411  C  CB    . PRO A 1  1101 ? 83.979  112.232 136.482 1.00 43.11  ? 1101 PRO A CB    1 
ATOM   8412  C  CG    . PRO A 1  1101 ? 84.665  111.045 137.225 1.00 47.47  ? 1101 PRO A CG    1 
ATOM   8413  C  CD    . PRO A 1  1101 ? 83.684  110.803 138.104 1.00 48.38  ? 1101 PRO A CD    1 
ATOM   8414  N  N     . GLU A 1  1102 ? 81.600  113.547 138.764 1.00 45.90  ? 1102 GLU A N     1 
ATOM   8415  C  CA    . GLU A 1  1102 ? 80.339  114.265 138.915 1.00 44.23  ? 1102 GLU A CA    1 
ATOM   8416  C  C     . GLU A 1  1102 ? 80.410  115.300 140.035 1.00 42.45  ? 1102 GLU A C     1 
ATOM   8417  O  O     . GLU A 1  1102 ? 79.519  116.145 140.159 1.00 43.37  ? 1102 GLU A O     1 
ATOM   8418  C  CB    . GLU A 1  1102 ? 79.197  113.275 139.150 1.00 43.49  ? 1102 GLU A CB    1 
ATOM   8419  C  CG    . GLU A 1  1102 ? 78.646  112.684 137.865 1.00 45.91  ? 1102 GLU A CG    1 
ATOM   8420  C  CD    . GLU A 1  1102 ? 79.080  111.248 137.629 1.00 47.04  ? 1102 GLU A CD    1 
ATOM   8421  O  OE1   . GLU A 1  1102 ? 79.622  110.619 138.560 1.00 46.44  ? 1102 GLU A OE1   1 
ATOM   8422  O  OE2   . GLU A 1  1102 ? 78.875  110.735 136.511 1.00 45.72  ? 1102 GLU A OE2   1 
ATOM   8423  N  N     . VAL A 1  1103 ? 81.450  115.239 140.871 1.00 38.61  ? 1103 VAL A N     1 
ATOM   8424  C  CA    . VAL A 1  1103 ? 81.641  116.240 141.913 1.00 38.71  ? 1103 VAL A CA    1 
ATOM   8425  C  C     . VAL A 1  1103 ? 82.763  117.217 141.597 1.00 42.37  ? 1103 VAL A C     1 
ATOM   8426  O  O     . VAL A 1  1103 ? 83.012  118.131 142.393 1.00 43.56  ? 1103 VAL A O     1 
ATOM   8427  C  CB    . VAL A 1  1103 ? 81.909  115.562 143.270 1.00 37.39  ? 1103 VAL A CB    1 
ATOM   8428  C  CG1   . VAL A 1  1103 ? 80.933  114.427 143.490 1.00 39.47  ? 1103 VAL A CG1   1 
ATOM   8429  C  CG2   . VAL A 1  1103 ? 83.334  115.054 143.326 1.00 37.66  ? 1103 VAL A CG2   1 
ATOM   8430  N  N     . GLU A 1  1104 ? 83.462  117.048 140.470 1.00 44.54  ? 1104 GLU A N     1 
ATOM   8431  C  CA    . GLU A 1  1104 ? 84.532  117.978 140.119 1.00 43.67  ? 1104 GLU A CA    1 
ATOM   8432  C  C     . GLU A 1  1104 ? 84.004  119.351 139.738 1.00 41.58  ? 1104 GLU A C     1 
ATOM   8433  O  O     . GLU A 1  1104 ? 84.734  120.339 139.858 1.00 37.97  ? 1104 GLU A O     1 
ATOM   8434  C  CB    . GLU A 1  1104 ? 85.368  117.441 138.957 1.00 40.58  ? 1104 GLU A CB    1 
ATOM   8435  C  CG    . GLU A 1  1104 ? 86.213  116.228 139.264 1.00 42.22  ? 1104 GLU A CG    1 
ATOM   8436  C  CD    . GLU A 1  1104 ? 86.407  115.337 138.052 1.00 45.09  ? 1104 GLU A CD    1 
ATOM   8437  O  OE1   . GLU A 1  1104 ? 85.822  115.637 136.990 1.00 43.94  ? 1104 GLU A OE1   1 
ATOM   8438  O  OE2   . GLU A 1  1104 ? 87.156  114.341 138.157 1.00 45.43  ? 1104 GLU A OE2   1 
ATOM   8439  N  N     . THR A 1  1105 ? 82.754  119.430 139.291 1.00 41.44  ? 1105 THR A N     1 
ATOM   8440  C  CA    . THR A 1  1105 ? 82.247  120.659 138.695 1.00 41.42  ? 1105 THR A CA    1 
ATOM   8441  C  C     . THR A 1  1105 ? 81.881  121.703 139.742 1.00 39.30  ? 1105 THR A C     1 
ATOM   8442  O  O     . THR A 1  1105 ? 81.661  122.866 139.394 1.00 36.47  ? 1105 THR A O     1 
ATOM   8443  C  CB    . THR A 1  1105 ? 81.045  120.335 137.812 1.00 39.78  ? 1105 THR A CB    1 
ATOM   8444  O  OG1   . THR A 1  1105 ? 80.298  119.265 138.403 1.00 40.40  ? 1105 THR A OG1   1 
ATOM   8445  C  CG2   . THR A 1  1105 ? 81.506  119.905 136.430 1.00 37.37  ? 1105 THR A CG2   1 
ATOM   8446  N  N     . ASN A 1  1106 ? 81.817  121.320 141.016 1.00 40.99  ? 1106 ASN A N     1 
ATOM   8447  C  CA    . ASN A 1  1106 ? 81.396  122.234 142.074 1.00 41.14  ? 1106 ASN A CA    1 
ATOM   8448  C  C     . ASN A 1  1106 ? 82.619  122.797 142.787 1.00 39.11  ? 1106 ASN A C     1 
ATOM   8449  O  O     . ASN A 1  1106 ? 83.397  122.050 143.385 1.00 37.43  ? 1106 ASN A O     1 
ATOM   8450  C  CB    . ASN A 1  1106 ? 80.467  121.515 143.049 1.00 40.34  ? 1106 ASN A CB    1 
ATOM   8451  C  CG    . ASN A 1  1106 ? 80.124  122.355 144.258 1.00 42.11  ? 1106 ASN A CG    1 
ATOM   8452  O  OD1   . ASN A 1  1106 ? 80.061  123.581 144.182 1.00 41.87  ? 1106 ASN A OD1   1 
ATOM   8453  N  ND2   . ASN A 1  1106 ? 79.873  121.697 145.378 1.00 41.77  ? 1106 ASN A ND2   1 
ATOM   8454  N  N     . LYS A 1  1107 ? 82.784  124.121 142.738 1.00 35.86  ? 1107 LYS A N     1 
ATOM   8455  C  CA    . LYS A 1  1107 ? 83.954  124.738 143.352 1.00 36.63  ? 1107 LYS A CA    1 
ATOM   8456  C  C     . LYS A 1  1107 ? 83.868  124.719 144.873 1.00 40.86  ? 1107 LYS A C     1 
ATOM   8457  O  O     . LYS A 1  1107 ? 84.890  124.581 145.554 1.00 40.97  ? 1107 LYS A O     1 
ATOM   8458  C  CB    . LYS A 1  1107 ? 84.127  126.169 142.853 1.00 35.39  ? 1107 LYS A CB    1 
ATOM   8459  C  CG    . LYS A 1  1107 ? 85.441  126.795 143.293 1.00 37.39  ? 1107 LYS A CG    1 
ATOM   8460  C  CD    . LYS A 1  1107 ? 85.608  128.203 142.763 1.00 38.52  ? 1107 LYS A CD    1 
ATOM   8461  C  CE    . LYS A 1  1107 ? 87.014  128.720 143.007 1.00 40.70  ? 1107 LYS A CE    1 
ATOM   8462  N  NZ    . LYS A 1  1107 ? 87.393  128.717 144.452 1.00 40.22  ? 1107 LYS A NZ    1 
ATOM   8463  N  N     . THR A 1  1108 ? 82.665  124.882 145.426 1.00 38.77  ? 1108 THR A N     1 
ATOM   8464  C  CA    . THR A 1  1108 ? 82.526  124.897 146.878 1.00 40.16  ? 1108 THR A CA    1 
ATOM   8465  C  C     . THR A 1  1108 ? 82.932  123.561 147.480 1.00 40.85  ? 1108 THR A C     1 
ATOM   8466  O  O     . THR A 1  1108 ? 83.571  123.515 148.536 1.00 40.58  ? 1108 THR A O     1 
ATOM   8467  C  CB    . THR A 1  1108 ? 81.092  125.253 147.272 1.00 39.82  ? 1108 THR A CB    1 
ATOM   8468  O  OG1   . THR A 1  1108 ? 80.183  124.313 146.685 1.00 41.20  ? 1108 THR A OG1   1 
ATOM   8469  C  CG2   . THR A 1  1108 ? 80.744  126.649 146.798 1.00 39.69  ? 1108 THR A CG2   1 
ATOM   8470  N  N     . TYR A 1  1109 ? 82.573  122.462 146.817 1.00 38.94  ? 1109 TYR A N     1 
ATOM   8471  C  CA    . TYR A 1  1109 ? 82.974  121.147 147.298 1.00 40.91  ? 1109 TYR A CA    1 
ATOM   8472  C  C     . TYR A 1  1109 ? 84.490  121.008 147.314 1.00 41.75  ? 1109 TYR A C     1 
ATOM   8473  O  O     . TYR A 1  1109 ? 85.063  120.480 148.274 1.00 42.40  ? 1109 TYR A O     1 
ATOM   8474  C  CB    . TYR A 1  1109 ? 82.340  120.068 146.426 1.00 38.98  ? 1109 TYR A CB    1 
ATOM   8475  C  CG    . TYR A 1  1109 ? 82.588  118.665 146.904 1.00 40.73  ? 1109 TYR A CG    1 
ATOM   8476  C  CD1   . TYR A 1  1109 ? 82.409  118.329 148.235 1.00 40.24  ? 1109 TYR A CD1   1 
ATOM   8477  C  CD2   . TYR A 1  1109 ? 82.979  117.670 146.021 1.00 41.32  ? 1109 TYR A CD2   1 
ATOM   8478  C  CE1   . TYR A 1  1109 ? 82.626  117.045 148.676 1.00 42.13  ? 1109 TYR A CE1   1 
ATOM   8479  C  CE2   . TYR A 1  1109 ? 83.198  116.382 146.453 1.00 43.23  ? 1109 TYR A CE2   1 
ATOM   8480  C  CZ    . TYR A 1  1109 ? 83.017  116.072 147.780 1.00 44.91  ? 1109 TYR A CZ    1 
ATOM   8481  O  OH    . TYR A 1  1109 ? 83.239  114.789 148.214 1.00 43.98  ? 1109 TYR A OH    1 
ATOM   8482  N  N     . ALA A 1  1110 ? 85.158  121.489 146.264 1.00 37.86  ? 1110 ALA A N     1 
ATOM   8483  C  CA    . ALA A 1  1110 ? 86.611  121.394 146.199 1.00 37.46  ? 1110 ALA A CA    1 
ATOM   8484  C  C     . ALA A 1  1110 ? 87.269  122.211 147.299 1.00 38.12  ? 1110 ALA A C     1 
ATOM   8485  O  O     . ALA A 1  1110 ? 88.282  121.795 147.871 1.00 36.38  ? 1110 ALA A O     1 
ATOM   8486  C  CB    . ALA A 1  1110 ? 87.105  121.853 144.830 1.00 38.46  ? 1110 ALA A CB    1 
ATOM   8487  N  N     . GLN A 1  1111 ? 86.716  123.385 147.600 1.00 41.61  ? 1111 GLN A N     1 
ATOM   8488  C  CA    . GLN A 1  1111 ? 87.255  124.185 148.692 1.00 39.12  ? 1111 GLN A CA    1 
ATOM   8489  C  C     . GLN A 1  1111 ? 87.085  123.493 150.034 1.00 39.93  ? 1111 GLN A C     1 
ATOM   8490  O  O     . GLN A 1  1111 ? 87.916  123.673 150.928 1.00 39.70  ? 1111 GLN A O     1 
ATOM   8491  C  CB    . GLN A 1  1111 ? 86.593  125.556 148.723 1.00 36.62  ? 1111 GLN A CB    1 
ATOM   8492  C  CG    . GLN A 1  1111 ? 87.484  126.672 148.241 1.00 36.83  ? 1111 GLN A CG    1 
ATOM   8493  C  CD    . GLN A 1  1111 ? 88.765  126.776 149.039 1.00 40.46  ? 1111 GLN A CD    1 
ATOM   8494  O  OE1   . GLN A 1  1111 ? 88.824  126.384 150.204 1.00 38.04  ? 1111 GLN A OE1   1 
ATOM   8495  N  NE2   . GLN A 1  1111 ? 89.803  127.310 148.412 1.00 38.67  ? 1111 GLN A NE2   1 
ATOM   8496  N  N     . GLU A 1  1112 ? 86.016  122.714 150.201 1.00 40.67  ? 1112 GLU A N     1 
ATOM   8497  C  CA    . GLU A 1  1112 ? 85.839  121.973 151.443 1.00 41.60  ? 1112 GLU A CA    1 
ATOM   8498  C  C     . GLU A 1  1112 ? 86.959  120.962 151.636 1.00 44.77  ? 1112 GLU A C     1 
ATOM   8499  O  O     . GLU A 1  1112 ? 87.624  120.944 152.678 1.00 40.68  ? 1112 GLU A O     1 
ATOM   8500  C  CB    . GLU A 1  1112 ? 84.483  121.267 151.449 1.00 40.09  ? 1112 GLU A CB    1 
ATOM   8501  C  CG    . GLU A 1  1112 ? 83.278  122.192 151.421 1.00 44.30  ? 1112 GLU A CG    1 
ATOM   8502  C  CD    . GLU A 1  1112 ? 81.963  121.430 151.371 1.00 47.97  ? 1112 GLU A CD    1 
ATOM   8503  O  OE1   . GLU A 1  1112 ? 81.998  120.184 151.392 1.00 46.66  ? 1112 GLU A OE1   1 
ATOM   8504  O  OE2   . GLU A 1  1112 ? 80.896  122.076 151.308 1.00 44.88  ? 1112 GLU A OE2   1 
ATOM   8505  N  N     . ILE A 1  1113 ? 87.197  120.123 150.627 1.00 41.05  ? 1113 ILE A N     1 
ATOM   8506  C  CA    . ILE A 1  1113 ? 88.197  119.069 150.757 1.00 36.09  ? 1113 ILE A CA    1 
ATOM   8507  C  C     . ILE A 1  1113 ? 89.596  119.661 150.819 1.00 37.22  ? 1113 ILE A C     1 
ATOM   8508  O  O     . ILE A 1  1113 ? 90.461  119.165 151.548 1.00 38.85  ? 1113 ILE A O     1 
ATOM   8509  C  CB    . ILE A 1  1113 ? 88.050  118.052 149.617 1.00 35.42  ? 1113 ILE A CB    1 
ATOM   8510  C  CG1   . ILE A 1  1113 ? 86.709  117.341 149.734 1.00 37.19  ? 1113 ILE A CG1   1 
ATOM   8511  C  CG2   . ILE A 1  1113 ? 89.169  117.036 149.663 1.00 37.51  ? 1113 ILE A CG2   1 
ATOM   8512  C  CD1   . ILE A 1  1113 ? 86.129  116.972 148.414 1.00 37.10  ? 1113 ILE A CD1   1 
ATOM   8513  N  N     . ALA A 1  1114 ? 89.836  120.742 150.077 1.00 34.35  ? 1114 ALA A N     1 
ATOM   8514  C  CA    . ALA A 1  1114 ? 91.117  121.431 150.165 1.00 32.16  ? 1114 ALA A CA    1 
ATOM   8515  C  C     . ALA A 1  1114 ? 91.445  121.847 151.593 1.00 35.12  ? 1114 ALA A C     1 
ATOM   8516  O  O     . ALA A 1  1114 ? 92.624  121.932 151.949 1.00 34.84  ? 1114 ALA A O     1 
ATOM   8517  C  CB    . ALA A 1  1114 ? 91.115  122.653 149.251 1.00 31.03  ? 1114 ALA A CB    1 
ATOM   8518  N  N     . ASN A 1  1115 ? 90.430  122.112 152.415 1.00 38.36  ? 1115 ASN A N     1 
ATOM   8519  C  CA    . ASN A 1  1115 ? 90.659  122.435 153.817 1.00 39.66  ? 1115 ASN A CA    1 
ATOM   8520  C  C     . ASN A 1  1115 ? 90.830  121.183 154.664 1.00 39.03  ? 1115 ASN A C     1 
ATOM   8521  O  O     . ASN A 1  1115 ? 91.488  121.229 155.708 1.00 36.76  ? 1115 ASN A O     1 
ATOM   8522  C  CB    . ASN A 1  1115 ? 89.499  123.268 154.352 1.00 38.87  ? 1115 ASN A CB    1 
ATOM   8523  C  CG    . ASN A 1  1115 ? 89.203  124.472 153.489 1.00 38.18  ? 1115 ASN A CG    1 
ATOM   8524  O  OD1   . ASN A 1  1115 ? 90.072  124.970 152.776 1.00 36.77  ? 1115 ASN A OD1   1 
ATOM   8525  N  ND2   . ASN A 1  1115 ? 87.967  124.948 153.548 1.00 37.18  ? 1115 ASN A ND2   1 
ATOM   8526  N  N     . SER A 1  1116 ? 90.261  120.064 154.218 1.00 38.10  ? 1116 SER A N     1 
ATOM   8527  C  CA    . SER A 1  1116 ? 90.260  118.844 155.015 1.00 38.12  ? 1116 SER A CA    1 
ATOM   8528  C  C     . SER A 1  1116 ? 91.650  118.237 155.125 1.00 38.24  ? 1116 SER A C     1 
ATOM   8529  O  O     . SER A 1  1116 ? 91.996  117.652 156.158 1.00 39.84  ? 1116 SER A O     1 
ATOM   8530  C  CB    . SER A 1  1116 ? 89.293  117.833 154.406 1.00 36.55  ? 1116 SER A CB    1 
ATOM   8531  O  OG    . SER A 1  1116 ? 89.718  116.515 154.681 1.00 39.27  ? 1116 SER A OG    1 
ATOM   8532  N  N     . ILE A 1  1117 ? 92.453  118.342 154.063 1.00 39.52  ? 1117 ILE A N     1 
ATOM   8533  C  CA    . ILE A 1  1117 ? 93.708  117.601 153.999 1.00 38.26  ? 1117 ILE A CA    1 
ATOM   8534  C  C     . ILE A 1  1117 ? 94.915  118.416 154.439 1.00 36.06  ? 1117 ILE A C     1 
ATOM   8535  O  O     . ILE A 1  1117 ? 95.994  117.846 154.618 1.00 37.42  ? 1117 ILE A O     1 
ATOM   8536  C  CB    . ILE A 1  1117 ? 93.928  117.057 152.579 1.00 37.28  ? 1117 ILE A CB    1 
ATOM   8537  C  CG1   . ILE A 1  1117 ? 94.353  118.179 151.633 1.00 33.21  ? 1117 ILE A CG1   1 
ATOM   8538  C  CG2   . ILE A 1  1117 ? 92.672  116.372 152.070 1.00 36.25  ? 1117 ILE A CG2   1 
ATOM   8539  C  CD1   . ILE A 1  1117 ? 94.262  117.802 150.196 1.00 33.54  ? 1117 ILE A CD1   1 
ATOM   8540  N  N     . GLU A 1  1118 ? 94.778  119.726 154.609 1.00 37.91  ? 1118 GLU A N     1 
ATOM   8541  C  CA    . GLU A 1  1118 ? 95.931  120.532 154.983 1.00 39.21  ? 1118 GLU A CA    1 
ATOM   8542  C  C     . GLU A 1  1118 ? 96.341  120.254 156.427 1.00 39.08  ? 1118 GLU A C     1 
ATOM   8543  O  O     . GLU A 1  1118 ? 95.511  120.210 157.337 1.00 41.32  ? 1118 GLU A O     1 
ATOM   8544  C  CB    . GLU A 1  1118 ? 95.628  122.014 154.788 1.00 38.60  ? 1118 GLU A CB    1 
ATOM   8545  C  CG    . GLU A 1  1118 ? 96.799  122.918 155.089 1.00 38.91  ? 1118 GLU A CG    1 
ATOM   8546  C  CD    . GLU A 1  1118 ? 96.379  124.308 155.517 1.00 42.79  ? 1118 GLU A CD    1 
ATOM   8547  O  OE1   . GLU A 1  1118 ? 96.741  124.719 156.638 1.00 41.45  ? 1118 GLU A OE1   1 
ATOM   8548  O  OE2   . GLU A 1  1118 ? 95.689  124.994 154.732 1.00 42.13  ? 1118 GLU A OE2   1 
ATOM   8549  N  N     . LEU A 1  1119 ? 97.643  120.077 156.630 1.00 30.22  ? 1119 LEU A N     1 
ATOM   8550  C  CA    . LEU A 1  1119 ? 98.193  119.685 157.927 1.00 31.70  ? 1119 LEU A CA    1 
ATOM   8551  C  C     . LEU A 1  1119 ? 97.993  120.819 158.919 1.00 34.25  ? 1119 LEU A C     1 
ATOM   8552  O  O     . LEU A 1  1119 ? 98.610  121.879 158.805 1.00 35.55  ? 1119 LEU A O     1 
ATOM   8553  C  CB    . LEU A 1  1119 ? 99.668  119.323 157.791 1.00 33.43  ? 1119 LEU A CB    1 
ATOM   8554  C  CG    . LEU A 1  1119 ? 100.512 118.799 158.958 1.00 34.90  ? 1119 LEU A CG    1 
ATOM   8555  C  CD1   . LEU A 1  1119 ? 100.986 119.906 159.871 1.00 34.84  ? 1119 LEU A CD1   1 
ATOM   8556  C  CD2   . LEU A 1  1119 ? 99.749  117.762 159.743 1.00 30.71  ? 1119 LEU A CD2   1 
ATOM   8557  N  N     . ILE A 1  1120 ? 97.124  120.591 159.897 1.00 39.11  ? 1120 ILE A N     1 
ATOM   8558  C  CA    . ILE A 1  1120 ? 96.983  121.470 161.055 1.00 36.26  ? 1120 ILE A CA    1 
ATOM   8559  C  C     . ILE A 1  1120 ? 97.654  120.743 162.215 1.00 38.18  ? 1120 ILE A C     1 
ATOM   8560  O  O     . ILE A 1  1120 ? 97.137  119.765 162.756 1.00 36.71  ? 1120 ILE A O     1 
ATOM   8561  C  CB    . ILE A 1  1120 ? 95.523  121.805 161.351 1.00 34.34  ? 1120 ILE A CB    1 
ATOM   8562  C  CG1   . ILE A 1  1120 ? 94.974  122.786 160.320 1.00 34.55  ? 1120 ILE A CG1   1 
ATOM   8563  C  CG2   . ILE A 1  1120 ? 95.394  122.390 162.737 1.00 35.35  ? 1120 ILE A CG2   1 
ATOM   8564  C  CD1   . ILE A 1  1120 ? 95.947  123.875 159.938 1.00 37.05  ? 1120 ILE A CD1   1 
ATOM   8565  N  N     . THR A 1  1121 ? 98.832  121.221 162.591 1.00 38.98  ? 1121 THR A N     1 
ATOM   8566  C  CA    . THR A 1  1121 ? 99.571  120.658 163.710 1.00 39.89  ? 1121 THR A CA    1 
ATOM   8567  C  C     . THR A 1  1121 ? 99.027  121.232 165.015 1.00 41.14  ? 1121 THR A C     1 
ATOM   8568  O  O     . THR A 1  1121 ? 98.150  122.100 165.025 1.00 42.53  ? 1121 THR A O     1 
ATOM   8569  C  CB    . THR A 1  1121 ? 101.061 120.925 163.536 1.00 40.93  ? 1121 THR A CB    1 
ATOM   8570  O  OG1   . THR A 1  1121 ? 101.794 120.268 164.574 1.00 40.52  ? 1121 THR A OG1   1 
ATOM   8571  C  CG2   . THR A 1  1121 ? 101.345 122.413 163.567 1.00 37.97  ? 1121 THR A CG2   1 
ATOM   8572  N  N     . PHE A 1  1122 ? 99.542  120.750 166.144 1.00 47.12  ? 1122 PHE A N     1 
ATOM   8573  C  CA    . PHE A 1  1122 ? 99.078  121.244 167.434 1.00 48.28  ? 1122 PHE A CA    1 
ATOM   8574  C  C     . PHE A 1  1122 ? 99.664  122.597 167.812 1.00 49.12  ? 1122 PHE A C     1 
ATOM   8575  O  O     . PHE A 1  1122 ? 99.029  123.334 168.573 1.00 46.32  ? 1122 PHE A O     1 
ATOM   8576  C  CB    . PHE A 1  1122 ? 99.391  120.235 168.537 1.00 46.60  ? 1122 PHE A CB    1 
ATOM   8577  C  CG    . PHE A 1  1122 ? 98.616  120.474 169.792 1.00 48.42  ? 1122 PHE A CG    1 
ATOM   8578  C  CD1   . PHE A 1  1122 ? 97.300  120.888 169.731 1.00 47.36  ? 1122 PHE A CD1   1 
ATOM   8579  C  CD2   . PHE A 1  1122 ? 99.201  120.295 171.033 1.00 49.37  ? 1122 PHE A CD2   1 
ATOM   8580  C  CE1   . PHE A 1  1122 ? 96.580  121.120 170.885 1.00 47.82  ? 1122 PHE A CE1   1 
ATOM   8581  C  CE2   . PHE A 1  1122 ? 98.488  120.525 172.191 1.00 49.79  ? 1122 PHE A CE2   1 
ATOM   8582  C  CZ    . PHE A 1  1122 ? 97.176  120.937 172.118 1.00 47.76  ? 1122 PHE A CZ    1 
ATOM   8583  N  N     . GLU A 1  1123 ? 100.844 122.946 167.296 1.00 48.34  ? 1123 GLU A N     1 
ATOM   8584  C  CA    . GLU A 1  1123 ? 101.481 124.198 167.689 1.00 44.87  ? 1123 GLU A CA    1 
ATOM   8585  C  C     . GLU A 1  1123 ? 100.631 125.400 167.299 1.00 45.47  ? 1123 GLU A C     1 
ATOM   8586  O  O     . GLU A 1  1123 ? 100.501 126.357 168.067 1.00 45.87  ? 1123 GLU A O     1 
ATOM   8587  C  CB    . GLU A 1  1123 ? 102.869 124.309 167.059 1.00 46.46  ? 1123 GLU A CB    1 
ATOM   8588  C  CG    . GLU A 1  1123 ? 103.917 123.364 167.627 1.00 48.94  ? 1123 GLU A CG    1 
ATOM   8589  C  CD    . GLU A 1  1123 ? 104.097 122.105 166.797 1.00 49.63  ? 1123 GLU A CD    1 
ATOM   8590  O  OE1   . GLU A 1  1123 ? 103.417 121.965 165.763 1.00 47.31  ? 1123 GLU A OE1   1 
ATOM   8591  O  OE2   . GLU A 1  1123 ? 104.944 121.265 167.161 1.00 48.33  ? 1123 GLU A OE2   1 
ATOM   8592  N  N     . ARG A 1  1124 ? 100.044 125.372 166.104 1.00 45.25  ? 1124 ARG A N     1 
ATOM   8593  C  CA    . ARG A 1  1124 ? 99.401  126.575 165.593 1.00 47.41  ? 1124 ARG A CA    1 
ATOM   8594  C  C     . ARG A 1  1124 ? 98.018  126.806 166.186 1.00 46.86  ? 1124 ARG A C     1 
ATOM   8595  O  O     . ARG A 1  1124 ? 97.465  127.898 166.019 1.00 46.80  ? 1124 ARG A O     1 
ATOM   8596  C  CB    . ARG A 1  1124 ? 99.318  126.516 164.069 1.00 44.03  ? 1124 ARG A CB    1 
ATOM   8597  C  CG    . ARG A 1  1124 ? 98.352  125.491 163.541 1.00 44.25  ? 1124 ARG A CG    1 
ATOM   8598  C  CD    . ARG A 1  1124 ? 98.542  125.332 162.056 1.00 47.78  ? 1124 ARG A CD    1 
ATOM   8599  N  NE    . ARG A 1  1124 ? 98.360  126.590 161.345 1.00 47.84  ? 1124 ARG A NE    1 
ATOM   8600  C  CZ    . ARG A 1  1124 ? 98.624  126.760 160.058 1.00 47.36  ? 1124 ARG A CZ    1 
ATOM   8601  N  NH1   . ARG A 1  1124 ? 99.073  125.766 159.310 1.00 44.18  ? 1124 ARG A NH1   1 
ATOM   8602  N  NH2   . ARG A 1  1124 ? 98.428  127.954 159.507 1.00 47.48  ? 1124 ARG A NH2   1 
ATOM   8603  N  N     . LEU A 1  1125 ? 97.434  125.815 166.858 1.00 47.35  ? 1125 LEU A N     1 
ATOM   8604  C  CA    . LEU A 1  1125 ? 96.164  126.063 167.529 1.00 51.36  ? 1125 LEU A CA    1 
ATOM   8605  C  C     . LEU A 1  1125 ? 96.339  126.879 168.803 1.00 52.73  ? 1125 LEU A C     1 
ATOM   8606  O  O     . LEU A 1  1125 ? 95.546  127.790 169.064 1.00 51.99  ? 1125 LEU A O     1 
ATOM   8607  C  CB    . LEU A 1  1125 ? 95.456  124.748 167.850 1.00 50.03  ? 1125 LEU A CB    1 
ATOM   8608  C  CG    . LEU A 1  1125 ? 94.884  124.001 166.649 1.00 49.35  ? 1125 LEU A CG    1 
ATOM   8609  C  CD1   . LEU A 1  1125 ? 94.312  122.664 167.079 1.00 47.29  ? 1125 LEU A CD1   1 
ATOM   8610  C  CD2   . LEU A 1  1125 ? 93.832  124.845 165.953 1.00 47.38  ? 1125 LEU A CD2   1 
ATOM   8611  N  N     . ILE A 1  1126 ? 97.368  126.584 169.590 1.00 48.31  ? 1126 ILE A N     1 
ATOM   8612  C  CA    . ILE A 1  1126 ? 97.582  127.267 170.859 1.00 47.99  ? 1126 ILE A CA    1 
ATOM   8613  C  C     . ILE A 1  1126 ? 98.214  128.626 170.587 1.00 50.73  ? 1126 ILE A C     1 
ATOM   8614  O  O     . ILE A 1  1126 ? 99.059  128.764 169.697 1.00 48.75  ? 1126 ILE A O     1 
ATOM   8615  C  CB    . ILE A 1  1126 ? 98.452  126.424 171.801 1.00 47.32  ? 1126 ILE A CB    1 
ATOM   8616  C  CG1   . ILE A 1  1126 ? 99.824  126.160 171.188 1.00 46.78  ? 1126 ILE A CG1   1 
ATOM   8617  C  CG2   . ILE A 1  1126 ? 97.768  125.105 172.099 1.00 46.76  ? 1126 ILE A CG2   1 
ATOM   8618  C  CD1   . ILE A 1  1126 ? 100.935 126.953 171.813 1.00 46.07  ? 1126 ILE A CD1   1 
ATOM   8619  N  N     . LEU A 1  1127 ? 97.782  129.639 171.333 1.00 53.99  ? 1127 LEU A N     1 
ATOM   8620  C  CA    . LEU A 1  1127 ? 98.377  130.965 171.236 1.00 52.37  ? 1127 LEU A CA    1 
ATOM   8621  C  C     . LEU A 1  1127 ? 99.559  131.106 172.191 1.00 52.40  ? 1127 LEU A C     1 
ATOM   8622  O  O     . LEU A 1  1127 ? 100.576 131.713 171.845 1.00 52.64  ? 1127 LEU A O     1 
ATOM   8623  C  CB    . LEU A 1  1127 ? 97.314  132.035 171.518 1.00 51.75  ? 1127 LEU A CB    1 
ATOM   8624  C  CG    . LEU A 1  1127 ? 97.522  133.418 170.892 1.00 52.92  ? 1127 LEU A CG    1 
ATOM   8625  C  CD1   . LEU A 1  1127 ? 96.186  134.123 170.686 1.00 50.48  ? 1127 LEU A CD1   1 
ATOM   8626  C  CD2   . LEU A 1  1127 ? 98.457  134.277 171.733 1.00 50.99  ? 1127 LEU A CD2   1 
ATOM   8627  N  N     . GLN A 1  1128 ? 99.430  130.552 173.392 1.00 54.40  ? 1128 GLN A N     1 
ATOM   8628  C  CA    . GLN A 1  1128 ? 100.454 130.593 174.422 1.00 54.67  ? 1128 GLN A CA    1 
ATOM   8629  C  C     . GLN A 1  1128 ? 100.560 129.209 175.038 1.00 56.78  ? 1128 GLN A C     1 
ATOM   8630  O  O     . GLN A 1  1128 ? 99.586  128.451 175.044 1.00 57.82  ? 1128 GLN A O     1 
ATOM   8631  C  CB    . GLN A 1  1128 ? 100.090 131.617 175.497 1.00 54.86  ? 1128 GLN A CB    1 
ATOM   8632  C  CG    . GLN A 1  1128 ? 99.875  133.025 174.960 1.00 56.07  ? 1128 GLN A CG    1 
ATOM   8633  C  CD    . GLN A 1  1128 ? 98.940  133.840 175.831 1.00 57.27  ? 1128 GLN A CD    1 
ATOM   8634  O  OE1   . GLN A 1  1128 ? 98.282  133.305 176.723 1.00 56.69  ? 1128 GLN A OE1   1 
ATOM   8635  N  NE2   . GLN A 1  1128 ? 98.874  135.141 175.574 1.00 54.34  ? 1128 GLN A NE2   1 
ATOM   8636  N  N     . TRP A 1  1129 ? 101.737 128.878 175.558 1.00 60.54  ? 1129 TRP A N     1 
ATOM   8637  C  CA    . TRP A 1  1129 ? 101.918 127.600 176.226 1.00 60.71  ? 1129 TRP A CA    1 
ATOM   8638  C  C     . TRP A 1  1129 ? 103.012 127.730 177.273 1.00 61.30  ? 1129 TRP A C     1 
ATOM   8639  O  O     . TRP A 1  1129 ? 104.103 128.230 176.993 1.00 61.97  ? 1129 TRP A O     1 
ATOM   8640  C  CB    . TRP A 1  1129 ? 102.250 126.486 175.227 1.00 58.93  ? 1129 TRP A CB    1 
ATOM   8641  C  CG    . TRP A 1  1129 ? 103.633 126.535 174.651 1.00 60.56  ? 1129 TRP A CG    1 
ATOM   8642  C  CD1   . TRP A 1  1129 ? 104.076 127.348 173.648 1.00 62.09  ? 1129 TRP A CD1   1 
ATOM   8643  C  CD2   . TRP A 1  1129 ? 104.752 125.726 175.035 1.00 62.44  ? 1129 TRP A CD2   1 
ATOM   8644  N  NE1   . TRP A 1  1129 ? 105.401 127.098 173.386 1.00 62.63  ? 1129 TRP A NE1   1 
ATOM   8645  C  CE2   . TRP A 1  1129 ? 105.841 126.108 174.225 1.00 62.54  ? 1129 TRP A CE2   1 
ATOM   8646  C  CE3   . TRP A 1  1129 ? 104.940 124.718 175.986 1.00 62.03  ? 1129 TRP A CE3   1 
ATOM   8647  C  CZ2   . TRP A 1  1129 ? 107.097 125.519 174.338 1.00 59.76  ? 1129 TRP A CZ2   1 
ATOM   8648  C  CZ3   . TRP A 1  1129 ? 106.188 124.135 176.094 1.00 61.61  ? 1129 TRP A CZ3   1 
ATOM   8649  C  CH2   . TRP A 1  1129 ? 107.250 124.537 175.276 1.00 59.92  ? 1129 TRP A CH2   1 
ATOM   8650  N  N     . HIS A 1  1130 ? 102.708 127.266 178.484 1.00 60.49  ? 1130 HIS A N     1 
ATOM   8651  C  CA    . HIS A 1  1130 ? 103.633 127.338 179.606 1.00 60.09  ? 1130 HIS A CA    1 
ATOM   8652  C  C     . HIS A 1  1130 ? 104.045 125.925 179.980 1.00 60.16  ? 1130 HIS A C     1 
ATOM   8653  O  O     . HIS A 1  1130 ? 103.187 125.083 180.263 1.00 58.74  ? 1130 HIS A O     1 
ATOM   8654  C  CB    . HIS A 1  1130 ? 103.004 128.029 180.825 1.00 57.48  ? 1130 HIS A CB    1 
ATOM   8655  C  CG    . HIS A 1  1130 ? 102.260 129.286 180.501 1.00 59.82  ? 1130 HIS A CG    1 
ATOM   8656  N  ND1   . HIS A 1  1130 ? 100.945 129.287 180.090 1.00 60.17  ? 1130 HIS A ND1   1 
ATOM   8657  C  CD2   . HIS A 1  1130 ? 102.643 130.584 180.541 1.00 60.21  ? 1130 HIS A CD2   1 
ATOM   8658  C  CE1   . HIS A 1  1130 ? 100.551 130.531 179.883 1.00 59.41  ? 1130 HIS A CE1   1 
ATOM   8659  N  NE2   . HIS A 1  1130 ? 101.563 131.338 180.149 1.00 60.65  ? 1130 HIS A NE2   1 
ATOM   8660  N  N     . LEU A 1  1131 ? 105.348 125.672 180.000 1.00 49.68  ? 1131 LEU A N     1 
ATOM   8661  C  CA    . LEU A 1  1131 ? 105.872 124.359 180.345 1.00 51.18  ? 1131 LEU A CA    1 
ATOM   8662  C  C     . LEU A 1  1131 ? 106.139 124.302 181.843 1.00 50.93  ? 1131 LEU A C     1 
ATOM   8663  O  O     . LEU A 1  1131 ? 106.830 125.167 182.393 1.00 49.44  ? 1131 LEU A O     1 
ATOM   8664  C  CB    . LEU A 1  1131 ? 107.145 124.038 179.551 1.00 51.02  ? 1131 LEU A CB    1 
ATOM   8665  C  CG    . LEU A 1  1131 ? 108.505 124.628 179.947 1.00 50.24  ? 1131 LEU A CG    1 
ATOM   8666  C  CD1   . LEU A 1  1131 ? 109.646 123.841 179.314 1.00 47.81  ? 1131 LEU A CD1   1 
ATOM   8667  C  CD2   . LEU A 1  1131 ? 108.601 126.104 179.578 1.00 48.29  ? 1131 LEU A CD2   1 
ATOM   8668  N  N     . LEU A 1  1132 ? 105.556 123.304 182.502 1.00 48.67  ? 1132 LEU A N     1 
ATOM   8669  C  CA    . LEU A 1  1132 ? 105.767 123.083 183.929 1.00 49.98  ? 1132 LEU A CA    1 
ATOM   8670  C  C     . LEU A 1  1132 ? 105.729 121.588 184.224 1.00 51.65  ? 1132 LEU A C     1 
ATOM   8671  O  O     . LEU A 1  1132 ? 105.645 120.769 183.306 1.00 52.90  ? 1132 LEU A O     1 
ATOM   8672  C  CB    . LEU A 1  1132 ? 104.717 123.818 184.769 1.00 49.28  ? 1132 LEU A CB    1 
ATOM   8673  C  CG    . LEU A 1  1132 ? 104.791 125.347 184.808 1.00 49.89  ? 1132 LEU A CG    1 
ATOM   8674  C  CD1   . LEU A 1  1132 ? 103.565 125.953 185.483 1.00 47.05  ? 1132 LEU A CD1   1 
ATOM   8675  C  CD2   . LEU A 1  1132 ? 106.077 125.806 185.489 1.00 47.43  ? 1132 LEU A CD2   1 
ATOM   8676  N  N     . VAL A 1  1143 ? 98.853  124.415 196.868 1.00 47.12  ? 1143 VAL A N     1 
ATOM   8677  C  CA    . VAL A 1  1143 ? 98.902  125.765 196.324 1.00 49.12  ? 1143 VAL A CA    1 
ATOM   8678  C  C     . VAL A 1  1143 ? 99.932  125.823 195.206 1.00 48.35  ? 1143 VAL A C     1 
ATOM   8679  O  O     . VAL A 1  1143 ? 101.138 125.777 195.453 1.00 47.31  ? 1143 VAL A O     1 
ATOM   8680  C  CB    . VAL A 1  1143 ? 99.217  126.800 197.417 1.00 49.14  ? 1143 VAL A CB    1 
ATOM   8681  C  CG1   . VAL A 1  1143 ? 98.941  128.214 196.910 1.00 47.76  ? 1143 VAL A CG1   1 
ATOM   8682  C  CG2   . VAL A 1  1143 ? 98.415  126.508 198.671 1.00 46.80  ? 1143 VAL A CG2   1 
ATOM   8683  N  N     . MET A 1  1144 ? 99.442  125.908 193.974 1.00 57.35  ? 1144 MET A N     1 
ATOM   8684  C  CA    . MET A 1  1144 ? 100.284 125.881 192.789 1.00 57.89  ? 1144 MET A CA    1 
ATOM   8685  C  C     . MET A 1  1144 ? 100.595 127.301 192.316 1.00 58.28  ? 1144 MET A C     1 
ATOM   8686  O  O     . MET A 1  1144 ? 100.389 128.285 193.030 1.00 57.29  ? 1144 MET A O     1 
ATOM   8687  C  CB    . MET A 1  1144 ? 99.623  125.045 191.696 1.00 56.15  ? 1144 MET A CB    1 
ATOM   8688  C  CG    . MET A 1  1144 ? 98.883  123.831 192.220 1.00 57.01  ? 1144 MET A CG    1 
ATOM   8689  S  SD    . MET A 1  1144 ? 99.975  122.767 193.182 1.00 66.45  ? 1144 MET A SD    1 
ATOM   8690  C  CE    . MET A 1  1144 ? 98.789  121.729 194.027 1.00 55.55  ? 1144 MET A CE    1 
ATOM   8691  N  N     . TYR A 1  1145 ? 101.102 127.402 191.092 1.00 56.54  ? 1145 TYR A N     1 
ATOM   8692  C  CA    . TYR A 1  1145 ? 101.581 128.618 190.449 1.00 54.04  ? 1145 TYR A CA    1 
ATOM   8693  C  C     . TYR A 1  1145 ? 100.499 129.694 190.412 1.00 54.29  ? 1145 TYR A C     1 
ATOM   8694  O  O     . TYR A 1  1145 ? 99.311  129.386 190.569 1.00 51.90  ? 1145 TYR A O     1 
ATOM   8695  C  CB    . TYR A 1  1145 ? 102.058 128.284 189.033 1.00 52.94  ? 1145 TYR A CB    1 
ATOM   8696  C  CG    . TYR A 1  1145 ? 103.171 127.259 188.986 1.00 53.28  ? 1145 TYR A CG    1 
ATOM   8697  C  CD1   . TYR A 1  1145 ? 104.499 127.648 188.859 1.00 54.79  ? 1145 TYR A CD1   1 
ATOM   8698  C  CD2   . TYR A 1  1145 ? 102.892 125.899 189.067 1.00 54.13  ? 1145 TYR A CD2   1 
ATOM   8699  C  CE1   . TYR A 1  1145 ? 105.516 126.706 188.811 1.00 57.25  ? 1145 TYR A CE1   1 
ATOM   8700  C  CE2   . TYR A 1  1145 ? 103.898 124.956 189.020 1.00 53.27  ? 1145 TYR A CE2   1 
ATOM   8701  C  CZ    . TYR A 1  1145 ? 105.207 125.360 188.892 1.00 54.75  ? 1145 TYR A CZ    1 
ATOM   8702  O  OH    . TYR A 1  1145 ? 106.206 124.414 188.847 1.00 50.47  ? 1145 TYR A OH    1 
ATOM   8703  N  N     . PRO A 1  1146 ? 100.864 130.959 190.212 1.00 47.66  ? 1146 PRO A N     1 
ATOM   8704  C  CA    . PRO A 1  1146 ? 99.848  132.008 190.089 1.00 48.37  ? 1146 PRO A CA    1 
ATOM   8705  C  C     . PRO A 1  1146 ? 99.035  131.865 188.812 1.00 47.43  ? 1146 PRO A C     1 
ATOM   8706  O  O     . PRO A 1  1146 ? 99.420  131.173 187.868 1.00 44.38  ? 1146 PRO A O     1 
ATOM   8707  C  CB    . PRO A 1  1146 ? 100.672 133.300 190.078 1.00 48.28  ? 1146 PRO A CB    1 
ATOM   8708  C  CG    . PRO A 1  1146 ? 102.017 132.882 189.598 1.00 44.79  ? 1146 PRO A CG    1 
ATOM   8709  C  CD    . PRO A 1  1146 ? 102.229 131.511 190.158 1.00 43.37  ? 1146 PRO A CD    1 
ATOM   8710  N  N     . ASP A 1  1147 ? 97.882  132.542 188.805 1.00 53.08  ? 1147 ASP A N     1 
ATOM   8711  C  CA    . ASP A 1  1147 ? 96.911  132.492 187.712 1.00 55.87  ? 1147 ASP A CA    1 
ATOM   8712  C  C     . ASP A 1  1147 ? 96.374  131.083 187.487 1.00 57.69  ? 1147 ASP A C     1 
ATOM   8713  O  O     . ASP A 1  1147 ? 95.924  130.754 186.383 1.00 56.44  ? 1147 ASP A O     1 
ATOM   8714  C  CB    . ASP A 1  1147 ? 97.505  133.038 186.405 1.00 56.43  ? 1147 ASP A CB    1 
ATOM   8715  C  CG    . ASP A 1  1147 ? 97.653  134.551 186.408 1.00 57.58  ? 1147 ASP A CG    1 
ATOM   8716  O  OD1   . ASP A 1  1147 ? 96.860  135.232 187.093 1.00 57.97  ? 1147 ASP A OD1   1 
ATOM   8717  O  OD2   . ASP A 1  1147 ? 98.575  135.053 185.731 1.00 56.43  ? 1147 ASP A OD2   1 
ATOM   8718  N  N     . PHE A 1  1148 ? 96.429  130.232 188.511 1.00 56.87  ? 1148 PHE A N     1 
ATOM   8719  C  CA    . PHE A 1  1148 ? 96.003  128.843 188.399 1.00 56.22  ? 1148 PHE A CA    1 
ATOM   8720  C  C     . PHE A 1  1148 ? 94.764  128.527 189.227 1.00 56.38  ? 1148 PHE A C     1 
ATOM   8721  O  O     . PHE A 1  1148 ? 94.508  127.353 189.515 1.00 55.27  ? 1148 PHE A O     1 
ATOM   8722  C  CB    . PHE A 1  1148 ? 97.146  127.896 188.783 1.00 56.91  ? 1148 PHE A CB    1 
ATOM   8723  C  CG    . PHE A 1  1148 ? 98.146  127.659 187.679 1.00 56.84  ? 1148 PHE A CG    1 
ATOM   8724  C  CD1   . PHE A 1  1148 ? 98.205  128.495 186.575 1.00 56.45  ? 1148 PHE A CD1   1 
ATOM   8725  C  CD2   . PHE A 1  1148 ? 98.992  126.562 187.724 1.00 55.27  ? 1148 PHE A CD2   1 
ATOM   8726  C  CE1   . PHE A 1  1148 ? 99.109  128.259 185.553 1.00 57.97  ? 1148 PHE A CE1   1 
ATOM   8727  C  CE2   . PHE A 1  1148 ? 99.899  126.321 186.707 1.00 55.74  ? 1148 PHE A CE2   1 
ATOM   8728  C  CZ    . PHE A 1  1148 ? 99.955  127.170 185.620 1.00 57.98  ? 1148 PHE A CZ    1 
ATOM   8729  N  N     . ALA A 1  1149 ? 93.990  129.541 189.622 1.00 49.64  ? 1149 ALA A N     1 
ATOM   8730  C  CA    . ALA A 1  1149 ? 92.748  129.277 190.343 1.00 50.45  ? 1149 ALA A CA    1 
ATOM   8731  C  C     . ALA A 1  1149 ? 91.699  128.623 189.449 1.00 49.99  ? 1149 ALA A C     1 
ATOM   8732  O  O     . ALA A 1  1149 ? 90.984  127.719 189.892 1.00 48.20  ? 1149 ALA A O     1 
ATOM   8733  C  CB    . ALA A 1  1149 ? 92.201  130.572 190.943 1.00 48.88  ? 1149 ALA A CB    1 
ATOM   8734  N  N     . SER A 1  1150 ? 91.583  129.063 188.195 1.00 50.07  ? 1150 SER A N     1 
ATOM   8735  C  CA    . SER A 1  1150 ? 90.625  128.430 187.295 1.00 50.98  ? 1150 SER A CA    1 
ATOM   8736  C  C     . SER A 1  1150 ? 91.068  127.019 186.923 1.00 54.09  ? 1150 SER A C     1 
ATOM   8737  O  O     . SER A 1  1150 ? 90.243  126.184 186.531 1.00 53.24  ? 1150 SER A O     1 
ATOM   8738  C  CB    . SER A 1  1150 ? 90.425  129.287 186.045 1.00 50.42  ? 1150 SER A CB    1 
ATOM   8739  O  OG    . SER A 1  1150 ? 89.890  130.555 186.380 1.00 51.60  ? 1150 SER A OG    1 
ATOM   8740  N  N     . ASP A 1  1151 ? 92.369  126.738 187.032 1.00 52.94  ? 1151 ASP A N     1 
ATOM   8741  C  CA    . ASP A 1  1151 ? 92.868  125.396 186.747 1.00 51.96  ? 1151 ASP A CA    1 
ATOM   8742  C  C     . ASP A 1  1151 ? 92.414  124.395 187.800 1.00 52.37  ? 1151 ASP A C     1 
ATOM   8743  O  O     . ASP A 1  1151 ? 92.003  123.277 187.466 1.00 51.51  ? 1151 ASP A O     1 
ATOM   8744  C  CB    . ASP A 1  1151 ? 94.389  125.422 186.650 1.00 52.23  ? 1151 ASP A CB    1 
ATOM   8745  C  CG    . ASP A 1  1151 ? 94.879  126.314 185.537 1.00 55.13  ? 1151 ASP A CG    1 
ATOM   8746  O  OD1   . ASP A 1  1151 ? 94.094  126.596 184.607 1.00 57.08  ? 1151 ASP A OD1   1 
ATOM   8747  O  OD2   . ASP A 1  1151 ? 96.048  126.735 185.598 1.00 51.87  ? 1151 ASP A OD2   1 
ATOM   8748  N  N     . VAL A 1  1152 ? 92.502  124.763 189.081 1.00 51.09  ? 1152 VAL A N     1 
ATOM   8749  C  CA    . VAL A 1  1152 ? 91.897  123.917 190.104 1.00 51.17  ? 1152 VAL A CA    1 
ATOM   8750  C  C     . VAL A 1  1152 ? 90.380  123.990 190.009 1.00 50.03  ? 1152 VAL A C     1 
ATOM   8751  O  O     . VAL A 1  1152 ? 89.686  123.020 190.336 1.00 50.47  ? 1152 VAL A O     1 
ATOM   8752  C  CB    . VAL A 1  1152 ? 92.415  124.283 191.509 1.00 50.63  ? 1152 VAL A CB    1 
ATOM   8753  C  CG1   . VAL A 1  1152 ? 91.885  125.626 191.963 1.00 49.27  ? 1152 VAL A CG1   1 
ATOM   8754  C  CG2   . VAL A 1  1152 ? 92.036  123.199 192.507 1.00 50.37  ? 1152 VAL A CG2   1 
ATOM   8755  N  N     . GLU A 1  1153 ? 89.838  125.123 189.551 1.00 48.06  ? 1153 GLU A N     1 
ATOM   8756  C  CA    . GLU A 1  1153 ? 88.432  125.152 189.160 1.00 50.72  ? 1153 GLU A CA    1 
ATOM   8757  C  C     . GLU A 1  1153 ? 88.181  124.234 187.973 1.00 51.02  ? 1153 GLU A C     1 
ATOM   8758  O  O     . GLU A 1  1153 ? 87.151  123.552 187.920 1.00 49.96  ? 1153 GLU A O     1 
ATOM   8759  C  CB    . GLU A 1  1153 ? 87.985  126.576 188.831 1.00 49.55  ? 1153 GLU A CB    1 
ATOM   8760  C  CG    . GLU A 1  1153 ? 86.479  126.708 188.657 1.00 48.99  ? 1153 GLU A CG    1 
ATOM   8761  C  CD    . GLU A 1  1153 ? 86.047  128.118 188.313 1.00 49.99  ? 1153 GLU A CD    1 
ATOM   8762  O  OE1   . GLU A 1  1153 ? 86.927  128.987 188.142 1.00 48.85  ? 1153 GLU A OE1   1 
ATOM   8763  O  OE2   . GLU A 1  1153 ? 84.825  128.353 188.206 1.00 49.27  ? 1153 GLU A OE2   1 
ATOM   8764  N  N     . TRP A 1  1154 ? 89.106  124.204 187.008 1.00 47.67  ? 1154 TRP A N     1 
ATOM   8765  C  CA    . TRP A 1  1154 ? 89.022  123.206 185.946 1.00 49.00  ? 1154 TRP A CA    1 
ATOM   8766  C  C     . TRP A 1  1154 ? 89.142  121.799 186.509 1.00 50.21  ? 1154 TRP A C     1 
ATOM   8767  O  O     . TRP A 1  1154 ? 88.477  120.878 186.026 1.00 49.04  ? 1154 TRP A O     1 
ATOM   8768  C  CB    . TRP A 1  1154 ? 90.102  123.448 184.892 1.00 46.25  ? 1154 TRP A CB    1 
ATOM   8769  N  N     . MET A 1  1155 ? 89.978  121.616 187.530 1.00 57.49  ? 1155 MET A N     1 
ATOM   8770  C  CA    . MET A 1  1155 ? 90.033  120.328 188.209 1.00 59.31  ? 1155 MET A CA    1 
ATOM   8771  C  C     . MET A 1  1155 ? 88.735  120.031 188.947 1.00 60.29  ? 1155 MET A C     1 
ATOM   8772  O  O     . MET A 1  1155 ? 88.396  118.861 189.165 1.00 60.51  ? 1155 MET A O     1 
ATOM   8773  C  CB    . MET A 1  1155 ? 91.210  120.304 189.181 1.00 57.42  ? 1155 MET A CB    1 
ATOM   8774  C  CG    . MET A 1  1155 ? 92.564  120.118 188.520 1.00 58.27  ? 1155 MET A CG    1 
ATOM   8775  S  SD    . MET A 1  1155 ? 93.806  119.523 189.684 1.00 67.17  ? 1155 MET A SD    1 
ATOM   8776  C  CE    . MET A 1  1155 ? 92.986  119.819 191.248 1.00 58.16  ? 1155 MET A CE    1 
ATOM   8777  N  N     . THR A 1  1156 ? 87.992  121.073 189.326 1.00 51.81  ? 1156 THR A N     1 
ATOM   8778  C  CA    . THR A 1  1156 ? 86.812  120.883 190.163 1.00 54.11  ? 1156 THR A CA    1 
ATOM   8779  C  C     . THR A 1  1156 ? 85.599  120.499 189.325 1.00 53.89  ? 1156 THR A C     1 
ATOM   8780  O  O     . THR A 1  1156 ? 84.899  119.526 189.628 1.00 52.69  ? 1156 THR A O     1 
ATOM   8781  C  CB    . THR A 1  1156 ? 86.528  122.159 190.959 1.00 52.80  ? 1156 THR A CB    1 
ATOM   8782  O  OG1   . THR A 1  1156 ? 87.724  122.593 191.614 1.00 51.72  ? 1156 THR A OG1   1 
ATOM   8783  C  CG2   . THR A 1  1156 ? 85.457  121.901 192.008 1.00 51.23  ? 1156 THR A CG2   1 
ATOM   8784  N  N     . ASP A 1  1157 ? 85.328  121.269 188.271 1.00 54.40  ? 1157 ASP A N     1 
ATOM   8785  C  CA    . ASP A 1  1157 ? 84.106  121.072 187.499 1.00 55.30  ? 1157 ASP A CA    1 
ATOM   8786  C  C     . ASP A 1  1157 ? 84.242  119.949 186.476 1.00 54.93  ? 1157 ASP A C     1 
ATOM   8787  O  O     . ASP A 1  1157 ? 83.232  119.465 185.958 1.00 51.65  ? 1157 ASP A O     1 
ATOM   8788  C  CB    . ASP A 1  1157 ? 83.718  122.383 186.818 1.00 53.09  ? 1157 ASP A CB    1 
ATOM   8789  C  CG    . ASP A 1  1157 ? 84.860  122.985 186.023 1.00 54.40  ? 1157 ASP A CG    1 
ATOM   8790  O  OD1   . ASP A 1  1157 ? 85.905  122.316 185.880 1.00 52.34  ? 1157 ASP A OD1   1 
ATOM   8791  O  OD2   . ASP A 1  1157 ? 84.722  124.138 185.566 1.00 54.86  ? 1157 ASP A OD2   1 
ATOM   8792  N  N     . PHE A 1  1158 ? 85.469  119.542 186.146 1.00 59.12  ? 1158 PHE A N     1 
ATOM   8793  C  CA    . PHE A 1  1158 ? 85.640  118.486 185.154 1.00 58.72  ? 1158 PHE A CA    1 
ATOM   8794  C  C     . PHE A 1  1158 ? 85.361  117.117 185.759 1.00 58.87  ? 1158 PHE A C     1 
ATOM   8795  O  O     . PHE A 1  1158 ? 84.753  116.257 185.111 1.00 58.66  ? 1158 PHE A O     1 
ATOM   8796  C  CB    . PHE A 1  1158 ? 87.053  118.528 184.570 1.00 57.60  ? 1158 PHE A CB    1 
ATOM   8797  C  CG    . PHE A 1  1158 ? 87.252  117.627 183.381 1.00 60.11  ? 1158 PHE A CG    1 
ATOM   8798  C  CD1   . PHE A 1  1158 ? 87.093  118.118 182.095 1.00 57.65  ? 1158 PHE A CD1   1 
ATOM   8799  C  CD2   . PHE A 1  1158 ? 87.567  116.289 183.544 1.00 60.26  ? 1158 PHE A CD2   1 
ATOM   8800  C  CE1   . PHE A 1  1158 ? 87.273  117.302 180.999 1.00 55.99  ? 1158 PHE A CE1   1 
ATOM   8801  C  CE2   . PHE A 1  1158 ? 87.746  115.467 182.449 1.00 60.72  ? 1158 PHE A CE2   1 
ATOM   8802  C  CZ    . PHE A 1  1158 ? 87.597  115.977 181.176 1.00 59.45  ? 1158 PHE A CZ    1 
ATOM   8803  N  N     . LEU A 1  1159 ? 85.801  116.895 187.002 1.00 52.29  ? 1159 LEU A N     1 
ATOM   8804  C  CA    . LEU A 1  1159 ? 85.656  115.580 187.618 1.00 53.80  ? 1159 LEU A CA    1 
ATOM   8805  C  C     . LEU A 1  1159 ? 84.200  115.233 187.890 1.00 54.66  ? 1159 LEU A C     1 
ATOM   8806  O  O     . LEU A 1  1159 ? 83.878  114.061 188.109 1.00 54.28  ? 1159 LEU A O     1 
ATOM   8807  C  CB    . LEU A 1  1159 ? 86.474  115.505 188.907 1.00 52.90  ? 1159 LEU A CB    1 
ATOM   8808  C  CG    . LEU A 1  1159 ? 87.783  114.717 188.810 1.00 52.28  ? 1159 LEU A CG    1 
ATOM   8809  C  CD1   . LEU A 1  1159 ? 87.480  113.231 188.772 1.00 51.63  ? 1159 LEU A CD1   1 
ATOM   8810  C  CD2   . LEU A 1  1159 ? 88.584  115.127 187.584 1.00 51.53  ? 1159 LEU A CD2   1 
ATOM   8811  N  N     . GLU A 1  1160 ? 83.313  116.226 187.896 1.00 58.51  ? 1160 GLU A N     1 
ATOM   8812  C  CA    . GLU A 1  1160 ? 81.889  115.939 187.993 1.00 57.73  ? 1160 GLU A CA    1 
ATOM   8813  C  C     . GLU A 1  1160 ? 81.240  115.702 186.637 1.00 56.71  ? 1160 GLU A C     1 
ATOM   8814  O  O     . GLU A 1  1160 ? 80.130  115.162 186.586 1.00 56.93  ? 1160 GLU A O     1 
ATOM   8815  C  CB    . GLU A 1  1160 ? 81.171  117.081 188.718 1.00 56.14  ? 1160 GLU A CB    1 
ATOM   8816  C  CG    . GLU A 1  1160 ? 81.297  118.436 188.040 1.00 53.93  ? 1160 GLU A CG    1 
ATOM   8817  C  CD    . GLU A 1  1160 ? 80.206  118.700 187.028 1.00 56.19  ? 1160 GLU A CD    1 
ATOM   8818  O  OE1   . GLU A 1  1160 ? 79.147  118.046 187.105 1.00 55.93  ? 1160 GLU A OE1   1 
ATOM   8819  O  OE2   . GLU A 1  1160 ? 80.407  119.566 186.151 1.00 58.11  ? 1160 GLU A OE2   1 
ATOM   8820  N  N     . ASN A 1  1161 ? 81.898  116.091 185.543 1.00 51.13  ? 1161 ASN A N     1 
ATOM   8821  C  CA    . ASN A 1  1161 ? 81.261  116.003 184.233 1.00 52.66  ? 1161 ASN A CA    1 
ATOM   8822  C  C     . ASN A 1  1161 ? 81.105  114.554 183.784 1.00 53.56  ? 1161 ASN A C     1 
ATOM   8823  O  O     . ASN A 1  1161 ? 80.021  114.137 183.361 1.00 51.23  ? 1161 ASN A O     1 
ATOM   8824  C  CB    . ASN A 1  1161 ? 82.055  116.815 183.214 1.00 53.04  ? 1161 ASN A CB    1 
ATOM   8825  C  CG    . ASN A 1  1161 ? 81.780  118.296 183.321 1.00 53.04  ? 1161 ASN A CG    1 
ATOM   8826  O  OD1   . ASN A 1  1161 ? 80.629  118.717 183.419 1.00 52.86  ? 1161 ASN A OD1   1 
ATOM   8827  N  ND2   . ASN A 1  1161 ? 82.836  119.099 183.302 1.00 51.80  ? 1161 ASN A ND2   1 
ATOM   8828  N  N     . HIS A 1  1162 ? 82.175  113.767 183.879 1.00 53.76  ? 1162 HIS A N     1 
ATOM   8829  C  CA    . HIS A 1  1162 ? 82.053  112.336 183.632 1.00 54.98  ? 1162 HIS A CA    1 
ATOM   8830  C  C     . HIS A 1  1162 ? 83.001  111.576 184.552 1.00 56.15  ? 1162 HIS A C     1 
ATOM   8831  O  O     . HIS A 1  1162 ? 84.224  111.762 184.487 1.00 53.51  ? 1162 HIS A O     1 
ATOM   8832  C  CB    . HIS A 1  1162 ? 82.330  112.003 182.162 1.00 52.47  ? 1162 HIS A CB    1 
ATOM   8833  C  CG    . HIS A 1  1162 ? 83.680  112.432 181.683 1.00 54.28  ? 1162 HIS A CG    1 
ATOM   8834  N  ND1   . HIS A 1  1162 ? 84.791  111.621 181.769 1.00 55.50  ? 1162 HIS A ND1   1 
ATOM   8835  C  CD2   . HIS A 1  1162 ? 84.102  113.591 181.123 1.00 54.29  ? 1162 HIS A CD2   1 
ATOM   8836  C  CE1   . HIS A 1  1162 ? 85.838  112.258 181.274 1.00 54.41  ? 1162 HIS A CE1   1 
ATOM   8837  N  NE2   . HIS A 1  1162 ? 85.447  113.456 180.877 1.00 54.24  ? 1162 HIS A NE2   1 
ATOM   8838  N  N     . PRO A 1  1163 ? 82.477  110.717 185.424 1.00 53.78  ? 1163 PRO A N     1 
ATOM   8839  C  CA    . PRO A 1  1163 ? 83.327  109.965 186.357 1.00 50.59  ? 1163 PRO A CA    1 
ATOM   8840  C  C     . PRO A 1  1163 ? 83.978  108.727 185.760 1.00 48.09  ? 1163 PRO A C     1 
ATOM   8841  O  O     . PRO A 1  1163 ? 84.576  107.949 186.509 1.00 46.41  ? 1163 PRO A O     1 
ATOM   8842  C  CB    . PRO A 1  1163 ? 82.330  109.565 187.451 1.00 49.20  ? 1163 PRO A CB    1 
ATOM   8843  C  CG    . PRO A 1  1163 ? 81.045  109.381 186.713 1.00 48.06  ? 1163 PRO A CG    1 
ATOM   8844  C  CD    . PRO A 1  1163 ? 81.052  110.372 185.570 1.00 47.50  ? 1163 PRO A CD    1 
ATOM   8845  N  N     . LEU A 1  1164 ? 83.868  108.530 184.446 1.00 47.76  ? 1164 LEU A N     1 
ATOM   8846  C  CA    . LEU A 1  1164 ? 84.522  107.394 183.806 1.00 50.46  ? 1164 LEU A CA    1 
ATOM   8847  C  C     . LEU A 1  1164 ? 86.032  107.468 183.984 1.00 48.45  ? 1164 LEU A C     1 
ATOM   8848  O  O     . LEU A 1  1164 ? 86.686  106.465 184.294 1.00 45.49  ? 1164 LEU A O     1 
ATOM   8849  C  CB    . LEU A 1  1164 ? 84.154  107.355 182.324 1.00 49.35  ? 1164 LEU A CB    1 
ATOM   8850  C  CG    . LEU A 1  1164 ? 85.075  106.532 181.425 1.00 48.15  ? 1164 LEU A CG    1 
ATOM   8851  C  CD1   . LEU A 1  1164 ? 84.874  105.043 181.684 1.00 46.27  ? 1164 LEU A CD1   1 
ATOM   8852  C  CD2   . LEU A 1  1164 ? 84.846  106.875 179.963 1.00 46.50  ? 1164 LEU A CD2   1 
ATOM   8853  N  N     . LEU A 1  1165 ? 86.599  108.658 183.813 1.00 49.52  ? 1165 LEU A N     1 
ATOM   8854  C  CA    . LEU A 1  1165 ? 88.032  108.872 183.937 1.00 48.93  ? 1165 LEU A CA    1 
ATOM   8855  C  C     . LEU A 1  1165 ? 88.320  109.771 185.127 1.00 48.83  ? 1165 LEU A C     1 
ATOM   8856  O  O     . LEU A 1  1165 ? 87.422  110.435 185.654 1.00 48.33  ? 1165 LEU A O     1 
ATOM   8857  C  CB    . LEU A 1  1165 ? 88.624  109.496 182.668 1.00 47.11  ? 1165 LEU A CB    1 
ATOM   8858  C  CG    . LEU A 1  1165 ? 88.810  108.571 181.465 1.00 49.43  ? 1165 LEU A CG    1 
ATOM   8859  C  CD1   . LEU A 1  1165 ? 89.156  109.384 180.229 1.00 47.83  ? 1165 LEU A CD1   1 
ATOM   8860  C  CD2   . LEU A 1  1165 ? 89.881  107.516 181.738 1.00 46.14  ? 1165 LEU A CD2   1 
ATOM   8861  N  N     . GLN A 1  1166 ? 89.572  109.760 185.555 1.00 50.84  ? 1166 GLN A N     1 
ATOM   8862  C  CA    . GLN A 1  1166 ? 90.085  110.650 186.584 1.00 51.17  ? 1166 GLN A CA    1 
ATOM   8863  C  C     . GLN A 1  1166 ? 91.603  110.669 186.447 1.00 53.64  ? 1166 GLN A C     1 
ATOM   8864  O  O     . GLN A 1  1166 ? 92.156  109.838 185.714 1.00 51.54  ? 1166 GLN A O     1 
ATOM   8865  C  CB    . GLN A 1  1166 ? 89.639  110.182 187.969 1.00 48.36  ? 1166 GLN A CB    1 
ATOM   8866  C  CG    . GLN A 1  1166 ? 89.923  108.724 188.243 1.00 49.94  ? 1166 GLN A CG    1 
ATOM   8867  C  CD    . GLN A 1  1166 ? 91.059  108.540 189.221 1.00 51.54  ? 1166 GLN A CD    1 
ATOM   8868  O  OE1   . GLN A 1  1166 ? 91.225  109.327 190.151 1.00 51.72  ? 1166 GLN A OE1   1 
ATOM   8869  N  NE2   . GLN A 1  1166 ? 91.854  107.498 189.013 1.00 51.42  ? 1166 GLN A NE2   1 
ATOM   8870  N  N     . PRO A 1  1167 ? 92.304  111.604 187.086 1.00 58.51  ? 1167 PRO A N     1 
ATOM   8871  C  CA    . PRO A 1  1167 ? 93.770  111.582 187.054 1.00 55.26  ? 1167 PRO A CA    1 
ATOM   8872  C  C     . PRO A 1  1167 ? 94.299  110.219 187.457 1.00 55.38  ? 1167 PRO A C     1 
ATOM   8873  O  O     . PRO A 1  1167 ? 94.070  109.756 188.585 1.00 51.56  ? 1167 PRO A O     1 
ATOM   8874  C  CB    . PRO A 1  1167 ? 94.158  112.664 188.069 1.00 52.26  ? 1167 PRO A CB    1 
ATOM   8875  C  CG    . PRO A 1  1167 ? 93.046  113.650 187.962 1.00 52.56  ? 1167 PRO A CG    1 
ATOM   8876  C  CD    . PRO A 1  1167 ? 91.793  112.841 187.706 1.00 54.54  ? 1167 PRO A CD    1 
ATOM   8877  N  N     . PRO A 1  1168 ? 95.017  109.545 186.554 1.00 55.76  ? 1168 PRO A N     1 
ATOM   8878  C  CA    . PRO A 1  1168 ? 95.304  108.120 186.748 1.00 52.33  ? 1168 PRO A CA    1 
ATOM   8879  C  C     . PRO A 1  1168 ? 96.341  107.855 187.825 1.00 52.50  ? 1168 PRO A C     1 
ATOM   8880  O  O     . PRO A 1  1168 ? 96.782  108.766 188.533 1.00 51.51  ? 1168 PRO A O     1 
ATOM   8881  C  CB    . PRO A 1  1168 ? 95.808  107.681 185.370 1.00 53.00  ? 1168 PRO A CB    1 
ATOM   8882  C  CG    . PRO A 1  1168 ? 96.424  108.907 184.803 1.00 53.17  ? 1168 PRO A CG    1 
ATOM   8883  C  CD    . PRO A 1  1168 ? 95.630  110.072 185.322 1.00 52.85  ? 1168 PRO A CD    1 
ATOM   8884  N  N     . GLU A 1  1169 ? 96.730  106.587 187.948 1.00 51.66  ? 1169 GLU A N     1 
ATOM   8885  C  CA    . GLU A 1  1169 ? 97.646  106.176 189.001 1.00 50.81  ? 1169 GLU A CA    1 
ATOM   8886  C  C     . GLU A 1  1169 ? 99.055  106.705 188.778 1.00 52.13  ? 1169 GLU A C     1 
ATOM   8887  O  O     . GLU A 1  1169 ? 99.847  106.752 189.726 1.00 50.70  ? 1169 GLU A O     1 
ATOM   8888  C  CB    . GLU A 1  1169 ? 97.664  104.651 189.082 1.00 47.98  ? 1169 GLU A CB    1 
ATOM   8889  C  CG    . GLU A 1  1169 ? 96.378  104.052 189.631 1.00 49.40  ? 1169 GLU A CG    1 
ATOM   8890  C  CD    . GLU A 1  1169 ? 95.257  104.004 188.596 1.00 52.97  ? 1169 GLU A CD    1 
ATOM   8891  O  OE1   . GLU A 1  1169 ? 95.502  104.379 187.428 1.00 51.98  ? 1169 GLU A OE1   1 
ATOM   8892  O  OE2   . GLU A 1  1169 ? 94.133  103.588 188.950 1.00 52.34  ? 1169 GLU A OE2   1 
ATOM   8893  N  N     . ASP A 1  1170 ? 99.378  107.118 187.555 1.00 57.17  ? 1170 ASP A N     1 
ATOM   8894  C  CA    . ASP A 1  1170 ? 100.739 107.485 187.172 1.00 56.87  ? 1170 ASP A CA    1 
ATOM   8895  C  C     . ASP A 1  1170 ? 100.734 108.945 186.717 1.00 54.18  ? 1170 ASP A C     1 
ATOM   8896  O  O     . ASP A 1  1170 ? 100.539 109.245 185.539 1.00 52.70  ? 1170 ASP A O     1 
ATOM   8897  C  CB    . ASP A 1  1170 ? 101.255 106.550 186.075 1.00 54.91  ? 1170 ASP A CB    1 
ATOM   8898  C  CG    . ASP A 1  1170 ? 102.764 106.464 186.050 1.00 55.65  ? 1170 ASP A CG    1 
ATOM   8899  O  OD1   . ASP A 1  1170 ? 103.397 107.078 186.934 1.00 55.46  ? 1170 ASP A OD1   1 
ATOM   8900  O  OD2   . ASP A 1  1170 ? 103.317 105.789 185.153 1.00 53.94  ? 1170 ASP A OD2   1 
ATOM   8901  N  N     . ILE A 1  1171 ? 100.926 109.853 187.669 1.00 49.82  ? 1171 ILE A N     1 
ATOM   8902  C  CA    . ILE A 1  1171 ? 101.090 111.274 187.379 1.00 51.59  ? 1171 ILE A CA    1 
ATOM   8903  C  C     . ILE A 1  1171 ? 102.045 111.858 188.414 1.00 53.33  ? 1171 ILE A C     1 
ATOM   8904  O  O     . ILE A 1  1171 ? 101.708 111.953 189.600 1.00 50.99  ? 1171 ILE A O     1 
ATOM   8905  C  CB    . ILE A 1  1171 ? 99.728  111.994 187.369 1.00 50.13  ? 1171 ILE A CB    1 
ATOM   8906  C  CG1   . ILE A 1  1171 ? 99.899  113.493 187.601 1.00 50.68  ? 1171 ILE A CG1   1 
ATOM   8907  C  CG2   . ILE A 1  1171 ? 98.772  111.376 188.388 1.00 50.00  ? 1171 ILE A CG2   1 
ATOM   8908  C  CD1   . ILE A 1  1171 ? 98.608  114.250 187.532 1.00 51.08  ? 1171 ILE A CD1   1 
ATOM   8909  N  N     . ALA A 1  1172 ? 103.256 112.226 187.986 1.00 49.57  ? 1172 ALA A N     1 
ATOM   8910  C  CA    . ALA A 1  1172 ? 104.302 112.502 188.966 1.00 49.08  ? 1172 ALA A CA    1 
ATOM   8911  C  C     . ALA A 1  1172 ? 104.517 113.972 189.308 1.00 49.40  ? 1172 ALA A C     1 
ATOM   8912  O  O     . ALA A 1  1172 ? 104.259 114.385 190.443 1.00 47.20  ? 1172 ALA A O     1 
ATOM   8913  C  CB    . ALA A 1  1172 ? 105.625 111.909 188.481 1.00 45.53  ? 1172 ALA A CB    1 
ATOM   8914  N  N     . ASN A 1  1173 ? 104.990 114.779 188.351 1.00 54.96  ? 1173 ASN A N     1 
ATOM   8915  C  CA    . ASN A 1  1173 ? 105.452 116.109 188.735 1.00 52.81  ? 1173 ASN A CA    1 
ATOM   8916  C  C     . ASN A 1  1173 ? 105.212 117.223 187.721 1.00 53.76  ? 1173 ASN A C     1 
ATOM   8917  O  O     . ASN A 1  1173 ? 105.614 118.360 187.999 1.00 54.65  ? 1173 ASN A O     1 
ATOM   8918  C  CB    . ASN A 1  1173 ? 106.952 116.056 189.053 1.00 51.78  ? 1173 ASN A CB    1 
ATOM   8919  C  CG    . ASN A 1  1173 ? 107.727 115.209 188.062 1.00 54.03  ? 1173 ASN A CG    1 
ATOM   8920  O  OD1   . ASN A 1  1173 ? 107.160 114.656 187.123 1.00 52.39  ? 1173 ASN A OD1   1 
ATOM   8921  N  ND2   . ASN A 1  1173 ? 109.031 115.095 188.275 1.00 53.56  ? 1173 ASN A ND2   1 
ATOM   8922  N  N     . TRP A 1  1174 ? 104.581 116.973 186.578 1.00 57.17  ? 1174 TRP A N     1 
ATOM   8923  C  CA    . TRP A 1  1174 ? 104.557 117.954 185.502 1.00 56.77  ? 1174 TRP A CA    1 
ATOM   8924  C  C     . TRP A 1  1174 ? 103.134 118.444 185.257 1.00 58.16  ? 1174 TRP A C     1 
ATOM   8925  O  O     . TRP A 1  1174 ? 102.168 117.684 185.369 1.00 59.56  ? 1174 TRP A O     1 
ATOM   8926  C  CB    . TRP A 1  1174 ? 105.134 117.369 184.203 1.00 56.83  ? 1174 TRP A CB    1 
ATOM   8927  C  CG    . TRP A 1  1174 ? 106.555 116.894 184.319 1.00 59.59  ? 1174 TRP A CG    1 
ATOM   8928  C  CD1   . TRP A 1  1174 ? 106.985 115.598 184.310 1.00 58.67  ? 1174 TRP A CD1   1 
ATOM   8929  C  CD2   . TRP A 1  1174 ? 107.729 117.701 184.492 1.00 60.30  ? 1174 TRP A CD2   1 
ATOM   8930  N  NE1   . TRP A 1  1174 ? 108.353 115.548 184.445 1.00 59.48  ? 1174 TRP A NE1   1 
ATOM   8931  C  CE2   . TRP A 1  1174 ? 108.831 116.826 184.564 1.00 60.60  ? 1174 TRP A CE2   1 
ATOM   8932  C  CE3   . TRP A 1  1174 ? 107.954 119.076 184.586 1.00 57.70  ? 1174 TRP A CE3   1 
ATOM   8933  C  CZ2   . TRP A 1  1174 ? 110.133 117.282 184.725 1.00 57.49  ? 1174 TRP A CZ2   1 
ATOM   8934  C  CZ3   . TRP A 1  1174 ? 109.249 119.524 184.746 1.00 59.30  ? 1174 TRP A CZ3   1 
ATOM   8935  C  CH2   . TRP A 1  1174 ? 110.322 118.631 184.812 1.00 59.27  ? 1174 TRP A CH2   1 
ATOM   8936  N  N     . CYS A 1  1175 ? 103.016 119.726 184.912 1.00 53.05  ? 1175 CYS A N     1 
ATOM   8937  C  CA    . CYS A 1  1175 ? 101.732 120.372 184.625 1.00 54.13  ? 1175 CYS A CA    1 
ATOM   8938  C  C     . CYS A 1  1175 ? 101.893 121.195 183.347 1.00 53.93  ? 1175 CYS A C     1 
ATOM   8939  O  O     . CYS A 1  1175 ? 102.245 122.375 183.398 1.00 53.00  ? 1175 CYS A O     1 
ATOM   8940  C  CB    . CYS A 1  1175 ? 101.284 121.243 185.801 1.00 55.00  ? 1175 CYS A CB    1 
ATOM   8941  S  SG    . CYS A 1  1175 ? 101.116 120.373 187.379 1.00 58.75  ? 1175 CYS A SG    1 
ATOM   8942  N  N     . ILE A 1  1176 ? 101.621 120.578 182.199 1.00 55.63  ? 1176 ILE A N     1 
ATOM   8943  C  CA    . ILE A 1  1176 ? 101.809 121.234 180.904 1.00 54.53  ? 1176 ILE A CA    1 
ATOM   8944  C  C     . ILE A 1  1176 ? 100.462 121.839 180.516 1.00 54.92  ? 1176 ILE A C     1 
ATOM   8945  O  O     . ILE A 1  1176 ? 99.709  121.279 179.720 1.00 54.54  ? 1176 ILE A O     1 
ATOM   8946  C  CB    . ILE A 1  1176 ? 102.337 120.268 179.849 1.00 53.67  ? 1176 ILE A CB    1 
ATOM   8947  C  CG1   . ILE A 1  1176 ? 103.442 119.390 180.438 1.00 53.61  ? 1176 ILE A CG1   1 
ATOM   8948  C  CG2   . ILE A 1  1176 ? 102.878 121.035 178.657 1.00 54.48  ? 1176 ILE A CG2   1 
ATOM   8949  C  CD1   . ILE A 1  1176 ? 103.774 118.181 179.596 1.00 53.96  ? 1176 ILE A CD1   1 
ATOM   8950  N  N     . ARG A 1  1177 ? 100.165 123.012 181.071 1.00 56.99  ? 1177 ARG A N     1 
ATOM   8951  C  CA    . ARG A 1  1177 ? 98.938  123.727 180.748 1.00 57.54  ? 1177 ARG A CA    1 
ATOM   8952  C  C     . ARG A 1  1177 ? 99.114  124.559 179.487 1.00 56.79  ? 1177 ARG A C     1 
ATOM   8953  O  O     . ARG A 1  1177 ? 100.147 125.206 179.293 1.00 55.83  ? 1177 ARG A O     1 
ATOM   8954  C  CB    . ARG A 1  1177 ? 98.509  124.642 181.896 1.00 56.98  ? 1177 ARG A CB    1 
ATOM   8955  C  CG    . ARG A 1  1177 ? 97.296  125.502 181.553 1.00 56.13  ? 1177 ARG A CG    1 
ATOM   8956  C  CD    . ARG A 1  1177 ? 96.899  126.431 182.677 1.00 56.91  ? 1177 ARG A CD    1 
ATOM   8957  N  NE    . ARG A 1  1177 ? 97.742  127.618 182.774 1.00 58.45  ? 1177 ARG A NE    1 
ATOM   8958  C  CZ    . ARG A 1  1177 ? 97.534  128.751 182.118 1.00 58.93  ? 1177 ARG A CZ    1 
ATOM   8959  N  NH1   . ARG A 1  1177 ? 96.532  128.884 181.265 1.00 56.38  ? 1177 ARG A NH1   1 
ATOM   8960  N  NH2   . ARG A 1  1177 ? 98.357  129.778 182.318 1.00 58.13  ? 1177 ARG A NH2   1 
ATOM   8961  N  N     . LEU A 1  1178 ? 98.093  124.539 178.633 1.00 46.05  ? 1178 LEU A N     1 
ATOM   8962  C  CA    . LEU A 1  1178 ? 98.062  125.315 177.405 1.00 47.51  ? 1178 LEU A CA    1 
ATOM   8963  C  C     . LEU A 1  1178 ? 96.691  125.969 177.267 1.00 47.02  ? 1178 LEU A C     1 
ATOM   8964  O  O     . LEU A 1  1178 ? 95.736  125.605 177.957 1.00 44.30  ? 1178 LEU A O     1 
ATOM   8965  C  CB    . LEU A 1  1178 ? 98.368  124.436 176.182 1.00 47.84  ? 1178 LEU A CB    1 
ATOM   8966  C  CG    . LEU A 1  1178 ? 99.813  124.041 175.850 1.00 50.48  ? 1178 LEU A CG    1 
ATOM   8967  C  CD1   . LEU A 1  1178 ? 100.417 123.086 176.863 1.00 47.23  ? 1178 LEU A CD1   1 
ATOM   8968  C  CD2   . LEU A 1  1178 ? 99.889  123.439 174.458 1.00 50.54  ? 1178 LEU A CD2   1 
ATOM   8969  N  N     . GLU A 1  1179 ? 96.599  126.961 176.381 1.00 49.61  ? 1179 GLU A N     1 
ATOM   8970  C  CA    . GLU A 1  1179 ? 95.313  127.547 176.027 1.00 51.13  ? 1179 GLU A CA    1 
ATOM   8971  C  C     . GLU A 1  1179 ? 95.234  127.630 174.510 1.00 52.77  ? 1179 GLU A C     1 
ATOM   8972  O  O     . GLU A 1  1179 ? 96.252  127.544 173.822 1.00 51.83  ? 1179 GLU A O     1 
ATOM   8973  C  CB    . GLU A 1  1179 ? 95.115  128.935 176.664 1.00 50.92  ? 1179 GLU A CB    1 
ATOM   8974  C  CG    . GLU A 1  1179 ? 96.244  129.933 176.438 1.00 50.36  ? 1179 GLU A CG    1 
ATOM   8975  C  CD    . GLU A 1  1179 ? 96.375  130.341 174.980 1.00 52.68  ? 1179 GLU A CD    1 
ATOM   8976  O  OE1   . GLU A 1  1179 ? 97.496  130.396 174.461 1.00 50.84  ? 1179 GLU A OE1   1 
ATOM   8977  O  OE2   . GLU A 1  1179 ? 95.335  130.630 174.350 1.00 52.04  ? 1179 GLU A OE2   1 
ATOM   8978  N  N     . LEU A 1  1180 ? 94.027  127.815 173.991 1.00 49.36  ? 1180 LEU A N     1 
ATOM   8979  C  CA    . LEU A 1  1180 ? 93.795  127.793 172.553 1.00 49.71  ? 1180 LEU A CA    1 
ATOM   8980  C  C     . LEU A 1  1180 ? 93.354  129.173 172.087 1.00 51.33  ? 1180 LEU A C     1 
ATOM   8981  O  O     . LEU A 1  1180 ? 92.564  129.837 172.766 1.00 54.69  ? 1180 LEU A O     1 
ATOM   8982  C  CB    . LEU A 1  1180 ? 92.740  126.749 172.182 1.00 49.05  ? 1180 LEU A CB    1 
ATOM   8983  C  CG    . LEU A 1  1180 ? 92.835  125.357 172.813 1.00 49.83  ? 1180 LEU A CG    1 
ATOM   8984  C  CD1   . LEU A 1  1180 ? 91.839  124.430 172.147 1.00 48.45  ? 1180 LEU A CD1   1 
ATOM   8985  C  CD2   . LEU A 1  1180 ? 94.238  124.782 172.749 1.00 48.90  ? 1180 LEU A CD2   1 
ATOM   8986  N  N     . ASN A 1  1181 ? 93.874  129.607 170.943 1.00 50.03  ? 1181 ASN A N     1 
ATOM   8987  C  CA    . ASN A 1  1181 ? 93.288  130.749 170.258 1.00 48.83  ? 1181 ASN A CA    1 
ATOM   8988  C  C     . ASN A 1  1181 ? 91.925  130.362 169.702 1.00 46.55  ? 1181 ASN A C     1 
ATOM   8989  O  O     . ASN A 1  1181 ? 91.810  129.420 168.916 1.00 45.93  ? 1181 ASN A O     1 
ATOM   8990  C  CB    . ASN A 1  1181 ? 94.207  131.221 169.129 1.00 48.28  ? 1181 ASN A CB    1 
ATOM   8991  C  CG    . ASN A 1  1181 ? 93.696  132.474 168.443 1.00 50.75  ? 1181 ASN A CG    1 
ATOM   8992  O  OD1   . ASN A 1  1181 ? 92.714  133.077 168.872 1.00 49.78  ? 1181 ASN A OD1   1 
ATOM   8993  N  ND2   . ASN A 1  1181 ? 94.364  132.871 167.367 1.00 48.08  ? 1181 ASN A ND2   1 
ATOM   8994  N  N     . LYS A 1  1182 ? 90.894  131.106 170.091 1.00 48.81  ? 1182 LYS A N     1 
ATOM   8995  C  CA    . LYS A 1  1182 ? 89.541  130.751 169.691 1.00 50.87  ? 1182 LYS A CA    1 
ATOM   8996  C  C     . LYS A 1  1182 ? 89.209  131.184 168.271 1.00 49.78  ? 1182 LYS A C     1 
ATOM   8997  O  O     . LYS A 1  1182 ? 88.240  130.679 167.694 1.00 47.49  ? 1182 LYS A O     1 
ATOM   8998  C  CB    . LYS A 1  1182 ? 88.522  131.356 170.662 1.00 49.10  ? 1182 LYS A CB    1 
ATOM   8999  C  CG    . LYS A 1  1182 ? 87.170  130.655 170.656 1.00 49.14  ? 1182 LYS A CG    1 
ATOM   9000  C  CD    . LYS A 1  1182 ? 86.416  130.899 171.952 1.00 51.90  ? 1182 LYS A CD    1 
ATOM   9001  C  CE    . LYS A 1  1182 ? 85.988  132.351 172.057 1.00 49.49  ? 1182 LYS A CE    1 
ATOM   9002  N  NZ    . LYS A 1  1182 ? 85.088  132.576 173.212 1.00 50.11  ? 1182 LYS A NZ    1 
ATOM   9003  N  N     . THR A 1  1183 ? 89.998  132.087 167.689 1.00 43.14  ? 1183 THR A N     1 
ATOM   9004  C  CA    . THR A 1  1183 ? 89.748  132.505 166.314 1.00 47.82  ? 1183 THR A CA    1 
ATOM   9005  C  C     . THR A 1  1183 ? 90.107  131.394 165.336 1.00 48.66  ? 1183 THR A C     1 
ATOM   9006  O  O     . THR A 1  1183 ? 89.601  131.352 164.208 1.00 47.37  ? 1183 THR A O     1 
ATOM   9007  C  CB    . THR A 1  1183 ? 90.546  133.770 165.997 1.00 48.96  ? 1183 THR A CB    1 
ATOM   9008  O  OG1   . THR A 1  1183 ? 91.945  133.495 166.128 1.00 46.71  ? 1183 THR A OG1   1 
ATOM   9009  C  CG2   . THR A 1  1183 ? 90.172  134.883 166.954 1.00 44.81  ? 1183 THR A CG2   1 
ATOM   9010  N  N     . THR A 1  1184 ? 90.992  130.487 165.754 1.00 48.80  ? 1184 THR A N     1 
ATOM   9011  C  CA    . THR A 1  1184 ? 91.475  129.447 164.854 1.00 47.78  ? 1184 THR A CA    1 
ATOM   9012  C  C     . THR A 1  1184 ? 90.374  128.463 164.479 1.00 46.44  ? 1184 THR A C     1 
ATOM   9013  O  O     . THR A 1  1184 ? 90.147  128.212 163.290 1.00 45.60  ? 1184 THR A O     1 
ATOM   9014  C  CB    . THR A 1  1184 ? 92.651  128.713 165.495 1.00 47.15  ? 1184 THR A CB    1 
ATOM   9015  O  OG1   . THR A 1  1184 ? 92.274  128.254 166.800 1.00 44.76  ? 1184 THR A OG1   1 
ATOM   9016  C  CG2   . THR A 1  1184 ? 93.860  129.636 165.608 1.00 45.31  ? 1184 THR A CG2   1 
ATOM   9017  N  N     . MET A 1  1185 ? 89.671  127.900 165.468 1.00 47.24  ? 1185 MET A N     1 
ATOM   9018  C  CA    . MET A 1  1185 ? 88.701  126.853 165.155 1.00 50.25  ? 1185 MET A CA    1 
ATOM   9019  C  C     . MET A 1  1185 ? 87.524  127.388 164.352 1.00 51.79  ? 1185 MET A C     1 
ATOM   9020  O  O     . MET A 1  1185 ? 87.049  126.721 163.427 1.00 50.16  ? 1185 MET A O     1 
ATOM   9021  C  CB    . MET A 1  1185 ? 88.214  126.144 166.419 1.00 48.19  ? 1185 MET A CB    1 
ATOM   9022  C  CG    . MET A 1  1185 ? 89.320  125.594 167.295 1.00 49.12  ? 1185 MET A CG    1 
ATOM   9023  S  SD    . MET A 1  1185 ? 90.423  126.821 167.972 1.00 55.09  ? 1185 MET A SD    1 
ATOM   9024  C  CE    . MET A 1  1185 ? 89.415  127.323 169.359 1.00 49.90  ? 1185 MET A CE    1 
ATOM   9025  N  N     . ILE A 1  1186 ? 87.035  128.584 164.685 1.00 45.63  ? 1186 ILE A N     1 
ATOM   9026  C  CA    . ILE A 1  1186 ? 85.965  129.164 163.880 1.00 45.77  ? 1186 ILE A CA    1 
ATOM   9027  C  C     . ILE A 1  1186 ? 86.440  129.380 162.451 1.00 43.89  ? 1186 ILE A C     1 
ATOM   9028  O  O     . ILE A 1  1186 ? 85.659  129.253 161.499 1.00 42.35  ? 1186 ILE A O     1 
ATOM   9029  C  CB    . ILE A 1  1186 ? 85.460  130.475 164.509 1.00 44.48  ? 1186 ILE A CB    1 
ATOM   9030  C  CG1   . ILE A 1  1186 ? 85.200  130.289 166.003 1.00 45.57  ? 1186 ILE A CG1   1 
ATOM   9031  C  CG2   . ILE A 1  1186 ? 84.189  130.942 163.815 1.00 42.78  ? 1186 ILE A CG2   1 
ATOM   9032  C  CD1   . ILE A 1  1186 ? 84.173  129.214 166.316 1.00 45.67  ? 1186 ILE A CD1   1 
ATOM   9033  N  N     . LEU A 1  1187 ? 87.725  129.692 162.276 1.00 42.94  ? 1187 LEU A N     1 
ATOM   9034  C  CA    . LEU A 1  1187 ? 88.276  129.890 160.939 1.00 44.53  ? 1187 LEU A CA    1 
ATOM   9035  C  C     . LEU A 1  1187 ? 88.348  128.577 160.167 1.00 44.92  ? 1187 LEU A C     1 
ATOM   9036  O  O     . LEU A 1  1187 ? 88.104  128.541 158.956 1.00 43.57  ? 1187 LEU A O     1 
ATOM   9037  C  CB    . LEU A 1  1187 ? 89.654  130.542 161.045 1.00 43.79  ? 1187 LEU A CB    1 
ATOM   9038  C  CG    . LEU A 1  1187 ? 90.389  130.901 159.756 1.00 47.40  ? 1187 LEU A CG    1 
ATOM   9039  C  CD1   . LEU A 1  1187 ? 89.597  131.909 158.936 1.00 42.59  ? 1187 LEU A CD1   1 
ATOM   9040  C  CD2   . LEU A 1  1187 ? 91.753  131.464 160.110 1.00 45.51  ? 1187 LEU A CD2   1 
ATOM   9041  N  N     . LYS A 1  1188 ? 88.667  127.479 160.856 1.00 49.21  ? 1188 LYS A N     1 
ATOM   9042  C  CA    . LYS A 1  1188 ? 88.866  126.188 160.209 1.00 49.39  ? 1188 LYS A CA    1 
ATOM   9043  C  C     . LYS A 1  1188 ? 87.833  125.144 160.624 1.00 47.77  ? 1188 LYS A C     1 
ATOM   9044  O  O     . LYS A 1  1188 ? 88.028  123.953 160.364 1.00 46.78  ? 1188 LYS A O     1 
ATOM   9045  C  CB    . LYS A 1  1188 ? 90.281  125.680 160.485 1.00 47.08  ? 1188 LYS A CB    1 
ATOM   9046  C  CG    . LYS A 1  1188 ? 91.331  126.321 159.596 1.00 46.59  ? 1188 LYS A CG    1 
ATOM   9047  C  CD    . LYS A 1  1188 ? 92.732  125.952 160.025 1.00 47.46  ? 1188 LYS A CD    1 
ATOM   9048  C  CE    . LYS A 1  1188 ? 93.215  126.871 161.124 1.00 48.15  ? 1188 LYS A CE    1 
ATOM   9049  N  NZ    . LYS A 1  1188 ? 93.536  128.224 160.596 1.00 49.20  ? 1188 LYS A NZ    1 
ATOM   9050  N  N     . SER A 1  1189 ? 86.737  125.567 161.257 1.00 43.81  ? 1189 SER A N     1 
ATOM   9051  C  CA    . SER A 1  1189 ? 85.626  124.677 161.607 1.00 46.17  ? 1189 SER A CA    1 
ATOM   9052  C  C     . SER A 1  1189 ? 86.093  123.503 162.466 1.00 46.77  ? 1189 SER A C     1 
ATOM   9053  O  O     . SER A 1  1189 ? 85.612  122.377 162.328 1.00 44.14  ? 1189 SER A O     1 
ATOM   9054  C  CB    . SER A 1  1189 ? 84.897  124.181 160.356 1.00 45.82  ? 1189 SER A CB    1 
ATOM   9055  O  OG    . SER A 1  1189 ? 83.731  123.450 160.701 1.00 46.34  ? 1189 SER A OG    1 
ATOM   9056  N  N     . ILE A 1  1190 ? 87.041  123.770 163.366 1.00 45.63  ? 1190 ILE A N     1 
ATOM   9057  C  CA    . ILE A 1  1190 ? 87.491  122.736 164.285 1.00 45.65  ? 1190 ILE A CA    1 
ATOM   9058  C  C     . ILE A 1  1190 ? 86.540  122.652 165.475 1.00 47.76  ? 1190 ILE A C     1 
ATOM   9059  O  O     . ILE A 1  1190 ? 85.883  123.627 165.861 1.00 48.27  ? 1190 ILE A O     1 
ATOM   9060  C  CB    . ILE A 1  1190 ? 88.933  122.999 164.748 1.00 44.43  ? 1190 ILE A CB    1 
ATOM   9061  C  CG1   . ILE A 1  1190 ? 89.764  123.612 163.618 1.00 46.38  ? 1190 ILE A CG1   1 
ATOM   9062  C  CG2   . ILE A 1  1190 ? 89.578  121.707 165.237 1.00 44.61  ? 1190 ILE A CG2   1 
ATOM   9063  C  CD1   . ILE A 1  1190 ? 90.178  122.629 162.546 1.00 45.04  ? 1190 ILE A CD1   1 
ATOM   9064  N  N     . SER A 1  1191 ? 86.457  121.459 166.057 1.00 47.95  ? 1191 SER A N     1 
ATOM   9065  C  CA    . SER A 1  1191 ? 85.693  121.224 167.272 1.00 45.62  ? 1191 SER A CA    1 
ATOM   9066  C  C     . SER A 1  1191 ? 86.614  120.718 168.375 1.00 47.58  ? 1191 SER A C     1 
ATOM   9067  O  O     . SER A 1  1191 ? 87.542  119.942 168.122 1.00 46.54  ? 1191 SER A O     1 
ATOM   9068  C  CB    . SER A 1  1191 ? 84.569  120.216 167.034 1.00 44.49  ? 1191 SER A CB    1 
ATOM   9069  O  OG    . SER A 1  1191 ? 83.935  119.873 168.252 1.00 46.90  ? 1191 SER A OG    1 
ATOM   9070  N  N     . LEU A 1  1192 ? 86.353  121.172 169.606 1.00 46.34  ? 1192 LEU A N     1 
ATOM   9071  C  CA    . LEU A 1  1192 ? 87.150  120.728 170.748 1.00 46.89  ? 1192 LEU A CA    1 
ATOM   9072  C  C     . LEU A 1  1192 ? 87.066  119.220 170.941 1.00 47.04  ? 1192 LEU A C     1 
ATOM   9073  O  O     . LEU A 1  1192 ? 87.965  118.620 171.540 1.00 45.50  ? 1192 LEU A O     1 
ATOM   9074  C  CB    . LEU A 1  1192 ? 86.697  121.445 172.017 1.00 46.17  ? 1192 LEU A CB    1 
ATOM   9075  C  CG    . LEU A 1  1192 ? 87.541  121.215 173.274 1.00 46.10  ? 1192 LEU A CG    1 
ATOM   9076  C  CD1   . LEU A 1  1192 ? 88.972  121.679 173.059 1.00 44.57  ? 1192 LEU A CD1   1 
ATOM   9077  C  CD2   . LEU A 1  1192 ? 86.920  121.911 174.459 1.00 45.75  ? 1192 LEU A CD2   1 
ATOM   9078  N  N     . GLU A 1  1193 ? 85.989  118.597 170.461 1.00 48.20  ? 1193 GLU A N     1 
ATOM   9079  C  CA    . GLU A 1  1193 ? 85.918  117.142 170.444 1.00 48.25  ? 1193 GLU A CA    1 
ATOM   9080  C  C     . GLU A 1  1193 ? 87.006  116.547 169.564 1.00 48.27  ? 1193 GLU A C     1 
ATOM   9081  O  O     . GLU A 1  1193 ? 87.629  115.544 169.927 1.00 46.58  ? 1193 GLU A O     1 
ATOM   9082  C  CB    . GLU A 1  1193 ? 84.542  116.693 169.957 1.00 46.41  ? 1193 GLU A CB    1 
ATOM   9083  C  CG    . GLU A 1  1193 ? 83.459  116.712 171.007 1.00 46.41  ? 1193 GLU A CG    1 
ATOM   9084  C  CD    . GLU A 1  1193 ? 83.470  115.452 171.848 1.00 50.16  ? 1193 GLU A CD    1 
ATOM   9085  O  OE1   . GLU A 1  1193 ? 83.728  114.368 171.281 1.00 49.50  ? 1193 GLU A OE1   1 
ATOM   9086  O  OE2   . GLU A 1  1193 ? 83.214  115.537 173.066 1.00 51.25  ? 1193 GLU A OE2   1 
ATOM   9087  N  N     . SER A 1  1194 ? 87.248  117.152 168.399 1.00 46.12  ? 1194 SER A N     1 
ATOM   9088  C  CA    . SER A 1  1194 ? 88.201  116.573 167.460 1.00 46.75  ? 1194 SER A CA    1 
ATOM   9089  C  C     . SER A 1  1194 ? 89.596  116.530 168.059 1.00 45.52  ? 1194 SER A C     1 
ATOM   9090  O  O     . SER A 1  1194 ? 90.310  115.531 167.916 1.00 46.46  ? 1194 SER A O     1 
ATOM   9091  C  CB    . SER A 1  1194 ? 88.202  117.367 166.156 1.00 44.81  ? 1194 SER A CB    1 
ATOM   9092  O  OG    . SER A 1  1194 ? 86.922  117.341 165.554 1.00 46.15  ? 1194 SER A OG    1 
ATOM   9093  N  N     . ILE A 1  1195 ? 89.997  117.599 168.744 1.00 42.42  ? 1195 ILE A N     1 
ATOM   9094  C  CA    . ILE A 1  1195 ? 91.341  117.646 169.302 1.00 42.32  ? 1195 ILE A CA    1 
ATOM   9095  C  C     . ILE A 1  1195 ? 91.524  116.568 170.357 1.00 43.59  ? 1195 ILE A C     1 
ATOM   9096  O  O     . ILE A 1  1195 ? 92.447  115.752 170.270 1.00 42.55  ? 1195 ILE A O     1 
ATOM   9097  C  CB    . ILE A 1  1195 ? 91.633  119.047 169.861 1.00 42.80  ? 1195 ILE A CB    1 
ATOM   9098  C  CG1   . ILE A 1  1195 ? 90.901  120.105 169.037 1.00 42.29  ? 1195 ILE A CG1   1 
ATOM   9099  C  CG2   . ILE A 1  1195 ? 93.123  119.308 169.887 1.00 41.98  ? 1195 ILE A CG2   1 
ATOM   9100  C  CD1   . ILE A 1  1195 ? 91.222  121.521 169.458 1.00 41.40  ? 1195 ILE A CD1   1 
ATOM   9101  N  N     . ILE A 1  1196 ? 90.613  116.500 171.328 1.00 44.78  ? 1196 ILE A N     1 
ATOM   9102  C  CA    . ILE A 1  1196 ? 90.796  115.595 172.459 1.00 44.88  ? 1196 ILE A CA    1 
ATOM   9103  C  C     . ILE A 1  1196 ? 90.810  114.148 171.988 1.00 45.90  ? 1196 ILE A C     1 
ATOM   9104  O  O     . ILE A 1  1196 ? 91.607  113.330 172.462 1.00 45.80  ? 1196 ILE A O     1 
ATOM   9105  C  CB    . ILE A 1  1196 ? 89.713  115.843 173.522 1.00 44.30  ? 1196 ILE A CB    1 
ATOM   9106  C  CG1   . ILE A 1  1196 ? 89.768  117.297 173.972 1.00 44.24  ? 1196 ILE A CG1   1 
ATOM   9107  C  CG2   . ILE A 1  1196 ? 89.917  114.931 174.716 1.00 45.30  ? 1196 ILE A CG2   1 
ATOM   9108  C  CD1   . ILE A 1  1196 ? 91.148  117.731 174.404 1.00 43.53  ? 1196 ILE A CD1   1 
ATOM   9109  N  N     . ASN A 1  1197 ? 89.935  113.812 171.043 1.00 49.26  ? 1197 ASN A N     1 
ATOM   9110  C  CA    . ASN A 1  1197 ? 89.976  112.480 170.456 1.00 49.17  ? 1197 ASN A CA    1 
ATOM   9111  C  C     . ASN A 1  1197 ? 91.278  112.250 169.704 1.00 49.91  ? 1197 ASN A C     1 
ATOM   9112  O  O     . ASN A 1  1197 ? 91.785  111.123 169.673 1.00 50.91  ? 1197 ASN A O     1 
ATOM   9113  C  CB    . ASN A 1  1197 ? 88.784  112.285 169.524 1.00 48.54  ? 1197 ASN A CB    1 
ATOM   9114  C  CG    . ASN A 1  1197 ? 87.465  112.516 170.219 1.00 48.80  ? 1197 ASN A CG    1 
ATOM   9115  O  OD1   . ASN A 1  1197 ? 87.283  112.137 171.375 1.00 47.79  ? 1197 ASN A OD1   1 
ATOM   9116  N  ND2   . ASN A 1  1197 ? 86.533  113.148 169.519 1.00 46.14  ? 1197 ASN A ND2   1 
ATOM   9117  N  N     . SER A 1  1198 ? 91.844  113.306 169.112 1.00 44.57  ? 1198 SER A N     1 
ATOM   9118  C  CA    . SER A 1  1198 ? 93.072  113.148 168.339 1.00 45.23  ? 1198 SER A CA    1 
ATOM   9119  C  C     . SER A 1  1198 ? 94.261  112.792 169.224 1.00 45.43  ? 1198 SER A C     1 
ATOM   9120  O  O     . SER A 1  1198 ? 94.973  111.822 168.940 1.00 45.67  ? 1198 SER A O     1 
ATOM   9121  C  CB    . SER A 1  1198 ? 93.369  114.422 167.546 1.00 44.78  ? 1198 SER A CB    1 
ATOM   9122  O  OG    . SER A 1  1198 ? 92.359  114.687 166.588 1.00 47.22  ? 1198 SER A OG    1 
ATOM   9123  N  N     . LEU A 1  1199 ? 94.495  113.553 170.303 1.00 43.77  ? 1199 LEU A N     1 
ATOM   9124  C  CA    . LEU A 1  1199 ? 95.746  113.377 171.040 1.00 46.91  ? 1199 LEU A CA    1 
ATOM   9125  C  C     . LEU A 1  1199 ? 95.823  112.023 171.728 1.00 47.85  ? 1199 LEU A C     1 
ATOM   9126  O  O     . LEU A 1  1199 ? 96.902  111.423 171.779 1.00 44.86  ? 1199 LEU A O     1 
ATOM   9127  C  CB    . LEU A 1  1199 ? 95.972  114.487 172.073 1.00 45.29  ? 1199 LEU A CB    1 
ATOM   9128  C  CG    . LEU A 1  1199 ? 95.704  115.971 171.806 1.00 46.35  ? 1199 LEU A CG    1 
ATOM   9129  C  CD1   . LEU A 1  1199 ? 94.374  116.406 172.382 1.00 45.31  ? 1199 LEU A CD1   1 
ATOM   9130  C  CD2   . LEU A 1  1199 ? 96.833  116.842 172.327 1.00 42.62  ? 1199 LEU A CD2   1 
ATOM   9131  N  N     . ARG A 1  1200 ? 94.709  111.523 172.260 1.00 55.05  ? 1200 ARG A N     1 
ATOM   9132  C  CA    . ARG A 1  1200 ? 94.718  110.273 173.010 1.00 56.71  ? 1200 ARG A CA    1 
ATOM   9133  C  C     . ARG A 1  1200 ? 94.383  109.066 172.136 1.00 56.80  ? 1200 ARG A C     1 
ATOM   9134  O  O     . ARG A 1  1200 ? 94.194  107.960 172.644 1.00 58.54  ? 1200 ARG A O     1 
ATOM   9135  C  CB    . ARG A 1  1200 ? 93.780  110.357 174.211 1.00 53.88  ? 1200 ARG A CB    1 
ATOM   9136  C  CG    . ARG A 1  1200 ? 94.359  111.182 175.353 1.00 55.36  ? 1200 ARG A CG    1 
ATOM   9137  C  CD    . ARG A 1  1200 ? 93.906  110.663 176.709 1.00 58.23  ? 1200 ARG A CD    1 
ATOM   9138  N  NE    . ARG A 1  1200 ? 94.876  109.736 177.284 1.00 60.63  ? 1200 ARG A NE    1 
ATOM   9139  C  CZ    . ARG A 1  1200 ? 94.742  108.416 177.292 1.00 59.29  ? 1200 ARG A CZ    1 
ATOM   9140  N  NH1   . ARG A 1  1200 ? 93.686  107.824 176.758 1.00 57.29  ? 1200 ARG A NH1   1 
ATOM   9141  N  NH2   . ARG A 1  1200 ? 95.696  107.671 177.843 1.00 55.57  ? 1200 ARG A NH2   1 
ATOM   9142  N  N     . ALA A 1  1201 ? 94.320  109.258 170.821 1.00 43.75  ? 1201 ALA A N     1 
ATOM   9143  C  CA    . ALA A 1  1201 ? 94.329  108.147 169.883 1.00 44.62  ? 1201 ALA A CA    1 
ATOM   9144  C  C     . ALA A 1  1201 ? 95.720  107.889 169.327 1.00 46.99  ? 1201 ALA A C     1 
ATOM   9145  O  O     . ALA A 1  1201 ? 95.892  106.977 168.509 1.00 44.42  ? 1201 ALA A O     1 
ATOM   9146  C  CB    . ALA A 1  1201 ? 93.347  108.399 168.733 1.00 42.01  ? 1201 ALA A CB    1 
ATOM   9147  N  N     . LYS A 1  1202 ? 96.714  108.671 169.749 1.00 52.03  ? 1202 LYS A N     1 
ATOM   9148  C  CA    . LYS A 1  1202 ? 98.100  108.491 169.340 1.00 51.47  ? 1202 LYS A CA    1 
ATOM   9149  C  C     . LYS A 1  1202 ? 99.089  108.501 170.495 1.00 52.06  ? 1202 LYS A C     1 
ATOM   9150  O  O     . LYS A 1  1202 ? 100.227 108.058 170.305 1.00 51.51  ? 1202 LYS A O     1 
ATOM   9151  C  CB    . LYS A 1  1202 ? 98.511  109.579 168.335 1.00 47.34  ? 1202 LYS A CB    1 
ATOM   9152  C  CG    . LYS A 1  1202 ? 98.690  109.075 166.919 1.00 48.44  ? 1202 LYS A CG    1 
ATOM   9153  C  CD    . LYS A 1  1202 ? 99.217  110.160 165.982 1.00 52.69  ? 1202 LYS A CD    1 
ATOM   9154  C  CE    . LYS A 1  1202 ? 98.425  111.449 166.105 1.00 51.62  ? 1202 LYS A CE    1 
ATOM   9155  N  NZ    . LYS A 1  1202 ? 99.005  112.543 165.287 1.00 48.62  ? 1202 LYS A NZ    1 
ATOM   9156  N  N     . HIS A 1  1203 ? 98.705  108.989 171.672 1.00 54.53  ? 1203 HIS A N     1 
ATOM   9157  C  CA    . HIS A 1  1203 ? 99.617  109.186 172.797 1.00 54.02  ? 1203 HIS A CA    1 
ATOM   9158  C  C     . HIS A 1  1203 ? 98.998  108.584 174.051 1.00 56.67  ? 1203 HIS A C     1 
ATOM   9159  O  O     . HIS A 1  1203 ? 98.418  109.300 174.879 1.00 54.02  ? 1203 HIS A O     1 
ATOM   9160  C  CB    . HIS A 1  1203 ? 99.930  110.671 172.978 1.00 52.56  ? 1203 HIS A CB    1 
ATOM   9161  C  CG    . HIS A 1  1203 ? 100.576 111.294 171.782 1.00 55.46  ? 1203 HIS A CG    1 
ATOM   9162  N  ND1   . HIS A 1  1203 ? 101.926 111.185 171.525 1.00 57.29  ? 1203 HIS A ND1   1 
ATOM   9163  C  CD2   . HIS A 1  1203 ? 100.055 112.009 170.758 1.00 55.68  ? 1203 HIS A CD2   1 
ATOM   9164  C  CE1   . HIS A 1  1203 ? 102.211 111.822 170.403 1.00 56.46  ? 1203 HIS A CE1   1 
ATOM   9165  N  NE2   . HIS A 1  1203 ? 101.093 112.330 169.917 1.00 58.19  ? 1203 HIS A NE2   1 
ATOM   9166  N  N     . PRO A 1  1204 ? 99.106  107.255 174.230 1.00 57.53  ? 1204 PRO A N     1 
ATOM   9167  C  CA    . PRO A 1  1204 ? 98.467  106.569 175.361 1.00 54.63  ? 1204 PRO A CA    1 
ATOM   9168  C  C     . PRO A 1  1204 ? 99.286  106.649 176.648 1.00 54.07  ? 1204 PRO A C     1 
ATOM   9169  O  O     . PRO A 1  1204 ? 99.477  105.655 177.351 1.00 52.31  ? 1204 PRO A O     1 
ATOM   9170  C  CB    . PRO A 1  1204 ? 98.332  105.132 174.851 1.00 52.49  ? 1204 PRO A CB    1 
ATOM   9171  C  CG    . PRO A 1  1204 ? 99.471  104.965 173.881 1.00 53.11  ? 1204 PRO A CG    1 
ATOM   9172  C  CD    . PRO A 1  1204 ? 99.889  106.330 173.392 1.00 52.43  ? 1204 PRO A CD    1 
ATOM   9173  N  N     . ASN A 1  1205 ? 99.778  107.848 176.954 1.00 51.61  ? 1205 ASN A N     1 
ATOM   9174  C  CA    . ASN A 1  1205 ? 100.573 108.101 178.148 1.00 51.16  ? 1205 ASN A CA    1 
ATOM   9175  C  C     . ASN A 1  1205 ? 100.164 109.393 178.841 1.00 52.35  ? 1205 ASN A C     1 
ATOM   9176  O  O     . ASN A 1  1205 ? 100.886 109.864 179.727 1.00 50.67  ? 1205 ASN A O     1 
ATOM   9177  C  CB    . ASN A 1  1205 ? 102.064 108.154 177.798 1.00 50.96  ? 1205 ASN A CB    1 
ATOM   9178  C  CG    . ASN A 1  1205 ? 102.631 106.797 177.444 1.00 52.25  ? 1205 ASN A CG    1 
ATOM   9179  O  OD1   . ASN A 1  1205 ? 103.316 106.169 178.249 1.00 53.87  ? 1205 ASN A OD1   1 
ATOM   9180  N  ND2   . ASN A 1  1205 ? 102.358 106.340 176.229 1.00 49.02  ? 1205 ASN A ND2   1 
ATOM   9181  N  N     . THR A 1  1206 ? 99.036  109.986 178.456 1.00 55.34  ? 1206 THR A N     1 
ATOM   9182  C  CA    . THR A 1  1206 ? 98.612  111.263 179.007 1.00 57.37  ? 1206 THR A CA    1 
ATOM   9183  C  C     . THR A 1  1206 ? 97.137  111.208 179.372 1.00 56.75  ? 1206 THR A C     1 
ATOM   9184  O  O     . THR A 1  1206 ? 96.355  110.458 178.784 1.00 57.75  ? 1206 THR A O     1 
ATOM   9185  C  CB    . THR A 1  1206 ? 98.844  112.425 178.025 1.00 56.01  ? 1206 THR A CB    1 
ATOM   9186  O  OG1   . THR A 1  1206 ? 98.280  112.098 176.749 1.00 56.63  ? 1206 THR A OG1   1 
ATOM   9187  C  CG2   . THR A 1  1206 ? 100.332 112.723 177.868 1.00 54.01  ? 1206 THR A CG2   1 
ATOM   9188  N  N     . TYR A 1  1207 ? 96.771  112.013 180.368 1.00 55.80  ? 1207 TYR A N     1 
ATOM   9189  C  CA    . TYR A 1  1207 ? 95.382  112.336 180.658 1.00 57.27  ? 1207 TYR A CA    1 
ATOM   9190  C  C     . TYR A 1  1207 ? 95.215  113.836 180.481 1.00 57.61  ? 1207 TYR A C     1 
ATOM   9191  O  O     . TYR A 1  1207 ? 96.016  114.617 181.002 1.00 56.94  ? 1207 TYR A O     1 
ATOM   9192  C  CB    . TYR A 1  1207 ? 94.980  111.882 182.058 1.00 59.90  ? 1207 TYR A CB    1 
ATOM   9193  C  CG    . TYR A 1  1207 ? 93.512  112.075 182.355 1.00 60.78  ? 1207 TYR A CG    1 
ATOM   9194  C  CD1   . TYR A 1  1207 ? 92.538  111.631 181.468 1.00 59.10  ? 1207 TYR A CD1   1 
ATOM   9195  C  CD2   . TYR A 1  1207 ? 93.098  112.656 183.545 1.00 56.39  ? 1207 TYR A CD2   1 
ATOM   9196  C  CE1   . TYR A 1  1207 ? 91.189  111.805 181.743 1.00 60.47  ? 1207 TYR A CE1   1 
ATOM   9197  C  CE2   . TYR A 1  1207 ? 91.757  112.821 183.832 1.00 56.48  ? 1207 TYR A CE2   1 
ATOM   9198  C  CZ    . TYR A 1  1207 ? 90.808  112.398 182.931 1.00 59.18  ? 1207 TYR A CZ    1 
ATOM   9199  O  OH    . TYR A 1  1207 ? 89.475  112.571 183.222 1.00 55.64  ? 1207 TYR A OH    1 
ATOM   9200  N  N     . ILE A 1  1208 ? 94.180  114.234 179.746 1.00 50.87  ? 1208 ILE A N     1 
ATOM   9201  C  CA    . ILE A 1  1208 ? 94.233  115.504 179.029 1.00 51.48  ? 1208 ILE A CA    1 
ATOM   9202  C  C     . ILE A 1  1208 ? 93.673  116.660 179.853 1.00 51.12  ? 1208 ILE A C     1 
ATOM   9203  O  O     . ILE A 1  1208 ? 94.183  117.778 179.762 1.00 51.04  ? 1208 ILE A O     1 
ATOM   9204  C  CB    . ILE A 1  1208 ? 93.517  115.363 177.666 1.00 50.49  ? 1208 ILE A CB    1 
ATOM   9205  C  CG1   . ILE A 1  1208 ? 94.234  116.184 176.600 1.00 50.78  ? 1208 ILE A CG1   1 
ATOM   9206  C  CG2   . ILE A 1  1208 ? 92.075  115.796 177.739 1.00 48.29  ? 1208 ILE A CG2   1 
ATOM   9207  C  CD1   . ILE A 1  1208 ? 95.689  115.802 176.438 1.00 46.95  ? 1208 ILE A CD1   1 
ATOM   9208  N  N     . MET A 1  1209 ? 92.643  116.432 180.677 1.00 50.72  ? 1209 MET A N     1 
ATOM   9209  C  CA    . MET A 1  1209 ? 91.945  117.501 181.399 1.00 50.29  ? 1209 MET A CA    1 
ATOM   9210  C  C     . MET A 1  1209 ? 91.364  118.527 180.418 1.00 49.75  ? 1209 MET A C     1 
ATOM   9211  O  O     . MET A 1  1209 ? 91.783  119.684 180.370 1.00 49.36  ? 1209 MET A O     1 
ATOM   9212  C  CB    . MET A 1  1209 ? 92.881  118.213 182.391 1.00 48.55  ? 1209 MET A CB    1 
ATOM   9213  C  CG    . MET A 1  1209 ? 93.308  117.480 183.671 1.00 51.22  ? 1209 MET A CG    1 
ATOM   9214  S  SD    . MET A 1  1209 ? 92.457  115.997 184.249 1.00 60.69  ? 1209 MET A SD    1 
ATOM   9215  C  CE    . MET A 1  1209 ? 90.767  116.540 184.444 1.00 48.11  ? 1209 MET A CE    1 
ATOM   9216  N  N     . HIS A 1  1210 ? 90.388  118.082 179.622 1.00 52.79  ? 1210 HIS A N     1 
ATOM   9217  C  CA    . HIS A 1  1210 ? 90.009  118.892 178.466 1.00 52.82  ? 1210 HIS A CA    1 
ATOM   9218  C  C     . HIS A 1  1210 ? 89.092  120.060 178.810 1.00 53.32  ? 1210 HIS A C     1 
ATOM   9219  O  O     . HIS A 1  1210 ? 88.829  120.889 177.933 1.00 52.96  ? 1210 HIS A O     1 
ATOM   9220  C  CB    . HIS A 1  1210 ? 89.380  118.036 177.360 1.00 51.95  ? 1210 HIS A CB    1 
ATOM   9221  C  CG    . HIS A 1  1210 ? 88.001  117.534 177.650 1.00 53.90  ? 1210 HIS A CG    1 
ATOM   9222  N  ND1   . HIS A 1  1210 ? 86.894  118.355 177.655 1.00 53.56  ? 1210 HIS A ND1   1 
ATOM   9223  C  CD2   . HIS A 1  1210 ? 87.539  116.280 177.867 1.00 53.16  ? 1210 HIS A CD2   1 
ATOM   9224  C  CE1   . HIS A 1  1210 ? 85.816  117.635 177.908 1.00 53.17  ? 1210 HIS A CE1   1 
ATOM   9225  N  NE2   . HIS A 1  1210 ? 86.180  116.372 178.038 1.00 54.90  ? 1210 HIS A NE2   1 
ATOM   9226  N  N     . SER A 1  1211 ? 88.594  120.143 180.039 1.00 49.63  ? 1211 SER A N     1 
ATOM   9227  C  CA    . SER A 1  1211 ? 87.846  121.322 180.502 1.00 49.04  ? 1211 SER A CA    1 
ATOM   9228  C  C     . SER A 1  1211 ? 86.625  121.534 179.605 1.00 48.18  ? 1211 SER A C     1 
ATOM   9229  O  O     . SER A 1  1211 ? 86.110  120.583 179.003 1.00 50.45  ? 1211 SER A O     1 
ATOM   9230  C  CB    . SER A 1  1211 ? 88.777  122.516 180.575 1.00 47.05  ? 1211 SER A CB    1 
ATOM   9231  O  OG    . SER A 1  1211 ? 88.046  123.703 180.826 1.00 47.05  ? 1211 SER A OG    1 
ATOM   9232  N  N     . VAL A 1  1212 ? 86.162  122.778 179.496 1.00 43.05  ? 1212 VAL A N     1 
ATOM   9233  C  CA    . VAL A 1  1212 ? 85.041  123.108 178.621 1.00 46.75  ? 1212 VAL A CA    1 
ATOM   9234  C  C     . VAL A 1  1212 ? 85.311  124.383 177.835 1.00 45.64  ? 1212 VAL A C     1 
ATOM   9235  O  O     . VAL A 1  1212 ? 84.490  124.801 177.018 1.00 45.32  ? 1212 VAL A O     1 
ATOM   9236  C  CB    . VAL A 1  1212 ? 83.736  123.246 179.412 1.00 45.97  ? 1212 VAL A CB    1 
ATOM   9237  C  CG1   . VAL A 1  1212 ? 83.129  121.878 179.670 1.00 44.34  ? 1212 VAL A CG1   1 
ATOM   9238  C  CG2   . VAL A 1  1212 ? 83.989  123.979 180.712 1.00 44.34  ? 1212 VAL A CG2   1 
ATOM   9239  N  N     . ILE A 1  1221 ? 88.837  128.757 176.520 1.00 44.79  ? 1221 ILE A N     1 
ATOM   9240  C  CA    . ILE A 1  1221 ? 89.278  127.385 176.318 1.00 46.04  ? 1221 ILE A CA    1 
ATOM   9241  C  C     . ILE A 1  1221 ? 90.662  127.194 176.922 1.00 44.90  ? 1221 ILE A C     1 
ATOM   9242  O  O     . ILE A 1  1221 ? 91.570  127.976 176.661 1.00 46.14  ? 1221 ILE A O     1 
ATOM   9243  C  CB    . ILE A 1  1221 ? 89.279  127.016 174.832 1.00 46.50  ? 1221 ILE A CB    1 
ATOM   9244  C  CG1   . ILE A 1  1221 ? 87.912  127.295 174.206 1.00 45.19  ? 1221 ILE A CG1   1 
ATOM   9245  C  CG2   . ILE A 1  1221 ? 89.617  125.546 174.667 1.00 45.92  ? 1221 ILE A CG2   1 
ATOM   9246  C  CD1   . ILE A 1  1221 ? 86.801  126.425 174.753 1.00 42.91  ? 1221 ILE A CD1   1 
ATOM   9247  N  N     . ILE A 1  1222 ? 90.815  126.157 177.740 1.00 40.95  ? 1222 ILE A N     1 
ATOM   9248  C  CA    . ILE A 1  1222 ? 92.071  125.874 178.420 1.00 43.83  ? 1222 ILE A CA    1 
ATOM   9249  C  C     . ILE A 1  1222 ? 92.294  124.368 178.421 1.00 45.49  ? 1222 ILE A C     1 
ATOM   9250  O  O     . ILE A 1  1222 ? 91.345  123.582 178.337 1.00 46.13  ? 1222 ILE A O     1 
ATOM   9251  C  CB    . ILE A 1  1222 ? 92.070  126.452 179.854 1.00 44.63  ? 1222 ILE A CB    1 
ATOM   9252  C  CG1   . ILE A 1  1222 ? 93.493  126.688 180.355 1.00 45.44  ? 1222 ILE A CG1   1 
ATOM   9253  C  CG2   . ILE A 1  1222 ? 91.318  125.547 180.808 1.00 43.86  ? 1222 ILE A CG2   1 
ATOM   9254  C  CD1   . ILE A 1  1222 ? 93.561  127.681 181.488 1.00 43.53  ? 1222 ILE A CD1   1 
ATOM   9255  N  N     . ILE A 1  1223 ? 93.559  123.963 178.502 1.00 44.52  ? 1223 ILE A N     1 
ATOM   9256  C  CA    . ILE A 1  1223 ? 93.924  122.550 178.429 1.00 43.36  ? 1223 ILE A CA    1 
ATOM   9257  C  C     . ILE A 1  1223 ? 95.153  122.321 179.300 1.00 46.14  ? 1223 ILE A C     1 
ATOM   9258  O  O     . ILE A 1  1223 ? 96.124  123.080 179.238 1.00 45.16  ? 1223 ILE A O     1 
ATOM   9259  C  CB    . ILE A 1  1223 ? 94.157  122.114 176.961 1.00 44.62  ? 1223 ILE A CB    1 
ATOM   9260  C  CG1   . ILE A 1  1223 ? 94.416  120.611 176.852 1.00 45.72  ? 1223 ILE A CG1   1 
ATOM   9261  C  CG2   . ILE A 1  1223 ? 95.277  122.900 176.312 1.00 45.97  ? 1223 ILE A CG2   1 
ATOM   9262  C  CD1   . ILE A 1  1223 ? 93.428  119.779 177.598 1.00 43.76  ? 1223 ILE A CD1   1 
ATOM   9263  N  N     . ARG A 1  1224 ? 95.105  121.274 180.126 1.00 49.71  ? 1224 ARG A N     1 
ATOM   9264  C  CA    . ARG A 1  1224 ? 96.192  120.966 181.059 1.00 52.69  ? 1224 ARG A CA    1 
ATOM   9265  C  C     . ARG A 1  1224 ? 96.551  119.492 180.907 1.00 53.57  ? 1224 ARG A C     1 
ATOM   9266  O  O     . ARG A 1  1224 ? 95.985  118.636 181.592 1.00 53.12  ? 1224 ARG A O     1 
ATOM   9267  C  CB    . ARG A 1  1224 ? 95.807  121.288 182.502 1.00 51.71  ? 1224 ARG A CB    1 
ATOM   9268  C  CG    . ARG A 1  1224 ? 95.183  122.657 182.689 1.00 51.46  ? 1224 ARG A CG    1 
ATOM   9269  C  CD    . ARG A 1  1224 ? 94.926  122.987 184.151 1.00 52.01  ? 1224 ARG A CD    1 
ATOM   9270  N  NE    . ARG A 1  1224 ? 96.149  123.356 184.858 1.00 52.72  ? 1224 ARG A NE    1 
ATOM   9271  C  CZ    . ARG A 1  1224 ? 96.695  122.653 185.841 1.00 53.25  ? 1224 ARG A CZ    1 
ATOM   9272  N  NH1   . ARG A 1  1224 ? 96.118  121.560 186.315 1.00 52.33  ? 1224 ARG A NH1   1 
ATOM   9273  N  NH2   . ARG A 1  1224 ? 97.845  123.061 186.369 1.00 51.20  ? 1224 ARG A NH2   1 
ATOM   9274  N  N     . ILE A 1  1225 ? 97.508  119.206 180.035 1.00 55.01  ? 1225 ILE A N     1 
ATOM   9275  C  CA    . ILE A 1  1225 ? 97.912  117.834 179.750 1.00 55.91  ? 1225 ILE A CA    1 
ATOM   9276  C  C     . ILE A 1  1225 ? 98.822  117.336 180.864 1.00 55.54  ? 1225 ILE A C     1 
ATOM   9277  O  O     . ILE A 1  1225 ? 99.825  117.979 181.198 1.00 52.36  ? 1225 ILE A O     1 
ATOM   9278  C  CB    . ILE A 1  1225 ? 98.612  117.739 178.386 1.00 55.17  ? 1225 ILE A CB    1 
ATOM   9279  C  CG1   . ILE A 1  1225 ? 97.795  118.468 177.319 1.00 53.92  ? 1225 ILE A CG1   1 
ATOM   9280  C  CG2   . ILE A 1  1225 ? 98.872  116.285 178.014 1.00 53.11  ? 1225 ILE A CG2   1 
ATOM   9281  C  CD1   . ILE A 1  1225 ? 98.505  118.579 175.983 1.00 54.57  ? 1225 ILE A CD1   1 
ATOM   9282  N  N     . TYR A 1  1226 ? 98.469  116.191 181.438 1.00 59.12  ? 1226 TYR A N     1 
ATOM   9283  C  CA    . TYR A 1  1226 ? 99.266  115.520 182.451 1.00 59.11  ? 1226 TYR A CA    1 
ATOM   9284  C  C     . TYR A 1  1226 ? 99.840  114.234 181.880 1.00 59.47  ? 1226 TYR A C     1 
ATOM   9285  O  O     . TYR A 1  1226 ? 99.227  113.571 181.042 1.00 58.31  ? 1226 TYR A O     1 
ATOM   9286  C  CB    . TYR A 1  1226 ? 98.434  115.209 183.699 1.00 60.02  ? 1226 TYR A CB    1 
ATOM   9287  C  CG    . TYR A 1  1226 ? 98.147  116.407 184.572 1.00 60.70  ? 1226 TYR A CG    1 
ATOM   9288  C  CD1   . TYR A 1  1226 ? 98.978  117.516 184.560 1.00 58.70  ? 1226 TYR A CD1   1 
ATOM   9289  C  CD2   . TYR A 1  1226 ? 97.035  116.432 185.403 1.00 59.63  ? 1226 TYR A CD2   1 
ATOM   9290  C  CE1   . TYR A 1  1226 ? 98.716  118.612 185.356 1.00 59.77  ? 1226 TYR A CE1   1 
ATOM   9291  C  CE2   . TYR A 1  1226 ? 96.767  117.522 186.203 1.00 60.05  ? 1226 TYR A CE2   1 
ATOM   9292  C  CZ    . TYR A 1  1226 ? 97.610  118.610 186.175 1.00 61.53  ? 1226 TYR A CZ    1 
ATOM   9293  O  OH    . TYR A 1  1226 ? 97.342  119.700 186.972 1.00 60.67  ? 1226 TYR A OH    1 
ATOM   9294  N  N     . LEU A 1  1227 ? 101.028 113.878 182.364 1.00 55.86  ? 1227 LEU A N     1 
ATOM   9295  C  CA    . LEU A 1  1227 ? 101.765 112.751 181.809 1.00 55.99  ? 1227 LEU A CA    1 
ATOM   9296  C  C     . LEU A 1  1227 ? 101.899 111.614 182.811 1.00 56.47  ? 1227 LEU A C     1 
ATOM   9297  O  O     . LEU A 1  1227 ? 101.384 111.696 183.930 1.00 56.42  ? 1227 LEU A O     1 
ATOM   9298  C  CB    . LEU A 1  1227 ? 103.145 113.214 181.333 1.00 53.68  ? 1227 LEU A CB    1 
ATOM   9299  C  CG    . LEU A 1  1227 ? 103.820 114.319 182.152 1.00 55.44  ? 1227 LEU A CG    1 
ATOM   9300  C  CD1   . LEU A 1  1227 ? 104.260 113.826 183.526 1.00 55.48  ? 1227 LEU A CD1   1 
ATOM   9301  C  CD2   . LEU A 1  1227 ? 104.998 114.914 181.388 1.00 53.78  ? 1227 LEU A CD2   1 
ATOM   9302  N  N     . ARG A 1  1228 ? 102.599 110.556 182.414 1.00 58.26  ? 1228 ARG A N     1 
ATOM   9303  C  CA    . ARG A 1  1228 ? 102.839 109.394 183.253 1.00 58.31  ? 1228 ARG A CA    1 
ATOM   9304  C  C     . ARG A 1  1228 ? 104.338 109.192 183.418 1.00 59.70  ? 1228 ARG A C     1 
ATOM   9305  O  O     . ARG A 1  1228 ? 105.143 109.648 182.603 1.00 58.22  ? 1228 ARG A O     1 
ATOM   9306  C  CB    . ARG A 1  1228 ? 102.210 108.119 182.660 1.00 57.03  ? 1228 ARG A CB    1 
ATOM   9307  C  CG    . ARG A 1  1228 ? 100.698 108.142 182.534 1.00 56.16  ? 1228 ARG A CG    1 
ATOM   9308  C  CD    . ARG A 1  1228 ? 100.198 107.023 181.623 1.00 57.36  ? 1228 ARG A CD    1 
ATOM   9309  N  NE    . ARG A 1  1228 ? 100.536 105.689 182.104 1.00 58.47  ? 1228 ARG A NE    1 
ATOM   9310  C  CZ    . ARG A 1  1228 ? 99.727  104.919 182.820 1.00 59.80  ? 1228 ARG A CZ    1 
ATOM   9311  N  NH1   . ARG A 1  1228 ? 98.512  105.319 183.164 1.00 59.38  ? 1228 ARG A NH1   1 
ATOM   9312  N  NH2   . ARG A 1  1228 ? 100.146 103.714 183.198 1.00 57.95  ? 1228 ARG A NH2   1 
ATOM   9313  N  N     . GLU A 1  1229 ? 104.705 108.502 184.498 1.00 59.57  ? 1229 GLU A N     1 
ATOM   9314  C  CA    . GLU A 1  1229 ? 106.087 108.079 184.675 1.00 58.46  ? 1229 GLU A CA    1 
ATOM   9315  C  C     . GLU A 1  1229 ? 106.446 106.918 183.758 1.00 60.04  ? 1229 GLU A C     1 
ATOM   9316  O  O     . GLU A 1  1229 ? 107.636 106.672 183.526 1.00 59.88  ? 1229 GLU A O     1 
ATOM   9317  C  CB    . GLU A 1  1229 ? 106.331 107.672 186.129 1.00 56.77  ? 1229 GLU A CB    1 
ATOM   9318  C  CG    . GLU A 1  1229 ? 106.643 108.817 187.071 1.00 57.34  ? 1229 GLU A CG    1 
ATOM   9319  C  CD    . GLU A 1  1229 ? 108.088 109.263 187.008 1.00 60.25  ? 1229 GLU A CD    1 
ATOM   9320  O  OE1   . GLU A 1  1229 ? 108.963 108.420 186.721 1.00 62.05  ? 1229 GLU A OE1   1 
ATOM   9321  O  OE2   . GLU A 1  1229 ? 108.349 110.455 187.265 1.00 59.97  ? 1229 GLU A OE2   1 
ATOM   9322  N  N     . SER A 1  1230 ? 105.447 106.201 183.232 1.00 50.68  ? 1230 SER A N     1 
ATOM   9323  C  CA    . SER A 1  1230 ? 105.704 105.017 182.420 1.00 52.45  ? 1230 SER A CA    1 
ATOM   9324  C  C     . SER A 1  1230 ? 106.404 105.344 181.110 1.00 52.69  ? 1230 SER A C     1 
ATOM   9325  O  O     . SER A 1  1230 ? 106.960 104.437 180.481 1.00 54.06  ? 1230 SER A O     1 
ATOM   9326  C  CB    . SER A 1  1230 ? 104.397 104.278 182.127 1.00 51.09  ? 1230 SER A CB    1 
ATOM   9327  O  OG    . SER A 1  1230 ? 103.553 105.040 181.283 1.00 51.08  ? 1230 SER A OG    1 
ATOM   9328  N  N     . ALA A 1  1231 ? 106.385 106.605 180.685 1.00 49.75  ? 1231 ALA A N     1 
ATOM   9329  C  CA    . ALA A 1  1231 ? 107.096 107.023 179.488 1.00 49.65  ? 1231 ALA A CA    1 
ATOM   9330  C  C     . ALA A 1  1231 ? 108.500 107.532 179.786 1.00 46.41  ? 1231 ALA A C     1 
ATOM   9331  O  O     . ALA A 1  1231 ? 109.156 108.055 178.880 1.00 47.51  ? 1231 ALA A O     1 
ATOM   9332  C  CB    . ALA A 1  1231 ? 106.294 108.100 178.752 1.00 48.20  ? 1231 ALA A CB    1 
ATOM   9333  N  N     . PHE A 1  1232 ? 108.972 107.396 181.028 1.00 52.70  ? 1232 PHE A N     1 
ATOM   9334  C  CA    . PHE A 1  1232 ? 110.292 107.873 181.417 1.00 56.29  ? 1232 PHE A CA    1 
ATOM   9335  C  C     . PHE A 1  1232 ? 111.326 106.770 181.583 1.00 58.17  ? 1232 PHE A C     1 
ATOM   9336  O  O     . PHE A 1  1232 ? 112.516 107.081 181.681 1.00 58.91  ? 1232 PHE A O     1 
ATOM   9337  C  CB    . PHE A 1  1232 ? 110.220 108.655 182.740 1.00 55.87  ? 1232 PHE A CB    1 
ATOM   9338  C  CG    . PHE A 1  1232 ? 109.393 109.907 182.671 1.00 57.21  ? 1232 PHE A CG    1 
ATOM   9339  C  CD1   . PHE A 1  1232 ? 109.223 110.581 181.477 1.00 57.55  ? 1232 PHE A CD1   1 
ATOM   9340  C  CD2   . PHE A 1  1232 ? 108.790 110.412 183.811 1.00 56.90  ? 1232 PHE A CD2   1 
ATOM   9341  C  CE1   . PHE A 1  1232 ? 108.458 111.734 181.418 1.00 57.92  ? 1232 PHE A CE1   1 
ATOM   9342  C  CE2   . PHE A 1  1232 ? 108.027 111.562 183.761 1.00 57.27  ? 1232 PHE A CE2   1 
ATOM   9343  C  CZ    . PHE A 1  1232 ? 107.860 112.224 182.565 1.00 56.77  ? 1232 PHE A CZ    1 
ATOM   9344  N  N     . ARG A 1  1233 ? 110.913 105.505 181.648 1.00 56.51  ? 1233 ARG A N     1 
ATOM   9345  C  CA    . ARG A 1  1233 ? 111.838 104.432 181.992 1.00 55.79  ? 1233 ARG A CA    1 
ATOM   9346  C  C     . ARG A 1  1233 ? 112.289 103.583 180.806 1.00 54.55  ? 1233 ARG A C     1 
ATOM   9347  O  O     . ARG A 1  1233 ? 113.221 102.787 180.961 1.00 52.36  ? 1233 ARG A O     1 
ATOM   9348  C  CB    . ARG A 1  1233 ? 111.220 103.527 183.067 1.00 54.44  ? 1233 ARG A CB    1 
ATOM   9349  C  CG    . ARG A 1  1233 ? 112.264 102.794 183.892 1.00 53.79  ? 1233 ARG A CG    1 
ATOM   9350  C  CD    . ARG A 1  1233 ? 113.305 103.756 184.443 1.00 53.02  ? 1233 ARG A CD    1 
ATOM   9351  N  NE    . ARG A 1  1233 ? 114.565 103.075 184.723 1.00 56.25  ? 1233 ARG A NE    1 
ATOM   9352  C  CZ    . ARG A 1  1233 ? 115.555 102.952 183.848 1.00 55.45  ? 1233 ARG A CZ    1 
ATOM   9353  N  NH1   . ARG A 1  1233 ? 115.478 103.482 182.638 1.00 54.68  ? 1233 ARG A NH1   1 
ATOM   9354  N  NH2   . ARG A 1  1233 ? 116.650 102.279 184.194 1.00 52.70  ? 1233 ARG A NH2   1 
ATOM   9355  N  N     . ARG A 1  1234 ? 111.680 103.728 179.627 1.00 62.87  ? 1234 ARG A N     1 
ATOM   9356  C  CA    . ARG A 1  1234 ? 112.074 102.945 178.459 1.00 63.32  ? 1234 ARG A CA    1 
ATOM   9357  C  C     . ARG A 1  1234 ? 113.206 103.600 177.668 1.00 63.37  ? 1234 ARG A C     1 
ATOM   9358  O  O     . ARG A 1  1234 ? 113.428 103.255 176.497 1.00 64.52  ? 1234 ARG A O     1 
ATOM   9359  C  CB    . ARG A 1  1234 ? 110.861 102.699 177.558 1.00 60.97  ? 1234 ARG A CB    1 
ATOM   9360  C  CG    . ARG A 1  1234 ? 110.964 101.462 176.668 1.00 60.87  ? 1234 ARG A CG    1 
ATOM   9361  C  CD    . ARG A 1  1234 ? 109.597 100.890 176.328 1.00 63.52  ? 1234 ARG A CD    1 
ATOM   9362  N  NE    . ARG A 1  1234 ? 109.191 99.823  177.235 1.00 63.70  ? 1234 ARG A NE    1 
ATOM   9363  C  CZ    . ARG A 1  1234 ? 108.283 99.958  178.191 1.00 63.63  ? 1234 ARG A CZ    1 
ATOM   9364  N  NH1   . ARG A 1  1234 ? 107.685 101.117 178.419 1.00 61.95  ? 1234 ARG A NH1   1 
ATOM   9365  N  NH2   . ARG A 1  1234 ? 107.965 98.904  178.938 1.00 63.59  ? 1234 ARG A NH2   1 
ATOM   9366  N  N     . SER A 1  1235 ? 113.938 104.530 178.278 1.00 56.05  ? 1235 SER A N     1 
ATOM   9367  C  CA    . SER A 1  1235 ? 115.018 105.254 177.609 1.00 57.16  ? 1235 SER A CA    1 
ATOM   9368  C  C     . SER A 1  1235 ? 116.382 104.669 177.941 1.00 56.82  ? 1235 SER A C     1 
ATOM   9369  O  O     . SER A 1  1235 ? 117.365 105.405 178.065 1.00 54.18  ? 1235 SER A O     1 
ATOM   9370  C  CB    . SER A 1  1235 ? 114.969 106.734 177.973 1.00 55.38  ? 1235 SER A CB    1 
ATOM   9371  O  OG    . SER A 1  1235 ? 116.008 107.457 177.335 1.00 53.22  ? 1235 SER A OG    1 
ATOM   9372  N  N     . THR A 1  1236 ? 116.465 103.342 178.084 1.00 51.56  ? 1236 THR A N     1 
ATOM   9373  C  CA    . THR A 1  1236 ? 117.718 102.698 178.466 1.00 50.39  ? 1236 THR A CA    1 
ATOM   9374  C  C     . THR A 1  1236 ? 118.839 102.964 177.468 1.00 50.43  ? 1236 THR A C     1 
ATOM   9375  O  O     . THR A 1  1236 ? 120.015 102.837 177.827 1.00 47.96  ? 1236 THR A O     1 
ATOM   9376  C  CB    . THR A 1  1236 ? 117.514 101.187 178.619 1.00 52.62  ? 1236 THR A CB    1 
ATOM   9377  O  OG1   . THR A 1  1236 ? 118.735 100.579 179.058 1.00 50.34  ? 1236 THR A OG1   1 
ATOM   9378  C  CG2   . THR A 1  1236 ? 117.086 100.556 177.293 1.00 48.54  ? 1236 THR A CG2   1 
ATOM   9379  N  N     . ASN A 1  1237 ? 118.506 103.337 176.235 1.00 51.47  ? 1237 ASN A N     1 
ATOM   9380  C  CA    . ASN A 1  1237 ? 119.501 103.667 175.225 1.00 51.39  ? 1237 ASN A CA    1 
ATOM   9381  C  C     . ASN A 1  1237 ? 120.201 104.994 175.502 1.00 51.57  ? 1237 ASN A C     1 
ATOM   9382  O  O     . ASN A 1  1237 ? 121.241 105.270 174.893 1.00 49.09  ? 1237 ASN A O     1 
ATOM   9383  C  CB    . ASN A 1  1237 ? 118.845 103.709 173.844 1.00 48.41  ? 1237 ASN A CB    1 
ATOM   9384  C  CG    . ASN A 1  1237 ? 117.795 102.629 173.665 1.00 50.12  ? 1237 ASN A CG    1 
ATOM   9385  O  OD1   . ASN A 1  1237 ? 116.614 102.923 173.492 1.00 49.86  ? 1237 ASN A OD1   1 
ATOM   9386  N  ND2   . ASN A 1  1237 ? 118.220 101.373 173.710 1.00 48.17  ? 1237 ASN A ND2   1 
ATOM   9387  N  N     . THR A 1  1238 ? 119.656 105.812 176.403 1.00 51.25  ? 1238 THR A N     1 
ATOM   9388  C  CA    . THR A 1  1238 ? 120.262 107.081 176.794 1.00 53.19  ? 1238 THR A CA    1 
ATOM   9389  C  C     . THR A 1  1238 ? 120.518 107.048 178.291 1.00 54.22  ? 1238 THR A C     1 
ATOM   9390  O  O     . THR A 1  1238 ? 119.598 106.786 179.071 1.00 55.13  ? 1238 THR A O     1 
ATOM   9391  C  CB    . THR A 1  1238 ? 119.360 108.268 176.434 1.00 54.00  ? 1238 THR A CB    1 
ATOM   9392  O  OG1   . THR A 1  1238 ? 119.393 108.492 175.020 1.00 52.37  ? 1238 THR A OG1   1 
ATOM   9393  C  CG2   . THR A 1  1238 ? 119.805 109.522 177.162 1.00 50.65  ? 1238 THR A CG2   1 
ATOM   9394  N  N     . ARG A 1  1239 ? 121.757 107.318 178.697 1.00 58.91  ? 1239 ARG A N     1 
ATOM   9395  C  CA    . ARG A 1  1239 ? 122.116 107.269 180.108 1.00 60.12  ? 1239 ARG A CA    1 
ATOM   9396  C  C     . ARG A 1  1239 ? 122.268 108.654 180.728 1.00 61.74  ? 1239 ARG A C     1 
ATOM   9397  O  O     . ARG A 1  1239 ? 122.537 108.756 181.931 1.00 62.37  ? 1239 ARG A O     1 
ATOM   9398  C  CB    . ARG A 1  1239 ? 123.397 106.447 180.296 1.00 60.58  ? 1239 ARG A CB    1 
ATOM   9399  C  CG    . ARG A 1  1239 ? 123.188 104.973 179.958 1.00 61.18  ? 1239 ARG A CG    1 
ATOM   9400  C  CD    . ARG A 1  1239 ? 124.227 104.048 180.571 1.00 61.01  ? 1239 ARG A CD    1 
ATOM   9401  N  NE    . ARG A 1  1239 ? 123.906 102.654 180.278 1.00 61.36  ? 1239 ARG A NE    1 
ATOM   9402  C  CZ    . ARG A 1  1239 ? 124.504 101.607 180.829 1.00 60.17  ? 1239 ARG A CZ    1 
ATOM   9403  N  NH1   . ARG A 1  1239 ? 125.460 101.752 181.733 1.00 59.19  ? 1239 ARG A NH1   1 
ATOM   9404  N  NH2   . ARG A 1  1239 ? 124.129 100.383 180.470 1.00 59.83  ? 1239 ARG A NH2   1 
ATOM   9405  N  N     . MET A 1  1240 ? 122.083 109.722 179.950 1.00 57.57  ? 1240 MET A N     1 
ATOM   9406  C  CA    . MET A 1  1240 ? 122.118 111.086 180.463 1.00 56.31  ? 1240 MET A CA    1 
ATOM   9407  C  C     . MET A 1  1240 ? 120.736 111.731 180.478 1.00 55.72  ? 1240 MET A C     1 
ATOM   9408  O  O     . MET A 1  1240 ? 120.628 112.959 180.558 1.00 53.90  ? 1240 MET A O     1 
ATOM   9409  C  CB    . MET A 1  1240 ? 123.085 111.942 179.642 1.00 53.61  ? 1240 MET A CB    1 
ATOM   9410  C  CG    . MET A 1  1240 ? 124.513 111.964 180.161 1.00 55.39  ? 1240 MET A CG    1 
ATOM   9411  S  SD    . MET A 1  1240 ? 125.102 110.346 180.685 1.00 62.00  ? 1240 MET A SD    1 
ATOM   9412  C  CE    . MET A 1  1240 ? 126.874 110.598 180.687 1.00 52.83  ? 1240 MET A CE    1 
ATOM   9413  N  N     . ALA A 1  1241 ? 119.678 110.928 180.402 1.00 50.71  ? 1241 ALA A N     1 
ATOM   9414  C  CA    . ALA A 1  1241 ? 118.315 111.448 180.329 1.00 51.27  ? 1241 ALA A CA    1 
ATOM   9415  C  C     . ALA A 1  1241 ? 117.922 112.017 181.686 1.00 50.91  ? 1241 ALA A C     1 
ATOM   9416  O  O     . ALA A 1  1241 ? 117.783 111.286 182.669 1.00 50.56  ? 1241 ALA A O     1 
ATOM   9417  C  CB    . ALA A 1  1241 ? 117.348 110.356 179.888 1.00 49.53  ? 1241 ALA A CB    1 
ATOM   9418  N  N     . THR A 1  1242 ? 117.762 113.334 181.748 1.00 47.77  ? 1242 THR A N     1 
ATOM   9419  C  CA    . THR A 1  1242 ? 117.221 113.986 182.927 1.00 50.16  ? 1242 THR A CA    1 
ATOM   9420  C  C     . THR A 1  1242 ? 115.711 114.139 182.755 1.00 51.00  ? 1242 THR A C     1 
ATOM   9421  O  O     . THR A 1  1242 ? 115.101 113.519 181.881 1.00 48.39  ? 1242 THR A O     1 
ATOM   9422  C  CB    . THR A 1  1242 ? 117.903 115.330 183.164 1.00 50.81  ? 1242 THR A CB    1 
ATOM   9423  O  OG1   . THR A 1  1242 ? 117.317 115.963 184.309 1.00 49.75  ? 1242 THR A OG1   1 
ATOM   9424  C  CG2   . THR A 1  1242 ? 117.730 116.230 181.948 1.00 49.27  ? 1242 THR A CG2   1 
ATOM   9425  N  N     . ASP A 1  1243 ? 115.090 114.962 183.599 1.00 50.57  ? 1243 ASP A N     1 
ATOM   9426  C  CA    . ASP A 1  1243 ? 113.655 115.190 183.508 1.00 50.15  ? 1243 ASP A CA    1 
ATOM   9427  C  C     . ASP A 1  1243 ? 113.298 116.392 182.644 1.00 52.01  ? 1243 ASP A C     1 
ATOM   9428  O  O     . ASP A 1  1243 ? 112.230 116.399 182.023 1.00 50.36  ? 1243 ASP A O     1 
ATOM   9429  C  CB    . ASP A 1  1243 ? 113.060 115.373 184.906 1.00 49.61  ? 1243 ASP A CB    1 
ATOM   9430  C  CG    . ASP A 1  1243 ? 113.386 114.220 185.836 1.00 51.30  ? 1243 ASP A CG    1 
ATOM   9431  O  OD1   . ASP A 1  1243 ? 113.796 113.150 185.337 1.00 50.42  ? 1243 ASP A OD1   1 
ATOM   9432  O  OD2   . ASP A 1  1243 ? 113.224 114.383 187.064 1.00 50.17  ? 1243 ASP A OD2   1 
ATOM   9433  N  N     . GLU A 1  1244 ? 114.158 117.413 182.596 1.00 55.42  ? 1244 GLU A N     1 
ATOM   9434  C  CA    . GLU A 1  1244 ? 113.857 118.600 181.800 1.00 54.70  ? 1244 GLU A CA    1 
ATOM   9435  C  C     . GLU A 1  1244 ? 113.855 118.280 180.311 1.00 55.27  ? 1244 GLU A C     1 
ATOM   9436  O  O     . GLU A 1  1244 ? 112.887 118.580 179.601 1.00 53.79  ? 1244 GLU A O     1 
ATOM   9437  C  CB    . GLU A 1  1244 ? 114.874 119.704 182.100 1.00 54.27  ? 1244 GLU A CB    1 
ATOM   9438  C  CG    . GLU A 1  1244 ? 114.741 120.362 183.464 1.00 55.44  ? 1244 GLU A CG    1 
ATOM   9439  C  CD    . GLU A 1  1244 ? 113.531 121.267 183.561 1.00 57.37  ? 1244 GLU A CD    1 
ATOM   9440  O  OE1   . GLU A 1  1244 ? 113.115 121.819 182.521 1.00 56.80  ? 1244 GLU A OE1   1 
ATOM   9441  O  OE2   . GLU A 1  1244 ? 113.008 121.445 184.680 1.00 56.88  ? 1244 GLU A OE2   1 
ATOM   9442  N  N     . LYS A 1  1245 ? 114.934 117.664 179.822 1.00 55.75  ? 1245 LYS A N     1 
ATOM   9443  C  CA    . LYS A 1  1245 ? 115.046 117.367 178.399 1.00 55.93  ? 1245 LYS A CA    1 
ATOM   9444  C  C     . LYS A 1  1245 ? 113.987 116.365 177.965 1.00 55.49  ? 1245 LYS A C     1 
ATOM   9445  O  O     . LYS A 1  1245 ? 113.363 116.519 176.908 1.00 54.75  ? 1245 LYS A O     1 
ATOM   9446  C  CB    . LYS A 1  1245 ? 116.445 116.837 178.085 1.00 54.94  ? 1245 LYS A CB    1 
ATOM   9447  C  CG    . LYS A 1  1245 ? 116.719 116.630 176.601 1.00 54.93  ? 1245 LYS A CG    1 
ATOM   9448  C  CD    . LYS A 1  1245 ? 118.141 116.141 176.363 1.00 55.01  ? 1245 LYS A CD    1 
ATOM   9449  C  CE    . LYS A 1  1245 ? 118.397 115.898 174.886 1.00 54.39  ? 1245 LYS A CE    1 
ATOM   9450  N  NZ    . LYS A 1  1245 ? 119.763 115.371 174.626 1.00 54.52  ? 1245 LYS A NZ    1 
ATOM   9451  N  N     . ILE A 1  1246 ? 113.770 115.329 178.777 1.00 50.97  ? 1246 ILE A N     1 
ATOM   9452  C  CA    . ILE A 1  1246 ? 112.784 114.312 178.436 1.00 50.47  ? 1246 ILE A CA    1 
ATOM   9453  C  C     . ILE A 1  1246 ? 111.381 114.905 178.451 1.00 51.14  ? 1246 ILE A C     1 
ATOM   9454  O  O     . ILE A 1  1246 ? 110.494 114.436 177.730 1.00 50.23  ? 1246 ILE A O     1 
ATOM   9455  C  CB    . ILE A 1  1246 ? 112.931 113.110 179.390 1.00 49.97  ? 1246 ILE A CB    1 
ATOM   9456  C  CG1   . ILE A 1  1246 ? 112.420 111.830 178.731 1.00 50.18  ? 1246 ILE A CG1   1 
ATOM   9457  C  CG2   . ILE A 1  1246 ? 112.199 113.358 180.697 1.00 49.04  ? 1246 ILE A CG2   1 
ATOM   9458  C  CD1   . ILE A 1  1246 ? 112.874 110.570 179.441 1.00 50.74  ? 1246 ILE A CD1   1 
ATOM   9459  N  N     . ALA A 1  1247 ? 111.158 115.947 179.259 1.00 49.17  ? 1247 ALA A N     1 
ATOM   9460  C  CA    . ALA A 1  1247 ? 109.887 116.663 179.221 1.00 48.90  ? 1247 ALA A CA    1 
ATOM   9461  C  C     . ALA A 1  1247 ? 109.765 117.499 177.954 1.00 47.71  ? 1247 ALA A C     1 
ATOM   9462  O  O     . ALA A 1  1247 ? 108.673 117.618 177.386 1.00 45.82  ? 1247 ALA A O     1 
ATOM   9463  C  CB    . ALA A 1  1247 ? 109.736 117.544 180.460 1.00 44.41  ? 1247 ALA A CB    1 
ATOM   9464  N  N     . VAL A 1  1248 ? 110.869 118.098 177.503 1.00 46.51  ? 1248 VAL A N     1 
ATOM   9465  C  CA    . VAL A 1  1248 ? 110.833 118.831 176.242 1.00 48.71  ? 1248 VAL A CA    1 
ATOM   9466  C  C     . VAL A 1  1248 ? 110.581 117.879 175.084 1.00 49.79  ? 1248 VAL A C     1 
ATOM   9467  O  O     . VAL A 1  1248 ? 109.808 118.193 174.172 1.00 46.52  ? 1248 VAL A O     1 
ATOM   9468  C  CB    . VAL A 1  1248 ? 112.131 119.636 176.037 1.00 47.65  ? 1248 VAL A CB    1 
ATOM   9469  C  CG1   . VAL A 1  1248 ? 112.074 120.404 174.736 1.00 45.11  ? 1248 VAL A CG1   1 
ATOM   9470  C  CG2   . VAL A 1  1248 ? 112.351 120.597 177.188 1.00 47.42  ? 1248 VAL A CG2   1 
ATOM   9471  N  N     . ASN A 1  1249 ? 111.206 116.699 175.112 1.00 51.97  ? 1249 ASN A N     1 
ATOM   9472  C  CA    . ASN A 1  1249 ? 111.072 115.748 174.012 1.00 52.23  ? 1249 ASN A CA    1 
ATOM   9473  C  C     . ASN A 1  1249 ? 109.628 115.283 173.849 1.00 52.31  ? 1249 ASN A C     1 
ATOM   9474  O  O     . ASN A 1  1249 ? 109.105 115.235 172.730 1.00 51.72  ? 1249 ASN A O     1 
ATOM   9475  C  CB    . ASN A 1  1249 ? 112.004 114.557 174.242 1.00 50.33  ? 1249 ASN A CB    1 
ATOM   9476  C  CG    . ASN A 1  1249 ? 112.192 113.705 172.997 1.00 52.45  ? 1249 ASN A CG    1 
ATOM   9477  O  OD1   . ASN A 1  1249 ? 111.675 114.021 171.925 1.00 53.53  ? 1249 ASN A OD1   1 
ATOM   9478  N  ND2   . ASN A 1  1249 ? 112.954 112.625 173.131 1.00 51.80  ? 1249 ASN A ND2   1 
ATOM   9479  N  N     . VAL A 1  1250 ? 108.964 114.935 174.953 1.00 46.30  ? 1250 VAL A N     1 
ATOM   9480  C  CA    . VAL A 1  1250 ? 107.588 114.461 174.829 1.00 47.41  ? 1250 VAL A CA    1 
ATOM   9481  C  C     . VAL A 1  1250 ? 106.653 115.595 174.425 1.00 47.62  ? 1250 VAL A C     1 
ATOM   9482  O  O     . VAL A 1  1250 ? 105.716 115.380 173.650 1.00 47.10  ? 1250 VAL A O     1 
ATOM   9483  C  CB    . VAL A 1  1250 ? 107.126 113.760 176.118 1.00 47.62  ? 1250 VAL A CB    1 
ATOM   9484  C  CG1   . VAL A 1  1250 ? 107.926 112.488 176.325 1.00 46.51  ? 1250 VAL A CG1   1 
ATOM   9485  C  CG2   . VAL A 1  1250 ? 107.257 114.684 177.317 1.00 48.39  ? 1250 VAL A CG2   1 
ATOM   9486  N  N     . VAL A 1  1251 ? 106.881 116.810 174.931 1.00 46.08  ? 1251 VAL A N     1 
ATOM   9487  C  CA    . VAL A 1  1251 ? 106.166 117.970 174.403 1.00 48.25  ? 1251 VAL A CA    1 
ATOM   9488  C  C     . VAL A 1  1251 ? 106.524 118.176 172.937 1.00 48.01  ? 1251 VAL A C     1 
ATOM   9489  O  O     . VAL A 1  1251 ? 105.657 118.462 172.101 1.00 44.42  ? 1251 VAL A O     1 
ATOM   9490  C  CB    . VAL A 1  1251 ? 106.467 119.223 175.246 1.00 45.37  ? 1251 VAL A CB    1 
ATOM   9491  C  CG1   . VAL A 1  1251 ? 106.108 120.484 174.475 1.00 44.24  ? 1251 VAL A CG1   1 
ATOM   9492  C  CG2   . VAL A 1  1251 ? 105.711 119.174 176.553 1.00 43.20  ? 1251 VAL A CG2   1 
ATOM   9493  N  N     . ASP A 1  1252 ? 107.810 118.029 172.605 1.00 49.00  ? 1252 ASP A N     1 
ATOM   9494  C  CA    . ASP A 1  1252 ? 108.225 118.030 171.206 1.00 51.84  ? 1252 ASP A CA    1 
ATOM   9495  C  C     . ASP A 1  1252 ? 107.570 116.890 170.437 1.00 51.73  ? 1252 ASP A C     1 
ATOM   9496  O  O     . ASP A 1  1252 ? 107.089 117.085 169.314 1.00 51.38  ? 1252 ASP A O     1 
ATOM   9497  C  CB    . ASP A 1  1252 ? 109.746 117.926 171.114 1.00 49.33  ? 1252 ASP A CB    1 
ATOM   9498  C  CG    . ASP A 1  1252 ? 110.255 118.102 169.710 1.00 51.82  ? 1252 ASP A CG    1 
ATOM   9499  O  OD1   . ASP A 1  1252 ? 110.363 119.260 169.259 1.00 51.69  ? 1252 ASP A OD1   1 
ATOM   9500  O  OD2   . ASP A 1  1252 ? 110.546 117.080 169.055 1.00 52.37  ? 1252 ASP A OD2   1 
ATOM   9501  N  N     . LYS A 1  1253 ? 107.537 115.693 171.026 1.00 48.15  ? 1253 LYS A N     1 
ATOM   9502  C  CA    . LYS A 1  1253 ? 106.859 114.573 170.388 1.00 49.96  ? 1253 LYS A CA    1 
ATOM   9503  C  C     . LYS A 1  1253 ? 105.349 114.752 170.337 1.00 49.95  ? 1253 LYS A C     1 
ATOM   9504  O  O     . LYS A 1  1253 ? 104.693 114.083 169.533 1.00 50.39  ? 1253 LYS A O     1 
ATOM   9505  C  CB    . LYS A 1  1253 ? 107.187 113.253 171.099 1.00 48.80  ? 1253 LYS A CB    1 
ATOM   9506  C  CG    . LYS A 1  1253 ? 108.520 112.637 170.698 1.00 49.28  ? 1253 LYS A CG    1 
ATOM   9507  C  CD    . LYS A 1  1253 ? 108.620 111.165 171.110 1.00 49.92  ? 1253 LYS A CD    1 
ATOM   9508  C  CE    . LYS A 1  1253 ? 109.691 110.905 172.158 1.00 50.47  ? 1253 LYS A CE    1 
ATOM   9509  N  NZ    . LYS A 1  1253 ? 109.325 111.345 173.532 1.00 48.70  ? 1253 LYS A NZ    1 
ATOM   9510  N  N     . LEU A 1  1254 ? 104.788 115.632 171.167 1.00 44.93  ? 1254 LEU A N     1 
ATOM   9511  C  CA    . LEU A 1  1254 ? 103.340 115.789 171.252 1.00 47.14  ? 1254 LEU A CA    1 
ATOM   9512  C  C     . LEU A 1  1254 ? 102.829 116.958 170.419 1.00 47.52  ? 1254 LEU A C     1 
ATOM   9513  O  O     . LEU A 1  1254 ? 101.753 116.865 169.823 1.00 45.55  ? 1254 LEU A O     1 
ATOM   9514  C  CB    . LEU A 1  1254 ? 102.925 115.958 172.720 1.00 44.97  ? 1254 LEU A CB    1 
ATOM   9515  C  CG    . LEU A 1  1254 ? 101.530 116.391 173.175 1.00 45.91  ? 1254 LEU A CG    1 
ATOM   9516  C  CD1   . LEU A 1  1254 ? 101.334 115.903 174.590 1.00 45.03  ? 1254 LEU A CD1   1 
ATOM   9517  C  CD2   . LEU A 1  1254 ? 101.332 117.892 173.130 1.00 44.91  ? 1254 LEU A CD2   1 
ATOM   9518  N  N     . LEU A 1  1255 ? 103.569 118.066 170.381 1.00 48.18  ? 1255 LEU A N     1 
ATOM   9519  C  CA    . LEU A 1  1255 ? 103.101 119.223 169.630 1.00 47.23  ? 1255 LEU A CA    1 
ATOM   9520  C  C     . LEU A 1  1255 ? 103.121 118.956 168.131 1.00 48.48  ? 1255 LEU A C     1 
ATOM   9521  O  O     . LEU A 1  1255 ? 102.361 119.578 167.380 1.00 46.49  ? 1255 LEU A O     1 
ATOM   9522  C  CB    . LEU A 1  1255 ? 103.947 120.453 169.963 1.00 45.54  ? 1255 LEU A CB    1 
ATOM   9523  C  CG    . LEU A 1  1255 ? 103.453 121.432 171.039 1.00 48.70  ? 1255 LEU A CG    1 
ATOM   9524  C  CD1   . LEU A 1  1255 ? 102.268 122.251 170.554 1.00 46.74  ? 1255 LEU A CD1   1 
ATOM   9525  C  CD2   . LEU A 1  1255 ? 103.133 120.756 172.351 1.00 47.48  ? 1255 LEU A CD2   1 
ATOM   9526  N  N     . ASN A 1  1256 ? 103.970 118.035 167.678 1.00 49.27  ? 1256 ASN A N     1 
ATOM   9527  C  CA    . ASN A 1  1256 ? 104.027 117.683 166.266 1.00 49.81  ? 1256 ASN A CA    1 
ATOM   9528  C  C     . ASN A 1  1256 ? 102.914 116.737 165.849 1.00 48.63  ? 1256 ASN A C     1 
ATOM   9529  O  O     . ASN A 1  1256 ? 102.793 116.442 164.655 1.00 50.37  ? 1256 ASN A O     1 
ATOM   9530  C  CB    . ASN A 1  1256 ? 105.377 117.049 165.926 1.00 49.12  ? 1256 ASN A CB    1 
ATOM   9531  C  CG    . ASN A 1  1256 ? 106.514 118.043 165.974 1.00 50.16  ? 1256 ASN A CG    1 
ATOM   9532  O  OD1   . ASN A 1  1256 ? 106.365 119.190 165.558 1.00 49.78  ? 1256 ASN A OD1   1 
ATOM   9533  N  ND2   . ASN A 1  1256 ? 107.664 117.603 166.469 1.00 48.61  ? 1256 ASN A ND2   1 
ATOM   9534  N  N     . SER A 1  1257 ? 102.111 116.251 166.788 1.00 43.76  ? 1257 SER A N     1 
ATOM   9535  C  CA    . SER A 1  1257 ? 101.040 115.333 166.440 1.00 46.26  ? 1257 SER A CA    1 
ATOM   9536  C  C     . SER A 1  1257 ? 99.980  116.055 165.624 1.00 46.03  ? 1257 SER A C     1 
ATOM   9537  O  O     . SER A 1  1257 ? 99.523  117.139 165.996 1.00 47.67  ? 1257 SER A O     1 
ATOM   9538  C  CB    . SER A 1  1257 ? 100.427 114.732 167.700 1.00 47.30  ? 1257 SER A CB    1 
ATOM   9539  O  OG    . SER A 1  1257 ? 101.392 113.988 168.422 1.00 48.61  ? 1257 SER A OG    1 
ATOM   9540  N  N     . THR A 1  1258 ? 99.590  115.450 164.508 1.00 42.40  ? 1258 THR A N     1 
ATOM   9541  C  CA    . THR A 1  1258 ? 98.602  116.059 163.630 1.00 43.25  ? 1258 THR A CA    1 
ATOM   9542  C  C     . THR A 1  1258 ? 97.258  116.140 164.343 1.00 43.50  ? 1258 THR A C     1 
ATOM   9543  O  O     . THR A 1  1258 ? 96.955  115.319 165.215 1.00 40.91  ? 1258 THR A O     1 
ATOM   9544  C  CB    . THR A 1  1258 ? 98.477  115.259 162.334 1.00 43.33  ? 1258 THR A CB    1 
ATOM   9545  O  OG1   . THR A 1  1258 ? 97.729  116.015 161.375 1.00 46.18  ? 1258 THR A OG1   1 
ATOM   9546  C  CG2   . THR A 1  1258 ? 97.762  113.941 162.577 1.00 38.54  ? 1258 THR A CG2   1 
ATOM   9547  N  N     . ILE A 1  1259 ? 96.477  117.163 164.011 1.00 42.13  ? 1259 ILE A N     1 
ATOM   9548  C  CA    . ILE A 1  1259 ? 95.088  117.196 164.443 1.00 41.01  ? 1259 ILE A CA    1 
ATOM   9549  C  C     . ILE A 1  1259 ? 94.175  116.856 163.278 1.00 43.66  ? 1259 ILE A C     1 
ATOM   9550  O  O     . ILE A 1  1259 ? 93.213  116.094 163.420 1.00 42.12  ? 1259 ILE A O     1 
ATOM   9551  C  CB    . ILE A 1  1259 ? 94.748  118.568 165.053 1.00 43.61  ? 1259 ILE A CB    1 
ATOM   9552  C  CG1   . ILE A 1  1259 ? 95.576  118.809 166.316 1.00 41.41  ? 1259 ILE A CG1   1 
ATOM   9553  C  CG2   . ILE A 1  1259 ? 93.263  118.665 165.363 1.00 40.89  ? 1259 ILE A CG2   1 
ATOM   9554  C  CD1   . ILE A 1  1259 ? 95.317  117.820 167.409 1.00 43.10  ? 1259 ILE A CD1   1 
ATOM   9555  N  N     . ARG A 1  1260 ? 94.479  117.396 162.102 1.00 44.77  ? 1260 ARG A N     1 
ATOM   9556  C  CA    . ARG A 1  1260 ? 93.690  117.098 160.916 1.00 44.54  ? 1260 ARG A CA    1 
ATOM   9557  C  C     . ARG A 1  1260 ? 94.538  117.361 159.680 1.00 42.93  ? 1260 ARG A C     1 
ATOM   9558  O  O     . ARG A 1  1260 ? 95.315  118.317 159.656 1.00 43.26  ? 1260 ARG A O     1 
ATOM   9559  C  CB    . ARG A 1  1260 ? 92.404  117.930 160.912 1.00 41.67  ? 1260 ARG A CB    1 
ATOM   9560  C  CG    . ARG A 1  1260 ? 91.434  117.562 159.824 1.00 42.29  ? 1260 ARG A CG    1 
ATOM   9561  C  CD    . ARG A 1  1260 ? 90.490  118.700 159.518 1.00 41.95  ? 1260 ARG A CD    1 
ATOM   9562  N  NE    . ARG A 1  1260 ? 91.140  120.002 159.553 1.00 44.45  ? 1260 ARG A NE    1 
ATOM   9563  C  CZ    . ARG A 1  1260 ? 90.515  121.146 159.319 1.00 46.13  ? 1260 ARG A CZ    1 
ATOM   9564  N  NH1   . ARG A 1  1260 ? 89.234  121.178 158.994 1.00 42.84  ? 1260 ARG A NH1   1 
ATOM   9565  N  NH2   . ARG A 1  1260 ? 91.192  122.286 159.411 1.00 45.02  ? 1260 ARG A NH2   1 
ATOM   9566  N  N     . GLY A 1  1261 ? 94.415  116.490 158.676 1.00 40.02  ? 1261 GLY A N     1 
ATOM   9567  C  CA    . GLY A 1  1261 ? 95.072  116.643 157.399 1.00 38.60  ? 1261 GLY A CA    1 
ATOM   9568  C  C     . GLY A 1  1261 ? 96.006  115.491 157.115 1.00 41.22  ? 1261 GLY A C     1 
ATOM   9569  O  O     . GLY A 1  1261 ? 95.887  114.402 157.682 1.00 42.53  ? 1261 GLY A O     1 
ATOM   9570  N  N     . ILE A 1  1262 ? 96.947  115.729 156.215 1.00 38.92  ? 1262 ILE A N     1 
ATOM   9571  C  CA    . ILE A 1  1262 ? 97.965  114.756 155.826 1.00 33.93  ? 1262 ILE A CA    1 
ATOM   9572  C  C     . ILE A 1  1262 ? 99.327  115.370 156.109 1.00 34.56  ? 1262 ILE A C     1 
ATOM   9573  O  O     . ILE A 1  1262 ? 99.575  116.506 155.694 1.00 37.10  ? 1262 ILE A O     1 
ATOM   9574  C  CB    . ILE A 1  1262 ? 97.847  114.366 154.340 1.00 37.60  ? 1262 ILE A CB    1 
ATOM   9575  C  CG1   . ILE A 1  1262 ? 96.486  113.736 154.048 1.00 35.45  ? 1262 ILE A CG1   1 
ATOM   9576  C  CG2   . ILE A 1  1262 ? 98.953  113.414 153.945 1.00 39.16  ? 1262 ILE A CG2   1 
ATOM   9577  C  CD1   . ILE A 1  1262 ? 96.119  113.743 152.591 1.00 33.55  ? 1262 ILE A CD1   1 
ATOM   9578  N  N     . PRO A 1  1263 ? 100.226 114.674 156.802 1.00 29.15  ? 1263 PRO A N     1 
ATOM   9579  C  CA    . PRO A 1  1263 ? 101.525 115.271 157.128 1.00 30.26  ? 1263 PRO A CA    1 
ATOM   9580  C  C     . PRO A 1  1263 ? 102.303 115.637 155.875 1.00 35.12  ? 1263 PRO A C     1 
ATOM   9581  O  O     . PRO A 1  1263 ? 102.241 114.946 154.857 1.00 35.46  ? 1263 PRO A O     1 
ATOM   9582  C  CB    . PRO A 1  1263 ? 102.233 114.169 157.923 1.00 27.97  ? 1263 PRO A CB    1 
ATOM   9583  C  CG    . PRO A 1  1263 ? 101.155 113.280 158.393 1.00 31.85  ? 1263 PRO A CG    1 
ATOM   9584  C  CD    . PRO A 1  1263 ? 100.095 113.316 157.344 1.00 28.71  ? 1263 PRO A CD    1 
ATOM   9585  N  N     . GLY A 1  1264 ? 103.034 116.742 155.952 1.00 32.42  ? 1264 GLY A N     1 
ATOM   9586  C  CA    . GLY A 1  1264 ? 103.808 117.223 154.839 1.00 26.51  ? 1264 GLY A CA    1 
ATOM   9587  C  C     . GLY A 1  1264 ? 103.055 118.107 153.871 1.00 30.60  ? 1264 GLY A C     1 
ATOM   9588  O  O     . GLY A 1  1264 ? 103.665 118.634 152.940 1.00 36.13  ? 1264 GLY A O     1 
ATOM   9589  N  N     . ILE A 1  1265 ? 101.749 118.285 154.057 1.00 33.25  ? 1265 ILE A N     1 
ATOM   9590  C  CA    . ILE A 1  1265 ? 100.956 119.162 153.196 1.00 35.56  ? 1265 ILE A CA    1 
ATOM   9591  C  C     . ILE A 1  1265 ? 100.769 120.468 153.962 1.00 36.36  ? 1265 ILE A C     1 
ATOM   9592  O  O     . ILE A 1  1265 ? 100.096 120.526 154.985 1.00 42.34  ? 1265 ILE A O     1 
ATOM   9593  C  CB    . ILE A 1  1265 ? 99.635  118.522 152.784 1.00 34.06  ? 1265 ILE A CB    1 
ATOM   9594  C  CG1   . ILE A 1  1265 ? 99.859  117.590 151.594 1.00 38.88  ? 1265 ILE A CG1   1 
ATOM   9595  C  CG2   . ILE A 1  1265 ? 98.632  119.569 152.397 1.00 34.64  ? 1265 ILE A CG2   1 
ATOM   9596  C  CD1   . ILE A 1  1265 ? 99.006  116.348 151.597 1.00 35.85  ? 1265 ILE A CD1   1 
ATOM   9597  N  N     . LYS A 1  1266 ? 101.387 121.534 153.455 1.00 33.89  ? 1266 LYS A N     1 
ATOM   9598  C  CA    . LYS A 1  1266 ? 101.381 122.800 154.178 1.00 33.16  ? 1266 LYS A CA    1 
ATOM   9599  C  C     . LYS A 1  1266 ? 100.239 123.697 153.712 1.00 34.62  ? 1266 LYS A C     1 
ATOM   9600  O  O     . LYS A 1  1266 ? 99.587  124.358 154.525 1.00 41.04  ? 1266 LYS A O     1 
ATOM   9601  C  CB    . LYS A 1  1266 ? 102.736 123.492 154.021 1.00 32.75  ? 1266 LYS A CB    1 
ATOM   9602  C  CG    . LYS A 1  1266 ? 102.660 124.989 153.861 1.00 36.02  ? 1266 LYS A CG    1 
ATOM   9603  C  CD    . LYS A 1  1266 ? 103.968 125.668 154.232 1.00 40.14  ? 1266 LYS A CD    1 
ATOM   9604  C  CE    . LYS A 1  1266 ? 104.971 125.637 153.094 1.00 38.73  ? 1266 LYS A CE    1 
ATOM   9605  N  NZ    . LYS A 1  1266 ? 104.728 126.742 152.124 1.00 37.08  ? 1266 LYS A NZ    1 
ATOM   9606  N  N     . ASN A 1  1267 ? 99.988  123.740 152.408 1.00 33.70  ? 1267 ASN A N     1 
ATOM   9607  C  CA    . ASN A 1  1267 ? 98.858  124.454 151.824 1.00 35.91  ? 1267 ASN A CA    1 
ATOM   9608  C  C     . ASN A 1  1267 ? 98.029  123.477 151.010 1.00 35.69  ? 1267 ASN A C     1 
ATOM   9609  O  O     . ASN A 1  1267 ? 98.389  122.312 150.854 1.00 38.39  ? 1267 ASN A O     1 
ATOM   9610  C  CB    . ASN A 1  1267 ? 99.315  125.622 150.941 1.00 35.24  ? 1267 ASN A CB    1 
ATOM   9611  C  CG    . ASN A 1  1267 ? 100.172 126.617 151.684 1.00 38.89  ? 1267 ASN A CG    1 
ATOM   9612  O  OD1   . ASN A 1  1267 ? 100.298 126.550 152.897 1.00 37.63  ? 1267 ASN A OD1   1 
ATOM   9613  N  ND2   . ASN A 1  1267 ? 100.774 127.544 150.953 1.00 36.89  ? 1267 ASN A ND2   1 
ATOM   9614  N  N     . ALA A 1  1268 ? 96.886  123.947 150.519 1.00 28.08  ? 1268 ALA A N     1 
ATOM   9615  C  CA    . ALA A 1  1268 ? 96.153  123.222 149.489 1.00 25.39  ? 1268 ALA A CA    1 
ATOM   9616  C  C     . ALA A 1  1268 ? 95.147  124.127 148.795 1.00 25.79  ? 1268 ALA A C     1 
ATOM   9617  O  O     . ALA A 1  1268 ? 94.047  124.340 149.310 1.00 34.93  ? 1268 ALA A O     1 
ATOM   9618  C  CB    . ALA A 1  1268 ? 95.442  122.008 150.084 1.00 26.01  ? 1268 ALA A CB    1 
ATOM   9619  N  N     . ASN A 1  1269 ? 95.476  124.612 147.606 1.00 24.03  ? 1269 ASN A N     1 
ATOM   9620  C  CA    . ASN A 1  1269 ? 94.608  125.519 146.874 1.00 25.33  ? 1269 ASN A CA    1 
ATOM   9621  C  C     . ASN A 1  1269 ? 93.801  124.748 145.845 1.00 29.91  ? 1269 ASN A C     1 
ATOM   9622  O  O     . ASN A 1  1269 ? 94.047  123.570 145.587 1.00 36.81  ? 1269 ASN A O     1 
ATOM   9623  C  CB    . ASN A 1  1269 ? 95.408  126.618 146.183 1.00 26.30  ? 1269 ASN A CB    1 
ATOM   9624  C  CG    . ASN A 1  1269 ? 96.238  127.421 147.150 1.00 32.54  ? 1269 ASN A CG    1 
ATOM   9625  O  OD1   . ASN A 1  1269 ? 96.647  126.921 148.195 1.00 34.02  ? 1269 ASN A OD1   1 
ATOM   9626  N  ND2   . ASN A 1  1269 ? 96.508  128.669 146.802 1.00 31.98  ? 1269 ASN A ND2   1 
ATOM   9627  N  N     . VAL A 1  1270 ? 92.817  125.422 145.272 1.00 26.22  ? 1270 VAL A N     1 
ATOM   9628  C  CA    . VAL A 1  1270 ? 91.920  124.828 144.290 1.00 28.91  ? 1270 VAL A CA    1 
ATOM   9629  C  C     . VAL A 1  1270 ? 92.244  125.423 142.930 1.00 32.68  ? 1270 VAL A C     1 
ATOM   9630  O  O     . VAL A 1  1270 ? 92.340  126.647 142.789 1.00 37.67  ? 1270 VAL A O     1 
ATOM   9631  C  CB    . VAL A 1  1270 ? 90.448  125.063 144.669 1.00 26.07  ? 1270 VAL A CB    1 
ATOM   9632  C  CG1   . VAL A 1  1270 ? 89.531  124.618 143.555 1.00 27.51  ? 1270 VAL A CG1   1 
ATOM   9633  C  CG2   . VAL A 1  1270 ? 90.123  124.321 145.933 1.00 26.19  ? 1270 VAL A CG2   1 
ATOM   9634  N  N     . VAL A 1  1271 ? 92.439  124.563 141.935 1.00 27.04  ? 1271 VAL A N     1 
ATOM   9635  C  CA    . VAL A 1  1271 ? 92.834  125.003 140.607 1.00 26.68  ? 1271 VAL A CA    1 
ATOM   9636  C  C     . VAL A 1  1271 ? 91.885  124.399 139.581 1.00 27.03  ? 1271 VAL A C     1 
ATOM   9637  O  O     . VAL A 1  1271 ? 91.262  123.361 139.805 1.00 31.26  ? 1271 VAL A O     1 
ATOM   9638  C  CB    . VAL A 1  1271 ? 94.305  124.644 140.287 1.00 29.85  ? 1271 VAL A CB    1 
ATOM   9639  C  CG1   . VAL A 1  1271 ? 95.206  124.966 141.463 1.00 25.39  ? 1271 VAL A CG1   1 
ATOM   9640  C  CG2   . VAL A 1  1271 ? 94.439  123.176 139.925 1.00 31.09  ? 1271 VAL A CG2   1 
ATOM   9641  N  N     . LYS A 1  1272 ? 91.775  125.077 138.445 1.00 24.27  ? 1272 LYS A N     1 
ATOM   9642  C  CA    . LYS A 1  1272 ? 90.916  124.656 137.348 1.00 32.01  ? 1272 LYS A CA    1 
ATOM   9643  C  C     . LYS A 1  1272 ? 91.747  123.961 136.278 1.00 35.62  ? 1272 LYS A C     1 
ATOM   9644  O  O     . LYS A 1  1272 ? 92.708  124.537 135.760 1.00 35.67  ? 1272 LYS A O     1 
ATOM   9645  C  CB    . LYS A 1  1272 ? 90.183  125.851 136.740 1.00 34.67  ? 1272 LYS A CB    1 
ATOM   9646  C  CG    . LYS A 1  1272 ? 88.738  125.575 136.369 1.00 35.05  ? 1272 LYS A CG    1 
ATOM   9647  C  CD    . LYS A 1  1272 ? 88.078  126.815 135.798 1.00 34.46  ? 1272 LYS A CD    1 
ATOM   9648  C  CE    . LYS A 1  1272 ? 86.570  126.673 135.758 1.00 34.76  ? 1272 LYS A CE    1 
ATOM   9649  N  NZ    . LYS A 1  1272 ? 85.889  127.566 136.736 1.00 31.29  ? 1272 LYS A NZ    1 
ATOM   9650  N  N     . LEU A 1  1273 ? 91.370  122.734 135.940 1.00 30.33  ? 1273 LEU A N     1 
ATOM   9651  C  CA    . LEU A 1  1273 ? 92.135  121.910 135.023 1.00 26.71  ? 1273 LEU A CA    1 
ATOM   9652  C  C     . LEU A 1  1273 ? 91.457  121.826 133.667 1.00 29.80  ? 1273 LEU A C     1 
ATOM   9653  O  O     . LEU A 1  1273 ? 90.245  122.008 133.541 1.00 32.74  ? 1273 LEU A O     1 
ATOM   9654  C  CB    . LEU A 1  1273 ? 92.317  120.496 135.564 1.00 28.26  ? 1273 LEU A CB    1 
ATOM   9655  C  CG    . LEU A 1  1273 ? 93.089  120.361 136.860 1.00 29.99  ? 1273 LEU A CG    1 
ATOM   9656  C  CD1   . LEU A 1  1273 ? 93.242  118.897 137.168 1.00 28.25  ? 1273 LEU A CD1   1 
ATOM   9657  C  CD2   . LEU A 1  1273 ? 94.423  121.054 136.752 1.00 27.54  ? 1273 LEU A CD2   1 
ATOM   9658  N  N     . MET A 1  1274 ? 92.256  121.527 132.659 1.00 33.05  ? 1274 MET A N     1 
ATOM   9659  C  CA    . MET A 1  1274 ? 91.769  121.279 131.313 1.00 33.67  ? 1274 MET A CA    1 
ATOM   9660  C  C     . MET A 1  1274 ? 92.117  119.842 130.951 1.00 31.60  ? 1274 MET A C     1 
ATOM   9661  O  O     . MET A 1  1274 ? 93.294  119.476 130.927 1.00 37.58  ? 1274 MET A O     1 
ATOM   9662  C  CB    . MET A 1  1274 ? 92.403  122.262 130.334 1.00 32.52  ? 1274 MET A CB    1 
ATOM   9663  C  CG    . MET A 1  1274 ? 91.654  122.441 129.048 1.00 35.01  ? 1274 MET A CG    1 
ATOM   9664  S  SD    . MET A 1  1274 ? 92.414  123.739 128.064 1.00 52.78  ? 1274 MET A SD    1 
ATOM   9665  C  CE    . MET A 1  1274 ? 92.503  125.054 129.273 1.00 37.01  ? 1274 MET A CE    1 
ATOM   9666  N  N     . ARG A 1  1275 ? 91.101  119.025 130.702 1.00 20.96  ? 1275 ARG A N     1 
ATOM   9667  C  CA    . ARG A 1  1275 ? 91.307  117.619 130.399 1.00 23.47  ? 1275 ARG A CA    1 
ATOM   9668  C  C     . ARG A 1  1275 ? 90.397  117.214 129.251 1.00 24.07  ? 1275 ARG A C     1 
ATOM   9669  O  O     . ARG A 1  1275 ? 89.357  117.826 129.024 1.00 31.41  ? 1275 ARG A O     1 
ATOM   9670  C  CB    . ARG A 1  1275 ? 91.041  116.737 131.623 1.00 21.25  ? 1275 ARG A CB    1 
ATOM   9671  C  CG    . ARG A 1  1275 ? 92.007  116.940 132.775 1.00 22.50  ? 1275 ARG A CG    1 
ATOM   9672  C  CD    . ARG A 1  1275 ? 93.401  116.450 132.434 1.00 24.96  ? 1275 ARG A CD    1 
ATOM   9673  N  NE    . ARG A 1  1275 ? 94.292  116.478 133.585 1.00 21.76  ? 1275 ARG A NE    1 
ATOM   9674  C  CZ    . ARG A 1  1275 ? 95.028  117.522 133.932 1.00 23.03  ? 1275 ARG A CZ    1 
ATOM   9675  N  NH1   . ARG A 1  1275 ? 95.008  118.641 133.236 1.00 23.82  ? 1275 ARG A NH1   1 
ATOM   9676  N  NH2   . ARG A 1  1275 ? 95.806  117.439 135.004 1.00 18.05  ? 1275 ARG A NH2   1 
ATOM   9677  N  N     . HIS A 1  1276 ? 90.797  116.183 128.523 1.00 20.86  ? 1276 HIS A N     1 
ATOM   9678  C  CA    . HIS A 1  1276 ? 89.962  115.635 127.469 1.00 22.30  ? 1276 HIS A CA    1 
ATOM   9679  C  C     . HIS A 1  1276 ? 89.133  114.467 127.983 1.00 24.44  ? 1276 HIS A C     1 
ATOM   9680  O  O     . HIS A 1  1276 ? 89.460  113.831 128.985 1.00 29.65  ? 1276 HIS A O     1 
ATOM   9681  C  CB    . HIS A 1  1276 ? 90.794  115.186 126.270 1.00 22.07  ? 1276 HIS A CB    1 
ATOM   9682  C  CG    . HIS A 1  1276 ? 91.292  116.309 125.422 1.00 23.43  ? 1276 HIS A CG    1 
ATOM   9683  N  ND1   . HIS A 1  1276 ? 92.354  117.106 125.784 1.00 22.68  ? 1276 HIS A ND1   1 
ATOM   9684  C  CD2   . HIS A 1  1276 ? 90.863  116.773 124.227 1.00 25.53  ? 1276 HIS A CD2   1 
ATOM   9685  C  CE1   . HIS A 1  1276 ? 92.561  118.009 124.845 1.00 22.54  ? 1276 HIS A CE1   1 
ATOM   9686  N  NE2   . HIS A 1  1276 ? 91.670  117.828 123.890 1.00 27.00  ? 1276 HIS A NE2   1 
ATOM   9687  N  N     . ARG A 1  1277 ? 88.041  114.196 127.277 1.00 26.22  ? 1277 ARG A N     1 
ATOM   9688  C  CA    . ARG A 1  1277 ? 87.164  113.089 127.613 1.00 25.15  ? 1277 ARG A CA    1 
ATOM   9689  C  C     . ARG A 1  1277 ? 86.376  112.709 126.372 1.00 28.35  ? 1277 ARG A C     1 
ATOM   9690  O  O     . ARG A 1  1277 ? 86.102  113.553 125.519 1.00 30.75  ? 1277 ARG A O     1 
ATOM   9691  C  CB    . ARG A 1  1277 ? 86.231  113.458 128.766 1.00 25.98  ? 1277 ARG A CB    1 
ATOM   9692  C  CG    . ARG A 1  1277 ? 85.491  112.288 129.379 1.00 31.04  ? 1277 ARG A CG    1 
ATOM   9693  C  CD    . ARG A 1  1277 ? 84.905  112.682 130.715 1.00 32.73  ? 1277 ARG A CD    1 
ATOM   9694  N  NE    . ARG A 1  1277 ? 85.953  113.043 131.660 1.00 32.15  ? 1277 ARG A NE    1 
ATOM   9695  C  CZ    . ARG A 1  1277 ? 85.748  113.685 132.800 1.00 34.16  ? 1277 ARG A CZ    1 
ATOM   9696  N  NH1   . ARG A 1  1277 ? 84.538  114.058 133.175 1.00 33.22  ? 1277 ARG A NH1   1 
ATOM   9697  N  NH2   . ARG A 1  1277 ? 86.784  113.961 133.583 1.00 32.54  ? 1277 ARG A NH2   1 
ATOM   9698  N  N     . VAL A 1  1278 ? 86.023  111.436 126.276 1.00 25.42  ? 1278 VAL A N     1 
ATOM   9699  C  CA    . VAL A 1  1278 ? 85.289  110.918 125.128 1.00 28.14  ? 1278 VAL A CA    1 
ATOM   9700  C  C     . VAL A 1  1278 ? 83.802  110.909 125.456 1.00 29.94  ? 1278 VAL A C     1 
ATOM   9701  O  O     . VAL A 1  1278 ? 83.393  110.420 126.514 1.00 34.66  ? 1278 VAL A O     1 
ATOM   9702  C  CB    . VAL A 1  1278 ? 85.785  109.514 124.748 1.00 28.24  ? 1278 VAL A CB    1 
ATOM   9703  C  CG1   . VAL A 1  1278 ? 84.744  108.777 123.939 1.00 27.05  ? 1278 VAL A CG1   1 
ATOM   9704  C  CG2   . VAL A 1  1278 ? 87.079  109.611 123.971 1.00 28.43  ? 1278 VAL A CG2   1 
ATOM   9705  N  N     . ASP A 1  1279 ? 82.993  111.456 124.553 1.00 33.06  ? 1279 ASP A N     1 
ATOM   9706  C  CA    . ASP A 1  1279 ? 81.565  111.599 124.793 1.00 32.27  ? 1279 ASP A CA    1 
ATOM   9707  C  C     . ASP A 1  1279 ? 80.832  110.286 124.542 1.00 34.87  ? 1279 ASP A C     1 
ATOM   9708  O  O     . ASP A 1  1279 ? 81.426  109.245 124.253 1.00 35.80  ? 1279 ASP A O     1 
ATOM   9709  C  CB    . ASP A 1  1279 ? 80.980  112.688 123.906 1.00 33.95  ? 1279 ASP A CB    1 
ATOM   9710  C  CG    . ASP A 1  1279 ? 81.388  114.061 124.340 1.00 38.18  ? 1279 ASP A CG    1 
ATOM   9711  O  OD1   . ASP A 1  1279 ? 81.962  114.182 125.442 1.00 37.94  ? 1279 ASP A OD1   1 
ATOM   9712  O  OD2   . ASP A 1  1279 ? 81.125  115.017 123.586 1.00 35.65  ? 1279 ASP A OD2   1 
ATOM   9713  N  N     . ALA A 1  1280 ? 79.507  110.349 124.669 1.00 36.43  ? 1280 ALA A N     1 
ATOM   9714  C  CA    . ALA A 1  1280 ? 78.669  109.206 124.346 1.00 37.38  ? 1280 ALA A CA    1 
ATOM   9715  C  C     . ALA A 1  1280 ? 78.527  109.014 122.847 1.00 37.41  ? 1280 ALA A C     1 
ATOM   9716  O  O     . ALA A 1  1280 ? 78.230  107.901 122.402 1.00 37.07  ? 1280 ALA A O     1 
ATOM   9717  C  CB    . ALA A 1  1280 ? 77.296  109.365 124.990 1.00 36.18  ? 1280 ALA A CB    1 
ATOM   9718  N  N     . GLN A 1  1281 ? 78.730  110.070 122.064 1.00 38.74  ? 1281 GLN A N     1 
ATOM   9719  C  CA    . GLN A 1  1281 ? 78.721  109.992 120.611 1.00 39.21  ? 1281 GLN A CA    1 
ATOM   9720  C  C     . GLN A 1  1281 ? 80.073  109.599 120.040 1.00 40.08  ? 1281 GLN A C     1 
ATOM   9721  O  O     . GLN A 1  1281 ? 80.186  109.419 118.826 1.00 40.28  ? 1281 GLN A O     1 
ATOM   9722  C  CB    . GLN A 1  1281 ? 78.287  111.331 120.014 1.00 37.58  ? 1281 GLN A CB    1 
ATOM   9723  C  CG    . GLN A 1  1281 ? 76.793  111.534 119.997 1.00 37.92  ? 1281 GLN A CG    1 
ATOM   9724  C  CD    . GLN A 1  1281 ? 76.250  111.849 121.373 1.00 42.49  ? 1281 GLN A CD    1 
ATOM   9725  O  OE1   . GLN A 1  1281 ? 75.476  111.075 121.940 1.00 44.00  ? 1281 GLN A OE1   1 
ATOM   9726  N  NE2   . GLN A 1  1281 ? 76.654  112.988 121.923 1.00 39.43  ? 1281 GLN A NE2   1 
ATOM   9727  N  N     . GLY A 1  1282 ? 81.095  109.465 120.884 1.00 36.26  ? 1282 GLY A N     1 
ATOM   9728  C  CA    . GLY A 1  1282 ? 82.421  109.086 120.455 1.00 32.27  ? 1282 GLY A CA    1 
ATOM   9729  C  C     . GLY A 1  1282 ? 83.338  110.225 120.081 1.00 32.17  ? 1282 GLY A C     1 
ATOM   9730  O  O     . GLY A 1  1282 ? 84.366  109.978 119.446 1.00 32.90  ? 1282 GLY A O     1 
ATOM   9731  N  N     . LYS A 1  1283 ? 83.000  111.457 120.437 1.00 31.54  ? 1283 LYS A N     1 
ATOM   9732  C  CA    . LYS A 1  1283 ? 83.862  112.591 120.153 1.00 30.27  ? 1283 LYS A CA    1 
ATOM   9733  C  C     . LYS A 1  1283 ? 84.777  112.871 121.332 1.00 29.81  ? 1283 LYS A C     1 
ATOM   9734  O  O     . LYS A 1  1283 ? 84.430  112.608 122.483 1.00 33.61  ? 1283 LYS A O     1 
ATOM   9735  C  CB    . LYS A 1  1283 ? 83.036  113.834 119.841 1.00 29.11  ? 1283 LYS A CB    1 
ATOM   9736  C  CG    . LYS A 1  1283 ? 83.532  114.606 118.639 1.00 30.26  ? 1283 LYS A CG    1 
ATOM   9737  C  CD    . LYS A 1  1283 ? 82.593  115.724 118.275 1.00 30.71  ? 1283 LYS A CD    1 
ATOM   9738  C  CE    . LYS A 1  1283 ? 82.460  116.706 119.417 1.00 32.40  ? 1283 LYS A CE    1 
ATOM   9739  N  NZ    . LYS A 1  1283 ? 83.782  117.229 119.837 1.00 29.88  ? 1283 LYS A NZ    1 
ATOM   9740  N  N     . LEU A 1  1284 ? 85.948  113.409 121.040 1.00 25.35  ? 1284 LEU A N     1 
ATOM   9741  C  CA    . LEU A 1  1284 ? 86.916  113.778 122.061 1.00 27.42  ? 1284 LEU A CA    1 
ATOM   9742  C  C     . LEU A 1  1284 ? 86.776  115.272 122.321 1.00 26.61  ? 1284 LEU A C     1 
ATOM   9743  O  O     . LEU A 1  1284 ? 87.067  116.090 121.444 1.00 33.04  ? 1284 LEU A O     1 
ATOM   9744  C  CB    . LEU A 1  1284 ? 88.327  113.410 121.614 1.00 25.54  ? 1284 LEU A CB    1 
ATOM   9745  C  CG    . LEU A 1  1284 ? 89.446  113.587 122.629 1.00 24.69  ? 1284 LEU A CG    1 
ATOM   9746  C  CD1   . LEU A 1  1284 ? 89.433  112.452 123.620 1.00 27.22  ? 1284 LEU A CD1   1 
ATOM   9747  C  CD2   . LEU A 1  1284 ? 90.763  113.646 121.913 1.00 25.56  ? 1284 LEU A CD2   1 
ATOM   9748  N  N     . VAL A 1  1285 ? 86.324  115.628 123.517 1.00 24.97  ? 1285 VAL A N     1 
ATOM   9749  C  CA    . VAL A 1  1285 ? 86.035  117.014 123.858 1.00 30.29  ? 1285 VAL A CA    1 
ATOM   9750  C  C     . VAL A 1  1285 ? 86.947  117.450 124.990 1.00 28.19  ? 1285 VAL A C     1 
ATOM   9751  O  O     . VAL A 1  1285 ? 87.461  116.631 125.755 1.00 33.57  ? 1285 VAL A O     1 
ATOM   9752  C  CB    . VAL A 1  1285 ? 84.556  117.219 124.245 1.00 33.21  ? 1285 VAL A CB    1 
ATOM   9753  C  CG1   . VAL A 1  1285 ? 83.654  116.800 123.116 1.00 27.92  ? 1285 VAL A CG1   1 
ATOM   9754  C  CG2   . VAL A 1  1285 ? 84.226  116.453 125.506 1.00 30.83  ? 1285 VAL A CG2   1 
ATOM   9755  N  N     . ARG A 1  1286 ? 87.136  118.754 125.100 1.00 31.10  ? 1286 ARG A N     1 
ATOM   9756  C  CA    . ARG A 1  1286 ? 88.020  119.340 126.096 1.00 32.96  ? 1286 ARG A CA    1 
ATOM   9757  C  C     . ARG A 1  1286 ? 87.173  119.974 127.192 1.00 38.39  ? 1286 ARG A C     1 
ATOM   9758  O  O     . ARG A 1  1286 ? 86.418  120.915 126.936 1.00 42.29  ? 1286 ARG A O     1 
ATOM   9759  C  CB    . ARG A 1  1286 ? 88.937  120.373 125.458 1.00 31.57  ? 1286 ARG A CB    1 
ATOM   9760  C  CG    . ARG A 1  1286 ? 89.993  120.870 126.390 1.00 36.37  ? 1286 ARG A CG    1 
ATOM   9761  C  CD    . ARG A 1  1286 ? 91.061  121.595 125.627 1.00 39.58  ? 1286 ARG A CD    1 
ATOM   9762  N  NE    . ARG A 1  1286 ? 90.484  122.707 124.888 1.00 35.97  ? 1286 ARG A NE    1 
ATOM   9763  C  CZ    . ARG A 1  1286 ? 91.048  123.897 124.764 1.00 36.78  ? 1286 ARG A CZ    1 
ATOM   9764  N  NH1   . ARG A 1  1286 ? 92.203  124.176 125.340 1.00 36.35  ? 1286 ARG A NH1   1 
ATOM   9765  N  NH2   . ARG A 1  1286 ? 90.432  124.834 124.050 1.00 40.16  ? 1286 ARG A NH2   1 
ATOM   9766  N  N     . LEU A 1  1287 ? 87.296  119.462 128.408 1.00 33.91  ? 1287 LEU A N     1 
ATOM   9767  C  CA    . LEU A 1  1287 ? 86.494  119.955 129.513 1.00 31.66  ? 1287 LEU A CA    1 
ATOM   9768  C  C     . LEU A 1  1287 ? 87.301  120.935 130.348 1.00 33.25  ? 1287 LEU A C     1 
ATOM   9769  O  O     . LEU A 1  1287 ? 88.349  120.582 130.891 1.00 33.67  ? 1287 LEU A O     1 
ATOM   9770  C  CB    . LEU A 1  1287 ? 86.019  118.794 130.374 1.00 29.36  ? 1287 LEU A CB    1 
ATOM   9771  C  CG    . LEU A 1  1287 ? 85.239  117.740 129.606 1.00 32.81  ? 1287 LEU A CG    1 
ATOM   9772  C  CD1   . LEU A 1  1287 ? 85.130  116.483 130.438 1.00 35.13  ? 1287 LEU A CD1   1 
ATOM   9773  C  CD2   . LEU A 1  1287 ? 83.873  118.260 129.211 1.00 34.02  ? 1287 LEU A CD2   1 
ATOM   9774  N  N     . ASP A 1  1288 ? 86.794  122.161 130.471 1.00 38.13  ? 1288 ASP A N     1 
ATOM   9775  C  CA    . ASP A 1  1288 ? 87.503  123.220 131.167 1.00 36.19  ? 1288 ASP A CA    1 
ATOM   9776  C  C     . ASP A 1  1288 ? 86.972  123.487 132.566 1.00 41.45  ? 1288 ASP A C     1 
ATOM   9777  O  O     . ASP A 1  1288 ? 87.581  124.270 133.301 1.00 40.39  ? 1288 ASP A O     1 
ATOM   9778  C  CB    . ASP A 1  1288 ? 87.445  124.511 130.349 1.00 38.44  ? 1288 ASP A CB    1 
ATOM   9779  C  CG    . ASP A 1  1288 ? 87.935  124.319 128.928 1.00 45.89  ? 1288 ASP A CG    1 
ATOM   9780  O  OD1   . ASP A 1  1288 ? 87.779  125.244 128.104 1.00 46.31  ? 1288 ASP A OD1   1 
ATOM   9781  O  OD2   . ASP A 1  1288 ? 88.477  123.240 128.632 1.00 47.10  ? 1288 ASP A OD2   1 
ATOM   9782  N  N     . ASN A 1  1289 ? 85.858  122.871 132.945 1.00 40.84  ? 1289 ASN A N     1 
ATOM   9783  C  CA    . ASN A 1  1289 ? 85.258  123.083 134.261 1.00 37.94  ? 1289 ASN A CA    1 
ATOM   9784  C  C     . ASN A 1  1289 ? 85.567  121.915 135.196 1.00 40.83  ? 1289 ASN A C     1 
ATOM   9785  O  O     . ASN A 1  1289 ? 84.685  121.198 135.653 1.00 42.03  ? 1289 ASN A O     1 
ATOM   9786  C  CB    . ASN A 1  1289 ? 83.756  123.302 134.117 1.00 36.99  ? 1289 ASN A CB    1 
ATOM   9787  C  CG    . ASN A 1  1289 ? 83.098  122.273 133.220 1.00 38.13  ? 1289 ASN A CG    1 
ATOM   9788  O  OD1   . ASN A 1  1289 ? 83.024  121.093 133.557 1.00 40.88  ? 1289 ASN A OD1   1 
ATOM   9789  N  ND2   . ASN A 1  1289 ? 82.640  122.712 132.059 1.00 39.04  ? 1289 ASN A ND2   1 
ATOM   9790  N  N     . ILE A 1  1290 ? 86.851  121.731 135.487 1.00 38.85  ? 1290 ILE A N     1 
ATOM   9791  C  CA    . ILE A 1  1290 ? 87.312  120.675 136.379 1.00 35.34  ? 1290 ILE A CA    1 
ATOM   9792  C  C     . ILE A 1  1290 ? 88.136  121.316 137.480 1.00 33.91  ? 1290 ILE A C     1 
ATOM   9793  O  O     . ILE A 1  1290 ? 89.070  122.070 137.199 1.00 35.70  ? 1290 ILE A O     1 
ATOM   9794  C  CB    . ILE A 1  1290 ? 88.132  119.609 135.630 1.00 33.70  ? 1290 ILE A CB    1 
ATOM   9795  C  CG1   . ILE A 1  1290 ? 87.258  118.887 134.607 1.00 34.08  ? 1290 ILE A CG1   1 
ATOM   9796  C  CG2   . ILE A 1  1290 ? 88.722  118.611 136.601 1.00 33.79  ? 1290 ILE A CG2   1 
ATOM   9797  C  CD1   . ILE A 1  1290 ? 88.030  118.095 133.610 1.00 33.18  ? 1290 ILE A CD1   1 
ATOM   9798  N  N     . TYR A 1  1291 ? 87.788  121.024 138.725 1.00 36.04  ? 1291 TYR A N     1 
ATOM   9799  C  CA    . TYR A 1  1291 ? 88.494  121.563 139.872 1.00 38.28  ? 1291 TYR A CA    1 
ATOM   9800  C  C     . TYR A 1  1291 ? 89.325  120.472 140.525 1.00 37.79  ? 1291 TYR A C     1 
ATOM   9801  O  O     . TYR A 1  1291 ? 88.946  119.298 140.535 1.00 39.55  ? 1291 TYR A O     1 
ATOM   9802  C  CB    . TYR A 1  1291 ? 87.522  122.169 140.891 1.00 41.35  ? 1291 TYR A CB    1 
ATOM   9803  C  CG    . TYR A 1  1291 ? 86.904  123.459 140.418 1.00 41.31  ? 1291 TYR A CG    1 
ATOM   9804  C  CD1   . TYR A 1  1291 ? 87.580  124.654 140.553 1.00 39.41  ? 1291 TYR A CD1   1 
ATOM   9805  C  CD2   . TYR A 1  1291 ? 85.657  123.475 139.813 1.00 38.92  ? 1291 TYR A CD2   1 
ATOM   9806  C  CE1   . TYR A 1  1291 ? 87.033  125.828 140.109 1.00 41.58  ? 1291 TYR A CE1   1 
ATOM   9807  C  CE2   . TYR A 1  1291 ? 85.102  124.646 139.366 1.00 39.20  ? 1291 TYR A CE2   1 
ATOM   9808  C  CZ    . TYR A 1  1291 ? 85.796  125.820 139.519 1.00 41.95  ? 1291 TYR A CZ    1 
ATOM   9809  O  OH    . TYR A 1  1291 ? 85.254  127.000 139.082 1.00 41.41  ? 1291 TYR A OH    1 
ATOM   9810  N  N     . ALA A 1  1292 ? 90.469  120.871 141.067 1.00 29.05  ? 1292 ALA A N     1 
ATOM   9811  C  CA    . ALA A 1  1292 ? 91.399  119.929 141.661 1.00 30.17  ? 1292 ALA A CA    1 
ATOM   9812  C  C     . ALA A 1  1292 ? 92.222  120.666 142.705 1.00 25.86  ? 1292 ALA A C     1 
ATOM   9813  O  O     . ALA A 1  1292 ? 92.236  121.898 142.752 1.00 28.14  ? 1292 ALA A O     1 
ATOM   9814  C  CB    . ALA A 1  1292 ? 92.269  119.284 140.575 1.00 33.35  ? 1292 ALA A CB    1 
ATOM   9815  N  N     . ILE A 1  1293 ? 92.927  119.911 143.535 1.00 16.11  ? 1293 ILE A N     1 
ATOM   9816  C  CA    . ILE A 1  1293 ? 93.669  120.463 144.658 1.00 23.07  ? 1293 ILE A CA    1 
ATOM   9817  C  C     . ILE A 1  1293 ? 95.153  120.362 144.355 1.00 25.55  ? 1293 ILE A C     1 
ATOM   9818  O  O     . ILE A 1  1293 ? 95.654  119.281 144.031 1.00 30.04  ? 1293 ILE A O     1 
ATOM   9819  C  CB    . ILE A 1  1293 ? 93.323  119.741 145.970 1.00 25.98  ? 1293 ILE A CB    1 
ATOM   9820  C  CG1   . ILE A 1  1293 ? 91.866  120.011 146.345 1.00 24.84  ? 1293 ILE A CG1   1 
ATOM   9821  C  CG2   . ILE A 1  1293 ? 94.257  120.177 147.079 1.00 23.20  ? 1293 ILE A CG2   1 
ATOM   9822  C  CD1   . ILE A 1  1293 ? 91.014  118.780 146.422 1.00 23.84  ? 1293 ILE A CD1   1 
ATOM   9823  N  N     . LYS A 1  1294 ? 95.852  121.486 144.455 1.00 18.75  ? 1294 LYS A N     1 
ATOM   9824  C  CA    . LYS A 1  1294 ? 97.288  121.553 144.213 1.00 22.54  ? 1294 LYS A CA    1 
ATOM   9825  C  C     . LYS A 1  1294 ? 97.962  121.857 145.543 1.00 24.35  ? 1294 LYS A C     1 
ATOM   9826  O  O     . LYS A 1  1294 ? 98.132  123.020 145.912 1.00 27.36  ? 1294 LYS A O     1 
ATOM   9827  C  CB    . LYS A 1  1294 ? 97.619  122.602 143.158 1.00 23.38  ? 1294 LYS A CB    1 
ATOM   9828  C  CG    . LYS A 1  1294 ? 99.094  122.709 142.843 1.00 25.05  ? 1294 LYS A CG    1 
ATOM   9829  C  CD    . LYS A 1  1294 ? 99.364  123.724 141.751 1.00 24.40  ? 1294 LYS A CD    1 
ATOM   9830  C  CE    . LYS A 1  1294 ? 99.810  123.061 140.458 1.00 26.12  ? 1294 LYS A CE    1 
ATOM   9831  N  NZ    . LYS A 1  1294 ? 98.684  122.464 139.691 1.00 27.44  ? 1294 LYS A NZ    1 
ATOM   9832  N  N     . THR A 1  1295 ? 98.363  120.818 146.259 1.00 22.93  ? 1295 THR A N     1 
ATOM   9833  C  CA    . THR A 1  1295 ? 98.934  121.034 147.571 1.00 25.15  ? 1295 THR A CA    1 
ATOM   9834  C  C     . THR A 1  1295 ? 100.326 121.639 147.450 1.00 26.76  ? 1295 THR A C     1 
ATOM   9835  O  O     . THR A 1  1295 ? 100.824 121.917 146.361 1.00 33.59  ? 1295 THR A O     1 
ATOM   9836  C  CB    . THR A 1  1295 ? 98.999  119.728 148.354 1.00 29.21  ? 1295 THR A CB    1 
ATOM   9837  O  OG1   . THR A 1  1295 ? 99.952  118.853 147.750 1.00 32.60  ? 1295 THR A OG1   1 
ATOM   9838  C  CG2   . THR A 1  1295 ? 97.653  119.054 148.327 1.00 26.70  ? 1295 THR A CG2   1 
ATOM   9839  N  N     . ASN A 1  1296 ? 100.948 121.858 148.599 1.00 28.31  ? 1296 ASN A N     1 
ATOM   9840  C  CA    . ASN A 1  1296 ? 102.293 122.409 148.698 1.00 26.81  ? 1296 ASN A CA    1 
ATOM   9841  C  C     . ASN A 1  1296 ? 103.065 121.445 149.593 1.00 30.69  ? 1296 ASN A C     1 
ATOM   9842  O  O     . ASN A 1  1296 ? 102.825 121.365 150.799 1.00 34.71  ? 1296 ASN A O     1 
ATOM   9843  C  CB    . ASN A 1  1296 ? 102.230 123.850 149.234 1.00 31.77  ? 1296 ASN A CB    1 
ATOM   9844  C  CG    . ASN A 1  1296 ? 103.536 124.340 149.823 1.00 37.12  ? 1296 ASN A CG    1 
ATOM   9845  O  OD1   . ASN A 1  1296 ? 104.128 123.716 150.697 1.00 36.98  ? 1296 ASN A OD1   1 
ATOM   9846  N  ND2   . ASN A 1  1296 ? 103.991 125.486 149.337 1.00 37.15  ? 1296 ASN A ND2   1 
ATOM   9847  N  N     . GLY A 1  1297 ? 103.995 120.706 149.001 1.00 31.72  ? 1297 GLY A N     1 
ATOM   9848  C  CA    . GLY A 1  1297 ? 104.628 119.603 149.693 1.00 30.97  ? 1297 GLY A CA    1 
ATOM   9849  C  C     . GLY A 1  1297 ? 104.109 118.294 149.144 1.00 32.65  ? 1297 GLY A C     1 
ATOM   9850  O  O     . GLY A 1  1297 ? 103.016 118.260 148.579 1.00 34.22  ? 1297 GLY A O     1 
ATOM   9851  N  N     . THR A 1  1298 ? 104.871 117.217 149.289 1.00 28.05  ? 1298 THR A N     1 
ATOM   9852  C  CA    . THR A 1  1298 ? 104.549 115.944 148.661 1.00 29.13  ? 1298 THR A CA    1 
ATOM   9853  C  C     . THR A 1  1298 ? 104.367 114.867 149.720 1.00 30.60  ? 1298 THR A C     1 
ATOM   9854  O  O     . THR A 1  1298 ? 105.237 114.679 150.575 1.00 32.41  ? 1298 THR A O     1 
ATOM   9855  C  CB    . THR A 1  1298 ? 105.647 115.524 147.679 1.00 29.90  ? 1298 THR A CB    1 
ATOM   9856  O  OG1   . THR A 1  1298 ? 105.515 116.260 146.460 1.00 27.42  ? 1298 THR A OG1   1 
ATOM   9857  C  CG2   . THR A 1  1298 ? 105.555 114.057 147.367 1.00 26.19  ? 1298 THR A CG2   1 
ATOM   9858  N  N     . ASN A 1  1299 ? 103.235 114.169 149.663 1.00 22.75  ? 1299 ASN A N     1 
ATOM   9859  C  CA    . ASN A 1  1299 ? 103.068 112.925 150.412 1.00 22.24  ? 1299 ASN A CA    1 
ATOM   9860  C  C     . ASN A 1  1299 ? 102.108 112.052 149.604 1.00 29.04  ? 1299 ASN A C     1 
ATOM   9861  O  O     . ASN A 1  1299 ? 100.890 112.160 149.745 1.00 33.83  ? 1299 ASN A O     1 
ATOM   9862  C  CB    . ASN A 1  1299 ? 102.554 113.180 151.817 1.00 24.85  ? 1299 ASN A CB    1 
ATOM   9863  C  CG    . ASN A 1  1299 ? 102.840 112.037 152.755 1.00 29.65  ? 1299 ASN A CG    1 
ATOM   9864  O  OD1   . ASN A 1  1299 ? 102.165 111.014 152.723 1.00 31.68  ? 1299 ASN A OD1   1 
ATOM   9865  N  ND2   . ASN A 1  1299 ? 103.840 112.206 153.603 1.00 31.38  ? 1299 ASN A ND2   1 
ATOM   9866  N  N     . ILE A 1  1300 ? 102.673 111.190 148.758 1.00 26.08  ? 1300 ILE A N     1 
ATOM   9867  C  CA    . ILE A 1  1300 ? 101.839 110.361 147.896 1.00 23.64  ? 1300 ILE A CA    1 
ATOM   9868  C  C     . ILE A 1  1300 ? 101.113 109.305 148.715 1.00 28.60  ? 1300 ILE A C     1 
ATOM   9869  O  O     . ILE A 1  1300 ? 99.927  109.045 148.498 1.00 31.25  ? 1300 ILE A O     1 
ATOM   9870  C  CB    . ILE A 1  1300 ? 102.678 109.728 146.771 1.00 25.92  ? 1300 ILE A CB    1 
ATOM   9871  C  CG1   . ILE A 1  1300 ? 103.060 110.777 145.733 1.00 26.20  ? 1300 ILE A CG1   1 
ATOM   9872  C  CG2   . ILE A 1  1300 ? 101.901 108.637 146.074 1.00 24.86  ? 1300 ILE A CG2   1 
ATOM   9873  C  CD1   . ILE A 1  1300 ? 104.013 110.272 144.691 1.00 21.95  ? 1300 ILE A CD1   1 
ATOM   9874  N  N     . PHE A 1  1301 ? 101.810 108.682 149.668 1.00 27.37  ? 1301 PHE A N     1 
ATOM   9875  C  CA    . PHE A 1  1301 ? 101.202 107.620 150.463 1.00 24.21  ? 1301 PHE A CA    1 
ATOM   9876  C  C     . PHE A 1  1301 ? 100.058 108.137 151.321 1.00 31.05  ? 1301 PHE A C     1 
ATOM   9877  O  O     . PHE A 1  1301 ? 99.032  107.463 151.449 1.00 33.29  ? 1301 PHE A O     1 
ATOM   9878  C  CB    . PHE A 1  1301 ? 102.265 106.943 151.325 1.00 27.45  ? 1301 PHE A CB    1 
ATOM   9879  C  CG    . PHE A 1  1301 ? 101.730 105.877 152.230 1.00 28.20  ? 1301 PHE A CG    1 
ATOM   9880  C  CD1   . PHE A 1  1301 ? 100.806 104.957 151.776 1.00 25.37  ? 1301 PHE A CD1   1 
ATOM   9881  C  CD2   . PHE A 1  1301 ? 102.179 105.774 153.528 1.00 27.06  ? 1301 PHE A CD2   1 
ATOM   9882  C  CE1   . PHE A 1  1301 ? 100.320 103.971 152.607 1.00 26.82  ? 1301 PHE A CE1   1 
ATOM   9883  C  CE2   . PHE A 1  1301 ? 101.702 104.787 154.359 1.00 26.13  ? 1301 PHE A CE2   1 
ATOM   9884  C  CZ    . PHE A 1  1301 ? 100.773 103.885 153.898 1.00 26.15  ? 1301 PHE A CZ    1 
ATOM   9885  N  N     . GLY A 1  1302 ? 100.209 109.322 151.909 1.00 33.02  ? 1302 GLY A N     1 
ATOM   9886  C  CA    . GLY A 1  1302 ? 99.121  109.895 152.679 1.00 29.32  ? 1302 GLY A CA    1 
ATOM   9887  C  C     . GLY A 1  1302 ? 97.893  110.186 151.840 1.00 28.89  ? 1302 GLY A C     1 
ATOM   9888  O  O     . GLY A 1  1302 ? 96.765  110.006 152.296 1.00 33.73  ? 1302 GLY A O     1 
ATOM   9889  N  N     . ALA A 1  1303 ? 98.091  110.630 150.601 1.00 24.60  ? 1303 ALA A N     1 
ATOM   9890  C  CA    . ALA A 1  1303 ? 96.959  110.971 149.751 1.00 25.74  ? 1303 ALA A CA    1 
ATOM   9891  C  C     . ALA A 1  1303 ? 96.157  109.754 149.306 1.00 28.00  ? 1303 ALA A C     1 
ATOM   9892  O  O     . ALA A 1  1303 ? 94.974  109.900 148.991 1.00 31.21  ? 1303 ALA A O     1 
ATOM   9893  C  CB    . ALA A 1  1303 ? 97.427  111.755 148.529 1.00 26.70  ? 1303 ALA A CB    1 
ATOM   9894  N  N     . MET A 1  1304 ? 96.763  108.568 149.226 1.00 28.67  ? 1304 MET A N     1 
ATOM   9895  C  CA    . MET A 1  1304 ? 95.948  107.395 148.934 1.00 31.65  ? 1304 MET A CA    1 
ATOM   9896  C  C     . MET A 1  1304 ? 95.216  106.899 150.171 1.00 37.69  ? 1304 MET A C     1 
ATOM   9897  O  O     . MET A 1  1304 ? 94.273  106.109 150.053 1.00 36.27  ? 1304 MET A O     1 
ATOM   9898  C  CB    . MET A 1  1304 ? 96.783  106.267 148.327 1.00 32.78  ? 1304 MET A CB    1 
ATOM   9899  C  CG    . MET A 1  1304 ? 98.145  106.657 147.831 1.00 35.27  ? 1304 MET A CG    1 
ATOM   9900  S  SD    . MET A 1  1304 ? 99.049  105.255 147.141 1.00 47.41  ? 1304 MET A SD    1 
ATOM   9901  C  CE    . MET A 1  1304 ? 99.740  104.504 148.600 1.00 31.57  ? 1304 MET A CE    1 
ATOM   9902  N  N     . LEU A 1  1305 ? 95.637  107.342 151.356 1.00 39.58  ? 1305 LEU A N     1 
ATOM   9903  C  CA    . LEU A 1  1305 ? 94.878  107.111 152.576 1.00 34.63  ? 1305 LEU A CA    1 
ATOM   9904  C  C     . LEU A 1  1305 ? 93.874  108.237 152.773 1.00 35.88  ? 1305 LEU A C     1 
ATOM   9905  O  O     . LEU A 1  1305 ? 93.862  108.896 153.817 1.00 38.79  ? 1305 LEU A O     1 
ATOM   9906  C  CB    . LEU A 1  1305 ? 95.806  107.006 153.782 1.00 34.05  ? 1305 LEU A CB    1 
ATOM   9907  C  CG    . LEU A 1  1305 ? 96.931  105.988 153.681 1.00 32.67  ? 1305 LEU A CG    1 
ATOM   9908  C  CD1   . LEU A 1  1305 ? 97.726  105.972 154.968 1.00 32.16  ? 1305 LEU A CD1   1 
ATOM   9909  C  CD2   . LEU A 1  1305 ? 96.387  104.615 153.354 1.00 33.47  ? 1305 LEU A CD2   1 
ATOM   9910  N  N     . ASP A 1  1306 ? 93.047  108.477 151.762 1.00 38.26  ? 1306 ASP A N     1 
ATOM   9911  C  CA    . ASP A 1  1306 ? 92.029  109.515 151.813 1.00 38.72  ? 1306 ASP A CA    1 
ATOM   9912  C  C     . ASP A 1  1306 ? 90.965  109.235 150.767 1.00 41.89  ? 1306 ASP A C     1 
ATOM   9913  O  O     . ASP A 1  1306 ? 91.276  109.073 149.584 1.00 43.83  ? 1306 ASP A O     1 
ATOM   9914  C  CB    . ASP A 1  1306 ? 92.643  110.898 151.605 1.00 36.88  ? 1306 ASP A CB    1 
ATOM   9915  C  CG    . ASP A 1  1306 ? 91.665  112.018 151.904 1.00 43.58  ? 1306 ASP A CG    1 
ATOM   9916  O  OD1   . ASP A 1  1306 ? 90.506  111.725 152.266 1.00 43.18  ? 1306 ASP A OD1   1 
ATOM   9917  O  OD2   . ASP A 1  1306 ? 92.050  113.196 151.783 1.00 46.32  ? 1306 ASP A OD2   1 
ATOM   9918  N  N     . ASP A 1  1307 ? 89.708  109.174 151.193 1.00 43.53  ? 1307 ASP A N     1 
ATOM   9919  C  CA    . ASP A 1  1307 ? 88.617  108.793 150.313 1.00 43.80  ? 1307 ASP A CA    1 
ATOM   9920  C  C     . ASP A 1  1307 ? 88.140  109.928 149.423 1.00 46.94  ? 1307 ASP A C     1 
ATOM   9921  O  O     . ASP A 1  1307 ? 87.415  109.671 148.457 1.00 47.11  ? 1307 ASP A O     1 
ATOM   9922  C  CB    . ASP A 1  1307 ? 87.442  108.277 151.140 1.00 44.40  ? 1307 ASP A CB    1 
ATOM   9923  C  CG    . ASP A 1  1307 ? 87.866  107.267 152.176 1.00 51.54  ? 1307 ASP A CG    1 
ATOM   9924  O  OD1   . ASP A 1  1307 ? 88.960  107.434 152.754 1.00 52.36  ? 1307 ASP A OD1   1 
ATOM   9925  O  OD2   . ASP A 1  1307 ? 87.105  106.305 152.418 1.00 50.88  ? 1307 ASP A OD2   1 
ATOM   9926  N  N     . ASN A 1  1308 ? 88.525  111.167 149.714 1.00 44.82  ? 1308 ASN A N     1 
ATOM   9927  C  CA    . ASN A 1  1308 ? 88.074  112.295 148.916 1.00 45.73  ? 1308 ASN A CA    1 
ATOM   9928  C  C     . ASN A 1  1308 ? 88.920  112.518 147.674 1.00 46.53  ? 1308 ASN A C     1 
ATOM   9929  O  O     . ASN A 1  1308 ? 88.567  113.363 146.847 1.00 47.83  ? 1308 ASN A O     1 
ATOM   9930  C  CB    . ASN A 1  1308 ? 88.068  113.567 149.763 1.00 45.09  ? 1308 ASN A CB    1 
ATOM   9931  C  CG    . ASN A 1  1308 ? 87.220  113.433 151.010 1.00 47.46  ? 1308 ASN A CG    1 
ATOM   9932  O  OD1   . ASN A 1  1308 ? 87.702  113.624 152.126 1.00 46.69  ? 1308 ASN A OD1   1 
ATOM   9933  N  ND2   . ASN A 1  1308 ? 85.950  113.090 150.826 1.00 44.30  ? 1308 ASN A ND2   1 
ATOM   9934  N  N     . ILE A 1  1309 ? 90.009  111.777 147.517 1.00 39.03  ? 1309 ILE A N     1 
ATOM   9935  C  CA    . ILE A 1  1309 ? 90.941  111.947 146.415 1.00 34.15  ? 1309 ILE A CA    1 
ATOM   9936  C  C     . ILE A 1  1309 ? 90.996  110.654 145.619 1.00 35.85  ? 1309 ILE A C     1 
ATOM   9937  O  O     . ILE A 1  1309 ? 90.995  109.564 146.198 1.00 36.17  ? 1309 ILE A O     1 
ATOM   9938  C  CB    . ILE A 1  1309 ? 92.340  112.338 146.932 1.00 34.50  ? 1309 ILE A CB    1 
ATOM   9939  C  CG1   . ILE A 1  1309 ? 92.342  113.787 147.417 1.00 35.25  ? 1309 ILE A CG1   1 
ATOM   9940  C  CG2   . ILE A 1  1309 ? 93.383  112.115 145.868 1.00 35.62  ? 1309 ILE A CG2   1 
ATOM   9941  C  CD1   . ILE A 1  1309 ? 93.143  113.995 148.664 1.00 33.95  ? 1309 ILE A CD1   1 
ATOM   9942  N  N     . ASP A 1  1310 ? 91.025  110.776 144.297 1.00 36.26  ? 1310 ASP A N     1 
ATOM   9943  C  CA    . ASP A 1  1310 ? 91.210  109.613 143.441 1.00 32.13  ? 1310 ASP A CA    1 
ATOM   9944  C  C     . ASP A 1  1310 ? 92.648  109.135 143.558 1.00 31.70  ? 1310 ASP A C     1 
ATOM   9945  O  O     . ASP A 1  1310 ? 93.567  109.871 143.177 1.00 32.71  ? 1310 ASP A O     1 
ATOM   9946  C  CB    . ASP A 1  1310 ? 90.879  109.957 141.998 1.00 31.82  ? 1310 ASP A CB    1 
ATOM   9947  C  CG    . ASP A 1  1310 ? 90.780  108.735 141.123 1.00 35.39  ? 1310 ASP A CG    1 
ATOM   9948  O  OD1   . ASP A 1  1310 ? 89.957  107.855 141.438 1.00 36.59  ? 1310 ASP A OD1   1 
ATOM   9949  O  OD2   . ASP A 1  1310 ? 91.499  108.657 140.109 1.00 32.11  ? 1310 ASP A OD2   1 
ATOM   9950  N  N     . PRO A 1  1311 ? 92.893  107.924 144.064 1.00 29.13  ? 1311 PRO A N     1 
ATOM   9951  C  CA    . PRO A 1  1311 ? 94.268  107.512 144.368 1.00 27.85  ? 1311 PRO A CA    1 
ATOM   9952  C  C     . PRO A 1  1311 ? 95.032  106.966 143.176 1.00 28.27  ? 1311 PRO A C     1 
ATOM   9953  O  O     . PRO A 1  1311 ? 96.221  106.661 143.315 1.00 27.07  ? 1311 PRO A O     1 
ATOM   9954  C  CB    . PRO A 1  1311 ? 94.065  106.427 145.429 1.00 27.78  ? 1311 PRO A CB    1 
ATOM   9955  C  CG    . PRO A 1  1311 ? 92.773  105.814 145.052 1.00 25.49  ? 1311 PRO A CG    1 
ATOM   9956  C  CD    . PRO A 1  1311 ? 91.915  106.903 144.468 1.00 26.68  ? 1311 PRO A CD    1 
ATOM   9957  N  N     . TYR A 1  1312 ? 94.393  106.827 142.024 1.00 25.92  ? 1312 TYR A N     1 
ATOM   9958  C  CA    . TYR A 1  1312 ? 95.021  106.305 140.823 1.00 22.86  ? 1312 TYR A CA    1 
ATOM   9959  C  C     . TYR A 1  1312 ? 95.552  107.397 139.910 1.00 24.33  ? 1312 TYR A C     1 
ATOM   9960  O  O     . TYR A 1  1312 ? 95.988  107.091 138.801 1.00 29.06  ? 1312 TYR A O     1 
ATOM   9961  C  CB    . TYR A 1  1312 ? 94.017  105.445 140.057 1.00 21.73  ? 1312 TYR A CB    1 
ATOM   9962  C  CG    . TYR A 1  1312 ? 93.645  104.176 140.774 1.00 26.10  ? 1312 TYR A CG    1 
ATOM   9963  C  CD1   . TYR A 1  1312 ? 94.616  103.289 141.207 1.00 27.35  ? 1312 TYR A CD1   1 
ATOM   9964  C  CD2   . TYR A 1  1312 ? 92.324  103.893 141.074 1.00 27.02  ? 1312 TYR A CD2   1 
ATOM   9965  C  CE1   . TYR A 1  1312 ? 94.277  102.135 141.875 1.00 24.17  ? 1312 TYR A CE1   1 
ATOM   9966  C  CE2   . TYR A 1  1312 ? 91.977  102.749 141.749 1.00 25.26  ? 1312 TYR A CE2   1 
ATOM   9967  C  CZ    . TYR A 1  1312 ? 92.955  101.872 142.147 1.00 27.56  ? 1312 TYR A CZ    1 
ATOM   9968  O  OH    . TYR A 1  1312 ? 92.608  100.728 142.822 1.00 31.31  ? 1312 TYR A OH    1 
ATOM   9969  N  N     . THR A 1  1313 ? 95.514  108.656 140.331 1.00 19.84  ? 1313 THR A N     1 
ATOM   9970  C  CA    . THR A 1  1313 ? 95.795  109.761 139.430 1.00 17.82  ? 1313 THR A CA    1 
ATOM   9971  C  C     . THR A 1  1313 ? 96.594  110.833 140.182 1.00 17.73  ? 1313 THR A C     1 
ATOM   9972  O  O     . THR A 1  1313 ? 96.606  112.013 139.825 1.00 24.08  ? 1313 THR A O     1 
ATOM   9973  C  CB    . THR A 1  1313 ? 94.475  110.273 138.835 1.00 22.67  ? 1313 THR A CB    1 
ATOM   9974  O  OG1   . THR A 1  1313 ? 93.959  109.271 137.961 1.00 22.48  ? 1313 THR A OG1   1 
ATOM   9975  C  CG2   . THR A 1  1313 ? 94.654  111.475 137.949 1.00 24.98  ? 1313 THR A CG2   1 
ATOM   9976  N  N     . ILE A 1  1314 ? 97.310  110.426 141.222 1.00 15.90  ? 1314 ILE A N     1 
ATOM   9977  C  CA    . ILE A 1  1314 ? 98.085  111.371 142.018 1.00 15.48  ? 1314 ILE A CA    1 
ATOM   9978  C  C     . ILE A 1  1314 ? 99.338  111.759 141.245 1.00 23.35  ? 1314 ILE A C     1 
ATOM   9979  O  O     . ILE A 1  1314 ? 100.094 110.894 140.794 1.00 29.24  ? 1314 ILE A O     1 
ATOM   9980  C  CB    . ILE A 1  1314 ? 98.448  110.780 143.385 1.00 17.81  ? 1314 ILE A CB    1 
ATOM   9981  C  CG1   . ILE A 1  1314 ? 97.190  110.510 144.201 1.00 20.06  ? 1314 ILE A CG1   1 
ATOM   9982  C  CG2   . ILE A 1  1314 ? 99.367  111.717 144.133 1.00 21.10  ? 1314 ILE A CG2   1 
ATOM   9983  C  CD1   . ILE A 1  1314 ? 97.420  109.597 145.375 1.00 21.98  ? 1314 ILE A CD1   1 
ATOM   9984  N  N     . VAL A 1  1315 ? 99.563  113.057 141.094 1.00 17.00  ? 1315 VAL A N     1 
ATOM   9985  C  CA    . VAL A 1  1315 ? 100.724 113.581 140.391 1.00 14.29  ? 1315 VAL A CA    1 
ATOM   9986  C  C     . VAL A 1  1315 ? 101.557 114.374 141.378 1.00 12.66  ? 1315 VAL A C     1 
ATOM   9987  O  O     . VAL A 1  1315 ? 101.097 115.385 141.914 1.00 28.74  ? 1315 VAL A O     1 
ATOM   9988  C  CB    . VAL A 1  1315 ? 100.317 114.454 139.197 1.00 11.54  ? 1315 VAL A CB    1 
ATOM   9989  C  CG1   . VAL A 1  1315 ? 101.509 115.183 138.659 1.00 17.96  ? 1315 VAL A CG1   1 
ATOM   9990  C  CG2   . VAL A 1  1315 ? 99.712  113.606 138.131 1.00 8.36   ? 1315 VAL A CG2   1 
ATOM   9991  N  N     . SER A 1  1316 ? 102.784 113.935 141.601 1.00 7.47   ? 1316 SER A N     1 
ATOM   9992  C  CA    . SER A 1  1316 ? 103.740 114.662 142.415 1.00 10.38  ? 1316 SER A CA    1 
ATOM   9993  C  C     . SER A 1  1316 ? 104.831 115.229 141.522 1.00 16.29  ? 1316 SER A C     1 
ATOM   9994  O  O     . SER A 1  1316 ? 105.081 114.727 140.429 1.00 28.77  ? 1316 SER A O     1 
ATOM   9995  C  CB    . SER A 1  1316 ? 104.359 113.761 143.481 1.00 13.62  ? 1316 SER A CB    1 
ATOM   9996  O  OG    . SER A 1  1316 ? 105.414 114.424 144.139 1.00 11.84  ? 1316 SER A OG    1 
ATOM   9997  N  N     . SER A 1  1317 ? 105.467 116.289 141.982 1.00 14.46  ? 1317 SER A N     1 
ATOM   9998  C  CA    . SER A 1  1317 ? 106.603 116.848 141.274 1.00 15.90  ? 1317 SER A CA    1 
ATOM   9999  C  C     . SER A 1  1317 ? 107.920 116.279 141.769 1.00 20.76  ? 1317 SER A C     1 
ATOM   10000 O  O     . SER A 1  1317 ? 108.981 116.728 141.334 1.00 25.22  ? 1317 SER A O     1 
ATOM   10001 C  CB    . SER A 1  1317 ? 106.607 118.373 141.404 1.00 15.30  ? 1317 SER A CB    1 
ATOM   10002 O  OG    . SER A 1  1317 ? 107.185 118.777 142.627 1.00 21.31  ? 1317 SER A OG    1 
ATOM   10003 N  N     . SER A 1  1318 ? 107.874 115.307 142.666 1.00 18.06  ? 1318 SER A N     1 
ATOM   10004 C  CA    . SER A 1  1318 ? 109.064 114.763 143.299 1.00 18.73  ? 1318 SER A CA    1 
ATOM   10005 C  C     . SER A 1  1318 ? 109.495 113.497 142.571 1.00 19.72  ? 1318 SER A C     1 
ATOM   10006 O  O     . SER A 1  1318 ? 108.682 112.598 142.338 1.00 15.95  ? 1318 SER A O     1 
ATOM   10007 C  CB    . SER A 1  1318 ? 108.793 114.474 144.774 1.00 20.68  ? 1318 SER A CB    1 
ATOM   10008 O  OG    . SER A 1  1318 ? 109.891 113.840 145.393 1.00 18.63  ? 1318 SER A OG    1 
ATOM   10009 N  N     . ILE A 1  1319 ? 110.772 113.438 142.201 1.00 19.25  ? 1319 ILE A N     1 
ATOM   10010 C  CA    . ILE A 1  1319 ? 111.323 112.227 141.608 1.00 16.70  ? 1319 ILE A CA    1 
ATOM   10011 C  C     . ILE A 1  1319 ? 111.564 111.169 142.675 1.00 17.63  ? 1319 ILE A C     1 
ATOM   10012 O  O     . ILE A 1  1319 ? 111.257 109.990 142.478 1.00 15.48  ? 1319 ILE A O     1 
ATOM   10013 C  CB    . ILE A 1  1319 ? 112.604 112.567 140.826 1.00 12.49  ? 1319 ILE A CB    1 
ATOM   10014 C  CG1   . ILE A 1  1319 ? 112.255 113.430 139.613 1.00 13.80  ? 1319 ILE A CG1   1 
ATOM   10015 C  CG2   . ILE A 1  1319 ? 113.334 111.310 140.414 1.00 11.99  ? 1319 ILE A CG2   1 
ATOM   10016 C  CD1   . ILE A 1  1319 ? 113.401 114.211 139.058 1.00 13.99  ? 1319 ILE A CD1   1 
ATOM   10017 N  N     . GLY A 1  1320 ? 112.106 111.573 143.822 1.00 18.42  ? 1320 GLY A N     1 
ATOM   10018 C  CA    . GLY A 1  1320 ? 112.413 110.613 144.867 1.00 19.77  ? 1320 GLY A CA    1 
ATOM   10019 C  C     . GLY A 1  1320 ? 111.179 109.971 145.468 1.00 19.91  ? 1320 GLY A C     1 
ATOM   10020 O  O     . GLY A 1  1320 ? 111.196 108.794 145.826 1.00 20.08  ? 1320 GLY A O     1 
ATOM   10021 N  N     . ASP A 1  1321 ? 110.101 110.742 145.606 1.00 22.63  ? 1321 ASP A N     1 
ATOM   10022 C  CA    . ASP A 1  1321 ? 108.849 110.201 146.124 1.00 17.39  ? 1321 ASP A CA    1 
ATOM   10023 C  C     . ASP A 1  1321 ? 108.175 109.289 145.112 1.00 16.47  ? 1321 ASP A C     1 
ATOM   10024 O  O     . ASP A 1  1321 ? 107.631 108.246 145.478 1.00 17.06  ? 1321 ASP A O     1 
ATOM   10025 C  CB    . ASP A 1  1321 ? 107.917 111.343 146.513 1.00 22.43  ? 1321 ASP A CB    1 
ATOM   10026 C  CG    . ASP A 1  1321 ? 107.051 111.009 147.705 1.00 27.88  ? 1321 ASP A CG    1 
ATOM   10027 O  OD1   . ASP A 1  1321 ? 107.600 110.797 148.805 1.00 30.13  ? 1321 ASP A OD1   1 
ATOM   10028 O  OD2   . ASP A 1  1321 ? 105.819 110.962 147.541 1.00 25.22  ? 1321 ASP A OD2   1 
ATOM   10029 N  N     . THR A 1  1322 ? 108.198 109.672 143.835 1.00 19.80  ? 1322 THR A N     1 
ATOM   10030 C  CA    . THR A 1  1322 ? 107.639 108.835 142.779 1.00 15.68  ? 1322 THR A CA    1 
ATOM   10031 C  C     . THR A 1  1322 ? 108.381 107.512 142.668 1.00 15.89  ? 1322 THR A C     1 
ATOM   10032 O  O     . THR A 1  1322 ? 107.780 106.480 142.358 1.00 13.14  ? 1322 THR A O     1 
ATOM   10033 C  CB    . THR A 1  1322 ? 107.691 109.583 141.452 1.00 10.72  ? 1322 THR A CB    1 
ATOM   10034 O  OG1   . THR A 1  1322 ? 107.144 110.894 141.628 1.00 13.64  ? 1322 THR A OG1   1 
ATOM   10035 C  CG2   . THR A 1  1322 ? 106.912 108.849 140.397 1.00 8.16   ? 1322 THR A CG2   1 
ATOM   10036 N  N     . MET A 1  1323 ? 109.691 107.530 142.894 1.00 13.27  ? 1323 MET A N     1 
ATOM   10037 C  CA    . MET A 1  1323 ? 110.472 106.306 142.834 1.00 11.03  ? 1323 MET A CA    1 
ATOM   10038 C  C     . MET A 1  1323 ? 110.096 105.358 143.964 1.00 19.20  ? 1323 MET A C     1 
ATOM   10039 O  O     . MET A 1  1323 ? 109.967 104.147 143.758 1.00 22.51  ? 1323 MET A O     1 
ATOM   10040 C  CB    . MET A 1  1323 ? 111.958 106.655 142.891 1.00 12.90  ? 1323 MET A CB    1 
ATOM   10041 C  CG    . MET A 1  1323 ? 112.892 105.486 143.058 1.00 15.42  ? 1323 MET A CG    1 
ATOM   10042 S  SD    . MET A 1  1323 ? 112.931 104.472 141.584 1.00 18.11  ? 1323 MET A SD    1 
ATOM   10043 C  CE    . MET A 1  1323 ? 113.716 103.011 142.209 1.00 11.29  ? 1323 MET A CE    1 
ATOM   10044 N  N     . GLU A 1  1324 ? 109.907 105.897 145.166 1.00 23.59  ? 1324 GLU A N     1 
ATOM   10045 C  CA    . GLU A 1  1324 ? 109.648 105.066 146.335 1.00 20.96  ? 1324 GLU A CA    1 
ATOM   10046 C  C     . GLU A 1  1324 ? 108.277 104.409 146.261 1.00 24.87  ? 1324 GLU A C     1 
ATOM   10047 O  O     . GLU A 1  1324 ? 108.104 103.266 146.693 1.00 26.16  ? 1324 GLU A O     1 
ATOM   10048 C  CB    . GLU A 1  1324 ? 109.782 105.919 147.592 1.00 21.49  ? 1324 GLU A CB    1 
ATOM   10049 C  CG    . GLU A 1  1324 ? 110.405 105.217 148.771 1.00 27.24  ? 1324 GLU A CG    1 
ATOM   10050 C  CD    . GLU A 1  1324 ? 109.381 104.819 149.807 1.00 35.85  ? 1324 GLU A CD    1 
ATOM   10051 O  OE1   . GLU A 1  1324 ? 109.609 103.822 150.524 1.00 37.27  ? 1324 GLU A OE1   1 
ATOM   10052 O  OE2   . GLU A 1  1324 ? 108.346 105.510 149.906 1.00 31.82  ? 1324 GLU A OE2   1 
ATOM   10053 N  N     . LEU A 1  1325 ? 107.298 105.106 145.699 1.00 21.39  ? 1325 LEU A N     1 
ATOM   10054 C  CA    . LEU A 1  1325 ? 105.926 104.631 145.691 1.00 19.24  ? 1325 LEU A CA    1 
ATOM   10055 C  C     . LEU A 1  1325 ? 105.581 103.832 144.442 1.00 22.98  ? 1325 LEU A C     1 
ATOM   10056 O  O     . LEU A 1  1325 ? 104.732 102.941 144.501 1.00 27.34  ? 1325 LEU A O     1 
ATOM   10057 C  CB    . LEU A 1  1325 ? 104.968 105.817 145.819 1.00 23.27  ? 1325 LEU A CB    1 
ATOM   10058 C  CG    . LEU A 1  1325 ? 104.276 106.057 147.162 1.00 26.15  ? 1325 LEU A CG    1 
ATOM   10059 C  CD1   . LEU A 1  1325 ? 103.402 104.880 147.533 1.00 25.04  ? 1325 LEU A CD1   1 
ATOM   10060 C  CD2   . LEU A 1  1325 ? 105.292 106.329 148.239 1.00 24.29  ? 1325 LEU A CD2   1 
ATOM   10061 N  N     . TYR A 1  1326 ? 106.212 104.131 143.308 1.00 19.68  ? 1326 TYR A N     1 
ATOM   10062 C  CA    . TYR A 1  1326 ? 105.780 103.577 142.033 1.00 12.69  ? 1326 TYR A CA    1 
ATOM   10063 C  C     . TYR A 1  1326 ? 106.799 102.677 141.355 1.00 14.16  ? 1326 TYR A C     1 
ATOM   10064 O  O     . TYR A 1  1326 ? 106.404 101.720 140.695 1.00 16.86  ? 1326 TYR A O     1 
ATOM   10065 C  CB    . TYR A 1  1326 ? 105.401 104.703 141.071 1.00 10.31  ? 1326 TYR A CB    1 
ATOM   10066 C  CG    . TYR A 1  1326 ? 104.202 105.513 141.501 1.00 18.63  ? 1326 TYR A CG    1 
ATOM   10067 C  CD1   . TYR A 1  1326 ? 103.194 104.955 142.259 1.00 18.41  ? 1326 TYR A CD1   1 
ATOM   10068 C  CD2   . TYR A 1  1326 ? 104.082 106.841 141.145 1.00 22.28  ? 1326 TYR A CD2   1 
ATOM   10069 C  CE1   . TYR A 1  1326 ? 102.107 105.697 142.649 1.00 14.98  ? 1326 TYR A CE1   1 
ATOM   10070 C  CE2   . TYR A 1  1326 ? 103.006 107.586 141.532 1.00 17.35  ? 1326 TYR A CE2   1 
ATOM   10071 C  CZ    . TYR A 1  1326 ? 102.020 107.013 142.283 1.00 19.68  ? 1326 TYR A CZ    1 
ATOM   10072 O  OH    . TYR A 1  1326 ? 100.937 107.765 142.663 1.00 27.29  ? 1326 TYR A OH    1 
ATOM   10073 N  N     . GLY A 1  1327 ? 108.085 102.953 141.479 1.00 12.02  ? 1327 GLY A N     1 
ATOM   10074 C  CA    . GLY A 1  1327 ? 109.094 102.142 140.842 1.00 12.36  ? 1327 GLY A CA    1 
ATOM   10075 C  C     . GLY A 1  1327 ? 109.966 102.965 139.930 1.00 11.70  ? 1327 GLY A C     1 
ATOM   10076 O  O     . GLY A 1  1327 ? 109.907 104.196 139.914 1.00 11.11  ? 1327 GLY A O     1 
ATOM   10077 N  N     . ILE A 1  1328 ? 110.785 102.273 139.139 1.00 10.76  ? 1328 ILE A N     1 
ATOM   10078 C  CA    . ILE A 1  1328 ? 111.782 102.960 138.326 1.00 3.82   ? 1328 ILE A CA    1 
ATOM   10079 C  C     . ILE A 1  1328 ? 111.185 103.488 137.033 1.00 7.58   ? 1328 ILE A C     1 
ATOM   10080 O  O     . ILE A 1  1328 ? 111.573 104.559 136.566 1.00 11.70  ? 1328 ILE A O     1 
ATOM   10081 C  CB    . ILE A 1  1328 ? 112.992 102.041 138.063 1.00 1.02   ? 1328 ILE A CB    1 
ATOM   10082 C  CG1   . ILE A 1  1328 ? 114.129 102.830 137.430 1.00 2.71   ? 1328 ILE A CG1   1 
ATOM   10083 C  CG2   . ILE A 1  1328 ? 112.630 100.864 137.192 1.00 5.00   ? 1328 ILE A CG2   1 
ATOM   10084 C  CD1   . ILE A 1  1328 ? 114.609 103.944 138.276 1.00 3.34   ? 1328 ILE A CD1   1 
ATOM   10085 N  N     . GLU A 1  1329 ? 110.239 102.770 136.435 1.00 5.18   ? 1329 GLU A N     1 
ATOM   10086 C  CA    . GLU A 1  1329 ? 109.698 103.189 135.152 1.00 3.07   ? 1329 GLU A CA    1 
ATOM   10087 C  C     . GLU A 1  1329 ? 108.849 104.441 135.282 1.00 6.67   ? 1329 GLU A C     1 
ATOM   10088 O  O     . GLU A 1  1329 ? 108.829 105.271 134.370 1.00 13.23  ? 1329 GLU A O     1 
ATOM   10089 C  CB    . GLU A 1  1329 ? 108.898 102.051 134.539 1.00 1.56   ? 1329 GLU A CB    1 
ATOM   10090 C  CG    . GLU A 1  1329 ? 109.757 100.948 133.958 1.00 4.59   ? 1329 GLU A CG    1 
ATOM   10091 C  CD    . GLU A 1  1329 ? 110.363 101.315 132.628 1.00 10.91  ? 1329 GLU A CD    1 
ATOM   10092 O  OE1   . GLU A 1  1329 ? 109.694 102.010 131.842 1.00 11.75  ? 1329 GLU A OE1   1 
ATOM   10093 O  OE2   . GLU A 1  1329 ? 111.510 100.916 132.364 1.00 11.32  ? 1329 GLU A OE2   1 
ATOM   10094 N  N     . ALA A 1  1330 ? 108.133 104.589 136.392 1.00 9.62   ? 1330 ALA A N     1 
ATOM   10095 C  CA    . ALA A 1  1330 ? 107.381 105.811 136.627 1.00 3.93   ? 1330 ALA A CA    1 
ATOM   10096 C  C     . ALA A 1  1330 ? 108.293 106.963 137.009 1.00 2.16   ? 1330 ALA A C     1 
ATOM   10097 O  O     . ALA A 1  1330 ? 108.005 108.113 136.674 1.00 9.57   ? 1330 ALA A O     1 
ATOM   10098 C  CB    . ALA A 1  1330 ? 106.337 105.572 137.710 1.00 5.11   ? 1330 ALA A CB    1 
ATOM   10099 N  N     . ALA A 1  1331 ? 109.391 106.677 137.708 1.00 2.37   ? 1331 ALA A N     1 
ATOM   10100 C  CA    . ALA A 1  1331 ? 110.367 107.709 138.030 1.00 3.76   ? 1331 ALA A CA    1 
ATOM   10101 C  C     . ALA A 1  1331 ? 111.106 108.203 136.792 1.00 8.50   ? 1331 ALA A C     1 
ATOM   10102 O  O     . ALA A 1  1331 ? 111.558 109.348 136.763 1.00 12.51  ? 1331 ALA A O     1 
ATOM   10103 C  CB    . ALA A 1  1331 ? 111.357 107.183 139.059 1.00 1.10   ? 1331 ALA A CB    1 
ATOM   10104 N  N     . ARG A 1  1332 ? 111.258 107.359 135.773 1.00 3.62   ? 1332 ARG A N     1 
ATOM   10105 C  CA    . ARG A 1  1332 ? 111.833 107.816 134.515 1.00 13.87  ? 1332 ARG A CA    1 
ATOM   10106 C  C     . ARG A 1  1332 ? 110.910 108.792 133.802 1.00 2.56   ? 1332 ARG A C     1 
ATOM   10107 O  O     . ARG A 1  1332 ? 111.362 109.828 133.311 1.00 9.03   ? 1332 ARG A O     1 
ATOM   10108 C  CB    . ARG A 1  1332 ? 112.140 106.626 133.617 1.00 2.82   ? 1332 ARG A CB    1 
ATOM   10109 C  CG    . ARG A 1  1332 ? 112.909 106.987 132.374 1.00 4.84   ? 1332 ARG A CG    1 
ATOM   10110 C  CD    . ARG A 1  1332 ? 112.823 105.902 131.352 1.00 4.70   ? 1332 ARG A CD    1 
ATOM   10111 N  NE    . ARG A 1  1332 ? 111.567 105.955 130.620 1.00 6.03   ? 1332 ARG A NE    1 
ATOM   10112 C  CZ    . ARG A 1  1332 ? 111.445 106.337 129.358 1.00 10.43  ? 1332 ARG A CZ    1 
ATOM   10113 N  NH1   . ARG A 1  1332 ? 112.493 106.696 128.640 1.00 5.84   ? 1332 ARG A NH1   1 
ATOM   10114 N  NH2   . ARG A 1  1332 ? 110.243 106.341 128.798 1.00 5.28   ? 1332 ARG A NH2   1 
ATOM   10115 N  N     . GLN A 1  1333 ? 109.617 108.479 133.728 1.00 4.47   ? 1333 GLN A N     1 
ATOM   10116 C  CA    . GLN A 1  1333 ? 108.656 109.420 133.167 1.00 11.82  ? 1333 GLN A CA    1 
ATOM   10117 C  C     . GLN A 1  1333 ? 108.619 110.717 133.955 1.00 1.73   ? 1333 GLN A C     1 
ATOM   10118 O  O     . GLN A 1  1333 ? 108.398 111.780 133.378 1.00 10.51  ? 1333 GLN A O     1 
ATOM   10119 C  CB    . GLN A 1  1333 ? 107.263 108.809 133.140 1.00 0.30   ? 1333 GLN A CB    1 
ATOM   10120 C  CG    . GLN A 1  1333 ? 107.050 107.712 132.143 1.00 3.68   ? 1333 GLN A CG    1 
ATOM   10121 C  CD    . GLN A 1  1333 ? 107.000 108.201 130.719 1.00 13.82  ? 1333 GLN A CD    1 
ATOM   10122 O  OE1   . GLN A 1  1333 ? 106.985 109.397 130.458 1.00 16.28  ? 1333 GLN A OE1   1 
ATOM   10123 N  NE2   . GLN A 1  1333 ? 106.931 107.269 129.786 1.00 9.28   ? 1333 GLN A NE2   1 
ATOM   10124 N  N     . LYS A 1  1334 ? 108.810 110.644 135.268 1.00 15.05  ? 1334 LYS A N     1 
ATOM   10125 C  CA    . LYS A 1  1334 ? 108.829 111.842 136.095 1.00 2.13   ? 1334 LYS A CA    1 
ATOM   10126 C  C     . LYS A 1  1334 ? 109.995 112.752 135.744 1.00 3.82   ? 1334 LYS A C     1 
ATOM   10127 O  O     . LYS A 1  1334 ? 109.846 113.975 135.738 1.00 14.34  ? 1334 LYS A O     1 
ATOM   10128 C  CB    . LYS A 1  1334 ? 108.872 111.447 137.572 1.00 8.85   ? 1334 LYS A CB    1 
ATOM   10129 C  CG    . LYS A 1  1334 ? 108.775 112.600 138.555 1.00 10.49  ? 1334 LYS A CG    1 
ATOM   10130 C  CD    . LYS A 1  1334 ? 107.610 113.516 138.260 1.00 10.30  ? 1334 LYS A CD    1 
ATOM   10131 C  CE    . LYS A 1  1334 ? 106.296 112.798 138.369 1.00 6.33   ? 1334 LYS A CE    1 
ATOM   10132 N  NZ    . LYS A 1  1334 ? 105.168 113.675 137.983 1.00 6.05   ? 1334 LYS A NZ    1 
ATOM   10133 N  N     . ILE A 1  1335 ? 111.163 112.179 135.454 1.00 10.16  ? 1335 ILE A N     1 
ATOM   10134 C  CA    . ILE A 1  1335 ? 112.329 112.981 135.089 1.00 2.70   ? 1335 ILE A CA    1 
ATOM   10135 C  C     . ILE A 1  1335 ? 112.098 113.706 133.768 1.00 4.27   ? 1335 ILE A C     1 
ATOM   10136 O  O     . ILE A 1  1335 ? 112.479 114.868 133.614 1.00 10.00  ? 1335 ILE A O     1 
ATOM   10137 C  CB    . ILE A 1  1335 ? 113.592 112.100 135.044 1.00 2.33   ? 1335 ILE A CB    1 
ATOM   10138 C  CG1   . ILE A 1  1335 ? 113.924 111.569 136.433 1.00 2.40   ? 1335 ILE A CG1   1 
ATOM   10139 C  CG2   . ILE A 1  1335 ? 114.773 112.880 134.519 1.00 5.15   ? 1335 ILE A CG2   1 
ATOM   10140 C  CD1   . ILE A 1  1335 ? 115.039 110.577 136.458 1.00 4.04   ? 1335 ILE A CD1   1 
ATOM   10141 N  N     . ILE A 1  1336 ? 111.475 113.038 132.796 1.00 2.99   ? 1336 ILE A N     1 
ATOM   10142 C  CA    . ILE A 1  1336 ? 111.182 113.675 131.512 1.00 2.39   ? 1336 ILE A CA    1 
ATOM   10143 C  C     . ILE A 1  1336 ? 110.248 114.859 131.708 1.00 7.19   ? 1336 ILE A C     1 
ATOM   10144 O  O     . ILE A 1  1336 ? 110.430 115.923 131.110 1.00 9.29   ? 1336 ILE A O     1 
ATOM   10145 C  CB    . ILE A 1  1336 ? 110.579 112.657 130.529 1.00 13.65  ? 1336 ILE A CB    1 
ATOM   10146 C  CG1   . ILE A 1  1336 ? 111.590 111.588 130.151 1.00 1.81   ? 1336 ILE A CG1   1 
ATOM   10147 C  CG2   . ILE A 1  1336 ? 110.072 113.348 129.294 1.00 1.95   ? 1336 ILE A CG2   1 
ATOM   10148 C  CD1   . ILE A 1  1336 ? 110.958 110.289 129.770 1.00 13.00  ? 1336 ILE A CD1   1 
ATOM   10149 N  N     . SER A 1  1337 ? 109.217 114.677 132.534 1.00 12.92  ? 1337 SER A N     1 
ATOM   10150 C  CA    . SER A 1  1337 ? 108.245 115.731 132.796 1.00 2.02   ? 1337 SER A CA    1 
ATOM   10151 C  C     . SER A 1  1337 ? 108.868 116.902 133.537 1.00 9.34   ? 1337 SER A C     1 
ATOM   10152 O  O     . SER A 1  1337 ? 108.540 118.058 133.267 1.00 16.33  ? 1337 SER A O     1 
ATOM   10153 C  CB    . SER A 1  1337 ? 107.084 115.168 133.598 1.00 2.21   ? 1337 SER A CB    1 
ATOM   10154 O  OG    . SER A 1  1337 ? 106.354 114.247 132.820 1.00 12.86  ? 1337 SER A OG    1 
ATOM   10155 N  N     . GLU A 1  1338 ? 109.747 116.625 134.489 1.00 5.59   ? 1338 GLU A N     1 
ATOM   10156 C  CA    . GLU A 1  1338 ? 110.301 117.697 135.296 1.00 9.95   ? 1338 GLU A CA    1 
ATOM   10157 C  C     . GLU A 1  1338 ? 111.373 118.484 134.555 1.00 17.07  ? 1338 GLU A C     1 
ATOM   10158 O  O     . GLU A 1  1338 ? 111.506 119.690 134.776 1.00 24.08  ? 1338 GLU A O     1 
ATOM   10159 C  CB    . GLU A 1  1338 ? 110.829 117.131 136.611 1.00 8.03   ? 1338 GLU A CB    1 
ATOM   10160 C  CG    . GLU A 1  1338 ? 109.720 116.569 137.501 1.00 13.66  ? 1338 GLU A CG    1 
ATOM   10161 C  CD    . GLU A 1  1338 ? 108.575 117.564 137.748 1.00 25.45  ? 1338 GLU A CD    1 
ATOM   10162 O  OE1   . GLU A 1  1338 ? 107.408 117.244 137.424 1.00 20.10  ? 1338 GLU A OE1   1 
ATOM   10163 O  OE2   . GLU A 1  1338 ? 108.842 118.666 138.270 1.00 28.28  ? 1338 GLU A OE2   1 
ATOM   10164 N  N     . ILE A 1  1339 ? 112.153 117.841 133.687 1.00 16.46  ? 1339 ILE A N     1 
ATOM   10165 C  CA    . ILE A 1  1339 ? 113.091 118.601 132.867 1.00 12.01  ? 1339 ILE A CA    1 
ATOM   10166 C  C     . ILE A 1  1339 ? 112.335 119.448 131.858 1.00 12.38  ? 1339 ILE A C     1 
ATOM   10167 O  O     . ILE A 1  1339 ? 112.705 120.593 131.592 1.00 15.86  ? 1339 ILE A O     1 
ATOM   10168 C  CB    . ILE A 1  1339 ? 114.105 117.668 132.179 1.00 9.42   ? 1339 ILE A CB    1 
ATOM   10169 C  CG1   . ILE A 1  1339 ? 114.976 116.962 133.207 1.00 10.45  ? 1339 ILE A CG1   1 
ATOM   10170 C  CG2   . ILE A 1  1339 ? 115.008 118.444 131.252 1.00 7.15   ? 1339 ILE A CG2   1 
ATOM   10171 C  CD1   . ILE A 1  1339 ? 115.900 115.953 132.602 1.00 8.66   ? 1339 ILE A CD1   1 
ATOM   10172 N  N     . ARG A 1  1340 ? 111.246 118.911 131.307 1.00 11.21  ? 1340 ARG A N     1 
ATOM   10173 C  CA    . ARG A 1  1340 ? 110.487 119.623 130.287 1.00 6.41   ? 1340 ARG A CA    1 
ATOM   10174 C  C     . ARG A 1  1340 ? 109.933 120.943 130.808 1.00 16.96  ? 1340 ARG A C     1 
ATOM   10175 O  O     . ARG A 1  1340 ? 109.872 121.930 130.069 1.00 25.24  ? 1340 ARG A O     1 
ATOM   10176 C  CB    . ARG A 1  1340 ? 109.356 118.742 129.771 1.00 5.96   ? 1340 ARG A CB    1 
ATOM   10177 C  CG    . ARG A 1  1340 ? 108.681 119.290 128.543 1.00 9.11   ? 1340 ARG A CG    1 
ATOM   10178 C  CD    . ARG A 1  1340 ? 107.238 118.879 128.463 1.00 11.33  ? 1340 ARG A CD    1 
ATOM   10179 N  NE    . ARG A 1  1340 ? 107.063 117.477 128.119 1.00 10.82  ? 1340 ARG A NE    1 
ATOM   10180 C  CZ    . ARG A 1  1340 ? 106.482 116.582 128.902 1.00 12.92  ? 1340 ARG A CZ    1 
ATOM   10181 N  NH1   . ARG A 1  1340 ? 106.067 116.894 130.116 1.00 14.32  ? 1340 ARG A NH1   1 
ATOM   10182 N  NH2   . ARG A 1  1340 ? 106.314 115.344 128.456 1.00 13.35  ? 1340 ARG A NH2   1 
ATOM   10183 N  N     . THR A 1  1341 ? 109.504 120.980 132.068 1.00 16.25  ? 1341 THR A N     1 
ATOM   10184 C  CA    . THR A 1  1341 ? 108.961 122.219 132.616 1.00 14.88  ? 1341 THR A CA    1 
ATOM   10185 C  C     . THR A 1  1341 ? 110.043 123.274 132.787 1.00 19.01  ? 1341 THR A C     1 
ATOM   10186 O  O     . THR A 1  1341 ? 109.792 124.465 132.578 1.00 22.86  ? 1341 THR A O     1 
ATOM   10187 C  CB    . THR A 1  1341 ? 108.262 121.950 133.946 1.00 16.44  ? 1341 THR A CB    1 
ATOM   10188 O  OG1   . THR A 1  1341 ? 109.204 121.428 134.885 1.00 22.07  ? 1341 THR A OG1   1 
ATOM   10189 C  CG2   . THR A 1  1341 ? 107.145 120.964 133.758 1.00 15.31  ? 1341 THR A CG2   1 
ATOM   10190 N  N     . VAL A 1  1342 ? 111.245 122.860 133.178 1.00 18.54  ? 1342 VAL A N     1 
ATOM   10191 C  CA    . VAL A 1  1342 ? 112.350 123.792 133.360 1.00 21.79  ? 1342 VAL A CA    1 
ATOM   10192 C  C     . VAL A 1  1342 ? 112.812 124.379 132.027 1.00 22.32  ? 1342 VAL A C     1 
ATOM   10193 O  O     . VAL A 1  1342 ? 113.293 125.514 131.974 1.00 27.67  ? 1342 VAL A O     1 
ATOM   10194 C  CB    . VAL A 1  1342 ? 113.485 123.079 134.120 1.00 19.95  ? 1342 VAL A CB    1 
ATOM   10195 C  CG1   . VAL A 1  1342 ? 114.828 123.643 133.760 1.00 20.55  ? 1342 VAL A CG1   1 
ATOM   10196 C  CG2   . VAL A 1  1342 ? 113.259 123.187 135.600 1.00 20.81  ? 1342 VAL A CG2   1 
ATOM   10197 N  N     . MET A 1  1343 ? 112.669 123.633 130.933 1.00 19.99  ? 1343 MET A N     1 
ATOM   10198 C  CA    . MET A 1  1343 ? 113.101 124.140 129.634 1.00 20.24  ? 1343 MET A CA    1 
ATOM   10199 C  C     . MET A 1  1343 ? 112.308 125.366 129.211 1.00 24.02  ? 1343 MET A C     1 
ATOM   10200 O  O     . MET A 1  1343 ? 112.862 126.291 128.610 1.00 26.28  ? 1343 MET A O     1 
ATOM   10201 C  CB    . MET A 1  1343 ? 112.993 123.050 128.567 1.00 19.52  ? 1343 MET A CB    1 
ATOM   10202 C  CG    . MET A 1  1343 ? 113.733 121.780 128.898 1.00 16.81  ? 1343 MET A CG    1 
ATOM   10203 S  SD    . MET A 1  1343 ? 115.486 121.910 128.540 1.00 23.64  ? 1343 MET A SD    1 
ATOM   10204 C  CE    . MET A 1  1343 ? 116.157 121.911 130.190 1.00 17.69  ? 1343 MET A CE    1 
ATOM   10205 N  N     . GLY A 1  1344 ? 111.008 125.384 129.479 1.00 30.15  ? 1344 GLY A N     1 
ATOM   10206 C  CA    . GLY A 1  1344 ? 110.184 126.492 129.040 1.00 29.48  ? 1344 GLY A CA    1 
ATOM   10207 C  C     . GLY A 1  1344 ? 109.477 126.207 127.730 1.00 33.39  ? 1344 GLY A C     1 
ATOM   10208 O  O     . GLY A 1  1344 ? 108.974 125.100 127.524 1.00 38.95  ? 1344 GLY A O     1 
ATOM   10209 N  N     . ASP A 1  1345 ? 109.432 127.188 126.831 1.00 36.70  ? 1345 ASP A N     1 
ATOM   10210 C  CA    . ASP A 1  1345 ? 108.711 127.023 125.575 1.00 41.72  ? 1345 ASP A CA    1 
ATOM   10211 C  C     . ASP A 1  1345 ? 109.608 126.685 124.396 1.00 41.59  ? 1345 ASP A C     1 
ATOM   10212 O  O     . ASP A 1  1345 ? 109.190 125.927 123.515 1.00 39.29  ? 1345 ASP A O     1 
ATOM   10213 C  CB    . ASP A 1  1345 ? 107.911 128.287 125.246 1.00 41.49  ? 1345 ASP A CB    1 
ATOM   10214 C  CG    . ASP A 1  1345 ? 108.707 129.545 125.462 1.00 42.26  ? 1345 ASP A CG    1 
ATOM   10215 O  OD1   . ASP A 1  1345 ? 109.858 129.438 125.926 1.00 45.50  ? 1345 ASP A OD1   1 
ATOM   10216 O  OD2   . ASP A 1  1345 ? 108.187 130.637 125.159 1.00 43.05  ? 1345 ASP A OD2   1 
ATOM   10217 N  N     . LYS A 1  1346 ? 110.831 127.208 124.358 1.00 39.45  ? 1346 LYS A N     1 
ATOM   10218 C  CA    . LYS A 1  1346 ? 111.791 126.862 123.312 1.00 39.64  ? 1346 LYS A CA    1 
ATOM   10219 C  C     . LYS A 1  1346 ? 112.679 125.701 123.727 1.00 38.94  ? 1346 LYS A C     1 
ATOM   10220 O  O     . LYS A 1  1346 ? 113.894 125.734 123.523 1.00 34.44  ? 1346 LYS A O     1 
ATOM   10221 C  CB    . LYS A 1  1346 ? 112.638 128.070 122.925 1.00 41.09  ? 1346 LYS A CB    1 
ATOM   10222 C  CG    . LYS A 1  1346 ? 111.990 128.991 121.911 1.00 40.52  ? 1346 LYS A CG    1 
ATOM   10223 C  CD    . LYS A 1  1346 ? 113.007 129.961 121.350 1.00 39.02  ? 1346 LYS A CD    1 
ATOM   10224 C  CE    . LYS A 1  1346 ? 112.386 130.870 120.307 1.00 40.03  ? 1346 LYS A CE    1 
ATOM   10225 N  NZ    . LYS A 1  1346 ? 113.379 131.820 119.731 1.00 39.07  ? 1346 LYS A NZ    1 
ATOM   10226 N  N     . GLY A 1  1347 ? 112.087 124.672 124.333 1.00 28.53  ? 1347 GLY A N     1 
ATOM   10227 C  CA    . GLY A 1  1347 ? 112.808 123.497 124.751 1.00 23.42  ? 1347 GLY A CA    1 
ATOM   10228 C  C     . GLY A 1  1347 ? 113.243 122.641 123.583 1.00 23.49  ? 1347 GLY A C     1 
ATOM   10229 O  O     . GLY A 1  1347 ? 112.795 122.821 122.449 1.00 28.83  ? 1347 GLY A O     1 
ATOM   10230 N  N     . PRO A 1  1348 ? 114.126 121.689 123.840 1.00 13.74  ? 1348 PRO A N     1 
ATOM   10231 C  CA    . PRO A 1  1348 ? 114.652 120.865 122.753 1.00 8.59   ? 1348 PRO A CA    1 
ATOM   10232 C  C     . PRO A 1  1348 ? 113.666 119.830 122.254 1.00 4.09   ? 1348 PRO A C     1 
ATOM   10233 O  O     . PRO A 1  1348 ? 112.534 119.752 122.731 1.00 8.73   ? 1348 PRO A O     1 
ATOM   10234 C  CB    . PRO A 1  1348 ? 115.873 120.202 123.394 1.00 5.34   ? 1348 PRO A CB    1 
ATOM   10235 C  CG    . PRO A 1  1348 ? 115.536 120.120 124.796 1.00 3.65   ? 1348 PRO A CG    1 
ATOM   10236 C  CD    . PRO A 1  1348 ? 114.744 121.343 125.124 1.00 10.74  ? 1348 PRO A CD    1 
ATOM   10237 N  N     . ASN A 1  1349 ? 114.088 119.032 121.284 1.00 1.71   ? 1349 ASN A N     1 
ATOM   10238 C  CA    . ASN A 1  1349 ? 113.288 117.902 120.867 1.00 12.66  ? 1349 ASN A CA    1 
ATOM   10239 C  C     . ASN A 1  1349 ? 113.116 116.940 122.035 1.00 5.83   ? 1349 ASN A C     1 
ATOM   10240 O  O     . ASN A 1  1349 ? 113.877 116.951 123.001 1.00 10.83  ? 1349 ASN A O     1 
ATOM   10241 C  CB    . ASN A 1  1349 ? 113.943 117.179 119.697 1.00 4.48   ? 1349 ASN A CB    1 
ATOM   10242 C  CG    . ASN A 1  1349 ? 112.951 116.465 118.846 1.00 0.97   ? 1349 ASN A CG    1 
ATOM   10243 O  OD1   . ASN A 1  1349 ? 111.969 117.047 118.416 1.00 16.24  ? 1349 ASN A OD1   1 
ATOM   10244 N  ND2   . ASN A 1  1349 ? 113.158 115.183 118.647 1.00 1.71   ? 1349 ASN A ND2   1 
ATOM   10245 N  N     . HIS A 1  1350 ? 112.101 116.089 121.931 1.00 2.81   ? 1350 HIS A N     1 
ATOM   10246 C  CA    . HIS A 1  1350 ? 111.771 115.203 123.036 1.00 6.18   ? 1350 HIS A CA    1 
ATOM   10247 C  C     . HIS A 1  1350 ? 112.798 114.091 123.212 1.00 4.34   ? 1350 HIS A C     1 
ATOM   10248 O  O     . HIS A 1  1350 ? 112.965 113.586 124.323 1.00 12.54  ? 1350 HIS A O     1 
ATOM   10249 C  CB    . HIS A 1  1350 ? 110.375 114.623 122.826 1.00 7.30   ? 1350 HIS A CB    1 
ATOM   10250 C  CG    . HIS A 1  1350 ? 109.861 113.861 124.004 1.00 4.13   ? 1350 HIS A CG    1 
ATOM   10251 N  ND1   . HIS A 1  1350 ? 109.551 114.465 125.198 1.00 6.01   ? 1350 HIS A ND1   1 
ATOM   10252 C  CD2   . HIS A 1  1350 ? 109.631 112.540 124.179 1.00 3.88   ? 1350 HIS A CD2   1 
ATOM   10253 C  CE1   . HIS A 1  1350 ? 109.145 113.551 126.057 1.00 1.29   ? 1350 HIS A CE1   1 
ATOM   10254 N  NE2   . HIS A 1  1350 ? 109.187 112.375 125.465 1.00 13.48  ? 1350 HIS A NE2   1 
ATOM   10255 N  N     . ARG A 1  1351 ? 113.495 113.699 122.146 1.00 9.64   ? 1351 ARG A N     1 
ATOM   10256 C  CA    . ARG A 1  1351 ? 114.422 112.579 122.234 1.00 3.20   ? 1351 ARG A CA    1 
ATOM   10257 C  C     . ARG A 1  1351 ? 115.692 112.920 122.993 1.00 4.15   ? 1351 ARG A C     1 
ATOM   10258 O  O     . ARG A 1  1351 ? 116.408 112.006 123.405 1.00 2.43   ? 1351 ARG A O     1 
ATOM   10259 C  CB    . ARG A 1  1351 ? 114.783 112.073 120.842 1.00 3.17   ? 1351 ARG A CB    1 
ATOM   10260 C  CG    . ARG A 1  1351 ? 115.731 112.960 120.049 1.00 1.74   ? 1351 ARG A CG    1 
ATOM   10261 C  CD    . ARG A 1  1351 ? 115.783 112.514 118.609 1.00 15.51  ? 1351 ARG A CD    1 
ATOM   10262 N  NE    . ARG A 1  1351 ? 114.457 112.531 118.010 1.00 1.55   ? 1351 ARG A NE    1 
ATOM   10263 C  CZ    . ARG A 1  1351 ? 113.766 111.454 117.669 1.00 3.72   ? 1351 ARG A CZ    1 
ATOM   10264 N  NH1   . ARG A 1  1351 ? 114.277 110.242 117.775 1.00 9.32   ? 1351 ARG A NH1   1 
ATOM   10265 N  NH2   . ARG A 1  1351 ? 112.528 111.598 117.217 1.00 1.77   ? 1351 ARG A NH2   1 
ATOM   10266 N  N     . HIS A 1  1352 ? 115.999 114.201 123.173 1.00 1.98   ? 1352 HIS A N     1 
ATOM   10267 C  CA    . HIS A 1  1352 ? 117.112 114.605 124.014 1.00 15.17  ? 1352 HIS A CA    1 
ATOM   10268 C  C     . HIS A 1  1352 ? 116.782 114.521 125.494 1.00 8.14   ? 1352 HIS A C     1 
ATOM   10269 O  O     . HIS A 1  1352 ? 117.694 114.387 126.307 1.00 5.46   ? 1352 HIS A O     1 
ATOM   10270 C  CB    . HIS A 1  1352 ? 117.556 116.025 123.663 1.00 5.28   ? 1352 HIS A CB    1 
ATOM   10271 C  CG    . HIS A 1  1352 ? 117.928 116.209 122.224 1.00 1.05   ? 1352 HIS A CG    1 
ATOM   10272 N  ND1   . HIS A 1  1352 ? 118.940 115.500 121.620 1.00 10.18  ? 1352 HIS A ND1   1 
ATOM   10273 C  CD2   . HIS A 1  1352 ? 117.409 117.007 121.266 1.00 13.26  ? 1352 HIS A CD2   1 
ATOM   10274 C  CE1   . HIS A 1  1352 ? 119.037 115.865 120.357 1.00 0.79   ? 1352 HIS A CE1   1 
ATOM   10275 N  NE2   . HIS A 1  1352 ? 118.115 116.774 120.117 1.00 9.53   ? 1352 HIS A NE2   1 
ATOM   10276 N  N     . LEU A 1  1353 ? 115.507 114.617 125.860 1.00 1.03   ? 1353 LEU A N     1 
ATOM   10277 C  CA    . LEU A 1  1353 ? 115.041 114.385 127.219 1.00 5.87   ? 1353 LEU A CA    1 
ATOM   10278 C  C     . LEU A 1  1353 ? 115.061 112.911 127.587 1.00 7.86   ? 1353 LEU A C     1 
ATOM   10279 O  O     . LEU A 1  1353 ? 115.372 112.566 128.727 1.00 10.52  ? 1353 LEU A O     1 
ATOM   10280 C  CB    . LEU A 1  1353 ? 113.619 114.920 127.394 1.00 2.45   ? 1353 LEU A CB    1 
ATOM   10281 C  CG    . LEU A 1  1353 ? 113.222 116.341 127.014 1.00 3.52   ? 1353 LEU A CG    1 
ATOM   10282 C  CD1   . LEU A 1  1353 ? 111.745 116.486 127.217 1.00 3.43   ? 1353 LEU A CD1   1 
ATOM   10283 C  CD2   . LEU A 1  1353 ? 113.952 117.344 127.854 1.00 4.70   ? 1353 LEU A CD2   1 
ATOM   10284 N  N     . LEU A 1  1354 ? 114.705 112.037 126.647 1.00 12.56  ? 1354 LEU A N     1 
ATOM   10285 C  CA    . LEU A 1  1354 ? 114.812 110.603 126.861 1.00 14.51  ? 1354 LEU A CA    1 
ATOM   10286 C  C     . LEU A 1  1354 ? 116.246 110.156 127.053 1.00 3.11   ? 1354 LEU A C     1 
ATOM   10287 O  O     . LEU A 1  1354 ? 116.476 109.111 127.654 1.00 3.71   ? 1354 LEU A O     1 
ATOM   10288 C  CB    . LEU A 1  1354 ? 114.210 109.847 125.686 1.00 5.61   ? 1354 LEU A CB    1 
ATOM   10289 C  CG    . LEU A 1  1354 ? 112.771 110.161 125.342 1.00 0.26   ? 1354 LEU A CG    1 
ATOM   10290 C  CD1   . LEU A 1  1354 ? 112.430 109.560 124.021 1.00 11.86  ? 1354 LEU A CD1   1 
ATOM   10291 C  CD2   . LEU A 1  1354 ? 111.904 109.607 126.413 1.00 0.17   ? 1354 LEU A CD2   1 
ATOM   10292 N  N     . MET A 1  1355 ? 117.210 110.905 126.530 1.00 0.35   ? 1355 MET A N     1 
ATOM   10293 C  CA    . MET A 1  1355 ? 118.609 110.587 126.746 1.00 1.85   ? 1355 MET A CA    1 
ATOM   10294 C  C     . MET A 1  1355 ? 119.015 110.793 128.197 1.00 0.15   ? 1355 MET A C     1 
ATOM   10295 O  O     . MET A 1  1355 ? 119.755 109.982 128.752 1.00 0.61   ? 1355 MET A O     1 
ATOM   10296 C  CB    . MET A 1  1355 ? 119.473 111.423 125.805 1.00 1.57   ? 1355 MET A CB    1 
ATOM   10297 C  CG    . MET A 1  1355 ? 120.702 110.697 125.310 1.00 1.72   ? 1355 MET A CG    1 
ATOM   10298 S  SD    . MET A 1  1355 ? 120.275 109.272 124.338 1.00 19.13  ? 1355 MET A SD    1 
ATOM   10299 C  CE    . MET A 1  1355 ? 121.063 108.063 125.354 1.00 10.00  ? 1355 MET A CE    1 
ATOM   10300 N  N     . TYR A 1  1356 ? 118.554 111.874 128.823 1.00 6.60   ? 1356 TYR A N     1 
ATOM   10301 C  CA    . TYR A 1  1356 ? 118.820 112.085 130.240 1.00 1.78   ? 1356 TYR A CA    1 
ATOM   10302 C  C     . TYR A 1  1356 ? 118.102 111.064 131.106 1.00 10.11  ? 1356 TYR A C     1 
ATOM   10303 O  O     . TYR A 1  1356 ? 118.700 110.483 132.010 1.00 5.45   ? 1356 TYR A O     1 
ATOM   10304 C  CB    . TYR A 1  1356 ? 118.389 113.481 130.654 1.00 2.17   ? 1356 TYR A CB    1 
ATOM   10305 C  CG    . TYR A 1  1356 ? 119.339 114.584 130.309 1.00 1.78   ? 1356 TYR A CG    1 
ATOM   10306 C  CD1   . TYR A 1  1356 ? 119.530 114.982 128.999 1.00 0.53   ? 1356 TYR A CD1   1 
ATOM   10307 C  CD2   . TYR A 1  1356 ? 120.036 115.241 131.297 1.00 1.39   ? 1356 TYR A CD2   1 
ATOM   10308 C  CE1   . TYR A 1  1356 ? 120.386 115.994 128.695 1.00 3.54   ? 1356 TYR A CE1   1 
ATOM   10309 C  CE2   . TYR A 1  1356 ? 120.891 116.249 130.996 1.00 7.82   ? 1356 TYR A CE2   1 
ATOM   10310 C  CZ    . TYR A 1  1356 ? 121.064 116.623 129.696 1.00 2.16   ? 1356 TYR A CZ    1 
ATOM   10311 O  OH    . TYR A 1  1356 ? 121.925 117.638 129.403 1.00 4.60   ? 1356 TYR A OH    1 
ATOM   10312 N  N     . ALA A 1  1357 ? 116.814 110.848 130.859 1.00 4.42   ? 1357 ALA A N     1 
ATOM   10313 C  CA    . ALA A 1  1357 ? 116.020 109.982 131.720 1.00 12.35  ? 1357 ALA A CA    1 
ATOM   10314 C  C     . ALA A 1  1357 ? 116.487 108.539 131.657 1.00 7.22   ? 1357 ALA A C     1 
ATOM   10315 O  O     . ALA A 1  1357 ? 116.527 107.852 132.678 1.00 6.96   ? 1357 ALA A O     1 
ATOM   10316 C  CB    . ALA A 1  1357 ? 114.549 110.077 131.336 1.00 4.86   ? 1357 ALA A CB    1 
ATOM   10317 N  N     . ASP A 1  1358 ? 116.825 108.053 130.468 1.00 6.16   ? 1358 ASP A N     1 
ATOM   10318 C  CA    . ASP A 1  1358 ? 117.206 106.656 130.321 1.00 3.82   ? 1358 ASP A CA    1 
ATOM   10319 C  C     . ASP A 1  1358 ? 118.605 106.382 130.848 1.00 10.06  ? 1358 ASP A C     1 
ATOM   10320 O  O     . ASP A 1  1358 ? 118.905 105.253 131.235 1.00 4.60   ? 1358 ASP A O     1 
ATOM   10321 C  CB    . ASP A 1  1358 ? 117.092 106.244 128.861 1.00 14.91  ? 1358 ASP A CB    1 
ATOM   10322 C  CG    . ASP A 1  1358 ? 115.760 105.608 128.542 1.00 7.74   ? 1358 ASP A CG    1 
ATOM   10323 O  OD1   . ASP A 1  1358 ? 114.785 106.339 128.321 1.00 12.26  ? 1358 ASP A OD1   1 
ATOM   10324 O  OD2   . ASP A 1  1358 ? 115.685 104.370 128.492 1.00 12.44  ? 1358 ASP A OD2   1 
ATOM   10325 N  N     . LEU A 1  1359 ? 119.474 107.387 130.852 1.00 3.66   ? 1359 LEU A N     1 
ATOM   10326 C  CA    . LEU A 1  1359 ? 120.807 107.217 131.410 1.00 2.16   ? 1359 LEU A CA    1 
ATOM   10327 C  C     . LEU A 1  1359 ? 120.773 107.203 132.931 1.00 2.04   ? 1359 LEU A C     1 
ATOM   10328 O  O     . LEU A 1  1359 ? 121.477 106.420 133.571 1.00 5.84   ? 1359 LEU A O     1 
ATOM   10329 C  CB    . LEU A 1  1359 ? 121.727 108.323 130.904 1.00 3.33   ? 1359 LEU A CB    1 
ATOM   10330 C  CG    . LEU A 1  1359 ? 123.084 108.346 131.604 1.00 1.67   ? 1359 LEU A CG    1 
ATOM   10331 C  CD1   . LEU A 1  1359 ? 124.086 107.506 130.866 1.00 13.86  ? 1359 LEU A CD1   1 
ATOM   10332 C  CD2   . LEU A 1  1359 ? 123.573 109.755 131.786 1.00 0.82   ? 1359 LEU A CD2   1 
ATOM   10333 N  N     . MET A 1  1360 ? 119.959 108.069 133.525 1.00 7.47   ? 1360 MET A N     1 
ATOM   10334 C  CA    . MET A 1  1360 ? 119.866 108.197 134.970 1.00 5.03   ? 1360 MET A CA    1 
ATOM   10335 C  C     . MET A 1  1360 ? 119.112 107.055 135.630 1.00 1.95   ? 1360 MET A C     1 
ATOM   10336 O  O     . MET A 1  1360 ? 119.131 106.961 136.858 1.00 9.06   ? 1360 MET A O     1 
ATOM   10337 C  CB    . MET A 1  1360 ? 119.194 109.515 135.327 1.00 2.75   ? 1360 MET A CB    1 
ATOM   10338 C  CG    . MET A 1  1360 ? 119.998 110.746 134.969 1.00 1.57   ? 1360 MET A CG    1 
ATOM   10339 S  SD    . MET A 1  1360 ? 118.986 112.230 134.994 1.00 15.15  ? 1360 MET A SD    1 
ATOM   10340 C  CE    . MET A 1  1360 ? 119.424 112.888 136.589 1.00 10.22  ? 1360 MET A CE    1 
ATOM   10341 N  N     . THR A 1  1361 ? 118.450 106.190 134.864 1.00 6.84   ? 1361 THR A N     1 
ATOM   10342 C  CA    . THR A 1  1361 ? 117.654 105.116 135.436 1.00 5.84   ? 1361 THR A CA    1 
ATOM   10343 C  C     . THR A 1  1361 ? 118.045 103.737 134.918 1.00 8.51   ? 1361 THR A C     1 
ATOM   10344 O  O     . THR A 1  1361 ? 117.329 102.771 135.181 1.00 5.20   ? 1361 THR A O     1 
ATOM   10345 C  CB    . THR A 1  1361 ? 116.158 105.358 135.181 1.00 1.61   ? 1361 THR A CB    1 
ATOM   10346 O  OG1   . THR A 1  1361 ? 115.910 105.456 133.778 1.00 4.69   ? 1361 THR A OG1   1 
ATOM   10347 C  CG2   . THR A 1  1361 ? 115.679 106.619 135.857 1.00 1.46   ? 1361 THR A CG2   1 
ATOM   10348 N  N     . ARG A 1  1362 ? 119.167 103.612 134.211 1.00 2.45   ? 1362 ARG A N     1 
ATOM   10349 C  CA    . ARG A 1  1362 ? 119.509 102.365 133.534 1.00 4.26   ? 1362 ARG A CA    1 
ATOM   10350 C  C     . ARG A 1  1362 ? 119.890 101.250 134.494 1.00 2.27   ? 1362 ARG A C     1 
ATOM   10351 O  O     . ARG A 1  1362 ? 119.851 100.080 134.110 1.00 2.53   ? 1362 ARG A O     1 
ATOM   10352 C  CB    . ARG A 1  1362 ? 120.643 102.611 132.543 1.00 0.72   ? 1362 ARG A CB    1 
ATOM   10353 C  CG    . ARG A 1  1362 ? 122.029 102.408 133.106 1.00 8.39   ? 1362 ARG A CG    1 
ATOM   10354 C  CD    . ARG A 1  1362 ? 122.993 101.990 132.037 1.00 5.83   ? 1362 ARG A CD    1 
ATOM   10355 N  NE    . ARG A 1  1362 ? 122.706 100.657 131.529 1.00 5.21   ? 1362 ARG A NE    1 
ATOM   10356 C  CZ    . ARG A 1  1362 ? 122.997 99.534  132.162 1.00 10.79  ? 1362 ARG A CZ    1 
ATOM   10357 N  NH1   . ARG A 1  1362 ? 123.572 99.541  133.346 1.00 3.50   ? 1362 ARG A NH1   1 
ATOM   10358 N  NH2   . ARG A 1  1362 ? 122.700 98.377  131.595 1.00 0.59   ? 1362 ARG A NH2   1 
ATOM   10359 N  N     . THR A 1  1363 ? 120.238 101.582 135.730 1.00 8.58   ? 1363 THR A N     1 
ATOM   10360 C  CA    . THR A 1  1363 ? 120.670 100.614 136.725 1.00 13.34  ? 1363 THR A CA    1 
ATOM   10361 C  C     . THR A 1  1363 ? 119.543 100.116 137.616 1.00 3.61   ? 1363 THR A C     1 
ATOM   10362 O  O     . THR A 1  1363 ? 119.793 99.286  138.489 1.00 11.46  ? 1363 THR A O     1 
ATOM   10363 C  CB    . THR A 1  1363 ? 121.758 101.229 137.601 1.00 0.89   ? 1363 THR A CB    1 
ATOM   10364 O  OG1   . THR A 1  1363 ? 121.317 102.509 138.053 1.00 10.27  ? 1363 THR A OG1   1 
ATOM   10365 C  CG2   . THR A 1  1363 ? 123.033 101.413 136.823 1.00 1.72   ? 1363 THR A CG2   1 
ATOM   10366 N  N     . GLY A 1  1364 ? 118.317 100.586 137.424 1.00 4.42   ? 1364 GLY A N     1 
ATOM   10367 C  CA    . GLY A 1  1364 ? 117.213 100.240 138.288 1.00 4.14   ? 1364 GLY A CA    1 
ATOM   10368 C  C     . GLY A 1  1364 ? 117.033 101.173 139.460 1.00 8.59   ? 1364 GLY A C     1 
ATOM   10369 O  O     . GLY A 1  1364 ? 116.049 101.045 140.189 1.00 13.06  ? 1364 GLY A O     1 
ATOM   10370 N  N     . GLN A 1  1365 ? 117.964 102.094 139.658 1.00 5.35   ? 1365 GLN A N     1 
ATOM   10371 C  CA    . GLN A 1  1365 ? 117.890 103.134 140.663 1.00 5.38   ? 1365 GLN A CA    1 
ATOM   10372 C  C     . GLN A 1  1365 ? 118.104 104.462 139.965 1.00 8.88   ? 1365 GLN A C     1 
ATOM   10373 O  O     . GLN A 1  1365 ? 118.513 104.510 138.807 1.00 14.19  ? 1365 GLN A O     1 
ATOM   10374 C  CB    . GLN A 1  1365 ? 118.941 102.941 141.757 1.00 6.36   ? 1365 GLN A CB    1 
ATOM   10375 C  CG    . GLN A 1  1365 ? 118.624 101.846 142.749 1.00 10.44  ? 1365 GLN A CG    1 
ATOM   10376 C  CD    . GLN A 1  1365 ? 119.232 100.510 142.372 1.00 18.01  ? 1365 GLN A CD    1 
ATOM   10377 O  OE1   . GLN A 1  1365 ? 118.539 99.497  142.313 1.00 17.03  ? 1365 GLN A OE1   1 
ATOM   10378 N  NE2   . GLN A 1  1365 ? 120.533 100.501 142.111 1.00 16.99  ? 1365 GLN A NE2   1 
ATOM   10379 N  N     . VAL A 1  1366 ? 117.828 105.551 140.671 1.00 4.13   ? 1366 VAL A N     1 
ATOM   10380 C  CA    . VAL A 1  1366 ? 118.056 106.874 140.107 1.00 3.02   ? 1366 VAL A CA    1 
ATOM   10381 C  C     . VAL A 1  1366 ? 119.447 107.332 140.525 1.00 3.20   ? 1366 VAL A C     1 
ATOM   10382 O  O     . VAL A 1  1366 ? 119.723 107.509 141.710 1.00 11.96  ? 1366 VAL A O     1 
ATOM   10383 C  CB    . VAL A 1  1366 ? 116.982 107.873 140.543 1.00 5.91   ? 1366 VAL A CB    1 
ATOM   10384 C  CG1   . VAL A 1  1366 ? 117.223 109.213 139.886 1.00 1.53   ? 1366 VAL A CG1   1 
ATOM   10385 C  CG2   . VAL A 1  1366 ? 115.611 107.352 140.186 1.00 6.26   ? 1366 VAL A CG2   1 
ATOM   10386 N  N     . THR A 1  1367 ? 120.328 107.504 139.550 1.00 3.97   ? 1367 THR A N     1 
ATOM   10387 C  CA    . THR A 1  1367 ? 121.671 108.015 139.757 1.00 9.67   ? 1367 THR A CA    1 
ATOM   10388 C  C     . THR A 1  1367 ? 121.762 109.445 139.242 1.00 8.29   ? 1367 THR A C     1 
ATOM   10389 O  O     . THR A 1  1367 ? 120.972 109.881 138.409 1.00 11.96  ? 1367 THR A O     1 
ATOM   10390 C  CB    . THR A 1  1367 ? 122.711 107.136 139.060 1.00 6.80   ? 1367 THR A CB    1 
ATOM   10391 O  OG1   . THR A 1  1367 ? 122.421 107.072 137.664 1.00 14.83  ? 1367 THR A OG1   1 
ATOM   10392 C  CG2   . THR A 1  1367 ? 122.699 105.735 139.617 1.00 1.46   ? 1367 THR A CG2   1 
ATOM   10393 N  N     . SER A 1  1368 ? 122.737 110.174 139.758 1.00 8.08   ? 1368 SER A N     1 
ATOM   10394 C  CA    . SER A 1  1368 ? 122.890 111.584 139.456 1.00 7.68   ? 1368 SER A CA    1 
ATOM   10395 C  C     . SER A 1  1368 ? 123.764 111.810 138.227 1.00 13.32  ? 1368 SER A C     1 
ATOM   10396 O  O     . SER A 1  1368 ? 124.338 110.887 137.650 1.00 16.47  ? 1368 SER A O     1 
ATOM   10397 C  CB    . SER A 1  1368 ? 123.487 112.308 140.651 1.00 12.78  ? 1368 SER A CB    1 
ATOM   10398 O  OG    . SER A 1  1368 ? 124.724 111.738 141.015 1.00 16.13  ? 1368 SER A OG    1 
ATOM   10399 N  N     . LEU A 1  1369 ? 123.839 113.071 137.816 1.00 10.90  ? 1369 LEU A N     1 
ATOM   10400 C  CA    . LEU A 1  1369 ? 124.813 113.538 136.847 1.00 9.84   ? 1369 LEU A CA    1 
ATOM   10401 C  C     . LEU A 1  1369 ? 126.001 114.193 137.513 1.00 18.61  ? 1369 LEU A C     1 
ATOM   10402 O  O     . LEU A 1  1369 ? 126.531 115.174 136.989 1.00 22.79  ? 1369 LEU A O     1 
ATOM   10403 C  CB    . LEU A 1  1369 ? 124.173 114.512 135.864 1.00 8.68   ? 1369 LEU A CB    1 
ATOM   10404 C  CG    . LEU A 1  1369 ? 123.413 113.929 134.684 1.00 11.64  ? 1369 LEU A CG    1 
ATOM   10405 C  CD1   . LEU A 1  1369 ? 122.848 115.058 133.869 1.00 10.94  ? 1369 LEU A CD1   1 
ATOM   10406 C  CD2   . LEU A 1  1369 ? 124.328 113.079 133.843 1.00 13.01  ? 1369 LEU A CD2   1 
ATOM   10407 N  N     . GLU A 1  1370 ? 126.382 113.716 138.687 1.00 16.52  ? 1370 GLU A N     1 
ATOM   10408 C  CA    . GLU A 1  1370 ? 127.563 114.168 139.393 1.00 12.47  ? 1370 GLU A CA    1 
ATOM   10409 C  C     . GLU A 1  1370 ? 128.590 113.049 139.448 1.00 16.70  ? 1370 GLU A C     1 
ATOM   10410 O  O     . GLU A 1  1370 ? 128.427 111.985 138.854 1.00 19.80  ? 1370 GLU A O     1 
ATOM   10411 C  CB    . GLU A 1  1370 ? 127.201 114.643 140.795 1.00 18.96  ? 1370 GLU A CB    1 
ATOM   10412 C  CG    . GLU A 1  1370 ? 125.931 115.434 140.866 1.00 18.72  ? 1370 GLU A CG    1 
ATOM   10413 C  CD    . GLU A 1  1370 ? 126.173 116.914 140.713 1.00 25.60  ? 1370 GLU A CD    1 
ATOM   10414 O  OE1   . GLU A 1  1370 ? 126.979 117.469 141.485 1.00 17.90  ? 1370 GLU A OE1   1 
ATOM   10415 O  OE2   . GLU A 1  1370 ? 125.548 117.530 139.822 1.00 27.71  ? 1370 GLU A OE2   1 
ATOM   10416 N  N     . LYS A 1  1371 ? 129.664 113.300 140.189 1.00 19.53  ? 1371 LYS A N     1 
ATOM   10417 C  CA    . LYS A 1  1371 ? 130.747 112.334 140.297 1.00 18.93  ? 1371 LYS A CA    1 
ATOM   10418 C  C     . LYS A 1  1371 ? 130.291 111.037 140.951 1.00 16.97  ? 1371 LYS A C     1 
ATOM   10419 O  O     . LYS A 1  1371 ? 130.857 109.976 140.679 1.00 17.78  ? 1371 LYS A O     1 
ATOM   10420 C  CB    . LYS A 1  1371 ? 131.906 112.969 141.062 1.00 19.90  ? 1371 LYS A CB    1 
ATOM   10421 C  CG    . LYS A 1  1371 ? 132.508 112.124 142.141 1.00 20.63  ? 1371 LYS A CG    1 
ATOM   10422 C  CD    . LYS A 1  1371 ? 133.608 112.870 142.856 1.00 20.45  ? 1371 LYS A CD    1 
ATOM   10423 C  CE    . LYS A 1  1371 ? 133.060 113.792 143.915 1.00 21.15  ? 1371 LYS A CE    1 
ATOM   10424 N  NZ    . LYS A 1  1371 ? 134.056 114.000 144.997 1.00 24.47  ? 1371 LYS A NZ    1 
ATOM   10425 N  N     . ALA A 1  1372 ? 129.274 111.097 141.807 1.00 14.86  ? 1372 ALA A N     1 
ATOM   10426 C  CA    . ALA A 1  1372 ? 128.769 109.887 142.444 1.00 14.22  ? 1372 ALA A CA    1 
ATOM   10427 C  C     . ALA A 1  1372 ? 128.039 108.994 141.451 1.00 16.58  ? 1372 ALA A C     1 
ATOM   10428 O  O     . ALA A 1  1372 ? 128.174 107.769 141.497 1.00 12.68  ? 1372 ALA A O     1 
ATOM   10429 C  CB    . ALA A 1  1372 ? 127.854 110.256 143.608 1.00 13.22  ? 1372 ALA A CB    1 
ATOM   10430 N  N     . GLY A 1  1373 ? 127.242 109.590 140.561 1.00 17.52  ? 1373 GLY A N     1 
ATOM   10431 C  CA    . GLY A 1  1373 ? 126.537 108.805 139.559 1.00 8.83   ? 1373 GLY A CA    1 
ATOM   10432 C  C     . GLY A 1  1373 ? 127.462 108.192 138.528 1.00 8.52   ? 1373 GLY A C     1 
ATOM   10433 O  O     . GLY A 1  1373 ? 127.216 107.089 138.041 1.00 8.93   ? 1373 GLY A O     1 
ATOM   10434 N  N     . LEU A 1  1374 ? 128.530 108.904 138.174 1.00 11.65  ? 1374 LEU A N     1 
ATOM   10435 C  CA    . LEU A 1  1374 ? 129.520 108.363 137.252 1.00 8.06   ? 1374 LEU A CA    1 
ATOM   10436 C  C     . LEU A 1  1374 ? 130.222 107.154 137.845 1.00 11.22  ? 1374 LEU A C     1 
ATOM   10437 O  O     . LEU A 1  1374 ? 130.573 106.215 137.127 1.00 15.46  ? 1374 LEU A O     1 
ATOM   10438 C  CB    . LEU A 1  1374 ? 130.533 109.442 136.896 1.00 12.98  ? 1374 LEU A CB    1 
ATOM   10439 C  CG    . LEU A 1  1374 ? 131.317 109.273 135.601 1.00 7.62   ? 1374 LEU A CG    1 
ATOM   10440 C  CD1   . LEU A 1  1374 ? 130.384 109.280 134.419 1.00 5.59   ? 1374 LEU A CD1   1 
ATOM   10441 C  CD2   . LEU A 1  1374 ? 132.341 110.374 135.489 1.00 8.11   ? 1374 LEU A CD2   1 
ATOM   10442 N  N     . ASN A 1  1375 ? 130.454 107.171 139.156 1.00 12.31  ? 1375 ASN A N     1 
ATOM   10443 C  CA    . ASN A 1  1375 ? 131.050 106.026 139.829 1.00 7.34   ? 1375 ASN A CA    1 
ATOM   10444 C  C     . ASN A 1  1375 ? 130.089 104.847 139.878 1.00 9.74   ? 1375 ASN A C     1 
ATOM   10445 O  O     . ASN A 1  1375 ? 130.516 103.691 139.906 1.00 15.93  ? 1375 ASN A O     1 
ATOM   10446 C  CB    . ASN A 1  1375 ? 131.478 106.436 141.233 1.00 11.15  ? 1375 ASN A CB    1 
ATOM   10447 C  CG    . ASN A 1  1375 ? 132.417 105.451 141.867 1.00 16.42  ? 1375 ASN A CG    1 
ATOM   10448 O  OD1   . ASN A 1  1375 ? 132.873 104.509 141.229 1.00 22.33  ? 1375 ASN A OD1   1 
ATOM   10449 N  ND2   . ASN A 1  1375 ? 132.699 105.650 143.140 1.00 16.23  ? 1375 ASN A ND2   1 
ATOM   10450 N  N     . ALA A 1  1376 ? 128.787 105.117 139.911 1.00 12.99  ? 1376 ALA A N     1 
ATOM   10451 C  CA    . ALA A 1  1376 ? 127.806 104.042 139.984 1.00 8.39   ? 1376 ALA A CA    1 
ATOM   10452 C  C     . ALA A 1  1376 ? 127.583 103.383 138.630 1.00 11.89  ? 1376 ALA A C     1 
ATOM   10453 O  O     . ALA A 1  1376 ? 127.309 102.182 138.560 1.00 10.71  ? 1376 ALA A O     1 
ATOM   10454 C  CB    . ALA A 1  1376 ? 126.494 104.579 140.541 1.00 7.69   ? 1376 ALA A CB    1 
ATOM   10455 N  N     . ARG A 1  1377 ? 127.675 104.155 137.544 1.00 8.76   ? 1377 ARG A N     1 
ATOM   10456 C  CA    . ARG A 1  1377 ? 127.359 103.641 136.218 1.00 6.02   ? 1377 ARG A CA    1 
ATOM   10457 C  C     . ARG A 1  1377 ? 128.577 103.073 135.508 1.00 12.39  ? 1377 ARG A C     1 
ATOM   10458 O  O     . ARG A 1  1377 ? 128.468 102.061 134.811 1.00 9.73   ? 1377 ARG A O     1 
ATOM   10459 C  CB    . ARG A 1  1377 ? 126.736 104.736 135.362 1.00 6.46   ? 1377 ARG A CB    1 
ATOM   10460 C  CG    . ARG A 1  1377 ? 125.344 105.134 135.763 1.00 8.46   ? 1377 ARG A CG    1 
ATOM   10461 C  CD    . ARG A 1  1377 ? 124.777 106.107 134.773 1.00 2.31   ? 1377 ARG A CD    1 
ATOM   10462 N  NE    . ARG A 1  1377 ? 125.556 107.333 134.695 1.00 7.97   ? 1377 ARG A NE    1 
ATOM   10463 C  CZ    . ARG A 1  1377 ? 125.236 108.462 135.305 1.00 6.78   ? 1377 ARG A CZ    1 
ATOM   10464 N  NH1   . ARG A 1  1377 ? 124.157 108.555 136.054 1.00 7.48   ? 1377 ARG A NH1   1 
ATOM   10465 N  NH2   . ARG A 1  1377 ? 126.016 109.525 135.153 1.00 5.15   ? 1377 ARG A NH2   1 
ATOM   10466 N  N     . GLU A 1  1378 ? 129.728 103.728 135.625 1.00 15.46  ? 1378 GLU A N     1 
ATOM   10467 C  CA    . GLU A 1  1378 ? 130.956 103.304 134.954 1.00 7.28   ? 1378 GLU A CA    1 
ATOM   10468 C  C     . GLU A 1  1378 ? 132.093 103.305 135.961 1.00 11.10  ? 1378 GLU A C     1 
ATOM   10469 O  O     . GLU A 1  1378 ? 132.976 104.167 135.913 1.00 5.90   ? 1378 GLU A O     1 
ATOM   10470 C  CB    . GLU A 1  1378 ? 131.289 104.213 133.773 1.00 4.55   ? 1378 GLU A CB    1 
ATOM   10471 C  CG    . GLU A 1  1378 ? 130.082 104.779 133.074 1.00 4.63   ? 1378 GLU A CG    1 
ATOM   10472 C  CD    . GLU A 1  1378 ? 130.427 105.591 131.854 1.00 10.91  ? 1378 GLU A CD    1 
ATOM   10473 O  OE1   . GLU A 1  1378 ? 131.489 105.360 131.257 1.00 14.36  ? 1378 GLU A OE1   1 
ATOM   10474 O  OE2   . GLU A 1  1378 ? 129.638 106.481 131.502 1.00 15.95  ? 1378 GLU A OE2   1 
ATOM   10475 N  N     . PRO A 1  1379 ? 132.107 102.349 136.891 1.00 10.53  ? 1379 PRO A N     1 
ATOM   10476 C  CA    . PRO A 1  1379 ? 133.178 102.342 137.896 1.00 6.03   ? 1379 PRO A CA    1 
ATOM   10477 C  C     . PRO A 1  1379 ? 134.548 101.986 137.341 1.00 8.73   ? 1379 PRO A C     1 
ATOM   10478 O  O     . PRO A 1  1379 ? 135.548 102.544 137.804 1.00 11.12  ? 1379 PRO A O     1 
ATOM   10479 C  CB    . PRO A 1  1379 ? 132.686 101.306 138.911 1.00 5.16   ? 1379 PRO A CB    1 
ATOM   10480 C  CG    . PRO A 1  1379 ? 131.795 100.425 138.145 1.00 7.33   ? 1379 PRO A CG    1 
ATOM   10481 C  CD    . PRO A 1  1379 ? 131.153 101.245 137.089 1.00 6.35   ? 1379 PRO A CD    1 
ATOM   10482 N  N     . SER A 1  1380 ? 134.634 101.089 136.362 1.00 9.73   ? 1380 SER A N     1 
ATOM   10483 C  CA    . SER A 1  1380 ? 135.925 100.658 135.846 1.00 7.88   ? 1380 SER A CA    1 
ATOM   10484 C  C     . SER A 1  1380 ? 136.568 101.672 134.915 1.00 9.20   ? 1380 SER A C     1 
ATOM   10485 O  O     . SER A 1  1380 ? 137.727 101.491 134.539 1.00 14.79  ? 1380 SER A O     1 
ATOM   10486 C  CB    . SER A 1  1380 ? 135.785 99.328  135.117 1.00 6.74   ? 1380 SER A CB    1 
ATOM   10487 O  OG    . SER A 1  1380 ? 134.584 99.287  134.377 1.00 19.43  ? 1380 SER A OG    1 
ATOM   10488 N  N     . ASN A 1  1381 ? 135.854 102.722 134.532 1.00 5.53   ? 1381 ASN A N     1 
ATOM   10489 C  CA    . ASN A 1  1381 ? 136.401 103.771 133.679 1.00 3.02   ? 1381 ASN A CA    1 
ATOM   10490 C  C     . ASN A 1  1381 ? 137.128 104.775 134.559 1.00 15.68  ? 1381 ASN A C     1 
ATOM   10491 O  O     . ASN A 1  1381 ? 136.609 105.833 134.894 1.00 4.55   ? 1381 ASN A O     1 
ATOM   10492 C  CB    . ASN A 1  1381 ? 135.295 104.434 132.875 1.00 1.75   ? 1381 ASN A CB    1 
ATOM   10493 C  CG    . ASN A 1  1381 ? 135.770 104.960 131.546 1.00 1.74   ? 1381 ASN A CG    1 
ATOM   10494 O  OD1   . ASN A 1  1381 ? 136.942 104.888 131.219 1.00 7.40   ? 1381 ASN A OD1   1 
ATOM   10495 N  ND2   . ASN A 1  1381 ? 134.850 105.483 130.765 1.00 2.48   ? 1381 ASN A ND2   1 
ATOM   10496 N  N     . VAL A 1  1382 ? 138.357 104.434 134.931 1.00 1.40   ? 1382 VAL A N     1 
ATOM   10497 C  CA    . VAL A 1  1382 ? 139.183 105.330 135.732 1.00 7.22   ? 1382 VAL A CA    1 
ATOM   10498 C  C     . VAL A 1  1382 ? 139.538 106.584 134.948 1.00 6.78   ? 1382 VAL A C     1 
ATOM   10499 O  O     . VAL A 1  1382 ? 139.523 107.692 135.491 1.00 5.86   ? 1382 VAL A O     1 
ATOM   10500 C  CB    . VAL A 1  1382 ? 140.441 104.588 136.213 1.00 3.24   ? 1382 VAL A CB    1 
ATOM   10501 C  CG1   . VAL A 1  1382 ? 141.346 105.518 136.996 1.00 9.40   ? 1382 VAL A CG1   1 
ATOM   10502 C  CG2   . VAL A 1  1382 ? 140.051 103.383 137.025 1.00 0.51   ? 1382 VAL A CG2   1 
ATOM   10503 N  N     . LEU A 1  1383 ? 139.868 106.433 133.666 1.00 1.89   ? 1383 LEU A N     1 
ATOM   10504 C  CA    . LEU A 1  1383 ? 140.326 107.568 132.875 1.00 9.13   ? 1383 LEU A CA    1 
ATOM   10505 C  C     . LEU A 1  1383 ? 139.234 108.604 132.661 1.00 3.91   ? 1383 LEU A C     1 
ATOM   10506 O  O     . LEU A 1  1383 ? 139.524 109.801 132.665 1.00 11.04  ? 1383 LEU A O     1 
ATOM   10507 C  CB    . LEU A 1  1383 ? 140.876 107.086 131.536 1.00 7.08   ? 1383 LEU A CB    1 
ATOM   10508 C  CG    . LEU A 1  1383 ? 142.245 106.412 131.589 1.00 0.85   ? 1383 LEU A CG    1 
ATOM   10509 C  CD1   . LEU A 1  1383 ? 142.540 105.714 130.299 1.00 0.18   ? 1383 LEU A CD1   1 
ATOM   10510 C  CD2   . LEU A 1  1383 ? 143.305 107.415 131.903 1.00 1.02   ? 1383 LEU A CD2   1 
ATOM   10511 N  N     . LEU A 1  1384 ? 137.987 108.179 132.449 1.00 0.72   ? 1384 LEU A N     1 
ATOM   10512 C  CA    . LEU A 1  1384 ? 136.892 109.137 132.339 1.00 15.54  ? 1384 LEU A CA    1 
ATOM   10513 C  C     . LEU A 1  1384 ? 136.646 109.859 133.655 1.00 1.16   ? 1384 LEU A C     1 
ATOM   10514 O  O     . LEU A 1  1384 ? 136.414 111.069 133.669 1.00 4.95   ? 1384 LEU A O     1 
ATOM   10515 C  CB    . LEU A 1  1384 ? 135.620 108.435 131.876 1.00 4.59   ? 1384 LEU A CB    1 
ATOM   10516 C  CG    . LEU A 1  1384 ? 134.271 109.148 132.006 1.00 1.63   ? 1384 LEU A CG    1 
ATOM   10517 C  CD1   . LEU A 1  1384 ? 134.187 110.335 131.107 1.00 1.27   ? 1384 LEU A CD1   1 
ATOM   10518 C  CD2   . LEU A 1  1384 ? 133.177 108.196 131.698 1.00 0.70   ? 1384 LEU A CD2   1 
ATOM   10519 N  N     . ARG A 1  1385 ? 136.702 109.137 134.770 1.00 4.89   ? 1385 ARG A N     1 
ATOM   10520 C  CA    . ARG A 1  1385 ? 136.412 109.733 136.068 1.00 8.94   ? 1385 ARG A CA    1 
ATOM   10521 C  C     . ARG A 1  1385 ? 137.541 110.622 136.565 1.00 1.02   ? 1385 ARG A C     1 
ATOM   10522 O  O     . ARG A 1  1385 ? 137.295 111.542 137.346 1.00 7.00   ? 1385 ARG A O     1 
ATOM   10523 C  CB    . ARG A 1  1385 ? 136.101 108.633 137.069 1.00 1.80   ? 1385 ARG A CB    1 
ATOM   10524 C  CG    . ARG A 1  1385 ? 134.810 107.923 136.752 1.00 5.61   ? 1385 ARG A CG    1 
ATOM   10525 C  CD    . ARG A 1  1385 ? 134.718 106.585 137.422 1.00 5.02   ? 1385 ARG A CD    1 
ATOM   10526 N  NE    . ARG A 1  1385 ? 135.041 106.681 138.833 1.00 9.65   ? 1385 ARG A NE    1 
ATOM   10527 C  CZ    . ARG A 1  1385 ? 135.946 105.931 139.437 1.00 8.74   ? 1385 ARG A CZ    1 
ATOM   10528 N  NH1   . ARG A 1  1385 ? 136.606 104.992 138.787 1.00 5.98   ? 1385 ARG A NH1   1 
ATOM   10529 N  NH2   . ARG A 1  1385 ? 136.197 106.133 140.724 1.00 13.33  ? 1385 ARG A NH2   1 
ATOM   10530 N  N     . MET A 1  1386 ? 138.775 110.371 136.132 1.00 10.13  ? 1386 MET A N     1 
ATOM   10531 C  CA    . MET A 1  1386 ? 139.875 111.281 136.439 1.00 2.00   ? 1386 MET A CA    1 
ATOM   10532 C  C     . MET A 1  1386 ? 139.708 112.610 135.719 1.00 4.98   ? 1386 MET A C     1 
ATOM   10533 O  O     . MET A 1  1386 ? 140.070 113.661 136.251 1.00 13.71  ? 1386 MET A O     1 
ATOM   10534 C  CB    . MET A 1  1386 ? 141.205 110.646 136.048 1.00 1.90   ? 1386 MET A CB    1 
ATOM   10535 C  CG    . MET A 1  1386 ? 141.882 109.867 137.129 1.00 8.85   ? 1386 MET A CG    1 
ATOM   10536 S  SD    . MET A 1  1386 ? 143.154 108.797 136.465 1.00 22.29  ? 1386 MET A SD    1 
ATOM   10537 C  CE    . MET A 1  1386 ? 144.574 109.864 136.606 1.00 9.19   ? 1386 MET A CE    1 
ATOM   10538 N  N     . ALA A 1  1387 ? 139.174 112.580 134.498 1.00 9.20   ? 1387 ALA A N     1 
ATOM   10539 C  CA    . ALA A 1  1387 ? 139.062 113.789 133.695 1.00 7.79   ? 1387 ALA A CA    1 
ATOM   10540 C  C     . ALA A 1  1387 ? 137.968 114.718 134.204 1.00 3.67   ? 1387 ALA A C     1 
ATOM   10541 O  O     . ALA A 1  1387 ? 137.969 115.907 133.880 1.00 15.74  ? 1387 ALA A O     1 
ATOM   10542 C  CB    . ALA A 1  1387 ? 138.811 113.420 132.236 1.00 0.71   ? 1387 ALA A CB    1 
ATOM   10543 N  N     . LEU A 1  1388 ? 137.027 114.204 134.992 1.00 2.49   ? 1388 LEU A N     1 
ATOM   10544 C  CA    . LEU A 1  1388 ? 135.952 115.029 135.523 1.00 5.65   ? 1388 LEU A CA    1 
ATOM   10545 C  C     . LEU A 1  1388 ? 136.369 115.894 136.709 1.00 14.61  ? 1388 LEU A C     1 
ATOM   10546 O  O     . LEU A 1  1388 ? 136.395 117.121 136.598 1.00 13.61  ? 1388 LEU A O     1 
ATOM   10547 C  CB    . LEU A 1  1388 ? 134.772 114.142 135.928 1.00 7.36   ? 1388 LEU A CB    1 
ATOM   10548 C  CG    . LEU A 1  1388 ? 133.552 114.780 136.605 1.00 3.83   ? 1388 LEU A CG    1 
ATOM   10549 C  CD1   . LEU A 1  1388 ? 132.908 115.823 135.727 1.00 9.44   ? 1388 LEU A CD1   1 
ATOM   10550 C  CD2   . LEU A 1  1388 ? 132.544 113.735 137.001 1.00 4.97   ? 1388 LEU A CD2   1 
ATOM   10551 N  N     . SER A 1  1389 ? 136.700 115.282 137.847 1.00 17.48  ? 1389 SER A N     1 
ATOM   10552 C  CA    . SER A 1  1389 ? 136.673 116.014 139.110 1.00 17.84  ? 1389 SER A CA    1 
ATOM   10553 C  C     . SER A 1  1389 ? 137.998 116.029 139.860 1.00 22.21  ? 1389 SER A C     1 
ATOM   10554 O  O     . SER A 1  1389 ? 138.511 117.113 140.157 1.00 25.55  ? 1389 SER A O     1 
ATOM   10555 C  CB    . SER A 1  1389 ? 135.560 115.442 139.996 1.00 22.58  ? 1389 SER A CB    1 
ATOM   10556 O  OG    . SER A 1  1389 ? 135.761 114.059 140.221 1.00 29.83  ? 1389 SER A OG    1 
ATOM   10557 N  N     . SER A 1  1390 ? 138.573 114.878 140.195 1.00 19.90  ? 1390 SER A N     1 
ATOM   10558 C  CA    . SER A 1  1390 ? 139.718 114.843 141.106 1.00 21.35  ? 1390 SER A CA    1 
ATOM   10559 C  C     . SER A 1  1390 ? 140.612 113.687 140.731 1.00 19.85  ? 1390 SER A C     1 
ATOM   10560 O  O     . SER A 1  1390 ? 140.406 112.552 141.175 1.00 17.69  ? 1390 SER A O     1 
ATOM   10561 C  CB    . SER A 1  1390 ? 139.279 114.722 142.561 1.00 20.23  ? 1390 SER A CB    1 
ATOM   10562 O  OG    . SER A 1  1390 ? 138.753 113.437 142.810 1.00 28.41  ? 1390 SER A OG    1 
ATOM   10563 N  N     . PRO A 1  1391 ? 141.642 113.940 139.929 1.00 11.70  ? 1391 PRO A N     1 
ATOM   10564 C  CA    . PRO A 1  1391 ? 142.433 112.827 139.394 1.00 11.70  ? 1391 PRO A CA    1 
ATOM   10565 C  C     . PRO A 1  1391 ? 143.235 112.067 140.432 1.00 14.32  ? 1391 PRO A C     1 
ATOM   10566 O  O     . PRO A 1  1391 ? 143.352 110.845 140.327 1.00 18.84  ? 1391 PRO A O     1 
ATOM   10567 C  CB    . PRO A 1  1391 ? 143.334 113.521 138.368 1.00 12.75  ? 1391 PRO A CB    1 
ATOM   10568 C  CG    . PRO A 1  1391 ? 143.390 114.920 138.796 1.00 18.08  ? 1391 PRO A CG    1 
ATOM   10569 C  CD    . PRO A 1  1391 ? 142.080 115.236 139.398 1.00 12.63  ? 1391 PRO A CD    1 
ATOM   10570 N  N     . VAL A 1  1392 ? 143.795 112.749 141.432 1.00 17.33  ? 1392 VAL A N     1 
ATOM   10571 C  CA    . VAL A 1  1392 ? 144.697 112.084 142.367 1.00 15.69  ? 1392 VAL A CA    1 
ATOM   10572 C  C     . VAL A 1  1392 ? 143.943 111.091 143.243 1.00 15.67  ? 1392 VAL A C     1 
ATOM   10573 O  O     . VAL A 1  1392 ? 144.424 109.983 143.494 1.00 19.09  ? 1392 VAL A O     1 
ATOM   10574 C  CB    . VAL A 1  1392 ? 145.458 113.129 143.200 1.00 20.61  ? 1392 VAL A CB    1 
ATOM   10575 C  CG1   . VAL A 1  1392 ? 146.413 112.457 144.162 1.00 15.90  ? 1392 VAL A CG1   1 
ATOM   10576 C  CG2   . VAL A 1  1392 ? 146.214 114.067 142.286 1.00 16.59  ? 1392 VAL A CG2   1 
ATOM   10577 N  N     . GLN A 1  1393 ? 142.761 111.468 143.731 1.00 16.34  ? 1393 GLN A N     1 
ATOM   10578 C  CA    . GLN A 1  1393 ? 141.951 110.536 144.508 1.00 11.89  ? 1393 GLN A CA    1 
ATOM   10579 C  C     . GLN A 1  1393 ? 141.476 109.358 143.663 1.00 21.04  ? 1393 GLN A C     1 
ATOM   10580 O  O     . GLN A 1  1393 ? 141.513 108.211 144.117 1.00 21.52  ? 1393 GLN A O     1 
ATOM   10581 C  CB    . GLN A 1  1393 ? 140.766 111.272 145.125 1.00 13.01  ? 1393 GLN A CB    1 
ATOM   10582 C  CG    . GLN A 1  1393 ? 139.840 110.406 145.963 1.00 20.16  ? 1393 GLN A CG    1 
ATOM   10583 C  CD    . GLN A 1  1393 ? 138.556 110.033 145.229 1.00 30.29  ? 1393 GLN A CD    1 
ATOM   10584 O  OE1   . GLN A 1  1393 ? 138.239 108.854 145.063 1.00 22.84  ? 1393 GLN A OE1   1 
ATOM   10585 N  NE2   . GLN A 1  1393 ? 137.815 111.041 144.783 1.00 28.99  ? 1393 GLN A NE2   1 
ATOM   10586 N  N     . VAL A 1  1394 ? 141.017 109.618 142.438 1.00 20.39  ? 1394 VAL A N     1 
ATOM   10587 C  CA    . VAL A 1  1394 ? 140.578 108.537 141.561 1.00 12.77  ? 1394 VAL A CA    1 
ATOM   10588 C  C     . VAL A 1  1394 ? 141.741 107.619 141.217 1.00 12.76  ? 1394 VAL A C     1 
ATOM   10589 O  O     . VAL A 1  1394 ? 141.592 106.395 141.182 1.00 20.80  ? 1394 VAL A O     1 
ATOM   10590 C  CB    . VAL A 1  1394 ? 139.915 109.109 140.295 1.00 10.16  ? 1394 VAL A CB    1 
ATOM   10591 C  CG1   . VAL A 1  1394 ? 139.636 108.015 139.304 1.00 12.32  ? 1394 VAL A CG1   1 
ATOM   10592 C  CG2   . VAL A 1  1394 ? 138.623 109.789 140.649 1.00 13.68  ? 1394 VAL A CG2   1 
ATOM   10593 N  N     . LEU A 1  1395 ? 142.910 108.196 140.947 1.00 16.29  ? 1395 LEU A N     1 
ATOM   10594 C  CA    . LEU A 1  1395 ? 144.086 107.404 140.612 1.00 11.90  ? 1395 LEU A CA    1 
ATOM   10595 C  C     . LEU A 1  1395 ? 144.541 106.543 141.782 1.00 15.44  ? 1395 LEU A C     1 
ATOM   10596 O  O     . LEU A 1  1395 ? 144.973 105.405 141.587 1.00 16.37  ? 1395 LEU A O     1 
ATOM   10597 C  CB    . LEU A 1  1395 ? 145.208 108.330 140.163 1.00 11.49  ? 1395 LEU A CB    1 
ATOM   10598 C  CG    . LEU A 1  1395 ? 146.535 107.702 139.769 1.00 21.76  ? 1395 LEU A CG    1 
ATOM   10599 C  CD1   . LEU A 1  1395 ? 146.385 106.872 138.516 1.00 19.97  ? 1395 LEU A CD1   1 
ATOM   10600 C  CD2   . LEU A 1  1395 ? 147.567 108.788 139.597 1.00 17.38  ? 1395 LEU A CD2   1 
ATOM   10601 N  N     . THR A 1  1396 ? 144.472 107.076 143.001 1.00 20.34  ? 1396 THR A N     1 
ATOM   10602 C  CA    . THR A 1  1396 ? 144.887 106.313 144.173 1.00 18.16  ? 1396 THR A CA    1 
ATOM   10603 C  C     . THR A 1  1396 ? 143.982 105.114 144.413 1.00 18.12  ? 1396 THR A C     1 
ATOM   10604 O  O     . THR A 1  1396 ? 144.457 104.033 144.772 1.00 21.73  ? 1396 THR A O     1 
ATOM   10605 C  CB    . THR A 1  1396 ? 144.908 107.213 145.399 1.00 21.06  ? 1396 THR A CB    1 
ATOM   10606 O  OG1   . THR A 1  1396 ? 145.616 108.415 145.090 1.00 26.74  ? 1396 THR A OG1   1 
ATOM   10607 C  CG2   . THR A 1  1396 ? 145.592 106.517 146.546 1.00 21.85  ? 1396 THR A CG2   1 
ATOM   10608 N  N     . ASP A 1  1397 ? 142.673 105.287 144.232 1.00 19.05  ? 1397 ASP A N     1 
ATOM   10609 C  CA    . ASP A 1  1397 ? 141.759 104.164 144.389 1.00 19.27  ? 1397 ASP A CA    1 
ATOM   10610 C  C     . ASP A 1  1397 ? 141.961 103.129 143.294 1.00 16.83  ? 1397 ASP A C     1 
ATOM   10611 O  O     . ASP A 1  1397 ? 141.844 101.930 143.541 1.00 22.29  ? 1397 ASP A O     1 
ATOM   10612 C  CB    . ASP A 1  1397 ? 140.318 104.654 144.400 1.00 22.54  ? 1397 ASP A CB    1 
ATOM   10613 C  CG    . ASP A 1  1397 ? 140.014 105.535 145.585 1.00 28.56  ? 1397 ASP A CG    1 
ATOM   10614 O  OD1   . ASP A 1  1397 ? 140.756 105.473 146.585 1.00 32.57  ? 1397 ASP A OD1   1 
ATOM   10615 O  OD2   . ASP A 1  1397 ? 139.021 106.285 145.523 1.00 29.85  ? 1397 ASP A OD2   1 
ATOM   10616 N  N     . ALA A 1  1398 ? 142.259 103.567 142.075 1.00 9.99   ? 1398 ALA A N     1 
ATOM   10617 C  CA    . ALA A 1  1398 ? 142.438 102.619 140.983 1.00 14.13  ? 1398 ALA A CA    1 
ATOM   10618 C  C     . ALA A 1  1398 ? 143.632 101.705 141.207 1.00 20.85  ? 1398 ALA A C     1 
ATOM   10619 O  O     . ALA A 1  1398 ? 143.555 100.509 140.916 1.00 21.12  ? 1398 ALA A O     1 
ATOM   10620 C  CB    . ALA A 1  1398 ? 142.595 103.364 139.662 1.00 14.45  ? 1398 ALA A CB    1 
ATOM   10621 N  N     . ALA A 1  1399 ? 144.743 102.250 141.701 1.00 22.86  ? 1399 ALA A N     1 
ATOM   10622 C  CA    . ALA A 1  1399 ? 145.953 101.457 141.884 1.00 15.58  ? 1399 ALA A CA    1 
ATOM   10623 C  C     . ALA A 1  1399 ? 145.775 100.400 142.966 1.00 17.42  ? 1399 ALA A C     1 
ATOM   10624 O  O     . ALA A 1  1399 ? 146.273 99.279  142.832 1.00 21.14  ? 1399 ALA A O     1 
ATOM   10625 C  CB    . ALA A 1  1399 ? 147.125 102.374 142.214 1.00 18.04  ? 1399 ALA A CB    1 
ATOM   10626 N  N     . VAL A 1  1400 ? 145.078 100.739 144.051 1.00 18.71  ? 1400 VAL A N     1 
ATOM   10627 C  CA    . VAL A 1  1400 ? 144.863 99.792  145.141 1.00 23.24  ? 1400 VAL A CA    1 
ATOM   10628 C  C     . VAL A 1  1400 ? 143.958 98.633  144.754 1.00 25.21  ? 1400 VAL A C     1 
ATOM   10629 O  O     . VAL A 1  1400 ? 144.253 97.485  145.107 1.00 26.41  ? 1400 VAL A O     1 
ATOM   10630 C  CB    . VAL A 1  1400 ? 144.308 100.541 146.366 1.00 20.33  ? 1400 VAL A CB    1 
ATOM   10631 C  CG1   . VAL A 1  1400 ? 143.782 99.578  147.376 1.00 23.01  ? 1400 VAL A CG1   1 
ATOM   10632 C  CG2   . VAL A 1  1400 ? 145.384 101.393 146.996 1.00 18.63  ? 1400 VAL A CG2   1 
ATOM   10633 N  N     . ASP A 1  1401 ? 142.873 98.892  144.030 1.00 24.00  ? 1401 ASP A N     1 
ATOM   10634 C  CA    . ASP A 1  1401 ? 141.972 97.855  143.544 1.00 21.80  ? 1401 ASP A CA    1 
ATOM   10635 C  C     . ASP A 1  1401 ? 142.450 97.161  142.278 1.00 25.89  ? 1401 ASP A C     1 
ATOM   10636 O  O     . ASP A 1  1401 ? 141.809 96.201  141.848 1.00 31.11  ? 1401 ASP A O     1 
ATOM   10637 C  CB    . ASP A 1  1401 ? 140.582 98.439  143.306 1.00 23.59  ? 1401 ASP A CB    1 
ATOM   10638 C  CG    . ASP A 1  1401 ? 140.103 99.291  144.456 1.00 33.25  ? 1401 ASP A CG    1 
ATOM   10639 O  OD1   . ASP A 1  1401 ? 138.937 99.132  144.860 1.00 37.52  ? 1401 ASP A OD1   1 
ATOM   10640 O  OD2   . ASP A 1  1401 ? 140.900 100.055 145.025 1.00 33.12  ? 1401 ASP A OD2   1 
ATOM   10641 N  N     . SER A 1  1402 ? 143.548 97.612  141.679 1.00 23.02  ? 1402 SER A N     1 
ATOM   10642 C  CA    . SER A 1  1402 ? 144.079 97.030  140.449 1.00 21.97  ? 1402 SER A CA    1 
ATOM   10643 C  C     . SER A 1  1402 ? 143.049 97.081  139.325 1.00 21.79  ? 1402 SER A C     1 
ATOM   10644 O  O     . SER A 1  1402 ? 142.747 96.080  138.675 1.00 25.48  ? 1402 SER A O     1 
ATOM   10645 C  CB    . SER A 1  1402 ? 144.561 95.601  140.683 1.00 22.14  ? 1402 SER A CB    1 
ATOM   10646 O  OG    . SER A 1  1402 ? 145.709 95.594  141.502 1.00 28.95  ? 1402 SER A OG    1 
ATOM   10647 N  N     . ALA A 1  1403 ? 142.519 98.274  139.088 1.00 15.33  ? 1403 ALA A N     1 
ATOM   10648 C  CA    . ALA A 1  1403 ? 141.435 98.444  138.133 1.00 15.92  ? 1403 ALA A CA    1 
ATOM   10649 C  C     . ALA A 1  1403 ? 141.903 98.174  136.707 1.00 16.52  ? 1403 ALA A C     1 
ATOM   10650 O  O     . ALA A 1  1403 ? 142.977 98.618  136.301 1.00 18.88  ? 1403 ALA A O     1 
ATOM   10651 C  CB    . ALA A 1  1403 ? 140.871 99.854  138.244 1.00 12.97  ? 1403 ALA A CB    1 
ATOM   10652 N  N     . VAL A 1  1404 ? 141.095 97.441  135.950 1.00 15.02  ? 1404 VAL A N     1 
ATOM   10653 C  CA    . VAL A 1  1404 ? 141.307 97.272  134.518 1.00 13.55  ? 1404 VAL A CA    1 
ATOM   10654 C  C     . VAL A 1  1404 ? 140.335 98.178  133.782 1.00 13.07  ? 1404 VAL A C     1 
ATOM   10655 O  O     . VAL A 1  1404 ? 139.117 98.049  133.932 1.00 19.41  ? 1404 VAL A O     1 
ATOM   10656 C  CB    . VAL A 1  1404 ? 141.113 95.810  134.093 1.00 10.62  ? 1404 VAL A CB    1 
ATOM   10657 C  CG1   . VAL A 1  1404 ? 141.320 95.683  132.610 1.00 9.25   ? 1404 VAL A CG1   1 
ATOM   10658 C  CG2   . VAL A 1  1404 ? 142.062 94.909  134.837 1.00 14.47  ? 1404 VAL A CG2   1 
ATOM   10659 N  N     . ASN A 1  1405 ? 140.868 99.084  132.975 1.00 10.62  ? 1405 ASN A N     1 
ATOM   10660 C  CA    . ASN A 1  1405 ? 140.075 100.122 132.324 1.00 2.34   ? 1405 ASN A CA    1 
ATOM   10661 C  C     . ASN A 1  1405 ? 140.046 99.874  130.826 1.00 8.88   ? 1405 ASN A C     1 
ATOM   10662 O  O     . ASN A 1  1405 ? 141.031 100.164 130.127 1.00 8.00   ? 1405 ASN A O     1 
ATOM   10663 C  CB    . ASN A 1  1405 ? 140.654 101.498 132.652 1.00 8.52   ? 1405 ASN A CB    1 
ATOM   10664 C  CG    . ASN A 1  1405 ? 139.878 102.635 132.038 1.00 2.56   ? 1405 ASN A CG    1 
ATOM   10665 O  OD1   . ASN A 1  1405 ? 138.824 102.448 131.453 1.00 12.44  ? 1405 ASN A OD1   1 
ATOM   10666 N  ND2   . ASN A 1  1405 ? 140.367 103.835 132.235 1.00 2.13   ? 1405 ASN A ND2   1 
ATOM   10667 N  N     . PRO A 1  1406 ? 138.959 99.323  130.288 1.00 11.73  ? 1406 PRO A N     1 
ATOM   10668 C  CA    . PRO A 1  1406 ? 138.846 99.193  128.835 1.00 5.29   ? 1406 PRO A CA    1 
ATOM   10669 C  C     . PRO A 1  1406 ? 138.702 100.555 128.180 1.00 1.25   ? 1406 PRO A C     1 
ATOM   10670 O  O     . PRO A 1  1406 ? 138.212 101.509 128.781 1.00 7.43   ? 1406 PRO A O     1 
ATOM   10671 C  CB    . PRO A 1  1406 ? 137.589 98.340  128.654 1.00 0.09   ? 1406 PRO A CB    1 
ATOM   10672 C  CG    . PRO A 1  1406 ? 136.816 98.564  129.875 1.00 4.64   ? 1406 PRO A CG    1 
ATOM   10673 C  CD    . PRO A 1  1406 ? 137.777 98.789  130.979 1.00 7.67   ? 1406 PRO A CD    1 
ATOM   10674 N  N     . ILE A 1  1407 ? 139.156 100.648 126.940 1.00 15.34  ? 1407 ILE A N     1 
ATOM   10675 C  CA    . ILE A 1  1407 ? 139.172 101.918 126.227 1.00 1.62   ? 1407 ILE A CA    1 
ATOM   10676 C  C     . ILE A 1  1407 ? 137.927 101.976 125.352 1.00 6.89   ? 1407 ILE A C     1 
ATOM   10677 O  O     . ILE A 1  1407 ? 137.774 101.197 124.411 1.00 11.31  ? 1407 ILE A O     1 
ATOM   10678 C  CB    . ILE A 1  1407 ? 140.459 102.089 125.411 1.00 11.74  ? 1407 ILE A CB    1 
ATOM   10679 C  CG1   . ILE A 1  1407 ? 141.685 101.952 126.316 1.00 2.48   ? 1407 ILE A CG1   1 
ATOM   10680 C  CG2   . ILE A 1  1407 ? 140.495 103.432 124.740 1.00 2.47   ? 1407 ILE A CG2   1 
ATOM   10681 C  CD1   . ILE A 1  1407 ? 141.752 102.953 127.418 1.00 1.28   ? 1407 ILE A CD1   1 
ATOM   10682 N  N     . TYR A 1  1408 ? 137.022 102.889 125.687 1.00 3.32   ? 1408 TYR A N     1 
ATOM   10683 C  CA    . TYR A 1  1408 ? 135.787 103.087 124.951 1.00 1.08   ? 1408 TYR A CA    1 
ATOM   10684 C  C     . TYR A 1  1408 ? 135.325 104.512 125.199 1.00 0.70   ? 1408 TYR A C     1 
ATOM   10685 O  O     . TYR A 1  1408 ? 135.800 105.187 126.112 1.00 1.66   ? 1408 TYR A O     1 
ATOM   10686 C  CB    . TYR A 1  1408 ? 134.715 102.065 125.350 1.00 4.77   ? 1408 TYR A CB    1 
ATOM   10687 C  CG    . TYR A 1  1408 ? 134.187 102.221 126.753 1.00 7.24   ? 1408 TYR A CG    1 
ATOM   10688 C  CD1   . TYR A 1  1408 ? 134.755 101.533 127.807 1.00 3.28   ? 1408 TYR A CD1   1 
ATOM   10689 C  CD2   . TYR A 1  1408 ? 133.131 103.072 127.030 1.00 1.47   ? 1408 TYR A CD2   1 
ATOM   10690 C  CE1   . TYR A 1  1408 ? 134.285 101.686 129.080 1.00 4.14   ? 1408 TYR A CE1   1 
ATOM   10691 C  CE2   . TYR A 1  1408 ? 132.665 103.230 128.296 1.00 13.86  ? 1408 TYR A CE2   1 
ATOM   10692 C  CZ    . TYR A 1  1408 ? 133.237 102.538 129.316 1.00 3.59   ? 1408 TYR A CZ    1 
ATOM   10693 O  OH    . TYR A 1  1408 ? 132.750 102.696 130.588 1.00 7.73   ? 1408 TYR A OH    1 
ATOM   10694 N  N     . GLY A 1  1409 ? 134.397 104.969 124.367 1.00 1.40   ? 1409 GLY A N     1 
ATOM   10695 C  CA    . GLY A 1  1409 ? 133.814 106.278 124.554 1.00 5.31   ? 1409 GLY A CA    1 
ATOM   10696 C  C     . GLY A 1  1409 ? 134.677 107.397 124.025 1.00 0.72   ? 1409 GLY A C     1 
ATOM   10697 O  O     . GLY A 1  1409 ? 135.283 107.263 122.965 1.00 8.73   ? 1409 GLY A O     1 
ATOM   10698 N  N     . ILE A 1  1410 ? 134.744 108.504 124.752 1.00 1.18   ? 1410 ILE A N     1 
ATOM   10699 C  CA    . ILE A 1  1410 ? 135.420 109.709 124.298 1.00 1.57   ? 1410 ILE A CA    1 
ATOM   10700 C  C     . ILE A 1  1410 ? 136.687 109.974 125.104 1.00 1.60   ? 1410 ILE A C     1 
ATOM   10701 O  O     . ILE A 1  1410 ? 137.774 110.080 124.543 1.00 5.65   ? 1410 ILE A O     1 
ATOM   10702 C  CB    . ILE A 1  1410 ? 134.471 110.931 124.348 1.00 2.90   ? 1410 ILE A CB    1 
ATOM   10703 C  CG1   . ILE A 1  1410 ? 133.140 110.667 123.646 1.00 10.59  ? 1410 ILE A CG1   1 
ATOM   10704 C  CG2   . ILE A 1  1410 ? 135.107 112.108 123.677 1.00 0.29   ? 1410 ILE A CG2   1 
ATOM   10705 C  CD1   . ILE A 1  1410 ? 133.252 110.338 122.247 1.00 8.68   ? 1410 ILE A CD1   1 
ATOM   10706 N  N     . ALA A 1  1411 ? 136.563 110.078 126.429 1.00 10.15  ? 1411 ALA A N     1 
ATOM   10707 C  CA    . ALA A 1  1411 ? 137.645 110.603 127.258 1.00 3.34   ? 1411 ALA A CA    1 
ATOM   10708 C  C     . ALA A 1  1411 ? 138.770 109.594 127.458 1.00 4.23   ? 1411 ALA A C     1 
ATOM   10709 O  O     . ALA A 1  1411 ? 139.940 109.976 127.518 1.00 9.59   ? 1411 ALA A O     1 
ATOM   10710 C  CB    . ALA A 1  1411 ? 137.098 111.055 128.609 1.00 12.17  ? 1411 ALA A CB    1 
ATOM   10711 N  N     . ALA A 1  1412 ? 138.448 108.315 127.608 1.00 2.74   ? 1412 ALA A N     1 
ATOM   10712 C  CA    . ALA A 1  1412 ? 139.504 107.321 127.789 1.00 2.10   ? 1412 ALA A CA    1 
ATOM   10713 C  C     . ALA A 1  1412 ? 140.434 107.209 126.585 1.00 7.08   ? 1412 ALA A C     1 
ATOM   10714 O  O     . ALA A 1  1412 ? 141.657 107.158 126.789 1.00 5.79   ? 1412 ALA A O     1 
ATOM   10715 C  CB    . ALA A 1  1412 ? 138.893 105.969 128.161 1.00 1.61   ? 1412 ALA A CB    1 
ATOM   10716 N  N     . PRO A 1  1413 ? 139.956 107.142 125.336 1.00 5.16   ? 1413 PRO A N     1 
ATOM   10717 C  CA    . PRO A 1  1413 ? 140.897 107.174 124.206 1.00 15.45  ? 1413 PRO A CA    1 
ATOM   10718 C  C     . PRO A 1  1413 ? 141.696 108.452 124.111 1.00 5.33   ? 1413 PRO A C     1 
ATOM   10719 O  O     . PRO A 1  1413 ? 142.841 108.413 123.665 1.00 1.59   ? 1413 PRO A O     1 
ATOM   10720 C  CB    . PRO A 1  1413 ? 139.982 107.001 122.989 1.00 3.87   ? 1413 PRO A CB    1 
ATOM   10721 C  CG    . PRO A 1  1413 ? 138.774 106.412 123.518 1.00 4.59   ? 1413 PRO A CG    1 
ATOM   10722 C  CD    . PRO A 1  1413 ? 138.581 106.963 124.857 1.00 6.28   ? 1413 PRO A CD    1 
ATOM   10723 N  N     . THR A 1  1414 ? 141.122 109.583 124.502 1.00 0.96   ? 1414 THR A N     1 
ATOM   10724 C  CA    . THR A 1  1414 ? 141.800 110.865 124.374 1.00 6.19   ? 1414 THR A CA    1 
ATOM   10725 C  C     . THR A 1  1414 ? 142.941 110.998 125.373 1.00 3.16   ? 1414 THR A C     1 
ATOM   10726 O  O     . THR A 1  1414 ? 144.005 111.524 125.041 1.00 9.94   ? 1414 THR A O     1 
ATOM   10727 C  CB    . THR A 1  1414 ? 140.788 111.992 124.551 1.00 0.36   ? 1414 THR A CB    1 
ATOM   10728 O  OG1   . THR A 1  1414 ? 139.787 111.885 123.537 1.00 3.06   ? 1414 THR A OG1   1 
ATOM   10729 C  CG2   . THR A 1  1414 ? 141.453 113.336 124.453 1.00 2.86   ? 1414 THR A CG2   1 
ATOM   10730 N  N     . LEU A 1  1415 ? 142.740 110.526 126.602 1.00 6.90   ? 1415 LEU A N     1 
ATOM   10731 C  CA    . LEU A 1  1415 ? 143.789 110.595 127.610 1.00 0.76   ? 1415 LEU A CA    1 
ATOM   10732 C  C     . LEU A 1  1415 ? 144.913 109.614 127.321 1.00 3.90   ? 1415 LEU A C     1 
ATOM   10733 O  O     . LEU A 1  1415 ? 146.022 109.780 127.832 1.00 11.50  ? 1415 LEU A O     1 
ATOM   10734 C  CB    . LEU A 1  1415 ? 143.194 110.346 128.991 1.00 2.29   ? 1415 LEU A CB    1 
ATOM   10735 C  CG    . LEU A 1  1415 ? 142.849 111.581 129.823 1.00 2.39   ? 1415 LEU A CG    1 
ATOM   10736 C  CD1   . LEU A 1  1415 ? 141.840 112.430 129.124 1.00 3.68   ? 1415 LEU A CD1   1 
ATOM   10737 C  CD2   . LEU A 1  1415 ? 142.331 111.191 131.171 1.00 1.72   ? 1415 LEU A CD2   1 
ATOM   10738 N  N     . MET A 1  1416 ? 144.659 108.609 126.496 1.00 2.06   ? 1416 MET A N     1 
ATOM   10739 C  CA    . MET A 1  1416 ? 145.670 107.667 126.045 1.00 5.04   ? 1416 MET A CA    1 
ATOM   10740 C  C     . MET A 1  1416 ? 146.332 108.088 124.744 1.00 4.39   ? 1416 MET A C     1 
ATOM   10741 O  O     . MET A 1  1416 ? 147.095 107.308 124.172 1.00 15.57  ? 1416 MET A O     1 
ATOM   10742 C  CB    . MET A 1  1416 ? 145.059 106.277 125.899 1.00 1.64   ? 1416 MET A CB    1 
ATOM   10743 C  CG    . MET A 1  1416 ? 144.980 105.522 127.198 1.00 2.26   ? 1416 MET A CG    1 
ATOM   10744 S  SD    . MET A 1  1416 ? 146.572 105.435 128.035 1.00 19.96  ? 1416 MET A SD    1 
ATOM   10745 C  CE    . MET A 1  1416 ? 146.201 106.287 129.544 1.00 4.91   ? 1416 MET A CE    1 
ATOM   10746 N  N     . GLY A 1  1417 ? 146.053 109.293 124.260 1.00 1.54   ? 1417 GLY A N     1 
ATOM   10747 C  CA    . GLY A 1  1417 ? 146.679 109.819 123.073 1.00 15.91  ? 1417 GLY A CA    1 
ATOM   10748 C  C     . GLY A 1  1417 ? 146.071 109.381 121.766 1.00 2.54   ? 1417 GLY A C     1 
ATOM   10749 O  O     . GLY A 1  1417 ? 146.634 109.688 120.714 1.00 5.62   ? 1417 GLY A O     1 
ATOM   10750 N  N     . SER A 1  1418 ? 144.949 108.680 121.792 1.00 6.79   ? 1418 SER A N     1 
ATOM   10751 C  CA    . SER A 1  1418 ? 144.341 108.117 120.602 1.00 3.90   ? 1418 SER A CA    1 
ATOM   10752 C  C     . SER A 1  1418 ? 143.089 108.900 120.217 1.00 2.34   ? 1418 SER A C     1 
ATOM   10753 O  O     . SER A 1  1418 ? 142.824 109.988 120.728 1.00 3.53   ? 1418 SER A O     1 
ATOM   10754 C  CB    . SER A 1  1418 ? 144.039 106.645 120.836 1.00 8.46   ? 1418 SER A CB    1 
ATOM   10755 O  OG    . SER A 1  1418 ? 143.491 106.061 119.679 1.00 14.91  ? 1418 SER A OG    1 
ATOM   10756 N  N     . VAL A 1  1419 ? 142.317 108.348 119.287 1.00 6.05   ? 1419 VAL A N     1 
ATOM   10757 C  CA    . VAL A 1  1419 ? 141.067 108.941 118.819 1.00 3.77   ? 1419 VAL A CA    1 
ATOM   10758 C  C     . VAL A 1  1419 ? 139.896 108.038 119.173 1.00 2.40   ? 1419 VAL A C     1 
ATOM   10759 O  O     . VAL A 1  1419 ? 140.030 106.811 119.137 1.00 8.04   ? 1419 VAL A O     1 
ATOM   10760 C  CB    . VAL A 1  1419 ? 141.106 109.212 117.306 1.00 3.22   ? 1419 VAL A CB    1 
ATOM   10761 C  CG1   . VAL A 1  1419 ? 141.876 110.478 117.021 1.00 4.44   ? 1419 VAL A CG1   1 
ATOM   10762 C  CG2   . VAL A 1  1419 ? 141.748 108.052 116.586 1.00 12.85  ? 1419 VAL A CG2   1 
ATOM   10763 N  N     . PRO A 1  1420 ? 138.746 108.599 119.530 1.00 0.99   ? 1420 PRO A N     1 
ATOM   10764 C  CA    . PRO A 1  1420 ? 137.566 107.773 119.786 1.00 5.57   ? 1420 PRO A CA    1 
ATOM   10765 C  C     . PRO A 1  1420 ? 137.111 107.018 118.547 1.00 11.78  ? 1420 PRO A C     1 
ATOM   10766 O  O     . PRO A 1  1420 ? 137.186 107.518 117.429 1.00 7.01   ? 1420 PRO A O     1 
ATOM   10767 C  CB    . PRO A 1  1420 ? 136.523 108.795 120.238 1.00 2.11   ? 1420 PRO A CB    1 
ATOM   10768 C  CG    . PRO A 1  1420 ? 137.300 109.916 120.751 1.00 0.21   ? 1420 PRO A CG    1 
ATOM   10769 C  CD    . PRO A 1  1420 ? 138.528 109.996 119.927 1.00 3.40   ? 1420 PRO A CD    1 
ATOM   10770 N  N     . ARG A 1  1421 ? 136.628 105.800 118.764 1.00 6.98   ? 1421 ARG A N     1 
ATOM   10771 C  CA    . ARG A 1  1421 ? 136.102 104.936 117.709 1.00 15.66  ? 1421 ARG A CA    1 
ATOM   10772 C  C     . ARG A 1  1421 ? 134.640 105.272 117.487 1.00 4.69   ? 1421 ARG A C     1 
ATOM   10773 O  O     . ARG A 1  1421 ? 133.744 104.581 117.955 1.00 10.55  ? 1421 ARG A O     1 
ATOM   10774 C  CB    . ARG A 1  1421 ? 136.270 103.475 118.080 1.00 15.43  ? 1421 ARG A CB    1 
ATOM   10775 C  CG    . ARG A 1  1421 ? 136.043 102.535 116.939 1.00 5.74   ? 1421 ARG A CG    1 
ATOM   10776 C  CD    . ARG A 1  1421 ? 136.043 101.105 117.410 1.00 8.82   ? 1421 ARG A CD    1 
ATOM   10777 N  NE    . ARG A 1  1421 ? 137.366 100.695 117.863 1.00 13.59  ? 1421 ARG A NE    1 
ATOM   10778 C  CZ    . ARG A 1  1421 ? 138.354 100.329 117.061 1.00 11.59  ? 1421 ARG A CZ    1 
ATOM   10779 N  NH1   . ARG A 1  1421 ? 138.206 100.310 115.749 1.00 10.16  ? 1421 ARG A NH1   1 
ATOM   10780 N  NH2   . ARG A 1  1421 ? 139.519 99.973  117.590 1.00 12.43  ? 1421 ARG A NH2   1 
ATOM   10781 N  N     . ILE A 1  1422 ? 134.403 106.333 116.723 1.00 2.84   ? 1422 ILE A N     1 
ATOM   10782 C  CA    . ILE A 1  1422 ? 133.138 107.047 116.729 1.00 4.21   ? 1422 ILE A CA    1 
ATOM   10783 C  C     . ILE A 1  1422 ? 133.061 107.833 115.440 1.00 9.71   ? 1422 ILE A C     1 
ATOM   10784 O  O     . ILE A 1  1422 ? 134.076 108.284 114.922 1.00 12.34  ? 1422 ILE A O     1 
ATOM   10785 C  CB    . ILE A 1  1422 ? 133.056 107.945 117.991 1.00 12.28  ? 1422 ILE A CB    1 
ATOM   10786 C  CG1   . ILE A 1  1422 ? 132.522 107.140 119.162 1.00 1.14   ? 1422 ILE A CG1   1 
ATOM   10787 C  CG2   . ILE A 1  1422 ? 132.301 109.229 117.768 1.00 13.49  ? 1422 ILE A CG2   1 
ATOM   10788 C  CD1   . ILE A 1  1422 ? 133.144 107.513 120.421 1.00 4.42   ? 1422 ILE A CD1   1 
ATOM   10789 N  N     . GLY A 1  1423 ? 131.858 107.976 114.904 1.00 0.91   ? 1423 GLY A N     1 
ATOM   10790 C  CA    . GLY A 1  1423 ? 131.689 108.773 113.713 1.00 2.10   ? 1423 GLY A CA    1 
ATOM   10791 C  C     . GLY A 1  1423 ? 132.220 108.110 112.468 1.00 3.99   ? 1423 GLY A C     1 
ATOM   10792 O  O     . GLY A 1  1423 ? 131.819 106.994 112.144 1.00 10.26  ? 1423 GLY A O     1 
ATOM   10793 N  N     . THR A 1  1424 ? 133.113 108.790 111.750 1.00 2.34   ? 1424 THR A N     1 
ATOM   10794 C  CA    . THR A 1  1424 ? 133.708 108.195 110.561 1.00 3.58   ? 1424 THR A CA    1 
ATOM   10795 C  C     . THR A 1  1424 ? 134.627 107.041 110.913 1.00 13.05  ? 1424 THR A C     1 
ATOM   10796 O  O     . THR A 1  1424 ? 134.970 106.248 110.039 1.00 4.39   ? 1424 THR A O     1 
ATOM   10797 C  CB    . THR A 1  1424 ? 134.469 109.244 109.743 1.00 2.80   ? 1424 THR A CB    1 
ATOM   10798 O  OG1   . THR A 1  1424 ? 135.263 110.060 110.604 1.00 13.15  ? 1424 THR A OG1   1 
ATOM   10799 C  CG2   . THR A 1  1424 ? 133.512 110.126 108.976 1.00 12.11  ? 1424 THR A CG2   1 
ATOM   10800 N  N     . MET A 1  1425 ? 134.992 106.907 112.181 1.00 9.06   ? 1425 MET A N     1 
ATOM   10801 C  CA    . MET A 1  1425 ? 135.896 105.868 112.637 1.00 6.14   ? 1425 MET A CA    1 
ATOM   10802 C  C     . MET A 1  1425 ? 135.183 104.714 113.316 1.00 14.79  ? 1425 MET A C     1 
ATOM   10803 O  O     . MET A 1  1425 ? 135.830 103.910 113.981 1.00 15.82  ? 1425 MET A O     1 
ATOM   10804 C  CB    . MET A 1  1425 ? 136.940 106.468 113.568 1.00 7.44   ? 1425 MET A CB    1 
ATOM   10805 C  CG    . MET A 1  1425 ? 138.323 106.118 113.124 1.00 3.88   ? 1425 MET A CG    1 
ATOM   10806 S  SD    . MET A 1  1425 ? 139.057 107.214 111.928 1.00 12.44  ? 1425 MET A SD    1 
ATOM   10807 C  CE    . MET A 1  1425 ? 139.627 108.487 113.014 1.00 12.97  ? 1425 MET A CE    1 
ATOM   10808 N  N     . TYR A 1  1426 ? 133.871 104.604 113.150 1.00 7.44   ? 1426 TYR A N     1 
ATOM   10809 C  CA    . TYR A 1  1426 ? 133.128 103.565 113.841 1.00 2.38   ? 1426 TYR A CA    1 
ATOM   10810 C  C     . TYR A 1  1426 ? 133.262 102.217 113.150 1.00 10.00  ? 1426 TYR A C     1 
ATOM   10811 O  O     . TYR A 1  1426 ? 133.334 101.182 113.815 1.00 10.61  ? 1426 TYR A O     1 
ATOM   10812 C  CB    . TYR A 1  1426 ? 131.664 103.968 113.957 1.00 8.62   ? 1426 TYR A CB    1 
ATOM   10813 C  CG    . TYR A 1  1426 ? 130.871 103.082 114.865 1.00 5.08   ? 1426 TYR A CG    1 
ATOM   10814 C  CD1   . TYR A 1  1426 ? 131.102 103.069 116.222 1.00 6.44   ? 1426 TYR A CD1   1 
ATOM   10815 C  CD2   . TYR A 1  1426 ? 129.899 102.247 114.363 1.00 14.34  ? 1426 TYR A CD2   1 
ATOM   10816 C  CE1   . TYR A 1  1426 ? 130.390 102.255 117.041 1.00 14.53  ? 1426 TYR A CE1   1 
ATOM   10817 C  CE2   . TYR A 1  1426 ? 129.181 101.432 115.182 1.00 9.04   ? 1426 TYR A CE2   1 
ATOM   10818 C  CZ    . TYR A 1  1426 ? 129.432 101.437 116.519 1.00 2.50   ? 1426 TYR A CZ    1 
ATOM   10819 O  OH    . TYR A 1  1426 ? 128.725 100.625 117.352 1.00 7.84   ? 1426 TYR A OH    1 
ATOM   10820 N  N     . SER A 1  1427 ? 133.279 102.201 111.828 1.00 4.27   ? 1427 SER A N     1 
ATOM   10821 C  CA    . SER A 1  1427 ? 133.331 100.967 111.063 1.00 8.91   ? 1427 SER A CA    1 
ATOM   10822 C  C     . SER A 1  1427 ? 134.702 100.797 110.430 1.00 4.68   ? 1427 SER A C     1 
ATOM   10823 O  O     . SER A 1  1427 ? 135.304 101.766 109.965 1.00 11.72  ? 1427 SER A O     1 
ATOM   10824 C  CB    . SER A 1  1427 ? 132.259 100.947 109.976 1.00 10.20  ? 1427 SER A CB    1 
ATOM   10825 O  OG    . SER A 1  1427 ? 130.971 100.786 110.528 1.00 4.43   ? 1427 SER A OG    1 
ATOM   10826 N  N     . ASP A 1  1428 ? 135.187 99.562  110.419 1.00 4.19   ? 1428 ASP A N     1 
ATOM   10827 C  CA    . ASP A 1  1428 ? 136.460 99.224  109.806 1.00 1.36   ? 1428 ASP A CA    1 
ATOM   10828 C  C     . ASP A 1  1428 ? 136.339 99.209  108.291 1.00 5.00   ? 1428 ASP A C     1 
ATOM   10829 O  O     . ASP A 1  1428 ? 135.280 98.900  107.743 1.00 8.54   ? 1428 ASP A O     1 
ATOM   10830 C  CB    . ASP A 1  1428 ? 136.938 97.859  110.288 1.00 2.00   ? 1428 ASP A CB    1 
ATOM   10831 C  CG    . ASP A 1  1428 ? 138.046 97.955  111.304 1.00 19.45  ? 1428 ASP A CG    1 
ATOM   10832 O  OD1   . ASP A 1  1428 ? 138.896 98.857  111.184 1.00 23.61  ? 1428 ASP A OD1   1 
ATOM   10833 O  OD2   . ASP A 1  1428 ? 138.074 97.122  112.230 1.00 26.23  ? 1428 ASP A OD2   1 
ATOM   10834 N  N     . ILE A 1  1429 ? 137.431 99.549  107.618 1.00 8.32   ? 1429 ILE A N     1 
ATOM   10835 C  CA    . ILE A 1  1429 ? 137.546 99.420  106.171 1.00 6.59   ? 1429 ILE A CA    1 
ATOM   10836 C  C     . ILE A 1  1429 ? 138.628 98.390  105.883 1.00 7.17   ? 1429 ILE A C     1 
ATOM   10837 O  O     . ILE A 1  1429 ? 139.684 98.399  106.520 1.00 7.79   ? 1429 ILE A O     1 
ATOM   10838 C  CB    . ILE A 1  1429 ? 137.873 100.770 105.509 1.00 5.12   ? 1429 ILE A CB    1 
ATOM   10839 C  CG1   . ILE A 1  1429 ? 136.868 101.852 105.916 1.00 6.01   ? 1429 ILE A CG1   1 
ATOM   10840 C  CG2   . ILE A 1  1429 ? 137.919 100.634 104.012 1.00 3.96   ? 1429 ILE A CG2   1 
ATOM   10841 C  CD1   . ILE A 1  1429 ? 135.440 101.586 105.523 1.00 0.80   ? 1429 ILE A CD1   1 
ATOM   10842 N  N     . ILE A 1  1430 ? 138.355 97.477  104.958 1.00 6.17   ? 1430 ILE A N     1 
ATOM   10843 C  CA    . ILE A 1  1430 ? 139.342 96.511  104.500 1.00 7.88   ? 1430 ILE A CA    1 
ATOM   10844 C  C     . ILE A 1  1430 ? 139.392 96.557  102.981 1.00 8.94   ? 1430 ILE A C     1 
ATOM   10845 O  O     . ILE A 1  1430 ? 138.456 96.999  102.318 1.00 14.46  ? 1430 ILE A O     1 
ATOM   10846 C  CB    . ILE A 1  1430 ? 139.051 95.080  104.994 1.00 9.19   ? 1430 ILE A CB    1 
ATOM   10847 C  CG1   . ILE A 1  1430 ? 137.745 94.565  104.409 1.00 10.94  ? 1430 ILE A CG1   1 
ATOM   10848 C  CG2   . ILE A 1  1430 ? 139.014 95.028  106.496 1.00 5.34   ? 1430 ILE A CG2   1 
ATOM   10849 C  CD1   . ILE A 1  1430 ? 137.447 93.157  104.773 1.00 10.89  ? 1430 ILE A CD1   1 
ATOM   10850 N  N     . MET A 1  1431 ? 140.508 96.103  102.429 1.00 8.12   ? 1431 MET A N     1 
ATOM   10851 C  CA    . MET A 1  1431 ? 140.722 96.179  100.993 1.00 13.28  ? 1431 MET A CA    1 
ATOM   10852 C  C     . MET A 1  1431 ? 140.041 94.999  100.317 1.00 18.29  ? 1431 MET A C     1 
ATOM   10853 O  O     . MET A 1  1431 ? 140.072 93.879  100.832 1.00 19.45  ? 1431 MET A O     1 
ATOM   10854 C  CB    . MET A 1  1431 ? 142.212 96.205  100.662 1.00 10.34  ? 1431 MET A CB    1 
ATOM   10855 C  CG    . MET A 1  1431 ? 142.962 97.300  101.384 1.00 9.68   ? 1431 MET A CG    1 
ATOM   10856 S  SD    . MET A 1  1431 ? 143.041 98.881  100.538 1.00 25.24  ? 1431 MET A SD    1 
ATOM   10857 C  CE    . MET A 1  1431 ? 143.097 98.388  98.838  1.00 15.24  ? 1431 MET A CE    1 
ATOM   10858 N  N     . ASP A 1  1432 ? 139.411 95.260  99.179  1.00 17.66  ? 1432 ASP A N     1 
ATOM   10859 C  CA    . ASP A 1  1432 ? 138.668 94.252  98.426  1.00 13.43  ? 1432 ASP A CA    1 
ATOM   10860 C  C     . ASP A 1  1432 ? 139.636 93.492  97.527  1.00 24.49  ? 1432 ASP A C     1 
ATOM   10861 O  O     . ASP A 1  1432 ? 139.871 93.857  96.377  1.00 29.37  ? 1432 ASP A O     1 
ATOM   10862 C  CB    . ASP A 1  1432 ? 137.562 94.918  97.627  1.00 12.90  ? 1432 ASP A CB    1 
ATOM   10863 C  CG    . ASP A 1  1432 ? 136.508 93.954  97.173  1.00 22.19  ? 1432 ASP A CG    1 
ATOM   10864 O  OD1   . ASP A 1  1432 ? 136.690 92.732  97.343  1.00 23.67  ? 1432 ASP A OD1   1 
ATOM   10865 O  OD2   . ASP A 1  1432 ? 135.488 94.420  96.635  1.00 20.43  ? 1432 ASP A OD2   1 
ATOM   10866 N  N     . GLU A 1  1433 ? 140.200 92.408  98.064  1.00 27.41  ? 1433 GLU A N     1 
ATOM   10867 C  CA    . GLU A 1  1433 ? 141.230 91.655  97.356  1.00 23.25  ? 1433 GLU A CA    1 
ATOM   10868 C  C     . GLU A 1  1433 ? 140.687 90.991  96.100  1.00 27.19  ? 1433 GLU A C     1 
ATOM   10869 O  O     . GLU A 1  1433 ? 141.343 90.999  95.055  1.00 31.39  ? 1433 GLU A O     1 
ATOM   10870 C  CB    . GLU A 1  1433 ? 141.823 90.605  98.285  1.00 23.15  ? 1433 GLU A CB    1 
ATOM   10871 C  CG    . GLU A 1  1433 ? 142.979 91.093  99.101  1.00 26.57  ? 1433 GLU A CG    1 
ATOM   10872 C  CD    . GLU A 1  1433 ? 142.997 90.495  100.488 1.00 33.15  ? 1433 GLU A CD    1 
ATOM   10873 O  OE1   . GLU A 1  1433 ? 143.071 89.256  100.602 1.00 32.42  ? 1433 GLU A OE1   1 
ATOM   10874 O  OE2   . GLU A 1  1433 ? 142.937 91.262  101.469 1.00 34.04  ? 1433 GLU A OE2   1 
ATOM   10875 N  N     . LYS A 1  1434 ? 139.501 90.397  96.183  1.00 28.31  ? 1434 LYS A N     1 
ATOM   10876 C  CA    . LYS A 1  1434 ? 138.933 89.684  95.048  1.00 26.65  ? 1434 LYS A CA    1 
ATOM   10877 C  C     . LYS A 1  1434 ? 138.565 90.613  93.900  1.00 25.04  ? 1434 LYS A C     1 
ATOM   10878 O  O     . LYS A 1  1434 ? 138.367 90.145  92.778  1.00 31.04  ? 1434 LYS A O     1 
ATOM   10879 C  CB    . LYS A 1  1434 ? 137.709 88.901  95.515  1.00 29.11  ? 1434 LYS A CB    1 
ATOM   10880 C  CG    . LYS A 1  1434 ? 137.266 87.774  94.612  1.00 29.46  ? 1434 LYS A CG    1 
ATOM   10881 C  CD    . LYS A 1  1434 ? 135.836 87.380  94.941  1.00 30.11  ? 1434 LYS A CD    1 
ATOM   10882 C  CE    . LYS A 1  1434 ? 135.149 86.701  93.770  1.00 31.66  ? 1434 LYS A CE    1 
ATOM   10883 N  NZ    . LYS A 1  1434 ? 135.064 85.223  93.966  1.00 30.29  ? 1434 LYS A NZ    1 
ATOM   10884 N  N     . TYR A 1  1435 ? 138.446 91.909  94.159  1.00 23.23  ? 1435 TYR A N     1 
ATOM   10885 C  CA    . TYR A 1  1435 ? 138.121 92.893  93.136  1.00 24.50  ? 1435 TYR A CA    1 
ATOM   10886 C  C     . TYR A 1  1435 ? 139.358 93.569  92.572  1.00 28.82  ? 1435 TYR A C     1 
ATOM   10887 O  O     . TYR A 1  1435 ? 139.381 93.916  91.389  1.00 26.78  ? 1435 TYR A O     1 
ATOM   10888 C  CB    . TYR A 1  1435 ? 137.179 93.948  93.720  1.00 19.98  ? 1435 TYR A CB    1 
ATOM   10889 C  CG    . TYR A 1  1435 ? 136.732 95.024  92.762  1.00 22.28  ? 1435 TYR A CG    1 
ATOM   10890 C  CD1   . TYR A 1  1435 ? 135.723 94.791  91.851  1.00 23.37  ? 1435 TYR A CD1   1 
ATOM   10891 C  CD2   . TYR A 1  1435 ? 137.306 96.280  92.787  1.00 23.40  ? 1435 TYR A CD2   1 
ATOM   10892 C  CE1   . TYR A 1  1435 ? 135.306 95.771  90.991  1.00 18.93  ? 1435 TYR A CE1   1 
ATOM   10893 C  CE2   . TYR A 1  1435 ? 136.896 97.263  91.925  1.00 21.34  ? 1435 TYR A CE2   1 
ATOM   10894 C  CZ    . TYR A 1  1435 ? 135.897 97.002  91.032  1.00 19.66  ? 1435 TYR A CZ    1 
ATOM   10895 O  OH    . TYR A 1  1435 ? 135.490 97.986  90.171  1.00 25.13  ? 1435 TYR A OH    1 
ATOM   10896 N  N     . ILE A 1  1436 ? 140.372 93.789  93.403  1.00 27.06  ? 1436 ILE A N     1 
ATOM   10897 C  CA    . ILE A 1  1436 ? 141.617 94.386  92.941  1.00 23.57  ? 1436 ILE A CA    1 
ATOM   10898 C  C     . ILE A 1  1436 ? 142.416 93.392  92.117  1.00 28.84  ? 1436 ILE A C     1 
ATOM   10899 O  O     . ILE A 1  1436 ? 143.000 93.749  91.091  1.00 31.64  ? 1436 ILE A O     1 
ATOM   10900 C  CB    . ILE A 1  1436 ? 142.425 94.901  94.139  1.00 26.69  ? 1436 ILE A CB    1 
ATOM   10901 C  CG1   . ILE A 1  1436 ? 141.719 96.081  94.790  1.00 23.89  ? 1436 ILE A CG1   1 
ATOM   10902 C  CG2   . ILE A 1  1436 ? 143.811 95.313  93.709  1.00 28.31  ? 1436 ILE A CG2   1 
ATOM   10903 C  CD1   . ILE A 1  1436 ? 142.294 96.438  96.125  1.00 20.87  ? 1436 ILE A CD1   1 
ATOM   10904 N  N     . THR A 1  1437 ? 142.466 92.134  92.555  1.00 30.18  ? 1437 THR A N     1 
ATOM   10905 C  CA    . THR A 1  1437 ? 143.252 91.131  91.851  1.00 29.84  ? 1437 THR A CA    1 
ATOM   10906 C  C     . THR A 1  1437 ? 142.678 90.814  90.480  1.00 29.90  ? 1437 THR A C     1 
ATOM   10907 O  O     . THR A 1  1437 ? 143.397 90.285  89.628  1.00 33.94  ? 1437 THR A O     1 
ATOM   10908 C  CB    . THR A 1  1437 ? 143.347 89.852  92.685  1.00 27.98  ? 1437 THR A CB    1 
ATOM   10909 O  OG1   . THR A 1  1437 ? 144.595 89.208  92.429  1.00 28.35  ? 1437 THR A OG1   1 
ATOM   10910 C  CG2   . THR A 1  1437 ? 142.232 88.892  92.332  1.00 27.76  ? 1437 THR A CG2   1 
ATOM   10911 N  N     . GLU A 1  1438 ? 141.413 91.137  90.245  1.00 28.86  ? 1438 GLU A N     1 
ATOM   10912 C  CA    . GLU A 1  1438 ? 140.755 90.857  88.984  1.00 29.45  ? 1438 GLU A CA    1 
ATOM   10913 C  C     . GLU A 1  1438 ? 140.703 92.072  88.070  1.00 32.16  ? 1438 GLU A C     1 
ATOM   10914 O  O     . GLU A 1  1438 ? 140.565 91.915  86.854  1.00 35.33  ? 1438 GLU A O     1 
ATOM   10915 C  CB    . GLU A 1  1438 ? 139.352 90.309  89.259  1.00 28.67  ? 1438 GLU A CB    1 
ATOM   10916 C  CG    . GLU A 1  1438 ? 138.279 90.718  88.289  1.00 30.10  ? 1438 GLU A CG    1 
ATOM   10917 C  CD    . GLU A 1  1438 ? 136.984 89.984  88.533  1.00 36.75  ? 1438 GLU A CD    1 
ATOM   10918 O  OE1   . GLU A 1  1438 ? 136.756 89.547  89.680  1.00 38.34  ? 1438 GLU A OE1   1 
ATOM   10919 O  OE2   . GLU A 1  1438 ? 136.196 89.835  87.577  1.00 38.18  ? 1438 GLU A OE2   1 
ATOM   10920 N  N     . ASN A 1  1439 ? 140.866 93.273  88.614  1.00 32.64  ? 1439 ASN A N     1 
ATOM   10921 C  CA    . ASN A 1  1439 ? 140.730 94.507  87.855  1.00 29.25  ? 1439 ASN A CA    1 
ATOM   10922 C  C     . ASN A 1  1439 ? 142.004 95.328  87.770  1.00 32.13  ? 1439 ASN A C     1 
ATOM   10923 O  O     . ASN A 1  1439 ? 142.146 96.104  86.819  1.00 31.53  ? 1439 ASN A O     1 
ATOM   10924 C  CB    . ASN A 1  1439 ? 139.636 95.386  88.474  1.00 28.81  ? 1439 ASN A CB    1 
ATOM   10925 C  CG    . ASN A 1  1439 ? 138.253 94.815  88.293  1.00 31.57  ? 1439 ASN A CG    1 
ATOM   10926 O  OD1   . ASN A 1  1439 ? 137.699 94.210  89.203  1.00 31.42  ? 1439 ASN A OD1   1 
ATOM   10927 N  ND2   . ASN A 1  1439 ? 137.680 95.017  87.121  1.00 31.74  ? 1439 ASN A ND2   1 
ATOM   10928 N  N     . TYR A 1  1440 ? 142.919 95.206  88.725  1.00 36.99  ? 1440 TYR A N     1 
ATOM   10929 C  CA    . TYR A 1  1440 ? 144.129 96.010  88.790  1.00 35.80  ? 1440 TYR A CA    1 
ATOM   10930 C  C     . TYR A 1  1440 ? 145.331 95.157  88.408  1.00 38.15  ? 1440 TYR A C     1 
ATOM   10931 O  O     . TYR A 1  1440 ? 145.254 93.928  88.337  1.00 40.23  ? 1440 TYR A O     1 
ATOM   10932 C  CB    . TYR A 1  1440 ? 144.326 96.615  90.188  1.00 31.85  ? 1440 TYR A CB    1 
ATOM   10933 C  CG    . TYR A 1  1440 ? 143.329 97.696  90.563  1.00 35.48  ? 1440 TYR A CG    1 
ATOM   10934 C  CD1   . TYR A 1  1440 ? 143.722 98.808  91.279  1.00 35.99  ? 1440 TYR A CD1   1 
ATOM   10935 C  CD2   . TYR A 1  1440 ? 141.994 97.598  90.207  1.00 38.04  ? 1440 TYR A CD2   1 
ATOM   10936 C  CE1   . TYR A 1  1440 ? 142.819 99.791  91.616  1.00 33.71  ? 1440 TYR A CE1   1 
ATOM   10937 C  CE2   . TYR A 1  1440 ? 141.092 98.571  90.543  1.00 33.60  ? 1440 TYR A CE2   1 
ATOM   10938 C  CZ    . TYR A 1  1440 ? 141.509 99.666  91.244  1.00 31.72  ? 1440 TYR A CZ    1 
ATOM   10939 O  OH    . TYR A 1  1440 ? 140.602 100.640 91.575  1.00 36.47  ? 1440 TYR A OH    1 
ATOM   10940 N  N     . LYS A 1  1441 ? 146.453 95.822  88.155  1.00 40.30  ? 1441 LYS A N     1 
ATOM   10941 C  CA    . LYS A 1  1441 ? 147.653 95.158  87.671  1.00 39.74  ? 1441 LYS A CA    1 
ATOM   10942 C  C     . LYS A 1  1441 ? 148.868 95.635  88.452  1.00 39.16  ? 1441 LYS A C     1 
ATOM   10943 O  O     . LYS A 1  1441 ? 148.939 96.790  88.877  1.00 40.70  ? 1441 LYS A O     1 
ATOM   10944 C  CB    . LYS A 1  1441 ? 147.842 95.405  86.168  1.00 39.36  ? 1441 LYS A CB    1 
ATOM   10945 C  CG    . LYS A 1  1441 ? 148.057 96.861  85.780  1.00 39.25  ? 1441 LYS A CG    1 
ATOM   10946 C  CD    . LYS A 1  1441 ? 147.970 97.034  84.273  1.00 40.36  ? 1441 LYS A CD    1 
ATOM   10947 C  CE    . LYS A 1  1441 ? 149.113 96.331  83.556  1.00 44.06  ? 1441 LYS A CE    1 
ATOM   10948 N  NZ    . LYS A 1  1441 ? 149.032 96.496  82.076  1.00 43.78  ? 1441 LYS A NZ    1 
ATOM   10949 N  N     . SER A 1  1442 ? 149.822 94.729  88.642  1.00 33.98  ? 1442 SER A N     1 
ATOM   10950 C  CA    . SER A 1  1442 ? 151.011 95.020  89.437  1.00 35.50  ? 1442 SER A CA    1 
ATOM   10951 C  C     . SER A 1  1442 ? 151.895 96.065  88.767  1.00 37.05  ? 1442 SER A C     1 
ATOM   10952 O  O     . SER A 1  1442 ? 152.300 97.042  89.394  1.00 37.58  ? 1442 SER A O     1 
ATOM   10953 C  CB    . SER A 1  1442 ? 151.815 93.744  89.684  1.00 34.14  ? 1442 SER A CB    1 
ATOM   10954 O  OG    . SER A 1  1442 ? 151.083 92.813  90.459  1.00 31.96  ? 1442 SER A OG    1 
ATOM   10955 N  N     . ILE B 2  8    ? 122.869 183.925 162.653 1.00 44.48  ? 8    ILE B N     1 
ATOM   10956 C  CA    . ILE B 2  8    ? 122.491 184.867 161.610 1.00 45.95  ? 8    ILE B CA    1 
ATOM   10957 C  C     . ILE B 2  8    ? 120.996 184.747 161.335 1.00 48.85  ? 8    ILE B C     1 
ATOM   10958 O  O     . ILE B 2  8    ? 120.442 183.647 161.358 1.00 49.30  ? 8    ILE B O     1 
ATOM   10959 C  CB    . ILE B 2  8    ? 123.309 184.628 160.328 1.00 44.81  ? 8    ILE B CB    1 
ATOM   10960 C  CG1   . ILE B 2  8    ? 124.804 184.697 160.635 1.00 44.47  ? 8    ILE B CG1   1 
ATOM   10961 C  CG2   . ILE B 2  8    ? 122.952 185.649 159.262 1.00 42.45  ? 8    ILE B CG2   1 
ATOM   10962 C  CD1   . ILE B 2  8    ? 125.683 184.274 159.483 1.00 44.94  ? 8    ILE B CD1   1 
ATOM   10963 N  N     . THR B 2  9    ? 120.346 185.881 161.081 1.00 44.50  ? 9    THR B N     1 
ATOM   10964 C  CA    . THR B 2  9    ? 118.936 185.921 160.698 1.00 41.95  ? 9    THR B CA    1 
ATOM   10965 C  C     . THR B 2  9    ? 118.860 186.134 159.189 1.00 43.22  ? 9    THR B C     1 
ATOM   10966 O  O     . THR B 2  9    ? 119.549 186.994 158.635 1.00 43.28  ? 9    THR B O     1 
ATOM   10967 C  CB    . THR B 2  9    ? 118.193 187.019 161.453 1.00 42.34  ? 9    THR B CB    1 
ATOM   10968 O  OG1   . THR B 2  9    ? 118.820 188.283 161.204 1.00 45.08  ? 9    THR B OG1   1 
ATOM   10969 C  CG2   . THR B 2  9    ? 118.192 186.741 162.946 1.00 41.37  ? 9    THR B CG2   1 
ATOM   10970 N  N     . TYR B 2  10   ? 118.030 185.339 158.523 1.00 43.37  ? 10   TYR B N     1 
ATOM   10971 C  CA    . TYR B 2  10   ? 117.863 185.474 157.086 1.00 43.33  ? 10   TYR B CA    1 
ATOM   10972 C  C     . TYR B 2  10   ? 116.525 186.133 156.765 1.00 43.17  ? 10   TYR B C     1 
ATOM   10973 O  O     . TYR B 2  10   ? 115.521 185.929 157.451 1.00 42.90  ? 10   TYR B O     1 
ATOM   10974 C  CB    . TYR B 2  10   ? 117.978 184.107 156.413 1.00 37.06  ? 10   TYR B CB    1 
ATOM   10975 C  CG    . TYR B 2  10   ? 119.257 183.404 156.789 1.00 38.41  ? 10   TYR B CG    1 
ATOM   10976 C  CD1   . TYR B 2  10   ? 120.484 183.864 156.328 1.00 40.99  ? 10   TYR B CD1   1 
ATOM   10977 C  CD2   . TYR B 2  10   ? 119.246 182.299 157.622 1.00 40.90  ? 10   TYR B CD2   1 
ATOM   10978 C  CE1   . TYR B 2  10   ? 121.657 183.237 156.679 1.00 41.35  ? 10   TYR B CE1   1 
ATOM   10979 C  CE2   . TYR B 2  10   ? 120.415 181.662 157.976 1.00 42.36  ? 10   TYR B CE2   1 
ATOM   10980 C  CZ    . TYR B 2  10   ? 121.619 182.135 157.502 1.00 43.75  ? 10   TYR B CZ    1 
ATOM   10981 O  OH    . TYR B 2  10   ? 122.791 181.504 157.851 1.00 43.58  ? 10   TYR B OH    1 
ATOM   10982 N  N     . GLY B 2  11   ? 116.523 186.932 155.700 1.00 38.31  ? 11   GLY B N     1 
ATOM   10983 C  CA    . GLY B 2  11   ? 115.367 187.709 155.325 1.00 38.50  ? 11   GLY B CA    1 
ATOM   10984 C  C     . GLY B 2  11   ? 114.181 186.828 155.002 1.00 41.03  ? 11   GLY B C     1 
ATOM   10985 O  O     . GLY B 2  11   ? 114.335 185.652 154.660 1.00 42.53  ? 11   GLY B O     1 
ATOM   10986 N  N     . PRO B 2  12   ? 112.973 187.377 155.107 1.00 40.73  ? 12   PRO B N     1 
ATOM   10987 C  CA    . PRO B 2  12   ? 111.776 186.542 154.960 1.00 38.75  ? 12   PRO B CA    1 
ATOM   10988 C  C     . PRO B 2  12   ? 111.741 185.858 153.603 1.00 41.30  ? 12   PRO B C     1 
ATOM   10989 O  O     . PRO B 2  12   ? 112.024 186.467 152.571 1.00 41.41  ? 12   PRO B O     1 
ATOM   10990 C  CB    . PRO B 2  12   ? 110.625 187.541 155.122 1.00 38.44  ? 12   PRO B CB    1 
ATOM   10991 C  CG    . PRO B 2  12   ? 111.217 188.865 154.774 1.00 39.16  ? 12   PRO B CG    1 
ATOM   10992 C  CD    . PRO B 2  12   ? 112.646 188.806 155.228 1.00 39.00  ? 12   PRO B CD    1 
ATOM   10993 N  N     . ILE B 2  13   ? 111.380 184.574 153.617 1.00 37.20  ? 13   ILE B N     1 
ATOM   10994 C  CA    . ILE B 2  13   ? 111.394 183.780 152.396 1.00 36.91  ? 13   ILE B CA    1 
ATOM   10995 C  C     . ILE B 2  13   ? 110.297 184.201 151.436 1.00 38.08  ? 13   ILE B C     1 
ATOM   10996 O  O     . ILE B 2  13   ? 110.322 183.809 150.264 1.00 39.19  ? 13   ILE B O     1 
ATOM   10997 C  CB    . ILE B 2  13   ? 111.270 182.285 152.734 1.00 36.69  ? 13   ILE B CB    1 
ATOM   10998 C  CG1   . ILE B 2  13   ? 111.837 181.422 151.606 1.00 33.32  ? 13   ILE B CG1   1 
ATOM   10999 C  CG2   . ILE B 2  13   ? 109.825 181.918 153.009 1.00 35.55  ? 13   ILE B CG2   1 
ATOM   11000 C  CD1   . ILE B 2  13   ? 113.306 181.585 151.387 1.00 34.43  ? 13   ILE B CD1   1 
ATOM   11001 N  N     . GLU B 2  14   ? 109.346 185.007 151.892 1.00 35.85  ? 14   GLU B N     1 
ATOM   11002 C  CA    . GLU B 2  14   ? 108.226 185.412 151.059 1.00 37.62  ? 14   GLU B CA    1 
ATOM   11003 C  C     . GLU B 2  14   ? 108.548 186.597 150.164 1.00 37.99  ? 14   GLU B C     1 
ATOM   11004 O  O     . GLU B 2  14   ? 107.642 187.118 149.511 1.00 40.83  ? 14   GLU B O     1 
ATOM   11005 C  CB    . GLU B 2  14   ? 107.027 185.734 151.944 1.00 37.88  ? 14   GLU B CB    1 
ATOM   11006 C  CG    . GLU B 2  14   ? 106.740 184.639 152.952 1.00 39.25  ? 14   GLU B CG    1 
ATOM   11007 C  CD    . GLU B 2  14   ? 106.427 185.169 154.331 1.00 43.67  ? 14   GLU B CD    1 
ATOM   11008 O  OE1   . GLU B 2  14   ? 107.299 185.834 154.926 1.00 42.44  ? 14   GLU B OE1   1 
ATOM   11009 O  OE2   . GLU B 2  14   ? 105.309 184.913 154.824 1.00 42.77  ? 14   GLU B OE2   1 
ATOM   11010 N  N     . THR B 2  15   ? 109.800 187.038 150.125 1.00 38.53  ? 15   THR B N     1 
ATOM   11011 C  CA    . THR B 2  15   ? 110.230 188.153 149.293 1.00 37.73  ? 15   THR B CA    1 
ATOM   11012 C  C     . THR B 2  15   ? 111.492 187.805 148.513 1.00 39.07  ? 15   THR B C     1 
ATOM   11013 O  O     . THR B 2  15   ? 112.457 188.570 148.487 1.00 39.88  ? 15   THR B O     1 
ATOM   11014 C  CB    . THR B 2  15   ? 110.461 189.404 150.134 1.00 38.29  ? 15   THR B CB    1 
ATOM   11015 O  OG1   . THR B 2  15   ? 111.380 189.103 151.189 1.00 40.34  ? 15   THR B OG1   1 
ATOM   11016 C  CG2   . THR B 2  15   ? 109.149 189.902 150.730 1.00 35.58  ? 15   THR B CG2   1 
ATOM   11017 N  N     . VAL B 2  16   ? 111.504 186.640 147.873 1.00 37.91  ? 16   VAL B N     1 
ATOM   11018 C  CA    . VAL B 2  16   ? 112.606 186.209 147.020 1.00 39.35  ? 16   VAL B CA    1 
ATOM   11019 C  C     . VAL B 2  16   ? 112.080 186.085 145.597 1.00 38.27  ? 16   VAL B C     1 
ATOM   11020 O  O     . VAL B 2  16   ? 110.992 185.542 145.376 1.00 36.08  ? 16   VAL B O     1 
ATOM   11021 C  CB    . VAL B 2  16   ? 113.217 184.883 147.508 1.00 38.51  ? 16   VAL B CB    1 
ATOM   11022 C  CG1   . VAL B 2  16   ? 114.410 184.500 146.658 1.00 33.75  ? 16   VAL B CG1   1 
ATOM   11023 C  CG2   . VAL B 2  16   ? 113.635 185.000 148.959 1.00 35.51  ? 16   VAL B CG2   1 
ATOM   11024 N  N     . ASP B 2  17   ? 112.835 186.614 144.638 1.00 36.70  ? 17   ASP B N     1 
ATOM   11025 C  CA    . ASP B 2  17   ? 112.441 186.587 143.234 1.00 38.05  ? 17   ASP B CA    1 
ATOM   11026 C  C     . ASP B 2  17   ? 113.130 185.420 142.542 1.00 39.46  ? 17   ASP B C     1 
ATOM   11027 O  O     . ASP B 2  17   ? 114.308 185.507 142.187 1.00 40.88  ? 17   ASP B O     1 
ATOM   11028 C  CB    . ASP B 2  17   ? 112.792 187.900 142.544 1.00 39.97  ? 17   ASP B CB    1 
ATOM   11029 C  CG    . ASP B 2  17   ? 112.117 189.086 143.178 1.00 42.03  ? 17   ASP B CG    1 
ATOM   11030 O  OD1   . ASP B 2  17   ? 112.659 190.202 143.058 1.00 39.85  ? 17   ASP B OD1   1 
ATOM   11031 O  OD2   . ASP B 2  17   ? 111.051 188.907 143.800 1.00 43.20  ? 17   ASP B OD2   1 
ATOM   11032 N  N     . ASN B 2  18   ? 112.390 184.334 142.344 1.00 36.21  ? 18   ASN B N     1 
ATOM   11033 C  CA    . ASN B 2  18   ? 112.894 183.168 141.646 1.00 34.83  ? 18   ASN B CA    1 
ATOM   11034 C  C     . ASN B 2  18   ? 111.975 182.692 140.540 1.00 39.74  ? 18   ASN B C     1 
ATOM   11035 O  O     . ASN B 2  18   ? 112.214 181.614 139.989 1.00 41.59  ? 18   ASN B O     1 
ATOM   11036 C  CB    . ASN B 2  18   ? 113.112 182.004 142.614 1.00 33.40  ? 18   ASN B CB    1 
ATOM   11037 C  CG    . ASN B 2  18   ? 114.130 182.307 143.647 1.00 34.40  ? 18   ASN B CG    1 
ATOM   11038 O  OD1   . ASN B 2  18   ? 114.993 183.144 143.437 1.00 38.66  ? 18   ASN B OD1   1 
ATOM   11039 N  ND2   . ASN B 2  18   ? 114.067 181.608 144.765 1.00 32.90  ? 18   ASN B ND2   1 
ATOM   11040 N  N     . GLU B 2  19   ? 110.922 183.436 140.216 1.00 40.83  ? 19   GLU B N     1 
ATOM   11041 C  CA    . GLU B 2  19   ? 109.993 182.959 139.205 1.00 38.73  ? 19   GLU B CA    1 
ATOM   11042 C  C     . GLU B 2  19   ? 110.607 182.937 137.818 1.00 40.00  ? 19   GLU B C     1 
ATOM   11043 O  O     . GLU B 2  19   ? 110.080 182.250 136.939 1.00 41.57  ? 19   GLU B O     1 
ATOM   11044 C  CB    . GLU B 2  19   ? 108.732 183.813 139.227 1.00 39.75  ? 19   GLU B CB    1 
ATOM   11045 C  CG    . GLU B 2  19   ? 107.925 183.617 140.490 1.00 41.51  ? 19   GLU B CG    1 
ATOM   11046 C  CD    . GLU B 2  19   ? 107.700 182.147 140.804 1.00 46.52  ? 19   GLU B CD    1 
ATOM   11047 O  OE1   . GLU B 2  19   ? 108.062 181.705 141.917 1.00 42.86  ? 19   GLU B OE1   1 
ATOM   11048 O  OE2   . GLU B 2  19   ? 107.151 181.433 139.941 1.00 45.99  ? 19   GLU B OE2   1 
ATOM   11049 N  N     . GLU B 2  20   ? 111.705 183.651 137.604 1.00 36.34  ? 20   GLU B N     1 
ATOM   11050 C  CA    . GLU B 2  20   ? 112.414 183.635 136.337 1.00 34.83  ? 20   GLU B CA    1 
ATOM   11051 C  C     . GLU B 2  20   ? 113.665 182.772 136.387 1.00 37.54  ? 20   GLU B C     1 
ATOM   11052 O  O     . GLU B 2  20   ? 114.548 182.929 135.540 1.00 36.64  ? 20   GLU B O     1 
ATOM   11053 C  CB    . GLU B 2  20   ? 112.764 185.059 135.901 1.00 37.96  ? 20   GLU B CB    1 
ATOM   11054 C  CG    . GLU B 2  20   ? 113.685 185.830 136.840 1.00 39.98  ? 20   GLU B CG    1 
ATOM   11055 C  CD    . GLU B 2  20   ? 113.003 186.307 138.106 1.00 41.50  ? 20   GLU B CD    1 
ATOM   11056 O  OE1   . GLU B 2  20   ? 113.712 186.771 139.020 1.00 38.00  ? 20   GLU B OE1   1 
ATOM   11057 O  OE2   . GLU B 2  20   ? 111.762 186.223 138.184 1.00 41.34  ? 20   GLU B OE2   1 
ATOM   11058 N  N     . LEU B 2  21   ? 113.769 181.885 137.370 1.00 30.34  ? 21   LEU B N     1 
ATOM   11059 C  CA    . LEU B 2  21   ? 114.817 180.869 137.404 1.00 26.89  ? 21   LEU B CA    1 
ATOM   11060 C  C     . LEU B 2  21   ? 114.461 179.777 136.411 1.00 28.25  ? 21   LEU B C     1 
ATOM   11061 O  O     . LEU B 2  21   ? 113.398 179.165 136.502 1.00 32.14  ? 21   LEU B O     1 
ATOM   11062 C  CB    . LEU B 2  21   ? 114.964 180.291 138.806 1.00 24.19  ? 21   LEU B CB    1 
ATOM   11063 C  CG    . LEU B 2  21   ? 116.164 180.690 139.655 1.00 24.92  ? 21   LEU B CG    1 
ATOM   11064 C  CD1   . LEU B 2  21   ? 116.119 179.979 140.982 1.00 25.11  ? 21   LEU B CD1   1 
ATOM   11065 C  CD2   . LEU B 2  21   ? 117.433 180.349 138.927 1.00 26.27  ? 21   LEU B CD2   1 
ATOM   11066 N  N     . THR B 2  22   ? 115.344 179.525 135.453 1.00 25.86  ? 22   THR B N     1 
ATOM   11067 C  CA    . THR B 2  22   ? 115.130 178.427 134.528 1.00 23.96  ? 22   THR B CA    1 
ATOM   11068 C  C     . THR B 2  22   ? 116.044 177.258 134.867 1.00 24.54  ? 22   THR B C     1 
ATOM   11069 O  O     . THR B 2  22   ? 116.965 177.367 135.675 1.00 26.66  ? 22   THR B O     1 
ATOM   11070 C  CB    . THR B 2  22   ? 115.367 178.870 133.085 1.00 26.72  ? 22   THR B CB    1 
ATOM   11071 O  OG1   . THR B 2  22   ? 116.703 179.350 132.942 1.00 26.31  ? 22   THR B OG1   1 
ATOM   11072 C  CG2   . THR B 2  22   ? 114.409 179.970 132.705 1.00 24.99  ? 22   THR B CG2   1 
ATOM   11073 N  N     . GLU B 2  23   ? 115.773 176.121 134.230 1.00 26.63  ? 23   GLU B N     1 
ATOM   11074 C  CA    . GLU B 2  23   ? 116.604 174.941 134.404 1.00 21.93  ? 23   GLU B CA    1 
ATOM   11075 C  C     . GLU B 2  23   ? 117.989 175.101 133.799 1.00 22.83  ? 23   GLU B C     1 
ATOM   11076 O  O     . GLU B 2  23   ? 118.894 174.350 134.166 1.00 26.97  ? 23   GLU B O     1 
ATOM   11077 C  CB    . GLU B 2  23   ? 115.906 173.727 133.805 1.00 23.43  ? 23   GLU B CB    1 
ATOM   11078 C  CG    . GLU B 2  23   ? 114.748 173.237 134.642 1.00 27.46  ? 23   GLU B CG    1 
ATOM   11079 C  CD    . GLU B 2  23   ? 114.295 171.841 134.265 1.00 32.92  ? 23   GLU B CD    1 
ATOM   11080 O  OE1   . GLU B 2  23   ? 113.340 171.718 133.471 1.00 33.32  ? 23   GLU B OE1   1 
ATOM   11081 O  OE2   . GLU B 2  23   ? 114.888 170.863 134.771 1.00 28.22  ? 23   GLU B OE2   1 
ATOM   11082 N  N     . ALA B 2  24   ? 118.176 176.040 132.878 1.00 23.66  ? 24   ALA B N     1 
ATOM   11083 C  CA    . ALA B 2  24   ? 119.514 176.358 132.397 1.00 25.41  ? 24   ALA B CA    1 
ATOM   11084 C  C     . ALA B 2  24   ? 120.246 177.292 133.347 1.00 26.74  ? 24   ALA B C     1 
ATOM   11085 O  O     . ALA B 2  24   ? 121.476 177.367 133.312 1.00 29.33  ? 24   ALA B O     1 
ATOM   11086 C  CB    . ALA B 2  24   ? 119.439 176.979 131.004 1.00 26.63  ? 24   ALA B CB    1 
ATOM   11087 N  N     . ASP B 2  25   ? 119.506 178.020 134.182 1.00 24.68  ? 25   ASP B N     1 
ATOM   11088 C  CA    . ASP B 2  25   ? 120.118 178.824 135.232 1.00 23.54  ? 25   ASP B CA    1 
ATOM   11089 C  C     . ASP B 2  25   ? 120.687 177.953 136.335 1.00 24.57  ? 25   ASP B C     1 
ATOM   11090 O  O     . ASP B 2  25   ? 121.641 178.344 137.009 1.00 25.29  ? 25   ASP B O     1 
ATOM   11091 C  CB    . ASP B 2  25   ? 119.082 179.774 135.818 1.00 24.11  ? 25   ASP B CB    1 
ATOM   11092 C  CG    . ASP B 2  25   ? 118.945 181.045 135.031 1.00 32.16  ? 25   ASP B CG    1 
ATOM   11093 O  OD1   . ASP B 2  25   ? 119.011 180.989 133.788 1.00 32.95  ? 25   ASP B OD1   1 
ATOM   11094 O  OD2   . ASP B 2  25   ? 118.738 182.102 135.659 1.00 34.71  ? 25   ASP B OD2   1 
ATOM   11095 N  N     . MET B 2  26   ? 120.108 176.779 136.537 1.00 21.82  ? 26   MET B N     1 
ATOM   11096 C  CA    . MET B 2  26   ? 120.496 175.870 137.598 1.00 14.36  ? 26   MET B CA    1 
ATOM   11097 C  C     . MET B 2  26   ? 121.772 175.106 137.290 1.00 19.89  ? 26   MET B C     1 
ATOM   11098 O  O     . MET B 2  26   ? 122.341 174.500 138.198 1.00 30.87  ? 26   MET B O     1 
ATOM   11099 C  CB    . MET B 2  26   ? 119.357 174.891 137.855 1.00 16.76  ? 26   MET B CB    1 
ATOM   11100 C  CG    . MET B 2  26   ? 118.136 175.513 138.490 1.00 18.15  ? 26   MET B CG    1 
ATOM   11101 S  SD    . MET B 2  26   ? 118.524 176.684 139.790 1.00 27.34  ? 26   MET B SD    1 
ATOM   11102 C  CE    . MET B 2  26   ? 117.688 175.910 141.155 1.00 18.23  ? 26   MET B CE    1 
ATOM   11103 N  N     . LEU B 2  27   ? 122.224 175.102 136.037 1.00 17.56  ? 27   LEU B N     1 
ATOM   11104 C  CA    . LEU B 2  27   ? 123.486 174.461 135.692 1.00 13.40  ? 27   LEU B CA    1 
ATOM   11105 C  C     . LEU B 2  27   ? 124.684 175.256 136.182 1.00 16.12  ? 27   LEU B C     1 
ATOM   11106 O  O     . LEU B 2  27   ? 125.793 174.716 136.260 1.00 20.82  ? 27   LEU B O     1 
ATOM   11107 C  CB    . LEU B 2  27   ? 123.575 174.275 134.185 1.00 17.32  ? 27   LEU B CB    1 
ATOM   11108 C  CG    . LEU B 2  27   ? 122.878 173.059 133.603 1.00 14.22  ? 27   LEU B CG    1 
ATOM   11109 C  CD1   . LEU B 2  27   ? 122.951 173.137 132.116 1.00 13.56  ? 27   LEU B CD1   1 
ATOM   11110 C  CD2   . LEU B 2  27   ? 123.555 171.815 134.087 1.00 14.84  ? 27   LEU B CD2   1 
ATOM   11111 N  N     . SER B 2  28   ? 124.484 176.529 136.505 1.00 20.38  ? 28   SER B N     1 
ATOM   11112 C  CA    . SER B 2  28   ? 125.556 177.324 137.080 1.00 16.81  ? 28   SER B CA    1 
ATOM   11113 C  C     . SER B 2  28   ? 125.911 176.857 138.484 1.00 17.89  ? 28   SER B C     1 
ATOM   11114 O  O     . SER B 2  28   ? 127.055 177.014 138.912 1.00 23.82  ? 28   SER B O     1 
ATOM   11115 C  CB    . SER B 2  28   ? 125.158 178.789 137.070 1.00 16.16  ? 28   SER B CB    1 
ATOM   11116 O  OG    . SER B 2  28   ? 123.958 178.965 137.779 1.00 22.54  ? 28   SER B OG    1 
ATOM   11117 N  N     . PHE B 2  29   ? 124.957 176.280 139.213 1.00 14.17  ? 29   PHE B N     1 
ATOM   11118 C  CA    . PHE B 2  29   ? 125.284 175.672 140.496 1.00 10.87  ? 29   PHE B CA    1 
ATOM   11119 C  C     . PHE B 2  29   ? 126.250 174.511 140.317 1.00 14.97  ? 29   PHE B C     1 
ATOM   11120 O  O     . PHE B 2  29   ? 127.196 174.350 141.095 1.00 19.33  ? 29   PHE B O     1 
ATOM   11121 C  CB    . PHE B 2  29   ? 124.012 175.206 141.199 1.00 12.11  ? 29   PHE B CB    1 
ATOM   11122 C  CG    . PHE B 2  29   ? 124.258 174.595 142.543 1.00 17.46  ? 29   PHE B CG    1 
ATOM   11123 C  CD1   . PHE B 2  29   ? 124.499 175.388 143.647 1.00 18.03  ? 29   PHE B CD1   1 
ATOM   11124 C  CD2   . PHE B 2  29   ? 124.265 173.225 142.703 1.00 13.95  ? 29   PHE B CD2   1 
ATOM   11125 C  CE1   . PHE B 2  29   ? 124.737 174.820 144.874 1.00 13.47  ? 29   PHE B CE1   1 
ATOM   11126 C  CE2   . PHE B 2  29   ? 124.500 172.664 143.926 1.00 10.68  ? 29   PHE B CE2   1 
ATOM   11127 C  CZ    . PHE B 2  29   ? 124.737 173.464 145.010 1.00 12.22  ? 29   PHE B CZ    1 
ATOM   11128 N  N     . ILE B 2  30   ? 126.026 173.691 139.295 1.00 13.14  ? 30   ILE B N     1 
ATOM   11129 C  CA    . ILE B 2  30   ? 126.932 172.592 139.000 1.00 11.78  ? 30   ILE B CA    1 
ATOM   11130 C  C     . ILE B 2  30   ? 128.289 173.124 138.571 1.00 15.80  ? 30   ILE B C     1 
ATOM   11131 O  O     . ILE B 2  30   ? 129.338 172.577 138.940 1.00 20.15  ? 30   ILE B O     1 
ATOM   11132 C  CB    . ILE B 2  30   ? 126.303 171.685 137.933 1.00 11.54  ? 30   ILE B CB    1 
ATOM   11133 C  CG1   . ILE B 2  30   ? 125.102 170.967 138.528 1.00 12.09  ? 30   ILE B CG1   1 
ATOM   11134 C  CG2   . ILE B 2  30   ? 127.305 170.685 137.418 1.00 8.15   ? 30   ILE B CG2   1 
ATOM   11135 C  CD1   . ILE B 2  30   ? 124.514 169.967 137.636 1.00 11.53  ? 30   ILE B CD1   1 
ATOM   11136 N  N     . SER B 2  31   ? 128.294 174.205 137.797 1.00 20.40  ? 31   SER B N     1 
ATOM   11137 C  CA    . SER B 2  31   ? 129.553 174.835 137.421 1.00 16.36  ? 31   SER B CA    1 
ATOM   11138 C  C     . SER B 2  31   ? 130.327 175.295 138.650 1.00 20.81  ? 31   SER B C     1 
ATOM   11139 O  O     . SER B 2  31   ? 131.533 175.061 138.759 1.00 28.78  ? 31   SER B O     1 
ATOM   11140 C  CB    . SER B 2  31   ? 129.281 176.005 136.484 1.00 19.97  ? 31   SER B CB    1 
ATOM   11141 O  OG    . SER B 2  31   ? 130.476 176.683 136.162 1.00 27.66  ? 31   SER B OG    1 
ATOM   11142 N  N     . ALA B 2  32   ? 129.642 175.945 139.592 1.00 20.04  ? 32   ALA B N     1 
ATOM   11143 C  CA    . ALA B 2  32   ? 130.295 176.410 140.811 1.00 18.75  ? 32   ALA B CA    1 
ATOM   11144 C  C     . ALA B 2  32   ? 130.832 175.247 141.631 1.00 18.93  ? 32   ALA B C     1 
ATOM   11145 O  O     . ALA B 2  32   ? 131.949 175.310 142.162 1.00 25.42  ? 32   ALA B O     1 
ATOM   11146 C  CB    . ALA B 2  32   ? 129.319 177.241 141.640 1.00 10.67  ? 32   ALA B CB    1 
ATOM   11147 N  N     . ALA B 2  33   ? 130.049 174.176 141.748 1.00 19.17  ? 33   ALA B N     1 
ATOM   11148 C  CA    . ALA B 2  33   ? 130.489 173.019 142.512 1.00 16.98  ? 33   ALA B CA    1 
ATOM   11149 C  C     . ALA B 2  33   ? 131.755 172.416 141.925 1.00 22.69  ? 33   ALA B C     1 
ATOM   11150 O  O     . ALA B 2  33   ? 132.710 172.127 142.656 1.00 26.35  ? 33   ALA B O     1 
ATOM   11151 C  CB    . ALA B 2  33   ? 129.374 171.982 142.564 1.00 16.63  ? 33   ALA B CB    1 
ATOM   11152 N  N     . VAL B 2  34   ? 131.795 172.236 140.604 1.00 24.85  ? 34   VAL B N     1 
ATOM   11153 C  CA    . VAL B 2  34   ? 132.979 171.643 139.992 1.00 23.00  ? 34   VAL B CA    1 
ATOM   11154 C  C     . VAL B 2  34   ? 134.169 172.594 140.084 1.00 25.84  ? 34   VAL B C     1 
ATOM   11155 O  O     . VAL B 2  34   ? 135.302 172.164 140.320 1.00 29.37  ? 34   VAL B O     1 
ATOM   11156 C  CB    . VAL B 2  34   ? 132.682 171.228 138.542 1.00 16.32  ? 34   VAL B CB    1 
ATOM   11157 C  CG1   . VAL B 2  34   ? 133.916 170.677 137.889 1.00 18.14  ? 34   VAL B CG1   1 
ATOM   11158 C  CG2   . VAL B 2  34   ? 131.601 170.189 138.517 1.00 21.55  ? 34   VAL B CG2   1 
ATOM   11159 N  N     . ASN B 2  35   ? 133.939 173.897 139.910 1.00 22.91  ? 35   ASN B N     1 
ATOM   11160 C  CA    . ASN B 2  35   ? 135.042 174.850 139.965 1.00 25.96  ? 35   ASN B CA    1 
ATOM   11161 C  C     . ASN B 2  35   ? 135.687 174.879 141.342 1.00 33.89  ? 35   ASN B C     1 
ATOM   11162 O  O     . ASN B 2  35   ? 136.913 174.952 141.454 1.00 40.31  ? 35   ASN B O     1 
ATOM   11163 C  CB    . ASN B 2  35   ? 134.563 176.247 139.581 1.00 28.37  ? 35   ASN B CB    1 
ATOM   11164 C  CG    . ASN B 2  35   ? 134.391 176.411 138.093 1.00 35.29  ? 35   ASN B CG    1 
ATOM   11165 O  OD1   . ASN B 2  35   ? 135.090 175.780 137.305 1.00 38.29  ? 35   ASN B OD1   1 
ATOM   11166 N  ND2   . ASN B 2  35   ? 133.464 177.272 137.696 1.00 34.33  ? 35   ASN B ND2   1 
ATOM   11167 N  N     . SER B 2  36   ? 134.882 174.853 142.402 1.00 30.88  ? 36   SER B N     1 
ATOM   11168 C  CA    . SER B 2  36   ? 135.458 174.791 143.740 1.00 29.63  ? 36   SER B CA    1 
ATOM   11169 C  C     . SER B 2  36   ? 136.159 173.460 143.971 1.00 31.69  ? 36   SER B C     1 
ATOM   11170 O  O     . SER B 2  36   ? 137.314 173.420 144.408 1.00 29.42  ? 36   SER B O     1 
ATOM   11171 C  CB    . SER B 2  36   ? 134.374 174.996 144.788 1.00 31.37  ? 36   SER B CB    1 
ATOM   11172 O  OG    . SER B 2  36   ? 133.727 173.770 145.053 1.00 32.63  ? 36   SER B OG    1 
ATOM   11173 N  N     . THR B 2  37   ? 135.469 172.357 143.676 1.00 29.35  ? 37   THR B N     1 
ATOM   11174 C  CA    . THR B 2  37   ? 136.000 171.032 143.975 1.00 30.36  ? 37   THR B CA    1 
ATOM   11175 C  C     . THR B 2  37   ? 137.198 170.697 143.095 1.00 31.84  ? 37   THR B C     1 
ATOM   11176 O  O     . THR B 2  37   ? 138.171 170.096 143.561 1.00 34.40  ? 37   THR B O     1 
ATOM   11177 C  CB    . THR B 2  37   ? 134.886 169.996 143.800 1.00 34.30  ? 37   THR B CB    1 
ATOM   11178 O  OG1   . THR B 2  37   ? 133.884 170.203 144.799 1.00 38.27  ? 37   THR B OG1   1 
ATOM   11179 C  CG2   . THR B 2  37   ? 135.410 168.581 143.924 1.00 31.28  ? 37   THR B CG2   1 
ATOM   11180 N  N     . GLY B 2  38   ? 137.146 171.076 141.821 1.00 35.92  ? 38   GLY B N     1 
ATOM   11181 C  CA    . GLY B 2  38   ? 138.078 170.567 140.832 1.00 35.87  ? 38   GLY B CA    1 
ATOM   11182 C  C     . GLY B 2  38   ? 137.677 169.157 140.456 1.00 36.18  ? 38   GLY B C     1 
ATOM   11183 O  O     . GLY B 2  38   ? 137.072 168.461 141.273 1.00 35.76  ? 38   GLY B O     1 
ATOM   11184 N  N     . LEU B 2  39   ? 137.972 168.711 139.237 1.00 34.88  ? 39   LEU B N     1 
ATOM   11185 C  CA    . LEU B 2  39   ? 137.614 167.342 138.878 1.00 32.75  ? 39   LEU B CA    1 
ATOM   11186 C  C     . LEU B 2  39   ? 138.358 166.348 139.757 1.00 33.37  ? 39   LEU B C     1 
ATOM   11187 O  O     . LEU B 2  39   ? 137.785 165.356 140.217 1.00 34.26  ? 39   LEU B O     1 
ATOM   11188 C  CB    . LEU B 2  39   ? 137.891 167.073 137.399 1.00 35.63  ? 39   LEU B CB    1 
ATOM   11189 C  CG    . LEU B 2  39   ? 136.938 167.696 136.373 1.00 35.62  ? 39   LEU B CG    1 
ATOM   11190 C  CD1   . LEU B 2  39   ? 135.495 167.373 136.728 1.00 31.20  ? 39   LEU B CD1   1 
ATOM   11191 C  CD2   . LEU B 2  39   ? 137.148 169.191 136.212 1.00 36.24  ? 39   LEU B CD2   1 
ATOM   11192 N  N     . ILE B 2  40   ? 139.639 166.606 140.007 1.00 39.90  ? 40   ILE B N     1 
ATOM   11193 C  CA    . ILE B 2  40   ? 140.443 165.812 140.928 1.00 40.86  ? 40   ILE B CA    1 
ATOM   11194 C  C     . ILE B 2  40   ? 140.846 166.703 142.094 1.00 41.40  ? 40   ILE B C     1 
ATOM   11195 O  O     . ILE B 2  40   ? 141.863 167.403 142.030 1.00 42.08  ? 40   ILE B O     1 
ATOM   11196 C  CB    . ILE B 2  40   ? 141.688 165.235 140.230 1.00 40.74  ? 40   ILE B CB    1 
ATOM   11197 C  CG1   . ILE B 2  40   ? 141.305 164.430 138.984 1.00 40.65  ? 40   ILE B CG1   1 
ATOM   11198 C  CG2   . ILE B 2  40   ? 142.478 164.374 141.195 1.00 39.78  ? 40   ILE B CG2   1 
ATOM   11199 C  CD1   . ILE B 2  40   ? 140.118 163.528 139.162 1.00 39.18  ? 40   ILE B CD1   1 
ATOM   11200 N  N     . GLY B 2  41   ? 140.053 166.704 143.160 1.00 34.23  ? 41   GLY B N     1 
ATOM   11201 C  CA    . GLY B 2  41   ? 140.363 167.571 144.279 1.00 33.64  ? 41   GLY B CA    1 
ATOM   11202 C  C     . GLY B 2  41   ? 140.933 166.850 145.479 1.00 33.49  ? 41   GLY B C     1 
ATOM   11203 O  O     . GLY B 2  41   ? 141.947 167.263 146.044 1.00 34.21  ? 41   GLY B O     1 
ATOM   11204 N  N     . TYR B 2  42   ? 140.294 165.744 145.853 1.00 36.84  ? 42   TYR B N     1 
ATOM   11205 C  CA    . TYR B 2  42   ? 140.660 165.022 147.062 1.00 34.61  ? 42   TYR B CA    1 
ATOM   11206 C  C     . TYR B 2  42   ? 141.996 164.316 146.931 1.00 37.52  ? 42   TYR B C     1 
ATOM   11207 O  O     . TYR B 2  42   ? 142.699 164.143 147.930 1.00 39.09  ? 42   TYR B O     1 
ATOM   11208 C  CB    . TYR B 2  42   ? 139.567 164.011 147.402 1.00 34.01  ? 42   TYR B CB    1 
ATOM   11209 C  CG    . TYR B 2  42   ? 139.936 162.982 148.452 1.00 34.74  ? 42   TYR B CG    1 
ATOM   11210 C  CD1   . TYR B 2  42   ? 140.021 163.327 149.791 1.00 34.28  ? 42   TYR B CD1   1 
ATOM   11211 C  CD2   . TYR B 2  42   ? 140.164 161.658 148.102 1.00 34.93  ? 42   TYR B CD2   1 
ATOM   11212 C  CE1   . TYR B 2  42   ? 140.336 162.390 150.748 1.00 36.96  ? 42   TYR B CE1   1 
ATOM   11213 C  CE2   . TYR B 2  42   ? 140.482 160.715 149.053 1.00 34.74  ? 42   TYR B CE2   1 
ATOM   11214 C  CZ    . TYR B 2  42   ? 140.566 161.085 150.374 1.00 36.80  ? 42   TYR B CZ    1 
ATOM   11215 O  OH    . TYR B 2  42   ? 140.880 160.148 151.328 1.00 35.84  ? 42   TYR B OH    1 
ATOM   11216 N  N     . ASN B 2  43   ? 142.360 163.898 145.722 1.00 35.29  ? 43   ASN B N     1 
ATOM   11217 C  CA    . ASN B 2  43   ? 143.567 163.101 145.563 1.00 36.04  ? 43   ASN B CA    1 
ATOM   11218 C  C     . ASN B 2  43   ? 144.815 163.902 145.912 1.00 38.09  ? 43   ASN B C     1 
ATOM   11219 O  O     . ASN B 2  43   ? 145.789 163.337 146.420 1.00 41.12  ? 43   ASN B O     1 
ATOM   11220 C  CB    . ASN B 2  43   ? 143.641 162.558 144.139 1.00 38.37  ? 43   ASN B CB    1 
ATOM   11221 C  CG    . ASN B 2  43   ? 144.084 161.116 144.092 1.00 38.13  ? 43   ASN B CG    1 
ATOM   11222 O  OD1   . ASN B 2  43   ? 144.379 160.512 145.121 1.00 38.62  ? 43   ASN B OD1   1 
ATOM   11223 N  ND2   . ASN B 2  43   ? 144.106 160.545 142.900 1.00 34.60  ? 43   ASN B ND2   1 
ATOM   11224 N  N     . ILE B 2  44   ? 144.808 165.209 145.668 1.00 33.64  ? 44   ILE B N     1 
ATOM   11225 C  CA    . ILE B 2  44   ? 145.963 166.021 146.026 1.00 36.90  ? 44   ILE B CA    1 
ATOM   11226 C  C     . ILE B 2  44   ? 145.869 166.567 147.452 1.00 39.31  ? 44   ILE B C     1 
ATOM   11227 O  O     . ILE B 2  44   ? 146.895 166.706 148.128 1.00 43.67  ? 44   ILE B O     1 
ATOM   11228 C  CB    . ILE B 2  44   ? 146.166 167.150 145.003 1.00 35.71  ? 44   ILE B CB    1 
ATOM   11229 C  CG1   . ILE B 2  44   ? 146.282 166.565 143.596 1.00 38.97  ? 44   ILE B CG1   1 
ATOM   11230 C  CG2   . ILE B 2  44   ? 147.413 167.940 145.325 1.00 32.15  ? 44   ILE B CG2   1 
ATOM   11231 C  CD1   . ILE B 2  44   ? 146.265 167.592 142.496 1.00 39.69  ? 44   ILE B CD1   1 
ATOM   11232 N  N     . LYS B 2  45   ? 144.667 166.873 147.936 1.00 34.54  ? 45   LYS B N     1 
ATOM   11233 C  CA    . LYS B 2  45   ? 144.520 167.290 149.325 1.00 35.37  ? 45   LYS B CA    1 
ATOM   11234 C  C     . LYS B 2  45   ? 144.958 166.186 150.279 1.00 37.06  ? 45   LYS B C     1 
ATOM   11235 O  O     . LYS B 2  45   ? 145.630 166.449 151.285 1.00 38.81  ? 45   LYS B O     1 
ATOM   11236 C  CB    . LYS B 2  45   ? 143.071 167.680 149.599 1.00 34.54  ? 45   LYS B CB    1 
ATOM   11237 C  CG    . LYS B 2  45   ? 142.775 169.152 149.445 1.00 37.48  ? 45   LYS B CG    1 
ATOM   11238 C  CD    . LYS B 2  45   ? 141.371 169.449 149.918 1.00 37.15  ? 45   LYS B CD    1 
ATOM   11239 C  CE    . LYS B 2  45   ? 141.267 169.327 151.428 1.00 35.18  ? 45   LYS B CE    1 
ATOM   11240 N  NZ    . LYS B 2  45   ? 140.034 169.980 151.949 1.00 37.15  ? 45   LYS B NZ    1 
ATOM   11241 N  N     . SER B 2  46   ? 144.586 164.942 149.977 1.00 37.66  ? 46   SER B N     1 
ATOM   11242 C  CA    . SER B 2  46   ? 144.976 163.821 150.821 1.00 37.60  ? 46   SER B CA    1 
ATOM   11243 C  C     . SER B 2  46   ? 146.488 163.654 150.857 1.00 37.27  ? 46   SER B C     1 
ATOM   11244 O  O     . SER B 2  46   ? 147.066 163.403 151.920 1.00 42.84  ? 46   SER B O     1 
ATOM   11245 C  CB    . SER B 2  46   ? 144.305 162.543 150.327 1.00 39.55  ? 46   SER B CB    1 
ATOM   11246 O  OG    . SER B 2  46   ? 144.750 161.419 151.061 1.00 40.65  ? 46   SER B OG    1 
ATOM   11247 N  N     . PHE B 2  47   ? 147.151 163.790 149.708 1.00 36.51  ? 47   PHE B N     1 
ATOM   11248 C  CA    . PHE B 2  47   ? 148.601 163.642 149.689 1.00 36.33  ? 47   PHE B CA    1 
ATOM   11249 C  C     . PHE B 2  47   ? 149.287 164.801 150.398 1.00 38.20  ? 47   PHE B C     1 
ATOM   11250 O  O     . PHE B 2  47   ? 150.316 164.609 151.054 1.00 39.70  ? 47   PHE B O     1 
ATOM   11251 C  CB    . PHE B 2  47   ? 149.111 163.511 148.258 1.00 32.17  ? 47   PHE B CB    1 
ATOM   11252 C  CG    . PHE B 2  47   ? 150.496 162.953 148.171 1.00 34.83  ? 47   PHE B CG    1 
ATOM   11253 C  CD1   . PHE B 2  47   ? 150.716 161.597 148.309 1.00 36.27  ? 47   PHE B CD1   1 
ATOM   11254 C  CD2   . PHE B 2  47   ? 151.585 163.788 147.978 1.00 35.79  ? 47   PHE B CD2   1 
ATOM   11255 C  CE1   . PHE B 2  47   ? 151.991 161.084 148.242 1.00 38.08  ? 47   PHE B CE1   1 
ATOM   11256 C  CE2   . PHE B 2  47   ? 152.862 163.279 147.910 1.00 36.18  ? 47   PHE B CE2   1 
ATOM   11257 C  CZ    . PHE B 2  47   ? 153.064 161.927 148.044 1.00 37.41  ? 47   PHE B CZ    1 
ATOM   11258 N  N     . ASP B 2  48   ? 148.741 166.011 150.279 1.00 36.43  ? 48   ASP B N     1 
ATOM   11259 C  CA    . ASP B 2  48   ? 149.307 167.134 151.018 1.00 39.08  ? 48   ASP B CA    1 
ATOM   11260 C  C     . ASP B 2  48   ? 149.188 166.922 152.521 1.00 41.54  ? 48   ASP B C     1 
ATOM   11261 O  O     . ASP B 2  48   ? 150.127 167.213 153.270 1.00 43.60  ? 48   ASP B O     1 
ATOM   11262 C  CB    . ASP B 2  48   ? 148.627 168.436 150.604 1.00 39.03  ? 48   ASP B CB    1 
ATOM   11263 C  CG    . ASP B 2  48   ? 149.161 168.972 149.303 1.00 39.30  ? 48   ASP B CG    1 
ATOM   11264 O  OD1   . ASP B 2  48   ? 150.273 168.562 148.919 1.00 39.84  ? 48   ASP B OD1   1 
ATOM   11265 O  OD2   . ASP B 2  48   ? 148.486 169.815 148.677 1.00 38.56  ? 48   ASP B OD2   1 
ATOM   11266 N  N     . ASP B 2  49   ? 148.045 166.414 152.983 1.00 44.37  ? 49   ASP B N     1 
ATOM   11267 C  CA    . ASP B 2  49   ? 147.934 166.069 154.397 1.00 43.39  ? 49   ASP B CA    1 
ATOM   11268 C  C     . ASP B 2  49   ? 148.913 164.970 154.790 1.00 43.08  ? 49   ASP B C     1 
ATOM   11269 O  O     . ASP B 2  49   ? 149.489 165.022 155.880 1.00 42.81  ? 49   ASP B O     1 
ATOM   11270 C  CB    . ASP B 2  49   ? 146.510 165.642 154.740 1.00 42.01  ? 49   ASP B CB    1 
ATOM   11271 C  CG    . ASP B 2  49   ? 146.349 165.313 156.211 1.00 47.97  ? 49   ASP B CG    1 
ATOM   11272 O  OD1   . ASP B 2  49   ? 146.318 166.250 157.033 1.00 49.33  ? 49   ASP B OD1   1 
ATOM   11273 O  OD2   . ASP B 2  49   ? 146.260 164.115 156.551 1.00 49.23  ? 49   ASP B OD2   1 
ATOM   11274 N  N     . LEU B 2  50   ? 149.107 163.969 153.933 1.00 38.22  ? 50   LEU B N     1 
ATOM   11275 C  CA    . LEU B 2  50   ? 150.050 162.905 154.261 1.00 40.29  ? 50   LEU B CA    1 
ATOM   11276 C  C     . LEU B 2  50   ? 151.473 163.441 154.366 1.00 43.14  ? 50   LEU B C     1 
ATOM   11277 O  O     . LEU B 2  50   ? 152.261 162.972 155.194 1.00 45.81  ? 50   LEU B O     1 
ATOM   11278 C  CB    . LEU B 2  50   ? 149.972 161.790 153.223 1.00 40.03  ? 50   LEU B CB    1 
ATOM   11279 C  CG    . LEU B 2  50   ? 150.908 160.617 153.499 1.00 40.00  ? 50   LEU B CG    1 
ATOM   11280 C  CD1   . LEU B 2  50   ? 150.513 159.956 154.796 1.00 38.71  ? 50   LEU B CD1   1 
ATOM   11281 C  CD2   . LEU B 2  50   ? 150.887 159.621 152.358 1.00 38.24  ? 50   LEU B CD2   1 
ATOM   11282 N  N     . MET B 2  51   ? 151.826 164.407 153.530 1.00 39.20  ? 51   MET B N     1 
ATOM   11283 C  CA    . MET B 2  51   ? 153.150 165.013 153.583 1.00 38.49  ? 51   MET B CA    1 
ATOM   11284 C  C     . MET B 2  51   ? 153.264 166.114 154.624 1.00 41.82  ? 51   MET B C     1 
ATOM   11285 O  O     . MET B 2  51   ? 154.370 166.610 154.855 1.00 45.47  ? 51   MET B O     1 
ATOM   11286 C  CB    . MET B 2  51   ? 153.536 165.572 152.213 1.00 38.70  ? 51   MET B CB    1 
ATOM   11287 C  CG    . MET B 2  51   ? 153.632 164.523 151.139 1.00 41.43  ? 51   MET B CG    1 
ATOM   11288 S  SD    . MET B 2  51   ? 155.061 163.465 151.346 1.00 48.93  ? 51   MET B SD    1 
ATOM   11289 C  CE    . MET B 2  51   ? 154.285 162.008 152.026 1.00 39.63  ? 51   MET B CE    1 
ATOM   11290 N  N     . ASP B 2  52   ? 152.160 166.516 155.249 1.00 38.84  ? 52   ASP B N     1 
ATOM   11291 C  CA    . ASP B 2  52   ? 152.184 167.587 156.235 1.00 41.50  ? 52   ASP B CA    1 
ATOM   11292 C  C     . ASP B 2  52   ? 151.858 167.101 157.642 1.00 44.45  ? 52   ASP B C     1 
ATOM   11293 O  O     . ASP B 2  52   ? 152.455 167.577 158.612 1.00 43.72  ? 52   ASP B O     1 
ATOM   11294 C  CB    . ASP B 2  52   ? 151.217 168.701 155.813 1.00 42.95  ? 52   ASP B CB    1 
ATOM   11295 C  CG    . ASP B 2  52   ? 151.209 169.864 156.784 1.00 46.81  ? 52   ASP B CG    1 
ATOM   11296 O  OD1   . ASP B 2  52   ? 152.174 170.654 156.778 1.00 47.79  ? 52   ASP B OD1   1 
ATOM   11297 O  OD2   . ASP B 2  52   ? 150.230 169.995 157.548 1.00 44.23  ? 52   ASP B OD2   1 
ATOM   11298 N  N     . ASN B 2  53   ? 150.910 166.178 157.794 1.00 44.19  ? 53   ASN B N     1 
ATOM   11299 C  CA    . ASN B 2  53   ? 150.443 165.797 159.116 1.00 41.35  ? 53   ASN B CA    1 
ATOM   11300 C  C     . ASN B 2  53   ? 150.455 164.300 159.379 1.00 42.78  ? 53   ASN B C     1 
ATOM   11301 O  O     . ASN B 2  53   ? 150.359 163.897 160.539 1.00 42.71  ? 53   ASN B O     1 
ATOM   11302 C  CB    . ASN B 2  53   ? 149.021 166.325 159.336 1.00 41.57  ? 53   ASN B CB    1 
ATOM   11303 C  CG    . ASN B 2  53   ? 148.952 167.828 159.277 1.00 44.30  ? 53   ASN B CG    1 
ATOM   11304 O  OD1   . ASN B 2  53   ? 149.814 168.520 159.812 1.00 45.83  ? 53   ASN B OD1   1 
ATOM   11305 N  ND2   . ASN B 2  53   ? 147.920 168.347 158.624 1.00 42.99  ? 53   ASN B ND2   1 
ATOM   11306 N  N     . GLY B 2  54   ? 150.545 163.470 158.351 1.00 41.46  ? 54   GLY B N     1 
ATOM   11307 C  CA    . GLY B 2  54   ? 150.428 162.043 158.559 1.00 42.43  ? 54   GLY B CA    1 
ATOM   11308 C  C     . GLY B 2  54   ? 151.746 161.343 158.792 1.00 41.55  ? 54   GLY B C     1 
ATOM   11309 O  O     . GLY B 2  54   ? 151.899 160.602 159.766 1.00 42.12  ? 54   GLY B O     1 
ATOM   11310 N  N     . ILE B 2  55   ? 152.701 161.560 157.887 1.00 39.16  ? 55   ILE B N     1 
ATOM   11311 C  CA    . ILE B 2  55   ? 153.990 160.872 157.994 1.00 40.06  ? 55   ILE B CA    1 
ATOM   11312 C  C     . ILE B 2  55   ? 154.732 161.238 159.271 1.00 40.88  ? 55   ILE B C     1 
ATOM   11313 O  O     . ILE B 2  55   ? 155.236 160.328 159.947 1.00 41.09  ? 55   ILE B O     1 
ATOM   11314 C  CB    . ILE B 2  55   ? 154.818 161.104 156.722 1.00 38.78  ? 55   ILE B CB    1 
ATOM   11315 C  CG1   . ILE B 2  55   ? 154.432 160.082 155.652 1.00 39.50  ? 55   ILE B CG1   1 
ATOM   11316 C  CG2   . ILE B 2  55   ? 156.299 161.034 157.026 1.00 41.26  ? 55   ILE B CG2   1 
ATOM   11317 C  CD1   . ILE B 2  55   ? 154.625 158.657 156.067 1.00 38.82  ? 55   ILE B CD1   1 
ATOM   11318 N  N     . PRO B 2  56   ? 154.858 162.512 159.667 1.00 44.01  ? 56   PRO B N     1 
ATOM   11319 C  CA    . PRO B 2  56   ? 155.566 162.793 160.930 1.00 46.58  ? 56   PRO B CA    1 
ATOM   11320 C  C     . PRO B 2  56   ? 154.890 162.196 162.152 1.00 47.70  ? 56   PRO B C     1 
ATOM   11321 O  O     . PRO B 2  56   ? 155.567 161.590 162.993 1.00 44.48  ? 56   PRO B O     1 
ATOM   11322 C  CB    . PRO B 2  56   ? 155.597 164.328 160.987 1.00 45.79  ? 56   PRO B CB    1 
ATOM   11323 C  CG    . PRO B 2  56   ? 155.342 164.773 159.584 1.00 44.46  ? 56   PRO B CG    1 
ATOM   11324 C  CD    . PRO B 2  56   ? 154.442 163.755 158.992 1.00 41.08  ? 56   PRO B CD    1 
ATOM   11325 N  N     . GLN B 2  57   ? 153.569 162.339 162.268 1.00 46.25  ? 57   GLN B N     1 
ATOM   11326 C  CA    . GLN B 2  57   ? 152.866 161.770 163.411 1.00 43.50  ? 57   GLN B CA    1 
ATOM   11327 C  C     . GLN B 2  57   ? 152.969 160.252 163.422 1.00 44.91  ? 57   GLN B C     1 
ATOM   11328 O  O     . GLN B 2  57   ? 153.100 159.644 164.490 1.00 46.48  ? 57   GLN B O     1 
ATOM   11329 C  CB    . GLN B 2  57   ? 151.404 162.199 163.392 1.00 43.31  ? 57   GLN B CB    1 
ATOM   11330 C  CG    . GLN B 2  57   ? 151.199 163.682 163.567 1.00 45.38  ? 57   GLN B CG    1 
ATOM   11331 C  CD    . GLN B 2  57   ? 149.737 164.049 163.607 1.00 47.90  ? 57   GLN B CD    1 
ATOM   11332 O  OE1   . GLN B 2  57   ? 148.870 163.182 163.502 1.00 49.52  ? 57   GLN B OE1   1 
ATOM   11333 N  NE2   . GLN B 2  57   ? 149.450 165.338 163.743 1.00 47.64  ? 57   GLN B NE2   1 
ATOM   11334 N  N     . ILE B 2  58   ? 152.899 159.621 162.248 1.00 40.94  ? 58   ILE B N     1 
ATOM   11335 C  CA    . ILE B 2  58   ? 152.962 158.165 162.206 1.00 43.75  ? 58   ILE B CA    1 
ATOM   11336 C  C     . ILE B 2  58   ? 154.372 157.658 162.476 1.00 45.91  ? 58   ILE B C     1 
ATOM   11337 O  O     . ILE B 2  58   ? 154.546 156.535 162.958 1.00 46.85  ? 58   ILE B O     1 
ATOM   11338 C  CB    . ILE B 2  58   ? 152.410 157.623 160.874 1.00 44.74  ? 58   ILE B CB    1 
ATOM   11339 C  CG1   . ILE B 2  58   ? 151.942 156.181 161.061 1.00 44.88  ? 58   ILE B CG1   1 
ATOM   11340 C  CG2   . ILE B 2  58   ? 153.452 157.689 159.776 1.00 44.21  ? 58   ILE B CG2   1 
ATOM   11341 C  CD1   . ILE B 2  58   ? 150.507 156.046 161.438 1.00 45.96  ? 58   ILE B CD1   1 
ATOM   11342 N  N     . VAL B 2  59   ? 155.398 158.453 162.178 1.00 46.74  ? 59   VAL B N     1 
ATOM   11343 C  CA    . VAL B 2  59   ? 156.761 158.007 162.455 1.00 46.65  ? 59   VAL B CA    1 
ATOM   11344 C  C     . VAL B 2  59   ? 157.094 158.199 163.928 1.00 46.04  ? 59   VAL B C     1 
ATOM   11345 O  O     . VAL B 2  59   ? 157.672 157.317 164.574 1.00 48.19  ? 59   VAL B O     1 
ATOM   11346 C  CB    . VAL B 2  59   ? 157.768 158.736 161.549 1.00 44.79  ? 59   VAL B CB    1 
ATOM   11347 C  CG1   . VAL B 2  59   ? 159.168 158.591 162.102 1.00 44.43  ? 59   VAL B CG1   1 
ATOM   11348 C  CG2   . VAL B 2  59   ? 157.705 158.173 160.141 1.00 43.56  ? 59   VAL B CG2   1 
ATOM   11349 N  N     . LYS B 2  60   ? 156.715 159.346 164.487 1.00 45.48  ? 60   LYS B N     1 
ATOM   11350 C  CA    . LYS B 2  60   ? 157.145 159.687 165.836 1.00 47.01  ? 60   LYS B CA    1 
ATOM   11351 C  C     . LYS B 2  60   ? 156.328 158.949 166.893 1.00 47.68  ? 60   LYS B C     1 
ATOM   11352 O  O     . LYS B 2  60   ? 156.886 158.309 167.790 1.00 47.96  ? 60   LYS B O     1 
ATOM   11353 C  CB    . LYS B 2  60   ? 157.033 161.196 166.048 1.00 46.42  ? 60   LYS B CB    1 
ATOM   11354 C  CG    . LYS B 2  60   ? 157.864 162.049 165.125 1.00 46.76  ? 60   LYS B CG    1 
ATOM   11355 C  CD    . LYS B 2  60   ? 157.493 163.508 165.327 1.00 47.16  ? 60   LYS B CD    1 
ATOM   11356 C  CE    . LYS B 2  60   ? 158.112 164.402 164.276 1.00 47.63  ? 60   LYS B CE    1 
ATOM   11357 N  NZ    . LYS B 2  60   ? 157.702 165.815 164.470 1.00 46.77  ? 60   LYS B NZ    1 
ATOM   11358 N  N     . GLN B 2  61   ? 155.002 159.037 166.808 1.00 49.28  ? 61   GLN B N     1 
ATOM   11359 C  CA    . GLN B 2  61   ? 154.129 158.667 167.912 1.00 48.53  ? 61   GLN B CA    1 
ATOM   11360 C  C     . GLN B 2  61   ? 153.505 157.287 167.760 1.00 47.61  ? 61   GLN B C     1 
ATOM   11361 O  O     . GLN B 2  61   ? 152.487 157.013 168.402 1.00 48.06  ? 61   GLN B O     1 
ATOM   11362 C  CB    . GLN B 2  61   ? 153.029 159.717 168.084 1.00 45.76  ? 61   GLN B CB    1 
ATOM   11363 C  CG    . GLN B 2  61   ? 153.513 160.957 168.790 1.00 45.53  ? 61   GLN B CG    1 
ATOM   11364 C  CD    . GLN B 2  61   ? 154.266 161.866 167.857 1.00 46.69  ? 61   GLN B CD    1 
ATOM   11365 O  OE1   . GLN B 2  61   ? 154.144 161.745 166.645 1.00 49.54  ? 61   GLN B OE1   1 
ATOM   11366 N  NE2   . GLN B 2  61   ? 155.073 162.758 168.410 1.00 47.01  ? 61   GLN B NE2   1 
ATOM   11367 N  N     . MET B 2  62   ? 154.074 156.417 166.931 1.00 50.07  ? 62   MET B N     1 
ATOM   11368 C  CA    . MET B 2  62   ? 153.493 155.097 166.724 1.00 52.68  ? 62   MET B CA    1 
ATOM   11369 C  C     . MET B 2  62   ? 154.444 153.944 166.994 1.00 54.01  ? 62   MET B C     1 
ATOM   11370 O  O     . MET B 2  62   ? 153.966 152.826 167.217 1.00 55.68  ? 62   MET B O     1 
ATOM   11371 C  CB    . MET B 2  62   ? 152.969 154.956 165.287 1.00 53.38  ? 62   MET B CB    1 
ATOM   11372 C  CG    . MET B 2  62   ? 151.996 156.032 164.856 1.00 54.16  ? 62   MET B CG    1 
ATOM   11373 S  SD    . MET B 2  62   ? 150.609 156.352 165.954 1.00 63.30  ? 62   MET B SD    1 
ATOM   11374 C  CE    . MET B 2  62   ? 149.918 157.780 165.124 1.00 51.44  ? 62   MET B CE    1 
ATOM   11375 N  N     . PHE B 2  63   ? 155.756 154.161 166.984 1.00 55.69  ? 63   PHE B N     1 
ATOM   11376 C  CA    . PHE B 2  63   ? 156.735 153.077 167.032 1.00 56.41  ? 63   PHE B CA    1 
ATOM   11377 C  C     . PHE B 2  63   ? 157.772 153.311 168.125 1.00 57.86  ? 63   PHE B C     1 
ATOM   11378 O  O     . PHE B 2  63   ? 158.970 153.103 167.926 1.00 56.60  ? 63   PHE B O     1 
ATOM   11379 C  CB    . PHE B 2  63   ? 157.438 152.911 165.686 1.00 55.50  ? 63   PHE B CB    1 
ATOM   11380 C  CG    . PHE B 2  63   ? 156.824 151.869 164.793 1.00 56.33  ? 63   PHE B CG    1 
ATOM   11381 C  CD1   . PHE B 2  63   ? 155.679 152.136 164.067 1.00 55.54  ? 63   PHE B CD1   1 
ATOM   11382 C  CD2   . PHE B 2  63   ? 157.411 150.620 164.672 1.00 56.88  ? 63   PHE B CD2   1 
ATOM   11383 C  CE1   . PHE B 2  63   ? 155.130 151.170 163.240 1.00 56.48  ? 63   PHE B CE1   1 
ATOM   11384 C  CE2   . PHE B 2  63   ? 156.868 149.653 163.847 1.00 55.52  ? 63   PHE B CE2   1 
ATOM   11385 C  CZ    . PHE B 2  63   ? 155.729 149.926 163.132 1.00 55.70  ? 63   PHE B CZ    1 
ATOM   11386 N  N     . ASN B 2  64   ? 157.330 153.731 169.310 1.00 50.32  ? 64   ASN B N     1 
ATOM   11387 C  CA    . ASN B 2  64   ? 158.240 153.823 170.454 1.00 49.81  ? 64   ASN B CA    1 
ATOM   11388 C  C     . ASN B 2  64   ? 158.549 152.408 170.918 1.00 50.51  ? 64   ASN B C     1 
ATOM   11389 O  O     . ASN B 2  64   ? 157.858 151.836 171.761 1.00 49.85  ? 64   ASN B O     1 
ATOM   11390 C  CB    . ASN B 2  64   ? 157.652 154.667 171.578 1.00 46.93  ? 64   ASN B CB    1 
ATOM   11391 C  CG    . ASN B 2  64   ? 157.515 156.126 171.206 1.00 47.83  ? 64   ASN B CG    1 
ATOM   11392 O  OD1   . ASN B 2  64   ? 158.413 156.707 170.600 1.00 46.75  ? 64   ASN B OD1   1 
ATOM   11393 N  ND2   . ASN B 2  64   ? 156.403 156.736 171.593 1.00 47.03  ? 64   ASN B ND2   1 
ATOM   11394 N  N     . VAL B 2  65   ? 159.599 151.832 170.347 1.00 53.27  ? 65   VAL B N     1 
ATOM   11395 C  CA    . VAL B 2  65   ? 160.016 150.478 170.692 1.00 53.59  ? 65   VAL B CA    1 
ATOM   11396 C  C     . VAL B 2  65   ? 160.543 150.464 172.118 1.00 55.05  ? 65   VAL B C     1 
ATOM   11397 O  O     . VAL B 2  65   ? 161.324 151.336 172.520 1.00 51.69  ? 65   VAL B O     1 
ATOM   11398 C  CB    . VAL B 2  65   ? 161.077 149.966 169.700 1.00 52.84  ? 65   VAL B CB    1 
ATOM   11399 C  CG1   . VAL B 2  65   ? 161.544 148.577 170.096 1.00 51.47  ? 65   VAL B CG1   1 
ATOM   11400 C  CG2   . VAL B 2  65   ? 160.524 149.952 168.284 1.00 50.18  ? 65   VAL B CG2   1 
ATOM   11401 N  N     . ASP B 2  66   ? 160.093 149.482 172.897 1.00 54.46  ? 66   ASP B N     1 
ATOM   11402 C  CA    . ASP B 2  66   ? 160.616 149.263 174.244 1.00 53.23  ? 66   ASP B CA    1 
ATOM   11403 C  C     . ASP B 2  66   ? 160.521 147.772 174.519 1.00 51.68  ? 66   ASP B C     1 
ATOM   11404 O  O     . ASP B 2  66   ? 159.458 147.277 174.906 1.00 49.33  ? 66   ASP B O     1 
ATOM   11405 C  CB    . ASP B 2  66   ? 159.847 150.068 175.288 1.00 53.98  ? 66   ASP B CB    1 
ATOM   11406 C  CG    . ASP B 2  66   ? 160.423 149.909 176.682 1.00 55.63  ? 66   ASP B CG    1 
ATOM   11407 O  OD1   . ASP B 2  66   ? 161.486 150.501 176.954 1.00 54.91  ? 66   ASP B OD1   1 
ATOM   11408 O  OD2   . ASP B 2  66   ? 159.817 149.192 177.502 1.00 54.29  ? 66   ASP B OD2   1 
ATOM   11409 N  N     . ILE B 2  67   ? 161.627 147.064 174.315 1.00 50.58  ? 67   ILE B N     1 
ATOM   11410 C  CA    . ILE B 2  67   ? 161.646 145.612 174.419 1.00 49.47  ? 67   ILE B CA    1 
ATOM   11411 C  C     . ILE B 2  67   ? 162.862 145.200 175.241 1.00 50.75  ? 67   ILE B C     1 
ATOM   11412 O  O     . ILE B 2  67   ? 163.823 145.966 175.372 1.00 50.05  ? 67   ILE B O     1 
ATOM   11413 C  CB    . ILE B 2  67   ? 161.649 144.973 173.017 1.00 48.03  ? 67   ILE B CB    1 
ATOM   11414 C  CG1   . ILE B 2  67   ? 160.990 143.592 173.044 1.00 50.13  ? 67   ILE B CG1   1 
ATOM   11415 C  CG2   . ILE B 2  67   ? 163.061 144.904 172.466 1.00 46.93  ? 67   ILE B CG2   1 
ATOM   11416 C  CD1   . ILE B 2  67   ? 160.760 142.994 171.670 1.00 45.98  ? 67   ILE B CD1   1 
ATOM   11417 N  N     . THR B 2  68   ? 162.826 143.997 175.813 1.00 53.27  ? 68   THR B N     1 
ATOM   11418 C  CA    . THR B 2  68   ? 163.897 143.514 176.672 1.00 53.19  ? 68   THR B CA    1 
ATOM   11419 C  C     . THR B 2  68   ? 164.379 142.166 176.159 1.00 54.29  ? 68   THR B C     1 
ATOM   11420 O  O     . THR B 2  68   ? 163.571 141.265 175.917 1.00 54.93  ? 68   THR B O     1 
ATOM   11421 C  CB    . THR B 2  68   ? 163.436 143.376 178.131 1.00 52.57  ? 68   THR B CB    1 
ATOM   11422 O  OG1   . THR B 2  68   ? 162.878 144.617 178.576 1.00 54.13  ? 68   THR B OG1   1 
ATOM   11423 C  CG2   . THR B 2  68   ? 164.608 143.020 179.028 1.00 49.87  ? 68   THR B CG2   1 
ATOM   11424 N  N     . TYR B 2  69   ? 165.694 142.028 175.999 1.00 55.45  ? 69   TYR B N     1 
ATOM   11425 C  CA    . TYR B 2  69   ? 166.278 140.812 175.454 1.00 55.45  ? 69   TYR B CA    1 
ATOM   11426 C  C     . TYR B 2  69   ? 167.336 140.277 176.407 1.00 57.65  ? 69   TYR B C     1 
ATOM   11427 O  O     . TYR B 2  69   ? 168.217 141.018 176.852 1.00 55.57  ? 69   TYR B O     1 
ATOM   11428 C  CB    . TYR B 2  69   ? 166.903 141.058 174.077 1.00 54.57  ? 69   TYR B CB    1 
ATOM   11429 C  CG    . TYR B 2  69   ? 167.485 139.812 173.448 1.00 56.87  ? 69   TYR B CG    1 
ATOM   11430 C  CD1   . TYR B 2  69   ? 166.664 138.751 173.092 1.00 56.01  ? 69   TYR B CD1   1 
ATOM   11431 C  CD2   . TYR B 2  69   ? 168.849 139.683 173.228 1.00 56.75  ? 69   TYR B CD2   1 
ATOM   11432 C  CE1   . TYR B 2  69   ? 167.179 137.605 172.517 1.00 55.62  ? 69   TYR B CE1   1 
ATOM   11433 C  CE2   . TYR B 2  69   ? 169.375 138.533 172.656 1.00 56.59  ? 69   TYR B CE2   1 
ATOM   11434 C  CZ    . TYR B 2  69   ? 168.531 137.498 172.303 1.00 56.98  ? 69   TYR B CZ    1 
ATOM   11435 O  OH    . TYR B 2  69   ? 169.034 136.351 171.733 1.00 57.51  ? 69   TYR B OH    1 
ATOM   11436 N  N     . LYS B 2  70   ? 167.247 138.982 176.705 1.00 57.82  ? 70   LYS B N     1 
ATOM   11437 C  CA    . LYS B 2  70   ? 168.237 138.332 177.552 1.00 56.37  ? 70   LYS B CA    1 
ATOM   11438 C  C     . LYS B 2  70   ? 169.554 138.181 176.799 1.00 56.99  ? 70   LYS B C     1 
ATOM   11439 O  O     . LYS B 2  70   ? 169.579 137.718 175.654 1.00 55.19  ? 70   LYS B O     1 
ATOM   11440 C  CB    . LYS B 2  70   ? 167.722 136.968 178.005 1.00 55.72  ? 70   LYS B CB    1 
ATOM   11441 C  CG    . LYS B 2  70   ? 168.721 136.140 178.798 1.00 57.41  ? 70   LYS B CG    1 
ATOM   11442 C  CD    . LYS B 2  70   ? 168.141 134.771 179.139 1.00 58.13  ? 70   LYS B CD    1 
ATOM   11443 C  CE    . LYS B 2  70   ? 169.142 133.907 179.888 1.00 56.92  ? 70   LYS B CE    1 
ATOM   11444 N  NZ    . LYS B 2  70   ? 168.573 132.577 180.238 1.00 56.21  ? 70   LYS B NZ    1 
ATOM   11445 N  N     . ASP B 2  71   ? 170.648 138.570 177.441 1.00 54.59  ? 71   ASP B N     1 
ATOM   11446 C  CA    . ASP B 2  71   ? 171.969 138.481 176.841 1.00 56.95  ? 71   ASP B CA    1 
ATOM   11447 C  C     . ASP B 2  71   ? 172.606 137.136 177.169 1.00 57.51  ? 71   ASP B C     1 
ATOM   11448 O  O     . ASP B 2  71   ? 172.421 136.590 178.260 1.00 58.62  ? 71   ASP B O     1 
ATOM   11449 C  CB    . ASP B 2  71   ? 172.869 139.614 177.332 1.00 55.19  ? 71   ASP B CB    1 
ATOM   11450 C  CG    . ASP B 2  71   ? 174.031 139.877 176.399 1.00 55.59  ? 71   ASP B CG    1 
ATOM   11451 O  OD1   . ASP B 2  71   ? 174.223 139.089 175.447 1.00 54.03  ? 71   ASP B OD1   1 
ATOM   11452 O  OD2   . ASP B 2  71   ? 174.763 140.862 176.632 1.00 54.34  ? 71   ASP B OD2   1 
ATOM   11453 N  N     . GLN B 2  72   ? 173.377 136.615 176.217 1.00 54.28  ? 72   GLN B N     1 
ATOM   11454 C  CA    . GLN B 2  72   ? 173.945 135.274 176.320 1.00 54.62  ? 72   GLN B CA    1 
ATOM   11455 C  C     . GLN B 2  72   ? 175.455 135.312 176.097 1.00 57.69  ? 72   GLN B C     1 
ATOM   11456 O  O     . GLN B 2  72   ? 176.030 134.467 175.410 1.00 57.08  ? 72   GLN B O     1 
ATOM   11457 C  CB    . GLN B 2  72   ? 173.261 134.332 175.331 1.00 54.43  ? 72   GLN B CB    1 
ATOM   11458 C  CG    . GLN B 2  72   ? 171.884 133.853 175.775 1.00 55.54  ? 72   GLN B CG    1 
ATOM   11459 C  CD    . GLN B 2  72   ? 171.077 133.255 174.636 1.00 57.44  ? 72   GLN B CD    1 
ATOM   11460 O  OE1   . GLN B 2  72   ? 171.469 133.338 173.472 1.00 57.60  ? 72   GLN B OE1   1 
ATOM   11461 N  NE2   . GLN B 2  72   ? 169.946 132.643 174.967 1.00 54.36  ? 72   GLN B NE2   1 
ATOM   11462 N  N     . ARG B 2  73   ? 176.119 136.297 176.695 1.00 58.86  ? 73   ARG B N     1 
ATOM   11463 C  CA    . ARG B 2  73   ? 177.569 136.416 176.625 1.00 58.34  ? 73   ARG B CA    1 
ATOM   11464 C  C     . ARG B 2  73   ? 178.158 135.893 177.930 1.00 58.38  ? 73   ARG B C     1 
ATOM   11465 O  O     . ARG B 2  73   ? 177.880 136.439 179.003 1.00 59.25  ? 73   ARG B O     1 
ATOM   11466 C  CB    . ARG B 2  73   ? 177.994 137.866 176.382 1.00 58.30  ? 73   ARG B CB    1 
ATOM   11467 C  CG    . ARG B 2  73   ? 179.484 138.033 176.079 1.00 59.17  ? 73   ARG B CG    1 
ATOM   11468 C  CD    . ARG B 2  73   ? 179.809 137.610 174.651 1.00 59.02  ? 73   ARG B CD    1 
ATOM   11469 N  NE    . ARG B 2  73   ? 179.992 136.169 174.522 1.00 61.43  ? 73   ARG B NE    1 
ATOM   11470 C  CZ    . ARG B 2  73   ? 180.012 135.524 173.364 1.00 59.71  ? 73   ARG B CZ    1 
ATOM   11471 N  NH1   . ARG B 2  73   ? 179.916 136.168 172.215 1.00 57.59  ? 73   ARG B NH1   1 
ATOM   11472 N  NH2   . ARG B 2  73   ? 180.121 134.199 173.359 1.00 58.41  ? 73   ARG B NH2   1 
ATOM   11473 N  N     . ASP B 2  74   ? 178.977 134.850 177.836 1.00 53.13  ? 74   ASP B N     1 
ATOM   11474 C  CA    . ASP B 2  74   ? 179.478 134.148 179.015 1.00 55.13  ? 74   ASP B CA    1 
ATOM   11475 C  C     . ASP B 2  74   ? 180.992 133.982 178.923 1.00 54.52  ? 74   ASP B C     1 
ATOM   11476 O  O     . ASP B 2  74   ? 181.526 132.873 178.941 1.00 52.88  ? 74   ASP B O     1 
ATOM   11477 C  CB    . ASP B 2  74   ? 178.776 132.800 179.193 1.00 53.04  ? 74   ASP B CB    1 
ATOM   11478 C  CG    . ASP B 2  74   ? 178.563 132.070 177.880 1.00 54.66  ? 74   ASP B CG    1 
ATOM   11479 O  OD1   . ASP B 2  74   ? 178.774 132.681 176.811 1.00 54.80  ? 74   ASP B OD1   1 
ATOM   11480 O  OD2   . ASP B 2  74   ? 178.193 130.880 177.917 1.00 52.28  ? 74   ASP B OD2   1 
ATOM   11481 N  N     . HIS B 2  75   ? 181.703 135.102 178.801 1.00 58.63  ? 75   HIS B N     1 
ATOM   11482 C  CA    . HIS B 2  75   ? 183.159 135.089 178.718 1.00 57.89  ? 75   HIS B CA    1 
ATOM   11483 C  C     . HIS B 2  75   ? 183.833 135.598 179.988 1.00 57.78  ? 75   HIS B C     1 
ATOM   11484 O  O     . HIS B 2  75   ? 184.728 134.936 180.522 1.00 57.57  ? 75   HIS B O     1 
ATOM   11485 C  CB    . HIS B 2  75   ? 183.616 135.905 177.506 1.00 56.82  ? 75   HIS B CB    1 
ATOM   11486 C  CG    . HIS B 2  75   ? 183.710 135.098 176.250 1.00 60.23  ? 75   HIS B CG    1 
ATOM   11487 N  ND1   . HIS B 2  75   ? 184.663 134.120 176.064 1.00 59.29  ? 75   HIS B ND1   1 
ATOM   11488 C  CD2   . HIS B 2  75   ? 182.955 135.106 175.125 1.00 58.64  ? 75   HIS B CD2   1 
ATOM   11489 C  CE1   . HIS B 2  75   ? 184.499 133.569 174.875 1.00 57.96  ? 75   HIS B CE1   1 
ATOM   11490 N  NE2   . HIS B 2  75   ? 183.469 134.149 174.285 1.00 58.73  ? 75   HIS B NE2   1 
ATOM   11491 N  N     . THR B 2  76   ? 183.427 136.758 180.486 1.00 53.21  ? 76   THR B N     1 
ATOM   11492 C  CA    . THR B 2  76   ? 184.040 137.345 181.667 1.00 54.57  ? 76   THR B CA    1 
ATOM   11493 C  C     . THR B 2  76   ? 183.108 137.228 182.874 1.00 53.69  ? 76   THR B C     1 
ATOM   11494 O  O     . THR B 2  76   ? 181.906 136.988 182.746 1.00 51.76  ? 76   THR B O     1 
ATOM   11495 C  CB    . THR B 2  76   ? 184.406 138.809 181.404 1.00 52.88  ? 76   THR B CB    1 
ATOM   11496 O  OG1   . THR B 2  76   ? 183.224 139.556 181.104 1.00 50.08  ? 76   THR B OG1   1 
ATOM   11497 C  CG2   . THR B 2  76   ? 185.343 138.901 180.216 1.00 50.20  ? 76   THR B CG2   1 
ATOM   11498 N  N     . GLU B 2  77   ? 183.691 137.395 184.066 1.00 52.54  ? 77   GLU B N     1 
ATOM   11499 C  CA    . GLU B 2  77   ? 182.892 137.360 185.288 1.00 54.09  ? 77   GLU B CA    1 
ATOM   11500 C  C     . GLU B 2  77   ? 181.880 138.496 185.315 1.00 53.14  ? 77   GLU B C     1 
ATOM   11501 O  O     . GLU B 2  77   ? 180.768 138.336 185.831 1.00 51.67  ? 77   GLU B O     1 
ATOM   11502 C  CB    . GLU B 2  77   ? 183.795 137.418 186.523 1.00 53.77  ? 77   GLU B CB    1 
ATOM   11503 C  CG    . GLU B 2  77   ? 184.846 136.322 186.590 1.00 52.99  ? 77   GLU B CG    1 
ATOM   11504 C  CD    . GLU B 2  77   ? 185.686 136.394 187.853 1.00 53.99  ? 77   GLU B CD    1 
ATOM   11505 O  OE1   . GLU B 2  77   ? 185.552 137.380 188.608 1.00 52.84  ? 77   GLU B OE1   1 
ATOM   11506 O  OE2   . GLU B 2  77   ? 186.467 135.453 188.101 1.00 53.16  ? 77   GLU B OE2   1 
ATOM   11507 N  N     . ILE B 2  78   ? 182.254 139.659 184.777 1.00 51.29  ? 78   ILE B N     1 
ATOM   11508 C  CA    . ILE B 2  78   ? 181.300 140.753 184.647 1.00 52.51  ? 78   ILE B CA    1 
ATOM   11509 C  C     . ILE B 2  78   ? 180.158 140.350 183.729 1.00 53.28  ? 78   ILE B C     1 
ATOM   11510 O  O     . ILE B 2  78   ? 178.997 140.703 183.975 1.00 51.55  ? 78   ILE B O     1 
ATOM   11511 C  CB    . ILE B 2  78   ? 182.014 142.024 184.147 1.00 52.73  ? 78   ILE B CB    1 
ATOM   11512 C  CG1   . ILE B 2  78   ? 183.386 142.155 184.813 1.00 53.32  ? 78   ILE B CG1   1 
ATOM   11513 C  CG2   . ILE B 2  78   ? 181.172 143.258 184.432 1.00 49.43  ? 78   ILE B CG2   1 
ATOM   11514 C  CD1   . ILE B 2  78   ? 184.318 143.125 184.119 1.00 51.49  ? 78   ILE B CD1   1 
ATOM   11515 N  N     . ASP B 2  79   ? 180.457 139.590 182.671 1.00 53.78  ? 79   ASP B N     1 
ATOM   11516 C  CA    . ASP B 2  79   ? 179.408 139.130 181.768 1.00 54.86  ? 79   ASP B CA    1 
ATOM   11517 C  C     . ASP B 2  79   ? 178.448 138.168 182.459 1.00 55.79  ? 79   ASP B C     1 
ATOM   11518 O  O     . ASP B 2  79   ? 177.325 137.967 181.981 1.00 55.36  ? 79   ASP B O     1 
ATOM   11519 C  CB    . ASP B 2  79   ? 180.026 138.480 180.527 1.00 54.01  ? 79   ASP B CB    1 
ATOM   11520 C  CG    . ASP B 2  79   ? 180.660 139.498 179.586 1.00 56.71  ? 79   ASP B CG    1 
ATOM   11521 O  OD1   . ASP B 2  79   ? 180.255 140.679 179.618 1.00 54.53  ? 79   ASP B OD1   1 
ATOM   11522 O  OD2   . ASP B 2  79   ? 181.560 139.118 178.807 1.00 56.45  ? 79   ASP B OD2   1 
ATOM   11523 N  N     . LYS B 2  80   ? 178.866 137.561 183.571 1.00 56.27  ? 80   LYS B N     1 
ATOM   11524 C  CA    . LYS B 2  80   ? 177.997 136.693 184.356 1.00 55.91  ? 80   LYS B CA    1 
ATOM   11525 C  C     . LYS B 2  80   ? 177.123 137.456 185.344 1.00 55.33  ? 80   LYS B C     1 
ATOM   11526 O  O     . LYS B 2  80   ? 176.163 136.880 185.868 1.00 54.80  ? 80   LYS B O     1 
ATOM   11527 C  CB    . LYS B 2  80   ? 178.830 135.657 185.114 1.00 54.40  ? 80   LYS B CB    1 
ATOM   11528 C  CG    . LYS B 2  80   ? 179.580 134.682 184.227 1.00 54.39  ? 80   LYS B CG    1 
ATOM   11529 C  CD    . LYS B 2  80   ? 180.483 133.779 185.056 1.00 54.32  ? 80   LYS B CD    1 
ATOM   11530 C  CE    . LYS B 2  80   ? 181.191 132.751 184.190 1.00 54.25  ? 80   LYS B CE    1 
ATOM   11531 N  NZ    . LYS B 2  80   ? 182.134 133.402 183.238 1.00 54.53  ? 80   LYS B NZ    1 
ATOM   11532 N  N     . LEU B 2  81   ? 177.417 138.730 185.598 1.00 55.04  ? 81   LEU B N     1 
ATOM   11533 C  CA    . LEU B 2  81   ? 176.668 139.540 186.551 1.00 56.28  ? 81   LEU B CA    1 
ATOM   11534 C  C     . LEU B 2  81   ? 175.474 140.233 185.912 1.00 57.42  ? 81   LEU B C     1 
ATOM   11535 O  O     . LEU B 2  81   ? 174.823 141.053 186.567 1.00 55.29  ? 81   LEU B O     1 
ATOM   11536 C  CB    . LEU B 2  81   ? 177.588 140.584 187.190 1.00 55.19  ? 81   LEU B CB    1 
ATOM   11537 C  CG    . LEU B 2  81   ? 178.122 140.266 188.589 1.00 57.74  ? 81   LEU B CG    1 
ATOM   11538 C  CD1   . LEU B 2  81   ? 179.047 139.055 188.546 1.00 53.82  ? 81   LEU B CD1   1 
ATOM   11539 C  CD2   . LEU B 2  81   ? 178.836 141.474 189.190 1.00 53.04  ? 81   LEU B CD2   1 
ATOM   11540 N  N     . ARG B 2  82   ? 175.176 139.909 184.659 1.00 60.45  ? 82   ARG B N     1 
ATOM   11541 C  CA    . ARG B 2  82   ? 174.154 140.559 183.858 1.00 60.97  ? 82   ARG B CA    1 
ATOM   11542 C  C     . ARG B 2  82   ? 172.991 139.605 183.612 1.00 60.58  ? 82   ARG B C     1 
ATOM   11543 O  O     . ARG B 2  82   ? 173.154 138.382 183.651 1.00 59.19  ? 82   ARG B O     1 
ATOM   11544 C  CB    . ARG B 2  82   ? 174.752 141.010 182.527 1.00 57.91  ? 82   ARG B CB    1 
ATOM   11545 C  CG    . ARG B 2  82   ? 173.896 141.920 181.686 1.00 59.41  ? 82   ARG B CG    1 
ATOM   11546 C  CD    . ARG B 2  82   ? 174.614 142.209 180.385 1.00 60.82  ? 82   ARG B CD    1 
ATOM   11547 N  NE    . ARG B 2  82   ? 174.865 140.982 179.635 1.00 61.94  ? 82   ARG B NE    1 
ATOM   11548 C  CZ    . ARG B 2  82   ? 176.036 140.361 179.576 1.00 60.83  ? 82   ARG B CZ    1 
ATOM   11549 N  NH1   . ARG B 2  82   ? 177.098 140.828 180.209 1.00 59.52  ? 82   ARG B NH1   1 
ATOM   11550 N  NH2   . ARG B 2  82   ? 176.144 139.246 178.860 1.00 59.22  ? 82   ARG B NH2   1 
ATOM   11551 N  N     . GLU B 2  83   ? 171.810 140.173 183.362 1.00 58.25  ? 83   GLU B N     1 
ATOM   11552 C  CA    . GLU B 2  83   ? 170.611 139.387 183.096 1.00 58.92  ? 83   GLU B CA    1 
ATOM   11553 C  C     . GLU B 2  83   ? 170.078 139.590 181.683 1.00 59.69  ? 83   GLU B C     1 
ATOM   11554 O  O     . GLU B 2  83   ? 169.929 138.620 180.934 1.00 58.59  ? 83   GLU B O     1 
ATOM   11555 C  CB    . GLU B 2  83   ? 169.525 139.720 184.130 1.00 56.30  ? 83   GLU B CB    1 
ATOM   11556 C  CG    . GLU B 2  83   ? 169.717 139.033 185.476 1.00 57.09  ? 83   GLU B CG    1 
ATOM   11557 C  CD    . GLU B 2  83   ? 168.612 139.356 186.468 1.00 59.55  ? 83   GLU B CD    1 
ATOM   11558 O  OE1   . GLU B 2  83   ? 167.774 140.232 186.170 1.00 56.95  ? 83   GLU B OE1   1 
ATOM   11559 O  OE2   . GLU B 2  83   ? 168.589 138.742 187.555 1.00 59.12  ? 83   GLU B OE2   1 
ATOM   11560 N  N     . SER B 2  84   ? 169.781 140.826 181.293 1.00 53.70  ? 84   SER B N     1 
ATOM   11561 C  CA    . SER B 2  84   ? 169.134 141.083 180.014 1.00 54.09  ? 84   SER B CA    1 
ATOM   11562 C  C     . SER B 2  84   ? 169.348 142.544 179.636 1.00 56.28  ? 84   SER B C     1 
ATOM   11563 O  O     . SER B 2  84   ? 169.822 143.355 180.437 1.00 56.81  ? 84   SER B O     1 
ATOM   11564 C  CB    . SER B 2  84   ? 167.642 140.740 180.074 1.00 52.40  ? 84   SER B CB    1 
ATOM   11565 O  OG    . SER B 2  84   ? 166.964 141.566 181.002 1.00 52.54  ? 84   SER B OG    1 
ATOM   11566 N  N     . VAL B 2  85   ? 168.971 142.875 178.403 1.00 52.12  ? 85   VAL B N     1 
ATOM   11567 C  CA    . VAL B 2  85   ? 169.110 144.219 177.858 1.00 51.62  ? 85   VAL B CA    1 
ATOM   11568 C  C     . VAL B 2  85   ? 167.716 144.770 177.608 1.00 52.49  ? 85   VAL B C     1 
ATOM   11569 O  O     . VAL B 2  85   ? 166.914 144.136 176.916 1.00 53.45  ? 85   VAL B O     1 
ATOM   11570 C  CB    . VAL B 2  85   ? 169.928 144.223 176.553 1.00 51.51  ? 85   VAL B CB    1 
ATOM   11571 C  CG1   . VAL B 2  85   ? 169.974 145.622 175.961 1.00 51.07  ? 85   VAL B CG1   1 
ATOM   11572 C  CG2   . VAL B 2  85   ? 171.327 143.688 176.796 1.00 51.02  ? 85   VAL B CG2   1 
ATOM   11573 N  N     . GLN B 2  86   ? 167.425 145.940 178.169 1.00 52.00  ? 86   GLN B N     1 
ATOM   11574 C  CA    . GLN B 2  86   ? 166.146 146.604 177.941 1.00 52.13  ? 86   GLN B CA    1 
ATOM   11575 C  C     . GLN B 2  86   ? 166.351 147.666 176.865 1.00 52.94  ? 86   GLN B C     1 
ATOM   11576 O  O     . GLN B 2  86   ? 166.963 148.709 177.116 1.00 51.46  ? 86   GLN B O     1 
ATOM   11577 C  CB    . GLN B 2  86   ? 165.601 147.214 179.229 1.00 51.16  ? 86   GLN B CB    1 
ATOM   11578 C  CG    . GLN B 2  86   ? 164.105 147.501 179.172 1.00 53.40  ? 86   GLN B CG    1 
ATOM   11579 C  CD    . GLN B 2  86   ? 163.552 148.047 180.475 1.00 53.52  ? 86   GLN B CD    1 
ATOM   11580 O  OE1   . GLN B 2  86   ? 164.303 148.380 181.392 1.00 52.98  ? 86   GLN B OE1   1 
ATOM   11581 N  NE2   . GLN B 2  86   ? 162.230 148.144 180.561 1.00 49.74  ? 86   GLN B NE2   1 
ATOM   11582 N  N     . ILE B 2  87   ? 165.831 147.401 175.672 1.00 53.98  ? 87   ILE B N     1 
ATOM   11583 C  CA    . ILE B 2  87   ? 166.086 148.246 174.512 1.00 54.55  ? 87   ILE B CA    1 
ATOM   11584 C  C     . ILE B 2  87   ? 164.966 149.272 174.381 1.00 57.06  ? 87   ILE B C     1 
ATOM   11585 O  O     . ILE B 2  87   ? 163.780 148.929 174.445 1.00 53.43  ? 87   ILE B O     1 
ATOM   11586 C  CB    . ILE B 2  87   ? 166.225 147.384 173.246 1.00 53.21  ? 87   ILE B CB    1 
ATOM   11587 C  CG1   . ILE B 2  87   ? 167.503 146.537 173.331 1.00 49.89  ? 87   ILE B CG1   1 
ATOM   11588 C  CG2   . ILE B 2  87   ? 166.203 148.241 171.990 1.00 52.95  ? 87   ILE B CG2   1 
ATOM   11589 C  CD1   . ILE B 2  87   ? 167.486 145.280 172.483 1.00 49.62  ? 87   ILE B CD1   1 
ATOM   11590 N  N     . GLN B 2  88   ? 165.345 150.539 174.209 1.00 54.04  ? 88   GLN B N     1 
ATOM   11591 C  CA    . GLN B 2  88   ? 164.396 151.639 174.078 1.00 55.25  ? 88   GLN B CA    1 
ATOM   11592 C  C     . GLN B 2  88   ? 164.953 152.677 173.112 1.00 56.85  ? 88   GLN B C     1 
ATOM   11593 O  O     . GLN B 2  88   ? 166.108 153.086 173.251 1.00 54.32  ? 88   GLN B O     1 
ATOM   11594 C  CB    . GLN B 2  88   ? 164.126 152.295 175.432 1.00 52.39  ? 88   GLN B CB    1 
ATOM   11595 C  CG    . GLN B 2  88   ? 163.283 153.548 175.342 1.00 53.58  ? 88   GLN B CG    1 
ATOM   11596 C  CD    . GLN B 2  88   ? 162.935 154.117 176.696 1.00 52.98  ? 88   GLN B CD    1 
ATOM   11597 O  OE1   . GLN B 2  88   ? 163.256 153.534 177.730 1.00 53.17  ? 88   GLN B OE1   1 
ATOM   11598 N  NE2   . GLN B 2  88   ? 162.278 155.268 176.699 1.00 52.16  ? 88   GLN B NE2   1 
ATOM   11599 N  N     . PHE B 2  89   ? 164.134 153.111 172.151 1.00 57.09  ? 89   PHE B N     1 
ATOM   11600 C  CA    . PHE B 2  89   ? 164.549 154.168 171.236 1.00 56.24  ? 89   PHE B CA    1 
ATOM   11601 C  C     . PHE B 2  89   ? 163.328 154.784 170.567 1.00 56.16  ? 89   PHE B C     1 
ATOM   11602 O  O     . PHE B 2  89   ? 162.267 154.161 170.472 1.00 56.43  ? 89   PHE B O     1 
ATOM   11603 C  CB    . PHE B 2  89   ? 165.552 153.647 170.195 1.00 54.49  ? 89   PHE B CB    1 
ATOM   11604 C  CG    . PHE B 2  89   ? 165.035 152.517 169.350 1.00 55.60  ? 89   PHE B CG    1 
ATOM   11605 C  CD1   . PHE B 2  89   ? 165.125 151.208 169.794 1.00 54.71  ? 89   PHE B CD1   1 
ATOM   11606 C  CD2   . PHE B 2  89   ? 164.498 152.759 168.098 1.00 54.95  ? 89   PHE B CD2   1 
ATOM   11607 C  CE1   . PHE B 2  89   ? 164.668 150.164 169.019 1.00 55.64  ? 89   PHE B CE1   1 
ATOM   11608 C  CE2   . PHE B 2  89   ? 164.039 151.719 167.318 1.00 57.00  ? 89   PHE B CE2   1 
ATOM   11609 C  CZ    . PHE B 2  89   ? 164.125 150.419 167.779 1.00 56.88  ? 89   PHE B CZ    1 
ATOM   11610 N  N     . ASN B 2  90   ? 163.496 156.024 170.102 1.00 49.34  ? 90   ASN B N     1 
ATOM   11611 C  CA    . ASN B 2  90   ? 162.423 156.758 169.443 1.00 51.59  ? 90   ASN B CA    1 
ATOM   11612 C  C     . ASN B 2  90   ? 163.026 157.677 168.385 1.00 51.05  ? 90   ASN B C     1 
ATOM   11613 O  O     . ASN B 2  90   ? 164.233 157.929 168.367 1.00 50.33  ? 90   ASN B O     1 
ATOM   11614 C  CB    . ASN B 2  90   ? 161.574 157.533 170.460 1.00 51.46  ? 90   ASN B CB    1 
ATOM   11615 C  CG    . ASN B 2  90   ? 162.382 158.532 171.267 1.00 51.46  ? 90   ASN B CG    1 
ATOM   11616 O  OD1   . ASN B 2  90   ? 163.584 158.695 171.059 1.00 50.41  ? 90   ASN B OD1   1 
ATOM   11617 N  ND2   . ASN B 2  90   ? 161.724 159.192 172.213 1.00 49.78  ? 90   ASN B ND2   1 
ATOM   11618 N  N     . PHE B 2  91   ? 162.167 158.172 167.493 1.00 52.08  ? 91   PHE B N     1 
ATOM   11619 C  CA    . PHE B 2  91   ? 162.561 158.975 166.342 1.00 49.64  ? 91   PHE B CA    1 
ATOM   11620 C  C     . PHE B 2  91   ? 161.994 160.385 166.453 1.00 49.88  ? 91   PHE B C     1 
ATOM   11621 O  O     . PHE B 2  91   ? 160.822 160.567 166.794 1.00 49.87  ? 91   PHE B O     1 
ATOM   11622 C  CB    . PHE B 2  91   ? 162.092 158.301 165.059 1.00 47.09  ? 91   PHE B CB    1 
ATOM   11623 C  CG    . PHE B 2  91   ? 162.723 156.965 164.828 1.00 48.37  ? 91   PHE B CG    1 
ATOM   11624 C  CD1   . PHE B 2  91   ? 163.974 156.870 164.256 1.00 48.52  ? 91   PHE B CD1   1 
ATOM   11625 C  CD2   . PHE B 2  91   ? 162.101 155.810 165.256 1.00 49.36  ? 91   PHE B CD2   1 
ATOM   11626 C  CE1   . PHE B 2  91   ? 164.568 155.643 164.054 1.00 49.48  ? 91   PHE B CE1   1 
ATOM   11627 C  CE2   . PHE B 2  91   ? 162.692 154.578 165.066 1.00 50.09  ? 91   PHE B CE2   1 
ATOM   11628 C  CZ    . PHE B 2  91   ? 163.929 154.495 164.463 1.00 49.38  ? 91   PHE B CZ    1 
ATOM   11629 N  N     . THR B 2  92   ? 162.832 161.381 166.160 1.00 45.47  ? 92   THR B N     1 
ATOM   11630 C  CA    . THR B 2  92   ? 162.550 162.764 166.537 1.00 47.29  ? 92   THR B CA    1 
ATOM   11631 C  C     . THR B 2  92   ? 162.030 163.620 165.388 1.00 46.85  ? 92   THR B C     1 
ATOM   11632 O  O     . THR B 2  92   ? 160.919 164.149 165.464 1.00 43.83  ? 92   THR B O     1 
ATOM   11633 C  CB    . THR B 2  92   ? 163.805 163.416 167.127 1.00 47.49  ? 92   THR B CB    1 
ATOM   11634 O  OG1   . THR B 2  92   ? 164.338 162.587 168.169 1.00 48.51  ? 92   THR B OG1   1 
ATOM   11635 C  CG2   . THR B 2  92   ? 163.468 164.780 167.689 1.00 44.45  ? 92   THR B CG2   1 
ATOM   11636 N  N     . ASP B 2  93   ? 162.817 163.785 164.328 1.00 48.98  ? 93   ASP B N     1 
ATOM   11637 C  CA    . ASP B 2  93   ? 162.483 164.744 163.282 1.00 50.80  ? 93   ASP B CA    1 
ATOM   11638 C  C     . ASP B 2  93   ? 162.256 164.011 161.973 1.00 50.71  ? 93   ASP B C     1 
ATOM   11639 O  O     . ASP B 2  93   ? 163.024 163.114 161.618 1.00 47.90  ? 93   ASP B O     1 
ATOM   11640 C  CB    . ASP B 2  93   ? 163.585 165.794 163.102 1.00 48.77  ? 93   ASP B CB    1 
ATOM   11641 C  CG    . ASP B 2  93   ? 163.131 166.975 162.261 1.00 50.41  ? 93   ASP B CG    1 
ATOM   11642 O  OD1   . ASP B 2  93   ? 161.946 167.006 161.871 1.00 50.51  ? 93   ASP B OD1   1 
ATOM   11643 O  OD2   . ASP B 2  93   ? 163.955 167.873 161.988 1.00 49.22  ? 93   ASP B OD2   1 
ATOM   11644 N  N     . VAL B 2  94   ? 161.199 164.394 161.263 1.00 45.98  ? 94   VAL B N     1 
ATOM   11645 C  CA    . VAL B 2  94   ? 160.838 163.783 159.994 1.00 46.36  ? 94   VAL B CA    1 
ATOM   11646 C  C     . VAL B 2  94   ? 160.687 164.894 158.967 1.00 46.03  ? 94   VAL B C     1 
ATOM   11647 O  O     . VAL B 2  94   ? 160.025 165.904 159.230 1.00 43.13  ? 94   VAL B O     1 
ATOM   11648 C  CB    . VAL B 2  94   ? 159.542 162.956 160.103 1.00 46.03  ? 94   VAL B CB    1 
ATOM   11649 C  CG1   . VAL B 2  94   ? 159.391 162.041 158.894 1.00 45.47  ? 94   VAL B CG1   1 
ATOM   11650 C  CG2   . VAL B 2  94   ? 159.509 162.165 161.398 1.00 46.91  ? 94   VAL B CG2   1 
ATOM   11651 N  N     . ASN B 2  95   ? 161.315 164.715 157.809 1.00 47.79  ? 95   ASN B N     1 
ATOM   11652 C  CA    . ASN B 2  95   ? 161.166 165.650 156.706 1.00 47.43  ? 95   ASN B CA    1 
ATOM   11653 C  C     . ASN B 2  95   ? 161.232 164.887 155.394 1.00 48.67  ? 95   ASN B C     1 
ATOM   11654 O  O     . ASN B 2  95   ? 161.903 163.859 155.279 1.00 46.13  ? 95   ASN B O     1 
ATOM   11655 C  CB    . ASN B 2  95   ? 162.234 166.748 156.734 1.00 45.85  ? 95   ASN B CB    1 
ATOM   11656 C  CG    . ASN B 2  95   ? 161.769 168.025 156.068 1.00 47.33  ? 95   ASN B CG    1 
ATOM   11657 O  OD1   . ASN B 2  95   ? 160.685 168.076 155.489 1.00 47.00  ? 95   ASN B OD1   1 
ATOM   11658 N  ND2   . ASN B 2  95   ? 162.585 169.065 156.147 1.00 47.43  ? 95   ASN B ND2   1 
ATOM   11659 N  N     . ILE B 2  96   ? 160.514 165.408 154.403 1.00 49.47  ? 96   ILE B N     1 
ATOM   11660 C  CA    . ILE B 2  96   ? 160.488 164.853 153.058 1.00 47.67  ? 96   ILE B CA    1 
ATOM   11661 C  C     . ILE B 2  96   ? 160.771 165.985 152.082 1.00 47.91  ? 96   ILE B C     1 
ATOM   11662 O  O     . ILE B 2  96   ? 160.108 167.027 152.126 1.00 47.03  ? 96   ILE B O     1 
ATOM   11663 C  CB    . ILE B 2  96   ? 159.137 164.181 152.752 1.00 48.63  ? 96   ILE B CB    1 
ATOM   11664 C  CG1   . ILE B 2  96   ? 158.885 163.053 153.754 1.00 47.30  ? 96   ILE B CG1   1 
ATOM   11665 C  CG2   . ILE B 2  96   ? 159.118 163.643 151.334 1.00 46.12  ? 96   ILE B CG2   1 
ATOM   11666 C  CD1   . ILE B 2  96   ? 157.606 162.306 153.544 1.00 47.11  ? 96   ILE B CD1   1 
ATOM   11667 N  N     . GLU B 2  97   ? 161.763 165.790 151.221 1.00 45.56  ? 97   GLU B N     1 
ATOM   11668 C  CA    . GLU B 2  97   ? 162.164 166.786 150.239 1.00 45.73  ? 97   GLU B CA    1 
ATOM   11669 C  C     . GLU B 2  97   ? 161.850 166.294 148.832 1.00 45.74  ? 97   GLU B C     1 
ATOM   11670 O  O     . GLU B 2  97   ? 161.570 165.116 148.602 1.00 46.61  ? 97   GLU B O     1 
ATOM   11671 C  CB    . GLU B 2  97   ? 163.656 167.113 150.370 1.00 44.16  ? 97   GLU B CB    1 
ATOM   11672 C  CG    . GLU B 2  97   ? 164.564 165.897 150.321 1.00 45.35  ? 97   GLU B CG    1 
ATOM   11673 C  CD    . GLU B 2  97   ? 165.975 166.198 150.778 1.00 48.74  ? 97   GLU B CD    1 
ATOM   11674 O  OE1   . GLU B 2  97   ? 166.243 167.351 151.176 1.00 47.65  ? 97   GLU B OE1   1 
ATOM   11675 O  OE2   . GLU B 2  97   ? 166.822 165.285 150.730 1.00 48.16  ? 97   GLU B OE2   1 
ATOM   11676 N  N     . ARG B 2  98   ? 161.928 167.221 147.881 1.00 45.52  ? 98   ARG B N     1 
ATOM   11677 C  CA    . ARG B 2  98   ? 161.507 166.960 146.515 1.00 47.57  ? 98   ARG B CA    1 
ATOM   11678 C  C     . ARG B 2  98   ? 162.421 165.932 145.853 1.00 48.81  ? 98   ARG B C     1 
ATOM   11679 O  O     . ARG B 2  98   ? 163.578 165.778 146.243 1.00 49.21  ? 98   ARG B O     1 
ATOM   11680 C  CB    . ARG B 2  98   ? 161.502 168.265 145.728 1.00 44.80  ? 98   ARG B CB    1 
ATOM   11681 C  CG    . ARG B 2  98   ? 160.437 169.225 146.200 1.00 45.07  ? 98   ARG B CG    1 
ATOM   11682 C  CD    . ARG B 2  98   ? 160.397 170.492 145.377 1.00 44.19  ? 98   ARG B CD    1 
ATOM   11683 N  NE    . ARG B 2  98   ? 159.088 171.130 145.446 1.00 46.88  ? 98   ARG B NE    1 
ATOM   11684 C  CZ    . ARG B 2  98   ? 158.661 171.855 146.470 1.00 49.52  ? 98   ARG B CZ    1 
ATOM   11685 N  NH1   . ARG B 2  98   ? 159.396 172.013 147.558 1.00 48.22  ? 98   ARG B NH1   1 
ATOM   11686 N  NH2   . ARG B 2  98   ? 157.461 172.423 146.408 1.00 47.64  ? 98   ARG B NH2   1 
ATOM   11687 N  N     . PRO B 2  99   ? 161.912 165.200 144.857 1.00 49.05  ? 99   PRO B N     1 
ATOM   11688 C  CA    . PRO B 2  99   ? 162.723 164.149 144.226 1.00 45.31  ? 99   PRO B CA    1 
ATOM   11689 C  C     . PRO B 2  99   ? 163.996 164.716 143.622 1.00 46.56  ? 99   PRO B C     1 
ATOM   11690 O  O     . PRO B 2  99   ? 164.027 165.849 143.136 1.00 46.98  ? 99   PRO B O     1 
ATOM   11691 C  CB    . PRO B 2  99   ? 161.795 163.583 143.150 1.00 42.51  ? 99   PRO B CB    1 
ATOM   11692 C  CG    . PRO B 2  99   ? 160.432 163.890 143.641 1.00 44.21  ? 99   PRO B CG    1 
ATOM   11693 C  CD    . PRO B 2  99   ? 160.541 165.219 144.321 1.00 45.10  ? 99   PRO B CD    1 
ATOM   11694 N  N     . GLN B 2  100  ? 165.059 163.913 143.666 1.00 45.38  ? 100  GLN B N     1 
ATOM   11695 C  CA    . GLN B 2  100  ? 166.395 164.395 143.351 1.00 45.51  ? 100  GLN B CA    1 
ATOM   11696 C  C     . GLN B 2  100  ? 167.138 163.359 142.516 1.00 46.20  ? 100  GLN B C     1 
ATOM   11697 O  O     . GLN B 2  100  ? 166.790 162.178 142.495 1.00 47.30  ? 100  GLN B O     1 
ATOM   11698 C  CB    . GLN B 2  100  ? 167.167 164.727 144.634 1.00 46.10  ? 100  GLN B CB    1 
ATOM   11699 C  CG    . GLN B 2  100  ? 167.871 166.066 144.604 1.00 45.44  ? 100  GLN B CG    1 
ATOM   11700 C  CD    . GLN B 2  100  ? 166.935 167.233 144.810 1.00 46.62  ? 100  GLN B CD    1 
ATOM   11701 O  OE1   . GLN B 2  100  ? 165.727 167.059 144.941 1.00 46.41  ? 100  GLN B OE1   1 
ATOM   11702 N  NE2   . GLN B 2  100  ? 167.489 168.438 144.825 1.00 45.59  ? 100  GLN B NE2   1 
ATOM   11703 N  N     . HIS B 2  101  ? 168.184 163.818 141.828 1.00 49.69  ? 101  HIS B N     1 
ATOM   11704 C  CA    . HIS B 2  101  ? 168.944 162.969 140.920 1.00 51.14  ? 101  HIS B CA    1 
ATOM   11705 C  C     . HIS B 2  101  ? 170.428 163.083 141.238 1.00 53.20  ? 101  HIS B C     1 
ATOM   11706 O  O     . HIS B 2  101  ? 170.882 164.062 141.836 1.00 51.26  ? 101  HIS B O     1 
ATOM   11707 C  CB    . HIS B 2  101  ? 168.683 163.345 139.457 1.00 48.93  ? 101  HIS B CB    1 
ATOM   11708 C  CG    . HIS B 2  101  ? 169.113 162.297 138.481 1.00 51.31  ? 101  HIS B CG    1 
ATOM   11709 N  ND1   . HIS B 2  101  ? 170.316 162.351 137.811 1.00 53.27  ? 101  HIS B ND1   1 
ATOM   11710 C  CD2   . HIS B 2  101  ? 168.503 161.163 138.066 1.00 51.37  ? 101  HIS B CD2   1 
ATOM   11711 C  CE1   . HIS B 2  101  ? 170.426 161.297 137.023 1.00 51.46  ? 101  HIS B CE1   1 
ATOM   11712 N  NE2   . HIS B 2  101  ? 169.340 160.560 137.159 1.00 51.01  ? 101  HIS B NE2   1 
ATOM   11713 N  N     . ARG B 2  102  ? 171.188 162.071 140.816 1.00 59.05  ? 102  ARG B N     1 
ATOM   11714 C  CA    . ARG B 2  102  ? 172.613 161.991 141.121 1.00 59.05  ? 102  ARG B CA    1 
ATOM   11715 C  C     . ARG B 2  102  ? 173.501 162.639 140.062 1.00 57.64  ? 102  ARG B C     1 
ATOM   11716 O  O     . ARG B 2  102  ? 174.494 163.284 140.410 1.00 55.08  ? 102  ARG B O     1 
ATOM   11717 C  CB    . ARG B 2  102  ? 173.032 160.526 141.319 1.00 56.14  ? 102  ARG B CB    1 
ATOM   11718 C  CG    . ARG B 2  102  ? 173.083 159.679 140.050 1.00 55.99  ? 102  ARG B CG    1 
ATOM   11719 C  CD    . ARG B 2  102  ? 173.022 158.193 140.354 1.00 55.77  ? 102  ARG B CD    1 
ATOM   11720 N  NE    . ARG B 2  102  ? 171.658 157.678 140.378 1.00 56.94  ? 102  ARG B NE    1 
ATOM   11721 C  CZ    . ARG B 2  102  ? 171.330 156.454 140.765 1.00 57.46  ? 102  ARG B CZ    1 
ATOM   11722 N  NH1   . ARG B 2  102  ? 172.239 155.605 141.212 1.00 57.68  ? 102  ARG B NH1   1 
ATOM   11723 N  NH2   . ARG B 2  102  ? 170.059 156.071 140.698 1.00 56.14  ? 102  ARG B NH2   1 
ATOM   11724 N  N     . ASN B 2  103  ? 173.175 162.472 138.779 1.00 55.84  ? 103  ASN B N     1 
ATOM   11725 C  CA    . ASN B 2  103  ? 173.852 163.051 137.621 1.00 55.86  ? 103  ASN B CA    1 
ATOM   11726 C  C     . ASN B 2  103  ? 175.251 162.484 137.391 1.00 56.71  ? 103  ASN B C     1 
ATOM   11727 O  O     . ASN B 2  103  ? 175.894 162.856 136.399 1.00 55.00  ? 103  ASN B O     1 
ATOM   11728 C  CB    . ASN B 2  103  ? 173.946 164.583 137.701 1.00 55.54  ? 103  ASN B CB    1 
ATOM   11729 C  CG    . ASN B 2  103  ? 173.958 165.236 136.334 1.00 57.83  ? 103  ASN B CG    1 
ATOM   11730 O  OD1   . ASN B 2  103  ? 173.733 164.579 135.316 1.00 55.29  ? 103  ASN B OD1   1 
ATOM   11731 N  ND2   . ASN B 2  103  ? 174.222 166.535 136.304 1.00 57.65  ? 103  ASN B ND2   1 
ATOM   11732 N  N     . TYR B 2  104  ? 175.744 161.603 138.265 1.00 50.62  ? 104  TYR B N     1 
ATOM   11733 C  CA    . TYR B 2  104  ? 177.006 160.882 138.075 1.00 50.56  ? 104  TYR B CA    1 
ATOM   11734 C  C     . TYR B 2  104  ? 178.174 161.847 137.829 1.00 50.50  ? 104  TYR B C     1 
ATOM   11735 O  O     . TYR B 2  104  ? 178.773 161.899 136.754 1.00 51.80  ? 104  TYR B O     1 
ATOM   11736 C  CB    . TYR B 2  104  ? 176.870 159.859 136.941 1.00 49.32  ? 104  TYR B CB    1 
ATOM   11737 C  CG    . TYR B 2  104  ? 178.137 159.102 136.631 1.00 50.92  ? 104  TYR B CG    1 
ATOM   11738 C  CD1   . TYR B 2  104  ? 178.787 158.363 137.607 1.00 49.75  ? 104  TYR B CD1   1 
ATOM   11739 C  CD2   . TYR B 2  104  ? 178.677 159.123 135.355 1.00 49.41  ? 104  TYR B CD2   1 
ATOM   11740 C  CE1   . TYR B 2  104  ? 179.951 157.668 137.319 1.00 49.77  ? 104  TYR B CE1   1 
ATOM   11741 C  CE2   . TYR B 2  104  ? 179.837 158.435 135.057 1.00 49.31  ? 104  TYR B CE2   1 
ATOM   11742 C  CZ    . TYR B 2  104  ? 180.472 157.709 136.040 1.00 50.26  ? 104  TYR B CZ    1 
ATOM   11743 O  OH    . TYR B 2  104  ? 181.625 157.022 135.738 1.00 48.50  ? 104  TYR B OH    1 
ATOM   11744 N  N     . SER B 2  105  ? 178.463 162.645 138.860 1.00 46.81  ? 105  SER B N     1 
ATOM   11745 C  CA    . SER B 2  105  ? 179.694 163.428 138.865 1.00 48.48  ? 105  SER B CA    1 
ATOM   11746 C  C     . SER B 2  105  ? 180.310 163.519 140.259 1.00 49.50  ? 105  SER B C     1 
ATOM   11747 O  O     . SER B 2  105  ? 181.258 164.291 140.456 1.00 47.15  ? 105  SER B O     1 
ATOM   11748 C  CB    . SER B 2  105  ? 179.466 164.836 138.299 1.00 46.01  ? 105  SER B CB    1 
ATOM   11749 O  OG    . SER B 2  105  ? 179.351 164.812 136.884 1.00 47.21  ? 105  SER B OG    1 
ATOM   11750 N  N     . GLN B 2  106  ? 179.799 162.749 141.223 1.00 49.27  ? 106  GLN B N     1 
ATOM   11751 C  CA    . GLN B 2  106  ? 180.310 162.725 142.593 1.00 48.21  ? 106  GLN B CA    1 
ATOM   11752 C  C     . GLN B 2  106  ? 180.207 164.114 143.236 1.00 49.38  ? 106  GLN B C     1 
ATOM   11753 O  O     . GLN B 2  106  ? 181.147 164.628 143.848 1.00 48.65  ? 106  GLN B O     1 
ATOM   11754 C  CB    . GLN B 2  106  ? 181.750 162.192 142.618 1.00 47.69  ? 106  GLN B CB    1 
ATOM   11755 C  CG    . GLN B 2  106  ? 182.288 161.782 143.987 1.00 48.54  ? 106  GLN B CG    1 
ATOM   11756 C  CD    . GLN B 2  106  ? 181.604 160.561 144.557 1.00 49.62  ? 106  GLN B CD    1 
ATOM   11757 O  OE1   . GLN B 2  106  ? 180.670 160.667 145.350 1.00 48.14  ? 106  GLN B OE1   1 
ATOM   11758 N  NE2   . GLN B 2  106  ? 182.087 159.388 144.175 1.00 48.59  ? 106  GLN B NE2   1 
ATOM   11759 N  N     . GLY B 2  107  ? 179.025 164.714 143.095 1.00 46.01  ? 107  GLY B N     1 
ATOM   11760 C  CA    . GLY B 2  107  ? 178.749 166.005 143.700 1.00 43.43  ? 107  GLY B CA    1 
ATOM   11761 C  C     . GLY B 2  107  ? 177.569 165.937 144.649 1.00 45.01  ? 107  GLY B C     1 
ATOM   11762 O  O     . GLY B 2  107  ? 177.439 164.965 145.399 1.00 43.75  ? 107  GLY B O     1 
ATOM   11763 N  N     . ASN B 2  108  ? 176.712 166.957 144.644 1.00 54.28  ? 108  ASN B N     1 
ATOM   11764 C  CA    . ASN B 2  108  ? 175.469 166.904 145.401 1.00 55.91  ? 108  ASN B CA    1 
ATOM   11765 C  C     . ASN B 2  108  ? 174.356 166.352 144.510 1.00 56.55  ? 108  ASN B C     1 
ATOM   11766 O  O     . ASN B 2  108  ? 174.591 165.902 143.385 1.00 56.87  ? 108  ASN B O     1 
ATOM   11767 C  CB    . ASN B 2  108  ? 175.113 168.278 145.968 1.00 52.78  ? 108  ASN B CB    1 
ATOM   11768 C  CG    . ASN B 2  108  ? 176.181 168.828 146.894 1.00 54.96  ? 108  ASN B CG    1 
ATOM   11769 O  OD1   . ASN B 2  108  ? 176.766 169.878 146.633 1.00 55.34  ? 108  ASN B OD1   1 
ATOM   11770 N  ND2   . ASN B 2  108  ? 176.438 168.118 147.987 1.00 53.87  ? 108  ASN B ND2   1 
ATOM   11771 N  N     . LYS B 2  109  ? 173.123 166.390 145.004 1.00 49.32  ? 109  LYS B N     1 
ATOM   11772 C  CA    . LYS B 2  109  ? 171.985 165.804 144.312 1.00 50.21  ? 109  LYS B CA    1 
ATOM   11773 C  C     . LYS B 2  109  ? 171.182 166.904 143.630 1.00 51.02  ? 109  LYS B C     1 
ATOM   11774 O  O     . LYS B 2  109  ? 170.875 167.929 144.247 1.00 48.82  ? 109  LYS B O     1 
ATOM   11775 C  CB    . LYS B 2  109  ? 171.107 165.016 145.287 1.00 49.45  ? 109  LYS B CB    1 
ATOM   11776 C  CG    . LYS B 2  109  ? 171.822 163.867 145.994 1.00 49.06  ? 109  LYS B CG    1 
ATOM   11777 C  CD    . LYS B 2  109  ? 172.100 162.709 145.041 1.00 49.20  ? 109  LYS B CD    1 
ATOM   11778 C  CE    . LYS B 2  109  ? 170.852 161.886 144.761 1.00 50.27  ? 109  LYS B CE    1 
ATOM   11779 N  NZ    . LYS B 2  109  ? 170.410 161.101 145.950 1.00 51.82  ? 109  LYS B NZ    1 
ATOM   11780 N  N     . ILE B 2  110  ? 170.848 166.688 142.358 1.00 49.06  ? 110  ILE B N     1 
ATOM   11781 C  CA    . ILE B 2  110  ? 170.170 167.682 141.536 1.00 49.07  ? 110  ILE B CA    1 
ATOM   11782 C  C     . ILE B 2  110  ? 168.700 167.310 141.390 1.00 49.39  ? 110  ILE B C     1 
ATOM   11783 O  O     . ILE B 2  110  ? 168.303 166.155 141.567 1.00 46.25  ? 110  ILE B O     1 
ATOM   11784 C  CB    . ILE B 2  110  ? 170.827 167.819 140.151 1.00 45.91  ? 110  ILE B CB    1 
ATOM   11785 C  CG1   . ILE B 2  110  ? 170.702 166.500 139.389 1.00 47.30  ? 110  ILE B CG1   1 
ATOM   11786 C  CG2   . ILE B 2  110  ? 172.278 168.219 140.293 1.00 45.53  ? 110  ILE B CG2   1 
ATOM   11787 C  CD1   . ILE B 2  110  ? 170.906 166.626 137.913 1.00 45.88  ? 110  ILE B CD1   1 
ATOM   11788 N  N     . ASN B 2  111  ? 167.892 168.309 141.027 1.00 44.84  ? 111  ASN B N     1 
ATOM   11789 C  CA    . ASN B 2  111  ? 166.456 168.107 140.873 1.00 43.24  ? 111  ASN B CA    1 
ATOM   11790 C  C     . ASN B 2  111  ? 166.168 167.025 139.840 1.00 45.22  ? 111  ASN B C     1 
ATOM   11791 O  O     . ASN B 2  111  ? 166.841 166.935 138.809 1.00 46.46  ? 111  ASN B O     1 
ATOM   11792 C  CB    . ASN B 2  111  ? 165.773 169.409 140.452 1.00 42.45  ? 111  ASN B CB    1 
ATOM   11793 C  CG    . ASN B 2  111  ? 165.695 170.422 141.571 1.00 45.63  ? 111  ASN B CG    1 
ATOM   11794 O  OD1   . ASN B 2  111  ? 165.474 170.070 142.729 1.00 46.80  ? 111  ASN B OD1   1 
ATOM   11795 N  ND2   . ASN B 2  111  ? 165.851 171.696 141.226 1.00 44.44  ? 111  ASN B ND2   1 
ATOM   11796 N  N     . LEU B 2  112  ? 165.165 166.200 140.124 1.00 39.06  ? 112  LEU B N     1 
ATOM   11797 C  CA    . LEU B 2  112  ? 164.733 165.136 139.226 1.00 38.61  ? 112  LEU B CA    1 
ATOM   11798 C  C     . LEU B 2  112  ? 163.352 165.488 138.694 1.00 40.99  ? 112  LEU B C     1 
ATOM   11799 O  O     . LEU B 2  112  ? 162.377 165.495 139.448 1.00 39.34  ? 112  LEU B O     1 
ATOM   11800 C  CB    . LEU B 2  112  ? 164.716 163.800 139.955 1.00 38.27  ? 112  LEU B CB    1 
ATOM   11801 C  CG    . LEU B 2  112  ? 164.188 162.595 139.196 1.00 38.18  ? 112  LEU B CG    1 
ATOM   11802 C  CD1   . LEU B 2  112  ? 165.116 162.250 138.068 1.00 36.46  ? 112  LEU B CD1   1 
ATOM   11803 C  CD2   . LEU B 2  112  ? 164.049 161.428 140.146 1.00 41.05  ? 112  LEU B CD2   1 
ATOM   11804 N  N     . LEU B 2  113  ? 163.268 165.769 137.394 1.00 39.63  ? 113  LEU B N     1 
ATOM   11805 C  CA    . LEU B 2  113  ? 162.018 166.164 136.764 1.00 35.36  ? 113  LEU B CA    1 
ATOM   11806 C  C     . LEU B 2  113  ? 161.217 164.937 136.324 1.00 35.50  ? 113  LEU B C     1 
ATOM   11807 O  O     . LEU B 2  113  ? 161.792 163.887 136.028 1.00 33.38  ? 113  LEU B O     1 
ATOM   11808 C  CB    . LEU B 2  113  ? 162.300 167.069 135.573 1.00 34.20  ? 113  LEU B CB    1 
ATOM   11809 C  CG    . LEU B 2  113  ? 162.771 168.469 135.971 1.00 34.39  ? 113  LEU B CG    1 
ATOM   11810 C  CD1   . LEU B 2  113  ? 163.110 169.289 134.753 1.00 34.26  ? 113  LEU B CD1   1 
ATOM   11811 C  CD2   . LEU B 2  113  ? 161.717 169.165 136.793 1.00 32.47  ? 113  LEU B CD2   1 
ATOM   11812 N  N     . PRO B 2  114  ? 159.882 165.045 136.285 1.00 39.38  ? 114  PRO B N     1 
ATOM   11813 C  CA    . PRO B 2  114  ? 159.058 163.857 135.986 1.00 36.80  ? 114  PRO B CA    1 
ATOM   11814 C  C     . PRO B 2  114  ? 159.342 163.223 134.634 1.00 38.45  ? 114  PRO B C     1 
ATOM   11815 O  O     . PRO B 2  114  ? 159.295 161.993 134.507 1.00 37.40  ? 114  PRO B O     1 
ATOM   11816 C  CB    . PRO B 2  114  ? 157.626 164.403 136.062 1.00 34.22  ? 114  PRO B CB    1 
ATOM   11817 C  CG    . PRO B 2  114  ? 157.726 165.642 136.863 1.00 36.38  ? 114  PRO B CG    1 
ATOM   11818 C  CD    . PRO B 2  114  ? 159.056 166.232 136.553 1.00 34.76  ? 114  PRO B CD    1 
ATOM   11819 N  N     . ASN B 2  115  ? 159.631 164.028 133.612 1.00 33.89  ? 115  ASN B N     1 
ATOM   11820 C  CA    . ASN B 2  115  ? 159.913 163.464 132.300 1.00 31.62  ? 115  ASN B CA    1 
ATOM   11821 C  C     . ASN B 2  115  ? 161.213 162.670 132.303 1.00 32.72  ? 115  ASN B C     1 
ATOM   11822 O  O     . ASN B 2  115  ? 161.314 161.647 131.619 1.00 30.37  ? 115  ASN B O     1 
ATOM   11823 C  CB    . ASN B 2  115  ? 159.952 164.576 131.255 1.00 31.65  ? 115  ASN B CB    1 
ATOM   11824 C  CG    . ASN B 2  115  ? 159.524 164.101 129.881 1.00 35.96  ? 115  ASN B CG    1 
ATOM   11825 O  OD1   . ASN B 2  115  ? 158.716 163.181 129.752 1.00 39.99  ? 115  ASN B OD1   1 
ATOM   11826 N  ND2   . ASN B 2  115  ? 160.065 164.728 128.844 1.00 32.54  ? 115  ASN B ND2   1 
ATOM   11827 N  N     . LYS B 2  116  ? 162.208 163.114 133.072 1.00 37.52  ? 116  LYS B N     1 
ATOM   11828 C  CA    . LYS B 2  116  ? 163.441 162.347 133.216 1.00 34.75  ? 116  LYS B CA    1 
ATOM   11829 C  C     . LYS B 2  116  ? 163.167 160.978 133.830 1.00 34.64  ? 116  LYS B C     1 
ATOM   11830 O  O     . LYS B 2  116  ? 163.714 159.967 133.378 1.00 35.34  ? 116  LYS B O     1 
ATOM   11831 C  CB    . LYS B 2  116  ? 164.438 163.136 134.064 1.00 33.58  ? 116  LYS B CB    1 
ATOM   11832 C  CG    . LYS B 2  116  ? 165.664 162.366 134.524 1.00 35.86  ? 116  LYS B CG    1 
ATOM   11833 C  CD    . LYS B 2  116  ? 166.596 162.038 133.376 1.00 39.13  ? 116  LYS B CD    1 
ATOM   11834 C  CE    . LYS B 2  116  ? 168.031 162.416 133.712 1.00 38.44  ? 116  LYS B CE    1 
ATOM   11835 N  NZ    . LYS B 2  116  ? 169.021 161.758 132.818 1.00 36.81  ? 116  LYS B NZ    1 
ATOM   11836 N  N     . ALA B 2  117  ? 162.318 160.925 134.857 1.00 33.55  ? 117  ALA B N     1 
ATOM   11837 C  CA    . ALA B 2  117  ? 161.959 159.646 135.461 1.00 34.39  ? 117  ALA B CA    1 
ATOM   11838 C  C     . ALA B 2  117  ? 161.179 158.772 134.488 1.00 35.07  ? 117  ALA B C     1 
ATOM   11839 O  O     . ALA B 2  117  ? 161.332 157.546 134.486 1.00 33.92  ? 117  ALA B O     1 
ATOM   11840 C  CB    . ALA B 2  117  ? 161.157 159.875 136.740 1.00 33.47  ? 117  ALA B CB    1 
ATOM   11841 N  N     . ARG B 2  118  ? 160.320 159.381 133.669 1.00 39.14  ? 118  ARG B N     1 
ATOM   11842 C  CA    . ARG B 2  118  ? 159.597 158.610 132.664 1.00 33.43  ? 118  ARG B CA    1 
ATOM   11843 C  C     . ARG B 2  118  ? 160.549 157.988 131.654 1.00 36.63  ? 118  ARG B C     1 
ATOM   11844 O  O     . ARG B 2  118  ? 160.447 156.796 131.346 1.00 38.87  ? 118  ARG B O     1 
ATOM   11845 C  CB    . ARG B 2  118  ? 158.583 159.499 131.952 1.00 32.57  ? 118  ARG B CB    1 
ATOM   11846 C  CG    . ARG B 2  118  ? 157.406 159.909 132.798 1.00 32.74  ? 118  ARG B CG    1 
ATOM   11847 C  CD    . ARG B 2  118  ? 156.313 160.521 131.951 1.00 32.52  ? 118  ARG B CD    1 
ATOM   11848 N  NE    . ARG B 2  118  ? 155.298 161.164 132.773 1.00 32.42  ? 118  ARG B NE    1 
ATOM   11849 C  CZ    . ARG B 2  118  ? 155.229 162.467 133.000 1.00 32.54  ? 118  ARG B CZ    1 
ATOM   11850 N  NH1   . ARG B 2  118  ? 156.101 163.307 132.474 1.00 29.55  ? 118  ARG B NH1   1 
ATOM   11851 N  NH2   . ARG B 2  118  ? 154.258 162.939 133.771 1.00 33.04  ? 118  ARG B NH2   1 
ATOM   11852 N  N     . LEU B 2  119  ? 161.481 158.781 131.125 1.00 36.70  ? 119  LEU B N     1 
ATOM   11853 C  CA    . LEU B 2  119  ? 162.338 158.299 130.047 1.00 37.89  ? 119  LEU B CA    1 
ATOM   11854 C  C     . LEU B 2  119  ? 163.413 157.345 130.547 1.00 39.62  ? 119  LEU B C     1 
ATOM   11855 O  O     . LEU B 2  119  ? 163.754 156.381 129.855 1.00 41.62  ? 119  LEU B O     1 
ATOM   11856 C  CB    . LEU B 2  119  ? 162.974 159.474 129.302 1.00 39.76  ? 119  LEU B CB    1 
ATOM   11857 C  CG    . LEU B 2  119  ? 162.006 160.543 128.794 1.00 40.30  ? 119  LEU B CG    1 
ATOM   11858 C  CD1   . LEU B 2  119  ? 162.736 161.821 128.426 1.00 37.33  ? 119  LEU B CD1   1 
ATOM   11859 C  CD2   . LEU B 2  119  ? 161.203 160.018 127.621 1.00 39.87  ? 119  LEU B CD2   1 
ATOM   11860 N  N     . CYS B 2  120  ? 163.959 157.588 131.734 1.00 41.06  ? 120  CYS B N     1 
ATOM   11861 C  CA    . CYS B 2  120  ? 165.060 156.787 132.247 1.00 39.84  ? 120  CYS B CA    1 
ATOM   11862 C  C     . CYS B 2  120  ? 164.604 155.556 133.013 1.00 38.70  ? 120  CYS B C     1 
ATOM   11863 O  O     . CYS B 2  120  ? 165.437 154.709 133.342 1.00 40.54  ? 120  CYS B O     1 
ATOM   11864 C  CB    . CYS B 2  120  ? 165.954 157.643 133.147 1.00 41.53  ? 120  CYS B CB    1 
ATOM   11865 S  SG    . CYS B 2  120  ? 167.129 158.683 132.264 1.00 48.66  ? 120  CYS B SG    1 
ATOM   11866 N  N     . GLY B 2  121  ? 163.312 155.420 133.288 1.00 35.12  ? 121  GLY B N     1 
ATOM   11867 C  CA    . GLY B 2  121  ? 162.849 154.309 134.095 1.00 35.35  ? 121  GLY B CA    1 
ATOM   11868 C  C     . GLY B 2  121  ? 163.157 154.455 135.565 1.00 35.94  ? 121  GLY B C     1 
ATOM   11869 O  O     . GLY B 2  121  ? 163.336 153.449 136.256 1.00 33.51  ? 121  GLY B O     1 
ATOM   11870 N  N     . LEU B 2  122  ? 163.231 155.687 136.058 1.00 35.69  ? 122  LEU B N     1 
ATOM   11871 C  CA    . LEU B 2  122  ? 163.515 155.961 137.455 1.00 36.64  ? 122  LEU B CA    1 
ATOM   11872 C  C     . LEU B 2  122  ? 162.218 155.964 138.262 1.00 38.70  ? 122  LEU B C     1 
ATOM   11873 O  O     . LEU B 2  122  ? 161.144 155.617 137.765 1.00 39.44  ? 122  LEU B O     1 
ATOM   11874 C  CB    . LEU B 2  122  ? 164.251 157.289 137.588 1.00 36.77  ? 122  LEU B CB    1 
ATOM   11875 C  CG    . LEU B 2  122  ? 165.517 157.481 136.755 1.00 36.99  ? 122  LEU B CG    1 
ATOM   11876 C  CD1   . LEU B 2  122  ? 165.986 158.919 136.854 1.00 35.36  ? 122  LEU B CD1   1 
ATOM   11877 C  CD2   . LEU B 2  122  ? 166.614 156.516 137.185 1.00 35.72  ? 122  LEU B CD2   1 
ATOM   11878 N  N     . SER B 2  123  ? 162.311 156.352 139.528 1.00 39.13  ? 123  SER B N     1 
ATOM   11879 C  CA    . SER B 2  123  ? 161.159 156.533 140.396 1.00 38.13  ? 123  SER B CA    1 
ATOM   11880 C  C     . SER B 2  123  ? 161.150 157.967 140.896 1.00 40.75  ? 123  SER B C     1 
ATOM   11881 O  O     . SER B 2  123  ? 162.193 158.508 141.270 1.00 42.82  ? 123  SER B O     1 
ATOM   11882 C  CB    . SER B 2  123  ? 161.190 155.570 141.583 1.00 39.13  ? 123  SER B CB    1 
ATOM   11883 O  OG    . SER B 2  123  ? 161.106 154.223 141.161 1.00 42.09  ? 123  SER B OG    1 
ATOM   11884 N  N     . TYR B 2  124  ? 159.971 158.583 140.896 1.00 37.98  ? 124  TYR B N     1 
ATOM   11885 C  CA    . TYR B 2  124  ? 159.826 159.981 141.297 1.00 38.88  ? 124  TYR B CA    1 
ATOM   11886 C  C     . TYR B 2  124  ? 159.674 160.065 142.816 1.00 40.41  ? 124  TYR B C     1 
ATOM   11887 O  O     . TYR B 2  124  ? 158.707 160.605 143.357 1.00 42.25  ? 124  TYR B O     1 
ATOM   11888 C  CB    . TYR B 2  124  ? 158.647 160.607 140.568 1.00 41.62  ? 124  TYR B CB    1 
ATOM   11889 C  CG    . TYR B 2  124  ? 158.673 162.110 140.508 1.00 40.27  ? 124  TYR B CG    1 
ATOM   11890 C  CD1   . TYR B 2  124  ? 159.725 162.782 139.917 1.00 40.49  ? 124  TYR B CD1   1 
ATOM   11891 C  CD2   . TYR B 2  124  ? 157.625 162.853 141.013 1.00 38.18  ? 124  TYR B CD2   1 
ATOM   11892 C  CE1   . TYR B 2  124  ? 159.744 164.147 139.862 1.00 38.81  ? 124  TYR B CE1   1 
ATOM   11893 C  CE2   . TYR B 2  124  ? 157.636 164.221 140.956 1.00 39.99  ? 124  TYR B CE2   1 
ATOM   11894 C  CZ    . TYR B 2  124  ? 158.698 164.863 140.379 1.00 40.14  ? 124  TYR B CZ    1 
ATOM   11895 O  OH    . TYR B 2  124  ? 158.717 166.232 140.318 1.00 42.23  ? 124  TYR B OH    1 
ATOM   11896 N  N     . SER B 2  125  ? 160.679 159.538 143.509 1.00 41.41  ? 125  SER B N     1 
ATOM   11897 C  CA    . SER B 2  125  ? 160.647 159.387 144.956 1.00 39.22  ? 125  SER B CA    1 
ATOM   11898 C  C     . SER B 2  125  ? 161.493 160.461 145.617 1.00 41.15  ? 125  SER B C     1 
ATOM   11899 O  O     . SER B 2  125  ? 162.640 160.692 145.225 1.00 42.07  ? 125  SER B O     1 
ATOM   11900 C  CB    . SER B 2  125  ? 161.149 158.007 145.376 1.00 38.48  ? 125  SER B CB    1 
ATOM   11901 O  OG    . SER B 2  125  ? 160.359 156.975 144.818 1.00 43.23  ? 125  SER B OG    1 
ATOM   11902 N  N     . GLY B 2  126  ? 160.921 161.108 146.630 1.00 39.57  ? 126  GLY B N     1 
ATOM   11903 C  CA    . GLY B 2  126  ? 161.606 162.130 147.382 1.00 38.65  ? 126  GLY B CA    1 
ATOM   11904 C  C     . GLY B 2  126  ? 162.224 161.598 148.659 1.00 41.92  ? 126  GLY B C     1 
ATOM   11905 O  O     . GLY B 2  126  ? 161.672 160.724 149.334 1.00 38.34  ? 126  GLY B O     1 
ATOM   11906 N  N     . PRO B 2  127  ? 163.401 162.114 149.003 1.00 45.40  ? 127  PRO B N     1 
ATOM   11907 C  CA    . PRO B 2  127  ? 164.117 161.618 150.185 1.00 44.91  ? 127  PRO B CA    1 
ATOM   11908 C  C     . PRO B 2  127  ? 163.415 161.966 151.488 1.00 44.05  ? 127  PRO B C     1 
ATOM   11909 O  O     . PRO B 2  127  ? 162.897 163.069 151.672 1.00 43.26  ? 127  PRO B O     1 
ATOM   11910 C  CB    . PRO B 2  127  ? 165.478 162.319 150.092 1.00 43.14  ? 127  PRO B CB    1 
ATOM   11911 C  CG    . PRO B 2  127  ? 165.577 162.800 148.686 1.00 42.49  ? 127  PRO B CG    1 
ATOM   11912 C  CD    . PRO B 2  127  ? 164.188 163.100 148.251 1.00 40.78  ? 127  PRO B CD    1 
ATOM   11913 N  N     . VAL B 2  128  ? 163.434 161.009 152.412 1.00 44.07  ? 128  VAL B N     1 
ATOM   11914 C  CA    . VAL B 2  128  ? 162.848 161.165 153.738 1.00 44.54  ? 128  VAL B CA    1 
ATOM   11915 C  C     . VAL B 2  128  ? 163.975 161.178 154.759 1.00 46.32  ? 128  VAL B C     1 
ATOM   11916 O  O     . VAL B 2  128  ? 164.746 160.217 154.859 1.00 46.74  ? 128  VAL B O     1 
ATOM   11917 C  CB    . VAL B 2  128  ? 161.841 160.045 154.065 1.00 44.11  ? 128  VAL B CB    1 
ATOM   11918 C  CG1   . VAL B 2  128  ? 161.059 160.387 155.324 1.00 42.66  ? 128  VAL B CG1   1 
ATOM   11919 C  CG2   . VAL B 2  128  ? 160.908 159.801 152.902 1.00 42.46  ? 128  VAL B CG2   1 
ATOM   11920 N  N     . ASN B 2  129  ? 164.054 162.258 155.530 1.00 45.78  ? 129  ASN B N     1 
ATOM   11921 C  CA    . ASN B 2  129  ? 165.128 162.485 156.485 1.00 45.25  ? 129  ASN B CA    1 
ATOM   11922 C  C     . ASN B 2  129  ? 164.596 162.253 157.892 1.00 48.30  ? 129  ASN B C     1 
ATOM   11923 O  O     . ASN B 2  129  ? 163.510 162.735 158.232 1.00 47.70  ? 129  ASN B O     1 
ATOM   11924 C  CB    . ASN B 2  129  ? 165.669 163.908 156.361 1.00 43.63  ? 129  ASN B CB    1 
ATOM   11925 C  CG    . ASN B 2  129  ? 165.971 164.291 154.931 1.00 45.78  ? 129  ASN B CG    1 
ATOM   11926 O  OD1   . ASN B 2  129  ? 166.434 163.475 154.141 1.00 46.60  ? 129  ASN B OD1   1 
ATOM   11927 N  ND2   . ASN B 2  129  ? 165.698 165.541 154.588 1.00 45.45  ? 129  ASN B ND2   1 
ATOM   11928 N  N     . LEU B 2  130  ? 165.352 161.520 158.707 1.00 46.62  ? 130  LEU B N     1 
ATOM   11929 C  CA    . LEU B 2  130  ? 164.923 161.195 160.058 1.00 45.20  ? 130  LEU B CA    1 
ATOM   11930 C  C     . LEU B 2  130  ? 166.026 161.496 161.061 1.00 46.64  ? 130  LEU B C     1 
ATOM   11931 O  O     . LEU B 2  130  ? 167.212 161.534 160.721 1.00 47.42  ? 130  LEU B O     1 
ATOM   11932 C  CB    . LEU B 2  130  ? 164.522 159.719 160.197 1.00 44.85  ? 130  LEU B CB    1 
ATOM   11933 C  CG    . LEU B 2  130  ? 163.044 159.373 160.027 1.00 45.50  ? 130  LEU B CG    1 
ATOM   11934 C  CD1   . LEU B 2  130  ? 162.641 159.490 158.561 1.00 48.80  ? 130  LEU B CD1   1 
ATOM   11935 C  CD2   . LEU B 2  130  ? 162.720 157.995 160.572 1.00 43.27  ? 130  LEU B CD2   1 
ATOM   11936 N  N     . ALA B 2  131  ? 165.613 161.714 162.306 1.00 46.98  ? 131  ALA B N     1 
ATOM   11937 C  CA    . ALA B 2  131  ? 166.498 161.733 163.460 1.00 46.11  ? 131  ALA B CA    1 
ATOM   11938 C  C     . ALA B 2  131  ? 166.041 160.662 164.442 1.00 47.45  ? 131  ALA B C     1 
ATOM   11939 O  O     . ALA B 2  131  ? 164.933 160.127 164.332 1.00 48.21  ? 131  ALA B O     1 
ATOM   11940 C  CB    . ALA B 2  131  ? 166.516 163.107 164.138 1.00 45.43  ? 131  ALA B CB    1 
ATOM   11941 N  N     . ALA B 2  132  ? 166.909 160.332 165.396 1.00 46.06  ? 132  ALA B N     1 
ATOM   11942 C  CA    . ALA B 2  132  ? 166.584 159.285 166.355 1.00 47.92  ? 132  ALA B CA    1 
ATOM   11943 C  C     . ALA B 2  132  ? 167.289 159.548 167.677 1.00 48.69  ? 132  ALA B C     1 
ATOM   11944 O  O     . ALA B 2  132  ? 168.267 160.298 167.750 1.00 45.97  ? 132  ALA B O     1 
ATOM   11945 C  CB    . ALA B 2  132  ? 166.958 157.894 165.824 1.00 44.49  ? 132  ALA B CB    1 
ATOM   11946 N  N     . GLU B 2  133  ? 166.764 158.921 168.728 1.00 54.10  ? 133  GLU B N     1 
ATOM   11947 C  CA    . GLU B 2  133  ? 167.364 158.925 170.055 1.00 52.30  ? 133  GLU B CA    1 
ATOM   11948 C  C     . GLU B 2  133  ? 167.389 157.502 170.588 1.00 52.61  ? 133  GLU B C     1 
ATOM   11949 O  O     . GLU B 2  133  ? 166.368 156.807 170.556 1.00 51.90  ? 133  GLU B O     1 
ATOM   11950 C  CB    . GLU B 2  133  ? 166.594 159.829 171.019 1.00 49.89  ? 133  GLU B CB    1 
ATOM   11951 C  CG    . GLU B 2  133  ? 166.761 161.308 170.754 1.00 51.63  ? 133  GLU B CG    1 
ATOM   11952 C  CD    . GLU B 2  133  ? 168.152 161.798 171.102 1.00 51.84  ? 133  GLU B CD    1 
ATOM   11953 O  OE1   . GLU B 2  133  ? 168.818 161.145 171.929 1.00 53.36  ? 133  GLU B OE1   1 
ATOM   11954 O  OE2   . GLU B 2  133  ? 168.572 162.841 170.562 1.00 52.18  ? 133  GLU B OE2   1 
ATOM   11955 N  N     . VAL B 2  134  ? 168.542 157.075 171.090 1.00 49.63  ? 134  VAL B N     1 
ATOM   11956 C  CA    . VAL B 2  134  ? 168.720 155.723 171.603 1.00 51.30  ? 134  VAL B CA    1 
ATOM   11957 C  C     . VAL B 2  134  ? 169.003 155.835 173.094 1.00 49.92  ? 134  VAL B C     1 
ATOM   11958 O  O     . VAL B 2  134  ? 169.993 156.457 173.498 1.00 49.00  ? 134  VAL B O     1 
ATOM   11959 C  CB    . VAL B 2  134  ? 169.852 154.978 170.882 1.00 49.63  ? 134  VAL B CB    1 
ATOM   11960 C  CG1   . VAL B 2  134  ? 170.061 153.613 171.499 1.00 47.11  ? 134  VAL B CG1   1 
ATOM   11961 C  CG2   . VAL B 2  134  ? 169.565 154.871 169.391 1.00 49.31  ? 134  VAL B CG2   1 
ATOM   11962 N  N     . ILE B 2  135  ? 168.138 155.240 173.914 1.00 51.86  ? 135  ILE B N     1 
ATOM   11963 C  CA    . ILE B 2  135  ? 168.349 155.138 175.356 1.00 51.48  ? 135  ILE B CA    1 
ATOM   11964 C  C     . ILE B 2  135  ? 168.175 153.681 175.760 1.00 50.82  ? 135  ILE B C     1 
ATOM   11965 O  O     . ILE B 2  135  ? 167.052 153.165 175.760 1.00 49.49  ? 135  ILE B O     1 
ATOM   11966 C  CB    . ILE B 2  135  ? 167.392 156.040 176.156 1.00 50.79  ? 135  ILE B CB    1 
ATOM   11967 C  CG1   . ILE B 2  135  ? 167.672 157.516 175.863 1.00 50.61  ? 135  ILE B CG1   1 
ATOM   11968 C  CG2   . ILE B 2  135  ? 167.497 155.754 177.639 1.00 47.61  ? 135  ILE B CG2   1 
ATOM   11969 C  CD1   . ILE B 2  135  ? 166.634 158.463 176.430 1.00 48.33  ? 135  ILE B CD1   1 
ATOM   11970 N  N     . LEU B 2  136  ? 169.275 153.027 176.120 1.00 51.26  ? 136  LEU B N     1 
ATOM   11971 C  CA    . LEU B 2  136  ? 169.267 151.615 176.471 1.00 54.18  ? 136  LEU B CA    1 
ATOM   11972 C  C     . LEU B 2  136  ? 169.514 151.439 177.963 1.00 52.20  ? 136  LEU B C     1 
ATOM   11973 O  O     . LEU B 2  136  ? 170.137 152.284 178.611 1.00 50.39  ? 136  LEU B O     1 
ATOM   11974 C  CB    . LEU B 2  136  ? 170.316 150.844 175.668 1.00 52.62  ? 136  LEU B CB    1 
ATOM   11975 C  CG    . LEU B 2  136  ? 170.215 151.053 174.158 1.00 52.32  ? 136  LEU B CG    1 
ATOM   11976 C  CD1   . LEU B 2  136  ? 171.347 150.330 173.443 1.00 52.08  ? 136  LEU B CD1   1 
ATOM   11977 C  CD2   . LEU B 2  136  ? 168.864 150.595 173.640 1.00 50.29  ? 136  LEU B CD2   1 
ATOM   11978 N  N     . THR B 2  137  ? 169.005 150.333 178.503 1.00 49.43  ? 137  THR B N     1 
ATOM   11979 C  CA    . THR B 2  137  ? 169.056 150.047 179.929 1.00 49.15  ? 137  THR B CA    1 
ATOM   11980 C  C     . THR B 2  137  ? 169.719 148.698 180.161 1.00 51.69  ? 137  THR B C     1 
ATOM   11981 O  O     . THR B 2  137  ? 169.444 147.728 179.447 1.00 52.49  ? 137  THR B O     1 
ATOM   11982 C  CB    . THR B 2  137  ? 167.652 150.043 180.546 1.00 49.84  ? 137  THR B CB    1 
ATOM   11983 O  OG1   . THR B 2  137  ? 166.896 151.145 180.027 1.00 50.18  ? 137  THR B OG1   1 
ATOM   11984 C  CG2   . THR B 2  137  ? 167.738 150.166 182.058 1.00 49.82  ? 137  THR B CG2   1 
ATOM   11985 N  N     . ALA B 2  138  ? 170.586 148.640 181.169 1.00 50.25  ? 138  ALA B N     1 
ATOM   11986 C  CA    . ALA B 2  138  ? 171.345 147.440 181.496 1.00 49.32  ? 138  ALA B CA    1 
ATOM   11987 C  C     . ALA B 2  138  ? 170.859 146.881 182.823 1.00 50.04  ? 138  ALA B C     1 
ATOM   11988 O  O     . ALA B 2  138  ? 170.876 147.584 183.837 1.00 48.44  ? 138  ALA B O     1 
ATOM   11989 C  CB    . ALA B 2  138  ? 172.843 147.741 181.571 1.00 45.30  ? 138  ALA B CB    1 
ATOM   11990 N  N     . HIS B 2  139  ? 170.443 145.619 182.816 1.00 57.74  ? 139  HIS B N     1 
ATOM   11991 C  CA    . HIS B 2  139  ? 169.963 144.938 184.009 1.00 57.38  ? 139  HIS B CA    1 
ATOM   11992 C  C     . HIS B 2  139  ? 171.012 143.944 184.483 1.00 58.21  ? 139  HIS B C     1 
ATOM   11993 O  O     . HIS B 2  139  ? 171.591 143.210 183.674 1.00 58.17  ? 139  HIS B O     1 
ATOM   11994 C  CB    . HIS B 2  139  ? 168.639 144.218 183.748 1.00 56.44  ? 139  HIS B CB    1 
ATOM   11995 C  CG    . HIS B 2  139  ? 167.525 145.131 183.346 1.00 58.15  ? 139  HIS B CG    1 
ATOM   11996 N  ND1   . HIS B 2  139  ? 167.070 146.148 184.157 1.00 57.18  ? 139  HIS B ND1   1 
ATOM   11997 C  CD2   . HIS B 2  139  ? 166.754 145.163 182.234 1.00 57.46  ? 139  HIS B CD2   1 
ATOM   11998 C  CE1   . HIS B 2  139  ? 166.082 146.781 183.553 1.00 57.96  ? 139  HIS B CE1   1 
ATOM   11999 N  NE2   . HIS B 2  139  ? 165.867 146.201 182.386 1.00 58.81  ? 139  HIS B NE2   1 
ATOM   12000 N  N     . TYR B 2  140  ? 171.261 143.934 185.787 1.00 58.33  ? 140  TYR B N     1 
ATOM   12001 C  CA    . TYR B 2  140  ? 172.205 143.019 186.402 1.00 57.78  ? 140  TYR B CA    1 
ATOM   12002 C  C     . TYR B 2  140  ? 171.453 141.883 187.094 1.00 57.60  ? 140  TYR B C     1 
ATOM   12003 O  O     . TYR B 2  140  ? 170.226 141.781 187.030 1.00 57.02  ? 140  TYR B O     1 
ATOM   12004 C  CB    . TYR B 2  140  ? 173.102 143.772 187.385 1.00 56.90  ? 140  TYR B CB    1 
ATOM   12005 C  CG    . TYR B 2  140  ? 174.072 144.723 186.725 1.00 57.77  ? 140  TYR B CG    1 
ATOM   12006 C  CD1   . TYR B 2  140  ? 173.676 145.998 186.342 1.00 56.22  ? 140  TYR B CD1   1 
ATOM   12007 C  CD2   . TYR B 2  140  ? 175.390 144.352 186.497 1.00 57.74  ? 140  TYR B CD2   1 
ATOM   12008 C  CE1   . TYR B 2  140  ? 174.565 146.872 185.742 1.00 56.68  ? 140  TYR B CE1   1 
ATOM   12009 C  CE2   . TYR B 2  140  ? 176.282 145.219 185.900 1.00 57.18  ? 140  TYR B CE2   1 
ATOM   12010 C  CZ    . TYR B 2  140  ? 175.866 146.477 185.526 1.00 57.36  ? 140  TYR B CZ    1 
ATOM   12011 O  OH    . TYR B 2  140  ? 176.757 147.338 184.931 1.00 56.68  ? 140  TYR B OH    1 
ATOM   12012 N  N     . SER B 2  141  ? 172.213 141.018 187.771 1.00 52.48  ? 141  SER B N     1 
ATOM   12013 C  CA    . SER B 2  141  ? 171.615 139.907 188.506 1.00 51.87  ? 141  SER B CA    1 
ATOM   12014 C  C     . SER B 2  141  ? 170.893 140.389 189.758 1.00 48.71  ? 141  SER B C     1 
ATOM   12015 O  O     . SER B 2  141  ? 169.817 139.881 190.096 1.00 45.34  ? 141  SER B O     1 
ATOM   12016 C  CB    . SER B 2  141  ? 172.692 138.891 188.885 1.00 50.70  ? 141  SER B CB    1 
ATOM   12017 O  OG    . SER B 2  141  ? 173.600 139.444 189.826 1.00 47.52  ? 141  SER B OG    1 
ATOM   12018 N  N     . ASN B 2  142  ? 171.479 141.357 190.466 1.00 49.84  ? 142  ASN B N     1 
ATOM   12019 C  CA    . ASN B 2  142  ? 170.951 141.756 191.766 1.00 48.36  ? 142  ASN B CA    1 
ATOM   12020 C  C     . ASN B 2  142  ? 169.669 142.568 191.629 1.00 49.19  ? 142  ASN B C     1 
ATOM   12021 O  O     . ASN B 2  142  ? 168.732 142.392 192.416 1.00 48.52  ? 142  ASN B O     1 
ATOM   12022 C  CB    . ASN B 2  142  ? 172.009 142.545 192.539 1.00 46.04  ? 142  ASN B CB    1 
ATOM   12023 C  CG    . ASN B 2  142  ? 172.537 143.738 191.760 1.00 50.26  ? 142  ASN B CG    1 
ATOM   12024 O  OD1   . ASN B 2  142  ? 172.106 144.004 190.640 1.00 51.12  ? 142  ASN B OD1   1 
ATOM   12025 N  ND2   . ASN B 2  142  ? 173.478 144.461 192.353 1.00 48.39  ? 142  ASN B ND2   1 
ATOM   12026 N  N     . GLY B 2  143  ? 169.607 143.463 190.645 1.00 46.79  ? 143  GLY B N     1 
ATOM   12027 C  CA    . GLY B 2  143  ? 168.461 144.341 190.516 1.00 44.70  ? 143  GLY B CA    1 
ATOM   12028 C  C     . GLY B 2  143  ? 168.809 145.802 190.307 1.00 46.67  ? 143  GLY B C     1 
ATOM   12029 O  O     . GLY B 2  143  ? 167.970 146.679 190.527 1.00 45.66  ? 143  GLY B O     1 
ATOM   12030 N  N     . ARG B 2  144  ? 170.051 146.081 189.919 1.00 57.09  ? 144  ARG B N     1 
ATOM   12031 C  CA    . ARG B 2  144  ? 170.482 147.438 189.617 1.00 57.00  ? 144  ARG B CA    1 
ATOM   12032 C  C     . ARG B 2  144  ? 170.519 147.672 188.107 1.00 56.52  ? 144  ARG B C     1 
ATOM   12033 O  O     . ARG B 2  144  ? 170.719 146.749 187.313 1.00 55.68  ? 144  ARG B O     1 
ATOM   12034 C  CB    . ARG B 2  144  ? 171.844 147.715 190.258 1.00 55.46  ? 144  ARG B CB    1 
ATOM   12035 C  CG    . ARG B 2  144  ? 173.027 146.959 189.669 1.00 56.03  ? 144  ARG B CG    1 
ATOM   12036 C  CD    . ARG B 2  144  ? 174.262 147.196 190.534 1.00 57.59  ? 144  ARG B CD    1 
ATOM   12037 N  NE    . ARG B 2  144  ? 175.444 146.466 190.089 1.00 58.47  ? 144  ARG B NE    1 
ATOM   12038 C  CZ    . ARG B 2  144  ? 176.432 146.997 189.380 1.00 57.51  ? 144  ARG B CZ    1 
ATOM   12039 N  NH1   . ARG B 2  144  ? 176.417 148.269 189.020 1.00 54.49  ? 144  ARG B NH1   1 
ATOM   12040 N  NH2   . ARG B 2  144  ? 177.468 146.235 189.038 1.00 56.87  ? 144  ARG B NH2   1 
ATOM   12041 N  N     . GLN B 2  145  ? 170.319 148.933 187.717 1.00 57.75  ? 145  GLN B N     1 
ATOM   12042 C  CA    . GLN B 2  145  ? 170.098 149.301 186.325 1.00 57.25  ? 145  GLN B CA    1 
ATOM   12043 C  C     . GLN B 2  145  ? 171.111 150.339 185.868 1.00 59.30  ? 145  GLN B C     1 
ATOM   12044 O  O     . GLN B 2  145  ? 171.497 151.231 186.628 1.00 59.09  ? 145  GLN B O     1 
ATOM   12045 C  CB    . GLN B 2  145  ? 168.685 149.853 186.112 1.00 55.16  ? 145  GLN B CB    1 
ATOM   12046 C  CG    . GLN B 2  145  ? 167.623 148.784 185.966 1.00 56.87  ? 145  GLN B CG    1 
ATOM   12047 C  CD    . GLN B 2  145  ? 167.238 148.167 187.296 1.00 59.69  ? 145  GLN B CD    1 
ATOM   12048 O  OE1   . GLN B 2  145  ? 167.338 148.808 188.343 1.00 59.10  ? 145  GLN B OE1   1 
ATOM   12049 N  NE2   . GLN B 2  145  ? 166.795 146.912 187.262 1.00 57.04  ? 145  GLN B NE2   1 
ATOM   12050 N  N     . GLU B 2  146  ? 171.524 150.218 184.605 1.00 54.44  ? 146  GLU B N     1 
ATOM   12051 C  CA    . GLU B 2  146  ? 172.444 151.154 183.967 1.00 50.89  ? 146  GLU B CA    1 
ATOM   12052 C  C     . GLU B 2  146  ? 171.817 151.650 182.675 1.00 52.23  ? 146  GLU B C     1 
ATOM   12053 O  O     . GLU B 2  146  ? 171.426 150.845 181.826 1.00 51.70  ? 146  GLU B O     1 
ATOM   12054 C  CB    . GLU B 2  146  ? 173.796 150.502 183.676 1.00 50.76  ? 146  GLU B CB    1 
ATOM   12055 C  CG    . GLU B 2  146  ? 174.788 151.439 183.016 1.00 52.24  ? 146  GLU B CG    1 
ATOM   12056 C  CD    . GLU B 2  146  ? 175.371 152.443 183.987 1.00 53.01  ? 146  GLU B CD    1 
ATOM   12057 O  OE1   . GLU B 2  146  ? 175.334 152.181 185.205 1.00 53.44  ? 146  GLU B OE1   1 
ATOM   12058 O  OE2   . GLU B 2  146  ? 175.860 153.497 183.533 1.00 52.65  ? 146  GLU B OE2   1 
ATOM   12059 N  N     . VAL B 2  147  ? 171.741 152.969 182.520 1.00 49.90  ? 147  VAL B N     1 
ATOM   12060 C  CA    . VAL B 2  147  ? 171.093 153.600 181.377 1.00 48.91  ? 147  VAL B CA    1 
ATOM   12061 C  C     . VAL B 2  147  ? 172.125 154.418 180.611 1.00 46.67  ? 147  VAL B C     1 
ATOM   12062 O  O     . VAL B 2  147  ? 172.815 155.263 181.194 1.00 47.09  ? 147  VAL B O     1 
ATOM   12063 C  CB    . VAL B 2  147  ? 169.911 154.478 181.824 1.00 46.83  ? 147  VAL B CB    1 
ATOM   12064 C  CG1   . VAL B 2  147  ? 169.283 155.171 180.638 1.00 43.95  ? 147  VAL B CG1   1 
ATOM   12065 C  CG2   . VAL B 2  147  ? 168.877 153.630 182.545 1.00 44.81  ? 147  VAL B CG2   1 
ATOM   12066 N  N     . LYS B 2  148  ? 172.222 154.169 179.305 1.00 48.24  ? 148  LYS B N     1 
ATOM   12067 C  CA    . LYS B 2  148  ? 173.064 154.933 178.396 1.00 48.88  ? 148  LYS B CA    1 
ATOM   12068 C  C     . LYS B 2  148  ? 172.194 155.625 177.355 1.00 50.23  ? 148  LYS B C     1 
ATOM   12069 O  O     . LYS B 2  148  ? 171.120 155.133 176.994 1.00 48.90  ? 148  LYS B O     1 
ATOM   12070 C  CB    . LYS B 2  148  ? 174.096 154.041 177.687 1.00 48.19  ? 148  LYS B CB    1 
ATOM   12071 C  CG    . LYS B 2  148  ? 175.352 153.731 178.489 1.00 47.79  ? 148  LYS B CG    1 
ATOM   12072 C  CD    . LYS B 2  148  ? 176.400 153.070 177.603 1.00 48.34  ? 148  LYS B CD    1 
ATOM   12073 C  CE    . LYS B 2  148  ? 177.655 152.698 178.382 1.00 50.73  ? 148  LYS B CE    1 
ATOM   12074 N  NZ    . LYS B 2  148  ? 178.461 153.885 178.784 1.00 49.16  ? 148  LYS B NZ    1 
ATOM   12075 N  N     . ARG B 2  149  ? 172.668 156.772 176.869 1.00 51.53  ? 149  ARG B N     1 
ATOM   12076 C  CA    . ARG B 2  149  ? 171.915 157.590 175.931 1.00 51.62  ? 149  ARG B CA    1 
ATOM   12077 C  C     . ARG B 2  149  ? 172.755 157.876 174.695 1.00 53.24  ? 149  ARG B C     1 
ATOM   12078 O  O     . ARG B 2  149  ? 173.987 157.906 174.752 1.00 51.41  ? 149  ARG B O     1 
ATOM   12079 C  CB    . ARG B 2  149  ? 171.463 158.911 176.568 1.00 50.16  ? 149  ARG B CB    1 
ATOM   12080 C  CG    . ARG B 2  149  ? 170.688 158.737 177.857 1.00 50.57  ? 149  ARG B CG    1 
ATOM   12081 C  CD    . ARG B 2  149  ? 170.234 160.070 178.420 1.00 52.85  ? 149  ARG B CD    1 
ATOM   12082 N  NE    . ARG B 2  149  ? 169.072 160.576 177.698 1.00 54.47  ? 149  ARG B NE    1 
ATOM   12083 C  CZ    . ARG B 2  149  ? 168.469 161.729 177.951 1.00 53.49  ? 149  ARG B CZ    1 
ATOM   12084 N  NH1   . ARG B 2  149  ? 168.902 162.542 178.900 1.00 52.03  ? 149  ARG B NH1   1 
ATOM   12085 N  NH2   . ARG B 2  149  ? 167.401 162.073 177.237 1.00 52.09  ? 149  ARG B NH2   1 
ATOM   12086 N  N     . ALA B 2  150  ? 172.071 158.078 173.570 1.00 50.21  ? 150  ALA B N     1 
ATOM   12087 C  CA    . ALA B 2  150  ? 172.729 158.342 172.300 1.00 48.26  ? 150  ALA B CA    1 
ATOM   12088 C  C     . ALA B 2  150  ? 171.870 159.284 171.473 1.00 49.62  ? 150  ALA B C     1 
ATOM   12089 O  O     . ALA B 2  150  ? 170.670 159.055 171.303 1.00 48.33  ? 150  ALA B O     1 
ATOM   12090 C  CB    . ALA B 2  150  ? 172.984 157.049 171.517 1.00 46.10  ? 150  ALA B CB    1 
ATOM   12091 N  N     . SER B 2  151  ? 172.497 160.332 170.949 1.00 44.77  ? 151  SER B N     1 
ATOM   12092 C  CA    . SER B 2  151  ? 171.842 161.294 170.078 1.00 43.17  ? 151  SER B CA    1 
ATOM   12093 C  C     . SER B 2  151  ? 172.374 161.135 168.662 1.00 45.56  ? 151  SER B C     1 
ATOM   12094 O  O     . SER B 2  151  ? 173.589 161.098 168.446 1.00 46.01  ? 151  SER B O     1 
ATOM   12095 C  CB    . SER B 2  151  ? 172.073 162.725 170.564 1.00 40.86  ? 151  SER B CB    1 
ATOM   12096 O  OG    . SER B 2  151  ? 171.471 163.663 169.693 1.00 40.76  ? 151  SER B OG    1 
ATOM   12097 N  N     . ILE B 2  152  ? 171.463 161.042 167.699 1.00 44.92  ? 152  ILE B N     1 
ATOM   12098 C  CA    . ILE B 2  152  ? 171.803 160.835 166.299 1.00 43.64  ? 152  ILE B CA    1 
ATOM   12099 C  C     . ILE B 2  152  ? 171.414 162.091 165.532 1.00 42.51  ? 152  ILE B C     1 
ATOM   12100 O  O     . ILE B 2  152  ? 170.317 162.612 165.735 1.00 41.10  ? 152  ILE B O     1 
ATOM   12101 C  CB    . ILE B 2  152  ? 171.111 159.599 165.696 1.00 42.57  ? 152  ILE B CB    1 
ATOM   12102 C  CG1   . ILE B 2  152  ? 171.433 158.353 166.527 1.00 41.37  ? 152  ILE B CG1   1 
ATOM   12103 C  CG2   . ILE B 2  152  ? 171.542 159.396 164.259 1.00 40.02  ? 152  ILE B CG2   1 
ATOM   12104 C  CD1   . ILE B 2  152  ? 170.508 157.188 166.273 1.00 41.33  ? 152  ILE B CD1   1 
ATOM   12105 N  N     . PRO B 2  153  ? 172.286 162.624 164.681 1.00 43.75  ? 153  PRO B N     1 
ATOM   12106 C  CA    . PRO B 2  153  ? 171.918 163.763 163.835 1.00 43.18  ? 153  PRO B CA    1 
ATOM   12107 C  C     . PRO B 2  153  ? 170.970 163.334 162.728 1.00 45.76  ? 153  PRO B C     1 
ATOM   12108 O  O     . PRO B 2  153  ? 170.670 162.137 162.594 1.00 43.52  ? 153  PRO B O     1 
ATOM   12109 C  CB    . PRO B 2  153  ? 173.271 164.228 163.268 1.00 42.20  ? 153  PRO B CB    1 
ATOM   12110 C  CG    . PRO B 2  153  ? 174.312 163.564 164.115 1.00 41.85  ? 153  PRO B CG    1 
ATOM   12111 C  CD    . PRO B 2  153  ? 173.709 162.279 164.551 1.00 41.72  ? 153  PRO B CD    1 
ATOM   12112 N  N     . PRO B 2  154  ? 170.470 164.275 161.923 1.00 48.30  ? 154  PRO B N     1 
ATOM   12113 C  CA    . PRO B 2  154  ? 169.560 163.908 160.829 1.00 45.33  ? 154  PRO B CA    1 
ATOM   12114 C  C     . PRO B 2  154  ? 170.171 162.888 159.881 1.00 45.35  ? 154  PRO B C     1 
ATOM   12115 O  O     . PRO B 2  154  ? 171.367 162.921 159.585 1.00 47.31  ? 154  PRO B O     1 
ATOM   12116 C  CB    . PRO B 2  154  ? 169.305 165.244 160.129 1.00 44.84  ? 154  PRO B CB    1 
ATOM   12117 C  CG    . PRO B 2  154  ? 169.418 166.243 161.213 1.00 46.81  ? 154  PRO B CG    1 
ATOM   12118 C  CD    . PRO B 2  154  ? 170.457 165.729 162.172 1.00 45.18  ? 154  PRO B CD    1 
ATOM   12119 N  N     . PHE B 2  155  ? 169.328 161.979 159.397 1.00 48.16  ? 155  PHE B N     1 
ATOM   12120 C  CA    . PHE B 2  155  ? 169.787 160.818 158.644 1.00 50.49  ? 155  PHE B CA    1 
ATOM   12121 C  C     . PHE B 2  155  ? 168.689 160.379 157.684 1.00 52.93  ? 155  PHE B C     1 
ATOM   12122 O  O     . PHE B 2  155  ? 167.538 160.202 158.095 1.00 50.68  ? 155  PHE B O     1 
ATOM   12123 C  CB    . PHE B 2  155  ? 170.177 159.701 159.618 1.00 47.30  ? 155  PHE B CB    1 
ATOM   12124 C  CG    . PHE B 2  155  ? 170.022 158.317 159.072 1.00 49.60  ? 155  PHE B CG    1 
ATOM   12125 C  CD1   . PHE B 2  155  ? 170.758 157.894 157.979 1.00 49.91  ? 155  PHE B CD1   1 
ATOM   12126 C  CD2   . PHE B 2  155  ? 169.161 157.422 159.683 1.00 48.66  ? 155  PHE B CD2   1 
ATOM   12127 C  CE1   . PHE B 2  155  ? 170.618 156.612 157.493 1.00 51.07  ? 155  PHE B CE1   1 
ATOM   12128 C  CE2   . PHE B 2  155  ? 169.017 156.141 159.207 1.00 50.42  ? 155  PHE B CE2   1 
ATOM   12129 C  CZ    . PHE B 2  155  ? 169.745 155.731 158.109 1.00 51.37  ? 155  PHE B CZ    1 
ATOM   12130 N  N     . GLN B 2  156  ? 169.048 160.208 156.411 1.00 52.01  ? 156  GLN B N     1 
ATOM   12131 C  CA    . GLN B 2  156  ? 168.101 159.819 155.369 1.00 52.23  ? 156  GLN B CA    1 
ATOM   12132 C  C     . GLN B 2  156  ? 167.730 158.349 155.525 1.00 53.63  ? 156  GLN B C     1 
ATOM   12133 O  O     . GLN B 2  156  ? 168.574 157.468 155.343 1.00 54.21  ? 156  GLN B O     1 
ATOM   12134 C  CB    . GLN B 2  156  ? 168.710 160.081 153.994 1.00 51.65  ? 156  GLN B CB    1 
ATOM   12135 C  CG    . GLN B 2  156  ? 167.794 159.770 152.813 1.00 50.92  ? 156  GLN B CG    1 
ATOM   12136 C  CD    . GLN B 2  156  ? 168.453 160.052 151.469 1.00 54.93  ? 156  GLN B CD    1 
ATOM   12137 O  OE1   . GLN B 2  156  ? 169.541 160.632 151.405 1.00 54.61  ? 156  GLN B OE1   1 
ATOM   12138 N  NE2   . GLN B 2  156  ? 167.810 159.617 150.391 1.00 54.90  ? 156  GLN B NE2   1 
ATOM   12139 N  N     . VAL B 2  157  ? 166.465 158.076 155.839 1.00 44.21  ? 157  VAL B N     1 
ATOM   12140 C  CA    . VAL B 2  157  ? 166.017 156.695 156.000 1.00 42.62  ? 157  VAL B CA    1 
ATOM   12141 C  C     . VAL B 2  157  ? 165.754 156.045 154.646 1.00 43.16  ? 157  VAL B C     1 
ATOM   12142 O  O     . VAL B 2  157  ? 166.234 154.940 154.368 1.00 44.18  ? 157  VAL B O     1 
ATOM   12143 C  CB    . VAL B 2  157  ? 164.772 156.632 156.902 1.00 44.73  ? 157  VAL B CB    1 
ATOM   12144 C  CG1   . VAL B 2  157  ? 164.036 155.322 156.690 1.00 43.27  ? 157  VAL B CG1   1 
ATOM   12145 C  CG2   . VAL B 2  157  ? 165.177 156.762 158.343 1.00 42.50  ? 157  VAL B CG2   1 
ATOM   12146 N  N     . SER B 2  158  ? 164.974 156.706 153.793 1.00 43.08  ? 158  SER B N     1 
ATOM   12147 C  CA    . SER B 2  158  ? 164.641 156.142 152.491 1.00 44.05  ? 158  SER B CA    1 
ATOM   12148 C  C     . SER B 2  158  ? 164.036 157.225 151.612 1.00 43.49  ? 158  SER B C     1 
ATOM   12149 O  O     . SER B 2  158  ? 164.157 158.422 151.883 1.00 41.11  ? 158  SER B O     1 
ATOM   12150 C  CB    . SER B 2  158  ? 163.677 154.957 152.618 1.00 40.30  ? 158  SER B CB    1 
ATOM   12151 O  OG    . SER B 2  158  ? 163.475 154.335 151.359 1.00 42.36  ? 158  SER B OG    1 
ATOM   12152 N  N     . THR B 2  159  ? 163.404 156.778 150.531 1.00 42.15  ? 159  THR B N     1 
ATOM   12153 C  CA    . THR B 2  159  ? 162.696 157.643 149.598 1.00 39.11  ? 159  THR B CA    1 
ATOM   12154 C  C     . THR B 2  159  ? 161.222 157.265 149.580 1.00 41.88  ? 159  THR B C     1 
ATOM   12155 O  O     . THR B 2  159  ? 160.880 156.078 149.596 1.00 40.94  ? 159  THR B O     1 
ATOM   12156 C  CB    . THR B 2  159  ? 163.285 157.532 148.191 1.00 40.31  ? 159  THR B CB    1 
ATOM   12157 O  OG1   . THR B 2  159  ? 163.365 156.152 147.813 1.00 40.69  ? 159  THR B OG1   1 
ATOM   12158 C  CG2   . THR B 2  159  ? 164.664 158.160 148.128 1.00 38.75  ? 159  THR B CG2   1 
ATOM   12159 N  N     . PHE B 2  160  ? 160.356 158.274 149.549 1.00 44.90  ? 160  PHE B N     1 
ATOM   12160 C  CA    . PHE B 2  160  ? 158.918 158.070 149.518 1.00 42.05  ? 160  PHE B CA    1 
ATOM   12161 C  C     . PHE B 2  160  ? 158.366 158.519 148.177 1.00 43.69  ? 160  PHE B C     1 
ATOM   12162 O  O     . PHE B 2  160  ? 158.726 159.604 147.704 1.00 41.05  ? 160  PHE B O     1 
ATOM   12163 C  CB    . PHE B 2  160  ? 158.244 158.854 150.647 1.00 41.19  ? 160  PHE B CB    1 
ATOM   12164 C  CG    . PHE B 2  160  ? 156.891 158.335 151.021 1.00 44.25  ? 160  PHE B CG    1 
ATOM   12165 C  CD1   . PHE B 2  160  ? 156.739 157.045 151.495 1.00 43.82  ? 160  PHE B CD1   1 
ATOM   12166 C  CD2   . PHE B 2  160  ? 155.772 159.135 150.906 1.00 45.76  ? 160  PHE B CD2   1 
ATOM   12167 C  CE1   . PHE B 2  160  ? 155.501 156.566 151.841 1.00 44.18  ? 160  PHE B CE1   1 
ATOM   12168 C  CE2   . PHE B 2  160  ? 154.533 158.659 151.254 1.00 44.58  ? 160  PHE B CE2   1 
ATOM   12169 C  CZ    . PHE B 2  160  ? 154.396 157.376 151.722 1.00 45.17  ? 160  PHE B CZ    1 
ATOM   12170 N  N     . PRO B 2  161  ? 157.516 157.722 147.530 1.00 45.42  ? 161  PRO B N     1 
ATOM   12171 C  CA    . PRO B 2  161  ? 156.964 158.137 146.235 1.00 42.03  ? 161  PRO B CA    1 
ATOM   12172 C  C     . PRO B 2  161  ? 156.173 159.429 146.362 1.00 42.56  ? 161  PRO B C     1 
ATOM   12173 O  O     . PRO B 2  161  ? 155.491 159.668 147.358 1.00 43.33  ? 161  PRO B O     1 
ATOM   12174 C  CB    . PRO B 2  161  ? 156.064 156.968 145.827 1.00 43.18  ? 161  PRO B CB    1 
ATOM   12175 C  CG    . PRO B 2  161  ? 156.295 155.883 146.798 1.00 44.92  ? 161  PRO B CG    1 
ATOM   12176 C  CD    . PRO B 2  161  ? 157.172 156.340 147.894 1.00 44.74  ? 161  PRO B CD    1 
ATOM   12177 N  N     . ILE B 2  162  ? 156.258 160.259 145.329 1.00 40.35  ? 162  ILE B N     1 
ATOM   12178 C  CA    . ILE B 2  162  ? 155.693 161.600 145.346 1.00 38.25  ? 162  ILE B CA    1 
ATOM   12179 C  C     . ILE B 2  162  ? 154.619 161.678 144.270 1.00 39.63  ? 162  ILE B C     1 
ATOM   12180 O  O     . ILE B 2  162  ? 154.816 161.181 143.154 1.00 41.77  ? 162  ILE B O     1 
ATOM   12181 C  CB    . ILE B 2  162  ? 156.787 162.658 145.135 1.00 39.02  ? 162  ILE B CB    1 
ATOM   12182 C  CG1   . ILE B 2  162  ? 157.655 162.740 146.391 1.00 42.97  ? 162  ILE B CG1   1 
ATOM   12183 C  CG2   . ILE B 2  162  ? 156.189 164.003 144.786 1.00 37.86  ? 162  ILE B CG2   1 
ATOM   12184 C  CD1   . ILE B 2  162  ? 157.135 163.649 147.461 1.00 43.08  ? 162  ILE B CD1   1 
ATOM   12185 N  N     . MET B 2  163  ? 153.474 162.265 144.614 1.00 35.72  ? 163  MET B N     1 
ATOM   12186 C  CA    . MET B 2  163  ? 152.372 162.393 143.671 1.00 36.19  ? 163  MET B CA    1 
ATOM   12187 C  C     . MET B 2  163  ? 152.558 163.619 142.788 1.00 34.96  ? 163  MET B C     1 
ATOM   12188 O  O     . MET B 2  163  ? 152.923 164.696 143.265 1.00 35.46  ? 163  MET B O     1 
ATOM   12189 C  CB    . MET B 2  163  ? 151.039 162.471 144.415 1.00 33.96  ? 163  MET B CB    1 
ATOM   12190 C  CG    . MET B 2  163  ? 150.017 163.403 143.795 1.00 35.38  ? 163  MET B CG    1 
ATOM   12191 S  SD    . MET B 2  163  ? 148.466 163.477 144.692 1.00 37.79  ? 163  MET B SD    1 
ATOM   12192 C  CE    . MET B 2  163  ? 148.059 161.742 144.748 1.00 30.92  ? 163  MET B CE    1 
ATOM   12193 N  N     . ARG B 2  164  ? 152.319 163.442 141.491 1.00 29.64  ? 164  ARG B N     1 
ATOM   12194 C  CA    . ARG B 2  164  ? 152.402 164.549 140.550 1.00 34.32  ? 164  ARG B CA    1 
ATOM   12195 C  C     . ARG B 2  164  ? 151.323 165.585 140.836 1.00 34.48  ? 164  ARG B C     1 
ATOM   12196 O  O     . ARG B 2  164  ? 150.187 165.248 141.169 1.00 32.46  ? 164  ARG B O     1 
ATOM   12197 C  CB    . ARG B 2  164  ? 152.265 164.040 139.118 1.00 36.24  ? 164  ARG B CB    1 
ATOM   12198 C  CG    . ARG B 2  164  ? 153.518 164.176 138.279 1.00 35.65  ? 164  ARG B CG    1 
ATOM   12199 C  CD    . ARG B 2  164  ? 153.597 165.558 137.682 1.00 34.91  ? 164  ARG B CD    1 
ATOM   12200 N  NE    . ARG B 2  164  ? 152.550 165.768 136.694 1.00 37.99  ? 164  ARG B NE    1 
ATOM   12201 C  CZ    . ARG B 2  164  ? 152.063 166.952 136.352 1.00 38.30  ? 164  ARG B CZ    1 
ATOM   12202 N  NH1   . ARG B 2  164  ? 152.515 168.068 136.894 1.00 40.00  ? 164  ARG B NH1   1 
ATOM   12203 N  NH2   . ARG B 2  164  ? 151.098 167.017 135.443 1.00 35.62  ? 164  ARG B NH2   1 
ATOM   12204 N  N     . GLY B 2  165  ? 151.685 166.856 140.696 1.00 31.10  ? 165  GLY B N     1 
ATOM   12205 C  CA    . GLY B 2  165  ? 150.776 167.937 141.003 1.00 32.11  ? 165  GLY B CA    1 
ATOM   12206 C  C     . GLY B 2  165  ? 150.643 168.255 142.472 1.00 32.91  ? 165  GLY B C     1 
ATOM   12207 O  O     . GLY B 2  165  ? 149.835 169.117 142.834 1.00 31.27  ? 165  GLY B O     1 
ATOM   12208 N  N     . SER B 2  166  ? 151.416 167.596 143.328 1.00 37.74  ? 166  SER B N     1 
ATOM   12209 C  CA    . SER B 2  166  ? 151.322 167.769 144.767 1.00 36.63  ? 166  SER B CA    1 
ATOM   12210 C  C     . SER B 2  166  ? 152.289 168.858 145.221 1.00 39.27  ? 166  SER B C     1 
ATOM   12211 O  O     . SER B 2  166  ? 153.014 169.450 144.419 1.00 43.18  ? 166  SER B O     1 
ATOM   12212 C  CB    . SER B 2  166  ? 151.590 166.444 145.466 1.00 32.89  ? 166  SER B CB    1 
ATOM   12213 O  OG    . SER B 2  166  ? 152.891 165.985 145.156 1.00 35.92  ? 166  SER B OG    1 
ATOM   12214 N  N     . ASN B 2  167  ? 152.313 169.125 146.526 1.00 44.23  ? 167  ASN B N     1 
ATOM   12215 C  CA    . ASN B 2  167  ? 153.123 170.224 147.039 1.00 46.03  ? 167  ASN B CA    1 
ATOM   12216 C  C     . ASN B 2  167  ? 154.614 169.920 146.960 1.00 45.54  ? 167  ASN B C     1 
ATOM   12217 O  O     . ASN B 2  167  ? 155.422 170.838 146.788 1.00 43.98  ? 167  ASN B O     1 
ATOM   12218 C  CB    . ASN B 2  167  ? 152.709 170.545 148.475 1.00 44.41  ? 167  ASN B CB    1 
ATOM   12219 C  CG    . ASN B 2  167  ? 153.448 171.731 149.038 1.00 46.42  ? 167  ASN B CG    1 
ATOM   12220 O  OD1   . ASN B 2  167  ? 154.445 171.581 149.741 1.00 47.17  ? 167  ASN B OD1   1 
ATOM   12221 N  ND2   . ASN B 2  167  ? 152.975 172.925 148.713 1.00 45.55  ? 167  ASN B ND2   1 
ATOM   12222 N  N     . ARG B 2  168  ? 154.997 168.652 147.074 1.00 47.75  ? 168  ARG B N     1 
ATOM   12223 C  CA    . ARG B 2  168  ? 156.395 168.244 147.015 1.00 49.25  ? 168  ARG B CA    1 
ATOM   12224 C  C     . ARG B 2  168  ? 156.868 167.930 145.601 1.00 49.43  ? 168  ARG B C     1 
ATOM   12225 O  O     . ARG B 2  168  ? 157.979 167.421 145.438 1.00 50.65  ? 168  ARG B O     1 
ATOM   12226 C  CB    . ARG B 2  168  ? 156.623 167.021 147.904 1.00 48.85  ? 168  ARG B CB    1 
ATOM   12227 C  CG    . ARG B 2  168  ? 156.346 167.242 149.381 1.00 47.78  ? 168  ARG B CG    1 
ATOM   12228 C  CD    . ARG B 2  168  ? 157.403 168.106 150.043 1.00 50.15  ? 168  ARG B CD    1 
ATOM   12229 N  NE    . ARG B 2  168  ? 157.101 168.317 151.453 1.00 50.77  ? 168  ARG B NE    1 
ATOM   12230 C  CZ    . ARG B 2  168  ? 156.481 169.385 151.934 1.00 50.63  ? 168  ARG B CZ    1 
ATOM   12231 N  NH1   . ARG B 2  168  ? 156.109 170.380 151.149 1.00 50.27  ? 168  ARG B NH1   1 
ATOM   12232 N  NH2   . ARG B 2  168  ? 156.231 169.458 153.238 1.00 47.04  ? 168  ARG B NH2   1 
ATOM   12233 N  N     . CYS B 2  169  ? 156.045 168.179 144.589 1.00 49.05  ? 169  CYS B N     1 
ATOM   12234 C  CA    . CYS B 2  169  ? 156.413 167.965 143.199 1.00 46.71  ? 169  CYS B CA    1 
ATOM   12235 C  C     . CYS B 2  169  ? 157.075 169.212 142.633 1.00 48.14  ? 169  CYS B C     1 
ATOM   12236 O  O     . CYS B 2  169  ? 156.819 170.332 143.083 1.00 50.52  ? 169  CYS B O     1 
ATOM   12237 C  CB    . CYS B 2  169  ? 155.181 167.607 142.367 1.00 47.21  ? 169  CYS B CB    1 
ATOM   12238 S  SG    . CYS B 2  169  ? 155.507 167.113 140.663 1.00 56.77  ? 169  CYS B SG    1 
ATOM   12239 N  N     . HIS B 2  170  ? 157.939 169.008 141.634 1.00 41.48  ? 170  HIS B N     1 
ATOM   12240 C  CA    . HIS B 2  170  ? 158.570 170.144 140.973 1.00 41.58  ? 170  HIS B CA    1 
ATOM   12241 C  C     . HIS B 2  170  ? 157.572 170.958 140.164 1.00 45.15  ? 170  HIS B C     1 
ATOM   12242 O  O     . HIS B 2  170  ? 157.750 172.171 140.009 1.00 44.03  ? 170  HIS B O     1 
ATOM   12243 C  CB    . HIS B 2  170  ? 159.708 169.676 140.073 1.00 41.12  ? 170  HIS B CB    1 
ATOM   12244 C  CG    . HIS B 2  170  ? 160.842 169.047 140.813 1.00 43.49  ? 170  HIS B CG    1 
ATOM   12245 N  ND1   . HIS B 2  170  ? 161.208 169.436 142.082 1.00 45.72  ? 170  HIS B ND1   1 
ATOM   12246 C  CD2   . HIS B 2  170  ? 161.700 168.065 140.459 1.00 44.10  ? 170  HIS B CD2   1 
ATOM   12247 C  CE1   . HIS B 2  170  ? 162.239 168.715 142.480 1.00 44.34  ? 170  HIS B CE1   1 
ATOM   12248 N  NE2   . HIS B 2  170  ? 162.556 167.873 141.514 1.00 44.60  ? 170  HIS B NE2   1 
ATOM   12249 N  N     . THR B 2  171  ? 156.529 170.322 139.640 1.00 46.24  ? 171  THR B N     1 
ATOM   12250 C  CA    . THR B 2  171  ? 155.513 171.024 138.858 1.00 45.51  ? 171  THR B CA    1 
ATOM   12251 C  C     . THR B 2  171  ? 154.430 171.612 139.754 1.00 45.68  ? 171  THR B C     1 
ATOM   12252 O  O     . THR B 2  171  ? 153.238 171.386 139.560 1.00 47.70  ? 171  THR B O     1 
ATOM   12253 C  CB    . THR B 2  171  ? 154.909 170.089 137.817 1.00 43.49  ? 171  THR B CB    1 
ATOM   12254 O  OG1   . THR B 2  171  ? 154.317 168.961 138.473 1.00 40.32  ? 171  THR B OG1   1 
ATOM   12255 C  CG2   . THR B 2  171  ? 155.967 169.610 136.825 1.00 42.74  ? 171  THR B CG2   1 
ATOM   12256 N  N     . HIS B 2  172  ? 154.850 172.375 140.754 1.00 51.38  ? 172  HIS B N     1 
ATOM   12257 C  CA    . HIS B 2  172  ? 153.934 173.086 141.635 1.00 50.33  ? 172  HIS B CA    1 
ATOM   12258 C  C     . HIS B 2  172  ? 154.158 174.590 141.612 1.00 52.23  ? 172  HIS B C     1 
ATOM   12259 O  O     . HIS B 2  172  ? 153.188 175.351 141.583 1.00 52.00  ? 172  HIS B O     1 
ATOM   12260 C  CB    . HIS B 2  172  ? 154.066 172.536 143.068 1.00 49.09  ? 172  HIS B CB    1 
ATOM   12261 C  CG    . HIS B 2  172  ? 153.157 173.188 144.063 1.00 51.98  ? 172  HIS B CG    1 
ATOM   12262 N  ND1   . HIS B 2  172  ? 152.120 172.514 144.670 1.00 51.05  ? 172  HIS B ND1   1 
ATOM   12263 C  CD2   . HIS B 2  172  ? 153.149 174.437 144.586 1.00 50.80  ? 172  HIS B CD2   1 
ATOM   12264 C  CE1   . HIS B 2  172  ? 151.495 173.326 145.502 1.00 50.66  ? 172  HIS B CE1   1 
ATOM   12265 N  NE2   . HIS B 2  172  ? 152.101 174.499 145.472 1.00 52.65  ? 172  HIS B NE2   1 
ATOM   12266 N  N     . HIS B 2  173  ? 155.415 175.041 141.612 1.00 57.16  ? 173  HIS B N     1 
ATOM   12267 C  CA    . HIS B 2  173  ? 155.739 176.444 141.378 1.00 56.67  ? 173  HIS B CA    1 
ATOM   12268 C  C     . HIS B 2  173  ? 155.651 176.835 139.909 1.00 57.52  ? 173  HIS B C     1 
ATOM   12269 O  O     . HIS B 2  173  ? 155.468 178.021 139.611 1.00 58.56  ? 173  HIS B O     1 
ATOM   12270 C  CB    . HIS B 2  173  ? 157.156 176.765 141.864 1.00 56.34  ? 173  HIS B CB    1 
ATOM   12271 C  CG    . HIS B 2  173  ? 157.374 176.536 143.326 1.00 57.94  ? 173  HIS B CG    1 
ATOM   12272 N  ND1   . HIS B 2  173  ? 157.491 175.277 143.874 1.00 57.77  ? 173  HIS B ND1   1 
ATOM   12273 C  CD2   . HIS B 2  173  ? 157.558 177.409 144.345 1.00 57.33  ? 173  HIS B CD2   1 
ATOM   12274 C  CE1   . HIS B 2  173  ? 157.702 175.384 145.174 1.00 58.54  ? 173  HIS B CE1   1 
ATOM   12275 N  NE2   . HIS B 2  173  ? 157.750 176.667 145.484 1.00 58.16  ? 173  HIS B NE2   1 
ATOM   12276 N  N     . LEU B 2  174  ? 155.785 175.878 138.995 1.00 51.07  ? 174  LEU B N     1 
ATOM   12277 C  CA    . LEU B 2  174  ? 155.827 176.146 137.566 1.00 47.36  ? 174  LEU B CA    1 
ATOM   12278 C  C     . LEU B 2  174  ? 154.456 176.580 137.084 1.00 47.29  ? 174  LEU B C     1 
ATOM   12279 O  O     . LEU B 2  174  ? 153.434 176.100 137.586 1.00 47.26  ? 174  LEU B O     1 
ATOM   12280 C  CB    . LEU B 2  174  ? 156.271 174.911 136.786 1.00 45.61  ? 174  LEU B CB    1 
ATOM   12281 C  CG    . LEU B 2  174  ? 157.639 174.344 137.121 1.00 47.05  ? 174  LEU B CG    1 
ATOM   12282 C  CD1   . LEU B 2  174  ? 157.828 173.069 136.353 1.00 44.71  ? 174  LEU B CD1   1 
ATOM   12283 C  CD2   . LEU B 2  174  ? 158.716 175.356 136.769 1.00 47.00  ? 174  LEU B CD2   1 
ATOM   12284 N  N     . SER B 2  175  ? 154.440 177.486 136.117 1.00 42.61  ? 175  SER B N     1 
ATOM   12285 C  CA    . SER B 2  175  ? 153.206 177.906 135.481 1.00 40.83  ? 175  SER B CA    1 
ATOM   12286 C  C     . SER B 2  175  ? 152.971 177.060 134.234 1.00 43.54  ? 175  SER B C     1 
ATOM   12287 O  O     . SER B 2  175  ? 153.673 176.079 133.973 1.00 43.63  ? 175  SER B O     1 
ATOM   12288 C  CB    . SER B 2  175  ? 153.253 179.395 135.159 1.00 41.88  ? 175  SER B CB    1 
ATOM   12289 O  OG    . SER B 2  175  ? 153.380 180.164 136.343 1.00 44.85  ? 175  SER B OG    1 
ATOM   12290 N  N     . LYS B 2  176  ? 151.964 177.442 133.452 1.00 46.43  ? 176  LYS B N     1 
ATOM   12291 C  CA    . LYS B 2  176  ? 151.607 176.682 132.262 1.00 45.33  ? 176  LYS B CA    1 
ATOM   12292 C  C     . LYS B 2  176  ? 152.713 176.754 131.214 1.00 42.79  ? 176  LYS B C     1 
ATOM   12293 O  O     . LYS B 2  176  ? 153.072 175.743 130.600 1.00 41.37  ? 176  LYS B O     1 
ATOM   12294 C  CB    . LYS B 2  176  ? 150.278 177.209 131.725 1.00 42.54  ? 176  LYS B CB    1 
ATOM   12295 C  CG    . LYS B 2  176  ? 149.771 176.569 130.466 1.00 43.58  ? 176  LYS B CG    1 
ATOM   12296 C  CD    . LYS B 2  176  ? 148.335 177.003 130.233 1.00 44.85  ? 176  LYS B CD    1 
ATOM   12297 C  CE    . LYS B 2  176  ? 148.240 178.512 130.067 1.00 44.97  ? 176  LYS B CE    1 
ATOM   12298 N  NZ    . LYS B 2  176  ? 146.847 178.964 129.800 1.00 44.53  ? 176  LYS B NZ    1 
ATOM   12299 N  N     . THR B 2  177  ? 153.278 177.945 131.011 1.00 37.30  ? 177  THR B N     1 
ATOM   12300 C  CA    . THR B 2  177  ? 154.372 178.093 130.057 1.00 41.53  ? 177  THR B CA    1 
ATOM   12301 C  C     . THR B 2  177  ? 155.604 177.317 130.507 1.00 43.15  ? 177  THR B C     1 
ATOM   12302 O  O     . THR B 2  177  ? 156.268 176.664 129.698 1.00 40.37  ? 177  THR B O     1 
ATOM   12303 C  CB    . THR B 2  177  ? 154.705 179.572 129.862 1.00 41.54  ? 177  THR B CB    1 
ATOM   12304 O  OG1   . THR B 2  177  ? 153.569 180.248 129.312 1.00 40.93  ? 177  THR B OG1   1 
ATOM   12305 C  CG2   . THR B 2  177  ? 155.879 179.733 128.913 1.00 37.79  ? 177  THR B CG2   1 
ATOM   12306 N  N     . ALA B 2  178  ? 155.922 177.368 131.802 1.00 43.13  ? 178  ALA B N     1 
ATOM   12307 C  CA    . ALA B 2  178  ? 157.073 176.626 132.306 1.00 41.73  ? 178  ALA B CA    1 
ATOM   12308 C  C     . ALA B 2  178  ? 156.860 175.118 132.206 1.00 43.39  ? 178  ALA B C     1 
ATOM   12309 O  O     . ALA B 2  178  ? 157.773 174.384 131.805 1.00 43.19  ? 178  ALA B O     1 
ATOM   12310 C  CB    . ALA B 2  178  ? 157.367 177.037 133.745 1.00 41.00  ? 178  ALA B CB    1 
ATOM   12311 N  N     . LYS B 2  179  ? 155.666 174.638 132.567 1.00 41.29  ? 179  LYS B N     1 
ATOM   12312 C  CA    . LYS B 2  179  ? 155.367 173.213 132.438 1.00 41.65  ? 179  LYS B CA    1 
ATOM   12313 C  C     . LYS B 2  179  ? 155.468 172.764 130.989 1.00 44.40  ? 179  LYS B C     1 
ATOM   12314 O  O     . LYS B 2  179  ? 155.976 171.676 130.699 1.00 42.71  ? 179  LYS B O     1 
ATOM   12315 C  CB    . LYS B 2  179  ? 153.970 172.914 132.977 1.00 41.62  ? 179  LYS B CB    1 
ATOM   12316 C  CG    . LYS B 2  179  ? 153.854 172.843 134.480 1.00 43.45  ? 179  LYS B CG    1 
ATOM   12317 C  CD    . LYS B 2  179  ? 152.392 172.840 134.896 1.00 42.56  ? 179  LYS B CD    1 
ATOM   12318 C  CE    . LYS B 2  179  ? 151.664 171.649 134.306 1.00 44.53  ? 179  LYS B CE    1 
ATOM   12319 N  NZ    . LYS B 2  179  ? 150.249 171.576 134.751 1.00 43.89  ? 179  LYS B NZ    1 
ATOM   12320 N  N     . LYS B 2  180  ? 154.970 173.589 130.068 1.00 45.44  ? 180  LYS B N     1 
ATOM   12321 C  CA    . LYS B 2  180  ? 155.079 173.292 128.645 1.00 44.24  ? 180  LYS B CA    1 
ATOM   12322 C  C     . LYS B 2  180  ? 156.533 173.304 128.188 1.00 43.07  ? 180  LYS B C     1 
ATOM   12323 O  O     . LYS B 2  180  ? 156.919 172.536 127.303 1.00 45.40  ? 180  LYS B O     1 
ATOM   12324 C  CB    . LYS B 2  180  ? 154.243 174.307 127.864 1.00 42.98  ? 180  LYS B CB    1 
ATOM   12325 C  CG    . LYS B 2  180  ? 154.353 174.256 126.362 1.00 41.74  ? 180  LYS B CG    1 
ATOM   12326 C  CD    . LYS B 2  180  ? 153.318 175.182 125.748 1.00 42.66  ? 180  LYS B CD    1 
ATOM   12327 C  CE    . LYS B 2  180  ? 153.466 176.593 126.304 1.00 46.41  ? 180  LYS B CE    1 
ATOM   12328 N  NZ    . LYS B 2  180  ? 152.410 177.538 125.847 1.00 44.41  ? 180  LYS B NZ    1 
ATOM   12329 N  N     . GLU B 2  181  ? 157.352 174.171 128.781 1.00 46.74  ? 181  GLU B N     1 
ATOM   12330 C  CA    . GLU B 2  181  ? 158.738 174.300 128.349 1.00 50.13  ? 181  GLU B CA    1 
ATOM   12331 C  C     . GLU B 2  181  ? 159.588 173.128 128.828 1.00 50.48  ? 181  GLU B C     1 
ATOM   12332 O  O     . GLU B 2  181  ? 160.520 172.709 128.132 1.00 49.43  ? 181  GLU B O     1 
ATOM   12333 C  CB    . GLU B 2  181  ? 159.315 175.627 128.844 1.00 48.90  ? 181  GLU B CB    1 
ATOM   12334 C  CG    . GLU B 2  181  ? 158.892 176.827 128.006 1.00 49.32  ? 181  GLU B CG    1 
ATOM   12335 C  CD    . GLU B 2  181  ? 159.314 178.158 128.609 1.00 51.67  ? 181  GLU B CD    1 
ATOM   12336 O  OE1   . GLU B 2  181  ? 159.841 178.170 129.744 1.00 50.05  ? 181  GLU B OE1   1 
ATOM   12337 O  OE2   . GLU B 2  181  ? 159.108 179.196 127.949 1.00 51.37  ? 181  GLU B OE2   1 
ATOM   12338 N  N     . ILE B 2  182  ? 159.301 172.597 130.021 1.00 42.11  ? 182  ILE B N     1 
ATOM   12339 C  CA    . ILE B 2  182  ? 160.145 171.539 130.573 1.00 41.18  ? 182  ILE B CA    1 
ATOM   12340 C  C     . ILE B 2  182  ? 159.726 170.141 130.146 1.00 42.66  ? 182  ILE B C     1 
ATOM   12341 O  O     . ILE B 2  182  ? 160.339 169.161 130.598 1.00 42.20  ? 182  ILE B O     1 
ATOM   12342 C  CB    . ILE B 2  182  ? 160.195 171.566 132.111 1.00 41.94  ? 182  ILE B CB    1 
ATOM   12343 C  CG1   . ILE B 2  182  ? 158.868 171.103 132.701 1.00 39.50  ? 182  ILE B CG1   1 
ATOM   12344 C  CG2   . ILE B 2  182  ? 160.549 172.964 132.602 1.00 42.20  ? 182  ILE B CG2   1 
ATOM   12345 C  CD1   . ILE B 2  182  ? 158.986 170.676 134.130 1.00 40.76  ? 182  ILE B CD1   1 
ATOM   12346 N  N     . GLY B 2  183  ? 158.688 170.006 129.323 1.00 42.73  ? 183  GLY B N     1 
ATOM   12347 C  CA    . GLY B 2  183  ? 158.341 168.709 128.774 1.00 41.86  ? 183  GLY B CA    1 
ATOM   12348 C  C     . GLY B 2  183  ? 157.174 168.025 129.452 1.00 41.56  ? 183  GLY B C     1 
ATOM   12349 O  O     . GLY B 2  183  ? 157.096 166.794 129.466 1.00 43.65  ? 183  GLY B O     1 
ATOM   12350 N  N     . GLU B 2  184  ? 156.255 168.805 130.009 1.00 40.83  ? 184  GLU B N     1 
ATOM   12351 C  CA    . GLU B 2  184  ? 155.083 168.277 130.687 1.00 39.30  ? 184  GLU B CA    1 
ATOM   12352 C  C     . GLU B 2  184  ? 153.817 168.642 129.924 1.00 41.05  ? 184  GLU B C     1 
ATOM   12353 O  O     . GLU B 2  184  ? 153.796 169.573 129.116 1.00 44.39  ? 184  GLU B O     1 
ATOM   12354 C  CB    . GLU B 2  184  ? 154.997 168.806 132.124 1.00 39.43  ? 184  GLU B CB    1 
ATOM   12355 C  CG    . GLU B 2  184  ? 156.078 168.276 133.041 1.00 39.96  ? 184  GLU B CG    1 
ATOM   12356 C  CD    . GLU B 2  184  ? 155.913 166.807 133.334 1.00 42.70  ? 184  GLU B CD    1 
ATOM   12357 O  OE1   . GLU B 2  184  ? 154.770 166.368 133.558 1.00 45.48  ? 184  GLU B OE1   1 
ATOM   12358 O  OE2   . GLU B 2  184  ? 156.923 166.081 133.316 1.00 41.11  ? 184  GLU B OE2   1 
ATOM   12359 N  N     . ASP B 2  185  ? 152.760 167.885 130.187 1.00 39.99  ? 185  ASP B N     1 
ATOM   12360 C  CA    . ASP B 2  185  ? 151.424 168.186 129.690 1.00 38.44  ? 185  ASP B CA    1 
ATOM   12361 C  C     . ASP B 2  185  ? 150.856 169.366 130.468 1.00 37.92  ? 185  ASP B C     1 
ATOM   12362 O  O     . ASP B 2  185  ? 150.494 169.219 131.642 1.00 39.69  ? 185  ASP B O     1 
ATOM   12363 C  CB    . ASP B 2  185  ? 150.524 166.956 129.819 1.00 39.28  ? 185  ASP B CB    1 
ATOM   12364 C  CG    . ASP B 2  185  ? 149.290 167.046 128.967 1.00 41.79  ? 185  ASP B CG    1 
ATOM   12365 O  OD1   . ASP B 2  185  ? 149.167 168.028 128.219 1.00 43.86  ? 185  ASP B OD1   1 
ATOM   12366 O  OD2   . ASP B 2  185  ? 148.435 166.139 129.044 1.00 42.38  ? 185  ASP B OD2   1 
ATOM   12367 N  N     . PRO B 2  186  ? 150.762 170.550 129.855 1.00 38.70  ? 186  PRO B N     1 
ATOM   12368 C  CA    . PRO B 2  186  ? 150.353 171.744 130.610 1.00 41.57  ? 186  PRO B CA    1 
ATOM   12369 C  C     . PRO B 2  186  ? 148.895 171.750 131.012 1.00 43.25  ? 186  PRO B C     1 
ATOM   12370 O  O     . PRO B 2  186  ? 148.488 172.640 131.767 1.00 42.21  ? 186  PRO B O     1 
ATOM   12371 C  CB    . PRO B 2  186  ? 150.660 172.890 129.644 1.00 40.45  ? 186  PRO B CB    1 
ATOM   12372 C  CG    . PRO B 2  186  ? 150.552 172.274 128.303 1.00 42.41  ? 186  PRO B CG    1 
ATOM   12373 C  CD    . PRO B 2  186  ? 151.028 170.858 128.440 1.00 41.51  ? 186  PRO B CD    1 
ATOM   12374 N  N     . ASN B 2  187  ? 148.094 170.809 130.527 1.00 41.23  ? 187  ASN B N     1 
ATOM   12375 C  CA    . ASN B 2  187  ? 146.680 170.756 130.853 1.00 38.75  ? 187  ASN B CA    1 
ATOM   12376 C  C     . ASN B 2  187  ? 146.345 169.612 131.792 1.00 39.89  ? 187  ASN B C     1 
ATOM   12377 O  O     . ASN B 2  187  ? 145.333 169.681 132.495 1.00 41.49  ? 187  ASN B O     1 
ATOM   12378 C  CB    . ASN B 2  187  ? 145.857 170.629 129.570 1.00 41.64  ? 187  ASN B CB    1 
ATOM   12379 C  CG    . ASN B 2  187  ? 145.250 171.943 129.135 1.00 44.80  ? 187  ASN B CG    1 
ATOM   12380 O  OD1   . ASN B 2  187  ? 145.196 172.904 129.902 1.00 45.91  ? 187  ASN B OD1   1 
ATOM   12381 N  ND2   . ASN B 2  187  ? 144.795 171.995 127.891 1.00 40.80  ? 187  ASN B ND2   1 
ATOM   12382 N  N     . GLU B 2  188  ? 147.176 168.586 131.838 1.00 38.81  ? 188  GLU B N     1 
ATOM   12383 C  CA    . GLU B 2  188  ? 146.945 167.435 132.696 1.00 38.23  ? 188  GLU B CA    1 
ATOM   12384 C  C     . GLU B 2  188  ? 146.955 167.868 134.157 1.00 38.24  ? 188  GLU B C     1 
ATOM   12385 O  O     . GLU B 2  188  ? 147.900 168.533 134.593 1.00 39.62  ? 188  GLU B O     1 
ATOM   12386 C  CB    . GLU B 2  188  ? 148.018 166.379 132.436 1.00 39.76  ? 188  GLU B CB    1 
ATOM   12387 C  CG    . GLU B 2  188  ? 148.370 165.474 133.603 1.00 41.91  ? 188  GLU B CG    1 
ATOM   12388 C  CD    . GLU B 2  188  ? 147.370 164.351 133.810 1.00 43.65  ? 188  GLU B CD    1 
ATOM   12389 O  OE1   . GLU B 2  188  ? 147.367 163.398 133.006 1.00 43.21  ? 188  GLU B OE1   1 
ATOM   12390 O  OE2   . GLU B 2  188  ? 146.607 164.406 134.795 1.00 41.21  ? 188  GLU B OE2   1 
ATOM   12391 N  N     . PRO B 2  189  ? 145.924 167.526 134.935 1.00 37.21  ? 189  PRO B N     1 
ATOM   12392 C  CA    . PRO B 2  189  ? 145.904 167.949 136.342 1.00 40.11  ? 189  PRO B CA    1 
ATOM   12393 C  C     . PRO B 2  189  ? 146.891 167.197 137.221 1.00 39.09  ? 189  PRO B C     1 
ATOM   12394 O  O     . PRO B 2  189  ? 147.280 167.715 138.274 1.00 35.22  ? 189  PRO B O     1 
ATOM   12395 C  CB    . PRO B 2  189  ? 144.453 167.686 136.760 1.00 36.22  ? 189  PRO B CB    1 
ATOM   12396 C  CG    . PRO B 2  189  ? 144.009 166.568 135.872 1.00 34.80  ? 189  PRO B CG    1 
ATOM   12397 C  CD    . PRO B 2  189  ? 144.714 166.773 134.559 1.00 35.72  ? 189  PRO B CD    1 
ATOM   12398 N  N     . GLY B 2  190  ? 147.295 165.996 136.836 1.00 37.66  ? 190  GLY B N     1 
ATOM   12399 C  CA    . GLY B 2  190  ? 148.248 165.231 137.623 1.00 36.53  ? 190  GLY B CA    1 
ATOM   12400 C  C     . GLY B 2  190  ? 147.548 164.289 138.578 1.00 36.21  ? 190  GLY B C     1 
ATOM   12401 O  O     . GLY B 2  190  ? 146.542 163.682 138.228 1.00 36.33  ? 190  GLY B O     1 
ATOM   12402 N  N     . GLY B 2  191  ? 148.079 164.180 139.790 1.00 37.32  ? 191  GLY B N     1 
ATOM   12403 C  CA    . GLY B 2  191  ? 147.542 163.275 140.788 1.00 31.77  ? 191  GLY B CA    1 
ATOM   12404 C  C     . GLY B 2  191  ? 147.885 161.814 140.598 1.00 32.19  ? 191  GLY B C     1 
ATOM   12405 O  O     . GLY B 2  191  ? 147.120 160.946 141.029 1.00 33.09  ? 191  GLY B O     1 
ATOM   12406 N  N     . TYR B 2  192  ? 149.033 161.516 139.997 1.00 33.58  ? 192  TYR B N     1 
ATOM   12407 C  CA    . TYR B 2  192  ? 149.450 160.136 139.798 1.00 33.34  ? 192  TYR B CA    1 
ATOM   12408 C  C     . TYR B 2  192  ? 150.882 159.970 140.283 1.00 33.79  ? 192  TYR B C     1 
ATOM   12409 O  O     . TYR B 2  192  ? 151.536 160.927 140.698 1.00 37.09  ? 192  TYR B O     1 
ATOM   12410 C  CB    . TYR B 2  192  ? 149.336 159.703 138.332 1.00 33.11  ? 192  TYR B CB    1 
ATOM   12411 C  CG    . TYR B 2  192  ? 150.058 160.598 137.353 1.00 34.53  ? 192  TYR B CG    1 
ATOM   12412 C  CD1   . TYR B 2  192  ? 149.405 161.647 136.727 1.00 34.54  ? 192  TYR B CD1   1 
ATOM   12413 C  CD2   . TYR B 2  192  ? 151.398 160.402 137.068 1.00 33.65  ? 192  TYR B CD2   1 
ATOM   12414 C  CE1   . TYR B 2  192  ? 150.063 162.459 135.837 1.00 34.20  ? 192  TYR B CE1   1 
ATOM   12415 C  CE2   . TYR B 2  192  ? 152.063 161.213 136.191 1.00 32.75  ? 192  TYR B CE2   1 
ATOM   12416 C  CZ    . TYR B 2  192  ? 151.394 162.237 135.573 1.00 33.60  ? 192  TYR B CZ    1 
ATOM   12417 O  OH    . TYR B 2  192  ? 152.063 163.048 134.688 1.00 35.34  ? 192  TYR B OH    1 
ATOM   12418 N  N     . PHE B 2  193  ? 151.364 158.734 140.211 1.00 32.75  ? 193  PHE B N     1 
ATOM   12419 C  CA    . PHE B 2  193  ? 152.688 158.355 140.674 1.00 35.39  ? 193  PHE B CA    1 
ATOM   12420 C  C     . PHE B 2  193  ? 153.498 157.768 139.529 1.00 36.22  ? 193  PHE B C     1 
ATOM   12421 O  O     . PHE B 2  193  ? 152.968 157.057 138.675 1.00 40.62  ? 193  PHE B O     1 
ATOM   12422 C  CB    . PHE B 2  193  ? 152.599 157.323 141.805 1.00 35.19  ? 193  PHE B CB    1 
ATOM   12423 C  CG    . PHE B 2  193  ? 152.093 157.883 143.093 1.00 38.08  ? 193  PHE B CG    1 
ATOM   12424 C  CD1   . PHE B 2  193  ? 150.855 157.524 143.576 1.00 36.17  ? 193  PHE B CD1   1 
ATOM   12425 C  CD2   . PHE B 2  193  ? 152.858 158.757 143.828 1.00 35.48  ? 193  PHE B CD2   1 
ATOM   12426 C  CE1   . PHE B 2  193  ? 150.388 158.043 144.753 1.00 37.30  ? 193  PHE B CE1   1 
ATOM   12427 C  CE2   . PHE B 2  193  ? 152.393 159.266 145.008 1.00 36.21  ? 193  PHE B CE2   1 
ATOM   12428 C  CZ    . PHE B 2  193  ? 151.158 158.911 145.469 1.00 38.29  ? 193  PHE B CZ    1 
ATOM   12429 N  N     . ILE B 2  194  ? 154.797 158.050 139.538 1.00 35.89  ? 194  ILE B N     1 
ATOM   12430 C  CA    . ILE B 2  194  ? 155.743 157.493 138.579 1.00 37.52  ? 194  ILE B CA    1 
ATOM   12431 C  C     . ILE B 2  194  ? 156.693 156.583 139.342 1.00 40.57  ? 194  ILE B C     1 
ATOM   12432 O  O     . ILE B 2  194  ? 157.378 157.029 140.269 1.00 43.54  ? 194  ILE B O     1 
ATOM   12433 C  CB    . ILE B 2  194  ? 156.515 158.595 137.840 1.00 37.85  ? 194  ILE B CB    1 
ATOM   12434 C  CG1   . ILE B 2  194  ? 155.547 159.508 137.081 1.00 34.91  ? 194  ILE B CG1   1 
ATOM   12435 C  CG2   . ILE B 2  194  ? 157.552 157.985 136.914 1.00 35.94  ? 194  ILE B CG2   1 
ATOM   12436 C  CD1   . ILE B 2  194  ? 156.180 160.780 136.574 1.00 34.91  ? 194  ILE B CD1   1 
ATOM   12437 N  N     . ALA B 2  195  ? 156.729 155.309 138.965 1.00 36.46  ? 195  ALA B N     1 
ATOM   12438 C  CA    . ALA B 2  195  ? 157.599 154.335 139.608 1.00 36.69  ? 195  ALA B CA    1 
ATOM   12439 C  C     . ALA B 2  195  ? 158.127 153.380 138.553 1.00 38.91  ? 195  ALA B C     1 
ATOM   12440 O  O     . ALA B 2  195  ? 157.342 152.734 137.852 1.00 40.95  ? 195  ALA B O     1 
ATOM   12441 C  CB    . ALA B 2  195  ? 156.861 153.559 140.701 1.00 34.91  ? 195  ALA B CB    1 
ATOM   12442 N  N     . ARG B 2  196  ? 159.453 153.281 138.460 1.00 40.45  ? 196  ARG B N     1 
ATOM   12443 C  CA    . ARG B 2  196  ? 160.119 152.523 137.404 1.00 40.08  ? 196  ARG B CA    1 
ATOM   12444 C  C     . ARG B 2  196  ? 159.713 153.043 136.029 1.00 42.81  ? 196  ARG B C     1 
ATOM   12445 O  O     . ARG B 2  196  ? 159.569 152.286 135.066 1.00 43.82  ? 196  ARG B O     1 
ATOM   12446 C  CB    . ARG B 2  196  ? 159.847 151.022 137.530 1.00 41.49  ? 196  ARG B CB    1 
ATOM   12447 C  CG    . ARG B 2  196  ? 160.422 150.393 138.797 1.00 41.42  ? 196  ARG B CG    1 
ATOM   12448 C  CD    . ARG B 2  196  ? 159.361 150.161 139.865 1.00 45.27  ? 196  ARG B CD    1 
ATOM   12449 N  NE    . ARG B 2  196  ? 158.089 149.737 139.294 1.00 45.32  ? 196  ARG B NE    1 
ATOM   12450 C  CZ    . ARG B 2  196  ? 157.840 148.509 138.859 1.00 47.08  ? 196  ARG B CZ    1 
ATOM   12451 N  NH1   . ARG B 2  196  ? 158.757 147.557 138.916 1.00 45.83  ? 196  ARG B NH1   1 
ATOM   12452 N  NH2   . ARG B 2  196  ? 156.647 148.232 138.341 1.00 46.03  ? 196  ARG B NH2   1 
ATOM   12453 N  N     . GLY B 2  197  ? 159.506 154.356 135.946 1.00 36.56  ? 197  GLY B N     1 
ATOM   12454 C  CA    . GLY B 2  197  ? 159.195 155.009 134.696 1.00 35.81  ? 197  GLY B CA    1 
ATOM   12455 C  C     . GLY B 2  197  ? 157.757 154.909 134.247 1.00 36.79  ? 197  GLY B C     1 
ATOM   12456 O  O     . GLY B 2  197  ? 157.377 155.599 133.295 1.00 37.22  ? 197  GLY B O     1 
ATOM   12457 N  N     . GLY B 2  198  ? 156.942 154.078 134.893 1.00 34.12  ? 198  GLY B N     1 
ATOM   12458 C  CA    . GLY B 2  198  ? 155.551 153.931 134.537 1.00 33.18  ? 198  GLY B CA    1 
ATOM   12459 C  C     . GLY B 2  198  ? 154.650 154.730 135.459 1.00 32.65  ? 198  GLY B C     1 
ATOM   12460 O  O     . GLY B 2  198  ? 155.003 155.059 136.583 1.00 36.88  ? 198  GLY B O     1 
ATOM   12461 N  N     . GLU B 2  199  ? 153.458 155.027 134.961 1.00 32.27  ? 199  GLU B N     1 
ATOM   12462 C  CA    . GLU B 2  199  ? 152.511 155.887 135.653 1.00 29.97  ? 199  GLU B CA    1 
ATOM   12463 C  C     . GLU B 2  199  ? 151.462 155.031 136.345 1.00 34.35  ? 199  GLU B C     1 
ATOM   12464 O  O     . GLU B 2  199  ? 150.833 154.178 135.711 1.00 34.72  ? 199  GLU B O     1 
ATOM   12465 C  CB    . GLU B 2  199  ? 151.857 156.860 134.677 1.00 32.00  ? 199  GLU B CB    1 
ATOM   12466 C  CG    . GLU B 2  199  ? 152.500 158.219 134.687 1.00 33.67  ? 199  GLU B CG    1 
ATOM   12467 C  CD    . GLU B 2  199  ? 152.636 158.822 133.310 1.00 37.01  ? 199  GLU B CD    1 
ATOM   12468 O  OE1   . GLU B 2  199  ? 153.339 159.841 133.176 1.00 35.59  ? 199  GLU B OE1   1 
ATOM   12469 O  OE2   . GLU B 2  199  ? 152.036 158.285 132.362 1.00 37.07  ? 199  GLU B OE2   1 
ATOM   12470 N  N     . TRP B 2  200  ? 151.282 155.257 137.643 1.00 33.52  ? 200  TRP B N     1 
ATOM   12471 C  CA    . TRP B 2  200  ? 150.415 154.428 138.459 1.00 30.45  ? 200  TRP B CA    1 
ATOM   12472 C  C     . TRP B 2  200  ? 149.436 155.298 139.227 1.00 31.23  ? 200  TRP B C     1 
ATOM   12473 O  O     . TRP B 2  200  ? 149.773 156.396 139.675 1.00 32.66  ? 200  TRP B O     1 
ATOM   12474 C  CB    . TRP B 2  200  ? 151.223 153.564 139.433 1.00 32.86  ? 200  TRP B CB    1 
ATOM   12475 C  CG    . TRP B 2  200  ? 152.185 152.656 138.751 1.00 31.08  ? 200  TRP B CG    1 
ATOM   12476 C  CD1   . TRP B 2  200  ? 153.474 152.934 138.405 1.00 29.99  ? 200  TRP B CD1   1 
ATOM   12477 C  CD2   . TRP B 2  200  ? 151.928 151.324 138.307 1.00 32.54  ? 200  TRP B CD2   1 
ATOM   12478 N  NE1   . TRP B 2  200  ? 154.037 151.853 137.782 1.00 31.48  ? 200  TRP B NE1   1 
ATOM   12479 C  CE2   . TRP B 2  200  ? 153.109 150.850 137.709 1.00 34.31  ? 200  TRP B CE2   1 
ATOM   12480 C  CE3   . TRP B 2  200  ? 150.815 150.483 138.363 1.00 29.72  ? 200  TRP B CE3   1 
ATOM   12481 C  CZ2   . TRP B 2  200  ? 153.209 149.574 137.174 1.00 35.52  ? 200  TRP B CZ2   1 
ATOM   12482 C  CZ3   . TRP B 2  200  ? 150.916 149.220 137.833 1.00 33.45  ? 200  TRP B CZ3   1 
ATOM   12483 C  CH2   . TRP B 2  200  ? 152.103 148.775 137.243 1.00 35.04  ? 200  TRP B CH2   1 
ATOM   12484 N  N     . VAL B 2  201  ? 148.219 154.788 139.380 1.00 34.17  ? 201  VAL B N     1 
ATOM   12485 C  CA    . VAL B 2  201  ? 147.145 155.485 140.074 1.00 33.81  ? 201  VAL B CA    1 
ATOM   12486 C  C     . VAL B 2  201  ? 146.778 154.682 141.310 1.00 32.53  ? 201  VAL B C     1 
ATOM   12487 O  O     . VAL B 2  201  ? 146.421 153.506 141.209 1.00 32.67  ? 201  VAL B O     1 
ATOM   12488 C  CB    . VAL B 2  201  ? 145.914 155.678 139.159 1.00 32.15  ? 201  VAL B CB    1 
ATOM   12489 C  CG1   . VAL B 2  201  ? 144.704 156.131 139.956 1.00 29.36  ? 201  VAL B CG1   1 
ATOM   12490 C  CG2   . VAL B 2  201  ? 146.224 156.669 138.058 1.00 31.66  ? 201  VAL B CG2   1 
ATOM   12491 N  N     . VAL B 2  202  ? 146.864 155.315 142.475 1.00 32.65  ? 202  VAL B N     1 
ATOM   12492 C  CA    . VAL B 2  202  ? 146.450 154.671 143.715 1.00 35.60  ? 202  VAL B CA    1 
ATOM   12493 C  C     . VAL B 2  202  ? 144.938 154.787 143.833 1.00 37.55  ? 202  VAL B C     1 
ATOM   12494 O  O     . VAL B 2  202  ? 144.396 155.887 143.979 1.00 37.01  ? 202  VAL B O     1 
ATOM   12495 C  CB    . VAL B 2  202  ? 147.151 155.284 144.933 1.00 38.56  ? 202  VAL B CB    1 
ATOM   12496 C  CG1   . VAL B 2  202  ? 146.660 154.612 146.192 1.00 37.51  ? 202  VAL B CG1   1 
ATOM   12497 C  CG2   . VAL B 2  202  ? 148.652 155.111 144.814 1.00 35.08  ? 202  VAL B CG2   1 
ATOM   12498 N  N     . ASP B 2  203  ? 144.258 153.647 143.774 1.00 37.37  ? 203  ASP B N     1 
ATOM   12499 C  CA    . ASP B 2  203  ? 142.810 153.631 143.647 1.00 35.28  ? 203  ASP B CA    1 
ATOM   12500 C  C     . ASP B 2  203  ? 142.134 154.048 144.944 1.00 36.53  ? 203  ASP B C     1 
ATOM   12501 O  O     . ASP B 2  203  ? 142.597 153.723 146.039 1.00 41.36  ? 203  ASP B O     1 
ATOM   12502 C  CB    . ASP B 2  203  ? 142.336 152.237 143.247 1.00 38.53  ? 203  ASP B CB    1 
ATOM   12503 C  CG    . ASP B 2  203  ? 143.117 151.665 142.075 1.00 43.51  ? 203  ASP B CG    1 
ATOM   12504 O  OD1   . ASP B 2  203  ? 143.664 152.456 141.279 1.00 45.07  ? 203  ASP B OD1   1 
ATOM   12505 O  OD2   . ASP B 2  203  ? 143.166 150.424 141.940 1.00 41.54  ? 203  ASP B OD2   1 
ATOM   12506 N  N     . LEU B 2  204  ? 141.025 154.771 144.815 1.00 26.76  ? 204  LEU B N     1 
ATOM   12507 C  CA    . LEU B 2  204  ? 140.137 154.999 145.946 1.00 27.93  ? 204  LEU B CA    1 
ATOM   12508 C  C     . LEU B 2  204  ? 139.510 153.671 146.342 1.00 30.79  ? 204  LEU B C     1 
ATOM   12509 O  O     . LEU B 2  204  ? 138.769 153.070 145.561 1.00 34.26  ? 204  LEU B O     1 
ATOM   12510 C  CB    . LEU B 2  204  ? 139.062 156.019 145.591 1.00 26.44  ? 204  LEU B CB    1 
ATOM   12511 C  CG    . LEU B 2  204  ? 139.457 157.481 145.410 1.00 31.43  ? 204  LEU B CG    1 
ATOM   12512 C  CD1   . LEU B 2  204  ? 138.373 158.242 144.660 1.00 29.15  ? 204  LEU B CD1   1 
ATOM   12513 C  CD2   . LEU B 2  204  ? 139.706 158.111 146.759 1.00 29.07  ? 204  LEU B CD2   1 
ATOM   12514 N  N     . LEU B 2  205  ? 139.817 153.195 147.541 1.00 31.93  ? 205  LEU B N     1 
ATOM   12515 C  CA    . LEU B 2  205  ? 139.303 151.922 148.014 1.00 32.63  ? 205  LEU B CA    1 
ATOM   12516 C  C     . LEU B 2  205  ? 138.071 152.152 148.871 1.00 33.74  ? 205  LEU B C     1 
ATOM   12517 O  O     . LEU B 2  205  ? 138.046 153.059 149.707 1.00 32.20  ? 205  LEU B O     1 
ATOM   12518 C  CB    . LEU B 2  205  ? 140.358 151.146 148.799 1.00 33.59  ? 205  LEU B CB    1 
ATOM   12519 C  CG    . LEU B 2  205  ? 140.106 149.637 148.805 1.00 33.98  ? 205  LEU B CG    1 
ATOM   12520 C  CD1   . LEU B 2  205  ? 140.643 148.986 147.549 1.00 30.62  ? 205  LEU B CD1   1 
ATOM   12521 C  CD2   . LEU B 2  205  ? 140.701 149.001 150.042 1.00 35.95  ? 205  LEU B CD2   1 
ATOM   12522 N  N     . GLU B 2  206  ? 137.050 151.336 148.643 1.00 34.56  ? 206  GLU B N     1 
ATOM   12523 C  CA    . GLU B 2  206  ? 135.784 151.403 149.361 1.00 33.34  ? 206  GLU B CA    1 
ATOM   12524 C  C     . GLU B 2  206  ? 135.886 150.504 150.584 1.00 38.24  ? 206  GLU B C     1 
ATOM   12525 O  O     . GLU B 2  206  ? 135.913 149.279 150.484 1.00 41.09  ? 206  GLU B O     1 
ATOM   12526 C  CB    . GLU B 2  206  ? 134.646 150.986 148.444 1.00 37.08  ? 206  GLU B CB    1 
ATOM   12527 C  CG    . GLU B 2  206  ? 133.254 151.215 148.974 1.00 35.91  ? 206  GLU B CG    1 
ATOM   12528 C  CD    . GLU B 2  206  ? 132.323 150.100 148.556 1.00 39.21  ? 206  GLU B CD    1 
ATOM   12529 O  OE1   . GLU B 2  206  ? 132.655 149.399 147.582 1.00 39.47  ? 206  GLU B OE1   1 
ATOM   12530 O  OE2   . GLU B 2  206  ? 131.266 149.921 149.186 1.00 38.67  ? 206  GLU B OE2   1 
ATOM   12531 N  N     . ASN B 2  207  ? 135.956 151.123 151.755 1.00 35.42  ? 207  ASN B N     1 
ATOM   12532 C  CA    . ASN B 2  207  ? 136.030 150.383 153.002 1.00 33.17  ? 207  ASN B CA    1 
ATOM   12533 C  C     . ASN B 2  207  ? 134.784 150.642 153.846 1.00 34.03  ? 207  ASN B C     1 
ATOM   12534 O  O     . ASN B 2  207  ? 134.004 151.556 153.588 1.00 33.78  ? 207  ASN B O     1 
ATOM   12535 C  CB    . ASN B 2  207  ? 137.294 150.763 153.770 1.00 34.65  ? 207  ASN B CB    1 
ATOM   12536 C  CG    . ASN B 2  207  ? 137.745 149.680 154.721 1.00 38.42  ? 207  ASN B CG    1 
ATOM   12537 O  OD1   . ASN B 2  207  ? 138.360 149.955 155.748 1.00 38.26  ? 207  ASN B OD1   1 
ATOM   12538 N  ND2   . ASN B 2  207  ? 137.457 148.433 154.372 1.00 37.08  ? 207  ASN B ND2   1 
ATOM   12539 N  N     . ILE B 2  208  ? 134.610 149.831 154.858 1.00 32.05  ? 208  ILE B N     1 
ATOM   12540 C  CA    . ILE B 2  208  ? 133.469 149.909 155.760 1.00 27.93  ? 208  ILE B CA    1 
ATOM   12541 C  C     . ILE B 2  208  ? 133.736 151.003 156.783 1.00 25.30  ? 208  ILE B C     1 
ATOM   12542 O  O     . ILE B 2  208  ? 134.884 151.327 157.087 1.00 33.11  ? 208  ILE B O     1 
ATOM   12543 C  CB    . ILE B 2  208  ? 133.200 148.552 156.448 1.00 29.29  ? 208  ILE B CB    1 
ATOM   12544 C  CG1   . ILE B 2  208  ? 133.374 147.378 155.484 1.00 31.22  ? 208  ILE B CG1   1 
ATOM   12545 C  CG2   . ILE B 2  208  ? 131.807 148.502 156.987 1.00 28.35  ? 208  ILE B CG2   1 
ATOM   12546 C  CD1   . ILE B 2  208  ? 134.799 146.837 155.383 1.00 29.37  ? 208  ILE B CD1   1 
ATOM   12547 N  N     . ARG B 2  209  ? 132.669 151.593 157.307 1.00 19.68  ? 209  ARG B N     1 
ATOM   12548 C  CA    . ARG B 2  209  ? 132.816 152.640 158.307 1.00 21.80  ? 209  ARG B CA    1 
ATOM   12549 C  C     . ARG B 2  209  ? 133.238 152.041 159.642 1.00 29.69  ? 209  ARG B C     1 
ATOM   12550 O  O     . ARG B 2  209  ? 132.694 151.027 160.084 1.00 35.91  ? 209  ARG B O     1 
ATOM   12551 C  CB    . ARG B 2  209  ? 131.505 153.401 158.470 1.00 25.29  ? 209  ARG B CB    1 
ATOM   12552 C  CG    . ARG B 2  209  ? 131.525 154.417 159.574 1.00 24.05  ? 209  ARG B CG    1 
ATOM   12553 C  CD    . ARG B 2  209  ? 130.309 155.295 159.537 1.00 23.42  ? 209  ARG B CD    1 
ATOM   12554 N  NE    . ARG B 2  209  ? 129.113 154.569 159.933 1.00 24.67  ? 209  ARG B NE    1 
ATOM   12555 C  CZ    . ARG B 2  209  ? 127.986 155.141 160.328 1.00 26.70  ? 209  ARG B CZ    1 
ATOM   12556 N  NH1   . ARG B 2  209  ? 127.840 156.452 160.327 1.00 25.42  ? 209  ARG B NH1   1 
ATOM   12557 N  NH2   . ARG B 2  209  ? 126.979 154.378 160.735 1.00 27.12  ? 209  ARG B NH2   1 
ATOM   12558 N  N     . PHE B 2  210  ? 134.205 152.679 160.292 1.00 32.73  ? 210  PHE B N     1 
ATOM   12559 C  CA    . PHE B 2  210  ? 134.705 152.213 161.574 1.00 30.41  ? 210  PHE B CA    1 
ATOM   12560 C  C     . PHE B 2  210  ? 133.866 152.786 162.708 1.00 30.48  ? 210  PHE B C     1 
ATOM   12561 O  O     . PHE B 2  210  ? 133.067 153.703 162.517 1.00 32.74  ? 210  PHE B O     1 
ATOM   12562 C  CB    . PHE B 2  210  ? 136.171 152.605 161.755 1.00 27.94  ? 210  PHE B CB    1 
ATOM   12563 C  CG    . PHE B 2  210  ? 137.113 151.836 160.882 1.00 30.50  ? 210  PHE B CG    1 
ATOM   12564 C  CD1   . PHE B 2  210  ? 136.760 150.599 160.383 1.00 29.47  ? 210  PHE B CD1   1 
ATOM   12565 C  CD2   . PHE B 2  210  ? 138.347 152.357 160.548 1.00 32.21  ? 210  PHE B CD2   1 
ATOM   12566 C  CE1   . PHE B 2  210  ? 137.625 149.894 159.580 1.00 32.07  ? 210  PHE B CE1   1 
ATOM   12567 C  CE2   . PHE B 2  210  ? 139.211 151.656 159.743 1.00 31.96  ? 210  PHE B CE2   1 
ATOM   12568 C  CZ    . PHE B 2  210  ? 138.849 150.423 159.259 1.00 30.79  ? 210  PHE B CZ    1 
ATOM   12569 N  N     . ASN B 2  211  ? 134.059 152.223 163.904 1.00 25.32  ? 211  ASN B N     1 
ATOM   12570 C  CA    . ASN B 2  211  ? 133.391 152.671 165.127 1.00 25.50  ? 211  ASN B CA    1 
ATOM   12571 C  C     . ASN B 2  211  ? 131.889 152.414 165.090 1.00 27.50  ? 211  ASN B C     1 
ATOM   12572 O  O     . ASN B 2  211  ? 131.123 153.095 165.773 1.00 27.02  ? 211  ASN B O     1 
ATOM   12573 C  CB    . ASN B 2  211  ? 133.649 154.157 165.387 1.00 26.94  ? 211  ASN B CB    1 
ATOM   12574 C  CG    . ASN B 2  211  ? 134.915 154.405 166.153 1.00 31.65  ? 211  ASN B CG    1 
ATOM   12575 O  OD1   . ASN B 2  211  ? 135.812 153.573 166.170 1.00 35.16  ? 211  ASN B OD1   1 
ATOM   12576 N  ND2   . ASN B 2  211  ? 135.008 155.567 166.772 1.00 27.37  ? 211  ASN B ND2   1 
ATOM   12577 N  N     . THR B 2  212  ? 131.441 151.451 164.285 1.00 25.41  ? 212  THR B N     1 
ATOM   12578 C  CA    . THR B 2  212  ? 130.016 151.201 164.108 1.00 25.82  ? 212  THR B CA    1 
ATOM   12579 C  C     . THR B 2  212  ? 129.745 149.708 164.034 1.00 25.94  ? 212  THR B C     1 
ATOM   12580 O  O     . THR B 2  212  ? 130.614 148.918 163.665 1.00 27.00  ? 212  THR B O     1 
ATOM   12581 C  CB    . THR B 2  212  ? 129.440 151.883 162.838 1.00 31.48  ? 212  THR B CB    1 
ATOM   12582 O  OG1   . THR B 2  212  ? 130.006 151.302 161.658 1.00 29.87  ? 212  THR B OG1   1 
ATOM   12583 C  CG2   . THR B 2  212  ? 129.713 153.372 162.842 1.00 28.13  ? 212  THR B CG2   1 
ATOM   12584 N  N     . LEU B 2  213  ? 128.507 149.344 164.357 1.00 28.82  ? 213  LEU B N     1 
ATOM   12585 C  CA    . LEU B 2  213  ? 128.102 147.955 164.531 1.00 29.64  ? 213  LEU B CA    1 
ATOM   12586 C  C     . LEU B 2  213  ? 127.451 147.423 163.261 1.00 31.03  ? 213  LEU B C     1 
ATOM   12587 O  O     . LEU B 2  213  ? 126.486 148.006 162.763 1.00 35.66  ? 213  LEU B O     1 
ATOM   12588 C  CB    . LEU B 2  213  ? 127.137 147.844 165.711 1.00 30.46  ? 213  LEU B CB    1 
ATOM   12589 C  CG    . LEU B 2  213  ? 126.737 146.451 166.189 1.00 34.51  ? 213  LEU B CG    1 
ATOM   12590 C  CD1   . LEU B 2  213  ? 127.816 145.859 167.065 1.00 35.17  ? 213  LEU B CD1   1 
ATOM   12591 C  CD2   . LEU B 2  213  ? 125.435 146.531 166.942 1.00 29.42  ? 213  LEU B CD2   1 
ATOM   12592 N  N     . HIS B 2  214  ? 127.963 146.312 162.751 1.00 31.39  ? 214  HIS B N     1 
ATOM   12593 C  CA    . HIS B 2  214  ? 127.410 145.669 161.568 1.00 33.81  ? 214  HIS B CA    1 
ATOM   12594 C  C     . HIS B 2  214  ? 126.865 144.300 161.940 1.00 36.73  ? 214  HIS B C     1 
ATOM   12595 O  O     . HIS B 2  214  ? 127.629 143.401 162.295 1.00 42.35  ? 214  HIS B O     1 
ATOM   12596 C  CB    . HIS B 2  214  ? 128.466 145.553 160.470 1.00 33.97  ? 214  HIS B CB    1 
ATOM   12597 C  CG    . HIS B 2  214  ? 129.059 146.869 160.079 1.00 39.95  ? 214  HIS B CG    1 
ATOM   12598 N  ND1   . HIS B 2  214  ? 128.448 147.724 159.190 1.00 40.23  ? 214  HIS B ND1   1 
ATOM   12599 C  CD2   . HIS B 2  214  ? 130.196 147.488 160.474 1.00 38.85  ? 214  HIS B CD2   1 
ATOM   12600 C  CE1   . HIS B 2  214  ? 129.184 148.811 159.051 1.00 37.94  ? 214  HIS B CE1   1 
ATOM   12601 N  NE2   . HIS B 2  214  ? 130.251 148.692 159.818 1.00 37.09  ? 214  HIS B NE2   1 
ATOM   12602 N  N     . ILE B 2  215  ? 125.553 144.137 161.816 1.00 37.13  ? 215  ILE B N     1 
ATOM   12603 C  CA    . ILE B 2  215  ? 124.848 142.931 162.226 1.00 33.11  ? 215  ILE B CA    1 
ATOM   12604 C  C     . ILE B 2  215  ? 124.466 142.149 160.981 1.00 36.41  ? 215  ILE B C     1 
ATOM   12605 O  O     . ILE B 2  215  ? 123.810 142.686 160.083 1.00 42.08  ? 215  ILE B O     1 
ATOM   12606 C  CB    . ILE B 2  215  ? 123.602 143.276 163.059 1.00 35.47  ? 215  ILE B CB    1 
ATOM   12607 C  CG1   . ILE B 2  215  ? 123.999 144.105 164.281 1.00 36.63  ? 215  ILE B CG1   1 
ATOM   12608 C  CG2   . ILE B 2  215  ? 122.856 142.022 163.460 1.00 36.19  ? 215  ILE B CG2   1 
ATOM   12609 C  CD1   . ILE B 2  215  ? 122.841 144.678 165.040 1.00 34.84  ? 215  ILE B CD1   1 
ATOM   12610 N  N     . HIS B 2  216  ? 124.867 140.883 160.927 1.00 39.78  ? 216  HIS B N     1 
ATOM   12611 C  CA    . HIS B 2  216  ? 124.560 140.035 159.785 1.00 42.67  ? 216  HIS B CA    1 
ATOM   12612 C  C     . HIS B 2  216  ? 123.909 138.741 160.246 1.00 43.43  ? 216  HIS B C     1 
ATOM   12613 O  O     . HIS B 2  216  ? 123.586 138.556 161.420 1.00 45.04  ? 216  HIS B O     1 
ATOM   12614 C  CB    . HIS B 2  216  ? 125.806 139.715 158.952 1.00 41.10  ? 216  HIS B CB    1 
ATOM   12615 C  CG    . HIS B 2  216  ? 126.862 140.771 159.005 1.00 44.43  ? 216  HIS B CG    1 
ATOM   12616 N  ND1   . HIS B 2  216  ? 128.100 140.557 159.568 1.00 47.23  ? 216  HIS B ND1   1 
ATOM   12617 C  CD2   . HIS B 2  216  ? 126.867 142.049 158.556 1.00 45.75  ? 216  HIS B CD2   1 
ATOM   12618 C  CE1   . HIS B 2  216  ? 128.822 141.658 159.467 1.00 45.55  ? 216  HIS B CE1   1 
ATOM   12619 N  NE2   . HIS B 2  216  ? 128.098 142.578 158.857 1.00 47.15  ? 216  HIS B NE2   1 
ATOM   12620 N  N     . TYR B 2  217  ? 123.707 137.848 159.283 1.00 46.50  ? 217  TYR B N     1 
ATOM   12621 C  CA    . TYR B 2  217  ? 123.201 136.507 159.534 1.00 45.49  ? 217  TYR B CA    1 
ATOM   12622 C  C     . TYR B 2  217  ? 124.201 135.468 159.053 1.00 47.73  ? 217  TYR B C     1 
ATOM   12623 O  O     . TYR B 2  217  ? 125.007 135.740 158.164 1.00 47.70  ? 217  TYR B O     1 
ATOM   12624 C  CB    . TYR B 2  217  ? 121.858 136.296 158.842 1.00 44.46  ? 217  TYR B CB    1 
ATOM   12625 C  CG    . TYR B 2  217  ? 120.679 136.786 159.636 1.00 46.24  ? 217  TYR B CG    1 
ATOM   12626 C  CD1   . TYR B 2  217  ? 120.811 137.130 160.969 1.00 45.40  ? 217  TYR B CD1   1 
ATOM   12627 C  CD2   . TYR B 2  217  ? 119.429 136.897 159.054 1.00 47.93  ? 217  TYR B CD2   1 
ATOM   12628 C  CE1   . TYR B 2  217  ? 119.733 137.576 161.700 1.00 45.72  ? 217  TYR B CE1   1 
ATOM   12629 C  CE2   . TYR B 2  217  ? 118.344 137.341 159.777 1.00 47.88  ? 217  TYR B CE2   1 
ATOM   12630 C  CZ    . TYR B 2  217  ? 118.501 137.679 161.099 1.00 48.84  ? 217  TYR B CZ    1 
ATOM   12631 O  OH    . TYR B 2  217  ? 117.420 138.122 161.823 1.00 48.89  ? 217  TYR B OH    1 
ATOM   12632 N  N     . ASN B 2  225  ? 124.582 126.232 164.642 1.00 52.66  ? 225  ASN B N     1 
ATOM   12633 C  CA    . ASN B 2  225  ? 125.518 126.974 165.476 1.00 55.26  ? 225  ASN B CA    1 
ATOM   12634 C  C     . ASN B 2  225  ? 125.270 128.473 165.385 1.00 56.71  ? 225  ASN B C     1 
ATOM   12635 O  O     . ASN B 2  225  ? 124.189 128.957 165.711 1.00 54.76  ? 225  ASN B O     1 
ATOM   12636 C  CB    . ASN B 2  225  ? 126.960 126.662 165.073 1.00 56.67  ? 225  ASN B CB    1 
ATOM   12637 C  CG    . ASN B 2  225  ? 127.423 125.305 165.560 1.00 57.69  ? 225  ASN B CG    1 
ATOM   12638 O  OD1   . ASN B 2  225  ? 127.349 125.001 166.752 1.00 56.94  ? 225  ASN B OD1   1 
ATOM   12639 N  ND2   . ASN B 2  225  ? 127.894 124.475 164.635 1.00 56.57  ? 225  ASN B ND2   1 
ATOM   12640 N  N     . GLU B 2  226  ? 126.285 129.202 164.931 1.00 58.33  ? 226  GLU B N     1 
ATOM   12641 C  CA    . GLU B 2  226  ? 126.215 130.655 164.850 1.00 56.90  ? 226  GLU B CA    1 
ATOM   12642 C  C     . GLU B 2  226  ? 125.206 131.066 163.785 1.00 56.10  ? 226  GLU B C     1 
ATOM   12643 O  O     . GLU B 2  226  ? 125.424 130.830 162.592 1.00 57.40  ? 226  GLU B O     1 
ATOM   12644 C  CB    . GLU B 2  226  ? 127.594 131.222 164.534 1.00 56.56  ? 226  GLU B CB    1 
ATOM   12645 C  CG    . GLU B 2  226  ? 127.625 132.718 164.349 1.00 54.73  ? 226  GLU B CG    1 
ATOM   12646 C  CD    . GLU B 2  226  ? 128.929 133.197 163.759 1.00 55.66  ? 226  GLU B CD    1 
ATOM   12647 O  OE1   . GLU B 2  226  ? 129.764 132.354 163.379 1.00 56.99  ? 226  GLU B OE1   1 
ATOM   12648 O  OE2   . GLU B 2  226  ? 129.121 134.422 163.671 1.00 56.46  ? 226  GLU B OE2   1 
ATOM   12649 N  N     . ILE B 2  227  ? 124.108 131.686 164.209 1.00 48.18  ? 227  ILE B N     1 
ATOM   12650 C  CA    . ILE B 2  227  ? 123.085 132.127 163.267 1.00 51.26  ? 227  ILE B CA    1 
ATOM   12651 C  C     . ILE B 2  227  ? 123.285 133.602 162.940 1.00 52.17  ? 227  ILE B C     1 
ATOM   12652 O  O     . ILE B 2  227  ? 123.045 134.035 161.807 1.00 49.34  ? 227  ILE B O     1 
ATOM   12653 C  CB    . ILE B 2  227  ? 121.668 131.866 163.810 1.00 49.51  ? 227  ILE B CB    1 
ATOM   12654 C  CG1   . ILE B 2  227  ? 121.550 132.311 165.265 1.00 48.28  ? 227  ILE B CG1   1 
ATOM   12655 C  CG2   . ILE B 2  227  ? 121.303 130.403 163.669 1.00 48.89  ? 227  ILE B CG2   1 
ATOM   12656 C  CD1   . ILE B 2  227  ? 120.133 132.255 165.793 1.00 48.77  ? 227  ILE B CD1   1 
ATOM   12657 N  N     . ILE B 2  228  ? 123.734 134.383 163.925 1.00 47.84  ? 228  ILE B N     1 
ATOM   12658 C  CA    . ILE B 2  228  ? 123.932 135.816 163.767 1.00 46.93  ? 228  ILE B CA    1 
ATOM   12659 C  C     . ILE B 2  228  ? 125.326 136.192 164.250 1.00 48.24  ? 228  ILE B C     1 
ATOM   12660 O  O     . ILE B 2  228  ? 125.989 135.440 164.966 1.00 49.10  ? 228  ILE B O     1 
ATOM   12661 C  CB    . ILE B 2  228  ? 122.877 136.635 164.525 1.00 45.38  ? 228  ILE B CB    1 
ATOM   12662 C  CG1   . ILE B 2  228  ? 123.320 136.821 165.969 1.00 45.68  ? 228  ILE B CG1   1 
ATOM   12663 C  CG2   . ILE B 2  228  ? 121.527 135.956 164.459 1.00 44.84  ? 228  ILE B CG2   1 
ATOM   12664 C  CD1   . ILE B 2  228  ? 122.289 137.436 166.816 1.00 45.99  ? 228  ILE B CD1   1 
ATOM   12665 N  N     . ARG B 2  229  ? 125.757 137.388 163.855 1.00 42.90  ? 229  ARG B N     1 
ATOM   12666 C  CA    . ARG B 2  229  ? 127.137 137.818 164.042 1.00 42.45  ? 229  ARG B CA    1 
ATOM   12667 C  C     . ARG B 2  229  ? 127.175 139.335 164.060 1.00 44.68  ? 229  ARG B C     1 
ATOM   12668 O  O     . ARG B 2  229  ? 126.728 139.974 163.105 1.00 49.14  ? 229  ARG B O     1 
ATOM   12669 C  CB    . ARG B 2  229  ? 128.018 137.273 162.918 1.00 42.99  ? 229  ARG B CB    1 
ATOM   12670 C  CG    . ARG B 2  229  ? 129.499 137.540 163.065 1.00 41.61  ? 229  ARG B CG    1 
ATOM   12671 C  CD    . ARG B 2  229  ? 130.267 136.830 161.967 1.00 44.55  ? 229  ARG B CD    1 
ATOM   12672 N  NE    . ARG B 2  229  ? 131.705 137.025 162.086 1.00 48.68  ? 229  ARG B NE    1 
ATOM   12673 C  CZ    . ARG B 2  229  ? 132.596 136.587 161.208 1.00 46.51  ? 229  ARG B CZ    1 
ATOM   12674 N  NH1   . ARG B 2  229  ? 132.229 135.949 160.108 1.00 44.89  ? 229  ARG B NH1   1 
ATOM   12675 N  NH2   . ARG B 2  229  ? 133.888 136.796 161.438 1.00 44.37  ? 229  ARG B NH2   1 
ATOM   12676 N  N     . GLY B 2  230  ? 127.703 139.913 165.130 1.00 34.42  ? 230  GLY B N     1 
ATOM   12677 C  CA    . GLY B 2  230  ? 127.864 141.350 165.183 1.00 32.43  ? 230  GLY B CA    1 
ATOM   12678 C  C     . GLY B 2  230  ? 129.319 141.758 165.239 1.00 36.48  ? 230  GLY B C     1 
ATOM   12679 O  O     . GLY B 2  230  ? 129.995 141.480 166.229 1.00 40.01  ? 230  GLY B O     1 
ATOM   12680 N  N     . GLU B 2  231  ? 129.828 142.402 164.194 1.00 35.47  ? 231  GLU B N     1 
ATOM   12681 C  CA    . GLU B 2  231  ? 131.204 142.870 164.190 1.00 36.01  ? 231  GLU B CA    1 
ATOM   12682 C  C     . GLU B 2  231  ? 131.253 144.350 164.538 1.00 35.13  ? 231  GLU B C     1 
ATOM   12683 O  O     . GLU B 2  231  ? 130.251 145.061 164.466 1.00 41.38  ? 231  GLU B O     1 
ATOM   12684 C  CB    . GLU B 2  231  ? 131.886 142.626 162.841 1.00 38.66  ? 231  GLU B CB    1 
ATOM   12685 C  CG    . GLU B 2  231  ? 131.310 141.480 162.032 1.00 40.12  ? 231  GLU B CG    1 
ATOM   12686 C  CD    . GLU B 2  231  ? 131.856 141.444 160.615 1.00 41.42  ? 231  GLU B CD    1 
ATOM   12687 O  OE1   . GLU B 2  231  ? 132.527 140.451 160.260 1.00 42.18  ? 231  GLU B OE1   1 
ATOM   12688 O  OE2   . GLU B 2  231  ? 131.639 142.415 159.863 1.00 41.46  ? 231  GLU B OE2   1 
ATOM   12689 N  N     . PHE B 2  232  ? 132.436 144.796 164.944 1.00 23.65  ? 232  PHE B N     1 
ATOM   12690 C  CA    . PHE B 2  232  ? 132.649 146.165 165.389 1.00 23.94  ? 232  PHE B CA    1 
ATOM   12691 C  C     . PHE B 2  232  ? 134.142 146.426 165.372 1.00 31.13  ? 232  PHE B C     1 
ATOM   12692 O  O     . PHE B 2  232  ? 134.863 145.926 166.236 1.00 36.39  ? 232  PHE B O     1 
ATOM   12693 C  CB    . PHE B 2  232  ? 132.086 146.374 166.797 1.00 22.25  ? 232  PHE B CB    1 
ATOM   12694 C  CG    . PHE B 2  232  ? 131.999 147.811 167.225 1.00 21.98  ? 232  PHE B CG    1 
ATOM   12695 C  CD1   . PHE B 2  232  ? 133.136 148.525 167.539 1.00 26.77  ? 232  PHE B CD1   1 
ATOM   12696 C  CD2   . PHE B 2  232  ? 130.780 148.430 167.369 1.00 25.62  ? 232  PHE B CD2   1 
ATOM   12697 C  CE1   . PHE B 2  232  ? 133.059 149.833 167.949 1.00 27.51  ? 232  PHE B CE1   1 
ATOM   12698 C  CE2   . PHE B 2  232  ? 130.704 149.742 167.780 1.00 26.67  ? 232  PHE B CE2   1 
ATOM   12699 C  CZ    . PHE B 2  232  ? 131.845 150.438 168.073 1.00 25.57  ? 232  PHE B CZ    1 
ATOM   12700 N  N     . ILE B 2  233  ? 134.602 147.212 164.413 1.00 29.03  ? 233  ILE B N     1 
ATOM   12701 C  CA    . ILE B 2  233  ? 136.016 147.534 164.279 1.00 24.91  ? 233  ILE B CA    1 
ATOM   12702 C  C     . ILE B 2  233  ? 136.202 148.902 164.920 1.00 29.19  ? 233  ILE B C     1 
ATOM   12703 O  O     . ILE B 2  233  ? 135.898 149.937 164.326 1.00 35.36  ? 233  ILE B O     1 
ATOM   12704 C  CB    . ILE B 2  233  ? 136.491 147.523 162.826 1.00 26.22  ? 233  ILE B CB    1 
ATOM   12705 C  CG1   . ILE B 2  233  ? 136.601 146.093 162.298 1.00 26.35  ? 233  ILE B CG1   1 
ATOM   12706 C  CG2   . ILE B 2  233  ? 137.842 148.178 162.714 1.00 27.13  ? 233  ILE B CG2   1 
ATOM   12707 C  CD1   . ILE B 2  233  ? 135.312 145.508 161.802 1.00 27.98  ? 233  ILE B CD1   1 
ATOM   12708 N  N     . SER B 2  234  ? 136.694 148.917 166.151 1.00 33.81  ? 234  SER B N     1 
ATOM   12709 C  CA    . SER B 2  234  ? 136.909 150.166 166.861 1.00 36.63  ? 234  SER B CA    1 
ATOM   12710 C  C     . SER B 2  234  ? 138.281 150.736 166.526 1.00 37.34  ? 234  SER B C     1 
ATOM   12711 O  O     . SER B 2  234  ? 139.230 149.999 166.249 1.00 40.16  ? 234  SER B O     1 
ATOM   12712 C  CB    . SER B 2  234  ? 136.782 149.951 168.371 1.00 33.81  ? 234  SER B CB    1 
ATOM   12713 O  OG    . SER B 2  234  ? 137.088 151.134 169.080 1.00 34.14  ? 234  SER B OG    1 
ATOM   12714 N  N     . GLN B 2  235  ? 138.381 152.064 166.550 1.00 34.01  ? 235  GLN B N     1 
ATOM   12715 C  CA    . GLN B 2  235  ? 139.629 152.727 166.202 1.00 36.24  ? 235  GLN B CA    1 
ATOM   12716 C  C     . GLN B 2  235  ? 139.896 153.881 167.159 1.00 39.52  ? 235  GLN B C     1 
ATOM   12717 O  O     . GLN B 2  235  ? 139.043 154.757 167.326 1.00 37.93  ? 235  GLN B O     1 
ATOM   12718 C  CB    . GLN B 2  235  ? 139.584 153.226 164.764 1.00 37.61  ? 235  GLN B CB    1 
ATOM   12719 C  CG    . GLN B 2  235  ? 140.776 154.054 164.343 1.00 38.89  ? 235  GLN B CG    1 
ATOM   12720 C  CD    . GLN B 2  235  ? 141.269 153.684 162.966 1.00 41.53  ? 235  GLN B CD    1 
ATOM   12721 O  OE1   . GLN B 2  235  ? 140.938 152.626 162.442 1.00 41.31  ? 235  GLN B OE1   1 
ATOM   12722 N  NE2   . GLN B 2  235  ? 142.053 154.563 162.365 1.00 39.36  ? 235  GLN B NE2   1 
ATOM   12723 N  N     . PRO B 2  236  ? 141.074 153.909 167.798 1.00 47.72  ? 236  PRO B N     1 
ATOM   12724 C  CA    . PRO B 2  236  ? 141.362 154.887 168.852 1.00 45.35  ? 236  PRO B CA    1 
ATOM   12725 C  C     . PRO B 2  236  ? 141.044 156.343 168.548 1.00 44.87  ? 236  PRO B C     1 
ATOM   12726 O  O     . PRO B 2  236  ? 140.854 157.141 169.471 1.00 45.97  ? 236  PRO B O     1 
ATOM   12727 C  CB    . PRO B 2  236  ? 142.882 154.706 169.029 1.00 43.53  ? 236  PRO B CB    1 
ATOM   12728 C  CG    . PRO B 2  236  ? 143.183 153.347 168.257 1.00 43.89  ? 236  PRO B CG    1 
ATOM   12729 C  CD    . PRO B 2  236  ? 141.850 152.731 168.168 1.00 47.08  ? 236  PRO B CD    1 
ATOM   12730 N  N     . GLY B 2  237  ? 140.963 156.710 167.278 1.00 38.06  ? 237  GLY B N     1 
ATOM   12731 C  CA    . GLY B 2  237  ? 140.749 158.098 166.931 1.00 38.23  ? 237  GLY B CA    1 
ATOM   12732 C  C     . GLY B 2  237  ? 141.816 158.618 165.997 1.00 41.58  ? 237  GLY B C     1 
ATOM   12733 O  O     . GLY B 2  237  ? 142.941 158.917 166.411 1.00 41.73  ? 237  GLY B O     1 
ATOM   12734 N  N     . GLY B 2  238  ? 141.455 158.744 164.732 1.00 36.46  ? 238  GLY B N     1 
ATOM   12735 C  CA    . GLY B 2  238  ? 142.376 159.036 163.659 1.00 37.77  ? 238  GLY B CA    1 
ATOM   12736 C  C     . GLY B 2  238  ? 142.288 158.000 162.551 1.00 40.49  ? 238  GLY B C     1 
ATOM   12737 O  O     . GLY B 2  238  ? 141.825 156.873 162.741 1.00 41.11  ? 238  GLY B O     1 
ATOM   12738 N  N     . ALA B 2  239  ? 142.739 158.404 161.370 1.00 40.53  ? 239  ALA B N     1 
ATOM   12739 C  CA    . ALA B 2  239  ? 142.643 157.565 160.187 1.00 37.64  ? 239  ALA B CA    1 
ATOM   12740 C  C     . ALA B 2  239  ? 143.703 156.477 160.128 1.00 40.24  ? 239  ALA B C     1 
ATOM   12741 O  O     . ALA B 2  239  ? 143.478 155.456 159.470 1.00 38.49  ? 239  ALA B O     1 
ATOM   12742 C  CB    . ALA B 2  239  ? 142.740 158.429 158.927 1.00 36.97  ? 239  ALA B CB    1 
ATOM   12743 N  N     . PHE B 2  240  ? 144.838 156.659 160.805 1.00 45.61  ? 240  PHE B N     1 
ATOM   12744 C  CA    . PHE B 2  240  ? 145.990 155.782 160.647 1.00 45.74  ? 240  PHE B CA    1 
ATOM   12745 C  C     . PHE B 2  240  ? 146.214 154.839 161.820 1.00 47.20  ? 240  PHE B C     1 
ATOM   12746 O  O     . PHE B 2  240  ? 147.083 153.966 161.728 1.00 46.30  ? 240  PHE B O     1 
ATOM   12747 C  CB    . PHE B 2  240  ? 147.263 156.615 160.441 1.00 44.02  ? 240  PHE B CB    1 
ATOM   12748 C  CG    . PHE B 2  240  ? 147.117 157.726 159.440 1.00 45.63  ? 240  PHE B CG    1 
ATOM   12749 C  CD1   . PHE B 2  240  ? 147.186 157.471 158.082 1.00 44.60  ? 240  PHE B CD1   1 
ATOM   12750 C  CD2   . PHE B 2  240  ? 146.927 159.029 159.860 1.00 45.53  ? 240  PHE B CD2   1 
ATOM   12751 C  CE1   . PHE B 2  240  ? 147.065 158.493 157.166 1.00 45.78  ? 240  PHE B CE1   1 
ATOM   12752 C  CE2   . PHE B 2  240  ? 146.796 160.056 158.943 1.00 46.13  ? 240  PHE B CE2   1 
ATOM   12753 C  CZ    . PHE B 2  240  ? 146.867 159.786 157.598 1.00 46.12  ? 240  PHE B CZ    1 
ATOM   12754 N  N     . GLU B 2  241  ? 145.452 154.978 162.900 1.00 47.68  ? 241  GLU B N     1 
ATOM   12755 C  CA    . GLU B 2  241  ? 145.664 154.202 164.113 1.00 43.93  ? 241  GLU B CA    1 
ATOM   12756 C  C     . GLU B 2  241  ? 145.345 152.730 163.880 1.00 48.96  ? 241  GLU B C     1 
ATOM   12757 O  O     . GLU B 2  241  ? 144.726 152.348 162.883 1.00 47.59  ? 241  GLU B O     1 
ATOM   12758 C  CB    . GLU B 2  241  ? 144.792 154.748 165.240 1.00 45.43  ? 241  GLU B CB    1 
ATOM   12759 C  CG    . GLU B 2  241  ? 144.870 156.252 165.385 1.00 46.17  ? 241  GLU B CG    1 
ATOM   12760 C  CD    . GLU B 2  241  ? 146.051 156.699 166.213 1.00 47.74  ? 241  GLU B CD    1 
ATOM   12761 O  OE1   . GLU B 2  241  ? 147.183 156.616 165.712 1.00 47.76  ? 241  GLU B OE1   1 
ATOM   12762 O  OE2   . GLU B 2  241  ? 145.844 157.166 167.351 1.00 47.93  ? 241  GLU B OE2   1 
ATOM   12763 N  N     . ASN B 2  242  ? 145.795 151.892 164.809 1.00 51.11  ? 242  ASN B N     1 
ATOM   12764 C  CA    . ASN B 2  242  ? 145.487 150.472 164.727 1.00 49.02  ? 242  ASN B CA    1 
ATOM   12765 C  C     . ASN B 2  242  ? 144.080 150.199 165.247 1.00 47.44  ? 242  ASN B C     1 
ATOM   12766 O  O     . ASN B 2  242  ? 143.626 150.793 166.228 1.00 46.94  ? 242  ASN B O     1 
ATOM   12767 C  CB    . ASN B 2  242  ? 146.504 149.647 165.510 1.00 45.53  ? 242  ASN B CB    1 
ATOM   12768 C  CG    . ASN B 2  242  ? 146.510 148.188 165.086 1.00 50.05  ? 242  ASN B CG    1 
ATOM   12769 O  OD1   . ASN B 2  242  ? 146.317 147.870 163.911 1.00 51.05  ? 242  ASN B OD1   1 
ATOM   12770 N  ND2   . ASN B 2  242  ? 146.729 147.293 166.042 1.00 48.59  ? 242  ASN B ND2   1 
ATOM   12771 N  N     . SER B 2  243  ? 143.393 149.277 164.582 1.00 41.46  ? 243  SER B N     1 
ATOM   12772 C  CA    . SER B 2  243  ? 141.988 149.002 164.840 1.00 41.14  ? 243  SER B CA    1 
ATOM   12773 C  C     . SER B 2  243  ? 141.829 147.613 165.441 1.00 41.28  ? 243  SER B C     1 
ATOM   12774 O  O     . SER B 2  243  ? 142.456 146.656 164.979 1.00 42.00  ? 243  SER B O     1 
ATOM   12775 C  CB    . SER B 2  243  ? 141.172 149.113 163.553 1.00 41.54  ? 243  SER B CB    1 
ATOM   12776 O  OG    . SER B 2  243  ? 141.186 150.436 163.051 1.00 43.68  ? 243  SER B OG    1 
ATOM   12777 N  N     . SER B 2  244  ? 140.976 147.506 166.453 1.00 36.62  ? 244  SER B N     1 
ATOM   12778 C  CA    . SER B 2  244  ? 140.694 146.243 167.118 1.00 38.86  ? 244  SER B CA    1 
ATOM   12779 C  C     . SER B 2  244  ? 139.274 145.808 166.785 1.00 39.32  ? 244  SER B C     1 
ATOM   12780 O  O     . SER B 2  244  ? 138.318 146.541 167.051 1.00 38.12  ? 244  SER B O     1 
ATOM   12781 C  CB    . SER B 2  244  ? 140.856 146.372 168.628 1.00 40.69  ? 244  SER B CB    1 
ATOM   12782 O  OG    . SER B 2  244  ? 139.807 147.151 169.161 1.00 41.89  ? 244  SER B OG    1 
ATOM   12783 N  N     . GLN B 2  245  ? 139.142 144.611 166.231 1.00 38.00  ? 245  GLN B N     1 
ATOM   12784 C  CA    . GLN B 2  245  ? 137.851 144.041 165.890 1.00 36.27  ? 245  GLN B CA    1 
ATOM   12785 C  C     . GLN B 2  245  ? 137.341 143.180 167.036 1.00 37.43  ? 245  GLN B C     1 
ATOM   12786 O  O     . GLN B 2  245  ? 138.085 142.374 167.596 1.00 41.33  ? 245  GLN B O     1 
ATOM   12787 C  CB    . GLN B 2  245  ? 137.979 143.202 164.617 1.00 34.12  ? 245  GLN B CB    1 
ATOM   12788 C  CG    . GLN B 2  245  ? 136.748 142.427 164.211 1.00 33.88  ? 245  GLN B CG    1 
ATOM   12789 C  CD    . GLN B 2  245  ? 136.971 141.665 162.920 1.00 38.46  ? 245  GLN B CD    1 
ATOM   12790 O  OE1   . GLN B 2  245  ? 138.030 141.770 162.307 1.00 40.63  ? 245  GLN B OE1   1 
ATOM   12791 N  NE2   . GLN B 2  245  ? 135.976 140.896 162.499 1.00 36.64  ? 245  GLN B NE2   1 
ATOM   12792 N  N     . ILE B 2  246  ? 136.072 143.355 167.392 1.00 33.11  ? 246  ILE B N     1 
ATOM   12793 C  CA    . ILE B 2  246  ? 135.406 142.457 168.328 1.00 34.87  ? 246  ILE B CA    1 
ATOM   12794 C  C     . ILE B 2  246  ? 134.190 141.877 167.630 1.00 29.99  ? 246  ILE B C     1 
ATOM   12795 O  O     . ILE B 2  246  ? 133.548 142.557 166.824 1.00 34.74  ? 246  ILE B O     1 
ATOM   12796 C  CB    . ILE B 2  246  ? 134.986 143.147 169.640 1.00 31.33  ? 246  ILE B CB    1 
ATOM   12797 C  CG1   . ILE B 2  246  ? 133.902 144.184 169.400 1.00 29.40  ? 246  ILE B CG1   1 
ATOM   12798 C  CG2   . ILE B 2  246  ? 136.178 143.818 170.293 1.00 34.97  ? 246  ILE B CG2   1 
ATOM   12799 C  CD1   . ILE B 2  246  ? 133.260 144.657 170.669 1.00 30.14  ? 246  ILE B CD1   1 
ATOM   12800 N  N     . ILE B 2  247  ? 133.888 140.618 167.914 1.00 31.17  ? 247  ILE B N     1 
ATOM   12801 C  CA    . ILE B 2  247  ? 132.728 139.945 167.351 1.00 35.68  ? 247  ILE B CA    1 
ATOM   12802 C  C     . ILE B 2  247  ? 131.873 139.430 168.497 1.00 35.57  ? 247  ILE B C     1 
ATOM   12803 O  O     . ILE B 2  247  ? 132.371 138.725 169.379 1.00 43.91  ? 247  ILE B O     1 
ATOM   12804 C  CB    . ILE B 2  247  ? 133.136 138.800 166.408 1.00 36.36  ? 247  ILE B CB    1 
ATOM   12805 C  CG1   . ILE B 2  247  ? 134.036 139.332 165.294 1.00 38.11  ? 247  ILE B CG1   1 
ATOM   12806 C  CG2   . ILE B 2  247  ? 131.914 138.140 165.827 1.00 37.09  ? 247  ILE B CG2   1 
ATOM   12807 C  CD1   . ILE B 2  247  ? 134.782 138.261 164.545 1.00 35.38  ? 247  ILE B CD1   1 
ATOM   12808 N  N     . ILE B 2  248  ? 130.595 139.787 168.482 1.00 30.45  ? 248  ILE B N     1 
ATOM   12809 C  CA    . ILE B 2  248  ? 129.618 139.330 169.462 1.00 31.69  ? 248  ILE B CA    1 
ATOM   12810 C  C     . ILE B 2  248  ? 128.653 138.408 168.736 1.00 32.81  ? 248  ILE B C     1 
ATOM   12811 O  O     . ILE B 2  248  ? 127.713 138.873 168.083 1.00 35.57  ? 248  ILE B O     1 
ATOM   12812 C  CB    . ILE B 2  248  ? 128.875 140.503 170.110 1.00 30.79  ? 248  ILE B CB    1 
ATOM   12813 C  CG1   . ILE B 2  248  ? 129.849 141.383 170.883 1.00 30.58  ? 248  ILE B CG1   1 
ATOM   12814 C  CG2   . ILE B 2  248  ? 127.766 140.005 171.012 1.00 29.53  ? 248  ILE B CG2   1 
ATOM   12815 C  CD1   . ILE B 2  248  ? 129.275 142.707 171.282 1.00 33.01  ? 248  ILE B CD1   1 
ATOM   12816 N  N     . ARG B 2  249  ? 128.869 137.103 168.848 1.00 41.06  ? 249  ARG B N     1 
ATOM   12817 C  CA    . ARG B 2  249  ? 128.081 136.123 168.117 1.00 44.23  ? 249  ARG B CA    1 
ATOM   12818 C  C     . ARG B 2  249  ? 127.113 135.406 169.048 1.00 45.02  ? 249  ARG B C     1 
ATOM   12819 O  O     . ARG B 2  249  ? 127.336 135.309 170.255 1.00 43.44  ? 249  ARG B O     1 
ATOM   12820 C  CB    . ARG B 2  249  ? 128.982 135.105 167.416 1.00 40.72  ? 249  ARG B CB    1 
ATOM   12821 C  CG    . ARG B 2  249  ? 130.044 134.547 168.312 1.00 43.45  ? 249  ARG B CG    1 
ATOM   12822 C  CD    . ARG B 2  249  ? 131.424 134.597 167.689 1.00 45.49  ? 249  ARG B CD    1 
ATOM   12823 N  NE    . ARG B 2  249  ? 131.475 133.946 166.387 1.00 43.87  ? 249  ARG B NE    1 
ATOM   12824 C  CZ    . ARG B 2  249  ? 132.417 134.166 165.483 1.00 43.18  ? 249  ARG B CZ    1 
ATOM   12825 N  NH1   . ARG B 2  249  ? 133.413 135.002 165.717 1.00 45.40  ? 249  ARG B NH1   1 
ATOM   12826 N  NH2   . ARG B 2  249  ? 132.363 133.524 164.320 1.00 40.93  ? 249  ARG B NH2   1 
ATOM   12827 N  N     . TYR B 2  250  ? 126.025 134.916 168.463 1.00 46.52  ? 250  TYR B N     1 
ATOM   12828 C  CA    . TYR B 2  250  ? 124.957 134.227 169.172 1.00 46.63  ? 250  TYR B CA    1 
ATOM   12829 C  C     . TYR B 2  250  ? 124.717 132.892 168.487 1.00 49.68  ? 250  TYR B C     1 
ATOM   12830 O  O     . TYR B 2  250  ? 124.467 132.852 167.277 1.00 50.80  ? 250  TYR B O     1 
ATOM   12831 C  CB    . TYR B 2  250  ? 123.688 135.083 169.171 1.00 46.29  ? 250  TYR B CB    1 
ATOM   12832 C  CG    . TYR B 2  250  ? 122.460 134.473 169.803 1.00 49.48  ? 250  TYR B CG    1 
ATOM   12833 C  CD1   . TYR B 2  250  ? 122.442 134.111 171.136 1.00 46.28  ? 250  TYR B CD1   1 
ATOM   12834 C  CD2   . TYR B 2  250  ? 121.298 134.299 169.066 1.00 49.73  ? 250  TYR B CD2   1 
ATOM   12835 C  CE1   . TYR B 2  250  ? 121.311 133.571 171.711 1.00 47.13  ? 250  TYR B CE1   1 
ATOM   12836 C  CE2   . TYR B 2  250  ? 120.165 133.762 169.631 1.00 46.83  ? 250  TYR B CE2   1 
ATOM   12837 C  CZ    . TYR B 2  250  ? 120.174 133.399 170.953 1.00 47.29  ? 250  TYR B CZ    1 
ATOM   12838 O  OH    . TYR B 2  250  ? 119.040 132.864 171.517 1.00 48.13  ? 250  TYR B OH    1 
ATOM   12839 N  N     . MET B 2  251  ? 124.791 131.807 169.252 1.00 47.12  ? 251  MET B N     1 
ATOM   12840 C  CA    . MET B 2  251  ? 124.699 130.456 168.716 1.00 47.50  ? 251  MET B CA    1 
ATOM   12841 C  C     . MET B 2  251  ? 123.322 129.861 168.975 1.00 46.92  ? 251  MET B C     1 
ATOM   12842 O  O     . MET B 2  251  ? 122.502 130.417 169.706 1.00 44.61  ? 251  MET B O     1 
ATOM   12843 C  CB    . MET B 2  251  ? 125.783 129.555 169.314 1.00 45.96  ? 251  MET B CB    1 
ATOM   12844 C  CG    . MET B 2  251  ? 127.108 129.623 168.595 1.00 45.92  ? 251  MET B CG    1 
ATOM   12845 S  SD    . MET B 2  251  ? 128.245 130.806 169.318 1.00 54.74  ? 251  MET B SD    1 
ATOM   12846 C  CE    . MET B 2  251  ? 129.769 130.273 168.545 1.00 47.30  ? 251  MET B CE    1 
ATOM   12847 N  N     . THR B 2  252  ? 123.075 128.707 168.347 1.00 45.00  ? 252  THR B N     1 
ATOM   12848 C  CA    . THR B 2  252  ? 121.783 128.046 168.501 1.00 45.42  ? 252  THR B CA    1 
ATOM   12849 C  C     . THR B 2  252  ? 121.587 127.541 169.923 1.00 43.06  ? 252  THR B C     1 
ATOM   12850 O  O     . THR B 2  252  ? 120.460 127.518 170.431 1.00 42.41  ? 252  THR B O     1 
ATOM   12851 C  CB    . THR B 2  252  ? 121.646 126.892 167.505 1.00 46.73  ? 252  THR B CB    1 
ATOM   12852 O  OG1   . THR B 2  252  ? 122.807 126.056 167.568 1.00 46.46  ? 252  THR B OG1   1 
ATOM   12853 C  CG2   . THR B 2  252  ? 121.475 127.423 166.092 1.00 41.03  ? 252  THR B CG2   1 
ATOM   12854 N  N     . THR B 2  253  ? 122.674 127.121 170.578 1.00 39.23  ? 253  THR B N     1 
ATOM   12855 C  CA    . THR B 2  253  ? 122.571 126.644 171.953 1.00 42.57  ? 253  THR B CA    1 
ATOM   12856 C  C     . THR B 2  253  ? 122.047 127.736 172.875 1.00 41.34  ? 253  THR B C     1 
ATOM   12857 O  O     . THR B 2  253  ? 121.155 127.494 173.694 1.00 40.30  ? 253  THR B O     1 
ATOM   12858 C  CB    . THR B 2  253  ? 123.932 126.153 172.442 1.00 39.70  ? 253  THR B CB    1 
ATOM   12859 O  OG1   . THR B 2  253  ? 124.738 127.278 172.812 1.00 38.25  ? 253  THR B OG1   1 
ATOM   12860 C  CG2   . THR B 2  253  ? 124.644 125.388 171.344 1.00 37.72  ? 253  THR B CG2   1 
ATOM   12861 N  N     . GLY B 2  254  ? 122.569 128.950 172.737 1.00 38.30  ? 254  GLY B N     1 
ATOM   12862 C  CA    . GLY B 2  254  ? 122.136 130.063 173.555 1.00 39.36  ? 254  GLY B CA    1 
ATOM   12863 C  C     . GLY B 2  254  ? 123.299 130.903 174.035 1.00 40.44  ? 254  GLY B C     1 
ATOM   12864 O  O     . GLY B 2  254  ? 123.111 132.012 174.538 1.00 42.26  ? 254  GLY B O     1 
ATOM   12865 N  N     . ALA B 2  255  ? 124.509 130.381 173.876 1.00 42.17  ? 255  ALA B N     1 
ATOM   12866 C  CA    . ALA B 2  255  ? 125.697 131.095 174.312 1.00 41.09  ? 255  ALA B CA    1 
ATOM   12867 C  C     . ALA B 2  255  ? 125.917 132.351 173.481 1.00 43.18  ? 255  ALA B C     1 
ATOM   12868 O  O     . ALA B 2  255  ? 125.802 132.336 172.253 1.00 42.78  ? 255  ALA B O     1 
ATOM   12869 C  CB    . ALA B 2  255  ? 126.923 130.190 174.213 1.00 38.69  ? 255  ALA B CB    1 
ATOM   12870 N  N     . ILE B 2  256  ? 126.243 133.442 174.161 1.00 44.20  ? 256  ILE B N     1 
ATOM   12871 C  CA    . ILE B 2  256  ? 126.652 134.686 173.526 1.00 41.46  ? 256  ILE B CA    1 
ATOM   12872 C  C     . ILE B 2  256  ? 128.120 134.881 173.862 1.00 40.58  ? 256  ILE B C     1 
ATOM   12873 O  O     . ILE B 2  256  ? 128.459 135.334 174.960 1.00 39.59  ? 256  ILE B O     1 
ATOM   12874 C  CB    . ILE B 2  256  ? 125.808 135.875 173.998 1.00 40.70  ? 256  ILE B CB    1 
ATOM   12875 C  CG1   . ILE B 2  256  ? 124.339 135.665 173.635 1.00 41.00  ? 256  ILE B CG1   1 
ATOM   12876 C  CG2   . ILE B 2  256  ? 126.339 137.171 173.416 1.00 40.77  ? 256  ILE B CG2   1 
ATOM   12877 C  CD1   . ILE B 2  256  ? 123.383 136.458 174.495 1.00 41.94  ? 256  ILE B CD1   1 
ATOM   12878 N  N     . THR B 2  257  ? 128.995 134.545 172.922 1.00 40.93  ? 257  THR B N     1 
ATOM   12879 C  CA    . THR B 2  257  ? 130.427 134.586 173.152 1.00 41.68  ? 257  THR B CA    1 
ATOM   12880 C  C     . THR B 2  257  ? 131.035 135.756 172.393 1.00 40.54  ? 257  THR B C     1 
ATOM   12881 O  O     . THR B 2  257  ? 130.504 136.210 171.379 1.00 42.14  ? 257  THR B O     1 
ATOM   12882 C  CB    . THR B 2  257  ? 131.095 133.264 172.741 1.00 44.85  ? 257  THR B CB    1 
ATOM   12883 O  OG1   . THR B 2  257  ? 132.507 133.341 172.970 1.00 45.77  ? 257  THR B OG1   1 
ATOM   12884 C  CG2   . THR B 2  257  ? 130.839 132.962 171.282 1.00 41.12  ? 257  THR B CG2   1 
ATOM   12885 N  N     . ILE B 2  258  ? 132.156 136.251 172.908 1.00 38.07  ? 258  ILE B N     1 
ATOM   12886 C  CA    . ILE B 2  258  ? 132.797 137.464 172.415 1.00 36.87  ? 258  ILE B CA    1 
ATOM   12887 C  C     . ILE B 2  258  ? 134.221 137.132 171.997 1.00 40.24  ? 258  ILE B C     1 
ATOM   12888 O  O     . ILE B 2  258  ? 134.976 136.537 172.772 1.00 42.88  ? 258  ILE B O     1 
ATOM   12889 C  CB    . ILE B 2  258  ? 132.790 138.576 173.480 1.00 39.47  ? 258  ILE B CB    1 
ATOM   12890 C  CG1   . ILE B 2  258  ? 131.368 139.096 173.685 1.00 38.06  ? 258  ILE B CG1   1 
ATOM   12891 C  CG2   . ILE B 2  258  ? 133.750 139.690 173.108 1.00 38.17  ? 258  ILE B CG2   1 
ATOM   12892 C  CD1   . ILE B 2  258  ? 131.248 140.145 174.756 1.00 38.46  ? 258  ILE B CD1   1 
ATOM   12893 N  N     . GLU B 2  259  ? 134.585 137.520 170.781 1.00 40.53  ? 259  GLU B N     1 
ATOM   12894 C  CA    . GLU B 2  259  ? 135.909 137.286 170.225 1.00 42.38  ? 259  GLU B CA    1 
ATOM   12895 C  C     . GLU B 2  259  ? 136.593 138.627 170.009 1.00 42.40  ? 259  GLU B C     1 
ATOM   12896 O  O     . GLU B 2  259  ? 135.921 139.643 169.823 1.00 47.54  ? 259  GLU B O     1 
ATOM   12897 C  CB    . GLU B 2  259  ? 135.812 136.511 168.905 1.00 42.18  ? 259  GLU B CB    1 
ATOM   12898 C  CG    . GLU B 2  259  ? 137.069 136.520 168.060 1.00 43.70  ? 259  GLU B CG    1 
ATOM   12899 C  CD    . GLU B 2  259  ? 136.889 135.828 166.727 1.00 47.29  ? 259  GLU B CD    1 
ATOM   12900 O  OE1   . GLU B 2  259  ? 135.862 135.146 166.537 1.00 47.70  ? 259  GLU B OE1   1 
ATOM   12901 O  OE2   . GLU B 2  259  ? 137.781 135.965 165.867 1.00 46.82  ? 259  GLU B OE2   1 
ATOM   12902 N  N     . ILE B 2  260  ? 137.917 138.649 170.081 1.00 37.09  ? 260  ILE B N     1 
ATOM   12903 C  CA    . ILE B 2  260  ? 138.689 139.856 169.790 1.00 39.28  ? 260  ILE B CA    1 
ATOM   12904 C  C     . ILE B 2  260  ? 139.785 139.477 168.800 1.00 42.38  ? 260  ILE B C     1 
ATOM   12905 O  O     . ILE B 2  260  ? 140.881 139.063 169.187 1.00 45.13  ? 260  ILE B O     1 
ATOM   12906 C  CB    . ILE B 2  260  ? 139.270 140.502 171.049 1.00 39.43  ? 260  ILE B CB    1 
ATOM   12907 C  CG1   . ILE B 2  260  ? 138.162 140.789 172.060 1.00 39.20  ? 260  ILE B CG1   1 
ATOM   12908 C  CG2   . ILE B 2  260  ? 139.994 141.784 170.696 1.00 38.95  ? 260  ILE B CG2   1 
ATOM   12909 C  CD1   . ILE B 2  260  ? 138.670 141.247 173.397 1.00 41.18  ? 260  ILE B CD1   1 
ATOM   12910 N  N     . ASN B 2  261  ? 139.503 139.645 167.508 1.00 44.43  ? 261  ASN B N     1 
ATOM   12911 C  CA    . ASN B 2  261  ? 140.535 139.550 166.484 1.00 43.84  ? 261  ASN B CA    1 
ATOM   12912 C  C     . ASN B 2  261  ? 141.483 140.736 166.607 1.00 44.72  ? 261  ASN B C     1 
ATOM   12913 O  O     . ASN B 2  261  ? 141.060 141.891 166.503 1.00 45.33  ? 261  ASN B O     1 
ATOM   12914 C  CB    . ASN B 2  261  ? 139.915 139.526 165.086 1.00 43.51  ? 261  ASN B CB    1 
ATOM   12915 C  CG    . ASN B 2  261  ? 139.754 138.120 164.526 1.00 46.07  ? 261  ASN B CG    1 
ATOM   12916 O  OD1   . ASN B 2  261  ? 140.641 137.279 164.656 1.00 47.47  ? 261  ASN B OD1   1 
ATOM   12917 N  ND2   . ASN B 2  261  ? 138.623 137.867 163.885 1.00 43.47  ? 261  ASN B ND2   1 
ATOM   12918 N  N     . SER B 2  262  ? 142.760 140.452 166.839 1.00 44.39  ? 262  SER B N     1 
ATOM   12919 C  CA    . SER B 2  262  ? 143.801 141.475 166.862 1.00 44.30  ? 262  SER B CA    1 
ATOM   12920 C  C     . SER B 2  262  ? 145.147 140.768 166.748 1.00 46.54  ? 262  SER B C     1 
ATOM   12921 O  O     . SER B 2  262  ? 145.218 139.541 166.634 1.00 46.67  ? 262  SER B O     1 
ATOM   12922 C  CB    . SER B 2  262  ? 143.725 142.351 168.117 1.00 41.59  ? 262  SER B CB    1 
ATOM   12923 O  OG    . SER B 2  262  ? 143.771 141.574 169.301 1.00 42.99  ? 262  SER B OG    1 
ATOM   12924 N  N     . THR B 2  263  ? 146.219 141.562 166.775 1.00 43.55  ? 263  THR B N     1 
ATOM   12925 C  CA    . THR B 2  263  ? 147.566 141.018 166.622 1.00 43.77  ? 263  THR B CA    1 
ATOM   12926 C  C     . THR B 2  263  ? 147.960 140.130 167.800 1.00 43.49  ? 263  THR B C     1 
ATOM   12927 O  O     . THR B 2  263  ? 148.486 139.028 167.602 1.00 41.46  ? 263  THR B O     1 
ATOM   12928 C  CB    . THR B 2  263  ? 148.567 142.164 166.454 1.00 43.16  ? 263  THR B CB    1 
ATOM   12929 O  OG1   . THR B 2  263  ? 148.418 142.747 165.152 1.00 42.63  ? 263  THR B OG1   1 
ATOM   12930 C  CG2   . THR B 2  263  ? 149.999 141.683 166.650 1.00 39.14  ? 263  THR B CG2   1 
ATOM   12931 N  N     . LYS B 2  264  ? 147.712 140.586 169.030 1.00 42.96  ? 264  LYS B N     1 
ATOM   12932 C  CA    . LYS B 2  264  ? 148.223 139.865 170.192 1.00 43.92  ? 264  LYS B CA    1 
ATOM   12933 C  C     . LYS B 2  264  ? 147.524 138.525 170.376 1.00 43.58  ? 264  LYS B C     1 
ATOM   12934 O  O     . LYS B 2  264  ? 148.126 137.566 170.871 1.00 43.95  ? 264  LYS B O     1 
ATOM   12935 C  CB    . LYS B 2  264  ? 148.081 140.716 171.453 1.00 43.22  ? 264  LYS B CB    1 
ATOM   12936 C  CG    . LYS B 2  264  ? 149.299 141.568 171.760 1.00 42.14  ? 264  LYS B CG    1 
ATOM   12937 C  CD    . LYS B 2  264  ? 149.243 142.902 171.040 1.00 43.35  ? 264  LYS B CD    1 
ATOM   12938 C  CE    . LYS B 2  264  ? 148.265 143.838 171.725 1.00 40.97  ? 264  LYS B CE    1 
ATOM   12939 N  NZ    . LYS B 2  264  ? 148.255 145.183 171.109 1.00 44.46  ? 264  LYS B NZ    1 
ATOM   12940 N  N     . PHE B 2  265  ? 146.257 138.442 170.000 1.00 48.98  ? 265  PHE B N     1 
ATOM   12941 C  CA    . PHE B 2  265  ? 145.467 137.241 170.198 1.00 50.38  ? 265  PHE B CA    1 
ATOM   12942 C  C     . PHE B 2  265  ? 145.135 136.591 168.858 1.00 52.14  ? 265  PHE B C     1 
ATOM   12943 O  O     . PHE B 2  265  ? 145.544 137.054 167.791 1.00 49.33  ? 265  PHE B O     1 
ATOM   12944 C  CB    . PHE B 2  265  ? 144.209 137.584 170.990 1.00 50.87  ? 265  PHE B CB    1 
ATOM   12945 C  CG    . PHE B 2  265  ? 144.496 138.103 172.362 1.00 50.47  ? 265  PHE B CG    1 
ATOM   12946 C  CD1   . PHE B 2  265  ? 144.746 137.230 173.405 1.00 51.43  ? 265  PHE B CD1   1 
ATOM   12947 C  CD2   . PHE B 2  265  ? 144.554 139.461 172.604 1.00 50.34  ? 265  PHE B CD2   1 
ATOM   12948 C  CE1   . PHE B 2  265  ? 145.026 137.706 174.675 1.00 51.95  ? 265  PHE B CE1   1 
ATOM   12949 C  CE2   . PHE B 2  265  ? 144.836 139.940 173.869 1.00 51.77  ? 265  PHE B CE2   1 
ATOM   12950 C  CZ    . PHE B 2  265  ? 145.069 139.062 174.905 1.00 52.33  ? 265  PHE B CZ    1 
ATOM   12951 N  N     . SER B 2  266  ? 144.390 135.486 168.921 1.00 51.93  ? 266  SER B N     1 
ATOM   12952 C  CA    . SER B 2  266  ? 143.981 134.770 167.712 1.00 48.39  ? 266  SER B CA    1 
ATOM   12953 C  C     . SER B 2  266  ? 142.609 134.148 167.976 1.00 46.88  ? 266  SER B C     1 
ATOM   12954 O  O     . SER B 2  266  ? 142.512 133.049 168.525 1.00 48.31  ? 266  SER B O     1 
ATOM   12955 C  CB    . SER B 2  266  ? 144.998 133.711 167.313 1.00 47.80  ? 266  SER B CB    1 
ATOM   12956 O  OG    . SER B 2  266  ? 145.050 132.668 168.270 1.00 47.77  ? 266  SER B OG    1 
ATOM   12957 N  N     . LYS B 2  267  ? 141.564 134.867 167.566 1.00 49.39  ? 267  LYS B N     1 
ATOM   12958 C  CA    . LYS B 2  267  ? 140.197 134.343 167.475 1.00 50.35  ? 267  LYS B CA    1 
ATOM   12959 C  C     . LYS B 2  267  ? 139.817 133.475 168.677 1.00 49.47  ? 267  LYS B C     1 
ATOM   12960 O  O     . LYS B 2  267  ? 139.236 132.396 168.539 1.00 46.90  ? 267  LYS B O     1 
ATOM   12961 C  CB    . LYS B 2  267  ? 139.991 133.597 166.147 1.00 47.04  ? 267  LYS B CB    1 
ATOM   12962 C  CG    . LYS B 2  267  ? 140.854 132.355 165.917 1.00 47.87  ? 267  LYS B CG    1 
ATOM   12963 C  CD    . LYS B 2  267  ? 140.614 131.764 164.538 1.00 48.46  ? 267  LYS B CD    1 
ATOM   12964 C  CE    . LYS B 2  267  ? 141.498 130.555 164.299 1.00 48.82  ? 267  LYS B CE    1 
ATOM   12965 N  NZ    . LYS B 2  267  ? 141.154 129.429 165.210 1.00 49.27  ? 267  LYS B NZ    1 
ATOM   12966 N  N     . LEU B 2  268  ? 140.138 133.958 169.877 1.00 49.87  ? 268  LEU B N     1 
ATOM   12967 C  CA    . LEU B 2  268  ? 139.680 133.310 171.097 1.00 50.66  ? 268  LEU B CA    1 
ATOM   12968 C  C     . LEU B 2  268  ? 138.274 133.796 171.415 1.00 49.16  ? 268  LEU B C     1 
ATOM   12969 O  O     . LEU B 2  268  ? 137.989 134.993 171.339 1.00 47.77  ? 268  LEU B O     1 
ATOM   12970 C  CB    . LEU B 2  268  ? 140.610 133.607 172.276 1.00 49.46  ? 268  LEU B CB    1 
ATOM   12971 C  CG    . LEU B 2  268  ? 140.531 134.991 172.930 1.00 49.42  ? 268  LEU B CG    1 
ATOM   12972 C  CD1   . LEU B 2  268  ? 140.751 134.887 174.433 1.00 47.84  ? 268  LEU B CD1   1 
ATOM   12973 C  CD2   . LEU B 2  268  ? 141.499 135.965 172.297 1.00 47.58  ? 268  LEU B CD2   1 
ATOM   12974 N  N     . ARG B 2  269  ? 137.391 132.865 171.757 1.00 52.37  ? 269  ARG B N     1 
ATOM   12975 C  CA    . ARG B 2  269  ? 135.999 133.187 172.042 1.00 51.35  ? 269  ARG B CA    1 
ATOM   12976 C  C     . ARG B 2  269  ? 135.756 133.105 173.539 1.00 50.22  ? 269  ARG B C     1 
ATOM   12977 O  O     . ARG B 2  269  ? 136.009 132.069 174.162 1.00 53.31  ? 269  ARG B O     1 
ATOM   12978 C  CB    . ARG B 2  269  ? 135.035 132.278 171.276 1.00 48.81  ? 269  ARG B CB    1 
ATOM   12979 C  CG    . ARG B 2  269  ? 134.984 132.598 169.788 1.00 52.82  ? 269  ARG B CG    1 
ATOM   12980 C  CD    . ARG B 2  269  ? 133.674 132.161 169.134 1.00 53.29  ? 269  ARG B CD    1 
ATOM   12981 N  NE    . ARG B 2  269  ? 133.590 130.740 168.834 1.00 54.93  ? 269  ARG B NE    1 
ATOM   12982 C  CZ    . ARG B 2  269  ? 133.996 130.212 167.688 1.00 54.11  ? 269  ARG B CZ    1 
ATOM   12983 N  NH1   . ARG B 2  269  ? 134.536 130.961 166.739 1.00 50.75  ? 269  ARG B NH1   1 
ATOM   12984 N  NH2   . ARG B 2  269  ? 133.861 128.904 167.490 1.00 52.71  ? 269  ARG B NH2   1 
ATOM   12985 N  N     . ILE B 2  270  ? 135.266 134.200 174.105 1.00 40.23  ? 270  ILE B N     1 
ATOM   12986 C  CA    . ILE B 2  270  ? 134.971 134.311 175.527 1.00 41.56  ? 270  ILE B CA    1 
ATOM   12987 C  C     . ILE B 2  270  ? 133.476 134.520 175.673 1.00 43.96  ? 270  ILE B C     1 
ATOM   12988 O  O     . ILE B 2  270  ? 132.909 135.362 174.974 1.00 44.39  ? 270  ILE B O     1 
ATOM   12989 C  CB    . ILE B 2  270  ? 135.733 135.473 176.190 1.00 40.44  ? 270  ILE B CB    1 
ATOM   12990 C  CG1   . ILE B 2  270  ? 137.220 135.396 175.850 1.00 42.69  ? 270  ILE B CG1   1 
ATOM   12991 C  CG2   . ILE B 2  270  ? 135.487 135.475 177.684 1.00 39.68  ? 270  ILE B CG2   1 
ATOM   12992 C  CD1   . ILE B 2  270  ? 137.983 136.686 176.107 1.00 41.11  ? 270  ILE B CD1   1 
ATOM   12993 N  N     . PRO B 2  271  ? 132.790 133.783 176.542 1.00 42.76  ? 271  PRO B N     1 
ATOM   12994 C  CA    . PRO B 2  271  ? 131.396 134.111 176.842 1.00 41.25  ? 271  PRO B CA    1 
ATOM   12995 C  C     . PRO B 2  271  ? 131.269 135.506 177.437 1.00 40.69  ? 271  PRO B C     1 
ATOM   12996 O  O     . PRO B 2  271  ? 132.173 136.019 178.098 1.00 40.50  ? 271  PRO B O     1 
ATOM   12997 C  CB    . PRO B 2  271  ? 131.021 133.017 177.858 1.00 38.98  ? 271  PRO B CB    1 
ATOM   12998 C  CG    . PRO B 2  271  ? 132.429 132.542 178.287 1.00 43.05  ? 271  PRO B CG    1 
ATOM   12999 C  CD    . PRO B 2  271  ? 132.970 132.389 176.953 1.00 41.85  ? 271  PRO B CD    1 
ATOM   13000 N  N     . TRP B 2  272  ? 130.118 136.127 177.181 1.00 41.48  ? 272  TRP B N     1 
ATOM   13001 C  CA    . TRP B 2  272  ? 129.932 137.547 177.455 1.00 42.80  ? 272  TRP B CA    1 
ATOM   13002 C  C     . TRP B 2  272  ? 129.913 137.893 178.935 1.00 44.99  ? 272  TRP B C     1 
ATOM   13003 O  O     . TRP B 2  272  ? 130.349 138.992 179.294 1.00 45.79  ? 272  TRP B O     1 
ATOM   13004 C  CB    . TRP B 2  272  ? 128.650 138.035 176.787 1.00 42.35  ? 272  TRP B CB    1 
ATOM   13005 C  CG    . TRP B 2  272  ? 127.393 137.618 177.467 1.00 40.77  ? 272  TRP B CG    1 
ATOM   13006 C  CD1   . TRP B 2  272  ? 126.770 136.415 177.358 1.00 41.04  ? 272  TRP B CD1   1 
ATOM   13007 C  CD2   . TRP B 2  272  ? 126.581 138.413 178.330 1.00 41.66  ? 272  TRP B CD2   1 
ATOM   13008 N  NE1   . TRP B 2  272  ? 125.625 136.404 178.109 1.00 42.81  ? 272  TRP B NE1   1 
ATOM   13009 C  CE2   . TRP B 2  272  ? 125.486 137.621 178.718 1.00 43.40  ? 272  TRP B CE2   1 
ATOM   13010 C  CE3   . TRP B 2  272  ? 126.676 139.718 178.821 1.00 40.67  ? 272  TRP B CE3   1 
ATOM   13011 C  CZ2   . TRP B 2  272  ? 124.498 138.086 179.572 1.00 39.98  ? 272  TRP B CZ2   1 
ATOM   13012 C  CZ3   . TRP B 2  272  ? 125.691 140.177 179.667 1.00 41.20  ? 272  TRP B CZ3   1 
ATOM   13013 C  CH2   . TRP B 2  272  ? 124.618 139.366 180.034 1.00 42.22  ? 272  TRP B CH2   1 
ATOM   13014 N  N     . TYR B 2  273  ? 129.425 137.004 179.797 1.00 49.42  ? 273  TYR B N     1 
ATOM   13015 C  CA    . TYR B 2  273  ? 129.392 137.283 181.228 1.00 49.94  ? 273  TYR B CA    1 
ATOM   13016 C  C     . TYR B 2  273  ? 130.792 137.428 181.812 1.00 49.48  ? 273  TYR B C     1 
ATOM   13017 O  O     . TYR B 2  273  ? 131.008 138.243 182.714 1.00 46.29  ? 273  TYR B O     1 
ATOM   13018 C  CB    . TYR B 2  273  ? 128.625 136.175 181.956 1.00 46.02  ? 273  TYR B CB    1 
ATOM   13019 C  CG    . TYR B 2  273  ? 129.345 134.844 181.953 1.00 47.43  ? 273  TYR B CG    1 
ATOM   13020 C  CD1   . TYR B 2  273  ? 129.172 133.945 180.911 1.00 48.81  ? 273  TYR B CD1   1 
ATOM   13021 C  CD2   . TYR B 2  273  ? 130.197 134.486 182.990 1.00 44.93  ? 273  TYR B CD2   1 
ATOM   13022 C  CE1   . TYR B 2  273  ? 129.826 132.731 180.904 1.00 48.03  ? 273  TYR B CE1   1 
ATOM   13023 C  CE2   . TYR B 2  273  ? 130.862 133.279 182.985 1.00 47.47  ? 273  TYR B CE2   1 
ATOM   13024 C  CZ    . TYR B 2  273  ? 130.674 132.406 181.940 1.00 49.39  ? 273  TYR B CZ    1 
ATOM   13025 O  OH    . TYR B 2  273  ? 131.329 131.196 181.930 1.00 48.24  ? 273  TYR B OH    1 
ATOM   13026 N  N     . LEU B 2  274  ? 131.751 136.656 181.296 1.00 45.30  ? 274  LEU B N     1 
ATOM   13027 C  CA    . LEU B 2  274  ? 133.091 136.644 181.869 1.00 43.69  ? 274  LEU B CA    1 
ATOM   13028 C  C     . LEU B 2  274  ? 133.814 137.965 181.621 1.00 45.20  ? 274  LEU B C     1 
ATOM   13029 O  O     . LEU B 2  274  ? 134.606 138.414 182.459 1.00 45.36  ? 274  LEU B O     1 
ATOM   13030 C  CB    . LEU B 2  274  ? 133.875 135.468 181.291 1.00 45.03  ? 274  LEU B CB    1 
ATOM   13031 C  CG    . LEU B 2  274  ? 135.146 135.023 182.009 1.00 47.77  ? 274  LEU B CG    1 
ATOM   13032 C  CD1   . LEU B 2  274  ? 135.157 133.513 182.096 1.00 44.88  ? 274  LEU B CD1   1 
ATOM   13033 C  CD2   . LEU B 2  274  ? 136.393 135.535 181.300 1.00 44.25  ? 274  LEU B CD2   1 
ATOM   13034 N  N     . ILE B 2  275  ? 133.559 138.596 180.471 1.00 45.94  ? 275  ILE B N     1 
ATOM   13035 C  CA    . ILE B 2  275  ? 134.145 139.904 180.183 1.00 45.26  ? 275  ILE B CA    1 
ATOM   13036 C  C     . ILE B 2  275  ? 133.634 140.950 181.165 1.00 44.99  ? 275  ILE B C     1 
ATOM   13037 O  O     . ILE B 2  275  ? 134.399 141.786 181.657 1.00 42.07  ? 275  ILE B O     1 
ATOM   13038 C  CB    . ILE B 2  275  ? 133.862 140.312 178.726 1.00 42.94  ? 275  ILE B CB    1 
ATOM   13039 C  CG1   . ILE B 2  275  ? 134.283 139.199 177.773 1.00 43.83  ? 275  ILE B CG1   1 
ATOM   13040 C  CG2   . ILE B 2  275  ? 134.614 141.582 178.376 1.00 43.19  ? 275  ILE B CG2   1 
ATOM   13041 C  CD1   . ILE B 2  275  ? 135.781 138.991 177.741 1.00 43.75  ? 275  ILE B CD1   1 
ATOM   13042 N  N     . PHE B 2  276  ? 132.332 140.932 181.453 1.00 47.29  ? 276  PHE B N     1 
ATOM   13043 C  CA    . PHE B 2  276  ? 131.791 141.869 182.429 1.00 49.17  ? 276  PHE B CA    1 
ATOM   13044 C  C     . PHE B 2  276  ? 132.346 141.617 183.824 1.00 52.50  ? 276  PHE B C     1 
ATOM   13045 O  O     . PHE B 2  276  ? 132.616 142.573 184.560 1.00 52.83  ? 276  PHE B O     1 
ATOM   13046 C  CB    . PHE B 2  276  ? 130.264 141.806 182.451 1.00 48.38  ? 276  PHE B CB    1 
ATOM   13047 C  CG    . PHE B 2  276  ? 129.600 142.470 181.275 1.00 50.14  ? 276  PHE B CG    1 
ATOM   13048 C  CD1   . PHE B 2  276  ? 130.344 143.074 180.284 1.00 49.08  ? 276  PHE B CD1   1 
ATOM   13049 C  CD2   . PHE B 2  276  ? 128.222 142.521 181.186 1.00 48.73  ? 276  PHE B CD2   1 
ATOM   13050 C  CE1   . PHE B 2  276  ? 129.727 143.690 179.223 1.00 49.39  ? 276  PHE B CE1   1 
ATOM   13051 C  CE2   . PHE B 2  276  ? 127.605 143.138 180.127 1.00 48.45  ? 276  PHE B CE2   1 
ATOM   13052 C  CZ    . PHE B 2  276  ? 128.359 143.724 179.148 1.00 49.16  ? 276  PHE B CZ    1 
ATOM   13053 N  N     . ARG B 2  277  ? 132.514 140.349 184.208 1.00 54.64  ? 277  ARG B N     1 
ATOM   13054 C  CA    . ARG B 2  277  ? 133.053 140.026 185.526 1.00 50.40  ? 277  ARG B CA    1 
ATOM   13055 C  C     . ARG B 2  277  ? 134.513 140.434 185.667 1.00 50.01  ? 277  ARG B C     1 
ATOM   13056 O  O     . ARG B 2  277  ? 134.905 140.947 186.719 1.00 49.80  ? 277  ARG B O     1 
ATOM   13057 C  CB    . ARG B 2  277  ? 132.880 138.531 185.805 1.00 48.20  ? 277  ARG B CB    1 
ATOM   13058 C  CG    . ARG B 2  277  ? 131.454 138.173 186.184 1.00 49.92  ? 277  ARG B CG    1 
ATOM   13059 C  CD    . ARG B 2  277  ? 131.228 136.679 186.312 1.00 50.98  ? 277  ARG B CD    1 
ATOM   13060 N  NE    . ARG B 2  277  ? 129.828 136.396 186.607 1.00 53.12  ? 277  ARG B NE    1 
ATOM   13061 C  CZ    . ARG B 2  277  ? 129.281 135.188 186.596 1.00 51.72  ? 277  ARG B CZ    1 
ATOM   13062 N  NH1   . ARG B 2  277  ? 129.987 134.110 186.297 1.00 51.59  ? 277  ARG B NH1   1 
ATOM   13063 N  NH2   . ARG B 2  277  ? 127.989 135.059 186.884 1.00 47.68  ? 277  ARG B NH2   1 
ATOM   13064 N  N     . MET B 2  278  ? 135.320 140.248 184.617 1.00 48.84  ? 278  MET B N     1 
ATOM   13065 C  CA    . MET B 2  278  ? 136.718 140.659 184.661 1.00 49.76  ? 278  MET B CA    1 
ATOM   13066 C  C     . MET B 2  278  ? 136.884 142.149 184.917 1.00 51.14  ? 278  MET B C     1 
ATOM   13067 O  O     . MET B 2  278  ? 137.973 142.580 185.311 1.00 52.11  ? 278  MET B O     1 
ATOM   13068 C  CB    . MET B 2  278  ? 137.426 140.318 183.350 1.00 50.46  ? 278  MET B CB    1 
ATOM   13069 C  CG    . MET B 2  278  ? 138.046 138.950 183.280 1.00 50.72  ? 278  MET B CG    1 
ATOM   13070 S  SD    . MET B 2  278  ? 139.542 138.998 182.281 1.00 56.56  ? 278  MET B SD    1 
ATOM   13071 C  CE    . MET B 2  278  ? 139.262 137.646 181.142 1.00 51.70  ? 278  MET B CE    1 
ATOM   13072 N  N     . PHE B 2  279  ? 135.852 142.948 184.669 1.00 49.25  ? 279  PHE B N     1 
ATOM   13073 C  CA    . PHE B 2  279  ? 135.972 144.396 184.694 1.00 49.93  ? 279  PHE B CA    1 
ATOM   13074 C  C     . PHE B 2  279  ? 135.302 145.041 185.900 1.00 50.31  ? 279  PHE B C     1 
ATOM   13075 O  O     . PHE B 2  279  ? 134.976 146.231 185.846 1.00 49.77  ? 279  PHE B O     1 
ATOM   13076 C  CB    . PHE B 2  279  ? 135.409 144.990 183.402 1.00 48.11  ? 279  PHE B CB    1 
ATOM   13077 C  CG    . PHE B 2  279  ? 136.278 144.753 182.193 1.00 49.59  ? 279  PHE B CG    1 
ATOM   13078 C  CD1   . PHE B 2  279  ? 137.459 144.033 182.292 1.00 49.03  ? 279  PHE B CD1   1 
ATOM   13079 C  CD2   . PHE B 2  279  ? 135.931 145.285 180.966 1.00 49.82  ? 279  PHE B CD2   1 
ATOM   13080 C  CE1   . PHE B 2  279  ? 138.257 143.825 181.187 1.00 49.65  ? 279  PHE B CE1   1 
ATOM   13081 C  CE2   . PHE B 2  279  ? 136.729 145.083 179.863 1.00 50.81  ? 279  PHE B CE2   1 
ATOM   13082 C  CZ    . PHE B 2  279  ? 137.893 144.351 179.971 1.00 51.34  ? 279  PHE B CZ    1 
ATOM   13083 N  N     . GLY B 2  280  ? 135.087 144.296 186.981 1.00 44.48  ? 280  GLY B N     1 
ATOM   13084 C  CA    . GLY B 2  280  ? 134.621 144.876 188.223 1.00 44.35  ? 280  GLY B CA    1 
ATOM   13085 C  C     . GLY B 2  280  ? 133.122 144.917 188.416 1.00 45.60  ? 280  GLY B C     1 
ATOM   13086 O  O     . GLY B 2  280  ? 132.645 145.722 189.226 1.00 47.64  ? 280  GLY B O     1 
ATOM   13087 N  N     . MET B 2  281  ? 132.363 144.090 187.702 1.00 48.17  ? 281  MET B N     1 
ATOM   13088 C  CA    . MET B 2  281  ? 130.906 144.097 187.767 1.00 46.28  ? 281  MET B CA    1 
ATOM   13089 C  C     . MET B 2  281  ? 130.446 142.647 187.864 1.00 47.17  ? 281  MET B C     1 
ATOM   13090 O  O     . MET B 2  281  ? 130.703 141.851 186.955 1.00 49.92  ? 281  MET B O     1 
ATOM   13091 C  CB    . MET B 2  281  ? 130.332 144.801 186.538 1.00 47.76  ? 281  MET B CB    1 
ATOM   13092 C  CG    . MET B 2  281  ? 128.839 144.734 186.364 1.00 49.61  ? 281  MET B CG    1 
ATOM   13093 S  SD    . MET B 2  281  ? 128.256 146.277 185.637 1.00 58.14  ? 281  MET B SD    1 
ATOM   13094 C  CE    . MET B 2  281  ? 126.614 146.397 186.315 1.00 44.53  ? 281  MET B CE    1 
ATOM   13095 N  N     . THR B 2  282  ? 129.780 142.295 188.966 1.00 45.36  ? 282  THR B N     1 
ATOM   13096 C  CA    . THR B 2  282  ? 129.474 140.897 189.256 1.00 47.36  ? 282  THR B CA    1 
ATOM   13097 C  C     . THR B 2  282  ? 127.989 140.564 189.325 1.00 47.99  ? 282  THR B C     1 
ATOM   13098 O  O     . THR B 2  282  ? 127.583 139.535 188.780 1.00 47.49  ? 282  THR B O     1 
ATOM   13099 C  CB    . THR B 2  282  ? 130.122 140.474 190.581 1.00 47.75  ? 282  THR B CB    1 
ATOM   13100 O  OG1   . THR B 2  282  ? 131.495 140.881 190.599 1.00 49.24  ? 282  THR B OG1   1 
ATOM   13101 C  CG2   . THR B 2  282  ? 130.042 138.967 190.753 1.00 46.37  ? 282  THR B CG2   1 
ATOM   13102 N  N     . GLY B 2  283  ? 127.175 141.389 189.983 1.00 46.15  ? 283  GLY B N     1 
ATOM   13103 C  CA    . GLY B 2  283  ? 125.782 141.052 190.224 1.00 44.11  ? 283  GLY B CA    1 
ATOM   13104 C  C     . GLY B 2  283  ? 124.967 140.777 188.974 1.00 44.88  ? 283  GLY B C     1 
ATOM   13105 O  O     . GLY B 2  283  ? 124.921 141.609 188.064 1.00 42.28  ? 283  GLY B O     1 
ATOM   13106 N  N     . ASP B 2  284  ? 124.297 139.621 188.935 1.00 42.94  ? 284  ASP B N     1 
ATOM   13107 C  CA    . ASP B 2  284  ? 123.577 139.212 187.732 1.00 43.53  ? 284  ASP B CA    1 
ATOM   13108 C  C     . ASP B 2  284  ? 122.470 140.195 187.368 1.00 46.82  ? 284  ASP B C     1 
ATOM   13109 O  O     . ASP B 2  284  ? 122.279 140.504 186.185 1.00 47.47  ? 284  ASP B O     1 
ATOM   13110 C  CB    . ASP B 2  284  ? 123.009 137.806 187.911 1.00 43.36  ? 284  ASP B CB    1 
ATOM   13111 C  CG    . ASP B 2  284  ? 124.017 136.727 187.582 1.00 46.89  ? 284  ASP B CG    1 
ATOM   13112 O  OD1   . ASP B 2  284  ? 124.999 137.027 186.873 1.00 45.72  ? 284  ASP B OD1   1 
ATOM   13113 O  OD2   . ASP B 2  284  ? 123.832 135.577 188.031 1.00 49.00  ? 284  ASP B OD2   1 
ATOM   13114 N  N     . ASP B 2  285  ? 121.725 140.691 188.358 1.00 44.51  ? 285  ASP B N     1 
ATOM   13115 C  CA    . ASP B 2  285  ? 120.745 141.732 188.069 1.00 43.01  ? 285  ASP B CA    1 
ATOM   13116 C  C     . ASP B 2  285  ? 121.421 142.951 187.461 1.00 45.95  ? 285  ASP B C     1 
ATOM   13117 O  O     . ASP B 2  285  ? 120.951 143.505 186.459 1.00 47.57  ? 285  ASP B O     1 
ATOM   13118 C  CB    . ASP B 2  285  ? 119.997 142.128 189.341 1.00 44.72  ? 285  ASP B CB    1 
ATOM   13119 C  CG    . ASP B 2  285  ? 120.925 142.335 190.528 1.00 46.57  ? 285  ASP B CG    1 
ATOM   13120 O  OD1   . ASP B 2  285  ? 122.088 141.881 190.471 1.00 43.12  ? 285  ASP B OD1   1 
ATOM   13121 O  OD2   . ASP B 2  285  ? 120.493 142.969 191.514 1.00 45.43  ? 285  ASP B OD2   1 
ATOM   13122 N  N     . SER B 2  286  ? 122.542 143.368 188.048 1.00 45.07  ? 286  SER B N     1 
ATOM   13123 C  CA    . SER B 2  286  ? 123.279 144.506 187.522 1.00 44.26  ? 286  SER B CA    1 
ATOM   13124 C  C     . SER B 2  286  ? 123.839 144.205 186.138 1.00 45.57  ? 286  SER B C     1 
ATOM   13125 O  O     . SER B 2  286  ? 123.848 145.078 185.263 1.00 48.10  ? 286  SER B O     1 
ATOM   13126 C  CB    . SER B 2  286  ? 124.390 144.889 188.495 1.00 42.47  ? 286  SER B CB    1 
ATOM   13127 O  OG    . SER B 2  286  ? 123.854 145.312 189.733 1.00 43.39  ? 286  SER B OG    1 
ATOM   13128 N  N     . ILE B 2  287  ? 124.300 142.972 185.920 1.00 42.05  ? 287  ILE B N     1 
ATOM   13129 C  CA    . ILE B 2  287  ? 124.825 142.590 184.612 1.00 41.18  ? 287  ILE B CA    1 
ATOM   13130 C  C     . ILE B 2  287  ? 123.739 142.708 183.551 1.00 42.37  ? 287  ILE B C     1 
ATOM   13131 O  O     . ILE B 2  287  ? 123.976 143.227 182.456 1.00 46.41  ? 287  ILE B O     1 
ATOM   13132 C  CB    . ILE B 2  287  ? 125.408 141.167 184.665 1.00 42.01  ? 287  ILE B CB    1 
ATOM   13133 C  CG1   . ILE B 2  287  ? 126.649 141.134 185.550 1.00 44.17  ? 287  ILE B CG1   1 
ATOM   13134 C  CG2   . ILE B 2  287  ? 125.763 140.682 183.275 1.00 43.35  ? 287  ILE B CG2   1 
ATOM   13135 C  CD1   . ILE B 2  287  ? 127.858 141.724 184.913 1.00 45.98  ? 287  ILE B CD1   1 
ATOM   13136 N  N     . ILE B 2  288  ? 122.531 142.231 183.856 1.00 40.99  ? 288  ILE B N     1 
ATOM   13137 C  CA    . ILE B 2  288  ? 121.427 142.382 182.918 1.00 41.14  ? 288  ILE B CA    1 
ATOM   13138 C  C     . ILE B 2  288  ? 121.057 143.846 182.724 1.00 43.07  ? 288  ILE B C     1 
ATOM   13139 O  O     . ILE B 2  288  ? 120.721 144.252 181.607 1.00 46.44  ? 288  ILE B O     1 
ATOM   13140 C  CB    . ILE B 2  288  ? 120.220 141.542 183.375 1.00 42.13  ? 288  ILE B CB    1 
ATOM   13141 C  CG1   . ILE B 2  288  ? 120.230 140.171 182.690 1.00 42.76  ? 288  ILE B CG1   1 
ATOM   13142 C  CG2   . ILE B 2  288  ? 118.916 142.265 183.100 1.00 38.65  ? 288  ILE B CG2   1 
ATOM   13143 C  CD1   . ILE B 2  288  ? 121.457 139.327 182.977 1.00 40.39  ? 288  ILE B CD1   1 
ATOM   13144 N  N     . GLU B 2  289  ? 121.141 144.669 183.770 1.00 47.66  ? 289  GLU B N     1 
ATOM   13145 C  CA    . GLU B 2  289  ? 120.892 146.093 183.585 1.00 48.96  ? 289  GLU B CA    1 
ATOM   13146 C  C     . GLU B 2  289  ? 121.896 146.763 182.660 1.00 48.22  ? 289  GLU B C     1 
ATOM   13147 O  O     . GLU B 2  289  ? 121.643 147.887 182.214 1.00 49.55  ? 289  GLU B O     1 
ATOM   13148 C  CB    . GLU B 2  289  ? 120.879 146.829 184.923 1.00 48.41  ? 289  GLU B CB    1 
ATOM   13149 C  CG    . GLU B 2  289  ? 119.553 146.766 185.629 1.00 48.00  ? 289  GLU B CG    1 
ATOM   13150 C  CD    . GLU B 2  289  ? 118.777 148.069 185.509 1.00 51.54  ? 289  GLU B CD    1 
ATOM   13151 O  OE1   . GLU B 2  289  ? 117.557 148.068 185.770 1.00 47.87  ? 289  GLU B OE1   1 
ATOM   13152 O  OE2   . GLU B 2  289  ? 119.387 149.094 185.137 1.00 52.34  ? 289  GLU B OE2   1 
ATOM   13153 N  N     . GLN B 2  290  ? 123.027 146.125 182.374 1.00 41.51  ? 290  GLN B N     1 
ATOM   13154 C  CA    . GLN B 2  290  ? 123.890 146.611 181.309 1.00 45.19  ? 290  GLN B CA    1 
ATOM   13155 C  C     . GLN B 2  290  ? 123.280 146.415 179.930 1.00 45.64  ? 290  GLN B C     1 
ATOM   13156 O  O     . GLN B 2  290  ? 123.527 147.234 179.040 1.00 42.92  ? 290  GLN B O     1 
ATOM   13157 C  CB    . GLN B 2  290  ? 125.253 145.919 181.367 1.00 44.63  ? 290  GLN B CB    1 
ATOM   13158 C  CG    . GLN B 2  290  ? 126.020 146.196 182.631 1.00 43.17  ? 290  GLN B CG    1 
ATOM   13159 C  CD    . GLN B 2  290  ? 126.492 147.633 182.718 1.00 46.02  ? 290  GLN B CD    1 
ATOM   13160 O  OE1   . GLN B 2  290  ? 125.973 148.421 183.507 1.00 43.77  ? 290  GLN B OE1   1 
ATOM   13161 N  NE2   . GLN B 2  290  ? 127.481 147.982 181.904 1.00 46.32  ? 290  GLN B NE2   1 
ATOM   13162 N  N     . VAL B 2  291  ? 122.477 145.369 179.736 1.00 40.75  ? 291  VAL B N     1 
ATOM   13163 C  CA    . VAL B 2  291  ? 121.939 145.010 178.431 1.00 40.05  ? 291  VAL B CA    1 
ATOM   13164 C  C     . VAL B 2  291  ? 120.506 145.499 178.260 1.00 40.90  ? 291  VAL B C     1 
ATOM   13165 O  O     . VAL B 2  291  ? 120.155 146.076 177.229 1.00 44.73  ? 291  VAL B O     1 
ATOM   13166 C  CB    . VAL B 2  291  ? 122.029 143.491 178.187 1.00 41.10  ? 291  VAL B CB    1 
ATOM   13167 C  CG1   . VAL B 2  291  ? 121.307 143.120 176.909 1.00 39.90  ? 291  VAL B CG1   1 
ATOM   13168 C  CG2   . VAL B 2  291  ? 123.478 143.065 178.129 1.00 42.52  ? 291  VAL B CG2   1 
ATOM   13169 N  N     . VAL B 2  292  ? 119.661 145.278 179.265 1.00 38.99  ? 292  VAL B N     1 
ATOM   13170 C  CA    . VAL B 2  292  ? 118.251 145.631 179.148 1.00 40.57  ? 292  VAL B CA    1 
ATOM   13171 C  C     . VAL B 2  292  ? 117.972 147.056 179.611 1.00 43.08  ? 292  VAL B C     1 
ATOM   13172 O  O     . VAL B 2  292  ? 116.929 147.623 179.253 1.00 43.64  ? 292  VAL B O     1 
ATOM   13173 C  CB    . VAL B 2  292  ? 117.424 144.582 179.921 1.00 40.81  ? 292  VAL B CB    1 
ATOM   13174 C  CG1   . VAL B 2  292  ? 115.952 144.939 179.961 1.00 39.82  ? 292  VAL B CG1   1 
ATOM   13175 C  CG2   . VAL B 2  292  ? 117.626 143.208 179.302 1.00 39.48  ? 292  VAL B CG2   1 
ATOM   13176 N  N     . PHE B 2  293  ? 118.887 147.662 180.368 1.00 44.46  ? 293  PHE B N     1 
ATOM   13177 C  CA    . PHE B 2  293  ? 118.754 149.010 180.916 1.00 43.73  ? 293  PHE B CA    1 
ATOM   13178 C  C     . PHE B 2  293  ? 117.591 149.113 181.896 1.00 46.39  ? 293  PHE B C     1 
ATOM   13179 O  O     . PHE B 2  293  ? 117.287 150.206 182.381 1.00 46.16  ? 293  PHE B O     1 
ATOM   13180 C  CB    . PHE B 2  293  ? 118.572 150.066 179.818 1.00 45.54  ? 293  PHE B CB    1 
ATOM   13181 C  CG    . PHE B 2  293  ? 119.253 149.744 178.519 1.00 47.39  ? 293  PHE B CG    1 
ATOM   13182 C  CD1   . PHE B 2  293  ? 120.628 149.600 178.451 1.00 43.71  ? 293  PHE B CD1   1 
ATOM   13183 C  CD2   . PHE B 2  293  ? 118.511 149.610 177.355 1.00 44.13  ? 293  PHE B CD2   1 
ATOM   13184 C  CE1   . PHE B 2  293  ? 121.243 149.313 177.256 1.00 45.54  ? 293  PHE B CE1   1 
ATOM   13185 C  CE2   . PHE B 2  293  ? 119.124 149.321 176.159 1.00 43.68  ? 293  PHE B CE2   1 
ATOM   13186 C  CZ    . PHE B 2  293  ? 120.492 149.172 176.109 1.00 46.56  ? 293  PHE B CZ    1 
ATOM   13187 N  N     . ASP B 2  294  ? 116.937 147.993 182.197 1.00 49.79  ? 294  ASP B N     1 
ATOM   13188 C  CA    . ASP B 2  294  ? 115.793 148.014 183.098 1.00 47.62  ? 294  ASP B CA    1 
ATOM   13189 C  C     . ASP B 2  294  ? 115.550 146.621 183.659 1.00 48.94  ? 294  ASP B C     1 
ATOM   13190 O  O     . ASP B 2  294  ? 116.034 145.625 183.117 1.00 50.62  ? 294  ASP B O     1 
ATOM   13191 C  CB    . ASP B 2  294  ? 114.533 148.521 182.394 1.00 44.96  ? 294  ASP B CB    1 
ATOM   13192 C  CG    . ASP B 2  294  ? 113.523 149.093 183.361 1.00 47.72  ? 294  ASP B CG    1 
ATOM   13193 O  OD1   . ASP B 2  294  ? 113.815 149.105 184.573 1.00 48.67  ? 294  ASP B OD1   1 
ATOM   13194 O  OD2   . ASP B 2  294  ? 112.446 149.538 182.917 1.00 49.51  ? 294  ASP B OD2   1 
ATOM   13195 N  N     . LEU B 2  295  ? 114.803 146.573 184.763 1.00 45.89  ? 295  LEU B N     1 
ATOM   13196 C  CA    . LEU B 2  295  ? 114.299 145.329 185.330 1.00 44.33  ? 295  LEU B CA    1 
ATOM   13197 C  C     . LEU B 2  295  ? 112.832 145.433 185.722 1.00 45.81  ? 295  LEU B C     1 
ATOM   13198 O  O     . LEU B 2  295  ? 112.270 144.464 186.244 1.00 45.43  ? 295  LEU B O     1 
ATOM   13199 C  CB    . LEU B 2  295  ? 115.120 144.912 186.553 1.00 45.89  ? 295  LEU B CB    1 
ATOM   13200 C  CG    . LEU B 2  295  ? 116.643 144.993 186.520 1.00 44.93  ? 295  LEU B CG    1 
ATOM   13201 C  CD1   . LEU B 2  295  ? 117.171 145.300 187.910 1.00 44.67  ? 295  LEU B CD1   1 
ATOM   13202 C  CD2   . LEU B 2  295  ? 117.237 143.701 185.997 1.00 43.43  ? 295  LEU B CD2   1 
ATOM   13203 N  N     . GLU B 2  296  ? 112.202 146.584 185.497 1.00 49.48  ? 296  GLU B N     1 
ATOM   13204 C  CA    . GLU B 2  296  ? 110.842 146.835 185.956 1.00 50.94  ? 296  GLU B CA    1 
ATOM   13205 C  C     . GLU B 2  296  ? 109.874 147.136 184.822 1.00 50.59  ? 296  GLU B C     1 
ATOM   13206 O  O     . GLU B 2  296  ? 108.785 147.663 185.079 1.00 50.13  ? 296  GLU B O     1 
ATOM   13207 C  CB    . GLU B 2  296  ? 110.831 147.981 186.969 1.00 48.83  ? 296  GLU B CB    1 
ATOM   13208 C  CG    . GLU B 2  296  ? 111.277 147.558 188.349 1.00 47.58  ? 296  GLU B CG    1 
ATOM   13209 C  CD    . GLU B 2  296  ? 112.780 147.450 188.464 1.00 50.08  ? 296  GLU B CD    1 
ATOM   13210 O  OE1   . GLU B 2  296  ? 113.485 147.905 187.536 1.00 50.15  ? 296  GLU B OE1   1 
ATOM   13211 O  OE2   . GLU B 2  296  ? 113.254 146.898 189.479 1.00 49.03  ? 296  GLU B OE2   1 
ATOM   13212 N  N     . SER B 2  297  ? 110.239 146.837 183.582 1.00 47.20  ? 297  SER B N     1 
ATOM   13213 C  CA    . SER B 2  297  ? 109.326 146.935 182.451 1.00 47.68  ? 297  SER B CA    1 
ATOM   13214 C  C     . SER B 2  297  ? 109.018 145.527 181.966 1.00 48.66  ? 297  SER B C     1 
ATOM   13215 O  O     . SER B 2  297  ? 109.936 144.763 181.651 1.00 50.20  ? 297  SER B O     1 
ATOM   13216 C  CB    . SER B 2  297  ? 109.923 147.780 181.327 1.00 45.70  ? 297  SER B CB    1 
ATOM   13217 O  OG    . SER B 2  297  ? 110.095 149.123 181.748 1.00 46.50  ? 297  SER B OG    1 
ATOM   13218 N  N     . ASN B 2  298  ? 107.734 145.186 181.912 1.00 48.87  ? 298  ASN B N     1 
ATOM   13219 C  CA    . ASN B 2  298  ? 107.284 143.854 181.523 1.00 48.26  ? 298  ASN B CA    1 
ATOM   13220 C  C     . ASN B 2  298  ? 106.670 143.856 180.129 1.00 50.28  ? 298  ASN B C     1 
ATOM   13221 O  O     . ASN B 2  298  ? 105.714 143.130 179.855 1.00 49.89  ? 298  ASN B O     1 
ATOM   13222 C  CB    . ASN B 2  298  ? 106.288 143.298 182.535 1.00 47.12  ? 298  ASN B CB    1 
ATOM   13223 C  CG    . ASN B 2  298  ? 106.840 143.275 183.938 1.00 50.44  ? 298  ASN B CG    1 
ATOM   13224 O  OD1   . ASN B 2  298  ? 106.406 144.039 184.800 1.00 50.75  ? 298  ASN B OD1   1 
ATOM   13225 N  ND2   . ASN B 2  298  ? 107.803 142.394 184.179 1.00 50.80  ? 298  ASN B ND2   1 
ATOM   13226 N  N     . SER B 2  299  ? 107.210 144.678 179.237 1.00 49.38  ? 299  SER B N     1 
ATOM   13227 C  CA    . SER B 2  299  ? 106.809 144.654 177.842 1.00 49.46  ? 299  SER B CA    1 
ATOM   13228 C  C     . SER B 2  299  ? 107.420 143.438 177.154 1.00 50.10  ? 299  SER B C     1 
ATOM   13229 O  O     . SER B 2  299  ? 108.455 142.916 177.573 1.00 50.01  ? 299  SER B O     1 
ATOM   13230 C  CB    . SER B 2  299  ? 107.225 145.945 177.150 1.00 48.88  ? 299  SER B CB    1 
ATOM   13231 O  OG    . SER B 2  299  ? 106.739 145.977 175.824 1.00 50.99  ? 299  SER B OG    1 
ATOM   13232 N  N     . LEU B 2  300  ? 106.790 143.003 176.059 1.00 42.30  ? 300  LEU B N     1 
ATOM   13233 C  CA    . LEU B 2  300  ? 107.162 141.739 175.426 1.00 43.90  ? 300  LEU B CA    1 
ATOM   13234 C  C     . LEU B 2  300  ? 108.646 141.689 175.086 1.00 46.82  ? 300  LEU B C     1 
ATOM   13235 O  O     . LEU B 2  300  ? 109.317 140.679 175.339 1.00 44.27  ? 300  LEU B O     1 
ATOM   13236 C  CB    . LEU B 2  300  ? 106.324 141.525 174.166 1.00 43.29  ? 300  LEU B CB    1 
ATOM   13237 C  CG    . LEU B 2  300  ? 106.745 140.353 173.276 1.00 45.61  ? 300  LEU B CG    1 
ATOM   13238 C  CD1   . LEU B 2  300  ? 106.316 139.024 173.891 1.00 43.12  ? 300  LEU B CD1   1 
ATOM   13239 C  CD2   . LEU B 2  300  ? 106.200 140.509 171.859 1.00 42.62  ? 300  LEU B CD2   1 
ATOM   13240 N  N     . VAL B 2  301  ? 109.178 142.775 174.523 1.00 44.40  ? 301  VAL B N     1 
ATOM   13241 C  CA    . VAL B 2  301  ? 110.584 142.802 174.133 1.00 44.99  ? 301  VAL B CA    1 
ATOM   13242 C  C     . VAL B 2  301  ? 111.473 142.606 175.353 1.00 43.88  ? 301  VAL B C     1 
ATOM   13243 O  O     . VAL B 2  301  ? 112.445 141.845 175.316 1.00 43.76  ? 301  VAL B O     1 
ATOM   13244 C  CB    . VAL B 2  301  ? 110.912 144.109 173.389 1.00 44.29  ? 301  VAL B CB    1 
ATOM   13245 C  CG1   . VAL B 2  301  ? 112.364 144.497 173.592 1.00 43.22  ? 301  VAL B CG1   1 
ATOM   13246 C  CG2   . VAL B 2  301  ? 110.607 143.966 171.909 1.00 38.61  ? 301  VAL B CG2   1 
ATOM   13247 N  N     . ASN B 2  302  ? 111.143 143.275 176.458 1.00 44.44  ? 302  ASN B N     1 
ATOM   13248 C  CA    . ASN B 2  302  ? 111.969 143.159 177.657 1.00 47.59  ? 302  ASN B CA    1 
ATOM   13249 C  C     . ASN B 2  302  ? 111.967 141.738 178.206 1.00 48.55  ? 302  ASN B C     1 
ATOM   13250 O  O     . ASN B 2  302  ? 113.034 141.175 178.469 1.00 46.39  ? 302  ASN B O     1 
ATOM   13251 C  CB    . ASN B 2  302  ? 111.492 144.140 178.722 1.00 46.19  ? 302  ASN B CB    1 
ATOM   13252 C  CG    . ASN B 2  302  ? 111.775 145.574 178.352 1.00 48.45  ? 302  ASN B CG    1 
ATOM   13253 O  OD1   . ASN B 2  302  ? 112.907 145.928 178.027 1.00 49.38  ? 302  ASN B OD1   1 
ATOM   13254 N  ND2   . ASN B 2  302  ? 110.744 146.410 178.384 1.00 47.29  ? 302  ASN B ND2   1 
ATOM   13255 N  N     . THR B 2  303  ? 110.786 141.141 178.385 1.00 44.19  ? 303  THR B N     1 
ATOM   13256 C  CA    . THR B 2  303  ? 110.722 139.796 178.948 1.00 45.19  ? 303  THR B CA    1 
ATOM   13257 C  C     . THR B 2  303  ? 111.421 138.794 178.041 1.00 48.34  ? 303  THR B C     1 
ATOM   13258 O  O     . THR B 2  303  ? 112.135 137.902 178.513 1.00 45.18  ? 303  THR B O     1 
ATOM   13259 C  CB    . THR B 2  303  ? 109.269 139.382 179.180 1.00 46.12  ? 303  THR B CB    1 
ATOM   13260 O  OG1   . THR B 2  303  ? 108.752 138.768 177.993 1.00 48.66  ? 303  THR B OG1   1 
ATOM   13261 C  CG2   . THR B 2  303  ? 108.414 140.576 179.550 1.00 43.86  ? 303  THR B CG2   1 
ATOM   13262 N  N     . PHE B 2  304  ? 111.224 138.930 176.729 1.00 47.81  ? 304  PHE B N     1 
ATOM   13263 C  CA    . PHE B 2  304  ? 111.893 138.062 175.768 1.00 47.84  ? 304  PHE B CA    1 
ATOM   13264 C  C     . PHE B 2  304  ? 113.410 138.221 175.852 1.00 49.81  ? 304  PHE B C     1 
ATOM   13265 O  O     . PHE B 2  304  ? 114.146 137.226 175.847 1.00 49.79  ? 304  PHE B O     1 
ATOM   13266 C  CB    . PHE B 2  304  ? 111.354 138.400 174.374 1.00 44.87  ? 304  PHE B CB    1 
ATOM   13267 C  CG    . PHE B 2  304  ? 111.626 137.366 173.314 1.00 47.06  ? 304  PHE B CG    1 
ATOM   13268 C  CD1   . PHE B 2  304  ? 112.540 136.346 173.506 1.00 47.58  ? 304  PHE B CD1   1 
ATOM   13269 C  CD2   . PHE B 2  304  ? 110.946 137.427 172.108 1.00 49.29  ? 304  PHE B CD2   1 
ATOM   13270 C  CE1   . PHE B 2  304  ? 112.773 135.413 172.516 1.00 48.87  ? 304  PHE B CE1   1 
ATOM   13271 C  CE2   . PHE B 2  304  ? 111.173 136.499 171.116 1.00 48.77  ? 304  PHE B CE2   1 
ATOM   13272 C  CZ    . PHE B 2  304  ? 112.088 135.490 171.318 1.00 48.22  ? 304  PHE B CZ    1 
ATOM   13273 N  N     . MET B 2  305  ? 113.889 139.459 175.974 1.00 48.54  ? 305  MET B N     1 
ATOM   13274 C  CA    . MET B 2  305  ? 115.319 139.708 176.095 1.00 49.16  ? 305  MET B CA    1 
ATOM   13275 C  C     . MET B 2  305  ? 115.879 139.072 177.361 1.00 50.58  ? 305  MET B C     1 
ATOM   13276 O  O     . MET B 2  305  ? 116.930 138.420 177.328 1.00 51.25  ? 305  MET B O     1 
ATOM   13277 C  CB    . MET B 2  305  ? 115.561 141.218 176.089 1.00 49.61  ? 305  MET B CB    1 
ATOM   13278 C  CG    . MET B 2  305  ? 116.963 141.664 175.726 1.00 48.98  ? 305  MET B CG    1 
ATOM   13279 S  SD    . MET B 2  305  ? 117.015 142.340 174.056 1.00 60.80  ? 305  MET B SD    1 
ATOM   13280 C  CE    . MET B 2  305  ? 115.930 143.754 174.209 1.00 49.24  ? 305  MET B CE    1 
ATOM   13281 N  N     . ILE B 2  306  ? 115.187 139.255 178.491 1.00 45.18  ? 306  ILE B N     1 
ATOM   13282 C  CA    . ILE B 2  306  ? 115.651 138.682 179.753 1.00 47.81  ? 306  ILE B CA    1 
ATOM   13283 C  C     . ILE B 2  306  ? 115.671 137.166 179.677 1.00 49.62  ? 306  ILE B C     1 
ATOM   13284 O  O     . ILE B 2  306  ? 116.602 136.528 180.182 1.00 48.19  ? 306  ILE B O     1 
ATOM   13285 C  CB    . ILE B 2  306  ? 114.805 139.179 180.948 1.00 47.91  ? 306  ILE B CB    1 
ATOM   13286 C  CG1   . ILE B 2  306  ? 115.097 140.651 181.257 1.00 46.30  ? 306  ILE B CG1   1 
ATOM   13287 C  CG2   . ILE B 2  306  ? 115.058 138.341 182.187 1.00 44.91  ? 306  ILE B CG2   1 
ATOM   13288 C  CD1   . ILE B 2  306  ? 113.874 141.541 181.308 1.00 44.86  ? 306  ILE B CD1   1 
ATOM   13289 N  N     . GLU B 2  307  ? 114.662 136.564 179.046 1.00 46.47  ? 307  GLU B N     1 
ATOM   13290 C  CA    . GLU B 2  307  ? 114.671 135.117 178.852 1.00 47.10  ? 307  GLU B CA    1 
ATOM   13291 C  C     . GLU B 2  307  ? 115.888 134.682 178.048 1.00 46.15  ? 307  GLU B C     1 
ATOM   13292 O  O     . GLU B 2  307  ? 116.559 133.699 178.391 1.00 45.05  ? 307  GLU B O     1 
ATOM   13293 C  CB    . GLU B 2  307  ? 113.393 134.676 178.146 1.00 45.50  ? 307  GLU B CB    1 
ATOM   13294 C  CG    . GLU B 2  307  ? 113.046 133.217 178.362 1.00 45.10  ? 307  GLU B CG    1 
ATOM   13295 C  CD    . GLU B 2  307  ? 112.470 132.570 177.118 1.00 47.03  ? 307  GLU B CD    1 
ATOM   13296 O  OE1   . GLU B 2  307  ? 113.142 131.685 176.549 1.00 47.87  ? 307  GLU B OE1   1 
ATOM   13297 O  OE2   . GLU B 2  307  ? 111.354 132.948 176.704 1.00 45.84  ? 307  GLU B OE2   1 
ATOM   13298 N  N     . ILE B 2  308  ? 116.184 135.407 176.966 1.00 42.81  ? 308  ILE B N     1 
ATOM   13299 C  CA    . ILE B 2  308  ? 117.331 135.060 176.131 1.00 44.62  ? 308  ILE B CA    1 
ATOM   13300 C  C     . ILE B 2  308  ? 118.616 135.127 176.942 1.00 44.42  ? 308  ILE B C     1 
ATOM   13301 O  O     . ILE B 2  308  ? 119.452 134.218 176.887 1.00 43.30  ? 308  ILE B O     1 
ATOM   13302 C  CB    . ILE B 2  308  ? 117.397 135.978 174.895 1.00 42.98  ? 308  ILE B CB    1 
ATOM   13303 C  CG1   . ILE B 2  308  ? 116.228 135.700 173.955 1.00 44.31  ? 308  ILE B CG1   1 
ATOM   13304 C  CG2   . ILE B 2  308  ? 118.711 135.791 174.157 1.00 42.35  ? 308  ILE B CG2   1 
ATOM   13305 C  CD1   . ILE B 2  308  ? 116.097 136.707 172.844 1.00 44.46  ? 308  ILE B CD1   1 
ATOM   13306 N  N     . LEU B 2  309  ? 118.782 136.192 177.726 1.00 40.93  ? 309  LEU B N     1 
ATOM   13307 C  CA    . LEU B 2  309  ? 120.016 136.358 178.488 1.00 42.89  ? 309  LEU B CA    1 
ATOM   13308 C  C     . LEU B 2  309  ? 120.138 135.305 179.586 1.00 43.87  ? 309  LEU B C     1 
ATOM   13309 O  O     . LEU B 2  309  ? 121.234 134.786 179.842 1.00 43.57  ? 309  LEU B O     1 
ATOM   13310 C  CB    . LEU B 2  309  ? 120.086 137.769 179.073 1.00 43.38  ? 309  LEU B CB    1 
ATOM   13311 C  CG    . LEU B 2  309  ? 120.299 138.892 178.047 1.00 45.51  ? 309  LEU B CG    1 
ATOM   13312 C  CD1   . LEU B 2  309  ? 119.341 140.045 178.282 1.00 42.90  ? 309  LEU B CD1   1 
ATOM   13313 C  CD2   . LEU B 2  309  ? 121.730 139.389 178.027 1.00 43.52  ? 309  LEU B CD2   1 
ATOM   13314 N  N     . GLU B 2  310  ? 119.022 134.979 180.247 1.00 49.57  ? 310  GLU B N     1 
ATOM   13315 C  CA    . GLU B 2  310  ? 119.041 133.974 181.305 1.00 47.92  ? 310  GLU B CA    1 
ATOM   13316 C  C     . GLU B 2  310  ? 119.387 132.599 180.757 1.00 47.05  ? 310  GLU B C     1 
ATOM   13317 O  O     . GLU B 2  310  ? 120.151 131.851 181.376 1.00 46.52  ? 310  GLU B O     1 
ATOM   13318 C  CB    . GLU B 2  310  ? 117.692 133.947 182.019 1.00 45.61  ? 310  GLU B CB    1 
ATOM   13319 C  CG    . GLU B 2  310  ? 117.566 134.991 183.113 1.00 48.18  ? 310  GLU B CG    1 
ATOM   13320 C  CD    . GLU B 2  310  ? 116.152 135.117 183.643 1.00 50.12  ? 310  GLU B CD    1 
ATOM   13321 O  OE1   . GLU B 2  310  ? 115.238 134.492 183.066 1.00 49.31  ? 310  GLU B OE1   1 
ATOM   13322 O  OE2   . GLU B 2  310  ? 115.957 135.844 184.638 1.00 48.23  ? 310  GLU B OE2   1 
ATOM   13323 N  N     . LYS B 2  311  ? 118.839 132.246 179.594 1.00 43.78  ? 311  LYS B N     1 
ATOM   13324 C  CA    . LYS B 2  311  ? 119.261 131.006 178.954 1.00 45.64  ? 311  LYS B CA    1 
ATOM   13325 C  C     . LYS B 2  311  ? 120.717 131.080 178.512 1.00 47.98  ? 311  LYS B C     1 
ATOM   13326 O  O     . LYS B 2  311  ? 121.421 130.064 178.512 1.00 50.45  ? 311  LYS B O     1 
ATOM   13327 C  CB    . LYS B 2  311  ? 118.337 130.689 177.777 1.00 45.78  ? 311  LYS B CB    1 
ATOM   13328 C  CG    . LYS B 2  311  ? 118.937 129.807 176.699 1.00 45.45  ? 311  LYS B CG    1 
ATOM   13329 C  CD    . LYS B 2  311  ? 118.905 128.353 177.086 1.00 45.44  ? 311  LYS B CD    1 
ATOM   13330 C  CE    . LYS B 2  311  ? 120.170 127.657 176.642 1.00 46.06  ? 311  LYS B CE    1 
ATOM   13331 N  NZ    . LYS B 2  311  ? 121.291 127.879 177.593 1.00 47.21  ? 311  LYS B NZ    1 
ATOM   13332 N  N     . SER B 2  312  ? 121.192 132.272 178.150 1.00 44.74  ? 312  SER B N     1 
ATOM   13333 C  CA    . SER B 2  312  ? 122.567 132.412 177.684 1.00 47.52  ? 312  SER B CA    1 
ATOM   13334 C  C     . SER B 2  312  ? 123.572 132.174 178.803 1.00 47.37  ? 312  SER B C     1 
ATOM   13335 O  O     . SER B 2  312  ? 124.633 131.579 178.579 1.00 46.56  ? 312  SER B O     1 
ATOM   13336 C  CB    . SER B 2  312  ? 122.768 133.799 177.076 1.00 48.70  ? 312  SER B CB    1 
ATOM   13337 O  OG    . SER B 2  312  ? 122.738 134.798 178.076 1.00 49.96  ? 312  SER B OG    1 
ATOM   13338 N  N     . ILE B 2  313  ? 123.264 132.634 180.012 1.00 44.54  ? 313  ILE B N     1 
ATOM   13339 C  CA    . ILE B 2  313  ? 124.275 132.630 181.068 1.00 48.82  ? 313  ILE B CA    1 
ATOM   13340 C  C     . ILE B 2  313  ? 124.393 131.253 181.714 1.00 51.90  ? 313  ILE B C     1 
ATOM   13341 O  O     . ILE B 2  313  ? 125.095 131.088 182.717 1.00 49.89  ? 313  ILE B O     1 
ATOM   13342 C  CB    . ILE B 2  313  ? 123.992 133.708 182.133 1.00 49.32  ? 313  ILE B CB    1 
ATOM   13343 C  CG1   . ILE B 2  313  ? 122.520 133.714 182.533 1.00 48.97  ? 313  ILE B CG1   1 
ATOM   13344 C  CG2   . ILE B 2  313  ? 124.425 135.076 181.641 1.00 50.64  ? 313  ILE B CG2   1 
ATOM   13345 C  CD1   . ILE B 2  313  ? 122.247 134.520 183.780 1.00 50.16  ? 313  ILE B CD1   1 
ATOM   13346 N  N     . HIS B 2  314  ? 123.724 130.252 181.139 1.00 54.34  ? 314  HIS B N     1 
ATOM   13347 C  CA    . HIS B 2  314  ? 123.777 128.898 181.677 1.00 52.74  ? 314  HIS B CA    1 
ATOM   13348 C  C     . HIS B 2  314  ? 124.208 127.886 180.624 1.00 53.91  ? 314  HIS B C     1 
ATOM   13349 O  O     . HIS B 2  314  ? 123.524 126.882 180.405 1.00 54.03  ? 314  HIS B O     1 
ATOM   13350 C  CB    . HIS B 2  314  ? 122.422 128.494 182.257 1.00 51.52  ? 314  HIS B CB    1 
ATOM   13351 C  CG    . HIS B 2  314  ? 122.041 129.263 183.480 1.00 53.83  ? 314  HIS B CG    1 
ATOM   13352 N  ND1   . HIS B 2  314  ? 122.762 129.196 184.652 1.00 54.34  ? 314  HIS B ND1   1 
ATOM   13353 C  CD2   . HIS B 2  314  ? 121.008 130.104 183.720 1.00 53.86  ? 314  HIS B CD2   1 
ATOM   13354 C  CE1   . HIS B 2  314  ? 122.200 129.977 185.557 1.00 54.90  ? 314  HIS B CE1   1 
ATOM   13355 N  NE2   . HIS B 2  314  ? 121.132 130.538 185.018 1.00 55.49  ? 314  HIS B NE2   1 
ATOM   13356 N  N     . VAL B 2  315  ? 125.322 128.149 179.955 1.00 48.27  ? 315  VAL B N     1 
ATOM   13357 C  CA    . VAL B 2  315  ? 125.881 127.232 178.971 1.00 49.47  ? 315  VAL B CA    1 
ATOM   13358 C  C     . VAL B 2  315  ? 127.258 126.794 179.452 1.00 49.60  ? 315  VAL B C     1 
ATOM   13359 O  O     . VAL B 2  315  ? 127.919 127.496 180.226 1.00 48.83  ? 315  VAL B O     1 
ATOM   13360 C  CB    . VAL B 2  315  ? 125.963 127.879 177.571 1.00 49.12  ? 315  VAL B CB    1 
ATOM   13361 C  CG1   . VAL B 2  315  ? 127.096 128.881 177.525 1.00 47.66  ? 315  VAL B CG1   1 
ATOM   13362 C  CG2   . VAL B 2  315  ? 126.132 126.821 176.490 1.00 45.95  ? 315  VAL B CG2   1 
ATOM   13363 N  N     . LEU B 2  316  ? 127.686 125.618 178.995 1.00 46.63  ? 316  LEU B N     1 
ATOM   13364 C  CA    . LEU B 2  316  ? 128.992 125.063 179.353 1.00 47.37  ? 316  LEU B CA    1 
ATOM   13365 C  C     . LEU B 2  316  ? 129.930 125.208 178.159 1.00 48.97  ? 316  LEU B C     1 
ATOM   13366 O  O     . LEU B 2  316  ? 129.961 124.365 177.262 1.00 47.17  ? 316  LEU B O     1 
ATOM   13367 C  CB    . LEU B 2  316  ? 128.867 123.606 179.785 1.00 45.91  ? 316  LEU B CB    1 
ATOM   13368 C  CG    . LEU B 2  316  ? 130.159 122.994 180.335 1.00 48.00  ? 316  LEU B CG    1 
ATOM   13369 C  CD1   . LEU B 2  316  ? 130.633 123.751 181.569 1.00 46.45  ? 316  LEU B CD1   1 
ATOM   13370 C  CD2   . LEU B 2  316  ? 129.989 121.520 180.634 1.00 47.23  ? 316  LEU B CD2   1 
ATOM   13371 N  N     . ASP B 2  317  ? 130.703 126.287 178.151 1.00 51.87  ? 317  ASP B N     1 
ATOM   13372 C  CA    . ASP B 2  317  ? 131.745 126.426 177.149 1.00 51.99  ? 317  ASP B CA    1 
ATOM   13373 C  C     . ASP B 2  317  ? 132.887 125.466 177.475 1.00 53.57  ? 317  ASP B C     1 
ATOM   13374 O  O     . ASP B 2  317  ? 133.331 125.402 178.626 1.00 50.59  ? 317  ASP B O     1 
ATOM   13375 C  CB    . ASP B 2  317  ? 132.273 127.859 177.106 1.00 54.11  ? 317  ASP B CB    1 
ATOM   13376 C  CG    . ASP B 2  317  ? 133.308 128.068 176.012 1.00 56.02  ? 317  ASP B CG    1 
ATOM   13377 O  OD1   . ASP B 2  317  ? 132.912 128.199 174.833 1.00 53.98  ? 317  ASP B OD1   1 
ATOM   13378 O  OD2   . ASP B 2  317  ? 134.517 128.053 176.323 1.00 53.64  ? 317  ASP B OD2   1 
ATOM   13379 N  N     . PRO B 2  318  ? 133.384 124.711 176.491 1.00 53.86  ? 318  PRO B N     1 
ATOM   13380 C  CA    . PRO B 2  318  ? 134.415 123.705 176.794 1.00 53.35  ? 318  PRO B CA    1 
ATOM   13381 C  C     . PRO B 2  318  ? 135.667 124.291 177.415 1.00 51.65  ? 318  PRO B C     1 
ATOM   13382 O  O     . PRO B 2  318  ? 136.304 123.627 178.241 1.00 51.27  ? 318  PRO B O     1 
ATOM   13383 C  CB    . PRO B 2  318  ? 134.718 123.083 175.422 1.00 50.93  ? 318  PRO B CB    1 
ATOM   13384 C  CG    . PRO B 2  318  ? 133.545 123.422 174.569 1.00 51.74  ? 318  PRO B CG    1 
ATOM   13385 C  CD    . PRO B 2  318  ? 133.058 124.751 175.056 1.00 50.79  ? 318  PRO B CD    1 
ATOM   13386 N  N     . ILE B 2  319  ? 136.031 125.515 177.057 1.00 49.55  ? 319  ILE B N     1 
ATOM   13387 C  CA    . ILE B 2  319  ? 137.283 126.092 177.525 1.00 51.56  ? 319  ILE B CA    1 
ATOM   13388 C  C     . ILE B 2  319  ? 137.092 126.887 178.813 1.00 52.36  ? 319  ILE B C     1 
ATOM   13389 O  O     . ILE B 2  319  ? 138.044 127.060 179.580 1.00 50.99  ? 319  ILE B O     1 
ATOM   13390 C  CB    . ILE B 2  319  ? 137.889 126.958 176.407 1.00 52.09  ? 319  ILE B CB    1 
ATOM   13391 C  CG1   . ILE B 2  319  ? 137.795 126.218 175.068 1.00 49.51  ? 319  ILE B CG1   1 
ATOM   13392 C  CG2   . ILE B 2  319  ? 139.336 127.319 176.722 1.00 51.04  ? 319  ILE B CG2   1 
ATOM   13393 C  CD1   . ILE B 2  319  ? 138.522 124.889 175.052 1.00 50.16  ? 319  ILE B CD1   1 
ATOM   13394 N  N     . PHE B 2  320  ? 135.873 127.342 179.081 1.00 54.35  ? 320  PHE B N     1 
ATOM   13395 C  CA    . PHE B 2  320  ? 135.536 128.167 180.234 1.00 55.25  ? 320  PHE B CA    1 
ATOM   13396 C  C     . PHE B 2  320  ? 134.630 127.412 181.202 1.00 54.74  ? 320  PHE B C     1 
ATOM   13397 O  O     . PHE B 2  320  ? 133.625 127.936 181.687 1.00 54.59  ? 320  PHE B O     1 
ATOM   13398 C  CB    . PHE B 2  320  ? 134.893 129.475 179.779 1.00 53.32  ? 320  PHE B CB    1 
ATOM   13399 C  CG    . PHE B 2  320  ? 135.830 130.378 179.026 1.00 54.46  ? 320  PHE B CG    1 
ATOM   13400 C  CD1   . PHE B 2  320  ? 136.529 131.375 179.681 1.00 51.83  ? 320  PHE B CD1   1 
ATOM   13401 C  CD2   . PHE B 2  320  ? 136.050 130.198 177.672 1.00 54.38  ? 320  PHE B CD2   1 
ATOM   13402 C  CE1   . PHE B 2  320  ? 137.394 132.200 178.994 1.00 52.96  ? 320  PHE B CE1   1 
ATOM   13403 C  CE2   . PHE B 2  320  ? 136.922 131.016 176.980 1.00 53.72  ? 320  PHE B CE2   1 
ATOM   13404 C  CZ    . PHE B 2  320  ? 137.593 132.020 177.643 1.00 53.23  ? 320  PHE B CZ    1 
ATOM   13405 N  N     . GLN B 2  321  ? 134.976 126.148 181.481 1.00 52.43  ? 321  GLN B N     1 
ATOM   13406 C  CA    . GLN B 2  321  ? 134.185 125.363 182.430 1.00 53.28  ? 321  GLN B CA    1 
ATOM   13407 C  C     . GLN B 2  321  ? 134.551 125.664 183.879 1.00 54.34  ? 321  GLN B C     1 
ATOM   13408 O  O     . GLN B 2  321  ? 133.649 125.982 184.674 1.00 52.52  ? 321  GLN B O     1 
ATOM   13409 C  CB    . GLN B 2  321  ? 134.304 123.873 182.097 1.00 53.58  ? 321  GLN B CB    1 
ATOM   13410 C  CG    . GLN B 2  321  ? 133.734 122.941 183.155 1.00 51.83  ? 321  GLN B CG    1 
ATOM   13411 C  CD    . GLN B 2  321  ? 133.665 121.509 182.669 1.00 53.39  ? 321  GLN B CD    1 
ATOM   13412 O  OE1   . GLN B 2  321  ? 134.057 121.209 181.544 1.00 54.32  ? 321  GLN B OE1   1 
ATOM   13413 N  NE2   . GLN B 2  321  ? 133.159 120.619 183.512 1.00 53.65  ? 321  GLN B NE2   1 
ATOM   13414 N  N     . PRO B 2  322  ? 135.820 125.586 184.300 1.00 54.54  ? 322  PRO B N     1 
ATOM   13415 C  CA    . PRO B 2  322  ? 136.133 125.808 185.719 1.00 52.24  ? 322  PRO B CA    1 
ATOM   13416 C  C     . PRO B 2  322  ? 136.050 127.259 186.164 1.00 50.34  ? 322  PRO B C     1 
ATOM   13417 O  O     . PRO B 2  322  ? 136.342 127.546 187.331 1.00 49.11  ? 322  PRO B O     1 
ATOM   13418 C  CB    . PRO B 2  322  ? 137.574 125.284 185.848 1.00 49.95  ? 322  PRO B CB    1 
ATOM   13419 C  CG    . PRO B 2  322  ? 137.858 124.553 184.568 1.00 49.61  ? 322  PRO B CG    1 
ATOM   13420 C  CD    . PRO B 2  322  ? 137.033 125.233 183.544 1.00 50.33  ? 322  PRO B CD    1 
ATOM   13421 N  N     . VAL B 2  323  ? 135.678 128.184 185.284 1.00 45.82  ? 323  VAL B N     1 
ATOM   13422 C  CA    . VAL B 2  323  ? 135.625 129.600 185.631 1.00 49.16  ? 323  VAL B CA    1 
ATOM   13423 C  C     . VAL B 2  323  ? 134.172 130.045 185.495 1.00 48.19  ? 323  VAL B C     1 
ATOM   13424 O  O     . VAL B 2  323  ? 133.830 131.210 185.731 1.00 44.04  ? 323  VAL B O     1 
ATOM   13425 C  CB    . VAL B 2  323  ? 136.579 130.400 184.721 1.00 47.43  ? 323  VAL B CB    1 
ATOM   13426 C  CG1   . VAL B 2  323  ? 136.298 130.087 183.249 1.00 43.98  ? 323  VAL B CG1   1 
ATOM   13427 C  CG2   . VAL B 2  323  ? 136.571 131.900 185.032 1.00 45.12  ? 323  VAL B CG2   1 
ATOM   13428 N  N     . GLN B 2  324  ? 133.304 129.086 185.170 1.00 47.98  ? 324  GLN B N     1 
ATOM   13429 C  CA    . GLN B 2  324  ? 131.923 129.361 184.787 1.00 49.19  ? 324  GLN B CA    1 
ATOM   13430 C  C     . GLN B 2  324  ? 131.171 130.125 185.871 1.00 50.66  ? 324  GLN B C     1 
ATOM   13431 O  O     . GLN B 2  324  ? 130.354 131.001 185.570 1.00 49.27  ? 324  GLN B O     1 
ATOM   13432 C  CB    . GLN B 2  324  ? 131.218 128.038 184.469 1.00 49.03  ? 324  GLN B CB    1 
ATOM   13433 C  CG    . GLN B 2  324  ? 129.751 128.140 184.090 1.00 47.85  ? 324  GLN B CG    1 
ATOM   13434 C  CD    . GLN B 2  324  ? 129.536 128.732 182.721 1.00 50.13  ? 324  GLN B CD    1 
ATOM   13435 O  OE1   . GLN B 2  324  ? 129.124 129.883 182.588 1.00 51.02  ? 324  GLN B OE1   1 
ATOM   13436 N  NE2   . GLN B 2  324  ? 129.802 127.943 181.688 1.00 48.33  ? 324  GLN B NE2   1 
ATOM   13437 N  N     . HIS B 2  325  ? 131.435 129.809 187.138 1.00 49.98  ? 325  HIS B N     1 
ATOM   13438 C  CA    . HIS B 2  325  ? 130.703 130.388 188.256 1.00 49.74  ? 325  HIS B CA    1 
ATOM   13439 C  C     . HIS B 2  325  ? 131.613 131.128 189.234 1.00 50.62  ? 325  HIS B C     1 
ATOM   13440 O  O     . HIS B 2  325  ? 131.229 131.348 190.386 1.00 51.90  ? 325  HIS B O     1 
ATOM   13441 C  CB    . HIS B 2  325  ? 129.918 129.289 188.972 1.00 50.06  ? 325  HIS B CB    1 
ATOM   13442 C  CG    . HIS B 2  325  ? 128.882 128.633 188.110 1.00 50.48  ? 325  HIS B CG    1 
ATOM   13443 N  ND1   . HIS B 2  325  ? 128.342 127.398 188.400 1.00 50.78  ? 325  HIS B ND1   1 
ATOM   13444 C  CD2   . HIS B 2  325  ? 128.274 129.050 186.975 1.00 49.54  ? 325  HIS B CD2   1 
ATOM   13445 C  CE1   . HIS B 2  325  ? 127.456 127.078 187.474 1.00 50.22  ? 325  HIS B CE1   1 
ATOM   13446 N  NE2   . HIS B 2  325  ? 127.396 128.063 186.597 1.00 53.10  ? 325  HIS B NE2   1 
ATOM   13447 N  N     . GLU B 2  326  ? 132.798 131.538 188.790 1.00 50.61  ? 326  GLU B N     1 
ATOM   13448 C  CA    . GLU B 2  326  ? 133.746 132.216 189.664 1.00 52.72  ? 326  GLU B CA    1 
ATOM   13449 C  C     . GLU B 2  326  ? 133.201 133.566 190.119 1.00 52.30  ? 326  GLU B C     1 
ATOM   13450 O  O     . GLU B 2  326  ? 132.427 134.220 189.417 1.00 50.86  ? 326  GLU B O     1 
ATOM   13451 C  CB    . GLU B 2  326  ? 135.079 132.410 188.944 1.00 50.86  ? 326  GLU B CB    1 
ATOM   13452 C  CG    . GLU B 2  326  ? 136.176 133.022 189.788 1.00 49.69  ? 326  GLU B CG    1 
ATOM   13453 C  CD    . GLU B 2  326  ? 137.549 132.715 189.247 1.00 53.25  ? 326  GLU B CD    1 
ATOM   13454 O  OE1   . GLU B 2  326  ? 137.683 131.740 188.475 1.00 52.27  ? 326  GLU B OE1   1 
ATOM   13455 O  OE2   . GLU B 2  326  ? 138.491 133.460 189.579 1.00 52.53  ? 326  GLU B OE2   1 
ATOM   13456 N  N     . LEU B 2  327  ? 133.621 133.986 191.311 1.00 51.24  ? 327  LEU B N     1 
ATOM   13457 C  CA    . LEU B 2  327  ? 133.081 135.181 191.945 1.00 50.67  ? 327  LEU B CA    1 
ATOM   13458 C  C     . LEU B 2  327  ? 133.973 136.411 191.827 1.00 52.40  ? 327  LEU B C     1 
ATOM   13459 O  O     . LEU B 2  327  ? 133.453 137.530 191.857 1.00 50.82  ? 327  LEU B O     1 
ATOM   13460 C  CB    . LEU B 2  327  ? 132.799 134.902 193.426 1.00 51.44  ? 327  LEU B CB    1 
ATOM   13461 C  CG    . LEU B 2  327  ? 131.475 134.209 193.759 1.00 53.59  ? 327  LEU B CG    1 
ATOM   13462 C  CD1   . LEU B 2  327  ? 131.554 132.719 193.513 1.00 50.94  ? 327  LEU B CD1   1 
ATOM   13463 C  CD2   . LEU B 2  327  ? 131.084 134.487 195.204 1.00 50.42  ? 327  LEU B CD2   1 
ATOM   13464 N  N     . ASN B 2  328  ? 135.289 136.254 191.681 1.00 48.39  ? 328  ASN B N     1 
ATOM   13465 C  CA    . ASN B 2  328  ? 136.201 137.394 191.658 1.00 50.26  ? 328  ASN B CA    1 
ATOM   13466 C  C     . ASN B 2  328  ? 136.827 137.539 190.277 1.00 52.08  ? 328  ASN B C     1 
ATOM   13467 O  O     . ASN B 2  328  ? 136.394 136.918 189.302 1.00 52.36  ? 328  ASN B O     1 
ATOM   13468 C  CB    . ASN B 2  328  ? 137.297 137.282 192.724 1.00 51.15  ? 328  ASN B CB    1 
ATOM   13469 C  CG    . ASN B 2  328  ? 137.612 138.622 193.373 1.00 52.78  ? 328  ASN B CG    1 
ATOM   13470 O  OD1   . ASN B 2  328  ? 136.982 139.636 193.065 1.00 49.58  ? 328  ASN B OD1   1 
ATOM   13471 N  ND2   . ASN B 2  328  ? 138.602 138.637 194.257 1.00 51.17  ? 328  ASN B ND2   1 
ATOM   13472 N  N     . ARG B 2  329  ? 137.843 138.401 190.194 1.00 51.97  ? 329  ARG B N     1 
ATOM   13473 C  CA    . ARG B 2  329  ? 138.412 138.784 188.908 1.00 54.44  ? 329  ARG B CA    1 
ATOM   13474 C  C     . ARG B 2  329  ? 139.850 138.314 188.716 1.00 55.82  ? 329  ARG B C     1 
ATOM   13475 O  O     . ARG B 2  329  ? 140.205 137.874 187.619 1.00 52.49  ? 329  ARG B O     1 
ATOM   13476 C  CB    . ARG B 2  329  ? 138.359 140.304 188.746 1.00 52.23  ? 329  ARG B CB    1 
ATOM   13477 C  CG    . ARG B 2  329  ? 137.078 140.940 189.233 1.00 49.58  ? 329  ARG B CG    1 
ATOM   13478 C  CD    . ARG B 2  329  ? 137.181 142.451 189.181 1.00 51.59  ? 329  ARG B CD    1 
ATOM   13479 N  NE    . ARG B 2  329  ? 138.300 142.969 189.960 1.00 55.18  ? 329  ARG B NE    1 
ATOM   13480 C  CZ    . ARG B 2  329  ? 138.235 143.285 191.246 1.00 56.33  ? 329  ARG B CZ    1 
ATOM   13481 N  NH1   . ARG B 2  329  ? 137.116 143.143 191.938 1.00 54.46  ? 329  ARG B NH1   1 
ATOM   13482 N  NH2   . ARG B 2  329  ? 139.319 143.760 191.852 1.00 52.11  ? 329  ARG B NH2   1 
ATOM   13483 N  N     . GLU B 2  330  ? 140.682 138.405 189.762 1.00 55.76  ? 330  GLU B N     1 
ATOM   13484 C  CA    . GLU B 2  330  ? 142.124 138.218 189.602 1.00 53.33  ? 330  GLU B CA    1 
ATOM   13485 C  C     . GLU B 2  330  ? 142.460 136.801 189.146 1.00 53.59  ? 330  GLU B C     1 
ATOM   13486 O  O     . GLU B 2  330  ? 143.330 136.603 188.287 1.00 51.71  ? 330  GLU B O     1 
ATOM   13487 C  CB    . GLU B 2  330  ? 142.837 138.573 190.910 1.00 53.36  ? 330  GLU B CB    1 
ATOM   13488 C  CG    . GLU B 2  330  ? 144.336 138.868 190.780 1.00 55.40  ? 330  GLU B CG    1 
ATOM   13489 C  CD    . GLU B 2  330  ? 145.219 137.808 191.416 1.00 57.75  ? 330  GLU B CD    1 
ATOM   13490 O  OE1   . GLU B 2  330  ? 144.856 137.298 192.497 1.00 55.58  ? 330  GLU B OE1   1 
ATOM   13491 O  OE2   . GLU B 2  330  ? 146.285 137.495 190.848 1.00 56.73  ? 330  GLU B OE2   1 
ATOM   13492 N  N     . LYS B 2  331  ? 141.770 135.800 189.686 1.00 50.58  ? 331  LYS B N     1 
ATOM   13493 C  CA    . LYS B 2  331  ? 141.996 134.441 189.211 1.00 53.71  ? 331  LYS B CA    1 
ATOM   13494 C  C     . LYS B 2  331  ? 141.393 134.186 187.834 1.00 54.05  ? 331  LYS B C     1 
ATOM   13495 O  O     . LYS B 2  331  ? 141.919 133.352 187.092 1.00 53.21  ? 331  LYS B O     1 
ATOM   13496 C  CB    . LYS B 2  331  ? 141.469 133.427 190.225 1.00 51.79  ? 331  LYS B CB    1 
ATOM   13497 C  CG    . LYS B 2  331  ? 142.210 133.467 191.551 1.00 50.55  ? 331  LYS B CG    1 
ATOM   13498 C  CD    . LYS B 2  331  ? 143.677 133.118 191.341 1.00 51.12  ? 331  LYS B CD    1 
ATOM   13499 C  CE    . LYS B 2  331  ? 144.451 133.093 192.650 1.00 51.59  ? 331  LYS B CE    1 
ATOM   13500 N  NZ    . LYS B 2  331  ? 145.869 132.675 192.448 1.00 52.55  ? 331  LYS B NZ    1 
ATOM   13501 N  N     . ILE B 2  332  ? 140.323 134.892 187.460 1.00 51.16  ? 332  ILE B N     1 
ATOM   13502 C  CA    . ILE B 2  332  ? 139.849 134.818 186.079 1.00 48.64  ? 332  ILE B CA    1 
ATOM   13503 C  C     . ILE B 2  332  ? 140.910 135.356 185.128 1.00 49.08  ? 332  ILE B C     1 
ATOM   13504 O  O     . ILE B 2  332  ? 141.154 134.789 184.055 1.00 48.98  ? 332  ILE B O     1 
ATOM   13505 C  CB    . ILE B 2  332  ? 138.516 135.570 185.922 1.00 46.40  ? 332  ILE B CB    1 
ATOM   13506 C  CG1   . ILE B 2  332  ? 137.433 134.923 186.786 1.00 47.89  ? 332  ILE B CG1   1 
ATOM   13507 C  CG2   . ILE B 2  332  ? 138.096 135.585 184.473 1.00 47.91  ? 332  ILE B CG2   1 
ATOM   13508 C  CD1   . ILE B 2  332  ? 136.036 135.433 186.523 1.00 46.43  ? 332  ILE B CD1   1 
ATOM   13509 N  N     . ILE B 2  333  ? 141.549 136.465 185.506 1.00 45.44  ? 333  ILE B N     1 
ATOM   13510 C  CA    . ILE B 2  333  ? 142.667 137.006 184.741 1.00 48.62  ? 333  ILE B CA    1 
ATOM   13511 C  C     . ILE B 2  333  ? 143.803 135.998 184.665 1.00 51.69  ? 333  ILE B C     1 
ATOM   13512 O  O     . ILE B 2  333  ? 144.462 135.864 183.625 1.00 46.98  ? 333  ILE B O     1 
ATOM   13513 C  CB    . ILE B 2  333  ? 143.134 138.332 185.372 1.00 47.79  ? 333  ILE B CB    1 
ATOM   13514 C  CG1   . ILE B 2  333  ? 141.957 139.291 185.527 1.00 46.27  ? 333  ILE B CG1   1 
ATOM   13515 C  CG2   . ILE B 2  333  ? 144.252 138.959 184.556 1.00 46.39  ? 333  ILE B CG2   1 
ATOM   13516 C  CD1   . ILE B 2  333  ? 142.154 140.318 186.610 1.00 46.92  ? 333  ILE B CD1   1 
ATOM   13517 N  N     . GLN B 2  334  ? 144.064 135.287 185.763 1.00 52.94  ? 334  GLN B N     1 
ATOM   13518 C  CA    . GLN B 2  334  ? 145.114 134.273 185.750 1.00 54.13  ? 334  GLN B CA    1 
ATOM   13519 C  C     . GLN B 2  334  ? 144.779 133.149 184.775 1.00 53.90  ? 334  GLN B C     1 
ATOM   13520 O  O     . GLN B 2  334  ? 145.640 132.689 184.016 1.00 52.83  ? 334  GLN B O     1 
ATOM   13521 C  CB    . GLN B 2  334  ? 145.335 133.726 187.160 1.00 53.37  ? 334  GLN B CB    1 
ATOM   13522 C  CG    . GLN B 2  334  ? 146.362 132.610 187.212 1.00 53.33  ? 334  GLN B CG    1 
ATOM   13523 C  CD    . GLN B 2  334  ? 147.722 133.059 186.709 1.00 55.90  ? 334  GLN B CD    1 
ATOM   13524 O  OE1   . GLN B 2  334  ? 148.234 134.104 187.114 1.00 57.14  ? 334  GLN B OE1   1 
ATOM   13525 N  NE2   . GLN B 2  334  ? 148.302 132.280 185.801 1.00 54.92  ? 334  GLN B NE2   1 
ATOM   13526 N  N     . PHE B 2  335  ? 143.523 132.697 184.780 1.00 50.54  ? 335  PHE B N     1 
ATOM   13527 C  CA    . PHE B 2  335  ? 143.090 131.668 183.838 1.00 52.16  ? 335  PHE B CA    1 
ATOM   13528 C  C     . PHE B 2  335  ? 143.201 132.158 182.399 1.00 51.71  ? 335  PHE B C     1 
ATOM   13529 O  O     . PHE B 2  335  ? 143.598 131.394 181.503 1.00 47.51  ? 335  PHE B O     1 
ATOM   13530 C  CB    . PHE B 2  335  ? 141.658 131.241 184.177 1.00 52.56  ? 335  PHE B CB    1 
ATOM   13531 C  CG    . PHE B 2  335  ? 141.194 130.003 183.456 1.00 53.76  ? 335  PHE B CG    1 
ATOM   13532 C  CD1   . PHE B 2  335  ? 141.748 128.768 183.745 1.00 52.86  ? 335  PHE B CD1   1 
ATOM   13533 C  CD2   . PHE B 2  335  ? 140.165 130.068 182.533 1.00 51.82  ? 335  PHE B CD2   1 
ATOM   13534 C  CE1   . PHE B 2  335  ? 141.317 127.627 183.094 1.00 53.10  ? 335  PHE B CE1   1 
ATOM   13535 C  CE2   . PHE B 2  335  ? 139.725 128.931 181.879 1.00 54.11  ? 335  PHE B CE2   1 
ATOM   13536 C  CZ    . PHE B 2  335  ? 140.300 127.709 182.161 1.00 54.57  ? 335  PHE B CZ    1 
ATOM   13537 N  N     . LEU B 2  336  ? 142.884 133.432 182.166 1.00 49.34  ? 336  LEU B N     1 
ATOM   13538 C  CA    . LEU B 2  336  ? 143.076 134.016 180.844 1.00 50.91  ? 336  LEU B CA    1 
ATOM   13539 C  C     . LEU B 2  336  ? 144.538 133.960 180.428 1.00 50.20  ? 336  LEU B C     1 
ATOM   13540 O  O     . LEU B 2  336  ? 144.860 133.558 179.305 1.00 50.33  ? 336  LEU B O     1 
ATOM   13541 C  CB    . LEU B 2  336  ? 142.579 135.459 180.830 1.00 50.10  ? 336  LEU B CB    1 
ATOM   13542 C  CG    . LEU B 2  336  ? 142.872 136.198 179.526 1.00 50.13  ? 336  LEU B CG    1 
ATOM   13543 C  CD1   . LEU B 2  336  ? 142.010 135.630 178.407 1.00 46.08  ? 336  LEU B CD1   1 
ATOM   13544 C  CD2   . LEU B 2  336  ? 142.642 137.691 179.689 1.00 49.15  ? 336  LEU B CD2   1 
ATOM   13545 N  N     . SER B 2  337  ? 145.438 134.365 181.326 1.00 44.71  ? 337  SER B N     1 
ATOM   13546 C  CA    . SER B 2  337  ? 146.862 134.350 181.007 1.00 47.14  ? 337  SER B CA    1 
ATOM   13547 C  C     . SER B 2  337  ? 147.346 132.930 180.747 1.00 48.68  ? 337  SER B C     1 
ATOM   13548 O  O     . SER B 2  337  ? 148.252 132.711 179.935 1.00 44.92  ? 337  SER B O     1 
ATOM   13549 C  CB    . SER B 2  337  ? 147.659 134.995 182.139 1.00 46.82  ? 337  SER B CB    1 
ATOM   13550 O  OG    . SER B 2  337  ? 149.030 135.102 181.805 1.00 46.40  ? 337  SER B OG    1 
ATOM   13551 N  N     . GLU B 2  338  ? 146.761 131.952 181.443 1.00 51.37  ? 338  GLU B N     1 
ATOM   13552 C  CA    . GLU B 2  338  ? 147.060 130.552 181.158 1.00 51.59  ? 338  GLU B CA    1 
ATOM   13553 C  C     . GLU B 2  338  ? 146.651 130.179 179.740 1.00 51.96  ? 338  GLU B C     1 
ATOM   13554 O  O     . GLU B 2  338  ? 147.371 129.458 179.042 1.00 48.94  ? 338  GLU B O     1 
ATOM   13555 C  CB    . GLU B 2  338  ? 146.345 129.642 182.158 1.00 52.59  ? 338  GLU B CB    1 
ATOM   13556 C  CG    . GLU B 2  338  ? 146.900 129.666 183.569 1.00 51.76  ? 338  GLU B CG    1 
ATOM   13557 C  CD    . GLU B 2  338  ? 146.343 128.542 184.418 1.00 53.01  ? 338  GLU B CD    1 
ATOM   13558 O  OE1   . GLU B 2  338  ? 145.612 127.690 183.875 1.00 52.97  ? 338  GLU B OE1   1 
ATOM   13559 O  OE2   . GLU B 2  338  ? 146.622 128.515 185.632 1.00 53.52  ? 338  GLU B OE2   1 
ATOM   13560 N  N     . LYS B 2  339  ? 145.482 130.648 179.306 1.00 54.81  ? 339  LYS B N     1 
ATOM   13561 C  CA    . LYS B 2  339  ? 144.987 130.282 177.981 1.00 53.10  ? 339  LYS B CA    1 
ATOM   13562 C  C     . LYS B 2  339  ? 145.755 130.977 176.857 1.00 53.39  ? 339  LYS B C     1 
ATOM   13563 O  O     . LYS B 2  339  ? 146.088 130.353 175.843 1.00 53.36  ? 339  LYS B O     1 
ATOM   13564 C  CB    . LYS B 2  339  ? 143.493 130.591 177.877 1.00 50.09  ? 339  LYS B CB    1 
ATOM   13565 C  CG    . LYS B 2  339  ? 142.643 129.773 178.826 1.00 54.43  ? 339  LYS B CG    1 
ATOM   13566 C  CD    . LYS B 2  339  ? 141.172 129.935 178.514 1.00 56.23  ? 339  LYS B CD    1 
ATOM   13567 C  CE    . LYS B 2  339  ? 140.789 131.400 178.598 1.00 55.39  ? 339  LYS B CE    1 
ATOM   13568 N  NZ    . LYS B 2  339  ? 140.684 131.875 180.000 1.00 52.13  ? 339  LYS B NZ    1 
ATOM   13569 N  N     . VAL B 2  340  ? 146.034 132.272 177.007 1.00 48.13  ? 340  VAL B N     1 
ATOM   13570 C  CA    . VAL B 2  340  ? 146.450 133.067 175.855 1.00 51.24  ? 340  VAL B CA    1 
ATOM   13571 C  C     . VAL B 2  340  ? 147.959 133.237 175.702 1.00 50.77  ? 340  VAL B C     1 
ATOM   13572 O  O     . VAL B 2  340  ? 148.433 133.426 174.572 1.00 49.64  ? 340  VAL B O     1 
ATOM   13573 C  CB    . VAL B 2  340  ? 145.782 134.454 175.889 1.00 50.93  ? 340  VAL B CB    1 
ATOM   13574 C  CG1   . VAL B 2  340  ? 144.286 134.303 176.041 1.00 50.06  ? 340  VAL B CG1   1 
ATOM   13575 C  CG2   . VAL B 2  340  ? 146.351 135.302 177.014 1.00 48.89  ? 340  VAL B CG2   1 
ATOM   13576 N  N     . SER B 2  341  ? 148.726 133.165 176.789 1.00 47.47  ? 341  SER B N     1 
ATOM   13577 C  CA    . SER B 2  341  ? 150.163 133.423 176.721 1.00 49.59  ? 341  SER B CA    1 
ATOM   13578 C  C     . SER B 2  341  ? 150.843 132.321 175.914 1.00 50.85  ? 341  SER B C     1 
ATOM   13579 O  O     . SER B 2  341  ? 150.868 131.158 176.332 1.00 47.44  ? 341  SER B O     1 
ATOM   13580 C  CB    . SER B 2  341  ? 150.749 133.521 178.125 1.00 49.70  ? 341  SER B CB    1 
ATOM   13581 O  OG    . SER B 2  341  ? 152.102 133.933 178.087 1.00 49.33  ? 341  SER B OG    1 
ATOM   13582 N  N     . LYS B 2  342  ? 151.372 132.685 174.742 1.00 53.03  ? 342  LYS B N     1 
ATOM   13583 C  CA    . LYS B 2  342  ? 151.985 131.698 173.857 1.00 51.94  ? 342  LYS B CA    1 
ATOM   13584 C  C     . LYS B 2  342  ? 153.380 131.307 174.331 1.00 52.67  ? 342  LYS B C     1 
ATOM   13585 O  O     . LYS B 2  342  ? 153.773 130.139 174.224 1.00 51.88  ? 342  LYS B O     1 
ATOM   13586 C  CB    . LYS B 2  342  ? 152.022 132.237 172.428 1.00 50.32  ? 342  LYS B CB    1 
ATOM   13587 C  CG    . LYS B 2  342  ? 150.640 132.434 171.835 1.00 50.75  ? 342  LYS B CG    1 
ATOM   13588 C  CD    . LYS B 2  342  ? 150.680 133.098 170.472 1.00 51.29  ? 342  LYS B CD    1 
ATOM   13589 C  CE    . LYS B 2  342  ? 149.289 133.121 169.857 1.00 51.59  ? 342  LYS B CE    1 
ATOM   13590 N  NZ    . LYS B 2  342  ? 148.352 133.990 170.625 1.00 51.10  ? 342  LYS B NZ    1 
ATOM   13591 N  N     . PHE B 2  343  ? 154.144 132.268 174.851 1.00 51.85  ? 343  PHE B N     1 
ATOM   13592 C  CA    . PHE B 2  343  ? 155.471 131.987 175.385 1.00 52.22  ? 343  PHE B CA    1 
ATOM   13593 C  C     . PHE B 2  343  ? 155.429 131.240 176.714 1.00 52.50  ? 343  PHE B C     1 
ATOM   13594 O  O     . PHE B 2  343  ? 156.484 130.825 177.206 1.00 52.78  ? 343  PHE B O     1 
ATOM   13595 C  CB    . PHE B 2  343  ? 156.264 133.291 175.539 1.00 52.56  ? 343  PHE B CB    1 
ATOM   13596 C  CG    . PHE B 2  343  ? 155.654 134.262 176.512 1.00 53.66  ? 343  PHE B CG    1 
ATOM   13597 C  CD1   . PHE B 2  343  ? 154.678 135.153 176.099 1.00 52.12  ? 343  PHE B CD1   1 
ATOM   13598 C  CD2   . PHE B 2  343  ? 156.051 134.279 177.841 1.00 51.74  ? 343  PHE B CD2   1 
ATOM   13599 C  CE1   . PHE B 2  343  ? 154.115 136.044 176.988 1.00 52.61  ? 343  PHE B CE1   1 
ATOM   13600 C  CE2   . PHE B 2  343  ? 155.486 135.165 178.734 1.00 53.23  ? 343  PHE B CE2   1 
ATOM   13601 C  CZ    . PHE B 2  343  ? 154.518 136.048 178.307 1.00 53.88  ? 343  PHE B CZ    1 
ATOM   13602 N  N     . VAL B 2  344  ? 154.252 131.076 177.308 1.00 48.54  ? 344  VAL B N     1 
ATOM   13603 C  CA    . VAL B 2  344  ? 154.078 130.284 178.520 1.00 52.33  ? 344  VAL B CA    1 
ATOM   13604 C  C     . VAL B 2  344  ? 153.592 128.904 178.102 1.00 52.86  ? 344  VAL B C     1 
ATOM   13605 O  O     . VAL B 2  344  ? 152.591 128.776 177.390 1.00 51.57  ? 344  VAL B O     1 
ATOM   13606 C  CB    . VAL B 2  344  ? 153.102 130.945 179.503 1.00 51.63  ? 344  VAL B CB    1 
ATOM   13607 C  CG1   . VAL B 2  344  ? 152.611 129.927 180.518 1.00 49.89  ? 344  VAL B CG1   1 
ATOM   13608 C  CG2   . VAL B 2  344  ? 153.777 132.110 180.213 1.00 49.71  ? 344  VAL B CG2   1 
ATOM   13609 N  N     . SER B 2  345  ? 154.315 127.866 178.527 1.00 49.74  ? 345  SER B N     1 
ATOM   13610 C  CA    . SER B 2  345  ? 153.936 126.489 178.244 1.00 48.71  ? 345  SER B CA    1 
ATOM   13611 C  C     . SER B 2  345  ? 154.208 125.558 179.421 1.00 49.11  ? 345  SER B C     1 
ATOM   13612 O  O     . SER B 2  345  ? 154.042 124.340 179.285 1.00 47.86  ? 345  SER B O     1 
ATOM   13613 C  CB    . SER B 2  345  ? 154.661 125.983 176.990 1.00 46.04  ? 345  SER B CB    1 
ATOM   13614 O  OG    . SER B 2  345  ? 156.062 125.969 177.179 1.00 46.19  ? 345  SER B OG    1 
ATOM   13615 N  N     . ASN B 2  346  ? 154.608 126.097 180.571 1.00 49.99  ? 346  ASN B N     1 
ATOM   13616 C  CA    . ASN B 2  346  ? 154.921 125.309 181.763 1.00 49.98  ? 346  ASN B CA    1 
ATOM   13617 C  C     . ASN B 2  346  ? 154.107 125.851 182.928 1.00 49.72  ? 346  ASN B C     1 
ATOM   13618 O  O     . ASN B 2  346  ? 154.601 126.660 183.726 1.00 48.89  ? 346  ASN B O     1 
ATOM   13619 C  CB    . ASN B 2  346  ? 156.417 125.343 182.079 1.00 49.29  ? 346  ASN B CB    1 
ATOM   13620 C  CG    . ASN B 2  346  ? 156.809 124.353 183.160 1.00 50.36  ? 346  ASN B CG    1 
ATOM   13621 O  OD1   . ASN B 2  346  ? 155.961 123.663 183.726 1.00 47.92  ? 346  ASN B OD1   1 
ATOM   13622 N  ND2   . ASN B 2  346  ? 158.099 124.287 183.460 1.00 47.80  ? 346  ASN B ND2   1 
ATOM   13623 N  N     . PRO B 2  347  ? 152.851 125.435 183.054 1.00 48.59  ? 347  PRO B N     1 
ATOM   13624 C  CA    . PRO B 2  347  ? 152.066 125.806 184.233 1.00 48.39  ? 347  PRO B CA    1 
ATOM   13625 C  C     . PRO B 2  347  ? 152.624 125.141 185.483 1.00 49.99  ? 347  PRO B C     1 
ATOM   13626 O  O     . PRO B 2  347  ? 153.441 124.220 185.426 1.00 49.53  ? 347  PRO B O     1 
ATOM   13627 C  CB    . PRO B 2  347  ? 150.657 125.301 183.904 1.00 47.26  ? 347  PRO B CB    1 
ATOM   13628 C  CG    . PRO B 2  347  ? 150.664 125.026 182.423 1.00 47.39  ? 347  PRO B CG    1 
ATOM   13629 C  CD    . PRO B 2  347  ? 152.066 124.633 182.102 1.00 47.88  ? 347  PRO B CD    1 
ATOM   13630 N  N     . SER B 2  348  ? 152.176 125.643 186.632 1.00 47.90  ? 348  SER B N     1 
ATOM   13631 C  CA    . SER B 2  348  ? 152.604 125.201 187.957 1.00 47.54  ? 348  SER B CA    1 
ATOM   13632 C  C     . SER B 2  348  ? 154.094 125.420 188.202 1.00 47.32  ? 348  SER B C     1 
ATOM   13633 O  O     . SER B 2  348  ? 154.656 124.844 189.142 1.00 47.01  ? 348  SER B O     1 
ATOM   13634 C  CB    . SER B 2  348  ? 152.242 123.732 188.208 1.00 43.74  ? 348  SER B CB    1 
ATOM   13635 O  OG    . SER B 2  348  ? 152.687 123.309 189.484 1.00 43.75  ? 348  SER B OG    1 
ATOM   13636 N  N     . ALA B 2  349  ? 154.750 126.242 187.383 1.00 47.21  ? 349  ALA B N     1 
ATOM   13637 C  CA    . ALA B 2  349  ? 156.123 126.670 187.618 1.00 48.86  ? 349  ALA B CA    1 
ATOM   13638 C  C     . ALA B 2  349  ? 156.220 128.154 187.935 1.00 48.37  ? 349  ALA B C     1 
ATOM   13639 O  O     . ALA B 2  349  ? 156.865 128.537 188.914 1.00 47.70  ? 349  ALA B O     1 
ATOM   13640 C  CB    . ALA B 2  349  ? 157.001 126.335 186.403 1.00 47.12  ? 349  ALA B CB    1 
ATOM   13641 N  N     . TYR B 2  350  ? 155.592 129.011 187.127 1.00 53.62  ? 350  TYR B N     1 
ATOM   13642 C  CA    . TYR B 2  350  ? 155.585 130.436 187.434 1.00 55.31  ? 350  TYR B CA    1 
ATOM   13643 C  C     . TYR B 2  350  ? 154.614 130.772 188.558 1.00 55.86  ? 350  TYR B C     1 
ATOM   13644 O  O     . TYR B 2  350  ? 154.739 131.837 189.174 1.00 54.12  ? 350  TYR B O     1 
ATOM   13645 C  CB    . TYR B 2  350  ? 155.240 131.254 186.187 1.00 53.15  ? 350  TYR B CB    1 
ATOM   13646 C  CG    . TYR B 2  350  ? 153.877 130.968 185.602 1.00 54.82  ? 350  TYR B CG    1 
ATOM   13647 C  CD1   . TYR B 2  350  ? 153.686 129.929 184.699 1.00 55.48  ? 350  TYR B CD1   1 
ATOM   13648 C  CD2   . TYR B 2  350  ? 152.779 131.751 185.942 1.00 54.65  ? 350  TYR B CD2   1 
ATOM   13649 C  CE1   . TYR B 2  350  ? 152.435 129.672 184.157 1.00 55.75  ? 350  TYR B CE1   1 
ATOM   13650 C  CE2   . TYR B 2  350  ? 151.528 131.499 185.406 1.00 56.07  ? 350  TYR B CE2   1 
ATOM   13651 C  CZ    . TYR B 2  350  ? 151.363 130.458 184.516 1.00 56.44  ? 350  TYR B CZ    1 
ATOM   13652 O  OH    . TYR B 2  350  ? 150.123 130.209 183.983 1.00 53.53  ? 350  TYR B OH    1 
ATOM   13653 N  N     . LYS B 2  351  ? 153.651 129.890 188.832 1.00 51.59  ? 351  LYS B N     1 
ATOM   13654 C  CA    . LYS B 2  351  ? 152.708 130.073 189.924 1.00 50.00  ? 351  LYS B CA    1 
ATOM   13655 C  C     . LYS B 2  351  ? 153.331 129.806 191.286 1.00 51.20  ? 351  LYS B C     1 
ATOM   13656 O  O     . LYS B 2  351  ? 152.717 130.141 192.306 1.00 50.99  ? 351  LYS B O     1 
ATOM   13657 C  CB    . LYS B 2  351  ? 151.501 129.154 189.726 1.00 50.74  ? 351  LYS B CB    1 
ATOM   13658 C  CG    . LYS B 2  351  ? 150.842 129.287 188.365 1.00 51.34  ? 351  LYS B CG    1 
ATOM   13659 C  CD    . LYS B 2  351  ? 149.995 128.064 188.049 1.00 50.31  ? 351  LYS B CD    1 
ATOM   13660 C  CE    . LYS B 2  351  ? 149.606 128.033 186.586 1.00 47.88  ? 351  LYS B CE    1 
ATOM   13661 N  NZ    . LYS B 2  351  ? 148.919 126.761 186.230 1.00 48.46  ? 351  LYS B NZ    1 
ATOM   13662 N  N     . SER B 2  352  ? 154.519 129.199 191.326 1.00 50.49  ? 352  SER B N     1 
ATOM   13663 C  CA    . SER B 2  352  ? 155.250 129.003 192.571 1.00 48.85  ? 352  SER B CA    1 
ATOM   13664 C  C     . SER B 2  352  ? 155.795 130.303 193.138 1.00 48.40  ? 352  SER B C     1 
ATOM   13665 O  O     . SER B 2  352  ? 156.133 130.346 194.326 1.00 46.74  ? 352  SER B O     1 
ATOM   13666 C  CB    . SER B 2  352  ? 156.408 128.022 192.363 1.00 45.27  ? 352  SER B CB    1 
ATOM   13667 O  OG    . SER B 2  352  ? 155.945 126.743 191.971 1.00 44.59  ? 352  SER B OG    1 
ATOM   13668 N  N     . ASP B 2  353  ? 155.883 131.352 192.326 1.00 54.16  ? 353  ASP B N     1 
ATOM   13669 C  CA    . ASP B 2  353  ? 156.365 132.658 192.746 1.00 55.50  ? 353  ASP B CA    1 
ATOM   13670 C  C     . ASP B 2  353  ? 155.194 133.634 192.763 1.00 56.83  ? 353  ASP B C     1 
ATOM   13671 O  O     . ASP B 2  353  ? 154.070 133.297 192.382 1.00 57.50  ? 353  ASP B O     1 
ATOM   13672 C  CB    . ASP B 2  353  ? 157.491 133.151 191.824 1.00 53.38  ? 353  ASP B CB    1 
ATOM   13673 C  CG    . ASP B 2  353  ? 158.411 134.156 192.506 1.00 57.71  ? 353  ASP B CG    1 
ATOM   13674 O  OD1   . ASP B 2  353  ? 159.223 133.737 193.358 1.00 56.24  ? 353  ASP B OD1   1 
ATOM   13675 O  OD2   . ASP B 2  353  ? 158.331 135.362 192.186 1.00 58.90  ? 353  ASP B OD2   1 
ATOM   13676 N  N     . GLU B 2  354  ? 155.456 134.854 193.232 1.00 52.27  ? 354  GLU B N     1 
ATOM   13677 C  CA    . GLU B 2  354  ? 154.401 135.849 193.395 1.00 52.61  ? 354  GLU B CA    1 
ATOM   13678 C  C     . GLU B 2  354  ? 154.453 136.974 192.371 1.00 52.99  ? 354  GLU B C     1 
ATOM   13679 O  O     . GLU B 2  354  ? 153.406 137.375 191.852 1.00 53.42  ? 354  GLU B O     1 
ATOM   13680 C  CB    . GLU B 2  354  ? 154.454 136.453 194.802 1.00 52.64  ? 354  GLU B CB    1 
ATOM   13681 C  CG    . GLU B 2  354  ? 153.294 137.380 195.095 1.00 53.48  ? 354  GLU B CG    1 
ATOM   13682 C  CD    . GLU B 2  354  ? 153.665 138.836 194.906 1.00 56.09  ? 354  GLU B CD    1 
ATOM   13683 O  OE1   . GLU B 2  354  ? 154.818 139.200 195.224 1.00 54.75  ? 354  GLU B OE1   1 
ATOM   13684 O  OE2   . GLU B 2  354  ? 152.815 139.609 194.417 1.00 54.70  ? 354  GLU B OE2   1 
ATOM   13685 N  N     . ASN B 2  355  ? 155.644 137.497 192.067 1.00 50.10  ? 355  ASN B N     1 
ATOM   13686 C  CA    . ASN B 2  355  ? 155.739 138.668 191.199 1.00 51.73  ? 355  ASN B CA    1 
ATOM   13687 C  C     . ASN B 2  355  ? 155.182 138.384 189.809 1.00 53.66  ? 355  ASN B C     1 
ATOM   13688 O  O     . ASN B 2  355  ? 154.581 139.267 189.187 1.00 54.01  ? 355  ASN B O     1 
ATOM   13689 C  CB    . ASN B 2  355  ? 157.189 139.141 191.105 1.00 51.73  ? 355  ASN B CB    1 
ATOM   13690 C  CG    . ASN B 2  355  ? 157.642 139.892 192.342 1.00 53.71  ? 355  ASN B CG    1 
ATOM   13691 O  OD1   . ASN B 2  355  ? 156.893 140.683 192.910 1.00 53.97  ? 355  ASN B OD1   1 
ATOM   13692 N  ND2   . ASN B 2  355  ? 158.880 139.654 192.758 1.00 52.93  ? 355  ASN B ND2   1 
ATOM   13693 N  N     . ALA B 2  356  ? 155.380 137.163 189.303 1.00 49.39  ? 356  ALA B N     1 
ATOM   13694 C  CA    . ALA B 2  356  ? 154.914 136.835 187.958 1.00 48.43  ? 356  ALA B CA    1 
ATOM   13695 C  C     . ALA B 2  356  ? 153.395 136.902 187.865 1.00 47.60  ? 356  ALA B C     1 
ATOM   13696 O  O     . ALA B 2  356  ? 152.850 137.322 186.840 1.00 46.57  ? 356  ALA B O     1 
ATOM   13697 C  CB    . ALA B 2  356  ? 155.419 135.454 187.545 1.00 48.08  ? 356  ALA B CB    1 
ATOM   13698 N  N     . VAL B 2  357  ? 152.695 136.490 188.923 1.00 46.85  ? 357  VAL B N     1 
ATOM   13699 C  CA    . VAL B 2  357  ? 151.233 136.519 188.913 1.00 49.37  ? 357  VAL B CA    1 
ATOM   13700 C  C     . VAL B 2  357  ? 150.728 137.951 188.775 1.00 50.87  ? 357  VAL B C     1 
ATOM   13701 O  O     . VAL B 2  357  ? 149.844 138.243 187.960 1.00 48.10  ? 357  VAL B O     1 
ATOM   13702 C  CB    . VAL B 2  357  ? 150.679 135.847 190.182 1.00 48.18  ? 357  VAL B CB    1 
ATOM   13703 C  CG1   . VAL B 2  357  ? 149.160 135.776 190.129 1.00 45.91  ? 357  VAL B CG1   1 
ATOM   13704 C  CG2   . VAL B 2  357  ? 151.284 134.461 190.354 1.00 46.21  ? 357  VAL B CG2   1 
ATOM   13705 N  N     . GLN B 2  358  ? 151.283 138.867 189.573 1.00 53.66  ? 358  GLN B N     1 
ATOM   13706 C  CA    . GLN B 2  358  ? 150.883 140.267 189.481 1.00 53.43  ? 358  GLN B CA    1 
ATOM   13707 C  C     . GLN B 2  358  ? 151.282 140.868 188.145 1.00 54.37  ? 358  GLN B C     1 
ATOM   13708 O  O     . GLN B 2  358  ? 150.540 141.674 187.574 1.00 55.19  ? 358  GLN B O     1 
ATOM   13709 C  CB    . GLN B 2  358  ? 151.494 141.072 190.625 1.00 53.13  ? 358  GLN B CB    1 
ATOM   13710 C  CG    . GLN B 2  358  ? 150.719 141.001 191.926 1.00 54.37  ? 358  GLN B CG    1 
ATOM   13711 C  CD    . GLN B 2  358  ? 151.362 141.834 193.011 1.00 56.80  ? 358  GLN B CD    1 
ATOM   13712 O  OE1   . GLN B 2  358  ? 152.471 142.342 192.838 1.00 57.10  ? 358  GLN B OE1   1 
ATOM   13713 N  NE2   . GLN B 2  358  ? 150.672 141.983 194.136 1.00 54.36  ? 358  GLN B NE2   1 
ATOM   13714 N  N     . TYR B 2  359  ? 152.464 140.507 187.641 1.00 54.88  ? 359  TYR B N     1 
ATOM   13715 C  CA    . TYR B 2  359  ? 152.891 140.991 186.333 1.00 54.61  ? 359  TYR B CA    1 
ATOM   13716 C  C     . TYR B 2  359  ? 151.902 140.572 185.252 1.00 56.56  ? 359  TYR B C     1 
ATOM   13717 O  O     . TYR B 2  359  ? 151.483 141.391 184.427 1.00 53.98  ? 359  TYR B O     1 
ATOM   13718 C  CB    . TYR B 2  359  ? 154.294 140.467 186.024 1.00 52.91  ? 359  TYR B CB    1 
ATOM   13719 C  CG    . TYR B 2  359  ? 154.856 140.890 184.684 1.00 55.88  ? 359  TYR B CG    1 
ATOM   13720 C  CD1   . TYR B 2  359  ? 155.273 142.196 184.462 1.00 55.09  ? 359  TYR B CD1   1 
ATOM   13721 C  CD2   . TYR B 2  359  ? 154.997 139.973 183.649 1.00 54.44  ? 359  TYR B CD2   1 
ATOM   13722 C  CE1   . TYR B 2  359  ? 155.798 142.583 183.240 1.00 54.60  ? 359  TYR B CE1   1 
ATOM   13723 C  CE2   . TYR B 2  359  ? 155.523 140.350 182.427 1.00 56.07  ? 359  TYR B CE2   1 
ATOM   13724 C  CZ    . TYR B 2  359  ? 155.922 141.657 182.228 1.00 56.57  ? 359  TYR B CZ    1 
ATOM   13725 O  OH    . TYR B 2  359  ? 156.442 142.037 181.013 1.00 54.83  ? 359  TYR B OH    1 
ATOM   13726 N  N     . LEU B 2  360  ? 151.497 139.301 185.264 1.00 53.42  ? 360  LEU B N     1 
ATOM   13727 C  CA    . LEU B 2  360  ? 150.538 138.810 184.281 1.00 54.19  ? 360  LEU B CA    1 
ATOM   13728 C  C     . LEU B 2  360  ? 149.179 139.483 184.442 1.00 54.63  ? 360  LEU B C     1 
ATOM   13729 O  O     . LEU B 2  360  ? 148.522 139.813 183.448 1.00 53.72  ? 360  LEU B O     1 
ATOM   13730 C  CB    . LEU B 2  360  ? 150.410 137.289 184.395 1.00 53.46  ? 360  LEU B CB    1 
ATOM   13731 C  CG    . LEU B 2  360  ? 151.666 136.476 184.064 1.00 53.08  ? 360  LEU B CG    1 
ATOM   13732 C  CD1   . LEU B 2  360  ? 151.499 135.022 184.465 1.00 52.67  ? 360  LEU B CD1   1 
ATOM   13733 C  CD2   . LEU B 2  360  ? 152.016 136.590 182.589 1.00 53.24  ? 360  LEU B CD2   1 
ATOM   13734 N  N     . ASN B 2  361  ? 148.735 139.684 185.686 1.00 52.82  ? 361  ASN B N     1 
ATOM   13735 C  CA    . ASN B 2  361  ? 147.450 140.339 185.919 1.00 52.15  ? 361  ASN B CA    1 
ATOM   13736 C  C     . ASN B 2  361  ? 147.456 141.772 185.394 1.00 52.63  ? 361  ASN B C     1 
ATOM   13737 O  O     . ASN B 2  361  ? 146.518 142.194 184.704 1.00 51.37  ? 361  ASN B O     1 
ATOM   13738 C  CB    . ASN B 2  361  ? 147.125 140.316 187.410 1.00 51.00  ? 361  ASN B CB    1 
ATOM   13739 C  CG    . ASN B 2  361  ? 146.663 138.956 187.887 1.00 55.07  ? 361  ASN B CG    1 
ATOM   13740 O  OD1   . ASN B 2  361  ? 145.830 138.310 187.253 1.00 53.84  ? 361  ASN B OD1   1 
ATOM   13741 N  ND2   . ASN B 2  361  ? 147.223 138.503 188.998 1.00 53.94  ? 361  ASN B ND2   1 
ATOM   13742 N  N     . GLU B 2  362  ? 148.518 142.527 185.694 1.00 50.55  ? 362  GLU B N     1 
ATOM   13743 C  CA    . GLU B 2  362  ? 148.653 143.876 185.155 1.00 51.35  ? 362  GLU B CA    1 
ATOM   13744 C  C     . GLU B 2  362  ? 148.714 143.864 183.637 1.00 53.58  ? 362  GLU B C     1 
ATOM   13745 O  O     . GLU B 2  362  ? 148.108 144.717 182.981 1.00 51.02  ? 362  GLU B O     1 
ATOM   13746 C  CB    . GLU B 2  362  ? 149.905 144.551 185.705 1.00 51.69  ? 362  GLU B CB    1 
ATOM   13747 C  CG    . GLU B 2  362  ? 150.033 146.007 185.275 1.00 52.43  ? 362  GLU B CG    1 
ATOM   13748 C  CD    . GLU B 2  362  ? 151.354 146.631 185.683 1.00 55.45  ? 362  GLU B CD    1 
ATOM   13749 O  OE1   . GLU B 2  362  ? 152.297 145.876 186.002 1.00 53.43  ? 362  GLU B OE1   1 
ATOM   13750 O  OE2   . GLU B 2  362  ? 151.451 147.876 185.671 1.00 56.59  ? 362  GLU B OE2   1 
ATOM   13751 N  N     . ARG B 2  363  ? 149.466 142.923 183.063 1.00 56.89  ? 363  ARG B N     1 
ATOM   13752 C  CA    . ARG B 2  363  ? 149.621 142.870 181.614 1.00 56.66  ? 363  ARG B CA    1 
ATOM   13753 C  C     . ARG B 2  363  ? 148.288 142.600 180.932 1.00 53.33  ? 363  ARG B C     1 
ATOM   13754 O  O     . ARG B 2  363  ? 147.936 143.258 179.947 1.00 51.39  ? 363  ARG B O     1 
ATOM   13755 C  CB    . ARG B 2  363  ? 150.650 141.800 181.247 1.00 55.57  ? 363  ARG B CB    1 
ATOM   13756 C  CG    . ARG B 2  363  ? 151.057 141.782 179.788 1.00 56.41  ? 363  ARG B CG    1 
ATOM   13757 C  CD    . ARG B 2  363  ? 150.366 140.650 179.062 1.00 55.76  ? 363  ARG B CD    1 
ATOM   13758 N  NE    . ARG B 2  363  ? 150.932 140.421 177.740 1.00 55.49  ? 363  ARG B NE    1 
ATOM   13759 C  CZ    . ARG B 2  363  ? 151.936 139.590 177.495 1.00 56.96  ? 363  ARG B CZ    1 
ATOM   13760 N  NH1   . ARG B 2  363  ? 152.504 138.889 178.463 1.00 53.41  ? 363  ARG B NH1   1 
ATOM   13761 N  NH2   . ARG B 2  363  ? 152.378 139.458 176.247 1.00 56.72  ? 363  ARG B NH2   1 
ATOM   13762 N  N     . GLN B 2  364  ? 147.527 141.633 181.445 1.00 50.03  ? 364  GLN B N     1 
ATOM   13763 C  CA    . GLN B 2  364  ? 146.222 141.345 180.862 1.00 53.64  ? 364  GLN B CA    1 
ATOM   13764 C  C     . GLN B 2  364  ? 145.262 142.510 181.043 1.00 52.45  ? 364  GLN B C     1 
ATOM   13765 O  O     . GLN B 2  364  ? 144.531 142.859 180.106 1.00 50.18  ? 364  GLN B O     1 
ATOM   13766 C  CB    . GLN B 2  364  ? 145.645 140.069 181.466 1.00 52.01  ? 364  GLN B CB    1 
ATOM   13767 C  CG    . GLN B 2  364  ? 145.886 138.843 180.613 1.00 52.25  ? 364  GLN B CG    1 
ATOM   13768 C  CD    . GLN B 2  364  ? 147.310 138.344 180.710 1.00 53.90  ? 364  GLN B CD    1 
ATOM   13769 O  OE1   . GLN B 2  364  ? 147.975 138.118 179.697 1.00 53.96  ? 364  GLN B OE1   1 
ATOM   13770 N  NE2   . GLN B 2  364  ? 147.792 138.179 181.934 1.00 53.32  ? 364  GLN B NE2   1 
ATOM   13771 N  N     . LEU B 2  365  ? 145.265 143.140 182.219 1.00 47.79  ? 365  LEU B N     1 
ATOM   13772 C  CA    . LEU B 2  365  ? 144.394 144.288 182.431 1.00 47.66  ? 365  LEU B CA    1 
ATOM   13773 C  C     . LEU B 2  365  ? 144.725 145.412 181.458 1.00 50.17  ? 365  LEU B C     1 
ATOM   13774 O  O     . LEU B 2  365  ? 143.828 145.975 180.827 1.00 52.56  ? 365  LEU B O     1 
ATOM   13775 C  CB    . LEU B 2  365  ? 144.511 144.769 183.874 1.00 47.47  ? 365  LEU B CB    1 
ATOM   13776 C  CG    . LEU B 2  365  ? 143.678 143.970 184.877 1.00 50.77  ? 365  LEU B CG    1 
ATOM   13777 C  CD1   . LEU B 2  365  ? 144.209 144.175 186.294 1.00 48.65  ? 365  LEU B CD1   1 
ATOM   13778 C  CD2   . LEU B 2  365  ? 142.199 144.315 184.778 1.00 49.42  ? 365  LEU B CD2   1 
ATOM   13779 N  N     . THR B 2  366  ? 146.012 145.725 181.284 1.00 46.63  ? 366  THR B N     1 
ATOM   13780 C  CA    . THR B 2  366  ? 146.371 146.847 180.423 1.00 47.68  ? 366  THR B CA    1 
ATOM   13781 C  C     . THR B 2  366  ? 146.152 146.516 178.951 1.00 48.66  ? 366  THR B C     1 
ATOM   13782 O  O     . THR B 2  366  ? 145.744 147.387 178.169 1.00 47.50  ? 366  THR B O     1 
ATOM   13783 C  CB    . THR B 2  366  ? 147.817 147.287 180.672 1.00 49.11  ? 366  THR B CB    1 
ATOM   13784 O  OG1   . THR B 2  366  ? 148.097 148.464 179.904 1.00 49.24  ? 366  THR B OG1   1 
ATOM   13785 C  CG2   . THR B 2  366  ? 148.807 146.206 180.279 1.00 47.77  ? 366  THR B CG2   1 
ATOM   13786 N  N     . ILE B 2  367  ? 146.394 145.267 178.546 1.00 46.49  ? 367  ILE B N     1 
ATOM   13787 C  CA    . ILE B 2  367  ? 146.211 144.922 177.142 1.00 48.56  ? 367  ILE B CA    1 
ATOM   13788 C  C     . ILE B 2  367  ? 144.729 144.935 176.787 1.00 49.87  ? 367  ILE B C     1 
ATOM   13789 O  O     . ILE B 2  367  ? 144.330 145.515 175.770 1.00 47.16  ? 367  ILE B O     1 
ATOM   13790 C  CB    . ILE B 2  367  ? 146.887 143.577 176.813 1.00 46.67  ? 367  ILE B CB    1 
ATOM   13791 C  CG1   . ILE B 2  367  ? 146.932 143.364 175.301 1.00 48.86  ? 367  ILE B CG1   1 
ATOM   13792 C  CG2   . ILE B 2  367  ? 146.181 142.407 177.469 1.00 44.77  ? 367  ILE B CG2   1 
ATOM   13793 C  CD1   . ILE B 2  367  ? 147.763 142.174 174.892 1.00 49.25  ? 367  ILE B CD1   1 
ATOM   13794 N  N     . LEU B 2  368  ? 143.879 144.348 177.640 1.00 51.00  ? 368  LEU B N     1 
ATOM   13795 C  CA    . LEU B 2  368  ? 142.448 144.435 177.392 1.00 49.03  ? 368  LEU B CA    1 
ATOM   13796 C  C     . LEU B 2  368  ? 141.913 145.840 177.604 1.00 48.33  ? 368  LEU B C     1 
ATOM   13797 O  O     . LEU B 2  368  ? 140.843 146.159 177.083 1.00 51.16  ? 368  LEU B O     1 
ATOM   13798 C  CB    . LEU B 2  368  ? 141.681 143.445 178.269 1.00 47.76  ? 368  LEU B CB    1 
ATOM   13799 C  CG    . LEU B 2  368  ? 141.287 142.147 177.559 1.00 47.86  ? 368  LEU B CG    1 
ATOM   13800 C  CD1   . LEU B 2  368  ? 142.471 141.200 177.496 1.00 46.98  ? 368  LEU B CD1   1 
ATOM   13801 C  CD2   . LEU B 2  368  ? 140.092 141.481 178.226 1.00 46.68  ? 368  LEU B CD2   1 
ATOM   13802 N  N     . ASP B 2  369  ? 142.627 146.686 178.342 1.00 44.09  ? 369  ASP B N     1 
ATOM   13803 C  CA    . ASP B 2  369  ? 142.237 148.084 178.410 1.00 46.20  ? 369  ASP B CA    1 
ATOM   13804 C  C     . ASP B 2  369  ? 142.695 148.835 177.170 1.00 48.31  ? 369  ASP B C     1 
ATOM   13805 O  O     . ASP B 2  369  ? 142.288 149.980 176.952 1.00 46.36  ? 369  ASP B O     1 
ATOM   13806 C  CB    . ASP B 2  369  ? 142.797 148.731 179.673 1.00 43.08  ? 369  ASP B CB    1 
ATOM   13807 C  CG    . ASP B 2  369  ? 141.868 149.773 180.248 1.00 45.86  ? 369  ASP B CG    1 
ATOM   13808 O  OD1   . ASP B 2  369  ? 141.506 150.720 179.526 1.00 45.60  ? 369  ASP B OD1   1 
ATOM   13809 O  OD2   . ASP B 2  369  ? 141.492 149.644 181.430 1.00 47.25  ? 369  ASP B OD2   1 
ATOM   13810 N  N     . LYS B 2  370  ? 143.559 148.222 176.359 1.00 45.33  ? 370  LYS B N     1 
ATOM   13811 C  CA    . LYS B 2  370  ? 143.835 148.756 175.034 1.00 46.64  ? 370  LYS B CA    1 
ATOM   13812 C  C     . LYS B 2  370  ? 143.175 147.984 173.901 1.00 45.88  ? 370  LYS B C     1 
ATOM   13813 O  O     . LYS B 2  370  ? 142.909 148.579 172.854 1.00 45.54  ? 370  LYS B O     1 
ATOM   13814 C  CB    . LYS B 2  370  ? 145.347 148.823 174.768 1.00 46.27  ? 370  LYS B CB    1 
ATOM   13815 C  CG    . LYS B 2  370  ? 145.726 149.964 173.828 1.00 44.49  ? 370  LYS B CG    1 
ATOM   13816 C  CD    . LYS B 2  370  ? 145.832 149.480 172.381 1.00 44.97  ? 370  LYS B CD    1 
ATOM   13817 C  CE    . LYS B 2  370  ? 146.086 150.617 171.399 1.00 44.93  ? 370  LYS B CE    1 
ATOM   13818 N  NZ    . LYS B 2  370  ? 144.991 151.623 171.385 1.00 47.38  ? 370  LYS B NZ    1 
ATOM   13819 N  N     . ILE B 2  371  ? 142.907 146.684 174.065 1.00 42.18  ? 371  ILE B N     1 
ATOM   13820 C  CA    . ILE B 2  371  ? 142.348 145.910 172.958 1.00 41.05  ? 371  ILE B CA    1 
ATOM   13821 C  C     . ILE B 2  371  ? 140.839 145.721 173.036 1.00 42.40  ? 371  ILE B C     1 
ATOM   13822 O  O     . ILE B 2  371  ? 140.267 145.069 172.150 1.00 44.41  ? 371  ILE B O     1 
ATOM   13823 C  CB    . ILE B 2  371  ? 142.989 144.516 172.828 1.00 40.55  ? 371  ILE B CB    1 
ATOM   13824 C  CG1   . ILE B 2  371  ? 142.540 143.613 173.975 1.00 41.61  ? 371  ILE B CG1   1 
ATOM   13825 C  CG2   . ILE B 2  371  ? 144.498 144.630 172.744 1.00 41.44  ? 371  ILE B CG2   1 
ATOM   13826 C  CD1   . ILE B 2  371  ? 142.282 142.193 173.568 1.00 41.10  ? 371  ILE B CD1   1 
ATOM   13827 N  N     . LEU B 2  372  ? 140.173 146.243 174.061 1.00 40.40  ? 372  LEU B N     1 
ATOM   13828 C  CA    . LEU B 2  372  ? 138.716 146.248 174.108 1.00 39.46  ? 372  LEU B CA    1 
ATOM   13829 C  C     . LEU B 2  372  ? 138.222 147.684 173.998 1.00 43.94  ? 372  LEU B C     1 
ATOM   13830 O  O     . LEU B 2  372  ? 138.453 148.490 174.906 1.00 42.09  ? 372  LEU B O     1 
ATOM   13831 C  CB    . LEU B 2  372  ? 138.179 145.609 175.387 1.00 36.50  ? 372  LEU B CB    1 
ATOM   13832 C  CG    . LEU B 2  372  ? 136.677 145.338 175.262 1.00 36.60  ? 372  LEU B CG    1 
ATOM   13833 C  CD1   . LEU B 2  372  ? 136.420 144.062 174.470 1.00 37.02  ? 372  LEU B CD1   1 
ATOM   13834 C  CD2   . LEU B 2  372  ? 135.982 145.300 176.598 1.00 36.30  ? 372  LEU B CD2   1 
ATOM   13835 N  N     . LEU B 2  373  ? 137.530 147.982 172.901 1.00 35.08  ? 373  LEU B N     1 
ATOM   13836 C  CA    . LEU B 2  373  ? 136.993 149.308 172.615 1.00 30.67  ? 373  LEU B CA    1 
ATOM   13837 C  C     . LEU B 2  373  ? 138.003 150.438 172.839 1.00 32.35  ? 373  LEU B C     1 
ATOM   13838 O  O     . LEU B 2  373  ? 137.764 151.335 173.652 1.00 30.74  ? 373  LEU B O     1 
ATOM   13839 C  CB    . LEU B 2  373  ? 135.732 149.559 173.429 1.00 30.33  ? 373  LEU B CB    1 
ATOM   13840 C  CG    . LEU B 2  373  ? 134.697 148.444 173.541 1.00 34.52  ? 373  LEU B CG    1 
ATOM   13841 C  CD1   . LEU B 2  373  ? 133.450 148.969 174.230 1.00 33.30  ? 373  LEU B CD1   1 
ATOM   13842 C  CD2   . LEU B 2  373  ? 134.362 147.860 172.179 1.00 32.78  ? 373  LEU B CD2   1 
ATOM   13843 N  N     . PRO B 2  374  ? 139.126 150.437 172.117 1.00 35.00  ? 374  PRO B N     1 
ATOM   13844 C  CA    . PRO B 2  374  ? 140.110 151.513 172.308 1.00 35.84  ? 374  PRO B CA    1 
ATOM   13845 C  C     . PRO B 2  374  ? 139.566 152.905 172.055 1.00 36.40  ? 374  PRO B C     1 
ATOM   13846 O  O     . PRO B 2  374  ? 140.110 153.866 172.609 1.00 38.11  ? 374  PRO B O     1 
ATOM   13847 C  CB    . PRO B 2  374  ? 141.219 151.166 171.302 1.00 35.52  ? 374  PRO B CB    1 
ATOM   13848 C  CG    . PRO B 2  374  ? 140.714 150.031 170.494 1.00 34.73  ? 374  PRO B CG    1 
ATOM   13849 C  CD    . PRO B 2  374  ? 139.660 149.357 171.278 1.00 35.00  ? 374  PRO B CD    1 
ATOM   13850 N  N     . HIS B 2  375  ? 138.523 153.055 171.234 1.00 40.00  ? 375  HIS B N     1 
ATOM   13851 C  CA    . HIS B 2  375  ? 138.032 154.382 170.879 1.00 38.02  ? 375  HIS B CA    1 
ATOM   13852 C  C     . HIS B 2  375  ? 137.432 155.131 172.058 1.00 38.56  ? 375  HIS B C     1 
ATOM   13853 O  O     . HIS B 2  375  ? 137.231 156.344 171.957 1.00 37.41  ? 375  HIS B O     1 
ATOM   13854 C  CB    . HIS B 2  375  ? 136.999 154.292 169.758 1.00 36.46  ? 375  HIS B CB    1 
ATOM   13855 C  CG    . HIS B 2  375  ? 135.656 153.805 170.203 1.00 38.55  ? 375  HIS B CG    1 
ATOM   13856 N  ND1   . HIS B 2  375  ? 135.389 152.478 170.452 1.00 37.38  ? 375  HIS B ND1   1 
ATOM   13857 C  CD2   . HIS B 2  375  ? 134.504 154.473 170.449 1.00 37.67  ? 375  HIS B CD2   1 
ATOM   13858 C  CE1   . HIS B 2  375  ? 134.131 152.349 170.832 1.00 38.33  ? 375  HIS B CE1   1 
ATOM   13859 N  NE2   . HIS B 2  375  ? 133.572 153.546 170.840 1.00 35.56  ? 375  HIS B NE2   1 
ATOM   13860 N  N     . MET B 2  376  ? 137.128 154.447 173.157 1.00 45.44  ? 376  MET B N     1 
ATOM   13861 C  CA    . MET B 2  376  ? 136.566 155.092 174.332 1.00 46.90  ? 376  MET B CA    1 
ATOM   13862 C  C     . MET B 2  376  ? 137.615 155.496 175.358 1.00 46.93  ? 376  MET B C     1 
ATOM   13863 O  O     . MET B 2  376  ? 137.273 156.168 176.337 1.00 44.47  ? 376  MET B O     1 
ATOM   13864 C  CB    . MET B 2  376  ? 135.541 154.168 174.989 1.00 41.81  ? 376  MET B CB    1 
ATOM   13865 C  CG    . MET B 2  376  ? 134.222 154.123 174.267 1.00 42.74  ? 376  MET B CG    1 
ATOM   13866 S  SD    . MET B 2  376  ? 133.052 153.014 175.056 1.00 54.86  ? 376  MET B SD    1 
ATOM   13867 C  CE    . MET B 2  376  ? 131.752 154.178 175.448 1.00 44.19  ? 376  MET B CE    1 
ATOM   13868 N  N     . GLY B 2  377  ? 138.873 155.119 175.152 1.00 42.11  ? 377  GLY B N     1 
ATOM   13869 C  CA    . GLY B 2  377  ? 139.927 155.373 176.115 1.00 39.74  ? 377  GLY B CA    1 
ATOM   13870 C  C     . GLY B 2  377  ? 140.708 154.113 176.428 1.00 43.15  ? 377  GLY B C     1 
ATOM   13871 O  O     . GLY B 2  377  ? 140.212 153.006 176.212 1.00 42.29  ? 377  GLY B O     1 
ATOM   13872 N  N     . GLN B 2  378  ? 141.924 154.260 176.951 1.00 45.89  ? 378  GLN B N     1 
ATOM   13873 C  CA    . GLN B 2  378  ? 142.763 153.096 177.204 1.00 45.34  ? 378  GLN B CA    1 
ATOM   13874 C  C     . GLN B 2  378  ? 143.226 152.999 178.653 1.00 45.73  ? 378  GLN B C     1 
ATOM   13875 O  O     . GLN B 2  378  ? 144.106 152.182 178.950 1.00 49.11  ? 378  GLN B O     1 
ATOM   13876 C  CB    . GLN B 2  378  ? 143.977 153.106 176.276 1.00 45.97  ? 378  GLN B CB    1 
ATOM   13877 C  CG    . GLN B 2  378  ? 144.844 154.344 176.420 1.00 45.79  ? 378  GLN B CG    1 
ATOM   13878 C  CD    . GLN B 2  378  ? 144.400 155.475 175.517 1.00 47.63  ? 378  GLN B CD    1 
ATOM   13879 O  OE1   . GLN B 2  378  ? 143.255 155.509 175.062 1.00 44.39  ? 378  GLN B OE1   1 
ATOM   13880 N  NE2   . GLN B 2  378  ? 145.308 156.407 175.249 1.00 47.56  ? 378  GLN B NE2   1 
ATOM   13881 N  N     . THR B 2  379  ? 142.664 153.785 179.561 1.00 41.79  ? 379  THR B N     1 
ATOM   13882 C  CA    . THR B 2  379  ? 143.031 153.735 180.967 1.00 42.54  ? 379  THR B CA    1 
ATOM   13883 C  C     . THR B 2  379  ? 141.925 153.052 181.761 1.00 43.91  ? 379  THR B C     1 
ATOM   13884 O  O     . THR B 2  379  ? 140.824 152.809 181.259 1.00 42.52  ? 379  THR B O     1 
ATOM   13885 C  CB    . THR B 2  379  ? 143.297 155.141 181.516 1.00 44.50  ? 379  THR B CB    1 
ATOM   13886 O  OG1   . THR B 2  379  ? 142.099 155.921 181.431 1.00 45.53  ? 379  THR B OG1   1 
ATOM   13887 C  CG2   . THR B 2  379  ? 144.392 155.823 180.709 1.00 40.00  ? 379  THR B CG2   1 
ATOM   13888 N  N     . ALA B 2  380  ? 142.232 152.748 183.024 1.00 41.83  ? 380  ALA B N     1 
ATOM   13889 C  CA    . ALA B 2  380  ? 141.329 151.939 183.836 1.00 43.57  ? 380  ALA B CA    1 
ATOM   13890 C  C     . ALA B 2  380  ? 140.063 152.692 184.229 1.00 42.39  ? 380  ALA B C     1 
ATOM   13891 O  O     . ALA B 2  380  ? 139.060 152.061 184.578 1.00 40.69  ? 380  ALA B O     1 
ATOM   13892 C  CB    . ALA B 2  380  ? 142.052 151.442 185.088 1.00 41.07  ? 380  ALA B CB    1 
ATOM   13893 N  N     . ASP B 2  381  ? 140.087 154.026 184.213 1.00 46.64  ? 381  ASP B N     1 
ATOM   13894 C  CA    . ASP B 2  381  ? 138.894 154.772 184.601 1.00 47.61  ? 381  ASP B CA    1 
ATOM   13895 C  C     . ASP B 2  381  ? 137.813 154.739 183.529 1.00 50.10  ? 381  ASP B C     1 
ATOM   13896 O  O     . ASP B 2  381  ? 136.657 155.066 183.818 1.00 50.92  ? 381  ASP B O     1 
ATOM   13897 C  CB    . ASP B 2  381  ? 139.256 156.215 184.951 1.00 46.50  ? 381  ASP B CB    1 
ATOM   13898 C  CG    . ASP B 2  381  ? 140.148 156.855 183.924 1.00 50.92  ? 381  ASP B CG    1 
ATOM   13899 O  OD1   . ASP B 2  381  ? 140.793 156.113 183.155 1.00 49.38  ? 381  ASP B OD1   1 
ATOM   13900 O  OD2   . ASP B 2  381  ? 140.205 158.102 183.886 1.00 51.42  ? 381  ASP B OD2   1 
ATOM   13901 N  N     . THR B 2  382  ? 138.152 154.355 182.305 1.00 47.79  ? 382  THR B N     1 
ATOM   13902 C  CA    . THR B 2  382  ? 137.165 154.212 181.247 1.00 48.21  ? 382  THR B CA    1 
ATOM   13903 C  C     . THR B 2  382  ? 136.698 152.776 181.066 1.00 48.69  ? 382  THR B C     1 
ATOM   13904 O  O     . THR B 2  382  ? 136.363 152.390 179.942 1.00 49.49  ? 382  THR B O     1 
ATOM   13905 C  CB    . THR B 2  382  ? 137.721 154.738 179.922 1.00 50.49  ? 382  THR B CB    1 
ATOM   13906 O  OG1   . THR B 2  382  ? 138.797 153.899 179.488 1.00 48.33  ? 382  THR B OG1   1 
ATOM   13907 C  CG2   . THR B 2  382  ? 138.223 156.160 180.086 1.00 47.61  ? 382  THR B CG2   1 
ATOM   13908 N  N     . ARG B 2  383  ? 136.706 151.965 182.127 1.00 49.23  ? 383  ARG B N     1 
ATOM   13909 C  CA    . ARG B 2  383  ? 136.294 150.572 181.986 1.00 48.31  ? 383  ARG B CA    1 
ATOM   13910 C  C     . ARG B 2  383  ? 134.791 150.405 182.188 1.00 47.14  ? 383  ARG B C     1 
ATOM   13911 O  O     . ARG B 2  383  ? 134.165 149.547 181.553 1.00 50.21  ? 383  ARG B O     1 
ATOM   13912 C  CB    . ARG B 2  383  ? 137.090 149.693 182.950 1.00 47.26  ? 383  ARG B CB    1 
ATOM   13913 C  CG    . ARG B 2  383  ? 136.911 148.209 182.693 1.00 48.73  ? 383  ARG B CG    1 
ATOM   13914 C  CD    . ARG B 2  383  ? 138.047 147.382 183.269 1.00 50.32  ? 383  ARG B CD    1 
ATOM   13915 N  NE    . ARG B 2  383  ? 138.060 147.361 184.725 1.00 52.92  ? 383  ARG B NE    1 
ATOM   13916 C  CZ    . ARG B 2  383  ? 139.132 147.606 185.465 1.00 51.65  ? 383  ARG B CZ    1 
ATOM   13917 N  NH1   . ARG B 2  383  ? 140.303 147.882 184.915 1.00 50.55  ? 383  ARG B NH1   1 
ATOM   13918 N  NH2   . ARG B 2  383  ? 139.030 147.563 186.790 1.00 48.51  ? 383  ARG B NH2   1 
ATOM   13919 N  N     . VAL B 2  384  ? 134.190 151.223 183.051 1.00 41.72  ? 384  VAL B N     1 
ATOM   13920 C  CA    . VAL B 2  384  ? 132.751 151.124 183.283 1.00 42.18  ? 384  VAL B CA    1 
ATOM   13921 C  C     . VAL B 2  384  ? 131.978 151.595 182.058 1.00 46.48  ? 384  VAL B C     1 
ATOM   13922 O  O     . VAL B 2  384  ? 130.974 150.988 181.660 1.00 45.25  ? 384  VAL B O     1 
ATOM   13923 C  CB    . VAL B 2  384  ? 132.354 151.913 184.542 1.00 40.85  ? 384  VAL B CB    1 
ATOM   13924 C  CG1   . VAL B 2  384  ? 130.843 151.989 184.670 1.00 37.96  ? 384  VAL B CG1   1 
ATOM   13925 C  CG2   . VAL B 2  384  ? 132.950 151.256 185.765 1.00 43.82  ? 384  VAL B CG2   1 
ATOM   13926 N  N     . ARG B 2  385  ? 132.421 152.695 181.445 1.00 48.01  ? 385  ARG B N     1 
ATOM   13927 C  CA    . ARG B 2  385  ? 131.766 153.118 180.217 1.00 46.14  ? 385  ARG B CA    1 
ATOM   13928 C  C     . ARG B 2  385  ? 131.977 152.116 179.095 1.00 45.28  ? 385  ARG B C     1 
ATOM   13929 O  O     . ARG B 2  385  ? 131.084 151.954 178.259 1.00 51.33  ? 385  ARG B O     1 
ATOM   13930 C  CB    . ARG B 2  385  ? 132.235 154.511 179.786 1.00 44.16  ? 385  ARG B CB    1 
ATOM   13931 C  CG    . ARG B 2  385  ? 133.719 154.673 179.607 1.00 48.02  ? 385  ARG B CG    1 
ATOM   13932 C  CD    . ARG B 2  385  ? 134.063 156.138 179.409 1.00 45.81  ? 385  ARG B CD    1 
ATOM   13933 N  NE    . ARG B 2  385  ? 133.569 156.953 180.511 1.00 48.28  ? 385  ARG B NE    1 
ATOM   13934 C  CZ    . ARG B 2  385  ? 133.614 158.278 180.545 1.00 48.00  ? 385  ARG B CZ    1 
ATOM   13935 N  NH1   . ARG B 2  385  ? 134.169 158.975 179.569 1.00 46.41  ? 385  ARG B NH1   1 
ATOM   13936 N  NH2   . ARG B 2  385  ? 133.091 158.917 181.586 1.00 46.01  ? 385  ARG B NH2   1 
ATOM   13937 N  N     . LYS B 2  386  ? 133.116 151.422 179.068 1.00 33.16  ? 386  LYS B N     1 
ATOM   13938 C  CA    . LYS B 2  386  ? 133.266 150.325 178.120 1.00 36.01  ? 386  LYS B CA    1 
ATOM   13939 C  C     . LYS B 2  386  ? 132.224 149.250 178.371 1.00 37.52  ? 386  LYS B C     1 
ATOM   13940 O  O     . LYS B 2  386  ? 131.652 148.691 177.427 1.00 41.33  ? 386  LYS B O     1 
ATOM   13941 C  CB    . LYS B 2  386  ? 134.669 149.732 178.198 1.00 37.26  ? 386  LYS B CB    1 
ATOM   13942 C  CG    . LYS B 2  386  ? 135.703 150.535 177.457 1.00 39.68  ? 386  LYS B CG    1 
ATOM   13943 C  CD    . LYS B 2  386  ? 137.085 149.951 177.620 1.00 38.79  ? 386  LYS B CD    1 
ATOM   13944 C  CE    . LYS B 2  386  ? 138.126 150.919 177.098 1.00 37.30  ? 386  LYS B CE    1 
ATOM   13945 N  NZ    . LYS B 2  386  ? 139.516 150.473 177.354 1.00 37.38  ? 386  LYS B NZ    1 
ATOM   13946 N  N     . LEU B 2  387  ? 131.967 148.944 179.642 1.00 41.17  ? 387  LEU B N     1 
ATOM   13947 C  CA    . LEU B 2  387  ? 130.966 147.937 179.972 1.00 42.49  ? 387  LEU B CA    1 
ATOM   13948 C  C     . LEU B 2  387  ? 129.580 148.365 179.502 1.00 42.84  ? 387  LEU B C     1 
ATOM   13949 O  O     . LEU B 2  387  ? 128.825 147.562 178.939 1.00 44.35  ? 387  LEU B O     1 
ATOM   13950 C  CB    . LEU B 2  387  ? 130.982 147.681 181.477 1.00 41.49  ? 387  LEU B CB    1 
ATOM   13951 C  CG    . LEU B 2  387  ? 132.249 146.975 181.958 1.00 41.32  ? 387  LEU B CG    1 
ATOM   13952 C  CD1   . LEU B 2  387  ? 132.266 146.889 183.470 1.00 43.38  ? 387  LEU B CD1   1 
ATOM   13953 C  CD2   . LEU B 2  387  ? 132.382 145.601 181.327 1.00 41.37  ? 387  LEU B CD2   1 
ATOM   13954 N  N     . ARG B 2  388  ? 129.227 149.634 179.727 1.00 39.69  ? 388  ARG B N     1 
ATOM   13955 C  CA    . ARG B 2  388  ? 127.925 150.128 179.278 1.00 40.94  ? 388  ARG B CA    1 
ATOM   13956 C  C     . ARG B 2  388  ? 127.810 150.089 177.759 1.00 42.10  ? 388  ARG B C     1 
ATOM   13957 O  O     . ARG B 2  388  ? 126.762 149.714 177.215 1.00 41.12  ? 388  ARG B O     1 
ATOM   13958 C  CB    . ARG B 2  388  ? 127.671 151.546 179.785 1.00 39.49  ? 388  ARG B CB    1 
ATOM   13959 C  CG    . ARG B 2  388  ? 127.566 151.670 181.286 1.00 41.17  ? 388  ARG B CG    1 
ATOM   13960 C  CD    . ARG B 2  388  ? 127.265 153.096 181.705 1.00 38.47  ? 388  ARG B CD    1 
ATOM   13961 N  NE    . ARG B 2  388  ? 125.857 153.425 181.529 1.00 39.27  ? 388  ARG B NE    1 
ATOM   13962 C  CZ    . ARG B 2  388  ? 125.306 154.580 181.873 1.00 41.36  ? 388  ARG B CZ    1 
ATOM   13963 N  NH1   . ARG B 2  388  ? 126.017 155.551 182.419 1.00 40.36  ? 388  ARG B NH1   1 
ATOM   13964 N  NH2   . ARG B 2  388  ? 124.006 154.765 181.669 1.00 37.72  ? 388  ARG B NH2   1 
ATOM   13965 N  N     . PHE B 2  389  ? 128.873 150.480 177.053 1.00 38.00  ? 389  PHE B N     1 
ATOM   13966 C  CA    . PHE B 2  389  ? 128.831 150.435 175.597 1.00 35.51  ? 389  PHE B CA    1 
ATOM   13967 C  C     . PHE B 2  389  ? 128.664 149.010 175.089 1.00 35.50  ? 389  PHE B C     1 
ATOM   13968 O  O     . PHE B 2  389  ? 127.894 148.772 174.153 1.00 41.48  ? 389  PHE B O     1 
ATOM   13969 C  CB    . PHE B 2  389  ? 130.083 151.070 175.006 1.00 33.77  ? 389  PHE B CB    1 
ATOM   13970 C  CG    . PHE B 2  389  ? 129.989 151.316 173.533 1.00 36.71  ? 389  PHE B CG    1 
ATOM   13971 C  CD1   . PHE B 2  389  ? 129.151 152.293 173.036 1.00 37.25  ? 389  PHE B CD1   1 
ATOM   13972 C  CD2   . PHE B 2  389  ? 130.725 150.561 172.644 1.00 38.35  ? 389  PHE B CD2   1 
ATOM   13973 C  CE1   . PHE B 2  389  ? 129.057 152.512 171.690 1.00 37.27  ? 389  PHE B CE1   1 
ATOM   13974 C  CE2   . PHE B 2  389  ? 130.634 150.779 171.298 1.00 36.64  ? 389  PHE B CE2   1 
ATOM   13975 C  CZ    . PHE B 2  389  ? 129.800 151.755 170.819 1.00 35.17  ? 389  PHE B CZ    1 
ATOM   13976 N  N     . LEU B 2  390  ? 129.373 148.049 175.687 1.00 35.34  ? 390  LEU B N     1 
ATOM   13977 C  CA    . LEU B 2  390  ? 129.208 146.656 175.277 1.00 37.28  ? 390  LEU B CA    1 
ATOM   13978 C  C     . LEU B 2  390  ? 127.794 146.160 175.559 1.00 38.66  ? 390  LEU B C     1 
ATOM   13979 O  O     . LEU B 2  390  ? 127.223 145.396 174.765 1.00 37.52  ? 390  LEU B O     1 
ATOM   13980 C  CB    . LEU B 2  390  ? 130.244 145.773 175.969 1.00 37.90  ? 390  LEU B CB    1 
ATOM   13981 C  CG    . LEU B 2  390  ? 131.019 144.822 175.050 1.00 40.38  ? 390  LEU B CG    1 
ATOM   13982 C  CD1   . LEU B 2  390  ? 131.573 145.542 173.833 1.00 36.30  ? 390  LEU B CD1   1 
ATOM   13983 C  CD2   . LEU B 2  390  ? 132.136 144.129 175.814 1.00 38.32  ? 390  LEU B CD2   1 
ATOM   13984 N  N     . GLY B 2  391  ? 127.211 146.587 176.679 1.00 39.16  ? 391  GLY B N     1 
ATOM   13985 C  CA    . GLY B 2  391  ? 125.833 146.224 176.954 1.00 38.17  ? 391  GLY B CA    1 
ATOM   13986 C  C     . GLY B 2  391  ? 124.877 146.750 175.902 1.00 39.27  ? 391  GLY B C     1 
ATOM   13987 O  O     . GLY B 2  391  ? 123.991 146.029 175.435 1.00 41.11  ? 391  GLY B O     1 
ATOM   13988 N  N     . LEU B 2  392  ? 125.056 148.010 175.501 1.00 39.33  ? 392  LEU B N     1 
ATOM   13989 C  CA    . LEU B 2  392  ? 124.192 148.593 174.477 1.00 36.61  ? 392  LEU B CA    1 
ATOM   13990 C  C     . LEU B 2  392  ? 124.376 147.899 173.129 1.00 35.43  ? 392  LEU B C     1 
ATOM   13991 O  O     . LEU B 2  392  ? 123.402 147.686 172.394 1.00 39.87  ? 392  LEU B O     1 
ATOM   13992 C  CB    . LEU B 2  392  ? 124.458 150.092 174.369 1.00 34.70  ? 392  LEU B CB    1 
ATOM   13993 C  CG    . LEU B 2  392  ? 123.840 150.866 173.211 1.00 37.63  ? 392  LEU B CG    1 
ATOM   13994 C  CD1   . LEU B 2  392  ? 122.337 150.842 173.322 1.00 34.96  ? 392  LEU B CD1   1 
ATOM   13995 C  CD2   . LEU B 2  392  ? 124.342 152.295 173.224 1.00 37.38  ? 392  LEU B CD2   1 
ATOM   13996 N  N     . LEU B 2  393  ? 125.613 147.529 172.790 1.00 28.50  ? 393  LEU B N     1 
ATOM   13997 C  CA    . LEU B 2  393  ? 125.838 146.788 171.551 1.00 27.35  ? 393  LEU B CA    1 
ATOM   13998 C  C     . LEU B 2  393  ? 125.096 145.459 171.557 1.00 35.86  ? 393  LEU B C     1 
ATOM   13999 O  O     . LEU B 2  393  ? 124.399 145.127 170.589 1.00 36.85  ? 393  LEU B O     1 
ATOM   14000 C  CB    . LEU B 2  393  ? 127.331 146.556 171.327 1.00 26.54  ? 393  LEU B CB    1 
ATOM   14001 C  CG    . LEU B 2  393  ? 128.252 147.773 171.267 1.00 33.53  ? 393  LEU B CG    1 
ATOM   14002 C  CD1   . LEU B 2  393  ? 129.640 147.353 170.835 1.00 31.66  ? 393  LEU B CD1   1 
ATOM   14003 C  CD2   . LEU B 2  393  ? 127.693 148.832 170.335 1.00 35.25  ? 393  LEU B CD2   1 
ATOM   14004 N  N     . ILE B 2  394  ? 125.222 144.689 172.643 1.00 39.15  ? 394  ILE B N     1 
ATOM   14005 C  CA    . ILE B 2  394  ? 124.523 143.407 172.721 1.00 34.13  ? 394  ILE B CA    1 
ATOM   14006 C  C     . ILE B 2  394  ? 123.016 143.621 172.658 1.00 35.48  ? 394  ILE B C     1 
ATOM   14007 O  O     . ILE B 2  394  ? 122.279 142.823 172.060 1.00 35.06  ? 394  ILE B O     1 
ATOM   14008 C  CB    . ILE B 2  394  ? 124.940 142.639 173.987 1.00 37.87  ? 394  ILE B CB    1 
ATOM   14009 C  CG1   . ILE B 2  394  ? 126.409 142.223 173.899 1.00 38.67  ? 394  ILE B CG1   1 
ATOM   14010 C  CG2   . ILE B 2  394  ? 124.067 141.415 174.191 1.00 38.58  ? 394  ILE B CG2   1 
ATOM   14011 C  CD1   . ILE B 2  394  ? 126.925 141.551 175.143 1.00 37.28  ? 394  ILE B CD1   1 
ATOM   14012 N  N     . HIS B 2  395  ? 122.536 144.707 173.265 1.00 38.02  ? 395  HIS B N     1 
ATOM   14013 C  CA    . HIS B 2  395  ? 121.122 145.047 173.179 1.00 36.70  ? 395  HIS B CA    1 
ATOM   14014 C  C     . HIS B 2  395  ? 120.684 145.221 171.728 1.00 40.00  ? 395  HIS B C     1 
ATOM   14015 O  O     . HIS B 2  395  ? 119.622 144.733 171.323 1.00 41.25  ? 395  HIS B O     1 
ATOM   14016 C  CB    . HIS B 2  395  ? 120.862 146.316 173.984 1.00 36.07  ? 395  HIS B CB    1 
ATOM   14017 C  CG    . HIS B 2  395  ? 119.454 146.805 173.906 1.00 39.00  ? 395  HIS B CG    1 
ATOM   14018 N  ND1   . HIS B 2  395  ? 118.451 146.314 174.711 1.00 41.36  ? 395  HIS B ND1   1 
ATOM   14019 C  CD2   . HIS B 2  395  ? 118.882 147.751 173.126 1.00 39.00  ? 395  HIS B CD2   1 
ATOM   14020 C  CE1   . HIS B 2  395  ? 117.321 146.932 174.426 1.00 41.53  ? 395  HIS B CE1   1 
ATOM   14021 N  NE2   . HIS B 2  395  ? 117.554 147.808 173.466 1.00 40.37  ? 395  HIS B NE2   1 
ATOM   14022 N  N     . LYS B 2  396  ? 121.499 145.912 170.927 1.00 38.90  ? 396  LYS B N     1 
ATOM   14023 C  CA    . LYS B 2  396  ? 121.169 146.085 169.512 1.00 36.03  ? 396  LYS B CA    1 
ATOM   14024 C  C     . LYS B 2  396  ? 121.156 144.752 168.771 1.00 35.30  ? 396  LYS B C     1 
ATOM   14025 O  O     . LYS B 2  396  ? 120.252 144.489 167.961 1.00 33.56  ? 396  LYS B O     1 
ATOM   14026 C  CB    . LYS B 2  396  ? 122.162 147.036 168.853 1.00 35.12  ? 396  LYS B CB    1 
ATOM   14027 C  CG    . LYS B 2  396  ? 122.123 148.444 169.379 1.00 33.43  ? 396  LYS B CG    1 
ATOM   14028 C  CD    . LYS B 2  396  ? 123.000 149.347 168.550 1.00 35.22  ? 396  LYS B CD    1 
ATOM   14029 C  CE    . LYS B 2  396  ? 123.113 150.716 169.189 1.00 37.80  ? 396  LYS B CE    1 
ATOM   14030 N  NZ    . LYS B 2  396  ? 121.790 151.379 169.326 1.00 37.95  ? 396  LYS B NZ    1 
ATOM   14031 N  N     . ILE B 2  397  ? 122.160 143.906 169.015 1.00 33.77  ? 397  ILE B N     1 
ATOM   14032 C  CA    . ILE B 2  397  ? 122.192 142.613 168.331 1.00 35.47  ? 397  ILE B CA    1 
ATOM   14033 C  C     . ILE B 2  397  ? 120.931 141.817 168.643 1.00 36.26  ? 397  ILE B C     1 
ATOM   14034 O  O     . ILE B 2  397  ? 120.290 141.246 167.746 1.00 36.67  ? 397  ILE B O     1 
ATOM   14035 C  CB    . ILE B 2  397  ? 123.461 141.815 168.693 1.00 34.18  ? 397  ILE B CB    1 
ATOM   14036 C  CG1   . ILE B 2  397  ? 124.720 142.439 168.092 1.00 32.69  ? 397  ILE B CG1   1 
ATOM   14037 C  CG2   . ILE B 2  397  ? 123.341 140.389 168.232 1.00 31.76  ? 397  ILE B CG2   1 
ATOM   14038 C  CD1   . ILE B 2  397  ? 125.701 142.949 169.085 1.00 31.14  ? 397  ILE B CD1   1 
ATOM   14039 N  N     . LEU B 2  398  ? 120.536 141.791 169.914 1.00 39.74  ? 398  LEU B N     1 
ATOM   14040 C  CA    . LEU B 2  398  ? 119.354 141.033 170.299 1.00 39.85  ? 398  LEU B CA    1 
ATOM   14041 C  C     . LEU B 2  398  ? 118.074 141.668 169.768 1.00 41.34  ? 398  LEU B C     1 
ATOM   14042 O  O     . LEU B 2  398  ? 117.082 140.966 169.550 1.00 42.01  ? 398  LEU B O     1 
ATOM   14043 C  CB    . LEU B 2  398  ? 119.314 140.893 171.816 1.00 40.71  ? 398  LEU B CB    1 
ATOM   14044 C  CG    . LEU B 2  398  ? 119.036 139.483 172.316 1.00 38.93  ? 398  LEU B CG    1 
ATOM   14045 C  CD1   . LEU B 2  398  ? 120.092 138.538 171.791 1.00 39.68  ? 398  LEU B CD1   1 
ATOM   14046 C  CD2   . LEU B 2  398  ? 119.069 139.498 173.816 1.00 39.37  ? 398  LEU B CD2   1 
ATOM   14047 N  N     . LEU B 2  399  ? 118.068 142.986 169.559 1.00 38.42  ? 399  LEU B N     1 
ATOM   14048 C  CA    . LEU B 2  399  ? 116.932 143.611 168.887 1.00 36.78  ? 399  LEU B CA    1 
ATOM   14049 C  C     . LEU B 2  399  ? 116.805 143.142 167.448 1.00 39.19  ? 399  LEU B C     1 
ATOM   14050 O  O     . LEU B 2  399  ? 115.692 142.949 166.951 1.00 35.90  ? 399  LEU B O     1 
ATOM   14051 C  CB    . LEU B 2  399  ? 117.065 145.126 168.920 1.00 37.16  ? 399  LEU B CB    1 
ATOM   14052 C  CG    . LEU B 2  399  ? 115.783 145.879 169.227 1.00 36.22  ? 399  LEU B CG    1 
ATOM   14053 C  CD1   . LEU B 2  399  ? 114.980 145.134 170.276 1.00 35.31  ? 399  LEU B CD1   1 
ATOM   14054 C  CD2   . LEU B 2  399  ? 116.128 147.277 169.690 1.00 37.45  ? 399  LEU B CD2   1 
ATOM   14055 N  N     . VAL B 2  400  ? 117.929 142.987 166.754 1.00 43.07  ? 400  VAL B N     1 
ATOM   14056 C  CA    . VAL B 2  400  ? 117.854 142.406 165.418 1.00 39.88  ? 400  VAL B CA    1 
ATOM   14057 C  C     . VAL B 2  400  ? 117.357 140.965 165.487 1.00 39.63  ? 400  VAL B C     1 
ATOM   14058 O  O     . VAL B 2  400  ? 116.621 140.517 164.600 1.00 39.36  ? 400  VAL B O     1 
ATOM   14059 C  CB    . VAL B 2  400  ? 119.206 142.515 164.700 1.00 38.37  ? 400  VAL B CB    1 
ATOM   14060 C  CG1   . VAL B 2  400  ? 119.208 141.691 163.428 1.00 36.35  ? 400  VAL B CG1   1 
ATOM   14061 C  CG2   . VAL B 2  400  ? 119.480 143.961 164.370 1.00 39.94  ? 400  VAL B CG2   1 
ATOM   14062 N  N     . ILE B 2  401  ? 117.727 140.224 166.536 1.00 41.44  ? 401  ILE B N     1 
ATOM   14063 C  CA    . ILE B 2  401  ? 117.157 138.888 166.729 1.00 42.46  ? 401  ILE B CA    1 
ATOM   14064 C  C     . ILE B 2  401  ? 115.639 138.930 166.828 1.00 43.00  ? 401  ILE B C     1 
ATOM   14065 O  O     . ILE B 2  401  ? 114.947 138.060 166.284 1.00 41.54  ? 401  ILE B O     1 
ATOM   14066 C  CB    . ILE B 2  401  ? 117.768 138.216 167.972 1.00 41.09  ? 401  ILE B CB    1 
ATOM   14067 C  CG1   . ILE B 2  401  ? 119.008 137.443 167.571 1.00 40.91  ? 401  ILE B CG1   1 
ATOM   14068 C  CG2   . ILE B 2  401  ? 116.760 137.304 168.659 1.00 37.81  ? 401  ILE B CG2   1 
ATOM   14069 C  CD1   . ILE B 2  401  ? 118.706 136.356 166.586 1.00 41.34  ? 401  ILE B CD1   1 
ATOM   14070 N  N     . MET B 2  402  ? 115.094 139.937 167.505 1.00 47.76  ? 402  MET B N     1 
ATOM   14071 C  CA    . MET B 2  402  ? 113.675 139.957 167.826 1.00 46.21  ? 402  MET B CA    1 
ATOM   14072 C  C     . MET B 2  402  ? 112.799 140.215 166.608 1.00 45.13  ? 402  MET B C     1 
ATOM   14073 O  O     . MET B 2  402  ? 111.571 140.214 166.742 1.00 45.53  ? 402  MET B O     1 
ATOM   14074 C  CB    . MET B 2  402  ? 113.426 141.025 168.889 1.00 45.56  ? 402  MET B CB    1 
ATOM   14075 C  CG    . MET B 2  402  ? 112.274 140.738 169.810 1.00 47.64  ? 402  MET B CG    1 
ATOM   14076 S  SD    . MET B 2  402  ? 112.750 141.174 171.491 1.00 57.69  ? 402  MET B SD    1 
ATOM   14077 C  CE    . MET B 2  402  ? 113.684 139.718 171.945 1.00 46.81  ? 402  MET B CE    1 
ATOM   14078 N  N     . ASN B 2  403  ? 113.398 140.424 165.435 1.00 42.00  ? 403  ASN B N     1 
ATOM   14079 C  CA    . ASN B 2  403  ? 112.683 140.807 164.217 1.00 42.74  ? 403  ASN B CA    1 
ATOM   14080 C  C     . ASN B 2  403  ? 111.948 142.131 164.396 1.00 41.88  ? 403  ASN B C     1 
ATOM   14081 O  O     . ASN B 2  403  ? 110.880 142.343 163.820 1.00 41.04  ? 403  ASN B O     1 
ATOM   14082 C  CB    . ASN B 2  403  ? 111.712 139.717 163.756 1.00 43.09  ? 403  ASN B CB    1 
ATOM   14083 C  CG    . ASN B 2  403  ? 112.422 138.483 163.251 1.00 47.21  ? 403  ASN B CG    1 
ATOM   14084 O  OD1   . ASN B 2  403  ? 113.485 138.570 162.638 1.00 46.56  ? 403  ASN B OD1   1 
ATOM   14085 N  ND2   . ASN B 2  403  ? 111.835 137.320 163.502 1.00 45.43  ? 403  ASN B ND2   1 
ATOM   14086 N  N     . VAL B 2  404  ? 112.504 143.019 165.213 1.00 42.36  ? 404  VAL B N     1 
ATOM   14087 C  CA    . VAL B 2  404  ? 111.981 144.374 165.333 1.00 41.72  ? 404  VAL B CA    1 
ATOM   14088 C  C     . VAL B 2  404  ? 112.607 145.290 164.291 1.00 42.39  ? 404  VAL B C     1 
ATOM   14089 O  O     . VAL B 2  404  ? 111.928 146.141 163.710 1.00 42.28  ? 404  VAL B O     1 
ATOM   14090 C  CB    . VAL B 2  404  ? 112.212 144.901 166.764 1.00 40.57  ? 404  VAL B CB    1 
ATOM   14091 C  CG1   . VAL B 2  404  ? 111.953 146.395 166.836 1.00 39.79  ? 404  VAL B CG1   1 
ATOM   14092 C  CG2   . VAL B 2  404  ? 111.339 144.156 167.755 1.00 40.93  ? 404  VAL B CG2   1 
ATOM   14093 N  N     . PHE B 2  405  ? 113.898 145.110 164.035 1.00 43.89  ? 405  PHE B N     1 
ATOM   14094 C  CA    . PHE B 2  405  ? 114.666 145.843 163.046 1.00 41.21  ? 405  PHE B CA    1 
ATOM   14095 C  C     . PHE B 2  405  ? 115.394 144.867 162.136 1.00 41.00  ? 405  PHE B C     1 
ATOM   14096 O  O     . PHE B 2  405  ? 115.678 143.735 162.535 1.00 42.31  ? 405  PHE B O     1 
ATOM   14097 C  CB    . PHE B 2  405  ? 115.681 146.779 163.714 1.00 40.79  ? 405  PHE B CB    1 
ATOM   14098 C  CG    . PHE B 2  405  ? 115.061 147.768 164.645 1.00 43.65  ? 405  PHE B CG    1 
ATOM   14099 C  CD1   . PHE B 2  405  ? 114.011 148.565 164.226 1.00 44.42  ? 405  PHE B CD1   1 
ATOM   14100 C  CD2   . PHE B 2  405  ? 115.527 147.911 165.936 1.00 41.51  ? 405  PHE B CD2   1 
ATOM   14101 C  CE1   . PHE B 2  405  ? 113.433 149.477 165.078 1.00 42.81  ? 405  PHE B CE1   1 
ATOM   14102 C  CE2   . PHE B 2  405  ? 114.954 148.829 166.794 1.00 42.09  ? 405  PHE B CE2   1 
ATOM   14103 C  CZ    . PHE B 2  405  ? 113.906 149.612 166.363 1.00 44.55  ? 405  PHE B CZ    1 
ATOM   14104 N  N     . PRO B 2  406  ? 115.680 145.268 160.902 1.00 37.71  ? 406  PRO B N     1 
ATOM   14105 C  CA    . PRO B 2  406  ? 116.402 144.387 159.982 1.00 35.68  ? 406  PRO B CA    1 
ATOM   14106 C  C     . PRO B 2  406  ? 117.882 144.355 160.314 1.00 35.21  ? 406  PRO B C     1 
ATOM   14107 O  O     . PRO B 2  406  ? 118.364 145.162 161.123 1.00 35.48  ? 406  PRO B O     1 
ATOM   14108 C  CB    . PRO B 2  406  ? 116.159 145.023 158.606 1.00 35.39  ? 406  PRO B CB    1 
ATOM   14109 C  CG    . PRO B 2  406  ? 115.683 146.390 158.864 1.00 37.39  ? 406  PRO B CG    1 
ATOM   14110 C  CD    . PRO B 2  406  ? 115.180 146.490 160.254 1.00 35.77  ? 406  PRO B CD    1 
ATOM   14111 N  N     . PRO B 2  407  ? 118.637 143.434 159.721 1.00 34.96  ? 407  PRO B N     1 
ATOM   14112 C  CA    . PRO B 2  407  ? 120.098 143.496 159.839 1.00 33.49  ? 407  PRO B CA    1 
ATOM   14113 C  C     . PRO B 2  407  ? 120.699 144.660 159.066 1.00 34.44  ? 407  PRO B C     1 
ATOM   14114 O  O     . PRO B 2  407  ? 119.975 145.459 158.465 1.00 36.24  ? 407  PRO B O     1 
ATOM   14115 C  CB    . PRO B 2  407  ? 120.551 142.148 159.267 1.00 32.93  ? 407  PRO B CB    1 
ATOM   14116 C  CG    . PRO B 2  407  ? 119.449 141.720 158.391 1.00 33.91  ? 407  PRO B CG    1 
ATOM   14117 C  CD    . PRO B 2  407  ? 118.196 142.210 159.037 1.00 34.18  ? 407  PRO B CD    1 
ATOM   14118 N  N     . THR B 2  408  ? 122.023 144.768 159.083 1.00 33.69  ? 408  THR B N     1 
ATOM   14119 C  CA    . THR B 2  408  ? 122.706 145.865 158.409 1.00 34.71  ? 408  THR B CA    1 
ATOM   14120 C  C     . THR B 2  408  ? 122.679 145.677 156.897 1.00 38.91  ? 408  THR B C     1 
ATOM   14121 O  O     . THR B 2  408  ? 122.919 144.576 156.393 1.00 41.12  ? 408  THR B O     1 
ATOM   14122 C  CB    . THR B 2  408  ? 124.145 145.967 158.919 1.00 34.74  ? 408  THR B CB    1 
ATOM   14123 O  OG1   . THR B 2  408  ? 124.168 146.765 160.105 1.00 37.13  ? 408  THR B OG1   1 
ATOM   14124 C  CG2   . THR B 2  408  ? 125.066 146.584 157.885 1.00 35.35  ? 408  THR B CG2   1 
ATOM   14125 N  N     . ASP B 2  409  ? 122.381 146.756 156.174 1.00 38.03  ? 409  ASP B N     1 
ATOM   14126 C  CA    . ASP B 2  409  ? 122.426 146.757 154.715 1.00 36.55  ? 409  ASP B CA    1 
ATOM   14127 C  C     . ASP B 2  409  ? 123.873 146.927 154.264 1.00 36.34  ? 409  ASP B C     1 
ATOM   14128 O  O     . ASP B 2  409  ? 124.461 148.000 154.425 1.00 38.40  ? 409  ASP B O     1 
ATOM   14129 C  CB    . ASP B 2  409  ? 121.529 147.863 154.168 1.00 37.32  ? 409  ASP B CB    1 
ATOM   14130 C  CG    . ASP B 2  409  ? 121.270 147.728 152.683 1.00 40.66  ? 409  ASP B CG    1 
ATOM   14131 O  OD1   . ASP B 2  409  ? 121.877 146.846 152.044 1.00 39.05  ? 409  ASP B OD1   1 
ATOM   14132 O  OD2   . ASP B 2  409  ? 120.437 148.491 152.155 1.00 38.15  ? 409  ASP B OD2   1 
ATOM   14133 N  N     . ARG B 2  410  ? 124.446 145.872 153.691 1.00 38.56  ? 410  ARG B N     1 
ATOM   14134 C  CA    . ARG B 2  410  ? 125.862 145.853 153.351 1.00 38.40  ? 410  ARG B CA    1 
ATOM   14135 C  C     . ARG B 2  410  ? 126.207 146.723 152.156 1.00 41.95  ? 410  ARG B C     1 
ATOM   14136 O  O     . ARG B 2  410  ? 127.391 146.983 151.927 1.00 40.67  ? 410  ARG B O     1 
ATOM   14137 C  CB    . ARG B 2  410  ? 126.322 144.419 153.078 1.00 40.03  ? 410  ARG B CB    1 
ATOM   14138 C  CG    . ARG B 2  410  ? 126.774 143.681 154.323 1.00 44.81  ? 410  ARG B CG    1 
ATOM   14139 C  CD    . ARG B 2  410  ? 127.041 142.214 154.058 1.00 42.86  ? 410  ARG B CD    1 
ATOM   14140 N  NE    . ARG B 2  410  ? 125.814 141.429 154.019 1.00 44.83  ? 410  ARG B NE    1 
ATOM   14141 C  CZ    . ARG B 2  410  ? 125.776 140.118 153.826 1.00 46.65  ? 410  ARG B CZ    1 
ATOM   14142 N  NH1   . ARG B 2  410  ? 126.883 139.411 153.668 1.00 45.68  ? 410  ARG B NH1   1 
ATOM   14143 N  NH2   . ARG B 2  410  ? 124.599 139.501 153.787 1.00 42.68  ? 410  ARG B NH2   1 
ATOM   14144 N  N     . ASP B 2  411  ? 125.218 147.183 151.394 1.00 40.45  ? 411  ASP B N     1 
ATOM   14145 C  CA    . ASP B 2  411  ? 125.473 147.978 150.205 1.00 36.21  ? 411  ASP B CA    1 
ATOM   14146 C  C     . ASP B 2  411  ? 125.126 149.444 150.356 1.00 33.90  ? 411  ASP B C     1 
ATOM   14147 O  O     . ASP B 2  411  ? 125.524 150.239 149.503 1.00 35.19  ? 411  ASP B O     1 
ATOM   14148 C  CB    . ASP B 2  411  ? 124.705 147.407 149.009 1.00 31.38  ? 411  ASP B CB    1 
ATOM   14149 C  CG    . ASP B 2  411  ? 124.892 145.923 148.871 1.00 37.76  ? 411  ASP B CG    1 
ATOM   14150 O  OD1   . ASP B 2  411  ? 126.051 145.473 148.891 1.00 39.23  ? 411  ASP B OD1   1 
ATOM   14151 O  OD2   . ASP B 2  411  ? 123.885 145.200 148.746 1.00 43.29  ? 411  ASP B OD2   1 
ATOM   14152 N  N     . SER B 2  412  ? 124.412 149.826 151.404 1.00 24.52  ? 412  SER B N     1 
ATOM   14153 C  CA    . SER B 2  412  ? 124.078 151.223 151.595 1.00 24.96  ? 412  SER B CA    1 
ATOM   14154 C  C     . SER B 2  412  ? 125.334 152.025 151.920 1.00 25.81  ? 412  SER B C     1 
ATOM   14155 O  O     . SER B 2  412  ? 126.301 151.508 152.478 1.00 32.03  ? 412  SER B O     1 
ATOM   14156 C  CB    . SER B 2  412  ? 123.037 151.366 152.696 1.00 22.49  ? 412  SER B CB    1 
ATOM   14157 O  OG    . SER B 2  412  ? 122.863 152.720 153.035 1.00 27.47  ? 412  SER B OG    1 
ATOM   14158 N  N     . TYR B 2  413  ? 125.330 153.292 151.528 1.00 23.99  ? 413  TYR B N     1 
ATOM   14159 C  CA    . TYR B 2  413  ? 126.505 154.132 151.682 1.00 21.42  ? 413  TYR B CA    1 
ATOM   14160 C  C     . TYR B 2  413  ? 126.492 154.975 152.944 1.00 25.80  ? 413  TYR B C     1 
ATOM   14161 O  O     . TYR B 2  413  ? 127.395 155.794 153.122 1.00 27.38  ? 413  TYR B O     1 
ATOM   14162 C  CB    . TYR B 2  413  ? 126.682 155.054 150.474 1.00 20.00  ? 413  TYR B CB    1 
ATOM   14163 C  CG    . TYR B 2  413  ? 127.791 154.602 149.567 1.00 24.21  ? 413  TYR B CG    1 
ATOM   14164 C  CD1   . TYR B 2  413  ? 127.699 153.407 148.878 1.00 23.29  ? 413  TYR B CD1   1 
ATOM   14165 C  CD2   . TYR B 2  413  ? 128.961 155.327 149.463 1.00 23.44  ? 413  TYR B CD2   1 
ATOM   14166 C  CE1   . TYR B 2  413  ? 128.715 152.978 148.073 1.00 23.36  ? 413  TYR B CE1   1 
ATOM   14167 C  CE2   . TYR B 2  413  ? 129.987 154.899 148.663 1.00 21.22  ? 413  TYR B CE2   1 
ATOM   14168 C  CZ    . TYR B 2  413  ? 129.859 153.725 147.971 1.00 23.69  ? 413  TYR B CZ    1 
ATOM   14169 O  OH    . TYR B 2  413  ? 130.879 153.292 147.167 1.00 26.79  ? 413  TYR B OH    1 
ATOM   14170 N  N     . ARG B 2  414  ? 125.503 154.815 153.819 1.00 24.31  ? 414  ARG B N     1 
ATOM   14171 C  CA    . ARG B 2  414  ? 125.607 155.498 155.099 1.00 28.23  ? 414  ARG B CA    1 
ATOM   14172 C  C     . ARG B 2  414  ? 126.678 154.879 155.986 1.00 30.67  ? 414  ARG B C     1 
ATOM   14173 O  O     . ARG B 2  414  ? 127.040 155.474 157.003 1.00 29.51  ? 414  ARG B O     1 
ATOM   14174 C  CB    . ARG B 2  414  ? 124.269 155.484 155.833 1.00 25.39  ? 414  ARG B CB    1 
ATOM   14175 C  CG    . ARG B 2  414  ? 123.473 154.217 155.650 1.00 30.43  ? 414  ARG B CG    1 
ATOM   14176 C  CD    . ARG B 2  414  ? 122.199 154.248 156.464 1.00 31.46  ? 414  ARG B CD    1 
ATOM   14177 N  NE    . ARG B 2  414  ? 122.381 154.961 157.722 1.00 34.51  ? 414  ARG B NE    1 
ATOM   14178 C  CZ    . ARG B 2  414  ? 122.951 154.451 158.806 1.00 33.99  ? 414  ARG B CZ    1 
ATOM   14179 N  NH1   . ARG B 2  414  ? 123.391 153.203 158.835 1.00 27.86  ? 414  ARG B NH1   1 
ATOM   14180 N  NH2   . ARG B 2  414  ? 123.087 155.213 159.886 1.00 31.22  ? 414  ARG B NH2   1 
ATOM   14181 N  N     . THR B 2  415  ? 127.193 153.711 155.620 1.00 27.57  ? 415  THR B N     1 
ATOM   14182 C  CA    . THR B 2  415  ? 128.201 152.994 156.382 1.00 25.69  ? 415  THR B CA    1 
ATOM   14183 C  C     . THR B 2  415  ? 129.364 152.591 155.491 1.00 28.73  ? 415  THR B C     1 
ATOM   14184 O  O     . THR B 2  415  ? 129.916 151.497 155.618 1.00 34.65  ? 415  THR B O     1 
ATOM   14185 C  CB    . THR B 2  415  ? 127.597 151.768 157.062 1.00 33.52  ? 415  THR B CB    1 
ATOM   14186 O  OG1   . THR B 2  415  ? 126.836 151.014 156.108 1.00 35.72  ? 415  THR B OG1   1 
ATOM   14187 C  CG2   . THR B 2  415  ? 126.689 152.184 158.208 1.00 29.72  ? 415  THR B CG2   1 
ATOM   14188 N  N     . LYS B 2  416  ? 129.747 153.458 154.562 1.00 21.07  ? 416  LYS B N     1 
ATOM   14189 C  CA    . LYS B 2  416  ? 130.896 153.220 153.705 1.00 20.77  ? 416  LYS B CA    1 
ATOM   14190 C  C     . LYS B 2  416  ? 131.829 154.414 153.774 1.00 26.50  ? 416  LYS B C     1 
ATOM   14191 O  O     . LYS B 2  416  ? 131.406 155.545 154.015 1.00 32.77  ? 416  LYS B O     1 
ATOM   14192 C  CB    . LYS B 2  416  ? 130.504 152.979 152.246 1.00 23.93  ? 416  LYS B CB    1 
ATOM   14193 C  CG    . LYS B 2  416  ? 129.563 151.837 152.018 1.00 25.10  ? 416  LYS B CG    1 
ATOM   14194 C  CD    . LYS B 2  416  ? 130.278 150.528 152.115 1.00 26.36  ? 416  LYS B CD    1 
ATOM   14195 C  CE    . LYS B 2  416  ? 129.401 149.405 151.616 1.00 28.98  ? 416  LYS B CE    1 
ATOM   14196 N  NZ    . LYS B 2  416  ? 129.193 149.500 150.157 1.00 24.84  ? 416  LYS B NZ    1 
ATOM   14197 N  N     . ARG B 2  417  ? 133.111 154.145 153.560 1.00 27.80  ? 417  ARG B N     1 
ATOM   14198 C  CA    . ARG B 2  417  ? 134.126 155.183 153.528 1.00 22.32  ? 417  ARG B CA    1 
ATOM   14199 C  C     . ARG B 2  417  ? 135.038 154.925 152.340 1.00 27.28  ? 417  ARG B C     1 
ATOM   14200 O  O     . ARG B 2  417  ? 135.262 153.777 151.952 1.00 26.79  ? 417  ARG B O     1 
ATOM   14201 C  CB    . ARG B 2  417  ? 134.926 155.219 154.830 1.00 24.30  ? 417  ARG B CB    1 
ATOM   14202 C  CG    . ARG B 2  417  ? 134.114 155.646 156.038 1.00 20.82  ? 417  ARG B CG    1 
ATOM   14203 C  CD    . ARG B 2  417  ? 133.571 157.027 155.849 1.00 21.45  ? 417  ARG B CD    1 
ATOM   14204 N  NE    . ARG B 2  417  ? 132.177 157.151 156.252 1.00 25.16  ? 417  ARG B NE    1 
ATOM   14205 C  CZ    . ARG B 2  417  ? 131.772 157.729 157.370 1.00 25.83  ? 417  ARG B CZ    1 
ATOM   14206 N  NH1   . ARG B 2  417  ? 132.631 158.218 158.240 1.00 29.40  ? 417  ARG B NH1   1 
ATOM   14207 N  NH2   . ARG B 2  417  ? 130.472 157.845 157.607 1.00 24.11  ? 417  ARG B NH2   1 
ATOM   14208 N  N     . VAL B 2  418  ? 135.555 156.003 151.758 1.00 27.12  ? 418  VAL B N     1 
ATOM   14209 C  CA    . VAL B 2  418  ? 136.406 155.941 150.574 1.00 25.92  ? 418  VAL B CA    1 
ATOM   14210 C  C     . VAL B 2  418  ? 137.727 156.604 150.938 1.00 29.32  ? 418  VAL B C     1 
ATOM   14211 O  O     . VAL B 2  418  ? 137.770 157.814 151.185 1.00 33.73  ? 418  VAL B O     1 
ATOM   14212 C  CB    . VAL B 2  418  ? 135.752 156.628 149.368 1.00 24.77  ? 418  VAL B CB    1 
ATOM   14213 C  CG1   . VAL B 2  418  ? 136.649 156.550 148.162 1.00 28.54  ? 418  VAL B CG1   1 
ATOM   14214 C  CG2   . VAL B 2  418  ? 134.405 156.014 149.075 1.00 28.06  ? 418  VAL B CG2   1 
ATOM   14215 N  N     . HIS B 2  419  ? 138.808 155.827 150.962 1.00 30.79  ? 419  HIS B N     1 
ATOM   14216 C  CA    . HIS B 2  419  ? 140.038 156.306 151.585 1.00 33.84  ? 419  HIS B CA    1 
ATOM   14217 C  C     . HIS B 2  419  ? 141.054 156.871 150.594 1.00 32.10  ? 419  HIS B C     1 
ATOM   14218 O  O     . HIS B 2  419  ? 141.392 158.056 150.658 1.00 33.96  ? 419  HIS B O     1 
ATOM   14219 C  CB    . HIS B 2  419  ? 140.641 155.183 152.428 1.00 33.32  ? 419  HIS B CB    1 
ATOM   14220 C  CG    . HIS B 2  419  ? 139.816 154.849 153.626 1.00 30.91  ? 419  HIS B CG    1 
ATOM   14221 N  ND1   . HIS B 2  419  ? 139.116 153.670 153.747 1.00 32.10  ? 419  HIS B ND1   1 
ATOM   14222 C  CD2   . HIS B 2  419  ? 139.533 155.571 154.735 1.00 31.19  ? 419  HIS B CD2   1 
ATOM   14223 C  CE1   . HIS B 2  419  ? 138.460 153.668 154.893 1.00 33.05  ? 419  HIS B CE1   1 
ATOM   14224 N  NE2   . HIS B 2  419  ? 138.697 154.810 155.510 1.00 35.56  ? 419  HIS B NE2   1 
ATOM   14225 N  N     . GLY B 2  420  ? 141.564 156.048 149.690 1.00 27.76  ? 420  GLY B N     1 
ATOM   14226 C  CA    . GLY B 2  420  ? 142.448 156.592 148.679 1.00 32.39  ? 420  GLY B CA    1 
ATOM   14227 C  C     . GLY B 2  420  ? 143.939 156.514 148.939 1.00 36.35  ? 420  GLY B C     1 
ATOM   14228 O  O     . GLY B 2  420  ? 144.413 155.604 149.621 1.00 40.79  ? 420  GLY B O     1 
ATOM   14229 N  N     . SER B 2  421  ? 144.691 157.472 148.390 1.00 42.37  ? 421  SER B N     1 
ATOM   14230 C  CA    . SER B 2  421  ? 146.144 157.336 148.322 1.00 41.88  ? 421  SER B CA    1 
ATOM   14231 C  C     . SER B 2  421  ? 146.800 157.561 149.677 1.00 42.26  ? 421  SER B C     1 
ATOM   14232 O  O     . SER B 2  421  ? 147.654 156.775 150.096 1.00 43.64  ? 421  SER B O     1 
ATOM   14233 C  CB    . SER B 2  421  ? 146.722 158.308 147.294 1.00 41.96  ? 421  SER B CB    1 
ATOM   14234 O  OG    . SER B 2  421  ? 146.597 159.648 147.737 1.00 44.26  ? 421  SER B OG    1 
ATOM   14235 N  N     . GLY B 2  422  ? 146.424 158.631 150.375 1.00 36.18  ? 422  GLY B N     1 
ATOM   14236 C  CA    . GLY B 2  422  ? 147.122 158.967 151.605 1.00 37.73  ? 422  GLY B CA    1 
ATOM   14237 C  C     . GLY B 2  422  ? 146.996 157.891 152.666 1.00 38.94  ? 422  GLY B C     1 
ATOM   14238 O  O     . GLY B 2  422  ? 147.998 157.399 153.195 1.00 41.78  ? 422  GLY B O     1 
ATOM   14239 N  N     . VAL B 2  423  ? 145.764 157.491 152.972 1.00 40.14  ? 423  VAL B N     1 
ATOM   14240 C  CA    . VAL B 2  423  ? 145.543 156.536 154.052 1.00 37.18  ? 423  VAL B CA    1 
ATOM   14241 C  C     . VAL B 2  423  ? 146.161 155.187 153.712 1.00 36.62  ? 423  VAL B C     1 
ATOM   14242 O  O     . VAL B 2  423  ? 146.862 154.590 154.534 1.00 39.96  ? 423  VAL B O     1 
ATOM   14243 C  CB    . VAL B 2  423  ? 144.041 156.414 154.360 1.00 37.05  ? 423  VAL B CB    1 
ATOM   14244 C  CG1   . VAL B 2  423  ? 143.784 155.243 155.277 1.00 39.02  ? 423  VAL B CG1   1 
ATOM   14245 C  CG2   . VAL B 2  423  ? 143.534 157.701 154.989 1.00 36.59  ? 423  VAL B CG2   1 
ATOM   14246 N  N     . SER B 2  424  ? 145.918 154.689 152.498 1.00 34.38  ? 424  SER B N     1 
ATOM   14247 C  CA    . SER B 2  424  ? 146.454 153.387 152.109 1.00 35.01  ? 424  SER B CA    1 
ATOM   14248 C  C     . SER B 2  424  ? 147.977 153.401 152.075 1.00 37.16  ? 424  SER B C     1 
ATOM   14249 O  O     . SER B 2  424  ? 148.626 152.431 152.491 1.00 36.22  ? 424  SER B O     1 
ATOM   14250 C  CB    . SER B 2  424  ? 145.892 152.980 150.748 1.00 37.66  ? 424  SER B CB    1 
ATOM   14251 O  OG    . SER B 2  424  ? 146.217 151.638 150.436 1.00 41.24  ? 424  SER B OG    1 
ATOM   14252 N  N     . LEU B 2  425  ? 148.563 154.491 151.574 1.00 34.61  ? 425  LEU B N     1 
ATOM   14253 C  CA    . LEU B 2  425  ? 150.014 154.608 151.535 1.00 34.44  ? 425  LEU B CA    1 
ATOM   14254 C  C     . LEU B 2  425  ? 150.602 154.600 152.937 1.00 38.31  ? 425  LEU B C     1 
ATOM   14255 O  O     . LEU B 2  425  ? 151.622 153.953 153.179 1.00 40.53  ? 425  LEU B O     1 
ATOM   14256 C  CB    . LEU B 2  425  ? 150.427 155.878 150.795 1.00 34.61  ? 425  LEU B CB    1 
ATOM   14257 C  CG    . LEU B 2  425  ? 150.587 155.793 149.275 1.00 36.65  ? 425  LEU B CG    1 
ATOM   14258 C  CD1   . LEU B 2  425  ? 151.302 157.030 148.760 1.00 35.84  ? 425  LEU B CD1   1 
ATOM   14259 C  CD2   . LEU B 2  425  ? 151.304 154.528 148.850 1.00 34.80  ? 425  LEU B CD2   1 
ATOM   14260 N  N     . ALA B 2  426  ? 149.975 155.313 153.876 1.00 42.42  ? 426  ALA B N     1 
ATOM   14261 C  CA    . ALA B 2  426  ? 150.465 155.299 155.253 1.00 40.56  ? 426  ALA B CA    1 
ATOM   14262 C  C     . ALA B 2  426  ? 150.323 153.914 155.883 1.00 37.91  ? 426  ALA B C     1 
ATOM   14263 O  O     . ALA B 2  426  ? 151.239 153.432 156.562 1.00 41.48  ? 426  ALA B O     1 
ATOM   14264 C  CB    . ALA B 2  426  ? 149.733 156.352 156.079 1.00 36.69  ? 426  ALA B CB    1 
ATOM   14265 N  N     . LYS B 2  427  ? 149.186 153.252 155.662 1.00 32.30  ? 427  LYS B N     1 
ATOM   14266 C  CA    . LYS B 2  427  ? 149.002 151.909 156.199 1.00 35.67  ? 427  LYS B CA    1 
ATOM   14267 C  C     . LYS B 2  427  ? 150.055 150.937 155.687 1.00 39.33  ? 427  LYS B C     1 
ATOM   14268 O  O     . LYS B 2  427  ? 150.595 150.158 156.477 1.00 40.45  ? 427  LYS B O     1 
ATOM   14269 C  CB    . LYS B 2  427  ? 147.611 151.372 155.851 1.00 37.51  ? 427  LYS B CB    1 
ATOM   14270 C  CG    . LYS B 2  427  ? 146.437 152.179 156.388 1.00 36.40  ? 427  LYS B CG    1 
ATOM   14271 C  CD    . LYS B 2  427  ? 146.502 152.377 157.887 1.00 38.85  ? 427  LYS B CD    1 
ATOM   14272 C  CE    . LYS B 2  427  ? 146.028 151.123 158.613 1.00 39.73  ? 427  LYS B CE    1 
ATOM   14273 N  NZ    . LYS B 2  427  ? 146.004 151.287 160.093 1.00 37.45  ? 427  LYS B NZ    1 
ATOM   14274 N  N     . ALA B 2  428  ? 150.367 150.967 154.393 1.00 40.79  ? 428  ALA B N     1 
ATOM   14275 C  CA    . ALA B 2  428  ? 151.425 150.114 153.865 1.00 41.72  ? 428  ALA B CA    1 
ATOM   14276 C  C     . ALA B 2  428  ? 152.815 150.559 154.299 1.00 42.51  ? 428  ALA B C     1 
ATOM   14277 O  O     . ALA B 2  428  ? 153.711 149.719 154.450 1.00 42.09  ? 428  ALA B O     1 
ATOM   14278 C  CB    . ALA B 2  428  ? 151.363 150.074 152.338 1.00 42.28  ? 428  ALA B CB    1 
ATOM   14279 N  N     . PHE B 2  429  ? 153.018 151.862 154.498 1.00 44.14  ? 429  PHE B N     1 
ATOM   14280 C  CA    . PHE B 2  429  ? 154.321 152.360 154.914 1.00 44.97  ? 429  PHE B CA    1 
ATOM   14281 C  C     . PHE B 2  429  ? 154.604 151.995 156.358 1.00 48.32  ? 429  PHE B C     1 
ATOM   14282 O  O     . PHE B 2  429  ? 155.763 151.994 156.784 1.00 50.02  ? 429  PHE B O     1 
ATOM   14283 C  CB    . PHE B 2  429  ? 154.378 153.873 154.706 1.00 44.65  ? 429  PHE B CB    1 
ATOM   14284 C  CG    . PHE B 2  429  ? 155.574 154.532 155.314 1.00 45.07  ? 429  PHE B CG    1 
ATOM   14285 C  CD1   . PHE B 2  429  ? 156.810 154.440 154.704 1.00 47.60  ? 429  PHE B CD1   1 
ATOM   14286 C  CD2   . PHE B 2  429  ? 155.462 155.272 156.474 1.00 45.99  ? 429  PHE B CD2   1 
ATOM   14287 C  CE1   . PHE B 2  429  ? 157.916 155.055 155.251 1.00 48.23  ? 429  PHE B CE1   1 
ATOM   14288 C  CE2   . PHE B 2  429  ? 156.564 155.891 157.026 1.00 47.40  ? 429  PHE B CE2   1 
ATOM   14289 C  CZ    . PHE B 2  429  ? 157.790 155.785 156.414 1.00 47.09  ? 429  PHE B CZ    1 
ATOM   14290 N  N     . LYS B 2  430  ? 153.559 151.690 157.123 1.00 51.32  ? 430  LYS B N     1 
ATOM   14291 C  CA    . LYS B 2  430  ? 153.729 151.242 158.499 1.00 49.72  ? 430  LYS B CA    1 
ATOM   14292 C  C     . LYS B 2  430  ? 153.697 149.728 158.650 1.00 47.14  ? 430  LYS B C     1 
ATOM   14293 O  O     . LYS B 2  430  ? 154.438 149.188 159.475 1.00 48.11  ? 430  LYS B O     1 
ATOM   14294 C  CB    . LYS B 2  430  ? 152.649 151.866 159.386 1.00 50.00  ? 430  LYS B CB    1 
ATOM   14295 C  CG    . LYS B 2  430  ? 153.231 152.682 160.497 1.00 50.63  ? 430  LYS B CG    1 
ATOM   14296 C  CD    . LYS B 2  430  ? 154.287 153.620 159.930 1.00 48.40  ? 430  LYS B CD    1 
ATOM   14297 C  CE    . LYS B 2  430  ? 155.183 154.160 161.027 1.00 53.34  ? 430  LYS B CE    1 
ATOM   14298 N  NZ    . LYS B 2  430  ? 156.474 154.697 160.509 1.00 54.07  ? 430  LYS B NZ    1 
ATOM   14299 N  N     . ALA B 2  431  ? 152.866 149.028 157.875 1.00 44.19  ? 431  ALA B N     1 
ATOM   14300 C  CA    . ALA B 2  431  ? 152.795 147.573 157.965 1.00 45.86  ? 431  ALA B CA    1 
ATOM   14301 C  C     . ALA B 2  431  ? 154.082 146.893 157.521 1.00 44.32  ? 431  ALA B C     1 
ATOM   14302 O  O     . ALA B 2  431  ? 154.549 145.974 158.199 1.00 44.60  ? 431  ALA B O     1 
ATOM   14303 C  CB    . ALA B 2  431  ? 151.624 147.052 157.132 1.00 42.87  ? 431  ALA B CB    1 
ATOM   14304 N  N     . ILE B 2  432  ? 154.664 147.319 156.404 1.00 47.61  ? 432  ILE B N     1 
ATOM   14305 C  CA    . ILE B 2  432  ? 155.946 146.785 155.963 1.00 50.44  ? 432  ILE B CA    1 
ATOM   14306 C  C     . ILE B 2  432  ? 157.098 147.397 156.756 1.00 52.00  ? 432  ILE B C     1 
ATOM   14307 O  O     . ILE B 2  432  ? 158.190 146.810 156.799 1.00 51.74  ? 432  ILE B O     1 
ATOM   14308 C  CB    . ILE B 2  432  ? 156.120 147.001 154.442 1.00 52.01  ? 432  ILE B CB    1 
ATOM   14309 C  CG1   . ILE B 2  432  ? 154.939 146.377 153.696 1.00 50.54  ? 432  ILE B CG1   1 
ATOM   14310 C  CG2   . ILE B 2  432  ? 157.380 146.345 153.931 1.00 50.83  ? 432  ILE B CG2   1 
ATOM   14311 C  CD1   . ILE B 2  432  ? 154.495 147.144 152.476 1.00 49.13  ? 432  ILE B CD1   1 
ATOM   14312 N  N     . PHE B 2  433  ? 156.876 148.542 157.404 1.00 52.07  ? 433  PHE B N     1 
ATOM   14313 C  CA    . PHE B 2  433  ? 157.833 149.080 158.363 1.00 50.64  ? 433  PHE B CA    1 
ATOM   14314 C  C     . PHE B 2  433  ? 158.054 148.124 159.528 1.00 54.72  ? 433  PHE B C     1 
ATOM   14315 O  O     . PHE B 2  433  ? 159.147 148.084 160.107 1.00 51.97  ? 433  PHE B O     1 
ATOM   14316 C  CB    . PHE B 2  433  ? 157.319 150.422 158.873 1.00 50.56  ? 433  PHE B CB    1 
ATOM   14317 C  CG    . PHE B 2  433  ? 158.392 151.389 159.262 1.00 53.36  ? 433  PHE B CG    1 
ATOM   14318 C  CD1   . PHE B 2  433  ? 158.861 152.319 158.355 1.00 50.48  ? 433  PHE B CD1   1 
ATOM   14319 C  CD2   . PHE B 2  433  ? 158.905 151.392 160.544 1.00 51.93  ? 433  PHE B CD2   1 
ATOM   14320 C  CE1   . PHE B 2  433  ? 159.832 153.220 158.712 1.00 49.12  ? 433  PHE B CE1   1 
ATOM   14321 C  CE2   . PHE B 2  433  ? 159.874 152.290 160.902 1.00 51.61  ? 433  PHE B CE2   1 
ATOM   14322 C  CZ    . PHE B 2  433  ? 160.339 153.207 159.982 1.00 50.60  ? 433  PHE B CZ    1 
ATOM   14323 N  N     . ASN B 2  434  ? 157.023 147.356 159.890 1.00 52.27  ? 434  ASN B N     1 
ATOM   14324 C  CA    . ASN B 2  434  ? 157.141 146.409 160.991 1.00 52.04  ? 434  ASN B CA    1 
ATOM   14325 C  C     . ASN B 2  434  ? 158.201 145.352 160.707 1.00 51.19  ? 434  ASN B C     1 
ATOM   14326 O  O     . ASN B 2  434  ? 159.027 145.041 161.573 1.00 51.32  ? 434  ASN B O     1 
ATOM   14327 C  CB    . ASN B 2  434  ? 155.787 145.746 161.244 1.00 48.79  ? 434  ASN B CB    1 
ATOM   14328 C  CG    . ASN B 2  434  ? 155.780 144.883 162.487 1.00 51.21  ? 434  ASN B CG    1 
ATOM   14329 O  OD1   . ASN B 2  434  ? 156.723 144.900 163.277 1.00 50.32  ? 434  ASN B OD1   1 
ATOM   14330 N  ND2   . ASN B 2  434  ? 154.717 144.107 162.658 1.00 50.82  ? 434  ASN B ND2   1 
ATOM   14331 N  N     . THR B 2  435  ? 158.203 144.797 159.500 1.00 46.81  ? 435  THR B N     1 
ATOM   14332 C  CA    . THR B 2  435  ? 158.997 143.606 159.234 1.00 49.69  ? 435  THR B CA    1 
ATOM   14333 C  C     . THR B 2  435  ? 160.456 143.917 158.921 1.00 50.78  ? 435  THR B C     1 
ATOM   14334 O  O     . THR B 2  435  ? 161.351 143.207 159.391 1.00 49.55  ? 435  THR B O     1 
ATOM   14335 C  CB    . THR B 2  435  ? 158.362 142.806 158.093 1.00 50.90  ? 435  THR B CB    1 
ATOM   14336 O  OG1   . THR B 2  435  ? 157.080 142.322 158.514 1.00 52.38  ? 435  THR B OG1   1 
ATOM   14337 C  CG2   . THR B 2  435  ? 159.233 141.626 157.694 1.00 47.91  ? 435  THR B CG2   1 
ATOM   14338 N  N     . SER B 2  436  ? 160.726 144.966 158.151 1.00 50.69  ? 436  SER B N     1 
ATOM   14339 C  CA    . SER B 2  436  ? 162.075 145.221 157.670 1.00 51.56  ? 436  SER B CA    1 
ATOM   14340 C  C     . SER B 2  436  ? 162.736 146.439 158.309 1.00 51.53  ? 436  SER B C     1 
ATOM   14341 O  O     . SER B 2  436  ? 163.692 146.972 157.738 1.00 50.93  ? 436  SER B O     1 
ATOM   14342 C  CB    . SER B 2  436  ? 162.072 145.367 156.148 1.00 50.86  ? 436  SER B CB    1 
ATOM   14343 O  OG    . SER B 2  436  ? 163.383 145.584 155.657 1.00 50.36  ? 436  SER B OG    1 
ATOM   14344 N  N     . VAL B 2  437  ? 162.250 146.912 159.457 1.00 48.31  ? 437  VAL B N     1 
ATOM   14345 C  CA    . VAL B 2  437  ? 163.030 147.889 160.212 1.00 49.16  ? 437  VAL B CA    1 
ATOM   14346 C  C     . VAL B 2  437  ? 163.264 147.425 161.647 1.00 52.77  ? 437  VAL B C     1 
ATOM   14347 O  O     . VAL B 2  437  ? 164.414 147.233 162.057 1.00 46.73  ? 437  VAL B O     1 
ATOM   14348 C  CB    . VAL B 2  437  ? 162.380 149.284 160.177 1.00 49.29  ? 437  VAL B CB    1 
ATOM   14349 C  CG1   . VAL B 2  437  ? 163.041 150.202 161.192 1.00 47.51  ? 437  VAL B CG1   1 
ATOM   14350 C  CG2   . VAL B 2  437  ? 162.525 149.877 158.794 1.00 45.31  ? 437  VAL B CG2   1 
ATOM   14351 N  N     . ILE B 2  438  ? 162.193 147.240 162.426 1.00 54.24  ? 438  ILE B N     1 
ATOM   14352 C  CA    . ILE B 2  438  ? 162.394 146.954 163.846 1.00 52.62  ? 438  ILE B CA    1 
ATOM   14353 C  C     . ILE B 2  438  ? 162.929 145.541 164.048 1.00 51.87  ? 438  ILE B C     1 
ATOM   14354 O  O     . ILE B 2  438  ? 163.802 145.319 164.890 1.00 49.14  ? 438  ILE B O     1 
ATOM   14355 C  CB    . ILE B 2  438  ? 161.108 147.196 164.664 1.00 52.16  ? 438  ILE B CB    1 
ATOM   14356 C  CG1   . ILE B 2  438  ? 160.031 146.157 164.355 1.00 50.10  ? 438  ILE B CG1   1 
ATOM   14357 C  CG2   . ILE B 2  438  ? 160.568 148.598 164.410 1.00 50.03  ? 438  ILE B CG2   1 
ATOM   14358 C  CD1   . ILE B 2  438  ? 158.950 146.083 165.412 1.00 48.96  ? 438  ILE B CD1   1 
ATOM   14359 N  N     . ALA B 2  439  ? 162.414 144.565 163.299 1.00 48.22  ? 439  ALA B N     1 
ATOM   14360 C  CA    . ALA B 2  439  ? 162.918 143.200 163.426 1.00 48.41  ? 439  ALA B CA    1 
ATOM   14361 C  C     . ALA B 2  439  ? 164.374 143.063 162.993 1.00 48.90  ? 439  ALA B C     1 
ATOM   14362 O  O     . ALA B 2  439  ? 165.124 142.343 163.678 1.00 45.90  ? 439  ALA B O     1 
ATOM   14363 C  CB    . ALA B 2  439  ? 162.013 142.231 162.651 1.00 45.73  ? 439  ALA B CB    1 
ATOM   14364 N  N     . PRO B 2  440  ? 164.827 143.656 161.880 1.00 52.94  ? 440  PRO B N     1 
ATOM   14365 C  CA    . PRO B 2  440  ? 166.274 143.642 161.610 1.00 52.59  ? 440  PRO B CA    1 
ATOM   14366 C  C     . PRO B 2  440  ? 167.090 144.288 162.713 1.00 53.17  ? 440  PRO B C     1 
ATOM   14367 O  O     . PRO B 2  440  ? 168.184 143.805 163.022 1.00 52.36  ? 440  PRO B O     1 
ATOM   14368 C  CB    . PRO B 2  440  ? 166.386 144.411 160.288 1.00 48.91  ? 440  PRO B CB    1 
ATOM   14369 C  CG    . PRO B 2  440  ? 165.081 144.191 159.631 1.00 50.09  ? 440  PRO B CG    1 
ATOM   14370 C  CD    . PRO B 2  440  ? 164.074 144.207 160.739 1.00 48.03  ? 440  PRO B CD    1 
ATOM   14371 N  N     . ILE B 2  441  ? 166.582 145.360 163.326 1.00 48.89  ? 441  ILE B N     1 
ATOM   14372 C  CA    . ILE B 2  441  ? 167.278 145.972 164.456 1.00 51.30  ? 441  ILE B CA    1 
ATOM   14373 C  C     . ILE B 2  441  ? 167.362 144.995 165.622 1.00 51.74  ? 441  ILE B C     1 
ATOM   14374 O  O     . ILE B 2  441  ? 168.405 144.870 166.277 1.00 47.69  ? 441  ILE B O     1 
ATOM   14375 C  CB    . ILE B 2  441  ? 166.588 147.288 164.860 1.00 50.79  ? 441  ILE B CB    1 
ATOM   14376 C  CG1   . ILE B 2  441  ? 166.851 148.367 163.811 1.00 49.33  ? 441  ILE B CG1   1 
ATOM   14377 C  CG2   . ILE B 2  441  ? 167.066 147.757 166.227 1.00 47.82  ? 441  ILE B CG2   1 
ATOM   14378 C  CD1   . ILE B 2  441  ? 165.928 149.552 163.924 1.00 49.35  ? 441  ILE B CD1   1 
ATOM   14379 N  N     . ILE B 2  442  ? 166.269 144.280 165.892 1.00 48.52  ? 442  ILE B N     1 
ATOM   14380 C  CA    . ILE B 2  442  ? 166.249 143.317 166.988 1.00 49.10  ? 442  ILE B CA    1 
ATOM   14381 C  C     . ILE B 2  442  ? 167.267 142.214 166.742 1.00 47.93  ? 442  ILE B C     1 
ATOM   14382 O  O     . ILE B 2  442  ? 168.043 141.852 167.632 1.00 47.25  ? 442  ILE B O     1 
ATOM   14383 C  CB    . ILE B 2  442  ? 164.832 142.743 167.168 1.00 48.36  ? 442  ILE B CB    1 
ATOM   14384 C  CG1   . ILE B 2  442  ? 163.915 143.791 167.792 1.00 46.46  ? 442  ILE B CG1   1 
ATOM   14385 C  CG2   . ILE B 2  442  ? 164.865 141.485 168.025 1.00 46.99  ? 442  ILE B CG2   1 
ATOM   14386 C  CD1   . ILE B 2  442  ? 164.295 144.136 169.210 1.00 46.45  ? 442  ILE B CD1   1 
ATOM   14387 N  N     . ASN B 2  443  ? 167.281 141.669 165.526 1.00 47.43  ? 443  ASN B N     1 
ATOM   14388 C  CA    . ASN B 2  443  ? 168.197 140.574 165.217 1.00 48.93  ? 443  ASN B CA    1 
ATOM   14389 C  C     . ASN B 2  443  ? 169.646 141.050 165.214 1.00 47.70  ? 443  ASN B C     1 
ATOM   14390 O  O     . ASN B 2  443  ? 170.548 140.319 165.644 1.00 46.68  ? 443  ASN B O     1 
ATOM   14391 C  CB    . ASN B 2  443  ? 167.817 139.945 163.878 1.00 47.01  ? 443  ASN B CB    1 
ATOM   14392 C  CG    . ASN B 2  443  ? 166.459 139.268 163.923 1.00 49.81  ? 443  ASN B CG    1 
ATOM   14393 O  OD1   . ASN B 2  443  ? 166.151 138.538 164.865 1.00 49.54  ? 443  ASN B OD1   1 
ATOM   14394 N  ND2   . ASN B 2  443  ? 165.635 139.514 162.909 1.00 47.43  ? 443  ASN B ND2   1 
ATOM   14395 N  N     . GLY B 2  444  ? 169.888 142.275 164.739 1.00 45.48  ? 444  GLY B N     1 
ATOM   14396 C  CA    . GLY B 2  444  ? 171.227 142.832 164.795 1.00 47.52  ? 444  GLY B CA    1 
ATOM   14397 C  C     . GLY B 2  444  ? 171.704 143.045 166.216 1.00 48.70  ? 444  GLY B C     1 
ATOM   14398 O  O     . GLY B 2  444  ? 172.870 142.810 166.530 1.00 46.88  ? 444  GLY B O     1 
ATOM   14399 N  N     . PHE B 2  445  ? 170.808 143.492 167.098 1.00 52.02  ? 445  PHE B N     1 
ATOM   14400 C  CA    . PHE B 2  445  ? 171.152 143.585 168.513 1.00 54.00  ? 445  PHE B CA    1 
ATOM   14401 C  C     . PHE B 2  445  ? 171.390 142.210 169.126 1.00 53.02  ? 445  PHE B C     1 
ATOM   14402 O  O     . PHE B 2  445  ? 172.277 142.058 169.969 1.00 52.48  ? 445  PHE B O     1 
ATOM   14403 C  CB    . PHE B 2  445  ? 170.054 144.329 169.270 1.00 53.11  ? 445  PHE B CB    1 
ATOM   14404 C  CG    . PHE B 2  445  ? 170.120 145.820 169.118 1.00 53.64  ? 445  PHE B CG    1 
ATOM   14405 C  CD1   . PHE B 2  445  ? 171.323 146.447 168.839 1.00 53.62  ? 445  PHE B CD1   1 
ATOM   14406 C  CD2   . PHE B 2  445  ? 168.984 146.595 169.262 1.00 53.38  ? 445  PHE B CD2   1 
ATOM   14407 C  CE1   . PHE B 2  445  ? 171.392 147.821 168.705 1.00 53.25  ? 445  PHE B CE1   1 
ATOM   14408 C  CE2   . PHE B 2  445  ? 169.045 147.971 169.131 1.00 54.43  ? 445  PHE B CE2   1 
ATOM   14409 C  CZ    . PHE B 2  445  ? 170.251 148.583 168.850 1.00 54.69  ? 445  PHE B CZ    1 
ATOM   14410 N  N     . LYS B 2  446  ? 170.610 141.206 168.716 1.00 52.63  ? 446  LYS B N     1 
ATOM   14411 C  CA    . LYS B 2  446  ? 170.828 139.839 169.182 1.00 53.06  ? 446  LYS B CA    1 
ATOM   14412 C  C     . LYS B 2  446  ? 172.219 139.349 168.805 1.00 55.33  ? 446  LYS B C     1 
ATOM   14413 O  O     . LYS B 2  446  ? 172.910 138.719 169.612 1.00 56.00  ? 446  LYS B O     1 
ATOM   14414 C  CB    . LYS B 2  446  ? 169.769 138.906 168.595 1.00 51.67  ? 446  LYS B CB    1 
ATOM   14415 C  CG    . LYS B 2  446  ? 168.386 139.034 169.200 1.00 53.13  ? 446  LYS B CG    1 
ATOM   14416 C  CD    . LYS B 2  446  ? 167.375 138.256 168.371 1.00 52.18  ? 446  LYS B CD    1 
ATOM   14417 C  CE    . LYS B 2  446  ? 167.613 136.761 168.470 1.00 52.64  ? 446  LYS B CE    1 
ATOM   14418 N  NZ    . LYS B 2  446  ? 166.589 135.989 167.711 1.00 53.65  ? 446  LYS B NZ    1 
ATOM   14419 N  N     . GLU B 2  447  ? 172.637 139.614 167.567 1.00 52.27  ? 447  GLU B N     1 
ATOM   14420 C  CA    . GLU B 2  447  ? 173.947 139.171 167.111 1.00 51.67  ? 447  GLU B CA    1 
ATOM   14421 C  C     . GLU B 2  447  ? 175.083 140.015 167.672 1.00 55.37  ? 447  GLU B C     1 
ATOM   14422 O  O     . GLU B 2  447  ? 176.189 139.494 167.858 1.00 54.53  ? 447  GLU B O     1 
ATOM   14423 C  CB    . GLU B 2  447  ? 174.005 139.173 165.585 1.00 52.91  ? 447  GLU B CB    1 
ATOM   14424 C  CG    . GLU B 2  447  ? 173.065 138.175 164.945 1.00 53.21  ? 447  GLU B CG    1 
ATOM   14425 C  CD    . GLU B 2  447  ? 173.277 136.768 165.460 1.00 54.33  ? 447  GLU B CD    1 
ATOM   14426 O  OE1   . GLU B 2  447  ? 174.443 136.383 165.681 1.00 52.43  ? 447  GLU B OE1   1 
ATOM   14427 O  OE2   . GLU B 2  447  ? 172.272 136.047 165.648 1.00 54.06  ? 447  GLU B OE2   1 
ATOM   14428 N  N     . LEU B 2  448  ? 174.845 141.305 167.921 1.00 54.00  ? 448  LEU B N     1 
ATOM   14429 C  CA    . LEU B 2  448  ? 175.810 142.134 168.633 1.00 52.44  ? 448  LEU B CA    1 
ATOM   14430 C  C     . LEU B 2  448  ? 176.023 141.620 170.046 1.00 51.97  ? 448  LEU B C     1 
ATOM   14431 O  O     . LEU B 2  448  ? 177.161 141.558 170.526 1.00 52.67  ? 448  LEU B O     1 
ATOM   14432 C  CB    . LEU B 2  448  ? 175.329 143.587 168.669 1.00 51.07  ? 448  LEU B CB    1 
ATOM   14433 C  CG    . LEU B 2  448  ? 176.205 144.616 169.391 1.00 53.39  ? 448  LEU B CG    1 
ATOM   14434 C  CD1   . LEU B 2  448  ? 177.262 145.229 168.486 1.00 49.68  ? 448  LEU B CD1   1 
ATOM   14435 C  CD2   . LEU B 2  448  ? 175.344 145.687 170.049 1.00 51.65  ? 448  LEU B CD2   1 
ATOM   14436 N  N     . LEU B 2  449  ? 174.935 141.250 170.722 1.00 48.85  ? 449  LEU B N     1 
ATOM   14437 C  CA    . LEU B 2  449  ? 175.043 140.649 172.044 1.00 53.47  ? 449  LEU B CA    1 
ATOM   14438 C  C     . LEU B 2  449  ? 175.655 139.259 171.969 1.00 55.44  ? 449  LEU B C     1 
ATOM   14439 O  O     . LEU B 2  449  ? 176.282 138.805 172.933 1.00 55.41  ? 449  LEU B O     1 
ATOM   14440 C  CB    . LEU B 2  449  ? 173.663 140.597 172.700 1.00 53.06  ? 449  LEU B CB    1 
ATOM   14441 C  CG    . LEU B 2  449  ? 173.060 141.954 173.075 1.00 54.68  ? 449  LEU B CG    1 
ATOM   14442 C  CD1   . LEU B 2  449  ? 171.656 141.801 173.643 1.00 52.04  ? 449  LEU B CD1   1 
ATOM   14443 C  CD2   . LEU B 2  449  ? 173.964 142.669 174.060 1.00 51.87  ? 449  LEU B CD2   1 
ATOM   14444 N  N     . LYS B 2  450  ? 175.488 138.577 170.832 1.00 53.78  ? 450  LYS B N     1 
ATOM   14445 C  CA    . LYS B 2  450  ? 175.974 137.212 170.682 1.00 53.74  ? 450  LYS B CA    1 
ATOM   14446 C  C     . LYS B 2  450  ? 177.468 137.165 170.377 1.00 53.83  ? 450  LYS B C     1 
ATOM   14447 O  O     . LYS B 2  450  ? 178.045 136.072 170.349 1.00 56.06  ? 450  LYS B O     1 
ATOM   14448 C  CB    . LYS B 2  450  ? 175.180 136.497 169.583 1.00 52.23  ? 450  LYS B CB    1 
ATOM   14449 C  CG    . LYS B 2  450  ? 175.223 134.970 169.643 1.00 52.92  ? 450  LYS B CG    1 
ATOM   14450 C  CD    . LYS B 2  450  ? 174.389 134.469 170.820 1.00 53.21  ? 450  LYS B CD    1 
ATOM   14451 C  CE    . LYS B 2  450  ? 174.047 132.997 170.709 1.00 51.88  ? 450  LYS B CE    1 
ATOM   14452 N  NZ    . LYS B 2  450  ? 175.255 132.140 170.825 1.00 51.19  ? 450  LYS B NZ    1 
ATOM   14453 N  N     . GLN B 2  451  ? 178.102 138.313 170.125 1.00 50.88  ? 451  GLN B N     1 
ATOM   14454 C  CA    . GLN B 2  451  ? 179.544 138.380 169.907 1.00 53.36  ? 451  GLN B CA    1 
ATOM   14455 C  C     . GLN B 2  451  ? 180.256 139.338 170.849 1.00 53.72  ? 451  GLN B C     1 
ATOM   14456 O  O     . GLN B 2  451  ? 181.306 138.994 171.400 1.00 53.11  ? 451  GLN B O     1 
ATOM   14457 C  CB    . GLN B 2  451  ? 179.853 138.762 168.452 1.00 52.23  ? 451  GLN B CB    1 
ATOM   14458 C  CG    . GLN B 2  451  ? 179.679 137.607 167.477 1.00 53.02  ? 451  GLN B CG    1 
ATOM   14459 C  CD    . GLN B 2  451  ? 180.078 137.961 166.060 1.00 53.19  ? 451  GLN B CD    1 
ATOM   14460 O  OE1   . GLN B 2  451  ? 180.472 139.092 165.775 1.00 52.54  ? 451  GLN B OE1   1 
ATOM   14461 N  NE2   . GLN B 2  451  ? 179.971 136.992 165.159 1.00 51.87  ? 451  GLN B NE2   1 
ATOM   14462 N  N     . THR B 2  452  ? 179.723 140.539 171.050 1.00 55.25  ? 452  THR B N     1 
ATOM   14463 C  CA    . THR B 2  452  ? 180.383 141.553 171.860 1.00 55.18  ? 452  THR B CA    1 
ATOM   14464 C  C     . THR B 2  452  ? 179.729 141.615 173.232 1.00 55.60  ? 452  THR B C     1 
ATOM   14465 O  O     . THR B 2  452  ? 178.500 141.550 173.342 1.00 56.03  ? 452  THR B O     1 
ATOM   14466 C  CB    . THR B 2  452  ? 180.327 142.927 171.190 1.00 54.31  ? 452  THR B CB    1 
ATOM   14467 O  OG1   . THR B 2  452  ? 180.399 142.772 169.768 1.00 53.20  ? 452  THR B OG1   1 
ATOM   14468 C  CG2   . THR B 2  452  ? 181.498 143.788 171.661 1.00 52.99  ? 452  THR B CG2   1 
ATOM   14469 N  N     . ALA B 2  453  ? 180.554 141.728 174.271 1.00 51.03  ? 453  ALA B N     1 
ATOM   14470 C  CA    . ALA B 2  453  ? 180.046 141.810 175.633 1.00 53.37  ? 453  ALA B CA    1 
ATOM   14471 C  C     . ALA B 2  453  ? 179.277 143.109 175.832 1.00 54.45  ? 453  ALA B C     1 
ATOM   14472 O  O     . ALA B 2  453  ? 179.661 144.157 175.306 1.00 52.07  ? 453  ALA B O     1 
ATOM   14473 C  CB    . ALA B 2  453  ? 181.199 141.716 176.631 1.00 51.28  ? 453  ALA B CB    1 
ATOM   14474 N  N     . PHE B 2  454  ? 178.181 143.034 176.589 1.00 56.24  ? 454  PHE B N     1 
ATOM   14475 C  CA    . PHE B 2  454  ? 177.347 144.211 176.805 1.00 56.29  ? 454  PHE B CA    1 
ATOM   14476 C  C     . PHE B 2  454  ? 178.025 145.229 177.720 1.00 55.30  ? 454  PHE B C     1 
ATOM   14477 O  O     . PHE B 2  454  ? 177.898 146.439 177.504 1.00 53.66  ? 454  PHE B O     1 
ATOM   14478 C  CB    . PHE B 2  454  ? 175.990 143.793 177.373 1.00 56.03  ? 454  PHE B CB    1 
ATOM   14479 C  CG    . PHE B 2  454  ? 174.952 144.881 177.330 1.00 57.73  ? 454  PHE B CG    1 
ATOM   14480 C  CD1   . PHE B 2  454  ? 174.504 145.377 176.116 1.00 55.31  ? 454  PHE B CD1   1 
ATOM   14481 C  CD2   . PHE B 2  454  ? 174.421 145.404 178.494 1.00 56.05  ? 454  PHE B CD2   1 
ATOM   14482 C  CE1   . PHE B 2  454  ? 173.548 146.370 176.064 1.00 54.18  ? 454  PHE B CE1   1 
ATOM   14483 C  CE2   . PHE B 2  454  ? 173.463 146.400 178.444 1.00 55.04  ? 454  PHE B CE2   1 
ATOM   14484 C  CZ    . PHE B 2  454  ? 173.029 146.882 177.229 1.00 54.95  ? 454  PHE B CZ    1 
ATOM   14485 N  N     . GLU B 2  455  ? 178.738 144.766 178.751 1.00 53.81  ? 455  GLU B N     1 
ATOM   14486 C  CA    . GLU B 2  455  ? 179.441 145.698 179.629 1.00 54.85  ? 455  GLU B CA    1 
ATOM   14487 C  C     . GLU B 2  455  ? 180.581 146.415 178.919 1.00 54.82  ? 455  GLU B C     1 
ATOM   14488 O  O     . GLU B 2  455  ? 180.909 147.547 179.288 1.00 52.32  ? 455  GLU B O     1 
ATOM   14489 C  CB    . GLU B 2  455  ? 179.978 144.980 180.870 1.00 54.11  ? 455  GLU B CB    1 
ATOM   14490 C  CG    . GLU B 2  455  ? 178.957 144.812 181.989 1.00 53.64  ? 455  GLU B CG    1 
ATOM   14491 C  CD    . GLU B 2  455  ? 178.320 143.439 182.014 1.00 54.86  ? 455  GLU B CD    1 
ATOM   14492 O  OE1   . GLU B 2  455  ? 178.744 142.570 181.225 1.00 55.43  ? 455  GLU B OE1   1 
ATOM   14493 O  OE2   . GLU B 2  455  ? 177.392 143.230 182.824 1.00 53.75  ? 455  GLU B OE2   1 
ATOM   14494 N  N     . GLU B 2  456  ? 181.194 145.782 177.920 1.00 58.65  ? 456  GLU B N     1 
ATOM   14495 C  CA    . GLU B 2  456  ? 182.242 146.415 177.135 1.00 57.52  ? 456  GLU B CA    1 
ATOM   14496 C  C     . GLU B 2  456  ? 181.689 147.317 176.041 1.00 57.87  ? 456  GLU B C     1 
ATOM   14497 O  O     . GLU B 2  456  ? 182.437 148.137 175.495 1.00 55.42  ? 456  GLU B O     1 
ATOM   14498 C  CB    . GLU B 2  456  ? 183.153 145.346 176.515 1.00 54.86  ? 456  GLU B CB    1 
ATOM   14499 C  CG    . GLU B 2  456  ? 184.516 145.865 176.075 1.00 56.37  ? 456  GLU B CG    1 
ATOM   14500 C  CD    . GLU B 2  456  ? 184.629 146.027 174.571 1.00 59.08  ? 456  GLU B CD    1 
ATOM   14501 O  OE1   . GLU B 2  456  ? 184.019 145.225 173.838 1.00 59.17  ? 456  GLU B OE1   1 
ATOM   14502 O  OE2   . GLU B 2  456  ? 185.322 146.964 174.122 1.00 58.62  ? 456  GLU B OE2   1 
ATOM   14503 N  N     . LEU B 2  457  ? 180.401 147.201 175.727 1.00 54.52  ? 457  LEU B N     1 
ATOM   14504 C  CA    . LEU B 2  457  ? 179.778 148.055 174.726 1.00 55.07  ? 457  LEU B CA    1 
ATOM   14505 C  C     . LEU B 2  457  ? 179.766 149.497 175.217 1.00 55.27  ? 457  LEU B C     1 
ATOM   14506 O  O     . LEU B 2  457  ? 179.529 149.758 176.401 1.00 54.41  ? 457  LEU B O     1 
ATOM   14507 C  CB    . LEU B 2  457  ? 178.348 147.593 174.439 1.00 53.55  ? 457  LEU B CB    1 
ATOM   14508 C  CG    . LEU B 2  457  ? 178.098 146.304 173.647 1.00 54.85  ? 457  LEU B CG    1 
ATOM   14509 C  CD1   . LEU B 2  457  ? 176.608 146.120 173.387 1.00 52.86  ? 457  LEU B CD1   1 
ATOM   14510 C  CD2   . LEU B 2  457  ? 178.882 146.247 172.350 1.00 53.80  ? 457  LEU B CD2   1 
ATOM   14511 N  N     . THR B 2  458  ? 180.035 150.428 174.312 1.00 54.36  ? 458  THR B N     1 
ATOM   14512 C  CA    . THR B 2  458  ? 179.887 151.852 174.569 1.00 53.99  ? 458  THR B CA    1 
ATOM   14513 C  C     . THR B 2  458  ? 178.991 152.457 173.489 1.00 55.87  ? 458  THR B C     1 
ATOM   14514 O  O     . THR B 2  458  ? 178.409 151.746 172.662 1.00 53.70  ? 458  THR B O     1 
ATOM   14515 C  CB    . THR B 2  458  ? 181.248 152.552 174.627 1.00 55.45  ? 458  THR B CB    1 
ATOM   14516 O  OG1   . THR B 2  458  ? 182.085 152.078 173.565 1.00 55.95  ? 458  THR B OG1   1 
ATOM   14517 C  CG2   . THR B 2  458  ? 181.928 152.305 175.964 1.00 53.72  ? 458  THR B CG2   1 
ATOM   14518 N  N     . GLN B 2  459  ? 178.894 153.788 173.501 1.00 58.80  ? 459  GLN B N     1 
ATOM   14519 C  CA    . GLN B 2  459  ? 178.009 154.480 172.570 1.00 58.50  ? 459  GLN B CA    1 
ATOM   14520 C  C     . GLN B 2  459  ? 178.423 154.231 171.122 1.00 58.33  ? 459  GLN B C     1 
ATOM   14521 O  O     . GLN B 2  459  ? 177.572 154.166 170.225 1.00 57.13  ? 459  GLN B O     1 
ATOM   14522 C  CB    . GLN B 2  459  ? 178.003 155.973 172.895 1.00 55.93  ? 459  GLN B CB    1 
ATOM   14523 C  CG    . GLN B 2  459  ? 176.973 156.788 172.150 1.00 56.58  ? 459  GLN B CG    1 
ATOM   14524 C  CD    . GLN B 2  459  ? 177.109 158.269 172.432 1.00 58.53  ? 459  GLN B CD    1 
ATOM   14525 O  OE1   . GLN B 2  459  ? 178.009 158.695 173.159 1.00 57.86  ? 459  GLN B OE1   1 
ATOM   14526 N  NE2   . GLN B 2  459  ? 176.209 159.064 171.867 1.00 58.29  ? 459  GLN B NE2   1 
ATOM   14527 N  N     . ARG B 2  460  ? 179.727 154.070 170.880 1.00 57.17  ? 460  ARG B N     1 
ATOM   14528 C  CA    . ARG B 2  460  ? 180.200 153.769 169.533 1.00 58.65  ? 460  ARG B CA    1 
ATOM   14529 C  C     . ARG B 2  460  ? 179.632 152.446 169.027 1.00 58.03  ? 460  ARG B C     1 
ATOM   14530 O  O     . ARG B 2  460  ? 179.161 152.362 167.890 1.00 57.36  ? 460  ARG B O     1 
ATOM   14531 C  CB    . ARG B 2  460  ? 181.732 153.746 169.502 1.00 57.85  ? 460  ARG B CB    1 
ATOM   14532 C  CG    . ARG B 2  460  ? 182.378 152.653 170.361 1.00 56.83  ? 460  ARG B CG    1 
ATOM   14533 C  CD    . ARG B 2  460  ? 183.869 152.882 170.560 1.00 57.14  ? 460  ARG B CD    1 
ATOM   14534 N  NE    . ARG B 2  460  ? 184.510 151.760 171.236 1.00 58.20  ? 460  ARG B NE    1 
ATOM   14535 C  CZ    . ARG B 2  460  ? 185.789 151.727 171.587 1.00 58.86  ? 460  ARG B CZ    1 
ATOM   14536 N  NH1   . ARG B 2  460  ? 186.600 152.741 171.337 1.00 58.99  ? 460  ARG B NH1   1 
ATOM   14537 N  NH2   . ARG B 2  460  ? 186.267 150.649 172.204 1.00 56.23  ? 460  ARG B NH2   1 
ATOM   14538 N  N     . ASN B 2  461  ? 179.646 151.408 169.865 1.00 53.05  ? 461  ASN B N     1 
ATOM   14539 C  CA    . ASN B 2  461  ? 179.115 150.115 169.448 1.00 52.95  ? 461  ASN B CA    1 
ATOM   14540 C  C     . ASN B 2  461  ? 177.603 150.152 169.297 1.00 52.32  ? 461  ASN B C     1 
ATOM   14541 O  O     . ASN B 2  461  ? 177.054 149.445 168.448 1.00 50.38  ? 461  ASN B O     1 
ATOM   14542 C  CB    . ASN B 2  461  ? 179.521 149.032 170.443 1.00 52.26  ? 461  ASN B CB    1 
ATOM   14543 C  CG    . ASN B 2  461  ? 180.969 148.626 170.303 1.00 54.50  ? 461  ASN B CG    1 
ATOM   14544 O  OD1   . ASN B 2  461  ? 181.556 148.735 169.224 1.00 53.18  ? 461  ASN B OD1   1 
ATOM   14545 N  ND2   . ASN B 2  461  ? 181.560 148.159 171.397 1.00 52.28  ? 461  ASN B ND2   1 
ATOM   14546 N  N     . ILE B 2  462  ? 176.919 150.967 170.102 1.00 49.88  ? 462  ILE B N     1 
ATOM   14547 C  CA    . ILE B 2  462  ? 175.479 151.142 169.937 1.00 50.87  ? 462  ILE B CA    1 
ATOM   14548 C  C     . ILE B 2  462  ? 175.171 151.753 168.577 1.00 50.18  ? 462  ILE B C     1 
ATOM   14549 O  O     . ILE B 2  462  ? 174.293 151.275 167.845 1.00 47.92  ? 462  ILE B O     1 
ATOM   14550 C  CB    . ILE B 2  462  ? 174.919 152.003 171.084 1.00 49.29  ? 462  ILE B CB    1 
ATOM   14551 C  CG1   . ILE B 2  462  ? 175.177 151.323 172.432 1.00 48.92  ? 462  ILE B CG1   1 
ATOM   14552 C  CG2   . ILE B 2  462  ? 173.432 152.282 170.873 1.00 46.82  ? 462  ILE B CG2   1 
ATOM   14553 C  CD1   . ILE B 2  462  ? 174.892 152.206 173.618 1.00 49.37  ? 462  ILE B CD1   1 
ATOM   14554 N  N     . ILE B 2  463  ? 175.899 152.814 168.213 1.00 48.90  ? 463  ILE B N     1 
ATOM   14555 C  CA    . ILE B 2  463  ? 175.702 153.442 166.910 1.00 48.60  ? 463  ILE B CA    1 
ATOM   14556 C  C     . ILE B 2  463  ? 176.043 152.469 165.795 1.00 49.88  ? 463  ILE B C     1 
ATOM   14557 O  O     . ILE B 2  463  ? 175.344 152.397 164.778 1.00 52.04  ? 463  ILE B O     1 
ATOM   14558 C  CB    . ILE B 2  463  ? 176.531 154.734 166.798 1.00 49.24  ? 463  ILE B CB    1 
ATOM   14559 C  CG1   . ILE B 2  463  ? 176.091 155.757 167.846 1.00 48.70  ? 463  ILE B CG1   1 
ATOM   14560 C  CG2   . ILE B 2  463  ? 176.440 155.306 165.395 1.00 48.02  ? 463  ILE B CG2   1 
ATOM   14561 C  CD1   . ILE B 2  463  ? 177.053 156.908 168.001 1.00 47.57  ? 463  ILE B CD1   1 
ATOM   14562 N  N     . GLU B 2  464  ? 177.131 151.719 165.957 1.00 51.43  ? 464  GLU B N     1 
ATOM   14563 C  CA    . GLU B 2  464  ? 177.546 150.781 164.922 1.00 51.98  ? 464  GLU B CA    1 
ATOM   14564 C  C     . GLU B 2  464  ? 176.502 149.692 164.724 1.00 50.32  ? 464  GLU B C     1 
ATOM   14565 O  O     . GLU B 2  464  ? 176.196 149.313 163.590 1.00 50.78  ? 464  GLU B O     1 
ATOM   14566 C  CB    . GLU B 2  464  ? 178.909 150.186 165.277 1.00 50.59  ? 464  GLU B CB    1 
ATOM   14567 C  CG    . GLU B 2  464  ? 180.051 151.190 165.170 1.00 50.70  ? 464  GLU B CG    1 
ATOM   14568 C  CD    . GLU B 2  464  ? 181.400 150.597 165.531 1.00 52.88  ? 464  GLU B CD    1 
ATOM   14569 O  OE1   . GLU B 2  464  ? 181.445 149.413 165.931 1.00 54.77  ? 464  GLU B OE1   1 
ATOM   14570 O  OE2   . GLU B 2  464  ? 182.413 151.318 165.425 1.00 50.34  ? 464  GLU B OE2   1 
ATOM   14571 N  N     . ALA B 2  465  ? 175.936 149.179 165.820 1.00 44.35  ? 465  ALA B N     1 
ATOM   14572 C  CA    . ALA B 2  465  ? 174.899 148.160 165.709 1.00 43.14  ? 465  ALA B CA    1 
ATOM   14573 C  C     . ALA B 2  465  ? 173.645 148.717 165.048 1.00 44.92  ? 465  ALA B C     1 
ATOM   14574 O  O     . ALA B 2  465  ? 173.049 148.059 164.184 1.00 44.24  ? 465  ALA B O     1 
ATOM   14575 C  CB    . ALA B 2  465  ? 174.570 147.588 167.086 1.00 41.93  ? 465  ALA B CB    1 
ATOM   14576 N  N     . PHE B 2  466  ? 173.230 149.929 165.434 1.00 51.29  ? 466  PHE B N     1 
ATOM   14577 C  CA    . PHE B 2  466  ? 172.044 150.510 164.811 1.00 52.43  ? 466  PHE B CA    1 
ATOM   14578 C  C     . PHE B 2  466  ? 172.261 150.735 163.320 1.00 50.91  ? 466  PHE B C     1 
ATOM   14579 O  O     . PHE B 2  466  ? 171.385 150.419 162.507 1.00 49.93  ? 466  PHE B O     1 
ATOM   14580 C  CB    . PHE B 2  466  ? 171.659 151.819 165.499 1.00 50.31  ? 466  PHE B CB    1 
ATOM   14581 C  CG    . PHE B 2  466  ? 170.258 152.271 165.186 1.00 51.84  ? 466  PHE B CG    1 
ATOM   14582 C  CD1   . PHE B 2  466  ? 169.167 151.603 165.717 1.00 50.65  ? 466  PHE B CD1   1 
ATOM   14583 C  CD2   . PHE B 2  466  ? 170.033 153.359 164.357 1.00 50.33  ? 466  PHE B CD2   1 
ATOM   14584 C  CE1   . PHE B 2  466  ? 167.874 152.014 165.431 1.00 51.66  ? 466  PHE B CE1   1 
ATOM   14585 C  CE2   . PHE B 2  466  ? 168.744 153.773 164.065 1.00 51.85  ? 466  PHE B CE2   1 
ATOM   14586 C  CZ    . PHE B 2  466  ? 167.664 153.100 164.601 1.00 52.33  ? 466  PHE B CZ    1 
ATOM   14587 N  N     . SER B 2  467  ? 173.429 151.256 162.940 1.00 41.41  ? 467  SER B N     1 
ATOM   14588 C  CA    . SER B 2  467  ? 173.733 151.486 161.536 1.00 42.69  ? 467  SER B CA    1 
ATOM   14589 C  C     . SER B 2  467  ? 173.887 150.193 160.745 1.00 43.33  ? 467  SER B C     1 
ATOM   14590 O  O     . SER B 2  467  ? 173.542 150.166 159.559 1.00 43.06  ? 467  SER B O     1 
ATOM   14591 C  CB    . SER B 2  467  ? 175.001 152.332 161.407 1.00 43.89  ? 467  SER B CB    1 
ATOM   14592 O  OG    . SER B 2  467  ? 174.813 153.618 161.976 1.00 45.84  ? 467  SER B OG    1 
ATOM   14593 N  N     . ALA B 2  468  ? 174.390 149.126 161.367 1.00 40.08  ? 468  ALA B N     1 
ATOM   14594 C  CA    . ALA B 2  468  ? 174.475 147.842 160.684 1.00 41.17  ? 468  ALA B CA    1 
ATOM   14595 C  C     . ALA B 2  468  ? 173.096 147.234 160.476 1.00 43.77  ? 468  ALA B C     1 
ATOM   14596 O  O     . ALA B 2  468  ? 172.840 146.604 159.443 1.00 41.47  ? 468  ALA B O     1 
ATOM   14597 C  CB    . ALA B 2  468  ? 175.368 146.884 161.473 1.00 38.23  ? 468  ALA B CB    1 
ATOM   14598 N  N     . ALA B 2  469  ? 172.195 147.419 161.443 1.00 44.15  ? 469  ALA B N     1 
ATOM   14599 C  CA    . ALA B 2  469  ? 170.841 146.898 161.306 1.00 44.89  ? 469  ALA B CA    1 
ATOM   14600 C  C     . ALA B 2  469  ? 170.029 147.658 160.263 1.00 46.20  ? 469  ALA B C     1 
ATOM   14601 O  O     . ALA B 2  469  ? 168.912 147.241 159.939 1.00 45.51  ? 469  ALA B O     1 
ATOM   14602 C  CB    . ALA B 2  469  ? 170.132 146.939 162.657 1.00 42.90  ? 469  ALA B CB    1 
ATOM   14603 N  N     . LEU B 2  470  ? 170.553 148.769 159.747 1.00 44.72  ? 470  LEU B N     1 
ATOM   14604 C  CA    . LEU B 2  470  ? 169.879 149.578 158.732 1.00 44.94  ? 470  LEU B CA    1 
ATOM   14605 C  C     . LEU B 2  470  ? 170.644 149.612 157.414 1.00 44.76  ? 470  LEU B C     1 
ATOM   14606 O  O     . LEU B 2  470  ? 170.751 150.666 156.784 1.00 40.63  ? 470  LEU B O     1 
ATOM   14607 C  CB    . LEU B 2  470  ? 169.657 150.995 159.248 1.00 43.11  ? 470  LEU B CB    1 
ATOM   14608 C  CG    . LEU B 2  470  ? 168.838 151.142 160.528 1.00 44.40  ? 470  LEU B CG    1 
ATOM   14609 C  CD1   . LEU B 2  470  ? 168.556 152.604 160.798 1.00 41.27  ? 470  LEU B CD1   1 
ATOM   14610 C  CD2   . LEU B 2  470  ? 167.550 150.341 160.443 1.00 42.63  ? 470  LEU B CD2   1 
ATOM   14611 N  N     . SER B 2  471  ? 171.184 148.484 156.968 1.00 45.80  ? 471  SER B N     1 
ATOM   14612 C  CA    . SER B 2  471  ? 171.987 148.459 155.751 1.00 45.54  ? 471  SER B CA    1 
ATOM   14613 C  C     . SER B 2  471  ? 171.079 148.423 154.519 1.00 46.37  ? 471  SER B C     1 
ATOM   14614 O  O     . SER B 2  471  ? 169.861 148.612 154.592 1.00 46.15  ? 471  SER B O     1 
ATOM   14615 C  CB    . SER B 2  471  ? 172.954 147.281 155.775 1.00 46.02  ? 471  SER B CB    1 
ATOM   14616 O  OG    . SER B 2  471  ? 172.262 146.048 155.746 1.00 47.31  ? 471  SER B OG    1 
ATOM   14617 N  N     . LYS B 2  472  ? 171.688 148.182 153.356 1.00 52.11  ? 472  LYS B N     1 
ATOM   14618 C  CA    . LYS B 2  472  ? 170.958 148.182 152.093 1.00 53.98  ? 472  LYS B CA    1 
ATOM   14619 C  C     . LYS B 2  472  ? 169.918 147.073 152.022 1.00 53.32  ? 472  LYS B C     1 
ATOM   14620 O  O     . LYS B 2  472  ? 168.936 147.205 151.282 1.00 52.08  ? 472  LYS B O     1 
ATOM   14621 C  CB    . LYS B 2  472  ? 171.946 148.042 150.936 1.00 51.84  ? 472  LYS B CB    1 
ATOM   14622 C  CG    . LYS B 2  472  ? 172.866 149.238 150.790 1.00 51.61  ? 472  LYS B CG    1 
ATOM   14623 C  CD    . LYS B 2  472  ? 173.808 149.079 149.618 1.00 52.79  ? 472  LYS B CD    1 
ATOM   14624 C  CE    . LYS B 2  472  ? 174.879 150.159 149.635 1.00 53.05  ? 472  LYS B CE    1 
ATOM   14625 N  NZ    . LYS B 2  472  ? 175.871 149.981 148.540 1.00 52.04  ? 472  LYS B NZ    1 
ATOM   14626 N  N     . ASN B 2  473  ? 170.113 145.987 152.774 1.00 50.43  ? 473  ASN B N     1 
ATOM   14627 C  CA    . ASN B 2  473  ? 169.169 144.877 152.735 1.00 50.14  ? 473  ASN B CA    1 
ATOM   14628 C  C     . ASN B 2  473  ? 167.796 145.297 153.240 1.00 49.75  ? 473  ASN B C     1 
ATOM   14629 O  O     . ASN B 2  473  ? 166.776 144.977 152.620 1.00 49.52  ? 473  ASN B O     1 
ATOM   14630 C  CB    . ASN B 2  473  ? 169.714 143.703 153.548 1.00 48.87  ? 473  ASN B CB    1 
ATOM   14631 C  CG    . ASN B 2  473  ? 170.158 144.115 154.932 1.00 49.12  ? 473  ASN B CG    1 
ATOM   14632 O  OD1   . ASN B 2  473  ? 170.121 145.296 155.278 1.00 49.16  ? 473  ASN B OD1   1 
ATOM   14633 N  ND2   . ASN B 2  473  ? 170.592 143.148 155.730 1.00 46.66  ? 473  ASN B ND2   1 
ATOM   14634 N  N     . THR B 2  474  ? 167.747 146.031 154.354 1.00 46.97  ? 474  THR B N     1 
ATOM   14635 C  CA    . THR B 2  474  ? 166.456 146.433 154.908 1.00 49.24  ? 474  THR B CA    1 
ATOM   14636 C  C     . THR B 2  474  ? 165.756 147.438 154.000 1.00 48.06  ? 474  THR B C     1 
ATOM   14637 O  O     . THR B 2  474  ? 164.545 147.340 153.768 1.00 45.95  ? 474  THR B O     1 
ATOM   14638 C  CB    . THR B 2  474  ? 166.635 147.006 156.314 1.00 48.82  ? 474  THR B CB    1 
ATOM   14639 O  OG1   . THR B 2  474  ? 167.398 148.217 156.252 1.00 48.57  ? 474  THR B OG1   1 
ATOM   14640 C  CG2   . THR B 2  474  ? 167.359 146.003 157.198 1.00 48.12  ? 474  THR B CG2   1 
ATOM   14641 N  N     . ALA B 2  475  ? 166.500 148.421 153.489 1.00 47.31  ? 475  ALA B N     1 
ATOM   14642 C  CA    . ALA B 2  475  ? 165.900 149.413 152.602 1.00 48.13  ? 475  ALA B CA    1 
ATOM   14643 C  C     . ALA B 2  475  ? 165.367 148.762 151.336 1.00 47.96  ? 475  ALA B C     1 
ATOM   14644 O  O     . ALA B 2  475  ? 164.251 149.067 150.892 1.00 46.74  ? 475  ALA B O     1 
ATOM   14645 C  CB    . ALA B 2  475  ? 166.920 150.498 152.257 1.00 45.46  ? 475  ALA B CB    1 
ATOM   14646 N  N     . SER B 2  476  ? 166.148 147.852 150.748 1.00 47.08  ? 476  SER B N     1 
ATOM   14647 C  CA    . SER B 2  476  ? 165.700 147.145 149.556 1.00 50.10  ? 476  SER B CA    1 
ATOM   14648 C  C     . SER B 2  476  ? 164.470 146.298 149.854 1.00 50.73  ? 476  SER B C     1 
ATOM   14649 O  O     . SER B 2  476  ? 163.507 146.301 149.083 1.00 49.46  ? 476  SER B O     1 
ATOM   14650 C  CB    . SER B 2  476  ? 166.828 146.276 149.004 1.00 49.96  ? 476  SER B CB    1 
ATOM   14651 O  OG    . SER B 2  476  ? 167.005 145.117 149.798 1.00 50.06  ? 476  SER B OG    1 
ATOM   14652 N  N     . ASP B 2  477  ? 164.475 145.576 150.979 1.00 51.25  ? 477  ASP B N     1 
ATOM   14653 C  CA    . ASP B 2  477  ? 163.320 144.757 151.328 1.00 54.46  ? 477  ASP B CA    1 
ATOM   14654 C  C     . ASP B 2  477  ? 162.067 145.609 151.483 1.00 53.22  ? 477  ASP B C     1 
ATOM   14655 O  O     . ASP B 2  477  ? 161.012 145.276 150.932 1.00 51.10  ? 477  ASP B O     1 
ATOM   14656 C  CB    . ASP B 2  477  ? 163.596 143.974 152.612 1.00 52.78  ? 477  ASP B CB    1 
ATOM   14657 C  CG    . ASP B 2  477  ? 164.263 142.636 152.350 1.00 54.35  ? 477  ASP B CG    1 
ATOM   14658 O  OD1   . ASP B 2  477  ? 163.942 141.992 151.327 1.00 55.13  ? 477  ASP B OD1   1 
ATOM   14659 O  OD2   . ASP B 2  477  ? 165.105 142.224 153.174 1.00 53.39  ? 477  ASP B OD2   1 
ATOM   14660 N  N     . LEU B 2  478  ? 162.175 146.733 152.196 1.00 53.12  ? 478  LEU B N     1 
ATOM   14661 C  CA    . LEU B 2  478  ? 161.006 147.571 152.445 1.00 54.23  ? 478  LEU B CA    1 
ATOM   14662 C  C     . LEU B 2  478  ? 160.479 148.193 151.156 1.00 54.45  ? 478  LEU B C     1 
ATOM   14663 O  O     . LEU B 2  478  ? 159.272 148.147 150.883 1.00 52.42  ? 478  LEU B O     1 
ATOM   14664 C  CB    . LEU B 2  478  ? 161.343 148.650 153.478 1.00 54.21  ? 478  LEU B CB    1 
ATOM   14665 C  CG    . LEU B 2  478  ? 160.258 149.690 153.763 1.00 56.18  ? 478  LEU B CG    1 
ATOM   14666 C  CD1   . LEU B 2  478  ? 159.947 149.775 155.249 1.00 53.53  ? 478  LEU B CD1   1 
ATOM   14667 C  CD2   . LEU B 2  478  ? 160.691 151.047 153.236 1.00 52.71  ? 478  LEU B CD2   1 
ATOM   14668 N  N     . ASN B 2  479  ? 161.365 148.785 150.348 1.00 55.09  ? 479  ASN B N     1 
ATOM   14669 C  CA    . ASN B 2  479  ? 160.908 149.408 149.107 1.00 56.11  ? 479  ASN B CA    1 
ATOM   14670 C  C     . ASN B 2  479  ? 160.354 148.377 148.131 1.00 57.27  ? 479  ASN B C     1 
ATOM   14671 O  O     . ASN B 2  479  ? 159.299 148.596 147.524 1.00 58.21  ? 479  ASN B O     1 
ATOM   14672 C  CB    . ASN B 2  479  ? 162.035 150.205 148.455 1.00 53.69  ? 479  ASN B CB    1 
ATOM   14673 C  CG    . ASN B 2  479  ? 162.248 151.546 149.110 1.00 56.33  ? 479  ASN B CG    1 
ATOM   14674 O  OD1   . ASN B 2  479  ? 161.315 152.146 149.641 1.00 56.91  ? 479  ASN B OD1   1 
ATOM   14675 N  ND2   . ASN B 2  479  ? 163.480 152.034 149.066 1.00 54.80  ? 479  ASN B ND2   1 
ATOM   14676 N  N     . ARG B 2  480  ? 161.042 147.244 147.965 1.00 58.09  ? 480  ARG B N     1 
ATOM   14677 C  CA    . ARG B 2  480  ? 160.537 146.210 147.073 1.00 59.02  ? 480  ARG B CA    1 
ATOM   14678 C  C     . ARG B 2  480  ? 159.179 145.699 147.537 1.00 58.02  ? 480  ARG B C     1 
ATOM   14679 O  O     . ARG B 2  480  ? 158.272 145.519 146.721 1.00 55.96  ? 480  ARG B O     1 
ATOM   14680 C  CB    . ARG B 2  480  ? 161.538 145.057 146.974 1.00 59.41  ? 480  ARG B CB    1 
ATOM   14681 C  CG    . ARG B 2  480  ? 162.784 145.329 146.122 1.00 59.10  ? 480  ARG B CG    1 
ATOM   14682 C  CD    . ARG B 2  480  ? 162.483 146.137 144.861 1.00 58.41  ? 480  ARG B CD    1 
ATOM   14683 N  NE    . ARG B 2  480  ? 162.781 147.554 145.034 1.00 60.46  ? 480  ARG B NE    1 
ATOM   14684 C  CZ    . ARG B 2  480  ? 161.931 148.541 144.786 1.00 60.87  ? 480  ARG B CZ    1 
ATOM   14685 N  NH1   . ARG B 2  480  ? 160.697 148.304 144.373 1.00 58.89  ? 480  ARG B NH1   1 
ATOM   14686 N  NH2   . ARG B 2  480  ? 162.330 149.800 144.956 1.00 58.66  ? 480  ARG B NH2   1 
ATOM   14687 N  N     . SER B 2  481  ? 159.011 145.476 148.845 1.00 53.27  ? 481  SER B N     1 
ATOM   14688 C  CA    . SER B 2  481  ? 157.728 144.995 149.348 1.00 54.49  ? 481  SER B CA    1 
ATOM   14689 C  C     . SER B 2  481  ? 156.618 146.020 149.157 1.00 55.44  ? 481  SER B C     1 
ATOM   14690 O  O     . SER B 2  481  ? 155.510 145.653 148.752 1.00 52.38  ? 481  SER B O     1 
ATOM   14691 C  CB    . SER B 2  481  ? 157.851 144.608 150.821 1.00 51.63  ? 481  SER B CB    1 
ATOM   14692 O  OG    . SER B 2  481  ? 158.812 143.582 150.997 1.00 54.08  ? 481  SER B OG    1 
ATOM   14693 N  N     . MET B 2  482  ? 156.887 147.304 149.420 1.00 56.19  ? 482  MET B N     1 
ATOM   14694 C  CA    . MET B 2  482  ? 155.839 148.307 149.251 1.00 57.19  ? 482  MET B CA    1 
ATOM   14695 C  C     . MET B 2  482  ? 155.437 148.443 147.785 1.00 56.75  ? 482  MET B C     1 
ATOM   14696 O  O     . MET B 2  482  ? 154.244 148.525 147.464 1.00 51.40  ? 482  MET B O     1 
ATOM   14697 C  CB    . MET B 2  482  ? 156.278 149.662 149.826 1.00 54.74  ? 482  MET B CB    1 
ATOM   14698 C  CG    . MET B 2  482  ? 157.361 150.393 149.043 1.00 53.10  ? 482  MET B CG    1 
ATOM   14699 S  SD    . MET B 2  482  ? 157.193 152.189 149.024 1.00 59.53  ? 482  MET B SD    1 
ATOM   14700 C  CE    . MET B 2  482  ? 156.998 152.569 150.760 1.00 54.01  ? 482  MET B CE    1 
ATOM   14701 N  N     . GLU B 2  483  ? 156.417 148.445 146.874 1.00 53.53  ? 483  GLU B N     1 
ATOM   14702 C  CA    . GLU B 2  483  ? 156.081 148.642 145.469 1.00 52.49  ? 483  GLU B CA    1 
ATOM   14703 C  C     . GLU B 2  483  ? 155.425 147.397 144.891 1.00 53.57  ? 483  GLU B C     1 
ATOM   14704 O  O     . GLU B 2  483  ? 154.499 147.493 144.076 1.00 52.56  ? 483  GLU B O     1 
ATOM   14705 C  CB    . GLU B 2  483  ? 157.324 149.027 144.670 1.00 50.21  ? 483  GLU B CB    1 
ATOM   14706 C  CG    . GLU B 2  483  ? 158.120 150.217 145.215 1.00 48.30  ? 483  GLU B CG    1 
ATOM   14707 C  CD    . GLU B 2  483  ? 157.365 151.528 145.305 1.00 51.20  ? 483  GLU B CD    1 
ATOM   14708 O  OE1   . GLU B 2  483  ? 156.218 151.551 145.790 1.00 51.74  ? 483  GLU B OE1   1 
ATOM   14709 O  OE2   . GLU B 2  483  ? 157.936 152.558 144.893 1.00 52.29  ? 483  GLU B OE2   1 
ATOM   14710 N  N     . GLN B 2  484  ? 155.889 146.217 145.306 1.00 49.11  ? 484  GLN B N     1 
ATOM   14711 C  CA    . GLN B 2  484  ? 155.232 144.974 144.934 1.00 49.81  ? 484  GLN B CA    1 
ATOM   14712 C  C     . GLN B 2  484  ? 153.793 144.940 145.432 1.00 49.37  ? 484  GLN B C     1 
ATOM   14713 O  O     . GLN B 2  484  ? 152.908 144.448 144.726 1.00 46.77  ? 484  GLN B O     1 
ATOM   14714 C  CB    . GLN B 2  484  ? 156.047 143.800 145.483 1.00 50.56  ? 484  GLN B CB    1 
ATOM   14715 C  CG    . GLN B 2  484  ? 155.533 142.407 145.157 1.00 51.78  ? 484  GLN B CG    1 
ATOM   14716 C  CD    . GLN B 2  484  ? 155.024 141.683 146.387 1.00 50.78  ? 484  GLN B CD    1 
ATOM   14717 O  OE1   . GLN B 2  484  ? 155.537 141.879 147.489 1.00 48.14  ? 484  GLN B OE1   1 
ATOM   14718 N  NE2   . GLN B 2  484  ? 154.020 140.834 146.205 1.00 49.91  ? 484  GLN B NE2   1 
ATOM   14719 N  N     . SER B 2  485  ? 153.538 145.478 146.627 1.00 48.07  ? 485  SER B N     1 
ATOM   14720 C  CA    . SER B 2  485  ? 152.171 145.581 147.123 1.00 49.79  ? 485  SER B CA    1 
ATOM   14721 C  C     . SER B 2  485  ? 151.333 146.529 146.271 1.00 49.26  ? 485  SER B C     1 
ATOM   14722 O  O     . SER B 2  485  ? 150.200 146.196 145.904 1.00 44.81  ? 485  SER B O     1 
ATOM   14723 C  CB    . SER B 2  485  ? 152.180 146.037 148.583 1.00 49.30  ? 485  SER B CB    1 
ATOM   14724 O  OG    . SER B 2  485  ? 150.867 146.211 149.078 1.00 48.58  ? 485  SER B OG    1 
ATOM   14725 N  N     . ILE B 2  486  ? 151.864 147.713 145.941 1.00 48.69  ? 486  ILE B N     1 
ATOM   14726 C  CA    . ILE B 2  486  ? 151.051 148.669 145.187 1.00 48.13  ? 486  ILE B CA    1 
ATOM   14727 C  C     . ILE B 2  486  ? 150.756 148.138 143.787 1.00 47.26  ? 486  ILE B C     1 
ATOM   14728 O  O     . ILE B 2  486  ? 149.654 148.330 143.260 1.00 47.65  ? 486  ILE B O     1 
ATOM   14729 C  CB    . ILE B 2  486  ? 151.695 150.073 145.129 1.00 46.18  ? 486  ILE B CB    1 
ATOM   14730 C  CG1   . ILE B 2  486  ? 152.847 150.131 144.122 1.00 45.25  ? 486  ILE B CG1   1 
ATOM   14731 C  CG2   . ILE B 2  486  ? 152.123 150.535 146.498 1.00 47.54  ? 486  ILE B CG2   1 
ATOM   14732 C  CD1   . ILE B 2  486  ? 153.053 151.494 143.481 1.00 44.49  ? 486  ILE B CD1   1 
ATOM   14733 N  N     . ILE B 2  487  ? 151.714 147.446 143.173 1.00 41.77  ? 487  ILE B N     1 
ATOM   14734 C  CA    . ILE B 2  487  ? 151.531 147.028 141.788 1.00 42.40  ? 487  ILE B CA    1 
ATOM   14735 C  C     . ILE B 2  487  ? 150.764 145.706 141.698 1.00 42.24  ? 487  ILE B C     1 
ATOM   14736 O  O     . ILE B 2  487  ? 150.051 145.467 140.716 1.00 40.07  ? 487  ILE B O     1 
ATOM   14737 C  CB    . ILE B 2  487  ? 152.903 146.990 141.092 1.00 43.32  ? 487  ILE B CB    1 
ATOM   14738 C  CG1   . ILE B 2  487  ? 153.457 148.417 141.010 1.00 39.34  ? 487  ILE B CG1   1 
ATOM   14739 C  CG2   . ILE B 2  487  ? 152.812 146.377 139.708 1.00 42.37  ? 487  ILE B CG2   1 
ATOM   14740 C  CD1   . ILE B 2  487  ? 154.949 148.512 140.988 1.00 38.17  ? 487  ILE B CD1   1 
ATOM   14741 N  N     . SER B 2  488  ? 150.867 144.845 142.715 1.00 42.24  ? 488  SER B N     1 
ATOM   14742 C  CA    . SER B 2  488  ? 150.024 143.656 142.780 1.00 42.76  ? 488  SER B CA    1 
ATOM   14743 C  C     . SER B 2  488  ? 148.602 143.969 143.226 1.00 43.99  ? 488  SER B C     1 
ATOM   14744 O  O     . SER B 2  488  ? 147.695 143.170 142.966 1.00 44.29  ? 488  SER B O     1 
ATOM   14745 C  CB    . SER B 2  488  ? 150.633 142.623 143.728 1.00 44.77  ? 488  SER B CB    1 
ATOM   14746 O  OG    . SER B 2  488  ? 151.885 142.160 143.257 1.00 43.36  ? 488  SER B OG    1 
ATOM   14747 N  N     . GLY B 2  489  ? 148.387 145.097 143.896 1.00 45.68  ? 489  GLY B N     1 
ATOM   14748 C  CA    . GLY B 2  489  ? 147.069 145.454 144.390 1.00 41.75  ? 489  GLY B CA    1 
ATOM   14749 C  C     . GLY B 2  489  ? 146.939 145.332 145.897 1.00 41.42  ? 489  GLY B C     1 
ATOM   14750 O  O     . GLY B 2  489  ? 146.594 144.272 146.422 1.00 40.66  ? 489  GLY B O     1 
ATOM   14751 N  N     . VAL B 2  504  ? 148.740 147.791 148.410 1.00 41.00  ? 504  VAL B N     1 
ATOM   14752 C  CA    . VAL B 2  504  ? 147.930 148.941 148.036 1.00 43.40  ? 504  VAL B CA    1 
ATOM   14753 C  C     . VAL B 2  504  ? 147.285 148.684 146.677 1.00 45.02  ? 504  VAL B C     1 
ATOM   14754 O  O     . VAL B 2  504  ? 147.970 148.360 145.710 1.00 40.35  ? 504  VAL B O     1 
ATOM   14755 C  CB    . VAL B 2  504  ? 148.771 150.236 148.019 1.00 39.23  ? 504  VAL B CB    1 
ATOM   14756 C  CG1   . VAL B 2  504  ? 147.913 151.421 147.632 1.00 39.75  ? 504  VAL B CG1   1 
ATOM   14757 C  CG2   . VAL B 2  504  ? 149.401 150.478 149.366 1.00 34.73  ? 504  VAL B CG2   1 
ATOM   14758 N  N     . SER B 2  505  ? 145.965 148.830 146.603 1.00 44.79  ? 505  SER B N     1 
ATOM   14759 C  CA    . SER B 2  505  ? 145.242 148.580 145.361 1.00 44.20  ? 505  SER B CA    1 
ATOM   14760 C  C     . SER B 2  505  ? 145.469 149.751 144.414 1.00 46.44  ? 505  SER B C     1 
ATOM   14761 O  O     . SER B 2  505  ? 144.889 150.825 144.595 1.00 45.20  ? 505  SER B O     1 
ATOM   14762 C  CB    . SER B 2  505  ? 143.756 148.379 145.634 1.00 42.63  ? 505  SER B CB    1 
ATOM   14763 O  OG    . SER B 2  505  ? 143.048 148.150 144.428 1.00 45.92  ? 505  SER B OG    1 
ATOM   14764 N  N     . THR B 2  506  ? 146.315 149.547 143.405 1.00 40.93  ? 506  THR B N     1 
ATOM   14765 C  CA    . THR B 2  506  ? 146.631 150.574 142.426 1.00 38.30  ? 506  THR B CA    1 
ATOM   14766 C  C     . THR B 2  506  ? 146.467 150.012 141.022 1.00 41.79  ? 506  THR B C     1 
ATOM   14767 O  O     . THR B 2  506  ? 146.586 148.807 140.786 1.00 43.42  ? 506  THR B O     1 
ATOM   14768 C  CB    . THR B 2  506  ? 148.059 151.114 142.596 1.00 43.34  ? 506  THR B CB    1 
ATOM   14769 O  OG1   . THR B 2  506  ? 149.001 150.095 142.250 1.00 45.09  ? 506  THR B OG1   1 
ATOM   14770 C  CG2   . THR B 2  506  ? 148.306 151.553 144.027 1.00 40.49  ? 506  THR B CG2   1 
ATOM   14771 N  N     . GLN B 2  507  ? 146.210 150.918 140.082 1.00 40.67  ? 507  GLN B N     1 
ATOM   14772 C  CA    . GLN B 2  507  ? 146.063 150.583 138.675 1.00 37.66  ? 507  GLN B CA    1 
ATOM   14773 C  C     . GLN B 2  507  ? 147.081 151.380 137.878 1.00 38.80  ? 507  GLN B C     1 
ATOM   14774 O  O     . GLN B 2  507  ? 147.447 152.499 138.242 1.00 38.91  ? 507  GLN B O     1 
ATOM   14775 C  CB    . GLN B 2  507  ? 144.649 150.889 138.157 1.00 35.78  ? 507  GLN B CB    1 
ATOM   14776 C  CG    . GLN B 2  507  ? 143.553 149.965 138.660 1.00 37.16  ? 507  GLN B CG    1 
ATOM   14777 C  CD    . GLN B 2  507  ? 143.600 148.592 138.026 1.00 41.03  ? 507  GLN B CD    1 
ATOM   14778 O  OE1   . GLN B 2  507  ? 143.872 147.598 138.697 1.00 45.06  ? 507  GLN B OE1   1 
ATOM   14779 N  NE2   . GLN B 2  507  ? 143.331 148.527 136.725 1.00 37.58  ? 507  GLN B NE2   1 
ATOM   14780 N  N     . SER B 2  508  ? 147.533 150.794 136.778 1.00 35.36  ? 508  SER B N     1 
ATOM   14781 C  CA    . SER B 2  508  ? 148.392 151.511 135.848 1.00 34.45  ? 508  SER B CA    1 
ATOM   14782 C  C     . SER B 2  508  ? 147.562 152.534 135.085 1.00 34.61  ? 508  SER B C     1 
ATOM   14783 O  O     . SER B 2  508  ? 146.470 152.223 134.604 1.00 32.06  ? 508  SER B O     1 
ATOM   14784 C  CB    . SER B 2  508  ? 149.065 150.540 134.882 1.00 32.77  ? 508  SER B CB    1 
ATOM   14785 O  OG    . SER B 2  508  ? 149.900 151.231 133.972 1.00 32.06  ? 508  SER B OG    1 
ATOM   14786 N  N     . LEU B 2  509  ? 148.074 153.758 134.990 1.00 34.53  ? 509  LEU B N     1 
ATOM   14787 C  CA    . LEU B 2  509  ? 147.369 154.853 134.327 1.00 33.09  ? 509  LEU B CA    1 
ATOM   14788 C  C     . LEU B 2  509  ? 147.439 154.632 132.823 1.00 33.54  ? 509  LEU B C     1 
ATOM   14789 O  O     . LEU B 2  509  ? 148.492 154.761 132.201 1.00 35.73  ? 509  LEU B O     1 
ATOM   14790 C  CB    . LEU B 2  509  ? 147.964 156.198 134.720 1.00 31.26  ? 509  LEU B CB    1 
ATOM   14791 C  CG    . LEU B 2  509  ? 147.294 157.419 134.092 1.00 30.37  ? 509  LEU B CG    1 
ATOM   14792 C  CD1   . LEU B 2  509  ? 145.842 157.514 134.502 1.00 32.41  ? 509  LEU B CD1   1 
ATOM   14793 C  CD2   . LEU B 2  509  ? 148.035 158.686 134.450 1.00 30.82  ? 509  LEU B CD2   1 
ATOM   14794 N  N     . GLU B 2  510  ? 146.302 154.278 132.233 1.00 39.77  ? 510  GLU B N     1 
ATOM   14795 C  CA    . GLU B 2  510  ? 146.219 154.055 130.792 1.00 40.84  ? 510  GLU B CA    1 
ATOM   14796 C  C     . GLU B 2  510  ? 145.603 155.295 130.165 1.00 41.74  ? 510  GLU B C     1 
ATOM   14797 O  O     . GLU B 2  510  ? 144.398 155.532 130.258 1.00 42.81  ? 510  GLU B O     1 
ATOM   14798 C  CB    . GLU B 2  510  ? 145.406 152.806 130.484 1.00 40.81  ? 510  GLU B CB    1 
ATOM   14799 C  CG    . GLU B 2  510  ? 145.891 151.581 131.224 1.00 40.08  ? 510  GLU B CG    1 
ATOM   14800 C  CD    . GLU B 2  510  ? 147.222 151.097 130.715 1.00 42.06  ? 510  GLU B CD    1 
ATOM   14801 O  OE1   . GLU B 2  510  ? 147.444 151.156 129.491 1.00 46.86  ? 510  GLU B OE1   1 
ATOM   14802 O  OE2   . GLU B 2  510  ? 148.050 150.657 131.536 1.00 40.37  ? 510  GLU B OE2   1 
ATOM   14803 N  N     . ARG B 2  511  ? 146.439 156.114 129.527 1.00 37.20  ? 511  ARG B N     1 
ATOM   14804 C  CA    . ARG B 2  511  ? 145.965 157.370 128.947 1.00 40.40  ? 511  ARG B CA    1 
ATOM   14805 C  C     . ARG B 2  511  ? 145.506 157.142 127.505 1.00 39.76  ? 511  ARG B C     1 
ATOM   14806 O  O     . ARG B 2  511  ? 146.164 157.503 126.528 1.00 35.63  ? 511  ARG B O     1 
ATOM   14807 C  CB    . ARG B 2  511  ? 147.033 158.447 129.056 1.00 37.68  ? 511  ARG B CB    1 
ATOM   14808 C  CG    . ARG B 2  511  ? 148.439 157.957 128.869 1.00 38.78  ? 511  ARG B CG    1 
ATOM   14809 C  CD    . ARG B 2  511  ? 149.409 159.082 129.134 1.00 39.82  ? 511  ARG B CD    1 
ATOM   14810 N  NE    . ARG B 2  511  ? 149.224 159.630 130.471 1.00 40.21  ? 511  ARG B NE    1 
ATOM   14811 C  CZ    . ARG B 2  511  ? 149.029 160.914 130.733 1.00 38.76  ? 511  ARG B CZ    1 
ATOM   14812 N  NH1   . ARG B 2  511  ? 149.049 161.825 129.776 1.00 39.96  ? 511  ARG B NH1   1 
ATOM   14813 N  NH2   . ARG B 2  511  ? 148.815 161.293 131.987 1.00 36.62  ? 511  ARG B NH2   1 
ATOM   14814 N  N     . LYS B 2  512  ? 144.334 156.511 127.398 1.00 39.06  ? 512  LYS B N     1 
ATOM   14815 C  CA    . LYS B 2  512  ? 143.653 156.379 126.115 1.00 38.93  ? 512  LYS B CA    1 
ATOM   14816 C  C     . LYS B 2  512  ? 143.155 157.729 125.610 1.00 38.46  ? 512  LYS B C     1 
ATOM   14817 O  O     . LYS B 2  512  ? 143.257 158.031 124.417 1.00 42.47  ? 512  LYS B O     1 
ATOM   14818 C  CB    . LYS B 2  512  ? 142.508 155.385 126.260 1.00 37.12  ? 512  LYS B CB    1 
ATOM   14819 C  CG    . LYS B 2  512  ? 142.962 153.941 126.278 1.00 37.00  ? 512  LYS B CG    1 
ATOM   14820 C  CD    . LYS B 2  512  ? 142.262 153.198 127.383 1.00 39.30  ? 512  LYS B CD    1 
ATOM   14821 C  CE    . LYS B 2  512  ? 140.949 152.628 126.927 1.00 40.75  ? 512  LYS B CE    1 
ATOM   14822 N  NZ    . LYS B 2  512  ? 141.083 151.284 126.302 1.00 41.35  ? 512  LYS B NZ    1 
ATOM   14823 N  N     . ASN B 2  513  ? 142.606 158.547 126.499 1.00 31.72  ? 513  ASN B N     1 
ATOM   14824 C  CA    . ASN B 2  513  ? 142.332 159.946 126.210 1.00 30.78  ? 513  ASN B CA    1 
ATOM   14825 C  C     . ASN B 2  513  ? 142.280 160.688 127.537 1.00 33.15  ? 513  ASN B C     1 
ATOM   14826 O  O     . ASN B 2  513  ? 142.477 160.103 128.603 1.00 36.00  ? 513  ASN B O     1 
ATOM   14827 C  CB    . ASN B 2  513  ? 141.038 160.125 125.402 1.00 33.72  ? 513  ASN B CB    1 
ATOM   14828 C  CG    . ASN B 2  513  ? 139.846 159.434 126.031 1.00 32.52  ? 513  ASN B CG    1 
ATOM   14829 O  OD1   . ASN B 2  513  ? 139.939 158.865 127.106 1.00 33.97  ? 513  ASN B OD1   1 
ATOM   14830 N  ND2   . ASN B 2  513  ? 138.721 159.478 125.353 1.00 28.93  ? 513  ASN B ND2   1 
ATOM   14831 N  N     . LEU B 2  514  ? 142.017 161.992 127.471 1.00 29.23  ? 514  LEU B N     1 
ATOM   14832 C  CA    . LEU B 2  514  ? 141.925 162.775 128.697 1.00 29.46  ? 514  LEU B CA    1 
ATOM   14833 C  C     . LEU B 2  514  ? 140.740 162.352 129.554 1.00 31.07  ? 514  LEU B C     1 
ATOM   14834 O  O     . LEU B 2  514  ? 140.842 162.344 130.785 1.00 36.33  ? 514  LEU B O     1 
ATOM   14835 C  CB    . LEU B 2  514  ? 141.835 164.260 128.369 1.00 31.40  ? 514  LEU B CB    1 
ATOM   14836 C  CG    . LEU B 2  514  ? 143.049 164.846 127.660 1.00 32.75  ? 514  LEU B CG    1 
ATOM   14837 C  CD1   . LEU B 2  514  ? 142.633 166.063 126.877 1.00 33.10  ? 514  LEU B CD1   1 
ATOM   14838 C  CD2   . LEU B 2  514  ? 144.119 165.192 128.655 1.00 33.92  ? 514  LEU B CD2   1 
ATOM   14839 N  N     . LEU B 2  515  ? 139.610 162.014 128.932 1.00 25.35  ? 515  LEU B N     1 
ATOM   14840 C  CA    . LEU B 2  515  ? 138.450 161.580 129.700 1.00 24.40  ? 515  LEU B CA    1 
ATOM   14841 C  C     . LEU B 2  515  ? 138.764 160.331 130.507 1.00 24.11  ? 515  LEU B C     1 
ATOM   14842 O  O     . LEU B 2  515  ? 138.370 160.225 131.671 1.00 28.51  ? 515  LEU B O     1 
ATOM   14843 C  CB    . LEU B 2  515  ? 137.264 161.325 128.770 1.00 25.70  ? 515  LEU B CB    1 
ATOM   14844 C  CG    . LEU B 2  515  ? 135.931 160.972 129.433 1.00 22.70  ? 515  LEU B CG    1 
ATOM   14845 C  CD1   . LEU B 2  515  ? 135.366 162.159 130.182 1.00 21.63  ? 515  LEU B CD1   1 
ATOM   14846 C  CD2   . LEU B 2  515  ? 134.942 160.443 128.426 1.00 22.11  ? 515  LEU B CD2   1 
ATOM   14847 N  N     . ASN B 2  516  ? 139.470 159.373 129.907 1.00 31.01  ? 516  ASN B N     1 
ATOM   14848 C  CA    . ASN B 2  516  ? 139.854 158.170 130.638 1.00 34.43  ? 516  ASN B CA    1 
ATOM   14849 C  C     . ASN B 2  516  ? 140.803 158.499 131.782 1.00 36.63  ? 516  ASN B C     1 
ATOM   14850 O  O     . ASN B 2  516  ? 140.715 157.905 132.861 1.00 32.08  ? 516  ASN B O     1 
ATOM   14851 C  CB    . ASN B 2  516  ? 140.495 157.155 129.695 1.00 30.97  ? 516  ASN B CB    1 
ATOM   14852 C  CG    . ASN B 2  516  ? 140.489 155.756 130.263 1.00 33.29  ? 516  ASN B CG    1 
ATOM   14853 O  OD1   . ASN B 2  516  ? 139.553 155.357 130.950 1.00 30.48  ? 516  ASN B OD1   1 
ATOM   14854 N  ND2   . ASN B 2  516  ? 141.546 155.009 130.000 1.00 33.38  ? 516  ASN B ND2   1 
ATOM   14855 N  N     . THR B 2  517  ? 141.722 159.441 131.562 1.00 35.38  ? 517  THR B N     1 
ATOM   14856 C  CA    . THR B 2  517  ? 142.638 159.855 132.619 1.00 33.00  ? 517  THR B CA    1 
ATOM   14857 C  C     . THR B 2  517  ? 141.879 160.428 133.809 1.00 33.36  ? 517  THR B C     1 
ATOM   14858 O  O     . THR B 2  517  ? 142.129 160.053 134.960 1.00 33.97  ? 517  THR B O     1 
ATOM   14859 C  CB    . THR B 2  517  ? 143.638 160.877 132.068 1.00 29.89  ? 517  THR B CB    1 
ATOM   14860 O  OG1   . THR B 2  517  ? 144.701 160.201 131.389 1.00 31.73  ? 517  THR B OG1   1 
ATOM   14861 C  CG2   . THR B 2  517  ? 144.224 161.721 133.177 1.00 31.28  ? 517  THR B CG2   1 
ATOM   14862 N  N     . ILE B 2  518  ? 140.932 161.330 133.550 1.00 27.26  ? 518  ILE B N     1 
ATOM   14863 C  CA    . ILE B 2  518  ? 140.174 161.933 134.641 1.00 25.44  ? 518  ILE B CA    1 
ATOM   14864 C  C     . ILE B 2  518  ? 139.263 160.905 135.301 1.00 27.13  ? 518  ILE B C     1 
ATOM   14865 O  O     . ILE B 2  518  ? 139.069 160.924 136.520 1.00 33.43  ? 518  ILE B O     1 
ATOM   14866 C  CB    . ILE B 2  518  ? 139.390 163.158 134.136 1.00 27.89  ? 518  ILE B CB    1 
ATOM   14867 C  CG1   . ILE B 2  518  ? 140.310 164.369 134.045 1.00 30.51  ? 518  ILE B CG1   1 
ATOM   14868 C  CG2   . ILE B 2  518  ? 138.221 163.473 135.045 1.00 28.23  ? 518  ILE B CG2   1 
ATOM   14869 C  CD1   . ILE B 2  518  ? 139.574 165.689 133.944 1.00 31.89  ? 518  ILE B CD1   1 
ATOM   14870 N  N     . SER B 2  519  ? 138.690 159.991 134.519 1.00 22.24  ? 519  SER B N     1 
ATOM   14871 C  CA    . SER B 2  519  ? 137.773 159.011 135.086 1.00 23.06  ? 519  SER B CA    1 
ATOM   14872 C  C     . SER B 2  519  ? 138.500 157.941 135.891 1.00 30.96  ? 519  SER B C     1 
ATOM   14873 O  O     . SER B 2  519  ? 137.898 157.324 136.774 1.00 24.61  ? 519  SER B O     1 
ATOM   14874 C  CB    . SER B 2  519  ? 136.950 158.362 133.978 1.00 26.36  ? 519  SER B CB    1 
ATOM   14875 O  OG    . SER B 2  519  ? 137.457 157.082 133.668 1.00 32.23  ? 519  SER B OG    1 
ATOM   14876 N  N     . ALA B 2  520  ? 139.777 157.685 135.591 1.00 33.61  ? 520  ALA B N     1 
ATOM   14877 C  CA    . ALA B 2  520  ? 140.537 156.723 136.382 1.00 27.67  ? 520  ALA B CA    1 
ATOM   14878 C  C     . ALA B 2  520  ? 140.862 157.261 137.766 1.00 27.56  ? 520  ALA B C     1 
ATOM   14879 O  O     . ALA B 2  520  ? 141.080 156.478 138.694 1.00 33.22  ? 520  ALA B O     1 
ATOM   14880 C  CB    . ALA B 2  520  ? 141.820 156.332 135.654 1.00 27.28  ? 520  ALA B CB    1 
ATOM   14881 N  N     . LEU B 2  521  ? 140.910 158.583 137.922 1.00 27.96  ? 521  LEU B N     1 
ATOM   14882 C  CA    . LEU B 2  521  ? 141.175 159.200 139.213 1.00 27.96  ? 521  LEU B CA    1 
ATOM   14883 C  C     . LEU B 2  521  ? 139.919 159.433 140.039 1.00 32.75  ? 521  LEU B C     1 
ATOM   14884 O  O     . LEU B 2  521  ? 140.032 159.851 141.194 1.00 34.06  ? 521  LEU B O     1 
ATOM   14885 C  CB    . LEU B 2  521  ? 141.904 160.531 139.028 1.00 28.11  ? 521  LEU B CB    1 
ATOM   14886 C  CG    . LEU B 2  521  ? 143.288 160.521 138.381 1.00 32.49  ? 521  LEU B CG    1 
ATOM   14887 C  CD1   . LEU B 2  521  ? 143.678 161.917 137.954 1.00 29.64  ? 521  LEU B CD1   1 
ATOM   14888 C  CD2   . LEU B 2  521  ? 144.311 159.962 139.336 1.00 30.12  ? 521  LEU B CD2   1 
ATOM   14889 N  N     . ARG B 2  522  ? 138.732 159.191 139.486 1.00 31.05  ? 522  ARG B N     1 
ATOM   14890 C  CA    . ARG B 2  522  ? 137.488 159.301 140.234 1.00 23.96  ? 522  ARG B CA    1 
ATOM   14891 C  C     . ARG B 2  522  ? 136.802 157.951 140.401 1.00 24.71  ? 522  ARG B C     1 
ATOM   14892 O  O     . ARG B 2  522  ? 135.608 157.900 140.697 1.00 22.60  ? 522  ARG B O     1 
ATOM   14893 C  CB    . ARG B 2  522  ? 136.546 160.297 139.561 1.00 21.42  ? 522  ARG B CB    1 
ATOM   14894 C  CG    . ARG B 2  522  ? 137.020 161.732 139.608 1.00 25.60  ? 522  ARG B CG    1 
ATOM   14895 C  CD    . ARG B 2  522  ? 136.171 162.644 138.745 1.00 22.51  ? 522  ARG B CD    1 
ATOM   14896 N  NE    . ARG B 2  522  ? 134.852 162.868 139.322 1.00 25.72  ? 522  ARG B NE    1 
ATOM   14897 C  CZ    . ARG B 2  522  ? 134.557 163.856 140.153 1.00 27.15  ? 522  ARG B CZ    1 
ATOM   14898 N  NH1   . ARG B 2  522  ? 135.459 164.753 140.505 1.00 29.04  ? 522  ARG B NH1   1 
ATOM   14899 N  NH2   . ARG B 2  522  ? 133.330 163.942 140.651 1.00 22.14  ? 522  ARG B NH2   1 
ATOM   14900 N  N     . THR B 2  523  ? 137.535 156.860 140.221 1.00 26.16  ? 523  THR B N     1 
ATOM   14901 C  CA    . THR B 2  523  ? 136.985 155.515 140.282 1.00 27.46  ? 523  THR B CA    1 
ATOM   14902 C  C     . THR B 2  523  ? 137.079 154.987 141.707 1.00 32.31  ? 523  THR B C     1 
ATOM   14903 O  O     . THR B 2  523  ? 138.127 155.099 142.346 1.00 38.32  ? 523  THR B O     1 
ATOM   14904 C  CB    . THR B 2  523  ? 137.729 154.579 139.326 1.00 30.75  ? 523  THR B CB    1 
ATOM   14905 O  OG1   . THR B 2  523  ? 137.320 154.840 137.979 1.00 31.51  ? 523  THR B OG1   1 
ATOM   14906 C  CG2   . THR B 2  523  ? 137.429 153.132 139.646 1.00 27.28  ? 523  THR B CG2   1 
ATOM   14907 N  N     . VAL B 2  524  ? 135.982 154.426 142.201 1.00 26.74  ? 524  VAL B N     1 
ATOM   14908 C  CA    . VAL B 2  524  ? 135.921 153.814 143.521 1.00 23.76  ? 524  VAL B CA    1 
ATOM   14909 C  C     . VAL B 2  524  ? 135.874 152.306 143.348 1.00 26.40  ? 524  VAL B C     1 
ATOM   14910 O  O     . VAL B 2  524  ? 134.984 151.779 142.671 1.00 32.28  ? 524  VAL B O     1 
ATOM   14911 C  CB    . VAL B 2  524  ? 134.700 154.315 144.307 1.00 28.13  ? 524  VAL B CB    1 
ATOM   14912 C  CG1   . VAL B 2  524  ? 134.650 153.662 145.664 1.00 28.65  ? 524  VAL B CG1   1 
ATOM   14913 C  CG2   . VAL B 2  524  ? 134.743 155.815 144.439 1.00 21.45  ? 524  VAL B CG2   1 
ATOM   14914 N  N     . ASN B 2  525  ? 136.814 151.605 143.972 1.00 34.12  ? 525  ASN B N     1 
ATOM   14915 C  CA    . ASN B 2  525  ? 136.954 150.169 143.792 1.00 33.53  ? 525  ASN B CA    1 
ATOM   14916 C  C     . ASN B 2  525  ? 136.606 149.431 145.074 1.00 36.67  ? 525  ASN B C     1 
ATOM   14917 O  O     . ASN B 2  525  ? 136.812 149.935 146.179 1.00 36.89  ? 525  ASN B O     1 
ATOM   14918 C  CB    . ASN B 2  525  ? 138.366 149.802 143.351 1.00 32.74  ? 525  ASN B CB    1 
ATOM   14919 C  CG    . ASN B 2  525  ? 138.553 149.922 141.860 1.00 36.43  ? 525  ASN B CG    1 
ATOM   14920 O  OD1   . ASN B 2  525  ? 137.824 149.311 141.084 1.00 40.11  ? 525  ASN B OD1   1 
ATOM   14921 N  ND2   . ASN B 2  525  ? 139.536 150.705 141.449 1.00 34.09  ? 525  ASN B ND2   1 
ATOM   14922 N  N     . THR B 2  526  ? 136.063 148.232 144.906 1.00 38.00  ? 526  THR B N     1 
ATOM   14923 C  CA    . THR B 2  526  ? 135.679 147.385 146.025 1.00 37.35  ? 526  THR B CA    1 
ATOM   14924 C  C     . THR B 2  526  ? 136.893 146.712 146.658 1.00 39.00  ? 526  THR B C     1 
ATOM   14925 O  O     . THR B 2  526  ? 137.505 145.824 146.072 1.00 38.20  ? 526  THR B O     1 
ATOM   14926 C  CB    . THR B 2  526  ? 134.676 146.312 145.582 1.00 35.92  ? 526  THR B CB    1 
ATOM   14927 O  OG1   . THR B 2  526  ? 135.005 145.871 144.260 1.00 40.43  ? 526  THR B OG1   1 
ATOM   14928 C  CG2   . THR B 2  526  ? 133.267 146.872 145.579 1.00 35.85  ? 526  THR B CG2   1 
ATOM   14929 N  N     . GLU B 2  537  ? 124.537 134.942 146.154 1.00 59.49  ? 537  GLU B N     1 
ATOM   14930 C  CA    . GLU B 2  537  ? 123.665 136.041 145.760 1.00 60.05  ? 537  GLU B CA    1 
ATOM   14931 C  C     . GLU B 2  537  ? 124.261 137.371 146.196 1.00 59.80  ? 537  GLU B C     1 
ATOM   14932 O  O     . GLU B 2  537  ? 123.804 138.433 145.784 1.00 60.98  ? 537  GLU B O     1 
ATOM   14933 C  CB    . GLU B 2  537  ? 122.275 135.863 146.361 1.00 58.55  ? 537  GLU B CB    1 
ATOM   14934 C  CG    . GLU B 2  537  ? 122.260 135.778 147.872 1.00 58.61  ? 537  GLU B CG    1 
ATOM   14935 C  CD    . GLU B 2  537  ? 120.977 135.157 148.400 1.00 61.99  ? 537  GLU B CD    1 
ATOM   14936 O  OE1   . GLU B 2  537  ? 120.127 134.755 147.577 1.00 62.93  ? 537  GLU B OE1   1 
ATOM   14937 O  OE2   . GLU B 2  537  ? 120.817 135.073 149.636 1.00 60.01  ? 537  GLU B OE2   1 
ATOM   14938 N  N     . ARG B 2  538  ? 125.281 137.295 147.054 1.00 48.74  ? 538  ARG B N     1 
ATOM   14939 C  CA    . ARG B 2  538  ? 126.006 138.493 147.461 1.00 45.01  ? 538  ARG B CA    1 
ATOM   14940 C  C     . ARG B 2  538  ? 126.710 139.136 146.274 1.00 46.43  ? 538  ARG B C     1 
ATOM   14941 O  O     . ARG B 2  538  ? 126.638 140.357 146.080 1.00 46.18  ? 538  ARG B O     1 
ATOM   14942 C  CB    . ARG B 2  538  ? 127.014 138.135 148.553 1.00 45.09  ? 538  ARG B CB    1 
ATOM   14943 C  CG    . ARG B 2  538  ? 127.856 139.292 149.041 1.00 48.05  ? 538  ARG B CG    1 
ATOM   14944 C  CD    . ARG B 2  538  ? 127.346 139.831 150.366 1.00 47.41  ? 538  ARG B CD    1 
ATOM   14945 N  NE    . ARG B 2  538  ? 126.334 140.858 150.164 1.00 47.67  ? 538  ARG B NE    1 
ATOM   14946 C  CZ    . ARG B 2  538  ? 126.599 142.115 149.842 1.00 47.09  ? 538  ARG B CZ    1 
ATOM   14947 N  NH1   . ARG B 2  538  ? 127.841 142.542 149.693 1.00 45.35  ? 538  ARG B NH1   1 
ATOM   14948 N  NH2   . ARG B 2  538  ? 125.592 142.961 149.656 1.00 44.98  ? 538  ARG B NH2   1 
ATOM   14949 N  N     . ALA B 2  539  ? 127.372 138.316 145.454 1.00 43.89  ? 539  ALA B N     1 
ATOM   14950 C  CA    . ALA B 2  539  ? 128.143 138.811 144.321 1.00 46.05  ? 539  ALA B CA    1 
ATOM   14951 C  C     . ALA B 2  539  ? 127.268 139.475 143.271 1.00 43.76  ? 539  ALA B C     1 
ATOM   14952 O  O     . ALA B 2  539  ? 127.785 140.212 142.427 1.00 43.37  ? 539  ALA B O     1 
ATOM   14953 C  CB    . ALA B 2  539  ? 128.937 137.665 143.689 1.00 43.84  ? 539  ALA B CB    1 
ATOM   14954 N  N     . ASP B 2  540  ? 125.964 139.219 143.293 1.00 43.29  ? 540  ASP B N     1 
ATOM   14955 C  CA    . ASP B 2  540  ? 125.035 139.855 142.375 1.00 45.55  ? 540  ASP B CA    1 
ATOM   14956 C  C     . ASP B 2  540  ? 124.291 141.015 143.007 1.00 48.72  ? 540  ASP B C     1 
ATOM   14957 O  O     . ASP B 2  540  ? 124.079 142.034 142.341 1.00 46.41  ? 540  ASP B O     1 
ATOM   14958 C  CB    . ASP B 2  540  ? 124.019 138.830 141.872 1.00 44.65  ? 540  ASP B CB    1 
ATOM   14959 C  CG    . ASP B 2  540  ? 124.571 137.976 140.761 1.00 50.19  ? 540  ASP B CG    1 
ATOM   14960 O  OD1   . ASP B 2  540  ? 125.320 138.507 139.915 1.00 49.99  ? 540  ASP B OD1   1 
ATOM   14961 O  OD2   . ASP B 2  540  ? 124.288 136.761 140.763 1.00 49.54  ? 540  ASP B OD2   1 
ATOM   14962 N  N     . MET B 2  541  ? 123.908 140.878 144.276 1.00 49.11  ? 541  MET B N     1 
ATOM   14963 C  CA    . MET B 2  541  ? 123.243 141.957 144.994 1.00 43.65  ? 541  MET B CA    1 
ATOM   14964 C  C     . MET B 2  541  ? 124.159 143.159 145.175 1.00 46.30  ? 541  MET B C     1 
ATOM   14965 O  O     . MET B 2  541  ? 123.676 144.287 145.307 1.00 45.41  ? 541  MET B O     1 
ATOM   14966 C  CB    . MET B 2  541  ? 122.754 141.436 146.344 1.00 44.19  ? 541  MET B CB    1 
ATOM   14967 C  CG    . MET B 2  541  ? 121.759 142.314 147.071 1.00 47.05  ? 541  MET B CG    1 
ATOM   14968 S  SD    . MET B 2  541  ? 120.230 142.608 146.176 1.00 55.75  ? 541  MET B SD    1 
ATOM   14969 C  CE    . MET B 2  541  ? 120.139 144.389 146.288 1.00 45.74  ? 541  MET B CE    1 
ATOM   14970 N  N     . MET B 2  542  ? 125.472 142.945 145.190 1.00 48.69  ? 542  MET B N     1 
ATOM   14971 C  CA    . MET B 2  542  ? 126.414 144.040 145.386 1.00 45.34  ? 542  MET B CA    1 
ATOM   14972 C  C     . MET B 2  542  ? 126.725 144.812 144.112 1.00 45.03  ? 542  MET B C     1 
ATOM   14973 O  O     . MET B 2  542  ? 127.393 145.847 144.184 1.00 45.96  ? 542  MET B O     1 
ATOM   14974 C  CB    . MET B 2  542  ? 127.709 143.507 146.006 1.00 45.84  ? 542  MET B CB    1 
ATOM   14975 C  CG    . MET B 2  542  ? 128.772 143.068 145.024 1.00 44.31  ? 542  MET B CG    1 
ATOM   14976 S  SD    . MET B 2  542  ? 129.733 141.744 145.770 1.00 57.17  ? 542  MET B SD    1 
ATOM   14977 C  CE    . MET B 2  542  ? 131.226 141.814 144.801 1.00 45.07  ? 542  MET B CE    1 
ATOM   14978 N  N     . ARG B 2  543  ? 126.252 144.352 142.957 1.00 43.19  ? 543  ARG B N     1 
ATOM   14979 C  CA    . ARG B 2  543  ? 126.432 145.058 141.698 1.00 40.60  ? 543  ARG B CA    1 
ATOM   14980 C  C     . ARG B 2  543  ? 125.203 145.861 141.293 1.00 40.59  ? 543  ARG B C     1 
ATOM   14981 O  O     . ARG B 2  543  ? 125.183 146.430 140.200 1.00 41.77  ? 543  ARG B O     1 
ATOM   14982 C  CB    . ARG B 2  543  ? 126.796 144.064 140.595 1.00 39.50  ? 543  ARG B CB    1 
ATOM   14983 C  CG    . ARG B 2  543  ? 127.860 143.090 141.017 1.00 40.78  ? 543  ARG B CG    1 
ATOM   14984 C  CD    . ARG B 2  543  ? 128.369 142.254 139.878 1.00 39.28  ? 543  ARG B CD    1 
ATOM   14985 N  NE    . ARG B 2  543  ? 128.935 140.999 140.357 1.00 42.44  ? 543  ARG B NE    1 
ATOM   14986 C  CZ    . ARG B 2  543  ? 130.065 140.469 139.911 1.00 45.12  ? 543  ARG B CZ    1 
ATOM   14987 N  NH1   . ARG B 2  543  ? 130.801 141.077 138.998 1.00 39.97  ? 543  ARG B NH1   1 
ATOM   14988 N  NH2   . ARG B 2  543  ? 130.474 139.306 140.406 1.00 44.54  ? 543  ARG B NH2   1 
ATOM   14989 N  N     . ARG B 2  544  ? 124.192 145.928 142.150 1.00 35.28  ? 544  ARG B N     1 
ATOM   14990 C  CA    . ARG B 2  544  ? 122.949 146.621 141.868 1.00 32.17  ? 544  ARG B CA    1 
ATOM   14991 C  C     . ARG B 2  544  ? 123.169 148.132 141.880 1.00 31.25  ? 544  ARG B C     1 
ATOM   14992 O  O     . ARG B 2  544  ? 124.238 148.630 142.230 1.00 35.94  ? 544  ARG B O     1 
ATOM   14993 C  CB    . ARG B 2  544  ? 121.898 146.241 142.905 1.00 35.04  ? 544  ARG B CB    1 
ATOM   14994 C  CG    . ARG B 2  544  ? 121.475 144.793 142.902 1.00 32.32  ? 544  ARG B CG    1 
ATOM   14995 C  CD    . ARG B 2  544  ? 120.360 144.527 141.936 1.00 33.04  ? 544  ARG B CD    1 
ATOM   14996 N  NE    . ARG B 2  544  ? 119.372 143.611 142.494 1.00 36.30  ? 544  ARG B NE    1 
ATOM   14997 C  CZ    . ARG B 2  544  ? 119.563 142.311 142.676 1.00 38.41  ? 544  ARG B CZ    1 
ATOM   14998 N  NH1   . ARG B 2  544  ? 120.695 141.720 142.327 1.00 35.97  ? 544  ARG B NH1   1 
ATOM   14999 N  NH2   . ARG B 2  544  ? 118.591 141.582 143.215 1.00 32.94  ? 544  ARG B NH2   1 
ATOM   15000 N  N     . VAL B 2  545  ? 122.134 148.872 141.504 1.00 25.64  ? 545  VAL B N     1 
ATOM   15001 C  CA    . VAL B 2  545  ? 122.067 150.311 141.712 1.00 18.56  ? 545  VAL B CA    1 
ATOM   15002 C  C     . VAL B 2  545  ? 121.315 150.517 143.016 1.00 18.37  ? 545  VAL B C     1 
ATOM   15003 O  O     . VAL B 2  545  ? 120.112 150.254 143.093 1.00 26.81  ? 545  VAL B O     1 
ATOM   15004 C  CB    . VAL B 2  545  ? 121.372 151.030 140.547 1.00 20.27  ? 545  VAL B CB    1 
ATOM   15005 C  CG1   . VAL B 2  545  ? 121.145 152.497 140.884 1.00 20.23  ? 545  VAL B CG1   1 
ATOM   15006 C  CG2   . VAL B 2  545  ? 122.172 150.888 139.271 1.00 20.23  ? 545  VAL B CG2   1 
ATOM   15007 N  N     . HIS B 2  546  ? 122.016 150.960 144.052 1.00 19.14  ? 546  HIS B N     1 
ATOM   15008 C  CA    . HIS B 2  546  ? 121.412 151.113 145.363 1.00 17.32  ? 546  HIS B CA    1 
ATOM   15009 C  C     . HIS B 2  546  ? 120.718 152.463 145.483 1.00 14.53  ? 546  HIS B C     1 
ATOM   15010 O  O     . HIS B 2  546  ? 121.064 153.423 144.797 1.00 21.04  ? 546  HIS B O     1 
ATOM   15011 C  CB    . HIS B 2  546  ? 122.458 150.951 146.467 1.00 16.36  ? 546  HIS B CB    1 
ATOM   15012 C  CG    . HIS B 2  546  ? 121.863 150.707 147.818 1.00 20.66  ? 546  HIS B CG    1 
ATOM   15013 N  ND1   . HIS B 2  546  ? 121.623 151.722 148.716 1.00 17.54  ? 546  HIS B ND1   1 
ATOM   15014 C  CD2   . HIS B 2  546  ? 121.426 149.572 148.409 1.00 23.63  ? 546  HIS B CD2   1 
ATOM   15015 C  CE1   . HIS B 2  546  ? 121.066 151.223 149.802 1.00 17.13  ? 546  HIS B CE1   1 
ATOM   15016 N  NE2   . HIS B 2  546  ? 120.945 149.919 149.646 1.00 22.50  ? 546  HIS B NE2   1 
ATOM   15017 N  N     . ALA B 2  547  ? 119.727 152.523 146.372 1.00 7.58   ? 547  ALA B N     1 
ATOM   15018 C  CA    . ALA B 2  547  ? 118.943 153.734 146.579 1.00 10.68  ? 547  ALA B CA    1 
ATOM   15019 C  C     . ALA B 2  547  ? 119.739 154.866 147.209 1.00 14.31  ? 547  ALA B C     1 
ATOM   15020 O  O     . ALA B 2  547  ? 119.253 156.000 147.236 1.00 16.34  ? 547  ALA B O     1 
ATOM   15021 C  CB    . ALA B 2  547  ? 117.730 153.429 147.448 1.00 12.35  ? 547  ALA B CB    1 
ATOM   15022 N  N     . SER B 2  548  ? 120.931 154.591 147.719 1.00 13.28  ? 548  SER B N     1 
ATOM   15023 C  CA    . SER B 2  548  ? 121.772 155.607 148.324 1.00 13.21  ? 548  SER B CA    1 
ATOM   15024 C  C     . SER B 2  548  ? 122.723 156.261 147.333 1.00 13.52  ? 548  SER B C     1 
ATOM   15025 O  O     . SER B 2  548  ? 123.385 157.237 147.689 1.00 18.75  ? 548  SER B O     1 
ATOM   15026 C  CB    . SER B 2  548  ? 122.564 154.995 149.483 1.00 19.85  ? 548  SER B CB    1 
ATOM   15027 O  OG    . SER B 2  548  ? 123.352 153.909 149.039 1.00 22.44  ? 548  SER B OG    1 
ATOM   15028 N  N     . TYR B 2  549  ? 122.797 155.752 146.107 1.00 15.14  ? 549  TYR B N     1 
ATOM   15029 C  CA    . TYR B 2  549  ? 123.727 156.291 145.115 1.00 10.33  ? 549  TYR B CA    1 
ATOM   15030 C  C     . TYR B 2  549  ? 123.413 157.711 144.666 1.00 8.88   ? 549  TYR B C     1 
ATOM   15031 O  O     . TYR B 2  549  ? 124.340 158.535 144.649 1.00 13.52  ? 549  TYR B O     1 
ATOM   15032 C  CB    . TYR B 2  549  ? 123.785 155.356 143.908 1.00 7.48   ? 549  TYR B CB    1 
ATOM   15033 C  CG    . TYR B 2  549  ? 124.547 154.089 144.155 1.00 14.42  ? 549  TYR B CG    1 
ATOM   15034 C  CD1   . TYR B 2  549  ? 124.852 153.229 143.120 1.00 15.76  ? 549  TYR B CD1   1 
ATOM   15035 C  CD2   . TYR B 2  549  ? 124.964 153.750 145.427 1.00 15.15  ? 549  TYR B CD2   1 
ATOM   15036 C  CE1   . TYR B 2  549  ? 125.542 152.074 143.347 1.00 12.24  ? 549  TYR B CE1   1 
ATOM   15037 C  CE2   . TYR B 2  549  ? 125.654 152.597 145.662 1.00 17.66  ? 549  TYR B CE2   1 
ATOM   15038 C  CZ    . TYR B 2  549  ? 125.941 151.766 144.622 1.00 18.52  ? 549  TYR B CZ    1 
ATOM   15039 O  OH    . TYR B 2  549  ? 126.629 150.613 144.871 1.00 23.96  ? 549  TYR B OH    1 
ATOM   15040 N  N     . PRO B 2  550  ? 122.166 158.071 144.269 1.00 6.37   ? 550  PRO B N     1 
ATOM   15041 C  CA    . PRO B 2  550  ? 121.955 159.338 143.554 1.00 8.01   ? 550  PRO B CA    1 
ATOM   15042 C  C     . PRO B 2  550  ? 122.544 160.587 144.182 1.00 6.24   ? 550  PRO B C     1 
ATOM   15043 O  O     . PRO B 2  550  ? 122.150 161.016 145.268 1.00 11.68  ? 550  PRO B O     1 
ATOM   15044 C  CB    . PRO B 2  550  ? 120.425 159.431 143.465 1.00 6.23   ? 550  PRO B CB    1 
ATOM   15045 C  CG    . PRO B 2  550  ? 119.904 158.361 144.311 1.00 8.28   ? 550  PRO B CG    1 
ATOM   15046 C  CD    . PRO B 2  550  ? 120.918 157.299 144.296 1.00 9.06   ? 550  PRO B CD    1 
ATOM   15047 N  N     . GLY B 2  551  ? 123.486 161.193 143.457 1.00 4.26   ? 551  GLY B N     1 
ATOM   15048 C  CA    . GLY B 2  551  ? 124.211 162.357 143.898 1.00 1.76   ? 551  GLY B CA    1 
ATOM   15049 C  C     . GLY B 2  551  ? 125.640 162.065 144.302 1.00 4.79   ? 551  GLY B C     1 
ATOM   15050 O  O     . GLY B 2  551  ? 126.474 162.971 144.282 1.00 6.86   ? 551  GLY B O     1 
ATOM   15051 N  N     . TYR B 2  552  ? 125.938 160.824 144.663 1.00 6.56   ? 552  TYR B N     1 
ATOM   15052 C  CA    . TYR B 2  552  ? 127.268 160.423 145.093 1.00 6.27   ? 552  TYR B CA    1 
ATOM   15053 C  C     . TYR B 2  552  ? 127.937 159.458 144.136 1.00 9.07   ? 552  TYR B C     1 
ATOM   15054 O  O     . TYR B 2  552  ? 129.118 159.616 143.842 1.00 15.11  ? 552  TYR B O     1 
ATOM   15055 C  CB    . TYR B 2  552  ? 127.202 159.803 146.498 1.00 8.20   ? 552  TYR B CB    1 
ATOM   15056 C  CG    . TYR B 2  552  ? 126.450 160.675 147.471 1.00 3.27   ? 552  TYR B CG    1 
ATOM   15057 C  CD1   . TYR B 2  552  ? 127.039 161.797 148.018 1.00 15.71  ? 552  TYR B CD1   1 
ATOM   15058 C  CD2   . TYR B 2  552  ? 125.149 160.386 147.824 1.00 3.27   ? 552  TYR B CD2   1 
ATOM   15059 C  CE1   . TYR B 2  552  ? 126.354 162.597 148.875 1.00 4.44   ? 552  TYR B CE1   1 
ATOM   15060 C  CE2   . TYR B 2  552  ? 124.466 161.179 148.682 1.00 4.20   ? 552  TYR B CE2   1 
ATOM   15061 C  CZ    . TYR B 2  552  ? 125.071 162.283 149.203 1.00 3.15   ? 552  TYR B CZ    1 
ATOM   15062 O  OH    . TYR B 2  552  ? 124.378 163.082 150.067 1.00 0.57   ? 552  TYR B OH    1 
ATOM   15063 N  N     . ILE B 2  553  ? 127.211 158.467 143.641 1.00 6.45   ? 553  ILE B N     1 
ATOM   15064 C  CA    . ILE B 2  553  ? 127.717 157.513 142.665 1.00 4.83   ? 553  ILE B CA    1 
ATOM   15065 C  C     . ILE B 2  553  ? 126.896 157.665 141.396 1.00 9.76   ? 553  ILE B C     1 
ATOM   15066 O  O     . ILE B 2  553  ? 125.671 157.790 141.457 1.00 23.67  ? 553  ILE B O     1 
ATOM   15067 C  CB    . ILE B 2  553  ? 127.656 156.071 143.205 1.00 8.16   ? 553  ILE B CB    1 
ATOM   15068 C  CG1   . ILE B 2  553  ? 128.379 155.960 144.550 1.00 9.01   ? 553  ILE B CG1   1 
ATOM   15069 C  CG2   . ILE B 2  553  ? 128.219 155.086 142.206 1.00 8.03   ? 553  ILE B CG2   1 
ATOM   15070 C  CD1   . ILE B 2  553  ? 129.854 156.203 144.471 1.00 5.62   ? 553  ILE B CD1   1 
ATOM   15071 N  N     . CYS B 2  554  ? 127.572 157.700 140.251 1.00 8.44   ? 554  CYS B N     1 
ATOM   15072 C  CA    . CYS B 2  554  ? 126.879 157.818 138.974 1.00 6.53   ? 554  CYS B CA    1 
ATOM   15073 C  C     . CYS B 2  554  ? 125.940 156.639 138.775 1.00 5.88   ? 554  CYS B C     1 
ATOM   15074 O  O     . CYS B 2  554  ? 126.327 155.486 138.973 1.00 11.67  ? 554  CYS B O     1 
ATOM   15075 C  CB    . CYS B 2  554  ? 127.891 157.893 137.834 1.00 9.91   ? 554  CYS B CB    1 
ATOM   15076 S  SG    . CYS B 2  554  ? 127.172 157.963 136.180 1.00 12.58  ? 554  CYS B SG    1 
ATOM   15077 N  N     . VAL B 2  555  ? 124.702 156.928 138.374 1.00 6.53   ? 555  VAL B N     1 
ATOM   15078 C  CA    . VAL B 2  555  ? 123.701 155.873 138.281 1.00 10.08  ? 555  VAL B CA    1 
ATOM   15079 C  C     . VAL B 2  555  ? 123.867 155.066 137.005 1.00 13.73  ? 555  VAL B C     1 
ATOM   15080 O  O     . VAL B 2  555  ? 123.348 153.951 136.900 1.00 20.91  ? 555  VAL B O     1 
ATOM   15081 C  CB    . VAL B 2  555  ? 122.285 156.462 138.391 1.00 8.15   ? 555  VAL B CB    1 
ATOM   15082 C  CG1   . VAL B 2  555  ? 121.958 156.784 139.835 1.00 9.33   ? 555  VAL B CG1   1 
ATOM   15083 C  CG2   . VAL B 2  555  ? 122.169 157.693 137.541 1.00 8.83   ? 555  VAL B CG2   1 
ATOM   15084 N  N     . ALA B 2  556  ? 124.597 155.594 136.026 1.00 15.80  ? 556  ALA B N     1 
ATOM   15085 C  CA    . ALA B 2  556  ? 124.686 154.938 134.731 1.00 14.06  ? 556  ALA B CA    1 
ATOM   15086 C  C     . ALA B 2  556  ? 126.010 154.206 134.550 1.00 14.81  ? 556  ALA B C     1 
ATOM   15087 O  O     . ALA B 2  556  ? 126.048 153.119 133.971 1.00 22.81  ? 556  ALA B O     1 
ATOM   15088 C  CB    . ALA B 2  556  ? 124.483 155.964 133.618 1.00 17.50  ? 556  ALA B CB    1 
ATOM   15089 N  N     . GLN B 2  557  ? 127.102 154.772 135.051 1.00 24.18  ? 557  GLN B N     1 
ATOM   15090 C  CA    . GLN B 2  557  ? 128.428 154.293 134.682 1.00 26.70  ? 557  GLN B CA    1 
ATOM   15091 C  C     . GLN B 2  557  ? 128.792 153.003 135.404 1.00 28.94  ? 557  GLN B C     1 
ATOM   15092 O  O     . GLN B 2  557  ? 128.750 152.929 136.634 1.00 29.59  ? 557  GLN B O     1 
ATOM   15093 C  CB    . GLN B 2  557  ? 129.474 155.364 134.971 1.00 21.85  ? 557  GLN B CB    1 
ATOM   15094 C  CG    . GLN B 2  557  ? 130.911 154.877 134.868 1.00 23.06  ? 557  GLN B CG    1 
ATOM   15095 C  CD    . GLN B 2  557  ? 131.852 155.975 134.427 1.00 29.37  ? 557  GLN B CD    1 
ATOM   15096 O  OE1   . GLN B 2  557  ? 133.044 155.749 134.236 1.00 25.28  ? 557  GLN B OE1   1 
ATOM   15097 N  NE2   . GLN B 2  557  ? 131.314 157.176 134.253 1.00 33.72  ? 557  GLN B NE2   1 
ATOM   15098 N  N     . SER B 2  558  ? 129.164 151.994 134.625 1.00 36.08  ? 558  SER B N     1 
ATOM   15099 C  CA    . SER B 2  558  ? 129.748 150.739 135.091 1.00 36.86  ? 558  SER B CA    1 
ATOM   15100 C  C     . SER B 2  558  ? 130.288 150.017 133.862 1.00 38.35  ? 558  SER B C     1 
ATOM   15101 O  O     . SER B 2  558  ? 130.248 150.549 132.746 1.00 38.52  ? 558  SER B O     1 
ATOM   15102 C  CB    . SER B 2  558  ? 128.734 149.884 135.848 1.00 34.24  ? 558  SER B CB    1 
ATOM   15103 O  OG    . SER B 2  558  ? 127.790 149.310 134.968 1.00 36.07  ? 558  SER B OG    1 
ATOM   15104 N  N     . ALA B 2  559  ? 130.803 148.807 134.060 1.00 38.78  ? 559  ALA B N     1 
ATOM   15105 C  CA    . ALA B 2  559  ? 131.161 147.962 132.933 1.00 39.12  ? 559  ALA B CA    1 
ATOM   15106 C  C     . ALA B 2  559  ? 129.913 147.288 132.374 1.00 40.82  ? 559  ALA B C     1 
ATOM   15107 O  O     . ALA B 2  559  ? 128.871 147.216 133.030 1.00 43.60  ? 559  ALA B O     1 
ATOM   15108 C  CB    . ALA B 2  559  ? 132.194 146.914 133.339 1.00 36.64  ? 559  ALA B CB    1 
ATOM   15109 N  N     . ASP B 2  560  ? 130.018 146.804 131.134 1.00 41.66  ? 560  ASP B N     1 
ATOM   15110 C  CA    . ASP B 2  560  ? 128.869 146.205 130.471 1.00 43.19  ? 560  ASP B CA    1 
ATOM   15111 C  C     . ASP B 2  560  ? 128.999 144.711 130.210 1.00 43.85  ? 560  ASP B C     1 
ATOM   15112 O  O     . ASP B 2  560  ? 127.972 144.046 130.046 1.00 45.98  ? 560  ASP B O     1 
ATOM   15113 C  CB    . ASP B 2  560  ? 128.578 146.925 129.145 1.00 41.23  ? 560  ASP B CB    1 
ATOM   15114 C  CG    . ASP B 2  560  ? 129.827 147.203 128.349 1.00 46.44  ? 560  ASP B CG    1 
ATOM   15115 O  OD1   . ASP B 2  560  ? 130.919 146.786 128.790 1.00 44.54  ? 560  ASP B OD1   1 
ATOM   15116 O  OD2   . ASP B 2  560  ? 129.723 147.860 127.293 1.00 46.68  ? 560  ASP B OD2   1 
ATOM   15117 N  N     . THR B 2  561  ? 130.211 144.163 130.176 1.00 42.22  ? 561  THR B N     1 
ATOM   15118 C  CA    . THR B 2  561  ? 130.390 142.731 129.981 1.00 43.53  ? 561  THR B CA    1 
ATOM   15119 C  C     . THR B 2  561  ? 131.372 142.196 131.012 1.00 45.71  ? 561  THR B C     1 
ATOM   15120 O  O     . THR B 2  561  ? 132.193 142.932 131.565 1.00 47.70  ? 561  THR B O     1 
ATOM   15121 C  CB    . THR B 2  561  ? 130.885 142.378 128.562 1.00 43.82  ? 561  THR B CB    1 
ATOM   15122 O  OG1   . THR B 2  561  ? 132.031 143.169 128.229 1.00 40.52  ? 561  THR B OG1   1 
ATOM   15123 C  CG2   . THR B 2  561  ? 129.795 142.598 127.526 1.00 43.07  ? 561  THR B CG2   1 
ATOM   15124 N  N     . GLY B 2  562  ? 131.273 140.897 131.264 1.00 38.80  ? 562  GLY B N     1 
ATOM   15125 C  CA    . GLY B 2  562  ? 132.190 140.232 132.160 1.00 38.74  ? 562  GLY B CA    1 
ATOM   15126 C  C     . GLY B 2  562  ? 131.813 140.371 133.622 1.00 42.32  ? 562  GLY B C     1 
ATOM   15127 O  O     . GLY B 2  562  ? 130.710 140.778 133.994 1.00 42.86  ? 562  GLY B O     1 
ATOM   15128 N  N     . GLU B 2  563  ? 132.768 139.988 134.467 1.00 47.38  ? 563  GLU B N     1 
ATOM   15129 C  CA    . GLU B 2  563  ? 132.607 140.076 135.911 1.00 46.09  ? 563  GLU B CA    1 
ATOM   15130 C  C     . GLU B 2  563  ? 132.795 141.491 136.435 1.00 48.31  ? 563  GLU B C     1 
ATOM   15131 O  O     . GLU B 2  563  ? 132.375 141.779 137.560 1.00 48.97  ? 563  GLU B O     1 
ATOM   15132 C  CB    . GLU B 2  563  ? 133.597 139.126 136.587 1.00 47.47  ? 563  GLU B CB    1 
ATOM   15133 C  CG    . GLU B 2  563  ? 133.137 138.565 137.916 1.00 48.45  ? 563  GLU B CG    1 
ATOM   15134 C  CD    . GLU B 2  563  ? 134.275 138.349 138.893 1.00 50.00  ? 563  GLU B CD    1 
ATOM   15135 O  OE1   . GLU B 2  563  ? 135.435 138.637 138.540 1.00 48.13  ? 563  GLU B OE1   1 
ATOM   15136 O  OE2   . GLU B 2  563  ? 134.005 137.878 140.017 1.00 50.01  ? 563  GLU B OE2   1 
ATOM   15137 N  N     . LYS B 2  564  ? 133.407 142.377 135.652 1.00 41.70  ? 564  LYS B N     1 
ATOM   15138 C  CA    . LYS B 2  564  ? 133.674 143.746 136.069 1.00 41.24  ? 564  LYS B CA    1 
ATOM   15139 C  C     . LYS B 2  564  ? 132.424 144.611 136.108 1.00 42.64  ? 564  LYS B C     1 
ATOM   15140 O  O     . LYS B 2  564  ? 132.507 145.768 136.535 1.00 38.88  ? 564  LYS B O     1 
ATOM   15141 C  CB    . LYS B 2  564  ? 134.709 144.384 135.140 1.00 43.71  ? 564  LYS B CB    1 
ATOM   15142 C  CG    . LYS B 2  564  ? 135.997 144.800 135.823 1.00 44.30  ? 564  LYS B CG    1 
ATOM   15143 C  CD    . LYS B 2  564  ? 136.761 145.809 134.980 1.00 45.12  ? 564  LYS B CD    1 
ATOM   15144 C  CE    . LYS B 2  564  ? 136.106 147.181 135.036 1.00 44.22  ? 564  LYS B CE    1 
ATOM   15145 N  NZ    . LYS B 2  564  ? 136.781 148.170 134.154 1.00 44.12  ? 564  LYS B NZ    1 
ATOM   15146 N  N     . VAL B 2  565  ? 131.283 144.093 135.655 1.00 42.54  ? 565  VAL B N     1 
ATOM   15147 C  CA    . VAL B 2  565  ? 130.031 144.833 135.731 1.00 41.23  ? 565  VAL B CA    1 
ATOM   15148 C  C     . VAL B 2  565  ? 129.687 145.090 137.192 1.00 39.98  ? 565  VAL B C     1 
ATOM   15149 O  O     . VAL B 2  565  ? 129.815 144.202 138.041 1.00 38.20  ? 565  VAL B O     1 
ATOM   15150 C  CB    . VAL B 2  565  ? 128.913 144.072 134.998 1.00 39.12  ? 565  VAL B CB    1 
ATOM   15151 C  CG1   . VAL B 2  565  ? 128.626 142.733 135.667 1.00 38.00  ? 565  VAL B CG1   1 
ATOM   15152 C  CG2   . VAL B 2  565  ? 127.644 144.904 134.943 1.00 37.73  ? 565  VAL B CG2   1 
ATOM   15153 N  N     . GLY B 2  566  ? 129.308 146.327 137.502 1.00 42.85  ? 566  GLY B N     1 
ATOM   15154 C  CA    . GLY B 2  566  ? 128.909 146.679 138.850 1.00 42.36  ? 566  GLY B CA    1 
ATOM   15155 C  C     . GLY B 2  566  ? 130.011 146.676 139.886 1.00 42.82  ? 566  GLY B C     1 
ATOM   15156 O  O     . GLY B 2  566  ? 129.710 146.742 141.082 1.00 41.67  ? 566  GLY B O     1 
ATOM   15157 N  N     . MET B 2  567  ? 131.275 146.608 139.474 1.00 42.02  ? 567  MET B N     1 
ATOM   15158 C  CA    . MET B 2  567  ? 132.400 146.525 140.397 1.00 39.01  ? 567  MET B CA    1 
ATOM   15159 C  C     . MET B 2  567  ? 133.064 147.869 140.657 1.00 40.22  ? 567  MET B C     1 
ATOM   15160 O  O     . MET B 2  567  ? 133.263 148.240 141.816 1.00 44.64  ? 567  MET B O     1 
ATOM   15161 C  CB    . MET B 2  567  ? 133.441 145.546 139.860 1.00 39.77  ? 567  MET B CB    1 
ATOM   15162 C  CG    . MET B 2  567  ? 132.989 144.108 139.890 1.00 39.84  ? 567  MET B CG    1 
ATOM   15163 S  SD    . MET B 2  567  ? 132.114 143.671 141.398 1.00 52.68  ? 567  MET B SD    1 
ATOM   15164 C  CE    . MET B 2  567  ? 133.338 142.640 142.190 1.00 41.55  ? 567  MET B CE    1 
ATOM   15165 N  N     . SER B 2  568  ? 133.414 148.602 139.610 1.00 32.49  ? 568  SER B N     1 
ATOM   15166 C  CA    . SER B 2  568  ? 134.042 149.915 139.732 1.00 29.15  ? 568  SER B CA    1 
ATOM   15167 C  C     . SER B 2  568  ? 132.944 150.968 139.661 1.00 32.48  ? 568  SER B C     1 
ATOM   15168 O  O     . SER B 2  568  ? 132.186 151.031 138.692 1.00 35.92  ? 568  SER B O     1 
ATOM   15169 C  CB    . SER B 2  568  ? 135.079 150.127 138.637 1.00 29.96  ? 568  SER B CB    1 
ATOM   15170 O  OG    . SER B 2  568  ? 136.128 149.190 138.747 1.00 35.70  ? 568  SER B OG    1 
ATOM   15171 N  N     . LYS B 2  569  ? 132.853 151.785 140.696 1.00 25.85  ? 569  LYS B N     1 
ATOM   15172 C  CA    . LYS B 2  569  ? 131.906 152.881 140.730 1.00 18.50  ? 569  LYS B CA    1 
ATOM   15173 C  C     . LYS B 2  569  ? 132.609 154.198 140.431 1.00 18.38  ? 569  LYS B C     1 
ATOM   15174 O  O     . LYS B 2  569  ? 133.815 154.348 140.619 1.00 24.45  ? 569  LYS B O     1 
ATOM   15175 C  CB    . LYS B 2  569  ? 131.217 152.936 142.088 1.00 20.95  ? 569  LYS B CB    1 
ATOM   15176 C  CG    . LYS B 2  569  ? 131.015 151.575 142.691 1.00 18.40  ? 569  LYS B CG    1 
ATOM   15177 C  CD    . LYS B 2  569  ? 130.489 151.660 144.096 1.00 20.98  ? 569  LYS B CD    1 
ATOM   15178 C  CE    . LYS B 2  569  ? 129.606 150.474 144.399 1.00 27.40  ? 569  LYS B CE    1 
ATOM   15179 N  NZ    . LYS B 2  569  ? 130.337 149.363 145.067 1.00 30.18  ? 569  LYS B NZ    1 
ATOM   15180 N  N     . GLN B 2  570  ? 131.830 155.157 139.962 1.00 11.95  ? 570  GLN B N     1 
ATOM   15181 C  CA    . GLN B 2  570  ? 132.322 156.455 139.541 1.00 9.11   ? 570  GLN B CA    1 
ATOM   15182 C  C     . GLN B 2  570  ? 131.661 157.522 140.392 1.00 9.30   ? 570  GLN B C     1 
ATOM   15183 O  O     . GLN B 2  570  ? 130.475 157.428 140.696 1.00 18.11  ? 570  GLN B O     1 
ATOM   15184 C  CB    . GLN B 2  570  ? 132.011 156.683 138.063 1.00 12.62  ? 570  GLN B CB    1 
ATOM   15185 C  CG    . GLN B 2  570  ? 132.650 157.895 137.442 1.00 16.88  ? 570  GLN B CG    1 
ATOM   15186 C  CD    . GLN B 2  570  ? 134.151 157.785 137.348 1.00 21.31  ? 570  GLN B CD    1 
ATOM   15187 O  OE1   . GLN B 2  570  ? 134.706 156.690 137.316 1.00 24.77  ? 570  GLN B OE1   1 
ATOM   15188 N  NE2   . GLN B 2  570  ? 134.820 158.924 137.285 1.00 20.09  ? 570  GLN B NE2   1 
ATOM   15189 N  N     . LEU B 2  571  ? 132.425 158.527 140.789 1.00 6.72   ? 571  LEU B N     1 
ATOM   15190 C  CA    . LEU B 2  571  ? 131.841 159.639 141.516 1.00 10.14  ? 571  LEU B CA    1 
ATOM   15191 C  C     . LEU B 2  571  ? 130.931 160.450 140.605 1.00 12.74  ? 571  LEU B C     1 
ATOM   15192 O  O     . LEU B 2  571  ? 131.220 160.648 139.424 1.00 18.35  ? 571  LEU B O     1 
ATOM   15193 C  CB    . LEU B 2  571  ? 132.929 160.546 142.080 1.00 13.92  ? 571  LEU B CB    1 
ATOM   15194 C  CG    . LEU B 2  571  ? 133.806 160.071 143.230 1.00 12.12  ? 571  LEU B CG    1 
ATOM   15195 C  CD1   . LEU B 2  571  ? 134.690 161.211 143.654 1.00 13.39  ? 571  LEU B CD1   1 
ATOM   15196 C  CD2   . LEU B 2  571  ? 132.970 159.592 144.390 1.00 7.56   ? 571  LEU B CD2   1 
ATOM   15197 N  N     . ALA B 2  572  ? 129.827 160.933 141.164 1.00 6.67   ? 572  ALA B N     1 
ATOM   15198 C  CA    . ALA B 2  572  ? 128.975 161.830 140.412 1.00 4.44   ? 572  ALA B CA    1 
ATOM   15199 C  C     . ALA B 2  572  ? 129.637 163.199 140.302 1.00 6.74   ? 572  ALA B C     1 
ATOM   15200 O  O     . ALA B 2  572  ? 130.688 163.461 140.882 1.00 15.09  ? 572  ALA B O     1 
ATOM   15201 C  CB    . ALA B 2  572  ? 127.595 161.932 141.049 1.00 4.88   ? 572  ALA B CB    1 
ATOM   15202 N  N     . ILE B 2  573  ? 129.009 164.081 139.529 1.00 9.88   ? 573  ILE B N     1 
ATOM   15203 C  CA    . ILE B 2  573  ? 129.700 165.277 139.065 1.00 11.52  ? 573  ILE B CA    1 
ATOM   15204 C  C     . ILE B 2  573  ? 129.972 166.267 140.201 1.00 13.80  ? 573  ILE B C     1 
ATOM   15205 O  O     . ILE B 2  573  ? 130.989 166.966 140.183 1.00 16.03  ? 573  ILE B O     1 
ATOM   15206 C  CB    . ILE B 2  573  ? 128.909 165.905 137.901 1.00 7.18   ? 573  ILE B CB    1 
ATOM   15207 C  CG1   . ILE B 2  573  ? 129.722 166.999 137.223 1.00 12.07  ? 573  ILE B CG1   1 
ATOM   15208 C  CG2   . ILE B 2  573  ? 127.592 166.442 138.365 1.00 8.21   ? 573  ILE B CG2   1 
ATOM   15209 C  CD1   . ILE B 2  573  ? 131.049 166.533 136.707 1.00 10.92  ? 573  ILE B CD1   1 
ATOM   15210 N  N     . THR B 2  574  ? 129.097 166.358 141.200 1.00 15.41  ? 574  THR B N     1 
ATOM   15211 C  CA    . THR B 2  574  ? 129.305 167.288 142.303 1.00 13.18  ? 574  THR B CA    1 
ATOM   15212 C  C     . THR B 2  574  ? 129.837 166.626 143.570 1.00 13.89  ? 574  THR B C     1 
ATOM   15213 O  O     . THR B 2  574  ? 130.062 167.323 144.557 1.00 17.59  ? 574  THR B O     1 
ATOM   15214 C  CB    . THR B 2  574  ? 128.009 168.035 142.633 1.00 8.48   ? 574  THR B CB    1 
ATOM   15215 O  OG1   . THR B 2  574  ? 126.964 167.096 142.899 1.00 18.91  ? 574  THR B OG1   1 
ATOM   15216 C  CG2   . THR B 2  574  ? 127.603 168.938 141.504 1.00 5.49   ? 574  THR B CG2   1 
ATOM   15217 N  N     . ALA B 2  575  ? 130.062 165.318 143.563 1.00 11.38  ? 575  ALA B N     1 
ATOM   15218 C  CA    . ALA B 2  575  ? 130.453 164.614 144.774 1.00 8.22   ? 575  ALA B CA    1 
ATOM   15219 C  C     . ALA B 2  575  ? 131.940 164.781 145.060 1.00 16.72  ? 575  ALA B C     1 
ATOM   15220 O  O     . ALA B 2  575  ? 132.780 164.686 144.164 1.00 23.04  ? 575  ALA B O     1 
ATOM   15221 C  CB    . ALA B 2  575  ? 130.109 163.136 144.654 1.00 4.09   ? 575  ALA B CB    1 
ATOM   15222 N  N     . ASN B 2  576  ? 132.263 165.014 146.327 1.00 22.63  ? 576  ASN B N     1 
ATOM   15223 C  CA    . ASN B 2  576  ? 133.628 165.172 146.801 1.00 17.88  ? 576  ASN B CA    1 
ATOM   15224 C  C     . ASN B 2  576  ? 133.863 164.202 147.952 1.00 20.74  ? 576  ASN B C     1 
ATOM   15225 O  O     . ASN B 2  576  ? 132.930 163.601 148.480 1.00 24.35  ? 576  ASN B O     1 
ATOM   15226 C  CB    . ASN B 2  576  ? 133.889 166.616 147.237 1.00 21.89  ? 576  ASN B CB    1 
ATOM   15227 C  CG    . ASN B 2  576  ? 135.334 167.006 147.105 1.00 26.49  ? 576  ASN B CG    1 
ATOM   15228 O  OD1   . ASN B 2  576  ? 136.158 166.222 146.644 1.00 31.33  ? 576  ASN B OD1   1 
ATOM   15229 N  ND2   . ASN B 2  576  ? 135.656 168.224 147.510 1.00 24.03  ? 576  ASN B ND2   1 
ATOM   15230 N  N     . VAL B 2  577  ? 135.121 164.041 148.343 1.00 22.76  ? 577  VAL B N     1 
ATOM   15231 C  CA    . VAL B 2  577  ? 135.490 163.190 149.468 1.00 22.62  ? 577  VAL B CA    1 
ATOM   15232 C  C     . VAL B 2  577  ? 135.967 164.082 150.604 1.00 24.35  ? 577  VAL B C     1 
ATOM   15233 O  O     . VAL B 2  577  ? 136.794 164.973 150.393 1.00 30.78  ? 577  VAL B O     1 
ATOM   15234 C  CB    . VAL B 2  577  ? 136.565 162.162 149.080 1.00 21.15  ? 577  VAL B CB    1 
ATOM   15235 C  CG1   . VAL B 2  577  ? 136.615 161.066 150.106 1.00 23.45  ? 577  VAL B CG1   1 
ATOM   15236 C  CG2   . VAL B 2  577  ? 136.261 161.584 147.720 1.00 23.99  ? 577  VAL B CG2   1 
ATOM   15237 N  N     . CYS B 2  578  ? 135.431 163.854 151.798 1.00 24.66  ? 578  CYS B N     1 
ATOM   15238 C  CA    . CYS B 2  578  ? 135.687 164.722 152.939 1.00 24.88  ? 578  CYS B CA    1 
ATOM   15239 C  C     . CYS B 2  578  ? 136.965 164.326 153.675 1.00 30.15  ? 578  CYS B C     1 
ATOM   15240 O  O     . CYS B 2  578  ? 137.306 163.147 153.783 1.00 30.04  ? 578  CYS B O     1 
ATOM   15241 C  CB    . CYS B 2  578  ? 134.505 164.681 153.906 1.00 24.14  ? 578  CYS B CB    1 
ATOM   15242 S  SG    . CYS B 2  578  ? 133.362 166.059 153.783 1.00 36.11  ? 578  CYS B SG    1 
ATOM   15243 N  N     . THR B 2  579  ? 137.679 165.336 154.176 1.00 33.66  ? 579  THR B N     1 
ATOM   15244 C  CA    . THR B 2  579  ? 138.856 165.121 155.009 1.00 32.91  ? 579  THR B CA    1 
ATOM   15245 C  C     . THR B 2  579  ? 138.493 165.264 156.488 1.00 31.75  ? 579  THR B C     1 
ATOM   15246 O  O     . THR B 2  579  ? 137.490 165.880 156.853 1.00 32.47  ? 579  THR B O     1 
ATOM   15247 C  CB    . THR B 2  579  ? 139.980 166.082 154.624 1.00 28.67  ? 579  THR B CB    1 
ATOM   15248 O  OG1   . THR B 2  579  ? 139.521 167.435 154.716 1.00 26.48  ? 579  THR B OG1   1 
ATOM   15249 C  CG2   . THR B 2  579  ? 140.450 165.810 153.213 1.00 30.37  ? 579  THR B CG2   1 
ATOM   15250 N  N     . ALA B 2  580  ? 139.341 164.713 157.352 1.00 25.91  ? 580  ALA B N     1 
ATOM   15251 C  CA    . ALA B 2  580  ? 139.031 164.554 158.767 1.00 25.67  ? 580  ALA B CA    1 
ATOM   15252 C  C     . ALA B 2  580  ? 138.981 165.902 159.468 1.00 27.81  ? 580  ALA B C     1 
ATOM   15253 O  O     . ALA B 2  580  ? 139.899 166.716 159.336 1.00 33.90  ? 580  ALA B O     1 
ATOM   15254 C  CB    . ALA B 2  580  ? 140.060 163.653 159.444 1.00 26.13  ? 580  ALA B CB    1 
ATOM   15255 N  N     . GLY B 2  581  ? 137.911 166.128 160.220 1.00 24.10  ? 581  GLY B N     1 
ATOM   15256 C  CA    . GLY B 2  581  ? 137.722 167.379 160.913 1.00 28.92  ? 581  GLY B CA    1 
ATOM   15257 C  C     . GLY B 2  581  ? 138.333 167.380 162.296 1.00 31.81  ? 581  GLY B C     1 
ATOM   15258 O  O     . GLY B 2  581  ? 138.832 166.376 162.803 1.00 30.38  ? 581  GLY B O     1 
ATOM   15259 N  N     . GLU B 2  582  ? 138.284 168.550 162.920 1.00 37.13  ? 582  GLU B N     1 
ATOM   15260 C  CA    . GLU B 2  582  ? 138.828 168.740 164.260 1.00 36.49  ? 582  GLU B CA    1 
ATOM   15261 C  C     . GLU B 2  582  ? 137.786 168.235 165.246 1.00 37.34  ? 582  GLU B C     1 
ATOM   15262 O  O     . GLU B 2  582  ? 136.981 168.991 165.788 1.00 38.00  ? 582  GLU B O     1 
ATOM   15263 C  CB    . GLU B 2  582  ? 139.186 170.202 164.484 1.00 36.03  ? 582  GLU B CB    1 
ATOM   15264 C  CG    . GLU B 2  582  ? 139.626 170.896 163.208 1.00 36.42  ? 582  GLU B CG    1 
ATOM   15265 C  CD    . GLU B 2  582  ? 140.602 172.032 163.439 1.00 39.29  ? 582  GLU B CD    1 
ATOM   15266 O  OE1   . GLU B 2  582  ? 140.151 173.185 163.599 1.00 37.99  ? 582  GLU B OE1   1 
ATOM   15267 O  OE2   . GLU B 2  582  ? 141.825 171.777 163.441 1.00 39.29  ? 582  GLU B OE2   1 
ATOM   15268 N  N     . VAL B 2  583  ? 137.808 166.923 165.474 1.00 30.57  ? 583  VAL B N     1 
ATOM   15269 C  CA    . VAL B 2  583  ? 136.798 166.282 166.308 1.00 31.98  ? 583  VAL B CA    1 
ATOM   15270 C  C     . VAL B 2  583  ? 136.946 166.712 167.763 1.00 35.10  ? 583  VAL B C     1 
ATOM   15271 O  O     . VAL B 2  583  ? 135.962 166.776 168.509 1.00 36.47  ? 583  VAL B O     1 
ATOM   15272 C  CB    . VAL B 2  583  ? 136.886 164.756 166.139 1.00 29.80  ? 583  VAL B CB    1 
ATOM   15273 C  CG1   . VAL B 2  583  ? 138.321 164.306 166.239 1.00 32.05  ? 583  VAL B CG1   1 
ATOM   15274 C  CG2   . VAL B 2  583  ? 136.037 164.044 167.163 1.00 33.53  ? 583  VAL B CG2   1 
ATOM   15275 N  N     . LEU B 2  584  ? 138.170 167.034 168.184 1.00 36.28  ? 584  LEU B N     1 
ATOM   15276 C  CA    . LEU B 2  584  ? 138.414 167.384 169.580 1.00 35.89  ? 584  LEU B CA    1 
ATOM   15277 C  C     . LEU B 2  584  ? 137.690 168.668 169.967 1.00 35.49  ? 584  LEU B C     1 
ATOM   15278 O  O     . LEU B 2  584  ? 137.124 168.766 171.063 1.00 38.65  ? 584  LEU B O     1 
ATOM   15279 C  CB    . LEU B 2  584  ? 139.915 167.528 169.819 1.00 37.86  ? 584  LEU B CB    1 
ATOM   15280 C  CG    . LEU B 2  584  ? 140.664 166.326 170.399 1.00 39.93  ? 584  LEU B CG    1 
ATOM   15281 C  CD1   . LEU B 2  584  ? 140.143 165.956 171.777 1.00 36.10  ? 584  LEU B CD1   1 
ATOM   15282 C  CD2   . LEU B 2  584  ? 140.606 165.138 169.452 1.00 39.74  ? 584  LEU B CD2   1 
ATOM   15283 N  N     . SER B 2  585  ? 137.703 169.665 169.081 1.00 34.63  ? 585  SER B N     1 
ATOM   15284 C  CA    . SER B 2  585  ? 137.043 170.935 169.368 1.00 38.16  ? 585  SER B CA    1 
ATOM   15285 C  C     . SER B 2  585  ? 135.538 170.756 169.511 1.00 39.03  ? 585  SER B C     1 
ATOM   15286 O  O     . SER B 2  585  ? 134.917 171.306 170.429 1.00 38.78  ? 585  SER B O     1 
ATOM   15287 C  CB    . SER B 2  585  ? 137.360 171.943 168.266 1.00 38.40  ? 585  SER B CB    1 
ATOM   15288 O  OG    . SER B 2  585  ? 137.143 173.268 168.710 1.00 39.83  ? 585  SER B OG    1 
ATOM   15289 N  N     . LEU B 2  586  ? 134.929 169.983 168.610 1.00 36.39  ? 586  LEU B N     1 
ATOM   15290 C  CA    . LEU B 2  586  ? 133.500 169.722 168.726 1.00 33.95  ? 586  LEU B CA    1 
ATOM   15291 C  C     . LEU B 2  586  ? 133.194 168.933 169.986 1.00 33.73  ? 586  LEU B C     1 
ATOM   15292 O  O     . LEU B 2  586  ? 132.202 169.207 170.665 1.00 31.77  ? 586  LEU B O     1 
ATOM   15293 C  CB    . LEU B 2  586  ? 132.987 168.978 167.493 1.00 31.80  ? 586  LEU B CB    1 
ATOM   15294 C  CG    . LEU B 2  586  ? 131.463 168.893 167.377 1.00 32.44  ? 586  LEU B CG    1 
ATOM   15295 C  CD1   . LEU B 2  586  ? 130.850 170.271 167.300 1.00 30.35  ? 586  LEU B CD1   1 
ATOM   15296 C  CD2   . LEU B 2  586  ? 131.064 168.066 166.187 1.00 31.40  ? 586  LEU B CD2   1 
ATOM   15297 N  N     . LYS B 2  587  ? 134.039 167.954 170.314 1.00 33.87  ? 587  LYS B N     1 
ATOM   15298 C  CA    . LYS B 2  587  ? 133.821 167.150 171.511 1.00 33.14  ? 587  LYS B CA    1 
ATOM   15299 C  C     . LYS B 2  587  ? 133.846 168.012 172.762 1.00 33.80  ? 587  LYS B C     1 
ATOM   15300 O  O     . LYS B 2  587  ? 132.999 167.854 173.648 1.00 30.95  ? 587  LYS B O     1 
ATOM   15301 C  CB    . LYS B 2  587  ? 134.877 166.054 171.600 1.00 29.34  ? 587  LYS B CB    1 
ATOM   15302 C  CG    . LYS B 2  587  ? 134.583 164.978 172.615 1.00 27.97  ? 587  LYS B CG    1 
ATOM   15303 C  CD    . LYS B 2  587  ? 135.748 164.023 172.723 1.00 29.65  ? 587  LYS B CD    1 
ATOM   15304 C  CE    . LYS B 2  587  ? 136.000 163.326 171.396 1.00 33.04  ? 587  LYS B CE    1 
ATOM   15305 N  NZ    . LYS B 2  587  ? 137.021 162.246 171.505 1.00 33.86  ? 587  LYS B NZ    1 
ATOM   15306 N  N     . GLN B 2  588  ? 134.802 168.936 172.852 1.00 38.73  ? 588  GLN B N     1 
ATOM   15307 C  CA    . GLN B 2  588  ? 134.856 169.790 174.029 1.00 41.05  ? 588  GLN B CA    1 
ATOM   15308 C  C     . GLN B 2  588  ? 133.762 170.849 174.022 1.00 40.56  ? 588  GLN B C     1 
ATOM   15309 O  O     . GLN B 2  588  ? 133.378 171.327 175.093 1.00 40.92  ? 588  GLN B O     1 
ATOM   15310 C  CB    . GLN B 2  588  ? 136.235 170.441 174.162 1.00 39.51  ? 588  GLN B CB    1 
ATOM   15311 C  CG    . GLN B 2  588  ? 136.580 171.483 173.122 1.00 39.63  ? 588  GLN B CG    1 
ATOM   15312 C  CD    . GLN B 2  588  ? 136.414 172.894 173.652 1.00 43.80  ? 588  GLN B CD    1 
ATOM   15313 O  OE1   . GLN B 2  588  ? 136.570 173.140 174.846 1.00 44.24  ? 588  GLN B OE1   1 
ATOM   15314 N  NE2   . GLN B 2  588  ? 136.115 173.831 172.763 1.00 43.61  ? 588  GLN B NE2   1 
ATOM   15315 N  N     . ARG B 2  589  ? 133.245 171.225 172.851 1.00 39.41  ? 589  ARG B N     1 
ATOM   15316 C  CA    . ARG B 2  589  ? 132.096 172.126 172.829 1.00 40.74  ? 589  ARG B CA    1 
ATOM   15317 C  C     . ARG B 2  589  ? 130.814 171.426 173.266 1.00 38.73  ? 589  ARG B C     1 
ATOM   15318 O  O     . ARG B 2  589  ? 129.982 172.027 173.950 1.00 37.37  ? 589  ARG B O     1 
ATOM   15319 C  CB    . ARG B 2  589  ? 131.913 172.719 171.437 1.00 38.35  ? 589  ARG B CB    1 
ATOM   15320 C  CG    . ARG B 2  589  ? 130.813 173.750 171.373 1.00 35.62  ? 589  ARG B CG    1 
ATOM   15321 C  CD    . ARG B 2  589  ? 130.930 174.590 170.133 1.00 38.28  ? 589  ARG B CD    1 
ATOM   15322 N  NE    . ARG B 2  589  ? 131.607 175.856 170.380 1.00 42.41  ? 589  ARG B NE    1 
ATOM   15323 C  CZ    . ARG B 2  589  ? 130.998 176.969 170.764 1.00 43.15  ? 589  ARG B CZ    1 
ATOM   15324 N  NH1   . ARG B 2  589  ? 129.691 177.009 170.962 1.00 38.11  ? 589  ARG B NH1   1 
ATOM   15325 N  NH2   . ARG B 2  589  ? 131.720 178.069 170.954 1.00 40.67  ? 589  ARG B NH2   1 
ATOM   15326 N  N     . LEU B 2  590  ? 130.629 170.167 172.861 1.00 34.35  ? 590  LEU B N     1 
ATOM   15327 C  CA    . LEU B 2  590  ? 129.430 169.422 173.235 1.00 32.49  ? 590  LEU B CA    1 
ATOM   15328 C  C     . LEU B 2  590  ? 129.387 169.157 174.733 1.00 35.18  ? 590  LEU B C     1 
ATOM   15329 O  O     . LEU B 2  590  ? 128.347 169.330 175.375 1.00 39.00  ? 590  LEU B O     1 
ATOM   15330 C  CB    . LEU B 2  590  ? 129.369 168.102 172.464 1.00 34.67  ? 590  LEU B CB    1 
ATOM   15331 C  CG    . LEU B 2  590  ? 128.889 168.120 171.014 1.00 33.09  ? 590  LEU B CG    1 
ATOM   15332 C  CD1   . LEU B 2  590  ? 129.227 166.814 170.335 1.00 28.71  ? 590  LEU B CD1   1 
ATOM   15333 C  CD2   . LEU B 2  590  ? 127.406 168.370 170.977 1.00 33.29  ? 590  LEU B CD2   1 
ATOM   15334 N  N     . LEU B 2  591  ? 130.513 168.737 175.311 1.00 33.51  ? 591  LEU B N     1 
ATOM   15335 C  CA    . LEU B 2  591  ? 130.547 168.461 176.742 1.00 31.01  ? 591  LEU B CA    1 
ATOM   15336 C  C     . LEU B 2  591  ? 130.337 169.719 177.571 1.00 29.98  ? 591  LEU B C     1 
ATOM   15337 O  O     . LEU B 2  591  ? 130.058 169.619 178.768 1.00 31.86  ? 591  LEU B O     1 
ATOM   15338 C  CB    . LEU B 2  591  ? 131.866 167.785 177.109 1.00 31.99  ? 591  LEU B CB    1 
ATOM   15339 C  CG    . LEU B 2  591  ? 131.982 166.330 176.647 1.00 31.46  ? 591  LEU B CG    1 
ATOM   15340 C  CD1   . LEU B 2  591  ? 132.973 165.570 177.496 1.00 30.81  ? 591  LEU B CD1   1 
ATOM   15341 C  CD2   . LEU B 2  591  ? 130.631 165.650 176.688 1.00 29.29  ? 591  LEU B CD2   1 
ATOM   15342 N  N     . SER B 2  592  ? 130.466 170.896 176.964 1.00 31.88  ? 592  SER B N     1 
ATOM   15343 C  CA    . SER B 2  592  ? 130.131 172.148 177.625 1.00 35.49  ? 592  SER B CA    1 
ATOM   15344 C  C     . SER B 2  592  ? 128.683 172.563 177.407 1.00 35.91  ? 592  SER B C     1 
ATOM   15345 O  O     . SER B 2  592  ? 128.253 173.567 177.981 1.00 35.26  ? 592  SER B O     1 
ATOM   15346 C  CB    . SER B 2  592  ? 131.054 173.263 177.132 1.00 33.55  ? 592  SER B CB    1 
ATOM   15347 O  OG    . SER B 2  592  ? 132.411 172.897 177.277 1.00 34.68  ? 592  SER B OG    1 
ATOM   15348 N  N     . ASP B 2  593  ? 127.931 171.827 176.598 1.00 36.67  ? 593  ASP B N     1 
ATOM   15349 C  CA    . ASP B 2  593  ? 126.551 172.190 176.305 1.00 36.39  ? 593  ASP B CA    1 
ATOM   15350 C  C     . ASP B 2  593  ? 125.674 171.889 177.512 1.00 39.32  ? 593  ASP B C     1 
ATOM   15351 O  O     . ASP B 2  593  ? 125.655 170.746 177.980 1.00 39.09  ? 593  ASP B O     1 
ATOM   15352 C  CB    . ASP B 2  593  ? 126.044 171.427 175.087 1.00 35.36  ? 593  ASP B CB    1 
ATOM   15353 C  CG    . ASP B 2  593  ? 124.939 172.161 174.351 1.00 41.46  ? 593  ASP B CG    1 
ATOM   15354 O  OD1   . ASP B 2  593  ? 124.068 172.766 175.008 1.00 40.20  ? 593  ASP B OD1   1 
ATOM   15355 O  OD2   . ASP B 2  593  ? 124.950 172.142 173.107 1.00 40.92  ? 593  ASP B OD2   1 
ATOM   15356 N  N     . PRO B 2  594  ? 124.945 172.868 178.046 1.00 38.37  ? 594  PRO B N     1 
ATOM   15357 C  CA    . PRO B 2  594  ? 124.059 172.578 179.183 1.00 37.83  ? 594  PRO B CA    1 
ATOM   15358 C  C     . PRO B 2  594  ? 122.940 171.605 178.850 1.00 37.20  ? 594  PRO B C     1 
ATOM   15359 O  O     . PRO B 2  594  ? 122.374 170.991 179.762 1.00 35.76  ? 594  PRO B O     1 
ATOM   15360 C  CB    . PRO B 2  594  ? 123.518 173.963 179.568 1.00 32.83  ? 594  PRO B CB    1 
ATOM   15361 C  CG    . PRO B 2  594  ? 123.729 174.811 178.364 1.00 35.63  ? 594  PRO B CG    1 
ATOM   15362 C  CD    . PRO B 2  594  ? 124.971 174.299 177.711 1.00 36.09  ? 594  PRO B CD    1 
ATOM   15363 N  N     . ALA B 2  595  ? 122.610 171.434 177.574 1.00 36.18  ? 595  ALA B N     1 
ATOM   15364 C  CA    . ALA B 2  595  ? 121.539 170.539 177.159 1.00 36.79  ? 595  ALA B CA    1 
ATOM   15365 C  C     . ALA B 2  595  ? 121.977 169.084 177.062 1.00 33.95  ? 595  ALA B C     1 
ATOM   15366 O  O     . ALA B 2  595  ? 121.155 168.231 176.722 1.00 32.77  ? 595  ALA B O     1 
ATOM   15367 C  CB    . ALA B 2  595  ? 120.960 170.996 175.820 1.00 36.32  ? 595  ALA B CB    1 
ATOM   15368 N  N     . ILE B 2  596  ? 123.237 168.775 177.350 1.00 33.65  ? 596  ILE B N     1 
ATOM   15369 C  CA    . ILE B 2  596  ? 123.747 167.412 177.282 1.00 37.51  ? 596  ILE B CA    1 
ATOM   15370 C  C     . ILE B 2  596  ? 124.228 167.013 178.670 1.00 39.87  ? 596  ILE B C     1 
ATOM   15371 O  O     . ILE B 2  596  ? 125.001 167.745 179.296 1.00 42.12  ? 596  ILE B O     1 
ATOM   15372 C  CB    . ILE B 2  596  ? 124.882 167.274 176.254 1.00 36.16  ? 596  ILE B CB    1 
ATOM   15373 C  CG1   . ILE B 2  596  ? 124.342 167.508 174.847 1.00 34.51  ? 596  ILE B CG1   1 
ATOM   15374 C  CG2   . ILE B 2  596  ? 125.522 165.899 176.334 1.00 33.94  ? 596  ILE B CG2   1 
ATOM   15375 C  CD1   . ILE B 2  596  ? 125.401 167.559 173.814 1.00 33.91  ? 596  ILE B CD1   1 
ATOM   15376 N  N     . GLN B 2  597  ? 123.763 165.865 179.152 1.00 37.65  ? 597  GLN B N     1 
ATOM   15377 C  CA    . GLN B 2  597  ? 124.202 165.324 180.430 1.00 37.39  ? 597  GLN B CA    1 
ATOM   15378 C  C     . GLN B 2  597  ? 125.377 164.382 180.206 1.00 41.23  ? 597  GLN B C     1 
ATOM   15379 O  O     . GLN B 2  597  ? 125.368 163.589 179.261 1.00 42.77  ? 597  GLN B O     1 
ATOM   15380 C  CB    . GLN B 2  597  ? 123.055 164.594 181.124 1.00 35.83  ? 597  GLN B CB    1 
ATOM   15381 C  CG    . GLN B 2  597  ? 122.021 165.526 181.730 1.00 40.51  ? 597  GLN B CG    1 
ATOM   15382 C  CD    . GLN B 2  597  ? 120.691 165.481 181.003 1.00 40.92  ? 597  GLN B CD    1 
ATOM   15383 O  OE1   . GLN B 2  597  ? 120.161 164.409 180.730 1.00 42.14  ? 597  GLN B OE1   1 
ATOM   15384 N  NE2   . GLN B 2  597  ? 120.149 166.649 180.681 1.00 38.98  ? 597  GLN B NE2   1 
ATOM   15385 N  N     . GLN B 2  598  ? 126.381 164.468 181.075 1.00 39.82  ? 598  GLN B N     1 
ATOM   15386 C  CA    . GLN B 2  598  ? 127.571 163.646 180.923 1.00 39.45  ? 598  GLN B CA    1 
ATOM   15387 C  C     . GLN B 2  598  ? 127.241 162.173 181.132 1.00 40.91  ? 598  GLN B C     1 
ATOM   15388 O  O     . GLN B 2  598  ? 126.238 161.810 181.750 1.00 38.27  ? 598  GLN B O     1 
ATOM   15389 C  CB    . GLN B 2  598  ? 128.662 164.079 181.898 1.00 40.11  ? 598  GLN B CB    1 
ATOM   15390 C  CG    . GLN B 2  598  ? 129.728 164.978 181.287 1.00 40.53  ? 598  GLN B CG    1 
ATOM   15391 C  CD    . GLN B 2  598  ? 129.236 166.392 181.063 1.00 42.62  ? 598  GLN B CD    1 
ATOM   15392 O  OE1   . GLN B 2  598  ? 129.515 167.003 180.033 1.00 42.55  ? 598  GLN B OE1   1 
ATOM   15393 N  NE2   . GLN B 2  598  ? 128.491 166.918 182.028 1.00 42.36  ? 598  GLN B NE2   1 
ATOM   15394 N  N     . LEU B 2  599  ? 128.106 161.319 180.584 1.00 41.45  ? 599  LEU B N     1 
ATOM   15395 C  CA    . LEU B 2  599  ? 127.823 159.889 180.554 1.00 39.35  ? 599  LEU B CA    1 
ATOM   15396 C  C     . LEU B 2  599  ? 127.713 159.315 181.959 1.00 40.17  ? 599  LEU B C     1 
ATOM   15397 O  O     . LEU B 2  599  ? 126.784 158.556 182.257 1.00 39.38  ? 599  LEU B O     1 
ATOM   15398 C  CB    . LEU B 2  599  ? 128.911 159.176 179.748 1.00 39.84  ? 599  LEU B CB    1 
ATOM   15399 C  CG    . LEU B 2  599  ? 128.772 157.721 179.290 1.00 41.31  ? 599  LEU B CG    1 
ATOM   15400 C  CD1   . LEU B 2  599  ? 128.711 156.714 180.432 1.00 41.35  ? 599  LEU B CD1   1 
ATOM   15401 C  CD2   . LEU B 2  599  ? 127.541 157.603 178.434 1.00 37.18  ? 599  LEU B CD2   1 
ATOM   15402 N  N     . ALA B 2  600  ? 128.649 159.663 182.836 1.00 42.11  ? 600  ALA B N     1 
ATOM   15403 C  CA    . ALA B 2  600  ? 128.671 159.110 184.180 1.00 42.55  ? 600  ALA B CA    1 
ATOM   15404 C  C     . ALA B 2  600  ? 127.686 159.792 185.117 1.00 38.62  ? 600  ALA B C     1 
ATOM   15405 O  O     . ALA B 2  600  ? 127.545 159.357 186.262 1.00 39.81  ? 600  ALA B O     1 
ATOM   15406 C  CB    . ALA B 2  600  ? 130.086 159.199 184.753 1.00 42.03  ? 600  ALA B CB    1 
ATOM   15407 N  N     . ASP B 2  601  ? 127.017 160.848 184.665 1.00 40.76  ? 601  ASP B N     1 
ATOM   15408 C  CA    . ASP B 2  601  ? 126.043 161.580 185.459 1.00 44.73  ? 601  ASP B CA    1 
ATOM   15409 C  C     . ASP B 2  601  ? 124.622 161.054 185.259 1.00 45.43  ? 601  ASP B C     1 
ATOM   15410 O  O     . ASP B 2  601  ? 123.677 161.605 185.829 1.00 41.58  ? 601  ASP B O     1 
ATOM   15411 C  CB    . ASP B 2  601  ? 126.113 163.069 185.107 1.00 44.51  ? 601  ASP B CB    1 
ATOM   15412 C  CG    . ASP B 2  601  ? 125.710 163.973 186.257 1.00 45.80  ? 601  ASP B CG    1 
ATOM   15413 O  OD1   . ASP B 2  601  ? 126.353 165.029 186.424 1.00 45.26  ? 601  ASP B OD1   1 
ATOM   15414 O  OD2   . ASP B 2  601  ? 124.775 163.635 187.006 1.00 44.27  ? 601  ASP B OD2   1 
ATOM   15415 N  N     . VAL B 2  602  ? 124.442 160.018 184.441 1.00 44.08  ? 602  VAL B N     1 
ATOM   15416 C  CA    . VAL B 2  602  ? 123.116 159.467 184.191 1.00 43.08  ? 602  VAL B CA    1 
ATOM   15417 C  C     . VAL B 2  602  ? 123.227 157.953 184.069 1.00 42.28  ? 602  VAL B C     1 
ATOM   15418 O  O     . VAL B 2  602  ? 124.270 157.418 183.682 1.00 42.11  ? 602  VAL B O     1 
ATOM   15419 C  CB    . VAL B 2  602  ? 122.474 160.104 182.937 1.00 43.68  ? 602  VAL B CB    1 
ATOM   15420 C  CG1   . VAL B 2  602  ? 122.974 159.435 181.667 1.00 42.63  ? 602  VAL B CG1   1 
ATOM   15421 C  CG2   . VAL B 2  602  ? 120.962 160.054 183.034 1.00 43.17  ? 602  VAL B CG2   1 
ATOM   15422 N  N     . SER B 2  603  ? 122.136 157.263 184.395 1.00 40.99  ? 603  SER B N     1 
ATOM   15423 C  CA    . SER B 2  603  ? 122.125 155.812 184.479 1.00 44.56  ? 603  SER B CA    1 
ATOM   15424 C  C     . SER B 2  603  ? 121.225 155.208 183.410 1.00 44.16  ? 603  SER B C     1 
ATOM   15425 O  O     . SER B 2  603  ? 120.375 155.882 182.825 1.00 42.36  ? 603  SER B O     1 
ATOM   15426 C  CB    . SER B 2  603  ? 121.649 155.337 185.854 1.00 43.56  ? 603  SER B CB    1 
ATOM   15427 O  OG    . SER B 2  603  ? 120.280 155.649 186.046 1.00 44.83  ? 603  SER B OG    1 
ATOM   15428 N  N     . ASN B 2  604  ? 121.416 153.906 183.183 1.00 43.89  ? 604  ASN B N     1 
ATOM   15429 C  CA    . ASN B 2  604  ? 120.615 153.189 182.197 1.00 44.11  ? 604  ASN B CA    1 
ATOM   15430 C  C     . ASN B 2  604  ? 119.139 153.205 182.570 1.00 44.16  ? 604  ASN B C     1 
ATOM   15431 O  O     . ASN B 2  604  ? 118.270 153.433 181.716 1.00 44.44  ? 604  ASN B O     1 
ATOM   15432 C  CB    . ASN B 2  604  ? 121.121 151.755 182.072 1.00 43.36  ? 604  ASN B CB    1 
ATOM   15433 C  CG    . ASN B 2  604  ? 122.479 151.674 181.423 1.00 42.31  ? 604  ASN B CG    1 
ATOM   15434 O  OD1   . ASN B 2  604  ? 122.712 152.266 180.373 1.00 43.17  ? 604  ASN B OD1   1 
ATOM   15435 N  ND2   . ASN B 2  604  ? 123.387 150.938 182.045 1.00 43.85  ? 604  ASN B ND2   1 
ATOM   15436 N  N     . LYS B 2  605  ? 118.839 152.964 183.845 1.00 44.66  ? 605  LYS B N     1 
ATOM   15437 C  CA    . LYS B 2  605  ? 117.477 153.148 184.327 1.00 47.37  ? 605  LYS B CA    1 
ATOM   15438 C  C     . LYS B 2  605  ? 116.991 154.558 184.026 1.00 48.17  ? 605  LYS B C     1 
ATOM   15439 O  O     . LYS B 2  605  ? 115.863 154.750 183.559 1.00 45.09  ? 605  LYS B O     1 
ATOM   15440 C  CB    . LYS B 2  605  ? 117.430 152.822 185.828 1.00 47.18  ? 605  LYS B CB    1 
ATOM   15441 C  CG    . LYS B 2  605  ? 116.160 153.187 186.627 1.00 45.15  ? 605  LYS B CG    1 
ATOM   15442 C  CD    . LYS B 2  605  ? 116.025 154.684 186.907 1.00 47.37  ? 605  LYS B CD    1 
ATOM   15443 C  CE    . LYS B 2  605  ? 115.250 154.970 188.173 1.00 48.75  ? 605  LYS B CE    1 
ATOM   15444 N  NZ    . LYS B 2  605  ? 115.304 156.427 188.475 1.00 50.65  ? 605  LYS B NZ    1 
ATOM   15445 N  N     . ASP B 2  606  ? 117.832 155.557 184.285 1.00 48.73  ? 606  ASP B N     1 
ATOM   15446 C  CA    . ASP B 2  606  ? 117.415 156.940 184.099 1.00 49.69  ? 606  ASP B CA    1 
ATOM   15447 C  C     . ASP B 2  606  ? 117.156 157.247 182.629 1.00 49.71  ? 606  ASP B C     1 
ATOM   15448 O  O     . ASP B 2  606  ? 116.237 158.005 182.298 1.00 49.84  ? 606  ASP B O     1 
ATOM   15449 C  CB    . ASP B 2  606  ? 118.469 157.877 184.679 1.00 48.30  ? 606  ASP B CB    1 
ATOM   15450 C  CG    . ASP B 2  606  ? 117.863 159.119 185.291 1.00 52.06  ? 606  ASP B CG    1 
ATOM   15451 O  OD1   . ASP B 2  606  ? 116.621 159.259 185.244 1.00 52.14  ? 606  ASP B OD1   1 
ATOM   15452 O  OD2   . ASP B 2  606  ? 118.624 159.941 185.844 1.00 52.65  ? 606  ASP B OD2   1 
ATOM   15453 N  N     . ILE B 2  607  ? 117.959 156.673 181.732 1.00 45.07  ? 607  ILE B N     1 
ATOM   15454 C  CA    . ILE B 2  607  ? 117.812 156.965 180.310 1.00 43.56  ? 607  ILE B CA    1 
ATOM   15455 C  C     . ILE B 2  607  ? 116.751 156.113 179.630 1.00 44.92  ? 607  ILE B C     1 
ATOM   15456 O  O     . ILE B 2  607  ? 116.407 156.388 178.476 1.00 46.38  ? 607  ILE B O     1 
ATOM   15457 C  CB    . ILE B 2  607  ? 119.157 156.822 179.577 1.00 45.39  ? 607  ILE B CB    1 
ATOM   15458 C  CG1   . ILE B 2  607  ? 119.593 155.364 179.517 1.00 42.11  ? 607  ILE B CG1   1 
ATOM   15459 C  CG2   . ILE B 2  607  ? 120.222 157.690 180.216 1.00 44.28  ? 607  ILE B CG2   1 
ATOM   15460 C  CD1   . ILE B 2  607  ? 120.855 155.157 178.734 1.00 42.56  ? 607  ILE B CD1   1 
ATOM   15461 N  N     . VAL B 2  608  ? 116.210 155.091 180.290 1.00 44.07  ? 608  VAL B N     1 
ATOM   15462 C  CA    . VAL B 2  608  ? 115.015 154.471 179.724 1.00 44.88  ? 608  VAL B CA    1 
ATOM   15463 C  C     . VAL B 2  608  ? 113.760 155.077 180.337 1.00 45.38  ? 608  VAL B C     1 
ATOM   15464 O  O     . VAL B 2  608  ? 112.722 155.167 179.672 1.00 43.36  ? 608  VAL B O     1 
ATOM   15465 C  CB    . VAL B 2  608  ? 115.009 152.942 179.887 1.00 44.84  ? 608  VAL B CB    1 
ATOM   15466 C  CG1   . VAL B 2  608  ? 116.044 152.310 178.973 1.00 43.91  ? 608  VAL B CG1   1 
ATOM   15467 C  CG2   . VAL B 2  608  ? 115.237 152.562 181.330 1.00 42.59  ? 608  VAL B CG2   1 
ATOM   15468 N  N     . ARG B 2  609  ? 113.837 155.501 181.602 1.00 47.99  ? 609  ARG B N     1 
ATOM   15469 C  CA    . ARG B 2  609  ? 112.658 156.051 182.264 1.00 47.31  ? 609  ARG B CA    1 
ATOM   15470 C  C     . ARG B 2  609  ? 112.225 157.356 181.609 1.00 45.90  ? 609  ARG B C     1 
ATOM   15471 O  O     . ARG B 2  609  ? 111.091 157.483 181.135 1.00 45.42  ? 609  ARG B O     1 
ATOM   15472 C  CB    . ARG B 2  609  ? 112.937 156.269 183.754 1.00 48.59  ? 609  ARG B CB    1 
ATOM   15473 C  CG    . ARG B 2  609  ? 112.981 155.004 184.603 1.00 47.71  ? 609  ARG B CG    1 
ATOM   15474 C  CD    . ARG B 2  609  ? 111.661 154.249 184.592 1.00 48.10  ? 609  ARG B CD    1 
ATOM   15475 N  NE    . ARG B 2  609  ? 111.569 153.285 185.685 1.00 50.75  ? 609  ARG B NE    1 
ATOM   15476 C  CZ    . ARG B 2  609  ? 112.210 152.124 185.718 1.00 48.56  ? 609  ARG B CZ    1 
ATOM   15477 N  NH1   . ARG B 2  609  ? 113.031 151.759 184.749 1.00 48.40  ? 609  ARG B NH1   1 
ATOM   15478 N  NH2   . ARG B 2  609  ? 112.029 151.312 186.755 1.00 44.41  ? 609  ARG B NH2   1 
ATOM   15479 N  N     . LYS B 2  610  ? 113.126 158.336 181.562 1.00 46.02  ? 610  LYS B N     1 
ATOM   15480 C  CA    . LYS B 2  610  ? 112.816 159.632 180.974 1.00 44.75  ? 610  LYS B CA    1 
ATOM   15481 C  C     . LYS B 2  610  ? 112.879 159.637 179.454 1.00 43.02  ? 610  LYS B C     1 
ATOM   15482 O  O     . LYS B 2  610  ? 112.543 160.657 178.844 1.00 39.83  ? 610  LYS B O     1 
ATOM   15483 C  CB    . LYS B 2  610  ? 113.762 160.703 181.511 1.00 41.83  ? 610  LYS B CB    1 
ATOM   15484 C  CG    . LYS B 2  610  ? 113.617 161.010 182.979 1.00 40.48  ? 610  LYS B CG    1 
ATOM   15485 C  CD    . LYS B 2  610  ? 113.823 162.495 183.207 1.00 42.65  ? 610  LYS B CD    1 
ATOM   15486 C  CE    . LYS B 2  610  ? 115.172 162.799 183.834 1.00 43.44  ? 610  LYS B CE    1 
ATOM   15487 N  NZ    . LYS B 2  610  ? 115.761 164.053 183.277 1.00 42.08  ? 610  LYS B NZ    1 
ATOM   15488 N  N     . GLY B 2  611  ? 113.296 158.539 178.832 1.00 41.99  ? 611  GLY B N     1 
ATOM   15489 C  CA    . GLY B 2  611  ? 113.368 158.479 177.383 1.00 42.89  ? 611  GLY B CA    1 
ATOM   15490 C  C     . GLY B 2  611  ? 114.422 159.378 176.776 1.00 44.74  ? 611  GLY B C     1 
ATOM   15491 O  O     . GLY B 2  611  ? 114.189 159.973 175.717 1.00 44.66  ? 611  GLY B O     1 
ATOM   15492 N  N     . LEU B 2  612  ? 115.577 159.489 177.421 1.00 39.71  ? 612  LEU B N     1 
ATOM   15493 C  CA    . LEU B 2  612  ? 116.651 160.322 176.906 1.00 39.88  ? 612  LEU B CA    1 
ATOM   15494 C  C     . LEU B 2  612  ? 117.292 159.673 175.685 1.00 41.77  ? 612  LEU B C     1 
ATOM   15495 O  O     . LEU B 2  612  ? 117.199 158.462 175.474 1.00 40.20  ? 612  LEU B O     1 
ATOM   15496 C  CB    . LEU B 2  612  ? 117.701 160.564 177.990 1.00 41.69  ? 612  LEU B CB    1 
ATOM   15497 C  CG    . LEU B 2  612  ? 117.233 161.122 179.338 1.00 43.37  ? 612  LEU B CG    1 
ATOM   15498 C  CD1   . LEU B 2  612  ? 118.362 161.859 180.011 1.00 37.90  ? 612  LEU B CD1   1 
ATOM   15499 C  CD2   . LEU B 2  612  ? 116.064 162.068 179.157 1.00 40.48  ? 612  LEU B CD2   1 
ATOM   15500 N  N     . ALA B 2  613  ? 117.946 160.497 174.874 1.00 37.53  ? 613  ALA B N     1 
ATOM   15501 C  CA    . ALA B 2  613  ? 118.583 160.053 173.643 1.00 33.30  ? 613  ALA B CA    1 
ATOM   15502 C  C     . ALA B 2  613  ? 120.094 160.090 173.805 1.00 32.28  ? 613  ALA B C     1 
ATOM   15503 O  O     . ALA B 2  613  ? 120.649 161.104 174.234 1.00 34.39  ? 613  ALA B O     1 
ATOM   15504 C  CB    . ALA B 2  613  ? 118.156 160.931 172.465 1.00 33.14  ? 613  ALA B CB    1 
ATOM   15505 N  N     . ARG B 2  614  ? 120.752 158.990 173.453 1.00 31.22  ? 614  ARG B N     1 
ATOM   15506 C  CA    . ARG B 2  614  ? 122.201 158.888 173.535 1.00 34.40  ? 614  ARG B CA    1 
ATOM   15507 C  C     . ARG B 2  614  ? 122.864 159.659 172.404 1.00 31.62  ? 614  ARG B C     1 
ATOM   15508 O  O     . ARG B 2  614  ? 122.525 159.476 171.234 1.00 33.63  ? 614  ARG B O     1 
ATOM   15509 C  CB    . ARG B 2  614  ? 122.631 157.425 173.481 1.00 33.14  ? 614  ARG B CB    1 
ATOM   15510 C  CG    . ARG B 2  614  ? 121.663 156.483 174.142 1.00 31.75  ? 614  ARG B CG    1 
ATOM   15511 C  CD    . ARG B 2  614  ? 122.382 155.267 174.684 1.00 33.45  ? 614  ARG B CD    1 
ATOM   15512 N  NE    . ARG B 2  614  ? 121.647 154.014 174.549 1.00 36.02  ? 614  ARG B NE    1 
ATOM   15513 C  CZ    . ARG B 2  614  ? 120.453 153.765 175.074 1.00 39.01  ? 614  ARG B CZ    1 
ATOM   15514 N  NH1   . ARG B 2  614  ? 119.807 154.666 175.794 1.00 36.82  ? 614  ARG B NH1   1 
ATOM   15515 N  NH2   . ARG B 2  614  ? 119.893 152.577 174.873 1.00 36.42  ? 614  ARG B NH2   1 
ATOM   15516 N  N     . VAL B 2  615  ? 123.840 160.489 172.757 1.00 25.18  ? 615  VAL B N     1 
ATOM   15517 C  CA    . VAL B 2  615  ? 124.504 161.394 171.823 1.00 28.46  ? 615  VAL B CA    1 
ATOM   15518 C  C     . VAL B 2  615  ? 125.895 160.847 171.538 1.00 27.53  ? 615  VAL B C     1 
ATOM   15519 O  O     . VAL B 2  615  ? 126.676 160.609 172.464 1.00 36.21  ? 615  VAL B O     1 
ATOM   15520 C  CB    . VAL B 2  615  ? 124.580 162.821 172.373 1.00 26.52  ? 615  VAL B CB    1 
ATOM   15521 C  CG1   . VAL B 2  615  ? 125.288 163.725 171.398 1.00 22.77  ? 615  VAL B CG1   1 
ATOM   15522 C  CG2   . VAL B 2  615  ? 123.194 163.340 172.662 1.00 25.42  ? 615  VAL B CG2   1 
ATOM   15523 N  N     . PHE B 2  616  ? 126.210 160.654 170.264 1.00 20.29  ? 616  PHE B N     1 
ATOM   15524 C  CA    . PHE B 2  616  ? 127.505 160.141 169.843 1.00 22.14  ? 616  PHE B CA    1 
ATOM   15525 C  C     . PHE B 2  616  ? 128.251 161.205 169.054 1.00 25.79  ? 616  PHE B C     1 
ATOM   15526 O  O     . PHE B 2  616  ? 127.644 162.018 168.357 1.00 28.62  ? 616  PHE B O     1 
ATOM   15527 C  CB    . PHE B 2  616  ? 127.359 158.892 168.974 1.00 16.82  ? 616  PHE B CB    1 
ATOM   15528 C  CG    . PHE B 2  616  ? 126.734 157.725 169.674 1.00 26.49  ? 616  PHE B CG    1 
ATOM   15529 C  CD1   . PHE B 2  616  ? 125.452 157.800 170.174 1.00 26.16  ? 616  PHE B CD1   1 
ATOM   15530 C  CD2   . PHE B 2  616  ? 127.428 156.544 169.824 1.00 30.01  ? 616  PHE B CD2   1 
ATOM   15531 C  CE1   . PHE B 2  616  ? 124.882 156.729 170.811 1.00 28.23  ? 616  PHE B CE1   1 
ATOM   15532 C  CE2   . PHE B 2  616  ? 126.858 155.471 170.457 1.00 28.62  ? 616  PHE B CE2   1 
ATOM   15533 C  CZ    . PHE B 2  616  ? 125.583 155.567 170.954 1.00 28.74  ? 616  PHE B CZ    1 
ATOM   15534 N  N     . ILE B 2  617  ? 129.574 161.211 169.177 1.00 21.69  ? 617  ILE B N     1 
ATOM   15535 C  CA    . ILE B 2  617  ? 130.419 161.987 168.279 1.00 20.51  ? 617  ILE B CA    1 
ATOM   15536 C  C     . ILE B 2  617  ? 131.501 161.074 167.732 1.00 18.41  ? 617  ILE B C     1 
ATOM   15537 O  O     . ILE B 2  617  ? 132.208 160.408 168.494 1.00 23.72  ? 617  ILE B O     1 
ATOM   15538 C  CB    . ILE B 2  617  ? 131.026 163.239 168.936 1.00 22.77  ? 617  ILE B CB    1 
ATOM   15539 C  CG1   . ILE B 2  617  ? 131.708 164.085 167.863 1.00 22.08  ? 617  ILE B CG1   1 
ATOM   15540 C  CG2   . ILE B 2  617  ? 131.982 162.896 170.059 1.00 28.65  ? 617  ILE B CG2   1 
ATOM   15541 C  CD1   . ILE B 2  617  ? 132.544 165.207 168.394 1.00 24.87  ? 617  ILE B CD1   1 
ATOM   15542 N  N     . ASN B 2  618  ? 131.586 161.003 166.410 1.00 23.71  ? 618  ASN B N     1 
ATOM   15543 C  CA    . ASN B 2  618  ? 132.598 160.244 165.689 1.00 18.89  ? 618  ASN B CA    1 
ATOM   15544 C  C     . ASN B 2  618  ? 132.652 158.785 166.118 1.00 19.59  ? 618  ASN B C     1 
ATOM   15545 O  O     . ASN B 2  618  ? 133.675 158.127 165.944 1.00 25.85  ? 618  ASN B O     1 
ATOM   15546 C  CB    . ASN B 2  618  ? 133.969 160.908 165.829 1.00 23.01  ? 618  ASN B CB    1 
ATOM   15547 C  CG    . ASN B 2  618  ? 134.785 160.823 164.566 1.00 25.90  ? 618  ASN B CG    1 
ATOM   15548 O  OD1   . ASN B 2  618  ? 134.505 160.011 163.695 1.00 27.61  ? 618  ASN B OD1   1 
ATOM   15549 N  ND2   . ASN B 2  618  ? 135.777 161.690 164.442 1.00 26.56  ? 618  ASN B ND2   1 
ATOM   15550 N  N     . GLY B 2  619  ? 131.558 158.260 166.675 1.00 24.56  ? 619  GLY B N     1 
ATOM   15551 C  CA    . GLY B 2  619  ? 131.419 156.844 166.972 1.00 24.76  ? 619  GLY B CA    1 
ATOM   15552 C  C     . GLY B 2  619  ? 131.209 156.530 168.442 1.00 27.74  ? 619  GLY B C     1 
ATOM   15553 O  O     . GLY B 2  619  ? 130.609 155.503 168.768 1.00 30.86  ? 619  GLY B O     1 
ATOM   15554 N  N     . GLU B 2  620  ? 131.686 157.391 169.331 1.00 30.01  ? 620  GLU B N     1 
ATOM   15555 C  CA    . GLU B 2  620  ? 131.721 157.100 170.757 1.00 31.54  ? 620  GLU B CA    1 
ATOM   15556 C  C     . GLU B 2  620  ? 130.642 157.858 171.523 1.00 33.90  ? 620  GLU B C     1 
ATOM   15557 O  O     . GLU B 2  620  ? 130.344 159.018 171.237 1.00 36.39  ? 620  GLU B O     1 
ATOM   15558 C  CB    . GLU B 2  620  ? 133.105 157.420 171.321 1.00 33.99  ? 620  GLU B CB    1 
ATOM   15559 C  CG    . GLU B 2  620  ? 133.436 158.890 171.405 1.00 35.13  ? 620  GLU B CG    1 
ATOM   15560 C  CD    . GLU B 2  620  ? 134.648 159.152 172.259 1.00 38.77  ? 620  GLU B CD    1 
ATOM   15561 O  OE1   . GLU B 2  620  ? 135.264 158.171 172.722 1.00 37.91  ? 620  GLU B OE1   1 
ATOM   15562 O  OE2   . GLU B 2  620  ? 134.993 160.333 172.457 1.00 38.85  ? 620  GLU B OE2   1 
ATOM   15563 N  N     . TRP B 2  621  ? 130.063 157.179 172.509 1.00 28.90  ? 621  TRP B N     1 
ATOM   15564 C  CA    . TRP B 2  621  ? 128.924 157.684 173.262 1.00 29.43  ? 621  TRP B CA    1 
ATOM   15565 C  C     . TRP B 2  621  ? 129.411 158.631 174.347 1.00 30.56  ? 621  TRP B C     1 
ATOM   15566 O  O     . TRP B 2  621  ? 130.169 158.228 175.232 1.00 39.13  ? 621  TRP B O     1 
ATOM   15567 C  CB    . TRP B 2  621  ? 128.147 156.511 173.862 1.00 30.30  ? 621  TRP B CB    1 
ATOM   15568 C  CG    . TRP B 2  621  ? 126.971 156.874 174.703 1.00 31.92  ? 621  TRP B CG    1 
ATOM   15569 C  CD1   . TRP B 2  621  ? 126.321 158.064 174.736 1.00 28.55  ? 621  TRP B CD1   1 
ATOM   15570 C  CD2   . TRP B 2  621  ? 126.297 156.023 175.633 1.00 35.27  ? 621  TRP B CD2   1 
ATOM   15571 N  NE1   . TRP B 2  621  ? 125.288 158.018 175.635 1.00 29.14  ? 621  TRP B NE1   1 
ATOM   15572 C  CE2   . TRP B 2  621  ? 125.249 156.770 176.197 1.00 34.66  ? 621  TRP B CE2   1 
ATOM   15573 C  CE3   . TRP B 2  621  ? 126.483 154.702 176.049 1.00 34.90  ? 621  TRP B CE3   1 
ATOM   15574 C  CZ2   . TRP B 2  621  ? 124.396 156.244 177.162 1.00 32.04  ? 621  TRP B CZ2   1 
ATOM   15575 C  CZ3   . TRP B 2  621  ? 125.631 154.180 176.998 1.00 32.90  ? 621  TRP B CZ3   1 
ATOM   15576 C  CH2   . TRP B 2  621  ? 124.598 154.948 177.542 1.00 31.28  ? 621  TRP B CH2   1 
ATOM   15577 N  N     . ILE B 2  622  ? 128.986 159.888 174.280 1.00 24.72  ? 622  ILE B N     1 
ATOM   15578 C  CA    . ILE B 2  622  ? 129.586 160.907 175.133 1.00 28.39  ? 622  ILE B CA    1 
ATOM   15579 C  C     . ILE B 2  622  ? 128.550 161.609 175.998 1.00 33.42  ? 622  ILE B C     1 
ATOM   15580 O  O     . ILE B 2  622  ? 128.838 162.656 176.585 1.00 33.22  ? 622  ILE B O     1 
ATOM   15581 C  CB    . ILE B 2  622  ? 130.355 161.945 174.300 1.00 27.80  ? 622  ILE B CB    1 
ATOM   15582 C  CG1   . ILE B 2  622  ? 129.381 162.778 173.470 1.00 29.23  ? 622  ILE B CG1   1 
ATOM   15583 C  CG2   . ILE B 2  622  ? 131.377 161.261 173.416 1.00 28.85  ? 622  ILE B CG2   1 
ATOM   15584 C  CD1   . ILE B 2  622  ? 129.829 164.187 173.242 1.00 29.72  ? 622  ILE B CD1   1 
ATOM   15585 N  N     . GLY B 2  623  ? 127.355 161.062 176.092 1.00 31.37  ? 623  GLY B N     1 
ATOM   15586 C  CA    . GLY B 2  623  ? 126.357 161.639 176.963 1.00 31.53  ? 623  GLY B CA    1 
ATOM   15587 C  C     . GLY B 2  623  ? 124.955 161.263 176.535 1.00 34.59  ? 623  GLY B C     1 
ATOM   15588 O  O     . GLY B 2  623  ? 124.736 160.274 175.848 1.00 35.18  ? 623  GLY B O     1 
ATOM   15589 N  N     . CYS B 2  624  ? 124.006 162.072 176.998 1.00 35.67  ? 624  CYS B N     1 
ATOM   15590 C  CA    . CYS B 2  624  ? 122.596 161.919 176.684 1.00 34.90  ? 624  CYS B CA    1 
ATOM   15591 C  C     . CYS B 2  624  ? 121.936 163.286 176.713 1.00 36.91  ? 624  CYS B C     1 
ATOM   15592 O  O     . CYS B 2  624  ? 122.440 164.213 177.351 1.00 37.73  ? 624  CYS B O     1 
ATOM   15593 C  CB    . CYS B 2  624  ? 121.893 160.974 177.662 1.00 36.61  ? 624  CYS B CB    1 
ATOM   15594 S  SG    . CYS B 2  624  ? 122.225 159.219 177.401 1.00 45.47  ? 624  CYS B SG    1 
ATOM   15595 N  N     . CYS B 2  625  ? 120.819 163.413 176.009 1.00 36.89  ? 625  CYS B N     1 
ATOM   15596 C  CA    . CYS B 2  625  ? 120.073 164.657 175.936 1.00 36.18  ? 625  CYS B CA    1 
ATOM   15597 C  C     . CYS B 2  625  ? 118.585 164.394 176.109 1.00 37.29  ? 625  CYS B C     1 
ATOM   15598 O  O     . CYS B 2  625  ? 118.106 163.268 175.961 1.00 35.07  ? 625  CYS B O     1 
ATOM   15599 C  CB    . CYS B 2  625  ? 120.330 165.373 174.608 1.00 37.83  ? 625  CYS B CB    1 
ATOM   15600 S  SG    . CYS B 2  625  ? 119.354 164.752 173.226 1.00 54.76  ? 625  CYS B SG    1 
ATOM   15601 N  N     . THR B 2  626  ? 117.853 165.459 176.423 1.00 37.33  ? 626  THR B N     1 
ATOM   15602 C  CA    . THR B 2  626  ? 116.416 165.330 176.631 1.00 38.47  ? 626  THR B CA    1 
ATOM   15603 C  C     . THR B 2  626  ? 115.676 165.232 175.304 1.00 42.47  ? 626  THR B C     1 
ATOM   15604 O  O     . THR B 2  626  ? 114.866 164.321 175.099 1.00 44.32  ? 626  THR B O     1 
ATOM   15605 C  CB    . THR B 2  626  ? 115.896 166.518 177.435 1.00 39.51  ? 626  THR B CB    1 
ATOM   15606 O  OG1   . THR B 2  626  ? 115.541 167.573 176.537 1.00 41.08  ? 626  THR B OG1   1 
ATOM   15607 C  CG2   . THR B 2  626  ? 116.966 167.024 178.376 1.00 39.41  ? 626  THR B CG2   1 
ATOM   15608 N  N     . ASN B 2  627  ? 115.938 166.164 174.392 1.00 38.70  ? 627  ASN B N     1 
ATOM   15609 C  CA    . ASN B 2  627  ? 115.223 166.268 173.122 1.00 34.91  ? 627  ASN B CA    1 
ATOM   15610 C  C     . ASN B 2  627  ? 116.230 166.134 171.985 1.00 38.42  ? 627  ASN B C     1 
ATOM   15611 O  O     . ASN B 2  627  ? 116.988 167.067 171.709 1.00 40.90  ? 627  ASN B O     1 
ATOM   15612 C  CB    . ASN B 2  627  ? 114.478 167.593 173.047 1.00 37.45  ? 627  ASN B CB    1 
ATOM   15613 C  CG    . ASN B 2  627  ? 113.287 167.536 172.134 1.00 40.29  ? 627  ASN B CG    1 
ATOM   15614 O  OD1   . ASN B 2  627  ? 112.922 166.473 171.639 1.00 41.57  ? 627  ASN B OD1   1 
ATOM   15615 N  ND2   . ASN B 2  627  ? 112.673 168.684 171.898 1.00 35.72  ? 627  ASN B ND2   1 
ATOM   15616 N  N     . ALA B 2  628  ? 116.233 164.982 171.314 1.00 35.19  ? 628  ALA B N     1 
ATOM   15617 C  CA    . ALA B 2  628  ? 117.214 164.746 170.258 1.00 31.91  ? 628  ALA B CA    1 
ATOM   15618 C  C     . ALA B 2  628  ? 116.968 165.640 169.052 1.00 28.93  ? 628  ALA B C     1 
ATOM   15619 O  O     . ALA B 2  628  ? 117.916 166.143 168.438 1.00 31.89  ? 628  ALA B O     1 
ATOM   15620 C  CB    . ALA B 2  628  ? 117.197 163.278 169.848 1.00 33.48  ? 628  ALA B CB    1 
ATOM   15621 N  N     . PHE B 2  629  ? 115.703 165.841 168.692 1.00 30.02  ? 629  PHE B N     1 
ATOM   15622 C  CA    . PHE B 2  629  ? 115.370 166.659 167.533 1.00 28.95  ? 629  PHE B CA    1 
ATOM   15623 C  C     . PHE B 2  629  ? 115.840 168.093 167.717 1.00 30.63  ? 629  PHE B C     1 
ATOM   15624 O  O     . PHE B 2  629  ? 116.419 168.696 166.803 1.00 35.37  ? 629  PHE B O     1 
ATOM   15625 C  CB    . PHE B 2  629  ? 113.864 166.612 167.295 1.00 32.06  ? 629  PHE B CB    1 
ATOM   15626 C  CG    . PHE B 2  629  ? 113.382 167.586 166.267 1.00 33.25  ? 629  PHE B CG    1 
ATOM   15627 C  CD1   . PHE B 2  629  ? 113.744 167.446 164.944 1.00 34.20  ? 629  PHE B CD1   1 
ATOM   15628 C  CD2   . PHE B 2  629  ? 112.562 168.637 166.625 1.00 30.32  ? 629  PHE B CD2   1 
ATOM   15629 C  CE1   . PHE B 2  629  ? 113.304 168.340 164.001 1.00 33.73  ? 629  PHE B CE1   1 
ATOM   15630 C  CE2   . PHE B 2  629  ? 112.119 169.529 165.686 1.00 29.16  ? 629  PHE B CE2   1 
ATOM   15631 C  CZ    . PHE B 2  629  ? 112.491 169.380 164.371 1.00 33.56  ? 629  PHE B CZ    1 
ATOM   15632 N  N     . GLU B 2  630  ? 115.607 168.654 168.902 1.00 33.85  ? 630  GLU B N     1 
ATOM   15633 C  CA    . GLU B 2  630  ? 116.018 170.025 169.167 1.00 38.88  ? 630  GLU B CA    1 
ATOM   15634 C  C     . GLU B 2  630  ? 117.531 170.180 169.088 1.00 39.19  ? 630  GLU B C     1 
ATOM   15635 O  O     . GLU B 2  630  ? 118.029 171.159 168.525 1.00 38.80  ? 630  GLU B O     1 
ATOM   15636 C  CB    . GLU B 2  630  ? 115.504 170.462 170.532 1.00 40.87  ? 630  GLU B CB    1 
ATOM   15637 C  CG    . GLU B 2  630  ? 115.549 171.955 170.756 1.00 41.94  ? 630  GLU B CG    1 
ATOM   15638 C  CD    . GLU B 2  630  ? 115.098 172.335 172.146 1.00 43.05  ? 630  GLU B CD    1 
ATOM   15639 O  OE1   . GLU B 2  630  ? 114.523 171.468 172.835 1.00 43.17  ? 630  GLU B OE1   1 
ATOM   15640 O  OE2   . GLU B 2  630  ? 115.313 173.496 172.549 1.00 42.81  ? 630  GLU B OE2   1 
ATOM   15641 N  N     . LEU B 2  631  ? 118.280 169.230 169.650 1.00 31.61  ? 631  LEU B N     1 
ATOM   15642 C  CA    . LEU B 2  631  ? 119.737 169.306 169.595 1.00 31.39  ? 631  LEU B CA    1 
ATOM   15643 C  C     . LEU B 2  631  ? 120.245 169.199 168.165 1.00 30.99  ? 631  LEU B C     1 
ATOM   15644 O  O     . LEU B 2  631  ? 121.110 169.977 167.739 1.00 34.06  ? 631  LEU B O     1 
ATOM   15645 C  CB    . LEU B 2  631  ? 120.354 168.208 170.461 1.00 32.73  ? 631  LEU B CB    1 
ATOM   15646 C  CG    . LEU B 2  631  ? 121.848 168.340 170.748 1.00 28.86  ? 631  LEU B CG    1 
ATOM   15647 C  CD1   . LEU B 2  631  ? 122.066 169.032 172.072 1.00 33.75  ? 631  LEU B CD1   1 
ATOM   15648 C  CD2   . LEU B 2  631  ? 122.497 166.978 170.751 1.00 30.34  ? 631  LEU B CD2   1 
ATOM   15649 N  N     . ALA B 2  632  ? 119.719 168.233 167.408 1.00 30.60  ? 632  ALA B N     1 
ATOM   15650 C  CA    . ALA B 2  632  ? 120.157 168.068 166.029 1.00 23.67  ? 632  ALA B CA    1 
ATOM   15651 C  C     . ALA B 2  632  ? 119.902 169.328 165.224 1.00 25.99  ? 632  ALA B C     1 
ATOM   15652 O  O     . ALA B 2  632  ? 120.783 169.798 164.498 1.00 31.63  ? 632  ALA B O     1 
ATOM   15653 C  CB    . ALA B 2  632  ? 119.449 166.878 165.389 1.00 23.96  ? 632  ALA B CB    1 
ATOM   15654 N  N     . GLN B 2  633  ? 118.714 169.915 165.364 1.00 26.35  ? 633  GLN B N     1 
ATOM   15655 C  CA    . GLN B 2  633  ? 118.401 171.080 164.552 1.00 30.20  ? 633  GLN B CA    1 
ATOM   15656 C  C     . GLN B 2  633  ? 119.137 172.325 165.034 1.00 32.45  ? 633  GLN B C     1 
ATOM   15657 O  O     . GLN B 2  633  ? 119.490 173.185 164.219 1.00 35.39  ? 633  GLN B O     1 
ATOM   15658 C  CB    . GLN B 2  633  ? 116.887 171.283 164.506 1.00 30.50  ? 633  GLN B CB    1 
ATOM   15659 C  CG    . GLN B 2  633  ? 116.272 171.973 165.689 1.00 32.76  ? 633  GLN B CG    1 
ATOM   15660 C  CD    . GLN B 2  633  ? 114.843 172.383 165.417 1.00 35.78  ? 633  GLN B CD    1 
ATOM   15661 O  OE1   . GLN B 2  633  ? 114.450 172.563 164.267 1.00 35.47  ? 633  GLN B OE1   1 
ATOM   15662 N  NE2   . GLN B 2  633  ? 114.053 172.530 166.474 1.00 36.16  ? 633  GLN B NE2   1 
ATOM   15663 N  N     . ARG B 2  634  ? 119.426 172.426 166.332 1.00 35.96  ? 634  ARG B N     1 
ATOM   15664 C  CA    . ARG B 2  634  ? 120.229 173.545 166.815 1.00 37.63  ? 634  ARG B CA    1 
ATOM   15665 C  C     . ARG B 2  634  ? 121.646 173.493 166.264 1.00 35.11  ? 634  ARG B C     1 
ATOM   15666 O  O     . ARG B 2  634  ? 122.185 174.512 165.818 1.00 36.17  ? 634  ARG B O     1 
ATOM   15667 C  CB    . ARG B 2  634  ? 120.252 173.553 168.338 1.00 36.42  ? 634  ARG B CB    1 
ATOM   15668 C  CG    . ARG B 2  634  ? 119.289 174.535 168.961 1.00 38.39  ? 634  ARG B CG    1 
ATOM   15669 C  CD    . ARG B 2  634  ? 119.697 174.888 170.387 1.00 38.41  ? 634  ARG B CD    1 
ATOM   15670 N  NE    . ARG B 2  634  ? 121.143 174.976 170.538 1.00 41.35  ? 634  ARG B NE    1 
ATOM   15671 C  CZ    . ARG B 2  634  ? 121.880 174.097 171.201 1.00 40.89  ? 634  ARG B CZ    1 
ATOM   15672 N  NH1   . ARG B 2  634  ? 121.339 173.039 171.779 1.00 40.82  ? 634  ARG B NH1   1 
ATOM   15673 N  NH2   . ARG B 2  634  ? 123.192 174.281 171.282 1.00 36.52  ? 634  ARG B NH2   1 
ATOM   15674 N  N     . TYR B 2  635  ? 122.265 172.316 166.272 1.00 28.97  ? 635  TYR B N     1 
ATOM   15675 C  CA    . TYR B 2  635  ? 123.622 172.251 165.748 1.00 30.01  ? 635  TYR B CA    1 
ATOM   15676 C  C     . TYR B 2  635  ? 123.647 172.331 164.230 1.00 31.22  ? 635  TYR B C     1 
ATOM   15677 O  O     . TYR B 2  635  ? 124.646 172.778 163.660 1.00 30.61  ? 635  TYR B O     1 
ATOM   15678 C  CB    . TYR B 2  635  ? 124.335 170.998 166.239 1.00 28.17  ? 635  TYR B CB    1 
ATOM   15679 C  CG    . TYR B 2  635  ? 124.972 171.207 167.586 1.00 32.01  ? 635  TYR B CG    1 
ATOM   15680 C  CD1   . TYR B 2  635  ? 124.237 171.699 168.652 1.00 32.73  ? 635  TYR B CD1   1 
ATOM   15681 C  CD2   . TYR B 2  635  ? 126.322 170.975 167.778 1.00 33.64  ? 635  TYR B CD2   1 
ATOM   15682 C  CE1   . TYR B 2  635  ? 124.817 171.906 169.881 1.00 31.98  ? 635  TYR B CE1   1 
ATOM   15683 C  CE2   . TYR B 2  635  ? 126.910 171.186 169.003 1.00 31.23  ? 635  TYR B CE2   1 
ATOM   15684 C  CZ    . TYR B 2  635  ? 126.152 171.650 170.049 1.00 30.63  ? 635  TYR B CZ    1 
ATOM   15685 O  OH    . TYR B 2  635  ? 126.734 171.863 171.273 1.00 35.53  ? 635  TYR B OH    1 
ATOM   15686 N  N     . ARG B 2  636  ? 122.569 171.921 163.556 1.00 31.74  ? 636  ARG B N     1 
ATOM   15687 C  CA    . ARG B 2  636  ? 122.475 172.177 162.121 1.00 25.75  ? 636  ARG B CA    1 
ATOM   15688 C  C     . ARG B 2  636  ? 122.406 173.669 161.839 1.00 25.78  ? 636  ARG B C     1 
ATOM   15689 O  O     . ARG B 2  636  ? 123.012 174.151 160.879 1.00 28.57  ? 636  ARG B O     1 
ATOM   15690 C  CB    . ARG B 2  636  ? 121.263 171.469 161.528 1.00 19.25  ? 636  ARG B CB    1 
ATOM   15691 C  CG    . ARG B 2  636  ? 121.537 170.049 161.123 1.00 22.36  ? 636  ARG B CG    1 
ATOM   15692 C  CD    . ARG B 2  636  ? 120.260 169.284 160.937 1.00 19.65  ? 636  ARG B CD    1 
ATOM   15693 N  NE    . ARG B 2  636  ? 120.522 167.884 160.651 1.00 14.13  ? 636  ARG B NE    1 
ATOM   15694 C  CZ    . ARG B 2  636  ? 119.630 166.920 160.800 1.00 19.25  ? 636  ARG B CZ    1 
ATOM   15695 N  NH1   . ARG B 2  636  ? 118.402 167.177 161.204 1.00 21.45  ? 636  ARG B NH1   1 
ATOM   15696 N  NH2   . ARG B 2  636  ? 119.979 165.668 160.533 1.00 21.30  ? 636  ARG B NH2   1 
ATOM   15697 N  N     . MET B 2  637  ? 121.661 174.414 162.653 1.00 29.36  ? 637  MET B N     1 
ATOM   15698 C  CA    . MET B 2  637  ? 121.621 175.859 162.476 1.00 28.52  ? 637  MET B CA    1 
ATOM   15699 C  C     . MET B 2  637  ? 122.976 176.489 162.770 1.00 31.64  ? 637  MET B C     1 
ATOM   15700 O  O     . MET B 2  637  ? 123.340 177.500 162.160 1.00 37.30  ? 637  MET B O     1 
ATOM   15701 C  CB    . MET B 2  637  ? 120.537 176.466 163.360 1.00 29.22  ? 637  MET B CB    1 
ATOM   15702 C  CG    . MET B 2  637  ? 119.220 176.693 162.641 1.00 33.30  ? 637  MET B CG    1 
ATOM   15703 S  SD    . MET B 2  637  ? 119.428 176.937 160.869 1.00 45.43  ? 637  MET B SD    1 
ATOM   15704 C  CE    . MET B 2  637  ? 119.525 178.723 160.781 1.00 35.08  ? 637  MET B CE    1 
ATOM   15705 N  N     . LEU B 2  638  ? 123.725 175.924 163.718 1.00 29.81  ? 638  LEU B N     1 
ATOM   15706 C  CA    . LEU B 2  638  ? 125.081 176.410 163.962 1.00 28.97  ? 638  LEU B CA    1 
ATOM   15707 C  C     . LEU B 2  638  ? 125.995 176.136 162.774 1.00 31.38  ? 638  LEU B C     1 
ATOM   15708 O  O     . LEU B 2  638  ? 126.808 176.986 162.403 1.00 32.09  ? 638  LEU B O     1 
ATOM   15709 C  CB    . LEU B 2  638  ? 125.667 175.774 165.221 1.00 31.25  ? 638  LEU B CB    1 
ATOM   15710 C  CG    . LEU B 2  638  ? 125.132 176.169 166.595 1.00 30.37  ? 638  LEU B CG    1 
ATOM   15711 C  CD1   . LEU B 2  638  ? 125.890 175.411 167.660 1.00 28.49  ? 638  LEU B CD1   1 
ATOM   15712 C  CD2   . LEU B 2  638  ? 125.245 177.653 166.812 1.00 28.82  ? 638  LEU B CD2   1 
ATOM   15713 N  N     . ARG B 2  639  ? 125.887 174.947 162.174 1.00 29.29  ? 639  ARG B N     1 
ATOM   15714 C  CA    . ARG B 2  639  ? 126.751 174.595 161.051 1.00 22.54  ? 639  ARG B CA    1 
ATOM   15715 C  C     . ARG B 2  639  ? 126.554 175.537 159.876 1.00 25.52  ? 639  ARG B C     1 
ATOM   15716 O  O     . ARG B 2  639  ? 127.446 175.678 159.035 1.00 27.28  ? 639  ARG B O     1 
ATOM   15717 C  CB    . ARG B 2  639  ? 126.481 173.158 160.618 1.00 22.33  ? 639  ARG B CB    1 
ATOM   15718 C  CG    . ARG B 2  639  ? 127.372 172.643 159.511 1.00 21.59  ? 639  ARG B CG    1 
ATOM   15719 C  CD    . ARG B 2  639  ? 126.990 171.237 159.127 1.00 23.16  ? 639  ARG B CD    1 
ATOM   15720 N  NE    . ARG B 2  639  ? 125.582 171.141 158.776 1.00 24.70  ? 639  ARG B NE    1 
ATOM   15721 C  CZ    . ARG B 2  639  ? 124.971 170.015 158.443 1.00 21.89  ? 639  ARG B CZ    1 
ATOM   15722 N  NH1   . ARG B 2  639  ? 125.616 168.865 158.409 1.00 18.42  ? 639  ARG B NH1   1 
ATOM   15723 N  NH2   . ARG B 2  639  ? 123.679 170.044 158.139 1.00 22.70  ? 639  ARG B NH2   1 
ATOM   15724 N  N     . ARG B 2  640  ? 125.401 176.194 159.803 1.00 29.42  ? 640  ARG B N     1 
ATOM   15725 C  CA    . ARG B 2  640  ? 125.115 177.053 158.668 1.00 27.91  ? 640  ARG B CA    1 
ATOM   15726 C  C     . ARG B 2  640  ? 125.890 178.363 158.727 1.00 36.44  ? 640  ARG B C     1 
ATOM   15727 O  O     . ARG B 2  640  ? 126.251 178.906 157.677 1.00 39.09  ? 640  ARG B O     1 
ATOM   15728 C  CB    . ARG B 2  640  ? 123.616 177.311 158.587 1.00 28.48  ? 640  ARG B CB    1 
ATOM   15729 C  CG    . ARG B 2  640  ? 123.183 177.828 157.248 1.00 32.69  ? 640  ARG B CG    1 
ATOM   15730 C  CD    . ARG B 2  640  ? 121.785 178.372 157.293 1.00 35.95  ? 640  ARG B CD    1 
ATOM   15731 N  NE    . ARG B 2  640  ? 120.786 177.321 157.388 1.00 33.64  ? 640  ARG B NE    1 
ATOM   15732 C  CZ    . ARG B 2  640  ? 119.636 177.337 156.733 1.00 33.59  ? 640  ARG B CZ    1 
ATOM   15733 N  NH1   . ARG B 2  640  ? 119.308 178.342 155.942 1.00 31.29  ? 640  ARG B NH1   1 
ATOM   15734 N  NH2   . ARG B 2  640  ? 118.792 176.322 156.882 1.00 33.32  ? 640  ARG B NH2   1 
ATOM   15735 N  N     . GLU B 2  641  ? 126.147 178.899 159.925 1.00 39.06  ? 641  GLU B N     1 
ATOM   15736 C  CA    . GLU B 2  641  ? 126.955 180.114 160.012 1.00 37.56  ? 641  GLU B CA    1 
ATOM   15737 C  C     . GLU B 2  641  ? 128.438 179.810 159.831 1.00 36.39  ? 641  GLU B C     1 
ATOM   15738 O  O     . GLU B 2  641  ? 129.195 180.676 159.386 1.00 38.79  ? 641  GLU B O     1 
ATOM   15739 C  CB    . GLU B 2  641  ? 126.688 180.847 161.331 1.00 37.14  ? 641  GLU B CB    1 
ATOM   15740 C  CG    . GLU B 2  641  ? 126.887 180.043 162.609 1.00 40.37  ? 641  GLU B CG    1 
ATOM   15741 C  CD    . GLU B 2  641  ? 128.350 179.867 162.994 1.00 42.24  ? 641  GLU B CD    1 
ATOM   15742 O  OE1   . GLU B 2  641  ? 128.876 178.742 162.883 1.00 39.36  ? 641  GLU B OE1   1 
ATOM   15743 O  OE2   . GLU B 2  641  ? 128.965 180.853 163.443 1.00 42.26  ? 641  GLU B OE2   1 
ATOM   15744 N  N     . GLY B 2  642  ? 128.869 178.597 160.167 1.00 33.42  ? 642  GLY B N     1 
ATOM   15745 C  CA    . GLY B 2  642  ? 130.162 178.100 159.746 1.00 35.37  ? 642  GLY B CA    1 
ATOM   15746 C  C     . GLY B 2  642  ? 131.323 178.339 160.683 1.00 37.98  ? 642  GLY B C     1 
ATOM   15747 O  O     . GLY B 2  642  ? 132.427 177.855 160.400 1.00 38.66  ? 642  GLY B O     1 
ATOM   15748 N  N     . LYS B 2  643  ? 131.123 179.058 161.787 1.00 40.49  ? 643  LYS B N     1 
ATOM   15749 C  CA    . LYS B 2  643  ? 132.208 179.384 162.707 1.00 38.61  ? 643  LYS B CA    1 
ATOM   15750 C  C     . LYS B 2  643  ? 132.247 178.485 163.932 1.00 40.02  ? 643  LYS B C     1 
ATOM   15751 O  O     . LYS B 2  643  ? 133.331 178.106 164.381 1.00 43.63  ? 643  LYS B O     1 
ATOM   15752 C  CB    . LYS B 2  643  ? 132.099 180.848 163.136 1.00 38.59  ? 643  LYS B CB    1 
ATOM   15753 C  CG    . LYS B 2  643  ? 131.905 181.784 161.957 1.00 38.31  ? 643  LYS B CG    1 
ATOM   15754 C  CD    . LYS B 2  643  ? 133.026 181.581 160.943 1.00 39.85  ? 643  LYS B CD    1 
ATOM   15755 C  CE    . LYS B 2  643  ? 132.979 182.585 159.807 1.00 40.27  ? 643  LYS B CE    1 
ATOM   15756 N  NZ    . LYS B 2  643  ? 131.741 182.465 158.996 1.00 41.15  ? 643  LYS B NZ    1 
ATOM   15757 N  N     . VAL B 2  644  ? 131.093 178.127 164.479 1.00 34.11  ? 644  VAL B N     1 
ATOM   15758 C  CA    . VAL B 2  644  ? 131.034 177.238 165.633 1.00 36.59  ? 644  VAL B CA    1 
ATOM   15759 C  C     . VAL B 2  644  ? 131.189 175.784 165.219 1.00 34.95  ? 644  VAL B C     1 
ATOM   15760 O  O     . VAL B 2  644  ? 131.946 175.028 165.833 1.00 34.52  ? 644  VAL B O     1 
ATOM   15761 C  CB    . VAL B 2  644  ? 129.717 177.472 166.398 1.00 39.82  ? 644  VAL B CB    1 
ATOM   15762 C  CG1   . VAL B 2  644  ? 129.576 176.477 167.524 1.00 34.39  ? 644  VAL B CG1   1 
ATOM   15763 C  CG2   . VAL B 2  644  ? 129.673 178.888 166.929 1.00 35.70  ? 644  VAL B CG2   1 
ATOM   15764 N  N     . VAL B 2  645  ? 130.474 175.373 164.178 1.00 30.54  ? 645  VAL B N     1 
ATOM   15765 C  CA    . VAL B 2  645  ? 130.539 174.019 163.643 1.00 27.08  ? 645  VAL B CA    1 
ATOM   15766 C  C     . VAL B 2  645  ? 131.074 174.103 162.223 1.00 28.22  ? 645  VAL B C     1 
ATOM   15767 O  O     . VAL B 2  645  ? 130.635 174.945 161.434 1.00 30.54  ? 645  VAL B O     1 
ATOM   15768 C  CB    . VAL B 2  645  ? 129.158 173.335 163.678 1.00 28.63  ? 645  VAL B CB    1 
ATOM   15769 C  CG1   . VAL B 2  645  ? 129.267 171.878 163.274 1.00 26.19  ? 645  VAL B CG1   1 
ATOM   15770 C  CG2   . VAL B 2  645  ? 128.532 173.465 165.051 1.00 28.39  ? 645  VAL B CG2   1 
ATOM   15771 N  N     . HIS B 2  646  ? 132.042 173.255 161.907 1.00 27.32  ? 646  HIS B N     1 
ATOM   15772 C  CA    . HIS B 2  646  ? 132.618 173.275 160.573 1.00 23.97  ? 646  HIS B CA    1 
ATOM   15773 C  C     . HIS B 2  646  ? 131.587 172.802 159.550 1.00 29.62  ? 646  HIS B C     1 
ATOM   15774 O  O     . HIS B 2  646  ? 130.837 171.858 159.815 1.00 25.34  ? 646  HIS B O     1 
ATOM   15775 C  CB    . HIS B 2  646  ? 133.862 172.395 160.509 1.00 20.83  ? 646  HIS B CB    1 
ATOM   15776 C  CG    . HIS B 2  646  ? 134.659 172.580 159.259 1.00 24.95  ? 646  HIS B CG    1 
ATOM   15777 N  ND1   . HIS B 2  646  ? 134.518 171.765 158.159 1.00 28.79  ? 646  HIS B ND1   1 
ATOM   15778 C  CD2   . HIS B 2  646  ? 135.595 173.500 158.927 1.00 28.64  ? 646  HIS B CD2   1 
ATOM   15779 C  CE1   . HIS B 2  646  ? 135.336 172.170 157.205 1.00 28.34  ? 646  HIS B CE1   1 
ATOM   15780 N  NE2   . HIS B 2  646  ? 136.002 173.220 157.647 1.00 27.58  ? 646  HIS B NE2   1 
ATOM   15781 N  N     . PRO B 2  647  ? 131.538 173.425 158.370 1.00 31.01  ? 647  PRO B N     1 
ATOM   15782 C  CA    . PRO B 2  647  ? 130.492 173.080 157.392 1.00 27.90  ? 647  PRO B CA    1 
ATOM   15783 C  C     . PRO B 2  647  ? 130.510 171.641 156.915 1.00 24.14  ? 647  PRO B C     1 
ATOM   15784 O  O     . PRO B 2  647  ? 129.492 171.175 156.396 1.00 27.75  ? 647  PRO B O     1 
ATOM   15785 C  CB    . PRO B 2  647  ? 130.765 174.052 156.240 1.00 26.13  ? 647  PRO B CB    1 
ATOM   15786 C  CG    . PRO B 2  647  ? 131.443 175.205 156.888 1.00 24.41  ? 647  PRO B CG    1 
ATOM   15787 C  CD    . PRO B 2  647  ? 132.290 174.622 157.965 1.00 28.15  ? 647  PRO B CD    1 
ATOM   15788 N  N     . HIS B 2  648  ? 131.613 170.917 157.064 1.00 18.34  ? 648  HIS B N     1 
ATOM   15789 C  CA    . HIS B 2  648  ? 131.706 169.549 156.578 1.00 22.36  ? 648  HIS B CA    1 
ATOM   15790 C  C     . HIS B 2  648  ? 131.372 168.516 157.649 1.00 26.33  ? 648  HIS B C     1 
ATOM   15791 O  O     . HIS B 2  648  ? 131.831 167.376 157.564 1.00 28.21  ? 648  HIS B O     1 
ATOM   15792 C  CB    . HIS B 2  648  ? 133.098 169.295 156.006 1.00 23.45  ? 648  HIS B CB    1 
ATOM   15793 C  CG    . HIS B 2  648  ? 133.281 169.807 154.612 1.00 24.98  ? 648  HIS B CG    1 
ATOM   15794 N  ND1   . HIS B 2  648  ? 133.102 169.016 153.499 1.00 24.44  ? 648  HIS B ND1   1 
ATOM   15795 C  CD2   . HIS B 2  648  ? 133.623 171.032 154.151 1.00 26.15  ? 648  HIS B CD2   1 
ATOM   15796 C  CE1   . HIS B 2  648  ? 133.334 169.730 152.413 1.00 25.62  ? 648  HIS B CE1   1 
ATOM   15797 N  NE2   . HIS B 2  648  ? 133.648 170.957 152.781 1.00 25.57  ? 648  HIS B NE2   1 
ATOM   15798 N  N     . THR B 2  649  ? 130.561 168.880 158.635 1.00 20.86  ? 649  THR B N     1 
ATOM   15799 C  CA    . THR B 2  649  ? 130.209 167.981 159.726 1.00 20.55  ? 649  THR B CA    1 
ATOM   15800 C  C     . THR B 2  649  ? 128.885 167.285 159.436 1.00 22.13  ? 649  THR B C     1 
ATOM   15801 O  O     . THR B 2  649  ? 127.891 167.941 159.122 1.00 29.18  ? 649  THR B O     1 
ATOM   15802 C  CB    . THR B 2  649  ? 130.104 168.757 161.038 1.00 24.42  ? 649  THR B CB    1 
ATOM   15803 O  OG1   . THR B 2  649  ? 131.329 169.451 161.282 1.00 29.98  ? 649  THR B OG1   1 
ATOM   15804 C  CG2   . THR B 2  649  ? 129.842 167.820 162.192 1.00 17.77  ? 649  THR B CG2   1 
ATOM   15805 N  N     . THR B 2  650  ? 128.875 165.961 159.551 1.00 17.39  ? 650  THR B N     1 
ATOM   15806 C  CA    . THR B 2  650  ? 127.648 165.185 159.449 1.00 9.96   ? 650  THR B CA    1 
ATOM   15807 C  C     . THR B 2  650  ? 126.870 165.270 160.753 1.00 16.88  ? 650  THR B C     1 
ATOM   15808 O  O     . THR B 2  650  ? 127.453 165.186 161.834 1.00 26.53  ? 650  THR B O     1 
ATOM   15809 C  CB    . THR B 2  650  ? 127.969 163.729 159.128 1.00 10.45  ? 650  THR B CB    1 
ATOM   15810 O  OG1   . THR B 2  650  ? 128.697 163.656 157.903 1.00 16.80  ? 650  THR B OG1   1 
ATOM   15811 C  CG2   . THR B 2  650  ? 126.717 162.913 159.008 1.00 12.93  ? 650  THR B CG2   1 
ATOM   15812 N  N     . ILE B 2  651  ? 125.560 165.459 160.654 1.00 15.46  ? 651  ILE B N     1 
ATOM   15813 C  CA    . ILE B 2  651  ? 124.672 165.523 161.814 1.00 14.51  ? 651  ILE B CA    1 
ATOM   15814 C  C     . ILE B 2  651  ? 123.468 164.643 161.497 1.00 17.87  ? 651  ILE B C     1 
ATOM   15815 O  O     . ILE B 2  651  ? 122.512 165.070 160.849 1.00 23.53  ? 651  ILE B O     1 
ATOM   15816 C  CB    . ILE B 2  651  ? 124.244 166.952 162.149 1.00 14.16  ? 651  ILE B CB    1 
ATOM   15817 C  CG1   . ILE B 2  651  ? 125.464 167.844 162.344 1.00 18.57  ? 651  ILE B CG1   1 
ATOM   15818 C  CG2   . ILE B 2  651  ? 123.409 166.960 163.391 1.00 17.01  ? 651  ILE B CG2   1 
ATOM   15819 C  CD1   . ILE B 2  651  ? 125.143 169.304 162.444 1.00 19.09  ? 651  ILE B CD1   1 
ATOM   15820 N  N     . TYR B 2  652  ? 123.497 163.405 161.964 1.00 16.94  ? 652  TYR B N     1 
ATOM   15821 C  CA    . TYR B 2  652  ? 122.422 162.454 161.743 1.00 18.60  ? 652  TYR B CA    1 
ATOM   15822 C  C     . TYR B 2  652  ? 121.596 162.278 163.011 1.00 24.54  ? 652  TYR B C     1 
ATOM   15823 O  O     . TYR B 2  652  ? 122.117 162.335 164.123 1.00 30.87  ? 652  TYR B O     1 
ATOM   15824 C  CB    . TYR B 2  652  ? 122.991 161.114 161.286 1.00 18.84  ? 652  TYR B CB    1 
ATOM   15825 C  CG    . TYR B 2  652  ? 121.974 160.018 161.146 1.00 21.70  ? 652  TYR B CG    1 
ATOM   15826 C  CD1   . TYR B 2  652  ? 120.902 160.150 160.285 1.00 20.04  ? 652  TYR B CD1   1 
ATOM   15827 C  CD2   . TYR B 2  652  ? 122.106 158.835 161.843 1.00 23.53  ? 652  TYR B CD2   1 
ATOM   15828 C  CE1   . TYR B 2  652  ? 119.977 159.148 160.144 1.00 24.78  ? 652  TYR B CE1   1 
ATOM   15829 C  CE2   . TYR B 2  652  ? 121.189 157.829 161.709 1.00 23.17  ? 652  TYR B CE2   1 
ATOM   15830 C  CZ    . TYR B 2  652  ? 120.126 157.989 160.858 1.00 28.44  ? 652  TYR B CZ    1 
ATOM   15831 O  OH    . TYR B 2  652  ? 119.204 156.980 160.719 1.00 30.17  ? 652  TYR B OH    1 
ATOM   15832 N  N     . TRP B 2  653  ? 120.293 162.074 162.836 1.00 28.84  ? 653  TRP B N     1 
ATOM   15833 C  CA    . TRP B 2  653  ? 119.358 161.925 163.948 1.00 19.84  ? 653  TRP B CA    1 
ATOM   15834 C  C     . TRP B 2  653  ? 118.446 160.739 163.675 1.00 23.04  ? 653  TRP B C     1 
ATOM   15835 O  O     . TRP B 2  653  ? 117.566 160.819 162.819 1.00 28.52  ? 653  TRP B O     1 
ATOM   15836 C  CB    . TRP B 2  653  ? 118.543 163.199 164.157 1.00 17.49  ? 653  TRP B CB    1 
ATOM   15837 C  CG    . TRP B 2  653  ? 117.391 163.008 165.089 1.00 29.18  ? 653  TRP B CG    1 
ATOM   15838 C  CD1   . TRP B 2  653  ? 117.439 162.504 166.352 1.00 29.52  ? 653  TRP B CD1   1 
ATOM   15839 C  CD2   . TRP B 2  653  ? 116.018 163.322 164.837 1.00 31.37  ? 653  TRP B CD2   1 
ATOM   15840 N  NE1   . TRP B 2  653  ? 116.184 162.478 166.900 1.00 28.13  ? 653  TRP B NE1   1 
ATOM   15841 C  CE2   . TRP B 2  653  ? 115.293 162.977 165.991 1.00 29.97  ? 653  TRP B CE2   1 
ATOM   15842 C  CE3   . TRP B 2  653  ? 115.330 163.856 163.745 1.00 28.43  ? 653  TRP B CE3   1 
ATOM   15843 C  CZ2   . TRP B 2  653  ? 113.918 163.151 166.088 1.00 27.55  ? 653  TRP B CZ2   1 
ATOM   15844 C  CZ3   . TRP B 2  653  ? 113.965 164.028 163.845 1.00 28.26  ? 653  TRP B CZ3   1 
ATOM   15845 C  CH2   . TRP B 2  653  ? 113.274 163.676 165.007 1.00 27.51  ? 653  TRP B CH2   1 
ATOM   15846 N  N     . ASP B 2  654  ? 118.642 159.651 164.412 1.00 26.81  ? 654  ASP B N     1 
ATOM   15847 C  CA    . ASP B 2  654  ? 117.901 158.408 164.201 1.00 22.81  ? 654  ASP B CA    1 
ATOM   15848 C  C     . ASP B 2  654  ? 116.614 158.455 165.013 1.00 27.91  ? 654  ASP B C     1 
ATOM   15849 O  O     . ASP B 2  654  ? 116.621 158.224 166.218 1.00 32.66  ? 654  ASP B O     1 
ATOM   15850 C  CB    . ASP B 2  654  ? 118.754 157.211 164.592 1.00 23.59  ? 654  ASP B CB    1 
ATOM   15851 C  CG    . ASP B 2  654  ? 118.197 155.905 164.077 1.00 29.62  ? 654  ASP B CG    1 
ATOM   15852 O  OD1   . ASP B 2  654  ? 117.045 155.886 163.610 1.00 37.85  ? 654  ASP B OD1   1 
ATOM   15853 O  OD2   . ASP B 2  654  ? 118.912 154.889 164.140 1.00 29.63  ? 654  ASP B OD2   1 
ATOM   15854 N  N     . SER B 2  655  ? 115.497 158.732 164.345 1.00 32.32  ? 655  SER B N     1 
ATOM   15855 C  CA    . SER B 2  655  ? 114.223 158.880 165.035 1.00 30.07  ? 655  SER B CA    1 
ATOM   15856 C  C     . SER B 2  655  ? 113.580 157.548 165.390 1.00 30.04  ? 655  SER B C     1 
ATOM   15857 O  O     . SER B 2  655  ? 112.612 157.530 166.153 1.00 31.33  ? 655  SER B O     1 
ATOM   15858 C  CB    . SER B 2  655  ? 113.260 159.703 164.183 1.00 31.65  ? 655  SER B CB    1 
ATOM   15859 O  OG    . SER B 2  655  ? 113.019 159.068 162.946 1.00 33.25  ? 655  SER B OG    1 
ATOM   15860 N  N     . MET B 2  656  ? 114.075 156.439 164.846 1.00 31.01  ? 656  MET B N     1 
ATOM   15861 C  CA    . MET B 2  656  ? 113.516 155.143 165.199 1.00 33.08  ? 656  MET B CA    1 
ATOM   15862 C  C     . MET B 2  656  ? 113.982 154.685 166.574 1.00 39.14  ? 656  MET B C     1 
ATOM   15863 O  O     . MET B 2  656  ? 113.196 154.126 167.345 1.00 43.40  ? 656  MET B O     1 
ATOM   15864 C  CB    . MET B 2  656  ? 113.890 154.110 164.145 1.00 34.13  ? 656  MET B CB    1 
ATOM   15865 C  CG    . MET B 2  656  ? 113.226 152.770 164.346 1.00 40.96  ? 656  MET B CG    1 
ATOM   15866 S  SD    . MET B 2  656  ? 112.440 152.150 162.848 1.00 53.16  ? 656  MET B SD    1 
ATOM   15867 C  CE    . MET B 2  656  ? 113.840 152.146 161.737 1.00 38.98  ? 656  MET B CE    1 
ATOM   15868 N  N     . VAL B 2  657  ? 115.253 154.916 166.898 1.00 35.57  ? 657  VAL B N     1 
ATOM   15869 C  CA    . VAL B 2  657  ? 115.835 154.520 168.175 1.00 31.10  ? 657  VAL B CA    1 
ATOM   15870 C  C     . VAL B 2  657  ? 116.309 155.706 168.989 1.00 33.41  ? 657  VAL B C     1 
ATOM   15871 O  O     . VAL B 2  657  ? 116.868 155.510 170.075 1.00 37.95  ? 657  VAL B O     1 
ATOM   15872 C  CB    . VAL B 2  657  ? 116.982 153.517 167.974 1.00 30.20  ? 657  VAL B CB    1 
ATOM   15873 C  CG1   . VAL B 2  657  ? 116.504 152.334 167.166 1.00 34.26  ? 657  VAL B CG1   1 
ATOM   15874 C  CG2   . VAL B 2  657  ? 118.116 154.185 167.266 1.00 32.44  ? 657  VAL B CG2   1 
ATOM   15875 N  N     . ASP B 2  658  ? 116.098 156.931 168.508 1.00 37.81  ? 658  ASP B N     1 
ATOM   15876 C  CA    . ASP B 2  658  ? 116.312 158.164 169.269 1.00 35.78  ? 658  ASP B CA    1 
ATOM   15877 C  C     . ASP B 2  658  ? 117.781 158.329 169.679 1.00 35.98  ? 658  ASP B C     1 
ATOM   15878 O  O     . ASP B 2  658  ? 118.147 158.243 170.848 1.00 39.91  ? 658  ASP B O     1 
ATOM   15879 C  CB    . ASP B 2  658  ? 115.383 158.199 170.485 1.00 35.93  ? 658  ASP B CB    1 
ATOM   15880 C  CG    . ASP B 2  658  ? 114.754 159.553 170.691 1.00 40.58  ? 658  ASP B CG    1 
ATOM   15881 O  OD1   . ASP B 2  658  ? 115.046 160.468 169.899 1.00 40.61  ? 658  ASP B OD1   1 
ATOM   15882 O  OD2   . ASP B 2  658  ? 113.961 159.702 171.640 1.00 39.91  ? 658  ASP B OD2   1 
ATOM   15883 N  N     . GLU B 2  659  ? 118.623 158.551 168.667 1.00 31.91  ? 659  GLU B N     1 
ATOM   15884 C  CA    . GLU B 2  659  ? 120.025 158.889 168.876 1.00 28.30  ? 659  GLU B CA    1 
ATOM   15885 C  C     . GLU B 2  659  ? 120.410 160.068 167.999 1.00 29.26  ? 659  GLU B C     1 
ATOM   15886 O  O     . GLU B 2  659  ? 119.779 160.342 166.981 1.00 36.47  ? 659  GLU B O     1 
ATOM   15887 C  CB    . GLU B 2  659  ? 120.970 157.719 168.577 1.00 28.78  ? 659  GLU B CB    1 
ATOM   15888 C  CG    . GLU B 2  659  ? 120.364 156.355 168.745 1.00 33.24  ? 659  GLU B CG    1 
ATOM   15889 C  CD    . GLU B 2  659  ? 121.400 155.252 168.690 1.00 34.87  ? 659  GLU B CD    1 
ATOM   15890 O  OE1   . GLU B 2  659  ? 122.379 155.393 167.931 1.00 35.19  ? 659  GLU B OE1   1 
ATOM   15891 O  OE2   . GLU B 2  659  ? 121.242 154.246 169.411 1.00 32.47  ? 659  GLU B OE2   1 
ATOM   15892 N  N     . VAL B 2  660  ? 121.461 160.769 168.415 1.00 22.82  ? 660  VAL B N     1 
ATOM   15893 C  CA    . VAL B 2  660  ? 122.082 161.830 167.634 1.00 18.56  ? 660  VAL B CA    1 
ATOM   15894 C  C     . VAL B 2  660  ? 123.527 161.438 167.380 1.00 22.98  ? 660  VAL B C     1 
ATOM   15895 O  O     . VAL B 2  660  ? 124.225 161.002 168.297 1.00 34.17  ? 660  VAL B O     1 
ATOM   15896 C  CB    . VAL B 2  660  ? 122.014 163.193 168.347 1.00 24.33  ? 660  VAL B CB    1 
ATOM   15897 C  CG1   . VAL B 2  660  ? 122.633 164.268 167.484 1.00 23.47  ? 660  VAL B CG1   1 
ATOM   15898 C  CG2   . VAL B 2  660  ? 120.590 163.545 168.693 1.00 26.81  ? 660  VAL B CG2   1 
ATOM   15899 N  N     . GLU B 2  661  ? 123.972 161.577 166.135 1.00 21.27  ? 661  GLU B N     1 
ATOM   15900 C  CA    . GLU B 2  661  ? 125.336 161.244 165.749 1.00 21.03  ? 661  GLU B CA    1 
ATOM   15901 C  C     . GLU B 2  661  ? 126.000 162.459 165.123 1.00 25.47  ? 661  GLU B C     1 
ATOM   15902 O  O     . GLU B 2  661  ? 125.361 163.202 164.377 1.00 31.53  ? 661  GLU B O     1 
ATOM   15903 C  CB    . GLU B 2  661  ? 125.377 160.080 164.764 1.00 19.00  ? 661  GLU B CB    1 
ATOM   15904 C  CG    . GLU B 2  661  ? 124.775 158.793 165.261 1.00 22.00  ? 661  GLU B CG    1 
ATOM   15905 C  CD    . GLU B 2  661  ? 124.869 157.677 164.233 1.00 29.55  ? 661  GLU B CD    1 
ATOM   15906 O  OE1   . GLU B 2  661  ? 125.424 157.909 163.141 1.00 28.65  ? 661  GLU B OE1   1 
ATOM   15907 O  OE2   . GLU B 2  661  ? 124.372 156.567 164.503 1.00 33.29  ? 661  GLU B OE2   1 
ATOM   15908 N  N     . PHE B 2  662  ? 127.273 162.666 165.444 1.00 20.90  ? 662  PHE B N     1 
ATOM   15909 C  CA    . PHE B 2  662  ? 128.132 163.622 164.764 1.00 16.77  ? 662  PHE B CA    1 
ATOM   15910 C  C     . PHE B 2  662  ? 129.292 162.855 164.153 1.00 19.75  ? 662  PHE B C     1 
ATOM   15911 O  O     . PHE B 2  662  ? 129.834 161.946 164.784 1.00 25.93  ? 662  PHE B O     1 
ATOM   15912 C  CB    . PHE B 2  662  ? 128.675 164.680 165.722 1.00 16.31  ? 662  PHE B CB    1 
ATOM   15913 C  CG    . PHE B 2  662  ? 127.630 165.572 166.321 1.00 20.31  ? 662  PHE B CG    1 
ATOM   15914 C  CD1   . PHE B 2  662  ? 126.908 165.169 167.427 1.00 22.75  ? 662  PHE B CD1   1 
ATOM   15915 C  CD2   . PHE B 2  662  ? 127.407 166.832 165.813 1.00 20.20  ? 662  PHE B CD2   1 
ATOM   15916 C  CE1   . PHE B 2  662  ? 125.965 165.992 167.986 1.00 20.48  ? 662  PHE B CE1   1 
ATOM   15917 C  CE2   . PHE B 2  662  ? 126.466 167.659 166.375 1.00 19.86  ? 662  PHE B CE2   1 
ATOM   15918 C  CZ    . PHE B 2  662  ? 125.743 167.238 167.462 1.00 18.89  ? 662  PHE B CZ    1 
ATOM   15919 N  N     . TRP B 2  663  ? 129.665 163.203 162.922 1.00 15.56  ? 663  TRP B N     1 
ATOM   15920 C  CA    . TRP B 2  663  ? 130.755 162.534 162.224 1.00 16.98  ? 663  TRP B CA    1 
ATOM   15921 C  C     . TRP B 2  663  ? 131.700 163.549 161.606 1.00 21.22  ? 663  TRP B C     1 
ATOM   15922 O  O     . TRP B 2  663  ? 131.260 164.555 161.053 1.00 25.54  ? 663  TRP B O     1 
ATOM   15923 C  CB    . TRP B 2  663  ? 130.238 161.613 161.148 1.00 14.41  ? 663  TRP B CB    1 
ATOM   15924 C  CG    . TRP B 2  663  ? 129.536 160.436 161.667 1.00 19.24  ? 663  TRP B CG    1 
ATOM   15925 C  CD1   . TRP B 2  663  ? 128.198 160.277 161.797 1.00 21.20  ? 663  TRP B CD1   1 
ATOM   15926 C  CD2   . TRP B 2  663  ? 130.134 159.226 162.133 1.00 22.44  ? 663  TRP B CD2   1 
ATOM   15927 N  NE1   . TRP B 2  663  ? 127.918 159.038 162.306 1.00 21.11  ? 663  TRP B NE1   1 
ATOM   15928 C  CE2   . TRP B 2  663  ? 129.094 158.375 162.528 1.00 20.79  ? 663  TRP B CE2   1 
ATOM   15929 C  CE3   . TRP B 2  663  ? 131.452 158.782 162.256 1.00 19.95  ? 663  TRP B CE3   1 
ATOM   15930 C  CZ2   . TRP B 2  663  ? 129.328 157.106 163.033 1.00 18.92  ? 663  TRP B CZ2   1 
ATOM   15931 C  CZ3   . TRP B 2  663  ? 131.679 157.527 162.756 1.00 19.19  ? 663  TRP B CZ3   1 
ATOM   15932 C  CH2   . TRP B 2  663  ? 130.625 156.701 163.134 1.00 19.13  ? 663  TRP B CH2   1 
ATOM   15933 N  N     . LEU B 2  664  ? 133.009 163.296 161.733 1.00 16.71  ? 664  LEU B N     1 
ATOM   15934 C  CA    . LEU B 2  664  ? 134.017 164.173 161.150 1.00 16.01  ? 664  LEU B CA    1 
ATOM   15935 C  C     . LEU B 2  664  ? 135.235 163.412 160.642 1.00 18.91  ? 664  LEU B C     1 
ATOM   15936 O  O     . LEU B 2  664  ? 136.325 163.981 160.562 1.00 24.20  ? 664  LEU B O     1 
ATOM   15937 C  CB    . LEU B 2  664  ? 134.488 165.230 162.147 1.00 16.26  ? 664  LEU B CB    1 
ATOM   15938 C  CG    . LEU B 2  664  ? 133.494 166.236 162.710 1.00 20.97  ? 664  LEU B CG    1 
ATOM   15939 C  CD1   . LEU B 2  664  ? 132.958 165.767 164.039 1.00 21.88  ? 664  LEU B CD1   1 
ATOM   15940 C  CD2   . LEU B 2  664  ? 134.144 167.590 162.843 1.00 22.43  ? 664  LEU B CD2   1 
ATOM   15941 N  N     . ASP B 2  665  ? 135.091 162.148 160.286 1.00 15.60  ? 665  ASP B N     1 
ATOM   15942 C  CA    . ASP B 2  665  ? 136.248 161.378 159.866 1.00 17.01  ? 665  ASP B CA    1 
ATOM   15943 C  C     . ASP B 2  665  ? 136.434 161.477 158.355 1.00 18.98  ? 665  ASP B C     1 
ATOM   15944 O  O     . ASP B 2  665  ? 135.640 162.097 157.649 1.00 24.87  ? 665  ASP B O     1 
ATOM   15945 C  CB    . ASP B 2  665  ? 136.115 159.928 160.328 1.00 23.91  ? 665  ASP B CB    1 
ATOM   15946 C  CG    . ASP B 2  665  ? 134.755 159.353 160.061 1.00 23.60  ? 665  ASP B CG    1 
ATOM   15947 O  OD1   . ASP B 2  665  ? 133.756 160.018 160.383 1.00 23.22  ? 665  ASP B OD1   1 
ATOM   15948 O  OD2   . ASP B 2  665  ? 134.682 158.222 159.544 1.00 22.19  ? 665  ASP B OD2   1 
ATOM   15949 N  N     . VAL B 2  666  ? 137.496 160.868 157.853 1.00 23.89  ? 666  VAL B N     1 
ATOM   15950 C  CA    . VAL B 2  666  ? 137.810 160.879 156.430 1.00 22.64  ? 666  VAL B CA    1 
ATOM   15951 C  C     . VAL B 2  666  ? 136.939 159.860 155.721 1.00 26.37  ? 666  VAL B C     1 
ATOM   15952 O  O     . VAL B 2  666  ? 136.383 158.952 156.346 1.00 24.62  ? 666  VAL B O     1 
ATOM   15953 C  CB    . VAL B 2  666  ? 139.298 160.575 156.176 1.00 24.59  ? 666  VAL B CB    1 
ATOM   15954 C  CG1   . VAL B 2  666  ? 140.130 161.808 156.345 1.00 23.37  ? 666  VAL B CG1   1 
ATOM   15955 C  CG2   . VAL B 2  666  ? 139.782 159.447 157.058 1.00 23.88  ? 666  VAL B CG2   1 
ATOM   15956 N  N     . GLY B 2  667  ? 136.845 159.996 154.401 1.00 21.55  ? 667  GLY B N     1 
ATOM   15957 C  CA    . GLY B 2  667  ? 136.180 159.018 153.576 1.00 21.14  ? 667  GLY B CA    1 
ATOM   15958 C  C     . GLY B 2  667  ? 134.700 159.226 153.385 1.00 24.34  ? 667  GLY B C     1 
ATOM   15959 O  O     . GLY B 2  667  ? 134.055 158.380 152.762 1.00 25.22  ? 667  GLY B O     1 
ATOM   15960 N  N     . ARG B 2  668  ? 134.139 160.307 153.910 1.00 19.64  ? 668  ARG B N     1 
ATOM   15961 C  CA    . ARG B 2  668  ? 132.734 160.614 153.699 1.00 14.42  ? 668  ARG B CA    1 
ATOM   15962 C  C     . ARG B 2  668  ? 132.554 161.255 152.333 1.00 16.86  ? 668  ARG B C     1 
ATOM   15963 O  O     . ARG B 2  668  ? 133.308 162.158 151.966 1.00 26.03  ? 668  ARG B O     1 
ATOM   15964 C  CB    . ARG B 2  668  ? 132.229 161.544 154.794 1.00 19.88  ? 668  ARG B CB    1 
ATOM   15965 C  CG    . ARG B 2  668  ? 132.106 160.907 156.152 1.00 19.16  ? 668  ARG B CG    1 
ATOM   15966 C  CD    . ARG B 2  668  ? 131.757 161.933 157.198 1.00 12.90  ? 668  ARG B CD    1 
ATOM   15967 N  NE    . ARG B 2  668  ? 132.820 162.914 157.344 1.00 10.22  ? 668  ARG B NE    1 
ATOM   15968 C  CZ    . ARG B 2  668  ? 132.628 164.219 157.444 1.00 15.51  ? 668  ARG B CZ    1 
ATOM   15969 N  NH1   . ARG B 2  668  ? 131.419 164.743 157.410 1.00 16.18  ? 668  ARG B NH1   1 
ATOM   15970 N  NH2   . ARG B 2  668  ? 133.677 165.019 157.595 1.00 16.35  ? 668  ARG B NH2   1 
ATOM   15971 N  N     . LEU B 2  669  ? 131.566 160.789 151.580 1.00 15.52  ? 669  LEU B N     1 
ATOM   15972 C  CA    . LEU B 2  669  ? 131.194 161.456 150.343 1.00 13.62  ? 669  LEU B CA    1 
ATOM   15973 C  C     . LEU B 2  669  ? 130.233 162.595 150.641 1.00 10.24  ? 669  LEU B C     1 
ATOM   15974 O  O     . LEU B 2  669  ? 129.233 162.405 151.330 1.00 16.36  ? 669  LEU B O     1 
ATOM   15975 C  CB    . LEU B 2  669  ? 130.554 160.466 149.376 1.00 9.92   ? 669  LEU B CB    1 
ATOM   15976 C  CG    . LEU B 2  669  ? 131.425 159.323 148.875 1.00 10.58  ? 669  LEU B CG    1 
ATOM   15977 C  CD1   . LEU B 2  669  ? 130.671 158.455 147.901 1.00 7.91   ? 669  LEU B CD1   1 
ATOM   15978 C  CD2   . LEU B 2  669  ? 132.669 159.870 148.233 1.00 13.12  ? 669  LEU B CD2   1 
ATOM   15979 N  N     . THR B 2  670  ? 130.532 163.778 150.124 1.00 8.51   ? 670  THR B N     1 
ATOM   15980 C  CA    . THR B 2  670  ? 129.665 164.935 150.271 1.00 13.61  ? 670  THR B CA    1 
ATOM   15981 C  C     . THR B 2  670  ? 129.211 165.421 148.910 1.00 15.14  ? 670  THR B C     1 
ATOM   15982 O  O     . THR B 2  670  ? 129.783 165.066 147.883 1.00 14.87  ? 670  THR B O     1 
ATOM   15983 C  CB    . THR B 2  670  ? 130.349 166.104 150.978 1.00 17.30  ? 670  THR B CB    1 
ATOM   15984 O  OG1   . THR B 2  670  ? 131.747 166.104 150.669 1.00 22.76  ? 670  THR B OG1   1 
ATOM   15985 C  CG2   . THR B 2  670  ? 130.129 166.049 152.462 1.00 14.65  ? 670  THR B CG2   1 
ATOM   15986 N  N     . ARG B 2  671  ? 128.165 166.238 148.920 1.00 12.45  ? 671  ARG B N     1 
ATOM   15987 C  CA    . ARG B 2  671  ? 127.733 166.976 147.749 1.00 5.16   ? 671  ARG B CA    1 
ATOM   15988 C  C     . ARG B 2  671  ? 126.951 168.182 148.229 1.00 3.19   ? 671  ARG B C     1 
ATOM   15989 O  O     . ARG B 2  671  ? 126.224 168.085 149.219 1.00 11.65  ? 671  ARG B O     1 
ATOM   15990 C  CB    . ARG B 2  671  ? 126.883 166.112 146.805 1.00 5.34   ? 671  ARG B CB    1 
ATOM   15991 C  CG    . ARG B 2  671  ? 125.455 165.892 147.224 1.00 7.28   ? 671  ARG B CG    1 
ATOM   15992 C  CD    . ARG B 2  671  ? 124.854 164.804 146.391 1.00 5.20   ? 671  ARG B CD    1 
ATOM   15993 N  NE    . ARG B 2  671  ? 123.409 164.691 146.532 1.00 8.96   ? 671  ARG B NE    1 
ATOM   15994 C  CZ    . ARG B 2  671  ? 122.536 165.116 145.630 1.00 12.50  ? 671  ARG B CZ    1 
ATOM   15995 N  NH1   . ARG B 2  671  ? 122.923 165.763 144.548 1.00 15.50  ? 671  ARG B NH1   1 
ATOM   15996 N  NH2   . ARG B 2  671  ? 121.243 164.889 145.819 1.00 7.50   ? 671  ARG B NH2   1 
ATOM   15997 N  N     . PRO B 2  672  ? 127.106 169.332 147.586 1.00 3.94   ? 672  PRO B N     1 
ATOM   15998 C  CA    . PRO B 2  672  ? 126.307 170.498 147.968 1.00 7.55   ? 672  PRO B CA    1 
ATOM   15999 C  C     . PRO B 2  672  ? 124.859 170.362 147.531 1.00 8.90   ? 672  PRO B C     1 
ATOM   16000 O  O     . PRO B 2  672  ? 124.549 169.733 146.517 1.00 14.82  ? 672  PRO B O     1 
ATOM   16001 C  CB    . PRO B 2  672  ? 127.002 171.649 147.238 1.00 13.38  ? 672  PRO B CB    1 
ATOM   16002 C  CG    . PRO B 2  672  ? 127.641 171.005 146.080 1.00 7.30   ? 672  PRO B CG    1 
ATOM   16003 C  CD    . PRO B 2  672  ? 128.050 169.642 146.503 1.00 7.93   ? 672  PRO B CD    1 
ATOM   16004 N  N     . LEU B 2  673  ? 123.969 170.962 148.311 1.00 4.68   ? 673  LEU B N     1 
ATOM   16005 C  CA    . LEU B 2  673  ? 122.546 170.989 148.015 1.00 2.98   ? 673  LEU B CA    1 
ATOM   16006 C  C     . LEU B 2  673  ? 121.985 172.342 148.409 1.00 10.54  ? 673  LEU B C     1 
ATOM   16007 O  O     . LEU B 2  673  ? 122.305 172.849 149.483 1.00 17.88  ? 673  LEU B O     1 
ATOM   16008 C  CB    . LEU B 2  673  ? 121.799 169.880 148.753 1.00 3.96   ? 673  LEU B CB    1 
ATOM   16009 C  CG    . LEU B 2  673  ? 121.696 168.527 148.058 1.00 4.28   ? 673  LEU B CG    1 
ATOM   16010 C  CD1   . LEU B 2  673  ? 121.340 167.463 149.057 1.00 7.35   ? 673  LEU B CD1   1 
ATOM   16011 C  CD2   . LEU B 2  673  ? 120.677 168.583 146.966 1.00 3.51   ? 673  LEU B CD2   1 
ATOM   16012 N  N     . LEU B 2  674  ? 121.161 172.925 147.547 1.00 9.80   ? 674  LEU B N     1 
ATOM   16013 C  CA    . LEU B 2  674  ? 120.518 174.192 147.864 1.00 7.80   ? 674  LEU B CA    1 
ATOM   16014 C  C     . LEU B 2  674  ? 119.425 173.980 148.899 1.00 7.73   ? 674  LEU B C     1 
ATOM   16015 O  O     . LEU B 2  674  ? 118.698 172.992 148.848 1.00 14.92  ? 674  LEU B O     1 
ATOM   16016 C  CB    . LEU B 2  674  ? 119.942 174.831 146.605 1.00 5.26   ? 674  LEU B CB    1 
ATOM   16017 C  CG    . LEU B 2  674  ? 120.937 175.399 145.600 1.00 10.48  ? 674  LEU B CG    1 
ATOM   16018 C  CD1   . LEU B 2  674  ? 120.248 175.691 144.297 1.00 12.28  ? 674  LEU B CD1   1 
ATOM   16019 C  CD2   . LEU B 2  674  ? 121.578 176.649 146.140 1.00 15.61  ? 674  LEU B CD2   1 
ATOM   16020 N  N     . ILE B 2  675  ? 119.304 174.913 149.830 1.00 4.17   ? 675  ILE B N     1 
ATOM   16021 C  CA    . ILE B 2  675  ? 118.438 174.765 150.994 1.00 7.89   ? 675  ILE B CA    1 
ATOM   16022 C  C     . ILE B 2  675  ? 117.077 175.388 150.704 1.00 14.78  ? 675  ILE B C     1 
ATOM   16023 O  O     . ILE B 2  675  ? 116.989 176.444 150.071 1.00 17.31  ? 675  ILE B O     1 
ATOM   16024 C  CB    . ILE B 2  675  ? 119.091 175.398 152.235 1.00 12.10  ? 675  ILE B CB    1 
ATOM   16025 C  CG1   . ILE B 2  675  ? 120.196 174.494 152.771 1.00 14.29  ? 675  ILE B CG1   1 
ATOM   16026 C  CG2   . ILE B 2  675  ? 118.081 175.686 153.310 1.00 16.15  ? 675  ILE B CG2   1 
ATOM   16027 C  CD1   . ILE B 2  675  ? 121.105 175.166 153.745 1.00 14.14  ? 675  ILE B CD1   1 
ATOM   16028 N  N     . VAL B 2  676  ? 116.013 174.729 151.162 1.00 10.66  ? 676  VAL B N     1 
ATOM   16029 C  CA    . VAL B 2  676  ? 114.648 175.231 151.051 1.00 12.47  ? 676  VAL B CA    1 
ATOM   16030 C  C     . VAL B 2  676  ? 114.194 175.706 152.425 1.00 15.77  ? 676  VAL B C     1 
ATOM   16031 O  O     . VAL B 2  676  ? 114.407 175.016 153.426 1.00 21.18  ? 676  VAL B O     1 
ATOM   16032 C  CB    . VAL B 2  676  ? 113.703 174.151 150.498 1.00 9.29   ? 676  VAL B CB    1 
ATOM   16033 C  CG1   . VAL B 2  676  ? 112.268 174.573 150.629 1.00 11.92  ? 676  VAL B CG1   1 
ATOM   16034 C  CG2   . VAL B 2  676  ? 114.024 173.864 149.061 1.00 16.09  ? 676  VAL B CG2   1 
ATOM   16035 N  N     . ASP B 2  677  ? 113.601 176.891 152.482 1.00 15.63  ? 677  ASP B N     1 
ATOM   16036 C  CA    . ASP B 2  677  ? 113.045 177.447 153.707 1.00 17.86  ? 677  ASP B CA    1 
ATOM   16037 C  C     . ASP B 2  677  ? 111.566 177.749 153.513 1.00 24.63  ? 677  ASP B C     1 
ATOM   16038 O  O     . ASP B 2  677  ? 111.107 178.026 152.407 1.00 33.38  ? 677  ASP B O     1 
ATOM   16039 C  CB    . ASP B 2  677  ? 113.797 178.718 154.116 1.00 21.37  ? 677  ASP B CB    1 
ATOM   16040 C  CG    . ASP B 2  677  ? 115.124 178.424 154.800 1.00 29.18  ? 677  ASP B CG    1 
ATOM   16041 O  OD1   . ASP B 2  677  ? 115.236 177.389 155.490 1.00 27.05  ? 677  ASP B OD1   1 
ATOM   16042 O  OD2   . ASP B 2  677  ? 116.062 179.232 154.644 1.00 32.03  ? 677  ASP B OD2   1 
ATOM   16043 N  N     . ASN B 2  678  ? 110.815 177.725 154.606 1.00 23.33  ? 678  ASN B N     1 
ATOM   16044 C  CA    . ASN B 2  678  ? 109.380 177.966 154.528 1.00 21.06  ? 678  ASN B CA    1 
ATOM   16045 C  C     . ASN B 2  678  ? 108.978 178.919 155.643 1.00 22.32  ? 678  ASN B C     1 
ATOM   16046 O  O     . ASN B 2  678  ? 109.823 179.499 156.326 1.00 23.03  ? 678  ASN B O     1 
ATOM   16047 C  CB    . ASN B 2  678  ? 108.582 176.659 154.589 1.00 21.40  ? 678  ASN B CB    1 
ATOM   16048 C  CG    . ASN B 2  678  ? 108.921 175.815 155.794 1.00 22.66  ? 678  ASN B CG    1 
ATOM   16049 O  OD1   . ASN B 2  678  ? 109.191 176.326 156.874 1.00 27.54  ? 678  ASN B OD1   1 
ATOM   16050 N  ND2   . ASN B 2  678  ? 108.884 174.510 155.619 1.00 22.85  ? 678  ASN B ND2   1 
ATOM   16051 N  N     . ASN B 2  679  ? 107.666 179.085 155.810 1.00 24.57  ? 679  ASN B N     1 
ATOM   16052 C  CA    . ASN B 2  679  ? 107.117 179.930 156.859 1.00 24.43  ? 679  ASN B CA    1 
ATOM   16053 C  C     . ASN B 2  679  ? 106.124 179.135 157.689 1.00 28.01  ? 679  ASN B C     1 
ATOM   16054 O  O     . ASN B 2  679  ? 105.018 179.606 157.961 1.00 28.71  ? 679  ASN B O     1 
ATOM   16055 C  CB    . ASN B 2  679  ? 106.439 181.169 156.271 1.00 27.36  ? 679  ASN B CB    1 
ATOM   16056 C  CG    . ASN B 2  679  ? 105.295 180.831 155.336 1.00 31.84  ? 679  ASN B CG    1 
ATOM   16057 O  OD1   . ASN B 2  679  ? 104.939 179.672 155.160 1.00 32.51  ? 679  ASN B OD1   1 
ATOM   16058 N  ND2   . ASN B 2  679  ? 104.709 181.853 154.734 1.00 32.81  ? 679  ASN B ND2   1 
ATOM   16059 N  N     . ILE B 2  680  ? 106.504 177.920 158.083 1.00 28.26  ? 680  ILE B N     1 
ATOM   16060 C  CA    . ILE B 2  680  ? 105.570 177.034 158.767 1.00 26.81  ? 680  ILE B CA    1 
ATOM   16061 C  C     . ILE B 2  680  ? 105.160 177.606 160.119 1.00 34.94  ? 680  ILE B C     1 
ATOM   16062 O  O     . ILE B 2  680  ? 104.068 177.317 160.615 1.00 33.35  ? 680  ILE B O     1 
ATOM   16063 C  CB    . ILE B 2  680  ? 106.186 175.628 158.898 1.00 24.47  ? 680  ILE B CB    1 
ATOM   16064 C  CG1   . ILE B 2  680  ? 105.158 174.623 159.412 1.00 24.91  ? 680  ILE B CG1   1 
ATOM   16065 C  CG2   . ILE B 2  680  ? 107.403 175.662 159.795 1.00 27.33  ? 680  ILE B CG2   1 
ATOM   16066 C  CD1   . ILE B 2  680  ? 103.963 174.474 158.525 1.00 27.63  ? 680  ILE B CD1   1 
ATOM   16067 N  N     . GLU B 2  681  ? 106.009 178.433 160.732 1.00 35.18  ? 681  GLU B N     1 
ATOM   16068 C  CA    . GLU B 2  681  ? 105.674 178.975 162.046 1.00 30.09  ? 681  GLU B CA    1 
ATOM   16069 C  C     . GLU B 2  681  ? 104.571 180.023 161.952 1.00 31.83  ? 681  GLU B C     1 
ATOM   16070 O  O     . GLU B 2  681  ? 103.620 180.006 162.740 1.00 35.08  ? 681  GLU B O     1 
ATOM   16071 C  CB    . GLU B 2  681  ? 106.920 179.564 162.700 1.00 30.26  ? 681  GLU B CB    1 
ATOM   16072 C  CG    . GLU B 2  681  ? 107.895 178.520 163.221 1.00 33.35  ? 681  GLU B CG    1 
ATOM   16073 C  CD    . GLU B 2  681  ? 107.237 177.454 164.072 1.00 37.66  ? 681  GLU B CD    1 
ATOM   16074 O  OE1   . GLU B 2  681  ? 107.667 176.285 163.996 1.00 36.00  ? 681  GLU B OE1   1 
ATOM   16075 O  OE2   . GLU B 2  681  ? 106.307 177.782 164.835 1.00 38.04  ? 681  GLU B OE2   1 
ATOM   16076 N  N     . LYS B 2  682  ? 104.676 180.938 160.990 1.00 33.06  ? 682  LYS B N     1 
ATOM   16077 C  CA    . LYS B 2  682  ? 103.628 181.933 160.799 1.00 32.79  ? 682  LYS B CA    1 
ATOM   16078 C  C     . LYS B 2  682  ? 102.337 181.287 160.315 1.00 34.57  ? 682  LYS B C     1 
ATOM   16079 O  O     . LYS B 2  682  ? 101.242 181.682 160.729 1.00 38.87  ? 682  LYS B O     1 
ATOM   16080 C  CB    . LYS B 2  682  ? 104.107 182.999 159.823 1.00 30.79  ? 682  LYS B CB    1 
ATOM   16081 C  CG    . LYS B 2  682  ? 105.282 183.785 160.358 1.00 33.09  ? 682  LYS B CG    1 
ATOM   16082 C  CD    . LYS B 2  682  ? 105.061 185.275 160.253 1.00 35.20  ? 682  LYS B CD    1 
ATOM   16083 C  CE    . LYS B 2  682  ? 105.566 185.805 158.933 1.00 36.48  ? 682  LYS B CE    1 
ATOM   16084 N  NZ    . LYS B 2  682  ? 107.046 185.696 158.850 1.00 37.68  ? 682  LYS B NZ    1 
ATOM   16085 N  N     . TYR B 2  683  ? 102.450 180.289 159.441 1.00 31.05  ? 683  TYR B N     1 
ATOM   16086 C  CA    . TYR B 2  683  ? 101.282 179.523 159.027 1.00 31.50  ? 683  TYR B CA    1 
ATOM   16087 C  C     . TYR B 2  683  ? 100.615 178.853 160.221 1.00 32.06  ? 683  TYR B C     1 
ATOM   16088 O  O     . TYR B 2  683  ? 99.385  178.853 160.339 1.00 31.54  ? 683  TYR B O     1 
ATOM   16089 C  CB    . TYR B 2  683  ? 101.704 178.488 157.985 1.00 33.40  ? 683  TYR B CB    1 
ATOM   16090 C  CG    . TYR B 2  683  ? 100.613 177.569 157.505 1.00 31.60  ? 683  TYR B CG    1 
ATOM   16091 C  CD1   . TYR B 2  683  ? 99.782  177.932 156.463 1.00 31.12  ? 683  TYR B CD1   1 
ATOM   16092 C  CD2   . TYR B 2  683  ? 100.428 176.326 158.086 1.00 30.45  ? 683  TYR B CD2   1 
ATOM   16093 C  CE1   . TYR B 2  683  ? 98.792  177.089 156.022 1.00 30.28  ? 683  TYR B CE1   1 
ATOM   16094 C  CE2   . TYR B 2  683  ? 99.443  175.481 157.653 1.00 30.68  ? 683  TYR B CE2   1 
ATOM   16095 C  CZ    . TYR B 2  683  ? 98.627  175.866 156.622 1.00 33.47  ? 683  TYR B CZ    1 
ATOM   16096 O  OH    . TYR B 2  683  ? 97.639  175.017 156.190 1.00 37.07  ? 683  TYR B OH    1 
ATOM   16097 N  N     . ASN B 2  684  ? 101.416 178.279 161.119 1.00 33.34  ? 684  ASN B N     1 
ATOM   16098 C  CA    . ASN B 2  684  ? 100.877 177.610 162.296 1.00 34.47  ? 684  ASN B CA    1 
ATOM   16099 C  C     . ASN B 2  684  ? 100.177 178.600 163.216 1.00 35.87  ? 684  ASN B C     1 
ATOM   16100 O  O     . ASN B 2  684  ? 99.099  178.312 163.751 1.00 35.62  ? 684  ASN B O     1 
ATOM   16101 C  CB    . ASN B 2  684  ? 102.003 176.895 163.039 1.00 33.38  ? 684  ASN B CB    1 
ATOM   16102 C  CG    . ASN B 2  684  ? 102.278 175.515 162.491 1.00 33.03  ? 684  ASN B CG    1 
ATOM   16103 O  OD1   . ASN B 2  684  ? 101.536 175.009 161.654 1.00 33.99  ? 684  ASN B OD1   1 
ATOM   16104 N  ND2   . ASN B 2  684  ? 103.350 174.896 162.964 1.00 30.63  ? 684  ASN B ND2   1 
ATOM   16105 N  N     . GLN B 2  685  ? 100.780 179.770 163.415 1.00 37.70  ? 685  GLN B N     1 
ATOM   16106 C  CA    . GLN B 2  685  ? 100.161 180.785 164.255 1.00 35.95  ? 685  GLN B CA    1 
ATOM   16107 C  C     . GLN B 2  685  ? 98.852  181.276 163.658 1.00 38.57  ? 685  GLN B C     1 
ATOM   16108 O  O     . GLN B 2  685  ? 97.878  181.485 164.389 1.00 42.95  ? 685  GLN B O     1 
ATOM   16109 C  CB    . GLN B 2  685  ? 101.118 181.956 164.454 1.00 36.01  ? 685  GLN B CB    1 
ATOM   16110 C  CG    . GLN B 2  685  ? 102.052 181.802 165.644 1.00 38.42  ? 685  GLN B CG    1 
ATOM   16111 C  CD    . GLN B 2  685  ? 101.428 181.033 166.787 1.00 40.29  ? 685  GLN B CD    1 
ATOM   16112 O  OE1   . GLN B 2  685  ? 100.648 181.578 167.565 1.00 42.23  ? 685  GLN B OE1   1 
ATOM   16113 N  NE2   . GLN B 2  685  ? 101.783 179.758 166.905 1.00 38.62  ? 685  GLN B NE2   1 
ATOM   16114 N  N     . ALA B 2  686  ? 98.812  181.476 162.341 1.00 32.00  ? 686  ALA B N     1 
ATOM   16115 C  CA    . ALA B 2  686  ? 97.572  181.893 161.698 1.00 32.06  ? 686  ALA B CA    1 
ATOM   16116 C  C     . ALA B 2  686  ? 96.506  180.815 161.809 1.00 33.46  ? 686  ALA B C     1 
ATOM   16117 O  O     . ALA B 2  686  ? 95.325  181.125 161.979 1.00 35.75  ? 686  ALA B O     1 
ATOM   16118 C  CB    . ALA B 2  686  ? 97.830  182.251 160.237 1.00 33.85  ? 686  ALA B CB    1 
ATOM   16119 N  N     . CYS B 2  687  ? 96.898  179.542 161.709 1.00 36.63  ? 687  CYS B N     1 
ATOM   16120 C  CA    . CYS B 2  687  ? 95.941  178.462 161.931 1.00 37.33  ? 687  CYS B CA    1 
ATOM   16121 C  C     . CYS B 2  687  ? 95.384  178.504 163.348 1.00 40.90  ? 687  CYS B C     1 
ATOM   16122 O  O     . CYS B 2  687  ? 94.173  178.355 163.555 1.00 42.32  ? 687  CYS B O     1 
ATOM   16123 C  CB    . CYS B 2  687  ? 96.597  177.107 161.665 1.00 36.34  ? 687  CYS B CB    1 
ATOM   16124 S  SG    . CYS B 2  687  ? 96.513  176.530 159.957 1.00 47.32  ? 687  CYS B SG    1 
ATOM   16125 N  N     . TYR B 2  688  ? 96.254  178.720 164.338 1.00 40.06  ? 688  TYR B N     1 
ATOM   16126 C  CA    . TYR B 2  688  ? 95.797  178.775 165.723 1.00 41.37  ? 688  TYR B CA    1 
ATOM   16127 C  C     . TYR B 2  688  ? 94.840  179.941 165.944 1.00 43.39  ? 688  TYR B C     1 
ATOM   16128 O  O     . TYR B 2  688  ? 93.820  179.797 166.626 1.00 40.99  ? 688  TYR B O     1 
ATOM   16129 C  CB    . TYR B 2  688  ? 96.992  178.887 166.666 1.00 39.94  ? 688  TYR B CB    1 
ATOM   16130 C  CG    . TYR B 2  688  ? 97.826  177.629 166.780 1.00 43.49  ? 688  TYR B CG    1 
ATOM   16131 C  CD1   . TYR B 2  688  ? 99.210  177.704 166.827 1.00 43.07  ? 688  TYR B CD1   1 
ATOM   16132 C  CD2   . TYR B 2  688  ? 97.236  176.372 166.827 1.00 41.23  ? 688  TYR B CD2   1 
ATOM   16133 C  CE1   . TYR B 2  688  ? 99.983  176.573 166.927 1.00 40.69  ? 688  TYR B CE1   1 
ATOM   16134 C  CE2   . TYR B 2  688  ? 98.005  175.230 166.926 1.00 40.80  ? 688  TYR B CE2   1 
ATOM   16135 C  CZ    . TYR B 2  688  ? 99.382  175.339 166.977 1.00 41.74  ? 688  TYR B CZ    1 
ATOM   16136 O  OH    . TYR B 2  688  ? 100.177 174.219 167.078 1.00 42.55  ? 688  TYR B OH    1 
ATOM   16137 N  N     . LYS B 2  689  ? 95.152  181.104 165.372 1.00 42.94  ? 689  LYS B N     1 
ATOM   16138 C  CA    . LYS B 2  689  ? 94.298  182.277 165.539 1.00 42.54  ? 689  LYS B CA    1 
ATOM   16139 C  C     . LYS B 2  689  ? 92.976  182.130 164.793 1.00 43.41  ? 689  LYS B C     1 
ATOM   16140 O  O     . LYS B 2  689  ? 91.929  182.585 165.276 1.00 46.66  ? 689  LYS B O     1 
ATOM   16141 C  CB    . LYS B 2  689  ? 95.057  183.519 165.081 1.00 41.75  ? 689  LYS B CB    1 
ATOM   16142 C  CG    . LYS B 2  689  ? 94.291  184.465 164.192 1.00 42.07  ? 689  LYS B CG    1 
ATOM   16143 C  CD    . LYS B 2  689  ? 94.943  185.832 164.246 1.00 44.39  ? 689  LYS B CD    1 
ATOM   16144 C  CE    . LYS B 2  689  ? 94.314  186.805 163.271 1.00 43.39  ? 689  LYS B CE    1 
ATOM   16145 N  NZ    . LYS B 2  689  ? 95.108  188.057 163.183 1.00 43.33  ? 689  LYS B NZ    1 
ATOM   16146 N  N     . ALA B 2  690  ? 92.994  181.484 163.628 1.00 40.38  ? 690  ALA B N     1 
ATOM   16147 C  CA    . ALA B 2  690  ? 91.748  181.181 162.941 1.00 40.87  ? 690  ALA B CA    1 
ATOM   16148 C  C     . ALA B 2  690  ? 90.892  180.236 163.770 1.00 39.52  ? 690  ALA B C     1 
ATOM   16149 O  O     . ALA B 2  690  ? 89.668  180.377 163.818 1.00 40.16  ? 690  ALA B O     1 
ATOM   16150 C  CB    . ALA B 2  690  ? 92.039  180.593 161.561 1.00 40.57  ? 690  ALA B CB    1 
ATOM   16151 N  N     . ALA B 2  691  ? 91.521  179.272 164.443 1.00 41.44  ? 691  ALA B N     1 
ATOM   16152 C  CA    . ALA B 2  691  ? 90.767  178.398 165.337 1.00 44.20  ? 691  ALA B CA    1 
ATOM   16153 C  C     . ALA B 2  691  ? 90.215  179.167 166.533 1.00 46.95  ? 691  ALA B C     1 
ATOM   16154 O  O     . ALA B 2  691  ? 89.101  178.892 166.994 1.00 47.12  ? 691  ALA B O     1 
ATOM   16155 C  CB    . ALA B 2  691  ? 91.639  177.235 165.801 1.00 44.59  ? 691  ALA B CB    1 
ATOM   16156 N  N     . GLU B 2  692  ? 90.987  180.116 167.064 1.00 48.87  ? 692  GLU B N     1 
ATOM   16157 C  CA    . GLU B 2  692  ? 90.506  180.917 168.189 1.00 49.65  ? 692  GLU B CA    1 
ATOM   16158 C  C     . GLU B 2  692  ? 89.269  181.710 167.803 1.00 49.55  ? 692  GLU B C     1 
ATOM   16159 O  O     . GLU B 2  692  ? 88.313  181.813 168.583 1.00 50.97  ? 692  GLU B O     1 
ATOM   16160 C  CB    . GLU B 2  692  ? 91.603  181.852 168.695 1.00 47.56  ? 692  GLU B CB    1 
ATOM   16161 C  CG    . GLU B 2  692  ? 92.746  181.142 169.388 1.00 49.49  ? 692  GLU B CG    1 
ATOM   16162 C  CD    . GLU B 2  692  ? 92.275  180.273 170.532 1.00 53.83  ? 692  GLU B CD    1 
ATOM   16163 O  OE1   . GLU B 2  692  ? 91.851  179.124 170.281 1.00 53.39  ? 692  GLU B OE1   1 
ATOM   16164 O  OE2   . GLU B 2  692  ? 92.327  180.741 171.687 1.00 53.52  ? 692  GLU B OE2   1 
ATOM   16165 N  N     . ALA B 2  693  ? 89.270  182.287 166.603 1.00 42.84  ? 693  ALA B N     1 
ATOM   16166 C  CA    . ALA B 2  693  ? 88.052  182.916 166.110 1.00 46.15  ? 693  ALA B CA    1 
ATOM   16167 C  C     . ALA B 2  693  ? 86.939  181.901 165.870 1.00 48.37  ? 693  ALA B C     1 
ATOM   16168 O  O     . ALA B 2  693  ? 85.771  182.204 166.136 1.00 48.77  ? 693  ALA B O     1 
ATOM   16169 C  CB    . ALA B 2  693  ? 88.342  183.694 164.827 1.00 44.71  ? 693  ALA B CB    1 
ATOM   16170 N  N     . ARG B 2  694  ? 87.275  180.704 165.392 1.00 50.74  ? 694  ARG B N     1 
ATOM   16171 C  CA    . ARG B 2  694  ? 86.273  179.704 165.038 1.00 50.38  ? 694  ARG B CA    1 
ATOM   16172 C  C     . ARG B 2  694  ? 85.506  179.208 166.257 1.00 52.34  ? 694  ARG B C     1 
ATOM   16173 O  O     . ARG B 2  694  ? 84.271  179.160 166.242 1.00 52.38  ? 694  ARG B O     1 
ATOM   16174 C  CB    . ARG B 2  694  ? 86.959  178.540 164.323 1.00 52.63  ? 694  ARG B CB    1 
ATOM   16175 C  CG    . ARG B 2  694  ? 86.191  177.237 164.280 1.00 51.20  ? 694  ARG B CG    1 
ATOM   16176 C  CD    . ARG B 2  694  ? 85.186  177.251 163.143 1.00 50.81  ? 694  ARG B CD    1 
ATOM   16177 N  NE    . ARG B 2  694  ? 85.203  176.010 162.377 1.00 53.50  ? 694  ARG B NE    1 
ATOM   16178 C  CZ    . ARG B 2  694  ? 84.725  174.850 162.804 1.00 53.53  ? 694  ARG B CZ    1 
ATOM   16179 N  NH1   . ARG B 2  694  ? 84.170  174.727 163.999 1.00 52.12  ? 694  ARG B NH1   1 
ATOM   16180 N  NH2   . ARG B 2  694  ? 84.806  173.786 162.010 1.00 53.06  ? 694  ARG B NH2   1 
ATOM   16181 N  N     . LYS B 2  695  ? 86.222  178.824 167.316 1.00 48.77  ? 695  LYS B N     1 
ATOM   16182 C  CA    . LYS B 2  695  ? 85.567  178.290 168.505 1.00 48.40  ? 695  LYS B CA    1 
ATOM   16183 C  C     . LYS B 2  695  ? 84.781  179.357 169.254 1.00 48.87  ? 695  LYS B C     1 
ATOM   16184 O  O     . LYS B 2  695  ? 83.682  179.082 169.749 1.00 47.78  ? 695  LYS B O     1 
ATOM   16185 C  CB    . LYS B 2  695  ? 86.603  177.657 169.437 1.00 47.29  ? 695  LYS B CB    1 
ATOM   16186 C  CG    . LYS B 2  695  ? 86.003  176.968 170.648 1.00 47.02  ? 695  LYS B CG    1 
ATOM   16187 C  CD    . LYS B 2  695  ? 87.058  176.245 171.467 1.00 47.58  ? 695  LYS B CD    1 
ATOM   16188 C  CE    . LYS B 2  695  ? 86.432  175.559 172.676 1.00 48.91  ? 695  LYS B CE    1 
ATOM   16189 N  NZ    . LYS B 2  695  ? 87.424  174.799 173.484 1.00 47.71  ? 695  LYS B NZ    1 
ATOM   16190 N  N     . LYS B 2  696  ? 85.318  180.573 169.337 1.00 48.31  ? 696  LYS B N     1 
ATOM   16191 C  CA    . LYS B 2  696  ? 84.669  181.639 170.085 1.00 46.74  ? 696  LYS B CA    1 
ATOM   16192 C  C     . LYS B 2  696  ? 83.363  182.088 169.444 1.00 48.63  ? 696  LYS B C     1 
ATOM   16193 O  O     . LYS B 2  696  ? 82.445  182.498 170.163 1.00 49.88  ? 696  LYS B O     1 
ATOM   16194 C  CB    . LYS B 2  696  ? 85.626  182.823 170.227 1.00 47.31  ? 696  LYS B CB    1 
ATOM   16195 C  CG    . LYS B 2  696  ? 85.009  184.076 170.801 1.00 47.87  ? 696  LYS B CG    1 
ATOM   16196 C  CD    . LYS B 2  696  ? 85.859  185.288 170.499 1.00 47.79  ? 696  LYS B CD    1 
ATOM   16197 C  CE    . LYS B 2  696  ? 86.183  185.365 169.022 1.00 47.00  ? 696  LYS B CE    1 
ATOM   16198 N  NZ    . LYS B 2  696  ? 84.955  185.212 168.192 1.00 45.88  ? 696  LYS B NZ    1 
ATOM   16199 N  N     . GLY B 2  697  ? 83.248  182.013 168.122 1.00 44.29  ? 697  GLY B N     1 
ATOM   16200 C  CA    . GLY B 2  697  ? 81.974  182.277 167.483 1.00 45.61  ? 697  GLY B CA    1 
ATOM   16201 C  C     . GLY B 2  697  ? 82.031  183.189 166.276 1.00 47.29  ? 697  GLY B C     1 
ATOM   16202 O  O     . GLY B 2  697  ? 80.991  183.588 165.745 1.00 46.92  ? 697  GLY B O     1 
ATOM   16203 N  N     . ASP B 2  698  ? 83.236  183.519 165.823 1.00 48.19  ? 698  ASP B N     1 
ATOM   16204 C  CA    . ASP B 2  698  ? 83.386  184.353 164.640 1.00 48.61  ? 698  ASP B CA    1 
ATOM   16205 C  C     . ASP B 2  698  ? 83.044  183.540 163.398 1.00 50.08  ? 698  ASP B C     1 
ATOM   16206 O  O     . ASP B 2  698  ? 83.581  182.446 163.195 1.00 51.58  ? 698  ASP B O     1 
ATOM   16207 C  CB    . ASP B 2  698  ? 84.811  184.897 164.557 1.00 48.20  ? 698  ASP B CB    1 
ATOM   16208 C  CG    . ASP B 2  698  ? 84.934  186.069 163.607 1.00 49.81  ? 698  ASP B CG    1 
ATOM   16209 O  OD1   . ASP B 2  698  ? 84.538  187.189 163.986 1.00 48.27  ? 698  ASP B OD1   1 
ATOM   16210 O  OD2   . ASP B 2  698  ? 85.438  185.874 162.484 1.00 51.49  ? 698  ASP B OD2   1 
ATOM   16211 N  N     . LYS B 2  699  ? 82.137  184.066 162.573 1.00 48.89  ? 699  LYS B N     1 
ATOM   16212 C  CA    . LYS B 2  699  ? 81.764  183.388 161.338 1.00 51.21  ? 699  LYS B CA    1 
ATOM   16213 C  C     . LYS B 2  699  ? 82.732  183.672 160.199 1.00 50.31  ? 699  LYS B C     1 
ATOM   16214 O  O     . LYS B 2  699  ? 82.531  183.160 159.094 1.00 49.52  ? 699  LYS B O     1 
ATOM   16215 C  CB    . LYS B 2  699  ? 80.348  183.783 160.928 1.00 50.06  ? 699  LYS B CB    1 
ATOM   16216 C  CG    . LYS B 2  699  ? 79.281  183.248 161.858 1.00 49.03  ? 699  LYS B CG    1 
ATOM   16217 C  CD    . LYS B 2  699  ? 77.896  183.658 161.399 1.00 49.53  ? 699  LYS B CD    1 
ATOM   16218 C  CE    . LYS B 2  699  ? 76.828  183.090 162.316 1.00 49.09  ? 699  LYS B CE    1 
ATOM   16219 N  NZ    . LYS B 2  699  ? 75.462  183.497 161.889 1.00 48.72  ? 699  LYS B NZ    1 
ATOM   16220 N  N     . ASP B 2  700  ? 83.760  184.483 160.439 1.00 50.04  ? 700  ASP B N     1 
ATOM   16221 C  CA    . ASP B 2  700  ? 84.789  184.734 159.442 1.00 51.55  ? 700  ASP B CA    1 
ATOM   16222 C  C     . ASP B 2  700  ? 86.137  184.260 159.964 1.00 52.90  ? 700  ASP B C     1 
ATOM   16223 O  O     . ASP B 2  700  ? 87.139  184.976 159.867 1.00 53.01  ? 700  ASP B O     1 
ATOM   16224 C  CB    . ASP B 2  700  ? 84.825  186.216 159.085 1.00 50.71  ? 700  ASP B CB    1 
ATOM   16225 C  CG    . ASP B 2  700  ? 83.544  186.677 158.442 1.00 51.95  ? 700  ASP B CG    1 
ATOM   16226 O  OD1   . ASP B 2  700  ? 82.862  185.837 157.825 1.00 52.15  ? 700  ASP B OD1   1 
ATOM   16227 O  OD2   . ASP B 2  700  ? 83.211  187.872 158.557 1.00 51.07  ? 700  ASP B OD2   1 
ATOM   16228 N  N     . TRP B 2  701  ? 86.164  183.059 160.540 1.00 52.83  ? 701  TRP B N     1 
ATOM   16229 C  CA    . TRP B 2  701  ? 87.398  182.556 161.128 1.00 54.24  ? 701  TRP B CA    1 
ATOM   16230 C  C     . TRP B 2  701  ? 88.427  182.198 160.065 1.00 55.75  ? 701  TRP B C     1 
ATOM   16231 O  O     . TRP B 2  701  ? 89.632  182.267 160.329 1.00 55.55  ? 701  TRP B O     1 
ATOM   16232 C  CB    . TRP B 2  701  ? 87.109  181.338 162.000 1.00 53.14  ? 701  TRP B CB    1 
ATOM   16233 C  CG    . TRP B 2  701  ? 86.410  180.251 161.266 1.00 55.27  ? 701  TRP B CG    1 
ATOM   16234 C  CD1   . TRP B 2  701  ? 85.071  180.116 161.087 1.00 55.26  ? 701  TRP B CD1   1 
ATOM   16235 C  CD2   . TRP B 2  701  ? 87.021  179.147 160.589 1.00 54.82  ? 701  TRP B CD2   1 
ATOM   16236 N  NE1   . TRP B 2  701  ? 84.804  178.991 160.348 1.00 56.76  ? 701  TRP B NE1   1 
ATOM   16237 C  CE2   . TRP B 2  701  ? 85.987  178.380 160.027 1.00 55.14  ? 701  TRP B CE2   1 
ATOM   16238 C  CE3   . TRP B 2  701  ? 88.344  178.735 160.404 1.00 53.54  ? 701  TRP B CE3   1 
ATOM   16239 C  CZ2   . TRP B 2  701  ? 86.231  177.223 159.297 1.00 54.27  ? 701  TRP B CZ2   1 
ATOM   16240 C  CZ3   . TRP B 2  701  ? 88.584  177.589 159.682 1.00 54.64  ? 701  TRP B CZ3   1 
ATOM   16241 C  CH2   . TRP B 2  701  ? 87.533  176.844 159.138 1.00 55.26  ? 701  TRP B CH2   1 
ATOM   16242 N  N     . GLU B 2  702  ? 87.983  181.818 158.870 1.00 53.11  ? 702  GLU B N     1 
ATOM   16243 C  CA    . GLU B 2  702  ? 88.903  181.324 157.855 1.00 55.02  ? 702  GLU B CA    1 
ATOM   16244 C  C     . GLU B 2  702  ? 89.633  182.434 157.111 1.00 54.00  ? 702  GLU B C     1 
ATOM   16245 O  O     . GLU B 2  702  ? 90.512  182.129 156.299 1.00 53.89  ? 702  GLU B O     1 
ATOM   16246 C  CB    . GLU B 2  702  ? 88.164  180.446 156.843 1.00 54.35  ? 702  GLU B CB    1 
ATOM   16247 C  CG    . GLU B 2  702  ? 87.196  181.207 155.964 1.00 53.78  ? 702  GLU B CG    1 
ATOM   16248 C  CD    . GLU B 2  702  ? 87.769  181.478 154.588 1.00 56.07  ? 702  GLU B CD    1 
ATOM   16249 O  OE1   . GLU B 2  702  ? 88.717  180.768 154.190 1.00 57.51  ? 702  GLU B OE1   1 
ATOM   16250 O  OE2   . GLU B 2  702  ? 87.284  182.407 153.907 1.00 54.73  ? 702  GLU B OE2   1 
ATOM   16251 N  N     . LYS B 2  703  ? 89.304  183.700 157.348 1.00 48.27  ? 703  LYS B N     1 
ATOM   16252 C  CA    . LYS B 2  703  ? 90.024  184.768 156.669 1.00 48.95  ? 703  LYS B CA    1 
ATOM   16253 C  C     . LYS B 2  703  ? 91.331  185.121 157.362 1.00 47.70  ? 703  LYS B C     1 
ATOM   16254 O  O     . LYS B 2  703  ? 92.113  185.902 156.811 1.00 49.26  ? 703  LYS B O     1 
ATOM   16255 C  CB    . LYS B 2  703  ? 89.136  186.013 156.534 1.00 49.63  ? 703  LYS B CB    1 
ATOM   16256 C  CG    . LYS B 2  703  ? 88.786  186.738 157.836 1.00 50.36  ? 703  LYS B CG    1 
ATOM   16257 C  CD    . LYS B 2  703  ? 89.787  187.835 158.192 1.00 51.30  ? 703  LYS B CD    1 
ATOM   16258 C  CE    . LYS B 2  703  ? 89.215  188.790 159.231 1.00 49.49  ? 703  LYS B CE    1 
ATOM   16259 N  NZ    . LYS B 2  703  ? 89.886  190.123 159.207 1.00 48.42  ? 703  LYS B NZ    1 
ATOM   16260 N  N     . HIS B 2  704  ? 91.583  184.570 158.547 1.00 48.02  ? 704  HIS B N     1 
ATOM   16261 C  CA    . HIS B 2  704  ? 92.822  184.815 159.269 1.00 51.14  ? 704  HIS B CA    1 
ATOM   16262 C  C     . HIS B 2  704  ? 93.972  183.937 158.799 1.00 50.24  ? 704  HIS B C     1 
ATOM   16263 O  O     . HIS B 2  704  ? 95.122  184.221 159.146 1.00 50.23  ? 704  HIS B O     1 
ATOM   16264 C  CB    . HIS B 2  704  ? 92.601  184.610 160.770 1.00 50.21  ? 704  HIS B CB    1 
ATOM   16265 C  CG    . HIS B 2  704  ? 91.722  185.648 161.396 1.00 53.62  ? 704  HIS B CG    1 
ATOM   16266 N  ND1   . HIS B 2  704  ? 91.003  185.421 162.549 1.00 54.09  ? 704  HIS B ND1   1 
ATOM   16267 C  CD2   . HIS B 2  704  ? 91.468  186.929 161.041 1.00 51.43  ? 704  HIS B CD2   1 
ATOM   16268 C  CE1   . HIS B 2  704  ? 90.332  186.512 162.869 1.00 51.07  ? 704  HIS B CE1   1 
ATOM   16269 N  NE2   . HIS B 2  704  ? 90.597  187.442 161.970 1.00 51.47  ? 704  HIS B NE2   1 
ATOM   16270 N  N     . LYS B 2  705  ? 93.696  182.888 158.030 1.00 39.60  ? 705  LYS B N     1 
ATOM   16271 C  CA    . LYS B 2  705  ? 94.747  182.007 157.549 1.00 38.27  ? 705  LYS B CA    1 
ATOM   16272 C  C     . LYS B 2  705  ? 95.539  182.658 156.422 1.00 40.20  ? 705  LYS B C     1 
ATOM   16273 O  O     . LYS B 2  705  ? 95.004  183.418 155.612 1.00 38.67  ? 705  LYS B O     1 
ATOM   16274 C  CB    . LYS B 2  705  ? 94.164  180.680 157.067 1.00 38.03  ? 705  LYS B CB    1 
ATOM   16275 C  CG    . LYS B 2  705  ? 92.841  180.323 157.686 1.00 37.68  ? 705  LYS B CG    1 
ATOM   16276 C  CD    . LYS B 2  705  ? 92.292  179.033 157.102 1.00 38.93  ? 705  LYS B CD    1 
ATOM   16277 C  CE    . LYS B 2  705  ? 92.727  177.831 157.919 1.00 37.90  ? 705  LYS B CE    1 
ATOM   16278 N  NZ    . LYS B 2  705  ? 91.716  176.738 157.860 1.00 38.71  ? 705  LYS B NZ    1 
ATOM   16279 N  N     . ILE B 2  706  ? 96.830  182.346 156.382 1.00 37.77  ? 706  ILE B N     1 
ATOM   16280 C  CA    . ILE B 2  706  ? 97.725  182.788 155.317 1.00 36.21  ? 706  ILE B CA    1 
ATOM   16281 C  C     . ILE B 2  706  ? 98.121  181.561 154.506 1.00 36.46  ? 706  ILE B C     1 
ATOM   16282 O  O     . ILE B 2  706  ? 98.018  180.435 155.009 1.00 36.87  ? 706  ILE B O     1 
ATOM   16283 C  CB    . ILE B 2  706  ? 98.966  183.498 155.877 1.00 32.77  ? 706  ILE B CB    1 
ATOM   16284 C  CG1   . ILE B 2  706  ? 99.705  182.569 156.835 1.00 33.82  ? 706  ILE B CG1   1 
ATOM   16285 C  CG2   . ILE B 2  706  ? 98.576  184.794 156.552 1.00 34.90  ? 706  ILE B CG2   1 
ATOM   16286 C  CD1   . ILE B 2  706  ? 101.161 182.860 156.948 1.00 32.89  ? 706  ILE B CD1   1 
ATOM   16287 N  N     . PRO B 2  707  ? 98.541  181.716 153.255 1.00 30.52  ? 707  PRO B N     1 
ATOM   16288 C  CA    . PRO B 2  707  ? 99.018  180.557 152.496 1.00 31.09  ? 707  PRO B CA    1 
ATOM   16289 C  C     . PRO B 2  707  ? 100.394 180.102 152.958 1.00 31.81  ? 707  PRO B C     1 
ATOM   16290 O  O     . PRO B 2  707  ? 101.171 180.865 153.533 1.00 32.64  ? 707  PRO B O     1 
ATOM   16291 C  CB    . PRO B 2  707  ? 99.057  181.072 151.055 1.00 30.82  ? 707  PRO B CB    1 
ATOM   16292 C  CG    . PRO B 2  707  ? 99.246  182.535 151.198 1.00 31.50  ? 707  PRO B CG    1 
ATOM   16293 C  CD    . PRO B 2  707  ? 98.496  182.933 152.430 1.00 29.59  ? 707  PRO B CD    1 
ATOM   16294 N  N     . PHE B 2  708  ? 100.680 178.829 152.704 1.00 26.15  ? 708  PHE B N     1 
ATOM   16295 C  CA    . PHE B 2  708  ? 102.003 178.271 152.942 1.00 25.02  ? 708  PHE B CA    1 
ATOM   16296 C  C     . PHE B 2  708  ? 102.942 178.640 151.802 1.00 25.71  ? 708  PHE B C     1 
ATOM   16297 O  O     . PHE B 2  708  ? 102.525 178.728 150.647 1.00 31.83  ? 708  PHE B O     1 
ATOM   16298 C  CB    . PHE B 2  708  ? 101.913 176.754 153.084 1.00 27.26  ? 708  PHE B CB    1 
ATOM   16299 C  CG    . PHE B 2  708  ? 103.235 176.086 153.273 1.00 25.52  ? 708  PHE B CG    1 
ATOM   16300 C  CD1   . PHE B 2  708  ? 103.934 176.235 154.449 1.00 23.94  ? 708  PHE B CD1   1 
ATOM   16301 C  CD2   . PHE B 2  708  ? 103.775 175.304 152.273 1.00 24.09  ? 708  PHE B CD2   1 
ATOM   16302 C  CE1   . PHE B 2  708  ? 105.144 175.624 154.618 1.00 23.95  ? 708  PHE B CE1   1 
ATOM   16303 C  CE2   . PHE B 2  708  ? 104.982 174.693 152.442 1.00 23.42  ? 708  PHE B CE2   1 
ATOM   16304 C  CZ    . PHE B 2  708  ? 105.666 174.849 153.614 1.00 22.19  ? 708  PHE B CZ    1 
ATOM   16305 N  N     . ILE B 2  709  ? 104.207 178.888 152.132 1.00 23.49  ? 709  ILE B N     1 
ATOM   16306 C  CA    . ILE B 2  709  ? 105.220 179.248 151.145 1.00 23.39  ? 709  ILE B CA    1 
ATOM   16307 C  C     . ILE B 2  709  ? 106.507 178.500 151.459 1.00 25.70  ? 709  ILE B C     1 
ATOM   16308 O  O     . ILE B 2  709  ? 106.979 178.525 152.599 1.00 25.18  ? 709  ILE B O     1 
ATOM   16309 C  CB    . ILE B 2  709  ? 105.482 180.761 151.116 1.00 23.43  ? 709  ILE B CB    1 
ATOM   16310 C  CG1   . ILE B 2  709  ? 104.267 181.502 150.579 1.00 23.09  ? 709  ILE B CG1   1 
ATOM   16311 C  CG2   . ILE B 2  709  ? 106.711 181.078 150.286 1.00 23.62  ? 709  ILE B CG2   1 
ATOM   16312 C  CD1   . ILE B 2  709  ? 104.297 182.967 150.868 1.00 26.96  ? 709  ILE B CD1   1 
ATOM   16313 N  N     . GLN B 2  710  ? 107.072 177.840 150.452 1.00 23.89  ? 710  GLN B N     1 
ATOM   16314 C  CA    . GLN B 2  710  ? 108.393 177.236 150.530 1.00 17.76  ? 710  GLN B CA    1 
ATOM   16315 C  C     . GLN B 2  710  ? 109.197 177.652 149.312 1.00 14.81  ? 710  GLN B C     1 
ATOM   16316 O  O     . GLN B 2  710  ? 108.671 177.695 148.201 1.00 24.67  ? 710  GLN B O     1 
ATOM   16317 C  CB    . GLN B 2  710  ? 108.311 175.714 150.617 1.00 12.65  ? 710  GLN B CB    1 
ATOM   16318 C  CG    . GLN B 2  710  ? 107.481 175.056 149.547 1.00 15.43  ? 710  GLN B CG    1 
ATOM   16319 C  CD    . GLN B 2  710  ? 107.445 173.561 149.696 1.00 17.77  ? 710  GLN B CD    1 
ATOM   16320 O  OE1   . GLN B 2  710  ? 108.196 172.991 150.473 1.00 22.63  ? 710  GLN B OE1   1 
ATOM   16321 N  NE2   . GLN B 2  710  ? 106.559 172.919 148.967 1.00 16.39  ? 710  GLN B NE2   1 
ATOM   16322 N  N     . ASN B 2  711  ? 110.470 177.969 149.518 1.00 14.46  ? 711  ASN B N     1 
ATOM   16323 C  CA    . ASN B 2  711  ? 111.281 178.462 148.417 1.00 19.63  ? 711  ASN B CA    1 
ATOM   16324 C  C     . ASN B 2  711  ? 112.750 178.273 148.751 1.00 21.34  ? 711  ASN B C     1 
ATOM   16325 O  O     . ASN B 2  711  ? 113.113 177.991 149.892 1.00 26.99  ? 711  ASN B O     1 
ATOM   16326 C  CB    . ASN B 2  711  ? 110.974 179.934 148.126 1.00 20.11  ? 711  ASN B CB    1 
ATOM   16327 C  CG    . ASN B 2  711  ? 111.283 180.324 146.705 1.00 21.39  ? 711  ASN B CG    1 
ATOM   16328 O  OD1   . ASN B 2  711  ? 111.814 179.533 145.936 1.00 20.51  ? 711  ASN B OD1   1 
ATOM   16329 N  ND2   . ASN B 2  711  ? 110.930 181.544 146.339 1.00 25.53  ? 711  ASN B ND2   1 
ATOM   16330 N  N     . THR B 2  712  ? 113.585 178.412 147.732 1.00 18.45  ? 712  THR B N     1 
ATOM   16331 C  CA    . THR B 2  712  ? 115.023 178.513 147.903 1.00 17.83  ? 712  THR B CA    1 
ATOM   16332 C  C     . THR B 2  712  ? 115.447 179.969 147.755 1.00 24.51  ? 712  THR B C     1 
ATOM   16333 O  O     . THR B 2  712  ? 114.715 180.797 147.214 1.00 30.13  ? 712  THR B O     1 
ATOM   16334 C  CB    . THR B 2  712  ? 115.760 177.634 146.891 1.00 20.31  ? 712  THR B CB    1 
ATOM   16335 O  OG1   . THR B 2  712  ? 117.153 177.603 147.210 1.00 23.33  ? 712  THR B OG1   1 
ATOM   16336 C  CG2   . THR B 2  712  ? 115.593 178.166 145.491 1.00 20.31  ? 712  THR B CG2   1 
ATOM   16337 N  N     . ARG B 2  713  ? 116.631 180.282 148.262 1.00 28.27  ? 713  ARG B N     1 
ATOM   16338 C  CA    . ARG B 2  713  ? 117.138 181.646 148.209 1.00 27.62  ? 713  ARG B CA    1 
ATOM   16339 C  C     . ARG B 2  713  ? 118.059 181.900 147.027 1.00 28.67  ? 713  ARG B C     1 
ATOM   16340 O  O     . ARG B 2  713  ? 118.563 183.014 146.889 1.00 33.14  ? 713  ARG B O     1 
ATOM   16341 C  CB    . ARG B 2  713  ? 117.857 181.988 149.514 1.00 27.95  ? 713  ARG B CB    1 
ATOM   16342 C  CG    . ARG B 2  713  ? 116.953 181.895 150.728 1.00 30.50  ? 713  ARG B CG    1 
ATOM   16343 C  CD    . ARG B 2  713  ? 117.611 182.441 151.973 1.00 29.86  ? 713  ARG B CD    1 
ATOM   16344 N  NE    . ARG B 2  713  ? 116.816 182.163 153.162 1.00 31.56  ? 713  ARG B NE    1 
ATOM   16345 C  CZ    . ARG B 2  713  ? 115.804 182.906 153.584 1.00 32.38  ? 713  ARG B CZ    1 
ATOM   16346 N  NH1   . ARG B 2  713  ? 115.457 184.020 152.964 1.00 30.50  ? 713  ARG B NH1   1 
ATOM   16347 N  NH2   . ARG B 2  713  ? 115.135 182.532 154.668 1.00 32.28  ? 713  ARG B NH2   1 
ATOM   16348 N  N     . PHE B 2  714  ? 118.287 180.903 146.181 1.00 21.99  ? 714  PHE B N     1 
ATOM   16349 C  CA    . PHE B 2  714  ? 119.075 181.072 144.969 1.00 16.93  ? 714  PHE B CA    1 
ATOM   16350 C  C     . PHE B 2  714  ? 118.286 181.903 143.969 1.00 24.52  ? 714  PHE B C     1 
ATOM   16351 O  O     . PHE B 2  714  ? 117.112 181.624 143.724 1.00 30.46  ? 714  PHE B O     1 
ATOM   16352 C  CB    . PHE B 2  714  ? 119.405 179.699 144.399 1.00 21.20  ? 714  PHE B CB    1 
ATOM   16353 C  CG    . PHE B 2  714  ? 120.407 179.710 143.292 1.00 21.40  ? 714  PHE B CG    1 
ATOM   16354 C  CD1   . PHE B 2  714  ? 121.749 179.850 143.559 1.00 18.82  ? 714  PHE B CD1   1 
ATOM   16355 C  CD2   . PHE B 2  714  ? 120.010 179.528 141.987 1.00 21.56  ? 714  PHE B CD2   1 
ATOM   16356 C  CE1   . PHE B 2  714  ? 122.664 179.839 142.549 1.00 21.60  ? 714  PHE B CE1   1 
ATOM   16357 C  CE2   . PHE B 2  714  ? 120.927 179.517 140.975 1.00 24.10  ? 714  PHE B CE2   1 
ATOM   16358 C  CZ    . PHE B 2  714  ? 122.252 179.670 141.255 1.00 21.90  ? 714  PHE B CZ    1 
ATOM   16359 N  N     . THR B 2  715  ? 118.918 182.914 143.390 1.00 23.13  ? 715  THR B N     1 
ATOM   16360 C  CA    . THR B 2  715  ? 118.265 183.846 142.486 1.00 21.07  ? 715  THR B CA    1 
ATOM   16361 C  C     . THR B 2  715  ? 118.943 183.846 141.121 1.00 25.31  ? 715  THR B C     1 
ATOM   16362 O  O     . THR B 2  715  ? 120.073 183.371 140.983 1.00 28.87  ? 715  THR B O     1 
ATOM   16363 C  CB    . THR B 2  715  ? 118.281 185.268 143.063 1.00 26.93  ? 715  THR B CB    1 
ATOM   16364 O  OG1   . THR B 2  715  ? 119.630 185.673 143.305 1.00 31.76  ? 715  THR B OG1   1 
ATOM   16365 C  CG2   . THR B 2  715  ? 117.502 185.327 144.356 1.00 25.80  ? 715  THR B CG2   1 
ATOM   16366 N  N     . PRO B 2  716  ? 118.269 184.342 140.078 1.00 26.81  ? 716  PRO B N     1 
ATOM   16367 C  CA    . PRO B 2  716  ? 118.925 184.429 138.764 1.00 26.78  ? 716  PRO B CA    1 
ATOM   16368 C  C     . PRO B 2  716  ? 120.174 185.287 138.763 1.00 31.58  ? 716  PRO B C     1 
ATOM   16369 O  O     . PRO B 2  716  ? 121.118 185.002 138.013 1.00 35.76  ? 716  PRO B O     1 
ATOM   16370 C  CB    . PRO B 2  716  ? 117.834 185.036 137.876 1.00 27.93  ? 716  PRO B CB    1 
ATOM   16371 C  CG    . PRO B 2  716  ? 116.583 184.712 138.545 1.00 29.15  ? 716  PRO B CG    1 
ATOM   16372 C  CD    . PRO B 2  716  ? 116.859 184.754 140.000 1.00 30.02  ? 716  PRO B CD    1 
ATOM   16373 N  N     . GLN B 2  717  ? 120.207 186.335 139.585 1.00 28.72  ? 717  GLN B N     1 
ATOM   16374 C  CA    . GLN B 2  717  ? 121.400 187.164 139.679 1.00 26.88  ? 717  GLN B CA    1 
ATOM   16375 C  C     . GLN B 2  717  ? 122.578 186.371 140.227 1.00 28.58  ? 717  GLN B C     1 
ATOM   16376 O  O     . GLN B 2  717  ? 123.721 186.587 139.815 1.00 30.31  ? 717  GLN B O     1 
ATOM   16377 C  CB    . GLN B 2  717  ? 121.113 188.388 140.543 1.00 29.06  ? 717  GLN B CB    1 
ATOM   16378 C  CG    . GLN B 2  717  ? 122.108 189.522 140.366 1.00 29.06  ? 717  GLN B CG    1 
ATOM   16379 C  CD    . GLN B 2  717  ? 122.264 189.931 138.919 1.00 30.74  ? 717  GLN B CD    1 
ATOM   16380 O  OE1   . GLN B 2  717  ? 123.372 189.972 138.388 1.00 32.20  ? 717  GLN B OE1   1 
ATOM   16381 N  NE2   . GLN B 2  717  ? 121.150 190.244 138.273 1.00 30.04  ? 717  GLN B NE2   1 
ATOM   16382 N  N     . MET B 2  718  ? 122.324 185.444 141.154 1.00 24.74  ? 718  MET B N     1 
ATOM   16383 C  CA    . MET B 2  718  ? 123.405 184.596 141.647 1.00 24.93  ? 718  MET B CA    1 
ATOM   16384 C  C     . MET B 2  718  ? 123.951 183.694 140.552 1.00 29.31  ? 718  MET B C     1 
ATOM   16385 O  O     . MET B 2  718  ? 125.163 183.472 140.474 1.00 33.77  ? 718  MET B O     1 
ATOM   16386 C  CB    . MET B 2  718  ? 122.944 183.758 142.837 1.00 27.71  ? 718  MET B CB    1 
ATOM   16387 C  CG    . MET B 2  718  ? 122.696 184.543 144.101 1.00 28.14  ? 718  MET B CG    1 
ATOM   16388 S  SD    . MET B 2  718  ? 122.007 183.524 145.408 1.00 32.57  ? 718  MET B SD    1 
ATOM   16389 C  CE    . MET B 2  718  ? 121.123 184.753 146.350 1.00 25.51  ? 718  MET B CE    1 
ATOM   16390 N  N     . ALA B 2  719  ? 123.079 183.151 139.705 1.00 24.96  ? 719  ALA B N     1 
ATOM   16391 C  CA    . ALA B 2  719  ? 123.559 182.355 138.581 1.00 24.88  ? 719  ALA B CA    1 
ATOM   16392 C  C     . ALA B 2  719  ? 124.389 183.204 137.630 1.00 22.98  ? 719  ALA B C     1 
ATOM   16393 O  O     . ALA B 2  719  ? 125.439 182.767 137.135 1.00 21.96  ? 719  ALA B O     1 
ATOM   16394 C  CB    . ALA B 2  719  ? 122.379 181.719 137.853 1.00 24.39  ? 719  ALA B CB    1 
ATOM   16395 N  N     . LYS B 2  720  ? 123.940 184.434 137.381 1.00 26.71  ? 720  LYS B N     1 
ATOM   16396 C  CA    . LYS B 2  720  ? 124.686 185.339 136.517 1.00 30.51  ? 720  LYS B CA    1 
ATOM   16397 C  C     . LYS B 2  720  ? 126.057 185.651 137.099 1.00 31.46  ? 720  LYS B C     1 
ATOM   16398 O  O     . LYS B 2  720  ? 127.052 185.712 136.368 1.00 29.66  ? 720  LYS B O     1 
ATOM   16399 C  CB    . LYS B 2  720  ? 123.887 186.619 136.307 1.00 27.60  ? 720  LYS B CB    1 
ATOM   16400 C  CG    . LYS B 2  720  ? 123.890 187.123 134.885 1.00 30.22  ? 720  LYS B CG    1 
ATOM   16401 C  CD    . LYS B 2  720  ? 123.106 188.413 134.762 1.00 30.33  ? 720  LYS B CD    1 
ATOM   16402 C  CE    . LYS B 2  720  ? 121.801 188.361 135.524 1.00 29.74  ? 720  LYS B CE    1 
ATOM   16403 N  NZ    . LYS B 2  720  ? 120.951 187.230 135.101 1.00 29.98  ? 720  LYS B NZ    1 
ATOM   16404 N  N     . ASP B 2  721  ? 126.127 185.850 138.417 1.00 26.09  ? 721  ASP B N     1 
ATOM   16405 C  CA    . ASP B 2  721  ? 127.402 186.123 139.072 1.00 23.72  ? 721  ASP B CA    1 
ATOM   16406 C  C     . ASP B 2  721  ? 128.309 184.901 139.066 1.00 27.34  ? 721  ASP B C     1 
ATOM   16407 O  O     . ASP B 2  721  ? 129.534 185.034 138.987 1.00 29.29  ? 721  ASP B O     1 
ATOM   16408 C  CB    . ASP B 2  721  ? 127.159 186.596 140.499 1.00 26.43  ? 721  ASP B CB    1 
ATOM   16409 C  CG    . ASP B 2  721  ? 126.704 188.032 140.563 1.00 35.88  ? 721  ASP B CG    1 
ATOM   16410 O  OD1   . ASP B 2  721  ? 125.658 188.301 141.189 1.00 33.23  ? 721  ASP B OD1   1 
ATOM   16411 O  OD2   . ASP B 2  721  ? 127.392 188.898 139.988 1.00 40.27  ? 721  ASP B OD2   1 
ATOM   16412 N  N     . ILE B 2  722  ? 127.736 183.704 139.178 1.00 27.05  ? 722  ILE B N     1 
ATOM   16413 C  CA    . ILE B 2  722  ? 128.546 182.496 139.085 1.00 23.25  ? 722  ILE B CA    1 
ATOM   16414 C  C     . ILE B 2  722  ? 129.194 182.405 137.714 1.00 26.05  ? 722  ILE B C     1 
ATOM   16415 O  O     . ILE B 2  722  ? 130.398 182.149 137.595 1.00 26.88  ? 722  ILE B O     1 
ATOM   16416 C  CB    . ILE B 2  722  ? 127.697 181.248 139.382 1.00 23.38  ? 722  ILE B CB    1 
ATOM   16417 C  CG1   . ILE B 2  722  ? 127.358 181.155 140.866 1.00 24.88  ? 722  ILE B CG1   1 
ATOM   16418 C  CG2   . ILE B 2  722  ? 128.427 180.003 138.940 1.00 24.59  ? 722  ILE B CG2   1 
ATOM   16419 C  CD1   . ILE B 2  722  ? 126.321 180.108 141.181 1.00 20.89  ? 722  ILE B CD1   1 
ATOM   16420 N  N     . LEU B 2  723  ? 128.412 182.624 136.655 1.00 29.04  ? 723  LEU B N     1 
ATOM   16421 C  CA    . LEU B 2  723  ? 128.970 182.503 135.312 1.00 29.00  ? 723  LEU B CA    1 
ATOM   16422 C  C     . LEU B 2  723  ? 129.993 183.592 135.025 1.00 32.45  ? 723  LEU B C     1 
ATOM   16423 O  O     . LEU B 2  723  ? 130.829 183.437 134.128 1.00 34.07  ? 723  LEU B O     1 
ATOM   16424 C  CB    . LEU B 2  723  ? 127.852 182.532 134.275 1.00 29.36  ? 723  LEU B CB    1 
ATOM   16425 C  CG    . LEU B 2  723  ? 126.963 181.291 134.287 1.00 31.58  ? 723  LEU B CG    1 
ATOM   16426 C  CD1   . LEU B 2  723  ? 125.784 181.475 133.360 1.00 31.59  ? 723  LEU B CD1   1 
ATOM   16427 C  CD2   . LEU B 2  723  ? 127.770 180.072 133.898 1.00 27.63  ? 723  LEU B CD2   1 
ATOM   16428 N  N     . ALA B 2  724  ? 129.947 184.691 135.772 1.00 35.52  ? 724  ALA B N     1 
ATOM   16429 C  CA    . ALA B 2  724  ? 130.882 185.794 135.613 1.00 33.19  ? 724  ALA B CA    1 
ATOM   16430 C  C     . ALA B 2  724  ? 132.109 185.678 136.505 1.00 32.25  ? 724  ALA B C     1 
ATOM   16431 O  O     . ALA B 2  724  ? 132.986 186.541 136.437 1.00 38.42  ? 724  ALA B O     1 
ATOM   16432 C  CB    . ALA B 2  724  ? 130.175 187.121 135.891 1.00 31.34  ? 724  ALA B CB    1 
ATOM   16433 N  N     . GLY B 2  725  ? 132.196 184.648 137.340 1.00 28.81  ? 725  GLY B N     1 
ATOM   16434 C  CA    . GLY B 2  725  ? 133.345 184.448 138.197 1.00 26.51  ? 725  GLY B CA    1 
ATOM   16435 C  C     . GLY B 2  725  ? 133.334 185.220 139.496 1.00 26.72  ? 725  GLY B C     1 
ATOM   16436 O  O     . GLY B 2  725  ? 134.273 185.079 140.285 1.00 27.55  ? 725  GLY B O     1 
ATOM   16437 N  N     . THR B 2  726  ? 132.302 186.015 139.756 1.00 33.31  ? 726  THR B N     1 
ATOM   16438 C  CA    . THR B 2  726  ? 132.227 186.823 140.963 1.00 34.85  ? 726  THR B CA    1 
ATOM   16439 C  C     . THR B 2  726  ? 131.640 186.072 142.153 1.00 32.56  ? 726  THR B C     1 
ATOM   16440 O  O     . THR B 2  726  ? 131.677 186.591 143.272 1.00 33.01  ? 726  THR B O     1 
ATOM   16441 C  CB    . THR B 2  726  ? 131.390 188.078 140.694 1.00 34.08  ? 726  THR B CB    1 
ATOM   16442 O  OG1   . THR B 2  726  ? 131.603 188.508 139.346 1.00 33.21  ? 726  THR B OG1   1 
ATOM   16443 C  CG2   . THR B 2  726  ? 131.802 189.203 141.622 1.00 32.40  ? 726  THR B CG2   1 
ATOM   16444 N  N     . LEU B 2  727  ? 131.109 184.869 141.946 1.00 28.47  ? 727  LEU B N     1 
ATOM   16445 C  CA    . LEU B 2  727  ? 130.473 184.086 142.994 1.00 27.52  ? 727  LEU B CA    1 
ATOM   16446 C  C     . LEU B 2  727  ? 131.052 182.679 142.977 1.00 31.18  ? 727  LEU B C     1 
ATOM   16447 O  O     . LEU B 2  727  ? 131.376 182.151 141.910 1.00 32.78  ? 727  LEU B O     1 
ATOM   16448 C  CB    . LEU B 2  727  ? 128.957 184.041 142.792 1.00 28.84  ? 727  LEU B CB    1 
ATOM   16449 C  CG    . LEU B 2  727  ? 128.034 183.761 143.976 1.00 29.32  ? 727  LEU B CG    1 
ATOM   16450 C  CD1   . LEU B 2  727  ? 128.037 184.926 144.925 1.00 30.34  ? 727  LEU B CD1   1 
ATOM   16451 C  CD2   . LEU B 2  727  ? 126.627 183.481 143.504 1.00 28.59  ? 727  LEU B CD2   1 
ATOM   16452 N  N     . THR B 2  728  ? 131.188 182.076 144.155 1.00 26.64  ? 728  THR B N     1 
ATOM   16453 C  CA    . THR B 2  728  ? 131.807 180.765 144.301 1.00 24.33  ? 728  THR B CA    1 
ATOM   16454 C  C     . THR B 2  728  ? 130.953 179.870 145.192 1.00 23.33  ? 728  THR B C     1 
ATOM   16455 O  O     . THR B 2  728  ? 129.997 180.315 145.822 1.00 29.00  ? 728  THR B O     1 
ATOM   16456 C  CB    . THR B 2  728  ? 133.221 180.886 144.876 1.00 27.24  ? 728  THR B CB    1 
ATOM   16457 O  OG1   . THR B 2  728  ? 133.201 181.766 146.003 1.00 32.87  ? 728  THR B OG1   1 
ATOM   16458 C  CG2   . THR B 2  728  ? 134.158 181.458 143.843 1.00 25.65  ? 728  THR B CG2   1 
ATOM   16459 N  N     . LEU B 2  729  ? 131.300 178.582 145.220 1.00 23.72  ? 729  LEU B N     1 
ATOM   16460 C  CA    . LEU B 2  729  ? 130.572 177.639 146.063 1.00 24.58  ? 729  LEU B CA    1 
ATOM   16461 C  C     . LEU B 2  729  ? 130.781 177.935 147.537 1.00 30.09  ? 729  LEU B C     1 
ATOM   16462 O  O     . LEU B 2  729  ? 129.838 177.865 148.332 1.00 29.35  ? 729  LEU B O     1 
ATOM   16463 C  CB    . LEU B 2  729  ? 130.995 176.204 145.754 1.00 25.07  ? 729  LEU B CB    1 
ATOM   16464 C  CG    . LEU B 2  729  ? 130.191 175.130 146.494 1.00 24.77  ? 729  LEU B CG    1 
ATOM   16465 C  CD1   . LEU B 2  729  ? 128.789 175.034 145.950 1.00 21.94  ? 729  LEU B CD1   1 
ATOM   16466 C  CD2   . LEU B 2  729  ? 130.870 173.785 146.422 1.00 25.06  ? 729  LEU B CD2   1 
ATOM   16467 N  N     . GLU B 2  730  ? 132.014 178.262 147.921 1.00 36.68  ? 730  GLU B N     1 
ATOM   16468 C  CA    . GLU B 2  730  ? 132.306 178.524 149.323 1.00 30.06  ? 730  GLU B CA    1 
ATOM   16469 C  C     . GLU B 2  730  ? 131.743 179.861 149.767 1.00 31.77  ? 730  GLU B C     1 
ATOM   16470 O  O     . GLU B 2  730  ? 131.695 180.150 150.966 1.00 36.57  ? 730  GLU B O     1 
ATOM   16471 C  CB    . GLU B 2  730  ? 133.808 178.459 149.557 1.00 28.87  ? 730  GLU B CB    1 
ATOM   16472 C  CG    . GLU B 2  730  ? 134.420 177.070 149.375 1.00 35.37  ? 730  GLU B CG    1 
ATOM   16473 C  CD    . GLU B 2  730  ? 133.676 175.940 150.090 1.00 40.77  ? 730  GLU B CD    1 
ATOM   16474 O  OE1   . GLU B 2  730  ? 132.894 176.195 151.033 1.00 37.85  ? 730  GLU B OE1   1 
ATOM   16475 O  OE2   . GLU B 2  730  ? 133.888 174.770 149.708 1.00 38.73  ? 730  GLU B OE2   1 
ATOM   16476 N  N     . ASP B 2  731  ? 131.331 180.694 148.822 1.00 28.91  ? 731  ASP B N     1 
ATOM   16477 C  CA    . ASP B 2  731  ? 130.628 181.916 149.175 1.00 30.09  ? 731  ASP B CA    1 
ATOM   16478 C  C     . ASP B 2  731  ? 129.128 181.657 149.268 1.00 28.21  ? 731  ASP B C     1 
ATOM   16479 O  O     . ASP B 2  731  ? 128.452 182.245 150.114 1.00 24.70  ? 731  ASP B O     1 
ATOM   16480 C  CB    . ASP B 2  731  ? 131.019 182.997 148.158 1.00 28.08  ? 731  ASP B CB    1 
ATOM   16481 C  CG    . ASP B 2  731  ? 130.013 184.123 148.010 1.00 35.57  ? 731  ASP B CG    1 
ATOM   16482 O  OD1   . ASP B 2  731  ? 130.156 184.842 147.007 1.00 38.35  ? 731  ASP B OD1   1 
ATOM   16483 O  OD2   . ASP B 2  731  ? 129.152 184.372 148.878 1.00 36.08  ? 731  ASP B OD2   1 
ATOM   16484 N  N     . LEU B 2  732  ? 128.605 180.741 148.452 1.00 27.49  ? 732  LEU B N     1 
ATOM   16485 C  CA    . LEU B 2  732  ? 127.225 180.306 148.621 1.00 22.44  ? 732  LEU B CA    1 
ATOM   16486 C  C     . LEU B 2  732  ? 127.023 179.621 149.965 1.00 24.18  ? 732  LEU B C     1 
ATOM   16487 O  O     . LEU B 2  732  ? 125.995 179.819 150.618 1.00 28.26  ? 732  LEU B O     1 
ATOM   16488 C  CB    . LEU B 2  732  ? 126.821 179.372 147.485 1.00 22.60  ? 732  LEU B CB    1 
ATOM   16489 C  CG    . LEU B 2  732  ? 126.573 179.981 146.109 1.00 23.76  ? 732  LEU B CG    1 
ATOM   16490 C  CD1   . LEU B 2  732  ? 126.546 178.904 145.047 1.00 25.13  ? 732  LEU B CD1   1 
ATOM   16491 C  CD2   . LEU B 2  732  ? 125.285 180.757 146.112 1.00 24.09  ? 732  LEU B CD2   1 
ATOM   16492 N  N     . VAL B 2  733  ? 127.985 178.803 150.391 1.00 20.62  ? 733  VAL B N     1 
ATOM   16493 C  CA    . VAL B 2  733  ? 127.893 178.182 151.709 1.00 17.13  ? 733  VAL B CA    1 
ATOM   16494 C  C     . VAL B 2  733  ? 127.962 179.236 152.807 1.00 23.91  ? 733  VAL B C     1 
ATOM   16495 O  O     . VAL B 2  733  ? 127.249 179.152 153.813 1.00 26.82  ? 733  VAL B O     1 
ATOM   16496 C  CB    . VAL B 2  733  ? 128.992 177.121 151.877 1.00 22.67  ? 733  VAL B CB    1 
ATOM   16497 C  CG1   . VAL B 2  733  ? 129.081 176.689 153.313 1.00 24.67  ? 733  VAL B CG1   1 
ATOM   16498 C  CG2   . VAL B 2  733  ? 128.701 175.926 151.008 1.00 19.97  ? 733  VAL B CG2   1 
ATOM   16499 N  N     . ALA B 2  734  ? 128.797 180.261 152.617 1.00 29.41  ? 734  ALA B N     1 
ATOM   16500 C  CA    . ALA B 2  734  ? 129.038 181.243 153.668 1.00 26.01  ? 734  ALA B CA    1 
ATOM   16501 C  C     . ALA B 2  734  ? 127.770 181.973 154.083 1.00 27.03  ? 734  ALA B C     1 
ATOM   16502 O  O     . ALA B 2  734  ? 127.607 182.299 155.262 1.00 31.45  ? 734  ALA B O     1 
ATOM   16503 C  CB    . ALA B 2  734  ? 130.092 182.246 153.212 1.00 27.52  ? 734  ALA B CB    1 
ATOM   16504 N  N     . GLN B 2  735  ? 126.875 182.264 153.144 1.00 27.86  ? 735  GLN B N     1 
ATOM   16505 C  CA    . GLN B 2  735  ? 125.595 182.880 153.466 1.00 26.21  ? 735  GLN B CA    1 
ATOM   16506 C  C     . GLN B 2  735  ? 124.470 181.857 153.556 1.00 30.29  ? 735  GLN B C     1 
ATOM   16507 O  O     . GLN B 2  735  ? 123.293 182.213 153.522 1.00 31.55  ? 735  GLN B O     1 
ATOM   16508 C  CB    . GLN B 2  735  ? 125.256 183.981 152.468 1.00 23.05  ? 735  GLN B CB    1 
ATOM   16509 C  CG    . GLN B 2  735  ? 126.005 183.912 151.173 1.00 28.89  ? 735  GLN B CG    1 
ATOM   16510 C  CD    . GLN B 2  735  ? 125.526 184.952 150.191 1.00 31.30  ? 735  GLN B CD    1 
ATOM   16511 O  OE1   . GLN B 2  735  ? 124.491 185.583 150.398 1.00 31.49  ? 735  GLN B OE1   1 
ATOM   16512 N  NE2   . GLN B 2  735  ? 126.285 185.151 149.121 1.00 29.10  ? 735  GLN B NE2   1 
ATOM   16513 N  N     . GLY B 2  736  ? 124.823 180.583 153.683 1.00 26.87  ? 736  GLY B N     1 
ATOM   16514 C  CA    . GLY B 2  736  ? 123.842 179.554 153.982 1.00 27.22  ? 736  GLY B CA    1 
ATOM   16515 C  C     . GLY B 2  736  ? 122.805 179.323 152.908 1.00 30.73  ? 736  GLY B C     1 
ATOM   16516 O  O     . GLY B 2  736  ? 121.664 178.963 153.218 1.00 30.79  ? 736  GLY B O     1 
ATOM   16517 N  N     . ILE B 2  737  ? 123.181 179.500 151.647 1.00 21.46  ? 737  ILE B N     1 
ATOM   16518 C  CA    . ILE B 2  737  ? 122.314 179.178 150.526 1.00 18.62  ? 737  ILE B CA    1 
ATOM   16519 C  C     . ILE B 2  737  ? 122.392 177.700 150.172 1.00 14.42  ? 737  ILE B C     1 
ATOM   16520 O  O     . ILE B 2  737  ? 121.416 177.119 149.700 1.00 16.48  ? 737  ILE B O     1 
ATOM   16521 C  CB    . ILE B 2  737  ? 122.664 180.077 149.322 1.00 20.51  ? 737  ILE B CB    1 
ATOM   16522 C  CG1   . ILE B 2  737  ? 122.379 181.530 149.669 1.00 21.45  ? 737  ILE B CG1   1 
ATOM   16523 C  CG2   . ILE B 2  737  ? 121.864 179.710 148.105 1.00 15.36  ? 737  ILE B CG2   1 
ATOM   16524 C  CD1   . ILE B 2  737  ? 123.027 182.492 148.737 1.00 21.35  ? 737  ILE B CD1   1 
ATOM   16525 N  N     . CYS B 2  738  ? 123.526 177.065 150.430 1.00 12.02  ? 738  CYS B N     1 
ATOM   16526 C  CA    . CYS B 2  738  ? 123.658 175.631 150.264 1.00 14.59  ? 738  CYS B CA    1 
ATOM   16527 C  C     . CYS B 2  738  ? 124.421 175.045 151.442 1.00 18.16  ? 738  CYS B C     1 
ATOM   16528 O  O     . CYS B 2  738  ? 124.980 175.764 152.271 1.00 21.77  ? 738  CYS B O     1 
ATOM   16529 C  CB    . CYS B 2  738  ? 124.350 175.270 148.944 1.00 13.34  ? 738  CYS B CB    1 
ATOM   16530 S  SG    . CYS B 2  738  ? 125.999 175.884 148.722 1.00 32.12  ? 738  CYS B SG    1 
ATOM   16531 N  N     . GLU B 2  739  ? 124.413 173.720 151.522 1.00 14.26  ? 739  GLU B N     1 
ATOM   16532 C  CA    . GLU B 2  739  ? 125.164 173.012 152.542 1.00 12.88  ? 739  GLU B CA    1 
ATOM   16533 C  C     . GLU B 2  739  ? 125.578 171.656 152.006 1.00 13.27  ? 739  GLU B C     1 
ATOM   16534 O  O     . GLU B 2  739  ? 125.036 171.180 151.014 1.00 22.07  ? 739  GLU B O     1 
ATOM   16535 C  CB    . GLU B 2  739  ? 124.356 172.840 153.820 1.00 16.74  ? 739  GLU B CB    1 
ATOM   16536 C  CG    . GLU B 2  739  ? 123.162 171.955 153.684 1.00 12.88  ? 739  GLU B CG    1 
ATOM   16537 C  CD    . GLU B 2  739  ? 122.370 171.906 154.953 1.00 19.23  ? 739  GLU B CD    1 
ATOM   16538 O  OE1   . GLU B 2  739  ? 122.768 172.593 155.910 1.00 25.25  ? 739  GLU B OE1   1 
ATOM   16539 O  OE2   . GLU B 2  739  ? 121.353 171.190 155.003 1.00 20.81  ? 739  GLU B OE2   1 
ATOM   16540 N  N     . PHE B 2  740  ? 126.551 171.043 152.663 1.00 6.19   ? 740  PHE B N     1 
ATOM   16541 C  CA    . PHE B 2  740  ? 127.039 169.742 152.242 1.00 6.87   ? 740  PHE B CA    1 
ATOM   16542 C  C     . PHE B 2  740  ? 126.279 168.644 152.967 1.00 11.50  ? 740  PHE B C     1 
ATOM   16543 O  O     . PHE B 2  740  ? 126.011 168.754 154.164 1.00 24.32  ? 740  PHE B O     1 
ATOM   16544 C  CB    . PHE B 2  740  ? 128.533 169.621 152.516 1.00 12.55  ? 740  PHE B CB    1 
ATOM   16545 C  CG    . PHE B 2  740  ? 129.362 170.580 151.735 1.00 14.29  ? 740  PHE B CG    1 
ATOM   16546 C  CD1   . PHE B 2  740  ? 129.702 170.305 150.427 1.00 12.59  ? 740  PHE B CD1   1 
ATOM   16547 C  CD2   . PHE B 2  740  ? 129.819 171.751 152.311 1.00 16.59  ? 740  PHE B CD2   1 
ATOM   16548 C  CE1   . PHE B 2  740  ? 130.461 171.181 149.700 1.00 9.88   ? 740  PHE B CE1   1 
ATOM   16549 C  CE2   . PHE B 2  740  ? 130.586 172.631 151.592 1.00 17.29  ? 740  PHE B CE2   1 
ATOM   16550 C  CZ    . PHE B 2  740  ? 130.907 172.348 150.283 1.00 14.08  ? 740  PHE B CZ    1 
ATOM   16551 N  N     . ILE B 2  741  ? 125.913 167.597 152.239 1.00 3.20   ? 741  ILE B N     1 
ATOM   16552 C  CA    . ILE B 2  741  ? 125.156 166.483 152.788 1.00 8.63   ? 741  ILE B CA    1 
ATOM   16553 C  C     . ILE B 2  741  ? 125.851 165.190 152.401 1.00 11.72  ? 741  ILE B C     1 
ATOM   16554 O  O     . ILE B 2  741  ? 126.116 164.952 151.220 1.00 22.08  ? 741  ILE B O     1 
ATOM   16555 C  CB    . ILE B 2  741  ? 123.696 166.492 152.288 1.00 11.62  ? 741  ILE B CB    1 
ATOM   16556 C  CG1   . ILE B 2  741  ? 123.012 167.815 152.622 1.00 13.04  ? 741  ILE B CG1   1 
ATOM   16557 C  CG2   . ILE B 2  741  ? 122.912 165.353 152.882 1.00 7.36   ? 741  ILE B CG2   1 
ATOM   16558 C  CD1   . ILE B 2  741  ? 122.821 168.046 154.087 1.00 10.63  ? 741  ILE B CD1   1 
ATOM   16559 N  N     . THR B 2  742  ? 126.145 164.359 153.389 1.00 10.19  ? 742  THR B N     1 
ATOM   16560 C  CA    . THR B 2  742  ? 126.681 163.022 153.186 1.00 6.02   ? 742  THR B CA    1 
ATOM   16561 C  C     . THR B 2  742  ? 125.545 162.015 153.070 1.00 7.25   ? 742  THR B C     1 
ATOM   16562 O  O     . THR B 2  742  ? 124.393 162.335 153.358 1.00 8.72   ? 742  THR B O     1 
ATOM   16563 C  CB    . THR B 2  742  ? 127.604 162.642 154.343 1.00 8.97   ? 742  THR B CB    1 
ATOM   16564 O  OG1   . THR B 2  742  ? 126.867 162.662 155.564 1.00 20.26  ? 742  THR B OG1   1 
ATOM   16565 C  CG2   . THR B 2  742  ? 128.743 163.603 154.463 1.00 7.46   ? 742  THR B CG2   1 
ATOM   16566 N  N     . PRO B 2  743  ? 125.818 160.789 152.628 1.00 8.90   ? 743  PRO B N     1 
ATOM   16567 C  CA    . PRO B 2  743  ? 124.752 159.783 152.603 1.00 9.31   ? 743  PRO B CA    1 
ATOM   16568 C  C     . PRO B 2  743  ? 124.141 159.490 153.962 1.00 15.30  ? 743  PRO B C     1 
ATOM   16569 O  O     . PRO B 2  743  ? 122.991 159.050 154.010 1.00 28.42  ? 743  PRO B O     1 
ATOM   16570 C  CB    . PRO B 2  743  ? 125.451 158.553 152.019 1.00 7.08   ? 743  PRO B CB    1 
ATOM   16571 C  CG    . PRO B 2  743  ? 126.539 159.089 151.229 1.00 4.05   ? 743  PRO B CG    1 
ATOM   16572 C  CD    . PRO B 2  743  ? 127.017 160.306 151.930 1.00 7.69   ? 743  PRO B CD    1 
ATOM   16573 N  N     . GLU B 2  744  ? 124.864 159.695 155.065 1.00 15.34  ? 744  GLU B N     1 
ATOM   16574 C  CA    . GLU B 2  744  ? 124.264 159.501 156.382 1.00 14.67  ? 744  GLU B CA    1 
ATOM   16575 C  C     . GLU B 2  744  ? 123.177 160.529 156.647 1.00 14.91  ? 744  GLU B C     1 
ATOM   16576 O  O     . GLU B 2  744  ? 122.061 160.183 157.037 1.00 21.18  ? 744  GLU B O     1 
ATOM   16577 C  CB    . GLU B 2  744  ? 125.323 159.584 157.481 1.00 15.77  ? 744  GLU B CB    1 
ATOM   16578 C  CG    . GLU B 2  744  ? 126.402 158.544 157.412 1.00 19.98  ? 744  GLU B CG    1 
ATOM   16579 C  CD    . GLU B 2  744  ? 127.703 159.092 156.898 1.00 24.75  ? 744  GLU B CD    1 
ATOM   16580 O  OE1   . GLU B 2  744  ? 127.920 159.077 155.671 1.00 17.26  ? 744  GLU B OE1   1 
ATOM   16581 O  OE2   . GLU B 2  744  ? 128.526 159.517 157.729 1.00 28.62  ? 744  GLU B OE2   1 
ATOM   16582 N  N     . GLU B 2  745  ? 123.491 161.801 156.445 1.00 14.72  ? 745  GLU B N     1 
ATOM   16583 C  CA    . GLU B 2  745  ? 122.544 162.871 156.695 1.00 10.85  ? 745  GLU B CA    1 
ATOM   16584 C  C     . GLU B 2  745  ? 121.439 162.944 155.652 1.00 16.77  ? 745  GLU B C     1 
ATOM   16585 O  O     . GLU B 2  745  ? 120.414 163.576 155.909 1.00 20.99  ? 745  GLU B O     1 
ATOM   16586 C  CB    . GLU B 2  745  ? 123.292 164.198 156.762 1.00 10.98  ? 745  GLU B CB    1 
ATOM   16587 C  CG    . GLU B 2  745  ? 122.501 165.347 157.322 1.00 16.35  ? 745  GLU B CG    1 
ATOM   16588 C  CD    . GLU B 2  745  ? 123.385 166.502 157.700 1.00 23.50  ? 745  GLU B CD    1 
ATOM   16589 O  OE1   . GLU B 2  745  ? 124.613 166.372 157.546 1.00 24.66  ? 745  GLU B OE1   1 
ATOM   16590 O  OE2   . GLU B 2  745  ? 122.860 167.543 158.137 1.00 26.63  ? 745  GLU B OE2   1 
ATOM   16591 N  N     . ALA B 2  746  ? 121.617 162.313 154.488 1.00 18.22  ? 746  ALA B N     1 
ATOM   16592 C  CA    . ALA B 2  746  ? 120.583 162.333 153.459 1.00 16.56  ? 746  ALA B CA    1 
ATOM   16593 C  C     . ALA B 2  746  ? 119.285 161.708 153.938 1.00 20.15  ? 746  ALA B C     1 
ATOM   16594 O  O     . ALA B 2  746  ? 118.214 162.085 153.459 1.00 25.97  ? 746  ALA B O     1 
ATOM   16595 C  CB    . ALA B 2  746  ? 121.064 161.609 152.204 1.00 12.35  ? 746  ALA B CB    1 
ATOM   16596 N  N     . GLU B 2  747  ? 119.354 160.781 154.884 1.00 21.12  ? 747  GLU B N     1 
ATOM   16597 C  CA    . GLU B 2  747  ? 118.171 160.112 155.394 1.00 14.99  ? 747  GLU B CA    1 
ATOM   16598 C  C     . GLU B 2  747  ? 117.308 161.016 156.254 1.00 16.20  ? 747  GLU B C     1 
ATOM   16599 O  O     . GLU B 2  747  ? 116.204 160.615 156.624 1.00 24.98  ? 747  GLU B O     1 
ATOM   16600 C  CB    . GLU B 2  747  ? 118.599 158.881 156.172 1.00 18.46  ? 747  GLU B CB    1 
ATOM   16601 C  CG    . GLU B 2  747  ? 119.677 158.126 155.447 1.00 20.03  ? 747  GLU B CG    1 
ATOM   16602 C  CD    . GLU B 2  747  ? 119.453 156.643 155.440 1.00 28.72  ? 747  GLU B CD    1 
ATOM   16603 O  OE1   . GLU B 2  747  ? 119.405 156.059 154.339 1.00 27.94  ? 747  GLU B OE1   1 
ATOM   16604 O  OE2   . GLU B 2  747  ? 119.339 156.054 156.532 1.00 30.00  ? 747  GLU B OE2   1 
ATOM   16605 N  N     . ASN B 2  748  ? 117.788 162.211 156.585 1.00 13.53  ? 748  ASN B N     1 
ATOM   16606 C  CA    . ASN B 2  748  ? 117.001 163.240 157.243 1.00 15.86  ? 748  ASN B CA    1 
ATOM   16607 C  C     . ASN B 2  748  ? 116.506 164.302 156.275 1.00 19.97  ? 748  ASN B C     1 
ATOM   16608 O  O     . ASN B 2  748  ? 116.032 165.350 156.716 1.00 23.51  ? 748  ASN B O     1 
ATOM   16609 C  CB    . ASN B 2  748  ? 117.821 163.916 158.343 1.00 17.96  ? 748  ASN B CB    1 
ATOM   16610 C  CG    . ASN B 2  748  ? 118.120 162.999 159.510 1.00 18.94  ? 748  ASN B CG    1 
ATOM   16611 O  OD1   . ASN B 2  748  ? 119.268 162.683 159.782 1.00 18.94  ? 748  ASN B OD1   1 
ATOM   16612 N  ND2   . ASN B 2  748  ? 117.086 162.590 160.219 1.00 27.53  ? 748  ASN B ND2   1 
ATOM   16613 N  N     . CYS B 2  749  ? 116.613 164.067 154.973 1.00 17.34  ? 749  CYS B N     1 
ATOM   16614 C  CA    . CYS B 2  749  ? 116.377 165.086 153.964 1.00 11.55  ? 749  CYS B CA    1 
ATOM   16615 C  C     . CYS B 2  749  ? 115.247 164.675 153.033 1.00 11.08  ? 749  CYS B C     1 
ATOM   16616 O  O     . CYS B 2  749  ? 115.168 163.522 152.611 1.00 11.32  ? 749  CYS B O     1 
ATOM   16617 C  CB    . CYS B 2  749  ? 117.645 165.343 153.149 1.00 15.47  ? 749  CYS B CB    1 
ATOM   16618 S  SG    . CYS B 2  749  ? 119.040 165.999 154.069 1.00 15.94  ? 749  CYS B SG    1 
ATOM   16619 N  N     . LEU B 2  750  ? 114.370 165.625 152.729 1.00 10.40  ? 750  LEU B N     1 
ATOM   16620 C  CA    . LEU B 2  750  ? 113.344 165.480 151.702 1.00 6.30   ? 750  LEU B CA    1 
ATOM   16621 C  C     . LEU B 2  750  ? 113.687 166.454 150.583 1.00 5.08   ? 750  LEU B C     1 
ATOM   16622 O  O     . LEU B 2  750  ? 113.558 167.667 150.753 1.00 9.75   ? 750  LEU B O     1 
ATOM   16623 C  CB    . LEU B 2  750  ? 111.950 165.747 152.266 1.00 10.90  ? 750  LEU B CB    1 
ATOM   16624 C  CG    . LEU B 2  750  ? 110.769 165.451 151.337 1.00 8.49   ? 750  LEU B CG    1 
ATOM   16625 C  CD1   . LEU B 2  750  ? 110.750 164.006 150.929 1.00 3.96   ? 750  LEU B CD1   1 
ATOM   16626 C  CD2   . LEU B 2  750  ? 109.477 165.836 151.997 1.00 6.85   ? 750  LEU B CD2   1 
ATOM   16627 N  N     . VAL B 2  751  ? 114.111 165.924 149.442 1.00 1.63   ? 751  VAL B N     1 
ATOM   16628 C  CA    . VAL B 2  751  ? 114.752 166.700 148.390 1.00 1.05   ? 751  VAL B CA    1 
ATOM   16629 C  C     . VAL B 2  751  ? 113.807 166.809 147.204 1.00 3.27   ? 751  VAL B C     1 
ATOM   16630 O  O     . VAL B 2  751  ? 113.284 165.798 146.727 1.00 10.40  ? 751  VAL B O     1 
ATOM   16631 C  CB    . VAL B 2  751  ? 116.087 166.057 147.979 1.00 4.18   ? 751  VAL B CB    1 
ATOM   16632 C  CG1   . VAL B 2  751  ? 116.812 166.913 146.984 1.00 6.67   ? 751  VAL B CG1   1 
ATOM   16633 C  CG2   . VAL B 2  751  ? 116.949 165.836 149.188 1.00 9.26   ? 751  VAL B CG2   1 
ATOM   16634 N  N     . ALA B 2  752  ? 113.584 168.034 146.734 1.00 3.92   ? 752  ALA B N     1 
ATOM   16635 C  CA    . ALA B 2  752  ? 112.840 168.262 145.503 1.00 4.81   ? 752  ALA B CA    1 
ATOM   16636 C  C     . ALA B 2  752  ? 113.751 168.006 144.313 1.00 6.97   ? 752  ALA B C     1 
ATOM   16637 O  O     . ALA B 2  752  ? 114.859 168.538 144.253 1.00 9.71   ? 752  ALA B O     1 
ATOM   16638 C  CB    . ALA B 2  752  ? 112.297 169.685 145.466 1.00 1.57   ? 752  ALA B CB    1 
ATOM   16639 N  N     . PHE B 2  753  ? 113.301 167.180 143.369 1.00 4.06   ? 753  PHE B N     1 
ATOM   16640 C  CA    . PHE B 2  753  ? 114.237 166.699 142.364 1.00 2.84   ? 753  PHE B CA    1 
ATOM   16641 C  C     . PHE B 2  753  ? 114.643 167.780 141.371 1.00 6.30   ? 753  PHE B C     1 
ATOM   16642 O  O     . PHE B 2  753  ? 115.647 167.607 140.679 1.00 8.57   ? 753  PHE B O     1 
ATOM   16643 C  CB    . PHE B 2  753  ? 113.685 165.458 141.643 1.00 0.83   ? 753  PHE B CB    1 
ATOM   16644 C  CG    . PHE B 2  753  ? 112.457 165.700 140.808 1.00 9.42   ? 753  PHE B CG    1 
ATOM   16645 C  CD1   . PHE B 2  753  ? 112.558 166.166 139.510 1.00 10.25  ? 753  PHE B CD1   1 
ATOM   16646 C  CD2   . PHE B 2  753  ? 111.210 165.388 141.291 1.00 6.23   ? 753  PHE B CD2   1 
ATOM   16647 C  CE1   . PHE B 2  753  ? 111.444 166.367 138.747 1.00 7.08   ? 753  PHE B CE1   1 
ATOM   16648 C  CE2   . PHE B 2  753  ? 110.095 165.586 140.524 1.00 3.33   ? 753  PHE B CE2   1 
ATOM   16649 C  CZ    . PHE B 2  753  ? 110.213 166.077 139.255 1.00 8.92   ? 753  PHE B CZ    1 
ATOM   16650 N  N     . SER B 2  754  ? 113.915 168.891 141.300 1.00 4.01   ? 754  SER B N     1 
ATOM   16651 C  CA    . SER B 2  754  ? 114.327 170.022 140.480 1.00 14.89  ? 754  SER B CA    1 
ATOM   16652 C  C     . SER B 2  754  ? 113.526 171.245 140.895 1.00 8.13   ? 754  SER B C     1 
ATOM   16653 O  O     . SER B 2  754  ? 112.576 171.152 141.669 1.00 14.24  ? 754  SER B O     1 
ATOM   16654 C  CB    . SER B 2  754  ? 114.151 169.738 138.991 1.00 7.51   ? 754  SER B CB    1 
ATOM   16655 O  OG    . SER B 2  754  ? 112.905 170.199 138.520 1.00 14.94  ? 754  SER B OG    1 
ATOM   16656 N  N     . ILE B 2  755  ? 113.928 172.400 140.363 1.00 12.01  ? 755  ILE B N     1 
ATOM   16657 C  CA    . ILE B 2  755  ? 113.265 173.662 140.678 1.00 7.95   ? 755  ILE B CA    1 
ATOM   16658 C  C     . ILE B 2  755  ? 111.840 173.688 140.139 1.00 13.40  ? 755  ILE B C     1 
ATOM   16659 O  O     . ILE B 2  755  ? 110.980 174.399 140.671 1.00 18.24  ? 755  ILE B O     1 
ATOM   16660 C  CB    . ILE B 2  755  ? 114.110 174.835 140.144 1.00 13.64  ? 755  ILE B CB    1 
ATOM   16661 C  CG1   . ILE B 2  755  ? 113.604 176.175 140.679 1.00 13.15  ? 755  ILE B CG1   1 
ATOM   16662 C  CG2   . ILE B 2  755  ? 114.151 174.843 138.623 1.00 14.32  ? 755  ILE B CG2   1 
ATOM   16663 C  CD1   . ILE B 2  755  ? 113.841 176.372 142.131 1.00 14.95  ? 755  ILE B CD1   1 
ATOM   16664 N  N     . ILE B 2  756  ? 111.561 172.923 139.086 1.00 13.76  ? 756  ILE B N     1 
ATOM   16665 C  CA    . ILE B 2  756  ? 110.195 172.809 138.587 1.00 17.59  ? 756  ILE B CA    1 
ATOM   16666 C  C     . ILE B 2  756  ? 109.305 172.137 139.624 1.00 17.31  ? 756  ILE B C     1 
ATOM   16667 O  O     . ILE B 2  756  ? 108.173 172.572 139.867 1.00 20.44  ? 756  ILE B O     1 
ATOM   16668 C  CB    . ILE B 2  756  ? 110.186 172.052 137.247 1.00 16.37  ? 756  ILE B CB    1 
ATOM   16669 C  CG1   . ILE B 2  756  ? 111.263 172.600 136.319 1.00 14.47  ? 756  ILE B CG1   1 
ATOM   16670 C  CG2   . ILE B 2  756  ? 108.854 172.181 136.573 1.00 16.29  ? 756  ILE B CG2   1 
ATOM   16671 C  CD1   . ILE B 2  756  ? 110.986 173.992 135.833 1.00 14.79  ? 756  ILE B CD1   1 
ATOM   16672 N  N     . GLU B 2  757  ? 109.803 171.070 140.252 1.00 13.65  ? 757  GLU B N     1 
ATOM   16673 C  CA    . GLU B 2  757  ? 109.066 170.405 141.323 1.00 10.59  ? 757  GLU B CA    1 
ATOM   16674 C  C     . GLU B 2  757  ? 108.862 171.322 142.521 1.00 16.34  ? 757  GLU B C     1 
ATOM   16675 O  O     . GLU B 2  757  ? 107.800 171.306 143.149 1.00 18.28  ? 757  GLU B O     1 
ATOM   16676 C  CB    . GLU B 2  757  ? 109.804 169.137 141.747 1.00 9.62   ? 757  GLU B CB    1 
ATOM   16677 C  CG    . GLU B 2  757  ? 109.037 168.195 142.664 1.00 12.79  ? 757  GLU B CG    1 
ATOM   16678 C  CD    . GLU B 2  757  ? 107.818 167.549 142.023 1.00 25.11  ? 757  GLU B CD    1 
ATOM   16679 O  OE1   . GLU B 2  757  ? 107.494 167.861 140.860 1.00 26.24  ? 757  GLU B OE1   1 
ATOM   16680 O  OE2   . GLU B 2  757  ? 107.180 166.709 142.689 1.00 26.21  ? 757  GLU B OE2   1 
ATOM   16681 N  N     . LEU B 2  758  ? 109.881 172.104 142.872 1.00 18.26  ? 758  LEU B N     1 
ATOM   16682 C  CA    . LEU B 2  758  ? 109.759 173.033 143.987 1.00 12.42  ? 758  LEU B CA    1 
ATOM   16683 C  C     . LEU B 2  758  ? 108.726 174.117 143.706 1.00 14.69  ? 758  LEU B C     1 
ATOM   16684 O  O     . LEU B 2  758  ? 107.977 174.508 144.605 1.00 16.81  ? 758  LEU B O     1 
ATOM   16685 C  CB    . LEU B 2  758  ? 111.119 173.650 144.298 1.00 12.30  ? 758  LEU B CB    1 
ATOM   16686 C  CG    . LEU B 2  758  ? 111.189 174.662 145.443 1.00 14.27  ? 758  LEU B CG    1 
ATOM   16687 C  CD1   . LEU B 2  758  ? 110.722 174.058 146.745 1.00 12.89  ? 758  LEU B CD1   1 
ATOM   16688 C  CD2   . LEU B 2  758  ? 112.590 175.187 145.578 1.00 14.80  ? 758  LEU B CD2   1 
ATOM   16689 N  N     . ARG B 2  759  ? 108.678 174.630 142.473 1.00 19.78  ? 759  ARG B N     1 
ATOM   16690 C  CA    . ARG B 2  759  ? 107.662 175.620 142.126 1.00 19.77  ? 759  ARG B CA    1 
ATOM   16691 C  C     . ARG B 2  759  ? 106.269 175.011 142.061 1.00 20.23  ? 759  ARG B C     1 
ATOM   16692 O  O     . ARG B 2  759  ? 105.285 175.692 142.359 1.00 16.88  ? 759  ARG B O     1 
ATOM   16693 C  CB    . ARG B 2  759  ? 107.994 176.287 140.796 1.00 16.07  ? 759  ARG B CB    1 
ATOM   16694 C  CG    . ARG B 2  759  ? 108.832 177.533 140.937 1.00 23.22  ? 759  ARG B CG    1 
ATOM   16695 C  CD    . ARG B 2  759  ? 108.629 178.489 139.788 1.00 22.00  ? 759  ARG B CD    1 
ATOM   16696 N  NE    . ARG B 2  759  ? 109.252 178.005 138.565 1.00 24.25  ? 759  ARG B NE    1 
ATOM   16697 C  CZ    . ARG B 2  759  ? 110.473 178.333 138.170 1.00 24.04  ? 759  ARG B CZ    1 
ATOM   16698 N  NH1   . ARG B 2  759  ? 111.238 179.137 138.886 1.00 20.65  ? 759  ARG B NH1   1 
ATOM   16699 N  NH2   . ARG B 2  759  ? 110.938 177.840 137.027 1.00 26.81  ? 759  ARG B NH2   1 
ATOM   16700 N  N     . LYS B 2  760  ? 106.161 173.746 141.663 1.00 20.25  ? 760  LYS B N     1 
ATOM   16701 C  CA    . LYS B 2  760  ? 104.852 173.111 141.589 1.00 17.86  ? 760  LYS B CA    1 
ATOM   16702 C  C     . LYS B 2  760  ? 104.192 173.041 142.959 1.00 22.56  ? 760  LYS B C     1 
ATOM   16703 O  O     . LYS B 2  760  ? 102.977 173.228 143.081 1.00 28.55  ? 760  LYS B O     1 
ATOM   16704 C  CB    . LYS B 2  760  ? 104.988 171.718 140.984 1.00 19.29  ? 760  LYS B CB    1 
ATOM   16705 C  CG    . LYS B 2  760  ? 103.707 170.953 140.880 1.00 13.63  ? 760  LYS B CG    1 
ATOM   16706 C  CD    . LYS B 2  760  ? 103.974 169.563 140.379 1.00 20.43  ? 760  LYS B CD    1 
ATOM   16707 C  CE    . LYS B 2  760  ? 102.735 168.702 140.430 1.00 26.48  ? 760  LYS B CE    1 
ATOM   16708 N  NZ    . LYS B 2  760  ? 103.024 167.309 139.999 1.00 25.80  ? 760  LYS B NZ    1 
ATOM   16709 N  N     . HIS B 2  761  ? 104.975 172.770 144.002 1.00 20.79  ? 761  HIS B N     1 
ATOM   16710 C  CA    . HIS B 2  761  ? 104.480 172.665 145.367 1.00 15.43  ? 761  HIS B CA    1 
ATOM   16711 C  C     . HIS B 2  761  ? 104.785 173.903 146.200 1.00 18.90  ? 761  HIS B C     1 
ATOM   16712 O  O     . HIS B 2  761  ? 105.029 173.784 147.401 1.00 24.58  ? 761  HIS B O     1 
ATOM   16713 C  CB    . HIS B 2  761  ? 105.069 171.432 146.045 1.00 16.70  ? 761  HIS B CB    1 
ATOM   16714 C  CG    . HIS B 2  761  ? 104.771 170.152 145.338 1.00 20.09  ? 761  HIS B CG    1 
ATOM   16715 N  ND1   . HIS B 2  761  ? 103.538 169.547 145.385 1.00 22.69  ? 761  HIS B ND1   1 
ATOM   16716 C  CD2   . HIS B 2  761  ? 105.549 169.361 144.567 1.00 21.00  ? 761  HIS B CD2   1 
ATOM   16717 C  CE1   . HIS B 2  761  ? 103.567 168.437 144.672 1.00 23.03  ? 761  HIS B CE1   1 
ATOM   16718 N  NE2   . HIS B 2  761  ? 104.776 168.302 144.164 1.00 21.85  ? 761  HIS B NE2   1 
ATOM   16719 N  N     . LYS B 2  762  ? 104.771 175.090 145.595 1.00 20.84  ? 762  LYS B N     1 
ATOM   16720 C  CA    . LYS B 2  762  ? 105.204 176.282 146.319 1.00 19.88  ? 762  LYS B CA    1 
ATOM   16721 C  C     . LYS B 2  762  ? 104.294 176.584 147.501 1.00 22.18  ? 762  LYS B C     1 
ATOM   16722 O  O     . LYS B 2  762  ? 104.734 177.166 148.496 1.00 24.15  ? 762  LYS B O     1 
ATOM   16723 C  CB    . LYS B 2  762  ? 105.269 177.481 145.377 1.00 20.88  ? 762  LYS B CB    1 
ATOM   16724 C  CG    . LYS B 2  762  ? 105.847 178.718 146.030 1.00 19.25  ? 762  LYS B CG    1 
ATOM   16725 C  CD    . LYS B 2  762  ? 106.041 179.856 145.056 1.00 21.49  ? 762  LYS B CD    1 
ATOM   16726 C  CE    . LYS B 2  762  ? 106.733 181.022 145.743 1.00 24.54  ? 762  LYS B CE    1 
ATOM   16727 N  NZ    . LYS B 2  762  ? 107.109 182.111 144.797 1.00 25.85  ? 762  LYS B NZ    1 
ATOM   16728 N  N     . HIS B 2  763  ? 103.024 176.198 147.415 1.00 26.23  ? 763  HIS B N     1 
ATOM   16729 C  CA    . HIS B 2  763  ? 102.055 176.437 148.474 1.00 20.73  ? 763  HIS B CA    1 
ATOM   16730 C  C     . HIS B 2  763  ? 101.456 175.138 149.003 1.00 25.16  ? 763  HIS B C     1 
ATOM   16731 O  O     . HIS B 2  763  ? 100.319 175.122 149.474 1.00 31.73  ? 763  HIS B O     1 
ATOM   16732 C  CB    . HIS B 2  763  ? 100.952 177.368 147.982 1.00 21.35  ? 763  HIS B CB    1 
ATOM   16733 C  CG    . HIS B 2  763  ? 101.452 178.674 147.452 1.00 27.51  ? 763  HIS B CG    1 
ATOM   16734 N  ND1   . HIS B 2  763  ? 102.017 179.640 148.255 1.00 28.26  ? 763  HIS B ND1   1 
ATOM   16735 C  CD2   . HIS B 2  763  ? 101.480 179.170 146.193 1.00 29.22  ? 763  HIS B CD2   1 
ATOM   16736 C  CE1   . HIS B 2  763  ? 102.368 180.676 147.515 1.00 25.21  ? 763  HIS B CE1   1 
ATOM   16737 N  NE2   . HIS B 2  763  ? 102.054 180.415 146.260 1.00 28.54  ? 763  HIS B NE2   1 
ATOM   16738 N  N     . ASP B 2  764  ? 102.207 174.046 148.936 1.00 21.17  ? 764  ASP B N     1 
ATOM   16739 C  CA    . ASP B 2  764  ? 101.752 172.735 149.392 1.00 21.14  ? 764  ASP B CA    1 
ATOM   16740 C  C     . ASP B 2  764  ? 102.301 172.492 150.790 1.00 22.96  ? 764  ASP B C     1 
ATOM   16741 O  O     . ASP B 2  764  ? 103.485 172.193 150.958 1.00 25.74  ? 764  ASP B O     1 
ATOM   16742 C  CB    . ASP B 2  764  ? 102.199 171.638 148.433 1.00 20.56  ? 764  ASP B CB    1 
ATOM   16743 C  CG    . ASP B 2  764  ? 101.469 170.340 148.662 1.00 24.49  ? 764  ASP B CG    1 
ATOM   16744 O  OD1   . ASP B 2  764  ? 100.578 170.311 149.526 1.00 26.67  ? 764  ASP B OD1   1 
ATOM   16745 O  OD2   . ASP B 2  764  ? 101.783 169.345 147.985 1.00 24.68  ? 764  ASP B OD2   1 
ATOM   16746 N  N     . VAL B 2  765  ? 101.432 172.605 151.795 1.00 23.94  ? 765  VAL B N     1 
ATOM   16747 C  CA    . VAL B 2  765  ? 101.844 172.366 153.172 1.00 22.63  ? 765  VAL B CA    1 
ATOM   16748 C  C     . VAL B 2  765  ? 102.002 170.888 153.481 1.00 23.95  ? 765  VAL B C     1 
ATOM   16749 O  O     . VAL B 2  765  ? 102.563 170.539 154.523 1.00 28.83  ? 765  VAL B O     1 
ATOM   16750 C  CB    . VAL B 2  765  ? 100.838 173.020 154.141 1.00 21.00  ? 765  VAL B CB    1 
ATOM   16751 C  CG1   . VAL B 2  765  ? 99.732  172.055 154.511 1.00 23.03  ? 765  VAL B CG1   1 
ATOM   16752 C  CG2   . VAL B 2  765  ? 101.539 173.517 155.374 1.00 24.00  ? 765  VAL B CG2   1 
ATOM   16753 N  N     . THR B 2  766  ? 101.525 170.010 152.604 1.00 19.74  ? 766  THR B N     1 
ATOM   16754 C  CA    . THR B 2  766  ? 101.618 168.575 152.809 1.00 22.14  ? 766  THR B CA    1 
ATOM   16755 C  C     . THR B 2  766  ? 102.840 167.956 152.148 1.00 25.98  ? 766  THR B C     1 
ATOM   16756 O  O     . THR B 2  766  ? 102.973 166.729 152.152 1.00 30.41  ? 766  THR B O     1 
ATOM   16757 C  CB    . THR B 2  766  ? 100.357 167.888 152.292 1.00 26.04  ? 766  THR B CB    1 
ATOM   16758 O  OG1   . THR B 2  766  ? 100.363 167.891 150.863 1.00 27.23  ? 766  THR B OG1   1 
ATOM   16759 C  CG2   . THR B 2  766  ? 99.133  168.632 152.775 1.00 25.51  ? 766  THR B CG2   1 
ATOM   16760 N  N     . ARG B 2  767  ? 103.724 168.762 151.565 1.00 23.51  ? 767  ARG B N     1 
ATOM   16761 C  CA    . ARG B 2  767  ? 105.003 168.261 151.062 1.00 19.27  ? 767  ARG B CA    1 
ATOM   16762 C  C     . ARG B 2  767  ? 106.024 169.383 151.238 1.00 19.71  ? 767  ARG B C     1 
ATOM   16763 O  O     . ARG B 2  767  ? 106.184 170.237 150.367 1.00 22.30  ? 767  ARG B O     1 
ATOM   16764 C  CB    . ARG B 2  767  ? 104.904 167.814 149.615 1.00 19.66  ? 767  ARG B CB    1 
ATOM   16765 C  CG    . ARG B 2  767  ? 105.890 166.729 149.247 1.00 18.81  ? 767  ARG B CG    1 
ATOM   16766 C  CD    . ARG B 2  767  ? 105.407 165.983 148.030 1.00 23.91  ? 767  ARG B CD    1 
ATOM   16767 N  NE    . ARG B 2  767  ? 104.571 164.847 148.389 1.00 23.68  ? 767  ARG B NE    1 
ATOM   16768 C  CZ    . ARG B 2  767  ? 104.687 163.638 147.860 1.00 24.74  ? 767  ARG B CZ    1 
ATOM   16769 N  NH1   . ARG B 2  767  ? 105.575 163.382 146.915 1.00 25.32  ? 767  ARG B NH1   1 
ATOM   16770 N  NH2   . ARG B 2  767  ? 103.887 162.665 148.282 1.00 21.37  ? 767  ARG B NH2   1 
ATOM   16771 N  N     . ARG B 2  768  ? 106.711 169.359 152.368 1.00 17.75  ? 768  ARG B N     1 
ATOM   16772 C  CA    . ARG B 2  768  ? 107.657 170.398 152.741 1.00 15.65  ? 768  ARG B CA    1 
ATOM   16773 C  C     . ARG B 2  768  ? 109.060 169.873 152.480 1.00 14.25  ? 768  ARG B C     1 
ATOM   16774 O  O     . ARG B 2  768  ? 109.480 168.882 153.082 1.00 21.34  ? 768  ARG B O     1 
ATOM   16775 C  CB    . ARG B 2  768  ? 107.473 170.795 154.203 1.00 15.90  ? 768  ARG B CB    1 
ATOM   16776 C  CG    . ARG B 2  768  ? 106.153 171.462 154.491 1.00 13.59  ? 768  ARG B CG    1 
ATOM   16777 C  CD    . ARG B 2  768  ? 106.110 172.050 155.888 1.00 17.63  ? 768  ARG B CD    1 
ATOM   16778 N  NE    . ARG B 2  768  ? 106.070 171.022 156.919 1.00 19.76  ? 768  ARG B NE    1 
ATOM   16779 C  CZ    . ARG B 2  768  ? 104.957 170.467 157.373 1.00 19.85  ? 768  ARG B CZ    1 
ATOM   16780 N  NH1   . ARG B 2  768  ? 103.772 170.827 156.916 1.00 17.15  ? 768  ARG B NH1   1 
ATOM   16781 N  NH2   . ARG B 2  768  ? 105.036 169.520 158.299 1.00 15.85  ? 768  ARG B NH2   1 
ATOM   16782 N  N     . PHE B 2  769  ? 109.785 170.539 151.594 1.00 11.42  ? 769  PHE B N     1 
ATOM   16783 C  CA    . PHE B 2  769  ? 111.113 170.088 151.227 1.00 6.24   ? 769  PHE B CA    1 
ATOM   16784 C  C     . PHE B 2  769  ? 112.173 170.750 152.088 1.00 10.84  ? 769  PHE B C     1 
ATOM   16785 O  O     . PHE B 2  769  ? 112.042 171.901 152.504 1.00 17.23  ? 769  PHE B O     1 
ATOM   16786 C  CB    . PHE B 2  769  ? 111.392 170.379 149.757 1.00 9.41   ? 769  PHE B CB    1 
ATOM   16787 C  CG    . PHE B 2  769  ? 110.463 169.694 148.818 1.00 10.95  ? 769  PHE B CG    1 
ATOM   16788 C  CD1   . PHE B 2  769  ? 110.486 168.326 148.681 1.00 6.31   ? 769  PHE B CD1   1 
ATOM   16789 C  CD2   . PHE B 2  769  ? 109.583 170.423 148.051 1.00 11.39  ? 769  PHE B CD2   1 
ATOM   16790 C  CE1   . PHE B 2  769  ? 109.647 167.701 147.815 1.00 4.98   ? 769  PHE B CE1   1 
ATOM   16791 C  CE2   . PHE B 2  769  ? 108.740 169.800 147.185 1.00 8.31   ? 769  PHE B CE2   1 
ATOM   16792 C  CZ    . PHE B 2  769  ? 108.772 168.439 147.065 1.00 11.88  ? 769  PHE B CZ    1 
ATOM   16793 N  N     . THR B 2  770  ? 113.239 170.005 152.348 1.00 8.79   ? 770  THR B N     1 
ATOM   16794 C  CA    . THR B 2  770  ? 114.396 170.556 153.032 1.00 9.67   ? 770  THR B CA    1 
ATOM   16795 C  C     . THR B 2  770  ? 115.406 171.137 152.053 1.00 9.94   ? 770  THR B C     1 
ATOM   16796 O  O     . THR B 2  770  ? 115.966 172.206 152.301 1.00 12.92  ? 770  THR B O     1 
ATOM   16797 C  CB    . THR B 2  770  ? 115.061 169.479 153.891 1.00 12.29  ? 770  THR B CB    1 
ATOM   16798 O  OG1   . THR B 2  770  ? 115.655 168.496 153.044 1.00 18.77  ? 770  THR B OG1   1 
ATOM   16799 C  CG2   . THR B 2  770  ? 114.046 168.798 154.760 1.00 8.01   ? 770  THR B CG2   1 
ATOM   16800 N  N     . HIS B 2  771  ? 115.637 170.461 150.934 1.00 6.90   ? 771  HIS B N     1 
ATOM   16801 C  CA    . HIS B 2  771  ? 116.594 170.895 149.933 1.00 8.41   ? 771  HIS B CA    1 
ATOM   16802 C  C     . HIS B 2  771  ? 115.983 170.728 148.554 1.00 10.95  ? 771  HIS B C     1 
ATOM   16803 O  O     . HIS B 2  771  ? 114.977 170.043 148.382 1.00 16.42  ? 771  HIS B O     1 
ATOM   16804 C  CB    . HIS B 2  771  ? 117.903 170.103 150.015 1.00 6.42   ? 771  HIS B CB    1 
ATOM   16805 C  CG    . HIS B 2  771  ? 118.537 170.125 151.369 1.00 7.62   ? 771  HIS B CG    1 
ATOM   16806 N  ND1   . HIS B 2  771  ? 118.257 169.187 152.334 1.00 12.94  ? 771  HIS B ND1   1 
ATOM   16807 C  CD2   . HIS B 2  771  ? 119.433 170.972 151.918 1.00 7.57   ? 771  HIS B CD2   1 
ATOM   16808 C  CE1   . HIS B 2  771  ? 118.952 169.456 153.421 1.00 14.75  ? 771  HIS B CE1   1 
ATOM   16809 N  NE2   . HIS B 2  771  ? 119.673 170.536 153.195 1.00 12.54  ? 771  HIS B NE2   1 
ATOM   16810 N  N     . VAL B 2  772  ? 116.597 171.372 147.567 1.00 8.36   ? 772  VAL B N     1 
ATOM   16811 C  CA    . VAL B 2  772  ? 116.215 171.216 146.171 1.00 10.21  ? 772  VAL B CA    1 
ATOM   16812 C  C     . VAL B 2  772  ? 117.456 170.856 145.372 1.00 10.13  ? 772  VAL B C     1 
ATOM   16813 O  O     . VAL B 2  772  ? 118.538 171.400 145.604 1.00 9.53   ? 772  VAL B O     1 
ATOM   16814 C  CB    . VAL B 2  772  ? 115.531 172.482 145.615 1.00 5.11   ? 772  VAL B CB    1 
ATOM   16815 C  CG1   . VAL B 2  772  ? 116.352 173.704 145.901 1.00 7.51   ? 772  VAL B CG1   1 
ATOM   16816 C  CG2   . VAL B 2  772  ? 115.265 172.342 144.143 1.00 1.41   ? 772  VAL B CG2   1 
ATOM   16817 N  N     . ASP B 2  773  ? 117.304 169.922 144.448 1.00 9.23   ? 773  ASP B N     1 
ATOM   16818 C  CA    . ASP B 2  773  ? 118.414 169.365 143.697 1.00 2.22   ? 773  ASP B CA    1 
ATOM   16819 C  C     . ASP B 2  773  ? 118.482 169.954 142.294 1.00 4.30   ? 773  ASP B C     1 
ATOM   16820 O  O     . ASP B 2  773  ? 117.535 170.562 141.799 1.00 10.62  ? 773  ASP B O     1 
ATOM   16821 C  CB    . ASP B 2  773  ? 118.278 167.848 143.628 1.00 1.74   ? 773  ASP B CB    1 
ATOM   16822 C  CG    . ASP B 2  773  ? 119.587 167.160 143.428 1.00 11.28  ? 773  ASP B CG    1 
ATOM   16823 O  OD1   . ASP B 2  773  ? 120.608 167.849 143.254 1.00 14.83  ? 773  ASP B OD1   1 
ATOM   16824 O  OD2   . ASP B 2  773  ? 119.604 165.920 143.461 1.00 12.41  ? 773  ASP B OD2   1 
ATOM   16825 N  N     . VAL B 2  774  ? 119.639 169.789 141.668 1.00 6.46   ? 774  VAL B N     1 
ATOM   16826 C  CA    . VAL B 2  774  ? 119.850 170.067 140.254 1.00 3.78   ? 774  VAL B CA    1 
ATOM   16827 C  C     . VAL B 2  774  ? 119.948 168.720 139.543 1.00 5.74   ? 774  VAL B C     1 
ATOM   16828 O  O     . VAL B 2  774  ? 120.841 167.925 139.856 1.00 8.48   ? 774  VAL B O     1 
ATOM   16829 C  CB    . VAL B 2  774  ? 121.102 170.921 140.017 1.00 3.46   ? 774  VAL B CB    1 
ATOM   16830 C  CG1   . VAL B 2  774  ? 121.201 171.306 138.567 1.00 1.04   ? 774  VAL B CG1   1 
ATOM   16831 C  CG2   . VAL B 2  774  ? 121.061 172.160 140.878 1.00 1.52   ? 774  VAL B CG2   1 
ATOM   16832 N  N     . PRO B 2  775  ? 119.061 168.424 138.592 1.00 2.37   ? 775  PRO B N     1 
ATOM   16833 C  CA    . PRO B 2  775  ? 118.948 167.049 138.080 1.00 4.04   ? 775  PRO B CA    1 
ATOM   16834 C  C     . PRO B 2  775  ? 120.223 166.464 137.498 1.00 2.98   ? 775  PRO B C     1 
ATOM   16835 O  O     . PRO B 2  775  ? 120.421 165.249 137.573 1.00 11.63  ? 775  PRO B O     1 
ATOM   16836 C  CB    . PRO B 2  775  ? 117.861 167.190 137.015 1.00 0.48   ? 775  PRO B CB    1 
ATOM   16837 C  CG    . PRO B 2  775  ? 117.066 168.312 137.461 1.00 4.29   ? 775  PRO B CG    1 
ATOM   16838 C  CD    . PRO B 2  775  ? 117.994 169.281 138.065 1.00 3.97   ? 775  PRO B CD    1 
ATOM   16839 N  N     . GLN B 2  776  ? 121.093 167.286 136.913 1.00 4.27   ? 776  GLN B N     1 
ATOM   16840 C  CA    . GLN B 2  776  ? 122.281 166.764 136.254 1.00 11.50  ? 776  GLN B CA    1 
ATOM   16841 C  C     . GLN B 2  776  ? 123.311 166.232 137.238 1.00 7.83   ? 776  GLN B C     1 
ATOM   16842 O  O     . GLN B 2  776  ? 124.291 165.614 136.817 1.00 10.64  ? 776  GLN B O     1 
ATOM   16843 C  CB    . GLN B 2  776  ? 122.906 167.844 135.377 1.00 1.77   ? 776  GLN B CB    1 
ATOM   16844 C  CG    . GLN B 2  776  ? 122.099 168.222 134.160 1.00 3.29   ? 776  GLN B CG    1 
ATOM   16845 C  CD    . GLN B 2  776  ? 121.061 169.274 134.439 1.00 2.75   ? 776  GLN B CD    1 
ATOM   16846 O  OE1   . GLN B 2  776  ? 121.090 169.935 135.466 1.00 11.81  ? 776  GLN B OE1   1 
ATOM   16847 N  NE2   . GLN B 2  776  ? 120.139 169.439 133.521 1.00 2.40   ? 776  GLN B NE2   1 
ATOM   16848 N  N     . ALA B 2  777  ? 123.110 166.455 138.537 1.00 12.36  ? 777  ALA B N     1 
ATOM   16849 C  CA    . ALA B 2  777  ? 124.054 166.052 139.569 1.00 2.45   ? 777  ALA B CA    1 
ATOM   16850 C  C     . ALA B 2  777  ? 124.052 164.557 139.842 1.00 4.63   ? 777  ALA B C     1 
ATOM   16851 O  O     . ALA B 2  777  ? 124.947 164.079 140.536 1.00 14.16  ? 777  ALA B O     1 
ATOM   16852 C  CB    . ALA B 2  777  ? 123.750 166.807 140.854 1.00 6.84   ? 777  ALA B CB    1 
ATOM   16853 N  N     . ILE B 2  778  ? 123.083 163.807 139.311 1.00 1.04   ? 778  ILE B N     1 
ATOM   16854 C  CA    . ILE B 2  778  ? 123.034 162.364 139.524 1.00 8.38   ? 778  ILE B CA    1 
ATOM   16855 C  C     . ILE B 2  778  ? 123.884 161.590 138.535 1.00 1.06   ? 778  ILE B C     1 
ATOM   16856 O  O     . ILE B 2  778  ? 123.970 160.364 138.639 1.00 7.20   ? 778  ILE B O     1 
ATOM   16857 C  CB    . ILE B 2  778  ? 121.591 161.832 139.444 1.00 6.19   ? 778  ILE B CB    1 
ATOM   16858 C  CG1   . ILE B 2  778  ? 121.046 161.983 138.026 1.00 1.84   ? 778  ILE B CG1   1 
ATOM   16859 C  CG2   . ILE B 2  778  ? 120.708 162.546 140.449 1.00 1.14   ? 778  ILE B CG2   1 
ATOM   16860 C  CD1   . ILE B 2  778  ? 119.931 161.054 137.700 1.00 5.60   ? 778  ILE B CD1   1 
ATOM   16861 N  N     . LEU B 2  779  ? 124.526 162.263 137.589 1.00 3.99   ? 779  LEU B N     1 
ATOM   16862 C  CA    . LEU B 2  779  ? 125.362 161.613 136.596 1.00 4.02   ? 779  LEU B CA    1 
ATOM   16863 C  C     . LEU B 2  779  ? 126.815 162.016 136.790 1.00 6.81   ? 779  LEU B C     1 
ATOM   16864 O  O     . LEU B 2  779  ? 127.112 163.094 137.304 1.00 14.39  ? 779  LEU B O     1 
ATOM   16865 C  CB    . LEU B 2  779  ? 124.926 161.973 135.176 1.00 5.55   ? 779  LEU B CB    1 
ATOM   16866 C  CG    . LEU B 2  779  ? 123.592 161.479 134.633 1.00 1.54   ? 779  LEU B CG    1 
ATOM   16867 C  CD1   . LEU B 2  779  ? 123.451 161.955 133.227 1.00 3.52   ? 779  LEU B CD1   1 
ATOM   16868 C  CD2   . LEU B 2  779  ? 123.497 159.983 134.704 1.00 6.17   ? 779  LEU B CD2   1 
ATOM   16869 N  N     . GLY B 2  780  ? 127.717 161.130 136.387 1.00 5.63   ? 780  GLY B N     1 
ATOM   16870 C  CA    . GLY B 2  780  ? 129.128 161.434 136.366 1.00 7.41   ? 780  GLY B CA    1 
ATOM   16871 C  C     . GLY B 2  780  ? 129.526 162.129 135.088 1.00 8.01   ? 780  GLY B C     1 
ATOM   16872 O  O     . GLY B 2  780  ? 128.718 162.368 134.198 1.00 15.42  ? 780  GLY B O     1 
ATOM   16873 N  N     . LEU B 2  781  ? 130.812 162.455 134.996 1.00 8.66   ? 781  LEU B N     1 
ATOM   16874 C  CA    . LEU B 2  781  ? 131.307 163.240 133.870 1.00 11.38  ? 781  LEU B CA    1 
ATOM   16875 C  C     . LEU B 2  781  ? 131.223 162.491 132.544 1.00 11.05  ? 781  LEU B C     1 
ATOM   16876 O  O     . LEU B 2  781  ? 130.881 163.093 131.526 1.00 18.58  ? 781  LEU B O     1 
ATOM   16877 C  CB    . LEU B 2  781  ? 132.746 163.679 134.132 1.00 11.19  ? 781  LEU B CB    1 
ATOM   16878 C  CG    . LEU B 2  781  ? 133.317 164.726 133.180 1.00 10.61  ? 781  LEU B CG    1 
ATOM   16879 C  CD1   . LEU B 2  781  ? 132.612 166.050 133.335 1.00 10.41  ? 781  LEU B CD1   1 
ATOM   16880 C  CD2   . LEU B 2  781  ? 134.789 164.885 133.401 1.00 11.17  ? 781  LEU B CD2   1 
ATOM   16881 N  N     . ALA B 2  782  ? 131.533 161.196 132.525 1.00 11.11  ? 782  ALA B N     1 
ATOM   16882 C  CA    . ALA B 2  782  ? 131.469 160.437 131.281 1.00 9.13   ? 782  ALA B CA    1 
ATOM   16883 C  C     . ALA B 2  782  ? 130.036 160.277 130.787 1.00 13.62  ? 782  ALA B C     1 
ATOM   16884 O  O     . ALA B 2  782  ? 129.784 160.328 129.581 1.00 18.89  ? 782  ALA B O     1 
ATOM   16885 C  CB    . ALA B 2  782  ? 132.119 159.072 131.465 1.00 12.58  ? 782  ALA B CB    1 
ATOM   16886 N  N     . ALA B 2  783  ? 129.086 160.065 131.697 1.00 9.25   ? 783  ALA B N     1 
ATOM   16887 C  CA    . ALA B 2  783  ? 127.696 159.902 131.298 1.00 5.50   ? 783  ALA B CA    1 
ATOM   16888 C  C     . ALA B 2  783  ? 127.068 161.201 130.819 1.00 4.32   ? 783  ALA B C     1 
ATOM   16889 O  O     . ALA B 2  783  ? 126.061 161.159 130.109 1.00 3.08   ? 783  ALA B O     1 
ATOM   16890 C  CB    . ALA B 2  783  ? 126.884 159.329 132.455 1.00 10.36  ? 783  ALA B CB    1 
ATOM   16891 N  N     . LEU B 2  784  ? 127.630 162.345 131.192 1.00 2.46   ? 784  LEU B N     1 
ATOM   16892 C  CA    . LEU B 2  784  ? 127.113 163.639 130.779 1.00 1.96   ? 784  LEU B CA    1 
ATOM   16893 C  C     . LEU B 2  784  ? 127.593 164.052 129.397 1.00 8.35   ? 784  LEU B C     1 
ATOM   16894 O  O     . LEU B 2  784  ? 127.157 165.087 128.893 1.00 10.46  ? 784  LEU B O     1 
ATOM   16895 C  CB    . LEU B 2  784  ? 127.497 164.701 131.806 1.00 4.90   ? 784  LEU B CB    1 
ATOM   16896 C  CG    . LEU B 2  784  ? 126.616 164.814 133.052 1.00 9.89   ? 784  LEU B CG    1 
ATOM   16897 C  CD1   . LEU B 2  784  ? 127.208 165.795 134.015 1.00 6.28   ? 784  LEU B CD1   1 
ATOM   16898 C  CD2   . LEU B 2  784  ? 125.220 165.242 132.685 1.00 9.96   ? 784  LEU B CD2   1 
ATOM   16899 N  N     . VAL B 2  785  ? 128.483 163.281 128.782 1.00 10.61  ? 785  VAL B N     1 
ATOM   16900 C  CA    . VAL B 2  785  ? 128.881 163.538 127.403 1.00 8.93   ? 785  VAL B CA    1 
ATOM   16901 C  C     . VAL B 2  785  ? 127.748 163.191 126.448 1.00 9.75   ? 785  VAL B C     1 
ATOM   16902 O  O     . VAL B 2  785  ? 127.578 163.830 125.405 1.00 12.56  ? 785  VAL B O     1 
ATOM   16903 C  CB    . VAL B 2  785  ? 130.170 162.761 127.080 1.00 10.00  ? 785  VAL B CB    1 
ATOM   16904 C  CG1   . VAL B 2  785  ? 130.451 162.779 125.607 1.00 10.57  ? 785  VAL B CG1   1 
ATOM   16905 C  CG2   . VAL B 2  785  ? 131.337 163.361 127.821 1.00 10.74  ? 785  VAL B CG2   1 
ATOM   16906 N  N     . SER B 2  786  ? 126.961 162.185 126.790 1.00 10.53  ? 786  SER B N     1 
ATOM   16907 C  CA    . SER B 2  786  ? 125.841 161.771 125.960 1.00 2.96   ? 786  SER B CA    1 
ATOM   16908 C  C     . SER B 2  786  ? 124.750 162.836 125.968 1.00 1.99   ? 786  SER B C     1 
ATOM   16909 O  O     . SER B 2  786  ? 124.279 163.222 127.039 1.00 7.78   ? 786  SER B O     1 
ATOM   16910 C  CB    . SER B 2  786  ? 125.309 160.445 126.480 1.00 3.97   ? 786  SER B CB    1 
ATOM   16911 O  OG    . SER B 2  786  ? 124.242 159.963 125.700 1.00 22.83  ? 786  SER B OG    1 
ATOM   16912 N  N     . PRO B 2  787  ? 124.337 163.345 124.810 1.00 8.57   ? 787  PRO B N     1 
ATOM   16913 C  CA    . PRO B 2  787  ? 123.317 164.394 124.782 1.00 7.00   ? 787  PRO B CA    1 
ATOM   16914 C  C     . PRO B 2  787  ? 121.915 163.817 124.712 1.00 5.83   ? 787  PRO B C     1 
ATOM   16915 O  O     . PRO B 2  787  ? 121.679 162.773 124.102 1.00 16.68  ? 787  PRO B O     1 
ATOM   16916 C  CB    . PRO B 2  787  ? 123.661 165.166 123.506 1.00 3.31   ? 787  PRO B CB    1 
ATOM   16917 C  CG    . PRO B 2  787  ? 124.222 164.140 122.623 1.00 4.16   ? 787  PRO B CG    1 
ATOM   16918 C  CD    . PRO B 2  787  ? 124.882 163.089 123.469 1.00 4.34   ? 787  PRO B CD    1 
ATOM   16919 N  N     . TYR B 2  788  ? 120.977 164.527 125.337 1.00 0.48   ? 788  TYR B N     1 
ATOM   16920 C  CA    . TYR B 2  788  ? 119.594 164.069 125.481 1.00 0.97   ? 788  TYR B CA    1 
ATOM   16921 C  C     . TYR B 2  788  ? 119.548 162.667 126.064 1.00 0.43   ? 788  TYR B C     1 
ATOM   16922 O  O     . TYR B 2  788  ? 118.876 161.777 125.555 1.00 6.35   ? 788  TYR B O     1 
ATOM   16923 C  CB    . TYR B 2  788  ? 118.835 164.134 124.154 1.00 0.65   ? 788  TYR B CB    1 
ATOM   16924 C  CG    . TYR B 2  788  ? 118.888 165.487 123.519 1.00 1.37   ? 788  TYR B CG    1 
ATOM   16925 C  CD1   . TYR B 2  788  ? 118.196 166.536 124.069 1.00 1.76   ? 788  TYR B CD1   1 
ATOM   16926 C  CD2   . TYR B 2  788  ? 119.633 165.720 122.380 1.00 0.42   ? 788  TYR B CD2   1 
ATOM   16927 C  CE1   . TYR B 2  788  ? 118.242 167.776 123.518 1.00 3.56   ? 788  TYR B CE1   1 
ATOM   16928 C  CE2   . TYR B 2  788  ? 119.684 166.965 121.820 1.00 0.79   ? 788  TYR B CE2   1 
ATOM   16929 C  CZ    . TYR B 2  788  ? 118.982 167.989 122.397 1.00 7.00   ? 788  TYR B CZ    1 
ATOM   16930 O  OH    . TYR B 2  788  ? 119.007 169.250 121.869 1.00 6.82   ? 788  TYR B OH    1 
ATOM   16931 N  N     . ALA B 2  789  ? 120.288 162.474 127.149 1.00 3.43   ? 789  ALA B N     1 
ATOM   16932 C  CA    . ALA B 2  789  ? 120.490 161.138 127.683 1.00 2.06   ? 789  ALA B CA    1 
ATOM   16933 C  C     . ALA B 2  789  ? 119.247 160.570 128.347 1.00 5.85   ? 789  ALA B C     1 
ATOM   16934 O  O     . ALA B 2  789  ? 119.119 159.348 128.427 1.00 11.26  ? 789  ALA B O     1 
ATOM   16935 C  CB    . ALA B 2  789  ? 121.657 161.146 128.660 1.00 2.50   ? 789  ALA B CB    1 
ATOM   16936 N  N     . ASN B 2  790  ? 118.331 161.415 128.820 1.00 4.64   ? 790  ASN B N     1 
ATOM   16937 C  CA    . ASN B 2  790  ? 117.078 160.936 129.383 1.00 0.29   ? 790  ASN B CA    1 
ATOM   16938 C  C     . ASN B 2  790  ? 116.053 160.567 128.322 1.00 6.47   ? 790  ASN B C     1 
ATOM   16939 O  O     . ASN B 2  790  ? 114.997 160.038 128.668 1.00 7.11   ? 790  ASN B O     1 
ATOM   16940 C  CB    . ASN B 2  790  ? 116.474 161.972 130.328 1.00 0.09   ? 790  ASN B CB    1 
ATOM   16941 C  CG    . ASN B 2  790  ? 116.601 163.370 129.818 1.00 14.06  ? 790  ASN B CG    1 
ATOM   16942 O  OD1   . ASN B 2  790  ? 117.583 163.716 129.186 1.00 6.08   ? 790  ASN B OD1   1 
ATOM   16943 N  ND2   . ASN B 2  790  ? 115.590 164.182 130.064 1.00 14.77  ? 790  ASN B ND2   1 
ATOM   16944 N  N     . CYS B 2  791  ? 116.323 160.841 127.051 1.00 5.38   ? 791  CYS B N     1 
ATOM   16945 C  CA    . CYS B 2  791  ? 115.483 160.365 125.966 1.00 11.11  ? 791  CYS B CA    1 
ATOM   16946 C  C     . CYS B 2  791  ? 115.948 159.033 125.407 1.00 1.15   ? 791  CYS B C     1 
ATOM   16947 O  O     . CYS B 2  791  ? 115.338 158.527 124.469 1.00 3.72   ? 791  CYS B O     1 
ATOM   16948 C  CB    . CYS B 2  791  ? 115.424 161.405 124.854 1.00 1.12   ? 791  CYS B CB    1 
ATOM   16949 S  SG    . CYS B 2  791  ? 114.910 163.018 125.423 1.00 12.55  ? 791  CYS B SG    1 
ATOM   16950 N  N     . THR B 2  792  ? 116.995 158.459 125.971 1.00 4.35   ? 792  THR B N     1 
ATOM   16951 C  CA    . THR B 2  792  ? 117.567 157.183 125.579 1.00 6.41   ? 792  THR B CA    1 
ATOM   16952 C  C     . THR B 2  792  ? 117.372 156.176 126.703 1.00 8.47   ? 792  THR B C     1 
ATOM   16953 O  O     . THR B 2  792  ? 117.326 156.541 127.878 1.00 11.07  ? 792  THR B O     1 
ATOM   16954 C  CB    . THR B 2  792  ? 119.059 157.353 125.264 1.00 7.40   ? 792  THR B CB    1 
ATOM   16955 O  OG1   . THR B 2  792  ? 119.229 158.409 124.316 1.00 15.59  ? 792  THR B OG1   1 
ATOM   16956 C  CG2   . THR B 2  792  ? 119.671 156.101 124.716 1.00 9.07   ? 792  THR B CG2   1 
ATOM   16957 N  N     . GLN B 2  793  ? 117.241 154.911 126.338 1.00 12.29  ? 793  GLN B N     1 
ATOM   16958 C  CA    . GLN B 2  793  ? 117.143 153.866 127.344 1.00 12.18  ? 793  GLN B CA    1 
ATOM   16959 C  C     . GLN B 2  793  ? 118.434 153.813 128.154 1.00 20.67  ? 793  GLN B C     1 
ATOM   16960 O  O     . GLN B 2  793  ? 119.522 153.783 127.574 1.00 27.78  ? 793  GLN B O     1 
ATOM   16961 C  CB    . GLN B 2  793  ? 116.854 152.521 126.695 1.00 14.88  ? 793  GLN B CB    1 
ATOM   16962 C  CG    . GLN B 2  793  ? 117.517 151.358 127.376 1.00 18.40  ? 793  GLN B CG    1 
ATOM   16963 C  CD    . GLN B 2  793  ? 117.294 150.043 126.667 1.00 23.35  ? 793  GLN B CD    1 
ATOM   16964 O  OE1   . GLN B 2  793  ? 117.997 149.705 125.724 1.00 29.05  ? 793  GLN B OE1   1 
ATOM   16965 N  NE2   . GLN B 2  793  ? 116.321 149.282 127.139 1.00 22.79  ? 793  GLN B NE2   1 
ATOM   16966 N  N     . PRO B 2  794  ? 118.356 153.798 129.486 1.00 28.90  ? 794  PRO B N     1 
ATOM   16967 C  CA    . PRO B 2  794  ? 119.562 154.019 130.307 1.00 24.26  ? 794  PRO B CA    1 
ATOM   16968 C  C     . PRO B 2  794  ? 120.692 153.006 130.108 1.00 23.48  ? 794  PRO B C     1 
ATOM   16969 O  O     . PRO B 2  794  ? 121.871 153.387 130.222 1.00 22.32  ? 794  PRO B O     1 
ATOM   16970 C  CB    . PRO B 2  794  ? 119.006 153.978 131.736 1.00 21.58  ? 794  PRO B CB    1 
ATOM   16971 C  CG    . PRO B 2  794  ? 117.569 154.362 131.588 1.00 19.26  ? 794  PRO B CG    1 
ATOM   16972 C  CD    . PRO B 2  794  ? 117.134 153.741 130.308 1.00 22.44  ? 794  PRO B CD    1 
ATOM   16973 N  N     . ALA B 2  795  ? 120.383 151.741 129.820 1.00 18.76  ? 795  ALA B N     1 
ATOM   16974 C  CA    . ALA B 2  795  ? 121.438 150.755 129.603 1.00 24.88  ? 795  ALA B CA    1 
ATOM   16975 C  C     . ALA B 2  795  ? 122.369 151.183 128.476 1.00 30.20  ? 795  ALA B C     1 
ATOM   16976 O  O     . ALA B 2  795  ? 123.576 150.910 128.510 1.00 28.47  ? 795  ALA B O     1 
ATOM   16977 C  CB    . ALA B 2  795  ? 120.823 149.388 129.307 1.00 23.37  ? 795  ALA B CB    1 
ATOM   16978 N  N     . ARG B 2  796  ? 121.827 151.870 127.471 1.00 25.96  ? 796  ARG B N     1 
ATOM   16979 C  CA    . ARG B 2  796  ? 122.664 152.409 126.408 1.00 22.49  ? 796  ARG B CA    1 
ATOM   16980 C  C     . ARG B 2  796  ? 123.552 153.542 126.907 1.00 24.89  ? 796  ARG B C     1 
ATOM   16981 O  O     . ARG B 2  796  ? 124.659 153.727 126.394 1.00 21.90  ? 796  ARG B O     1 
ATOM   16982 C  CB    . ARG B 2  796  ? 121.787 152.865 125.245 1.00 25.16  ? 796  ARG B CB    1 
ATOM   16983 C  CG    . ARG B 2  796  ? 121.023 151.738 124.551 1.00 24.61  ? 796  ARG B CG    1 
ATOM   16984 C  CD    . ARG B 2  796  ? 121.809 150.437 124.541 1.00 23.92  ? 796  ARG B CD    1 
ATOM   16985 N  NE    . ARG B 2  796  ? 122.963 150.506 123.651 1.00 27.86  ? 796  ARG B NE    1 
ATOM   16986 C  CZ    . ARG B 2  796  ? 123.442 149.479 122.962 1.00 30.03  ? 796  ARG B CZ    1 
ATOM   16987 N  NH1   . ARG B 2  796  ? 122.912 148.271 123.061 1.00 27.46  ? 796  ARG B NH1   1 
ATOM   16988 N  NH2   . ARG B 2  796  ? 124.487 149.664 122.165 1.00 24.46  ? 796  ARG B NH2   1 
ATOM   16989 N  N     . VAL B 2  797  ? 123.108 154.292 127.916 1.00 28.25  ? 797  VAL B N     1 
ATOM   16990 C  CA    . VAL B 2  797  ? 123.975 155.312 128.500 1.00 27.33  ? 797  VAL B CA    1 
ATOM   16991 C  C     . VAL B 2  797  ? 125.131 154.658 129.248 1.00 27.37  ? 797  VAL B C     1 
ATOM   16992 O  O     . VAL B 2  797  ? 126.258 155.171 129.256 1.00 27.22  ? 797  VAL B O     1 
ATOM   16993 C  CB    . VAL B 2  797  ? 123.165 156.261 129.402 1.00 22.93  ? 797  VAL B CB    1 
ATOM   16994 C  CG1   . VAL B 2  797  ? 123.931 157.553 129.637 1.00 20.57  ? 797  VAL B CG1   1 
ATOM   16995 C  CG2   . VAL B 2  797  ? 121.813 156.558 128.788 1.00 20.19  ? 797  VAL B CG2   1 
ATOM   16996 N  N     . THR B 2  798  ? 124.874 153.518 129.890 1.00 25.73  ? 798  THR B N     1 
ATOM   16997 C  CA    . THR B 2  798  ? 125.968 152.743 130.474 1.00 25.71  ? 798  THR B CA    1 
ATOM   16998 C  C     . THR B 2  798  ? 126.952 152.275 129.402 1.00 27.47  ? 798  THR B C     1 
ATOM   16999 O  O     . THR B 2  798  ? 128.179 152.396 129.568 1.00 32.32  ? 798  THR B O     1 
ATOM   17000 C  CB    . THR B 2  798  ? 125.401 151.549 131.238 1.00 26.85  ? 798  THR B CB    1 
ATOM   17001 O  OG1   . THR B 2  798  ? 124.613 152.019 132.334 1.00 30.28  ? 798  THR B OG1   1 
ATOM   17002 C  CG2   . THR B 2  798  ? 126.510 150.669 131.769 1.00 25.66  ? 798  THR B CG2   1 
ATOM   17003 N  N     . TYR B 2  799  ? 126.427 151.744 128.294 1.00 25.86  ? 799  TYR B N     1 
ATOM   17004 C  CA    . TYR B 2  799  ? 127.274 151.367 127.164 1.00 25.36  ? 799  TYR B CA    1 
ATOM   17005 C  C     . TYR B 2  799  ? 128.125 152.541 126.702 1.00 25.42  ? 799  TYR B C     1 
ATOM   17006 O  O     . TYR B 2  799  ? 129.286 152.367 126.320 1.00 24.57  ? 799  TYR B O     1 
ATOM   17007 C  CB    . TYR B 2  799  ? 126.416 150.875 126.000 1.00 26.88  ? 799  TYR B CB    1 
ATOM   17008 C  CG    . TYR B 2  799  ? 126.087 149.405 126.002 1.00 26.80  ? 799  TYR B CG    1 
ATOM   17009 C  CD1   . TYR B 2  799  ? 126.766 148.523 125.185 1.00 27.87  ? 799  TYR B CD1   1 
ATOM   17010 C  CD2   . TYR B 2  799  ? 125.064 148.908 126.792 1.00 26.59  ? 799  TYR B CD2   1 
ATOM   17011 C  CE1   . TYR B 2  799  ? 126.452 147.180 125.178 1.00 32.38  ? 799  TYR B CE1   1 
ATOM   17012 C  CE2   . TYR B 2  799  ? 124.743 147.575 126.792 1.00 23.28  ? 799  TYR B CE2   1 
ATOM   17013 C  CZ    . TYR B 2  799  ? 125.438 146.714 125.985 1.00 33.07  ? 799  TYR B CZ    1 
ATOM   17014 O  OH    . TYR B 2  799  ? 125.115 145.380 125.984 1.00 34.13  ? 799  TYR B OH    1 
ATOM   17015 N  N     . GLU B 2  800  ? 127.549 153.743 126.699 1.00 23.77  ? 800  GLU B N     1 
ATOM   17016 C  CA    . GLU B 2  800  ? 128.293 154.918 126.261 1.00 26.96  ? 800  GLU B CA    1 
ATOM   17017 C  C     . GLU B 2  800  ? 129.418 155.261 127.228 1.00 24.49  ? 800  GLU B C     1 
ATOM   17018 O  O     . GLU B 2  800  ? 130.541 155.555 126.807 1.00 19.32  ? 800  GLU B O     1 
ATOM   17019 C  CB    . GLU B 2  800  ? 127.360 156.112 126.089 1.00 23.09  ? 800  GLU B CB    1 
ATOM   17020 C  CG    . GLU B 2  800  ? 128.053 157.464 126.246 1.00 22.73  ? 800  GLU B CG    1 
ATOM   17021 C  CD    . GLU B 2  800  ? 129.061 157.765 125.147 1.00 25.07  ? 800  GLU B CD    1 
ATOM   17022 O  OE1   . GLU B 2  800  ? 129.244 156.935 124.238 1.00 21.04  ? 800  GLU B OE1   1 
ATOM   17023 O  OE2   . GLU B 2  800  ? 129.677 158.847 125.189 1.00 26.49  ? 800  GLU B OE2   1 
ATOM   17024 N  N     . THR B 2  801  ? 129.132 155.247 128.530 1.00 28.48  ? 801  THR B N     1 
ATOM   17025 C  CA    . THR B 2  801  ? 130.201 155.472 129.500 1.00 28.18  ? 801  THR B CA    1 
ATOM   17026 C  C     . THR B 2  801  ? 131.352 154.503 129.272 1.00 30.38  ? 801  THR B C     1 
ATOM   17027 O  O     . THR B 2  801  ? 132.520 154.884 129.385 1.00 28.54  ? 801  THR B O     1 
ATOM   17028 C  CB    . THR B 2  801  ? 129.682 155.320 130.926 1.00 26.68  ? 801  THR B CB    1 
ATOM   17029 O  OG1   . THR B 2  801  ? 129.180 153.993 131.104 1.00 30.81  ? 801  THR B OG1   1 
ATOM   17030 C  CG2   . THR B 2  801  ? 128.575 156.297 131.190 1.00 25.57  ? 801  THR B CG2   1 
ATOM   17031 N  N     . ASN B 2  802  ? 131.036 153.254 128.932 1.00 35.46  ? 802  ASN B N     1 
ATOM   17032 C  CA    . ASN B 2  802  ? 132.087 152.304 128.573 1.00 30.67  ? 802  ASN B CA    1 
ATOM   17033 C  C     . ASN B 2  802  ? 132.811 152.714 127.293 1.00 33.09  ? 802  ASN B C     1 
ATOM   17034 O  O     . ASN B 2  802  ? 134.037 152.601 127.209 1.00 33.78  ? 802  ASN B O     1 
ATOM   17035 C  CB    . ASN B 2  802  ? 131.493 150.908 128.435 1.00 29.85  ? 802  ASN B CB    1 
ATOM   17036 C  CG    . ASN B 2  802  ? 131.391 150.196 129.760 1.00 33.09  ? 802  ASN B CG    1 
ATOM   17037 O  OD1   . ASN B 2  802  ? 132.399 149.818 130.351 1.00 34.66  ? 802  ASN B OD1   1 
ATOM   17038 N  ND2   . ASN B 2  802  ? 130.171 150.040 130.254 1.00 34.17  ? 802  ASN B ND2   1 
ATOM   17039 N  N     . GLN B 2  803  ? 132.080 153.205 126.292 1.00 32.51  ? 803  GLN B N     1 
ATOM   17040 C  CA    . GLN B 2  803  ? 132.671 153.505 124.990 1.00 27.99  ? 803  GLN B CA    1 
ATOM   17041 C  C     . GLN B 2  803  ? 133.263 154.903 124.876 1.00 30.44  ? 803  GLN B C     1 
ATOM   17042 O  O     . GLN B 2  803  ? 134.154 155.102 124.053 1.00 29.45  ? 803  GLN B O     1 
ATOM   17043 C  CB    . GLN B 2  803  ? 131.635 153.330 123.879 1.00 25.73  ? 803  GLN B CB    1 
ATOM   17044 C  CG    . GLN B 2  803  ? 131.205 151.904 123.644 1.00 30.94  ? 803  GLN B CG    1 
ATOM   17045 C  CD    . GLN B 2  803  ? 129.850 151.832 122.995 1.00 33.34  ? 803  GLN B CD    1 
ATOM   17046 O  OE1   . GLN B 2  803  ? 129.277 152.853 122.641 1.00 33.99  ? 803  GLN B OE1   1 
ATOM   17047 N  NE2   . GLN B 2  803  ? 129.315 150.631 122.861 1.00 29.67  ? 803  GLN B NE2   1 
ATOM   17048 N  N     . GLY B 2  804  ? 132.796 155.872 125.662 1.00 32.59  ? 804  GLY B N     1 
ATOM   17049 C  CA    . GLY B 2  804  ? 133.326 157.223 125.547 1.00 28.63  ? 804  GLY B CA    1 
ATOM   17050 C  C     . GLY B 2  804  ? 134.791 157.330 125.929 1.00 33.67  ? 804  GLY B C     1 
ATOM   17051 O  O     . GLY B 2  804  ? 135.507 158.207 125.439 1.00 27.63  ? 804  GLY B O     1 
ATOM   17052 N  N     . ARG B 2  805  ? 135.251 156.457 126.825 1.00 36.21  ? 805  ARG B N     1 
ATOM   17053 C  CA    . ARG B 2  805  ? 136.639 156.468 127.272 1.00 32.60  ? 805  ARG B CA    1 
ATOM   17054 C  C     . ARG B 2  805  ? 137.573 155.627 126.408 1.00 34.23  ? 805  ARG B C     1 
ATOM   17055 O  O     . ARG B 2  805  ? 138.787 155.677 126.616 1.00 38.98  ? 805  ARG B O     1 
ATOM   17056 C  CB    . ARG B 2  805  ? 136.708 156.009 128.730 1.00 33.15  ? 805  ARG B CB    1 
ATOM   17057 C  CG    . ARG B 2  805  ? 135.765 156.775 129.643 1.00 32.90  ? 805  ARG B CG    1 
ATOM   17058 C  CD    . ARG B 2  805  ? 135.703 156.221 131.052 1.00 31.38  ? 805  ARG B CD    1 
ATOM   17059 N  NE    . ARG B 2  805  ? 135.127 154.883 131.108 1.00 35.34  ? 805  ARG B NE    1 
ATOM   17060 C  CZ    . ARG B 2  805  ? 135.795 153.783 131.421 1.00 35.45  ? 805  ARG B CZ    1 
ATOM   17061 N  NH1   . ARG B 2  805  ? 137.085 153.814 131.703 1.00 34.00  ? 805  ARG B NH1   1 
ATOM   17062 N  NH2   . ARG B 2  805  ? 135.149 152.622 131.458 1.00 32.15  ? 805  ARG B NH2   1 
ATOM   17063 N  N     . GLN B 2  806  ? 137.049 154.860 125.451 1.00 31.73  ? 806  GLN B N     1 
ATOM   17064 C  CA    . GLN B 2  806  ? 137.884 154.068 124.555 1.00 27.12  ? 806  GLN B CA    1 
ATOM   17065 C  C     . GLN B 2  806  ? 138.242 154.800 123.271 1.00 26.98  ? 806  GLN B C     1 
ATOM   17066 O  O     . GLN B 2  806  ? 139.032 154.277 122.483 1.00 27.36  ? 806  GLN B O     1 
ATOM   17067 C  CB    . GLN B 2  806  ? 137.178 152.759 124.197 1.00 26.75  ? 806  GLN B CB    1 
ATOM   17068 C  CG    . GLN B 2  806  ? 136.546 152.046 125.371 1.00 30.98  ? 806  GLN B CG    1 
ATOM   17069 C  CD    . GLN B 2  806  ? 137.426 150.960 125.945 1.00 36.42  ? 806  GLN B CD    1 
ATOM   17070 O  OE1   . GLN B 2  806  ? 138.643 151.014 125.835 1.00 34.36  ? 806  GLN B OE1   1 
ATOM   17071 N  NE2   . GLN B 2  806  ? 136.810 149.972 126.579 1.00 35.60  ? 806  GLN B NE2   1 
ATOM   17072 N  N     . THR B 2  807  ? 137.695 155.986 123.045 1.00 26.69  ? 807  THR B N     1 
ATOM   17073 C  CA    . THR B 2  807  ? 137.786 156.634 121.746 1.00 22.28  ? 807  THR B CA    1 
ATOM   17074 C  C     . THR B 2  807  ? 139.103 157.377 121.575 1.00 18.66  ? 807  THR B C     1 
ATOM   17075 O  O     . THR B 2  807  ? 139.717 157.817 122.550 1.00 23.98  ? 807  THR B O     1 
ATOM   17076 C  CB    . THR B 2  807  ? 136.627 157.605 121.553 1.00 21.78  ? 807  THR B CB    1 
ATOM   17077 O  OG1   . THR B 2  807  ? 136.994 158.878 122.072 1.00 17.99  ? 807  THR B OG1   1 
ATOM   17078 C  CG2   . THR B 2  807  ? 135.419 157.132 122.292 1.00 17.91  ? 807  THR B CG2   1 
ATOM   17079 N  N     . GLY B 2  808  ? 139.532 157.516 120.312 1.00 11.80  ? 808  GLY B N     1 
ATOM   17080 C  CA    . GLY B 2  808  ? 140.774 158.190 120.009 1.00 10.12  ? 808  GLY B CA    1 
ATOM   17081 C  C     . GLY B 2  808  ? 140.685 159.694 120.132 1.00 12.77  ? 808  GLY B C     1 
ATOM   17082 O  O     . GLY B 2  808  ? 139.609 160.274 120.196 1.00 16.95  ? 808  GLY B O     1 
ATOM   17083 N  N     . GLY B 2  809  ? 141.852 160.330 120.157 1.00 13.40  ? 809  GLY B N     1 
ATOM   17084 C  CA    . GLY B 2  809  ? 141.908 161.782 120.221 1.00 11.02  ? 809  GLY B CA    1 
ATOM   17085 C  C     . GLY B 2  809  ? 143.310 162.272 120.512 1.00 16.64  ? 809  GLY B C     1 
ATOM   17086 O  O     . GLY B 2  809  ? 144.293 161.578 120.246 1.00 19.18  ? 809  GLY B O     1 
ATOM   17087 N  N     . TRP B 2  810  ? 143.387 163.488 121.053 1.00 15.92  ? 810  TRP B N     1 
ATOM   17088 C  CA    . TRP B 2  810  ? 144.640 164.048 121.563 1.00 15.58  ? 810  TRP B CA    1 
ATOM   17089 C  C     . TRP B 2  810  ? 144.845 163.502 122.975 1.00 25.94  ? 810  TRP B C     1 
ATOM   17090 O  O     . TRP B 2  810  ? 144.512 164.139 123.976 1.00 29.18  ? 810  TRP B O     1 
ATOM   17091 C  CB    . TRP B 2  810  ? 144.593 165.571 121.565 1.00 12.27  ? 810  TRP B CB    1 
ATOM   17092 C  CG    . TRP B 2  810  ? 144.372 166.205 120.232 1.00 16.49  ? 810  TRP B CG    1 
ATOM   17093 C  CD1   . TRP B 2  810  ? 144.544 165.629 119.017 1.00 13.66  ? 810  TRP B CD1   1 
ATOM   17094 C  CD2   . TRP B 2  810  ? 143.912 167.539 119.982 1.00 18.11  ? 810  TRP B CD2   1 
ATOM   17095 N  NE1   . TRP B 2  810  ? 144.236 166.520 118.020 1.00 10.29  ? 810  TRP B NE1   1 
ATOM   17096 C  CE2   . TRP B 2  810  ? 143.843 167.701 118.587 1.00 12.88  ? 810  TRP B CE2   1 
ATOM   17097 C  CE3   . TRP B 2  810  ? 143.554 168.612 120.802 1.00 13.78  ? 810  TRP B CE3   1 
ATOM   17098 C  CZ2   . TRP B 2  810  ? 143.431 168.890 117.992 1.00 9.28   ? 810  TRP B CZ2   1 
ATOM   17099 C  CZ3   . TRP B 2  810  ? 143.150 169.796 120.207 1.00 15.81  ? 810  TRP B CZ3   1 
ATOM   17100 C  CH2   . TRP B 2  810  ? 143.093 169.923 118.817 1.00 9.02   ? 810  TRP B CH2   1 
ATOM   17101 N  N     . TYR B 2  811  ? 145.407 162.290 123.053 1.00 22.02  ? 811  TYR B N     1 
ATOM   17102 C  CA    . TYR B 2  811  ? 145.464 161.580 124.328 1.00 24.51  ? 811  TYR B CA    1 
ATOM   17103 C  C     . TYR B 2  811  ? 146.352 162.279 125.349 1.00 29.44  ? 811  TYR B C     1 
ATOM   17104 O  O     . TYR B 2  811  ? 146.145 162.101 126.554 1.00 29.94  ? 811  TYR B O     1 
ATOM   17105 C  CB    . TYR B 2  811  ? 145.921 160.134 124.115 1.00 26.18  ? 811  TYR B CB    1 
ATOM   17106 C  CG    . TYR B 2  811  ? 147.392 159.937 123.810 1.00 30.15  ? 811  TYR B CG    1 
ATOM   17107 C  CD1   . TYR B 2  811  ? 147.940 160.356 122.609 1.00 24.72  ? 811  TYR B CD1   1 
ATOM   17108 C  CD2   . TYR B 2  811  ? 148.226 159.311 124.726 1.00 31.61  ? 811  TYR B CD2   1 
ATOM   17109 C  CE1   . TYR B 2  811  ? 149.275 160.166 122.332 1.00 23.39  ? 811  TYR B CE1   1 
ATOM   17110 C  CE2   . TYR B 2  811  ? 149.560 159.120 124.460 1.00 29.98  ? 811  TYR B CE2   1 
ATOM   17111 C  CZ    . TYR B 2  811  ? 150.080 159.546 123.258 1.00 29.36  ? 811  TYR B CZ    1 
ATOM   17112 O  OH    . TYR B 2  811  ? 151.414 159.361 122.987 1.00 30.71  ? 811  TYR B OH    1 
ATOM   17113 N  N     . CYS B 2  812  ? 147.327 163.061 124.898 1.00 26.69  ? 812  CYS B N     1 
ATOM   17114 C  CA    . CYS B 2  812  ? 148.080 163.959 125.760 1.00 31.58  ? 812  CYS B CA    1 
ATOM   17115 C  C     . CYS B 2  812  ? 148.720 165.013 124.875 1.00 35.18  ? 812  CYS B C     1 
ATOM   17116 O  O     . CYS B 2  812  ? 148.978 164.775 123.694 1.00 34.77  ? 812  CYS B O     1 
ATOM   17117 C  CB    . CYS B 2  812  ? 149.139 163.214 126.584 1.00 33.00  ? 812  CYS B CB    1 
ATOM   17118 S  SG    . CYS B 2  812  ? 150.498 162.503 125.643 1.00 45.74  ? 812  CYS B SG    1 
ATOM   17119 N  N     . PHE B 2  813  ? 148.967 166.183 125.451 1.00 33.57  ? 813  PHE B N     1 
ATOM   17120 C  CA    . PHE B 2  813  ? 149.577 167.281 124.715 1.00 29.55  ? 813  PHE B CA    1 
ATOM   17121 C  C     . PHE B 2  813  ? 151.096 167.245 124.754 1.00 33.39  ? 813  PHE B C     1 
ATOM   17122 O  O     . PHE B 2  813  ? 151.737 168.137 124.197 1.00 38.87  ? 813  PHE B O     1 
ATOM   17123 C  CB    . PHE B 2  813  ? 149.075 168.626 125.244 1.00 30.71  ? 813  PHE B CB    1 
ATOM   17124 C  CG    . PHE B 2  813  ? 147.626 168.885 124.962 1.00 34.00  ? 813  PHE B CG    1 
ATOM   17125 C  CD1   . PHE B 2  813  ? 146.646 168.400 125.802 1.00 34.52  ? 813  PHE B CD1   1 
ATOM   17126 C  CD2   . PHE B 2  813  ? 147.247 169.627 123.859 1.00 30.92  ? 813  PHE B CD2   1 
ATOM   17127 C  CE1   . PHE B 2  813  ? 145.319 168.635 125.541 1.00 36.63  ? 813  PHE B CE1   1 
ATOM   17128 C  CE2   . PHE B 2  813  ? 145.926 169.870 123.598 1.00 31.59  ? 813  PHE B CE2   1 
ATOM   17129 C  CZ    . PHE B 2  813  ? 144.958 169.373 124.438 1.00 34.06  ? 813  PHE B CZ    1 
ATOM   17130 N  N     . SER B 2  814  ? 151.685 166.244 125.401 1.00 36.47  ? 814  SER B N     1 
ATOM   17131 C  CA    . SER B 2  814  ? 153.131 166.063 125.387 1.00 37.96  ? 814  SER B CA    1 
ATOM   17132 C  C     . SER B 2  814  ? 153.517 164.716 124.790 1.00 38.21  ? 814  SER B C     1 
ATOM   17133 O  O     . SER B 2  814  ? 154.467 164.090 125.261 1.00 40.13  ? 814  SER B O     1 
ATOM   17134 C  CB    . SER B 2  814  ? 153.714 166.199 126.791 1.00 35.56  ? 814  SER B CB    1 
ATOM   17135 O  OG    . SER B 2  814  ? 153.145 165.240 127.660 1.00 40.37  ? 814  SER B OG    1 
ATOM   17136 N  N     . TRP B 2  815  ? 152.786 164.257 123.777 1.00 28.65  ? 815  TRP B N     1 
ATOM   17137 C  CA    . TRP B 2  815  ? 153.122 162.995 123.124 1.00 27.21  ? 815  TRP B CA    1 
ATOM   17138 C  C     . TRP B 2  815  ? 154.532 162.939 122.536 1.00 30.91  ? 815  TRP B C     1 
ATOM   17139 O  O     . TRP B 2  815  ? 155.173 161.883 122.675 1.00 30.68  ? 815  TRP B O     1 
ATOM   17140 C  CB    . TRP B 2  815  ? 152.064 162.673 122.055 1.00 29.72  ? 815  TRP B CB    1 
ATOM   17141 C  CG    . TRP B 2  815  ? 151.762 163.794 121.109 1.00 28.71  ? 815  TRP B CG    1 
ATOM   17142 C  CD1   . TRP B 2  815  ? 151.029 164.909 121.373 1.00 26.35  ? 815  TRP B CD1   1 
ATOM   17143 C  CD2   . TRP B 2  815  ? 152.172 163.899 119.745 1.00 25.92  ? 815  TRP B CD2   1 
ATOM   17144 N  NE1   . TRP B 2  815  ? 150.969 165.709 120.265 1.00 26.64  ? 815  TRP B NE1   1 
ATOM   17145 C  CE2   . TRP B 2  815  ? 151.663 165.110 119.249 1.00 26.82  ? 815  TRP B CE2   1 
ATOM   17146 C  CE3   . TRP B 2  815  ? 152.928 163.090 118.897 1.00 28.85  ? 815  TRP B CE3   1 
ATOM   17147 C  CZ2   . TRP B 2  815  ? 151.882 165.530 117.942 1.00 28.56  ? 815  TRP B CZ2   1 
ATOM   17148 C  CZ3   . TRP B 2  815  ? 153.147 163.510 117.603 1.00 29.42  ? 815  TRP B CZ3   1 
ATOM   17149 C  CH2   . TRP B 2  815  ? 152.625 164.717 117.137 1.00 29.02  ? 815  TRP B CH2   1 
ATOM   17150 N  N     . PRO B 2  816  ? 155.072 163.974 121.873 1.00 33.27  ? 816  PRO B N     1 
ATOM   17151 C  CA    . PRO B 2  816  ? 156.399 163.808 121.262 1.00 34.26  ? 816  PRO B CA    1 
ATOM   17152 C  C     . PRO B 2  816  ? 157.517 163.642 122.271 1.00 35.64  ? 816  PRO B C     1 
ATOM   17153 O  O     . PRO B 2  816  ? 158.600 163.178 121.899 1.00 34.01  ? 816  PRO B O     1 
ATOM   17154 C  CB    . PRO B 2  816  ? 156.580 165.093 120.440 1.00 31.70  ? 816  PRO B CB    1 
ATOM   17155 C  CG    . PRO B 2  816  ? 155.329 165.861 120.579 1.00 28.99  ? 816  PRO B CG    1 
ATOM   17156 C  CD    . PRO B 2  816  ? 154.653 165.383 121.794 1.00 30.54  ? 816  PRO B CD    1 
ATOM   17157 N  N     . TYR B 2  817  ? 157.294 164.006 123.535 1.00 37.33  ? 817  TYR B N     1 
ATOM   17158 C  CA    . TYR B 2  817  ? 158.295 163.871 124.582 1.00 37.13  ? 817  TYR B CA    1 
ATOM   17159 C  C     . TYR B 2  817  ? 158.192 162.537 125.304 1.00 33.54  ? 817  TYR B C     1 
ATOM   17160 O  O     . TYR B 2  817  ? 158.996 162.247 126.192 1.00 37.79  ? 817  TYR B O     1 
ATOM   17161 C  CB    . TYR B 2  817  ? 158.171 165.018 125.581 1.00 35.41  ? 817  TYR B CB    1 
ATOM   17162 C  CG    . TYR B 2  817  ? 158.383 166.374 124.970 1.00 35.14  ? 817  TYR B CG    1 
ATOM   17163 C  CD1   . TYR B 2  817  ? 159.648 166.795 124.598 1.00 35.82  ? 817  TYR B CD1   1 
ATOM   17164 C  CD2   . TYR B 2  817  ? 157.317 167.235 124.763 1.00 35.13  ? 817  TYR B CD2   1 
ATOM   17165 C  CE1   . TYR B 2  817  ? 159.846 168.031 124.034 1.00 38.36  ? 817  TYR B CE1   1 
ATOM   17166 C  CE2   . TYR B 2  817  ? 157.503 168.476 124.201 1.00 36.03  ? 817  TYR B CE2   1 
ATOM   17167 C  CZ    . TYR B 2  817  ? 158.771 168.869 123.839 1.00 37.61  ? 817  TYR B CZ    1 
ATOM   17168 O  OH    . TYR B 2  817  ? 158.971 170.105 123.279 1.00 37.52  ? 817  TYR B OH    1 
ATOM   17169 N  N     . ARG B 2  818  ? 157.233 161.706 124.920 1.00 32.66  ? 818  ARG B N     1 
ATOM   17170 C  CA    . ARG B 2  818  ? 156.964 160.462 125.616 1.00 36.38  ? 818  ARG B CA    1 
ATOM   17171 C  C     . ARG B 2  818  ? 157.297 159.291 124.706 1.00 38.11  ? 818  ARG B C     1 
ATOM   17172 O  O     . ARG B 2  818  ? 157.258 159.395 123.479 1.00 35.63  ? 818  ARG B O     1 
ATOM   17173 C  CB    . ARG B 2  818  ? 155.501 160.372 126.051 1.00 33.04  ? 818  ARG B CB    1 
ATOM   17174 C  CG    . ARG B 2  818  ? 155.064 161.509 126.929 1.00 31.66  ? 818  ARG B CG    1 
ATOM   17175 C  CD    . ARG B 2  818  ? 153.576 161.465 127.169 1.00 33.74  ? 818  ARG B CD    1 
ATOM   17176 N  NE    . ARG B 2  818  ? 153.198 160.330 127.997 1.00 36.93  ? 818  ARG B NE    1 
ATOM   17177 C  CZ    . ARG B 2  818  ? 152.927 160.413 129.289 1.00 35.54  ? 818  ARG B CZ    1 
ATOM   17178 N  NH1   . ARG B 2  818  ? 152.965 161.569 129.929 1.00 34.69  ? 818  ARG B NH1   1 
ATOM   17179 N  NH2   . ARG B 2  818  ? 152.612 159.309 129.957 1.00 33.19  ? 818  ARG B NH2   1 
ATOM   17180 N  N     . VAL B 2  819  ? 157.633 158.172 125.335 1.00 39.64  ? 819  VAL B N     1 
ATOM   17181 C  CA    . VAL B 2  819  ? 157.853 156.904 124.645 1.00 39.40  ? 819  VAL B CA    1 
ATOM   17182 C  C     . VAL B 2  819  ? 156.839 155.932 125.240 1.00 37.74  ? 819  VAL B C     1 
ATOM   17183 O  O     . VAL B 2  819  ? 157.099 155.278 126.253 1.00 41.07  ? 819  VAL B O     1 
ATOM   17184 C  CB    . VAL B 2  819  ? 159.286 156.388 124.797 1.00 37.93  ? 819  VAL B CB    1 
ATOM   17185 C  CG1   . VAL B 2  819  ? 159.469 155.115 124.024 1.00 37.19  ? 819  VAL B CG1   1 
ATOM   17186 C  CG2   . VAL B 2  819  ? 160.271 157.435 124.312 1.00 35.98  ? 819  VAL B CG2   1 
ATOM   17187 N  N     . ASP B 2  820  ? 155.673 155.837 124.617 1.00 39.21  ? 820  ASP B N     1 
ATOM   17188 C  CA    . ASP B 2  820  ? 154.557 155.077 125.151 1.00 35.92  ? 820  ASP B CA    1 
ATOM   17189 C  C     . ASP B 2  820  ? 154.368 153.784 124.367 1.00 35.64  ? 820  ASP B C     1 
ATOM   17190 O  O     . ASP B 2  820  ? 154.965 153.570 123.312 1.00 36.94  ? 820  ASP B O     1 
ATOM   17191 C  CB    . ASP B 2  820  ? 153.277 155.916 125.110 1.00 35.89  ? 820  ASP B CB    1 
ATOM   17192 C  CG    . ASP B 2  820  ? 153.241 156.987 126.182 1.00 37.87  ? 820  ASP B CG    1 
ATOM   17193 O  OD1   . ASP B 2  820  ? 153.758 156.749 127.290 1.00 40.89  ? 820  ASP B OD1   1 
ATOM   17194 O  OD2   . ASP B 2  820  ? 152.704 158.076 125.912 1.00 36.01  ? 820  ASP B OD2   1 
ATOM   17195 N  N     . MET B 2  821  ? 153.521 152.917 124.906 1.00 38.48  ? 821  MET B N     1 
ATOM   17196 C  CA    . MET B 2  821  ? 153.167 151.646 124.285 1.00 38.04  ? 821  MET B CA    1 
ATOM   17197 C  C     . MET B 2  821  ? 151.684 151.686 123.946 1.00 37.81  ? 821  MET B C     1 
ATOM   17198 O  O     . MET B 2  821  ? 150.854 151.969 124.815 1.00 37.78  ? 821  MET B O     1 
ATOM   17199 C  CB    . MET B 2  821  ? 153.488 150.472 125.212 1.00 39.32  ? 821  MET B CB    1 
ATOM   17200 C  CG    . MET B 2  821  ? 153.442 149.098 124.555 1.00 37.48  ? 821  MET B CG    1 
ATOM   17201 S  SD    . MET B 2  821  ? 154.601 148.926 123.186 1.00 49.35  ? 821  MET B SD    1 
ATOM   17202 C  CE    . MET B 2  821  ? 154.566 147.157 122.926 1.00 35.42  ? 821  MET B CE    1 
ATOM   17203 N  N     . ASN B 2  822  ? 151.362 151.413 122.683 1.00 28.02  ? 822  ASN B N     1 
ATOM   17204 C  CA    . ASN B 2  822  ? 149.988 151.249 122.218 1.00 30.32  ? 822  ASN B CA    1 
ATOM   17205 C  C     . ASN B 2  822  ? 149.134 152.483 122.513 1.00 31.10  ? 822  ASN B C     1 
ATOM   17206 O  O     . ASN B 2  822  ? 148.055 152.404 123.100 1.00 30.23  ? 822  ASN B O     1 
ATOM   17207 C  CB    . ASN B 2  822  ? 149.370 149.983 122.815 1.00 27.37  ? 822  ASN B CB    1 
ATOM   17208 C  CG    . ASN B 2  822  ? 150.183 148.753 122.512 1.00 31.45  ? 822  ASN B CG    1 
ATOM   17209 O  OD1   . ASN B 2  822  ? 151.141 148.809 121.749 1.00 32.06  ? 822  ASN B OD1   1 
ATOM   17210 N  ND2   . ASN B 2  822  ? 149.802 147.627 123.099 1.00 35.67  ? 822  ASN B ND2   1 
ATOM   17211 N  N     . ARG B 2  823  ? 149.629 153.629 122.064 1.00 24.40  ? 823  ARG B N     1 
ATOM   17212 C  CA    . ARG B 2  823  ? 148.936 154.900 122.196 1.00 21.46  ? 823  ARG B CA    1 
ATOM   17213 C  C     . ARG B 2  823  ? 148.659 155.476 120.818 1.00 24.06  ? 823  ARG B C     1 
ATOM   17214 O  O     . ARG B 2  823  ? 149.490 155.376 119.912 1.00 25.29  ? 823  ARG B O     1 
ATOM   17215 C  CB    . ARG B 2  823  ? 149.747 155.893 123.022 1.00 22.52  ? 823  ARG B CB    1 
ATOM   17216 C  CG    . ARG B 2  823  ? 149.810 155.555 124.492 1.00 27.76  ? 823  ARG B CG    1 
ATOM   17217 C  CD    . ARG B 2  823  ? 148.434 155.421 125.088 1.00 26.96  ? 823  ARG B CD    1 
ATOM   17218 N  NE    . ARG B 2  823  ? 148.313 154.248 125.941 1.00 31.78  ? 823  ARG B NE    1 
ATOM   17219 C  CZ    . ARG B 2  823  ? 147.241 153.472 125.988 1.00 33.66  ? 823  ARG B CZ    1 
ATOM   17220 N  NH1   . ARG B 2  823  ? 146.172 153.726 125.253 1.00 29.66  ? 823  ARG B NH1   1 
ATOM   17221 N  NH2   . ARG B 2  823  ? 147.239 152.419 126.796 1.00 30.82  ? 823  ARG B NH2   1 
ATOM   17222 N  N     . PHE B 2  824  ? 147.486 156.081 120.671 1.00 18.07  ? 824  PHE B N     1 
ATOM   17223 C  CA    . PHE B 2  824  ? 147.007 156.585 119.395 1.00 10.08  ? 824  PHE B CA    1 
ATOM   17224 C  C     . PHE B 2  824  ? 146.761 158.079 119.503 1.00 8.67   ? 824  PHE B C     1 
ATOM   17225 O  O     . PHE B 2  824  ? 146.040 158.529 120.394 1.00 18.65  ? 824  PHE B O     1 
ATOM   17226 C  CB    . PHE B 2  824  ? 145.729 155.851 118.977 1.00 8.97   ? 824  PHE B CB    1 
ATOM   17227 C  CG    . PHE B 2  824  ? 145.149 156.324 117.681 1.00 9.16   ? 824  PHE B CG    1 
ATOM   17228 C  CD1   . PHE B 2  824  ? 145.763 156.027 116.488 1.00 6.79   ? 824  PHE B CD1   1 
ATOM   17229 C  CD2   . PHE B 2  824  ? 143.980 157.056 117.657 1.00 11.81  ? 824  PHE B CD2   1 
ATOM   17230 C  CE1   . PHE B 2  824  ? 145.233 156.456 115.311 1.00 7.73   ? 824  PHE B CE1   1 
ATOM   17231 C  CE2   . PHE B 2  824  ? 143.455 157.486 116.474 1.00 7.28   ? 824  PHE B CE2   1 
ATOM   17232 C  CZ    . PHE B 2  824  ? 144.080 157.182 115.306 1.00 8.10   ? 824  PHE B CZ    1 
ATOM   17233 N  N     . PHE B 2  825  ? 147.355 158.839 118.599 1.00 4.94   ? 825  PHE B N     1 
ATOM   17234 C  CA    . PHE B 2  825  ? 147.124 160.271 118.500 1.00 9.07   ? 825  PHE B CA    1 
ATOM   17235 C  C     . PHE B 2  825  ? 146.339 160.543 117.228 1.00 5.87   ? 825  PHE B C     1 
ATOM   17236 O  O     . PHE B 2  825  ? 146.812 160.235 116.137 1.00 7.73   ? 825  PHE B O     1 
ATOM   17237 C  CB    . PHE B 2  825  ? 148.443 161.042 118.489 1.00 10.63  ? 825  PHE B CB    1 
ATOM   17238 C  CG    . PHE B 2  825  ? 148.274 162.521 118.369 1.00 9.01   ? 825  PHE B CG    1 
ATOM   17239 C  CD1   . PHE B 2  825  ? 148.001 163.288 119.475 1.00 12.33  ? 825  PHE B CD1   1 
ATOM   17240 C  CD2   . PHE B 2  825  ? 148.382 163.145 117.145 1.00 11.04  ? 825  PHE B CD2   1 
ATOM   17241 C  CE1   . PHE B 2  825  ? 147.841 164.643 119.361 1.00 10.50  ? 825  PHE B CE1   1 
ATOM   17242 C  CE2   . PHE B 2  825  ? 148.219 164.500 117.033 1.00 13.62  ? 825  PHE B CE2   1 
ATOM   17243 C  CZ    . PHE B 2  825  ? 147.948 165.247 118.139 1.00 9.32   ? 825  PHE B CZ    1 
ATOM   17244 N  N     . GLN B 2  826  ? 145.162 161.140 117.368 1.00 7.36   ? 826  GLN B N     1 
ATOM   17245 C  CA    . GLN B 2  826  ? 144.295 161.455 116.243 1.00 4.37   ? 826  GLN B CA    1 
ATOM   17246 C  C     . GLN B 2  826  ? 144.399 162.936 115.919 1.00 5.78   ? 826  GLN B C     1 
ATOM   17247 O  O     . GLN B 2  826  ? 144.192 163.776 116.791 1.00 10.93  ? 826  GLN B O     1 
ATOM   17248 C  CB    . GLN B 2  826  ? 142.852 161.070 116.560 1.00 11.24  ? 826  GLN B CB    1 
ATOM   17249 C  CG    . GLN B 2  826  ? 141.815 161.736 115.717 1.00 12.26  ? 826  GLN B CG    1 
ATOM   17250 C  CD    . GLN B 2  826  ? 140.458 161.137 115.903 1.00 1.87   ? 826  GLN B CD    1 
ATOM   17251 O  OE1   . GLN B 2  826  ? 140.328 159.952 116.156 1.00 1.84   ? 826  GLN B OE1   1 
ATOM   17252 N  NE2   . GLN B 2  826  ? 139.434 161.962 115.821 1.00 0.77   ? 826  GLN B NE2   1 
ATOM   17253 N  N     . PHE B 2  827  ? 144.692 163.243 114.655 1.00 2.65   ? 827  PHE B N     1 
ATOM   17254 C  CA    . PHE B 2  827  ? 145.077 164.594 114.258 1.00 3.67   ? 827  PHE B CA    1 
ATOM   17255 C  C     . PHE B 2  827  ? 143.947 165.594 114.446 1.00 5.95   ? 827  PHE B C     1 
ATOM   17256 O  O     . PHE B 2  827  ? 144.140 166.653 115.045 1.00 9.02   ? 827  PHE B O     1 
ATOM   17257 C  CB    . PHE B 2  827  ? 145.526 164.596 112.799 1.00 0.92   ? 827  PHE B CB    1 
ATOM   17258 C  CG    . PHE B 2  827  ? 146.732 163.757 112.530 1.00 5.65   ? 827  PHE B CG    1 
ATOM   17259 C  CD1   . PHE B 2  827  ? 147.714 163.604 113.480 1.00 7.08   ? 827  PHE B CD1   1 
ATOM   17260 C  CD2   . PHE B 2  827  ? 146.879 163.114 111.326 1.00 5.39   ? 827  PHE B CD2   1 
ATOM   17261 C  CE1   . PHE B 2  827  ? 148.810 162.834 113.229 1.00 4.61   ? 827  PHE B CE1   1 
ATOM   17262 C  CE2   . PHE B 2  827  ? 147.976 162.346 111.079 1.00 6.84   ? 827  PHE B CE2   1 
ATOM   17263 C  CZ    . PHE B 2  827  ? 148.941 162.207 112.032 1.00 4.81   ? 827  PHE B CZ    1 
ATOM   17264 N  N     . TYR B 2  828  ? 142.769 165.294 113.914 1.00 1.77   ? 828  TYR B N     1 
ATOM   17265 C  CA    . TYR B 2  828  ? 141.678 166.256 113.811 1.00 9.94   ? 828  TYR B CA    1 
ATOM   17266 C  C     . TYR B 2  828  ? 140.574 165.917 114.793 1.00 12.88  ? 828  TYR B C     1 
ATOM   17267 O  O     . TYR B 2  828  ? 140.150 164.765 114.880 1.00 6.15   ? 828  TYR B O     1 
ATOM   17268 C  CB    . TYR B 2  828  ? 141.107 166.292 112.396 1.00 12.01  ? 828  TYR B CB    1 
ATOM   17269 C  CG    . TYR B 2  828  ? 142.033 166.870 111.370 1.00 0.51   ? 828  TYR B CG    1 
ATOM   17270 C  CD1   . TYR B 2  828  ? 142.210 168.232 111.263 1.00 3.36   ? 828  TYR B CD1   1 
ATOM   17271 C  CD2   . TYR B 2  828  ? 142.730 166.055 110.509 1.00 2.01   ? 828  TYR B CD2   1 
ATOM   17272 C  CE1   . TYR B 2  828  ? 143.051 168.756 110.337 1.00 2.50   ? 828  TYR B CE1   1 
ATOM   17273 C  CE2   . TYR B 2  828  ? 143.572 166.573 109.584 1.00 1.28   ? 828  TYR B CE2   1 
ATOM   17274 C  CZ    . TYR B 2  828  ? 143.728 167.921 109.500 1.00 3.44   ? 828  TYR B CZ    1 
ATOM   17275 O  OH    . TYR B 2  828  ? 144.571 168.439 108.563 1.00 12.76  ? 828  TYR B OH    1 
ATOM   17276 N  N     . ASN B 2  829  ? 140.099 166.928 115.510 1.00 10.12  ? 829  ASN B N     1 
ATOM   17277 C  CA    . ASN B 2  829  ? 139.026 166.784 116.480 1.00 4.94   ? 829  ASN B CA    1 
ATOM   17278 C  C     . ASN B 2  829  ? 138.079 167.957 116.333 1.00 5.74   ? 829  ASN B C     1 
ATOM   17279 O  O     . ASN B 2  829  ? 138.460 169.015 115.841 1.00 6.99   ? 829  ASN B O     1 
ATOM   17280 C  CB    . ASN B 2  829  ? 139.558 166.727 117.911 1.00 1.73   ? 829  ASN B CB    1 
ATOM   17281 C  CG    . ASN B 2  829  ? 140.272 165.444 118.216 1.00 7.90   ? 829  ASN B CG    1 
ATOM   17282 O  OD1   . ASN B 2  829  ? 139.722 164.361 118.086 1.00 9.40   ? 829  ASN B OD1   1 
ATOM   17283 N  ND2   . ASN B 2  829  ? 141.512 165.557 118.607 1.00 11.65  ? 829  ASN B ND2   1 
ATOM   17284 N  N     . GLU B 2  830  ? 136.844 167.769 116.769 1.00 13.13  ? 830  GLU B N     1 
ATOM   17285 C  CA    . GLU B 2  830  ? 135.822 168.793 116.620 1.00 6.80   ? 830  GLU B CA    1 
ATOM   17286 C  C     . GLU B 2  830  ? 135.024 168.954 117.897 1.00 0.36   ? 830  GLU B C     1 
ATOM   17287 O  O     . GLU B 2  830  ? 134.922 168.024 118.696 1.00 11.46  ? 830  GLU B O     1 
ATOM   17288 C  CB    . GLU B 2  830  ? 134.884 168.464 115.478 1.00 4.02   ? 830  GLU B CB    1 
ATOM   17289 C  CG    . GLU B 2  830  ? 135.486 168.723 114.139 1.00 0.65   ? 830  GLU B CG    1 
ATOM   17290 C  CD    . GLU B 2  830  ? 134.521 168.510 113.034 1.00 8.47   ? 830  GLU B CD    1 
ATOM   17291 O  OE1   . GLU B 2  830  ? 133.408 168.055 113.315 1.00 13.19  ? 830  GLU B OE1   1 
ATOM   17292 O  OE2   . GLU B 2  830  ? 134.871 168.777 111.876 1.00 14.86  ? 830  GLU B OE2   1 
ATOM   17293 N  N     . MET B 2  831  ? 134.487 170.146 118.094 1.00 1.95   ? 831  MET B N     1 
ATOM   17294 C  CA    . MET B 2  831  ? 133.446 170.337 119.086 1.00 6.35   ? 831  MET B CA    1 
ATOM   17295 C  C     . MET B 2  831  ? 132.117 169.829 118.536 1.00 9.63   ? 831  MET B C     1 
ATOM   17296 O  O     . MET B 2  831  ? 131.775 170.115 117.390 1.00 3.95   ? 831  MET B O     1 
ATOM   17297 C  CB    . MET B 2  831  ? 133.338 171.814 119.460 1.00 1.17   ? 831  MET B CB    1 
ATOM   17298 C  CG    . MET B 2  831  ? 132.182 172.176 120.368 1.00 12.90  ? 831  MET B CG    1 
ATOM   17299 S  SD    . MET B 2  831  ? 132.430 171.780 122.105 1.00 22.60  ? 831  MET B SD    1 
ATOM   17300 C  CE    . MET B 2  831  ? 133.979 172.594 122.451 1.00 2.92   ? 831  MET B CE    1 
ATOM   17301 N  N     . PRO B 2  832  ? 131.351 169.070 119.316 1.00 1.21   ? 832  PRO B N     1 
ATOM   17302 C  CA    . PRO B 2  832  ? 130.048 168.619 118.827 1.00 3.75   ? 832  PRO B CA    1 
ATOM   17303 C  C     . PRO B 2  832  ? 129.149 169.797 118.489 1.00 15.49  ? 832  PRO B C     1 
ATOM   17304 O  O     . PRO B 2  832  ? 129.244 170.868 119.082 1.00 7.71   ? 832  PRO B O     1 
ATOM   17305 C  CB    . PRO B 2  832  ? 129.497 167.809 119.998 1.00 9.00   ? 832  PRO B CB    1 
ATOM   17306 C  CG    . PRO B 2  832  ? 130.659 167.423 120.768 1.00 15.48  ? 832  PRO B CG    1 
ATOM   17307 C  CD    . PRO B 2  832  ? 131.649 168.508 120.640 1.00 2.62   ? 832  PRO B CD    1 
ATOM   17308 N  N     . LEU B 2  833  ? 128.302 169.609 117.480 1.00 0.12   ? 833  LEU B N     1 
ATOM   17309 C  CA    . LEU B 2  833  ? 127.311 170.627 117.158 1.00 14.37  ? 833  LEU B CA    1 
ATOM   17310 C  C     . LEU B 2  833  ? 126.293 170.776 118.274 1.00 7.85   ? 833  LEU B C     1 
ATOM   17311 O  O     . LEU B 2  833  ? 125.811 171.879 118.528 1.00 9.09   ? 833  LEU B O     1 
ATOM   17312 C  CB    . LEU B 2  833  ? 126.609 170.291 115.849 1.00 0.90   ? 833  LEU B CB    1 
ATOM   17313 C  CG    . LEU B 2  833  ? 127.154 170.847 114.547 1.00 0.49   ? 833  LEU B CG    1 
ATOM   17314 C  CD1   . LEU B 2  833  ? 126.402 170.199 113.443 1.00 2.92   ? 833  LEU B CD1   1 
ATOM   17315 C  CD2   . LEU B 2  833  ? 126.992 172.338 114.490 1.00 8.58   ? 833  LEU B CD2   1 
ATOM   17316 N  N     . VAL B 2  834  ? 125.947 169.676 118.929 1.00 1.16   ? 834  VAL B N     1 
ATOM   17317 C  CA    . VAL B 2  834  ? 125.147 169.679 120.143 1.00 8.32   ? 834  VAL B CA    1 
ATOM   17318 C  C     . VAL B 2  834  ? 126.057 169.258 121.286 1.00 4.40   ? 834  VAL B C     1 
ATOM   17319 O  O     . VAL B 2  834  ? 126.280 168.066 121.504 1.00 5.53   ? 834  VAL B O     1 
ATOM   17320 C  CB    . VAL B 2  834  ? 123.928 168.746 120.013 1.00 0.58   ? 834  VAL B CB    1 
ATOM   17321 C  CG1   . VAL B 2  834  ? 123.032 168.874 121.212 1.00 7.79   ? 834  VAL B CG1   1 
ATOM   17322 C  CG2   . VAL B 2  834  ? 123.154 169.051 118.760 1.00 14.51  ? 834  VAL B CG2   1 
ATOM   17323 N  N     . LYS B 2  835  ? 126.613 170.225 122.003 1.00 4.40   ? 835  LYS B N     1 
ATOM   17324 C  CA    . LYS B 2  835  ? 127.528 169.951 123.102 1.00 0.53   ? 835  LYS B CA    1 
ATOM   17325 C  C     . LYS B 2  835  ? 126.778 169.851 124.426 1.00 9.70   ? 835  LYS B C     1 
ATOM   17326 O  O     . LYS B 2  835  ? 125.595 170.161 124.520 1.00 19.03  ? 835  LYS B O     1 
ATOM   17327 C  CB    . LYS B 2  835  ? 128.597 171.034 123.187 1.00 3.22   ? 835  LYS B CB    1 
ATOM   17328 C  CG    . LYS B 2  835  ? 128.097 172.349 123.727 1.00 3.87   ? 835  LYS B CG    1 
ATOM   17329 C  CD    . LYS B 2  835  ? 129.224 173.314 123.938 1.00 5.48   ? 835  LYS B CD    1 
ATOM   17330 C  CE    . LYS B 2  835  ? 130.164 172.843 125.023 1.00 11.96  ? 835  LYS B CE    1 
ATOM   17331 N  NZ    . LYS B 2  835  ? 129.591 172.997 126.385 1.00 19.88  ? 835  LYS B NZ    1 
ATOM   17332 N  N     . THR B 2  836  ? 127.478 169.384 125.450 1.00 11.29  ? 836  THR B N     1 
ATOM   17333 C  CA    . THR B 2  836  ? 126.925 169.289 126.793 1.00 5.27   ? 836  THR B CA    1 
ATOM   17334 C  C     . THR B 2  836  ? 127.837 170.008 127.784 1.00 11.50  ? 836  THR B C     1 
ATOM   17335 O  O     . THR B 2  836  ? 128.851 170.597 127.422 1.00 12.23  ? 836  THR B O     1 
ATOM   17336 C  CB    . THR B 2  836  ? 126.712 167.831 127.208 1.00 3.51   ? 836  THR B CB    1 
ATOM   17337 O  OG1   . THR B 2  836  ? 127.974 167.211 127.448 1.00 11.03  ? 836  THR B OG1   1 
ATOM   17338 C  CG2   . THR B 2  836  ? 125.971 167.057 126.133 1.00 2.37   ? 836  THR B CG2   1 
ATOM   17339 N  N     . ILE B 2  837  ? 127.450 169.971 129.058 1.00 17.84  ? 837  ILE B N     1 
ATOM   17340 C  CA    . ILE B 2  837  ? 128.245 170.615 130.093 1.00 12.63  ? 837  ILE B CA    1 
ATOM   17341 C  C     . ILE B 2  837  ? 129.570 169.902 130.307 1.00 10.38  ? 837  ILE B C     1 
ATOM   17342 O  O     . ILE B 2  837  ? 130.520 170.509 130.801 1.00 15.51  ? 837  ILE B O     1 
ATOM   17343 C  CB    . ILE B 2  837  ? 127.448 170.708 131.408 1.00 10.86  ? 837  ILE B CB    1 
ATOM   17344 C  CG1   . ILE B 2  837  ? 128.100 171.716 132.350 1.00 14.60  ? 837  ILE B CG1   1 
ATOM   17345 C  CG2   . ILE B 2  837  ? 127.336 169.359 132.071 1.00 7.24   ? 837  ILE B CG2   1 
ATOM   17346 C  CD1   . ILE B 2  837  ? 127.307 172.031 133.585 1.00 16.98  ? 837  ILE B CD1   1 
ATOM   17347 N  N     . ALA B 2  838  ? 129.667 168.626 129.940 1.00 6.11   ? 838  ALA B N     1 
ATOM   17348 C  CA    . ALA B 2  838  ? 130.919 167.905 130.097 1.00 4.64   ? 838  ALA B CA    1 
ATOM   17349 C  C     . ALA B 2  838  ? 132.010 168.434 129.186 1.00 8.99   ? 838  ALA B C     1 
ATOM   17350 O  O     . ALA B 2  838  ? 133.186 168.188 129.445 1.00 20.78  ? 838  ALA B O     1 
ATOM   17351 C  CB    . ALA B 2  838  ? 130.714 166.417 129.838 1.00 3.22   ? 838  ALA B CB    1 
ATOM   17352 N  N     . HIS B 2  839  ? 131.658 169.141 128.125 1.00 13.04  ? 839  HIS B N     1 
ATOM   17353 C  CA    . HIS B 2  839  ? 132.646 169.705 127.224 1.00 9.13   ? 839  HIS B CA    1 
ATOM   17354 C  C     . HIS B 2  839  ? 133.141 171.060 127.686 1.00 12.25  ? 839  HIS B C     1 
ATOM   17355 O  O     . HIS B 2  839  ? 133.898 171.709 126.963 1.00 21.45  ? 839  HIS B O     1 
ATOM   17356 C  CB    . HIS B 2  839  ? 132.086 169.790 125.806 1.00 6.18   ? 839  HIS B CB    1 
ATOM   17357 C  CG    . HIS B 2  839  ? 131.867 168.453 125.180 1.00 10.04  ? 839  HIS B CG    1 
ATOM   17358 N  ND1   . HIS B 2  839  ? 130.617 167.966 124.877 1.00 6.03   ? 839  HIS B ND1   1 
ATOM   17359 C  CD2   . HIS B 2  839  ? 132.740 167.472 124.861 1.00 12.11  ? 839  HIS B CD2   1 
ATOM   17360 C  CE1   . HIS B 2  839  ? 130.732 166.757 124.361 1.00 12.43  ? 839  HIS B CE1   1 
ATOM   17361 N  NE2   . HIS B 2  839  ? 132.011 166.434 124.339 1.00 10.35  ? 839  HIS B NE2   1 
ATOM   17362 N  N     . ASN B 2  840  ? 132.710 171.504 128.861 1.00 13.41  ? 840  ASN B N     1 
ATOM   17363 C  CA    . ASN B 2  840  ? 133.342 172.612 129.551 1.00 13.80  ? 840  ASN B CA    1 
ATOM   17364 C  C     . ASN B 2  840  ? 134.569 172.178 130.336 1.00 15.54  ? 840  ASN B C     1 
ATOM   17365 O  O     . ASN B 2  840  ? 135.297 173.040 130.830 1.00 24.84  ? 840  ASN B O     1 
ATOM   17366 C  CB    . ASN B 2  840  ? 132.354 173.269 130.513 1.00 14.77  ? 840  ASN B CB    1 
ATOM   17367 C  CG    . ASN B 2  840  ? 131.177 173.893 129.812 1.00 20.41  ? 840  ASN B CG    1 
ATOM   17368 O  OD1   . ASN B 2  840  ? 131.319 174.530 128.778 1.00 30.93  ? 840  ASN B OD1   1 
ATOM   17369 N  ND2   . ASN B 2  840  ? 129.999 173.720 130.384 1.00 15.29  ? 840  ASN B ND2   1 
ATOM   17370 N  N     . TYR B 2  841  ? 134.809 170.875 130.468 1.00 13.02  ? 841  TYR B N     1 
ATOM   17371 C  CA    . TYR B 2  841  ? 135.864 170.360 131.329 1.00 11.05  ? 841  TYR B CA    1 
ATOM   17372 C  C     . TYR B 2  841  ? 136.785 169.347 130.676 1.00 14.26  ? 841  TYR B C     1 
ATOM   17373 O  O     . TYR B 2  841  ? 137.882 169.133 131.196 1.00 23.86  ? 841  TYR B O     1 
ATOM   17374 C  CB    . TYR B 2  841  ? 135.264 169.732 132.597 1.00 14.56  ? 841  TYR B CB    1 
ATOM   17375 C  CG    . TYR B 2  841  ? 134.278 170.637 133.289 1.00 15.16  ? 841  TYR B CG    1 
ATOM   17376 C  CD1   . TYR B 2  841  ? 134.700 171.797 133.913 1.00 14.98  ? 841  TYR B CD1   1 
ATOM   17377 C  CD2   . TYR B 2  841  ? 132.930 170.342 133.305 1.00 18.40  ? 841  TYR B CD2   1 
ATOM   17378 C  CE1   . TYR B 2  841  ? 133.813 172.634 134.521 1.00 15.84  ? 841  TYR B CE1   1 
ATOM   17379 C  CE2   . TYR B 2  841  ? 132.035 171.178 133.918 1.00 18.33  ? 841  TYR B CE2   1 
ATOM   17380 C  CZ    . TYR B 2  841  ? 132.484 172.322 134.521 1.00 15.14  ? 841  TYR B CZ    1 
ATOM   17381 O  OH    . TYR B 2  841  ? 131.597 173.161 135.139 1.00 23.97  ? 841  TYR B OH    1 
ATOM   17382 N  N     . VAL B 2  842  ? 136.401 168.719 129.574 1.00 14.14  ? 842  VAL B N     1 
ATOM   17383 C  CA    . VAL B 2  842  ? 137.296 167.823 128.857 1.00 10.41  ? 842  VAL B CA    1 
ATOM   17384 C  C     . VAL B 2  842  ? 137.347 168.252 127.402 1.00 15.41  ? 842  VAL B C     1 
ATOM   17385 O  O     . VAL B 2  842  ? 136.466 168.959 126.907 1.00 19.53  ? 842  VAL B O     1 
ATOM   17386 C  CB    . VAL B 2  842  ? 136.888 166.337 128.971 1.00 13.37  ? 842  VAL B CB    1 
ATOM   17387 C  CG1   . VAL B 2  842  ? 137.374 165.759 130.271 1.00 19.26  ? 842  VAL B CG1   1 
ATOM   17388 C  CG2   . VAL B 2  842  ? 135.402 166.179 128.867 1.00 12.98  ? 842  VAL B CG2   1 
ATOM   17389 N  N     . ILE B 2  843  ? 138.414 167.850 126.732 1.00 20.81  ? 843  ILE B N     1 
ATOM   17390 C  CA    . ILE B 2  843  ? 138.555 168.087 125.297 1.00 13.17  ? 843  ILE B CA    1 
ATOM   17391 C  C     . ILE B 2  843  ? 137.695 167.077 124.548 1.00 11.62  ? 843  ILE B C     1 
ATOM   17392 O  O     . ILE B 2  843  ? 137.780 165.876 124.834 1.00 17.48  ? 843  ILE B O     1 
ATOM   17393 C  CB    . ILE B 2  843  ? 140.014 167.982 124.880 1.00 15.26  ? 843  ILE B CB    1 
ATOM   17394 C  CG1   . ILE B 2  843  ? 140.733 169.274 125.212 1.00 15.11  ? 843  ILE B CG1   1 
ATOM   17395 C  CG2   . ILE B 2  843  ? 140.131 167.711 123.390 1.00 18.46  ? 843  ILE B CG2   1 
ATOM   17396 C  CD1   . ILE B 2  843  ? 140.642 170.245 124.102 1.00 17.99  ? 843  ILE B CD1   1 
ATOM   17397 N  N     . PRO B 2  844  ? 136.844 167.517 123.625 1.00 8.24   ? 844  PRO B N     1 
ATOM   17398 C  CA    . PRO B 2  844  ? 136.100 166.563 122.803 1.00 6.83   ? 844  PRO B CA    1 
ATOM   17399 C  C     . PRO B 2  844  ? 137.014 165.846 121.829 1.00 7.49   ? 844  PRO B C     1 
ATOM   17400 O  O     . PRO B 2  844  ? 137.927 166.437 121.254 1.00 15.98  ? 844  PRO B O     1 
ATOM   17401 C  CB    . PRO B 2  844  ? 135.087 167.445 122.072 1.00 4.54   ? 844  PRO B CB    1 
ATOM   17402 C  CG    . PRO B 2  844  ? 135.660 168.781 122.108 1.00 7.61   ? 844  PRO B CG    1 
ATOM   17403 C  CD    . PRO B 2  844  ? 136.454 168.903 123.344 1.00 13.11  ? 844  PRO B CD    1 
ATOM   17404 N  N     . ASN B 2  845  ? 136.748 164.564 121.620 1.00 3.39   ? 845  ASN B N     1 
ATOM   17405 C  CA    . ASN B 2  845  ? 137.516 163.773 120.665 1.00 1.17   ? 845  ASN B CA    1 
ATOM   17406 C  C     . ASN B 2  845  ? 136.556 162.994 119.772 1.00 1.85   ? 845  ASN B C     1 
ATOM   17407 O  O     . ASN B 2  845  ? 135.938 162.016 120.190 1.00 10.07  ? 845  ASN B O     1 
ATOM   17408 C  CB    . ASN B 2  845  ? 138.509 162.880 121.388 1.00 9.71   ? 845  ASN B CB    1 
ATOM   17409 C  CG    . ASN B 2  845  ? 137.856 161.937 122.345 1.00 11.07  ? 845  ASN B CG    1 
ATOM   17410 O  OD1   . ASN B 2  845  ? 137.695 162.230 123.523 1.00 13.16  ? 845  ASN B OD1   1 
ATOM   17411 N  ND2   . ASN B 2  845  ? 137.461 160.795 121.843 1.00 12.46  ? 845  ASN B ND2   1 
ATOM   17412 N  N     . GLY B 2  846  ? 136.415 163.462 118.541 1.00 1.67   ? 846  GLY B N     1 
ATOM   17413 C  CA    . GLY B 2  846  ? 135.480 162.887 117.596 1.00 2.34   ? 846  GLY B CA    1 
ATOM   17414 C  C     . GLY B 2  846  ? 135.278 163.862 116.466 1.00 14.24  ? 846  GLY B C     1 
ATOM   17415 O  O     . GLY B 2  846  ? 135.956 164.884 116.377 1.00 6.26   ? 846  GLY B O     1 
ATOM   17416 N  N     . LEU B 2  847  ? 134.323 163.544 115.602 1.00 3.90   ? 847  LEU B N     1 
ATOM   17417 C  CA    . LEU B 2  847  ? 134.028 164.370 114.443 1.00 1.99   ? 847  LEU B CA    1 
ATOM   17418 C  C     . LEU B 2  847  ? 132.529 164.444 114.226 1.00 8.98   ? 847  LEU B C     1 
ATOM   17419 O  O     . LEU B 2  847  ? 131.790 163.536 114.594 1.00 2.14   ? 847  LEU B O     1 
ATOM   17420 C  CB    . LEU B 2  847  ? 134.690 163.829 113.176 1.00 8.23   ? 847  LEU B CB    1 
ATOM   17421 C  CG    . LEU B 2  847  ? 136.205 163.898 113.066 1.00 2.47   ? 847  LEU B CG    1 
ATOM   17422 C  CD1   . LEU B 2  847  ? 136.628 163.118 111.866 1.00 8.85   ? 847  LEU B CD1   1 
ATOM   17423 C  CD2   . LEU B 2  847  ? 136.689 165.330 112.980 1.00 2.40   ? 847  LEU B CD2   1 
ATOM   17424 N  N     . ASN B 2  848  ? 132.095 165.532 113.594 1.00 3.07   ? 848  ASN B N     1 
ATOM   17425 C  CA    . ASN B 2  848  ? 130.684 165.754 113.277 1.00 8.17   ? 848  ASN B CA    1 
ATOM   17426 C  C     . ASN B 2  848  ? 130.351 165.153 111.913 1.00 0.40   ? 848  ASN B C     1 
ATOM   17427 O  O     . ASN B 2  848  ? 130.124 165.845 110.926 1.00 15.91  ? 848  ASN B O     1 
ATOM   17428 C  CB    . ASN B 2  848  ? 130.363 167.240 113.307 1.00 5.68   ? 848  ASN B CB    1 
ATOM   17429 C  CG    . ASN B 2  848  ? 130.092 167.748 114.683 1.00 5.37   ? 848  ASN B CG    1 
ATOM   17430 O  OD1   . ASN B 2  848  ? 129.151 167.323 115.331 1.00 5.50   ? 848  ASN B OD1   1 
ATOM   17431 N  ND2   . ASN B 2  848  ? 130.899 168.682 115.132 1.00 4.73   ? 848  ASN B ND2   1 
ATOM   17432 N  N     . THR B 2  849  ? 130.300 163.831 111.882 1.00 8.17   ? 849  THR B N     1 
ATOM   17433 C  CA    . THR B 2  849  ? 130.072 163.111 110.637 1.00 13.00  ? 849  THR B CA    1 
ATOM   17434 C  C     . THR B 2  849  ? 128.651 163.315 110.132 1.00 12.75  ? 849  THR B C     1 
ATOM   17435 O  O     . THR B 2  849  ? 127.709 163.405 110.915 1.00 19.79  ? 849  THR B O     1 
ATOM   17436 C  CB    . THR B 2  849  ? 130.339 161.626 110.847 1.00 13.50  ? 849  THR B CB    1 
ATOM   17437 O  OG1   . THR B 2  849  ? 129.514 161.150 111.910 1.00 16.48  ? 849  THR B OG1   1 
ATOM   17438 C  CG2   . THR B 2  849  ? 131.769 161.398 111.231 1.00 16.48  ? 849  THR B CG2   1 
ATOM   17439 N  N     . ILE B 2  850  ? 128.495 163.394 108.814 1.00 1.78   ? 850  ILE B N     1 
ATOM   17440 C  CA    . ILE B 2  850  ? 127.172 163.372 108.198 1.00 14.93  ? 850  ILE B CA    1 
ATOM   17441 C  C     . ILE B 2  850  ? 126.752 161.914 108.067 1.00 8.84   ? 850  ILE B C     1 
ATOM   17442 O  O     . ILE B 2  850  ? 127.479 161.102 107.499 1.00 10.85  ? 850  ILE B O     1 
ATOM   17443 C  CB    . ILE B 2  850  ? 127.159 164.074 106.837 1.00 0.97   ? 850  ILE B CB    1 
ATOM   17444 C  CG1   . ILE B 2  850  ? 127.683 165.500 106.947 1.00 0.75   ? 850  ILE B CG1   1 
ATOM   17445 C  CG2   . ILE B 2  850  ? 125.767 164.079 106.268 1.00 5.23   ? 850  ILE B CG2   1 
ATOM   17446 C  CD1   . ILE B 2  850  ? 126.860 166.412 107.779 1.00 14.47  ? 850  ILE B CD1   1 
ATOM   17447 N  N     . VAL B 2  851  ? 125.585 161.578 108.598 1.00 0.78   ? 851  VAL B N     1 
ATOM   17448 C  CA    . VAL B 2  851  ? 125.084 160.210 108.623 1.00 1.40   ? 851  VAL B CA    1 
ATOM   17449 C  C     . VAL B 2  851  ? 123.761 160.157 107.877 1.00 11.18  ? 851  VAL B C     1 
ATOM   17450 O  O     . VAL B 2  851  ? 122.887 160.999 108.087 1.00 1.47   ? 851  VAL B O     1 
ATOM   17451 C  CB    . VAL B 2  851  ? 124.923 159.695 110.063 1.00 9.68   ? 851  VAL B CB    1 
ATOM   17452 C  CG1   . VAL B 2  851  ? 124.370 158.307 110.063 1.00 4.66   ? 851  VAL B CG1   1 
ATOM   17453 C  CG2   . VAL B 2  851  ? 126.234 159.724 110.790 1.00 3.25   ? 851  VAL B CG2   1 
ATOM   17454 N  N     . ALA B 2  852  ? 123.626 159.182 106.993 1.00 8.68   ? 852  ALA B N     1 
ATOM   17455 C  CA    . ALA B 2  852  ? 122.359 158.841 106.370 1.00 5.89   ? 852  ALA B CA    1 
ATOM   17456 C  C     . ALA B 2  852  ? 121.833 157.572 107.018 1.00 5.65   ? 852  ALA B C     1 
ATOM   17457 O  O     . ALA B 2  852  ? 122.571 156.604 107.172 1.00 10.55  ? 852  ALA B O     1 
ATOM   17458 C  CB    . ALA B 2  852  ? 122.524 158.654 104.865 1.00 8.69   ? 852  ALA B CB    1 
ATOM   17459 N  N     . TYR B 2  853  ? 120.571 157.588 107.416 1.00 3.37   ? 853  TYR B N     1 
ATOM   17460 C  CA    . TYR B 2  853  ? 119.928 156.451 108.073 1.00 11.06  ? 853  TYR B CA    1 
ATOM   17461 C  C     . TYR B 2  853  ? 119.073 155.726 107.047 1.00 9.50   ? 853  TYR B C     1 
ATOM   17462 O  O     . TYR B 2  853  ? 117.919 156.087 106.831 1.00 10.45  ? 853  TYR B O     1 
ATOM   17463 C  CB    . TYR B 2  853  ? 119.088 156.915 109.255 1.00 4.85   ? 853  TYR B CB    1 
ATOM   17464 C  CG    . TYR B 2  853  ? 119.873 157.572 110.353 1.00 14.10  ? 853  TYR B CG    1 
ATOM   17465 C  CD1   . TYR B 2  853  ? 120.242 158.898 110.275 1.00 14.24  ? 853  TYR B CD1   1 
ATOM   17466 C  CD2   . TYR B 2  853  ? 120.239 156.864 111.470 1.00 1.91   ? 853  TYR B CD2   1 
ATOM   17467 C  CE1   . TYR B 2  853  ? 120.961 159.486 111.261 1.00 1.45   ? 853  TYR B CE1   1 
ATOM   17468 C  CE2   . TYR B 2  853  ? 120.951 157.447 112.468 1.00 0.54   ? 853  TYR B CE2   1 
ATOM   17469 C  CZ    . TYR B 2  853  ? 121.307 158.756 112.364 1.00 4.84   ? 853  TYR B CZ    1 
ATOM   17470 O  OH    . TYR B 2  853  ? 122.021 159.336 113.375 1.00 8.14   ? 853  TYR B OH    1 
ATOM   17471 N  N     . MET B 2  854  ? 119.634 154.700 106.417 1.00 5.16   ? 854  MET B N     1 
ATOM   17472 C  CA    . MET B 2  854  ? 118.996 154.112 105.253 1.00 15.34  ? 854  MET B CA    1 
ATOM   17473 C  C     . MET B 2  854  ? 119.527 152.711 105.006 1.00 12.34  ? 854  MET B C     1 
ATOM   17474 O  O     . MET B 2  854  ? 120.470 152.264 105.652 1.00 3.00   ? 854  MET B O     1 
ATOM   17475 C  CB    . MET B 2  854  ? 119.212 154.997 104.027 1.00 3.10   ? 854  MET B CB    1 
ATOM   17476 C  CG    . MET B 2  854  ? 120.624 155.005 103.506 1.00 3.54   ? 854  MET B CG    1 
ATOM   17477 S  SD    . MET B 2  854  ? 120.915 156.241 102.259 1.00 11.14  ? 854  MET B SD    1 
ATOM   17478 C  CE    . MET B 2  854  ? 120.184 155.441 100.866 1.00 9.49   ? 854  MET B CE    1 
ATOM   17479 N  N     . ILE B 2  855  ? 118.893 152.023 104.071 1.00 12.87  ? 855  ILE B N     1 
ATOM   17480 C  CA    . ILE B 2  855  ? 119.347 150.724 103.594 1.00 14.32  ? 855  ILE B CA    1 
ATOM   17481 C  C     . ILE B 2  855  ? 120.063 150.940 102.269 1.00 13.95  ? 855  ILE B C     1 
ATOM   17482 O  O     . ILE B 2  855  ? 119.490 151.506 101.334 1.00 20.24  ? 855  ILE B O     1 
ATOM   17483 C  CB    . ILE B 2  855  ? 118.170 149.752 103.427 1.00 16.19  ? 855  ILE B CB    1 
ATOM   17484 C  CG1   . ILE B 2  855  ? 117.509 149.463 104.772 1.00 12.48  ? 855  ILE B CG1   1 
ATOM   17485 C  CG2   . ILE B 2  855  ? 118.622 148.481 102.760 1.00 15.55  ? 855  ILE B CG2   1 
ATOM   17486 C  CD1   . ILE B 2  855  ? 116.292 148.598 104.679 1.00 11.74  ? 855  ILE B CD1   1 
ATOM   17487 N  N     . TYR B 2  856  ? 121.309 150.486 102.174 1.00 1.93   ? 856  TYR B N     1 
ATOM   17488 C  CA    . TYR B 2  856  ? 122.075 150.631 100.935 1.00 2.06   ? 856  TYR B CA    1 
ATOM   17489 C  C     . TYR B 2  856  ? 122.779 149.313 100.619 1.00 4.64   ? 856  TYR B C     1 
ATOM   17490 O  O     . TYR B 2  856  ? 123.960 149.143 100.915 1.00 8.90   ? 856  TYR B O     1 
ATOM   17491 C  CB    . TYR B 2  856  ? 123.055 151.788 101.064 1.00 0.13   ? 856  TYR B CB    1 
ATOM   17492 C  CG    . TYR B 2  856  ? 123.457 152.447 99.767  1.00 4.82   ? 856  TYR B CG    1 
ATOM   17493 C  CD1   . TYR B 2  856  ? 122.522 153.070 98.970  1.00 2.13   ? 856  TYR B CD1   1 
ATOM   17494 C  CD2   . TYR B 2  856  ? 124.779 152.487 99.369  1.00 6.34   ? 856  TYR B CD2   1 
ATOM   17495 C  CE1   . TYR B 2  856  ? 122.884 153.686 97.801  1.00 2.29   ? 856  TYR B CE1   1 
ATOM   17496 C  CE2   . TYR B 2  856  ? 125.150 153.104 98.201  1.00 4.10   ? 856  TYR B CE2   1 
ATOM   17497 C  CZ    . TYR B 2  856  ? 124.201 153.703 97.421  1.00 3.27   ? 856  TYR B CZ    1 
ATOM   17498 O  OH    . TYR B 2  856  ? 124.570 154.312 96.257  1.00 4.31   ? 856  TYR B OH    1 
ATOM   17499 N  N     . GLY B 2  857  ? 122.060 148.389 99.994  1.00 1.67   ? 857  GLY B N     1 
ATOM   17500 C  CA    . GLY B 2  857  ? 122.656 147.166 99.507  1.00 4.22   ? 857  GLY B CA    1 
ATOM   17501 C  C     . GLY B 2  857  ? 122.917 146.093 100.534 1.00 10.92  ? 857  GLY B C     1 
ATOM   17502 O  O     . GLY B 2  857  ? 123.437 145.037 100.173 1.00 5.81   ? 857  GLY B O     1 
ATOM   17503 N  N     . GLY B 2  858  ? 122.591 146.321 101.796 1.00 0.01   ? 858  GLY B N     1 
ATOM   17504 C  CA    . GLY B 2  858  ? 122.729 145.311 102.816 1.00 6.52   ? 858  GLY B CA    1 
ATOM   17505 C  C     . GLY B 2  858  ? 124.084 145.190 103.466 1.00 1.00   ? 858  GLY B C     1 
ATOM   17506 O  O     . GLY B 2  858  ? 124.344 144.173 104.107 1.00 8.85   ? 858  GLY B O     1 
ATOM   17507 N  N     . TYR B 2  859  ? 124.952 146.183 103.340 1.00 11.25  ? 859  TYR B N     1 
ATOM   17508 C  CA    . TYR B 2  859  ? 126.275 146.106 103.939 1.00 4.78   ? 859  TYR B CA    1 
ATOM   17509 C  C     . TYR B 2  859  ? 126.374 146.754 105.312 1.00 4.59   ? 859  TYR B C     1 
ATOM   17510 O  O     . TYR B 2  859  ? 127.443 146.702 105.917 1.00 3.00   ? 859  TYR B O     1 
ATOM   17511 C  CB    . TYR B 2  859  ? 127.307 146.743 103.015 1.00 0.68   ? 859  TYR B CB    1 
ATOM   17512 C  CG    . TYR B 2  859  ? 127.612 145.930 101.796 1.00 15.18  ? 859  TYR B CG    1 
ATOM   17513 C  CD1   . TYR B 2  859  ? 128.619 144.983 101.812 1.00 4.47   ? 859  TYR B CD1   1 
ATOM   17514 C  CD2   . TYR B 2  859  ? 126.895 146.099 100.632 1.00 6.64   ? 859  TYR B CD2   1 
ATOM   17515 C  CE1   . TYR B 2  859  ? 128.904 144.237 100.706 1.00 5.93   ? 859  TYR B CE1   1 
ATOM   17516 C  CE2   . TYR B 2  859  ? 127.172 145.350 99.522  1.00 3.50   ? 859  TYR B CE2   1 
ATOM   17517 C  CZ    . TYR B 2  859  ? 128.174 144.422 99.568  1.00 3.05   ? 859  TYR B CZ    1 
ATOM   17518 O  OH    . TYR B 2  859  ? 128.453 143.673 98.460  1.00 9.13   ? 859  TYR B OH    1 
ATOM   17519 N  N     . ASN B 2  860  ? 125.313 147.370 105.819 1.00 5.11   ? 860  ASN B N     1 
ATOM   17520 C  CA    . ASN B 2  860  ? 125.331 147.940 107.155 1.00 4.88   ? 860  ASN B CA    1 
ATOM   17521 C  C     . ASN B 2  860  ? 124.458 147.152 108.118 1.00 2.84   ? 860  ASN B C     1 
ATOM   17522 O  O     . ASN B 2  860  ? 124.124 147.650 109.190 1.00 5.33   ? 860  ASN B O     1 
ATOM   17523 C  CB    . ASN B 2  860  ? 124.919 149.416 107.129 1.00 1.10   ? 860  ASN B CB    1 
ATOM   17524 C  CG    . ASN B 2  860  ? 123.762 149.691 106.214 1.00 7.68   ? 860  ASN B CG    1 
ATOM   17525 O  OD1   . ASN B 2  860  ? 123.293 148.819 105.496 1.00 2.94   ? 860  ASN B OD1   1 
ATOM   17526 N  ND2   . ASN B 2  860  ? 123.284 150.908 106.242 1.00 0.53   ? 860  ASN B ND2   1 
ATOM   17527 N  N     . GLN B 2  861  ? 124.129 145.919 107.779 1.00 4.86   ? 861  GLN B N     1 
ATOM   17528 C  CA    . GLN B 2  861  ? 123.247 145.115 108.604 1.00 5.82   ? 861  GLN B CA    1 
ATOM   17529 C  C     . GLN B 2  861  ? 123.948 144.631 109.861 1.00 5.85   ? 861  GLN B C     1 
ATOM   17530 O  O     . GLN B 2  861  ? 125.120 144.266 109.835 1.00 0.64   ? 861  GLN B O     1 
ATOM   17531 C  CB    . GLN B 2  861  ? 122.750 143.921 107.811 1.00 13.29  ? 861  GLN B CB    1 
ATOM   17532 C  CG    . GLN B 2  861  ? 121.368 144.055 107.297 1.00 10.20  ? 861  GLN B CG    1 
ATOM   17533 C  CD    . GLN B 2  861  ? 121.126 143.124 106.163 1.00 6.34   ? 861  GLN B CD    1 
ATOM   17534 O  OE1   . GLN B 2  861  ? 121.897 143.088 105.218 1.00 0.08   ? 861  GLN B OE1   1 
ATOM   17535 N  NE2   . GLN B 2  861  ? 120.070 142.337 106.253 1.00 2.40   ? 861  GLN B NE2   1 
ATOM   17536 N  N     . GLU B 2  862  ? 123.204 144.615 110.962 1.00 8.45   ? 862  GLU B N     1 
ATOM   17537 C  CA    . GLU B 2  862  ? 123.618 144.051 112.243 1.00 4.66   ? 862  GLU B CA    1 
ATOM   17538 C  C     . GLU B 2  862  ? 124.874 144.730 112.789 1.00 1.50   ? 862  GLU B C     1 
ATOM   17539 O  O     . GLU B 2  862  ? 125.901 144.104 113.025 1.00 17.53  ? 862  GLU B O     1 
ATOM   17540 C  CB    . GLU B 2  862  ? 123.822 142.544 112.134 1.00 3.63   ? 862  GLU B CB    1 
ATOM   17541 C  CG    . GLU B 2  862  ? 122.818 141.778 112.933 1.00 10.93  ? 862  GLU B CG    1 
ATOM   17542 C  CD    . GLU B 2  862  ? 122.758 140.350 112.528 1.00 16.84  ? 862  GLU B CD    1 
ATOM   17543 O  OE1   . GLU B 2  862  ? 123.594 139.960 111.696 1.00 20.15  ? 862  GLU B OE1   1 
ATOM   17544 O  OE2   . GLU B 2  862  ? 121.883 139.618 113.035 1.00 16.02  ? 862  GLU B OE2   1 
ATOM   17545 N  N     . ASP B 2  863  ? 124.730 146.032 113.023 1.00 0.79   ? 863  ASP B N     1 
ATOM   17546 C  CA    . ASP B 2  863  ? 125.745 146.860 113.663 1.00 0.85   ? 863  ASP B CA    1 
ATOM   17547 C  C     . ASP B 2  863  ? 126.974 147.058 112.785 1.00 1.80   ? 863  ASP B C     1 
ATOM   17548 O  O     . ASP B 2  863  ? 128.095 147.051 113.276 1.00 14.50  ? 863  ASP B O     1 
ATOM   17549 C  CB    . ASP B 2  863  ? 126.160 146.289 115.022 1.00 10.76  ? 863  ASP B CB    1 
ATOM   17550 C  CG    . ASP B 2  863  ? 125.000 146.159 115.981 1.00 24.65  ? 863  ASP B CG    1 
ATOM   17551 O  OD1   . ASP B 2  863  ? 123.970 146.830 115.769 1.00 25.62  ? 863  ASP B OD1   1 
ATOM   17552 O  OD2   . ASP B 2  863  ? 125.115 145.376 116.948 1.00 24.19  ? 863  ASP B OD2   1 
ATOM   17553 N  N     . SER B 2  864  ? 126.790 147.232 111.489 1.00 1.75   ? 864  SER B N     1 
ATOM   17554 C  CA    . SER B 2  864  ? 127.868 147.602 110.592 1.00 14.00  ? 864  SER B CA    1 
ATOM   17555 C  C     . SER B 2  864  ? 127.559 148.954 109.973 1.00 4.19   ? 864  SER B C     1 
ATOM   17556 O  O     . SER B 2  864  ? 126.418 149.416 109.988 1.00 10.41  ? 864  SER B O     1 
ATOM   17557 C  CB    . SER B 2  864  ? 128.061 146.561 109.498 1.00 0.31   ? 864  SER B CB    1 
ATOM   17558 O  OG    . SER B 2  864  ? 127.748 145.280 109.967 1.00 10.03  ? 864  SER B OG    1 
ATOM   17559 N  N     . VAL B 2  865  ? 128.589 149.604 109.449 1.00 7.14   ? 865  VAL B N     1 
ATOM   17560 C  CA    . VAL B 2  865  ? 128.412 150.870 108.756 1.00 10.82  ? 865  VAL B CA    1 
ATOM   17561 C  C     . VAL B 2  865  ? 129.135 150.817 107.423 1.00 11.04  ? 865  VAL B C     1 
ATOM   17562 O  O     . VAL B 2  865  ? 130.074 150.044 107.227 1.00 1.13   ? 865  VAL B O     1 
ATOM   17563 C  CB    . VAL B 2  865  ? 128.895 152.087 109.584 1.00 10.84  ? 865  VAL B CB    1 
ATOM   17564 C  CG1   . VAL B 2  865  ? 128.069 152.249 110.820 1.00 0.05   ? 865  VAL B CG1   1 
ATOM   17565 C  CG2   . VAL B 2  865  ? 130.338 151.945 109.949 1.00 0.35   ? 865  VAL B CG2   1 
ATOM   17566 N  N     . ILE B 2  866  ? 128.671 151.640 106.499 1.00 4.69   ? 866  ILE B N     1 
ATOM   17567 C  CA    . ILE B 2  866  ? 129.363 151.908 105.252 1.00 10.57  ? 866  ILE B CA    1 
ATOM   17568 C  C     . ILE B 2  866  ? 130.039 153.261 105.390 1.00 3.88   ? 866  ILE B C     1 
ATOM   17569 O  O     . ILE B 2  866  ? 129.395 154.245 105.759 1.00 1.23   ? 866  ILE B O     1 
ATOM   17570 C  CB    . ILE B 2  866  ? 128.394 151.882 104.060 1.00 2.67   ? 866  ILE B CB    1 
ATOM   17571 C  CG1   . ILE B 2  866  ? 127.662 150.544 104.010 1.00 10.01  ? 866  ILE B CG1   1 
ATOM   17572 C  CG2   . ILE B 2  866  ? 129.132 152.147 102.773 1.00 15.08  ? 866  ILE B CG2   1 
ATOM   17573 C  CD1   . ILE B 2  866  ? 126.427 150.547 103.180 1.00 9.32   ? 866  ILE B CD1   1 
ATOM   17574 N  N     . VAL B 2  867  ? 131.336 153.305 105.125 1.00 0.58   ? 867  VAL B N     1 
ATOM   17575 C  CA    . VAL B 2  867  ? 132.133 154.516 105.239 1.00 13.88  ? 867  VAL B CA    1 
ATOM   17576 C  C     . VAL B 2  867  ? 132.417 155.050 103.847 1.00 13.84  ? 867  VAL B C     1 
ATOM   17577 O  O     . VAL B 2  867  ? 132.467 154.306 102.871 1.00 15.70  ? 867  VAL B O     1 
ATOM   17578 C  CB    . VAL B 2  867  ? 133.449 154.263 106.006 1.00 14.82  ? 867  VAL B CB    1 
ATOM   17579 C  CG1   . VAL B 2  867  ? 134.036 155.564 106.503 1.00 7.62   ? 867  VAL B CG1   1 
ATOM   17580 C  CG2   . VAL B 2  867  ? 133.217 153.338 107.163 1.00 2.37   ? 867  VAL B CG2   1 
ATOM   17581 N  N     . SER B 2  868  ? 132.579 156.360 103.762 1.00 14.14  ? 868  SER B N     1 
ATOM   17582 C  CA    . SER B 2  868  ? 133.067 157.001 102.552 1.00 8.57   ? 868  SER B CA    1 
ATOM   17583 C  C     . SER B 2  868  ? 134.577 156.820 102.476 1.00 6.77   ? 868  SER B C     1 
ATOM   17584 O  O     . SER B 2  868  ? 135.282 157.098 103.443 1.00 13.45  ? 868  SER B O     1 
ATOM   17585 C  CB    . SER B 2  868  ? 132.688 158.476 102.568 1.00 12.08  ? 868  SER B CB    1 
ATOM   17586 O  OG    . SER B 2  868  ? 132.988 159.098 101.344 1.00 21.44  ? 868  SER B OG    1 
ATOM   17587 N  N     . GLN B 2  869  ? 135.073 156.332 101.341 1.00 11.47  ? 869  GLN B N     1 
ATOM   17588 C  CA    . GLN B 2  869  ? 136.513 156.210 101.167 1.00 10.97  ? 869  GLN B CA    1 
ATOM   17589 C  C     . GLN B 2  869  ? 137.185 157.570 101.078 1.00 2.95   ? 869  GLN B C     1 
ATOM   17590 O  O     . GLN B 2  869  ? 138.312 157.732 101.538 1.00 5.22   ? 869  GLN B O     1 
ATOM   17591 C  CB    . GLN B 2  869  ? 136.827 155.375 99.928  1.00 1.09   ? 869  GLN B CB    1 
ATOM   17592 C  CG    . GLN B 2  869  ? 138.295 155.131 99.699  1.00 3.32   ? 869  GLN B CG    1 
ATOM   17593 C  CD    . GLN B 2  869  ? 138.938 154.290 100.767 1.00 3.58   ? 869  GLN B CD    1 
ATOM   17594 O  OE1   . GLN B 2  869  ? 138.528 153.168 101.012 1.00 11.27  ? 869  GLN B OE1   1 
ATOM   17595 N  NE2   . GLN B 2  869  ? 139.945 154.831 101.417 1.00 2.54   ? 869  GLN B NE2   1 
ATOM   17596 N  N     . SER B 2  870  ? 136.517 158.554 100.487 1.00 4.03   ? 870  SER B N     1 
ATOM   17597 C  CA    . SER B 2  870  ? 137.056 159.906 100.445 1.00 13.75  ? 870  SER B CA    1 
ATOM   17598 C  C     . SER B 2  870  ? 137.217 160.490 101.838 1.00 14.52  ? 870  SER B C     1 
ATOM   17599 O  O     . SER B 2  870  ? 138.215 161.148 102.123 1.00 4.03   ? 870  SER B O     1 
ATOM   17600 C  CB    . SER B 2  870  ? 136.153 160.787 99.607  1.00 1.82   ? 870  SER B CB    1 
ATOM   17601 O  OG    . SER B 2  870  ? 136.067 160.287 98.302  1.00 11.30  ? 870  SER B OG    1 
ATOM   17602 N  N     . PHE B 2  871  ? 136.236 160.276 102.708 1.00 1.44   ? 871  PHE B N     1 
ATOM   17603 C  CA    . PHE B 2  871  ? 136.340 160.704 104.095 1.00 5.31   ? 871  PHE B CA    1 
ATOM   17604 C  C     . PHE B 2  871  ? 137.565 160.099 104.770 1.00 10.77  ? 871  PHE B C     1 
ATOM   17605 O  O     . PHE B 2  871  ? 138.246 160.769 105.548 1.00 1.71   ? 871  PHE B O     1 
ATOM   17606 C  CB    . PHE B 2  871  ? 135.048 160.326 104.825 1.00 8.14   ? 871  PHE B CB    1 
ATOM   17607 C  CG    . PHE B 2  871  ? 135.079 160.554 106.303 1.00 12.98  ? 871  PHE B CG    1 
ATOM   17608 C  CD1   . PHE B 2  871  ? 134.943 161.815 106.826 1.00 12.77  ? 871  PHE B CD1   1 
ATOM   17609 C  CD2   . PHE B 2  871  ? 135.227 159.497 107.167 1.00 14.18  ? 871  PHE B CD2   1 
ATOM   17610 C  CE1   . PHE B 2  871  ? 134.967 162.015 108.161 1.00 8.18   ? 871  PHE B CE1   1 
ATOM   17611 C  CE2   . PHE B 2  871  ? 135.258 159.696 108.500 1.00 8.04   ? 871  PHE B CE2   1 
ATOM   17612 C  CZ    . PHE B 2  871  ? 135.125 160.955 109.003 1.00 15.05  ? 871  PHE B CZ    1 
ATOM   17613 N  N     . ILE B 2  872  ? 137.862 158.833 104.476 1.00 5.68   ? 872  ILE B N     1 
ATOM   17614 C  CA    . ILE B 2  872  ? 139.048 158.174 105.010 1.00 6.11   ? 872  ILE B CA    1 
ATOM   17615 C  C     . ILE B 2  872  ? 140.320 158.786 104.439 1.00 0.02   ? 872  ILE B C     1 
ATOM   17616 O  O     . ILE B 2  872  ? 141.284 159.027 105.170 1.00 11.64  ? 872  ILE B O     1 
ATOM   17617 C  CB    . ILE B 2  872  ? 138.984 156.664 104.730 1.00 15.89  ? 872  ILE B CB    1 
ATOM   17618 C  CG1   . ILE B 2  872  ? 137.853 156.017 105.515 1.00 4.95   ? 872  ILE B CG1   1 
ATOM   17619 C  CG2   . ILE B 2  872  ? 140.303 156.002 105.058 1.00 15.85  ? 872  ILE B CG2   1 
ATOM   17620 C  CD1   . ILE B 2  872  ? 137.462 154.664 104.986 1.00 2.76   ? 872  ILE B CD1   1 
ATOM   17621 N  N     . ASP B 2  873  ? 140.353 159.030 103.128 1.00 1.11   ? 873  ASP B N     1 
ATOM   17622 C  CA    . ASP B 2  873  ? 141.553 159.570 102.500 1.00 2.42   ? 873  ASP B CA    1 
ATOM   17623 C  C     . ASP B 2  873  ? 141.891 160.954 103.019 1.00 8.35   ? 873  ASP B C     1 
ATOM   17624 O  O     . ASP B 2  873  ? 143.064 161.324 103.069 1.00 12.33  ? 873  ASP B O     1 
ATOM   17625 C  CB    . ASP B 2  873  ? 141.394 159.641 100.985 1.00 13.05  ? 873  ASP B CB    1 
ATOM   17626 C  CG    . ASP B 2  873  ? 141.272 158.296 100.345 1.00 5.01   ? 873  ASP B CG    1 
ATOM   17627 O  OD1   . ASP B 2  873  ? 141.713 157.303 100.941 1.00 11.17  ? 873  ASP B OD1   1 
ATOM   17628 O  OD2   . ASP B 2  873  ? 140.735 158.227 99.230  1.00 3.93   ? 873  ASP B OD2   1 
ATOM   17629 N  N     . ARG B 2  874  ? 140.889 161.735 103.389 1.00 0.22   ? 874  ARG B N     1 
ATOM   17630 C  CA    . ARG B 2  874  ? 141.085 163.105 103.826 1.00 3.27   ? 874  ARG B CA    1 
ATOM   17631 C  C     . ARG B 2  874  ? 141.511 163.212 105.278 1.00 3.10   ? 874  ARG B C     1 
ATOM   17632 O  O     . ARG B 2  874  ? 141.766 164.319 105.751 1.00 11.12  ? 874  ARG B O     1 
ATOM   17633 C  CB    . ARG B 2  874  ? 139.809 163.904 103.603 1.00 8.48   ? 874  ARG B CB    1 
ATOM   17634 C  CG    . ARG B 2  874  ? 139.448 164.049 102.168 1.00 15.50  ? 874  ARG B CG    1 
ATOM   17635 C  CD    . ARG B 2  874  ? 138.223 164.870 101.978 1.00 2.34   ? 874  ARG B CD    1 
ATOM   17636 N  NE    . ARG B 2  874  ? 137.811 164.878 100.584 1.00 11.17  ? 874  ARG B NE    1 
ATOM   17637 C  CZ    . ARG B 2  874  ? 136.672 164.384 100.132 1.00 0.89   ? 874  ARG B CZ    1 
ATOM   17638 N  NH1   . ARG B 2  874  ? 135.779 163.857 100.941 1.00 15.67  ? 874  ARG B NH1   1 
ATOM   17639 N  NH2   . ARG B 2  874  ? 136.426 164.420 98.833  1.00 11.33  ? 874  ARG B NH2   1 
ATOM   17640 N  N     . GLY B 2  875  ? 141.609 162.104 105.991 1.00 8.77   ? 875  GLY B N     1 
ATOM   17641 C  CA    . GLY B 2  875  ? 142.096 162.116 107.344 1.00 12.16  ? 875  GLY B CA    1 
ATOM   17642 C  C     . GLY B 2  875  ? 141.044 162.019 108.408 1.00 11.78  ? 875  GLY B C     1 
ATOM   17643 O  O     . GLY B 2  875  ? 141.341 162.322 109.563 1.00 21.58  ? 875  GLY B O     1 
ATOM   17644 N  N     . GLY B 2  876  ? 139.822 161.630 108.061 1.00 1.68   ? 876  GLY B N     1 
ATOM   17645 C  CA    . GLY B 2  876  ? 138.797 161.426 109.055 1.00 3.88   ? 876  GLY B CA    1 
ATOM   17646 C  C     . GLY B 2  876  ? 139.134 160.247 109.933 1.00 2.09   ? 876  GLY B C     1 
ATOM   17647 O  O     . GLY B 2  876  ? 139.204 159.107 109.449 1.00 3.34   ? 876  GLY B O     1 
ATOM   17648 N  N     . PHE B 2  877  ? 139.345 160.499 111.227 1.00 4.47   ? 877  PHE B N     1 
ATOM   17649 C  CA    . PHE B 2  877  ? 139.719 159.497 112.225 1.00 0.74   ? 877  PHE B CA    1 
ATOM   17650 C  C     . PHE B 2  877  ? 141.096 158.892 111.966 1.00 14.91  ? 877  PHE B C     1 
ATOM   17651 O  O     . PHE B 2  877  ? 141.378 157.772 112.378 1.00 4.33   ? 877  PHE B O     1 
ATOM   17652 C  CB    . PHE B 2  877  ? 138.658 158.399 112.340 1.00 8.45   ? 877  PHE B CB    1 
ATOM   17653 C  CG    . PHE B 2  877  ? 137.326 158.894 112.813 1.00 3.75   ? 877  PHE B CG    1 
ATOM   17654 C  CD1   . PHE B 2  877  ? 137.226 159.628 113.968 1.00 12.93  ? 877  PHE B CD1   1 
ATOM   17655 C  CD2   . PHE B 2  877  ? 136.179 158.628 112.108 1.00 1.82   ? 877  PHE B CD2   1 
ATOM   17656 C  CE1   . PHE B 2  877  ? 136.025 160.087 114.402 1.00 3.20   ? 877  PHE B CE1   1 
ATOM   17657 C  CE2   . PHE B 2  877  ? 134.975 159.087 112.551 1.00 0.41   ? 877  PHE B CE2   1 
ATOM   17658 C  CZ    . PHE B 2  877  ? 134.903 159.813 113.698 1.00 7.59   ? 877  PHE B CZ    1 
ATOM   17659 N  N     . ALA B 2  878  ? 141.975 159.635 111.312 1.00 1.48   ? 878  ALA B N     1 
ATOM   17660 C  CA    . ALA B 2  878  ? 143.335 159.198 111.040 1.00 7.47   ? 878  ALA B CA    1 
ATOM   17661 C  C     . ALA B 2  878  ? 144.276 159.723 112.114 1.00 5.78   ? 878  ALA B C     1 
ATOM   17662 O  O     . ALA B 2  878  ? 144.012 160.748 112.741 1.00 11.10  ? 878  ALA B O     1 
ATOM   17663 C  CB    . ALA B 2  878  ? 143.800 159.672 109.666 1.00 3.92   ? 878  ALA B CB    1 
ATOM   17664 N  N     . GLY B 2  879  ? 145.359 159.010 112.333 1.00 8.76   ? 879  GLY B N     1 
ATOM   17665 C  CA    . GLY B 2  879  ? 146.315 159.415 113.328 1.00 8.91   ? 879  GLY B CA    1 
ATOM   17666 C  C     . GLY B 2  879  ? 147.547 158.559 113.299 1.00 12.62  ? 879  GLY B C     1 
ATOM   17667 O  O     . GLY B 2  879  ? 147.803 157.839 112.337 1.00 15.88  ? 879  GLY B O     1 
ATOM   17668 N  N     . THR B 2  880  ? 148.326 158.646 114.368 1.00 10.66  ? 880  THR B N     1 
ATOM   17669 C  CA    . THR B 2  880  ? 149.570 157.902 114.463 1.00 11.85  ? 880  THR B CA    1 
ATOM   17670 C  C     . THR B 2  880  ? 149.573 157.039 115.714 1.00 8.56   ? 880  THR B C     1 
ATOM   17671 O  O     . THR B 2  880  ? 149.141 157.467 116.784 1.00 13.40  ? 880  THR B O     1 
ATOM   17672 C  CB    . THR B 2  880  ? 150.783 158.839 114.447 1.00 19.52  ? 880  THR B CB    1 
ATOM   17673 O  OG1   . THR B 2  880  ? 151.982 158.076 114.606 1.00 25.70  ? 880  THR B OG1   1 
ATOM   17674 C  CG2   . THR B 2  880  ? 150.687 159.862 115.548 1.00 20.00  ? 880  THR B CG2   1 
ATOM   17675 N  N     . PHE B 2  881  ? 150.053 155.815 115.555 1.00 14.84  ? 881  PHE B N     1 
ATOM   17676 C  CA    . PHE B 2  881  ? 150.090 154.804 116.598 1.00 17.71  ? 881  PHE B CA    1 
ATOM   17677 C  C     . PHE B 2  881  ? 151.538 154.557 116.997 1.00 21.53  ? 881  PHE B C     1 
ATOM   17678 O  O     . PHE B 2  881  ? 152.436 154.604 116.156 1.00 17.07  ? 881  PHE B O     1 
ATOM   17679 C  CB    . PHE B 2  881  ? 149.437 153.518 116.091 1.00 15.93  ? 881  PHE B CB    1 
ATOM   17680 C  CG    . PHE B 2  881  ? 149.217 152.478 117.134 1.00 20.11  ? 881  PHE B CG    1 
ATOM   17681 C  CD1   . PHE B 2  881  ? 148.171 152.573 118.025 1.00 22.01  ? 881  PHE B CD1   1 
ATOM   17682 C  CD2   . PHE B 2  881  ? 150.041 151.373 117.195 1.00 20.50  ? 881  PHE B CD2   1 
ATOM   17683 C  CE1   . PHE B 2  881  ? 147.968 151.595 118.976 1.00 18.83  ? 881  PHE B CE1   1 
ATOM   17684 C  CE2   . PHE B 2  881  ? 149.842 150.395 118.139 1.00 17.79  ? 881  PHE B CE2   1 
ATOM   17685 C  CZ    . PHE B 2  881  ? 148.803 150.504 119.027 1.00 18.29  ? 881  PHE B CZ    1 
ATOM   17686 N  N     . TYR B 2  882  ? 151.766 154.294 118.278 1.00 24.63  ? 882  TYR B N     1 
ATOM   17687 C  CA    . TYR B 2  882  ? 153.116 154.231 118.824 1.00 21.15  ? 882  TYR B CA    1 
ATOM   17688 C  C     . TYR B 2  882  ? 153.361 152.922 119.553 1.00 25.44  ? 882  TYR B C     1 
ATOM   17689 O  O     . TYR B 2  882  ? 152.469 152.401 120.227 1.00 25.41  ? 882  TYR B O     1 
ATOM   17690 C  CB    . TYR B 2  882  ? 153.367 155.401 119.770 1.00 18.93  ? 882  TYR B CB    1 
ATOM   17691 C  CG    . TYR B 2  882  ? 153.501 156.710 119.051 1.00 21.78  ? 882  TYR B CG    1 
ATOM   17692 C  CD1   . TYR B 2  882  ? 154.584 156.956 118.229 1.00 20.65  ? 882  TYR B CD1   1 
ATOM   17693 C  CD2   . TYR B 2  882  ? 152.537 157.691 119.175 1.00 21.77  ? 882  TYR B CD2   1 
ATOM   17694 C  CE1   . TYR B 2  882  ? 154.711 158.135 117.566 1.00 19.02  ? 882  TYR B CE1   1 
ATOM   17695 C  CE2   . TYR B 2  882  ? 152.658 158.883 118.513 1.00 22.11  ? 882  TYR B CE2   1 
ATOM   17696 C  CZ    . TYR B 2  882  ? 153.748 159.099 117.709 1.00 23.15  ? 882  TYR B CZ    1 
ATOM   17697 O  OH    . TYR B 2  882  ? 153.880 160.290 117.041 1.00 28.96  ? 882  TYR B OH    1 
ATOM   17698 N  N     . ARG B 2  883  ? 154.578 152.402 119.415 1.00 28.20  ? 883  ARG B N     1 
ATOM   17699 C  CA    . ARG B 2  883  ? 155.068 151.285 120.207 1.00 29.33  ? 883  ARG B CA    1 
ATOM   17700 C  C     . ARG B 2  883  ? 156.481 151.586 120.683 1.00 30.82  ? 883  ARG B C     1 
ATOM   17701 O  O     . ARG B 2  883  ? 157.285 152.168 119.954 1.00 27.71  ? 883  ARG B O     1 
ATOM   17702 C  CB    . ARG B 2  883  ? 155.053 149.982 119.419 1.00 28.85  ? 883  ARG B CB    1 
ATOM   17703 C  CG    . ARG B 2  883  ? 153.750 149.250 119.520 1.00 24.53  ? 883  ARG B CG    1 
ATOM   17704 C  CD    . ARG B 2  883  ? 153.645 148.166 118.492 1.00 28.14  ? 883  ARG B CD    1 
ATOM   17705 N  NE    . ARG B 2  883  ? 152.480 147.330 118.736 1.00 30.11  ? 883  ARG B NE    1 
ATOM   17706 C  CZ    . ARG B 2  883  ? 151.797 146.709 117.786 1.00 30.31  ? 883  ARG B CZ    1 
ATOM   17707 N  NH1   . ARG B 2  883  ? 152.148 146.795 116.515 1.00 27.16  ? 883  ARG B NH1   1 
ATOM   17708 N  NH2   . ARG B 2  883  ? 150.724 145.999 118.119 1.00 29.81  ? 883  ARG B NH2   1 
ATOM   17709 N  N     . GLU B 2  884  ? 156.777 151.175 121.912 1.00 39.12  ? 884  GLU B N     1 
ATOM   17710 C  CA    . GLU B 2  884  ? 158.056 151.438 122.554 1.00 39.25  ? 884  GLU B CA    1 
ATOM   17711 C  C     . GLU B 2  884  ? 158.864 150.156 122.677 1.00 39.94  ? 884  GLU B C     1 
ATOM   17712 O  O     . GLU B 2  884  ? 158.348 149.052 122.489 1.00 38.46  ? 884  GLU B O     1 
ATOM   17713 C  CB    . GLU B 2  884  ? 157.871 152.046 123.948 1.00 38.80  ? 884  GLU B CB    1 
ATOM   17714 C  CG    . GLU B 2  884  ? 157.386 151.062 124.997 1.00 38.29  ? 884  GLU B CG    1 
ATOM   17715 C  CD    . GLU B 2  884  ? 158.018 151.295 126.363 1.00 44.45  ? 884  GLU B CD    1 
ATOM   17716 O  OE1   . GLU B 2  884  ? 157.466 152.087 127.157 1.00 43.28  ? 884  GLU B OE1   1 
ATOM   17717 O  OE2   . GLU B 2  884  ? 159.066 150.678 126.645 1.00 44.64  ? 884  GLU B OE2   1 
ATOM   17718 N  N     . GLU B 2  885  ? 160.147 150.319 122.996 1.00 44.40  ? 885  GLU B N     1 
ATOM   17719 C  CA    . GLU B 2  885  ? 161.001 149.200 123.369 1.00 44.39  ? 885  GLU B CA    1 
ATOM   17720 C  C     . GLU B 2  885  ? 161.984 149.597 124.456 1.00 43.60  ? 885  GLU B C     1 
ATOM   17721 O  O     . GLU B 2  885  ? 162.300 150.776 124.631 1.00 41.39  ? 885  GLU B O     1 
ATOM   17722 C  CB    . GLU B 2  885  ? 161.778 148.648 122.190 1.00 39.53  ? 885  GLU B CB    1 
ATOM   17723 C  CG    . GLU B 2  885  ? 160.991 147.657 121.414 1.00 41.64  ? 885  GLU B CG    1 
ATOM   17724 C  CD    . GLU B 2  885  ? 161.768 147.125 120.271 1.00 46.37  ? 885  GLU B CD    1 
ATOM   17725 O  OE1   . GLU B 2  885  ? 162.777 147.765 119.917 1.00 46.74  ? 885  GLU B OE1   1 
ATOM   17726 O  OE2   . GLU B 2  885  ? 161.376 146.072 119.733 1.00 46.48  ? 885  GLU B OE2   1 
ATOM   17727 N  N     . LYS B 2  886  ? 162.467 148.585 125.175 1.00 42.41  ? 886  LYS B N     1 
ATOM   17728 C  CA    . LYS B 2  886  ? 163.408 148.757 126.279 1.00 41.14  ? 886  LYS B CA    1 
ATOM   17729 C  C     . LYS B 2  886  ? 164.240 147.482 126.361 1.00 39.43  ? 886  LYS B C     1 
ATOM   17730 O  O     . LYS B 2  886  ? 163.752 146.450 126.830 1.00 41.52  ? 886  LYS B O     1 
ATOM   17731 C  CB    . LYS B 2  886  ? 162.675 149.032 127.586 1.00 40.61  ? 886  LYS B CB    1 
ATOM   17732 C  CG    . LYS B 2  886  ? 163.475 149.805 128.605 1.00 41.00  ? 886  LYS B CG    1 
ATOM   17733 C  CD    . LYS B 2  886  ? 164.036 148.876 129.668 1.00 40.50  ? 886  LYS B CD    1 
ATOM   17734 C  CE    . LYS B 2  886  ? 163.109 148.790 130.867 1.00 41.49  ? 886  LYS B CE    1 
ATOM   17735 N  NZ    . LYS B 2  886  ? 163.761 148.156 132.043 1.00 40.48  ? 886  LYS B NZ    1 
ATOM   17736 N  N     . VAL B 2  887  ? 165.485 147.551 125.896 1.00 43.07  ? 887  VAL B N     1 
ATOM   17737 C  CA    . VAL B 2  887  ? 166.431 146.444 125.980 1.00 44.83  ? 887  VAL B CA    1 
ATOM   17738 C  C     . VAL B 2  887  ? 167.588 146.873 126.870 1.00 44.65  ? 887  VAL B C     1 
ATOM   17739 O  O     . VAL B 2  887  ? 168.180 147.937 126.656 1.00 44.60  ? 887  VAL B O     1 
ATOM   17740 C  CB    . VAL B 2  887  ? 166.939 146.015 124.592 1.00 44.15  ? 887  VAL B CB    1 
ATOM   17741 C  CG1   . VAL B 2  887  ? 167.996 144.941 124.731 1.00 41.29  ? 887  VAL B CG1   1 
ATOM   17742 C  CG2   . VAL B 2  887  ? 165.788 145.513 123.741 1.00 43.49  ? 887  VAL B CG2   1 
ATOM   17743 N  N     . GLU B 2  888  ? 167.909 146.049 127.861 1.00 46.57  ? 888  GLU B N     1 
ATOM   17744 C  CA    . GLU B 2  888  ? 168.888 146.369 128.888 1.00 48.17  ? 888  GLU B CA    1 
ATOM   17745 C  C     . GLU B 2  888  ? 170.215 145.670 128.603 1.00 47.52  ? 888  GLU B C     1 
ATOM   17746 O  O     . GLU B 2  888  ? 170.308 144.759 127.776 1.00 46.91  ? 888  GLU B O     1 
ATOM   17747 C  CB    . GLU B 2  888  ? 168.342 145.989 130.265 1.00 48.34  ? 888  GLU B CB    1 
ATOM   17748 C  CG    . GLU B 2  888  ? 167.154 146.837 130.697 1.00 47.94  ? 888  GLU B CG    1 
ATOM   17749 C  CD    . GLU B 2  888  ? 166.559 146.392 132.014 1.00 50.25  ? 888  GLU B CD    1 
ATOM   17750 O  OE1   . GLU B 2  888  ? 167.007 145.361 132.554 1.00 50.86  ? 888  GLU B OE1   1 
ATOM   17751 O  OE2   . GLU B 2  888  ? 165.638 147.072 132.511 1.00 50.47  ? 888  GLU B OE2   1 
ATOM   17752 N  N     . LEU B 2  889  ? 171.256 146.109 129.307 1.00 49.25  ? 889  LEU B N     1 
ATOM   17753 C  CA    . LEU B 2  889  ? 172.587 145.540 129.172 1.00 51.26  ? 889  LEU B CA    1 
ATOM   17754 C  C     . LEU B 2  889  ? 173.088 145.023 130.512 1.00 51.92  ? 889  LEU B C     1 
ATOM   17755 O  O     . LEU B 2  889  ? 172.638 145.438 131.582 1.00 52.08  ? 889  LEU B O     1 
ATOM   17756 C  CB    . LEU B 2  889  ? 173.589 146.556 128.608 1.00 48.77  ? 889  LEU B CB    1 
ATOM   17757 C  CG    . LEU B 2  889  ? 173.558 146.789 127.098 1.00 49.60  ? 889  LEU B CG    1 
ATOM   17758 C  CD1   . LEU B 2  889  ? 174.678 147.734 126.689 1.00 48.13  ? 889  LEU B CD1   1 
ATOM   17759 C  CD2   . LEU B 2  889  ? 173.656 145.471 126.353 1.00 48.67  ? 889  LEU B CD2   1 
ATOM   17760 N  N     . GLU B 2  890  ? 174.031 144.095 130.425 1.00 55.15  ? 890  GLU B N     1 
ATOM   17761 C  CA    . GLU B 2  890  ? 174.731 143.538 131.569 1.00 55.06  ? 890  GLU B CA    1 
ATOM   17762 C  C     . GLU B 2  890  ? 176.094 144.200 131.704 1.00 56.21  ? 890  GLU B C     1 
ATOM   17763 O  O     . GLU B 2  890  ? 176.697 144.639 130.722 1.00 54.00  ? 890  GLU B O     1 
ATOM   17764 C  CB    . GLU B 2  890  ? 174.893 142.023 131.419 1.00 52.63  ? 890  GLU B CB    1 
ATOM   17765 C  CG    . GLU B 2  890  ? 173.603 141.245 131.581 1.00 53.71  ? 890  GLU B CG    1 
ATOM   17766 C  CD    . GLU B 2  890  ? 173.827 139.752 131.636 1.00 56.77  ? 890  GLU B CD    1 
ATOM   17767 O  OE1   . GLU B 2  890  ? 174.997 139.321 131.551 1.00 55.80  ? 890  GLU B OE1   1 
ATOM   17768 O  OE2   . GLU B 2  890  ? 172.831 139.008 131.765 1.00 56.72  ? 890  GLU B OE2   1 
ATOM   17769 N  N     . SER B 2  891  ? 176.576 144.269 132.939 1.00 48.97  ? 891  SER B N     1 
ATOM   17770 C  CA    . SER B 2  891  ? 177.843 144.936 133.225 1.00 46.52  ? 891  SER B CA    1 
ATOM   17771 C  C     . SER B 2  891  ? 178.986 144.103 132.659 1.00 46.99  ? 891  SER B C     1 
ATOM   17772 O  O     . SER B 2  891  ? 179.287 143.016 133.156 1.00 46.27  ? 891  SER B O     1 
ATOM   17773 C  CB    . SER B 2  891  ? 178.002 145.160 134.725 1.00 45.99  ? 891  SER B CB    1 
ATOM   17774 O  OG    . SER B 2  891  ? 177.097 146.148 135.186 1.00 45.85  ? 891  SER B OG    1 
ATOM   17775 N  N     . ASP B 2  892  ? 179.607 144.609 131.594 1.00 48.72  ? 892  ASP B N     1 
ATOM   17776 C  CA    . ASP B 2  892  ? 180.810 144.067 130.968 1.00 47.96  ? 892  ASP B CA    1 
ATOM   17777 C  C     . ASP B 2  892  ? 180.583 142.760 130.218 1.00 48.16  ? 892  ASP B C     1 
ATOM   17778 O  O     . ASP B 2  892  ? 181.509 142.273 129.564 1.00 47.47  ? 892  ASP B O     1 
ATOM   17779 C  CB    . ASP B 2  892  ? 181.933 143.863 131.993 1.00 46.42  ? 892  ASP B CB    1 
ATOM   17780 C  CG    . ASP B 2  892  ? 183.313 143.993 131.384 1.00 48.02  ? 892  ASP B CG    1 
ATOM   17781 O  OD1   . ASP B 2  892  ? 183.407 144.333 130.188 1.00 47.23  ? 892  ASP B OD1   1 
ATOM   17782 O  OD2   . ASP B 2  892  ? 184.300 143.744 132.104 1.00 45.20  ? 892  ASP B OD2   1 
ATOM   17783 N  N     . ILE B 2  893  ? 179.387 142.182 130.271 1.00 48.20  ? 893  ILE B N     1 
ATOM   17784 C  CA    . ILE B 2  893  ? 179.093 140.956 129.539 1.00 46.56  ? 893  ILE B CA    1 
ATOM   17785 C  C     . ILE B 2  893  ? 178.521 141.253 128.160 1.00 51.28  ? 893  ILE B C     1 
ATOM   17786 O  O     . ILE B 2  893  ? 179.018 140.745 127.155 1.00 49.34  ? 893  ILE B O     1 
ATOM   17787 C  CB    . ILE B 2  893  ? 178.131 140.055 130.341 1.00 47.79  ? 893  ILE B CB    1 
ATOM   17788 C  CG1   . ILE B 2  893  ? 178.699 139.736 131.725 1.00 49.56  ? 893  ILE B CG1   1 
ATOM   17789 C  CG2   . ILE B 2  893  ? 177.835 138.780 129.566 1.00 46.59  ? 893  ILE B CG2   1 
ATOM   17790 C  CD1   . ILE B 2  893  ? 177.847 140.251 132.870 1.00 47.40  ? 893  ILE B CD1   1 
ATOM   17791 N  N     . GLU B 2  894  ? 177.488 142.089 128.105 1.00 56.35  ? 894  GLU B N     1 
ATOM   17792 C  CA    . GLU B 2  894  ? 176.782 142.417 126.878 1.00 53.21  ? 894  GLU B CA    1 
ATOM   17793 C  C     . GLU B 2  894  ? 177.113 143.845 126.473 1.00 54.58  ? 894  GLU B C     1 
ATOM   17794 O  O     . GLU B 2  894  ? 177.561 144.650 127.294 1.00 55.59  ? 894  GLU B O     1 
ATOM   17795 C  CB    . GLU B 2  894  ? 175.274 142.271 127.061 1.00 53.42  ? 894  GLU B CB    1 
ATOM   17796 C  CG    . GLU B 2  894  ? 174.815 140.874 127.421 1.00 54.29  ? 894  GLU B CG    1 
ATOM   17797 C  CD    . GLU B 2  894  ? 173.435 140.864 128.044 1.00 56.74  ? 894  GLU B CD    1 
ATOM   17798 O  OE1   . GLU B 2  894  ? 172.973 141.941 128.480 1.00 55.70  ? 894  GLU B OE1   1 
ATOM   17799 O  OE2   . GLU B 2  894  ? 172.806 139.784 128.088 1.00 55.50  ? 894  GLU B OE2   1 
ATOM   17800 N  N     . SER B 2  895  ? 176.890 144.155 125.199 1.00 47.70  ? 895  SER B N     1 
ATOM   17801 C  CA    . SER B 2  895  ? 177.138 145.498 124.700 1.00 47.17  ? 895  SER B CA    1 
ATOM   17802 C  C     . SER B 2  895  ? 176.302 145.732 123.451 1.00 49.52  ? 895  SER B C     1 
ATOM   17803 O  O     . SER B 2  895  ? 175.832 144.790 122.808 1.00 49.92  ? 895  SER B O     1 
ATOM   17804 C  CB    . SER B 2  895  ? 178.626 145.722 124.402 1.00 46.91  ? 895  SER B CB    1 
ATOM   17805 O  OG    . SER B 2  895  ? 179.060 144.915 123.319 1.00 46.58  ? 895  SER B OG    1 
ATOM   17806 N  N     . PHE B 2  896  ? 176.114 147.006 123.119 1.00 46.92  ? 896  PHE B N     1 
ATOM   17807 C  CA    . PHE B 2  896  ? 175.414 147.366 121.896 1.00 46.69  ? 896  PHE B CA    1 
ATOM   17808 C  C     . PHE B 2  896  ? 176.399 147.543 120.750 1.00 43.63  ? 896  PHE B C     1 
ATOM   17809 O  O     . PHE B 2  896  ? 177.418 148.222 120.885 1.00 44.79  ? 896  PHE B O     1 
ATOM   17810 C  CB    . PHE B 2  896  ? 174.598 148.646 122.086 1.00 42.26  ? 896  PHE B CB    1 
ATOM   17811 C  CG    . PHE B 2  896  ? 173.451 148.496 123.036 1.00 40.68  ? 896  PHE B CG    1 
ATOM   17812 C  CD1   . PHE B 2  896  ? 172.609 147.403 122.950 1.00 43.08  ? 896  PHE B CD1   1 
ATOM   17813 C  CD2   . PHE B 2  896  ? 173.197 149.459 123.992 1.00 42.57  ? 896  PHE B CD2   1 
ATOM   17814 C  CE1   . PHE B 2  896  ? 171.550 147.258 123.816 1.00 44.10  ? 896  PHE B CE1   1 
ATOM   17815 C  CE2   . PHE B 2  896  ? 172.134 149.324 124.861 1.00 45.66  ? 896  PHE B CE2   1 
ATOM   17816 C  CZ    . PHE B 2  896  ? 171.309 148.220 124.771 1.00 44.26  ? 896  PHE B CZ    1 
ATOM   17817 N  N     . GLY B 2  897  ? 176.079 146.930 119.617 1.00 40.67  ? 897  GLY B N     1 
ATOM   17818 C  CA    . GLY B 2  897  ? 176.932 146.981 118.449 1.00 38.97  ? 897  GLY B CA    1 
ATOM   17819 C  C     . GLY B 2  897  ? 176.511 145.982 117.394 1.00 40.99  ? 897  GLY B C     1 
ATOM   17820 O  O     . GLY B 2  897  ? 175.867 144.976 117.705 1.00 41.04  ? 897  GLY B O     1 
ATOM   17821 N  N     . LYS B 2  898  ? 176.871 146.245 116.144 1.00 39.59  ? 898  LYS B N     1 
ATOM   17822 C  CA    . LYS B 2  898  ? 176.460 145.393 115.038 1.00 39.62  ? 898  LYS B CA    1 
ATOM   17823 C  C     . LYS B 2  898  ? 177.199 144.064 115.106 1.00 38.96  ? 898  LYS B C     1 
ATOM   17824 O  O     . LYS B 2  898  ? 178.432 144.034 115.017 1.00 41.67  ? 898  LYS B O     1 
ATOM   17825 C  CB    . LYS B 2  898  ? 176.721 146.094 113.703 1.00 41.72  ? 898  LYS B CB    1 
ATOM   17826 C  CG    . LYS B 2  898  ? 175.970 145.496 112.530 1.00 42.09  ? 898  LYS B CG    1 
ATOM   17827 C  CD    . LYS B 2  898  ? 176.780 145.575 111.252 1.00 39.61  ? 898  LYS B CD    1 
ATOM   17828 C  CE    . LYS B 2  898  ? 176.368 144.482 110.287 1.00 40.57  ? 898  LYS B CE    1 
ATOM   17829 N  NZ    . LYS B 2  898  ? 176.045 143.212 110.997 1.00 40.07  ? 898  LYS B NZ    1 
ATOM   17830 N  N     . PRO B 2  899  ? 176.488 142.952 115.250 1.00 41.40  ? 899  PRO B N     1 
ATOM   17831 C  CA    . PRO B 2  899  ? 177.159 141.659 115.408 1.00 42.39  ? 899  PRO B CA    1 
ATOM   17832 C  C     . PRO B 2  899  ? 177.929 141.250 114.161 1.00 45.12  ? 899  PRO B C     1 
ATOM   17833 O  O     . PRO B 2  899  ? 177.561 141.564 113.027 1.00 43.51  ? 899  PRO B O     1 
ATOM   17834 C  CB    . PRO B 2  899  ? 176.005 140.687 115.687 1.00 39.91  ? 899  PRO B CB    1 
ATOM   17835 C  CG    . PRO B 2  899  ? 174.860 141.545 116.096 1.00 43.81  ? 899  PRO B CG    1 
ATOM   17836 C  CD    . PRO B 2  899  ? 175.028 142.828 115.349 1.00 43.63  ? 899  PRO B CD    1 
ATOM   17837 N  N     . ASP B 2  900  ? 179.019 140.523 114.397 1.00 50.46  ? 900  ASP B N     1 
ATOM   17838 C  CA    . ASP B 2  900  ? 179.854 139.965 113.350 1.00 50.01  ? 900  ASP B CA    1 
ATOM   17839 C  C     . ASP B 2  900  ? 179.589 138.474 113.245 1.00 50.62  ? 900  ASP B C     1 
ATOM   17840 O  O     . ASP B 2  900  ? 179.867 137.741 114.202 1.00 47.31  ? 900  ASP B O     1 
ATOM   17841 C  CB    . ASP B 2  900  ? 181.332 140.211 113.656 1.00 49.95  ? 900  ASP B CB    1 
ATOM   17842 C  CG    . ASP B 2  900  ? 181.727 141.660 113.484 1.00 51.74  ? 900  ASP B CG    1 
ATOM   17843 O  OD1   . ASP B 2  900  ? 181.012 142.394 112.770 1.00 52.37  ? 900  ASP B OD1   1 
ATOM   17844 O  OD2   . ASP B 2  900  ? 182.754 142.069 114.062 1.00 49.42  ? 900  ASP B OD2   1 
ATOM   17845 N  N     . PRO B 2  901  ? 179.058 137.988 112.117 1.00 48.73  ? 901  PRO B N     1 
ATOM   17846 C  CA    . PRO B 2  901  ? 178.591 136.593 112.061 1.00 49.24  ? 901  PRO B CA    1 
ATOM   17847 C  C     . PRO B 2  901  ? 179.680 135.568 112.297 1.00 47.02  ? 901  PRO B C     1 
ATOM   17848 O  O     . PRO B 2  901  ? 179.369 134.460 112.753 1.00 48.89  ? 901  PRO B O     1 
ATOM   17849 C  CB    . PRO B 2  901  ? 178.019 136.466 110.638 1.00 48.42  ? 901  PRO B CB    1 
ATOM   17850 C  CG    . PRO B 2  901  ? 177.818 137.872 110.169 1.00 46.70  ? 901  PRO B CG    1 
ATOM   17851 C  CD    . PRO B 2  901  ? 178.882 138.680 110.832 1.00 45.17  ? 901  PRO B CD    1 
ATOM   17852 N  N     . LEU B 2  902  ? 180.936 135.899 112.015 1.00 44.34  ? 902  LEU B N     1 
ATOM   17853 C  CA    . LEU B 2  902  ? 182.009 134.918 112.079 1.00 46.09  ? 902  LEU B CA    1 
ATOM   17854 C  C     . LEU B 2  902  ? 182.438 134.615 113.510 1.00 46.96  ? 902  LEU B C     1 
ATOM   17855 O  O     . LEU B 2  902  ? 182.743 133.463 113.833 1.00 47.77  ? 902  LEU B O     1 
ATOM   17856 C  CB    . LEU B 2  902  ? 183.203 135.404 111.256 1.00 45.10  ? 902  LEU B CB    1 
ATOM   17857 C  CG    . LEU B 2  902  ? 182.880 135.691 109.785 1.00 45.67  ? 902  LEU B CG    1 
ATOM   17858 C  CD1   . LEU B 2  902  ? 184.150 135.943 108.978 1.00 42.84  ? 902  LEU B CD1   1 
ATOM   17859 C  CD2   . LEU B 2  902  ? 182.050 134.577 109.171 1.00 44.80  ? 902  LEU B CD2   1 
ATOM   17860 N  N     . ILE B 2  903  ? 182.464 135.621 114.379 1.00 48.51  ? 903  ILE B N     1 
ATOM   17861 C  CA    . ILE B 2  903  ? 182.885 135.446 115.762 1.00 49.33  ? 903  ILE B CA    1 
ATOM   17862 C  C     . ILE B 2  903  ? 181.715 135.439 116.728 1.00 52.02  ? 903  ILE B C     1 
ATOM   17863 O  O     . ILE B 2  903  ? 181.933 135.440 117.948 1.00 50.92  ? 903  ILE B O     1 
ATOM   17864 C  CB    . ILE B 2  903  ? 183.914 136.517 116.173 1.00 50.13  ? 903  ILE B CB    1 
ATOM   17865 C  CG1   . ILE B 2  903  ? 183.240 137.882 116.333 1.00 48.14  ? 903  ILE B CG1   1 
ATOM   17866 C  CG2   . ILE B 2  903  ? 185.018 136.606 115.140 1.00 47.73  ? 903  ILE B CG2   1 
ATOM   17867 C  CD1   . ILE B 2  903  ? 184.134 138.944 116.934 1.00 47.22  ? 903  ILE B CD1   1 
ATOM   17868 N  N     . THR B 2  904  ? 180.481 135.437 116.228 1.00 51.16  ? 904  THR B N     1 
ATOM   17869 C  CA    . THR B 2  904  ? 179.288 135.392 117.061 1.00 49.35  ? 904  THR B CA    1 
ATOM   17870 C  C     . THR B 2  904  ? 178.472 134.160 116.695 1.00 49.45  ? 904  THR B C     1 
ATOM   17871 O  O     . THR B 2  904  ? 178.264 133.876 115.511 1.00 46.33  ? 904  THR B O     1 
ATOM   17872 C  CB    . THR B 2  904  ? 178.448 136.662 116.894 1.00 51.22  ? 904  THR B CB    1 
ATOM   17873 O  OG1   . THR B 2  904  ? 179.291 137.814 117.025 1.00 49.88  ? 904  THR B OG1   1 
ATOM   17874 C  CG2   . THR B 2  904  ? 177.359 136.727 117.949 1.00 48.35  ? 904  THR B CG2   1 
ATOM   17875 N  N     . LYS B 2  905  ? 178.022 133.432 117.712 1.00 52.46  ? 905  LYS B N     1 
ATOM   17876 C  CA    . LYS B 2  905  ? 177.254 132.208 117.540 1.00 52.75  ? 905  LYS B CA    1 
ATOM   17877 C  C     . LYS B 2  905  ? 175.764 132.495 117.674 1.00 52.88  ? 905  LYS B C     1 
ATOM   17878 O  O     . LYS B 2  905  ? 175.355 133.500 118.261 1.00 52.03  ? 905  LYS B O     1 
ATOM   17879 C  CB    . LYS B 2  905  ? 177.675 131.158 118.572 1.00 49.90  ? 905  LYS B CB    1 
ATOM   17880 C  CG    . LYS B 2  905  ? 177.147 129.756 118.322 1.00 50.03  ? 905  LYS B CG    1 
ATOM   17881 C  CD    . LYS B 2  905  ? 177.419 128.836 119.507 1.00 50.61  ? 905  LYS B CD    1 
ATOM   17882 C  CE    . LYS B 2  905  ? 178.874 128.403 119.548 1.00 50.69  ? 905  LYS B CE    1 
ATOM   17883 N  NZ    . LYS B 2  905  ? 179.140 127.428 120.644 1.00 48.72  ? 905  LYS B NZ    1 
ATOM   17884 N  N     . ASN B 2  906  ? 174.956 131.600 117.103 1.00 53.04  ? 906  ASN B N     1 
ATOM   17885 C  CA    . ASN B 2  906  ? 173.502 131.617 117.261 1.00 52.68  ? 906  ASN B CA    1 
ATOM   17886 C  C     . ASN B 2  906  ? 172.884 132.912 116.736 1.00 52.50  ? 906  ASN B C     1 
ATOM   17887 O  O     . ASN B 2  906  ? 172.027 133.523 117.378 1.00 51.03  ? 906  ASN B O     1 
ATOM   17888 C  CB    . ASN B 2  906  ? 173.106 131.375 118.718 1.00 50.84  ? 906  ASN B CB    1 
ATOM   17889 C  CG    . ASN B 2  906  ? 173.284 129.936 119.128 1.00 54.51  ? 906  ASN B CG    1 
ATOM   17890 O  OD1   . ASN B 2  906  ? 173.041 129.022 118.339 1.00 53.97  ? 906  ASN B OD1   1 
ATOM   17891 N  ND2   . ASN B 2  906  ? 173.707 129.719 120.369 1.00 53.46  ? 906  ASN B ND2   1 
ATOM   17892 N  N     . LEU B 2  907  ? 173.324 133.328 115.552 1.00 46.12  ? 907  LEU B N     1 
ATOM   17893 C  CA    . LEU B 2  907  ? 172.633 134.403 114.860 1.00 47.68  ? 907  LEU B CA    1 
ATOM   17894 C  C     . LEU B 2  907  ? 171.249 133.939 114.431 1.00 50.36  ? 907  LEU B C     1 
ATOM   17895 O  O     . LEU B 2  907  ? 171.074 132.833 113.911 1.00 48.49  ? 907  LEU B O     1 
ATOM   17896 C  CB    . LEU B 2  907  ? 173.430 134.869 113.644 1.00 44.62  ? 907  LEU B CB    1 
ATOM   17897 C  CG    . LEU B 2  907  ? 174.304 136.097 113.879 1.00 46.66  ? 907  LEU B CG    1 
ATOM   17898 C  CD1   . LEU B 2  907  ? 175.538 135.733 114.679 1.00 47.84  ? 907  LEU B CD1   1 
ATOM   17899 C  CD2   . LEU B 2  907  ? 174.682 136.728 112.557 1.00 45.53  ? 907  LEU B CD2   1 
ATOM   17900 N  N     . LYS B 2  908  ? 170.260 134.798 114.658 1.00 49.74  ? 908  LYS B N     1 
ATOM   17901 C  CA    . LYS B 2  908  ? 168.878 134.423 114.396 1.00 47.35  ? 908  LYS B CA    1 
ATOM   17902 C  C     . LYS B 2  908  ? 168.709 134.122 112.911 1.00 48.35  ? 908  LYS B C     1 
ATOM   17903 O  O     . LYS B 2  908  ? 169.121 134.930 112.070 1.00 48.28  ? 908  LYS B O     1 
ATOM   17904 C  CB    . LYS B 2  908  ? 167.926 135.536 114.821 1.00 46.29  ? 908  LYS B CB    1 
ATOM   17905 C  CG    . LYS B 2  908  ? 167.727 135.669 116.317 1.00 45.47  ? 908  LYS B CG    1 
ATOM   17906 C  CD    . LYS B 2  908  ? 168.622 136.756 116.883 1.00 47.93  ? 908  LYS B CD    1 
ATOM   17907 C  CE    . LYS B 2  908  ? 168.497 136.872 118.401 1.00 49.03  ? 908  LYS B CE    1 
ATOM   17908 N  NZ    . LYS B 2  908  ? 169.178 135.761 119.126 1.00 48.11  ? 908  LYS B NZ    1 
ATOM   17909 N  N     . PRO B 2  909  ? 168.136 132.973 112.551 1.00 48.48  ? 909  PRO B N     1 
ATOM   17910 C  CA    . PRO B 2  909  ? 168.049 132.598 111.131 1.00 46.94  ? 909  PRO B CA    1 
ATOM   17911 C  C     . PRO B 2  909  ? 167.197 133.574 110.332 1.00 47.41  ? 909  PRO B C     1 
ATOM   17912 O  O     . PRO B 2  909  ? 166.149 134.031 110.792 1.00 44.72  ? 909  PRO B O     1 
ATOM   17913 C  CB    . PRO B 2  909  ? 167.417 131.202 111.170 1.00 46.14  ? 909  PRO B CB    1 
ATOM   17914 C  CG    . PRO B 2  909  ? 167.646 130.709 112.565 1.00 47.17  ? 909  PRO B CG    1 
ATOM   17915 C  CD    . PRO B 2  909  ? 167.619 131.920 113.438 1.00 47.11  ? 909  PRO B CD    1 
ATOM   17916 N  N     . GLY B 2  910  ? 167.656 133.877 109.119 1.00 41.14  ? 910  GLY B N     1 
ATOM   17917 C  CA    . GLY B 2  910  ? 166.916 134.716 108.197 1.00 39.03  ? 910  GLY B CA    1 
ATOM   17918 C  C     . GLY B 2  910  ? 166.747 136.158 108.615 1.00 40.79  ? 910  GLY B C     1 
ATOM   17919 O  O     . GLY B 2  910  ? 165.976 136.887 107.987 1.00 41.48  ? 910  GLY B O     1 
ATOM   17920 N  N     . ALA B 2  911  ? 167.466 136.603 109.636 1.00 42.32  ? 911  ALA B N     1 
ATOM   17921 C  CA    . ALA B 2  911  ? 167.318 137.948 110.167 1.00 43.51  ? 911  ALA B CA    1 
ATOM   17922 C  C     . ALA B 2  911  ? 168.220 138.927 109.425 1.00 43.58  ? 911  ALA B C     1 
ATOM   17923 O  O     . ALA B 2  911  ? 169.392 138.654 109.161 1.00 43.05  ? 911  ALA B O     1 
ATOM   17924 C  CB    . ALA B 2  911  ? 167.639 137.973 111.662 1.00 42.48  ? 911  ALA B CB    1 
ATOM   17925 N  N     . ASN B 2  912  ? 167.654 140.087 109.105 1.00 41.58  ? 912  ASN B N     1 
ATOM   17926 C  CA    . ASN B 2  912  ? 168.334 141.122 108.339 1.00 42.47  ? 912  ASN B CA    1 
ATOM   17927 C  C     . ASN B 2  912  ? 169.104 142.022 109.295 1.00 45.08  ? 912  ASN B C     1 
ATOM   17928 O  O     . ASN B 2  912  ? 168.505 142.840 109.999 1.00 45.45  ? 912  ASN B O     1 
ATOM   17929 C  CB    . ASN B 2  912  ? 167.332 141.939 107.523 1.00 39.99  ? 912  ASN B CB    1 
ATOM   17930 C  CG    . ASN B 2  912  ? 167.995 142.782 106.451 1.00 42.00  ? 912  ASN B CG    1 
ATOM   17931 O  OD1   . ASN B 2  912  ? 167.692 143.964 106.299 1.00 40.52  ? 912  ASN B OD1   1 
ATOM   17932 N  ND2   . ASN B 2  912  ? 168.897 142.173 105.695 1.00 44.36  ? 912  ASN B ND2   1 
ATOM   17933 N  N     . TYR B 2  913  ? 170.426 141.865 109.319 1.00 43.42  ? 913  TYR B N     1 
ATOM   17934 C  CA    . TYR B 2  913  ? 171.298 142.667 110.164 1.00 42.52  ? 913  TYR B CA    1 
ATOM   17935 C  C     . TYR B 2  913  ? 171.841 143.891 109.446 1.00 42.72  ? 913  TYR B C     1 
ATOM   17936 O  O     . TYR B 2  913  ? 172.601 144.657 110.043 1.00 44.73  ? 913  TYR B O     1 
ATOM   17937 C  CB    . TYR B 2  913  ? 172.467 141.820 110.676 1.00 41.75  ? 913  TYR B CB    1 
ATOM   17938 C  CG    . TYR B 2  913  ? 172.106 140.825 111.755 1.00 42.20  ? 913  TYR B CG    1 
ATOM   17939 C  CD1   . TYR B 2  913  ? 171.628 139.564 111.431 1.00 39.94  ? 913  TYR B CD1   1 
ATOM   17940 C  CD2   . TYR B 2  913  ? 172.259 141.138 113.096 1.00 41.62  ? 913  TYR B CD2   1 
ATOM   17941 C  CE1   . TYR B 2  913  ? 171.303 138.652 112.408 1.00 40.76  ? 913  TYR B CE1   1 
ATOM   17942 C  CE2   . TYR B 2  913  ? 171.934 140.228 114.080 1.00 39.70  ? 913  TYR B CE2   1 
ATOM   17943 C  CZ    . TYR B 2  913  ? 171.459 138.988 113.728 1.00 42.85  ? 913  TYR B CZ    1 
ATOM   17944 O  OH    . TYR B 2  913  ? 171.132 138.080 114.704 1.00 42.18  ? 913  TYR B OH    1 
ATOM   17945 N  N     . GLU B 2  914  ? 171.462 144.103 108.187 1.00 41.68  ? 914  GLU B N     1 
ATOM   17946 C  CA    . GLU B 2  914  ? 172.064 145.180 107.412 1.00 44.30  ? 914  GLU B CA    1 
ATOM   17947 C  C     . GLU B 2  914  ? 171.469 146.540 107.751 1.00 45.53  ? 914  GLU B C     1 
ATOM   17948 O  O     . GLU B 2  914  ? 172.002 147.568 107.319 1.00 44.86  ? 914  GLU B O     1 
ATOM   17949 C  CB    . GLU B 2  914  ? 171.925 144.896 105.920 1.00 46.08  ? 914  GLU B CB    1 
ATOM   17950 C  CG    . GLU B 2  914  ? 172.719 143.693 105.459 1.00 47.42  ? 914  GLU B CG    1 
ATOM   17951 C  CD    . GLU B 2  914  ? 174.183 144.020 105.231 1.00 48.67  ? 914  GLU B CD    1 
ATOM   17952 O  OE1   . GLU B 2  914  ? 174.948 143.111 104.849 1.00 45.28  ? 914  GLU B OE1   1 
ATOM   17953 O  OE2   . GLU B 2  914  ? 174.572 145.188 105.442 1.00 48.68  ? 914  GLU B OE2   1 
ATOM   17954 N  N     . LYS B 2  915  ? 170.369 146.576 108.499 1.00 41.18  ? 915  LYS B N     1 
ATOM   17955 C  CA    . LYS B 2  915  ? 169.829 147.864 108.909 1.00 42.41  ? 915  LYS B CA    1 
ATOM   17956 C  C     . LYS B 2  915  ? 170.630 148.508 110.031 1.00 42.60  ? 915  LYS B C     1 
ATOM   17957 O  O     . LYS B 2  915  ? 170.621 149.738 110.144 1.00 42.66  ? 915  LYS B O     1 
ATOM   17958 C  CB    . LYS B 2  915  ? 168.372 147.717 109.346 1.00 42.70  ? 915  LYS B CB    1 
ATOM   17959 C  CG    . LYS B 2  915  ? 167.429 147.277 108.240 1.00 40.76  ? 915  LYS B CG    1 
ATOM   17960 C  CD    . LYS B 2  915  ? 167.206 148.394 107.243 1.00 37.94  ? 915  LYS B CD    1 
ATOM   17961 C  CE    . LYS B 2  915  ? 166.088 148.057 106.292 1.00 39.02  ? 915  LYS B CE    1 
ATOM   17962 N  NZ    . LYS B 2  915  ? 164.789 147.999 107.005 1.00 39.02  ? 915  LYS B NZ    1 
ATOM   17963 N  N     . LEU B 2  916  ? 171.334 147.720 110.839 1.00 41.50  ? 916  LEU B N     1 
ATOM   17964 C  CA    . LEU B 2  916  ? 171.993 148.240 112.025 1.00 40.29  ? 916  LEU B CA    1 
ATOM   17965 C  C     . LEU B 2  916  ? 173.159 149.144 111.661 1.00 41.56  ? 916  LEU B C     1 
ATOM   17966 O  O     . LEU B 2  916  ? 174.002 148.794 110.833 1.00 45.02  ? 916  LEU B O     1 
ATOM   17967 C  CB    . LEU B 2  916  ? 172.504 147.097 112.899 1.00 42.44  ? 916  LEU B CB    1 
ATOM   17968 C  CG    . LEU B 2  916  ? 171.545 145.986 113.315 1.00 42.48  ? 916  LEU B CG    1 
ATOM   17969 C  CD1   . LEU B 2  916  ? 172.337 144.843 113.898 1.00 41.09  ? 916  LEU B CD1   1 
ATOM   17970 C  CD2   . LEU B 2  916  ? 170.534 146.502 114.315 1.00 40.72  ? 916  LEU B CD2   1 
ATOM   17971 N  N     . VAL B 2  917  ? 173.205 150.314 112.291 1.00 39.92  ? 917  VAL B N     1 
ATOM   17972 C  CA    . VAL B 2  917  ? 174.400 151.147 112.312 1.00 42.14  ? 917  VAL B CA    1 
ATOM   17973 C  C     . VAL B 2  917  ? 174.682 151.485 113.771 1.00 42.29  ? 917  VAL B C     1 
ATOM   17974 O  O     . VAL B 2  917  ? 173.792 151.953 114.490 1.00 40.11  ? 917  VAL B O     1 
ATOM   17975 C  CB    . VAL B 2  917  ? 174.269 152.414 111.437 1.00 40.00  ? 917  VAL B CB    1 
ATOM   17976 C  CG1   . VAL B 2  917  ? 173.630 152.079 110.093 1.00 38.73  ? 917  VAL B CG1   1 
ATOM   17977 C  CG2   . VAL B 2  917  ? 173.488 153.524 112.113 1.00 37.84  ? 917  VAL B CG2   1 
ATOM   17978 N  N     . ASP B 2  918  ? 175.893 151.168 114.227 1.00 47.56  ? 918  ASP B N     1 
ATOM   17979 C  CA    . ASP B 2  918  ? 176.320 151.470 115.592 1.00 47.39  ? 918  ASP B CA    1 
ATOM   17980 C  C     . ASP B 2  918  ? 175.417 150.792 116.623 1.00 47.36  ? 918  ASP B C     1 
ATOM   17981 O  O     . ASP B 2  918  ? 175.260 151.262 117.751 1.00 48.41  ? 918  ASP B O     1 
ATOM   17982 C  CB    . ASP B 2  918  ? 176.374 152.983 115.808 1.00 47.20  ? 918  ASP B CB    1 
ATOM   17983 C  CG    . ASP B 2  918  ? 177.318 153.382 116.916 1.00 48.62  ? 918  ASP B CG    1 
ATOM   17984 O  OD1   . ASP B 2  918  ? 177.927 152.484 117.536 1.00 51.25  ? 918  ASP B OD1   1 
ATOM   17985 O  OD2   . ASP B 2  918  ? 177.465 154.598 117.153 1.00 49.17  ? 918  ASP B OD2   1 
ATOM   17986 N  N     . GLY B 2  919  ? 174.812 149.672 116.230 1.00 44.32  ? 919  GLY B N     1 
ATOM   17987 C  CA    . GLY B 2  919  ? 174.019 148.859 117.125 1.00 43.32  ? 919  GLY B CA    1 
ATOM   17988 C  C     . GLY B 2  919  ? 172.523 149.095 117.078 1.00 43.27  ? 919  GLY B C     1 
ATOM   17989 O  O     . GLY B 2  919  ? 171.760 148.196 117.448 1.00 43.36  ? 919  GLY B O     1 
ATOM   17990 N  N     . PHE B 2  920  ? 172.081 150.267 116.625 1.00 43.35  ? 920  PHE B N     1 
ATOM   17991 C  CA    . PHE B 2  920  ? 170.668 150.598 116.523 1.00 42.23  ? 920  PHE B CA    1 
ATOM   17992 C  C     . PHE B 2  920  ? 170.348 151.033 115.102 1.00 43.18  ? 920  PHE B C     1 
ATOM   17993 O  O     . PHE B 2  920  ? 171.195 151.588 114.400 1.00 45.59  ? 920  PHE B O     1 
ATOM   17994 C  CB    . PHE B 2  920  ? 170.271 151.718 117.494 1.00 39.66  ? 920  PHE B CB    1 
ATOM   17995 C  CG    . PHE B 2  920  ? 170.309 151.316 118.934 1.00 42.01  ? 920  PHE B CG    1 
ATOM   17996 C  CD1   . PHE B 2  920  ? 170.178 149.994 119.303 1.00 44.01  ? 920  PHE B CD1   1 
ATOM   17997 C  CD2   . PHE B 2  920  ? 170.485 152.260 119.922 1.00 42.53  ? 920  PHE B CD2   1 
ATOM   17998 C  CE1   . PHE B 2  920  ? 170.218 149.627 120.629 1.00 43.21  ? 920  PHE B CE1   1 
ATOM   17999 C  CE2   . PHE B 2  920  ? 170.527 151.895 121.246 1.00 42.11  ? 920  PHE B CE2   1 
ATOM   18000 C  CZ    . PHE B 2  920  ? 170.392 150.579 121.600 1.00 41.33  ? 920  PHE B CZ    1 
ATOM   18001 N  N     . VAL B 2  921  ? 169.122 150.772 114.679 1.00 37.16  ? 921  VAL B N     1 
ATOM   18002 C  CA    . VAL B 2  921  ? 168.675 151.251 113.366 1.00 36.37  ? 921  VAL B CA    1 
ATOM   18003 C  C     . VAL B 2  921  ? 168.487 152.764 113.426 1.00 37.78  ? 921  VAL B C     1 
ATOM   18004 O  O     . VAL B 2  921  ? 167.937 153.277 114.414 1.00 37.98  ? 921  VAL B O     1 
ATOM   18005 C  CB    . VAL B 2  921  ? 167.387 150.542 112.957 1.00 36.18  ? 921  VAL B CB    1 
ATOM   18006 C  CG1   . VAL B 2  921  ? 167.109 150.743 111.494 1.00 38.78  ? 921  VAL B CG1   1 
ATOM   18007 C  CG2   . VAL B 2  921  ? 167.519 149.077 113.236 1.00 35.75  ? 921  VAL B CG2   1 
ATOM   18008 N  N     . PRO B 2  922  ? 168.935 153.513 112.422 1.00 37.67  ? 922  PRO B N     1 
ATOM   18009 C  CA    . PRO B 2  922  ? 168.804 154.972 112.475 1.00 39.25  ? 922  PRO B CA    1 
ATOM   18010 C  C     . PRO B 2  922  ? 167.357 155.436 112.413 1.00 37.73  ? 922  PRO B C     1 
ATOM   18011 O  O     . PRO B 2  922  ? 166.458 154.720 111.971 1.00 37.04  ? 922  PRO B O     1 
ATOM   18012 C  CB    . PRO B 2  922  ? 169.594 155.443 111.249 1.00 38.39  ? 922  PRO B CB    1 
ATOM   18013 C  CG    . PRO B 2  922  ? 169.640 154.273 110.347 1.00 34.97  ? 922  PRO B CG    1 
ATOM   18014 C  CD    . PRO B 2  922  ? 169.659 153.066 111.221 1.00 34.21  ? 922  PRO B CD    1 
ATOM   18015 N  N     . VAL B 2  923  ? 167.142 156.659 112.891 1.00 36.16  ? 923  VAL B N     1 
ATOM   18016 C  CA    . VAL B 2  923  ? 165.799 157.211 112.981 1.00 36.09  ? 923  VAL B CA    1 
ATOM   18017 C  C     . VAL B 2  923  ? 165.294 157.555 111.587 1.00 40.21  ? 923  VAL B C     1 
ATOM   18018 O  O     . VAL B 2  923  ? 165.958 158.268 110.823 1.00 41.20  ? 923  VAL B O     1 
ATOM   18019 C  CB    . VAL B 2  923  ? 165.790 158.442 113.896 1.00 38.28  ? 923  VAL B CB    1 
ATOM   18020 C  CG1   . VAL B 2  923  ? 164.619 159.347 113.564 1.00 38.00  ? 923  VAL B CG1   1 
ATOM   18021 C  CG2   . VAL B 2  923  ? 165.746 158.016 115.353 1.00 37.97  ? 923  VAL B CG2   1 
ATOM   18022 N  N     . GLY B 2  924  ? 164.112 157.047 111.247 1.00 37.49  ? 924  GLY B N     1 
ATOM   18023 C  CA    . GLY B 2  924  ? 163.482 157.352 109.981 1.00 35.59  ? 924  GLY B CA    1 
ATOM   18024 C  C     . GLY B 2  924  ? 163.480 156.229 108.976 1.00 38.59  ? 924  GLY B C     1 
ATOM   18025 O  O     . GLY B 2  924  ? 163.041 156.444 107.842 1.00 40.15  ? 924  GLY B O     1 
ATOM   18026 N  N     . THR B 2  925  ? 163.938 155.040 109.340 1.00 38.72  ? 925  THR B N     1 
ATOM   18027 C  CA    . THR B 2  925  ? 163.965 153.920 108.416 1.00 38.57  ? 925  THR B CA    1 
ATOM   18028 C  C     . THR B 2  925  ? 162.845 152.948 108.751 1.00 36.06  ? 925  THR B C     1 
ATOM   18029 O  O     . THR B 2  925  ? 162.529 152.713 109.919 1.00 34.01  ? 925  THR B O     1 
ATOM   18030 C  CB    . THR B 2  925  ? 165.309 153.187 108.455 1.00 37.36  ? 925  THR B CB    1 
ATOM   18031 O  OG1   . THR B 2  925  ? 165.266 152.169 109.458 1.00 32.96  ? 925  THR B OG1   1 
ATOM   18032 C  CG2   . THR B 2  925  ? 166.430 154.154 108.777 1.00 35.87  ? 925  THR B CG2   1 
ATOM   18033 N  N     . VAL B 2  926  ? 162.249 152.388 107.707 1.00 32.82  ? 926  VAL B N     1 
ATOM   18034 C  CA    . VAL B 2  926  ? 161.126 151.473 107.860 1.00 31.10  ? 926  VAL B CA    1 
ATOM   18035 C  C     . VAL B 2  926  ? 161.656 150.082 108.175 1.00 30.63  ? 926  VAL B C     1 
ATOM   18036 O  O     . VAL B 2  926  ? 162.489 149.541 107.443 1.00 34.38  ? 926  VAL B O     1 
ATOM   18037 C  CB    . VAL B 2  926  ? 160.249 151.466 106.602 1.00 33.35  ? 926  VAL B CB    1 
ATOM   18038 C  CG1   . VAL B 2  926  ? 161.100 151.368 105.364 1.00 32.88  ? 926  VAL B CG1   1 
ATOM   18039 C  CG2   . VAL B 2  926  ? 159.264 150.316 106.658 1.00 32.82  ? 926  VAL B CG2   1 
ATOM   18040 N  N     . VAL B 2  927  ? 161.189 149.513 109.264 1.00 31.33  ? 927  VAL B N     1 
ATOM   18041 C  CA    . VAL B 2  927  ? 161.585 148.170 109.659 1.00 32.02  ? 927  VAL B CA    1 
ATOM   18042 C  C     . VAL B 2  927  ? 160.487 147.199 109.258 1.00 34.16  ? 927  VAL B C     1 
ATOM   18043 O  O     . VAL B 2  927  ? 159.303 147.544 109.235 1.00 36.65  ? 927  VAL B O     1 
ATOM   18044 C  CB    . VAL B 2  927  ? 161.888 148.104 111.167 1.00 30.55  ? 927  VAL B CB    1 
ATOM   18045 C  CG1   . VAL B 2  927  ? 162.723 149.296 111.576 1.00 30.62  ? 927  VAL B CG1   1 
ATOM   18046 C  CG2   . VAL B 2  927  ? 160.620 148.048 111.980 1.00 30.50  ? 927  VAL B CG2   1 
ATOM   18047 N  N     . LYS B 2  928  ? 160.886 145.986 108.913 1.00 37.51  ? 928  LYS B N     1 
ATOM   18048 C  CA    . LYS B 2  928  ? 159.987 144.977 108.384 1.00 36.47  ? 928  LYS B CA    1 
ATOM   18049 C  C     . LYS B 2  928  ? 160.002 143.761 109.295 1.00 35.09  ? 928  LYS B C     1 
ATOM   18050 O  O     . LYS B 2  928  ? 160.713 143.714 110.298 1.00 36.53  ? 928  LYS B O     1 
ATOM   18051 C  CB    . LYS B 2  928  ? 160.403 144.595 106.963 1.00 35.48  ? 928  LYS B CB    1 
ATOM   18052 C  CG    . LYS B 2  928  ? 159.280 144.150 106.062 1.00 34.94  ? 928  LYS B CG    1 
ATOM   18053 C  CD    . LYS B 2  928  ? 159.672 144.317 104.607 1.00 34.94  ? 928  LYS B CD    1 
ATOM   18054 C  CE    . LYS B 2  928  ? 160.218 145.709 104.330 1.00 38.10  ? 928  LYS B CE    1 
ATOM   18055 N  NZ    . LYS B 2  928  ? 159.387 146.782 104.947 1.00 41.05  ? 928  LYS B NZ    1 
ATOM   18056 N  N     . LYS B 2  929  ? 159.195 142.771 108.945 1.00 32.86  ? 929  LYS B N     1 
ATOM   18057 C  CA    . LYS B 2  929  ? 159.228 141.516 109.676 1.00 36.42  ? 929  LYS B CA    1 
ATOM   18058 C  C     . LYS B 2  929  ? 160.492 140.759 109.299 1.00 39.23  ? 929  LYS B C     1 
ATOM   18059 O  O     . LYS B 2  929  ? 160.764 140.543 108.115 1.00 41.09  ? 929  LYS B O     1 
ATOM   18060 C  CB    . LYS B 2  929  ? 157.985 140.686 109.378 1.00 34.69  ? 929  LYS B CB    1 
ATOM   18061 C  CG    . LYS B 2  929  ? 157.878 139.444 110.222 1.00 32.24  ? 929  LYS B CG    1 
ATOM   18062 C  CD    . LYS B 2  929  ? 156.563 138.739 109.989 1.00 33.78  ? 929  LYS B CD    1 
ATOM   18063 C  CE    . LYS B 2  929  ? 156.430 137.534 110.894 1.00 36.56  ? 929  LYS B CE    1 
ATOM   18064 N  NZ    . LYS B 2  929  ? 156.336 137.944 112.318 1.00 38.33  ? 929  LYS B NZ    1 
ATOM   18065 N  N     . GLY B 2  930  ? 161.269 140.365 110.305 1.00 41.33  ? 930  GLY B N     1 
ATOM   18066 C  CA    . GLY B 2  930  ? 162.534 139.706 110.106 1.00 39.44  ? 930  GLY B CA    1 
ATOM   18067 C  C     . GLY B 2  930  ? 163.746 140.598 110.271 1.00 41.08  ? 930  GLY B C     1 
ATOM   18068 O  O     . GLY B 2  930  ? 164.858 140.082 110.413 1.00 42.02  ? 930  GLY B O     1 
ATOM   18069 N  N     . ASP B 2  931  ? 163.564 141.914 110.265 1.00 39.22  ? 931  ASP B N     1 
ATOM   18070 C  CA    . ASP B 2  931  ? 164.686 142.825 110.430 1.00 35.54  ? 931  ASP B CA    1 
ATOM   18071 C  C     . ASP B 2  931  ? 165.204 142.811 111.862 1.00 37.98  ? 931  ASP B C     1 
ATOM   18072 O  O     . ASP B 2  931  ? 164.465 142.558 112.816 1.00 37.10  ? 931  ASP B O     1 
ATOM   18073 C  CB    . ASP B 2  931  ? 164.290 144.246 110.042 1.00 33.82  ? 931  ASP B CB    1 
ATOM   18074 C  CG    . ASP B 2  931  ? 164.107 144.409 108.554 1.00 36.99  ? 931  ASP B CG    1 
ATOM   18075 O  OD1   . ASP B 2  931  ? 164.403 143.454 107.811 1.00 39.22  ? 931  ASP B OD1   1 
ATOM   18076 O  OD2   . ASP B 2  931  ? 163.680 145.495 108.122 1.00 36.90  ? 931  ASP B OD2   1 
ATOM   18077 N  N     . ILE B 2  932  ? 166.496 143.073 112.000 1.00 43.33  ? 932  ILE B N     1 
ATOM   18078 C  CA    . ILE B 2  932  ? 167.129 143.233 113.302 1.00 43.26  ? 932  ILE B CA    1 
ATOM   18079 C  C     . ILE B 2  932  ? 167.140 144.716 113.636 1.00 41.83  ? 932  ILE B C     1 
ATOM   18080 O  O     . ILE B 2  932  ? 167.582 145.542 112.830 1.00 40.99  ? 932  ILE B O     1 
ATOM   18081 C  CB    . ILE B 2  932  ? 168.553 142.648 113.305 1.00 41.02  ? 932  ILE B CB    1 
ATOM   18082 C  CG1   . ILE B 2  932  ? 168.508 141.136 113.096 1.00 37.84  ? 932  ILE B CG1   1 
ATOM   18083 C  CG2   . ILE B 2  932  ? 169.265 142.965 114.613 1.00 38.94  ? 932  ILE B CG2   1 
ATOM   18084 C  CD1   . ILE B 2  932  ? 167.937 140.383 114.277 1.00 38.67  ? 932  ILE B CD1   1 
ATOM   18085 N  N     . ILE B 2  933  ? 166.643 145.054 114.817 1.00 40.39  ? 933  ILE B N     1 
ATOM   18086 C  CA    . ILE B 2  933  ? 166.444 146.444 115.194 1.00 40.18  ? 933  ILE B CA    1 
ATOM   18087 C  C     . ILE B 2  933  ? 167.323 146.888 116.355 1.00 40.94  ? 933  ILE B C     1 
ATOM   18088 O  O     . ILE B 2  933  ? 167.715 148.064 116.394 1.00 39.34  ? 933  ILE B O     1 
ATOM   18089 C  CB    . ILE B 2  933  ? 164.956 146.722 115.494 1.00 38.76  ? 933  ILE B CB    1 
ATOM   18090 C  CG1   . ILE B 2  933  ? 164.425 145.693 116.482 1.00 40.43  ? 933  ILE B CG1   1 
ATOM   18091 C  CG2   . ILE B 2  933  ? 164.135 146.732 114.219 1.00 36.88  ? 933  ILE B CG2   1 
ATOM   18092 C  CD1   . ILE B 2  933  ? 163.495 146.255 117.456 1.00 39.17  ? 933  ILE B CD1   1 
ATOM   18093 N  N     . ILE B 2  934  ? 167.642 146.008 117.298 1.00 42.01  ? 934  ILE B N     1 
ATOM   18094 C  CA    . ILE B 2  934  ? 168.588 146.313 118.364 1.00 41.09  ? 934  ILE B CA    1 
ATOM   18095 C  C     . ILE B 2  934  ? 169.614 145.191 118.419 1.00 40.47  ? 934  ILE B C     1 
ATOM   18096 O  O     . ILE B 2  934  ? 169.273 144.051 118.754 1.00 40.17  ? 934  ILE B O     1 
ATOM   18097 C  CB    . ILE B 2  934  ? 167.896 146.490 119.724 1.00 37.69  ? 934  ILE B CB    1 
ATOM   18098 C  CG1   . ILE B 2  934  ? 167.112 147.803 119.747 1.00 38.33  ? 934  ILE B CG1   1 
ATOM   18099 C  CG2   . ILE B 2  934  ? 168.916 146.456 120.851 1.00 35.64  ? 934  ILE B CG2   1 
ATOM   18100 C  CD1   . ILE B 2  934  ? 166.411 148.081 121.055 1.00 40.13  ? 934  ILE B CD1   1 
ATOM   18101 N  N     . GLY B 2  935  ? 170.863 145.511 118.080 1.00 44.13  ? 935  GLY B N     1 
ATOM   18102 C  CA    . GLY B 2  935  ? 171.922 144.522 118.132 1.00 45.78  ? 935  GLY B CA    1 
ATOM   18103 C  C     . GLY B 2  935  ? 172.519 144.388 119.521 1.00 47.02  ? 935  GLY B C     1 
ATOM   18104 O  O     . GLY B 2  935  ? 172.746 145.366 120.230 1.00 46.72  ? 935  GLY B O     1 
ATOM   18105 N  N     . LYS B 2  936  ? 172.789 143.144 119.906 1.00 48.27  ? 936  LYS B N     1 
ATOM   18106 C  CA    . LYS B 2  936  ? 173.286 142.857 121.249 1.00 47.08  ? 936  LYS B CA    1 
ATOM   18107 C  C     . LYS B 2  936  ? 174.132 141.596 121.201 1.00 49.39  ? 936  LYS B C     1 
ATOM   18108 O  O     . LYS B 2  936  ? 173.655 140.547 120.760 1.00 52.24  ? 936  LYS B O     1 
ATOM   18109 C  CB    . LYS B 2  936  ? 172.127 142.696 122.222 1.00 46.93  ? 936  LYS B CB    1 
ATOM   18110 C  CG    . LYS B 2  936  ? 172.352 143.280 123.602 1.00 48.26  ? 936  LYS B CG    1 
ATOM   18111 C  CD    . LYS B 2  936  ? 171.210 142.884 124.511 1.00 49.93  ? 936  LYS B CD    1 
ATOM   18112 C  CE    . LYS B 2  936  ? 171.276 141.406 124.840 1.00 48.29  ? 936  LYS B CE    1 
ATOM   18113 N  NZ    . LYS B 2  936  ? 169.939 140.848 125.174 1.00 46.93  ? 936  LYS B NZ    1 
ATOM   18114 N  N     . VAL B 2  937  ? 175.381 141.699 121.643 1.00 48.61  ? 937  VAL B N     1 
ATOM   18115 C  CA    . VAL B 2  937  ? 176.301 140.571 121.693 1.00 47.30  ? 937  VAL B CA    1 
ATOM   18116 C  C     . VAL B 2  937  ? 176.791 140.410 123.123 1.00 47.46  ? 937  VAL B C     1 
ATOM   18117 O  O     . VAL B 2  937  ? 177.131 141.387 123.796 1.00 48.24  ? 937  VAL B O     1 
ATOM   18118 C  CB    . VAL B 2  937  ? 177.486 140.749 120.718 1.00 47.35  ? 937  VAL B CB    1 
ATOM   18119 C  CG1   . VAL B 2  937  ? 177.038 140.475 119.292 1.00 43.20  ? 937  VAL B CG1   1 
ATOM   18120 C  CG2   . VAL B 2  937  ? 178.044 142.155 120.825 1.00 46.17  ? 937  VAL B CG2   1 
ATOM   18121 N  N     . ALA B 2  938  ? 176.820 139.163 123.588 1.00 46.78  ? 938  ALA B N     1 
ATOM   18122 C  CA    . ALA B 2  938  ? 177.160 138.857 124.974 1.00 46.79  ? 938  ALA B CA    1 
ATOM   18123 C  C     . ALA B 2  938  ? 178.424 138.017 125.002 1.00 47.83  ? 938  ALA B C     1 
ATOM   18124 O  O     . ALA B 2  938  ? 178.469 136.947 124.388 1.00 49.12  ? 938  ALA B O     1 
ATOM   18125 C  CB    . ALA B 2  938  ? 176.018 138.113 125.670 1.00 44.84  ? 938  ALA B CB    1 
ATOM   18126 N  N     . LYS B 2  939  ? 179.440 138.488 125.723 1.00 48.82  ? 939  LYS B N     1 
ATOM   18127 C  CA    . LYS B 2  939  ? 180.661 137.708 125.858 1.00 49.74  ? 939  LYS B CA    1 
ATOM   18128 C  C     . LYS B 2  939  ? 180.388 136.441 126.658 1.00 50.76  ? 939  LYS B C     1 
ATOM   18129 O  O     . LYS B 2  939  ? 179.722 136.469 127.696 1.00 50.45  ? 939  LYS B O     1 
ATOM   18130 C  CB    . LYS B 2  939  ? 181.771 138.526 126.524 1.00 46.14  ? 939  LYS B CB    1 
ATOM   18131 C  CG    . LYS B 2  939  ? 182.468 139.483 125.576 1.00 47.93  ? 939  LYS B CG    1 
ATOM   18132 C  CD    . LYS B 2  939  ? 183.745 140.081 126.145 1.00 49.50  ? 939  LYS B CD    1 
ATOM   18133 C  CE    . LYS B 2  939  ? 183.519 141.467 126.718 1.00 50.19  ? 939  LYS B CE    1 
ATOM   18134 N  NZ    . LYS B 2  939  ? 182.822 141.407 128.028 1.00 49.45  ? 939  LYS B NZ    1 
ATOM   18135 N  N     . ILE B 2  940  ? 180.913 135.327 126.162 1.00 45.50  ? 940  ILE B N     1 
ATOM   18136 C  CA    . ILE B 2  940  ? 180.733 134.034 126.799 1.00 46.21  ? 940  ILE B CA    1 
ATOM   18137 C  C     . ILE B 2  940  ? 181.590 133.945 128.057 1.00 43.27  ? 940  ILE B C     1 
ATOM   18138 O  O     . ILE B 2  940  ? 182.319 134.879 128.390 1.00 43.38  ? 940  ILE B O     1 
ATOM   18139 C  CB    . ILE B 2  940  ? 181.063 132.896 125.815 1.00 45.56  ? 940  ILE B CB    1 
ATOM   18140 C  CG1   . ILE B 2  940  ? 180.091 132.929 124.635 1.00 45.11  ? 940  ILE B CG1   1 
ATOM   18141 C  CG2   . ILE B 2  940  ? 181.011 131.549 126.515 1.00 40.59  ? 940  ILE B CG2   1 
ATOM   18142 C  CD1   . ILE B 2  940  ? 180.410 131.933 123.540 1.00 43.16  ? 940  ILE B CD1   1 
ATOM   18143 N  N     . LYS B 2  949  ? 182.700 132.191 121.208 1.00 52.09  ? 949  LYS B N     1 
ATOM   18144 C  CA    . LYS B 2  949  ? 183.235 133.513 121.510 1.00 54.36  ? 949  LYS B CA    1 
ATOM   18145 C  C     . LYS B 2  949  ? 182.126 134.459 121.954 1.00 55.32  ? 949  LYS B C     1 
ATOM   18146 O  O     . LYS B 2  949  ? 182.230 135.112 122.994 1.00 53.26  ? 949  LYS B O     1 
ATOM   18147 C  CB    . LYS B 2  949  ? 183.968 134.086 120.295 1.00 53.11  ? 949  LYS B CB    1 
ATOM   18148 C  CG    . LYS B 2  949  ? 184.651 135.412 120.559 1.00 52.49  ? 949  LYS B CG    1 
ATOM   18149 C  CD    . LYS B 2  949  ? 185.792 135.258 121.546 1.00 52.29  ? 949  LYS B CD    1 
ATOM   18150 C  CE    . LYS B 2  949  ? 186.563 136.561 121.707 1.00 53.01  ? 949  LYS B CE    1 
ATOM   18151 N  NZ    . LYS B 2  949  ? 185.737 137.636 122.325 1.00 52.83  ? 949  LYS B NZ    1 
ATOM   18152 N  N     . TYR B 2  950  ? 181.064 134.519 121.153 1.00 55.85  ? 950  TYR B N     1 
ATOM   18153 C  CA    . TYR B 2  950  ? 179.893 135.335 121.434 1.00 53.35  ? 950  TYR B CA    1 
ATOM   18154 C  C     . TYR B 2  950  ? 178.631 134.534 121.160 1.00 53.36  ? 950  TYR B C     1 
ATOM   18155 O  O     . TYR B 2  950  ? 178.628 133.611 120.341 1.00 55.15  ? 950  TYR B O     1 
ATOM   18156 C  CB    . TYR B 2  950  ? 179.879 136.598 120.582 1.00 52.42  ? 950  TYR B CB    1 
ATOM   18157 C  CG    . TYR B 2  950  ? 180.942 137.599 120.942 1.00 53.80  ? 950  TYR B CG    1 
ATOM   18158 C  CD1   . TYR B 2  950  ? 180.801 138.412 122.053 1.00 52.25  ? 950  TYR B CD1   1 
ATOM   18159 C  CD2   . TYR B 2  950  ? 182.094 137.722 120.180 1.00 53.00  ? 950  TYR B CD2   1 
ATOM   18160 C  CE1   . TYR B 2  950  ? 181.765 139.331 122.378 1.00 53.88  ? 950  TYR B CE1   1 
ATOM   18161 C  CE2   . TYR B 2  950  ? 183.071 138.632 120.509 1.00 53.71  ? 950  TYR B CE2   1 
ATOM   18162 C  CZ    . TYR B 2  950  ? 182.902 139.433 121.612 1.00 54.76  ? 950  TYR B CZ    1 
ATOM   18163 O  OH    . TYR B 2  950  ? 183.869 140.350 121.952 1.00 54.82  ? 950  TYR B OH    1 
ATOM   18164 N  N     . ILE B 2  951  ? 177.553 134.901 121.844 1.00 46.52  ? 951  ILE B N     1 
ATOM   18165 C  CA    . ILE B 2  951  ? 176.220 134.407 121.526 1.00 49.09  ? 951  ILE B CA    1 
ATOM   18166 C  C     . ILE B 2  951  ? 175.371 135.610 121.141 1.00 50.48  ? 951  ILE B C     1 
ATOM   18167 O  O     . ILE B 2  951  ? 175.543 136.706 121.686 1.00 52.93  ? 951  ILE B O     1 
ATOM   18168 C  CB    . ILE B 2  951  ? 175.592 133.601 122.687 1.00 49.58  ? 951  ILE B CB    1 
ATOM   18169 C  CG1   . ILE B 2  951  ? 174.579 132.593 122.145 1.00 48.77  ? 951  ILE B CG1   1 
ATOM   18170 C  CG2   . ILE B 2  951  ? 174.919 134.505 123.706 1.00 49.21  ? 951  ILE B CG2   1 
ATOM   18171 C  CD1   . ILE B 2  951  ? 174.279 131.451 123.093 1.00 48.87  ? 951  ILE B CD1   1 
ATOM   18172 N  N     . ASP B 2  952  ? 174.496 135.418 120.158 1.00 47.54  ? 952  ASP B N     1 
ATOM   18173 C  CA    . ASP B 2  952  ? 173.777 136.523 119.528 1.00 48.29  ? 952  ASP B CA    1 
ATOM   18174 C  C     . ASP B 2  952  ? 172.435 136.702 120.225 1.00 48.72  ? 952  ASP B C     1 
ATOM   18175 O  O     . ASP B 2  952  ? 171.461 136.016 119.908 1.00 51.62  ? 952  ASP B O     1 
ATOM   18176 C  CB    . ASP B 2  952  ? 173.595 136.254 118.039 1.00 47.74  ? 952  ASP B CB    1 
ATOM   18177 C  CG    . ASP B 2  952  ? 173.287 137.505 117.258 1.00 50.27  ? 952  ASP B CG    1 
ATOM   18178 O  OD1   . ASP B 2  952  ? 174.240 138.240 116.931 1.00 49.88  ? 952  ASP B OD1   1 
ATOM   18179 O  OD2   . ASP B 2  952  ? 172.094 137.756 116.976 1.00 47.46  ? 952  ASP B OD2   1 
ATOM   18180 N  N     . ARG B 2  953  ? 172.383 137.614 121.188 1.00 49.05  ? 953  ARG B N     1 
ATOM   18181 C  CA    . ARG B 2  953  ? 171.126 137.952 121.855 1.00 52.63  ? 953  ARG B CA    1 
ATOM   18182 C  C     . ARG B 2  953  ? 170.536 139.243 121.282 1.00 51.32  ? 953  ARG B C     1 
ATOM   18183 O  O     . ARG B 2  953  ? 170.288 140.220 121.980 1.00 48.79  ? 953  ARG B O     1 
ATOM   18184 C  CB    . ARG B 2  953  ? 171.333 138.037 123.366 1.00 51.85  ? 953  ARG B CB    1 
ATOM   18185 C  CG    . ARG B 2  953  ? 171.278 136.669 124.047 1.00 51.05  ? 953  ARG B CG    1 
ATOM   18186 C  CD    . ARG B 2  953  ? 170.866 136.750 125.519 1.00 51.37  ? 953  ARG B CD    1 
ATOM   18187 N  NE    . ARG B 2  953  ? 171.945 137.160 126.411 1.00 54.51  ? 953  ARG B NE    1 
ATOM   18188 C  CZ    . ARG B 2  953  ? 172.824 136.323 126.947 1.00 53.95  ? 953  ARG B CZ    1 
ATOM   18189 N  NH1   . ARG B 2  953  ? 172.802 135.029 126.675 1.00 52.32  ? 953  ARG B NH1   1 
ATOM   18190 N  NH2   . ARG B 2  953  ? 173.746 136.794 127.781 1.00 52.13  ? 953  ARG B NH2   1 
ATOM   18191 N  N     . SER B 2  954  ? 170.289 139.217 119.975 1.00 44.74  ? 954  SER B N     1 
ATOM   18192 C  CA    . SER B 2  954  ? 169.705 140.344 119.268 1.00 42.30  ? 954  SER B CA    1 
ATOM   18193 C  C     . SER B 2  954  ? 168.180 140.322 119.386 1.00 44.92  ? 954  SER B C     1 
ATOM   18194 O  O     . SER B 2  954  ? 167.590 139.451 120.032 1.00 42.88  ? 954  SER B O     1 
ATOM   18195 C  CB    . SER B 2  954  ? 170.126 140.323 117.801 1.00 44.55  ? 954  SER B CB    1 
ATOM   18196 O  OG    . SER B 2  954  ? 171.531 140.443 117.677 1.00 44.71  ? 954  SER B OG    1 
ATOM   18197 N  N     . VAL B 2  955  ? 167.538 141.309 118.760 1.00 43.06  ? 955  VAL B N     1 
ATOM   18198 C  CA    . VAL B 2  955  ? 166.090 141.483 118.818 1.00 39.93  ? 955  VAL B CA    1 
ATOM   18199 C  C     . VAL B 2  955  ? 165.554 141.622 117.400 1.00 42.66  ? 955  VAL B C     1 
ATOM   18200 O  O     . VAL B 2  955  ? 166.057 142.438 116.619 1.00 42.21  ? 955  VAL B O     1 
ATOM   18201 C  CB    . VAL B 2  955  ? 165.694 142.707 119.664 1.00 39.23  ? 955  VAL B CB    1 
ATOM   18202 C  CG1   . VAL B 2  955  ? 164.190 142.774 119.808 1.00 40.78  ? 955  VAL B CG1   1 
ATOM   18203 C  CG2   . VAL B 2  955  ? 166.347 142.658 121.029 1.00 39.22  ? 955  VAL B CG2   1 
ATOM   18204 N  N     . MET B 2  956  ? 164.531 140.839 117.075 1.00 48.44  ? 956  MET B N     1 
ATOM   18205 C  CA    . MET B 2  956  ? 163.850 140.939 115.795 1.00 50.01  ? 956  MET B CA    1 
ATOM   18206 C  C     . MET B 2  956  ? 162.634 141.849 115.908 1.00 51.21  ? 956  MET B C     1 
ATOM   18207 O  O     . MET B 2  956  ? 162.171 142.163 117.008 1.00 51.00  ? 956  MET B O     1 
ATOM   18208 C  CB    . MET B 2  956  ? 163.384 139.572 115.291 1.00 50.59  ? 956  MET B CB    1 
ATOM   18209 C  CG    . MET B 2  956  ? 164.382 138.793 114.472 1.00 50.24  ? 956  MET B CG    1 
ATOM   18210 S  SD    . MET B 2  956  ? 163.543 137.369 113.757 1.00 59.54  ? 956  MET B SD    1 
ATOM   18211 C  CE    . MET B 2  956  ? 164.911 136.403 113.143 1.00 48.95  ? 956  MET B CE    1 
ATOM   18212 N  N     . TYR B 2  957  ? 162.120 142.263 114.752 1.00 39.74  ? 957  TYR B N     1 
ATOM   18213 C  CA    . TYR B 2  957  ? 160.820 142.921 114.661 1.00 35.70  ? 957  TYR B CA    1 
ATOM   18214 C  C     . TYR B 2  957  ? 159.791 141.868 114.275 1.00 36.46  ? 957  TYR B C     1 
ATOM   18215 O  O     . TYR B 2  957  ? 159.662 141.508 113.105 1.00 35.95  ? 957  TYR B O     1 
ATOM   18216 C  CB    . TYR B 2  957  ? 160.843 144.063 113.653 1.00 34.89  ? 957  TYR B CB    1 
ATOM   18217 C  CG    . TYR B 2  957  ? 159.539 144.816 113.613 1.00 36.08  ? 957  TYR B CG    1 
ATOM   18218 C  CD1   . TYR B 2  957  ? 159.167 145.653 114.648 1.00 36.28  ? 957  TYR B CD1   1 
ATOM   18219 C  CD2   . TYR B 2  957  ? 158.659 144.657 112.558 1.00 34.09  ? 957  TYR B CD2   1 
ATOM   18220 C  CE1   . TYR B 2  957  ? 157.973 146.324 114.621 1.00 35.13  ? 957  TYR B CE1   1 
ATOM   18221 C  CE2   . TYR B 2  957  ? 157.464 145.326 112.525 1.00 35.02  ? 957  TYR B CE2   1 
ATOM   18222 C  CZ    . TYR B 2  957  ? 157.126 146.158 113.561 1.00 34.11  ? 957  TYR B CZ    1 
ATOM   18223 O  OH    . TYR B 2  957  ? 155.930 146.831 113.540 1.00 33.68  ? 957  TYR B OH    1 
ATOM   18224 N  N     . GLY B 2  958  ? 159.068 141.355 115.263 1.00 35.66  ? 958  GLY B N     1 
ATOM   18225 C  CA    . GLY B 2  958  ? 158.072 140.339 114.998 1.00 35.82  ? 958  GLY B CA    1 
ATOM   18226 C  C     . GLY B 2  958  ? 156.653 140.850 114.897 1.00 35.43  ? 958  GLY B C     1 
ATOM   18227 O  O     . GLY B 2  958  ? 155.796 140.446 115.686 1.00 40.71  ? 958  GLY B O     1 
ATOM   18228 N  N     . PHE B 2  959  ? 156.381 141.726 113.933 1.00 34.15  ? 959  PHE B N     1 
ATOM   18229 C  CA    . PHE B 2  959  ? 155.042 142.259 113.729 1.00 35.07  ? 959  PHE B CA    1 
ATOM   18230 C  C     . PHE B 2  959  ? 154.674 142.189 112.259 1.00 34.14  ? 959  PHE B C     1 
ATOM   18231 O  O     . PHE B 2  959  ? 155.536 142.210 111.380 1.00 34.06  ? 959  PHE B O     1 
ATOM   18232 C  CB    . PHE B 2  959  ? 154.906 143.699 114.217 1.00 32.50  ? 959  PHE B CB    1 
ATOM   18233 C  CG    . PHE B 2  959  ? 154.746 143.819 115.696 1.00 32.08  ? 959  PHE B CG    1 
ATOM   18234 C  CD1   . PHE B 2  959  ? 153.621 143.329 116.318 1.00 29.95  ? 959  PHE B CD1   1 
ATOM   18235 C  CD2   . PHE B 2  959  ? 155.714 144.430 116.461 1.00 31.98  ? 959  PHE B CD2   1 
ATOM   18236 C  CE1   . PHE B 2  959  ? 153.469 143.436 117.672 1.00 32.55  ? 959  PHE B CE1   1 
ATOM   18237 C  CE2   . PHE B 2  959  ? 155.564 144.542 117.814 1.00 33.40  ? 959  PHE B CE2   1 
ATOM   18238 C  CZ    . PHE B 2  959  ? 154.440 144.041 118.421 1.00 32.94  ? 959  PHE B CZ    1 
ATOM   18239 N  N     . ASP B 2  960  ? 153.368 142.113 112.010 1.00 38.14  ? 960  ASP B N     1 
ATOM   18240 C  CA    . ASP B 2  960  ? 152.870 141.885 110.660 1.00 39.61  ? 960  ASP B CA    1 
ATOM   18241 C  C     . ASP B 2  960  ? 152.966 143.142 109.807 1.00 39.93  ? 960  ASP B C     1 
ATOM   18242 O  O     . ASP B 2  960  ? 153.133 143.056 108.587 1.00 40.14  ? 960  ASP B O     1 
ATOM   18243 C  CB    . ASP B 2  960  ? 151.428 141.398 110.726 1.00 42.45  ? 960  ASP B CB    1 
ATOM   18244 C  CG    . ASP B 2  960  ? 151.263 140.197 111.634 1.00 47.28  ? 960  ASP B CG    1 
ATOM   18245 O  OD1   . ASP B 2  960  ? 152.215 139.392 111.728 1.00 48.57  ? 960  ASP B OD1   1 
ATOM   18246 O  OD2   . ASP B 2  960  ? 150.176 140.051 112.243 1.00 44.69  ? 960  ASP B OD2   1 
ATOM   18247 N  N     . GLU B 2  961  ? 152.838 144.313 110.424 1.00 32.52  ? 961  GLU B N     1 
ATOM   18248 C  CA    . GLU B 2  961  ? 152.903 145.489 109.572 1.00 30.80  ? 961  GLU B CA    1 
ATOM   18249 C  C     . GLU B 2  961  ? 154.166 146.288 109.846 1.00 30.73  ? 961  GLU B C     1 
ATOM   18250 O  O     . GLU B 2  961  ? 154.602 146.383 110.996 1.00 31.42  ? 961  GLU B O     1 
ATOM   18251 C  CB    . GLU B 2  961  ? 151.684 146.387 109.783 1.00 30.82  ? 961  GLU B CB    1 
ATOM   18252 C  CG    . GLU B 2  961  ? 151.346 146.655 111.228 1.00 33.39  ? 961  GLU B CG    1 
ATOM   18253 C  CD    . GLU B 2  961  ? 150.509 147.897 111.393 1.00 34.42  ? 961  GLU B CD    1 
ATOM   18254 O  OE1   . GLU B 2  961  ? 150.390 148.657 110.416 1.00 30.14  ? 961  GLU B OE1   1 
ATOM   18255 O  OE2   . GLU B 2  961  ? 149.975 148.118 112.499 1.00 34.29  ? 961  GLU B OE2   1 
ATOM   18256 N  N     . PRO B 2  962  ? 154.755 146.868 108.805 1.00 26.26  ? 962  PRO B N     1 
ATOM   18257 C  CA    . PRO B 2  962  ? 155.999 147.619 108.989 1.00 24.53  ? 962  PRO B CA    1 
ATOM   18258 C  C     . PRO B 2  962  ? 155.789 148.848 109.856 1.00 26.38  ? 962  PRO B C     1 
ATOM   18259 O  O     . PRO B 2  962  ? 154.712 149.444 109.873 1.00 32.89  ? 962  PRO B O     1 
ATOM   18260 C  CB    . PRO B 2  962  ? 156.394 148.002 107.562 1.00 22.07  ? 962  PRO B CB    1 
ATOM   18261 C  CG    . PRO B 2  962  ? 155.135 147.950 106.797 1.00 28.22  ? 962  PRO B CG    1 
ATOM   18262 C  CD    . PRO B 2  962  ? 154.322 146.857 107.401 1.00 26.26  ? 962  PRO B CD    1 
ATOM   18263 N  N     . ALA B 2  963  ? 156.831 149.221 110.578 1.00 21.90  ? 963  ALA B N     1 
ATOM   18264 C  CA    . ALA B 2  963  ? 156.847 150.436 111.368 1.00 23.48  ? 963  ALA B CA    1 
ATOM   18265 C  C     . ALA B 2  963  ? 157.935 151.358 110.845 1.00 28.22  ? 963  ALA B C     1 
ATOM   18266 O  O     . ALA B 2  963  ? 158.591 151.081 109.844 1.00 32.43  ? 963  ALA B O     1 
ATOM   18267 C  CB    . ALA B 2  963  ? 157.059 150.123 112.848 1.00 21.06  ? 963  ALA B CB    1 
ATOM   18268 N  N     . VAL B 2  964  ? 158.102 152.482 111.523 1.00 25.01  ? 964  VAL B N     1 
ATOM   18269 C  CA    . VAL B 2  964  ? 159.177 153.419 111.245 1.00 23.53  ? 964  VAL B CA    1 
ATOM   18270 C  C     . VAL B 2  964  ? 159.772 153.835 112.576 1.00 29.79  ? 964  VAL B C     1 
ATOM   18271 O  O     . VAL B 2  964  ? 159.044 154.078 113.543 1.00 33.02  ? 964  VAL B O     1 
ATOM   18272 C  CB    . VAL B 2  964  ? 158.688 154.637 110.436 1.00 23.73  ? 964  VAL B CB    1 
ATOM   18273 C  CG1   . VAL B 2  964  ? 159.700 155.740 110.471 1.00 24.76  ? 964  VAL B CG1   1 
ATOM   18274 C  CG2   . VAL B 2  964  ? 158.444 154.241 109.002 1.00 24.81  ? 964  VAL B CG2   1 
ATOM   18275 N  N     . VAL B 2  965  ? 161.100 153.875 112.639 1.00 35.63  ? 965  VAL B N     1 
ATOM   18276 C  CA    . VAL B 2  965  ? 161.785 154.259 113.867 1.00 35.29  ? 965  VAL B CA    1 
ATOM   18277 C  C     . VAL B 2  965  ? 161.539 155.743 114.098 1.00 32.62  ? 965  VAL B C     1 
ATOM   18278 O  O     . VAL B 2  965  ? 161.864 156.576 113.250 1.00 36.21  ? 965  VAL B O     1 
ATOM   18279 C  CB    . VAL B 2  965  ? 163.280 153.942 113.800 1.00 33.14  ? 965  VAL B CB    1 
ATOM   18280 C  CG1   . VAL B 2  965  ? 163.848 153.853 115.192 1.00 32.73  ? 965  VAL B CG1   1 
ATOM   18281 C  CG2   . VAL B 2  965  ? 163.498 152.641 113.056 1.00 32.12  ? 965  VAL B CG2   1 
ATOM   18282 N  N     . ASP B 2  966  ? 160.951 156.077 115.242 1.00 27.97  ? 966  ASP B N     1 
ATOM   18283 C  CA    . ASP B 2  966  ? 160.647 157.471 115.524 1.00 34.14  ? 966  ASP B CA    1 
ATOM   18284 C  C     . ASP B 2  966  ? 161.741 158.118 116.360 1.00 35.22  ? 966  ASP B C     1 
ATOM   18285 O  O     . ASP B 2  966  ? 162.212 159.213 116.038 1.00 33.98  ? 966  ASP B O     1 
ATOM   18286 C  CB    . ASP B 2  966  ? 159.296 157.581 116.229 1.00 35.69  ? 966  ASP B CB    1 
ATOM   18287 C  CG    . ASP B 2  966  ? 158.618 158.903 115.973 1.00 34.87  ? 966  ASP B CG    1 
ATOM   18288 O  OD1   . ASP B 2  966  ? 157.390 158.985 116.152 1.00 38.00  ? 966  ASP B OD1   1 
ATOM   18289 O  OD2   . ASP B 2  966  ? 159.309 159.865 115.594 1.00 33.81  ? 966  ASP B OD2   1 
ATOM   18290 N  N     . ALA B 2  967  ? 162.160 157.455 117.434 1.00 38.68  ? 967  ALA B N     1 
ATOM   18291 C  CA    . ALA B 2  967  ? 163.171 158.007 118.323 1.00 38.75  ? 967  ALA B CA    1 
ATOM   18292 C  C     . ALA B 2  967  ? 164.015 156.881 118.893 1.00 38.01  ? 967  ALA B C     1 
ATOM   18293 O  O     . ALA B 2  967  ? 163.480 155.838 119.274 1.00 38.65  ? 967  ALA B O     1 
ATOM   18294 C  CB    . ALA B 2  967  ? 162.527 158.809 119.458 1.00 35.33  ? 967  ALA B CB    1 
ATOM   18295 N  N     . VAL B 2  968  ? 165.327 157.095 118.946 1.00 41.07  ? 968  VAL B N     1 
ATOM   18296 C  CA    . VAL B 2  968  ? 166.253 156.189 119.615 1.00 41.79  ? 968  VAL B CA    1 
ATOM   18297 C  C     . VAL B 2  968  ? 167.012 156.976 120.673 1.00 43.25  ? 968  VAL B C     1 
ATOM   18298 O  O     . VAL B 2  968  ? 167.649 157.990 120.369 1.00 43.75  ? 968  VAL B O     1 
ATOM   18299 C  CB    . VAL B 2  968  ? 167.229 155.525 118.623 1.00 41.60  ? 968  VAL B CB    1 
ATOM   18300 C  CG1   . VAL B 2  968  ? 168.530 155.178 119.311 1.00 41.85  ? 968  VAL B CG1   1 
ATOM   18301 C  CG2   . VAL B 2  968  ? 166.608 154.291 118.019 1.00 41.59  ? 968  VAL B CG2   1 
ATOM   18302 N  N     . MET B 2  969  ? 166.945 156.504 121.915 1.00 45.54  ? 969  MET B N     1 
ATOM   18303 C  CA    . MET B 2  969  ? 167.631 157.147 123.025 1.00 44.85  ? 969  MET B CA    1 
ATOM   18304 C  C     . MET B 2  969  ? 168.386 156.092 123.818 1.00 48.62  ? 969  MET B C     1 
ATOM   18305 O  O     . MET B 2  969  ? 168.046 154.907 123.795 1.00 48.93  ? 969  MET B O     1 
ATOM   18306 C  CB    . MET B 2  969  ? 166.656 157.900 123.938 1.00 43.21  ? 969  MET B CB    1 
ATOM   18307 C  CG    . MET B 2  969  ? 165.579 158.686 123.212 1.00 46.11  ? 969  MET B CG    1 
ATOM   18308 S  SD    . MET B 2  969  ? 165.206 160.237 124.046 1.00 54.03  ? 969  MET B SD    1 
ATOM   18309 C  CE    . MET B 2  969  ? 164.419 161.168 122.731 1.00 43.45  ? 969  MET B CE    1 
ATOM   18310 N  N     . ARG B 2  970  ? 169.423 156.541 124.532 1.00 52.80  ? 970  ARG B N     1 
ATOM   18311 C  CA    . ARG B 2  970  ? 170.265 155.673 125.355 1.00 50.85  ? 970  ARG B CA    1 
ATOM   18312 C  C     . ARG B 2  970  ? 170.387 156.269 126.756 1.00 51.77  ? 970  ARG B C     1 
ATOM   18313 O  O     . ARG B 2  970  ? 171.469 156.730 127.149 1.00 53.08  ? 970  ARG B O     1 
ATOM   18314 C  CB    . ARG B 2  970  ? 171.645 155.503 124.723 1.00 49.94  ? 970  ARG B CB    1 
ATOM   18315 C  CG    . ARG B 2  970  ? 171.653 154.744 123.394 1.00 51.11  ? 970  ARG B CG    1 
ATOM   18316 C  CD    . ARG B 2  970  ? 173.047 154.720 122.799 1.00 51.53  ? 970  ARG B CD    1 
ATOM   18317 N  NE    . ARG B 2  970  ? 173.117 154.004 121.532 1.00 51.43  ? 970  ARG B NE    1 
ATOM   18318 C  CZ    . ARG B 2  970  ? 172.975 154.574 120.344 1.00 52.68  ? 970  ARG B CZ    1 
ATOM   18319 N  NH1   . ARG B 2  970  ? 172.692 155.859 120.223 1.00 50.66  ? 970  ARG B NH1   1 
ATOM   18320 N  NH2   . ARG B 2  970  ? 173.122 153.836 119.248 1.00 53.90  ? 970  ARG B NH2   1 
ATOM   18321 N  N     . PRO B 2  971  ? 169.297 156.297 127.539 1.00 46.43  ? 971  PRO B N     1 
ATOM   18322 C  CA    . PRO B 2  971  ? 169.389 156.844 128.903 1.00 46.27  ? 971  PRO B CA    1 
ATOM   18323 C  C     . PRO B 2  971  ? 170.047 155.925 129.921 1.00 46.14  ? 971  PRO B C     1 
ATOM   18324 O  O     . PRO B 2  971  ? 170.495 154.824 129.589 1.00 43.05  ? 971  PRO B O     1 
ATOM   18325 C  CB    . PRO B 2  971  ? 167.901 157.060 129.202 1.00 46.08  ? 971  PRO B CB    1 
ATOM   18326 C  CG    . PRO B 2  971  ? 167.412 155.856 128.441 1.00 47.58  ? 971  PRO B CG    1 
ATOM   18327 C  CD    . PRO B 2  971  ? 167.869 156.370 127.195 1.00 45.93  ? 971  PRO B CD    1 
ATOM   18328 N  N     . HIS B 2  972  ? 170.091 156.371 131.177 1.00 50.20  ? 972  HIS B N     1 
ATOM   18329 C  CA    . HIS B 2  972  ? 170.717 155.638 132.268 1.00 50.82  ? 972  HIS B CA    1 
ATOM   18330 C  C     . HIS B 2  972  ? 169.647 155.087 133.199 1.00 50.20  ? 972  HIS B C     1 
ATOM   18331 O  O     . HIS B 2  972  ? 168.770 155.825 133.656 1.00 50.05  ? 972  HIS B O     1 
ATOM   18332 C  CB    . HIS B 2  972  ? 171.667 156.541 133.057 1.00 50.16  ? 972  HIS B CB    1 
ATOM   18333 C  CG    . HIS B 2  972  ? 172.805 157.078 132.247 1.00 52.30  ? 972  HIS B CG    1 
ATOM   18334 N  ND1   . HIS B 2  972  ? 173.928 156.336 131.955 1.00 50.73  ? 972  HIS B ND1   1 
ATOM   18335 C  CD2   . HIS B 2  972  ? 172.990 158.286 131.665 1.00 50.18  ? 972  HIS B CD2   1 
ATOM   18336 C  CE1   . HIS B 2  972  ? 174.758 157.065 131.230 1.00 49.84  ? 972  HIS B CE1   1 
ATOM   18337 N  NE2   . HIS B 2  972  ? 174.211 158.252 131.037 1.00 50.04  ? 972  HIS B NE2   1 
ATOM   18338 N  N     . GLY B 2  973  ? 169.735 153.793 133.498 1.00 43.90  ? 973  GLY B N     1 
ATOM   18339 C  CA    . GLY B 2  973  ? 168.706 153.129 134.260 1.00 44.15  ? 973  GLY B CA    1 
ATOM   18340 C  C     . GLY B 2  973  ? 168.788 153.440 135.736 1.00 47.96  ? 973  GLY B C     1 
ATOM   18341 O  O     . GLY B 2  973  ? 169.585 154.271 136.195 1.00 44.98  ? 973  GLY B O     1 
ATOM   18342 N  N     . PRO B 2  974  ? 167.924 152.774 136.510 1.00 48.58  ? 974  PRO B N     1 
ATOM   18343 C  CA    . PRO B 2  974  ? 167.968 152.946 137.971 1.00 46.32  ? 974  PRO B CA    1 
ATOM   18344 C  C     . PRO B 2  974  ? 169.309 152.575 138.570 1.00 48.13  ? 974  PRO B C     1 
ATOM   18345 O  O     . PRO B 2  974  ? 169.757 153.236 139.515 1.00 48.41  ? 974  PRO B O     1 
ATOM   18346 C  CB    . PRO B 2  974  ? 166.852 152.017 138.467 1.00 45.10  ? 974  PRO B CB    1 
ATOM   18347 C  CG    . PRO B 2  974  ? 165.953 151.837 137.295 1.00 45.95  ? 974  PRO B CG    1 
ATOM   18348 C  CD    . PRO B 2  974  ? 166.841 151.873 136.088 1.00 45.14  ? 974  PRO B CD    1 
ATOM   18349 N  N     . ASN B 2  975  ? 169.967 151.542 138.040 1.00 47.37  ? 975  ASN B N     1 
ATOM   18350 C  CA    . ASN B 2  975  ? 171.315 151.166 138.440 1.00 46.59  ? 975  ASN B CA    1 
ATOM   18351 C  C     . ASN B 2  975  ? 172.380 151.833 137.588 1.00 46.08  ? 975  ASN B C     1 
ATOM   18352 O  O     . ASN B 2  975  ? 173.506 151.328 137.514 1.00 44.29  ? 975  ASN B O     1 
ATOM   18353 C  CB    . ASN B 2  975  ? 171.487 149.648 138.381 1.00 45.41  ? 975  ASN B CB    1 
ATOM   18354 C  CG    . ASN B 2  975  ? 170.873 148.951 139.568 1.00 46.96  ? 975  ASN B CG    1 
ATOM   18355 O  OD1   . ASN B 2  975  ? 170.963 149.433 140.696 1.00 48.19  ? 975  ASN B OD1   1 
ATOM   18356 N  ND2   . ASN B 2  975  ? 170.243 147.809 139.323 1.00 44.82  ? 975  ASN B ND2   1 
ATOM   18357 N  N     . ASP B 2  976  ? 172.040 152.942 136.931 1.00 51.56  ? 976  ASP B N     1 
ATOM   18358 C  CA    . ASP B 2  976  ? 172.979 153.716 136.121 1.00 53.86  ? 976  ASP B CA    1 
ATOM   18359 C  C     . ASP B 2  976  ? 173.603 152.850 135.031 1.00 53.59  ? 976  ASP B C     1 
ATOM   18360 O  O     . ASP B 2  976  ? 174.766 153.012 134.663 1.00 52.73  ? 976  ASP B O     1 
ATOM   18361 C  CB    . ASP B 2  976  ? 174.048 154.354 137.005 1.00 52.49  ? 976  ASP B CB    1 
ATOM   18362 C  CG    . ASP B 2  976  ? 173.452 155.215 138.092 1.00 54.15  ? 976  ASP B CG    1 
ATOM   18363 O  OD1   . ASP B 2  976  ? 172.461 155.917 137.816 1.00 53.60  ? 976  ASP B OD1   1 
ATOM   18364 O  OD2   . ASP B 2  976  ? 173.955 155.167 139.232 1.00 56.47  ? 976  ASP B OD2   1 
ATOM   18365 N  N     . GLU B 2  977  ? 172.801 151.930 134.502 1.00 51.00  ? 977  GLU B N     1 
ATOM   18366 C  CA    . GLU B 2  977  ? 173.223 151.035 133.438 1.00 50.65  ? 977  GLU B CA    1 
ATOM   18367 C  C     . GLU B 2  977  ? 172.583 151.494 132.140 1.00 50.38  ? 977  GLU B C     1 
ATOM   18368 O  O     . GLU B 2  977  ? 171.452 151.988 132.137 1.00 50.48  ? 977  GLU B O     1 
ATOM   18369 C  CB    . GLU B 2  977  ? 172.837 149.580 133.731 1.00 47.84  ? 977  GLU B CB    1 
ATOM   18370 C  CG    . GLU B 2  977  ? 171.344 149.332 133.829 1.00 49.14  ? 977  GLU B CG    1 
ATOM   18371 C  CD    . GLU B 2  977  ? 170.771 148.718 132.560 1.00 52.38  ? 977  GLU B CD    1 
ATOM   18372 O  OE1   . GLU B 2  977  ? 171.556 148.186 131.750 1.00 51.74  ? 977  GLU B OE1   1 
ATOM   18373 O  OE2   . GLU B 2  977  ? 169.536 148.764 132.376 1.00 52.10  ? 977  GLU B OE2   1 
ATOM   18374 N  N     . ILE B 2  978  ? 173.319 151.349 131.041 1.00 44.97  ? 978  ILE B N     1 
ATOM   18375 C  CA    . ILE B 2  978  ? 172.821 151.798 129.750 1.00 45.11  ? 978  ILE B CA    1 
ATOM   18376 C  C     . ILE B 2  978  ? 171.826 150.778 129.217 1.00 45.53  ? 978  ILE B C     1 
ATOM   18377 O  O     . ILE B 2  978  ? 172.110 149.575 129.167 1.00 46.35  ? 978  ILE B O     1 
ATOM   18378 C  CB    . ILE B 2  978  ? 173.984 152.012 128.771 1.00 47.88  ? 978  ILE B CB    1 
ATOM   18379 C  CG1   . ILE B 2  978  ? 174.778 153.266 129.155 1.00 46.34  ? 978  ILE B CG1   1 
ATOM   18380 C  CG2   . ILE B 2  978  ? 173.462 152.124 127.350 1.00 45.09  ? 978  ILE B CG2   1 
ATOM   18381 C  CD1   . ILE B 2  978  ? 174.064 154.565 128.877 1.00 45.43  ? 978  ILE B CD1   1 
ATOM   18382 N  N     . PHE B 2  979  ? 170.646 151.252 128.832 1.00 46.71  ? 979  PHE B N     1 
ATOM   18383 C  CA    . PHE B 2  979  ? 169.624 150.407 128.236 1.00 45.29  ? 979  PHE B CA    1 
ATOM   18384 C  C     . PHE B 2  979  ? 169.046 151.104 127.013 1.00 45.14  ? 979  PHE B C     1 
ATOM   18385 O  O     . PHE B 2  979  ? 168.864 152.323 127.002 1.00 46.34  ? 979  PHE B O     1 
ATOM   18386 C  CB    . PHE B 2  979  ? 168.523 150.075 129.252 1.00 44.15  ? 979  PHE B CB    1 
ATOM   18387 C  CG    . PHE B 2  979  ? 167.720 151.262 129.691 1.00 46.28  ? 979  PHE B CG    1 
ATOM   18388 C  CD1   . PHE B 2  979  ? 168.225 152.156 130.612 1.00 44.54  ? 979  PHE B CD1   1 
ATOM   18389 C  CD2   . PHE B 2  979  ? 166.438 151.461 129.208 1.00 48.73  ? 979  PHE B CD2   1 
ATOM   18390 C  CE1   . PHE B 2  979  ? 167.481 153.245 131.015 1.00 45.42  ? 979  PHE B CE1   1 
ATOM   18391 C  CE2   . PHE B 2  979  ? 165.686 152.543 129.615 1.00 45.99  ? 979  PHE B CE2   1 
ATOM   18392 C  CZ    . PHE B 2  979  ? 166.209 153.434 130.520 1.00 45.60  ? 979  PHE B CZ    1 
ATOM   18393 N  N     . GLY B 2  980  ? 168.769 150.316 125.976 1.00 41.81  ? 980  GLY B N     1 
ATOM   18394 C  CA    . GLY B 2  980  ? 168.241 150.867 124.738 1.00 39.73  ? 980  GLY B CA    1 
ATOM   18395 C  C     . GLY B 2  980  ? 166.757 151.158 124.849 1.00 40.90  ? 980  GLY B C     1 
ATOM   18396 O  O     . GLY B 2  980  ? 166.002 150.383 125.442 1.00 41.71  ? 980  GLY B O     1 
ATOM   18397 N  N     . LEU B 2  981  ? 166.337 152.283 124.275 1.00 42.73  ? 981  LEU B N     1 
ATOM   18398 C  CA    . LEU B 2  981  ? 164.947 152.723 124.306 1.00 42.60  ? 981  LEU B CA    1 
ATOM   18399 C  C     . LEU B 2  981  ? 164.529 153.101 122.894 1.00 43.25  ? 981  LEU B C     1 
ATOM   18400 O  O     . LEU B 2  981  ? 164.976 154.125 122.367 1.00 42.22  ? 981  LEU B O     1 
ATOM   18401 C  CB    . LEU B 2  981  ? 164.772 153.907 125.260 1.00 43.01  ? 981  LEU B CB    1 
ATOM   18402 C  CG    . LEU B 2  981  ? 163.379 154.490 125.472 1.00 41.61  ? 981  LEU B CG    1 
ATOM   18403 C  CD1   . LEU B 2  981  ? 162.492 153.503 126.194 1.00 42.09  ? 981  LEU B CD1   1 
ATOM   18404 C  CD2   . LEU B 2  981  ? 163.472 155.783 126.248 1.00 42.34  ? 981  LEU B CD2   1 
ATOM   18405 N  N     . MET B 2  982  ? 163.673 152.282 122.290 1.00 44.66  ? 982  MET B N     1 
ATOM   18406 C  CA    . MET B 2  982  ? 163.229 152.455 120.913 1.00 40.85  ? 982  MET B CA    1 
ATOM   18407 C  C     . MET B 2  982  ? 161.760 152.851 120.901 1.00 43.06  ? 982  MET B C     1 
ATOM   18408 O  O     . MET B 2  982  ? 160.963 152.303 121.667 1.00 42.24  ? 982  MET B O     1 
ATOM   18409 C  CB    . MET B 2  982  ? 163.415 151.165 120.114 1.00 41.53  ? 982  MET B CB    1 
ATOM   18410 C  CG    . MET B 2  982  ? 163.379 151.326 118.605 1.00 42.14  ? 982  MET B CG    1 
ATOM   18411 S  SD    . MET B 2  982  ? 164.384 150.087 117.759 1.00 53.28  ? 982  MET B SD    1 
ATOM   18412 C  CE    . MET B 2  982  ? 165.610 151.098 116.950 1.00 39.94  ? 982  MET B CE    1 
ATOM   18413 N  N     . ARG B 2  983  ? 161.404 153.793 120.034 1.00 40.40  ? 983  ARG B N     1 
ATOM   18414 C  CA    . ARG B 2  983  ? 160.011 154.107 119.748 1.00 36.16  ? 983  ARG B CA    1 
ATOM   18415 C  C     . ARG B 2  983  ? 159.726 153.816 118.282 1.00 36.11  ? 983  ARG B C     1 
ATOM   18416 O  O     . ARG B 2  983  ? 160.414 154.334 117.397 1.00 35.15  ? 983  ARG B O     1 
ATOM   18417 C  CB    . ARG B 2  983  ? 159.684 155.561 120.071 1.00 34.17  ? 983  ARG B CB    1 
ATOM   18418 C  CG    . ARG B 2  983  ? 158.195 155.838 120.101 1.00 36.56  ? 983  ARG B CG    1 
ATOM   18419 C  CD    . ARG B 2  983  ? 157.897 157.217 120.630 1.00 36.28  ? 983  ARG B CD    1 
ATOM   18420 N  NE    . ARG B 2  983  ? 158.346 158.255 119.712 1.00 37.92  ? 983  ARG B NE    1 
ATOM   18421 C  CZ    . ARG B 2  983  ? 158.589 159.507 120.067 1.00 39.08  ? 983  ARG B CZ    1 
ATOM   18422 N  NH1   . ARG B 2  983  ? 158.451 159.907 121.320 1.00 37.88  ? 983  ARG B NH1   1 
ATOM   18423 N  NH2   . ARG B 2  983  ? 158.987 160.377 119.145 1.00 38.51  ? 983  ARG B NH2   1 
ATOM   18424 N  N     . LEU B 2  984  ? 158.707 153.001 118.033 1.00 30.59  ? 984  LEU B N     1 
ATOM   18425 C  CA    . LEU B 2  984  ? 158.221 152.708 116.693 1.00 31.12  ? 984  LEU B CA    1 
ATOM   18426 C  C     . LEU B 2  984  ? 156.889 153.417 116.497 1.00 29.89  ? 984  LEU B C     1 
ATOM   18427 O  O     . LEU B 2  984  ? 156.099 153.523 117.438 1.00 29.50  ? 984  LEU B O     1 
ATOM   18428 C  CB    . LEU B 2  984  ? 158.047 151.204 116.495 1.00 32.97  ? 984  LEU B CB    1 
ATOM   18429 C  CG    . LEU B 2  984  ? 159.254 150.302 116.728 1.00 33.42  ? 984  LEU B CG    1 
ATOM   18430 C  CD1   . LEU B 2  984  ? 158.788 148.866 116.793 1.00 30.14  ? 984  LEU B CD1   1 
ATOM   18431 C  CD2   . LEU B 2  984  ? 160.291 150.480 115.636 1.00 29.59  ? 984  LEU B CD2   1 
ATOM   18432 N  N     . ARG B 2  985  ? 156.643 153.908 115.287 1.00 21.97  ? 985  ARG B N     1 
ATOM   18433 C  CA    . ARG B 2  985  ? 155.407 154.611 114.982 1.00 24.70  ? 985  ARG B CA    1 
ATOM   18434 C  C     . ARG B 2  985  ? 154.705 153.984 113.785 1.00 23.97  ? 985  ARG B C     1 
ATOM   18435 O  O     . ARG B 2  985  ? 155.338 153.416 112.894 1.00 22.12  ? 985  ARG B O     1 
ATOM   18436 C  CB    . ARG B 2  985  ? 155.670 156.089 114.711 1.00 19.47  ? 985  ARG B CB    1 
ATOM   18437 C  CG    . ARG B 2  985  ? 156.387 156.336 113.427 1.00 20.30  ? 985  ARG B CG    1 
ATOM   18438 C  CD    . ARG B 2  985  ? 156.411 157.792 113.070 1.00 24.28  ? 985  ARG B CD    1 
ATOM   18439 N  NE    . ARG B 2  985  ? 156.805 157.949 111.680 1.00 27.36  ? 985  ARG B NE    1 
ATOM   18440 C  CZ    . ARG B 2  985  ? 157.835 158.669 111.268 1.00 23.64  ? 985  ARG B CZ    1 
ATOM   18441 N  NH1   . ARG B 2  985  ? 158.614 159.309 112.120 1.00 22.44  ? 985  ARG B NH1   1 
ATOM   18442 N  NH2   . ARG B 2  985  ? 158.100 158.734 109.969 1.00 26.12  ? 985  ARG B NH2   1 
ATOM   18443 N  N     . TYR B 2  986  ? 153.382 154.096 113.775 1.00 22.98  ? 986  TYR B N     1 
ATOM   18444 C  CA    . TYR B 2  986  ? 152.552 153.540 112.719 1.00 18.63  ? 986  TYR B CA    1 
ATOM   18445 C  C     . TYR B 2  986  ? 151.626 154.612 112.166 1.00 19.15  ? 986  TYR B C     1 
ATOM   18446 O  O     . TYR B 2  986  ? 151.160 155.480 112.901 1.00 18.27  ? 986  TYR B O     1 
ATOM   18447 C  CB    . TYR B 2  986  ? 151.733 152.364 113.233 1.00 19.80  ? 986  TYR B CB    1 
ATOM   18448 C  CG    . TYR B 2  986  ? 152.571 151.253 113.809 1.00 23.49  ? 986  TYR B CG    1 
ATOM   18449 C  CD1   . TYR B 2  986  ? 152.975 151.278 115.131 1.00 21.65  ? 986  TYR B CD1   1 
ATOM   18450 C  CD2   . TYR B 2  986  ? 152.966 150.182 113.028 1.00 25.78  ? 986  TYR B CD2   1 
ATOM   18451 C  CE1   . TYR B 2  986  ? 153.744 150.271 115.654 1.00 22.37  ? 986  TYR B CE1   1 
ATOM   18452 C  CE2   . TYR B 2  986  ? 153.728 149.171 113.547 1.00 23.13  ? 986  TYR B CE2   1 
ATOM   18453 C  CZ    . TYR B 2  986  ? 154.115 149.219 114.856 1.00 23.33  ? 986  TYR B CZ    1 
ATOM   18454 O  OH    . TYR B 2  986  ? 154.878 148.201 115.366 1.00 23.59  ? 986  TYR B OH    1 
ATOM   18455 N  N     . GLU B 2  987  ? 151.371 154.542 110.865 1.00 24.01  ? 987  GLU B N     1 
ATOM   18456 C  CA    . GLU B 2  987  ? 150.415 155.411 110.180 1.00 13.03  ? 987  GLU B CA    1 
ATOM   18457 C  C     . GLU B 2  987  ? 149.091 154.667 110.117 1.00 17.43  ? 987  GLU B C     1 
ATOM   18458 O  O     . GLU B 2  987  ? 148.984 153.634 109.459 1.00 26.00  ? 987  GLU B O     1 
ATOM   18459 C  CB    . GLU B 2  987  ? 150.919 155.749 108.785 1.00 13.36  ? 987  GLU B CB    1 
ATOM   18460 C  CG    . GLU B 2  987  ? 151.516 157.121 108.629 1.00 18.98  ? 987  GLU B CG    1 
ATOM   18461 C  CD    . GLU B 2  987  ? 152.911 157.234 109.196 1.00 25.94  ? 987  GLU B CD    1 
ATOM   18462 O  OE1   . GLU B 2  987  ? 153.082 157.903 110.232 1.00 27.03  ? 987  GLU B OE1   1 
ATOM   18463 O  OE2   . GLU B 2  987  ? 153.843 156.660 108.603 1.00 29.93  ? 987  GLU B OE2   1 
ATOM   18464 N  N     . ARG B 2  988  ? 148.076 155.172 110.808 1.00 13.02  ? 988  ARG B N     1 
ATOM   18465 C  CA    . ARG B 2  988  ? 146.789 154.490 110.912 1.00 10.03  ? 988  ARG B CA    1 
ATOM   18466 C  C     . ARG B 2  988  ? 145.679 155.349 110.316 1.00 10.90  ? 988  ARG B C     1 
ATOM   18467 O  O     . ARG B 2  988  ? 145.247 156.327 110.926 1.00 14.18  ? 988  ARG B O     1 
ATOM   18468 C  CB    . ARG B 2  988  ? 146.482 154.144 112.364 1.00 12.16  ? 988  ARG B CB    1 
ATOM   18469 C  CG    . ARG B 2  988  ? 147.339 153.035 112.916 1.00 16.36  ? 988  ARG B CG    1 
ATOM   18470 C  CD    . ARG B 2  988  ? 146.835 151.678 112.477 1.00 19.15  ? 988  ARG B CD    1 
ATOM   18471 N  NE    . ARG B 2  988  ? 147.703 150.587 112.900 1.00 15.92  ? 988  ARG B NE    1 
ATOM   18472 C  CZ    . ARG B 2  988  ? 147.673 150.019 114.097 1.00 21.44  ? 988  ARG B CZ    1 
ATOM   18473 N  NH1   . ARG B 2  988  ? 146.838 150.426 115.034 1.00 16.43  ? 988  ARG B NH1   1 
ATOM   18474 N  NH2   . ARG B 2  988  ? 148.505 149.020 114.360 1.00 20.95  ? 988  ARG B NH2   1 
ATOM   18475 N  N     . ASN B 2  989  ? 145.214 154.977 109.134 1.00 10.07  ? 989  ASN B N     1 
ATOM   18476 C  CA    . ASN B 2  989  ? 143.933 155.444 108.641 1.00 4.72   ? 989  ASN B CA    1 
ATOM   18477 C  C     . ASN B 2  989  ? 142.819 154.576 109.211 1.00 6.77   ? 989  ASN B C     1 
ATOM   18478 O  O     . ASN B 2  989  ? 143.058 153.511 109.776 1.00 19.66  ? 989  ASN B O     1 
ATOM   18479 C  CB    . ASN B 2  989  ? 143.889 155.392 107.118 1.00 3.90   ? 989  ASN B CB    1 
ATOM   18480 C  CG    . ASN B 2  989  ? 144.787 156.398 106.473 1.00 9.26   ? 989  ASN B CG    1 
ATOM   18481 O  OD1   . ASN B 2  989  ? 145.903 156.078 106.085 1.00 22.02  ? 989  ASN B OD1   1 
ATOM   18482 N  ND2   . ASN B 2  989  ? 144.303 157.617 106.327 1.00 7.88   ? 989  ASN B ND2   1 
ATOM   18483 N  N     . LEU B 2  990  ? 141.586 155.032 109.061 1.00 8.98   ? 990  LEU B N     1 
ATOM   18484 C  CA    . LEU B 2  990  ? 140.457 154.154 109.320 1.00 3.54   ? 990  LEU B CA    1 
ATOM   18485 C  C     . LEU B 2  990  ? 140.408 153.072 108.255 1.00 4.39   ? 990  LEU B C     1 
ATOM   18486 O  O     . LEU B 2  990  ? 140.614 153.342 107.072 1.00 15.40  ? 990  LEU B O     1 
ATOM   18487 C  CB    . LEU B 2  990  ? 139.160 154.951 109.335 1.00 5.64   ? 990  LEU B CB    1 
ATOM   18488 C  CG    . LEU B 2  990  ? 137.881 154.238 109.753 1.00 5.39   ? 990  LEU B CG    1 
ATOM   18489 C  CD1   . LEU B 2  990  ? 137.771 154.195 111.253 1.00 2.81   ? 990  LEU B CD1   1 
ATOM   18490 C  CD2   . LEU B 2  990  ? 136.698 154.942 109.159 1.00 3.78   ? 990  LEU B CD2   1 
ATOM   18491 N  N     . ASN B 2  991  ? 140.163 151.832 108.661 1.00 3.18   ? 991  ASN B N     1 
ATOM   18492 C  CA    . ASN B 2  991  ? 140.101 150.775 107.667 1.00 7.94   ? 991  ASN B CA    1 
ATOM   18493 C  C     . ASN B 2  991  ? 139.001 149.792 108.023 1.00 4.08   ? 991  ASN B C     1 
ATOM   18494 O  O     . ASN B 2  991  ? 138.430 149.832 109.111 1.00 14.14  ? 991  ASN B O     1 
ATOM   18495 C  CB    . ASN B 2  991  ? 141.458 150.092 107.492 1.00 11.87  ? 991  ASN B CB    1 
ATOM   18496 C  CG    . ASN B 2  991  ? 142.087 149.702 108.787 1.00 15.70  ? 991  ASN B CG    1 
ATOM   18497 O  OD1   . ASN B 2  991  ? 141.404 149.391 109.752 1.00 21.64  ? 991  ASN B OD1   1 
ATOM   18498 N  ND2   . ASN B 2  991  ? 143.408 149.740 108.827 1.00 8.82   ? 991  ASN B ND2   1 
ATOM   18499 N  N     . ILE B 2  992  ? 138.690 148.925 107.067 1.00 2.27   ? 992  ILE B N     1 
ATOM   18500 C  CA    . ILE B 2  992  ? 137.607 147.965 107.214 1.00 15.46  ? 992  ILE B CA    1 
ATOM   18501 C  C     . ILE B 2  992  ? 137.902 147.065 108.402 1.00 4.99   ? 992  ILE B C     1 
ATOM   18502 O  O     . ILE B 2  992  ? 138.955 146.426 108.473 1.00 19.85  ? 992  ILE B O     1 
ATOM   18503 C  CB    . ILE B 2  992  ? 137.421 147.160 105.923 1.00 3.27   ? 992  ILE B CB    1 
ATOM   18504 C  CG1   . ILE B 2  992  ? 136.971 148.080 104.788 1.00 2.22   ? 992  ILE B CG1   1 
ATOM   18505 C  CG2   . ILE B 2  992  ? 136.486 145.984 106.130 1.00 1.06   ? 992  ILE B CG2   1 
ATOM   18506 C  CD1   . ILE B 2  992  ? 135.941 149.078 105.181 1.00 3.17   ? 992  ILE B CD1   1 
ATOM   18507 N  N     . GLY B 2  993  ? 136.970 147.012 109.340 1.00 14.24  ? 993  GLY B N     1 
ATOM   18508 C  CA    . GLY B 2  993  ? 137.129 146.251 110.554 1.00 9.17   ? 993  GLY B CA    1 
ATOM   18509 C  C     . GLY B 2  993  ? 137.362 147.082 111.782 1.00 0.56   ? 993  GLY B C     1 
ATOM   18510 O  O     . GLY B 2  993  ? 137.492 146.512 112.868 1.00 8.50   ? 993  GLY B O     1 
ATOM   18511 N  N     . ASP B 2  994  ? 137.424 148.403 111.652 1.00 4.39   ? 994  ASP B N     1 
ATOM   18512 C  CA    . ASP B 2  994  ? 137.597 149.299 112.785 1.00 2.11   ? 994  ASP B CA    1 
ATOM   18513 C  C     . ASP B 2  994  ? 136.248 149.691 113.374 1.00 1.82   ? 994  ASP B C     1 
ATOM   18514 O  O     . ASP B 2  994  ? 135.234 149.696 112.682 1.00 10.12  ? 994  ASP B O     1 
ATOM   18515 C  CB    . ASP B 2  994  ? 138.378 150.546 112.372 1.00 4.91   ? 994  ASP B CB    1 
ATOM   18516 C  CG    . ASP B 2  994  ? 139.883 150.329 112.392 1.00 15.18  ? 994  ASP B CG    1 
ATOM   18517 O  OD1   . ASP B 2  994  ? 140.324 149.239 112.795 1.00 13.97  ? 994  ASP B OD1   1 
ATOM   18518 O  OD2   . ASP B 2  994  ? 140.630 151.257 112.039 1.00 12.11  ? 994  ASP B OD2   1 
ATOM   18519 N  N     . LYS B 2  995  ? 136.248 150.029 114.655 1.00 3.47   ? 995  LYS B N     1 
ATOM   18520 C  CA    . LYS B 2  995  ? 135.021 150.243 115.404 1.00 1.02   ? 995  LYS B CA    1 
ATOM   18521 C  C     . LYS B 2  995  ? 134.792 151.726 115.653 1.00 2.41   ? 995  LYS B C     1 
ATOM   18522 O  O     . LYS B 2  995  ? 135.673 152.421 116.156 1.00 8.50   ? 995  LYS B O     1 
ATOM   18523 C  CB    . LYS B 2  995  ? 135.075 149.498 116.733 1.00 3.02   ? 995  LYS B CB    1 
ATOM   18524 C  CG    . LYS B 2  995  ? 133.752 148.954 117.184 1.00 12.95  ? 995  LYS B CG    1 
ATOM   18525 C  CD    . LYS B 2  995  ? 133.836 148.381 118.570 1.00 12.38  ? 995  LYS B CD    1 
ATOM   18526 C  CE    . LYS B 2  995  ? 134.873 147.294 118.650 1.00 16.66  ? 995  LYS B CE    1 
ATOM   18527 N  NZ    . LYS B 2  995  ? 134.903 146.686 120.001 1.00 21.51  ? 995  LYS B NZ    1 
ATOM   18528 N  N     . MET B 2  996  ? 133.606 152.203 115.301 1.00 4.82   ? 996  MET B N     1 
ATOM   18529 C  CA    . MET B 2  996  ? 133.158 153.550 115.608 1.00 3.35   ? 996  MET B CA    1 
ATOM   18530 C  C     . MET B 2  996  ? 131.946 153.500 116.520 1.00 2.74   ? 996  MET B C     1 
ATOM   18531 O  O     . MET B 2  996  ? 131.389 152.442 116.792 1.00 8.89   ? 996  MET B O     1 
ATOM   18532 C  CB    . MET B 2  996  ? 132.832 154.341 114.339 1.00 3.43   ? 996  MET B CB    1 
ATOM   18533 C  CG    . MET B 2  996  ? 134.003 154.541 113.413 1.00 7.12   ? 996  MET B CG    1 
ATOM   18534 S  SD    . MET B 2  996  ? 133.488 154.671 111.705 1.00 37.28  ? 996  MET B SD    1 
ATOM   18535 C  CE    . MET B 2  996  ? 133.483 152.945 111.302 1.00 13.46  ? 996  MET B CE    1 
ATOM   18536 N  N     . SER B 2  997  ? 131.549 154.669 117.001 1.00 1.29   ? 997  SER B N     1 
ATOM   18537 C  CA    . SER B 2  997  ? 130.442 154.754 117.934 1.00 2.04   ? 997  SER B CA    1 
ATOM   18538 C  C     . SER B 2  997  ? 129.952 156.188 117.997 1.00 1.65   ? 997  SER B C     1 
ATOM   18539 O  O     . SER B 2  997  ? 130.725 157.117 117.792 1.00 8.25   ? 997  SER B O     1 
ATOM   18540 C  CB    . SER B 2  997  ? 130.872 154.277 119.323 1.00 11.62  ? 997  SER B CB    1 
ATOM   18541 O  OG    . SER B 2  997  ? 129.817 154.357 120.248 1.00 20.56  ? 997  SER B OG    1 
ATOM   18542 N  N     . SER B 2  998  ? 128.677 156.359 118.302 1.00 0.54   ? 998  SER B N     1 
ATOM   18543 C  CA    . SER B 2  998  ? 128.143 157.666 118.637 1.00 1.40   ? 998  SER B CA    1 
ATOM   18544 C  C     . SER B 2  998  ? 128.055 157.815 120.154 1.00 9.79   ? 998  SER B C     1 
ATOM   18545 O  O     . SER B 2  998  ? 128.380 156.905 120.914 1.00 20.18  ? 998  SER B O     1 
ATOM   18546 C  CB    . SER B 2  998  ? 126.780 157.869 117.990 1.00 2.93   ? 998  SER B CB    1 
ATOM   18547 O  OG    . SER B 2  998  ? 125.871 156.899 118.443 1.00 8.12   ? 998  SER B OG    1 
ATOM   18548 N  N     . ARG B 2  999  ? 127.608 158.984 120.599 1.00 6.62   ? 999  ARG B N     1 
ATOM   18549 C  CA    . ARG B 2  999  ? 127.593 159.263 122.025 1.00 7.47   ? 999  ARG B CA    1 
ATOM   18550 C  C     . ARG B 2  999  ? 126.432 158.595 122.749 1.00 9.81   ? 999  ARG B C     1 
ATOM   18551 O  O     . ARG B 2  999  ? 126.353 158.696 123.970 1.00 16.55  ? 999  ARG B O     1 
ATOM   18552 C  CB    . ARG B 2  999  ? 127.561 160.773 122.263 1.00 4.06   ? 999  ARG B CB    1 
ATOM   18553 C  CG    . ARG B 2  999  ? 128.828 161.491 121.906 1.00 3.59   ? 999  ARG B CG    1 
ATOM   18554 C  CD    . ARG B 2  999  ? 128.684 162.979 122.071 1.00 3.79   ? 999  ARG B CD    1 
ATOM   18555 N  NE    . ARG B 2  999  ? 127.803 163.559 121.070 1.00 3.41   ? 999  ARG B NE    1 
ATOM   18556 C  CZ    . ARG B 2  999  ? 127.359 164.806 121.098 1.00 4.01   ? 999  ARG B CZ    1 
ATOM   18557 N  NH1   . ARG B 2  999  ? 127.675 165.629 122.077 1.00 8.58   ? 999  ARG B NH1   1 
ATOM   18558 N  NH2   . ARG B 2  999  ? 126.575 165.236 120.121 1.00 4.70   ? 999  ARG B NH2   1 
ATOM   18559 N  N     . SER B 2  1000 ? 125.532 157.928 122.043 1.00 7.00   ? 1000 SER B N     1 
ATOM   18560 C  CA    . SER B 2  1000 ? 124.473 157.155 122.672 1.00 9.46   ? 1000 SER B CA    1 
ATOM   18561 C  C     . SER B 2  1000 ? 124.821 155.688 122.840 1.00 16.38  ? 1000 SER B C     1 
ATOM   18562 O  O     . SER B 2  1000 ? 123.950 154.904 123.217 1.00 23.66  ? 1000 SER B O     1 
ATOM   18563 C  CB    . SER B 2  1000 ? 123.178 157.268 121.873 1.00 12.44  ? 1000 SER B CB    1 
ATOM   18564 O  OG    . SER B 2  1000 ? 122.605 158.542 122.045 1.00 24.11  ? 1000 SER B OG    1 
ATOM   18565 N  N     . GLY B 2  1001 ? 126.056 155.295 122.563 1.00 17.42  ? 1001 GLY B N     1 
ATOM   18566 C  CA    . GLY B 2  1001 ? 126.469 153.926 122.762 1.00 19.02  ? 1001 GLY B CA    1 
ATOM   18567 C  C     . GLY B 2  1001 ? 126.208 152.999 121.606 1.00 24.87  ? 1001 GLY B C     1 
ATOM   18568 O  O     . GLY B 2  1001 ? 126.291 151.781 121.781 1.00 24.77  ? 1001 GLY B O     1 
ATOM   18569 N  N     . ASN B 2  1002 ? 125.905 153.536 120.429 1.00 26.58  ? 1002 ASN B N     1 
ATOM   18570 C  CA    . ASN B 2  1002 ? 125.602 152.757 119.230 1.00 19.14  ? 1002 ASN B CA    1 
ATOM   18571 C  C     . ASN B 2  1002 ? 126.902 152.496 118.484 1.00 18.19  ? 1002 ASN B C     1 
ATOM   18572 O  O     . ASN B 2  1002 ? 127.367 153.327 117.711 1.00 26.17  ? 1002 ASN B O     1 
ATOM   18573 C  CB    . ASN B 2  1002 ? 124.609 153.519 118.366 1.00 19.53  ? 1002 ASN B CB    1 
ATOM   18574 C  CG    . ASN B 2  1002 ? 123.499 152.651 117.843 1.00 26.56  ? 1002 ASN B CG    1 
ATOM   18575 O  OD1   . ASN B 2  1002 ? 122.786 152.009 118.608 1.00 25.49  ? 1002 ASN B OD1   1 
ATOM   18576 N  ND2   . ASN B 2  1002 ? 123.336 152.633 116.528 1.00 25.01  ? 1002 ASN B ND2   1 
ATOM   18577 N  N     . LYS B 2  1003 ? 127.491 151.326 118.699 1.00 10.80  ? 1003 LYS B N     1 
ATOM   18578 C  CA    . LYS B 2  1003 ? 128.797 151.019 118.135 1.00 13.94  ? 1003 LYS B CA    1 
ATOM   18579 C  C     . LYS B 2  1003 ? 128.702 149.993 117.014 1.00 16.58  ? 1003 LYS B C     1 
ATOM   18580 O  O     . LYS B 2  1003 ? 127.819 149.138 117.004 1.00 30.41  ? 1003 LYS B O     1 
ATOM   18581 C  CB    . LYS B 2  1003 ? 129.750 150.519 119.221 1.00 16.29  ? 1003 LYS B CB    1 
ATOM   18582 C  CG    . LYS B 2  1003 ? 129.464 149.140 119.744 1.00 15.93  ? 1003 LYS B CG    1 
ATOM   18583 C  CD    . LYS B 2  1003 ? 130.597 148.664 120.631 1.00 24.83  ? 1003 LYS B CD    1 
ATOM   18584 C  CE    . LYS B 2  1003 ? 130.408 147.223 121.070 1.00 26.32  ? 1003 LYS B CE    1 
ATOM   18585 N  NZ    . LYS B 2  1003 ? 129.258 147.048 121.994 1.00 21.14  ? 1003 LYS B NZ    1 
ATOM   18586 N  N     . GLY B 2  1004 ? 129.629 150.080 116.066 1.00 11.45  ? 1004 GLY B N     1 
ATOM   18587 C  CA    . GLY B 2  1004 ? 129.592 149.214 114.905 1.00 0.98   ? 1004 GLY B CA    1 
ATOM   18588 C  C     . GLY B 2  1004 ? 130.932 149.117 114.219 1.00 3.19   ? 1004 GLY B C     1 
ATOM   18589 O  O     . GLY B 2  1004 ? 131.854 149.877 114.511 1.00 9.93   ? 1004 GLY B O     1 
ATOM   18590 N  N     . ILE B 2  1005 ? 131.025 148.186 113.278 1.00 0.47   ? 1005 ILE B N     1 
ATOM   18591 C  CA    . ILE B 2  1005 ? 132.256 147.888 112.557 1.00 0.65   ? 1005 ILE B CA    1 
ATOM   18592 C  C     . ILE B 2  1005 ? 132.147 148.455 111.149 1.00 3.01   ? 1005 ILE B C     1 
ATOM   18593 O  O     . ILE B 2  1005 ? 131.098 148.349 110.512 1.00 8.08   ? 1005 ILE B O     1 
ATOM   18594 C  CB    . ILE B 2  1005 ? 132.511 146.368 112.526 1.00 0.13   ? 1005 ILE B CB    1 
ATOM   18595 C  CG1   . ILE B 2  1005 ? 133.028 145.870 113.871 1.00 7.83   ? 1005 ILE B CG1   1 
ATOM   18596 C  CG2   . ILE B 2  1005 ? 133.448 145.967 111.421 1.00 9.71   ? 1005 ILE B CG2   1 
ATOM   18597 C  CD1   . ILE B 2  1005 ? 134.346 146.399 114.255 1.00 6.82   ? 1005 ILE B CD1   1 
ATOM   18598 N  N     . ALA B 2  1006 ? 133.223 149.070 110.666 1.00 15.33  ? 1006 ALA B N     1 
ATOM   18599 C  CA    . ALA B 2  1006 ? 133.293 149.489 109.273 1.00 13.39  ? 1006 ALA B CA    1 
ATOM   18600 C  C     . ALA B 2  1006 ? 133.392 148.275 108.363 1.00 1.98   ? 1006 ALA B C     1 
ATOM   18601 O  O     . ALA B 2  1006 ? 134.354 147.511 108.439 1.00 13.71  ? 1006 ALA B O     1 
ATOM   18602 C  CB    . ALA B 2  1006 ? 134.489 150.404 109.062 1.00 15.10  ? 1006 ALA B CB    1 
ATOM   18603 N  N     . ALA B 2  1007 ? 132.407 148.099 107.493 1.00 15.19  ? 1007 ALA B N     1 
ATOM   18604 C  CA    . ALA B 2  1007 ? 132.322 146.903 106.670 1.00 5.03   ? 1007 ALA B CA    1 
ATOM   18605 C  C     . ALA B 2  1007 ? 132.632 147.145 105.204 1.00 3.92   ? 1007 ALA B C     1 
ATOM   18606 O  O     . ALA B 2  1007 ? 133.168 146.257 104.543 1.00 6.85   ? 1007 ALA B O     1 
ATOM   18607 C  CB    . ALA B 2  1007 ? 130.929 146.285 106.789 1.00 0.79   ? 1007 ALA B CB    1 
ATOM   18608 N  N     . LEU B 2  1008 ? 132.308 148.317 104.681 1.00 8.15   ? 1008 LEU B N     1 
ATOM   18609 C  CA    . LEU B 2  1008 ? 132.499 148.635 103.281 1.00 10.99  ? 1008 LEU B CA    1 
ATOM   18610 C  C     . LEU B 2  1008 ? 132.909 150.091 103.181 1.00 3.73   ? 1008 LEU B C     1 
ATOM   18611 O  O     . LEU B 2  1008 ? 132.474 150.915 103.979 1.00 5.48   ? 1008 LEU B O     1 
ATOM   18612 C  CB    . LEU B 2  1008 ? 131.221 148.375 102.483 1.00 6.36   ? 1008 LEU B CB    1 
ATOM   18613 C  CG    . LEU B 2  1008 ? 131.247 148.554 100.972 1.00 8.50   ? 1008 LEU B CG    1 
ATOM   18614 C  CD1   . LEU B 2  1008 ? 131.926 147.397 100.318 1.00 13.47  ? 1008 LEU B CD1   1 
ATOM   18615 C  CD2   . LEU B 2  1008 ? 129.854 148.724 100.451 1.00 13.15  ? 1008 LEU B CD2   1 
ATOM   18616 N  N     . ALA B 2  1009 ? 133.772 150.397 102.217 1.00 11.59  ? 1009 ALA B N     1 
ATOM   18617 C  CA    . ALA B 2  1009 ? 134.150 151.769 101.905 1.00 5.90   ? 1009 ALA B CA    1 
ATOM   18618 C  C     . ALA B 2  1009 ? 133.907 152.018 100.428 1.00 9.95   ? 1009 ALA B C     1 
ATOM   18619 O  O     . ALA B 2  1009 ? 134.405 151.271 99.586  1.00 16.81  ? 1009 ALA B O     1 
ATOM   18620 C  CB    . ALA B 2  1009 ? 135.607 152.045 102.263 1.00 8.20   ? 1009 ALA B CB    1 
ATOM   18621 N  N     . LEU B 2  1010 ? 133.160 153.065 100.114 1.00 2.80   ? 1010 LEU B N     1 
ATOM   18622 C  CA    . LEU B 2  1010 ? 132.783 153.329 98.742  1.00 10.93  ? 1010 LEU B CA    1 
ATOM   18623 C  C     . LEU B 2  1010 ? 133.452 154.586 98.217  1.00 9.64   ? 1010 LEU B C     1 
ATOM   18624 O  O     . LEU B 2  1010 ? 133.711 155.519 98.977  1.00 5.20   ? 1010 LEU B O     1 
ATOM   18625 C  CB    . LEU B 2  1010 ? 131.270 153.505 98.595  1.00 0.58   ? 1010 LEU B CB    1 
ATOM   18626 C  CG    . LEU B 2  1010 ? 130.363 152.314 98.840  1.00 15.30  ? 1010 LEU B CG    1 
ATOM   18627 C  CD1   . LEU B 2  1010 ? 128.952 152.806 98.974  1.00 12.54  ? 1010 LEU B CD1   1 
ATOM   18628 C  CD2   . LEU B 2  1010 ? 130.493 151.334 97.719  1.00 2.68   ? 1010 LEU B CD2   1 
ATOM   18629 N  N     . PRO B 2  1011 ? 133.741 154.641 96.921  1.00 3.79   ? 1011 PRO B N     1 
ATOM   18630 C  CA    . PRO B 2  1011 ? 134.211 155.888 96.309  1.00 14.72  ? 1011 PRO B CA    1 
ATOM   18631 C  C     . PRO B 2  1011 ? 133.135 156.963 96.313  1.00 1.31   ? 1011 PRO B C     1 
ATOM   18632 O  O     . PRO B 2  1011 ? 131.967 156.721 96.593  1.00 7.04   ? 1011 PRO B O     1 
ATOM   18633 C  CB    . PRO B 2  1011 ? 134.558 155.467 94.884  1.00 10.33  ? 1011 PRO B CB    1 
ATOM   18634 C  CG    . PRO B 2  1011 ? 134.760 154.032 94.959  1.00 4.55   ? 1011 PRO B CG    1 
ATOM   18635 C  CD    . PRO B 2  1011 ? 133.848 153.511 95.991  1.00 1.99   ? 1011 PRO B CD    1 
ATOM   18636 N  N     . THR B 2  1012 ? 133.561 158.178 95.975  1.00 5.49   ? 1012 THR B N     1 
ATOM   18637 C  CA    . THR B 2  1012 ? 132.670 159.333 96.003  1.00 8.33   ? 1012 THR B CA    1 
ATOM   18638 C  C     . THR B 2  1012 ? 131.524 159.182 95.018  1.00 3.99   ? 1012 THR B C     1 
ATOM   18639 O  O     . THR B 2  1012 ? 130.379 159.510 95.333  1.00 11.68  ? 1012 THR B O     1 
ATOM   18640 C  CB    . THR B 2  1012 ? 133.467 160.602 95.710  1.00 1.35   ? 1012 THR B CB    1 
ATOM   18641 O  OG1   . THR B 2  1012 ? 134.402 160.816 96.763  1.00 10.71  ? 1012 THR B OG1   1 
ATOM   18642 C  CG2   . THR B 2  1012 ? 132.575 161.795 95.615  1.00 0.38   ? 1012 THR B CG2   1 
ATOM   18643 N  N     . SER B 2  1013 ? 131.808 158.682 93.824  1.00 8.88   ? 1013 SER B N     1 
ATOM   18644 C  CA    . SER B 2  1013 ? 130.777 158.497 92.821  1.00 15.39  ? 1013 SER B CA    1 
ATOM   18645 C  C     . SER B 2  1013 ? 129.806 157.375 93.159  1.00 5.06   ? 1013 SER B C     1 
ATOM   18646 O  O     . SER B 2  1013 ? 128.779 157.257 92.494  1.00 0.23   ? 1013 SER B O     1 
ATOM   18647 C  CB    . SER B 2  1013 ? 131.420 158.243 91.464  1.00 2.12   ? 1013 SER B CB    1 
ATOM   18648 O  OG    . SER B 2  1013 ? 132.489 157.330 91.574  1.00 11.29  ? 1013 SER B OG    1 
ATOM   18649 N  N     . ASP B 2  1014 ? 130.082 156.572 94.179  1.00 4.42   ? 1014 ASP B N     1 
ATOM   18650 C  CA    . ASP B 2  1014 ? 129.244 155.440 94.533  1.00 9.28   ? 1014 ASP B CA    1 
ATOM   18651 C  C     . ASP B 2  1014 ? 128.333 155.693 95.720  1.00 8.52   ? 1014 ASP B C     1 
ATOM   18652 O  O     . ASP B 2  1014 ? 127.457 154.871 95.979  1.00 4.01   ? 1014 ASP B O     1 
ATOM   18653 C  CB    . ASP B 2  1014 ? 130.109 154.220 94.839  1.00 3.31   ? 1014 ASP B CB    1 
ATOM   18654 C  CG    . ASP B 2  1014 ? 130.626 153.552 93.599  1.00 6.59   ? 1014 ASP B CG    1 
ATOM   18655 O  OD1   . ASP B 2  1014 ? 130.046 153.754 92.522  1.00 14.52  ? 1014 ASP B OD1   1 
ATOM   18656 O  OD2   . ASP B 2  1014 ? 131.613 152.813 93.695  1.00 6.74   ? 1014 ASP B OD2   1 
ATOM   18657 N  N     . MET B 2  1015 ? 128.519 156.779 96.447  1.00 6.18   ? 1015 MET B N     1 
ATOM   18658 C  CA    . MET B 2  1015 ? 127.699 157.088 97.602  1.00 1.27   ? 1015 MET B CA    1 
ATOM   18659 C  C     . MET B 2  1015 ? 126.403 157.780 97.181  1.00 12.05  ? 1015 MET B C     1 
ATOM   18660 O  O     . MET B 2  1015 ? 126.339 158.385 96.113  1.00 5.16   ? 1015 MET B O     1 
ATOM   18661 C  CB    . MET B 2  1015 ? 128.465 157.975 98.581  1.00 0.55   ? 1015 MET B CB    1 
ATOM   18662 C  CG    . MET B 2  1015 ? 129.740 157.370 99.156  1.00 14.84  ? 1015 MET B CG    1 
ATOM   18663 S  SD    . MET B 2  1015 ? 129.470 156.105 100.408 1.00 16.93  ? 1015 MET B SD    1 
ATOM   18664 C  CE    . MET B 2  1015 ? 129.133 157.054 101.875 1.00 9.95   ? 1015 MET B CE    1 
ATOM   18665 N  N     . PRO B 2  1016 ? 125.352 157.689 97.995  1.00 4.63   ? 1016 PRO B N     1 
ATOM   18666 C  CA    . PRO B 2  1016 ? 124.128 158.435 97.703  1.00 3.62   ? 1016 PRO B CA    1 
ATOM   18667 C  C     . PRO B 2  1016 ? 124.324 159.924 97.928  1.00 12.26  ? 1016 PRO B C     1 
ATOM   18668 O  O     . PRO B 2  1016 ? 125.165 160.356 98.710  1.00 2.41   ? 1016 PRO B O     1 
ATOM   18669 C  CB    . PRO B 2  1016 ? 123.117 157.870 98.704  1.00 10.85  ? 1016 PRO B CB    1 
ATOM   18670 C  CG    . PRO B 2  1016 ? 123.788 156.780 99.392  1.00 2.12   ? 1016 PRO B CG    1 
ATOM   18671 C  CD    . PRO B 2  1016 ? 125.236 156.966 99.266  1.00 4.00   ? 1016 PRO B CD    1 
ATOM   18672 N  N     . PHE B 2  1017 ? 123.518 160.714 97.240  1.00 2.05   ? 1017 PHE B N     1 
ATOM   18673 C  CA    . PHE B 2  1017 ? 123.598 162.161 97.338  1.00 4.43   ? 1017 PHE B CA    1 
ATOM   18674 C  C     . PHE B 2  1017 ? 122.199 162.745 97.258  1.00 4.08   ? 1017 PHE B C     1 
ATOM   18675 O  O     . PHE B 2  1017 ? 121.300 162.129 96.692  1.00 7.59   ? 1017 PHE B O     1 
ATOM   18676 C  CB    . PHE B 2  1017 ? 124.508 162.744 96.240  1.00 12.87  ? 1017 PHE B CB    1 
ATOM   18677 C  CG    . PHE B 2  1017 ? 124.079 162.411 94.844  1.00 2.35   ? 1017 PHE B CG    1 
ATOM   18678 C  CD1   . PHE B 2  1017 ? 124.333 161.168 94.306  1.00 2.78   ? 1017 PHE B CD1   1 
ATOM   18679 C  CD2   . PHE B 2  1017 ? 123.440 163.345 94.067  1.00 0.81   ? 1017 PHE B CD2   1 
ATOM   18680 C  CE1   . PHE B 2  1017 ? 123.939 160.863 93.042  1.00 5.32   ? 1017 PHE B CE1   1 
ATOM   18681 C  CE2   . PHE B 2  1017 ? 123.047 163.042 92.803  1.00 7.05   ? 1017 PHE B CE2   1 
ATOM   18682 C  CZ    . PHE B 2  1017 ? 123.301 161.800 92.287  1.00 13.91  ? 1017 PHE B CZ    1 
ATOM   18683 N  N     . THR B 2  1018 ? 122.013 163.925 97.836  1.00 9.46   ? 1018 THR B N     1 
ATOM   18684 C  CA    . THR B 2  1018 ? 120.710 164.562 97.800  1.00 2.68   ? 1018 THR B CA    1 
ATOM   18685 C  C     . THR B 2  1018 ? 120.611 165.481 96.588  1.00 2.14   ? 1018 THR B C     1 
ATOM   18686 O  O     . THR B 2  1018 ? 121.531 165.597 95.785  1.00 13.65  ? 1018 THR B O     1 
ATOM   18687 C  CB    . THR B 2  1018 ? 120.436 165.321 99.097  1.00 3.64   ? 1018 THR B CB    1 
ATOM   18688 O  OG1   . THR B 2  1018 ? 121.213 166.513 99.135  1.00 6.13   ? 1018 THR B OG1   1 
ATOM   18689 C  CG2   . THR B 2  1018 ? 120.783 164.490 100.292 1.00 1.87   ? 1018 THR B CG2   1 
ATOM   18690 N  N     . GLU B 2  1019 ? 119.466 166.141 96.451  1.00 1.30   ? 1019 GLU B N     1 
ATOM   18691 C  CA    . GLU B 2  1019 ? 119.250 167.032 95.320  1.00 2.96   ? 1019 GLU B CA    1 
ATOM   18692 C  C     . GLU B 2  1019 ? 120.212 168.211 95.324  1.00 8.22   ? 1019 GLU B C     1 
ATOM   18693 O  O     . GLU B 2  1019 ? 120.506 168.767 94.265  1.00 6.85   ? 1019 GLU B O     1 
ATOM   18694 C  CB    . GLU B 2  1019 ? 117.813 167.533 95.329  1.00 15.59  ? 1019 GLU B CB    1 
ATOM   18695 C  CG    . GLU B 2  1019 ? 117.397 168.212 94.055  1.00 3.55   ? 1019 GLU B CG    1 
ATOM   18696 C  CD    . GLU B 2  1019 ? 116.057 168.887 94.176  1.00 10.06  ? 1019 GLU B CD    1 
ATOM   18697 O  OE1   . GLU B 2  1019 ? 115.553 168.990 95.311  1.00 18.23  ? 1019 GLU B OE1   1 
ATOM   18698 O  OE2   . GLU B 2  1019 ? 115.508 169.317 93.142  1.00 7.97   ? 1019 GLU B OE2   1 
ATOM   18699 N  N     . ASP B 2  1020 ? 120.694 168.617 96.494  1.00 1.43   ? 1020 ASP B N     1 
ATOM   18700 C  CA    . ASP B 2  1020 ? 121.672 169.685 96.632  1.00 8.49   ? 1020 ASP B CA    1 
ATOM   18701 C  C     . ASP B 2  1020 ? 123.101 169.181 96.718  1.00 10.49  ? 1020 ASP B C     1 
ATOM   18702 O  O     . ASP B 2  1020 ? 124.005 169.979 96.958  1.00 9.10   ? 1020 ASP B O     1 
ATOM   18703 C  CB    . ASP B 2  1020 ? 121.381 170.517 97.875  1.00 0.69   ? 1020 ASP B CB    1 
ATOM   18704 C  CG    . ASP B 2  1020 ? 119.937 170.919 97.978  1.00 19.28  ? 1020 ASP B CG    1 
ATOM   18705 O  OD1   . ASP B 2  1020 ? 119.246 170.390 98.871  1.00 19.72  ? 1020 ASP B OD1   1 
ATOM   18706 O  OD2   . ASP B 2  1020 ? 119.489 171.765 97.176  1.00 19.41  ? 1020 ASP B OD2   1 
ATOM   18707 N  N     . GLY B 2  1021 ? 123.326 167.886 96.572  1.00 0.96   ? 1021 GLY B N     1 
ATOM   18708 C  CA    . GLY B 2  1021 ? 124.655 167.339 96.566  1.00 3.95   ? 1021 GLY B CA    1 
ATOM   18709 C  C     . GLY B 2  1021 ? 125.195 166.894 97.900  1.00 4.00   ? 1021 GLY B C     1 
ATOM   18710 O  O     . GLY B 2  1021 ? 126.364 166.510 97.966  1.00 9.07   ? 1021 GLY B O     1 
ATOM   18711 N  N     . LEU B 2  1022 ? 124.402 166.939 98.964  1.00 2.00   ? 1022 LEU B N     1 
ATOM   18712 C  CA    . LEU B 2  1022 ? 124.869 166.456 100.253 1.00 12.08  ? 1022 LEU B CA    1 
ATOM   18713 C  C     . LEU B 2  1022 ? 124.993 164.944 100.222 1.00 0.67   ? 1022 LEU B C     1 
ATOM   18714 O  O     . LEU B 2  1022 ? 124.088 164.244 99.774  1.00 11.32  ? 1022 LEU B O     1 
ATOM   18715 C  CB    . LEU B 2  1022 ? 123.920 166.884 101.369 1.00 8.31   ? 1022 LEU B CB    1 
ATOM   18716 C  CG    . LEU B 2  1022 ? 124.244 166.473 102.812 1.00 2.49   ? 1022 LEU B CG    1 
ATOM   18717 C  CD1   . LEU B 2  1022 ? 125.371 167.297 103.391 1.00 6.03   ? 1022 LEU B CD1   1 
ATOM   18718 C  CD2   . LEU B 2  1022 ? 123.027 166.558 103.701 1.00 8.95   ? 1022 LEU B CD2   1 
ATOM   18719 N  N     . GLN B 2  1023 ? 126.117 164.437 100.688 1.00 7.44   ? 1023 GLN B N     1 
ATOM   18720 C  CA    . GLN B 2  1023 ? 126.315 163.006 100.738 1.00 11.76  ? 1023 GLN B CA    1 
ATOM   18721 C  C     . GLN B 2  1023 ? 126.865 162.628 102.099 1.00 2.95   ? 1023 GLN B C     1 
ATOM   18722 O  O     . GLN B 2  1023 ? 127.461 163.460 102.778 1.00 3.03   ? 1023 GLN B O     1 
ATOM   18723 C  CB    . GLN B 2  1023 ? 127.258 162.551 99.623  1.00 10.14  ? 1023 GLN B CB    1 
ATOM   18724 C  CG    . GLN B 2  1023 ? 128.675 162.925 99.811  1.00 2.32   ? 1023 GLN B CG    1 
ATOM   18725 C  CD    . GLN B 2  1023 ? 129.509 162.458 98.669  1.00 8.14   ? 1023 GLN B CD    1 
ATOM   18726 O  OE1   . GLN B 2  1023 ? 128.988 162.100 97.622  1.00 10.56  ? 1023 GLN B OE1   1 
ATOM   18727 N  NE2   . GLN B 2  1023 ? 130.813 162.433 98.862  1.00 13.28  ? 1023 GLN B NE2   1 
ATOM   18728 N  N     . PRO B 2  1024 ? 126.643 161.401 102.541 1.00 9.04   ? 1024 PRO B N     1 
ATOM   18729 C  CA    . PRO B 2  1024 ? 127.052 161.025 103.891 1.00 15.19  ? 1024 PRO B CA    1 
ATOM   18730 C  C     . PRO B 2  1024 ? 128.515 160.614 103.981 1.00 2.58   ? 1024 PRO B C     1 
ATOM   18731 O  O     . PRO B 2  1024 ? 129.167 160.270 102.997 1.00 6.61   ? 1024 PRO B O     1 
ATOM   18732 C  CB    . PRO B 2  1024 ? 126.129 159.846 104.203 1.00 3.34   ? 1024 PRO B CB    1 
ATOM   18733 C  CG    . PRO B 2  1024 ? 125.879 159.247 102.911 1.00 3.99   ? 1024 PRO B CG    1 
ATOM   18734 C  CD    . PRO B 2  1024 ? 125.825 160.350 101.915 1.00 3.99   ? 1024 PRO B CD    1 
ATOM   18735 N  N     . ASP B 2  1025 ? 129.027 160.677 105.204 1.00 10.26  ? 1025 ASP B N     1 
ATOM   18736 C  CA    . ASP B 2  1025 ? 130.274 160.021 105.565 1.00 10.51  ? 1025 ASP B CA    1 
ATOM   18737 C  C     . ASP B 2  1025 ? 130.036 158.592 106.006 1.00 12.66  ? 1025 ASP B C     1 
ATOM   18738 O  O     . ASP B 2  1025 ? 130.864 157.721 105.744 1.00 18.16  ? 1025 ASP B O     1 
ATOM   18739 C  CB    . ASP B 2  1025 ? 130.968 160.773 106.696 1.00 12.89  ? 1025 ASP B CB    1 
ATOM   18740 C  CG    . ASP B 2  1025 ? 131.455 162.120 106.275 1.00 23.63  ? 1025 ASP B CG    1 
ATOM   18741 O  OD1   . ASP B 2  1025 ? 131.766 162.275 105.084 1.00 31.21  ? 1025 ASP B OD1   1 
ATOM   18742 O  OD2   . ASP B 2  1025 ? 131.513 163.031 107.123 1.00 20.63  ? 1025 ASP B OD2   1 
ATOM   18743 N  N     . LEU B 2  1026 ? 128.916 158.354 106.682 1.00 8.30   ? 1026 LEU B N     1 
ATOM   18744 C  CA    . LEU B 2  1026 ? 128.527 157.056 107.203 1.00 4.75   ? 1026 LEU B CA    1 
ATOM   18745 C  C     . LEU B 2  1026 ? 127.086 156.763 106.832 1.00 8.90   ? 1026 LEU B C     1 
ATOM   18746 O  O     . LEU B 2  1026 ? 126.260 157.668 106.767 1.00 2.70   ? 1026 LEU B O     1 
ATOM   18747 C  CB    . LEU B 2  1026 ? 128.669 157.003 108.718 1.00 0.96   ? 1026 LEU B CB    1 
ATOM   18748 C  CG    . LEU B 2  1026 ? 130.032 157.224 109.355 1.00 3.36   ? 1026 LEU B CG    1 
ATOM   18749 C  CD1   . LEU B 2  1026 ? 129.928 157.057 110.842 1.00 14.40  ? 1026 LEU B CD1   1 
ATOM   18750 C  CD2   . LEU B 2  1026 ? 131.018 156.250 108.794 1.00 5.86   ? 1026 LEU B CD2   1 
ATOM   18751 N  N     . ILE B 2  1027 ? 126.792 155.495 106.583 1.00 0.07   ? 1027 ILE B N     1 
ATOM   18752 C  CA    . ILE B 2  1027 ? 125.432 155.012 106.390 1.00 5.38   ? 1027 ILE B CA    1 
ATOM   18753 C  C     . ILE B 2  1027 ? 125.177 153.979 107.474 1.00 3.18   ? 1027 ILE B C     1 
ATOM   18754 O  O     . ILE B 2  1027 ? 125.811 152.921 107.483 1.00 3.21   ? 1027 ILE B O     1 
ATOM   18755 C  CB    . ILE B 2  1027 ? 125.223 154.415 104.996 1.00 0.40   ? 1027 ILE B CB    1 
ATOM   18756 C  CG1   . ILE B 2  1027 ? 125.657 155.397 103.916 1.00 1.03   ? 1027 ILE B CG1   1 
ATOM   18757 C  CG2   . ILE B 2  1027 ? 123.775 154.033 104.796 1.00 15.92  ? 1027 ILE B CG2   1 
ATOM   18758 C  CD1   . ILE B 2  1027 ? 125.833 154.774 102.590 1.00 5.25   ? 1027 ILE B CD1   1 
ATOM   18759 N  N     . VAL B 2  1028 ? 124.269 154.277 108.394 1.00 9.16   ? 1028 VAL B N     1 
ATOM   18760 C  CA    . VAL B 2  1028 ? 123.941 153.345 109.461 1.00 15.24  ? 1028 VAL B CA    1 
ATOM   18761 C  C     . VAL B 2  1028 ? 122.553 152.773 109.206 1.00 9.34   ? 1028 VAL B C     1 
ATOM   18762 O  O     . VAL B 2  1028 ? 121.681 153.422 108.629 1.00 5.29   ? 1028 VAL B O     1 
ATOM   18763 C  CB    . VAL B 2  1028 ? 124.045 153.971 110.874 1.00 17.77  ? 1028 VAL B CB    1 
ATOM   18764 C  CG1   . VAL B 2  1028 ? 125.217 154.933 110.961 1.00 14.58  ? 1028 VAL B CG1   1 
ATOM   18765 C  CG2   . VAL B 2  1028 ? 122.776 154.619 111.288 1.00 19.54  ? 1028 VAL B CG2   1 
ATOM   18766 N  N     . ASN B 2  1029 ? 122.375 151.524 109.611 1.00 8.91   ? 1029 ASN B N     1 
ATOM   18767 C  CA    . ASN B 2  1029 ? 121.137 150.809 109.366 1.00 13.07  ? 1029 ASN B CA    1 
ATOM   18768 C  C     . ASN B 2  1029 ? 120.028 151.327 110.274 1.00 0.76   ? 1029 ASN B C     1 
ATOM   18769 O  O     . ASN B 2  1029 ? 120.231 151.470 111.480 1.00 2.07   ? 1029 ASN B O     1 
ATOM   18770 C  CB    . ASN B 2  1029 ? 121.335 149.324 109.613 1.00 5.09   ? 1029 ASN B CB    1 
ATOM   18771 C  CG    . ASN B 2  1029 ? 120.474 148.471 108.748 1.00 1.72   ? 1029 ASN B CG    1 
ATOM   18772 O  OD1   . ASN B 2  1029 ? 120.135 148.831 107.639 1.00 5.91   ? 1029 ASN B OD1   1 
ATOM   18773 N  ND2   . ASN B 2  1029 ? 120.096 147.327 109.263 1.00 5.96   ? 1029 ASN B ND2   1 
ATOM   18774 N  N     . PRO B 2  1030 ? 118.845 151.607 109.729 1.00 2.08   ? 1030 PRO B N     1 
ATOM   18775 C  CA    . PRO B 2  1030 ? 117.726 152.002 110.587 1.00 5.86   ? 1030 PRO B CA    1 
ATOM   18776 C  C     . PRO B 2  1030 ? 117.271 150.916 111.550 1.00 6.86   ? 1030 PRO B C     1 
ATOM   18777 O  O     . PRO B 2  1030 ? 116.643 151.240 112.556 1.00 8.17   ? 1030 PRO B O     1 
ATOM   18778 C  CB    . PRO B 2  1030 ? 116.635 152.377 109.578 1.00 0.72   ? 1030 PRO B CB    1 
ATOM   18779 C  CG    . PRO B 2  1030 ? 117.030 151.772 108.332 1.00 13.79  ? 1030 PRO B CG    1 
ATOM   18780 C  CD    . PRO B 2  1030 ? 118.493 151.694 108.309 1.00 14.15  ? 1030 PRO B CD    1 
ATOM   18781 N  N     . HIS B 2  1031 ? 117.595 149.652 111.299 1.00 14.78  ? 1031 HIS B N     1 
ATOM   18782 C  CA    . HIS B 2  1031 ? 117.225 148.557 112.185 1.00 15.54  ? 1031 HIS B CA    1 
ATOM   18783 C  C     . HIS B 2  1031 ? 118.045 148.524 113.451 1.00 9.62   ? 1031 HIS B C     1 
ATOM   18784 O  O     . HIS B 2  1031 ? 117.790 147.684 114.312 1.00 8.02   ? 1031 HIS B O     1 
ATOM   18785 C  CB    . HIS B 2  1031 ? 117.370 147.217 111.478 1.00 15.09  ? 1031 HIS B CB    1 
ATOM   18786 C  CG    . HIS B 2  1031 ? 116.432 147.045 110.334 1.00 1.92   ? 1031 HIS B CG    1 
ATOM   18787 N  ND1   . HIS B 2  1031 ? 116.562 147.755 109.164 1.00 13.14  ? 1031 HIS B ND1   1 
ATOM   18788 C  CD2   . HIS B 2  1031 ? 115.339 146.268 110.186 1.00 11.79  ? 1031 HIS B CD2   1 
ATOM   18789 C  CE1   . HIS B 2  1031 ? 115.587 147.424 108.343 1.00 9.17   ? 1031 HIS B CE1   1 
ATOM   18790 N  NE2   . HIS B 2  1031 ? 114.841 146.512 108.934 1.00 5.31   ? 1031 HIS B NE2   1 
ATOM   18791 N  N     . SER B 2  1032 ? 119.049 149.377 113.564 1.00 1.77   ? 1032 SER B N     1 
ATOM   18792 C  CA    . SER B 2  1032 ? 119.784 149.525 114.802 1.00 0.22   ? 1032 SER B CA    1 
ATOM   18793 C  C     . SER B 2  1032 ? 119.039 150.371 115.817 1.00 5.72   ? 1032 SER B C     1 
ATOM   18794 O  O     . SER B 2  1032 ? 119.464 150.442 116.968 1.00 18.72  ? 1032 SER B O     1 
ATOM   18795 C  CB    . SER B 2  1032 ? 121.148 150.137 114.517 1.00 6.04   ? 1032 SER B CB    1 
ATOM   18796 O  OG    . SER B 2  1032 ? 121.020 151.359 113.828 1.00 13.17  ? 1032 SER B OG    1 
ATOM   18797 N  N     . HIS B 2  1033 ? 117.970 151.038 115.419 1.00 10.09  ? 1033 HIS B N     1 
ATOM   18798 C  CA    . HIS B 2  1033 ? 117.239 151.903 116.332 1.00 12.36  ? 1033 HIS B CA    1 
ATOM   18799 C  C     . HIS B 2  1033 ? 116.153 151.225 117.176 1.00 16.20  ? 1033 HIS B C     1 
ATOM   18800 O  O     . HIS B 2  1033 ? 116.188 151.339 118.404 1.00 20.39  ? 1033 HIS B O     1 
ATOM   18801 C  CB    . HIS B 2  1033 ? 116.633 153.069 115.555 1.00 6.45   ? 1033 HIS B CB    1 
ATOM   18802 C  CG    . HIS B 2  1033 ? 115.885 154.027 116.421 1.00 12.30  ? 1033 HIS B CG    1 
ATOM   18803 N  ND1   . HIS B 2  1033 ? 114.555 153.864 116.735 1.00 18.80  ? 1033 HIS B ND1   1 
ATOM   18804 C  CD2   . HIS B 2  1033 ? 116.296 155.131 117.084 1.00 16.41  ? 1033 HIS B CD2   1 
ATOM   18805 C  CE1   . HIS B 2  1033 ? 114.174 154.840 117.537 1.00 11.49  ? 1033 HIS B CE1   1 
ATOM   18806 N  NE2   . HIS B 2  1033 ? 115.212 155.622 117.763 1.00 12.34  ? 1033 HIS B NE2   1 
ATOM   18807 N  N     . PRO B 2  1034 ? 115.172 150.529 116.582 1.00 18.95  ? 1034 PRO B N     1 
ATOM   18808 C  CA    . PRO B 2  1034 ? 113.919 150.271 117.323 1.00 15.11  ? 1034 PRO B CA    1 
ATOM   18809 C  C     . PRO B 2  1034 ? 114.061 149.466 118.608 1.00 17.77  ? 1034 PRO B C     1 
ATOM   18810 O  O     . PRO B 2  1034 ? 113.293 149.703 119.545 1.00 25.51  ? 1034 PRO B O     1 
ATOM   18811 C  CB    . PRO B 2  1034 ? 113.055 149.538 116.288 1.00 11.40  ? 1034 PRO B CB    1 
ATOM   18812 C  CG    . PRO B 2  1034 ? 113.991 148.987 115.338 1.00 12.65  ? 1034 PRO B CG    1 
ATOM   18813 C  CD    . PRO B 2  1034 ? 115.124 149.926 115.243 1.00 13.27  ? 1034 PRO B CD    1 
ATOM   18814 N  N     . SER B 2  1035 ? 114.992 148.514 118.688 1.00 16.74  ? 1035 SER B N     1 
ATOM   18815 C  CA    . SER B 2  1035 ? 115.145 147.749 119.925 1.00 17.59  ? 1035 SER B CA    1 
ATOM   18816 C  C     . SER B 2  1035 ? 116.064 148.442 120.924 1.00 21.88  ? 1035 SER B C     1 
ATOM   18817 O  O     . SER B 2  1035 ? 115.818 148.384 122.131 1.00 25.35  ? 1035 SER B O     1 
ATOM   18818 C  CB    . SER B 2  1035 ? 115.666 146.344 119.630 1.00 19.44  ? 1035 SER B CB    1 
ATOM   18819 O  OG    . SER B 2  1035 ? 114.633 145.498 119.179 1.00 24.71  ? 1035 SER B OG    1 
ATOM   18820 N  N     . ARG B 2  1036 ? 117.142 149.073 120.450 1.00 25.62  ? 1036 ARG B N     1 
ATOM   18821 C  CA    . ARG B 2  1036 ? 118.048 149.771 121.349 1.00 20.87  ? 1036 ARG B CA    1 
ATOM   18822 C  C     . ARG B 2  1036 ? 117.449 151.048 121.910 1.00 20.72  ? 1036 ARG B C     1 
ATOM   18823 O  O     . ARG B 2  1036 ? 117.841 151.464 123.002 1.00 22.27  ? 1036 ARG B O     1 
ATOM   18824 C  CB    . ARG B 2  1036 ? 119.371 150.088 120.653 1.00 14.23  ? 1036 ARG B CB    1 
ATOM   18825 C  CG    . ARG B 2  1036 ? 120.165 148.869 120.238 1.00 17.07  ? 1036 ARG B CG    1 
ATOM   18826 C  CD    . ARG B 2  1036 ? 121.204 149.203 119.170 1.00 21.41  ? 1036 ARG B CD    1 
ATOM   18827 N  NE    . ARG B 2  1036 ? 122.581 148.995 119.606 1.00 28.32  ? 1036 ARG B NE    1 
ATOM   18828 C  CZ    . ARG B 2  1036 ? 123.650 149.165 118.837 1.00 29.90  ? 1036 ARG B CZ    1 
ATOM   18829 N  NH1   . ARG B 2  1036 ? 123.546 149.591 117.590 1.00 23.03  ? 1036 ARG B NH1   1 
ATOM   18830 N  NH2   . ARG B 2  1036 ? 124.854 148.891 119.329 1.00 24.91  ? 1036 ARG B NH2   1 
ATOM   18831 N  N     . MET B 2  1037 ? 116.507 151.664 121.200 1.00 17.94  ? 1037 MET B N     1 
ATOM   18832 C  CA    . MET B 2  1037 ? 115.803 152.851 121.675 1.00 16.24  ? 1037 MET B CA    1 
ATOM   18833 C  C     . MET B 2  1037 ? 116.773 153.972 122.029 1.00 19.67  ? 1037 MET B C     1 
ATOM   18834 O  O     . MET B 2  1037 ? 116.670 154.602 123.079 1.00 17.35  ? 1037 MET B O     1 
ATOM   18835 C  CB    . MET B 2  1037 ? 114.899 152.514 122.857 1.00 15.01  ? 1037 MET B CB    1 
ATOM   18836 C  CG    . MET B 2  1037 ? 113.962 151.346 122.607 1.00 14.55  ? 1037 MET B CG    1 
ATOM   18837 S  SD    . MET B 2  1037 ? 112.459 151.436 123.580 1.00 27.49  ? 1037 MET B SD    1 
ATOM   18838 C  CE    . MET B 2  1037 ? 112.742 150.130 124.756 1.00 16.46  ? 1037 MET B CE    1 
ATOM   18839 N  N     . THR B 2  1038 ? 117.732 154.219 121.138 1.00 19.63  ? 1038 THR B N     1 
ATOM   18840 C  CA    . THR B 2  1038 ? 118.676 155.324 121.280 1.00 15.97  ? 1038 THR B CA    1 
ATOM   18841 C  C     . THR B 2  1038 ? 118.087 156.556 120.600 1.00 16.02  ? 1038 THR B C     1 
ATOM   18842 O  O     . THR B 2  1038 ? 118.521 156.990 119.534 1.00 12.20  ? 1038 THR B O     1 
ATOM   18843 C  CB    . THR B 2  1038 ? 120.028 154.947 120.694 1.00 12.59  ? 1038 THR B CB    1 
ATOM   18844 O  OG1   . THR B 2  1038 ? 119.855 154.528 119.337 1.00 22.41  ? 1038 THR B OG1   1 
ATOM   18845 C  CG2   . THR B 2  1038 ? 120.649 153.824 121.481 1.00 10.47  ? 1038 THR B CG2   1 
ATOM   18846 N  N     . ASN B 2  1039 ? 117.073 157.129 121.246 1.00 10.60  ? 1039 ASN B N     1 
ATOM   18847 C  CA    . ASN B 2  1039 ? 116.329 158.232 120.654 1.00 5.85   ? 1039 ASN B CA    1 
ATOM   18848 C  C     . ASN B 2  1039 ? 117.062 159.554 120.729 1.00 5.53   ? 1039 ASN B C     1 
ATOM   18849 O  O     . ASN B 2  1039 ? 116.740 160.460 119.961 1.00 12.46  ? 1039 ASN B O     1 
ATOM   18850 C  CB    . ASN B 2  1039 ? 114.965 158.376 121.322 1.00 4.92   ? 1039 ASN B CB    1 
ATOM   18851 C  CG    . ASN B 2  1039 ? 114.202 157.092 121.341 1.00 15.62  ? 1039 ASN B CG    1 
ATOM   18852 O  OD1   . ASN B 2  1039 ? 113.969 156.510 122.391 1.00 16.17  ? 1039 ASN B OD1   1 
ATOM   18853 N  ND2   . ASN B 2  1039 ? 113.838 156.614 120.169 1.00 19.73  ? 1039 ASN B ND2   1 
ATOM   18854 N  N     . GLY B 2  1040 ? 118.023 159.696 121.639 1.00 13.00  ? 1040 GLY B N     1 
ATOM   18855 C  CA    . GLY B 2  1040 ? 118.773 160.930 121.717 1.00 1.41   ? 1040 GLY B CA    1 
ATOM   18856 C  C     . GLY B 2  1040 ? 119.703 161.150 120.548 1.00 6.52   ? 1040 GLY B C     1 
ATOM   18857 O  O     . GLY B 2  1040 ? 120.045 162.294 120.252 1.00 13.97  ? 1040 GLY B O     1 
ATOM   18858 N  N     . GLN B 2  1041 ? 120.122 160.076 119.881 1.00 4.22   ? 1041 GLN B N     1 
ATOM   18859 C  CA    . GLN B 2  1041 ? 120.948 160.191 118.685 1.00 0.21   ? 1041 GLN B CA    1 
ATOM   18860 C  C     . GLN B 2  1041 ? 120.165 160.734 117.497 1.00 2.29   ? 1041 GLN B C     1 
ATOM   18861 O  O     . GLN B 2  1041 ? 120.730 161.433 116.657 1.00 8.42   ? 1041 GLN B O     1 
ATOM   18862 C  CB    . GLN B 2  1041 ? 121.539 158.830 118.351 1.00 5.37   ? 1041 GLN B CB    1 
ATOM   18863 C  CG    . GLN B 2  1041 ? 122.383 158.775 117.119 1.00 4.31   ? 1041 GLN B CG    1 
ATOM   18864 C  CD    . GLN B 2  1041 ? 122.703 157.363 116.747 1.00 7.21   ? 1041 GLN B CD    1 
ATOM   18865 O  OE1   . GLN B 2  1041 ? 122.299 156.436 117.434 1.00 16.87  ? 1041 GLN B OE1   1 
ATOM   18866 N  NE2   . GLN B 2  1041 ? 123.436 157.180 115.660 1.00 2.75   ? 1041 GLN B NE2   1 
ATOM   18867 N  N     . MET B 2  1042 ? 118.876 160.416 117.401 1.00 3.08   ? 1042 MET B N     1 
ATOM   18868 C  CA    . MET B 2  1042 ? 118.040 160.964 116.342 1.00 6.61   ? 1042 MET B CA    1 
ATOM   18869 C  C     . MET B 2  1042 ? 117.671 162.413 116.608 1.00 3.90   ? 1042 MET B C     1 
ATOM   18870 O  O     . MET B 2  1042 ? 117.544 163.198 115.670 1.00 4.88   ? 1042 MET B O     1 
ATOM   18871 C  CB    . MET B 2  1042 ? 116.777 160.126 116.182 1.00 5.81   ? 1042 MET B CB    1 
ATOM   18872 C  CG    . MET B 2  1042 ? 117.029 158.642 116.098 1.00 10.38  ? 1042 MET B CG    1 
ATOM   18873 S  SD    . MET B 2  1042 ? 117.782 158.090 114.560 1.00 19.62  ? 1042 MET B SD    1 
ATOM   18874 C  CE    . MET B 2  1042 ? 116.543 158.605 113.396 1.00 0.58   ? 1042 MET B CE    1 
ATOM   18875 N  N     . ILE B 2  1043 ? 117.469 162.780 117.872 1.00 2.75   ? 1043 ILE B N     1 
ATOM   18876 C  CA    . ILE B 2  1043 ? 117.206 164.174 118.212 1.00 0.29   ? 1043 ILE B CA    1 
ATOM   18877 C  C     . ILE B 2  1043 ? 118.427 165.029 117.925 1.00 11.01  ? 1043 ILE B C     1 
ATOM   18878 O  O     . ILE B 2  1043 ? 118.311 166.187 117.522 1.00 8.64   ? 1043 ILE B O     1 
ATOM   18879 C  CB    . ILE B 2  1043 ? 116.768 164.290 119.684 1.00 3.52   ? 1043 ILE B CB    1 
ATOM   18880 C  CG1   . ILE B 2  1043 ? 115.540 163.428 119.954 1.00 4.46   ? 1043 ILE B CG1   1 
ATOM   18881 C  CG2   . ILE B 2  1043 ? 116.482 165.724 120.061 1.00 0.90   ? 1043 ILE B CG2   1 
ATOM   18882 C  CD1   . ILE B 2  1043 ? 115.205 163.326 121.396 1.00 15.74  ? 1043 ILE B CD1   1 
ATOM   18883 N  N     . GLU B 2  1044 ? 119.616 164.478 118.147 1.00 14.02  ? 1044 GLU B N     1 
ATOM   18884 C  CA    . GLU B 2  1044 ? 120.847 165.210 117.887 1.00 1.60   ? 1044 GLU B CA    1 
ATOM   18885 C  C     . GLU B 2  1044 ? 121.011 165.520 116.405 1.00 9.63   ? 1044 GLU B C     1 
ATOM   18886 O  O     . GLU B 2  1044 ? 121.479 166.601 116.041 1.00 5.42   ? 1044 GLU B O     1 
ATOM   18887 C  CB    . GLU B 2  1044 ? 122.030 164.402 118.407 1.00 8.55   ? 1044 GLU B CB    1 
ATOM   18888 C  CG    . GLU B 2  1044 ? 123.365 165.005 118.084 1.00 5.12   ? 1044 GLU B CG    1 
ATOM   18889 C  CD    . GLU B 2  1044 ? 124.493 164.008 118.088 1.00 7.97   ? 1044 GLU B CD    1 
ATOM   18890 O  OE1   . GLU B 2  1044 ? 124.241 162.795 118.090 1.00 15.25  ? 1044 GLU B OE1   1 
ATOM   18891 O  OE2   . GLU B 2  1044 ? 125.651 164.449 118.110 1.00 10.88  ? 1044 GLU B OE2   1 
ATOM   18892 N  N     . THR B 2  1045 ? 120.641 164.579 115.534 1.00 4.10   ? 1045 THR B N     1 
ATOM   18893 C  CA    . THR B 2  1045 ? 120.668 164.826 114.097 1.00 5.26   ? 1045 THR B CA    1 
ATOM   18894 C  C     . THR B 2  1045 ? 119.662 165.895 113.702 1.00 11.85  ? 1045 THR B C     1 
ATOM   18895 O  O     . THR B 2  1045 ? 119.936 166.719 112.828 1.00 3.99   ? 1045 THR B O     1 
ATOM   18896 C  CB    . THR B 2  1045 ? 120.392 163.528 113.342 1.00 5.73   ? 1045 THR B CB    1 
ATOM   18897 O  OG1   . THR B 2  1045 ? 121.289 162.518 113.799 1.00 6.39   ? 1045 THR B OG1   1 
ATOM   18898 C  CG2   . THR B 2  1045 ? 120.580 163.701 111.858 1.00 14.83  ? 1045 THR B CG2   1 
ATOM   18899 N  N     . THR B 2  1046 ? 118.489 165.886 114.328 1.00 1.55   ? 1046 THR B N     1 
ATOM   18900 C  CA    . THR B 2  1046 ? 117.475 166.897 114.056 1.00 5.14   ? 1046 THR B CA    1 
ATOM   18901 C  C     . THR B 2  1046 ? 117.943 168.278 114.480 1.00 0.50   ? 1046 THR B C     1 
ATOM   18902 O  O     . THR B 2  1046 ? 117.790 169.252 113.739 1.00 3.78   ? 1046 THR B O     1 
ATOM   18903 C  CB    . THR B 2  1046 ? 116.183 166.534 114.785 1.00 14.16  ? 1046 THR B CB    1 
ATOM   18904 O  OG1   . THR B 2  1046 ? 115.678 165.298 114.280 1.00 10.38  ? 1046 THR B OG1   1 
ATOM   18905 C  CG2   . THR B 2  1046 ? 115.137 167.608 114.615 1.00 11.69  ? 1046 THR B CG2   1 
ATOM   18906 N  N     . VAL B 2  1047 ? 118.493 168.384 115.689 1.00 2.25   ? 1047 VAL B N     1 
ATOM   18907 C  CA    . VAL B 2  1047 ? 118.899 169.679 116.221 1.00 7.00   ? 1047 VAL B CA    1 
ATOM   18908 C  C     . VAL B 2  1047 ? 120.136 170.190 115.502 1.00 2.88   ? 1047 VAL B C     1 
ATOM   18909 O  O     . VAL B 2  1047 ? 120.205 171.360 115.121 1.00 0.98   ? 1047 VAL B O     1 
ATOM   18910 C  CB    . VAL B 2  1047 ? 119.120 169.589 117.741 1.00 4.00   ? 1047 VAL B CB    1 
ATOM   18911 C  CG1   . VAL B 2  1047 ? 119.617 170.896 118.277 1.00 11.26  ? 1047 VAL B CG1   1 
ATOM   18912 C  CG2   . VAL B 2  1047 ? 117.842 169.230 118.422 1.00 3.39   ? 1047 VAL B CG2   1 
ATOM   18913 N  N     . GLY B 2  1048 ? 121.126 169.324 115.296 1.00 15.58  ? 1048 GLY B N     1 
ATOM   18914 C  CA    . GLY B 2  1048 ? 122.366 169.751 114.677 1.00 1.22   ? 1048 GLY B CA    1 
ATOM   18915 C  C     . GLY B 2  1048 ? 122.230 170.141 113.229 1.00 3.88   ? 1048 GLY B C     1 
ATOM   18916 O  O     . GLY B 2  1048 ? 123.046 170.914 112.727 1.00 2.01   ? 1048 GLY B O     1 
ATOM   18917 N  N     . LEU B 2  1049 ? 121.215 169.624 112.550 1.00 8.69   ? 1049 LEU B N     1 
ATOM   18918 C  CA    . LEU B 2  1049 ? 120.954 169.979 111.163 1.00 3.39   ? 1049 LEU B CA    1 
ATOM   18919 C  C     . LEU B 2  1049 ? 120.603 171.449 111.017 1.00 1.09   ? 1049 LEU B C     1 
ATOM   18920 O  O     . LEU B 2  1049 ? 121.065 172.110 110.084 1.00 13.62  ? 1049 LEU B O     1 
ATOM   18921 C  CB    . LEU B 2  1049 ? 119.832 169.094 110.648 1.00 2.45   ? 1049 LEU B CB    1 
ATOM   18922 C  CG    . LEU B 2  1049 ? 119.543 168.830 109.187 1.00 2.94   ? 1049 LEU B CG    1 
ATOM   18923 C  CD1   . LEU B 2  1049 ? 120.793 168.435 108.466 1.00 13.21  ? 1049 LEU B CD1   1 
ATOM   18924 C  CD2   . LEU B 2  1049 ? 118.558 167.698 109.178 1.00 4.68   ? 1049 LEU B CD2   1 
ATOM   18925 N  N     . ALA B 2  1050 ? 119.776 171.974 111.920 1.00 4.97   ? 1050 ALA B N     1 
ATOM   18926 C  CA    . ALA B 2  1050 ? 119.460 173.392 111.975 1.00 5.46   ? 1050 ALA B CA    1 
ATOM   18927 C  C     . ALA B 2  1050 ? 120.571 174.226 112.588 1.00 9.12   ? 1050 ALA B C     1 
ATOM   18928 O  O     . ALA B 2  1050 ? 120.679 175.410 112.270 1.00 8.54   ? 1050 ALA B O     1 
ATOM   18929 C  CB    . ALA B 2  1050 ? 118.170 173.609 112.762 1.00 6.17   ? 1050 ALA B CB    1 
ATOM   18930 N  N     . ASN B 2  1051 ? 121.386 173.640 113.465 1.00 8.64   ? 1051 ASN B N     1 
ATOM   18931 C  CA    . ASN B 2  1051 ? 122.551 174.337 113.996 1.00 0.31   ? 1051 ASN B CA    1 
ATOM   18932 C  C     . ASN B 2  1051 ? 123.538 174.681 112.895 1.00 2.78   ? 1051 ASN B C     1 
ATOM   18933 O  O     . ASN B 2  1051 ? 124.107 175.774 112.884 1.00 5.48   ? 1051 ASN B O     1 
ATOM   18934 C  CB    . ASN B 2  1051 ? 123.252 173.478 115.044 1.00 3.17   ? 1051 ASN B CB    1 
ATOM   18935 C  CG    . ASN B 2  1051 ? 122.571 173.500 116.367 1.00 5.55   ? 1051 ASN B CG    1 
ATOM   18936 O  OD1   . ASN B 2  1051 ? 121.695 174.309 116.606 1.00 6.39   ? 1051 ASN B OD1   1 
ATOM   18937 N  ND2   . ASN B 2  1051 ? 122.984 172.621 117.251 1.00 0.38   ? 1051 ASN B ND2   1 
ATOM   18938 N  N     . ALA B 2  1052 ? 123.778 173.744 111.979 1.00 0.59   ? 1052 ALA B N     1 
ATOM   18939 C  CA    . ALA B 2  1052 ? 124.775 173.952 110.938 1.00 11.09  ? 1052 ALA B CA    1 
ATOM   18940 C  C     . ALA B 2  1052 ? 124.368 175.067 109.989 1.00 3.33   ? 1052 ALA B C     1 
ATOM   18941 O  O     . ALA B 2  1052 ? 125.215 175.848 109.548 1.00 13.59  ? 1052 ALA B O     1 
ATOM   18942 C  CB    . ALA B 2  1052 ? 125.010 172.656 110.176 1.00 13.46  ? 1052 ALA B CB    1 
ATOM   18943 N  N     . LEU B 2  1053 ? 123.083 175.151 109.647 1.00 6.27   ? 1053 LEU B N     1 
ATOM   18944 C  CA    . LEU B 2  1053 ? 122.625 176.214 108.761 1.00 7.61   ? 1053 LEU B CA    1 
ATOM   18945 C  C     . LEU B 2  1053 ? 122.527 177.550 109.479 1.00 10.03  ? 1053 LEU B C     1 
ATOM   18946 O  O     . LEU B 2  1053 ? 122.700 178.599 108.857 1.00 16.05  ? 1053 LEU B O     1 
ATOM   18947 C  CB    . LEU B 2  1053 ? 121.280 175.844 108.142 1.00 9.09   ? 1053 LEU B CB    1 
ATOM   18948 C  CG    . LEU B 2  1053 ? 121.287 174.634 107.216 1.00 11.08  ? 1053 LEU B CG    1 
ATOM   18949 C  CD1   . LEU B 2  1053 ? 119.930 174.435 106.621 1.00 7.78   ? 1053 LEU B CD1   1 
ATOM   18950 C  CD2   . LEU B 2  1053 ? 122.323 174.803 106.138 1.00 9.39   ? 1053 LEU B CD2   1 
ATOM   18951 N  N     . GLN B 2  1054 ? 122.230 177.530 110.774 1.00 12.16  ? 1054 GLN B N     1 
ATOM   18952 C  CA    . GLN B 2  1054 ? 122.232 178.742 111.580 1.00 7.22   ? 1054 GLN B CA    1 
ATOM   18953 C  C     . GLN B 2  1054 ? 123.642 179.249 111.840 1.00 13.62  ? 1054 GLN B C     1 
ATOM   18954 O  O     . GLN B 2  1054 ? 123.858 180.460 111.921 1.00 13.13  ? 1054 GLN B O     1 
ATOM   18955 C  CB    . GLN B 2  1054 ? 121.537 178.458 112.901 1.00 6.87   ? 1054 GLN B CB    1 
ATOM   18956 C  CG    . GLN B 2  1054 ? 120.603 179.509 113.353 1.00 13.06  ? 1054 GLN B CG    1 
ATOM   18957 C  CD    . GLN B 2  1054 ? 119.183 179.129 113.097 1.00 18.87  ? 1054 GLN B CD    1 
ATOM   18958 O  OE1   . GLN B 2  1054 ? 118.609 178.310 113.808 1.00 22.50  ? 1054 GLN B OE1   1 
ATOM   18959 N  NE2   . GLN B 2  1054 ? 118.595 179.721 112.075 1.00 19.64  ? 1054 GLN B NE2   1 
ATOM   18960 N  N     . GLY B 2  1055 ? 124.600 178.347 112.003 1.00 9.94   ? 1055 GLY B N     1 
ATOM   18961 C  CA    . GLY B 2  1055 ? 125.956 178.732 112.313 1.00 2.01   ? 1055 GLY B CA    1 
ATOM   18962 C  C     . GLY B 2  1055 ? 126.296 178.742 113.781 1.00 5.29   ? 1055 GLY B C     1 
ATOM   18963 O  O     . GLY B 2  1055 ? 127.151 179.526 114.194 1.00 15.79  ? 1055 GLY B O     1 
ATOM   18964 N  N     . VAL B 2  1056 ? 125.672 177.880 114.586 1.00 6.23   ? 1056 VAL B N     1 
ATOM   18965 C  CA    . VAL B 2  1056 ? 125.781 177.930 116.037 1.00 2.06   ? 1056 VAL B CA    1 
ATOM   18966 C  C     . VAL B 2  1056 ? 126.055 176.540 116.590 1.00 2.23   ? 1056 VAL B C     1 
ATOM   18967 O  O     . VAL B 2  1056 ? 125.868 175.530 115.919 1.00 9.63   ? 1056 VAL B O     1 
ATOM   18968 C  CB    . VAL B 2  1056 ? 124.513 178.512 116.695 1.00 1.74   ? 1056 VAL B CB    1 
ATOM   18969 C  CG1   . VAL B 2  1056 ? 124.297 179.927 116.263 1.00 7.78   ? 1056 VAL B CG1   1 
ATOM   18970 C  CG2   . VAL B 2  1056 ? 123.314 177.674 116.344 1.00 3.93   ? 1056 VAL B CG2   1 
ATOM   18971 N  N     . VAL B 2  1057 ? 126.522 176.509 117.832 1.00 4.16   ? 1057 VAL B N     1 
ATOM   18972 C  CA    . VAL B 2  1057 ? 126.682 175.291 118.617 1.00 0.44   ? 1057 VAL B CA    1 
ATOM   18973 C  C     . VAL B 2  1057 ? 125.813 175.445 119.855 1.00 0.50   ? 1057 VAL B C     1 
ATOM   18974 O  O     . VAL B 2  1057 ? 125.964 176.417 120.600 1.00 9.62   ? 1057 VAL B O     1 
ATOM   18975 C  CB    . VAL B 2  1057 ? 128.150 175.049 119.001 1.00 3.61   ? 1057 VAL B CB    1 
ATOM   18976 C  CG1   . VAL B 2  1057 ? 128.269 173.938 120.010 1.00 2.84   ? 1057 VAL B CG1   1 
ATOM   18977 C  CG2   . VAL B 2  1057 ? 128.979 174.741 117.781 1.00 4.94   ? 1057 VAL B CG2   1 
ATOM   18978 N  N     . THR B 2  1058 ? 124.901 174.508 120.074 1.00 3.29   ? 1058 THR B N     1 
ATOM   18979 C  CA    . THR B 2  1058 ? 123.968 174.598 121.188 1.00 5.91   ? 1058 THR B CA    1 
ATOM   18980 C  C     . THR B 2  1058 ? 124.212 173.489 122.199 1.00 4.84   ? 1058 THR B C     1 
ATOM   18981 O  O     . THR B 2  1058 ? 125.045 172.605 122.010 1.00 3.26   ? 1058 THR B O     1 
ATOM   18982 C  CB    . THR B 2  1058 ? 122.519 174.541 120.709 1.00 9.03   ? 1058 THR B CB    1 
ATOM   18983 O  OG1   . THR B 2  1058 ? 122.281 173.279 120.086 1.00 14.34  ? 1058 THR B OG1   1 
ATOM   18984 C  CG2   . THR B 2  1058 ? 122.241 175.655 119.723 1.00 4.05   ? 1058 THR B CG2   1 
ATOM   18985 N  N     . ASP B 2  1059 ? 123.445 173.547 123.282 1.00 11.35  ? 1059 ASP B N     1 
ATOM   18986 C  CA    . ASP B 2  1059 ? 123.606 172.654 124.420 1.00 4.90   ? 1059 ASP B CA    1 
ATOM   18987 C  C     . ASP B 2  1059 ? 122.495 171.617 124.436 1.00 10.54  ? 1059 ASP B C     1 
ATOM   18988 O  O     . ASP B 2  1059 ? 121.317 171.963 124.336 1.00 15.85  ? 1059 ASP B O     1 
ATOM   18989 C  CB    . ASP B 2  1059 ? 123.605 173.439 125.725 1.00 10.79  ? 1059 ASP B CB    1 
ATOM   18990 C  CG    . ASP B 2  1059 ? 124.437 172.778 126.792 1.00 21.54  ? 1059 ASP B CG    1 
ATOM   18991 O  OD1   . ASP B 2  1059 ? 125.673 172.934 126.750 1.00 26.38  ? 1059 ASP B OD1   1 
ATOM   18992 O  OD2   . ASP B 2  1059 ? 123.867 172.099 127.667 1.00 17.24  ? 1059 ASP B OD2   1 
ATOM   18993 N  N     . GLY B 2  1060 ? 122.873 170.353 124.575 1.00 6.83   ? 1060 GLY B N     1 
ATOM   18994 C  CA    . GLY B 2  1060 ? 121.912 169.282 124.689 1.00 5.14   ? 1060 GLY B CA    1 
ATOM   18995 C  C     . GLY B 2  1060 ? 122.123 168.423 125.910 1.00 6.22   ? 1060 GLY B C     1 
ATOM   18996 O  O     . GLY B 2  1060 ? 122.003 167.202 125.841 1.00 8.22   ? 1060 GLY B O     1 
ATOM   18997 N  N     . THR B 2  1061 ? 122.442 169.053 127.033 1.00 6.50   ? 1061 THR B N     1 
ATOM   18998 C  CA    . THR B 2  1061 ? 122.685 168.338 128.274 1.00 7.52   ? 1061 THR B CA    1 
ATOM   18999 C  C     . THR B 2  1061 ? 121.436 167.594 128.721 1.00 10.55  ? 1061 THR B C     1 
ATOM   19000 O  O     . THR B 2  1061 ? 120.308 168.027 128.477 1.00 13.22  ? 1061 THR B O     1 
ATOM   19001 C  CB    . THR B 2  1061 ? 123.127 169.314 129.365 1.00 5.49   ? 1061 THR B CB    1 
ATOM   19002 O  OG1   . THR B 2  1061 ? 124.018 170.278 128.799 1.00 10.50  ? 1061 THR B OG1   1 
ATOM   19003 C  CG2   . THR B 2  1061 ? 123.826 168.586 130.490 1.00 3.35   ? 1061 THR B CG2   1 
ATOM   19004 N  N     . ALA B 2  1062 ? 121.648 166.460 129.381 1.00 5.39   ? 1062 ALA B N     1 
ATOM   19005 C  CA    . ALA B 2  1062 ? 120.541 165.680 129.904 1.00 7.63   ? 1062 ALA B CA    1 
ATOM   19006 C  C     . ALA B 2  1062 ? 119.725 166.503 130.890 1.00 3.19   ? 1062 ALA B C     1 
ATOM   19007 O  O     . ALA B 2  1062 ? 120.245 167.378 131.578 1.00 13.12  ? 1062 ALA B O     1 
ATOM   19008 C  CB    . ALA B 2  1062 ? 121.062 164.419 130.583 1.00 4.28   ? 1062 ALA B CB    1 
ATOM   19009 N  N     . PHE B 2  1063 ? 118.424 166.227 130.930 1.00 4.20   ? 1063 PHE B N     1 
ATOM   19010 C  CA    . PHE B 2  1063 ? 117.454 166.766 131.879 1.00 3.08   ? 1063 PHE B CA    1 
ATOM   19011 C  C     . PHE B 2  1063 ? 117.171 168.245 131.695 1.00 5.20   ? 1063 PHE B C     1 
ATOM   19012 O  O     . PHE B 2  1063 ? 116.520 168.848 132.546 1.00 12.79  ? 1063 PHE B O     1 
ATOM   19013 C  CB    . PHE B 2  1063 ? 117.862 166.507 133.333 1.00 1.60   ? 1063 PHE B CB    1 
ATOM   19014 C  CG    . PHE B 2  1063 ? 118.067 165.074 133.642 1.00 7.38   ? 1063 PHE B CG    1 
ATOM   19015 C  CD1   . PHE B 2  1063 ? 117.015 164.197 133.598 1.00 1.95   ? 1063 PHE B CD1   1 
ATOM   19016 C  CD2   . PHE B 2  1063 ? 119.309 164.597 133.964 1.00 11.37  ? 1063 PHE B CD2   1 
ATOM   19017 C  CE1   . PHE B 2  1063 ? 117.201 162.881 133.864 1.00 1.13   ? 1063 PHE B CE1   1 
ATOM   19018 C  CE2   . PHE B 2  1063 ? 119.497 163.279 134.223 1.00 1.11   ? 1063 PHE B CE2   1 
ATOM   19019 C  CZ    . PHE B 2  1063 ? 118.442 162.422 134.176 1.00 1.61   ? 1063 PHE B CZ    1 
ATOM   19020 N  N     . LEU B 2  1064 ? 117.642 168.844 130.637 1.00 4.88   ? 1064 LEU B N     1 
ATOM   19021 C  CA    . LEU B 2  1064 ? 117.120 170.139 130.250 1.00 5.13   ? 1064 LEU B CA    1 
ATOM   19022 C  C     . LEU B 2  1064 ? 115.768 169.941 129.573 1.00 9.42   ? 1064 LEU B C     1 
ATOM   19023 O  O     . LEU B 2  1064 ? 115.475 168.853 129.080 1.00 14.90  ? 1064 LEU B O     1 
ATOM   19024 C  CB    . LEU B 2  1064 ? 118.085 170.843 129.309 1.00 4.20   ? 1064 LEU B CB    1 
ATOM   19025 C  CG    . LEU B 2  1064 ? 119.377 171.415 129.896 1.00 7.05   ? 1064 LEU B CG    1 
ATOM   19026 C  CD1   . LEU B 2  1064 ? 120.264 171.910 128.779 1.00 10.25  ? 1064 LEU B CD1   1 
ATOM   19027 C  CD2   . LEU B 2  1064 ? 119.103 172.525 130.878 1.00 6.85   ? 1064 LEU B CD2   1 
ATOM   19028 N  N     . PRO B 2  1065 ? 114.902 170.952 129.577 1.00 10.72  ? 1065 PRO B N     1 
ATOM   19029 C  CA    . PRO B 2  1065 ? 113.604 170.799 128.911 1.00 9.21   ? 1065 PRO B CA    1 
ATOM   19030 C  C     . PRO B 2  1065 ? 113.777 170.666 127.406 1.00 8.23   ? 1065 PRO B C     1 
ATOM   19031 O  O     . PRO B 2  1065 ? 114.556 171.396 126.793 1.00 12.57  ? 1065 PRO B O     1 
ATOM   19032 C  CB    . PRO B 2  1065 ? 112.862 172.085 129.282 1.00 10.98  ? 1065 PRO B CB    1 
ATOM   19033 C  CG    . PRO B 2  1065 ? 113.915 173.037 129.633 1.00 9.91   ? 1065 PRO B CG    1 
ATOM   19034 C  CD    . PRO B 2  1065 ? 115.007 172.249 130.258 1.00 11.80  ? 1065 PRO B CD    1 
ATOM   19035 N  N     . ILE B 2  1066 ? 113.054 169.720 126.810 1.00 11.90  ? 1066 ILE B N     1 
ATOM   19036 C  CA    . ILE B 2  1066 ? 113.082 169.537 125.367 1.00 12.42  ? 1066 ILE B CA    1 
ATOM   19037 C  C     . ILE B 2  1066 ? 111.661 169.431 124.836 1.00 10.21  ? 1066 ILE B C     1 
ATOM   19038 O  O     . ILE B 2  1066 ? 110.714 169.141 125.566 1.00 20.11  ? 1066 ILE B O     1 
ATOM   19039 C  CB    . ILE B 2  1066 ? 113.897 168.306 124.928 1.00 10.11  ? 1066 ILE B CB    1 
ATOM   19040 C  CG1   . ILE B 2  1066 ? 113.106 167.031 125.141 1.00 7.40   ? 1066 ILE B CG1   1 
ATOM   19041 C  CG2   . ILE B 2  1066 ? 115.208 168.240 125.662 1.00 14.51  ? 1066 ILE B CG2   1 
ATOM   19042 C  CD1   . ILE B 2  1066 ? 113.482 165.966 124.170 1.00 11.70  ? 1066 ILE B CD1   1 
ATOM   19043 N  N     . ASN B 2  1067 ? 111.529 169.680 123.540 1.00 4.10   ? 1067 ASN B N     1 
ATOM   19044 C  CA    . ASN B 2  1067 ? 110.251 169.620 122.839 1.00 5.70   ? 1067 ASN B CA    1 
ATOM   19045 C  C     . ASN B 2  1067 ? 110.571 169.247 121.399 1.00 9.26   ? 1067 ASN B C     1 
ATOM   19046 O  O     . ASN B 2  1067 ? 110.958 170.105 120.608 1.00 15.37  ? 1067 ASN B O     1 
ATOM   19047 C  CB    . ASN B 2  1067 ? 109.514 170.947 122.923 1.00 6.41   ? 1067 ASN B CB    1 
ATOM   19048 C  CG    . ASN B 2  1067 ? 108.041 170.806 122.700 1.00 13.19  ? 1067 ASN B CG    1 
ATOM   19049 O  OD1   . ASN B 2  1067 ? 107.538 169.710 122.514 1.00 21.67  ? 1067 ASN B OD1   1 
ATOM   19050 N  ND2   . ASN B 2  1067 ? 107.336 171.917 122.706 1.00 13.84  ? 1067 ASN B ND2   1 
ATOM   19051 N  N     . VAL B 2  1068 ? 110.431 167.964 121.072 1.00 3.76   ? 1068 VAL B N     1 
ATOM   19052 C  CA    . VAL B 2  1068 ? 110.768 167.492 119.735 1.00 0.76   ? 1068 VAL B CA    1 
ATOM   19053 C  C     . VAL B 2  1068 ? 109.822 168.071 118.695 1.00 4.71   ? 1068 VAL B C     1 
ATOM   19054 O  O     . VAL B 2  1068 ? 110.184 168.203 117.526 1.00 12.21  ? 1068 VAL B O     1 
ATOM   19055 C  CB    . VAL B 2  1068 ? 110.789 165.955 119.722 1.00 5.56   ? 1068 VAL B CB    1 
ATOM   19056 C  CG1   . VAL B 2  1068 ? 111.081 165.427 118.348 1.00 7.41   ? 1068 VAL B CG1   1 
ATOM   19057 C  CG2   . VAL B 2  1068 ? 111.838 165.463 120.670 1.00 3.71   ? 1068 VAL B CG2   1 
ATOM   19058 N  N     . GLN B 2  1069 ? 108.604 168.425 119.092 1.00 7.62   ? 1069 GLN B N     1 
ATOM   19059 C  CA    . GLN B 2  1069 ? 107.695 169.105 118.180 1.00 2.29   ? 1069 GLN B CA    1 
ATOM   19060 C  C     . GLN B 2  1069 ? 108.212 170.481 117.793 1.00 5.72   ? 1069 GLN B C     1 
ATOM   19061 O  O     . GLN B 2  1069 ? 108.153 170.866 116.623 1.00 10.31  ? 1069 GLN B O     1 
ATOM   19062 C  CB    . GLN B 2  1069 ? 106.314 169.207 118.818 1.00 5.53   ? 1069 GLN B CB    1 
ATOM   19063 C  CG    . GLN B 2  1069 ? 105.369 170.174 118.152 1.00 6.72   ? 1069 GLN B CG    1 
ATOM   19064 C  CD    . GLN B 2  1069 ? 104.832 169.678 116.839 1.00 10.96  ? 1069 GLN B CD    1 
ATOM   19065 O  OE1   . GLN B 2  1069 ? 104.543 168.497 116.677 1.00 14.37  ? 1069 GLN B OE1   1 
ATOM   19066 N  NE2   . GLN B 2  1069 ? 104.677 170.584 115.894 1.00 11.65  ? 1069 GLN B NE2   1 
ATOM   19067 N  N     . LEU B 2  1070 ? 108.714 171.242 118.760 1.00 6.95   ? 1070 LEU B N     1 
ATOM   19068 C  CA    . LEU B 2  1070 ? 109.200 172.583 118.474 1.00 6.37   ? 1070 LEU B CA    1 
ATOM   19069 C  C     . LEU B 2  1070 ? 110.550 172.565 117.784 1.00 10.85  ? 1070 LEU B C     1 
ATOM   19070 O  O     . LEU B 2  1070 ? 110.872 173.496 117.044 1.00 15.73  ? 1070 LEU B O     1 
ATOM   19071 C  CB    . LEU B 2  1070 ? 109.290 173.401 119.756 1.00 11.68  ? 1070 LEU B CB    1 
ATOM   19072 C  CG    . LEU B 2  1070 ? 108.013 174.072 120.238 1.00 16.43  ? 1070 LEU B CG    1 
ATOM   19073 C  CD1   . LEU B 2  1070 ? 108.294 174.831 121.503 1.00 16.01  ? 1070 LEU B CD1   1 
ATOM   19074 C  CD2   . LEU B 2  1070 ? 107.462 174.993 119.175 1.00 12.37  ? 1070 LEU B CD2   1 
ATOM   19075 N  N     . LEU B 2  1071 ? 111.354 171.534 118.030 1.00 11.75  ? 1071 LEU B N     1 
ATOM   19076 C  CA    . LEU B 2  1071 ? 112.616 171.386 117.327 1.00 3.96   ? 1071 LEU B CA    1 
ATOM   19077 C  C     . LEU B 2  1071 ? 112.396 171.029 115.866 1.00 8.40   ? 1071 LEU B C     1 
ATOM   19078 O  O     . LEU B 2  1071 ? 113.158 171.468 115.003 1.00 12.18  ? 1071 LEU B O     1 
ATOM   19079 C  CB    . LEU B 2  1071 ? 113.469 170.329 118.018 1.00 3.16   ? 1071 LEU B CB    1 
ATOM   19080 C  CG    . LEU B 2  1071 ? 113.980 170.648 119.421 1.00 3.63   ? 1071 LEU B CG    1 
ATOM   19081 C  CD1   . LEU B 2  1071 ? 114.522 169.397 120.087 1.00 6.46   ? 1071 LEU B CD1   1 
ATOM   19082 C  CD2   . LEU B 2  1071 ? 115.031 171.741 119.400 1.00 6.87   ? 1071 LEU B CD2   1 
ATOM   19083 N  N     . SER B 2  1072 ? 111.367 170.241 115.572 1.00 6.02   ? 1072 SER B N     1 
ATOM   19084 C  CA    . SER B 2  1072 ? 111.042 169.890 114.199 1.00 4.94   ? 1072 SER B CA    1 
ATOM   19085 C  C     . SER B 2  1072 ? 110.441 171.055 113.425 1.00 8.82   ? 1072 SER B C     1 
ATOM   19086 O  O     . SER B 2  1072 ? 110.465 171.048 112.194 1.00 8.43   ? 1072 SER B O     1 
ATOM   19087 C  CB    . SER B 2  1072 ? 110.085 168.705 114.183 1.00 8.23   ? 1072 SER B CB    1 
ATOM   19088 O  OG    . SER B 2  1072 ? 110.677 167.564 114.764 1.00 8.40   ? 1072 SER B OG    1 
ATOM   19089 N  N     . GLU B 2  1073 ? 109.875 172.042 114.116 1.00 13.72  ? 1073 GLU B N     1 
ATOM   19090 C  CA    . GLU B 2  1073 ? 109.393 173.241 113.443 1.00 10.50  ? 1073 GLU B CA    1 
ATOM   19091 C  C     . GLU B 2  1073 ? 110.515 174.232 113.181 1.00 13.44  ? 1073 GLU B C     1 
ATOM   19092 O  O     . GLU B 2  1073 ? 110.399 175.076 112.291 1.00 23.25  ? 1073 GLU B O     1 
ATOM   19093 C  CB    . GLU B 2  1073 ? 108.288 173.877 114.269 1.00 10.76  ? 1073 GLU B CB    1 
ATOM   19094 C  CG    . GLU B 2  1073 ? 107.058 173.016 114.324 1.00 13.01  ? 1073 GLU B CG    1 
ATOM   19095 C  CD    . GLU B 2  1073 ? 106.038 173.504 115.310 1.00 22.62  ? 1073 GLU B CD    1 
ATOM   19096 O  OE1   . GLU B 2  1073 ? 106.288 174.528 115.974 1.00 24.03  ? 1073 GLU B OE1   1 
ATOM   19097 O  OE2   . GLU B 2  1073 ? 104.976 172.862 115.416 1.00 24.13  ? 1073 GLU B OE2   1 
ATOM   19098 N  N     . ARG B 2  1074 ? 111.600 174.145 113.944 1.00 6.41   ? 1074 ARG B N     1 
ATOM   19099 C  CA    . ARG B 2  1074 ? 112.803 174.912 113.656 1.00 6.19   ? 1074 ARG B CA    1 
ATOM   19100 C  C     . ARG B 2  1074 ? 113.396 174.530 112.311 1.00 9.89   ? 1074 ARG B C     1 
ATOM   19101 O  O     . ARG B 2  1074 ? 113.922 175.388 111.601 1.00 15.64  ? 1074 ARG B O     1 
ATOM   19102 C  CB    . ARG B 2  1074 ? 113.820 174.677 114.770 1.00 12.56  ? 1074 ARG B CB    1 
ATOM   19103 C  CG    . ARG B 2  1074 ? 114.910 175.695 114.921 1.00 7.89   ? 1074 ARG B CG    1 
ATOM   19104 C  CD    . ARG B 2  1074 ? 115.775 175.295 116.093 1.00 7.58   ? 1074 ARG B CD    1 
ATOM   19105 N  NE    . ARG B 2  1074 ? 117.139 175.793 115.995 1.00 13.61  ? 1074 ARG B NE    1 
ATOM   19106 C  CZ    . ARG B 2  1074 ? 118.221 175.064 116.215 1.00 8.73   ? 1074 ARG B CZ    1 
ATOM   19107 N  NH1   . ARG B 2  1074 ? 118.138 173.782 116.508 1.00 5.80   ? 1074 ARG B NH1   1 
ATOM   19108 N  NH2   . ARG B 2  1074 ? 119.414 175.641 116.152 1.00 6.96   ? 1074 ARG B NH2   1 
ATOM   19109 N  N     . LEU B 2  1075 ? 113.333 173.246 111.954 1.00 13.77  ? 1075 LEU B N     1 
ATOM   19110 C  CA    . LEU B 2  1075 ? 113.847 172.792 110.667 1.00 10.74  ? 1075 LEU B CA    1 
ATOM   19111 C  C     . LEU B 2  1075 ? 113.087 173.425 109.519 1.00 9.00   ? 1075 LEU B C     1 
ATOM   19112 O  O     . LEU B 2  1075 ? 113.683 173.866 108.535 1.00 12.66  ? 1075 LEU B O     1 
ATOM   19113 C  CB    . LEU B 2  1075 ? 113.758 171.274 110.572 1.00 6.47   ? 1075 LEU B CB    1 
ATOM   19114 C  CG    . LEU B 2  1075 ? 114.852 170.491 111.269 1.00 4.64   ? 1075 LEU B CG    1 
ATOM   19115 C  CD1   . LEU B 2  1075 ? 114.522 169.037 111.248 1.00 3.52   ? 1075 LEU B CD1   1 
ATOM   19116 C  CD2   . LEU B 2  1075 ? 116.148 170.746 110.578 1.00 5.56   ? 1075 LEU B CD2   1 
ATOM   19117 N  N     . ALA B 2  1076 ? 111.764 173.471 109.625 1.00 6.74   ? 1076 ALA B N     1 
ATOM   19118 C  CA    . ALA B 2  1076 ? 110.961 174.080 108.579 1.00 8.32   ? 1076 ALA B CA    1 
ATOM   19119 C  C     . ALA B 2  1076 ? 111.237 175.571 108.462 1.00 17.64  ? 1076 ALA B C     1 
ATOM   19120 O  O     . ALA B 2  1076 ? 111.204 176.121 107.357 1.00 22.00  ? 1076 ALA B O     1 
ATOM   19121 C  CB    . ALA B 2  1076 ? 109.483 173.812 108.846 1.00 7.23   ? 1076 ALA B CB    1 
ATOM   19122 N  N     . GLN B 2  1077 ? 111.514 176.240 109.581 1.00 19.23  ? 1077 GLN B N     1 
ATOM   19123 C  CA    . GLN B 2  1077 ? 111.841 177.660 109.549 1.00 17.84  ? 1077 GLN B CA    1 
ATOM   19124 C  C     . GLN B 2  1077 ? 113.168 177.936 108.862 1.00 15.79  ? 1077 GLN B C     1 
ATOM   19125 O  O     . GLN B 2  1077 ? 113.411 179.070 108.451 1.00 23.43  ? 1077 GLN B O     1 
ATOM   19126 C  CB    . GLN B 2  1077 ? 111.874 178.222 110.967 1.00 20.01  ? 1077 GLN B CB    1 
ATOM   19127 C  CG    . GLN B 2  1077 ? 110.574 178.851 111.416 1.00 21.22  ? 1077 GLN B CG    1 
ATOM   19128 C  CD    . GLN B 2  1077 ? 110.195 178.468 112.836 1.00 25.46  ? 1077 GLN B CD    1 
ATOM   19129 O  OE1   . GLN B 2  1077 ? 111.055 178.328 113.706 1.00 26.89  ? 1077 GLN B OE1   1 
ATOM   19130 N  NE2   . GLN B 2  1077 ? 108.899 178.299 113.077 1.00 21.48  ? 1077 GLN B NE2   1 
ATOM   19131 N  N     . GLU B 2  1078 ? 114.027 176.933 108.738 1.00 18.94  ? 1078 GLU B N     1 
ATOM   19132 C  CA    . GLU B 2  1078 ? 115.333 177.062 108.114 1.00 17.99  ? 1078 GLU B CA    1 
ATOM   19133 C  C     . GLU B 2  1078 ? 115.326 176.664 106.647 1.00 19.05  ? 1078 GLU B C     1 
ATOM   19134 O  O     . GLU B 2  1078 ? 116.387 176.640 106.020 1.00 18.85  ? 1078 GLU B O     1 
ATOM   19135 C  CB    . GLU B 2  1078 ? 116.354 176.218 108.878 1.00 14.92  ? 1078 GLU B CB    1 
ATOM   19136 C  CG    . GLU B 2  1078 ? 117.749 176.799 108.894 1.00 23.29  ? 1078 GLU B CG    1 
ATOM   19137 C  CD    . GLU B 2  1078 ? 117.816 178.106 109.645 1.00 27.49  ? 1078 GLU B CD    1 
ATOM   19138 O  OE1   . GLU B 2  1078 ? 117.177 178.202 110.710 1.00 25.00  ? 1078 GLU B OE1   1 
ATOM   19139 O  OE2   . GLU B 2  1078 ? 118.499 179.039 109.176 1.00 24.82  ? 1078 GLU B OE2   1 
ATOM   19140 N  N     . GLY B 2  1079 ? 114.160 176.348 106.089 1.00 19.24  ? 1079 GLY B N     1 
ATOM   19141 C  CA    . GLY B 2  1079 ? 114.039 175.952 104.704 1.00 19.60  ? 1079 GLY B CA    1 
ATOM   19142 C  C     . GLY B 2  1079 ? 114.004 174.462 104.453 1.00 21.58  ? 1079 GLY B C     1 
ATOM   19143 O  O     . GLY B 2  1079 ? 113.843 174.054 103.301 1.00 23.27  ? 1079 GLY B O     1 
ATOM   19144 N  N     . LEU B 2  1080 ? 114.144 173.642 105.485 1.00 11.34  ? 1080 LEU B N     1 
ATOM   19145 C  CA    . LEU B 2  1080 ? 114.163 172.199 105.350 1.00 7.83   ? 1080 LEU B CA    1 
ATOM   19146 C  C     . LEU B 2  1080 ? 112.758 171.642 105.543 1.00 5.27   ? 1080 LEU B C     1 
ATOM   19147 O  O     . LEU B 2  1080 ? 111.793 172.380 105.729 1.00 13.68  ? 1080 LEU B O     1 
ATOM   19148 C  CB    . LEU B 2  1080 ? 115.158 171.601 106.342 1.00 7.61   ? 1080 LEU B CB    1 
ATOM   19149 C  CG    . LEU B 2  1080 ? 116.625 171.950 106.096 1.00 5.77   ? 1080 LEU B CG    1 
ATOM   19150 C  CD1   . LEU B 2  1080 ? 117.470 171.610 107.290 1.00 8.37   ? 1080 LEU B CD1   1 
ATOM   19151 C  CD2   . LEU B 2  1080 ? 117.143 171.211 104.886 1.00 8.56   ? 1080 LEU B CD2   1 
ATOM   19152 N  N     . ARG B 2  1081 ? 112.633 170.323 105.476 1.00 3.02   ? 1081 ARG B N     1 
ATOM   19153 C  CA    . ARG B 2  1081 ? 111.348 169.699 105.740 1.00 3.48   ? 1081 ARG B CA    1 
ATOM   19154 C  C     . ARG B 2  1081 ? 111.129 169.568 107.239 1.00 4.48   ? 1081 ARG B C     1 
ATOM   19155 O  O     . ARG B 2  1081 ? 112.046 169.715 108.042 1.00 13.45  ? 1081 ARG B O     1 
ATOM   19156 C  CB    . ARG B 2  1081 ? 111.247 168.324 105.083 1.00 4.07   ? 1081 ARG B CB    1 
ATOM   19157 C  CG    . ARG B 2  1081 ? 111.278 168.330 103.576 1.00 2.15   ? 1081 ARG B CG    1 
ATOM   19158 C  CD    . ARG B 2  1081 ? 110.909 166.980 103.000 1.00 0.35   ? 1081 ARG B CD    1 
ATOM   19159 N  NE    . ARG B 2  1081 ? 111.267 166.898 101.592 1.00 7.24   ? 1081 ARG B NE    1 
ATOM   19160 C  CZ    . ARG B 2  1081 ? 111.001 165.874 100.798 1.00 2.73   ? 1081 ARG B CZ    1 
ATOM   19161 N  NH1   . ARG B 2  1081 ? 110.361 164.812 101.234 1.00 2.42   ? 1081 ARG B NH1   1 
ATOM   19162 N  NH2   . ARG B 2  1081 ? 111.389 165.918 99.534  1.00 0.81   ? 1081 ARG B NH2   1 
ATOM   19163 N  N     . PHE B 2  1082 ? 109.883 169.288 107.608 1.00 4.69   ? 1082 PHE B N     1 
ATOM   19164 C  CA    . PHE B 2  1082 ? 109.551 169.090 109.010 1.00 7.48   ? 1082 PHE B CA    1 
ATOM   19165 C  C     . PHE B 2  1082 ? 110.297 167.896 109.590 1.00 4.64   ? 1082 PHE B C     1 
ATOM   19166 O  O     . PHE B 2  1082 ? 110.776 167.945 110.727 1.00 10.08  ? 1082 PHE B O     1 
ATOM   19167 C  CB    . PHE B 2  1082 ? 108.039 168.919 109.150 1.00 0.79   ? 1082 PHE B CB    1 
ATOM   19168 C  CG    . PHE B 2  1082 ? 107.570 168.726 110.557 1.00 9.61   ? 1082 PHE B CG    1 
ATOM   19169 C  CD1   . PHE B 2  1082 ? 107.259 169.810 111.350 1.00 10.96  ? 1082 PHE B CD1   1 
ATOM   19170 C  CD2   . PHE B 2  1082 ? 107.430 167.458 111.084 1.00 8.30   ? 1082 PHE B CD2   1 
ATOM   19171 C  CE1   . PHE B 2  1082 ? 106.834 169.630 112.635 1.00 9.80   ? 1082 PHE B CE1   1 
ATOM   19172 C  CE2   . PHE B 2  1082 ? 107.013 167.279 112.364 1.00 5.44   ? 1082 PHE B CE2   1 
ATOM   19173 C  CZ    . PHE B 2  1082 ? 106.710 168.367 113.144 1.00 7.61   ? 1082 PHE B CZ    1 
ATOM   19174 N  N     . ASN B 2  1083 ? 110.408 166.812 108.829 1.00 7.38   ? 1083 ASN B N     1 
ATOM   19175 C  CA    . ASN B 2  1083 ? 111.040 165.603 109.329 1.00 0.39   ? 1083 ASN B CA    1 
ATOM   19176 C  C     . ASN B 2  1083 ? 112.548 165.585 109.140 1.00 5.47   ? 1083 ASN B C     1 
ATOM   19177 O  O     . ASN B 2  1083 ? 113.202 164.680 109.660 1.00 8.69   ? 1083 ASN B O     1 
ATOM   19178 C  CB    . ASN B 2  1083 ? 110.426 164.373 108.664 1.00 0.22   ? 1083 ASN B CB    1 
ATOM   19179 C  CG    . ASN B 2  1083 ? 110.299 164.509 107.171 1.00 1.94   ? 1083 ASN B CG    1 
ATOM   19180 O  OD1   . ASN B 2  1083 ? 110.599 165.542 106.607 1.00 6.27   ? 1083 ASN B OD1   1 
ATOM   19181 N  ND2   . ASN B 2  1083 ? 109.833 163.464 106.527 1.00 12.86  ? 1083 ASN B ND2   1 
ATOM   19182 N  N     . GLY B 2  1084 ? 113.114 166.558 108.436 1.00 7.53   ? 1084 GLY B N     1 
ATOM   19183 C  CA    . GLY B 2  1084 ? 114.533 166.549 108.178 1.00 10.18  ? 1084 GLY B CA    1 
ATOM   19184 C  C     . GLY B 2  1084 ? 114.980 165.545 107.148 1.00 3.56   ? 1084 GLY B C     1 
ATOM   19185 O  O     . GLY B 2  1084 ? 116.145 165.156 107.148 1.00 17.22  ? 1084 GLY B O     1 
ATOM   19186 N  N     . CYS B 2  1085 ? 114.086 165.113 106.270 1.00 3.78   ? 1085 CYS B N     1 
ATOM   19187 C  CA    . CYS B 2  1085 ? 114.378 164.132 105.241 1.00 8.11   ? 1085 CYS B CA    1 
ATOM   19188 C  C     . CYS B 2  1085 ? 114.450 164.816 103.885 1.00 3.33   ? 1085 CYS B C     1 
ATOM   19189 O  O     . CYS B 2  1085 ? 113.777 165.813 103.647 1.00 10.04  ? 1085 CYS B O     1 
ATOM   19190 C  CB    . CYS B 2  1085 ? 113.311 163.042 105.223 1.00 5.22   ? 1085 CYS B CB    1 
ATOM   19191 S  SG    . CYS B 2  1085 ? 113.265 161.964 106.656 1.00 4.42   ? 1085 CYS B SG    1 
ATOM   19192 N  N     . GLN B 2  1086 ? 115.278 164.281 102.996 1.00 12.26  ? 1086 GLN B N     1 
ATOM   19193 C  CA    . GLN B 2  1086 ? 115.492 164.884 101.692 1.00 6.78   ? 1086 GLN B CA    1 
ATOM   19194 C  C     . GLN B 2  1086 ? 115.341 163.854 100.592 1.00 3.61   ? 1086 GLN B C     1 
ATOM   19195 O  O     . GLN B 2  1086 ? 115.390 162.650 100.833 1.00 0.27   ? 1086 GLN B O     1 
ATOM   19196 C  CB    . GLN B 2  1086 ? 116.876 165.508 101.549 1.00 3.24   ? 1086 GLN B CB    1 
ATOM   19197 C  CG    . GLN B 2  1086 ? 117.365 166.288 102.719 1.00 10.85  ? 1086 GLN B CG    1 
ATOM   19198 C  CD    . GLN B 2  1086 ? 118.418 167.253 102.308 1.00 6.36   ? 1086 GLN B CD    1 
ATOM   19199 O  OE1   . GLN B 2  1086 ? 118.440 167.691 101.170 1.00 10.35  ? 1086 GLN B OE1   1 
ATOM   19200 N  NE2   . GLN B 2  1086 ? 119.304 167.594 103.217 1.00 1.89   ? 1086 GLN B NE2   1 
ATOM   19201 N  N     . LYS B 2  1087 ? 115.173 164.352 99.375  1.00 4.24   ? 1087 LYS B N     1 
ATOM   19202 C  CA    . LYS B 2  1087 ? 115.244 163.521 98.183  1.00 2.18   ? 1087 LYS B CA    1 
ATOM   19203 C  C     . LYS B 2  1087 ? 116.687 163.115 97.901  1.00 6.86   ? 1087 LYS B C     1 
ATOM   19204 O  O     . LYS B 2  1087 ? 117.584 163.957 97.884  1.00 1.00   ? 1087 LYS B O     1 
ATOM   19205 C  CB    . LYS B 2  1087 ? 114.656 164.291 97.010  1.00 10.68  ? 1087 LYS B CB    1 
ATOM   19206 C  CG    . LYS B 2  1087 ? 114.769 163.626 95.670  1.00 5.37   ? 1087 LYS B CG    1 
ATOM   19207 C  CD    . LYS B 2  1087 ? 114.420 164.608 94.593  1.00 1.60   ? 1087 LYS B CD    1 
ATOM   19208 C  CE    . LYS B 2  1087 ? 113.040 165.164 94.823  1.00 1.83   ? 1087 LYS B CE    1 
ATOM   19209 N  NZ    . LYS B 2  1087 ? 112.699 166.290 93.944  1.00 8.11   ? 1087 LYS B NZ    1 
ATOM   19210 N  N     . MET B 2  1088 ? 116.910 161.826 97.667  1.00 10.46  ? 1088 MET B N     1 
ATOM   19211 C  CA    . MET B 2  1088 ? 118.243 161.282 97.471  1.00 3.52   ? 1088 MET B CA    1 
ATOM   19212 C  C     . MET B 2  1088 ? 118.279 160.466 96.190  1.00 15.17  ? 1088 MET B C     1 
ATOM   19213 O  O     . MET B 2  1088 ? 117.251 160.003 95.706  1.00 13.45  ? 1088 MET B O     1 
ATOM   19214 C  CB    . MET B 2  1088 ? 118.681 160.408 98.654  1.00 5.86   ? 1088 MET B CB    1 
ATOM   19215 C  CG    . MET B 2  1088 ? 119.249 161.173 99.826  1.00 2.57   ? 1088 MET B CG    1 
ATOM   19216 S  SD    . MET B 2  1088 ? 120.310 160.206 100.898 1.00 4.63   ? 1088 MET B SD    1 
ATOM   19217 C  CE    . MET B 2  1088 ? 121.897 160.933 100.616 1.00 15.39  ? 1088 MET B CE    1 
ATOM   19218 N  N     . PHE B 2  1089 ? 119.477 160.316 95.636  1.00 0.48   ? 1089 PHE B N     1 
ATOM   19219 C  CA    . PHE B 2  1089 ? 119.722 159.528 94.440  1.00 2.35   ? 1089 PHE B CA    1 
ATOM   19220 C  C     . PHE B 2  1089 ? 120.743 158.447 94.736  1.00 0.24   ? 1089 PHE B C     1 
ATOM   19221 O  O     . PHE B 2  1089 ? 121.627 158.617 95.574  1.00 12.42  ? 1089 PHE B O     1 
ATOM   19222 C  CB    . PHE B 2  1089 ? 120.246 160.384 93.291  1.00 12.45  ? 1089 PHE B CB    1 
ATOM   19223 C  CG    . PHE B 2  1089 ? 119.319 161.454 92.859  1.00 7.37   ? 1089 PHE B CG    1 
ATOM   19224 C  CD1   . PHE B 2  1089 ? 119.239 162.631 93.566  1.00 9.60   ? 1089 PHE B CD1   1 
ATOM   19225 C  CD2   . PHE B 2  1089 ? 118.548 161.308 91.736  1.00 10.66  ? 1089 PHE B CD2   1 
ATOM   19226 C  CE1   . PHE B 2  1089 ? 118.395 163.616 93.177  1.00 13.42  ? 1089 PHE B CE1   1 
ATOM   19227 C  CE2   . PHE B 2  1089 ? 117.703 162.298 91.345  1.00 11.79  ? 1089 PHE B CE2   1 
ATOM   19228 C  CZ    . PHE B 2  1089 ? 117.626 163.450 92.064  1.00 14.82  ? 1089 PHE B CZ    1 
ATOM   19229 N  N     . ASN B 2  1090 ? 120.610 157.333 94.035  1.00 8.90   ? 1090 ASN B N     1 
ATOM   19230 C  CA    . ASN B 2  1090 ? 121.586 156.258 94.082  1.00 15.26  ? 1090 ASN B CA    1 
ATOM   19231 C  C     . ASN B 2  1090 ? 122.813 156.695 93.302  1.00 3.08   ? 1090 ASN B C     1 
ATOM   19232 O  O     . ASN B 2  1090 ? 122.700 157.129 92.155  1.00 8.14   ? 1090 ASN B O     1 
ATOM   19233 C  CB    . ASN B 2  1090 ? 120.980 154.990 93.490  1.00 2.98   ? 1090 ASN B CB    1 
ATOM   19234 C  CG    . ASN B 2  1090 ? 121.754 153.745 93.832  1.00 1.57   ? 1090 ASN B CG    1 
ATOM   19235 O  OD1   . ASN B 2  1090 ? 122.837 153.513 93.320  1.00 9.19   ? 1090 ASN B OD1   1 
ATOM   19236 N  ND2   . ASN B 2  1090 ? 121.185 152.922 94.684  1.00 5.84   ? 1090 ASN B ND2   1 
ATOM   19237 N  N     . GLY B 2  1091 ? 123.987 156.591 93.917  1.00 3.86   ? 1091 GLY B N     1 
ATOM   19238 C  CA    . GLY B 2  1091 ? 125.183 157.056 93.251  1.00 4.37   ? 1091 GLY B CA    1 
ATOM   19239 C  C     . GLY B 2  1091 ? 125.631 156.159 92.122  1.00 13.29  ? 1091 GLY B C     1 
ATOM   19240 O  O     . GLY B 2  1091 ? 126.319 156.608 91.208  1.00 0.78   ? 1091 GLY B O     1 
ATOM   19241 N  N     . GLN B 2  1092 ? 125.243 154.891 92.157  1.00 8.27   ? 1092 GLN B N     1 
ATOM   19242 C  CA    . GLN B 2  1092 ? 125.738 153.933 91.179  1.00 6.75   ? 1092 GLN B CA    1 
ATOM   19243 C  C     . GLN B 2  1092 ? 124.908 153.932 89.907  1.00 3.41   ? 1092 GLN B C     1 
ATOM   19244 O  O     . GLN B 2  1092 ? 125.445 153.727 88.816  1.00 2.65   ? 1092 GLN B O     1 
ATOM   19245 C  CB    . GLN B 2  1092 ? 125.779 152.548 91.805  1.00 9.60   ? 1092 GLN B CB    1 
ATOM   19246 C  CG    . GLN B 2  1092 ? 126.710 152.493 92.977  1.00 0.05   ? 1092 GLN B CG    1 
ATOM   19247 C  CD    . GLN B 2  1092 ? 126.420 151.354 93.907  1.00 6.02   ? 1092 GLN B CD    1 
ATOM   19248 O  OE1   . GLN B 2  1092 ? 125.521 150.560 93.670  1.00 3.98   ? 1092 GLN B OE1   1 
ATOM   19249 N  NE2   . GLN B 2  1092 ? 127.173 151.275 94.988  1.00 7.75   ? 1092 GLN B NE2   1 
ATOM   19250 N  N     . THR B 2  1093 ? 123.608 154.178 90.019  1.00 0.41   ? 1093 THR B N     1 
ATOM   19251 C  CA    . THR B 2  1093 ? 122.734 154.224 88.861  1.00 2.54   ? 1093 THR B CA    1 
ATOM   19252 C  C     . THR B 2  1093 ? 122.232 155.617 88.529  1.00 2.46   ? 1093 THR B C     1 
ATOM   19253 O  O     . THR B 2  1093 ? 121.881 155.863 87.375  1.00 4.61   ? 1093 THR B O     1 
ATOM   19254 C  CB    . THR B 2  1093 ? 121.523 153.309 89.069  1.00 4.34   ? 1093 THR B CB    1 
ATOM   19255 O  OG1   . THR B 2  1093 ? 120.892 153.627 90.310  1.00 5.95   ? 1093 THR B OG1   1 
ATOM   19256 C  CG2   . THR B 2  1093 ? 121.957 151.883 89.124  1.00 1.06   ? 1093 THR B CG2   1 
ATOM   19257 N  N     . GLY B 2  1094 ? 122.199 156.529 89.494  1.00 0.76   ? 1094 GLY B N     1 
ATOM   19258 C  CA    . GLY B 2  1094 ? 121.654 157.847 89.260  1.00 9.01   ? 1094 GLY B CA    1 
ATOM   19259 C  C     . GLY B 2  1094 ? 120.167 157.957 89.452  1.00 7.75   ? 1094 GLY B C     1 
ATOM   19260 O  O     . GLY B 2  1094 ? 119.590 158.992 89.125  1.00 10.89  ? 1094 GLY B O     1 
ATOM   19261 N  N     . GLU B 2  1095 ? 119.530 156.928 89.991  1.00 12.72  ? 1095 GLU B N     1 
ATOM   19262 C  CA    . GLU B 2  1095 ? 118.089 156.880 90.161  1.00 12.55  ? 1095 GLU B CA    1 
ATOM   19263 C  C     . GLU B 2  1095 ? 117.715 157.356 91.551  1.00 13.07  ? 1095 GLU B C     1 
ATOM   19264 O  O     . GLU B 2  1095 ? 118.442 157.102 92.510  1.00 4.13   ? 1095 GLU B O     1 
ATOM   19265 C  CB    . GLU B 2  1095 ? 117.579 155.463 89.957  1.00 0.67   ? 1095 GLU B CB    1 
ATOM   19266 C  CG    . GLU B 2  1095 ? 118.142 154.793 88.756  1.00 3.54   ? 1095 GLU B CG    1 
ATOM   19267 C  CD    . GLU B 2  1095 ? 117.180 153.809 88.173  1.00 10.84  ? 1095 GLU B CD    1 
ATOM   19268 O  OE1   . GLU B 2  1095 ? 115.998 153.867 88.548  1.00 8.76   ? 1095 GLU B OE1   1 
ATOM   19269 O  OE2   . GLU B 2  1095 ? 117.603 152.966 87.362  1.00 13.04  ? 1095 GLU B OE2   1 
ATOM   19270 N  N     . TYR B 2  1096 ? 116.575 158.021 91.659  1.00 0.64   ? 1096 TYR B N     1 
ATOM   19271 C  CA    . TYR B 2  1096 ? 116.128 158.526 92.944  1.00 14.43  ? 1096 TYR B CA    1 
ATOM   19272 C  C     . TYR B 2  1096 ? 115.315 157.479 93.685  1.00 9.36   ? 1096 TYR B C     1 
ATOM   19273 O  O     . TYR B 2  1096 ? 114.639 156.650 93.077  1.00 6.22   ? 1096 TYR B O     1 
ATOM   19274 C  CB    . TYR B 2  1096 ? 115.310 159.797 92.753  1.00 7.27   ? 1096 TYR B CB    1 
ATOM   19275 C  CG    . TYR B 2  1096 ? 114.074 159.649 91.894  1.00 2.15   ? 1096 TYR B CG    1 
ATOM   19276 C  CD1   . TYR B 2  1096 ? 114.132 159.824 90.527  1.00 1.02   ? 1096 TYR B CD1   1 
ATOM   19277 C  CD2   . TYR B 2  1096 ? 112.850 159.364 92.452  1.00 2.44   ? 1096 TYR B CD2   1 
ATOM   19278 C  CE1   . TYR B 2  1096 ? 113.015 159.702 89.751  1.00 14.73  ? 1096 TYR B CE1   1 
ATOM   19279 C  CE2   . TYR B 2  1096 ? 111.737 159.240 91.681  1.00 0.67   ? 1096 TYR B CE2   1 
ATOM   19280 C  CZ    . TYR B 2  1096 ? 111.823 159.415 90.333  1.00 0.66   ? 1096 TYR B CZ    1 
ATOM   19281 O  OH    . TYR B 2  1096 ? 110.702 159.295 89.565  1.00 4.70   ? 1096 TYR B OH    1 
ATOM   19282 N  N     . PHE B 2  1097 ? 115.401 157.504 95.009  1.00 14.45  ? 1097 PHE B N     1 
ATOM   19283 C  CA    . PHE B 2  1097 ? 114.556 156.654 95.825  1.00 15.52  ? 1097 PHE B CA    1 
ATOM   19284 C  C     . PHE B 2  1097 ? 113.143 157.214 95.860  1.00 6.48   ? 1097 PHE B C     1 
ATOM   19285 O  O     . PHE B 2  1097 ? 112.929 158.413 95.705  1.00 6.35   ? 1097 PHE B O     1 
ATOM   19286 C  CB    . PHE B 2  1097 ? 115.113 156.547 97.242  1.00 12.39  ? 1097 PHE B CB    1 
ATOM   19287 C  CG    . PHE B 2  1097 ? 116.530 156.089 97.305  1.00 5.37   ? 1097 PHE B CG    1 
ATOM   19288 C  CD1   . PHE B 2  1097 ? 116.845 154.751 97.249  1.00 7.77   ? 1097 PHE B CD1   1 
ATOM   19289 C  CD2   . PHE B 2  1097 ? 117.553 156.998 97.436  1.00 9.30   ? 1097 PHE B CD2   1 
ATOM   19290 C  CE1   . PHE B 2  1097 ? 118.141 154.341 97.308  1.00 5.57   ? 1097 PHE B CE1   1 
ATOM   19291 C  CE2   . PHE B 2  1097 ? 118.847 156.587 97.498  1.00 7.74   ? 1097 PHE B CE2   1 
ATOM   19292 C  CZ    . PHE B 2  1097 ? 119.144 155.265 97.429  1.00 2.72   ? 1097 PHE B CZ    1 
ATOM   19293 N  N     . ASP B 2  1098 ? 112.168 156.338 96.076  1.00 11.87  ? 1098 ASP B N     1 
ATOM   19294 C  CA    . ASP B 2  1098 ? 110.789 156.793 96.172  1.00 0.05   ? 1098 ASP B CA    1 
ATOM   19295 C  C     . ASP B 2  1098 ? 110.431 157.169 97.594  1.00 6.70   ? 1098 ASP B C     1 
ATOM   19296 O  O     . ASP B 2  1098 ? 109.294 156.987 98.018  1.00 23.10  ? 1098 ASP B O     1 
ATOM   19297 C  CB    . ASP B 2  1098 ? 109.834 155.698 95.706  1.00 1.99   ? 1098 ASP B CB    1 
ATOM   19298 C  CG    . ASP B 2  1098 ? 109.840 155.516 94.227  1.00 8.89   ? 1098 ASP B CG    1 
ATOM   19299 O  OD1   . ASP B 2  1098 ? 110.041 156.505 93.507  1.00 14.05  ? 1098 ASP B OD1   1 
ATOM   19300 O  OD2   . ASP B 2  1098 ? 109.645 154.378 93.776  1.00 17.86  ? 1098 ASP B OD2   1 
ATOM   19301 N  N     . ALA B 2  1099 ? 111.361 157.778 98.306  1.00 5.63   ? 1099 ALA B N     1 
ATOM   19302 C  CA    . ALA B 2  1099 ? 111.234 158.014 99.731  1.00 1.53   ? 1099 ALA B CA    1 
ATOM   19303 C  C     . ALA B 2  1099 ? 112.310 158.997 100.127 1.00 10.73  ? 1099 ALA B C     1 
ATOM   19304 O  O     . ALA B 2  1099 ? 113.439 158.903 99.657  1.00 10.30  ? 1099 ALA B O     1 
ATOM   19305 C  CB    . ALA B 2  1099 ? 111.371 156.720 100.537 1.00 11.08  ? 1099 ALA B CB    1 
ATOM   19306 N  N     . ALA B 2  1100 ? 111.944 159.955 100.959 1.00 2.06   ? 1100 ALA B N     1 
ATOM   19307 C  CA    . ALA B 2  1100 ? 112.915 160.890 101.478 1.00 8.29   ? 1100 ALA B CA    1 
ATOM   19308 C  C     . ALA B 2  1100 ? 113.761 160.198 102.536 1.00 0.31   ? 1100 ALA B C     1 
ATOM   19309 O  O     . ALA B 2  1100 ? 113.273 159.358 103.286 1.00 9.99   ? 1100 ALA B O     1 
ATOM   19310 C  CB    . ALA B 2  1100 ? 112.205 162.110 102.046 1.00 0.07   ? 1100 ALA B CB    1 
ATOM   19311 N  N     . ILE B 2  1101 ? 115.041 160.531 102.580 1.00 9.67   ? 1101 ILE B N     1 
ATOM   19312 C  CA    . ILE B 2  1101 ? 115.993 159.872 103.462 1.00 0.88   ? 1101 ILE B CA    1 
ATOM   19313 C  C     . ILE B 2  1101 ? 116.411 160.846 104.548 1.00 5.85   ? 1101 ILE B C     1 
ATOM   19314 O  O     . ILE B 2  1101 ? 116.662 162.021 104.280 1.00 4.74   ? 1101 ILE B O     1 
ATOM   19315 C  CB    . ILE B 2  1101 ? 117.219 159.342 102.688 1.00 6.41   ? 1101 ILE B CB    1 
ATOM   19316 C  CG1   . ILE B 2  1101 ? 116.789 158.395 101.566 1.00 13.11  ? 1101 ILE B CG1   1 
ATOM   19317 C  CG2   . ILE B 2  1101 ? 118.211 158.677 103.615 1.00 4.90   ? 1101 ILE B CG2   1 
ATOM   19318 C  CD1   . ILE B 2  1101 ? 116.198 157.101 102.017 1.00 8.99   ? 1101 ILE B CD1   1 
ATOM   19319 N  N     . PHE B 2  1102 ? 116.482 160.352 105.776 1.00 0.96   ? 1102 PHE B N     1 
ATOM   19320 C  CA    . PHE B 2  1102 ? 116.927 161.139 106.918 1.00 10.84  ? 1102 PHE B CA    1 
ATOM   19321 C  C     . PHE B 2  1102 ? 118.452 161.196 106.924 1.00 8.63   ? 1102 PHE B C     1 
ATOM   19322 O  O     . PHE B 2  1102 ? 119.117 160.188 107.160 1.00 3.03   ? 1102 PHE B O     1 
ATOM   19323 C  CB    . PHE B 2  1102 ? 116.381 160.518 108.198 1.00 2.74   ? 1102 PHE B CB    1 
ATOM   19324 C  CG    . PHE B 2  1102 ? 116.597 161.349 109.416 1.00 2.69   ? 1102 PHE B CG    1 
ATOM   19325 C  CD1   . PHE B 2  1102 ? 116.209 162.663 109.446 1.00 7.54   ? 1102 PHE B CD1   1 
ATOM   19326 C  CD2   . PHE B 2  1102 ? 117.176 160.806 110.539 1.00 5.97   ? 1102 PHE B CD2   1 
ATOM   19327 C  CE1   . PHE B 2  1102 ? 116.406 163.420 110.563 1.00 13.30  ? 1102 PHE B CE1   1 
ATOM   19328 C  CE2   . PHE B 2  1102 ? 117.368 161.558 111.656 1.00 1.70   ? 1102 PHE B CE2   1 
ATOM   19329 C  CZ    . PHE B 2  1102 ? 116.978 162.865 111.669 1.00 4.80   ? 1102 PHE B CZ    1 
ATOM   19330 N  N     . ILE B 2  1103 ? 119.010 162.368 106.653 1.00 14.60  ? 1103 ILE B N     1 
ATOM   19331 C  CA    . ILE B 2  1103 ? 120.451 162.547 106.559 1.00 7.62   ? 1103 ILE B CA    1 
ATOM   19332 C  C     . ILE B 2  1103 ? 120.833 163.842 107.267 1.00 11.91  ? 1103 ILE B C     1 
ATOM   19333 O  O     . ILE B 2  1103 ? 120.174 164.869 107.105 1.00 8.15   ? 1103 ILE B O     1 
ATOM   19334 C  CB    . ILE B 2  1103 ? 120.924 162.528 105.084 1.00 12.23  ? 1103 ILE B CB    1 
ATOM   19335 C  CG1   . ILE B 2  1103 ? 122.425 162.782 104.990 1.00 13.51  ? 1103 ILE B CG1   1 
ATOM   19336 C  CG2   . ILE B 2  1103 ? 120.142 163.500 104.244 1.00 2.27   ? 1103 ILE B CG2   1 
ATOM   19337 C  CD1   . ILE B 2  1103 ? 122.974 162.633 103.648 1.00 13.65  ? 1103 ILE B CD1   1 
ATOM   19338 N  N     . GLY B 2  1104 ? 121.880 163.786 108.074 1.00 8.49   ? 1104 GLY B N     1 
ATOM   19339 C  CA    . GLY B 2  1104 ? 122.328 164.934 108.822 1.00 9.84   ? 1104 GLY B CA    1 
ATOM   19340 C  C     . GLY B 2  1104 ? 123.519 164.613 109.691 1.00 5.59   ? 1104 GLY B C     1 
ATOM   19341 O  O     . GLY B 2  1104 ? 123.978 163.475 109.739 1.00 11.31  ? 1104 GLY B O     1 
ATOM   19342 N  N     . PRO B 2  1105 ? 124.037 165.609 110.412 1.00 4.44   ? 1105 PRO B N     1 
ATOM   19343 C  CA    . PRO B 2  1105 ? 125.296 165.443 111.156 1.00 4.33   ? 1105 PRO B CA    1 
ATOM   19344 C  C     . PRO B 2  1105 ? 125.092 164.798 112.522 1.00 3.25   ? 1105 PRO B C     1 
ATOM   19345 O  O     . PRO B 2  1105 ? 124.248 165.230 113.307 1.00 8.01   ? 1105 PRO B O     1 
ATOM   19346 C  CB    . PRO B 2  1105 ? 125.812 166.877 111.283 1.00 11.47  ? 1105 PRO B CB    1 
ATOM   19347 C  CG    . PRO B 2  1105 ? 124.594 167.704 111.247 1.00 14.43  ? 1105 PRO B CG    1 
ATOM   19348 C  CD    . PRO B 2  1105 ? 123.586 167.008 110.403 1.00 6.71   ? 1105 PRO B CD    1 
ATOM   19349 N  N     . THR B 2  1106 ? 125.880 163.768 112.809 1.00 11.31  ? 1106 THR B N     1 
ATOM   19350 C  CA    . THR B 2  1106 ? 125.862 163.072 114.087 1.00 1.31   ? 1106 THR B CA    1 
ATOM   19351 C  C     . THR B 2  1106 ? 127.295 162.845 114.537 1.00 6.57   ? 1106 THR B C     1 
ATOM   19352 O  O     . THR B 2  1106 ? 128.085 162.255 113.802 1.00 10.94  ? 1106 THR B O     1 
ATOM   19353 C  CB    . THR B 2  1106 ? 125.120 161.732 113.982 1.00 4.80   ? 1106 THR B CB    1 
ATOM   19354 O  OG1   . THR B 2  1106 ? 123.807 161.951 113.468 1.00 4.16   ? 1106 THR B OG1   1 
ATOM   19355 C  CG2   . THR B 2  1106 ? 125.006 161.055 115.322 1.00 3.67   ? 1106 THR B CG2   1 
ATOM   19356 N  N     . TYR B 2  1107 ? 127.621 163.295 115.740 1.00 6.70   ? 1107 TYR B N     1 
ATOM   19357 C  CA    . TYR B 2  1107 ? 128.980 163.202 116.260 1.00 2.22   ? 1107 TYR B CA    1 
ATOM   19358 C  C     . TYR B 2  1107 ? 129.372 161.749 116.508 1.00 15.71  ? 1107 TYR B C     1 
ATOM   19359 O  O     . TYR B 2  1107 ? 128.638 161.008 117.162 1.00 8.18   ? 1107 TYR B O     1 
ATOM   19360 C  CB    . TYR B 2  1107 ? 129.077 164.005 117.548 1.00 9.95   ? 1107 TYR B CB    1 
ATOM   19361 C  CG    . TYR B 2  1107 ? 130.453 164.420 117.964 1.00 5.12   ? 1107 TYR B CG    1 
ATOM   19362 C  CD1   . TYR B 2  1107 ? 131.053 165.516 117.409 1.00 3.43   ? 1107 TYR B CD1   1 
ATOM   19363 C  CD2   . TYR B 2  1107 ? 131.137 163.727 118.938 1.00 15.25  ? 1107 TYR B CD2   1 
ATOM   19364 C  CE1   . TYR B 2  1107 ? 132.290 165.908 117.790 1.00 4.73   ? 1107 TYR B CE1   1 
ATOM   19365 C  CE2   . TYR B 2  1107 ? 132.373 164.113 119.331 1.00 6.81   ? 1107 TYR B CE2   1 
ATOM   19366 C  CZ    . TYR B 2  1107 ? 132.945 165.207 118.754 1.00 0.66   ? 1107 TYR B CZ    1 
ATOM   19367 O  OH    . TYR B 2  1107 ? 134.187 165.612 119.140 1.00 11.21  ? 1107 TYR B OH    1 
ATOM   19368 N  N     . HIS B 2  1108 ? 130.546 161.351 116.019 1.00 1.92   ? 1108 HIS B N     1 
ATOM   19369 C  CA    . HIS B 2  1108 ? 130.999 159.973 116.100 1.00 0.54   ? 1108 HIS B CA    1 
ATOM   19370 C  C     . HIS B 2  1108 ? 132.427 159.911 116.622 1.00 11.41  ? 1108 HIS B C     1 
ATOM   19371 O  O     . HIS B 2  1108 ? 133.164 160.893 116.604 1.00 3.93   ? 1108 HIS B O     1 
ATOM   19372 C  CB    . HIS B 2  1108 ? 130.901 159.276 114.742 1.00 1.78   ? 1108 HIS B CB    1 
ATOM   19373 C  CG    . HIS B 2  1108 ? 129.604 158.566 114.522 1.00 2.65   ? 1108 HIS B CG    1 
ATOM   19374 N  ND1   . HIS B 2  1108 ? 129.492 157.198 114.567 1.00 2.12   ? 1108 HIS B ND1   1 
ATOM   19375 C  CD2   . HIS B 2  1108 ? 128.361 159.035 114.283 1.00 13.23  ? 1108 HIS B CD2   1 
ATOM   19376 C  CE1   . HIS B 2  1108 ? 128.237 156.854 114.359 1.00 10.93  ? 1108 HIS B CE1   1 
ATOM   19377 N  NE2   . HIS B 2  1108 ? 127.531 157.951 114.182 1.00 3.64   ? 1108 HIS B NE2   1 
ATOM   19378 N  N     . GLN B 2  1109 ? 132.800 158.732 117.104 1.00 0.48   ? 1109 GLN B N     1 
ATOM   19379 C  CA    . GLN B 2  1109 ? 134.074 158.485 117.759 1.00 3.60   ? 1109 GLN B CA    1 
ATOM   19380 C  C     . GLN B 2  1109 ? 134.696 157.222 117.187 1.00 2.41   ? 1109 GLN B C     1 
ATOM   19381 O  O     . GLN B 2  1109 ? 134.001 156.283 116.819 1.00 9.44   ? 1109 GLN B O     1 
ATOM   19382 C  CB    . GLN B 2  1109 ? 133.899 158.308 119.273 1.00 4.17   ? 1109 GLN B CB    1 
ATOM   19383 C  CG    . GLN B 2  1109 ? 133.590 159.559 120.059 1.00 6.57   ? 1109 GLN B CG    1 
ATOM   19384 C  CD    . GLN B 2  1109 ? 132.798 159.278 121.333 1.00 15.89  ? 1109 GLN B CD    1 
ATOM   19385 O  OE1   . GLN B 2  1109 ? 132.080 158.281 121.430 1.00 15.37  ? 1109 GLN B OE1   1 
ATOM   19386 N  NE2   . GLN B 2  1109 ? 132.933 160.160 122.319 1.00 16.97  ? 1109 GLN B NE2   1 
ATOM   19387 N  N     . ARG B 2  1110 ? 136.018 157.186 117.145 1.00 1.79   ? 1110 ARG B N     1 
ATOM   19388 C  CA    . ARG B 2  1110 ? 136.746 155.990 116.754 1.00 0.07   ? 1110 ARG B CA    1 
ATOM   19389 C  C     . ARG B 2  1110 ? 137.224 155.270 118.008 1.00 8.07   ? 1110 ARG B C     1 
ATOM   19390 O  O     . ARG B 2  1110 ? 138.004 155.822 118.782 1.00 13.07  ? 1110 ARG B O     1 
ATOM   19391 C  CB    . ARG B 2  1110 ? 137.928 156.337 115.857 1.00 0.37   ? 1110 ARG B CB    1 
ATOM   19392 C  CG    . ARG B 2  1110 ? 138.708 155.136 115.424 1.00 4.90   ? 1110 ARG B CG    1 
ATOM   19393 C  CD    . ARG B 2  1110 ? 139.974 155.506 114.706 1.00 6.61   ? 1110 ARG B CD    1 
ATOM   19394 N  NE    . ARG B 2  1110 ? 140.607 154.321 114.154 1.00 3.94   ? 1110 ARG B NE    1 
ATOM   19395 C  CZ    . ARG B 2  1110 ? 141.565 154.336 113.243 1.00 8.64   ? 1110 ARG B CZ    1 
ATOM   19396 N  NH1   . ARG B 2  1110 ? 142.036 155.464 112.755 1.00 4.40   ? 1110 ARG B NH1   1 
ATOM   19397 N  NH2   . ARG B 2  1110 ? 142.055 153.187 112.803 1.00 11.72  ? 1110 ARG B NH2   1 
ATOM   19398 N  N     . LEU B 2  1111 ? 136.764 154.039 118.200 1.00 13.06  ? 1111 LEU B N     1 
ATOM   19399 C  CA    . LEU B 2  1111 ? 137.158 153.251 119.359 1.00 12.89  ? 1111 LEU B CA    1 
ATOM   19400 C  C     . LEU B 2  1111 ? 138.512 152.599 119.124 1.00 14.93  ? 1111 LEU B C     1 
ATOM   19401 O  O     . LEU B 2  1111 ? 138.820 152.154 118.018 1.00 13.82  ? 1111 LEU B O     1 
ATOM   19402 C  CB    . LEU B 2  1111 ? 136.107 152.191 119.658 1.00 8.29   ? 1111 LEU B CB    1 
ATOM   19403 C  CG    . LEU B 2  1111 ? 134.700 152.751 119.855 1.00 10.01  ? 1111 LEU B CG    1 
ATOM   19404 C  CD1   . LEU B 2  1111 ? 133.748 151.668 120.246 1.00 7.05   ? 1111 LEU B CD1   1 
ATOM   19405 C  CD2   . LEU B 2  1111 ? 134.716 153.823 120.901 1.00 10.85  ? 1111 LEU B CD2   1 
ATOM   19406 N  N     . GLN B 2  1112 ? 139.329 152.552 120.175 1.00 20.63  ? 1112 GLN B N     1 
ATOM   19407 C  CA    . GLN B 2  1112 ? 140.702 152.062 120.064 1.00 20.40  ? 1112 GLN B CA    1 
ATOM   19408 C  C     . GLN B 2  1112 ? 140.748 150.534 120.115 1.00 20.81  ? 1112 GLN B C     1 
ATOM   19409 O  O     . GLN B 2  1112 ? 141.275 149.918 121.036 1.00 25.98  ? 1112 GLN B O     1 
ATOM   19410 C  CB    . GLN B 2  1112 ? 141.571 152.684 121.144 1.00 20.36  ? 1112 GLN B CB    1 
ATOM   19411 C  CG    . GLN B 2  1112 ? 142.238 153.985 120.733 1.00 19.06  ? 1112 GLN B CG    1 
ATOM   19412 C  CD    . GLN B 2  1112 ? 142.325 154.967 121.864 1.00 21.18  ? 1112 GLN B CD    1 
ATOM   19413 O  OE1   . GLN B 2  1112 ? 142.368 156.169 121.654 1.00 24.39  ? 1112 GLN B OE1   1 
ATOM   19414 N  NE2   . GLN B 2  1112 ? 142.323 154.459 123.080 1.00 25.47  ? 1112 GLN B NE2   1 
ATOM   19415 N  N     . LYS B 2  1113 ? 140.184 149.931 119.076 1.00 21.21  ? 1113 LYS B N     1 
ATOM   19416 C  CA    . LYS B 2  1113 ? 140.160 148.490 118.852 1.00 19.45  ? 1113 LYS B CA    1 
ATOM   19417 C  C     . LYS B 2  1113 ? 140.508 148.284 117.381 1.00 19.56  ? 1113 LYS B C     1 
ATOM   19418 O  O     . LYS B 2  1113 ? 139.630 148.306 116.517 1.00 18.47  ? 1113 LYS B O     1 
ATOM   19419 C  CB    . LYS B 2  1113 ? 138.793 147.902 119.208 1.00 18.99  ? 1113 LYS B CB    1 
ATOM   19420 C  CG    . LYS B 2  1113 ? 138.818 146.441 119.567 1.00 22.02  ? 1113 LYS B CG    1 
ATOM   19421 C  CD    . LYS B 2  1113 ? 139.313 146.249 120.981 1.00 26.70  ? 1113 LYS B CD    1 
ATOM   19422 C  CE    . LYS B 2  1113 ? 139.990 144.905 121.156 1.00 25.21  ? 1113 LYS B CE    1 
ATOM   19423 N  NZ    . LYS B 2  1113 ? 141.285 145.043 121.867 1.00 27.82  ? 1113 LYS B NZ    1 
ATOM   19424 N  N     . PHE B 2  1114 ? 141.792 148.104 117.096 1.00 20.38  ? 1114 PHE B N     1 
ATOM   19425 C  CA    . PHE B 2  1114 ? 142.276 148.117 115.723 1.00 17.01  ? 1114 PHE B CA    1 
ATOM   19426 C  C     . PHE B 2  1114 ? 142.389 146.707 115.163 1.00 18.52  ? 1114 PHE B C     1 
ATOM   19427 O  O     . PHE B 2  1114 ? 142.922 145.806 115.811 1.00 18.20  ? 1114 PHE B O     1 
ATOM   19428 C  CB    . PHE B 2  1114 ? 143.630 148.820 115.647 1.00 18.15  ? 1114 PHE B CB    1 
ATOM   19429 C  CG    . PHE B 2  1114 ? 143.622 150.210 116.207 1.00 17.56  ? 1114 PHE B CG    1 
ATOM   19430 C  CD1   . PHE B 2  1114 ? 143.920 150.436 117.536 1.00 16.58  ? 1114 PHE B CD1   1 
ATOM   19431 C  CD2   . PHE B 2  1114 ? 143.314 151.293 115.407 1.00 14.13  ? 1114 PHE B CD2   1 
ATOM   19432 C  CE1   . PHE B 2  1114 ? 143.912 151.712 118.054 1.00 15.95  ? 1114 PHE B CE1   1 
ATOM   19433 C  CE2   . PHE B 2  1114 ? 143.311 152.569 115.923 1.00 13.69  ? 1114 PHE B CE2   1 
ATOM   19434 C  CZ    . PHE B 2  1114 ? 143.608 152.776 117.246 1.00 17.23  ? 1114 PHE B CZ    1 
ATOM   19435 N  N     . VAL B 2  1115 ? 141.904 146.531 113.935 1.00 18.63  ? 1115 VAL B N     1 
ATOM   19436 C  CA    . VAL B 2  1115 ? 141.845 145.206 113.328 1.00 14.22  ? 1115 VAL B CA    1 
ATOM   19437 C  C     . VAL B 2  1115 ? 143.246 144.670 113.044 1.00 18.22  ? 1115 VAL B C     1 
ATOM   19438 O  O     . VAL B 2  1115 ? 143.472 143.458 113.069 1.00 19.57  ? 1115 VAL B O     1 
ATOM   19439 C  CB    . VAL B 2  1115 ? 140.967 145.253 112.064 1.00 10.53  ? 1115 VAL B CB    1 
ATOM   19440 C  CG1   . VAL B 2  1115 ? 141.499 146.272 111.087 1.00 15.38  ? 1115 VAL B CG1   1 
ATOM   19441 C  CG2   . VAL B 2  1115 ? 140.840 143.883 111.425 1.00 10.61  ? 1115 VAL B CG2   1 
ATOM   19442 N  N     . LEU B 2  1116 ? 144.208 145.555 112.772 1.00 20.66  ? 1116 LEU B N     1 
ATOM   19443 C  CA    . LEU B 2  1116 ? 145.578 145.113 112.523 1.00 18.69  ? 1116 LEU B CA    1 
ATOM   19444 C  C     . LEU B 2  1116 ? 146.216 144.499 113.762 1.00 22.54  ? 1116 LEU B C     1 
ATOM   19445 O  O     . LEU B 2  1116 ? 147.073 143.617 113.647 1.00 19.66  ? 1116 LEU B O     1 
ATOM   19446 C  CB    . LEU B 2  1116 ? 146.424 146.280 112.017 1.00 16.70  ? 1116 LEU B CB    1 
ATOM   19447 C  CG    . LEU B 2  1116 ? 146.024 146.861 110.661 1.00 19.75  ? 1116 LEU B CG    1 
ATOM   19448 C  CD1   . LEU B 2  1116 ? 146.811 148.106 110.329 1.00 18.04  ? 1116 LEU B CD1   1 
ATOM   19449 C  CD2   . LEU B 2  1116 ? 146.239 145.819 109.595 1.00 16.42  ? 1116 LEU B CD2   1 
ATOM   19450 N  N     . ASP B 2  1117 ? 145.823 144.955 114.950 1.00 24.08  ? 1117 ASP B N     1 
ATOM   19451 C  CA    . ASP B 2  1117 ? 146.377 144.414 116.182 1.00 14.83  ? 1117 ASP B CA    1 
ATOM   19452 C  C     . ASP B 2  1117 ? 145.795 143.059 116.550 1.00 19.49  ? 1117 ASP B C     1 
ATOM   19453 O  O     . ASP B 2  1117 ? 146.531 142.196 117.029 1.00 29.14  ? 1117 ASP B O     1 
ATOM   19454 C  CB    . ASP B 2  1117 ? 146.147 145.388 117.333 1.00 21.03  ? 1117 ASP B CB    1 
ATOM   19455 C  CG    . ASP B 2  1117 ? 146.860 146.699 117.138 1.00 24.37  ? 1117 ASP B CG    1 
ATOM   19456 O  OD1   . ASP B 2  1117 ? 147.697 146.795 116.224 1.00 22.21  ? 1117 ASP B OD1   1 
ATOM   19457 O  OD2   . ASP B 2  1117 ? 146.588 147.636 117.910 1.00 28.62  ? 1117 ASP B OD2   1 
ATOM   19458 N  N     . ASP B 2  1118 ? 144.492 142.853 116.365 1.00 21.73  ? 1118 ASP B N     1 
ATOM   19459 C  CA    . ASP B 2  1118 ? 143.843 141.618 116.793 1.00 24.81  ? 1118 ASP B CA    1 
ATOM   19460 C  C     . ASP B 2  1118 ? 144.066 140.459 115.833 1.00 25.60  ? 1118 ASP B C     1 
ATOM   19461 O  O     . ASP B 2  1118 ? 143.976 139.294 116.234 1.00 28.22  ? 1118 ASP B O     1 
ATOM   19462 C  CB    . ASP B 2  1118 ? 142.335 141.837 116.954 1.00 25.08  ? 1118 ASP B CB    1 
ATOM   19463 C  CG    . ASP B 2  1118 ? 141.998 143.024 117.838 1.00 31.73  ? 1118 ASP B CG    1 
ATOM   19464 O  OD1   . ASP B 2  1118 ? 142.228 142.947 119.062 1.00 32.17  ? 1118 ASP B OD1   1 
ATOM   19465 O  OD2   . ASP B 2  1118 ? 141.470 144.024 117.319 1.00 31.13  ? 1118 ASP B OD2   1 
ATOM   19466 N  N     . ARG B 2  1119 ? 144.354 140.771 114.583 1.00 16.03  ? 1119 ARG B N     1 
ATOM   19467 C  CA    . ARG B 2  1119 ? 144.427 139.797 113.511 1.00 9.33   ? 1119 ARG B CA    1 
ATOM   19468 C  C     . ARG B 2  1119 ? 145.634 138.873 113.681 1.00 14.77  ? 1119 ARG B C     1 
ATOM   19469 O  O     . ARG B 2  1119 ? 146.704 139.316 114.099 1.00 30.76  ? 1119 ARG B O     1 
ATOM   19470 C  CB    . ARG B 2  1119 ? 144.502 140.590 112.216 1.00 9.53   ? 1119 ARG B CB    1 
ATOM   19471 C  CG    . ARG B 2  1119 ? 144.802 139.846 111.011 1.00 15.87  ? 1119 ARG B CG    1 
ATOM   19472 C  CD    . ARG B 2  1119 ? 145.146 140.791 109.899 1.00 17.45  ? 1119 ARG B CD    1 
ATOM   19473 N  NE    . ARG B 2  1119 ? 146.331 141.578 110.214 1.00 18.28  ? 1119 ARG B NE    1 
ATOM   19474 C  CZ    . ARG B 2  1119 ? 146.963 142.349 109.341 1.00 23.09  ? 1119 ARG B CZ    1 
ATOM   19475 N  NH1   . ARG B 2  1119 ? 146.547 142.458 108.093 1.00 19.52  ? 1119 ARG B NH1   1 
ATOM   19476 N  NH2   . ARG B 2  1119 ? 148.049 143.010 109.724 1.00 26.08  ? 1119 ARG B NH2   1 
ATOM   19477 N  N     . TYR B 2  1120 ? 145.476 137.589 113.358 1.00 2.10   ? 1120 TYR B N     1 
ATOM   19478 C  CA    . TYR B 2  1120 ? 146.581 136.654 113.519 1.00 2.61   ? 1120 TYR B CA    1 
ATOM   19479 C  C     . TYR B 2  1120 ? 146.451 135.483 112.553 1.00 3.65   ? 1120 TYR B C     1 
ATOM   19480 O  O     . TYR B 2  1120 ? 145.349 135.029 112.257 1.00 13.47  ? 1120 TYR B O     1 
ATOM   19481 C  CB    . TYR B 2  1120 ? 146.654 136.119 114.953 1.00 5.58   ? 1120 TYR B CB    1 
ATOM   19482 C  CG    . TYR B 2  1120 ? 147.882 135.286 115.219 1.00 11.87  ? 1120 TYR B CG    1 
ATOM   19483 C  CD1   . TYR B 2  1120 ? 149.145 135.836 115.098 1.00 13.60  ? 1120 TYR B CD1   1 
ATOM   19484 C  CD2   . TYR B 2  1120 ? 147.786 133.947 115.554 1.00 13.63  ? 1120 TYR B CD2   1 
ATOM   19485 C  CE1   . TYR B 2  1120 ? 150.272 135.089 115.324 1.00 14.87  ? 1120 TYR B CE1   1 
ATOM   19486 C  CE2   . TYR B 2  1120 ? 148.911 133.189 115.780 1.00 9.12   ? 1120 TYR B CE2   1 
ATOM   19487 C  CZ    . TYR B 2  1120 ? 150.151 133.770 115.664 1.00 11.99  ? 1120 TYR B CZ    1 
ATOM   19488 O  OH    . TYR B 2  1120 ? 151.285 133.040 115.887 1.00 15.22  ? 1120 TYR B OH    1 
ATOM   19489 N  N     . ALA B 2  1121 ? 147.590 134.986 112.078 1.00 1.45   ? 1121 ALA B N     1 
ATOM   19490 C  CA    . ALA B 2  1121 ? 147.634 133.793 111.246 1.00 0.75   ? 1121 ALA B CA    1 
ATOM   19491 C  C     . ALA B 2  1121 ? 148.998 133.138 111.370 1.00 2.14   ? 1121 ALA B C     1 
ATOM   19492 O  O     . ALA B 2  1121 ? 150.020 133.814 111.309 1.00 13.54  ? 1121 ALA B O     1 
ATOM   19493 C  CB    . ALA B 2  1121 ? 147.353 134.114 109.780 1.00 14.64  ? 1121 ALA B CB    1 
ATOM   19494 N  N     . VAL B 2  1122 ? 149.012 131.820 111.519 1.00 10.23  ? 1122 VAL B N     1 
ATOM   19495 C  CA    . VAL B 2  1122 ? 150.248 131.066 111.655 1.00 2.51   ? 1122 VAL B CA    1 
ATOM   19496 C  C     . VAL B 2  1122 ? 150.204 129.859 110.719 1.00 6.38   ? 1122 VAL B C     1 
ATOM   19497 O  O     . VAL B 2  1122 ? 149.153 129.459 110.232 1.00 11.31  ? 1122 VAL B O     1 
ATOM   19498 C  CB    . VAL B 2  1122 ? 150.513 130.650 113.117 1.00 0.60   ? 1122 VAL B CB    1 
ATOM   19499 C  CG1   . VAL B 2  1122 ? 149.697 129.434 113.512 1.00 2.35   ? 1122 VAL B CG1   1 
ATOM   19500 C  CG2   . VAL B 2  1122 ? 151.987 130.423 113.352 1.00 1.46   ? 1122 VAL B CG2   1 
ATOM   19501 N  N     . ALA B 2  1123 ? 151.373 129.294 110.461 1.00 8.81   ? 1123 ALA B N     1 
ATOM   19502 C  CA    . ALA B 2  1123 ? 151.536 128.130 109.605 1.00 7.46   ? 1123 ALA B CA    1 
ATOM   19503 C  C     . ALA B 2  1123 ? 152.087 126.967 110.427 1.00 11.04  ? 1123 ALA B C     1 
ATOM   19504 O  O     . ALA B 2  1123 ? 152.084 126.987 111.653 1.00 19.26  ? 1123 ALA B O     1 
ATOM   19505 C  CB    . ALA B 2  1123 ? 152.429 128.453 108.410 1.00 8.07   ? 1123 ALA B CB    1 
ATOM   19506 N  N     . SER B 2  1124 ? 152.557 125.940 109.729 1.00 13.92  ? 1124 SER B N     1 
ATOM   19507 C  CA    . SER B 2  1124 ? 152.781 124.627 110.314 1.00 16.28  ? 1124 SER B CA    1 
ATOM   19508 C  C     . SER B 2  1124 ? 154.021 124.514 111.192 1.00 13.09  ? 1124 SER B C     1 
ATOM   19509 O  O     . SER B 2  1124 ? 154.375 123.394 111.560 1.00 21.66  ? 1124 SER B O     1 
ATOM   19510 C  CB    . SER B 2  1124 ? 152.853 123.596 109.193 1.00 21.24  ? 1124 SER B CB    1 
ATOM   19511 O  OG    . SER B 2  1124 ? 153.833 123.956 108.252 1.00 24.94  ? 1124 SER B OG    1 
ATOM   19512 N  N     . TYR B 2  1125 ? 154.686 125.605 111.551 1.00 19.06  ? 1125 TYR B N     1 
ATOM   19513 C  CA    . TYR B 2  1125 ? 155.888 125.488 112.365 1.00 26.38  ? 1125 TYR B CA    1 
ATOM   19514 C  C     . TYR B 2  1125 ? 156.124 126.768 113.151 1.00 29.55  ? 1125 TYR B C     1 
ATOM   19515 O  O     . TYR B 2  1125 ? 155.619 127.837 112.810 1.00 30.63  ? 1125 TYR B O     1 
ATOM   19516 C  CB    . TYR B 2  1125 ? 157.126 125.161 111.514 1.00 30.30  ? 1125 TYR B CB    1 
ATOM   19517 C  CG    . TYR B 2  1125 ? 157.357 126.119 110.376 1.00 30.58  ? 1125 TYR B CG    1 
ATOM   19518 C  CD1   . TYR B 2  1125 ? 158.349 127.081 110.451 1.00 29.69  ? 1125 TYR B CD1   1 
ATOM   19519 C  CD2   . TYR B 2  1125 ? 156.590 126.057 109.219 1.00 28.84  ? 1125 TYR B CD2   1 
ATOM   19520 C  CE1   . TYR B 2  1125 ? 158.561 127.964 109.416 1.00 32.74  ? 1125 TYR B CE1   1 
ATOM   19521 C  CE2   . TYR B 2  1125 ? 156.793 126.935 108.181 1.00 31.07  ? 1125 TYR B CE2   1 
ATOM   19522 C  CZ    . TYR B 2  1125 ? 157.781 127.884 108.282 1.00 34.87  ? 1125 TYR B CZ    1 
ATOM   19523 O  OH    . TYR B 2  1125 ? 157.990 128.759 107.245 1.00 36.20  ? 1125 TYR B OH    1 
ATOM   19524 N  N     . GLY B 2  1126 ? 156.910 126.640 114.218 1.00 22.30  ? 1126 GLY B N     1 
ATOM   19525 C  CA    . GLY B 2  1126 ? 157.195 127.738 115.108 1.00 20.25  ? 1126 GLY B CA    1 
ATOM   19526 C  C     . GLY B 2  1126 ? 157.679 127.265 116.463 1.00 21.63  ? 1126 GLY B C     1 
ATOM   19527 O  O     . GLY B 2  1126 ? 157.995 126.091 116.656 1.00 24.39  ? 1126 GLY B O     1 
ATOM   19528 N  N     . PRO B 2  1127 ? 157.742 128.178 117.431 1.00 22.14  ? 1127 PRO B N     1 
ATOM   19529 C  CA    . PRO B 2  1127 ? 158.185 127.805 118.778 1.00 21.66  ? 1127 PRO B CA    1 
ATOM   19530 C  C     . PRO B 2  1127 ? 157.264 126.789 119.439 1.00 22.19  ? 1127 PRO B C     1 
ATOM   19531 O  O     . PRO B 2  1127 ? 156.052 126.782 119.231 1.00 27.71  ? 1127 PRO B O     1 
ATOM   19532 C  CB    . PRO B 2  1127 ? 158.166 129.136 119.532 1.00 20.34  ? 1127 PRO B CB    1 
ATOM   19533 C  CG    . PRO B 2  1127 ? 158.248 130.158 118.496 1.00 19.18  ? 1127 PRO B CG    1 
ATOM   19534 C  CD    . PRO B 2  1127 ? 157.541 129.627 117.308 1.00 22.38  ? 1127 PRO B CD    1 
ATOM   19535 N  N     . THR B 2  1128 ? 157.857 125.946 120.277 1.00 21.25  ? 1128 THR B N     1 
ATOM   19536 C  CA    . THR B 2  1128 ? 157.183 124.803 120.872 1.00 24.27  ? 1128 THR B CA    1 
ATOM   19537 C  C     . THR B 2  1128 ? 157.478 124.755 122.365 1.00 19.01  ? 1128 THR B C     1 
ATOM   19538 O  O     . THR B 2  1128 ? 158.562 125.147 122.798 1.00 25.47  ? 1128 THR B O     1 
ATOM   19539 C  CB    . THR B 2  1128 ? 157.635 123.511 120.179 1.00 21.28  ? 1128 THR B CB    1 
ATOM   19540 O  OG1   . THR B 2  1128 ? 157.039 123.441 118.883 1.00 21.30  ? 1128 THR B OG1   1 
ATOM   19541 C  CG2   . THR B 2  1128 ? 157.221 122.302 120.946 1.00 18.42  ? 1128 THR B CG2   1 
ATOM   19542 N  N     . ASP B 2  1129 ? 156.500 124.305 123.147 1.00 15.10  ? 1129 ASP B N     1 
ATOM   19543 C  CA    . ASP B 2  1129 ? 156.691 124.100 124.577 1.00 17.77  ? 1129 ASP B CA    1 
ATOM   19544 C  C     . ASP B 2  1129 ? 157.739 123.025 124.843 1.00 20.95  ? 1129 ASP B C     1 
ATOM   19545 O  O     . ASP B 2  1129 ? 157.849 122.042 124.107 1.00 22.39  ? 1129 ASP B O     1 
ATOM   19546 C  CB    . ASP B 2  1129 ? 155.370 123.705 125.229 1.00 19.80  ? 1129 ASP B CB    1 
ATOM   19547 C  CG    . ASP B 2  1129 ? 155.407 123.805 126.734 1.00 25.92  ? 1129 ASP B CG    1 
ATOM   19548 O  OD1   . ASP B 2  1129 ? 155.376 124.931 127.264 1.00 32.06  ? 1129 ASP B OD1   1 
ATOM   19549 O  OD2   . ASP B 2  1129 ? 155.458 122.756 127.397 1.00 26.69  ? 1129 ASP B OD2   1 
ATOM   19550 N  N     . ALA B 2  1130 ? 158.513 123.216 125.910 1.00 22.08  ? 1130 ALA B N     1 
ATOM   19551 C  CA    . ALA B 2  1130 ? 159.609 122.298 126.204 1.00 22.33  ? 1130 ALA B CA    1 
ATOM   19552 C  C     . ALA B 2  1130 ? 159.108 120.985 126.792 1.00 19.36  ? 1130 ALA B C     1 
ATOM   19553 O  O     . ALA B 2  1130 ? 159.749 119.943 126.627 1.00 16.74  ? 1130 ALA B O     1 
ATOM   19554 C  CB    . ALA B 2  1130 ? 160.601 122.961 127.156 1.00 21.13  ? 1130 ALA B CB    1 
ATOM   19555 N  N     . LEU B 2  1131 ? 157.972 121.015 127.489 1.00 19.23  ? 1131 LEU B N     1 
ATOM   19556 C  CA    . LEU B 2  1131 ? 157.476 119.831 128.181 1.00 17.55  ? 1131 LEU B CA    1 
ATOM   19557 C  C     . LEU B 2  1131 ? 156.461 119.060 127.339 1.00 21.63  ? 1131 LEU B C     1 
ATOM   19558 O  O     . LEU B 2  1131 ? 156.650 117.874 127.055 1.00 23.28  ? 1131 LEU B O     1 
ATOM   19559 C  CB    . LEU B 2  1131 ? 156.871 120.245 129.524 1.00 17.94  ? 1131 LEU B CB    1 
ATOM   19560 C  CG    . LEU B 2  1131 ? 156.275 119.196 130.466 1.00 17.86  ? 1131 LEU B CG    1 
ATOM   19561 C  CD1   . LEU B 2  1131 ? 157.202 118.039 130.670 1.00 18.73  ? 1131 LEU B CD1   1 
ATOM   19562 C  CD2   . LEU B 2  1131 ? 155.947 119.830 131.787 1.00 19.77  ? 1131 LEU B CD2   1 
ATOM   19563 N  N     . THR B 2  1132 ? 155.375 119.721 126.930 1.00 21.07  ? 1132 THR B N     1 
ATOM   19564 C  CA    . THR B 2  1132 ? 154.265 119.032 126.277 1.00 15.27  ? 1132 THR B CA    1 
ATOM   19565 C  C     . THR B 2  1132 ? 154.492 118.813 124.788 1.00 14.67  ? 1132 THR B C     1 
ATOM   19566 O  O     . THR B 2  1132 ? 153.841 117.951 124.194 1.00 13.45  ? 1132 THR B O     1 
ATOM   19567 C  CB    . THR B 2  1132 ? 152.968 119.810 126.487 1.00 15.64  ? 1132 THR B CB    1 
ATOM   19568 O  OG1   . THR B 2  1132 ? 153.048 121.058 125.798 1.00 21.39  ? 1132 THR B OG1   1 
ATOM   19569 C  CG2   . THR B 2  1132 ? 152.749 120.088 127.955 1.00 14.65  ? 1132 THR B CG2   1 
ATOM   19570 N  N     . GLY B 2  1133 ? 155.392 119.570 124.169 1.00 16.27  ? 1133 GLY B N     1 
ATOM   19571 C  CA    . GLY B 2  1133 ? 155.625 119.465 122.747 1.00 14.87  ? 1133 GLY B CA    1 
ATOM   19572 C  C     . GLY B 2  1133 ? 154.659 120.234 121.878 1.00 16.67  ? 1133 GLY B C     1 
ATOM   19573 O  O     . GLY B 2  1133 ? 154.770 120.166 120.650 1.00 20.06  ? 1133 GLY B O     1 
ATOM   19574 N  N     . GLN B 2  1134 ? 153.726 120.960 122.467 1.00 14.88  ? 1134 GLN B N     1 
ATOM   19575 C  CA    . GLN B 2  1134 ? 152.724 121.699 121.730 1.00 6.85   ? 1134 GLN B CA    1 
ATOM   19576 C  C     . GLN B 2  1134 ? 153.228 123.098 121.401 1.00 15.01  ? 1134 GLN B C     1 
ATOM   19577 O  O     . GLN B 2  1134 ? 154.222 123.552 121.966 1.00 24.26  ? 1134 GLN B O     1 
ATOM   19578 C  CB    . GLN B 2  1134 ? 151.443 121.768 122.546 1.00 9.21   ? 1134 GLN B CB    1 
ATOM   19579 C  CG    . GLN B 2  1134 ? 150.773 120.433 122.704 1.00 9.71   ? 1134 GLN B CG    1 
ATOM   19580 C  CD    . GLN B 2  1134 ? 149.526 120.509 123.533 1.00 11.29  ? 1134 GLN B CD    1 
ATOM   19581 O  OE1   . GLN B 2  1134 ? 149.070 121.588 123.888 1.00 20.50  ? 1134 GLN B OE1   1 
ATOM   19582 N  NE2   . GLN B 2  1134 ? 148.971 119.364 123.859 1.00 13.29  ? 1134 GLN B NE2   1 
ATOM   19583 N  N     . PRO B 2  1135 ? 152.578 123.796 120.466 1.00 18.33  ? 1135 PRO B N     1 
ATOM   19584 C  CA    . PRO B 2  1135 ? 152.936 125.196 120.223 1.00 15.23  ? 1135 PRO B CA    1 
ATOM   19585 C  C     . PRO B 2  1135 ? 152.892 126.049 121.480 1.00 15.97  ? 1135 PRO B C     1 
ATOM   19586 O  O     . PRO B 2  1135 ? 152.353 125.632 122.507 1.00 16.97  ? 1135 PRO B O     1 
ATOM   19587 C  CB    . PRO B 2  1135 ? 151.883 125.648 119.207 1.00 11.17  ? 1135 PRO B CB    1 
ATOM   19588 C  CG    . PRO B 2  1135 ? 151.476 124.433 118.520 1.00 2.48   ? 1135 PRO B CG    1 
ATOM   19589 C  CD    . PRO B 2  1135 ? 151.625 123.293 119.461 1.00 9.51   ? 1135 PRO B CD    1 
ATOM   19590 N  N     . LEU B 2  1136 ? 153.465 127.244 121.419 1.00 20.55  ? 1136 LEU B N     1 
ATOM   19591 C  CA    . LEU B 2  1136 ? 153.337 128.183 122.518 1.00 25.04  ? 1136 LEU B CA    1 
ATOM   19592 C  C     . LEU B 2  1136 ? 151.962 128.848 122.464 1.00 27.00  ? 1136 LEU B C     1 
ATOM   19593 O  O     . LEU B 2  1136 ? 151.137 128.556 121.602 1.00 26.93  ? 1136 LEU B O     1 
ATOM   19594 C  CB    . LEU B 2  1136 ? 154.477 129.193 122.469 1.00 22.37  ? 1136 LEU B CB    1 
ATOM   19595 C  CG    . LEU B 2  1136 ? 155.850 128.576 122.731 1.00 26.10  ? 1136 LEU B CG    1 
ATOM   19596 C  CD1   . LEU B 2  1136 ? 156.910 129.642 122.880 1.00 24.72  ? 1136 LEU B CD1   1 
ATOM   19597 C  CD2   . LEU B 2  1136 ? 155.809 127.701 123.974 1.00 24.05  ? 1136 LEU B CD2   1 
ATOM   19598 N  N     . ASP B 2  1137 ? 151.705 129.758 123.397 1.00 37.60  ? 1137 ASP B N     1 
ATOM   19599 C  CA    . ASP B 2  1137 ? 150.363 130.304 123.603 1.00 36.26  ? 1137 ASP B CA    1 
ATOM   19600 C  C     . ASP B 2  1137 ? 150.202 131.630 122.864 1.00 38.42  ? 1137 ASP B C     1 
ATOM   19601 O  O     . ASP B 2  1137 ? 150.497 132.699 123.397 1.00 39.34  ? 1137 ASP B O     1 
ATOM   19602 C  CB    . ASP B 2  1137 ? 150.077 130.488 125.087 1.00 36.41  ? 1137 ASP B CB    1 
ATOM   19603 C  CG    . ASP B 2  1137 ? 149.694 129.201 125.775 1.00 42.41  ? 1137 ASP B CG    1 
ATOM   19604 O  OD1   . ASP B 2  1137 ? 149.595 128.160 125.098 1.00 42.05  ? 1137 ASP B OD1   1 
ATOM   19605 O  OD2   . ASP B 2  1137 ? 149.484 129.232 127.005 1.00 42.41  ? 1137 ASP B OD2   1 
ATOM   19606 N  N     . GLY B 2  1138 ? 149.706 131.555 121.634 1.00 30.02  ? 1138 GLY B N     1 
ATOM   19607 C  CA    . GLY B 2  1138 ? 149.094 132.698 120.991 1.00 26.25  ? 1138 GLY B CA    1 
ATOM   19608 C  C     . GLY B 2  1138 ? 150.036 133.634 120.260 1.00 31.12  ? 1138 GLY B C     1 
ATOM   19609 O  O     . GLY B 2  1138 ? 151.214 133.364 120.025 1.00 32.30  ? 1138 GLY B O     1 
ATOM   19610 N  N     . LYS B 2  1139 ? 149.466 134.789 119.903 1.00 31.49  ? 1139 LYS B N     1 
ATOM   19611 C  CA    . LYS B 2  1139 ? 150.138 135.763 119.049 1.00 27.29  ? 1139 LYS B CA    1 
ATOM   19612 C  C     . LYS B 2  1139 ? 151.334 136.401 119.741 1.00 28.08  ? 1139 LYS B C     1 
ATOM   19613 O  O     . LYS B 2  1139 ? 152.335 136.718 119.090 1.00 27.80  ? 1139 LYS B O     1 
ATOM   19614 C  CB    . LYS B 2  1139 ? 149.136 136.835 118.618 1.00 29.73  ? 1139 LYS B CB    1 
ATOM   19615 C  CG    . LYS B 2  1139 ? 149.718 137.953 117.773 1.00 28.36  ? 1139 LYS B CG    1 
ATOM   19616 C  CD    . LYS B 2  1139 ? 148.626 138.837 117.201 1.00 27.85  ? 1139 LYS B CD    1 
ATOM   19617 C  CE    . LYS B 2  1139 ? 149.200 139.845 116.227 1.00 29.77  ? 1139 LYS B CE    1 
ATOM   19618 N  NZ    . LYS B 2  1139 ? 148.150 140.679 115.596 1.00 30.48  ? 1139 LYS B NZ    1 
ATOM   19619 N  N     . ARG B 2  1140 ? 151.244 136.603 121.057 1.00 42.35  ? 1140 ARG B N     1 
ATOM   19620 C  CA    . ARG B 2  1140 ? 152.306 137.293 121.785 1.00 45.09  ? 1140 ARG B CA    1 
ATOM   19621 C  C     . ARG B 2  1140 ? 153.622 136.524 121.727 1.00 44.97  ? 1140 ARG B C     1 
ATOM   19622 O  O     . ARG B 2  1140 ? 154.693 137.127 121.604 1.00 44.84  ? 1140 ARG B O     1 
ATOM   19623 C  CB    . ARG B 2  1140 ? 151.868 137.524 123.230 1.00 45.14  ? 1140 ARG B CB    1 
ATOM   19624 C  CG    . ARG B 2  1140 ? 152.980 137.452 124.254 1.00 46.86  ? 1140 ARG B CG    1 
ATOM   19625 C  CD    . ARG B 2  1140 ? 152.427 137.172 125.640 1.00 46.73  ? 1140 ARG B CD    1 
ATOM   19626 N  NE    . ARG B 2  1140 ? 152.189 135.753 125.873 1.00 48.72  ? 1140 ARG B NE    1 
ATOM   19627 C  CZ    . ARG B 2  1140 ? 151.027 135.245 126.259 1.00 48.80  ? 1140 ARG B CZ    1 
ATOM   19628 N  NH1   . ARG B 2  1140 ? 149.969 136.015 126.464 1.00 45.23  ? 1140 ARG B NH1   1 
ATOM   19629 N  NH2   . ARG B 2  1140 ? 150.923 133.933 126.447 1.00 47.79  ? 1140 ARG B NH2   1 
ATOM   19630 N  N     . SER B 2  1141 ? 153.563 135.196 121.804 1.00 33.37  ? 1141 SER B N     1 
ATOM   19631 C  CA    . SER B 2  1141 ? 154.750 134.354 121.782 1.00 31.54  ? 1141 SER B CA    1 
ATOM   19632 C  C     . SER B 2  1141 ? 155.005 133.706 120.427 1.00 29.44  ? 1141 SER B C     1 
ATOM   19633 O  O     . SER B 2  1141 ? 155.845 132.807 120.337 1.00 33.34  ? 1141 SER B O     1 
ATOM   19634 C  CB    . SER B 2  1141 ? 154.643 133.277 122.857 1.00 33.19  ? 1141 SER B CB    1 
ATOM   19635 O  OG    . SER B 2  1141 ? 153.293 132.931 123.080 1.00 36.96  ? 1141 SER B OG    1 
ATOM   19636 N  N     . HIS B 2  1142 ? 154.299 134.135 119.380 1.00 25.13  ? 1142 HIS B N     1 
ATOM   19637 C  CA    . HIS B 2  1142 ? 154.453 133.630 118.015 1.00 23.19  ? 1142 HIS B CA    1 
ATOM   19638 C  C     . HIS B 2  1142 ? 154.092 132.154 117.893 1.00 22.37  ? 1142 HIS B C     1 
ATOM   19639 O  O     . HIS B 2  1142 ? 154.601 131.460 117.009 1.00 21.08  ? 1142 HIS B O     1 
ATOM   19640 C  CB    . HIS B 2  1142 ? 155.871 133.870 117.479 1.00 21.06  ? 1142 HIS B CB    1 
ATOM   19641 C  CG    . HIS B 2  1142 ? 156.345 135.287 117.604 1.00 28.87  ? 1142 HIS B CG    1 
ATOM   19642 N  ND1   . HIS B 2  1142 ? 157.048 135.923 116.605 1.00 31.03  ? 1142 HIS B ND1   1 
ATOM   19643 C  CD2   . HIS B 2  1142 ? 156.238 136.183 118.615 1.00 28.30  ? 1142 HIS B CD2   1 
ATOM   19644 C  CE1   . HIS B 2  1142 ? 157.340 137.154 116.988 1.00 29.77  ? 1142 HIS B CE1   1 
ATOM   19645 N  NE2   . HIS B 2  1142 ? 156.860 137.337 118.204 1.00 29.22  ? 1142 HIS B NE2   1 
ATOM   19646 N  N     . GLY B 2  1143 ? 153.210 131.667 118.760 1.00 23.44  ? 1143 GLY B N     1 
ATOM   19647 C  CA    . GLY B 2  1143 ? 152.794 130.281 118.765 1.00 19.53  ? 1143 GLY B CA    1 
ATOM   19648 C  C     . GLY B 2  1143 ? 151.511 130.064 117.999 1.00 16.81  ? 1143 GLY B C     1 
ATOM   19649 O  O     . GLY B 2  1143 ? 151.189 130.789 117.057 1.00 22.33  ? 1143 GLY B O     1 
ATOM   19650 N  N     . GLY B 2  1144 ? 150.768 129.041 118.412 1.00 8.78   ? 1144 GLY B N     1 
ATOM   19651 C  CA    . GLY B 2  1144 ? 149.511 128.704 117.788 1.00 5.45   ? 1144 GLY B CA    1 
ATOM   19652 C  C     . GLY B 2  1144 ? 148.316 129.166 118.597 1.00 7.64   ? 1144 GLY B C     1 
ATOM   19653 O  O     . GLY B 2  1144 ? 148.442 129.776 119.649 1.00 17.31  ? 1144 GLY B O     1 
ATOM   19654 N  N     . LEU B 2  1145 ? 147.135 128.862 118.074 1.00 2.64   ? 1145 LEU B N     1 
ATOM   19655 C  CA    . LEU B 2  1145 ? 145.880 129.151 118.746 1.00 1.50   ? 1145 LEU B CA    1 
ATOM   19656 C  C     . LEU B 2  1145 ? 145.288 127.871 119.310 1.00 0.75   ? 1145 LEU B C     1 
ATOM   19657 O  O     . LEU B 2  1145 ? 145.636 126.766 118.909 1.00 12.22  ? 1145 LEU B O     1 
ATOM   19658 C  CB    . LEU B 2  1145 ? 144.895 129.827 117.795 1.00 5.90   ? 1145 LEU B CB    1 
ATOM   19659 C  CG    . LEU B 2  1145 ? 145.375 131.139 117.184 1.00 6.61   ? 1145 LEU B CG    1 
ATOM   19660 C  CD1   . LEU B 2  1145 ? 144.431 131.570 116.102 1.00 1.46   ? 1145 LEU B CD1   1 
ATOM   19661 C  CD2   . LEU B 2  1145 ? 145.519 132.209 118.244 1.00 4.67   ? 1145 LEU B CD2   1 
ATOM   19662 N  N     . ARG B 2  1146 ? 144.366 128.033 120.246 1.00 0.79   ? 1146 ARG B N     1 
ATOM   19663 C  CA    . ARG B 2  1146 ? 143.867 126.926 121.046 1.00 1.89   ? 1146 ARG B CA    1 
ATOM   19664 C  C     . ARG B 2  1146 ? 142.561 126.376 120.495 1.00 3.70   ? 1146 ARG B C     1 
ATOM   19665 O  O     . ARG B 2  1146 ? 141.619 127.131 120.248 1.00 13.05  ? 1146 ARG B O     1 
ATOM   19666 C  CB    . ARG B 2  1146 ? 143.663 127.360 122.492 1.00 1.14   ? 1146 ARG B CB    1 
ATOM   19667 C  CG    . ARG B 2  1146 ? 143.189 126.251 123.354 1.00 15.89  ? 1146 ARG B CG    1 
ATOM   19668 C  CD    . ARG B 2  1146 ? 143.269 126.595 124.795 1.00 2.68   ? 1146 ARG B CD    1 
ATOM   19669 N  NE    . ARG B 2  1146 ? 142.735 125.511 125.602 1.00 9.11   ? 1146 ARG B NE    1 
ATOM   19670 C  CZ    . ARG B 2  1146 ? 143.391 124.396 125.882 1.00 11.70  ? 1146 ARG B CZ    1 
ATOM   19671 N  NH1   . ARG B 2  1146 ? 144.643 124.219 125.506 1.00 5.80   ? 1146 ARG B NH1   1 
ATOM   19672 N  NH2   . ARG B 2  1146 ? 142.773 123.434 126.555 1.00 14.34  ? 1146 ARG B NH2   1 
ATOM   19673 N  N     . LEU B 2  1147 ? 142.513 125.059 120.316 1.00 0.99   ? 1147 LEU B N     1 
ATOM   19674 C  CA    . LEU B 2  1147 ? 141.270 124.318 120.116 1.00 0.92   ? 1147 LEU B CA    1 
ATOM   19675 C  C     . LEU B 2  1147 ? 140.970 123.620 121.436 1.00 1.54   ? 1147 LEU B C     1 
ATOM   19676 O  O     . LEU B 2  1147 ? 141.514 122.562 121.734 1.00 0.29   ? 1147 LEU B O     1 
ATOM   19677 C  CB    . LEU B 2  1147 ? 141.394 123.319 118.975 1.00 6.95   ? 1147 LEU B CB    1 
ATOM   19678 C  CG    . LEU B 2  1147 ? 141.464 123.845 117.546 1.00 6.48   ? 1147 LEU B CG    1 
ATOM   19679 C  CD1   . LEU B 2  1147 ? 141.306 122.712 116.570 1.00 0.07   ? 1147 LEU B CD1   1 
ATOM   19680 C  CD2   . LEU B 2  1147 ? 140.429 124.910 117.303 1.00 8.00   ? 1147 LEU B CD2   1 
ATOM   19681 N  N     . GLY B 2  1148 ? 140.089 124.214 122.225 1.00 9.91   ? 1148 GLY B N     1 
ATOM   19682 C  CA    . GLY B 2  1148 ? 139.878 123.762 123.581 1.00 7.25   ? 1148 GLY B CA    1 
ATOM   19683 C  C     . GLY B 2  1148 ? 138.998 122.546 123.762 1.00 8.10   ? 1148 GLY B C     1 
ATOM   19684 O  O     . GLY B 2  1148 ? 138.687 121.835 122.811 1.00 7.71   ? 1148 GLY B O     1 
ATOM   19685 N  N     . GLU B 2  1149 ? 138.607 122.301 125.008 1.00 14.94  ? 1149 GLU B N     1 
ATOM   19686 C  CA    . GLU B 2  1149 ? 137.769 121.158 125.349 1.00 2.31   ? 1149 GLU B CA    1 
ATOM   19687 C  C     . GLU B 2  1149 ? 136.406 121.240 124.676 1.00 12.46  ? 1149 GLU B C     1 
ATOM   19688 O  O     . GLU B 2  1149 ? 135.884 120.236 124.192 1.00 2.57   ? 1149 GLU B O     1 
ATOM   19689 C  CB    . GLU B 2  1149 ? 137.619 121.096 126.862 1.00 7.98   ? 1149 GLU B CB    1 
ATOM   19690 C  CG    . GLU B 2  1149 ? 137.196 119.785 127.418 1.00 5.97   ? 1149 GLU B CG    1 
ATOM   19691 C  CD    . GLU B 2  1149 ? 137.149 119.801 128.924 1.00 13.21  ? 1149 GLU B CD    1 
ATOM   19692 O  OE1   . GLU B 2  1149 ? 137.549 120.813 129.523 1.00 13.46  ? 1149 GLU B OE1   1 
ATOM   19693 O  OE2   . GLU B 2  1149 ? 136.688 118.808 129.514 1.00 12.21  ? 1149 GLU B OE2   1 
ATOM   19694 N  N     . MET B 2  1150 ? 135.821 122.431 124.638 1.00 1.58   ? 1150 MET B N     1 
ATOM   19695 C  CA    . MET B 2  1150 ? 134.499 122.645 124.072 1.00 4.58   ? 1150 MET B CA    1 
ATOM   19696 C  C     . MET B 2  1150 ? 134.481 122.482 122.560 1.00 6.93   ? 1150 MET B C     1 
ATOM   19697 O  O     . MET B 2  1150 ? 133.441 122.132 122.004 1.00 2.06   ? 1150 MET B O     1 
ATOM   19698 C  CB    . MET B 2  1150 ? 134.036 124.038 124.463 1.00 11.91  ? 1150 MET B CB    1 
ATOM   19699 C  CG    . MET B 2  1150 ? 133.358 124.098 125.806 1.00 3.07   ? 1150 MET B CG    1 
ATOM   19700 S  SD    . MET B 2  1150 ? 132.623 125.694 126.170 1.00 26.08  ? 1150 MET B SD    1 
ATOM   19701 C  CE    . MET B 2  1150 ? 131.166 125.606 125.168 1.00 4.51   ? 1150 MET B CE    1 
ATOM   19702 N  N     . GLU B 2  1151 ? 135.600 122.735 121.886 1.00 1.34   ? 1151 GLU B N     1 
ATOM   19703 C  CA    . GLU B 2  1151 ? 135.687 122.549 120.444 1.00 9.66   ? 1151 GLU B CA    1 
ATOM   19704 C  C     . GLU B 2  1151 ? 135.832 121.088 120.061 1.00 15.03  ? 1151 GLU B C     1 
ATOM   19705 O  O     . GLU B 2  1151 ? 135.443 120.705 118.962 1.00 0.15   ? 1151 GLU B O     1 
ATOM   19706 C  CB    . GLU B 2  1151 ? 136.855 123.356 119.876 1.00 12.50  ? 1151 GLU B CB    1 
ATOM   19707 C  CG    . GLU B 2  1151 ? 136.577 124.834 119.733 1.00 7.60   ? 1151 GLU B CG    1 
ATOM   19708 C  CD    . GLU B 2  1151 ? 136.915 125.628 120.978 1.00 10.72  ? 1151 GLU B CD    1 
ATOM   19709 O  OE1   . GLU B 2  1151 ? 138.082 126.020 121.132 1.00 14.44  ? 1151 GLU B OE1   1 
ATOM   19710 O  OE2   . GLU B 2  1151 ? 136.024 125.864 121.814 1.00 14.42  ? 1151 GLU B OE2   1 
ATOM   19711 N  N     . HIS B 2  1152 ? 136.403 120.269 120.936 1.00 8.30   ? 1152 HIS B N     1 
ATOM   19712 C  CA    . HIS B 2  1152 ? 136.479 118.835 120.696 1.00 5.17   ? 1152 HIS B CA    1 
ATOM   19713 C  C     . HIS B 2  1152 ? 135.142 118.149 120.896 1.00 5.78   ? 1152 HIS B C     1 
ATOM   19714 O  O     . HIS B 2  1152 ? 134.876 117.138 120.246 1.00 3.50   ? 1152 HIS B O     1 
ATOM   19715 C  CB    . HIS B 2  1152 ? 137.522 118.207 121.611 1.00 4.54   ? 1152 HIS B CB    1 
ATOM   19716 C  CG    . HIS B 2  1152 ? 138.923 118.403 121.140 1.00 2.11   ? 1152 HIS B CG    1 
ATOM   19717 N  ND1   . HIS B 2  1152 ? 139.632 119.556 121.386 1.00 1.81   ? 1152 HIS B ND1   1 
ATOM   19718 C  CD2   . HIS B 2  1152 ? 139.745 117.599 120.431 1.00 9.47   ? 1152 HIS B CD2   1 
ATOM   19719 C  CE1   . HIS B 2  1152 ? 140.832 119.453 120.851 1.00 2.06   ? 1152 HIS B CE1   1 
ATOM   19720 N  NE2   . HIS B 2  1152 ? 140.925 118.276 120.264 1.00 9.01   ? 1152 HIS B NE2   1 
ATOM   19721 N  N     . TRP B 2  1153 ? 134.310 118.662 121.801 1.00 3.87   ? 1153 TRP B N     1 
ATOM   19722 C  CA    . TRP B 2  1153 ? 132.950 118.158 121.940 1.00 11.98  ? 1153 TRP B CA    1 
ATOM   19723 C  C     . TRP B 2  1153 ? 132.147 118.405 120.677 1.00 0.55   ? 1153 TRP B C     1 
ATOM   19724 O  O     . TRP B 2  1153 ? 131.373 117.546 120.251 1.00 4.94   ? 1153 TRP B O     1 
ATOM   19725 C  CB    . TRP B 2  1153 ? 132.255 118.823 123.121 1.00 6.33   ? 1153 TRP B CB    1 
ATOM   19726 C  CG    . TRP B 2  1153 ? 132.897 118.619 124.442 1.00 2.07   ? 1153 TRP B CG    1 
ATOM   19727 C  CD1   . TRP B 2  1153 ? 133.775 117.647 124.788 1.00 8.62   ? 1153 TRP B CD1   1 
ATOM   19728 C  CD2   . TRP B 2  1153 ? 132.714 119.427 125.601 1.00 1.34   ? 1153 TRP B CD2   1 
ATOM   19729 N  NE1   . TRP B 2  1153 ? 134.151 117.797 126.092 1.00 3.11   ? 1153 TRP B NE1   1 
ATOM   19730 C  CE2   . TRP B 2  1153 ? 133.508 118.886 126.614 1.00 1.31   ? 1153 TRP B CE2   1 
ATOM   19731 C  CE3   . TRP B 2  1153 ? 131.946 120.559 125.879 1.00 0.28   ? 1153 TRP B CE3   1 
ATOM   19732 C  CZ2   . TRP B 2  1153 ? 133.563 119.432 127.883 1.00 1.28   ? 1153 TRP B CZ2   1 
ATOM   19733 C  CZ3   . TRP B 2  1153 ? 131.998 121.095 127.135 1.00 0.17   ? 1153 TRP B CZ3   1 
ATOM   19734 C  CH2   . TRP B 2  1153 ? 132.804 120.537 128.125 1.00 3.07   ? 1153 TRP B CH2   1 
ATOM   19735 N  N     . VAL B 2  1154 ? 132.308 119.583 120.072 1.00 3.82   ? 1154 VAL B N     1 
ATOM   19736 C  CA    . VAL B 2  1154 ? 131.567 119.908 118.860 1.00 4.35   ? 1154 VAL B CA    1 
ATOM   19737 C  C     . VAL B 2  1154 ? 132.016 119.032 117.700 1.00 5.42   ? 1154 VAL B C     1 
ATOM   19738 O  O     . VAL B 2  1154 ? 131.194 118.573 116.908 1.00 8.85   ? 1154 VAL B O     1 
ATOM   19739 C  CB    . VAL B 2  1154 ? 131.698 121.405 118.531 1.00 15.98  ? 1154 VAL B CB    1 
ATOM   19740 C  CG1   . VAL B 2  1154 ? 131.080 121.715 117.187 1.00 4.42   ? 1154 VAL B CG1   1 
ATOM   19741 C  CG2   . VAL B 2  1154 ? 131.034 122.223 119.580 1.00 13.67  ? 1154 VAL B CG2   1 
ATOM   19742 N  N     . LEU B 2  1155 ? 133.317 118.785 117.574 1.00 10.60  ? 1155 LEU B N     1 
ATOM   19743 C  CA    . LEU B 2  1155 ? 133.803 117.974 116.465 1.00 11.42  ? 1155 LEU B CA    1 
ATOM   19744 C  C     . LEU B 2  1155 ? 133.470 116.502 116.644 1.00 2.53   ? 1155 LEU B C     1 
ATOM   19745 O  O     . LEU B 2  1155 ? 133.334 115.779 115.656 1.00 2.62   ? 1155 LEU B O     1 
ATOM   19746 C  CB    . LEU B 2  1155 ? 135.304 118.161 116.289 1.00 12.37  ? 1155 LEU B CB    1 
ATOM   19747 C  CG    . LEU B 2  1155 ? 135.770 119.396 115.532 1.00 7.85   ? 1155 LEU B CG    1 
ATOM   19748 C  CD1   . LEU B 2  1155 ? 137.253 119.563 115.695 1.00 0.46   ? 1155 LEU B CD1   1 
ATOM   19749 C  CD2   . LEU B 2  1155 ? 135.412 119.288 114.070 1.00 2.43   ? 1155 LEU B CD2   1 
ATOM   19750 N  N     . THR B 2  1156 ? 133.357 116.034 117.883 1.00 13.56  ? 1156 THR B N     1 
ATOM   19751 C  CA    . THR B 2  1156 ? 132.925 114.665 118.131 1.00 17.98  ? 1156 THR B CA    1 
ATOM   19752 C  C     . THR B 2  1156 ? 131.426 114.505 117.922 1.00 13.51  ? 1156 THR B C     1 
ATOM   19753 O  O     . THR B 2  1156 ? 130.970 113.453 117.474 1.00 17.99  ? 1156 THR B O     1 
ATOM   19754 C  CB    . THR B 2  1156 ? 133.311 114.241 119.544 1.00 11.37  ? 1156 THR B CB    1 
ATOM   19755 O  OG1   . THR B 2  1156 ? 134.648 114.656 119.814 1.00 13.46  ? 1156 THR B OG1   1 
ATOM   19756 C  CG2   . THR B 2  1156 ? 133.251 112.755 119.666 1.00 15.57  ? 1156 THR B CG2   1 
ATOM   19757 N  N     . ALA B 2  1157 ? 130.644 115.527 118.254 1.00 15.70  ? 1157 ALA B N     1 
ATOM   19758 C  CA    . ALA B 2  1157 ? 129.217 115.490 117.973 1.00 11.60  ? 1157 ALA B CA    1 
ATOM   19759 C  C     . ALA B 2  1157 ? 128.953 115.447 116.479 1.00 14.34  ? 1157 ALA B C     1 
ATOM   19760 O  O     . ALA B 2  1157 ? 127.908 114.965 116.040 1.00 19.92  ? 1157 ALA B O     1 
ATOM   19761 C  CB    . ALA B 2  1157 ? 128.528 116.694 118.605 1.00 12.57  ? 1157 ALA B CB    1 
ATOM   19762 N  N     . GLN B 2  1158 ? 129.882 115.958 115.679 1.00 6.74   ? 1158 GLN B N     1 
ATOM   19763 C  CA    . GLN B 2  1158 ? 129.745 115.883 114.236 1.00 4.48   ? 1158 GLN B CA    1 
ATOM   19764 C  C     . GLN B 2  1158 ? 130.258 114.570 113.668 1.00 3.97   ? 1158 GLN B C     1 
ATOM   19765 O  O     . GLN B 2  1158 ? 129.873 114.207 112.559 1.00 6.91   ? 1158 GLN B O     1 
ATOM   19766 C  CB    . GLN B 2  1158 ? 130.472 117.054 113.587 1.00 2.76   ? 1158 GLN B CB    1 
ATOM   19767 C  CG    . GLN B 2  1158 ? 129.895 118.392 113.960 1.00 8.12   ? 1158 GLN B CG    1 
ATOM   19768 C  CD    . GLN B 2  1158 ? 130.696 119.554 113.441 1.00 0.15   ? 1158 GLN B CD    1 
ATOM   19769 O  OE1   . GLN B 2  1158 ? 131.767 119.383 112.886 1.00 1.44   ? 1158 GLN B OE1   1 
ATOM   19770 N  NE2   . GLN B 2  1158 ? 130.170 120.750 113.610 1.00 1.65   ? 1158 GLN B NE2   1 
ATOM   19771 N  N     . GLY B 2  1159 ? 131.094 113.844 114.399 1.00 9.38   ? 1159 GLY B N     1 
ATOM   19772 C  CA    . GLY B 2  1159 ? 131.716 112.651 113.877 1.00 7.66   ? 1159 GLY B CA    1 
ATOM   19773 C  C     . GLY B 2  1159 ? 132.950 112.885 113.046 1.00 13.85  ? 1159 GLY B C     1 
ATOM   19774 O  O     . GLY B 2  1159 ? 133.366 111.983 112.321 1.00 14.27  ? 1159 GLY B O     1 
ATOM   19775 N  N     . ALA B 2  1160 ? 133.546 114.072 113.130 1.00 21.51  ? 1160 ALA B N     1 
ATOM   19776 C  CA    . ALA B 2  1160 ? 134.681 114.468 112.304 1.00 9.72   ? 1160 ALA B CA    1 
ATOM   19777 C  C     . ALA B 2  1160 ? 135.971 114.047 112.994 1.00 7.38   ? 1160 ALA B C     1 
ATOM   19778 O  O     . ALA B 2  1160 ? 136.643 114.829 113.660 1.00 11.77  ? 1160 ALA B O     1 
ATOM   19779 C  CB    . ALA B 2  1160 ? 134.646 115.967 112.054 1.00 10.73  ? 1160 ALA B CB    1 
ATOM   19780 N  N     . MET B 2  1161 ? 136.319 112.779 112.820 1.00 1.51   ? 1161 MET B N     1 
ATOM   19781 C  CA    . MET B 2  1161 ? 137.442 112.175 113.521 1.00 7.27   ? 1161 MET B CA    1 
ATOM   19782 C  C     . MET B 2  1161 ? 138.754 112.305 112.772 1.00 12.69  ? 1161 MET B C     1 
ATOM   19783 O  O     . MET B 2  1161 ? 139.811 112.333 113.401 1.00 5.21   ? 1161 MET B O     1 
ATOM   19784 C  CB    . MET B 2  1161 ? 137.152 110.703 113.787 1.00 3.64   ? 1161 MET B CB    1 
ATOM   19785 C  CG    . MET B 2  1161 ? 136.134 110.456 114.855 1.00 10.80  ? 1161 MET B CG    1 
ATOM   19786 S  SD    . MET B 2  1161 ? 136.605 111.125 116.446 1.00 15.89  ? 1161 MET B SD    1 
ATOM   19787 C  CE    . MET B 2  1161 ? 135.334 112.347 116.636 1.00 7.14   ? 1161 MET B CE    1 
ATOM   19788 N  N     . GLN B 2  1162 ? 138.714 112.374 111.447 1.00 2.59   ? 1162 GLN B N     1 
ATOM   19789 C  CA    . GLN B 2  1162 ? 139.905 112.627 110.654 1.00 11.86  ? 1162 GLN B CA    1 
ATOM   19790 C  C     . GLN B 2  1162 ? 140.386 114.063 110.757 1.00 13.48  ? 1162 GLN B C     1 
ATOM   19791 O  O     . GLN B 2  1162 ? 141.543 114.339 110.442 1.00 14.97  ? 1162 GLN B O     1 
ATOM   19792 C  CB    . GLN B 2  1162 ? 139.637 112.267 109.197 1.00 2.44   ? 1162 GLN B CB    1 
ATOM   19793 C  CG    . GLN B 2  1162 ? 139.615 110.788 108.970 1.00 5.18   ? 1162 GLN B CG    1 
ATOM   19794 C  CD    . GLN B 2  1162 ? 138.627 110.364 107.929 1.00 4.78   ? 1162 GLN B CD    1 
ATOM   19795 O  OE1   . GLN B 2  1162 ? 137.691 111.082 107.611 1.00 7.03   ? 1162 GLN B OE1   1 
ATOM   19796 N  NE2   . GLN B 2  1162 ? 138.840 109.191 107.371 1.00 10.63  ? 1162 GLN B NE2   1 
ATOM   19797 N  N     . THR B 2  1163 ? 139.515 114.977 111.163 1.00 2.19   ? 1163 THR B N     1 
ATOM   19798 C  CA    . THR B 2  1163 ? 139.901 116.348 111.446 1.00 5.75   ? 1163 THR B CA    1 
ATOM   19799 C  C     . THR B 2  1163 ? 140.549 116.479 112.813 1.00 3.26   ? 1163 THR B C     1 
ATOM   19800 O  O     . THR B 2  1163 ? 141.435 117.314 112.994 1.00 0.73   ? 1163 THR B O     1 
ATOM   19801 C  CB    . THR B 2  1163 ? 138.672 117.245 111.335 1.00 15.85  ? 1163 THR B CB    1 
ATOM   19802 O  OG1   . THR B 2  1163 ? 138.023 116.976 110.092 1.00 2.97   ? 1163 THR B OG1   1 
ATOM   19803 C  CG2   . THR B 2  1163 ? 139.042 118.706 111.404 1.00 12.19  ? 1163 THR B CG2   1 
ATOM   19804 N  N     . ILE B 2  1164 ? 140.122 115.667 113.776 1.00 12.38  ? 1164 ILE B N     1 
ATOM   19805 C  CA    . ILE B 2  1164 ? 140.747 115.657 115.091 1.00 0.82   ? 1164 ILE B CA    1 
ATOM   19806 C  C     . ILE B 2  1164 ? 142.170 115.118 115.002 1.00 1.24   ? 1164 ILE B C     1 
ATOM   19807 O  O     . ILE B 2  1164 ? 143.069 115.584 115.706 1.00 7.57   ? 1164 ILE B O     1 
ATOM   19808 C  CB    . ILE B 2  1164 ? 139.874 114.855 116.075 1.00 15.40  ? 1164 ILE B CB    1 
ATOM   19809 C  CG1   . ILE B 2  1164 ? 138.635 115.667 116.436 1.00 2.18   ? 1164 ILE B CG1   1 
ATOM   19810 C  CG2   . ILE B 2  1164 ? 140.627 114.513 117.332 1.00 5.34   ? 1164 ILE B CG2   1 
ATOM   19811 C  CD1   . ILE B 2  1164 ? 137.706 115.004 117.378 1.00 10.70  ? 1164 ILE B CD1   1 
ATOM   19812 N  N     . ILE B 2  1165 ? 142.399 114.138 114.131 1.00 5.63   ? 1165 ILE B N     1 
ATOM   19813 C  CA    . ILE B 2  1165 ? 143.751 113.646 113.897 1.00 1.29   ? 1165 ILE B CA    1 
ATOM   19814 C  C     . ILE B 2  1165 ? 144.624 114.741 113.310 1.00 11.11  ? 1165 ILE B C     1 
ATOM   19815 O  O     . ILE B 2  1165 ? 145.780 114.910 113.702 1.00 10.08  ? 1165 ILE B O     1 
ATOM   19816 C  CB    . ILE B 2  1165 ? 143.725 112.408 112.986 1.00 3.83   ? 1165 ILE B CB    1 
ATOM   19817 C  CG1   . ILE B 2  1165 ? 143.079 111.237 113.702 1.00 2.63   ? 1165 ILE B CG1   1 
ATOM   19818 C  CG2   . ILE B 2  1165 ? 145.118 112.028 112.570 1.00 4.79   ? 1165 ILE B CG2   1 
ATOM   19819 C  CD1   . ILE B 2  1165 ? 142.776 110.101 112.809 1.00 12.31  ? 1165 ILE B CD1   1 
ATOM   19820 N  N     . GLU B 2  1166 ? 144.091 115.504 112.366 1.00 8.10   ? 1166 GLU B N     1 
ATOM   19821 C  CA    . GLU B 2  1166 ? 144.905 116.501 111.690 1.00 1.98   ? 1166 GLU B CA    1 
ATOM   19822 C  C     . GLU B 2  1166 ? 145.292 117.643 112.616 1.00 1.60   ? 1166 GLU B C     1 
ATOM   19823 O  O     . GLU B 2  1166 ? 146.373 118.213 112.479 1.00 3.31   ? 1166 GLU B O     1 
ATOM   19824 C  CB    . GLU B 2  1166 ? 144.167 117.037 110.483 1.00 3.64   ? 1166 GLU B CB    1 
ATOM   19825 C  CG    . GLU B 2  1166 ? 145.080 117.596 109.441 1.00 2.54   ? 1166 GLU B CG    1 
ATOM   19826 C  CD    . GLU B 2  1166 ? 144.473 118.743 108.710 1.00 2.95   ? 1166 GLU B CD    1 
ATOM   19827 O  OE1   . GLU B 2  1166 ? 143.735 119.518 109.334 1.00 9.95   ? 1166 GLU B OE1   1 
ATOM   19828 O  OE2   . GLU B 2  1166 ? 144.697 118.855 107.501 1.00 4.66   ? 1166 GLU B OE2   1 
ATOM   19829 N  N     . LYS B 2  1167 ? 144.429 117.999 113.555 1.00 3.36   ? 1167 LYS B N     1 
ATOM   19830 C  CA    . LYS B 2  1167 ? 144.667 119.180 114.368 1.00 5.41   ? 1167 LYS B CA    1 
ATOM   19831 C  C     . LYS B 2  1167 ? 145.342 118.849 115.690 1.00 3.23   ? 1167 LYS B C     1 
ATOM   19832 O  O     . LYS B 2  1167 ? 146.307 119.507 116.073 1.00 7.63   ? 1167 LYS B O     1 
ATOM   19833 C  CB    . LYS B 2  1167 ? 143.351 119.921 114.618 1.00 9.14   ? 1167 LYS B CB    1 
ATOM   19834 C  CG    . LYS B 2  1167 ? 142.664 120.414 113.364 1.00 5.24   ? 1167 LYS B CG    1 
ATOM   19835 C  CD    . LYS B 2  1167 ? 143.633 121.113 112.446 1.00 0.82   ? 1167 LYS B CD    1 
ATOM   19836 C  CE    . LYS B 2  1167 ? 143.967 122.490 112.930 1.00 4.46   ? 1167 LYS B CE    1 
ATOM   19837 N  NZ    . LYS B 2  1167 ? 144.924 123.141 112.025 1.00 5.95   ? 1167 LYS B NZ    1 
ATOM   19838 N  N     . SER B 2  1168 ? 144.845 117.850 116.408 1.00 1.03   ? 1168 SER B N     1 
ATOM   19839 C  CA    . SER B 2  1168 ? 145.401 117.540 117.714 1.00 1.51   ? 1168 SER B CA    1 
ATOM   19840 C  C     . SER B 2  1168 ? 146.601 116.616 117.644 1.00 1.56   ? 1168 SER B C     1 
ATOM   19841 O  O     . SER B 2  1168 ? 147.290 116.450 118.648 1.00 16.41  ? 1168 SER B O     1 
ATOM   19842 C  CB    . SER B 2  1168 ? 144.331 116.925 118.603 1.00 9.13   ? 1168 SER B CB    1 
ATOM   19843 O  OG    . SER B 2  1168 ? 143.341 117.883 118.894 1.00 10.58  ? 1168 SER B OG    1 
ATOM   19844 N  N     . HIS B 2  1169 ? 146.866 116.005 116.499 1.00 8.92   ? 1169 HIS B N     1 
ATOM   19845 C  CA    . HIS B 2  1169 ? 148.025 115.145 116.349 1.00 1.11   ? 1169 HIS B CA    1 
ATOM   19846 C  C     . HIS B 2  1169 ? 149.018 115.694 115.336 1.00 4.65   ? 1169 HIS B C     1 
ATOM   19847 O  O     . HIS B 2  1169 ? 150.156 115.991 115.686 1.00 15.00  ? 1169 HIS B O     1 
ATOM   19848 C  CB    . HIS B 2  1169 ? 147.577 113.734 115.958 1.00 1.80   ? 1169 HIS B CB    1 
ATOM   19849 C  CG    . HIS B 2  1169 ? 146.767 113.042 117.009 1.00 1.34   ? 1169 HIS B CG    1 
ATOM   19850 N  ND1   . HIS B 2  1169 ? 145.521 113.479 117.397 1.00 3.86   ? 1169 HIS B ND1   1 
ATOM   19851 C  CD2   . HIS B 2  1169 ? 147.031 111.951 117.761 1.00 14.16  ? 1169 HIS B CD2   1 
ATOM   19852 C  CE1   . HIS B 2  1169 ? 145.051 112.686 118.339 1.00 1.23   ? 1169 HIS B CE1   1 
ATOM   19853 N  NE2   . HIS B 2  1169 ? 145.948 111.749 118.578 1.00 0.24   ? 1169 HIS B NE2   1 
ATOM   19854 N  N     . ASP B 2  1170 ? 148.609 115.875 114.087 1.00 8.67   ? 1170 ASP B N     1 
ATOM   19855 C  CA    . ASP B 2  1170 ? 149.531 116.336 113.060 1.00 7.85   ? 1170 ASP B CA    1 
ATOM   19856 C  C     . ASP B 2  1170 ? 149.937 117.779 113.253 1.00 10.62  ? 1170 ASP B C     1 
ATOM   19857 O  O     . ASP B 2  1170 ? 151.045 118.156 112.871 1.00 6.05   ? 1170 ASP B O     1 
ATOM   19858 C  CB    . ASP B 2  1170 ? 148.906 116.179 111.683 1.00 1.44   ? 1170 ASP B CB    1 
ATOM   19859 C  CG    . ASP B 2  1170 ? 148.626 114.754 111.341 1.00 7.34   ? 1170 ASP B CG    1 
ATOM   19860 O  OD1   . ASP B 2  1170 ? 148.926 113.884 112.168 1.00 9.10   ? 1170 ASP B OD1   1 
ATOM   19861 O  OD2   . ASP B 2  1170 ? 148.068 114.499 110.258 1.00 15.10  ? 1170 ASP B OD2   1 
ATOM   19862 N  N     . ASP B 2  1171 ? 149.071 118.590 113.833 1.00 6.67   ? 1171 ASP B N     1 
ATOM   19863 C  CA    . ASP B 2  1171 ? 149.359 119.992 114.028 1.00 10.60  ? 1171 ASP B CA    1 
ATOM   19864 C  C     . ASP B 2  1171 ? 149.635 120.358 115.467 1.00 0.94   ? 1171 ASP B C     1 
ATOM   19865 O  O     . ASP B 2  1171 ? 150.019 121.498 115.717 1.00 2.76   ? 1171 ASP B O     1 
ATOM   19866 C  CB    . ASP B 2  1171 ? 148.201 120.856 113.515 1.00 0.13   ? 1171 ASP B CB    1 
ATOM   19867 C  CG    . ASP B 2  1171 ? 148.284 121.111 112.040 1.00 1.84   ? 1171 ASP B CG    1 
ATOM   19868 O  OD1   . ASP B 2  1171 ? 149.403 121.188 111.515 1.00 13.70  ? 1171 ASP B OD1   1 
ATOM   19869 O  OD2   . ASP B 2  1171 ? 147.235 121.234 111.397 1.00 5.55   ? 1171 ASP B OD2   1 
ATOM   19870 N  N     . SER B 2  1172 ? 149.367 119.479 116.429 1.00 6.34   ? 1172 SER B N     1 
ATOM   19871 C  CA    . SER B 2  1172 ? 149.791 119.820 117.774 1.00 0.25   ? 1172 SER B CA    1 
ATOM   19872 C  C     . SER B 2  1172 ? 151.039 119.081 118.243 1.00 7.49   ? 1172 SER B C     1 
ATOM   19873 O  O     . SER B 2  1172 ? 152.145 119.607 118.121 1.00 19.43  ? 1172 SER B O     1 
ATOM   19874 C  CB    . SER B 2  1172 ? 148.636 119.553 118.735 1.00 12.39  ? 1172 SER B CB    1 
ATOM   19875 O  OG    . SER B 2  1172 ? 148.920 120.009 120.033 1.00 5.62   ? 1172 SER B OG    1 
ATOM   19876 N  N     . ASP B 2  1173 ? 150.897 117.829 118.702 1.00 6.29   ? 1173 ASP B N     1 
ATOM   19877 C  CA    . ASP B 2  1173 ? 152.028 117.148 119.330 1.00 2.59   ? 1173 ASP B CA    1 
ATOM   19878 C  C     . ASP B 2  1173 ? 151.992 115.638 119.147 1.00 0.05   ? 1173 ASP B C     1 
ATOM   19879 O  O     . ASP B 2  1173 ? 152.452 114.906 120.026 1.00 4.67   ? 1173 ASP B O     1 
ATOM   19880 C  CB    . ASP B 2  1173 ? 152.125 117.473 120.824 1.00 1.15   ? 1173 ASP B CB    1 
ATOM   19881 C  CG    . ASP B 2  1173 ? 150.904 117.044 121.605 1.00 10.99  ? 1173 ASP B CG    1 
ATOM   19882 O  OD1   . ASP B 2  1173 ? 149.805 116.983 121.031 1.00 14.25  ? 1173 ASP B OD1   1 
ATOM   19883 O  OD2   . ASP B 2  1173 ? 151.034 116.803 122.814 1.00 5.86   ? 1173 ASP B OD2   1 
ATOM   19884 N  N     . GLY B 2  1174 ? 151.444 115.149 118.044 1.00 0.17   ? 1174 GLY B N     1 
ATOM   19885 C  CA    . GLY B 2  1174 ? 151.400 113.718 117.838 1.00 7.33   ? 1174 GLY B CA    1 
ATOM   19886 C  C     . GLY B 2  1174 ? 152.789 113.115 117.781 1.00 7.00   ? 1174 GLY B C     1 
ATOM   19887 O  O     . GLY B 2  1174 ? 153.721 113.690 117.226 1.00 13.37  ? 1174 GLY B O     1 
ATOM   19888 N  N     . CYS B 2  1175 ? 152.916 111.927 118.359 1.00 11.17  ? 1175 CYS B N     1 
ATOM   19889 C  CA    . CYS B 2  1175 ? 154.170 111.192 118.386 1.00 5.62   ? 1175 CYS B CA    1 
ATOM   19890 C  C     . CYS B 2  1175 ? 153.855 109.734 118.091 1.00 9.40   ? 1175 CYS B C     1 
ATOM   19891 O  O     . CYS B 2  1175 ? 152.715 109.376 117.794 1.00 11.22  ? 1175 CYS B O     1 
ATOM   19892 C  CB    . CYS B 2  1175 ? 154.883 111.357 119.729 1.00 5.73   ? 1175 CYS B CB    1 
ATOM   19893 S  SG    . CYS B 2  1175 ? 154.096 110.558 121.119 1.00 21.74  ? 1175 CYS B SG    1 
ATOM   19894 N  N     . ILE B 2  1176 ? 154.880 108.895 118.145 1.00 15.96  ? 1176 ILE B N     1 
ATOM   19895 C  CA    . ILE B 2  1176 ? 154.723 107.454 118.004 1.00 10.56  ? 1176 ILE B CA    1 
ATOM   19896 C  C     . ILE B 2  1176 ? 155.272 106.796 119.256 1.00 12.54  ? 1176 ILE B C     1 
ATOM   19897 O  O     . ILE B 2  1176 ? 156.380 107.113 119.699 1.00 16.31  ? 1176 ILE B O     1 
ATOM   19898 C  CB    . ILE B 2  1176 ? 155.420 106.914 116.747 1.00 3.84   ? 1176 ILE B CB    1 
ATOM   19899 C  CG1   . ILE B 2  1176 ? 154.676 107.378 115.501 1.00 5.40   ? 1176 ILE B CG1   1 
ATOM   19900 C  CG2   . ILE B 2  1176 ? 155.414 105.410 116.771 1.00 8.18   ? 1176 ILE B CG2   1 
ATOM   19901 C  CD1   . ILE B 2  1176 ? 155.424 107.155 114.234 1.00 11.26  ? 1176 ILE B CD1   1 
ATOM   19902 N  N     . SER B 2  1177 ? 154.490 105.901 119.832 1.00 11.70  ? 1177 SER B N     1 
ATOM   19903 C  CA    . SER B 2  1177 ? 154.853 105.187 121.041 1.00 6.44   ? 1177 SER B CA    1 
ATOM   19904 C  C     . SER B 2  1177 ? 155.147 103.736 120.686 1.00 11.00  ? 1177 SER B C     1 
ATOM   19905 O  O     . SER B 2  1177 ? 154.565 103.189 119.751 1.00 17.22  ? 1177 SER B O     1 
ATOM   19906 C  CB    . SER B 2  1177 ? 153.718 105.284 122.057 1.00 6.68   ? 1177 SER B CB    1 
ATOM   19907 O  OG    . SER B 2  1177 ? 154.030 104.638 123.268 1.00 20.17  ? 1177 SER B OG    1 
ATOM   19908 N  N     . TYR B 2  1178 ? 156.077 103.124 121.404 1.00 9.57   ? 1178 TYR B N     1 
ATOM   19909 C  CA    . TYR B 2  1178 ? 156.398 101.719 121.213 1.00 4.23   ? 1178 TYR B CA    1 
ATOM   19910 C  C     . TYR B 2  1178 ? 156.113 100.969 122.502 1.00 7.82   ? 1178 TYR B C     1 
ATOM   19911 O  O     . TYR B 2  1178 ? 156.527 101.399 123.579 1.00 12.64  ? 1178 TYR B O     1 
ATOM   19912 C  CB    . TYR B 2  1178 ? 157.847 101.543 120.759 1.00 8.64   ? 1178 TYR B CB    1 
ATOM   19913 C  CG    . TYR B 2  1178 ? 158.085 102.150 119.399 1.00 12.70  ? 1178 TYR B CG    1 
ATOM   19914 C  CD1   . TYR B 2  1178 ? 157.686 101.494 118.249 1.00 7.97   ? 1178 TYR B CD1   1 
ATOM   19915 C  CD2   . TYR B 2  1178 ? 158.673 103.391 119.268 1.00 10.19  ? 1178 TYR B CD2   1 
ATOM   19916 C  CE1   . TYR B 2  1178 ? 157.875 102.048 117.022 1.00 7.32   ? 1178 TYR B CE1   1 
ATOM   19917 C  CE2   . TYR B 2  1178 ? 158.866 103.951 118.040 1.00 5.60   ? 1178 TYR B CE2   1 
ATOM   19918 C  CZ    . TYR B 2  1178 ? 158.470 103.277 116.920 1.00 10.04  ? 1178 TYR B CZ    1 
ATOM   19919 O  OH    . TYR B 2  1178 ? 158.668 103.841 115.685 1.00 13.89  ? 1178 TYR B OH    1 
ATOM   19920 N  N     . ILE B 2  1179 ? 155.369 99.876  122.385 1.00 7.98   ? 1179 ILE B N     1 
ATOM   19921 C  CA    . ILE B 2  1179 ? 154.886 99.100  123.518 1.00 6.81   ? 1179 ILE B CA    1 
ATOM   19922 C  C     . ILE B 2  1179 ? 155.238 97.645  123.263 1.00 11.26  ? 1179 ILE B C     1 
ATOM   19923 O  O     . ILE B 2  1179 ? 155.226 97.191  122.118 1.00 17.72  ? 1179 ILE B O     1 
ATOM   19924 C  CB    . ILE B 2  1179 ? 153.362 99.267  123.707 1.00 8.37   ? 1179 ILE B CB    1 
ATOM   19925 C  CG1   . ILE B 2  1179 ? 152.974 100.743 123.684 1.00 3.87   ? 1179 ILE B CG1   1 
ATOM   19926 C  CG2   . ILE B 2  1179 ? 152.891 98.614  124.982 1.00 9.83   ? 1179 ILE B CG2   1 
ATOM   19927 C  CD1   . ILE B 2  1179 ? 152.965 101.390 125.015 1.00 7.36   ? 1179 ILE B CD1   1 
ATOM   19928 N  N     . CYS B 2  1180 ? 155.563 96.914  124.320 1.00 12.97  ? 1180 CYS B N     1 
ATOM   19929 C  CA    . CYS B 2  1180 ? 155.780 95.483  124.194 1.00 12.95  ? 1180 CYS B CA    1 
ATOM   19930 C  C     . CYS B 2  1180 ? 154.470 94.733  124.409 1.00 14.81  ? 1180 CYS B C     1 
ATOM   19931 O  O     . CYS B 2  1180 ? 153.768 94.970  125.393 1.00 17.45  ? 1180 CYS B O     1 
ATOM   19932 C  CB    . CYS B 2  1180 ? 156.837 95.019  125.192 1.00 17.31  ? 1180 CYS B CB    1 
ATOM   19933 S  SG    . CYS B 2  1180 ? 157.262 93.269  125.093 1.00 33.91  ? 1180 CYS B SG    1 
ATOM   19934 N  N     . ARG B 2  1181 ? 154.154 93.813  123.494 1.00 17.61  ? 1181 ARG B N     1 
ATOM   19935 C  CA    . ARG B 2  1181 ? 152.965 92.980  123.645 1.00 17.78  ? 1181 ARG B CA    1 
ATOM   19936 C  C     . ARG B 2  1181 ? 152.978 92.224  124.967 1.00 22.36  ? 1181 ARG B C     1 
ATOM   19937 O  O     . ARG B 2  1181 ? 151.955 92.138  125.652 1.00 29.45  ? 1181 ARG B O     1 
ATOM   19938 C  CB    . ARG B 2  1181 ? 152.874 91.969  122.502 1.00 17.72  ? 1181 ARG B CB    1 
ATOM   19939 C  CG    . ARG B 2  1181 ? 152.315 92.472  121.209 1.00 21.98  ? 1181 ARG B CG    1 
ATOM   19940 C  CD    . ARG B 2  1181 ? 150.834 92.570  121.272 1.00 23.72  ? 1181 ARG B CD    1 
ATOM   19941 N  NE    . ARG B 2  1181 ? 150.295 93.178  120.065 1.00 22.93  ? 1181 ARG B NE    1 
ATOM   19942 C  CZ    . ARG B 2  1181 ? 149.257 92.718  119.393 1.00 17.69  ? 1181 ARG B CZ    1 
ATOM   19943 N  NH1   . ARG B 2  1181 ? 148.579 91.670  119.813 1.00 24.23  ? 1181 ARG B NH1   1 
ATOM   19944 N  NH2   . ARG B 2  1181 ? 148.879 93.337  118.284 1.00 17.28  ? 1181 ARG B NH2   1 
ATOM   19945 N  N     . ASN B 2  1182 ? 154.125 91.652  125.332 1.00 22.34  ? 1182 ASN B N     1 
ATOM   19946 C  CA    . ASN B 2  1182 ? 154.171 90.666  126.403 1.00 21.39  ? 1182 ASN B CA    1 
ATOM   19947 C  C     . ASN B 2  1182 ? 154.072 91.267  127.790 1.00 23.23  ? 1182 ASN B C     1 
ATOM   19948 O  O     . ASN B 2  1182 ? 153.557 90.606  128.692 1.00 32.05  ? 1182 ASN B O     1 
ATOM   19949 C  CB    . ASN B 2  1182 ? 155.450 89.852  126.320 1.00 26.02  ? 1182 ASN B CB    1 
ATOM   19950 C  CG    . ASN B 2  1182 ? 155.485 88.963  125.127 1.00 28.95  ? 1182 ASN B CG    1 
ATOM   19951 O  OD1   . ASN B 2  1182 ? 156.448 88.236  124.917 1.00 34.68  ? 1182 ASN B OD1   1 
ATOM   19952 N  ND2   . ASN B 2  1182 ? 154.425 88.993  124.337 1.00 27.85  ? 1182 ASN B ND2   1 
ATOM   19953 N  N     . CYS B 2  1183 ? 154.569 92.473  128.002 1.00 20.54  ? 1183 CYS B N     1 
ATOM   19954 C  CA    . CYS B 2  1183 ? 154.501 93.068  129.321 1.00 21.58  ? 1183 CYS B CA    1 
ATOM   19955 C  C     . CYS B 2  1183 ? 153.616 94.296  129.401 1.00 26.30  ? 1183 CYS B C     1 
ATOM   19956 O  O     . CYS B 2  1183 ? 153.237 94.678  130.511 1.00 30.99  ? 1183 CYS B O     1 
ATOM   19957 C  CB    . CYS B 2  1183 ? 155.905 93.423  129.832 1.00 21.91  ? 1183 CYS B CB    1 
ATOM   19958 S  SG    . CYS B 2  1183 ? 156.906 94.451  128.763 1.00 25.47  ? 1183 CYS B SG    1 
ATOM   19959 N  N     . GLY B 2  1184 ? 153.255 94.911  128.280 1.00 14.67  ? 1184 GLY B N     1 
ATOM   19960 C  CA    . GLY B 2  1184 ? 152.480 96.127  128.316 1.00 11.54  ? 1184 GLY B CA    1 
ATOM   19961 C  C     . GLY B 2  1184 ? 153.255 97.358  128.707 1.00 16.67  ? 1184 GLY B C     1 
ATOM   19962 O  O     . GLY B 2  1184 ? 152.647 98.385  129.012 1.00 17.89  ? 1184 GLY B O     1 
ATOM   19963 N  N     . GLU B 2  1185 ? 154.557 97.286  128.721 1.00 17.37  ? 1185 GLU B N     1 
ATOM   19964 C  CA    . GLU B 2  1185 ? 155.425 98.376  129.120 1.00 15.67  ? 1185 GLU B CA    1 
ATOM   19965 C  C     . GLU B 2  1185 ? 156.033 99.045  127.898 1.00 18.35  ? 1185 GLU B C     1 
ATOM   19966 O  O     . GLU B 2  1185 ? 156.197 98.416  126.851 1.00 18.28  ? 1185 GLU B O     1 
ATOM   19967 C  CB    . GLU B 2  1185 ? 156.527 97.848  130.029 1.00 20.26  ? 1185 GLU B CB    1 
ATOM   19968 C  CG    . GLU B 2  1185 ? 156.036 97.094  131.245 1.00 23.77  ? 1185 GLU B CG    1 
ATOM   19969 C  CD    . GLU B 2  1185 ? 155.507 98.002  132.331 1.00 29.35  ? 1185 GLU B CD    1 
ATOM   19970 O  OE1   . GLU B 2  1185 ? 156.007 99.138  132.453 1.00 28.51  ? 1185 GLU B OE1   1 
ATOM   19971 O  OE2   . GLU B 2  1185 ? 154.588 97.581  133.064 1.00 26.26  ? 1185 GLU B OE2   1 
ATOM   19972 N  N     . PRO B 2  1186 ? 156.368 100.329 127.993 1.00 13.27  ? 1186 PRO B N     1 
ATOM   19973 C  CA    . PRO B 2  1186 ? 157.005 101.005 126.859 1.00 14.33  ? 1186 PRO B CA    1 
ATOM   19974 C  C     . PRO B 2  1186 ? 158.344 100.377 126.504 1.00 11.15  ? 1186 PRO B C     1 
ATOM   19975 O  O     . PRO B 2  1186 ? 159.137 100.016 127.372 1.00 12.61  ? 1186 PRO B O     1 
ATOM   19976 C  CB    . PRO B 2  1186 ? 157.165 102.446 127.350 1.00 14.52  ? 1186 PRO B CB    1 
ATOM   19977 C  CG    . PRO B 2  1186 ? 157.004 102.395 128.794 1.00 14.95  ? 1186 PRO B CG    1 
ATOM   19978 C  CD    . PRO B 2  1186 ? 156.140 101.242 129.120 1.00 10.27  ? 1186 PRO B CD    1 
ATOM   19979 N  N     . ALA B 2  1187 ? 158.590 100.256 125.210 1.00 13.69  ? 1187 ALA B N     1 
ATOM   19980 C  CA    . ALA B 2  1187 ? 159.779 99.619  124.677 1.00 12.56  ? 1187 ALA B CA    1 
ATOM   19981 C  C     . ALA B 2  1187 ? 160.670 100.652 124.001 1.00 18.52  ? 1187 ALA B C     1 
ATOM   19982 O  O     . ALA B 2  1187 ? 160.331 101.832 123.894 1.00 24.97  ? 1187 ALA B O     1 
ATOM   19983 C  CB    . ALA B 2  1187 ? 159.399 98.507  123.704 1.00 13.91  ? 1187 ALA B CB    1 
ATOM   19984 N  N     . ILE B 2  1188 ? 161.829 100.190 123.542 1.00 24.42  ? 1188 ILE B N     1 
ATOM   19985 C  CA    . ILE B 2  1188 ? 162.813 101.025 122.864 1.00 22.19  ? 1188 ILE B CA    1 
ATOM   19986 C  C     . ILE B 2  1188 ? 162.971 100.510 121.444 1.00 20.98  ? 1188 ILE B C     1 
ATOM   19987 O  O     . ILE B 2  1188 ? 163.392 99.367  121.236 1.00 25.35  ? 1188 ILE B O     1 
ATOM   19988 C  CB    . ILE B 2  1188 ? 164.162 101.023 123.591 1.00 22.58  ? 1188 ILE B CB    1 
ATOM   19989 C  CG1   . ILE B 2  1188 ? 163.967 101.284 125.076 1.00 24.34  ? 1188 ILE B CG1   1 
ATOM   19990 C  CG2   . ILE B 2  1188 ? 165.057 102.069 123.012 1.00 26.00  ? 1188 ILE B CG2   1 
ATOM   19991 C  CD1   . ILE B 2  1188 ? 165.235 101.230 125.856 1.00 24.64  ? 1188 ILE B CD1   1 
ATOM   19992 N  N     . TYR B 2  1189 ? 162.639 101.348 120.471 1.00 19.08  ? 1189 TYR B N     1 
ATOM   19993 C  CA    . TYR B 2  1189 ? 162.711 100.972 119.069 1.00 19.91  ? 1189 TYR B CA    1 
ATOM   19994 C  C     . TYR B 2  1189 ? 163.406 102.079 118.291 1.00 25.34  ? 1189 TYR B C     1 
ATOM   19995 O  O     . TYR B 2  1189 ? 163.124 103.260 118.505 1.00 30.83  ? 1189 TYR B O     1 
ATOM   19996 C  CB    . TYR B 2  1189 ? 161.316 100.704 118.508 1.00 14.56  ? 1189 TYR B CB    1 
ATOM   19997 C  CG    . TYR B 2  1189 ? 161.314 100.281 117.069 1.00 16.86  ? 1189 TYR B CG    1 
ATOM   19998 C  CD1   . TYR B 2  1189 ? 161.507 98.964  116.715 1.00 19.63  ? 1189 TYR B CD1   1 
ATOM   19999 C  CD2   . TYR B 2  1189 ? 161.144 101.206 116.063 1.00 20.37  ? 1189 TYR B CD2   1 
ATOM   20000 C  CE1   . TYR B 2  1189 ? 161.515 98.583  115.397 1.00 21.77  ? 1189 TYR B CE1   1 
ATOM   20001 C  CE2   . TYR B 2  1189 ? 161.148 100.837 114.752 1.00 21.72  ? 1189 TYR B CE2   1 
ATOM   20002 C  CZ    . TYR B 2  1189 ? 161.334 99.527  114.419 1.00 22.58  ? 1189 TYR B CZ    1 
ATOM   20003 O  OH    . TYR B 2  1189 ? 161.339 99.168  113.094 1.00 23.70  ? 1189 TYR B OH    1 
ATOM   20004 N  N     . ASN B 2  1190 ? 164.309 101.697 117.391 1.00 26.79  ? 1190 ASN B N     1 
ATOM   20005 C  CA    . ASN B 2  1190 ? 165.045 102.653 116.570 1.00 28.75  ? 1190 ASN B CA    1 
ATOM   20006 C  C     . ASN B 2  1190 ? 165.431 101.948 115.279 1.00 32.54  ? 1190 ASN B C     1 
ATOM   20007 O  O     . ASN B 2  1190 ? 166.234 101.016 115.302 1.00 35.12  ? 1190 ASN B O     1 
ATOM   20008 C  CB    . ASN B 2  1190 ? 166.278 103.172 117.308 1.00 26.93  ? 1190 ASN B CB    1 
ATOM   20009 C  CG    . ASN B 2  1190 ? 166.816 104.451 116.722 1.00 29.99  ? 1190 ASN B CG    1 
ATOM   20010 O  OD1   . ASN B 2  1190 ? 166.530 104.789 115.580 1.00 33.36  ? 1190 ASN B OD1   1 
ATOM   20011 N  ND2   . ASN B 2  1190 ? 167.584 105.185 117.512 1.00 27.39  ? 1190 ASN B ND2   1 
ATOM   20012 N  N     . ALA B 2  1191 ? 164.862 102.387 114.155 1.00 37.27  ? 1191 ALA B N     1 
ATOM   20013 C  CA    . ALA B 2  1191 ? 165.111 101.718 112.881 1.00 34.08  ? 1191 ALA B CA    1 
ATOM   20014 C  C     . ALA B 2  1191 ? 166.542 101.941 112.407 1.00 40.08  ? 1191 ALA B C     1 
ATOM   20015 O  O     . ALA B 2  1191 ? 167.276 100.984 112.143 1.00 44.14  ? 1191 ALA B O     1 
ATOM   20016 C  CB    . ALA B 2  1191 ? 164.110 102.204 111.835 1.00 37.13  ? 1191 ALA B CB    1 
ATOM   20017 N  N     . SER B 2  1192 ? 166.949 103.200 112.261 1.00 41.58  ? 1192 SER B N     1 
ATOM   20018 C  CA    . SER B 2  1192 ? 168.345 103.527 112.003 1.00 39.73  ? 1192 SER B CA    1 
ATOM   20019 C  C     . SER B 2  1192 ? 169.148 103.379 113.285 1.00 41.33  ? 1192 SER B C     1 
ATOM   20020 O  O     . SER B 2  1192 ? 168.710 103.799 114.357 1.00 44.05  ? 1192 SER B O     1 
ATOM   20021 C  CB    . SER B 2  1192 ? 168.480 104.955 111.481 1.00 40.95  ? 1192 SER B CB    1 
ATOM   20022 O  OG    . SER B 2  1192 ? 167.818 105.123 110.242 1.00 45.38  ? 1192 SER B OG    1 
ATOM   20023 N  N     . HIS B 2  1193 ? 170.347 102.808 113.166 1.00 46.11  ? 1193 HIS B N     1 
ATOM   20024 C  CA    . HIS B 2  1193 ? 171.087 102.406 114.356 1.00 46.73  ? 1193 HIS B CA    1 
ATOM   20025 C  C     . HIS B 2  1193 ? 170.195 101.451 115.131 1.00 49.14  ? 1193 HIS B C     1 
ATOM   20026 O  O     . HIS B 2  1193 ? 169.662 101.817 116.184 1.00 51.38  ? 1193 HIS B O     1 
ATOM   20027 C  CB    . HIS B 2  1193 ? 171.474 103.590 115.242 1.00 48.37  ? 1193 HIS B CB    1 
ATOM   20028 C  CG    . HIS B 2  1193 ? 172.268 103.203 116.451 1.00 51.03  ? 1193 HIS B CG    1 
ATOM   20029 N  ND1   . HIS B 2  1193 ? 171.726 102.482 117.494 1.00 47.84  ? 1193 HIS B ND1   1 
ATOM   20030 C  CD2   . HIS B 2  1193 ? 173.543 103.481 116.808 1.00 50.93  ? 1193 HIS B CD2   1 
ATOM   20031 C  CE1   . HIS B 2  1193 ? 172.647 102.296 118.421 1.00 49.39  ? 1193 HIS B CE1   1 
ATOM   20032 N  NE2   . HIS B 2  1193 ? 173.756 102.901 118.034 1.00 51.05  ? 1193 HIS B NE2   1 
ATOM   20033 N  N     . PRO B 2  1194 ? 170.026 100.223 114.663 1.00 46.00  ? 1194 PRO B N     1 
ATOM   20034 C  CA    . PRO B 2  1194 ? 168.882 99.429  115.097 1.00 40.99  ? 1194 PRO B CA    1 
ATOM   20035 C  C     . PRO B 2  1194 ? 168.907 98.962  116.543 1.00 41.29  ? 1194 PRO B C     1 
ATOM   20036 O  O     . PRO B 2  1194 ? 169.816 98.260  116.992 1.00 42.83  ? 1194 PRO B O     1 
ATOM   20037 C  CB    . PRO B 2  1194 ? 168.933 98.270  114.102 1.00 41.68  ? 1194 PRO B CB    1 
ATOM   20038 C  CG    . PRO B 2  1194 ? 170.452 98.005  113.974 1.00 44.73  ? 1194 PRO B CG    1 
ATOM   20039 C  CD    . PRO B 2  1194 ? 171.158 99.311  114.431 1.00 42.54  ? 1194 PRO B CD    1 
ATOM   20040 N  N     . ILE B 2  1195 ? 167.883 99.378  117.279 1.00 31.01  ? 1195 ILE B N     1 
ATOM   20041 C  CA    . ILE B 2  1195 ? 167.620 98.922  118.637 1.00 29.14  ? 1195 ILE B CA    1 
ATOM   20042 C  C     . ILE B 2  1195 ? 166.235 98.308  118.636 1.00 35.59  ? 1195 ILE B C     1 
ATOM   20043 O  O     . ILE B 2  1195 ? 165.323 98.828  117.983 1.00 37.61  ? 1195 ILE B O     1 
ATOM   20044 C  CB    . ILE B 2  1195 ? 167.706 100.064 119.665 1.00 29.73  ? 1195 ILE B CB    1 
ATOM   20045 C  CG1   . ILE B 2  1195 ? 169.051 100.782 119.556 1.00 34.35  ? 1195 ILE B CG1   1 
ATOM   20046 C  CG2   . ILE B 2  1195 ? 167.528 99.525  121.066 1.00 31.67  ? 1195 ILE B CG2   1 
ATOM   20047 C  CD1   . ILE B 2  1195 ? 169.150 102.011 120.413 1.00 33.81  ? 1195 ILE B CD1   1 
ATOM   20048 N  N     . TYR B 2  1196 ? 166.084 97.185  119.329 1.00 35.23  ? 1196 TYR B N     1 
ATOM   20049 C  CA    . TYR B 2  1196 ? 164.796 96.506  119.459 1.00 29.42  ? 1196 TYR B CA    1 
ATOM   20050 C  C     . TYR B 2  1196 ? 164.858 95.820  120.820 1.00 29.62  ? 1196 TYR B C     1 
ATOM   20051 O  O     . TYR B 2  1196 ? 165.333 94.690  120.930 1.00 34.98  ? 1196 TYR B O     1 
ATOM   20052 C  CB    . TYR B 2  1196 ? 164.596 95.524  118.315 1.00 27.57  ? 1196 TYR B CB    1 
ATOM   20053 C  CG    . TYR B 2  1196 ? 163.236 94.876  118.218 1.00 30.71  ? 1196 TYR B CG    1 
ATOM   20054 C  CD1   . TYR B 2  1196 ? 162.813 93.945  119.148 1.00 31.99  ? 1196 TYR B CD1   1 
ATOM   20055 C  CD2   . TYR B 2  1196 ? 162.393 95.173  117.162 1.00 32.07  ? 1196 TYR B CD2   1 
ATOM   20056 C  CE1   . TYR B 2  1196 ? 161.575 93.354  119.045 1.00 31.55  ? 1196 TYR B CE1   1 
ATOM   20057 C  CE2   . TYR B 2  1196 ? 161.159 94.585  117.049 1.00 31.70  ? 1196 TYR B CE2   1 
ATOM   20058 C  CZ    . TYR B 2  1196 ? 160.755 93.678  117.991 1.00 33.62  ? 1196 TYR B CZ    1 
ATOM   20059 O  OH    . TYR B 2  1196 ? 159.522 93.092  117.871 1.00 33.49  ? 1196 TYR B OH    1 
ATOM   20060 N  N     . LYS B 2  1197 ? 164.393 96.509  121.858 1.00 30.10  ? 1197 LYS B N     1 
ATOM   20061 C  CA    . LYS B 2  1197 ? 164.653 96.037  123.207 1.00 32.46  ? 1197 LYS B CA    1 
ATOM   20062 C  C     . LYS B 2  1197 ? 163.486 96.354  124.130 1.00 34.30  ? 1197 LYS B C     1 
ATOM   20063 O  O     . LYS B 2  1197 ? 162.765 97.333  123.939 1.00 35.10  ? 1197 LYS B O     1 
ATOM   20064 C  CB    . LYS B 2  1197 ? 165.933 96.659  123.779 1.00 32.77  ? 1197 LYS B CB    1 
ATOM   20065 C  CG    . LYS B 2  1197 ? 166.561 95.831  124.880 1.00 36.02  ? 1197 LYS B CG    1 
ATOM   20066 C  CD    . LYS B 2  1197 ? 167.091 96.684  126.013 1.00 35.27  ? 1197 LYS B CD    1 
ATOM   20067 C  CE    . LYS B 2  1197 ? 168.088 97.703  125.521 1.00 37.76  ? 1197 LYS B CE    1 
ATOM   20068 N  NZ    . LYS B 2  1197 ? 169.004 98.127  126.610 1.00 36.04  ? 1197 LYS B NZ    1 
ATOM   20069 N  N     . CYS B 2  1198 ? 163.334 95.518  125.150 1.00 34.96  ? 1198 CYS B N     1 
ATOM   20070 C  CA    . CYS B 2  1198 ? 162.403 95.739  126.242 1.00 33.33  ? 1198 CYS B CA    1 
ATOM   20071 C  C     . CYS B 2  1198 ? 163.159 95.567  127.550 1.00 37.54  ? 1198 CYS B C     1 
ATOM   20072 O  O     . CYS B 2  1198 ? 163.843 94.559  127.744 1.00 40.38  ? 1198 CYS B O     1 
ATOM   20073 C  CB    . CYS B 2  1198 ? 161.226 94.767  126.165 1.00 33.50  ? 1198 CYS B CB    1 
ATOM   20074 S  SG    . CYS B 2  1198 ? 160.120 94.827  127.568 1.00 44.08  ? 1198 CYS B SG    1 
ATOM   20075 N  N     . MET B 2  1199 ? 163.042 96.547  128.442 1.00 41.51  ? 1199 MET B N     1 
ATOM   20076 C  CA    . MET B 2  1199 ? 163.706 96.502  129.738 1.00 41.54  ? 1199 MET B CA    1 
ATOM   20077 C  C     . MET B 2  1199 ? 163.055 95.529  130.710 1.00 43.06  ? 1199 MET B C     1 
ATOM   20078 O  O     . MET B 2  1199 ? 163.567 95.352  131.819 1.00 44.16  ? 1199 MET B O     1 
ATOM   20079 C  CB    . MET B 2  1199 ? 163.746 97.901  130.358 1.00 42.65  ? 1199 MET B CB    1 
ATOM   20080 C  CG    . MET B 2  1199 ? 165.055 98.252  131.043 1.00 43.06  ? 1199 MET B CG    1 
ATOM   20081 S  SD    . MET B 2  1199 ? 166.529 98.155  130.015 1.00 57.40  ? 1199 MET B SD    1 
ATOM   20082 C  CE    . MET B 2  1199 ? 165.992 99.047  128.566 1.00 44.73  ? 1199 MET B CE    1 
ATOM   20083 N  N     . ASN B 2  1200 ? 161.952 94.892  130.324 1.00 44.24  ? 1200 ASN B N     1 
ATOM   20084 C  CA    . ASN B 2  1200 ? 161.243 93.959  131.190 1.00 45.14  ? 1200 ASN B CA    1 
ATOM   20085 C  C     . ASN B 2  1200 ? 161.312 92.513  130.734 1.00 44.51  ? 1200 ASN B C     1 
ATOM   20086 O  O     . ASN B 2  1200 ? 161.365 91.625  131.593 1.00 44.04  ? 1200 ASN B O     1 
ATOM   20087 C  CB    . ASN B 2  1200 ? 159.767 94.366  131.320 1.00 39.83  ? 1200 ASN B CB    1 
ATOM   20088 C  CG    . ASN B 2  1200 ? 159.594 95.750  131.913 1.00 45.85  ? 1200 ASN B CG    1 
ATOM   20089 O  OD1   . ASN B 2  1200 ? 159.610 95.917  133.130 1.00 47.32  ? 1200 ASN B OD1   1 
ATOM   20090 N  ND2   . ASN B 2  1200 ? 159.482 96.757  131.055 1.00 43.99  ? 1200 ASN B ND2   1 
ATOM   20091 N  N     . CYS B 2  1201 ? 161.331 92.241  129.431 1.00 39.06  ? 1201 CYS B N     1 
ATOM   20092 C  CA    . CYS B 2  1201 ? 161.405 90.883  128.909 1.00 38.49  ? 1201 CYS B CA    1 
ATOM   20093 C  C     . CYS B 2  1201 ? 162.751 90.583  128.271 1.00 39.74  ? 1201 CYS B C     1 
ATOM   20094 O  O     . CYS B 2  1201 ? 163.420 89.623  128.670 1.00 41.83  ? 1201 CYS B O     1 
ATOM   20095 C  CB    . CYS B 2  1201 ? 160.279 90.653  127.888 1.00 39.09  ? 1201 CYS B CB    1 
ATOM   20096 S  SG    . CYS B 2  1201 ? 158.656 91.246  128.393 1.00 45.14  ? 1201 CYS B SG    1 
ATOM   20097 N  N     . ASP B 2  1202 ? 163.143 91.360  127.261 1.00 47.50  ? 1202 ASP B N     1 
ATOM   20098 C  CA    . ASP B 2  1202 ? 164.501 91.441  126.727 1.00 48.16  ? 1202 ASP B CA    1 
ATOM   20099 C  C     . ASP B 2  1202 ? 164.927 90.231  125.898 1.00 48.12  ? 1202 ASP B C     1 
ATOM   20100 O  O     . ASP B 2  1202 ? 166.000 90.250  125.289 1.00 48.93  ? 1202 ASP B O     1 
ATOM   20101 C  CB    . ASP B 2  1202 ? 165.509 91.674  127.858 1.00 47.47  ? 1202 ASP B CB    1 
ATOM   20102 C  CG    . ASP B 2  1202 ? 166.797 92.306  127.365 1.00 48.31  ? 1202 ASP B CG    1 
ATOM   20103 O  OD1   . ASP B 2  1202 ? 166.845 93.546  127.234 1.00 45.87  ? 1202 ASP B OD1   1 
ATOM   20104 O  OD2   . ASP B 2  1202 ? 167.757 91.556  127.091 1.00 51.29  ? 1202 ASP B OD2   1 
ATOM   20105 N  N     . VAL B 2  1203 ? 164.119 89.176  125.857 1.00 41.08  ? 1203 VAL B N     1 
ATOM   20106 C  CA    . VAL B 2  1203 ? 164.234 88.187  124.788 1.00 40.79  ? 1203 VAL B CA    1 
ATOM   20107 C  C     . VAL B 2  1203 ? 162.908 87.898  124.119 1.00 39.28  ? 1203 VAL B C     1 
ATOM   20108 O  O     . VAL B 2  1203 ? 162.890 87.410  122.977 1.00 39.41  ? 1203 VAL B O     1 
ATOM   20109 C  CB    . VAL B 2  1203 ? 164.868 86.868  125.293 1.00 42.59  ? 1203 VAL B CB    1 
ATOM   20110 C  CG1   . VAL B 2  1203 ? 166.273 87.099  125.817 1.00 38.55  ? 1203 VAL B CG1   1 
ATOM   20111 C  CG2   . VAL B 2  1203 ? 163.991 86.222  126.352 1.00 42.94  ? 1203 VAL B CG2   1 
ATOM   20112 N  N     . GLN B 2  1204 ? 161.788 88.197  124.769 1.00 39.62  ? 1204 GLN B N     1 
ATOM   20113 C  CA    . GLN B 2  1204 ? 160.461 87.978  124.225 1.00 39.73  ? 1204 GLN B CA    1 
ATOM   20114 C  C     . GLN B 2  1204 ? 159.853 89.263  123.681 1.00 39.54  ? 1204 GLN B C     1 
ATOM   20115 O  O     . GLN B 2  1204 ? 158.637 89.334  123.492 1.00 40.08  ? 1204 GLN B O     1 
ATOM   20116 C  CB    . GLN B 2  1204 ? 159.559 87.381  125.303 1.00 36.51  ? 1204 GLN B CB    1 
ATOM   20117 C  CG    . GLN B 2  1204 ? 159.991 86.012  125.770 1.00 37.34  ? 1204 GLN B CG    1 
ATOM   20118 C  CD    . GLN B 2  1204 ? 159.805 84.950  124.716 1.00 41.05  ? 1204 GLN B CD    1 
ATOM   20119 O  OE1   . GLN B 2  1204 ? 158.844 84.980  123.952 1.00 43.21  ? 1204 GLN B OE1   1 
ATOM   20120 N  NE2   . GLN B 2  1204 ? 160.729 83.999  124.668 1.00 39.56  ? 1204 GLN B NE2   1 
ATOM   20121 N  N     . ALA B 2  1205 ? 160.680 90.272  123.420 1.00 32.75  ? 1205 ALA B N     1 
ATOM   20122 C  CA    . ALA B 2  1205 ? 160.179 91.584  123.044 1.00 28.63  ? 1205 ALA B CA    1 
ATOM   20123 C  C     . ALA B 2  1205 ? 159.403 91.510  121.739 1.00 29.96  ? 1205 ALA B C     1 
ATOM   20124 O  O     . ALA B 2  1205 ? 159.959 91.186  120.687 1.00 33.51  ? 1205 ALA B O     1 
ATOM   20125 C  CB    . ALA B 2  1205 ? 161.331 92.575  122.920 1.00 29.67  ? 1205 ALA B CB    1 
ATOM   20126 N  N     . ASP B 2  1206 ? 158.107 91.801  121.822 1.00 28.45  ? 1206 ASP B N     1 
ATOM   20127 C  CA    . ASP B 2  1206 ? 157.200 91.895  120.682 1.00 25.51  ? 1206 ASP B CA    1 
ATOM   20128 C  C     . ASP B 2  1206 ? 156.653 93.317  120.709 1.00 24.98  ? 1206 ASP B C     1 
ATOM   20129 O  O     . ASP B 2  1206 ? 155.737 93.617  121.474 1.00 28.04  ? 1206 ASP B O     1 
ATOM   20130 C  CB    . ASP B 2  1206 ? 156.096 90.857  120.777 1.00 26.39  ? 1206 ASP B CB    1 
ATOM   20131 C  CG    . ASP B 2  1206 ? 155.430 90.598  119.454 1.00 31.27  ? 1206 ASP B CG    1 
ATOM   20132 O  OD1   . ASP B 2  1206 ? 155.767 91.289  118.475 1.00 33.63  ? 1206 ASP B OD1   1 
ATOM   20133 O  OD2   . ASP B 2  1206 ? 154.565 89.707  119.394 1.00 30.74  ? 1206 ASP B OD2   1 
ATOM   20134 N  N     . ILE B 2  1207 ? 157.219 94.188  119.891 1.00 18.11  ? 1207 ILE B N     1 
ATOM   20135 C  CA    . ILE B 2  1207 ? 156.956 95.619  119.972 1.00 18.14  ? 1207 ILE B CA    1 
ATOM   20136 C  C     . ILE B 2  1207 ? 155.985 96.031  118.875 1.00 16.76  ? 1207 ILE B C     1 
ATOM   20137 O  O     . ILE B 2  1207 ? 156.178 95.697  117.702 1.00 16.99  ? 1207 ILE B O     1 
ATOM   20138 C  CB    . ILE B 2  1207 ? 158.266 96.416  119.883 1.00 18.29  ? 1207 ILE B CB    1 
ATOM   20139 C  CG1   . ILE B 2  1207 ? 159.201 96.010  121.019 1.00 18.41  ? 1207 ILE B CG1   1 
ATOM   20140 C  CG2   . ILE B 2  1207 ? 157.999 97.902  119.930 1.00 16.50  ? 1207 ILE B CG2   1 
ATOM   20141 C  CD1   . ILE B 2  1207 ? 160.591 96.543  120.875 1.00 20.61  ? 1207 ILE B CD1   1 
ATOM   20142 N  N     . GLY B 2  1208 ? 154.941 96.750  119.257 1.00 9.07   ? 1208 GLY B N     1 
ATOM   20143 C  CA    . GLY B 2  1208 ? 154.003 97.329  118.308 1.00 5.09   ? 1208 GLY B CA    1 
ATOM   20144 C  C     . GLY B 2  1208 ? 153.991 98.838  118.442 1.00 4.97   ? 1208 GLY B C     1 
ATOM   20145 O  O     . GLY B 2  1208 ? 154.186 99.365  119.532 1.00 9.80   ? 1208 GLY B O     1 
ATOM   20146 N  N     . MET B 2  1209 ? 153.781 99.526  117.326 1.00 5.09   ? 1209 MET B N     1 
ATOM   20147 C  CA    . MET B 2  1209 ? 153.796 100.982 117.313 1.00 5.67   ? 1209 MET B CA    1 
ATOM   20148 C  C     . MET B 2  1209 ? 152.374 101.523 117.414 1.00 11.51  ? 1209 MET B C     1 
ATOM   20149 O  O     . MET B 2  1209 ? 151.508 101.175 116.608 1.00 17.64  ? 1209 MET B O     1 
ATOM   20150 C  CB    . MET B 2  1209 ? 154.501 101.507 116.063 1.00 10.30  ? 1209 MET B CB    1 
ATOM   20151 C  CG    . MET B 2  1209 ? 153.807 101.246 114.756 1.00 11.20  ? 1209 MET B CG    1 
ATOM   20152 S  SD    . MET B 2  1209 ? 154.481 102.220 113.410 1.00 29.48  ? 1209 MET B SD    1 
ATOM   20153 C  CE    . MET B 2  1209 ? 153.093 102.220 112.282 1.00 9.70   ? 1209 MET B CE    1 
ATOM   20154 N  N     . VAL B 2  1210 ? 152.133 102.369 118.407 1.00 4.61   ? 1210 VAL B N     1 
ATOM   20155 C  CA    . VAL B 2  1210 ? 150.820 102.953 118.625 1.00 6.02   ? 1210 VAL B CA    1 
ATOM   20156 C  C     . VAL B 2  1210 ? 150.937 104.457 118.445 1.00 7.53   ? 1210 VAL B C     1 
ATOM   20157 O  O     . VAL B 2  1210 ? 151.961 105.057 118.781 1.00 17.32  ? 1210 VAL B O     1 
ATOM   20158 C  CB    . VAL B 2  1210 ? 150.232 102.583 120.008 1.00 1.47   ? 1210 VAL B CB    1 
ATOM   20159 C  CG1   . VAL B 2  1210 ? 150.765 101.252 120.481 1.00 3.28   ? 1210 VAL B CG1   1 
ATOM   20160 C  CG2   . VAL B 2  1210 ? 150.451 103.661 121.030 1.00 7.37   ? 1210 VAL B CG2   1 
ATOM   20161 N  N     . ASP B 2  1211 ? 149.906 105.054 117.865 1.00 8.67   ? 1211 ASP B N     1 
ATOM   20162 C  CA    . ASP B 2  1211 ? 149.872 106.494 117.684 1.00 10.96  ? 1211 ASP B CA    1 
ATOM   20163 C  C     . ASP B 2  1211 ? 149.458 107.169 118.976 1.00 2.79   ? 1211 ASP B C     1 
ATOM   20164 O  O     . ASP B 2  1211 ? 148.385 106.894 119.514 1.00 16.10  ? 1211 ASP B O     1 
ATOM   20165 C  CB    . ASP B 2  1211 ? 148.899 106.858 116.573 1.00 3.35   ? 1211 ASP B CB    1 
ATOM   20166 C  CG    . ASP B 2  1211 ? 149.477 106.636 115.207 1.00 12.51  ? 1211 ASP B CG    1 
ATOM   20167 O  OD1   . ASP B 2  1211 ? 150.604 107.102 114.958 1.00 20.85  ? 1211 ASP B OD1   1 
ATOM   20168 O  OD2   . ASP B 2  1211 ? 148.825 105.965 114.391 1.00 11.76  ? 1211 ASP B OD2   1 
ATOM   20169 N  N     . SER B 2  1212 ? 150.300 108.066 119.469 1.00 5.35   ? 1212 SER B N     1 
ATOM   20170 C  CA    . SER B 2  1212 ? 150.028 108.770 120.706 1.00 3.33   ? 1212 SER B CA    1 
ATOM   20171 C  C     . SER B 2  1212 ? 150.350 110.237 120.487 1.00 5.38   ? 1212 SER B C     1 
ATOM   20172 O  O     . SER B 2  1212 ? 150.510 110.697 119.357 1.00 8.24   ? 1212 SER B O     1 
ATOM   20173 C  CB    . SER B 2  1212 ? 150.824 108.161 121.864 1.00 5.30   ? 1212 SER B CB    1 
ATOM   20174 O  OG    . SER B 2  1212 ? 150.512 108.794 123.086 1.00 7.59   ? 1212 SER B OG    1 
ATOM   20175 N  N     . ARG B 2  1213 ? 150.403 110.987 121.573 1.00 7.05   ? 1213 ARG B N     1 
ATOM   20176 C  CA    . ARG B 2  1213 ? 150.857 112.362 121.533 1.00 5.40   ? 1213 ARG B CA    1 
ATOM   20177 C  C     . ARG B 2  1213 ? 151.642 112.641 122.798 1.00 5.19   ? 1213 ARG B C     1 
ATOM   20178 O  O     . ARG B 2  1213 ? 151.462 111.972 123.812 1.00 10.43  ? 1213 ARG B O     1 
ATOM   20179 C  CB    . ARG B 2  1213 ? 149.699 113.344 121.346 1.00 1.63   ? 1213 ARG B CB    1 
ATOM   20180 C  CG    . ARG B 2  1213 ? 148.468 113.001 122.078 1.00 4.27   ? 1213 ARG B CG    1 
ATOM   20181 C  CD    . ARG B 2  1213 ? 147.298 113.823 121.604 1.00 0.82   ? 1213 ARG B CD    1 
ATOM   20182 N  NE    . ARG B 2  1213 ? 147.494 115.222 121.942 1.00 6.56   ? 1213 ARG B NE    1 
ATOM   20183 C  CZ    . ARG B 2  1213 ? 146.537 116.028 122.371 1.00 10.88  ? 1213 ARG B CZ    1 
ATOM   20184 N  NH1   . ARG B 2  1213 ? 145.324 115.579 122.621 1.00 9.70   ? 1213 ARG B NH1   1 
ATOM   20185 N  NH2   . ARG B 2  1213 ? 146.819 117.303 122.607 1.00 3.06   ? 1213 ARG B NH2   1 
ATOM   20186 N  N     . ARG B 2  1214 ? 152.539 113.621 122.716 1.00 8.91   ? 1214 ARG B N     1 
ATOM   20187 C  CA    . ARG B 2  1214 ? 153.613 113.726 123.696 1.00 6.78   ? 1214 ARG B CA    1 
ATOM   20188 C  C     . ARG B 2  1214 ? 153.092 114.068 125.080 1.00 5.12   ? 1214 ARG B C     1 
ATOM   20189 O  O     . ARG B 2  1214 ? 153.661 113.637 126.083 1.00 12.56  ? 1214 ARG B O     1 
ATOM   20190 C  CB    . ARG B 2  1214 ? 154.631 114.765 123.253 1.00 11.42  ? 1214 ARG B CB    1 
ATOM   20191 C  CG    . ARG B 2  1214 ? 155.918 114.682 124.018 1.00 13.22  ? 1214 ARG B CG    1 
ATOM   20192 C  CD    . ARG B 2  1214 ? 156.933 115.651 123.499 1.00 16.55  ? 1214 ARG B CD    1 
ATOM   20193 N  NE    . ARG B 2  1214 ? 158.167 115.599 124.269 1.00 22.61  ? 1214 ARG B NE    1 
ATOM   20194 C  CZ    . ARG B 2  1214 ? 159.202 114.827 123.968 1.00 26.43  ? 1214 ARG B CZ    1 
ATOM   20195 N  NH1   . ARG B 2  1214 ? 159.187 114.034 122.911 1.00 15.36  ? 1214 ARG B NH1   1 
ATOM   20196 N  NH2   . ARG B 2  1214 ? 160.281 114.858 124.743 1.00 27.01  ? 1214 ARG B NH2   1 
ATOM   20197 N  N     . SER B 2  1215 ? 152.038 114.865 125.164 1.00 3.17   ? 1215 SER B N     1 
ATOM   20198 C  CA    . SER B 2  1215 ? 151.502 115.218 126.468 1.00 0.76   ? 1215 SER B CA    1 
ATOM   20199 C  C     . SER B 2  1215 ? 150.821 114.040 127.145 1.00 7.87   ? 1215 SER B C     1 
ATOM   20200 O  O     . SER B 2  1215 ? 150.666 114.048 128.367 1.00 15.62  ? 1215 SER B O     1 
ATOM   20201 C  CB    . SER B 2  1215 ? 150.545 116.395 126.326 1.00 5.35   ? 1215 SER B CB    1 
ATOM   20202 O  OG    . SER B 2  1215 ? 149.569 116.116 125.350 1.00 13.86  ? 1215 SER B OG    1 
ATOM   20203 N  N     . SER B 2  1216 ? 150.397 113.039 126.381 1.00 9.14   ? 1216 SER B N     1 
ATOM   20204 C  CA    . SER B 2  1216 ? 149.848 111.827 126.969 1.00 5.39   ? 1216 SER B CA    1 
ATOM   20205 C  C     . SER B 2  1216 ? 150.939 110.948 127.555 1.00 3.99   ? 1216 SER B C     1 
ATOM   20206 O  O     . SER B 2  1216 ? 150.761 110.366 128.626 1.00 11.22  ? 1216 SER B O     1 
ATOM   20207 C  CB    . SER B 2  1216 ? 149.065 111.053 125.924 1.00 5.75   ? 1216 SER B CB    1 
ATOM   20208 O  OG    . SER B 2  1216 ? 148.580 109.848 126.471 1.00 15.29  ? 1216 SER B OG    1 
ATOM   20209 N  N     . ILE B 2  1217 ? 152.061 110.828 126.849 1.00 6.87   ? 1217 ILE B N     1 
ATOM   20210 C  CA    . ILE B 2  1217 ? 153.205 110.080 127.348 1.00 1.57   ? 1217 ILE B CA    1 
ATOM   20211 C  C     . ILE B 2  1217 ? 153.812 110.765 128.564 1.00 6.51   ? 1217 ILE B C     1 
ATOM   20212 O  O     . ILE B 2  1217 ? 154.288 110.104 129.490 1.00 12.41  ? 1217 ILE B O     1 
ATOM   20213 C  CB    . ILE B 2  1217 ? 154.228 109.901 126.216 1.00 1.99   ? 1217 ILE B CB    1 
ATOM   20214 C  CG1   . ILE B 2  1217 ? 153.714 108.892 125.202 1.00 2.22   ? 1217 ILE B CG1   1 
ATOM   20215 C  CG2   . ILE B 2  1217 ? 155.575 109.491 126.751 1.00 12.14  ? 1217 ILE B CG2   1 
ATOM   20216 C  CD1   . ILE B 2  1217 ? 154.664 108.641 124.109 1.00 8.04   ? 1217 ILE B CD1   1 
ATOM   20217 N  N     . VAL B 2  1218 ? 153.817 112.094 128.579 1.00 2.26   ? 1218 VAL B N     1 
ATOM   20218 C  CA    . VAL B 2  1218 ? 154.276 112.816 129.760 1.00 5.35   ? 1218 VAL B CA    1 
ATOM   20219 C  C     . VAL B 2  1218 ? 153.342 112.552 130.933 1.00 11.68  ? 1218 VAL B C     1 
ATOM   20220 O  O     . VAL B 2  1218 ? 153.779 112.406 132.077 1.00 19.43  ? 1218 VAL B O     1 
ATOM   20221 C  CB    . VAL B 2  1218 ? 154.403 114.317 129.442 1.00 6.87   ? 1218 VAL B CB    1 
ATOM   20222 C  CG1   . VAL B 2  1218 ? 154.545 115.134 130.696 1.00 8.06   ? 1218 VAL B CG1   1 
ATOM   20223 C  CG2   . VAL B 2  1218 ? 155.576 114.545 128.531 1.00 11.50  ? 1218 VAL B CG2   1 
ATOM   20224 N  N     . PHE B 2  1219 ? 152.046 112.459 130.657 1.00 11.22  ? 1219 PHE B N     1 
ATOM   20225 C  CA    . PHE B 2  1219 ? 151.057 112.147 131.681 1.00 3.63   ? 1219 PHE B CA    1 
ATOM   20226 C  C     . PHE B 2  1219 ? 151.287 110.763 132.280 1.00 8.04   ? 1219 PHE B C     1 
ATOM   20227 O  O     . PHE B 2  1219 ? 151.086 110.559 133.478 1.00 16.10  ? 1219 PHE B O     1 
ATOM   20228 C  CB    . PHE B 2  1219 ? 149.668 112.271 131.052 1.00 8.24   ? 1219 PHE B CB    1 
ATOM   20229 C  CG    . PHE B 2  1219 ? 148.541 111.781 131.905 1.00 14.89  ? 1219 PHE B CG    1 
ATOM   20230 C  CD1   . PHE B 2  1219 ? 148.302 112.322 133.144 1.00 11.83  ? 1219 PHE B CD1   1 
ATOM   20231 C  CD2   . PHE B 2  1219 ? 147.691 110.800 131.438 1.00 9.92   ? 1219 PHE B CD2   1 
ATOM   20232 C  CE1   . PHE B 2  1219 ? 147.258 111.877 133.908 1.00 9.62   ? 1219 PHE B CE1   1 
ATOM   20233 C  CE2   . PHE B 2  1219 ? 146.651 110.360 132.200 1.00 8.54   ? 1219 PHE B CE2   1 
ATOM   20234 C  CZ    . PHE B 2  1219 ? 146.433 110.902 133.433 1.00 9.38   ? 1219 PHE B CZ    1 
ATOM   20235 N  N     . GLN B 2  1220 ? 151.700 109.796 131.464 1.00 9.08   ? 1220 GLN B N     1 
ATOM   20236 C  CA    . GLN B 2  1220 ? 151.905 108.445 131.969 1.00 4.52   ? 1220 GLN B CA    1 
ATOM   20237 C  C     . GLN B 2  1220 ? 153.199 108.312 132.759 1.00 15.01  ? 1220 GLN B C     1 
ATOM   20238 O  O     . GLN B 2  1220 ? 153.256 107.527 133.707 1.00 19.20  ? 1220 GLN B O     1 
ATOM   20239 C  CB    . GLN B 2  1220 ? 151.878 107.451 130.821 1.00 3.23   ? 1220 GLN B CB    1 
ATOM   20240 C  CG    . GLN B 2  1220 ? 150.612 107.520 130.017 1.00 6.72   ? 1220 GLN B CG    1 
ATOM   20241 C  CD    . GLN B 2  1220 ? 150.658 106.662 128.793 1.00 8.59   ? 1220 GLN B CD    1 
ATOM   20242 O  OE1   . GLN B 2  1220 ? 151.290 105.616 128.785 1.00 12.90  ? 1220 GLN B OE1   1 
ATOM   20243 N  NE2   . GLN B 2  1220 ? 150.017 107.118 127.730 1.00 9.66   ? 1220 GLN B NE2   1 
ATOM   20244 N  N     . HIS B 2  1221 ? 154.247 109.050 132.388 1.00 15.48  ? 1221 HIS B N     1 
ATOM   20245 C  CA    . HIS B 2  1221 ? 155.446 109.088 133.216 1.00 11.78  ? 1221 HIS B CA    1 
ATOM   20246 C  C     . HIS B 2  1221 ? 155.177 109.751 134.557 1.00 11.75  ? 1221 HIS B C     1 
ATOM   20247 O  O     . HIS B 2  1221 ? 155.786 109.380 135.563 1.00 16.30  ? 1221 HIS B O     1 
ATOM   20248 C  CB    . HIS B 2  1221 ? 156.577 109.837 132.521 1.00 11.45  ? 1221 HIS B CB    1 
ATOM   20249 C  CG    . HIS B 2  1221 ? 157.173 109.119 131.355 1.00 11.14  ? 1221 HIS B CG    1 
ATOM   20250 N  ND1   . HIS B 2  1221 ? 157.409 107.765 131.351 1.00 13.01  ? 1221 HIS B ND1   1 
ATOM   20251 C  CD2   . HIS B 2  1221 ? 157.638 109.582 130.173 1.00 13.37  ? 1221 HIS B CD2   1 
ATOM   20252 C  CE1   . HIS B 2  1221 ? 157.952 107.417 130.200 1.00 16.45  ? 1221 HIS B CE1   1 
ATOM   20253 N  NE2   . HIS B 2  1221 ? 158.105 108.504 129.469 1.00 18.81  ? 1221 HIS B NE2   1 
ATOM   20254 N  N     . GLU B 2  1222 ? 154.308 110.759 134.589 1.00 8.07   ? 1222 GLU B N     1 
ATOM   20255 C  CA    . GLU B 2  1222 ? 153.972 111.395 135.855 1.00 9.73   ? 1222 GLU B CA    1 
ATOM   20256 C  C     . GLU B 2  1222 ? 153.147 110.481 136.747 1.00 15.31  ? 1222 GLU B C     1 
ATOM   20257 O  O     . GLU B 2  1222 ? 153.231 110.576 137.972 1.00 21.01  ? 1222 GLU B O     1 
ATOM   20258 C  CB    . GLU B 2  1222 ? 153.228 112.696 135.610 1.00 10.30  ? 1222 GLU B CB    1 
ATOM   20259 C  CG    . GLU B 2  1222 ? 154.084 113.770 135.018 1.00 15.69  ? 1222 GLU B CG    1 
ATOM   20260 C  CD    . GLU B 2  1222 ? 153.275 114.940 134.536 1.00 20.34  ? 1222 GLU B CD    1 
ATOM   20261 O  OE1   . GLU B 2  1222 ? 152.036 114.871 134.613 1.00 26.19  ? 1222 GLU B OE1   1 
ATOM   20262 O  OE2   . GLU B 2  1222 ? 153.876 115.937 134.096 1.00 17.69  ? 1222 GLU B OE2   1 
ATOM   20263 N  N     . MET B 2  1223 ? 152.337 109.606 136.163 1.00 16.72  ? 1223 MET B N     1 
ATOM   20264 C  CA    . MET B 2  1223 ? 151.627 108.627 136.972 1.00 17.94  ? 1223 MET B CA    1 
ATOM   20265 C  C     . MET B 2  1223 ? 152.585 107.585 137.537 1.00 17.58  ? 1223 MET B C     1 
ATOM   20266 O  O     . MET B 2  1223 ? 152.384 107.103 138.652 1.00 22.92  ? 1223 MET B O     1 
ATOM   20267 C  CB    . MET B 2  1223 ? 150.516 107.974 136.149 1.00 14.09  ? 1223 MET B CB    1 
ATOM   20268 C  CG    . MET B 2  1223 ? 149.170 108.675 136.283 1.00 15.71  ? 1223 MET B CG    1 
ATOM   20269 S  SD    . MET B 2  1223 ? 147.819 108.032 135.268 1.00 34.34  ? 1223 MET B SD    1 
ATOM   20270 C  CE    . MET B 2  1223 ? 148.624 107.596 133.741 1.00 13.85  ? 1223 MET B CE    1 
ATOM   20271 N  N     . ARG B 2  1224 ? 153.635 107.235 136.789 1.00 14.88  ? 1224 ARG B N     1 
ATOM   20272 C  CA    . ARG B 2  1224 ? 154.611 106.265 137.273 1.00 12.97  ? 1224 ARG B CA    1 
ATOM   20273 C  C     . ARG B 2  1224 ? 155.554 106.862 138.307 1.00 20.75  ? 1224 ARG B C     1 
ATOM   20274 O  O     . ARG B 2  1224 ? 156.042 106.143 139.184 1.00 20.63  ? 1224 ARG B O     1 
ATOM   20275 C  CB    . ARG B 2  1224 ? 155.413 105.703 136.107 1.00 13.97  ? 1224 ARG B CB    1 
ATOM   20276 C  CG    . ARG B 2  1224 ? 154.588 104.925 135.131 1.00 17.23  ? 1224 ARG B CG    1 
ATOM   20277 C  CD    . ARG B 2  1224 ? 155.440 104.234 134.103 1.00 15.86  ? 1224 ARG B CD    1 
ATOM   20278 N  NE    . ARG B 2  1224 ? 154.641 103.746 132.988 1.00 20.82  ? 1224 ARG B NE    1 
ATOM   20279 C  CZ    . ARG B 2  1224 ? 154.602 104.312 131.789 1.00 21.78  ? 1224 ARG B CZ    1 
ATOM   20280 N  NH1   . ARG B 2  1224 ? 155.327 105.379 131.505 1.00 17.26  ? 1224 ARG B NH1   1 
ATOM   20281 N  NH2   . ARG B 2  1224 ? 153.822 103.789 130.850 1.00 19.24  ? 1224 ARG B NH2   1 
ATOM   20282 N  N     . ALA B 2  1225 ? 155.841 108.160 138.215 1.00 22.04  ? 1225 ALA B N     1 
ATOM   20283 C  CA    . ALA B 2  1225 ? 156.694 108.801 139.204 1.00 20.62  ? 1225 ALA B CA    1 
ATOM   20284 C  C     . ALA B 2  1225 ? 156.064 108.794 140.584 1.00 26.33  ? 1225 ALA B C     1 
ATOM   20285 O  O     . ALA B 2  1225 ? 156.787 108.799 141.584 1.00 33.52  ? 1225 ALA B O     1 
ATOM   20286 C  CB    . ALA B 2  1225 ? 157.009 110.233 138.783 1.00 21.71  ? 1225 ALA B CB    1 
ATOM   20287 N  N     . ALA B 2  1226 ? 154.736 108.792 140.663 1.00 18.53  ? 1226 ALA B N     1 
ATOM   20288 C  CA    . ALA B 2  1226 ? 154.024 108.636 141.919 1.00 15.69  ? 1226 ALA B CA    1 
ATOM   20289 C  C     . ALA B 2  1226 ? 153.761 107.176 142.246 1.00 20.01  ? 1226 ALA B C     1 
ATOM   20290 O  O     . ALA B 2  1226 ? 152.837 106.874 143.004 1.00 25.15  ? 1226 ALA B O     1 
ATOM   20291 C  CB    . ALA B 2  1226 ? 152.717 109.417 141.887 1.00 19.47  ? 1226 ALA B CB    1 
ATOM   20292 N  N     . ASN B 2  1227 ? 154.548 106.269 141.671 1.00 17.61  ? 1227 ASN B N     1 
ATOM   20293 C  CA    . ASN B 2  1227 ? 154.534 104.841 141.964 1.00 22.05  ? 1227 ASN B CA    1 
ATOM   20294 C  C     . ASN B 2  1227 ? 153.223 104.166 141.601 1.00 23.88  ? 1227 ASN B C     1 
ATOM   20295 O  O     . ASN B 2  1227 ? 152.788 103.246 142.296 1.00 29.11  ? 1227 ASN B O     1 
ATOM   20296 C  CB    . ASN B 2  1227 ? 154.875 104.569 143.432 1.00 23.23  ? 1227 ASN B CB    1 
ATOM   20297 C  CG    . ASN B 2  1227 ? 156.094 105.328 143.891 1.00 25.86  ? 1227 ASN B CG    1 
ATOM   20298 O  OD1   . ASN B 2  1227 ? 156.025 106.147 144.801 1.00 26.09  ? 1227 ASN B OD1   1 
ATOM   20299 N  ND2   . ASN B 2  1227 ? 157.219 105.065 143.259 1.00 24.46  ? 1227 ASN B ND2   1 
ATOM   20300 N  N     . VAL B 2  1228 ? 152.589 104.595 140.517 1.00 24.16  ? 1228 VAL B N     1 
ATOM   20301 C  CA    . VAL B 2  1228 ? 151.439 103.908 139.944 1.00 20.55  ? 1228 VAL B CA    1 
ATOM   20302 C  C     . VAL B 2  1228 ? 151.896 103.275 138.640 1.00 20.34  ? 1228 VAL B C     1 
ATOM   20303 O  O     . VAL B 2  1228 ? 152.372 103.972 137.741 1.00 23.75  ? 1228 VAL B O     1 
ATOM   20304 C  CB    . VAL B 2  1228 ? 150.268 104.873 139.707 1.00 16.63  ? 1228 VAL B CB    1 
ATOM   20305 C  CG1   . VAL B 2  1228 ? 149.123 104.155 139.032 1.00 18.91  ? 1228 VAL B CG1   1 
ATOM   20306 C  CG2   . VAL B 2  1228 ? 149.823 105.504 141.001 1.00 20.72  ? 1228 VAL B CG2   1 
ATOM   20307 N  N     . ASN B 2  1229 ? 151.761 101.963 138.524 1.00 19.12  ? 1229 ASN B N     1 
ATOM   20308 C  CA    . ASN B 2  1229 ? 152.207 101.269 137.327 1.00 18.15  ? 1229 ASN B CA    1 
ATOM   20309 C  C     . ASN B 2  1229 ? 151.093 101.239 136.290 1.00 22.07  ? 1229 ASN B C     1 
ATOM   20310 O  O     . ASN B 2  1229 ? 149.969 100.834 136.591 1.00 31.00  ? 1229 ASN B O     1 
ATOM   20311 C  CB    . ASN B 2  1229 ? 152.650 99.848  137.654 1.00 22.02  ? 1229 ASN B CB    1 
ATOM   20312 C  CG    . ASN B 2  1229 ? 153.625 99.308  136.645 1.00 27.33  ? 1229 ASN B CG    1 
ATOM   20313 O  OD1   . ASN B 2  1229 ? 154.117 100.041 135.794 1.00 31.55  ? 1229 ASN B OD1   1 
ATOM   20314 N  ND2   . ASN B 2  1229 ? 153.893 98.019  136.713 1.00 29.51  ? 1229 ASN B ND2   1 
ATOM   20315 N  N     . ILE B 2  1230 ? 151.414 101.658 135.069 1.00 22.13  ? 1230 ILE B N     1 
ATOM   20316 C  CA    . ILE B 2  1230 ? 150.472 101.691 133.956 1.00 15.85  ? 1230 ILE B CA    1 
ATOM   20317 C  C     . ILE B 2  1230 ? 150.820 100.554 133.011 1.00 15.83  ? 1230 ILE B C     1 
ATOM   20318 O  O     . ILE B 2  1230 ? 151.949 100.473 132.518 1.00 27.60  ? 1230 ILE B O     1 
ATOM   20319 C  CB    . ILE B 2  1230 ? 150.511 103.038 133.223 1.00 16.44  ? 1230 ILE B CB    1 
ATOM   20320 C  CG1   . ILE B 2  1230 ? 150.286 104.193 134.193 1.00 16.63  ? 1230 ILE B CG1   1 
ATOM   20321 C  CG2   . ILE B 2  1230 ? 149.492 103.068 132.107 1.00 22.24  ? 1230 ILE B CG2   1 
ATOM   20322 C  CD1   . ILE B 2  1230 ? 148.974 104.135 134.897 1.00 21.67  ? 1230 ILE B CD1   1 
ATOM   20323 N  N     . THR B 2  1231 ? 149.860 99.678  132.757 1.00 9.19   ? 1231 THR B N     1 
ATOM   20324 C  CA    . THR B 2  1231 ? 150.034 98.548  131.859 1.00 9.17   ? 1231 THR B CA    1 
ATOM   20325 C  C     . THR B 2  1231 ? 149.100 98.726  130.675 1.00 19.12  ? 1231 THR B C     1 
ATOM   20326 O  O     . THR B 2  1231 ? 147.884 98.809  130.855 1.00 23.10  ? 1231 THR B O     1 
ATOM   20327 C  CB    . THR B 2  1231 ? 149.721 97.230  132.567 1.00 15.64  ? 1231 THR B CB    1 
ATOM   20328 O  OG1   . THR B 2  1231 ? 150.489 97.136  133.768 1.00 28.80  ? 1231 THR B OG1   1 
ATOM   20329 C  CG2   . THR B 2  1231 ? 150.050 96.060  131.681 1.00 15.44  ? 1231 THR B CG2   1 
ATOM   20330 N  N     . SER B 2  1232 ? 149.656 98.767  129.474 1.00 14.75  ? 1232 SER B N     1 
ATOM   20331 C  CA    . SER B 2  1232 ? 148.870 98.930  128.261 1.00 6.08   ? 1232 SER B CA    1 
ATOM   20332 C  C     . SER B 2  1232 ? 148.623 97.564  127.647 1.00 7.22   ? 1232 SER B C     1 
ATOM   20333 O  O     . SER B 2  1232 ? 149.565 96.877  127.254 1.00 20.48  ? 1232 SER B O     1 
ATOM   20334 C  CB    . SER B 2  1232 ? 149.570 99.842  127.261 1.00 8.55   ? 1232 SER B CB    1 
ATOM   20335 O  OG    . SER B 2  1232 ? 149.696 101.147 127.777 1.00 10.67  ? 1232 SER B OG    1 
ATOM   20336 N  N     . VAL B 2  1233 ? 147.361 97.172  127.580 1.00 7.16   ? 1233 VAL B N     1 
ATOM   20337 C  CA    . VAL B 2  1233 ? 146.969 95.965  126.869 1.00 9.14   ? 1233 VAL B CA    1 
ATOM   20338 C  C     . VAL B 2  1233 ? 146.720 96.338  125.416 1.00 7.45   ? 1233 VAL B C     1 
ATOM   20339 O  O     . VAL B 2  1233 ? 145.852 97.158  125.117 1.00 13.18  ? 1233 VAL B O     1 
ATOM   20340 C  CB    . VAL B 2  1233 ? 145.724 95.334  127.502 1.00 5.14   ? 1233 VAL B CB    1 
ATOM   20341 C  CG1   . VAL B 2  1233 ? 145.509 93.954  126.968 1.00 6.58   ? 1233 VAL B CG1   1 
ATOM   20342 C  CG2   . VAL B 2  1233 ? 145.860 95.308  129.006 1.00 5.49   ? 1233 VAL B CG2   1 
ATOM   20343 N  N     . LEU B 2  1234 ? 147.496 95.757  124.514 1.00 8.44   ? 1234 LEU B N     1 
ATOM   20344 C  CA    . LEU B 2  1234 ? 147.311 96.012  123.100 1.00 7.73   ? 1234 LEU B CA    1 
ATOM   20345 C  C     . LEU B 2  1234 ? 146.158 95.177  122.564 1.00 10.43  ? 1234 LEU B C     1 
ATOM   20346 O  O     . LEU B 2  1234 ? 145.765 94.167  123.145 1.00 17.49  ? 1234 LEU B O     1 
ATOM   20347 C  CB    . LEU B 2  1234 ? 148.592 95.712  122.326 1.00 11.02  ? 1234 LEU B CB    1 
ATOM   20348 C  CG    . LEU B 2  1234 ? 149.786 96.609  122.653 1.00 9.74   ? 1234 LEU B CG    1 
ATOM   20349 C  CD1   . LEU B 2  1234 ? 150.940 96.319  121.730 1.00 7.94   ? 1234 LEU B CD1   1 
ATOM   20350 C  CD2   . LEU B 2  1234 ? 149.406 98.079  122.595 1.00 7.13   ? 1234 LEU B CD2   1 
ATOM   20351 N  N     . SER B 2  1235 ? 145.608 95.623  121.454 1.00 10.79  ? 1235 SER B N     1 
ATOM   20352 C  CA    . SER B 2  1235 ? 144.527 94.891  120.817 1.00 8.41   ? 1235 SER B CA    1 
ATOM   20353 C  C     . SER B 2  1235 ? 145.048 93.558  120.300 1.00 14.74  ? 1235 SER B C     1 
ATOM   20354 O  O     . SER B 2  1235 ? 146.150 93.503  119.749 1.00 17.24  ? 1235 SER B O     1 
ATOM   20355 C  CB    . SER B 2  1235 ? 143.941 95.705  119.672 1.00 9.18   ? 1235 SER B CB    1 
ATOM   20356 O  OG    . SER B 2  1235 ? 142.857 96.489  120.115 1.00 15.05  ? 1235 SER B OG    1 
ATOM   20357 N  N     . PRO B 2  1236 ? 144.309 92.471  120.465 1.00 15.94  ? 1236 PRO B N     1 
ATOM   20358 C  CA    . PRO B 2  1236 ? 144.782 91.182  119.968 1.00 16.16  ? 1236 PRO B CA    1 
ATOM   20359 C  C     . PRO B 2  1236 ? 144.820 91.131  118.450 1.00 13.03  ? 1236 PRO B C     1 
ATOM   20360 O  O     . PRO B 2  1236 ? 144.107 91.846  117.746 1.00 18.34  ? 1236 PRO B O     1 
ATOM   20361 C  CB    . PRO B 2  1236 ? 143.761 90.192  120.531 1.00 13.20  ? 1236 PRO B CB    1 
ATOM   20362 C  CG    . PRO B 2  1236 ? 142.571 90.987  120.776 1.00 14.81  ? 1236 PRO B CG    1 
ATOM   20363 C  CD    . PRO B 2  1236 ? 143.022 92.347  121.160 1.00 12.21  ? 1236 PRO B CD    1 
ATOM   20364 N  N     . ARG B 2  1237 ? 145.708 90.280  117.953 1.00 12.97  ? 1237 ARG B N     1 
ATOM   20365 C  CA    . ARG B 2  1237 ? 145.747 89.966  116.537 1.00 10.16  ? 1237 ARG B CA    1 
ATOM   20366 C  C     . ARG B 2  1237 ? 144.530 89.139  116.152 1.00 8.75   ? 1237 ARG B C     1 
ATOM   20367 O  O     . ARG B 2  1237 ? 144.010 88.357  116.946 1.00 18.88  ? 1237 ARG B O     1 
ATOM   20368 C  CB    . ARG B 2  1237 ? 147.026 89.207  116.219 1.00 13.74  ? 1237 ARG B CB    1 
ATOM   20369 C  CG    . ARG B 2  1237 ? 148.284 89.925  116.656 1.00 11.35  ? 1237 ARG B CG    1 
ATOM   20370 C  CD    . ARG B 2  1237 ? 149.466 89.491  115.820 1.00 15.22  ? 1237 ARG B CD    1 
ATOM   20371 N  NE    . ARG B 2  1237 ? 150.616 90.369  115.981 1.00 13.07  ? 1237 ARG B NE    1 
ATOM   20372 C  CZ    . ARG B 2  1237 ? 151.536 90.242  116.923 1.00 17.08  ? 1237 ARG B CZ    1 
ATOM   20373 N  NH1   . ARG B 2  1237 ? 151.491 89.262  117.806 1.00 21.22  ? 1237 ARG B NH1   1 
ATOM   20374 N  NH2   . ARG B 2  1237 ? 152.532 91.114  116.974 1.00 18.17  ? 1237 ARG B NH2   1 
ATOM   20375 N  N     . VAL B 2  1238 ? 144.066 89.318  114.924 1.00 9.92   ? 1238 VAL B N     1 
ATOM   20376 C  CA    . VAL B 2  1238 ? 142.875 88.643  114.425 1.00 10.58  ? 1238 VAL B CA    1 
ATOM   20377 C  C     . VAL B 2  1238 ? 143.273 87.842  113.196 1.00 9.18   ? 1238 VAL B C     1 
ATOM   20378 O  O     . VAL B 2  1238 ? 144.062 88.315  112.377 1.00 16.65  ? 1238 VAL B O     1 
ATOM   20379 C  CB    . VAL B 2  1238 ? 141.751 89.645  114.087 1.00 11.20  ? 1238 VAL B CB    1 
ATOM   20380 C  CG1   . VAL B 2  1238 ? 140.474 88.917  113.751 1.00 13.74  ? 1238 VAL B CG1   1 
ATOM   20381 C  CG2   . VAL B 2  1238 ? 141.528 90.609  115.222 1.00 14.41  ? 1238 VAL B CG2   1 
ATOM   20382 N  N     . PHE B 2  1239 ? 142.745 86.630  113.068 1.00 9.70   ? 1239 PHE B N     1 
ATOM   20383 C  CA    . PHE B 2  1239 ? 143.127 85.747  111.976 1.00 13.37  ? 1239 PHE B CA    1 
ATOM   20384 C  C     . PHE B 2  1239 ? 141.888 85.166  111.323 1.00 17.54  ? 1239 PHE B C     1 
ATOM   20385 O  O     . PHE B 2  1239 ? 140.961 84.733  112.007 1.00 22.78  ? 1239 PHE B O     1 
ATOM   20386 C  CB    . PHE B 2  1239 ? 144.034 84.616  112.469 1.00 13.33  ? 1239 PHE B CB    1 
ATOM   20387 C  CG    . PHE B 2  1239 ? 145.373 85.087  112.921 1.00 14.99  ? 1239 PHE B CG    1 
ATOM   20388 C  CD1   . PHE B 2  1239 ? 145.712 85.072  114.252 1.00 16.47  ? 1239 PHE B CD1   1 
ATOM   20389 C  CD2   . PHE B 2  1239 ? 146.290 85.556  112.014 1.00 12.99  ? 1239 PHE B CD2   1 
ATOM   20390 C  CE1   . PHE B 2  1239 ? 146.929 85.524  114.659 1.00 16.41  ? 1239 PHE B CE1   1 
ATOM   20391 C  CE2   . PHE B 2  1239 ? 147.498 85.998  112.423 1.00 9.62   ? 1239 PHE B CE2   1 
ATOM   20392 C  CZ    . PHE B 2  1239 ? 147.820 85.983  113.743 1.00 11.86  ? 1239 PHE B CZ    1 
ATOM   20393 N  N     . GLN B 2  1240 ? 141.873 85.175  109.998 1.00 18.25  ? 1240 GLN B N     1 
ATOM   20394 C  CA    . GLN B 2  1240 ? 140.817 84.516  109.257 1.00 19.02  ? 1240 GLN B CA    1 
ATOM   20395 C  C     . GLN B 2  1240 ? 140.978 83.003  109.394 1.00 23.47  ? 1240 GLN B C     1 
ATOM   20396 O  O     . GLN B 2  1240 ? 142.099 82.493  109.385 1.00 22.10  ? 1240 GLN B O     1 
ATOM   20397 C  CB    . GLN B 2  1240 ? 140.883 84.930  107.795 1.00 17.28  ? 1240 GLN B CB    1 
ATOM   20398 C  CG    . GLN B 2  1240 ? 139.718 85.752  107.328 1.00 19.81  ? 1240 GLN B CG    1 
ATOM   20399 C  CD    . GLN B 2  1240 ? 139.821 86.089  105.865 1.00 25.16  ? 1240 GLN B CD    1 
ATOM   20400 O  OE1   . GLN B 2  1240 ? 140.914 86.096  105.295 1.00 26.50  ? 1240 GLN B OE1   1 
ATOM   20401 N  NE2   . GLN B 2  1240 ? 138.687 86.381  105.245 1.00 23.75  ? 1240 GLN B NE2   1 
ATOM   20402 N  N     . PRO B 2  1241 ? 139.880 82.262  109.525 1.00 33.15  ? 1241 PRO B N     1 
ATOM   20403 C  CA    . PRO B 2  1241 ? 139.989 80.842  109.879 1.00 28.70  ? 1241 PRO B CA    1 
ATOM   20404 C  C     . PRO B 2  1241 ? 140.724 80.023  108.830 1.00 27.40  ? 1241 PRO B C     1 
ATOM   20405 O  O     . PRO B 2  1241 ? 140.586 80.238  107.623 1.00 27.76  ? 1241 PRO B O     1 
ATOM   20406 C  CB    . PRO B 2  1241 ? 138.528 80.396  110.003 1.00 27.83  ? 1241 PRO B CB    1 
ATOM   20407 C  CG    . PRO B 2  1241 ? 137.775 81.357  109.188 1.00 27.71  ? 1241 PRO B CG    1 
ATOM   20408 C  CD    . PRO B 2  1241 ? 138.481 82.668  109.331 1.00 30.02  ? 1241 PRO B CD    1 
ATOM   20409 N  N     . ALA B 2  1242 ? 141.504 79.061  109.317 1.00 30.11  ? 1242 ALA B N     1 
ATOM   20410 C  CA    . ALA B 2  1242 ? 142.292 78.156  108.478 1.00 32.94  ? 1242 ALA B CA    1 
ATOM   20411 C  C     . ALA B 2  1242 ? 143.176 78.908  107.493 1.00 33.12  ? 1242 ALA B C     1 
ATOM   20412 O  O     . ALA B 2  1242 ? 143.238 78.561  106.316 1.00 34.94  ? 1242 ALA B O     1 
ATOM   20413 C  CB    . ALA B 2  1242 ? 141.381 77.190  107.733 1.00 31.87  ? 1242 ALA B CB    1 
ATOM   20414 N  N     . LYS C 3  3    ? 121.064 169.501 69.278  1.00 28.96  ? 3    LYS C N     1 
ATOM   20415 C  CA    . LYS C 3  3    ? 121.665 170.159 70.427  1.00 25.32  ? 3    LYS C CA    1 
ATOM   20416 C  C     . LYS C 3  3    ? 121.273 169.435 71.698  1.00 26.99  ? 3    LYS C C     1 
ATOM   20417 O  O     . LYS C 3  3    ? 120.219 169.696 72.264  1.00 26.88  ? 3    LYS C O     1 
ATOM   20418 C  CB    . LYS C 3  3    ? 121.230 171.613 70.495  1.00 28.68  ? 3    LYS C CB    1 
ATOM   20419 C  CG    . LYS C 3  3    ? 122.314 172.586 70.104  1.00 33.36  ? 3    LYS C CG    1 
ATOM   20420 C  CD    . LYS C 3  3    ? 122.888 173.298 71.312  1.00 31.83  ? 3    LYS C CD    1 
ATOM   20421 C  CE    . LYS C 3  3    ? 123.951 174.284 70.881  1.00 30.44  ? 3    LYS C CE    1 
ATOM   20422 N  NZ    . LYS C 3  3    ? 124.893 174.589 71.975  1.00 32.80  ? 3    LYS C NZ    1 
ATOM   20423 N  N     . ILE C 3  4    ? 122.121 168.510 72.143  1.00 25.91  ? 4    ILE C N     1 
ATOM   20424 C  CA    . ILE C 3  4    ? 121.750 167.684 73.284  1.00 21.06  ? 4    ILE C CA    1 
ATOM   20425 C  C     . ILE C 3  4    ? 121.737 168.507 74.557  1.00 22.73  ? 4    ILE C C     1 
ATOM   20426 O  O     . ILE C 3  4    ? 120.788 168.432 75.344  1.00 27.83  ? 4    ILE C O     1 
ATOM   20427 C  CB    . ILE C 3  4    ? 122.672 166.462 73.404  1.00 25.80  ? 4    ILE C CB    1 
ATOM   20428 C  CG1   . ILE C 3  4    ? 122.226 165.384 72.422  1.00 23.32  ? 4    ILE C CG1   1 
ATOM   20429 C  CG2   . ILE C 3  4    ? 122.621 165.907 74.813  1.00 26.00  ? 4    ILE C CG2   1 
ATOM   20430 C  CD1   . ILE C 3  4    ? 122.985 164.104 72.549  1.00 24.95  ? 4    ILE C CD1   1 
ATOM   20431 N  N     . PHE C 3  5    ? 122.760 169.321 74.787  1.00 22.29  ? 5    PHE C N     1 
ATOM   20432 C  CA    . PHE C 3  5    ? 122.739 170.132 75.989  1.00 27.66  ? 5    PHE C CA    1 
ATOM   20433 C  C     . PHE C 3  5    ? 122.859 171.603 75.632  1.00 22.34  ? 5    PHE C C     1 
ATOM   20434 O  O     . PHE C 3  5    ? 123.677 171.994 74.797  1.00 25.39  ? 5    PHE C O     1 
ATOM   20435 C  CB    . PHE C 3  5    ? 123.808 169.682 76.995  1.00 25.60  ? 5    PHE C CB    1 
ATOM   20436 C  CG    . PHE C 3  5    ? 125.044 170.512 77.050  1.00 24.72  ? 5    PHE C CG    1 
ATOM   20437 C  CD1   . PHE C 3  5    ? 126.118 170.236 76.250  1.00 21.38  ? 5    PHE C CD1   1 
ATOM   20438 C  CD2   . PHE C 3  5    ? 125.166 171.501 78.016  1.00 24.44  ? 5    PHE C CD2   1 
ATOM   20439 C  CE1   . PHE C 3  5    ? 127.261 170.981 76.354  1.00 27.49  ? 5    PHE C CE1   1 
ATOM   20440 C  CE2   . PHE C 3  5    ? 126.310 172.243 78.128  1.00 20.63  ? 5    PHE C CE2   1 
ATOM   20441 C  CZ    . PHE C 3  5    ? 127.360 171.987 77.294  1.00 23.84  ? 5    PHE C CZ    1 
ATOM   20442 N  N     . GLN C 3  6    ? 121.992 172.394 76.258  1.00 20.15  ? 6    GLN C N     1 
ATOM   20443 C  CA    . GLN C 3  6    ? 121.886 173.825 76.054  1.00 22.65  ? 6    GLN C CA    1 
ATOM   20444 C  C     . GLN C 3  6    ? 122.011 174.542 77.387  1.00 25.81  ? 6    GLN C C     1 
ATOM   20445 O  O     . GLN C 3  6    ? 122.090 173.899 78.435  1.00 29.65  ? 6    GLN C O     1 
ATOM   20446 C  CB    . GLN C 3  6    ? 120.551 174.171 75.405  1.00 24.41  ? 6    GLN C CB    1 
ATOM   20447 C  CG    . GLN C 3  6    ? 120.043 173.142 74.409  1.00 29.62  ? 6    GLN C CG    1 
ATOM   20448 C  CD    . GLN C 3  6    ? 118.976 172.229 74.984  1.00 29.47  ? 6    GLN C CD    1 
ATOM   20449 O  OE1   . GLN C 3  6    ? 118.444 172.478 76.064  1.00 30.59  ? 6    GLN C OE1   1 
ATOM   20450 N  NE2   . GLN C 3  6    ? 118.639 171.181 74.247  1.00 26.71  ? 6    GLN C NE2   1 
ATOM   20451 N  N     . ASN C 3  7    ? 122.059 175.868 77.359  1.00 32.79  ? 7    ASN C N     1 
ATOM   20452 C  CA    . ASN C 3  7    ? 121.837 176.690 78.543  1.00 29.91  ? 7    ASN C CA    1 
ATOM   20453 C  C     . ASN C 3  7    ? 122.758 176.293 79.698  1.00 32.67  ? 7    ASN C C     1 
ATOM   20454 O  O     . ASN C 3  7    ? 122.349 175.666 80.670  1.00 35.68  ? 7    ASN C O     1 
ATOM   20455 C  CB    . ASN C 3  7    ? 120.373 176.621 78.972  1.00 29.40  ? 7    ASN C CB    1 
ATOM   20456 C  CG    . ASN C 3  7    ? 119.997 177.747 79.891  1.00 35.02  ? 7    ASN C CG    1 
ATOM   20457 O  OD1   . ASN C 3  7    ? 120.530 177.871 80.991  1.00 32.37  ? 7    ASN C OD1   1 
ATOM   20458 N  ND2   . ASN C 3  7    ? 119.085 178.593 79.438  1.00 36.85  ? 7    ASN C ND2   1 
ATOM   20459 N  N     . VAL C 3  8    ? 124.022 176.638 79.546  1.00 26.00  ? 8    VAL C N     1 
ATOM   20460 C  CA    . VAL C 3  8    ? 124.967 176.528 80.647  1.00 21.71  ? 8    VAL C CA    1 
ATOM   20461 C  C     . VAL C 3  8    ? 124.944 177.821 81.447  1.00 20.79  ? 8    VAL C C     1 
ATOM   20462 O  O     . VAL C 3  8    ? 124.653 178.892 80.910  1.00 27.66  ? 8    VAL C O     1 
ATOM   20463 C  CB    . VAL C 3  8    ? 126.372 176.205 80.117  1.00 20.70  ? 8    VAL C CB    1 
ATOM   20464 C  CG1   . VAL C 3  8    ? 126.963 177.404 79.424  1.00 24.56  ? 8    VAL C CG1   1 
ATOM   20465 C  CG2   . VAL C 3  8    ? 127.270 175.725 81.238  1.00 22.10  ? 8    VAL C CG2   1 
ATOM   20466 N  N     . GLU C 3  9    ? 125.209 177.724 82.748  1.00 20.96  ? 9    GLU C N     1 
ATOM   20467 C  CA    . GLU C 3  9    ? 125.329 178.891 83.616  1.00 19.37  ? 9    GLU C CA    1 
ATOM   20468 C  C     . GLU C 3  9    ? 126.582 178.713 84.458  1.00 25.76  ? 9    GLU C C     1 
ATOM   20469 O  O     . GLU C 3  9    ? 126.760 177.672 85.093  1.00 26.74  ? 9    GLU C O     1 
ATOM   20470 C  CB    . GLU C 3  9    ? 124.099 179.058 84.507  1.00 21.02  ? 9    GLU C CB    1 
ATOM   20471 C  CG    . GLU C 3  9    ? 122.843 179.437 83.756  1.00 26.27  ? 9    GLU C CG    1 
ATOM   20472 C  CD    . GLU C 3  9    ? 122.946 180.777 83.055  1.00 33.32  ? 9    GLU C CD    1 
ATOM   20473 O  OE1   . GLU C 3  9    ? 123.284 181.780 83.721  1.00 35.16  ? 9    GLU C OE1   1 
ATOM   20474 O  OE2   . GLU C 3  9    ? 122.698 180.823 81.830  1.00 25.53  ? 9    GLU C OE2   1 
ATOM   20475 N  N     . ILE C 3  10   ? 127.441 179.724 84.474  1.00 22.24  ? 10   ILE C N     1 
ATOM   20476 C  CA    . ILE C 3  10   ? 128.716 179.674 85.175  1.00 14.08  ? 10   ILE C CA    1 
ATOM   20477 C  C     . ILE C 3  10   ? 128.748 180.788 86.207  1.00 21.58  ? 10   ILE C C     1 
ATOM   20478 O  O     . ILE C 3  10   ? 128.453 181.942 85.888  1.00 30.06  ? 10   ILE C O     1 
ATOM   20479 C  CB    . ILE C 3  10   ? 129.892 179.792 84.196  1.00 15.86  ? 10   ILE C CB    1 
ATOM   20480 C  CG1   . ILE C 3  10   ? 130.027 178.506 83.382  1.00 18.92  ? 10   ILE C CG1   1 
ATOM   20481 C  CG2   . ILE C 3  10   ? 131.151 180.109 84.934  1.00 18.74  ? 10   ILE C CG2   1 
ATOM   20482 C  CD1   . ILE C 3  10   ? 131.036 178.583 82.286  1.00 20.02  ? 10   ILE C CD1   1 
ATOM   20483 N  N     . LYS C 3  11   ? 129.106 180.447 87.439  1.00 19.14  ? 11   LYS C N     1 
ATOM   20484 C  CA    . LYS C 3  11   ? 129.091 181.432 88.510  1.00 17.10  ? 11   LYS C CA    1 
ATOM   20485 C  C     . LYS C 3  11   ? 130.227 181.217 89.500  1.00 19.28  ? 11   LYS C C     1 
ATOM   20486 O  O     . LYS C 3  11   ? 130.141 180.330 90.354  1.00 21.13  ? 11   LYS C O     1 
ATOM   20487 C  CB    . LYS C 3  11   ? 127.751 181.385 89.236  1.00 15.26  ? 11   LYS C CB    1 
ATOM   20488 C  CG    . LYS C 3  11   ? 127.300 182.711 89.789  1.00 22.50  ? 11   LYS C CG    1 
ATOM   20489 C  CD    . LYS C 3  11   ? 126.554 183.504 88.734  1.00 26.31  ? 11   LYS C CD    1 
ATOM   20490 C  CE    . LYS C 3  11   ? 125.536 182.649 87.996  1.00 23.92  ? 11   LYS C CE    1 
ATOM   20491 N  NZ    . LYS C 3  11   ? 125.216 183.216 86.658  1.00 18.89  ? 11   LYS C NZ    1 
ATOM   20492 N  N     . PRO C 3  12   ? 131.289 182.013 89.437  1.00 16.01  ? 12   PRO C N     1 
ATOM   20493 C  CA    . PRO C 3  12   ? 132.374 181.876 90.411  1.00 11.28  ? 12   PRO C CA    1 
ATOM   20494 C  C     . PRO C 3  12   ? 131.940 182.253 91.817  1.00 11.37  ? 12   PRO C C     1 
ATOM   20495 O  O     . PRO C 3  12   ? 131.052 183.079 92.030  1.00 18.98  ? 12   PRO C O     1 
ATOM   20496 C  CB    . PRO C 3  12   ? 133.441 182.839 89.885  1.00 13.75  ? 12   PRO C CB    1 
ATOM   20497 C  CG    . PRO C 3  12   ? 132.702 183.809 89.085  1.00 15.07  ? 12   PRO C CG    1 
ATOM   20498 C  CD    . PRO C 3  12   ? 131.577 183.063 88.450  1.00 14.20  ? 12   PRO C CD    1 
ATOM   20499 N  N     . PHE C 3  13   ? 132.594 181.627 92.788  1.00 7.08   ? 13   PHE C N     1 
ATOM   20500 C  CA    . PHE C 3  13   ? 132.394 181.926 94.202  1.00 9.08   ? 13   PHE C CA    1 
ATOM   20501 C  C     . PHE C 3  13   ? 133.402 182.995 94.608  1.00 18.11  ? 13   PHE C C     1 
ATOM   20502 O  O     . PHE C 3  13   ? 134.611 182.753 94.597  1.00 21.66  ? 13   PHE C O     1 
ATOM   20503 C  CB    . PHE C 3  13   ? 132.558 180.673 95.054  1.00 10.51  ? 13   PHE C CB    1 
ATOM   20504 C  CG    . PHE C 3  13   ? 131.405 179.730 94.975  1.00 13.14  ? 13   PHE C CG    1 
ATOM   20505 C  CD1   . PHE C 3  13   ? 130.114 180.197 94.943  1.00 18.26  ? 13   PHE C CD1   1 
ATOM   20506 C  CD2   . PHE C 3  13   ? 131.611 178.375 94.951  1.00 12.80  ? 13   PHE C CD2   1 
ATOM   20507 C  CE1   . PHE C 3  13   ? 129.055 179.321 94.876  1.00 18.81  ? 13   PHE C CE1   1 
ATOM   20508 C  CE2   . PHE C 3  13   ? 130.559 177.504 94.888  1.00 8.08   ? 13   PHE C CE2   1 
ATOM   20509 C  CZ    . PHE C 3  13   ? 129.284 177.972 94.852  1.00 11.62  ? 13   PHE C CZ    1 
ATOM   20510 N  N     . LEU C 3  14   ? 132.905 184.170 94.977  1.00 19.35  ? 14   LEU C N     1 
ATOM   20511 C  CA    . LEU C 3  14   ? 133.736 185.334 95.231  1.00 15.11  ? 14   LEU C CA    1 
ATOM   20512 C  C     . LEU C 3  14   ? 133.589 185.800 96.671  1.00 16.12  ? 14   LEU C C     1 
ATOM   20513 O  O     . LEU C 3  14   ? 132.588 185.537 97.333  1.00 21.29  ? 14   LEU C O     1 
ATOM   20514 C  CB    . LEU C 3  14   ? 133.376 186.474 94.277  1.00 20.50  ? 14   LEU C CB    1 
ATOM   20515 C  CG    . LEU C 3  14   ? 133.518 186.199 92.781  1.00 18.18  ? 14   LEU C CG    1 
ATOM   20516 C  CD1   . LEU C 3  14   ? 133.127 187.426 92.000  1.00 17.39  ? 14   LEU C CD1   1 
ATOM   20517 C  CD2   . LEU C 3  14   ? 134.935 185.794 92.437  1.00 17.28  ? 14   LEU C CD2   1 
ATOM   20518 N  N     . ILE C 3  15   ? 134.612 186.497 97.146  1.00 18.12  ? 15   ILE C N     1 
ATOM   20519 C  CA    . ILE C 3  15   ? 134.624 187.060 98.492  1.00 17.26  ? 15   ILE C CA    1 
ATOM   20520 C  C     . ILE C 3  15   ? 133.892 188.392 98.494  1.00 17.37  ? 15   ILE C C     1 
ATOM   20521 O  O     . ILE C 3  15   ? 134.054 189.209 97.584  1.00 25.72  ? 15   ILE C O     1 
ATOM   20522 C  CB    . ILE C 3  15   ? 136.068 187.224 98.993  1.00 17.00  ? 15   ILE C CB    1 
ATOM   20523 C  CG1   . ILE C 3  15   ? 136.725 185.864 99.203  1.00 18.96  ? 15   ILE C CG1   1 
ATOM   20524 C  CG2   . ILE C 3  15   ? 136.101 188.014 100.266 1.00 16.03  ? 15   ILE C CG2   1 
ATOM   20525 C  CD1   . ILE C 3  15   ? 138.166 185.942 99.631  1.00 18.92  ? 15   ILE C CD1   1 
ATOM   20526 N  N     . ASP C 3  16   ? 133.070 188.614 99.511  1.00 16.34  ? 16   ASP C N     1 
ATOM   20527 C  CA    . ASP C 3  16   ? 132.353 189.872 99.682  1.00 19.21  ? 16   ASP C CA    1 
ATOM   20528 C  C     . ASP C 3  16   ? 133.153 190.772 100.616 1.00 22.89  ? 16   ASP C C     1 
ATOM   20529 O  O     . ASP C 3  16   ? 133.130 190.588 101.835 1.00 23.39  ? 16   ASP C O     1 
ATOM   20530 C  CB    . ASP C 3  16   ? 130.957 189.621 100.237 1.00 20.76  ? 16   ASP C CB    1 
ATOM   20531 C  CG    . ASP C 3  16   ? 130.052 190.810 100.084 1.00 25.23  ? 16   ASP C CG    1 
ATOM   20532 O  OD1   . ASP C 3  16   ? 130.424 191.751 99.359  1.00 25.82  ? 16   ASP C OD1   1 
ATOM   20533 O  OD2   . ASP C 3  16   ? 128.968 190.813 100.700 1.00 24.94  ? 16   ASP C OD2   1 
ATOM   20534 N  N     . PHE C 3  17   ? 133.846 191.754 100.049 1.00 24.59  ? 17   PHE C N     1 
ATOM   20535 C  CA    . PHE C 3  17   ? 134.649 192.677 100.837 1.00 20.93  ? 17   PHE C CA    1 
ATOM   20536 C  C     . PHE C 3  17   ? 133.833 193.813 101.435 1.00 21.88  ? 17   PHE C C     1 
ATOM   20537 O  O     . PHE C 3  17   ? 134.394 194.647 102.149 1.00 24.17  ? 17   PHE C O     1 
ATOM   20538 C  CB    . PHE C 3  17   ? 135.792 193.236 99.991  1.00 22.98  ? 17   PHE C CB    1 
ATOM   20539 C  CG    . PHE C 3  17   ? 136.906 192.263 99.780  1.00 23.75  ? 17   PHE C CG    1 
ATOM   20540 C  CD1   . PHE C 3  17   ? 137.788 191.981 100.800 1.00 21.62  ? 17   PHE C CD1   1 
ATOM   20541 C  CD2   . PHE C 3  17   ? 137.061 191.618 98.572  1.00 23.95  ? 17   PHE C CD2   1 
ATOM   20542 C  CE1   . PHE C 3  17   ? 138.799 191.081 100.619 1.00 20.55  ? 17   PHE C CE1   1 
ATOM   20543 C  CE2   . PHE C 3  17   ? 138.077 190.719 98.388  1.00 23.32  ? 17   PHE C CE2   1 
ATOM   20544 C  CZ    . PHE C 3  17   ? 138.945 190.452 99.414  1.00 24.40  ? 17   PHE C CZ    1 
ATOM   20545 N  N     . SER C 3  18   ? 132.530 193.867 101.161 1.00 25.11  ? 18   SER C N     1 
ATOM   20546 C  CA    . SER C 3  18   ? 131.659 194.819 101.839 1.00 24.17  ? 18   SER C CA    1 
ATOM   20547 C  C     . SER C 3  18   ? 131.429 194.459 103.300 1.00 27.29  ? 18   SER C C     1 
ATOM   20548 O  O     . SER C 3  18   ? 131.100 195.342 104.095 1.00 28.88  ? 18   SER C O     1 
ATOM   20549 C  CB    . SER C 3  18   ? 130.319 194.911 101.119 1.00 25.68  ? 18   SER C CB    1 
ATOM   20550 O  OG    . SER C 3  18   ? 129.382 194.029 101.701 1.00 27.58  ? 18   SER C OG    1 
ATOM   20551 N  N     . ASN C 3  19   ? 131.581 193.190 103.669 1.00 22.50  ? 19   ASN C N     1 
ATOM   20552 C  CA    . ASN C 3  19   ? 131.578 192.804 105.072 1.00 17.43  ? 19   ASN C CA    1 
ATOM   20553 C  C     . ASN C 3  19   ? 132.849 193.328 105.718 1.00 20.74  ? 19   ASN C C     1 
ATOM   20554 O  O     . ASN C 3  19   ? 133.952 193.035 105.253 1.00 29.02  ? 19   ASN C O     1 
ATOM   20555 C  CB    . ASN C 3  19   ? 131.475 191.289 105.213 1.00 19.51  ? 19   ASN C CB    1 
ATOM   20556 C  CG    . ASN C 3  19   ? 131.220 190.848 106.636 1.00 18.99  ? 19   ASN C CG    1 
ATOM   20557 O  OD1   . ASN C 3  19   ? 132.041 191.064 107.515 1.00 18.32  ? 19   ASN C OD1   1 
ATOM   20558 N  ND2   . ASN C 3  19   ? 130.080 190.225 106.868 1.00 21.80  ? 19   ASN C ND2   1 
ATOM   20559 N  N     . LEU C 3  20   ? 132.698 194.112 106.783 1.00 23.88  ? 20   LEU C N     1 
ATOM   20560 C  CA    . LEU C 3  20   ? 133.846 194.805 107.355 1.00 24.10  ? 20   LEU C CA    1 
ATOM   20561 C  C     . LEU C 3  20   ? 134.806 193.844 108.038 1.00 23.09  ? 20   LEU C C     1 
ATOM   20562 O  O     . LEU C 3  20   ? 136.024 194.001 107.932 1.00 30.12  ? 20   LEU C O     1 
ATOM   20563 C  CB    . LEU C 3  20   ? 133.379 195.878 108.332 1.00 27.25  ? 20   LEU C CB    1 
ATOM   20564 C  CG    . LEU C 3  20   ? 133.640 197.308 107.863 1.00 29.20  ? 20   LEU C CG    1 
ATOM   20565 C  CD1   . LEU C 3  20   ? 132.830 197.637 106.620 1.00 21.25  ? 20   LEU C CD1   1 
ATOM   20566 C  CD2   . LEU C 3  20   ? 133.351 198.295 108.975 1.00 28.28  ? 20   LEU C CD2   1 
ATOM   20567 N  N     . PHE C 3  21   ? 134.281 192.859 108.761 1.00 17.36  ? 21   PHE C N     1 
ATOM   20568 C  CA    . PHE C 3  21   ? 135.141 191.943 109.499 1.00 18.25  ? 21   PHE C CA    1 
ATOM   20569 C  C     . PHE C 3  21   ? 135.995 191.105 108.554 1.00 21.76  ? 21   PHE C C     1 
ATOM   20570 O  O     . PHE C 3  21   ? 137.198 190.926 108.783 1.00 21.85  ? 21   PHE C O     1 
ATOM   20571 C  CB    . PHE C 3  21   ? 134.281 191.068 110.406 1.00 18.89  ? 21   PHE C CB    1 
ATOM   20572 C  CG    . PHE C 3  21   ? 133.398 191.853 111.319 1.00 20.31  ? 21   PHE C CG    1 
ATOM   20573 C  CD1   . PHE C 3  21   ? 133.862 192.287 112.544 1.00 20.60  ? 21   PHE C CD1   1 
ATOM   20574 C  CD2   . PHE C 3  21   ? 132.113 192.182 110.944 1.00 19.47  ? 21   PHE C CD2   1 
ATOM   20575 C  CE1   . PHE C 3  21   ? 133.059 193.020 113.378 1.00 18.24  ? 21   PHE C CE1   1 
ATOM   20576 C  CE2   . PHE C 3  21   ? 131.308 192.912 111.775 1.00 20.27  ? 21   PHE C CE2   1 
ATOM   20577 C  CZ    . PHE C 3  21   ? 131.780 193.330 112.994 1.00 20.75  ? 21   PHE C CZ    1 
ATOM   20578 N  N     . ILE C 3  22   ? 135.394 190.599 107.473 1.00 19.86  ? 22   ILE C N     1 
ATOM   20579 C  CA    . ILE C 3  22   ? 136.153 189.858 106.470 1.00 17.09  ? 22   ILE C CA    1 
ATOM   20580 C  C     . ILE C 3  22   ? 137.211 190.752 105.844 1.00 18.46  ? 22   ILE C C     1 
ATOM   20581 O  O     . ILE C 3  22   ? 138.360 190.340 105.655 1.00 24.11  ? 22   ILE C O     1 
ATOM   20582 C  CB    . ILE C 3  22   ? 135.210 189.271 105.402 1.00 20.30  ? 22   ILE C CB    1 
ATOM   20583 C  CG1   . ILE C 3  22   ? 134.229 188.271 106.014 1.00 20.38  ? 22   ILE C CG1   1 
ATOM   20584 C  CG2   . ILE C 3  22   ? 136.003 188.607 104.302 1.00 18.01  ? 22   ILE C CG2   1 
ATOM   20585 C  CD1   . ILE C 3  22   ? 134.877 187.082 106.646 1.00 16.48  ? 22   ILE C CD1   1 
ATOM   20586 N  N     . LYS C 3  23   ? 136.845 191.992 105.518 1.00 22.65  ? 23   LYS C N     1 
ATOM   20587 C  CA    . LYS C 3  23   ? 137.792 192.910 104.896 1.00 22.92  ? 23   LYS C CA    1 
ATOM   20588 C  C     . LYS C 3  23   ? 138.983 193.178 105.805 1.00 23.15  ? 23   LYS C C     1 
ATOM   20589 O  O     . LYS C 3  23   ? 140.136 193.148 105.363 1.00 26.16  ? 23   LYS C O     1 
ATOM   20590 C  CB    . LYS C 3  23   ? 137.094 194.217 104.536 1.00 21.40  ? 23   LYS C CB    1 
ATOM   20591 C  CG    . LYS C 3  23   ? 138.032 195.398 104.460 1.00 26.04  ? 23   LYS C CG    1 
ATOM   20592 C  CD    . LYS C 3  23   ? 137.381 196.599 103.815 1.00 25.89  ? 23   LYS C CD    1 
ATOM   20593 C  CE    . LYS C 3  23   ? 137.184 196.387 102.327 1.00 25.78  ? 23   LYS C CE    1 
ATOM   20594 N  NZ    . LYS C 3  23   ? 135.903 196.979 101.844 1.00 24.90  ? 23   LYS C NZ    1 
ATOM   20595 N  N     . ASN C 3  24   ? 138.723 193.442 107.083 1.00 18.40  ? 24   ASN C N     1 
ATOM   20596 C  CA    . ASN C 3  24   ? 139.811 193.742 108.004 1.00 19.86  ? 24   ASN C CA    1 
ATOM   20597 C  C     . ASN C 3  24   ? 140.711 192.533 108.215 1.00 20.28  ? 24   ASN C C     1 
ATOM   20598 O  O     . ASN C 3  24   ? 141.943 192.663 108.208 1.00 26.81  ? 24   ASN C O     1 
ATOM   20599 C  CB    . ASN C 3  24   ? 139.251 194.238 109.335 1.00 21.48  ? 24   ASN C CB    1 
ATOM   20600 C  CG    . ASN C 3  24   ? 138.513 195.553 109.204 1.00 23.96  ? 24   ASN C CG    1 
ATOM   20601 O  OD1   . ASN C 3  24   ? 138.833 196.374 108.354 1.00 26.82  ? 24   ASN C OD1   1 
ATOM   20602 N  ND2   . ASN C 3  24   ? 137.523 195.760 110.055 1.00 24.64  ? 24   ASN C ND2   1 
ATOM   20603 N  N     . ALA C 3  25   ? 140.121 191.348 108.392 1.00 20.04  ? 25   ALA C N     1 
ATOM   20604 C  CA    . ALA C 3  25   ? 140.932 190.151 108.581 1.00 19.91  ? 25   ALA C CA    1 
ATOM   20605 C  C     . ALA C 3  25   ? 141.792 189.867 107.358 1.00 19.80  ? 25   ALA C C     1 
ATOM   20606 O  O     . ALA C 3  25   ? 142.987 189.576 107.484 1.00 21.32  ? 25   ALA C O     1 
ATOM   20607 C  CB    . ALA C 3  25   ? 140.036 188.958 108.895 1.00 17.95  ? 25   ALA C CB    1 
ATOM   20608 N  N     . ALA C 3  26   ? 141.208 189.970 106.165 1.00 18.58  ? 26   ALA C N     1 
ATOM   20609 C  CA    . ALA C 3  26   ? 141.964 189.726 104.946 1.00 21.33  ? 26   ALA C CA    1 
ATOM   20610 C  C     . ALA C 3  26   ? 143.094 190.729 104.786 1.00 21.01  ? 26   ALA C C     1 
ATOM   20611 O  O     . ALA C 3  26   ? 144.231 190.352 104.481 1.00 22.13  ? 26   ALA C O     1 
ATOM   20612 C  CB    . ALA C 3  26   ? 141.025 189.772 103.745 1.00 21.95  ? 26   ALA C CB    1 
ATOM   20613 N  N     . LYS C 3  27   ? 142.808 192.010 105.024 1.00 26.87  ? 27   LYS C N     1 
ATOM   20614 C  CA    . LYS C 3  27   ? 143.814 193.049 104.846 1.00 25.27  ? 27   LYS C CA    1 
ATOM   20615 C  C     . LYS C 3  27   ? 144.973 192.867 105.807 1.00 23.79  ? 27   LYS C C     1 
ATOM   20616 O  O     . LYS C 3  27   ? 146.136 193.016 105.426 1.00 27.93  ? 27   LYS C O     1 
ATOM   20617 C  CB    . LYS C 3  27   ? 143.175 194.421 105.030 1.00 30.85  ? 27   LYS C CB    1 
ATOM   20618 C  CG    . LYS C 3  27   ? 144.123 195.493 105.512 1.00 32.17  ? 27   LYS C CG    1 
ATOM   20619 C  CD    . LYS C 3  27   ? 144.571 196.380 104.374 1.00 31.57  ? 27   LYS C CD    1 
ATOM   20620 C  CE    . LYS C 3  27   ? 145.869 197.094 104.706 1.00 32.80  ? 27   LYS C CE    1 
ATOM   20621 N  NZ    . LYS C 3  27   ? 147.060 196.346 104.227 1.00 31.71  ? 27   LYS C NZ    1 
ATOM   20622 N  N     . LYS C 3  28   ? 144.685 192.537 107.059 1.00 20.38  ? 28   LYS C N     1 
ATOM   20623 C  CA    . LYS C 3  28   ? 145.741 192.474 108.053 1.00 24.32  ? 28   LYS C CA    1 
ATOM   20624 C  C     . LYS C 3  28   ? 146.452 191.128 108.095 1.00 27.24  ? 28   LYS C C     1 
ATOM   20625 O  O     . LYS C 3  28   ? 147.530 191.033 108.686 1.00 27.68  ? 28   LYS C O     1 
ATOM   20626 C  CB    . LYS C 3  28   ? 145.182 192.830 109.425 1.00 21.78  ? 28   LYS C CB    1 
ATOM   20627 C  CG    . LYS C 3  28   ? 145.021 191.686 110.364 1.00 24.43  ? 28   LYS C CG    1 
ATOM   20628 C  CD    . LYS C 3  28   ? 144.791 192.231 111.751 1.00 32.96  ? 28   LYS C CD    1 
ATOM   20629 C  CE    . LYS C 3  28   ? 145.861 193.221 112.153 1.00 30.54  ? 28   LYS C CE    1 
ATOM   20630 N  NZ    . LYS C 3  28   ? 145.654 193.695 113.551 1.00 31.65  ? 28   LYS C NZ    1 
ATOM   20631 N  N     . LEU C 3  29   ? 145.901 190.093 107.457 1.00 27.20  ? 29   LEU C N     1 
ATOM   20632 C  CA    . LEU C 3  29   ? 146.593 188.813 107.377 1.00 17.98  ? 29   LEU C CA    1 
ATOM   20633 C  C     . LEU C 3  29   ? 147.383 188.644 106.087 1.00 20.48  ? 29   LEU C C     1 
ATOM   20634 O  O     . LEU C 3  29   ? 148.533 188.206 106.123 1.00 22.41  ? 29   LEU C O     1 
ATOM   20635 C  CB    . LEU C 3  29   ? 145.601 187.657 107.521 1.00 18.60  ? 29   LEU C CB    1 
ATOM   20636 C  CG    . LEU C 3  29   ? 145.464 186.975 108.879 1.00 21.66  ? 29   LEU C CG    1 
ATOM   20637 C  CD1   . LEU C 3  29   ? 144.084 186.389 109.026 1.00 19.38  ? 29   LEU C CD1   1 
ATOM   20638 C  CD2   . LEU C 3  29   ? 146.507 185.901 109.022 1.00 24.55  ? 29   LEU C CD2   1 
ATOM   20639 N  N     . PHE C 3  30   ? 146.790 188.964 104.940 1.00 22.56  ? 30   PHE C N     1 
ATOM   20640 C  CA    . PHE C 3  30   ? 147.441 188.683 103.670 1.00 19.92  ? 30   PHE C CA    1 
ATOM   20641 C  C     . PHE C 3  30   ? 147.610 189.917 102.792 1.00 25.93  ? 30   PHE C C     1 
ATOM   20642 O  O     . PHE C 3  30   ? 148.064 189.782 101.651 1.00 29.61  ? 30   PHE C O     1 
ATOM   20643 C  CB    . PHE C 3  30   ? 146.665 187.604 102.900 1.00 19.13  ? 30   PHE C CB    1 
ATOM   20644 C  CG    . PHE C 3  30   ? 146.430 186.353 103.686 1.00 20.90  ? 30   PHE C CG    1 
ATOM   20645 C  CD1   . PHE C 3  30   ? 147.453 185.448 103.892 1.00 21.33  ? 30   PHE C CD1   1 
ATOM   20646 C  CD2   . PHE C 3  30   ? 145.189 186.080 104.221 1.00 21.24  ? 30   PHE C CD2   1 
ATOM   20647 C  CE1   . PHE C 3  30   ? 147.243 184.305 104.619 1.00 22.13  ? 30   PHE C CE1   1 
ATOM   20648 C  CE2   . PHE C 3  30   ? 144.978 184.937 104.943 1.00 18.91  ? 30   PHE C CE2   1 
ATOM   20649 C  CZ    . PHE C 3  30   ? 146.005 184.050 105.143 1.00 22.14  ? 30   PHE C CZ    1 
ATOM   20650 N  N     . GLN C 3  31   ? 147.295 191.109 103.297 1.00 25.63  ? 31   GLN C N     1 
ATOM   20651 C  CA    . GLN C 3  31   ? 147.227 192.321 102.481 1.00 24.42  ? 31   GLN C CA    1 
ATOM   20652 C  C     . GLN C 3  31   ? 146.375 192.073 101.242 1.00 30.94  ? 31   GLN C C     1 
ATOM   20653 O  O     . GLN C 3  31   ? 146.747 192.400 100.116 1.00 35.13  ? 31   GLN C O     1 
ATOM   20654 C  CB    . GLN C 3  31   ? 148.619 192.836 102.103 1.00 25.84  ? 31   GLN C CB    1 
ATOM   20655 C  CG    . GLN C 3  31   ? 149.726 192.449 103.062 1.00 30.18  ? 31   GLN C CG    1 
ATOM   20656 C  CD    . GLN C 3  31   ? 149.600 193.147 104.392 1.00 33.93  ? 31   GLN C CD    1 
ATOM   20657 O  OE1   . GLN C 3  31   ? 149.163 194.293 104.461 1.00 33.16  ? 31   GLN C OE1   1 
ATOM   20658 N  NE2   . GLN C 3  31   ? 149.974 192.457 105.463 1.00 31.76  ? 31   GLN C NE2   1 
ATOM   20659 N  N     . LEU C 3  32   ? 145.224 191.459 101.464 1.00 28.49  ? 32   LEU C N     1 
ATOM   20660 C  CA    . LEU C 3  32   ? 144.313 191.077 100.398 1.00 30.10  ? 32   LEU C CA    1 
ATOM   20661 C  C     . LEU C 3  32   ? 143.143 192.053 100.372 1.00 34.57  ? 32   LEU C C     1 
ATOM   20662 O  O     . LEU C 3  32   ? 142.375 192.143 101.335 1.00 34.50  ? 32   LEU C O     1 
ATOM   20663 C  CB    . LEU C 3  32   ? 143.835 189.642 100.599 1.00 29.88  ? 32   LEU C CB    1 
ATOM   20664 C  CG    . LEU C 3  32   ? 142.966 189.066 99.485  1.00 31.43  ? 32   LEU C CG    1 
ATOM   20665 C  CD1   . LEU C 3  32   ? 143.775 188.817 98.231  1.00 29.10  ? 32   LEU C CD1   1 
ATOM   20666 C  CD2   . LEU C 3  32   ? 142.291 187.801 99.966  1.00 31.58  ? 32   LEU C CD2   1 
ATOM   20667 N  N     . GLU C 3  33   ? 143.018 192.789 99.270  1.00 34.76  ? 33   GLU C N     1 
ATOM   20668 C  CA    . GLU C 3  33   ? 141.898 193.685 99.047  1.00 33.78  ? 33   GLU C CA    1 
ATOM   20669 C  C     . GLU C 3  33   ? 141.098 193.325 97.810  1.00 32.48  ? 33   GLU C C     1 
ATOM   20670 O  O     . GLU C 3  33   ? 140.023 193.891 97.599  1.00 33.29  ? 33   GLU C O     1 
ATOM   20671 C  CB    . GLU C 3  33   ? 142.391 195.133 98.922  1.00 36.33  ? 33   GLU C CB    1 
ATOM   20672 C  CG    . GLU C 3  33   ? 143.537 195.484 99.847  1.00 36.28  ? 33   GLU C CG    1 
ATOM   20673 C  CD    . GLU C 3  33   ? 143.342 196.823 100.527 1.00 38.87  ? 33   GLU C CD    1 
ATOM   20674 O  OE1   . GLU C 3  33   ? 144.178 197.184 101.379 1.00 36.95  ? 33   GLU C OE1   1 
ATOM   20675 O  OE2   . GLU C 3  33   ? 142.349 197.511 100.213 1.00 39.02  ? 33   GLU C OE2   1 
ATOM   20676 N  N     . GLU C 3  34   ? 141.600 192.418 96.991  1.00 34.75  ? 34   GLU C N     1 
ATOM   20677 C  CA    . GLU C 3  34   ? 140.957 191.970 95.772  1.00 34.38  ? 34   GLU C CA    1 
ATOM   20678 C  C     . GLU C 3  34   ? 140.622 190.492 95.908  1.00 36.74  ? 34   GLU C C     1 
ATOM   20679 O  O     . GLU C 3  34   ? 140.769 189.894 96.972  1.00 38.52  ? 34   GLU C O     1 
ATOM   20680 C  CB    . GLU C 3  34   ? 141.862 192.239 94.568  1.00 34.20  ? 34   GLU C CB    1 
ATOM   20681 C  CG    . GLU C 3  34   ? 143.130 191.401 94.519  1.00 35.86  ? 34   GLU C CG    1 
ATOM   20682 C  CD    . GLU C 3  34   ? 144.172 191.803 95.546  1.00 41.40  ? 34   GLU C CD    1 
ATOM   20683 O  OE1   . GLU C 3  34   ? 143.954 192.790 96.272  1.00 43.91  ? 34   GLU C OE1   1 
ATOM   20684 O  OE2   . GLU C 3  34   ? 145.212 191.118 95.635  1.00 43.31  ? 34   GLU C OE2   1 
ATOM   20685 N  N     . GLN C 3  35   ? 140.154 189.899 94.821  1.00 28.33  ? 35   GLN C N     1 
ATOM   20686 C  CA    . GLN C 3  35   ? 139.830 188.485 94.854  1.00 21.55  ? 35   GLN C CA    1 
ATOM   20687 C  C     . GLN C 3  35   ? 141.103 187.647 94.819  1.00 25.04  ? 35   GLN C C     1 
ATOM   20688 O  O     . GLN C 3  35   ? 142.194 188.140 94.532  1.00 28.72  ? 35   GLN C O     1 
ATOM   20689 C  CB    . GLN C 3  35   ? 138.906 188.127 93.695  1.00 19.68  ? 35   GLN C CB    1 
ATOM   20690 C  CG    . GLN C 3  35   ? 137.622 188.933 93.670  1.00 24.12  ? 35   GLN C CG    1 
ATOM   20691 C  CD    . GLN C 3  35   ? 136.743 188.697 94.883  1.00 24.08  ? 35   GLN C CD    1 
ATOM   20692 O  OE1   . GLN C 3  35   ? 136.745 187.618 95.461  1.00 26.50  ? 35   GLN C OE1   1 
ATOM   20693 N  NE2   . GLN C 3  35   ? 135.988 189.710 95.272  1.00 25.41  ? 35   GLN C NE2   1 
ATOM   20694 N  N     . LEU C 3  36   ? 140.960 186.370 95.156  1.00 17.44  ? 36   LEU C N     1 
ATOM   20695 C  CA    . LEU C 3  36   ? 142.093 185.462 95.116  1.00 14.30  ? 36   LEU C CA    1 
ATOM   20696 C  C     . LEU C 3  36   ? 142.397 185.054 93.675  1.00 16.18  ? 36   LEU C C     1 
ATOM   20697 O  O     . LEU C 3  36   ? 141.527 185.132 92.809  1.00 20.42  ? 36   LEU C O     1 
ATOM   20698 C  CB    . LEU C 3  36   ? 141.816 184.230 95.969  1.00 14.70  ? 36   LEU C CB    1 
ATOM   20699 C  CG    . LEU C 3  36   ? 141.877 184.452 97.475  1.00 14.85  ? 36   LEU C CG    1 
ATOM   20700 C  CD1   . LEU C 3  36   ? 141.399 183.231 98.212  1.00 9.62   ? 36   LEU C CD1   1 
ATOM   20701 C  CD2   . LEU C 3  36   ? 143.279 184.808 97.888  1.00 17.16  ? 36   LEU C CD2   1 
ATOM   20702 N  N     . PRO C 3  37   ? 143.634 184.639 93.389  1.00 12.86  ? 37   PRO C N     1 
ATOM   20703 C  CA    . PRO C 3  37   ? 143.971 184.232 92.017  1.00 7.80   ? 37   PRO C CA    1 
ATOM   20704 C  C     . PRO C 3  37   ? 143.147 183.072 91.491  1.00 14.10  ? 37   PRO C C     1 
ATOM   20705 O  O     . PRO C 3  37   ? 142.858 183.035 90.292  1.00 18.43  ? 37   PRO C O     1 
ATOM   20706 C  CB    . PRO C 3  37   ? 145.453 183.853 92.124  1.00 10.68  ? 37   PRO C CB    1 
ATOM   20707 C  CG    . PRO C 3  37   ? 145.932 184.503 93.324  1.00 13.91  ? 37   PRO C CG    1 
ATOM   20708 C  CD    . PRO C 3  37   ? 144.801 184.556 94.275  1.00 14.55  ? 37   PRO C CD    1 
ATOM   20709 N  N     . LEU C 3  38   ? 142.762 182.122 92.338  1.00 9.60   ? 38   LEU C N     1 
ATOM   20710 C  CA    . LEU C 3  38   ? 141.985 180.957 91.933  1.00 7.49   ? 38   LEU C CA    1 
ATOM   20711 C  C     . LEU C 3  38   ? 140.683 180.947 92.716  1.00 11.11  ? 38   LEU C C     1 
ATOM   20712 O  O     . LEU C 3  38   ? 140.684 181.195 93.922  1.00 15.89  ? 38   LEU C O     1 
ATOM   20713 C  CB    . LEU C 3  38   ? 142.773 179.667 92.167  1.00 9.81   ? 38   LEU C CB    1 
ATOM   20714 C  CG    . LEU C 3  38   ? 143.737 179.212 91.067  1.00 8.88   ? 38   LEU C CG    1 
ATOM   20715 C  CD1   . LEU C 3  38   ? 145.003 180.007 91.096  1.00 8.99   ? 38   LEU C CD1   1 
ATOM   20716 C  CD2   . LEU C 3  38   ? 144.059 177.768 91.233  1.00 10.40  ? 38   LEU C CD2   1 
ATOM   20717 N  N     . VAL C 3  39   ? 139.574 180.680 92.034  1.00 12.10  ? 39   VAL C N     1 
ATOM   20718 C  CA    . VAL C 3  39   ? 138.257 180.698 92.669  1.00 12.81  ? 39   VAL C CA    1 
ATOM   20719 C  C     . VAL C 3  39   ? 137.503 179.411 92.357  1.00 10.73  ? 39   VAL C C     1 
ATOM   20720 O  O     . VAL C 3  39   ? 137.781 178.768 91.342  1.00 12.43  ? 39   VAL C O     1 
ATOM   20721 C  CB    . VAL C 3  39   ? 137.440 181.926 92.226  1.00 9.62   ? 39   VAL C CB    1 
ATOM   20722 C  CG1   . VAL C 3  39   ? 138.089 183.198 92.706  1.00 11.20  ? 39   VAL C CG1   1 
ATOM   20723 C  CG2   . VAL C 3  39   ? 137.296 181.954 90.724  1.00 11.24  ? 39   VAL C CG2   1 
ATOM   20724 N  N     . PRO C 3  40   ? 136.570 178.981 93.199  1.00 11.49  ? 40   PRO C N     1 
ATOM   20725 C  CA    . PRO C 3  40   ? 135.667 177.902 92.794  1.00 5.57   ? 40   PRO C CA    1 
ATOM   20726 C  C     . PRO C 3  40   ? 134.612 178.407 91.829  1.00 6.60   ? 40   PRO C C     1 
ATOM   20727 O  O     . PRO C 3  40   ? 134.154 179.546 91.912  1.00 17.16  ? 40   PRO C O     1 
ATOM   20728 C  CB    . PRO C 3  40   ? 135.035 177.449 94.115  1.00 2.06   ? 40   PRO C CB    1 
ATOM   20729 C  CG    . PRO C 3  40   ? 135.853 178.046 95.166  1.00 2.98   ? 40   PRO C CG    1 
ATOM   20730 C  CD    . PRO C 3  40   ? 136.404 179.306 94.620  1.00 11.15  ? 40   PRO C CD    1 
ATOM   20731 N  N     . VAL C 3  41   ? 134.215 177.543 90.906  1.00 4.09   ? 41   VAL C N     1 
ATOM   20732 C  CA    . VAL C 3  41   ? 133.247 177.903 89.881  1.00 6.24   ? 41   VAL C CA    1 
ATOM   20733 C  C     . VAL C 3  41   ? 132.117 176.890 89.911  1.00 5.68   ? 41   VAL C C     1 
ATOM   20734 O  O     . VAL C 3  41   ? 132.365 175.683 89.904  1.00 10.39  ? 41   VAL C O     1 
ATOM   20735 C  CB    . VAL C 3  41   ? 133.890 177.964 88.483  1.00 4.95   ? 41   VAL C CB    1 
ATOM   20736 C  CG1   . VAL C 3  41   ? 132.839 178.115 87.430  1.00 7.54   ? 41   VAL C CG1   1 
ATOM   20737 C  CG2   . VAL C 3  41   ? 134.852 179.117 88.406  1.00 11.14  ? 41   VAL C CG2   1 
ATOM   20738 N  N     . ASN C 3  42   ? 130.885 177.378 89.950  1.00 6.30   ? 42   ASN C N     1 
ATOM   20739 C  CA    . ASN C 3  42   ? 129.699 176.539 89.866  1.00 6.13   ? 42   ASN C CA    1 
ATOM   20740 C  C     . ASN C 3  42   ? 129.175 176.538 88.437  1.00 10.05  ? 42   ASN C C     1 
ATOM   20741 O  O     . ASN C 3  42   ? 128.938 177.600 87.861  1.00 11.67  ? 42   ASN C O     1 
ATOM   20742 C  CB    . ASN C 3  42   ? 128.617 177.037 90.818  1.00 4.69   ? 42   ASN C CB    1 
ATOM   20743 C  CG    . ASN C 3  42   ? 127.536 176.025 91.042  1.00 7.38   ? 42   ASN C CG    1 
ATOM   20744 O  OD1   . ASN C 3  42   ? 127.722 174.843 90.800  1.00 7.87   ? 42   ASN C OD1   1 
ATOM   20745 N  ND2   . ASN C 3  42   ? 126.380 176.489 91.473  1.00 13.14  ? 42   ASN C ND2   1 
ATOM   20746 N  N     . VAL C 3  43   ? 128.991 175.348 87.874  1.00 7.55   ? 43   VAL C N     1 
ATOM   20747 C  CA    . VAL C 3  43   ? 128.522 175.166 86.506  1.00 4.76   ? 43   VAL C CA    1 
ATOM   20748 C  C     . VAL C 3  43   ? 127.229 174.366 86.544  1.00 6.59   ? 43   VAL C C     1 
ATOM   20749 O  O     . VAL C 3  43   ? 127.201 173.257 87.079  1.00 11.72  ? 43   VAL C O     1 
ATOM   20750 C  CB    . VAL C 3  43   ? 129.575 174.445 85.647  1.00 8.79   ? 43   VAL C CB    1 
ATOM   20751 C  CG1   . VAL C 3  43   ? 129.115 174.332 84.217  1.00 8.41   ? 43   VAL C CG1   1 
ATOM   20752 C  CG2   . VAL C 3  43   ? 130.899 175.155 85.736  1.00 10.41  ? 43   VAL C CG2   1 
ATOM   20753 N  N     . VAL C 3  44   ? 126.168 174.918 85.962  1.00 12.78  ? 44   VAL C N     1 
ATOM   20754 C  CA    . VAL C 3  44   ? 124.860 174.272 85.912  1.00 11.13  ? 44   VAL C CA    1 
ATOM   20755 C  C     . VAL C 3  44   ? 124.487 174.068 84.450  1.00 11.57  ? 44   VAL C C     1 
ATOM   20756 O  O     . VAL C 3  44   ? 124.396 175.035 83.689  1.00 11.01  ? 44   VAL C O     1 
ATOM   20757 C  CB    . VAL C 3  44   ? 123.788 175.097 86.642  1.00 6.49   ? 44   VAL C CB    1 
ATOM   20758 C  CG1   . VAL C 3  44   ? 122.491 174.334 86.708  1.00 7.79   ? 44   VAL C CG1   1 
ATOM   20759 C  CG2   . VAL C 3  44   ? 124.254 175.455 88.024  1.00 7.25   ? 44   VAL C CG2   1 
ATOM   20760 N  N     . MET C 3  45   ? 124.254 172.816 84.066  1.00 5.28   ? 45   MET C N     1 
ATOM   20761 C  CA    . MET C 3  45   ? 124.028 172.439 82.680  1.00 6.21   ? 45   MET C CA    1 
ATOM   20762 C  C     . MET C 3  45   ? 122.685 171.743 82.520  1.00 10.54  ? 45   MET C C     1 
ATOM   20763 O  O     . MET C 3  45   ? 122.273 170.964 83.380  1.00 8.59   ? 45   MET C O     1 
ATOM   20764 C  CB    . MET C 3  45   ? 125.137 171.520 82.180  1.00 7.07   ? 45   MET C CB    1 
ATOM   20765 C  CG    . MET C 3  45   ? 126.521 171.885 82.651  1.00 8.63   ? 45   MET C CG    1 
ATOM   20766 S  SD    . MET C 3  45   ? 127.647 170.491 82.747  1.00 13.84  ? 45   MET C SD    1 
ATOM   20767 C  CE    . MET C 3  45   ? 127.611 170.143 84.497  1.00 7.28   ? 45   MET C CE    1 
ATOM   20768 N  N     . ASP C 3  46   ? 122.008 172.024 81.410  1.00 13.55  ? 46   ASP C N     1 
ATOM   20769 C  CA    . ASP C 3  46   ? 120.746 171.385 81.064  1.00 9.49   ? 46   ASP C CA    1 
ATOM   20770 C  C     . ASP C 3  46   ? 120.935 170.504 79.841  1.00 10.07  ? 46   ASP C C     1 
ATOM   20771 O  O     . ASP C 3  46   ? 121.448 170.960 78.819  1.00 15.32  ? 46   ASP C O     1 
ATOM   20772 C  CB    . ASP C 3  46   ? 119.655 172.416 80.790  1.00 11.11  ? 46   ASP C CB    1 
ATOM   20773 C  CG    . ASP C 3  46   ? 119.442 173.360 81.941  1.00 25.78  ? 46   ASP C CG    1 
ATOM   20774 O  OD1   . ASP C 3  46   ? 118.325 173.390 82.488  1.00 23.66  ? 46   ASP C OD1   1 
ATOM   20775 O  OD2   . ASP C 3  46   ? 120.387 174.086 82.302  1.00 29.13  ? 46   ASP C OD2   1 
ATOM   20776 N  N     . PHE C 3  47   ? 120.511 169.250 79.948  1.00 12.30  ? 47   PHE C N     1 
ATOM   20777 C  CA    . PHE C 3  47   ? 120.603 168.276 78.871  1.00 13.89  ? 47   PHE C CA    1 
ATOM   20778 C  C     . PHE C 3  47   ? 119.200 167.874 78.442  1.00 15.15  ? 47   PHE C C     1 
ATOM   20779 O  O     . PHE C 3  47   ? 118.296 167.785 79.274  1.00 15.34  ? 47   PHE C O     1 
ATOM   20780 C  CB    . PHE C 3  47   ? 121.383 167.035 79.308  1.00 12.98  ? 47   PHE C CB    1 
ATOM   20781 C  CG    . PHE C 3  47   ? 122.779 167.321 79.772  1.00 13.33  ? 47   PHE C CG    1 
ATOM   20782 C  CD1   . PHE C 3  47   ? 123.015 167.810 81.035  1.00 9.52   ? 47   PHE C CD1   1 
ATOM   20783 C  CD2   . PHE C 3  47   ? 123.854 167.078 78.951  1.00 15.17  ? 47   PHE C CD2   1 
ATOM   20784 C  CE1   . PHE C 3  47   ? 124.288 168.071 81.460  1.00 5.71   ? 47   PHE C CE1   1 
ATOM   20785 C  CE2   . PHE C 3  47   ? 125.127 167.347 79.373  1.00 10.58  ? 47   PHE C CE2   1 
ATOM   20786 C  CZ    . PHE C 3  47   ? 125.341 167.838 80.631  1.00 7.47   ? 47   PHE C CZ    1 
ATOM   20787 N  N     . LYS C 3  48   ? 119.009 167.652 77.146  1.00 12.92  ? 48   LYS C N     1 
ATOM   20788 C  CA    . LYS C 3  48   ? 117.715 167.245 76.623  1.00 7.99   ? 48   LYS C CA    1 
ATOM   20789 C  C     . LYS C 3  48   ? 117.883 166.119 75.620  1.00 10.25  ? 48   LYS C C     1 
ATOM   20790 O  O     . LYS C 3  48   ? 118.886 166.055 74.911  1.00 17.26  ? 48   LYS C O     1 
ATOM   20791 C  CB    . LYS C 3  48   ? 116.991 168.412 75.979  1.00 11.52  ? 48   LYS C CB    1 
ATOM   20792 C  CG    . LYS C 3  48   ? 115.506 168.225 75.908  1.00 16.69  ? 48   LYS C CG    1 
ATOM   20793 C  CD    . LYS C 3  48   ? 114.819 169.484 75.471  1.00 16.26  ? 48   LYS C CD    1 
ATOM   20794 C  CE    . LYS C 3  48   ? 113.315 169.317 75.495  1.00 16.41  ? 48   LYS C CE    1 
ATOM   20795 N  NZ    . LYS C 3  48   ? 112.624 170.555 75.062  1.00 18.98  ? 48   LYS C NZ    1 
ATOM   20796 N  N     . GLY C 3  49   ? 116.895 165.233 75.566  1.00 12.03  ? 49   GLY C N     1 
ATOM   20797 C  CA    . GLY C 3  49   ? 116.932 164.105 74.655  1.00 9.04   ? 49   GLY C CA    1 
ATOM   20798 C  C     . GLY C 3  49   ? 118.043 163.122 74.932  1.00 12.94  ? 49   GLY C C     1 
ATOM   20799 O  O     . GLY C 3  49   ? 118.723 162.684 74.000  1.00 22.07  ? 49   GLY C O     1 
ATOM   20800 N  N     . ILE C 3  50   ? 118.246 162.760 76.193  1.00 16.33  ? 50   ILE C N     1 
ATOM   20801 C  CA    . ILE C 3  50   ? 119.374 161.928 76.584  1.00 15.52  ? 50   ILE C CA    1 
ATOM   20802 C  C     . ILE C 3  50   ? 118.977 161.135 77.818  1.00 11.09  ? 50   ILE C C     1 
ATOM   20803 O  O     . ILE C 3  50   ? 118.170 161.585 78.630  1.00 14.19  ? 50   ILE C O     1 
ATOM   20804 C  CB    . ILE C 3  50   ? 120.628 162.796 76.829  1.00 12.42  ? 50   ILE C CB    1 
ATOM   20805 C  CG1   . ILE C 3  50   ? 121.876 161.937 76.960  1.00 10.25  ? 50   ILE C CG1   1 
ATOM   20806 C  CG2   . ILE C 3  50   ? 120.440 163.665 78.032  1.00 14.01  ? 50   ILE C CG2   1 
ATOM   20807 C  CD1   . ILE C 3  50   ? 123.127 162.731 77.002  1.00 15.51  ? 50   ILE C CD1   1 
ATOM   20808 N  N     . SER C 3  51   ? 119.528 159.936 77.947  1.00 10.04  ? 51   SER C N     1 
ATOM   20809 C  CA    . SER C 3  51   ? 119.247 159.104 79.104  1.00 9.79   ? 51   SER C CA    1 
ATOM   20810 C  C     . SER C 3  51   ? 120.031 159.582 80.315  1.00 8.80   ? 51   SER C C     1 
ATOM   20811 O  O     . SER C 3  51   ? 121.046 160.268 80.193  1.00 12.14  ? 51   SER C O     1 
ATOM   20812 C  CB    . SER C 3  51   ? 119.584 157.645 78.816  1.00 8.01   ? 51   SER C CB    1 
ATOM   20813 O  OG    . SER C 3  51   ? 120.956 157.486 78.528  1.00 12.26  ? 51   SER C OG    1 
ATOM   20814 N  N     . ARG C 3  52   ? 119.542 159.222 81.501  1.00 12.38  ? 52   ARG C N     1 
ATOM   20815 C  CA    . ARG C 3  52   ? 120.288 159.559 82.699  1.00 4.07   ? 52   ARG C CA    1 
ATOM   20816 C  C     . ARG C 3  52   ? 121.494 158.665 82.898  1.00 3.25   ? 52   ARG C C     1 
ATOM   20817 O  O     . ARG C 3  52   ? 122.353 158.998 83.710  1.00 8.47   ? 52   ARG C O     1 
ATOM   20818 C  CB    . ARG C 3  52   ? 119.402 159.504 83.935  1.00 1.46   ? 52   ARG C CB    1 
ATOM   20819 C  CG    . ARG C 3  52   ? 119.082 158.131 84.393  1.00 3.93   ? 52   ARG C CG    1 
ATOM   20820 C  CD    . ARG C 3  52   ? 118.125 158.169 85.541  1.00 10.01  ? 52   ARG C CD    1 
ATOM   20821 N  NE    . ARG C 3  52   ? 117.240 157.018 85.472  1.00 8.40   ? 52   ARG C NE    1 
ATOM   20822 C  CZ    . ARG C 3  52   ? 116.101 156.905 86.132  1.00 8.07   ? 52   ARG C CZ    1 
ATOM   20823 N  NH1   . ARG C 3  52   ? 115.691 157.841 86.965  1.00 9.19   ? 52   ARG C NH1   1 
ATOM   20824 N  NH2   . ARG C 3  52   ? 115.343 155.837 85.931  1.00 8.51   ? 52   ARG C NH2   1 
ATOM   20825 N  N     . ALA C 3  53   ? 121.596 157.554 82.176  1.00 1.39   ? 53   ALA C N     1 
ATOM   20826 C  CA    . ALA C 3  53   ? 122.843 156.806 82.181  1.00 11.79  ? 53   ALA C CA    1 
ATOM   20827 C  C     . ALA C 3  53   ? 123.984 157.664 81.663  1.00 8.78   ? 53   ALA C C     1 
ATOM   20828 O  O     . ALA C 3  53   ? 125.064 157.691 82.255  1.00 10.99  ? 53   ALA C O     1 
ATOM   20829 C  CB    . ALA C 3  53   ? 122.703 155.541 81.347  1.00 0.55   ? 53   ALA C CB    1 
ATOM   20830 N  N     . ALA C 3  54   ? 123.743 158.414 80.588  1.00 10.41  ? 54   ALA C N     1 
ATOM   20831 C  CA    . ALA C 3  54   ? 124.782 159.242 79.989  1.00 0.81   ? 54   ALA C CA    1 
ATOM   20832 C  C     . ALA C 3  54   ? 125.112 160.454 80.855  1.00 3.90   ? 54   ALA C C     1 
ATOM   20833 O  O     . ALA C 3  54   ? 126.286 160.764 81.080  1.00 14.50  ? 54   ALA C O     1 
ATOM   20834 C  CB    . ALA C 3  54   ? 124.341 159.678 78.598  1.00 3.08   ? 54   ALA C CB    1 
ATOM   20835 N  N     . VAL C 3  55   ? 124.089 161.154 81.345  1.00 4.40   ? 55   VAL C N     1 
ATOM   20836 C  CA    . VAL C 3  55   ? 124.307 162.333 82.176  1.00 2.28   ? 55   VAL C CA    1 
ATOM   20837 C  C     . VAL C 3  55   ? 124.962 161.949 83.498  1.00 3.86   ? 55   VAL C C     1 
ATOM   20838 O  O     . VAL C 3  55   ? 125.897 162.611 83.965  1.00 11.05  ? 55   VAL C O     1 
ATOM   20839 C  CB    . VAL C 3  55   ? 122.974 163.074 82.390  1.00 3.14   ? 55   VAL C CB    1 
ATOM   20840 C  CG1   . VAL C 3  55   ? 123.153 164.280 83.283  1.00 2.73   ? 55   VAL C CG1   1 
ATOM   20841 C  CG2   . VAL C 3  55   ? 122.402 163.495 81.073  1.00 5.93   ? 55   VAL C CG2   1 
ATOM   20842 N  N     . HIS C 3  56   ? 124.495 160.869 84.119  1.00 5.91   ? 56   HIS C N     1 
ATOM   20843 C  CA    . HIS C 3  56   ? 125.101 160.438 85.366  1.00 9.43   ? 56   HIS C CA    1 
ATOM   20844 C  C     . HIS C 3  56   ? 126.492 159.853 85.163  1.00 1.05   ? 56   HIS C C     1 
ATOM   20845 O  O     . HIS C 3  56   ? 127.345 160.010 86.034  1.00 7.08   ? 56   HIS C O     1 
ATOM   20846 C  CB    . HIS C 3  56   ? 124.208 159.437 86.083  1.00 14.34  ? 56   HIS C CB    1 
ATOM   20847 C  CG    . HIS C 3  56   ? 124.653 159.147 87.477  1.00 14.87  ? 56   HIS C CG    1 
ATOM   20848 N  ND1   . HIS C 3  56   ? 124.704 160.113 88.452  1.00 13.88  ? 56   HIS C ND1   1 
ATOM   20849 C  CD2   . HIS C 3  56   ? 125.108 158.011 88.050  1.00 0.46   ? 56   HIS C CD2   1 
ATOM   20850 C  CE1   . HIS C 3  56   ? 125.153 159.581 89.571  1.00 11.08  ? 56   HIS C CE1   1 
ATOM   20851 N  NE2   . HIS C 3  56   ? 125.405 158.306 89.353  1.00 3.11   ? 56   HIS C NE2   1 
ATOM   20852 N  N     . GLY C 3  57   ? 126.755 159.185 84.040  1.00 11.81  ? 57   GLY C N     1 
ATOM   20853 C  CA    . GLY C 3  57   ? 128.109 158.752 83.765  1.00 11.09  ? 57   GLY C CA    1 
ATOM   20854 C  C     . GLY C 3  57   ? 129.054 159.918 83.575  1.00 0.91   ? 57   GLY C C     1 
ATOM   20855 O  O     . GLY C 3  57   ? 130.183 159.899 84.068  1.00 11.96  ? 57   GLY C O     1 
ATOM   20856 N  N     . LEU C 3  58   ? 128.596 160.956 82.875  1.00 13.60  ? 58   LEU C N     1 
ATOM   20857 C  CA    . LEU C 3  58   ? 129.377 162.179 82.757  1.00 3.74   ? 58   LEU C CA    1 
ATOM   20858 C  C     . LEU C 3  58   ? 129.677 162.782 84.121  1.00 0.73   ? 58   LEU C C     1 
ATOM   20859 O  O     . LEU C 3  58   ? 130.816 163.175 84.398  1.00 6.79   ? 58   LEU C O     1 
ATOM   20860 C  CB    . LEU C 3  58   ? 128.627 163.175 81.883  1.00 4.37   ? 58   LEU C CB    1 
ATOM   20861 C  CG    . LEU C 3  58   ? 129.280 164.506 81.547  1.00 2.75   ? 58   LEU C CG    1 
ATOM   20862 C  CD1   . LEU C 3  58   ? 130.374 164.314 80.542  1.00 6.30   ? 58   LEU C CD1   1 
ATOM   20863 C  CD2   . LEU C 3  58   ? 128.233 165.438 81.009  1.00 3.28   ? 58   LEU C CD2   1 
ATOM   20864 N  N     . SER C 3  59   ? 128.671 162.853 84.990  1.00 8.94   ? 59   SER C N     1 
ATOM   20865 C  CA    . SER C 3  59   ? 128.880 163.395 86.328  1.00 15.20  ? 59   SER C CA    1 
ATOM   20866 C  C     . SER C 3  59   ? 129.869 162.556 87.130  1.00 5.91   ? 59   SER C C     1 
ATOM   20867 O  O     . SER C 3  59   ? 130.736 163.102 87.818  1.00 2.09   ? 59   SER C O     1 
ATOM   20868 C  CB    . SER C 3  59   ? 127.544 163.492 87.052  1.00 5.27   ? 59   SER C CB    1 
ATOM   20869 O  OG    . SER C 3  59   ? 127.707 163.788 88.420  1.00 3.00   ? 59   SER C OG    1 
ATOM   20870 N  N     . ARG C 3  60   ? 129.755 161.229 87.058  1.00 3.34   ? 60   ARG C N     1 
ATOM   20871 C  CA    . ARG C 3  60   ? 130.656 160.353 87.799  1.00 1.52   ? 60   ARG C CA    1 
ATOM   20872 C  C     . ARG C 3  60   ? 132.095 160.505 87.336  1.00 0.97   ? 60   ARG C C     1 
ATOM   20873 O  O     . ARG C 3  60   ? 133.027 160.509 88.153  1.00 3.14   ? 60   ARG C O     1 
ATOM   20874 C  CB    . ARG C 3  60   ? 130.220 158.902 87.643  1.00 11.56  ? 60   ARG C CB    1 
ATOM   20875 C  CG    . ARG C 3  60   ? 128.969 158.521 88.365  1.00 7.96   ? 60   ARG C CG    1 
ATOM   20876 C  CD    . ARG C 3  60   ? 128.539 157.141 87.958  1.00 6.53   ? 60   ARG C CD    1 
ATOM   20877 N  NE    . ARG C 3  60   ? 129.607 156.178 88.183  1.00 7.30   ? 60   ARG C NE    1 
ATOM   20878 C  CZ    . ARG C 3  60   ? 129.729 155.417 89.259  1.00 4.69   ? 60   ARG C CZ    1 
ATOM   20879 N  NH1   . ARG C 3  60   ? 128.825 155.421 90.213  1.00 3.63   ? 60   ARG C NH1   1 
ATOM   20880 N  NH2   . ARG C 3  60   ? 130.787 154.629 89.378  1.00 2.96   ? 60   ARG C NH2   1 
ATOM   20881 N  N     . VAL C 3  61   ? 132.298 160.590 86.022  1.00 3.77   ? 61   VAL C N     1 
ATOM   20882 C  CA    . VAL C 3  61   ? 133.641 160.776 85.488  1.00 0.71   ? 61   VAL C CA    1 
ATOM   20883 C  C     . VAL C 3  61   ? 134.203 162.119 85.926  1.00 1.04   ? 61   VAL C C     1 
ATOM   20884 O  O     . VAL C 3  61   ? 135.361 162.220 86.337  1.00 8.67   ? 61   VAL C O     1 
ATOM   20885 C  CB    . VAL C 3  61   ? 133.634 160.637 83.958  1.00 1.17   ? 61   VAL C CB    1 
ATOM   20886 C  CG1   . VAL C 3  61   ? 134.943 161.123 83.383  1.00 4.65   ? 61   VAL C CG1   1 
ATOM   20887 C  CG2   . VAL C 3  61   ? 133.381 159.209 83.568  1.00 2.14   ? 61   VAL C CG2   1 
ATOM   20888 N  N     . LEU C 3  62   ? 133.394 163.173 85.857  1.00 1.00   ? 62   LEU C N     1 
ATOM   20889 C  CA    . LEU C 3  62   ? 133.878 164.476 86.291  1.00 6.46   ? 62   LEU C CA    1 
ATOM   20890 C  C     . LEU C 3  62   ? 134.144 164.528 87.788  1.00 2.99   ? 62   LEU C C     1 
ATOM   20891 O  O     . LEU C 3  62   ? 134.951 165.348 88.228  1.00 10.02  ? 62   LEU C O     1 
ATOM   20892 C  CB    . LEU C 3  62   ? 132.882 165.558 85.898  1.00 5.15   ? 62   LEU C CB    1 
ATOM   20893 C  CG    . LEU C 3  62   ? 132.950 166.055 84.461  1.00 2.23   ? 62   LEU C CG    1 
ATOM   20894 C  CD1   . LEU C 3  62   ? 131.741 166.884 84.142  1.00 1.19   ? 62   LEU C CD1   1 
ATOM   20895 C  CD2   . LEU C 3  62   ? 134.204 166.862 84.255  1.00 14.64  ? 62   LEU C CD2   1 
ATOM   20896 N  N     . GLN C 3  63   ? 133.489 163.684 88.581  1.00 4.51   ? 63   GLN C N     1 
ATOM   20897 C  CA    . GLN C 3  63   ? 133.799 163.636 90.007  1.00 15.22  ? 63   GLN C CA    1 
ATOM   20898 C  C     . GLN C 3  63   ? 135.126 162.937 90.258  1.00 0.60   ? 63   GLN C C     1 
ATOM   20899 O  O     . GLN C 3  63   ? 136.062 163.541 90.783  1.00 6.12   ? 63   GLN C O     1 
ATOM   20900 C  CB    . GLN C 3  63   ? 132.695 162.923 90.787  1.00 14.20  ? 63   GLN C CB    1 
ATOM   20901 C  CG    . GLN C 3  63   ? 131.399 163.652 90.907  1.00 9.09   ? 63   GLN C CG    1 
ATOM   20902 C  CD    . GLN C 3  63   ? 130.309 162.726 91.358  1.00 1.32   ? 63   GLN C CD    1 
ATOM   20903 O  OE1   . GLN C 3  63   ? 130.531 161.870 92.192  1.00 5.78   ? 63   GLN C OE1   1 
ATOM   20904 N  NE2   . GLN C 3  63   ? 129.144 162.853 90.769  1.00 1.81   ? 63   GLN C NE2   1 
ATOM   20905 N  N     . ASP C 3  64   ? 135.223 161.646 89.922  1.00 3.32   ? 64   ASP C N     1 
ATOM   20906 C  CA    . ASP C 3  64   ? 136.425 160.957 90.377  1.00 0.15   ? 64   ASP C CA    1 
ATOM   20907 C  C     . ASP C 3  64   ? 136.924 159.878 89.422  1.00 7.64   ? 64   ASP C C     1 
ATOM   20908 O  O     . ASP C 3  64   ? 137.477 158.869 89.866  1.00 6.23   ? 64   ASP C O     1 
ATOM   20909 C  CB    . ASP C 3  64   ? 136.223 160.394 91.788  1.00 6.43   ? 64   ASP C CB    1 
ATOM   20910 C  CG    . ASP C 3  64   ? 135.253 159.238 91.849  1.00 6.12   ? 64   ASP C CG    1 
ATOM   20911 O  OD1   . ASP C 3  64   ? 134.673 158.856 90.823  1.00 18.64  ? 64   ASP C OD1   1 
ATOM   20912 O  OD2   . ASP C 3  64   ? 135.075 158.695 92.951  1.00 3.85   ? 64   ASP C OD2   1 
ATOM   20913 N  N     . GLU C 3  65   ? 136.768 160.066 88.116  1.00 5.05   ? 65   GLU C N     1 
ATOM   20914 C  CA    . GLU C 3  65   ? 137.323 159.117 87.159  1.00 2.51   ? 65   GLU C CA    1 
ATOM   20915 C  C     . GLU C 3  65   ? 138.061 159.816 86.029  1.00 5.65   ? 65   GLU C C     1 
ATOM   20916 O  O     . GLU C 3  65   ? 138.330 159.202 85.000  1.00 12.56  ? 65   GLU C O     1 
ATOM   20917 C  CB    . GLU C 3  65   ? 136.228 158.212 86.602  1.00 3.15   ? 65   GLU C CB    1 
ATOM   20918 C  CG    . GLU C 3  65   ? 135.619 157.326 87.652  1.00 5.81   ? 65   GLU C CG    1 
ATOM   20919 C  CD    . GLU C 3  65   ? 134.399 156.602 87.174  1.00 11.96  ? 65   GLU C CD    1 
ATOM   20920 O  OE1   . GLU C 3  65   ? 134.057 156.730 85.988  1.00 14.26  ? 65   GLU C OE1   1 
ATOM   20921 O  OE2   . GLU C 3  65   ? 133.783 155.900 87.988  1.00 15.29  ? 65   GLU C OE2   1 
ATOM   20922 N  N     . ILE C 3  66   ? 138.408 161.081 86.219  1.00 6.31   ? 66   ILE C N     1 
ATOM   20923 C  CA    . ILE C 3  66   ? 139.116 161.897 85.242  1.00 1.92   ? 66   ILE C CA    1 
ATOM   20924 C  C     . ILE C 3  66   ? 140.537 162.087 85.759  1.00 8.66   ? 66   ILE C C     1 
ATOM   20925 O  O     . ILE C 3  66   ? 140.731 162.247 86.971  1.00 12.44  ? 66   ILE C O     1 
ATOM   20926 C  CB    . ILE C 3  66   ? 138.381 163.231 85.030  1.00 2.43   ? 66   ILE C CB    1 
ATOM   20927 C  CG1   . ILE C 3  66   ? 139.064 164.092 83.981  1.00 7.89   ? 66   ILE C CG1   1 
ATOM   20928 C  CG2   . ILE C 3  66   ? 138.245 163.984 86.334  1.00 0.88   ? 66   ILE C CG2   1 
ATOM   20929 C  CD1   . ILE C 3  66   ? 138.281 165.310 83.641  1.00 7.62   ? 66   ILE C CD1   1 
ATOM   20930 N  N     . PRO C 3  67   ? 141.558 162.012 84.908  1.00 11.88  ? 67   PRO C N     1 
ATOM   20931 C  CA    . PRO C 3  67   ? 142.924 162.281 85.374  1.00 5.39   ? 67   PRO C CA    1 
ATOM   20932 C  C     . PRO C 3  67   ? 143.081 163.702 85.896  1.00 7.64   ? 67   PRO C C     1 
ATOM   20933 O  O     . PRO C 3  67   ? 142.639 164.666 85.275  1.00 8.63   ? 67   PRO C O     1 
ATOM   20934 C  CB    . PRO C 3  67   ? 143.768 162.037 84.126  1.00 6.65   ? 67   PRO C CB    1 
ATOM   20935 C  CG    . PRO C 3  67   ? 142.980 161.070 83.351  1.00 5.95   ? 67   PRO C CG    1 
ATOM   20936 C  CD    . PRO C 3  67   ? 141.552 161.408 83.568  1.00 7.04   ? 67   PRO C CD    1 
ATOM   20937 N  N     . ASN C 3  68   ? 143.744 163.819 87.041  1.00 6.14   ? 68   ASN C N     1 
ATOM   20938 C  CA    . ASN C 3  68   ? 143.886 165.071 87.763  1.00 1.78   ? 68   ASN C CA    1 
ATOM   20939 C  C     . ASN C 3  68   ? 145.272 165.107 88.381  1.00 4.05   ? 68   ASN C C     1 
ATOM   20940 O  O     . ASN C 3  68   ? 146.009 164.126 88.346  1.00 6.56   ? 68   ASN C O     1 
ATOM   20941 C  CB    . ASN C 3  68   ? 142.797 165.221 88.833  1.00 2.53   ? 68   ASN C CB    1 
ATOM   20942 C  CG    . ASN C 3  68   ? 142.493 166.661 89.165  1.00 2.22   ? 68   ASN C CG    1 
ATOM   20943 O  OD1   . ASN C 3  68   ? 142.866 167.574 88.439  1.00 8.07   ? 68   ASN C OD1   1 
ATOM   20944 N  ND2   . ASN C 3  68   ? 141.836 166.870 90.285  1.00 3.53   ? 68   ASN C ND2   1 
ATOM   20945 N  N     . TYR C 3  69   ? 145.623 166.248 88.965  1.00 12.74  ? 69   TYR C N     1 
ATOM   20946 C  CA    . TYR C 3  69   ? 146.959 166.500 89.482  1.00 3.23   ? 69   TYR C CA    1 
ATOM   20947 C  C     . TYR C 3  69   ? 146.904 166.937 90.933  1.00 6.86   ? 69   TYR C C     1 
ATOM   20948 O  O     . TYR C 3  69   ? 145.943 167.574 91.364  1.00 12.39  ? 69   TYR C O     1 
ATOM   20949 C  CB    . TYR C 3  69   ? 147.659 167.571 88.672  1.00 3.10   ? 69   TYR C CB    1 
ATOM   20950 C  CG    . TYR C 3  69   ? 147.949 167.147 87.269  1.00 12.44  ? 69   TYR C CG    1 
ATOM   20951 C  CD1   . TYR C 3  69   ? 148.952 166.237 87.002  1.00 12.59  ? 69   TYR C CD1   1 
ATOM   20952 C  CD2   . TYR C 3  69   ? 147.209 167.634 86.214  1.00 11.67  ? 69   TYR C CD2   1 
ATOM   20953 C  CE1   . TYR C 3  69   ? 149.218 165.837 85.731  1.00 13.79  ? 69   TYR C CE1   1 
ATOM   20954 C  CE2   . TYR C 3  69   ? 147.472 167.236 84.932  1.00 14.01  ? 69   TYR C CE2   1 
ATOM   20955 C  CZ    . TYR C 3  69   ? 148.480 166.337 84.696  1.00 18.86  ? 69   TYR C CZ    1 
ATOM   20956 O  OH    . TYR C 3  69   ? 148.758 165.932 83.412  1.00 26.58  ? 69   TYR C OH    1 
ATOM   20957 N  N     . MET C 3  70   ? 147.952 166.615 91.674  1.00 5.95   ? 70   MET C N     1 
ATOM   20958 C  CA    . MET C 3  70   ? 148.091 167.015 93.060  1.00 5.19   ? 70   MET C CA    1 
ATOM   20959 C  C     . MET C 3  70   ? 149.566 167.203 93.371  1.00 4.42   ? 70   MET C C     1 
ATOM   20960 O  O     . MET C 3  70   ? 150.437 166.781 92.619  1.00 9.02   ? 70   MET C O     1 
ATOM   20961 C  CB    . MET C 3  70   ? 147.459 165.988 94.009  1.00 0.52   ? 70   MET C CB    1 
ATOM   20962 C  CG    . MET C 3  70   ? 148.272 164.737 94.204  1.00 1.14   ? 70   MET C CG    1 
ATOM   20963 S  SD    . MET C 3  70   ? 148.054 164.073 95.841  1.00 14.20  ? 70   MET C SD    1 
ATOM   20964 C  CE    . MET C 3  70   ? 148.854 162.499 95.708  1.00 11.22  ? 70   MET C CE    1 
ATOM   20965 N  N     . LEU C 3  71   ? 149.839 167.850 94.494  1.00 4.05   ? 71   LEU C N     1 
ATOM   20966 C  CA    . LEU C 3  71   ? 151.194 168.042 94.988  1.00 14.89  ? 71   LEU C CA    1 
ATOM   20967 C  C     . LEU C 3  71   ? 151.531 166.904 95.938  1.00 7.94   ? 71   LEU C C     1 
ATOM   20968 O  O     . LEU C 3  71   ? 150.751 166.594 96.837  1.00 11.81  ? 71   LEU C O     1 
ATOM   20969 C  CB    . LEU C 3  71   ? 151.329 169.380 95.711  1.00 10.56  ? 71   LEU C CB    1 
ATOM   20970 C  CG    . LEU C 3  71   ? 151.227 170.700 94.959  1.00 5.27   ? 71   LEU C CG    1 
ATOM   20971 C  CD1   . LEU C 3  71   ? 151.161 171.824 95.961  1.00 5.29   ? 71   LEU C CD1   1 
ATOM   20972 C  CD2   . LEU C 3  71   ? 152.378 170.890 94.016  1.00 6.72   ? 71   LEU C CD2   1 
ATOM   20973 N  N     . ASP C 3  72   ? 152.691 166.291 95.746  1.00 6.55   ? 72   ASP C N     1 
ATOM   20974 C  CA    . ASP C 3  72   ? 153.160 165.240 96.631  1.00 5.02   ? 72   ASP C CA    1 
ATOM   20975 C  C     . ASP C 3  72   ? 154.607 165.496 97.030  1.00 13.46  ? 72   ASP C C     1 
ATOM   20976 O  O     . ASP C 3  72   ? 155.266 166.386 96.501  1.00 20.71  ? 72   ASP C O     1 
ATOM   20977 C  CB    . ASP C 3  72   ? 153.013 163.868 95.978  1.00 7.77   ? 72   ASP C CB    1 
ATOM   20978 C  CG    . ASP C 3  72   ? 152.865 162.765 96.990  1.00 15.35  ? 72   ASP C CG    1 
ATOM   20979 O  OD1   . ASP C 3  72   ? 152.839 163.062 98.196  1.00 20.92  ? 72   ASP C OD1   1 
ATOM   20980 O  OD2   . ASP C 3  72   ? 152.758 161.597 96.589  1.00 19.59  ? 72   ASP C OD2   1 
ATOM   20981 N  N     . ILE C 3  73   ? 155.086 164.717 97.993  1.00 12.62  ? 73   ILE C N     1 
ATOM   20982 C  CA    . ILE C 3  73   ? 156.459 164.800 98.480  1.00 12.41  ? 73   ILE C CA    1 
ATOM   20983 C  C     . ILE C 3  73   ? 157.200 163.541 98.057  1.00 15.26  ? 73   ILE C C     1 
ATOM   20984 O  O     . ILE C 3  73   ? 156.753 162.425 98.340  1.00 23.48  ? 73   ILE C O     1 
ATOM   20985 C  CB    . ILE C 3  73   ? 156.504 164.963 100.009 1.00 13.42  ? 73   ILE C CB    1 
ATOM   20986 C  CG1   . ILE C 3  73   ? 155.637 166.131 100.469 1.00 15.93  ? 73   ILE C CG1   1 
ATOM   20987 C  CG2   . ILE C 3  73   ? 157.912 165.181 100.472 1.00 11.31  ? 73   ILE C CG2   1 
ATOM   20988 C  CD1   . ILE C 3  73   ? 155.431 166.177 101.959 1.00 12.33  ? 73   ILE C CD1   1 
ATOM   20989 N  N     . LYS C 3  74   ? 158.332 163.710 97.386  1.00 19.86  ? 74   LYS C N     1 
ATOM   20990 C  CA    . LYS C 3  74   ? 159.149 162.563 97.034  1.00 23.88  ? 74   LYS C CA    1 
ATOM   20991 C  C     . LYS C 3  74   ? 159.787 161.960 98.283  1.00 30.17  ? 74   LYS C C     1 
ATOM   20992 O  O     . LYS C 3  74   ? 160.025 162.661 99.268  1.00 34.19  ? 74   LYS C O     1 
ATOM   20993 C  CB    . LYS C 3  74   ? 160.231 162.959 96.040  1.00 21.82  ? 74   LYS C CB    1 
ATOM   20994 C  CG    . LYS C 3  74   ? 159.747 162.923 94.625  1.00 24.08  ? 74   LYS C CG    1 
ATOM   20995 C  CD    . LYS C 3  74   ? 160.853 163.174 93.643  1.00 28.21  ? 74   LYS C CD    1 
ATOM   20996 C  CE    . LYS C 3  74   ? 160.279 163.265 92.250  1.00 31.69  ? 74   LYS C CE    1 
ATOM   20997 N  NZ    . LYS C 3  74   ? 159.506 162.036 91.920  1.00 27.79  ? 74   LYS C NZ    1 
ATOM   20998 N  N     . PRO C 3  75   ? 160.057 160.657 98.275  1.00 31.42  ? 75   PRO C N     1 
ATOM   20999 C  CA    . PRO C 3  75   ? 160.684 160.028 99.443  1.00 28.07  ? 75   PRO C CA    1 
ATOM   21000 C  C     . PRO C 3  75   ? 162.041 160.644 99.755  1.00 28.37  ? 75   PRO C C     1 
ATOM   21001 O  O     . PRO C 3  75   ? 162.844 160.919 98.862  1.00 25.15  ? 75   PRO C O     1 
ATOM   21002 C  CB    . PRO C 3  75   ? 160.802 158.558 99.035  1.00 25.73  ? 75   PRO C CB    1 
ATOM   21003 C  CG    . PRO C 3  75   ? 160.617 158.535 97.565  1.00 28.86  ? 75   PRO C CG    1 
ATOM   21004 C  CD    . PRO C 3  75   ? 159.737 159.679 97.226  1.00 27.66  ? 75   PRO C CD    1 
ATOM   21005 N  N     . GLY C 3  76   ? 162.288 160.867 101.041 1.00 24.03  ? 76   GLY C N     1 
ATOM   21006 C  CA    . GLY C 3  76   ? 163.471 161.566 101.474 1.00 22.42  ? 76   GLY C CA    1 
ATOM   21007 C  C     . GLY C 3  76   ? 163.390 163.072 101.394 1.00 25.89  ? 76   GLY C C     1 
ATOM   21008 O  O     . GLY C 3  76   ? 164.351 163.744 101.779 1.00 28.73  ? 76   GLY C O     1 
ATOM   21009 N  N     . GLY C 3  77   ? 162.278 163.625 100.905 1.00 26.74  ? 77   GLY C N     1 
ATOM   21010 C  CA    . GLY C 3  77   ? 162.132 165.064 100.808 1.00 18.89  ? 77   GLY C CA    1 
ATOM   21011 C  C     . GLY C 3  77   ? 161.855 165.741 102.128 1.00 20.93  ? 77   GLY C C     1 
ATOM   21012 O  O     . GLY C 3  77   ? 162.177 166.919 102.286 1.00 21.39  ? 77   GLY C O     1 
ATOM   21013 N  N     . TYR C 3  78   ? 161.259 165.027 103.073 1.00 21.81  ? 78   TYR C N     1 
ATOM   21014 C  CA    . TYR C 3  78   ? 161.042 165.540 104.421 1.00 21.17  ? 78   TYR C CA    1 
ATOM   21015 C  C     . TYR C 3  78   ? 162.356 165.407 105.177 1.00 23.50  ? 78   TYR C C     1 
ATOM   21016 O  O     . TYR C 3  78   ? 162.769 164.308 105.544 1.00 25.37  ? 78   TYR C O     1 
ATOM   21017 C  CB    . TYR C 3  78   ? 159.913 164.778 105.101 1.00 18.69  ? 78   TYR C CB    1 
ATOM   21018 C  CG    . TYR C 3  78   ? 159.541 165.290 106.470 1.00 21.79  ? 78   TYR C CG    1 
ATOM   21019 C  CD1   . TYR C 3  78   ? 158.549 166.236 106.631 1.00 20.98  ? 78   TYR C CD1   1 
ATOM   21020 C  CD2   . TYR C 3  78   ? 160.180 164.819 107.601 1.00 21.66  ? 78   TYR C CD2   1 
ATOM   21021 C  CE1   . TYR C 3  78   ? 158.209 166.699 107.875 1.00 19.74  ? 78   TYR C CE1   1 
ATOM   21022 C  CE2   . TYR C 3  78   ? 159.850 165.277 108.840 1.00 16.88  ? 78   TYR C CE2   1 
ATOM   21023 C  CZ    . TYR C 3  78   ? 158.863 166.216 108.975 1.00 19.77  ? 78   TYR C CZ    1 
ATOM   21024 O  OH    . TYR C 3  78   ? 158.528 166.676 110.221 1.00 21.23  ? 78   TYR C OH    1 
ATOM   21025 N  N     . LYS C 3  79   ? 163.031 166.529 105.394 1.00 24.77  ? 79   LYS C N     1 
ATOM   21026 C  CA    . LYS C 3  79   ? 164.369 166.527 105.979 1.00 27.47  ? 79   LYS C CA    1 
ATOM   21027 C  C     . LYS C 3  79   ? 164.259 166.385 107.486 1.00 29.02  ? 79   LYS C C     1 
ATOM   21028 O  O     . LYS C 3  79   ? 164.049 167.361 108.201 1.00 28.78  ? 79   LYS C O     1 
ATOM   21029 C  CB    . LYS C 3  79   ? 165.126 167.790 105.594 1.00 26.38  ? 79   LYS C CB    1 
ATOM   21030 C  CG    . LYS C 3  79   ? 165.308 167.946 104.103 1.00 26.71  ? 79   LYS C CG    1 
ATOM   21031 C  CD    . LYS C 3  79   ? 165.905 166.691 103.512 1.00 26.50  ? 79   LYS C CD    1 
ATOM   21032 C  CE    . LYS C 3  79   ? 166.046 166.797 102.018 1.00 24.85  ? 79   LYS C CE    1 
ATOM   21033 N  NZ    . LYS C 3  79   ? 166.364 165.483 101.415 1.00 28.47  ? 79   LYS C NZ    1 
ATOM   21034 N  N     . ILE C 3  80   ? 164.418 165.151 107.970 1.00 38.76  ? 80   ILE C N     1 
ATOM   21035 C  CA    . ILE C 3  80   ? 164.351 164.860 109.396 1.00 35.49  ? 80   ILE C CA    1 
ATOM   21036 C  C     . ILE C 3  80   ? 165.423 165.573 110.195 1.00 34.84  ? 80   ILE C C     1 
ATOM   21037 O  O     . ILE C 3  80   ? 165.182 165.935 111.348 1.00 36.98  ? 80   ILE C O     1 
ATOM   21038 C  CB    . ILE C 3  80   ? 164.465 163.339 109.621 1.00 35.30  ? 80   ILE C CB    1 
ATOM   21039 C  CG1   . ILE C 3  80   ? 163.380 162.605 108.830 1.00 36.88  ? 80   ILE C CG1   1 
ATOM   21040 C  CG2   . ILE C 3  80   ? 164.379 163.008 111.096 1.00 34.61  ? 80   ILE C CG2   1 
ATOM   21041 C  CD1   . ILE C 3  80   ? 162.966 161.282 109.425 1.00 36.79  ? 80   ILE C CD1   1 
ATOM   21042 N  N     . GLU C 3  81   ? 166.597 165.795 109.608 1.00 39.04  ? 81   GLU C N     1 
ATOM   21043 C  CA    . GLU C 3  81   ? 167.705 166.383 110.349 1.00 43.38  ? 81   GLU C CA    1 
ATOM   21044 C  C     . GLU C 3  81   ? 167.356 167.775 110.858 1.00 39.95  ? 81   GLU C C     1 
ATOM   21045 O  O     . GLU C 3  81   ? 167.501 168.071 112.048 1.00 38.91  ? 81   GLU C O     1 
ATOM   21046 C  CB    . GLU C 3  81   ? 168.957 166.447 109.468 1.00 43.81  ? 81   GLU C CB    1 
ATOM   21047 C  CG    . GLU C 3  81   ? 169.293 165.166 108.739 1.00 45.11  ? 81   GLU C CG    1 
ATOM   21048 C  CD    . GLU C 3  81   ? 168.748 165.150 107.324 1.00 46.65  ? 81   GLU C CD    1 
ATOM   21049 O  OE1   . GLU C 3  81   ? 168.465 166.241 106.786 1.00 43.96  ? 81   GLU C OE1   1 
ATOM   21050 O  OE2   . GLU C 3  81   ? 168.606 164.049 106.750 1.00 48.92  ? 81   GLU C OE2   1 
ATOM   21051 N  N     . ASP C 3  82   ? 166.894 168.639 109.964 1.00 31.99  ? 82   ASP C N     1 
ATOM   21052 C  CA    . ASP C 3  82   ? 166.593 170.021 110.292 1.00 36.42  ? 82   ASP C CA    1 
ATOM   21053 C  C     . ASP C 3  82   ? 165.099 170.307 110.402 1.00 40.38  ? 82   ASP C C     1 
ATOM   21054 O  O     . ASP C 3  82   ? 164.708 171.477 110.414 1.00 38.91  ? 82   ASP C O     1 
ATOM   21055 C  CB    . ASP C 3  82   ? 167.253 170.950 109.272 1.00 35.89  ? 82   ASP C CB    1 
ATOM   21056 C  CG    . ASP C 3  82   ? 167.471 170.283 107.934 1.00 38.65  ? 82   ASP C CG    1 
ATOM   21057 O  OD1   . ASP C 3  82   ? 167.045 169.128 107.775 1.00 39.94  ? 82   ASP C OD1   1 
ATOM   21058 O  OD2   . ASP C 3  82   ? 168.085 170.904 107.046 1.00 41.35  ? 82   ASP C OD2   1 
ATOM   21059 N  N     . SER C 3  83   ? 164.259 169.274 110.476 1.00 36.41  ? 83   SER C N     1 
ATOM   21060 C  CA    . SER C 3  83   ? 162.861 169.430 110.876 1.00 30.99  ? 83   SER C CA    1 
ATOM   21061 C  C     . SER C 3  83   ? 162.765 169.271 112.392 1.00 29.52  ? 83   SER C C     1 
ATOM   21062 O  O     . SER C 3  83   ? 162.329 168.254 112.928 1.00 28.33  ? 83   SER C O     1 
ATOM   21063 C  CB    . SER C 3  83   ? 161.973 168.427 110.155 1.00 31.56  ? 83   SER C CB    1 
ATOM   21064 O  OG    . SER C 3  83   ? 162.011 168.625 108.757 1.00 34.29  ? 83   SER C OG    1 
ATOM   21065 N  N     . THR C 3  84   ? 163.194 170.319 113.083 1.00 25.55  ? 84   THR C N     1 
ATOM   21066 C  CA    . THR C 3  84   ? 163.257 170.277 114.531 1.00 27.18  ? 84   THR C CA    1 
ATOM   21067 C  C     . THR C 3  84   ? 161.885 170.234 115.191 1.00 29.95  ? 84   THR C C     1 
ATOM   21068 O  O     . THR C 3  84   ? 161.793 169.774 116.334 1.00 31.89  ? 84   THR C O     1 
ATOM   21069 C  CB    . THR C 3  84   ? 164.045 171.480 115.047 1.00 27.97  ? 84   THR C CB    1 
ATOM   21070 O  OG1   . THR C 3  84   ? 163.448 172.677 114.553 1.00 32.38  ? 84   THR C OG1   1 
ATOM   21071 C  CG2   . THR C 3  84   ? 165.482 171.429 114.568 1.00 24.01  ? 84   THR C CG2   1 
ATOM   21072 N  N     . ASP C 3  85   ? 160.824 170.690 114.524 1.00 22.93  ? 85   ASP C N     1 
ATOM   21073 C  CA    . ASP C 3  85   ? 159.519 170.713 115.171 1.00 22.06  ? 85   ASP C CA    1 
ATOM   21074 C  C     . ASP C 3  85   ? 158.948 169.307 115.272 1.00 30.30  ? 85   ASP C C     1 
ATOM   21075 O  O     . ASP C 3  85   ? 159.013 168.519 114.326 1.00 30.18  ? 85   ASP C O     1 
ATOM   21076 C  CB    . ASP C 3  85   ? 158.544 171.621 114.431 1.00 20.75  ? 85   ASP C CB    1 
ATOM   21077 C  CG    . ASP C 3  85   ? 157.347 172.010 115.291 1.00 27.85  ? 85   ASP C CG    1 
ATOM   21078 O  OD1   . ASP C 3  85   ? 157.467 172.945 116.103 1.00 25.88  ? 85   ASP C OD1   1 
ATOM   21079 O  OD2   . ASP C 3  85   ? 156.284 171.375 115.171 1.00 29.65  ? 85   ASP C OD2   1 
ATOM   21080 N  N     . LEU C 3  86   ? 158.379 169.001 116.432 1.00 31.11  ? 86   LEU C N     1 
ATOM   21081 C  CA    . LEU C 3  86   ? 157.946 167.652 116.754 1.00 28.44  ? 86   LEU C CA    1 
ATOM   21082 C  C     . LEU C 3  86   ? 156.466 167.416 116.515 1.00 26.14  ? 86   LEU C C     1 
ATOM   21083 O  O     . LEU C 3  86   ? 156.059 166.265 116.351 1.00 30.12  ? 86   LEU C O     1 
ATOM   21084 C  CB    . LEU C 3  86   ? 158.285 167.335 118.213 1.00 30.43  ? 86   LEU C CB    1 
ATOM   21085 C  CG    . LEU C 3  86   ? 159.722 167.673 118.617 1.00 30.60  ? 86   LEU C CG    1 
ATOM   21086 C  CD1   . LEU C 3  86   ? 159.888 167.658 120.116 1.00 31.50  ? 86   LEU C CD1   1 
ATOM   21087 C  CD2   . LEU C 3  86   ? 160.679 166.697 117.978 1.00 27.62  ? 86   LEU C CD2   1 
ATOM   21088 N  N     . PHE C 3  87   ? 155.652 168.468 116.494 1.00 22.28  ? 87   PHE C N     1 
ATOM   21089 C  CA    . PHE C 3  87   ? 154.227 168.292 116.256 1.00 22.94  ? 87   PHE C CA    1 
ATOM   21090 C  C     . PHE C 3  87   ? 153.891 168.258 114.773 1.00 23.73  ? 87   PHE C C     1 
ATOM   21091 O  O     . PHE C 3  87   ? 152.899 167.638 114.383 1.00 25.78  ? 87   PHE C O     1 
ATOM   21092 C  CB    . PHE C 3  87   ? 153.443 169.398 116.958 1.00 22.12  ? 87   PHE C CB    1 
ATOM   21093 C  CG    . PHE C 3  87   ? 153.576 169.374 118.449 1.00 21.61  ? 87   PHE C CG    1 
ATOM   21094 C  CD1   . PHE C 3  87   ? 152.791 168.535 119.212 1.00 24.52  ? 87   PHE C CD1   1 
ATOM   21095 C  CD2   . PHE C 3  87   ? 154.492 170.183 119.089 1.00 26.73  ? 87   PHE C CD2   1 
ATOM   21096 C  CE1   . PHE C 3  87   ? 152.913 168.509 120.585 1.00 24.67  ? 87   PHE C CE1   1 
ATOM   21097 C  CE2   . PHE C 3  87   ? 154.618 170.158 120.458 1.00 24.65  ? 87   PHE C CE2   1 
ATOM   21098 C  CZ    . PHE C 3  87   ? 153.826 169.321 121.206 1.00 23.06  ? 87   PHE C CZ    1 
ATOM   21099 N  N     . MET C 3  88   ? 154.697 168.902 113.933 1.00 15.70  ? 88   MET C N     1 
ATOM   21100 C  CA    . MET C 3  88   ? 154.466 168.915 112.490 1.00 11.34  ? 88   MET C CA    1 
ATOM   21101 C  C     . MET C 3  88   ? 155.149 167.705 111.858 1.00 14.21  ? 88   MET C C     1 
ATOM   21102 O  O     . MET C 3  88   ? 156.214 167.788 111.249 1.00 17.96  ? 88   MET C O     1 
ATOM   21103 C  CB    . MET C 3  88   ? 154.959 170.220 111.884 1.00 10.15  ? 88   MET C CB    1 
ATOM   21104 C  CG    . MET C 3  88   ? 154.051 171.428 112.089 1.00 11.41  ? 88   MET C CG    1 
ATOM   21105 S  SD    . MET C 3  88   ? 152.279 171.123 112.000 1.00 29.88  ? 88   MET C SD    1 
ATOM   21106 C  CE    . MET C 3  88   ? 151.824 171.056 113.713 1.00 9.69   ? 88   MET C CE    1 
ATOM   21107 N  N     . THR C 3  89   ? 154.495 166.558 111.999 1.00 11.61  ? 89   THR C N     1 
ATOM   21108 C  CA    . THR C 3  89   ? 155.033 165.310 111.492 1.00 8.80   ? 89   THR C CA    1 
ATOM   21109 C  C     . THR C 3  89   ? 154.837 165.213 109.983 1.00 8.58   ? 89   THR C C     1 
ATOM   21110 O  O     . THR C 3  89   ? 154.111 165.989 109.371 1.00 14.76  ? 89   THR C O     1 
ATOM   21111 C  CB    . THR C 3  89   ? 154.380 164.124 112.191 1.00 9.97   ? 89   THR C CB    1 
ATOM   21112 O  OG1   . THR C 3  89   ? 152.990 164.080 111.869 1.00 11.49  ? 89   THR C OG1   1 
ATOM   21113 C  CG2   . THR C 3  89   ? 154.524 164.264 113.673 1.00 12.64  ? 89   THR C CG2   1 
ATOM   21114 N  N     . GLU C 3  90   ? 155.518 164.242 109.379 1.00 5.47   ? 90   GLU C N     1 
ATOM   21115 C  CA    . GLU C 3  90   ? 155.461 164.093 107.931 1.00 10.75  ? 90   GLU C CA    1 
ATOM   21116 C  C     . GLU C 3  90   ? 154.085 163.653 107.463 1.00 11.36  ? 90   GLU C C     1 
ATOM   21117 O  O     . GLU C 3  90   ? 153.619 164.091 106.409 1.00 12.93  ? 90   GLU C O     1 
ATOM   21118 C  CB    . GLU C 3  90   ? 156.507 163.094 107.458 1.00 12.84  ? 90   GLU C CB    1 
ATOM   21119 C  CG    . GLU C 3  90   ? 156.517 162.912 105.964 1.00 9.88   ? 90   GLU C CG    1 
ATOM   21120 C  CD    . GLU C 3  90   ? 157.522 161.889 105.521 1.00 24.50  ? 90   GLU C CD    1 
ATOM   21121 O  OE1   . GLU C 3  90   ? 158.176 161.292 106.396 1.00 28.67  ? 90   GLU C OE1   1 
ATOM   21122 O  OE2   . GLU C 3  90   ? 157.668 161.678 104.300 1.00 24.77  ? 90   GLU C OE2   1 
ATOM   21123 N  N     . GLN C 3  91   ? 153.433 162.766 108.211 1.00 6.19   ? 91   GLN C N     1 
ATOM   21124 C  CA    . GLN C 3  91   ? 152.107 162.302 107.827 1.00 2.06   ? 91   GLN C CA    1 
ATOM   21125 C  C     . GLN C 3  91   ? 151.115 163.457 107.791 1.00 6.20   ? 91   GLN C C     1 
ATOM   21126 O  O     . GLN C 3  91   ? 150.369 163.624 106.819 1.00 7.00   ? 91   GLN C O     1 
ATOM   21127 C  CB    . GLN C 3  91   ? 151.657 161.217 108.798 1.00 6.69   ? 91   GLN C CB    1 
ATOM   21128 C  CG    . GLN C 3  91   ? 150.346 160.561 108.467 1.00 10.45  ? 91   GLN C CG    1 
ATOM   21129 C  CD    . GLN C 3  91   ? 149.819 159.746 109.617 1.00 14.29  ? 91   GLN C CD    1 
ATOM   21130 O  OE1   . GLN C 3  91   ? 150.475 159.623 110.644 1.00 22.87  ? 91   GLN C OE1   1 
ATOM   21131 N  NE2   . GLN C 3  91   ? 148.623 159.191 109.460 1.00 10.12  ? 91   GLN C NE2   1 
ATOM   21132 N  N     . PHE C 3  92   ? 151.140 164.298 108.824 1.00 6.20   ? 92   PHE C N     1 
ATOM   21133 C  CA    . PHE C 3  92   ? 150.240 165.439 108.914 1.00 2.63   ? 92   PHE C CA    1 
ATOM   21134 C  C     . PHE C 3  92   ? 150.486 166.445 107.792 1.00 3.26   ? 92   PHE C C     1 
ATOM   21135 O  O     . PHE C 3  92   ? 149.551 166.873 107.109 1.00 8.43   ? 92   PHE C O     1 
ATOM   21136 C  CB    . PHE C 3  92   ? 150.409 166.088 110.286 1.00 0.96   ? 92   PHE C CB    1 
ATOM   21137 C  CG    . PHE C 3  92   ? 149.432 167.183 110.574 1.00 6.93   ? 92   PHE C CG    1 
ATOM   21138 C  CD1   . PHE C 3  92   ? 148.121 166.898 110.880 1.00 5.82   ? 92   PHE C CD1   1 
ATOM   21139 C  CD2   . PHE C 3  92   ? 149.835 168.499 110.558 1.00 3.25   ? 92   PHE C CD2   1 
ATOM   21140 C  CE1   . PHE C 3  92   ? 147.237 167.903 111.154 1.00 0.07   ? 92   PHE C CE1   1 
ATOM   21141 C  CE2   . PHE C 3  92   ? 148.953 169.497 110.824 1.00 5.58   ? 92   PHE C CE2   1 
ATOM   21142 C  CZ    . PHE C 3  92   ? 147.653 169.201 111.125 1.00 1.30   ? 92   PHE C CZ    1 
ATOM   21143 N  N     . ILE C 3  93   ? 151.742 166.834 107.585 1.00 5.58   ? 93   ILE C N     1 
ATOM   21144 C  CA    . ILE C 3  93   ? 152.055 167.849 106.585 1.00 3.27   ? 93   ILE C CA    1 
ATOM   21145 C  C     . ILE C 3  93   ? 151.809 167.319 105.180 1.00 4.70   ? 93   ILE C C     1 
ATOM   21146 O  O     . ILE C 3  93   ? 151.342 168.049 104.299 1.00 6.23   ? 93   ILE C O     1 
ATOM   21147 C  CB    . ILE C 3  93   ? 153.500 168.344 106.768 1.00 0.55   ? 93   ILE C CB    1 
ATOM   21148 C  CG1   . ILE C 3  93   ? 153.678 168.934 108.157 1.00 4.48   ? 93   ILE C CG1   1 
ATOM   21149 C  CG2   . ILE C 3  93   ? 153.842 169.384 105.753 1.00 1.79   ? 93   ILE C CG2   1 
ATOM   21150 C  CD1   . ILE C 3  93   ? 152.885 170.166 108.381 1.00 3.75   ? 93   ILE C CD1   1 
ATOM   21151 N  N     . ARG C 3  94   ? 152.117 166.045 104.944 1.00 2.33   ? 94   ARG C N     1 
ATOM   21152 C  CA    . ARG C 3  94   ? 151.853 165.452 103.642 1.00 1.22   ? 94   ARG C CA    1 
ATOM   21153 C  C     . ARG C 3  94   ? 150.363 165.408 103.343 1.00 6.20   ? 94   ARG C C     1 
ATOM   21154 O  O     . ARG C 3  94   ? 149.947 165.687 102.216 1.00 12.67  ? 94   ARG C O     1 
ATOM   21155 C  CB    . ARG C 3  94   ? 152.450 164.053 103.576 1.00 3.01   ? 94   ARG C CB    1 
ATOM   21156 C  CG    . ARG C 3  94   ? 152.203 163.364 102.266 1.00 2.46   ? 94   ARG C CG    1 
ATOM   21157 C  CD    . ARG C 3  94   ? 152.706 161.954 102.282 1.00 5.79   ? 94   ARG C CD    1 
ATOM   21158 N  NE    . ARG C 3  94   ? 153.793 161.757 101.335 1.00 14.99  ? 94   ARG C NE    1 
ATOM   21159 C  CZ    . ARG C 3  94   ? 155.011 161.361 101.674 1.00 18.08  ? 94   ARG C CZ    1 
ATOM   21160 N  NH1   . ARG C 3  94   ? 155.329 161.111 102.930 1.00 15.45  ? 94   ARG C NH1   1 
ATOM   21161 N  NH2   . ARG C 3  94   ? 155.931 161.213 100.728 1.00 11.36  ? 94   ARG C NH2   1 
ATOM   21162 N  N     . ASN C 3  95   ? 149.539 165.056 104.332 1.00 1.54   ? 95   ASN C N     1 
ATOM   21163 C  CA    . ASN C 3  95   ? 148.098 165.074 104.112 1.00 8.46   ? 95   ASN C CA    1 
ATOM   21164 C  C     . ASN C 3  95   ? 147.592 166.486 103.860 1.00 0.76   ? 95   ASN C C     1 
ATOM   21165 O  O     . ASN C 3  95   ? 146.685 166.686 103.051 1.00 7.36   ? 95   ASN C O     1 
ATOM   21166 C  CB    . ASN C 3  95   ? 147.376 164.451 105.299 1.00 3.83   ? 95   ASN C CB    1 
ATOM   21167 C  CG    . ASN C 3  95   ? 146.038 163.858 104.924 1.00 8.59   ? 95   ASN C CG    1 
ATOM   21168 O  OD1   . ASN C 3  95   ? 145.958 162.913 104.148 1.00 5.74   ? 95   ASN C OD1   1 
ATOM   21169 N  ND2   . ASN C 3  95   ? 144.974 164.428 105.463 1.00 8.67   ? 95   ASN C ND2   1 
ATOM   21170 N  N     . ARG C 3  96   ? 148.149 167.480 104.555 1.00 4.88   ? 96   ARG C N     1 
ATOM   21171 C  CA    . ARG C 3  96   ? 147.777 168.863 104.273 1.00 1.67   ? 96   ARG C CA    1 
ATOM   21172 C  C     . ARG C 3  96   ? 148.103 169.239 102.833 1.00 7.91   ? 96   ARG C C     1 
ATOM   21173 O  O     . ARG C 3  96   ? 147.275 169.826 102.134 1.00 6.35   ? 96   ARG C O     1 
ATOM   21174 C  CB    . ARG C 3  96   ? 148.496 169.817 105.224 1.00 3.61   ? 96   ARG C CB    1 
ATOM   21175 C  CG    . ARG C 3  96   ? 148.125 169.720 106.693 1.00 2.66   ? 96   ARG C CG    1 
ATOM   21176 C  CD    . ARG C 3  96   ? 146.725 170.118 106.915 1.00 2.45   ? 96   ARG C CD    1 
ATOM   21177 N  NE    . ARG C 3  96   ? 146.550 171.557 106.986 1.00 13.93  ? 96   ARG C NE    1 
ATOM   21178 C  CZ    . ARG C 3  96   ? 145.606 172.144 107.697 1.00 15.00  ? 96   ARG C CZ    1 
ATOM   21179 N  NH1   . ARG C 3  96   ? 144.738 171.441 108.396 1.00 1.43   ? 96   ARG C NH1   1 
ATOM   21180 N  NH2   . ARG C 3  96   ? 145.509 173.463 107.680 1.00 2.97   ? 96   ARG C NH2   1 
ATOM   21181 N  N     . ILE C 3  97   ? 149.309 168.906 102.374 1.00 0.50   ? 97   ILE C N     1 
ATOM   21182 C  CA    . ILE C 3  97   ? 149.784 169.342 101.064 1.00 1.38   ? 97   ILE C CA    1 
ATOM   21183 C  C     . ILE C 3  97   ? 149.104 168.595 99.927  1.00 0.15   ? 97   ILE C C     1 
ATOM   21184 O  O     . ILE C 3  97   ? 148.872 169.172 98.861  1.00 6.07   ? 97   ILE C O     1 
ATOM   21185 C  CB    . ILE C 3  97   ? 151.314 169.210 100.994 1.00 2.29   ? 97   ILE C CB    1 
ATOM   21186 C  CG1   . ILE C 3  97   ? 151.975 170.278 101.858 1.00 0.83   ? 97   ILE C CG1   1 
ATOM   21187 C  CG2   . ILE C 3  97   ? 151.821 169.322 99.569  1.00 0.12   ? 97   ILE C CG2   1 
ATOM   21188 C  CD1   . ILE C 3  97   ? 153.464 170.201 101.879 1.00 15.06  ? 97   ILE C CD1   1 
ATOM   21189 N  N     . ASN C 3  98   ? 148.769 167.320 100.122 1.00 2.67   ? 98   ASN C N     1 
ATOM   21190 C  CA    . ASN C 3  98   ? 148.150 166.543 99.055  1.00 2.72   ? 98   ASN C CA    1 
ATOM   21191 C  C     . ASN C 3  98   ? 146.813 167.118 98.621  1.00 1.92   ? 98   ASN C C     1 
ATOM   21192 O  O     . ASN C 3  98   ? 146.373 166.873 97.496  1.00 1.23   ? 98   ASN C O     1 
ATOM   21193 C  CB    . ASN C 3  98   ? 147.944 165.100 99.498  1.00 0.54   ? 98   ASN C CB    1 
ATOM   21194 C  CG    . ASN C 3  98   ? 149.204 164.294 99.454  1.00 4.50   ? 98   ASN C CG    1 
ATOM   21195 O  OD1   . ASN C 3  98   ? 150.163 164.658 98.793  1.00 7.17   ? 98   ASN C OD1   1 
ATOM   21196 N  ND2   . ASN C 3  98   ? 149.195 163.162 100.125 1.00 13.22  ? 98   ASN C ND2   1 
ATOM   21197 N  N     . PHE C 3  99   ? 146.144 167.865 99.493  1.00 7.56   ? 99   PHE C N     1 
ATOM   21198 C  CA    . PHE C 3  99   ? 144.766 168.259 99.267  1.00 0.24   ? 99   PHE C CA    1 
ATOM   21199 C  C     . PHE C 3  99   ? 144.605 169.726 98.916  1.00 1.14   ? 99   PHE C C     1 
ATOM   21200 O  O     . PHE C 3  99   ? 143.477 170.197 98.806  1.00 11.80  ? 99   PHE C O     1 
ATOM   21201 C  CB    . PHE C 3  99   ? 143.919 167.908 100.484 1.00 0.81   ? 99   PHE C CB    1 
ATOM   21202 C  CG    . PHE C 3  99   ? 143.541 166.469 100.536 1.00 7.91   ? 99   PHE C CG    1 
ATOM   21203 C  CD1   . PHE C 3  99   ? 142.484 165.996 99.797  1.00 7.34   ? 99   PHE C CD1   1 
ATOM   21204 C  CD2   . PHE C 3  99   ? 144.251 165.585 101.310 1.00 8.32   ? 99   PHE C CD2   1 
ATOM   21205 C  CE1   . PHE C 3  99   ? 142.149 164.688 99.836  1.00 11.64  ? 99   PHE C CE1   1 
ATOM   21206 C  CE2   . PHE C 3  99   ? 143.915 164.273 101.346 1.00 7.52   ? 99   PHE C CE2   1 
ATOM   21207 C  CZ    . PHE C 3  99   ? 142.862 163.825 100.611 1.00 2.79   ? 99   PHE C CZ    1 
ATOM   21208 N  N     . ILE C 3  100  ? 145.693 170.452 98.714  1.00 4.89   ? 100  ILE C N     1 
ATOM   21209 C  CA    . ILE C 3  100  ? 145.610 171.806 98.183  1.00 0.07   ? 100  ILE C CA    1 
ATOM   21210 C  C     . ILE C 3  100  ? 145.184 171.697 96.725  1.00 2.20   ? 100  ILE C C     1 
ATOM   21211 O  O     . ILE C 3  100  ? 145.816 170.960 95.959  1.00 8.08   ? 100  ILE C O     1 
ATOM   21212 C  CB    . ILE C 3  100  ? 146.947 172.546 98.321  1.00 0.28   ? 100  ILE C CB    1 
ATOM   21213 C  CG1   . ILE C 3  100  ? 147.261 172.815 99.786  1.00 1.54   ? 100  ILE C CG1   1 
ATOM   21214 C  CG2   . ILE C 3  100  ? 146.927 173.830 97.540  1.00 13.98  ? 100  ILE C CG2   1 
ATOM   21215 C  CD1   . ILE C 3  100  ? 148.630 173.377 100.005 1.00 12.53  ? 100  ILE C CD1   1 
ATOM   21216 N  N     . PRO C 3  101  ? 144.122 172.379 96.298  1.00 12.29  ? 101  PRO C N     1 
ATOM   21217 C  CA    . PRO C 3  101  ? 143.724 172.309 94.890  1.00 12.67  ? 101  PRO C CA    1 
ATOM   21218 C  C     . PRO C 3  101  ? 144.666 173.131 94.028  1.00 5.62   ? 101  PRO C C     1 
ATOM   21219 O  O     . PRO C 3  101  ? 144.945 174.293 94.323  1.00 13.43  ? 101  PRO C O     1 
ATOM   21220 C  CB    . PRO C 3  101  ? 142.310 172.898 94.890  1.00 6.56   ? 101  PRO C CB    1 
ATOM   21221 C  CG    . PRO C 3  101  ? 141.925 173.013 96.297  1.00 3.64   ? 101  PRO C CG    1 
ATOM   21222 C  CD    . PRO C 3  101  ? 143.164 173.171 97.078  1.00 11.96  ? 101  PRO C CD    1 
ATOM   21223 N  N     . ILE C 3  102  ? 145.136 172.532 92.948  1.00 4.79   ? 102  ILE C N     1 
ATOM   21224 C  CA    . ILE C 3  102  ? 146.072 173.192 92.056  1.00 4.63   ? 102  ILE C CA    1 
ATOM   21225 C  C     . ILE C 3  102  ? 145.489 173.186 90.655  1.00 6.35   ? 102  ILE C C     1 
ATOM   21226 O  O     . ILE C 3  102  ? 144.614 172.384 90.327  1.00 9.84   ? 102  ILE C O     1 
ATOM   21227 C  CB    . ILE C 3  102  ? 147.474 172.539 92.076  1.00 3.66   ? 102  ILE C CB    1 
ATOM   21228 C  CG1   . ILE C 3  102  ? 147.437 171.134 91.496  1.00 1.71   ? 102  ILE C CG1   1 
ATOM   21229 C  CG2   . ILE C 3  102  ? 148.033 172.497 93.481  1.00 4.91   ? 102  ILE C CG2   1 
ATOM   21230 C  CD1   . ILE C 3  102  ? 148.767 170.623 91.076  1.00 5.68   ? 102  ILE C CD1   1 
ATOM   21231 N  N     . TYR C 3  103  ? 145.959 174.116 89.837  1.00 7.22   ? 103  TYR C N     1 
ATOM   21232 C  CA    . TYR C 3  103  ? 145.632 174.185 88.419  1.00 7.27   ? 103  TYR C CA    1 
ATOM   21233 C  C     . TYR C 3  103  ? 146.969 174.259 87.695  1.00 16.40  ? 103  TYR C C     1 
ATOM   21234 O  O     . TYR C 3  103  ? 147.471 175.344 87.408  1.00 20.71  ? 103  TYR C O     1 
ATOM   21235 C  CB    . TYR C 3  103  ? 144.746 175.371 88.112  1.00 6.89   ? 103  TYR C CB    1 
ATOM   21236 C  CG    . TYR C 3  103  ? 144.103 175.317 86.754  1.00 9.25   ? 103  TYR C CG    1 
ATOM   21237 C  CD1   . TYR C 3  103  ? 142.941 174.597 86.542  1.00 8.34   ? 103  TYR C CD1   1 
ATOM   21238 C  CD2   . TYR C 3  103  ? 144.661 175.985 85.678  1.00 13.53  ? 103  TYR C CD2   1 
ATOM   21239 C  CE1   . TYR C 3  103  ? 142.357 174.544 85.303  1.00 8.62   ? 103  TYR C CE1   1 
ATOM   21240 C  CE2   . TYR C 3  103  ? 144.085 175.938 84.442  1.00 14.98  ? 103  TYR C CE2   1 
ATOM   21241 C  CZ    . TYR C 3  103  ? 142.936 175.217 84.257  1.00 15.68  ? 103  TYR C CZ    1 
ATOM   21242 O  OH    . TYR C 3  103  ? 142.365 175.173 83.014  1.00 19.87  ? 103  TYR C OH    1 
ATOM   21243 N  N     . ALA C 3  104  ? 147.550 173.102 87.416  1.00 19.04  ? 104  ALA C N     1 
ATOM   21244 C  CA    . ALA C 3  104  ? 148.902 173.014 86.895  1.00 16.31  ? 104  ALA C CA    1 
ATOM   21245 C  C     . ALA C 3  104  ? 148.901 172.495 85.467  1.00 26.53  ? 104  ALA C C     1 
ATOM   21246 O  O     . ALA C 3  104  ? 148.135 171.598 85.114  1.00 32.18  ? 104  ALA C O     1 
ATOM   21247 C  CB    . ALA C 3  104  ? 149.761 172.105 87.767  1.00 19.93  ? 104  ALA C CB    1 
ATOM   21248 N  N     . LYS C 3  105  ? 149.791 173.058 84.651  1.00 38.50  ? 105  LYS C N     1 
ATOM   21249 C  CA    . LYS C 3  105  ? 149.855 172.740 83.234  1.00 39.88  ? 105  LYS C CA    1 
ATOM   21250 C  C     . LYS C 3  105  ? 151.081 171.938 82.820  1.00 39.06  ? 105  LYS C C     1 
ATOM   21251 O  O     . LYS C 3  105  ? 151.212 171.623 81.633  1.00 42.06  ? 105  LYS C O     1 
ATOM   21252 C  CB    . LYS C 3  105  ? 149.779 174.024 82.402  1.00 38.11  ? 105  LYS C CB    1 
ATOM   21253 C  CG    . LYS C 3  105  ? 148.428 174.722 82.483  1.00 39.80  ? 105  LYS C CG    1 
ATOM   21254 C  CD    . LYS C 3  105  ? 147.340 173.933 81.771  1.00 38.39  ? 105  LYS C CD    1 
ATOM   21255 C  CE    . LYS C 3  105  ? 146.370 173.293 82.759  1.00 36.60  ? 105  LYS C CE    1 
ATOM   21256 N  NZ    . LYS C 3  105  ? 145.352 172.455 82.075  1.00 36.63  ? 105  LYS C NZ    1 
ATOM   21257 N  N     . ASN C 3  106  ? 151.981 171.602 83.740  1.00 30.16  ? 106  ASN C N     1 
ATOM   21258 C  CA    . ASN C 3  106  ? 153.020 170.626 83.440  1.00 33.98  ? 106  ASN C CA    1 
ATOM   21259 C  C     . ASN C 3  106  ? 153.544 170.034 84.735  1.00 33.24  ? 106  ASN C C     1 
ATOM   21260 O  O     . ASN C 3  106  ? 153.463 170.650 85.797  1.00 37.00  ? 106  ASN C O     1 
ATOM   21261 C  CB    . ASN C 3  106  ? 154.174 171.228 82.634  1.00 35.57  ? 106  ASN C CB    1 
ATOM   21262 C  CG    . ASN C 3  106  ? 154.583 172.582 83.129  1.00 36.11  ? 106  ASN C CG    1 
ATOM   21263 O  OD1   . ASN C 3  106  ? 153.937 173.158 83.995  1.00 37.10  ? 106  ASN C OD1   1 
ATOM   21264 N  ND2   . ASN C 3  106  ? 155.672 173.099 82.585  1.00 35.61  ? 106  ASN C ND2   1 
ATOM   21265 N  N     . GLU C 3  107  ? 154.102 168.837 84.620  1.00 31.83  ? 107  GLU C N     1 
ATOM   21266 C  CA    . GLU C 3  107  ? 154.601 168.084 85.758  1.00 32.37  ? 107  GLU C CA    1 
ATOM   21267 C  C     . GLU C 3  107  ? 156.065 168.356 86.054  1.00 36.94  ? 107  GLU C C     1 
ATOM   21268 O  O     . GLU C 3  107  ? 156.633 167.709 86.940  1.00 39.28  ? 107  GLU C O     1 
ATOM   21269 C  CB    . GLU C 3  107  ? 154.406 166.586 85.514  1.00 34.88  ? 107  GLU C CB    1 
ATOM   21270 C  CG    . GLU C 3  107  ? 153.027 166.069 85.890  1.00 36.66  ? 107  GLU C CG    1 
ATOM   21271 C  CD    . GLU C 3  107  ? 152.446 165.142 84.847  1.00 40.33  ? 107  GLU C CD    1 
ATOM   21272 O  OE1   . GLU C 3  107  ? 152.144 163.981 85.185  1.00 38.08  ? 107  GLU C OE1   1 
ATOM   21273 O  OE2   . GLU C 3  107  ? 152.285 165.579 83.688  1.00 36.31  ? 107  GLU C OE2   1 
ATOM   21274 N  N     . THR C 3  108  ? 156.687 169.286 85.332  1.00 32.65  ? 108  THR C N     1 
ATOM   21275 C  CA    . THR C 3  108  ? 158.108 169.548 85.506  1.00 28.83  ? 108  THR C CA    1 
ATOM   21276 C  C     . THR C 3  108  ? 158.374 170.465 86.697  1.00 31.84  ? 108  THR C C     1 
ATOM   21277 O  O     . THR C 3  108  ? 159.511 170.547 87.170  1.00 31.41  ? 108  THR C O     1 
ATOM   21278 C  CB    . THR C 3  108  ? 158.658 170.143 84.211  1.00 31.02  ? 108  THR C CB    1 
ATOM   21279 O  OG1   . THR C 3  108  ? 158.319 169.278 83.125  1.00 35.26  ? 108  THR C OG1   1 
ATOM   21280 C  CG2   . THR C 3  108  ? 160.166 170.278 84.256  1.00 33.57  ? 108  THR C CG2   1 
ATOM   21281 N  N     . LEU C 3  109  ? 157.346 171.143 87.202  1.00 22.35  ? 109  LEU C N     1 
ATOM   21282 C  CA    . LEU C 3  109  ? 157.522 172.050 88.330  1.00 20.91  ? 109  LEU C CA    1 
ATOM   21283 C  C     . LEU C 3  109  ? 157.851 171.286 89.607  1.00 19.87  ? 109  LEU C C     1 
ATOM   21284 O  O     . LEU C 3  109  ? 157.306 170.210 89.862  1.00 20.66  ? 109  LEU C O     1 
ATOM   21285 C  CB    . LEU C 3  109  ? 156.260 172.883 88.537  1.00 18.17  ? 109  LEU C CB    1 
ATOM   21286 C  CG    . LEU C 3  109  ? 155.615 173.556 87.334  1.00 22.75  ? 109  LEU C CG    1 
ATOM   21287 C  CD1   . LEU C 3  109  ? 154.257 174.087 87.712  1.00 21.41  ? 109  LEU C CD1   1 
ATOM   21288 C  CD2   . LEU C 3  109  ? 156.479 174.678 86.833  1.00 25.34  ? 109  LEU C CD2   1 
ATOM   21289 N  N     . VAL C 3  110  ? 158.742 171.851 90.415  1.00 13.76  ? 110  VAL C N     1 
ATOM   21290 C  CA    . VAL C 3  110  ? 159.103 171.305 91.716  1.00 15.71  ? 110  VAL C CA    1 
ATOM   21291 C  C     . VAL C 3  110  ? 159.148 172.460 92.705  1.00 15.29  ? 110  VAL C C     1 
ATOM   21292 O  O     . VAL C 3  110  ? 159.553 173.568 92.346  1.00 17.36  ? 110  VAL C O     1 
ATOM   21293 C  CB    . VAL C 3  110  ? 160.450 170.556 91.672  1.00 15.81  ? 110  VAL C CB    1 
ATOM   21294 C  CG1   . VAL C 3  110  ? 160.892 170.163 93.054  1.00 15.77  ? 110  VAL C CG1   1 
ATOM   21295 C  CG2   . VAL C 3  110  ? 160.343 169.324 90.797  1.00 20.19  ? 110  VAL C CG2   1 
ATOM   21296 N  N     . PHE C 3  111  ? 158.692 172.218 93.929  1.00 13.01  ? 111  PHE C N     1 
ATOM   21297 C  CA    . PHE C 3  111  ? 158.622 173.241 94.958  1.00 13.46  ? 111  PHE C CA    1 
ATOM   21298 C  C     . PHE C 3  111  ? 159.430 172.818 96.176  1.00 17.37  ? 111  PHE C C     1 
ATOM   21299 O  O     . PHE C 3  111  ? 159.943 171.702 96.253  1.00 16.59  ? 111  PHE C O     1 
ATOM   21300 C  CB    . PHE C 3  111  ? 157.169 173.516 95.365  1.00 15.92  ? 111  PHE C CB    1 
ATOM   21301 C  CG    . PHE C 3  111  ? 156.325 174.036 94.249  1.00 14.28  ? 111  PHE C CG    1 
ATOM   21302 C  CD1   . PHE C 3  111  ? 155.680 173.171 93.396  1.00 12.62  ? 111  PHE C CD1   1 
ATOM   21303 C  CD2   . PHE C 3  111  ? 156.194 175.390 94.041  1.00 11.19  ? 111  PHE C CD2   1 
ATOM   21304 C  CE1   . PHE C 3  111  ? 154.923 173.644 92.369  1.00 15.02  ? 111  PHE C CE1   1 
ATOM   21305 C  CE2   . PHE C 3  111  ? 155.434 175.866 93.014  1.00 11.57  ? 111  PHE C CE2   1 
ATOM   21306 C  CZ    . PHE C 3  111  ? 154.798 174.996 92.177  1.00 14.69  ? 111  PHE C CZ    1 
ATOM   21307 N  N     . ALA C 3  112  ? 159.536 173.732 97.134  1.00 17.52  ? 112  ALA C N     1 
ATOM   21308 C  CA    . ALA C 3  112  ? 160.267 173.482 98.364  1.00 15.34  ? 112  ALA C CA    1 
ATOM   21309 C  C     . ALA C 3  112  ? 159.689 174.335 99.481  1.00 15.57  ? 112  ALA C C     1 
ATOM   21310 O  O     . ALA C 3  112  ? 159.123 175.401 99.240  1.00 16.60  ? 112  ALA C O     1 
ATOM   21311 C  CB    . ALA C 3  112  ? 161.758 173.778 98.197  1.00 17.29  ? 112  ALA C CB    1 
ATOM   21312 N  N     . LEU C 3  113  ? 159.851 173.862 100.709 1.00 17.22  ? 113  LEU C N     1 
ATOM   21313 C  CA    . LEU C 3  113  ? 159.403 174.577 101.897 1.00 19.46  ? 113  LEU C CA    1 
ATOM   21314 C  C     . LEU C 3  113  ? 160.580 174.653 102.857 1.00 21.78  ? 113  LEU C C     1 
ATOM   21315 O  O     . LEU C 3  113  ? 161.080 173.618 103.300 1.00 27.27  ? 113  LEU C O     1 
ATOM   21316 C  CB    . LEU C 3  113  ? 158.205 173.875 102.535 1.00 20.98  ? 113  LEU C CB    1 
ATOM   21317 C  CG    . LEU C 3  113  ? 157.646 174.390 103.860 1.00 20.36  ? 113  LEU C CG    1 
ATOM   21318 C  CD1   . LEU C 3  113  ? 157.091 175.781 103.694 1.00 19.58  ? 113  LEU C CD1   1 
ATOM   21319 C  CD2   . LEU C 3  113  ? 156.573 173.458 104.363 1.00 18.79  ? 113  LEU C CD2   1 
ATOM   21320 N  N     . ARG C 3  114  ? 161.042 175.865 103.159 1.00 21.68  ? 114  ARG C N     1 
ATOM   21321 C  CA    . ARG C 3  114  ? 162.196 176.084 104.033 1.00 22.62  ? 114  ARG C CA    1 
ATOM   21322 C  C     . ARG C 3  114  ? 161.816 177.143 105.061 1.00 22.40  ? 114  ARG C C     1 
ATOM   21323 O  O     . ARG C 3  114  ? 161.910 178.341 104.787 1.00 23.73  ? 114  ARG C O     1 
ATOM   21324 C  CB    . ARG C 3  114  ? 163.425 176.507 103.230 1.00 23.13  ? 114  ARG C CB    1 
ATOM   21325 C  CG    . ARG C 3  114  ? 163.709 175.640 102.020 1.00 21.34  ? 114  ARG C CG    1 
ATOM   21326 C  CD    . ARG C 3  114  ? 165.047 175.969 101.400 1.00 23.42  ? 114  ARG C CD    1 
ATOM   21327 N  NE    . ARG C 3  114  ? 165.334 175.154 100.225 1.00 26.46  ? 114  ARG C NE    1 
ATOM   21328 C  CZ    . ARG C 3  114  ? 165.412 175.621 98.988  1.00 27.54  ? 114  ARG C CZ    1 
ATOM   21329 N  NH1   . ARG C 3  114  ? 165.231 176.900 98.721  1.00 23.74  ? 114  ARG C NH1   1 
ATOM   21330 N  NH2   . ARG C 3  114  ? 165.695 174.785 97.995  1.00 25.18  ? 114  ARG C NH2   1 
ATOM   21331 N  N     . SER C 3  115  ? 161.399 176.709 106.246 1.00 20.27  ? 115  SER C N     1 
ATOM   21332 C  CA    . SER C 3  115  ? 160.807 177.590 107.243 1.00 16.52  ? 115  SER C CA    1 
ATOM   21333 C  C     . SER C 3  115  ? 161.585 177.526 108.546 1.00 24.22  ? 115  SER C C     1 
ATOM   21334 O  O     . SER C 3  115  ? 161.964 176.443 108.995 1.00 25.91  ? 115  SER C O     1 
ATOM   21335 C  CB    . SER C 3  115  ? 159.347 177.224 107.492 1.00 18.42  ? 115  SER C CB    1 
ATOM   21336 O  OG    . SER C 3  115  ? 158.495 178.007 106.685 1.00 28.52  ? 115  SER C OG    1 
ATOM   21337 N  N     . LEU C 3  116  ? 161.817 178.689 109.148 1.00 25.08  ? 116  LEU C N     1 
ATOM   21338 C  CA    . LEU C 3  116  ? 162.467 178.810 110.445 1.00 20.99  ? 116  LEU C CA    1 
ATOM   21339 C  C     . LEU C 3  116  ? 161.615 179.683 111.347 1.00 22.73  ? 116  LEU C C     1 
ATOM   21340 O  O     . LEU C 3  116  ? 161.037 180.670 110.887 1.00 26.59  ? 116  LEU C O     1 
ATOM   21341 C  CB    . LEU C 3  116  ? 163.863 179.421 110.317 1.00 19.61  ? 116  LEU C CB    1 
ATOM   21342 C  CG    . LEU C 3  116  ? 165.071 178.502 110.474 1.00 24.83  ? 116  LEU C CG    1 
ATOM   21343 C  CD1   . LEU C 3  116  ? 165.099 177.883 111.868 1.00 24.13  ? 116  LEU C CD1   1 
ATOM   21344 C  CD2   . LEU C 3  116  ? 165.102 177.447 109.391 1.00 24.76  ? 116  LEU C CD2   1 
ATOM   21345 N  N     . ASN C 3  117  ? 161.543 179.331 112.623 1.00 21.62  ? 117  ASN C N     1 
ATOM   21346 C  CA    . ASN C 3  117  ? 160.873 180.143 113.635 1.00 18.46  ? 117  ASN C CA    1 
ATOM   21347 C  C     . ASN C 3  117  ? 161.953 180.742 114.528 1.00 23.42  ? 117  ASN C C     1 
ATOM   21348 O  O     . ASN C 3  117  ? 162.341 180.157 115.539 1.00 28.35  ? 117  ASN C O     1 
ATOM   21349 C  CB    . ASN C 3  117  ? 159.880 179.318 114.435 1.00 19.71  ? 117  ASN C CB    1 
ATOM   21350 C  CG    . ASN C 3  117  ? 158.996 180.163 115.318 1.00 18.58  ? 117  ASN C CG    1 
ATOM   21351 O  OD1   . ASN C 3  117  ? 159.072 181.382 115.305 1.00 17.59  ? 117  ASN C OD1   1 
ATOM   21352 N  ND2   . ASN C 3  117  ? 158.152 179.514 116.093 1.00 18.06  ? 117  ASN C ND2   1 
ATOM   21353 N  N     . ASN C 3  118  ? 162.440 181.919 114.148 1.00 27.63  ? 118  ASN C N     1 
ATOM   21354 C  CA    . ASN C 3  118  ? 163.425 182.647 114.931 1.00 27.73  ? 118  ASN C CA    1 
ATOM   21355 C  C     . ASN C 3  118  ? 162.782 183.694 115.826 1.00 29.38  ? 118  ASN C C     1 
ATOM   21356 O  O     . ASN C 3  118  ? 163.323 184.794 115.974 1.00 34.76  ? 118  ASN C O     1 
ATOM   21357 C  CB    . ASN C 3  118  ? 164.459 183.296 114.014 1.00 26.87  ? 118  ASN C CB    1 
ATOM   21358 C  CG    . ASN C 3  118  ? 165.675 182.423 113.806 1.00 29.62  ? 118  ASN C CG    1 
ATOM   21359 O  OD1   . ASN C 3  118  ? 166.621 182.472 114.585 1.00 32.29  ? 118  ASN C OD1   1 
ATOM   21360 N  ND2   . ASN C 3  118  ? 165.658 181.619 112.751 1.00 26.09  ? 118  ASN C ND2   1 
ATOM   21361 N  N     . SER C 3  119  ? 161.633 183.382 116.406 1.00 26.98  ? 119  SER C N     1 
ATOM   21362 C  CA    . SER C 3  119  ? 160.899 184.286 117.269 1.00 27.54  ? 119  SER C CA    1 
ATOM   21363 C  C     . SER C 3  119  ? 160.557 183.576 118.570 1.00 29.55  ? 119  SER C C     1 
ATOM   21364 O  O     . SER C 3  119  ? 160.974 182.444 118.816 1.00 31.95  ? 119  SER C O     1 
ATOM   21365 C  CB    . SER C 3  119  ? 159.637 184.794 116.573 1.00 29.82  ? 119  SER C CB    1 
ATOM   21366 O  OG    . SER C 3  119  ? 158.805 185.485 117.482 1.00 37.04  ? 119  SER C OG    1 
ATOM   21367 N  N     . CYS C 3  120  ? 159.791 184.260 119.411 1.00 32.23  ? 120  CYS C N     1 
ATOM   21368 C  CA    . CYS C 3  120  ? 159.396 183.744 120.712 1.00 34.63  ? 120  CYS C CA    1 
ATOM   21369 C  C     . CYS C 3  120  ? 157.947 183.290 120.748 1.00 34.43  ? 120  CYS C C     1 
ATOM   21370 O  O     . CYS C 3  120  ? 157.437 182.969 121.824 1.00 37.86  ? 120  CYS C O     1 
ATOM   21371 C  CB    . CYS C 3  120  ? 159.639 184.800 121.790 1.00 35.08  ? 120  CYS C CB    1 
ATOM   21372 S  SG    . CYS C 3  120  ? 159.411 186.498 121.218 1.00 46.10  ? 120  CYS C SG    1 
ATOM   21373 N  N     . GLU C 3  121  ? 157.271 183.258 119.604 1.00 28.29  ? 121  GLU C N     1 
ATOM   21374 C  CA    . GLU C 3  121  ? 155.876 182.860 119.536 1.00 26.33  ? 121  GLU C CA    1 
ATOM   21375 C  C     . GLU C 3  121  ? 155.713 181.738 118.524 1.00 26.61  ? 121  GLU C C     1 
ATOM   21376 O  O     . GLU C 3  121  ? 156.642 181.392 117.792 1.00 32.99  ? 121  GLU C O     1 
ATOM   21377 C  CB    . GLU C 3  121  ? 154.974 184.033 119.154 1.00 27.42  ? 121  GLU C CB    1 
ATOM   21378 C  CG    . GLU C 3  121  ? 155.363 185.348 119.786 1.00 31.84  ? 121  GLU C CG    1 
ATOM   21379 C  CD    . GLU C 3  121  ? 154.573 186.506 119.223 1.00 35.87  ? 121  GLU C CD    1 
ATOM   21380 O  OE1   . GLU C 3  121  ? 154.707 187.632 119.741 1.00 32.97  ? 121  GLU C OE1   1 
ATOM   21381 O  OE2   . GLU C 3  121  ? 153.810 186.286 118.260 1.00 37.86  ? 121  GLU C OE2   1 
ATOM   21382 N  N     . VAL C 3  122  ? 154.509 181.168 118.493 1.00 19.13  ? 122  VAL C N     1 
ATOM   21383 C  CA    . VAL C 3  122  ? 154.194 180.163 117.490 1.00 20.98  ? 122  VAL C CA    1 
ATOM   21384 C  C     . VAL C 3  122  ? 153.959 180.852 116.156 1.00 22.25  ? 122  VAL C C     1 
ATOM   21385 O  O     . VAL C 3  122  ? 153.171 181.799 116.057 1.00 25.53  ? 122  VAL C O     1 
ATOM   21386 C  CB    . VAL C 3  122  ? 152.980 179.334 117.930 1.00 17.69  ? 122  VAL C CB    1 
ATOM   21387 C  CG1   . VAL C 3  122  ? 152.620 178.320 116.878 1.00 16.51  ? 122  VAL C CG1   1 
ATOM   21388 C  CG2   . VAL C 3  122  ? 153.277 178.638 119.237 1.00 20.21  ? 122  VAL C CG2   1 
ATOM   21389 N  N     . LYS C 3  123  ? 154.658 180.392 115.126 1.00 16.41  ? 123  LYS C N     1 
ATOM   21390 C  CA    . LYS C 3  123  ? 154.599 180.981 113.797 1.00 16.47  ? 123  LYS C CA    1 
ATOM   21391 C  C     . LYS C 3  123  ? 153.810 180.069 112.873 1.00 21.29  ? 123  LYS C C     1 
ATOM   21392 O  O     . LYS C 3  123  ? 153.979 178.848 112.909 1.00 21.45  ? 123  LYS C O     1 
ATOM   21393 C  CB    . LYS C 3  123  ? 156.001 181.211 113.233 1.00 17.49  ? 123  LYS C CB    1 
ATOM   21394 C  CG    . LYS C 3  123  ? 156.009 181.864 111.869 1.00 19.73  ? 123  LYS C CG    1 
ATOM   21395 C  CD    . LYS C 3  123  ? 157.380 181.863 111.250 1.00 22.28  ? 123  LYS C CD    1 
ATOM   21396 C  CE    . LYS C 3  123  ? 157.772 180.478 110.794 1.00 22.89  ? 123  LYS C CE    1 
ATOM   21397 N  NZ    . LYS C 3  123  ? 156.928 179.985 109.674 1.00 23.86  ? 123  LYS C NZ    1 
ATOM   21398 N  N     . THR C 3  124  ? 152.961 180.662 112.041 1.00 19.23  ? 124  THR C N     1 
ATOM   21399 C  CA    . THR C 3  124  ? 152.115 179.904 111.134 1.00 14.57  ? 124  THR C CA    1 
ATOM   21400 C  C     . THR C 3  124  ? 152.724 179.896 109.739 1.00 15.53  ? 124  THR C C     1 
ATOM   21401 O  O     . THR C 3  124  ? 153.166 180.933 109.244 1.00 23.59  ? 124  THR C O     1 
ATOM   21402 C  CB    . THR C 3  124  ? 150.712 180.500 111.094 1.00 15.98  ? 124  THR C CB    1 
ATOM   21403 O  OG1   . THR C 3  124  ? 150.263 180.734 112.430 1.00 22.56  ? 124  THR C OG1   1 
ATOM   21404 C  CG2   . THR C 3  124  ? 149.753 179.546 110.426 1.00 12.34  ? 124  THR C CG2   1 
ATOM   21405 N  N     . ILE C 3  125  ? 152.744 178.725 109.116 1.00 11.47  ? 125  ILE C N     1 
ATOM   21406 C  CA    . ILE C 3  125  ? 153.232 178.563 107.752 1.00 7.96   ? 125  ILE C CA    1 
ATOM   21407 C  C     . ILE C 3  125  ? 152.043 178.619 106.808 1.00 11.94  ? 125  ILE C C     1 
ATOM   21408 O  O     . ILE C 3  125  ? 151.042 177.932 107.021 1.00 19.69  ? 125  ILE C O     1 
ATOM   21409 C  CB    . ILE C 3  125  ? 153.990 177.238 107.588 1.00 11.49  ? 125  ILE C CB    1 
ATOM   21410 C  CG1   . ILE C 3  125  ? 154.967 177.031 108.740 1.00 13.81  ? 125  ILE C CG1   1 
ATOM   21411 C  CG2   . ILE C 3  125  ? 154.713 177.207 106.272 1.00 14.95  ? 125  ILE C CG2   1 
ATOM   21412 C  CD1   . ILE C 3  125  ? 155.438 175.623 108.859 1.00 14.20  ? 125  ILE C CD1   1 
ATOM   21413 N  N     . TYR C 3  126  ? 152.147 179.434 105.769 1.00 12.28  ? 126  TYR C N     1 
ATOM   21414 C  CA    . TYR C 3  126  ? 151.113 179.545 104.757 1.00 8.61   ? 126  TYR C CA    1 
ATOM   21415 C  C     . TYR C 3  126  ? 151.640 179.021 103.428 1.00 13.38  ? 126  TYR C C     1 
ATOM   21416 O  O     . TYR C 3  126  ? 152.840 178.846 103.237 1.00 18.68  ? 126  TYR C O     1 
ATOM   21417 C  CB    . TYR C 3  126  ? 150.636 180.990 104.643 1.00 7.12   ? 126  TYR C CB    1 
ATOM   21418 C  CG    . TYR C 3  126  ? 149.973 181.497 105.893 1.00 14.40  ? 126  TYR C CG    1 
ATOM   21419 C  CD1   . TYR C 3  126  ? 148.692 181.107 106.225 1.00 12.41  ? 126  TYR C CD1   1 
ATOM   21420 C  CD2   . TYR C 3  126  ? 150.635 182.353 106.752 1.00 20.43  ? 126  TYR C CD2   1 
ATOM   21421 C  CE1   . TYR C 3  126  ? 148.088 181.562 107.365 1.00 15.84  ? 126  TYR C CE1   1 
ATOM   21422 C  CE2   . TYR C 3  126  ? 150.039 182.810 107.897 1.00 14.00  ? 126  TYR C CE2   1 
ATOM   21423 C  CZ    . TYR C 3  126  ? 148.766 182.413 108.198 1.00 18.69  ? 126  TYR C CZ    1 
ATOM   21424 O  OH    . TYR C 3  126  ? 148.163 182.870 109.339 1.00 24.01  ? 126  TYR C OH    1 
ATOM   21425 N  N     . SER C 3  127  ? 150.729 178.754 102.495 1.00 15.80  ? 127  SER C N     1 
ATOM   21426 C  CA    . SER C 3  127  ? 151.140 178.217 101.206 1.00 8.13   ? 127  SER C CA    1 
ATOM   21427 C  C     . SER C 3  127  ? 151.917 179.220 100.374 1.00 13.62  ? 127  SER C C     1 
ATOM   21428 O  O     . SER C 3  127  ? 152.580 178.823 99.416  1.00 23.49  ? 127  SER C O     1 
ATOM   21429 C  CB    . SER C 3  127  ? 149.935 177.724 100.412 1.00 10.07  ? 127  SER C CB    1 
ATOM   21430 O  OG    . SER C 3  127  ? 148.828 178.573 100.576 1.00 18.83  ? 127  SER C OG    1 
ATOM   21431 N  N     . ARG C 3  128  ? 151.867 180.503 100.719 1.00 15.60  ? 128  ARG C N     1 
ATOM   21432 C  CA    . ARG C 3  128  ? 152.729 181.477 100.069 1.00 16.32  ? 128  ARG C CA    1 
ATOM   21433 C  C     . ARG C 3  128  ? 154.194 181.248 100.391 1.00 17.62  ? 128  ARG C C     1 
ATOM   21434 O  O     . ARG C 3  128  ? 155.054 181.866 99.762  1.00 23.51  ? 128  ARG C O     1 
ATOM   21435 C  CB    . ARG C 3  128  ? 152.337 182.885 100.489 1.00 18.19  ? 128  ARG C CB    1 
ATOM   21436 C  CG    . ARG C 3  128  ? 152.545 183.111 101.944 1.00 18.21  ? 128  ARG C CG    1 
ATOM   21437 C  CD    . ARG C 3  128  ? 152.144 184.484 102.365 1.00 24.52  ? 128  ARG C CD    1 
ATOM   21438 N  NE    . ARG C 3  128  ? 152.317 184.632 103.803 1.00 31.06  ? 128  ARG C NE    1 
ATOM   21439 C  CZ    . ARG C 3  128  ? 152.002 185.719 104.488 1.00 22.66  ? 128  ARG C CZ    1 
ATOM   21440 N  NH1   . ARG C 3  128  ? 151.508 186.791 103.891 1.00 21.52  ? 128  ARG C NH1   1 
ATOM   21441 N  NH2   . ARG C 3  128  ? 152.170 185.723 105.806 1.00 16.01  ? 128  ARG C NH2   1 
ATOM   21442 N  N     . ASP C 3  129  ? 154.489 180.391 101.360 1.00 18.15  ? 129  ASP C N     1 
ATOM   21443 C  CA    . ASP C 3  129  ? 155.850 180.089 101.762 1.00 16.31  ? 129  ASP C CA    1 
ATOM   21444 C  C     . ASP C 3  129  ? 156.458 178.924 100.997 1.00 20.55  ? 129  ASP C C     1 
ATOM   21445 O  O     . ASP C 3  129  ? 157.608 178.573 101.262 1.00 24.22  ? 129  ASP C O     1 
ATOM   21446 C  CB    . ASP C 3  129  ? 155.879 179.823 103.264 1.00 16.33  ? 129  ASP C CB    1 
ATOM   21447 C  CG    . ASP C 3  129  ? 155.492 181.045 104.068 1.00 26.19  ? 129  ASP C CG    1 
ATOM   21448 O  OD1   . ASP C 3  129  ? 156.055 182.126 103.808 1.00 30.27  ? 129  ASP C OD1   1 
ATOM   21449 O  OD2   . ASP C 3  129  ? 154.622 180.941 104.952 1.00 28.10  ? 129  ASP C OD2   1 
ATOM   21450 N  N     . LEU C 3  130  ? 155.717 178.311 100.078 1.00 21.81  ? 130  LEU C N     1 
ATOM   21451 C  CA    . LEU C 3  130  ? 156.297 177.356 99.142  1.00 18.28  ? 130  LEU C CA    1 
ATOM   21452 C  C     . LEU C 3  130  ? 156.972 178.099 97.999  1.00 16.89  ? 130  LEU C C     1 
ATOM   21453 O  O     . LEU C 3  130  ? 156.362 178.967 97.372  1.00 23.05  ? 130  LEU C O     1 
ATOM   21454 C  CB    . LEU C 3  130  ? 155.219 176.432 98.585  1.00 14.15  ? 130  LEU C CB    1 
ATOM   21455 C  CG    . LEU C 3  130  ? 154.520 175.441 99.507  1.00 13.98  ? 130  LEU C CG    1 
ATOM   21456 C  CD1   . LEU C 3  130  ? 153.281 174.920 98.837  1.00 13.05  ? 130  LEU C CD1   1 
ATOM   21457 C  CD2   . LEU C 3  130  ? 155.429 174.296 99.830  1.00 18.67  ? 130  LEU C CD2   1 
ATOM   21458 N  N     . ILE C 3  131  ? 158.220 177.751 97.708  1.00 18.75  ? 131  ILE C N     1 
ATOM   21459 C  CA    . ILE C 3  131  ? 158.998 178.410 96.665  1.00 19.08  ? 131  ILE C CA    1 
ATOM   21460 C  C     . ILE C 3  131  ? 159.249 177.419 95.541  1.00 20.49  ? 131  ILE C C     1 
ATOM   21461 O  O     . ILE C 3  131  ? 159.514 176.240 95.789  1.00 21.71  ? 131  ILE C O     1 
ATOM   21462 C  CB    . ILE C 3  131  ? 160.326 178.973 97.205  1.00 16.85  ? 131  ILE C CB    1 
ATOM   21463 C  CG1   . ILE C 3  131  ? 161.008 177.953 98.104  1.00 21.05  ? 131  ILE C CG1   1 
ATOM   21464 C  CG2   . ILE C 3  131  ? 160.091 180.249 97.973  1.00 20.61  ? 131  ILE C CG2   1 
ATOM   21465 C  CD1   . ILE C 3  131  ? 162.324 178.407 98.628  1.00 24.45  ? 131  ILE C CD1   1 
ATOM   21466 N  N     . GLN C 3  132  ? 159.140 177.893 94.306  1.00 22.32  ? 132  GLN C N     1 
ATOM   21467 C  CA    . GLN C 3  132  ? 159.412 177.051 93.150  1.00 20.43  ? 132  GLN C CA    1 
ATOM   21468 C  C     . GLN C 3  132  ? 160.913 176.951 92.929  1.00 21.41  ? 132  GLN C C     1 
ATOM   21469 O  O     . GLN C 3  132  ? 161.597 177.970 92.814  1.00 25.50  ? 132  GLN C O     1 
ATOM   21470 C  CB    . GLN C 3  132  ? 158.730 177.605 91.907  1.00 18.44  ? 132  GLN C CB    1 
ATOM   21471 C  CG    . GLN C 3  132  ? 158.912 176.729 90.702  1.00 17.88  ? 132  GLN C CG    1 
ATOM   21472 C  CD    . GLN C 3  132  ? 158.589 177.438 89.429  1.00 20.26  ? 132  GLN C CD    1 
ATOM   21473 O  OE1   . GLN C 3  132  ? 158.241 178.611 89.434  1.00 24.61  ? 132  GLN C OE1   1 
ATOM   21474 N  NE2   . GLN C 3  132  ? 158.693 176.728 88.320  1.00 21.73  ? 132  GLN C NE2   1 
ATOM   21475 N  N     . VAL C 3  133  ? 161.420 175.727 92.850  1.00 24.92  ? 133  VAL C N     1 
ATOM   21476 C  CA    . VAL C 3  133  ? 162.848 175.499 92.710  1.00 24.45  ? 133  VAL C CA    1 
ATOM   21477 C  C     . VAL C 3  133  ? 163.219 174.824 91.395  1.00 26.83  ? 133  VAL C C     1 
ATOM   21478 O  O     . VAL C 3  133  ? 164.418 174.665 91.122  1.00 30.34  ? 133  VAL C O     1 
ATOM   21479 C  CB    . VAL C 3  133  ? 163.397 174.686 93.899  1.00 21.90  ? 133  VAL C CB    1 
ATOM   21480 C  CG1   . VAL C 3  133  ? 163.145 175.422 95.194  1.00 21.71  ? 133  VAL C CG1   1 
ATOM   21481 C  CG2   . VAL C 3  133  ? 162.779 173.314 93.934  1.00 21.32  ? 133  VAL C CG2   1 
ATOM   21482 N  N     . ALA C 3  134  ? 162.250 174.415 90.582  1.00 25.04  ? 134  ALA C N     1 
ATOM   21483 C  CA    . ALA C 3  134  ? 162.532 173.763 89.315  1.00 23.59  ? 134  ALA C CA    1 
ATOM   21484 C  C     . ALA C 3  134  ? 161.396 174.030 88.343  1.00 24.98  ? 134  ALA C C     1 
ATOM   21485 O  O     . ALA C 3  134  ? 160.326 174.501 88.730  1.00 26.07  ? 134  ALA C O     1 
ATOM   21486 C  CB    . ALA C 3  134  ? 162.737 172.258 89.481  1.00 21.45  ? 134  ALA C CB    1 
ATOM   21487 N  N     . GLY C 3  135  ? 161.646 173.741 87.073  1.00 28.93  ? 135  GLY C N     1 
ATOM   21488 C  CA    . GLY C 3  135  ? 160.676 173.983 86.036  1.00 26.53  ? 135  GLY C CA    1 
ATOM   21489 C  C     . GLY C 3  135  ? 160.727 175.413 85.548  1.00 27.43  ? 135  GLY C C     1 
ATOM   21490 O  O     . GLY C 3  135  ? 161.438 176.255 86.102  1.00 29.38  ? 135  GLY C O     1 
ATOM   21491 N  N     . PRO C 3  136  ? 159.983 175.712 84.489  1.00 27.54  ? 136  PRO C N     1 
ATOM   21492 C  CA    . PRO C 3  136  ? 159.908 177.095 84.012  1.00 26.07  ? 136  PRO C CA    1 
ATOM   21493 C  C     . PRO C 3  136  ? 159.207 177.987 85.021  1.00 25.46  ? 136  PRO C C     1 
ATOM   21494 O  O     . PRO C 3  136  ? 158.310 177.556 85.747  1.00 30.52  ? 136  PRO C O     1 
ATOM   21495 C  CB    . PRO C 3  136  ? 159.101 176.980 82.716  1.00 27.97  ? 136  PRO C CB    1 
ATOM   21496 C  CG    . PRO C 3  136  ? 158.328 175.734 82.863  1.00 29.47  ? 136  PRO C CG    1 
ATOM   21497 C  CD    . PRO C 3  136  ? 159.177 174.800 83.667  1.00 30.73  ? 136  PRO C CD    1 
ATOM   21498 N  N     . LYS C 3  137  ? 159.623 179.248 85.062  1.00 28.73  ? 137  LYS C N     1 
ATOM   21499 C  CA    . LYS C 3  137  ? 159.027 180.177 86.010  1.00 31.58  ? 137  LYS C CA    1 
ATOM   21500 C  C     . LYS C 3  137  ? 157.560 180.407 85.686  1.00 31.48  ? 137  LYS C C     1 
ATOM   21501 O  O     . LYS C 3  137  ? 157.185 180.605 84.530  1.00 30.30  ? 137  LYS C O     1 
ATOM   21502 C  CB    . LYS C 3  137  ? 159.768 181.508 86.011  1.00 29.78  ? 137  LYS C CB    1 
ATOM   21503 C  CG    . LYS C 3  137  ? 159.779 182.158 87.372  1.00 28.11  ? 137  LYS C CG    1 
ATOM   21504 C  CD    . LYS C 3  137  ? 160.494 183.485 87.361  1.00 30.24  ? 137  LYS C CD    1 
ATOM   21505 C  CE    . LYS C 3  137  ? 160.308 184.200 88.686  1.00 32.92  ? 137  LYS C CE    1 
ATOM   21506 N  NZ    . LYS C 3  137  ? 160.239 183.244 89.828  1.00 32.36  ? 137  LYS C NZ    1 
ATOM   21507 N  N     . LEU C 3  138  ? 156.732 180.397 86.724  1.00 30.96  ? 138  LEU C N     1 
ATOM   21508 C  CA    . LEU C 3  138  ? 155.293 180.537 86.565  1.00 28.39  ? 138  LEU C CA    1 
ATOM   21509 C  C     . LEU C 3  138  ? 154.938 181.992 86.307  1.00 30.57  ? 138  LEU C C     1 
ATOM   21510 O  O     . LEU C 3  138  ? 155.369 182.883 87.046  1.00 31.86  ? 138  LEU C O     1 
ATOM   21511 C  CB    . LEU C 3  138  ? 154.570 180.031 87.809  1.00 26.93  ? 138  LEU C CB    1 
ATOM   21512 C  CG    . LEU C 3  138  ? 154.605 178.540 88.116  1.00 29.97  ? 138  LEU C CG    1 
ATOM   21513 C  CD1   . LEU C 3  138  ? 153.981 178.284 89.464  1.00 26.42  ? 138  LEU C CD1   1 
ATOM   21514 C  CD2   . LEU C 3  138  ? 153.887 177.767 87.041  1.00 30.36  ? 138  LEU C CD2   1 
ATOM   21515 N  N     . LYS C 3  139  ? 154.159 182.235 85.256  1.00 31.61  ? 139  LYS C N     1 
ATOM   21516 C  CA    . LYS C 3  139  ? 153.582 183.552 85.044  1.00 32.04  ? 139  LYS C CA    1 
ATOM   21517 C  C     . LYS C 3  139  ? 152.385 183.810 85.946  1.00 32.18  ? 139  LYS C C     1 
ATOM   21518 O  O     . LYS C 3  139  ? 152.149 184.957 86.331  1.00 35.20  ? 139  LYS C O     1 
ATOM   21519 C  CB    . LYS C 3  139  ? 153.165 183.716 83.585  1.00 36.19  ? 139  LYS C CB    1 
ATOM   21520 C  CG    . LYS C 3  139  ? 154.310 183.984 82.619  1.00 36.54  ? 139  LYS C CG    1 
ATOM   21521 C  CD    . LYS C 3  139  ? 155.371 184.873 83.232  1.00 35.46  ? 139  LYS C CD    1 
ATOM   21522 C  CE    . LYS C 3  139  ? 156.732 184.621 82.604  1.00 35.91  ? 139  LYS C CE    1 
ATOM   21523 N  NZ    . LYS C 3  139  ? 157.170 183.203 82.729  1.00 37.70  ? 139  LYS C NZ    1 
ATOM   21524 N  N     . TYR C 3  140  ? 151.634 182.767 86.293  1.00 23.14  ? 140  TYR C N     1 
ATOM   21525 C  CA    . TYR C 3  140  ? 150.434 182.839 87.103  1.00 22.89  ? 140  TYR C CA    1 
ATOM   21526 C  C     . TYR C 3  140  ? 150.555 181.788 88.197  1.00 24.18  ? 140  TYR C C     1 
ATOM   21527 O  O     . TYR C 3  140  ? 151.229 180.771 87.997  1.00 27.43  ? 140  TYR C O     1 
ATOM   21528 C  CB    . TYR C 3  140  ? 149.182 182.583 86.251  1.00 21.01  ? 140  TYR C CB    1 
ATOM   21529 C  CG    . TYR C 3  140  ? 147.917 183.165 86.822  1.00 21.81  ? 140  TYR C CG    1 
ATOM   21530 C  CD1   . TYR C 3  140  ? 147.644 184.514 86.713  1.00 22.95  ? 140  TYR C CD1   1 
ATOM   21531 C  CD2   . TYR C 3  140  ? 146.996 182.363 87.478  1.00 22.57  ? 140  TYR C CD2   1 
ATOM   21532 C  CE1   . TYR C 3  140  ? 146.497 185.045 87.242  1.00 22.02  ? 140  TYR C CE1   1 
ATOM   21533 C  CE2   . TYR C 3  140  ? 145.849 182.889 88.008  1.00 19.81  ? 140  TYR C CE2   1 
ATOM   21534 C  CZ    . TYR C 3  140  ? 145.605 184.228 87.885  1.00 20.85  ? 140  TYR C CZ    1 
ATOM   21535 O  OH    . TYR C 3  140  ? 144.458 184.758 88.409  1.00 25.74  ? 140  TYR C OH    1 
ATOM   21536 N  N     . PRO C 3  141  ? 149.942 182.002 89.360  1.00 16.99  ? 141  PRO C N     1 
ATOM   21537 C  CA    . PRO C 3  141  ? 150.001 180.986 90.414  1.00 13.73  ? 141  PRO C CA    1 
ATOM   21538 C  C     . PRO C 3  141  ? 149.237 179.733 90.029  1.00 15.04  ? 141  PRO C C     1 
ATOM   21539 O  O     . PRO C 3  141  ? 148.348 179.760 89.179  1.00 16.60  ? 141  PRO C O     1 
ATOM   21540 C  CB    . PRO C 3  141  ? 149.353 181.681 91.615  1.00 15.71  ? 141  PRO C CB    1 
ATOM   21541 C  CG    . PRO C 3  141  ? 149.459 183.098 91.329  1.00 18.32  ? 141  PRO C CG    1 
ATOM   21542 C  CD    . PRO C 3  141  ? 149.356 183.254 89.856  1.00 15.55  ? 141  PRO C CD    1 
ATOM   21543 N  N     . ILE C 3  142  ? 149.595 178.615 90.662  1.00 13.19  ? 142  ILE C N     1 
ATOM   21544 C  CA    . ILE C 3  142  ? 148.840 177.385 90.479  1.00 13.18  ? 142  ILE C CA    1 
ATOM   21545 C  C     . ILE C 3  142  ? 148.057 176.995 91.720  1.00 12.53  ? 142  ILE C C     1 
ATOM   21546 O  O     . ILE C 3  142  ? 147.212 176.101 91.646  1.00 12.97  ? 142  ILE C O     1 
ATOM   21547 C  CB    . ILE C 3  142  ? 149.739 176.218 90.024  1.00 10.07  ? 142  ILE C CB    1 
ATOM   21548 C  CG1   . ILE C 3  142  ? 150.690 175.794 91.129  1.00 10.16  ? 142  ILE C CG1   1 
ATOM   21549 C  CG2   . ILE C 3  142  ? 150.507 176.589 88.787  1.00 8.84   ? 142  ILE C CG2   1 
ATOM   21550 C  CD1   . ILE C 3  142  ? 151.179 174.389 90.978  1.00 10.22  ? 142  ILE C CD1   1 
ATOM   21551 N  N     . PHE C 3  143  ? 148.302 177.646 92.852  1.00 10.74  ? 143  PHE C N     1 
ATOM   21552 C  CA    . PHE C 3  143  ? 147.488 177.464 94.043  1.00 3.76   ? 143  PHE C CA    1 
ATOM   21553 C  C     . PHE C 3  143  ? 147.372 178.798 94.758  1.00 8.34   ? 143  PHE C C     1 
ATOM   21554 O  O     . PHE C 3  143  ? 148.113 179.739 94.474  1.00 17.28  ? 143  PHE C O     1 
ATOM   21555 C  CB    . PHE C 3  143  ? 148.055 176.384 94.974  1.00 6.92   ? 143  PHE C CB    1 
ATOM   21556 C  CG    . PHE C 3  143  ? 149.521 176.507 95.250  1.00 6.69   ? 143  PHE C CG    1 
ATOM   21557 C  CD1   . PHE C 3  143  ? 150.007 177.464 96.115  1.00 8.96   ? 143  PHE C CD1   1 
ATOM   21558 C  CD2   . PHE C 3  143  ? 150.414 175.641 94.661  1.00 9.50   ? 143  PHE C CD2   1 
ATOM   21559 C  CE1   . PHE C 3  143  ? 151.342 177.565 96.364  1.00 7.04   ? 143  PHE C CE1   1 
ATOM   21560 C  CE2   . PHE C 3  143  ? 151.754 175.739 94.909  1.00 8.12   ? 143  PHE C CE2   1 
ATOM   21561 C  CZ    . PHE C 3  143  ? 152.218 176.700 95.759  1.00 8.65   ? 143  PHE C CZ    1 
ATOM   21562 N  N     . ASN C 3  144  ? 146.427 178.871 95.672  1.00 6.98   ? 144  ASN C N     1 
ATOM   21563 C  CA    . ASN C 3  144  ? 146.202 180.080 96.443  1.00 6.20   ? 144  ASN C CA    1 
ATOM   21564 C  C     . ASN C 3  144  ? 147.231 180.226 97.563  1.00 14.16  ? 144  ASN C C     1 
ATOM   21565 O  O     . ASN C 3  144  ? 147.758 179.235 98.067  1.00 15.89  ? 144  ASN C O     1 
ATOM   21566 C  CB    . ASN C 3  144  ? 144.801 180.075 97.033  1.00 4.90   ? 144  ASN C CB    1 
ATOM   21567 C  CG    . ASN C 3  144  ? 143.764 180.513 96.049  1.00 3.88   ? 144  ASN C CG    1 
ATOM   21568 O  OD1   . ASN C 3  144  ? 143.969 181.450 95.300  1.00 15.79  ? 144  ASN C OD1   1 
ATOM   21569 N  ND2   . ASN C 3  144  ? 142.635 179.843 96.052  1.00 7.59   ? 144  ASN C ND2   1 
ATOM   21570 N  N     . PRO C 3  145  ? 147.524 181.456 97.977  1.00 13.74  ? 145  PRO C N     1 
ATOM   21571 C  CA    . PRO C 3  145  ? 148.552 181.662 99.001  1.00 10.52  ? 145  PRO C CA    1 
ATOM   21572 C  C     . PRO C 3  145  ? 148.035 181.713 100.430 1.00 12.75  ? 145  PRO C C     1 
ATOM   21573 O  O     . PRO C 3  145  ? 148.784 182.063 101.344 1.00 19.84  ? 145  PRO C O     1 
ATOM   21574 C  CB    . PRO C 3  145  ? 149.151 183.007 98.594  1.00 5.44   ? 145  PRO C CB    1 
ATOM   21575 C  CG    . PRO C 3  145  ? 148.021 183.732 98.023  1.00 8.92   ? 145  PRO C CG    1 
ATOM   21576 C  CD    . PRO C 3  145  ? 147.139 182.725 97.341  1.00 9.63   ? 145  PRO C CD    1 
ATOM   21577 N  N     . THR C 3  146  ? 146.771 181.365 100.647 1.00 8.58   ? 146  THR C N     1 
ATOM   21578 C  CA    . THR C 3  146  ? 146.119 181.596 101.927 1.00 6.78   ? 146  THR C CA    1 
ATOM   21579 C  C     . THR C 3  146  ? 145.966 180.342 102.776 1.00 6.14   ? 146  THR C C     1 
ATOM   21580 O  O     . THR C 3  146  ? 145.419 180.425 103.875 1.00 11.48  ? 146  THR C O     1 
ATOM   21581 C  CB    . THR C 3  146  ? 144.755 182.245 101.700 1.00 10.99  ? 146  THR C CB    1 
ATOM   21582 O  OG1   . THR C 3  146  ? 143.982 181.430 100.819 1.00 13.91  ? 146  THR C OG1   1 
ATOM   21583 C  CG2   . THR C 3  146  ? 144.911 183.603 101.083 1.00 11.71  ? 146  THR C CG2   1 
ATOM   21584 N  N     . PHE C 3  147  ? 146.433 179.190 102.307 1.00 4.85   ? 147  PHE C N     1 
ATOM   21585 C  CA    . PHE C 3  147  ? 146.263 177.941 103.038 1.00 8.32   ? 147  PHE C CA    1 
ATOM   21586 C  C     . PHE C 3  147  ? 147.197 177.888 104.237 1.00 8.90   ? 147  PHE C C     1 
ATOM   21587 O  O     . PHE C 3  147  ? 148.341 178.328 104.154 1.00 15.92  ? 147  PHE C O     1 
ATOM   21588 C  CB    . PHE C 3  147  ? 146.543 176.745 102.131 1.00 10.09  ? 147  PHE C CB    1 
ATOM   21589 C  CG    . PHE C 3  147  ? 145.445 176.434 101.166 1.00 8.03   ? 147  PHE C CG    1 
ATOM   21590 C  CD1   . PHE C 3  147  ? 144.407 175.603 101.522 1.00 2.86   ? 147  PHE C CD1   1 
ATOM   21591 C  CD2   . PHE C 3  147  ? 145.456 176.967 99.898  1.00 4.64   ? 147  PHE C CD2   1 
ATOM   21592 C  CE1   . PHE C 3  147  ? 143.409 175.318 100.634 1.00 2.07   ? 147  PHE C CE1   1 
ATOM   21593 C  CE2   . PHE C 3  147  ? 144.464 176.685 99.017  1.00 3.60   ? 147  PHE C CE2   1 
ATOM   21594 C  CZ    . PHE C 3  147  ? 143.439 175.862 99.386  1.00 1.06   ? 147  PHE C CZ    1 
ATOM   21595 N  N     . GLU C 3  148  ? 146.717 177.329 105.342 1.00 10.02  ? 148  GLU C N     1 
ATOM   21596 C  CA    . GLU C 3  148  ? 147.550 177.052 106.510 1.00 5.67   ? 148  GLU C CA    1 
ATOM   21597 C  C     . GLU C 3  148  ? 148.141 175.663 106.344 1.00 4.52   ? 148  GLU C C     1 
ATOM   21598 O  O     . GLU C 3  148  ? 147.427 174.671 106.228 1.00 3.78   ? 148  GLU C O     1 
ATOM   21599 C  CB    . GLU C 3  148  ? 146.741 177.137 107.795 1.00 6.67   ? 148  GLU C CB    1 
ATOM   21600 C  CG    . GLU C 3  148  ? 146.334 178.520 108.208 1.00 6.53   ? 148  GLU C CG    1 
ATOM   21601 C  CD    . GLU C 3  148  ? 145.367 178.509 109.370 1.00 14.49  ? 148  GLU C CD    1 
ATOM   21602 O  OE1   . GLU C 3  148  ? 144.662 177.500 109.554 1.00 14.21  ? 148  GLU C OE1   1 
ATOM   21603 O  OE2   . GLU C 3  148  ? 145.318 179.503 110.117 1.00 19.69  ? 148  GLU C OE2   1 
ATOM   21604 N  N     . ILE C 3  149  ? 149.468 175.583 106.339 1.00 4.01   ? 149  ILE C N     1 
ATOM   21605 C  CA    . ILE C 3  149  ? 150.115 174.286 106.208 1.00 5.17   ? 149  ILE C CA    1 
ATOM   21606 C  C     . ILE C 3  149  ? 150.518 173.752 107.574 1.00 11.23  ? 149  ILE C C     1 
ATOM   21607 O  O     . ILE C 3  149  ? 150.473 172.543 107.820 1.00 13.77  ? 149  ILE C O     1 
ATOM   21608 C  CB    . ILE C 3  149  ? 151.311 174.388 105.245 1.00 6.87   ? 149  ILE C CB    1 
ATOM   21609 C  CG1   . ILE C 3  149  ? 150.814 174.671 103.830 1.00 6.57   ? 149  ILE C CG1   1 
ATOM   21610 C  CG2   . ILE C 3  149  ? 152.134 173.116 105.257 1.00 4.56   ? 149  ILE C CG2   1 
ATOM   21611 C  CD1   . ILE C 3  149  ? 151.897 174.900 102.844 1.00 6.82   ? 149  ILE C CD1   1 
ATOM   21612 N  N     . GLY C 3  150  ? 150.907 174.631 108.483 1.00 11.73  ? 150  GLY C N     1 
ATOM   21613 C  CA    . GLY C 3  150  ? 151.330 174.174 109.786 1.00 7.81   ? 150  GLY C CA    1 
ATOM   21614 C  C     . GLY C 3  150  ? 151.671 175.335 110.684 1.00 11.12  ? 150  GLY C C     1 
ATOM   21615 O  O     . GLY C 3  150  ? 151.449 176.493 110.344 1.00 14.27  ? 150  GLY C O     1 
ATOM   21616 N  N     . PHE C 3  151  ? 152.194 175.000 111.857 1.00 10.34  ? 151  PHE C N     1 
ATOM   21617 C  CA    . PHE C 3  151  ? 152.653 175.996 112.807 1.00 8.66   ? 151  PHE C CA    1 
ATOM   21618 C  C     . PHE C 3  151  ? 153.865 175.447 113.539 1.00 12.80  ? 151  PHE C C     1 
ATOM   21619 O  O     . PHE C 3  151  ? 153.938 174.256 113.844 1.00 15.44  ? 151  PHE C O     1 
ATOM   21620 C  CB    . PHE C 3  151  ? 151.549 176.403 113.794 1.00 12.22  ? 151  PHE C CB    1 
ATOM   21621 C  CG    . PHE C 3  151  ? 150.871 175.246 114.462 1.00 14.24  ? 151  PHE C CG    1 
ATOM   21622 C  CD1   . PHE C 3  151  ? 149.778 174.639 113.879 1.00 14.51  ? 151  PHE C CD1   1 
ATOM   21623 C  CD2   . PHE C 3  151  ? 151.319 174.772 115.677 1.00 14.73  ? 151  PHE C CD2   1 
ATOM   21624 C  CE1   . PHE C 3  151  ? 149.163 173.582 114.489 1.00 13.35  ? 151  PHE C CE1   1 
ATOM   21625 C  CE2   . PHE C 3  151  ? 150.699 173.714 116.285 1.00 15.67  ? 151  PHE C CE2   1 
ATOM   21626 C  CZ    . PHE C 3  151  ? 149.623 173.121 115.692 1.00 11.35  ? 151  PHE C CZ    1 
ATOM   21627 N  N     . LEU C 3  152  ? 154.820 176.332 113.811 1.00 18.75  ? 152  LEU C N     1 
ATOM   21628 C  CA    . LEU C 3  152  ? 156.095 175.977 114.417 1.00 15.07  ? 152  LEU C CA    1 
ATOM   21629 C  C     . LEU C 3  152  ? 156.179 176.557 115.818 1.00 18.47  ? 152  LEU C C     1 
ATOM   21630 O  O     . LEU C 3  152  ? 155.829 177.719 116.032 1.00 22.03  ? 152  LEU C O     1 
ATOM   21631 C  CB    . LEU C 3  152  ? 157.263 176.496 113.577 1.00 12.35  ? 152  LEU C CB    1 
ATOM   21632 C  CG    . LEU C 3  152  ? 157.452 175.917 112.182 1.00 15.60  ? 152  LEU C CG    1 
ATOM   21633 C  CD1   . LEU C 3  152  ? 158.469 176.724 111.425 1.00 18.03  ? 152  LEU C CD1   1 
ATOM   21634 C  CD2   . LEU C 3  152  ? 157.874 174.482 112.271 1.00 18.63  ? 152  LEU C CD2   1 
ATOM   21635 N  N     . GLN C 3  153  ? 156.638 175.746 116.766 1.00 23.01  ? 153  GLN C N     1 
ATOM   21636 C  CA    . GLN C 3  153  ? 156.955 176.230 118.097 1.00 21.76  ? 153  GLN C CA    1 
ATOM   21637 C  C     . GLN C 3  153  ? 158.193 177.120 118.032 1.00 23.08  ? 153  GLN C C     1 
ATOM   21638 O  O     . GLN C 3  153  ? 158.939 177.074 117.055 1.00 27.57  ? 153  GLN C O     1 
ATOM   21639 C  CB    . GLN C 3  153  ? 157.192 175.058 119.041 1.00 19.73  ? 153  GLN C CB    1 
ATOM   21640 C  CG    . GLN C 3  153  ? 156.083 174.039 119.057 1.00 18.77  ? 153  GLN C CG    1 
ATOM   21641 C  CD    . GLN C 3  153  ? 154.760 174.628 119.461 1.00 24.58  ? 153  GLN C CD    1 
ATOM   21642 O  OE1   . GLN C 3  153  ? 154.682 175.436 120.380 1.00 29.75  ? 153  GLN C OE1   1 
ATOM   21643 N  NE2   . GLN C 3  153  ? 153.707 174.235 118.765 1.00 27.71  ? 153  GLN C NE2   1 
ATOM   21644 N  N     . PRO C 3  154  ? 158.419 177.962 119.039 1.00 25.45  ? 154  PRO C N     1 
ATOM   21645 C  CA    . PRO C 3  154  ? 159.592 178.845 118.998 1.00 22.23  ? 154  PRO C CA    1 
ATOM   21646 C  C     . PRO C 3  154  ? 160.886 178.060 118.843 1.00 23.30  ? 154  PRO C C     1 
ATOM   21647 O  O     . PRO C 3  154  ? 161.112 177.060 119.525 1.00 24.79  ? 154  PRO C O     1 
ATOM   21648 C  CB    . PRO C 3  154  ? 159.532 179.573 120.343 1.00 24.77  ? 154  PRO C CB    1 
ATOM   21649 C  CG    . PRO C 3  154  ? 158.119 179.502 120.745 1.00 24.45  ? 154  PRO C CG    1 
ATOM   21650 C  CD    . PRO C 3  154  ? 157.595 178.208 120.235 1.00 23.45  ? 154  PRO C CD    1 
ATOM   21651 N  N     . GLY C 3  155  ? 161.738 178.525 117.935 1.00 21.95  ? 155  GLY C N     1 
ATOM   21652 C  CA    . GLY C 3  155  ? 163.031 177.935 117.703 1.00 20.55  ? 155  GLY C CA    1 
ATOM   21653 C  C     . GLY C 3  155  ? 163.029 176.711 116.811 1.00 24.13  ? 155  GLY C C     1 
ATOM   21654 O  O     . GLY C 3  155  ? 164.077 176.077 116.657 1.00 30.26  ? 155  GLY C O     1 
ATOM   21655 N  N     . LYS C 3  156  ? 161.894 176.359 116.226 1.00 22.64  ? 156  LYS C N     1 
ATOM   21656 C  CA    . LYS C 3  156  ? 161.792 175.151 115.427 1.00 18.58  ? 156  LYS C CA    1 
ATOM   21657 C  C     . LYS C 3  156  ? 161.775 175.476 113.938 1.00 21.64  ? 156  LYS C C     1 
ATOM   21658 O  O     . LYS C 3  156  ? 161.605 176.622 113.525 1.00 25.07  ? 156  LYS C O     1 
ATOM   21659 C  CB    . LYS C 3  156  ? 160.549 174.370 115.823 1.00 18.19  ? 156  LYS C CB    1 
ATOM   21660 C  CG    . LYS C 3  156  ? 160.503 174.034 117.286 1.00 24.20  ? 156  LYS C CG    1 
ATOM   21661 C  CD    . LYS C 3  156  ? 161.709 173.211 117.659 1.00 23.35  ? 156  LYS C CD    1 
ATOM   21662 C  CE    . LYS C 3  156  ? 161.645 172.735 119.089 1.00 23.28  ? 156  LYS C CE    1 
ATOM   21663 N  NZ    . LYS C 3  156  ? 162.744 171.779 119.371 1.00 22.20  ? 156  LYS C NZ    1 
ATOM   21664 N  N     . SER C 3  157  ? 161.961 174.440 113.124 1.00 20.64  ? 157  SER C N     1 
ATOM   21665 C  CA    . SER C 3  157  ? 162.011 174.597 111.681 1.00 19.33  ? 157  SER C CA    1 
ATOM   21666 C  C     . SER C 3  157  ? 161.286 173.442 111.012 1.00 22.01  ? 157  SER C C     1 
ATOM   21667 O  O     . SER C 3  157  ? 161.029 172.403 111.620 1.00 22.70  ? 157  SER C O     1 
ATOM   21668 C  CB    . SER C 3  157  ? 163.450 174.663 111.167 1.00 19.72  ? 157  SER C CB    1 
ATOM   21669 O  OG    . SER C 3  157  ? 164.199 173.554 111.617 1.00 22.58  ? 157  SER C OG    1 
ATOM   21670 N  N     . LEU C 3  158  ? 160.967 173.640 109.737 1.00 19.45  ? 158  LEU C N     1 
ATOM   21671 C  CA    . LEU C 3  158  ? 160.392 172.600 108.892 1.00 16.78  ? 158  LEU C CA    1 
ATOM   21672 C  C     . LEU C 3  158  ? 160.959 172.786 107.496 1.00 18.75  ? 158  LEU C C     1 
ATOM   21673 O  O     . LEU C 3  158  ? 160.774 173.842 106.889 1.00 24.52  ? 158  LEU C O     1 
ATOM   21674 C  CB    . LEU C 3  158  ? 158.866 172.670 108.875 1.00 19.72  ? 158  LEU C CB    1 
ATOM   21675 C  CG    . LEU C 3  158  ? 158.140 171.576 108.092 1.00 20.44  ? 158  LEU C CG    1 
ATOM   21676 C  CD1   . LEU C 3  158  ? 158.400 170.225 108.701 1.00 19.29  ? 158  LEU C CD1   1 
ATOM   21677 C  CD2   . LEU C 3  158  ? 156.662 171.861 108.064 1.00 15.73  ? 158  LEU C CD2   1 
ATOM   21678 N  N     . ILE C 3  159  ? 161.659 171.778 106.992 1.00 21.20  ? 159  ILE C N     1 
ATOM   21679 C  CA    . ILE C 3  159  ? 162.246 171.820 105.661 1.00 19.64  ? 159  ILE C CA    1 
ATOM   21680 C  C     . ILE C 3  159  ? 161.758 170.606 104.893 1.00 19.39  ? 159  ILE C C     1 
ATOM   21681 O  O     . ILE C 3  159  ? 161.964 169.468 105.328 1.00 21.69  ? 159  ILE C O     1 
ATOM   21682 C  CB    . ILE C 3  159  ? 163.778 171.856 105.716 1.00 23.21  ? 159  ILE C CB    1 
ATOM   21683 C  CG1   . ILE C 3  159  ? 164.248 173.232 106.167 1.00 23.78  ? 159  ILE C CG1   1 
ATOM   21684 C  CG2   . ILE C 3  159  ? 164.361 171.543 104.361 1.00 23.15  ? 159  ILE C CG2   1 
ATOM   21685 C  CD1   . ILE C 3  159  ? 165.238 173.180 107.266 1.00 22.41  ? 159  ILE C CD1   1 
ATOM   21686 N  N     . ILE C 3  160  ? 161.107 170.846 103.758 1.00 17.35  ? 160  ILE C N     1 
ATOM   21687 C  CA    . ILE C 3  160  ? 160.667 169.786 102.863 1.00 18.54  ? 160  ILE C CA    1 
ATOM   21688 C  C     . ILE C 3  160  ? 161.146 170.122 101.462 1.00 19.06  ? 160  ILE C C     1 
ATOM   21689 O  O     . ILE C 3  160  ? 160.843 171.198 100.939 1.00 21.00  ? 160  ILE C O     1 
ATOM   21690 C  CB    . ILE C 3  160  ? 159.141 169.597 102.877 1.00 19.22  ? 160  ILE C CB    1 
ATOM   21691 C  CG1   . ILE C 3  160  ? 158.662 169.171 104.255 1.00 15.72  ? 160  ILE C CG1   1 
ATOM   21692 C  CG2   . ILE C 3  160  ? 158.730 168.551 101.873 1.00 19.48  ? 160  ILE C CG2   1 
ATOM   21693 C  CD1   . ILE C 3  160  ? 157.430 169.864 104.681 1.00 18.80  ? 160  ILE C CD1   1 
ATOM   21694 N  N     . GLU C 3  161  ? 161.881 169.203 100.855 1.00 27.05  ? 161  GLU C N     1 
ATOM   21695 C  CA    . GLU C 3  161  ? 162.342 169.330 99.484  1.00 25.35  ? 161  GLU C CA    1 
ATOM   21696 C  C     . GLU C 3  161  ? 161.538 168.398 98.591  1.00 25.11  ? 161  GLU C C     1 
ATOM   21697 O  O     . GLU C 3  161  ? 160.822 167.517 99.065  1.00 24.89  ? 161  GLU C O     1 
ATOM   21698 C  CB    . GLU C 3  161  ? 163.830 168.991 99.377  1.00 21.36  ? 161  GLU C CB    1 
ATOM   21699 C  CG    . GLU C 3  161  ? 164.722 169.808 100.275 1.00 25.16  ? 161  GLU C CG    1 
ATOM   21700 C  CD    . GLU C 3  161  ? 164.800 171.253 99.861  1.00 31.72  ? 161  GLU C CD    1 
ATOM   21701 O  OE1   . GLU C 3  161  ? 164.754 171.524 98.646  1.00 32.72  ? 161  GLU C OE1   1 
ATOM   21702 O  OE2   . GLU C 3  161  ? 164.912 172.120 100.747 1.00 33.16  ? 161  GLU C OE2   1 
ATOM   21703 N  N     . ASP C 3  162  ? 161.659 168.609 97.285  1.00 26.94  ? 162  ASP C N     1 
ATOM   21704 C  CA    . ASP C 3  162  ? 161.144 167.681 96.283  1.00 25.02  ? 162  ASP C CA    1 
ATOM   21705 C  C     . ASP C 3  162  ? 159.626 167.530 96.380  1.00 24.53  ? 162  ASP C C     1 
ATOM   21706 O  O     . ASP C 3  162  ? 159.093 166.434 96.541  1.00 23.31  ? 162  ASP C O     1 
ATOM   21707 C  CB    . ASP C 3  162  ? 161.833 166.323 96.415  1.00 25.76  ? 162  ASP C CB    1 
ATOM   21708 C  CG    . ASP C 3  162  ? 163.315 166.397 96.152  1.00 31.48  ? 162  ASP C CG    1 
ATOM   21709 O  OD1   . ASP C 3  162  ? 163.720 167.171 95.264  1.00 32.62  ? 162  ASP C OD1   1 
ATOM   21710 O  OD2   . ASP C 3  162  ? 164.079 165.689 96.841  1.00 30.95  ? 162  ASP C OD2   1 
ATOM   21711 N  N     . ILE C 3  163  ? 158.937 168.657 96.264  1.00 17.56  ? 163  ILE C N     1 
ATOM   21712 C  CA    . ILE C 3  163  ? 157.483 168.695 96.184  1.00 10.19  ? 163  ILE C CA    1 
ATOM   21713 C  C     . ILE C 3  163  ? 157.112 168.789 94.710  1.00 13.17  ? 163  ILE C C     1 
ATOM   21714 O  O     . ILE C 3  163  ? 157.237 169.849 94.095  1.00 23.39  ? 163  ILE C O     1 
ATOM   21715 C  CB    . ILE C 3  163  ? 156.911 169.865 96.992  1.00 10.68  ? 163  ILE C CB    1 
ATOM   21716 C  CG1   . ILE C 3  163  ? 157.203 169.669 98.474  1.00 11.85  ? 163  ILE C CG1   1 
ATOM   21717 C  CG2   . ILE C 3  163  ? 155.423 170.004 96.763  1.00 13.90  ? 163  ILE C CG2   1 
ATOM   21718 C  CD1   . ILE C 3  163  ? 156.895 170.858 99.313  1.00 9.61   ? 163  ILE C CD1   1 
ATOM   21719 N  N     . TYR C 3  164  ? 156.659 167.685 94.134  1.00 8.90   ? 164  TYR C N     1 
ATOM   21720 C  CA    . TYR C 3  164  ? 156.400 167.580 92.708  1.00 10.06  ? 164  TYR C CA    1 
ATOM   21721 C  C     . TYR C 3  164  ? 154.907 167.420 92.449  1.00 9.97   ? 164  TYR C C     1 
ATOM   21722 O  O     . TYR C 3  164  ? 154.091 167.409 93.367  1.00 11.96  ? 164  TYR C O     1 
ATOM   21723 C  CB    . TYR C 3  164  ? 157.182 166.408 92.101  1.00 13.38  ? 164  TYR C CB    1 
ATOM   21724 C  CG    . TYR C 3  164  ? 156.668 165.051 92.509  1.00 13.06  ? 164  TYR C CG    1 
ATOM   21725 C  CD1   . TYR C 3  164  ? 156.706 164.648 93.827  1.00 14.01  ? 164  TYR C CD1   1 
ATOM   21726 C  CD2   . TYR C 3  164  ? 156.157 164.171 91.577  1.00 9.89   ? 164  TYR C CD2   1 
ATOM   21727 C  CE1   . TYR C 3  164  ? 156.238 163.427 94.205  1.00 14.64  ? 164  TYR C CE1   1 
ATOM   21728 C  CE2   . TYR C 3  164  ? 155.686 162.938 91.954  1.00 12.59  ? 164  TYR C CE2   1 
ATOM   21729 C  CZ    . TYR C 3  164  ? 155.732 162.576 93.272  1.00 17.92  ? 164  TYR C CZ    1 
ATOM   21730 O  OH    . TYR C 3  164  ? 155.276 161.349 93.672  1.00 21.98  ? 164  TYR C OH    1 
ATOM   21731 N  N     . ILE C 3  165  ? 154.554 167.291 91.177  1.00 14.91  ? 165  ILE C N     1 
ATOM   21732 C  CA    . ILE C 3  165  ? 153.166 167.175 90.750  1.00 8.00   ? 165  ILE C CA    1 
ATOM   21733 C  C     . ILE C 3  165  ? 152.912 165.746 90.291  1.00 13.66  ? 165  ILE C C     1 
ATOM   21734 O  O     . ILE C 3  165  ? 153.569 165.250 89.372  1.00 20.22  ? 165  ILE C O     1 
ATOM   21735 C  CB    . ILE C 3  165  ? 152.836 168.180 89.641  1.00 5.30   ? 165  ILE C CB    1 
ATOM   21736 C  CG1   . ILE C 3  165  ? 152.906 169.601 90.183  1.00 10.57  ? 165  ILE C CG1   1 
ATOM   21737 C  CG2   . ILE C 3  165  ? 151.471 167.908 89.084  1.00 6.78   ? 165  ILE C CG2   1 
ATOM   21738 C  CD1   . ILE C 3  165  ? 152.919 170.648 89.128  1.00 14.07  ? 165  ILE C CD1   1 
ATOM   21739 N  N     . LYS C 3  166  ? 151.939 165.101 90.918  1.00 6.79   ? 166  LYS C N     1 
ATOM   21740 C  CA    . LYS C 3  166  ? 151.611 163.702 90.706  1.00 4.05   ? 166  LYS C CA    1 
ATOM   21741 C  C     . LYS C 3  166  ? 150.287 163.599 89.959  1.00 11.77  ? 166  LYS C C     1 
ATOM   21742 O  O     . LYS C 3  166  ? 149.479 164.525 89.992  1.00 15.66  ? 166  LYS C O     1 
ATOM   21743 C  CB    . LYS C 3  166  ? 151.542 162.998 92.058  1.00 7.45   ? 166  LYS C CB    1 
ATOM   21744 C  CG    . LYS C 3  166  ? 151.396 161.511 92.033  1.00 7.72   ? 166  LYS C CG    1 
ATOM   21745 C  CD    . LYS C 3  166  ? 151.418 160.986 93.443  1.00 5.14   ? 166  LYS C CD    1 
ATOM   21746 C  CE    . LYS C 3  166  ? 151.471 159.478 93.483  1.00 15.14  ? 166  LYS C CE    1 
ATOM   21747 N  NZ    . LYS C 3  166  ? 151.458 158.872 92.125  1.00 20.22  ? 166  LYS C NZ    1 
ATOM   21748 N  N     . LYS C 3  167  ? 150.072 162.484 89.266  1.00 10.20  ? 167  LYS C N     1 
ATOM   21749 C  CA    . LYS C 3  167  ? 148.889 162.292 88.437  1.00 4.18   ? 167  LYS C CA    1 
ATOM   21750 C  C     . LYS C 3  167  ? 148.115 161.055 88.873  1.00 12.04  ? 167  LYS C C     1 
ATOM   21751 O  O     . LYS C 3  167  ? 148.705 160.068 89.317  1.00 17.99  ? 167  LYS C O     1 
ATOM   21752 C  CB    . LYS C 3  167  ? 149.282 162.170 86.973  1.00 3.25   ? 167  LYS C CB    1 
ATOM   21753 C  CG    . LYS C 3  167  ? 148.135 162.295 86.016  1.00 10.08  ? 167  LYS C CG    1 
ATOM   21754 C  CD    . LYS C 3  167  ? 148.593 162.051 84.602  1.00 12.17  ? 167  LYS C CD    1 
ATOM   21755 C  CE    . LYS C 3  167  ? 147.421 162.077 83.655  1.00 18.78  ? 167  LYS C CE    1 
ATOM   21756 N  NZ    . LYS C 3  167  ? 147.811 161.718 82.272  1.00 22.32  ? 167  LYS C NZ    1 
ATOM   21757 N  N     . GLY C 3  168  ? 146.795 161.111 88.751  1.00 4.97   ? 168  GLY C N     1 
ATOM   21758 C  CA    . GLY C 3  168  ? 145.968 159.994 89.155  1.00 1.22   ? 168  GLY C CA    1 
ATOM   21759 C  C     . GLY C 3  168  ? 144.501 160.291 88.954  1.00 6.57   ? 168  GLY C C     1 
ATOM   21760 O  O     . GLY C 3  168  ? 144.130 161.290 88.344  1.00 13.54  ? 168  GLY C O     1 
ATOM   21761 N  N     . ILE C 3  169  ? 143.662 159.395 89.463  1.00 6.40   ? 169  ILE C N     1 
ATOM   21762 C  CA    . ILE C 3  169  ? 142.214 159.560 89.432  1.00 2.88   ? 169  ILE C CA    1 
ATOM   21763 C  C     . ILE C 3  169  ? 141.672 159.425 90.846  1.00 15.27  ? 169  ILE C C     1 
ATOM   21764 O  O     . ILE C 3  169  ? 142.186 158.638 91.643  1.00 9.60   ? 169  ILE C O     1 
ATOM   21765 C  CB    . ILE C 3  169  ? 141.521 158.555 88.487  1.00 7.03   ? 169  ILE C CB    1 
ATOM   21766 C  CG1   . ILE C 3  169  ? 141.675 157.128 88.986  1.00 7.08   ? 169  ILE C CG1   1 
ATOM   21767 C  CG2   . ILE C 3  169  ? 142.053 158.685 87.088  1.00 5.97   ? 169  ILE C CG2   1 
ATOM   21768 C  CD1   . ILE C 3  169  ? 140.717 156.184 88.347  1.00 7.89   ? 169  ILE C CD1   1 
ATOM   21769 N  N     . GLY C 3  170  ? 140.630 160.193 91.154  1.00 0.51   ? 170  GLY C N     1 
ATOM   21770 C  CA    . GLY C 3  170  ? 140.091 160.265 92.500  1.00 8.42   ? 170  GLY C CA    1 
ATOM   21771 C  C     . GLY C 3  170  ? 139.492 158.983 93.008  1.00 14.99  ? 170  GLY C C     1 
ATOM   21772 O  O     . GLY C 3  170  ? 139.214 158.874 94.201  1.00 10.74  ? 170  GLY C O     1 
ATOM   21773 N  N     . ARG C 3  171  ? 139.274 158.021 92.131  1.00 3.93   ? 171  ARG C N     1 
ATOM   21774 C  CA    . ARG C 3  171  ? 138.766 156.724 92.535  1.00 3.80   ? 171  ARG C CA    1 
ATOM   21775 C  C     . ARG C 3  171  ? 139.798 155.947 93.342  1.00 8.96   ? 171  ARG C C     1 
ATOM   21776 O  O     . ARG C 3  171  ? 139.432 155.107 94.167  1.00 10.31  ? 171  ARG C O     1 
ATOM   21777 C  CB    . ARG C 3  171  ? 138.359 155.963 91.280  1.00 3.69   ? 171  ARG C CB    1 
ATOM   21778 C  CG    . ARG C 3  171  ? 137.507 154.780 91.497  1.00 11.17  ? 171  ARG C CG    1 
ATOM   21779 C  CD    . ARG C 3  171  ? 136.892 154.376 90.187  1.00 15.25  ? 171  ARG C CD    1 
ATOM   21780 N  NE    . ARG C 3  171  ? 137.907 154.126 89.176  1.00 12.32  ? 171  ARG C NE    1 
ATOM   21781 C  CZ    . ARG C 3  171  ? 138.479 152.949 88.975  1.00 13.47  ? 171  ARG C CZ    1 
ATOM   21782 N  NH1   . ARG C 3  171  ? 138.149 151.891 89.690  1.00 8.55   ? 171  ARG C NH1   1 
ATOM   21783 N  NH2   . ARG C 3  171  ? 139.407 152.833 88.034  1.00 11.59  ? 171  ARG C NH2   1 
ATOM   21784 N  N     . LYS C 3  172  ? 141.086 156.212 93.121  1.00 9.02   ? 172  LYS C N     1 
ATOM   21785 C  CA    . LYS C 3  172  ? 142.171 155.533 93.817  1.00 3.47   ? 172  LYS C CA    1 
ATOM   21786 C  C     . LYS C 3  172  ? 142.603 156.282 95.069  1.00 5.36   ? 172  LYS C C     1 
ATOM   21787 O  O     . LYS C 3  172  ? 142.707 155.688 96.142  1.00 12.40  ? 172  LYS C O     1 
ATOM   21788 C  CB    . LYS C 3  172  ? 143.363 155.351 92.882  1.00 8.61   ? 172  LYS C CB    1 
ATOM   21789 C  CG    . LYS C 3  172  ? 143.033 154.729 91.555  1.00 10.36  ? 172  LYS C CG    1 
ATOM   21790 C  CD    . LYS C 3  172  ? 142.559 153.317 91.711  1.00 10.05  ? 172  LYS C CD    1 
ATOM   21791 C  CE    . LYS C 3  172  ? 142.290 152.701 90.360  1.00 12.74  ? 172  LYS C CE    1 
ATOM   21792 N  NZ    . LYS C 3  172  ? 141.791 151.314 90.493  1.00 14.41  ? 172  LYS C NZ    1 
ATOM   21793 N  N     . HIS C 3  173  ? 142.878 157.574 94.947  1.00 2.88   ? 173  HIS C N     1 
ATOM   21794 C  CA    . HIS C 3  173  ? 143.073 158.443 96.096  1.00 1.77   ? 173  HIS C CA    1 
ATOM   21795 C  C     . HIS C 3  173  ? 142.263 159.708 95.888  1.00 5.08   ? 173  HIS C C     1 
ATOM   21796 O  O     . HIS C 3  173  ? 142.322 160.314 94.820  1.00 5.44   ? 173  HIS C O     1 
ATOM   21797 C  CB    . HIS C 3  173  ? 144.548 158.779 96.312  1.00 2.07   ? 173  HIS C CB    1 
ATOM   21798 C  CG    . HIS C 3  173  ? 144.841 159.355 97.661  1.00 1.97   ? 173  HIS C CG    1 
ATOM   21799 N  ND1   . HIS C 3  173  ? 145.037 160.701 97.865  1.00 3.42   ? 173  HIS C ND1   1 
ATOM   21800 C  CD2   . HIS C 3  173  ? 144.948 158.772 98.875  1.00 8.45   ? 173  HIS C CD2   1 
ATOM   21801 C  CE1   . HIS C 3  173  ? 145.266 160.923 99.144  1.00 2.92   ? 173  HIS C CE1   1 
ATOM   21802 N  NE2   . HIS C 3  173  ? 145.216 159.769 99.780  1.00 5.22   ? 173  HIS C NE2   1 
ATOM   21803 N  N     . ALA C 3  174  ? 141.530 160.114 96.922  1.00 9.13   ? 174  ALA C N     1 
ATOM   21804 C  CA    . ALA C 3  174  ? 140.585 161.219 96.850  1.00 13.78  ? 174  ALA C CA    1 
ATOM   21805 C  C     . ALA C 3  174  ? 141.246 162.575 96.705  1.00 0.52   ? 174  ALA C C     1 
ATOM   21806 O  O     . ALA C 3  174  ? 140.537 163.564 96.524  1.00 10.18  ? 174  ALA C O     1 
ATOM   21807 C  CB    . ALA C 3  174  ? 139.695 161.229 98.084  1.00 0.92   ? 174  ALA C CB    1 
ATOM   21808 N  N     . ALA C 3  175  ? 142.566 162.666 96.819  1.00 0.73   ? 175  ALA C N     1 
ATOM   21809 C  CA    . ALA C 3  175  ? 143.227 163.922 96.511  1.00 5.35   ? 175  ALA C CA    1 
ATOM   21810 C  C     . ALA C 3  175  ? 143.180 164.242 95.029  1.00 2.92   ? 175  ALA C C     1 
ATOM   21811 O  O     . ALA C 3  175  ? 143.480 165.373 94.648  1.00 8.86   ? 175  ALA C O     1 
ATOM   21812 C  CB    . ALA C 3  175  ? 144.669 163.888 96.992  1.00 13.45  ? 175  ALA C CB    1 
ATOM   21813 N  N     . PHE C 3  176  ? 142.807 163.279 94.192  1.00 6.61   ? 176  PHE C N     1 
ATOM   21814 C  CA    . PHE C 3  176  ? 142.625 163.490 92.769  1.00 0.16   ? 176  PHE C CA    1 
ATOM   21815 C  C     . PHE C 3  176  ? 141.173 163.717 92.388  1.00 2.83   ? 176  PHE C C     1 
ATOM   21816 O  O     . PHE C 3  176  ? 140.861 163.740 91.198  1.00 11.66  ? 176  PHE C O     1 
ATOM   21817 C  CB    . PHE C 3  176  ? 143.177 162.308 91.982  1.00 6.59   ? 176  PHE C CB    1 
ATOM   21818 C  CG    . PHE C 3  176  ? 144.636 162.066 92.181  1.00 5.38   ? 176  PHE C CG    1 
ATOM   21819 C  CD1   . PHE C 3  176  ? 145.567 162.901 91.608  1.00 6.02   ? 176  PHE C CD1   1 
ATOM   21820 C  CD2   . PHE C 3  176  ? 145.077 160.984 92.908  1.00 5.42   ? 176  PHE C CD2   1 
ATOM   21821 C  CE1   . PHE C 3  176  ? 146.898 162.676 91.780  1.00 2.34   ? 176  PHE C CE1   1 
ATOM   21822 C  CE2   . PHE C 3  176  ? 146.408 160.756 93.076  1.00 4.12   ? 176  PHE C CE2   1 
ATOM   21823 C  CZ    . PHE C 3  176  ? 147.319 161.605 92.510  1.00 4.43   ? 176  PHE C CZ    1 
ATOM   21824 N  N     . ASN C 3  177  ? 140.276 163.866 93.357  1.00 6.15   ? 177  ASN C N     1 
ATOM   21825 C  CA    . ASN C 3  177  ? 138.907 164.250 93.048  1.00 9.81   ? 177  ASN C CA    1 
ATOM   21826 C  C     . ASN C 3  177  ? 138.879 165.638 92.429  1.00 3.84   ? 177  ASN C C     1 
ATOM   21827 O  O     . ASN C 3  177  ? 139.709 166.493 92.740  1.00 5.45   ? 177  ASN C O     1 
ATOM   21828 C  CB    . ASN C 3  177  ? 138.039 164.241 94.300  1.00 12.12  ? 177  ASN C CB    1 
ATOM   21829 C  CG    . ASN C 3  177  ? 137.601 162.858 94.707  1.00 1.50   ? 177  ASN C CG    1 
ATOM   21830 O  OD1   . ASN C 3  177  ? 137.833 161.896 94.003  1.00 4.29   ? 177  ASN C OD1   1 
ATOM   21831 N  ND2   . ASN C 3  177  ? 136.911 162.767 95.820  1.00 1.77   ? 177  ASN C ND2   1 
ATOM   21832 N  N     . LEU C 3  178  ? 137.918 165.868 91.537  1.00 2.55   ? 178  LEU C N     1 
ATOM   21833 C  CA    . LEU C 3  178  ? 137.836 167.145 90.844  1.00 9.69   ? 178  LEU C CA    1 
ATOM   21834 C  C     . LEU C 3  178  ? 136.587 167.943 91.198  1.00 3.18   ? 178  LEU C C     1 
ATOM   21835 O  O     . LEU C 3  178  ? 136.700 169.003 91.807  1.00 5.66   ? 178  LEU C O     1 
ATOM   21836 C  CB    . LEU C 3  178  ? 137.913 166.920 89.331  1.00 1.73   ? 178  LEU C CB    1 
ATOM   21837 C  CG    . LEU C 3  178  ? 137.929 168.175 88.458  1.00 4.48   ? 178  LEU C CG    1 
ATOM   21838 C  CD1   . LEU C 3  178  ? 139.052 169.100 88.841  1.00 4.01   ? 178  LEU C CD1   1 
ATOM   21839 C  CD2   . LEU C 3  178  ? 138.005 167.809 87.007  1.00 3.88   ? 178  LEU C CD2   1 
ATOM   21840 N  N     . ALA C 3  179  ? 135.394 167.458 90.891  1.00 1.23   ? 179  ALA C N     1 
ATOM   21841 C  CA    . ALA C 3  179  ? 134.184 168.256 91.029  1.00 5.56   ? 179  ALA C CA    1 
ATOM   21842 C  C     . ALA C 3  179  ? 133.358 167.786 92.216  1.00 0.80   ? 179  ALA C C     1 
ATOM   21843 O  O     . ALA C 3  179  ? 133.345 166.598 92.539  1.00 7.10   ? 179  ALA C O     1 
ATOM   21844 C  CB    . ALA C 3  179  ? 133.339 168.192 89.762  1.00 13.49  ? 179  ALA C CB    1 
ATOM   21845 N  N     . VAL C 3  180  ? 132.675 168.729 92.872  1.00 7.18   ? 180  VAL C N     1 
ATOM   21846 C  CA    . VAL C 3  180  ? 131.742 168.415 93.945  1.00 0.47   ? 180  VAL C CA    1 
ATOM   21847 C  C     . VAL C 3  180  ? 130.328 168.630 93.425  1.00 2.05   ? 180  VAL C C     1 
ATOM   21848 O  O     . VAL C 3  180  ? 130.065 169.562 92.662  1.00 0.29   ? 180  VAL C O     1 
ATOM   21849 C  CB    . VAL C 3  180  ? 132.013 169.237 95.227  1.00 1.14   ? 180  VAL C CB    1 
ATOM   21850 C  CG1   . VAL C 3  180  ? 133.458 169.130 95.638  1.00 3.06   ? 180  VAL C CG1   1 
ATOM   21851 C  CG2   . VAL C 3  180  ? 131.603 170.668 95.094  1.00 4.94   ? 180  VAL C CG2   1 
ATOM   21852 N  N     . LYS C 3  181  ? 129.423 167.737 93.812  1.00 4.01   ? 181  LYS C N     1 
ATOM   21853 C  CA    . LYS C 3  181  ? 128.044 167.792 93.346  1.00 6.70   ? 181  LYS C CA    1 
ATOM   21854 C  C     . LYS C 3  181  ? 127.295 168.933 94.011  1.00 1.16   ? 181  LYS C C     1 
ATOM   21855 O  O     . LYS C 3  181  ? 127.366 169.105 95.226  1.00 7.39   ? 181  LYS C O     1 
ATOM   21856 C  CB    . LYS C 3  181  ? 127.334 166.479 93.651  1.00 13.61  ? 181  LYS C CB    1 
ATOM   21857 C  CG    . LYS C 3  181  ? 127.774 165.311 92.835  1.00 15.00  ? 181  LYS C CG    1 
ATOM   21858 C  CD    . LYS C 3  181  ? 127.104 164.057 93.301  1.00 11.96  ? 181  LYS C CD    1 
ATOM   21859 C  CE    . LYS C 3  181  ? 128.053 163.157 94.043  1.00 6.33   ? 181  LYS C CE    1 
ATOM   21860 N  NZ    . LYS C 3  181  ? 128.355 163.596 95.407  1.00 3.91   ? 181  LYS C NZ    1 
ATOM   21861 N  N     . THR C 3  182  ? 126.556 169.708 93.216  1.00 10.80  ? 182  THR C N     1 
ATOM   21862 C  CA    . THR C 3  182  ? 125.724 170.769 93.758  1.00 7.73   ? 182  THR C CA    1 
ATOM   21863 C  C     . THR C 3  182  ? 124.265 170.707 93.337  1.00 5.70   ? 182  THR C C     1 
ATOM   21864 O  O     . THR C 3  182  ? 123.432 171.303 94.021  1.00 8.87   ? 182  THR C O     1 
ATOM   21865 C  CB    . THR C 3  182  ? 126.276 172.159 93.394  1.00 8.70   ? 182  THR C CB    1 
ATOM   21866 O  OG1   . THR C 3  182  ? 126.198 172.371 91.985  1.00 10.57  ? 182  THR C OG1   1 
ATOM   21867 C  CG2   . THR C 3  182  ? 127.703 172.323 93.857  1.00 0.40   ? 182  THR C CG2   1 
ATOM   21868 N  N     . HIS C 3  183  ? 123.927 170.028 92.246  1.00 4.18   ? 183  HIS C N     1 
ATOM   21869 C  CA    . HIS C 3  183  ? 122.528 169.928 91.857  1.00 5.80   ? 183  HIS C CA    1 
ATOM   21870 C  C     . HIS C 3  183  ? 122.348 168.790 90.868  1.00 14.23  ? 183  HIS C C     1 
ATOM   21871 O  O     . HIS C 3  183  ? 123.225 168.538 90.049  1.00 8.21   ? 183  HIS C O     1 
ATOM   21872 C  CB    . HIS C 3  183  ? 122.020 171.228 91.232  1.00 13.02  ? 183  HIS C CB    1 
ATOM   21873 C  CG    . HIS C 3  183  ? 120.569 171.186 90.879  1.00 0.51   ? 183  HIS C CG    1 
ATOM   21874 N  ND1   . HIS C 3  183  ? 119.574 171.274 91.826  1.00 5.46   ? 183  HIS C ND1   1 
ATOM   21875 C  CD2   . HIS C 3  183  ? 119.944 171.031 89.692  1.00 4.09   ? 183  HIS C CD2   1 
ATOM   21876 C  CE1   . HIS C 3  183  ? 118.400 171.185 91.237  1.00 3.58   ? 183  HIS C CE1   1 
ATOM   21877 N  NE2   . HIS C 3  183  ? 118.597 171.038 89.942  1.00 1.98   ? 183  HIS C NE2   1 
ATOM   21878 N  N     . PHE C 3  184  ? 121.204 168.118 90.953  1.00 0.15   ? 184  PHE C N     1 
ATOM   21879 C  CA    . PHE C 3  184  ? 120.787 167.125 89.975  1.00 1.25   ? 184  PHE C CA    1 
ATOM   21880 C  C     . PHE C 3  184  ? 119.276 167.005 90.034  1.00 2.83   ? 184  PHE C C     1 
ATOM   21881 O  O     . PHE C 3  184  ? 118.713 166.863 91.119  1.00 3.72   ? 184  PHE C O     1 
ATOM   21882 C  CB    . PHE C 3  184  ? 121.435 165.764 90.237  1.00 2.85   ? 184  PHE C CB    1 
ATOM   21883 C  CG    . PHE C 3  184  ? 121.097 164.732 89.212  1.00 3.67   ? 184  PHE C CG    1 
ATOM   21884 C  CD1   . PHE C 3  184  ? 121.229 165.005 87.866  1.00 1.60   ? 184  PHE C CD1   1 
ATOM   21885 C  CD2   . PHE C 3  184  ? 120.651 163.488 89.589  1.00 2.44   ? 184  PHE C CD2   1 
ATOM   21886 C  CE1   . PHE C 3  184  ? 120.916 164.065 86.932  1.00 14.64  ? 184  PHE C CE1   1 
ATOM   21887 C  CE2   . PHE C 3  184  ? 120.342 162.548 88.656  1.00 5.74   ? 184  PHE C CE2   1 
ATOM   21888 C  CZ    . PHE C 3  184  ? 120.473 162.833 87.330  1.00 0.64   ? 184  PHE C CZ    1 
ATOM   21889 N  N     . SER C 3  185  ? 118.621 167.079 88.879  1.00 4.52   ? 185  SER C N     1 
ATOM   21890 C  CA    . SER C 3  185  ? 117.173 166.943 88.826  1.00 4.47   ? 185  SER C CA    1 
ATOM   21891 C  C     . SER C 3  185  ? 116.737 166.616 87.409  1.00 4.86   ? 185  SER C C     1 
ATOM   21892 O  O     . SER C 3  185  ? 117.468 166.834 86.446  1.00 7.07   ? 185  SER C O     1 
ATOM   21893 C  CB    . SER C 3  185  ? 116.464 168.208 89.324  1.00 3.29   ? 185  SER C CB    1 
ATOM   21894 O  OG    . SER C 3  185  ? 116.556 169.259 88.390  1.00 8.22   ? 185  SER C OG    1 
ATOM   21895 N  N     . HIS C 3  186  ? 115.527 166.082 87.298  1.00 4.32   ? 186  HIS C N     1 
ATOM   21896 C  CA    . HIS C 3  186  ? 114.888 165.807 86.020  1.00 7.33   ? 186  HIS C CA    1 
ATOM   21897 C  C     . HIS C 3  186  ? 113.799 166.840 85.794  1.00 5.78   ? 186  HIS C C     1 
ATOM   21898 O  O     . HIS C 3  186  ? 113.007 167.118 86.695  1.00 10.20  ? 186  HIS C O     1 
ATOM   21899 C  CB    . HIS C 3  186  ? 114.294 164.403 85.980  1.00 1.52   ? 186  HIS C CB    1 
ATOM   21900 C  CG    . HIS C 3  186  ? 115.190 163.356 86.554  1.00 0.80   ? 186  HIS C CG    1 
ATOM   21901 N  ND1   . HIS C 3  186  ? 116.359 162.960 85.945  1.00 4.92   ? 186  HIS C ND1   1 
ATOM   21902 C  CD2   . HIS C 3  186  ? 115.087 162.623 87.684  1.00 2.17   ? 186  HIS C CD2   1 
ATOM   21903 C  CE1   . HIS C 3  186  ? 116.940 162.032 86.679  1.00 3.96   ? 186  HIS C CE1   1 
ATOM   21904 N  NE2   . HIS C 3  186  ? 116.188 161.809 87.739  1.00 8.46   ? 186  HIS C NE2   1 
ATOM   21905 N  N     . LEU C 3  187  ? 113.778 167.415 84.603  1.00 6.30   ? 187  LEU C N     1 
ATOM   21906 C  CA    . LEU C 3  187  ? 112.873 168.506 84.299  1.00 3.94   ? 187  LEU C CA    1 
ATOM   21907 C  C     . LEU C 3  187  ? 111.583 168.053 83.631  1.00 11.20  ? 187  LEU C C     1 
ATOM   21908 O  O     . LEU C 3  187  ? 110.692 168.877 83.432  1.00 17.75  ? 187  LEU C O     1 
ATOM   21909 C  CB    . LEU C 3  187  ? 113.584 169.530 83.417  1.00 9.79   ? 187  LEU C CB    1 
ATOM   21910 C  CG    . LEU C 3  187  ? 114.874 170.128 83.972  1.00 7.65   ? 187  LEU C CG    1 
ATOM   21911 C  CD1   . LEU C 3  187  ? 115.588 170.914 82.907  1.00 8.09   ? 187  LEU C CD1   1 
ATOM   21912 C  CD2   . LEU C 3  187  ? 114.580 171.001 85.153  1.00 6.57   ? 187  LEU C CD2   1 
ATOM   21913 N  N     . ASP C 3  188  ? 111.453 166.775 83.286  1.00 16.12  ? 188  ASP C N     1 
ATOM   21914 C  CA    . ASP C 3  188  ? 110.251 166.274 82.639  1.00 14.21  ? 188  ASP C CA    1 
ATOM   21915 C  C     . ASP C 3  188  ? 109.433 165.354 83.536  1.00 16.41  ? 188  ASP C C     1 
ATOM   21916 O  O     . ASP C 3  188  ? 108.604 164.595 83.030  1.00 20.99  ? 188  ASP C O     1 
ATOM   21917 C  CB    . ASP C 3  188  ? 110.605 165.563 81.337  1.00 12.56  ? 188  ASP C CB    1 
ATOM   21918 C  CG    . ASP C 3  188  ? 111.591 164.448 81.532  1.00 19.09  ? 188  ASP C CG    1 
ATOM   21919 O  OD1   . ASP C 3  188  ? 112.114 164.311 82.650  1.00 17.91  ? 188  ASP C OD1   1 
ATOM   21920 O  OD2   . ASP C 3  188  ? 111.841 163.701 80.564  1.00 20.30  ? 188  ASP C OD2   1 
ATOM   21921 N  N     . ILE C 3  189  ? 109.655 165.396 84.847  1.00 14.21  ? 189  ILE C N     1 
ATOM   21922 C  CA    . ILE C 3  189  ? 108.814 164.728 85.831  1.00 9.02   ? 189  ILE C CA    1 
ATOM   21923 C  C     . ILE C 3  189  ? 108.280 165.800 86.768  1.00 11.33  ? 189  ILE C C     1 
ATOM   21924 O  O     . ILE C 3  189  ? 109.048 166.628 87.267  1.00 17.70  ? 189  ILE C O     1 
ATOM   21925 C  CB    . ILE C 3  189  ? 109.585 163.647 86.611  1.00 5.46   ? 189  ILE C CB    1 
ATOM   21926 C  CG1   . ILE C 3  189  ? 110.251 162.671 85.657  1.00 9.26   ? 189  ILE C CG1   1 
ATOM   21927 C  CG2   . ILE C 3  189  ? 108.664 162.864 87.516  1.00 9.65   ? 189  ILE C CG2   1 
ATOM   21928 C  CD1   . ILE C 3  189  ? 111.056 161.629 86.348  1.00 9.96   ? 189  ILE C CD1   1 
ATOM   21929 N  N     . GLU C 3  190  ? 106.973 165.801 86.986  1.00 12.79  ? 190  GLU C N     1 
ATOM   21930 C  CA    . GLU C 3  190  ? 106.337 166.791 87.836  1.00 12.56  ? 190  GLU C CA    1 
ATOM   21931 C  C     . GLU C 3  190  ? 106.613 166.474 89.300  1.00 14.31  ? 190  GLU C C     1 
ATOM   21932 O  O     . GLU C 3  190  ? 107.014 165.367 89.652  1.00 20.01  ? 190  GLU C O     1 
ATOM   21933 C  CB    . GLU C 3  190  ? 104.827 166.843 87.592  1.00 15.16  ? 190  GLU C CB    1 
ATOM   21934 C  CG    . GLU C 3  190  ? 104.353 166.667 86.146  1.00 19.40  ? 190  GLU C CG    1 
ATOM   21935 C  CD    . GLU C 3  190  ? 104.587 165.257 85.580  1.00 29.23  ? 190  GLU C CD    1 
ATOM   21936 O  OE1   . GLU C 3  190  ? 104.705 165.121 84.343  1.00 27.59  ? 190  GLU C OE1   1 
ATOM   21937 O  OE2   . GLU C 3  190  ? 104.662 164.290 86.369  1.00 20.55  ? 190  GLU C OE2   1 
ATOM   21938 N  N     . GLN C 3  191  ? 106.394 167.462 90.164  1.00 14.56  ? 191  GLN C N     1 
ATOM   21939 C  CA    . GLN C 3  191  ? 106.691 167.309 91.579  1.00 10.39  ? 191  GLN C CA    1 
ATOM   21940 C  C     . GLN C 3  191  ? 105.532 167.768 92.446  1.00 11.86  ? 191  GLN C C     1 
ATOM   21941 O  O     . GLN C 3  191  ? 104.781 168.672 92.084  1.00 19.96  ? 191  GLN C O     1 
ATOM   21942 C  CB    . GLN C 3  191  ? 107.944 168.084 91.975  1.00 16.15  ? 191  GLN C CB    1 
ATOM   21943 C  CG    . GLN C 3  191  ? 109.145 167.775 91.123  1.00 12.47  ? 191  GLN C CG    1 
ATOM   21944 C  CD    . GLN C 3  191  ? 110.438 168.022 91.838  1.00 17.38  ? 191  GLN C CD    1 
ATOM   21945 O  OE1   . GLN C 3  191  ? 110.556 167.763 93.030  1.00 16.60  ? 191  GLN C OE1   1 
ATOM   21946 N  NE2   . GLN C 3  191  ? 111.423 168.531 91.116  1.00 18.25  ? 191  GLN C NE2   1 
ATOM   21947 N  N     . TYR C 3  192  ? 105.400 167.126 93.598  1.00 15.72  ? 192  TYR C N     1 
ATOM   21948 C  CA    . TYR C 3  192  ? 104.500 167.547 94.657  1.00 16.39  ? 192  TYR C CA    1 
ATOM   21949 C  C     . TYR C 3  192  ? 105.092 168.715 95.430  1.00 21.83  ? 192  TYR C C     1 
ATOM   21950 O  O     . TYR C 3  192  ? 106.305 168.922 95.427  1.00 21.49  ? 192  TYR C O     1 
ATOM   21951 C  CB    . TYR C 3  192  ? 104.262 166.411 95.642  1.00 19.56  ? 192  TYR C CB    1 
ATOM   21952 C  CG    . TYR C 3  192  ? 103.566 165.201 95.104  1.00 21.83  ? 192  TYR C CG    1 
ATOM   21953 C  CD1   . TYR C 3  192  ? 102.314 165.295 94.524  1.00 23.66  ? 192  TYR C CD1   1 
ATOM   21954 C  CD2   . TYR C 3  192  ? 104.146 163.952 95.211  1.00 17.50  ? 192  TYR C CD2   1 
ATOM   21955 C  CE1   . TYR C 3  192  ? 101.670 164.180 94.048  1.00 23.35  ? 192  TYR C CE1   1 
ATOM   21956 C  CE2   . TYR C 3  192  ? 103.515 162.834 94.738  1.00 20.48  ? 192  TYR C CE2   1 
ATOM   21957 C  CZ    . TYR C 3  192  ? 102.276 162.950 94.158  1.00 26.28  ? 192  TYR C CZ    1 
ATOM   21958 O  OH    . TYR C 3  192  ? 101.639 161.833 93.682  1.00 24.94  ? 192  TYR C OH    1 
ATOM   21959 N  N     . PRO C 3  193  ? 104.258 169.486 96.118  1.00 32.94  ? 193  PRO C N     1 
ATOM   21960 C  CA    . PRO C 3  193  ? 104.780 170.355 97.178  1.00 31.39  ? 193  PRO C CA    1 
ATOM   21961 C  C     . PRO C 3  193  ? 105.051 169.554 98.440  1.00 30.66  ? 193  PRO C C     1 
ATOM   21962 O  O     . PRO C 3  193  ? 104.117 169.181 99.151  1.00 34.47  ? 193  PRO C O     1 
ATOM   21963 C  CB    . PRO C 3  193  ? 103.654 171.374 97.389  1.00 31.29  ? 193  PRO C CB    1 
ATOM   21964 C  CG    . PRO C 3  193  ? 102.737 171.206 96.228  1.00 32.85  ? 193  PRO C CG    1 
ATOM   21965 C  CD    . PRO C 3  193  ? 102.848 169.774 95.833  1.00 31.15  ? 193  PRO C CD    1 
ATOM   21966 N  N     . THR C 3  194  ? 106.314 169.287 98.736  1.00 29.47  ? 194  THR C N     1 
ATOM   21967 C  CA    . THR C 3  194  ? 106.668 168.380 99.817  1.00 30.28  ? 194  THR C CA    1 
ATOM   21968 C  C     . THR C 3  194  ? 106.803 169.076 101.162 1.00 29.37  ? 194  THR C C     1 
ATOM   21969 O  O     . THR C 3  194  ? 107.163 168.421 102.142 1.00 27.19  ? 194  THR C O     1 
ATOM   21970 C  CB    . THR C 3  194  ? 107.966 167.635 99.483  1.00 25.52  ? 194  THR C CB    1 
ATOM   21971 O  OG1   . THR C 3  194  ? 108.834 168.494 98.738  1.00 28.58  ? 194  THR C OG1   1 
ATOM   21972 C  CG2   . THR C 3  194  ? 107.670 166.402 98.659  1.00 19.27  ? 194  THR C CG2   1 
ATOM   21973 N  N     . ASP C 3  195  ? 106.542 170.385 101.230 1.00 35.85  ? 195  ASP C N     1 
ATOM   21974 C  CA    . ASP C 3  195  ? 106.442 171.054 102.522 1.00 33.24  ? 195  ASP C CA    1 
ATOM   21975 C  C     . ASP C 3  195  ? 105.193 170.634 103.280 1.00 34.57  ? 195  ASP C C     1 
ATOM   21976 O  O     . ASP C 3  195  ? 105.194 170.651 104.512 1.00 40.87  ? 195  ASP C O     1 
ATOM   21977 C  CB    . ASP C 3  195  ? 106.437 172.571 102.355 1.00 34.18  ? 195  ASP C CB    1 
ATOM   21978 C  CG    . ASP C 3  195  ? 105.354 173.050 101.421 1.00 37.52  ? 195  ASP C CG    1 
ATOM   21979 O  OD1   . ASP C 3  195  ? 104.724 172.210 100.748 1.00 39.33  ? 195  ASP C OD1   1 
ATOM   21980 O  OD2   . ASP C 3  195  ? 105.109 174.273 101.375 1.00 39.42  ? 195  ASP C OD2   1 
ATOM   21981 N  N     . LYS C 3  196  ? 104.129 170.274 102.574 1.00 29.89  ? 196  LYS C N     1 
ATOM   21982 C  CA    . LYS C 3  196  ? 102.948 169.747 103.235 1.00 28.23  ? 196  LYS C CA    1 
ATOM   21983 C  C     . LYS C 3  196  ? 103.277 168.433 103.920 1.00 26.97  ? 196  LYS C C     1 
ATOM   21984 O  O     . LYS C 3  196  ? 103.895 167.546 103.331 1.00 29.17  ? 196  LYS C O     1 
ATOM   21985 C  CB    . LYS C 3  196  ? 101.821 169.543 102.228 1.00 29.42  ? 196  LYS C CB    1 
ATOM   21986 C  CG    . LYS C 3  196  ? 101.228 170.833 101.714 1.00 31.41  ? 196  LYS C CG    1 
ATOM   21987 C  CD    . LYS C 3  196  ? 100.259 170.591 100.576 1.00 32.17  ? 196  LYS C CD    1 
ATOM   21988 C  CE    . LYS C 3  196  ? 99.513  171.873 100.234 1.00 31.22  ? 196  LYS C CE    1 
ATOM   21989 N  NZ    . LYS C 3  196  ? 100.431 172.963 99.796  1.00 33.49  ? 196  LYS C NZ    1 
ATOM   21990 N  N     . LYS C 3  197  ? 102.836 168.298 105.164 1.00 31.83  ? 197  LYS C N     1 
ATOM   21991 C  CA    . LYS C 3  197  ? 103.108 167.094 105.933 1.00 30.58  ? 197  LYS C CA    1 
ATOM   21992 C  C     . LYS C 3  197  ? 102.398 165.871 105.373 1.00 25.37  ? 197  LYS C C     1 
ATOM   21993 O  O     . LYS C 3  197  ? 102.516 164.785 105.946 1.00 26.34  ? 197  LYS C O     1 
ATOM   21994 C  CB    . LYS C 3  197  ? 102.737 167.320 107.402 1.00 27.56  ? 197  LYS C CB    1 
ATOM   21995 C  CG    . LYS C 3  197  ? 103.795 168.137 108.157 1.00 28.04  ? 197  LYS C CG    1 
ATOM   21996 C  CD    . LYS C 3  197  ? 103.381 168.482 109.577 1.00 25.18  ? 197  LYS C CD    1 
ATOM   21997 C  CE    . LYS C 3  197  ? 103.866 167.439 110.561 1.00 28.47  ? 197  LYS C CE    1 
ATOM   21998 N  NZ    . LYS C 3  197  ? 103.410 167.731 111.943 1.00 30.08  ? 197  LYS C NZ    1 
ATOM   21999 N  N     . GLU C 3  198  ? 101.661 166.028 104.275 1.00 25.53  ? 198  GLU C N     1 
ATOM   22000 C  CA    . GLU C 3  198  ? 101.076 164.891 103.578 1.00 27.04  ? 198  GLU C CA    1 
ATOM   22001 C  C     . GLU C 3  198  ? 102.083 164.202 102.667 1.00 25.09  ? 198  GLU C C     1 
ATOM   22002 O  O     . GLU C 3  198  ? 101.979 162.996 102.434 1.00 26.76  ? 198  GLU C O     1 
ATOM   22003 C  CB    . GLU C 3  198  ? 99.863  165.364 102.781 1.00 27.32  ? 198  GLU C CB    1 
ATOM   22004 C  CG    . GLU C 3  198  ? 99.203  164.310 101.931 1.00 31.26  ? 198  GLU C CG    1 
ATOM   22005 C  CD    . GLU C 3  198  ? 98.170  164.900 101.004 1.00 31.63  ? 198  GLU C CD    1 
ATOM   22006 O  OE1   . GLU C 3  198  ? 97.986  166.134 101.048 1.00 30.43  ? 198  GLU C OE1   1 
ATOM   22007 O  OE2   . GLU C 3  198  ? 97.542  164.138 100.239 1.00 31.02  ? 198  GLU C OE2   1 
ATOM   22008 N  N     . TYR C 3  199  ? 103.054 164.944 102.137 1.00 22.73  ? 199  TYR C N     1 
ATOM   22009 C  CA    . TYR C 3  199  ? 104.005 164.421 101.170 1.00 9.94   ? 199  TYR C CA    1 
ATOM   22010 C  C     . TYR C 3  199  ? 105.451 164.433 101.634 1.00 10.99  ? 199  TYR C C     1 
ATOM   22011 O  O     . TYR C 3  199  ? 106.340 164.264 100.801 1.00 20.57  ? 199  TYR C O     1 
ATOM   22012 C  CB    . TYR C 3  199  ? 103.933 165.216 99.864  1.00 17.02  ? 199  TYR C CB    1 
ATOM   22013 C  CG    . TYR C 3  199  ? 102.598 165.239 99.182  1.00 20.94  ? 199  TYR C CG    1 
ATOM   22014 C  CD1   . TYR C 3  199  ? 102.009 164.073 98.729  1.00 21.67  ? 199  TYR C CD1   1 
ATOM   22015 C  CD2   . TYR C 3  199  ? 101.937 166.434 98.963  1.00 21.96  ? 199  TYR C CD2   1 
ATOM   22016 C  CE1   . TYR C 3  199  ? 100.795 164.095 98.093  1.00 23.05  ? 199  TYR C CE1   1 
ATOM   22017 C  CE2   . TYR C 3  199  ? 100.725 166.466 98.328  1.00 19.72  ? 199  TYR C CE2   1 
ATOM   22018 C  CZ    . TYR C 3  199  ? 100.157 165.296 97.895  1.00 25.91  ? 199  TYR C CZ    1 
ATOM   22019 O  OH    . TYR C 3  199  ? 98.940  165.330 97.260  1.00 32.62  ? 199  TYR C OH    1 
ATOM   22020 N  N     . MET C 3  200  ? 105.724 164.649 102.918 1.00 10.96  ? 200  MET C N     1 
ATOM   22021 C  CA    . MET C 3  200  ? 107.101 164.856 103.342 1.00 7.75   ? 200  MET C CA    1 
ATOM   22022 C  C     . MET C 3  200  ? 107.879 163.565 103.545 1.00 4.38   ? 200  MET C C     1 
ATOM   22023 O  O     . MET C 3  200  ? 109.089 163.629 103.763 1.00 5.26   ? 200  MET C O     1 
ATOM   22024 C  CB    . MET C 3  200  ? 107.135 165.704 104.609 1.00 7.73   ? 200  MET C CB    1 
ATOM   22025 C  CG    . MET C 3  200  ? 106.341 165.166 105.764 1.00 9.07   ? 200  MET C CG    1 
ATOM   22026 S  SD    . MET C 3  200  ? 106.646 166.130 107.246 1.00 14.49  ? 200  MET C SD    1 
ATOM   22027 C  CE    . MET C 3  200  ? 106.340 164.914 108.507 1.00 4.04   ? 200  MET C CE    1 
ATOM   22028 N  N     . ALA C 3  201  ? 107.235 162.408 103.486 1.00 3.88   ? 201  ALA C N     1 
ATOM   22029 C  CA    . ALA C 3  201  ? 107.961 161.151 103.514 1.00 1.02   ? 201  ALA C CA    1 
ATOM   22030 C  C     . ALA C 3  201  ? 108.340 160.662 102.127 1.00 3.11   ? 201  ALA C C     1 
ATOM   22031 O  O     . ALA C 3  201  ? 109.107 159.705 102.012 1.00 2.45   ? 201  ALA C O     1 
ATOM   22032 C  CB    . ALA C 3  201  ? 107.137 160.081 104.227 1.00 3.11   ? 201  ALA C CB    1 
ATOM   22033 N  N     . LEU C 3  202  ? 107.842 161.310 101.087 1.00 1.48   ? 202  LEU C N     1 
ATOM   22034 C  CA    . LEU C 3  202  ? 108.041 160.920 99.706  1.00 2.65   ? 202  LEU C CA    1 
ATOM   22035 C  C     . LEU C 3  202  ? 109.127 161.767 99.067  1.00 3.21   ? 202  LEU C C     1 
ATOM   22036 O  O     . LEU C 3  202  ? 109.479 162.835 99.561  1.00 5.64   ? 202  LEU C O     1 
ATOM   22037 C  CB    . LEU C 3  202  ? 106.738 161.067 98.923  1.00 13.78  ? 202  LEU C CB    1 
ATOM   22038 C  CG    . LEU C 3  202  ? 105.489 160.463 99.548  1.00 9.22   ? 202  LEU C CG    1 
ATOM   22039 C  CD1   . LEU C 3  202  ? 104.327 160.652 98.612  1.00 2.90   ? 202  LEU C CD1   1 
ATOM   22040 C  CD2   . LEU C 3  202  ? 105.692 159.001 99.849  1.00 10.44  ? 202  LEU C CD2   1 
ATOM   22041 N  N     . SER C 3  203  ? 109.663 161.269 97.954  1.00 14.02  ? 203  SER C N     1 
ATOM   22042 C  CA    . SER C 3  203  ? 110.712 161.999 97.254  1.00 5.86   ? 203  SER C CA    1 
ATOM   22043 C  C     . SER C 3  203  ? 110.207 163.337 96.736  1.00 2.48   ? 203  SER C C     1 
ATOM   22044 O  O     . SER C 3  203  ? 110.877 164.361 96.888  1.00 9.29   ? 203  SER C O     1 
ATOM   22045 C  CB    . SER C 3  203  ? 111.268 161.162 96.105  1.00 0.93   ? 203  SER C CB    1 
ATOM   22046 O  OG    . SER C 3  203  ? 110.435 161.216 94.973  1.00 0.03   ? 203  SER C OG    1 
ATOM   22047 N  N     . GLY C 3  204  ? 109.024 163.356 96.143  1.00 4.75   ? 204  GLY C N     1 
ATOM   22048 C  CA    . GLY C 3  204  ? 108.501 164.579 95.583  1.00 2.59   ? 204  GLY C CA    1 
ATOM   22049 C  C     . GLY C 3  204  ? 108.090 164.430 94.140  1.00 0.92   ? 204  GLY C C     1 
ATOM   22050 O  O     . GLY C 3  204  ? 107.153 165.082 93.692  1.00 13.56  ? 204  GLY C O     1 
ATOM   22051 N  N     . TYR C 3  205  ? 108.795 163.586 93.404  1.00 2.70   ? 205  TYR C N     1 
ATOM   22052 C  CA    . TYR C 3  205  ? 108.431 163.276 92.034  1.00 2.86   ? 205  TYR C CA    1 
ATOM   22053 C  C     . TYR C 3  205  ? 107.099 162.542 91.983  1.00 7.26   ? 205  TYR C C     1 
ATOM   22054 O  O     . TYR C 3  205  ? 106.765 161.756 92.867  1.00 13.00  ? 205  TYR C O     1 
ATOM   22055 C  CB    . TYR C 3  205  ? 109.520 162.431 91.383  1.00 7.47   ? 205  TYR C CB    1 
ATOM   22056 C  CG    . TYR C 3  205  ? 110.753 163.211 91.029  1.00 6.00   ? 205  TYR C CG    1 
ATOM   22057 C  CD1   . TYR C 3  205  ? 110.703 164.225 90.095  1.00 8.62   ? 205  TYR C CD1   1 
ATOM   22058 C  CD2   . TYR C 3  205  ? 111.962 162.934 91.623  1.00 3.44   ? 205  TYR C CD2   1 
ATOM   22059 C  CE1   . TYR C 3  205  ? 111.812 164.935 89.769  1.00 3.80   ? 205  TYR C CE1   1 
ATOM   22060 C  CE2   . TYR C 3  205  ? 113.078 163.640 91.301  1.00 3.06   ? 205  TYR C CE2   1 
ATOM   22061 C  CZ    . TYR C 3  205  ? 112.997 164.643 90.370  1.00 5.44   ? 205  TYR C CZ    1 
ATOM   22062 O  OH    . TYR C 3  205  ? 114.108 165.368 90.038  1.00 7.46   ? 205  TYR C OH    1 
ATOM   22063 N  N     . LYS C 3  206  ? 106.335 162.801 90.930  1.00 6.24   ? 206  LYS C N     1 
ATOM   22064 C  CA    . LYS C 3  206  ? 104.996 162.247 90.798  1.00 6.81   ? 206  LYS C CA    1 
ATOM   22065 C  C     . LYS C 3  206  ? 104.968 160.885 90.124  1.00 10.10  ? 206  LYS C C     1 
ATOM   22066 O  O     . LYS C 3  206  ? 103.888 160.311 89.977  1.00 17.95  ? 206  LYS C O     1 
ATOM   22067 C  CB    . LYS C 3  206  ? 104.103 163.218 90.033  1.00 12.16  ? 206  LYS C CB    1 
ATOM   22068 C  CG    . LYS C 3  206  ? 103.615 164.354 90.882  1.00 13.77  ? 206  LYS C CG    1 
ATOM   22069 C  CD    . LYS C 3  206  ? 102.703 165.271 90.126  1.00 13.49  ? 206  LYS C CD    1 
ATOM   22070 C  CE    . LYS C 3  206  ? 102.191 166.362 91.031  1.00 15.90  ? 206  LYS C CE    1 
ATOM   22071 N  NZ    . LYS C 3  206  ? 101.342 167.329 90.301  1.00 16.88  ? 206  LYS C NZ    1 
ATOM   22072 N  N     . GLN C 3  207  ? 106.114 160.354 89.718  1.00 7.41   ? 207  GLN C N     1 
ATOM   22073 C  CA    . GLN C 3  207  ? 106.217 159.016 89.165  1.00 4.30   ? 207  GLN C CA    1 
ATOM   22074 C  C     . GLN C 3  207  ? 107.190 158.211 90.009  1.00 5.64   ? 207  GLN C C     1 
ATOM   22075 O  O     . GLN C 3  207  ? 108.116 158.766 90.595  1.00 9.74   ? 207  GLN C O     1 
ATOM   22076 C  CB    . GLN C 3  207  ? 106.687 159.045 87.715  1.00 3.75   ? 207  GLN C CB    1 
ATOM   22077 C  CG    . GLN C 3  207  ? 105.996 160.071 86.856  1.00 5.46   ? 207  GLN C CG    1 
ATOM   22078 C  CD    . GLN C 3  207  ? 106.494 160.060 85.429  1.00 14.49  ? 207  GLN C CD    1 
ATOM   22079 O  OE1   . GLN C 3  207  ? 107.139 159.115 84.997  1.00 18.04  ? 207  GLN C OE1   1 
ATOM   22080 N  NE2   . GLN C 3  207  ? 106.225 161.131 84.701  1.00 15.42  ? 207  GLN C NE2   1 
ATOM   22081 N  N     . SER C 3  208  ? 106.964 156.909 90.094  1.00 8.27   ? 208  SER C N     1 
ATOM   22082 C  CA    . SER C 3  208  ? 107.916 156.033 90.753  1.00 1.92   ? 208  SER C CA    1 
ATOM   22083 C  C     . SER C 3  208  ? 109.174 155.901 89.911  1.00 7.16   ? 208  SER C C     1 
ATOM   22084 O  O     . SER C 3  208  ? 109.135 155.995 88.686  1.00 14.51  ? 208  SER C O     1 
ATOM   22085 C  CB    . SER C 3  208  ? 107.297 154.659 90.986  1.00 7.05   ? 208  SER C CB    1 
ATOM   22086 O  OG    . SER C 3  208  ? 108.212 153.784 91.604  1.00 11.73  ? 208  SER C OG    1 
ATOM   22087 N  N     . SER C 3  209  ? 110.309 155.695 90.574  1.00 7.12   ? 209  SER C N     1 
ATOM   22088 C  CA    . SER C 3  209  ? 111.532 155.478 89.821  1.00 1.73   ? 209  SER C CA    1 
ATOM   22089 C  C     . SER C 3  209  ? 111.599 154.089 89.211  1.00 2.75   ? 209  SER C C     1 
ATOM   22090 O  O     . SER C 3  209  ? 112.508 153.825 88.425  1.00 13.86  ? 209  SER C O     1 
ATOM   22091 C  CB    . SER C 3  209  ? 112.758 155.742 90.691  1.00 12.11  ? 209  SER C CB    1 
ATOM   22092 O  OG    . SER C 3  209  ? 112.684 155.085 91.929  1.00 2.12   ? 209  SER C OG    1 
ATOM   22093 N  N     . MET C 3  210  ? 110.665 153.207 89.545  1.00 5.14   ? 210  MET C N     1 
ATOM   22094 C  CA    . MET C 3  210  ? 110.568 151.904 88.911  1.00 11.88  ? 210  MET C CA    1 
ATOM   22095 C  C     . MET C 3  210  ? 109.792 151.920 87.605  1.00 0.71   ? 210  MET C C     1 
ATOM   22096 O  O     . MET C 3  210  ? 109.692 150.879 86.961  1.00 7.40   ? 210  MET C O     1 
ATOM   22097 C  CB    . MET C 3  210  ? 109.934 150.897 89.862  1.00 0.32   ? 210  MET C CB    1 
ATOM   22098 C  CG    . MET C 3  210  ? 110.747 150.625 91.091  1.00 3.04   ? 210  MET C CG    1 
ATOM   22099 S  SD    . MET C 3  210  ? 111.934 149.324 90.733  1.00 19.85  ? 210  MET C SD    1 
ATOM   22100 C  CE    . MET C 3  210  ? 112.104 148.579 92.328  1.00 6.35   ? 210  MET C CE    1 
ATOM   22101 N  N     . THR C 3  211  ? 109.232 153.052 87.205  1.00 4.10   ? 211  THR C N     1 
ATOM   22102 C  CA    . THR C 3  211  ? 108.522 153.152 85.940  1.00 3.17   ? 211  THR C CA    1 
ATOM   22103 C  C     . THR C 3  211  ? 108.870 154.385 85.133  1.00 8.20   ? 211  THR C C     1 
ATOM   22104 O  O     . THR C 3  211  ? 108.606 154.393 83.928  1.00 14.79  ? 211  THR C O     1 
ATOM   22105 C  CB    . THR C 3  211  ? 106.999 153.131 86.158  1.00 3.66   ? 211  THR C CB    1 
ATOM   22106 O  OG1   . THR C 3  211  ? 106.645 154.029 87.212  1.00 10.87  ? 211  THR C OG1   1 
ATOM   22107 C  CG2   . THR C 3  211  ? 106.520 151.758 86.509  1.00 5.58   ? 211  THR C CG2   1 
ATOM   22108 N  N     . SER C 3  212  ? 109.447 155.417 85.738  1.00 8.22   ? 212  SER C N     1 
ATOM   22109 C  CA    . SER C 3  212  ? 109.751 156.647 85.024  1.00 9.72   ? 212  SER C CA    1 
ATOM   22110 C  C     . SER C 3  212  ? 110.999 156.482 84.177  1.00 9.17   ? 212  SER C C     1 
ATOM   22111 O  O     . SER C 3  212  ? 111.903 155.720 84.519  1.00 19.70  ? 212  SER C O     1 
ATOM   22112 C  CB    . SER C 3  212  ? 109.937 157.805 86.000  1.00 7.31   ? 212  SER C CB    1 
ATOM   22113 O  OG    . SER C 3  212  ? 111.173 157.711 86.667  1.00 6.17   ? 212  SER C OG    1 
ATOM   22114 N  N     . ASP C 3  213  ? 111.029 157.185 83.049  1.00 13.61  ? 213  ASP C N     1 
ATOM   22115 C  CA    . ASP C 3  213  ? 112.178 157.213 82.147  1.00 12.60  ? 213  ASP C CA    1 
ATOM   22116 C  C     . ASP C 3  213  ? 112.449 158.647 81.712  1.00 13.53  ? 213  ASP C C     1 
ATOM   22117 O  O     . ASP C 3  213  ? 112.089 159.048 80.601  1.00 19.95  ? 213  ASP C O     1 
ATOM   22118 C  CB    . ASP C 3  213  ? 111.937 156.315 80.936  1.00 14.17  ? 213  ASP C CB    1 
ATOM   22119 C  CG    . ASP C 3  213  ? 113.164 156.157 80.087  1.00 24.71  ? 213  ASP C CG    1 
ATOM   22120 O  OD1   . ASP C 3  213  ? 114.276 156.241 80.641  1.00 31.69  ? 213  ASP C OD1   1 
ATOM   22121 O  OD2   . ASP C 3  213  ? 113.025 155.954 78.865  1.00 25.18  ? 213  ASP C OD2   1 
ATOM   22122 N  N     . PRO C 3  214  ? 113.077 159.449 82.568  1.00 16.31  ? 214  PRO C N     1 
ATOM   22123 C  CA    . PRO C 3  214  ? 113.288 160.862 82.235  1.00 10.16  ? 214  PRO C CA    1 
ATOM   22124 C  C     . PRO C 3  214  ? 114.362 161.053 81.178  1.00 14.22  ? 214  PRO C C     1 
ATOM   22125 O  O     . PRO C 3  214  ? 115.319 160.284 81.092  1.00 21.38  ? 214  PRO C O     1 
ATOM   22126 C  CB    . PRO C 3  214  ? 113.703 161.472 83.571  1.00 7.78   ? 214  PRO C CB    1 
ATOM   22127 C  CG    . PRO C 3  214  ? 114.310 160.357 84.307  1.00 9.38   ? 214  PRO C CG    1 
ATOM   22128 C  CD    . PRO C 3  214  ? 113.637 159.105 83.882  1.00 13.55  ? 214  PRO C CD    1 
ATOM   22129 N  N     . ARG C 3  215  ? 114.196 162.098 80.366  1.00 15.84  ? 215  ARG C N     1 
ATOM   22130 C  CA    . ARG C 3  215  ? 115.128 162.397 79.285  1.00 14.15  ? 215  ARG C CA    1 
ATOM   22131 C  C     . ARG C 3  215  ? 115.408 163.891 79.190  1.00 10.75  ? 215  ARG C C     1 
ATOM   22132 O  O     . ARG C 3  215  ? 115.732 164.399 78.122  1.00 16.15  ? 215  ARG C O     1 
ATOM   22133 C  CB    . ARG C 3  215  ? 114.608 161.858 77.954  1.00 11.78  ? 215  ARG C CB    1 
ATOM   22134 C  CG    . ARG C 3  215  ? 114.489 160.353 77.934  1.00 11.49  ? 215  ARG C CG    1 
ATOM   22135 C  CD    . ARG C 3  215  ? 114.334 159.808 76.553  1.00 14.19  ? 215  ARG C CD    1 
ATOM   22136 N  NE    . ARG C 3  215  ? 115.596 159.706 75.834  1.00 21.44  ? 215  ARG C NE    1 
ATOM   22137 C  CZ    . ARG C 3  215  ? 116.484 158.740 76.014  1.00 18.18  ? 215  ARG C CZ    1 
ATOM   22138 N  NH1   . ARG C 3  215  ? 116.298 157.790 76.912  1.00 16.34  ? 215  ARG C NH1   1 
ATOM   22139 N  NH2   . ARG C 3  215  ? 117.579 158.720 75.264  1.00 19.49  ? 215  ARG C NH2   1 
ATOM   22140 N  N     . HIS C 3  216  ? 115.310 164.599 80.305  1.00 8.65   ? 216  HIS C N     1 
ATOM   22141 C  CA    . HIS C 3  216  ? 115.524 166.040 80.350  1.00 8.67   ? 216  HIS C CA    1 
ATOM   22142 C  C     . HIS C 3  216  ? 116.046 166.349 81.744  1.00 10.16  ? 216  HIS C C     1 
ATOM   22143 O  O     . HIS C 3  216  ? 115.323 166.167 82.722  1.00 9.35   ? 216  HIS C O     1 
ATOM   22144 C  CB    . HIS C 3  216  ? 114.227 166.781 80.050  1.00 11.61  ? 216  HIS C CB    1 
ATOM   22145 C  CG    . HIS C 3  216  ? 114.385 168.255 79.875  1.00 13.54  ? 216  HIS C CG    1 
ATOM   22146 N  ND1   . HIS C 3  216  ? 115.555 168.835 79.441  1.00 19.00  ? 216  HIS C ND1   1 
ATOM   22147 C  CD2   . HIS C 3  216  ? 113.506 169.267 80.048  1.00 9.65   ? 216  HIS C CD2   1 
ATOM   22148 C  CE1   . HIS C 3  216  ? 115.396 170.143 79.373  1.00 14.99  ? 216  HIS C CE1   1 
ATOM   22149 N  NE2   . HIS C 3  216  ? 114.160 170.431 79.735  1.00 11.29  ? 216  HIS C NE2   1 
ATOM   22150 N  N     . HIS C 3  217  ? 117.296 166.787 81.843  1.00 4.98   ? 217  HIS C N     1 
ATOM   22151 C  CA    . HIS C 3  217  ? 117.988 166.836 83.120  1.00 2.93   ? 217  HIS C CA    1 
ATOM   22152 C  C     . HIS C 3  217  ? 118.652 168.185 83.333  1.00 3.94   ? 217  HIS C C     1 
ATOM   22153 O  O     . HIS C 3  217  ? 118.911 168.931 82.393  1.00 15.45  ? 217  HIS C O     1 
ATOM   22154 C  CB    . HIS C 3  217  ? 119.052 165.739 83.226  1.00 4.20   ? 217  HIS C CB    1 
ATOM   22155 C  CG    . HIS C 3  217  ? 118.647 164.439 82.613  1.00 6.42   ? 217  HIS C CG    1 
ATOM   22156 N  ND1   . HIS C 3  217  ? 117.923 163.488 83.293  1.00 5.78   ? 217  HIS C ND1   1 
ATOM   22157 C  CD2   . HIS C 3  217  ? 118.871 163.929 81.382  1.00 8.96   ? 217  HIS C CD2   1 
ATOM   22158 C  CE1   . HIS C 3  217  ? 117.717 162.450 82.507  1.00 5.15   ? 217  HIS C CE1   1 
ATOM   22159 N  NE2   . HIS C 3  217  ? 118.282 162.692 81.342  1.00 6.62   ? 217  HIS C NE2   1 
ATOM   22160 N  N     . ARG C 3  218  ? 118.918 168.483 84.600  1.00 3.78   ? 218  ARG C N     1 
ATOM   22161 C  CA    . ARG C 3  218  ? 119.726 169.624 85.002  1.00 5.50   ? 218  ARG C CA    1 
ATOM   22162 C  C     . ARG C 3  218  ? 120.790 169.129 85.968  1.00 4.42   ? 218  ARG C C     1 
ATOM   22163 O  O     . ARG C 3  218  ? 120.467 168.512 86.984  1.00 6.90   ? 218  ARG C O     1 
ATOM   22164 C  CB    . ARG C 3  218  ? 118.866 170.709 85.648  1.00 2.10   ? 218  ARG C CB    1 
ATOM   22165 C  CG    . ARG C 3  218  ? 119.635 171.907 86.125  1.00 4.47   ? 218  ARG C CG    1 
ATOM   22166 C  CD    . ARG C 3  218  ? 118.700 173.018 86.523  1.00 4.01   ? 218  ARG C CD    1 
ATOM   22167 N  NE    . ARG C 3  218  ? 118.089 173.635 85.356  1.00 7.95   ? 218  ARG C NE    1 
ATOM   22168 C  CZ    . ARG C 3  218  ? 116.891 174.198 85.344  1.00 9.60   ? 218  ARG C CZ    1 
ATOM   22169 N  NH1   . ARG C 3  218  ? 116.135 174.235 86.424  1.00 6.80   ? 218  ARG C NH1   1 
ATOM   22170 N  NH2   . ARG C 3  218  ? 116.438 174.731 84.216  1.00 7.45   ? 218  ARG C NH2   1 
ATOM   22171 N  N     . LEU C 3  219  ? 122.052 169.390 85.649  1.00 8.77   ? 219  LEU C N     1 
ATOM   22172 C  CA    . LEU C 3  219  ? 123.185 168.931 86.434  1.00 7.12   ? 219  LEU C CA    1 
ATOM   22173 C  C     . LEU C 3  219  ? 124.035 170.119 86.849  1.00 7.68   ? 219  LEU C C     1 
ATOM   22174 O  O     . LEU C 3  219  ? 124.361 170.968 86.023  1.00 11.55  ? 219  LEU C O     1 
ATOM   22175 C  CB    . LEU C 3  219  ? 124.024 167.940 85.630  1.00 3.05   ? 219  LEU C CB    1 
ATOM   22176 C  CG    . LEU C 3  219  ? 125.364 167.490 86.207  1.00 4.30   ? 219  LEU C CG    1 
ATOM   22177 C  CD1   . LEU C 3  219  ? 125.156 166.704 87.467  1.00 3.71   ? 219  LEU C CD1   1 
ATOM   22178 C  CD2   . LEU C 3  219  ? 126.125 166.682 85.192  1.00 2.02   ? 219  LEU C CD2   1 
ATOM   22179 N  N     . GLY C 3  220  ? 124.400 170.169 88.122  1.00 3.58   ? 220  GLY C N     1 
ATOM   22180 C  CA    . GLY C 3  220  ? 125.252 171.222 88.630  1.00 0.71   ? 220  GLY C CA    1 
ATOM   22181 C  C     . GLY C 3  220  ? 126.483 170.697 89.332  1.00 1.60   ? 220  GLY C C     1 
ATOM   22182 O  O     . GLY C 3  220  ? 126.379 169.854 90.219  1.00 2.27   ? 220  GLY C O     1 
ATOM   22183 N  N     . LEU C 3  221  ? 127.655 171.181 88.941  1.00 1.97   ? 221  LEU C N     1 
ATOM   22184 C  CA    . LEU C 3  221  ? 128.920 170.753 89.515  1.00 13.72  ? 221  LEU C CA    1 
ATOM   22185 C  C     . LEU C 3  221  ? 129.765 171.971 89.838  1.00 3.88   ? 221  LEU C C     1 
ATOM   22186 O  O     . LEU C 3  221  ? 129.689 172.991 89.158  1.00 8.83   ? 221  LEU C O     1 
ATOM   22187 C  CB    . LEU C 3  221  ? 129.692 169.841 88.563  1.00 0.50   ? 221  LEU C CB    1 
ATOM   22188 C  CG    . LEU C 3  221  ? 129.040 168.529 88.141  1.00 1.91   ? 221  LEU C CG    1 
ATOM   22189 C  CD1   . LEU C 3  221  ? 129.709 168.020 86.902  1.00 1.74   ? 221  LEU C CD1   1 
ATOM   22190 C  CD2   . LEU C 3  221  ? 129.121 167.509 89.247  1.00 3.49   ? 221  LEU C CD2   1 
ATOM   22191 N  N     . CYS C 3  222  ? 130.576 171.859 90.880  1.00 1.87   ? 222  CYS C N     1 
ATOM   22192 C  CA    . CYS C 3  222  ? 131.473 172.927 91.291  1.00 10.66  ? 222  CYS C CA    1 
ATOM   22193 C  C     . CYS C 3  222  ? 132.907 172.449 91.133  1.00 1.92   ? 222  CYS C C     1 
ATOM   22194 O  O     . CYS C 3  222  ? 133.252 171.354 91.581  1.00 7.87   ? 222  CYS C O     1 
ATOM   22195 C  CB    . CYS C 3  222  ? 131.195 173.350 92.730  1.00 0.61   ? 222  CYS C CB    1 
ATOM   22196 S  SG    . CYS C 3  222  ? 132.177 174.719 93.339  1.00 14.29  ? 222  CYS C SG    1 
ATOM   22197 N  N     . PHE C 3  223  ? 133.721 173.251 90.497  1.00 6.92   ? 223  PHE C N     1 
ATOM   22198 C  CA    . PHE C 3  223  ? 135.139 172.967 90.347  1.00 5.56   ? 223  PHE C CA    1 
ATOM   22199 C  C     . PHE C 3  223  ? 135.929 173.805 91.341  1.00 8.14   ? 223  PHE C C     1 
ATOM   22200 O  O     . PHE C 3  223  ? 135.636 174.990 91.505  1.00 17.53  ? 223  PHE C O     1 
ATOM   22201 C  CB    . PHE C 3  223  ? 135.588 173.253 88.924  1.00 2.78   ? 223  PHE C CB    1 
ATOM   22202 C  CG    . PHE C 3  223  ? 134.923 172.378 87.900  1.00 7.70   ? 223  PHE C CG    1 
ATOM   22203 C  CD1   . PHE C 3  223  ? 135.369 171.093 87.671  1.00 8.49   ? 223  PHE C CD1   1 
ATOM   22204 C  CD2   . PHE C 3  223  ? 133.829 172.827 87.196  1.00 7.50   ? 223  PHE C CD2   1 
ATOM   22205 C  CE1   . PHE C 3  223  ? 134.749 170.289 86.747  1.00 6.05   ? 223  PHE C CE1   1 
ATOM   22206 C  CE2   . PHE C 3  223  ? 133.209 172.025 86.273  1.00 4.27   ? 223  PHE C CE2   1 
ATOM   22207 C  CZ    . PHE C 3  223  ? 133.667 170.759 86.048  1.00 6.37   ? 223  PHE C CZ    1 
ATOM   22208 N  N     . PRO C 3  224  ? 136.927 173.236 92.022  1.00 7.77   ? 224  PRO C N     1 
ATOM   22209 C  CA    . PRO C 3  224  ? 137.451 173.868 93.239  1.00 1.82   ? 224  PRO C CA    1 
ATOM   22210 C  C     . PRO C 3  224  ? 138.456 174.991 93.043  1.00 6.16   ? 224  PRO C C     1 
ATOM   22211 O  O     . PRO C 3  224  ? 138.582 175.827 93.943  1.00 15.15  ? 224  PRO C O     1 
ATOM   22212 C  CB    . PRO C 3  224  ? 138.091 172.690 93.973  1.00 2.53   ? 224  PRO C CB    1 
ATOM   22213 C  CG    . PRO C 3  224  ? 138.508 171.774 92.913  1.00 3.92   ? 224  PRO C CG    1 
ATOM   22214 C  CD    . PRO C 3  224  ? 137.566 171.938 91.762  1.00 4.15   ? 224  PRO C CD    1 
ATOM   22215 N  N     . ALA C 3  225  ? 139.189 175.051 91.936  1.00 7.45   ? 225  ALA C N     1 
ATOM   22216 C  CA    . ALA C 3  225  ? 140.262 176.036 91.824  1.00 1.73   ? 225  ALA C CA    1 
ATOM   22217 C  C     . ALA C 3  225  ? 140.503 176.354 90.359  1.00 8.19   ? 225  ALA C C     1 
ATOM   22218 O  O     . ALA C 3  225  ? 141.148 175.572 89.660  1.00 18.61  ? 225  ALA C O     1 
ATOM   22219 C  CB    . ALA C 3  225  ? 141.528 175.517 92.477  1.00 6.20   ? 225  ALA C CB    1 
ATOM   22220 N  N     . VAL C 3  226  ? 140.031 177.509 89.912  1.00 10.88  ? 226  VAL C N     1 
ATOM   22221 C  CA    . VAL C 3  226  ? 140.088 177.890 88.504  1.00 13.86  ? 226  VAL C CA    1 
ATOM   22222 C  C     . VAL C 3  226  ? 140.656 179.301 88.401  1.00 13.51  ? 226  VAL C C     1 
ATOM   22223 O  O     . VAL C 3  226  ? 140.305 180.163 89.215  1.00 18.72  ? 226  VAL C O     1 
ATOM   22224 C  CB    . VAL C 3  226  ? 138.696 177.770 87.863  1.00 11.47  ? 226  VAL C CB    1 
ATOM   22225 C  CG1   . VAL C 3  226  ? 138.587 178.608 86.631  1.00 14.51  ? 226  VAL C CG1   1 
ATOM   22226 C  CG2   . VAL C 3  226  ? 138.411 176.336 87.524  1.00 6.32   ? 226  VAL C CG2   1 
ATOM   22227 N  N     . PRO C 3  227  ? 141.549 179.578 87.453  1.00 11.91  ? 227  PRO C N     1 
ATOM   22228 C  CA    . PRO C 3  227  ? 142.071 180.942 87.307  1.00 17.43  ? 227  PRO C CA    1 
ATOM   22229 C  C     . PRO C 3  227  ? 140.961 181.931 86.989  1.00 16.81  ? 227  PRO C C     1 
ATOM   22230 O  O     . PRO C 3  227  ? 140.062 181.643 86.203  1.00 24.62  ? 227  PRO C O     1 
ATOM   22231 C  CB    . PRO C 3  227  ? 143.057 180.817 86.143  1.00 17.89  ? 227  PRO C CB    1 
ATOM   22232 C  CG    . PRO C 3  227  ? 143.393 179.394 86.082  1.00 13.49  ? 227  PRO C CG    1 
ATOM   22233 C  CD    . PRO C 3  227  ? 142.178 178.652 86.503  1.00 12.37  ? 227  PRO C CD    1 
ATOM   22234 N  N     . LEU C 3  228  ? 141.040 183.112 87.601  1.00 13.00  ? 228  LEU C N     1 
ATOM   22235 C  CA    . LEU C 3  228  ? 139.973 184.102 87.452  1.00 19.91  ? 228  LEU C CA    1 
ATOM   22236 C  C     . LEU C 3  228  ? 139.760 184.582 86.024  1.00 26.29  ? 228  LEU C C     1 
ATOM   22237 O  O     . LEU C 3  228  ? 138.596 184.696 85.606  1.00 29.95  ? 228  LEU C O     1 
ATOM   22238 C  CB    . LEU C 3  228  ? 140.226 185.288 88.382  1.00 21.93  ? 228  LEU C CB    1 
ATOM   22239 C  CG    . LEU C 3  228  ? 139.353 185.395 89.624  1.00 21.76  ? 228  LEU C CG    1 
ATOM   22240 C  CD1   . LEU C 3  228  ? 139.850 186.543 90.453  1.00 24.14  ? 228  LEU C CD1   1 
ATOM   22241 C  CD2   . LEU C 3  228  ? 137.899 185.599 89.242  1.00 19.78  ? 228  LEU C CD2   1 
ATOM   22242 N  N     . PRO C 3  229  ? 140.786 184.915 85.240  1.00 27.61  ? 229  PRO C N     1 
ATOM   22243 C  CA    . PRO C 3  229  ? 140.545 185.359 83.865  1.00 24.92  ? 229  PRO C CA    1 
ATOM   22244 C  C     . PRO C 3  229  ? 140.308 184.250 82.850  1.00 28.02  ? 229  PRO C C     1 
ATOM   22245 O  O     . PRO C 3  229  ? 140.184 184.556 81.662  1.00 29.65  ? 229  PRO C O     1 
ATOM   22246 C  CB    . PRO C 3  229  ? 141.830 186.125 83.537  1.00 28.97  ? 229  PRO C CB    1 
ATOM   22247 C  CG    . PRO C 3  229  ? 142.853 185.495 84.363  1.00 28.13  ? 229  PRO C CG    1 
ATOM   22248 C  CD    . PRO C 3  229  ? 142.192 185.128 85.631  1.00 24.75  ? 229  PRO C CD    1 
ATOM   22249 N  N     . HIS C 3  230  ? 140.221 182.976 83.251  1.00 28.73  ? 230  HIS C N     1 
ATOM   22250 C  CA    . HIS C 3  230  ? 140.070 181.900 82.276  1.00 26.12  ? 230  HIS C CA    1 
ATOM   22251 C  C     . HIS C 3  230  ? 139.036 180.871 82.711  1.00 25.89  ? 230  HIS C C     1 
ATOM   22252 O  O     . HIS C 3  230  ? 139.223 179.664 82.508  1.00 31.07  ? 230  HIS C O     1 
ATOM   22253 C  CB    . HIS C 3  230  ? 141.414 181.241 82.001  1.00 25.40  ? 230  HIS C CB    1 
ATOM   22254 C  CG    . HIS C 3  230  ? 142.472 182.214 81.595  1.00 31.13  ? 230  HIS C CG    1 
ATOM   22255 N  ND1   . HIS C 3  230  ? 143.416 182.700 82.472  1.00 30.53  ? 230  HIS C ND1   1 
ATOM   22256 C  CD2   . HIS C 3  230  ? 142.712 182.821 80.409  1.00 32.98  ? 230  HIS C CD2   1 
ATOM   22257 C  CE1   . HIS C 3  230  ? 144.203 183.551 81.839  1.00 31.85  ? 230  HIS C CE1   1 
ATOM   22258 N  NE2   . HIS C 3  230  ? 143.797 183.643 80.587  1.00 32.42  ? 230  HIS C NE2   1 
ATOM   22259 N  N     . ILE C 3  231  ? 137.923 181.339 83.273  1.00 23.35  ? 231  ILE C N     1 
ATOM   22260 C  CA    . ILE C 3  231  ? 136.897 180.438 83.785  1.00 21.07  ? 231  ILE C CA    1 
ATOM   22261 C  C     . ILE C 3  231  ? 136.275 179.629 82.654  1.00 18.67  ? 231  ILE C C     1 
ATOM   22262 O  O     . ILE C 3  231  ? 136.142 178.403 82.743  1.00 22.64  ? 231  ILE C O     1 
ATOM   22263 C  CB    . ILE C 3  231  ? 135.833 181.232 84.560  1.00 17.63  ? 231  ILE C CB    1 
ATOM   22264 C  CG1   . ILE C 3  231  ? 136.415 181.765 85.861  1.00 20.11  ? 231  ILE C CG1   1 
ATOM   22265 C  CG2   . ILE C 3  231  ? 134.654 180.371 84.856  1.00 20.13  ? 231  ILE C CG2   1 
ATOM   22266 C  CD1   . ILE C 3  231  ? 135.495 182.695 86.584  1.00 21.67  ? 231  ILE C CD1   1 
ATOM   22267 N  N     . ASN C 3  232  ? 135.869 180.306 81.580  1.00 14.29  ? 232  ASN C N     1 
ATOM   22268 C  CA    . ASN C 3  232  ? 135.193 179.612 80.491  1.00 16.42  ? 232  ASN C CA    1 
ATOM   22269 C  C     . ASN C 3  232  ? 136.109 178.591 79.836  1.00 18.75  ? 232  ASN C C     1 
ATOM   22270 O  O     . ASN C 3  232  ? 135.690 177.467 79.541  1.00 24.50  ? 232  ASN C O     1 
ATOM   22271 C  CB    . ASN C 3  232  ? 134.678 180.613 79.463  1.00 20.86  ? 232  ASN C CB    1 
ATOM   22272 C  CG    . ASN C 3  232  ? 133.546 181.462 79.992  1.00 21.53  ? 232  ASN C CG    1 
ATOM   22273 O  OD1   . ASN C 3  232  ? 132.872 181.093 80.945  1.00 19.70  ? 232  ASN C OD1   1 
ATOM   22274 N  ND2   . ASN C 3  232  ? 133.314 182.595 79.354  1.00 23.29  ? 232  ASN C ND2   1 
ATOM   22275 N  N     . GLN C 3  233  ? 137.368 178.957 79.616  1.00 17.88  ? 233  GLN C N     1 
ATOM   22276 C  CA    . GLN C 3  233  ? 138.317 178.016 79.043  1.00 15.06  ? 233  GLN C CA    1 
ATOM   22277 C  C     . GLN C 3  233  ? 138.515 176.793 79.926  1.00 18.48  ? 233  GLN C C     1 
ATOM   22278 O  O     . GLN C 3  233  ? 138.502 175.663 79.423  1.00 20.82  ? 233  GLN C O     1 
ATOM   22279 C  CB    . GLN C 3  233  ? 139.651 178.705 78.814  1.00 17.49  ? 233  GLN C CB    1 
ATOM   22280 C  CG    . GLN C 3  233  ? 140.547 177.977 77.858  1.00 24.16  ? 233  GLN C CG    1 
ATOM   22281 C  CD    . GLN C 3  233  ? 141.987 178.370 78.028  1.00 27.77  ? 233  GLN C CD    1 
ATOM   22282 O  OE1   . GLN C 3  233  ? 142.376 179.491 77.715  1.00 27.01  ? 233  GLN C OE1   1 
ATOM   22283 N  NE2   . GLN C 3  233  ? 142.794 177.448 78.529  1.00 26.64  ? 233  GLN C NE2   1 
ATOM   22284 N  N     . ALA C 3  234  ? 138.706 176.991 81.234  1.00 20.09  ? 234  ALA C N     1 
ATOM   22285 C  CA    . ALA C 3  234  ? 138.927 175.858 82.123  1.00 14.21  ? 234  ALA C CA    1 
ATOM   22286 C  C     . ALA C 3  234  ? 137.720 174.932 82.163  1.00 14.95  ? 234  ALA C C     1 
ATOM   22287 O  O     . ALA C 3  234  ? 137.866 173.704 82.121  1.00 20.38  ? 234  ALA C O     1 
ATOM   22288 C  CB    . ALA C 3  234  ? 139.265 176.357 83.522  1.00 15.02  ? 234  ALA C CB    1 
ATOM   22289 N  N     . VAL C 3  235  ? 136.518 175.505 82.238  1.00 16.45  ? 235  VAL C N     1 
ATOM   22290 C  CA    . VAL C 3  235  ? 135.308 174.691 82.310  1.00 19.95  ? 235  VAL C CA    1 
ATOM   22291 C  C     . VAL C 3  235  ? 135.130 173.896 81.024  1.00 18.05  ? 235  VAL C C     1 
ATOM   22292 O  O     . VAL C 3  235  ? 134.798 172.702 81.041  1.00 21.80  ? 235  VAL C O     1 
ATOM   22293 C  CB    . VAL C 3  235  ? 134.090 175.582 82.607  1.00 17.10  ? 235  VAL C CB    1 
ATOM   22294 C  CG1   . VAL C 3  235  ? 132.805 174.800 82.487  1.00 15.44  ? 235  VAL C CG1   1 
ATOM   22295 C  CG2   . VAL C 3  235  ? 134.217 176.179 83.984  1.00 14.22  ? 235  VAL C CG2   1 
ATOM   22296 N  N     . ARG C 3  236  ? 135.364 174.551 79.888  1.00 16.06  ? 236  ARG C N     1 
ATOM   22297 C  CA    . ARG C 3  236  ? 135.252 173.895 78.596  1.00 13.22  ? 236  ARG C CA    1 
ATOM   22298 C  C     . ARG C 3  236  ? 136.222 172.724 78.492  1.00 12.33  ? 236  ARG C C     1 
ATOM   22299 O  O     . ARG C 3  236  ? 135.860 171.633 78.029  1.00 18.77  ? 236  ARG C O     1 
ATOM   22300 C  CB    . ARG C 3  236  ? 135.513 174.936 77.509  1.00 14.66  ? 236  ARG C CB    1 
ATOM   22301 C  CG    . ARG C 3  236  ? 135.184 174.513 76.119  1.00 22.69  ? 236  ARG C CG    1 
ATOM   22302 C  CD    . ARG C 3  236  ? 135.107 175.712 75.205  1.00 24.30  ? 236  ARG C CD    1 
ATOM   22303 N  NE    . ARG C 3  236  ? 136.365 176.443 75.164  1.00 20.98  ? 236  ARG C NE    1 
ATOM   22304 C  CZ    . ARG C 3  236  ? 136.474 177.755 75.299  1.00 23.07  ? 236  ARG C CZ    1 
ATOM   22305 N  NH1   . ARG C 3  236  ? 135.412 178.523 75.456  1.00 20.06  ? 236  ARG C NH1   1 
ATOM   22306 N  NH2   . ARG C 3  236  ? 137.679 178.311 75.261  1.00 23.27  ? 236  ARG C NH2   1 
ATOM   22307 N  N     . THR C 3  237  ? 137.461 172.930 78.936  1.00 10.43  ? 237  THR C N     1 
ATOM   22308 C  CA    . THR C 3  237  ? 138.457 171.866 78.899  1.00 11.02  ? 237  THR C CA    1 
ATOM   22309 C  C     . THR C 3  237  ? 138.050 170.682 79.767  1.00 12.31  ? 237  THR C C     1 
ATOM   22310 O  O     . THR C 3  237  ? 138.205 169.522 79.367  1.00 19.32  ? 237  THR C O     1 
ATOM   22311 C  CB    . THR C 3  237  ? 139.809 172.413 79.345  1.00 14.79  ? 237  THR C CB    1 
ATOM   22312 O  OG1   . THR C 3  237  ? 140.160 173.532 78.528  1.00 14.69  ? 237  THR C OG1   1 
ATOM   22313 C  CG2   . THR C 3  237  ? 140.872 171.355 79.228  1.00 14.57  ? 237  THR C CG2   1 
ATOM   22314 N  N     . TYR C 3  238  ? 137.530 170.955 80.964  1.00 12.72  ? 238  TYR C N     1 
ATOM   22315 C  CA    . TYR C 3  238  ? 137.091 169.871 81.837  1.00 4.57   ? 238  TYR C CA    1 
ATOM   22316 C  C     . TYR C 3  238  ? 135.994 169.039 81.179  1.00 7.18   ? 238  TYR C C     1 
ATOM   22317 O  O     . TYR C 3  238  ? 136.044 167.801 81.178  1.00 14.30  ? 238  TYR C O     1 
ATOM   22318 C  CB    . TYR C 3  238  ? 136.597 170.441 83.167  1.00 8.58   ? 238  TYR C CB    1 
ATOM   22319 C  CG    . TYR C 3  238  ? 137.682 170.854 84.127  1.00 11.38  ? 238  TYR C CG    1 
ATOM   22320 C  CD1   . TYR C 3  238  ? 138.860 170.148 84.210  1.00 11.46  ? 238  TYR C CD1   1 
ATOM   22321 C  CD2   . TYR C 3  238  ? 137.527 171.958 84.946  1.00 12.45  ? 238  TYR C CD2   1 
ATOM   22322 C  CE1   . TYR C 3  238  ? 139.851 170.526 85.077  1.00 9.32   ? 238  TYR C CE1   1 
ATOM   22323 C  CE2   . TYR C 3  238  ? 138.516 172.337 85.818  1.00 8.54   ? 238  TYR C CE2   1 
ATOM   22324 C  CZ    . TYR C 3  238  ? 139.673 171.615 85.877  1.00 7.25   ? 238  TYR C CZ    1 
ATOM   22325 O  OH    . TYR C 3  238  ? 140.665 171.978 86.741  1.00 14.03  ? 238  TYR C OH    1 
ATOM   22326 N  N     . LEU C 3  239  ? 134.988 169.708 80.614  1.00 9.60   ? 239  LEU C N     1 
ATOM   22327 C  CA    . LEU C 3  239  ? 133.871 168.984 80.012  1.00 12.18  ? 239  LEU C CA    1 
ATOM   22328 C  C     . LEU C 3  239  ? 134.332 168.129 78.837  1.00 11.50  ? 239  LEU C C     1 
ATOM   22329 O  O     . LEU C 3  239  ? 133.929 166.962 78.693  1.00 13.24  ? 239  LEU C O     1 
ATOM   22330 C  CB    . LEU C 3  239  ? 132.788 169.969 79.579  1.00 9.97   ? 239  LEU C CB    1 
ATOM   22331 C  CG    . LEU C 3  239  ? 132.173 170.817 80.692  1.00 13.51  ? 239  LEU C CG    1 
ATOM   22332 C  CD1   . LEU C 3  239  ? 131.151 171.772 80.148  1.00 13.58  ? 239  LEU C CD1   1 
ATOM   22333 C  CD2   . LEU C 3  239  ? 131.560 169.949 81.759  1.00 10.09  ? 239  LEU C CD2   1 
ATOM   22334 N  N     . LYS C 3  240  ? 135.202 168.689 77.996  1.00 13.45  ? 240  LYS C N     1 
ATOM   22335 C  CA    . LYS C 3  240  ? 135.703 167.941 76.851  1.00 9.80   ? 240  LYS C CA    1 
ATOM   22336 C  C     . LYS C 3  240  ? 136.500 166.722 77.292  1.00 11.01  ? 240  LYS C C     1 
ATOM   22337 O  O     . LYS C 3  240  ? 136.385 165.645 76.695  1.00 18.28  ? 240  LYS C O     1 
ATOM   22338 C  CB    . LYS C 3  240  ? 136.549 168.850 75.976  1.00 15.52  ? 240  LYS C CB    1 
ATOM   22339 C  CG    . LYS C 3  240  ? 135.744 169.648 74.991  1.00 16.08  ? 240  LYS C CG    1 
ATOM   22340 C  CD    . LYS C 3  240  ? 136.331 171.020 74.825  1.00 18.76  ? 240  LYS C CD    1 
ATOM   22341 C  CE    . LYS C 3  240  ? 135.987 171.588 73.480  1.00 21.90  ? 240  LYS C CE    1 
ATOM   22342 N  NZ    . LYS C 3  240  ? 136.444 170.700 72.383  1.00 23.38  ? 240  LYS C NZ    1 
ATOM   22343 N  N     . ASN C 3  241  ? 137.321 166.869 78.335  1.00 9.61   ? 241  ASN C N     1 
ATOM   22344 C  CA    . ASN C 3  241  ? 138.103 165.728 78.798  1.00 11.36  ? 241  ASN C CA    1 
ATOM   22345 C  C     . ASN C 3  241  ? 137.210 164.626 79.348  1.00 11.95  ? 241  ASN C C     1 
ATOM   22346 O  O     . ASN C 3  241  ? 137.509 163.440 79.178  1.00 19.45  ? 241  ASN C O     1 
ATOM   22347 C  CB    . ASN C 3  241  ? 139.119 166.154 79.848  1.00 11.02  ? 241  ASN C CB    1 
ATOM   22348 C  CG    . ASN C 3  241  ? 140.153 167.086 79.304  1.00 13.24  ? 241  ASN C CG    1 
ATOM   22349 O  OD1   . ASN C 3  241  ? 140.313 167.213 78.099  1.00 21.24  ? 241  ASN C OD1   1 
ATOM   22350 N  ND2   . ASN C 3  241  ? 140.906 167.706 80.189  1.00 16.56  ? 241  ASN C ND2   1 
ATOM   22351 N  N     . ALA C 3  242  ? 136.123 164.988 80.031  1.00 9.80   ? 242  ALA C N     1 
ATOM   22352 C  CA    . ALA C 3  242  ? 135.202 163.955 80.504  1.00 13.60  ? 242  ALA C CA    1 
ATOM   22353 C  C     . ALA C 3  242  ? 134.614 163.160 79.340  1.00 13.52  ? 242  ALA C C     1 
ATOM   22354 O  O     . ALA C 3  242  ? 134.590 161.914 79.353  1.00 12.07  ? 242  ALA C O     1 
ATOM   22355 C  CB    . ALA C 3  242  ? 134.090 164.587 81.337  1.00 11.84  ? 242  ALA C CB    1 
ATOM   22356 N  N     . CYS C 3  243  ? 134.150 163.871 78.310  1.00 12.65  ? 243  CYS C N     1 
ATOM   22357 C  CA    . CYS C 3  243  ? 133.596 163.188 77.144  1.00 10.00  ? 243  CYS C CA    1 
ATOM   22358 C  C     . CYS C 3  243  ? 134.630 162.263 76.503  1.00 17.86  ? 243  CYS C C     1 
ATOM   22359 O  O     . CYS C 3  243  ? 134.329 161.116 76.143  1.00 24.65  ? 243  CYS C O     1 
ATOM   22360 C  CB    . CYS C 3  243  ? 133.083 164.214 76.139  1.00 16.54  ? 243  CYS C CB    1 
ATOM   22361 S  SG    . CYS C 3  243  ? 131.699 165.204 76.719  1.00 25.82  ? 243  CYS C SG    1 
ATOM   22362 N  N     . ARG C 3  244  ? 135.871 162.739 76.387  1.00 13.13  ? 244  ARG C N     1 
ATOM   22363 C  CA    . ARG C 3  244  ? 136.917 161.936 75.762  1.00 10.08  ? 244  ARG C CA    1 
ATOM   22364 C  C     . ARG C 3  244  ? 137.254 160.695 76.583  1.00 11.86  ? 244  ARG C C     1 
ATOM   22365 O  O     . ARG C 3  244  ? 137.537 159.632 76.020  1.00 19.86  ? 244  ARG C O     1 
ATOM   22366 C  CB    . ARG C 3  244  ? 138.165 162.782 75.550  1.00 15.75  ? 244  ARG C CB    1 
ATOM   22367 C  CG    . ARG C 3  244  ? 138.133 163.622 74.304  1.00 16.33  ? 244  ARG C CG    1 
ATOM   22368 C  CD    . ARG C 3  244  ? 139.375 164.473 74.219  1.00 22.09  ? 244  ARG C CD    1 
ATOM   22369 N  NE    . ARG C 3  244  ? 139.101 165.800 73.683  1.00 25.73  ? 244  ARG C NE    1 
ATOM   22370 C  CZ    . ARG C 3  244  ? 139.344 166.929 74.333  1.00 26.31  ? 244  ARG C CZ    1 
ATOM   22371 N  NH1   . ARG C 3  244  ? 139.877 166.929 75.542  1.00 20.24  ? 244  ARG C NH1   1 
ATOM   22372 N  NH2   . ARG C 3  244  ? 139.058 168.088 73.749  1.00 24.59  ? 244  ARG C NH2   1 
ATOM   22373 N  N     . ILE C 3  245  ? 137.258 160.813 77.911  1.00 11.33  ? 245  ILE C N     1 
ATOM   22374 C  CA    . ILE C 3  245  ? 137.535 159.658 78.765  1.00 10.11  ? 245  ILE C CA    1 
ATOM   22375 C  C     . ILE C 3  245  ? 136.499 158.568 78.529  1.00 11.25  ? 245  ILE C C     1 
ATOM   22376 O  O     . ILE C 3  245  ? 136.830 157.379 78.381  1.00 17.02  ? 245  ILE C O     1 
ATOM   22377 C  CB    . ILE C 3  245  ? 137.562 160.086 80.244  1.00 9.03   ? 245  ILE C CB    1 
ATOM   22378 C  CG1   . ILE C 3  245  ? 138.851 160.821 80.575  1.00 7.63   ? 245  ILE C CG1   1 
ATOM   22379 C  CG2   . ILE C 3  245  ? 137.422 158.887 81.149  1.00 13.83  ? 245  ILE C CG2   1 
ATOM   22380 C  CD1   . ILE C 3  245  ? 140.062 159.992 80.410  1.00 13.49  ? 245  ILE C CD1   1 
ATOM   22381 N  N     . ILE C 3  246  ? 135.224 158.961 78.485  1.00 7.33   ? 246  ILE C N     1 
ATOM   22382 C  CA    . ILE C 3  246  ? 134.168 157.972 78.275  1.00 11.17  ? 246  ILE C CA    1 
ATOM   22383 C  C     . ILE C 3  246  ? 134.319 157.307 76.910  1.00 15.11  ? 246  ILE C C     1 
ATOM   22384 O  O     . ILE C 3  246  ? 134.171 156.083 76.775  1.00 15.38  ? 246  ILE C O     1 
ATOM   22385 C  CB    . ILE C 3  246  ? 132.784 158.618 78.451  1.00 13.60  ? 246  ILE C CB    1 
ATOM   22386 C  CG1   . ILE C 3  246  ? 132.490 158.804 79.936  1.00 12.60  ? 246  ILE C CG1   1 
ATOM   22387 C  CG2   . ILE C 3  246  ? 131.712 157.762 77.817  1.00 11.40  ? 246  ILE C CG2   1 
ATOM   22388 C  CD1   . ILE C 3  246  ? 131.310 159.651 80.219  1.00 13.21  ? 246  ILE C CD1   1 
ATOM   22389 N  N     . ILE C 3  247  ? 134.623 158.101 75.878  1.00 17.97  ? 247  ILE C N     1 
ATOM   22390 C  CA    . ILE C 3  247  ? 134.795 157.531 74.541  1.00 16.60  ? 247  ILE C CA    1 
ATOM   22391 C  C     . ILE C 3  247  ? 135.939 156.523 74.531  1.00 15.43  ? 247  ILE C C     1 
ATOM   22392 O  O     . ILE C 3  247  ? 135.839 155.450 73.924  1.00 17.57  ? 247  ILE C O     1 
ATOM   22393 C  CB    . ILE C 3  247  ? 135.011 158.642 73.501  1.00 15.46  ? 247  ILE C CB    1 
ATOM   22394 C  CG1   . ILE C 3  247  ? 133.752 159.483 73.350  1.00 15.27  ? 247  ILE C CG1   1 
ATOM   22395 C  CG2   . ILE C 3  247  ? 135.356 158.046 72.157  1.00 10.01  ? 247  ILE C CG2   1 
ATOM   22396 C  CD1   . ILE C 3  247  ? 133.938 160.665 72.456  1.00 18.30  ? 247  ILE C CD1   1 
ATOM   22397 N  N     . GLY C 3  248  ? 137.037 156.845 75.213  1.00 9.07   ? 248  GLY C N     1 
ATOM   22398 C  CA    . GLY C 3  248  ? 138.171 155.934 75.243  1.00 5.81   ? 248  GLY C CA    1 
ATOM   22399 C  C     . GLY C 3  248  ? 137.846 154.599 75.879  1.00 11.45  ? 248  GLY C C     1 
ATOM   22400 O  O     . GLY C 3  248  ? 138.231 153.541 75.372  1.00 18.40  ? 248  GLY C O     1 
ATOM   22401 N  N     . ARG C 3  249  ? 137.131 154.626 77.004  1.00 12.76  ? 249  ARG C N     1 
ATOM   22402 C  CA    . ARG C 3  249  ? 136.799 153.367 77.674  1.00 7.57   ? 249  ARG C CA    1 
ATOM   22403 C  C     . ARG C 3  249  ? 135.818 152.529 76.853  1.00 7.81   ? 249  ARG C C     1 
ATOM   22404 O  O     . ARG C 3  249  ? 135.953 151.295 76.755  1.00 17.19  ? 249  ARG C O     1 
ATOM   22405 C  CB    . ARG C 3  249  ? 136.264 153.662 79.072  1.00 9.98   ? 249  ARG C CB    1 
ATOM   22406 C  CG    . ARG C 3  249  ? 137.367 153.999 80.061  1.00 15.57  ? 249  ARG C CG    1 
ATOM   22407 C  CD    . ARG C 3  249  ? 136.868 154.803 81.228  1.00 14.55  ? 249  ARG C CD    1 
ATOM   22408 N  NE    . ARG C 3  249  ? 136.181 153.975 82.206  1.00 14.59  ? 249  ARG C NE    1 
ATOM   22409 C  CZ    . ARG C 3  249  ? 135.512 154.441 83.250  1.00 11.49  ? 249  ARG C CZ    1 
ATOM   22410 N  NH1   . ARG C 3  249  ? 135.421 155.735 83.488  1.00 9.86   ? 249  ARG C NH1   1 
ATOM   22411 N  NH2   . ARG C 3  249  ? 134.918 153.586 84.070  1.00 10.29  ? 249  ARG C NH2   1 
ATOM   22412 N  N     . ILE C 3  250  ? 134.843 153.182 76.219  1.00 13.76  ? 250  ILE C N     1 
ATOM   22413 C  CA    . ILE C 3  250  ? 133.914 152.449 75.362  1.00 11.09  ? 250  ILE C CA    1 
ATOM   22414 C  C     . ILE C 3  250  ? 134.646 151.823 74.181  1.00 13.39  ? 250  ILE C C     1 
ATOM   22415 O  O     . ILE C 3  250  ? 134.335 150.703 73.762  1.00 14.02  ? 250  ILE C O     1 
ATOM   22416 C  CB    . ILE C 3  250  ? 132.765 153.368 74.914  1.00 12.66  ? 250  ILE C CB    1 
ATOM   22417 C  CG1   . ILE C 3  250  ? 131.816 153.604 76.082  1.00 12.49  ? 250  ILE C CG1   1 
ATOM   22418 C  CG2   . ILE C 3  250  ? 132.002 152.771 73.769  1.00 15.80  ? 250  ILE C CG2   1 
ATOM   22419 C  CD1   . ILE C 3  250  ? 131.248 152.333 76.657  1.00 14.12  ? 250  ILE C CD1   1 
ATOM   22420 N  N     . GLN C 3  251  ? 135.639 152.523 73.634  1.00 19.17  ? 251  GLN C N     1 
ATOM   22421 C  CA    . GLN C 3  251  ? 136.410 151.962 72.530  1.00 16.74  ? 251  GLN C CA    1 
ATOM   22422 C  C     . GLN C 3  251  ? 137.282 150.794 72.972  1.00 17.56  ? 251  GLN C C     1 
ATOM   22423 O  O     . GLN C 3  251  ? 137.511 149.861 72.192  1.00 23.58  ? 251  GLN C O     1 
ATOM   22424 C  CB    . GLN C 3  251  ? 137.251 153.053 71.889  1.00 12.27  ? 251  GLN C CB    1 
ATOM   22425 C  CG    . GLN C 3  251  ? 136.431 153.959 71.024  1.00 15.58  ? 251  GLN C CG    1 
ATOM   22426 C  CD    . GLN C 3  251  ? 137.242 155.057 70.399  1.00 23.16  ? 251  GLN C CD    1 
ATOM   22427 O  OE1   . GLN C 3  251  ? 138.356 155.341 70.829  1.00 24.24  ? 251  GLN C OE1   1 
ATOM   22428 N  NE2   . GLN C 3  251  ? 136.687 155.686 69.374  1.00 23.00  ? 251  GLN C NE2   1 
ATOM   22429 N  N     . SER C 3  252  ? 137.780 150.823 74.207  1.00 15.52  ? 252  SER C N     1 
ATOM   22430 C  CA    . SER C 3  252  ? 138.473 149.649 74.730  1.00 16.03  ? 252  SER C CA    1 
ATOM   22431 C  C     . SER C 3  252  ? 137.560 148.431 74.725  1.00 20.31  ? 252  SER C C     1 
ATOM   22432 O  O     . SER C 3  252  ? 137.990 147.322 74.399  1.00 22.32  ? 252  SER C O     1 
ATOM   22433 C  CB    . SER C 3  252  ? 138.995 149.910 76.139  1.00 18.60  ? 252  SER C CB    1 
ATOM   22434 O  OG    . SER C 3  252  ? 140.201 150.644 76.117  1.00 26.85  ? 252  SER C OG    1 
ATOM   22435 N  N     . ILE C 3  253  ? 136.297 148.611 75.111  1.00 25.35  ? 253  ILE C N     1 
ATOM   22436 C  CA    . ILE C 3  253  ? 135.377 147.467 75.048  1.00 20.41  ? 253  ILE C CA    1 
ATOM   22437 C  C     . ILE C 3  253  ? 135.070 147.074 73.603  1.00 19.31  ? 253  ILE C C     1 
ATOM   22438 O  O     . ILE C 3  253  ? 134.931 145.880 73.277  1.00 21.61  ? 253  ILE C O     1 
ATOM   22439 C  CB    . ILE C 3  253  ? 134.104 147.771 75.859  1.00 21.10  ? 253  ILE C CB    1 
ATOM   22440 C  CG1   . ILE C 3  253  ? 134.342 147.388 77.309  1.00 22.15  ? 253  ILE C CG1   1 
ATOM   22441 C  CG2   . ILE C 3  253  ? 132.920 146.991 75.342  1.00 21.27  ? 253  ILE C CG2   1 
ATOM   22442 C  CD1   . ILE C 3  253  ? 133.930 148.427 78.269  1.00 21.19  ? 253  ILE C CD1   1 
ATOM   22443 N  N     . GLN C 3  254  ? 134.965 148.062 72.717  1.00 26.33  ? 254  GLN C N     1 
ATOM   22444 C  CA    . GLN C 3  254  ? 134.710 147.795 71.307  1.00 25.83  ? 254  GLN C CA    1 
ATOM   22445 C  C     . GLN C 3  254  ? 135.784 146.909 70.705  1.00 23.56  ? 254  GLN C C     1 
ATOM   22446 O  O     . GLN C 3  254  ? 135.471 145.963 69.981  1.00 26.15  ? 254  GLN C O     1 
ATOM   22447 C  CB    . GLN C 3  254  ? 134.637 149.110 70.543  1.00 24.09  ? 254  GLN C CB    1 
ATOM   22448 C  CG    . GLN C 3  254  ? 133.910 149.059 69.231  1.00 25.24  ? 254  GLN C CG    1 
ATOM   22449 C  CD    . GLN C 3  254  ? 134.185 150.284 68.395  1.00 26.35  ? 254  GLN C CD    1 
ATOM   22450 O  OE1   . GLN C 3  254  ? 135.089 151.056 68.693  1.00 30.07  ? 254  GLN C OE1   1 
ATOM   22451 N  NE2   . GLN C 3  254  ? 133.392 150.484 67.358  1.00 25.66  ? 254  GLN C NE2   1 
ATOM   22452 N  N     . LYS C 3  255  ? 137.046 147.182 71.007  1.00 33.58  ? 255  LYS C N     1 
ATOM   22453 C  CA    . LYS C 3  255  ? 138.146 146.394 70.470  1.00 33.17  ? 255  LYS C CA    1 
ATOM   22454 C  C     . LYS C 3  255  ? 138.123 144.947 70.940  1.00 31.80  ? 255  LYS C C     1 
ATOM   22455 O  O     . LYS C 3  255  ? 138.737 144.093 70.299  1.00 39.96  ? 255  LYS C O     1 
ATOM   22456 C  CB    . LYS C 3  255  ? 139.482 147.045 70.823  1.00 30.53  ? 255  LYS C CB    1 
ATOM   22457 C  CG    . LYS C 3  255  ? 139.912 148.082 69.799  1.00 33.95  ? 255  LYS C CG    1 
ATOM   22458 C  CD    . LYS C 3  255  ? 141.063 148.929 70.297  1.00 36.56  ? 255  LYS C CD    1 
ATOM   22459 C  CE    . LYS C 3  255  ? 140.739 150.416 70.215  1.00 35.96  ? 255  LYS C CE    1 
ATOM   22460 N  NZ    . LYS C 3  255  ? 141.512 151.200 71.216  1.00 34.26  ? 255  LYS C NZ    1 
ATOM   22461 N  N     . ILE C 3  256  ? 137.430 144.649 72.031  1.00 30.34  ? 256  ILE C N     1 
ATOM   22462 C  CA    . ILE C 3  256  ? 137.213 143.278 72.473  1.00 28.28  ? 256  ILE C CA    1 
ATOM   22463 C  C     . ILE C 3  256  ? 136.081 142.628 71.699  1.00 30.77  ? 256  ILE C C     1 
ATOM   22464 O  O     . ILE C 3  256  ? 136.180 141.472 71.289  1.00 31.97  ? 256  ILE C O     1 
ATOM   22465 C  CB    . ILE C 3  256  ? 136.938 143.247 73.993  1.00 28.20  ? 256  ILE C CB    1 
ATOM   22466 C  CG1   . ILE C 3  256  ? 138.244 143.264 74.774  1.00 32.44  ? 256  ILE C CG1   1 
ATOM   22467 C  CG2   . ILE C 3  256  ? 136.109 142.041 74.374  1.00 29.02  ? 256  ILE C CG2   1 
ATOM   22468 C  CD1   . ILE C 3  256  ? 139.189 142.165 74.408  1.00 34.59  ? 256  ILE C CD1   1 
ATOM   22469 N  N     . TYR C 3  257  ? 135.000 143.381 71.474  1.00 38.11  ? 257  TYR C N     1 
ATOM   22470 C  CA    . TYR C 3  257  ? 133.826 142.806 70.813  1.00 34.68  ? 257  TYR C CA    1 
ATOM   22471 C  C     . TYR C 3  257  ? 134.154 142.243 69.432  1.00 33.68  ? 257  TYR C C     1 
ATOM   22472 O  O     . TYR C 3  257  ? 133.636 141.189 69.050  1.00 32.48  ? 257  TYR C O     1 
ATOM   22473 C  CB    . TYR C 3  257  ? 132.715 143.845 70.695  1.00 31.12  ? 257  TYR C CB    1 
ATOM   22474 C  CG    . TYR C 3  257  ? 131.738 143.843 71.838  1.00 34.36  ? 257  TYR C CG    1 
ATOM   22475 C  CD1   . TYR C 3  257  ? 131.753 142.835 72.787  1.00 35.85  ? 257  TYR C CD1   1 
ATOM   22476 C  CD2   . TYR C 3  257  ? 130.781 144.835 71.955  1.00 35.08  ? 257  TYR C CD2   1 
ATOM   22477 C  CE1   . TYR C 3  257  ? 130.854 142.828 73.832  1.00 37.07  ? 257  TYR C CE1   1 
ATOM   22478 C  CE2   . TYR C 3  257  ? 129.879 144.836 72.990  1.00 35.55  ? 257  TYR C CE2   1 
ATOM   22479 C  CZ    . TYR C 3  257  ? 129.925 143.835 73.929  1.00 39.96  ? 257  TYR C CZ    1 
ATOM   22480 O  OH    . TYR C 3  257  ? 129.026 143.838 74.962  1.00 38.57  ? 257  TYR C OH    1 
ATOM   22481 N  N     . GLU C 3  258  ? 134.998 142.930 68.663  1.00 45.66  ? 258  GLU C N     1 
ATOM   22482 C  CA    . GLU C 3  258  ? 135.204 142.573 67.264  1.00 48.31  ? 258  GLU C CA    1 
ATOM   22483 C  C     . GLU C 3  258  ? 135.965 141.271 67.063  1.00 50.14  ? 258  GLU C C     1 
ATOM   22484 O  O     . GLU C 3  258  ? 135.896 140.703 65.968  1.00 49.81  ? 258  GLU C O     1 
ATOM   22485 C  CB    . GLU C 3  258  ? 135.942 143.692 66.537  1.00 46.65  ? 258  GLU C CB    1 
ATOM   22486 C  CG    . GLU C 3  258  ? 135.643 145.070 67.054  1.00 46.53  ? 258  GLU C CG    1 
ATOM   22487 C  CD    . GLU C 3  258  ? 135.787 146.117 65.980  1.00 50.02  ? 258  GLU C CD    1 
ATOM   22488 O  OE1   . GLU C 3  258  ? 135.263 145.889 64.873  1.00 49.64  ? 258  GLU C OE1   1 
ATOM   22489 O  OE2   . GLU C 3  258  ? 136.422 147.162 66.235  1.00 50.11  ? 258  GLU C OE2   1 
ATOM   22490 N  N     . ASN C 3  259  ? 136.668 140.779 68.073  1.00 46.93  ? 259  ASN C N     1 
ATOM   22491 C  CA    . ASN C 3  259  ? 137.500 139.588 67.955  1.00 45.19  ? 259  ASN C CA    1 
ATOM   22492 C  C     . ASN C 3  259  ? 136.794 138.360 68.521  1.00 48.54  ? 259  ASN C C     1 
ATOM   22493 O  O     . ASN C 3  259  ? 137.408 137.516 69.176  1.00 50.76  ? 259  ASN C O     1 
ATOM   22494 C  CB    . ASN C 3  259  ? 138.839 139.799 68.654  1.00 44.82  ? 259  ASN C CB    1 
ATOM   22495 C  CG    . ASN C 3  259  ? 139.693 140.833 67.966  1.00 48.98  ? 259  ASN C CG    1 
ATOM   22496 O  OD1   . ASN C 3  259  ? 140.063 141.844 68.560  1.00 49.32  ? 259  ASN C OD1   1 
ATOM   22497 N  ND2   . ASN C 3  259  ? 140.036 140.575 66.714  1.00 49.95  ? 259  ASN C ND2   1 
ATOM   22498 N  N     . PHE C 3  260  ? 135.489 138.251 68.278  1.00 40.87  ? 260  PHE C N     1 
ATOM   22499 C  CA    . PHE C 3  260  ? 134.706 137.164 68.845  1.00 39.74  ? 260  PHE C CA    1 
ATOM   22500 C  C     . PHE C 3  260  ? 135.005 135.819 68.203  1.00 44.57  ? 260  PHE C C     1 
ATOM   22501 O  O     . PHE C 3  260  ? 134.489 134.800 68.673  1.00 44.12  ? 260  PHE C O     1 
ATOM   22502 C  CB    . PHE C 3  260  ? 133.213 137.479 68.750  1.00 38.92  ? 260  PHE C CB    1 
ATOM   22503 C  CG    . PHE C 3  260  ? 132.639 137.348 67.374  1.00 41.56  ? 260  PHE C CG    1 
ATOM   22504 C  CD1   . PHE C 3  260  ? 132.886 138.306 66.410  1.00 42.89  ? 260  PHE C CD1   1 
ATOM   22505 C  CD2   . PHE C 3  260  ? 131.812 136.289 67.059  1.00 41.70  ? 260  PHE C CD2   1 
ATOM   22506 C  CE1   . PHE C 3  260  ? 132.345 138.193 65.153  1.00 44.27  ? 260  PHE C CE1   1 
ATOM   22507 C  CE2   . PHE C 3  260  ? 131.266 136.173 65.804  1.00 41.50  ? 260  PHE C CE2   1 
ATOM   22508 C  CZ    . PHE C 3  260  ? 131.533 137.125 64.849  1.00 43.59  ? 260  PHE C CZ    1 
ATOM   22509 N  N     . GLU C 3  261  ? 135.812 135.794 67.143  1.00 48.10  ? 261  GLU C N     1 
ATOM   22510 C  CA    . GLU C 3  261  ? 136.265 134.534 66.570  1.00 44.25  ? 261  GLU C CA    1 
ATOM   22511 C  C     . GLU C 3  261  ? 137.454 133.967 67.336  1.00 45.66  ? 261  GLU C C     1 
ATOM   22512 O  O     . GLU C 3  261  ? 137.476 132.776 67.663  1.00 48.14  ? 261  GLU C O     1 
ATOM   22513 C  CB    . GLU C 3  261  ? 136.622 134.743 65.103  1.00 43.65  ? 261  GLU C CB    1 
ATOM   22514 C  CG    . GLU C 3  261  ? 135.513 135.405 64.315  1.00 45.92  ? 261  GLU C CG    1 
ATOM   22515 C  CD    . GLU C 3  261  ? 135.751 136.885 64.112  1.00 46.88  ? 261  GLU C CD    1 
ATOM   22516 O  OE1   . GLU C 3  261  ? 135.031 137.499 63.298  1.00 44.90  ? 261  GLU C OE1   1 
ATOM   22517 O  OE2   . GLU C 3  261  ? 136.654 137.437 64.772  1.00 49.78  ? 261  GLU C OE2   1 
ATOM   22518 N  N     . GLU C 3  262  ? 138.446 134.798 67.630  1.00 45.21  ? 262  GLU C N     1 
ATOM   22519 C  CA    . GLU C 3  262  ? 139.587 134.344 68.408  1.00 45.18  ? 262  GLU C CA    1 
ATOM   22520 C  C     . GLU C 3  262  ? 139.180 134.175 69.868  1.00 45.84  ? 262  GLU C C     1 
ATOM   22521 O  O     . GLU C 3  262  ? 138.439 135.005 70.404  1.00 46.57  ? 262  GLU C O     1 
ATOM   22522 C  CB    . GLU C 3  262  ? 140.735 135.342 68.305  1.00 45.62  ? 262  GLU C CB    1 
ATOM   22523 C  CG    . GLU C 3  262  ? 141.283 135.528 66.905  1.00 46.30  ? 262  GLU C CG    1 
ATOM   22524 C  CD    . GLU C 3  262  ? 140.507 136.559 66.112  1.00 49.57  ? 262  GLU C CD    1 
ATOM   22525 O  OE1   . GLU C 3  262  ? 139.482 137.060 66.620  1.00 46.29  ? 262  GLU C OE1   1 
ATOM   22526 O  OE2   . GLU C 3  262  ? 140.923 136.871 64.978  1.00 50.22  ? 262  GLU C OE2   1 
ATOM   22527 N  N     . PRO C 3  263  ? 139.653 133.128 70.542  1.00 41.10  ? 263  PRO C N     1 
ATOM   22528 C  CA    . PRO C 3  263  ? 139.255 132.917 71.939  1.00 39.93  ? 263  PRO C CA    1 
ATOM   22529 C  C     . PRO C 3  263  ? 139.872 133.957 72.857  1.00 40.87  ? 263  PRO C C     1 
ATOM   22530 O  O     . PRO C 3  263  ? 141.073 134.228 72.778  1.00 41.66  ? 263  PRO C O     1 
ATOM   22531 C  CB    . PRO C 3  263  ? 139.763 131.502 72.240  1.00 40.35  ? 263  PRO C CB    1 
ATOM   22532 C  CG    . PRO C 3  263  ? 140.902 131.304 71.311  1.00 40.58  ? 263  PRO C CG    1 
ATOM   22533 C  CD    . PRO C 3  263  ? 140.591 132.097 70.066  1.00 39.22  ? 263  PRO C CD    1 
ATOM   22534 N  N     . GLN C 3  264  ? 139.053 134.556 73.720  1.00 37.19  ? 264  GLN C N     1 
ATOM   22535 C  CA    . GLN C 3  264  ? 139.474 135.684 74.531  1.00 36.66  ? 264  GLN C CA    1 
ATOM   22536 C  C     . GLN C 3  264  ? 139.088 135.482 75.990  1.00 34.84  ? 264  GLN C C     1 
ATOM   22537 O  O     . GLN C 3  264  ? 138.020 134.936 76.279  1.00 32.97  ? 264  GLN C O     1 
ATOM   22538 C  CB    . GLN C 3  264  ? 138.839 136.974 74.007  1.00 29.78  ? 264  GLN C CB    1 
ATOM   22539 C  CG    . GLN C 3  264  ? 139.805 138.112 73.851  1.00 31.11  ? 264  GLN C CG    1 
ATOM   22540 C  CD    . GLN C 3  264  ? 139.375 139.070 72.770  1.00 38.93  ? 264  GLN C CD    1 
ATOM   22541 O  OE1   . GLN C 3  264  ? 138.215 139.085 72.366  1.00 36.09  ? 264  GLN C OE1   1 
ATOM   22542 N  NE2   . GLN C 3  264  ? 140.314 139.869 72.280  1.00 36.59  ? 264  GLN C NE2   1 
ATOM   22543 N  N     . PRO C 3  265  ? 139.931 135.903 76.930  1.00 36.15  ? 265  PRO C N     1 
ATOM   22544 C  CA    . PRO C 3  265  ? 139.569 135.762 78.346  1.00 35.62  ? 265  PRO C CA    1 
ATOM   22545 C  C     . PRO C 3  265  ? 138.547 136.783 78.821  1.00 37.02  ? 265  PRO C C     1 
ATOM   22546 O  O     . PRO C 3  265  ? 138.111 136.702 79.974  1.00 39.99  ? 265  PRO C O     1 
ATOM   22547 C  CB    . PRO C 3  265  ? 140.912 135.929 79.067  1.00 35.09  ? 265  PRO C CB    1 
ATOM   22548 C  CG    . PRO C 3  265  ? 141.725 136.757 78.146  1.00 36.16  ? 265  PRO C CG    1 
ATOM   22549 C  CD    . PRO C 3  265  ? 141.307 136.395 76.754  1.00 35.12  ? 265  PRO C CD    1 
ATOM   22550 N  N     . GLU C 3  266  ? 138.159 137.738 77.980  1.00 32.46  ? 266  GLU C N     1 
ATOM   22551 C  CA    . GLU C 3  266  ? 137.228 138.794 78.347  1.00 26.57  ? 266  GLU C CA    1 
ATOM   22552 C  C     . GLU C 3  266  ? 135.855 138.633 77.719  1.00 27.52  ? 266  GLU C C     1 
ATOM   22553 O  O     . GLU C 3  266  ? 134.933 139.346 78.106  1.00 33.15  ? 266  GLU C O     1 
ATOM   22554 C  CB    . GLU C 3  266  ? 137.801 140.153 77.952  1.00 27.83  ? 266  GLU C CB    1 
ATOM   22555 C  CG    . GLU C 3  266  ? 138.823 140.682 78.916  1.00 34.13  ? 266  GLU C CG    1 
ATOM   22556 C  CD    . GLU C 3  266  ? 140.222 140.668 78.343  1.00 39.94  ? 266  GLU C CD    1 
ATOM   22557 O  OE1   . GLU C 3  266  ? 141.190 140.661 79.131  1.00 38.41  ? 266  GLU C OE1   1 
ATOM   22558 O  OE2   . GLU C 3  266  ? 140.353 140.667 77.102  1.00 38.67  ? 266  GLU C OE2   1 
ATOM   22559 N  N     . LEU C 3  267  ? 135.694 137.730 76.758  1.00 24.72  ? 267  LEU C N     1 
ATOM   22560 C  CA    . LEU C 3  267  ? 134.414 137.528 76.091  1.00 20.07  ? 267  LEU C CA    1 
ATOM   22561 C  C     . LEU C 3  267  ? 134.142 136.040 76.020  1.00 18.05  ? 267  LEU C C     1 
ATOM   22562 O  O     . LEU C 3  267  ? 135.012 135.273 75.609  1.00 28.47  ? 267  LEU C O     1 
ATOM   22563 C  CB    . LEU C 3  267  ? 134.415 138.137 74.689  1.00 21.54  ? 267  LEU C CB    1 
ATOM   22564 C  CG    . LEU C 3  267  ? 133.158 137.921 73.854  1.00 17.45  ? 267  LEU C CG    1 
ATOM   22565 C  CD1   . LEU C 3  267  ? 131.953 138.471 74.565  1.00 21.32  ? 267  LEU C CD1   1 
ATOM   22566 C  CD2   . LEU C 3  267  ? 133.309 138.574 72.510  1.00 24.24  ? 267  LEU C CD2   1 
ATOM   22567 N  N     . VAL C 3  268  ? 132.947 135.633 76.428  1.00 17.48  ? 268  VAL C N     1 
ATOM   22568 C  CA    . VAL C 3  268  ? 132.514 134.245 76.363  1.00 18.87  ? 268  VAL C CA    1 
ATOM   22569 C  C     . VAL C 3  268  ? 131.164 134.202 75.664  1.00 22.24  ? 268  VAL C C     1 
ATOM   22570 O  O     . VAL C 3  268  ? 130.243 134.927 76.049  1.00 25.29  ? 268  VAL C O     1 
ATOM   22571 C  CB    . VAL C 3  268  ? 132.429 133.613 77.763  1.00 14.20  ? 268  VAL C CB    1 
ATOM   22572 C  CG1   . VAL C 3  268  ? 132.130 132.146 77.652  1.00 17.99  ? 268  VAL C CG1   1 
ATOM   22573 C  CG2   . VAL C 3  268  ? 133.715 133.818 78.506  1.00 14.69  ? 268  VAL C CG2   1 
ATOM   22574 N  N     . LEU C 3  269  ? 131.050 133.361 74.640  1.00 21.15  ? 269  LEU C N     1 
ATOM   22575 C  CA    . LEU C 3  269  ? 129.813 133.183 73.892  1.00 17.02  ? 269  LEU C CA    1 
ATOM   22576 C  C     . LEU C 3  269  ? 129.353 131.738 74.008  1.00 24.44  ? 269  LEU C C     1 
ATOM   22577 O  O     . LEU C 3  269  ? 130.118 130.816 73.719  1.00 29.43  ? 269  LEU C O     1 
ATOM   22578 C  CB    . LEU C 3  269  ? 130.003 133.547 72.424  1.00 20.78  ? 269  LEU C CB    1 
ATOM   22579 C  CG    . LEU C 3  269  ? 130.134 135.013 72.034  1.00 24.35  ? 269  LEU C CG    1 
ATOM   22580 C  CD1   . LEU C 3  269  ? 130.728 135.103 70.656  1.00 22.96  ? 269  LEU C CD1   1 
ATOM   22581 C  CD2   . LEU C 3  269  ? 128.790 135.693 72.062  1.00 25.27  ? 269  LEU C CD2   1 
ATOM   22582 N  N     . PHE C 3  270  ? 128.106 131.544 74.424  1.00 26.09  ? 270  PHE C N     1 
ATOM   22583 C  CA    . PHE C 3  270  ? 127.482 130.232 74.473  1.00 24.20  ? 270  PHE C CA    1 
ATOM   22584 C  C     . PHE C 3  270  ? 126.341 130.173 73.474  1.00 27.53  ? 270  PHE C C     1 
ATOM   22585 O  O     . PHE C 3  270  ? 125.764 131.196 73.105  1.00 29.35  ? 270  PHE C O     1 
ATOM   22586 C  CB    . PHE C 3  270  ? 126.892 129.897 75.842  1.00 20.98  ? 270  PHE C CB    1 
ATOM   22587 C  CG    . PHE C 3  270  ? 127.865 129.934 76.968  1.00 24.03  ? 270  PHE C CG    1 
ATOM   22588 C  CD1   . PHE C 3  270  ? 128.053 131.087 77.696  1.00 28.79  ? 270  PHE C CD1   1 
ATOM   22589 C  CD2   . PHE C 3  270  ? 128.562 128.801 77.331  1.00 30.01  ? 270  PHE C CD2   1 
ATOM   22590 C  CE1   . PHE C 3  270  ? 128.930 131.117 78.753  1.00 30.72  ? 270  PHE C CE1   1 
ATOM   22591 C  CE2   . PHE C 3  270  ? 129.449 128.827 78.392  1.00 29.44  ? 270  PHE C CE2   1 
ATOM   22592 C  CZ    . PHE C 3  270  ? 129.630 129.987 79.102  1.00 28.28  ? 270  PHE C CZ    1 
ATOM   22593 N  N     . SER C 3  271  ? 126.019 128.963 73.044  1.00 28.52  ? 271  SER C N     1 
ATOM   22594 C  CA    . SER C 3  271  ? 124.759 128.675 72.368  1.00 29.38  ? 271  SER C CA    1 
ATOM   22595 C  C     . SER C 3  271  ? 123.944 127.824 73.329  1.00 27.26  ? 271  SER C C     1 
ATOM   22596 O  O     . SER C 3  271  ? 124.163 126.618 73.441  1.00 35.81  ? 271  SER C O     1 
ATOM   22597 C  CB    . SER C 3  271  ? 124.986 127.978 71.034  1.00 31.73  ? 271  SER C CB    1 
ATOM   22598 O  OG    . SER C 3  271  ? 125.425 128.898 70.055  1.00 32.64  ? 271  SER C OG    1 
ATOM   22599 N  N     . MET C 3  272  ? 123.030 128.467 74.056  1.00 30.66  ? 272  MET C N     1 
ATOM   22600 C  CA    . MET C 3  272  ? 122.280 127.762 75.090  1.00 33.01  ? 272  MET C CA    1 
ATOM   22601 C  C     . MET C 3  272  ? 121.305 126.770 74.482  1.00 33.17  ? 272  MET C C     1 
ATOM   22602 O  O     . MET C 3  272  ? 121.156 125.649 74.978  1.00 37.26  ? 272  MET C O     1 
ATOM   22603 C  CB    . MET C 3  272  ? 121.541 128.756 75.981  1.00 35.71  ? 272  MET C CB    1 
ATOM   22604 C  CG    . MET C 3  272  ? 122.351 129.973 76.364  1.00 34.89  ? 272  MET C CG    1 
ATOM   22605 S  SD    . MET C 3  272  ? 121.606 130.846 77.743  1.00 45.08  ? 272  MET C SD    1 
ATOM   22606 C  CE    . MET C 3  272  ? 119.884 130.698 77.322  1.00 32.55  ? 272  MET C CE    1 
ATOM   22607 N  N     . ASP C 3  273  ? 120.637 127.162 73.407  1.00 35.80  ? 273  ASP C N     1 
ATOM   22608 C  CA    . ASP C 3  273  ? 119.688 126.289 72.734  1.00 40.12  ? 273  ASP C CA    1 
ATOM   22609 C  C     . ASP C 3  273  ? 119.910 126.358 71.234  1.00 42.59  ? 273  ASP C C     1 
ATOM   22610 O  O     . ASP C 3  273  ? 120.929 126.882 70.773  1.00 44.08  ? 273  ASP C O     1 
ATOM   22611 C  CB    . ASP C 3  273  ? 118.256 126.689 73.070  1.00 39.87  ? 273  ASP C CB    1 
ATOM   22612 C  CG    . ASP C 3  273  ? 117.947 126.559 74.530  1.00 44.36  ? 273  ASP C CG    1 
ATOM   22613 O  OD1   . ASP C 3  273  ? 118.396 125.570 75.143  1.00 44.17  ? 273  ASP C OD1   1 
ATOM   22614 O  OD2   . ASP C 3  273  ? 117.255 127.449 75.067  1.00 43.83  ? 273  ASP C OD2   1 
ATOM   22615 N  N     . GLU C 3  274  ? 118.963 125.835 70.463  1.00 41.35  ? 274  GLU C N     1 
ATOM   22616 C  CA    . GLU C 3  274  ? 119.035 125.967 69.017  1.00 41.58  ? 274  GLU C CA    1 
ATOM   22617 C  C     . GLU C 3  274  ? 118.749 127.385 68.546  1.00 43.30  ? 274  GLU C C     1 
ATOM   22618 O  O     . GLU C 3  274  ? 118.928 127.675 67.360  1.00 43.79  ? 274  GLU C O     1 
ATOM   22619 C  CB    . GLU C 3  274  ? 118.062 124.995 68.349  1.00 42.47  ? 274  GLU C CB    1 
ATOM   22620 C  CG    . GLU C 3  274  ? 116.596 125.361 68.505  1.00 44.64  ? 274  GLU C CG    1 
ATOM   22621 C  CD    . GLU C 3  274  ? 115.924 124.644 69.660  1.00 48.19  ? 274  GLU C CD    1 
ATOM   22622 O  OE1   . GLU C 3  274  ? 116.632 124.072 70.513  1.00 48.67  ? 274  GLU C OE1   1 
ATOM   22623 O  OE2   . GLU C 3  274  ? 114.678 124.640 69.705  1.00 45.85  ? 274  GLU C OE2   1 
ATOM   22624 N  N     . GLU C 3  275  ? 118.315 128.271 69.438  1.00 36.61  ? 275  GLU C N     1 
ATOM   22625 C  CA    . GLU C 3  275  ? 117.898 129.604 69.039  1.00 33.40  ? 275  GLU C CA    1 
ATOM   22626 C  C     . GLU C 3  275  ? 118.438 130.733 69.903  1.00 35.14  ? 275  GLU C C     1 
ATOM   22627 O  O     . GLU C 3  275  ? 118.369 131.886 69.473  1.00 36.77  ? 275  GLU C O     1 
ATOM   22628 C  CB    . GLU C 3  275  ? 116.364 129.671 69.013  1.00 31.31  ? 275  GLU C CB    1 
ATOM   22629 C  CG    . GLU C 3  275  ? 115.736 130.008 70.349  1.00 34.63  ? 275  GLU C CG    1 
ATOM   22630 C  CD    . GLU C 3  275  ? 115.745 128.830 71.309  1.00 38.43  ? 275  GLU C CD    1 
ATOM   22631 O  OE1   . GLU C 3  275  ? 116.334 127.789 70.971  1.00 38.11  ? 275  GLU C OE1   1 
ATOM   22632 O  OE2   . GLU C 3  275  ? 115.164 128.944 72.408  1.00 38.65  ? 275  GLU C OE2   1 
ATOM   22633 N  N     . LYS C 3  276  ? 118.990 130.454 71.079  1.00 28.44  ? 276  LYS C N     1 
ATOM   22634 C  CA    . LYS C 3  276  ? 119.341 131.488 72.039  1.00 24.84  ? 276  LYS C CA    1 
ATOM   22635 C  C     . LYS C 3  276  ? 120.849 131.519 72.257  1.00 22.80  ? 276  LYS C C     1 
ATOM   22636 O  O     . LYS C 3  276  ? 121.498 130.478 72.370  1.00 27.07  ? 276  LYS C O     1 
ATOM   22637 C  CB    . LYS C 3  276  ? 118.614 131.251 73.367  1.00 25.22  ? 276  LYS C CB    1 
ATOM   22638 C  CG    . LYS C 3  276  ? 118.209 132.515 74.096  1.00 24.43  ? 276  LYS C CG    1 
ATOM   22639 C  CD    . LYS C 3  276  ? 117.458 132.205 75.373  1.00 29.22  ? 276  LYS C CD    1 
ATOM   22640 C  CE    . LYS C 3  276  ? 116.060 131.701 75.125  1.00 30.04  ? 276  LYS C CE    1 
ATOM   22641 N  NZ    . LYS C 3  276  ? 115.224 132.733 74.485  1.00 27.82  ? 276  LYS C NZ    1 
ATOM   22642 N  N     . THR C 3  277  ? 121.401 132.728 72.329  1.00 18.85  ? 277  THR C N     1 
ATOM   22643 C  CA    . THR C 3  277  ? 122.835 132.940 72.470  1.00 19.99  ? 277  THR C CA    1 
ATOM   22644 C  C     . THR C 3  277  ? 123.098 133.773 73.716  1.00 21.47  ? 277  THR C C     1 
ATOM   22645 O  O     . THR C 3  277  ? 122.330 134.681 74.034  1.00 21.15  ? 277  THR C O     1 
ATOM   22646 C  CB    . THR C 3  277  ? 123.410 133.646 71.236  1.00 24.13  ? 277  THR C CB    1 
ATOM   22647 O  OG1   . THR C 3  277  ? 123.041 132.921 70.061  1.00 29.47  ? 277  THR C OG1   1 
ATOM   22648 C  CG2   . THR C 3  277  ? 124.916 133.701 71.302  1.00 20.08  ? 277  THR C CG2   1 
ATOM   22649 N  N     . LYS C 3  278  ? 124.181 133.463 74.420  1.00 20.26  ? 278  LYS C N     1 
ATOM   22650 C  CA    . LYS C 3  278  ? 124.524 134.124 75.671  1.00 15.06  ? 278  LYS C CA    1 
ATOM   22651 C  C     . LYS C 3  278  ? 125.940 134.674 75.604  1.00 15.35  ? 278  LYS C C     1 
ATOM   22652 O  O     . LYS C 3  278  ? 126.867 133.957 75.226  1.00 20.18  ? 278  LYS C O     1 
ATOM   22653 C  CB    . LYS C 3  278  ? 124.386 133.145 76.828  1.00 16.44  ? 278  LYS C CB    1 
ATOM   22654 C  CG    . LYS C 3  278  ? 124.665 133.710 78.178  1.00 13.86  ? 278  LYS C CG    1 
ATOM   22655 C  CD    . LYS C 3  278  ? 124.489 132.636 79.206  1.00 17.47  ? 278  LYS C CD    1 
ATOM   22656 C  CE    . LYS C 3  278  ? 124.659 133.173 80.589  1.00 20.92  ? 278  LYS C CE    1 
ATOM   22657 N  NZ    . LYS C 3  278  ? 124.472 132.096 81.578  1.00 22.59  ? 278  LYS C NZ    1 
ATOM   22658 N  N     . ALA C 3  279  ? 126.108 135.937 75.981  1.00 14.90  ? 279  ALA C N     1 
ATOM   22659 C  CA    . ALA C 3  279  ? 127.402 136.606 75.969  1.00 14.67  ? 279  ALA C CA    1 
ATOM   22660 C  C     . ALA C 3  279  ? 127.714 137.121 77.363  1.00 18.21  ? 279  ALA C C     1 
ATOM   22661 O  O     . ALA C 3  279  ? 126.841 137.682 78.026  1.00 27.86  ? 279  ALA C O     1 
ATOM   22662 C  CB    . ALA C 3  279  ? 127.415 137.760 74.970  1.00 10.75  ? 279  ALA C CB    1 
ATOM   22663 N  N     . ILE C 3  280  ? 128.948 136.921 77.813  1.00 7.65   ? 280  ILE C N     1 
ATOM   22664 C  CA    . ILE C 3  280  ? 129.394 137.399 79.114  1.00 4.05   ? 280  ILE C CA    1 
ATOM   22665 C  C     . ILE C 3  280  ? 130.700 138.147 78.920  1.00 9.82   ? 280  ILE C C     1 
ATOM   22666 O  O     . ILE C 3  280  ? 131.683 137.567 78.453  1.00 17.22  ? 280  ILE C O     1 
ATOM   22667 C  CB    . ILE C 3  280  ? 129.579 136.251 80.113  1.00 9.77   ? 280  ILE C CB    1 
ATOM   22668 C  CG1   . ILE C 3  280  ? 128.268 135.510 80.318  1.00 12.85  ? 280  ILE C CG1   1 
ATOM   22669 C  CG2   . ILE C 3  280  ? 130.063 136.779 81.428  1.00 11.43  ? 280  ILE C CG2   1 
ATOM   22670 C  CD1   . ILE C 3  280  ? 128.436 134.185 80.966  1.00 12.43  ? 280  ILE C CD1   1 
ATOM   22671 N  N     . ILE C 3  281  ? 130.724 139.418 79.300  1.00 12.19  ? 281  ILE C N     1 
ATOM   22672 C  CA    . ILE C 3  281  ? 131.884 140.282 79.119  1.00 10.83  ? 281  ILE C CA    1 
ATOM   22673 C  C     . ILE C 3  281  ? 132.399 140.670 80.494  1.00 6.18   ? 281  ILE C C     1 
ATOM   22674 O  O     . ILE C 3  281  ? 131.663 141.248 81.296  1.00 14.78  ? 281  ILE C O     1 
ATOM   22675 C  CB    . ILE C 3  281  ? 131.533 141.523 78.288  1.00 10.60  ? 281  ILE C CB    1 
ATOM   22676 C  CG1   . ILE C 3  281  ? 130.890 141.108 76.973  1.00 11.47  ? 281  ILE C CG1   1 
ATOM   22677 C  CG2   . ILE C 3  281  ? 132.764 142.329 78.002  1.00 16.77  ? 281  ILE C CG2   1 
ATOM   22678 C  CD1   . ILE C 3  281  ? 129.417 141.345 76.917  1.00 14.94  ? 281  ILE C CD1   1 
ATOM   22679 N  N     . THR C 3  282  ? 133.657 140.352 80.771  1.00 1.93   ? 282  THR C N     1 
ATOM   22680 C  CA    . THR C 3  282  ? 134.278 140.619 82.060  1.00 5.51   ? 282  THR C CA    1 
ATOM   22681 C  C     . THR C 3  282  ? 135.454 141.560 81.858  1.00 11.23  ? 282  THR C C     1 
ATOM   22682 O  O     . THR C 3  282  ? 136.463 141.173 81.265  1.00 22.03  ? 282  THR C O     1 
ATOM   22683 C  CB    . THR C 3  282  ? 134.742 139.324 82.722  1.00 13.19  ? 282  THR C CB    1 
ATOM   22684 O  OG1   . THR C 3  282  ? 133.640 138.419 82.829  1.00 17.19  ? 282  THR C OG1   1 
ATOM   22685 C  CG2   . THR C 3  282  ? 135.295 139.594 84.104  1.00 11.25  ? 282  THR C CG2   1 
ATOM   22686 N  N     . ILE C 3  283  ? 135.334 142.782 82.364  1.00 9.74   ? 283  ILE C N     1 
ATOM   22687 C  CA    . ILE C 3  283  ? 136.365 143.800 82.220  1.00 9.15   ? 283  ILE C CA    1 
ATOM   22688 C  C     . ILE C 3  283  ? 136.907 144.125 83.598  1.00 13.32  ? 283  ILE C C     1 
ATOM   22689 O  O     . ILE C 3  283  ? 136.156 144.542 84.482  1.00 16.12  ? 283  ILE C O     1 
ATOM   22690 C  CB    . ILE C 3  283  ? 135.830 145.070 81.538  1.00 10.77  ? 283  ILE C CB    1 
ATOM   22691 C  CG1   . ILE C 3  283  ? 134.948 144.707 80.352  1.00 13.79  ? 283  ILE C CG1   1 
ATOM   22692 C  CG2   . ILE C 3  283  ? 136.967 145.919 81.062  1.00 12.04  ? 283  ILE C CG2   1 
ATOM   22693 C  CD1   . ILE C 3  283  ? 135.692 144.060 79.249  1.00 14.98  ? 283  ILE C CD1   1 
ATOM   22694 N  N     . LYS C 3  284  ? 138.207 143.952 83.774  1.00 18.58  ? 284  LYS C N     1 
ATOM   22695 C  CA    . LYS C 3  284  ? 138.828 144.187 85.063  1.00 16.47  ? 284  LYS C CA    1 
ATOM   22696 C  C     . LYS C 3  284  ? 139.004 145.676 85.311  1.00 20.49  ? 284  LYS C C     1 
ATOM   22697 O  O     . LYS C 3  284  ? 139.413 146.424 84.421  1.00 24.22  ? 284  LYS C O     1 
ATOM   22698 C  CB    . LYS C 3  284  ? 140.175 143.480 85.135  1.00 18.93  ? 284  LYS C CB    1 
ATOM   22699 C  CG    . LYS C 3  284  ? 140.555 143.046 86.527  1.00 23.56  ? 284  LYS C CG    1 
ATOM   22700 C  CD    . LYS C 3  284  ? 139.995 141.677 86.862  1.00 27.14  ? 284  LYS C CD    1 
ATOM   22701 C  CE    . LYS C 3  284  ? 139.717 141.549 88.351  1.00 24.18  ? 284  LYS C CE    1 
ATOM   22702 N  NZ    . LYS C 3  284  ? 140.718 142.286 89.162  1.00 25.53  ? 284  LYS C NZ    1 
ATOM   22703 N  N     . ASP C 3  285  ? 138.689 146.095 86.537  1.00 23.14  ? 285  ASP C N     1 
ATOM   22704 C  CA    . ASP C 3  285  ? 138.803 147.482 86.983  1.00 22.42  ? 285  ASP C CA    1 
ATOM   22705 C  C     . ASP C 3  285  ? 137.853 148.421 86.242  1.00 21.70  ? 285  ASP C C     1 
ATOM   22706 O  O     . ASP C 3  285  ? 138.167 149.591 86.031  1.00 26.87  ? 285  ASP C O     1 
ATOM   22707 C  CB    . ASP C 3  285  ? 140.242 147.986 86.867  1.00 28.11  ? 285  ASP C CB    1 
ATOM   22708 C  CG    . ASP C 3  285  ? 140.670 148.801 88.061  1.00 33.18  ? 285  ASP C CG    1 
ATOM   22709 O  OD1   . ASP C 3  285  ? 140.002 148.715 89.111  1.00 30.48  ? 285  ASP C OD1   1 
ATOM   22710 O  OD2   . ASP C 3  285  ? 141.670 149.537 87.946  1.00 32.77  ? 285  ASP C OD2   1 
ATOM   22711 N  N     . GLU C 3  286  ? 136.680 147.940 85.858  1.00 12.88  ? 286  GLU C N     1 
ATOM   22712 C  CA    . GLU C 3  286  ? 135.661 148.822 85.322  1.00 14.57  ? 286  GLU C CA    1 
ATOM   22713 C  C     . GLU C 3  286  ? 134.592 149.092 86.375  1.00 18.59  ? 286  GLU C C     1 
ATOM   22714 O  O     . GLU C 3  286  ? 134.418 148.339 87.332  1.00 26.06  ? 286  GLU C O     1 
ATOM   22715 C  CB    . GLU C 3  286  ? 135.030 148.237 84.068  1.00 19.48  ? 286  GLU C CB    1 
ATOM   22716 C  CG    . GLU C 3  286  ? 135.684 148.676 82.785  1.00 20.87  ? 286  GLU C CG    1 
ATOM   22717 C  CD    . GLU C 3  286  ? 135.595 150.161 82.547  1.00 21.28  ? 286  GLU C CD    1 
ATOM   22718 O  OE1   . GLU C 3  286  ? 134.718 150.812 83.137  1.00 23.55  ? 286  GLU C OE1   1 
ATOM   22719 O  OE2   . GLU C 3  286  ? 136.393 150.678 81.745  1.00 20.92  ? 286  GLU C OE2   1 
ATOM   22720 N  N     . THR C 3  287  ? 133.867 150.187 86.186  1.00 9.18   ? 287  THR C N     1 
ATOM   22721 C  CA    . THR C 3  287  ? 132.998 150.722 87.217  1.00 7.97   ? 287  THR C CA    1 
ATOM   22722 C  C     . THR C 3  287  ? 131.562 150.765 86.708  1.00 4.56   ? 287  THR C C     1 
ATOM   22723 O  O     . THR C 3  287  ? 131.255 150.297 85.616  1.00 9.62   ? 287  THR C O     1 
ATOM   22724 C  CB    . THR C 3  287  ? 133.480 152.110 87.664  1.00 11.43  ? 287  THR C CB    1 
ATOM   22725 O  OG1   . THR C 3  287  ? 133.615 152.966 86.529  1.00 14.50  ? 287  THR C OG1   1 
ATOM   22726 C  CG2   . THR C 3  287  ? 134.822 152.001 88.325  1.00 7.10   ? 287  THR C CG2   1 
ATOM   22727 N  N     . HIS C 3  288  ? 130.677 151.330 87.526  1.00 6.56   ? 288  HIS C N     1 
ATOM   22728 C  CA    . HIS C 3  288  ? 129.261 151.402 87.194  1.00 2.68   ? 288  HIS C CA    1 
ATOM   22729 C  C     . HIS C 3  288  ? 128.982 152.314 86.014  1.00 2.89   ? 288  HIS C C     1 
ATOM   22730 O  O     . HIS C 3  288  ? 127.935 152.176 85.383  1.00 9.27   ? 288  HIS C O     1 
ATOM   22731 C  CB    . HIS C 3  288  ? 128.456 151.877 88.405  1.00 11.04  ? 288  HIS C CB    1 
ATOM   22732 C  CG    . HIS C 3  288  ? 128.365 150.871 89.503  1.00 5.10   ? 288  HIS C CG    1 
ATOM   22733 N  ND1   . HIS C 3  288  ? 127.467 149.829 89.481  1.00 12.87  ? 288  HIS C ND1   1 
ATOM   22734 C  CD2   . HIS C 3  288  ? 129.055 150.745 90.656  1.00 1.90   ? 288  HIS C CD2   1 
ATOM   22735 C  CE1   . HIS C 3  288  ? 127.609 149.104 90.573  1.00 1.85   ? 288  HIS C CE1   1 
ATOM   22736 N  NE2   . HIS C 3  288  ? 128.566 149.641 91.305  1.00 4.35   ? 288  HIS C NE2   1 
ATOM   22737 N  N     . THR C 3  289  ? 129.892 153.235 85.705  1.00 3.11   ? 289  THR C N     1 
ATOM   22738 C  CA    . THR C 3  289  ? 129.722 154.117 84.556  1.00 1.32   ? 289  THR C CA    1 
ATOM   22739 C  C     . THR C 3  289  ? 129.524 153.314 83.279  1.00 2.95   ? 289  THR C C     1 
ATOM   22740 O  O     . THR C 3  289  ? 128.485 153.408 82.616  1.00 6.07   ? 289  THR C O     1 
ATOM   22741 C  CB    . THR C 3  289  ? 130.944 155.036 84.430  1.00 1.39   ? 289  THR C CB    1 
ATOM   22742 O  OG1   . THR C 3  289  ? 131.189 155.687 85.676  1.00 2.48   ? 289  THR C OG1   1 
ATOM   22743 C  CG2   . THR C 3  289  ? 130.736 156.091 83.379  1.00 0.46   ? 289  THR C CG2   1 
ATOM   22744 N  N     . ILE C 3  290  ? 130.517 152.502 82.930  1.00 6.11   ? 290  ILE C N     1 
ATOM   22745 C  CA    . ILE C 3  290  ? 130.479 151.780 81.667  1.00 7.02   ? 290  ILE C CA    1 
ATOM   22746 C  C     . ILE C 3  290  ? 129.427 150.684 81.697  1.00 4.25   ? 290  ILE C C     1 
ATOM   22747 O  O     . ILE C 3  290  ? 128.738 150.454 80.701  1.00 10.41  ? 290  ILE C O     1 
ATOM   22748 C  CB    . ILE C 3  290  ? 131.870 151.229 81.325  1.00 6.90   ? 290  ILE C CB    1 
ATOM   22749 C  CG1   . ILE C 3  290  ? 132.865 152.373 81.175  1.00 6.52   ? 290  ILE C CG1   1 
ATOM   22750 C  CG2   . ILE C 3  290  ? 131.817 150.466 80.052  1.00 7.68   ? 290  ILE C CG2   1 
ATOM   22751 C  CD1   . ILE C 3  290  ? 132.468 153.403 80.173  1.00 4.88   ? 290  ILE C CD1   1 
ATOM   22752 N  N     . GLY C 3  291  ? 129.285 149.990 82.824  1.00 4.24   ? 291  GLY C N     1 
ATOM   22753 C  CA    . GLY C 3  291  ? 128.270 148.958 82.912  1.00 12.33  ? 291  GLY C CA    1 
ATOM   22754 C  C     . GLY C 3  291  ? 126.874 149.494 82.681  1.00 0.69   ? 291  GLY C C     1 
ATOM   22755 O  O     . GLY C 3  291  ? 126.106 148.935 81.893  1.00 12.32  ? 291  GLY C O     1 
ATOM   22756 N  N     . ASN C 3  292  ? 126.536 150.598 83.344  1.00 6.57   ? 292  ASN C N     1 
ATOM   22757 C  CA    . ASN C 3  292  ? 125.222 151.198 83.173  1.00 1.35   ? 292  ASN C CA    1 
ATOM   22758 C  C     . ASN C 3  292  ? 125.023 151.727 81.759  1.00 2.78   ? 292  ASN C C     1 
ATOM   22759 O  O     . ASN C 3  292  ? 123.953 151.536 81.171  1.00 10.05  ? 292  ASN C O     1 
ATOM   22760 C  CB    . ASN C 3  292  ? 125.029 152.307 84.196  1.00 11.97  ? 292  ASN C CB    1 
ATOM   22761 C  CG    . ASN C 3  292  ? 123.592 152.468 84.616  1.00 8.43   ? 292  ASN C CG    1 
ATOM   22762 O  OD1   . ASN C 3  292  ? 122.788 151.556 84.490  1.00 13.26  ? 292  ASN C OD1   1 
ATOM   22763 N  ND2   . ASN C 3  292  ? 123.255 153.646 85.090  1.00 10.15  ? 292  ASN C ND2   1 
ATOM   22764 N  N     . LEU C 3  293  ? 126.035 152.387 81.187  1.00 3.91   ? 293  LEU C N     1 
ATOM   22765 C  CA    . LEU C 3  293  ? 125.901 152.883 79.819  1.00 3.72   ? 293  LEU C CA    1 
ATOM   22766 C  C     . LEU C 3  293  ? 125.673 151.745 78.831  1.00 2.79   ? 293  LEU C C     1 
ATOM   22767 O  O     . LEU C 3  293  ? 124.788 151.816 77.969  1.00 3.91   ? 293  LEU C O     1 
ATOM   22768 C  CB    . LEU C 3  293  ? 127.142 153.676 79.422  1.00 2.57   ? 293  LEU C CB    1 
ATOM   22769 C  CG    . LEU C 3  293  ? 127.082 155.191 79.509  1.00 9.44   ? 293  LEU C CG    1 
ATOM   22770 C  CD1   . LEU C 3  293  ? 128.460 155.737 79.315  1.00 4.89   ? 293  LEU C CD1   1 
ATOM   22771 C  CD2   . LEU C 3  293  ? 126.147 155.743 78.483  1.00 2.41   ? 293  LEU C CD2   1 
ATOM   22772 N  N     . LEU C 3  294  ? 126.473 150.686 78.941  1.00 8.89   ? 294  LEU C N     1 
ATOM   22773 C  CA    . LEU C 3  294  ? 126.345 149.553 78.039  1.00 3.19   ? 294  LEU C CA    1 
ATOM   22774 C  C     . LEU C 3  294  ? 124.975 148.913 78.156  1.00 5.14   ? 294  LEU C C     1 
ATOM   22775 O  O     . LEU C 3  294  ? 124.332 148.628 77.144  1.00 14.92  ? 294  LEU C O     1 
ATOM   22776 C  CB    . LEU C 3  294  ? 127.432 148.527 78.335  1.00 2.87   ? 294  LEU C CB    1 
ATOM   22777 C  CG    . LEU C 3  294  ? 128.847 148.787 77.843  1.00 1.74   ? 294  LEU C CG    1 
ATOM   22778 C  CD1   . LEU C 3  294  ? 129.759 147.714 78.374  1.00 2.10   ? 294  LEU C CD1   1 
ATOM   22779 C  CD2   . LEU C 3  294  ? 128.871 148.815 76.353  1.00 6.01   ? 294  LEU C CD2   1 
ATOM   22780 N  N     . LYS C 3  295  ? 124.503 148.686 79.384  1.00 2.89   ? 295  LYS C N     1 
ATOM   22781 C  CA    . LYS C 3  295  ? 123.195 148.066 79.551  1.00 2.08   ? 295  LYS C CA    1 
ATOM   22782 C  C     . LYS C 3  295  ? 122.089 148.932 78.965  1.00 6.02   ? 295  LYS C C     1 
ATOM   22783 O  O     . LYS C 3  295  ? 121.209 148.433 78.259  1.00 13.90  ? 295  LYS C O     1 
ATOM   22784 C  CB    . LYS C 3  295  ? 122.927 147.775 81.025  1.00 1.31   ? 295  LYS C CB    1 
ATOM   22785 C  CG    . LYS C 3  295  ? 121.542 147.223 81.271  1.00 8.27   ? 295  LYS C CG    1 
ATOM   22786 C  CD    . LYS C 3  295  ? 121.370 146.711 82.661  1.00 0.82   ? 295  LYS C CD    1 
ATOM   22787 C  CE    . LYS C 3  295  ? 121.325 147.821 83.666  1.00 5.42   ? 295  LYS C CE    1 
ATOM   22788 N  NZ    . LYS C 3  295  ? 120.197 148.729 83.427  1.00 12.49  ? 295  LYS C NZ    1 
ATOM   22789 N  N     . THR C 3  296  ? 122.125 150.238 79.229  1.00 4.78   ? 296  THR C N     1 
ATOM   22790 C  CA    . THR C 3  296  ? 121.078 151.120 78.728  1.00 0.22   ? 296  THR C CA    1 
ATOM   22791 C  C     . THR C 3  296  ? 121.046 151.146 77.207  1.00 6.27   ? 296  THR C C     1 
ATOM   22792 O  O     . THR C 3  296  ? 119.972 151.083 76.600  1.00 14.05  ? 296  THR C O     1 
ATOM   22793 C  CB    . THR C 3  296  ? 121.281 152.527 79.285  1.00 8.28   ? 296  THR C CB    1 
ATOM   22794 O  OG1   . THR C 3  296  ? 121.063 152.511 80.698  1.00 11.21  ? 296  THR C OG1   1 
ATOM   22795 C  CG2   . THR C 3  296  ? 120.332 153.512 78.645  1.00 7.29   ? 296  THR C CG2   1 
ATOM   22796 N  N     . TYR C 3  297  ? 122.207 151.225 76.566  1.00 9.80   ? 297  TYR C N     1 
ATOM   22797 C  CA    . TYR C 3  297  ? 122.190 151.332 75.113  1.00 3.33   ? 297  TYR C CA    1 
ATOM   22798 C  C     . TYR C 3  297  ? 121.900 150.000 74.435  1.00 4.74   ? 297  TYR C C     1 
ATOM   22799 O  O     . TYR C 3  297  ? 121.246 149.978 73.387  1.00 11.84  ? 297  TYR C O     1 
ATOM   22800 C  CB    . TYR C 3  297  ? 123.501 151.932 74.627  1.00 7.07   ? 297  TYR C CB    1 
ATOM   22801 C  CG    . TYR C 3  297  ? 123.463 153.438 74.665  1.00 9.94   ? 297  TYR C CG    1 
ATOM   22802 C  CD1   . TYR C 3  297  ? 123.565 154.112 75.861  1.00 6.04   ? 297  TYR C CD1   1 
ATOM   22803 C  CD2   . TYR C 3  297  ? 123.284 154.179 73.516  1.00 11.95  ? 297  TYR C CD2   1 
ATOM   22804 C  CE1   . TYR C 3  297  ? 123.518 155.469 75.913  1.00 7.19   ? 297  TYR C CE1   1 
ATOM   22805 C  CE2   . TYR C 3  297  ? 123.232 155.545 73.559  1.00 12.51  ? 297  TYR C CE2   1 
ATOM   22806 C  CZ    . TYR C 3  297  ? 123.350 156.186 74.763  1.00 14.70  ? 297  TYR C CZ    1 
ATOM   22807 O  OH    . TYR C 3  297  ? 123.302 157.553 74.827  1.00 16.60  ? 297  TYR C OH    1 
ATOM   22808 N  N     . ILE C 3  298  ? 122.345 148.885 75.017  1.00 10.23  ? 298  ILE C N     1 
ATOM   22809 C  CA    . ILE C 3  298  ? 121.954 147.577 74.504  1.00 8.77   ? 298  ILE C CA    1 
ATOM   22810 C  C     . ILE C 3  298  ? 120.447 147.404 74.606  1.00 11.68  ? 298  ILE C C     1 
ATOM   22811 O  O     . ILE C 3  298  ? 119.806 146.875 73.693  1.00 11.66  ? 298  ILE C O     1 
ATOM   22812 C  CB    . ILE C 3  298  ? 122.702 146.462 75.255  1.00 4.96   ? 298  ILE C CB    1 
ATOM   22813 C  CG1   . ILE C 3  298  ? 124.174 146.453 74.876  1.00 7.09   ? 298  ILE C CG1   1 
ATOM   22814 C  CG2   . ILE C 3  298  ? 122.115 145.117 74.928  1.00 5.59   ? 298  ILE C CG2   1 
ATOM   22815 C  CD1   . ILE C 3  298  ? 125.042 145.669 75.826  1.00 8.81   ? 298  ILE C CD1   1 
ATOM   22816 N  N     . TYR C 3  299  ? 119.856 147.848 75.715  1.00 10.05  ? 299  TYR C N     1 
ATOM   22817 C  CA    . TYR C 3  299  ? 118.414 147.735 75.887  1.00 5.37   ? 299  TYR C CA    1 
ATOM   22818 C  C     . TYR C 3  299  ? 117.655 148.631 74.913  1.00 8.18   ? 299  TYR C C     1 
ATOM   22819 O  O     . TYR C 3  299  ? 116.570 148.270 74.449  1.00 9.74   ? 299  TYR C O     1 
ATOM   22820 C  CB    . TYR C 3  299  ? 118.057 148.059 77.332  1.00 4.85   ? 299  TYR C CB    1 
ATOM   22821 C  CG    . TYR C 3  299  ? 116.604 147.921 77.676  1.00 6.13   ? 299  TYR C CG    1 
ATOM   22822 C  CD1   . TYR C 3  299  ? 115.943 146.722 77.503  1.00 4.62   ? 299  TYR C CD1   1 
ATOM   22823 C  CD2   . TYR C 3  299  ? 115.902 148.983 78.204  1.00 9.72   ? 299  TYR C CD2   1 
ATOM   22824 C  CE1   . TYR C 3  299  ? 114.624 146.596 77.824  1.00 2.90   ? 299  TYR C CE1   1 
ATOM   22825 C  CE2   . TYR C 3  299  ? 114.588 148.863 78.528  1.00 10.64  ? 299  TYR C CE2   1 
ATOM   22826 C  CZ    . TYR C 3  299  ? 113.953 147.667 78.339  1.00 10.98  ? 299  TYR C CZ    1 
ATOM   22827 O  OH    . TYR C 3  299  ? 112.635 147.548 78.668  1.00 16.32  ? 299  TYR C OH    1 
ATOM   22828 N  N     . GLU C 3  300  ? 118.191 149.811 74.607  1.00 12.78  ? 300  GLU C N     1 
ATOM   22829 C  CA    . GLU C 3  300  ? 117.549 150.655 73.604  1.00 15.92  ? 300  GLU C CA    1 
ATOM   22830 C  C     . GLU C 3  300  ? 117.650 150.047 72.209  1.00 17.16  ? 300  GLU C C     1 
ATOM   22831 O  O     . GLU C 3  300  ? 116.745 150.219 71.388  1.00 15.18  ? 300  GLU C O     1 
ATOM   22832 C  CB    . GLU C 3  300  ? 118.146 152.057 73.620  1.00 11.60  ? 300  GLU C CB    1 
ATOM   22833 C  CG    . GLU C 3  300  ? 117.570 152.952 74.688  1.00 17.78  ? 300  GLU C CG    1 
ATOM   22834 C  CD    . GLU C 3  300  ? 118.321 154.263 74.831  1.00 27.83  ? 300  GLU C CD    1 
ATOM   22835 O  OE1   . GLU C 3  300  ? 119.339 154.456 74.133  1.00 23.27  ? 300  GLU C OE1   1 
ATOM   22836 O  OE2   . GLU C 3  300  ? 117.887 155.104 75.643  1.00 25.01  ? 300  GLU C OE2   1 
ATOM   22837 N  N     . MET C 3  301  ? 118.748 149.352 71.912  1.00 16.98  ? 301  MET C N     1 
ATOM   22838 C  CA    . MET C 3  301  ? 118.892 148.755 70.588  1.00 14.39  ? 301  MET C CA    1 
ATOM   22839 C  C     . MET C 3  301  ? 118.002 147.527 70.427  1.00 21.85  ? 301  MET C C     1 
ATOM   22840 O  O     . MET C 3  301  ? 117.422 147.309 69.358  1.00 20.27  ? 301  MET C O     1 
ATOM   22841 C  CB    . MET C 3  301  ? 120.354 148.401 70.338  1.00 13.69  ? 301  MET C CB    1 
ATOM   22842 C  CG    . MET C 3  301  ? 120.673 148.061 68.907  1.00 19.07  ? 301  MET C CG    1 
ATOM   22843 S  SD    . MET C 3  301  ? 121.064 149.538 67.963  1.00 39.72  ? 301  MET C SD    1 
ATOM   22844 C  CE    . MET C 3  301  ? 119.973 149.343 66.563  1.00 20.52  ? 301  MET C CE    1 
ATOM   22845 N  N     . ILE C 3  302  ? 117.877 146.718 71.474  1.00 21.06  ? 302  ILE C N     1 
ATOM   22846 C  CA    . ILE C 3  302  ? 117.082 145.494 71.438  1.00 12.74  ? 302  ILE C CA    1 
ATOM   22847 C  C     . ILE C 3  302  ? 115.974 145.588 72.477  1.00 15.52  ? 302  ILE C C     1 
ATOM   22848 O  O     . ILE C 3  302  ? 116.155 145.129 73.610  1.00 18.49  ? 302  ILE C O     1 
ATOM   22849 C  CB    . ILE C 3  302  ? 117.946 144.254 71.701  1.00 10.83  ? 302  ILE C CB    1 
ATOM   22850 C  CG1   . ILE C 3  302  ? 119.297 144.372 71.007  1.00 15.47  ? 302  ILE C CG1   1 
ATOM   22851 C  CG2   . ILE C 3  302  ? 117.236 143.026 71.229  1.00 11.87  ? 302  ILE C CG2   1 
ATOM   22852 C  CD1   . ILE C 3  302  ? 120.323 143.394 71.510  1.00 11.80  ? 302  ILE C CD1   1 
ATOM   22853 N  N     . PRO C 3  303  ? 114.822 146.169 72.146  1.00 16.82  ? 303  PRO C N     1 
ATOM   22854 C  CA    . PRO C 3  303  ? 113.739 146.269 73.137  1.00 14.97  ? 303  PRO C CA    1 
ATOM   22855 C  C     . PRO C 3  303  ? 113.175 144.930 73.576  1.00 19.57  ? 303  PRO C C     1 
ATOM   22856 O  O     . PRO C 3  303  ? 112.601 144.840 74.665  1.00 18.05  ? 303  PRO C O     1 
ATOM   22857 C  CB    . PRO C 3  303  ? 112.685 147.107 72.405  1.00 15.63  ? 303  PRO C CB    1 
ATOM   22858 C  CG    . PRO C 3  303  ? 113.420 147.784 71.321  1.00 20.30  ? 303  PRO C CG    1 
ATOM   22859 C  CD    . PRO C 3  303  ? 114.479 146.850 70.895  1.00 15.69  ? 303  PRO C CD    1 
ATOM   22860 N  N     . ASP C 3  304  ? 113.304 143.890 72.756  1.00 24.00  ? 304  ASP C N     1 
ATOM   22861 C  CA    . ASP C 3  304  ? 112.696 142.583 72.999  1.00 18.48  ? 304  ASP C CA    1 
ATOM   22862 C  C     . ASP C 3  304  ? 113.719 141.541 73.421  1.00 17.79  ? 304  ASP C C     1 
ATOM   22863 O  O     . ASP C 3  304  ? 113.660 140.394 72.981  1.00 18.63  ? 304  ASP C O     1 
ATOM   22864 C  CB    . ASP C 3  304  ? 111.944 142.116 71.761  1.00 19.26  ? 304  ASP C CB    1 
ATOM   22865 C  CG    . ASP C 3  304  ? 112.729 142.335 70.488  1.00 29.69  ? 304  ASP C CG    1 
ATOM   22866 O  OD1   . ASP C 3  304  ? 112.898 141.370 69.712  1.00 30.29  ? 304  ASP C OD1   1 
ATOM   22867 O  OD2   . ASP C 3  304  ? 113.172 143.476 70.250  1.00 29.07  ? 304  ASP C OD2   1 
ATOM   22868 N  N     . ILE C 3  305  ? 114.674 141.923 74.266  1.00 15.34  ? 305  ILE C N     1 
ATOM   22869 C  CA    . ILE C 3  305  ? 115.752 141.028 74.651  1.00 8.05   ? 305  ILE C CA    1 
ATOM   22870 C  C     . ILE C 3  305  ? 115.298 140.130 75.792  1.00 6.59   ? 305  ILE C C     1 
ATOM   22871 O  O     . ILE C 3  305  ? 114.373 140.465 76.536  1.00 7.44   ? 305  ILE C O     1 
ATOM   22872 C  CB    . ILE C 3  305  ? 116.996 141.854 75.021  1.00 0.33   ? 305  ILE C CB    1 
ATOM   22873 C  CG1   . ILE C 3  305  ? 118.248 140.988 75.020  1.00 5.55   ? 305  ILE C CG1   1 
ATOM   22874 C  CG2   . ILE C 3  305  ? 116.810 142.553 76.344  1.00 4.56   ? 305  ILE C CG2   1 
ATOM   22875 C  CD1   . ILE C 3  305  ? 119.504 141.775 74.966  1.00 8.01   ? 305  ILE C CD1   1 
ATOM   22876 N  N     . SER C 3  306  ? 115.927 138.959 75.913  1.00 7.78   ? 306  SER C N     1 
ATOM   22877 C  CA    . SER C 3  306  ? 115.604 138.062 77.015  1.00 3.30   ? 306  SER C CA    1 
ATOM   22878 C  C     . SER C 3  306  ? 116.156 138.579 78.330  1.00 4.71   ? 306  SER C C     1 
ATOM   22879 O  O     . SER C 3  306  ? 115.453 138.586 79.341  1.00 8.90   ? 306  SER C O     1 
ATOM   22880 C  CB    . SER C 3  306  ? 116.140 136.664 76.735  1.00 3.44   ? 306  SER C CB    1 
ATOM   22881 O  OG    . SER C 3  306  ? 115.607 136.157 75.536  1.00 13.78  ? 306  SER C OG    1 
ATOM   22882 N  N     . PHE C 3  307  ? 117.406 139.025 78.337  1.00 2.33   ? 307  PHE C N     1 
ATOM   22883 C  CA    . PHE C 3  307  ? 118.011 139.520 79.557  1.00 2.48   ? 307  PHE C CA    1 
ATOM   22884 C  C     . PHE C 3  307  ? 119.225 140.359 79.210  1.00 5.69   ? 307  PHE C C     1 
ATOM   22885 O  O     . PHE C 3  307  ? 120.007 139.989 78.340  1.00 11.08  ? 307  PHE C O     1 
ATOM   22886 C  CB    . PHE C 3  307  ? 118.413 138.368 80.485  1.00 9.17   ? 307  PHE C CB    1 
ATOM   22887 C  CG    . PHE C 3  307  ? 118.943 138.820 81.802  1.00 0.62   ? 307  PHE C CG    1 
ATOM   22888 C  CD1   . PHE C 3  307  ? 118.089 139.284 82.776  1.00 1.56   ? 307  PHE C CD1   1 
ATOM   22889 C  CD2   . PHE C 3  307  ? 120.294 138.791 82.065  1.00 1.49   ? 307  PHE C CD2   1 
ATOM   22890 C  CE1   . PHE C 3  307  ? 118.569 139.710 83.979  1.00 9.66   ? 307  PHE C CE1   1 
ATOM   22891 C  CE2   . PHE C 3  307  ? 120.774 139.214 83.269  1.00 0.48   ? 307  PHE C CE2   1 
ATOM   22892 C  CZ    . PHE C 3  307  ? 119.909 139.675 84.228  1.00 1.29   ? 307  PHE C CZ    1 
ATOM   22893 N  N     . VAL C 3  308  ? 119.366 141.493 79.886  1.00 3.63   ? 308  VAL C N     1 
ATOM   22894 C  CA    . VAL C 3  308  ? 120.617 142.237 79.917  1.00 3.07   ? 308  VAL C CA    1 
ATOM   22895 C  C     . VAL C 3  308  ? 120.819 142.718 81.346  1.00 3.55   ? 308  VAL C C     1 
ATOM   22896 O  O     . VAL C 3  308  ? 119.863 143.137 82.005  1.00 5.64   ? 308  VAL C O     1 
ATOM   22897 C  CB    . VAL C 3  308  ? 120.642 143.403 78.902  1.00 0.56   ? 308  VAL C CB    1 
ATOM   22898 C  CG1   . VAL C 3  308  ? 119.593 144.449 79.211  1.00 15.42  ? 308  VAL C CG1   1 
ATOM   22899 C  CG2   . VAL C 3  308  ? 122.020 144.014 78.821  1.00 3.23   ? 308  VAL C CG2   1 
ATOM   22900 N  N     . GLY C 3  309  ? 122.044 142.605 81.844  1.00 0.52   ? 309  GLY C N     1 
ATOM   22901 C  CA    . GLY C 3  309  ? 122.343 143.039 83.194  1.00 2.19   ? 309  GLY C CA    1 
ATOM   22902 C  C     . GLY C 3  309  ? 123.832 143.054 83.424  1.00 6.13   ? 309  GLY C C     1 
ATOM   22903 O  O     . GLY C 3  309  ? 124.594 142.402 82.715  1.00 10.11  ? 309  GLY C O     1 
ATOM   22904 N  N     . TYR C 3  310  ? 124.242 143.812 84.433  1.00 3.51   ? 310  TYR C N     1 
ATOM   22905 C  CA    . TYR C 3  310  ? 125.653 143.968 84.742  1.00 5.78   ? 310  TYR C CA    1 
ATOM   22906 C  C     . TYR C 3  310  ? 125.845 143.866 86.243  1.00 0.61   ? 310  TYR C C     1 
ATOM   22907 O  O     . TYR C 3  310  ? 124.894 143.935 87.017  1.00 2.43   ? 310  TYR C O     1 
ATOM   22908 C  CB    . TYR C 3  310  ? 126.214 145.293 84.200  1.00 2.58   ? 310  TYR C CB    1 
ATOM   22909 C  CG    . TYR C 3  310  ? 125.947 146.497 85.066  1.00 12.29  ? 310  TYR C CG    1 
ATOM   22910 C  CD1   . TYR C 3  310  ? 124.745 147.165 84.989  1.00 0.15   ? 310  TYR C CD1   1 
ATOM   22911 C  CD2   . TYR C 3  310  ? 126.901 146.975 85.944  1.00 8.12   ? 310  TYR C CD2   1 
ATOM   22912 C  CE1   . TYR C 3  310  ? 124.494 148.245 85.765  1.00 2.70   ? 310  TYR C CE1   1 
ATOM   22913 C  CE2   . TYR C 3  310  ? 126.655 148.058 86.724  1.00 12.98  ? 310  TYR C CE2   1 
ATOM   22914 C  CZ    . TYR C 3  310  ? 125.447 148.694 86.632  1.00 4.34   ? 310  TYR C CZ    1 
ATOM   22915 O  OH    . TYR C 3  310  ? 125.176 149.797 87.407  1.00 9.09   ? 310  TYR C OH    1 
ATOM   22916 N  N     . GLN C 3  311  ? 127.094 143.688 86.649  1.00 3.61   ? 311  GLN C N     1 
ATOM   22917 C  CA    . GLN C 3  311  ? 127.418 143.528 88.054  1.00 0.09   ? 311  GLN C CA    1 
ATOM   22918 C  C     . GLN C 3  311  ? 128.790 144.114 88.327  1.00 2.33   ? 311  GLN C C     1 
ATOM   22919 O  O     . GLN C 3  311  ? 129.725 143.865 87.569  1.00 7.22   ? 311  GLN C O     1 
ATOM   22920 C  CB    . GLN C 3  311  ? 127.387 142.055 88.442  1.00 14.88  ? 311  GLN C CB    1 
ATOM   22921 C  CG    . GLN C 3  311  ? 126.834 141.792 89.800  1.00 5.94   ? 311  GLN C CG    1 
ATOM   22922 C  CD    . GLN C 3  311  ? 126.865 140.328 90.130  1.00 11.11  ? 311  GLN C CD    1 
ATOM   22923 O  OE1   . GLN C 3  311  ? 126.988 139.488 89.241  1.00 14.35  ? 311  GLN C OE1   1 
ATOM   22924 N  NE2   . GLN C 3  311  ? 126.762 140.008 91.410  1.00 8.89   ? 311  GLN C NE2   1 
ATOM   22925 N  N     . CYS C 3  312  ? 128.904 144.901 89.393  1.00 3.31   ? 312  CYS C N     1 
ATOM   22926 C  CA    . CYS C 3  312  ? 130.189 145.368 89.906  1.00 2.22   ? 312  CYS C CA    1 
ATOM   22927 C  C     . CYS C 3  312  ? 130.230 145.042 91.391  1.00 2.03   ? 312  CYS C C     1 
ATOM   22928 O  O     . CYS C 3  312  ? 129.945 145.895 92.231  1.00 8.78   ? 312  CYS C O     1 
ATOM   22929 C  CB    . CYS C 3  312  ? 130.410 146.862 89.669  1.00 4.56   ? 312  CYS C CB    1 
ATOM   22930 S  SG    . CYS C 3  312  ? 130.385 147.415 87.978  1.00 6.92   ? 312  CYS C SG    1 
ATOM   22931 N  N     . VAL C 3  313  ? 130.615 143.820 91.713  1.00 0.17   ? 313  VAL C N     1 
ATOM   22932 C  CA    . VAL C 3  313  ? 130.739 143.404 93.112  1.00 1.50   ? 313  VAL C CA    1 
ATOM   22933 C  C     . VAL C 3  313  ? 131.960 144.079 93.723  1.00 4.24   ? 313  VAL C C     1 
ATOM   22934 O  O     . VAL C 3  313  ? 133.055 143.994 93.149  1.00 9.88   ? 313  VAL C O     1 
ATOM   22935 C  CB    . VAL C 3  313  ? 130.849 141.887 93.201  1.00 4.04   ? 313  VAL C CB    1 
ATOM   22936 C  CG1   . VAL C 3  313  ? 131.085 141.466 94.607  1.00 5.51   ? 313  VAL C CG1   1 
ATOM   22937 C  CG2   . VAL C 3  313  ? 129.597 141.252 92.661  1.00 2.56   ? 313  VAL C CG2   1 
ATOM   22938 N  N     . PRO C 3  314  ? 131.829 144.758 94.865  1.00 4.50   ? 314  PRO C N     1 
ATOM   22939 C  CA    . PRO C 3  314  ? 132.958 145.541 95.379  1.00 13.99  ? 314  PRO C CA    1 
ATOM   22940 C  C     . PRO C 3  314  ? 134.212 144.733 95.645  1.00 0.52   ? 314  PRO C C     1 
ATOM   22941 O  O     . PRO C 3  314  ? 135.311 145.270 95.486  1.00 10.41  ? 314  PRO C O     1 
ATOM   22942 C  CB    . PRO C 3  314  ? 132.390 146.149 96.663  1.00 4.46   ? 314  PRO C CB    1 
ATOM   22943 C  CG    . PRO C 3  314  ? 130.957 146.206 96.443  1.00 4.21   ? 314  PRO C CG    1 
ATOM   22944 C  CD    . PRO C 3  314  ? 130.612 144.994 95.653  1.00 1.59   ? 314  PRO C CD    1 
ATOM   22945 N  N     . HIS C 3  315  ? 134.099 143.466 96.020  1.00 1.53   ? 315  HIS C N     1 
ATOM   22946 C  CA    . HIS C 3  315  ? 135.264 142.666 96.360  1.00 1.10   ? 315  HIS C CA    1 
ATOM   22947 C  C     . HIS C 3  315  ? 135.854 141.926 95.168  1.00 6.78   ? 315  HIS C C     1 
ATOM   22948 O  O     . HIS C 3  315  ? 136.776 141.131 95.351  1.00 10.95  ? 315  HIS C O     1 
ATOM   22949 C  CB    . HIS C 3  315  ? 134.933 141.678 97.487  1.00 3.64   ? 315  HIS C CB    1 
ATOM   22950 C  CG    . HIS C 3  315  ? 134.058 140.527 97.085  1.00 3.78   ? 315  HIS C CG    1 
ATOM   22951 N  ND1   . HIS C 3  315  ? 134.525 139.447 96.373  1.00 7.00   ? 315  HIS C ND1   1 
ATOM   22952 C  CD2   . HIS C 3  315  ? 132.756 140.267 97.342  1.00 3.20   ? 315  HIS C CD2   1 
ATOM   22953 C  CE1   . HIS C 3  315  ? 133.543 138.587 96.183  1.00 2.65   ? 315  HIS C CE1   1 
ATOM   22954 N  NE2   . HIS C 3  315  ? 132.459 139.060 96.762  1.00 15.28  ? 315  HIS C NE2   1 
ATOM   22955 N  N     . LYS C 3  316  ? 135.369 142.171 93.958  1.00 8.15   ? 316  LYS C N     1 
ATOM   22956 C  CA    . LYS C 3  316  ? 135.909 141.515 92.781  1.00 4.76   ? 316  LYS C CA    1 
ATOM   22957 C  C     . LYS C 3  316  ? 136.681 142.435 91.856  1.00 10.19  ? 316  LYS C C     1 
ATOM   22958 O  O     . LYS C 3  316  ? 137.495 141.938 91.074  1.00 17.72  ? 316  LYS C O     1 
ATOM   22959 C  CB    . LYS C 3  316  ? 134.792 140.835 91.985  1.00 6.35   ? 316  LYS C CB    1 
ATOM   22960 C  CG    . LYS C 3  316  ? 134.044 139.823 92.789  1.00 9.11   ? 316  LYS C CG    1 
ATOM   22961 C  CD    . LYS C 3  316  ? 133.493 138.733 91.928  1.00 12.60  ? 316  LYS C CD    1 
ATOM   22962 C  CE    . LYS C 3  316  ? 134.607 137.803 91.526  1.00 17.82  ? 316  LYS C CE    1 
ATOM   22963 N  NZ    . LYS C 3  316  ? 135.372 137.346 92.707  1.00 8.93   ? 316  LYS C NZ    1 
ATOM   22964 N  N     . GLN C 3  317  ? 136.461 143.746 91.924  1.00 8.79   ? 317  GLN C N     1 
ATOM   22965 C  CA    . GLN C 3  317  ? 137.192 144.725 91.123  1.00 12.25  ? 317  GLN C CA    1 
ATOM   22966 C  C     . GLN C 3  317  ? 137.079 144.442 89.628  1.00 19.78  ? 317  GLN C C     1 
ATOM   22967 O  O     . GLN C 3  317  ? 138.061 144.498 88.890  1.00 21.75  ? 317  GLN C O     1 
ATOM   22968 C  CB    . GLN C 3  317  ? 138.654 144.795 91.551  1.00 16.50  ? 317  GLN C CB    1 
ATOM   22969 C  CG    . GLN C 3  317  ? 138.884 145.501 92.870  1.00 19.32  ? 317  GLN C CG    1 
ATOM   22970 C  CD    . GLN C 3  317  ? 139.821 144.748 93.785  1.00 18.41  ? 317  GLN C CD    1 
ATOM   22971 O  OE1   . GLN C 3  317  ? 139.606 143.581 94.086  1.00 15.74  ? 317  GLN C OE1   1 
ATOM   22972 N  NE2   . GLN C 3  317  ? 140.868 145.418 94.234  1.00 22.45  ? 317  GLN C NE2   1 
ATOM   22973 N  N     . GLU C 3  318  ? 135.866 144.146 89.174  1.00 16.69  ? 318  GLU C N     1 
ATOM   22974 C  CA    . GLU C 3  318  ? 135.615 143.911 87.761  1.00 9.96   ? 318  GLU C CA    1 
ATOM   22975 C  C     . GLU C 3  318  ? 134.148 144.175 87.475  1.00 16.46  ? 318  GLU C C     1 
ATOM   22976 O  O     . GLU C 3  318  ? 133.322 144.225 88.386  1.00 26.17  ? 318  GLU C O     1 
ATOM   22977 C  CB    . GLU C 3  318  ? 135.993 142.488 87.357  1.00 11.97  ? 318  GLU C CB    1 
ATOM   22978 C  CG    . GLU C 3  318  ? 134.925 141.475 87.621  1.00 14.44  ? 318  GLU C CG    1 
ATOM   22979 C  CD    . GLU C 3  318  ? 135.484 140.147 88.045  1.00 23.82  ? 318  GLU C CD    1 
ATOM   22980 O  OE1   . GLU C 3  318  ? 136.704 140.067 88.280  1.00 24.47  ? 318  GLU C OE1   1 
ATOM   22981 O  OE2   . GLU C 3  318  ? 134.709 139.179 88.147  1.00 23.55  ? 318  GLU C OE2   1 
ATOM   22982 N  N     . MET C 3  319  ? 133.837 144.348 86.197  1.00 9.88   ? 319  MET C N     1 
ATOM   22983 C  CA    . MET C 3  319  ? 132.473 144.521 85.724  1.00 1.73   ? 319  MET C CA    1 
ATOM   22984 C  C     . MET C 3  319  ? 132.128 143.361 84.803  1.00 5.39   ? 319  MET C C     1 
ATOM   22985 O  O     . MET C 3  319  ? 132.869 143.079 83.861  1.00 14.58  ? 319  MET C O     1 
ATOM   22986 C  CB    . MET C 3  319  ? 132.323 145.850 84.984  1.00 4.99   ? 319  MET C CB    1 
ATOM   22987 C  CG    . MET C 3  319  ? 130.896 146.272 84.683  1.00 6.56   ? 319  MET C CG    1 
ATOM   22988 S  SD    . MET C 3  319  ? 130.198 145.633 83.150  1.00 28.81  ? 319  MET C SD    1 
ATOM   22989 C  CE    . MET C 3  319  ? 131.330 146.274 81.938  1.00 4.56   ? 319  MET C CE    1 
ATOM   22990 N  N     . VAL C 3  320  ? 131.010 142.694 85.070  1.00 5.62   ? 320  VAL C N     1 
ATOM   22991 C  CA    . VAL C 3  320  ? 130.556 141.553 84.283  1.00 1.60   ? 320  VAL C CA    1 
ATOM   22992 C  C     . VAL C 3  320  ? 129.222 141.908 83.651  1.00 1.93   ? 320  VAL C C     1 
ATOM   22993 O  O     . VAL C 3  320  ? 128.249 142.172 84.360  1.00 7.29   ? 320  VAL C O     1 
ATOM   22994 C  CB    . VAL C 3  320  ? 130.418 140.287 85.140  1.00 1.38   ? 320  VAL C CB    1 
ATOM   22995 C  CG1   . VAL C 3  320  ? 130.063 139.103 84.272  1.00 3.83   ? 320  VAL C CG1   1 
ATOM   22996 C  CG2   . VAL C 3  320  ? 131.680 140.024 85.909  1.00 4.26   ? 320  VAL C CG2   1 
ATOM   22997 N  N     . LEU C 3  321  ? 129.162 141.878 82.327  1.00 7.07   ? 321  LEU C N     1 
ATOM   22998 C  CA    . LEU C 3  321  ? 127.945 142.172 81.586  1.00 14.95  ? 321  LEU C CA    1 
ATOM   22999 C  C     . LEU C 3  321  ? 127.424 140.893 80.943  1.00 4.15   ? 321  LEU C C     1 
ATOM   23000 O  O     . LEU C 3  321  ? 128.161 140.212 80.232  1.00 8.71   ? 321  LEU C O     1 
ATOM   23001 C  CB    . LEU C 3  321  ? 128.207 143.244 80.532  1.00 0.71   ? 321  LEU C CB    1 
ATOM   23002 C  CG    . LEU C 3  321  ? 127.044 143.651 79.631  1.00 4.82   ? 321  LEU C CG    1 
ATOM   23003 C  CD1   . LEU C 3  321  ? 126.085 144.578 80.334  1.00 1.93   ? 321  LEU C CD1   1 
ATOM   23004 C  CD2   . LEU C 3  321  ? 127.568 144.282 78.373  1.00 7.46   ? 321  LEU C CD2   1 
ATOM   23005 N  N     . THR C 3  322  ? 126.157 140.580 81.179  1.00 0.08   ? 322  THR C N     1 
ATOM   23006 C  CA    . THR C 3  322  ? 125.524 139.374 80.663  1.00 14.31  ? 322  THR C CA    1 
ATOM   23007 C  C     . THR C 3  322  ? 124.415 139.748 79.692  1.00 4.77   ? 322  THR C C     1 
ATOM   23008 O  O     . THR C 3  322  ? 123.556 140.569 80.016  1.00 15.27  ? 322  THR C O     1 
ATOM   23009 C  CB    . THR C 3  322  ? 124.947 138.525 81.797  1.00 4.98   ? 322  THR C CB    1 
ATOM   23010 O  OG1   . THR C 3  322  ? 125.965 138.241 82.759  1.00 12.06  ? 322  THR C OG1   1 
ATOM   23011 C  CG2   . THR C 3  322  ? 124.400 137.225 81.262  1.00 8.60   ? 322  THR C CG2   1 
ATOM   23012 N  N     . ILE C 3  323  ? 124.431 139.138 78.510  1.00 2.42   ? 323  ILE C N     1 
ATOM   23013 C  CA    . ILE C 3  323  ? 123.406 139.345 77.495  1.00 6.75   ? 323  ILE C CA    1 
ATOM   23014 C  C     . ILE C 3  323  ? 122.880 137.987 77.065  1.00 8.78   ? 323  ILE C C     1 
ATOM   23015 O  O     . ILE C 3  323  ? 123.661 137.068 76.813  1.00 13.49  ? 323  ILE C O     1 
ATOM   23016 C  CB    . ILE C 3  323  ? 123.947 140.124 76.282  1.00 3.24   ? 323  ILE C CB    1 
ATOM   23017 C  CG1   . ILE C 3  323  ? 124.554 141.443 76.735  1.00 3.70   ? 323  ILE C CG1   1 
ATOM   23018 C  CG2   . ILE C 3  323  ? 122.854 140.383 75.285  1.00 1.79   ? 323  ILE C CG2   1 
ATOM   23019 C  CD1   . ILE C 3  323  ? 125.655 141.914 75.872  1.00 4.24   ? 323  ILE C CD1   1 
ATOM   23020 N  N     . ILE C 3  324  ? 121.562 137.849 77.008  1.00 5.34   ? 324  ILE C N     1 
ATOM   23021 C  CA    . ILE C 3  324  ? 120.914 136.641 76.515  1.00 3.11   ? 324  ILE C CA    1 
ATOM   23022 C  C     . ILE C 3  324  ? 119.909 137.067 75.463  1.00 6.86   ? 324  ILE C C     1 
ATOM   23023 O  O     . ILE C 3  324  ? 118.977 137.815 75.763  1.00 14.21  ? 324  ILE C O     1 
ATOM   23024 C  CB    . ILE C 3  324  ? 120.231 135.851 77.641  1.00 0.59   ? 324  ILE C CB    1 
ATOM   23025 C  CG1   . ILE C 3  324  ? 121.276 135.319 78.612  1.00 2.24   ? 324  ILE C CG1   1 
ATOM   23026 C  CG2   . ILE C 3  324  ? 119.446 134.716 77.078  1.00 7.38   ? 324  ILE C CG2   1 
ATOM   23027 C  CD1   . ILE C 3  324  ? 120.723 134.799 79.874  1.00 2.63   ? 324  ILE C CD1   1 
ATOM   23028 N  N     . HIS C 3  325  ? 120.096 136.603 74.233  1.00 8.00   ? 325  HIS C N     1 
ATOM   23029 C  CA    . HIS C 3  325  ? 119.248 137.035 73.137  1.00 9.89   ? 325  HIS C CA    1 
ATOM   23030 C  C     . HIS C 3  325  ? 118.956 135.854 72.229  1.00 16.47  ? 325  HIS C C     1 
ATOM   23031 O  O     . HIS C 3  325  ? 119.697 134.874 72.188  1.00 18.18  ? 325  HIS C O     1 
ATOM   23032 C  CB    . HIS C 3  325  ? 119.889 138.179 72.347  1.00 9.96   ? 325  HIS C CB    1 
ATOM   23033 C  CG    . HIS C 3  325  ? 118.969 138.823 71.360  1.00 15.55  ? 325  HIS C CG    1 
ATOM   23034 N  ND1   . HIS C 3  325  ? 117.655 139.112 71.648  1.00 16.18  ? 325  HIS C ND1   1 
ATOM   23035 C  CD2   . HIS C 3  325  ? 119.178 139.248 70.094  1.00 14.77  ? 325  HIS C CD2   1 
ATOM   23036 C  CE1   . HIS C 3  325  ? 117.091 139.679 70.598  1.00 14.54  ? 325  HIS C CE1   1 
ATOM   23037 N  NE2   . HIS C 3  325  ? 117.994 139.775 69.642  1.00 10.92  ? 325  HIS C NE2   1 
ATOM   23038 N  N     . LYS C 3  326  ? 117.870 135.983 71.474  1.00 21.35  ? 326  LYS C N     1 
ATOM   23039 C  CA    . LYS C 3  326  ? 117.325 134.924 70.629  1.00 19.81  ? 326  LYS C CA    1 
ATOM   23040 C  C     . LYS C 3  326  ? 117.869 134.988 69.212  1.00 18.94  ? 326  LYS C C     1 
ATOM   23041 O  O     . LYS C 3  326  ? 117.145 134.722 68.257  1.00 29.15  ? 326  LYS C O     1 
ATOM   23042 C  CB    . LYS C 3  326  ? 115.807 135.010 70.613  1.00 23.04  ? 326  LYS C CB    1 
ATOM   23043 C  CG    . LYS C 3  326  ? 115.100 133.906 71.357  1.00 21.67  ? 326  LYS C CG    1 
ATOM   23044 C  CD    . LYS C 3  326  ? 113.592 134.134 71.344  1.00 24.20  ? 326  LYS C CD    1 
ATOM   23045 C  CE    . LYS C 3  326  ? 113.016 134.154 72.752  1.00 21.99  ? 326  LYS C CE    1 
ATOM   23046 N  NZ    . LYS C 3  326  ? 111.526 134.155 72.785  1.00 27.05  ? 326  LYS C NZ    1 
ATOM   23047 N  N     . ALA C 3  327  ? 119.129 135.355 69.041  1.00 23.76  ? 327  ALA C N     1 
ATOM   23048 C  CA    . ALA C 3  327  ? 119.765 135.457 67.738  1.00 27.53  ? 327  ALA C CA    1 
ATOM   23049 C  C     . ALA C 3  327  ? 121.022 134.595 67.708  1.00 25.94  ? 327  ALA C C     1 
ATOM   23050 O  O     . ALA C 3  327  ? 121.428 134.015 68.712  1.00 30.13  ? 327  ALA C O     1 
ATOM   23051 C  CB    . ALA C 3  327  ? 120.098 136.913 67.412  1.00 26.94  ? 327  ALA C CB    1 
ATOM   23052 N  N     . SER C 3  328  ? 121.637 134.508 66.531  1.00 31.08  ? 328  SER C N     1 
ATOM   23053 C  CA    . SER C 3  328  ? 122.899 133.802 66.382  1.00 33.52  ? 328  SER C CA    1 
ATOM   23054 C  C     . SER C 3  328  ? 124.045 134.690 66.855  1.00 34.06  ? 328  SER C C     1 
ATOM   23055 O  O     . SER C 3  328  ? 123.879 135.889 67.080  1.00 39.76  ? 328  SER C O     1 
ATOM   23056 C  CB    . SER C 3  328  ? 123.090 133.358 64.936  1.00 33.59  ? 328  SER C CB    1 
ATOM   23057 O  OG    . SER C 3  328  ? 123.223 134.466 64.067  1.00 36.52  ? 328  SER C OG    1 
ATOM   23058 N  N     . GLN C 3  329  ? 125.232 134.101 67.006  1.00 32.21  ? 329  GLN C N     1 
ATOM   23059 C  CA    . GLN C 3  329  ? 126.344 134.842 67.590  1.00 31.12  ? 329  GLN C CA    1 
ATOM   23060 C  C     . GLN C 3  329  ? 126.721 136.044 66.739  1.00 35.03  ? 329  GLN C C     1 
ATOM   23061 O  O     . GLN C 3  329  ? 127.004 137.128 67.266  1.00 40.81  ? 329  GLN C O     1 
ATOM   23062 C  CB    . GLN C 3  329  ? 127.548 133.926 67.787  1.00 27.08  ? 329  GLN C CB    1 
ATOM   23063 C  CG    . GLN C 3  329  ? 127.267 132.784 68.723  1.00 31.45  ? 329  GLN C CG    1 
ATOM   23064 C  CD    . GLN C 3  329  ? 128.486 131.961 69.023  1.00 36.62  ? 329  GLN C CD    1 
ATOM   23065 O  OE1   . GLN C 3  329  ? 129.566 132.218 68.499  1.00 37.89  ? 329  GLN C OE1   1 
ATOM   23066 N  NE2   . GLN C 3  329  ? 128.332 130.978 69.895  1.00 35.52  ? 329  GLN C NE2   1 
ATOM   23067 N  N     . GLU C 3  330  ? 126.720 135.876 65.421  1.00 34.45  ? 330  GLU C N     1 
ATOM   23068 C  CA    . GLU C 3  330  ? 127.110 136.962 64.536  1.00 36.70  ? 330  GLU C CA    1 
ATOM   23069 C  C     . GLU C 3  330  ? 126.120 138.119 64.613  1.00 39.19  ? 330  GLU C C     1 
ATOM   23070 O  O     . GLU C 3  330  ? 126.517 139.289 64.671  1.00 41.17  ? 330  GLU C O     1 
ATOM   23071 C  CB    . GLU C 3  330  ? 127.234 136.434 63.109  1.00 37.86  ? 330  GLU C CB    1 
ATOM   23072 C  CG    . GLU C 3  330  ? 128.352 135.416 62.906  1.00 38.82  ? 330  GLU C CG    1 
ATOM   23073 C  CD    . GLU C 3  330  ? 128.045 134.048 63.512  1.00 41.85  ? 330  GLU C CD    1 
ATOM   23074 O  OE1   . GLU C 3  330  ? 128.982 133.384 64.005  1.00 41.32  ? 330  GLU C OE1   1 
ATOM   23075 O  OE2   . GLU C 3  330  ? 126.865 133.641 63.506  1.00 39.70  ? 330  GLU C OE2   1 
ATOM   23076 N  N     . ASP C 3  331  ? 124.821 137.810 64.619  1.00 31.79  ? 331  ASP C N     1 
ATOM   23077 C  CA    . ASP C 3  331  ? 123.806 138.856 64.708  1.00 32.78  ? 331  ASP C CA    1 
ATOM   23078 C  C     . ASP C 3  331  ? 123.868 139.579 66.046  1.00 32.96  ? 331  ASP C C     1 
ATOM   23079 O  O     . ASP C 3  331  ? 123.674 140.803 66.112  1.00 38.84  ? 331  ASP C O     1 
ATOM   23080 C  CB    . ASP C 3  331  ? 122.422 138.259 64.479  1.00 35.25  ? 331  ASP C CB    1 
ATOM   23081 C  CG    . ASP C 3  331  ? 122.367 137.372 63.253  1.00 42.11  ? 331  ASP C CG    1 
ATOM   23082 O  OD1   . ASP C 3  331  ? 123.241 136.491 63.116  1.00 41.33  ? 331  ASP C OD1   1 
ATOM   23083 O  OD2   . ASP C 3  331  ? 121.448 137.549 62.428  1.00 39.16  ? 331  ASP C OD2   1 
ATOM   23084 N  N     . LEU C 3  332  ? 124.138 138.841 67.123  1.00 22.14  ? 332  LEU C N     1 
ATOM   23085 C  CA    . LEU C 3  332  ? 124.290 139.469 68.427  1.00 25.69  ? 332  LEU C CA    1 
ATOM   23086 C  C     . LEU C 3  332  ? 125.475 140.422 68.446  1.00 28.42  ? 332  LEU C C     1 
ATOM   23087 O  O     . LEU C 3  332  ? 125.370 141.543 68.954  1.00 29.69  ? 332  LEU C O     1 
ATOM   23088 C  CB    . LEU C 3  332  ? 124.441 138.404 69.507  1.00 28.26  ? 332  LEU C CB    1 
ATOM   23089 C  CG    . LEU C 3  332  ? 124.503 138.938 70.936  1.00 25.45  ? 332  LEU C CG    1 
ATOM   23090 C  CD1   . LEU C 3  332  ? 123.255 139.732 71.221  1.00 26.05  ? 332  LEU C CD1   1 
ATOM   23091 C  CD2   . LEU C 3  332  ? 124.657 137.811 71.924  1.00 20.27  ? 332  LEU C CD2   1 
ATOM   23092 N  N     . ILE C 3  333  ? 126.609 140.000 67.889  1.00 27.44  ? 333  ILE C N     1 
ATOM   23093 C  CA    . ILE C 3  333  ? 127.773 140.879 67.844  1.00 24.34  ? 333  ILE C CA    1 
ATOM   23094 C  C     . ILE C 3  333  ? 127.486 142.112 66.990  1.00 26.59  ? 333  ILE C C     1 
ATOM   23095 O  O     . ILE C 3  333  ? 127.942 143.218 67.302  1.00 30.24  ? 333  ILE C O     1 
ATOM   23096 C  CB    . ILE C 3  333  ? 128.999 140.100 67.344  1.00 24.47  ? 333  ILE C CB    1 
ATOM   23097 C  CG1   . ILE C 3  333  ? 129.359 138.998 68.332  1.00 23.94  ? 333  ILE C CG1   1 
ATOM   23098 C  CG2   . ILE C 3  333  ? 130.167 141.020 67.156  1.00 28.16  ? 333  ILE C CG2   1 
ATOM   23099 C  CD1   . ILE C 3  333  ? 129.739 139.494 69.688  1.00 27.17  ? 333  ILE C CD1   1 
ATOM   23100 N  N     . THR C 3  334  ? 126.720 141.949 65.910  1.00 24.62  ? 334  THR C N     1 
ATOM   23101 C  CA    . THR C 3  334  ? 126.340 143.096 65.089  1.00 23.91  ? 334  THR C CA    1 
ATOM   23102 C  C     . THR C 3  334  ? 125.540 144.110 65.899  1.00 28.66  ? 334  THR C C     1 
ATOM   23103 O  O     . THR C 3  334  ? 125.804 145.322 65.852  1.00 32.48  ? 334  THR C O     1 
ATOM   23104 C  CB    . THR C 3  334  ? 125.531 142.619 63.882  1.00 26.28  ? 334  THR C CB    1 
ATOM   23105 O  OG1   . THR C 3  334  ? 126.317 141.708 63.108  1.00 32.27  ? 334  THR C OG1   1 
ATOM   23106 C  CG2   . THR C 3  334  ? 125.125 143.788 63.008  1.00 25.90  ? 334  THR C CG2   1 
ATOM   23107 N  N     . LEU C 3  335  ? 124.562 143.624 66.666  1.00 23.63  ? 335  LEU C N     1 
ATOM   23108 C  CA    . LEU C 3  335  ? 123.762 144.513 67.504  1.00 25.84  ? 335  LEU C CA    1 
ATOM   23109 C  C     . LEU C 3  335  ? 124.608 145.199 68.570  1.00 28.35  ? 335  LEU C C     1 
ATOM   23110 O  O     . LEU C 3  335  ? 124.408 146.385 68.868  1.00 34.53  ? 335  LEU C O     1 
ATOM   23111 C  CB    . LEU C 3  335  ? 122.629 143.729 68.151  1.00 30.03  ? 335  LEU C CB    1 
ATOM   23112 C  CG    . LEU C 3  335  ? 121.543 143.257 67.197  1.00 29.25  ? 335  LEU C CG    1 
ATOM   23113 C  CD1   . LEU C 3  335  ? 120.667 142.254 67.895  1.00 25.16  ? 335  LEU C CD1   1 
ATOM   23114 C  CD2   . LEU C 3  335  ? 120.744 144.444 66.721  1.00 24.06  ? 335  LEU C CD2   1 
ATOM   23115 N  N     . LEU C 3  336  ? 125.547 144.464 69.165  1.00 21.49  ? 336  LEU C N     1 
ATOM   23116 C  CA    . LEU C 3  336  ? 126.395 145.042 70.202  1.00 21.27  ? 336  LEU C CA    1 
ATOM   23117 C  C     . LEU C 3  336  ? 127.271 146.151 69.643  1.00 25.65  ? 336  LEU C C     1 
ATOM   23118 O  O     . LEU C 3  336  ? 127.430 147.207 70.271  1.00 32.87  ? 336  LEU C O     1 
ATOM   23119 C  CB    . LEU C 3  336  ? 127.247 143.951 70.837  1.00 23.05  ? 336  LEU C CB    1 
ATOM   23120 C  CG    . LEU C 3  336  ? 126.471 142.875 71.596  1.00 24.13  ? 336  LEU C CG    1 
ATOM   23121 C  CD1   . LEU C 3  336  ? 127.357 142.186 72.601  1.00 27.38  ? 336  LEU C CD1   1 
ATOM   23122 C  CD2   . LEU C 3  336  ? 125.243 143.454 72.279  1.00 22.49  ? 336  LEU C CD2   1 
ATOM   23123 N  N     . GLU C 3  337  ? 127.847 145.935 68.460  1.00 26.28  ? 337  GLU C N     1 
ATOM   23124 C  CA    . GLU C 3  337  ? 128.647 146.990 67.847  1.00 23.55  ? 337  GLU C CA    1 
ATOM   23125 C  C     . GLU C 3  337  ? 127.793 148.209 67.532  1.00 23.96  ? 337  GLU C C     1 
ATOM   23126 O  O     . GLU C 3  337  ? 128.242 149.348 67.697  1.00 27.81  ? 337  GLU C O     1 
ATOM   23127 C  CB    . GLU C 3  337  ? 129.335 146.485 66.579  1.00 25.06  ? 337  GLU C CB    1 
ATOM   23128 C  CG    . GLU C 3  337  ? 130.191 145.215 66.688  1.00 27.54  ? 337  GLU C CG    1 
ATOM   23129 C  CD    . GLU C 3  337  ? 131.250 145.190 67.798  1.00 34.38  ? 337  GLU C CD    1 
ATOM   23130 O  OE1   . GLU C 3  337  ? 131.301 146.078 68.676  1.00 32.53  ? 337  GLU C OE1   1 
ATOM   23131 O  OE2   . GLU C 3  337  ? 132.071 144.250 67.770  1.00 34.00  ? 337  GLU C OE2   1 
ATOM   23132 N  N     . LYS C 3  338  ? 126.559 147.989 67.076  1.00 20.57  ? 338  LYS C N     1 
ATOM   23133 C  CA    . LYS C 3  338  ? 125.667 149.114 66.816  1.00 23.41  ? 338  LYS C CA    1 
ATOM   23134 C  C     . LYS C 3  338  ? 125.407 149.931 68.078  1.00 21.74  ? 338  LYS C C     1 
ATOM   23135 O  O     . LYS C 3  338  ? 125.409 151.170 68.044  1.00 22.58  ? 338  LYS C O     1 
ATOM   23136 C  CB    . LYS C 3  338  ? 124.356 148.605 66.233  1.00 20.98  ? 338  LYS C CB    1 
ATOM   23137 C  CG    . LYS C 3  338  ? 123.750 149.529 65.213  1.00 25.07  ? 338  LYS C CG    1 
ATOM   23138 C  CD    . LYS C 3  338  ? 122.795 148.783 64.312  1.00 27.81  ? 338  LYS C CD    1 
ATOM   23139 C  CE    . LYS C 3  338  ? 123.342 147.432 63.917  1.00 25.71  ? 338  LYS C CE    1 
ATOM   23140 N  NZ    . LYS C 3  338  ? 122.616 146.901 62.740  1.00 25.03  ? 338  LYS C NZ    1 
ATOM   23141 N  N     . SER C 3  339  ? 125.178 149.253 69.202  1.00 20.02  ? 339  SER C N     1 
ATOM   23142 C  CA    . SER C 3  339  ? 124.936 149.957 70.460  1.00 18.85  ? 339  SER C CA    1 
ATOM   23143 C  C     . SER C 3  339  ? 126.153 150.770 70.885  1.00 18.54  ? 339  SER C C     1 
ATOM   23144 O  O     . SER C 3  339  ? 126.033 151.922 71.330  1.00 18.86  ? 339  SER C O     1 
ATOM   23145 C  CB    . SER C 3  339  ? 124.558 148.956 71.544  1.00 16.67  ? 339  SER C CB    1 
ATOM   23146 O  OG    . SER C 3  339  ? 123.509 148.120 71.108  1.00 17.51  ? 339  SER C OG    1 
ATOM   23147 N  N     . ILE C 3  340  ? 127.339 150.183 70.756  1.00 15.74  ? 340  ILE C N     1 
ATOM   23148 C  CA    . ILE C 3  340  ? 128.547 150.889 71.167  1.00 14.80  ? 340  ILE C CA    1 
ATOM   23149 C  C     . ILE C 3  340  ? 128.784 152.109 70.283  1.00 19.61  ? 340  ILE C C     1 
ATOM   23150 O  O     . ILE C 3  340  ? 129.218 153.171 70.757  1.00 24.40  ? 340  ILE C O     1 
ATOM   23151 C  CB    . ILE C 3  340  ? 129.737 149.921 71.165  1.00 14.48  ? 340  ILE C CB    1 
ATOM   23152 C  CG1   . ILE C 3  340  ? 129.756 149.144 72.471  1.00 15.99  ? 340  ILE C CG1   1 
ATOM   23153 C  CG2   . ILE C 3  340  ? 131.036 150.665 70.996  1.00 19.66  ? 340  ILE C CG2   1 
ATOM   23154 C  CD1   . ILE C 3  340  ? 130.959 148.286 72.636  1.00 21.40  ? 340  ILE C CD1   1 
ATOM   23155 N  N     . GLN C 3  341  ? 128.482 151.993 68.990  1.00 16.67  ? 341  GLN C N     1 
ATOM   23156 C  CA    . GLN C 3  341  ? 128.562 153.161 68.123  1.00 15.95  ? 341  GLN C CA    1 
ATOM   23157 C  C     . GLN C 3  341  ? 127.582 154.241 68.550  1.00 17.59  ? 341  GLN C C     1 
ATOM   23158 O  O     . GLN C 3  341  ? 127.892 155.434 68.461  1.00 21.42  ? 341  GLN C O     1 
ATOM   23159 C  CB    . GLN C 3  341  ? 128.327 152.767 66.669  1.00 16.81  ? 341  GLN C CB    1 
ATOM   23160 C  CG    . GLN C 3  341  ? 129.574 152.264 65.987  1.00 18.24  ? 341  GLN C CG    1 
ATOM   23161 C  CD    . GLN C 3  341  ? 130.767 153.165 66.252  1.00 20.81  ? 341  GLN C CD    1 
ATOM   23162 O  OE1   . GLN C 3  341  ? 131.775 152.731 66.801  1.00 24.42  ? 341  GLN C OE1   1 
ATOM   23163 N  NE2   . GLN C 3  341  ? 130.655 154.427 65.863  1.00 19.42  ? 341  GLN C NE2   1 
ATOM   23164 N  N     . ASN C 3  342  ? 126.388 153.852 68.994  1.00 14.01  ? 342  ASN C N     1 
ATOM   23165 C  CA    . ASN C 3  342  ? 125.441 154.855 69.471  1.00 10.51  ? 342  ASN C CA    1 
ATOM   23166 C  C     . ASN C 3  342  ? 125.990 155.614 70.675  1.00 20.40  ? 342  ASN C C     1 
ATOM   23167 O  O     . ASN C 3  342  ? 125.842 156.842 70.769  1.00 20.47  ? 342  ASN C O     1 
ATOM   23168 C  CB    . ASN C 3  342  ? 124.112 154.203 69.810  1.00 13.38  ? 342  ASN C CB    1 
ATOM   23169 C  CG    . ASN C 3  342  ? 123.336 153.821 68.591  1.00 22.27  ? 342  ASN C CG    1 
ATOM   23170 O  OD1   . ASN C 3  342  ? 123.446 154.465 67.555  1.00 22.26  ? 342  ASN C OD1   1 
ATOM   23171 N  ND2   . ASN C 3  342  ? 122.519 152.788 68.708  1.00 21.33  ? 342  ASN C ND2   1 
ATOM   23172 N  N     . ILE C 3  343  ? 126.630 154.902 71.605  1.00 19.10  ? 343  ILE C N     1 
ATOM   23173 C  CA    . ILE C 3  343  ? 127.244 155.574 72.753  1.00 14.57  ? 343  ILE C CA    1 
ATOM   23174 C  C     . ILE C 3  343  ? 128.294 156.579 72.286  1.00 13.52  ? 343  ILE C C     1 
ATOM   23175 O  O     . ILE C 3  343  ? 128.308 157.749 72.711  1.00 21.23  ? 343  ILE C O     1 
ATOM   23176 C  CB    . ILE C 3  343  ? 127.860 154.546 73.717  1.00 12.88  ? 343  ILE C CB    1 
ATOM   23177 C  CG1   . ILE C 3  343  ? 126.814 153.554 74.208  1.00 14.25  ? 343  ILE C CG1   1 
ATOM   23178 C  CG2   . ILE C 3  343  ? 128.501 155.246 74.891  1.00 9.80   ? 343  ILE C CG2   1 
ATOM   23179 C  CD1   . ILE C 3  343  ? 127.376 152.479 75.097  1.00 7.46   ? 343  ILE C CD1   1 
ATOM   23180 N  N     . ILE C 3  344  ? 129.196 156.133 71.410  1.00 14.75  ? 344  ILE C N     1 
ATOM   23181 C  CA    . ILE C 3  344  ? 130.279 157.002 70.956  1.00 13.87  ? 344  ILE C CA    1 
ATOM   23182 C  C     . ILE C 3  344  ? 129.719 158.241 70.273  1.00 15.95  ? 344  ILE C C     1 
ATOM   23183 O  O     . ILE C 3  344  ? 130.200 159.362 70.487  1.00 19.77  ? 344  ILE C O     1 
ATOM   23184 C  CB    . ILE C 3  344  ? 131.237 156.225 70.034  1.00 11.80  ? 344  ILE C CB    1 
ATOM   23185 C  CG1   . ILE C 3  344  ? 132.078 155.253 70.847  1.00 13.58  ? 344  ILE C CG1   1 
ATOM   23186 C  CG2   . ILE C 3  344  ? 132.139 157.159 69.278  1.00 14.21  ? 344  ILE C CG2   1 
ATOM   23187 C  CD1   . ILE C 3  344  ? 132.749 154.213 70.026  1.00 18.46  ? 344  ILE C CD1   1 
ATOM   23188 N  N     . GLN C 3  345  ? 128.691 158.060 69.448  1.00 19.13  ? 345  GLN C N     1 
ATOM   23189 C  CA    . GLN C 3  345  ? 128.085 159.184 68.749  1.00 19.39  ? 345  GLN C CA    1 
ATOM   23190 C  C     . GLN C 3  345  ? 127.462 160.180 69.719  1.00 23.26  ? 345  GLN C C     1 
ATOM   23191 O  O     . GLN C 3  345  ? 127.587 161.397 69.532  1.00 24.41  ? 345  GLN C O     1 
ATOM   23192 C  CB    . GLN C 3  345  ? 127.049 158.660 67.761  1.00 18.49  ? 345  GLN C CB    1 
ATOM   23193 C  CG    . GLN C 3  345  ? 126.129 159.708 67.208  1.00 22.52  ? 345  GLN C CG    1 
ATOM   23194 C  CD    . GLN C 3  345  ? 124.983 159.104 66.441  1.00 28.40  ? 345  GLN C CD    1 
ATOM   23195 O  OE1   . GLN C 3  345  ? 123.937 159.728 66.266  1.00 26.78  ? 345  GLN C OE1   1 
ATOM   23196 N  NE2   . GLN C 3  345  ? 125.169 157.875 65.978  1.00 28.63  ? 345  GLN C NE2   1 
ATOM   23197 N  N     . THR C 3  346  ? 126.786 159.685 70.759  1.00 21.30  ? 346  THR C N     1 
ATOM   23198 C  CA    . THR C 3  346  ? 126.183 160.584 71.740  1.00 17.53  ? 346  THR C CA    1 
ATOM   23199 C  C     . THR C 3  346  ? 127.238 161.455 72.407  1.00 20.44  ? 346  THR C C     1 
ATOM   23200 O  O     . THR C 3  346  ? 127.063 162.673 72.553  1.00 25.14  ? 346  THR C O     1 
ATOM   23201 C  CB    . THR C 3  346  ? 125.407 159.779 72.786  1.00 18.55  ? 346  THR C CB    1 
ATOM   23202 O  OG1   . THR C 3  346  ? 124.165 159.345 72.228  1.00 21.82  ? 346  THR C OG1   1 
ATOM   23203 C  CG2   . THR C 3  346  ? 125.121 160.611 74.016  1.00 16.25  ? 346  THR C CG2   1 
ATOM   23204 N  N     . PHE C 3  347  ? 128.355 160.856 72.802  1.00 14.30  ? 347  PHE C N     1 
ATOM   23205 C  CA    . PHE C 3  347  ? 129.331 161.671 73.518  1.00 14.05  ? 347  PHE C CA    1 
ATOM   23206 C  C     . PHE C 3  347  ? 130.118 162.590 72.588  1.00 16.58  ? 347  PHE C C     1 
ATOM   23207 O  O     . PHE C 3  347  ? 130.541 163.679 73.005  1.00 21.88  ? 347  PHE C O     1 
ATOM   23208 C  CB    . PHE C 3  347  ? 130.236 160.780 74.357  1.00 17.10  ? 347  PHE C CB    1 
ATOM   23209 C  CG    . PHE C 3  347  ? 129.636 160.440 75.684  1.00 15.52  ? 347  PHE C CG    1 
ATOM   23210 C  CD1   . PHE C 3  347  ? 129.677 161.344 76.727  1.00 15.80  ? 347  PHE C CD1   1 
ATOM   23211 C  CD2   . PHE C 3  347  ? 128.973 159.247 75.870  1.00 13.27  ? 347  PHE C CD2   1 
ATOM   23212 C  CE1   . PHE C 3  347  ? 129.102 161.045 77.933  1.00 16.05  ? 347  PHE C CE1   1 
ATOM   23213 C  CE2   . PHE C 3  347  ? 128.395 158.945 77.076  1.00 18.47  ? 347  PHE C CE2   1 
ATOM   23214 C  CZ    . PHE C 3  347  ? 128.457 159.842 78.109  1.00 16.55  ? 347  PHE C CZ    1 
ATOM   23215 N  N     . GLN C 3  348  ? 130.288 162.211 71.322  1.00 20.85  ? 348  GLN C N     1 
ATOM   23216 C  CA    . GLN C 3  348  ? 130.872 163.144 70.364  1.00 19.44  ? 348  GLN C CA    1 
ATOM   23217 C  C     . GLN C 3  348  ? 129.972 164.358 70.151  1.00 19.06  ? 348  GLN C C     1 
ATOM   23218 O  O     . GLN C 3  348  ? 130.455 165.499 70.076  1.00 20.14  ? 348  GLN C O     1 
ATOM   23219 C  CB    . GLN C 3  348  ? 131.152 162.429 69.047  1.00 18.82  ? 348  GLN C CB    1 
ATOM   23220 C  CG    . GLN C 3  348  ? 132.424 161.615 69.090  1.00 19.83  ? 348  GLN C CG    1 
ATOM   23221 C  CD    . GLN C 3  348  ? 132.592 160.705 67.896  1.00 23.15  ? 348  GLN C CD    1 
ATOM   23222 O  OE1   . GLN C 3  348  ? 131.669 160.511 67.107  1.00 23.32  ? 348  GLN C OE1   1 
ATOM   23223 N  NE2   . GLN C 3  348  ? 133.780 160.137 67.759  1.00 18.22  ? 348  GLN C NE2   1 
ATOM   23224 N  N     . ILE C 3  349  ? 128.660 164.136 70.059  1.00 18.83  ? 349  ILE C N     1 
ATOM   23225 C  CA    . ILE C 3  349  ? 127.732 165.259 69.964  1.00 19.09  ? 349  ILE C CA    1 
ATOM   23226 C  C     . ILE C 3  349  ? 127.832 166.140 71.200  1.00 24.71  ? 349  ILE C C     1 
ATOM   23227 O  O     . ILE C 3  349  ? 127.774 167.372 71.106  1.00 28.58  ? 349  ILE C O     1 
ATOM   23228 C  CB    . ILE C 3  349  ? 126.293 164.760 69.749  1.00 21.38  ? 349  ILE C CB    1 
ATOM   23229 C  CG1   . ILE C 3  349  ? 126.102 164.276 68.320  1.00 25.50  ? 349  ILE C CG1   1 
ATOM   23230 C  CG2   . ILE C 3  349  ? 125.295 165.857 70.061  1.00 20.52  ? 349  ILE C CG2   1 
ATOM   23231 C  CD1   . ILE C 3  349  ? 124.743 163.705 68.067  1.00 26.36  ? 349  ILE C CD1   1 
ATOM   23232 N  N     . LEU C 3  350  ? 127.972 165.527 72.378  1.00 22.65  ? 350  LEU C N     1 
ATOM   23233 C  CA    . LEU C 3  350  ? 128.110 166.310 73.604  1.00 17.75  ? 350  LEU C CA    1 
ATOM   23234 C  C     . LEU C 3  350  ? 129.323 167.230 73.540  1.00 21.51  ? 350  LEU C C     1 
ATOM   23235 O  O     . LEU C 3  350  ? 129.246 168.406 73.913  1.00 27.52  ? 350  LEU C O     1 
ATOM   23236 C  CB    . LEU C 3  350  ? 128.216 165.387 74.814  1.00 21.58  ? 350  LEU C CB    1 
ATOM   23237 C  CG    . LEU C 3  350  ? 126.939 165.033 75.569  1.00 23.10  ? 350  LEU C CG    1 
ATOM   23238 C  CD1   . LEU C 3  350  ? 127.273 164.224 76.795  1.00 22.26  ? 350  LEU C CD1   1 
ATOM   23239 C  CD2   . LEU C 3  350  ? 126.163 166.267 75.932  1.00 23.47  ? 350  LEU C CD2   1 
ATOM   23240 N  N     . GLU C 3  351  ? 130.457 166.711 73.078  1.00 23.56  ? 351  GLU C N     1 
ATOM   23241 C  CA    . GLU C 3  351  ? 131.664 167.535 73.024  1.00 22.13  ? 351  GLU C CA    1 
ATOM   23242 C  C     . GLU C 3  351  ? 131.536 168.669 72.006  1.00 25.11  ? 351  GLU C C     1 
ATOM   23243 O  O     . GLU C 3  351  ? 131.970 169.805 72.260  1.00 29.35  ? 351  GLU C O     1 
ATOM   23244 C  CB    . GLU C 3  351  ? 132.865 166.645 72.737  1.00 23.02  ? 351  GLU C CB    1 
ATOM   23245 C  CG    . GLU C 3  351  ? 134.166 167.363 72.548  1.00 24.00  ? 351  GLU C CG    1 
ATOM   23246 C  CD    . GLU C 3  351  ? 135.324 166.403 72.430  1.00 30.73  ? 351  GLU C CD    1 
ATOM   23247 O  OE1   . GLU C 3  351  ? 135.077 165.187 72.308  1.00 31.65  ? 351  GLU C OE1   1 
ATOM   23248 O  OE2   . GLU C 3  351  ? 136.483 166.861 72.458  1.00 29.03  ? 351  GLU C OE2   1 
ATOM   23249 N  N     . LYS C 3  352  ? 130.924 168.392 70.856  1.00 27.75  ? 352  LYS C N     1 
ATOM   23250 C  CA    . LYS C 3  352  ? 130.691 169.454 69.881  1.00 25.77  ? 352  LYS C CA    1 
ATOM   23251 C  C     . LYS C 3  352  ? 129.773 170.540 70.446  1.00 31.35  ? 352  LYS C C     1 
ATOM   23252 O  O     . LYS C 3  352  ? 130.003 171.744 70.242  1.00 33.60  ? 352  LYS C O     1 
ATOM   23253 C  CB    . LYS C 3  352  ? 130.125 168.832 68.609  1.00 27.47  ? 352  LYS C CB    1 
ATOM   23254 C  CG    . LYS C 3  352  ? 130.048 169.738 67.416  1.00 28.98  ? 352  LYS C CG    1 
ATOM   23255 C  CD    . LYS C 3  352  ? 128.601 169.963 67.053  1.00 32.63  ? 352  LYS C CD    1 
ATOM   23256 C  CE    . LYS C 3  352  ? 127.813 168.662 67.088  1.00 34.03  ? 352  LYS C CE    1 
ATOM   23257 N  NZ    . LYS C 3  352  ? 126.339 168.886 67.148  1.00 33.70  ? 352  LYS C NZ    1 
ATOM   23258 N  N     . ASN C 3  353  ? 128.740 170.138 71.183  1.00 29.12  ? 353  ASN C N     1 
ATOM   23259 C  CA    . ASN C 3  353  ? 127.872 171.114 71.828  1.00 25.56  ? 353  ASN C CA    1 
ATOM   23260 C  C     . ASN C 3  353  ? 128.611 171.928 72.882  1.00 29.00  ? 353  ASN C C     1 
ATOM   23261 O  O     . ASN C 3  353  ? 128.326 173.118 73.050  1.00 31.41  ? 353  ASN C O     1 
ATOM   23262 C  CB    . ASN C 3  353  ? 126.672 170.411 72.452  1.00 24.76  ? 353  ASN C CB    1 
ATOM   23263 C  CG    . ASN C 3  353  ? 125.642 170.028 71.435  1.00 30.84  ? 353  ASN C CG    1 
ATOM   23264 O  OD1   . ASN C 3  353  ? 124.831 169.142 71.664  1.00 34.06  ? 353  ASN C OD1   1 
ATOM   23265 N  ND2   . ASN C 3  353  ? 125.672 170.688 70.291  1.00 35.03  ? 353  ASN C ND2   1 
ATOM   23266 N  N     . VAL C 3  354  ? 129.534 171.303 73.619  1.00 24.42  ? 354  VAL C N     1 
ATOM   23267 C  CA    . VAL C 3  354  ? 130.342 172.054 74.580  1.00 21.84  ? 354  VAL C CA    1 
ATOM   23268 C  C     . VAL C 3  354  ? 131.102 173.156 73.862  1.00 27.39  ? 354  VAL C C     1 
ATOM   23269 O  O     . VAL C 3  354  ? 131.125 174.310 74.303  1.00 31.76  ? 354  VAL C O     1 
ATOM   23270 C  CB    . VAL C 3  354  ? 131.305 171.124 75.339  1.00 20.64  ? 354  VAL C CB    1 
ATOM   23271 C  CG1   . VAL C 3  354  ? 132.366 171.942 76.038  1.00 21.00  ? 354  VAL C CG1   1 
ATOM   23272 C  CG2   . VAL C 3  354  ? 130.570 170.289 76.345  1.00 22.12  ? 354  VAL C CG2   1 
ATOM   23273 N  N     . ASP C 3  355  ? 131.716 172.817 72.725  1.00 30.54  ? 355  ASP C N     1 
ATOM   23274 C  CA    . ASP C 3  355  ? 132.403 173.836 71.931  1.00 29.28  ? 355  ASP C CA    1 
ATOM   23275 C  C     . ASP C 3  355  ? 131.475 174.975 71.529  1.00 29.37  ? 355  ASP C C     1 
ATOM   23276 O  O     . ASP C 3  355  ? 131.876 176.141 71.567  1.00 31.70  ? 355  ASP C O     1 
ATOM   23277 C  CB    . ASP C 3  355  ? 133.016 173.217 70.679  1.00 34.29  ? 355  ASP C CB    1 
ATOM   23278 C  CG    . ASP C 3  355  ? 134.503 173.037 70.799  1.00 37.72  ? 355  ASP C CG    1 
ATOM   23279 O  OD1   . ASP C 3  355  ? 135.028 172.047 70.249  1.00 34.93  ? 355  ASP C OD1   1 
ATOM   23280 O  OD2   . ASP C 3  355  ? 135.149 173.879 71.455  1.00 36.95  ? 355  ASP C OD2   1 
ATOM   23281 N  N     . GLU C 3  356  ? 130.244 174.663 71.127  1.00 31.17  ? 356  GLU C N     1 
ATOM   23282 C  CA    . GLU C 3  356  ? 129.323 175.725 70.712  1.00 32.51  ? 356  GLU C CA    1 
ATOM   23283 C  C     . GLU C 3  356  ? 128.829 176.604 71.861  1.00 32.09  ? 356  GLU C C     1 
ATOM   23284 O  O     . GLU C 3  356  ? 128.626 177.804 71.664  1.00 32.31  ? 356  GLU C O     1 
ATOM   23285 C  CB    . GLU C 3  356  ? 128.118 175.129 69.991  1.00 33.83  ? 356  GLU C CB    1 
ATOM   23286 C  CG    . GLU C 3  356  ? 128.443 174.519 68.658  1.00 35.10  ? 356  GLU C CG    1 
ATOM   23287 C  CD    . GLU C 3  356  ? 127.384 173.550 68.197  1.00 38.25  ? 356  GLU C CD    1 
ATOM   23288 O  OE1   . GLU C 3  356  ? 127.632 172.836 67.211  1.00 38.25  ? 356  GLU C OE1   1 
ATOM   23289 O  OE2   . GLU C 3  356  ? 126.321 173.472 68.841  1.00 37.67  ? 356  GLU C OE2   1 
ATOM   23290 N  N     . LEU C 3  357  ? 128.613 176.048 73.050  1.00 29.78  ? 357  LEU C N     1 
ATOM   23291 C  CA    . LEU C 3  357  ? 127.901 176.772 74.102  1.00 29.78  ? 357  LEU C CA    1 
ATOM   23292 C  C     . LEU C 3  357  ? 128.795 177.715 74.902  1.00 29.99  ? 357  LEU C C     1 
ATOM   23293 O  O     . LEU C 3  357  ? 128.445 178.876 75.124  1.00 27.94  ? 357  LEU C O     1 
ATOM   23294 C  CB    . LEU C 3  357  ? 127.236 175.784 75.060  1.00 31.21  ? 357  LEU C CB    1 
ATOM   23295 C  CG    . LEU C 3  357  ? 125.742 175.568 74.931  1.00 26.63  ? 357  LEU C CG    1 
ATOM   23296 C  CD1   . LEU C 3  357  ? 125.305 174.728 76.080  1.00 25.54  ? 357  LEU C CD1   1 
ATOM   23297 C  CD2   . LEU C 3  357  ? 125.003 176.881 74.915  1.00 28.05  ? 357  LEU C CD2   1 
ATOM   23298 N  N     . ILE C 3  358  ? 129.919 177.209 75.394  1.00 24.50  ? 358  ILE C N     1 
ATOM   23299 C  CA    . ILE C 3  358  ? 130.758 177.960 76.318  1.00 26.52  ? 358  ILE C CA    1 
ATOM   23300 C  C     . ILE C 3  358  ? 131.666 178.877 75.509  1.00 29.07  ? 358  ILE C C     1 
ATOM   23301 O  O     . ILE C 3  358  ? 132.545 178.416 74.779  1.00 27.92  ? 358  ILE C O     1 
ATOM   23302 C  CB    . ILE C 3  358  ? 131.563 177.023 77.223  1.00 26.79  ? 358  ILE C CB    1 
ATOM   23303 C  CG1   . ILE C 3  358  ? 130.603 176.205 78.086  1.00 26.59  ? 358  ILE C CG1   1 
ATOM   23304 C  CG2   . ILE C 3  358  ? 132.518 177.806 78.087  1.00 21.36  ? 358  ILE C CG2   1 
ATOM   23305 C  CD1   . ILE C 3  358  ? 131.254 175.096 78.834  1.00 23.96  ? 358  ILE C CD1   1 
ATOM   23306 N  N     . ALA C 3  359  ? 131.456 180.180 75.646  1.00 36.60  ? 359  ALA C N     1 
ATOM   23307 C  CA    . ALA C 3  359  ? 132.211 181.169 74.898  1.00 37.95  ? 359  ALA C CA    1 
ATOM   23308 C  C     . ALA C 3  359  ? 133.569 181.429 75.537  1.00 38.31  ? 359  ALA C C     1 
ATOM   23309 O  O     . ALA C 3  359  ? 134.152 182.498 75.361  1.00 38.12  ? 359  ALA C O     1 
ATOM   23310 C  CB    . ALA C 3  359  ? 131.420 182.458 74.794  1.00 35.59  ? 359  ALA C CB    1 
ATOM   23311 N  N     . MET D 4  1    ? 94.691  104.993 158.121 1.00 44.30  ? 1    MET D N     1 
ATOM   23312 C  CA    . MET D 4  1    ? 93.784  104.381 157.163 1.00 44.10  ? 1    MET D CA    1 
ATOM   23313 C  C     . MET D 4  1    ? 94.484  103.159 156.585 1.00 43.67  ? 1    MET D C     1 
ATOM   23314 O  O     . MET D 4  1    ? 93.891  102.360 155.868 1.00 43.39  ? 1    MET D O     1 
ATOM   23315 C  CB    . MET D 4  1    ? 93.407  105.384 156.066 1.00 43.84  ? 1    MET D CB    1 
ATOM   23316 C  CG    . MET D 4  1    ? 92.442  104.878 154.997 1.00 44.27  ? 1    MET D CG    1 
ATOM   23317 S  SD    . MET D 4  1    ? 91.220  103.725 155.641 1.00 59.14  ? 1    MET D SD    1 
ATOM   23318 C  CE    . MET D 4  1    ? 89.945  103.811 154.390 1.00 46.03  ? 1    MET D CE    1 
ATOM   23319 N  N     . ALA D 4  2    ? 95.759  103.005 156.943 1.00 37.05  ? 2    ALA D N     1 
ATOM   23320 C  CA    . ALA D 4  2    ? 96.587  101.986 156.310 1.00 37.28  ? 2    ALA D CA    1 
ATOM   23321 C  C     . ALA D 4  2    ? 96.027  100.589 156.533 1.00 38.45  ? 2    ALA D C     1 
ATOM   23322 O  O     . ALA D 4  2    ? 96.130  99.727  155.655 1.00 39.70  ? 2    ALA D O     1 
ATOM   23323 C  CB    . ALA D 4  2    ? 98.020  102.080 156.827 1.00 33.73  ? 2    ALA D CB    1 
ATOM   23324 N  N     . MET D 4  3    ? 95.428  100.342 157.696 1.00 41.31  ? 3    MET D N     1 
ATOM   23325 C  CA    . MET D 4  3    ? 94.933  99.002  157.990 1.00 41.23  ? 3    MET D CA    1 
ATOM   23326 C  C     . MET D 4  3    ? 93.713  98.655  157.144 1.00 40.49  ? 3    MET D C     1 
ATOM   23327 O  O     . MET D 4  3    ? 93.601  97.532  156.640 1.00 41.69  ? 3    MET D O     1 
ATOM   23328 C  CB    . MET D 4  3    ? 94.626  98.878  159.477 1.00 41.94  ? 3    MET D CB    1 
ATOM   23329 C  CG    . MET D 4  3    ? 95.759  98.251  160.262 1.00 42.71  ? 3    MET D CG    1 
ATOM   23330 S  SD    . MET D 4  3    ? 96.325  96.712  159.521 1.00 51.32  ? 3    MET D SD    1 
ATOM   23331 C  CE    . MET D 4  3    ? 97.932  96.528  160.282 1.00 40.86  ? 3    MET D CE    1 
ATOM   23332 N  N     . GLN D 4  4    ? 92.794  99.600  156.962 1.00 36.78  ? 4    GLN D N     1 
ATOM   23333 C  CA    . GLN D 4  4    ? 91.634  99.322  156.122 1.00 38.93  ? 4    GLN D CA    1 
ATOM   23334 C  C     . GLN D 4  4    ? 92.029  99.167  154.658 1.00 38.33  ? 4    GLN D C     1 
ATOM   23335 O  O     . GLN D 4  4    ? 91.486  98.310  153.953 1.00 37.47  ? 4    GLN D O     1 
ATOM   23336 C  CB    . GLN D 4  4    ? 90.583  100.421 156.290 1.00 40.84  ? 4    GLN D CB    1 
ATOM   23337 C  CG    . GLN D 4  4    ? 89.266  100.305 155.472 1.00 41.11  ? 4    GLN D CG    1 
ATOM   23338 C  CD    . GLN D 4  4    ? 88.588  98.923  155.442 1.00 41.81  ? 4    GLN D CD    1 
ATOM   23339 O  OE1   . GLN D 4  4    ? 89.229  97.874  155.428 1.00 41.44  ? 4    GLN D OE1   1 
ATOM   23340 N  NE2   . GLN D 4  4    ? 87.263  98.938  155.435 1.00 40.34  ? 4    GLN D NE2   1 
ATOM   23341 N  N     . LYS D 4  5    ? 92.965  99.989  154.178 1.00 36.87  ? 5    LYS D N     1 
ATOM   23342 C  CA    . LYS D 4  5    ? 93.446  99.834  152.807 1.00 34.23  ? 5    LYS D CA    1 
ATOM   23343 C  C     . LYS D 4  5    ? 94.148  98.495  152.617 1.00 32.55  ? 5    LYS D C     1 
ATOM   23344 O  O     . LYS D 4  5    ? 93.962  97.829  151.590 1.00 34.15  ? 5    LYS D O     1 
ATOM   23345 C  CB    . LYS D 4  5    ? 94.376  100.987 152.445 1.00 31.68  ? 5    LYS D CB    1 
ATOM   23346 C  CG    . LYS D 4  5    ? 93.703  102.339 152.406 1.00 32.22  ? 5    LYS D CG    1 
ATOM   23347 C  CD    . LYS D 4  5    ? 92.601  102.358 151.380 1.00 31.80  ? 5    LYS D CD    1 
ATOM   23348 C  CE    . LYS D 4  5    ? 91.919  103.704 151.329 1.00 34.94  ? 5    LYS D CE    1 
ATOM   23349 N  NZ    . LYS D 4  5    ? 90.798  103.702 150.361 1.00 33.46  ? 5    LYS D NZ    1 
ATOM   23350 N  N     . LEU D 4  6    ? 94.957  98.091  153.597 1.00 28.72  ? 6    LEU D N     1 
ATOM   23351 C  CA    . LEU D 4  6    ? 95.585  96.779  153.556 1.00 29.45  ? 6    LEU D CA    1 
ATOM   23352 C  C     . LEU D 4  6    ? 94.541  95.681  153.478 1.00 33.38  ? 6    LEU D C     1 
ATOM   23353 O  O     . LEU D 4  6    ? 94.667  94.751  152.679 1.00 37.37  ? 6    LEU D O     1 
ATOM   23354 C  CB    . LEU D 4  6    ? 96.464  96.570  154.784 1.00 29.18  ? 6    LEU D CB    1 
ATOM   23355 C  CG    . LEU D 4  6    ? 97.939  96.941  154.728 1.00 30.74  ? 6    LEU D CG    1 
ATOM   23356 C  CD1   . LEU D 4  6    ? 98.532  96.901  156.118 1.00 29.66  ? 6    LEU D CD1   1 
ATOM   23357 C  CD2   . LEU D 4  6    ? 98.664  95.987  153.821 1.00 34.59  ? 6    LEU D CD2   1 
ATOM   23358 N  N     . PHE D 4  7    ? 93.487  95.784  154.288 1.00 36.93  ? 7    PHE D N     1 
ATOM   23359 C  CA    . PHE D 4  7    ? 92.511  94.706  154.369 1.00 34.87  ? 7    PHE D CA    1 
ATOM   23360 C  C     . PHE D 4  7    ? 91.851  94.397  153.031 1.00 34.61  ? 7    PHE D C     1 
ATOM   23361 O  O     . PHE D 4  7    ? 91.389  93.272  152.834 1.00 36.57  ? 7    PHE D O     1 
ATOM   23362 C  CB    . PHE D 4  7    ? 91.436  95.043  155.401 1.00 39.23  ? 7    PHE D CB    1 
ATOM   23363 C  CG    . PHE D 4  7    ? 90.441  93.944  155.609 1.00 39.58  ? 7    PHE D CG    1 
ATOM   23364 C  CD1   . PHE D 4  7    ? 90.792  92.797  156.290 1.00 39.05  ? 7    PHE D CD1   1 
ATOM   23365 C  CD2   . PHE D 4  7    ? 89.169  94.041  155.085 1.00 37.35  ? 7    PHE D CD2   1 
ATOM   23366 C  CE1   . PHE D 4  7    ? 89.885  91.784  156.463 1.00 38.29  ? 7    PHE D CE1   1 
ATOM   23367 C  CE2   . PHE D 4  7    ? 88.262  93.027  155.256 1.00 38.50  ? 7    PHE D CE2   1 
ATOM   23368 C  CZ    . PHE D 4  7    ? 88.621  91.899  155.945 1.00 37.55  ? 7    PHE D CZ    1 
ATOM   23369 N  N     . THR D 4  8    ? 91.796  95.348  152.105 1.00 29.64  ? 8    THR D N     1 
ATOM   23370 C  CA    . THR D 4  8    ? 91.231  95.086  150.787 1.00 30.06  ? 8    THR D CA    1 
ATOM   23371 C  C     . THR D 4  8    ? 92.304  94.751  149.760 1.00 31.92  ? 8    THR D C     1 
ATOM   23372 O  O     . THR D 4  8    ? 92.186  93.784  148.984 1.00 35.00  ? 8    THR D O     1 
ATOM   23373 C  CB    . THR D 4  8    ? 90.424  96.300  150.306 1.00 32.78  ? 8    THR D CB    1 
ATOM   23374 O  OG1   . THR D 4  8    ? 91.067  97.503  150.735 1.00 30.98  ? 8    THR D OG1   1 
ATOM   23375 C  CG2   . THR D 4  8    ? 89.020  96.267  150.869 1.00 33.29  ? 8    THR D CG2   1 
ATOM   23376 N  N     . TYR D 4  9    ? 93.380  95.526  149.755 1.00 31.80  ? 9    TYR D N     1 
ATOM   23377 C  CA    . TYR D 4  9    ? 94.342  95.356  148.689 1.00 28.84  ? 9    TYR D CA    1 
ATOM   23378 C  C     . TYR D 4  9    ? 95.273  94.176  148.915 1.00 25.09  ? 9    TYR D C     1 
ATOM   23379 O  O     . TYR D 4  9    ? 95.919  93.746  147.964 1.00 28.62  ? 9    TYR D O     1 
ATOM   23380 C  CB    . TYR D 4  9    ? 95.107  96.657  148.492 1.00 23.83  ? 9    TYR D CB    1 
ATOM   23381 C  CG    . TYR D 4  9    ? 94.198  97.765  148.031 1.00 25.36  ? 9    TYR D CG    1 
ATOM   23382 C  CD1   . TYR D 4  9    ? 93.355  97.581  146.951 1.00 24.77  ? 9    TYR D CD1   1 
ATOM   23383 C  CD2   . TYR D 4  9    ? 94.170  98.986  148.674 1.00 26.24  ? 9    TYR D CD2   1 
ATOM   23384 C  CE1   . TYR D 4  9    ? 92.515  98.579  146.521 1.00 23.47  ? 9    TYR D CE1   1 
ATOM   23385 C  CE2   . TYR D 4  9    ? 93.333  99.995  148.247 1.00 25.94  ? 9    TYR D CE2   1 
ATOM   23386 C  CZ    . TYR D 4  9    ? 92.509  99.784  147.174 1.00 24.70  ? 9    TYR D CZ    1 
ATOM   23387 O  OH    . TYR D 4  9    ? 91.679  100.792 146.750 1.00 24.18  ? 9    TYR D OH    1 
ATOM   23388 N  N     . ILE D 4  10   ? 95.323  93.595  150.114 1.00 23.83  ? 10   ILE D N     1 
ATOM   23389 C  CA    . ILE D 4  10   ? 96.129  92.391  150.281 1.00 26.31  ? 10   ILE D CA    1 
ATOM   23390 C  C     . ILE D 4  10   ? 95.469  91.200  149.589 1.00 27.72  ? 10   ILE D C     1 
ATOM   23391 O  O     . ILE D 4  10   ? 96.141  90.389  148.943 1.00 30.45  ? 10   ILE D O     1 
ATOM   23392 C  CB    . ILE D 4  10   ? 96.415  92.124  151.771 1.00 27.46  ? 10   ILE D CB    1 
ATOM   23393 C  CG1   . ILE D 4  10   ? 97.519  91.083  151.912 1.00 26.13  ? 10   ILE D CG1   1 
ATOM   23394 C  CG2   . ILE D 4  10   ? 95.176  91.680  152.515 1.00 33.22  ? 10   ILE D CG2   1 
ATOM   23395 C  CD1   . ILE D 4  10   ? 98.789  91.466  151.224 1.00 27.94  ? 10   ILE D CD1   1 
ATOM   23396 N  N     . TYR D 4  11   ? 94.149  91.085  149.679 1.00 29.66  ? 11   TYR D N     1 
ATOM   23397 C  CA    . TYR D 4  11   ? 93.482  90.037  148.923 1.00 31.98  ? 11   TYR D CA    1 
ATOM   23398 C  C     . TYR D 4  11   ? 93.424  90.362  147.442 1.00 34.41  ? 11   TYR D C     1 
ATOM   23399 O  O     . TYR D 4  11   ? 93.437  89.444  146.615 1.00 38.99  ? 11   TYR D O     1 
ATOM   23400 C  CB    . TYR D 4  11   ? 92.088  89.774  149.486 1.00 33.87  ? 11   TYR D CB    1 
ATOM   23401 C  CG    . TYR D 4  11   ? 92.097  89.501  150.967 1.00 34.12  ? 11   TYR D CG    1 
ATOM   23402 C  CD1   . TYR D 4  11   ? 92.418  88.247  151.457 1.00 35.93  ? 11   TYR D CD1   1 
ATOM   23403 C  CD2   . TYR D 4  11   ? 91.821  90.499  151.872 1.00 34.58  ? 11   TYR D CD2   1 
ATOM   23404 C  CE1   . TYR D 4  11   ? 92.437  87.995  152.807 1.00 36.89  ? 11   TYR D CE1   1 
ATOM   23405 C  CE2   . TYR D 4  11   ? 91.844  90.258  153.222 1.00 36.44  ? 11   TYR D CE2   1 
ATOM   23406 C  CZ    . TYR D 4  11   ? 92.154  89.009  153.686 1.00 36.88  ? 11   TYR D CZ    1 
ATOM   23407 O  OH    . TYR D 4  11   ? 92.170  88.779  155.040 1.00 39.41  ? 11   TYR D OH    1 
ATOM   23408 N  N     . GLU D 4  12   ? 93.404  91.644  147.073 1.00 27.66  ? 12   GLU D N     1 
ATOM   23409 C  CA    . GLU D 4  12   ? 93.567  91.946  145.652 1.00 26.97  ? 12   GLU D CA    1 
ATOM   23410 C  C     . GLU D 4  12   ? 94.960  91.558  145.147 1.00 25.39  ? 12   GLU D C     1 
ATOM   23411 O  O     . GLU D 4  12   ? 95.106  91.080  144.019 1.00 26.31  ? 12   GLU D O     1 
ATOM   23412 C  CB    . GLU D 4  12   ? 93.266  93.413  145.380 1.00 25.52  ? 12   GLU D CB    1 
ATOM   23413 C  CG    . GLU D 4  12   ? 92.003  93.564  144.577 1.00 25.77  ? 12   GLU D CG    1 
ATOM   23414 C  CD    . GLU D 4  12   ? 91.334  94.890  144.771 1.00 30.97  ? 12   GLU D CD    1 
ATOM   23415 O  OE1   . GLU D 4  12   ? 90.090  94.940  144.723 1.00 32.24  ? 12   GLU D OE1   1 
ATOM   23416 O  OE2   . GLU D 4  12   ? 92.049  95.890  144.949 1.00 31.84  ? 12   GLU D OE2   1 
ATOM   23417 N  N     . PHE D 4  13   ? 95.990  91.745  145.974 1.00 24.81  ? 13   PHE D N     1 
ATOM   23418 C  CA    . PHE D 4  13   ? 97.342  91.309  145.637 1.00 18.71  ? 13   PHE D CA    1 
ATOM   23419 C  C     . PHE D 4  13   ? 97.419  89.798  145.498 1.00 20.38  ? 13   PHE D C     1 
ATOM   23420 O  O     . PHE D 4  13   ? 98.086  89.287  144.595 1.00 24.18  ? 13   PHE D O     1 
ATOM   23421 C  CB    . PHE D 4  13   ? 98.316  91.802  146.709 1.00 20.60  ? 13   PHE D CB    1 
ATOM   23422 C  CG    . PHE D 4  13   ? 99.630  91.073  146.738 1.00 22.95  ? 13   PHE D CG    1 
ATOM   23423 C  CD1   . PHE D 4  13   ? 100.649 91.420  145.872 1.00 24.47  ? 13   PHE D CD1   1 
ATOM   23424 C  CD2   . PHE D 4  13   ? 99.857  90.055  147.646 1.00 22.22  ? 13   PHE D CD2   1 
ATOM   23425 C  CE1   . PHE D 4  13   ? 101.855 90.763  145.903 1.00 21.82  ? 13   PHE D CE1   1 
ATOM   23426 C  CE2   . PHE D 4  13   ? 101.059 89.394  147.676 1.00 20.72  ? 13   PHE D CE2   1 
ATOM   23427 C  CZ    . PHE D 4  13   ? 102.059 89.750  146.805 1.00 21.96  ? 13   PHE D CZ    1 
ATOM   23428 N  N     . ILE D 4  14   ? 96.764  89.069  146.397 1.00 26.69  ? 14   ILE D N     1 
ATOM   23429 C  CA    . ILE D 4  14   ? 96.758  87.611  146.312 1.00 26.35  ? 14   ILE D CA    1 
ATOM   23430 C  C     . ILE D 4  14   ? 96.051  87.148  145.046 1.00 24.55  ? 14   ILE D C     1 
ATOM   23431 O  O     . ILE D 4  14   ? 96.507  86.217  144.374 1.00 27.78  ? 14   ILE D O     1 
ATOM   23432 C  CB    . ILE D 4  14   ? 96.127  87.006  147.578 1.00 25.78  ? 14   ILE D CB    1 
ATOM   23433 C  CG1   . ILE D 4  14   ? 97.115  87.086  148.733 1.00 23.94  ? 14   ILE D CG1   1 
ATOM   23434 C  CG2   . ILE D 4  14   ? 95.714  85.568  147.342 1.00 27.76  ? 14   ILE D CG2   1 
ATOM   23435 C  CD1   . ILE D 4  14   ? 96.477  86.944  150.063 1.00 29.72  ? 14   ILE D CD1   1 
ATOM   23436 N  N     . GLU D 4  15   ? 94.924  87.772  144.703 1.00 24.93  ? 15   GLU D N     1 
ATOM   23437 C  CA    . GLU D 4  15   ? 94.252  87.404  143.459 1.00 28.55  ? 15   GLU D CA    1 
ATOM   23438 C  C     . GLU D 4  15   ? 95.112  87.724  142.240 1.00 32.64  ? 15   GLU D C     1 
ATOM   23439 O  O     . GLU D 4  15   ? 95.172  86.932  141.294 1.00 32.40  ? 15   GLU D O     1 
ATOM   23440 C  CB    . GLU D 4  15   ? 92.900  88.104  143.356 1.00 26.09  ? 15   GLU D CB    1 
ATOM   23441 C  CG    . GLU D 4  15   ? 92.363  88.170  141.942 1.00 32.20  ? 15   GLU D CG    1 
ATOM   23442 C  CD    . GLU D 4  15   ? 90.904  87.770  141.833 1.00 37.46  ? 15   GLU D CD    1 
ATOM   23443 O  OE1   . GLU D 4  15   ? 90.083  88.245  142.645 1.00 37.89  ? 15   GLU D OE1   1 
ATOM   23444 O  OE2   . GLU D 4  15   ? 90.575  86.978  140.925 1.00 33.98  ? 15   GLU D OE2   1 
ATOM   23445 N  N     . TYR D 4  16   ? 95.790  88.874  142.245 1.00 26.61  ? 16   TYR D N     1 
ATOM   23446 C  CA    . TYR D 4  16   ? 96.584  89.270  141.088 1.00 23.16  ? 16   TYR D CA    1 
ATOM   23447 C  C     . TYR D 4  16   ? 97.745  88.320  140.840 1.00 25.70  ? 16   TYR D C     1 
ATOM   23448 O  O     . TYR D 4  16   ? 98.223  88.213  139.706 1.00 25.96  ? 16   TYR D O     1 
ATOM   23449 C  CB    . TYR D 4  16   ? 97.106  90.690  141.271 1.00 25.10  ? 16   TYR D CB    1 
ATOM   23450 C  CG    . TYR D 4  16   ? 97.931  91.193  140.116 1.00 23.06  ? 16   TYR D CG    1 
ATOM   23451 C  CD1   . TYR D 4  16   ? 97.332  91.619  138.949 1.00 24.62  ? 16   TYR D CD1   1 
ATOM   23452 C  CD2   . TYR D 4  16   ? 99.312  91.231  140.192 1.00 21.48  ? 16   TYR D CD2   1 
ATOM   23453 C  CE1   . TYR D 4  16   ? 98.082  92.078  137.896 1.00 25.65  ? 16   TYR D CE1   1 
ATOM   23454 C  CE2   . TYR D 4  16   ? 100.070 91.685  139.144 1.00 20.38  ? 16   TYR D CE2   1 
ATOM   23455 C  CZ    . TYR D 4  16   ? 99.450  92.108  138.000 1.00 24.85  ? 16   TYR D CZ    1 
ATOM   23456 O  OH    . TYR D 4  16   ? 100.203 92.561  136.951 1.00 29.58  ? 16   TYR D OH    1 
ATOM   23457 N  N     . ARG D 4  17   ? 98.209  87.624  141.872 1.00 26.32  ? 17   ARG D N     1 
ATOM   23458 C  CA    . ARG D 4  17   ? 99.327  86.703  141.752 1.00 24.24  ? 17   ARG D CA    1 
ATOM   23459 C  C     . ARG D 4  17   ? 98.890  85.284  141.422 1.00 27.20  ? 17   ARG D C     1 
ATOM   23460 O  O     . ARG D 4  17   ? 99.724  84.378  141.447 1.00 32.49  ? 17   ARG D O     1 
ATOM   23461 C  CB    . ARG D 4  17   ? 100.150 86.701  143.036 1.00 21.42  ? 17   ARG D CB    1 
ATOM   23462 C  CG    . ARG D 4  17   ? 101.432 87.490  142.940 1.00 20.15  ? 17   ARG D CG    1 
ATOM   23463 C  CD    . ARG D 4  17   ? 102.543 86.789  143.669 1.00 24.77  ? 17   ARG D CD    1 
ATOM   23464 N  NE    . ARG D 4  17   ? 103.538 87.715  144.184 1.00 24.24  ? 17   ARG D NE    1 
ATOM   23465 C  CZ    . ARG D 4  17   ? 104.521 87.371  145.000 1.00 24.14  ? 17   ARG D CZ    1 
ATOM   23466 N  NH1   . ARG D 4  17   ? 104.689 86.121  145.388 1.00 22.81  ? 17   ARG D NH1   1 
ATOM   23467 N  NH2   . ARG D 4  17   ? 105.354 88.306  145.441 1.00 23.75  ? 17   ARG D NH2   1 
ATOM   23468 N  N     . LYS D 4  18   ? 97.607  85.076  141.122 1.00 30.48  ? 18   LYS D N     1 
ATOM   23469 C  CA    . LYS D 4  18   ? 97.066  83.766  140.761 1.00 33.34  ? 18   LYS D CA    1 
ATOM   23470 C  C     . LYS D 4  18   ? 97.237  82.761  141.901 1.00 38.62  ? 18   LYS D C     1 
ATOM   23471 O  O     . LYS D 4  18   ? 97.825  81.692  141.737 1.00 39.55  ? 18   LYS D O     1 
ATOM   23472 C  CB    . LYS D 4  18   ? 97.700  83.239  139.474 1.00 33.93  ? 18   LYS D CB    1 
ATOM   23473 C  CG    . LYS D 4  18   ? 97.011  83.664  138.198 1.00 37.02  ? 18   LYS D CG    1 
ATOM   23474 C  CD    . LYS D 4  18   ? 97.387  85.075  137.820 1.00 36.44  ? 18   LYS D CD    1 
ATOM   23475 C  CE    . LYS D 4  18   ? 96.783  85.465  136.494 1.00 35.25  ? 18   LYS D CE    1 
ATOM   23476 N  NZ    . LYS D 4  18   ? 97.323  84.620  135.398 1.00 37.44  ? 18   LYS D NZ    1 
ATOM   23477 N  N     . MET D 4  19   ? 96.709  83.112  143.068 1.00 37.38  ? 19   MET D N     1 
ATOM   23478 C  CA    . MET D 4  19   ? 96.771  82.264  144.247 1.00 36.86  ? 19   MET D CA    1 
ATOM   23479 C  C     . MET D 4  19   ? 95.372  82.097  144.817 1.00 37.31  ? 19   MET D C     1 
ATOM   23480 O  O     . MET D 4  19   ? 94.527  82.986  144.677 1.00 36.09  ? 19   MET D O     1 
ATOM   23481 C  CB    . MET D 4  19   ? 97.712  82.852  145.309 1.00 34.61  ? 19   MET D CB    1 
ATOM   23482 C  CG    . MET D 4  19   ? 99.184  82.576  145.055 1.00 34.02  ? 19   MET D CG    1 
ATOM   23483 S  SD    . MET D 4  19   ? 100.277 83.196  146.341 1.00 44.49  ? 19   MET D SD    1 
ATOM   23484 C  CE    . MET D 4  19   ? 99.796  84.911  146.422 1.00 31.04  ? 19   MET D CE    1 
ATOM   23485 N  N     . VAL D 4  20   ? 95.124  80.958  145.448 1.00 33.94  ? 20   VAL D N     1 
ATOM   23486 C  CA    . VAL D 4  20   ? 93.825  80.680  146.047 1.00 34.30  ? 20   VAL D CA    1 
ATOM   23487 C  C     . VAL D 4  20   ? 93.964  80.698  147.562 1.00 35.99  ? 20   VAL D C     1 
ATOM   23488 O  O     . VAL D 4  20   ? 94.937  80.193  148.130 1.00 38.57  ? 20   VAL D O     1 
ATOM   23489 C  CB    . VAL D 4  20   ? 93.238  79.343  145.548 1.00 35.22  ? 20   VAL D CB    1 
ATOM   23490 C  CG1   . VAL D 4  20   ? 93.143  79.348  144.038 1.00 34.48  ? 20   VAL D CG1   1 
ATOM   23491 C  CG2   . VAL D 4  20   ? 94.070  78.180  146.015 1.00 36.13  ? 20   VAL D CG2   1 
ATOM   23492 N  N     . LEU D 4  21   ? 92.989  81.308  148.225 1.00 35.70  ? 21   LEU D N     1 
ATOM   23493 C  CA    . LEU D 4  21   ? 93.007  81.417  149.674 1.00 37.72  ? 21   LEU D CA    1 
ATOM   23494 C  C     . LEU D 4  21   ? 92.666  80.079  150.314 1.00 36.75  ? 21   LEU D C     1 
ATOM   23495 O  O     . LEU D 4  21   ? 91.734  79.391  149.889 1.00 37.53  ? 21   LEU D O     1 
ATOM   23496 C  CB    . LEU D 4  21   ? 92.033  82.495  150.148 1.00 36.38  ? 21   LEU D CB    1 
ATOM   23497 C  CG    . LEU D 4  21   ? 92.511  83.929  149.928 1.00 35.72  ? 21   LEU D CG    1 
ATOM   23498 C  CD1   . LEU D 4  21   ? 91.416  84.926  150.253 1.00 36.31  ? 21   LEU D CD1   1 
ATOM   23499 C  CD2   . LEU D 4  21   ? 93.746  84.194  150.761 1.00 32.51  ? 21   LEU D CD2   1 
ATOM   23500 N  N     . LEU D 4  22   ? 93.430  79.718  151.340 1.00 37.99  ? 22   LEU D N     1 
ATOM   23501 C  CA    . LEU D 4  22   ? 93.278  78.444  152.025 1.00 40.39  ? 22   LEU D CA    1 
ATOM   23502 C  C     . LEU D 4  22   ? 92.469  78.560  153.308 1.00 41.01  ? 22   LEU D C     1 
ATOM   23503 O  O     . LEU D 4  22   ? 92.394  77.594  154.073 1.00 40.52  ? 22   LEU D O     1 
ATOM   23504 C  CB    . LEU D 4  22   ? 94.652  77.855  152.337 1.00 37.49  ? 22   LEU D CB    1 
ATOM   23505 C  CG    . LEU D 4  22   ? 95.328  77.098  151.202 1.00 40.60  ? 22   LEU D CG    1 
ATOM   23506 C  CD1   . LEU D 4  22   ? 96.460  76.251  151.746 1.00 40.19  ? 22   LEU D CD1   1 
ATOM   23507 C  CD2   . LEU D 4  22   ? 94.316  76.253  150.441 1.00 39.74  ? 22   LEU D CD2   1 
ATOM   23508 N  N     . GLU D 4  23   ? 91.864  79.716  153.559 1.00 43.72  ? 23   GLU D N     1 
ATOM   23509 C  CA    . GLU D 4  23   ? 91.255  80.027  154.843 1.00 42.41  ? 23   GLU D CA    1 
ATOM   23510 C  C     . GLU D 4  23   ? 89.906  80.679  154.583 1.00 44.35  ? 23   GLU D C     1 
ATOM   23511 O  O     . GLU D 4  23   ? 89.401  80.687  153.457 1.00 42.88  ? 23   GLU D O     1 
ATOM   23512 C  CB    . GLU D 4  23   ? 92.178  80.937  155.660 1.00 43.15  ? 23   GLU D CB    1 
ATOM   23513 C  CG    . GLU D 4  23   ? 93.372  80.243  156.292 1.00 43.41  ? 23   GLU D CG    1 
ATOM   23514 C  CD    . GLU D 4  23   ? 94.469  81.228  156.667 1.00 46.33  ? 23   GLU D CD    1 
ATOM   23515 O  OE1   . GLU D 4  23   ? 94.505  82.326  156.074 1.00 41.87  ? 23   GLU D OE1   1 
ATOM   23516 O  OE2   . GLU D 4  23   ? 95.286  80.912  157.557 1.00 48.34  ? 23   GLU D OE2   1 
ATOM   23517 N  N     . GLU D 4  24   ? 89.316  81.231  155.636 1.00 49.58  ? 24   GLU D N     1 
ATOM   23518 C  CA    . GLU D 4  24   ? 88.076  81.983  155.539 1.00 47.99  ? 24   GLU D CA    1 
ATOM   23519 C  C     . GLU D 4  24   ? 88.347  83.446  155.858 1.00 47.48  ? 24   GLU D C     1 
ATOM   23520 O  O     . GLU D 4  24   ? 88.985  83.764  156.866 1.00 43.74  ? 24   GLU D O     1 
ATOM   23521 C  CB    . GLU D 4  24   ? 87.011  81.420  156.483 1.00 43.50  ? 24   GLU D CB    1 
ATOM   23522 C  CG    . GLU D 4  24   ? 86.360  80.137  155.981 1.00 47.22  ? 24   GLU D CG    1 
ATOM   23523 C  CD    . GLU D 4  24   ? 85.447  80.365  154.788 1.00 49.04  ? 24   GLU D CD    1 
ATOM   23524 O  OE1   . GLU D 4  24   ? 84.833  81.446  154.705 1.00 47.47  ? 24   GLU D OE1   1 
ATOM   23525 O  OE2   . GLU D 4  24   ? 85.346  79.462  153.931 1.00 49.81  ? 24   GLU D OE2   1 
ATOM   23526 N  N     . LYS D 4  25   ? 87.865  84.329  154.993 1.00 46.30  ? 25   LYS D N     1 
ATOM   23527 C  CA    . LYS D 4  25   ? 88.154  85.751  155.106 1.00 44.96  ? 25   LYS D CA    1 
ATOM   23528 C  C     . LYS D 4  25   ? 87.303  86.361  156.214 1.00 43.46  ? 25   LYS D C     1 
ATOM   23529 O  O     . LYS D 4  25   ? 86.083  86.472  156.073 1.00 46.41  ? 25   LYS D O     1 
ATOM   23530 C  CB    . LYS D 4  25   ? 87.883  86.433  153.769 1.00 43.83  ? 25   LYS D CB    1 
ATOM   23531 C  CG    . LYS D 4  25   ? 88.711  87.671  153.502 1.00 43.97  ? 25   LYS D CG    1 
ATOM   23532 C  CD    . LYS D 4  25   ? 88.344  88.261  152.157 1.00 43.86  ? 25   LYS D CD    1 
ATOM   23533 C  CE    . LYS D 4  25   ? 88.544  87.246  151.048 1.00 43.18  ? 25   LYS D CE    1 
ATOM   23534 N  NZ    . LYS D 4  25   ? 88.223  87.802  149.711 1.00 42.14  ? 25   LYS D NZ    1 
ATOM   23535 N  N     . VAL D 4  26   ? 87.941  86.764  157.308 1.00 37.85  ? 26   VAL D N     1 
ATOM   23536 C  CA    . VAL D 4  26   ? 87.214  87.279  158.465 1.00 40.86  ? 26   VAL D CA    1 
ATOM   23537 C  C     . VAL D 4  26   ? 86.838  88.738  158.230 1.00 39.61  ? 26   VAL D C     1 
ATOM   23538 O  O     . VAL D 4  26   ? 87.563  89.455  157.529 1.00 40.17  ? 26   VAL D O     1 
ATOM   23539 C  CB    . VAL D 4  26   ? 88.035  87.125  159.756 1.00 40.19  ? 26   VAL D CB    1 
ATOM   23540 C  CG1   . VAL D 4  26   ? 88.372  85.668  159.993 1.00 39.53  ? 26   VAL D CG1   1 
ATOM   23541 C  CG2   . VAL D 4  26   ? 89.290  87.962  159.693 1.00 39.32  ? 26   VAL D CG2   1 
ATOM   23542 N  N     . PRO D 4  27   ? 85.700  89.210  158.762 1.00 41.01  ? 27   PRO D N     1 
ATOM   23543 C  CA    . PRO D 4  27   ? 85.385  90.633  158.715 1.00 41.17  ? 27   PRO D CA    1 
ATOM   23544 C  C     . PRO D 4  27   ? 86.529  91.556  159.105 1.00 39.37  ? 27   PRO D C     1 
ATOM   23545 O  O     . PRO D 4  27   ? 87.486  91.136  159.754 1.00 40.47  ? 27   PRO D O     1 
ATOM   23546 C  CB    . PRO D 4  27   ? 84.245  90.722  159.732 1.00 40.40  ? 27   PRO D CB    1 
ATOM   23547 C  CG    . PRO D 4  27   ? 83.500  89.357  159.538 1.00 39.63  ? 27   PRO D CG    1 
ATOM   23548 C  CD    . PRO D 4  27   ? 84.438  88.470  158.695 1.00 39.21  ? 27   PRO D CD    1 
ATOM   23549 N  N     . TYR D 4  28   ? 86.423  92.829  158.712 1.00 36.11  ? 28   TYR D N     1 
ATOM   23550 C  CA    . TYR D 4  28   ? 87.482  93.785  159.015 1.00 38.94  ? 28   TYR D CA    1 
ATOM   23551 C  C     . TYR D 4  28   ? 87.632  93.991  160.515 1.00 37.81  ? 28   TYR D C     1 
ATOM   23552 O  O     . TYR D 4  28   ? 88.752  94.104  161.028 1.00 36.40  ? 28   TYR D O     1 
ATOM   23553 C  CB    . TYR D 4  28   ? 87.202  95.116  158.318 1.00 36.12  ? 28   TYR D CB    1 
ATOM   23554 C  CG    . TYR D 4  28   ? 88.067  96.242  158.815 1.00 38.72  ? 28   TYR D CG    1 
ATOM   23555 C  CD1   . TYR D 4  28   ? 89.448  96.183  158.700 1.00 39.98  ? 28   TYR D CD1   1 
ATOM   23556 C  CD2   . TYR D 4  28   ? 87.510  97.358  159.419 1.00 37.83  ? 28   TYR D CD2   1 
ATOM   23557 C  CE1   . TYR D 4  28   ? 90.243  97.204  159.164 1.00 39.94  ? 28   TYR D CE1   1 
ATOM   23558 C  CE2   . TYR D 4  28   ? 88.302  98.385  159.883 1.00 37.88  ? 28   TYR D CE2   1 
ATOM   23559 C  CZ    . TYR D 4  28   ? 89.666  98.300  159.753 1.00 39.52  ? 28   TYR D CZ    1 
ATOM   23560 O  OH    . TYR D 4  28   ? 90.462  99.319  160.217 1.00 38.66  ? 28   TYR D OH    1 
ATOM   23561 N  N     . ASP D 4  29   ? 86.512  94.057  161.234 1.00 40.28  ? 29   ASP D N     1 
ATOM   23562 C  CA    . ASP D 4  29   ? 86.555  94.298  162.672 1.00 41.13  ? 29   ASP D CA    1 
ATOM   23563 C  C     . ASP D 4  29   ? 87.258  93.164  163.406 1.00 41.75  ? 29   ASP D C     1 
ATOM   23564 O  O     . ASP D 4  29   ? 88.109  93.404  164.274 1.00 42.91  ? 29   ASP D O     1 
ATOM   23565 C  CB    . ASP D 4  29   ? 85.132  94.491  163.184 1.00 40.99  ? 29   ASP D CB    1 
ATOM   23566 C  CG    . ASP D 4  29   ? 84.411  95.605  162.455 1.00 43.93  ? 29   ASP D CG    1 
ATOM   23567 O  OD1   . ASP D 4  29   ? 83.835  95.330  161.384 1.00 42.81  ? 29   ASP D OD1   1 
ATOM   23568 O  OD2   . ASP D 4  29   ? 84.432  96.757  162.942 1.00 41.59  ? 29   ASP D OD2   1 
ATOM   23569 N  N     . LYS D 4  30   ? 86.939  91.922  163.048 1.00 40.64  ? 30   LYS D N     1 
ATOM   23570 C  CA    . LYS D 4  30   ? 87.657  90.791  163.619 1.00 41.00  ? 30   LYS D CA    1 
ATOM   23571 C  C     . LYS D 4  30   ? 89.132  90.850  163.258 1.00 42.65  ? 30   LYS D C     1 
ATOM   23572 O  O     . LYS D 4  30   ? 89.990  90.532  164.087 1.00 42.46  ? 30   LYS D O     1 
ATOM   23573 C  CB    . LYS D 4  30   ? 87.035  89.481  163.140 1.00 41.81  ? 30   LYS D CB    1 
ATOM   23574 C  CG    . LYS D 4  30   ? 87.131  88.342  164.136 1.00 42.40  ? 30   LYS D CG    1 
ATOM   23575 C  CD    . LYS D 4  30   ? 87.871  87.159  163.540 1.00 44.74  ? 30   LYS D CD    1 
ATOM   23576 C  CE    . LYS D 4  30   ? 87.582  85.881  164.300 1.00 42.66  ? 30   LYS D CE    1 
ATOM   23577 N  NZ    . LYS D 4  30   ? 88.359  84.733  163.760 1.00 41.61  ? 30   LYS D NZ    1 
ATOM   23578 N  N     . PHE D 4  31   ? 89.444  91.263  162.026 1.00 41.04  ? 31   PHE D N     1 
ATOM   23579 C  CA    . PHE D 4  31   ? 90.833  91.353  161.581 1.00 39.86  ? 31   PHE D CA    1 
ATOM   23580 C  C     . PHE D 4  31   ? 91.637  92.319  162.444 1.00 39.84  ? 31   PHE D C     1 
ATOM   23581 O  O     . PHE D 4  31   ? 92.733  91.987  162.912 1.00 35.02  ? 31   PHE D O     1 
ATOM   23582 C  CB    . PHE D 4  31   ? 90.885  91.791  160.115 1.00 38.80  ? 31   PHE D CB    1 
ATOM   23583 C  CG    . PHE D 4  31   ? 92.165  92.489  159.741 1.00 41.22  ? 31   PHE D CG    1 
ATOM   23584 C  CD1   . PHE D 4  31   ? 93.364  91.802  159.711 1.00 40.01  ? 31   PHE D CD1   1 
ATOM   23585 C  CD2   . PHE D 4  31   ? 92.174  93.846  159.474 1.00 40.55  ? 31   PHE D CD2   1 
ATOM   23586 C  CE1   . PHE D 4  31   ? 94.532  92.442  159.389 1.00 38.55  ? 31   PHE D CE1   1 
ATOM   23587 C  CE2   . PHE D 4  31   ? 93.340  94.488  159.157 1.00 39.60  ? 31   PHE D CE2   1 
ATOM   23588 C  CZ    . PHE D 4  31   ? 94.520  93.785  159.113 1.00 40.56  ? 31   PHE D CZ    1 
ATOM   23589 N  N     . VAL D 4  32   ? 91.119  93.533  162.646 1.00 39.03  ? 32   VAL D N     1 
ATOM   23590 C  CA    . VAL D 4  32   ? 91.857  94.507  163.444 1.00 39.90  ? 32   VAL D CA    1 
ATOM   23591 C  C     . VAL D 4  32   ? 91.912  94.055  164.896 1.00 42.74  ? 32   VAL D C     1 
ATOM   23592 O  O     . VAL D 4  32   ? 92.898  94.303  165.605 1.00 43.22  ? 32   VAL D O     1 
ATOM   23593 C  CB    . VAL D 4  32   ? 91.250  95.915  163.295 1.00 39.84  ? 32   VAL D CB    1 
ATOM   23594 C  CG1   . VAL D 4  32   ? 89.753  95.879  163.443 1.00 39.98  ? 32   VAL D CG1   1 
ATOM   23595 C  CG2   . VAL D 4  32   ? 91.863  96.877  164.293 1.00 36.91  ? 32   VAL D CG2   1 
ATOM   23596 N  N     . GLN D 4  33   ? 90.882  93.336  165.351 1.00 42.57  ? 33   GLN D N     1 
ATOM   23597 C  CA    . GLN D 4  33   ? 90.947  92.749  166.684 1.00 43.18  ? 33   GLN D CA    1 
ATOM   23598 C  C     . GLN D 4  33   ? 92.125  91.784  166.810 1.00 44.93  ? 33   GLN D C     1 
ATOM   23599 O  O     . GLN D 4  33   ? 92.911  91.882  167.763 1.00 42.59  ? 33   GLN D O     1 
ATOM   23600 C  CB    . GLN D 4  33   ? 89.624  92.052  167.001 1.00 41.60  ? 33   GLN D CB    1 
ATOM   23601 C  CG    . GLN D 4  33   ? 89.746  90.758  167.783 1.00 43.70  ? 33   GLN D CG    1 
ATOM   23602 C  CD    . GLN D 4  33   ? 88.430  90.016  167.871 1.00 44.11  ? 33   GLN D CD    1 
ATOM   23603 O  OE1   . GLN D 4  33   ? 87.395  90.597  168.198 1.00 42.72  ? 33   GLN D OE1   1 
ATOM   23604 N  NE2   . GLN D 4  33   ? 88.459  88.725  167.565 1.00 44.68  ? 33   GLN D NE2   1 
ATOM   23605 N  N     . MET D 4  34   ? 92.278  90.862  165.852 1.00 43.17  ? 34   MET D N     1 
ATOM   23606 C  CA    . MET D 4  34   ? 93.377  89.900  165.935 1.00 43.52  ? 34   MET D CA    1 
ATOM   23607 C  C     . MET D 4  34   ? 94.728  90.580  165.792 1.00 45.23  ? 34   MET D C     1 
ATOM   23608 O  O     . MET D 4  34   ? 95.700  90.168  166.431 1.00 44.60  ? 34   MET D O     1 
ATOM   23609 C  CB    . MET D 4  34   ? 93.246  88.792  164.893 1.00 41.72  ? 34   MET D CB    1 
ATOM   23610 C  CG    . MET D 4  34   ? 91.851  88.355  164.553 1.00 43.74  ? 34   MET D CG    1 
ATOM   23611 S  SD    . MET D 4  34   ? 91.872  86.786  163.678 1.00 57.68  ? 34   MET D SD    1 
ATOM   23612 C  CE    . MET D 4  34   ? 93.186  85.951  164.565 1.00 44.11  ? 34   MET D CE    1 
ATOM   23613 N  N     . VAL D 4  35   ? 94.819  91.607  164.945 1.00 42.06  ? 35   VAL D N     1 
ATOM   23614 C  CA    . VAL D 4  35   ? 96.083  92.330  164.825 1.00 42.51  ? 35   VAL D CA    1 
ATOM   23615 C  C     . VAL D 4  35   ? 96.447  92.978  166.154 1.00 40.84  ? 35   VAL D C     1 
ATOM   23616 O  O     . VAL D 4  35   ? 97.593  92.891  166.609 1.00 41.90  ? 35   VAL D O     1 
ATOM   23617 C  CB    . VAL D 4  35   ? 96.018  93.359  163.679 1.00 42.36  ? 35   VAL D CB    1 
ATOM   23618 C  CG1   . VAL D 4  35   ? 96.849  94.593  164.006 1.00 39.60  ? 35   VAL D CG1   1 
ATOM   23619 C  CG2   . VAL D 4  35   ? 96.524  92.737  162.397 1.00 39.26  ? 35   VAL D CG2   1 
ATOM   23620 N  N     . LEU D 4  36   ? 95.471  93.605  166.817 1.00 39.13  ? 36   LEU D N     1 
ATOM   23621 C  CA    . LEU D 4  36   ? 95.764  94.301  168.068 1.00 43.13  ? 36   LEU D CA    1 
ATOM   23622 C  C     . LEU D 4  36   ? 96.022  93.329  169.215 1.00 42.90  ? 36   LEU D C     1 
ATOM   23623 O  O     . LEU D 4  36   ? 96.698  93.691  170.184 1.00 39.19  ? 36   LEU D O     1 
ATOM   23624 C  CB    . LEU D 4  36   ? 94.619  95.251  168.422 1.00 44.09  ? 36   LEU D CB    1 
ATOM   23625 C  CG    . LEU D 4  36   ? 94.754  96.705  167.959 1.00 44.26  ? 36   LEU D CG    1 
ATOM   23626 C  CD1   . LEU D 4  36   ? 95.940  97.390  168.616 1.00 41.25  ? 36   LEU D CD1   1 
ATOM   23627 C  CD2   . LEU D 4  36   ? 94.855  96.793  166.445 1.00 42.98  ? 36   LEU D CD2   1 
ATOM   23628 N  N     . ASN D 4  37   ? 95.499  92.103  169.132 1.00 43.60  ? 37   ASN D N     1 
ATOM   23629 C  CA    . ASN D 4  37   ? 95.737  91.113  170.183 1.00 42.24  ? 37   ASN D CA    1 
ATOM   23630 C  C     . ASN D 4  37   ? 97.021  90.317  169.961 1.00 43.34  ? 37   ASN D C     1 
ATOM   23631 O  O     . ASN D 4  37   ? 97.968  90.420  170.747 1.00 41.39  ? 37   ASN D O     1 
ATOM   23632 C  CB    . ASN D 4  37   ? 94.553  90.143  170.284 1.00 41.14  ? 37   ASN D CB    1 
ATOM   23633 C  CG    . ASN D 4  37   ? 93.402  90.701  171.085 1.00 44.22  ? 37   ASN D CG    1 
ATOM   23634 O  OD1   . ASN D 4  37   ? 93.559  91.661  171.837 1.00 47.10  ? 37   ASN D OD1   1 
ATOM   23635 N  ND2   . ASN D 4  37   ? 92.234  90.090  170.941 1.00 41.78  ? 37   ASN D ND2   1 
ATOM   23636 N  N     . THR D 4  38   ? 97.063  89.522  168.888 1.00 40.42  ? 38   THR D N     1 
ATOM   23637 C  CA    . THR D 4  38   ? 98.167  88.589  168.682 1.00 38.67  ? 38   THR D CA    1 
ATOM   23638 C  C     . THR D 4  38   ? 99.431  89.292  168.211 1.00 40.54  ? 38   THR D C     1 
ATOM   23639 O  O     . THR D 4  38   ? 100.537 88.783  168.420 1.00 40.41  ? 38   THR D O     1 
ATOM   23640 C  CB    . THR D 4  38   ? 97.748  87.510  167.686 1.00 41.76  ? 38   THR D CB    1 
ATOM   23641 O  OG1   . THR D 4  38   ? 96.457  87.005  168.050 1.00 44.15  ? 38   THR D OG1   1 
ATOM   23642 C  CG2   . THR D 4  38   ? 98.752  86.364  167.661 1.00 39.44  ? 38   THR D CG2   1 
ATOM   23643 N  N     . GLY D 4  39   ? 99.296  90.457  167.588 1.00 43.11  ? 39   GLY D N     1 
ATOM   23644 C  CA    . GLY D 4  39   ? 100.418 91.189  167.051 1.00 43.63  ? 39   GLY D CA    1 
ATOM   23645 C  C     . GLY D 4  39   ? 100.613 91.032  165.558 1.00 43.83  ? 39   GLY D C     1 
ATOM   23646 O  O     . GLY D 4  39   ? 101.413 91.767  164.974 1.00 43.19  ? 39   GLY D O     1 
ATOM   23647 N  N     . PHE D 4  40   ? 99.908  90.094  164.929 1.00 39.32  ? 40   PHE D N     1 
ATOM   23648 C  CA    . PHE D 4  40   ? 100.020 89.908  163.494 1.00 37.73  ? 40   PHE D CA    1 
ATOM   23649 C  C     . PHE D 4  40   ? 98.788  89.183  162.979 1.00 40.23  ? 40   PHE D C     1 
ATOM   23650 O  O     . PHE D 4  40   ? 98.000  88.633  163.748 1.00 44.87  ? 40   PHE D O     1 
ATOM   23651 C  CB    . PHE D 4  40   ? 101.285 89.135  163.117 1.00 39.74  ? 40   PHE D CB    1 
ATOM   23652 C  CG    . PHE D 4  40   ? 101.333 87.737  163.650 1.00 38.67  ? 40   PHE D CG    1 
ATOM   23653 C  CD1   . PHE D 4  40   ? 100.755 86.695  162.951 1.00 38.27  ? 40   PHE D CD1   1 
ATOM   23654 C  CD2   . PHE D 4  40   ? 101.999 87.456  164.819 1.00 39.79  ? 40   PHE D CD2   1 
ATOM   23655 C  CE1   . PHE D 4  40   ? 100.811 85.410  163.430 1.00 39.88  ? 40   PHE D CE1   1 
ATOM   23656 C  CE2   . PHE D 4  40   ? 102.061 86.168  165.300 1.00 40.59  ? 40   PHE D CE2   1 
ATOM   23657 C  CZ    . PHE D 4  40   ? 101.466 85.145  164.602 1.00 40.02  ? 40   PHE D CZ    1 
ATOM   23658 N  N     . PHE D 4  41   ? 98.636  89.196  161.660 1.00 35.18  ? 41   PHE D N     1 
ATOM   23659 C  CA    . PHE D 4  41   ? 97.585  88.465  160.970 1.00 34.28  ? 41   PHE D CA    1 
ATOM   23660 C  C     . PHE D 4  41   ? 98.215  87.615  159.877 1.00 35.30  ? 41   PHE D C     1 
ATOM   23661 O  O     . PHE D 4  41   ? 98.988  88.123  159.063 1.00 40.56  ? 41   PHE D O     1 
ATOM   23662 C  CB    . PHE D 4  41   ? 96.548  89.425  160.387 1.00 33.50  ? 41   PHE D CB    1 
ATOM   23663 C  CG    . PHE D 4  41   ? 95.305  88.751  159.900 1.00 36.76  ? 41   PHE D CG    1 
ATOM   23664 C  CD1   . PHE D 4  41   ? 94.504  88.037  160.767 1.00 36.56  ? 41   PHE D CD1   1 
ATOM   23665 C  CD2   . PHE D 4  41   ? 94.925  88.851  158.576 1.00 35.26  ? 41   PHE D CD2   1 
ATOM   23666 C  CE1   . PHE D 4  41   ? 93.355  87.419  160.315 1.00 37.51  ? 41   PHE D CE1   1 
ATOM   23667 C  CE2   . PHE D 4  41   ? 93.780  88.241  158.122 1.00 34.53  ? 41   PHE D CE2   1 
ATOM   23668 C  CZ    . PHE D 4  41   ? 92.992  87.524  158.991 1.00 35.44  ? 41   PHE D CZ    1 
ATOM   23669 N  N     . ARG D 4  42   ? 97.882  86.331  159.860 1.00 34.01  ? 42   ARG D N     1 
ATOM   23670 C  CA    . ARG D 4  42   ? 98.451  85.366  158.931 1.00 30.07  ? 42   ARG D CA    1 
ATOM   23671 C  C     . ARG D 4  42   ? 97.444  85.047  157.840 1.00 35.90  ? 42   ARG D C     1 
ATOM   23672 O  O     . ARG D 4  42   ? 96.290  84.717  158.133 1.00 38.95  ? 42   ARG D O     1 
ATOM   23673 C  CB    . ARG D 4  42   ? 98.838  84.078  159.655 1.00 33.02  ? 42   ARG D CB    1 
ATOM   23674 C  CG    . ARG D 4  42   ? 99.568  83.056  158.801 1.00 33.66  ? 42   ARG D CG    1 
ATOM   23675 C  CD    . ARG D 4  42   ? 100.825 82.597  159.484 1.00 33.61  ? 42   ARG D CD    1 
ATOM   23676 N  NE    . ARG D 4  42   ? 101.585 81.641  158.690 1.00 36.99  ? 42   ARG D NE    1 
ATOM   23677 C  CZ    . ARG D 4  42   ? 101.416 80.328  158.738 1.00 39.59  ? 42   ARG D CZ    1 
ATOM   23678 N  NH1   . ARG D 4  42   ? 100.502 79.778  159.520 1.00 36.93  ? 42   ARG D NH1   1 
ATOM   23679 N  NH2   . ARG D 4  42   ? 102.186 79.545  157.987 1.00 39.36  ? 42   ARG D NH2   1 
ATOM   23680 N  N     . ILE D 4  43   ? 97.882  85.137  156.589 1.00 31.18  ? 43   ILE D N     1 
ATOM   23681 C  CA    . ILE D 4  43   ? 97.093  84.728  155.436 1.00 32.48  ? 43   ILE D CA    1 
ATOM   23682 C  C     . ILE D 4  43   ? 97.889  83.681  154.677 1.00 32.28  ? 43   ILE D C     1 
ATOM   23683 O  O     . ILE D 4  43   ? 99.096  83.842  154.475 1.00 32.95  ? 43   ILE D O     1 
ATOM   23684 C  CB    . ILE D 4  43   ? 96.741  85.915  154.521 1.00 31.79  ? 43   ILE D CB    1 
ATOM   23685 C  CG1   . ILE D 4  43   ? 96.202  87.085  155.334 1.00 29.35  ? 43   ILE D CG1   1 
ATOM   23686 C  CG2   . ILE D 4  43   ? 95.713  85.506  153.496 1.00 30.36  ? 43   ILE D CG2   1 
ATOM   23687 C  CD1   . ILE D 4  43   ? 95.980  88.325  154.516 1.00 31.48  ? 43   ILE D CD1   1 
ATOM   23688 N  N     . ASN D 4  44   ? 97.225  82.604  154.282 1.00 34.89  ? 44   ASN D N     1 
ATOM   23689 C  CA    . ASN D 4  44   ? 97.858  81.525  153.541 1.00 36.26  ? 44   ASN D CA    1 
ATOM   23690 C  C     . ASN D 4  44   ? 97.192  81.366  152.182 1.00 37.49  ? 44   ASN D C     1 
ATOM   23691 O  O     . ASN D 4  44   ? 95.963  81.340  152.083 1.00 40.77  ? 44   ASN D O     1 
ATOM   23692 C  CB    . ASN D 4  44   ? 97.784  80.210  154.320 1.00 34.84  ? 44   ASN D CB    1 
ATOM   23693 C  CG    . ASN D 4  44   ? 98.577  80.252  155.608 1.00 36.87  ? 44   ASN D CG    1 
ATOM   23694 O  OD1   . ASN D 4  44   ? 98.015  80.279  156.700 1.00 37.99  ? 44   ASN D OD1   1 
ATOM   23695 N  ND2   . ASN D 4  44   ? 99.894  80.252  155.484 1.00 36.49  ? 44   ASN D ND2   1 
ATOM   23696 N  N     . ALA D 4  45   ? 98.010  81.257  151.138 1.00 31.07  ? 45   ALA D N     1 
ATOM   23697 C  CA    . ALA D 4  45   ? 97.520  81.129  149.776 1.00 32.00  ? 45   ALA D CA    1 
ATOM   23698 C  C     . ALA D 4  45   ? 98.330  80.069  149.049 1.00 33.25  ? 45   ALA D C     1 
ATOM   23699 O  O     . ALA D 4  45   ? 99.465  79.767  149.419 1.00 32.72  ? 45   ALA D O     1 
ATOM   23700 C  CB    . ALA D 4  45   ? 97.587  82.461  149.026 1.00 32.10  ? 45   ALA D CB    1 
ATOM   23701 N  N     . GLU D 4  46   ? 97.730  79.514  147.999 1.00 38.35  ? 46   GLU D N     1 
ATOM   23702 C  CA    . GLU D 4  46   ? 98.274  78.386  147.252 1.00 37.81  ? 46   GLU D CA    1 
ATOM   23703 C  C     . GLU D 4  46   ? 98.597  78.803  145.826 1.00 40.46  ? 46   GLU D C     1 
ATOM   23704 O  O     . GLU D 4  46   ? 97.743  79.368  145.139 1.00 43.09  ? 46   GLU D O     1 
ATOM   23705 C  CB    . GLU D 4  46   ? 97.273  77.235  147.219 1.00 40.67  ? 46   GLU D CB    1 
ATOM   23706 C  CG    . GLU D 4  46   ? 97.816  75.963  146.611 1.00 44.27  ? 46   GLU D CG    1 
ATOM   23707 C  CD    . GLU D 4  46   ? 98.036  74.895  147.647 1.00 47.89  ? 46   GLU D CD    1 
ATOM   23708 O  OE1   . GLU D 4  46   ? 98.059  75.245  148.843 1.00 47.80  ? 46   GLU D OE1   1 
ATOM   23709 O  OE2   . GLU D 4  46   ? 98.188  73.716  147.267 1.00 45.69  ? 46   GLU D OE2   1 
ATOM   23710 N  N     . THR D 4  47   ? 99.808  78.496  145.368 1.00 39.74  ? 47   THR D N     1 
ATOM   23711 C  CA    . THR D 4  47   ? 100.181 78.835  144.003 1.00 41.10  ? 47   THR D CA    1 
ATOM   23712 C  C     . THR D 4  47   ? 99.781  77.710  143.050 1.00 39.38  ? 47   THR D C     1 
ATOM   23713 O  O     . THR D 4  47   ? 99.262  76.670  143.455 1.00 38.56  ? 47   THR D O     1 
ATOM   23714 C  CB    . THR D 4  47   ? 101.676 79.121  143.902 1.00 38.63  ? 47   THR D CB    1 
ATOM   23715 O  OG1   . THR D 4  47   ? 102.405 77.892  143.948 1.00 38.44  ? 47   THR D OG1   1 
ATOM   23716 C  CG2   . THR D 4  47   ? 102.132 80.004  145.046 1.00 35.40  ? 47   THR D CG2   1 
ATOM   23717 N  N     . LEU D 4  48   ? 100.019 77.926  141.756 1.00 41.29  ? 48   LEU D N     1 
ATOM   23718 C  CA    . LEU D 4  48   ? 99.701  76.903  140.765 1.00 42.54  ? 48   LEU D CA    1 
ATOM   23719 C  C     . LEU D 4  48   ? 100.624 75.697  140.885 1.00 43.69  ? 48   LEU D C     1 
ATOM   23720 O  O     . LEU D 4  48   ? 100.230 74.579  140.540 1.00 42.93  ? 48   LEU D O     1 
ATOM   23721 C  CB    . LEU D 4  48   ? 99.773  77.490  139.357 1.00 41.07  ? 48   LEU D CB    1 
ATOM   23722 C  CG    . LEU D 4  48   ? 98.748  78.575  139.029 1.00 42.81  ? 48   LEU D CG    1 
ATOM   23723 C  CD1   . LEU D 4  48   ? 99.055  79.237  137.693 1.00 42.42  ? 48   LEU D CD1   1 
ATOM   23724 C  CD2   . LEU D 4  48   ? 97.350  77.983  139.028 1.00 41.40  ? 48   LEU D CD2   1 
ATOM   23725 N  N     . ASN D 4  49   ? 101.847 75.901  141.367 1.00 45.31  ? 49   ASN D N     1 
ATOM   23726 C  CA    . ASN D 4  49   ? 102.746 74.806  141.699 1.00 44.08  ? 49   ASN D CA    1 
ATOM   23727 C  C     . ASN D 4  49   ? 102.430 74.188  143.044 1.00 42.85  ? 49   ASN D C     1 
ATOM   23728 O  O     . ASN D 4  49   ? 103.294 73.522  143.624 1.00 46.01  ? 49   ASN D O     1 
ATOM   23729 C  CB    . ASN D 4  49   ? 104.201 75.280  141.677 1.00 43.13  ? 49   ASN D CB    1 
ATOM   23730 C  CG    . ASN D 4  49   ? 104.681 75.619  140.282 1.00 46.28  ? 49   ASN D CG    1 
ATOM   23731 O  OD1   . ASN D 4  49   ? 104.703 74.765  139.398 1.00 48.47  ? 49   ASN D OD1   1 
ATOM   23732 N  ND2   . ASN D 4  49   ? 105.076 76.870  140.078 1.00 46.85  ? 49   ASN D ND2   1 
ATOM   23733 N  N     . HIS D 4  50   ? 101.226 74.429  143.561 1.00 40.65  ? 50   HIS D N     1 
ATOM   23734 C  CA    . HIS D 4  50   ? 100.738 73.804  144.786 1.00 43.51  ? 50   HIS D CA    1 
ATOM   23735 C  C     . HIS D 4  50   ? 101.583 74.194  145.992 1.00 43.09  ? 50   HIS D C     1 
ATOM   23736 O  O     . HIS D 4  50   ? 101.566 73.519  147.021 1.00 41.04  ? 50   HIS D O     1 
ATOM   23737 C  CB    . HIS D 4  50   ? 100.680 72.282  144.635 1.00 43.50  ? 50   HIS D CB    1 
ATOM   23738 C  CG    . HIS D 4  50   ? 99.606  71.813  143.706 1.00 45.50  ? 50   HIS D CG    1 
ATOM   23739 N  ND1   . HIS D 4  50   ? 98.558  72.618  143.315 1.00 46.65  ? 50   HIS D ND1   1 
ATOM   23740 C  CD2   . HIS D 4  50   ? 99.430  70.631  143.070 1.00 45.29  ? 50   HIS D CD2   1 
ATOM   23741 C  CE1   . HIS D 4  50   ? 97.777  71.948  142.487 1.00 45.03  ? 50   HIS D CE1   1 
ATOM   23742 N  NE2   . HIS D 4  50   ? 98.282  70.739  142.323 1.00 43.66  ? 50   HIS D NE2   1 
ATOM   23743 N  N     . GLY D 4  51   ? 102.314 75.294  145.881 1.00 38.06  ? 51   GLY D N     1 
ATOM   23744 C  CA    . GLY D 4  51   ? 103.128 75.795  146.967 1.00 38.16  ? 51   GLY D CA    1 
ATOM   23745 C  C     . GLY D 4  51   ? 102.347 76.776  147.820 1.00 39.46  ? 51   GLY D C     1 
ATOM   23746 O  O     . GLY D 4  51   ? 101.332 77.314  147.395 1.00 40.28  ? 51   GLY D O     1 
ATOM   23747 N  N     . ILE D 4  52   ? 102.830 77.001  149.036 1.00 36.68  ? 52   ILE D N     1 
ATOM   23748 C  CA    . ILE D 4  52   ? 102.145 77.852  150.001 1.00 36.81  ? 52   ILE D CA    1 
ATOM   23749 C  C     . ILE D 4  52   ? 102.935 79.141  150.156 1.00 36.61  ? 52   ILE D C     1 
ATOM   23750 O  O     . ILE D 4  52   ? 104.161 79.112  150.308 1.00 40.12  ? 52   ILE D O     1 
ATOM   23751 C  CB    . ILE D 4  52   ? 101.974 77.140  151.353 1.00 38.33  ? 52   ILE D CB    1 
ATOM   23752 C  CG1   . ILE D 4  52   ? 100.664 76.348  151.382 1.00 35.87  ? 52   ILE D CG1   1 
ATOM   23753 C  CG2   . ILE D 4  52   ? 101.923 78.147  152.478 1.00 35.72  ? 52   ILE D CG2   1 
ATOM   23754 C  CD1   . ILE D 4  52   ? 100.668 75.092  150.529 1.00 33.25  ? 52   ILE D CD1   1 
ATOM   23755 N  N     . VAL D 4  53   ? 102.240 80.273  150.095 1.00 34.24  ? 53   VAL D N     1 
ATOM   23756 C  CA    . VAL D 4  53   ? 102.814 81.579  150.388 1.00 34.73  ? 53   VAL D CA    1 
ATOM   23757 C  C     . VAL D 4  53   ? 102.094 82.116  151.615 1.00 32.28  ? 53   VAL D C     1 
ATOM   23758 O  O     . VAL D 4  53   ? 100.862 82.206  151.623 1.00 38.45  ? 53   VAL D O     1 
ATOM   23759 C  CB    . VAL D 4  53   ? 102.668 82.546  149.200 1.00 36.27  ? 53   VAL D CB    1 
ATOM   23760 C  CG1   . VAL D 4  53   ? 103.056 83.956  149.601 1.00 31.97  ? 53   VAL D CG1   1 
ATOM   23761 C  CG2   . VAL D 4  53   ? 103.479 82.073  148.014 1.00 34.46  ? 53   VAL D CG2   1 
ATOM   23762 N  N     . SER D 4  54   ? 102.848 82.460  152.651 1.00 23.52  ? 54   SER D N     1 
ATOM   23763 C  CA    . SER D 4  54   ? 102.279 82.965  153.893 1.00 28.19  ? 54   SER D CA    1 
ATOM   23764 C  C     . SER D 4  54   ? 102.547 84.456  154.004 1.00 30.97  ? 54   SER D C     1 
ATOM   23765 O  O     . SER D 4  54   ? 103.681 84.903  153.812 1.00 29.54  ? 54   SER D O     1 
ATOM   23766 C  CB    . SER D 4  54   ? 102.857 82.233  155.105 1.00 29.68  ? 54   SER D CB    1 
ATOM   23767 O  OG    . SER D 4  54   ? 103.104 80.874  154.805 1.00 36.25  ? 54   SER D OG    1 
ATOM   23768 N  N     . VAL D 4  55   ? 101.505 85.220  154.313 1.00 29.01  ? 55   VAL D N     1 
ATOM   23769 C  CA    . VAL D 4  55   ? 101.595 86.667  154.447 1.00 27.23  ? 55   VAL D CA    1 
ATOM   23770 C  C     . VAL D 4  55   ? 101.391 87.021  155.911 1.00 30.09  ? 55   VAL D C     1 
ATOM   23771 O  O     . VAL D 4  55   ? 100.386 86.635  156.514 1.00 34.85  ? 55   VAL D O     1 
ATOM   23772 C  CB    . VAL D 4  55   ? 100.561 87.381  153.562 1.00 25.43  ? 55   VAL D CB    1 
ATOM   23773 C  CG1   . VAL D 4  55   ? 100.689 88.881  153.704 1.00 27.96  ? 55   VAL D CG1   1 
ATOM   23774 C  CG2   . VAL D 4  55   ? 100.714 86.961  152.121 1.00 26.21  ? 55   VAL D CG2   1 
ATOM   23775 N  N     . PHE D 4  56   ? 102.342 87.754  156.479 1.00 27.66  ? 56   PHE D N     1 
ATOM   23776 C  CA    . PHE D 4  56   ? 102.276 88.228  157.854 1.00 26.43  ? 56   PHE D CA    1 
ATOM   23777 C  C     . PHE D 4  56   ? 102.095 89.736  157.826 1.00 31.99  ? 56   PHE D C     1 
ATOM   23778 O  O     . PHE D 4  56   ? 102.950 90.450  157.299 1.00 36.67  ? 56   PHE D O     1 
ATOM   23779 C  CB    . PHE D 4  56   ? 103.555 87.880  158.609 1.00 29.70  ? 56   PHE D CB    1 
ATOM   23780 C  CG    . PHE D 4  56   ? 103.675 86.438  158.986 1.00 28.69  ? 56   PHE D CG    1 
ATOM   23781 C  CD1   . PHE D 4  56   ? 103.274 85.996  160.228 1.00 30.26  ? 56   PHE D CD1   1 
ATOM   23782 C  CD2   . PHE D 4  56   ? 104.204 85.526  158.096 1.00 29.75  ? 56   PHE D CD2   1 
ATOM   23783 C  CE1   . PHE D 4  56   ? 103.399 84.673  160.571 1.00 32.42  ? 56   PHE D CE1   1 
ATOM   23784 C  CE2   . PHE D 4  56   ? 104.327 84.205  158.432 1.00 31.79  ? 56   PHE D CE2   1 
ATOM   23785 C  CZ    . PHE D 4  56   ? 103.928 83.777  159.671 1.00 31.77  ? 56   PHE D CZ    1 
ATOM   23786 N  N     . ILE D 4  57   ? 101.007 90.226  158.402 1.00 31.08  ? 57   ILE D N     1 
ATOM   23787 C  CA    . ILE D 4  57   ? 100.781 91.659  158.526 1.00 30.29  ? 57   ILE D CA    1 
ATOM   23788 C  C     . ILE D 4  57   ? 101.023 92.046  159.977 1.00 32.55  ? 57   ILE D C     1 
ATOM   23789 O  O     . ILE D 4  57   ? 100.283 91.622  160.870 1.00 36.96  ? 57   ILE D O     1 
ATOM   23790 C  CB    . ILE D 4  57   ? 99.368  92.048  158.067 1.00 30.51  ? 57   ILE D CB    1 
ATOM   23791 C  CG1   . ILE D 4  57   ? 99.100  91.496  156.670 1.00 32.78  ? 57   ILE D CG1   1 
ATOM   23792 C  CG2   . ILE D 4  57   ? 99.212  93.541  158.059 1.00 30.63  ? 57   ILE D CG2   1 
ATOM   23793 C  CD1   . ILE D 4  57   ? 97.681  91.656  156.205 1.00 34.56  ? 57   ILE D CD1   1 
ATOM   23794 N  N     . PHE D 4  58   ? 102.056 92.845  160.218 1.00 31.35  ? 58   PHE D N     1 
ATOM   23795 C  CA    . PHE D 4  58   ? 102.458 93.230  161.564 1.00 32.72  ? 58   PHE D CA    1 
ATOM   23796 C  C     . PHE D 4  58   ? 101.837 94.567  161.934 1.00 33.97  ? 58   PHE D C     1 
ATOM   23797 O  O     . PHE D 4  58   ? 101.783 95.483  161.113 1.00 34.60  ? 58   PHE D O     1 
ATOM   23798 C  CB    . PHE D 4  58   ? 103.982 93.335  161.674 1.00 32.68  ? 58   PHE D CB    1 
ATOM   23799 C  CG    . PHE D 4  58   ? 104.685 92.018  161.617 1.00 33.50  ? 58   PHE D CG    1 
ATOM   23800 C  CD1   . PHE D 4  58   ? 104.950 91.308  162.764 1.00 34.06  ? 58   PHE D CD1   1 
ATOM   23801 C  CD2   . PHE D 4  58   ? 105.058 91.476  160.403 1.00 34.41  ? 58   PHE D CD2   1 
ATOM   23802 C  CE1   . PHE D 4  58   ? 105.592 90.090  162.702 1.00 35.95  ? 58   PHE D CE1   1 
ATOM   23803 C  CE2   . PHE D 4  58   ? 105.694 90.261  160.336 1.00 35.01  ? 58   PHE D CE2   1 
ATOM   23804 C  CZ    . PHE D 4  58   ? 105.964 89.568  161.485 1.00 33.96  ? 58   PHE D CZ    1 
ATOM   23805 N  N     . GLY D 4  59   ? 101.368 94.674  163.173 1.00 36.57  ? 59   GLY D N     1 
ATOM   23806 C  CA    . GLY D 4  59   ? 100.885 95.948  163.663 1.00 34.29  ? 59   GLY D CA    1 
ATOM   23807 C  C     . GLY D 4  59   ? 102.022 96.872  164.054 1.00 32.59  ? 59   GLY D C     1 
ATOM   23808 O  O     . GLY D 4  59   ? 103.088 96.442  164.489 1.00 33.81  ? 59   GLY D O     1 
ATOM   23809 N  N     . ALA D 4  60   ? 101.768 98.171  163.928 1.00 34.03  ? 60   ALA D N     1 
ATOM   23810 C  CA    . ALA D 4  60   ? 102.807 99.186  164.059 1.00 36.85  ? 60   ALA D CA    1 
ATOM   23811 C  C     . ALA D 4  60   ? 103.368 99.307  165.468 1.00 36.19  ? 60   ALA D C     1 
ATOM   23812 O  O     . ALA D 4  60   ? 104.291 100.101 165.670 1.00 36.60  ? 60   ALA D O     1 
ATOM   23813 C  CB    . ALA D 4  60   ? 102.269 100.544 163.605 1.00 34.80  ? 60   ALA D CB    1 
ATOM   23814 N  N     . ASN D 4  61   ? 102.840 98.562  166.441 1.00 40.54  ? 61   ASN D N     1 
ATOM   23815 C  CA    . ASN D 4  61   ? 103.352 98.620  167.805 1.00 40.07  ? 61   ASN D CA    1 
ATOM   23816 C  C     . ASN D 4  61   ? 103.476 97.246  168.452 1.00 39.49  ? 61   ASN D C     1 
ATOM   23817 O  O     . ASN D 4  61   ? 103.594 97.168  169.680 1.00 42.56  ? 61   ASN D O     1 
ATOM   23818 C  CB    . ASN D 4  61   ? 102.461 99.520  168.667 1.00 40.28  ? 61   ASN D CB    1 
ATOM   23819 C  CG    . ASN D 4  61   ? 102.736 100.995 168.447 1.00 39.20  ? 61   ASN D CG    1 
ATOM   23820 O  OD1   . ASN D 4  61   ? 103.880 101.435 168.508 1.00 42.86  ? 61   ASN D OD1   1 
ATOM   23821 N  ND2   . ASN D 4  61   ? 101.685 101.764 168.185 1.00 37.81  ? 61   ASN D ND2   1 
ATOM   23822 N  N     . GLY D 4  62   ? 103.466 96.169  167.675 1.00 35.08  ? 62   GLY D N     1 
ATOM   23823 C  CA    . GLY D 4  62   ? 103.511 94.835  168.233 1.00 34.06  ? 62   GLY D CA    1 
ATOM   23824 C  C     . GLY D 4  62   ? 104.877 94.470  168.780 1.00 36.77  ? 62   GLY D C     1 
ATOM   23825 O  O     . GLY D 4  62   ? 105.864 95.193  168.642 1.00 36.88  ? 62   GLY D O     1 
ATOM   23826 N  N     . LYS D 4  63   ? 104.924 93.310  169.434 1.00 39.08  ? 63   LYS D N     1 
ATOM   23827 C  CA    . LYS D 4  63   ? 106.167 92.859  170.044 1.00 42.26  ? 63   LYS D CA    1 
ATOM   23828 C  C     . LYS D 4  63   ? 107.164 92.345  169.018 1.00 42.13  ? 63   LYS D C     1 
ATOM   23829 O  O     . LYS D 4  63   ? 108.373 92.487  169.224 1.00 41.43  ? 63   LYS D O     1 
ATOM   23830 C  CB    . LYS D 4  63   ? 105.878 91.776  171.093 1.00 39.76  ? 63   LYS D CB    1 
ATOM   23831 C  CG    . LYS D 4  63   ? 105.697 90.371  170.534 1.00 40.39  ? 63   LYS D CG    1 
ATOM   23832 C  CD    . LYS D 4  63   ? 104.517 89.663  171.175 1.00 41.72  ? 63   LYS D CD    1 
ATOM   23833 C  CE    . LYS D 4  63   ? 103.227 89.922  170.414 1.00 41.96  ? 63   LYS D CE    1 
ATOM   23834 N  NZ    . LYS D 4  63   ? 102.111 89.076  170.920 1.00 43.14  ? 63   LYS D NZ    1 
ATOM   23835 N  N     . TYR D 4  64   ? 106.687 91.772  167.913 1.00 42.29  ? 64   TYR D N     1 
ATOM   23836 C  CA    . TYR D 4  64   ? 107.575 91.160  166.935 1.00 42.39  ? 64   TYR D CA    1 
ATOM   23837 C  C     . TYR D 4  64   ? 108.452 92.179  166.228 1.00 43.64  ? 64   TYR D C     1 
ATOM   23838 O  O     . TYR D 4  64   ? 109.536 91.827  165.759 1.00 46.31  ? 64   TYR D O     1 
ATOM   23839 C  CB    . TYR D 4  64   ? 106.755 90.396  165.908 1.00 41.85  ? 64   TYR D CB    1 
ATOM   23840 C  CG    . TYR D 4  64   ? 105.993 89.225  166.470 1.00 43.40  ? 64   TYR D CG    1 
ATOM   23841 C  CD1   . TYR D 4  64   ? 106.591 87.983  166.602 1.00 41.14  ? 64   TYR D CD1   1 
ATOM   23842 C  CD2   . TYR D 4  64   ? 104.675 89.361  166.869 1.00 43.91  ? 64   TYR D CD2   1 
ATOM   23843 C  CE1   . TYR D 4  64   ? 105.896 86.912  167.109 1.00 42.37  ? 64   TYR D CE1   1 
ATOM   23844 C  CE2   . TYR D 4  64   ? 103.974 88.294  167.376 1.00 42.74  ? 64   TYR D CE2   1 
ATOM   23845 C  CZ    . TYR D 4  64   ? 104.587 87.072  167.493 1.00 43.15  ? 64   TYR D CZ    1 
ATOM   23846 O  OH    . TYR D 4  64   ? 103.888 86.005  168.002 1.00 42.03  ? 64   TYR D OH    1 
ATOM   23847 N  N     . VAL D 4  65   ? 108.012 93.428  166.149 1.00 39.08  ? 65   VAL D N     1 
ATOM   23848 C  CA    . VAL D 4  65   ? 108.771 94.468  165.471 1.00 38.82  ? 65   VAL D CA    1 
ATOM   23849 C  C     . VAL D 4  65   ? 109.790 95.109  166.399 1.00 41.48  ? 65   VAL D C     1 
ATOM   23850 O  O     . VAL D 4  65   ? 110.926 95.376  166.003 1.00 41.19  ? 65   VAL D O     1 
ATOM   23851 C  CB    . VAL D 4  65   ? 107.800 95.512  164.888 1.00 39.50  ? 65   VAL D CB    1 
ATOM   23852 C  CG1   . VAL D 4  65   ? 108.509 96.826  164.657 1.00 40.99  ? 65   VAL D CG1   1 
ATOM   23853 C  CG2   . VAL D 4  65   ? 107.187 94.992  163.601 1.00 38.39  ? 65   VAL D CG2   1 
ATOM   23854 N  N     . HIS D 4  66   ? 109.407 95.370  167.649 1.00 46.58  ? 66   HIS D N     1 
ATOM   23855 C  CA    . HIS D 4  66   ? 110.292 96.088  168.559 1.00 43.05  ? 66   HIS D CA    1 
ATOM   23856 C  C     . HIS D 4  66   ? 111.394 95.218  169.147 1.00 43.11  ? 66   HIS D C     1 
ATOM   23857 O  O     . HIS D 4  66   ? 112.461 95.745  169.471 1.00 45.87  ? 66   HIS D O     1 
ATOM   23858 C  CB    . HIS D 4  66   ? 109.486 96.736  169.679 1.00 42.35  ? 66   HIS D CB    1 
ATOM   23859 C  CG    . HIS D 4  66   ? 108.673 97.907  169.230 1.00 43.50  ? 66   HIS D CG    1 
ATOM   23860 N  ND1   . HIS D 4  66   ? 107.367 97.790  168.809 1.00 43.55  ? 66   HIS D ND1   1 
ATOM   23861 C  CD2   . HIS D 4  66   ? 108.987 99.219  169.120 1.00 43.57  ? 66   HIS D CD2   1 
ATOM   23862 C  CE1   . HIS D 4  66   ? 106.907 98.982  168.472 1.00 44.85  ? 66   HIS D CE1   1 
ATOM   23863 N  NE2   . HIS D 4  66   ? 107.871 99.865  168.648 1.00 45.67  ? 66   HIS D NE2   1 
ATOM   23864 N  N     . HIS D 4  67   ? 111.178 93.913  169.296 1.00 44.69  ? 67   HIS D N     1 
ATOM   23865 C  CA    . HIS D 4  67   ? 112.209 93.021  169.817 1.00 47.31  ? 67   HIS D CA    1 
ATOM   23866 C  C     . HIS D 4  67   ? 112.500 91.943  168.787 1.00 47.17  ? 67   HIS D C     1 
ATOM   23867 O  O     . HIS D 4  67   ? 111.574 91.372  168.203 1.00 46.76  ? 67   HIS D O     1 
ATOM   23868 C  CB    . HIS D 4  67   ? 111.799 92.389  171.155 1.00 47.09  ? 67   HIS D CB    1 
ATOM   23869 C  CG    . HIS D 4  67   ? 111.480 93.388  172.223 1.00 49.26  ? 67   HIS D CG    1 
ATOM   23870 N  ND1   . HIS D 4  67   ? 112.415 94.274  172.716 1.00 47.58  ? 67   HIS D ND1   1 
ATOM   23871 C  CD2   . HIS D 4  67   ? 110.336 93.630  172.905 1.00 47.73  ? 67   HIS D CD2   1 
ATOM   23872 C  CE1   . HIS D 4  67   ? 111.854 95.031  173.642 1.00 45.78  ? 67   HIS D CE1   1 
ATOM   23873 N  NE2   . HIS D 4  67   ? 110.594 94.660  173.777 1.00 48.14  ? 67   HIS D NE2   1 
ATOM   23874 N  N     . GLY D 4  68   ? 113.785 91.662  168.571 1.00 40.51  ? 68   GLY D N     1 
ATOM   23875 C  CA    . GLY D 4  68   ? 114.158 90.667  167.584 1.00 41.14  ? 68   GLY D CA    1 
ATOM   23876 C  C     . GLY D 4  68   ? 113.914 89.244  168.036 1.00 43.66  ? 68   GLY D C     1 
ATOM   23877 O  O     . GLY D 4  68   ? 113.781 88.343  167.204 1.00 43.57  ? 68   GLY D O     1 
ATOM   23878 N  N     . GLY D 4  69   ? 113.853 89.015  169.347 1.00 43.78  ? 69   GLY D N     1 
ATOM   23879 C  CA    . GLY D 4  69   ? 113.666 87.660  169.838 1.00 41.55  ? 69   GLY D CA    1 
ATOM   23880 C  C     . GLY D 4  69   ? 112.317 87.080  169.463 1.00 44.26  ? 69   GLY D C     1 
ATOM   23881 O  O     . GLY D 4  69   ? 112.218 85.920  169.054 1.00 44.04  ? 69   GLY D O     1 
ATOM   23882 N  N     . ASP D 4  70   ? 111.257 87.876  169.604 1.00 44.93  ? 70   ASP D N     1 
ATOM   23883 C  CA    . ASP D 4  70   ? 109.926 87.402  169.245 1.00 46.38  ? 70   ASP D CA    1 
ATOM   23884 C  C     . ASP D 4  70   ? 109.838 87.085  167.759 1.00 47.10  ? 70   ASP D C     1 
ATOM   23885 O  O     . ASP D 4  70   ? 109.268 86.057  167.369 1.00 45.63  ? 70   ASP D O     1 
ATOM   23886 C  CB    . ASP D 4  70   ? 108.880 88.442  169.642 1.00 47.65  ? 70   ASP D CB    1 
ATOM   23887 C  CG    . ASP D 4  70   ? 108.696 88.538  171.146 1.00 48.98  ? 70   ASP D CG    1 
ATOM   23888 O  OD1   . ASP D 4  70   ? 108.743 87.485  171.817 1.00 47.98  ? 70   ASP D OD1   1 
ATOM   23889 O  OD2   . ASP D 4  70   ? 108.522 89.663  171.660 1.00 48.86  ? 70   ASP D OD2   1 
ATOM   23890 N  N     . MET D 4  71   ? 110.408 87.948  166.915 1.00 46.02  ? 71   MET D N     1 
ATOM   23891 C  CA    . MET D 4  71   ? 110.398 87.686  165.482 1.00 45.35  ? 71   MET D CA    1 
ATOM   23892 C  C     . MET D 4  71   ? 111.200 86.439  165.141 1.00 44.31  ? 71   MET D C     1 
ATOM   23893 O  O     . MET D 4  71   ? 110.768 85.627  164.317 1.00 43.21  ? 71   MET D O     1 
ATOM   23894 C  CB    . MET D 4  71   ? 110.926 88.895  164.712 1.00 43.70  ? 71   MET D CB    1 
ATOM   23895 C  CG    . MET D 4  71   ? 111.092 88.625  163.229 1.00 43.90  ? 71   MET D CG    1 
ATOM   23896 S  SD    . MET D 4  71   ? 109.690 89.161  162.232 1.00 52.74  ? 71   MET D SD    1 
ATOM   23897 C  CE    . MET D 4  71   ? 109.476 90.841  162.785 1.00 42.52  ? 71   MET D CE    1 
ATOM   23898 N  N     . ARG D 4  72   ? 112.366 86.262  165.771 1.00 42.17  ? 72   ARG D N     1 
ATOM   23899 C  CA    . ARG D 4  72   ? 113.160 85.061  165.524 1.00 42.52  ? 72   ARG D CA    1 
ATOM   23900 C  C     . ARG D 4  72   ? 112.394 83.806  165.916 1.00 43.92  ? 72   ARG D C     1 
ATOM   23901 O  O     . ARG D 4  72   ? 112.392 82.812  165.177 1.00 41.98  ? 72   ARG D O     1 
ATOM   23902 C  CB    . ARG D 4  72   ? 114.485 85.139  166.280 1.00 42.51  ? 72   ARG D CB    1 
ATOM   23903 C  CG    . ARG D 4  72   ? 115.296 83.850  166.242 1.00 43.48  ? 72   ARG D CG    1 
ATOM   23904 C  CD    . ARG D 4  72   ? 116.789 84.120  166.191 1.00 44.04  ? 72   ARG D CD    1 
ATOM   23905 N  NE    . ARG D 4  72   ? 117.171 85.267  167.006 1.00 44.66  ? 72   ARG D NE    1 
ATOM   23906 C  CZ    . ARG D 4  72   ? 118.368 85.838  166.980 1.00 45.90  ? 72   ARG D CZ    1 
ATOM   23907 N  NH1   . ARG D 4  72   ? 119.329 85.393  166.188 1.00 43.88  ? 72   ARG D NH1   1 
ATOM   23908 N  NH2   . ARG D 4  72   ? 118.606 86.883  167.766 1.00 45.28  ? 72   ARG D NH2   1 
ATOM   23909 N  N     . THR D 4  73   ? 111.722 83.840  167.068 1.00 40.77  ? 73   THR D N     1 
ATOM   23910 C  CA    . THR D 4  73   ? 110.932 82.692  167.496 1.00 43.18  ? 73   THR D CA    1 
ATOM   23911 C  C     . THR D 4  73   ? 109.814 82.396  166.505 1.00 40.58  ? 73   THR D C     1 
ATOM   23912 O  O     . THR D 4  73   ? 109.607 81.239  166.119 1.00 36.69  ? 73   THR D O     1 
ATOM   23913 C  CB    . THR D 4  73   ? 110.355 82.945  168.890 1.00 43.89  ? 73   THR D CB    1 
ATOM   23914 O  OG1   . THR D 4  73   ? 111.424 83.081  169.834 1.00 44.84  ? 73   THR D OG1   1 
ATOM   23915 C  CG2   . THR D 4  73   ? 109.461 81.789  169.315 1.00 37.89  ? 73   THR D CG2   1 
ATOM   23916 N  N     . LEU D 4  74   ? 109.097 83.435  166.066 1.00 37.61  ? 74   LEU D N     1 
ATOM   23917 C  CA    . LEU D 4  74   ? 108.016 83.237  165.104 1.00 37.84  ? 74   LEU D CA    1 
ATOM   23918 C  C     . LEU D 4  74   ? 108.532 82.631  163.807 1.00 39.95  ? 74   LEU D C     1 
ATOM   23919 O  O     . LEU D 4  74   ? 107.928 81.699  163.259 1.00 37.02  ? 74   LEU D O     1 
ATOM   23920 C  CB    . LEU D 4  74   ? 107.324 84.566  164.818 1.00 36.89  ? 74   LEU D CB    1 
ATOM   23921 C  CG    . LEU D 4  74   ? 106.164 84.546  163.824 1.00 39.24  ? 74   LEU D CG    1 
ATOM   23922 C  CD1   . LEU D 4  74   ? 105.202 83.406  164.109 1.00 36.87  ? 74   LEU D CD1   1 
ATOM   23923 C  CD2   . LEU D 4  74   ? 105.442 85.878  163.811 1.00 39.99  ? 74   LEU D CD2   1 
ATOM   23924 N  N     . LEU D 4  75   ? 109.653 83.148  163.301 1.00 38.85  ? 75   LEU D N     1 
ATOM   23925 C  CA    . LEU D 4  75   ? 110.169 82.678  162.024 1.00 37.39  ? 75   LEU D CA    1 
ATOM   23926 C  C     . LEU D 4  75   ? 110.638 81.233  162.114 1.00 38.98  ? 75   LEU D C     1 
ATOM   23927 O  O     . LEU D 4  75   ? 110.368 80.434  161.211 1.00 35.72  ? 75   LEU D O     1 
ATOM   23928 C  CB    . LEU D 4  75   ? 111.296 83.593  161.548 1.00 38.01  ? 75   LEU D CB    1 
ATOM   23929 C  CG    . LEU D 4  75   ? 110.905 85.045  161.259 1.00 38.87  ? 75   LEU D CG    1 
ATOM   23930 C  CD1   . LEU D 4  75   ? 112.045 85.797  160.598 1.00 39.18  ? 75   LEU D CD1   1 
ATOM   23931 C  CD2   . LEU D 4  75   ? 109.649 85.115  160.413 1.00 34.13  ? 75   LEU D CD2   1 
ATOM   23932 N  N     . THR D 4  76   ? 111.334 80.872  163.199 1.00 40.04  ? 76   THR D N     1 
ATOM   23933 C  CA    . THR D 4  76   ? 111.760 79.484  163.357 1.00 38.45  ? 76   THR D CA    1 
ATOM   23934 C  C     . THR D 4  76   ? 110.568 78.552  163.518 1.00 38.45  ? 76   THR D C     1 
ATOM   23935 O  O     . THR D 4  76   ? 110.565 77.439  162.981 1.00 38.26  ? 76   THR D O     1 
ATOM   23936 C  CB    . THR D 4  76   ? 112.705 79.338  164.547 1.00 37.44  ? 76   THR D CB    1 
ATOM   23937 O  OG1   . THR D 4  76   ? 112.003 79.652  165.751 1.00 41.31  ? 76   THR D OG1   1 
ATOM   23938 C  CG2   . THR D 4  76   ? 113.896 80.248  164.409 1.00 37.13  ? 76   THR D CG2   1 
ATOM   23939 N  N     . ASN D 4  77   ? 109.543 78.984  164.255 1.00 36.52  ? 77   ASN D N     1 
ATOM   23940 C  CA    . ASN D 4  77   ? 108.376 78.133  164.442 1.00 37.70  ? 77   ASN D CA    1 
ATOM   23941 C  C     . ASN D 4  77   ? 107.595 77.927  163.156 1.00 40.04  ? 77   ASN D C     1 
ATOM   23942 O  O     . ASN D 4  77   ? 107.068 76.834  162.935 1.00 40.74  ? 77   ASN D O     1 
ATOM   23943 C  CB    . ASN D 4  77   ? 107.458 78.720  165.513 1.00 38.78  ? 77   ASN D CB    1 
ATOM   23944 C  CG    . ASN D 4  77   ? 107.776 78.203  166.894 1.00 40.63  ? 77   ASN D CG    1 
ATOM   23945 O  OD1   . ASN D 4  77   ? 108.796 78.558  167.484 1.00 40.35  ? 77   ASN D OD1   1 
ATOM   23946 N  ND2   . ASN D 4  77   ? 106.908 77.348  167.418 1.00 41.80  ? 77   ASN D ND2   1 
ATOM   23947 N  N     . THR D 4  78   ? 107.498 78.950  162.310 1.00 40.38  ? 78   THR D N     1 
ATOM   23948 C  CA    . THR D 4  78   ? 106.717 78.832  161.087 1.00 38.61  ? 78   THR D CA    1 
ATOM   23949 C  C     . THR D 4  78   ? 107.420 78.027  160.006 1.00 38.74  ? 78   THR D C     1 
ATOM   23950 O  O     . THR D 4  78   ? 106.763 77.265  159.290 1.00 37.25  ? 78   THR D O     1 
ATOM   23951 C  CB    . THR D 4  78   ? 106.372 80.221  160.552 1.00 40.63  ? 78   THR D CB    1 
ATOM   23952 O  OG1   . THR D 4  78   ? 106.123 81.100  161.654 1.00 42.77  ? 78   THR D OG1   1 
ATOM   23953 C  CG2   . THR D 4  78   ? 105.141 80.159  159.672 1.00 37.04  ? 78   THR D CG2   1 
ATOM   23954 N  N     . LEU D 4  79   ? 108.733 78.172  159.868 1.00 37.39  ? 79   LEU D N     1 
ATOM   23955 C  CA    . LEU D 4  79   ? 109.464 77.462  158.829 1.00 37.91  ? 79   LEU D CA    1 
ATOM   23956 C  C     . LEU D 4  79   ? 109.704 75.995  159.161 1.00 38.60  ? 79   LEU D C     1 
ATOM   23957 O  O     . LEU D 4  79   ? 110.186 75.255  158.297 1.00 32.70  ? 79   LEU D O     1 
ATOM   23958 C  CB    . LEU D 4  79   ? 110.793 78.161  158.555 1.00 37.49  ? 79   LEU D CB    1 
ATOM   23959 C  CG    . LEU D 4  79   ? 110.682 79.482  157.794 1.00 36.44  ? 79   LEU D CG    1 
ATOM   23960 C  CD1   . LEU D 4  79   ? 111.999 80.238  157.825 1.00 35.07  ? 79   LEU D CD1   1 
ATOM   23961 C  CD2   . LEU D 4  79   ? 110.232 79.237  156.370 1.00 34.61  ? 79   LEU D CD2   1 
ATOM   23962 N  N     . ASN D 4  80   ? 109.384 75.558  160.380 1.00 41.83  ? 80   ASN D N     1 
ATOM   23963 C  CA    . ASN D 4  80   ? 109.456 74.152  160.753 1.00 40.59  ? 80   ASN D CA    1 
ATOM   23964 C  C     . ASN D 4  80   ? 108.141 73.410  160.559 1.00 40.19  ? 80   ASN D C     1 
ATOM   23965 O  O     . ASN D 4  80   ? 108.088 72.206  160.822 1.00 40.52  ? 80   ASN D O     1 
ATOM   23966 C  CB    . ASN D 4  80   ? 109.907 74.003  162.210 1.00 39.29  ? 80   ASN D CB    1 
ATOM   23967 C  CG    . ASN D 4  80   ? 111.401 74.143  162.373 1.00 42.15  ? 80   ASN D CG    1 
ATOM   23968 O  OD1   . ASN D 4  80   ? 112.173 73.489  161.674 1.00 43.01  ? 80   ASN D OD1   1 
ATOM   23969 N  ND2   . ASN D 4  80   ? 111.819 74.984  163.307 1.00 40.05  ? 80   ASN D ND2   1 
ATOM   23970 N  N     . GLU D 4  81   ? 107.091 74.086  160.099 1.00 41.64  ? 81   GLU D N     1 
ATOM   23971 C  CA    . GLU D 4  81   ? 105.810 73.430  159.882 1.00 43.14  ? 81   GLU D CA    1 
ATOM   23972 C  C     . GLU D 4  81   ? 105.886 72.477  158.693 1.00 42.85  ? 81   GLU D C     1 
ATOM   23973 O  O     . GLU D 4  81   ? 106.873 72.421  157.957 1.00 42.50  ? 81   GLU D O     1 
ATOM   23974 C  CB    . GLU D 4  81   ? 104.704 74.454  159.659 1.00 41.55  ? 81   GLU D CB    1 
ATOM   23975 C  CG    . GLU D 4  81   ? 103.995 74.891  160.911 1.00 41.60  ? 81   GLU D CG    1 
ATOM   23976 C  CD    . GLU D 4  81   ? 103.619 76.346  160.868 1.00 44.27  ? 81   GLU D CD    1 
ATOM   23977 O  OE1   . GLU D 4  81   ? 102.902 76.741  159.928 1.00 40.52  ? 81   GLU D OE1   1 
ATOM   23978 O  OE2   . GLU D 4  81   ? 104.042 77.096  161.771 1.00 46.19  ? 81   GLU D OE2   1 
ATOM   23979 N  N     . LYS D 4  82   ? 104.820 71.711  158.509 1.00 41.03  ? 82   LYS D N     1 
ATOM   23980 C  CA    . LYS D 4  82   ? 104.746 70.724  157.436 1.00 41.64  ? 82   LYS D CA    1 
ATOM   23981 C  C     . LYS D 4  82   ? 103.983 71.290  156.240 1.00 41.68  ? 82   LYS D C     1 
ATOM   23982 O  O     . LYS D 4  82   ? 102.944 70.782  155.826 1.00 42.06  ? 82   LYS D O     1 
ATOM   23983 C  CB    . LYS D 4  82   ? 104.103 69.442  157.952 1.00 41.53  ? 82   LYS D CB    1 
ATOM   23984 C  CG    . LYS D 4  82   ? 104.916 68.748  159.031 1.00 42.24  ? 82   LYS D CG    1 
ATOM   23985 C  CD    . LYS D 4  82   ? 104.169 67.565  159.613 1.00 43.16  ? 82   LYS D CD    1 
ATOM   23986 C  CE    . LYS D 4  82   ? 104.491 66.276  158.869 1.00 42.28  ? 82   LYS D CE    1 
ATOM   23987 N  NZ    . LYS D 4  82   ? 103.894 65.096  159.549 1.00 42.50  ? 82   LYS D NZ    1 
ATOM   23988 N  N     . LYS D 4  83   ? 104.525 72.372  155.687 1.00 40.04  ? 83   LYS D N     1 
ATOM   23989 C  CA    . LYS D 4  83   ? 103.991 72.994  154.486 1.00 41.52  ? 83   LYS D CA    1 
ATOM   23990 C  C     . LYS D 4  83   ? 105.110 73.184  153.474 1.00 42.10  ? 83   LYS D C     1 
ATOM   23991 O  O     . LYS D 4  83   ? 106.244 73.515  153.828 1.00 39.27  ? 83   LYS D O     1 
ATOM   23992 C  CB    . LYS D 4  83   ? 103.328 74.347  154.776 1.00 40.53  ? 83   LYS D CB    1 
ATOM   23993 C  CG    . LYS D 4  83   ? 102.580 74.437  156.093 1.00 39.61  ? 83   LYS D CG    1 
ATOM   23994 C  CD    . LYS D 4  83   ? 101.631 75.617  156.074 1.00 39.16  ? 83   LYS D CD    1 
ATOM   23995 C  CE    . LYS D 4  83   ? 100.442 75.393  156.984 1.00 40.66  ? 83   LYS D CE    1 
ATOM   23996 N  NZ    . LYS D 4  83   ? 100.827 75.285  158.415 1.00 43.54  ? 83   LYS D NZ    1 
ATOM   23997 N  N     . HIS D 4  84   ? 104.769 72.980  152.202 1.00 47.47  ? 84   HIS D N     1 
ATOM   23998 C  CA    . HIS D 4  84   ? 105.732 73.073  151.108 1.00 47.24  ? 84   HIS D CA    1 
ATOM   23999 C  C     . HIS D 4  84   ? 105.879 74.546  150.735 1.00 49.18  ? 84   HIS D C     1 
ATOM   24000 O  O     . HIS D 4  84   ? 105.302 75.040  149.765 1.00 49.08  ? 84   HIS D O     1 
ATOM   24001 C  CB    . HIS D 4  84   ? 105.269 72.225  149.932 1.00 48.69  ? 84   HIS D CB    1 
ATOM   24002 C  CG    . HIS D 4  84   ? 106.279 72.100  148.837 1.00 49.41  ? 84   HIS D CG    1 
ATOM   24003 N  ND1   . HIS D 4  84   ? 105.937 71.738  147.551 1.00 49.51  ? 84   HIS D ND1   1 
ATOM   24004 C  CD2   . HIS D 4  84   ? 107.622 72.259  148.839 1.00 48.16  ? 84   HIS D CD2   1 
ATOM   24005 C  CE1   . HIS D 4  84   ? 107.025 71.698  146.805 1.00 50.10  ? 84   HIS D CE1   1 
ATOM   24006 N  NE2   . HIS D 4  84   ? 108.062 72.007  147.563 1.00 51.97  ? 84   HIS D NE2   1 
ATOM   24007 N  N     . TYR D 4  85   ? 106.675 75.254  151.532 1.00 42.06  ? 85   TYR D N     1 
ATOM   24008 C  CA    . TYR D 4  85   ? 106.758 76.703  151.434 1.00 37.56  ? 85   TYR D CA    1 
ATOM   24009 C  C     . TYR D 4  85   ? 107.469 77.152  150.166 1.00 40.89  ? 85   TYR D C     1 
ATOM   24010 O  O     . TYR D 4  85   ? 108.350 76.470  149.639 1.00 43.57  ? 85   TYR D O     1 
ATOM   24011 C  CB    . TYR D 4  85   ? 107.481 77.279  152.647 1.00 39.27  ? 85   TYR D CB    1 
ATOM   24012 C  CG    . TYR D 4  85   ? 106.596 77.451  153.853 1.00 42.65  ? 85   TYR D CG    1 
ATOM   24013 C  CD1   . TYR D 4  85   ? 107.132 77.528  155.125 1.00 42.11  ? 85   TYR D CD1   1 
ATOM   24014 C  CD2   . TYR D 4  85   ? 105.221 77.545  153.716 1.00 42.26  ? 85   TYR D CD2   1 
ATOM   24015 C  CE1   . TYR D 4  85   ? 106.322 77.688  156.227 1.00 40.96  ? 85   TYR D CE1   1 
ATOM   24016 C  CE2   . TYR D 4  85   ? 104.408 77.707  154.810 1.00 42.63  ? 85   TYR D CE2   1 
ATOM   24017 C  CZ    . TYR D 4  85   ? 104.960 77.776  156.063 1.00 43.26  ? 85   TYR D CZ    1 
ATOM   24018 O  OH    . TYR D 4  85   ? 104.138 77.935  157.152 1.00 44.23  ? 85   TYR D OH    1 
ATOM   24019 N  N     . GLU D 4  86   ? 107.069 78.325  149.678 1.00 42.92  ? 86   GLU D N     1 
ATOM   24020 C  CA    . GLU D 4  86   ? 107.730 78.970  148.554 1.00 41.05  ? 86   GLU D CA    1 
ATOM   24021 C  C     . GLU D 4  86   ? 108.205 80.359  148.943 1.00 39.80  ? 86   GLU D C     1 
ATOM   24022 O  O     . GLU D 4  86   ? 109.325 80.752  148.606 1.00 40.81  ? 86   GLU D O     1 
ATOM   24023 C  CB    . GLU D 4  86   ? 106.796 79.062  147.350 1.00 39.25  ? 86   GLU D CB    1 
ATOM   24024 C  CG    . GLU D 4  86   ? 106.062 77.787  147.031 1.00 41.32  ? 86   GLU D CG    1 
ATOM   24025 C  CD    . GLU D 4  86   ? 105.796 77.636  145.549 1.00 46.48  ? 86   GLU D CD    1 
ATOM   24026 O  OE1   . GLU D 4  86   ? 105.092 78.494  144.980 1.00 44.58  ? 86   GLU D OE1   1 
ATOM   24027 O  OE2   . GLU D 4  86   ? 106.290 76.658  144.951 1.00 48.92  ? 86   GLU D OE2   1 
ATOM   24028 N  N     . GLU D 4  87   ? 107.373 81.109  149.659 1.00 35.39  ? 87   GLU D N     1 
ATOM   24029 C  CA    . GLU D 4  87   ? 107.738 82.469  150.020 1.00 34.92  ? 87   GLU D CA    1 
ATOM   24030 C  C     . GLU D 4  87   ? 106.978 82.895  151.263 1.00 34.05  ? 87   GLU D C     1 
ATOM   24031 O  O     . GLU D 4  87   ? 105.825 82.516  151.462 1.00 37.70  ? 87   GLU D O     1 
ATOM   24032 C  CB    . GLU D 4  87   ? 107.455 83.443  148.873 1.00 33.27  ? 87   GLU D CB    1 
ATOM   24033 C  CG    . GLU D 4  87   ? 107.976 84.841  149.108 1.00 34.35  ? 87   GLU D CG    1 
ATOM   24034 C  CD    . GLU D 4  87   ? 107.525 85.806  148.053 1.00 38.90  ? 87   GLU D CD    1 
ATOM   24035 O  OE1   . GLU D 4  87   ? 108.007 86.955  148.055 1.00 39.43  ? 87   GLU D OE1   1 
ATOM   24036 O  OE2   . GLU D 4  87   ? 106.691 85.415  147.214 1.00 39.71  ? 87   GLU D OE2   1 
ATOM   24037 N  N     . LEU D 4  88   ? 107.643 83.692  152.093 1.00 25.76  ? 88   LEU D N     1 
ATOM   24038 C  CA    . LEU D 4  88   ? 107.017 84.369  153.218 1.00 27.64  ? 88   LEU D CA    1 
ATOM   24039 C  C     . LEU D 4  88   ? 107.121 85.865  152.982 1.00 29.09  ? 88   LEU D C     1 
ATOM   24040 O  O     . LEU D 4  88   ? 108.228 86.401  152.898 1.00 33.60  ? 88   LEU D O     1 
ATOM   24041 C  CB    . LEU D 4  88   ? 107.695 84.006  154.541 1.00 26.21  ? 88   LEU D CB    1 
ATOM   24042 C  CG    . LEU D 4  88   ? 107.794 82.559  155.012 1.00 26.64  ? 88   LEU D CG    1 
ATOM   24043 C  CD1   . LEU D 4  88   ? 108.362 82.541  156.409 1.00 28.51  ? 88   LEU D CD1   1 
ATOM   24044 C  CD2   . LEU D 4  88   ? 106.459 81.863  154.978 1.00 28.85  ? 88   LEU D CD2   1 
ATOM   24045 N  N     . ILE D 4  89   ? 105.983 86.540  152.890 1.00 25.05  ? 89   ILE D N     1 
ATOM   24046 C  CA    . ILE D 4  89   ? 105.946 87.993  152.800 1.00 28.15  ? 89   ILE D CA    1 
ATOM   24047 C  C     . ILE D 4  89   ? 105.623 88.547  154.179 1.00 28.74  ? 89   ILE D C     1 
ATOM   24048 O  O     . ILE D 4  89   ? 104.571 88.242  154.748 1.00 28.50  ? 89   ILE D O     1 
ATOM   24049 C  CB    . ILE D 4  89   ? 104.922 88.477  151.762 1.00 27.35  ? 89   ILE D CB    1 
ATOM   24050 C  CG1   . ILE D 4  89   ? 105.384 88.141  150.350 1.00 27.50  ? 89   ILE D CG1   1 
ATOM   24051 C  CG2   . ILE D 4  89   ? 104.700 89.968  151.889 1.00 27.45  ? 89   ILE D CG2   1 
ATOM   24052 C  CD1   . ILE D 4  89   ? 104.655 87.010  149.742 1.00 27.37  ? 89   ILE D CD1   1 
ATOM   24053 N  N     . LEU D 4  90   ? 106.520 89.365  154.711 1.00 25.11  ? 90   LEU D N     1 
ATOM   24054 C  CA    . LEU D 4  90   ? 106.314 90.056  155.977 1.00 25.87  ? 90   LEU D CA    1 
ATOM   24055 C  C     . LEU D 4  90   ? 106.054 91.520  155.665 1.00 26.45  ? 90   LEU D C     1 
ATOM   24056 O  O     . LEU D 4  90   ? 106.874 92.173  155.020 1.00 31.77  ? 90   LEU D O     1 
ATOM   24057 C  CB    . LEU D 4  90   ? 107.519 89.904  156.897 1.00 28.51  ? 90   LEU D CB    1 
ATOM   24058 C  CG    . LEU D 4  90   ? 108.166 88.532  157.036 1.00 30.08  ? 90   LEU D CG    1 
ATOM   24059 C  CD1   . LEU D 4  90   ? 109.319 88.641  157.997 1.00 27.16  ? 90   LEU D CD1   1 
ATOM   24060 C  CD2   . LEU D 4  90   ? 107.172 87.498  157.518 1.00 29.03  ? 90   LEU D CD2   1 
ATOM   24061 N  N     . ILE D 4  91   ? 104.917 92.032  156.110 1.00 24.94  ? 91   ILE D N     1 
ATOM   24062 C  CA    . ILE D 4  91   ? 104.536 93.415  155.859 1.00 21.17  ? 91   ILE D CA    1 
ATOM   24063 C  C     . ILE D 4  91   ? 104.670 94.197  157.157 1.00 24.61  ? 91   ILE D C     1 
ATOM   24064 O  O     . ILE D 4  91   ? 104.035 93.866  158.160 1.00 33.12  ? 91   ILE D O     1 
ATOM   24065 C  CB    . ILE D 4  91   ? 103.108 93.498  155.303 1.00 23.90  ? 91   ILE D CB    1 
ATOM   24066 C  CG1   . ILE D 4  91   ? 102.962 92.588  154.088 1.00 21.40  ? 91   ILE D CG1   1 
ATOM   24067 C  CG2   . ILE D 4  91   ? 102.757 94.911  154.936 1.00 28.26  ? 91   ILE D CG2   1 
ATOM   24068 C  CD1   . ILE D 4  91   ? 101.553 92.461  153.590 1.00 22.34  ? 91   ILE D CD1   1 
ATOM   24069 N  N     . VAL D 4  92   ? 105.491 95.242  157.144 1.00 26.50  ? 92   VAL D N     1 
ATOM   24070 C  CA    . VAL D 4  92   ? 105.724 96.067  158.318 1.00 27.51  ? 92   VAL D CA    1 
ATOM   24071 C  C     . VAL D 4  92   ? 105.475 97.519  157.952 1.00 31.67  ? 92   VAL D C     1 
ATOM   24072 O  O     . VAL D 4  92   ? 105.198 97.857  156.804 1.00 38.34  ? 92   VAL D O     1 
ATOM   24073 C  CB    . VAL D 4  92   ? 107.145 95.909  158.886 1.00 29.61  ? 92   VAL D CB    1 
ATOM   24074 C  CG1   . VAL D 4  92   ? 107.352 94.514  159.436 1.00 30.92  ? 92   VAL D CG1   1 
ATOM   24075 C  CG2   . VAL D 4  92   ? 108.161 96.237  157.819 1.00 29.36  ? 92   VAL D CG2   1 
ATOM   24076 N  N     . ASP D 4  93   ? 105.566 98.377  158.959 1.00 34.06  ? 93   ASP D N     1 
ATOM   24077 C  CA    . ASP D 4  93   ? 105.497 99.806  158.734 1.00 33.61  ? 93   ASP D CA    1 
ATOM   24078 C  C     . ASP D 4  93   ? 106.866 100.293 158.262 1.00 35.50  ? 93   ASP D C     1 
ATOM   24079 O  O     . ASP D 4  93   ? 107.869 99.591  158.380 1.00 37.61  ? 93   ASP D O     1 
ATOM   24080 C  CB    . ASP D 4  93   ? 105.065 100.514 160.020 1.00 35.86  ? 93   ASP D CB    1 
ATOM   24081 C  CG    . ASP D 4  93   ? 104.496 101.894 159.772 1.00 41.52  ? 93   ASP D CG    1 
ATOM   24082 O  OD1   . ASP D 4  93   ? 105.270 102.844 159.586 1.00 42.55  ? 93   ASP D OD1   1 
ATOM   24083 O  OD2   . ASP D 4  93   ? 103.258 102.034 159.777 1.00 38.27  ? 93   ASP D OD2   1 
ATOM   24084 N  N     . LYS D 4  94   ? 106.905 101.501 157.710 1.00 36.64  ? 94   LYS D N     1 
ATOM   24085 C  CA    . LYS D 4  94   ? 108.136 101.961 157.070 1.00 38.37  ? 94   LYS D CA    1 
ATOM   24086 C  C     . LYS D 4  94   ? 109.337 102.056 158.010 1.00 39.75  ? 94   LYS D C     1 
ATOM   24087 O  O     . LYS D 4  94   ? 110.425 101.610 157.608 1.00 41.35  ? 94   LYS D O     1 
ATOM   24088 C  CB    . LYS D 4  94   ? 107.899 103.301 156.362 1.00 38.69  ? 94   LYS D CB    1 
ATOM   24089 C  CG    . LYS D 4  94   ? 109.074 103.716 155.496 1.00 39.38  ? 94   LYS D CG    1 
ATOM   24090 C  CD    . LYS D 4  94   ? 108.813 104.985 154.711 1.00 40.98  ? 94   LYS D CD    1 
ATOM   24091 C  CE    . LYS D 4  94   ? 110.055 105.387 153.930 1.00 39.71  ? 94   LYS D CE    1 
ATOM   24092 N  NZ    . LYS D 4  94   ? 109.847 106.600 153.094 1.00 39.06  ? 94   LYS D NZ    1 
ATOM   24093 N  N     . PRO D 4  95   ? 109.242 102.619 159.221 1.00 39.95  ? 95   PRO D N     1 
ATOM   24094 C  CA    . PRO D 4  95   ? 110.443 102.699 160.069 1.00 38.96  ? 95   PRO D CA    1 
ATOM   24095 C  C     . PRO D 4  95   ? 110.999 101.356 160.507 1.00 36.72  ? 95   PRO D C     1 
ATOM   24096 O  O     . PRO D 4  95   ? 112.141 101.302 160.974 1.00 39.04  ? 95   PRO D O     1 
ATOM   24097 C  CB    . PRO D 4  95   ? 109.965 103.529 161.265 1.00 36.63  ? 95   PRO D CB    1 
ATOM   24098 C  CG    . PRO D 4  95   ? 108.843 104.316 160.737 1.00 38.78  ? 95   PRO D CG    1 
ATOM   24099 C  CD    . PRO D 4  95   ? 108.146 103.411 159.796 1.00 36.66  ? 95   PRO D CD    1 
ATOM   24100 N  N     . VAL D 4  96   ? 110.234 100.271 160.392 1.00 32.23  ? 96   VAL D N     1 
ATOM   24101 C  CA    . VAL D 4  96   ? 110.769 98.968  160.776 1.00 36.17  ? 96   VAL D CA    1 
ATOM   24102 C  C     . VAL D 4  96   ? 111.955 98.594  159.905 1.00 36.50  ? 96   VAL D C     1 
ATOM   24103 O  O     . VAL D 4  96   ? 112.909 97.965  160.375 1.00 39.05  ? 96   VAL D O     1 
ATOM   24104 C  CB    . VAL D 4  96   ? 109.670 97.896  160.710 1.00 38.04  ? 96   VAL D CB    1 
ATOM   24105 C  CG1   . VAL D 4  96   ? 110.153 96.615  161.356 1.00 35.62  ? 96   VAL D CG1   1 
ATOM   24106 C  CG2   . VAL D 4  96   ? 108.416 98.402  161.391 1.00 34.12  ? 96   VAL D CG2   1 
ATOM   24107 N  N     . LEU D 4  97   ? 111.920 98.973  158.629 1.00 35.23  ? 97   LEU D N     1 
ATOM   24108 C  CA    . LEU D 4  97   ? 112.991 98.631  157.707 1.00 35.30  ? 97   LEU D CA    1 
ATOM   24109 C  C     . LEU D 4  97   ? 114.313 99.282  158.089 1.00 35.28  ? 97   LEU D C     1 
ATOM   24110 O  O     . LEU D 4  97   ? 115.369 98.787  157.688 1.00 34.67  ? 97   LEU D O     1 
ATOM   24111 C  CB    . LEU D 4  97   ? 112.592 99.046  156.296 1.00 33.11  ? 97   LEU D CB    1 
ATOM   24112 C  CG    . LEU D 4  97   ? 111.246 98.506  155.817 1.00 33.09  ? 97   LEU D CG    1 
ATOM   24113 C  CD1   . LEU D 4  97   ? 110.837 99.219  154.552 1.00 34.50  ? 97   LEU D CD1   1 
ATOM   24114 C  CD2   . LEU D 4  97   ? 111.282 97.009  155.604 1.00 35.91  ? 97   LEU D CD2   1 
ATOM   24115 N  N     . SER D 4  98   ? 114.283 100.377 158.845 1.00 37.68  ? 98   SER D N     1 
ATOM   24116 C  CA    . SER D 4  98   ? 115.501 101.049 159.275 1.00 39.41  ? 98   SER D CA    1 
ATOM   24117 C  C     . SER D 4  98   ? 116.111 100.454 160.540 1.00 41.35  ? 98   SER D C     1 
ATOM   24118 O  O     . SER D 4  98   ? 117.297 100.677 160.797 1.00 42.67  ? 98   SER D O     1 
ATOM   24119 C  CB    . SER D 4  98   ? 115.228 102.539 159.504 1.00 39.07  ? 98   SER D CB    1 
ATOM   24120 O  OG    . SER D 4  98   ? 115.335 103.270 158.298 1.00 40.24  ? 98   SER D OG    1 
ATOM   24121 N  N     . LYS D 4  99   ? 115.347 99.701  161.325 1.00 41.41  ? 99   LYS D N     1 
ATOM   24122 C  CA    . LYS D 4  99   ? 115.880 99.068  162.524 1.00 39.75  ? 99   LYS D CA    1 
ATOM   24123 C  C     . LYS D 4  99   ? 116.719 97.871  162.102 1.00 41.52  ? 99   LYS D C     1 
ATOM   24124 O  O     . LYS D 4  99   ? 116.229 96.987  161.394 1.00 39.52  ? 99   LYS D O     1 
ATOM   24125 C  CB    . LYS D 4  99   ? 114.752 98.623  163.450 1.00 38.98  ? 99   LYS D CB    1 
ATOM   24126 C  CG    . LYS D 4  99   ? 113.613 99.612  163.582 1.00 38.91  ? 99   LYS D CG    1 
ATOM   24127 C  CD    . LYS D 4  99   ? 114.006 100.857 164.334 1.00 40.06  ? 99   LYS D CD    1 
ATOM   24128 C  CE    . LYS D 4  99   ? 112.826 101.799 164.444 1.00 39.04  ? 99   LYS D CE    1 
ATOM   24129 N  NZ    . LYS D 4  99   ? 111.737 101.228 165.283 1.00 39.60  ? 99   LYS D NZ    1 
ATOM   24130 N  N     . LYS D 4  100  ? 117.976 97.835  162.543 1.00 44.14  ? 100  LYS D N     1 
ATOM   24131 C  CA    . LYS D 4  100  ? 118.907 96.842  162.022 1.00 42.14  ? 100  LYS D CA    1 
ATOM   24132 C  C     . LYS D 4  100  ? 118.569 95.437  162.506 1.00 43.81  ? 100  LYS D C     1 
ATOM   24133 O  O     . LYS D 4  100  ? 118.716 94.466  161.755 1.00 43.11  ? 100  LYS D O     1 
ATOM   24134 C  CB    . LYS D 4  100  ? 120.334 97.216  162.411 1.00 41.11  ? 100  LYS D CB    1 
ATOM   24135 C  CG    . LYS D 4  100  ? 121.050 98.048  161.362 1.00 42.37  ? 100  LYS D CG    1 
ATOM   24136 C  CD    . LYS D 4  100  ? 122.416 98.518  161.845 1.00 43.57  ? 100  LYS D CD    1 
ATOM   24137 C  CE    . LYS D 4  100  ? 122.807 99.826  161.176 1.00 43.16  ? 100  LYS D CE    1 
ATOM   24138 N  NZ    . LYS D 4  100  ? 124.027 99.693  160.335 1.00 44.21  ? 100  LYS D NZ    1 
ATOM   24139 N  N     . ASN D 4  101  ? 118.087 95.316  163.744 1.00 43.88  ? 101  ASN D N     1 
ATOM   24140 C  CA    . ASN D 4  101  ? 117.980 94.018  164.409 1.00 42.96  ? 101  ASN D CA    1 
ATOM   24141 C  C     . ASN D 4  101  ? 117.072 93.067  163.640 1.00 43.37  ? 101  ASN D C     1 
ATOM   24142 O  O     . ASN D 4  101  ? 117.396 91.887  163.440 1.00 42.22  ? 101  ASN D O     1 
ATOM   24143 C  CB    . ASN D 4  101  ? 117.444 94.228  165.819 1.00 40.66  ? 101  ASN D CB    1 
ATOM   24144 C  CG    . ASN D 4  101  ? 117.562 95.664  166.264 1.00 42.68  ? 101  ASN D CG    1 
ATOM   24145 O  OD1   . ASN D 4  101  ? 116.567 96.383  166.337 1.00 42.04  ? 101  ASN D OD1   1 
ATOM   24146 N  ND2   . ASN D 4  101  ? 118.780 96.093  166.568 1.00 42.15  ? 101  ASN D ND2   1 
ATOM   24147 N  N     . ILE D 4  102  ? 115.912 93.563  163.210 1.00 41.28  ? 102  ILE D N     1 
ATOM   24148 C  CA    . ILE D 4  102  ? 114.997 92.708  162.471 1.00 41.30  ? 102  ILE D CA    1 
ATOM   24149 C  C     . ILE D 4  102  ? 115.612 92.289  161.151 1.00 44.60  ? 102  ILE D C     1 
ATOM   24150 O  O     . ILE D 4  102  ? 115.480 91.131  160.743 1.00 45.08  ? 102  ILE D O     1 
ATOM   24151 C  CB    . ILE D 4  102  ? 113.644 93.410  162.277 1.00 43.36  ? 102  ILE D CB    1 
ATOM   24152 C  CG1   . ILE D 4  102  ? 113.167 93.983  163.612 1.00 44.90  ? 102  ILE D CG1   1 
ATOM   24153 C  CG2   . ILE D 4  102  ? 112.626 92.432  161.720 1.00 41.50  ? 102  ILE D CG2   1 
ATOM   24154 C  CD1   . ILE D 4  102  ? 113.152 95.473  163.658 1.00 42.49  ? 102  ILE D CD1   1 
ATOM   24155 N  N     . LEU D 4  103  ? 116.319 93.200  160.480 1.00 44.06  ? 103  LEU D N     1 
ATOM   24156 C  CA    . LEU D 4  103  ? 116.975 92.842  159.228 1.00 41.23  ? 103  LEU D CA    1 
ATOM   24157 C  C     . LEU D 4  103  ? 118.009 91.748  159.446 1.00 40.73  ? 103  LEU D C     1 
ATOM   24158 O  O     . LEU D 4  103  ? 118.149 90.843  158.613 1.00 43.29  ? 103  LEU D O     1 
ATOM   24159 C  CB    . LEU D 4  103  ? 117.615 94.077  158.603 1.00 42.61  ? 103  LEU D CB    1 
ATOM   24160 C  CG    . LEU D 4  103  ? 116.729 95.321  158.642 1.00 43.77  ? 103  LEU D CG    1 
ATOM   24161 C  CD1   . LEU D 4  103  ? 117.531 96.576  158.332 1.00 42.69  ? 103  LEU D CD1   1 
ATOM   24162 C  CD2   . LEU D 4  103  ? 115.549 95.172  157.696 1.00 39.88  ? 103  LEU D CD2   1 
ATOM   24163 N  N     . ASP D 4  104  ? 118.740 91.812  160.562 1.00 38.16  ? 104  ASP D N     1 
ATOM   24164 C  CA    . ASP D 4  104  ? 119.659 90.727  160.892 1.00 40.70  ? 104  ASP D CA    1 
ATOM   24165 C  C     . ASP D 4  104  ? 118.909 89.418  161.076 1.00 42.78  ? 104  ASP D C     1 
ATOM   24166 O  O     . ASP D 4  104  ? 119.366 88.363  160.621 1.00 42.00  ? 104  ASP D O     1 
ATOM   24167 C  CB    . ASP D 4  104  ? 120.466 91.053  162.148 1.00 40.19  ? 104  ASP D CB    1 
ATOM   24168 C  CG    . ASP D 4  104  ? 121.195 92.374  162.054 1.00 44.51  ? 104  ASP D CG    1 
ATOM   24169 O  OD1   . ASP D 4  104  ? 122.178 92.460  161.289 1.00 46.23  ? 104  ASP D OD1   1 
ATOM   24170 O  OD2   . ASP D 4  104  ? 120.815 93.314  162.777 1.00 43.51  ? 104  ASP D OD2   1 
ATOM   24171 N  N     . ILE D 4  105  ? 117.753 89.466  161.736 1.00 40.33  ? 105  ILE D N     1 
ATOM   24172 C  CA    . ILE D 4  105  ? 116.966 88.246  161.903 1.00 41.37  ? 105  ILE D CA    1 
ATOM   24173 C  C     . ILE D 4  105  ? 116.585 87.672  160.547 1.00 42.32  ? 105  ILE D C     1 
ATOM   24174 O  O     . ILE D 4  105  ? 116.681 86.459  160.319 1.00 39.88  ? 105  ILE D O     1 
ATOM   24175 C  CB    . ILE D 4  105  ? 115.721 88.507  162.770 1.00 41.35  ? 105  ILE D CB    1 
ATOM   24176 C  CG1   . ILE D 4  105  ? 116.105 88.926  164.195 1.00 40.61  ? 105  ILE D CG1   1 
ATOM   24177 C  CG2   . ILE D 4  105  ? 114.839 87.273  162.798 1.00 39.93  ? 105  ILE D CG2   1 
ATOM   24178 C  CD1   . ILE D 4  105  ? 117.438 88.393  164.680 1.00 38.08  ? 105  ILE D CD1   1 
ATOM   24179 N  N     . ILE D 4  106  ? 116.149 88.533  159.624 1.00 39.54  ? 106  ILE D N     1 
ATOM   24180 C  CA    . ILE D 4  106  ? 115.691 88.054  158.320 1.00 39.07  ? 106  ILE D CA    1 
ATOM   24181 C  C     . ILE D 4  106  ? 116.840 87.445  157.529 1.00 38.06  ? 106  ILE D C     1 
ATOM   24182 O  O     . ILE D 4  106  ? 116.679 86.397  156.895 1.00 36.44  ? 106  ILE D O     1 
ATOM   24183 C  CB    . ILE D 4  106  ? 114.988 89.171  157.527 1.00 40.02  ? 106  ILE D CB    1 
ATOM   24184 C  CG1   . ILE D 4  106  ? 114.119 90.031  158.437 1.00 39.02  ? 106  ILE D CG1   1 
ATOM   24185 C  CG2   . ILE D 4  106  ? 114.144 88.580  156.412 1.00 38.28  ? 106  ILE D CG2   1 
ATOM   24186 C  CD1   . ILE D 4  106  ? 112.768 89.464  158.717 1.00 33.07  ? 106  ILE D CD1   1 
ATOM   24187 N  N     . VAL D 4  107  ? 118.011 88.085  157.531 1.00 35.61  ? 107  VAL D N     1 
ATOM   24188 C  CA    . VAL D 4  107  ? 119.118 87.509  156.768 1.00 40.13  ? 107  VAL D CA    1 
ATOM   24189 C  C     . VAL D 4  107  ? 119.581 86.200  157.404 1.00 39.93  ? 107  VAL D C     1 
ATOM   24190 O  O     . VAL D 4  107  ? 119.894 85.229  156.701 1.00 38.95  ? 107  VAL D O     1 
ATOM   24191 C  CB    . VAL D 4  107  ? 120.274 88.516  156.605 1.00 38.64  ? 107  VAL D CB    1 
ATOM   24192 C  CG1   . VAL D 4  107  ? 120.620 89.160  157.903 1.00 36.06  ? 107  VAL D CG1   1 
ATOM   24193 C  CG2   . VAL D 4  107  ? 121.504 87.830  156.024 1.00 38.91  ? 107  VAL D CG2   1 
ATOM   24194 N  N     . GLU D 4  108  ? 119.605 86.140  158.740 1.00 41.08  ? 108  GLU D N     1 
ATOM   24195 C  CA    . GLU D 4  108  ? 119.976 84.903  159.419 1.00 41.38  ? 108  GLU D CA    1 
ATOM   24196 C  C     . GLU D 4  108  ? 119.007 83.779  159.088 1.00 39.69  ? 108  GLU D C     1 
ATOM   24197 O  O     . GLU D 4  108  ? 119.416 82.623  158.939 1.00 39.22  ? 108  GLU D O     1 
ATOM   24198 C  CB    . GLU D 4  108  ? 120.026 85.130  160.928 1.00 42.93  ? 108  GLU D CB    1 
ATOM   24199 C  CG    . GLU D 4  108  ? 120.641 83.975  161.702 1.00 42.97  ? 108  GLU D CG    1 
ATOM   24200 C  CD    . GLU D 4  108  ? 119.759 83.479  162.832 1.00 45.70  ? 108  GLU D CD    1 
ATOM   24201 O  OE1   . GLU D 4  108  ? 118.564 83.844  162.866 1.00 44.88  ? 108  GLU D OE1   1 
ATOM   24202 O  OE2   . GLU D 4  108  ? 120.264 82.724  163.689 1.00 44.81  ? 108  GLU D OE2   1 
ATOM   24203 N  N     . GLN D 4  109  ? 117.717 84.093  158.985 1.00 40.20  ? 109  GLN D N     1 
ATOM   24204 C  CA    . GLN D 4  109  ? 116.739 83.063  158.663 1.00 40.19  ? 109  GLN D CA    1 
ATOM   24205 C  C     . GLN D 4  109  ? 116.799 82.668  157.195 1.00 40.54  ? 109  GLN D C     1 
ATOM   24206 O  O     . GLN D 4  109  ? 116.514 81.516  156.856 1.00 42.71  ? 109  GLN D O     1 
ATOM   24207 C  CB    . GLN D 4  109  ? 115.340 83.546  159.034 1.00 42.80  ? 109  GLN D CB    1 
ATOM   24208 C  CG    . GLN D 4  109  ? 115.111 83.608  160.527 1.00 42.00  ? 109  GLN D CG    1 
ATOM   24209 C  CD    . GLN D 4  109  ? 115.229 82.262  161.213 1.00 41.88  ? 109  GLN D CD    1 
ATOM   24210 O  OE1   . GLN D 4  109  ? 115.174 81.209  160.582 1.00 39.80  ? 109  GLN D OE1   1 
ATOM   24211 N  NE2   . GLN D 4  109  ? 115.431 82.297  162.517 1.00 42.44  ? 109  GLN D NE2   1 
ATOM   24212 N  N     . ARG D 4  110  ? 117.144 83.609  156.314 1.00 35.62  ? 110  ARG D N     1 
ATOM   24213 C  CA    . ARG D 4  110  ? 117.381 83.268  154.917 1.00 34.71  ? 110  ARG D CA    1 
ATOM   24214 C  C     . ARG D 4  110  ? 118.531 82.286  154.788 1.00 37.75  ? 110  ARG D C     1 
ATOM   24215 O  O     . ARG D 4  110  ? 118.433 81.300  154.050 1.00 36.52  ? 110  ARG D O     1 
ATOM   24216 C  CB    . ARG D 4  110  ? 117.697 84.524  154.112 1.00 34.33  ? 110  ARG D CB    1 
ATOM   24217 C  CG    . ARG D 4  110  ? 116.518 85.366  153.695 1.00 35.60  ? 110  ARG D CG    1 
ATOM   24218 C  CD    . ARG D 4  110  ? 117.040 86.658  153.108 1.00 36.46  ? 110  ARG D CD    1 
ATOM   24219 N  NE    . ARG D 4  110  ? 115.985 87.582  152.725 1.00 35.29  ? 110  ARG D NE    1 
ATOM   24220 C  CZ    . ARG D 4  110  ? 116.174 88.877  152.528 1.00 35.46  ? 110  ARG D CZ    1 
ATOM   24221 N  NH1   . ARG D 4  110  ? 117.358 89.435  152.700 1.00 33.25  ? 110  ARG D NH1   1 
ATOM   24222 N  NH2   . ARG D 4  110  ? 115.148 89.633  152.155 1.00 37.02  ? 110  ARG D NH2   1 
ATOM   24223 N  N     . ALA D 4  111  ? 119.629 82.544  155.505 1.00 36.90  ? 111  ALA D N     1 
ATOM   24224 C  CA    . ALA D 4  111  ? 120.792 81.667  155.433 1.00 34.17  ? 111  ALA D CA    1 
ATOM   24225 C  C     . ALA D 4  111  ? 120.446 80.254  155.876 1.00 35.81  ? 111  ALA D C     1 
ATOM   24226 O  O     . ALA D 4  111  ? 120.957 79.276  155.319 1.00 34.03  ? 111  ALA D O     1 
ATOM   24227 C  CB    . ALA D 4  111  ? 121.923 82.230  156.289 1.00 30.24  ? 111  ALA D CB    1 
ATOM   24228 N  N     . ALA D 4  112  ? 119.582 80.125  156.881 1.00 35.35  ? 112  ALA D N     1 
ATOM   24229 C  CA    . ALA D 4  112  ? 119.199 78.813  157.373 1.00 37.73  ? 112  ALA D CA    1 
ATOM   24230 C  C     . ALA D 4  112  ? 118.265 78.070  156.428 1.00 39.72  ? 112  ALA D C     1 
ATOM   24231 O  O     . ALA D 4  112  ? 118.147 76.845  156.543 1.00 38.42  ? 112  ALA D O     1 
ATOM   24232 C  CB    . ALA D 4  112  ? 118.545 78.950  158.747 1.00 35.66  ? 112  ALA D CB    1 
ATOM   24233 N  N     . ASN D 4  113  ? 117.601 78.767  155.507 1.00 37.63  ? 113  ASN D N     1 
ATOM   24234 C  CA    . ASN D 4  113  ? 116.620 78.152  154.614 1.00 37.06  ? 113  ASN D CA    1 
ATOM   24235 C  C     . ASN D 4  113  ? 116.892 78.575  153.179 1.00 39.13  ? 113  ASN D C     1 
ATOM   24236 O  O     . ASN D 4  113  ? 116.312 79.548  152.682 1.00 41.69  ? 113  ASN D O     1 
ATOM   24237 C  CB    . ASN D 4  113  ? 115.195 78.520  155.026 1.00 38.32  ? 113  ASN D CB    1 
ATOM   24238 C  CG    . ASN D 4  113  ? 114.758 77.816  156.286 1.00 40.12  ? 113  ASN D CG    1 
ATOM   24239 O  OD1   . ASN D 4  113  ? 114.805 78.384  157.373 1.00 40.34  ? 113  ASN D OD1   1 
ATOM   24240 N  ND2   . ASN D 4  113  ? 114.326 76.570  156.149 1.00 38.44  ? 113  ASN D ND2   1 
ATOM   24241 N  N     . PRO D 4  114  ? 117.777 77.863  152.477 1.00 38.35  ? 114  PRO D N     1 
ATOM   24242 C  CA    . PRO D 4  114  ? 118.098 78.249  151.095 1.00 37.77  ? 114  PRO D CA    1 
ATOM   24243 C  C     . PRO D 4  114  ? 116.985 78.002  150.093 1.00 36.65  ? 114  PRO D C     1 
ATOM   24244 O  O     . PRO D 4  114  ? 117.036 78.570  148.995 1.00 38.39  ? 114  PRO D O     1 
ATOM   24245 C  CB    . PRO D 4  114  ? 119.326 77.387  150.771 1.00 38.30  ? 114  PRO D CB    1 
ATOM   24246 C  CG    . PRO D 4  114  ? 119.158 76.185  151.622 1.00 38.18  ? 114  PRO D CG    1 
ATOM   24247 C  CD    . PRO D 4  114  ? 118.508 76.658  152.898 1.00 39.22  ? 114  PRO D CD    1 
ATOM   24248 N  N     . THR D 4  115  ? 115.993 77.180  150.419 1.00 35.46  ? 115  THR D N     1 
ATOM   24249 C  CA    . THR D 4  115  ? 114.915 76.842  149.502 1.00 38.85  ? 115  THR D CA    1 
ATOM   24250 C  C     . THR D 4  115  ? 113.732 77.806  149.616 1.00 41.90  ? 115  THR D C     1 
ATOM   24251 O  O     . THR D 4  115  ? 112.837 77.787  148.766 1.00 41.25  ? 115  THR D O     1 
ATOM   24252 C  CB    . THR D 4  115  ? 114.493 75.381  149.748 1.00 42.23  ? 115  THR D CB    1 
ATOM   24253 O  OG1   . THR D 4  115  ? 115.582 74.515  149.407 1.00 41.62  ? 115  THR D OG1   1 
ATOM   24254 C  CG2   . THR D 4  115  ? 113.300 74.953  148.901 1.00 40.30  ? 115  THR D CG2   1 
ATOM   24255 N  N     . ILE D 4  116  ? 113.733 78.685  150.615 1.00 38.56  ? 116  ILE D N     1 
ATOM   24256 C  CA    . ILE D 4  116  ? 112.590 79.538  150.925 1.00 35.79  ? 116  ILE D CA    1 
ATOM   24257 C  C     . ILE D 4  116  ? 112.975 80.993  150.701 1.00 36.86  ? 116  ILE D C     1 
ATOM   24258 O  O     . ILE D 4  116  ? 114.064 81.420  151.101 1.00 37.49  ? 116  ILE D O     1 
ATOM   24259 C  CB    . ILE D 4  116  ? 112.104 79.322  152.370 1.00 37.18  ? 116  ILE D CB    1 
ATOM   24260 C  CG1   . ILE D 4  116  ? 111.917 77.833  152.643 1.00 38.43  ? 116  ILE D CG1   1 
ATOM   24261 C  CG2   . ILE D 4  116  ? 110.821 80.084  152.635 1.00 32.55  ? 116  ILE D CG2   1 
ATOM   24262 C  CD1   . ILE D 4  116  ? 110.976 77.160  151.682 1.00 38.40  ? 116  ILE D CD1   1 
ATOM   24263 N  N     . VAL D 4  117  ? 112.079 81.749  150.072 1.00 33.26  ? 117  VAL D N     1 
ATOM   24264 C  CA    . VAL D 4  117  ? 112.241 83.188  149.893 1.00 30.06  ? 117  VAL D CA    1 
ATOM   24265 C  C     . VAL D 4  117  ? 111.578 83.897  151.065 1.00 28.95  ? 117  VAL D C     1 
ATOM   24266 O  O     . VAL D 4  117  ? 110.403 83.657  151.356 1.00 32.00  ? 117  VAL D O     1 
ATOM   24267 C  CB    . VAL D 4  117  ? 111.635 83.652  148.559 1.00 31.72  ? 117  VAL D CB    1 
ATOM   24268 C  CG1   . VAL D 4  117  ? 112.002 85.088  148.271 1.00 30.87  ? 117  VAL D CG1   1 
ATOM   24269 C  CG2   . VAL D 4  117  ? 112.091 82.753  147.425 1.00 32.59  ? 117  VAL D CG2   1 
ATOM   24270 N  N     . ILE D 4  118  ? 112.322 84.769  151.737 1.00 24.70  ? 118  ILE D N     1 
ATOM   24271 C  CA    . ILE D 4  118  ? 111.794 85.588  152.823 1.00 27.72  ? 118  ILE D CA    1 
ATOM   24272 C  C     . ILE D 4  118  ? 111.889 87.040  152.385 1.00 26.16  ? 118  ILE D C     1 
ATOM   24273 O  O     . ILE D 4  118  ? 112.988 87.550  152.141 1.00 27.24  ? 118  ILE D O     1 
ATOM   24274 C  CB    . ILE D 4  118  ? 112.549 85.372  154.143 1.00 25.97  ? 118  ILE D CB    1 
ATOM   24275 C  CG1   . ILE D 4  118  ? 112.698 83.889  154.465 1.00 24.27  ? 118  ILE D CG1   1 
ATOM   24276 C  CG2   . ILE D 4  118  ? 111.828 86.063  155.273 1.00 22.98  ? 118  ILE D CG2   1 
ATOM   24277 C  CD1   . ILE D 4  118  ? 111.402 83.192  154.620 1.00 24.29  ? 118  ILE D CD1   1 
ATOM   24278 N  N     . ASN D 4  119  ? 110.752 87.720  152.311 1.00 24.67  ? 119  ASN D N     1 
ATOM   24279 C  CA    . ASN D 4  119  ? 110.702 89.105  151.874 1.00 24.97  ? 119  ASN D CA    1 
ATOM   24280 C  C     . ASN D 4  119  ? 109.944 89.954  152.878 1.00 24.15  ? 119  ASN D C     1 
ATOM   24281 O  O     . ASN D 4  119  ? 108.895 89.548  153.376 1.00 27.76  ? 119  ASN D O     1 
ATOM   24282 C  CB    . ASN D 4  119  ? 110.046 89.221  150.500 1.00 27.20  ? 119  ASN D CB    1 
ATOM   24283 C  CG    . ASN D 4  119  ? 111.005 88.924  149.382 1.00 27.62  ? 119  ASN D CG    1 
ATOM   24284 O  OD1   . ASN D 4  119  ? 110.754 88.064  148.548 1.00 27.38  ? 119  ASN D OD1   1 
ATOM   24285 N  ND2   . ASN D 4  119  ? 112.126 89.628  149.369 1.00 26.63  ? 119  ASN D ND2   1 
ATOM   24286 N  N     . ILE D 4  120  ? 110.471 91.141  153.157 1.00 23.12  ? 120  ILE D N     1 
ATOM   24287 C  CA    . ILE D 4  120  ? 109.853 92.088  154.074 1.00 22.91  ? 120  ILE D CA    1 
ATOM   24288 C  C     . ILE D 4  120  ? 109.621 93.396  153.330 1.00 24.99  ? 120  ILE D C     1 
ATOM   24289 O  O     . ILE D 4  120  ? 110.561 93.973  152.775 1.00 33.05  ? 120  ILE D O     1 
ATOM   24290 C  CB    . ILE D 4  120  ? 110.718 92.296  155.331 1.00 26.61  ? 120  ILE D CB    1 
ATOM   24291 C  CG1   . ILE D 4  120  ? 110.278 93.536  156.105 1.00 28.09  ? 120  ILE D CG1   1 
ATOM   24292 C  CG2   . ILE D 4  120  ? 112.179 92.387  154.969 1.00 27.23  ? 120  ILE D CG2   1 
ATOM   24293 C  CD1   . ILE D 4  120  ? 110.784 93.563  157.540 1.00 28.62  ? 120  ILE D CD1   1 
ATOM   24294 N  N     . TYR D 4  121  ? 108.381 93.866  153.331 1.00 23.14  ? 121  TYR D N     1 
ATOM   24295 C  CA    . TYR D 4  121  ? 107.930 95.000  152.541 1.00 24.00  ? 121  TYR D CA    1 
ATOM   24296 C  C     . TYR D 4  121  ? 107.258 96.028  153.435 1.00 22.60  ? 121  TYR D C     1 
ATOM   24297 O  O     . TYR D 4  121  ? 106.731 95.683  154.494 1.00 30.85  ? 121  TYR D O     1 
ATOM   24298 C  CB    . TYR D 4  121  ? 106.943 94.548  151.457 1.00 23.88  ? 121  TYR D CB    1 
ATOM   24299 C  CG    . TYR D 4  121  ? 107.520 93.584  150.451 1.00 24.49  ? 121  TYR D CG    1 
ATOM   24300 C  CD1   . TYR D 4  121  ? 108.655 93.902  149.725 1.00 23.95  ? 121  TYR D CD1   1 
ATOM   24301 C  CD2   . TYR D 4  121  ? 106.921 92.363  150.220 1.00 21.83  ? 121  TYR D CD2   1 
ATOM   24302 C  CE1   . TYR D 4  121  ? 109.174 93.026  148.814 1.00 23.30  ? 121  TYR D CE1   1 
ATOM   24303 C  CE2   . TYR D 4  121  ? 107.431 91.486  149.311 1.00 20.66  ? 121  TYR D CE2   1 
ATOM   24304 C  CZ    . TYR D 4  121  ? 108.555 91.818  148.610 1.00 22.21  ? 121  TYR D CZ    1 
ATOM   24305 O  OH    . TYR D 4  121  ? 109.061 90.929  147.697 1.00 24.49  ? 121  TYR D OH    1 
ATOM   24306 N  N     . PRO D 4  122  ? 107.252 97.294  153.040 1.00 25.99  ? 122  PRO D N     1 
ATOM   24307 C  CA    . PRO D 4  122  ? 106.575 98.327  153.831 1.00 27.84  ? 122  PRO D CA    1 
ATOM   24308 C  C     . PRO D 4  122  ? 105.068 98.304  153.593 1.00 29.84  ? 122  PRO D C     1 
ATOM   24309 O  O     . PRO D 4  122  ? 104.537 97.471  152.865 1.00 32.80  ? 122  PRO D O     1 
ATOM   24310 C  CB    . PRO D 4  122  ? 107.205 99.623  153.323 1.00 26.92  ? 122  PRO D CB    1 
ATOM   24311 C  CG    . PRO D 4  122  ? 107.591 99.320  151.937 1.00 27.52  ? 122  PRO D CG    1 
ATOM   24312 C  CD    . PRO D 4  122  ? 107.981 97.872  151.901 1.00 30.94  ? 122  PRO D CD    1 
ATOM   24313 N  N     . TYR D 4  123  ? 104.376 99.246  154.235 1.00 26.39  ? 123  TYR D N     1 
ATOM   24314 C  CA    . TYR D 4  123  ? 102.919 99.273  154.151 1.00 30.10  ? 123  TYR D CA    1 
ATOM   24315 C  C     . TYR D 4  123  ? 102.446 99.798  152.807 1.00 33.77  ? 123  TYR D C     1 
ATOM   24316 O  O     . TYR D 4  123  ? 101.506 99.251  152.222 1.00 34.85  ? 123  TYR D O     1 
ATOM   24317 C  CB    . TYR D 4  123  ? 102.334 100.127 155.276 1.00 32.99  ? 123  TYR D CB    1 
ATOM   24318 C  CG    . TYR D 4  123  ? 102.113 99.396  156.577 1.00 32.97  ? 123  TYR D CG    1 
ATOM   24319 C  CD1   . TYR D 4  123  ? 101.865 100.091 157.747 1.00 33.14  ? 123  TYR D CD1   1 
ATOM   24320 C  CD2   . TYR D 4  123  ? 102.149 98.015  156.635 1.00 34.86  ? 123  TYR D CD2   1 
ATOM   24321 C  CE1   . TYR D 4  123  ? 101.669 99.435  158.937 1.00 33.83  ? 123  TYR D CE1   1 
ATOM   24322 C  CE2   . TYR D 4  123  ? 101.953 97.349  157.822 1.00 34.11  ? 123  TYR D CE2   1 
ATOM   24323 C  CZ    . TYR D 4  123  ? 101.712 98.066  158.968 1.00 33.31  ? 123  TYR D CZ    1 
ATOM   24324 O  OH    . TYR D 4  123  ? 101.514 97.411  160.152 1.00 35.36  ? 123  TYR D OH    1 
ATOM   24325 N  N     . HIS D 4  124  ? 103.082 100.859 152.301 1.00 30.74  ? 124  HIS D N     1 
ATOM   24326 C  CA    . HIS D 4  124  ? 102.564 101.548 151.124 1.00 26.43  ? 124  HIS D CA    1 
ATOM   24327 C  C     . HIS D 4  124  ? 102.557 100.667 149.891 1.00 27.19  ? 124  HIS D C     1 
ATOM   24328 O  O     . HIS D 4  124  ? 101.873 100.989 148.917 1.00 30.09  ? 124  HIS D O     1 
ATOM   24329 C  CB    . HIS D 4  124  ? 103.367 102.817 150.842 1.00 25.88  ? 124  HIS D CB    1 
ATOM   24330 C  CG    . HIS D 4  124  ? 104.831 102.585 150.634 1.00 28.01  ? 124  HIS D CG    1 
ATOM   24331 N  ND1   . HIS D 4  124  ? 105.334 101.936 149.528 1.00 27.72  ? 124  HIS D ND1   1 
ATOM   24332 C  CD2   . HIS D 4  124  ? 105.903 102.947 151.375 1.00 29.22  ? 124  HIS D CD2   1 
ATOM   24333 C  CE1   . HIS D 4  124  ? 106.650 101.886 149.609 1.00 29.12  ? 124  HIS D CE1   1 
ATOM   24334 N  NE2   . HIS D 4  124  ? 107.021 102.494 150.720 1.00 28.93  ? 124  HIS D NE2   1 
ATOM   24335 N  N     . LEU D 4  125  ? 103.290 99.561  149.913 1.00 26.37  ? 125  LEU D N     1 
ATOM   24336 C  CA    . LEU D 4  125  ? 103.367 98.708  148.743 1.00 22.85  ? 125  LEU D CA    1 
ATOM   24337 C  C     . LEU D 4  125  ? 102.085 97.919  148.537 1.00 23.28  ? 125  LEU D C     1 
ATOM   24338 O  O     . LEU D 4  125  ? 101.863 97.394  147.444 1.00 25.37  ? 125  LEU D O     1 
ATOM   24339 C  CB    . LEU D 4  125  ? 104.570 97.777  148.876 1.00 23.27  ? 125  LEU D CB    1 
ATOM   24340 C  CG    . LEU D 4  125  ? 105.061 97.036  147.637 1.00 23.81  ? 125  LEU D CG    1 
ATOM   24341 C  CD1   . LEU D 4  125  ? 106.571 97.054  147.622 1.00 20.41  ? 125  LEU D CD1   1 
ATOM   24342 C  CD2   . LEU D 4  125  ? 104.550 95.633  147.564 1.00 23.30  ? 125  LEU D CD2   1 
ATOM   24343 N  N     . PHE D 4  126  ? 101.229 97.834  149.557 1.00 29.47  ? 126  PHE D N     1 
ATOM   24344 C  CA    . PHE D 4  126  ? 100.008 97.041  149.478 1.00 25.64  ? 126  PHE D CA    1 
ATOM   24345 C  C     . PHE D 4  126  ? 98.762  97.852  149.810 1.00 27.52  ? 126  PHE D C     1 
ATOM   24346 O  O     . PHE D 4  126  ? 97.701  97.271  150.030 1.00 30.02  ? 126  PHE D O     1 
ATOM   24347 C  CB    . PHE D 4  126  ? 100.084 95.831  150.408 1.00 20.35  ? 126  PHE D CB    1 
ATOM   24348 C  CG    . PHE D 4  126  ? 101.189 94.885  150.084 1.00 22.99  ? 126  PHE D CG    1 
ATOM   24349 C  CD1   . PHE D 4  126  ? 101.002 93.876  149.168 1.00 23.00  ? 126  PHE D CD1   1 
ATOM   24350 C  CD2   . PHE D 4  126  ? 102.406 94.980  150.722 1.00 23.61  ? 126  PHE D CD2   1 
ATOM   24351 C  CE1   . PHE D 4  126  ? 102.011 93.006  148.876 1.00 23.35  ? 126  PHE D CE1   1 
ATOM   24352 C  CE2   . PHE D 4  126  ? 103.413 94.102  150.434 1.00 22.36  ? 126  PHE D CE2   1 
ATOM   24353 C  CZ    . PHE D 4  126  ? 103.211 93.114  149.515 1.00 21.93  ? 126  PHE D CZ    1 
ATOM   24354 N  N     . CYS D 4  127  ? 98.862  99.176  149.853 1.00 25.69  ? 127  CYS D N     1 
ATOM   24355 C  CA    . CYS D 4  127  ? 97.732  100.027 150.190 1.00 24.56  ? 127  CYS D CA    1 
ATOM   24356 C  C     . CYS D 4  127  ? 97.045  100.593 148.961 1.00 28.89  ? 127  CYS D C     1 
ATOM   24357 O  O     . CYS D 4  127  ? 96.345  101.602 149.065 1.00 29.98  ? 127  CYS D O     1 
ATOM   24358 C  CB    . CYS D 4  127  ? 98.175  101.160 151.112 1.00 24.45  ? 127  CYS D CB    1 
ATOM   24359 S  SG    . CYS D 4  127  ? 98.571  100.632 152.786 1.00 40.24  ? 127  CYS D SG    1 
ATOM   24360 N  N     . ILE D 4  128  ? 97.244  99.973  147.798 1.00 25.11  ? 128  ILE D N     1 
ATOM   24361 C  CA    . ILE D 4  128  ? 96.604  100.400 146.561 1.00 21.26  ? 128  ILE D CA    1 
ATOM   24362 C  C     . ILE D 4  128  ? 96.741  99.262  145.566 1.00 21.28  ? 128  ILE D C     1 
ATOM   24363 O  O     . ILE D 4  128  ? 97.588  98.382  145.725 1.00 21.48  ? 128  ILE D O     1 
ATOM   24364 C  CB    . ILE D 4  128  ? 97.233  101.716 146.038 1.00 20.89  ? 128  ILE D CB    1 
ATOM   24365 C  CG1   . ILE D 4  128  ? 96.385  102.330 144.931 1.00 20.50  ? 128  ILE D CG1   1 
ATOM   24366 C  CG2   . ILE D 4  128  ? 98.651  101.485 145.585 1.00 22.12  ? 128  ILE D CG2   1 
ATOM   24367 C  CD1   . ILE D 4  128  ? 96.912  103.645 144.454 1.00 23.03  ? 128  ILE D CD1   1 
ATOM   24368 N  N     . ASN D 4  129  ? 95.883  99.257  144.554 1.00 21.43  ? 129  ASN D N     1 
ATOM   24369 C  CA    . ASN D 4  129  ? 96.066  98.333  143.443 1.00 20.01  ? 129  ASN D CA    1 
ATOM   24370 C  C     . ASN D 4  129  ? 97.180  98.846  142.538 1.00 22.17  ? 129  ASN D C     1 
ATOM   24371 O  O     . ASN D 4  129  ? 96.943  99.688  141.671 1.00 21.76  ? 129  ASN D O     1 
ATOM   24372 C  CB    . ASN D 4  129  ? 94.763  98.160  142.672 1.00 16.51  ? 129  ASN D CB    1 
ATOM   24373 C  CG    . ASN D 4  129  ? 94.717  96.885  141.890 1.00 21.88  ? 129  ASN D CG    1 
ATOM   24374 O  OD1   . ASN D 4  129  ? 95.742  96.326  141.537 1.00 24.58  ? 129  ASN D OD1   1 
ATOM   24375 N  ND2   . ASN D 4  129  ? 93.517  96.403  141.622 1.00 24.28  ? 129  ASN D ND2   1 
ATOM   24376 N  N     . ILE D 4  130  ? 98.400  98.338  142.750 1.00 18.67  ? 130  ILE D N     1 
ATOM   24377 C  CA    . ILE D 4  130  ? 99.572  98.913  142.083 1.00 12.35  ? 130  ILE D CA    1 
ATOM   24378 C  C     . ILE D 4  130  ? 99.489  98.826  140.566 1.00 17.56  ? 130  ILE D C     1 
ATOM   24379 O  O     . ILE D 4  130  ? 99.796  99.822  139.897 1.00 19.87  ? 130  ILE D O     1 
ATOM   24380 C  CB    . ILE D 4  130  ? 100.856 98.295  142.652 1.00 13.17  ? 130  ILE D CB    1 
ATOM   24381 C  CG1   . ILE D 4  130  ? 101.194 98.907  144.014 1.00 13.13  ? 130  ILE D CG1   1 
ATOM   24382 C  CG2   . ILE D 4  130  ? 102.003 98.438  141.680 1.00 18.30  ? 130  ILE D CG2   1 
ATOM   24383 C  CD1   . ILE D 4  130  ? 101.745 100.287 143.947 1.00 10.38  ? 130  ILE D CD1   1 
ATOM   24384 N  N     . PRO D 4  131  ? 99.108  97.704  139.952 1.00 13.37  ? 131  PRO D N     1 
ATOM   24385 C  CA    . PRO D 4  131  ? 99.062  97.670  138.485 1.00 12.54  ? 131  PRO D CA    1 
ATOM   24386 C  C     . PRO D 4  131  ? 98.072  98.635  137.864 1.00 19.52  ? 131  PRO D C     1 
ATOM   24387 O  O     . PRO D 4  131  ? 98.165  98.889  136.660 1.00 28.26  ? 131  PRO D O     1 
ATOM   24388 C  CB    . PRO D 4  131  ? 98.689  96.217  138.187 1.00 16.92  ? 131  PRO D CB    1 
ATOM   24389 C  CG    . PRO D 4  131  ? 99.168  95.483  139.339 1.00 13.18  ? 131  PRO D CG    1 
ATOM   24390 C  CD    . PRO D 4  131  ? 98.936  96.354  140.507 1.00 12.93  ? 131  PRO D CD    1 
ATOM   24391 N  N     . LYS D 4  132  ? 97.120  99.168  138.620 1.00 15.92  ? 132  LYS D N     1 
ATOM   24392 C  CA    . LYS D 4  132  ? 96.130  100.071 138.053 1.00 12.25  ? 132  LYS D CA    1 
ATOM   24393 C  C     . LYS D 4  132  ? 96.479  101.540 138.229 1.00 13.11  ? 132  LYS D C     1 
ATOM   24394 O  O     . LYS D 4  132  ? 95.706  102.396 137.800 1.00 16.42  ? 132  LYS D O     1 
ATOM   24395 C  CB    . LYS D 4  132  ? 94.757  99.793  138.655 1.00 15.13  ? 132  LYS D CB    1 
ATOM   24396 C  CG    . LYS D 4  132  ? 94.178  98.459  138.263 1.00 13.42  ? 132  LYS D CG    1 
ATOM   24397 C  CD    . LYS D 4  132  ? 92.687  98.451  138.482 1.00 20.91  ? 132  LYS D CD    1 
ATOM   24398 C  CE    . LYS D 4  132  ? 92.144  97.045  138.597 1.00 22.90  ? 132  LYS D CE    1 
ATOM   24399 N  NZ    . LYS D 4  132  ? 91.852  96.454  137.271 1.00 23.85  ? 132  LYS D NZ    1 
ATOM   24400 N  N     . VAL D 4  133  ? 97.619  101.857 138.840 1.00 9.03   ? 133  VAL D N     1 
ATOM   24401 C  CA    . VAL D 4  133  ? 98.055  103.243 138.909 1.00 9.79   ? 133  VAL D CA    1 
ATOM   24402 C  C     . VAL D 4  133  ? 98.414  103.726 137.512 1.00 15.43  ? 133  VAL D C     1 
ATOM   24403 O  O     . VAL D 4  133  ? 99.059  103.015 136.734 1.00 21.99  ? 133  VAL D O     1 
ATOM   24404 C  CB    . VAL D 4  133  ? 99.236  103.380 139.880 1.00 10.97  ? 133  VAL D CB    1 
ATOM   24405 C  CG1   . VAL D 4  133  ? 99.775  104.787 139.869 1.00 14.33  ? 133  VAL D CG1   1 
ATOM   24406 C  CG2   . VAL D 4  133  ? 98.809  103.001 141.268 1.00 12.06  ? 133  VAL D CG2   1 
ATOM   24407 N  N     . SER D 4  134  ? 97.970  104.935 137.176 1.00 17.32  ? 134  SER D N     1 
ATOM   24408 C  CA    . SER D 4  134  ? 98.123  105.424 135.811 1.00 15.17  ? 134  SER D CA    1 
ATOM   24409 C  C     . SER D 4  134  ? 99.589  105.618 135.438 1.00 15.11  ? 134  SER D C     1 
ATOM   24410 O  O     . SER D 4  134  ? 99.992  105.306 134.315 1.00 19.33  ? 134  SER D O     1 
ATOM   24411 C  CB    . SER D 4  134  ? 97.338  106.723 135.631 1.00 14.66  ? 134  SER D CB    1 
ATOM   24412 O  OG    . SER D 4  134  ? 97.859  107.750 136.450 1.00 20.01  ? 134  SER D OG    1 
ATOM   24413 N  N     . ALA D 4  135  ? 100.399 106.127 136.362 1.00 12.23  ? 135  ALA D N     1 
ATOM   24414 C  CA    . ALA D 4  135  ? 101.791 106.444 136.079 1.00 5.76   ? 135  ALA D CA    1 
ATOM   24415 C  C     . ALA D 4  135  ? 102.655 105.223 135.815 1.00 11.23  ? 135  ALA D C     1 
ATOM   24416 O  O     . ALA D 4  135  ? 103.729 105.371 135.228 1.00 18.21  ? 135  ALA D O     1 
ATOM   24417 C  CB    . ALA D 4  135  ? 102.387 107.228 137.242 1.00 8.26   ? 135  ALA D CB    1 
ATOM   24418 N  N     . ILE D 4  136  ? 102.232 104.040 136.234 1.00 5.77   ? 136  ILE D N     1 
ATOM   24419 C  CA    . ILE D 4  136  ? 103.042 102.829 136.160 1.00 9.48   ? 136  ILE D CA    1 
ATOM   24420 C  C     . ILE D 4  136  ? 102.720 102.117 134.852 1.00 7.54   ? 136  ILE D C     1 
ATOM   24421 O  O     . ILE D 4  136  ? 101.558 101.756 134.636 1.00 10.59  ? 136  ILE D O     1 
ATOM   24422 C  CB    . ILE D 4  136  ? 102.780 101.912 137.362 1.00 9.44   ? 136  ILE D CB    1 
ATOM   24423 C  CG1   . ILE D 4  136  ? 103.185 102.612 138.656 1.00 11.06  ? 136  ILE D CG1   1 
ATOM   24424 C  CG2   . ILE D 4  136  ? 103.524 100.610 137.216 1.00 5.00   ? 136  ILE D CG2   1 
ATOM   24425 C  CD1   . ILE D 4  136  ? 102.961 101.791 139.882 1.00 8.58   ? 136  ILE D CD1   1 
ATOM   24426 N  N     . PRO D 4  137  ? 103.702 101.882 133.971 1.00 7.59   ? 137  PRO D N     1 
ATOM   24427 C  CA    . PRO D 4  137  ? 103.423 101.160 132.723 1.00 10.07  ? 137  PRO D CA    1 
ATOM   24428 C  C     . PRO D 4  137  ? 103.111 99.694  132.958 1.00 2.70   ? 137  PRO D C     1 
ATOM   24429 O  O     . PRO D 4  137  ? 103.163 99.221  134.091 1.00 15.81  ? 137  PRO D O     1 
ATOM   24430 C  CB    . PRO D 4  137  ? 104.719 101.328 131.926 1.00 11.26  ? 137  PRO D CB    1 
ATOM   24431 C  CG    . PRO D 4  137  ? 105.455 102.405 132.590 1.00 4.85   ? 137  PRO D CG    1 
ATOM   24432 C  CD    . PRO D 4  137  ? 105.096 102.342 134.020 1.00 6.63   ? 137  PRO D CD    1 
ATOM   24433 N  N     . LYS D 4  138  ? 102.808 98.955  131.902 1.00 2.38   ? 138  LYS D N     1 
ATOM   24434 C  CA    . LYS D 4  138  ? 102.434 97.555  132.027 1.00 3.50   ? 138  LYS D CA    1 
ATOM   24435 C  C     . LYS D 4  138  ? 103.684 96.688  132.090 1.00 6.33   ? 138  LYS D C     1 
ATOM   24436 O  O     . LYS D 4  138  ? 104.467 96.651  131.141 1.00 12.04  ? 138  LYS D O     1 
ATOM   24437 C  CB    . LYS D 4  138  ? 101.552 97.132  130.859 1.00 1.59   ? 138  LYS D CB    1 
ATOM   24438 C  CG    . LYS D 4  138  ? 100.210 96.622  131.276 1.00 9.61   ? 138  LYS D CG    1 
ATOM   24439 C  CD    . LYS D 4  138  ? 99.338  97.790  131.690 1.00 12.94  ? 138  LYS D CD    1 
ATOM   24440 C  CE    . LYS D 4  138  ? 98.189  97.362  132.572 1.00 10.79  ? 138  LYS D CE    1 
ATOM   24441 N  NZ    . LYS D 4  138  ? 97.621  98.525  133.282 1.00 6.97   ? 138  LYS D NZ    1 
ATOM   24442 N  N     . HIS D 4  139  ? 103.859 95.988  133.203 1.00 0.58   ? 139  HIS D N     1 
ATOM   24443 C  CA    . HIS D 4  139  ? 104.955 95.058  133.404 1.00 1.28   ? 139  HIS D CA    1 
ATOM   24444 C  C     . HIS D 4  139  ? 104.469 93.635  133.181 1.00 2.64   ? 139  HIS D C     1 
ATOM   24445 O  O     . HIS D 4  139  ? 103.313 93.311  133.440 1.00 10.05  ? 139  HIS D O     1 
ATOM   24446 C  CB    . HIS D 4  139  ? 105.527 95.195  134.810 1.00 2.97   ? 139  HIS D CB    1 
ATOM   24447 C  CG    . HIS D 4  139  ? 106.197 96.503  135.074 1.00 11.11  ? 139  HIS D CG    1 
ATOM   24448 N  ND1   . HIS D 4  139  ? 105.562 97.711  134.909 1.00 3.06   ? 139  HIS D ND1   1 
ATOM   24449 C  CD2   . HIS D 4  139  ? 107.431 96.789  135.541 1.00 1.71   ? 139  HIS D CD2   1 
ATOM   24450 C  CE1   . HIS D 4  139  ? 106.388 98.687  135.230 1.00 3.66   ? 139  HIS D CE1   1 
ATOM   24451 N  NE2   . HIS D 4  139  ? 107.527 98.154  135.623 1.00 5.14   ? 139  HIS D NE2   1 
ATOM   24452 N  N     . LYS D 4  140  ? 105.359 92.784  132.684 1.00 5.06   ? 140  LYS D N     1 
ATOM   24453 C  CA    . LYS D 4  140  ? 104.987 91.420  132.347 1.00 14.56  ? 140  LYS D CA    1 
ATOM   24454 C  C     . LYS D 4  140  ? 106.219 90.532  132.397 1.00 6.26   ? 140  LYS D C     1 
ATOM   24455 O  O     . LYS D 4  140  ? 107.268 90.882  131.861 1.00 15.83  ? 140  LYS D O     1 
ATOM   24456 C  CB    . LYS D 4  140  ? 104.339 91.373  130.964 1.00 13.04  ? 140  LYS D CB    1 
ATOM   24457 C  CG    . LYS D 4  140  ? 104.116 90.002  130.415 1.00 6.17   ? 140  LYS D CG    1 
ATOM   24458 C  CD    . LYS D 4  140  ? 103.157 90.045  129.254 1.00 11.53  ? 140  LYS D CD    1 
ATOM   24459 C  CE    . LYS D 4  140  ? 103.714 90.817  128.066 1.00 7.65   ? 140  LYS D CE    1 
ATOM   24460 N  NZ    . LYS D 4  140  ? 104.597 89.995  127.203 1.00 7.99   ? 140  LYS D NZ    1 
ATOM   24461 N  N     . LEU D 4  141  ? 106.085 89.375  133.030 1.00 3.66   ? 141  LEU D N     1 
ATOM   24462 C  CA    . LEU D 4  141  ? 107.182 88.424  133.142 1.00 6.04   ? 141  LEU D CA    1 
ATOM   24463 C  C     . LEU D 4  141  ? 107.208 87.526  131.915 1.00 9.38   ? 141  LEU D C     1 
ATOM   24464 O  O     . LEU D 4  141  ? 106.175 86.986  131.516 1.00 14.58  ? 141  LEU D O     1 
ATOM   24465 C  CB    . LEU D 4  141  ? 107.059 87.571  134.404 1.00 5.73   ? 141  LEU D CB    1 
ATOM   24466 C  CG    . LEU D 4  141  ? 107.330 88.231  135.752 1.00 10.20  ? 141  LEU D CG    1 
ATOM   24467 C  CD1   . LEU D 4  141  ? 107.134 87.225  136.849 1.00 12.04  ? 141  LEU D CD1   1 
ATOM   24468 C  CD2   . LEU D 4  141  ? 108.709 88.824  135.815 1.00 8.73   ? 141  LEU D CD2   1 
ATOM   24469 N  N     . ILE D 4  142  ? 108.387 87.359  131.329 1.00 5.75   ? 142  ILE D N     1 
ATOM   24470 C  CA    . ILE D 4  142  ? 108.567 86.499  130.169 1.00 14.43  ? 142  ILE D CA    1 
ATOM   24471 C  C     . ILE D 4  142  ? 109.453 85.328  130.562 1.00 20.30  ? 142  ILE D C     1 
ATOM   24472 O  O     . ILE D 4  142  ? 110.263 85.419  131.491 1.00 19.58  ? 142  ILE D O     1 
ATOM   24473 C  CB    . ILE D 4  142  ? 109.160 87.261  128.968 1.00 16.46  ? 142  ILE D CB    1 
ATOM   24474 C  CG1   . ILE D 4  142  ? 110.509 87.867  129.325 1.00 15.40  ? 142  ILE D CG1   1 
ATOM   24475 C  CG2   . ILE D 4  142  ? 108.212 88.348  128.520 1.00 14.44  ? 142  ILE D CG2   1 
ATOM   24476 C  CD1   . ILE D 4  142  ? 111.226 88.432  128.156 1.00 11.42  ? 142  ILE D CD1   1 
ATOM   24477 N  N     . THR D 4  143  ? 109.290 84.216  129.851 1.00 22.05  ? 143  THR D N     1 
ATOM   24478 C  CA    . THR D 4  143  ? 109.991 82.993  130.207 1.00 23.11  ? 143  THR D CA    1 
ATOM   24479 C  C     . THR D 4  143  ? 111.460 83.060  129.802 1.00 27.42  ? 143  THR D C     1 
ATOM   24480 O  O     . THR D 4  143  ? 111.892 83.940  129.059 1.00 31.31  ? 143  THR D O     1 
ATOM   24481 C  CB    . THR D 4  143  ? 109.341 81.781  129.549 1.00 25.15  ? 143  THR D CB    1 
ATOM   24482 O  OG1   . THR D 4  143  ? 109.478 81.874  128.135 1.00 23.54  ? 143  THR D OG1   1 
ATOM   24483 C  CG2   . THR D 4  143  ? 107.878 81.727  129.882 1.00 27.63  ? 143  THR D CG2   1 
ATOM   24484 N  N     . GLN D 4  144  ? 112.234 82.102  130.310 1.00 30.32  ? 144  GLN D N     1 
ATOM   24485 C  CA    . GLN D 4  144  ? 113.646 82.025  129.959 1.00 28.97  ? 144  GLN D CA    1 
ATOM   24486 C  C     . GLN D 4  144  ? 113.842 81.704  128.483 1.00 31.62  ? 144  GLN D C     1 
ATOM   24487 O  O     . GLN D 4  144  ? 114.869 82.062  127.904 1.00 34.62  ? 144  GLN D O     1 
ATOM   24488 C  CB    . GLN D 4  144  ? 114.341 80.975  130.821 1.00 27.23  ? 144  GLN D CB    1 
ATOM   24489 C  CG    . GLN D 4  144  ? 114.403 81.291  132.304 1.00 32.31  ? 144  GLN D CG    1 
ATOM   24490 C  CD    . GLN D 4  144  ? 115.363 82.414  132.648 1.00 32.01  ? 144  GLN D CD    1 
ATOM   24491 O  OE1   . GLN D 4  144  ? 114.978 83.412  133.253 1.00 27.44  ? 144  GLN D OE1   1 
ATOM   24492 N  NE2   . GLN D 4  144  ? 116.617 82.257  132.258 1.00 30.96  ? 144  GLN D NE2   1 
ATOM   24493 N  N     . GLU D 4  145  ? 112.876 81.036  127.856 1.00 27.95  ? 145  GLU D N     1 
ATOM   24494 C  CA    . GLU D 4  145  ? 113.018 80.684  126.448 1.00 28.99  ? 145  GLU D CA    1 
ATOM   24495 C  C     . GLU D 4  145  ? 112.846 81.894  125.536 1.00 35.62  ? 145  GLU D C     1 
ATOM   24496 O  O     . GLU D 4  145  ? 113.635 82.086  124.602 1.00 41.02  ? 145  GLU D O     1 
ATOM   24497 C  CB    . GLU D 4  145  ? 112.026 79.583  126.091 1.00 32.15  ? 145  GLU D CB    1 
ATOM   24498 C  CG    . GLU D 4  145  ? 112.417 78.222  126.650 1.00 34.20  ? 145  GLU D CG    1 
ATOM   24499 C  CD    . GLU D 4  145  ? 112.080 78.051  128.127 1.00 36.67  ? 145  GLU D CD    1 
ATOM   24500 O  OE1   . GLU D 4  145  ? 111.356 78.897  128.688 1.00 36.54  ? 145  GLU D OE1   1 
ATOM   24501 O  OE2   . GLU D 4  145  ? 112.559 77.070  128.734 1.00 37.53  ? 145  GLU D OE2   1 
ATOM   24502 N  N     . GLU D 4  146  ? 111.826 82.722  125.778 1.00 28.95  ? 146  GLU D N     1 
ATOM   24503 C  CA    . GLU D 4  146  ? 111.663 83.930  124.974 1.00 27.51  ? 146  GLU D CA    1 
ATOM   24504 C  C     . GLU D 4  146  ? 112.803 84.906  125.213 1.00 25.71  ? 146  GLU D C     1 
ATOM   24505 O  O     . GLU D 4  146  ? 113.287 85.549  124.276 1.00 31.09  ? 146  GLU D O     1 
ATOM   24506 C  CB    . GLU D 4  146  ? 110.327 84.602  125.271 1.00 26.16  ? 146  GLU D CB    1 
ATOM   24507 C  CG    . GLU D 4  146  ? 109.236 83.674  125.709 1.00 32.64  ? 146  GLU D CG    1 
ATOM   24508 C  CD    . GLU D 4  146  ? 107.870 84.329  125.674 1.00 37.39  ? 146  GLU D CD    1 
ATOM   24509 O  OE1   . GLU D 4  146  ? 107.158 84.289  126.702 1.00 31.44  ? 146  GLU D OE1   1 
ATOM   24510 O  OE2   . GLU D 4  146  ? 107.511 84.888  124.618 1.00 38.17  ? 146  GLU D OE2   1 
ATOM   24511 N  N     . ALA D 4  147  ? 113.233 85.038  126.465 1.00 18.83  ? 147  ALA D N     1 
ATOM   24512 C  CA    . ALA D 4  147  ? 114.374 85.887  126.773 1.00 17.70  ? 147  ALA D CA    1 
ATOM   24513 C  C     . ALA D 4  147  ? 115.631 85.390  126.081 1.00 18.99  ? 147  ALA D C     1 
ATOM   24514 O  O     . ALA D 4  147  ? 116.429 86.186  125.578 1.00 23.70  ? 147  ALA D O     1 
ATOM   24515 C  CB    . ALA D 4  147  ? 114.583 85.940  128.280 1.00 18.72  ? 147  ALA D CB    1 
ATOM   24516 N  N     . GLN D 4  148  ? 115.828 84.072  126.054 1.00 18.50  ? 148  GLN D N     1 
ATOM   24517 C  CA    . GLN D 4  148  ? 116.990 83.509  125.388 1.00 19.09  ? 148  GLN D CA    1 
ATOM   24518 C  C     . GLN D 4  148  ? 116.954 83.778  123.896 1.00 22.44  ? 148  GLN D C     1 
ATOM   24519 O  O     . GLN D 4  148  ? 117.975 84.120  123.296 1.00 22.64  ? 148  GLN D O     1 
ATOM   24520 C  CB    . GLN D 4  148  ? 117.067 82.013  125.663 1.00 22.10  ? 148  GLN D CB    1 
ATOM   24521 C  CG    . GLN D 4  148  ? 118.447 81.535  126.037 1.00 24.63  ? 148  GLN D CG    1 
ATOM   24522 C  CD    . GLN D 4  148  ? 119.099 82.411  127.081 1.00 30.76  ? 148  GLN D CD    1 
ATOM   24523 O  OE1   . GLN D 4  148  ? 118.584 82.569  128.186 1.00 27.45  ? 148  GLN D OE1   1 
ATOM   24524 N  NE2   . GLN D 4  148  ? 120.242 82.991  126.734 1.00 28.50  ? 148  GLN D NE2   1 
ATOM   24525 N  N     . GLU D 4  149  ? 115.791 83.623  123.274 1.00 23.57  ? 149  GLU D N     1 
ATOM   24526 C  CA    . GLU D 4  149  ? 115.706 83.878  121.843 1.00 20.20  ? 149  GLU D CA    1 
ATOM   24527 C  C     . GLU D 4  149  ? 115.948 85.352  121.530 1.00 21.98  ? 149  GLU D C     1 
ATOM   24528 O  O     . GLU D 4  149  ? 116.633 85.682  120.551 1.00 27.50  ? 149  GLU D O     1 
ATOM   24529 C  CB    . GLU D 4  149  ? 114.357 83.397  121.316 1.00 21.21  ? 149  GLU D CB    1 
ATOM   24530 C  CG    . GLU D 4  149  ? 113.874 84.095  120.073 1.00 27.59  ? 149  GLU D CG    1 
ATOM   24531 C  CD    . GLU D 4  149  ? 112.371 84.020  119.912 1.00 36.19  ? 149  GLU D CD    1 
ATOM   24532 O  OE1   . GLU D 4  149  ? 111.645 84.386  120.859 1.00 34.27  ? 149  GLU D OE1   1 
ATOM   24533 O  OE2   . GLU D 4  149  ? 111.915 83.587  118.834 1.00 36.60  ? 149  GLU D OE2   1 
ATOM   24534 N  N     . PHE D 4  150  ? 115.419 86.250  122.366 1.00 14.93  ? 150  PHE D N     1 
ATOM   24535 C  CA    . PHE D 4  150  ? 115.668 87.677  122.197 1.00 9.05   ? 150  PHE D CA    1 
ATOM   24536 C  C     . PHE D 4  150  ? 117.155 87.997  122.303 1.00 10.33  ? 150  PHE D C     1 
ATOM   24537 O  O     . PHE D 4  150  ? 117.726 88.652  121.425 1.00 6.39   ? 150  PHE D O     1 
ATOM   24538 C  CB    . PHE D 4  150  ? 114.863 88.460  123.238 1.00 8.95   ? 150  PHE D CB    1 
ATOM   24539 C  CG    . PHE D 4  150  ? 115.226 89.912  123.332 1.00 10.81  ? 150  PHE D CG    1 
ATOM   24540 C  CD1   . PHE D 4  150  ? 114.762 90.815  122.405 1.00 13.92  ? 150  PHE D CD1   1 
ATOM   24541 C  CD2   . PHE D 4  150  ? 116.023 90.375  124.357 1.00 8.39   ? 150  PHE D CD2   1 
ATOM   24542 C  CE1   . PHE D 4  150  ? 115.101 92.136  122.495 1.00 9.02   ? 150  PHE D CE1   1 
ATOM   24543 C  CE2   . PHE D 4  150  ? 116.355 91.693  124.444 1.00 5.69   ? 150  PHE D CE2   1 
ATOM   24544 C  CZ    . PHE D 4  150  ? 115.896 92.572  123.518 1.00 6.20   ? 150  PHE D CZ    1 
ATOM   24545 N  N     . LEU D 4  151  ? 117.808 87.511  123.360 1.00 14.16  ? 151  LEU D N     1 
ATOM   24546 C  CA    . LEU D 4  151  ? 119.223 87.802  123.559 1.00 5.48   ? 151  LEU D CA    1 
ATOM   24547 C  C     . LEU D 4  151  ? 120.084 87.176  122.473 1.00 6.44   ? 151  LEU D C     1 
ATOM   24548 O  O     . LEU D 4  151  ? 121.127 87.723  122.112 1.00 9.21   ? 151  LEU D O     1 
ATOM   24549 C  CB    . LEU D 4  151  ? 119.675 87.314  124.929 1.00 7.86   ? 151  LEU D CB    1 
ATOM   24550 C  CG    . LEU D 4  151  ? 119.066 87.947  126.172 1.00 9.30   ? 151  LEU D CG    1 
ATOM   24551 C  CD1   . LEU D 4  151  ? 119.434 87.133  127.381 1.00 6.30   ? 151  LEU D CD1   1 
ATOM   24552 C  CD2   . LEU D 4  151  ? 119.509 89.373  126.335 1.00 9.34   ? 151  LEU D CD2   1 
ATOM   24553 N  N     . GLY D 4  152  ? 119.685 86.015  121.964 1.00 10.45  ? 152  GLY D N     1 
ATOM   24554 C  CA    . GLY D 4  152  ? 120.431 85.402  120.885 1.00 8.98   ? 152  GLY D CA    1 
ATOM   24555 C  C     . GLY D 4  152  ? 120.335 86.177  119.589 1.00 9.48   ? 152  GLY D C     1 
ATOM   24556 O  O     . GLY D 4  152  ? 121.321 86.308  118.862 1.00 15.46  ? 152  GLY D O     1 
ATOM   24557 N  N     . ARG D 4  153  ? 119.149 86.688  119.270 1.00 7.29   ? 153  ARG D N     1 
ATOM   24558 C  CA    . ARG D 4  153  ? 119.034 87.541  118.092 1.00 4.78   ? 153  ARG D CA    1 
ATOM   24559 C  C     . ARG D 4  153  ? 119.807 88.840  118.272 1.00 9.02   ? 153  ARG D C     1 
ATOM   24560 O  O     . ARG D 4  153  ? 120.345 89.383  117.306 1.00 13.82  ? 153  ARG D O     1 
ATOM   24561 C  CB    . ARG D 4  153  ? 117.567 87.822  117.791 1.00 11.49  ? 153  ARG D CB    1 
ATOM   24562 C  CG    . ARG D 4  153  ? 117.305 88.470  116.456 1.00 6.24   ? 153  ARG D CG    1 
ATOM   24563 C  CD    . ARG D 4  153  ? 116.969 89.932  116.603 1.00 8.26   ? 153  ARG D CD    1 
ATOM   24564 N  NE    . ARG D 4  153  ? 116.829 90.586  115.310 1.00 2.90   ? 153  ARG D NE    1 
ATOM   24565 C  CZ    . ARG D 4  153  ? 116.943 91.891  115.116 1.00 8.17   ? 153  ARG D CZ    1 
ATOM   24566 N  NH1   . ARG D 4  153  ? 117.198 92.716  116.111 1.00 5.83   ? 153  ARG D NH1   1 
ATOM   24567 N  NH2   . ARG D 4  153  ? 116.792 92.379  113.893 1.00 6.15   ? 153  ARG D NH2   1 
ATOM   24568 N  N     . GLU D 4  154  ? 119.875 89.353  119.493 1.00 11.35  ? 154  GLU D N     1 
ATOM   24569 C  CA    . GLU D 4  154  ? 120.480 90.648  119.753 1.00 2.83   ? 154  GLU D CA    1 
ATOM   24570 C  C     . GLU D 4  154  ? 121.960 90.576  120.097 1.00 4.20   ? 154  GLU D C     1 
ATOM   24571 O  O     . GLU D 4  154  ? 122.585 91.626  120.245 1.00 8.18   ? 154  GLU D O     1 
ATOM   24572 C  CB    . GLU D 4  154  ? 119.737 91.342  120.891 1.00 1.57   ? 154  GLU D CB    1 
ATOM   24573 C  CG    . GLU D 4  154  ? 118.297 91.629  120.582 1.00 3.99   ? 154  GLU D CG    1 
ATOM   24574 C  CD    . GLU D 4  154  ? 118.100 92.921  119.840 1.00 11.62  ? 154  GLU D CD    1 
ATOM   24575 O  OE1   . GLU D 4  154  ? 118.679 93.946  120.245 1.00 8.38   ? 154  GLU D OE1   1 
ATOM   24576 O  OE2   . GLU D 4  154  ? 117.357 92.909  118.843 1.00 14.14  ? 154  GLU D OE2   1 
ATOM   24577 N  N     . TYR D 4  155  ? 122.528 89.379  120.228 1.00 5.44   ? 155  TYR D N     1 
ATOM   24578 C  CA    . TYR D 4  155  ? 123.934 89.187  120.595 1.00 2.09   ? 155  TYR D CA    1 
ATOM   24579 C  C     . TYR D 4  155  ? 124.263 89.870  121.920 1.00 1.96   ? 155  TYR D C     1 
ATOM   24580 O  O     . TYR D 4  155  ? 125.223 90.628  122.034 1.00 5.48   ? 155  TYR D O     1 
ATOM   24581 C  CB    . TYR D 4  155  ? 124.869 89.680  119.491 1.00 1.39   ? 155  TYR D CB    1 
ATOM   24582 C  CG    . TYR D 4  155  ? 125.156 88.671  118.417 1.00 2.96   ? 155  TYR D CG    1 
ATOM   24583 C  CD1   . TYR D 4  155  ? 126.030 87.627  118.639 1.00 6.72   ? 155  TYR D CD1   1 
ATOM   24584 C  CD2   . TYR D 4  155  ? 124.565 88.766  117.178 1.00 5.36   ? 155  TYR D CD2   1 
ATOM   24585 C  CE1   . TYR D 4  155  ? 126.295 86.703  117.662 1.00 2.69   ? 155  TYR D CE1   1 
ATOM   24586 C  CE2   . TYR D 4  155  ? 124.828 87.848  116.196 1.00 5.04   ? 155  TYR D CE2   1 
ATOM   24587 C  CZ    . TYR D 4  155  ? 125.693 86.820  116.443 1.00 4.71   ? 155  TYR D CZ    1 
ATOM   24588 O  OH    . TYR D 4  155  ? 125.949 85.906  115.457 1.00 13.40  ? 155  TYR D OH    1 
ATOM   24589 N  N     . LEU D 4  156  ? 123.459 89.579  122.936 1.00 2.49   ? 156  LEU D N     1 
ATOM   24590 C  CA    . LEU D 4  156  ? 123.568 90.211  124.239 1.00 4.02   ? 156  LEU D CA    1 
ATOM   24591 C  C     . LEU D 4  156  ? 123.662 89.158  125.331 1.00 11.71  ? 156  LEU D C     1 
ATOM   24592 O  O     . LEU D 4  156  ? 123.245 88.012  125.155 1.00 11.93  ? 156  LEU D O     1 
ATOM   24593 C  CB    . LEU D 4  156  ? 122.368 91.117  124.517 1.00 4.62   ? 156  LEU D CB    1 
ATOM   24594 C  CG    . LEU D 4  156  ? 122.268 92.472  123.823 1.00 5.16   ? 156  LEU D CG    1 
ATOM   24595 C  CD1   . LEU D 4  156  ? 120.908 93.068  124.062 1.00 4.78   ? 156  LEU D CD1   1 
ATOM   24596 C  CD2   . LEU D 4  156  ? 123.329 93.405  124.315 1.00 0.25   ? 156  LEU D CD2   1 
ATOM   24597 N  N     . GLN D 4  157  ? 124.210 89.543  126.415 1.00 9.18   ? 157  GLN D N     1 
ATOM   24598 C  CA    . GLN D 4  157  ? 124.232 88.852  127.689 1.00 6.10   ? 157  GLN D CA    1 
ATOM   24599 C  C     . GLN D 4  157  ? 123.193 89.452  128.625 1.00 14.14  ? 157  GLN D C     1 
ATOM   24600 O  O     . GLN D 4  157  ? 122.822 90.615  128.475 1.00 21.46  ? 157  GLN D O     1 
ATOM   24601 C  CB    . GLN D 4  157  ? 125.615 88.945  128.340 1.00 11.19  ? 157  GLN D CB    1 
ATOM   24602 C  CG    . GLN D 4  157  ? 126.751 88.405  127.497 1.00 11.70  ? 157  GLN D CG    1 
ATOM   24603 C  CD    . GLN D 4  157  ? 126.484 87.012  126.986 1.00 14.08  ? 157  GLN D CD    1 
ATOM   24604 O  OE1   . GLN D 4  157  ? 125.986 86.158  127.711 1.00 16.96  ? 157  GLN D OE1   1 
ATOM   24605 N  NE2   . GLN D 4  157  ? 126.799 86.777  125.723 1.00 17.69  ? 157  GLN D NE2   1 
ATOM   24606 N  N     . PRO D 4  158  ? 122.689 88.694  129.599 1.00 14.37  ? 158  PRO D N     1 
ATOM   24607 C  CA    . PRO D 4  158  ? 121.724 89.274  130.544 1.00 7.00   ? 158  PRO D CA    1 
ATOM   24608 C  C     . PRO D 4  158  ? 122.278 90.439  131.331 1.00 2.45   ? 158  PRO D C     1 
ATOM   24609 O  O     . PRO D 4  158  ? 121.503 91.259  131.827 1.00 6.84   ? 158  PRO D O     1 
ATOM   24610 C  CB    . PRO D 4  158  ? 121.382 88.092  131.455 1.00 9.94   ? 158  PRO D CB    1 
ATOM   24611 C  CG    . PRO D 4  158  ? 121.649 86.906  130.629 1.00 9.14   ? 158  PRO D CG    1 
ATOM   24612 C  CD    . PRO D 4  158  ? 122.818 87.241  129.778 1.00 11.40  ? 158  PRO D CD    1 
ATOM   24613 N  N     . GLN D 4  159  ? 123.593 90.543  131.455 1.00 6.87   ? 159  GLN D N     1 
ATOM   24614 C  CA    . GLN D 4  159  ? 124.233 91.622  132.187 1.00 11.66  ? 159  GLN D CA    1 
ATOM   24615 C  C     . GLN D 4  159  ? 124.335 92.909  131.381 1.00 11.95  ? 159  GLN D C     1 
ATOM   24616 O  O     . GLN D 4  159  ? 124.729 93.937  131.935 1.00 15.44  ? 159  GLN D O     1 
ATOM   24617 C  CB    . GLN D 4  159  ? 125.620 91.171  132.639 1.00 10.23  ? 159  GLN D CB    1 
ATOM   24618 C  CG    . GLN D 4  159  ? 125.607 90.157  133.770 1.00 15.01  ? 159  GLN D CG    1 
ATOM   24619 C  CD    . GLN D 4  159  ? 125.191 88.764  133.334 1.00 19.01  ? 159  GLN D CD    1 
ATOM   24620 O  OE1   . GLN D 4  159  ? 125.641 88.260  132.310 1.00 20.77  ? 159  GLN D OE1   1 
ATOM   24621 N  NE2   . GLN D 4  159  ? 124.345 88.128  134.129 1.00 18.11  ? 159  GLN D NE2   1 
ATOM   24622 N  N     . ASP D 4  160  ? 123.988 92.877  130.097 1.00 6.90   ? 160  ASP D N     1 
ATOM   24623 C  CA    . ASP D 4  160  ? 123.981 94.072  129.269 1.00 2.20   ? 160  ASP D CA    1 
ATOM   24624 C  C     . ASP D 4  160  ? 122.680 94.852  129.365 1.00 4.03   ? 160  ASP D C     1 
ATOM   24625 O  O     . ASP D 4  160  ? 122.677 96.053  129.091 1.00 5.17   ? 160  ASP D O     1 
ATOM   24626 C  CB    . ASP D 4  160  ? 124.232 93.697  127.812 1.00 0.16   ? 160  ASP D CB    1 
ATOM   24627 C  CG    . ASP D 4  160  ? 125.650 93.250  127.565 1.00 15.69  ? 160  ASP D CG    1 
ATOM   24628 O  OD1   . ASP D 4  160  ? 125.870 92.434  126.651 1.00 21.72  ? 160  ASP D OD1   1 
ATOM   24629 O  OD2   . ASP D 4  160  ? 126.554 93.715  128.284 1.00 16.99  ? 160  ASP D OD2   1 
ATOM   24630 N  N     . LEU D 4  161  ? 121.587 94.202  129.745 1.00 1.22   ? 161  LEU D N     1 
ATOM   24631 C  CA    . LEU D 4  161  ? 120.276 94.819  129.771 1.00 12.40  ? 161  LEU D CA    1 
ATOM   24632 C  C     . LEU D 4  161  ? 120.179 95.838  130.892 1.00 5.73   ? 161  LEU D C     1 
ATOM   24633 O  O     . LEU D 4  161  ? 120.960 95.825  131.841 1.00 15.13  ? 161  LEU D O     1 
ATOM   24634 C  CB    . LEU D 4  161  ? 119.196 93.759  129.955 1.00 2.46   ? 161  LEU D CB    1 
ATOM   24635 C  CG    . LEU D 4  161  ? 119.082 92.659  128.912 1.00 0.64   ? 161  LEU D CG    1 
ATOM   24636 C  CD1   . LEU D 4  161  ? 117.977 91.728  129.302 1.00 14.75  ? 161  LEU D CD1   1 
ATOM   24637 C  CD2   . LEU D 4  161  ? 118.833 93.248  127.545 1.00 0.79   ? 161  LEU D CD2   1 
ATOM   24638 N  N     . MET D 4  162  ? 119.202 96.734  130.777 1.00 0.87   ? 162  MET D N     1 
ATOM   24639 C  CA    . MET D 4  162  ? 118.830 97.545  131.922 1.00 0.18   ? 162  MET D CA    1 
ATOM   24640 C  C     . MET D 4  162  ? 118.290 96.645  133.022 1.00 2.40   ? 162  MET D C     1 
ATOM   24641 O  O     . MET D 4  162  ? 117.652 95.627  132.761 1.00 1.65   ? 162  MET D O     1 
ATOM   24642 C  CB    . MET D 4  162  ? 117.777 98.594  131.564 1.00 4.85   ? 162  MET D CB    1 
ATOM   24643 C  CG    . MET D 4  162  ? 118.179 99.664  130.564 1.00 1.27   ? 162  MET D CG    1 
ATOM   24644 S  SD    . MET D 4  162  ? 116.943 99.911  129.279 1.00 13.04  ? 162  MET D SD    1 
ATOM   24645 C  CE    . MET D 4  162  ? 117.703 99.124  127.879 1.00 5.43   ? 162  MET D CE    1 
ATOM   24646 N  N     . GLN D 4  163  ? 118.561 97.013  134.264 1.00 4.86   ? 163  GLN D N     1 
ATOM   24647 C  CA    . GLN D 4  163  ? 118.179 96.176  135.385 1.00 6.51   ? 163  GLN D CA    1 
ATOM   24648 C  C     . GLN D 4  163  ? 117.055 96.818  136.182 1.00 3.97   ? 163  GLN D C     1 
ATOM   24649 O  O     . GLN D 4  163  ? 116.808 98.018  136.089 1.00 3.77   ? 163  GLN D O     1 
ATOM   24650 C  CB    . GLN D 4  163  ? 119.377 95.863  136.284 1.00 1.20   ? 163  GLN D CB    1 
ATOM   24651 C  CG    . GLN D 4  163  ? 120.398 96.946  136.365 1.00 3.57   ? 163  GLN D CG    1 
ATOM   24652 C  CD    . GLN D 4  163  ? 121.789 96.414  136.606 1.00 7.07   ? 163  GLN D CD    1 
ATOM   24653 O  OE1   . GLN D 4  163  ? 122.016 95.212  136.596 1.00 7.31   ? 163  GLN D OE1   1 
ATOM   24654 N  NE2   . GLN D 4  163  ? 122.732 97.313  136.814 1.00 10.10  ? 163  GLN D NE2   1 
ATOM   24655 N  N     . ILE D 4  164  ? 116.340 95.984  136.921 1.00 9.92   ? 164  ILE D N     1 
ATOM   24656 C  CA    . ILE D 4  164  ? 115.246 96.414  137.776 1.00 9.23   ? 164  ILE D CA    1 
ATOM   24657 C  C     . ILE D 4  164  ? 115.338 95.639  139.081 1.00 3.82   ? 164  ILE D C     1 
ATOM   24658 O  O     . ILE D 4  164  ? 115.708 94.462  139.089 1.00 9.94   ? 164  ILE D O     1 
ATOM   24659 C  CB    . ILE D 4  164  ? 113.881 96.215  137.082 1.00 4.53   ? 164  ILE D CB    1 
ATOM   24660 C  CG1   . ILE D 4  164  ? 112.796 97.024  137.773 1.00 3.79   ? 164  ILE D CG1   1 
ATOM   24661 C  CG2   . ILE D 4  164  ? 113.510 94.758  136.981 1.00 1.37   ? 164  ILE D CG2   1 
ATOM   24662 C  CD1   . ILE D 4  164  ? 111.565 97.131  136.968 1.00 6.44   ? 164  ILE D CD1   1 
ATOM   24663 N  N     . SER D 4  165  ? 115.047 96.305  140.189 1.00 7.15   ? 165  SER D N     1 
ATOM   24664 C  CA    . SER D 4  165  ? 115.108 95.636  141.477 1.00 11.65  ? 165  SER D CA    1 
ATOM   24665 C  C     . SER D 4  165  ? 113.935 94.687  141.660 1.00 14.91  ? 165  SER D C     1 
ATOM   24666 O  O     . SER D 4  165  ? 112.825 94.933  141.186 1.00 18.97  ? 165  SER D O     1 
ATOM   24667 C  CB    . SER D 4  165  ? 115.126 96.649  142.610 1.00 10.34  ? 165  SER D CB    1 
ATOM   24668 O  OG    . SER D 4  165  ? 115.416 96.000  143.826 1.00 15.02  ? 165  SER D OG    1 
ATOM   24669 N  N     . ALA D 4  166  ? 114.191 93.588  142.365 1.00 11.78  ? 166  ALA D N     1 
ATOM   24670 C  CA    . ALA D 4  166  ? 113.145 92.616  142.637 1.00 8.44   ? 166  ALA D CA    1 
ATOM   24671 C  C     . ALA D 4  166  ? 112.112 93.128  143.625 1.00 19.13  ? 166  ALA D C     1 
ATOM   24672 O  O     . ALA D 4  166  ? 111.041 92.527  143.737 1.00 23.91  ? 166  ALA D O     1 
ATOM   24673 C  CB    . ALA D 4  166  ? 113.755 91.319  143.156 1.00 13.12  ? 166  ALA D CB    1 
ATOM   24674 N  N     . SER D 4  167  ? 112.403 94.215  144.333 1.00 17.05  ? 167  SER D N     1 
ATOM   24675 C  CA    . SER D 4  167  ? 111.466 94.849  145.244 1.00 15.93  ? 167  SER D CA    1 
ATOM   24676 C  C     . SER D 4  167  ? 110.806 96.077  144.633 1.00 16.84  ? 167  SER D C     1 
ATOM   24677 O  O     . SER D 4  167  ? 110.253 96.902  145.364 1.00 19.38  ? 167  SER D O     1 
ATOM   24678 C  CB    . SER D 4  167  ? 112.166 95.216  146.547 1.00 19.25  ? 167  SER D CB    1 
ATOM   24679 O  OG    . SER D 4  167  ? 112.998 96.340  146.372 1.00 21.89  ? 167  SER D OG    1 
ATOM   24680 N  N     . ASP D 4  168  ? 110.889 96.231  143.323 1.00 15.59  ? 168  ASP D N     1 
ATOM   24681 C  CA    . ASP D 4  168  ? 110.125 97.255  142.628 1.00 16.58  ? 168  ASP D CA    1 
ATOM   24682 C  C     . ASP D 4  168  ? 108.642 96.916  142.719 1.00 18.72  ? 168  ASP D C     1 
ATOM   24683 O  O     . ASP D 4  168  ? 108.268 95.766  142.480 1.00 18.92  ? 168  ASP D O     1 
ATOM   24684 C  CB    . ASP D 4  168  ? 110.569 97.327  141.171 1.00 13.85  ? 168  ASP D CB    1 
ATOM   24685 C  CG    . ASP D 4  168  ? 110.540 98.727  140.615 1.00 16.47  ? 168  ASP D CG    1 
ATOM   24686 O  OD1   . ASP D 4  168  ? 111.336 99.566  141.072 1.00 22.30  ? 168  ASP D OD1   1 
ATOM   24687 O  OD2   . ASP D 4  168  ? 109.740 98.981  139.700 1.00 17.47  ? 168  ASP D OD2   1 
ATOM   24688 N  N     . PRO D 4  169  ? 107.778 97.877  143.038 1.00 16.40  ? 169  PRO D N     1 
ATOM   24689 C  CA    . PRO D 4  169  ? 106.369 97.569  143.326 1.00 11.03  ? 169  PRO D CA    1 
ATOM   24690 C  C     . PRO D 4  169  ? 105.692 96.748  142.240 1.00 9.41   ? 169  PRO D C     1 
ATOM   24691 O  O     . PRO D 4  169  ? 105.047 95.737  142.559 1.00 16.45  ? 169  PRO D O     1 
ATOM   24692 C  CB    . PRO D 4  169  ? 105.737 98.957  143.474 1.00 9.41   ? 169  PRO D CB    1 
ATOM   24693 C  CG    . PRO D 4  169  ? 106.842 99.795  143.966 1.00 11.20  ? 169  PRO D CG    1 
ATOM   24694 C  CD    . PRO D 4  169  ? 108.101 99.277  143.353 1.00 12.18  ? 169  PRO D CD    1 
ATOM   24695 N  N     . PRO D 4  170  ? 105.786 97.124  140.957 1.00 19.05  ? 170  PRO D N     1 
ATOM   24696 C  CA    . PRO D 4  170  ? 105.162 96.274  139.933 1.00 14.91  ? 170  PRO D CA    1 
ATOM   24697 C  C     . PRO D 4  170  ? 105.745 94.877  139.871 1.00 15.36  ? 170  PRO D C     1 
ATOM   24698 O  O     . PRO D 4  170  ? 105.007 93.915  139.634 1.00 18.91  ? 170  PRO D O     1 
ATOM   24699 C  CB    . PRO D 4  170  ? 105.417 97.046  138.636 1.00 9.45   ? 170  PRO D CB    1 
ATOM   24700 C  CG    . PRO D 4  170  ? 105.722 98.397  139.056 1.00 7.57   ? 170  PRO D CG    1 
ATOM   24701 C  CD    . PRO D 4  170  ? 106.440 98.279  140.318 1.00 11.44  ? 170  PRO D CD    1 
ATOM   24702 N  N     . VAL D 4  171  ? 107.053 94.738  140.080 1.00 14.49  ? 171  VAL D N     1 
ATOM   24703 C  CA    . VAL D 4  171  ? 107.687 93.428  140.072 1.00 13.30  ? 171  VAL D CA    1 
ATOM   24704 C  C     . VAL D 4  171  ? 107.269 92.616  141.288 1.00 15.08  ? 171  VAL D C     1 
ATOM   24705 O  O     . VAL D 4  171  ? 107.114 91.395  141.198 1.00 20.41  ? 171  VAL D O     1 
ATOM   24706 C  CB    . VAL D 4  171  ? 109.217 93.591  139.974 1.00 15.20  ? 171  VAL D CB    1 
ATOM   24707 C  CG1   . VAL D 4  171  ? 109.886 92.256  139.812 1.00 11.14  ? 171  VAL D CG1   1 
ATOM   24708 C  CG2   . VAL D 4  171  ? 109.563 94.475  138.800 1.00 12.82  ? 171  VAL D CG2   1 
ATOM   24709 N  N     . VAL D 4  172  ? 107.096 93.263  142.443 1.00 16.94  ? 172  VAL D N     1 
ATOM   24710 C  CA    . VAL D 4  172  ? 106.583 92.564  143.619 1.00 13.97  ? 172  VAL D CA    1 
ATOM   24711 C  C     . VAL D 4  172  ? 105.187 92.028  143.354 1.00 10.88  ? 172  VAL D C     1 
ATOM   24712 O  O     . VAL D 4  172  ? 104.871 90.885  143.695 1.00 14.77  ? 172  VAL D O     1 
ATOM   24713 C  CB    . VAL D 4  172  ? 106.594 93.485  144.848 1.00 12.27  ? 172  VAL D CB    1 
ATOM   24714 C  CG1   . VAL D 4  172  ? 106.004 92.761  146.035 1.00 11.67  ? 172  VAL D CG1   1 
ATOM   24715 C  CG2   . VAL D 4  172  ? 107.988 93.933  145.155 1.00 13.60  ? 172  VAL D CG2   1 
ATOM   24716 N  N     . TRP D 4  173  ? 104.324 92.845  142.756 1.00 11.63  ? 173  TRP D N     1 
ATOM   24717 C  CA    . TRP D 4  173  ? 102.990 92.361  142.437 1.00 12.43  ? 173  TRP D CA    1 
ATOM   24718 C  C     . TRP D 4  173  ? 103.022 91.271  141.380 1.00 15.94  ? 173  TRP D C     1 
ATOM   24719 O  O     . TRP D 4  173  ? 102.107 90.449  141.320 1.00 18.03  ? 173  TRP D O     1 
ATOM   24720 C  CB    . TRP D 4  173  ? 102.107 93.512  141.982 1.00 14.70  ? 173  TRP D CB    1 
ATOM   24721 C  CG    . TRP D 4  173  ? 101.486 94.248  143.111 1.00 18.59  ? 173  TRP D CG    1 
ATOM   24722 C  CD1   . TRP D 4  173  ? 102.129 94.996  144.038 1.00 16.76  ? 173  TRP D CD1   1 
ATOM   24723 C  CD2   . TRP D 4  173  ? 100.098 94.312  143.435 1.00 18.52  ? 173  TRP D CD2   1 
ATOM   24724 N  NE1   . TRP D 4  173  ? 101.236 95.525  144.922 1.00 16.88  ? 173  TRP D NE1   1 
ATOM   24725 C  CE2   . TRP D 4  173  ? 99.977  95.119  144.573 1.00 18.64  ? 173  TRP D CE2   1 
ATOM   24726 C  CE3   . TRP D 4  173  ? 98.944  93.762  142.875 1.00 15.26  ? 173  TRP D CE3   1 
ATOM   24727 C  CZ2   . TRP D 4  173  ? 98.754  95.396  145.160 1.00 18.45  ? 173  TRP D CZ2   1 
ATOM   24728 C  CZ3   . TRP D 4  173  ? 97.735  94.042  143.455 1.00 15.84  ? 173  TRP D CZ3   1 
ATOM   24729 C  CH2   . TRP D 4  173  ? 97.646  94.850  144.586 1.00 14.37  ? 173  TRP D CH2   1 
ATOM   24730 N  N     . LEU D 4  174  ? 104.040 91.260  140.521 1.00 17.91  ? 174  LEU D N     1 
ATOM   24731 C  CA    . LEU D 4  174  ? 104.160 90.191  139.537 1.00 11.95  ? 174  LEU D CA    1 
ATOM   24732 C  C     . LEU D 4  174  ? 104.694 88.898  140.133 1.00 16.24  ? 174  LEU D C     1 
ATOM   24733 O  O     . LEU D 4  174  ? 104.298 87.816  139.699 1.00 19.18  ? 174  LEU D O     1 
ATOM   24734 C  CB    . LEU D 4  174  ? 105.067 90.626  138.393 1.00 12.95  ? 174  LEU D CB    1 
ATOM   24735 C  CG    . LEU D 4  174  ? 104.478 91.413  137.233 1.00 12.19  ? 174  LEU D CG    1 
ATOM   24736 C  CD1   . LEU D 4  174  ? 105.614 91.968  136.426 1.00 13.07  ? 174  LEU D CD1   1 
ATOM   24737 C  CD2   . LEU D 4  174  ? 103.616 90.523  136.388 1.00 9.06   ? 174  LEU D CD2   1 
ATOM   24738 N  N     . GLY D 4  175  ? 105.594 88.982  141.103 1.00 18.35  ? 175  GLY D N     1 
ATOM   24739 C  CA    . GLY D 4  175  ? 106.196 87.800  141.678 1.00 18.16  ? 175  GLY D CA    1 
ATOM   24740 C  C     . GLY D 4  175  ? 107.512 87.439  141.031 1.00 22.04  ? 175  GLY D C     1 
ATOM   24741 O  O     . GLY D 4  175  ? 107.856 86.262  140.926 1.00 26.67  ? 175  GLY D O     1 
ATOM   24742 N  N     . GLY D 4  176  ? 108.261 88.449  140.604 1.00 20.47  ? 176  GLY D N     1 
ATOM   24743 C  CA    . GLY D 4  176  ? 109.482 88.236  139.858 1.00 17.99  ? 176  GLY D CA    1 
ATOM   24744 C  C     . GLY D 4  176  ? 110.717 88.097  140.714 1.00 24.00  ? 176  GLY D C     1 
ATOM   24745 O  O     . GLY D 4  176  ? 110.975 88.924  141.590 1.00 25.63  ? 176  GLY D O     1 
ATOM   24746 N  N     . ARG D 4  177  ? 111.471 87.083  140.466 1.00 26.91  ? 177  ARG D N     1 
ATOM   24747 C  CA    . ARG D 4  177  ? 112.658 86.650  141.179 1.00 21.13  ? 177  ARG D CA    1 
ATOM   24748 C  C     . ARG D 4  177  ? 113.917 87.120  140.468 1.00 25.64  ? 177  ARG D C     1 
ATOM   24749 O  O     . ARG D 4  177  ? 113.907 87.328  139.255 1.00 29.57  ? 177  ARG D O     1 
ATOM   24750 C  CB    . ARG D 4  177  ? 112.676 85.134  141.286 1.00 23.76  ? 177  ARG D CB    1 
ATOM   24751 C  CG    . ARG D 4  177  ? 111.426 84.555  141.901 1.00 26.43  ? 177  ARG D CG    1 
ATOM   24752 C  CD    . ARG D 4  177  ? 111.449 84.713  143.404 1.00 29.20  ? 177  ARG D CD    1 
ATOM   24753 N  NE    . ARG D 4  177  ? 110.619 85.814  143.870 1.00 29.16  ? 177  ARG D NE    1 
ATOM   24754 C  CZ    . ARG D 4  177  ? 109.482 85.656  144.533 1.00 31.85  ? 177  ARG D CZ    1 
ATOM   24755 N  NH1   . ARG D 4  177  ? 109.003 84.455  144.805 1.00 26.83  ? 177  ARG D NH1   1 
ATOM   24756 N  NH2   . ARG D 4  177  ? 108.806 86.729  144.928 1.00 30.97  ? 177  ARG D NH2   1 
ATOM   24757 N  N     . PRO D 4  178  ? 115.015 87.316  141.193 1.00 20.47  ? 178  PRO D N     1 
ATOM   24758 C  CA    . PRO D 4  178  ? 116.275 87.668  140.532 1.00 17.62  ? 178  PRO D CA    1 
ATOM   24759 C  C     . PRO D 4  178  ? 116.716 86.598  139.547 1.00 18.89  ? 178  PRO D C     1 
ATOM   24760 O  O     . PRO D 4  178  ? 116.557 85.400  139.787 1.00 25.22  ? 178  PRO D O     1 
ATOM   24761 C  CB    . PRO D 4  178  ? 117.253 87.805  141.696 1.00 18.38  ? 178  PRO D CB    1 
ATOM   24762 C  CG    . PRO D 4  178  ? 116.402 88.187  142.830 1.00 20.11  ? 178  PRO D CG    1 
ATOM   24763 C  CD    . PRO D 4  178  ? 115.118 87.444  142.652 1.00 20.81  ? 178  PRO D CD    1 
ATOM   24764 N  N     . GLY D 4  179  ? 117.279 87.045  138.430 1.00 15.36  ? 179  GLY D N     1 
ATOM   24765 C  CA    . GLY D 4  179  ? 117.596 86.178  137.322 1.00 18.40  ? 179  GLY D CA    1 
ATOM   24766 C  C     . GLY D 4  179  ? 116.500 86.072  136.291 1.00 20.97  ? 179  GLY D C     1 
ATOM   24767 O  O     . GLY D 4  179  ? 116.661 85.337  135.314 1.00 26.02  ? 179  GLY D O     1 
ATOM   24768 N  N     . ASP D 4  180  ? 115.394 86.777  136.490 1.00 17.83  ? 180  ASP D N     1 
ATOM   24769 C  CA    . ASP D 4  180  ? 114.260 86.782  135.584 1.00 12.56  ? 180  ASP D CA    1 
ATOM   24770 C  C     . ASP D 4  180  ? 114.264 88.043  134.728 1.00 12.48  ? 180  ASP D C     1 
ATOM   24771 O  O     . ASP D 4  180  ? 115.024 88.981  134.957 1.00 15.88  ? 180  ASP D O     1 
ATOM   24772 C  CB    . ASP D 4  180  ? 112.955 86.704  136.366 1.00 19.40  ? 180  ASP D CB    1 
ATOM   24773 C  CG    . ASP D 4  180  ? 112.533 85.296  136.667 1.00 26.67  ? 180  ASP D CG    1 
ATOM   24774 O  OD1   . ASP D 4  180  ? 111.329 85.087  136.915 1.00 25.13  ? 180  ASP D OD1   1 
ATOM   24775 O  OD2   . ASP D 4  180  ? 113.398 84.400  136.676 1.00 30.13  ? 180  ASP D OD2   1 
ATOM   24776 N  N     . PHE D 4  181  ? 113.363 88.068  133.752 1.00 8.95   ? 181  PHE D N     1 
ATOM   24777 C  CA    . PHE D 4  181  ? 113.238 89.161  132.800 1.00 8.29   ? 181  PHE D CA    1 
ATOM   24778 C  C     . PHE D 4  181  ? 111.815 89.693  132.835 1.00 4.79   ? 181  PHE D C     1 
ATOM   24779 O  O     . PHE D 4  181  ? 110.870 88.919  132.978 1.00 13.22  ? 181  PHE D O     1 
ATOM   24780 C  CB    . PHE D 4  181  ? 113.582 88.696  131.385 1.00 10.23  ? 181  PHE D CB    1 
ATOM   24781 C  CG    . PHE D 4  181  ? 114.918 88.040  131.269 1.00 10.37  ? 181  PHE D CG    1 
ATOM   24782 C  CD1   . PHE D 4  181  ? 115.078 86.708  131.581 1.00 15.63  ? 181  PHE D CD1   1 
ATOM   24783 C  CD2   . PHE D 4  181  ? 116.018 88.754  130.857 1.00 9.99   ? 181  PHE D CD2   1 
ATOM   24784 C  CE1   . PHE D 4  181  ? 116.298 86.106  131.477 1.00 10.69  ? 181  PHE D CE1   1 
ATOM   24785 C  CE2   . PHE D 4  181  ? 117.239 88.150  130.753 1.00 9.64   ? 181  PHE D CE2   1 
ATOM   24786 C  CZ    . PHE D 4  181  ? 117.376 86.825  131.063 1.00 6.30   ? 181  PHE D CZ    1 
ATOM   24787 N  N     . VAL D 4  182  ? 111.659 91.006  132.711 1.00 4.70   ? 182  VAL D N     1 
ATOM   24788 C  CA    . VAL D 4  182  ? 110.346 91.641  132.699 1.00 3.90   ? 182  VAL D CA    1 
ATOM   24789 C  C     . VAL D 4  182  ? 110.254 92.541  131.468 1.00 2.96   ? 182  VAL D C     1 
ATOM   24790 O  O     . VAL D 4  182  ? 111.164 93.330  131.198 1.00 3.18   ? 182  VAL D O     1 
ATOM   24791 C  CB    . VAL D 4  182  ? 110.075 92.413  134.004 1.00 14.40  ? 182  VAL D CB    1 
ATOM   24792 C  CG1   . VAL D 4  182  ? 111.169 93.391  134.301 1.00 1.52   ? 182  VAL D CG1   1 
ATOM   24793 C  CG2   . VAL D 4  182  ? 108.759 93.118  133.949 1.00 1.87   ? 182  VAL D CG2   1 
ATOM   24794 N  N     . GLN D 4  183  ? 109.166 92.401  130.713 1.00 0.69   ? 183  GLN D N     1 
ATOM   24795 C  CA    . GLN D 4  183  ? 108.916 93.206  129.523 1.00 0.83   ? 183  GLN D CA    1 
ATOM   24796 C  C     . GLN D 4  183  ? 107.899 94.296  129.826 1.00 1.76   ? 183  GLN D C     1 
ATOM   24797 O  O     . GLN D 4  183  ? 106.872 94.036  130.450 1.00 15.25  ? 183  GLN D O     1 
ATOM   24798 C  CB    . GLN D 4  183  ? 108.429 92.324  128.379 1.00 1.27   ? 183  GLN D CB    1 
ATOM   24799 C  CG    . GLN D 4  183  ? 107.737 93.062  127.268 1.00 3.60   ? 183  GLN D CG    1 
ATOM   24800 C  CD    . GLN D 4  183  ? 107.534 92.204  126.043 1.00 10.31  ? 183  GLN D CD    1 
ATOM   24801 O  OE1   . GLN D 4  183  ? 108.281 91.266  125.803 1.00 10.90  ? 183  GLN D OE1   1 
ATOM   24802 N  NE2   . GLN D 4  183  ? 106.492 92.494  125.285 1.00 10.00  ? 183  GLN D NE2   1 
ATOM   24803 N  N     . ILE D 4  184  ? 108.193 95.516  129.395 1.00 3.77   ? 184  ILE D N     1 
ATOM   24804 C  CA    . ILE D 4  184  ? 107.399 96.687  129.739 1.00 3.45   ? 184  ILE D CA    1 
ATOM   24805 C  C     . ILE D 4  184  ? 106.945 97.377  128.462 1.00 2.55   ? 184  ILE D C     1 
ATOM   24806 O  O     . ILE D 4  184  ? 107.758 97.649  127.577 1.00 4.49   ? 184  ILE D O     1 
ATOM   24807 C  CB    . ILE D 4  184  ? 108.195 97.649  130.637 1.00 1.34   ? 184  ILE D CB    1 
ATOM   24808 C  CG1   . ILE D 4  184  ? 108.771 96.881  131.819 1.00 1.21   ? 184  ILE D CG1   1 
ATOM   24809 C  CG2   . ILE D 4  184  ? 107.312 98.758  131.138 1.00 1.81   ? 184  ILE D CG2   1 
ATOM   24810 C  CD1   . ILE D 4  184  ? 109.947 97.510  132.450 1.00 4.52   ? 184  ILE D CD1   1 
ATOM   24811 N  N     . GLU D 4  185  ? 105.649 97.651  128.375 1.00 5.61   ? 185  GLU D N     1 
ATOM   24812 C  CA    . GLU D 4  185  ? 105.058 98.525  127.369 1.00 3.22   ? 185  GLU D CA    1 
ATOM   24813 C  C     . GLU D 4  185  ? 104.948 99.932  127.932 1.00 3.77   ? 185  GLU D C     1 
ATOM   24814 O  O     . GLU D 4  185  ? 104.250 100.148 128.922 1.00 18.25  ? 185  GLU D O     1 
ATOM   24815 C  CB    . GLU D 4  185  ? 103.679 98.016  126.960 1.00 4.78   ? 185  GLU D CB    1 
ATOM   24816 C  CG    . GLU D 4  185  ? 103.184 98.486  125.600 1.00 13.41  ? 185  GLU D CG    1 
ATOM   24817 C  CD    . GLU D 4  185  ? 103.278 97.458  124.502 1.00 21.52  ? 185  GLU D CD    1 
ATOM   24818 O  OE1   . GLU D 4  185  ? 103.948 97.760  123.493 1.00 15.92  ? 185  GLU D OE1   1 
ATOM   24819 O  OE2   . GLU D 4  185  ? 102.725 96.347  124.658 1.00 23.44  ? 185  GLU D OE2   1 
ATOM   24820 N  N     . ARG D 4  186  ? 105.633 100.884 127.318 1.00 3.19   ? 186  ARG D N     1 
ATOM   24821 C  CA    . ARG D 4  186  ? 105.562 102.200 127.920 1.00 5.91   ? 186  ARG D CA    1 
ATOM   24822 C  C     . ARG D 4  186  ? 105.147 103.261 126.916 1.00 5.48   ? 186  ARG D C     1 
ATOM   24823 O  O     . ARG D 4  186  ? 105.490 103.184 125.737 1.00 10.11  ? 186  ARG D O     1 
ATOM   24824 C  CB    . ARG D 4  186  ? 106.894 102.584 128.579 1.00 7.23   ? 186  ARG D CB    1 
ATOM   24825 C  CG    . ARG D 4  186  ? 108.096 102.714 127.709 1.00 1.67   ? 186  ARG D CG    1 
ATOM   24826 C  CD    . ARG D 4  186  ? 109.298 102.371 128.549 1.00 1.95   ? 186  ARG D CD    1 
ATOM   24827 N  NE    . ARG D 4  186  ? 110.559 102.733 127.922 1.00 8.96   ? 186  ARG D NE    1 
ATOM   24828 C  CZ    . ARG D 4  186  ? 111.732 102.712 128.536 1.00 7.29   ? 186  ARG D CZ    1 
ATOM   24829 N  NH1   . ARG D 4  186  ? 111.851 102.319 129.788 1.00 3.96   ? 186  ARG D NH1   1 
ATOM   24830 N  NH2   . ARG D 4  186  ? 112.813 103.092 127.874 1.00 4.94   ? 186  ARG D NH2   1 
ATOM   24831 N  N     . PRO D 4  187  ? 104.385 104.254 127.367 1.00 11.12  ? 187  PRO D N     1 
ATOM   24832 C  CA    . PRO D 4  187  ? 103.939 105.320 126.467 1.00 5.67   ? 187  PRO D CA    1 
ATOM   24833 C  C     . PRO D 4  187  ? 105.098 106.173 125.991 1.00 11.16  ? 187  PRO D C     1 
ATOM   24834 O  O     . PRO D 4  187  ? 106.035 106.455 126.736 1.00 14.29  ? 187  PRO D O     1 
ATOM   24835 C  CB    . PRO D 4  187  ? 102.980 106.136 127.338 1.00 7.97   ? 187  PRO D CB    1 
ATOM   24836 C  CG    . PRO D 4  187  ? 102.701 105.292 128.502 1.00 9.92   ? 187  PRO D CG    1 
ATOM   24837 C  CD    . PRO D 4  187  ? 103.886 104.459 128.728 1.00 9.27   ? 187  PRO D CD    1 
ATOM   24838 N  N     . SER D 4  188  ? 105.009 106.616 124.750 1.00 8.44   ? 188  SER D N     1 
ATOM   24839 C  CA    . SER D 4  188  ? 106.078 107.379 124.137 1.00 10.47  ? 188  SER D CA    1 
ATOM   24840 C  C     . SER D 4  188  ? 105.487 108.618 123.491 1.00 6.73   ? 188  SER D C     1 
ATOM   24841 O  O     . SER D 4  188  ? 104.436 108.548 122.855 1.00 11.53  ? 188  SER D O     1 
ATOM   24842 C  CB    . SER D 4  188  ? 106.830 106.523 123.107 1.00 13.80  ? 188  SER D CB    1 
ATOM   24843 O  OG    . SER D 4  188  ? 108.041 107.129 122.719 1.00 8.14   ? 188  SER D OG    1 
ATOM   24844 N  N     . GLU D 4  189  ? 106.148 109.751 123.668 1.00 7.77   ? 189  GLU D N     1 
ATOM   24845 C  CA    . GLU D 4  189  ? 105.740 110.976 123.003 1.00 8.38   ? 189  GLU D CA    1 
ATOM   24846 C  C     . GLU D 4  189  ? 106.435 111.169 121.670 1.00 10.29  ? 189  GLU D C     1 
ATOM   24847 O  O     . GLU D 4  189  ? 106.340 112.251 121.092 1.00 17.51  ? 189  GLU D O     1 
ATOM   24848 C  CB    . GLU D 4  189  ? 106.000 112.182 123.898 1.00 6.00   ? 189  GLU D CB    1 
ATOM   24849 C  CG    . GLU D 4  189  ? 105.522 111.979 125.312 1.00 13.42  ? 189  GLU D CG    1 
ATOM   24850 C  CD    . GLU D 4  189  ? 104.931 113.222 125.909 1.00 19.33  ? 189  GLU D CD    1 
ATOM   24851 O  OE1   . GLU D 4  189  ? 103.954 113.741 125.331 1.00 22.92  ? 189  GLU D OE1   1 
ATOM   24852 O  OE2   . GLU D 4  189  ? 105.428 113.677 126.958 1.00 21.53  ? 189  GLU D OE2   1 
ATOM   24853 N  N     . THR D 4  190  ? 107.139 110.152 121.185 1.00 15.11  ? 190  THR D N     1 
ATOM   24854 C  CA    . THR D 4  190  ? 107.811 110.166 119.897 1.00 3.66   ? 190  THR D CA    1 
ATOM   24855 C  C     . THR D 4  190  ? 107.342 109.061 118.967 1.00 6.58   ? 190  THR D C     1 
ATOM   24856 O  O     . THR D 4  190  ? 107.279 109.274 117.761 1.00 20.80  ? 190  THR D O     1 
ATOM   24857 C  CB    . THR D 4  190  ? 109.327 110.050 120.088 1.00 4.65   ? 190  THR D CB    1 
ATOM   24858 O  OG1   . THR D 4  190  ? 109.612 108.965 120.971 1.00 15.41  ? 190  THR D OG1   1 
ATOM   24859 C  CG2   . THR D 4  190  ? 109.898 111.314 120.681 1.00 4.86   ? 190  THR D CG2   1 
ATOM   24860 N  N     . ALA D 4  191  ? 107.008 107.882 119.487 1.00 2.58   ? 191  ALA D N     1 
ATOM   24861 C  CA    . ALA D 4  191  ? 106.561 106.764 118.670 1.00 3.35   ? 191  ALA D CA    1 
ATOM   24862 C  C     . ALA D 4  191  ? 105.241 106.164 119.134 1.00 9.16   ? 191  ALA D C     1 
ATOM   24863 O  O     . ALA D 4  191  ? 104.844 105.110 118.626 1.00 12.42  ? 191  ALA D O     1 
ATOM   24864 C  CB    . ALA D 4  191  ? 107.638 105.676 118.638 1.00 8.35   ? 191  ALA D CB    1 
ATOM   24865 N  N     . MET D 4  192  ? 104.583 106.793 120.104 1.00 10.70  ? 192  MET D N     1 
ATOM   24866 C  CA    . MET D 4  192  ? 103.291 106.457 120.700 1.00 8.03   ? 192  MET D CA    1 
ATOM   24867 C  C     . MET D 4  192  ? 103.327 105.244 121.626 1.00 10.77  ? 192  MET D C     1 
ATOM   24868 O  O     . MET D 4  192  ? 102.484 105.146 122.514 1.00 18.18  ? 192  MET D O     1 
ATOM   24869 C  CB    . MET D 4  192  ? 102.244 106.215 119.609 1.00 7.34   ? 192  MET D CB    1 
ATOM   24870 C  CG    . MET D 4  192  ? 100.814 106.131 120.103 1.00 7.98   ? 192  MET D CG    1 
ATOM   24871 S  SD    . MET D 4  192  ? 99.890  104.764 119.403 1.00 24.20  ? 192  MET D SD    1 
ATOM   24872 C  CE    . MET D 4  192  ? 99.810  105.244 117.695 1.00 7.52   ? 192  MET D CE    1 
ATOM   24873 N  N     . HIS D 4  193  ? 104.345 104.389 121.521 1.00 8.35   ? 193  HIS D N     1 
ATOM   24874 C  CA    . HIS D 4  193  ? 104.617 103.356 122.519 1.00 6.99   ? 193  HIS D CA    1 
ATOM   24875 C  C     . HIS D 4  193  ? 105.874 102.567 122.183 1.00 6.25   ? 193  HIS D C     1 
ATOM   24876 O  O     . HIS D 4  193  ? 106.254 102.457 121.018 1.00 13.20  ? 193  HIS D O     1 
ATOM   24877 C  CB    . HIS D 4  193  ? 103.428 102.405 122.718 1.00 8.31   ? 193  HIS D CB    1 
ATOM   24878 C  CG    . HIS D 4  193  ? 102.883 101.801 121.465 1.00 5.82   ? 193  HIS D CG    1 
ATOM   24879 N  ND1   . HIS D 4  193  ? 101.805 100.950 121.477 1.00 7.39   ? 193  HIS D ND1   1 
ATOM   24880 C  CD2   . HIS D 4  193  ? 103.267 101.903 120.175 1.00 6.78   ? 193  HIS D CD2   1 
ATOM   24881 C  CE1   . HIS D 4  193  ? 101.540 100.561 120.247 1.00 11.85  ? 193  HIS D CE1   1 
ATOM   24882 N  NE2   . HIS D 4  193  ? 102.413 101.126 119.437 1.00 14.09  ? 193  HIS D NE2   1 
ATOM   24883 N  N     . ALA D 4  194  ? 106.510 102.001 123.205 1.00 1.41   ? 194  ALA D N     1 
ATOM   24884 C  CA    . ALA D 4  194  ? 107.802 101.347 123.087 1.00 10.89  ? 194  ALA D CA    1 
ATOM   24885 C  C     . ALA D 4  194  ? 107.802 100.101 123.955 1.00 14.80  ? 194  ALA D C     1 
ATOM   24886 O  O     . ALA D 4  194  ? 106.996 99.966  124.869 1.00 8.61   ? 194  ALA D O     1 
ATOM   24887 C  CB    . ALA D 4  194  ? 108.933 102.286 123.504 1.00 5.55   ? 194  ALA D CB    1 
ATOM   24888 N  N     . VAL D 4  195  ? 108.702 99.174  123.657 1.00 1.77   ? 195  VAL D N     1 
ATOM   24889 C  CA    . VAL D 4  195  ? 108.866 97.959  124.446 1.00 9.17   ? 195  VAL D CA    1 
ATOM   24890 C  C     . VAL D 4  195  ? 110.324 97.845  124.872 1.00 1.83   ? 195  VAL D C     1 
ATOM   24891 O  O     . VAL D 4  195  ? 111.227 97.985  124.043 1.00 3.42   ? 195  VAL D O     1 
ATOM   24892 C  CB    . VAL D 4  195  ? 108.425 96.712  123.662 1.00 3.67   ? 195  VAL D CB    1 
ATOM   24893 C  CG1   . VAL D 4  195  ? 108.881 95.463  124.358 1.00 2.79   ? 195  VAL D CG1   1 
ATOM   24894 C  CG2   . VAL D 4  195  ? 106.942 96.675  123.521 1.00 15.13  ? 195  VAL D CG2   1 
ATOM   24895 N  N     . VAL D 4  196  ? 110.553 97.617  126.165 1.00 0.86   ? 196  VAL D N     1 
ATOM   24896 C  CA    . VAL D 4  196  ? 111.877 97.328  126.696 1.00 1.22   ? 196  VAL D CA    1 
ATOM   24897 C  C     . VAL D 4  196  ? 111.802 96.040  127.499 1.00 4.31   ? 196  VAL D C     1 
ATOM   24898 O  O     . VAL D 4  196  ? 110.731 95.581  127.881 1.00 0.43   ? 196  VAL D O     1 
ATOM   24899 C  CB    . VAL D 4  196  ? 112.446 98.469  127.561 1.00 0.41   ? 196  VAL D CB    1 
ATOM   24900 C  CG1   . VAL D 4  196  ? 112.645 99.707  126.732 1.00 7.65   ? 196  VAL D CG1   1 
ATOM   24901 C  CG2   . VAL D 4  196  ? 111.554 98.739  128.739 1.00 9.63   ? 196  VAL D CG2   1 
ATOM   24902 N  N     . ILE D 4  197  ? 112.964 95.436  127.713 1.00 3.53   ? 197  ILE D N     1 
ATOM   24903 C  CA    . ILE D 4  197  ? 113.103 94.237  128.524 1.00 14.83  ? 197  ILE D CA    1 
ATOM   24904 C  C     . ILE D 4  197  ? 114.178 94.498  129.566 1.00 1.42   ? 197  ILE D C     1 
ATOM   24905 O  O     . ILE D 4  197  ? 115.297 94.888  129.228 1.00 11.59  ? 197  ILE D O     1 
ATOM   24906 C  CB    . ILE D 4  197  ? 113.443 93.007  127.667 1.00 5.68   ? 197  ILE D CB    1 
ATOM   24907 C  CG1   . ILE D 4  197  ? 112.250 92.660  126.788 1.00 0.44   ? 197  ILE D CG1   1 
ATOM   24908 C  CG2   . ILE D 4  197  ? 113.755 91.825  128.541 1.00 0.77   ? 197  ILE D CG2   1 
ATOM   24909 C  CD1   . ILE D 4  197  ? 112.463 91.499  125.907 1.00 4.83   ? 197  ILE D CD1   1 
ATOM   24910 N  N     . ARG D 4  198  ? 113.833 94.304  130.829 1.00 7.76   ? 198  ARG D N     1 
ATOM   24911 C  CA    . ARG D 4  198  ? 114.727 94.557  131.942 1.00 2.18   ? 198  ARG D CA    1 
ATOM   24912 C  C     . ARG D 4  198  ? 115.075 93.249  132.634 1.00 10.29  ? 198  ARG D C     1 
ATOM   24913 O  O     . ARG D 4  198  ? 114.371 92.251  132.513 1.00 6.37   ? 198  ARG D O     1 
ATOM   24914 C  CB    . ARG D 4  198  ? 114.102 95.527  132.940 1.00 1.70   ? 198  ARG D CB    1 
ATOM   24915 C  CG    . ARG D 4  198  ? 114.159 96.958  132.509 1.00 5.96   ? 198  ARG D CG    1 
ATOM   24916 C  CD    . ARG D 4  198  ? 113.742 97.877  133.605 1.00 6.40   ? 198  ARG D CD    1 
ATOM   24917 N  NE    . ARG D 4  198  ? 113.997 99.265  133.259 1.00 13.43  ? 198  ARG D NE    1 
ATOM   24918 C  CZ    . ARG D 4  198  ? 114.987 99.994  133.747 1.00 15.69  ? 198  ARG D CZ    1 
ATOM   24919 N  NH1   . ARG D 4  198  ? 115.816 99.516  134.649 1.00 2.40   ? 198  ARG D NH1   1 
ATOM   24920 N  NH2   . ARG D 4  198  ? 115.135 101.242 133.332 1.00 14.36  ? 198  ARG D NH2   1 
ATOM   24921 N  N     . PHE D 4  199  ? 116.182 93.269  133.360 1.00 3.13   ? 199  PHE D N     1 
ATOM   24922 C  CA    . PHE D 4  199  ? 116.709 92.104  134.057 1.00 4.55   ? 199  PHE D CA    1 
ATOM   24923 C  C     . PHE D 4  199  ? 116.545 92.309  135.555 1.00 10.02  ? 199  PHE D C     1 
ATOM   24924 O  O     . PHE D 4  199  ? 116.971 93.334  136.087 1.00 7.05   ? 199  PHE D O     1 
ATOM   24925 C  CB    . PHE D 4  199  ? 118.174 91.896  133.691 1.00 2.48   ? 199  PHE D CB    1 
ATOM   24926 C  CG    . PHE D 4  199  ? 118.743 90.610  134.169 1.00 5.32   ? 199  PHE D CG    1 
ATOM   24927 C  CD1   . PHE D 4  199  ? 118.251 89.410  133.721 1.00 8.94   ? 199  PHE D CD1   1 
ATOM   24928 C  CD2   . PHE D 4  199  ? 119.790 90.604  135.062 1.00 5.40   ? 199  PHE D CD2   1 
ATOM   24929 C  CE1   . PHE D 4  199  ? 118.783 88.234  134.158 1.00 7.12   ? 199  PHE D CE1   1 
ATOM   24930 C  CE2   . PHE D 4  199  ? 120.320 89.432  135.500 1.00 7.20   ? 199  PHE D CE2   1 
ATOM   24931 C  CZ    . PHE D 4  199  ? 119.816 88.246  135.046 1.00 7.97   ? 199  PHE D CZ    1 
ATOM   24932 N  N     . ILE D 4  200  ? 115.937 91.338  136.232 1.00 7.13   ? 200  ILE D N     1 
ATOM   24933 C  CA    . ILE D 4  200  ? 115.613 91.487  137.648 1.00 10.43  ? 200  ILE D CA    1 
ATOM   24934 C  C     . ILE D 4  200  ? 116.839 91.139  138.477 1.00 4.15   ? 200  ILE D C     1 
ATOM   24935 O  O     . ILE D 4  200  ? 117.395 90.045  138.350 1.00 13.40  ? 200  ILE D O     1 
ATOM   24936 C  CB    . ILE D 4  200  ? 114.412 90.616  138.041 1.00 14.43  ? 200  ILE D CB    1 
ATOM   24937 C  CG1   . ILE D 4  200  ? 113.193 90.952  137.194 1.00 8.34   ? 200  ILE D CG1   1 
ATOM   24938 C  CG2   . ILE D 4  200  ? 114.064 90.811  139.489 1.00 8.17   ? 200  ILE D CG2   1 
ATOM   24939 C  CD1   . ILE D 4  200  ? 112.065 89.986  137.361 1.00 6.24   ? 200  ILE D CD1   1 
ATOM   24940 N  N     . THR D 4  201  ? 117.271 92.073  139.315 1.00 6.71   ? 201  THR D N     1 
ATOM   24941 C  CA    . THR D 4  201  ? 118.416 91.899  140.189 1.00 14.12  ? 201  THR D CA    1 
ATOM   24942 C  C     . THR D 4  201  ? 117.939 91.700  141.629 1.00 16.13  ? 201  THR D C     1 
ATOM   24943 O  O     . THR D 4  201  ? 116.749 91.544  141.891 1.00 21.02  ? 201  THR D O     1 
ATOM   24944 C  CB    . THR D 4  201  ? 119.370 93.087  140.049 1.00 11.45  ? 201  THR D CB    1 
ATOM   24945 O  OG1   . THR D 4  201  ? 118.669 94.309  140.289 1.00 14.16  ? 201  THR D OG1   1 
ATOM   24946 C  CG2   . THR D 4  201  ? 119.967 93.123  138.662 1.00 3.63   ? 201  THR D CG2   1 
ATOM   24947 N  N     . LYS D 4  202  ? 118.872 91.690  142.576 1.00 24.10  ? 202  LYS D N     1 
ATOM   24948 C  CA    . LYS D 4  202  ? 118.523 91.423  143.964 1.00 25.77  ? 202  LYS D CA    1 
ATOM   24949 C  C     . LYS D 4  202  ? 117.763 92.598  144.573 1.00 25.09  ? 202  LYS D C     1 
ATOM   24950 O  O     . LYS D 4  202  ? 117.878 93.743  144.135 1.00 21.31  ? 202  LYS D O     1 
ATOM   24951 C  CB    . LYS D 4  202  ? 119.769 91.126  144.794 1.00 27.40  ? 202  LYS D CB    1 
ATOM   24952 C  CG    . LYS D 4  202  ? 120.834 92.196  144.714 1.00 28.69  ? 202  LYS D CG    1 
ATOM   24953 C  CD    . LYS D 4  202  ? 120.859 93.055  145.968 1.00 27.54  ? 202  LYS D CD    1 
ATOM   24954 C  CE    . LYS D 4  202  ? 122.269 93.492  146.302 1.00 29.68  ? 202  LYS D CE    1 
ATOM   24955 N  NZ    . LYS D 4  202  ? 122.283 94.630  147.251 1.00 31.66  ? 202  LYS D NZ    1 
ATOM   24956 N  N     . SER D 4  203  ? 116.980 92.294  145.604 1.00 27.49  ? 203  SER D N     1 
ATOM   24957 C  CA    . SER D 4  203  ? 116.086 93.265  146.211 1.00 29.35  ? 203  SER D CA    1 
ATOM   24958 C  C     . SER D 4  203  ? 116.825 94.157  147.205 1.00 33.00  ? 203  SER D C     1 
ATOM   24959 O  O     . SER D 4  203  ? 117.967 93.902  147.589 1.00 35.74  ? 203  SER D O     1 
ATOM   24960 C  CB    . SER D 4  203  ? 114.923 92.558  146.897 1.00 31.40  ? 203  SER D CB    1 
ATOM   24961 O  OG    . SER D 4  203  ? 115.377 91.776  147.979 1.00 35.72  ? 203  SER D OG    1 
ATOM   24962 N  N     . LYS D 4  204  ? 116.142 95.227  147.618 1.00 33.09  ? 204  LYS D N     1 
ATOM   24963 C  CA    . LYS D 4  204  ? 116.745 96.211  148.512 1.00 37.73  ? 204  LYS D CA    1 
ATOM   24964 C  C     . LYS D 4  204  ? 117.090 95.606  149.868 1.00 39.48  ? 204  LYS D C     1 
ATOM   24965 O  O     . LYS D 4  204  ? 118.156 95.884  150.428 1.00 36.83  ? 204  LYS D O     1 
ATOM   24966 C  CB    . LYS D 4  204  ? 115.800 97.397  148.690 1.00 34.31  ? 204  LYS D CB    1 
ATOM   24967 C  CG    . LYS D 4  204  ? 116.453 98.646  149.257 1.00 34.55  ? 204  LYS D CG    1 
ATOM   24968 C  CD    . LYS D 4  204  ? 115.418 99.735  149.528 1.00 35.41  ? 204  LYS D CD    1 
ATOM   24969 C  CE    . LYS D 4  204  ? 115.015 100.468 148.256 1.00 35.17  ? 204  LYS D CE    1 
ATOM   24970 N  NZ    . LYS D 4  204  ? 113.936 99.772  147.499 1.00 34.67  ? 204  LYS D NZ    1 
ATOM   24971 N  N     . ILE D 4  205  ? 116.200 94.791  150.415 1.00 41.59  ? 205  ILE D N     1 
ATOM   24972 C  CA    . ILE D 4  205  ? 116.401 94.222  151.738 1.00 40.31  ? 205  ILE D CA    1 
ATOM   24973 C  C     . ILE D 4  205  ? 116.270 92.705  151.688 1.00 42.56  ? 205  ILE D C     1 
ATOM   24974 O  O     . ILE D 4  205  ? 115.428 92.169  150.969 1.00 45.11  ? 205  ILE D O     1 
ATOM   24975 C  CB    . ILE D 4  205  ? 115.413 94.822  152.745 1.00 41.74  ? 205  ILE D CB    1 
ATOM   24976 C  CG1   . ILE D 4  205  ? 115.695 96.313  152.931 1.00 40.65  ? 205  ILE D CG1   1 
ATOM   24977 C  CG2   . ILE D 4  205  ? 115.490 94.083  154.064 1.00 40.25  ? 205  ILE D CG2   1 
ATOM   24978 C  CD1   . ILE D 4  205  ? 114.568 97.072  153.563 1.00 41.65  ? 205  ILE D CD1   1 
ATOM   24979 N  N     . SER E 5  42   ? 155.955 91.061  145.712 1.00 40.82  ? 42   SER E N     1 
ATOM   24980 C  CA    . SER E 5  42   ? 157.311 90.534  145.585 1.00 44.24  ? 42   SER E CA    1 
ATOM   24981 C  C     . SER E 5  42   ? 157.817 90.511  144.133 1.00 44.72  ? 42   SER E C     1 
ATOM   24982 O  O     . SER E 5  42   ? 158.937 90.948  143.875 1.00 42.59  ? 42   SER E O     1 
ATOM   24983 C  CB    . SER E 5  42   ? 157.383 89.123  146.172 1.00 30.00  ? 42   SER E CB    1 
ATOM   24984 O  OG    . SER E 5  42   ? 156.582 88.220  145.430 1.00 30.00  ? 42   SER E OG    1 
ATOM   24985 N  N     . PRO E 5  43   ? 157.017 89.998  143.172 1.00 45.94  ? 43   PRO E N     1 
ATOM   24986 C  CA    . PRO E 5  43   ? 157.466 90.054  141.777 1.00 46.03  ? 43   PRO E CA    1 
ATOM   24987 C  C     . PRO E 5  43   ? 157.078 91.358  141.104 1.00 46.27  ? 43   PRO E C     1 
ATOM   24988 O  O     . PRO E 5  43   ? 156.503 92.250  141.735 1.00 42.60  ? 43   PRO E O     1 
ATOM   24989 C  CB    . PRO E 5  43   ? 156.756 88.858  141.140 1.00 45.11  ? 43   PRO E CB    1 
ATOM   24990 C  CG    . PRO E 5  43   ? 155.479 88.795  141.866 1.00 44.57  ? 43   PRO E CG    1 
ATOM   24991 C  CD    . PRO E 5  43   ? 155.752 89.245  143.281 1.00 43.19  ? 43   PRO E CD    1 
ATOM   24992 N  N     . SER E 5  44   ? 157.397 91.477  139.823 1.00 46.66  ? 44   SER E N     1 
ATOM   24993 C  CA    . SER E 5  44   ? 156.983 92.622  139.035 1.00 44.74  ? 44   SER E CA    1 
ATOM   24994 C  C     . SER E 5  44   ? 155.625 92.345  138.398 1.00 47.44  ? 44   SER E C     1 
ATOM   24995 O  O     . SER E 5  44   ? 155.219 91.194  138.225 1.00 46.36  ? 44   SER E O     1 
ATOM   24996 C  CB    . SER E 5  44   ? 158.030 92.939  137.966 1.00 43.36  ? 44   SER E CB    1 
ATOM   24997 O  OG    . SER E 5  44   ? 157.731 94.149  137.294 1.00 47.71  ? 44   SER E OG    1 
ATOM   24998 N  N     . ILE E 5  45   ? 154.915 93.425  138.061 1.00 41.32  ? 45   ILE E N     1 
ATOM   24999 C  CA    . ILE E 5  45   ? 153.598 93.278  137.446 1.00 43.62  ? 45   ILE E CA    1 
ATOM   25000 C  C     . ILE E 5  45   ? 153.710 92.573  136.103 1.00 44.62  ? 45   ILE E C     1 
ATOM   25001 O  O     . ILE E 5  45   ? 152.807 91.830  135.698 1.00 42.60  ? 45   ILE E O     1 
ATOM   25002 C  CB    . ILE E 5  45   ? 152.905 94.647  137.310 1.00 43.05  ? 45   ILE E CB    1 
ATOM   25003 C  CG1   . ILE E 5  45   ? 153.139 95.492  138.558 1.00 40.38  ? 45   ILE E CG1   1 
ATOM   25004 C  CG2   . ILE E 5  45   ? 151.415 94.475  137.032 1.00 40.55  ? 45   ILE E CG2   1 
ATOM   25005 C  CD1   . ILE E 5  45   ? 152.254 95.107  139.718 1.00 37.97  ? 45   ILE E CD1   1 
ATOM   25006 N  N     . CYS E 5  46   ? 154.824 92.785  135.397 1.00 46.69  ? 46   CYS E N     1 
ATOM   25007 C  CA    . CYS E 5  46   ? 155.005 92.201  134.074 1.00 47.42  ? 46   CYS E CA    1 
ATOM   25008 C  C     . CYS E 5  46   ? 155.036 90.680  134.103 1.00 48.30  ? 46   CYS E C     1 
ATOM   25009 O  O     . CYS E 5  46   ? 154.689 90.049  133.097 1.00 47.66  ? 46   CYS E O     1 
ATOM   25010 C  CB    . CYS E 5  46   ? 156.294 92.724  133.447 1.00 48.15  ? 46   CYS E CB    1 
ATOM   25011 S  SG    . CYS E 5  46   ? 157.795 92.063  134.187 1.00 59.11  ? 46   CYS E SG    1 
ATOM   25012 N  N     . GLU E 5  47   ? 155.448 90.080  135.223 1.00 44.12  ? 47   GLU E N     1 
ATOM   25013 C  CA    . GLU E 5  47   ? 155.523 88.625  135.310 1.00 45.23  ? 47   GLU E CA    1 
ATOM   25014 C  C     . GLU E 5  47   ? 154.142 87.990  135.200 1.00 46.39  ? 47   GLU E C     1 
ATOM   25015 O  O     . GLU E 5  47   ? 153.914 87.101  134.372 1.00 45.36  ? 47   GLU E O     1 
ATOM   25016 C  CB    . GLU E 5  47   ? 156.204 88.219  136.616 1.00 44.63  ? 47   GLU E CB    1 
ATOM   25017 C  CG    . GLU E 5  47   ? 156.249 86.720  136.861 1.00 45.01  ? 47   GLU E CG    1 
ATOM   25018 C  CD    . GLU E 5  47   ? 155.113 86.243  137.751 1.00 48.28  ? 47   GLU E CD    1 
ATOM   25019 O  OE1   . GLU E 5  47   ? 154.675 87.020  138.624 1.00 48.23  ? 47   GLU E OE1   1 
ATOM   25020 O  OE2   . GLU E 5  47   ? 154.657 85.095  137.577 1.00 49.71  ? 47   GLU E OE2   1 
ATOM   25021 N  N     . GLY E 5  48   ? 153.202 88.442  136.028 1.00 41.84  ? 48   GLY E N     1 
ATOM   25022 C  CA    . GLY E 5  48   ? 151.863 87.886  136.010 1.00 41.36  ? 48   GLY E CA    1 
ATOM   25023 C  C     . GLY E 5  48   ? 150.980 88.370  134.883 1.00 43.08  ? 48   GLY E C     1 
ATOM   25024 O  O     . GLY E 5  48   ? 149.884 87.830  134.700 1.00 41.95  ? 48   GLY E O     1 
ATOM   25025 N  N     . PHE E 5  49   ? 151.426 89.371  134.128 1.00 37.63  ? 49   PHE E N     1 
ATOM   25026 C  CA    . PHE E 5  49   ? 150.645 89.870  133.006 1.00 35.95  ? 49   PHE E CA    1 
ATOM   25027 C  C     . PHE E 5  49   ? 150.596 88.833  131.895 1.00 35.29  ? 49   PHE E C     1 
ATOM   25028 O  O     . PHE E 5  49   ? 151.619 88.254  131.524 1.00 36.97  ? 49   PHE E O     1 
ATOM   25029 C  CB    . PHE E 5  49   ? 151.238 91.179  132.492 1.00 31.92  ? 49   PHE E CB    1 
ATOM   25030 C  CG    . PHE E 5  49   ? 150.533 91.738  131.294 1.00 33.31  ? 49   PHE E CG    1 
ATOM   25031 C  CD1   . PHE E 5  49   ? 149.409 92.522  131.437 1.00 35.88  ? 49   PHE E CD1   1 
ATOM   25032 C  CD2   . PHE E 5  49   ? 151.012 91.503  130.023 1.00 31.82  ? 49   PHE E CD2   1 
ATOM   25033 C  CE1   . PHE E 5  49   ? 148.768 93.041  130.329 1.00 34.86  ? 49   PHE E CE1   1 
ATOM   25034 C  CE2   . PHE E 5  49   ? 150.374 92.015  128.920 1.00 30.98  ? 49   PHE E CE2   1 
ATOM   25035 C  CZ    . PHE E 5  49   ? 149.255 92.786  129.073 1.00 31.95  ? 49   PHE E CZ    1 
ATOM   25036 N  N     . VAL E 5  50   ? 149.401 88.596  131.368 1.00 36.76  ? 50   VAL E N     1 
ATOM   25037 C  CA    . VAL E 5  50   ? 149.190 87.711  130.232 1.00 38.11  ? 50   VAL E CA    1 
ATOM   25038 C  C     . VAL E 5  50   ? 148.667 88.559  129.086 1.00 38.52  ? 50   VAL E C     1 
ATOM   25039 O  O     . VAL E 5  50   ? 147.681 89.286  129.249 1.00 35.94  ? 50   VAL E O     1 
ATOM   25040 C  CB    . VAL E 5  50   ? 148.199 86.579  130.564 1.00 40.11  ? 50   VAL E CB    1 
ATOM   25041 C  CG1   . VAL E 5  50   ? 148.162 85.559  129.441 1.00 37.25  ? 50   VAL E CG1   1 
ATOM   25042 C  CG2   . VAL E 5  50   ? 148.558 85.922  131.884 1.00 37.07  ? 50   VAL E CG2   1 
ATOM   25043 N  N     . GLN E 5  51   ? 149.328 88.483  127.937 1.00 40.63  ? 51   GLN E N     1 
ATOM   25044 C  CA    . GLN E 5  51   ? 148.837 89.219  126.785 1.00 38.70  ? 51   GLN E CA    1 
ATOM   25045 C  C     . GLN E 5  51   ? 147.515 88.620  126.323 1.00 39.05  ? 51   GLN E C     1 
ATOM   25046 O  O     . GLN E 5  51   ? 147.234 87.437  126.539 1.00 35.74  ? 51   GLN E O     1 
ATOM   25047 C  CB    . GLN E 5  51   ? 149.851 89.202  125.643 1.00 33.64  ? 51   GLN E CB    1 
ATOM   25048 C  CG    . GLN E 5  51   ? 149.692 88.044  124.693 1.00 33.88  ? 51   GLN E CG    1 
ATOM   25049 C  CD    . GLN E 5  51   ? 150.723 88.045  123.598 1.00 37.40  ? 51   GLN E CD    1 
ATOM   25050 O  OE1   . GLN E 5  51   ? 151.752 88.705  123.701 1.00 38.78  ? 51   GLN E OE1   1 
ATOM   25051 N  NE2   . GLN E 5  51   ? 150.443 87.320  122.524 1.00 38.94  ? 51   GLN E NE2   1 
ATOM   25052 N  N     . ALA E 5  52   ? 146.686 89.460  125.712 1.00 33.31  ? 52   ALA E N     1 
ATOM   25053 C  CA    . ALA E 5  52   ? 145.405 89.000  125.196 1.00 33.39  ? 52   ALA E CA    1 
ATOM   25054 C  C     . ALA E 5  52   ? 145.618 87.929  124.139 1.00 31.45  ? 52   ALA E C     1 
ATOM   25055 O  O     . ALA E 5  52   ? 146.446 88.083  123.238 1.00 33.24  ? 52   ALA E O     1 
ATOM   25056 C  CB    . ALA E 5  52   ? 144.620 90.171  124.610 1.00 34.51  ? 52   ALA E CB    1 
ATOM   25057 N  N     . SER E 5  53   ? 144.872 86.837  124.255 1.00 32.67  ? 53   SER E N     1 
ATOM   25058 C  CA    . SER E 5  53   ? 144.976 85.761  123.285 1.00 34.34  ? 53   SER E CA    1 
ATOM   25059 C  C     . SER E 5  53   ? 144.437 86.216  121.935 1.00 37.07  ? 53   SER E C     1 
ATOM   25060 O  O     . SER E 5  53   ? 143.489 87.000  121.853 1.00 40.57  ? 53   SER E O     1 
ATOM   25061 C  CB    . SER E 5  53   ? 144.212 84.536  123.781 1.00 34.44  ? 53   SER E CB    1 
ATOM   25062 O  OG    . SER E 5  53   ? 144.283 83.476  122.849 1.00 39.36  ? 53   SER E OG    1 
ATOM   25063 N  N     . SER E 5  54   ? 145.056 85.724  120.866 1.00 24.97  ? 54   SER E N     1 
ATOM   25064 C  CA    . SER E 5  54   ? 144.633 86.097  119.526 1.00 20.63  ? 54   SER E CA    1 
ATOM   25065 C  C     . SER E 5  54   ? 143.244 85.544  119.237 1.00 19.90  ? 54   SER E C     1 
ATOM   25066 O  O     . SER E 5  54   ? 142.800 84.576  119.855 1.00 24.94  ? 54   SER E O     1 
ATOM   25067 C  CB    . SER E 5  54   ? 145.640 85.599  118.493 1.00 22.23  ? 54   SER E CB    1 
ATOM   25068 O  OG    . SER E 5  54   ? 145.215 84.392  117.903 1.00 24.45  ? 54   SER E OG    1 
ATOM   25069 N  N     . GLN E 5  55   ? 142.550 86.182  118.299 1.00 13.62  ? 55   GLN E N     1 
ATOM   25070 C  CA    . GLN E 5  55   ? 141.149 85.913  118.019 1.00 17.32  ? 55   GLN E CA    1 
ATOM   25071 C  C     . GLN E 5  55   ? 140.958 85.261  116.657 1.00 16.45  ? 55   GLN E C     1 
ATOM   25072 O  O     . GLN E 5  55   ? 141.876 85.174  115.846 1.00 19.82  ? 55   GLN E O     1 
ATOM   25073 C  CB    . GLN E 5  55   ? 140.329 87.202  118.077 1.00 16.80  ? 55   GLN E CB    1 
ATOM   25074 C  CG    . GLN E 5  55   ? 140.171 87.760  119.460 1.00 16.46  ? 55   GLN E CG    1 
ATOM   25075 C  CD    . GLN E 5  55   ? 139.577 89.135  119.458 1.00 19.23  ? 55   GLN E CD    1 
ATOM   25076 O  OE1   . GLN E 5  55   ? 139.362 89.726  118.408 1.00 23.25  ? 55   GLN E OE1   1 
ATOM   25077 N  NE2   . GLN E 5  55   ? 139.296 89.655  120.639 1.00 18.28  ? 55   GLN E NE2   1 
ATOM   25078 N  N     . THR E 5  56   ? 139.737 84.795  116.428 1.00 11.34  ? 56   THR E N     1 
ATOM   25079 C  CA    . THR E 5  56   ? 139.307 84.257  115.147 1.00 11.73  ? 56   THR E CA    1 
ATOM   25080 C  C     . THR E 5  56   ? 138.253 85.180  114.561 1.00 17.15  ? 56   THR E C     1 
ATOM   25081 O  O     . THR E 5  56   ? 137.427 85.725  115.293 1.00 26.10  ? 56   THR E O     1 
ATOM   25082 C  CB    . THR E 5  56   ? 138.730 82.850  115.294 1.00 18.77  ? 56   THR E CB    1 
ATOM   25083 O  OG1   . THR E 5  56   ? 139.474 82.117  116.270 1.00 20.53  ? 56   THR E OG1   1 
ATOM   25084 C  CG2   . THR E 5  56   ? 138.774 82.118  113.970 1.00 19.32  ? 56   THR E CG2   1 
ATOM   25085 N  N     . LEU E 5  57   ? 138.284 85.356  113.249 1.00 10.20  ? 57   LEU E N     1 
ATOM   25086 C  CA    . LEU E 5  57   ? 137.334 86.226  112.577 1.00 9.07   ? 57   LEU E CA    1 
ATOM   25087 C  C     . LEU E 5  57   ? 136.169 85.387  112.072 1.00 12.70  ? 57   LEU E C     1 
ATOM   25088 O  O     . LEU E 5  57   ? 136.302 84.654  111.091 1.00 18.67  ? 57   LEU E O     1 
ATOM   25089 C  CB    . LEU E 5  57   ? 138.023 86.975  111.441 1.00 15.10  ? 57   LEU E CB    1 
ATOM   25090 C  CG    . LEU E 5  57   ? 137.305 88.186  110.859 1.00 12.94  ? 57   LEU E CG    1 
ATOM   25091 C  CD1   . LEU E 5  57   ? 137.450 89.384  111.767 1.00 13.52  ? 57   LEU E CD1   1 
ATOM   25092 C  CD2   . LEU E 5  57   ? 137.842 88.495  109.496 1.00 11.15  ? 57   LEU E CD2   1 
ATOM   25093 N  N     . VAL E 5  58   ? 135.029 85.491  112.737 1.00 12.86  ? 58   VAL E N     1 
ATOM   25094 C  CA    . VAL E 5  58   ? 133.825 84.769  112.344 1.00 11.31  ? 58   VAL E CA    1 
ATOM   25095 C  C     . VAL E 5  58   ? 132.951 85.701  111.524 1.00 7.79   ? 58   VAL E C     1 
ATOM   25096 O  O     . VAL E 5  58   ? 132.516 86.747  112.011 1.00 9.83   ? 58   VAL E O     1 
ATOM   25097 C  CB    . VAL E 5  58   ? 133.068 84.248  113.573 1.00 10.55  ? 58   VAL E CB    1 
ATOM   25098 C  CG1   . VAL E 5  58   ? 131.871 83.435  113.144 1.00 6.74   ? 58   VAL E CG1   1 
ATOM   25099 C  CG2   . VAL E 5  58   ? 133.985 83.437  114.448 1.00 12.06  ? 58   VAL E CG2   1 
ATOM   25100 N  N     . ILE E 5  59   ? 132.681 85.319  110.285 1.00 9.57   ? 59   ILE E N     1 
ATOM   25101 C  CA    . ILE E 5  59   ? 131.982 86.168  109.335 1.00 6.39   ? 59   ILE E CA    1 
ATOM   25102 C  C     . ILE E 5  59   ? 130.558 85.658  109.211 1.00 9.99   ? 59   ILE E C     1 
ATOM   25103 O  O     . ILE E 5  59   ? 130.336 84.511  108.811 1.00 17.27  ? 59   ILE E O     1 
ATOM   25104 C  CB    . ILE E 5  59   ? 132.692 86.192  107.976 1.00 6.53   ? 59   ILE E CB    1 
ATOM   25105 C  CG1   . ILE E 5  59   ? 134.082 86.789  108.138 1.00 9.87   ? 59   ILE E CG1   1 
ATOM   25106 C  CG2   . ILE E 5  59   ? 131.913 86.992  106.977 1.00 4.82   ? 59   ILE E CG2   1 
ATOM   25107 C  CD1   . ILE E 5  59   ? 134.927 86.707  106.920 1.00 10.06  ? 59   ILE E CD1   1 
ATOM   25108 N  N     . ILE E 5  60   ? 129.599 86.508  109.558 1.00 8.01   ? 60   ILE E N     1 
ATOM   25109 C  CA    . ILE E 5  60   ? 128.187 86.132  109.463 1.00 10.43  ? 60   ILE E CA    1 
ATOM   25110 C  C     . ILE E 5  60   ? 127.834 85.877  108.004 1.00 11.40  ? 60   ILE E C     1 
ATOM   25111 O  O     . ILE E 5  60   ? 128.184 86.694  107.134 1.00 14.97  ? 60   ILE E O     1 
ATOM   25112 C  CB    . ILE E 5  60   ? 127.303 87.236  110.066 1.00 4.08   ? 60   ILE E CB    1 
ATOM   25113 C  CG1   . ILE E 5  60   ? 127.595 87.373  111.554 1.00 3.26   ? 60   ILE E CG1   1 
ATOM   25114 C  CG2   . ILE E 5  60   ? 125.848 86.948  109.843 1.00 9.31   ? 60   ILE E CG2   1 
ATOM   25115 C  CD1   . ILE E 5  60   ? 126.922 88.535  112.193 1.00 9.56   ? 60   ILE E CD1   1 
ATOM   25116 N  N     . PRO E 5  61   ? 127.167 84.772  107.674 1.00 11.79  ? 61   PRO E N     1 
ATOM   25117 C  CA    . PRO E 5  61   ? 126.835 84.498  106.273 1.00 12.72  ? 61   PRO E CA    1 
ATOM   25118 C  C     . PRO E 5  61   ? 125.880 85.528  105.694 1.00 15.16  ? 61   PRO E C     1 
ATOM   25119 O  O     . PRO E 5  61   ? 125.074 86.135  106.394 1.00 19.87  ? 61   PRO E O     1 
ATOM   25120 C  CB    . PRO E 5  61   ? 126.198 83.103  106.322 1.00 15.04  ? 61   PRO E CB    1 
ATOM   25121 C  CG    . PRO E 5  61   ? 125.898 82.855  107.735 1.00 14.95  ? 61   PRO E CG    1 
ATOM   25122 C  CD    . PRO E 5  61   ? 126.878 83.620  108.536 1.00 12.94  ? 61   PRO E CD    1 
ATOM   25123 N  N     . ASP E 5  62   ? 125.972 85.697  104.374 1.00 19.66  ? 62   ASP E N     1 
ATOM   25124 C  CA    . ASP E 5  62   ? 125.338 86.826  103.700 1.00 17.49  ? 62   ASP E CA    1 
ATOM   25125 C  C     . ASP E 5  62   ? 123.837 86.879  103.915 1.00 20.71  ? 62   ASP E C     1 
ATOM   25126 O  O     . ASP E 5  62   ? 123.259 87.968  103.928 1.00 24.69  ? 62   ASP E O     1 
ATOM   25127 C  CB    . ASP E 5  62   ? 125.640 86.779  102.206 1.00 22.29  ? 62   ASP E CB    1 
ATOM   25128 C  CG    . ASP E 5  62   ? 126.961 87.419  101.863 1.00 29.82  ? 62   ASP E CG    1 
ATOM   25129 O  OD1   . ASP E 5  62   ? 127.300 87.465  100.666 1.00 31.00  ? 62   ASP E OD1   1 
ATOM   25130 O  OD2   . ASP E 5  62   ? 127.655 87.887  102.787 1.00 27.96  ? 62   ASP E OD2   1 
ATOM   25131 N  N     . ASN E 5  63   ? 123.185 85.734  104.078 1.00 22.60  ? 63   ASN E N     1 
ATOM   25132 C  CA    . ASN E 5  63   ? 121.739 85.732  104.225 1.00 19.93  ? 63   ASN E CA    1 
ATOM   25133 C  C     . ASN E 5  63   ? 121.284 85.890  105.665 1.00 21.77  ? 63   ASN E C     1 
ATOM   25134 O  O     . ASN E 5  63   ? 120.080 85.859  105.921 1.00 24.05  ? 63   ASN E O     1 
ATOM   25135 C  CB    . ASN E 5  63   ? 121.154 84.457  103.632 1.00 24.02  ? 63   ASN E CB    1 
ATOM   25136 C  CG    . ASN E 5  63   ? 120.676 84.649  102.212 1.00 31.91  ? 63   ASN E CG    1 
ATOM   25137 O  OD1   . ASN E 5  63   ? 121.076 85.589  101.531 1.00 27.70  ? 63   ASN E OD1   1 
ATOM   25138 N  ND2   . ASN E 5  63   ? 119.807 83.759  101.759 1.00 30.78  ? 63   ASN E ND2   1 
ATOM   25139 N  N     . GLU E 5  64   ? 122.207 86.060  106.607 1.00 20.27  ? 64   GLU E N     1 
ATOM   25140 C  CA    . GLU E 5  64   ? 121.867 86.244  108.010 1.00 13.44  ? 64   GLU E CA    1 
ATOM   25141 C  C     . GLU E 5  64   ? 122.219 87.632  108.521 1.00 17.48  ? 64   GLU E C     1 
ATOM   25142 O  O     . GLU E 5  64   ? 122.143 87.875  109.725 1.00 20.46  ? 64   GLU E O     1 
ATOM   25143 C  CB    . GLU E 5  64   ? 122.565 85.192  108.864 1.00 13.04  ? 64   GLU E CB    1 
ATOM   25144 C  CG    . GLU E 5  64   ? 121.983 83.818  108.752 1.00 16.14  ? 64   GLU E CG    1 
ATOM   25145 C  CD    . GLU E 5  64   ? 122.885 82.780  109.354 1.00 25.10  ? 64   GLU E CD    1 
ATOM   25146 O  OE1   . GLU E 5  64   ? 123.592 83.111  110.325 1.00 25.11  ? 64   GLU E OE1   1 
ATOM   25147 O  OE2   . GLU E 5  64   ? 122.894 81.636  108.863 1.00 28.22  ? 64   GLU E OE2   1 
ATOM   25148 N  N     . ARG E 5  65   ? 122.599 88.545  107.637 1.00 12.75  ? 65   ARG E N     1 
ATOM   25149 C  CA    . ARG E 5  65   ? 123.029 89.870  108.048 1.00 9.43   ? 65   ARG E CA    1 
ATOM   25150 C  C     . ARG E 5  65   ? 121.846 90.720  108.483 1.00 11.80  ? 65   ARG E C     1 
ATOM   25151 O  O     . ARG E 5  65   ? 120.791 90.721  107.847 1.00 12.04  ? 65   ARG E O     1 
ATOM   25152 C  CB    . ARG E 5  65   ? 123.792 90.554  106.918 1.00 10.15  ? 65   ARG E CB    1 
ATOM   25153 C  CG    . ARG E 5  65   ? 125.176 89.978  106.688 1.00 8.85   ? 65   ARG E CG    1 
ATOM   25154 C  CD    . ARG E 5  65   ? 125.909 90.706  105.597 1.00 6.75   ? 65   ARG E CD    1 
ATOM   25155 N  NE    . ARG E 5  65   ? 125.247 90.521  104.318 1.00 7.31   ? 65   ARG E NE    1 
ATOM   25156 C  CZ    . ARG E 5  65   ? 125.698 90.990  103.168 1.00 11.76  ? 65   ARG E CZ    1 
ATOM   25157 N  NH1   . ARG E 5  65   ? 126.840 91.642  103.092 1.00 10.00  ? 65   ARG E NH1   1 
ATOM   25158 N  NH2   . ARG E 5  65   ? 124.983 90.798  102.066 1.00 9.38   ? 65   ARG E NH2   1 
ATOM   25159 N  N     . ILE E 5  66   ? 122.043 91.462  109.570 1.00 6.85   ? 66   ILE E N     1 
ATOM   25160 C  CA    . ILE E 5  66   ? 120.974 92.186  110.231 1.00 4.36   ? 66   ILE E CA    1 
ATOM   25161 C  C     . ILE E 5  66   ? 121.064 93.695  110.017 1.00 4.10   ? 66   ILE E C     1 
ATOM   25162 O  O     . ILE E 5  66   ? 120.037 94.377  110.064 1.00 2.38   ? 66   ILE E O     1 
ATOM   25163 C  CB    . ILE E 5  66   ? 120.975 91.826  111.738 1.00 5.79   ? 66   ILE E CB    1 
ATOM   25164 C  CG1   . ILE E 5  66   ? 120.244 90.508  111.972 1.00 8.85   ? 66   ILE E CG1   1 
ATOM   25165 C  CG2   . ILE E 5  66   ? 120.376 92.889  112.599 1.00 4.37   ? 66   ILE E CG2   1 
ATOM   25166 C  CD1   . ILE E 5  66   ? 119.086 90.276  111.048 1.00 8.76   ? 66   ILE E CD1   1 
ATOM   25167 N  N     . THR E 5  67   ? 122.251 94.234  109.756 1.00 3.73   ? 67   THR E N     1 
ATOM   25168 C  CA    . THR E 5  67   ? 122.426 95.666  109.592 1.00 15.39  ? 67   THR E CA    1 
ATOM   25169 C  C     . THR E 5  67   ? 121.929 96.116  108.221 1.00 1.99   ? 67   THR E C     1 
ATOM   25170 O  O     . THR E 5  67   ? 121.612 95.312  107.347 1.00 10.60  ? 67   THR E O     1 
ATOM   25171 C  CB    . THR E 5  67   ? 123.887 96.047  109.787 1.00 13.33  ? 67   THR E CB    1 
ATOM   25172 O  OG1   . THR E 5  67   ? 124.710 95.079  109.142 1.00 11.13  ? 67   THR E OG1   1 
ATOM   25173 C  CG2   . THR E 5  67   ? 124.236 96.064  111.240 1.00 10.88  ? 67   THR E CG2   1 
ATOM   25174 N  N     . SER E 5  68   ? 121.864 97.431  108.039 1.00 1.98   ? 68   SER E N     1 
ATOM   25175 C  CA    . SER E 5  68   ? 121.218 97.985  106.859 1.00 0.06   ? 68   SER E CA    1 
ATOM   25176 C  C     . SER E 5  68   ? 122.098 97.866  105.628 1.00 12.14  ? 68   SER E C     1 
ATOM   25177 O  O     . SER E 5  68   ? 123.323 97.931  105.706 1.00 1.11   ? 68   SER E O     1 
ATOM   25178 C  CB    . SER E 5  68   ? 120.846 99.446  107.088 1.00 3.69   ? 68   SER E CB    1 
ATOM   25179 O  OG    . SER E 5  68   ? 121.974 100.276 107.039 1.00 9.56   ? 68   SER E OG    1 
ATOM   25180 N  N     . ASN E 5  69   ? 121.455 97.698  104.482 1.00 6.20   ? 69   ASN E N     1 
ATOM   25181 C  CA    . ASN E 5  69   ? 122.106 97.641  103.187 1.00 2.12   ? 69   ASN E CA    1 
ATOM   25182 C  C     . ASN E 5  69   ? 122.381 99.008  102.610 1.00 3.50   ? 69   ASN E C     1 
ATOM   25183 O  O     . ASN E 5  69   ? 122.786 99.112  101.455 1.00 10.40  ? 69   ASN E O     1 
ATOM   25184 C  CB    . ASN E 5  69   ? 121.260 96.820  102.216 1.00 4.25   ? 69   ASN E CB    1 
ATOM   25185 C  CG    . ASN E 5  69   ? 119.912 97.433  101.962 1.00 9.30   ? 69   ASN E CG    1 
ATOM   25186 O  OD1   . ASN E 5  69   ? 119.070 97.468  102.842 1.00 3.39   ? 69   ASN E OD1   1 
ATOM   25187 N  ND2   . ASN E 5  69   ? 119.708 97.943  100.767 1.00 2.96   ? 69   ASN E ND2   1 
ATOM   25188 N  N     . VAL E 5  70   ? 122.165 100.058 103.389 1.00 0.64   ? 70   VAL E N     1 
ATOM   25189 C  CA    . VAL E 5  70   ? 122.442 101.426 102.991 1.00 12.39  ? 70   VAL E CA    1 
ATOM   25190 C  C     . VAL E 5  70   ? 123.617 101.912 103.817 1.00 9.20   ? 70   VAL E C     1 
ATOM   25191 O  O     . VAL E 5  70   ? 123.664 101.680 105.028 1.00 9.42   ? 70   VAL E O     1 
ATOM   25192 C  CB    . VAL E 5  70   ? 121.213 102.329 103.185 1.00 0.06   ? 70   VAL E CB    1 
ATOM   25193 C  CG1   . VAL E 5  70   ? 121.502 103.733 102.710 1.00 1.38   ? 70   VAL E CG1   1 
ATOM   25194 C  CG2   . VAL E 5  70   ? 120.028 101.750 102.463 1.00 0.62   ? 70   VAL E CG2   1 
ATOM   25195 N  N     . LEU E 5  71   ? 124.583 102.542 103.158 1.00 2.19   ? 71   LEU E N     1 
ATOM   25196 C  CA    . LEU E 5  71   ? 125.715 103.119 103.865 1.00 3.88   ? 71   LEU E CA    1 
ATOM   25197 C  C     . LEU E 5  71   ? 125.269 104.283 104.731 1.00 8.30   ? 71   LEU E C     1 
ATOM   25198 O  O     . LEU E 5  71   ? 124.388 105.052 104.353 1.00 5.79   ? 71   LEU E O     1 
ATOM   25199 C  CB    . LEU E 5  71   ? 126.768 103.595 102.875 1.00 4.20   ? 71   LEU E CB    1 
ATOM   25200 C  CG    . LEU E 5  71   ? 127.611 102.555 102.161 1.00 2.18   ? 71   LEU E CG    1 
ATOM   25201 C  CD1   . LEU E 5  71   ? 128.193 103.155 100.917 1.00 6.34   ? 71   LEU E CD1   1 
ATOM   25202 C  CD2   . LEU E 5  71   ? 128.691 102.077 103.078 1.00 0.86   ? 71   LEU E CD2   1 
ATOM   25203 N  N     . THR E 5  72   ? 125.872 104.407 105.905 1.00 3.90   ? 72   THR E N     1 
ATOM   25204 C  CA    . THR E 5  72   ? 125.657 105.630 106.651 1.00 2.41   ? 72   THR E CA    1 
ATOM   25205 C  C     . THR E 5  72   ? 126.529 106.724 106.061 1.00 3.46   ? 72   THR E C     1 
ATOM   25206 O  O     . THR E 5  72   ? 127.445 106.469 105.286 1.00 12.89  ? 72   THR E O     1 
ATOM   25207 C  CB    . THR E 5  72   ? 125.944 105.450 108.149 1.00 3.11   ? 72   THR E CB    1 
ATOM   25208 O  OG1   . THR E 5  72   ? 127.346 105.320 108.388 1.00 2.04   ? 72   THR E OG1   1 
ATOM   25209 C  CG2   . THR E 5  72   ? 125.248 104.241 108.679 1.00 2.32   ? 72   THR E CG2   1 
ATOM   25210 N  N     . THR E 5  73   ? 126.209 107.961 106.412 1.00 5.54   ? 73   THR E N     1 
ATOM   25211 C  CA    . THR E 5  73   ? 126.986 109.086 105.918 1.00 4.31   ? 73   THR E CA    1 
ATOM   25212 C  C     . THR E 5  73   ? 128.425 108.998 106.411 1.00 0.79   ? 73   THR E C     1 
ATOM   25213 O  O     . THR E 5  73   ? 129.364 109.341 105.685 1.00 1.49   ? 73   THR E O     1 
ATOM   25214 C  CB    . THR E 5  73   ? 126.308 110.384 106.353 1.00 3.16   ? 73   THR E CB    1 
ATOM   25215 O  OG1   . THR E 5  73   ? 125.193 110.636 105.500 1.00 1.08   ? 73   THR E OG1   1 
ATOM   25216 C  CG2   . THR E 5  73   ? 127.230 111.545 106.226 1.00 2.14   ? 73   THR E CG2   1 
ATOM   25217 N  N     . PHE E 5  74   ? 128.613 108.505 107.637 1.00 3.18   ? 74   PHE E N     1 
ATOM   25218 C  CA    . PHE E 5  74   ? 129.945 108.249 108.177 1.00 1.36   ? 74   PHE E CA    1 
ATOM   25219 C  C     . PHE E 5  74   ? 130.718 107.233 107.339 1.00 1.77   ? 74   PHE E C     1 
ATOM   25220 O  O     . PHE E 5  74   ? 131.902 107.424 107.058 1.00 2.28   ? 74   PHE E O     1 
ATOM   25221 C  CB    . PHE E 5  74   ? 129.829 107.736 109.608 1.00 8.31   ? 74   PHE E CB    1 
ATOM   25222 C  CG    . PHE E 5  74   ? 129.254 108.709 110.590 1.00 3.85   ? 74   PHE E CG    1 
ATOM   25223 C  CD1   . PHE E 5  74   ? 129.532 110.053 110.513 1.00 14.01  ? 74   PHE E CD1   1 
ATOM   25224 C  CD2   . PHE E 5  74   ? 128.477 108.255 111.643 1.00 0.12   ? 74   PHE E CD2   1 
ATOM   25225 C  CE1   . PHE E 5  74   ? 129.026 110.921 111.442 1.00 2.92   ? 74   PHE E CE1   1 
ATOM   25226 C  CE2   . PHE E 5  74   ? 127.972 109.124 112.567 1.00 6.23   ? 74   PHE E CE2   1 
ATOM   25227 C  CZ    . PHE E 5  74   ? 128.250 110.458 112.465 1.00 7.03   ? 74   PHE E CZ    1 
ATOM   25228 N  N     . GLU E 5  75   ? 130.071 106.134 106.954 1.00 14.34  ? 75   GLU E N     1 
ATOM   25229 C  CA    . GLU E 5  75   ? 130.759 105.083 106.214 1.00 15.49  ? 75   GLU E CA    1 
ATOM   25230 C  C     . GLU E 5  75   ? 131.113 105.529 104.804 1.00 6.60   ? 75   GLU E C     1 
ATOM   25231 O  O     . GLU E 5  75   ? 132.208 105.242 104.318 1.00 10.65  ? 75   GLU E O     1 
ATOM   25232 C  CB    . GLU E 5  75   ? 129.900 103.822 106.177 1.00 3.68   ? 75   GLU E CB    1 
ATOM   25233 C  CG    . GLU E 5  75   ? 129.912 103.043 107.464 1.00 3.80   ? 75   GLU E CG    1 
ATOM   25234 C  CD    . GLU E 5  75   ? 128.710 102.139 107.641 1.00 3.76   ? 75   GLU E CD    1 
ATOM   25235 O  OE1   . GLU E 5  75   ? 127.794 102.178 106.807 1.00 1.60   ? 75   GLU E OE1   1 
ATOM   25236 O  OE2   . GLU E 5  75   ? 128.673 101.399 108.637 1.00 8.29   ? 75   GLU E OE2   1 
ATOM   25237 N  N     . ALA E 5  76   ? 130.204 106.230 104.131 1.00 6.67   ? 76   ALA E N     1 
ATOM   25238 C  CA    . ALA E 5  76   ? 130.510 106.767 102.813 1.00 11.18  ? 76   ALA E CA    1 
ATOM   25239 C  C     . ALA E 5  76   ? 131.632 107.796 102.875 1.00 13.64  ? 76   ALA E C     1 
ATOM   25240 O  O     . ALA E 5  76   ? 132.519 107.808 102.012 1.00 20.56  ? 76   ALA E O     1 
ATOM   25241 C  CB    . ALA E 5  76   ? 129.254 107.368 102.201 1.00 2.47   ? 76   ALA E CB    1 
ATOM   25242 N  N     . THR E 5  77   ? 131.613 108.669 103.882 1.00 6.52   ? 77   THR E N     1 
ATOM   25243 C  CA    . THR E 5  77   ? 132.681 109.647 104.037 1.00 8.92   ? 77   THR E CA    1 
ATOM   25244 C  C     . THR E 5  77   ? 134.025 108.968 104.254 1.00 7.61   ? 77   THR E C     1 
ATOM   25245 O  O     . THR E 5  77   ? 135.024 109.352 103.641 1.00 10.54  ? 77   THR E O     1 
ATOM   25246 C  CB    . THR E 5  77   ? 132.356 110.589 105.194 1.00 2.62   ? 77   THR E CB    1 
ATOM   25247 O  OG1   . THR E 5  77   ? 131.044 111.120 105.016 1.00 10.55  ? 77   THR E OG1   1 
ATOM   25248 C  CG2   . THR E 5  77   ? 133.325 111.733 105.263 1.00 8.67   ? 77   THR E CG2   1 
ATOM   25249 N  N     . ARG E 5  78   ? 134.070 107.956 105.117 1.00 5.73   ? 78   ARG E N     1 
ATOM   25250 C  CA    . ARG E 5  78   ? 135.316 107.242 105.363 1.00 5.97   ? 78   ARG E CA    1 
ATOM   25251 C  C     . ARG E 5  78   ? 135.796 106.496 104.123 1.00 2.06   ? 78   ARG E C     1 
ATOM   25252 O  O     . ARG E 5  78   ? 136.999 106.463 103.846 1.00 2.25   ? 78   ARG E O     1 
ATOM   25253 C  CB    . ARG E 5  78   ? 135.132 106.289 106.536 1.00 3.74   ? 78   ARG E CB    1 
ATOM   25254 C  CG    . ARG E 5  78   ? 136.292 105.378 106.812 1.00 2.65   ? 78   ARG E CG    1 
ATOM   25255 C  CD    . ARG E 5  78   ? 137.440 106.096 107.470 1.00 4.59   ? 78   ARG E CD    1 
ATOM   25256 N  NE    . ARG E 5  78   ? 138.469 105.147 107.868 1.00 5.91   ? 78   ARG E NE    1 
ATOM   25257 C  CZ    . ARG E 5  78   ? 139.688 105.471 108.274 1.00 5.23   ? 78   ARG E CZ    1 
ATOM   25258 N  NH1   . ARG E 5  78   ? 140.081 106.727 108.348 1.00 4.51   ? 78   ARG E NH1   1 
ATOM   25259 N  NH2   . ARG E 5  78   ? 140.538 104.506 108.601 1.00 9.80   ? 78   ARG E NH2   1 
ATOM   25260 N  N     . LEU E 5  79   ? 134.883 105.883 103.369 1.00 11.12  ? 79   LEU E N     1 
ATOM   25261 C  CA    . LEU E 5  79   ? 135.271 105.205 102.135 1.00 14.24  ? 79   LEU E CA    1 
ATOM   25262 C  C     . LEU E 5  79   ? 135.922 106.170 101.158 1.00 9.55   ? 79   LEU E C     1 
ATOM   25263 O  O     . LEU E 5  79   ? 136.996 105.891 100.613 1.00 12.04  ? 79   LEU E O     1 
ATOM   25264 C  CB    . LEU E 5  79   ? 134.057 104.549 101.482 1.00 10.34  ? 79   LEU E CB    1 
ATOM   25265 C  CG    . LEU E 5  79   ? 133.506 103.223 101.988 1.00 1.36   ? 79   LEU E CG    1 
ATOM   25266 C  CD1   . LEU E 5  79   ? 132.106 103.067 101.472 1.00 8.29   ? 79   LEU E CD1   1 
ATOM   25267 C  CD2   . LEU E 5  79   ? 134.359 102.081 101.532 1.00 4.90   ? 79   LEU E CD2   1 
ATOM   25268 N  N     . VAL E 5  80   ? 135.288 107.320 100.928 1.00 5.74   ? 80   VAL E N     1 
ATOM   25269 C  CA    . VAL E 5  80   ? 135.839 108.295 99.994  1.00 1.93   ? 80   VAL E CA    1 
ATOM   25270 C  C     . VAL E 5  80   ? 137.179 108.829 100.491 1.00 3.90   ? 80   VAL E C     1 
ATOM   25271 O  O     . VAL E 5  80   ? 138.112 108.998 99.706  1.00 3.74   ? 80   VAL E O     1 
ATOM   25272 C  CB    . VAL E 5  80   ? 134.822 109.421 99.737  1.00 3.50   ? 80   VAL E CB    1 
ATOM   25273 C  CG1   . VAL E 5  80   ? 135.447 110.538 98.963  1.00 1.04   ? 80   VAL E CG1   1 
ATOM   25274 C  CG2   . VAL E 5  80   ? 133.640 108.892 98.975  1.00 14.44  ? 80   VAL E CG2   1 
ATOM   25275 N  N     . ALA E 5  81   ? 137.307 109.099 101.790 1.00 9.24   ? 81   ALA E N     1 
ATOM   25276 C  CA    . ALA E 5  81   ? 138.560 109.638 102.313 1.00 15.47  ? 81   ALA E CA    1 
ATOM   25277 C  C     . ALA E 5  81   ? 139.709 108.645 102.174 1.00 8.66   ? 81   ALA E C     1 
ATOM   25278 O  O     . ALA E 5  81   ? 140.817 109.009 101.751 1.00 11.30  ? 81   ALA E O     1 
ATOM   25279 C  CB    . ALA E 5  81   ? 138.378 110.046 103.770 1.00 5.32   ? 81   ALA E CB    1 
ATOM   25280 N  N     . VAL E 5  82   ? 139.465 107.380 102.524 1.00 8.54   ? 82   VAL E N     1 
ATOM   25281 C  CA    . VAL E 5  82   ? 140.500 106.359 102.403 1.00 2.46   ? 82   VAL E CA    1 
ATOM   25282 C  C     . VAL E 5  82   ? 140.909 106.199 100.949 1.00 5.92   ? 82   VAL E C     1 
ATOM   25283 O  O     . VAL E 5  82   ? 142.101 106.152 100.622 1.00 12.73  ? 82   VAL E O     1 
ATOM   25284 C  CB    . VAL E 5  82   ? 140.014 105.028 103.011 1.00 4.75   ? 82   VAL E CB    1 
ATOM   25285 C  CG1   . VAL E 5  82   ? 140.937 103.899 102.647 1.00 1.91   ? 82   VAL E CG1   1 
ATOM   25286 C  CG2   . VAL E 5  82   ? 139.914 105.139 104.506 1.00 0.32   ? 82   VAL E CG2   1 
ATOM   25287 N  N     . ARG E 5  83   ? 139.926 106.135 100.051 1.00 8.66   ? 83   ARG E N     1 
ATOM   25288 C  CA    . ARG E 5  83   ? 140.231 105.974 98.637  1.00 6.70   ? 83   ARG E CA    1 
ATOM   25289 C  C     . ARG E 5  83   ? 141.013 107.161 98.089  1.00 3.57   ? 83   ARG E C     1 
ATOM   25290 O  O     . ARG E 5  83   ? 141.928 106.986 97.283  1.00 14.64  ? 83   ARG E O     1 
ATOM   25291 C  CB    . ARG E 5  83   ? 138.938 105.772 97.863  1.00 12.77  ? 83   ARG E CB    1 
ATOM   25292 C  CG    . ARG E 5  83   ? 139.122 105.440 96.415  1.00 3.60   ? 83   ARG E CG    1 
ATOM   25293 C  CD    . ARG E 5  83   ? 140.101 104.316 96.231  1.00 6.39   ? 83   ARG E CD    1 
ATOM   25294 N  NE    . ARG E 5  83   ? 140.224 103.958 94.826  1.00 14.05  ? 83   ARG E NE    1 
ATOM   25295 C  CZ    . ARG E 5  83   ? 141.328 103.500 94.259  1.00 11.21  ? 83   ARG E CZ    1 
ATOM   25296 N  NH1   . ARG E 5  83   ? 142.440 103.333 94.947  1.00 12.18  ? 83   ARG E NH1   1 
ATOM   25297 N  NH2   . ARG E 5  83   ? 141.315 103.207 92.966  1.00 14.26  ? 83   ARG E NH2   1 
ATOM   25298 N  N     . ALA E 5  84   ? 140.666 108.377 98.502  1.00 3.21   ? 84   ALA E N     1 
ATOM   25299 C  CA    . ALA E 5  84   ? 141.359 109.552 97.999  1.00 3.60   ? 84   ALA E CA    1 
ATOM   25300 C  C     . ALA E 5  84   ? 142.812 109.583 98.452  1.00 15.81  ? 84   ALA E C     1 
ATOM   25301 O  O     . ALA E 5  84   ? 143.703 109.924 97.669  1.00 6.50   ? 84   ALA E O     1 
ATOM   25302 C  CB    . ALA E 5  84   ? 140.622 110.811 98.439  1.00 12.16  ? 84   ALA E CB    1 
ATOM   25303 N  N     . GLN E 5  85   ? 143.076 109.234 99.711  1.00 1.87   ? 85   GLN E N     1 
ATOM   25304 C  CA    . GLN E 5  85   ? 144.465 109.174 100.159 1.00 1.18   ? 85   GLN E CA    1 
ATOM   25305 C  C     . GLN E 5  85   ? 145.244 108.085 99.428  1.00 6.08   ? 85   GLN E C     1 
ATOM   25306 O  O     . GLN E 5  85   ? 146.404 108.284 99.042  1.00 16.46  ? 85   GLN E O     1 
ATOM   25307 C  CB    . GLN E 5  85   ? 144.519 108.956 101.665 1.00 1.66   ? 85   GLN E CB    1 
ATOM   25308 C  CG    . GLN E 5  85   ? 145.915 108.856 102.226 1.00 2.46   ? 85   GLN E CG    1 
ATOM   25309 C  CD    . GLN E 5  85   ? 146.691 110.142 102.124 1.00 4.01   ? 85   GLN E CD    1 
ATOM   25310 O  OE1   . GLN E 5  85   ? 146.298 111.162 102.672 1.00 11.01  ? 85   GLN E OE1   1 
ATOM   25311 N  NE2   . GLN E 5  85   ? 147.806 110.098 101.425 1.00 4.06   ? 85   GLN E NE2   1 
ATOM   25312 N  N     . GLN E 5  86   ? 144.628 106.930 99.213  1.00 5.19   ? 86   GLN E N     1 
ATOM   25313 C  CA    . GLN E 5  86   ? 145.328 105.876 98.500  1.00 7.52   ? 86   GLN E CA    1 
ATOM   25314 C  C     . GLN E 5  86   ? 145.537 106.192 97.026  1.00 5.36   ? 86   GLN E C     1 
ATOM   25315 O  O     . GLN E 5  86   ? 146.444 105.624 96.416  1.00 8.52   ? 86   GLN E O     1 
ATOM   25316 C  CB    . GLN E 5  86   ? 144.578 104.568 98.671  1.00 5.20   ? 86   GLN E CB    1 
ATOM   25317 C  CG    . GLN E 5  86   ? 144.734 103.997 100.044 1.00 3.33   ? 86   GLN E CG    1 
ATOM   25318 C  CD    . GLN E 5  86   ? 143.822 102.837 100.269 1.00 8.26   ? 86   GLN E CD    1 
ATOM   25319 O  OE1   . GLN E 5  86   ? 142.946 102.564 99.459  1.00 12.53  ? 86   GLN E OE1   1 
ATOM   25320 N  NE2   . GLN E 5  86   ? 144.018 102.141 101.368 1.00 11.26  ? 86   GLN E NE2   1 
ATOM   25321 N  N     . LEU E 5  87   ? 144.710 107.056 96.437  1.00 6.66   ? 87   LEU E N     1 
ATOM   25322 C  CA    . LEU E 5  87   ? 144.995 107.573 95.101  1.00 5.33   ? 87   LEU E CA    1 
ATOM   25323 C  C     . LEU E 5  87   ? 146.110 108.602 95.128  1.00 10.17  ? 87   LEU E C     1 
ATOM   25324 O  O     . LEU E 5  87   ? 146.866 108.720 94.163  1.00 12.46  ? 87   LEU E O     1 
ATOM   25325 C  CB    . LEU E 5  87   ? 143.753 108.197 94.488  1.00 6.56   ? 87   LEU E CB    1 
ATOM   25326 C  CG    . LEU E 5  87   ? 142.744 107.236 93.895  1.00 9.40   ? 87   LEU E CG    1 
ATOM   25327 C  CD1   . LEU E 5  87   ? 141.384 107.876 93.932  1.00 5.20   ? 87   LEU E CD1   1 
ATOM   25328 C  CD2   . LEU E 5  87   ? 143.142 106.872 92.496  1.00 9.30   ? 87   LEU E CD2   1 
ATOM   25329 N  N     . ALA E 5  88   ? 146.205 109.380 96.200  1.00 13.44  ? 88   ALA E N     1 
ATOM   25330 C  CA    . ALA E 5  88   ? 147.369 110.233 96.373  1.00 3.16   ? 88   ALA E CA    1 
ATOM   25331 C  C     . ALA E 5  88   ? 148.640 109.417 96.527  1.00 12.58  ? 88   ALA E C     1 
ATOM   25332 O  O     . ALA E 5  88   ? 149.735 109.952 96.343  1.00 21.61  ? 88   ALA E O     1 
ATOM   25333 C  CB    . ALA E 5  88   ? 147.178 111.151 97.575  1.00 0.57   ? 88   ALA E CB    1 
ATOM   25334 N  N     . ILE E 5  89   ? 148.524 108.140 96.883  1.00 15.40  ? 89   ILE E N     1 
ATOM   25335 C  CA    . ILE E 5  89   ? 149.695 107.264 96.926  1.00 15.73  ? 89   ILE E CA    1 
ATOM   25336 C  C     . ILE E 5  89   ? 149.946 106.615 95.568  1.00 19.01  ? 89   ILE E C     1 
ATOM   25337 O  O     . ILE E 5  89   ? 151.056 106.669 95.030  1.00 26.90  ? 89   ILE E O     1 
ATOM   25338 C  CB    . ILE E 5  89   ? 149.531 106.195 98.021  1.00 18.21  ? 89   ILE E CB    1 
ATOM   25339 C  CG1   . ILE E 5  89   ? 149.625 106.809 99.415  1.00 20.69  ? 89   ILE E CG1   1 
ATOM   25340 C  CG2   . ILE E 5  89   ? 150.574 105.128 97.869  1.00 17.47  ? 89   ILE E CG2   1 
ATOM   25341 C  CD1   . ILE E 5  89   ? 149.220 105.839 100.520 1.00 17.19  ? 89   ILE E CD1   1 
ATOM   25342 N  N     . ASN E 5  90   ? 148.930 105.965 95.004  1.00 20.49  ? 90   ASN E N     1 
ATOM   25343 C  CA    . ASN E 5  90   ? 149.123 105.122 93.827  1.00 17.23  ? 90   ASN E CA    1 
ATOM   25344 C  C     . ASN E 5  90   ? 148.776 105.827 92.520  1.00 23.02  ? 90   ASN E C     1 
ATOM   25345 O  O     . ASN E 5  90   ? 149.645 106.033 91.668  1.00 31.09  ? 90   ASN E O     1 
ATOM   25346 C  CB    . ASN E 5  90   ? 148.287 103.849 93.961  1.00 20.74  ? 90   ASN E CB    1 
ATOM   25347 C  CG    . ASN E 5  90   ? 149.001 102.634 93.443  1.00 24.61  ? 90   ASN E CG    1 
ATOM   25348 O  OD1   . ASN E 5  90   ? 150.042 102.248 93.963  1.00 25.07  ? 90   ASN E OD1   1 
ATOM   25349 N  ND2   . ASN E 5  90   ? 148.454 102.027 92.400  1.00 23.94  ? 90   ASN E ND2   1 
ATOM   25350 N  N     . GLY E 5  91   ? 147.515 106.196 92.342  1.00 18.78  ? 91   GLY E N     1 
ATOM   25351 C  CA    . GLY E 5  91   ? 147.075 106.823 91.116  1.00 20.89  ? 91   GLY E CA    1 
ATOM   25352 C  C     . GLY E 5  91   ? 146.369 105.923 90.127  1.00 27.27  ? 91   GLY E C     1 
ATOM   25353 O  O     . GLY E 5  91   ? 145.810 106.430 89.150  1.00 30.41  ? 91   GLY E O     1 
ATOM   25354 N  N     . SER E 5  92   ? 146.349 104.618 90.353  1.00 26.57  ? 92   SER E N     1 
ATOM   25355 C  CA    . SER E 5  92   ? 145.703 103.680 89.445  1.00 28.18  ? 92   SER E CA    1 
ATOM   25356 C  C     . SER E 5  92   ? 144.217 103.570 89.773  1.00 32.00  ? 92   SER E C     1 
ATOM   25357 O  O     . SER E 5  92   ? 143.850 103.311 90.922  1.00 33.26  ? 92   SER E O     1 
ATOM   25358 C  CB    . SER E 5  92   ? 146.377 102.314 89.538  1.00 29.33  ? 92   SER E CB    1 
ATOM   25359 O  OG    . SER E 5  92   ? 145.669 101.347 88.790  1.00 32.39  ? 92   SER E OG    1 
ATOM   25360 N  N     . THR E 5  93   ? 143.369 103.734 88.758  1.00 31.12  ? 93   THR E N     1 
ATOM   25361 C  CA    . THR E 5  93   ? 141.924 103.677 88.922  1.00 31.32  ? 93   THR E CA    1 
ATOM   25362 C  C     . THR E 5  93   ? 141.292 103.010 87.708  1.00 33.51  ? 93   THR E C     1 
ATOM   25363 O  O     . THR E 5  93   ? 141.925 102.875 86.660  1.00 39.67  ? 93   THR E O     1 
ATOM   25364 C  CB    . THR E 5  93   ? 141.321 105.075 89.115  1.00 31.50  ? 93   THR E CB    1 
ATOM   25365 O  OG1   . THR E 5  93   ? 139.894 104.985 89.112  1.00 34.78  ? 93   THR E OG1   1 
ATOM   25366 C  CG2   . THR E 5  93   ? 141.756 106.007 88.015  1.00 30.61  ? 93   THR E CG2   1 
ATOM   25367 N  N     . MET E 5  94   ? 140.043 102.573 87.865  1.00 34.55  ? 94   MET E N     1 
ATOM   25368 C  CA    . MET E 5  94   ? 139.233 102.104 86.747  1.00 34.61  ? 94   MET E CA    1 
ATOM   25369 C  C     . MET E 5  94   ? 138.242 103.138 86.252  1.00 34.00  ? 94   MET E C     1 
ATOM   25370 O  O     . MET E 5  94   ? 137.497 102.861 85.311  1.00 34.33  ? 94   MET E O     1 
ATOM   25371 C  CB    . MET E 5  94   ? 138.456 100.848 87.117  1.00 36.00  ? 94   MET E CB    1 
ATOM   25372 C  CG    . MET E 5  94   ? 139.283 99.706  87.595  1.00 37.77  ? 94   MET E CG    1 
ATOM   25373 S  SD    . MET E 5  94   ? 138.234 98.263  87.577  1.00 48.40  ? 94   MET E SD    1 
ATOM   25374 C  CE    . MET E 5  94   ? 138.132 97.988  85.810  1.00 37.22  ? 94   MET E CE    1 
ATOM   25375 N  N     . LEU E 5  95   ? 138.200 104.307 86.872  1.00 33.58  ? 95   LEU E N     1 
ATOM   25376 C  CA    . LEU E 5  95   ? 137.259 105.336 86.465  1.00 34.85  ? 95   LEU E CA    1 
ATOM   25377 C  C     . LEU E 5  95   ? 137.655 105.878 85.099  1.00 39.73  ? 95   LEU E C     1 
ATOM   25378 O  O     . LEU E 5  95   ? 138.748 106.423 84.929  1.00 40.99  ? 95   LEU E O     1 
ATOM   25379 C  CB    . LEU E 5  95   ? 137.239 106.445 87.514  1.00 32.40  ? 95   LEU E CB    1 
ATOM   25380 C  CG    . LEU E 5  95   ? 136.127 107.479 87.473  1.00 32.88  ? 95   LEU E CG    1 
ATOM   25381 C  CD1   . LEU E 5  95   ? 134.796 106.814 87.714  1.00 33.63  ? 95   LEU E CD1   1 
ATOM   25382 C  CD2   . LEU E 5  95   ? 136.402 108.530 88.513  1.00 30.89  ? 95   LEU E CD2   1 
ATOM   25383 N  N     . LYS E 5  96   ? 136.762 105.719 84.120  1.00 38.36  ? 96   LYS E N     1 
ATOM   25384 C  CA    . LYS E 5  96   ? 137.121 106.019 82.737  1.00 33.28  ? 96   LYS E CA    1 
ATOM   25385 C  C     . LYS E 5  96   ? 137.376 107.504 82.522  1.00 34.77  ? 96   LYS E C     1 
ATOM   25386 O  O     . LYS E 5  96   ? 138.364 107.882 81.885  1.00 36.22  ? 96   LYS E O     1 
ATOM   25387 C  CB    . LYS E 5  96   ? 136.025 105.528 81.788  1.00 32.15  ? 96   LYS E CB    1 
ATOM   25388 C  CG    . LYS E 5  96   ? 135.981 104.015 81.450  1.00 34.72  ? 96   LYS E CG    1 
ATOM   25389 C  CD    . LYS E 5  96   ? 137.279 103.174 81.529  1.00 37.96  ? 96   LYS E CD    1 
ATOM   25390 C  CE    . LYS E 5  96   ? 138.535 103.793 80.913  1.00 36.40  ? 96   LYS E CE    1 
ATOM   25391 N  NZ    . LYS E 5  96   ? 139.743 102.977 81.200  1.00 34.13  ? 96   LYS E NZ    1 
ATOM   25392 N  N     . LYS E 5  97   ? 136.502 108.357 83.031  1.00 34.77  ? 97   LYS E N     1 
ATOM   25393 C  CA    . LYS E 5  97   ? 136.640 109.790 82.842  1.00 36.42  ? 97   LYS E CA    1 
ATOM   25394 C  C     . LYS E 5  97   ? 137.825 110.313 83.644  1.00 38.67  ? 97   LYS E C     1 
ATOM   25395 O  O     . LYS E 5  97   ? 138.174 109.774 84.696  1.00 41.77  ? 97   LYS E O     1 
ATOM   25396 C  CB    . LYS E 5  97   ? 135.360 110.509 83.257  1.00 34.87  ? 97   LYS E CB    1 
ATOM   25397 C  CG    . LYS E 5  97   ? 134.991 111.648 82.342  1.00 35.97  ? 97   LYS E CG    1 
ATOM   25398 C  CD    . LYS E 5  97   ? 133.633 112.224 82.683  1.00 36.65  ? 97   LYS E CD    1 
ATOM   25399 C  CE    . LYS E 5  97   ? 133.783 113.509 83.466  1.00 39.01  ? 97   LYS E CE    1 
ATOM   25400 N  NZ    . LYS E 5  97   ? 132.516 114.279 83.514  1.00 39.91  ? 97   LYS E NZ    1 
ATOM   25401 N  N     . LYS E 5  98   ? 138.446 111.372 83.138  1.00 33.22  ? 98   LYS E N     1 
ATOM   25402 C  CA    . LYS E 5  98   ? 139.674 111.898 83.715  1.00 32.17  ? 98   LYS E CA    1 
ATOM   25403 C  C     . LYS E 5  98   ? 139.377 113.070 84.639  1.00 33.49  ? 98   LYS E C     1 
ATOM   25404 O  O     . LYS E 5  98   ? 138.619 113.976 84.280  1.00 36.53  ? 98   LYS E O     1 
ATOM   25405 C  CB    . LYS E 5  98   ? 140.648 112.323 82.618  1.00 35.18  ? 98   LYS E CB    1 
ATOM   25406 C  CG    . LYS E 5  98   ? 141.140 111.170 81.772  1.00 37.63  ? 98   LYS E CG    1 
ATOM   25407 C  CD    . LYS E 5  98   ? 141.634 110.028 82.645  1.00 36.60  ? 98   LYS E CD    1 
ATOM   25408 C  CE    . LYS E 5  98   ? 141.949 108.793 81.819  1.00 34.14  ? 98   LYS E CE    1 
ATOM   25409 N  NZ    . LYS E 5  98   ? 143.195 108.953 81.025  1.00 35.80  ? 98   LYS E NZ    1 
ATOM   25410 N  N     . TYR E 5  99   ? 139.981 113.044 85.824  1.00 28.16  ? 99   TYR E N     1 
ATOM   25411 C  CA    . TYR E 5  99   ? 139.865 114.106 86.811  1.00 26.44  ? 99   TYR E CA    1 
ATOM   25412 C  C     . TYR E 5  99   ? 141.255 114.464 87.310  1.00 25.14  ? 99   TYR E C     1 
ATOM   25413 O  O     . TYR E 5  99   ? 142.191 113.672 87.215  1.00 25.52  ? 99   TYR E O     1 
ATOM   25414 C  CB    . TYR E 5  99   ? 138.983 113.694 87.992  1.00 25.41  ? 99   TYR E CB    1 
ATOM   25415 C  CG    . TYR E 5  99   ? 137.552 113.415 87.631  1.00 26.35  ? 99   TYR E CG    1 
ATOM   25416 C  CD1   . TYR E 5  99   ? 137.121 112.127 87.389  1.00 28.23  ? 99   TYR E CD1   1 
ATOM   25417 C  CD2   . TYR E 5  99   ? 136.628 114.436 87.561  1.00 26.32  ? 99   TYR E CD2   1 
ATOM   25418 C  CE1   . TYR E 5  99   ? 135.816 111.869 87.059  1.00 29.35  ? 99   TYR E CE1   1 
ATOM   25419 C  CE2   . TYR E 5  99   ? 135.322 114.186 87.241  1.00 28.18  ? 99   TYR E CE2   1 
ATOM   25420 C  CZ    . TYR E 5  99   ? 134.922 112.903 86.991  1.00 30.73  ? 99   TYR E CZ    1 
ATOM   25421 O  OH    . TYR E 5  99   ? 133.615 112.654 86.667  1.00 30.83  ? 99   TYR E OH    1 
ATOM   25422 N  N     . SER E 5  100  ? 141.384 115.671 87.848  1.00 19.69  ? 100  SER E N     1 
ATOM   25423 C  CA    . SER E 5  100  ? 142.675 116.172 88.293  1.00 17.50  ? 100  SER E CA    1 
ATOM   25424 C  C     . SER E 5  100  ? 142.841 116.151 89.807  1.00 17.90  ? 100  SER E C     1 
ATOM   25425 O  O     . SER E 5  100  ? 143.840 116.663 90.314  1.00 21.15  ? 100  SER E O     1 
ATOM   25426 C  CB    . SER E 5  100  ? 142.894 117.584 87.764  1.00 21.28  ? 100  SER E CB    1 
ATOM   25427 O  OG    . SER E 5  100  ? 143.862 118.244 88.541  1.00 30.09  ? 100  SER E OG    1 
ATOM   25428 N  N     . SER E 5  101  ? 141.901 115.569 90.540  1.00 22.47  ? 101  SER E N     1 
ATOM   25429 C  CA    . SER E 5  101  ? 141.964 115.528 91.989  1.00 18.12  ? 101  SER E CA    1 
ATOM   25430 C  C     . SER E 5  101  ? 141.680 114.117 92.467  1.00 18.21  ? 101  SER E C     1 
ATOM   25431 O  O     . SER E 5  101  ? 140.872 113.409 91.860  1.00 23.52  ? 101  SER E O     1 
ATOM   25432 C  CB    . SER E 5  101  ? 140.955 116.494 92.624  1.00 20.15  ? 101  SER E CB    1 
ATOM   25433 O  OG    . SER E 5  101  ? 141.429 116.978 93.865  1.00 29.50  ? 101  SER E OG    1 
ATOM   25434 N  N     . PRO E 5  102  ? 142.340 113.677 93.538  1.00 13.52  ? 102  PRO E N     1 
ATOM   25435 C  CA    . PRO E 5  102  ? 141.983 112.384 94.137  1.00 9.15   ? 102  PRO E CA    1 
ATOM   25436 C  C     . PRO E 5  102  ? 140.570 112.352 94.683  1.00 9.68   ? 102  PRO E C     1 
ATOM   25437 O  O     . PRO E 5  102  ? 139.921 111.302 94.652  1.00 12.74  ? 102  PRO E O     1 
ATOM   25438 C  CB    . PRO E 5  102  ? 143.013 112.222 95.263  1.00 4.77   ? 102  PRO E CB    1 
ATOM   25439 C  CG    . PRO E 5  102  ? 144.020 113.257 95.044  1.00 12.37  ? 102  PRO E CG    1 
ATOM   25440 C  CD    . PRO E 5  102  ? 143.377 114.367 94.312  1.00 13.80  ? 102  PRO E CD    1 
ATOM   25441 N  N     . ILE E 5  103  ? 140.077 113.484 95.184  1.00 6.84   ? 103  ILE E N     1 
ATOM   25442 C  CA    . ILE E 5  103  ? 138.762 113.531 95.808  1.00 8.41   ? 103  ILE E CA    1 
ATOM   25443 C  C     . ILE E 5  103  ? 137.663 113.342 94.771  1.00 11.97  ? 103  ILE E C     1 
ATOM   25444 O  O     . ILE E 5  103  ? 136.687 112.622 95.007  1.00 17.50  ? 103  ILE E O     1 
ATOM   25445 C  CB    . ILE E 5  103  ? 138.609 114.846 96.593  1.00 13.19  ? 103  ILE E CB    1 
ATOM   25446 C  CG1   . ILE E 5  103  ? 139.718 114.952 97.645  1.00 13.05  ? 103  ILE E CG1   1 
ATOM   25447 C  CG2   . ILE E 5  103  ? 137.260 114.924 97.243  1.00 11.22  ? 103  ILE E CG2   1 
ATOM   25448 C  CD1   . ILE E 5  103  ? 139.631 116.143 98.548  1.00 2.94   ? 103  ILE E CD1   1 
ATOM   25449 N  N     . ASP E 5  104  ? 137.805 113.972 93.606  1.00 16.95  ? 104  ASP E N     1 
ATOM   25450 C  CA    . ASP E 5  104  ? 136.829 113.792 92.536  1.00 16.06  ? 104  ASP E CA    1 
ATOM   25451 C  C     . ASP E 5  104  ? 136.817 112.359 92.027  1.00 18.98  ? 104  ASP E C     1 
ATOM   25452 O  O     . ASP E 5  104  ? 135.748 111.787 91.777  1.00 23.26  ? 104  ASP E O     1 
ATOM   25453 C  CB    . ASP E 5  104  ? 137.130 114.752 91.395  1.00 21.14  ? 104  ASP E CB    1 
ATOM   25454 C  CG    . ASP E 5  104  ? 136.800 116.176 91.741  1.00 26.09  ? 104  ASP E CG    1 
ATOM   25455 O  OD1   . ASP E 5  104  ? 137.487 116.743 92.612  1.00 27.30  ? 104  ASP E OD1   1 
ATOM   25456 O  OD2   . ASP E 5  104  ? 135.856 116.732 91.146  1.00 28.37  ? 104  ASP E OD2   1 
ATOM   25457 N  N     . ILE E 5  105  ? 137.997 111.762 91.872  1.00 11.96  ? 105  ILE E N     1 
ATOM   25458 C  CA    . ILE E 5  105  ? 138.077 110.377 91.432  1.00 10.82  ? 105  ILE E CA    1 
ATOM   25459 C  C     . ILE E 5  105  ? 137.397 109.464 92.440  1.00 14.03  ? 105  ILE E C     1 
ATOM   25460 O  O     . ILE E 5  105  ? 136.615 108.586 92.072  1.00 25.58  ? 105  ILE E O     1 
ATOM   25461 C  CB    . ILE E 5  105  ? 139.543 109.970 91.197  1.00 17.83  ? 105  ILE E CB    1 
ATOM   25462 C  CG1   . ILE E 5  105  ? 140.181 110.846 90.121  1.00 14.14  ? 105  ILE E CG1   1 
ATOM   25463 C  CG2   . ILE E 5  105  ? 139.633 108.524 90.787  1.00 13.91  ? 105  ILE E CG2   1 
ATOM   25464 C  CD1   . ILE E 5  105  ? 141.664 110.686 90.015  1.00 11.22  ? 105  ILE E CD1   1 
ATOM   25465 N  N     . ALA E 5  106  ? 137.672 109.662 93.729  1.00 11.86  ? 106  ALA E N     1 
ATOM   25466 C  CA    . ALA E 5  106  ? 137.090 108.793 94.748  1.00 4.49   ? 106  ALA E CA    1 
ATOM   25467 C  C     . ALA E 5  106  ? 135.577 108.943 94.824  1.00 7.71   ? 106  ALA E C     1 
ATOM   25468 O  O     . ALA E 5  106  ? 134.853 107.946 94.929  1.00 14.22  ? 106  ALA E O     1 
ATOM   25469 C  CB    . ALA E 5  106  ? 137.724 109.084 96.100  1.00 6.38   ? 106  ALA E CB    1 
ATOM   25470 N  N     . LYS E 5  107  ? 135.079 110.178 94.768  1.00 10.07  ? 107  LYS E N     1 
ATOM   25471 C  CA    . LYS E 5  107  ? 133.640 110.392 94.804  1.00 9.84   ? 107  LYS E CA    1 
ATOM   25472 C  C     . LYS E 5  107  ? 132.953 109.742 93.616  1.00 13.89  ? 107  LYS E C     1 
ATOM   25473 O  O     . LYS E 5  107  ? 131.912 109.093 93.770  1.00 23.98  ? 107  LYS E O     1 
ATOM   25474 C  CB    . LYS E 5  107  ? 133.339 111.883 94.832  1.00 9.99   ? 107  LYS E CB    1 
ATOM   25475 C  CG    . LYS E 5  107  ? 133.392 112.492 96.194  1.00 10.01  ? 107  LYS E CG    1 
ATOM   25476 C  CD    . LYS E 5  107  ? 132.516 113.701 96.269  1.00 14.05  ? 107  LYS E CD    1 
ATOM   25477 C  CE    . LYS E 5  107  ? 133.324 114.951 96.526  1.00 15.46  ? 107  LYS E CE    1 
ATOM   25478 N  NZ    . LYS E 5  107  ? 132.603 116.156 96.040  1.00 15.45  ? 107  LYS E NZ    1 
ATOM   25479 N  N     . GLN E 5  108  ? 133.511 109.907 92.416  1.00 15.76  ? 108  GLN E N     1 
ATOM   25480 C  CA    . GLN E 5  108  ? 132.881 109.304 91.250  1.00 15.25  ? 108  GLN E CA    1 
ATOM   25481 C  C     . GLN E 5  108  ? 133.014 107.792 91.254  1.00 17.21  ? 108  GLN E C     1 
ATOM   25482 O  O     . GLN E 5  108  ? 132.148 107.099 90.720  1.00 23.00  ? 108  GLN E O     1 
ATOM   25483 C  CB    . GLN E 5  108  ? 133.458 109.895 89.970  1.00 15.08  ? 108  GLN E CB    1 
ATOM   25484 C  CG    . GLN E 5  108  ? 133.125 111.351 89.790  1.00 15.73  ? 108  GLN E CG    1 
ATOM   25485 C  CD    . GLN E 5  108  ? 131.632 111.594 89.793  1.00 24.68  ? 108  GLN E CD    1 
ATOM   25486 O  OE1   . GLN E 5  108  ? 130.877 110.873 89.148  1.00 22.38  ? 108  GLN E OE1   1 
ATOM   25487 N  NE2   . GLN E 5  108  ? 131.197 112.599 90.539  1.00 22.31  ? 108  GLN E NE2   1 
ATOM   25488 N  N     . GLU E 5  109  ? 134.081 107.262 91.838  1.00 16.01  ? 109  GLU E N     1 
ATOM   25489 C  CA    . GLU E 5  109  ? 134.187 105.820 91.997  1.00 11.71  ? 109  GLU E CA    1 
ATOM   25490 C  C     . GLU E 5  109  ? 133.101 105.288 92.917  1.00 15.70  ? 109  GLU E C     1 
ATOM   25491 O  O     . GLU E 5  109  ? 132.526 104.229 92.654  1.00 21.96  ? 109  GLU E O     1 
ATOM   25492 C  CB    . GLU E 5  109  ? 135.566 105.458 92.534  1.00 15.70  ? 109  GLU E CB    1 
ATOM   25493 C  CG    . GLU E 5  109  ? 136.480 104.834 91.525  1.00 18.87  ? 109  GLU E CG    1 
ATOM   25494 C  CD    . GLU E 5  109  ? 137.876 104.677 92.050  1.00 18.17  ? 109  GLU E CD    1 
ATOM   25495 O  OE1   . GLU E 5  109  ? 138.035 104.544 93.276  1.00 15.52  ? 109  GLU E OE1   1 
ATOM   25496 O  OE2   . GLU E 5  109  ? 138.821 104.680 91.242  1.00 24.50  ? 109  GLU E OE2   1 
ATOM   25497 N  N     . LEU E 5  110  ? 132.813 105.998 94.007  1.00 15.48  ? 110  LEU E N     1 
ATOM   25498 C  CA    . LEU E 5  110  ? 131.734 105.574 94.893  1.00 12.08  ? 110  LEU E CA    1 
ATOM   25499 C  C     . LEU E 5  110  ? 130.385 105.646 94.196  1.00 9.73   ? 110  LEU E C     1 
ATOM   25500 O  O     . LEU E 5  110  ? 129.581 104.715 94.284  1.00 18.25  ? 110  LEU E O     1 
ATOM   25501 C  CB    . LEU E 5  110  ? 131.713 106.421 96.161  1.00 13.40  ? 110  LEU E CB    1 
ATOM   25502 C  CG    . LEU E 5  110  ? 130.612 106.067 97.167  1.00 8.71   ? 110  LEU E CG    1 
ATOM   25503 C  CD1   . LEU E 5  110  ? 130.964 104.833 97.977  1.00 9.10   ? 110  LEU E CD1   1 
ATOM   25504 C  CD2   . LEU E 5  110  ? 130.306 107.233 98.061  1.00 7.63   ? 110  LEU E CD2   1 
ATOM   25505 N  N     . PHE E 5  111  ? 130.114 106.749 93.497  1.00 10.45  ? 111  PHE E N     1 
ATOM   25506 C  CA    . PHE E 5  111  ? 128.802 106.916 92.880  1.00 13.45  ? 111  PHE E CA    1 
ATOM   25507 C  C     . PHE E 5  111  ? 128.590 105.937 91.737  1.00 15.83  ? 111  PHE E C     1 
ATOM   25508 O  O     . PHE E 5  111  ? 127.456 105.537 91.459  1.00 19.48  ? 111  PHE E O     1 
ATOM   25509 C  CB    . PHE E 5  111  ? 128.629 108.349 92.395  1.00 14.35  ? 111  PHE E CB    1 
ATOM   25510 C  CG    . PHE E 5  111  ? 128.565 109.347 93.500  1.00 18.00  ? 111  PHE E CG    1 
ATOM   25511 C  CD1   . PHE E 5  111  ? 127.960 109.024 94.700  1.00 20.71  ? 111  PHE E CD1   1 
ATOM   25512 C  CD2   . PHE E 5  111  ? 129.139 110.593 93.360  1.00 17.56  ? 111  PHE E CD2   1 
ATOM   25513 C  CE1   . PHE E 5  111  ? 127.908 109.932 95.726  1.00 18.39  ? 111  PHE E CE1   1 
ATOM   25514 C  CE2   . PHE E 5  111  ? 129.092 111.506 94.390  1.00 19.41  ? 111  PHE E CE2   1 
ATOM   25515 C  CZ    . PHE E 5  111  ? 128.476 111.173 95.572  1.00 19.72  ? 111  PHE E CZ    1 
ATOM   25516 N  N     . ASN E 5  112  ? 129.662 105.544 91.060  1.00 18.42  ? 112  ASN E N     1 
ATOM   25517 C  CA    . ASN E 5  112  ? 129.589 104.644 89.919  1.00 16.75  ? 112  ASN E CA    1 
ATOM   25518 C  C     . ASN E 5  112  ? 129.917 103.202 90.272  1.00 21.48  ? 112  ASN E C     1 
ATOM   25519 O  O     . ASN E 5  112  ? 130.068 102.381 89.366  1.00 23.51  ? 112  ASN E O     1 
ATOM   25520 C  CB    . ASN E 5  112  ? 130.519 105.129 88.810  1.00 17.17  ? 112  ASN E CB    1 
ATOM   25521 C  CG    . ASN E 5  112  ? 130.015 106.385 88.142  1.00 21.18  ? 112  ASN E CG    1 
ATOM   25522 O  OD1   . ASN E 5  112  ? 128.850 106.479 87.772  1.00 21.37  ? 112  ASN E OD1   1 
ATOM   25523 N  ND2   . ASN E 5  112  ? 130.888 107.359 87.988  1.00 19.43  ? 112  ASN E ND2   1 
ATOM   25524 N  N     . ARG E 5  113  ? 130.052 102.885 91.557  1.00 16.76  ? 113  ARG E N     1 
ATOM   25525 C  CA    . ARG E 5  113  ? 130.149 101.509 92.038  1.00 12.71  ? 113  ARG E CA    1 
ATOM   25526 C  C     . ARG E 5  113  ? 131.398 100.811 91.501  1.00 14.55  ? 113  ARG E C     1 
ATOM   25527 O  O     . ARG E 5  113  ? 131.342 99.728  90.924  1.00 17.24  ? 113  ARG E O     1 
ATOM   25528 C  CB    . ARG E 5  113  ? 128.872 100.742 91.694  1.00 14.63  ? 113  ARG E CB    1 
ATOM   25529 C  CG    . ARG E 5  113  ? 127.647 101.431 92.245  1.00 14.68  ? 113  ARG E CG    1 
ATOM   25530 C  CD    . ARG E 5  113  ? 126.380 100.644 92.058  1.00 15.15  ? 113  ARG E CD    1 
ATOM   25531 N  NE    . ARG E 5  113  ? 125.233 101.394 92.557  1.00 22.54  ? 113  ARG E NE    1 
ATOM   25532 C  CZ    . ARG E 5  113  ? 124.866 101.447 93.830  1.00 15.65  ? 113  ARG E CZ    1 
ATOM   25533 N  NH1   . ARG E 5  113  ? 125.521 100.789 94.768  1.00 9.63   ? 113  ARG E NH1   1 
ATOM   25534 N  NH2   . ARG E 5  113  ? 123.813 102.180 94.171  1.00 16.21  ? 113  ARG E NH2   1 
ATOM   25535 N  N     . LYS E 5  114  ? 132.542 101.456 91.729  1.00 20.86  ? 114  LYS E N     1 
ATOM   25536 C  CA    . LYS E 5  114  ? 133.836 100.947 91.301  1.00 15.93  ? 114  LYS E CA    1 
ATOM   25537 C  C     . LYS E 5  114  ? 134.878 100.985 92.409  1.00 18.45  ? 114  LYS E C     1 
ATOM   25538 O  O     . LYS E 5  114  ? 136.052 100.728 92.141  1.00 24.24  ? 114  LYS E O     1 
ATOM   25539 C  CB    . LYS E 5  114  ? 134.355 101.743 90.100  1.00 11.00  ? 114  LYS E CB    1 
ATOM   25540 C  CG    . LYS E 5  114  ? 133.670 101.442 88.805  1.00 15.34  ? 114  LYS E CG    1 
ATOM   25541 C  CD    . LYS E 5  114  ? 134.046 102.466 87.776  1.00 21.70  ? 114  LYS E CD    1 
ATOM   25542 C  CE    . LYS E 5  114  ? 133.321 102.236 86.465  1.00 22.21  ? 114  LYS E CE    1 
ATOM   25543 N  NZ    . LYS E 5  114  ? 133.418 103.431 85.590  1.00 22.94  ? 114  LYS E NZ    1 
ATOM   25544 N  N     . ILE E 5  115  ? 134.489 101.299 93.635  1.00 13.90  ? 115  ILE E N     1 
ATOM   25545 C  CA    . ILE E 5  115  ? 135.445 101.544 94.710  1.00 16.04  ? 115  ILE E CA    1 
ATOM   25546 C  C     . ILE E 5  115  ? 135.919 100.211 95.286  1.00 16.08  ? 115  ILE E C     1 
ATOM   25547 O  O     . ILE E 5  115  ? 135.099 99.372  95.676  1.00 20.72  ? 115  ILE E O     1 
ATOM   25548 C  CB    . ILE E 5  115  ? 134.827 102.487 95.759  1.00 16.91  ? 115  ILE E CB    1 
ATOM   25549 C  CG1   . ILE E 5  115  ? 135.861 102.946 96.781  1.00 13.16  ? 115  ILE E CG1   1 
ATOM   25550 C  CG2   . ILE E 5  115  ? 133.599 101.870 96.409  1.00 15.23  ? 115  ILE E CG2   1 
ATOM   25551 C  CD1   . ILE E 5  115  ? 135.519 104.256 97.407  1.00 10.95  ? 115  ILE E CD1   1 
ATOM   25552 N  N     . PRO E 5  116  ? 137.231 99.956  95.328  1.00 13.99  ? 116  PRO E N     1 
ATOM   25553 C  CA    . PRO E 5  116  ? 137.750 98.638  95.707  1.00 9.69   ? 116  PRO E CA    1 
ATOM   25554 C  C     . PRO E 5  116  ? 137.987 98.468  97.203  1.00 11.86  ? 116  PRO E C     1 
ATOM   25555 O  O     . PRO E 5  116  ? 139.093 98.156  97.647  1.00 17.28  ? 116  PRO E O     1 
ATOM   25556 C  CB    . PRO E 5  116  ? 139.069 98.569  94.930  1.00 16.38  ? 116  PRO E CB    1 
ATOM   25557 C  CG    . PRO E 5  116  ? 139.527 99.958  94.908  1.00 11.39  ? 116  PRO E CG    1 
ATOM   25558 C  CD    . PRO E 5  116  ? 138.309 100.841 94.865  1.00 12.82  ? 116  PRO E CD    1 
ATOM   25559 N  N     . LEU E 5  117  ? 136.942 98.668  97.996  1.00 13.23  ? 117  LEU E N     1 
ATOM   25560 C  CA    . LEU E 5  117  ? 137.030 98.563  99.441  1.00 4.90   ? 117  LEU E CA    1 
ATOM   25561 C  C     . LEU E 5  117  ? 135.803 97.835  99.964  1.00 7.89   ? 117  LEU E C     1 
ATOM   25562 O  O     . LEU E 5  117  ? 134.800 97.697  99.266  1.00 19.48  ? 117  LEU E O     1 
ATOM   25563 C  CB    . LEU E 5  117  ? 137.159 99.945  100.090 1.00 7.23   ? 117  LEU E CB    1 
ATOM   25564 C  CG    . LEU E 5  117  ? 138.388 100.785 99.738  1.00 2.97   ? 117  LEU E CG    1 
ATOM   25565 C  CD1   . LEU E 5  117  ? 138.236 102.199 100.226 1.00 1.30   ? 117  LEU E CD1   1 
ATOM   25566 C  CD2   . LEU E 5  117  ? 139.624 100.167 100.329 1.00 5.58   ? 117  LEU E CD2   1 
ATOM   25567 N  N     . LEU E 5  118  ? 135.899 97.350  101.197 1.00 0.42   ? 118  LEU E N     1 
ATOM   25568 C  CA    . LEU E 5  118  ? 134.794 96.682  101.866 1.00 0.45   ? 118  LEU E CA    1 
ATOM   25569 C  C     . LEU E 5  118  ? 134.584 97.295  103.244 1.00 4.70   ? 118  LEU E C     1 
ATOM   25570 O  O     . LEU E 5  118  ? 135.497 97.879  103.823 1.00 7.12   ? 118  LEU E O     1 
ATOM   25571 C  CB    . LEU E 5  118  ? 135.045 95.180  101.996 1.00 4.47   ? 118  LEU E CB    1 
ATOM   25572 C  CG    . LEU E 5  118  ? 135.220 94.351  100.728 1.00 6.30   ? 118  LEU E CG    1 
ATOM   25573 C  CD1   . LEU E 5  118  ? 135.691 92.979  101.100 1.00 3.53   ? 118  LEU E CD1   1 
ATOM   25574 C  CD2   . LEU E 5  118  ? 133.943 94.275  99.939  1.00 1.67   ? 118  LEU E CD2   1 
ATOM   25575 N  N     . VAL E 5  119  ? 133.370 97.154  103.766 1.00 6.50   ? 119  VAL E N     1 
ATOM   25576 C  CA    . VAL E 5  119  ? 132.997 97.680  105.076 1.00 0.20   ? 119  VAL E CA    1 
ATOM   25577 C  C     . VAL E 5  119  ? 132.840 96.511  106.038 1.00 9.16   ? 119  VAL E C     1 
ATOM   25578 O  O     . VAL E 5  119  ? 132.059 95.592  105.782 1.00 1.61   ? 119  VAL E O     1 
ATOM   25579 C  CB    . VAL E 5  119  ? 131.705 98.510  105.008 1.00 0.61   ? 119  VAL E CB    1 
ATOM   25580 C  CG1   . VAL E 5  119  ? 131.308 98.981  106.382 1.00 15.68  ? 119  VAL E CG1   1 
ATOM   25581 C  CG2   . VAL E 5  119  ? 131.874 99.689  104.077 1.00 14.50  ? 119  VAL E CG2   1 
ATOM   25582 N  N     . MET E 5  120  ? 133.575 96.548  107.147 1.00 3.75   ? 120  MET E N     1 
ATOM   25583 C  CA    . MET E 5  120  ? 133.493 95.534  108.192 1.00 1.24   ? 120  MET E CA    1 
ATOM   25584 C  C     . MET E 5  120  ? 132.771 96.104  109.403 1.00 0.75   ? 120  MET E C     1 
ATOM   25585 O  O     . MET E 5  120  ? 133.216 97.091  109.989 1.00 1.54   ? 120  MET E O     1 
ATOM   25586 C  CB    . MET E 5  120  ? 134.883 95.042  108.587 1.00 0.15   ? 120  MET E CB    1 
ATOM   25587 C  CG    . MET E 5  120  ? 134.943 93.579  108.962 1.00 13.20  ? 120  MET E CG    1 
ATOM   25588 S  SD    . MET E 5  120  ? 136.538 93.028  109.584 1.00 16.75  ? 120  MET E SD    1 
ATOM   25589 C  CE    . MET E 5  120  ? 136.616 93.874  111.146 1.00 8.53   ? 120  MET E CE    1 
ATOM   25590 N  N     . ARG E 5  121  ? 131.669 95.475  109.778 1.00 0.15   ? 121  ARG E N     1 
ATOM   25591 C  CA    . ARG E 5  121  ? 130.857 95.893  110.911 1.00 8.89   ? 121  ARG E CA    1 
ATOM   25592 C  C     . ARG E 5  121  ? 131.019 94.851  112.006 1.00 6.59   ? 121  ARG E C     1 
ATOM   25593 O  O     . ARG E 5  121  ? 130.554 93.722  111.862 1.00 8.97   ? 121  ARG E O     1 
ATOM   25594 C  CB    . ARG E 5  121  ? 129.396 96.049  110.495 1.00 15.83  ? 121  ARG E CB    1 
ATOM   25595 C  CG    . ARG E 5  121  ? 129.138 97.226  109.582 1.00 5.16   ? 121  ARG E CG    1 
ATOM   25596 C  CD    . ARG E 5  121  ? 127.730 97.210  109.071 1.00 5.28   ? 121  ARG E CD    1 
ATOM   25597 N  NE    . ARG E 5  121  ? 127.365 98.431  108.369 1.00 6.22   ? 121  ARG E NE    1 
ATOM   25598 C  CZ    . ARG E 5  121  ? 126.314 98.549  107.574 1.00 6.13   ? 121  ARG E CZ    1 
ATOM   25599 N  NH1   . ARG E 5  121  ? 125.501 97.541  107.356 1.00 6.58   ? 121  ARG E NH1   1 
ATOM   25600 N  NH2   . ARG E 5  121  ? 126.080 99.707  106.975 1.00 1.64   ? 121  ARG E NH2   1 
ATOM   25601 N  N     . CYS E 5  122  ? 131.696 95.216  113.085 1.00 6.44   ? 122  CYS E N     1 
ATOM   25602 C  CA    . CYS E 5  122  ? 131.980 94.280  114.162 1.00 11.45  ? 122  CYS E CA    1 
ATOM   25603 C  C     . CYS E 5  122  ? 130.782 94.202  115.093 1.00 15.10  ? 122  CYS E C     1 
ATOM   25604 O  O     . CYS E 5  122  ? 130.429 95.185  115.746 1.00 7.96   ? 122  CYS E O     1 
ATOM   25605 C  CB    . CYS E 5  122  ? 133.228 94.695  114.929 1.00 2.98   ? 122  CYS E CB    1 
ATOM   25606 S  SG    . CYS E 5  122  ? 133.605 93.612  116.328 1.00 24.87  ? 122  CYS E SG    1 
ATOM   25607 N  N     . ILE E 5  123  ? 130.180 93.022  115.190 1.00 1.78   ? 123  ILE E N     1 
ATOM   25608 C  CA    . ILE E 5  123  ? 128.980 92.871  115.996 1.00 0.06   ? 123  ILE E CA    1 
ATOM   25609 C  C     . ILE E 5  123  ? 129.334 92.564  117.444 1.00 9.48   ? 123  ILE E C     1 
ATOM   25610 O  O     . ILE E 5  123  ? 128.888 93.258  118.362 1.00 15.02  ? 123  ILE E O     1 
ATOM   25611 C  CB    . ILE E 5  123  ? 128.066 91.795  115.385 1.00 1.44   ? 123  ILE E CB    1 
ATOM   25612 C  CG1   . ILE E 5  123  ? 127.739 92.144  113.933 1.00 3.26   ? 123  ILE E CG1   1 
ATOM   25613 C  CG2   . ILE E 5  123  ? 126.810 91.638  116.196 1.00 4.99   ? 123  ILE E CG2   1 
ATOM   25614 C  CD1   . ILE E 5  123  ? 127.222 93.532  113.732 1.00 11.43  ? 123  ILE E CD1   1 
ATOM   25615 N  N     . LYS E 5  124  ? 130.155 91.546  117.678 1.00 7.35   ? 124  LYS E N     1 
ATOM   25616 C  CA    . LYS E 5  124  ? 130.456 91.130  119.038 1.00 1.67   ? 124  LYS E CA    1 
ATOM   25617 C  C     . LYS E 5  124  ? 131.853 90.532  119.109 1.00 10.01  ? 124  LYS E C     1 
ATOM   25618 O  O     . LYS E 5  124  ? 132.370 89.999  118.130 1.00 18.59  ? 124  LYS E O     1 
ATOM   25619 C  CB    . LYS E 5  124  ? 129.428 90.114  119.546 1.00 4.74   ? 124  LYS E CB    1 
ATOM   25620 C  CG    . LYS E 5  124  ? 129.415 89.978  121.041 1.00 12.00  ? 124  LYS E CG    1 
ATOM   25621 C  CD    . LYS E 5  124  ? 128.537 88.858  121.490 1.00 13.23  ? 124  LYS E CD    1 
ATOM   25622 C  CE    . LYS E 5  124  ? 128.609 88.691  122.994 1.00 16.33  ? 124  LYS E CE    1 
ATOM   25623 N  NZ    . LYS E 5  124  ? 128.299 89.947  123.722 1.00 16.86  ? 124  LYS E NZ    1 
ATOM   25624 N  N     . VAL E 5  125  ? 132.455 90.616  120.292 1.00 16.02  ? 125  VAL E N     1 
ATOM   25625 C  CA    . VAL E 5  125  ? 133.706 89.933  120.607 1.00 11.85  ? 125  VAL E CA    1 
ATOM   25626 C  C     . VAL E 5  125  ? 133.409 88.935  121.719 1.00 17.29  ? 125  VAL E C     1 
ATOM   25627 O  O     . VAL E 5  125  ? 133.316 89.302  122.894 1.00 22.66  ? 125  VAL E O     1 
ATOM   25628 C  CB    . VAL E 5  125  ? 134.818 90.898  121.017 1.00 9.73   ? 125  VAL E CB    1 
ATOM   25629 C  CG1   . VAL E 5  125  ? 136.075 90.126  121.321 1.00 13.38  ? 125  VAL E CG1   1 
ATOM   25630 C  CG2   . VAL E 5  125  ? 135.081 91.885  119.922 1.00 14.66  ? 125  VAL E CG2   1 
ATOM   25631 N  N     . THR E 5  126  ? 133.273 87.673  121.349 1.00 19.05  ? 126  THR E N     1 
ATOM   25632 C  CA    . THR E 5  126  ? 133.010 86.603  122.297 1.00 17.56  ? 126  THR E CA    1 
ATOM   25633 C  C     . THR E 5  126  ? 134.216 86.414  123.218 1.00 24.70  ? 126  THR E C     1 
ATOM   25634 O  O     . THR E 5  126  ? 135.356 86.561  122.769 1.00 32.21  ? 126  THR E O     1 
ATOM   25635 C  CB    . THR E 5  126  ? 132.726 85.332  121.495 1.00 22.81  ? 126  THR E CB    1 
ATOM   25636 O  OG1   . THR E 5  126  ? 131.815 85.656  120.446 1.00 30.18  ? 126  THR E OG1   1 
ATOM   25637 C  CG2   . THR E 5  126  ? 132.085 84.277  122.305 1.00 28.58  ? 126  THR E CG2   1 
ATOM   25638 N  N     . PRO E 5  127  ? 134.022 86.106  124.505 1.00 31.32  ? 127  PRO E N     1 
ATOM   25639 C  CA    . PRO E 5  127  ? 135.178 85.862  125.372 1.00 32.38  ? 127  PRO E CA    1 
ATOM   25640 C  C     . PRO E 5  127  ? 135.799 84.473  125.276 1.00 29.57  ? 127  PRO E C     1 
ATOM   25641 O  O     . PRO E 5  127  ? 136.729 84.191  126.036 1.00 28.39  ? 127  PRO E O     1 
ATOM   25642 C  CB    . PRO E 5  127  ? 134.598 86.144  126.761 1.00 27.99  ? 127  PRO E CB    1 
ATOM   25643 C  CG    . PRO E 5  127  ? 133.182 85.717  126.671 1.00 29.62  ? 127  PRO E CG    1 
ATOM   25644 C  CD    . PRO E 5  127  ? 132.806 85.639  125.194 1.00 26.23  ? 127  PRO E CD    1 
ATOM   25645 N  N     . GLU E 5  128  ? 135.340 83.608  124.369 1.00 29.18  ? 128  GLU E N     1 
ATOM   25646 C  CA    . GLU E 5  128  ? 136.172 82.498  123.922 1.00 28.45  ? 128  GLU E CA    1 
ATOM   25647 C  C     . GLU E 5  128  ? 137.104 82.892  122.790 1.00 30.90  ? 128  GLU E C     1 
ATOM   25648 O  O     . GLU E 5  128  ? 137.768 82.019  122.227 1.00 32.16  ? 128  GLU E O     1 
ATOM   25649 C  CB    . GLU E 5  128  ? 135.352 81.277  123.469 1.00 28.35  ? 128  GLU E CB    1 
ATOM   25650 C  CG    . GLU E 5  128  ? 134.232 80.822  124.379 1.00 31.76  ? 128  GLU E CG    1 
ATOM   25651 C  CD    . GLU E 5  128  ? 133.029 81.721  124.353 1.00 37.04  ? 128  GLU E CD    1 
ATOM   25652 O  OE1   . GLU E 5  128  ? 132.139 81.498  123.509 1.00 36.25  ? 128  GLU E OE1   1 
ATOM   25653 O  OE2   . GLU E 5  128  ? 132.983 82.653  125.176 1.00 35.08  ? 128  GLU E OE2   1 
ATOM   25654 N  N     . GLY E 5  129  ? 137.140 84.164  122.416 1.00 32.32  ? 129  GLY E N     1 
ATOM   25655 C  CA    . GLY E 5  129  ? 138.122 84.636  121.466 1.00 29.59  ? 129  GLY E CA    1 
ATOM   25656 C  C     . GLY E 5  129  ? 137.641 84.691  120.035 1.00 25.89  ? 129  GLY E C     1 
ATOM   25657 O  O     . GLY E 5  129  ? 138.380 84.332  119.119 1.00 29.76  ? 129  GLY E O     1 
ATOM   25658 N  N     . GLN E 5  130  ? 136.412 85.128  119.819 1.00 18.86  ? 130  GLN E N     1 
ATOM   25659 C  CA    . GLN E 5  130  ? 135.882 85.265  118.475 1.00 17.28  ? 130  GLN E CA    1 
ATOM   25660 C  C     . GLN E 5  130  ? 135.557 86.722  118.189 1.00 19.38  ? 130  GLN E C     1 
ATOM   25661 O  O     . GLN E 5  130  ? 135.323 87.522  119.095 1.00 22.50  ? 130  GLN E O     1 
ATOM   25662 C  CB    . GLN E 5  130  ? 134.633 84.410  118.277 1.00 17.98  ? 130  GLN E CB    1 
ATOM   25663 C  CG    . GLN E 5  130  ? 134.935 82.979  117.920 1.00 21.29  ? 130  GLN E CG    1 
ATOM   25664 C  CD    . GLN E 5  130  ? 133.874 82.026  118.403 1.00 23.86  ? 130  GLN E CD    1 
ATOM   25665 O  OE1   . GLN E 5  130  ? 132.859 81.829  117.740 1.00 19.21  ? 130  GLN E OE1   1 
ATOM   25666 N  NE2   . GLN E 5  130  ? 134.089 81.440  119.571 1.00 28.11  ? 130  GLN E NE2   1 
ATOM   25667 N  N     . LYS E 5  131  ? 135.566 87.062  116.905 1.00 9.38   ? 131  LYS E N     1 
ATOM   25668 C  CA    . LYS E 5  131  ? 135.186 88.390  116.441 1.00 5.97   ? 131  LYS E CA    1 
ATOM   25669 C  C     . LYS E 5  131  ? 134.137 88.197  115.358 1.00 6.19   ? 131  LYS E C     1 
ATOM   25670 O  O     . LYS E 5  131  ? 134.475 87.908  114.210 1.00 13.20  ? 131  LYS E O     1 
ATOM   25671 C  CB    . LYS E 5  131  ? 136.389 89.164  115.928 1.00 9.86   ? 131  LYS E CB    1 
ATOM   25672 C  CG    . LYS E 5  131  ? 136.288 90.644  116.192 1.00 7.90   ? 131  LYS E CG    1 
ATOM   25673 C  CD    . LYS E 5  131  ? 137.543 91.369  115.816 1.00 10.70  ? 131  LYS E CD    1 
ATOM   25674 C  CE    . LYS E 5  131  ? 137.254 92.751  115.316 1.00 10.63  ? 131  LYS E CE    1 
ATOM   25675 N  NZ    . LYS E 5  131  ? 138.351 93.250  114.469 1.00 16.27  ? 131  LYS E NZ    1 
ATOM   25676 N  N     . ILE E 5  132  ? 132.870 88.344  115.728 1.00 3.50   ? 132  ILE E N     1 
ATOM   25677 C  CA    . ILE E 5  132  ? 131.766 88.133  114.801 1.00 5.49   ? 132  ILE E CA    1 
ATOM   25678 C  C     . ILE E 5  132  ? 131.528 89.428  114.038 1.00 1.60   ? 132  ILE E C     1 
ATOM   25679 O  O     . ILE E 5  132  ? 131.272 90.472  114.640 1.00 10.93  ? 132  ILE E O     1 
ATOM   25680 C  CB    . ILE E 5  132  ? 130.504 87.676  115.545 1.00 6.36   ? 132  ILE E CB    1 
ATOM   25681 C  CG1   . ILE E 5  132  ? 130.681 86.256  116.070 1.00 6.79   ? 132  ILE E CG1   1 
ATOM   25682 C  CG2   . ILE E 5  132  ? 129.325 87.671  114.634 1.00 9.23   ? 132  ILE E CG2   1 
ATOM   25683 C  CD1   . ILE E 5  132  ? 130.809 86.176  117.541 1.00 6.02   ? 132  ILE E CD1   1 
ATOM   25684 N  N     . VAL E 5  133  ? 131.633 89.371  112.711 1.00 1.90   ? 133  VAL E N     1 
ATOM   25685 C  CA    . VAL E 5  133  ? 131.571 90.565  111.880 1.00 1.12   ? 133  VAL E CA    1 
ATOM   25686 C  C     . VAL E 5  133  ? 130.639 90.335  110.703 1.00 1.92   ? 133  VAL E C     1 
ATOM   25687 O  O     . VAL E 5  133  ? 130.361 89.205  110.306 1.00 5.89   ? 133  VAL E O     1 
ATOM   25688 C  CB    . VAL E 5  133  ? 132.962 91.008  111.363 1.00 1.31   ? 133  VAL E CB    1 
ATOM   25689 C  CG1   . VAL E 5  133  ? 133.904 91.289  112.511 1.00 1.28   ? 133  VAL E CG1   1 
ATOM   25690 C  CG2   . VAL E 5  133  ? 133.541 89.977  110.431 1.00 2.35   ? 133  VAL E CG2   1 
ATOM   25691 N  N     . GLU E 5  134  ? 130.158 91.442  110.149 1.00 0.73   ? 134  GLU E N     1 
ATOM   25692 C  CA    . GLU E 5  134  ? 129.396 91.467  108.909 1.00 12.78  ? 134  GLU E CA    1 
ATOM   25693 C  C     . GLU E 5  134  ? 130.201 92.229  107.870 1.00 6.78   ? 134  GLU E C     1 
ATOM   25694 O  O     . GLU E 5  134  ? 130.644 93.348  108.132 1.00 9.64   ? 134  GLU E O     1 
ATOM   25695 C  CB    . GLU E 5  134  ? 128.048 92.147  109.105 1.00 6.43   ? 134  GLU E CB    1 
ATOM   25696 C  CG    . GLU E 5  134  ? 126.957 91.256  109.611 1.00 7.77   ? 134  GLU E CG    1 
ATOM   25697 C  CD    . GLU E 5  134  ? 125.713 92.033  109.956 1.00 12.15  ? 134  GLU E CD    1 
ATOM   25698 O  OE1   . GLU E 5  134  ? 125.660 93.223  109.612 1.00 9.38   ? 134  GLU E OE1   1 
ATOM   25699 O  OE2   . GLU E 5  134  ? 124.790 91.467  110.568 1.00 12.03  ? 134  GLU E OE2   1 
ATOM   25700 N  N     . ILE E 5  135  ? 130.397 91.629  106.701 1.00 7.46   ? 135  ILE E N     1 
ATOM   25701 C  CA    . ILE E 5  135  ? 131.117 92.264  105.603 1.00 2.52   ? 135  ILE E CA    1 
ATOM   25702 C  C     . ILE E 5  135  ? 130.091 92.778  104.609 1.00 6.28   ? 135  ILE E C     1 
ATOM   25703 O  O     . ILE E 5  135  ? 129.226 92.024  104.156 1.00 12.83  ? 135  ILE E O     1 
ATOM   25704 C  CB    . ILE E 5  135  ? 132.087 91.293  104.913 1.00 2.97   ? 135  ILE E CB    1 
ATOM   25705 C  CG1   . ILE E 5  135  ? 133.027 90.623  105.909 1.00 5.86   ? 135  ILE E CG1   1 
ATOM   25706 C  CG2   . ILE E 5  135  ? 132.896 92.028  103.866 1.00 3.53   ? 135  ILE E CG2   1 
ATOM   25707 C  CD1   . ILE E 5  135  ? 134.097 91.484  106.400 1.00 3.27   ? 135  ILE E CD1   1 
ATOM   25708 N  N     . TRP E 5  136  ? 130.193 94.047  104.248 1.00 2.36   ? 136  TRP E N     1 
ATOM   25709 C  CA    . TRP E 5  136  ? 129.261 94.676  103.329 1.00 2.23   ? 136  TRP E CA    1 
ATOM   25710 C  C     . TRP E 5  136  ? 130.026 95.220  102.136 1.00 6.68   ? 136  TRP E C     1 
ATOM   25711 O  O     . TRP E 5  136  ? 131.112 95.779  102.294 1.00 7.90   ? 136  TRP E O     1 
ATOM   25712 C  CB    . TRP E 5  136  ? 128.471 95.784  104.032 1.00 6.43   ? 136  TRP E CB    1 
ATOM   25713 C  CG    . TRP E 5  136  ? 127.342 95.255  104.849 1.00 6.56   ? 136  TRP E CG    1 
ATOM   25714 C  CD1   . TRP E 5  136  ? 127.362 94.973  106.171 1.00 3.59   ? 136  TRP E CD1   1 
ATOM   25715 C  CD2   . TRP E 5  136  ? 126.024 94.946  104.392 1.00 3.60   ? 136  TRP E CD2   1 
ATOM   25716 N  NE1   . TRP E 5  136  ? 126.146 94.501  106.571 1.00 7.27   ? 136  TRP E NE1   1 
ATOM   25717 C  CE2   . TRP E 5  136  ? 125.303 94.480  105.495 1.00 3.34   ? 136  TRP E CE2   1 
ATOM   25718 C  CE3   . TRP E 5  136  ? 125.387 95.019  103.155 1.00 1.21   ? 136  TRP E CE3   1 
ATOM   25719 C  CZ2   . TRP E 5  136  ? 123.981 94.086  105.403 1.00 0.03   ? 136  TRP E CZ2   1 
ATOM   25720 C  CZ3   . TRP E 5  136  ? 124.075 94.633  103.069 1.00 2.73   ? 136  TRP E CZ3   1 
ATOM   25721 C  CH2   . TRP E 5  136  ? 123.388 94.169  104.181 1.00 1.27   ? 136  TRP E CH2   1 
ATOM   25722 N  N     . ASN E 5  137  ? 129.459 95.050  100.949 1.00 5.42   ? 137  ASN E N     1 
ATOM   25723 C  CA    . ASN E 5  137  ? 130.094 95.483  99.717  1.00 3.44   ? 137  ASN E CA    1 
ATOM   25724 C  C     . ASN E 5  137  ? 129.515 96.821  99.292  1.00 6.29   ? 137  ASN E C     1 
ATOM   25725 O  O     . ASN E 5  137  ? 128.360 96.866  98.858  1.00 7.95   ? 137  ASN E O     1 
ATOM   25726 C  CB    . ASN E 5  137  ? 129.870 94.438  98.631  1.00 4.83   ? 137  ASN E CB    1 
ATOM   25727 C  CG    . ASN E 5  137  ? 130.569 94.771  97.347  1.00 5.91   ? 137  ASN E CG    1 
ATOM   25728 O  OD1   . ASN E 5  137  ? 131.380 95.680  97.287  1.00 16.93  ? 137  ASN E OD1   1 
ATOM   25729 N  ND2   . ASN E 5  137  ? 130.249 94.038  96.304  1.00 6.69   ? 137  ASN E ND2   1 
ATOM   25730 N  N     . PRO E 5  138  ? 130.264 97.923  99.374  1.00 7.50   ? 138  PRO E N     1 
ATOM   25731 C  CA    . PRO E 5  138  ? 129.686 99.229  99.030  1.00 2.49   ? 138  PRO E CA    1 
ATOM   25732 C  C     . PRO E 5  138  ? 129.281 99.351  97.583  1.00 5.67   ? 138  PRO E C     1 
ATOM   25733 O  O     . PRO E 5  138  ? 128.515 100.256 97.244  1.00 8.46   ? 138  PRO E O     1 
ATOM   25734 C  CB    . PRO E 5  138  ? 130.805 100.213 99.387  1.00 1.18   ? 138  PRO E CB    1 
ATOM   25735 C  CG    . PRO E 5  138  ? 132.017 99.419  99.399  1.00 3.23   ? 138  PRO E CG    1 
ATOM   25736 C  CD    . PRO E 5  138  ? 131.649 98.053  99.838  1.00 4.60   ? 138  PRO E CD    1 
ATOM   25737 N  N     . ARG E 5  139  ? 129.787 98.481  96.715  1.00 11.39  ? 139  ARG E N     1 
ATOM   25738 C  CA    . ARG E 5  139  ? 129.398 98.500  95.316  1.00 11.06  ? 139  ARG E CA    1 
ATOM   25739 C  C     . ARG E 5  139  ? 127.996 97.957  95.110  1.00 9.03   ? 139  ARG E C     1 
ATOM   25740 O  O     . ARG E 5  139  ? 127.446 98.099  94.017  1.00 16.12  ? 139  ARG E O     1 
ATOM   25741 C  CB    . ARG E 5  139  ? 130.407 97.703  94.498  1.00 11.93  ? 139  ARG E CB    1 
ATOM   25742 C  CG    . ARG E 5  139  ? 131.761 98.370  94.390  1.00 11.22  ? 139  ARG E CG    1 
ATOM   25743 C  CD    . ARG E 5  139  ? 132.680 97.632  93.446  1.00 10.25  ? 139  ARG E CD    1 
ATOM   25744 N  NE    . ARG E 5  139  ? 132.920 96.258  93.858  1.00 11.26  ? 139  ARG E NE    1 
ATOM   25745 C  CZ    . ARG E 5  139  ? 133.677 95.906  94.885  1.00 11.33  ? 139  ARG E CZ    1 
ATOM   25746 N  NH1   . ARG E 5  139  ? 134.319 96.802  95.608  1.00 13.95  ? 139  ARG E NH1   1 
ATOM   25747 N  NH2   . ARG E 5  139  ? 133.798 94.621  95.190  1.00 7.53   ? 139  ARG E NH2   1 
ATOM   25748 N  N     . GLU E 5  140  ? 127.404 97.345  96.136  1.00 6.71   ? 140  GLU E N     1 
ATOM   25749 C  CA    . GLU E 5  140  ? 126.073 96.758  96.051  1.00 11.93  ? 140  GLU E CA    1 
ATOM   25750 C  C     . GLU E 5  140  ? 125.105 97.347  97.065  1.00 8.08   ? 140  GLU E C     1 
ATOM   25751 O  O     . GLU E 5  140  ? 124.065 96.748  97.336  1.00 10.35  ? 140  GLU E O     1 
ATOM   25752 C  CB    . GLU E 5  140  ? 126.147 95.247  96.242  1.00 9.77   ? 140  GLU E CB    1 
ATOM   25753 C  CG    . GLU E 5  140  ? 126.845 94.532  95.136  1.00 10.21  ? 140  GLU E CG    1 
ATOM   25754 C  CD    . GLU E 5  140  ? 127.311 93.174  95.558  1.00 17.12  ? 140  GLU E CD    1 
ATOM   25755 O  OE1   . GLU E 5  140  ? 126.790 92.658  96.562  1.00 21.95  ? 140  GLU E OE1   1 
ATOM   25756 O  OE2   . GLU E 5  140  ? 128.197 92.614  94.887  1.00 18.20  ? 140  GLU E OE2   1 
ATOM   25757 N  N     . MET E 5  141  ? 125.420 98.505  97.627  1.00 13.49  ? 141  MET E N     1 
ATOM   25758 C  CA    . MET E 5  141  ? 124.670 99.085  98.723  1.00 15.62  ? 141  MET E CA    1 
ATOM   25759 C  C     . MET E 5  141  ? 123.988 100.358 98.257  1.00 4.41   ? 141  MET E C     1 
ATOM   25760 O  O     . MET E 5  141  ? 124.306 100.909 97.205  1.00 15.52  ? 141  MET E O     1 
ATOM   25761 C  CB    . MET E 5  141  ? 125.588 99.383  99.910  1.00 9.54   ? 141  MET E CB    1 
ATOM   25762 C  CG    . MET E 5  141  ? 126.106 98.155  100.605 1.00 5.82   ? 141  MET E CG    1 
ATOM   25763 S  SD    . MET E 5  141  ? 127.248 98.509  101.934 1.00 15.31  ? 141  MET E SD    1 
ATOM   25764 C  CE    . MET E 5  141  ? 126.125 99.002  103.220 1.00 2.92   ? 141  MET E CE    1 
ATOM   25765 N  N     . GLY E 5  142  ? 123.029 100.817 99.053  1.00 4.90   ? 142  GLY E N     1 
ATOM   25766 C  CA    . GLY E 5  142  ? 122.478 102.139 98.842  1.00 12.23  ? 142  GLY E CA    1 
ATOM   25767 C  C     . GLY E 5  142  ? 123.428 103.204 99.355  1.00 3.25   ? 142  GLY E C     1 
ATOM   25768 O  O     . GLY E 5  142  ? 124.076 103.045 100.387 1.00 9.01   ? 142  GLY E O     1 
ATOM   25769 N  N     . ILE E 5  143  ? 123.508 104.302 98.622  1.00 0.84   ? 143  ILE E N     1 
ATOM   25770 C  CA    . ILE E 5  143  ? 124.441 105.384 98.915  1.00 7.54   ? 143  ILE E CA    1 
ATOM   25771 C  C     . ILE E 5  143  ? 123.649 106.588 99.406  1.00 11.28  ? 143  ILE E C     1 
ATOM   25772 O  O     . ILE E 5  143  ? 122.662 106.965 98.764  1.00 9.24   ? 143  ILE E O     1 
ATOM   25773 C  CB    . ILE E 5  143  ? 125.290 105.753 97.687  1.00 7.19   ? 143  ILE E CB    1 
ATOM   25774 C  CG1   . ILE E 5  143  ? 126.067 104.535 97.201  1.00 7.81   ? 143  ILE E CG1   1 
ATOM   25775 C  CG2   . ILE E 5  143  ? 126.252 106.874 98.018  1.00 7.81   ? 143  ILE E CG2   1 
ATOM   25776 C  CD1   . ILE E 5  143  ? 126.591 104.691 95.829  1.00 9.87   ? 143  ILE E CD1   1 
ATOM   25777 N  N     . PRO E 5  144  ? 124.036 107.204 100.517 1.00 11.16  ? 144  PRO E N     1 
ATOM   25778 C  CA    . PRO E 5  144  ? 123.306 108.369 101.016 1.00 8.71   ? 144  PRO E CA    1 
ATOM   25779 C  C     . PRO E 5  144  ? 123.507 109.597 100.140 1.00 11.73  ? 144  PRO E C     1 
ATOM   25780 O  O     . PRO E 5  144  ? 124.323 109.631 99.222  1.00 14.20  ? 144  PRO E O     1 
ATOM   25781 C  CB    . PRO E 5  144  ? 123.899 108.573 102.408 1.00 6.19   ? 144  PRO E CB    1 
ATOM   25782 C  CG    . PRO E 5  144  ? 125.221 107.973 102.333 1.00 6.63   ? 144  PRO E CG    1 
ATOM   25783 C  CD    . PRO E 5  144  ? 125.112 106.806 101.433 1.00 1.40   ? 144  PRO E CD    1 
ATOM   25784 N  N     . LEU E 5  145  ? 122.727 110.626 100.449 1.00 23.05  ? 145  LEU E N     1 
ATOM   25785 C  CA    . LEU E 5  145  ? 122.795 111.913 99.761  1.00 26.40  ? 145  LEU E CA    1 
ATOM   25786 C  C     . LEU E 5  145  ? 123.985 112.693 100.300 1.00 29.29  ? 145  LEU E C     1 
ATOM   25787 O  O     . LEU E 5  145  ? 123.989 113.125 101.453 1.00 29.72  ? 145  LEU E O     1 
ATOM   25788 C  CB    . LEU E 5  145  ? 121.505 112.696 99.969  1.00 26.78  ? 145  LEU E CB    1 
ATOM   25789 C  CG    . LEU E 5  145  ? 120.221 112.157 99.351  1.00 28.99  ? 145  LEU E CG    1 
ATOM   25790 C  CD1   . LEU E 5  145  ? 119.027 112.883 99.941  1.00 25.68  ? 145  LEU E CD1   1 
ATOM   25791 C  CD2   . LEU E 5  145  ? 120.250 112.295 97.849  1.00 26.48  ? 145  LEU E CD2   1 
ATOM   25792 N  N     . LEU E 5  146  ? 125.002 112.870 99.469  1.00 24.58  ? 146  LEU E N     1 
ATOM   25793 C  CA    . LEU E 5  146  ? 126.192 113.640 99.814  1.00 24.76  ? 146  LEU E CA    1 
ATOM   25794 C  C     . LEU E 5  146  ? 126.251 114.781 98.808  1.00 32.98  ? 146  LEU E C     1 
ATOM   25795 O  O     . LEU E 5  146  ? 126.968 114.704 97.811  1.00 34.46  ? 146  LEU E O     1 
ATOM   25796 C  CB    . LEU E 5  146  ? 127.443 112.777 99.749  1.00 19.85  ? 146  LEU E CB    1 
ATOM   25797 C  CG    . LEU E 5  146  ? 127.500 111.476 100.542 1.00 20.99  ? 146  LEU E CG    1 
ATOM   25798 C  CD1   . LEU E 5  146  ? 128.644 110.632 100.022 1.00 23.70  ? 146  LEU E CD1   1 
ATOM   25799 C  CD2   . LEU E 5  146  ? 127.654 111.743 102.027 1.00 16.87  ? 146  LEU E CD2   1 
ATOM   25800 N  N     . ASP E 5  147  ? 125.490 115.839 99.075  1.00 33.45  ? 147  ASP E N     1 
ATOM   25801 C  CA    . ASP E 5  147  ? 125.252 116.897 98.099  1.00 29.86  ? 147  ASP E CA    1 
ATOM   25802 C  C     . ASP E 5  147  ? 126.538 117.473 97.522  1.00 33.61  ? 147  ASP E C     1 
ATOM   25803 O  O     . ASP E 5  147  ? 126.981 117.058 96.452  1.00 33.18  ? 147  ASP E O     1 
ATOM   25804 C  CB    . ASP E 5  147  ? 124.418 118.019 98.722  1.00 28.06  ? 147  ASP E CB    1 
ATOM   25805 C  CG    . ASP E 5  147  ? 123.043 117.551 99.137  1.00 34.72  ? 147  ASP E CG    1 
ATOM   25806 O  OD1   . ASP E 5  147  ? 122.641 116.460 98.683  1.00 38.22  ? 147  ASP E OD1   1 
ATOM   25807 O  OD2   . ASP E 5  147  ? 122.351 118.279 99.884  1.00 32.01  ? 147  ASP E OD2   1 
ATOM   25808 N  N     . MET F 6  1    ? 170.680 72.418  116.524 1.00 49.60  ? 1    MET F N     1 
ATOM   25809 C  CA    . MET F 6  1    ? 169.724 71.564  115.832 1.00 50.73  ? 1    MET F CA    1 
ATOM   25810 C  C     . MET F 6  1    ? 168.794 72.441  114.993 1.00 51.43  ? 1    MET F C     1 
ATOM   25811 O  O     . MET F 6  1    ? 168.678 73.638  115.239 1.00 53.70  ? 1    MET F O     1 
ATOM   25812 C  CB    . MET F 6  1    ? 168.949 70.708  116.847 1.00 49.90  ? 1    MET F CB    1 
ATOM   25813 C  CG    . MET F 6  1    ? 167.805 69.875  116.285 1.00 52.11  ? 1    MET F CG    1 
ATOM   25814 S  SD    . MET F 6  1    ? 167.782 68.187  116.916 1.00 60.70  ? 1    MET F SD    1 
ATOM   25815 C  CE    . MET F 6  1    ? 166.131 67.658  116.457 1.00 48.58  ? 1    MET F CE    1 
ATOM   25816 N  N     . ILE F 6  2    ? 168.146 71.843  113.997 1.00 43.81  ? 2    ILE F N     1 
ATOM   25817 C  CA    . ILE F 6  2    ? 167.278 72.551  113.065 1.00 42.83  ? 2    ILE F CA    1 
ATOM   25818 C  C     . ILE F 6  2    ? 165.867 71.996  113.203 1.00 45.41  ? 2    ILE F C     1 
ATOM   25819 O  O     . ILE F 6  2    ? 165.668 70.776  113.180 1.00 45.98  ? 2    ILE F O     1 
ATOM   25820 C  CB    . ILE F 6  2    ? 167.794 72.407  111.619 1.00 40.45  ? 2    ILE F CB    1 
ATOM   25821 C  CG1   . ILE F 6  2    ? 168.834 73.481  111.303 1.00 41.76  ? 2    ILE F CG1   1 
ATOM   25822 C  CG2   . ILE F 6  2    ? 166.648 72.434  110.617 1.00 40.80  ? 2    ILE F CG2   1 
ATOM   25823 C  CD1   . ILE F 6  2    ? 169.218 73.538  109.838 1.00 41.46  ? 2    ILE F CD1   1 
ATOM   25824 N  N     . ASP F 6  3    ? 164.880 72.873  113.357 1.00 43.28  ? 3    ASP F N     1 
ATOM   25825 C  CA    . ASP F 6  3    ? 163.495 72.428  113.440 1.00 43.77  ? 3    ASP F CA    1 
ATOM   25826 C  C     . ASP F 6  3    ? 162.583 73.550  112.959 1.00 45.24  ? 3    ASP F C     1 
ATOM   25827 O  O     . ASP F 6  3    ? 163.037 74.548  112.389 1.00 44.12  ? 3    ASP F O     1 
ATOM   25828 C  CB    . ASP F 6  3    ? 163.140 71.991  114.863 1.00 43.00  ? 3    ASP F CB    1 
ATOM   25829 C  CG    . ASP F 6  3    ? 163.576 72.993  115.897 1.00 45.68  ? 3    ASP F CG    1 
ATOM   25830 O  OD1   . ASP F 6  3    ? 164.491 73.789  115.602 1.00 47.75  ? 3    ASP F OD1   1 
ATOM   25831 O  OD2   . ASP F 6  3    ? 163.001 72.989  117.004 1.00 44.08  ? 3    ASP F OD2   1 
ATOM   25832 N  N     . GLN F 6  4    ? 161.289 73.381  113.203 1.00 42.41  ? 4    GLN F N     1 
ATOM   25833 C  CA    . GLN F 6  4    ? 160.256 74.303  112.770 1.00 40.36  ? 4    GLN F CA    1 
ATOM   25834 C  C     . GLN F 6  4    ? 159.820 75.189  113.930 1.00 40.23  ? 4    GLN F C     1 
ATOM   25835 O  O     . GLN F 6  4    ? 160.065 74.883  115.099 1.00 39.26  ? 4    GLN F O     1 
ATOM   25836 C  CB    . GLN F 6  4    ? 159.051 73.538  112.225 1.00 38.45  ? 4    GLN F CB    1 
ATOM   25837 C  CG    . GLN F 6  4    ? 158.159 74.337  111.303 1.00 39.70  ? 4    GLN F CG    1 
ATOM   25838 C  CD    . GLN F 6  4    ? 158.226 73.855  109.875 1.00 42.46  ? 4    GLN F CD    1 
ATOM   25839 O  OE1   . GLN F 6  4    ? 157.864 72.720  109.578 1.00 41.61  ? 4    GLN F OE1   1 
ATOM   25840 N  NE2   . GLN F 6  4    ? 158.692 74.715  108.979 1.00 40.89  ? 4    GLN F NE2   1 
ATOM   25841 N  N     . LYS F 6  5    ? 159.182 76.302  113.591 1.00 37.69  ? 5    LYS F N     1 
ATOM   25842 C  CA    . LYS F 6  5    ? 158.635 77.221  114.572 1.00 35.56  ? 5    LYS F CA    1 
ATOM   25843 C  C     . LYS F 6  5    ? 157.459 77.942  113.940 1.00 37.41  ? 5    LYS F C     1 
ATOM   25844 O  O     . LYS F 6  5    ? 157.379 78.051  112.715 1.00 35.33  ? 5    LYS F O     1 
ATOM   25845 C  CB    . LYS F 6  5    ? 159.693 78.217  115.040 1.00 36.55  ? 5    LYS F CB    1 
ATOM   25846 C  CG    . LYS F 6  5    ? 159.445 78.820  116.404 1.00 34.94  ? 5    LYS F CG    1 
ATOM   25847 C  CD    . LYS F 6  5    ? 160.735 79.394  116.959 1.00 39.65  ? 5    LYS F CD    1 
ATOM   25848 C  CE    . LYS F 6  5    ? 160.558 79.948  118.359 1.00 38.95  ? 5    LYS F CE    1 
ATOM   25849 N  NZ    . LYS F 6  5    ? 159.737 81.183  118.361 1.00 36.93  ? 5    LYS F NZ    1 
ATOM   25850 N  N     . ILE F 6  6    ? 156.538 78.415  114.771 1.00 38.38  ? 6    ILE F N     1 
ATOM   25851 C  CA    . ILE F 6  6    ? 155.381 79.169  114.306 1.00 35.20  ? 6    ILE F CA    1 
ATOM   25852 C  C     . ILE F 6  6    ? 155.398 80.532  114.982 1.00 32.27  ? 6    ILE F C     1 
ATOM   25853 O  O     . ILE F 6  6    ? 155.414 80.625  116.213 1.00 32.70  ? 6    ILE F O     1 
ATOM   25854 C  CB    . ILE F 6  6    ? 154.075 78.407  114.575 1.00 31.34  ? 6    ILE F CB    1 
ATOM   25855 C  CG1   . ILE F 6  6    ? 154.035 77.149  113.706 1.00 33.10  ? 6    ILE F CG1   1 
ATOM   25856 C  CG2   . ILE F 6  6    ? 152.879 79.274  114.278 1.00 34.38  ? 6    ILE F CG2   1 
ATOM   25857 C  CD1   . ILE F 6  6    ? 152.859 76.255  113.954 1.00 33.27  ? 6    ILE F CD1   1 
ATOM   25858 N  N     . PHE F 6  7    ? 155.400 81.589  114.172 1.00 36.14  ? 7    PHE F N     1 
ATOM   25859 C  CA    . PHE F 6  7    ? 155.509 82.967  114.626 1.00 35.18  ? 7    PHE F CA    1 
ATOM   25860 C  C     . PHE F 6  7    ? 154.244 83.734  114.271 1.00 35.55  ? 7    PHE F C     1 
ATOM   25861 O  O     . PHE F 6  7    ? 153.556 83.417  113.301 1.00 33.86  ? 7    PHE F O     1 
ATOM   25862 C  CB    . PHE F 6  7    ? 156.701 83.674  113.977 1.00 34.26  ? 7    PHE F CB    1 
ATOM   25863 C  CG    . PHE F 6  7    ? 158.036 83.157  114.403 1.00 36.85  ? 7    PHE F CG    1 
ATOM   25864 C  CD1   . PHE F 6  7    ? 158.689 82.198  113.656 1.00 38.07  ? 7    PHE F CD1   1 
ATOM   25865 C  CD2   . PHE F 6  7    ? 158.664 83.666  115.519 1.00 39.03  ? 7    PHE F CD2   1 
ATOM   25866 C  CE1   . PHE F 6  7    ? 159.924 81.737  114.034 1.00 39.63  ? 7    PHE F CE1   1 
ATOM   25867 C  CE2   . PHE F 6  7    ? 159.899 83.208  115.897 1.00 36.45  ? 7    PHE F CE2   1 
ATOM   25868 C  CZ    . PHE F 6  7    ? 160.529 82.247  115.154 1.00 36.89  ? 7    PHE F CZ    1 
ATOM   25869 N  N     . GLU F 6  8    ? 153.955 84.769  115.057 1.00 27.97  ? 8    GLU F N     1 
ATOM   25870 C  CA    . GLU F 6  8    ? 152.881 85.709  114.764 1.00 22.10  ? 8    GLU F CA    1 
ATOM   25871 C  C     . GLU F 6  8    ? 153.460 87.110  114.691 1.00 21.31  ? 8    GLU F C     1 
ATOM   25872 O  O     . GLU F 6  8    ? 154.267 87.490  115.542 1.00 28.33  ? 8    GLU F O     1 
ATOM   25873 C  CB    . GLU F 6  8    ? 151.781 85.662  115.823 1.00 22.52  ? 8    GLU F CB    1 
ATOM   25874 C  CG    . GLU F 6  8    ? 150.974 84.391  115.843 1.00 23.23  ? 8    GLU F CG    1 
ATOM   25875 C  CD    . GLU F 6  8    ? 149.870 84.426  116.878 1.00 28.18  ? 8    GLU F CD    1 
ATOM   25876 O  OE1   . GLU F 6  8    ? 149.764 85.439  117.601 1.00 29.97  ? 8    GLU F OE1   1 
ATOM   25877 O  OE2   . GLU F 6  8    ? 149.115 83.437  116.978 1.00 25.01  ? 8    GLU F OE2   1 
ATOM   25878 N  N     . THR F 6  9    ? 153.040 87.882  113.693 1.00 17.91  ? 9    THR F N     1 
ATOM   25879 C  CA    . THR F 6  9    ? 153.538 89.240  113.530 1.00 17.06  ? 9    THR F CA    1 
ATOM   25880 C  C     . THR F 6  9    ? 152.501 90.093  112.812 1.00 16.87  ? 9    THR F C     1 
ATOM   25881 O  O     . THR F 6  9    ? 151.543 89.587  112.230 1.00 22.79  ? 9    THR F O     1 
ATOM   25882 C  CB    . THR F 6  9    ? 154.866 89.260  112.764 1.00 18.96  ? 9    THR F CB    1 
ATOM   25883 O  OG1   . THR F 6  9    ? 155.501 90.528  112.942 1.00 23.29  ? 9    THR F OG1   1 
ATOM   25884 C  CG2   . THR F 6  9    ? 154.640 89.036  111.283 1.00 18.50  ? 9    THR F CG2   1 
ATOM   25885 N  N     . THR F 6  10   ? 152.701 91.407  112.872 1.00 10.26  ? 10   THR F N     1 
ATOM   25886 C  CA    . THR F 6  10   ? 151.893 92.372  112.136 1.00 9.30   ? 10   THR F CA    1 
ATOM   25887 C  C     . THR F 6  10   ? 152.784 93.087  111.133 1.00 17.49  ? 10   THR F C     1 
ATOM   25888 O  O     . THR F 6  10   ? 153.862 93.566  111.492 1.00 23.35  ? 10   THR F O     1 
ATOM   25889 C  CB    . THR F 6  10   ? 151.233 93.388  113.071 1.00 12.53  ? 10   THR F CB    1 
ATOM   25890 O  OG1   . THR F 6  10   ? 150.338 92.719  113.958 1.00 14.63  ? 10   THR F OG1   1 
ATOM   25891 C  CG2   . THR F 6  10   ? 150.445 94.398  112.282 1.00 9.73   ? 10   THR F CG2   1 
ATOM   25892 N  N     . LEU F 6  11   ? 152.338 93.160  109.886 1.00 14.92  ? 11   LEU F N     1 
ATOM   25893 C  CA    . LEU F 6  11   ? 153.077 93.828  108.828 1.00 12.54  ? 11   LEU F CA    1 
ATOM   25894 C  C     . LEU F 6  11   ? 152.385 95.119  108.418 1.00 12.90  ? 11   LEU F C     1 
ATOM   25895 O  O     . LEU F 6  11   ? 151.187 95.126  108.143 1.00 16.74  ? 11   LEU F O     1 
ATOM   25896 C  CB    . LEU F 6  11   ? 153.213 92.929  107.601 1.00 11.13  ? 11   LEU F CB    1 
ATOM   25897 C  CG    . LEU F 6  11   ? 153.865 91.558  107.723 1.00 15.53  ? 11   LEU F CG    1 
ATOM   25898 C  CD1   . LEU F 6  11   ? 154.059 90.998  106.343 1.00 15.94  ? 11   LEU F CD1   1 
ATOM   25899 C  CD2   . LEU F 6  11   ? 155.191 91.626  108.451 1.00 18.57  ? 11   LEU F CD2   1 
ATOM   25900 N  N     . ASN F 6  12   ? 153.150 96.201  108.353 1.00 9.15   ? 12   ASN F N     1 
ATOM   25901 C  CA    . ASN F 6  12   ? 152.673 97.457  107.795 1.00 6.82   ? 12   ASN F CA    1 
ATOM   25902 C  C     . ASN F 6  12   ? 152.788 97.413  106.280 1.00 10.32  ? 12   ASN F C     1 
ATOM   25903 O  O     . ASN F 6  12   ? 153.840 97.063  105.744 1.00 24.84  ? 12   ASN F O     1 
ATOM   25904 C  CB    . ASN F 6  12   ? 153.470 98.640  108.334 1.00 8.09   ? 12   ASN F CB    1 
ATOM   25905 C  CG    . ASN F 6  12   ? 153.459 98.711  109.831 1.00 13.73  ? 12   ASN F CG    1 
ATOM   25906 O  OD1   . ASN F 6  12   ? 152.490 98.334  110.468 1.00 18.74  ? 12   ASN F OD1   1 
ATOM   25907 N  ND2   . ASN F 6  12   ? 154.533 99.211  110.404 1.00 14.75  ? 12   ASN F ND2   1 
ATOM   25908 N  N     . ILE F 6  13   ? 151.711 97.775  105.596 1.00 8.55   ? 13   ILE F N     1 
ATOM   25909 C  CA    . ILE F 6  13   ? 151.663 97.820  104.140 1.00 13.35  ? 13   ILE F CA    1 
ATOM   25910 C  C     . ILE F 6  13   ? 151.601 99.279  103.722 1.00 11.27  ? 13   ILE F C     1 
ATOM   25911 O  O     . ILE F 6  13   ? 150.657 99.991  104.075 1.00 22.63  ? 13   ILE F O     1 
ATOM   25912 C  CB    . ILE F 6  13   ? 150.463 97.039  103.588 1.00 14.53  ? 13   ILE F CB    1 
ATOM   25913 C  CG1   . ILE F 6  13   ? 150.658 95.543  103.786 1.00 14.20  ? 13   ILE F CG1   1 
ATOM   25914 C  CG2   . ILE F 6  13   ? 150.261 97.334  102.139 1.00 14.66  ? 13   ILE F CG2   1 
ATOM   25915 C  CD1   . ILE F 6  13   ? 149.847 94.965  104.855 1.00 11.63  ? 13   ILE F CD1   1 
ATOM   25916 N  N     . ASP F 6  14   ? 152.602 99.727  102.969 1.00 14.66  ? 14   ASP F N     1 
ATOM   25917 C  CA    . ASP F 6  14   ? 152.667 101.124 102.564 1.00 18.69  ? 14   ASP F CA    1 
ATOM   25918 C  C     . ASP F 6  14   ? 151.958 101.402 101.249 1.00 27.46  ? 14   ASP F C     1 
ATOM   25919 O  O     . ASP F 6  14   ? 151.886 102.565 100.840 1.00 31.80  ? 14   ASP F O     1 
ATOM   25920 C  CB    . ASP F 6  14   ? 154.119 101.576 102.465 1.00 21.16  ? 14   ASP F CB    1 
ATOM   25921 C  CG    . ASP F 6  14   ? 154.653 102.091 103.781 1.00 29.49  ? 14   ASP F CG    1 
ATOM   25922 O  OD1   . ASP F 6  14   ? 155.250 103.187 103.799 1.00 30.19  ? 14   ASP F OD1   1 
ATOM   25923 O  OD2   . ASP F 6  14   ? 154.475 101.402 104.810 1.00 33.84  ? 14   ASP F OD2   1 
ATOM   25924 N  N     . ASP F 6  15   ? 151.433 100.381 100.582 1.00 24.18  ? 15   ASP F N     1 
ATOM   25925 C  CA    . ASP F 6  15   ? 150.729 100.558 99.313  1.00 22.55  ? 15   ASP F CA    1 
ATOM   25926 C  C     . ASP F 6  15   ? 149.692 99.460  99.172  1.00 26.20  ? 15   ASP F C     1 
ATOM   25927 O  O     . ASP F 6  15   ? 149.887 98.486  98.439  1.00 29.18  ? 15   ASP F O     1 
ATOM   25928 C  CB    . ASP F 6  15   ? 151.706 100.533 98.142  1.00 25.19  ? 15   ASP F CB    1 
ATOM   25929 C  CG    . ASP F 6  15   ? 151.193 101.279 96.946  1.00 30.01  ? 15   ASP F CG    1 
ATOM   25930 O  OD1   . ASP F 6  15   ? 151.640 102.416 96.724  1.00 34.62  ? 15   ASP F OD1   1 
ATOM   25931 O  OD2   . ASP F 6  15   ? 150.332 100.734 96.235  1.00 27.68  ? 15   ASP F OD2   1 
ATOM   25932 N  N     . PRO F 6  16   ? 148.564 99.581  99.872  1.00 20.19  ? 16   PRO F N     1 
ATOM   25933 C  CA    . PRO F 6  16   ? 147.603 98.467  99.909  1.00 17.41  ? 16   PRO F CA    1 
ATOM   25934 C  C     . PRO F 6  16   ? 147.024 98.083  98.557  1.00 19.59  ? 16   PRO F C     1 
ATOM   25935 O  O     . PRO F 6  16   ? 146.769 96.897  98.318  1.00 21.03  ? 16   PRO F O     1 
ATOM   25936 C  CB    . PRO F 6  16   ? 146.527 98.986  100.869 1.00 20.55  ? 16   PRO F CB    1 
ATOM   25937 C  CG    . PRO F 6  16   ? 147.204 100.018 101.674 1.00 15.00  ? 16   PRO F CG    1 
ATOM   25938 C  CD    . PRO F 6  16   ? 148.163 100.678 100.763 1.00 17.95  ? 16   PRO F CD    1 
ATOM   25939 N  N     . THR F 6  17   ? 146.806 99.046  97.662  1.00 18.92  ? 17   THR F N     1 
ATOM   25940 C  CA    . THR F 6  17   ? 146.219 98.719  96.367  1.00 21.99  ? 17   THR F CA    1 
ATOM   25941 C  C     . THR F 6  17   ? 147.147 97.827  95.554  1.00 26.21  ? 17   THR F C     1 
ATOM   25942 O  O     . THR F 6  17   ? 146.698 96.878  94.904  1.00 25.84  ? 17   THR F O     1 
ATOM   25943 C  CB    . THR F 6  17   ? 145.902 99.995  95.593  1.00 22.33  ? 17   THR F CB    1 
ATOM   25944 O  OG1   . THR F 6  17   ? 145.531 101.031 96.507  1.00 25.77  ? 17   THR F OG1   1 
ATOM   25945 C  CG2   . THR F 6  17   ? 144.746 99.757  94.657  1.00 21.51  ? 17   THR F CG2   1 
ATOM   25946 N  N     . ASN F 6  18   ? 148.446 98.127  95.571  1.00 29.22  ? 18   ASN F N     1 
ATOM   25947 C  CA    . ASN F 6  18   ? 149.424 97.287  94.890  1.00 24.38  ? 18   ASN F CA    1 
ATOM   25948 C  C     . ASN F 6  18   ? 149.629 95.969  95.618  1.00 25.26  ? 18   ASN F C     1 
ATOM   25949 O  O     . ASN F 6  18   ? 149.729 94.915  94.984  1.00 28.36  ? 18   ASN F O     1 
ATOM   25950 C  CB    . ASN F 6  18   ? 150.752 98.024  94.780  1.00 27.82  ? 18   ASN F CB    1 
ATOM   25951 C  CG    . ASN F 6  18   ? 151.741 97.312  93.899  1.00 28.06  ? 18   ASN F CG    1 
ATOM   25952 O  OD1   . ASN F 6  18   ? 151.369 96.476  93.085  1.00 33.73  ? 18   ASN F OD1   1 
ATOM   25953 N  ND2   . ASN F 6  18   ? 153.015 97.617  94.078  1.00 29.20  ? 18   ASN F ND2   1 
ATOM   25954 N  N     . PHE F 6  19   ? 149.694 96.010  96.949  1.00 22.94  ? 19   PHE F N     1 
ATOM   25955 C  CA    . PHE F 6  19   ? 149.941 94.800  97.723  1.00 17.75  ? 19   PHE F CA    1 
ATOM   25956 C  C     . PHE F 6  19   ? 148.849 93.770  97.490  1.00 24.92  ? 19   PHE F C     1 
ATOM   25957 O  O     . PHE F 6  19   ? 149.129 92.574  97.377  1.00 30.53  ? 19   PHE F O     1 
ATOM   25958 C  CB    . PHE F 6  19   ? 150.048 95.148  99.204  1.00 16.21  ? 19   PHE F CB    1 
ATOM   25959 C  CG    . PHE F 6  19   ? 150.462 94.003  100.081 1.00 20.22  ? 19   PHE F CG    1 
ATOM   25960 C  CD1   . PHE F 6  19   ? 149.524 93.123  100.587 1.00 23.15  ? 19   PHE F CD1   1 
ATOM   25961 C  CD2   . PHE F 6  19   ? 151.783 93.831  100.438 1.00 21.17  ? 19   PHE F CD2   1 
ATOM   25962 C  CE1   . PHE F 6  19   ? 149.902 92.084  101.396 1.00 22.43  ? 19   PHE F CE1   1 
ATOM   25963 C  CE2   . PHE F 6  19   ? 152.157 92.798  101.254 1.00 21.26  ? 19   PHE F CE2   1 
ATOM   25964 C  CZ    . PHE F 6  19   ? 151.215 91.924  101.728 1.00 22.43  ? 19   PHE F CZ    1 
ATOM   25965 N  N     . CYS F 6  20   ? 147.600 94.212  97.406  1.00 22.10  ? 20   CYS F N     1 
ATOM   25966 C  CA    . CYS F 6  20   ? 146.490 93.284  97.253  1.00 23.52  ? 20   CYS F CA    1 
ATOM   25967 C  C     . CYS F 6  20   ? 146.322 92.767  95.829  1.00 24.40  ? 20   CYS F C     1 
ATOM   25968 O  O     . CYS F 6  20   ? 145.322 92.105  95.549  1.00 30.33  ? 20   CYS F O     1 
ATOM   25969 C  CB    . CYS F 6  20   ? 145.194 93.939  97.735  1.00 22.66  ? 20   CYS F CB    1 
ATOM   25970 S  SG    . CYS F 6  20   ? 145.070 94.076  99.523  1.00 25.66  ? 20   CYS F SG    1 
ATOM   25971 N  N     . THR F 6  21   ? 147.250 93.068  94.921  1.00 21.06  ? 21   THR F N     1 
ATOM   25972 C  CA    . THR F 6  21   ? 147.223 92.440  93.603  1.00 26.42  ? 21   THR F CA    1 
ATOM   25973 C  C     . THR F 6  21   ? 147.701 90.993  93.652  1.00 30.39  ? 21   THR F C     1 
ATOM   25974 O  O     . THR F 6  21   ? 147.236 90.164  92.866  1.00 32.46  ? 21   THR F O     1 
ATOM   25975 C  CB    . THR F 6  21   ? 148.065 93.245  92.615  1.00 27.82  ? 21   THR F CB    1 
ATOM   25976 O  OG1   . THR F 6  21   ? 149.338 93.534  93.199  1.00 30.64  ? 21   THR F OG1   1 
ATOM   25977 C  CG2   . THR F 6  21   ? 147.375 94.535  92.240  1.00 29.26  ? 21   THR F CG2   1 
ATOM   25978 N  N     . ASN F 6  22   ? 148.632 90.675  94.549  1.00 25.95  ? 22   ASN F N     1 
ATOM   25979 C  CA    . ASN F 6  22   ? 149.096 89.304  94.773  1.00 24.97  ? 22   ASN F CA    1 
ATOM   25980 C  C     . ASN F 6  22   ? 149.509 89.218  96.241  1.00 31.06  ? 22   ASN F C     1 
ATOM   25981 O  O     . ASN F 6  22   ? 150.647 89.530  96.595  1.00 29.54  ? 22   ASN F O     1 
ATOM   25982 C  CB    . ASN F 6  22   ? 150.247 88.949  93.846  1.00 27.94  ? 22   ASN F CB    1 
ATOM   25983 C  CG    . ASN F 6  22   ? 150.606 87.481  93.891  1.00 32.09  ? 22   ASN F CG    1 
ATOM   25984 O  OD1   . ASN F 6  22   ? 150.017 86.703  94.638  1.00 31.39  ? 22   ASN F OD1   1 
ATOM   25985 N  ND2   . ASN F 6  22   ? 151.587 87.096  93.091  1.00 29.82  ? 22   ASN F ND2   1 
ATOM   25986 N  N     . VAL F 6  23   ? 148.571 88.797  97.088  1.00 30.77  ? 23   VAL F N     1 
ATOM   25987 C  CA    . VAL F 6  23   ? 148.792 88.887  98.527  1.00 23.65  ? 23   VAL F CA    1 
ATOM   25988 C  C     . VAL F 6  23   ? 149.835 87.879  98.984  1.00 23.96  ? 23   VAL F C     1 
ATOM   25989 O  O     . VAL F 6  23   ? 150.708 88.200  99.794  1.00 29.84  ? 23   VAL F O     1 
ATOM   25990 C  CB    . VAL F 6  23   ? 147.464 88.713  99.282  1.00 26.34  ? 23   VAL F CB    1 
ATOM   25991 C  CG1   . VAL F 6  23   ? 147.677 88.910  100.760 1.00 25.68  ? 23   VAL F CG1   1 
ATOM   25992 C  CG2   . VAL F 6  23   ? 146.441 89.695  98.767  1.00 27.72  ? 23   VAL F CG2   1 
ATOM   25993 N  N     . GLU F 6  24   ? 149.759 86.648  98.489  1.00 27.72  ? 24   GLU F N     1 
ATOM   25994 C  CA    . GLU F 6  24   ? 150.650 85.596  98.968  1.00 28.12  ? 24   GLU F CA    1 
ATOM   25995 C  C     . GLU F 6  24   ? 152.106 85.889  98.613  1.00 31.08  ? 24   GLU F C     1 
ATOM   25996 O  O     . GLU F 6  24   ? 153.000 85.780  99.462  1.00 29.94  ? 24   GLU F O     1 
ATOM   25997 C  CB    . GLU F 6  24   ? 150.203 84.254  98.392  1.00 28.86  ? 24   GLU F CB    1 
ATOM   25998 C  CG    . GLU F 6  24   ? 149.754 84.326  96.936  1.00 31.46  ? 24   GLU F CG    1 
ATOM   25999 C  CD    . GLU F 6  24   ? 148.300 84.752  96.771  1.00 33.41  ? 24   GLU F CD    1 
ATOM   26000 O  OE1   . GLU F 6  24   ? 147.665 85.121  97.781  1.00 32.83  ? 24   GLU F OE1   1 
ATOM   26001 O  OE2   . GLU F 6  24   ? 147.794 84.729  95.629  1.00 34.69  ? 24   GLU F OE2   1 
ATOM   26002 N  N     . ALA F 6  25   ? 152.364 86.272  97.362  1.00 29.58  ? 25   ALA F N     1 
ATOM   26003 C  CA    . ALA F 6  25   ? 153.732 86.533  96.935  1.00 29.63  ? 25   ALA F CA    1 
ATOM   26004 C  C     . ALA F 6  25   ? 154.321 87.736  97.657  1.00 34.44  ? 25   ALA F C     1 
ATOM   26005 O  O     . ALA F 6  25   ? 155.450 87.678  98.160  1.00 33.98  ? 25   ALA F O     1 
ATOM   26006 C  CB    . ALA F 6  25   ? 153.777 86.737  95.424  1.00 27.53  ? 25   ALA F CB    1 
ATOM   26007 N  N     . HIS F 6  26   ? 153.573 88.838  97.716  1.00 29.49  ? 26   HIS F N     1 
ATOM   26008 C  CA    . HIS F 6  26   ? 154.058 90.023  98.414  1.00 24.74  ? 26   HIS F CA    1 
ATOM   26009 C  C     . HIS F 6  26   ? 154.294 89.733  99.888  1.00 28.03  ? 26   HIS F C     1 
ATOM   26010 O  O     . HIS F 6  26   ? 155.283 90.193  100.472 1.00 30.13  ? 26   HIS F O     1 
ATOM   26011 C  CB    . HIS F 6  26   ? 153.064 91.169  98.251  1.00 27.68  ? 26   HIS F CB    1 
ATOM   26012 C  CG    . HIS F 6  26   ? 152.900 91.645  96.841  1.00 30.14  ? 26   HIS F CG    1 
ATOM   26013 N  ND1   . HIS F 6  26   ? 152.150 90.966  95.908  1.00 30.79  ? 26   HIS F ND1   1 
ATOM   26014 C  CD2   . HIS F 6  26   ? 153.376 92.744  96.212  1.00 31.41  ? 26   HIS F CD2   1 
ATOM   26015 C  CE1   . HIS F 6  26   ? 152.179 91.621  94.761  1.00 32.13  ? 26   HIS F CE1   1 
ATOM   26016 N  NE2   . HIS F 6  26   ? 152.916 92.703  94.920  1.00 31.35  ? 26   HIS F NE2   1 
ATOM   26017 N  N     . LEU F 6  27   ? 153.393 88.967  100.505 1.00 24.21  ? 27   LEU F N     1 
ATOM   26018 C  CA    . LEU F 6  27   ? 153.536 88.604  101.908 1.00 24.43  ? 27   LEU F CA    1 
ATOM   26019 C  C     . LEU F 6  27   ? 154.800 87.796  102.153 1.00 31.66  ? 27   LEU F C     1 
ATOM   26020 O  O     . LEU F 6  27   ? 155.555 88.086  103.089 1.00 32.67  ? 27   LEU F O     1 
ATOM   26021 C  CB    . LEU F 6  27   ? 152.308 87.821  102.356 1.00 26.78  ? 27   LEU F CB    1 
ATOM   26022 C  CG    . LEU F 6  27   ? 152.010 87.768  103.846 1.00 26.63  ? 27   LEU F CG    1 
ATOM   26023 C  CD1   . LEU F 6  27   ? 151.795 89.162  104.355 1.00 29.25  ? 27   LEU F CD1   1 
ATOM   26024 C  CD2   . LEU F 6  27   ? 150.786 86.928  104.075 1.00 25.03  ? 27   LEU F CD2   1 
ATOM   26025 N  N     . LEU F 6  28   ? 155.052 86.785  101.318 1.00 35.20  ? 28   LEU F N     1 
ATOM   26026 C  CA    . LEU F 6  28   ? 156.274 86.000  101.463 1.00 32.90  ? 28   LEU F CA    1 
ATOM   26027 C  C     . LEU F 6  28   ? 157.516 86.858  101.265 1.00 34.61  ? 28   LEU F C     1 
ATOM   26028 O  O     . LEU F 6  28   ? 158.491 86.727  102.015 1.00 34.72  ? 28   LEU F O     1 
ATOM   26029 C  CB    . LEU F 6  28   ? 156.268 84.827  100.487 1.00 33.00  ? 28   LEU F CB    1 
ATOM   26030 C  CG    . LEU F 6  28   ? 156.155 83.436  101.111 1.00 34.30  ? 28   LEU F CG    1 
ATOM   26031 C  CD1   . LEU F 6  28   ? 157.336 83.184  102.028 1.00 37.51  ? 28   LEU F CD1   1 
ATOM   26032 C  CD2   . LEU F 6  28   ? 154.859 83.266  101.871 1.00 33.96  ? 28   LEU F CD2   1 
ATOM   26033 N  N     . LYS F 6  29   ? 157.499 87.750  100.270 1.00 35.39  ? 29   LYS F N     1 
ATOM   26034 C  CA    . LYS F 6  29   ? 158.652 88.615  100.039 1.00 34.89  ? 29   LYS F CA    1 
ATOM   26035 C  C     . LYS F 6  29   ? 158.941 89.485  101.253 1.00 39.98  ? 29   LYS F C     1 
ATOM   26036 O  O     . LYS F 6  29   ? 160.094 89.617  101.676 1.00 39.83  ? 29   LYS F O     1 
ATOM   26037 C  CB    . LYS F 6  29   ? 158.425 89.498  98.814  1.00 35.41  ? 29   LYS F CB    1 
ATOM   26038 C  CG    . LYS F 6  29   ? 158.182 88.771  97.516  1.00 40.13  ? 29   LYS F CG    1 
ATOM   26039 C  CD    . LYS F 6  29   ? 157.920 89.763  96.396  1.00 39.21  ? 29   LYS F CD    1 
ATOM   26040 C  CE    . LYS F 6  29   ? 157.973 89.097  95.032  1.00 40.12  ? 29   LYS F CE    1 
ATOM   26041 N  NZ    . LYS F 6  29   ? 156.971 89.678  94.093  1.00 38.23  ? 29   LYS F NZ    1 
ATOM   26042 N  N     . GLU F 6  30   ? 157.905 90.095  101.827 1.00 39.49  ? 30   GLU F N     1 
ATOM   26043 C  CA    . GLU F 6  30   ? 158.141 91.010  102.939 1.00 38.32  ? 30   GLU F CA    1 
ATOM   26044 C  C     . GLU F 6  30   ? 158.563 90.260  104.195 1.00 37.69  ? 30   GLU F C     1 
ATOM   26045 O  O     . GLU F 6  30   ? 159.409 90.744  104.961 1.00 38.88  ? 30   GLU F O     1 
ATOM   26046 C  CB    . GLU F 6  30   ? 156.901 91.861  103.197 1.00 37.47  ? 30   GLU F CB    1 
ATOM   26047 C  CG    . GLU F 6  30   ? 157.227 93.277  103.639 1.00 39.69  ? 30   GLU F CG    1 
ATOM   26048 C  CD    . GLU F 6  30   ? 158.287 93.945  102.770 1.00 42.88  ? 30   GLU F CD    1 
ATOM   26049 O  OE1   . GLU F 6  30   ? 158.255 93.769  101.535 1.00 42.62  ? 30   GLU F OE1   1 
ATOM   26050 O  OE2   . GLU F 6  30   ? 159.162 94.645  103.320 1.00 43.21  ? 30   GLU F OE2   1 
ATOM   26051 N  N     . LEU F 6  31   ? 157.998 89.071  104.420 1.00 33.35  ? 31   LEU F N     1 
ATOM   26052 C  CA    . LEU F 6  31   ? 158.451 88.256  105.541 1.00 34.52  ? 31   LEU F CA    1 
ATOM   26053 C  C     . LEU F 6  31   ? 159.919 87.896  105.390 1.00 34.60  ? 31   LEU F C     1 
ATOM   26054 O  O     . LEU F 6  31   ? 160.690 87.979  106.353 1.00 37.32  ? 31   LEU F O     1 
ATOM   26055 C  CB    . LEU F 6  31   ? 157.603 86.991  105.653 1.00 32.02  ? 31   LEU F CB    1 
ATOM   26056 C  CG    . LEU F 6  31   ? 156.200 87.146  106.237 1.00 30.89  ? 31   LEU F CG    1 
ATOM   26057 C  CD1   . LEU F 6  31   ? 155.421 85.865  106.067 1.00 29.88  ? 31   LEU F CD1   1 
ATOM   26058 C  CD2   . LEU F 6  31   ? 156.280 87.537  107.689 1.00 30.34  ? 31   LEU F CD2   1 
ATOM   26059 N  N     . GLU F 6  32   ? 160.329 87.513  104.179 1.00 38.99  ? 32   GLU F N     1 
ATOM   26060 C  CA    . GLU F 6  32   ? 161.727 87.174  103.946 1.00 39.11  ? 32   GLU F CA    1 
ATOM   26061 C  C     . GLU F 6  32   ? 162.627 88.385  104.143 1.00 36.72  ? 32   GLU F C     1 
ATOM   26062 O  O     . GLU F 6  32   ? 163.719 88.270  104.707 1.00 39.00  ? 32   GLU F O     1 
ATOM   26063 C  CB    . GLU F 6  32   ? 161.890 86.599  102.541 1.00 35.90  ? 32   GLU F CB    1 
ATOM   26064 C  CG    . GLU F 6  32   ? 161.308 85.207  102.392 1.00 37.43  ? 32   GLU F CG    1 
ATOM   26065 C  CD    . GLU F 6  32   ? 161.029 84.841  100.956 1.00 40.95  ? 32   GLU F CD    1 
ATOM   26066 O  OE1   . GLU F 6  32   ? 161.039 85.743  100.097 1.00 43.20  ? 32   GLU F OE1   1 
ATOM   26067 O  OE2   . GLU F 6  32   ? 160.799 83.646  100.683 1.00 41.21  ? 32   GLU F OE2   1 
ATOM   26068 N  N     . ASN F 6  33   ? 162.183 89.555  103.692 1.00 33.60  ? 33   ASN F N     1 
ATOM   26069 C  CA    . ASN F 6  33   ? 162.990 90.756  103.856 1.00 33.42  ? 33   ASN F CA    1 
ATOM   26070 C  C     . ASN F 6  33   ? 163.135 91.159  105.316 1.00 36.74  ? 33   ASN F C     1 
ATOM   26071 O  O     . ASN F 6  33   ? 164.151 91.752  105.692 1.00 40.32  ? 33   ASN F O     1 
ATOM   26072 C  CB    . ASN F 6  33   ? 162.394 91.906  103.052 1.00 33.06  ? 33   ASN F CB    1 
ATOM   26073 C  CG    . ASN F 6  33   ? 162.651 91.768  101.577 1.00 39.36  ? 33   ASN F CG    1 
ATOM   26074 O  OD1   . ASN F 6  33   ? 163.734 91.358  101.166 1.00 42.08  ? 33   ASN F OD1   1 
ATOM   26075 N  ND2   . ASN F 6  33   ? 161.663 92.118  100.766 1.00 39.71  ? 33   ASN F ND2   1 
ATOM   26076 N  N     . ILE F 6  34   ? 162.144 90.870  106.152 1.00 34.04  ? 34   ILE F N     1 
ATOM   26077 C  CA    . ILE F 6  34   ? 162.236 91.318  107.539 1.00 33.78  ? 34   ILE F CA    1 
ATOM   26078 C  C     . ILE F 6  34   ? 162.936 90.295  108.425 1.00 34.62  ? 34   ILE F C     1 
ATOM   26079 O  O     . ILE F 6  34   ? 163.761 90.661  109.265 1.00 33.49  ? 34   ILE F O     1 
ATOM   26080 C  CB    . ILE F 6  34   ? 160.840 91.667  108.088 1.00 34.06  ? 34   ILE F CB    1 
ATOM   26081 C  CG1   . ILE F 6  34   ? 160.240 92.839  107.320 1.00 33.54  ? 34   ILE F CG1   1 
ATOM   26082 C  CG2   . ILE F 6  34   ? 160.932 92.037  109.543 1.00 32.80  ? 34   ILE F CG2   1 
ATOM   26083 C  CD1   . ILE F 6  34   ? 158.847 93.187  107.756 1.00 31.28  ? 34   ILE F CD1   1 
ATOM   26084 N  N     . TYR F 6  35   ? 162.644 89.003  108.272 1.00 36.56  ? 35   TYR F N     1 
ATOM   26085 C  CA    . TYR F 6  35   ? 162.993 88.047  109.314 1.00 36.36  ? 35   TYR F CA    1 
ATOM   26086 C  C     . TYR F 6  35   ? 164.136 87.100  108.979 1.00 38.39  ? 35   TYR F C     1 
ATOM   26087 O  O     . TYR F 6  35   ? 164.689 86.494  109.899 1.00 40.82  ? 35   TYR F O     1 
ATOM   26088 C  CB    . TYR F 6  35   ? 161.759 87.219  109.700 1.00 33.69  ? 35   TYR F CB    1 
ATOM   26089 C  CG    . TYR F 6  35   ? 160.753 88.019  110.484 1.00 36.05  ? 35   TYR F CG    1 
ATOM   26090 C  CD1   . TYR F 6  35   ? 160.967 88.317  111.820 1.00 35.80  ? 35   TYR F CD1   1 
ATOM   26091 C  CD2   . TYR F 6  35   ? 159.600 88.499  109.883 1.00 34.73  ? 35   TYR F CD2   1 
ATOM   26092 C  CE1   . TYR F 6  35   ? 160.055 89.058  112.537 1.00 36.37  ? 35   TYR F CE1   1 
ATOM   26093 C  CE2   . TYR F 6  35   ? 158.688 89.241  110.590 1.00 32.66  ? 35   TYR F CE2   1 
ATOM   26094 C  CZ    . TYR F 6  35   ? 158.918 89.518  111.917 1.00 35.26  ? 35   TYR F CZ    1 
ATOM   26095 O  OH    . TYR F 6  35   ? 158.011 90.259  112.635 1.00 35.11  ? 35   TYR F OH    1 
ATOM   26096 N  N     . VAL F 6  36   ? 164.514 86.960  107.711 1.00 37.00  ? 36   VAL F N     1 
ATOM   26097 C  CA    . VAL F 6  36   ? 165.526 85.973  107.348 1.00 36.24  ? 36   VAL F CA    1 
ATOM   26098 C  C     . VAL F 6  36   ? 166.881 86.397  107.897 1.00 38.13  ? 36   VAL F C     1 
ATOM   26099 O  O     . VAL F 6  36   ? 167.332 87.530  107.685 1.00 39.81  ? 36   VAL F O     1 
ATOM   26100 C  CB    . VAL F 6  36   ? 165.573 85.788  105.826 1.00 36.70  ? 36   VAL F CB    1 
ATOM   26101 C  CG1   . VAL F 6  36   ? 166.907 85.223  105.407 1.00 34.72  ? 36   VAL F CG1   1 
ATOM   26102 C  CG2   . VAL F 6  36   ? 164.445 84.885  105.371 1.00 37.95  ? 36   VAL F CG2   1 
ATOM   26103 N  N     . GLY F 6  37   ? 167.538 85.487  108.610 1.00 37.23  ? 37   GLY F N     1 
ATOM   26104 C  CA    . GLY F 6  37   ? 168.869 85.750  109.114 1.00 39.31  ? 37   GLY F CA    1 
ATOM   26105 C  C     . GLY F 6  37   ? 168.944 86.631  110.337 1.00 41.78  ? 37   GLY F C     1 
ATOM   26106 O  O     . GLY F 6  37   ? 169.968 87.284  110.552 1.00 43.45  ? 37   GLY F O     1 
ATOM   26107 N  N     . LYS F 6  38   ? 167.896 86.668  111.153 1.00 38.78  ? 38   LYS F N     1 
ATOM   26108 C  CA    . LYS F 6  38   ? 167.870 87.520  112.329 1.00 40.53  ? 38   LYS F CA    1 
ATOM   26109 C  C     . LYS F 6  38   ? 167.336 86.724  113.510 1.00 37.93  ? 38   LYS F C     1 
ATOM   26110 O  O     . LYS F 6  38   ? 166.773 85.642  113.351 1.00 40.28  ? 38   LYS F O     1 
ATOM   26111 C  CB    . LYS F 6  38   ? 167.018 88.775  112.095 1.00 41.37  ? 38   LYS F CB    1 
ATOM   26112 C  CG    . LYS F 6  38   ? 167.561 89.691  111.009 1.00 39.70  ? 38   LYS F CG    1 
ATOM   26113 C  CD    . LYS F 6  38   ? 167.518 91.146  111.428 1.00 40.14  ? 38   LYS F CD    1 
ATOM   26114 C  CE    . LYS F 6  38   ? 167.194 92.042  110.246 1.00 37.87  ? 38   LYS F CE    1 
ATOM   26115 N  NZ    . LYS F 6  38   ? 167.685 93.431  110.443 1.00 38.14  ? 38   LYS F NZ    1 
ATOM   26116 N  N     . CYS F 6  39   ? 167.532 87.271  114.703 1.00 44.72  ? 39   CYS F N     1 
ATOM   26117 C  CA    . CYS F 6  39   ? 167.040 86.649  115.924 1.00 47.21  ? 39   CYS F CA    1 
ATOM   26118 C  C     . CYS F 6  39   ? 165.691 87.249  116.298 1.00 50.03  ? 39   CYS F C     1 
ATOM   26119 O  O     . CYS F 6  39   ? 165.514 88.470  116.258 1.00 51.24  ? 39   CYS F O     1 
ATOM   26120 C  CB    . CYS F 6  39   ? 168.038 86.830  117.067 1.00 47.31  ? 39   CYS F CB    1 
ATOM   26121 S  SG    . CYS F 6  39   ? 169.506 85.782  116.942 1.00 61.30  ? 39   CYS F SG    1 
ATOM   26122 N  N     . PHE F 6  40   ? 164.743 86.389  116.654 1.00 42.74  ? 40   PHE F N     1 
ATOM   26123 C  CA    . PHE F 6  40   ? 163.404 86.834  117.013 1.00 38.64  ? 40   PHE F CA    1 
ATOM   26124 C  C     . PHE F 6  40   ? 162.781 85.792  117.922 1.00 42.88  ? 40   PHE F C     1 
ATOM   26125 O  O     . PHE F 6  40   ? 162.619 84.637  117.519 1.00 44.14  ? 40   PHE F O     1 
ATOM   26126 C  CB    . PHE F 6  40   ? 162.541 87.054  115.769 1.00 37.73  ? 40   PHE F CB    1 
ATOM   26127 C  CG    . PHE F 6  40   ? 161.155 87.545  116.070 1.00 39.90  ? 40   PHE F CG    1 
ATOM   26128 C  CD1   . PHE F 6  40   ? 160.954 88.631  116.903 1.00 42.13  ? 40   PHE F CD1   1 
ATOM   26129 C  CD2   . PHE F 6  40   ? 160.051 86.918  115.518 1.00 41.54  ? 40   PHE F CD2   1 
ATOM   26130 C  CE1   . PHE F 6  40   ? 159.680 89.080  117.185 1.00 42.34  ? 40   PHE F CE1   1 
ATOM   26131 C  CE2   . PHE F 6  40   ? 158.774 87.364  115.794 1.00 42.41  ? 40   PHE F CE2   1 
ATOM   26132 C  CZ    . PHE F 6  40   ? 158.589 88.446  116.628 1.00 44.46  ? 40   PHE F CZ    1 
ATOM   26133 N  N     . LYS F 6  41   ? 162.449 86.201  119.145 1.00 41.64  ? 41   LYS F N     1 
ATOM   26134 C  CA    . LYS F 6  41   ? 161.769 85.348  120.115 1.00 40.01  ? 41   LYS F CA    1 
ATOM   26135 C  C     . LYS F 6  41   ? 162.597 84.103  120.444 1.00 41.53  ? 41   LYS F C     1 
ATOM   26136 O  O     . LYS F 6  41   ? 162.144 82.967  120.296 1.00 41.53  ? 41   LYS F O     1 
ATOM   26137 C  CB    . LYS F 6  41   ? 160.374 84.964  119.611 1.00 39.71  ? 41   LYS F CB    1 
ATOM   26138 C  CG    . LYS F 6  41   ? 159.275 85.889  120.070 1.00 40.87  ? 41   LYS F CG    1 
ATOM   26139 C  CD    . LYS F 6  41   ? 158.157 85.937  119.056 1.00 40.37  ? 41   LYS F CD    1 
ATOM   26140 C  CE    . LYS F 6  41   ? 156.966 86.708  119.590 1.00 40.50  ? 41   LYS F CE    1 
ATOM   26141 N  NZ    . LYS F 6  41   ? 155.834 86.701  118.630 1.00 39.09  ? 41   LYS F NZ    1 
ATOM   26142 N  N     . ASN F 6  42   ? 163.825 84.344  120.907 1.00 44.70  ? 42   ASN F N     1 
ATOM   26143 C  CA    . ASN F 6  42   ? 164.719 83.290  121.398 1.00 46.77  ? 42   ASN F CA    1 
ATOM   26144 C  C     . ASN F 6  42   ? 164.995 82.227  120.336 1.00 46.49  ? 42   ASN F C     1 
ATOM   26145 O  O     . ASN F 6  42   ? 164.941 81.027  120.606 1.00 44.65  ? 42   ASN F O     1 
ATOM   26146 C  CB    . ASN F 6  42   ? 164.159 82.645  122.666 1.00 45.71  ? 42   ASN F CB    1 
ATOM   26147 C  CG    . ASN F 6  42   ? 165.237 82.067  123.552 1.00 46.46  ? 42   ASN F CG    1 
ATOM   26148 O  OD1   . ASN F 6  42   ? 166.424 82.314  123.349 1.00 47.77  ? 42   ASN F OD1   1 
ATOM   26149 N  ND2   . ASN F 6  42   ? 164.828 81.282  124.539 1.00 46.45  ? 42   ASN F ND2   1 
ATOM   26150 N  N     . SER F 6  43   ? 165.293 82.668  119.117 1.00 43.82  ? 43   SER F N     1 
ATOM   26151 C  CA    . SER F 6  43   ? 165.585 81.756  118.019 1.00 43.95  ? 43   SER F CA    1 
ATOM   26152 C  C     . SER F 6  43   ? 166.279 82.530  116.911 1.00 46.33  ? 43   SER F C     1 
ATOM   26153 O  O     . SER F 6  43   ? 166.438 83.750  116.990 1.00 44.20  ? 43   SER F O     1 
ATOM   26154 C  CB    . SER F 6  43   ? 164.316 81.091  117.488 1.00 43.60  ? 43   SER F CB    1 
ATOM   26155 O  OG    . SER F 6  43   ? 163.833 81.786  116.358 1.00 44.37  ? 43   SER F OG    1 
ATOM   26156 N  N     . PHE F 6  44   ? 166.705 81.801  115.880 1.00 43.85  ? 44   PHE F N     1 
ATOM   26157 C  CA    . PHE F 6  44   ? 167.318 82.383  114.692 1.00 42.12  ? 44   PHE F CA    1 
ATOM   26158 C  C     . PHE F 6  44   ? 166.600 81.842  113.464 1.00 43.59  ? 44   PHE F C     1 
ATOM   26159 O  O     . PHE F 6  44   ? 166.516 80.625  113.281 1.00 46.09  ? 44   PHE F O     1 
ATOM   26160 C  CB    . PHE F 6  44   ? 168.812 82.058  114.634 1.00 39.14  ? 44   PHE F CB    1 
ATOM   26161 C  CG    . PHE F 6  44   ? 169.538 82.720  113.497 1.00 43.60  ? 44   PHE F CG    1 
ATOM   26162 C  CD1   . PHE F 6  44   ? 170.283 83.862  113.715 1.00 43.28  ? 44   PHE F CD1   1 
ATOM   26163 C  CD2   . PHE F 6  44   ? 169.485 82.194  112.215 1.00 44.14  ? 44   PHE F CD2   1 
ATOM   26164 C  CE1   . PHE F 6  44   ? 170.955 84.471  112.686 1.00 42.81  ? 44   PHE F CE1   1 
ATOM   26165 C  CE2   . PHE F 6  44   ? 170.151 82.802  111.177 1.00 43.41  ? 44   PHE F CE2   1 
ATOM   26166 C  CZ    . PHE F 6  44   ? 170.888 83.943  111.412 1.00 42.76  ? 44   PHE F CZ    1 
ATOM   26167 N  N     . ILE F 6  45   ? 166.108 82.738  112.617 1.00 38.74  ? 45   ILE F N     1 
ATOM   26168 C  CA    . ILE F 6  45   ? 165.291 82.357  111.469 1.00 41.06  ? 45   ILE F CA    1 
ATOM   26169 C  C     . ILE F 6  45   ? 166.193 82.105  110.268 1.00 38.84  ? 45   ILE F C     1 
ATOM   26170 O  O     . ILE F 6  45   ? 167.085 82.908  109.969 1.00 41.39  ? 45   ILE F O     1 
ATOM   26171 C  CB    . ILE F 6  45   ? 164.241 83.438  111.161 1.00 37.45  ? 45   ILE F CB    1 
ATOM   26172 C  CG1   . ILE F 6  45   ? 163.150 83.427  112.228 1.00 37.20  ? 45   ILE F CG1   1 
ATOM   26173 C  CG2   . ILE F 6  45   ? 163.619 83.216  109.794 1.00 35.92  ? 45   ILE F CG2   1 
ATOM   26174 C  CD1   . ILE F 6  45   ? 163.343 84.453  113.318 1.00 38.67  ? 45   ILE F CD1   1 
ATOM   26175 N  N     . LEU F 6  46   ? 165.969 80.983  109.585 1.00 34.81  ? 46   LEU F N     1 
ATOM   26176 C  CA    . LEU F 6  46   ? 166.722 80.605  108.398 1.00 34.65  ? 46   LEU F CA    1 
ATOM   26177 C  C     . LEU F 6  46   ? 165.909 80.739  107.121 1.00 36.46  ? 46   LEU F C     1 
ATOM   26178 O  O     . LEU F 6  46   ? 166.376 81.327  106.141 1.00 36.55  ? 46   LEU F O     1 
ATOM   26179 C  CB    . LEU F 6  46   ? 167.217 79.159  108.522 1.00 34.79  ? 46   LEU F CB    1 
ATOM   26180 C  CG    . LEU F 6  46   ? 168.578 78.925  109.169 1.00 37.03  ? 46   LEU F CG    1 
ATOM   26181 C  CD1   . LEU F 6  46   ? 169.611 79.867  108.572 1.00 35.73  ? 46   LEU F CD1   1 
ATOM   26182 C  CD2   . LEU F 6  46   ? 168.500 79.044  110.679 1.00 35.33  ? 46   LEU F CD2   1 
ATOM   26183 N  N     . ASN F 6  47   ? 164.699 80.191  107.105 1.00 38.90  ? 47   ASN F N     1 
ATOM   26184 C  CA    . ASN F 6  47   ? 163.831 80.245  105.942 1.00 37.47  ? 47   ASN F CA    1 
ATOM   26185 C  C     . ASN F 6  47   ? 162.403 80.488  106.407 1.00 39.08  ? 47   ASN F C     1 
ATOM   26186 O  O     . ASN F 6  47   ? 162.064 80.271  107.572 1.00 39.43  ? 47   ASN F O     1 
ATOM   26187 C  CB    . ASN F 6  47   ? 163.913 78.952  105.121 1.00 37.93  ? 47   ASN F CB    1 
ATOM   26188 C  CG    . ASN F 6  47   ? 163.297 79.094  103.749 1.00 40.16  ? 47   ASN F CG    1 
ATOM   26189 O  OD1   . ASN F 6  47   ? 162.926 80.191  103.338 1.00 40.02  ? 47   ASN F OD1   1 
ATOM   26190 N  ND2   . ASN F 6  47   ? 163.171 77.983  103.035 1.00 39.23  ? 47   ASN F ND2   1 
ATOM   26191 N  N     . ILE F 6  48   ? 161.569 80.958  105.488 1.00 38.04  ? 48   ILE F N     1 
ATOM   26192 C  CA    . ILE F 6  48   ? 160.136 81.077  105.718 1.00 37.16  ? 48   ILE F CA    1 
ATOM   26193 C  C     . ILE F 6  48   ? 159.498 79.875  105.031 1.00 37.97  ? 48   ILE F C     1 
ATOM   26194 O  O     . ILE F 6  48   ? 159.460 79.796  103.801 1.00 36.35  ? 48   ILE F O     1 
ATOM   26195 C  CB    . ILE F 6  48   ? 159.572 82.399  105.188 1.00 37.20  ? 48   ILE F CB    1 
ATOM   26196 C  CG1   . ILE F 6  48   ? 160.355 83.597  105.725 1.00 36.84  ? 48   ILE F CG1   1 
ATOM   26197 C  CG2   . ILE F 6  48   ? 158.117 82.540  105.578 1.00 35.30  ? 48   ILE F CG2   1 
ATOM   26198 C  CD1   . ILE F 6  48   ? 160.284 83.782  107.216 1.00 36.29  ? 48   ILE F CD1   1 
ATOM   26199 N  N     . THR F 6  49   ? 159.000 78.925  105.825 1.00 36.56  ? 49   THR F N     1 
ATOM   26200 C  CA    . THR F 6  49   ? 158.372 77.740  105.251 1.00 35.67  ? 49   THR F CA    1 
ATOM   26201 C  C     . THR F 6  49   ? 157.057 78.088  104.568 1.00 36.66  ? 49   THR F C     1 
ATOM   26202 O  O     . THR F 6  49   ? 156.796 77.650  103.443 1.00 39.07  ? 49   THR F O     1 
ATOM   26203 C  CB    . THR F 6  49   ? 158.148 76.683  106.333 1.00 38.40  ? 49   THR F CB    1 
ATOM   26204 O  OG1   . THR F 6  49   ? 159.384 76.407  107.001 1.00 39.71  ? 49   THR F OG1   1 
ATOM   26205 C  CG2   . THR F 6  49   ? 157.620 75.400  105.721 1.00 33.40  ? 49   THR F CG2   1 
ATOM   26206 N  N     . GLY F 6  50   ? 156.217 78.876  105.227 1.00 33.91  ? 50   GLY F N     1 
ATOM   26207 C  CA    . GLY F 6  50   ? 154.949 79.259  104.634 1.00 31.58  ? 50   GLY F CA    1 
ATOM   26208 C  C     . GLY F 6  50   ? 154.109 80.034  105.622 1.00 34.42  ? 50   GLY F C     1 
ATOM   26209 O  O     . GLY F 6  50   ? 154.446 80.156  106.802 1.00 37.99  ? 50   GLY F O     1 
ATOM   26210 N  N     . VAL F 6  51   ? 152.991 80.546  105.120 1.00 28.19  ? 51   VAL F N     1 
ATOM   26211 C  CA    . VAL F 6  51   ? 152.077 81.373  105.897 1.00 25.82  ? 51   VAL F CA    1 
ATOM   26212 C  C     . VAL F 6  51   ? 150.889 80.509  106.289 1.00 26.82  ? 51   VAL F C     1 
ATOM   26213 O  O     . VAL F 6  51   ? 150.077 80.126  105.439 1.00 28.23  ? 51   VAL F O     1 
ATOM   26214 C  CB    . VAL F 6  51   ? 151.633 82.616  105.121 1.00 27.11  ? 51   VAL F CB    1 
ATOM   26215 C  CG1   . VAL F 6  51   ? 150.515 83.331  105.854 1.00 26.23  ? 51   VAL F CG1   1 
ATOM   26216 C  CG2   . VAL F 6  51   ? 152.807 83.538  104.930 1.00 26.09  ? 51   VAL F CG2   1 
ATOM   26217 N  N     . ILE F 6  52   ? 150.792 80.205  107.582 1.00 26.84  ? 52   ILE F N     1 
ATOM   26218 C  CA    . ILE F 6  52   ? 149.719 79.354  108.080 1.00 26.09  ? 52   ILE F CA    1 
ATOM   26219 C  C     . ILE F 6  52   ? 148.386 80.082  108.030 1.00 28.52  ? 52   ILE F C     1 
ATOM   26220 O  O     . ILE F 6  52   ? 147.385 79.534  107.559 1.00 33.16  ? 52   ILE F O     1 
ATOM   26221 C  CB    . ILE F 6  52   ? 150.042 78.895  109.511 1.00 27.12  ? 52   ILE F CB    1 
ATOM   26222 C  CG1   . ILE F 6  52   ? 151.291 78.024  109.527 1.00 26.99  ? 52   ILE F CG1   1 
ATOM   26223 C  CG2   . ILE F 6  52   ? 148.866 78.165  110.108 1.00 27.84  ? 52   ILE F CG2   1 
ATOM   26224 C  CD1   . ILE F 6  52   ? 151.898 77.912  110.879 1.00 26.63  ? 52   ILE F CD1   1 
ATOM   26225 N  N     . GLN F 6  53   ? 148.353 81.326  108.501 1.00 26.99  ? 53   GLN F N     1 
ATOM   26226 C  CA    . GLN F 6  53   ? 147.098 82.015  108.762 1.00 25.68  ? 53   GLN F CA    1 
ATOM   26227 C  C     . GLN F 6  53   ? 147.331 83.512  108.665 1.00 25.15  ? 53   GLN F C     1 
ATOM   26228 O  O     . GLN F 6  53   ? 148.385 83.998  109.079 1.00 27.85  ? 53   GLN F O     1 
ATOM   26229 C  CB    . GLN F 6  53   ? 146.582 81.638  110.146 1.00 22.82  ? 53   GLN F CB    1 
ATOM   26230 C  CG    . GLN F 6  53   ? 145.096 81.499  110.260 1.00 26.46  ? 53   GLN F CG    1 
ATOM   26231 C  CD    . GLN F 6  53   ? 144.702 80.850  111.560 1.00 28.77  ? 53   GLN F CD    1 
ATOM   26232 O  OE1   . GLN F 6  53   ? 145.555 80.485  112.362 1.00 24.75  ? 53   GLN F OE1   1 
ATOM   26233 N  NE2   . GLN F 6  53   ? 143.406 80.717  111.786 1.00 28.47  ? 53   GLN F NE2   1 
ATOM   26234 N  N     . ARG F 6  54   ? 146.358 84.240  108.125 1.00 17.83  ? 54   ARG F N     1 
ATOM   26235 C  CA    . ARG F 6  54   ? 146.489 85.678  107.950 1.00 17.10  ? 54   ARG F CA    1 
ATOM   26236 C  C     . ARG F 6  54   ? 145.130 86.339  108.113 1.00 20.21  ? 54   ARG F C     1 
ATOM   26237 O  O     . ARG F 6  54   ? 144.089 85.689  108.049 1.00 27.01  ? 54   ARG F O     1 
ATOM   26238 C  CB    . ARG F 6  54   ? 147.082 86.024  106.582 1.00 15.93  ? 54   ARG F CB    1 
ATOM   26239 C  CG    . ARG F 6  54   ? 146.097 85.895  105.452 1.00 14.46  ? 54   ARG F CG    1 
ATOM   26240 C  CD    . ARG F 6  54   ? 146.660 86.401  104.162 1.00 13.57  ? 54   ARG F CD    1 
ATOM   26241 N  NE    . ARG F 6  54   ? 145.694 86.314  103.079 1.00 15.48  ? 54   ARG F NE    1 
ATOM   26242 C  CZ    . ARG F 6  54   ? 144.822 87.263  102.776 1.00 20.25  ? 54   ARG F CZ    1 
ATOM   26243 N  NH1   . ARG F 6  54   ? 144.760 88.387  103.463 1.00 23.45  ? 54   ARG F NH1   1 
ATOM   26244 N  NH2   . ARG F 6  54   ? 143.991 87.079  101.757 1.00 21.40  ? 54   ARG F NH2   1 
ATOM   26245 N  N     . SER F 6  55   ? 145.145 87.646  108.312 1.00 14.39  ? 55   SER F N     1 
ATOM   26246 C  CA    . SER F 6  55   ? 143.952 88.466  108.403 1.00 11.18  ? 55   SER F CA    1 
ATOM   26247 C  C     . SER F 6  55   ? 143.722 89.211  107.101 1.00 10.24  ? 55   SER F C     1 
ATOM   26248 O  O     . SER F 6  55   ? 144.560 89.177  106.197 1.00 16.01  ? 55   SER F O     1 
ATOM   26249 C  CB    . SER F 6  55   ? 144.081 89.468  109.549 1.00 10.35  ? 55   SER F CB    1 
ATOM   26250 O  OG    . SER F 6  55   ? 144.840 90.585  109.153 1.00 16.25  ? 55   SER F OG    1 
ATOM   26251 N  N     . PRO F 6  56   ? 142.574 89.870  106.950 1.00 17.27  ? 56   PRO F N     1 
ATOM   26252 C  CA    . PRO F 6  56   ? 142.416 90.820  105.843 1.00 15.50  ? 56   PRO F CA    1 
ATOM   26253 C  C     . PRO F 6  56   ? 143.392 91.982  105.963 1.00 13.34  ? 56   PRO F C     1 
ATOM   26254 O  O     . PRO F 6  56   ? 144.116 92.125  106.946 1.00 15.00  ? 56   PRO F O     1 
ATOM   26255 C  CB    . PRO F 6  56   ? 140.970 91.295  105.990 1.00 11.79  ? 56   PRO F CB    1 
ATOM   26256 C  CG    . PRO F 6  56   ? 140.298 90.206  106.696 1.00 12.18  ? 56   PRO F CG    1 
ATOM   26257 C  CD    . PRO F 6  56   ? 141.292 89.612  107.625 1.00 12.18  ? 56   PRO F CD    1 
ATOM   26258 N  N     . CYS F 6  57   ? 143.411 92.819  104.935 1.00 10.36  ? 57   CYS F N     1 
ATOM   26259 C  CA    . CYS F 6  57   ? 144.244 94.018  104.962 1.00 10.14  ? 57   CYS F CA    1 
ATOM   26260 C  C     . CYS F 6  57   ? 143.411 95.168  105.518 1.00 9.78   ? 57   CYS F C     1 
ATOM   26261 O  O     . CYS F 6  57   ? 142.614 95.783  104.818 1.00 11.68  ? 57   CYS F O     1 
ATOM   26262 C  CB    . CYS F 6  57   ? 144.790 94.329  103.575 1.00 10.47  ? 57   CYS F CB    1 
ATOM   26263 S  SG    . CYS F 6  57   ? 145.976 95.686  103.523 1.00 26.68  ? 57   CYS F SG    1 
ATOM   26264 N  N     . PHE F 6  58   ? 143.584 95.443  106.804 1.00 5.53   ? 58   PHE F N     1 
ATOM   26265 C  CA    . PHE F 6  58   ? 142.895 96.552  107.438 1.00 4.61   ? 58   PHE F CA    1 
ATOM   26266 C  C     . PHE F 6  58   ? 143.584 97.870  107.126 1.00 1.96   ? 58   PHE F C     1 
ATOM   26267 O  O     . PHE F 6  58   ? 144.805 97.945  107.026 1.00 17.18  ? 58   PHE F O     1 
ATOM   26268 C  CB    . PHE F 6  58   ? 142.848 96.370  108.951 1.00 8.41   ? 58   PHE F CB    1 
ATOM   26269 C  CG    . PHE F 6  58   ? 142.332 95.038  109.400 1.00 8.18   ? 58   PHE F CG    1 
ATOM   26270 C  CD1   . PHE F 6  58   ? 141.000 94.719  109.265 1.00 11.89  ? 58   PHE F CD1   1 
ATOM   26271 C  CD2   . PHE F 6  58   ? 143.168 94.126  109.997 1.00 5.88   ? 58   PHE F CD2   1 
ATOM   26272 C  CE1   . PHE F 6  58   ? 140.521 93.513  109.687 1.00 10.78  ? 58   PHE F CE1   1 
ATOM   26273 C  CE2   . PHE F 6  58   ? 142.689 92.923  110.427 1.00 6.78   ? 58   PHE F CE2   1 
ATOM   26274 C  CZ    . PHE F 6  58   ? 141.363 92.615  110.271 1.00 9.77   ? 58   PHE F CZ    1 
ATOM   26275 N  N     . ILE F 6  59   ? 142.791 98.920  107.002 1.00 0.08   ? 59   ILE F N     1 
ATOM   26276 C  CA    . ILE F 6  59   ? 143.311 100.267 106.817 1.00 1.81   ? 59   ILE F CA    1 
ATOM   26277 C  C     . ILE F 6  59   ? 143.590 100.866 108.182 1.00 1.67   ? 59   ILE F C     1 
ATOM   26278 O  O     . ILE F 6  59   ? 142.796 100.705 109.110 1.00 6.50   ? 59   ILE F O     1 
ATOM   26279 C  CB    . ILE F 6  59   ? 142.332 101.136 106.012 1.00 0.98   ? 59   ILE F CB    1 
ATOM   26280 C  CG1   . ILE F 6  59   ? 141.937 100.418 104.729 1.00 7.60   ? 59   ILE F CG1   1 
ATOM   26281 C  CG2   . ILE F 6  59   ? 142.958 102.474 105.678 1.00 9.55   ? 59   ILE F CG2   1 
ATOM   26282 C  CD1   . ILE F 6  59   ? 143.111 100.021 103.889 1.00 3.62   ? 59   ILE F CD1   1 
ATOM   26283 N  N     . MET F 6  60   ? 144.728 101.539 108.311 1.00 2.47   ? 60   MET F N     1 
ATOM   26284 C  CA    . MET F 6  60   ? 145.106 102.138 109.584 1.00 1.62   ? 60   MET F CA    1 
ATOM   26285 C  C     . MET F 6  60   ? 144.088 103.188 109.994 1.00 4.04   ? 60   MET F C     1 
ATOM   26286 O  O     . MET F 6  60   ? 143.534 103.901 109.158 1.00 16.22  ? 60   MET F O     1 
ATOM   26287 C  CB    . MET F 6  60   ? 146.494 102.753 109.481 1.00 9.77   ? 60   MET F CB    1 
ATOM   26288 C  CG    . MET F 6  60   ? 147.611 101.754 109.615 1.00 7.30   ? 60   MET F CG    1 
ATOM   26289 S  SD    . MET F 6  60   ? 149.227 102.527 109.637 1.00 24.92  ? 60   MET F SD    1 
ATOM   26290 C  CE    . MET F 6  60   ? 150.213 101.279 108.842 1.00 4.88   ? 60   MET F CE    1 
ATOM   26291 N  N     . ARG F 6  61   ? 143.839 103.277 111.291 1.00 2.80   ? 61   ARG F N     1 
ATOM   26292 C  CA    . ARG F 6  61   ? 142.694 104.002 111.809 1.00 1.77   ? 61   ARG F CA    1 
ATOM   26293 C  C     . ARG F 6  61   ? 143.061 105.221 112.640 1.00 4.23   ? 61   ARG F C     1 
ATOM   26294 O  O     . ARG F 6  61   ? 142.235 106.121 112.776 1.00 8.04   ? 61   ARG F O     1 
ATOM   26295 C  CB    . ARG F 6  61   ? 141.846 103.054 112.655 1.00 1.82   ? 61   ARG F CB    1 
ATOM   26296 C  CG    . ARG F 6  61   ? 140.422 103.448 112.856 1.00 9.92   ? 61   ARG F CG    1 
ATOM   26297 C  CD    . ARG F 6  61   ? 139.880 102.844 114.133 1.00 8.73   ? 61   ARG F CD    1 
ATOM   26298 N  NE    . ARG F 6  61   ? 139.707 103.844 115.179 1.00 13.57  ? 61   ARG F NE    1 
ATOM   26299 C  CZ    . ARG F 6  61   ? 140.278 103.796 116.373 1.00 10.92  ? 61   ARG F CZ    1 
ATOM   26300 N  NH1   . ARG F 6  61   ? 141.058 102.791 116.727 1.00 8.17   ? 61   ARG F NH1   1 
ATOM   26301 N  NH2   . ARG F 6  61   ? 140.065 104.785 117.232 1.00 5.36   ? 61   ARG F NH2   1 
ATOM   26302 N  N     . THR F 6  62   ? 144.263 105.279 113.199 1.00 3.17   ? 62   THR F N     1 
ATOM   26303 C  CA    . THR F 6  62   ? 144.635 106.338 114.122 1.00 4.06   ? 62   THR F CA    1 
ATOM   26304 C  C     . THR F 6  62   ? 145.497 107.412 113.481 1.00 0.05   ? 62   THR F C     1 
ATOM   26305 O  O     . THR F 6  62   ? 146.035 108.262 114.190 1.00 1.55   ? 62   THR F O     1 
ATOM   26306 C  CB    . THR F 6  62   ? 145.342 105.752 115.342 1.00 4.36   ? 62   THR F CB    1 
ATOM   26307 O  OG1   . THR F 6  62   ? 146.473 104.990 114.917 1.00 7.01   ? 62   THR F OG1   1 
ATOM   26308 C  CG2   . THR F 6  62   ? 144.406 104.868 116.136 1.00 0.29   ? 62   THR F CG2   1 
ATOM   26309 N  N     . ASN F 6  63   ? 145.635 107.398 112.161 1.00 0.36   ? 63   ASN F N     1 
ATOM   26310 C  CA    . ASN F 6  63   ? 146.340 108.450 111.451 1.00 1.69   ? 63   ASN F CA    1 
ATOM   26311 C  C     . ASN F 6  63   ? 145.767 108.536 110.048 1.00 3.56   ? 63   ASN F C     1 
ATOM   26312 O  O     . ASN F 6  63   ? 145.028 107.656 109.607 1.00 3.11   ? 63   ASN F O     1 
ATOM   26313 C  CB    . ASN F 6  63   ? 147.849 108.205 111.420 1.00 4.84   ? 63   ASN F CB    1 
ATOM   26314 C  CG    . ASN F 6  63   ? 148.209 106.863 110.864 1.00 2.91   ? 63   ASN F CG    1 
ATOM   26315 O  OD1   . ASN F 6  63   ? 147.356 106.106 110.445 1.00 8.22   ? 63   ASN F OD1   1 
ATOM   26316 N  ND2   . ASN F 6  63   ? 149.478 106.550 110.879 1.00 7.09   ? 63   ASN F ND2   1 
ATOM   26317 N  N     . ASN F 6  64   ? 146.105 109.618 109.351 1.00 0.83   ? 64   ASN F N     1 
ATOM   26318 C  CA    . ASN F 6  64   ? 145.542 109.902 108.040 1.00 1.62   ? 64   ASN F CA    1 
ATOM   26319 C  C     . ASN F 6  64   ? 146.422 109.424 106.901 1.00 14.95  ? 64   ASN F C     1 
ATOM   26320 O  O     . ASN F 6  64   ? 146.316 109.945 105.790 1.00 9.97   ? 64   ASN F O     1 
ATOM   26321 C  CB    . ASN F 6  64   ? 145.261 111.397 107.897 1.00 1.52   ? 64   ASN F CB    1 
ATOM   26322 C  CG    . ASN F 6  64   ? 144.083 111.863 108.725 1.00 1.01   ? 64   ASN F CG    1 
ATOM   26323 O  OD1   . ASN F 6  64   ? 143.199 111.089 109.054 1.00 2.93   ? 64   ASN F OD1   1 
ATOM   26324 N  ND2   . ASN F 6  64   ? 144.049 113.141 109.022 1.00 2.54   ? 64   ASN F ND2   1 
ATOM   26325 N  N     . SER F 6  65   ? 147.278 108.436 107.136 1.00 3.06   ? 65   SER F N     1 
ATOM   26326 C  CA    . SER F 6  65   ? 148.209 107.983 106.112 1.00 2.97   ? 65   SER F CA    1 
ATOM   26327 C  C     . SER F 6  65   ? 147.562 107.135 105.028 1.00 7.83   ? 65   SER F C     1 
ATOM   26328 O  O     . SER F 6  65   ? 148.078 107.100 103.912 1.00 11.99  ? 65   SER F O     1 
ATOM   26329 C  CB    . SER F 6  65   ? 149.352 107.203 106.753 1.00 4.23   ? 65   SER F CB    1 
ATOM   26330 O  OG    . SER F 6  65   ? 148.873 106.092 107.473 1.00 12.48  ? 65   SER F OG    1 
ATOM   26331 N  N     . GLY F 6  66   ? 146.458 106.457 105.316 1.00 1.89   ? 66   GLY F N     1 
ATOM   26332 C  CA    . GLY F 6  66   ? 145.839 105.601 104.325 1.00 2.79   ? 66   GLY F CA    1 
ATOM   26333 C  C     . GLY F 6  66   ? 146.535 104.282 104.117 1.00 9.30   ? 66   GLY F C     1 
ATOM   26334 O  O     . GLY F 6  66   ? 146.309 103.624 103.104 1.00 9.55   ? 66   GLY F O     1 
ATOM   26335 N  N     . ARG F 6  67   ? 147.372 103.874 105.058 1.00 6.32   ? 67   ARG F N     1 
ATOM   26336 C  CA    . ARG F 6  67   ? 148.204 102.691 104.947 1.00 3.18   ? 67   ARG F CA    1 
ATOM   26337 C  C     . ARG F 6  67   ? 147.495 101.492 105.564 1.00 12.37  ? 67   ARG F C     1 
ATOM   26338 O  O     . ARG F 6  67   ? 146.553 101.632 106.342 1.00 8.01   ? 67   ARG F O     1 
ATOM   26339 C  CB    . ARG F 6  67   ? 149.543 102.929 105.636 1.00 4.36   ? 67   ARG F CB    1 
ATOM   26340 C  CG    . ARG F 6  67   ? 150.586 103.560 104.757 1.00 8.74   ? 67   ARG F CG    1 
ATOM   26341 C  CD    . ARG F 6  67   ? 151.884 103.737 105.506 1.00 8.92   ? 67   ARG F CD    1 
ATOM   26342 N  NE    . ARG F 6  67   ? 151.710 104.475 106.745 1.00 11.49  ? 67   ARG F NE    1 
ATOM   26343 C  CZ    . ARG F 6  67   ? 152.456 104.310 107.827 1.00 18.36  ? 67   ARG F CZ    1 
ATOM   26344 N  NH1   . ARG F 6  67   ? 153.421 103.408 107.870 1.00 13.59  ? 67   ARG F NH1   1 
ATOM   26345 N  NH2   . ARG F 6  67   ? 152.220 105.062 108.897 1.00 11.31  ? 67   ARG F NH2   1 
ATOM   26346 N  N     . GLY F 6  68   ? 147.961 100.299 105.205 1.00 8.08   ? 68   GLY F N     1 
ATOM   26347 C  CA    . GLY F 6  68   ? 147.351 99.065  105.637 1.00 7.46   ? 68   GLY F CA    1 
ATOM   26348 C  C     . GLY F 6  68   ? 148.203 98.333  106.659 1.00 5.48   ? 68   GLY F C     1 
ATOM   26349 O  O     . GLY F 6  68   ? 149.333 98.702  106.953 1.00 10.06  ? 68   GLY F O     1 
ATOM   26350 N  N     . TYR F 6  69   ? 147.619 97.285  107.222 1.00 6.26   ? 69   TYR F N     1 
ATOM   26351 C  CA    . TYR F 6  69   ? 148.371 96.378  108.070 1.00 7.77   ? 69   TYR F CA    1 
ATOM   26352 C  C     . TYR F 6  69   ? 147.711 95.014  108.022 1.00 8.85   ? 69   TYR F C     1 
ATOM   26353 O  O     . TYR F 6  69   ? 146.536 94.889  107.678 1.00 11.69  ? 69   TYR F O     1 
ATOM   26354 C  CB    . TYR F 6  69   ? 148.499 96.898  109.511 1.00 4.66   ? 69   TYR F CB    1 
ATOM   26355 C  CG    . TYR F 6  69   ? 147.210 96.988  110.290 1.00 9.90   ? 69   TYR F CG    1 
ATOM   26356 C  CD1   . TYR F 6  69   ? 146.390 98.094  110.171 1.00 8.53   ? 69   TYR F CD1   1 
ATOM   26357 C  CD2   . TYR F 6  69   ? 146.829 95.984  111.168 1.00 5.79   ? 69   TYR F CD2   1 
ATOM   26358 C  CE1   . TYR F 6  69   ? 145.223 98.185  110.874 1.00 4.23   ? 69   TYR F CE1   1 
ATOM   26359 C  CE2   . TYR F 6  69   ? 145.664 96.073  111.875 1.00 2.17   ? 69   TYR F CE2   1 
ATOM   26360 C  CZ    . TYR F 6  69   ? 144.864 97.177  111.723 1.00 5.48   ? 69   TYR F CZ    1 
ATOM   26361 O  OH    . TYR F 6  69   ? 143.694 97.288  112.427 1.00 11.44  ? 69   TYR F OH    1 
ATOM   26362 N  N     . MET F 6  70   ? 148.491 93.990  108.343 1.00 8.56   ? 70   MET F N     1 
ATOM   26363 C  CA    . MET F 6  70   ? 148.044 92.610  108.250 1.00 9.14   ? 70   MET F CA    1 
ATOM   26364 C  C     . MET F 6  70   ? 148.642 91.822  109.397 1.00 14.40  ? 70   MET F C     1 
ATOM   26365 O  O     . MET F 6  70   ? 149.790 92.055  109.774 1.00 18.57  ? 70   MET F O     1 
ATOM   26366 C  CB    . MET F 6  70   ? 148.459 91.992  106.918 1.00 2.66   ? 70   MET F CB    1 
ATOM   26367 C  CG    . MET F 6  70   ? 147.649 90.801  106.513 1.00 10.77  ? 70   MET F CG    1 
ATOM   26368 S  SD    . MET F 6  70   ? 148.187 90.129  104.947 1.00 19.70  ? 70   MET F SD    1 
ATOM   26369 C  CE    . MET F 6  70   ? 146.935 90.801  103.877 1.00 5.93   ? 70   MET F CE    1 
ATOM   26370 N  N     . HIS F 6  71   ? 147.864 90.905  109.954 1.00 10.55  ? 71   HIS F N     1 
ATOM   26371 C  CA    . HIS F 6  71   ? 148.367 89.957  110.934 1.00 9.03   ? 71   HIS F CA    1 
ATOM   26372 C  C     . HIS F 6  71   ? 148.699 88.659  110.217 1.00 13.81  ? 71   HIS F C     1 
ATOM   26373 O  O     . HIS F 6  71   ? 147.892 88.160  109.432 1.00 22.36  ? 71   HIS F O     1 
ATOM   26374 C  CB    . HIS F 6  71   ? 147.340 89.703  112.037 1.00 14.10  ? 71   HIS F CB    1 
ATOM   26375 C  CG    . HIS F 6  71   ? 146.826 90.943  112.695 1.00 10.66  ? 71   HIS F CG    1 
ATOM   26376 N  ND1   . HIS F 6  71   ? 147.630 91.790  113.421 1.00 13.20  ? 71   HIS F ND1   1 
ATOM   26377 C  CD2   . HIS F 6  71   ? 145.583 91.469  112.749 1.00 5.91   ? 71   HIS F CD2   1 
ATOM   26378 C  CE1   . HIS F 6  71   ? 146.904 92.786  113.890 1.00 9.37   ? 71   HIS F CE1   1 
ATOM   26379 N  NE2   . HIS F 6  71   ? 145.659 92.613  113.497 1.00 5.08   ? 71   HIS F NE2   1 
ATOM   26380 N  N     . VAL F 6  72   ? 149.890 88.127  110.466 1.00 13.73  ? 72   VAL F N     1 
ATOM   26381 C  CA    . VAL F 6  72   ? 150.376 86.931  109.788 1.00 14.85  ? 72   VAL F CA    1 
ATOM   26382 C  C     . VAL F 6  72   ? 150.824 85.920  110.829 1.00 20.04  ? 72   VAL F C     1 
ATOM   26383 O  O     . VAL F 6  72   ? 151.495 86.278  111.802 1.00 22.28  ? 72   VAL F O     1 
ATOM   26384 C  CB    . VAL F 6  72   ? 151.527 87.249  108.818 1.00 15.10  ? 72   VAL F CB    1 
ATOM   26385 C  CG1   . VAL F 6  72   ? 151.827 86.057  107.957 1.00 17.12  ? 72   VAL F CG1   1 
ATOM   26386 C  CG2   . VAL F 6  72   ? 151.175 88.421  107.946 1.00 18.86  ? 72   VAL F CG2   1 
ATOM   26387 N  N     . ARG F 6  73   ? 150.448 84.665  110.626 1.00 21.88  ? 73   ARG F N     1 
ATOM   26388 C  CA    . ARG F 6  73   ? 150.958 83.540  111.399 1.00 22.54  ? 73   ARG F CA    1 
ATOM   26389 C  C     . ARG F 6  73   ? 151.692 82.633  110.423 1.00 24.21  ? 73   ARG F C     1 
ATOM   26390 O  O     . ARG F 6  73   ? 151.066 82.000  109.570 1.00 25.02  ? 73   ARG F O     1 
ATOM   26391 C  CB    . ARG F 6  73   ? 149.822 82.807  112.106 1.00 25.82  ? 73   ARG F CB    1 
ATOM   26392 C  CG    . ARG F 6  73   ? 150.265 81.836  113.162 1.00 22.85  ? 73   ARG F CG    1 
ATOM   26393 C  CD    . ARG F 6  73   ? 149.126 80.947  113.577 1.00 25.75  ? 73   ARG F CD    1 
ATOM   26394 N  NE    . ARG F 6  73   ? 148.617 81.304  114.895 1.00 28.21  ? 73   ARG F NE    1 
ATOM   26395 C  CZ    . ARG F 6  73   ? 147.369 81.675  115.145 1.00 27.60  ? 73   ARG F CZ    1 
ATOM   26396 N  NH1   . ARG F 6  73   ? 146.461 81.736  114.187 1.00 27.91  ? 73   ARG F NH1   1 
ATOM   26397 N  NH2   . ARG F 6  73   ? 147.020 81.984  116.388 1.00 25.97  ? 73   ARG F NH2   1 
ATOM   26398 N  N     . PHE F 6  74   ? 153.016 82.587  110.527 1.00 30.95  ? 74   PHE F N     1 
ATOM   26399 C  CA    . PHE F 6  74   ? 153.832 81.901  109.537 1.00 31.07  ? 74   PHE F CA    1 
ATOM   26400 C  C     . PHE F 6  74   ? 154.733 80.871  110.200 1.00 31.38  ? 74   PHE F C     1 
ATOM   26401 O  O     . PHE F 6  74   ? 155.091 80.984  111.373 1.00 29.43  ? 74   PHE F O     1 
ATOM   26402 C  CB    . PHE F 6  74   ? 154.667 82.892  108.706 1.00 31.39  ? 74   PHE F CB    1 
ATOM   26403 C  CG    . PHE F 6  74   ? 155.660 83.690  109.504 1.00 32.39  ? 74   PHE F CG    1 
ATOM   26404 C  CD1   . PHE F 6  74   ? 155.274 84.844  110.157 1.00 29.89  ? 74   PHE F CD1   1 
ATOM   26405 C  CD2   . PHE F 6  74   ? 156.981 83.300  109.578 1.00 33.20  ? 74   PHE F CD2   1 
ATOM   26406 C  CE1   . PHE F 6  74   ? 156.180 85.579  110.879 1.00 31.16  ? 74   PHE F CE1   1 
ATOM   26407 C  CE2   . PHE F 6  74   ? 157.891 84.033  110.299 1.00 31.53  ? 74   PHE F CE2   1 
ATOM   26408 C  CZ    . PHE F 6  74   ? 157.491 85.173  110.948 1.00 29.94  ? 74   PHE F CZ    1 
ATOM   26409 N  N     . SER F 6  75   ? 155.093 79.857  109.420 1.00 37.21  ? 75   SER F N     1 
ATOM   26410 C  CA    . SER F 6  75   ? 155.949 78.763  109.857 1.00 38.22  ? 75   SER F CA    1 
ATOM   26411 C  C     . SER F 6  75   ? 157.354 78.978  109.314 1.00 37.30  ? 75   SER F C     1 
ATOM   26412 O  O     . SER F 6  75   ? 157.523 79.268  108.127 1.00 37.24  ? 75   SER F O     1 
ATOM   26413 C  CB    . SER F 6  75   ? 155.396 77.420  109.378 1.00 38.85  ? 75   SER F CB    1 
ATOM   26414 O  OG    . SER F 6  75   ? 156.153 76.345  109.889 1.00 40.53  ? 75   SER F OG    1 
ATOM   26415 N  N     . ALA F 6  76   ? 158.355 78.843  110.177 1.00 36.69  ? 76   ALA F N     1 
ATOM   26416 C  CA    . ALA F 6  76   ? 159.728 79.143  109.803 1.00 38.81  ? 76   ALA F CA    1 
ATOM   26417 C  C     . ALA F 6  76   ? 160.661 78.015  110.215 1.00 39.54  ? 76   ALA F C     1 
ATOM   26418 O  O     . ALA F 6  76   ? 160.403 77.308  111.190 1.00 40.55  ? 76   ALA F O     1 
ATOM   26419 C  CB    . ALA F 6  76   ? 160.196 80.450  110.438 1.00 36.34  ? 76   ALA F CB    1 
ATOM   26420 N  N     . VAL F 6  77   ? 161.741 77.850  109.457 1.00 37.58  ? 77   VAL F N     1 
ATOM   26421 C  CA    . VAL F 6  77   ? 162.820 76.940  109.828 1.00 38.57  ? 77   VAL F CA    1 
ATOM   26422 C  C     . VAL F 6  77   ? 163.824 77.713  110.672 1.00 39.25  ? 77   VAL F C     1 
ATOM   26423 O  O     . VAL F 6  77   ? 164.428 78.681  110.201 1.00 39.89  ? 77   VAL F O     1 
ATOM   26424 C  CB    . VAL F 6  77   ? 163.493 76.337  108.587 1.00 36.72  ? 77   VAL F CB    1 
ATOM   26425 C  CG1   . VAL F 6  77   ? 164.745 75.584  108.985 1.00 35.27  ? 77   VAL F CG1   1 
ATOM   26426 C  CG2   . VAL F 6  77   ? 162.541 75.411  107.860 1.00 36.78  ? 77   VAL F CG2   1 
ATOM   26427 N  N     . VAL F 6  78   ? 164.006 77.289  111.919 1.00 38.11  ? 78   VAL F N     1 
ATOM   26428 C  CA    . VAL F 6  78   ? 164.858 77.991  112.865 1.00 38.34  ? 78   VAL F CA    1 
ATOM   26429 C  C     . VAL F 6  78   ? 165.922 77.030  113.381 1.00 42.43  ? 78   VAL F C     1 
ATOM   26430 O  O     . VAL F 6  78   ? 165.795 75.810  113.281 1.00 42.90  ? 78   VAL F O     1 
ATOM   26431 C  CB    . VAL F 6  78   ? 164.060 78.602  114.033 1.00 39.73  ? 78   VAL F CB    1 
ATOM   26432 C  CG1   . VAL F 6  78   ? 162.902 79.430  113.508 1.00 39.98  ? 78   VAL F CG1   1 
ATOM   26433 C  CG2   . VAL F 6  78   ? 163.553 77.510  114.965 1.00 37.73  ? 78   VAL F CG2   1 
ATOM   26434 N  N     . SER F 6  79   ? 166.988 77.603  113.935 1.00 42.86  ? 79   SER F N     1 
ATOM   26435 C  CA    . SER F 6  79   ? 168.119 76.837  114.446 1.00 44.01  ? 79   SER F CA    1 
ATOM   26436 C  C     . SER F 6  79   ? 168.399 77.275  115.874 1.00 44.31  ? 79   SER F C     1 
ATOM   26437 O  O     . SER F 6  79   ? 169.099 78.268  116.093 1.00 45.89  ? 79   SER F O     1 
ATOM   26438 C  CB    . SER F 6  79   ? 169.357 77.039  113.581 1.00 44.27  ? 79   SER F CB    1 
ATOM   26439 O  OG    . SER F 6  79   ? 169.940 78.302  113.837 1.00 42.81  ? 79   SER F OG    1 
ATOM   26440 N  N     . TYR F 6  80   ? 167.884 76.528  116.843 1.00 48.97  ? 80   TYR F N     1 
ATOM   26441 C  CA    . TYR F 6  80   ? 168.071 76.851  118.248 1.00 51.61  ? 80   TYR F CA    1 
ATOM   26442 C  C     . TYR F 6  80   ? 169.148 75.942  118.824 1.00 53.66  ? 80   TYR F C     1 
ATOM   26443 O  O     . TYR F 6  80   ? 168.997 74.715  118.824 1.00 53.01  ? 80   TYR F O     1 
ATOM   26444 C  CB    . TYR F 6  80   ? 166.768 76.702  119.032 1.00 51.22  ? 80   TYR F CB    1 
ATOM   26445 C  CG    . TYR F 6  80   ? 166.939 76.984  120.501 1.00 52.43  ? 80   TYR F CG    1 
ATOM   26446 C  CD1   . TYR F 6  80   ? 167.164 78.279  120.949 1.00 51.52  ? 80   TYR F CD1   1 
ATOM   26447 C  CD2   . TYR F 6  80   ? 166.882 75.966  121.442 1.00 52.37  ? 80   TYR F CD2   1 
ATOM   26448 C  CE1   . TYR F 6  80   ? 167.328 78.554  122.287 1.00 50.48  ? 80   TYR F CE1   1 
ATOM   26449 C  CE2   . TYR F 6  80   ? 167.045 76.234  122.790 1.00 52.58  ? 80   TYR F CE2   1 
ATOM   26450 C  CZ    . TYR F 6  80   ? 167.270 77.532  123.203 1.00 52.34  ? 80   TYR F CZ    1 
ATOM   26451 O  OH    . TYR F 6  80   ? 167.432 77.821  124.538 1.00 52.93  ? 80   TYR F OH    1 
ATOM   26452 N  N     . LEU F 6  81   ? 170.227 76.545  119.313 1.00 49.01  ? 81   LEU F N     1 
ATOM   26453 C  CA    . LEU F 6  81   ? 171.332 75.814  119.914 1.00 47.56  ? 81   LEU F CA    1 
ATOM   26454 C  C     . LEU F 6  81   ? 170.983 75.410  121.340 1.00 50.19  ? 81   LEU F C     1 
ATOM   26455 O  O     . LEU F 6  81   ? 170.309 76.152  122.060 1.00 51.30  ? 81   LEU F O     1 
ATOM   26456 C  CB    . LEU F 6  81   ? 172.603 76.662  119.904 1.00 44.76  ? 81   LEU F CB    1 
ATOM   26457 C  CG    . LEU F 6  81   ? 173.654 76.347  118.840 1.00 47.21  ? 81   LEU F CG    1 
ATOM   26458 C  CD1   . LEU F 6  81   ? 173.082 76.457  117.437 1.00 45.12  ? 81   LEU F CD1   1 
ATOM   26459 C  CD2   . LEU F 6  81   ? 174.836 77.287  119.006 1.00 46.01  ? 81   LEU F CD2   1 
ATOM   26460 N  N     . ASN F 6  82   ? 171.432 74.225  121.737 1.00 46.84  ? 82   ASN F N     1 
ATOM   26461 C  CA    . ASN F 6  82   ? 171.194 73.737  123.086 1.00 45.23  ? 82   ASN F CA    1 
ATOM   26462 C  C     . ASN F 6  82   ? 172.364 74.087  124.003 1.00 44.32  ? 82   ASN F C     1 
ATOM   26463 O  O     . ASN F 6  82   ? 173.470 74.399  123.558 1.00 43.27  ? 82   ASN F O     1 
ATOM   26464 C  CB    . ASN F 6  82   ? 170.958 72.229  123.079 1.00 46.08  ? 82   ASN F CB    1 
ATOM   26465 C  CG    . ASN F 6  82   ? 169.502 71.870  122.879 1.00 50.52  ? 82   ASN F CG    1 
ATOM   26466 O  OD1   . ASN F 6  82   ? 169.135 71.255  121.879 1.00 51.61  ? 82   ASN F OD1   1 
ATOM   26467 N  ND2   . ASN F 6  82   ? 168.660 72.265  123.828 1.00 46.86  ? 82   ASN F ND2   1 
ATOM   26468 N  N     . ALA F 6  83   ? 172.101 74.034  125.306 1.00 47.46  ? 83   ALA F N     1 
ATOM   26469 C  CA    . ALA F 6  83   ? 173.128 74.333  126.294 1.00 50.13  ? 83   ALA F CA    1 
ATOM   26470 C  C     . ALA F 6  83   ? 174.187 73.236  126.323 1.00 49.25  ? 83   ALA F C     1 
ATOM   26471 O  O     . ALA F 6  83   ? 173.877 72.046  126.219 1.00 47.49  ? 83   ALA F O     1 
ATOM   26472 C  CB    . ALA F 6  83   ? 172.502 74.501  127.676 1.00 44.05  ? 83   ALA F CB    1 
ATOM   26473 N  N     . PHE F 6  84   ? 175.445 73.650  126.476 1.00 53.46  ? 84   PHE F N     1 
ATOM   26474 C  CA    . PHE F 6  84   ? 176.594 72.743  126.434 1.00 53.94  ? 84   PHE F CA    1 
ATOM   26475 C  C     . PHE F 6  84   ? 176.663 71.987  125.107 1.00 53.24  ? 84   PHE F C     1 
ATOM   26476 O  O     . PHE F 6  84   ? 176.981 70.798  125.060 1.00 53.66  ? 84   PHE F O     1 
ATOM   26477 C  CB    . PHE F 6  84   ? 176.578 71.773  127.618 1.00 54.28  ? 84   PHE F CB    1 
ATOM   26478 C  CG    . PHE F 6  84   ? 176.671 72.449  128.958 1.00 54.28  ? 84   PHE F CG    1 
ATOM   26479 C  CD1   . PHE F 6  84   ? 177.896 72.846  129.466 1.00 54.66  ? 84   PHE F CD1   1 
ATOM   26480 C  CD2   . PHE F 6  84   ? 175.532 72.696  129.703 1.00 53.32  ? 84   PHE F CD2   1 
ATOM   26481 C  CE1   . PHE F 6  84   ? 177.988 73.471  130.702 1.00 53.75  ? 84   PHE F CE1   1 
ATOM   26482 C  CE2   . PHE F 6  84   ? 175.613 73.321  130.934 1.00 55.15  ? 84   PHE F CE2   1 
ATOM   26483 C  CZ    . PHE F 6  84   ? 176.846 73.711  131.436 1.00 53.72  ? 84   PHE F CZ    1 
ATOM   26484 N  N     . ASP F 6  85   ? 176.364 72.690  124.015 1.00 50.96  ? 85   ASP F N     1 
ATOM   26485 C  CA    . ASP F 6  85   ? 176.532 72.136  122.680 1.00 50.12  ? 85   ASP F CA    1 
ATOM   26486 C  C     . ASP F 6  85   ? 177.993 72.237  122.245 1.00 51.22  ? 85   ASP F C     1 
ATOM   26487 O  O     . ASP F 6  85   ? 178.838 72.818  122.930 1.00 50.39  ? 85   ASP F O     1 
ATOM   26488 C  CB    . ASP F 6  85   ? 175.607 72.833  121.687 1.00 49.61  ? 85   ASP F CB    1 
ATOM   26489 C  CG    . ASP F 6  85   ? 174.293 72.096  121.503 1.00 52.32  ? 85   ASP F CG    1 
ATOM   26490 O  OD1   . ASP F 6  85   ? 174.062 71.110  122.236 1.00 51.23  ? 85   ASP F OD1   1 
ATOM   26491 O  OD2   . ASP F 6  85   ? 173.496 72.494  120.623 1.00 50.24  ? 85   ASP F OD2   1 
ATOM   26492 N  N     . LEU F 6  86   ? 178.294 71.667  121.080 1.00 50.60  ? 86   LEU F N     1 
ATOM   26493 C  CA    . LEU F 6  86   ? 179.676 71.469  120.653 1.00 50.09  ? 86   LEU F CA    1 
ATOM   26494 C  C     . LEU F 6  86   ? 179.798 71.817  119.174 1.00 48.68  ? 86   LEU F C     1 
ATOM   26495 O  O     . LEU F 6  86   ? 179.222 71.133  118.322 1.00 48.60  ? 86   LEU F O     1 
ATOM   26496 C  CB    . LEU F 6  86   ? 180.111 70.030  120.931 1.00 48.23  ? 86   LEU F CB    1 
ATOM   26497 C  CG    . LEU F 6  86   ? 181.171 69.334  120.083 1.00 51.20  ? 86   LEU F CG    1 
ATOM   26498 C  CD1   . LEU F 6  86   ? 182.506 70.056  120.185 1.00 49.53  ? 86   LEU F CD1   1 
ATOM   26499 C  CD2   . LEU F 6  86   ? 181.293 67.894  120.542 1.00 50.55  ? 86   LEU F CD2   1 
ATOM   26500 N  N     . ILE F 6  87   ? 180.548 72.883  118.874 1.00 46.51  ? 87   ILE F N     1 
ATOM   26501 C  CA    . ILE F 6  87   ? 180.775 73.339  117.508 1.00 46.05  ? 87   ILE F CA    1 
ATOM   26502 C  C     . ILE F 6  87   ? 182.209 73.020  117.112 1.00 48.20  ? 87   ILE F C     1 
ATOM   26503 O  O     . ILE F 6  87   ? 183.133 73.068  117.932 1.00 47.74  ? 87   ILE F O     1 
ATOM   26504 C  CB    . ILE F 6  87   ? 180.469 74.845  117.359 1.00 47.61  ? 87   ILE F CB    1 
ATOM   26505 C  CG1   . ILE F 6  87   ? 179.083 75.162  117.924 1.00 46.49  ? 87   ILE F CG1   1 
ATOM   26506 C  CG2   . ILE F 6  87   ? 180.539 75.271  115.900 1.00 47.42  ? 87   ILE F CG2   1 
ATOM   26507 C  CD1   . ILE F 6  87   ? 178.707 76.620  117.827 1.00 45.89  ? 87   ILE F CD1   1 
ATOM   26508 N  N     . ALA F 6  88   ? 182.401 72.699  115.832 1.00 49.95  ? 88   ALA F N     1 
ATOM   26509 C  CA    . ALA F 6  88   ? 183.667 72.170  115.346 1.00 47.95  ? 88   ALA F CA    1 
ATOM   26510 C  C     . ALA F 6  88   ? 184.570 73.210  114.700 1.00 48.98  ? 88   ALA F C     1 
ATOM   26511 O  O     . ALA F 6  88   ? 185.778 72.972  114.602 1.00 49.80  ? 88   ALA F O     1 
ATOM   26512 C  CB    . ALA F 6  88   ? 183.413 71.049  114.334 1.00 46.41  ? 88   ALA F CB    1 
ATOM   26513 N  N     . ALA F 6  89   ? 184.034 74.344  114.258 1.00 47.04  ? 89   ALA F N     1 
ATOM   26514 C  CA    . ALA F 6  89   ? 184.832 75.338  113.547 1.00 48.64  ? 89   ALA F CA    1 
ATOM   26515 C  C     . ALA F 6  89   ? 184.583 76.717  114.136 1.00 49.34  ? 89   ALA F C     1 
ATOM   26516 O  O     . ALA F 6  89   ? 183.439 77.066  114.441 1.00 47.12  ? 89   ALA F O     1 
ATOM   26517 C  CB    . ALA F 6  89   ? 184.511 75.331  112.049 1.00 44.04  ? 89   ALA F CB    1 
ATOM   26518 N  N     . VAL F 6  90   ? 185.656 77.491  114.300 1.00 50.09  ? 90   VAL F N     1 
ATOM   26519 C  CA    . VAL F 6  90   ? 185.573 78.902  114.670 1.00 48.81  ? 90   VAL F CA    1 
ATOM   26520 C  C     . VAL F 6  90   ? 186.894 79.564  114.305 1.00 49.24  ? 90   VAL F C     1 
ATOM   26521 O  O     . VAL F 6  90   ? 187.963 79.010  114.569 1.00 51.41  ? 90   VAL F O     1 
ATOM   26522 C  CB    . VAL F 6  90   ? 185.256 79.095  116.169 1.00 49.85  ? 90   VAL F CB    1 
ATOM   26523 C  CG1   . VAL F 6  90   ? 186.218 78.309  117.028 1.00 46.68  ? 90   VAL F CG1   1 
ATOM   26524 C  CG2   . VAL F 6  90   ? 185.287 80.570  116.544 1.00 46.72  ? 90   VAL F CG2   1 
ATOM   26525 N  N     . LYS F 6  91   ? 186.828 80.741  113.683 1.00 48.42  ? 91   LYS F N     1 
ATOM   26526 C  CA    . LYS F 6  91   ? 188.014 81.542  113.388 1.00 49.14  ? 91   LYS F CA    1 
ATOM   26527 C  C     . LYS F 6  91   ? 188.103 82.672  114.405 1.00 49.49  ? 91   LYS F C     1 
ATOM   26528 O  O     . LYS F 6  91   ? 187.283 83.594  114.389 1.00 48.67  ? 91   LYS F O     1 
ATOM   26529 C  CB    . LYS F 6  91   ? 187.972 82.109  111.971 1.00 47.23  ? 91   LYS F CB    1 
ATOM   26530 C  CG    . LYS F 6  91   ? 187.524 81.137  110.912 1.00 48.11  ? 91   LYS F CG    1 
ATOM   26531 C  CD    . LYS F 6  91   ? 187.000 81.855  109.677 1.00 48.67  ? 91   LYS F CD    1 
ATOM   26532 C  CE    . LYS F 6  91   ? 187.947 81.715  108.495 1.00 48.53  ? 91   LYS F CE    1 
ATOM   26533 N  NZ    . LYS F 6  91   ? 187.351 82.271  107.248 1.00 46.87  ? 91   LYS F NZ    1 
ATOM   26534 N  N     . ILE F 6  92   ? 189.112 82.614  115.272 1.00 48.56  ? 92   ILE F N     1 
ATOM   26535 C  CA    . ILE F 6  92   ? 189.324 83.686  116.238 1.00 49.13  ? 92   ILE F CA    1 
ATOM   26536 C  C     . ILE F 6  92   ? 189.774 84.935  115.490 1.00 49.58  ? 92   ILE F C     1 
ATOM   26537 O  O     . ILE F 6  92   ? 190.769 84.914  114.756 1.00 47.23  ? 92   ILE F O     1 
ATOM   26538 C  CB    . ILE F 6  92   ? 190.348 83.278  117.306 1.00 48.66  ? 92   ILE F CB    1 
ATOM   26539 C  CG1   . ILE F 6  92   ? 189.780 82.193  118.225 1.00 46.96  ? 92   ILE F CG1   1 
ATOM   26540 C  CG2   . ILE F 6  92   ? 190.770 84.486  118.123 1.00 46.27  ? 92   ILE F CG2   1 
ATOM   26541 C  CD1   . ILE F 6  92   ? 190.052 80.775  117.750 1.00 48.11  ? 92   ILE F CD1   1 
ATOM   26542 N  N     . ILE F 6  93   ? 189.029 86.026  115.660 1.00 47.52  ? 93   ILE F N     1 
ATOM   26543 C  CA    . ILE F 6  93   ? 189.334 87.286  114.993 1.00 47.66  ? 93   ILE F CA    1 
ATOM   26544 C  C     . ILE F 6  93   ? 190.087 88.189  115.956 1.00 45.62  ? 93   ILE F C     1 
ATOM   26545 O  O     . ILE F 6  93   ? 191.148 88.730  115.628 1.00 44.09  ? 93   ILE F O     1 
ATOM   26546 C  CB    . ILE F 6  93   ? 188.054 87.982  114.495 1.00 47.73  ? 93   ILE F CB    1 
ATOM   26547 C  CG1   . ILE F 6  93   ? 187.071 86.962  113.916 1.00 46.48  ? 93   ILE F CG1   1 
ATOM   26548 C  CG2   . ILE F 6  93   ? 188.396 89.049  113.469 1.00 45.09  ? 93   ILE F CG2   1 
ATOM   26549 C  CD1   . ILE F 6  93   ? 185.736 87.563  113.531 1.00 45.22  ? 93   ILE F CD1   1 
ATOM   26550 N  N     . LYS F 6  94   ? 189.540 88.356  117.154 1.00 50.72  ? 94   LYS F N     1 
ATOM   26551 C  CA    . LYS F 6  94   ? 190.073 89.280  118.142 1.00 51.48  ? 94   LYS F CA    1 
ATOM   26552 C  C     . LYS F 6  94   ? 190.603 88.483  119.321 1.00 50.65  ? 94   LYS F C     1 
ATOM   26553 O  O     . LYS F 6  94   ? 189.875 87.680  119.913 1.00 50.84  ? 94   LYS F O     1 
ATOM   26554 C  CB    . LYS F 6  94   ? 189.000 90.271  118.595 1.00 49.47  ? 94   LYS F CB    1 
ATOM   26555 C  CG    . LYS F 6  94   ? 189.460 91.294  119.612 1.00 50.33  ? 94   LYS F CG    1 
ATOM   26556 C  CD    . LYS F 6  94   ? 188.258 91.967  120.246 1.00 50.41  ? 94   LYS F CD    1 
ATOM   26557 C  CE    . LYS F 6  94   ? 188.667 93.091  121.159 1.00 50.60  ? 94   LYS F CE    1 
ATOM   26558 N  NZ    . LYS F 6  94   ? 189.197 94.240  120.376 1.00 50.80  ? 94   LYS F NZ    1 
ATOM   26559 N  N     . ASN F 6  95   ? 191.874 88.701  119.651 1.00 52.47  ? 95   ASN F N     1 
ATOM   26560 C  CA    . ASN F 6  95   ? 192.557 87.970  120.713 1.00 55.01  ? 95   ASN F CA    1 
ATOM   26561 C  C     . ASN F 6  95   ? 193.283 89.002  121.573 1.00 54.63  ? 95   ASN F C     1 
ATOM   26562 O  O     . ASN F 6  95   ? 194.484 89.234  121.405 1.00 52.57  ? 95   ASN F O     1 
ATOM   26563 C  CB    . ASN F 6  95   ? 193.506 86.938  120.119 1.00 51.93  ? 95   ASN F CB    1 
ATOM   26564 C  CG    . ASN F 6  95   ? 193.962 85.915  121.129 1.00 53.43  ? 95   ASN F CG    1 
ATOM   26565 O  OD1   . ASN F 6  95   ? 193.615 85.990  122.307 1.00 54.13  ? 95   ASN F OD1   1 
ATOM   26566 N  ND2   . ASN F 6  95   ? 194.734 84.941  120.671 1.00 52.08  ? 95   ASN F ND2   1 
ATOM   26567 N  N     . ASP F 6  96   ? 192.549 89.605  122.505 1.00 55.10  ? 96   ASP F N     1 
ATOM   26568 C  CA    . ASP F 6  96   ? 193.035 90.675  123.359 1.00 54.45  ? 96   ASP F CA    1 
ATOM   26569 C  C     . ASP F 6  96   ? 193.192 90.152  124.786 1.00 56.00  ? 96   ASP F C     1 
ATOM   26570 O  O     . ASP F 6  96   ? 193.059 88.951  125.051 1.00 56.41  ? 96   ASP F O     1 
ATOM   26571 C  CB    . ASP F 6  96   ? 192.083 91.874  123.296 1.00 53.65  ? 96   ASP F CB    1 
ATOM   26572 C  CG    . ASP F 6  96   ? 192.407 92.823  122.152 1.00 56.42  ? 96   ASP F CG    1 
ATOM   26573 O  OD1   . ASP F 6  96   ? 193.413 92.602  121.448 1.00 55.36  ? 96   ASP F OD1   1 
ATOM   26574 O  OD2   . ASP F 6  96   ? 191.658 93.805  121.967 1.00 56.22  ? 96   ASP F OD2   1 
ATOM   26575 N  N     . SER F 6  97   ? 193.485 91.062  125.715 1.00 53.21  ? 97   SER F N     1 
ATOM   26576 C  CA    . SER F 6  97   ? 193.669 90.666  127.107 1.00 52.80  ? 97   SER F CA    1 
ATOM   26577 C  C     . SER F 6  97   ? 192.348 90.372  127.808 1.00 52.33  ? 97   SER F C     1 
ATOM   26578 O  O     . SER F 6  97   ? 192.323 89.594  128.769 1.00 50.82  ? 97   SER F O     1 
ATOM   26579 C  CB    . SER F 6  97   ? 194.430 91.752  127.869 1.00 51.50  ? 97   SER F CB    1 
ATOM   26580 O  OG    . SER F 6  97   ? 193.762 92.998  127.783 1.00 52.01  ? 97   SER F OG    1 
ATOM   26581 N  N     . ASN F 6  98   ? 191.251 90.977  127.356 1.00 46.94  ? 98   ASN F N     1 
ATOM   26582 C  CA    . ASN F 6  98   ? 189.969 90.830  128.036 1.00 49.10  ? 98   ASN F CA    1 
ATOM   26583 C  C     . ASN F 6  98   ? 189.173 89.628  127.540 1.00 51.13  ? 98   ASN F C     1 
ATOM   26584 O  O     . ASN F 6  98   ? 188.722 88.807  128.345 1.00 50.49  ? 98   ASN F O     1 
ATOM   26585 C  CB    . ASN F 6  98   ? 189.129 92.102  127.876 1.00 46.07  ? 98   ASN F CB    1 
ATOM   26586 C  CG    . ASN F 6  98   ? 189.545 93.198  128.831 1.00 48.26  ? 98   ASN F CG    1 
ATOM   26587 O  OD1   . ASN F 6  98   ? 189.961 92.927  129.956 1.00 48.93  ? 98   ASN F OD1   1 
ATOM   26588 N  ND2   . ASN F 6  98   ? 189.431 94.445  128.390 1.00 48.15  ? 98   ASN F ND2   1 
ATOM   26589 N  N     . ILE F 6  99   ? 188.971 89.522  126.227 1.00 53.57  ? 99   ILE F N     1 
ATOM   26590 C  CA    . ILE F 6  99   ? 188.080 88.525  125.649 1.00 53.83  ? 99   ILE F CA    1 
ATOM   26591 C  C     . ILE F 6  99   ? 188.728 87.916  124.412 1.00 55.15  ? 99   ILE F C     1 
ATOM   26592 O  O     . ILE F 6  99   ? 189.632 88.490  123.802 1.00 55.10  ? 99   ILE F O     1 
ATOM   26593 C  CB    . ILE F 6  99   ? 186.701 89.128  125.301 1.00 55.84  ? 99   ILE F CB    1 
ATOM   26594 C  CG1   . ILE F 6  99   ? 186.856 90.232  124.252 1.00 54.16  ? 99   ILE F CG1   1 
ATOM   26595 C  CG2   . ILE F 6  99   ? 185.985 89.637  126.563 1.00 51.80  ? 99   ILE F CG2   1 
ATOM   26596 C  CD1   . ILE F 6  99   ? 185.656 91.138  124.135 1.00 52.25  ? 99   ILE F CD1   1 
ATOM   26597 N  N     . ILE F 6  100  ? 188.247 86.731  124.047 1.00 53.41  ? 100  ILE F N     1 
ATOM   26598 C  CA    . ILE F 6  100  ? 188.675 86.029  122.845 1.00 53.51  ? 100  ILE F CA    1 
ATOM   26599 C  C     . ILE F 6  100  ? 187.469 85.913  121.927 1.00 53.66  ? 100  ILE F C     1 
ATOM   26600 O  O     . ILE F 6  100  ? 186.447 85.329  122.307 1.00 52.82  ? 100  ILE F O     1 
ATOM   26601 C  CB    . ILE F 6  100  ? 189.256 84.642  123.174 1.00 51.86  ? 100  ILE F CB    1 
ATOM   26602 C  CG1   . ILE F 6  100  ? 190.328 84.769  124.254 1.00 53.53  ? 100  ILE F CG1   1 
ATOM   26603 C  CG2   . ILE F 6  100  ? 189.837 83.999  121.929 1.00 50.63  ? 100  ILE F CG2   1 
ATOM   26604 C  CD1   . ILE F 6  100  ? 190.787 83.445  124.819 1.00 53.80  ? 100  ILE F CD1   1 
ATOM   26605 N  N     . LEU F 6  101  ? 187.593 86.449  120.718 1.00 49.03  ? 101  LEU F N     1 
ATOM   26606 C  CA    . LEU F 6  101  ? 186.452 86.657  119.837 1.00 50.48  ? 101  LEU F CA    1 
ATOM   26607 C  C     . LEU F 6  101  ? 186.602 85.781  118.603 1.00 49.67  ? 101  LEU F C     1 
ATOM   26608 O  O     . LEU F 6  101  ? 187.666 85.760  117.977 1.00 47.58  ? 101  LEU F O     1 
ATOM   26609 C  CB    . LEU F 6  101  ? 186.336 88.136  119.455 1.00 49.52  ? 101  LEU F CB    1 
ATOM   26610 C  CG    . LEU F 6  101  ? 185.172 88.626  118.593 1.00 50.11  ? 101  LEU F CG    1 
ATOM   26611 C  CD1   . LEU F 6  101  ? 185.431 88.458  117.096 1.00 47.39  ? 101  LEU F CD1   1 
ATOM   26612 C  CD2   . LEU F 6  101  ? 183.893 87.914  119.017 1.00 46.89  ? 101  LEU F CD2   1 
ATOM   26613 N  N     . GLY F 6  102  ? 185.525 85.071  118.251 1.00 43.94  ? 102  GLY F N     1 
ATOM   26614 C  CA    . GLY F 6  102  ? 185.505 84.247  117.065 1.00 45.22  ? 102  GLY F CA    1 
ATOM   26615 C  C     . GLY F 6  102  ? 184.098 84.151  116.499 1.00 46.74  ? 102  GLY F C     1 
ATOM   26616 O  O     . GLY F 6  102  ? 183.139 84.674  117.070 1.00 45.95  ? 102  GLY F O     1 
ATOM   26617 N  N     . GLU F 6  103  ? 183.997 83.480  115.349 1.00 51.63  ? 103  GLU F N     1 
ATOM   26618 C  CA    . GLU F 6  103  ? 182.725 83.250  114.675 1.00 51.69  ? 103  GLU F CA    1 
ATOM   26619 C  C     . GLU F 6  103  ? 182.673 81.840  114.101 1.00 53.49  ? 103  GLU F C     1 
ATOM   26620 O  O     . GLU F 6  103  ? 183.693 81.296  113.668 1.00 51.99  ? 103  GLU F O     1 
ATOM   26621 C  CB    . GLU F 6  103  ? 182.491 84.269  113.551 1.00 50.62  ? 103  GLU F CB    1 
ATOM   26622 C  CG    . GLU F 6  103  ? 182.455 85.715  114.007 1.00 51.56  ? 103  GLU F CG    1 
ATOM   26623 C  CD    . GLU F 6  103  ? 181.166 86.399  113.616 1.00 52.25  ? 103  GLU F CD    1 
ATOM   26624 O  OE1   . GLU F 6  103  ? 180.746 86.259  112.448 1.00 51.07  ? 103  GLU F OE1   1 
ATOM   26625 O  OE2   . GLU F 6  103  ? 180.569 87.076  114.479 1.00 52.65  ? 103  GLU F OE2   1 
ATOM   26626 N  N     . SER F 6  104  ? 181.476 81.259  114.083 1.00 49.68  ? 104  SER F N     1 
ATOM   26627 C  CA    . SER F 6  104  ? 181.296 79.932  113.506 1.00 48.88  ? 104  SER F CA    1 
ATOM   26628 C  C     . SER F 6  104  ? 181.271 79.985  111.973 1.00 48.57  ? 104  SER F C     1 
ATOM   26629 O  O     . SER F 6  104  ? 181.036 81.035  111.369 1.00 46.71  ? 104  SER F O     1 
ATOM   26630 C  CB    . SER F 6  104  ? 180.013 79.302  114.036 1.00 47.97  ? 104  SER F CB    1 
ATOM   26631 O  OG    . SER F 6  104  ? 179.790 78.050  113.419 1.00 48.98  ? 104  SER F OG    1 
ATOM   26632 N  N     . LEU F 6  105  ? 181.545 78.836  111.345 1.00 46.88  ? 105  LEU F N     1 
ATOM   26633 C  CA    . LEU F 6  105  ? 181.650 78.728  109.893 1.00 47.82  ? 105  LEU F CA    1 
ATOM   26634 C  C     . LEU F 6  105  ? 180.592 77.799  109.309 1.00 49.82  ? 105  LEU F C     1 
ATOM   26635 O  O     . LEU F 6  105  ? 179.841 78.189  108.413 1.00 49.13  ? 105  LEU F O     1 
ATOM   26636 C  CB    . LEU F 6  105  ? 183.048 78.235  109.477 1.00 45.81  ? 105  LEU F CB    1 
ATOM   26637 C  CG    . LEU F 6  105  ? 184.253 79.163  109.567 1.00 46.66  ? 105  LEU F CG    1 
ATOM   26638 C  CD1   . LEU F 6  105  ? 184.952 78.919  110.895 1.00 46.16  ? 105  LEU F CD1   1 
ATOM   26639 C  CD2   . LEU F 6  105  ? 185.183 78.946  108.388 1.00 45.77  ? 105  LEU F CD2   1 
ATOM   26640 N  N     . LEU F 6  106  ? 180.515 76.568  109.816 1.00 46.08  ? 106  LEU F N     1 
ATOM   26641 C  CA    . LEU F 6  106  ? 179.800 75.496  109.132 1.00 46.21  ? 106  LEU F CA    1 
ATOM   26642 C  C     . LEU F 6  106  ? 178.329 75.417  109.548 1.00 47.90  ? 106  LEU F C     1 
ATOM   26643 O  O     . LEU F 6  106  ? 177.482 74.970  108.767 1.00 46.50  ? 106  LEU F O     1 
ATOM   26644 C  CB    . LEU F 6  106  ? 180.574 74.198  109.351 1.00 46.02  ? 106  LEU F CB    1 
ATOM   26645 C  CG    . LEU F 6  106  ? 181.040 73.787  110.753 1.00 47.51  ? 106  LEU F CG    1 
ATOM   26646 C  CD1   . LEU F 6  106  ? 179.942 73.661  111.833 1.00 43.91  ? 106  LEU F CD1   1 
ATOM   26647 C  CD2   . LEU F 6  106  ? 181.910 72.575  110.592 1.00 46.32  ? 106  LEU F CD2   1 
ATOM   26648 N  N     . THR F 6  107  ? 178.002 75.845  110.764 1.00 48.53  ? 107  THR F N     1 
ATOM   26649 C  CA    . THR F 6  107  ? 176.604 75.985  111.160 1.00 49.56  ? 107  THR F CA    1 
ATOM   26650 C  C     . THR F 6  107  ? 176.080 77.397  110.874 1.00 49.41  ? 107  THR F C     1 
ATOM   26651 O  O     . THR F 6  107  ? 176.635 78.151  110.070 1.00 48.64  ? 107  THR F O     1 
ATOM   26652 C  CB    . THR F 6  107  ? 176.413 75.597  112.629 1.00 49.89  ? 107  THR F CB    1 
ATOM   26653 O  OG1   . THR F 6  107  ? 177.272 76.389  113.468 1.00 51.53  ? 107  THR F OG1   1 
ATOM   26654 C  CG2   . THR F 6  107  ? 176.637 74.095  112.839 1.00 47.50  ? 107  THR F CG2   1 
ATOM   26655 N  N     . GLU F 6  108  ? 174.960 77.753  111.508 1.00 49.62  ? 108  GLU F N     1 
ATOM   26656 C  CA    . GLU F 6  108  ? 174.375 79.071  111.319 1.00 50.02  ? 108  GLU F CA    1 
ATOM   26657 C  C     . GLU F 6  108  ? 175.239 80.141  111.986 1.00 51.04  ? 108  GLU F C     1 
ATOM   26658 O  O     . GLU F 6  108  ? 176.096 79.832  112.816 1.00 50.08  ? 108  GLU F O     1 
ATOM   26659 C  CB    . GLU F 6  108  ? 172.943 79.117  111.856 1.00 49.66  ? 108  GLU F CB    1 
ATOM   26660 C  CG    . GLU F 6  108  ? 171.942 78.367  110.992 1.00 50.91  ? 108  GLU F CG    1 
ATOM   26661 C  CD    . GLU F 6  108  ? 172.276 76.894  110.850 1.00 52.67  ? 108  GLU F CD    1 
ATOM   26662 O  OE1   . GLU F 6  108  ? 172.216 76.172  111.870 1.00 53.51  ? 108  GLU F OE1   1 
ATOM   26663 O  OE2   . GLU F 6  108  ? 172.616 76.453  109.730 1.00 52.18  ? 108  GLU F OE2   1 
ATOM   26664 N  N     . PRO F 6  109  ? 175.079 81.406  111.580 1.00 51.04  ? 109  PRO F N     1 
ATOM   26665 C  CA    . PRO F 6  109  ? 175.891 82.476  112.171 1.00 52.19  ? 109  PRO F CA    1 
ATOM   26666 C  C     . PRO F 6  109  ? 175.751 82.561  113.681 1.00 50.71  ? 109  PRO F C     1 
ATOM   26667 O  O     . PRO F 6  109  ? 174.692 82.924  114.204 1.00 49.07  ? 109  PRO F O     1 
ATOM   26668 C  CB    . PRO F 6  109  ? 175.361 83.746  111.486 1.00 50.41  ? 109  PRO F CB    1 
ATOM   26669 C  CG    . PRO F 6  109  ? 174.187 83.313  110.665 1.00 50.34  ? 109  PRO F CG    1 
ATOM   26670 C  CD    . PRO F 6  109  ? 174.347 81.872  110.395 1.00 50.57  ? 109  PRO F CD    1 
ATOM   26671 N  N     . VAL F 6  110  ? 176.828 82.215  114.383 1.00 48.35  ? 110  VAL F N     1 
ATOM   26672 C  CA    . VAL F 6  110  ? 176.928 82.333  115.834 1.00 48.19  ? 110  VAL F CA    1 
ATOM   26673 C  C     . VAL F 6  110  ? 178.273 82.957  116.171 1.00 50.81  ? 110  VAL F C     1 
ATOM   26674 O  O     . VAL F 6  110  ? 179.301 82.595  115.590 1.00 51.65  ? 110  VAL F O     1 
ATOM   26675 C  CB    . VAL F 6  110  ? 176.782 80.973  116.547 1.00 48.31  ? 110  VAL F CB    1 
ATOM   26676 C  CG1   . VAL F 6  110  ? 176.484 81.181  118.017 1.00 45.13  ? 110  VAL F CG1   1 
ATOM   26677 C  CG2   . VAL F 6  110  ? 175.683 80.131  115.902 1.00 48.01  ? 110  VAL F CG2   1 
ATOM   26678 N  N     . THR F 6  111  ? 178.265 83.898  117.107 1.00 49.12  ? 111  THR F N     1 
ATOM   26679 C  CA    . THR F 6  111  ? 179.483 84.530  117.593 1.00 47.09  ? 111  THR F CA    1 
ATOM   26680 C  C     . THR F 6  111  ? 179.770 84.030  119.002 1.00 46.49  ? 111  THR F C     1 
ATOM   26681 O  O     . THR F 6  111  ? 178.896 84.082  119.874 1.00 43.84  ? 111  THR F O     1 
ATOM   26682 C  CB    . THR F 6  111  ? 179.353 86.052  117.582 1.00 47.54  ? 111  THR F CB    1 
ATOM   26683 O  OG1   . THR F 6  111  ? 179.145 86.501  116.239 1.00 49.62  ? 111  THR F OG1   1 
ATOM   26684 C  CG2   . THR F 6  111  ? 180.618 86.688  118.111 1.00 46.11  ? 111  THR F CG2   1 
ATOM   26685 N  N     . ILE F 6  112  ? 180.985 83.535  119.217 1.00 49.76  ? 112  ILE F N     1 
ATOM   26686 C  CA    . ILE F 6  112  ? 181.378 82.935  120.488 1.00 50.70  ? 112  ILE F CA    1 
ATOM   26687 C  C     . ILE F 6  112  ? 182.503 83.766  121.085 1.00 49.91  ? 112  ILE F C     1 
ATOM   26688 O  O     . ILE F 6  112  ? 183.549 83.949  120.452 1.00 50.78  ? 112  ILE F O     1 
ATOM   26689 C  CB    . ILE F 6  112  ? 181.806 81.469  120.320 1.00 50.20  ? 112  ILE F CB    1 
ATOM   26690 C  CG1   . ILE F 6  112  ? 180.676 80.659  119.688 1.00 47.96  ? 112  ILE F CG1   1 
ATOM   26691 C  CG2   . ILE F 6  112  ? 182.197 80.874  121.659 1.00 48.38  ? 112  ILE F CG2   1 
ATOM   26692 C  CD1   . ILE F 6  112  ? 181.004 79.199  119.500 1.00 47.28  ? 112  ILE F CD1   1 
ATOM   26693 N  N     . VAL F 6  113  ? 182.291 84.260  122.300 1.00 46.37  ? 113  VAL F N     1 
ATOM   26694 C  CA    . VAL F 6  113  ? 183.282 85.055  123.015 1.00 48.92  ? 113  VAL F CA    1 
ATOM   26695 C  C     . VAL F 6  113  ? 183.777 84.217  124.185 1.00 49.01  ? 113  VAL F C     1 
ATOM   26696 O  O     . VAL F 6  113  ? 183.037 83.964  125.143 1.00 45.66  ? 113  VAL F O     1 
ATOM   26697 C  CB    . VAL F 6  113  ? 182.712 86.397  123.491 1.00 50.60  ? 113  VAL F CB    1 
ATOM   26698 C  CG1   . VAL F 6  113  ? 183.760 87.161  124.285 1.00 48.57  ? 113  VAL F CG1   1 
ATOM   26699 C  CG2   . VAL F 6  113  ? 182.236 87.222  122.302 1.00 47.99  ? 113  VAL F CG2   1 
ATOM   26700 N  N     . ILE F 6  114  ? 185.031 83.786  124.106 1.00 49.61  ? 114  ILE F N     1 
ATOM   26701 C  CA    . ILE F 6  114  ? 185.633 82.927  125.120 1.00 50.35  ? 114  ILE F CA    1 
ATOM   26702 C  C     . ILE F 6  114  ? 186.250 83.824  126.190 1.00 50.54  ? 114  ILE F C     1 
ATOM   26703 O  O     . ILE F 6  114  ? 187.068 84.693  125.850 1.00 49.33  ? 114  ILE F O     1 
ATOM   26704 C  CB    . ILE F 6  114  ? 186.688 81.999  124.509 1.00 47.76  ? 114  ILE F CB    1 
ATOM   26705 C  CG1   . ILE F 6  114  ? 186.091 81.243  123.323 1.00 48.76  ? 114  ILE F CG1   1 
ATOM   26706 C  CG2   . ILE F 6  114  ? 187.224 81.039  125.562 1.00 45.99  ? 114  ILE F CG2   1 
ATOM   26707 C  CD1   . ILE F 6  114  ? 187.118 80.604  122.422 1.00 47.32  ? 114  ILE F CD1   1 
ATOM   26708 N  N     . PRO F 6  115  ? 185.890 83.661  127.463 1.00 49.97  ? 115  PRO F N     1 
ATOM   26709 C  CA    . PRO F 6  115  ? 186.505 84.486  128.511 1.00 49.20  ? 115  PRO F CA    1 
ATOM   26710 C  C     . PRO F 6  115  ? 188.012 84.292  128.526 1.00 48.19  ? 115  PRO F C     1 
ATOM   26711 O  O     . PRO F 6  115  ? 188.510 83.192  128.768 1.00 47.32  ? 115  PRO F O     1 
ATOM   26712 C  CB    . PRO F 6  115  ? 185.858 83.969  129.802 1.00 48.05  ? 115  PRO F CB    1 
ATOM   26713 C  CG    . PRO F 6  115  ? 184.621 83.252  129.361 1.00 48.14  ? 115  PRO F CG    1 
ATOM   26714 C  CD    . PRO F 6  115  ? 184.933 82.687  128.012 1.00 47.52  ? 115  PRO F CD    1 
ATOM   26715 N  N     . SER F 6  116  ? 188.738 85.376  128.269 1.00 48.28  ? 116  SER F N     1 
ATOM   26716 C  CA    . SER F 6  116  ? 190.190 85.306  128.182 1.00 50.05  ? 116  SER F CA    1 
ATOM   26717 C  C     . SER F 6  116  ? 190.770 84.999  129.557 1.00 49.98  ? 116  SER F C     1 
ATOM   26718 O  O     . SER F 6  116  ? 190.696 85.827  130.471 1.00 50.35  ? 116  SER F O     1 
ATOM   26719 C  CB    . SER F 6  116  ? 190.756 86.612  127.631 1.00 48.70  ? 116  SER F CB    1 
ATOM   26720 O  OG    . SER F 6  116  ? 192.148 86.706  127.876 1.00 50.67  ? 116  SER F OG    1 
ATOM   26721 N  N     . SER F 6  117  ? 191.331 83.807  129.704 1.00 48.06  ? 117  SER F N     1 
ATOM   26722 C  CA    . SER F 6  117  ? 192.015 83.414  130.923 1.00 48.86  ? 117  SER F CA    1 
ATOM   26723 C  C     . SER F 6  117  ? 193.520 83.477  130.711 1.00 50.21  ? 117  SER F C     1 
ATOM   26724 O  O     . SER F 6  117  ? 194.010 83.843  129.639 1.00 47.15  ? 117  SER F O     1 
ATOM   26725 C  CB    . SER F 6  117  ? 191.608 82.005  131.363 1.00 48.99  ? 117  SER F CB    1 
ATOM   26726 O  OG    . SER F 6  117  ? 192.397 81.017  130.725 1.00 45.78  ? 117  SER F OG    1 
ATOM   26727 N  N     . GLU F 6  118  ? 194.253 83.120  131.764 1.00 55.86  ? 118  GLU F N     1 
ATOM   26728 C  CA    . GLU F 6  118  ? 195.706 83.181  131.712 1.00 55.18  ? 118  GLU F CA    1 
ATOM   26729 C  C     . GLU F 6  118  ? 196.306 81.977  130.995 1.00 55.40  ? 118  GLU F C     1 
ATOM   26730 O  O     . GLU F 6  118  ? 197.478 82.021  130.605 1.00 55.98  ? 118  GLU F O     1 
ATOM   26731 C  CB    . GLU F 6  118  ? 196.249 83.310  133.136 1.00 53.84  ? 118  GLU F CB    1 
ATOM   26732 C  CG    . GLU F 6  118  ? 196.338 84.750  133.623 1.00 53.63  ? 118  GLU F CG    1 
ATOM   26733 C  CD    . GLU F 6  118  ? 196.869 84.865  135.043 1.00 55.53  ? 118  GLU F CD    1 
ATOM   26734 O  OE1   . GLU F 6  118  ? 197.006 83.820  135.712 1.00 55.88  ? 118  GLU F OE1   1 
ATOM   26735 O  OE2   . GLU F 6  118  ? 197.129 86.000  135.498 1.00 53.82  ? 118  GLU F OE2   1 
ATOM   26736 N  N     . SER F 6  119  ? 195.535 80.908  130.805 1.00 54.03  ? 119  SER F N     1 
ATOM   26737 C  CA    . SER F 6  119  ? 196.002 79.736  130.073 1.00 55.30  ? 119  SER F CA    1 
ATOM   26738 C  C     . SER F 6  119  ? 195.512 79.699  128.632 1.00 55.88  ? 119  SER F C     1 
ATOM   26739 O  O     . SER F 6  119  ? 195.898 78.794  127.886 1.00 55.82  ? 119  SER F O     1 
ATOM   26740 C  CB    . SER F 6  119  ? 195.567 78.448  130.791 1.00 53.43  ? 119  SER F CB    1 
ATOM   26741 O  OG    . SER F 6  119  ? 194.157 78.307  130.807 1.00 53.23  ? 119  SER F OG    1 
ATOM   26742 N  N     . GLN F 6  120  ? 194.688 80.660  128.218 1.00 56.34  ? 120  GLN F N     1 
ATOM   26743 C  CA    . GLN F 6  120  ? 194.082 80.635  126.894 1.00 56.27  ? 120  GLN F CA    1 
ATOM   26744 C  C     . GLN F 6  120  ? 194.591 81.724  125.966 1.00 57.98  ? 120  GLN F C     1 
ATOM   26745 O  O     . GLN F 6  120  ? 194.683 81.490  124.759 1.00 57.06  ? 120  GLN F O     1 
ATOM   26746 C  CB    . GLN F 6  120  ? 192.558 80.762  127.005 1.00 54.88  ? 120  GLN F CB    1 
ATOM   26747 C  CG    . GLN F 6  120  ? 191.914 79.719  127.892 1.00 56.24  ? 120  GLN F CG    1 
ATOM   26748 C  CD    . GLN F 6  120  ? 190.503 80.101  128.286 1.00 58.02  ? 120  GLN F CD    1 
ATOM   26749 O  OE1   . GLN F 6  120  ? 189.987 81.129  127.848 1.00 58.86  ? 120  GLN F OE1   1 
ATOM   26750 N  NE2   . GLN F 6  120  ? 189.880 79.290  129.135 1.00 55.89  ? 120  GLN F NE2   1 
ATOM   26751 N  N     . ASN F 6  121  ? 194.918 82.908  126.494 1.00 55.99  ? 121  ASN F N     1 
ATOM   26752 C  CA    . ASN F 6  121  ? 195.460 83.968  125.650 1.00 56.34  ? 121  ASN F CA    1 
ATOM   26753 C  C     . ASN F 6  121  ? 196.828 83.612  125.085 1.00 56.82  ? 121  ASN F C     1 
ATOM   26754 O  O     . ASN F 6  121  ? 197.263 84.234  124.110 1.00 55.15  ? 121  ASN F O     1 
ATOM   26755 C  CB    . ASN F 6  121  ? 195.546 85.282  126.431 1.00 56.03  ? 121  ASN F CB    1 
ATOM   26756 C  CG    . ASN F 6  121  ? 194.420 86.241  126.088 1.00 57.63  ? 121  ASN F CG    1 
ATOM   26757 O  OD1   . ASN F 6  121  ? 193.708 86.053  125.102 1.00 58.06  ? 121  ASN F OD1   1 
ATOM   26758 N  ND2   . ASN F 6  121  ? 194.253 87.276  126.906 1.00 54.86  ? 121  ASN F ND2   1 
ATOM   26759 N  N     . ASN F 6  122  ? 197.508 82.627  125.670 1.00 56.92  ? 122  ASN F N     1 
ATOM   26760 C  CA    . ASN F 6  122  ? 198.822 82.193  125.216 1.00 58.65  ? 122  ASN F CA    1 
ATOM   26761 C  C     . ASN F 6  122  ? 198.754 81.062  124.196 1.00 57.45  ? 122  ASN F C     1 
ATOM   26762 O  O     . ASN F 6  122  ? 199.793 80.672  123.653 1.00 57.96  ? 122  ASN F O     1 
ATOM   26763 C  CB    . ASN F 6  122  ? 199.666 81.747  126.413 1.00 57.43  ? 122  ASN F CB    1 
ATOM   26764 C  CG    . ASN F 6  122  ? 199.565 82.702  127.583 1.00 58.01  ? 122  ASN F CG    1 
ATOM   26765 O  OD1   . ASN F 6  122  ? 199.458 83.915  127.400 1.00 58.04  ? 122  ASN F OD1   1 
ATOM   26766 N  ND2   . ASN F 6  122  ? 199.594 82.160  128.796 1.00 55.71  ? 122  ASN F ND2   1 
ATOM   26767 N  N     . VAL F 6  123  ? 197.564 80.536  123.915 1.00 51.33  ? 123  VAL F N     1 
ATOM   26768 C  CA    . VAL F 6  123  ? 197.434 79.352  123.072 1.00 52.18  ? 123  VAL F CA    1 
ATOM   26769 C  C     . VAL F 6  123  ? 196.680 79.691  121.794 1.00 50.15  ? 123  VAL F C     1 
ATOM   26770 O  O     . VAL F 6  123  ? 197.220 79.558  120.691 1.00 48.25  ? 123  VAL F O     1 
ATOM   26771 C  CB    . VAL F 6  123  ? 196.741 78.207  123.833 1.00 51.70  ? 123  VAL F CB    1 
ATOM   26772 C  CG1   . VAL F 6  123  ? 196.310 77.125  122.870 1.00 48.83  ? 123  VAL F CG1   1 
ATOM   26773 C  CG2   . VAL F 6  123  ? 197.676 77.634  124.891 1.00 47.42  ? 123  VAL F CG2   1 
ATOM   26774 N  N     . ALA F 6  124  ? 195.434 80.131  121.930 1.00 49.26  ? 124  ALA F N     1 
ATOM   26775 C  CA    . ALA F 6  124  ? 194.639 80.472  120.760 1.00 51.09  ? 124  ALA F CA    1 
ATOM   26776 C  C     . ALA F 6  124  ? 195.125 81.778  120.145 1.00 51.58  ? 124  ALA F C     1 
ATOM   26777 O  O     . ALA F 6  124  ? 195.311 82.779  120.839 1.00 50.99  ? 124  ALA F O     1 
ATOM   26778 C  CB    . ALA F 6  124  ? 193.161 80.584  121.135 1.00 48.26  ? 124  ALA F CB    1 
ATOM   26779 N  N     . GLU F 6  125  ? 195.326 81.763  118.829 1.00 53.59  ? 125  GLU F N     1 
ATOM   26780 C  CA    . GLU F 6  125  ? 195.763 82.931  118.081 1.00 52.52  ? 125  GLU F CA    1 
ATOM   26781 C  C     . GLU F 6  125  ? 194.832 83.143  116.893 1.00 51.45  ? 125  GLU F C     1 
ATOM   26782 O  O     . GLU F 6  125  ? 194.003 82.291  116.563 1.00 53.03  ? 125  GLU F O     1 
ATOM   26783 C  CB    . GLU F 6  125  ? 197.216 82.789  117.603 1.00 52.64  ? 125  GLU F CB    1 
ATOM   26784 C  CG    . GLU F 6  125  ? 198.195 82.297  118.666 1.00 51.72  ? 125  GLU F CG    1 
ATOM   26785 C  CD    . GLU F 6  125  ? 199.345 81.492  118.076 1.00 55.50  ? 125  GLU F CD    1 
ATOM   26786 O  OE1   . GLU F 6  125  ? 199.284 81.148  116.875 1.00 56.31  ? 125  GLU F OE1   1 
ATOM   26787 O  OE2   . GLU F 6  125  ? 200.307 81.196  118.815 1.00 55.55  ? 125  GLU F OE2   1 
ATOM   26788 N  N     . VAL F 6  126  ? 194.976 84.302  116.251 1.00 47.26  ? 126  VAL F N     1 
ATOM   26789 C  CA    . VAL F 6  126  ? 194.117 84.662  115.130 1.00 47.73  ? 126  VAL F CA    1 
ATOM   26790 C  C     . VAL F 6  126  ? 194.407 83.752  113.942 1.00 47.77  ? 126  VAL F C     1 
ATOM   26791 O  O     . VAL F 6  126  ? 195.566 83.432  113.648 1.00 45.93  ? 126  VAL F O     1 
ATOM   26792 C  CB    . VAL F 6  126  ? 194.305 86.145  114.772 1.00 44.84  ? 126  VAL F CB    1 
ATOM   26793 C  CG1   . VAL F 6  126  ? 195.784 86.496  114.717 1.00 43.45  ? 126  VAL F CG1   1 
ATOM   26794 C  CG2   . VAL F 6  126  ? 193.621 86.477  113.459 1.00 41.97  ? 126  VAL F CG2   1 
ATOM   26795 N  N     . GLY F 6  127  ? 193.344 83.312  113.266 1.00 46.86  ? 127  GLY F N     1 
ATOM   26796 C  CA    . GLY F 6  127  ? 193.433 82.454  112.101 1.00 44.41  ? 127  GLY F CA    1 
ATOM   26797 C  C     . GLY F 6  127  ? 193.167 80.991  112.376 1.00 45.47  ? 127  GLY F C     1 
ATOM   26798 O  O     . GLY F 6  127  ? 193.007 80.220  111.423 1.00 44.86  ? 127  GLY F O     1 
ATOM   26799 N  N     . GLN F 6  128  ? 193.090 80.586  113.639 1.00 52.65  ? 128  GLN F N     1 
ATOM   26800 C  CA    . GLN F 6  128  ? 193.005 79.179  113.999 1.00 53.18  ? 128  GLN F CA    1 
ATOM   26801 C  C     . GLN F 6  128  ? 191.558 78.699  114.016 1.00 54.45  ? 128  GLN F C     1 
ATOM   26802 O  O     . GLN F 6  128  ? 190.617 79.496  114.065 1.00 52.84  ? 128  GLN F O     1 
ATOM   26803 C  CB    . GLN F 6  128  ? 193.649 78.942  115.364 1.00 51.04  ? 128  GLN F CB    1 
ATOM   26804 C  CG    . GLN F 6  128  ? 195.156 79.079  115.354 1.00 51.22  ? 128  GLN F CG    1 
ATOM   26805 C  CD    . GLN F 6  128  ? 195.692 79.558  116.684 1.00 54.89  ? 128  GLN F CD    1 
ATOM   26806 O  OE1   . GLN F 6  128  ? 194.926 79.837  117.606 1.00 53.92  ? 128  GLN F OE1   1 
ATOM   26807 N  NE2   . GLN F 6  128  ? 197.010 79.677  116.787 1.00 51.53  ? 128  GLN F NE2   1 
ATOM   26808 N  N     . ILE F 6  129  ? 191.391 77.379  113.962 1.00 50.58  ? 129  ILE F N     1 
ATOM   26809 C  CA    . ILE F 6  129  ? 190.083 76.732  113.965 1.00 48.65  ? 129  ILE F CA    1 
ATOM   26810 C  C     . ILE F 6  129  ? 190.095 75.657  115.044 1.00 50.05  ? 129  ILE F C     1 
ATOM   26811 O  O     . ILE F 6  129  ? 190.909 74.727  114.989 1.00 53.21  ? 129  ILE F O     1 
ATOM   26812 C  CB    . ILE F 6  129  ? 189.745 76.133  112.591 1.00 50.12  ? 129  ILE F CB    1 
ATOM   26813 C  CG1   . ILE F 6  129  ? 189.669 77.242  111.537 1.00 49.62  ? 129  ILE F CG1   1 
ATOM   26814 C  CG2   . ILE F 6  129  ? 188.448 75.344  112.659 1.00 47.82  ? 129  ILE F CG2   1 
ATOM   26815 C  CD1   . ILE F 6  129  ? 189.924 76.771  110.133 1.00 48.04  ? 129  ILE F CD1   1 
ATOM   26816 N  N     . VAL F 6  130  ? 189.196 75.777  116.017 1.00 46.73  ? 130  VAL F N     1 
ATOM   26817 C  CA    . VAL F 6  130  ? 189.208 74.896  117.183 1.00 47.00  ? 130  VAL F CA    1 
ATOM   26818 C  C     . VAL F 6  130  ? 187.793 74.398  117.442 1.00 47.43  ? 130  VAL F C     1 
ATOM   26819 O  O     . VAL F 6  130  ? 186.808 75.015  117.006 1.00 47.05  ? 130  VAL F O     1 
ATOM   26820 C  CB    . VAL F 6  130  ? 189.768 75.614  118.436 1.00 47.60  ? 130  VAL F CB    1 
ATOM   26821 C  CG1   . VAL F 6  130  ? 191.098 76.288  118.129 1.00 46.14  ? 130  VAL F CG1   1 
ATOM   26822 C  CG2   . VAL F 6  130  ? 188.760 76.614  118.978 1.00 44.44  ? 130  VAL F CG2   1 
ATOM   26823 N  N     . PRO F 6  131  ? 187.656 73.270  118.137 1.00 52.06  ? 131  PRO F N     1 
ATOM   26824 C  CA    . PRO F 6  131  ? 186.341 72.856  118.635 1.00 52.10  ? 131  PRO F CA    1 
ATOM   26825 C  C     . PRO F 6  131  ? 185.991 73.522  119.957 1.00 53.44  ? 131  PRO F C     1 
ATOM   26826 O  O     . PRO F 6  131  ? 186.831 73.711  120.839 1.00 52.35  ? 131  PRO F O     1 
ATOM   26827 C  CB    . PRO F 6  131  ? 186.505 71.340  118.812 1.00 52.69  ? 131  PRO F CB    1 
ATOM   26828 C  CG    . PRO F 6  131  ? 187.944 71.167  119.128 1.00 52.59  ? 131  PRO F CG    1 
ATOM   26829 C  CD    . PRO F 6  131  ? 188.683 72.237  118.366 1.00 50.57  ? 131  PRO F CD    1 
ATOM   26830 N  N     . VAL F 6  132  ? 184.711 73.873  120.085 1.00 53.18  ? 132  VAL F N     1 
ATOM   26831 C  CA    . VAL F 6  132  ? 184.222 74.656  121.211 1.00 51.93  ? 132  VAL F CA    1 
ATOM   26832 C  C     . VAL F 6  132  ? 183.117 73.892  121.922 1.00 52.08  ? 132  VAL F C     1 
ATOM   26833 O  O     . VAL F 6  132  ? 182.317 73.189  121.297 1.00 48.67  ? 132  VAL F O     1 
ATOM   26834 C  CB    . VAL F 6  132  ? 183.706 76.043  120.771 1.00 51.75  ? 132  VAL F CB    1 
ATOM   26835 C  CG1   . VAL F 6  132  ? 183.734 77.019  121.941 1.00 50.63  ? 132  VAL F CG1   1 
ATOM   26836 C  CG2   . VAL F 6  132  ? 184.512 76.566  119.604 1.00 50.58  ? 132  VAL F CG2   1 
ATOM   26837 N  N     . GLN F 6  133  ? 183.080 74.037  123.244 1.00 53.38  ? 133  GLN F N     1 
ATOM   26838 C  CA    . GLN F 6  133  ? 182.024 73.488  124.080 1.00 50.91  ? 133  GLN F CA    1 
ATOM   26839 C  C     . GLN F 6  133  ? 181.247 74.628  124.724 1.00 51.97  ? 133  GLN F C     1 
ATOM   26840 O  O     . GLN F 6  133  ? 181.834 75.509  125.363 1.00 49.96  ? 133  GLN F O     1 
ATOM   26841 C  CB    . GLN F 6  133  ? 182.601 72.575  125.162 1.00 48.38  ? 133  GLN F CB    1 
ATOM   26842 C  CG    . GLN F 6  133  ? 181.597 71.608  125.757 1.00 51.51  ? 133  GLN F CG    1 
ATOM   26843 C  CD    . GLN F 6  133  ? 181.479 70.328  124.955 1.00 53.69  ? 133  GLN F CD    1 
ATOM   26844 O  OE1   . GLN F 6  133  ? 181.736 70.308  123.752 1.00 50.84  ? 133  GLN F OE1   1 
ATOM   26845 N  NE2   . GLN F 6  133  ? 181.099 69.247  125.623 1.00 52.34  ? 133  GLN F NE2   1 
ATOM   26846 N  N     . LEU F 6  134  ? 179.926 74.608  124.558 1.00 49.60  ? 134  LEU F N     1 
ATOM   26847 C  CA    . LEU F 6  134  ? 179.081 75.693  125.029 1.00 47.28  ? 134  LEU F CA    1 
ATOM   26848 C  C     . LEU F 6  134  ? 178.738 75.483  126.503 1.00 47.84  ? 134  LEU F C     1 
ATOM   26849 O  O     . LEU F 6  134  ? 179.196 74.532  127.141 1.00 48.77  ? 134  LEU F O     1 
ATOM   26850 C  CB    . LEU F 6  134  ? 177.832 75.803  124.159 1.00 46.67  ? 134  LEU F CB    1 
ATOM   26851 C  CG    . LEU F 6  134  ? 178.057 76.139  122.683 1.00 44.86  ? 134  LEU F CG    1 
ATOM   26852 C  CD1   . LEU F 6  134  ? 176.785 76.683  122.077 1.00 45.89  ? 134  LEU F CD1   1 
ATOM   26853 C  CD2   . LEU F 6  134  ? 179.192 77.130  122.514 1.00 44.01  ? 134  LEU F CD2   1 
ATOM   26854 N  N     . ALA F 6  135  ? 177.916 76.373  127.058 1.00 48.30  ? 135  ALA F N     1 
ATOM   26855 C  CA    . ALA F 6  135  ? 177.583 76.353  128.473 1.00 47.18  ? 135  ALA F CA    1 
ATOM   26856 C  C     . ALA F 6  135  ? 176.077 76.544  128.636 1.00 49.59  ? 135  ALA F C     1 
ATOM   26857 O  O     . ALA F 6  135  ? 175.318 76.541  127.661 1.00 47.24  ? 135  ALA F O     1 
ATOM   26858 C  CB    . ALA F 6  135  ? 178.373 77.419  129.238 1.00 44.24  ? 135  ALA F CB    1 
ATOM   26859 N  N     . ASN F 6  136  ? 175.647 76.722  129.885 1.00 52.07  ? 136  ASN F N     1 
ATOM   26860 C  CA    . ASN F 6  136  ? 174.229 76.698  130.223 1.00 52.54  ? 136  ASN F CA    1 
ATOM   26861 C  C     . ASN F 6  136  ? 173.579 78.043  129.931 1.00 52.29  ? 136  ASN F C     1 
ATOM   26862 O  O     . ASN F 6  136  ? 174.014 79.076  130.454 1.00 49.89  ? 136  ASN F O     1 
ATOM   26863 C  CB    . ASN F 6  136  ? 174.038 76.329  131.694 1.00 51.37  ? 136  ASN F CB    1 
ATOM   26864 C  CG    . ASN F 6  136  ? 172.620 75.882  132.004 1.00 53.65  ? 136  ASN F CG    1 
ATOM   26865 O  OD1   . ASN F 6  136  ? 171.650 76.464  131.520 1.00 52.32  ? 136  ASN F OD1   1 
ATOM   26866 N  ND2   . ASN F 6  136  ? 172.496 74.843  132.818 1.00 54.28  ? 136  ASN F ND2   1 
ATOM   26867 N  N     . SER F 6  137  ? 172.529 78.018  129.106 1.00 47.33  ? 137  SER F N     1 
ATOM   26868 C  CA    . SER F 6  137  ? 171.645 79.160  128.856 1.00 45.22  ? 137  SER F CA    1 
ATOM   26869 C  C     . SER F 6  137  ? 172.420 80.439  128.571 1.00 44.27  ? 137  SER F C     1 
ATOM   26870 O  O     . SER F 6  137  ? 172.020 81.524  129.000 1.00 43.71  ? 137  SER F O     1 
ATOM   26871 C  CB    . SER F 6  137  ? 170.674 79.372  130.022 1.00 44.43  ? 137  SER F CB    1 
ATOM   26872 O  OG    . SER F 6  137  ? 171.353 79.774  131.200 1.00 44.34  ? 137  SER F OG    1 
ATOM   26873 N  N     . SER F 6  138  ? 173.538 80.323  127.861 1.00 45.22  ? 138  SER F N     1 
ATOM   26874 C  CA    . SER F 6  138  ? 174.414 81.447  127.577 1.00 47.75  ? 138  SER F CA    1 
ATOM   26875 C  C     . SER F 6  138  ? 174.326 81.903  126.128 1.00 49.52  ? 138  SER F C     1 
ATOM   26876 O  O     . SER F 6  138  ? 175.176 82.680  125.682 1.00 47.26  ? 138  SER F O     1 
ATOM   26877 C  CB    . SER F 6  138  ? 175.857 81.080  127.920 1.00 48.44  ? 138  SER F CB    1 
ATOM   26878 O  OG    . SER F 6  138  ? 176.194 79.816  127.372 1.00 47.48  ? 138  SER F OG    1 
ATOM   26879 N  N     . VAL F 6  139  ? 173.314 81.448  125.394 1.00 45.96  ? 139  VAL F N     1 
ATOM   26880 C  CA    . VAL F 6  139  ? 173.266 81.599  123.944 1.00 44.28  ? 139  VAL F CA    1 
ATOM   26881 C  C     . VAL F 6  139  ? 172.223 82.649  123.564 1.00 45.39  ? 139  VAL F C     1 
ATOM   26882 O  O     . VAL F 6  139  ? 171.659 82.615  122.465 1.00 49.13  ? 139  VAL F O     1 
ATOM   26883 C  CB    . VAL F 6  139  ? 173.003 80.226  123.286 1.00 44.24  ? 139  VAL F CB    1 
ATOM   26884 C  CG1   . VAL F 6  139  ? 171.553 79.785  123.467 1.00 42.91  ? 139  VAL F CG1   1 
ATOM   26885 C  CG2   . VAL F 6  139  ? 173.425 80.220  121.817 1.00 45.23  ? 139  VAL F CG2   1 
ATOM   26886 N  N     . TYR F 6  140  ? 171.996 83.609  124.461 1.00 47.08  ? 140  TYR F N     1 
ATOM   26887 C  CA    . TYR F 6  140  ? 170.925 84.597  124.354 1.00 49.89  ? 140  TYR F CA    1 
ATOM   26888 C  C     . TYR F 6  140  ? 170.751 85.123  122.937 1.00 49.65  ? 140  TYR F C     1 
ATOM   26889 O  O     . TYR F 6  140  ? 171.706 85.589  122.308 1.00 47.72  ? 140  TYR F O     1 
ATOM   26890 C  CB    . TYR F 6  140  ? 171.195 85.765  125.309 1.00 47.28  ? 140  TYR F CB    1 
ATOM   26891 C  CG    . TYR F 6  140  ? 171.832 85.365  126.619 1.00 49.42  ? 140  TYR F CG    1 
ATOM   26892 C  CD1   . TYR F 6  140  ? 173.214 85.348  126.771 1.00 49.22  ? 140  TYR F CD1   1 
ATOM   26893 C  CD2   . TYR F 6  140  ? 171.051 85.002  127.703 1.00 47.96  ? 140  TYR F CD2   1 
ATOM   26894 C  CE1   . TYR F 6  140  ? 173.797 84.980  127.971 1.00 47.56  ? 140  TYR F CE1   1 
ATOM   26895 C  CE2   . TYR F 6  140  ? 171.624 84.636  128.904 1.00 48.88  ? 140  TYR F CE2   1 
ATOM   26896 C  CZ    . TYR F 6  140  ? 172.996 84.624  129.033 1.00 50.09  ? 140  TYR F CZ    1 
ATOM   26897 O  OH    . TYR F 6  140  ? 173.561 84.254  130.231 1.00 49.26  ? 140  TYR F OH    1 
ATOM   26898 N  N     . TYR F 6  141  ? 169.518 85.043  122.437 1.00 50.35  ? 141  TYR F N     1 
ATOM   26899 C  CA    . TYR F 6  141  ? 169.177 85.481  121.086 1.00 50.43  ? 141  TYR F CA    1 
ATOM   26900 C  C     . TYR F 6  141  ? 168.560 86.871  121.180 1.00 51.13  ? 141  TYR F C     1 
ATOM   26901 O  O     . TYR F 6  141  ? 167.342 87.041  121.230 1.00 51.36  ? 141  TYR F O     1 
ATOM   26902 C  CB    . TYR F 6  141  ? 168.224 84.489  120.432 1.00 49.28  ? 141  TYR F CB    1 
ATOM   26903 C  CG    . TYR F 6  141  ? 168.826 83.131  120.207 1.00 49.06  ? 141  TYR F CG    1 
ATOM   26904 C  CD1   . TYR F 6  141  ? 168.856 82.195  121.226 1.00 49.96  ? 141  TYR F CD1   1 
ATOM   26905 C  CD2   . TYR F 6  141  ? 169.344 82.773  118.973 1.00 49.24  ? 141  TYR F CD2   1 
ATOM   26906 C  CE1   . TYR F 6  141  ? 169.401 80.951  121.031 1.00 51.16  ? 141  TYR F CE1   1 
ATOM   26907 C  CE2   . TYR F 6  141  ? 169.888 81.524  118.767 1.00 49.91  ? 141  TYR F CE2   1 
ATOM   26908 C  CZ    . TYR F 6  141  ? 169.915 80.617  119.801 1.00 51.05  ? 141  TYR F CZ    1 
ATOM   26909 O  OH    . TYR F 6  141  ? 170.453 79.367  119.613 1.00 49.47  ? 141  TYR F OH    1 
ATOM   26910 N  N     . ILE F 6  142  ? 169.426 87.879  121.202 1.00 48.75  ? 142  ILE F N     1 
ATOM   26911 C  CA    . ILE F 6  142  ? 168.993 89.271  121.284 1.00 49.95  ? 142  ILE F CA    1 
ATOM   26912 C  C     . ILE F 6  142  ? 168.224 89.598  120.011 1.00 49.78  ? 142  ILE F C     1 
ATOM   26913 O  O     . ILE F 6  142  ? 168.785 89.501  118.911 1.00 47.95  ? 142  ILE F O     1 
ATOM   26914 C  CB    . ILE F 6  142  ? 170.187 90.216  121.476 1.00 47.83  ? 142  ILE F CB    1 
ATOM   26915 C  CG1   . ILE F 6  142  ? 171.161 89.636  122.503 1.00 49.25  ? 142  ILE F CG1   1 
ATOM   26916 C  CG2   . ILE F 6  142  ? 169.718 91.597  121.906 1.00 47.53  ? 142  ILE F CG2   1 
ATOM   26917 C  CD1   . ILE F 6  142  ? 172.487 90.363  122.576 1.00 47.08  ? 142  ILE F CD1   1 
ATOM   26918 N  N     . PRO F 6  143  ? 166.949 89.969  120.104 1.00 45.81  ? 143  PRO F N     1 
ATOM   26919 C  CA    . PRO F 6  143  ? 166.164 90.195  118.886 1.00 45.65  ? 143  PRO F CA    1 
ATOM   26920 C  C     . PRO F 6  143  ? 166.716 91.360  118.081 1.00 43.12  ? 143  PRO F C     1 
ATOM   26921 O  O     . PRO F 6  143  ? 167.087 92.398  118.631 1.00 43.31  ? 143  PRO F O     1 
ATOM   26922 C  CB    . PRO F 6  143  ? 164.756 90.488  119.419 1.00 42.28  ? 143  PRO F CB    1 
ATOM   26923 C  CG    . PRO F 6  143  ? 164.746 89.931  120.802 1.00 43.07  ? 143  PRO F CG    1 
ATOM   26924 C  CD    . PRO F 6  143  ? 166.131 90.103  121.319 1.00 42.38  ? 143  PRO F CD    1 
ATOM   26925 N  N     . GLY F 6  144  ? 166.744 91.187  116.763 1.00 34.21  ? 144  GLY F N     1 
ATOM   26926 C  CA    . GLY F 6  144  ? 167.278 92.191  115.873 1.00 33.94  ? 144  GLY F CA    1 
ATOM   26927 C  C     . GLY F 6  144  ? 168.751 92.064  115.550 1.00 39.38  ? 144  GLY F C     1 
ATOM   26928 O  O     . GLY F 6  144  ? 169.284 92.919  114.833 1.00 39.15  ? 144  GLY F O     1 
ATOM   26929 N  N     . ARG F 6  145  ? 169.428 91.037  116.053 1.00 53.00  ? 145  ARG F N     1 
ATOM   26930 C  CA    . ARG F 6  145  ? 170.822 90.804  115.707 1.00 51.93  ? 145  ARG F CA    1 
ATOM   26931 C  C     . ARG F 6  145  ? 170.946 89.663  114.706 1.00 52.98  ? 145  ARG F C     1 
ATOM   26932 O  O     . ARG F 6  145  ? 170.021 88.866  114.520 1.00 50.78  ? 145  ARG F O     1 
ATOM   26933 C  CB    . ARG F 6  145  ? 171.652 90.491  116.948 1.00 47.99  ? 145  ARG F CB    1 
ATOM   26934 C  CG    . ARG F 6  145  ? 171.822 91.666  117.878 1.00 50.99  ? 145  ARG F CG    1 
ATOM   26935 C  CD    . ARG F 6  145  ? 172.688 91.280  119.049 1.00 54.17  ? 145  ARG F CD    1 
ATOM   26936 N  NE    . ARG F 6  145  ? 174.099 91.247  118.686 1.00 54.25  ? 145  ARG F NE    1 
ATOM   26937 C  CZ    . ARG F 6  145  ? 174.938 92.253  118.883 1.00 53.65  ? 145  ARG F CZ    1 
ATOM   26938 N  NH1   . ARG F 6  145  ? 174.552 93.366  119.484 1.00 51.41  ? 145  ARG F NH1   1 
ATOM   26939 N  NH2   . ARG F 6  145  ? 176.199 92.136  118.477 1.00 52.71  ? 145  ARG F NH2   1 
ATOM   26940 N  N     . GLN F 6  146  ? 172.107 89.597  114.059 1.00 48.46  ? 146  GLN F N     1 
ATOM   26941 C  CA    . GLN F 6  146  ? 172.399 88.583  113.056 1.00 48.11  ? 146  GLN F CA    1 
ATOM   26942 C  C     . GLN F 6  146  ? 173.162 87.386  113.617 1.00 49.97  ? 146  GLN F C     1 
ATOM   26943 O  O     . GLN F 6  146  ? 173.592 86.528  112.839 1.00 50.30  ? 146  GLN F O     1 
ATOM   26944 C  CB    . GLN F 6  146  ? 173.191 89.205  111.904 1.00 48.07  ? 146  GLN F CB    1 
ATOM   26945 C  CG    . GLN F 6  146  ? 172.543 90.437  111.291 1.00 46.81  ? 146  GLN F CG    1 
ATOM   26946 C  CD    . GLN F 6  146  ? 173.379 91.691  111.468 1.00 49.09  ? 146  GLN F CD    1 
ATOM   26947 O  OE1   . GLN F 6  146  ? 173.402 92.289  112.542 1.00 49.18  ? 146  GLN F OE1   1 
ATOM   26948 N  NE2   . GLN F 6  146  ? 174.071 92.094  110.412 1.00 47.43  ? 146  GLN F NE2   1 
ATOM   26949 N  N     . GLN F 6  147  ? 173.342 87.305  114.934 1.00 50.48  ? 147  GLN F N     1 
ATOM   26950 C  CA    . GLN F 6  147  ? 174.115 86.230  115.540 1.00 48.08  ? 147  GLN F CA    1 
ATOM   26951 C  C     . GLN F 6  147  ? 173.610 85.976  116.951 1.00 49.64  ? 147  GLN F C     1 
ATOM   26952 O  O     . GLN F 6  147  ? 172.834 86.757  117.504 1.00 52.07  ? 147  GLN F O     1 
ATOM   26953 C  CB    . GLN F 6  147  ? 175.614 86.551  115.557 1.00 46.97  ? 147  GLN F CB    1 
ATOM   26954 C  CG    . GLN F 6  147  ? 175.967 87.907  116.144 1.00 48.18  ? 147  GLN F CG    1 
ATOM   26955 C  CD    . GLN F 6  147  ? 175.881 89.027  115.121 1.00 51.73  ? 147  GLN F CD    1 
ATOM   26956 O  OE1   . GLN F 6  147  ? 176.580 89.012  114.107 1.00 50.99  ? 147  GLN F OE1   1 
ATOM   26957 N  NE2   . GLN F 6  147  ? 175.027 90.007  115.386 1.00 50.30  ? 147  GLN F NE2   1 
ATOM   26958 N  N     . ALA F 6  148  ? 174.047 84.857  117.522 1.00 45.95  ? 148  ALA F N     1 
ATOM   26959 C  CA    . ALA F 6  148  ? 173.674 84.458  118.875 1.00 46.42  ? 148  ALA F CA    1 
ATOM   26960 C  C     . ALA F 6  148  ? 174.884 84.641  119.783 1.00 45.22  ? 148  ALA F C     1 
ATOM   26961 O  O     . ALA F 6  148  ? 175.905 83.971  119.610 1.00 45.80  ? 148  ALA F O     1 
ATOM   26962 C  CB    . ALA F 6  148  ? 173.180 83.014  118.904 1.00 42.30  ? 148  ALA F CB    1 
ATOM   26963 N  N     . SER F 6  149  ? 174.771 85.552  120.742 1.00 44.82  ? 149  SER F N     1 
ATOM   26964 C  CA    . SER F 6  149  ? 175.863 85.791  121.672 1.00 45.29  ? 149  SER F CA    1 
ATOM   26965 C  C     . SER F 6  149  ? 175.972 84.643  122.667 1.00 44.64  ? 149  SER F C     1 
ATOM   26966 O  O     . SER F 6  149  ? 175.015 84.315  123.370 1.00 44.23  ? 149  SER F O     1 
ATOM   26967 C  CB    . SER F 6  149  ? 175.649 87.115  122.398 1.00 45.09  ? 149  SER F CB    1 
ATOM   26968 O  OG    . SER F 6  149  ? 175.035 88.058  121.536 1.00 45.05  ? 149  SER F OG    1 
ATOM   26969 N  N     . ALA F 6  150  ? 177.155 84.036  122.729 1.00 45.34  ? 150  ALA F N     1 
ATOM   26970 C  CA    . ALA F 6  150  ? 177.346 82.825  123.513 1.00 47.47  ? 150  ALA F CA    1 
ATOM   26971 C  C     . ALA F 6  150  ? 178.790 82.748  123.987 1.00 51.03  ? 150  ALA F C     1 
ATOM   26972 O  O     . ALA F 6  150  ? 179.702 83.201  123.293 1.00 48.28  ? 150  ALA F O     1 
ATOM   26973 C  CB    . ALA F 6  150  ? 176.988 81.574  122.702 1.00 44.31  ? 150  ALA F CB    1 
ATOM   26974 N  N     . THR F 6  151  ? 178.981 82.190  125.179 1.00 51.19  ? 151  THR F N     1 
ATOM   26975 C  CA    . THR F 6  151  ? 180.318 81.913  125.679 1.00 50.11  ? 151  THR F CA    1 
ATOM   26976 C  C     . THR F 6  151  ? 180.617 80.419  125.585 1.00 51.84  ? 151  THR F C     1 
ATOM   26977 O  O     . THR F 6  151  ? 179.773 79.573  125.897 1.00 51.33  ? 151  THR F O     1 
ATOM   26978 C  CB    . THR F 6  151  ? 180.464 82.396  127.124 1.00 48.68  ? 151  THR F CB    1 
ATOM   26979 O  OG1   . THR F 6  151  ? 181.748 82.018  127.634 1.00 48.46  ? 151  THR F OG1   1 
ATOM   26980 C  CG2   . THR F 6  151  ? 179.377 81.803  128.009 1.00 46.58  ? 151  THR F CG2   1 
ATOM   26981 N  N     . GLY F 6  152  ? 181.836 80.098  125.149 1.00 49.26  ? 152  GLY F N     1 
ATOM   26982 C  CA    . GLY F 6  152  ? 182.214 78.711  124.964 1.00 47.74  ? 152  GLY F CA    1 
ATOM   26983 C  C     . GLY F 6  152  ? 183.630 78.448  125.428 1.00 48.79  ? 152  GLY F C     1 
ATOM   26984 O  O     . GLY F 6  152  ? 184.448 79.361  125.559 1.00 47.68  ? 152  GLY F O     1 
ATOM   26985 N  N     . SER F 6  153  ? 183.913 77.167  125.662 1.00 49.08  ? 153  SER F N     1 
ATOM   26986 C  CA    . SER F 6  153  ? 185.205 76.723  126.167 1.00 48.87  ? 153  SER F CA    1 
ATOM   26987 C  C     . SER F 6  153  ? 185.812 75.728  125.191 1.00 49.79  ? 153  SER F C     1 
ATOM   26988 O  O     . SER F 6  153  ? 185.088 75.046  124.459 1.00 48.86  ? 153  SER F O     1 
ATOM   26989 C  CB    . SER F 6  153  ? 185.072 76.079  127.553 1.00 46.54  ? 153  SER F CB    1 
ATOM   26990 O  OG    . SER F 6  153  ? 185.097 77.055  128.580 1.00 46.44  ? 153  SER F OG    1 
ATOM   26991 N  N     . ILE F 6  154  ? 187.144 75.659  125.176 1.00 47.49  ? 154  ILE F N     1 
ATOM   26992 C  CA    . ILE F 6  154  ? 187.836 74.772  124.248 1.00 48.57  ? 154  ILE F CA    1 
ATOM   26993 C  C     . ILE F 6  154  ? 187.509 73.329  124.603 1.00 51.13  ? 154  ILE F C     1 
ATOM   26994 O  O     . ILE F 6  154  ? 187.628 72.913  125.762 1.00 49.75  ? 154  ILE F O     1 
ATOM   26995 C  CB    . ILE F 6  154  ? 189.344 75.042  124.261 1.00 48.61  ? 154  ILE F CB    1 
ATOM   26996 C  CG1   . ILE F 6  154  ? 189.627 76.502  123.893 1.00 47.33  ? 154  ILE F CG1   1 
ATOM   26997 C  CG2   . ILE F 6  154  ? 190.066 74.100  123.303 1.00 47.51  ? 154  ILE F CG2   1 
ATOM   26998 C  CD1   . ILE F 6  154  ? 190.040 77.371  125.059 1.00 47.46  ? 154  ILE F CD1   1 
ATOM   26999 N  N     . PHE F 6  155  ? 187.095 72.556  123.601 1.00 53.79  ? 155  PHE F N     1 
ATOM   27000 C  CA    . PHE F 6  155  ? 186.604 71.206  123.831 1.00 52.95  ? 155  PHE F CA    1 
ATOM   27001 C  C     . PHE F 6  155  ? 187.753 70.218  123.970 1.00 53.07  ? 155  PHE F C     1 
ATOM   27002 O  O     . PHE F 6  155  ? 188.549 70.035  123.042 1.00 53.62  ? 155  PHE F O     1 
ATOM   27003 C  CB    . PHE F 6  155  ? 185.680 70.775  122.693 1.00 51.24  ? 155  PHE F CB    1 
ATOM   27004 C  CG    . PHE F 6  155  ? 185.349 69.308  122.703 1.00 53.84  ? 155  PHE F CG    1 
ATOM   27005 C  CD1   . PHE F 6  155  ? 184.859 68.700  123.846 1.00 52.31  ? 155  PHE F CD1   1 
ATOM   27006 C  CD2   . PHE F 6  155  ? 185.508 68.541  121.562 1.00 54.60  ? 155  PHE F CD2   1 
ATOM   27007 C  CE1   . PHE F 6  155  ? 184.554 67.352  123.853 1.00 52.78  ? 155  PHE F CE1   1 
ATOM   27008 C  CE2   . PHE F 6  155  ? 185.202 67.192  121.565 1.00 52.77  ? 155  PHE F CE2   1 
ATOM   27009 C  CZ    . PHE F 6  155  ? 184.724 66.599  122.709 1.00 52.40  ? 155  PHE F CZ    1 
ATOM   27010 N  N     . ILE F 6  156  ? 187.825 69.573  125.135 1.00 49.87  ? 156  ILE F N     1 
ATOM   27011 C  CA    . ILE F 6  156  ? 188.693 68.427  125.355 1.00 50.02  ? 156  ILE F CA    1 
ATOM   27012 C  C     . ILE F 6  156  ? 187.809 67.287  125.848 1.00 49.50  ? 156  ILE F C     1 
ATOM   27013 O  O     . ILE F 6  156  ? 187.062 67.462  126.814 1.00 48.20  ? 156  ILE F O     1 
ATOM   27014 C  CB    . ILE F 6  156  ? 189.816 68.722  126.365 1.00 48.21  ? 156  ILE F CB    1 
ATOM   27015 C  CG1   . ILE F 6  156  ? 189.264 69.489  127.571 1.00 48.75  ? 156  ILE F CG1   1 
ATOM   27016 C  CG2   . ILE F 6  156  ? 190.935 69.498  125.693 1.00 46.76  ? 156  ILE F CG2   1 
ATOM   27017 C  CD1   . ILE F 6  156  ? 190.328 70.037  128.498 1.00 49.00  ? 156  ILE F CD1   1 
ATOM   27018 N  N     . PRO F 6  157  ? 187.831 66.117  125.208 1.00 53.53  ? 157  PRO F N     1 
ATOM   27019 C  CA    . PRO F 6  157  ? 186.892 65.051  125.588 1.00 53.45  ? 157  PRO F CA    1 
ATOM   27020 C  C     . PRO F 6  157  ? 187.032 64.666  127.054 1.00 54.81  ? 157  PRO F C     1 
ATOM   27021 O  O     . PRO F 6  157  ? 188.139 64.504  127.571 1.00 53.95  ? 157  PRO F O     1 
ATOM   27022 C  CB    . PRO F 6  157  ? 187.274 63.893  124.657 1.00 51.24  ? 157  PRO F CB    1 
ATOM   27023 C  CG    . PRO F 6  157  ? 187.921 64.551  123.481 1.00 50.64  ? 157  PRO F CG    1 
ATOM   27024 C  CD    . PRO F 6  157  ? 188.633 65.758  124.025 1.00 51.84  ? 157  PRO F CD    1 
ATOM   27025 N  N     . LYS F 6  158  ? 185.888 64.515  127.720 1.00 54.44  ? 158  LYS F N     1 
ATOM   27026 C  CA    . LYS F 6  158  ? 185.861 64.294  129.156 1.00 54.21  ? 158  LYS F CA    1 
ATOM   27027 C  C     . LYS F 6  158  ? 186.185 62.844  129.499 1.00 55.25  ? 158  LYS F C     1 
ATOM   27028 O  O     . LYS F 6  158  ? 186.059 61.932  128.677 1.00 56.38  ? 158  LYS F O     1 
ATOM   27029 C  CB    . LYS F 6  158  ? 184.498 64.660  129.743 1.00 53.62  ? 158  LYS F CB    1 
ATOM   27030 C  CG    . LYS F 6  158  ? 184.048 66.090  129.517 1.00 52.95  ? 158  LYS F CG    1 
ATOM   27031 C  CD    . LYS F 6  158  ? 182.639 66.271  130.061 1.00 54.16  ? 158  LYS F CD    1 
ATOM   27032 C  CE    . LYS F 6  158  ? 181.960 67.525  129.543 1.00 53.49  ? 158  LYS F CE    1 
ATOM   27033 N  NZ    . LYS F 6  158  ? 180.581 67.632  130.096 1.00 51.57  ? 158  LYS F NZ    1 
ATOM   27034 N  N     . HIS F 6  159  ? 186.591 62.636  130.751 1.00 59.31  ? 159  HIS F N     1 
ATOM   27035 C  CA    . HIS F 6  159  ? 186.919 61.313  131.263 1.00 58.97  ? 159  HIS F CA    1 
ATOM   27036 C  C     . HIS F 6  159  ? 185.845 60.745  132.180 1.00 58.53  ? 159  HIS F C     1 
ATOM   27037 O  O     . HIS F 6  159  ? 186.058 59.684  132.775 1.00 58.66  ? 159  HIS F O     1 
ATOM   27038 C  CB    . HIS F 6  159  ? 188.260 61.358  132.006 1.00 56.32  ? 159  HIS F CB    1 
ATOM   27039 C  CG    . HIS F 6  159  ? 189.242 62.327  131.423 1.00 58.22  ? 159  HIS F CG    1 
ATOM   27040 N  ND1   . HIS F 6  159  ? 189.794 63.357  132.153 1.00 58.03  ? 159  HIS F ND1   1 
ATOM   27041 C  CD2   . HIS F 6  159  ? 189.766 62.426  130.178 1.00 58.99  ? 159  HIS F CD2   1 
ATOM   27042 C  CE1   . HIS F 6  159  ? 190.617 64.048  131.386 1.00 57.31  ? 159  HIS F CE1   1 
ATOM   27043 N  NE2   . HIS F 6  159  ? 190.618 63.504  130.182 1.00 60.10  ? 159  HIS F NE2   1 
ATOM   27044 N  N     . THR F 6  160  ? 184.702 61.415  132.309 1.00 54.99  ? 160  THR F N     1 
ATOM   27045 C  CA    . THR F 6  160  ? 183.617 61.002  133.190 1.00 56.44  ? 160  THR F CA    1 
ATOM   27046 C  C     . THR F 6  160  ? 182.363 60.672  132.379 1.00 55.89  ? 160  THR F C     1 
ATOM   27047 O  O     . THR F 6  160  ? 182.229 61.039  131.209 1.00 55.31  ? 160  THR F O     1 
ATOM   27048 C  CB    . THR F 6  160  ? 183.336 62.086  134.234 1.00 56.02  ? 160  THR F CB    1 
ATOM   27049 O  OG1   . THR F 6  160  ? 183.012 63.319  133.576 1.00 56.18  ? 160  THR F OG1   1 
ATOM   27050 C  CG2   . THR F 6  160  ? 184.547 62.291  135.127 1.00 52.63  ? 160  THR F CG2   1 
ATOM   27051 N  N     . PHE F 6  161  ? 181.441 59.961  133.024 1.00 55.38  ? 161  PHE F N     1 
ATOM   27052 C  CA    . PHE F 6  161  ? 180.190 59.565  132.394 1.00 56.82  ? 161  PHE F CA    1 
ATOM   27053 C  C     . PHE F 6  161  ? 179.122 59.451  133.474 1.00 56.58  ? 161  PHE F C     1 
ATOM   27054 O  O     . PHE F 6  161  ? 179.414 59.186  134.643 1.00 57.46  ? 161  PHE F O     1 
ATOM   27055 C  CB    . PHE F 6  161  ? 180.340 58.247  131.629 1.00 54.31  ? 161  PHE F CB    1 
ATOM   27056 C  CG    . PHE F 6  161  ? 180.570 57.055  132.513 1.00 56.77  ? 161  PHE F CG    1 
ATOM   27057 C  CD1   . PHE F 6  161  ? 181.813 56.813  133.073 1.00 55.77  ? 161  PHE F CD1   1 
ATOM   27058 C  CD2   . PHE F 6  161  ? 179.543 56.162  132.768 1.00 56.38  ? 161  PHE F CD2   1 
ATOM   27059 C  CE1   . PHE F 6  161  ? 182.023 55.711  133.886 1.00 55.95  ? 161  PHE F CE1   1 
ATOM   27060 C  CE2   . PHE F 6  161  ? 179.746 55.058  133.574 1.00 57.64  ? 161  PHE F CE2   1 
ATOM   27061 C  CZ    . PHE F 6  161  ? 180.987 54.834  134.135 1.00 56.95  ? 161  PHE F CZ    1 
ATOM   27062 N  N     . SER F 6  162  ? 177.873 59.637  133.057 1.00 53.87  ? 162  SER F N     1 
ATOM   27063 C  CA    . SER F 6  162  ? 176.742 59.687  133.965 1.00 54.71  ? 162  SER F CA    1 
ATOM   27064 C  C     . SER F 6  162  ? 175.876 58.452  133.777 1.00 55.88  ? 162  SER F C     1 
ATOM   27065 O  O     . SER F 6  162  ? 175.669 57.977  132.652 1.00 55.39  ? 162  SER F O     1 
ATOM   27066 C  CB    . SER F 6  162  ? 175.900 60.948  133.736 1.00 53.29  ? 162  SER F CB    1 
ATOM   27067 O  OG    . SER F 6  162  ? 176.673 62.122  133.914 1.00 53.76  ? 162  SER F OG    1 
ATOM   27068 N  N     . VAL F 6  163  ? 175.378 57.936  134.896 1.00 57.06  ? 163  VAL F N     1 
ATOM   27069 C  CA    . VAL F 6  163  ? 174.492 56.784  134.918 1.00 58.16  ? 163  VAL F CA    1 
ATOM   27070 C  C     . VAL F 6  163  ? 173.135 57.266  135.401 1.00 57.82  ? 163  VAL F C     1 
ATOM   27071 O  O     . VAL F 6  163  ? 173.046 57.955  136.422 1.00 55.17  ? 163  VAL F O     1 
ATOM   27072 C  CB    . VAL F 6  163  ? 175.035 55.666  135.835 1.00 58.35  ? 163  VAL F CB    1 
ATOM   27073 C  CG1   . VAL F 6  163  ? 174.060 54.488  135.906 1.00 55.12  ? 163  VAL F CG1   1 
ATOM   27074 C  CG2   . VAL F 6  163  ? 176.422 55.223  135.384 1.00 54.00  ? 163  VAL F CG2   1 
ATOM   27075 N  N     . TYR F 6  164  ? 172.087 56.928  134.654 1.00 60.81  ? 164  TYR F N     1 
ATOM   27076 C  CA    . TYR F 6  164  ? 170.708 57.241  135.014 1.00 61.04  ? 164  TYR F CA    1 
ATOM   27077 C  C     . TYR F 6  164  ? 169.981 55.918  135.212 1.00 60.65  ? 164  TYR F C     1 
ATOM   27078 O  O     . TYR F 6  164  ? 170.259 54.943  134.501 1.00 62.83  ? 164  TYR F O     1 
ATOM   27079 C  CB    . TYR F 6  164  ? 170.018 58.039  133.909 1.00 59.27  ? 164  TYR F CB    1 
ATOM   27080 C  CG    . TYR F 6  164  ? 170.831 59.160  133.324 1.00 59.31  ? 164  TYR F CG    1 
ATOM   27081 C  CD1   . TYR F 6  164  ? 170.885 60.391  133.932 1.00 59.52  ? 164  TYR F CD1   1 
ATOM   27082 C  CD2   . TYR F 6  164  ? 171.598 58.962  132.175 1.00 59.68  ? 164  TYR F CD2   1 
ATOM   27083 C  CE1   . TYR F 6  164  ? 171.653 61.418  133.401 1.00 59.48  ? 164  TYR F CE1   1 
ATOM   27084 C  CE2   . TYR F 6  164  ? 172.356 59.959  131.644 1.00 59.59  ? 164  TYR F CE2   1 
ATOM   27085 C  CZ    . TYR F 6  164  ? 172.389 61.197  132.257 1.00 59.08  ? 164  TYR F CZ    1 
ATOM   27086 O  OH    . TYR F 6  164  ? 173.169 62.207  131.724 1.00 57.73  ? 164  TYR F OH    1 
ATOM   27087 N  N     . HIS F 6  165  ? 169.072 55.875  136.181 1.00 56.28  ? 165  HIS F N     1 
ATOM   27088 C  CA    . HIS F 6  165  ? 168.281 54.680  136.438 1.00 57.29  ? 165  HIS F CA    1 
ATOM   27089 C  C     . HIS F 6  165  ? 166.944 54.821  135.725 1.00 57.79  ? 165  HIS F C     1 
ATOM   27090 O  O     . HIS F 6  165  ? 166.263 55.840  135.867 1.00 55.38  ? 165  HIS F O     1 
ATOM   27091 C  CB    . HIS F 6  165  ? 168.065 54.455  137.931 1.00 56.54  ? 165  HIS F CB    1 
ATOM   27092 C  CG    . HIS F 6  165  ? 167.375 53.166  138.250 1.00 58.09  ? 165  HIS F CG    1 
ATOM   27093 N  ND1   . HIS F 6  165  ? 167.279 52.121  137.353 1.00 56.69  ? 165  HIS F ND1   1 
ATOM   27094 C  CD2   . HIS F 6  165  ? 166.733 52.760  139.372 1.00 58.12  ? 165  HIS F CD2   1 
ATOM   27095 C  CE1   . HIS F 6  165  ? 166.611 51.127  137.914 1.00 55.97  ? 165  HIS F CE1   1 
ATOM   27096 N  NE2   . HIS F 6  165  ? 166.270 51.489  139.139 1.00 58.10  ? 165  HIS F NE2   1 
ATOM   27097 N  N     . VAL F 6  166  ? 166.562 53.788  134.978 1.00 54.34  ? 166  VAL F N     1 
ATOM   27098 C  CA    . VAL F 6  166  ? 165.262 53.705  134.322 1.00 52.97  ? 166  VAL F CA    1 
ATOM   27099 C  C     . VAL F 6  166  ? 164.403 52.705  135.078 1.00 54.47  ? 166  VAL F C     1 
ATOM   27100 O  O     . VAL F 6  166  ? 164.835 51.574  135.329 1.00 53.93  ? 166  VAL F O     1 
ATOM   27101 C  CB    . VAL F 6  166  ? 165.394 53.287  132.849 1.00 53.39  ? 166  VAL F CB    1 
ATOM   27102 C  CG1   . VAL F 6  166  ? 164.051 52.825  132.306 1.00 51.90  ? 166  VAL F CG1   1 
ATOM   27103 C  CG2   . VAL F 6  166  ? 165.906 54.439  132.023 1.00 53.15  ? 166  VAL F CG2   1 
ATOM   27104 N  N     . GLN F 6  167  ? 163.184 53.120  135.437 1.00 60.00  ? 167  GLN F N     1 
ATOM   27105 C  CA    . GLN F 6  167  ? 162.214 52.228  136.054 1.00 58.71  ? 167  GLN F CA    1 
ATOM   27106 C  C     . GLN F 6  167  ? 160.914 52.092  135.273 1.00 58.54  ? 167  GLN F C     1 
ATOM   27107 O  O     . GLN F 6  167  ? 160.028 51.347  135.710 1.00 58.83  ? 167  GLN F O     1 
ATOM   27108 C  CB    . GLN F 6  167  ? 161.894 52.693  137.482 1.00 55.56  ? 167  GLN F CB    1 
ATOM   27109 C  CG    . GLN F 6  167  ? 163.112 52.872  138.373 1.00 57.42  ? 167  GLN F CG    1 
ATOM   27110 C  CD    . GLN F 6  167  ? 162.785 53.577  139.677 1.00 58.15  ? 167  GLN F CD    1 
ATOM   27111 O  OE1   . GLN F 6  167  ? 161.957 54.485  139.714 1.00 58.80  ? 167  GLN F OE1   1 
ATOM   27112 N  NE2   . GLN F 6  167  ? 163.429 53.152  140.757 1.00 54.94  ? 167  GLN F NE2   1 
ATOM   27113 N  N     . GLU F 6  168  ? 160.764 52.775  134.140 1.00 63.17  ? 168  GLU F N     1 
ATOM   27114 C  CA    . GLU F 6  168  ? 159.533 52.714  133.364 1.00 63.84  ? 168  GLU F CA    1 
ATOM   27115 C  C     . GLU F 6  168  ? 159.822 52.265  131.940 1.00 64.93  ? 168  GLU F C     1 
ATOM   27116 O  O     . GLU F 6  168  ? 160.909 52.501  131.404 1.00 65.62  ? 168  GLU F O     1 
ATOM   27117 C  CB    . GLU F 6  168  ? 158.798 54.061  133.332 1.00 61.41  ? 168  GLU F CB    1 
ATOM   27118 C  CG    . GLU F 6  168  ? 158.259 54.524  134.674 1.00 63.07  ? 168  GLU F CG    1 
ATOM   27119 C  CD    . GLU F 6  168  ? 157.313 55.704  134.539 1.00 63.78  ? 168  GLU F CD    1 
ATOM   27120 O  OE1   . GLU F 6  168  ? 156.905 56.009  133.399 1.00 64.12  ? 168  GLU F OE1   1 
ATOM   27121 O  OE2   . GLU F 6  168  ? 156.988 56.328  135.571 1.00 63.18  ? 168  GLU F OE2   1 
ATOM   27122 N  N     . GLU F 6  169  ? 158.834 51.608  131.342 1.00 60.85  ? 169  GLU F N     1 
ATOM   27123 C  CA    . GLU F 6  169  ? 158.955 51.065  129.999 1.00 61.16  ? 169  GLU F CA    1 
ATOM   27124 C  C     . GLU F 6  169  ? 158.862 52.164  128.949 1.00 61.79  ? 169  GLU F C     1 
ATOM   27125 O  O     . GLU F 6  169  ? 158.314 53.244  129.188 1.00 61.11  ? 169  GLU F O     1 
ATOM   27126 C  CB    . GLU F 6  169  ? 157.863 50.023  129.756 1.00 59.50  ? 169  GLU F CB    1 
ATOM   27127 C  CG    . GLU F 6  169  ? 157.934 48.832  130.701 1.00 60.32  ? 169  GLU F CG    1 
ATOM   27128 C  CD    . GLU F 6  169  ? 158.847 47.734  130.189 1.00 62.49  ? 169  GLU F CD    1 
ATOM   27129 O  OE1   . GLU F 6  169  ? 159.283 47.821  129.020 1.00 60.57  ? 169  GLU F OE1   1 
ATOM   27130 O  OE2   . GLU F 6  169  ? 159.131 46.789  130.956 1.00 62.30  ? 169  GLU F OE2   1 
ATOM   27131 N  N     . LEU F 6  170  ? 159.417 51.876  127.777 1.00 56.99  ? 170  LEU F N     1 
ATOM   27132 C  CA    . LEU F 6  170  ? 159.259 52.745  126.619 1.00 55.09  ? 170  LEU F CA    1 
ATOM   27133 C  C     . LEU F 6  170  ? 158.021 52.301  125.853 1.00 54.46  ? 170  LEU F C     1 
ATOM   27134 O  O     . LEU F 6  170  ? 157.982 51.191  125.310 1.00 55.87  ? 170  LEU F O     1 
ATOM   27135 C  CB    . LEU F 6  170  ? 160.503 52.702  125.737 1.00 55.10  ? 170  LEU F CB    1 
ATOM   27136 C  CG    . LEU F 6  170  ? 160.337 53.306  124.338 1.00 55.32  ? 170  LEU F CG    1 
ATOM   27137 C  CD1   . LEU F 6  170  ? 160.473 54.822  124.353 1.00 52.80  ? 170  LEU F CD1   1 
ATOM   27138 C  CD2   . LEU F 6  170  ? 161.318 52.676  123.354 1.00 53.42  ? 170  LEU F CD2   1 
ATOM   27139 N  N     . THR F 6  171  ? 157.009 53.161  125.811 1.00 47.49  ? 171  THR F N     1 
ATOM   27140 C  CA    . THR F 6  171  ? 155.782 52.807  125.119 1.00 49.76  ? 171  THR F CA    1 
ATOM   27141 C  C     . THR F 6  171  ? 155.915 53.101  123.624 1.00 49.85  ? 171  THR F C     1 
ATOM   27142 O  O     . THR F 6  171  ? 156.906 53.670  123.156 1.00 48.53  ? 171  THR F O     1 
ATOM   27143 C  CB    . THR F 6  171  ? 154.590 53.545  125.736 1.00 49.34  ? 171  THR F CB    1 
ATOM   27144 O  OG1   . THR F 6  171  ? 154.868 54.952  125.796 1.00 49.37  ? 171  THR F OG1   1 
ATOM   27145 C  CG2   . THR F 6  171  ? 154.352 53.037  127.149 1.00 47.73  ? 171  THR F CG2   1 
ATOM   27146 N  N     . GLN F 6  172  ? 154.901 52.683  122.868 1.00 48.59  ? 172  GLN F N     1 
ATOM   27147 C  CA    . GLN F 6  172  ? 154.994 52.694  121.411 1.00 48.24  ? 172  GLN F CA    1 
ATOM   27148 C  C     . GLN F 6  172  ? 154.936 54.106  120.837 1.00 50.40  ? 172  GLN F C     1 
ATOM   27149 O  O     . GLN F 6  172  ? 155.616 54.400  119.849 1.00 49.15  ? 172  GLN F O     1 
ATOM   27150 C  CB    . GLN F 6  172  ? 153.882 51.833  120.820 1.00 50.23  ? 172  GLN F CB    1 
ATOM   27151 C  CG    . GLN F 6  172  ? 154.173 50.351  120.872 1.00 49.50  ? 172  GLN F CG    1 
ATOM   27152 C  CD    . GLN F 6  172  ? 153.250 49.564  119.983 1.00 49.08  ? 172  GLN F CD    1 
ATOM   27153 O  OE1   . GLN F 6  172  ? 152.224 50.074  119.530 1.00 47.67  ? 172  GLN F OE1   1 
ATOM   27154 N  NE2   . GLN F 6  172  ? 153.598 48.307  119.734 1.00 47.33  ? 172  GLN F NE2   1 
ATOM   27155 N  N     . GLU F 6  173  ? 154.129 54.992  121.431 1.00 51.02  ? 173  GLU F N     1 
ATOM   27156 C  CA    . GLU F 6  173  ? 153.976 56.339  120.879 1.00 50.90  ? 173  GLU F CA    1 
ATOM   27157 C  C     . GLU F 6  173  ? 155.180 57.235  121.173 1.00 51.19  ? 173  GLU F C     1 
ATOM   27158 O  O     . GLU F 6  173  ? 155.497 58.122  120.370 1.00 50.09  ? 173  GLU F O     1 
ATOM   27159 C  CB    . GLU F 6  173  ? 152.684 56.978  121.395 1.00 47.84  ? 173  GLU F CB    1 
ATOM   27160 C  CG    . GLU F 6  173  ? 152.794 57.575  122.781 1.00 49.15  ? 173  GLU F CG    1 
ATOM   27161 C  CD    . GLU F 6  173  ? 152.977 56.489  123.824 1.00 51.45  ? 173  GLU F CD    1 
ATOM   27162 O  OE1   . GLU F 6  173  ? 152.584 55.340  123.537 1.00 49.19  ? 173  GLU F OE1   1 
ATOM   27163 O  OE2   . GLU F 6  173  ? 153.466 56.778  124.928 1.00 50.78  ? 173  GLU F OE2   1 
ATOM   27164 N  N     . GLN F 6  174  ? 155.854 57.050  122.316 1.00 44.71  ? 174  GLN F N     1 
ATOM   27165 C  CA    . GLN F 6  174  ? 157.116 57.765  122.507 1.00 47.84  ? 174  GLN F CA    1 
ATOM   27166 C  C     . GLN F 6  174  ? 158.156 57.304  121.500 1.00 49.66  ? 174  GLN F C     1 
ATOM   27167 O  O     . GLN F 6  174  ? 158.962 58.111  121.029 1.00 46.72  ? 174  GLN F O     1 
ATOM   27168 C  CB    . GLN F 6  174  ? 157.640 57.610  123.945 1.00 46.65  ? 174  GLN F CB    1 
ATOM   27169 C  CG    . GLN F 6  174  ? 156.580 57.310  125.002 1.00 49.96  ? 174  GLN F CG    1 
ATOM   27170 C  CD    . GLN F 6  174  ? 155.564 58.433  125.182 1.00 50.49  ? 174  GLN F CD    1 
ATOM   27171 O  OE1   . GLN F 6  174  ? 155.562 59.428  124.455 1.00 48.99  ? 174  GLN F OE1   1 
ATOM   27172 N  NE2   . GLN F 6  174  ? 154.659 58.247  126.145 1.00 45.49  ? 174  GLN F NE2   1 
ATOM   27173 N  N     . ALA F 6  175  ? 158.160 56.010  121.172 1.00 46.88  ? 175  ALA F N     1 
ATOM   27174 C  CA    . ALA F 6  175  ? 159.008 55.522  120.090 1.00 48.21  ? 175  ALA F CA    1 
ATOM   27175 C  C     . ALA F 6  175  ? 158.606 56.152  118.759 1.00 45.91  ? 175  ALA F C     1 
ATOM   27176 O  O     . ALA F 6  175  ? 159.460 56.456  117.916 1.00 41.82  ? 175  ALA F O     1 
ATOM   27177 C  CB    . ALA F 6  175  ? 158.931 53.991  120.016 1.00 44.79  ? 175  ALA F CB    1 
ATOM   27178 N  N     . LEU F 6  176  ? 157.303 56.324  118.542 1.00 47.29  ? 176  LEU F N     1 
ATOM   27179 C  CA    . LEU F 6  176  ? 156.834 56.966  117.321 1.00 50.83  ? 176  LEU F CA    1 
ATOM   27180 C  C     . LEU F 6  176  ? 157.357 58.392  117.223 1.00 50.68  ? 176  LEU F C     1 
ATOM   27181 O  O     . LEU F 6  176  ? 157.780 58.833  116.148 1.00 49.51  ? 176  LEU F O     1 
ATOM   27182 C  CB    . LEU F 6  176  ? 155.306 56.940  117.277 1.00 49.29  ? 176  LEU F CB    1 
ATOM   27183 C  CG    . LEU F 6  176  ? 154.634 57.586  116.065 1.00 48.44  ? 176  LEU F CG    1 
ATOM   27184 C  CD1   . LEU F 6  176  ? 155.063 56.912  114.772 1.00 47.61  ? 176  LEU F CD1   1 
ATOM   27185 C  CD2   . LEU F 6  176  ? 153.124 57.549  116.206 1.00 46.75  ? 176  LEU F CD2   1 
ATOM   27186 N  N     . ASN F 6  177  ? 157.348 59.120  118.343 1.00 49.76  ? 177  ASN F N     1 
ATOM   27187 C  CA    . ASN F 6  177  ? 157.987 60.434  118.398 1.00 48.97  ? 177  ASN F CA    1 
ATOM   27188 C  C     . ASN F 6  177  ? 159.483 60.346  118.106 1.00 51.52  ? 177  ASN F C     1 
ATOM   27189 O  O     . ASN F 6  177  ? 160.002 61.068  117.247 1.00 52.33  ? 177  ASN F O     1 
ATOM   27190 C  CB    . ASN F 6  177  ? 157.751 61.070  119.771 1.00 49.54  ? 177  ASN F CB    1 
ATOM   27191 C  CG    . ASN F 6  177  ? 157.323 62.518  119.686 1.00 52.93  ? 177  ASN F CG    1 
ATOM   27192 O  OD1   . ASN F 6  177  ? 156.759 62.962  118.686 1.00 54.65  ? 177  ASN F OD1   1 
ATOM   27193 N  ND2   . ASN F 6  177  ? 157.585 63.265  120.750 1.00 50.55  ? 177  ASN F ND2   1 
ATOM   27194 N  N     . LEU F 6  178  ? 160.192 59.449  118.797 1.00 49.38  ? 178  LEU F N     1 
ATOM   27195 C  CA    . LEU F 6  178  ? 161.641 59.341  118.652 1.00 49.08  ? 178  LEU F CA    1 
ATOM   27196 C  C     . LEU F 6  178  ? 162.060 58.834  117.286 1.00 51.48  ? 178  LEU F C     1 
ATOM   27197 O  O     . LEU F 6  178  ? 163.260 58.840  116.987 1.00 52.29  ? 178  LEU F O     1 
ATOM   27198 C  CB    . LEU F 6  178  ? 162.226 58.418  119.724 1.00 48.16  ? 178  LEU F CB    1 
ATOM   27199 C  CG    . LEU F 6  178  ? 161.954 58.812  121.171 1.00 50.75  ? 178  LEU F CG    1 
ATOM   27200 C  CD1   . LEU F 6  178  ? 162.480 57.762  122.126 1.00 51.56  ? 178  LEU F CD1   1 
ATOM   27201 C  CD2   . LEU F 6  178  ? 162.575 60.163  121.450 1.00 49.48  ? 178  LEU F CD2   1 
ATOM   27202 N  N     . THR F 6  179  ? 161.111 58.354  116.481 1.00 46.09  ? 179  THR F N     1 
ATOM   27203 C  CA    . THR F 6  179  ? 161.428 57.956  115.117 1.00 46.56  ? 179  THR F CA    1 
ATOM   27204 C  C     . THR F 6  179  ? 162.127 59.073  114.359 1.00 48.68  ? 179  THR F C     1 
ATOM   27205 O  O     . THR F 6  179  ? 163.012 58.806  113.542 1.00 45.55  ? 179  THR F O     1 
ATOM   27206 C  CB    . THR F 6  179  ? 160.154 57.558  114.378 1.00 46.74  ? 179  THR F CB    1 
ATOM   27207 O  OG1   . THR F 6  179  ? 159.322 56.780  115.246 1.00 47.20  ? 179  THR F OG1   1 
ATOM   27208 C  CG2   . THR F 6  179  ? 160.497 56.727  113.149 1.00 44.21  ? 179  THR F CG2   1 
ATOM   27209 N  N     . LYS F 6  180  ? 161.748 60.329  114.614 1.00 52.14  ? 180  LYS F N     1 
ATOM   27210 C  CA    . LYS F 6  180  ? 162.390 61.441  113.921 1.00 52.16  ? 180  LYS F CA    1 
ATOM   27211 C  C     . LYS F 6  180  ? 163.868 61.538  114.281 1.00 51.41  ? 180  LYS F C     1 
ATOM   27212 O  O     . LYS F 6  180  ? 164.717 61.737  113.404 1.00 47.82  ? 180  LYS F O     1 
ATOM   27213 C  CB    . LYS F 6  180  ? 161.669 62.752  114.239 1.00 49.18  ? 180  LYS F CB    1 
ATOM   27214 C  CG    . LYS F 6  180  ? 162.223 63.949  113.474 1.00 50.49  ? 180  LYS F CG    1 
ATOM   27215 C  CD    . LYS F 6  180  ? 161.545 65.254  113.873 1.00 52.02  ? 180  LYS F CD    1 
ATOM   27216 C  CE    . LYS F 6  180  ? 162.238 66.447  113.221 1.00 50.16  ? 180  LYS F CE    1 
ATOM   27217 N  NZ    . LYS F 6  180  ? 161.626 67.745  113.600 1.00 50.22  ? 180  LYS F NZ    1 
ATOM   27218 N  N     . LEU F 6  181  ? 164.198 61.400  115.567 1.00 46.90  ? 181  LEU F N     1 
ATOM   27219 C  CA    . LEU F 6  181  ? 165.597 61.468  115.975 1.00 48.42  ? 181  LEU F CA    1 
ATOM   27220 C  C     . LEU F 6  181  ? 166.375 60.266  115.456 1.00 48.96  ? 181  LEU F C     1 
ATOM   27221 O  O     . LEU F 6  181  ? 167.546 60.388  115.065 1.00 47.03  ? 181  LEU F O     1 
ATOM   27222 C  CB    . LEU F 6  181  ? 165.697 61.568  117.497 1.00 48.93  ? 181  LEU F CB    1 
ATOM   27223 C  CG    . LEU F 6  181  ? 165.453 62.944  118.131 1.00 49.72  ? 181  LEU F CG    1 
ATOM   27224 C  CD1   . LEU F 6  181  ? 163.973 63.315  118.130 1.00 45.84  ? 181  LEU F CD1   1 
ATOM   27225 C  CD2   . LEU F 6  181  ? 166.027 63.011  119.539 1.00 46.63  ? 181  LEU F CD2   1 
ATOM   27226 N  N     . VAL F 6  182  ? 165.736 59.095  115.437 1.00 48.61  ? 182  VAL F N     1 
ATOM   27227 C  CA    . VAL F 6  182  ? 166.366 57.918  114.845 1.00 51.59  ? 182  VAL F CA    1 
ATOM   27228 C  C     . VAL F 6  182  ? 166.678 58.173  113.376 1.00 50.55  ? 182  VAL F C     1 
ATOM   27229 O  O     . VAL F 6  182  ? 167.782 57.888  112.899 1.00 47.98  ? 182  VAL F O     1 
ATOM   27230 C  CB    . VAL F 6  182  ? 165.467 56.681  115.032 1.00 50.38  ? 182  VAL F CB    1 
ATOM   27231 C  CG1   . VAL F 6  182  ? 166.073 55.470  114.341 1.00 47.98  ? 182  VAL F CG1   1 
ATOM   27232 C  CG2   . VAL F 6  182  ? 165.257 56.398  116.511 1.00 47.13  ? 182  VAL F CG2   1 
ATOM   27233 N  N     . ASN F 6  183  ? 165.721 58.751  112.647 1.00 48.90  ? 183  ASN F N     1 
ATOM   27234 C  CA    . ASN F 6  183  ? 165.925 59.053  111.236 1.00 50.24  ? 183  ASN F CA    1 
ATOM   27235 C  C     . ASN F 6  183  ? 167.017 60.099  111.037 1.00 50.94  ? 183  ASN F C     1 
ATOM   27236 O  O     . ASN F 6  183  ? 167.767 60.036  110.058 1.00 50.57  ? 183  ASN F O     1 
ATOM   27237 C  CB    . ASN F 6  183  ? 164.609 59.516  110.608 1.00 51.10  ? 183  ASN F CB    1 
ATOM   27238 C  CG    . ASN F 6  183  ? 163.564 58.404  110.534 1.00 52.67  ? 183  ASN F CG    1 
ATOM   27239 O  OD1   . ASN F 6  183  ? 163.897 57.225  110.423 1.00 52.36  ? 183  ASN F OD1   1 
ATOM   27240 N  ND2   . ASN F 6  183  ? 162.295 58.782  110.595 1.00 49.35  ? 183  ASN F ND2   1 
ATOM   27241 N  N     . ILE F 6  184  ? 167.107 61.081  111.938 1.00 48.35  ? 184  ILE F N     1 
ATOM   27242 C  CA    . ILE F 6  184  ? 168.165 62.088  111.838 1.00 48.26  ? 184  ILE F CA    1 
ATOM   27243 C  C     . ILE F 6  184  ? 169.537 61.447  112.029 1.00 49.20  ? 184  ILE F C     1 
ATOM   27244 O  O     . ILE F 6  184  ? 170.494 61.759  111.305 1.00 46.63  ? 184  ILE F O     1 
ATOM   27245 C  CB    . ILE F 6  184  ? 167.920 63.233  112.836 1.00 48.18  ? 184  ILE F CB    1 
ATOM   27246 C  CG1   . ILE F 6  184  ? 166.759 64.106  112.358 1.00 46.87  ? 184  ILE F CG1   1 
ATOM   27247 C  CG2   . ILE F 6  184  ? 169.168 64.081  112.997 1.00 47.39  ? 184  ILE F CG2   1 
ATOM   27248 C  CD1   . ILE F 6  184  ? 166.348 65.175  113.345 1.00 45.36  ? 184  ILE F CD1   1 
ATOM   27249 N  N     . ILE F 6  185  ? 169.653 60.534  112.999 1.00 49.07  ? 185  ILE F N     1 
ATOM   27250 C  CA    . ILE F 6  185  ? 170.877 59.745  113.130 1.00 51.90  ? 185  ILE F CA    1 
ATOM   27251 C  C     . ILE F 6  185  ? 171.152 58.974  111.842 1.00 52.81  ? 185  ILE F C     1 
ATOM   27252 O  O     . ILE F 6  185  ? 172.301 58.875  111.393 1.00 47.93  ? 185  ILE F O     1 
ATOM   27253 C  CB    . ILE F 6  185  ? 170.786 58.802  114.347 1.00 49.75  ? 185  ILE F CB    1 
ATOM   27254 C  CG1   . ILE F 6  185  ? 171.110 59.556  115.632 1.00 49.96  ? 185  ILE F CG1   1 
ATOM   27255 C  CG2   . ILE F 6  185  ? 171.733 57.620  114.196 1.00 48.68  ? 185  ILE F CG2   1 
ATOM   27256 C  CD1   . ILE F 6  185  ? 170.689 58.846  116.902 1.00 48.29  ? 185  ILE F CD1   1 
ATOM   27257 N  N     . GLU F 6  186  ? 170.104 58.417  111.227 1.00 53.98  ? 186  GLU F N     1 
ATOM   27258 C  CA    . GLU F 6  186  ? 170.293 57.627  110.012 1.00 54.22  ? 186  GLU F CA    1 
ATOM   27259 C  C     . GLU F 6  186  ? 170.840 58.476  108.868 1.00 54.96  ? 186  GLU F C     1 
ATOM   27260 O  O     . GLU F 6  186  ? 171.754 58.051  108.149 1.00 52.70  ? 186  GLU F O     1 
ATOM   27261 C  CB    . GLU F 6  186  ? 168.975 56.970  109.600 1.00 52.32  ? 186  GLU F CB    1 
ATOM   27262 C  CG    . GLU F 6  186  ? 168.456 55.932  110.582 1.00 54.14  ? 186  GLU F CG    1 
ATOM   27263 C  CD    . GLU F 6  186  ? 166.974 55.652  110.401 1.00 55.97  ? 186  GLU F CD    1 
ATOM   27264 O  OE1   . GLU F 6  186  ? 166.333 56.348  109.588 1.00 53.01  ? 186  GLU F OE1   1 
ATOM   27265 O  OE2   . GLU F 6  186  ? 166.448 54.744  111.077 1.00 57.07  ? 186  GLU F OE2   1 
ATOM   27266 N  N     . MET F 6  187  ? 170.282 59.676  108.673 1.00 51.84  ? 187  MET F N     1 
ATOM   27267 C  CA    . MET F 6  187  ? 170.752 60.524  107.580 1.00 52.90  ? 187  MET F CA    1 
ATOM   27268 C  C     . MET F 6  187  ? 172.152 61.051  107.865 1.00 54.75  ? 187  MET F C     1 
ATOM   27269 O  O     . MET F 6  187  ? 172.970 61.188  106.945 1.00 54.11  ? 187  MET F O     1 
ATOM   27270 C  CB    . MET F 6  187  ? 169.782 61.677  107.307 1.00 52.98  ? 187  MET F CB    1 
ATOM   27271 C  CG    . MET F 6  187  ? 169.112 62.273  108.518 1.00 51.96  ? 187  MET F CG    1 
ATOM   27272 S  SD    . MET F 6  187  ? 168.041 63.669  108.126 1.00 63.29  ? 187  MET F SD    1 
ATOM   27273 C  CE    . MET F 6  187  ? 169.237 64.983  107.912 1.00 52.58  ? 187  MET F CE    1 
ATOM   27274 N  N     . LEU F 6  188  ? 172.460 61.327  109.137 1.00 50.94  ? 188  LEU F N     1 
ATOM   27275 C  CA    . LEU F 6  188  ? 173.836 61.671  109.482 1.00 52.95  ? 188  LEU F CA    1 
ATOM   27276 C  C     . LEU F 6  188  ? 174.785 60.521  109.159 1.00 52.29  ? 188  LEU F C     1 
ATOM   27277 O  O     . LEU F 6  188  ? 175.894 60.745  108.664 1.00 48.52  ? 188  LEU F O     1 
ATOM   27278 C  CB    . LEU F 6  188  ? 173.937 62.059  110.958 1.00 51.47  ? 188  LEU F CB    1 
ATOM   27279 C  CG    . LEU F 6  188  ? 173.393 63.435  111.350 1.00 50.17  ? 188  LEU F CG    1 
ATOM   27280 C  CD1   . LEU F 6  188  ? 173.570 63.677  112.838 1.00 50.02  ? 188  LEU F CD1   1 
ATOM   27281 C  CD2   . LEU F 6  188  ? 174.070 64.531  110.545 1.00 49.45  ? 188  LEU F CD2   1 
ATOM   27282 N  N     . LEU F 6  189  ? 174.362 59.283  109.425 1.00 51.02  ? 189  LEU F N     1 
ATOM   27283 C  CA    . LEU F 6  189  ? 175.192 58.123  109.110 1.00 50.80  ? 189  LEU F CA    1 
ATOM   27284 C  C     . LEU F 6  189  ? 175.425 58.002  107.609 1.00 53.77  ? 189  LEU F C     1 
ATOM   27285 O  O     . LEU F 6  189  ? 176.555 57.765  107.162 1.00 51.09  ? 189  LEU F O     1 
ATOM   27286 C  CB    . LEU F 6  189  ? 174.538 56.846  109.639 1.00 47.73  ? 189  LEU F CB    1 
ATOM   27287 C  CG    . LEU F 6  189  ? 174.612 56.526  111.132 1.00 51.19  ? 189  LEU F CG    1 
ATOM   27288 C  CD1   . LEU F 6  189  ? 174.081 55.118  111.383 1.00 51.30  ? 189  LEU F CD1   1 
ATOM   27289 C  CD2   . LEU F 6  189  ? 176.029 56.683  111.670 1.00 48.60  ? 189  LEU F CD2   1 
ATOM   27290 N  N     . GLU F 6  190  ? 174.362 58.144  106.812 1.00 53.80  ? 190  GLU F N     1 
ATOM   27291 C  CA    . GLU F 6  190  ? 174.526 57.996  105.370 1.00 53.52  ? 190  GLU F CA    1 
ATOM   27292 C  C     . GLU F 6  190  ? 175.302 59.155  104.762 1.00 53.37  ? 190  GLU F C     1 
ATOM   27293 O  O     . GLU F 6  190  ? 175.908 58.984  103.700 1.00 54.03  ? 190  GLU F O     1 
ATOM   27294 C  CB    . GLU F 6  190  ? 173.175 57.852  104.662 1.00 51.49  ? 190  GLU F CB    1 
ATOM   27295 C  CG    . GLU F 6  190  ? 172.297 59.079  104.702 1.00 51.66  ? 190  GLU F CG    1 
ATOM   27296 C  CD    . GLU F 6  190  ? 170.858 58.774  104.352 1.00 54.63  ? 190  GLU F CD    1 
ATOM   27297 O  OE1   . GLU F 6  190  ? 170.098 58.352  105.248 1.00 51.02  ? 190  GLU F OE1   1 
ATOM   27298 O  OE2   . GLU F 6  190  ? 170.486 58.959  103.175 1.00 55.24  ? 190  GLU F OE2   1 
ATOM   27299 N  N     . SER F 6  191  ? 175.294 60.327  105.402 1.00 49.45  ? 191  SER F N     1 
ATOM   27300 C  CA    . SER F 6  191  ? 176.169 61.406  104.956 1.00 51.74  ? 191  SER F CA    1 
ATOM   27301 C  C     . SER F 6  191  ? 177.621 61.138  105.337 1.00 52.93  ? 191  SER F C     1 
ATOM   27302 O  O     . SER F 6  191  ? 178.531 61.376  104.536 1.00 50.28  ? 191  SER F O     1 
ATOM   27303 C  CB    . SER F 6  191  ? 175.708 62.739  105.542 1.00 50.89  ? 191  SER F CB    1 
ATOM   27304 O  OG    . SER F 6  191  ? 176.515 63.802  105.069 1.00 50.66  ? 191  SER F OG    1 
ATOM   27305 N  N     . ARG F 6  192  ? 177.849 60.634  106.552 1.00 53.60  ? 192  ARG F N     1 
ATOM   27306 C  CA    . ARG F 6  192  ? 179.201 60.325  107.000 1.00 53.34  ? 192  ARG F CA    1 
ATOM   27307 C  C     . ARG F 6  192  ? 179.838 59.226  106.158 1.00 54.35  ? 192  ARG F C     1 
ATOM   27308 O  O     . ARG F 6  192  ? 181.050 59.259  105.911 1.00 51.56  ? 192  ARG F O     1 
ATOM   27309 C  CB    . ARG F 6  192  ? 179.171 59.929  108.477 1.00 51.29  ? 192  ARG F CB    1 
ATOM   27310 C  CG    . ARG F 6  192  ? 180.317 59.046  108.920 1.00 52.99  ? 192  ARG F CG    1 
ATOM   27311 C  CD    . ARG F 6  192  ? 180.358 58.916  110.431 1.00 54.05  ? 192  ARG F CD    1 
ATOM   27312 N  NE    . ARG F 6  192  ? 181.162 57.777  110.855 1.00 55.14  ? 192  ARG F NE    1 
ATOM   27313 C  CZ    . ARG F 6  192  ? 181.667 57.628  112.071 1.00 55.33  ? 192  ARG F CZ    1 
ATOM   27314 N  NH1   . ARG F 6  192  ? 181.493 58.547  113.008 1.00 55.21  ? 192  ARG F NH1   1 
ATOM   27315 N  NH2   . ARG F 6  192  ? 182.373 56.536  112.351 1.00 53.62  ? 192  ARG F NH2   1 
ATOM   27316 N  N     . SER F 6  193  ? 179.041 58.255  105.706 1.00 51.61  ? 193  SER F N     1 
ATOM   27317 C  CA    . SER F 6  193  ? 179.574 57.166  104.895 1.00 52.23  ? 193  SER F CA    1 
ATOM   27318 C  C     . SER F 6  193  ? 180.179 57.651  103.580 1.00 54.01  ? 193  SER F C     1 
ATOM   27319 O  O     . SER F 6  193  ? 181.090 56.999  103.056 1.00 53.75  ? 193  SER F O     1 
ATOM   27320 C  CB    . SER F 6  193  ? 178.476 56.142  104.607 1.00 52.37  ? 193  SER F CB    1 
ATOM   27321 O  OG    . SER F 6  193  ? 177.499 56.682  103.735 1.00 52.89  ? 193  SER F OG    1 
ATOM   27322 N  N     . LYS F 6  194  ? 179.704 58.776  103.037 1.00 46.14  ? 194  LYS F N     1 
ATOM   27323 C  CA    . LYS F 6  194  ? 180.273 59.286  101.792 1.00 47.76  ? 194  LYS F CA    1 
ATOM   27324 C  C     . LYS F 6  194  ? 181.653 59.896  102.002 1.00 48.36  ? 194  LYS F C     1 
ATOM   27325 O  O     . LYS F 6  194  ? 182.418 60.034  101.040 1.00 49.27  ? 194  LYS F O     1 
ATOM   27326 C  CB    . LYS F 6  194  ? 179.346 60.324  101.161 1.00 47.69  ? 194  LYS F CB    1 
ATOM   27327 C  CG    . LYS F 6  194  ? 179.157 60.162  99.664  1.00 47.14  ? 194  LYS F CG    1 
ATOM   27328 C  CD    . LYS F 6  194  ? 178.645 61.448  99.041  1.00 47.50  ? 194  LYS F CD    1 
ATOM   27329 C  CE    . LYS F 6  194  ? 177.501 61.199  98.080  1.00 46.18  ? 194  LYS F CE    1 
ATOM   27330 N  NZ    . LYS F 6  194  ? 176.751 62.445  97.798  1.00 45.94  ? 194  LYS F NZ    1 
ATOM   27331 N  N     . LYS F 6  195  ? 181.986 60.268  103.234 1.00 51.99  ? 195  LYS F N     1 
ATOM   27332 C  CA    . LYS F 6  195  ? 183.252 60.931  103.499 1.00 52.39  ? 195  LYS F CA    1 
ATOM   27333 C  C     . LYS F 6  195  ? 184.412 59.945  103.390 1.00 52.36  ? 195  LYS F C     1 
ATOM   27334 O  O     . LYS F 6  195  ? 184.228 58.725  103.346 1.00 53.11  ? 195  LYS F O     1 
ATOM   27335 C  CB    . LYS F 6  195  ? 183.241 61.573  104.885 1.00 51.15  ? 195  LYS F CB    1 
ATOM   27336 C  CG    . LYS F 6  195  ? 182.074 62.506  105.116 1.00 52.36  ? 195  LYS F CG    1 
ATOM   27337 C  CD    . LYS F 6  195  ? 181.967 62.894  106.578 1.00 53.99  ? 195  LYS F CD    1 
ATOM   27338 C  CE    . LYS F 6  195  ? 180.776 63.806  106.818 1.00 53.17  ? 195  LYS F CE    1 
ATOM   27339 N  NZ    . LYS F 6  195  ? 180.784 64.995  105.931 1.00 53.47  ? 195  LYS F NZ    1 
ATOM   27340 N  N     . ASP F 6  196  ? 185.623 60.495  103.339 1.00 48.67  ? 196  ASP F N     1 
ATOM   27341 C  CA    . ASP F 6  196  ? 186.811 59.661  103.240 1.00 51.15  ? 196  ASP F CA    1 
ATOM   27342 C  C     . ASP F 6  196  ? 187.035 58.882  104.530 1.00 50.85  ? 196  ASP F C     1 
ATOM   27343 O  O     . ASP F 6  196  ? 186.701 59.343  105.624 1.00 48.26  ? 196  ASP F O     1 
ATOM   27344 C  CB    . ASP F 6  196  ? 188.039 60.515  102.923 1.00 49.48  ? 196  ASP F CB    1 
ATOM   27345 C  CG    . ASP F 6  196  ? 189.223 59.683  102.477 1.00 51.78  ? 196  ASP F CG    1 
ATOM   27346 O  OD1   . ASP F 6  196  ? 189.066 58.451  102.335 1.00 52.37  ? 196  ASP F OD1   1 
ATOM   27347 O  OD2   . ASP F 6  196  ? 190.307 60.263  102.256 1.00 50.47  ? 196  ASP F OD2   1 
ATOM   27348 N  N     . PHE F 6  197  ? 187.600 57.681  104.388 1.00 53.23  ? 197  PHE F N     1 
ATOM   27349 C  CA    . PHE F 6  197  ? 187.927 56.866  105.552 1.00 55.51  ? 197  PHE F CA    1 
ATOM   27350 C  C     . PHE F 6  197  ? 189.018 57.506  106.406 1.00 56.91  ? 197  PHE F C     1 
ATOM   27351 O  O     . PHE F 6  197  ? 188.909 57.538  107.638 1.00 53.45  ? 197  PHE F O     1 
ATOM   27352 C  CB    . PHE F 6  197  ? 188.358 55.473  105.100 1.00 53.66  ? 197  PHE F CB    1 
ATOM   27353 C  CG    . PHE F 6  197  ? 188.095 54.405  106.111 1.00 55.91  ? 197  PHE F CG    1 
ATOM   27354 C  CD1   . PHE F 6  197  ? 187.106 54.570  107.062 1.00 53.08  ? 197  PHE F CD1   1 
ATOM   27355 C  CD2   . PHE F 6  197  ? 188.847 53.240  106.122 1.00 55.18  ? 197  PHE F CD2   1 
ATOM   27356 C  CE1   . PHE F 6  197  ? 186.867 53.599  107.996 1.00 54.83  ? 197  PHE F CE1   1 
ATOM   27357 C  CE2   . PHE F 6  197  ? 188.611 52.257  107.061 1.00 54.31  ? 197  PHE F CE2   1 
ATOM   27358 C  CZ    . PHE F 6  197  ? 187.618 52.437  108.000 1.00 56.14  ? 197  PHE F CZ    1 
ATOM   27359 N  N     . LYS F 6  198  ? 190.080 58.015  105.770 1.00 51.51  ? 198  LYS F N     1 
ATOM   27360 C  CA    . LYS F 6  198  ? 191.240 58.492  106.520 1.00 49.28  ? 198  LYS F CA    1 
ATOM   27361 C  C     . LYS F 6  198  ? 190.897 59.698  107.386 1.00 52.19  ? 198  LYS F C     1 
ATOM   27362 O  O     . LYS F 6  198  ? 191.361 59.799  108.527 1.00 47.77  ? 198  LYS F O     1 
ATOM   27363 C  CB    . LYS F 6  198  ? 192.384 58.831  105.568 1.00 47.71  ? 198  LYS F CB    1 
ATOM   27364 C  CG    . LYS F 6  198  ? 193.764 58.547  106.141 1.00 48.73  ? 198  LYS F CG    1 
ATOM   27365 C  CD    . LYS F 6  198  ? 194.854 58.893  105.141 1.00 50.21  ? 198  LYS F CD    1 
ATOM   27366 C  CE    . LYS F 6  198  ? 196.096 58.044  105.347 1.00 48.12  ? 198  LYS F CE    1 
ATOM   27367 N  NZ    . LYS F 6  198  ? 197.334 58.869  105.340 1.00 48.90  ? 198  LYS F NZ    1 
ATOM   27368 N  N     . GLN F 6  199  ? 190.100 60.631  106.858 1.00 57.21  ? 199  GLN F N     1 
ATOM   27369 C  CA    . GLN F 6  199  ? 189.732 61.809  107.639 1.00 55.55  ? 199  GLN F CA    1 
ATOM   27370 C  C     . GLN F 6  199  ? 188.953 61.419  108.890 1.00 55.61  ? 199  GLN F C     1 
ATOM   27371 O  O     . GLN F 6  199  ? 189.305 61.828  110.006 1.00 56.29  ? 199  GLN F O     1 
ATOM   27372 C  CB    . GLN F 6  199  ? 188.922 62.779  106.778 1.00 53.70  ? 199  GLN F CB    1 
ATOM   27373 C  CG    . GLN F 6  199  ? 189.759 63.650  105.841 1.00 56.19  ? 199  GLN F CG    1 
ATOM   27374 C  CD    . GLN F 6  199  ? 190.092 62.962  104.532 1.00 58.29  ? 199  GLN F CD    1 
ATOM   27375 O  OE1   . GLN F 6  199  ? 190.604 61.842  104.517 1.00 57.06  ? 199  GLN F OE1   1 
ATOM   27376 N  NE2   . GLN F 6  199  ? 189.800 63.629  103.423 1.00 56.35  ? 199  GLN F NE2   1 
ATOM   27377 N  N     . ILE F 6  200  ? 187.900 60.612  108.723 1.00 51.85  ? 200  ILE F N     1 
ATOM   27378 C  CA    . ILE F 6  200  ? 187.069 60.235  109.861 1.00 51.72  ? 200  ILE F CA    1 
ATOM   27379 C  C     . ILE F 6  200  ? 187.878 59.414  110.855 1.00 52.97  ? 200  ILE F C     1 
ATOM   27380 O  O     . ILE F 6  200  ? 187.693 59.531  112.070 1.00 51.72  ? 200  ILE F O     1 
ATOM   27381 C  CB    . ILE F 6  200  ? 185.801 59.491  109.392 1.00 52.40  ? 200  ILE F CB    1 
ATOM   27382 C  CG1   . ILE F 6  200  ? 186.108 58.063  108.948 1.00 51.45  ? 200  ILE F CG1   1 
ATOM   27383 C  CG2   . ILE F 6  200  ? 185.134 60.226  108.243 1.00 50.45  ? 200  ILE F CG2   1 
ATOM   27384 C  CD1   . ILE F 6  200  ? 184.906 57.160  109.004 1.00 50.63  ? 200  ILE F CD1   1 
ATOM   27385 N  N     . CYS F 6  201  ? 188.804 58.590  110.359 1.00 53.01  ? 201  CYS F N     1 
ATOM   27386 C  CA    . CYS F 6  201  ? 189.636 57.793  111.254 1.00 53.12  ? 201  CYS F CA    1 
ATOM   27387 C  C     . CYS F 6  201  ? 190.575 58.681  112.062 1.00 52.98  ? 201  CYS F C     1 
ATOM   27388 O  O     . CYS F 6  201  ? 190.699 58.530  113.281 1.00 50.83  ? 201  CYS F O     1 
ATOM   27389 C  CB    . CYS F 6  201  ? 190.424 56.757  110.450 1.00 53.56  ? 201  CYS F CB    1 
ATOM   27390 S  SG    . CYS F 6  201  ? 189.457 55.315  109.930 1.00 59.43  ? 201  CYS F SG    1 
ATOM   27391 N  N     . PHE F 6  202  ? 191.242 59.624  111.401 1.00 54.67  ? 202  PHE F N     1 
ATOM   27392 C  CA    . PHE F 6  202  ? 192.156 60.504  112.116 1.00 55.54  ? 202  PHE F CA    1 
ATOM   27393 C  C     . PHE F 6  202  ? 191.413 61.317  113.170 1.00 55.30  ? 202  PHE F C     1 
ATOM   27394 O  O     . PHE F 6  202  ? 191.875 61.438  114.312 1.00 54.26  ? 202  PHE F O     1 
ATOM   27395 C  CB    . PHE F 6  202  ? 192.879 61.404  111.113 1.00 54.26  ? 202  PHE F CB    1 
ATOM   27396 C  CG    . PHE F 6  202  ? 193.746 62.453  111.739 1.00 54.87  ? 202  PHE F CG    1 
ATOM   27397 C  CD1   . PHE F 6  202  ? 194.687 62.117  112.698 1.00 55.03  ? 202  PHE F CD1   1 
ATOM   27398 C  CD2   . PHE F 6  202  ? 193.645 63.775  111.339 1.00 52.98  ? 202  PHE F CD2   1 
ATOM   27399 C  CE1   . PHE F 6  202  ? 195.494 63.083  113.265 1.00 56.29  ? 202  PHE F CE1   1 
ATOM   27400 C  CE2   . PHE F 6  202  ? 194.450 64.743  111.903 1.00 54.33  ? 202  PHE F CE2   1 
ATOM   27401 C  CZ    . PHE F 6  202  ? 195.377 64.398  112.865 1.00 55.66  ? 202  PHE F CZ    1 
ATOM   27402 N  N     . PHE F 6  203  ? 190.232 61.836  112.823 1.00 55.68  ? 203  PHE F N     1 
ATOM   27403 C  CA    . PHE F 6  203  ? 189.469 62.633  113.779 1.00 57.45  ? 203  PHE F CA    1 
ATOM   27404 C  C     . PHE F 6  203  ? 188.925 61.782  114.925 1.00 57.11  ? 203  PHE F C     1 
ATOM   27405 O  O     . PHE F 6  203  ? 188.896 62.230  116.078 1.00 55.87  ? 203  PHE F O     1 
ATOM   27406 C  CB    . PHE F 6  203  ? 188.350 63.374  113.053 1.00 56.82  ? 203  PHE F CB    1 
ATOM   27407 C  CG    . PHE F 6  203  ? 188.843 64.529  112.238 1.00 57.72  ? 203  PHE F CG    1 
ATOM   27408 C  CD1   . PHE F 6  203  ? 189.592 65.531  112.829 1.00 55.56  ? 203  PHE F CD1   1 
ATOM   27409 C  CD2   . PHE F 6  203  ? 188.599 64.594  110.876 1.00 56.03  ? 203  PHE F CD2   1 
ATOM   27410 C  CE1   . PHE F 6  203  ? 190.067 66.588  112.081 1.00 55.43  ? 203  PHE F CE1   1 
ATOM   27411 C  CE2   . PHE F 6  203  ? 189.074 65.647  110.123 1.00 56.21  ? 203  PHE F CE2   1 
ATOM   27412 C  CZ    . PHE F 6  203  ? 189.805 66.644  110.725 1.00 55.74  ? 203  PHE F CZ    1 
ATOM   27413 N  N     . GLU F 6  204  ? 188.496 60.551  114.633 1.00 53.60  ? 204  GLU F N     1 
ATOM   27414 C  CA    . GLU F 6  204  ? 187.985 59.679  115.685 1.00 53.18  ? 204  GLU F CA    1 
ATOM   27415 C  C     . GLU F 6  204  ? 189.090 59.262  116.650 1.00 53.74  ? 204  GLU F C     1 
ATOM   27416 O  O     . GLU F 6  204  ? 188.894 59.277  117.871 1.00 52.01  ? 204  GLU F O     1 
ATOM   27417 C  CB    . GLU F 6  204  ? 187.307 58.462  115.056 1.00 53.03  ? 204  GLU F CB    1 
ATOM   27418 C  CG    . GLU F 6  204  ? 187.324 57.185  115.893 1.00 53.25  ? 204  GLU F CG    1 
ATOM   27419 C  CD    . GLU F 6  204  ? 186.546 57.293  117.182 1.00 54.46  ? 204  GLU F CD    1 
ATOM   27420 O  OE1   . GLU F 6  204  ? 185.771 58.260  117.338 1.00 53.12  ? 204  GLU F OE1   1 
ATOM   27421 O  OE2   . GLU F 6  204  ? 186.710 56.398  118.037 1.00 55.49  ? 204  GLU F OE2   1 
ATOM   27422 N  N     . LYS F 6  205  ? 190.260 58.886  116.126 1.00 49.44  ? 205  LYS F N     1 
ATOM   27423 C  CA    . LYS F 6  205  ? 191.402 58.614  116.998 1.00 52.22  ? 205  LYS F CA    1 
ATOM   27424 C  C     . LYS F 6  205  ? 191.814 59.841  117.801 1.00 53.23  ? 205  LYS F C     1 
ATOM   27425 O  O     . LYS F 6  205  ? 192.199 59.716  118.970 1.00 54.06  ? 205  LYS F O     1 
ATOM   27426 C  CB    . LYS F 6  205  ? 192.587 58.063  116.199 1.00 50.57  ? 205  LYS F CB    1 
ATOM   27427 C  CG    . LYS F 6  205  ? 192.644 56.534  115.978 1.00 49.90  ? 205  LYS F CG    1 
ATOM   27428 C  CD    . LYS F 6  205  ? 191.339 55.732  115.895 1.00 51.14  ? 205  LYS F CD    1 
ATOM   27429 C  CE    . LYS F 6  205  ? 190.455 56.054  114.721 1.00 50.09  ? 205  LYS F CE    1 
ATOM   27430 N  NZ    . LYS F 6  205  ? 189.308 55.112  114.634 1.00 50.61  ? 205  LYS F NZ    1 
ATOM   27431 N  N     . LEU F 6  206  ? 191.760 61.034  117.202 1.00 50.62  ? 206  LEU F N     1 
ATOM   27432 C  CA    . LEU F 6  206  ? 192.090 62.228  117.974 1.00 51.16  ? 206  LEU F CA    1 
ATOM   27433 C  C     . LEU F 6  206  ? 191.109 62.445  119.120 1.00 55.05  ? 206  LEU F C     1 
ATOM   27434 O  O     . LEU F 6  206  ? 191.521 62.700  120.257 1.00 54.76  ? 206  LEU F O     1 
ATOM   27435 C  CB    . LEU F 6  206  ? 192.124 63.459  117.073 1.00 52.12  ? 206  LEU F CB    1 
ATOM   27436 C  CG    . LEU F 6  206  ? 192.313 64.758  117.861 1.00 53.32  ? 206  LEU F CG    1 
ATOM   27437 C  CD1   . LEU F 6  206  ? 193.563 64.693  118.724 1.00 52.53  ? 206  LEU F CD1   1 
ATOM   27438 C  CD2   . LEU F 6  206  ? 192.379 65.943  116.922 1.00 53.41  ? 206  LEU F CD2   1 
ATOM   27439 N  N     . TYR F 6  207  ? 189.811 62.340  118.852 1.00 58.48  ? 207  TYR F N     1 
ATOM   27440 C  CA    . TYR F 6  207  ? 188.813 62.718  119.843 1.00 58.26  ? 207  TYR F CA    1 
ATOM   27441 C  C     . TYR F 6  207  ? 188.303 61.544  120.663 1.00 60.36  ? 207  TYR F C     1 
ATOM   27442 O  O     . TYR F 6  207  ? 187.355 61.713  121.437 1.00 59.05  ? 207  TYR F O     1 
ATOM   27443 C  CB    . TYR F 6  207  ? 187.648 63.442  119.167 1.00 56.34  ? 207  TYR F CB    1 
ATOM   27444 C  CG    . TYR F 6  207  ? 188.043 64.819  118.696 1.00 57.90  ? 207  TYR F CG    1 
ATOM   27445 C  CD1   . TYR F 6  207  ? 188.553 65.012  117.423 1.00 59.27  ? 207  TYR F CD1   1 
ATOM   27446 C  CD2   . TYR F 6  207  ? 187.937 65.918  119.532 1.00 58.19  ? 207  TYR F CD2   1 
ATOM   27447 C  CE1   . TYR F 6  207  ? 188.932 66.260  116.988 1.00 60.12  ? 207  TYR F CE1   1 
ATOM   27448 C  CE2   . TYR F 6  207  ? 188.309 67.177  119.102 1.00 58.68  ? 207  TYR F CE2   1 
ATOM   27449 C  CZ    . TYR F 6  207  ? 188.810 67.338  117.827 1.00 60.25  ? 207  TYR F CZ    1 
ATOM   27450 O  OH    . TYR F 6  207  ? 189.188 68.582  117.384 1.00 59.33  ? 207  TYR F OH    1 
ATOM   27451 N  N     . TYR F 6  208  ? 188.903 60.366  120.515 1.00 57.53  ? 208  TYR F N     1 
ATOM   27452 C  CA    . TYR F 6  208  ? 188.625 59.265  121.424 1.00 57.23  ? 208  TYR F CA    1 
ATOM   27453 C  C     . TYR F 6  208  ? 189.271 59.564  122.770 1.00 54.05  ? 208  TYR F C     1 
ATOM   27454 O  O     . TYR F 6  208  ? 190.343 60.171  122.836 1.00 54.18  ? 208  TYR F O     1 
ATOM   27455 C  CB    . TYR F 6  208  ? 189.167 57.956  120.847 1.00 55.40  ? 208  TYR F CB    1 
ATOM   27456 C  CG    . TYR F 6  208  ? 188.685 56.699  121.537 1.00 54.66  ? 208  TYR F CG    1 
ATOM   27457 C  CD1   . TYR F 6  208  ? 187.346 56.531  121.858 1.00 54.62  ? 208  TYR F CD1   1 
ATOM   27458 C  CD2   . TYR F 6  208  ? 189.563 55.669  121.840 1.00 54.34  ? 208  TYR F CD2   1 
ATOM   27459 C  CE1   . TYR F 6  208  ? 186.895 55.379  122.474 1.00 56.57  ? 208  TYR F CE1   1 
ATOM   27460 C  CE2   . TYR F 6  208  ? 189.124 54.509  122.457 1.00 55.87  ? 208  TYR F CE2   1 
ATOM   27461 C  CZ    . TYR F 6  208  ? 187.788 54.368  122.772 1.00 57.47  ? 208  TYR F CZ    1 
ATOM   27462 O  OH    . TYR F 6  208  ? 187.346 53.217  123.387 1.00 53.29  ? 208  TYR F OH    1 
ATOM   27463 N  N     . THR F 6  209  ? 188.606 59.161  123.853 1.00 49.09  ? 209  THR F N     1 
ATOM   27464 C  CA    . THR F 6  209  ? 189.156 59.438  125.177 1.00 52.27  ? 209  THR F CA    1 
ATOM   27465 C  C     . THR F 6  209  ? 190.485 58.722  125.385 1.00 52.76  ? 209  THR F C     1 
ATOM   27466 O  O     . THR F 6  209  ? 191.443 59.311  125.898 1.00 50.39  ? 209  THR F O     1 
ATOM   27467 C  CB    . THR F 6  209  ? 188.160 59.040  126.264 1.00 52.86  ? 209  THR F CB    1 
ATOM   27468 O  OG1   . THR F 6  209  ? 186.840 59.422  125.863 1.00 54.97  ? 209  THR F OG1   1 
ATOM   27469 C  CG2   . THR F 6  209  ? 188.506 59.735  127.575 1.00 49.57  ? 209  THR F CG2   1 
ATOM   27470 N  N     . TYR F 6  210  ? 190.566 57.459  124.982 1.00 54.35  ? 210  TYR F N     1 
ATOM   27471 C  CA    . TYR F 6  210  ? 191.772 56.667  125.138 1.00 52.99  ? 210  TYR F CA    1 
ATOM   27472 C  C     . TYR F 6  210  ? 192.517 56.603  123.805 1.00 52.13  ? 210  TYR F C     1 
ATOM   27473 O  O     . TYR F 6  210  ? 192.113 57.209  122.809 1.00 52.91  ? 210  TYR F O     1 
ATOM   27474 C  CB    . TYR F 6  210  ? 191.419 55.274  125.671 1.00 52.97  ? 210  TYR F CB    1 
ATOM   27475 C  CG    . TYR F 6  210  ? 190.607 55.295  126.950 1.00 53.74  ? 210  TYR F CG    1 
ATOM   27476 C  CD1   . TYR F 6  210  ? 191.207 55.559  128.178 1.00 52.46  ? 210  TYR F CD1   1 
ATOM   27477 C  CD2   . TYR F 6  210  ? 189.245 55.033  126.933 1.00 50.86  ? 210  TYR F CD2   1 
ATOM   27478 C  CE1   . TYR F 6  210  ? 190.466 55.579  129.348 1.00 50.88  ? 210  TYR F CE1   1 
ATOM   27479 C  CE2   . TYR F 6  210  ? 188.501 55.048  128.099 1.00 50.73  ? 210  TYR F CE2   1 
ATOM   27480 C  CZ    . TYR F 6  210  ? 189.113 55.321  129.300 1.00 52.30  ? 210  TYR F CZ    1 
ATOM   27481 O  OH    . TYR F 6  210  ? 188.364 55.332  130.454 1.00 52.20  ? 210  TYR F OH    1 
ATOM   27482 N  N     . SER F 6  211  ? 193.619 55.861  123.782 1.00 49.17  ? 211  SER F N     1 
ATOM   27483 C  CA    . SER F 6  211  ? 194.454 55.715  122.600 1.00 49.90  ? 211  SER F CA    1 
ATOM   27484 C  C     . SER F 6  211  ? 194.601 54.238  122.261 1.00 50.07  ? 211  SER F C     1 
ATOM   27485 O  O     . SER F 6  211  ? 194.676 53.387  123.151 1.00 49.99  ? 211  SER F O     1 
ATOM   27486 C  CB    . SER F 6  211  ? 195.834 56.343  122.819 1.00 48.55  ? 211  SER F CB    1 
ATOM   27487 O  OG    . SER F 6  211  ? 196.505 55.723  123.900 1.00 49.79  ? 211  SER F OG    1 
ATOM   27488 N  N     . ILE F 6  212  ? 194.644 53.935  120.967 1.00 47.09  ? 212  ILE F N     1 
ATOM   27489 C  CA    . ILE F 6  212  ? 194.667 52.555  120.496 1.00 49.10  ? 212  ILE F CA    1 
ATOM   27490 C  C     . ILE F 6  212  ? 195.811 52.375  119.507 1.00 47.94  ? 212  ILE F C     1 
ATOM   27491 O  O     . ILE F 6  212  ? 196.365 53.353  118.996 1.00 50.11  ? 212  ILE F O     1 
ATOM   27492 C  CB    . ILE F 6  212  ? 193.306 52.144  119.887 1.00 49.66  ? 212  ILE F CB    1 
ATOM   27493 C  CG1   . ILE F 6  212  ? 192.747 53.216  118.942 1.00 48.74  ? 212  ILE F CG1   1 
ATOM   27494 C  CG2   . ILE F 6  212  ? 192.300 51.859  120.992 1.00 47.28  ? 212  ILE F CG2   1 
ATOM   27495 C  CD1   . ILE F 6  212  ? 193.426 53.336  117.604 1.00 47.76  ? 212  ILE F CD1   1 
ATOM   27496 N  N     . SER F 6  213  ? 196.169 51.116  119.245 1.00 44.96  ? 213  SER F N     1 
ATOM   27497 C  CA    . SER F 6  213  ? 197.275 50.795  118.345 1.00 47.16  ? 213  SER F CA    1 
ATOM   27498 C  C     . SER F 6  213  ? 196.782 50.620  116.905 1.00 47.86  ? 213  SER F C     1 
ATOM   27499 O  O     . SER F 6  213  ? 197.132 49.669  116.206 1.00 45.73  ? 213  SER F O     1 
ATOM   27500 C  CB    . SER F 6  213  ? 197.999 49.547  118.836 1.00 44.57  ? 213  SER F CB    1 
ATOM   27501 O  OG    . SER F 6  213  ? 197.096 48.473  119.034 1.00 46.18  ? 213  SER F OG    1 
ATOM   27502 N  N     . SER F 6  214  ? 195.950 51.574  116.473 1.00 45.76  ? 214  SER F N     1 
ATOM   27503 C  CA    . SER F 6  214  ? 195.543 51.733  115.076 1.00 46.26  ? 214  SER F CA    1 
ATOM   27504 C  C     . SER F 6  214  ? 194.645 50.608  114.565 1.00 46.44  ? 214  SER F C     1 
ATOM   27505 O  O     . SER F 6  214  ? 194.766 49.457  114.995 1.00 46.10  ? 214  SER F O     1 
ATOM   27506 C  CB    . SER F 6  214  ? 196.775 51.860  114.175 1.00 44.74  ? 214  SER F CB    1 
ATOM   27507 O  OG    . SER F 6  214  ? 197.349 50.590  113.923 1.00 44.14  ? 214  SER F OG    1 
ATOM   27508 N  N     . ASP F 6  215  ? 193.730 50.948  113.651 1.00 49.56  ? 215  ASP F N     1 
ATOM   27509 C  CA    . ASP F 6  215  ? 192.935 49.970  112.901 1.00 49.05  ? 215  ASP F CA    1 
ATOM   27510 C  C     . ASP F 6  215  ? 192.210 48.979  113.805 1.00 50.98  ? 215  ASP F C     1 
ATOM   27511 O  O     . ASP F 6  215  ? 192.159 47.783  113.511 1.00 51.47  ? 215  ASP F O     1 
ATOM   27512 C  CB    . ASP F 6  215  ? 193.800 49.226  111.881 1.00 48.01  ? 215  ASP F CB    1 
ATOM   27513 C  CG    . ASP F 6  215  ? 194.078 50.054  110.638 1.00 51.54  ? 215  ASP F CG    1 
ATOM   27514 O  OD1   . ASP F 6  215  ? 193.255 50.939  110.325 1.00 51.49  ? 215  ASP F OD1   1 
ATOM   27515 O  OD2   . ASP F 6  215  ? 195.119 49.830  109.985 1.00 49.65  ? 215  ASP F OD2   1 
ATOM   27516 N  N     . GLU F 6  216  ? 191.652 49.458  114.922 1.00 54.31  ? 216  GLU F N     1 
ATOM   27517 C  CA    . GLU F 6  216  ? 190.936 48.571  115.831 1.00 54.28  ? 216  GLU F CA    1 
ATOM   27518 C  C     . GLU F 6  216  ? 189.714 49.229  116.464 1.00 55.10  ? 216  GLU F C     1 
ATOM   27519 O  O     . GLU F 6  216  ? 189.285 48.804  117.543 1.00 56.14  ? 216  GLU F O     1 
ATOM   27520 C  CB    . GLU F 6  216  ? 191.881 48.075  116.928 1.00 53.47  ? 216  GLU F CB    1 
ATOM   27521 C  CG    . GLU F 6  216  ? 192.570 46.764  116.607 1.00 53.08  ? 216  GLU F CG    1 
ATOM   27522 C  CD    . GLU F 6  216  ? 192.970 46.010  117.855 1.00 56.21  ? 216  GLU F CD    1 
ATOM   27523 O  OE1   . GLU F 6  216  ? 192.825 46.577  118.958 1.00 57.49  ? 216  GLU F OE1   1 
ATOM   27524 O  OE2   . GLU F 6  216  ? 193.434 44.857  117.735 1.00 55.83  ? 216  GLU F OE2   1 
ATOM   27525 N  N     . ILE F 6  217  ? 189.127 50.237  115.822 1.00 52.43  ? 217  ILE F N     1 
ATOM   27526 C  CA    . ILE F 6  217  ? 188.062 51.013  116.452 1.00 52.91  ? 217  ILE F CA    1 
ATOM   27527 C  C     . ILE F 6  217  ? 186.775 51.041  115.648 1.00 53.26  ? 217  ILE F C     1 
ATOM   27528 O  O     . ILE F 6  217  ? 185.679 51.089  116.243 1.00 51.77  ? 217  ILE F O     1 
ATOM   27529 C  CB    . ILE F 6  217  ? 188.551 52.457  116.722 1.00 50.48  ? 217  ILE F CB    1 
ATOM   27530 C  CG1   . ILE F 6  217  ? 189.461 52.507  117.948 1.00 49.53  ? 217  ILE F CG1   1 
ATOM   27531 C  CG2   . ILE F 6  217  ? 187.387 53.414  116.883 1.00 48.10  ? 217  ILE F CG2   1 
ATOM   27532 C  CD1   . ILE F 6  217  ? 189.026 51.607  119.077 1.00 48.20  ? 217  ILE F CD1   1 
ATOM   27533 N  N     . LEU F 6  218  ? 186.816 50.941  114.323 1.00 54.57  ? 218  LEU F N     1 
ATOM   27534 C  CA    . LEU F 6  218  ? 185.676 51.345  113.519 1.00 53.71  ? 218  LEU F CA    1 
ATOM   27535 C  C     . LEU F 6  218  ? 185.210 50.178  112.664 1.00 55.02  ? 218  LEU F C     1 
ATOM   27536 O  O     . LEU F 6  218  ? 186.026 49.473  112.063 1.00 54.59  ? 218  LEU F O     1 
ATOM   27537 C  CB    . LEU F 6  218  ? 186.048 52.549  112.644 1.00 52.29  ? 218  LEU F CB    1 
ATOM   27538 C  CG    . LEU F 6  218  ? 185.075 53.175  111.646 1.00 54.18  ? 218  LEU F CG    1 
ATOM   27539 C  CD1   . LEU F 6  218  ? 185.553 54.580  111.345 1.00 53.38  ? 218  LEU F CD1   1 
ATOM   27540 C  CD2   . LEU F 6  218  ? 184.914 52.379  110.361 1.00 53.21  ? 218  LEU F CD2   1 
ATOM   27541 N  N     . ASP F 6  219  ? 183.896 49.990  112.611 1.00 53.58  ? 219  ASP F N     1 
ATOM   27542 C  CA    . ASP F 6  219  ? 183.261 49.039  111.704 1.00 55.17  ? 219  ASP F CA    1 
ATOM   27543 C  C     . ASP F 6  219  ? 182.016 49.739  111.168 1.00 55.26  ? 219  ASP F C     1 
ATOM   27544 O  O     . ASP F 6  219  ? 180.920 49.572  111.709 1.00 52.37  ? 219  ASP F O     1 
ATOM   27545 C  CB    . ASP F 6  219  ? 182.928 47.734  112.419 1.00 51.31  ? 219  ASP F CB    1 
ATOM   27546 C  CG    . ASP F 6  219  ? 183.036 46.526  111.508 1.00 52.88  ? 219  ASP F CG    1 
ATOM   27547 O  OD1   . ASP F 6  219  ? 183.104 46.705  110.272 1.00 53.02  ? 219  ASP F OD1   1 
ATOM   27548 O  OD2   . ASP F 6  219  ? 183.072 45.396  112.031 1.00 53.44  ? 219  ASP F OD2   1 
ATOM   27549 N  N     . LEU F 6  220  ? 182.190 50.520  110.099 1.00 52.10  ? 220  LEU F N     1 
ATOM   27550 C  CA    . LEU F 6  220  ? 181.131 51.424  109.657 1.00 51.75  ? 220  LEU F CA    1 
ATOM   27551 C  C     . LEU F 6  220  ? 179.876 50.658  109.248 1.00 51.55  ? 220  LEU F C     1 
ATOM   27552 O  O     . LEU F 6  220  ? 178.753 51.129  109.465 1.00 50.19  ? 220  LEU F O     1 
ATOM   27553 C  CB    . LEU F 6  220  ? 181.645 52.301  108.510 1.00 51.06  ? 220  LEU F CB    1 
ATOM   27554 C  CG    . LEU F 6  220  ? 182.107 51.646  107.201 1.00 51.29  ? 220  LEU F CG    1 
ATOM   27555 C  CD1   . LEU F 6  220  ? 180.963 51.527  106.212 1.00 48.97  ? 220  LEU F CD1   1 
ATOM   27556 C  CD2   . LEU F 6  220  ? 183.278 52.392  106.577 1.00 49.46  ? 220  LEU F CD2   1 
ATOM   27557 N  N     . LYS F 6  221  ? 180.047 49.479  108.650 1.00 52.01  ? 221  LYS F N     1 
ATOM   27558 C  CA    . LYS F 6  221  ? 178.905 48.674  108.232 1.00 51.12  ? 221  LYS F CA    1 
ATOM   27559 C  C     . LYS F 6  221  ? 178.209 47.992  109.405 1.00 50.78  ? 221  LYS F C     1 
ATOM   27560 O  O     . LYS F 6  221  ? 176.974 47.973  109.458 1.00 50.09  ? 221  LYS F O     1 
ATOM   27561 C  CB    . LYS F 6  221  ? 179.357 47.617  107.224 1.00 48.67  ? 221  LYS F CB    1 
ATOM   27562 C  CG    . LYS F 6  221  ? 179.896 48.184  105.928 1.00 48.62  ? 221  LYS F CG    1 
ATOM   27563 C  CD    . LYS F 6  221  ? 180.307 47.077  104.987 1.00 50.10  ? 221  LYS F CD    1 
ATOM   27564 C  CE    . LYS F 6  221  ? 181.051 47.620  103.782 1.00 48.85  ? 221  LYS F CE    1 
ATOM   27565 N  NZ    . LYS F 6  221  ? 181.405 46.525  102.844 1.00 50.33  ? 221  LYS F NZ    1 
ATOM   27566 N  N     . ILE F 6  222  ? 178.973 47.447  110.352 1.00 48.95  ? 222  ILE F N     1 
ATOM   27567 C  CA    . ILE F 6  222  ? 178.415 46.610  111.401 1.00 51.21  ? 222  ILE F CA    1 
ATOM   27568 C  C     . ILE F 6  222  ? 178.382 47.304  112.759 1.00 52.78  ? 222  ILE F C     1 
ATOM   27569 O  O     . ILE F 6  222  ? 177.484 47.018  113.561 1.00 51.04  ? 222  ILE F O     1 
ATOM   27570 C  CB    . ILE F 6  222  ? 179.191 45.278  111.492 1.00 51.55  ? 222  ILE F CB    1 
ATOM   27571 C  CG1   . ILE F 6  222  ? 179.484 44.733  110.092 1.00 49.01  ? 222  ILE F CG1   1 
ATOM   27572 C  CG2   . ILE F 6  222  ? 178.421 44.252  112.323 1.00 49.52  ? 222  ILE F CG2   1 
ATOM   27573 C  CD1   . ILE F 6  222  ? 180.206 43.403  110.093 1.00 47.96  ? 222  ILE F CD1   1 
ATOM   27574 N  N     . TRP F 6  223  ? 179.323 48.208  113.037 1.00 58.15  ? 223  TRP F N     1 
ATOM   27575 C  CA    . TRP F 6  223  ? 179.447 48.871  114.337 1.00 59.67  ? 223  TRP F CA    1 
ATOM   27576 C  C     . TRP F 6  223  ? 179.624 47.838  115.455 1.00 58.73  ? 223  TRP F C     1 
ATOM   27577 O  O     . TRP F 6  223  ? 178.758 47.645  116.311 1.00 56.70  ? 223  TRP F O     1 
ATOM   27578 C  CB    . TRP F 6  223  ? 178.249 49.792  114.609 1.00 58.84  ? 223  TRP F CB    1 
ATOM   27579 C  CG    . TRP F 6  223  ? 177.960 50.792  113.517 1.00 58.79  ? 223  TRP F CG    1 
ATOM   27580 C  CD1   . TRP F 6  223  ? 177.044 50.663  112.508 1.00 57.95  ? 223  TRP F CD1   1 
ATOM   27581 C  CD2   . TRP F 6  223  ? 178.592 52.065  113.320 1.00 59.66  ? 223  TRP F CD2   1 
ATOM   27582 N  NE1   . TRP F 6  223  ? 177.060 51.779  111.706 1.00 60.36  ? 223  TRP F NE1   1 
ATOM   27583 C  CE2   . TRP F 6  223  ? 178.003 52.653  112.181 1.00 61.84  ? 223  TRP F CE2   1 
ATOM   27584 C  CE3   . TRP F 6  223  ? 179.594 52.762  113.993 1.00 58.13  ? 223  TRP F CE3   1 
ATOM   27585 C  CZ2   . TRP F 6  223  ? 178.385 53.905  111.705 1.00 60.03  ? 223  TRP F CZ2   1 
ATOM   27586 C  CZ3   . TRP F 6  223  ? 179.971 54.005  113.521 1.00 59.34  ? 223  TRP F CZ3   1 
ATOM   27587 C  CH2   . TRP F 6  223  ? 179.369 54.563  112.388 1.00 59.36  ? 223  TRP F CH2   1 
ATOM   27588 N  N     . LYS F 6  224  ? 180.767 47.152  115.418 1.00 52.21  ? 224  LYS F N     1 
ATOM   27589 C  CA    . LYS F 6  224  ? 181.054 46.103  116.390 1.00 51.62  ? 224  LYS F CA    1 
ATOM   27590 C  C     . LYS F 6  224  ? 181.782 46.600  117.636 1.00 50.49  ? 224  LYS F C     1 
ATOM   27591 O  O     . LYS F 6  224  ? 181.942 45.822  118.582 1.00 48.84  ? 224  LYS F O     1 
ATOM   27592 C  CB    . LYS F 6  224  ? 181.869 44.986  115.732 1.00 50.97  ? 224  LYS F CB    1 
ATOM   27593 C  CG    . LYS F 6  224  ? 181.044 44.057  114.856 1.00 50.81  ? 224  LYS F CG    1 
ATOM   27594 C  CD    . LYS F 6  224  ? 181.844 42.838  114.431 1.00 52.17  ? 224  LYS F CD    1 
ATOM   27595 C  CE    . LYS F 6  224  ? 180.967 41.811  113.727 1.00 51.67  ? 224  LYS F CE    1 
ATOM   27596 N  NZ    . LYS F 6  224  ? 181.729 40.598  113.327 1.00 49.55  ? 224  LYS F NZ    1 
ATOM   27597 N  N     . GLY F 6  225  ? 182.219 47.859  117.669 1.00 44.02  ? 225  GLY F N     1 
ATOM   27598 C  CA    . GLY F 6  225  ? 182.827 48.422  118.854 1.00 43.17  ? 225  GLY F CA    1 
ATOM   27599 C  C     . GLY F 6  225  ? 184.335 48.256  118.918 1.00 44.74  ? 225  GLY F C     1 
ATOM   27600 O  O     . GLY F 6  225  ? 184.974 47.778  117.977 1.00 46.15  ? 225  GLY F O     1 
ATOM   27601 N  N     . PRO F 6  226  ? 184.935 48.665  120.036 1.00 46.57  ? 226  PRO F N     1 
ATOM   27602 C  CA    . PRO F 6  226  ? 186.394 48.584  120.160 1.00 47.92  ? 226  PRO F CA    1 
ATOM   27603 C  C     . PRO F 6  226  ? 186.838 47.199  120.598 1.00 49.80  ? 226  PRO F C     1 
ATOM   27604 O  O     . PRO F 6  226  ? 186.336 46.642  121.579 1.00 48.09  ? 226  PRO F O     1 
ATOM   27605 C  CB    . PRO F 6  226  ? 186.722 49.635  121.230 1.00 46.77  ? 226  PRO F CB    1 
ATOM   27606 C  CG    . PRO F 6  226  ? 185.443 49.837  122.003 1.00 44.76  ? 226  PRO F CG    1 
ATOM   27607 C  CD    . PRO F 6  226  ? 184.299 49.198  121.253 1.00 45.63  ? 226  PRO F CD    1 
ATOM   27608 N  N     . LYS F 6  227  ? 187.804 46.649  119.866 1.00 51.20  ? 227  LYS F N     1 
ATOM   27609 C  CA    . LYS F 6  227  ? 188.284 45.293  120.125 1.00 50.95  ? 227  LYS F CA    1 
ATOM   27610 C  C     . LYS F 6  227  ? 189.429 45.319  121.137 1.00 51.21  ? 227  LYS F C     1 
ATOM   27611 O  O     . LYS F 6  227  ? 190.481 44.707  120.946 1.00 51.90  ? 227  LYS F O     1 
ATOM   27612 C  CB    . LYS F 6  227  ? 188.728 44.629  118.826 1.00 51.60  ? 227  LYS F CB    1 
ATOM   27613 C  CG    . LYS F 6  227  ? 187.658 44.446  117.770 1.00 50.77  ? 227  LYS F CG    1 
ATOM   27614 C  CD    . LYS F 6  227  ? 188.309 43.936  116.491 1.00 49.78  ? 227  LYS F CD    1 
ATOM   27615 C  CE    . LYS F 6  227  ? 187.366 43.939  115.309 1.00 49.47  ? 227  LYS F CE    1 
ATOM   27616 N  NZ    . LYS F 6  227  ? 188.095 43.569  114.066 1.00 47.52  ? 227  LYS F NZ    1 
ATOM   27617 N  N     . GLY F 6  228  ? 189.208 46.038  122.234 1.00 44.55  ? 228  GLY F N     1 
ATOM   27618 C  CA    . GLY F 6  228  ? 190.249 46.146  123.235 1.00 44.08  ? 228  GLY F CA    1 
ATOM   27619 C  C     . GLY F 6  228  ? 190.131 45.129  124.351 1.00 45.57  ? 228  GLY F C     1 
ATOM   27620 O  O     . GLY F 6  228  ? 189.448 45.366  125.351 1.00 45.39  ? 228  GLY F O     1 
ATOM   27621 N  N     . LYS F 6  229  ? 190.814 43.994  124.179 1.00 44.17  ? 229  LYS F N     1 
ATOM   27622 C  CA    . LYS F 6  229  ? 191.002 42.973  125.216 1.00 45.14  ? 229  LYS F CA    1 
ATOM   27623 C  C     . LYS F 6  229  ? 189.705 42.617  125.945 1.00 42.52  ? 229  LYS F C     1 
ATOM   27624 O  O     . LYS F 6  229  ? 189.732 42.144  127.084 1.00 41.12  ? 229  LYS F O     1 
ATOM   27625 C  CB    . LYS F 6  229  ? 192.087 43.404  126.206 1.00 43.40  ? 229  LYS F CB    1 
ATOM   27626 C  CG    . LYS F 6  229  ? 193.491 43.193  125.658 1.00 40.33  ? 229  LYS F CG    1 
ATOM   27627 C  CD    . LYS F 6  229  ? 194.532 43.061  126.750 1.00 40.91  ? 229  LYS F CD    1 
ATOM   27628 C  CE    . LYS F 6  229  ? 195.902 42.800  126.149 1.00 42.10  ? 229  LYS F CE    1 
ATOM   27629 N  NZ    . LYS F 6  229  ? 196.924 42.523  127.188 1.00 43.27  ? 229  LYS F NZ    1 
ATOM   27630 N  N     . GLU F 6  230  ? 188.566 42.827  125.285 1.00 49.92  ? 230  GLU F N     1 
ATOM   27631 C  CA    . GLU F 6  230  ? 187.244 42.480  125.812 1.00 51.88  ? 230  GLU F CA    1 
ATOM   27632 C  C     . GLU F 6  230  ? 187.054 43.022  127.234 1.00 51.38  ? 230  GLU F C     1 
ATOM   27633 O  O     . GLU F 6  230  ? 186.913 42.279  128.205 1.00 48.01  ? 230  GLU F O     1 
ATOM   27634 C  CB    . GLU F 6  230  ? 187.030 40.964  125.763 1.00 50.57  ? 230  GLU F CB    1 
ATOM   27635 C  CG    . GLU F 6  230  ? 186.728 40.426  124.373 1.00 50.24  ? 230  GLU F CG    1 
ATOM   27636 C  CD    . GLU F 6  230  ? 186.229 38.995  124.397 1.00 50.61  ? 230  GLU F CD    1 
ATOM   27637 O  OE1   . GLU F 6  230  ? 186.183 38.400  125.493 1.00 50.95  ? 230  GLU F OE1   1 
ATOM   27638 O  OE2   . GLU F 6  230  ? 185.883 38.465  123.321 1.00 50.73  ? 230  GLU F OE2   1 
ATOM   27639 N  N     . MET F 6  231  ? 187.056 44.356  127.321 1.00 55.38  ? 231  MET F N     1 
ATOM   27640 C  CA    . MET F 6  231  ? 187.085 45.022  128.623 1.00 54.03  ? 231  MET F CA    1 
ATOM   27641 C  C     . MET F 6  231  ? 185.856 44.685  129.463 1.00 55.21  ? 231  MET F C     1 
ATOM   27642 O  O     . MET F 6  231  ? 185.966 44.480  130.678 1.00 56.48  ? 231  MET F O     1 
ATOM   27643 C  CB    . MET F 6  231  ? 187.220 46.534  128.436 1.00 52.93  ? 231  MET F CB    1 
ATOM   27644 C  CG    . MET F 6  231  ? 188.058 47.208  129.509 1.00 53.61  ? 231  MET F CG    1 
ATOM   27645 S  SD    . MET F 6  231  ? 188.340 48.963  129.216 1.00 63.54  ? 231  MET F SD    1 
ATOM   27646 C  CE    . MET F 6  231  ? 190.131 49.027  129.257 1.00 52.91  ? 231  MET F CE    1 
ATOM   27647 N  N     . SER F 6  232  ? 184.680 44.621  128.842 1.00 53.01  ? 232  SER F N     1 
ATOM   27648 C  CA    . SER F 6  232  ? 183.443 44.283  129.536 1.00 53.09  ? 232  SER F CA    1 
ATOM   27649 C  C     . SER F 6  232  ? 182.960 42.903  129.110 1.00 52.69  ? 232  SER F C     1 
ATOM   27650 O  O     . SER F 6  232  ? 183.167 42.488  127.965 1.00 51.17  ? 232  SER F O     1 
ATOM   27651 C  CB    . SER F 6  232  ? 182.349 45.317  129.259 1.00 49.82  ? 232  SER F CB    1 
ATOM   27652 O  OG    . SER F 6  232  ? 181.741 45.089  127.999 1.00 51.10  ? 232  SER F OG    1 
ATOM   27653 N  N     . ARG F 6  233  ? 182.323 42.191  130.043 1.00 63.41  ? 233  ARG F N     1 
ATOM   27654 C  CA    . ARG F 6  233  ? 181.758 40.878  129.747 1.00 64.71  ? 233  ARG F CA    1 
ATOM   27655 C  C     . ARG F 6  233  ? 180.399 40.953  129.054 1.00 64.38  ? 233  ARG F C     1 
ATOM   27656 O  O     . ARG F 6  233  ? 179.913 39.920  128.578 1.00 63.59  ? 233  ARG F O     1 
ATOM   27657 C  CB    . ARG F 6  233  ? 181.640 40.052  131.030 1.00 62.61  ? 233  ARG F CB    1 
ATOM   27658 C  CG    . ARG F 6  233  ? 182.953 39.440  131.500 1.00 62.05  ? 233  ARG F CG    1 
ATOM   27659 C  CD    . ARG F 6  233  ? 182.730 38.481  132.659 1.00 63.17  ? 233  ARG F CD    1 
ATOM   27660 N  NE    . ARG F 6  233  ? 183.979 38.081  133.297 1.00 66.58  ? 233  ARG F NE    1 
ATOM   27661 C  CZ    . ARG F 6  233  ? 184.055 37.345  134.398 1.00 64.49  ? 233  ARG F CZ    1 
ATOM   27662 N  NH1   . ARG F 6  233  ? 182.970 36.892  135.002 1.00 61.89  ? 233  ARG F NH1   1 
ATOM   27663 N  NH2   . ARG F 6  233  ? 185.249 37.051  134.902 1.00 63.90  ? 233  ARG F NH2   1 
ATOM   27664 N  N     . LEU F 6  234  ? 179.776 42.128  128.985 1.00 56.20  ? 234  LEU F N     1 
ATOM   27665 C  CA    . LEU F 6  234  ? 178.528 42.319  128.255 1.00 55.32  ? 234  LEU F CA    1 
ATOM   27666 C  C     . LEU F 6  234  ? 178.793 43.126  126.991 1.00 56.38  ? 234  LEU F C     1 
ATOM   27667 O  O     . LEU F 6  234  ? 179.501 44.139  127.031 1.00 56.30  ? 234  LEU F O     1 
ATOM   27668 C  CB    . LEU F 6  234  ? 177.475 43.024  129.113 1.00 55.20  ? 234  LEU F CB    1 
ATOM   27669 C  CG    . LEU F 6  234  ? 177.287 42.580  130.564 1.00 56.19  ? 234  LEU F CG    1 
ATOM   27670 C  CD1   . LEU F 6  234  ? 176.436 43.593  131.317 1.00 53.31  ? 234  LEU F CD1   1 
ATOM   27671 C  CD2   . LEU F 6  234  ? 176.663 41.199  130.624 1.00 54.23  ? 234  LEU F CD2   1 
ATOM   27672 N  N     . LYS F 6  235  ? 178.236 42.670  125.879 1.00 55.31  ? 235  LYS F N     1 
ATOM   27673 C  CA    . LYS F 6  235  ? 178.411 43.364  124.609 1.00 55.70  ? 235  LYS F CA    1 
ATOM   27674 C  C     . LYS F 6  235  ? 177.629 44.673  124.609 1.00 54.32  ? 235  LYS F C     1 
ATOM   27675 O  O     . LYS F 6  235  ? 176.527 44.730  125.170 1.00 53.30  ? 235  LYS F O     1 
ATOM   27676 C  CB    . LYS F 6  235  ? 177.946 42.480  123.456 1.00 53.11  ? 235  LYS F CB    1 
ATOM   27677 C  CG    . LYS F 6  235  ? 178.866 41.320  123.160 1.00 51.88  ? 235  LYS F CG    1 
ATOM   27678 C  CD    . LYS F 6  235  ? 178.234 40.369  122.157 1.00 53.32  ? 235  LYS F CD    1 
ATOM   27679 C  CE    . LYS F 6  235  ? 178.978 39.046  122.108 1.00 53.43  ? 235  LYS F CE    1 
ATOM   27680 N  NZ    . LYS F 6  235  ? 178.213 38.012  121.367 1.00 52.91  ? 235  LYS F NZ    1 
ATOM   27681 N  N     . PRO F 6  236  ? 178.153 45.736  124.002 1.00 52.94  ? 236  PRO F N     1 
ATOM   27682 C  CA    . PRO F 6  236  ? 177.383 46.978  123.906 1.00 54.29  ? 236  PRO F CA    1 
ATOM   27683 C  C     . PRO F 6  236  ? 176.106 46.762  123.110 1.00 55.35  ? 236  PRO F C     1 
ATOM   27684 O  O     . PRO F 6  236  ? 176.087 46.045  122.108 1.00 55.55  ? 236  PRO F O     1 
ATOM   27685 C  CB    . PRO F 6  236  ? 178.338 47.936  123.183 1.00 53.81  ? 236  PRO F CB    1 
ATOM   27686 C  CG    . PRO F 6  236  ? 179.314 47.047  122.483 1.00 53.17  ? 236  PRO F CG    1 
ATOM   27687 C  CD    . PRO F 6  236  ? 179.468 45.844  123.349 1.00 52.85  ? 236  PRO F CD    1 
ATOM   27688 N  N     . CYS F 6  237  ? 175.033 47.399  123.563 1.00 56.78  ? 237  CYS F N     1 
ATOM   27689 C  CA    . CYS F 6  237  ? 173.727 47.255  122.938 1.00 54.39  ? 237  CYS F CA    1 
ATOM   27690 C  C     . CYS F 6  237  ? 173.471 48.425  122.002 1.00 55.24  ? 237  CYS F C     1 
ATOM   27691 O  O     . CYS F 6  237  ? 173.582 49.588  122.399 1.00 52.07  ? 237  CYS F O     1 
ATOM   27692 C  CB    . CYS F 6  237  ? 172.618 47.179  123.988 1.00 54.46  ? 237  CYS F CB    1 
ATOM   27693 S  SG    . CYS F 6  237  ? 170.946 47.281  123.310 1.00 61.93  ? 237  CYS F SG    1 
ATOM   27694 N  N     . ASN F 6  238  ? 173.126 48.109  120.757 1.00 54.94  ? 238  ASN F N     1 
ATOM   27695 C  CA    . ASN F 6  238  ? 172.811 49.148  119.791 1.00 52.89  ? 238  ASN F CA    1 
ATOM   27696 C  C     . ASN F 6  238  ? 171.511 49.832  120.187 1.00 55.31  ? 238  ASN F C     1 
ATOM   27697 O  O     . ASN F 6  238  ? 170.499 49.171  120.438 1.00 53.75  ? 238  ASN F O     1 
ATOM   27698 C  CB    . ASN F 6  238  ? 172.710 48.555  118.385 1.00 51.61  ? 238  ASN F CB    1 
ATOM   27699 C  CG    . ASN F 6  238  ? 172.750 49.618  117.298 1.00 54.69  ? 238  ASN F CG    1 
ATOM   27700 O  OD1   . ASN F 6  238  ? 171.849 50.448  117.192 1.00 53.61  ? 238  ASN F OD1   1 
ATOM   27701 N  ND2   . ASN F 6  238  ? 173.808 49.606  116.496 1.00 54.31  ? 238  ASN F ND2   1 
ATOM   27702 N  N     . VAL F 6  239  ? 171.547 51.163  120.265 1.00 53.30  ? 239  VAL F N     1 
ATOM   27703 C  CA    . VAL F 6  239  ? 170.359 51.907  120.665 1.00 54.47  ? 239  VAL F CA    1 
ATOM   27704 C  C     . VAL F 6  239  ? 169.288 51.824  119.587 1.00 54.49  ? 239  VAL F C     1 
ATOM   27705 O  O     . VAL F 6  239  ? 168.102 51.632  119.883 1.00 50.87  ? 239  VAL F O     1 
ATOM   27706 C  CB    . VAL F 6  239  ? 170.725 53.366  120.984 1.00 52.51  ? 239  VAL F CB    1 
ATOM   27707 C  CG1   . VAL F 6  239  ? 169.521 54.255  120.773 1.00 51.79  ? 239  VAL F CG1   1 
ATOM   27708 C  CG2   . VAL F 6  239  ? 171.247 53.487  122.405 1.00 51.19  ? 239  VAL F CG2   1 
ATOM   27709 N  N     . LEU F 6  240  ? 169.688 51.974  118.323 1.00 52.86  ? 240  LEU F N     1 
ATOM   27710 C  CA    . LEU F 6  240  ? 168.725 51.947  117.229 1.00 54.20  ? 240  LEU F CA    1 
ATOM   27711 C  C     . LEU F 6  240  ? 168.019 50.599  117.147 1.00 57.74  ? 240  LEU F C     1 
ATOM   27712 O  O     . LEU F 6  240  ? 166.796 50.540  116.962 1.00 55.76  ? 240  LEU F O     1 
ATOM   27713 C  CB    . LEU F 6  240  ? 169.435 52.274  115.916 1.00 53.24  ? 240  LEU F CB    1 
ATOM   27714 C  CG    . LEU F 6  240  ? 168.683 52.067  114.606 1.00 54.85  ? 240  LEU F CG    1 
ATOM   27715 C  CD1   . LEU F 6  240  ? 168.968 53.231  113.671 1.00 54.30  ? 240  LEU F CD1   1 
ATOM   27716 C  CD2   . LEU F 6  240  ? 169.077 50.741  113.962 1.00 53.42  ? 240  LEU F CD2   1 
ATOM   27717 N  N     . SER F 6  241  ? 168.772 49.505  117.290 1.00 55.61  ? 241  SER F N     1 
ATOM   27718 C  CA    . SER F 6  241  ? 168.162 48.179  117.284 1.00 55.44  ? 241  SER F CA    1 
ATOM   27719 C  C     . SER F 6  241  ? 167.216 48.007  118.464 1.00 55.52  ? 241  SER F C     1 
ATOM   27720 O  O     . SER F 6  241  ? 166.138 47.417  118.326 1.00 54.82  ? 241  SER F O     1 
ATOM   27721 C  CB    . SER F 6  241  ? 169.241 47.099  117.310 1.00 55.53  ? 241  SER F CB    1 
ATOM   27722 O  OG    . SER F 6  241  ? 169.859 47.040  118.582 1.00 58.40  ? 241  SER F OG    1 
ATOM   27723 N  N     . PHE F 6  242  ? 167.607 48.514  119.635 1.00 53.22  ? 242  PHE F N     1 
ATOM   27724 C  CA    . PHE F 6  242  ? 166.740 48.417  120.804 1.00 55.96  ? 242  PHE F CA    1 
ATOM   27725 C  C     . PHE F 6  242  ? 165.438 49.177  120.590 1.00 55.35  ? 242  PHE F C     1 
ATOM   27726 O  O     . PHE F 6  242  ? 164.366 48.702  120.977 1.00 54.17  ? 242  PHE F O     1 
ATOM   27727 C  CB    . PHE F 6  242  ? 167.467 48.933  122.043 1.00 55.27  ? 242  PHE F CB    1 
ATOM   27728 C  CG    . PHE F 6  242  ? 166.709 48.721  123.318 1.00 55.51  ? 242  PHE F CG    1 
ATOM   27729 C  CD1   . PHE F 6  242  ? 165.916 47.600  123.487 1.00 55.97  ? 242  PHE F CD1   1 
ATOM   27730 C  CD2   . PHE F 6  242  ? 166.790 49.638  124.348 1.00 55.25  ? 242  PHE F CD2   1 
ATOM   27731 C  CE1   . PHE F 6  242  ? 165.218 47.401  124.660 1.00 55.63  ? 242  PHE F CE1   1 
ATOM   27732 C  CE2   . PHE F 6  242  ? 166.094 49.442  125.524 1.00 55.39  ? 242  PHE F CE2   1 
ATOM   27733 C  CZ    . PHE F 6  242  ? 165.309 48.325  125.679 1.00 54.22  ? 242  PHE F CZ    1 
ATOM   27734 N  N     . LEU F 6  243  ? 165.511 50.363  119.983 1.00 53.05  ? 243  LEU F N     1 
ATOM   27735 C  CA    . LEU F 6  243  ? 164.297 51.116  119.681 1.00 56.26  ? 243  LEU F CA    1 
ATOM   27736 C  C     . LEU F 6  243  ? 163.430 50.395  118.658 1.00 54.63  ? 243  LEU F C     1 
ATOM   27737 O  O     . LEU F 6  243  ? 162.202 50.360  118.791 1.00 51.61  ? 243  LEU F O     1 
ATOM   27738 C  CB    . LEU F 6  243  ? 164.657 52.514  119.184 1.00 56.59  ? 243  LEU F CB    1 
ATOM   27739 C  CG    . LEU F 6  243  ? 165.203 53.452  120.254 1.00 55.98  ? 243  LEU F CG    1 
ATOM   27740 C  CD1   . LEU F 6  243  ? 166.034 54.554  119.629 1.00 53.69  ? 243  LEU F CD1   1 
ATOM   27741 C  CD2   . LEU F 6  243  ? 164.035 54.034  121.026 1.00 53.74  ? 243  LEU F CD2   1 
ATOM   27742 N  N     . TYR F 6  244  ? 164.049 49.817  117.628 1.00 54.61  ? 244  TYR F N     1 
ATOM   27743 C  CA    . TYR F 6  244  ? 163.276 49.088  116.630 1.00 56.18  ? 244  TYR F CA    1 
ATOM   27744 C  C     . TYR F 6  244  ? 162.601 47.859  117.227 1.00 56.15  ? 244  TYR F C     1 
ATOM   27745 O  O     . TYR F 6  244  ? 161.502 47.488  116.800 1.00 54.76  ? 244  TYR F O     1 
ATOM   27746 C  CB    . TYR F 6  244  ? 164.175 48.698  115.461 1.00 54.78  ? 244  TYR F CB    1 
ATOM   27747 C  CG    . TYR F 6  244  ? 164.259 49.755  114.387 1.00 55.24  ? 244  TYR F CG    1 
ATOM   27748 C  CD1   . TYR F 6  244  ? 163.154 50.068  113.612 1.00 55.90  ? 244  TYR F CD1   1 
ATOM   27749 C  CD2   . TYR F 6  244  ? 165.440 50.446  114.155 1.00 56.48  ? 244  TYR F CD2   1 
ATOM   27750 C  CE1   . TYR F 6  244  ? 163.223 51.037  112.628 1.00 57.48  ? 244  TYR F CE1   1 
ATOM   27751 C  CE2   . TYR F 6  244  ? 165.519 51.414  113.174 1.00 57.19  ? 244  TYR F CE2   1 
ATOM   27752 C  CZ    . TYR F 6  244  ? 164.410 51.706  112.414 1.00 56.38  ? 244  TYR F CZ    1 
ATOM   27753 O  OH    . TYR F 6  244  ? 164.483 52.671  111.440 1.00 53.55  ? 244  TYR F OH    1 
ATOM   27754 N  N     . ASP F 6  245  ? 163.241 47.214  118.205 1.00 48.31  ? 245  ASP F N     1 
ATOM   27755 C  CA    . ASP F 6  245  ? 162.616 46.074  118.868 1.00 50.56  ? 245  ASP F CA    1 
ATOM   27756 C  C     . ASP F 6  245  ? 161.519 46.519  119.829 1.00 50.93  ? 245  ASP F C     1 
ATOM   27757 O  O     . ASP F 6  245  ? 160.450 45.901  119.886 1.00 48.10  ? 245  ASP F O     1 
ATOM   27758 C  CB    . ASP F 6  245  ? 163.670 45.250  119.605 1.00 51.85  ? 245  ASP F CB    1 
ATOM   27759 C  CG    . ASP F 6  245  ? 164.686 44.627  118.668 1.00 52.31  ? 245  ASP F CG    1 
ATOM   27760 O  OD1   . ASP F 6  245  ? 164.398 44.506  117.461 1.00 52.58  ? 245  ASP F OD1   1 
ATOM   27761 O  OD2   . ASP F 6  245  ? 165.774 44.246  119.146 1.00 53.05  ? 245  ASP F OD2   1 
ATOM   27762 N  N     . ALA F 6  246  ? 161.764 47.583  120.597 1.00 47.54  ? 246  ALA F N     1 
ATOM   27763 C  CA    . ALA F 6  246  ? 160.761 48.097  121.521 1.00 49.38  ? 246  ALA F CA    1 
ATOM   27764 C  C     . ALA F 6  246  ? 159.588 48.742  120.793 1.00 49.77  ? 246  ALA F C     1 
ATOM   27765 O  O     . ALA F 6  246  ? 158.555 49.008  121.418 1.00 46.98  ? 246  ALA F O     1 
ATOM   27766 C  CB    . ALA F 6  246  ? 161.403 49.094  122.487 1.00 46.56  ? 246  ALA F CB    1 
ATOM   27767 N  N     . LEU F 6  247  ? 159.742 49.026  119.497 1.00 46.91  ? 247  LEU F N     1 
ATOM   27768 C  CA    . LEU F 6  247  ? 158.590 49.349  118.664 1.00 45.38  ? 247  LEU F CA    1 
ATOM   27769 C  C     . LEU F 6  247  ? 157.588 48.203  118.655 1.00 45.32  ? 247  LEU F C     1 
ATOM   27770 O  O     . LEU F 6  247  ? 156.380 48.419  118.807 1.00 47.23  ? 247  LEU F O     1 
ATOM   27771 C  CB    . LEU F 6  247  ? 159.048 49.663  117.239 1.00 47.85  ? 247  LEU F CB    1 
ATOM   27772 C  CG    . LEU F 6  247  ? 159.123 51.125  116.792 1.00 47.08  ? 247  LEU F CG    1 
ATOM   27773 C  CD1   . LEU F 6  247  ? 160.272 51.335  115.819 1.00 45.30  ? 247  LEU F CD1   1 
ATOM   27774 C  CD2   . LEU F 6  247  ? 157.809 51.533  116.149 1.00 44.44  ? 247  LEU F CD2   1 
ATOM   27775 N  N     . LYS F 6  248  ? 158.073 46.976  118.490 1.00 44.67  ? 248  LYS F N     1 
ATOM   27776 C  CA    . LYS F 6  248  ? 157.236 45.785  118.467 1.00 47.70  ? 248  LYS F CA    1 
ATOM   27777 C  C     . LYS F 6  248  ? 157.090 45.142  119.840 1.00 52.22  ? 248  LYS F C     1 
ATOM   27778 O  O     . LYS F 6  248  ? 156.449 44.090  119.950 1.00 49.66  ? 248  LYS F O     1 
ATOM   27779 C  CB    . LYS F 6  248  ? 157.806 44.771  117.464 1.00 47.69  ? 248  LYS F CB    1 
ATOM   27780 C  CG    . LYS F 6  248  ? 158.926 43.904  118.015 1.00 47.53  ? 248  LYS F CG    1 
ATOM   27781 C  CD    . LYS F 6  248  ? 160.117 43.851  117.064 1.00 48.43  ? 248  LYS F CD    1 
ATOM   27782 C  CE    . LYS F 6  248  ? 159.791 43.124  115.768 1.00 47.74  ? 248  LYS F CE    1 
ATOM   27783 N  NZ    . LYS F 6  248  ? 161.018 42.573  115.123 1.00 46.17  ? 248  LYS F NZ    1 
ATOM   27784 N  N     . ASN F 6  249  ? 157.659 45.755  120.882 1.00 50.99  ? 249  ASN F N     1 
ATOM   27785 C  CA    . ASN F 6  249  ? 157.558 45.271  122.259 1.00 50.08  ? 249  ASN F CA    1 
ATOM   27786 C  C     . ASN F 6  249  ? 158.130 43.858  122.396 1.00 49.90  ? 249  ASN F C     1 
ATOM   27787 O  O     . ASN F 6  249  ? 157.414 42.886  122.651 1.00 48.91  ? 249  ASN F O     1 
ATOM   27788 C  CB    . ASN F 6  249  ? 156.112 45.331  122.763 1.00 47.74  ? 249  ASN F CB    1 
ATOM   27789 C  CG    . ASN F 6  249  ? 155.717 46.712  123.239 1.00 48.98  ? 249  ASN F CG    1 
ATOM   27790 O  OD1   . ASN F 6  249  ? 156.567 47.563  123.488 1.00 49.40  ? 249  ASN F OD1   1 
ATOM   27791 N  ND2   . ASN F 6  249  ? 154.418 46.935  123.389 1.00 48.69  ? 249  ASN F ND2   1 
ATOM   27792 N  N     . LYS F 6  250  ? 159.447 43.757  122.202 1.00 53.07  ? 250  LYS F N     1 
ATOM   27793 C  CA    . LYS F 6  250  ? 160.158 42.504  122.400 1.00 54.52  ? 250  LYS F CA    1 
ATOM   27794 C  C     . LYS F 6  250  ? 161.189 42.545  123.518 1.00 53.94  ? 250  LYS F C     1 
ATOM   27795 O  O     . LYS F 6  250  ? 161.587 41.478  124.000 1.00 53.15  ? 250  LYS F O     1 
ATOM   27796 C  CB    . LYS F 6  250  ? 160.851 42.064  121.101 1.00 51.96  ? 250  LYS F CB    1 
ATOM   27797 C  CG    . LYS F 6  250  ? 159.954 41.296  120.149 1.00 51.90  ? 250  LYS F CG    1 
ATOM   27798 C  CD    . LYS F 6  250  ? 160.755 40.717  118.997 1.00 53.90  ? 250  LYS F CD    1 
ATOM   27799 C  CE    . LYS F 6  250  ? 159.875 39.925  118.054 1.00 52.89  ? 250  LYS F CE    1 
ATOM   27800 N  NZ    . LYS F 6  250  ? 160.644 39.383  116.900 1.00 50.95  ? 250  LYS F NZ    1 
ATOM   27801 N  N     . ASN F 6  251  ? 161.634 43.725  123.943 1.00 56.31  ? 251  ASN F N     1 
ATOM   27802 C  CA    . ASN F 6  251  ? 162.584 43.846  125.038 1.00 56.90  ? 251  ASN F CA    1 
ATOM   27803 C  C     . ASN F 6  251  ? 162.146 44.954  125.984 1.00 58.26  ? 251  ASN F C     1 
ATOM   27804 O  O     . ASN F 6  251  ? 161.436 45.887  125.601 1.00 58.59  ? 251  ASN F O     1 
ATOM   27805 C  CB    . ASN F 6  251  ? 164.009 44.132  124.541 1.00 56.69  ? 251  ASN F CB    1 
ATOM   27806 C  CG    . ASN F 6  251  ? 164.730 42.884  124.073 1.00 58.00  ? 251  ASN F CG    1 
ATOM   27807 O  OD1   . ASN F 6  251  ? 164.344 41.764  124.405 1.00 57.23  ? 251  ASN F OD1   1 
ATOM   27808 N  ND2   . ASN F 6  251  ? 165.801 43.074  123.314 1.00 56.98  ? 251  ASN F ND2   1 
ATOM   27809 N  N     . SER F 6  252  ? 162.600 44.846  127.229 1.00 52.88  ? 252  SER F N     1 
ATOM   27810 C  CA    . SER F 6  252  ? 162.287 45.803  128.278 1.00 51.25  ? 252  SER F CA    1 
ATOM   27811 C  C     . SER F 6  252  ? 163.458 46.759  128.461 1.00 53.41  ? 252  SER F C     1 
ATOM   27812 O  O     . SER F 6  252  ? 164.621 46.363  128.332 1.00 51.97  ? 252  SER F O     1 
ATOM   27813 C  CB    . SER F 6  252  ? 161.976 45.085  129.593 1.00 51.70  ? 252  SER F CB    1 
ATOM   27814 O  OG    . SER F 6  252  ? 161.653 46.001  130.619 1.00 49.61  ? 252  SER F OG    1 
ATOM   27815 N  N     . SER F 6  253  ? 163.146 48.019  128.759 1.00 57.15  ? 253  SER F N     1 
ATOM   27816 C  CA    . SER F 6  253  ? 164.145 49.073  128.870 1.00 54.92  ? 253  SER F CA    1 
ATOM   27817 C  C     . SER F 6  253  ? 164.499 49.378  130.321 1.00 54.91  ? 253  SER F C     1 
ATOM   27818 O  O     . SER F 6  253  ? 165.196 50.355  130.604 1.00 56.14  ? 253  SER F O     1 
ATOM   27819 C  CB    . SER F 6  253  ? 163.662 50.340  128.165 1.00 55.17  ? 253  SER F CB    1 
ATOM   27820 O  OG    . SER F 6  253  ? 164.465 51.457  128.510 1.00 57.12  ? 253  SER F OG    1 
ATOM   27821 N  N     . LEU F 6  254  ? 164.038 48.546  131.246 1.00 50.58  ? 254  LEU F N     1 
ATOM   27822 C  CA    . LEU F 6  254  ? 164.268 48.782  132.660 1.00 52.14  ? 254  LEU F CA    1 
ATOM   27823 C  C     . LEU F 6  254  ? 165.711 48.458  133.033 1.00 53.18  ? 254  LEU F C     1 
ATOM   27824 O  O     . LEU F 6  254  ? 166.378 47.639  132.395 1.00 52.49  ? 254  LEU F O     1 
ATOM   27825 C  CB    . LEU F 6  254  ? 163.308 47.947  133.512 1.00 51.83  ? 254  LEU F CB    1 
ATOM   27826 C  CG    . LEU F 6  254  ? 161.835 47.926  133.098 1.00 53.70  ? 254  LEU F CG    1 
ATOM   27827 C  CD1   . LEU F 6  254  ? 161.001 47.161  134.116 1.00 49.69  ? 254  LEU F CD1   1 
ATOM   27828 C  CD2   . LEU F 6  254  ? 161.293 49.329  132.902 1.00 51.16  ? 254  LEU F CD2   1 
ATOM   27829 N  N     . GLY F 6  255  ? 166.187 49.118  134.090 1.00 48.88  ? 255  GLY F N     1 
ATOM   27830 C  CA    . GLY F 6  255  ? 167.514 48.886  134.621 1.00 49.82  ? 255  GLY F CA    1 
ATOM   27831 C  C     . GLY F 6  255  ? 168.395 50.118  134.488 1.00 51.37  ? 255  GLY F C     1 
ATOM   27832 O  O     . GLY F 6  255  ? 167.915 51.218  134.188 1.00 50.22  ? 255  GLY F O     1 
ATOM   27833 N  N     . PHE F 6  256  ? 169.694 49.913  134.693 1.00 60.85  ? 256  PHE F N     1 
ATOM   27834 C  CA    . PHE F 6  256  ? 170.680 50.985  134.684 1.00 60.46  ? 256  PHE F CA    1 
ATOM   27835 C  C     . PHE F 6  256  ? 171.332 51.066  133.312 1.00 61.58  ? 256  PHE F C     1 
ATOM   27836 O  O     . PHE F 6  256  ? 171.669 50.035  132.718 1.00 61.93  ? 256  PHE F O     1 
ATOM   27837 C  CB    . PHE F 6  256  ? 171.754 50.765  135.752 1.00 60.96  ? 256  PHE F CB    1 
ATOM   27838 C  CG    . PHE F 6  256  ? 171.248 50.866  137.162 1.00 61.86  ? 256  PHE F CG    1 
ATOM   27839 C  CD1   . PHE F 6  256  ? 171.245 52.084  137.826 1.00 61.27  ? 256  PHE F CD1   1 
ATOM   27840 C  CD2   . PHE F 6  256  ? 170.806 49.739  137.837 1.00 58.94  ? 256  PHE F CD2   1 
ATOM   27841 C  CE1   . PHE F 6  256  ? 170.792 52.181  139.132 1.00 60.82  ? 256  PHE F CE1   1 
ATOM   27842 C  CE2   . PHE F 6  256  ? 170.353 49.827  139.142 1.00 59.60  ? 256  PHE F CE2   1 
ATOM   27843 C  CZ    . PHE F 6  256  ? 170.346 51.051  139.790 1.00 60.29  ? 256  PHE F CZ    1 
ATOM   27844 N  N     . TRP F 6  257  ? 171.510 52.286  132.815 1.00 65.87  ? 257  TRP F N     1 
ATOM   27845 C  CA    . TRP F 6  257  ? 172.139 52.531  131.525 1.00 66.42  ? 257  TRP F CA    1 
ATOM   27846 C  C     . TRP F 6  257  ? 173.317 53.474  131.729 1.00 66.68  ? 257  TRP F C     1 
ATOM   27847 O  O     . TRP F 6  257  ? 173.306 54.292  132.656 1.00 66.25  ? 257  TRP F O     1 
ATOM   27848 C  CB    . TRP F 6  257  ? 171.146 53.142  130.534 1.00 66.03  ? 257  TRP F CB    1 
ATOM   27849 C  CG    . TRP F 6  257  ? 170.309 52.137  129.796 1.00 67.61  ? 257  TRP F CG    1 
ATOM   27850 C  CD1   . TRP F 6  257  ? 169.397 51.277  130.338 1.00 66.88  ? 257  TRP F CD1   1 
ATOM   27851 C  CD2   . TRP F 6  257  ? 170.334 51.860  128.391 1.00 67.85  ? 257  TRP F CD2   1 
ATOM   27852 N  NE1   . TRP F 6  257  ? 168.831 50.504  129.355 1.00 67.70  ? 257  TRP F NE1   1 
ATOM   27853 C  CE2   . TRP F 6  257  ? 169.392 50.838  128.151 1.00 68.13  ? 257  TRP F CE2   1 
ATOM   27854 C  CE3   . TRP F 6  257  ? 171.050 52.384  127.312 1.00 65.57  ? 257  TRP F CE3   1 
ATOM   27855 C  CZ2   . TRP F 6  257  ? 169.152 50.329  126.877 1.00 65.69  ? 257  TRP F CZ2   1 
ATOM   27856 C  CZ3   . TRP F 6  257  ? 170.810 51.876  126.048 1.00 67.20  ? 257  TRP F CZ3   1 
ATOM   27857 C  CH2   . TRP F 6  257  ? 169.870 50.858  125.842 1.00 67.05  ? 257  TRP F CH2   1 
ATOM   27858 N  N     . ALA F 6  258  ? 174.333 53.358  130.874 1.00 54.70  ? 258  ALA F N     1 
ATOM   27859 C  CA    . ALA F 6  258  ? 175.463 54.275  130.922 1.00 54.20  ? 258  ALA F CA    1 
ATOM   27860 C  C     . ALA F 6  258  ? 176.206 54.256  129.596 1.00 53.81  ? 258  ALA F C     1 
ATOM   27861 O  O     . ALA F 6  258  ? 176.085 53.312  128.811 1.00 54.69  ? 258  ALA F O     1 
ATOM   27862 C  CB    . ALA F 6  258  ? 176.432 53.931  132.057 1.00 52.55  ? 258  ALA F CB    1 
ATOM   27863 N  N     . ARG F 6  259  ? 176.987 55.309  129.362 1.00 52.79  ? 259  ARG F N     1 
ATOM   27864 C  CA    . ARG F 6  259  ? 177.835 55.431  128.176 1.00 53.39  ? 259  ARG F CA    1 
ATOM   27865 C  C     . ARG F 6  259  ? 179.236 55.831  128.623 1.00 55.29  ? 259  ARG F C     1 
ATOM   27866 O  O     . ARG F 6  259  ? 179.552 57.023  128.730 1.00 55.81  ? 259  ARG F O     1 
ATOM   27867 C  CB    . ARG F 6  259  ? 177.252 56.435  127.182 1.00 52.15  ? 259  ARG F CB    1 
ATOM   27868 C  CG    . ARG F 6  259  ? 175.954 55.963  126.543 1.00 52.01  ? 259  ARG F CG    1 
ATOM   27869 C  CD    . ARG F 6  259  ? 175.631 56.756  125.300 1.00 50.64  ? 259  ARG F CD    1 
ATOM   27870 N  NE    . ARG F 6  259  ? 176.570 56.462  124.227 1.00 53.38  ? 259  ARG F NE    1 
ATOM   27871 C  CZ    . ARG F 6  259  ? 176.716 57.198  123.136 1.00 56.00  ? 259  ARG F CZ    1 
ATOM   27872 N  NH1   . ARG F 6  259  ? 175.990 58.285  122.934 1.00 55.01  ? 259  ARG F NH1   1 
ATOM   27873 N  NH2   . ARG F 6  259  ? 177.611 56.834  122.223 1.00 53.50  ? 259  ARG F NH2   1 
ATOM   27874 N  N     . PRO F 6  260  ? 180.101 54.856  128.893 1.00 52.01  ? 260  PRO F N     1 
ATOM   27875 C  CA    . PRO F 6  260  ? 181.442 55.157  129.416 1.00 49.73  ? 260  PRO F CA    1 
ATOM   27876 C  C     . PRO F 6  260  ? 182.297 55.878  128.389 1.00 48.76  ? 260  PRO F C     1 
ATOM   27877 O  O     . PRO F 6  260  ? 182.034 55.795  127.181 1.00 46.81  ? 260  PRO F O     1 
ATOM   27878 C  CB    . PRO F 6  260  ? 182.015 53.768  129.738 1.00 49.98  ? 260  PRO F CB    1 
ATOM   27879 C  CG    . PRO F 6  260  ? 181.219 52.820  128.900 1.00 51.34  ? 260  PRO F CG    1 
ATOM   27880 C  CD    . PRO F 6  260  ? 179.853 53.410  128.779 1.00 50.36  ? 260  PRO F CD    1 
ATOM   27881 N  N     . PRO F 6  261  ? 183.329 56.602  128.835 1.00 52.24  ? 261  PRO F N     1 
ATOM   27882 C  CA    . PRO F 6  261  ? 184.211 57.296  127.881 1.00 52.52  ? 261  PRO F CA    1 
ATOM   27883 C  C     . PRO F 6  261  ? 184.877 56.371  126.881 1.00 51.02  ? 261  PRO F C     1 
ATOM   27884 O  O     . PRO F 6  261  ? 185.170 56.809  125.762 1.00 51.29  ? 261  PRO F O     1 
ATOM   27885 C  CB    . PRO F 6  261  ? 185.246 57.977  128.788 1.00 49.88  ? 261  PRO F CB    1 
ATOM   27886 C  CG    . PRO F 6  261  ? 184.583 58.070  130.120 1.00 49.94  ? 261  PRO F CG    1 
ATOM   27887 C  CD    . PRO F 6  261  ? 183.718 56.859  130.231 1.00 49.17  ? 261  PRO F CD    1 
ATOM   27888 N  N     . ASN F 6  262  ? 185.137 55.113  127.245 1.00 50.66  ? 262  ASN F N     1 
ATOM   27889 C  CA    . ASN F 6  262  ? 185.629 54.153  126.262 1.00 49.88  ? 262  ASN F CA    1 
ATOM   27890 C  C     . ASN F 6  262  ? 184.591 53.884  125.183 1.00 49.73  ? 262  ASN F C     1 
ATOM   27891 O  O     . ASN F 6  262  ? 184.950 53.639  124.026 1.00 48.20  ? 262  ASN F O     1 
ATOM   27892 C  CB    . ASN F 6  262  ? 186.040 52.851  126.956 1.00 49.54  ? 262  ASN F CB    1 
ATOM   27893 C  CG    . ASN F 6  262  ? 184.880 51.880  127.133 1.00 48.87  ? 262  ASN F CG    1 
ATOM   27894 O  OD1   . ASN F 6  262  ? 184.503 51.158  126.208 1.00 48.54  ? 262  ASN F OD1   1 
ATOM   27895 N  ND2   . ASN F 6  262  ? 184.309 51.861  128.331 1.00 48.72  ? 262  ASN F ND2   1 
ATOM   27896 N  N     . LEU F 6  263  ? 183.309 53.923  125.537 1.00 51.71  ? 263  LEU F N     1 
ATOM   27897 C  CA    . LEU F 6  263  ? 182.257 53.674  124.565 1.00 51.92  ? 263  LEU F CA    1 
ATOM   27898 C  C     . LEU F 6  263  ? 182.202 54.809  123.548 1.00 51.55  ? 263  LEU F C     1 
ATOM   27899 O  O     . LEU F 6  263  ? 182.287 55.991  123.895 1.00 51.06  ? 263  LEU F O     1 
ATOM   27900 C  CB    . LEU F 6  263  ? 180.910 53.525  125.268 1.00 49.63  ? 263  LEU F CB    1 
ATOM   27901 C  CG    . LEU F 6  263  ? 179.739 53.040  124.417 1.00 51.45  ? 263  LEU F CG    1 
ATOM   27902 C  CD1   . LEU F 6  263  ? 179.467 51.569  124.694 1.00 50.78  ? 263  LEU F CD1   1 
ATOM   27903 C  CD2   . LEU F 6  263  ? 178.514 53.886  124.689 1.00 51.16  ? 263  LEU F CD2   1 
ATOM   27904 N  N     . LEU F 6  264  ? 182.054 54.439  122.279 1.00 48.85  ? 264  LEU F N     1 
ATOM   27905 C  CA    . LEU F 6  264  ? 182.207 55.395  121.191 1.00 49.71  ? 264  LEU F CA    1 
ATOM   27906 C  C     . LEU F 6  264  ? 181.017 56.348  121.180 1.00 51.06  ? 264  LEU F C     1 
ATOM   27907 O  O     . LEU F 6  264  ? 179.863 55.914  121.089 1.00 47.47  ? 264  LEU F O     1 
ATOM   27908 C  CB    . LEU F 6  264  ? 182.344 54.664  119.857 1.00 49.14  ? 264  LEU F CB    1 
ATOM   27909 C  CG    . LEU F 6  264  ? 182.653 55.541  118.644 1.00 51.64  ? 264  LEU F CG    1 
ATOM   27910 C  CD1   . LEU F 6  264  ? 183.601 56.668  119.037 1.00 48.15  ? 264  LEU F CD1   1 
ATOM   27911 C  CD2   . LEU F 6  264  ? 183.246 54.717  117.513 1.00 47.75  ? 264  LEU F CD2   1 
ATOM   27912 N  N     . LYS F 6  265  ? 181.304 57.651  121.265 1.00 53.36  ? 265  LYS F N     1 
ATOM   27913 C  CA    . LYS F 6  265  ? 180.239 58.638  121.412 1.00 52.27  ? 265  LYS F CA    1 
ATOM   27914 C  C     . LYS F 6  265  ? 179.445 58.796  120.124 1.00 52.28  ? 265  LYS F C     1 
ATOM   27915 O  O     . LYS F 6  265  ? 178.252 59.120  120.159 1.00 53.51  ? 265  LYS F O     1 
ATOM   27916 C  CB    . LYS F 6  265  ? 180.820 59.983  121.853 1.00 52.22  ? 265  LYS F CB    1 
ATOM   27917 C  CG    . LYS F 6  265  ? 181.297 60.022  123.300 1.00 51.78  ? 265  LYS F CG    1 
ATOM   27918 C  CD    . LYS F 6  265  ? 182.368 61.087  123.498 1.00 52.61  ? 265  LYS F CD    1 
ATOM   27919 C  CE    . LYS F 6  265  ? 183.642 60.513  124.106 1.00 52.75  ? 265  LYS F CE    1 
ATOM   27920 N  NZ    . LYS F 6  265  ? 184.553 59.957  123.065 1.00 54.10  ? 265  LYS F NZ    1 
ATOM   27921 N  N     . SER F 6  266  ? 180.088 58.584  118.975 1.00 46.36  ? 266  SER F N     1 
ATOM   27922 C  CA    . SER F 6  266  ? 179.381 58.680  117.705 1.00 49.41  ? 266  SER F CA    1 
ATOM   27923 C  C     . SER F 6  266  ? 178.449 57.501  117.452 1.00 49.99  ? 266  SER F C     1 
ATOM   27924 O  O     . SER F 6  266  ? 177.302 57.715  117.046 1.00 48.84  ? 266  SER F O     1 
ATOM   27925 C  CB    . SER F 6  266  ? 180.380 58.783  116.551 1.00 49.87  ? 266  SER F CB    1 
ATOM   27926 O  OG    . SER F 6  266  ? 181.176 57.615  116.464 1.00 49.51  ? 266  SER F OG    1 
ATOM   27927 N  N     . SER F 6  267  ? 178.906 56.273  117.703 1.00 52.11  ? 267  SER F N     1 
ATOM   27928 C  CA    . SER F 6  267  ? 178.176 55.071  117.330 1.00 50.92  ? 267  SER F CA    1 
ATOM   27929 C  C     . SER F 6  267  ? 176.938 54.896  118.203 1.00 52.75  ? 267  SER F C     1 
ATOM   27930 O  O     . SER F 6  267  ? 176.885 55.397  119.328 1.00 52.86  ? 267  SER F O     1 
ATOM   27931 C  CB    . SER F 6  267  ? 179.086 53.854  117.451 1.00 50.71  ? 267  SER F CB    1 
ATOM   27932 O  OG    . SER F 6  267  ? 180.250 54.013  116.663 1.00 50.48  ? 267  SER F OG    1 
ATOM   27933 N  N     . PRO F 6  268  ? 175.915 54.176  117.704 1.00 53.37  ? 268  PRO F N     1 
ATOM   27934 C  CA    . PRO F 6  268  ? 174.660 54.063  118.461 1.00 52.97  ? 268  PRO F CA    1 
ATOM   27935 C  C     . PRO F 6  268  ? 174.721 53.013  119.557 1.00 52.98  ? 268  PRO F C     1 
ATOM   27936 O  O     . PRO F 6  268  ? 173.685 52.613  120.098 1.00 51.06  ? 268  PRO F O     1 
ATOM   27937 C  CB    . PRO F 6  268  ? 173.641 53.677  117.384 1.00 50.12  ? 268  PRO F CB    1 
ATOM   27938 C  CG    . PRO F 6  268  ? 174.446 52.903  116.398 1.00 50.66  ? 268  PRO F CG    1 
ATOM   27939 C  CD    . PRO F 6  268  ? 175.827 53.506  116.393 1.00 51.87  ? 268  PRO F CD    1 
ATOM   27940 N  N     . LEU F 6  269  ? 175.923 52.547  119.882 1.00 51.22  ? 269  LEU F N     1 
ATOM   27941 C  CA    . LEU F 6  269  ? 176.069 51.526  120.906 1.00 51.83  ? 269  LEU F CA    1 
ATOM   27942 C  C     . LEU F 6  269  ? 176.010 52.148  122.298 1.00 50.02  ? 269  LEU F C     1 
ATOM   27943 O  O     . LEU F 6  269  ? 176.333 53.320  122.500 1.00 49.59  ? 269  LEU F O     1 
ATOM   27944 C  CB    . LEU F 6  269  ? 177.372 50.743  120.703 1.00 52.21  ? 269  LEU F CB    1 
ATOM   27945 C  CG    . LEU F 6  269  ? 178.718 51.247  121.237 1.00 50.98  ? 269  LEU F CG    1 
ATOM   27946 C  CD1   . LEU F 6  269  ? 179.835 50.303  120.828 1.00 49.44  ? 269  LEU F CD1   1 
ATOM   27947 C  CD2   . LEU F 6  269  ? 179.034 52.650  120.760 1.00 47.07  ? 269  LEU F CD2   1 
ATOM   27948 N  N     . ALA F 6  270  ? 175.564 51.344  123.260 1.00 54.28  ? 270  ALA F N     1 
ATOM   27949 C  CA    . ALA F 6  270  ? 175.401 51.783  124.639 1.00 57.97  ? 270  ALA F CA    1 
ATOM   27950 C  C     . ALA F 6  270  ? 175.349 50.549  125.531 1.00 56.69  ? 270  ALA F C     1 
ATOM   27951 O  O     . ALA F 6  270  ? 175.339 49.413  125.051 1.00 54.77  ? 270  ALA F O     1 
ATOM   27952 C  CB    . ALA F 6  270  ? 174.147 52.646  124.810 1.00 54.61  ? 270  ALA F CB    1 
ATOM   27953 N  N     . TYR F 6  271  ? 175.316 50.787  126.841 1.00 60.74  ? 271  TYR F N     1 
ATOM   27954 C  CA    . TYR F 6  271  ? 175.385 49.721  127.833 1.00 62.87  ? 271  TYR F CA    1 
ATOM   27955 C  C     . TYR F 6  271  ? 174.099 49.683  128.651 1.00 62.85  ? 271  TYR F C     1 
ATOM   27956 O  O     . TYR F 6  271  ? 173.577 50.733  129.042 1.00 61.22  ? 271  TYR F O     1 
ATOM   27957 C  CB    . TYR F 6  271  ? 176.594 49.916  128.753 1.00 60.73  ? 271  TYR F CB    1 
ATOM   27958 C  CG    . TYR F 6  271  ? 177.856 49.257  128.241 1.00 61.08  ? 271  TYR F CG    1 
ATOM   27959 C  CD1   . TYR F 6  271  ? 177.801 48.057  127.540 1.00 60.70  ? 271  TYR F CD1   1 
ATOM   27960 C  CD2   . TYR F 6  271  ? 179.102 49.833  128.460 1.00 59.81  ? 271  TYR F CD2   1 
ATOM   27961 C  CE1   . TYR F 6  271  ? 178.953 47.450  127.068 1.00 60.81  ? 271  TYR F CE1   1 
ATOM   27962 C  CE2   . TYR F 6  271  ? 180.261 49.235  127.993 1.00 60.61  ? 271  TYR F CE2   1 
ATOM   27963 C  CZ    . TYR F 6  271  ? 180.180 48.042  127.297 1.00 61.93  ? 271  TYR F CZ    1 
ATOM   27964 O  OH    . TYR F 6  271  ? 181.323 47.439  126.830 1.00 60.16  ? 271  TYR F OH    1 
ATOM   27965 N  N     . GLN F 6  272  ? 173.586 48.476  128.897 1.00 61.35  ? 272  GLN F N     1 
ATOM   27966 C  CA    . GLN F 6  272  ? 172.425 48.277  129.756 1.00 60.21  ? 272  GLN F CA    1 
ATOM   27967 C  C     . GLN F 6  272  ? 172.720 47.193  130.784 1.00 59.49  ? 272  GLN F C     1 
ATOM   27968 O  O     . GLN F 6  272  ? 173.345 46.176  130.468 1.00 59.24  ? 272  GLN F O     1 
ATOM   27969 C  CB    . GLN F 6  272  ? 171.168 47.902  128.954 1.00 57.17  ? 272  GLN F CB    1 
ATOM   27970 C  CG    . GLN F 6  272  ? 171.242 46.571  128.229 1.00 58.62  ? 272  GLN F CG    1 
ATOM   27971 C  CD    . GLN F 6  272  ? 170.290 46.496  127.053 1.00 61.93  ? 272  GLN F CD    1 
ATOM   27972 O  OE1   . GLN F 6  272  ? 170.562 45.829  126.055 1.00 59.23  ? 272  GLN F OE1   1 
ATOM   27973 N  NE2   . GLN F 6  272  ? 169.154 47.172  127.174 1.00 61.88  ? 272  GLN F NE2   1 
ATOM   27974 N  N     . GLN F 6  273  ? 172.276 47.422  132.018 1.00 59.60  ? 273  GLN F N     1 
ATOM   27975 C  CA    . GLN F 6  273  ? 172.480 46.481  133.110 1.00 59.17  ? 273  GLN F CA    1 
ATOM   27976 C  C     . GLN F 6  273  ? 171.255 46.481  134.013 1.00 59.91  ? 273  GLN F C     1 
ATOM   27977 O  O     . GLN F 6  273  ? 170.614 47.512  134.228 1.00 58.40  ? 273  GLN F O     1 
ATOM   27978 C  CB    . GLN F 6  273  ? 173.732 46.820  133.940 1.00 57.12  ? 273  GLN F CB    1 
ATOM   27979 C  CG    . GLN F 6  273  ? 175.049 46.775  133.172 1.00 58.12  ? 273  GLN F CG    1 
ATOM   27980 C  CD    . GLN F 6  273  ? 176.233 47.224  134.012 1.00 59.91  ? 273  GLN F CD    1 
ATOM   27981 O  OE1   . GLN F 6  273  ? 176.066 47.742  135.116 1.00 58.11  ? 273  GLN F OE1   1 
ATOM   27982 N  NE2   . GLN F 6  273  ? 177.438 47.029  133.487 1.00 58.69  ? 273  GLN F NE2   1 
ATOM   27983 N  N     . ASP F 6  274  ? 170.946 45.302  134.557 1.00 59.93  ? 274  ASP F N     1 
ATOM   27984 C  CA    . ASP F 6  274  ? 169.882 45.182  135.546 1.00 59.66  ? 274  ASP F CA    1 
ATOM   27985 C  C     . ASP F 6  274  ? 170.342 45.564  136.946 1.00 59.62  ? 274  ASP F C     1 
ATOM   27986 O  O     . ASP F 6  274  ? 169.506 45.671  137.849 1.00 59.96  ? 274  ASP F O     1 
ATOM   27987 C  CB    . ASP F 6  274  ? 169.324 43.757  135.552 1.00 59.03  ? 274  ASP F CB    1 
ATOM   27988 C  CG    . ASP F 6  274  ? 168.059 43.622  134.722 1.00 60.95  ? 274  ASP F CG    1 
ATOM   27989 O  OD1   . ASP F 6  274  ? 167.422 44.660  134.437 1.00 60.90  ? 274  ASP F OD1   1 
ATOM   27990 O  OD2   . ASP F 6  274  ? 167.706 42.482  134.348 1.00 59.41  ? 274  ASP F OD2   1 
ATOM   27991 N  N     . GLN F 6  275  ? 171.643 45.764  137.148 1.00 56.65  ? 275  GLN F N     1 
ATOM   27992 C  CA    . GLN F 6  275  ? 172.177 46.220  138.421 1.00 58.03  ? 275  GLN F CA    1 
ATOM   27993 C  C     . GLN F 6  275  ? 173.169 47.348  138.180 1.00 60.65  ? 275  GLN F C     1 
ATOM   27994 O  O     . GLN F 6  275  ? 173.743 47.473  137.095 1.00 59.47  ? 275  GLN F O     1 
ATOM   27995 C  CB    . GLN F 6  275  ? 172.869 45.091  139.204 1.00 56.32  ? 275  GLN F CB    1 
ATOM   27996 C  CG    . GLN F 6  275  ? 174.211 44.640  138.637 1.00 57.08  ? 275  GLN F CG    1 
ATOM   27997 C  CD    . GLN F 6  275  ? 174.073 43.616  137.526 1.00 58.43  ? 275  GLN F CD    1 
ATOM   27998 O  OE1   . GLN F 6  275  ? 172.987 43.413  136.982 1.00 56.78  ? 275  GLN F OE1   1 
ATOM   27999 N  NE2   . GLN F 6  275  ? 175.178 42.959  137.189 1.00 55.43  ? 275  GLN F NE2   1 
ATOM   28000 N  N     . ASN F 6  276  ? 173.359 48.171  139.211 1.00 56.97  ? 276  ASN F N     1 
ATOM   28001 C  CA    . ASN F 6  276  ? 174.306 49.276  139.153 1.00 55.97  ? 276  ASN F CA    1 
ATOM   28002 C  C     . ASN F 6  276  ? 175.720 48.793  139.455 1.00 55.11  ? 276  ASN F C     1 
ATOM   28003 O  O     . ASN F 6  276  ? 176.099 48.646  140.620 1.00 54.85  ? 276  ASN F O     1 
ATOM   28004 C  CB    . ASN F 6  276  ? 173.889 50.376  140.133 1.00 54.13  ? 276  ASN F CB    1 
ATOM   28005 C  CG    . ASN F 6  276  ? 174.830 51.565  140.114 1.00 55.85  ? 276  ASN F CG    1 
ATOM   28006 O  OD1   . ASN F 6  276  ? 175.427 51.884  139.086 1.00 56.31  ? 276  ASN F OD1   1 
ATOM   28007 N  ND2   . ASN F 6  276  ? 174.965 52.228  141.256 1.00 53.38  ? 276  ASN F ND2   1 
ATOM   28008 N  N     . SER F 6  277  ? 176.501 48.526  138.410 1.00 51.16  ? 277  SER F N     1 
ATOM   28009 C  CA    . SER F 6  277  ? 177.891 48.115  138.553 1.00 52.19  ? 277  SER F CA    1 
ATOM   28010 C  C     . SER F 6  277  ? 178.859 49.099  137.910 1.00 52.34  ? 277  SER F C     1 
ATOM   28011 O  O     . SER F 6  277  ? 180.074 48.879  137.953 1.00 50.34  ? 277  SER F O     1 
ATOM   28012 C  CB    . SER F 6  277  ? 178.090 46.719  137.958 1.00 51.74  ? 277  SER F CB    1 
ATOM   28013 O  OG    . SER F 6  277  ? 177.790 46.711  136.572 1.00 50.57  ? 277  SER F OG    1 
ATOM   28014 N  N     . PHE F 6  278  ? 178.352 50.180  137.324 1.00 59.94  ? 278  PHE F N     1 
ATOM   28015 C  CA    . PHE F 6  278  ? 179.191 51.142  136.626 1.00 60.18  ? 278  PHE F CA    1 
ATOM   28016 C  C     . PHE F 6  278  ? 180.093 51.888  137.602 1.00 60.03  ? 278  PHE F C     1 
ATOM   28017 O  O     . PHE F 6  278  ? 179.686 52.227  138.717 1.00 59.81  ? 278  PHE F O     1 
ATOM   28018 C  CB    . PHE F 6  278  ? 178.319 52.132  135.854 1.00 58.91  ? 278  PHE F CB    1 
ATOM   28019 C  CG    . PHE F 6  278  ? 177.557 51.510  134.721 1.00 60.13  ? 278  PHE F CG    1 
ATOM   28020 C  CD1   . PHE F 6  278  ? 178.197 51.178  133.537 1.00 58.86  ? 278  PHE F CD1   1 
ATOM   28021 C  CD2   . PHE F 6  278  ? 176.206 51.229  134.851 1.00 60.59  ? 278  PHE F CD2   1 
ATOM   28022 C  CE1   . PHE F 6  278  ? 177.499 50.601  132.494 1.00 59.07  ? 278  PHE F CE1   1 
ATOM   28023 C  CE2   . PHE F 6  278  ? 175.500 50.648  133.814 1.00 61.28  ? 278  PHE F CE2   1 
ATOM   28024 C  CZ    . PHE F 6  278  ? 176.148 50.334  132.632 1.00 61.19  ? 278  PHE F CZ    1 
ATOM   28025 N  N     . ASN F 6  279  ? 181.328 52.137  137.174 1.00 54.11  ? 279  ASN F N     1 
ATOM   28026 C  CA    . ASN F 6  279  ? 182.305 52.867  137.983 1.00 54.02  ? 279  ASN F CA    1 
ATOM   28027 C  C     . ASN F 6  279  ? 182.148 54.374  137.778 1.00 53.75  ? 279  ASN F C     1 
ATOM   28028 O  O     . ASN F 6  279  ? 183.059 55.079  137.349 1.00 52.93  ? 279  ASN F O     1 
ATOM   28029 C  CB    . ASN F 6  279  ? 183.716 52.403  137.647 1.00 52.85  ? 279  ASN F CB    1 
ATOM   28030 C  CG    . ASN F 6  279  ? 183.975 50.979  138.082 1.00 54.64  ? 279  ASN F CG    1 
ATOM   28031 O  OD1   . ASN F 6  279  ? 183.181 50.393  138.816 1.00 55.37  ? 279  ASN F OD1   1 
ATOM   28032 N  ND2   . ASN F 6  279  ? 185.085 50.410  137.627 1.00 52.39  ? 279  ASN F ND2   1 
ATOM   28033 N  N     . ALA F 6  280  ? 180.953 54.859  138.098 1.00 51.64  ? 280  ALA F N     1 
ATOM   28034 C  CA    . ALA F 6  280  ? 180.622 56.265  137.939 1.00 53.00  ? 280  ALA F CA    1 
ATOM   28035 C  C     . ALA F 6  280  ? 180.846 57.020  139.242 1.00 53.29  ? 280  ALA F C     1 
ATOM   28036 O  O     . ALA F 6  280  ? 180.420 56.590  140.317 1.00 53.34  ? 280  ALA F O     1 
ATOM   28037 C  CB    . ALA F 6  280  ? 179.172 56.433  137.485 1.00 49.85  ? 280  ALA F CB    1 
ATOM   28038 N  N     . THR F 6  281  ? 181.508 58.170  139.131 1.00 53.21  ? 281  THR F N     1 
ATOM   28039 C  CA    . THR F 6  281  ? 181.806 59.003  140.287 1.00 51.78  ? 281  THR F CA    1 
ATOM   28040 C  C     . THR F 6  281  ? 180.571 59.686  140.865 1.00 51.52  ? 281  THR F C     1 
ATOM   28041 O  O     . THR F 6  281  ? 180.622 60.154  142.008 1.00 50.25  ? 281  THR F O     1 
ATOM   28042 C  CB    . THR F 6  281  ? 182.840 60.068  139.904 1.00 51.20  ? 281  THR F CB    1 
ATOM   28043 O  OG1   . THR F 6  281  ? 182.492 60.637  138.636 1.00 52.10  ? 281  THR F OG1   1 
ATOM   28044 C  CG2   . THR F 6  281  ? 184.227 59.457  139.799 1.00 50.26  ? 281  THR F CG2   1 
ATOM   28045 N  N     . GLU F 6  282  ? 179.467 59.734  140.121 1.00 56.77  ? 282  GLU F N     1 
ATOM   28046 C  CA    . GLU F 6  282  ? 178.280 60.486  140.501 1.00 57.50  ? 282  GLU F CA    1 
ATOM   28047 C  C     . GLU F 6  282  ? 177.127 59.536  140.798 1.00 58.19  ? 282  GLU F C     1 
ATOM   28048 O  O     . GLU F 6  282  ? 177.074 58.416  140.282 1.00 59.57  ? 282  GLU F O     1 
ATOM   28049 C  CB    . GLU F 6  282  ? 177.875 61.467  139.395 1.00 57.15  ? 282  GLU F CB    1 
ATOM   28050 C  CG    . GLU F 6  282  ? 178.736 62.721  139.339 1.00 59.03  ? 282  GLU F CG    1 
ATOM   28051 C  CD    . GLU F 6  282  ? 178.301 63.690  138.254 1.00 60.14  ? 282  GLU F CD    1 
ATOM   28052 O  OE1   . GLU F 6  282  ? 177.375 63.351  137.485 1.00 56.68  ? 282  GLU F OE1   1 
ATOM   28053 O  OE2   . GLU F 6  282  ? 178.882 64.795  138.179 1.00 59.05  ? 282  GLU F OE2   1 
ATOM   28054 N  N     . LEU F 6  283  ? 176.208 59.990  141.643 1.00 53.06  ? 283  LEU F N     1 
ATOM   28055 C  CA    . LEU F 6  283  ? 175.075 59.159  142.021 1.00 50.89  ? 283  LEU F CA    1 
ATOM   28056 C  C     . LEU F 6  283  ? 174.139 58.953  140.833 1.00 51.73  ? 283  LEU F C     1 
ATOM   28057 O  O     . LEU F 6  283  ? 173.907 59.883  140.053 1.00 52.34  ? 283  LEU F O     1 
ATOM   28058 C  CB    . LEU F 6  283  ? 174.308 59.785  143.187 1.00 49.44  ? 283  LEU F CB    1 
ATOM   28059 C  CG    . LEU F 6  283  ? 175.052 59.791  144.525 1.00 51.66  ? 283  LEU F CG    1 
ATOM   28060 C  CD1   . LEU F 6  283  ? 174.389 60.722  145.532 1.00 49.72  ? 283  LEU F CD1   1 
ATOM   28061 C  CD2   . LEU F 6  283  ? 175.152 58.376  145.077 1.00 49.97  ? 283  LEU F CD2   1 
ATOM   28062 N  N     . PRO F 6  284  ? 173.602 57.746  140.659 1.00 52.89  ? 284  PRO F N     1 
ATOM   28063 C  CA    . PRO F 6  284  ? 172.631 57.519  139.582 1.00 51.58  ? 284  PRO F CA    1 
ATOM   28064 C  C     . PRO F 6  284  ? 171.376 58.350  139.794 1.00 52.01  ? 284  PRO F C     1 
ATOM   28065 O  O     . PRO F 6  284  ? 170.956 58.602  140.925 1.00 50.73  ? 284  PRO F O     1 
ATOM   28066 C  CB    . PRO F 6  284  ? 172.333 56.018  139.679 1.00 50.64  ? 284  PRO F CB    1 
ATOM   28067 C  CG    . PRO F 6  284  ? 173.513 55.434  140.416 1.00 50.68  ? 284  PRO F CG    1 
ATOM   28068 C  CD    . PRO F 6  284  ? 173.949 56.505  141.375 1.00 50.75  ? 284  PRO F CD    1 
ATOM   28069 N  N     . ILE F 6  285  ? 170.770 58.768  138.687 1.00 52.42  ? 285  ILE F N     1 
ATOM   28070 C  CA    . ILE F 6  285  ? 169.594 59.632  138.707 1.00 52.05  ? 285  ILE F CA    1 
ATOM   28071 C  C     . ILE F 6  285  ? 168.371 58.781  138.388 1.00 51.82  ? 285  ILE F C     1 
ATOM   28072 O  O     . ILE F 6  285  ? 168.331 58.101  137.355 1.00 52.20  ? 285  ILE F O     1 
ATOM   28073 C  CB    . ILE F 6  285  ? 169.738 60.790  137.708 1.00 54.40  ? 285  ILE F CB    1 
ATOM   28074 C  CG1   . ILE F 6  285  ? 171.083 61.493  137.909 1.00 50.63  ? 285  ILE F CG1   1 
ATOM   28075 C  CG2   . ILE F 6  285  ? 168.581 61.773  137.864 1.00 50.67  ? 285  ILE F CG2   1 
ATOM   28076 C  CD1   . ILE F 6  285  ? 171.482 62.407  136.773 1.00 49.20  ? 285  ILE F CD1   1 
ATOM   28077 N  N     . ILE F 6  286  ? 167.368 58.826  139.261 1.00 49.00  ? 286  ILE F N     1 
ATOM   28078 C  CA    . ILE F 6  286  ? 166.183 57.987  139.112 1.00 52.84  ? 286  ILE F CA    1 
ATOM   28079 C  C     . ILE F 6  286  ? 165.181 58.712  138.219 1.00 52.51  ? 286  ILE F C     1 
ATOM   28080 O  O     . ILE F 6  286  ? 164.732 59.816  138.544 1.00 50.07  ? 286  ILE F O     1 
ATOM   28081 C  CB    . ILE F 6  286  ? 165.564 57.659  140.479 1.00 50.93  ? 286  ILE F CB    1 
ATOM   28082 C  CG1   . ILE F 6  286  ? 166.576 56.931  141.365 1.00 49.68  ? 286  ILE F CG1   1 
ATOM   28083 C  CG2   . ILE F 6  286  ? 164.323 56.800  140.302 1.00 47.99  ? 286  ILE F CG2   1 
ATOM   28084 C  CD1   . ILE F 6  286  ? 166.100 56.703  142.780 1.00 48.63  ? 286  ILE F CD1   1 
ATOM   28085 N  N     . CYS F 6  287  ? 164.813 58.086  137.101 1.00 55.85  ? 287  CYS F N     1 
ATOM   28086 C  CA    . CYS F 6  287  ? 163.952 58.742  136.127 1.00 55.91  ? 287  CYS F CA    1 
ATOM   28087 C  C     . CYS F 6  287  ? 163.313 57.699  135.222 1.00 56.74  ? 287  CYS F C     1 
ATOM   28088 O  O     . CYS F 6  287  ? 163.504 56.492  135.389 1.00 55.92  ? 287  CYS F O     1 
ATOM   28089 C  CB    . CYS F 6  287  ? 164.726 59.767  135.295 1.00 55.58  ? 287  CYS F CB    1 
ATOM   28090 S  SG    . CYS F 6  287  ? 166.169 59.098  134.439 1.00 65.23  ? 287  CYS F SG    1 
ATOM   28091 N  N     . SER F 6  288  ? 162.548 58.189  134.252 1.00 51.34  ? 288  SER F N     1 
ATOM   28092 C  CA    . SER F 6  288  ? 161.826 57.353  133.308 1.00 51.75  ? 288  SER F CA    1 
ATOM   28093 C  C     . SER F 6  288  ? 162.591 57.245  131.989 1.00 53.87  ? 288  SER F C     1 
ATOM   28094 O  O     . SER F 6  288  ? 163.516 58.010  131.706 1.00 53.23  ? 288  SER F O     1 
ATOM   28095 C  CB    . SER F 6  288  ? 160.421 57.907  133.072 1.00 50.11  ? 288  SER F CB    1 
ATOM   28096 O  OG    . SER F 6  288  ? 159.703 57.115  132.142 1.00 50.50  ? 288  SER F OG    1 
ATOM   28097 N  N     . ALA F 6  289  ? 162.186 56.264  131.178 1.00 51.17  ? 289  ALA F N     1 
ATOM   28098 C  CA    . ALA F 6  289  ? 162.963 55.889  130.001 1.00 50.27  ? 289  ALA F CA    1 
ATOM   28099 C  C     . ALA F 6  289  ? 162.907 56.937  128.896 1.00 50.31  ? 289  ALA F C     1 
ATOM   28100 O  O     . ALA F 6  289  ? 163.814 56.988  128.057 1.00 50.67  ? 289  ALA F O     1 
ATOM   28101 C  CB    . ALA F 6  289  ? 162.477 54.547  129.463 1.00 51.04  ? 289  ALA F CB    1 
ATOM   28102 N  N     . GLU F 6  290  ? 161.852 57.756  128.853 1.00 49.97  ? 290  GLU F N     1 
ATOM   28103 C  CA    . GLU F 6  290  ? 161.700 58.705  127.752 1.00 51.34  ? 290  GLU F CA    1 
ATOM   28104 C  C     . GLU F 6  290  ? 162.827 59.729  127.754 1.00 53.18  ? 290  GLU F C     1 
ATOM   28105 O  O     . GLU F 6  290  ? 163.385 60.067  126.701 1.00 48.71  ? 290  GLU F O     1 
ATOM   28106 C  CB    . GLU F 6  290  ? 160.346 59.405  127.843 1.00 49.38  ? 290  GLU F CB    1 
ATOM   28107 C  CG    . GLU F 6  290  ? 159.163 58.472  127.979 1.00 51.36  ? 290  GLU F CG    1 
ATOM   28108 C  CD    . GLU F 6  290  ? 158.764 58.272  129.426 1.00 55.08  ? 290  GLU F CD    1 
ATOM   28109 O  OE1   . GLU F 6  290  ? 158.248 59.233  130.037 1.00 54.32  ? 290  GLU F OE1   1 
ATOM   28110 O  OE2   . GLU F 6  290  ? 158.975 57.159  129.957 1.00 54.73  ? 290  GLU F OE2   1 
ATOM   28111 N  N     . VAL F 6  291  ? 163.173 60.236  128.938 1.00 53.53  ? 291  VAL F N     1 
ATOM   28112 C  CA    . VAL F 6  291  ? 164.239 61.224  129.054 1.00 52.99  ? 291  VAL F CA    1 
ATOM   28113 C  C     . VAL F 6  291  ? 165.593 60.582  128.766 1.00 53.56  ? 291  VAL F C     1 
ATOM   28114 O  O     . VAL F 6  291  ? 166.440 61.171  128.082 1.00 51.82  ? 291  VAL F O     1 
ATOM   28115 C  CB    . VAL F 6  291  ? 164.214 61.878  130.446 1.00 50.71  ? 291  VAL F CB    1 
ATOM   28116 C  CG1   . VAL F 6  291  ? 165.513 62.618  130.693 1.00 50.35  ? 291  VAL F CG1   1 
ATOM   28117 C  CG2   . VAL F 6  291  ? 162.976 62.768  130.638 1.00 47.72  ? 291  VAL F CG2   1 
ATOM   28118 N  N     . MET F 6  292  ? 165.820 59.364  129.277 1.00 57.25  ? 292  MET F N     1 
ATOM   28119 C  CA    . MET F 6  292  ? 167.017 58.627  128.879 1.00 57.36  ? 292  MET F CA    1 
ATOM   28120 C  C     . MET F 6  292  ? 167.148 58.569  127.364 1.00 58.48  ? 292  MET F C     1 
ATOM   28121 O  O     . MET F 6  292  ? 168.178 58.971  126.806 1.00 56.44  ? 292  MET F O     1 
ATOM   28122 C  CB    . MET F 6  292  ? 166.980 57.206  129.431 1.00 57.11  ? 292  MET F CB    1 
ATOM   28123 C  CG    . MET F 6  292  ? 168.129 56.302  128.901 1.00 59.29  ? 292  MET F CG    1 
ATOM   28124 S  SD    . MET F 6  292  ? 169.625 56.286  129.874 1.00 66.95  ? 292  MET F SD    1 
ATOM   28125 C  CE    . MET F 6  292  ? 168.849 56.140  131.500 1.00 56.87  ? 292  MET F CE    1 
ATOM   28126 N  N     . PHE F 6  293  ? 166.084 58.142  126.678 1.00 57.20  ? 293  PHE F N     1 
ATOM   28127 C  CA    . PHE F 6  293  ? 166.167 57.974  125.233 1.00 58.69  ? 293  PHE F CA    1 
ATOM   28128 C  C     . PHE F 6  293  ? 166.397 59.300  124.521 1.00 57.50  ? 293  PHE F C     1 
ATOM   28129 O  O     . PHE F 6  293  ? 167.236 59.381  123.618 1.00 55.89  ? 293  PHE F O     1 
ATOM   28130 C  CB    . PHE F 6  293  ? 164.913 57.289  124.699 1.00 57.53  ? 293  PHE F CB    1 
ATOM   28131 C  CG    . PHE F 6  293  ? 165.052 55.801  124.539 1.00 58.92  ? 293  PHE F CG    1 
ATOM   28132 C  CD1   . PHE F 6  293  ? 166.052 55.272  123.736 1.00 58.69  ? 293  PHE F CD1   1 
ATOM   28133 C  CD2   . PHE F 6  293  ? 164.177 54.939  125.166 1.00 55.83  ? 293  PHE F CD2   1 
ATOM   28134 C  CE1   . PHE F 6  293  ? 166.180 53.912  123.576 1.00 57.82  ? 293  PHE F CE1   1 
ATOM   28135 C  CE2   . PHE F 6  293  ? 164.295 53.574  125.011 1.00 56.59  ? 293  PHE F CE2   1 
ATOM   28136 C  CZ    . PHE F 6  293  ? 165.297 53.057  124.209 1.00 56.65  ? 293  PHE F CZ    1 
ATOM   28137 N  N     . VAL F 6  294  ? 165.662 60.347  124.906 1.00 51.48  ? 294  VAL F N     1 
ATOM   28138 C  CA    . VAL F 6  294  ? 165.804 61.634  124.230 1.00 51.87  ? 294  VAL F CA    1 
ATOM   28139 C  C     . VAL F 6  294  ? 167.216 62.174  124.412 1.00 53.04  ? 294  VAL F C     1 
ATOM   28140 O  O     . VAL F 6  294  ? 167.851 62.626  123.450 1.00 48.15  ? 294  VAL F O     1 
ATOM   28141 C  CB    . VAL F 6  294  ? 164.750 62.632  124.742 1.00 51.21  ? 294  VAL F CB    1 
ATOM   28142 C  CG1   . VAL F 6  294  ? 165.176 64.065  124.442 1.00 47.79  ? 294  VAL F CG1   1 
ATOM   28143 C  CG2   . VAL F 6  294  ? 163.387 62.335  124.140 1.00 50.75  ? 294  VAL F CG2   1 
ATOM   28144 N  N     . THR F 6  295  ? 167.734 62.129  125.645 1.00 50.86  ? 295  THR F N     1 
ATOM   28145 C  CA    . THR F 6  295  ? 169.078 62.636  125.900 1.00 49.91  ? 295  THR F CA    1 
ATOM   28146 C  C     . THR F 6  295  ? 170.129 61.836  125.145 1.00 52.87  ? 295  THR F C     1 
ATOM   28147 O  O     . THR F 6  295  ? 171.083 62.408  124.605 1.00 50.95  ? 295  THR F O     1 
ATOM   28148 C  CB    . THR F 6  295  ? 169.371 62.621  127.397 1.00 49.17  ? 295  THR F CB    1 
ATOM   28149 O  OG1   . THR F 6  295  ? 168.296 63.255  128.102 1.00 49.41  ? 295  THR F OG1   1 
ATOM   28150 C  CG2   . THR F 6  295  ? 170.687 63.335  127.689 1.00 49.03  ? 295  THR F CG2   1 
ATOM   28151 N  N     . LEU F 6  296  ? 169.979 60.510  125.091 1.00 49.97  ? 296  LEU F N     1 
ATOM   28152 C  CA    . LEU F 6  296  ? 170.979 59.705  124.400 1.00 49.03  ? 296  LEU F CA    1 
ATOM   28153 C  C     . LEU F 6  296  ? 170.954 59.944  122.890 1.00 50.49  ? 296  LEU F C     1 
ATOM   28154 O  O     . LEU F 6  296  ? 172.015 60.018  122.260 1.00 47.18  ? 296  LEU F O     1 
ATOM   28155 C  CB    . LEU F 6  296  ? 170.807 58.224  124.754 1.00 49.25  ? 296  LEU F CB    1 
ATOM   28156 C  CG    . LEU F 6  296  ? 169.641 57.342  124.309 1.00 50.25  ? 296  LEU F CG    1 
ATOM   28157 C  CD1   . LEU F 6  296  ? 169.798 56.900  122.887 1.00 47.95  ? 296  LEU F CD1   1 
ATOM   28158 C  CD2   . LEU F 6  296  ? 169.542 56.122  125.215 1.00 49.87  ? 296  LEU F CD2   1 
ATOM   28159 N  N     . LEU F 6  297  ? 169.767 60.072  122.282 1.00 52.18  ? 297  LEU F N     1 
ATOM   28160 C  CA    . LEU F 6  297  ? 169.739 60.389  120.853 1.00 53.30  ? 297  LEU F CA    1 
ATOM   28161 C  C     . LEU F 6  297  ? 170.253 61.797  120.580 1.00 53.30  ? 297  LEU F C     1 
ATOM   28162 O  O     . LEU F 6  297  ? 170.918 62.030  119.567 1.00 51.91  ? 297  LEU F O     1 
ATOM   28163 C  CB    . LEU F 6  297  ? 168.342 60.203  120.251 1.00 52.29  ? 297  LEU F CB    1 
ATOM   28164 C  CG    . LEU F 6  297  ? 167.385 59.109  120.721 1.00 54.48  ? 297  LEU F CG    1 
ATOM   28165 C  CD1   . LEU F 6  297  ? 165.953 59.418  120.326 1.00 52.10  ? 297  LEU F CD1   1 
ATOM   28166 C  CD2   . LEU F 6  297  ? 167.806 57.780  120.117 1.00 51.62  ? 297  LEU F CD2   1 
ATOM   28167 N  N     . LYS F 6  298  ? 169.972 62.747  121.472 1.00 55.04  ? 298  LYS F N     1 
ATOM   28168 C  CA    . LYS F 6  298  ? 170.541 64.079  121.307 1.00 54.33  ? 298  LYS F CA    1 
ATOM   28169 C  C     . LYS F 6  298  ? 172.061 64.033  121.375 1.00 54.79  ? 298  LYS F C     1 
ATOM   28170 O  O     . LYS F 6  298  ? 172.744 64.686  120.578 1.00 55.17  ? 298  LYS F O     1 
ATOM   28171 C  CB    . LYS F 6  298  ? 169.982 65.024  122.366 1.00 55.01  ? 298  LYS F CB    1 
ATOM   28172 C  CG    . LYS F 6  298  ? 168.697 65.713  121.951 1.00 55.68  ? 298  LYS F CG    1 
ATOM   28173 C  CD    . LYS F 6  298  ? 168.337 66.835  122.908 1.00 55.23  ? 298  LYS F CD    1 
ATOM   28174 C  CE    . LYS F 6  298  ? 167.047 67.512  122.485 1.00 53.68  ? 298  LYS F CE    1 
ATOM   28175 N  NZ    . LYS F 6  298  ? 166.563 68.479  123.508 1.00 53.69  ? 298  LYS F NZ    1 
ATOM   28176 N  N     . GLU F 6  299  ? 172.608 63.249  122.307 1.00 53.78  ? 299  GLU F N     1 
ATOM   28177 C  CA    . GLU F 6  299  ? 174.057 63.125  122.417 1.00 56.87  ? 299  GLU F CA    1 
ATOM   28178 C  C     . GLU F 6  299  ? 174.656 62.467  121.179 1.00 56.35  ? 299  GLU F C     1 
ATOM   28179 O  O     . GLU F 6  299  ? 175.681 62.926  120.656 1.00 55.10  ? 299  GLU F O     1 
ATOM   28180 C  CB    . GLU F 6  299  ? 174.415 62.335  123.674 1.00 54.56  ? 299  GLU F CB    1 
ATOM   28181 C  CG    . GLU F 6  299  ? 174.538 63.196  124.920 1.00 54.37  ? 299  GLU F CG    1 
ATOM   28182 C  CD    . GLU F 6  299  ? 175.318 64.470  124.668 1.00 55.92  ? 299  GLU F CD    1 
ATOM   28183 O  OE1   . GLU F 6  299  ? 176.552 64.391  124.487 1.00 56.16  ? 299  GLU F OE1   1 
ATOM   28184 O  OE2   . GLU F 6  299  ? 174.695 65.551  124.651 1.00 55.49  ? 299  GLU F OE2   1 
ATOM   28185 N  N     . ILE F 6  300  ? 174.029 61.392  120.692 1.00 54.33  ? 300  ILE F N     1 
ATOM   28186 C  CA    . ILE F 6  300  ? 174.541 60.715  119.501 1.00 55.22  ? 300  ILE F CA    1 
ATOM   28187 C  C     . ILE F 6  300  ? 174.501 61.653  118.305 1.00 55.42  ? 300  ILE F C     1 
ATOM   28188 O  O     . ILE F 6  300  ? 175.442 61.703  117.505 1.00 53.50  ? 300  ILE F O     1 
ATOM   28189 C  CB    . ILE F 6  300  ? 173.756 59.423  119.213 1.00 54.25  ? 300  ILE F CB    1 
ATOM   28190 C  CG1   . ILE F 6  300  ? 173.962 58.392  120.317 1.00 54.02  ? 300  ILE F CG1   1 
ATOM   28191 C  CG2   . ILE F 6  300  ? 174.193 58.833  117.887 1.00 53.36  ? 300  ILE F CG2   1 
ATOM   28192 C  CD1   . ILE F 6  300  ? 172.942 57.272  120.292 1.00 51.63  ? 300  ILE F CD1   1 
ATOM   28193 N  N     . ILE F 6  301  ? 173.399 62.392  118.146 1.00 51.64  ? 301  ILE F N     1 
ATOM   28194 C  CA    . ILE F 6  301  ? 173.286 63.311  117.018 1.00 52.53  ? 301  ILE F CA    1 
ATOM   28195 C  C     . ILE F 6  301  ? 174.334 64.406  117.122 1.00 52.06  ? 301  ILE F C     1 
ATOM   28196 O  O     . ILE F 6  301  ? 174.958 64.777  116.124 1.00 50.57  ? 301  ILE F O     1 
ATOM   28197 C  CB    . ILE F 6  301  ? 171.863 63.892  116.925 1.00 50.77  ? 301  ILE F CB    1 
ATOM   28198 C  CG1   . ILE F 6  301  ? 170.873 62.789  116.579 1.00 50.07  ? 301  ILE F CG1   1 
ATOM   28199 C  CG2   . ILE F 6  301  ? 171.801 64.978  115.869 1.00 49.11  ? 301  ILE F CG2   1 
ATOM   28200 C  CD1   . ILE F 6  301  ? 169.445 63.242  116.446 1.00 48.76  ? 301  ILE F CD1   1 
ATOM   28201 N  N     . ASN F 6  302  ? 174.548 64.939  118.326 1.00 52.08  ? 302  ASN F N     1 
ATOM   28202 C  CA    . ASN F 6  302  ? 175.564 65.970  118.498 1.00 52.60  ? 302  ASN F CA    1 
ATOM   28203 C  C     . ASN F 6  302  ? 176.941 65.446  118.120 1.00 52.90  ? 302  ASN F C     1 
ATOM   28204 O  O     . ASN F 6  302  ? 177.713 66.138  117.450 1.00 52.97  ? 302  ASN F O     1 
ATOM   28205 C  CB    . ASN F 6  302  ? 175.555 66.480  119.939 1.00 52.22  ? 302  ASN F CB    1 
ATOM   28206 C  CG    . ASN F 6  302  ? 176.715 67.410  120.239 1.00 55.50  ? 302  ASN F CG    1 
ATOM   28207 O  OD1   . ASN F 6  302  ? 177.546 67.123  121.100 1.00 55.46  ? 302  ASN F OD1   1 
ATOM   28208 N  ND2   . ASN F 6  302  ? 176.772 68.535  119.536 1.00 53.19  ? 302  ASN F ND2   1 
ATOM   28209 N  N     . TYR F 6  303  ? 177.263 64.217  118.518 1.00 55.05  ? 303  TYR F N     1 
ATOM   28210 C  CA    . TYR F 6  303  ? 178.595 63.703  118.220 1.00 56.19  ? 303  TYR F CA    1 
ATOM   28211 C  C     . TYR F 6  303  ? 178.758 63.315  116.753 1.00 56.50  ? 303  TYR F C     1 
ATOM   28212 O  O     . TYR F 6  303  ? 179.834 63.524  116.180 1.00 56.81  ? 303  TYR F O     1 
ATOM   28213 C  CB    . TYR F 6  303  ? 178.916 62.535  119.149 1.00 55.71  ? 303  TYR F CB    1 
ATOM   28214 C  CG    . TYR F 6  303  ? 179.490 63.021  120.463 1.00 57.66  ? 303  TYR F CG    1 
ATOM   28215 C  CD1   . TYR F 6  303  ? 180.757 63.586  120.520 1.00 55.87  ? 303  TYR F CD1   1 
ATOM   28216 C  CD2   . TYR F 6  303  ? 178.750 62.954  121.633 1.00 55.40  ? 303  TYR F CD2   1 
ATOM   28217 C  CE1   . TYR F 6  303  ? 181.279 64.046  121.711 1.00 55.73  ? 303  TYR F CE1   1 
ATOM   28218 C  CE2   . TYR F 6  303  ? 179.263 63.410  122.827 1.00 57.52  ? 303  TYR F CE2   1 
ATOM   28219 C  CZ    . TYR F 6  303  ? 180.528 63.955  122.863 1.00 58.56  ? 303  TYR F CZ    1 
ATOM   28220 O  OH    . TYR F 6  303  ? 181.043 64.413  124.054 1.00 56.81  ? 303  TYR F OH    1 
ATOM   28221 N  N     . LEU F 6  304  ? 177.712 62.775  116.123 1.00 54.03  ? 304  LEU F N     1 
ATOM   28222 C  CA    . LEU F 6  304  ? 177.750 62.553  114.681 1.00 53.49  ? 304  LEU F CA    1 
ATOM   28223 C  C     . LEU F 6  304  ? 177.908 63.866  113.930 1.00 54.58  ? 304  LEU F C     1 
ATOM   28224 O  O     . LEU F 6  304  ? 178.690 63.957  112.978 1.00 54.95  ? 304  LEU F O     1 
ATOM   28225 C  CB    . LEU F 6  304  ? 176.481 61.834  114.226 1.00 54.22  ? 304  LEU F CB    1 
ATOM   28226 C  CG    . LEU F 6  304  ? 176.598 60.394  113.731 1.00 56.63  ? 304  LEU F CG    1 
ATOM   28227 C  CD1   . LEU F 6  304  ? 175.216 59.790  113.529 1.00 54.28  ? 304  LEU F CD1   1 
ATOM   28228 C  CD2   . LEU F 6  304  ? 177.391 60.347  112.438 1.00 54.52  ? 304  LEU F CD2   1 
ATOM   28229 N  N     . GLN F 6  305  ? 177.169 64.896  114.347 1.00 54.35  ? 305  GLN F N     1 
ATOM   28230 C  CA    . GLN F 6  305  ? 177.294 66.211  113.735 1.00 53.41  ? 305  GLN F CA    1 
ATOM   28231 C  C     . GLN F 6  305  ? 178.703 66.753  113.910 1.00 53.84  ? 305  GLN F C     1 
ATOM   28232 O  O     . GLN F 6  305  ? 179.273 67.330  112.981 1.00 52.13  ? 305  GLN F O     1 
ATOM   28233 C  CB    . GLN F 6  305  ? 176.267 67.163  114.354 1.00 52.64  ? 305  GLN F CB    1 
ATOM   28234 C  CG    . GLN F 6  305  ? 174.852 66.998  113.813 1.00 54.58  ? 305  GLN F CG    1 
ATOM   28235 C  CD    . GLN F 6  305  ? 174.436 68.118  112.885 1.00 55.52  ? 305  GLN F CD    1 
ATOM   28236 O  OE1   . GLN F 6  305  ? 175.132 69.123  112.754 1.00 54.79  ? 305  GLN F OE1   1 
ATOM   28237 N  NE2   . GLN F 6  305  ? 173.298 67.944  112.225 1.00 51.40  ? 305  GLN F NE2   1 
ATOM   28238 N  N     . PHE F 6  306  ? 179.286 66.560  115.094 1.00 54.14  ? 306  PHE F N     1 
ATOM   28239 C  CA    . PHE F 6  306  ? 180.630 67.054  115.362 1.00 54.36  ? 306  PHE F CA    1 
ATOM   28240 C  C     . PHE F 6  306  ? 181.666 66.343  114.502 1.00 55.08  ? 306  PHE F C     1 
ATOM   28241 O  O     . PHE F 6  306  ? 182.590 66.974  113.983 1.00 51.91  ? 306  PHE F O     1 
ATOM   28242 C  CB    . PHE F 6  306  ? 180.954 66.896  116.846 1.00 54.03  ? 306  PHE F CB    1 
ATOM   28243 C  CG    . PHE F 6  306  ? 182.326 67.371  117.220 1.00 56.10  ? 306  PHE F CG    1 
ATOM   28244 C  CD1   . PHE F 6  306  ? 182.760 68.633  116.856 1.00 54.83  ? 306  PHE F CD1   1 
ATOM   28245 C  CD2   . PHE F 6  306  ? 183.180 66.555  117.947 1.00 55.44  ? 306  PHE F CD2   1 
ATOM   28246 C  CE1   . PHE F 6  306  ? 184.026 69.074  117.202 1.00 55.33  ? 306  PHE F CE1   1 
ATOM   28247 C  CE2   . PHE F 6  306  ? 184.441 66.990  118.301 1.00 55.37  ? 306  PHE F CE2   1 
ATOM   28248 C  CZ    . PHE F 6  306  ? 184.865 68.254  117.928 1.00 56.05  ? 306  PHE F CZ    1 
ATOM   28249 N  N     . ILE F 6  307  ? 181.543 65.023  114.353 1.00 53.84  ? 307  ILE F N     1 
ATOM   28250 C  CA    . ILE F 6  307  ? 182.525 64.293  113.555 1.00 54.34  ? 307  ILE F CA    1 
ATOM   28251 C  C     . ILE F 6  307  ? 182.360 64.614  112.070 1.00 53.07  ? 307  ILE F C     1 
ATOM   28252 O  O     . ILE F 6  307  ? 183.351 64.801  111.347 1.00 51.12  ? 307  ILE F O     1 
ATOM   28253 C  CB    . ILE F 6  307  ? 182.446 62.782  113.854 1.00 54.17  ? 307  ILE F CB    1 
ATOM   28254 C  CG1   . ILE F 6  307  ? 183.787 62.109  113.539 1.00 53.10  ? 307  ILE F CG1   1 
ATOM   28255 C  CG2   . ILE F 6  307  ? 181.285 62.112  113.116 1.00 52.61  ? 307  ILE F CG2   1 
ATOM   28256 C  CD1   . ILE F 6  307  ? 184.864 62.378  114.575 1.00 52.53  ? 307  ILE F CD1   1 
ATOM   28257 N  N     . ASN F 6  308  ? 181.111 64.738  111.602 1.00 52.30  ? 308  ASN F N     1 
ATOM   28258 C  CA    . ASN F 6  308  ? 180.868 65.166  110.231 1.00 53.22  ? 308  ASN F CA    1 
ATOM   28259 C  C     . ASN F 6  308  ? 181.441 66.557  109.996 1.00 54.28  ? 308  ASN F C     1 
ATOM   28260 O  O     . ASN F 6  308  ? 182.029 66.828  108.947 1.00 53.91  ? 308  ASN F O     1 
ATOM   28261 C  CB    . ASN F 6  308  ? 179.365 65.159  109.940 1.00 52.30  ? 308  ASN F CB    1 
ATOM   28262 C  CG    . ASN F 6  308  ? 178.800 63.761  109.778 1.00 56.57  ? 308  ASN F CG    1 
ATOM   28263 O  OD1   . ASN F 6  308  ? 178.357 63.373  108.699 1.00 56.90  ? 308  ASN F OD1   1 
ATOM   28264 N  ND2   . ASN F 6  308  ? 178.812 62.996  110.861 1.00 54.87  ? 308  ASN F ND2   1 
ATOM   28265 N  N     . ASP F 6  309  ? 181.279 67.446  110.974 1.00 51.90  ? 309  ASP F N     1 
ATOM   28266 C  CA    . ASP F 6  309  ? 181.748 68.817  110.859 1.00 51.07  ? 309  ASP F CA    1 
ATOM   28267 C  C     . ASP F 6  309  ? 183.269 68.901  110.900 1.00 53.95  ? 309  ASP F C     1 
ATOM   28268 O  O     . ASP F 6  309  ? 183.866 69.712  110.183 1.00 52.53  ? 309  ASP F O     1 
ATOM   28269 C  CB    . ASP F 6  309  ? 181.116 69.641  111.976 1.00 51.17  ? 309  ASP F CB    1 
ATOM   28270 C  CG    . ASP F 6  309  ? 179.723 70.103  111.633 1.00 53.35  ? 309  ASP F CG    1 
ATOM   28271 O  OD1   . ASP F 6  309  ? 179.334 69.952  110.462 1.00 53.46  ? 309  ASP F OD1   1 
ATOM   28272 O  OD2   . ASP F 6  309  ? 179.005 70.607  112.518 1.00 52.82  ? 309  ASP F OD2   1 
ATOM   28273 N  N     . LEU F 6  310  ? 183.915 68.067  111.721 1.00 53.94  ? 310  LEU F N     1 
ATOM   28274 C  CA    . LEU F 6  310  ? 185.372 68.012  111.716 1.00 54.16  ? 310  LEU F CA    1 
ATOM   28275 C  C     . LEU F 6  310  ? 185.889 67.550  110.365 1.00 54.23  ? 310  LEU F C     1 
ATOM   28276 O  O     . LEU F 6  310  ? 186.855 68.111  109.834 1.00 52.48  ? 310  LEU F O     1 
ATOM   28277 C  CB    . LEU F 6  310  ? 185.886 67.079  112.807 1.00 52.26  ? 310  LEU F CB    1 
ATOM   28278 C  CG    . LEU F 6  310  ? 186.058 67.633  114.216 1.00 53.37  ? 310  LEU F CG    1 
ATOM   28279 C  CD1   . LEU F 6  310  ? 185.920 66.497  115.213 1.00 52.11  ? 310  LEU F CD1   1 
ATOM   28280 C  CD2   . LEU F 6  310  ? 187.396 68.344  114.371 1.00 52.49  ? 310  LEU F CD2   1 
ATOM   28281 N  N     . CYS F 6  311  ? 185.254 66.527  109.787 1.00 56.02  ? 311  CYS F N     1 
ATOM   28282 C  CA    . CYS F 6  311  ? 185.685 66.057  108.475 1.00 56.65  ? 311  CYS F CA    1 
ATOM   28283 C  C     . CYS F 6  311  ? 185.406 67.087  107.383 1.00 56.28  ? 311  CYS F C     1 
ATOM   28284 O  O     . CYS F 6  311  ? 186.200 67.226  106.445 1.00 55.29  ? 311  CYS F O     1 
ATOM   28285 C  CB    . CYS F 6  311  ? 184.999 64.734  108.151 1.00 57.83  ? 311  CYS F CB    1 
ATOM   28286 S  SG    . CYS F 6  311  ? 185.367 63.446  109.341 1.00 70.71  ? 311  CYS F SG    1 
ATOM   28287 N  N     . ASP F 6  312  ? 184.287 67.809  107.484 1.00 51.10  ? 312  ASP F N     1 
ATOM   28288 C  CA    . ASP F 6  312  ? 183.921 68.782  106.459 1.00 51.49  ? 312  ASP F CA    1 
ATOM   28289 C  C     . ASP F 6  312  ? 184.803 70.022  106.527 1.00 52.81  ? 312  ASP F C     1 
ATOM   28290 O  O     . ASP F 6  312  ? 185.063 70.662  105.502 1.00 51.73  ? 312  ASP F O     1 
ATOM   28291 C  CB    . ASP F 6  312  ? 182.445 69.161  106.602 1.00 51.58  ? 312  ASP F CB    1 
ATOM   28292 C  CG    . ASP F 6  312  ? 181.508 68.110  106.018 1.00 53.62  ? 312  ASP F CG    1 
ATOM   28293 O  OD1   . ASP F 6  312  ? 181.898 67.439  105.039 1.00 52.32  ? 312  ASP F OD1   1 
ATOM   28294 O  OD2   . ASP F 6  312  ? 180.385 67.950  106.543 1.00 53.04  ? 312  ASP F OD2   1 
ATOM   28295 N  N     . THR F 6  313  ? 185.253 70.389  107.729 1.00 48.83  ? 313  THR F N     1 
ATOM   28296 C  CA    . THR F 6  313  ? 186.131 71.545  107.867 1.00 49.20  ? 313  THR F CA    1 
ATOM   28297 C  C     . THR F 6  313  ? 187.487 71.279  107.225 1.00 49.72  ? 313  THR F C     1 
ATOM   28298 O  O     . THR F 6  313  ? 187.974 72.077  106.416 1.00 48.02  ? 313  THR F O     1 
ATOM   28299 C  CB    . THR F 6  313  ? 186.302 71.900  109.347 1.00 49.14  ? 313  THR F CB    1 
ATOM   28300 O  OG1   . THR F 6  313  ? 185.158 72.633  109.802 1.00 49.97  ? 313  THR F OG1   1 
ATOM   28301 C  CG2   . THR F 6  313  ? 187.536 72.766  109.547 1.00 44.60  ? 313  THR F CG2   1 
ATOM   28302 N  N     . PHE F 6  314  ? 188.106 70.151  107.566 1.00 54.07  ? 314  PHE F N     1 
ATOM   28303 C  CA    . PHE F 6  314  ? 189.491 69.863  107.194 1.00 55.12  ? 314  PHE F CA    1 
ATOM   28304 C  C     . PHE F 6  314  ? 189.492 68.868  106.037 1.00 55.63  ? 314  PHE F C     1 
ATOM   28305 O  O     . PHE F 6  314  ? 189.578 67.654  106.229 1.00 55.13  ? 314  PHE F O     1 
ATOM   28306 C  CB    . PHE F 6  314  ? 190.269 69.346  108.398 1.00 52.46  ? 314  PHE F CB    1 
ATOM   28307 C  CG    . PHE F 6  314  ? 190.249 70.283  109.573 1.00 53.86  ? 314  PHE F CG    1 
ATOM   28308 C  CD1   . PHE F 6  314  ? 190.967 71.468  109.541 1.00 54.71  ? 314  PHE F CD1   1 
ATOM   28309 C  CD2   . PHE F 6  314  ? 189.515 69.983  110.708 1.00 53.51  ? 314  PHE F CD2   1 
ATOM   28310 C  CE1   . PHE F 6  314  ? 190.951 72.334  110.616 1.00 54.70  ? 314  PHE F CE1   1 
ATOM   28311 C  CE2   . PHE F 6  314  ? 189.497 70.845  111.790 1.00 54.36  ? 314  PHE F CE2   1 
ATOM   28312 C  CZ    . PHE F 6  314  ? 190.215 72.022  111.741 1.00 55.00  ? 314  PHE F CZ    1 
ATOM   28313 N  N     . ASN F 6  315  ? 189.393 69.399  104.822 1.00 52.62  ? 315  ASN F N     1 
ATOM   28314 C  CA    . ASN F 6  315  ? 189.404 68.594  103.611 1.00 52.17  ? 315  ASN F CA    1 
ATOM   28315 C  C     . ASN F 6  315  ? 190.809 68.316  103.094 1.00 51.31  ? 315  ASN F C     1 
ATOM   28316 O  O     . ASN F 6  315  ? 190.959 67.566  102.125 1.00 50.96  ? 315  ASN F O     1 
ATOM   28317 C  CB    . ASN F 6  315  ? 188.573 69.283  102.523 1.00 50.56  ? 315  ASN F CB    1 
ATOM   28318 C  CG    . ASN F 6  315  ? 188.871 70.767  102.415 1.00 52.96  ? 315  ASN F CG    1 
ATOM   28319 O  OD1   . ASN F 6  315  ? 189.756 71.287  103.094 1.00 51.64  ? 315  ASN F OD1   1 
ATOM   28320 N  ND2   . ASN F 6  315  ? 188.127 71.457  101.561 1.00 51.72  ? 315  ASN F ND2   1 
ATOM   28321 N  N     . ASN F 6  316  ? 191.833 68.895  103.718 1.00 51.61  ? 316  ASN F N     1 
ATOM   28322 C  CA    . ASN F 6  316  ? 193.222 68.710  103.323 1.00 52.69  ? 316  ASN F CA    1 
ATOM   28323 C  C     . ASN F 6  316  ? 194.062 68.402  104.552 1.00 53.45  ? 316  ASN F C     1 
ATOM   28324 O  O     . ASN F 6  316  ? 193.669 68.702  105.683 1.00 50.88  ? 316  ASN F O     1 
ATOM   28325 C  CB    . ASN F 6  316  ? 193.780 69.953  102.622 1.00 49.76  ? 316  ASN F CB    1 
ATOM   28326 C  CG    . ASN F 6  316  ? 193.864 71.154  103.547 1.00 52.64  ? 316  ASN F CG    1 
ATOM   28327 O  OD1   . ASN F 6  316  ? 194.803 71.283  104.328 1.00 51.85  ? 316  ASN F OD1   1 
ATOM   28328 N  ND2   . ASN F 6  316  ? 192.886 72.047  103.452 1.00 49.70  ? 316  ASN F ND2   1 
ATOM   28329 N  N     . GLU F 6  317  ? 195.225 67.786  104.321 1.00 54.62  ? 317  GLU F N     1 
ATOM   28330 C  CA    . GLU F 6  317  ? 196.166 67.546  105.410 1.00 55.87  ? 317  GLU F CA    1 
ATOM   28331 C  C     . GLU F 6  317  ? 196.975 68.788  105.771 1.00 56.06  ? 317  GLU F C     1 
ATOM   28332 O  O     . GLU F 6  317  ? 197.453 68.895  106.906 1.00 53.09  ? 317  GLU F O     1 
ATOM   28333 C  CB    . GLU F 6  317  ? 197.103 66.394  105.045 1.00 54.92  ? 317  GLU F CB    1 
ATOM   28334 C  CG    . GLU F 6  317  ? 196.486 65.021  105.247 1.00 54.27  ? 317  GLU F CG    1 
ATOM   28335 C  CD    . GLU F 6  317  ? 197.145 63.945  104.405 1.00 57.72  ? 317  GLU F CD    1 
ATOM   28336 O  OE1   . GLU F 6  317  ? 197.950 64.286  103.513 1.00 55.20  ? 317  GLU F OE1   1 
ATOM   28337 O  OE2   . GLU F 6  317  ? 196.857 62.752  104.641 1.00 59.02  ? 317  GLU F OE2   1 
ATOM   28338 N  N     . GLN F 6  318  ? 197.135 69.724  104.831 1.00 58.26  ? 318  GLN F N     1 
ATOM   28339 C  CA    . GLN F 6  318  ? 197.931 70.921  105.089 1.00 57.87  ? 318  GLN F CA    1 
ATOM   28340 C  C     . GLN F 6  318  ? 197.320 71.771  106.197 1.00 57.31  ? 318  GLN F C     1 
ATOM   28341 O  O     . GLN F 6  318  ? 198.032 72.244  107.090 1.00 56.96  ? 318  GLN F O     1 
ATOM   28342 C  CB    . GLN F 6  318  ? 198.074 71.732  103.800 1.00 57.50  ? 318  GLN F CB    1 
ATOM   28343 C  CG    . GLN F 6  318  ? 199.140 71.201  102.844 1.00 57.30  ? 318  GLN F CG    1 
ATOM   28344 C  CD    . GLN F 6  318  ? 199.400 72.139  101.676 1.00 59.81  ? 318  GLN F CD    1 
ATOM   28345 O  OE1   . GLN F 6  318  ? 198.678 73.116  101.475 1.00 59.08  ? 318  GLN F OE1   1 
ATOM   28346 N  NE2   . GLN F 6  318  ? 200.447 71.855  100.911 1.00 59.36  ? 318  GLN F NE2   1 
ATOM   28347 N  N     . LEU F 6  319  ? 196.000 71.969  106.163 1.00 49.35  ? 319  LEU F N     1 
ATOM   28348 C  CA    . LEU F 6  319  ? 195.330 72.678  107.248 1.00 48.65  ? 319  LEU F CA    1 
ATOM   28349 C  C     . LEU F 6  319  ? 195.422 71.907  108.554 1.00 48.82  ? 319  LEU F C     1 
ATOM   28350 O  O     . LEU F 6  319  ? 195.540 72.514  109.624 1.00 48.59  ? 319  LEU F O     1 
ATOM   28351 C  CB    . LEU F 6  319  ? 193.864 72.929  106.894 1.00 48.64  ? 319  LEU F CB    1 
ATOM   28352 C  CG    . LEU F 6  319  ? 193.520 74.164  106.056 1.00 51.11  ? 319  LEU F CG    1 
ATOM   28353 C  CD1   . LEU F 6  319  ? 192.079 74.574  106.294 1.00 47.96  ? 319  LEU F CD1   1 
ATOM   28354 C  CD2   . LEU F 6  319  ? 194.456 75.317  106.366 1.00 47.42  ? 319  LEU F CD2   1 
ATOM   28355 N  N     . ILE F 6  320  ? 195.361 70.578  108.488 1.00 49.00  ? 320  ILE F N     1 
ATOM   28356 C  CA    . ILE F 6  320  ? 195.468 69.765  109.695 1.00 51.98  ? 320  ILE F CA    1 
ATOM   28357 C  C     . ILE F 6  320  ? 196.810 70.003  110.369 1.00 52.70  ? 320  ILE F C     1 
ATOM   28358 O  O     . ILE F 6  320  ? 196.891 70.196  111.589 1.00 50.25  ? 320  ILE F O     1 
ATOM   28359 C  CB    . ILE F 6  320  ? 195.258 68.279  109.358 1.00 51.06  ? 320  ILE F CB    1 
ATOM   28360 C  CG1   . ILE F 6  320  ? 193.764 67.969  109.253 1.00 49.47  ? 320  ILE F CG1   1 
ATOM   28361 C  CG2   . ILE F 6  320  ? 195.943 67.395  110.386 1.00 49.21  ? 320  ILE F CG2   1 
ATOM   28362 C  CD1   . ILE F 6  320  ? 193.048 68.033  110.564 1.00 49.07  ? 320  ILE F CD1   1 
ATOM   28363 N  N     . LYS F 6  321  ? 197.884 70.012  109.579 1.00 54.85  ? 321  LYS F N     1 
ATOM   28364 C  CA    . LYS F 6  321  ? 199.192 70.343  110.133 1.00 54.61  ? 321  LYS F CA    1 
ATOM   28365 C  C     . LYS F 6  321  ? 199.235 71.792  110.601 1.00 53.77  ? 321  LYS F C     1 
ATOM   28366 O  O     . LYS F 6  321  ? 199.928 72.118  111.572 1.00 54.63  ? 321  LYS F O     1 
ATOM   28367 C  CB    . LYS F 6  321  ? 200.288 70.063  109.102 1.00 52.47  ? 321  LYS F CB    1 
ATOM   28368 C  CG    . LYS F 6  321  ? 200.716 68.599  109.067 1.00 53.05  ? 321  LYS F CG    1 
ATOM   28369 C  CD    . LYS F 6  321  ? 201.896 68.355  108.144 1.00 53.99  ? 321  LYS F CD    1 
ATOM   28370 C  CE    . LYS F 6  321  ? 202.278 66.880  108.136 1.00 53.54  ? 321  LYS F CE    1 
ATOM   28371 N  NZ    . LYS F 6  321  ? 203.302 66.554  107.102 1.00 53.81  ? 321  LYS F NZ    1 
ATOM   28372 N  N     . ARG F 6  322  ? 198.488 72.675  109.930 1.00 52.87  ? 322  ARG F N     1 
ATOM   28373 C  CA    . ARG F 6  322  ? 198.449 74.077  110.338 1.00 54.46  ? 322  ARG F CA    1 
ATOM   28374 C  C     . ARG F 6  322  ? 197.743 74.268  111.673 1.00 55.62  ? 322  ARG F C     1 
ATOM   28375 O  O     . ARG F 6  322  ? 197.941 75.293  112.335 1.00 55.38  ? 322  ARG F O     1 
ATOM   28376 C  CB    . ARG F 6  322  ? 197.776 74.927  109.264 1.00 52.58  ? 322  ARG F CB    1 
ATOM   28377 C  CG    . ARG F 6  322  ? 198.667 75.215  108.075 1.00 54.09  ? 322  ARG F CG    1 
ATOM   28378 C  CD    . ARG F 6  322  ? 197.893 75.892  106.970 1.00 54.07  ? 322  ARG F CD    1 
ATOM   28379 N  NE    . ARG F 6  322  ? 198.708 76.119  105.784 1.00 56.29  ? 322  ARG F NE    1 
ATOM   28380 C  CZ    . ARG F 6  322  ? 198.239 76.589  104.637 1.00 56.83  ? 322  ARG F CZ    1 
ATOM   28381 N  NH1   . ARG F 6  322  ? 196.956 76.872  104.479 1.00 55.89  ? 322  ARG F NH1   1 
ATOM   28382 N  NH2   . ARG F 6  322  ? 199.076 76.780  103.624 1.00 54.77  ? 322  ARG F NH2   1 
ATOM   28383 N  N     . HIS F 6  323  ? 196.898 73.319  112.073 1.00 54.42  ? 323  HIS F N     1 
ATOM   28384 C  CA    . HIS F 6  323  ? 196.184 73.398  113.339 1.00 54.47  ? 323  HIS F CA    1 
ATOM   28385 C  C     . HIS F 6  323  ? 196.524 72.239  114.265 1.00 54.05  ? 323  HIS F C     1 
ATOM   28386 O  O     . HIS F 6  323  ? 195.732 71.907  115.153 1.00 52.79  ? 323  HIS F O     1 
ATOM   28387 C  CB    . HIS F 6  323  ? 194.679 73.451  113.085 1.00 55.90  ? 323  HIS F CB    1 
ATOM   28388 C  CG    . HIS F 6  323  ? 194.261 74.586  112.206 1.00 56.16  ? 323  HIS F CG    1 
ATOM   28389 N  ND1   . HIS F 6  323  ? 194.105 74.448  110.844 1.00 55.71  ? 323  HIS F ND1   1 
ATOM   28390 C  CD2   . HIS F 6  323  ? 194.005 75.885  112.486 1.00 55.10  ? 323  HIS F CD2   1 
ATOM   28391 C  CE1   . HIS F 6  323  ? 193.748 75.609  110.325 1.00 55.69  ? 323  HIS F CE1   1 
ATOM   28392 N  NE2   . HIS F 6  323  ? 193.682 76.498  111.300 1.00 56.73  ? 323  HIS F NE2   1 
ATOM   28393 N  N     . GLU F 6  324  ? 197.691 71.619  114.072 1.00 54.47  ? 324  GLU F N     1 
ATOM   28394 C  CA    . GLU F 6  324  ? 198.048 70.432  114.841 1.00 55.36  ? 324  GLU F CA    1 
ATOM   28395 C  C     . GLU F 6  324  ? 198.284 70.746  116.313 1.00 54.24  ? 324  GLU F C     1 
ATOM   28396 O  O     . GLU F 6  324  ? 198.141 69.855  117.157 1.00 51.27  ? 324  GLU F O     1 
ATOM   28397 C  CB    . GLU F 6  324  ? 199.284 69.773  114.235 1.00 54.48  ? 324  GLU F CB    1 
ATOM   28398 C  CG    . GLU F 6  324  ? 199.266 68.260  114.293 1.00 53.86  ? 324  GLU F CG    1 
ATOM   28399 C  CD    . GLU F 6  324  ? 200.310 67.632  113.398 1.00 54.34  ? 324  GLU F CD    1 
ATOM   28400 O  OE1   . GLU F 6  324  ? 201.093 66.796  113.894 1.00 51.84  ? 324  GLU F OE1   1 
ATOM   28401 O  OE2   . GLU F 6  324  ? 200.337 67.964  112.196 1.00 53.04  ? 324  GLU F OE2   1 
ATOM   28402 N  N     . ASN F 6  325  ? 198.640 71.993  116.640 1.00 53.45  ? 325  ASN F N     1 
ATOM   28403 C  CA    . ASN F 6  325  ? 198.815 72.369  118.040 1.00 53.44  ? 325  ASN F CA    1 
ATOM   28404 C  C     . ASN F 6  325  ? 197.583 72.002  118.855 1.00 54.96  ? 325  ASN F C     1 
ATOM   28405 O  O     . ASN F 6  325  ? 197.696 71.432  119.947 1.00 52.87  ? 325  ASN F O     1 
ATOM   28406 C  CB    . ASN F 6  325  ? 199.106 73.866  118.159 1.00 52.76  ? 325  ASN F CB    1 
ATOM   28407 C  CG    . ASN F 6  325  ? 200.454 74.254  117.575 1.00 54.15  ? 325  ASN F CG    1 
ATOM   28408 O  OD1   . ASN F 6  325  ? 201.348 73.420  117.428 1.00 55.18  ? 325  ASN F OD1   1 
ATOM   28409 N  ND2   . ASN F 6  325  ? 200.606 75.530  117.245 1.00 51.91  ? 325  ASN F ND2   1 
ATOM   28410 N  N     . ILE F 6  326  ? 196.395 72.284  118.316 1.00 52.50  ? 326  ILE F N     1 
ATOM   28411 C  CA    . ILE F 6  326  ? 195.158 71.859  118.961 1.00 53.17  ? 326  ILE F CA    1 
ATOM   28412 C  C     . ILE F 6  326  ? 195.096 70.338  119.044 1.00 53.11  ? 326  ILE F C     1 
ATOM   28413 O  O     . ILE F 6  326  ? 194.580 69.773  120.018 1.00 51.10  ? 326  ILE F O     1 
ATOM   28414 C  CB    . ILE F 6  326  ? 193.946 72.445  118.211 1.00 53.89  ? 326  ILE F CB    1 
ATOM   28415 C  CG1   . ILE F 6  326  ? 193.998 73.974  118.269 1.00 52.95  ? 326  ILE F CG1   1 
ATOM   28416 C  CG2   . ILE F 6  326  ? 192.638 71.923  118.793 1.00 51.84  ? 326  ILE F CG2   1 
ATOM   28417 C  CD1   . ILE F 6  326  ? 193.838 74.530  119.674 1.00 51.27  ? 326  ILE F CD1   1 
ATOM   28418 N  N     . TRP F 6  327  ? 195.648 69.649  118.041 1.00 53.26  ? 327  TRP F N     1 
ATOM   28419 C  CA    . TRP F 6  327  ? 195.577 68.191  118.039 1.00 54.58  ? 327  TRP F CA    1 
ATOM   28420 C  C     . TRP F 6  327  ? 196.381 67.583  119.182 1.00 56.05  ? 327  TRP F C     1 
ATOM   28421 O  O     . TRP F 6  327  ? 195.860 66.745  119.924 1.00 55.89  ? 327  TRP F O     1 
ATOM   28422 C  CB    . TRP F 6  327  ? 196.031 67.629  116.692 1.00 53.84  ? 327  TRP F CB    1 
ATOM   28423 C  CG    . TRP F 6  327  ? 195.327 68.177  115.453 1.00 55.34  ? 327  TRP F CG    1 
ATOM   28424 C  CD1   . TRP F 6  327  ? 195.779 68.080  114.168 1.00 54.19  ? 327  TRP F CD1   1 
ATOM   28425 C  CD2   . TRP F 6  327  ? 194.053 68.853  115.372 1.00 54.92  ? 327  TRP F CD2   1 
ATOM   28426 N  NE1   . TRP F 6  327  ? 194.895 68.667  113.304 1.00 55.70  ? 327  TRP F NE1   1 
ATOM   28427 C  CE2   . TRP F 6  327  ? 193.827 69.148  114.015 1.00 55.98  ? 327  TRP F CE2   1 
ATOM   28428 C  CE3   . TRP F 6  327  ? 193.091 69.245  116.311 1.00 54.23  ? 327  TRP F CE3   1 
ATOM   28429 C  CZ2   . TRP F 6  327  ? 192.685 69.816  113.576 1.00 54.85  ? 327  TRP F CZ2   1 
ATOM   28430 C  CZ3   . TRP F 6  327  ? 191.960 69.907  115.871 1.00 54.55  ? 327  TRP F CZ3   1 
ATOM   28431 C  CH2   . TRP F 6  327  ? 191.767 70.184  114.517 1.00 54.50  ? 327  TRP F CH2   1 
ATOM   28432 N  N     . MET F 6  328  ? 197.646 67.990  119.362 1.00 57.59  ? 328  MET F N     1 
ATOM   28433 C  CA    . MET F 6  328  ? 198.371 67.426  120.505 1.00 58.17  ? 328  MET F CA    1 
ATOM   28434 C  C     . MET F 6  328  ? 197.918 68.036  121.826 1.00 56.41  ? 328  MET F C     1 
ATOM   28435 O  O     . MET F 6  328  ? 198.080 67.404  122.877 1.00 55.95  ? 328  MET F O     1 
ATOM   28436 C  CB    . MET F 6  328  ? 199.901 67.532  120.385 1.00 56.52  ? 328  MET F CB    1 
ATOM   28437 C  CG    . MET F 6  328  ? 200.551 67.004  119.104 1.00 55.79  ? 328  MET F CG    1 
ATOM   28438 S  SD    . MET F 6  328  ? 200.477 68.067  117.670 1.00 65.66  ? 328  MET F SD    1 
ATOM   28439 C  CE    . MET F 6  328  ? 200.933 69.615  118.442 1.00 56.00  ? 328  MET F CE    1 
ATOM   28440 N  N     . LEU F 6  329  ? 197.319 69.230  121.805 1.00 51.74  ? 329  LEU F N     1 
ATOM   28441 C  CA    . LEU F 6  329  ? 196.717 69.744  123.029 1.00 53.94  ? 329  LEU F CA    1 
ATOM   28442 C  C     . LEU F 6  329  ? 195.590 68.833  123.497 1.00 55.79  ? 329  LEU F C     1 
ATOM   28443 O  O     . LEU F 6  329  ? 195.433 68.595  124.700 1.00 56.31  ? 329  LEU F O     1 
ATOM   28444 C  CB    . LEU F 6  329  ? 196.219 71.173  122.815 1.00 52.75  ? 329  LEU F CB    1 
ATOM   28445 C  CG    . LEU F 6  329  ? 197.297 72.255  122.944 1.00 54.45  ? 329  LEU F CG    1 
ATOM   28446 C  CD1   . LEU F 6  329  ? 196.688 73.633  123.127 1.00 53.71  ? 329  LEU F CD1   1 
ATOM   28447 C  CD2   . LEU F 6  329  ? 198.254 71.937  124.084 1.00 51.96  ? 329  LEU F CD2   1 
ATOM   28448 N  N     . ILE F 6  330  ? 194.798 68.311  122.557 1.00 53.80  ? 330  ILE F N     1 
ATOM   28449 C  CA    . ILE F 6  330  ? 193.806 67.296  122.908 1.00 55.04  ? 330  ILE F CA    1 
ATOM   28450 C  C     . ILE F 6  330  ? 194.488 65.984  123.279 1.00 55.24  ? 330  ILE F C     1 
ATOM   28451 O  O     . ILE F 6  330  ? 194.075 65.294  124.219 1.00 54.15  ? 330  ILE F O     1 
ATOM   28452 C  CB    . ILE F 6  330  ? 192.807 67.099  121.753 1.00 55.39  ? 330  ILE F CB    1 
ATOM   28453 C  CG1   . ILE F 6  330  ? 192.063 68.400  121.464 1.00 55.30  ? 330  ILE F CG1   1 
ATOM   28454 C  CG2   . ILE F 6  330  ? 191.824 65.987  122.083 1.00 52.90  ? 330  ILE F CG2   1 
ATOM   28455 C  CD1   . ILE F 6  330  ? 191.319 68.381  120.162 1.00 54.31  ? 330  ILE F CD1   1 
ATOM   28456 N  N     . GLU F 6  331  ? 195.547 65.624  122.548 1.00 53.31  ? 331  GLU F N     1 
ATOM   28457 C  CA    . GLU F 6  331  ? 196.190 64.324  122.728 1.00 54.71  ? 331  GLU F CA    1 
ATOM   28458 C  C     . GLU F 6  331  ? 196.768 64.164  124.127 1.00 55.55  ? 331  GLU F C     1 
ATOM   28459 O  O     . GLU F 6  331  ? 196.700 63.078  124.714 1.00 52.92  ? 331  GLU F O     1 
ATOM   28460 C  CB    . GLU F 6  331  ? 197.283 64.132  121.679 1.00 53.49  ? 331  GLU F CB    1 
ATOM   28461 C  CG    . GLU F 6  331  ? 196.791 63.502  120.392 1.00 56.69  ? 331  GLU F CG    1 
ATOM   28462 C  CD    . GLU F 6  331  ? 197.839 63.504  119.301 1.00 58.04  ? 331  GLU F CD    1 
ATOM   28463 O  OE1   . GLU F 6  331  ? 198.852 64.220  119.448 1.00 56.37  ? 331  GLU F OE1   1 
ATOM   28464 O  OE2   . GLU F 6  331  ? 197.650 62.778  118.302 1.00 55.19  ? 331  GLU F OE2   1 
ATOM   28465 N  N     . GLN F 6  332  ? 197.362 65.226  124.671 1.00 55.27  ? 332  GLN F N     1 
ATOM   28466 C  CA    . GLN F 6  332  ? 197.939 65.133  126.006 1.00 55.37  ? 332  GLN F CA    1 
ATOM   28467 C  C     . GLN F 6  332  ? 196.885 64.975  127.093 1.00 57.02  ? 332  GLN F C     1 
ATOM   28468 O  O     . GLN F 6  332  ? 197.242 64.668  128.235 1.00 55.64  ? 332  GLN F O     1 
ATOM   28469 C  CB    . GLN F 6  332  ? 198.808 66.355  126.292 1.00 52.95  ? 332  GLN F CB    1 
ATOM   28470 C  CG    . GLN F 6  332  ? 200.252 66.189  125.845 1.00 54.88  ? 332  GLN F CG    1 
ATOM   28471 C  CD    . GLN F 6  332  ? 200.519 66.816  124.489 1.00 55.00  ? 332  GLN F CD    1 
ATOM   28472 O  OE1   . GLN F 6  332  ? 200.373 68.025  124.313 1.00 55.15  ? 332  GLN F OE1   1 
ATOM   28473 N  NE2   . GLN F 6  332  ? 200.919 65.997  123.524 1.00 53.60  ? 332  GLN F NE2   1 
ATOM   28474 N  N     . ARG F 6  333  ? 195.607 65.177  126.775 1.00 58.62  ? 333  ARG F N     1 
ATOM   28475 C  CA    . ARG F 6  333  ? 194.524 64.933  127.718 1.00 57.56  ? 333  ARG F CA    1 
ATOM   28476 C  C     . ARG F 6  333  ? 193.924 63.542  127.570 1.00 56.92  ? 333  ARG F C     1 
ATOM   28477 O  O     . ARG F 6  333  ? 192.929 63.234  128.235 1.00 55.72  ? 333  ARG F O     1 
ATOM   28478 C  CB    . ARG F 6  333  ? 193.429 65.993  127.564 1.00 56.99  ? 333  ARG F CB    1 
ATOM   28479 C  CG    . ARG F 6  333  ? 193.882 67.386  127.971 1.00 58.13  ? 333  ARG F CG    1 
ATOM   28480 C  CD    . ARG F 6  333  ? 194.426 67.392  129.393 1.00 57.58  ? 333  ARG F CD    1 
ATOM   28481 N  NE    . ARG F 6  333  ? 194.145 68.643  130.088 1.00 59.18  ? 333  ARG F NE    1 
ATOM   28482 C  CZ    . ARG F 6  333  ? 194.405 68.858  131.370 1.00 58.58  ? 333  ARG F CZ    1 
ATOM   28483 N  NH1   . ARG F 6  333  ? 194.971 67.933  132.125 1.00 57.07  ? 333  ARG F NH1   1 
ATOM   28484 N  NH2   . ARG F 6  333  ? 194.088 70.032  131.908 1.00 56.90  ? 333  ARG F NH2   1 
ATOM   28485 N  N     . LYS F 6  334  ? 194.495 62.707  126.708 1.00 54.56  ? 334  LYS F N     1 
ATOM   28486 C  CA    . LYS F 6  334  ? 194.083 61.320  126.587 1.00 54.97  ? 334  LYS F CA    1 
ATOM   28487 C  C     . LYS F 6  334  ? 194.575 60.521  127.790 1.00 54.30  ? 334  LYS F C     1 
ATOM   28488 O  O     . LYS F 6  334  ? 195.562 60.872  128.441 1.00 52.65  ? 334  LYS F O     1 
ATOM   28489 C  CB    . LYS F 6  334  ? 194.637 60.715  125.299 1.00 53.00  ? 334  LYS F CB    1 
ATOM   28490 C  CG    . LYS F 6  334  ? 194.033 61.280  124.035 1.00 52.82  ? 334  LYS F CG    1 
ATOM   28491 C  CD    . LYS F 6  334  ? 194.618 60.612  122.801 1.00 54.39  ? 334  LYS F CD    1 
ATOM   28492 C  CE    . LYS F 6  334  ? 194.179 61.334  121.543 1.00 53.10  ? 334  LYS F CE    1 
ATOM   28493 N  NZ    . LYS F 6  334  ? 194.749 60.731  120.314 1.00 55.76  ? 334  LYS F NZ    1 
ATOM   28494 N  N     . ILE F 6  335  ? 193.877 59.426  128.076 1.00 48.83  ? 335  ILE F N     1 
ATOM   28495 C  CA    . ILE F 6  335  ? 194.230 58.525  129.166 1.00 49.75  ? 335  ILE F CA    1 
ATOM   28496 C  C     . ILE F 6  335  ? 194.786 57.245  128.562 1.00 51.90  ? 335  ILE F C     1 
ATOM   28497 O  O     . ILE F 6  335  ? 194.134 56.612  127.722 1.00 49.19  ? 335  ILE F O     1 
ATOM   28498 C  CB    . ILE F 6  335  ? 193.026 58.222  130.076 1.00 49.66  ? 335  ILE F CB    1 
ATOM   28499 C  CG1   . ILE F 6  335  ? 192.548 59.490  130.785 1.00 47.03  ? 335  ILE F CG1   1 
ATOM   28500 C  CG2   . ILE F 6  335  ? 193.392 57.161  131.104 1.00 48.22  ? 335  ILE F CG2   1 
ATOM   28501 C  CD1   . ILE F 6  335  ? 191.345 59.261  131.674 1.00 46.95  ? 335  ILE F CD1   1 
ATOM   28502 N  N     . GLY F 6  336  ? 195.987 56.866  128.990 1.00 51.37  ? 336  GLY F N     1 
ATOM   28503 C  CA    . GLY F 6  336  ? 196.619 55.660  128.506 1.00 47.74  ? 336  GLY F CA    1 
ATOM   28504 C  C     . GLY F 6  336  ? 195.998 54.412  129.098 1.00 49.44  ? 336  GLY F C     1 
ATOM   28505 O  O     . GLY F 6  336  ? 195.147 54.455  129.986 1.00 47.66  ? 336  GLY F O     1 
ATOM   28506 N  N     . HIS F 6  337  ? 196.444 53.271  128.582 1.00 58.87  ? 337  HIS F N     1 
ATOM   28507 C  CA    . HIS F 6  337  ? 195.929 51.971  129.005 1.00 58.60  ? 337  HIS F CA    1 
ATOM   28508 C  C     . HIS F 6  337  ? 196.742 51.398  130.160 1.00 59.44  ? 337  HIS F C     1 
ATOM   28509 O  O     . HIS F 6  337  ? 197.249 50.280  130.102 1.00 59.94  ? 337  HIS F O     1 
ATOM   28510 C  CB    . HIS F 6  337  ? 195.906 51.016  127.818 1.00 56.60  ? 337  HIS F CB    1 
ATOM   28511 C  CG    . HIS F 6  337  ? 194.848 51.339  126.812 1.00 58.78  ? 337  HIS F CG    1 
ATOM   28512 N  ND1   . HIS F 6  337  ? 193.502 51.307  127.108 1.00 59.09  ? 337  HIS F ND1   1 
ATOM   28513 C  CD2   . HIS F 6  337  ? 194.939 51.727  125.518 1.00 59.13  ? 337  HIS F CD2   1 
ATOM   28514 C  CE1   . HIS F 6  337  ? 192.810 51.650  126.037 1.00 58.98  ? 337  HIS F CE1   1 
ATOM   28515 N  NE2   . HIS F 6  337  ? 193.657 51.911  125.058 1.00 59.23  ? 337  HIS F NE2   1 
ATOM   28516 N  N     . ASP F 6  338  ? 196.881 52.186  131.220 1.00 59.05  ? 338  ASP F N     1 
ATOM   28517 C  CA    . ASP F 6  338  ? 197.571 51.749  132.432 1.00 59.18  ? 338  ASP F CA    1 
ATOM   28518 C  C     . ASP F 6  338  ? 196.563 51.378  133.520 1.00 59.12  ? 338  ASP F C     1 
ATOM   28519 O  O     . ASP F 6  338  ? 196.509 51.977  134.595 1.00 58.13  ? 338  ASP F O     1 
ATOM   28520 C  CB    . ASP F 6  338  ? 198.533 52.835  132.902 1.00 58.17  ? 338  ASP F CB    1 
ATOM   28521 C  CG    . ASP F 6  338  ? 199.835 52.829  132.127 1.00 59.72  ? 338  ASP F CG    1 
ATOM   28522 O  OD1   . ASP F 6  338  ? 200.249 51.738  131.678 1.00 59.61  ? 338  ASP F OD1   1 
ATOM   28523 O  OD2   . ASP F 6  338  ? 200.438 53.911  131.957 1.00 60.34  ? 338  ASP F OD2   1 
ATOM   28524 N  N     . PHE F 6  339  ? 195.759 50.360  133.228 1.00 54.78  ? 339  PHE F N     1 
ATOM   28525 C  CA    . PHE F 6  339  ? 194.718 49.918  134.154 1.00 55.02  ? 339  PHE F CA    1 
ATOM   28526 C  C     . PHE F 6  339  ? 194.507 48.411  134.082 1.00 54.94  ? 339  PHE F C     1 
ATOM   28527 O  O     . PHE F 6  339  ? 194.010 47.894  133.083 1.00 57.50  ? 339  PHE F O     1 
ATOM   28528 C  CB    . PHE F 6  339  ? 193.398 50.639  133.867 1.00 55.16  ? 339  PHE F CB    1 
ATOM   28529 C  CG    . PHE F 6  339  ? 193.371 52.072  134.324 1.00 56.29  ? 339  PHE F CG    1 
ATOM   28530 C  CD1   . PHE F 6  339  ? 193.399 52.387  135.672 1.00 53.24  ? 339  PHE F CD1   1 
ATOM   28531 C  CD2   . PHE F 6  339  ? 193.300 53.106  133.403 1.00 55.58  ? 339  PHE F CD2   1 
ATOM   28532 C  CE1   . PHE F 6  339  ? 193.363 53.709  136.095 1.00 53.65  ? 339  PHE F CE1   1 
ATOM   28533 C  CE2   . PHE F 6  339  ? 193.264 54.428  133.820 1.00 54.25  ? 339  PHE F CE2   1 
ATOM   28534 C  CZ    . PHE F 6  339  ? 193.295 54.729  135.167 1.00 53.39  ? 339  PHE F CZ    1 
ATOM   28535 N  N     . GLY G 7  47   ? 102.974 142.203 169.228 1.00 44.48  ? 47   GLY G N     1 
ATOM   28536 C  CA    . GLY G 7  47   ? 102.164 143.261 168.651 1.00 44.64  ? 47   GLY G CA    1 
ATOM   28537 C  C     . GLY G 7  47   ? 102.941 144.534 168.371 1.00 49.22  ? 47   GLY G C     1 
ATOM   28538 O  O     . GLY G 7  47   ? 103.981 144.795 168.983 1.00 45.37  ? 47   GLY G O     1 
ATOM   28539 N  N     . GLU G 7  48   ? 102.430 145.335 167.445 1.00 57.96  ? 48   GLU G N     1 
ATOM   28540 C  CA    . GLU G 7  48   ? 103.079 146.564 167.012 1.00 56.87  ? 48   GLU G CA    1 
ATOM   28541 C  C     . GLU G 7  48   ? 102.397 147.766 167.658 1.00 56.74  ? 48   GLU G C     1 
ATOM   28542 O  O     . GLU G 7  48   ? 101.502 147.621 168.495 1.00 56.17  ? 48   GLU G O     1 
ATOM   28543 C  CB    . GLU G 7  48   ? 103.060 146.666 165.487 1.00 51.70  ? 48   GLU G CB    1 
ATOM   28544 C  CG    . GLU G 7  48   ? 103.834 145.570 164.786 1.00 54.16  ? 48   GLU G CG    1 
ATOM   28545 C  CD    . GLU G 7  48   ? 103.681 145.639 163.283 1.00 58.03  ? 48   GLU G CD    1 
ATOM   28546 O  OE1   . GLU G 7  48   ? 102.984 146.560 162.807 1.00 56.28  ? 48   GLU G OE1   1 
ATOM   28547 O  OE2   . GLU G 7  48   ? 104.276 144.795 162.579 1.00 58.97  ? 48   GLU G OE2   1 
ATOM   28548 N  N     . MET G 7  49   ? 102.877 148.958 167.301 1.00 52.87  ? 49   MET G N     1 
ATOM   28549 C  CA    . MET G 7  49   ? 102.220 150.221 167.627 1.00 51.66  ? 49   MET G CA    1 
ATOM   28550 C  C     . MET G 7  49   ? 102.332 150.539 169.118 1.00 52.29  ? 49   MET G C     1 
ATOM   28551 O  O     . MET G 7  49   ? 102.006 151.649 169.551 1.00 54.59  ? 49   MET G O     1 
ATOM   28552 C  CB    . MET G 7  49   ? 100.755 150.172 167.159 1.00 48.85  ? 49   MET G CB    1 
ATOM   28553 C  CG    . MET G 7  49   ? 99.888  151.372 167.490 1.00 50.66  ? 49   MET G CG    1 
ATOM   28554 S  SD    . MET G 7  49   ? 98.226  151.199 166.809 1.00 63.15  ? 49   MET G SD    1 
ATOM   28555 C  CE    . MET G 7  49   ? 97.644  152.889 166.870 1.00 50.07  ? 49   MET G CE    1 
ATOM   28556 N  N     . GLU G 7  50   ? 102.844 149.597 169.906 1.00 49.87  ? 50   GLU G N     1 
ATOM   28557 C  CA    . GLU G 7  50   ? 102.904 149.750 171.353 1.00 50.28  ? 50   GLU G CA    1 
ATOM   28558 C  C     . GLU G 7  50   ? 104.333 149.878 171.862 1.00 49.88  ? 50   GLU G C     1 
ATOM   28559 O  O     . GLU G 7  50   ? 104.664 150.850 172.544 1.00 49.09  ? 50   GLU G O     1 
ATOM   28560 C  CB    . GLU G 7  50   ? 102.206 148.570 172.040 1.00 49.64  ? 50   GLU G CB    1 
ATOM   28561 C  CG    . GLU G 7  50   ? 102.254 148.631 173.561 1.00 48.57  ? 50   GLU G CG    1 
ATOM   28562 C  CD    . GLU G 7  50   ? 102.042 150.037 174.095 1.00 51.14  ? 50   GLU G CD    1 
ATOM   28563 O  OE1   . GLU G 7  50   ? 100.966 150.616 173.840 1.00 49.22  ? 50   GLU G OE1   1 
ATOM   28564 O  OE2   . GLU G 7  50   ? 102.953 150.563 174.766 1.00 49.80  ? 50   GLU G OE2   1 
ATOM   28565 N  N     . ASP G 7  51   ? 105.190 148.908 171.564 1.00 46.98  ? 51   ASP G N     1 
ATOM   28566 C  CA    . ASP G 7  51   ? 106.552 148.962 172.072 1.00 46.77  ? 51   ASP G CA    1 
ATOM   28567 C  C     . ASP G 7  51   ? 107.548 148.687 170.962 1.00 46.73  ? 51   ASP G C     1 
ATOM   28568 O  O     . ASP G 7  51   ? 108.723 149.048 171.076 1.00 48.37  ? 51   ASP G O     1 
ATOM   28569 C  CB    . ASP G 7  51   ? 106.727 147.983 173.232 1.00 47.00  ? 51   ASP G CB    1 
ATOM   28570 C  CG    . ASP G 7  51   ? 106.649 148.670 174.586 1.00 48.91  ? 51   ASP G CG    1 
ATOM   28571 O  OD1   . ASP G 7  51   ? 107.248 149.754 174.743 1.00 47.01  ? 51   ASP G OD1   1 
ATOM   28572 O  OD2   . ASP G 7  51   ? 105.950 148.146 175.476 1.00 48.34  ? 51   ASP G OD2   1 
ATOM   28573 N  N     . LYS G 7  52   ? 107.091 148.053 169.883 1.00 42.15  ? 52   LYS G N     1 
ATOM   28574 C  CA    . LYS G 7  52   ? 107.967 147.882 168.735 1.00 44.38  ? 52   LYS G CA    1 
ATOM   28575 C  C     . LYS G 7  52   ? 108.332 149.212 168.094 1.00 44.67  ? 52   LYS G C     1 
ATOM   28576 O  O     . LYS G 7  52   ? 109.495 149.407 167.731 1.00 43.07  ? 52   LYS G O     1 
ATOM   28577 C  CB    . LYS G 7  52   ? 107.319 146.952 167.713 1.00 44.05  ? 52   LYS G CB    1 
ATOM   28578 C  CG    . LYS G 7  52   ? 107.244 145.521 168.188 1.00 45.37  ? 52   LYS G CG    1 
ATOM   28579 C  CD    . LYS G 7  52   ? 106.647 144.596 167.142 1.00 44.45  ? 52   LYS G CD    1 
ATOM   28580 C  CE    . LYS G 7  52   ? 106.650 143.160 167.642 1.00 43.86  ? 52   LYS G CE    1 
ATOM   28581 N  NZ    . LYS G 7  52   ? 106.049 142.230 166.661 1.00 46.13  ? 52   LYS G NZ    1 
ATOM   28582 N  N     . TYR G 7  53   ? 107.379 150.143 167.979 1.00 41.36  ? 53   TYR G N     1 
ATOM   28583 C  CA    . TYR G 7  53   ? 107.627 151.415 167.314 1.00 38.17  ? 53   TYR G CA    1 
ATOM   28584 C  C     . TYR G 7  53   ? 107.165 152.595 168.149 1.00 39.08  ? 53   TYR G C     1 
ATOM   28585 O  O     . TYR G 7  53   ? 106.752 153.615 167.597 1.00 40.87  ? 53   TYR G O     1 
ATOM   28586 C  CB    . TYR G 7  53   ? 106.939 151.488 165.953 1.00 37.26  ? 53   TYR G CB    1 
ATOM   28587 C  CG    . TYR G 7  53   ? 107.208 150.322 165.043 1.00 39.69  ? 53   TYR G CG    1 
ATOM   28588 C  CD1   . TYR G 7  53   ? 108.458 150.137 164.476 1.00 39.17  ? 53   TYR G CD1   1 
ATOM   28589 C  CD2   . TYR G 7  53   ? 106.200 149.432 164.712 1.00 41.06  ? 53   TYR G CD2   1 
ATOM   28590 C  CE1   . TYR G 7  53   ? 108.707 149.082 163.634 1.00 42.01  ? 53   TYR G CE1   1 
ATOM   28591 C  CE2   . TYR G 7  53   ? 106.436 148.373 163.861 1.00 40.41  ? 53   TYR G CE2   1 
ATOM   28592 C  CZ    . TYR G 7  53   ? 107.692 148.204 163.324 1.00 45.12  ? 53   TYR G CZ    1 
ATOM   28593 O  OH    . TYR G 7  53   ? 107.941 147.151 162.478 1.00 45.74  ? 53   TYR G OH    1 
ATOM   28594 N  N     . LYS G 7  54   ? 107.226 152.479 169.472 1.00 34.52  ? 54   LYS G N     1 
ATOM   28595 C  CA    . LYS G 7  54   ? 106.779 153.564 170.338 1.00 31.94  ? 54   LYS G CA    1 
ATOM   28596 C  C     . LYS G 7  54   ? 107.620 154.820 170.142 1.00 33.23  ? 54   LYS G C     1 
ATOM   28597 O  O     . LYS G 7  54   ? 107.084 155.930 170.052 1.00 32.26  ? 54   LYS G O     1 
ATOM   28598 C  CB    . LYS G 7  54   ? 106.827 153.108 171.794 1.00 35.43  ? 54   LYS G CB    1 
ATOM   28599 C  CG    . LYS G 7  54   ? 106.355 154.141 172.794 1.00 35.70  ? 54   LYS G CG    1 
ATOM   28600 C  CD    . LYS G 7  54   ? 106.778 153.778 174.207 1.00 33.35  ? 54   LYS G CD    1 
ATOM   28601 C  CE    . LYS G 7  54   ? 108.055 152.954 174.225 1.00 36.66  ? 54   LYS G CE    1 
ATOM   28602 N  NZ    . LYS G 7  54   ? 108.803 153.111 175.504 1.00 37.17  ? 54   LYS G NZ    1 
ATOM   28603 N  N     . ILE G 7  55   ? 108.945 154.664 170.078 1.00 36.22  ? 55   ILE G N     1 
ATOM   28604 C  CA    . ILE G 7  55   ? 109.824 155.818 169.891 1.00 34.65  ? 55   ILE G CA    1 
ATOM   28605 C  C     . ILE G 7  55   ? 109.600 156.441 168.520 1.00 34.08  ? 55   ILE G C     1 
ATOM   28606 O  O     . ILE G 7  55   ? 109.485 157.665 168.386 1.00 35.52  ? 55   ILE G O     1 
ATOM   28607 C  CB    . ILE G 7  55   ? 111.297 155.418 170.085 1.00 34.77  ? 55   ILE G CB    1 
ATOM   28608 C  CG1   . ILE G 7  55   ? 111.571 155.012 171.529 1.00 33.94  ? 55   ILE G CG1   1 
ATOM   28609 C  CG2   . ILE G 7  55   ? 112.204 156.551 169.686 1.00 32.39  ? 55   ILE G CG2   1 
ATOM   28610 C  CD1   . ILE G 7  55   ? 111.759 153.531 171.707 1.00 33.97  ? 55   ILE G CD1   1 
ATOM   28611 N  N     . PHE G 7  56   ? 109.537 155.609 167.478 1.00 28.82  ? 56   PHE G N     1 
ATOM   28612 C  CA    . PHE G 7  56   ? 109.318 156.140 166.138 1.00 22.72  ? 56   PHE G CA    1 
ATOM   28613 C  C     . PHE G 7  56   ? 107.978 156.849 166.037 1.00 24.26  ? 56   PHE G C     1 
ATOM   28614 O  O     . PHE G 7  56   ? 107.881 157.918 165.427 1.00 30.19  ? 56   PHE G O     1 
ATOM   28615 C  CB    . PHE G 7  56   ? 109.405 155.030 165.094 1.00 24.24  ? 56   PHE G CB    1 
ATOM   28616 C  CG    . PHE G 7  56   ? 108.981 155.469 163.729 1.00 28.99  ? 56   PHE G CG    1 
ATOM   28617 C  CD1   . PHE G 7  56   ? 109.802 156.273 162.961 1.00 28.73  ? 56   PHE G CD1   1 
ATOM   28618 C  CD2   . PHE G 7  56   ? 107.754 155.098 163.215 1.00 29.78  ? 56   PHE G CD2   1 
ATOM   28619 C  CE1   . PHE G 7  56   ? 109.410 156.693 161.715 1.00 27.19  ? 56   PHE G CE1   1 
ATOM   28620 C  CE2   . PHE G 7  56   ? 107.358 155.518 161.964 1.00 25.69  ? 56   PHE G CE2   1 
ATOM   28621 C  CZ    . PHE G 7  56   ? 108.188 156.313 161.215 1.00 24.64  ? 56   PHE G CZ    1 
ATOM   28622 N  N     . ILE G 7  57   ? 106.931 156.271 166.625 1.00 24.37  ? 57   ILE G N     1 
ATOM   28623 C  CA    . ILE G 7  57   ? 105.613 156.887 166.545 1.00 25.21  ? 57   ILE G CA    1 
ATOM   28624 C  C     . ILE G 7  57   ? 105.586 158.196 167.320 1.00 22.36  ? 57   ILE G C     1 
ATOM   28625 O  O     . ILE G 7  57   ? 104.925 159.156 166.914 1.00 25.14  ? 57   ILE G O     1 
ATOM   28626 C  CB    . ILE G 7  57   ? 104.532 155.907 167.028 1.00 21.64  ? 57   ILE G CB    1 
ATOM   28627 C  CG1   . ILE G 7  57   ? 104.313 154.816 165.989 1.00 22.11  ? 57   ILE G CG1   1 
ATOM   28628 C  CG2   . ILE G 7  57   ? 103.227 156.624 167.270 1.00 19.91  ? 57   ILE G CG2   1 
ATOM   28629 C  CD1   . ILE G 7  57   ? 103.602 153.619 166.524 1.00 25.72  ? 57   ILE G CD1   1 
ATOM   28630 N  N     . LYS G 7  58   ? 106.301 158.264 168.442 1.00 27.16  ? 58   LYS G N     1 
ATOM   28631 C  CA    . LYS G 7  58   ? 106.340 159.516 169.189 1.00 31.81  ? 58   LYS G CA    1 
ATOM   28632 C  C     . LYS G 7  58   ? 107.199 160.562 168.490 1.00 33.13  ? 58   LYS G C     1 
ATOM   28633 O  O     . LYS G 7  58   ? 107.031 161.762 168.735 1.00 31.21  ? 58   LYS G O     1 
ATOM   28634 C  CB    . LYS G 7  58   ? 106.840 159.270 170.613 1.00 32.28  ? 58   LYS G CB    1 
ATOM   28635 C  CG    . LYS G 7  58   ? 108.309 159.522 170.820 1.00 30.58  ? 58   LYS G CG    1 
ATOM   28636 C  CD    . LYS G 7  58   ? 108.642 159.623 172.287 1.00 31.42  ? 58   LYS G CD    1 
ATOM   28637 C  CE    . LYS G 7  58   ? 110.147 159.691 172.508 1.00 33.59  ? 58   LYS G CE    1 
ATOM   28638 N  NZ    . LYS G 7  58   ? 110.743 160.905 171.894 1.00 31.93  ? 58   LYS G NZ    1 
ATOM   28639 N  N     . ASN G 7  59   ? 108.118 160.135 167.624 1.00 28.06  ? 59   ASN G N     1 
ATOM   28640 C  CA    . ASN G 7  59   ? 108.952 161.056 166.866 1.00 25.74  ? 59   ASN G CA    1 
ATOM   28641 C  C     . ASN G 7  59   ? 108.371 161.412 165.507 1.00 30.97  ? 59   ASN G C     1 
ATOM   28642 O  O     . ASN G 7  59   ? 108.778 162.419 164.925 1.00 32.61  ? 59   ASN G O     1 
ATOM   28643 C  CB    . ASN G 7  59   ? 110.342 160.459 166.657 1.00 27.54  ? 59   ASN G CB    1 
ATOM   28644 C  CG    . ASN G 7  59   ? 111.165 160.443 167.913 1.00 31.16  ? 59   ASN G CG    1 
ATOM   28645 O  OD1   . ASN G 7  59   ? 110.973 161.262 168.803 1.00 32.29  ? 59   ASN G OD1   1 
ATOM   28646 N  ND2   . ASN G 7  59   ? 112.099 159.514 167.990 1.00 31.30  ? 59   ASN G ND2   1 
ATOM   28647 N  N     . ALA G 7  60   ? 107.412 160.632 165.016 1.00 29.24  ? 60   ALA G N     1 
ATOM   28648 C  CA    . ALA G 7  60   ? 106.882 160.814 163.665 1.00 25.46  ? 60   ALA G CA    1 
ATOM   28649 C  C     . ALA G 7  60   ? 106.386 162.226 163.375 1.00 25.17  ? 60   ALA G C     1 
ATOM   28650 O  O     . ALA G 7  60   ? 106.564 162.689 162.237 1.00 30.79  ? 60   ALA G O     1 
ATOM   28651 C  CB    . ALA G 7  60   ? 105.786 159.778 163.410 1.00 24.13  ? 60   ALA G CB    1 
ATOM   28652 N  N     . PRO G 7  61   ? 105.737 162.945 164.297 1.00 25.55  ? 61   PRO G N     1 
ATOM   28653 C  CA    . PRO G 7  61   ? 105.359 164.334 163.992 1.00 22.92  ? 61   PRO G CA    1 
ATOM   28654 C  C     . PRO G 7  61   ? 106.532 165.259 163.744 1.00 25.96  ? 61   PRO G C     1 
ATOM   28655 O  O     . PRO G 7  61   ? 106.331 166.332 163.167 1.00 28.54  ? 61   PRO G O     1 
ATOM   28656 C  CB    . PRO G 7  61   ? 104.579 164.772 165.236 1.00 27.56  ? 61   PRO G CB    1 
ATOM   28657 C  CG    . PRO G 7  61   ? 104.149 163.532 165.867 1.00 31.57  ? 61   PRO G CG    1 
ATOM   28658 C  CD    . PRO G 7  61   ? 105.204 162.532 165.604 1.00 30.42  ? 61   PRO G CD    1 
ATOM   28659 N  N     . PHE G 7  62   ? 107.740 164.906 164.175 1.00 29.40  ? 62   PHE G N     1 
ATOM   28660 C  CA    . PHE G 7  62   ? 108.871 165.815 164.070 1.00 29.19  ? 62   PHE G CA    1 
ATOM   28661 C  C     . PHE G 7  62   ? 109.878 165.422 163.005 1.00 28.41  ? 62   PHE G C     1 
ATOM   28662 O  O     . PHE G 7  62   ? 110.709 166.253 162.634 1.00 33.97  ? 62   PHE G O     1 
ATOM   28663 C  CB    . PHE G 7  62   ? 109.584 165.933 165.424 1.00 29.41  ? 62   PHE G CB    1 
ATOM   28664 C  CG    . PHE G 7  62   ? 108.711 166.484 166.512 1.00 31.74  ? 62   PHE G CG    1 
ATOM   28665 C  CD1   . PHE G 7  62   ? 108.584 167.845 166.686 1.00 30.42  ? 62   PHE G CD1   1 
ATOM   28666 C  CD2   . PHE G 7  62   ? 107.995 165.640 167.339 1.00 29.85  ? 62   PHE G CD2   1 
ATOM   28667 C  CE1   . PHE G 7  62   ? 107.779 168.353 167.677 1.00 30.26  ? 62   PHE G CE1   1 
ATOM   28668 C  CE2   . PHE G 7  62   ? 107.186 166.143 168.327 1.00 28.39  ? 62   PHE G CE2   1 
ATOM   28669 C  CZ    . PHE G 7  62   ? 107.076 167.500 168.497 1.00 29.26  ? 62   PHE G CZ    1 
ATOM   28670 N  N     . ASP G 7  63   ? 109.824 164.201 162.509 1.00 25.06  ? 63   ASP G N     1 
ATOM   28671 C  CA    . ASP G 7  63   ? 110.665 163.805 161.397 1.00 24.93  ? 63   ASP G CA    1 
ATOM   28672 C  C     . ASP G 7  63   ? 110.174 164.518 160.149 1.00 27.97  ? 63   ASP G C     1 
ATOM   28673 O  O     . ASP G 7  63   ? 109.005 164.358 159.783 1.00 31.65  ? 63   ASP G O     1 
ATOM   28674 C  CB    . ASP G 7  63   ? 110.605 162.297 161.216 1.00 25.83  ? 63   ASP G CB    1 
ATOM   28675 C  CG    . ASP G 7  63   ? 111.738 161.759 160.380 1.00 31.62  ? 63   ASP G CG    1 
ATOM   28676 O  OD1   . ASP G 7  63   ? 112.667 162.525 160.059 1.00 32.97  ? 63   ASP G OD1   1 
ATOM   28677 O  OD2   . ASP G 7  63   ? 111.699 160.560 160.046 1.00 30.60  ? 63   ASP G OD2   1 
ATOM   28678 N  N     . PRO G 7  64   ? 111.003 165.322 159.478 1.00 28.11  ? 64   PRO G N     1 
ATOM   28679 C  CA    . PRO G 7  64   ? 110.510 166.082 158.324 1.00 27.91  ? 64   PRO G CA    1 
ATOM   28680 C  C     . PRO G 7  64   ? 110.377 165.254 157.063 1.00 28.79  ? 64   PRO G C     1 
ATOM   28681 O  O     . PRO G 7  64   ? 109.833 165.751 156.071 1.00 31.59  ? 64   PRO G O     1 
ATOM   28682 C  CB    . PRO G 7  64   ? 111.565 167.176 158.156 1.00 24.47  ? 64   PRO G CB    1 
ATOM   28683 C  CG    . PRO G 7  64   ? 112.798 166.563 158.670 1.00 28.30  ? 64   PRO G CG    1 
ATOM   28684 C  CD    . PRO G 7  64   ? 112.404 165.646 159.786 1.00 25.07  ? 64   PRO G CD    1 
ATOM   28685 N  N     . THR G 7  65   ? 110.838 164.011 157.076 1.00 20.57  ? 65   THR G N     1 
ATOM   28686 C  CA    . THR G 7  65   ? 110.783 163.134 155.924 1.00 19.50  ? 65   THR G CA    1 
ATOM   28687 C  C     . THR G 7  65   ? 109.561 162.236 155.933 1.00 23.16  ? 65   THR G C     1 
ATOM   28688 O  O     . THR G 7  65   ? 109.525 161.257 155.186 1.00 27.45  ? 65   THR G O     1 
ATOM   28689 C  CB    . THR G 7  65   ? 112.047 162.282 155.859 1.00 21.50  ? 65   THR G CB    1 
ATOM   28690 O  OG1   . THR G 7  65   ? 111.980 161.248 156.843 1.00 23.09  ? 65   THR G OG1   1 
ATOM   28691 C  CG2   . THR G 7  65   ? 113.246 163.126 156.137 1.00 20.98  ? 65   THR G CG2   1 
ATOM   28692 N  N     . ASN G 7  66   ? 108.574 162.533 156.770 1.00 24.96  ? 66   ASN G N     1 
ATOM   28693 C  CA    . ASN G 7  66   ? 107.366 161.733 156.878 1.00 24.96  ? 66   ASN G CA    1 
ATOM   28694 C  C     . ASN G 7  66   ? 106.247 162.347 156.051 1.00 27.96  ? 66   ASN G C     1 
ATOM   28695 O  O     . ASN G 7  66   ? 106.142 163.567 155.923 1.00 32.54  ? 66   ASN G O     1 
ATOM   28696 C  CB    . ASN G 7  66   ? 106.928 161.608 158.339 1.00 20.80  ? 66   ASN G CB    1 
ATOM   28697 C  CG    . ASN G 7  66   ? 107.646 160.498 159.073 1.00 28.24  ? 66   ASN G CG    1 
ATOM   28698 O  OD1   . ASN G 7  66   ? 107.974 159.471 158.498 1.00 30.56  ? 66   ASN G OD1   1 
ATOM   28699 N  ND2   . ASN G 7  66   ? 107.894 160.703 160.351 1.00 29.18  ? 66   ASN G ND2   1 
ATOM   28700 N  N     . CYS G 7  67   ? 105.406 161.481 155.491 1.00 24.37  ? 67   CYS G N     1 
ATOM   28701 C  CA    . CYS G 7  67   ? 104.293 161.906 154.652 1.00 26.82  ? 67   CYS G CA    1 
ATOM   28702 C  C     . CYS G 7  67   ? 103.251 162.645 155.484 1.00 25.47  ? 67   CYS G C     1 
ATOM   28703 O  O     . CYS G 7  67   ? 102.972 162.261 156.621 1.00 30.18  ? 67   CYS G O     1 
ATOM   28704 C  CB    . CYS G 7  67   ? 103.667 160.695 153.967 1.00 26.72  ? 67   CYS G CB    1 
ATOM   28705 S  SG    . CYS G 7  67   ? 102.302 161.087 152.876 1.00 40.96  ? 67   CYS G SG    1 
ATOM   28706 N  N     . GLN G 7  68   ? 102.680 163.701 154.921 1.00 24.88  ? 68   GLN G N     1 
ATOM   28707 C  CA    . GLN G 7  68   ? 101.604 164.446 155.553 1.00 27.09  ? 68   GLN G CA    1 
ATOM   28708 C  C     . GLN G 7  68   ? 100.283 164.199 154.840 1.00 33.51  ? 68   GLN G C     1 
ATOM   28709 O  O     . GLN G 7  68   ? 100.238 163.650 153.738 1.00 35.44  ? 68   GLN G O     1 
ATOM   28710 C  CB    . GLN G 7  68   ? 101.895 165.944 155.568 1.00 25.60  ? 68   GLN G CB    1 
ATOM   28711 C  CG    . GLN G 7  68   ? 103.336 166.291 155.816 1.00 30.26  ? 68   GLN G CG    1 
ATOM   28712 C  CD    . GLN G 7  68   ? 103.674 166.366 157.282 1.00 30.33  ? 68   GLN G CD    1 
ATOM   28713 O  OE1   . GLN G 7  68   ? 103.644 167.435 157.879 1.00 31.78  ? 68   GLN G OE1   1 
ATOM   28714 N  NE2   . GLN G 7  68   ? 103.998 165.229 157.872 1.00 28.21  ? 68   GLN G NE2   1 
ATOM   28715 N  N     . ILE G 7  69   ? 99.201  164.594 155.502 1.00 34.78  ? 69   ILE G N     1 
ATOM   28716 C  CA    . ILE G 7  69   ? 97.847  164.490 154.980 1.00 31.83  ? 69   ILE G CA    1 
ATOM   28717 C  C     . ILE G 7  69   ? 97.096  165.763 155.332 1.00 31.14  ? 69   ILE G C     1 
ATOM   28718 O  O     . ILE G 7  69   ? 97.219  166.280 156.446 1.00 31.56  ? 69   ILE G O     1 
ATOM   28719 C  CB    . ILE G 7  69   ? 97.126  163.241 155.528 1.00 30.90  ? 69   ILE G CB    1 
ATOM   28720 C  CG1   . ILE G 7  69   ? 97.356  162.047 154.601 1.00 30.19  ? 69   ILE G CG1   1 
ATOM   28721 C  CG2   . ILE G 7  69   ? 95.646  163.496 155.746 1.00 30.58  ? 69   ILE G CG2   1 
ATOM   28722 C  CD1   . ILE G 7  69   ? 96.836  160.741 155.156 1.00 32.92  ? 69   ILE G CD1   1 
ATOM   28723 N  N     . LYS G 7  70   ? 96.337  166.281 154.367 1.00 31.95  ? 70   LYS G N     1 
ATOM   28724 C  CA    . LYS G 7  70   ? 95.532  167.489 154.548 1.00 33.53  ? 70   LYS G CA    1 
ATOM   28725 C  C     . LYS G 7  70   ? 94.254  167.106 155.287 1.00 34.71  ? 70   LYS G C     1 
ATOM   28726 O  O     . LYS G 7  70   ? 93.237  166.736 154.696 1.00 36.93  ? 70   LYS G O     1 
ATOM   28727 C  CB    . LYS G 7  70   ? 95.236  168.129 153.199 1.00 31.27  ? 70   LYS G CB    1 
ATOM   28728 C  CG    . LYS G 7  70   ? 94.869  169.602 153.221 1.00 32.06  ? 70   LYS G CG    1 
ATOM   28729 C  CD    . LYS G 7  70   ? 95.708  170.390 154.194 1.00 32.69  ? 70   LYS G CD    1 
ATOM   28730 C  CE    . LYS G 7  70   ? 95.086  171.736 154.457 1.00 32.81  ? 70   LYS G CE    1 
ATOM   28731 N  NZ    . LYS G 7  70   ? 94.884  172.500 153.200 1.00 34.32  ? 70   LYS G NZ    1 
ATOM   28732 N  N     . LYS G 7  71   ? 94.320  167.184 156.615 1.00 34.35  ? 71   LYS G N     1 
ATOM   28733 C  CA    . LYS G 7  71   ? 93.203  166.826 157.476 1.00 33.45  ? 71   LYS G CA    1 
ATOM   28734 C  C     . LYS G 7  71   ? 93.306  167.602 158.778 1.00 38.25  ? 71   LYS G C     1 
ATOM   28735 O  O     . LYS G 7  71   ? 94.382  167.684 159.371 1.00 40.83  ? 71   LYS G O     1 
ATOM   28736 C  CB    . LYS G 7  71   ? 93.178  165.326 157.766 1.00 34.21  ? 71   LYS G CB    1 
ATOM   28737 C  CG    . LYS G 7  71   ? 92.022  164.907 158.637 1.00 37.45  ? 71   LYS G CG    1 
ATOM   28738 C  CD    . LYS G 7  71   ? 92.005  163.413 158.882 1.00 38.76  ? 71   LYS G CD    1 
ATOM   28739 C  CE    . LYS G 7  71   ? 91.325  162.667 157.761 1.00 37.33  ? 71   LYS G CE    1 
ATOM   28740 N  NZ    . LYS G 7  71   ? 91.138  161.238 158.116 1.00 37.30  ? 71   LYS G NZ    1 
ATOM   28741 N  N     . ASP G 7  72   ? 92.184  168.160 159.223 1.00 43.67  ? 72   ASP G N     1 
ATOM   28742 C  CA    . ASP G 7  72   ? 92.173  169.000 160.413 1.00 41.43  ? 72   ASP G CA    1 
ATOM   28743 C  C     . ASP G 7  72   ? 92.359  168.164 161.676 1.00 39.64  ? 72   ASP G C     1 
ATOM   28744 O  O     . ASP G 7  72   ? 91.889  167.030 161.771 1.00 43.14  ? 72   ASP G O     1 
ATOM   28745 C  CB    . ASP G 7  72   ? 90.864  169.789 160.478 1.00 42.53  ? 72   ASP G CB    1 
ATOM   28746 C  CG    . ASP G 7  72   ? 90.928  170.961 161.438 1.00 46.50  ? 72   ASP G CG    1 
ATOM   28747 O  OD1   . ASP G 7  72   ? 91.613  171.955 161.127 1.00 47.07  ? 72   ASP G OD1   1 
ATOM   28748 O  OD2   . ASP G 7  72   ? 90.272  170.900 162.499 1.00 47.06  ? 72   ASP G OD2   1 
ATOM   28749 N  N     . CYS G 7  73   ? 93.053  168.742 162.660 1.00 37.43  ? 73   CYS G N     1 
ATOM   28750 C  CA    . CYS G 7  73   ? 93.282  168.029 163.914 1.00 39.20  ? 73   CYS G CA    1 
ATOM   28751 C  C     . CYS G 7  73   ? 92.187  168.333 164.926 1.00 42.82  ? 73   CYS G C     1 
ATOM   28752 O  O     . CYS G 7  73   ? 91.842  169.498 165.138 1.00 44.87  ? 73   CYS G O     1 
ATOM   28753 C  CB    . CYS G 7  73   ? 94.631  168.405 164.523 1.00 38.55  ? 73   CYS G CB    1 
ATOM   28754 S  SG    . CYS G 7  73   ? 95.056  167.467 166.004 1.00 48.07  ? 73   CYS G SG    1 
ATOM   28755 N  N     . PRO G 7  74   ? 91.633  167.311 165.566 1.00 40.78  ? 74   PRO G N     1 
ATOM   28756 C  CA    . PRO G 7  74   ? 90.589  167.546 166.570 1.00 39.11  ? 74   PRO G CA    1 
ATOM   28757 C  C     . PRO G 7  74   ? 91.079  168.258 167.825 1.00 39.51  ? 74   PRO G C     1 
ATOM   28758 O  O     . PRO G 7  74   ? 90.309  168.983 168.459 1.00 41.63  ? 74   PRO G O     1 
ATOM   28759 C  CB    . PRO G 7  74   ? 90.096  166.132 166.887 1.00 36.63  ? 74   PRO G CB    1 
ATOM   28760 C  CG    . PRO G 7  74   ? 91.234  165.255 166.553 1.00 36.34  ? 74   PRO G CG    1 
ATOM   28761 C  CD    . PRO G 7  74   ? 91.910  165.878 165.383 1.00 37.95  ? 74   PRO G CD    1 
ATOM   28762 N  N     . ASN G 7  75   ? 92.344  168.071 168.197 1.00 43.11  ? 75   ASN G N     1 
ATOM   28763 C  CA    . ASN G 7  75   ? 92.827  168.631 169.455 1.00 42.94  ? 75   ASN G CA    1 
ATOM   28764 C  C     . ASN G 7  75   ? 93.235  170.096 169.317 1.00 44.50  ? 75   ASN G C     1 
ATOM   28765 O  O     . ASN G 7  75   ? 92.651  170.974 169.959 1.00 47.21  ? 75   ASN G O     1 
ATOM   28766 C  CB    . ASN G 7  75   ? 93.990  167.796 169.990 1.00 40.96  ? 75   ASN G CB    1 
ATOM   28767 C  CG    . ASN G 7  75   ? 93.521  166.601 170.793 1.00 45.30  ? 75   ASN G CG    1 
ATOM   28768 O  OD1   . ASN G 7  75   ? 93.813  165.456 170.459 1.00 47.55  ? 75   ASN G OD1   1 
ATOM   28769 N  ND2   . ASN G 7  75   ? 92.779  166.867 171.857 1.00 44.85  ? 75   ASN G ND2   1 
ATOM   28770 N  N     . CYS G 7  76   ? 94.237  170.384 168.491 1.00 40.77  ? 76   CYS G N     1 
ATOM   28771 C  CA    . CYS G 7  76   ? 94.774  171.735 168.382 1.00 41.95  ? 76   CYS G CA    1 
ATOM   28772 C  C     . CYS G 7  76   ? 94.265  172.495 167.166 1.00 40.28  ? 76   CYS G C     1 
ATOM   28773 O  O     . CYS G 7  76   ? 94.672  173.641 166.961 1.00 39.16  ? 76   CYS G O     1 
ATOM   28774 C  CB    . CYS G 7  76   ? 96.307  171.693 168.357 1.00 40.64  ? 76   CYS G CB    1 
ATOM   28775 S  SG    . CYS G 7  76   ? 97.018  170.993 166.851 1.00 46.66  ? 76   CYS G SG    1 
ATOM   28776 N  N     . HIS G 7  77   ? 93.387  171.895 166.367 1.00 42.01  ? 77   HIS G N     1 
ATOM   28777 C  CA    . HIS G 7  77   ? 92.850  172.513 165.156 1.00 43.82  ? 77   HIS G CA    1 
ATOM   28778 C  C     . HIS G 7  77   ? 93.978  172.979 164.234 1.00 46.51  ? 77   HIS G C     1 
ATOM   28779 O  O     . HIS G 7  77   ? 94.169  174.167 163.974 1.00 42.21  ? 77   HIS G O     1 
ATOM   28780 C  CB    . HIS G 7  77   ? 91.897  173.660 165.498 1.00 43.20  ? 77   HIS G CB    1 
ATOM   28781 C  CG    . HIS G 7  77   ? 91.213  173.501 166.821 1.00 46.61  ? 77   HIS G CG    1 
ATOM   28782 N  ND1   . HIS G 7  77   ? 90.471  172.387 167.146 1.00 46.39  ? 77   HIS G ND1   1 
ATOM   28783 C  CD2   . HIS G 7  77   ? 91.177  174.308 167.908 1.00 44.82  ? 77   HIS G CD2   1 
ATOM   28784 C  CE1   . HIS G 7  77   ? 90.001  172.518 168.373 1.00 44.97  ? 77   HIS G CE1   1 
ATOM   28785 N  NE2   . HIS G 7  77   ? 90.416  173.674 168.858 1.00 45.96  ? 77   HIS G NE2   1 
ATOM   28786 N  N     . LEU G 7  78   ? 94.739  172.002 163.752 1.00 47.07  ? 78   LEU G N     1 
ATOM   28787 C  CA    . LEU G 7  78   ? 95.801  172.217 162.782 1.00 42.21  ? 78   LEU G CA    1 
ATOM   28788 C  C     . LEU G 7  78   ? 95.388  171.628 161.440 1.00 41.78  ? 78   LEU G C     1 
ATOM   28789 O  O     . LEU G 7  78   ? 94.747  170.578 161.376 1.00 40.91  ? 78   LEU G O     1 
ATOM   28790 C  CB    . LEU G 7  78   ? 97.105  171.586 163.264 1.00 37.25  ? 78   LEU G CB    1 
ATOM   28791 C  CG    . LEU G 7  78   ? 98.417  172.230 162.837 1.00 37.33  ? 78   LEU G CG    1 
ATOM   28792 C  CD1   . LEU G 7  78   ? 98.386  173.708 163.117 1.00 39.79  ? 78   LEU G CD1   1 
ATOM   28793 C  CD2   . LEU G 7  78   ? 99.560  171.586 163.599 1.00 38.16  ? 78   LEU G CD2   1 
ATOM   28794 N  N     . ASP G 7  79   ? 95.761  172.319 160.364 1.00 38.78  ? 79   ASP G N     1 
ATOM   28795 C  CA    . ASP G 7  79   ? 95.233  171.986 159.046 1.00 35.72  ? 79   ASP G CA    1 
ATOM   28796 C  C     . ASP G 7  79   ? 95.736  170.639 158.541 1.00 38.12  ? 79   ASP G C     1 
ATOM   28797 O  O     . ASP G 7  79   ? 95.015  169.943 157.821 1.00 37.27  ? 79   ASP G O     1 
ATOM   28798 C  CB    . ASP G 7  79   ? 95.598  173.088 158.057 1.00 34.29  ? 79   ASP G CB    1 
ATOM   28799 C  CG    . ASP G 7  79   ? 94.407  173.582 157.281 1.00 40.17  ? 79   ASP G CG    1 
ATOM   28800 O  OD1   . ASP G 7  79   ? 94.592  174.365 156.327 1.00 39.06  ? 79   ASP G OD1   1 
ATOM   28801 O  OD2   . ASP G 7  79   ? 93.277  173.184 157.624 1.00 42.46  ? 79   ASP G OD2   1 
ATOM   28802 N  N     . TYR G 7  80   ? 96.952  170.255 158.908 1.00 35.14  ? 80   TYR G N     1 
ATOM   28803 C  CA    . TYR G 7  80   ? 97.617  169.082 158.367 1.00 27.86  ? 80   TYR G CA    1 
ATOM   28804 C  C     . TYR G 7  80   ? 97.920  168.095 159.484 1.00 28.15  ? 80   TYR G C     1 
ATOM   28805 O  O     . TYR G 7  80   ? 98.047  168.467 160.652 1.00 30.86  ? 80   TYR G O     1 
ATOM   28806 C  CB    . TYR G 7  80   ? 98.919  169.471 157.663 1.00 28.93  ? 80   TYR G CB    1 
ATOM   28807 C  CG    . TYR G 7  80   ? 99.846  170.256 158.553 1.00 28.40  ? 80   TYR G CG    1 
ATOM   28808 C  CD1   . TYR G 7  80   ? 99.712  171.627 158.690 1.00 28.21  ? 80   TYR G CD1   1 
ATOM   28809 C  CD2   . TYR G 7  80   ? 100.841 169.625 159.278 1.00 26.55  ? 80   TYR G CD2   1 
ATOM   28810 C  CE1   . TYR G 7  80   ? 100.544 172.341 159.509 1.00 27.72  ? 80   TYR G CE1   1 
ATOM   28811 C  CE2   . TYR G 7  80   ? 101.675 170.339 160.102 1.00 26.35  ? 80   TYR G CE2   1 
ATOM   28812 C  CZ    . TYR G 7  80   ? 101.521 171.692 160.212 1.00 25.71  ? 80   TYR G CZ    1 
ATOM   28813 O  OH    . TYR G 7  80   ? 102.355 172.401 161.032 1.00 27.29  ? 80   TYR G OH    1 
ATOM   28814 N  N     . LEU G 7  81   ? 98.044  166.827 159.109 1.00 25.05  ? 81   LEU G N     1 
ATOM   28815 C  CA    . LEU G 7  81   ? 98.404  165.771 160.038 1.00 24.53  ? 81   LEU G CA    1 
ATOM   28816 C  C     . LEU G 7  81   ? 99.493  164.907 159.421 1.00 26.92  ? 81   LEU G C     1 
ATOM   28817 O  O     . LEU G 7  81   ? 99.740  164.950 158.217 1.00 34.06  ? 81   LEU G O     1 
ATOM   28818 C  CB    . LEU G 7  81   ? 97.196  164.908 160.408 1.00 29.05  ? 81   LEU G CB    1 
ATOM   28819 C  CG    . LEU G 7  81   ? 96.651  165.097 161.823 1.00 30.55  ? 81   LEU G CG    1 
ATOM   28820 C  CD1   . LEU G 7  81   ? 95.934  166.410 161.909 1.00 30.35  ? 81   LEU G CD1   1 
ATOM   28821 C  CD2   . LEU G 7  81   ? 95.722  163.973 162.192 1.00 28.38  ? 81   LEU G CD2   1 
ATOM   28822 N  N     . THR G 7  82   ? 100.152 164.125 160.265 1.00 20.96  ? 82   THR G N     1 
ATOM   28823 C  CA    . THR G 7  82   ? 101.200 163.211 159.836 1.00 19.73  ? 82   THR G CA    1 
ATOM   28824 C  C     . THR G 7  82   ? 100.622 161.808 159.776 1.00 21.85  ? 82   THR G C     1 
ATOM   28825 O  O     . THR G 7  82   ? 99.952  161.376 160.713 1.00 26.98  ? 82   THR G O     1 
ATOM   28826 C  CB    . THR G 7  82   ? 102.387 163.252 160.793 1.00 22.88  ? 82   THR G CB    1 
ATOM   28827 O  OG1   . THR G 7  82   ? 102.977 164.554 160.767 1.00 24.52  ? 82   THR G OG1   1 
ATOM   28828 C  CG2   . THR G 7  82   ? 103.419 162.216 160.404 1.00 21.83  ? 82   THR G CG2   1 
ATOM   28829 N  N     . GLN G 7  83   ? 100.869 161.102 158.682 1.00 21.79  ? 83   GLN G N     1 
ATOM   28830 C  CA    . GLN G 7  83   ? 100.376 159.744 158.523 1.00 19.60  ? 83   GLN G CA    1 
ATOM   28831 C  C     . GLN G 7  83   ? 101.541 158.774 158.413 1.00 18.09  ? 83   GLN G C     1 
ATOM   28832 O  O     . GLN G 7  83   ? 102.576 159.102 157.830 1.00 26.51  ? 83   GLN G O     1 
ATOM   28833 C  CB    . GLN G 7  83   ? 99.465  159.645 157.302 1.00 24.26  ? 83   GLN G CB    1 
ATOM   28834 C  CG    . GLN G 7  83   ? 100.163 159.518 155.973 1.00 26.96  ? 83   GLN G CG    1 
ATOM   28835 C  CD    . GLN G 7  83   ? 99.969  158.158 155.358 1.00 30.07  ? 83   GLN G CD    1 
ATOM   28836 O  OE1   . GLN G 7  83   ? 98.932  157.528 155.550 1.00 30.53  ? 83   GLN G OE1   1 
ATOM   28837 N  NE2   . GLN G 7  83   ? 100.965 157.692 154.615 1.00 26.03  ? 83   GLN G NE2   1 
ATOM   28838 N  N     . ILE G 7  84   ? 101.384 157.596 159.004 1.00 17.31  ? 84   ILE G N     1 
ATOM   28839 C  CA    . ILE G 7  84   ? 102.377 156.536 158.930 1.00 20.66  ? 84   ILE G CA    1 
ATOM   28840 C  C     . ILE G 7  84   ? 101.652 155.229 158.656 1.00 24.66  ? 84   ILE G C     1 
ATOM   28841 O  O     . ILE G 7  84   ? 100.441 155.128 158.864 1.00 29.04  ? 84   ILE G O     1 
ATOM   28842 C  CB    . ILE G 7  84   ? 103.226 156.439 160.214 1.00 21.57  ? 84   ILE G CB    1 
ATOM   28843 C  CG1   . ILE G 7  84   ? 102.336 156.401 161.452 1.00 23.22  ? 84   ILE G CG1   1 
ATOM   28844 C  CG2   . ILE G 7  84   ? 104.167 157.623 160.311 1.00 19.54  ? 84   ILE G CG2   1 
ATOM   28845 C  CD1   . ILE G 7  84   ? 103.069 156.659 162.744 1.00 25.40  ? 84   ILE G CD1   1 
ATOM   28846 N  N     . CYS G 7  85   ? 102.384 154.241 158.159 1.00 22.93  ? 85   CYS G N     1 
ATOM   28847 C  CA    . CYS G 7  85   ? 101.824 152.959 157.746 1.00 23.51  ? 85   CYS G CA    1 
ATOM   28848 C  C     . CYS G 7  85   ? 102.829 151.865 158.087 1.00 27.32  ? 85   CYS G C     1 
ATOM   28849 O  O     . CYS G 7  85   ? 103.656 151.489 157.257 1.00 26.82  ? 85   CYS G O     1 
ATOM   28850 C  CB    . CYS G 7  85   ? 101.494 152.983 156.266 1.00 26.33  ? 85   CYS G CB    1 
ATOM   28851 S  SG    . CYS G 7  85   ? 100.835 151.459 155.607 1.00 39.35  ? 85   CYS G SG    1 
ATOM   28852 N  N     . ILE G 7  86   ? 102.733 151.327 159.297 1.00 36.33  ? 86   ILE G N     1 
ATOM   28853 C  CA    . ILE G 7  86   ? 103.732 150.403 159.816 1.00 35.57  ? 86   ILE G CA    1 
ATOM   28854 C  C     . ILE G 7  86   ? 103.195 148.982 159.784 1.00 34.67  ? 86   ILE G C     1 
ATOM   28855 O  O     . ILE G 7  86   ? 102.004 148.734 159.993 1.00 33.11  ? 86   ILE G O     1 
ATOM   28856 C  CB    . ILE G 7  86   ? 104.164 150.780 161.247 1.00 33.15  ? 86   ILE G CB    1 
ATOM   28857 C  CG1   . ILE G 7  86   ? 102.963 151.283 162.045 1.00 34.72  ? 86   ILE G CG1   1 
ATOM   28858 C  CG2   . ILE G 7  86   ? 105.261 151.822 161.215 1.00 31.80  ? 86   ILE G CG2   1 
ATOM   28859 C  CD1   . ILE G 7  86   ? 103.131 151.161 163.542 1.00 37.59  ? 86   ILE G CD1   1 
ATOM   28860 N  N     . GLY G 7  87   ? 104.095 148.043 159.520 1.00 33.47  ? 87   GLY G N     1 
ATOM   28861 C  CA    . GLY G 7  87   ? 103.788 146.635 159.629 1.00 33.38  ? 87   GLY G CA    1 
ATOM   28862 C  C     . GLY G 7  87   ? 103.206 146.043 158.362 1.00 34.56  ? 87   GLY G C     1 
ATOM   28863 O  O     . GLY G 7  87   ? 102.878 146.729 157.398 1.00 33.56  ? 87   GLY G O     1 
ATOM   28864 N  N     . SER G 7  88   ? 103.078 144.717 158.380 1.00 38.67  ? 88   SER G N     1 
ATOM   28865 C  CA    . SER G 7  88   ? 102.533 143.993 157.243 1.00 35.80  ? 88   SER G CA    1 
ATOM   28866 C  C     . SER G 7  88   ? 101.024 144.094 157.159 1.00 34.49  ? 88   SER G C     1 
ATOM   28867 O  O     . SER G 7  88   ? 100.448 143.727 156.131 1.00 35.96  ? 88   SER G O     1 
ATOM   28868 C  CB    . SER G 7  88   ? 102.939 142.524 157.305 1.00 37.49  ? 88   SER G CB    1 
ATOM   28869 O  OG    . SER G 7  88   ? 102.997 141.976 156.002 1.00 41.91  ? 88   SER G OG    1 
ATOM   28870 N  N     . GLN G 7  89   ? 100.370 144.557 158.215 1.00 33.67  ? 89   GLN G N     1 
ATOM   28871 C  CA    . GLN G 7  89   ? 98.943  144.817 158.149 1.00 33.46  ? 89   GLN G CA    1 
ATOM   28872 C  C     . GLN G 7  89   ? 98.635  146.233 157.697 1.00 35.13  ? 89   GLN G C     1 
ATOM   28873 O  O     . GLN G 7  89   ? 97.460  146.563 157.513 1.00 33.90  ? 89   GLN G O     1 
ATOM   28874 C  CB    . GLN G 7  89   ? 98.294  144.539 159.504 1.00 32.09  ? 89   GLN G CB    1 
ATOM   28875 C  CG    . GLN G 7  89   ? 98.304  143.060 159.860 1.00 35.21  ? 89   GLN G CG    1 
ATOM   28876 C  CD    . GLN G 7  89   ? 97.612  142.212 158.810 1.00 36.63  ? 89   GLN G CD    1 
ATOM   28877 O  OE1   . GLN G 7  89   ? 96.510  142.529 158.372 1.00 40.41  ? 89   GLN G OE1   1 
ATOM   28878 N  NE2   . GLN G 7  89   ? 98.269  141.139 158.386 1.00 33.52  ? 89   GLN G NE2   1 
ATOM   28879 N  N     . LYS G 7  90   ? 99.658  147.060 157.502 1.00 30.38  ? 90   LYS G N     1 
ATOM   28880 C  CA    . LYS G 7  90   ? 99.506  148.418 157.000 1.00 27.13  ? 90   LYS G CA    1 
ATOM   28881 C  C     . LYS G 7  90   ? 98.506  149.201 157.842 1.00 27.55  ? 90   LYS G C     1 
ATOM   28882 O  O     . LYS G 7  90   ? 97.500  149.714 157.353 1.00 30.70  ? 90   LYS G O     1 
ATOM   28883 C  CB    . LYS G 7  90   ? 99.099  148.412 155.527 1.00 29.38  ? 90   LYS G CB    1 
ATOM   28884 C  CG    . LYS G 7  90   ? 99.934  147.494 154.656 1.00 28.11  ? 90   LYS G CG    1 
ATOM   28885 C  CD    . LYS G 7  90   ? 99.736  147.804 153.190 1.00 28.48  ? 90   LYS G CD    1 
ATOM   28886 C  CE    . LYS G 7  90   ? 99.895  149.284 152.904 1.00 30.31  ? 90   LYS G CE    1 
ATOM   28887 N  NZ    . LYS G 7  90   ? 101.206 149.605 152.288 1.00 28.18  ? 90   LYS G NZ    1 
ATOM   28888 N  N     . ILE G 7  91   ? 98.796  149.276 159.132 1.00 30.87  ? 91   ILE G N     1 
ATOM   28889 C  CA    . ILE G 7  91   ? 97.998  150.092 160.034 1.00 31.84  ? 91   ILE G CA    1 
ATOM   28890 C  C     . ILE G 7  91   ? 98.283  151.553 159.733 1.00 30.06  ? 91   ILE G C     1 
ATOM   28891 O  O     . ILE G 7  91   ? 99.443  151.964 159.641 1.00 32.23  ? 91   ILE G O     1 
ATOM   28892 C  CB    . ILE G 7  91   ? 98.306  149.761 161.503 1.00 33.39  ? 91   ILE G CB    1 
ATOM   28893 C  CG1   . ILE G 7  91   ? 98.167  148.264 161.771 1.00 32.99  ? 91   ILE G CG1   1 
ATOM   28894 C  CG2   . ILE G 7  91   ? 97.384  150.532 162.415 1.00 31.47  ? 91   ILE G CG2   1 
ATOM   28895 C  CD1   . ILE G 7  91   ? 99.475  147.575 162.040 1.00 32.49  ? 91   ILE G CD1   1 
ATOM   28896 N  N     . ILE G 7  92   ? 97.230  152.340 159.576 1.00 26.44  ? 92   ILE G N     1 
ATOM   28897 C  CA    . ILE G 7  92   ? 97.354  153.763 159.304 1.00 28.57  ? 92   ILE G CA    1 
ATOM   28898 C  C     . ILE G 7  92   ? 97.164  154.515 160.609 1.00 30.17  ? 92   ILE G C     1 
ATOM   28899 O  O     . ILE G 7  92   ? 96.121  154.392 161.260 1.00 35.68  ? 92   ILE G O     1 
ATOM   28900 C  CB    . ILE G 7  92   ? 96.339  154.216 158.245 1.00 29.27  ? 92   ILE G CB    1 
ATOM   28901 C  CG1   . ILE G 7  92   ? 96.609  153.497 156.926 1.00 32.08  ? 92   ILE G CG1   1 
ATOM   28902 C  CG2   . ILE G 7  92   ? 96.409  155.711 158.047 1.00 28.30  ? 92   ILE G CG2   1 
ATOM   28903 C  CD1   . ILE G 7  92   ? 97.881  153.928 156.238 1.00 30.12  ? 92   ILE G CD1   1 
ATOM   28904 N  N     . ILE G 7  93   ? 98.174  155.288 160.998 1.00 25.96  ? 93   ILE G N     1 
ATOM   28905 C  CA    . ILE G 7  93   ? 98.150  156.068 162.227 1.00 26.05  ? 93   ILE G CA    1 
ATOM   28906 C  C     . ILE G 7  93   ? 98.364  157.528 161.870 1.00 24.79  ? 93   ILE G C     1 
ATOM   28907 O  O     . ILE G 7  93   ? 99.305  157.859 161.146 1.00 30.32  ? 93   ILE G O     1 
ATOM   28908 C  CB    . ILE G 7  93   ? 99.227  155.604 163.225 1.00 27.62  ? 93   ILE G CB    1 
ATOM   28909 C  CG1   . ILE G 7  93   ? 99.171  154.094 163.433 1.00 28.23  ? 93   ILE G CG1   1 
ATOM   28910 C  CG2   . ILE G 7  93   ? 99.076  156.323 164.542 1.00 24.85  ? 93   ILE G CG2   1 
ATOM   28911 C  CD1   . ILE G 7  93   ? 100.350 153.554 164.199 1.00 26.32  ? 93   ILE G CD1   1 
ATOM   28912 N  N     . LEU G 7  94   ? 97.506  158.394 162.382 1.00 19.06  ? 94   LEU G N     1 
ATOM   28913 C  CA    . LEU G 7  94   ? 97.637  159.834 162.209 1.00 21.91  ? 94   LEU G CA    1 
ATOM   28914 C  C     . LEU G 7  94   ? 98.101  160.418 163.535 1.00 26.56  ? 94   LEU G C     1 
ATOM   28915 O  O     . LEU G 7  94   ? 97.527  160.110 164.581 1.00 37.32  ? 94   LEU G O     1 
ATOM   28916 C  CB    . LEU G 7  94   ? 96.318  160.458 161.767 1.00 24.86  ? 94   LEU G CB    1 
ATOM   28917 C  CG    . LEU G 7  94   ? 95.601  159.827 160.574 1.00 27.57  ? 94   LEU G CG    1 
ATOM   28918 C  CD1   . LEU G 7  94   ? 94.350  160.613 160.244 1.00 25.89  ? 94   LEU G CD1   1 
ATOM   28919 C  CD2   . LEU G 7  94   ? 96.515  159.744 159.366 1.00 24.52  ? 94   LEU G CD2   1 
ATOM   28920 N  N     . VAL G 7  95   ? 99.141  161.240 163.501 1.00 24.70  ? 95   VAL G N     1 
ATOM   28921 C  CA    . VAL G 7  95   ? 99.696  161.838 164.707 1.00 23.60  ? 95   VAL G CA    1 
ATOM   28922 C  C     . VAL G 7  95   ? 99.860  163.335 164.498 1.00 24.61  ? 95   VAL G C     1 
ATOM   28923 O  O     . VAL G 7  95   ? 99.939  163.820 163.368 1.00 31.29  ? 95   VAL G O     1 
ATOM   28924 C  CB    . VAL G 7  95   ? 101.038 161.187 165.100 1.00 22.17  ? 95   VAL G CB    1 
ATOM   28925 C  CG1   . VAL G 7  95   ? 100.838 159.728 165.436 1.00 24.88  ? 95   VAL G CG1   1 
ATOM   28926 C  CG2   . VAL G 7  95   ? 102.027 161.318 163.982 1.00 23.61  ? 95   VAL G CG2   1 
ATOM   28927 N  N     . CYS G 7  96   ? 99.913  164.071 165.603 1.00 30.25  ? 96   CYS G N     1 
ATOM   28928 C  CA    . CYS G 7  96   ? 100.066 165.516 165.569 1.00 29.05  ? 96   CYS G CA    1 
ATOM   28929 C  C     . CYS G 7  96   ? 101.183 165.950 166.502 1.00 31.04  ? 96   CYS G C     1 
ATOM   28930 O  O     . CYS G 7  96   ? 101.599 165.215 167.399 1.00 33.72  ? 96   CYS G O     1 
ATOM   28931 C  CB    . CYS G 7  96   ? 98.776  166.239 165.958 1.00 32.86  ? 96   CYS G CB    1 
ATOM   28932 S  SG    . CYS G 7  96   ? 98.862  168.032 165.812 1.00 42.46  ? 96   CYS G SG    1 
ATOM   28933 N  N     . ARG G 7  97   ? 101.669 167.168 166.262 1.00 33.50  ? 97   ARG G N     1 
ATOM   28934 C  CA    . ARG G 7  97   ? 102.707 167.740 167.110 1.00 35.63  ? 97   ARG G CA    1 
ATOM   28935 C  C     . ARG G 7  97   ? 102.212 167.966 168.530 1.00 39.63  ? 97   ARG G C     1 
ATOM   28936 O  O     . ARG G 7  97   ? 102.942 167.706 169.492 1.00 39.33  ? 97   ARG G O     1 
ATOM   28937 C  CB    . ARG G 7  97   ? 103.201 169.053 166.508 1.00 36.83  ? 97   ARG G CB    1 
ATOM   28938 C  CG    . ARG G 7  97   ? 104.615 169.401 166.887 1.00 37.49  ? 97   ARG G CG    1 
ATOM   28939 C  CD    . ARG G 7  97   ? 105.145 170.551 166.061 1.00 39.40  ? 97   ARG G CD    1 
ATOM   28940 N  NE    . ARG G 7  97   ? 106.384 170.191 165.385 1.00 43.25  ? 97   ARG G NE    1 
ATOM   28941 C  CZ    . ARG G 7  97   ? 106.976 170.931 164.459 1.00 42.77  ? 97   ARG G CZ    1 
ATOM   28942 N  NH1   . ARG G 7  97   ? 106.461 172.083 164.064 1.00 41.05  ? 97   ARG G NH1   1 
ATOM   28943 N  NH2   . ARG G 7  97   ? 108.111 170.503 163.914 1.00 39.95  ? 97   ARG G NH2   1 
ATOM   28944 N  N     . CYS G 7  98   ? 100.976 168.439 168.680 1.00 35.89  ? 98   CYS G N     1 
ATOM   28945 C  CA    . CYS G 7  98   ? 100.402 168.718 169.987 1.00 32.23  ? 98   CYS G CA    1 
ATOM   28946 C  C     . CYS G 7  98   ? 100.292 167.482 170.860 1.00 35.40  ? 98   CYS G C     1 
ATOM   28947 O  O     . CYS G 7  98   ? 100.158 167.619 172.079 1.00 38.28  ? 98   CYS G O     1 
ATOM   28948 C  CB    . CYS G 7  98   ? 99.021  169.346 169.815 1.00 33.28  ? 98   CYS G CB    1 
ATOM   28949 S  SG    . CYS G 7  98   ? 97.772  168.195 169.220 1.00 44.75  ? 98   CYS G SG    1 
ATOM   28950 N  N     . GLY G 7  99   ? 100.355 166.290 170.278 1.00 33.94  ? 99   GLY G N     1 
ATOM   28951 C  CA    . GLY G 7  99   ? 100.233 165.059 171.021 1.00 32.54  ? 99   GLY G CA    1 
ATOM   28952 C  C     . GLY G 7  99   ? 99.081  164.181 170.600 1.00 34.35  ? 99   GLY G C     1 
ATOM   28953 O  O     . GLY G 7  99   ? 98.977  163.053 171.090 1.00 34.99  ? 99   GLY G O     1 
ATOM   28954 N  N     . TYR G 7  100  ? 98.225  164.653 169.701 1.00 36.45  ? 100  TYR G N     1 
ATOM   28955 C  CA    . TYR G 7  100  ? 97.123  163.833 169.225 1.00 34.53  ? 100  TYR G CA    1 
ATOM   28956 C  C     . TYR G 7  100  ? 97.654  162.605 168.501 1.00 33.64  ? 100  TYR G C     1 
ATOM   28957 O  O     . TYR G 7  100  ? 98.759  162.614 167.957 1.00 39.24  ? 100  TYR G O     1 
ATOM   28958 C  CB    . TYR G 7  100  ? 96.223  164.644 168.297 1.00 34.37  ? 100  TYR G CB    1 
ATOM   28959 C  CG    . TYR G 7  100  ? 95.253  163.797 167.520 1.00 35.59  ? 100  TYR G CG    1 
ATOM   28960 C  CD1   . TYR G 7  100  ? 94.176  163.197 168.144 1.00 36.91  ? 100  TYR G CD1   1 
ATOM   28961 C  CD2   . TYR G 7  100  ? 95.428  163.574 166.167 1.00 35.82  ? 100  TYR G CD2   1 
ATOM   28962 C  CE1   . TYR G 7  100  ? 93.292  162.409 167.437 1.00 36.63  ? 100  TYR G CE1   1 
ATOM   28963 C  CE2   . TYR G 7  100  ? 94.551  162.786 165.457 1.00 38.36  ? 100  TYR G CE2   1 
ATOM   28964 C  CZ    . TYR G 7  100  ? 93.486  162.208 166.097 1.00 36.48  ? 100  TYR G CZ    1 
ATOM   28965 O  OH    . TYR G 7  100  ? 92.608  161.423 165.391 1.00 37.43  ? 100  TYR G OH    1 
ATOM   28966 N  N     . MET G 7  101  ? 96.875  161.533 168.520 1.00 30.05  ? 101  MET G N     1 
ATOM   28967 C  CA    . MET G 7  101  ? 97.249  160.316 167.822 1.00 28.22  ? 101  MET G CA    1 
ATOM   28968 C  C     . MET G 7  101  ? 95.985  159.511 167.579 1.00 31.58  ? 101  MET G C     1 
ATOM   28969 O  O     . MET G 7  101  ? 95.081  159.519 168.416 1.00 37.42  ? 101  MET G O     1 
ATOM   28970 C  CB    . MET G 7  101  ? 98.272  159.521 168.636 1.00 29.82  ? 101  MET G CB    1 
ATOM   28971 C  CG    . MET G 7  101  ? 98.257  158.029 168.405 1.00 32.12  ? 101  MET G CG    1 
ATOM   28972 S  SD    . MET G 7  101  ? 99.888  157.309 168.564 1.00 44.75  ? 101  MET G SD    1 
ATOM   28973 C  CE    . MET G 7  101  ? 99.494  155.570 168.437 1.00 33.10  ? 101  MET G CE    1 
ATOM   28974 N  N     . SER G 7  102  ? 95.908  158.849 166.430 1.00 32.61  ? 102  SER G N     1 
ATOM   28975 C  CA    . SER G 7  102  ? 94.732  158.058 166.112 1.00 33.20  ? 102  SER G CA    1 
ATOM   28976 C  C     . SER G 7  102  ? 94.771  156.710 166.823 1.00 37.63  ? 102  SER G C     1 
ATOM   28977 O  O     . SER G 7  102  ? 95.805  156.263 167.322 1.00 37.19  ? 102  SER G O     1 
ATOM   28978 C  CB    . SER G 7  102  ? 94.603  157.856 164.607 1.00 32.83  ? 102  SER G CB    1 
ATOM   28979 O  OG    . SER G 7  102  ? 93.757  158.840 164.048 1.00 36.35  ? 102  SER G OG    1 
ATOM   28980 N  N     . ASN G 7  103  ? 93.612  156.054 166.838 1.00 50.98  ? 103  ASN G N     1 
ATOM   28981 C  CA    . ASN G 7  103  ? 93.398  154.810 167.577 1.00 53.36  ? 103  ASN G CA    1 
ATOM   28982 C  C     . ASN G 7  103  ? 93.695  154.976 169.065 1.00 52.45  ? 103  ASN G C     1 
ATOM   28983 O  O     . ASN G 7  103  ? 94.356  154.132 169.675 1.00 53.36  ? 103  ASN G O     1 
ATOM   28984 C  CB    . ASN G 7  103  ? 94.209  153.655 166.984 1.00 52.45  ? 103  ASN G CB    1 
ATOM   28985 C  CG    . ASN G 7  103  ? 93.854  153.378 165.534 1.00 54.30  ? 103  ASN G CG    1 
ATOM   28986 O  OD1   . ASN G 7  103  ? 92.724  153.618 165.106 1.00 54.39  ? 103  ASN G OD1   1 
ATOM   28987 N  ND2   . ASN G 7  103  ? 94.812  152.854 164.776 1.00 52.09  ? 103  ASN G ND2   1 
ATOM   28988 N  N     . ARG G 7  104  ? 93.212  156.076 169.649 1.00 49.77  ? 104  ARG G N     1 
ATOM   28989 C  CA    . ARG G 7  104  ? 93.240  156.311 171.092 1.00 51.63  ? 104  ARG G CA    1 
ATOM   28990 C  C     . ARG G 7  104  ? 94.674  156.289 171.630 1.00 53.48  ? 104  ARG G C     1 
ATOM   28991 O  O     . ARG G 7  104  ? 95.046  155.486 172.487 1.00 54.07  ? 104  ARG G O     1 
ATOM   28992 C  CB    . ARG G 7  104  ? 92.358  155.290 171.821 1.00 51.45  ? 104  ARG G CB    1 
ATOM   28993 C  CG    . ARG G 7  104  ? 90.887  155.340 171.442 1.00 52.61  ? 104  ARG G CG    1 
ATOM   28994 C  CD    . ARG G 7  104  ? 90.268  156.690 171.770 1.00 54.22  ? 104  ARG G CD    1 
ATOM   28995 N  NE    . ARG G 7  104  ? 90.293  157.635 170.660 1.00 55.41  ? 104  ARG G NE    1 
ATOM   28996 C  CZ    . ARG G 7  104  ? 90.227  158.950 170.813 1.00 54.08  ? 104  ARG G CZ    1 
ATOM   28997 N  NH1   . ARG G 7  104  ? 90.086  159.498 172.007 1.00 53.28  ? 104  ARG G NH1   1 
ATOM   28998 N  NH2   . ARG G 7  104  ? 90.303  159.734 169.742 1.00 50.16  ? 104  ARG G NH2   1 
ATOM   28999 N  N     . GLY G 7  105  ? 95.468  157.215 171.108 1.00 43.20  ? 105  GLY G N     1 
ATOM   29000 C  CA    . GLY G 7  105  ? 96.819  157.401 171.593 1.00 43.85  ? 105  GLY G CA    1 
ATOM   29001 C  C     . GLY G 7  105  ? 96.915  158.555 172.569 1.00 44.36  ? 105  GLY G C     1 
ATOM   29002 O  O     . GLY G 7  105  ? 96.232  159.568 172.413 1.00 43.46  ? 105  GLY G O     1 
ATOM   29003 N  N     . MET H 8  1    ? 144.660 169.317 113.820 1.00 1.28   ? 1    MET H N     1 
ATOM   29004 C  CA    . MET H 8  1    ? 145.119 170.352 114.725 1.00 0.97   ? 1    MET H CA    1 
ATOM   29005 C  C     . MET H 8  1    ? 144.767 171.722 114.197 1.00 2.05   ? 1    MET H C     1 
ATOM   29006 O  O     . MET H 8  1    ? 144.995 172.723 114.854 1.00 4.73   ? 1    MET H O     1 
ATOM   29007 C  CB    . MET H 8  1    ? 146.622 170.248 114.931 1.00 7.48   ? 1    MET H CB    1 
ATOM   29008 C  CG    . MET H 8  1    ? 147.106 168.877 115.335 1.00 11.63  ? 1    MET H CG    1 
ATOM   29009 S  SD    . MET H 8  1    ? 148.806 168.915 115.883 1.00 16.80  ? 1    MET H SD    1 
ATOM   29010 C  CE    . MET H 8  1    ? 149.541 167.896 114.630 1.00 5.89   ? 1    MET H CE    1 
ATOM   29011 N  N     . LEU H 8  2    ? 144.210 171.754 112.993 1.00 4.77   ? 2    LEU H N     1 
ATOM   29012 C  CA    . LEU H 8  2    ? 143.813 172.981 112.327 1.00 9.94   ? 2    LEU H CA    1 
ATOM   29013 C  C     . LEU H 8  2    ? 142.488 172.724 111.636 1.00 0.93   ? 2    LEU H C     1 
ATOM   29014 O  O     . LEU H 8  2    ? 141.978 171.608 111.636 1.00 12.12  ? 2    LEU H O     1 
ATOM   29015 C  CB    . LEU H 8  2    ? 144.863 173.438 111.308 1.00 3.43   ? 2    LEU H CB    1 
ATOM   29016 C  CG    . LEU H 8  2    ? 146.258 173.829 111.779 1.00 3.73   ? 2    LEU H CG    1 
ATOM   29017 C  CD1   . LEU H 8  2    ? 147.240 173.720 110.646 1.00 3.71   ? 2    LEU H CD1   1 
ATOM   29018 C  CD2   . LEU H 8  2    ? 146.256 175.220 112.336 1.00 5.21   ? 2    LEU H CD2   1 
ATOM   29019 N  N     . ILE H 8  3    ? 141.918 173.764 111.052 1.00 15.03  ? 3    ILE H N     1 
ATOM   29020 C  CA    . ILE H 8  3    ? 140.770 173.551 110.168 1.00 1.10   ? 3    ILE H CA    1 
ATOM   29021 C  C     . ILE H 8  3    ? 141.249 172.814 108.925 1.00 5.52   ? 3    ILE H C     1 
ATOM   29022 O  O     . ILE H 8  3    ? 142.286 173.187 108.357 1.00 3.69   ? 3    ILE H O     1 
ATOM   29023 C  CB    . ILE H 8  3    ? 140.111 174.888 109.813 1.00 9.98   ? 3    ILE H CB    1 
ATOM   29024 C  CG1   . ILE H 8  3    ? 139.461 175.504 111.048 1.00 11.14  ? 3    ILE H CG1   1 
ATOM   29025 C  CG2   . ILE H 8  3    ? 139.062 174.721 108.741 1.00 13.12  ? 3    ILE H CG2   1 
ATOM   29026 C  CD1   . ILE H 8  3    ? 138.954 176.902 110.836 1.00 1.58   ? 3    ILE H CD1   1 
ATOM   29027 N  N     . PRO H 8  4    ? 140.563 171.764 108.479 1.00 5.53   ? 4    PRO H N     1 
ATOM   29028 C  CA    . PRO H 8  4    ? 141.080 170.967 107.367 1.00 2.92   ? 4    PRO H CA    1 
ATOM   29029 C  C     . PRO H 8  4    ? 141.201 171.780 106.089 1.00 2.99   ? 4    PRO H C     1 
ATOM   29030 O  O     . PRO H 8  4    ? 140.591 172.834 105.930 1.00 9.00   ? 4    PRO H O     1 
ATOM   29031 C  CB    . PRO H 8  4    ? 140.045 169.850 107.228 1.00 1.34   ? 4    PRO H CB    1 
ATOM   29032 C  CG    . PRO H 8  4    ? 138.831 170.390 107.851 1.00 0.02   ? 4    PRO H CG    1 
ATOM   29033 C  CD    . PRO H 8  4    ? 139.290 171.224 108.977 1.00 0.91   ? 4    PRO H CD    1 
ATOM   29034 N  N     . VAL H 8  5    ? 142.045 171.283 105.185 1.00 6.27   ? 5    VAL H N     1 
ATOM   29035 C  CA    . VAL H 8  5    ? 142.263 171.951 103.908 1.00 3.59   ? 5    VAL H CA    1 
ATOM   29036 C  C     . VAL H 8  5    ? 140.998 171.924 103.068 1.00 5.40   ? 5    VAL H C     1 
ATOM   29037 O  O     . VAL H 8  5    ? 140.647 172.908 102.413 1.00 14.79  ? 5    VAL H O     1 
ATOM   29038 C  CB    . VAL H 8  5    ? 143.452 171.312 103.170 1.00 10.60  ? 5    VAL H CB    1 
ATOM   29039 C  CG1   . VAL H 8  5    ? 143.573 171.868 101.789 1.00 0.12   ? 5    VAL H CG1   1 
ATOM   29040 C  CG2   . VAL H 8  5    ? 144.718 171.566 103.923 1.00 13.04  ? 5    VAL H CG2   1 
ATOM   29041 N  N     . VAL H 8  6    ? 140.300 170.795 103.067 1.00 4.61   ? 6    VAL H N     1 
ATOM   29042 C  CA    . VAL H 8  6    ? 139.052 170.626 102.342 1.00 12.33  ? 6    VAL H CA    1 
ATOM   29043 C  C     . VAL H 8  6    ? 138.018 170.069 103.307 1.00 12.15  ? 6    VAL H C     1 
ATOM   29044 O  O     . VAL H 8  6    ? 138.345 169.550 104.372 1.00 4.47   ? 6    VAL H O     1 
ATOM   29045 C  CB    . VAL H 8  6    ? 139.205 169.705 101.114 1.00 7.26   ? 6    VAL H CB    1 
ATOM   29046 C  CG1   . VAL H 8  6    ? 140.027 170.377 100.047 1.00 6.44   ? 6    VAL H CG1   1 
ATOM   29047 C  CG2   . VAL H 8  6    ? 139.835 168.407 101.504 1.00 1.55   ? 6    VAL H CG2   1 
ATOM   29048 N  N     . CYS H 8  7    ? 136.754 170.199 102.931 1.00 3.27   ? 7    CYS H N     1 
ATOM   29049 C  CA    . CYS H 8  7    ? 135.688 169.600 103.715 1.00 8.03   ? 7    CYS H CA    1 
ATOM   29050 C  C     . CYS H 8  7    ? 135.836 168.084 103.717 1.00 2.41   ? 7    CYS H C     1 
ATOM   29051 O  O     . CYS H 8  7    ? 135.997 167.465 102.667 1.00 5.62   ? 7    CYS H O     1 
ATOM   29052 C  CB    . CYS H 8  7    ? 134.336 170.013 103.149 1.00 6.83   ? 7    CYS H CB    1 
ATOM   29053 S  SG    . CYS H 8  7    ? 132.916 169.191 103.865 1.00 5.23   ? 7    CYS H SG    1 
ATOM   29054 N  N     . PHE H 8  8    ? 135.782 167.491 104.908 1.00 4.34   ? 8    PHE H N     1 
ATOM   29055 C  CA    . PHE H 8  8    ? 135.949 166.051 105.048 1.00 14.63  ? 8    PHE H CA    1 
ATOM   29056 C  C     . PHE H 8  8    ? 134.916 165.271 104.258 1.00 4.86   ? 8    PHE H C     1 
ATOM   29057 O  O     . PHE H 8  8    ? 135.163 164.124 103.883 1.00 3.65   ? 8    PHE H O     1 
ATOM   29058 C  CB    . PHE H 8  8    ? 135.838 165.652 106.514 1.00 5.37   ? 8    PHE H CB    1 
ATOM   29059 C  CG    . PHE H 8  8    ? 137.043 165.966 107.330 1.00 2.66   ? 8    PHE H CG    1 
ATOM   29060 C  CD1   . PHE H 8  8    ? 138.243 165.345 107.084 1.00 0.52   ? 8    PHE H CD1   1 
ATOM   29061 C  CD2   . PHE H 8  8    ? 136.968 166.875 108.365 1.00 4.24   ? 8    PHE H CD2   1 
ATOM   29062 C  CE1   . PHE H 8  8    ? 139.345 165.633 107.844 1.00 1.05   ? 8    PHE H CE1   1 
ATOM   29063 C  CE2   . PHE H 8  8    ? 138.067 167.161 109.124 1.00 3.50   ? 8    PHE H CE2   1 
ATOM   29064 C  CZ    . PHE H 8  8    ? 139.257 166.536 108.860 1.00 2.50   ? 8    PHE H CZ    1 
ATOM   29065 N  N     . THR H 8  9    ? 133.752 165.858 104.016 1.00 3.89   ? 9    THR H N     1 
ATOM   29066 C  CA    . THR H 8  9    ? 132.628 165.123 103.464 1.00 6.10   ? 9    THR H CA    1 
ATOM   29067 C  C     . THR H 8  9    ? 132.538 165.262 101.951 1.00 3.83   ? 9    THR H C     1 
ATOM   29068 O  O     . THR H 8  9    ? 132.348 164.269 101.252 1.00 5.65   ? 9    THR H O     1 
ATOM   29069 C  CB    . THR H 8  9    ? 131.333 165.587 104.128 1.00 2.15   ? 9    THR H CB    1 
ATOM   29070 O  OG1   . THR H 8  9    ? 131.411 165.337 105.530 1.00 9.30   ? 9    THR H OG1   1 
ATOM   29071 C  CG2   . THR H 8  9    ? 130.159 164.826 103.583 1.00 3.78   ? 9    THR H CG2   1 
ATOM   29072 N  N     . CYS H 8  10   ? 132.689 166.471 101.428 1.00 7.43   ? 10   CYS H N     1 
ATOM   29073 C  CA    . CYS H 8  10   ? 132.517 166.709 100.008 1.00 5.67   ? 10   CYS H CA    1 
ATOM   29074 C  C     . CYS H 8  10   ? 133.788 167.103 99.277  1.00 2.30   ? 10   CYS H C     1 
ATOM   29075 O  O     . CYS H 8  10   ? 133.868 166.883 98.068  1.00 1.96   ? 10   CYS H O     1 
ATOM   29076 C  CB    . CYS H 8  10   ? 131.455 167.789 99.774  1.00 13.03  ? 10   CYS H CB    1 
ATOM   29077 S  SG    . CYS H 8  10   ? 131.917 169.448 100.173 1.00 6.51   ? 10   CYS H SG    1 
ATOM   29078 N  N     . GLY H 8  11   ? 134.775 167.660 99.963  1.00 0.03   ? 11   GLY H N     1 
ATOM   29079 C  CA    . GLY H 8  11   ? 136.004 168.056 99.325  1.00 1.79   ? 11   GLY H CA    1 
ATOM   29080 C  C     . GLY H 8  11   ? 136.064 169.484 98.850  1.00 11.89  ? 11   GLY H C     1 
ATOM   29081 O  O     . GLY H 8  11   ? 137.003 169.834 98.136  1.00 4.69   ? 11   GLY H O     1 
ATOM   29082 N  N     . PHE H 8  12   ? 135.095 170.313 99.205  1.00 4.10   ? 12   PHE H N     1 
ATOM   29083 C  CA    . PHE H 8  12   ? 135.170 171.727 98.886  1.00 5.55   ? 12   PHE H CA    1 
ATOM   29084 C  C     . PHE H 8  12   ? 136.321 172.367 99.658  1.00 8.32   ? 12   PHE H C     1 
ATOM   29085 O  O     . PHE H 8  12   ? 136.521 172.062 100.835 1.00 4.39   ? 12   PHE H O     1 
ATOM   29086 C  CB    . PHE H 8  12   ? 133.845 172.412 99.226  1.00 3.36   ? 12   PHE H CB    1 
ATOM   29087 C  CG    . PHE H 8  12   ? 133.790 173.861 98.857  1.00 7.18   ? 12   PHE H CG    1 
ATOM   29088 C  CD1   . PHE H 8  12   ? 133.378 174.254 97.603  1.00 0.99   ? 12   PHE H CD1   1 
ATOM   29089 C  CD2   . PHE H 8  12   ? 134.153 174.831 99.769  1.00 6.26   ? 12   PHE H CD2   1 
ATOM   29090 C  CE1   . PHE H 8  12   ? 133.334 175.578 97.269  1.00 0.32   ? 12   PHE H CE1   1 
ATOM   29091 C  CE2   . PHE H 8  12   ? 134.121 176.152 99.438  1.00 1.80   ? 12   PHE H CE2   1 
ATOM   29092 C  CZ    . PHE H 8  12   ? 133.704 176.527 98.186  1.00 5.73   ? 12   PHE H CZ    1 
ATOM   29093 N  N     . PRO H 8  13   ? 137.097 173.242 99.037  1.00 1.66   ? 13   PRO H N     1 
ATOM   29094 C  CA    . PRO H 8  13   ? 138.263 173.798 99.729  1.00 0.11   ? 13   PRO H CA    1 
ATOM   29095 C  C     . PRO H 8  13   ? 137.912 174.848 100.771 1.00 9.78   ? 13   PRO H C     1 
ATOM   29096 O  O     . PRO H 8  13   ? 138.078 176.041 100.532 1.00 11.21  ? 13   PRO H O     1 
ATOM   29097 C  CB    . PRO H 8  13   ? 139.082 174.398 98.583  1.00 15.64  ? 13   PRO H CB    1 
ATOM   29098 C  CG    . PRO H 8  13   ? 138.090 174.716 97.558  1.00 14.70  ? 13   PRO H CG    1 
ATOM   29099 C  CD    . PRO H 8  13   ? 137.048 173.665 97.630  1.00 5.27   ? 13   PRO H CD    1 
ATOM   29100 N  N     . ILE H 8  14   ? 137.447 174.427 101.943 1.00 6.55   ? 14   ILE H N     1 
ATOM   29101 C  CA    . ILE H 8  14   ? 137.123 175.396 102.981 1.00 1.43   ? 14   ILE H CA    1 
ATOM   29102 C  C     . ILE H 8  14   ? 138.367 175.980 103.624 1.00 3.70   ? 14   ILE H C     1 
ATOM   29103 O  O     . ILE H 8  14   ? 138.266 176.954 104.369 1.00 11.12  ? 14   ILE H O     1 
ATOM   29104 C  CB    . ILE H 8  14   ? 136.238 174.775 104.074 1.00 10.86  ? 14   ILE H CB    1 
ATOM   29105 C  CG1   . ILE H 8  14   ? 136.880 173.506 104.620 1.00 9.12   ? 14   ILE H CG1   1 
ATOM   29106 C  CG2   . ILE H 8  14   ? 134.873 174.478 103.541 1.00 5.07   ? 14   ILE H CG2   1 
ATOM   29107 C  CD1   . ILE H 8  14   ? 136.470 173.159 105.994 1.00 5.73   ? 14   ILE H CD1   1 
ATOM   29108 N  N     . GLY H 8  15   ? 139.541 175.416 103.348 1.00 3.93   ? 15   GLY H N     1 
ATOM   29109 C  CA    . GLY H 8  15   ? 140.740 175.819 104.054 1.00 1.00   ? 15   GLY H CA    1 
ATOM   29110 C  C     . GLY H 8  15   ? 141.422 177.034 103.470 1.00 8.81   ? 15   GLY H C     1 
ATOM   29111 O  O     . GLY H 8  15   ? 142.365 177.557 104.064 1.00 17.20  ? 15   GLY H O     1 
ATOM   29112 N  N     . THR H 8  16   ? 140.977 177.493 102.303 1.00 5.66   ? 16   THR H N     1 
ATOM   29113 C  CA    . THR H 8  16   ? 141.522 178.727 101.759 1.00 4.90   ? 16   THR H CA    1 
ATOM   29114 C  C     . THR H 8  16   ? 140.945 179.952 102.448 1.00 10.77  ? 16   THR H C     1 
ATOM   29115 O  O     . THR H 8  16   ? 141.487 181.050 102.292 1.00 16.02  ? 16   THR H O     1 
ATOM   29116 C  CB    . THR H 8  16   ? 141.290 178.795 100.246 1.00 8.09   ? 16   THR H CB    1 
ATOM   29117 O  OG1   . THR H 8  16   ? 141.461 180.137 99.789  1.00 14.20  ? 16   THR H OG1   1 
ATOM   29118 C  CG2   . THR H 8  16   ? 139.928 178.332 99.886  1.00 1.48   ? 16   THR H CG2   1 
ATOM   29119 N  N     . TYR H 8  17   ? 139.875 179.791 103.220 1.00 11.35  ? 17   TYR H N     1 
ATOM   29120 C  CA    . TYR H 8  17   ? 139.299 180.878 103.991 1.00 6.44   ? 17   TYR H CA    1 
ATOM   29121 C  C     . TYR H 8  17   ? 139.408 180.682 105.491 1.00 9.52   ? 17   TYR H C     1 
ATOM   29122 O  O     . TYR H 8  17   ? 138.804 181.450 106.235 1.00 17.61  ? 17   TYR H O     1 
ATOM   29123 C  CB    . TYR H 8  17   ? 137.826 181.062 103.637 1.00 7.67   ? 17   TYR H CB    1 
ATOM   29124 C  CG    . TYR H 8  17   ? 137.487 180.835 102.198 1.00 9.96   ? 17   TYR H CG    1 
ATOM   29125 C  CD1   . TYR H 8  17   ? 136.891 179.660 101.787 1.00 9.26   ? 17   TYR H CD1   1 
ATOM   29126 C  CD2   . TYR H 8  17   ? 137.746 181.803 101.250 1.00 10.93  ? 17   TYR H CD2   1 
ATOM   29127 C  CE1   . TYR H 8  17   ? 136.572 179.455 100.480 1.00 6.77   ? 17   TYR H CE1   1 
ATOM   29128 C  CE2   . TYR H 8  17   ? 137.430 181.605 99.939  1.00 15.82  ? 17   TYR H CE2   1 
ATOM   29129 C  CZ    . TYR H 8  17   ? 136.842 180.432 99.560  1.00 16.67  ? 17   TYR H CZ    1 
ATOM   29130 O  OH    . TYR H 8  17   ? 136.524 180.230 98.248  1.00 21.35  ? 17   TYR H OH    1 
ATOM   29131 N  N     . ALA H 8  18   ? 140.152 179.682 105.953 1.00 7.24   ? 18   ALA H N     1 
ATOM   29132 C  CA    . ALA H 8  18   ? 140.134 179.323 107.364 1.00 3.40   ? 18   ALA H CA    1 
ATOM   29133 C  C     . ALA H 8  18   ? 140.746 180.413 108.239 1.00 10.25  ? 18   ALA H C     1 
ATOM   29134 O  O     . ALA H 8  18   ? 140.220 180.728 109.311 1.00 17.91  ? 18   ALA H O     1 
ATOM   29135 C  CB    . ALA H 8  18   ? 140.857 177.996 107.564 1.00 8.95   ? 18   ALA H CB    1 
ATOM   29136 N  N     . ALA H 8  19   ? 141.868 180.993 107.808 1.00 15.35  ? 19   ALA H N     1 
ATOM   29137 C  CA    . ALA H 8  19   ? 142.529 182.025 108.603 1.00 10.14  ? 19   ALA H CA    1 
ATOM   29138 C  C     . ALA H 8  19   ? 141.675 183.282 108.704 1.00 16.68  ? 19   ALA H C     1 
ATOM   29139 O  O     . ALA H 8  19   ? 141.504 183.854 109.794 1.00 23.73  ? 19   ALA H O     1 
ATOM   29140 C  CB    . ALA H 8  19   ? 143.888 182.353 107.995 1.00 8.03   ? 19   ALA H CB    1 
ATOM   29141 N  N     . ILE H 8  20   ? 141.133 183.730 107.570 1.00 12.37  ? 20   ILE H N     1 
ATOM   29142 C  CA    . ILE H 8  20   ? 140.250 184.887 107.577 1.00 10.64  ? 20   ILE H CA    1 
ATOM   29143 C  C     . ILE H 8  20   ? 139.041 184.613 108.452 1.00 8.29   ? 20   ILE H C     1 
ATOM   29144 O  O     . ILE H 8  20   ? 138.617 185.469 109.231 1.00 16.61  ? 20   ILE H O     1 
ATOM   29145 C  CB    . ILE H 8  20   ? 139.830 185.268 106.147 1.00 11.39  ? 20   ILE H CB    1 
ATOM   29146 C  CG1   . ILE H 8  20   ? 141.040 185.601 105.289 1.00 13.71  ? 20   ILE H CG1   1 
ATOM   29147 C  CG2   . ILE H 8  20   ? 138.887 186.444 106.164 1.00 6.86   ? 20   ILE H CG2   1 
ATOM   29148 C  CD1   . ILE H 8  20   ? 140.741 185.595 103.823 1.00 17.07  ? 20   ILE H CD1   1 
ATOM   29149 N  N     . PHE H 8  21   ? 138.469 183.415 108.343 1.00 8.78   ? 21   PHE H N     1 
ATOM   29150 C  CA    . PHE H 8  21   ? 137.288 183.101 109.130 1.00 7.97   ? 21   PHE H CA    1 
ATOM   29151 C  C     . PHE H 8  21   ? 137.595 183.125 110.617 1.00 13.91  ? 21   PHE H C     1 
ATOM   29152 O  O     . PHE H 8  21   ? 136.802 183.642 111.404 1.00 20.57  ? 21   PHE H O     1 
ATOM   29153 C  CB    . PHE H 8  21   ? 136.726 181.740 108.731 1.00 6.65   ? 21   PHE H CB    1 
ATOM   29154 C  CG    . PHE H 8  21   ? 135.631 181.265 109.626 1.00 10.53  ? 21   PHE H CG    1 
ATOM   29155 C  CD1   . PHE H 8  21   ? 134.392 181.869 109.598 1.00 7.44   ? 21   PHE H CD1   1 
ATOM   29156 C  CD2   . PHE H 8  21   ? 135.848 180.245 110.524 1.00 9.44   ? 21   PHE H CD2   1 
ATOM   29157 C  CE1   . PHE H 8  21   ? 133.395 181.453 110.430 1.00 6.85   ? 21   PHE H CE1   1 
ATOM   29158 C  CE2   . PHE H 8  21   ? 134.853 179.831 111.355 1.00 8.05   ? 21   PHE H CE2   1 
ATOM   29159 C  CZ    . PHE H 8  21   ? 133.625 180.431 111.304 1.00 6.74   ? 21   PHE H CZ    1 
ATOM   29160 N  N     . ASP H 8  22   ? 138.731 182.564 111.028 1.00 11.29  ? 22   ASP H N     1 
ATOM   29161 C  CA    . ASP H 8  22   ? 139.050 182.519 112.450 1.00 10.97  ? 22   ASP H CA    1 
ATOM   29162 C  C     . ASP H 8  22   ? 139.243 183.924 113.018 1.00 18.43  ? 22   ASP H C     1 
ATOM   29163 O  O     . ASP H 8  22   ? 138.674 184.274 114.062 1.00 22.52  ? 22   ASP H O     1 
ATOM   29164 C  CB    . ASP H 8  22   ? 140.285 181.654 112.676 1.00 17.30  ? 22   ASP H CB    1 
ATOM   29165 C  CG    . ASP H 8  22   ? 140.664 181.544 114.143 1.00 26.44  ? 22   ASP H CG    1 
ATOM   29166 O  OD1   . ASP H 8  22   ? 139.883 180.960 114.923 1.00 22.92  ? 22   ASP H OD1   1 
ATOM   29167 O  OD2   . ASP H 8  22   ? 141.752 182.033 114.516 1.00 26.60  ? 22   ASP H OD2   1 
ATOM   29168 N  N     . LYS H 8  23   ? 140.018 184.761 112.326 1.00 15.51  ? 23   LYS H N     1 
ATOM   29169 C  CA    . LYS H 8  23   ? 140.216 186.121 112.821 1.00 15.63  ? 23   LYS H CA    1 
ATOM   29170 C  C     . LYS H 8  23   ? 138.916 186.918 112.816 1.00 18.53  ? 23   LYS H C     1 
ATOM   29171 O  O     . LYS H 8  23   ? 138.611 187.645 113.773 1.00 22.17  ? 23   LYS H O     1 
ATOM   29172 C  CB    . LYS H 8  23   ? 141.272 186.840 111.996 1.00 14.08  ? 23   LYS H CB    1 
ATOM   29173 C  CG    . LYS H 8  23   ? 142.571 187.011 112.719 1.00 16.62  ? 23   LYS H CG    1 
ATOM   29174 C  CD    . LYS H 8  23   ? 143.387 188.093 112.061 1.00 24.49  ? 23   LYS H CD    1 
ATOM   29175 C  CE    . LYS H 8  23   ? 142.980 189.447 112.601 1.00 26.05  ? 23   LYS H CE    1 
ATOM   29176 N  NZ    . LYS H 8  23   ? 143.825 189.865 113.750 1.00 22.51  ? 23   LYS H NZ    1 
ATOM   29177 N  N     . ALA H 8  24   ? 138.141 186.809 111.737 1.00 13.33  ? 24   ALA H N     1 
ATOM   29178 C  CA    . ALA H 8  24   ? 136.906 187.569 111.627 1.00 11.87  ? 24   ALA H CA    1 
ATOM   29179 C  C     . ALA H 8  24   ? 135.891 187.123 112.666 1.00 16.61  ? 24   ALA H C     1 
ATOM   29180 O  O     . ALA H 8  24   ? 135.142 187.939 113.204 1.00 21.94  ? 24   ALA H O     1 
ATOM   29181 C  CB    . ALA H 8  24   ? 136.342 187.433 110.217 1.00 12.30  ? 24   ALA H CB    1 
ATOM   29182 N  N     . ARG H 8  25   ? 135.846 185.826 112.961 1.00 15.10  ? 25   ARG H N     1 
ATOM   29183 C  CA    . ARG H 8  25   ? 134.961 185.341 114.005 1.00 12.12  ? 25   ARG H CA    1 
ATOM   29184 C  C     . ARG H 8  25   ? 135.371 185.883 115.362 1.00 16.73  ? 25   ARG H C     1 
ATOM   29185 O  O     . ARG H 8  25   ? 134.519 186.266 116.169 1.00 27.01  ? 25   ARG H O     1 
ATOM   29186 C  CB    . ARG H 8  25   ? 134.949 183.815 114.025 1.00 13.54  ? 25   ARG H CB    1 
ATOM   29187 C  CG    . ARG H 8  25   ? 134.284 183.254 115.252 1.00 16.53  ? 25   ARG H CG    1 
ATOM   29188 C  CD    . ARG H 8  25   ? 134.204 181.772 115.197 1.00 14.49  ? 25   ARG H CD    1 
ATOM   29189 N  NE    . ARG H 8  25   ? 135.518 181.153 115.161 1.00 17.02  ? 25   ARG H NE    1 
ATOM   29190 C  CZ    . ARG H 8  25   ? 135.719 179.845 115.114 1.00 20.65  ? 25   ARG H CZ    1 
ATOM   29191 N  NH1   . ARG H 8  25   ? 134.710 178.993 115.100 1.00 14.95  ? 25   ARG H NH1   1 
ATOM   29192 N  NH2   . ARG H 8  25   ? 136.962 179.381 115.071 1.00 20.10  ? 25   ARG H NH2   1 
ATOM   29193 N  N     . THR H 8  26   ? 136.675 185.921 115.638 1.00 17.17  ? 26   THR H N     1 
ATOM   29194 C  CA    . THR H 8  26   ? 137.126 186.518 116.893 1.00 19.85  ? 26   THR H CA    1 
ATOM   29195 C  C     . THR H 8  26   ? 136.643 187.960 117.018 1.00 20.53  ? 26   THR H C     1 
ATOM   29196 O  O     . THR H 8  26   ? 136.051 188.347 118.035 1.00 23.39  ? 26   THR H O     1 
ATOM   29197 C  CB    . THR H 8  26   ? 138.649 186.455 116.989 1.00 22.12  ? 26   THR H CB    1 
ATOM   29198 O  OG1   . THR H 8  26   ? 139.048 185.134 117.363 1.00 29.68  ? 26   THR H OG1   1 
ATOM   29199 C  CG2   . THR H 8  26   ? 139.148 187.413 118.032 1.00 21.21  ? 26   THR H CG2   1 
ATOM   29200 N  N     . GLU H 8  27   ? 136.861 188.758 115.970 1.00 21.75  ? 27   GLU H N     1 
ATOM   29201 C  CA    . GLU H 8  27   ? 136.448 190.161 116.002 1.00 19.81  ? 27   GLU H CA    1 
ATOM   29202 C  C     . GLU H 8  27   ? 134.939 190.308 116.154 1.00 20.03  ? 27   GLU H C     1 
ATOM   29203 O  O     . GLU H 8  27   ? 134.461 191.164 116.905 1.00 27.41  ? 27   GLU H O     1 
ATOM   29204 C  CB    . GLU H 8  27   ? 136.915 190.877 114.739 1.00 21.40  ? 27   GLU H CB    1 
ATOM   29205 C  CG    . GLU H 8  27   ? 138.236 191.611 114.866 1.00 23.06  ? 27   GLU H CG    1 
ATOM   29206 C  CD    . GLU H 8  27   ? 139.372 190.730 115.333 1.00 30.68  ? 27   GLU H CD    1 
ATOM   29207 O  OE1   . GLU H 8  27   ? 139.669 190.737 116.545 1.00 30.82  ? 27   GLU H OE1   1 
ATOM   29208 O  OE2   . GLU H 8  27   ? 139.984 190.049 114.485 1.00 30.64  ? 27   GLU H OE2   1 
ATOM   29209 N  N     . TYR H 8  28   ? 134.175 189.490 115.436 1.00 20.63  ? 28   TYR H N     1 
ATOM   29210 C  CA    . TYR H 8  28   ? 132.720 189.567 115.472 1.00 22.53  ? 28   TYR H CA    1 
ATOM   29211 C  C     . TYR H 8  28   ? 132.163 189.214 116.847 1.00 23.86  ? 28   TYR H C     1 
ATOM   29212 O  O     . TYR H 8  28   ? 131.255 189.884 117.352 1.00 20.27  ? 28   TYR H O     1 
ATOM   29213 C  CB    . TYR H 8  28   ? 132.164 188.630 114.408 1.00 19.62  ? 28   TYR H CB    1 
ATOM   29214 C  CG    . TYR H 8  28   ? 130.702 188.777 114.119 1.00 22.72  ? 28   TYR H CG    1 
ATOM   29215 C  CD1   . TYR H 8  28   ? 130.242 189.768 113.281 1.00 23.44  ? 28   TYR H CD1   1 
ATOM   29216 C  CD2   . TYR H 8  28   ? 129.785 187.903 114.664 1.00 22.03  ? 28   TYR H CD2   1 
ATOM   29217 C  CE1   . TYR H 8  28   ? 128.912 189.893 113.009 1.00 24.69  ? 28   TYR H CE1   1 
ATOM   29218 C  CE2   . TYR H 8  28   ? 128.456 188.023 114.398 1.00 22.63  ? 28   TYR H CE2   1 
ATOM   29219 C  CZ    . TYR H 8  28   ? 128.021 189.019 113.569 1.00 24.98  ? 28   TYR H CZ    1 
ATOM   29220 O  OH    . TYR H 8  28   ? 126.684 189.144 113.294 1.00 28.47  ? 28   TYR H OH    1 
ATOM   29221 N  N     . ILE H 8  29   ? 132.680 188.153 117.461 1.00 22.40  ? 29   ILE H N     1 
ATOM   29222 C  CA    . ILE H 8  29   ? 132.215 187.781 118.791 1.00 24.46  ? 29   ILE H CA    1 
ATOM   29223 C  C     . ILE H 8  29   ? 132.584 188.854 119.804 1.00 28.08  ? 29   ILE H C     1 
ATOM   29224 O  O     . ILE H 8  29   ? 131.796 189.177 120.702 1.00 25.13  ? 29   ILE H O     1 
ATOM   29225 C  CB    . ILE H 8  29   ? 132.776 186.409 119.186 1.00 23.34  ? 29   ILE H CB    1 
ATOM   29226 C  CG1   . ILE H 8  29   ? 132.066 185.311 118.405 1.00 23.16  ? 29   ILE H CG1   1 
ATOM   29227 C  CG2   . ILE H 8  29   ? 132.625 186.182 120.666 1.00 23.51  ? 29   ILE H CG2   1 
ATOM   29228 C  CD1   . ILE H 8  29   ? 132.676 183.967 118.595 1.00 25.90  ? 29   ILE H CD1   1 
ATOM   29229 N  N     . LYS H 8  30   ? 133.783 189.428 119.682 1.00 30.46  ? 30   LYS H N     1 
ATOM   29230 C  CA    . LYS H 8  30   ? 134.135 190.526 120.568 1.00 28.44  ? 30   LYS H CA    1 
ATOM   29231 C  C     . LYS H 8  30   ? 133.189 191.704 120.401 1.00 30.65  ? 30   LYS H C     1 
ATOM   29232 O  O     . LYS H 8  30   ? 132.784 192.306 121.398 1.00 35.57  ? 30   LYS H O     1 
ATOM   29233 C  CB    . LYS H 8  30   ? 135.577 190.954 120.316 1.00 27.92  ? 30   LYS H CB    1 
ATOM   29234 C  CG    . LYS H 8  30   ? 136.024 192.156 121.104 1.00 28.66  ? 30   LYS H CG    1 
ATOM   29235 C  CD    . LYS H 8  30   ? 137.535 192.253 121.100 1.00 29.63  ? 30   LYS H CD    1 
ATOM   29236 C  CE    . LYS H 8  30   ? 138.008 193.699 121.100 1.00 31.76  ? 30   LYS H CE    1 
ATOM   29237 N  NZ    . LYS H 8  30   ? 137.125 194.588 120.292 1.00 31.65  ? 30   LYS H NZ    1 
ATOM   29238 N  N     . THR H 8  31   ? 132.811 192.028 119.168 1.00 26.38  ? 31   THR H N     1 
ATOM   29239 C  CA    . THR H 8  31   ? 131.842 193.095 118.948 1.00 24.29  ? 31   THR H CA    1 
ATOM   29240 C  C     . THR H 8  31   ? 130.500 192.774 119.594 1.00 24.99  ? 31   THR H C     1 
ATOM   29241 O  O     . THR H 8  31   ? 129.880 193.646 120.208 1.00 29.18  ? 31   THR H O     1 
ATOM   29242 C  CB    . THR H 8  31   ? 131.676 193.345 117.451 1.00 26.35  ? 31   THR H CB    1 
ATOM   29243 O  OG1   . THR H 8  31   ? 132.677 194.265 117.011 1.00 26.32  ? 31   THR H OG1   1 
ATOM   29244 C  CG2   . THR H 8  31   ? 130.308 193.911 117.142 1.00 26.10  ? 31   THR H CG2   1 
ATOM   29245 N  N     . LYS H 8  32   ? 130.039 191.534 119.474 1.00 34.18  ? 32   LYS H N     1 
ATOM   29246 C  CA    . LYS H 8  32   ? 128.752 191.143 120.043 1.00 31.43  ? 32   LYS H CA    1 
ATOM   29247 C  C     . LYS H 8  32   ? 128.736 191.135 121.565 1.00 30.21  ? 32   LYS H C     1 
ATOM   29248 O  O     . LYS H 8  32   ? 127.695 191.435 122.152 1.00 31.18  ? 32   LYS H O     1 
ATOM   29249 C  CB    . LYS H 8  32   ? 128.342 189.762 119.536 1.00 29.48  ? 32   LYS H CB    1 
ATOM   29250 C  CG    . LYS H 8  32   ? 127.919 189.728 118.085 1.00 30.39  ? 32   LYS H CG    1 
ATOM   29251 C  CD    . LYS H 8  32   ? 126.657 190.514 117.855 1.00 27.09  ? 32   LYS H CD    1 
ATOM   29252 C  CE    . LYS H 8  32   ? 126.684 191.185 116.505 1.00 29.85  ? 32   LYS H CE    1 
ATOM   29253 N  NZ    . LYS H 8  32   ? 125.340 191.186 115.864 1.00 31.78  ? 32   LYS H NZ    1 
ATOM   29254 N  N     . MET H 8  33   ? 129.841 190.785 122.220 1.00 40.72  ? 33   MET H N     1 
ATOM   29255 C  CA    . MET H 8  33   ? 129.910 190.830 123.678 1.00 42.49  ? 33   MET H CA    1 
ATOM   29256 C  C     . MET H 8  33   ? 130.197 192.229 124.211 1.00 45.84  ? 33   MET H C     1 
ATOM   29257 O  O     . MET H 8  33   ? 129.581 192.658 125.188 1.00 49.00  ? 33   MET H O     1 
ATOM   29258 C  CB    . MET H 8  33   ? 130.971 189.851 124.192 1.00 42.11  ? 33   MET H CB    1 
ATOM   29259 C  CG    . MET H 8  33   ? 130.882 188.451 123.611 1.00 44.76  ? 33   MET H CG    1 
ATOM   29260 S  SD    . MET H 8  33   ? 129.711 187.361 124.433 1.00 53.97  ? 33   MET H SD    1 
ATOM   29261 C  CE    . MET H 8  33   ? 128.174 187.806 123.637 1.00 45.15  ? 33   MET H CE    1 
ATOM   29262 N  N     . GLY H 8  34   ? 131.129 192.948 123.594 1.00 40.45  ? 34   GLY H N     1 
ATOM   29263 C  CA    . GLY H 8  34   ? 131.392 194.320 123.981 1.00 39.13  ? 34   GLY H CA    1 
ATOM   29264 C  C     . GLY H 8  34   ? 132.528 194.493 124.968 1.00 39.97  ? 34   GLY H C     1 
ATOM   29265 O  O     . GLY H 8  34   ? 132.367 195.167 125.989 1.00 38.77  ? 34   GLY H O     1 
ATOM   29266 N  N     . GLY H 8  35   ? 133.677 193.879 124.688 1.00 39.48  ? 35   GLY H N     1 
ATOM   29267 C  CA    . GLY H 8  35   ? 134.855 194.092 125.509 1.00 41.00  ? 35   GLY H CA    1 
ATOM   29268 C  C     . GLY H 8  35   ? 134.780 193.514 126.910 1.00 42.04  ? 35   GLY H C     1 
ATOM   29269 O  O     . GLY H 8  35   ? 134.640 194.260 127.884 1.00 39.98  ? 35   GLY H O     1 
ATOM   29270 N  N     . THR H 8  36   ? 134.848 192.191 127.024 1.00 43.93  ? 36   THR H N     1 
ATOM   29271 C  CA    . THR H 8  36   ? 134.807 191.493 128.301 1.00 42.25  ? 36   THR H CA    1 
ATOM   29272 C  C     . THR H 8  36   ? 136.001 190.549 128.410 1.00 44.86  ? 36   THR H C     1 
ATOM   29273 O  O     . THR H 8  36   ? 136.591 190.144 127.404 1.00 43.73  ? 36   THR H O     1 
ATOM   29274 C  CB    . THR H 8  36   ? 133.492 190.716 128.458 1.00 42.40  ? 36   THR H CB    1 
ATOM   29275 O  OG1   . THR H 8  36   ? 132.418 191.486 127.905 1.00 42.33  ? 36   THR H OG1   1 
ATOM   29276 C  CG2   . THR H 8  36   ? 133.192 190.427 129.922 1.00 41.53  ? 36   THR H CG2   1 
ATOM   29277 N  N     . LEU H 8  37   ? 136.359 190.212 129.646 1.00 46.08  ? 37   LEU H N     1 
ATOM   29278 C  CA    . LEU H 8  37   ? 137.504 189.344 129.876 1.00 45.15  ? 37   LEU H CA    1 
ATOM   29279 C  C     . LEU H 8  37   ? 137.277 187.992 129.204 1.00 46.47  ? 37   LEU H C     1 
ATOM   29280 O  O     . LEU H 8  37   ? 136.158 187.465 129.231 1.00 41.15  ? 37   LEU H O     1 
ATOM   29281 C  CB    . LEU H 8  37   ? 137.741 189.141 131.374 1.00 43.89  ? 37   LEU H CB    1 
ATOM   29282 C  CG    . LEU H 8  37   ? 138.959 188.297 131.780 1.00 47.62  ? 37   LEU H CG    1 
ATOM   29283 C  CD1   . LEU H 8  37   ? 140.252 189.093 131.673 1.00 44.13  ? 37   LEU H CD1   1 
ATOM   29284 C  CD2   . LEU H 8  37   ? 138.807 187.670 133.164 1.00 44.39  ? 37   LEU H CD2   1 
ATOM   29285 N  N     . PRO H 8  38   ? 138.312 187.403 128.599 1.00 52.80  ? 38   PRO H N     1 
ATOM   29286 C  CA    . PRO H 8  38   ? 138.137 186.088 127.964 1.00 51.93  ? 38   PRO H CA    1 
ATOM   29287 C  C     . PRO H 8  38   ? 137.609 185.022 128.907 1.00 50.82  ? 38   PRO H C     1 
ATOM   29288 O  O     . PRO H 8  38   ? 136.841 184.155 128.470 1.00 51.65  ? 38   PRO H O     1 
ATOM   29289 C  CB    . PRO H 8  38   ? 139.552 185.750 127.468 1.00 50.69  ? 38   PRO H CB    1 
ATOM   29290 C  CG    . PRO H 8  38   ? 140.465 186.735 128.157 1.00 51.21  ? 38   PRO H CG    1 
ATOM   29291 C  CD    . PRO H 8  38   ? 139.647 187.959 128.339 1.00 49.67  ? 38   PRO H CD    1 
ATOM   29292 N  N     . GLN H 8  39   ? 137.999 185.044 130.183 1.00 51.18  ? 39   GLN H N     1 
ATOM   29293 C  CA    . GLN H 8  39   ? 137.450 184.075 131.123 1.00 53.47  ? 39   GLN H CA    1 
ATOM   29294 C  C     . GLN H 8  39   ? 136.067 184.479 131.615 1.00 52.54  ? 39   GLN H C     1 
ATOM   29295 O  O     . GLN H 8  39   ? 135.266 183.613 131.982 1.00 53.28  ? 39   GLN H O     1 
ATOM   29296 C  CB    . GLN H 8  39   ? 138.389 183.886 132.314 1.00 53.45  ? 39   GLN H CB    1 
ATOM   29297 C  CG    . GLN H 8  39   ? 138.124 182.601 133.084 1.00 52.47  ? 39   GLN H CG    1 
ATOM   29298 C  CD    . GLN H 8  39   ? 138.915 182.511 134.369 1.00 54.49  ? 39   GLN H CD    1 
ATOM   29299 O  OE1   . GLN H 8  39   ? 139.516 183.488 134.811 1.00 54.32  ? 39   GLN H OE1   1 
ATOM   29300 N  NE2   . GLN H 8  39   ? 138.921 181.330 134.976 1.00 53.37  ? 39   GLN H NE2   1 
ATOM   29301 N  N     . ASN H 8  40   ? 135.773 185.779 131.642 1.00 46.50  ? 40   ASN H N     1 
ATOM   29302 C  CA    . ASN H 8  40   ? 134.449 186.230 132.044 1.00 48.75  ? 40   ASN H CA    1 
ATOM   29303 C  C     . ASN H 8  40   ? 133.413 186.050 130.947 1.00 48.72  ? 40   ASN H C     1 
ATOM   29304 O  O     . ASN H 8  40   ? 132.217 186.168 131.229 1.00 50.18  ? 40   ASN H O     1 
ATOM   29305 C  CB    . ASN H 8  40   ? 134.508 187.689 132.483 1.00 50.25  ? 40   ASN H CB    1 
ATOM   29306 C  CG    . ASN H 8  40   ? 135.279 187.871 133.773 1.00 51.36  ? 40   ASN H CG    1 
ATOM   29307 O  OD1   . ASN H 8  40   ? 135.390 186.946 134.576 1.00 48.42  ? 40   ASN H OD1   1 
ATOM   29308 N  ND2   . ASN H 8  40   ? 135.800 189.070 133.987 1.00 49.44  ? 40   ASN H ND2   1 
ATOM   29309 N  N     . ILE H 8  41   ? 133.841 185.777 129.717 1.00 42.78  ? 41   ILE H N     1 
ATOM   29310 C  CA    . ILE H 8  41   ? 132.939 185.389 128.637 1.00 41.90  ? 41   ILE H CA    1 
ATOM   29311 C  C     . ILE H 8  41   ? 132.747 183.877 128.724 1.00 42.92  ? 41   ILE H C     1 
ATOM   29312 O  O     . ILE H 8  41   ? 133.734 183.135 128.588 1.00 43.87  ? 41   ILE H O     1 
ATOM   29313 C  CB    . ILE H 8  41   ? 133.497 185.788 127.266 1.00 43.48  ? 41   ILE H CB    1 
ATOM   29314 C  CG1   . ILE H 8  41   ? 133.396 187.297 127.052 1.00 42.03  ? 41   ILE H CG1   1 
ATOM   29315 C  CG2   . ILE H 8  41   ? 132.763 185.045 126.153 1.00 40.23  ? 41   ILE H CG2   1 
ATOM   29316 C  CD1   . ILE H 8  41   ? 133.829 187.729 125.664 1.00 40.39  ? 41   ILE H CD1   1 
ATOM   29317 N  N     . PRO H 8  42   ? 131.536 183.384 128.970 1.00 40.26  ? 42   PRO H N     1 
ATOM   29318 C  CA    . PRO H 8  42   ? 131.327 181.936 129.000 1.00 38.84  ? 42   PRO H CA    1 
ATOM   29319 C  C     . PRO H 8  42   ? 131.535 181.314 127.630 1.00 38.18  ? 42   PRO H C     1 
ATOM   29320 O  O     . PRO H 8  42   ? 131.279 181.933 126.596 1.00 34.44  ? 42   PRO H O     1 
ATOM   29321 C  CB    . PRO H 8  42   ? 129.866 181.822 129.449 1.00 37.78  ? 42   PRO H CB    1 
ATOM   29322 C  CG    . PRO H 8  42   ? 129.725 183.039 130.314 1.00 37.13  ? 42   PRO H CG    1 
ATOM   29323 C  CD    . PRO H 8  42   ? 130.299 184.065 129.377 1.00 36.79  ? 42   PRO H CD    1 
ATOM   29324 N  N     . LEU H 8  43   ? 132.007 180.067 127.633 1.00 36.70  ? 43   LEU H N     1 
ATOM   29325 C  CA    . LEU H 8  43   ? 132.163 179.337 126.379 1.00 35.35  ? 43   LEU H CA    1 
ATOM   29326 C  C     . LEU H 8  43   ? 130.820 179.152 125.689 1.00 37.00  ? 43   LEU H C     1 
ATOM   29327 O  O     . LEU H 8  43   ? 130.728 179.223 124.460 1.00 35.49  ? 43   LEU H O     1 
ATOM   29328 C  CB    . LEU H 8  43   ? 132.827 177.985 126.634 1.00 31.21  ? 43   LEU H CB    1 
ATOM   29329 C  CG    . LEU H 8  43   ? 132.897 176.993 125.468 1.00 33.62  ? 43   LEU H CG    1 
ATOM   29330 C  CD1   . LEU H 8  43   ? 133.958 177.388 124.448 1.00 31.43  ? 43   LEU H CD1   1 
ATOM   29331 C  CD2   . LEU H 8  43   ? 133.134 175.574 125.967 1.00 33.01  ? 43   LEU H CD2   1 
ATOM   29332 N  N     . ASP H 8  44   ? 129.767 178.916 126.470 1.00 34.01  ? 44   ASP H N     1 
ATOM   29333 C  CA    . ASP H 8  44   ? 128.440 178.686 125.913 1.00 34.61  ? 44   ASP H CA    1 
ATOM   29334 C  C     . ASP H 8  44   ? 127.857 179.924 125.245 1.00 36.16  ? 44   ASP H C     1 
ATOM   29335 O  O     . ASP H 8  44   ? 127.214 179.802 124.201 1.00 34.83  ? 44   ASP H O     1 
ATOM   29336 C  CB    . ASP H 8  44   ? 127.501 178.196 127.014 1.00 34.35  ? 44   ASP H CB    1 
ATOM   29337 C  CG    . ASP H 8  44   ? 127.613 176.707 127.250 1.00 41.56  ? 44   ASP H CG    1 
ATOM   29338 O  OD1   . ASP H 8  44   ? 128.280 176.027 126.445 1.00 38.86  ? 44   ASP H OD1   1 
ATOM   29339 O  OD2   . ASP H 8  44   ? 127.039 176.215 128.245 1.00 41.64  ? 44   ASP H OD2   1 
ATOM   29340 N  N     . ALA H 8  45   ? 128.057 181.106 125.822 1.00 34.74  ? 45   ALA H N     1 
ATOM   29341 C  CA    . ALA H 8  45   ? 127.446 182.323 125.304 1.00 33.37  ? 45   ALA H CA    1 
ATOM   29342 C  C     . ALA H 8  45   ? 128.021 182.764 123.966 1.00 34.55  ? 45   ALA H C     1 
ATOM   29343 O  O     . ALA H 8  45   ? 127.287 183.311 123.138 1.00 31.59  ? 45   ALA H O     1 
ATOM   29344 C  CB    . ALA H 8  45   ? 127.598 183.456 126.321 1.00 36.00  ? 45   ALA H CB    1 
ATOM   29345 N  N     . SER H 8  46   ? 129.320 182.557 123.742 1.00 31.96  ? 46   SER H N     1 
ATOM   29346 C  CA    . SER H 8  46   ? 129.927 182.943 122.475 1.00 26.56  ? 46   SER H CA    1 
ATOM   29347 C  C     . SER H 8  46   ? 129.579 181.972 121.355 1.00 25.29  ? 46   SER H C     1 
ATOM   29348 O  O     . SER H 8  46   ? 129.608 182.354 120.182 1.00 30.01  ? 46   SER H O     1 
ATOM   29349 C  CB    . SER H 8  46   ? 131.440 183.042 122.629 1.00 27.15  ? 46   SER H CB    1 
ATOM   29350 O  OG    . SER H 8  46   ? 131.923 182.030 123.492 1.00 29.36  ? 46   SER H OG    1 
ATOM   29351 N  N     . LEU H 8  47   ? 129.265 180.717 121.680 1.00 22.20  ? 47   LEU H N     1 
ATOM   29352 C  CA    . LEU H 8  47   ? 128.891 179.759 120.649 1.00 19.59  ? 47   LEU H CA    1 
ATOM   29353 C  C     . LEU H 8  47   ? 127.469 179.945 120.149 1.00 21.30  ? 47   LEU H C     1 
ATOM   29354 O  O     . LEU H 8  47   ? 127.111 179.340 119.136 1.00 22.28  ? 47   LEU H O     1 
ATOM   29355 C  CB    . LEU H 8  47   ? 129.066 178.318 121.143 1.00 17.90  ? 47   LEU H CB    1 
ATOM   29356 C  CG    . LEU H 8  47   ? 130.465 177.838 121.526 1.00 21.98  ? 47   LEU H CG    1 
ATOM   29357 C  CD1   . LEU H 8  47   ? 130.398 176.587 122.361 1.00 16.80  ? 47   LEU H CD1   1 
ATOM   29358 C  CD2   . LEU H 8  47   ? 131.278 177.584 120.287 1.00 19.10  ? 47   LEU H CD2   1 
ATOM   29359 N  N     . GLN H 8  48   ? 126.658 180.760 120.816 1.00 19.09  ? 48   GLN H N     1 
ATOM   29360 C  CA    . GLN H 8  48   ? 125.295 181.018 120.381 1.00 13.43  ? 48   GLN H CA    1 
ATOM   29361 C  C     . GLN H 8  48   ? 125.185 182.191 119.422 1.00 20.03  ? 48   GLN H C     1 
ATOM   29362 O  O     . GLN H 8  48   ? 124.080 182.495 118.971 1.00 23.67  ? 48   GLN H O     1 
ATOM   29363 C  CB    . GLN H 8  48   ? 124.388 181.270 121.585 1.00 20.97  ? 48   GLN H CB    1 
ATOM   29364 C  CG    . GLN H 8  48   ? 124.504 180.254 122.689 1.00 24.41  ? 48   GLN H CG    1 
ATOM   29365 C  CD    . GLN H 8  48   ? 124.250 178.846 122.230 1.00 22.96  ? 48   GLN H CD    1 
ATOM   29366 O  OE1   . GLN H 8  48   ? 124.831 177.901 122.760 1.00 22.30  ? 48   GLN H OE1   1 
ATOM   29367 N  NE2   . GLN H 8  48   ? 123.359 178.688 121.258 1.00 24.18  ? 48   GLN H NE2   1 
ATOM   29368 N  N     . ILE H 8  49   ? 126.290 182.868 119.120 1.00 19.39  ? 49   ILE H N     1 
ATOM   29369 C  CA    . ILE H 8  49   ? 126.275 183.913 118.107 1.00 20.01  ? 49   ILE H CA    1 
ATOM   29370 C  C     . ILE H 8  49   ? 126.199 183.269 116.733 1.00 21.41  ? 49   ILE H C     1 
ATOM   29371 O  O     . ILE H 8  49   ? 126.957 182.344 116.422 1.00 21.38  ? 49   ILE H O     1 
ATOM   29372 C  CB    . ILE H 8  49   ? 127.519 184.804 118.226 1.00 21.49  ? 49   ILE H CB    1 
ATOM   29373 C  CG1   . ILE H 8  49   ? 127.704 185.296 119.663 1.00 22.36  ? 49   ILE H CG1   1 
ATOM   29374 C  CG2   . ILE H 8  49   ? 127.444 185.953 117.240 1.00 14.07  ? 49   ILE H CG2   1 
ATOM   29375 C  CD1   . ILE H 8  49   ? 126.608 186.194 120.155 1.00 21.53  ? 49   ILE H CD1   1 
ATOM   29376 N  N     . GLU H 8  50   ? 125.289 183.758 115.901 1.00 17.59  ? 50   GLU H N     1 
ATOM   29377 C  CA    . GLU H 8  50   ? 125.112 183.217 114.564 1.00 10.84  ? 50   GLU H CA    1 
ATOM   29378 C  C     . GLU H 8  50   ? 126.242 183.688 113.666 1.00 15.00  ? 50   GLU H C     1 
ATOM   29379 O  O     . GLU H 8  50   ? 126.507 184.889 113.579 1.00 22.93  ? 50   GLU H O     1 
ATOM   29380 C  CB    . GLU H 8  50   ? 123.769 183.650 113.994 1.00 12.43  ? 50   GLU H CB    1 
ATOM   29381 C  CG    . GLU H 8  50   ? 122.590 183.220 114.823 1.00 17.78  ? 50   GLU H CG    1 
ATOM   29382 C  CD    . GLU H 8  50   ? 121.322 183.144 114.013 1.00 24.13  ? 50   GLU H CD    1 
ATOM   29383 O  OE1   . GLU H 8  50   ? 120.312 182.629 114.536 1.00 21.94  ? 50   GLU H OE1   1 
ATOM   29384 O  OE2   . GLU H 8  50   ? 121.340 183.590 112.848 1.00 22.67  ? 50   GLU H OE2   1 
ATOM   29385 N  N     . LEU H 8  51   ? 126.902 182.749 112.995 1.00 17.43  ? 51   LEU H N     1 
ATOM   29386 C  CA    . LEU H 8  51   ? 127.925 183.059 112.008 1.00 12.81  ? 51   LEU H CA    1 
ATOM   29387 C  C     . LEU H 8  51   ? 127.477 182.751 110.591 1.00 15.37  ? 51   LEU H C     1 
ATOM   29388 O  O     . LEU H 8  51   ? 128.318 182.534 109.724 1.00 21.35  ? 51   LEU H O     1 
ATOM   29389 C  CB    . LEU H 8  51   ? 129.209 182.296 112.310 1.00 12.98  ? 51   LEU H CB    1 
ATOM   29390 C  CG    . LEU H 8  51   ? 129.768 182.372 113.721 1.00 14.66  ? 51   LEU H CG    1 
ATOM   29391 C  CD1   . LEU H 8  51   ? 130.893 181.386 113.858 1.00 15.44  ? 51   LEU H CD1   1 
ATOM   29392 C  CD2   . LEU H 8  51   ? 130.224 183.767 114.046 1.00 18.96  ? 51   LEU H CD2   1 
ATOM   29393 N  N     . LYS H 8  52   ? 126.173 182.713 110.346 1.00 14.25  ? 52   LYS H N     1 
ATOM   29394 C  CA    . LYS H 8  52   ? 125.654 182.415 109.017 1.00 6.61   ? 52   LYS H CA    1 
ATOM   29395 C  C     . LYS H 8  52   ? 126.164 183.399 107.974 1.00 15.56  ? 52   LYS H C     1 
ATOM   29396 O  O     . LYS H 8  52   ? 126.734 183.001 106.952 1.00 15.41  ? 52   LYS H O     1 
ATOM   29397 C  CB    . LYS H 8  52   ? 124.131 182.435 109.077 1.00 11.69  ? 52   LYS H CB    1 
ATOM   29398 C  CG    . LYS H 8  52   ? 123.401 181.675 108.020 1.00 14.27  ? 52   LYS H CG    1 
ATOM   29399 C  CD    . LYS H 8  52   ? 122.115 182.414 107.731 1.00 19.08  ? 52   LYS H CD    1 
ATOM   29400 C  CE    . LYS H 8  52   ? 121.582 182.174 106.344 1.00 23.57  ? 52   LYS H CE    1 
ATOM   29401 N  NZ    . LYS H 8  52   ? 120.617 181.051 106.328 1.00 17.18  ? 52   LYS H NZ    1 
ATOM   29402 N  N     . ASP H 8  53   ? 125.986 184.694 108.226 1.00 21.91  ? 53   ASP H N     1 
ATOM   29403 C  CA    . ASP H 8  53   ? 126.263 185.699 107.206 1.00 14.29  ? 53   ASP H CA    1 
ATOM   29404 C  C     . ASP H 8  53   ? 127.754 185.961 107.043 1.00 14.39  ? 53   ASP H C     1 
ATOM   29405 O  O     . ASP H 8  53   ? 128.195 186.349 105.959 1.00 18.28  ? 53   ASP H O     1 
ATOM   29406 C  CB    . ASP H 8  53   ? 125.521 186.984 107.547 1.00 18.56  ? 53   ASP H CB    1 
ATOM   29407 C  CG    . ASP H 8  53   ? 124.064 186.930 107.153 1.00 27.48  ? 53   ASP H CG    1 
ATOM   29408 O  OD1   . ASP H 8  53   ? 123.269 186.331 107.902 1.00 28.88  ? 53   ASP H OD1   1 
ATOM   29409 O  OD2   . ASP H 8  53   ? 123.705 187.480 106.091 1.00 28.83  ? 53   ASP H OD2   1 
ATOM   29410 N  N     . LEU H 8  54   ? 128.543 185.752 108.094 1.00 6.73   ? 54   LEU H N     1 
ATOM   29411 C  CA    . LEU H 8  54   ? 129.994 185.836 107.974 1.00 9.88   ? 54   LEU H CA    1 
ATOM   29412 C  C     . LEU H 8  54   ? 130.530 184.771 107.022 1.00 14.97  ? 54   LEU H C     1 
ATOM   29413 O  O     . LEU H 8  54   ? 131.351 185.052 106.135 1.00 18.50  ? 54   LEU H O     1 
ATOM   29414 C  CB    . LEU H 8  54   ? 130.610 185.684 109.359 1.00 15.89  ? 54   LEU H CB    1 
ATOM   29415 C  CG    . LEU H 8  54   ? 131.963 186.276 109.721 1.00 13.86  ? 54   LEU H CG    1 
ATOM   29416 C  CD1   . LEU H 8  54   ? 131.888 187.770 109.752 1.00 13.35  ? 54   LEU H CD1   1 
ATOM   29417 C  CD2   . LEU H 8  54   ? 132.356 185.735 111.070 1.00 12.21  ? 54   LEU H CD2   1 
ATOM   29418 N  N     . ILE H 8  55   ? 130.061 183.535 107.186 1.00 15.03  ? 55   ILE H N     1 
ATOM   29419 C  CA    . ILE H 8  55   ? 130.463 182.459 106.293 1.00 11.58  ? 55   ILE H CA    1 
ATOM   29420 C  C     . ILE H 8  55   ? 129.946 182.718 104.889 1.00 6.55   ? 55   ILE H C     1 
ATOM   29421 O  O     . ILE H 8  55   ? 130.624 182.423 103.901 1.00 9.26   ? 55   ILE H O     1 
ATOM   29422 C  CB    . ILE H 8  55   ? 129.982 181.105 106.837 1.00 8.01   ? 55   ILE H CB    1 
ATOM   29423 C  CG1   . ILE H 8  55   ? 130.564 180.853 108.215 1.00 7.33   ? 55   ILE H CG1   1 
ATOM   29424 C  CG2   . ILE H 8  55   ? 130.393 179.992 105.924 1.00 11.19  ? 55   ILE H CG2   1 
ATOM   29425 C  CD1   . ILE H 8  55   ? 129.941 179.703 108.906 1.00 2.62   ? 55   ILE H CD1   1 
ATOM   29426 N  N     . THR H 8  56   ? 128.738 183.268 104.774 1.00 6.24   ? 56   THR H N     1 
ATOM   29427 C  CA    . THR H 8  56   ? 128.229 183.609 103.452 1.00 7.38   ? 56   THR H CA    1 
ATOM   29428 C  C     . THR H 8  56   ? 129.117 184.639 102.773 1.00 8.95   ? 56   THR H C     1 
ATOM   29429 O  O     . THR H 8  56   ? 129.364 184.557 101.568 1.00 14.07  ? 56   THR H O     1 
ATOM   29430 C  CB    . THR H 8  56   ? 126.800 184.131 103.546 1.00 12.50  ? 56   THR H CB    1 
ATOM   29431 O  OG1   . THR H 8  56   ? 125.989 183.199 104.261 1.00 17.13  ? 56   THR H OG1   1 
ATOM   29432 C  CG2   . THR H 8  56   ? 126.218 184.313 102.164 1.00 5.72   ? 56   THR H CG2   1 
ATOM   29433 N  N     . ALA H 8  57   ? 129.594 185.627 103.530 1.00 13.92  ? 57   ALA H N     1 
ATOM   29434 C  CA    . ALA H 8  57   ? 130.473 186.649 102.981 1.00 8.92   ? 57   ALA H CA    1 
ATOM   29435 C  C     . ALA H 8  57   ? 131.829 186.097 102.582 1.00 8.67   ? 57   ALA H C     1 
ATOM   29436 O  O     . ALA H 8  57   ? 132.464 186.652 101.685 1.00 13.97  ? 57   ALA H O     1 
ATOM   29437 C  CB    . ALA H 8  57   ? 130.659 187.780 103.985 1.00 11.81  ? 57   ALA H CB    1 
ATOM   29438 N  N     . LEU H 8  58   ? 132.299 185.033 103.229 1.00 15.99  ? 58   LEU H N     1 
ATOM   29439 C  CA    . LEU H 8  58   ? 133.528 184.409 102.751 1.00 17.51  ? 58   LEU H CA    1 
ATOM   29440 C  C     . LEU H 8  58   ? 133.385 183.782 101.369 1.00 14.75  ? 58   LEU H C     1 
ATOM   29441 O  O     . LEU H 8  58   ? 134.400 183.477 100.741 1.00 17.19  ? 58   LEU H O     1 
ATOM   29442 C  CB    . LEU H 8  58   ? 134.002 183.342 103.730 1.00 13.84  ? 58   LEU H CB    1 
ATOM   29443 C  CG    . LEU H 8  58   ? 134.828 183.815 104.914 1.00 11.91  ? 58   LEU H CG    1 
ATOM   29444 C  CD1   . LEU H 8  58   ? 134.862 182.714 105.922 1.00 16.34  ? 58   LEU H CD1   1 
ATOM   29445 C  CD2   . LEU H 8  58   ? 136.220 184.203 104.494 1.00 12.98  ? 58   LEU H CD2   1 
ATOM   29446 N  N     . GLY H 8  59   ? 132.167 183.579 100.883 1.00 15.02  ? 59   GLY H N     1 
ATOM   29447 C  CA    . GLY H 8  59   ? 131.955 182.901 99.625  1.00 18.11  ? 59   GLY H CA    1 
ATOM   29448 C  C     . GLY H 8  59   ? 131.736 181.410 99.725  1.00 19.49  ? 59   GLY H C     1 
ATOM   29449 O  O     . GLY H 8  59   ? 131.700 180.735 98.695  1.00 24.56  ? 59   GLY H O     1 
ATOM   29450 N  N     . ILE H 8  60   ? 131.599 180.872 100.929 1.00 8.22   ? 60   ILE H N     1 
ATOM   29451 C  CA    . ILE H 8  60   ? 131.387 179.445 101.142 1.00 3.95   ? 60   ILE H CA    1 
ATOM   29452 C  C     . ILE H 8  60   ? 129.903 179.149 100.960 1.00 11.17  ? 60   ILE H C     1 
ATOM   29453 O  O     . ILE H 8  60   ? 129.063 179.921 101.435 1.00 14.39  ? 60   ILE H O     1 
ATOM   29454 C  CB    . ILE H 8  60   ? 131.904 179.027 102.526 1.00 12.50  ? 60   ILE H CB    1 
ATOM   29455 C  CG1   . ILE H 8  60   ? 133.424 179.135 102.552 1.00 10.65  ? 60   ILE H CG1   1 
ATOM   29456 C  CG2   . ILE H 8  60   ? 131.480 177.620 102.880 1.00 6.61   ? 60   ILE H CG2   1 
ATOM   29457 C  CD1   . ILE H 8  60   ? 134.015 178.959 103.896 1.00 10.34  ? 60   ILE H CD1   1 
ATOM   29458 N  N     . PRO H 8  61   ? 129.530 178.070 100.269 1.00 11.22  ? 61   PRO H N     1 
ATOM   29459 C  CA    . PRO H 8  61   ? 128.109 177.827 99.990  1.00 7.71   ? 61   PRO H CA    1 
ATOM   29460 C  C     . PRO H 8  61   ? 127.308 177.420 101.216 1.00 11.31  ? 61   PRO H C     1 
ATOM   29461 O  O     . PRO H 8  61   ? 127.847 177.309 102.317 1.00 11.87  ? 61   PRO H O     1 
ATOM   29462 C  CB    . PRO H 8  61   ? 128.145 176.690 98.965  1.00 8.08   ? 61   PRO H CB    1 
ATOM   29463 C  CG    . PRO H 8  61   ? 129.540 176.617 98.495  1.00 10.06  ? 61   PRO H CG    1 
ATOM   29464 C  CD    . PRO H 8  61   ? 130.387 177.077 99.606  1.00 9.41   ? 61   PRO H CD    1 
ATOM   29465 N  N     . MET H 8  62   ? 126.019 177.147 101.018 1.00 9.30   ? 62   MET H N     1 
ATOM   29466 C  CA    . MET H 8  62   ? 125.103 176.785 102.094 1.00 8.68   ? 62   MET H CA    1 
ATOM   29467 C  C     . MET H 8  62   ? 125.069 175.291 102.374 1.00 10.55  ? 62   MET H C     1 
ATOM   29468 O  O     . MET H 8  62   ? 124.022 174.761 102.747 1.00 12.95  ? 62   MET H O     1 
ATOM   29469 C  CB    . MET H 8  62   ? 123.699 177.292 101.777 1.00 16.41  ? 62   MET H CB    1 
ATOM   29470 C  CG    . MET H 8  62   ? 123.338 178.521 102.549 1.00 16.41  ? 62   MET H CG    1 
ATOM   29471 S  SD    . MET H 8  62   ? 123.497 178.192 104.301 1.00 29.61  ? 62   MET H SD    1 
ATOM   29472 C  CE    . MET H 8  62   ? 123.579 179.852 104.899 1.00 15.22  ? 62   MET H CE    1 
ATOM   29473 N  N     . ARG H 8  63   ? 126.184 174.602 102.202 1.00 8.51   ? 63   ARG H N     1 
ATOM   29474 C  CA    . ARG H 8  63   ? 126.256 173.172 102.439 1.00 1.11   ? 63   ARG H CA    1 
ATOM   29475 C  C     . ARG H 8  63   ? 126.387 172.867 103.924 1.00 2.01   ? 63   ARG H C     1 
ATOM   29476 O  O     . ARG H 8  63   ? 127.110 173.545 104.647 1.00 13.41  ? 63   ARG H O     1 
ATOM   29477 C  CB    . ARG H 8  63   ? 127.434 172.597 101.668 1.00 5.49   ? 63   ARG H CB    1 
ATOM   29478 C  CG    . ARG H 8  63   ? 127.470 173.067 100.241 1.00 0.76   ? 63   ARG H CG    1 
ATOM   29479 C  CD    . ARG H 8  63   ? 128.742 172.664 99.560  1.00 5.17   ? 63   ARG H CD    1 
ATOM   29480 N  NE    . ARG H 8  63   ? 128.827 171.224 99.378  1.00 3.23   ? 63   ARG H NE    1 
ATOM   29481 C  CZ    . ARG H 8  63   ? 128.255 170.553 98.395  1.00 5.31   ? 63   ARG H CZ    1 
ATOM   29482 N  NH1   . ARG H 8  63   ? 127.526 171.158 97.479  1.00 1.66   ? 63   ARG H NH1   1 
ATOM   29483 N  NH2   . ARG H 8  63   ? 128.415 169.239 98.332  1.00 7.11   ? 63   ARG H NH2   1 
ATOM   29484 N  N     . VAL H 8  64   ? 125.674 171.835 104.375 1.00 1.21   ? 64   VAL H N     1 
ATOM   29485 C  CA    . VAL H 8  64   ? 125.653 171.485 105.792 1.00 2.96   ? 64   VAL H CA    1 
ATOM   29486 C  C     . VAL H 8  64   ? 127.030 171.037 106.257 1.00 0.72   ? 64   VAL H C     1 
ATOM   29487 O  O     . VAL H 8  64   ? 127.504 171.427 107.334 1.00 12.54  ? 64   VAL H O     1 
ATOM   29488 C  CB    . VAL H 8  64   ? 124.590 170.400 106.042 1.00 2.00   ? 64   VAL H CB    1 
ATOM   29489 C  CG1   . VAL H 8  64   ? 124.714 169.818 107.432 1.00 1.08   ? 64   VAL H CG1   1 
ATOM   29490 C  CG2   . VAL H 8  64   ? 123.216 170.961 105.842 1.00 2.44   ? 64   VAL H CG2   1 
ATOM   29491 N  N     . CYS H 8  65   ? 127.693 170.219 105.449 1.00 3.10   ? 65   CYS H N     1 
ATOM   29492 C  CA    . CYS H 8  65   ? 128.973 169.633 105.818 1.00 3.74   ? 65   CYS H CA    1 
ATOM   29493 C  C     . CYS H 8  65   ? 130.069 170.686 105.924 1.00 0.02   ? 65   CYS H C     1 
ATOM   29494 O  O     . CYS H 8  65   ? 130.876 170.668 106.859 1.00 13.60  ? 65   CYS H O     1 
ATOM   29495 C  CB    . CYS H 8  65   ? 129.331 168.564 104.791 1.00 15.83  ? 65   CYS H CB    1 
ATOM   29496 S  SG    . CYS H 8  65   ? 129.245 169.110 103.064 1.00 4.69   ? 65   CYS H SG    1 
ATOM   29497 N  N     . CYS H 8  66   ? 130.125 171.600 104.961 1.00 12.05  ? 66   CYS H N     1 
ATOM   29498 C  CA    . CYS H 8  66   ? 131.219 172.560 104.918 1.00 10.94  ? 66   CYS H CA    1 
ATOM   29499 C  C     . CYS H 8  66   ? 131.150 173.521 106.086 1.00 7.72   ? 66   CYS H C     1 
ATOM   29500 O  O     . CYS H 8  66   ? 132.169 173.822 106.718 1.00 10.60  ? 66   CYS H O     1 
ATOM   29501 C  CB    . CYS H 8  66   ? 131.190 173.316 103.597 1.00 1.24   ? 66   CYS H CB    1 
ATOM   29502 S  SG    . CYS H 8  66   ? 131.287 172.257 102.170 1.00 9.67   ? 66   CYS H SG    1 
ATOM   29503 N  N     . ARG H 8  67   ? 129.952 174.008 106.391 1.00 5.26   ? 67   ARG H N     1 
ATOM   29504 C  CA    . ARG H 8  67   ? 129.782 174.901 107.522 1.00 0.19   ? 67   ARG H CA    1 
ATOM   29505 C  C     . ARG H 8  67   ? 129.970 174.177 108.843 1.00 4.20   ? 67   ARG H C     1 
ATOM   29506 O  O     . ARG H 8  67   ? 130.563 174.738 109.769 1.00 9.50   ? 67   ARG H O     1 
ATOM   29507 C  CB    . ARG H 8  67   ? 128.426 175.577 107.419 1.00 12.68  ? 67   ARG H CB    1 
ATOM   29508 C  CG    . ARG H 8  67   ? 128.434 176.597 106.322 1.00 1.74   ? 67   ARG H CG    1 
ATOM   29509 C  CD    . ARG H 8  67   ? 127.083 177.091 105.962 1.00 6.23   ? 67   ARG H CD    1 
ATOM   29510 N  NE    . ARG H 8  67   ? 127.151 177.981 104.812 1.00 12.31  ? 67   ARG H NE    1 
ATOM   29511 C  CZ    . ARG H 8  67   ? 127.025 179.298 104.874 1.00 10.10  ? 67   ARG H CZ    1 
ATOM   29512 N  NH1   . ARG H 8  67   ? 126.805 179.916 106.019 1.00 8.58   ? 67   ARG H NH1   1 
ATOM   29513 N  NH2   . ARG H 8  67   ? 127.105 180.009 103.756 1.00 3.78   ? 67   ARG H NH2   1 
ATOM   29514 N  N     . THR H 8  68   ? 129.532 172.923 108.936 1.00 5.17   ? 68   THR H N     1 
ATOM   29515 C  CA    . THR H 8  68   ? 129.817 172.132 110.126 1.00 7.51   ? 68   THR H CA    1 
ATOM   29516 C  C     . THR H 8  68   ? 131.316 172.058 110.397 1.00 9.37   ? 68   THR H C     1 
ATOM   29517 O  O     . THR H 8  68   ? 131.777 172.358 111.507 1.00 1.26   ? 68   THR H O     1 
ATOM   29518 C  CB    . THR H 8  68   ? 129.236 170.733 109.953 1.00 1.30   ? 68   THR H CB    1 
ATOM   29519 O  OG1   . THR H 8  68   ? 127.843 170.838 109.662 1.00 0.83   ? 68   THR H OG1   1 
ATOM   29520 C  CG2   . THR H 8  68   ? 129.412 169.929 111.197 1.00 0.03   ? 68   THR H CG2   1 
ATOM   29521 N  N     . HIS H 8  69   ? 132.100 171.681 109.385 1.00 15.58  ? 69   HIS H N     1 
ATOM   29522 C  CA    . HIS H 8  69   ? 133.523 171.464 109.620 1.00 1.23   ? 69   HIS H CA    1 
ATOM   29523 C  C     . HIS H 8  69   ? 134.280 172.773 109.785 1.00 1.02   ? 69   HIS H C     1 
ATOM   29524 O  O     . HIS H 8  69   ? 135.304 172.806 110.469 1.00 5.45   ? 69   HIS H O     1 
ATOM   29525 C  CB    . HIS H 8  69   ? 134.136 170.630 108.498 1.00 11.94  ? 69   HIS H CB    1 
ATOM   29526 C  CG    . HIS H 8  69   ? 133.541 169.266 108.369 1.00 4.04   ? 69   HIS H CG    1 
ATOM   29527 N  ND1   . HIS H 8  69   ? 133.301 168.457 109.455 1.00 4.99   ? 69   HIS H ND1   1 
ATOM   29528 C  CD2   . HIS H 8  69   ? 133.150 168.562 107.284 1.00 1.30   ? 69   HIS H CD2   1 
ATOM   29529 C  CE1   . HIS H 8  69   ? 132.768 167.322 109.046 1.00 1.75   ? 69   HIS H CE1   1 
ATOM   29530 N  NE2   . HIS H 8  69   ? 132.669 167.359 107.733 1.00 4.75   ? 69   HIS H NE2   1 
ATOM   29531 N  N     . LEU H 8  70   ? 133.807 173.852 109.170 1.00 1.37   ? 70   LEU H N     1 
ATOM   29532 C  CA    . LEU H 8  70   ? 134.443 175.147 109.362 1.00 0.80   ? 70   LEU H CA    1 
ATOM   29533 C  C     . LEU H 8  70   ? 134.152 175.723 110.740 1.00 1.55   ? 70   LEU H C     1 
ATOM   29534 O  O     . LEU H 8  70   ? 134.960 176.481 111.280 1.00 14.57  ? 70   LEU H O     1 
ATOM   29535 C  CB    . LEU H 8  70   ? 133.972 176.107 108.280 1.00 3.82   ? 70   LEU H CB    1 
ATOM   29536 C  CG    . LEU H 8  70   ? 134.552 177.506 108.268 1.00 2.08   ? 70   LEU H CG    1 
ATOM   29537 C  CD1   . LEU H 8  70   ? 135.946 177.504 107.704 1.00 1.12   ? 70   LEU H CD1   1 
ATOM   29538 C  CD2   . LEU H 8  70   ? 133.639 178.369 107.462 1.00 3.21   ? 70   LEU H CD2   1 
ATOM   29539 N  N     . ILE H 8  71   ? 133.005 175.381 111.323 1.00 1.93   ? 71   ILE H N     1 
ATOM   29540 C  CA    . ILE H 8  71   ? 132.584 176.005 112.571 1.00 0.32   ? 71   ILE H CA    1 
ATOM   29541 C  C     . ILE H 8  71   ? 133.064 175.226 113.786 1.00 2.23   ? 71   ILE H C     1 
ATOM   29542 O  O     . ILE H 8  71   ? 133.344 175.811 114.834 1.00 9.30   ? 71   ILE H O     1 
ATOM   29543 C  CB    . ILE H 8  71   ? 131.055 176.162 112.553 1.00 1.65   ? 71   ILE H CB    1 
ATOM   29544 C  CG1   . ILE H 8  71   ? 130.664 177.500 111.962 1.00 7.59   ? 71   ILE H CG1   1 
ATOM   29545 C  CG2   . ILE H 8  71   ? 130.424 175.969 113.912 1.00 0.31   ? 71   ILE H CG2   1 
ATOM   29546 C  CD1   . ILE H 8  71   ? 129.231 177.544 111.634 1.00 6.31   ? 71   ILE H CD1   1 
ATOM   29547 N  N     . THR H 8  72   ? 133.153 173.906 113.688 1.00 4.11   ? 72   THR H N     1 
ATOM   29548 C  CA    . THR H 8  72   ? 133.334 173.084 114.874 1.00 0.81   ? 72   THR H CA    1 
ATOM   29549 C  C     . THR H 8  72   ? 134.751 172.580 115.087 1.00 1.80   ? 72   THR H C     1 
ATOM   29550 O  O     . THR H 8  72   ? 135.010 171.956 116.115 1.00 4.79   ? 72   THR H O     1 
ATOM   29551 C  CB    . THR H 8  72   ? 132.383 171.891 114.821 1.00 5.94   ? 72   THR H CB    1 
ATOM   29552 O  OG1   . THR H 8  72   ? 132.468 171.283 113.532 1.00 9.94   ? 72   THR H OG1   1 
ATOM   29553 C  CG2   . THR H 8  72   ? 130.967 172.328 115.076 1.00 2.71   ? 72   THR H CG2   1 
ATOM   29554 N  N     . THR H 8  73   ? 135.671 172.815 114.160 1.00 4.30   ? 73   THR H N     1 
ATOM   29555 C  CA    . THR H 8  73   ? 136.992 172.203 114.239 1.00 1.86   ? 73   THR H CA    1 
ATOM   29556 C  C     . THR H 8  73   ? 137.844 172.877 115.309 1.00 2.55   ? 73   THR H C     1 
ATOM   29557 O  O     . THR H 8  73   ? 137.930 174.103 115.364 1.00 9.02   ? 73   THR H O     1 
ATOM   29558 C  CB    . THR H 8  73   ? 137.689 172.273 112.884 1.00 3.61   ? 73   THR H CB    1 
ATOM   29559 O  OG1   . THR H 8  73   ? 136.800 171.796 111.871 1.00 4.13   ? 73   THR H OG1   1 
ATOM   29560 C  CG2   . THR H 8  73   ? 138.925 171.411 112.880 1.00 4.37   ? 73   THR H CG2   1 
ATOM   29561 N  N     . LEU H 8  74   ? 138.484 172.065 116.148 1.00 5.56   ? 74   LEU H N     1 
ATOM   29562 C  CA    . LEU H 8  74   ? 139.296 172.566 117.248 1.00 2.37   ? 74   LEU H CA    1 
ATOM   29563 C  C     . LEU H 8  74   ? 140.681 172.968 116.763 1.00 4.64   ? 74   LEU H C     1 
ATOM   29564 O  O     . LEU H 8  74   ? 141.255 172.326 115.882 1.00 10.13  ? 74   LEU H O     1 
ATOM   29565 C  CB    . LEU H 8  74   ? 139.423 171.513 118.342 1.00 7.27   ? 74   LEU H CB    1 
ATOM   29566 C  CG    . LEU H 8  74   ? 138.150 171.047 119.029 1.00 2.21   ? 74   LEU H CG    1 
ATOM   29567 C  CD1   . LEU H 8  74   ? 138.478 169.977 120.021 1.00 5.07   ? 74   LEU H CD1   1 
ATOM   29568 C  CD2   . LEU H 8  74   ? 137.433 172.193 119.692 1.00 4.48   ? 74   LEU H CD2   1 
ATOM   29569 N  N     . ASP H 8  75   ? 141.221 174.020 117.357 1.00 12.34  ? 75   ASP H N     1 
ATOM   29570 C  CA    . ASP H 8  75   ? 142.517 174.553 116.975 1.00 5.18   ? 75   ASP H CA    1 
ATOM   29571 C  C     . ASP H 8  75   ? 143.545 174.225 118.046 1.00 15.47  ? 75   ASP H C     1 
ATOM   29572 O  O     . ASP H 8  75   ? 143.365 174.573 119.214 1.00 19.81  ? 75   ASP H O     1 
ATOM   29573 C  CB    . ASP H 8  75   ? 142.418 176.058 116.777 1.00 6.37   ? 75   ASP H CB    1 
ATOM   29574 C  CG    . ASP H 8  75   ? 143.570 176.612 116.005 1.00 17.39  ? 75   ASP H CG    1 
ATOM   29575 O  OD1   . ASP H 8  75   ? 143.684 177.845 115.909 1.00 21.89  ? 75   ASP H OD1   1 
ATOM   29576 O  OD2   . ASP H 8  75   ? 144.368 175.816 115.491 1.00 21.13  ? 75   ASP H OD2   1 
ATOM   29577 N  N     . TYR H 8  76   ? 144.622 173.553 117.643 1.00 17.57  ? 76   TYR H N     1 
ATOM   29578 C  CA    . TYR H 8  76   ? 145.642 173.129 118.590 1.00 14.20  ? 76   TYR H CA    1 
ATOM   29579 C  C     . TYR H 8  76   ? 146.451 174.296 119.128 1.00 17.30  ? 76   TYR H C     1 
ATOM   29580 O  O     . TYR H 8  76   ? 147.021 174.191 120.213 1.00 24.71  ? 76   TYR H O     1 
ATOM   29581 C  CB    . TYR H 8  76   ? 146.565 172.124 117.921 1.00 12.63  ? 76   TYR H CB    1 
ATOM   29582 C  CG    . TYR H 8  76   ? 147.279 171.178 118.844 1.00 13.87  ? 76   TYR H CG    1 
ATOM   29583 C  CD1   . TYR H 8  76   ? 146.620 170.120 119.429 1.00 17.18  ? 76   TYR H CD1   1 
ATOM   29584 C  CD2   . TYR H 8  76   ? 148.630 171.332 119.109 1.00 20.72  ? 76   TYR H CD2   1 
ATOM   29585 C  CE1   . TYR H 8  76   ? 147.281 169.246 120.254 1.00 17.58  ? 76   TYR H CE1   1 
ATOM   29586 C  CE2   . TYR H 8  76   ? 149.295 170.467 119.936 1.00 20.37  ? 76   TYR H CE2   1 
ATOM   29587 C  CZ    . TYR H 8  76   ? 148.618 169.428 120.505 1.00 21.52  ? 76   TYR H CZ    1 
ATOM   29588 O  OH    . TYR H 8  76   ? 149.289 168.566 121.332 1.00 24.78  ? 76   TYR H OH    1 
ATOM   29589 N  N     . ARG H 8  77   ? 146.516 175.402 118.398 1.00 15.03  ? 77   ARG H N     1 
ATOM   29590 C  CA    . ARG H 8  77   ? 147.244 176.566 118.870 1.00 16.60  ? 77   ARG H CA    1 
ATOM   29591 C  C     . ARG H 8  77   ? 146.537 177.278 120.007 1.00 24.17  ? 77   ARG H C     1 
ATOM   29592 O  O     . ARG H 8  77   ? 147.150 178.132 120.652 1.00 31.28  ? 77   ARG H O     1 
ATOM   29593 C  CB    . ARG H 8  77   ? 147.475 177.537 117.717 1.00 15.65  ? 77   ARG H CB    1 
ATOM   29594 C  CG    . ARG H 8  77   ? 148.242 176.930 116.575 1.00 16.83  ? 77   ARG H CG    1 
ATOM   29595 C  CD    . ARG H 8  77   ? 148.218 177.813 115.367 1.00 12.98  ? 77   ARG H CD    1 
ATOM   29596 N  NE    . ARG H 8  77   ? 146.878 177.913 114.815 1.00 20.05  ? 77   ARG H NE    1 
ATOM   29597 C  CZ    . ARG H 8  77   ? 146.576 178.564 113.704 1.00 21.52  ? 77   ARG H CZ    1 
ATOM   29598 N  NH1   . ARG H 8  77   ? 147.502 179.164 112.983 1.00 19.20  ? 77   ARG H NH1   1 
ATOM   29599 N  NH2   . ARG H 8  77   ? 145.311 178.624 113.313 1.00 23.97  ? 77   ARG H NH2   1 
ATOM   29600 N  N     . LYS H 8  78   ? 145.276 176.958 120.264 1.00 22.75  ? 78   LYS H N     1 
ATOM   29601 C  CA    . LYS H 8  78   ? 144.514 177.581 121.332 1.00 19.16  ? 78   LYS H CA    1 
ATOM   29602 C  C     . LYS H 8  78   ? 144.352 176.687 122.549 1.00 19.57  ? 78   LYS H C     1 
ATOM   29603 O  O     . LYS H 8  78   ? 143.621 177.048 123.471 1.00 24.93  ? 78   LYS H O     1 
ATOM   29604 C  CB    . LYS H 8  78   ? 143.145 178.006 120.803 1.00 18.41  ? 78   LYS H CB    1 
ATOM   29605 C  CG    . LYS H 8  78   ? 143.231 179.231 119.943 1.00 20.01  ? 78   LYS H CG    1 
ATOM   29606 C  CD    . LYS H 8  78   ? 141.881 179.733 119.511 1.00 24.95  ? 78   LYS H CD    1 
ATOM   29607 C  CE    . LYS H 8  78   ? 141.476 179.168 118.190 1.00 22.91  ? 78   LYS H CE    1 
ATOM   29608 N  NZ    . LYS H 8  78   ? 140.371 179.960 117.609 1.00 23.83  ? 78   LYS H NZ    1 
ATOM   29609 N  N     . TYR H 8  79   ? 145.009 175.531 122.573 1.00 24.14  ? 79   TYR H N     1 
ATOM   29610 C  CA    . TYR H 8  79   ? 144.896 174.568 123.660 1.00 24.92  ? 79   TYR H CA    1 
ATOM   29611 C  C     . TYR H 8  79   ? 146.259 174.194 124.224 1.00 32.33  ? 79   TYR H C     1 
ATOM   29612 O  O     . TYR H 8  79   ? 146.339 173.514 125.248 1.00 38.11  ? 79   TYR H O     1 
ATOM   29613 C  CB    . TYR H 8  79   ? 144.165 173.310 123.187 1.00 23.80  ? 79   TYR H CB    1 
ATOM   29614 C  CG    . TYR H 8  79   ? 142.673 173.473 123.083 1.00 25.84  ? 79   TYR H CG    1 
ATOM   29615 C  CD1   . TYR H 8  79   ? 142.056 173.636 121.853 1.00 23.55  ? 79   TYR H CD1   1 
ATOM   29616 C  CD2   . TYR H 8  79   ? 141.881 173.468 124.215 1.00 24.90  ? 79   TYR H CD2   1 
ATOM   29617 C  CE1   . TYR H 8  79   ? 140.697 173.793 121.756 1.00 24.76  ? 79   TYR H CE1   1 
ATOM   29618 C  CE2   . TYR H 8  79   ? 140.520 173.622 124.129 1.00 26.90  ? 79   TYR H CE2   1 
ATOM   29619 C  CZ    . TYR H 8  79   ? 139.930 173.783 122.896 1.00 31.28  ? 79   TYR H CZ    1 
ATOM   29620 O  OH    . TYR H 8  79   ? 138.563 173.936 122.810 1.00 29.84  ? 79   TYR H OH    1 
ATOM   29621 N  N     . TYR H 8  80   ? 147.329 174.615 123.567 1.00 34.98  ? 80   TYR H N     1 
ATOM   29622 C  CA    . TYR H 8  80   ? 148.675 174.242 123.962 1.00 35.63  ? 80   TYR H CA    1 
ATOM   29623 C  C     . TYR H 8  80   ? 149.562 175.476 124.065 1.00 38.07  ? 80   TYR H C     1 
ATOM   29624 O  O     . TYR H 8  80   ? 149.970 176.043 123.054 1.00 38.06  ? 80   TYR H O     1 
ATOM   29625 C  CB    . TYR H 8  80   ? 149.257 173.238 122.967 1.00 29.52  ? 80   TYR H CB    1 
ATOM   29626 C  CG    . TYR H 8  80   ? 150.598 172.667 123.366 1.00 35.17  ? 80   TYR H CG    1 
ATOM   29627 C  CD1   . TYR H 8  80   ? 150.696 171.656 124.303 1.00 35.42  ? 80   TYR H CD1   1 
ATOM   29628 C  CD2   . TYR H 8  80   ? 151.769 173.138 122.792 1.00 34.72  ? 80   TYR H CD2   1 
ATOM   29629 C  CE1   . TYR H 8  80   ? 151.918 171.136 124.660 1.00 35.81  ? 80   TYR H CE1   1 
ATOM   29630 C  CE2   . TYR H 8  80   ? 152.988 172.625 123.140 1.00 34.23  ? 80   TYR H CE2   1 
ATOM   29631 C  CZ    . TYR H 8  80   ? 153.060 171.624 124.074 1.00 37.55  ? 80   TYR H CZ    1 
ATOM   29632 O  OH    . TYR H 8  80   ? 154.284 171.109 124.422 1.00 36.82  ? 80   TYR H OH    1 
ATOM   29633 P  P     . DG  I 9  1    ? 133.700 133.286 136.540 1.00 97.80  ? 20   DG  X P     1 
ATOM   29634 O  OP1   . DG  I 9  1    ? 133.375 133.604 135.133 1.00 96.86  ? 20   DG  X OP1   1 
ATOM   29635 O  OP2   . DG  I 9  1    ? 133.764 131.872 136.974 1.00 95.64  ? 20   DG  X OP2   1 
ATOM   29636 O  "O5'" . DG  I 9  1    ? 135.085 133.990 136.918 1.00 97.31  ? 20   DG  X "O5'" 1 
ATOM   29637 C  "C5'" . DG  I 9  1    ? 136.100 134.135 135.932 1.00 96.25  ? 20   DG  X "C5'" 1 
ATOM   29638 C  "C4'" . DG  I 9  1    ? 137.377 133.422 136.348 1.00 96.33  ? 20   DG  X "C4'" 1 
ATOM   29639 O  "O4'" . DG  I 9  1    ? 138.058 134.186 137.382 1.00 97.47  ? 20   DG  X "O4'" 1 
ATOM   29640 C  "C3'" . DG  I 9  1    ? 137.185 132.021 136.920 1.00 96.12  ? 20   DG  X "C3'" 1 
ATOM   29641 O  "O3'" . DG  I 9  1    ? 138.255 131.188 136.499 1.00 98.60  ? 20   DG  X "O3'" 1 
ATOM   29642 C  "C2'" . DG  I 9  1    ? 137.228 132.266 138.425 1.00 96.00  ? 20   DG  X "C2'" 1 
ATOM   29643 C  "C1'" . DG  I 9  1    ? 138.260 133.375 138.521 1.00 96.57  ? 20   DG  X "C1'" 1 
ATOM   29644 N  N9    . DG  I 9  1    ? 138.104 134.204 139.713 1.00 97.16  ? 20   DG  X N9    1 
ATOM   29645 C  C8    . DG  I 9  1    ? 137.231 135.251 139.881 1.00 95.70  ? 20   DG  X C8    1 
ATOM   29646 N  N7    . DG  I 9  1    ? 137.309 135.807 141.055 1.00 96.49  ? 20   DG  X N7    1 
ATOM   29647 C  C5    . DG  I 9  1    ? 138.296 135.084 141.712 1.00 97.15  ? 20   DG  X C5    1 
ATOM   29648 C  C6    . DG  I 9  1    ? 138.816 135.232 143.018 1.00 97.13  ? 20   DG  X C6    1 
ATOM   29649 O  O6    . DG  I 9  1    ? 138.495 136.059 143.881 1.00 96.88  ? 20   DG  X O6    1 
ATOM   29650 N  N1    . DG  I 9  1    ? 139.806 134.292 143.288 1.00 97.26  ? 20   DG  X N1    1 
ATOM   29651 C  C2    . DG  I 9  1    ? 140.241 133.332 142.408 1.00 96.38  ? 20   DG  X C2    1 
ATOM   29652 N  N2    . DG  I 9  1    ? 141.208 132.515 142.850 1.00 95.14  ? 20   DG  X N2    1 
ATOM   29653 N  N3    . DG  I 9  1    ? 139.763 133.183 141.179 1.00 96.40  ? 20   DG  X N3    1 
ATOM   29654 C  C4    . DG  I 9  1    ? 138.795 134.092 140.901 1.00 97.17  ? 20   DG  X C4    1 
ATOM   29655 P  P     . DC  I 9  2    ? 138.102 129.591 136.521 1.00 103.01 ? 21   DC  X P     1 
ATOM   29656 O  OP1   . DC  I 9  2    ? 139.428 129.032 136.857 1.00 98.71  ? 21   DC  X OP1   1 
ATOM   29657 O  OP2   . DC  I 9  2    ? 137.421 129.185 135.270 1.00 97.22  ? 21   DC  X OP2   1 
ATOM   29658 O  "O5'" . DC  I 9  2    ? 137.096 129.320 137.730 1.00 97.59  ? 21   DC  X "O5'" 1 
ATOM   29659 C  "C5'" . DC  I 9  2    ? 136.843 128.003 138.160 1.00 96.08  ? 21   DC  X "C5'" 1 
ATOM   29660 C  "C4'" . DC  I 9  2    ? 137.819 127.604 139.247 1.00 96.89  ? 21   DC  X "C4'" 1 
ATOM   29661 O  "O4'" . DC  I 9  2    ? 138.198 128.776 140.018 1.00 96.69  ? 21   DC  X "O4'" 1 
ATOM   29662 C  "C3'" . DC  I 9  2    ? 137.269 126.588 140.248 1.00 98.47  ? 21   DC  X "C3'" 1 
ATOM   29663 O  "O3'" . DC  I 9  2    ? 138.213 125.559 140.475 1.00 99.19  ? 21   DC  X "O3'" 1 
ATOM   29664 C  "C2'" . DC  I 9  2    ? 137.038 127.419 141.501 1.00 97.52  ? 21   DC  X "C2'" 1 
ATOM   29665 C  "C1'" . DC  I 9  2    ? 138.130 128.465 141.386 1.00 96.54  ? 21   DC  X "C1'" 1 
ATOM   29666 N  N1    . DC  I 9  2    ? 137.823 129.702 142.144 1.00 97.25  ? 21   DC  X N1    1 
ATOM   29667 C  C2    . DC  I 9  2    ? 138.469 129.945 143.359 1.00 98.28  ? 21   DC  X C2    1 
ATOM   29668 O  O2    . DC  I 9  2    ? 139.303 129.131 143.774 1.00 97.63  ? 21   DC  X O2    1 
ATOM   29669 N  N3    . DC  I 9  2    ? 138.168 131.071 144.044 1.00 98.99  ? 21   DC  X N3    1 
ATOM   29670 C  C4    . DC  I 9  2    ? 137.265 131.923 143.563 1.00 97.07  ? 21   DC  X C4    1 
ATOM   29671 N  N4    . DC  I 9  2    ? 137.000 133.020 144.277 1.00 96.83  ? 21   DC  X N4    1 
ATOM   29672 C  C5    . DC  I 9  2    ? 136.593 131.690 142.330 1.00 96.19  ? 21   DC  X C5    1 
ATOM   29673 C  C6    . DC  I 9  2    ? 136.897 130.577 141.663 1.00 96.73  ? 21   DC  X C6    1 
ATOM   29674 P  P     . DC  I 9  3    ? 137.735 124.181 141.142 1.00 103.34 ? 22   DC  X P     1 
ATOM   29675 O  OP1   . DC  I 9  3    ? 138.392 123.056 140.432 1.00 97.76  ? 22   DC  X OP1   1 
ATOM   29676 O  OP2   . DC  I 9  3    ? 136.259 124.252 141.215 1.00 96.26  ? 22   DC  X OP2   1 
ATOM   29677 O  "O5'" . DC  I 9  3    ? 138.284 124.268 142.643 1.00 98.38  ? 22   DC  X "O5'" 1 
ATOM   29678 C  "C5'" . DC  I 9  3    ? 139.657 124.550 142.894 1.00 96.28  ? 22   DC  X "C5'" 1 
ATOM   29679 C  "C4'" . DC  I 9  3    ? 139.897 124.697 144.386 1.00 95.82  ? 22   DC  X "C4'" 1 
ATOM   29680 O  "O4'" . DC  I 9  3    ? 139.511 126.030 144.802 1.00 96.46  ? 22   DC  X "O4'" 1 
ATOM   29681 C  "C3'" . DC  I 9  3    ? 139.092 123.727 145.251 1.00 96.83  ? 22   DC  X "C3'" 1 
ATOM   29682 O  "O3'" . DC  I 9  3    ? 139.899 123.166 146.279 1.00 99.36  ? 22   DC  X "O3'" 1 
ATOM   29683 C  "C2'" . DC  I 9  3    ? 137.977 124.593 145.820 1.00 96.62  ? 22   DC  X "C2'" 1 
ATOM   29684 C  "C1'" . DC  I 9  3    ? 138.641 125.954 145.906 1.00 97.57  ? 22   DC  X "C1'" 1 
ATOM   29685 N  N1    . DC  I 9  3    ? 137.673 127.071 145.810 1.00 97.73  ? 22   DC  X N1    1 
ATOM   29686 C  C2    . DC  I 9  3    ? 137.684 128.090 146.769 1.00 97.12  ? 22   DC  X C2    1 
ATOM   29687 O  O2    . DC  I 9  3    ? 138.516 128.050 147.684 1.00 96.73  ? 22   DC  X O2    1 
ATOM   29688 N  N3    . DC  I 9  3    ? 136.784 129.099 146.662 1.00 96.24  ? 22   DC  X N3    1 
ATOM   29689 C  C4    . DC  I 9  3    ? 135.906 129.105 145.658 1.00 96.63  ? 22   DC  X C4    1 
ATOM   29690 N  N4    . DC  I 9  3    ? 135.036 130.116 145.595 1.00 96.11  ? 22   DC  X N4    1 
ATOM   29691 C  C5    . DC  I 9  3    ? 135.879 128.072 144.679 1.00 96.71  ? 22   DC  X C5    1 
ATOM   29692 C  C6    . DC  I 9  3    ? 136.768 127.085 144.796 1.00 96.62  ? 22   DC  X C6    1 
ATOM   29693 P  P     . DG  I 9  4    ? 139.532 121.715 146.868 1.00 105.72 ? 23   DG  X P     1 
ATOM   29694 O  OP1   . DG  I 9  4    ? 140.799 120.976 147.072 1.00 101.37 ? 23   DG  X OP1   1 
ATOM   29695 O  OP2   . DG  I 9  4    ? 138.464 121.146 146.012 1.00 100.40 ? 23   DG  X OP2   1 
ATOM   29696 O  "O5'" . DG  I 9  4    ? 138.875 122.026 148.292 1.00 102.79 ? 23   DG  X "O5'" 1 
ATOM   29697 C  "C5'" . DG  I 9  4    ? 139.666 122.576 149.336 1.00 101.44 ? 23   DG  X "C5'" 1 
ATOM   29698 C  "C4'" . DG  I 9  4    ? 138.789 123.081 150.466 1.00 101.64 ? 23   DG  X "C4'" 1 
ATOM   29699 O  "O4'" . DG  I 9  4    ? 138.204 124.358 150.096 1.00 102.80 ? 23   DG  X "O4'" 1 
ATOM   29700 C  "C3'" . DG  I 9  4    ? 137.610 122.165 150.829 1.00 102.12 ? 23   DG  X "C3'" 1 
ATOM   29701 O  "O3'" . DG  I 9  4    ? 137.456 122.106 152.238 1.00 101.81 ? 23   DG  X "O3'" 1 
ATOM   29702 C  "C2'" . DG  I 9  4    ? 136.423 122.870 150.179 1.00 101.39 ? 23   DG  X "C2'" 1 
ATOM   29703 C  "C1'" . DG  I 9  4    ? 136.827 124.317 150.380 1.00 102.46 ? 23   DG  X "C1'" 1 
ATOM   29704 N  N9    . DG  I 9  4    ? 136.122 125.253 149.511 1.00 102.68 ? 23   DG  X N9    1 
ATOM   29705 C  C8    . DG  I 9  4    ? 135.726 125.052 148.212 1.00 101.36 ? 23   DG  X C8    1 
ATOM   29706 N  N7    . DG  I 9  4    ? 135.103 126.077 147.697 1.00 101.53 ? 23   DG  X N7    1 
ATOM   29707 C  C5    . DG  I 9  4    ? 135.082 127.010 148.725 1.00 101.56 ? 23   DG  X C5    1 
ATOM   29708 C  C6    . DG  I 9  4    ? 134.543 128.314 148.764 1.00 101.45 ? 23   DG  X C6    1 
ATOM   29709 O  O6    . DG  I 9  4    ? 133.949 128.930 147.866 1.00 101.72 ? 23   DG  X O6    1 
ATOM   29710 N  N1    . DG  I 9  4    ? 134.740 128.913 150.006 1.00 101.25 ? 23   DG  X N1    1 
ATOM   29711 C  C2    . DG  I 9  4    ? 135.381 128.331 151.069 1.00 100.91 ? 23   DG  X C2    1 
ATOM   29712 N  N2    . DG  I 9  4    ? 135.481 129.068 152.185 1.00 100.38 ? 23   DG  X N2    1 
ATOM   29713 N  N3    . DG  I 9  4    ? 135.891 127.113 151.044 1.00 101.38 ? 23   DG  X N3    1 
ATOM   29714 C  C4    . DG  I 9  4    ? 135.704 126.514 149.846 1.00 102.09 ? 23   DG  X C4    1 
ATOM   29715 P  P     . DA  I 9  5    ? 138.001 120.842 153.065 1.00 110.47 ? 24   DA  X P     1 
ATOM   29716 O  OP1   . DA  I 9  5    ? 139.413 120.630 152.671 1.00 108.71 ? 24   DA  X OP1   1 
ATOM   29717 O  OP2   . DA  I 9  5    ? 137.020 119.744 152.926 1.00 108.20 ? 24   DA  X OP2   1 
ATOM   29718 O  "O5'" . DA  I 9  5    ? 137.949 121.336 154.584 1.00 108.67 ? 24   DA  X "O5'" 1 
ATOM   29719 C  "C5'" . DA  I 9  5    ? 138.748 122.429 154.996 1.00 107.87 ? 24   DA  X "C5'" 1 
ATOM   29720 C  "C4'" . DA  I 9  5    ? 137.891 123.564 155.523 1.00 108.25 ? 24   DA  X "C4'" 1 
ATOM   29721 O  "O4'" . DA  I 9  5    ? 137.091 124.126 154.449 1.00 108.59 ? 24   DA  X "O4'" 1 
ATOM   29722 C  "C3'" . DA  I 9  5    ? 136.905 123.183 156.635 1.00 109.05 ? 24   DA  X "C3'" 1 
ATOM   29723 O  "O3'" . DA  I 9  5    ? 137.017 124.109 157.712 1.00 110.86 ? 24   DA  X "O3'" 1 
ATOM   29724 C  "C2'" . DA  I 9  5    ? 135.542 123.289 155.952 1.00 108.10 ? 24   DA  X "C2'" 1 
ATOM   29725 C  "C1'" . DA  I 9  5    ? 135.805 124.393 154.949 1.00 108.39 ? 24   DA  X "C1'" 1 
ATOM   29726 N  N9    . DA  I 9  5    ? 134.860 124.414 153.839 1.00 108.60 ? 24   DA  X N9    1 
ATOM   29727 C  C8    . DA  I 9  5    ? 134.587 123.397 152.969 1.00 108.62 ? 24   DA  X C8    1 
ATOM   29728 N  N7    . DA  I 9  5    ? 133.685 123.703 152.066 1.00 107.95 ? 24   DA  X N7    1 
ATOM   29729 C  C5    . DA  I 9  5    ? 133.344 125.012 152.367 1.00 108.39 ? 24   DA  X C5    1 
ATOM   29730 C  C6    . DA  I 9  5    ? 132.437 125.915 151.781 1.00 108.46 ? 24   DA  X C6    1 
ATOM   29731 N  N6    . DA  I 9  5    ? 131.679 125.614 150.723 1.00 107.47 ? 24   DA  X N6    1 
ATOM   29732 N  N1    . DA  I 9  5    ? 132.334 127.143 152.328 1.00 108.53 ? 24   DA  X N1    1 
ATOM   29733 C  C2    . DA  I 9  5    ? 133.092 127.441 153.390 1.00 108.65 ? 24   DA  X C2    1 
ATOM   29734 N  N3    . DA  I 9  5    ? 133.981 126.679 154.025 1.00 108.47 ? 24   DA  X N3    1 
ATOM   29735 C  C4    . DA  I 9  5    ? 134.057 125.463 153.458 1.00 108.22 ? 24   DA  X C4    1 
ATOM   29736 P  P     . DG  I 9  6    ? 136.443 123.741 159.165 1.00 115.71 ? 25   DG  X P     1 
ATOM   29737 O  OP1   . DG  I 9  6    ? 137.597 123.655 160.090 1.00 110.73 ? 25   DG  X OP1   1 
ATOM   29738 O  OP2   . DG  I 9  6    ? 135.544 122.574 159.016 1.00 111.12 ? 25   DG  X OP2   1 
ATOM   29739 O  "O5'" . DG  I 9  6    ? 135.561 125.020 159.563 1.00 111.28 ? 25   DG  X "O5'" 1 
ATOM   29740 C  "C5'" . DG  I 9  6    ? 134.803 125.707 158.569 1.00 110.19 ? 25   DG  X "C5'" 1 
ATOM   29741 C  "C4'" . DG  I 9  6    ? 133.323 125.695 158.913 1.00 110.87 ? 25   DG  X "C4'" 1 
ATOM   29742 O  "O4'" . DG  I 9  6    ? 132.542 125.512 157.695 1.00 110.26 ? 25   DG  X "O4'" 1 
ATOM   29743 C  "C3'" . DG  I 9  6    ? 132.890 124.558 159.837 1.00 111.69 ? 25   DG  X "C3'" 1 
ATOM   29744 O  "O3'" . DG  I 9  6    ? 131.706 124.923 160.551 1.00 112.72 ? 25   DG  X "O3'" 1 
ATOM   29745 C  "C2'" . DG  I 9  6    ? 132.566 123.475 158.820 1.00 110.99 ? 25   DG  X "C2'" 1 
ATOM   29746 C  "C1'" . DG  I 9  6    ? 131.804 124.312 157.806 1.00 110.91 ? 25   DG  X "C1'" 1 
ATOM   29747 N  N9    . DG  I 9  6    ? 131.684 123.699 156.486 1.00 110.81 ? 25   DG  X N9    1 
ATOM   29748 C  C8    . DG  I 9  6    ? 132.203 122.495 156.078 1.00 109.77 ? 25   DG  X C8    1 
ATOM   29749 N  N7    . DG  I 9  6    ? 131.925 122.203 154.838 1.00 110.16 ? 25   DG  X N7    1 
ATOM   29750 C  C5    . DG  I 9  6    ? 131.164 123.278 154.398 1.00 110.73 ? 25   DG  X C5    1 
ATOM   29751 C  C6    . DG  I 9  6    ? 130.574 123.521 153.135 1.00 110.63 ? 25   DG  X C6    1 
ATOM   29752 O  O6    . DG  I 9  6    ? 130.613 122.811 152.120 1.00 109.96 ? 25   DG  X O6    1 
ATOM   29753 N  N1    . DG  I 9  6    ? 129.886 124.734 153.112 1.00 110.53 ? 25   DG  X N1    1 
ATOM   29754 C  C2    . DG  I 9  6    ? 129.783 125.601 154.174 1.00 109.89 ? 25   DG  X C2    1 
ATOM   29755 N  N2    . DG  I 9  6    ? 129.078 126.721 153.961 1.00 109.35 ? 25   DG  X N2    1 
ATOM   29756 N  N3    . DG  I 9  6    ? 130.331 125.384 155.363 1.00 110.16 ? 25   DG  X N3    1 
ATOM   29757 C  C4    . DG  I 9  6    ? 131.004 124.207 155.402 1.00 110.80 ? 25   DG  X C4    1 
ATOM   29758 P  P     . DC  I 9  7    ? 131.696 126.067 161.685 1.00 110.39 ? 26   DC  X P     1 
ATOM   29759 O  OP1   . DC  I 9  7    ? 132.862 126.966 161.567 1.00 106.62 ? 26   DC  X OP1   1 
ATOM   29760 O  OP2   . DC  I 9  7    ? 131.460 125.374 162.969 1.00 105.54 ? 26   DC  X OP2   1 
ATOM   29761 O  "O5'" . DC  I 9  7    ? 130.375 126.898 161.336 1.00 106.98 ? 26   DC  X "O5'" 1 
ATOM   29762 C  "C5'" . DC  I 9  7    ? 130.020 127.117 159.971 1.00 105.35 ? 26   DC  X "C5'" 1 
ATOM   29763 C  "C4'" . DC  I 9  7    ? 128.565 126.757 159.718 1.00 106.26 ? 26   DC  X "C4'" 1 
ATOM   29764 O  "O4'" . DC  I 9  7    ? 128.455 125.953 158.505 1.00 106.56 ? 26   DC  X "O4'" 1 
ATOM   29765 C  "C3'" . DC  I 9  7    ? 127.893 125.926 160.820 1.00 106.09 ? 26   DC  X "C3'" 1 
ATOM   29766 O  "O3'" . DC  I 9  7    ? 126.513 126.282 160.930 1.00 105.68 ? 26   DC  X "O3'" 1 
ATOM   29767 C  "C2'" . DC  I 9  7    ? 128.015 124.517 160.256 1.00 106.25 ? 26   DC  X "C2'" 1 
ATOM   29768 C  "C1'" . DC  I 9  7    ? 127.677 124.818 158.809 1.00 106.68 ? 26   DC  X "C1'" 1 
ATOM   29769 N  N1    . DC  I 9  7    ? 127.976 123.713 157.838 1.00 106.83 ? 26   DC  X N1    1 
ATOM   29770 C  C2    . DC  I 9  7    ? 127.511 123.811 156.522 1.00 106.26 ? 26   DC  X C2    1 
ATOM   29771 O  O2    . DC  I 9  7    ? 126.880 124.818 156.180 1.00 104.90 ? 26   DC  X O2    1 
ATOM   29772 N  N3    . DC  I 9  7    ? 127.775 122.804 155.654 1.00 107.15 ? 26   DC  X N3    1 
ATOM   29773 C  C4    . DC  I 9  7    ? 128.458 121.733 156.062 1.00 106.15 ? 26   DC  X C4    1 
ATOM   29774 N  N4    . DC  I 9  7    ? 128.691 120.764 155.171 1.00 105.18 ? 26   DC  X N4    1 
ATOM   29775 C  C5    . DC  I 9  7    ? 128.932 121.609 157.403 1.00 105.70 ? 26   DC  X C5    1 
ATOM   29776 C  C6    . DC  I 9  7    ? 128.666 122.609 158.250 1.00 106.06 ? 26   DC  X C6    1 
ATOM   29777 P  P     . DA  I 9  8    ? 126.038 127.746 161.401 1.00 103.44 ? 27   DA  X P     1 
ATOM   29778 O  OP1   . DA  I 9  8    ? 127.191 128.622 161.701 1.00 100.67 ? 27   DA  X OP1   1 
ATOM   29779 O  OP2   . DA  I 9  8    ? 125.024 127.503 162.443 1.00 99.17  ? 27   DA  X OP2   1 
ATOM   29780 O  "O5'" . DA  I 9  8    ? 125.253 128.316 160.127 1.00 103.67 ? 27   DA  X "O5'" 1 
ATOM   29781 C  "C5'" . DA  I 9  8    ? 125.228 127.565 158.905 1.00 102.52 ? 27   DA  X "C5'" 1 
ATOM   29782 C  "C4'" . DA  I 9  8    ? 123.837 127.025 158.622 1.00 102.75 ? 27   DA  X "C4'" 1 
ATOM   29783 O  "O4'" . DA  I 9  8    ? 123.946 125.791 157.860 1.00 102.13 ? 27   DA  X "O4'" 1 
ATOM   29784 C  "C3'" . DA  I 9  8    ? 123.012 126.677 159.862 1.00 103.12 ? 27   DA  X "C3'" 1 
ATOM   29785 O  "O3'" . DA  I 9  8    ? 121.641 126.972 159.631 1.00 102.11 ? 27   DA  X "O3'" 1 
ATOM   29786 C  "C2'" . DA  I 9  8    ? 123.242 125.178 160.008 1.00 102.38 ? 27   DA  X "C2'" 1 
ATOM   29787 C  "C1'" . DA  I 9  8    ? 123.288 124.748 158.549 1.00 102.43 ? 27   DA  X "C1'" 1 
ATOM   29788 N  N9    . DA  I 9  8    ? 124.020 123.504 158.329 1.00 103.42 ? 27   DA  X N9    1 
ATOM   29789 C  C8    . DA  I 9  8    ? 124.686 122.762 159.266 1.00 102.74 ? 27   DA  X C8    1 
ATOM   29790 N  N7    . DA  I 9  8    ? 125.255 121.682 158.779 1.00 103.17 ? 27   DA  X N7    1 
ATOM   29791 C  C5    . DA  I 9  8    ? 124.937 121.717 157.430 1.00 103.68 ? 27   DA  X C5    1 
ATOM   29792 C  C6    . DA  I 9  8    ? 125.241 120.854 156.360 1.00 102.95 ? 27   DA  X C6    1 
ATOM   29793 N  N6    . DA  I 9  8    ? 125.968 119.741 156.496 1.00 102.12 ? 27   DA  X N6    1 
ATOM   29794 N  N1    . DA  I 9  8    ? 124.774 121.182 155.141 1.00 102.07 ? 27   DA  X N1    1 
ATOM   29795 C  C2    . DA  I 9  8    ? 124.050 122.297 155.007 1.00 101.89 ? 27   DA  X C2    1 
ATOM   29796 N  N3    . DA  I 9  8    ? 123.697 123.186 155.934 1.00 101.89 ? 27   DA  X N3    1 
ATOM   29797 C  C4    . DA  I 9  8    ? 124.177 122.834 157.137 1.00 103.39 ? 27   DA  X C4    1 
ATOM   29798 P  P     . DT  J 10 1    ? 123.351 131.712 148.541 1.00 100.60 ? -24  DT  Y P     1 
ATOM   29799 O  OP1   . DT  J 10 1    ? 122.235 132.530 149.066 1.00 95.24  ? -24  DT  Y OP1   1 
ATOM   29800 O  OP2   . DT  J 10 1    ? 123.705 131.790 147.106 1.00 98.48  ? -24  DT  Y OP2   1 
ATOM   29801 O  "O5'" . DT  J 10 1    ? 124.648 132.003 149.440 1.00 97.62  ? -24  DT  Y "O5'" 1 
ATOM   29802 C  "C5'" . DT  J 10 1    ? 124.482 132.514 150.761 1.00 96.44  ? -24  DT  Y "C5'" 1 
ATOM   29803 C  "C4'" . DT  J 10 1    ? 125.729 132.308 151.606 1.00 96.84  ? -24  DT  Y "C4'" 1 
ATOM   29804 O  "O4'" . DT  J 10 1    ? 126.343 131.032 151.293 1.00 97.62  ? -24  DT  Y "O4'" 1 
ATOM   29805 C  "C3'" . DT  J 10 1    ? 126.829 133.365 151.429 1.00 97.08  ? -24  DT  Y "C3'" 1 
ATOM   29806 O  "O3'" . DT  J 10 1    ? 127.159 133.932 152.701 1.00 98.77  ? -24  DT  Y "O3'" 1 
ATOM   29807 C  "C2'" . DT  J 10 1    ? 128.005 132.574 150.847 1.00 96.26  ? -24  DT  Y "C2'" 1 
ATOM   29808 C  "C1'" . DT  J 10 1    ? 127.734 131.187 151.398 1.00 97.07  ? -24  DT  Y "C1'" 1 
ATOM   29809 N  N1    . DT  J 10 1    ? 128.416 130.084 150.651 1.00 98.17  ? -24  DT  Y N1    1 
ATOM   29810 C  C2    . DT  J 10 1    ? 129.303 129.273 151.322 1.00 98.04  ? -24  DT  Y C2    1 
ATOM   29811 O  O2    . DT  J 10 1    ? 129.561 129.403 152.502 1.00 97.82  ? -24  DT  Y O2    1 
ATOM   29812 N  N3    . DT  J 10 1    ? 129.880 128.295 150.556 1.00 97.45  ? -24  DT  Y N3    1 
ATOM   29813 C  C4    . DT  J 10 1    ? 129.658 128.046 149.212 1.00 96.28  ? -24  DT  Y C4    1 
ATOM   29814 O  O4    . DT  J 10 1    ? 130.228 127.142 148.610 1.00 95.88  ? -24  DT  Y O4    1 
ATOM   29815 C  C5    . DT  J 10 1    ? 128.719 128.933 148.567 1.00 96.32  ? -24  DT  Y C5    1 
ATOM   29816 C  C7    . DT  J 10 1    ? 128.405 128.765 147.110 1.00 96.17  ? -24  DT  Y C7    1 
ATOM   29817 C  C6    . DT  J 10 1    ? 128.149 129.898 149.309 1.00 97.03  ? -24  DT  Y C6    1 
ATOM   29818 P  P     . DC  J 10 2    ? 128.039 135.275 152.795 1.00 100.27 ? -23  DC  Y P     1 
ATOM   29819 O  OP1   . DC  J 10 2    ? 127.459 136.121 153.861 1.00 95.78  ? -23  DC  Y OP1   1 
ATOM   29820 O  OP2   . DC  J 10 2    ? 128.178 135.831 151.435 1.00 96.21  ? -23  DC  Y OP2   1 
ATOM   29821 O  "O5'" . DC  J 10 2    ? 129.480 134.756 153.250 1.00 98.21  ? -23  DC  Y "O5'" 1 
ATOM   29822 C  "C5'" . DC  J 10 2    ? 129.675 134.238 154.566 1.00 96.40  ? -23  DC  Y "C5'" 1 
ATOM   29823 C  "C4'" . DC  J 10 2    ? 131.122 133.823 154.776 1.00 96.58  ? -23  DC  Y "C4'" 1 
ATOM   29824 O  "O4'" . DC  J 10 2    ? 131.387 132.603 154.031 1.00 95.67  ? -23  DC  Y "O4'" 1 
ATOM   29825 C  "C3'" . DC  J 10 2    ? 132.162 134.840 154.300 1.00 96.56  ? -23  DC  Y "C3'" 1 
ATOM   29826 O  "O3'" . DC  J 10 2    ? 133.277 134.860 155.185 1.00 98.08  ? -23  DC  Y "O3'" 1 
ATOM   29827 C  "C2'" . DC  J 10 2    ? 132.553 134.299 152.933 1.00 96.28  ? -23  DC  Y "C2'" 1 
ATOM   29828 C  "C1'" . DC  J 10 2    ? 132.494 132.805 153.185 1.00 96.46  ? -23  DC  Y "C1'" 1 
ATOM   29829 N  N1    . DC  J 10 2    ? 132.308 132.018 151.945 1.00 97.13  ? -23  DC  Y N1    1 
ATOM   29830 C  C2    . DC  J 10 2    ? 133.041 130.853 151.757 1.00 97.18  ? -23  DC  Y C2    1 
ATOM   29831 O  O2    . DC  J 10 2    ? 133.822 130.487 152.640 1.00 97.61  ? -23  DC  Y O2    1 
ATOM   29832 N  N3    . DC  J 10 2    ? 132.871 130.149 150.614 1.00 96.84  ? -23  DC  Y N3    1 
ATOM   29833 C  C4    . DC  J 10 2    ? 132.021 130.577 149.687 1.00 96.36  ? -23  DC  Y C4    1 
ATOM   29834 N  N4    . DC  J 10 2    ? 131.893 129.851 148.573 1.00 96.01  ? -23  DC  Y N4    1 
ATOM   29835 C  C5    . DC  J 10 2    ? 131.265 131.771 149.857 1.00 96.03  ? -23  DC  Y C5    1 
ATOM   29836 C  C6    . DC  J 10 2    ? 131.444 132.457 150.989 1.00 96.57  ? -23  DC  Y C6    1 
ATOM   29837 P  P     . DG  J 10 3    ? 134.348 136.057 155.119 1.00 108.02 ? -22  DG  Y P     1 
ATOM   29838 O  OP1   . DG  J 10 3    ? 134.091 136.940 156.281 1.00 104.17 ? -22  DG  Y OP1   1 
ATOM   29839 O  OP2   . DG  J 10 3    ? 134.336 136.632 153.757 1.00 104.60 ? -22  DG  Y OP2   1 
ATOM   29840 O  "O5'" . DG  J 10 3    ? 135.760 135.321 155.287 1.00 105.12 ? -22  DG  Y "O5'" 1 
ATOM   29841 C  "C5'" . DG  J 10 3    ? 135.886 134.195 156.155 1.00 103.87 ? -22  DG  Y "C5'" 1 
ATOM   29842 C  "C4'" . DG  J 10 3    ? 136.944 133.232 155.639 1.00 105.48 ? -22  DG  Y "C4'" 1 
ATOM   29843 O  "O4'" . DG  J 10 3    ? 136.440 132.530 154.470 1.00 106.38 ? -22  DG  Y "O4'" 1 
ATOM   29844 C  "C3'" . DG  J 10 3    ? 138.261 133.886 155.207 1.00 105.28 ? -22  DG  Y "C3'" 1 
ATOM   29845 O  "O3'" . DG  J 10 3    ? 139.362 133.137 155.697 1.00 104.40 ? -22  DG  Y "O3'" 1 
ATOM   29846 C  "C2'" . DG  J 10 3    ? 138.196 133.843 153.684 1.00 104.77 ? -22  DG  Y "C2'" 1 
ATOM   29847 C  "C1'" . DG  J 10 3    ? 137.421 132.559 153.460 1.00 105.89 ? -22  DG  Y "C1'" 1 
ATOM   29848 N  N9    . DG  J 10 3    ? 136.764 132.497 152.159 1.00 104.59 ? -22  DG  Y N9    1 
ATOM   29849 C  C8    . DG  J 10 3    ? 135.745 133.299 151.704 1.00 104.18 ? -22  DG  Y C8    1 
ATOM   29850 N  N7    . DG  J 10 3    ? 135.362 133.010 150.491 1.00 104.67 ? -22  DG  Y N7    1 
ATOM   29851 C  C5    . DG  J 10 3    ? 136.181 131.951 150.120 1.00 104.72 ? -22  DG  Y C5    1 
ATOM   29852 C  C6    . DG  J 10 3    ? 136.233 131.222 148.909 1.00 104.67 ? -22  DG  Y C6    1 
ATOM   29853 O  O6    . DG  J 10 3    ? 135.534 131.365 147.895 1.00 104.39 ? -22  DG  Y O6    1 
ATOM   29854 N  N1    . DG  J 10 3    ? 137.211 130.228 148.949 1.00 104.25 ? -22  DG  Y N1    1 
ATOM   29855 C  C2    . DG  J 10 3    ? 138.035 129.978 150.023 1.00 105.19 ? -22  DG  Y C2    1 
ATOM   29856 N  N2    . DG  J 10 3    ? 138.920 128.981 149.875 1.00 104.23 ? -22  DG  Y N2    1 
ATOM   29857 N  N3    . DG  J 10 3    ? 138.000 130.662 151.159 1.00 104.11 ? -22  DG  Y N3    1 
ATOM   29858 C  C4    . DG  J 10 3    ? 137.051 131.627 151.135 1.00 103.75 ? -22  DG  Y C4    1 
ATOM   29859 P  P     . DG  J 10 4    ? 140.853 133.726 155.577 1.00 106.93 ? -21  DG  Y P     1 
ATOM   29860 O  OP1   . DG  J 10 4    ? 141.608 133.242 156.753 1.00 104.75 ? -21  DG  Y OP1   1 
ATOM   29861 O  OP2   . DG  J 10 4    ? 140.746 135.179 155.310 1.00 104.71 ? -21  DG  Y OP2   1 
ATOM   29862 O  "O5'" . DG  J 10 4    ? 141.443 133.015 154.272 1.00 105.09 ? -21  DG  Y "O5'" 1 
ATOM   29863 C  "C5'" . DG  J 10 4    ? 141.510 131.594 154.218 1.00 104.18 ? -21  DG  Y "C5'" 1 
ATOM   29864 C  "C4'" . DG  J 10 4    ? 141.947 131.114 152.846 1.00 104.22 ? -21  DG  Y "C4'" 1 
ATOM   29865 O  "O4'" . DG  J 10 4    ? 140.904 131.354 151.892 1.00 103.99 ? -21  DG  Y "O4'" 1 
ATOM   29866 C  "C3'" . DG  J 10 4    ? 143.181 131.808 152.278 1.00 104.28 ? -21  DG  Y "C3'" 1 
ATOM   29867 O  "O3'" . DG  J 10 4    ? 144.319 130.974 152.460 1.00 105.33 ? -21  DG  Y "O3'" 1 
ATOM   29868 C  "C2'" . DG  J 10 4    ? 142.856 132.016 150.783 1.00 103.74 ? -21  DG  Y "C2'" 1 
ATOM   29869 C  "C1'" . DG  J 10 4    ? 141.480 131.373 150.618 1.00 103.96 ? -21  DG  Y "C1'" 1 
ATOM   29870 N  N9    . DG  J 10 4    ? 140.587 132.105 149.727 1.00 105.46 ? -21  DG  Y N9    1 
ATOM   29871 C  C8    . DG  J 10 4    ? 139.961 133.299 149.982 1.00 104.39 ? -21  DG  Y C8    1 
ATOM   29872 N  N7    . DG  J 10 4    ? 139.210 133.709 149.000 1.00 104.04 ? -21  DG  Y N7    1 
ATOM   29873 C  C5    . DG  J 10 4    ? 139.341 132.721 148.037 1.00 104.17 ? -21  DG  Y C5    1 
ATOM   29874 C  C6    . DG  J 10 4    ? 138.758 132.620 146.757 1.00 103.52 ? -21  DG  Y C6    1 
ATOM   29875 O  O6    . DG  J 10 4    ? 137.985 133.413 146.202 1.00 103.99 ? -21  DG  Y O6    1 
ATOM   29876 N  N1    . DG  J 10 4    ? 139.158 131.459 146.099 1.00 103.96 ? -21  DG  Y N1    1 
ATOM   29877 C  C2    . DG  J 10 4    ? 140.012 130.516 146.618 1.00 104.19 ? -21  DG  Y C2    1 
ATOM   29878 N  N2    . DG  J 10 4    ? 140.280 129.459 145.837 1.00 104.62 ? -21  DG  Y N2    1 
ATOM   29879 N  N3    . DG  J 10 4    ? 140.565 130.601 147.819 1.00 104.07 ? -21  DG  Y N3    1 
ATOM   29880 C  C4    . DG  J 10 4    ? 140.186 131.728 148.468 1.00 105.24 ? -21  DG  Y C4    1 
ATOM   29881 P  P     . DC  J 10 5    ? 145.750 131.397 151.864 1.00 108.52 ? -20  DC  Y P     1 
ATOM   29882 O  OP1   . DC  J 10 5    ? 146.782 130.746 152.701 1.00 104.55 ? -20  DC  Y OP1   1 
ATOM   29883 O  OP2   . DC  J 10 5    ? 145.774 132.864 151.663 1.00 104.67 ? -20  DC  Y OP2   1 
ATOM   29884 O  "O5'" . DC  J 10 5    ? 145.772 130.725 150.421 1.00 105.61 ? -20  DC  Y "O5'" 1 
ATOM   29885 C  "C5'" . DC  J 10 5    ? 146.876 130.931 149.569 1.00 104.55 ? -20  DC  Y "C5'" 1 
ATOM   29886 C  "C4'" . DC  J 10 5    ? 146.854 129.950 148.413 1.00 104.74 ? -20  DC  Y "C4'" 1 
ATOM   29887 O  "O4'" . DC  J 10 5    ? 145.532 129.948 147.814 1.00 105.64 ? -20  DC  Y "O4'" 1 
ATOM   29888 C  "C3'" . DC  J 10 5    ? 147.807 130.295 147.282 1.00 104.78 ? -20  DC  Y "C3'" 1 
ATOM   29889 O  "O3'" . DC  J 10 5    ? 148.185 129.123 146.573 1.00 104.62 ? -20  DC  Y "O3'" 1 
ATOM   29890 C  "C2'" . DC  J 10 5    ? 146.952 131.215 146.426 1.00 104.54 ? -20  DC  Y "C2'" 1 
ATOM   29891 C  "C1'" . DC  J 10 5    ? 145.587 130.545 146.533 1.00 105.17 ? -20  DC  Y "C1'" 1 
ATOM   29892 N  N1    . DC  J 10 5    ? 144.460 131.506 146.404 1.00 105.38 ? -20  DC  Y N1    1 
ATOM   29893 C  C2    . DC  J 10 5    ? 143.463 131.282 145.447 1.00 105.13 ? -20  DC  Y C2    1 
ATOM   29894 O  O2    . DC  J 10 5    ? 143.528 130.276 144.733 1.00 104.23 ? -20  DC  Y O2    1 
ATOM   29895 N  N3    . DC  J 10 5    ? 142.446 132.175 145.338 1.00 104.75 ? -20  DC  Y N3    1 
ATOM   29896 C  C4    . DC  J 10 5    ? 142.416 133.251 146.129 1.00 104.70 ? -20  DC  Y C4    1 
ATOM   29897 N  N4    . DC  J 10 5    ? 141.398 134.105 145.983 1.00 103.83 ? -20  DC  Y N4    1 
ATOM   29898 C  C5    . DC  J 10 5    ? 143.427 133.496 147.106 1.00 104.53 ? -20  DC  Y C5    1 
ATOM   29899 C  C6    . DC  J 10 5    ? 144.420 132.609 147.206 1.00 104.47 ? -20  DC  Y C6    1 
ATOM   29900 P  P     . DT  J 10 6    ? 149.419 129.173 145.545 1.00 111.25 ? -19  DT  Y P     1 
ATOM   29901 O  OP1   . DT  J 10 6    ? 149.817 127.779 145.244 1.00 107.68 ? -19  DT  Y OP1   1 
ATOM   29902 O  OP2   . DT  J 10 6    ? 150.410 130.117 146.109 1.00 107.85 ? -19  DT  Y OP2   1 
ATOM   29903 O  "O5'" . DT  J 10 6    ? 148.810 129.852 144.227 1.00 108.22 ? -19  DT  Y "O5'" 1 
ATOM   29904 C  "C5'" . DT  J 10 6    ? 147.674 129.279 143.581 1.00 106.97 ? -19  DT  Y "C5'" 1 
ATOM   29905 C  "C4'" . DT  J 10 6    ? 147.238 130.135 142.402 1.00 106.99 ? -19  DT  Y "C4'" 1 
ATOM   29906 O  "O4'" . DT  J 10 6    ? 146.217 131.070 142.827 1.00 107.36 ? -19  DT  Y "O4'" 1 
ATOM   29907 C  "C3'" . DT  J 10 6    ? 148.352 130.975 141.764 1.00 107.42 ? -19  DT  Y "C3'" 1 
ATOM   29908 O  "O3'" . DT  J 10 6    ? 148.443 130.709 140.362 1.00 108.17 ? -19  DT  Y "O3'" 1 
ATOM   29909 C  "C2'" . DT  J 10 6    ? 147.929 132.420 142.036 1.00 107.39 ? -19  DT  Y "C2'" 1 
ATOM   29910 C  "C1'" . DT  J 10 6    ? 146.424 132.292 142.174 1.00 107.69 ? -19  DT  Y "C1'" 1 
ATOM   29911 N  N1    . DT  J 10 6    ? 145.817 133.383 142.991 1.00 108.06 ? -19  DT  Y N1    1 
ATOM   29912 C  C2    . DT  J 10 6    ? 144.636 133.960 142.577 1.00 107.18 ? -19  DT  Y C2    1 
ATOM   29913 O  O2    . DT  J 10 6    ? 144.040 133.617 141.573 1.00 107.17 ? -19  DT  Y O2    1 
ATOM   29914 N  N3    . DT  J 10 6    ? 144.171 134.957 143.391 1.00 106.52 ? -19  DT  Y N3    1 
ATOM   29915 C  C4    . DT  J 10 6    ? 144.758 135.431 144.552 1.00 107.32 ? -19  DT  Y C4    1 
ATOM   29916 O  O4    . DT  J 10 6    ? 144.260 136.334 145.218 1.00 106.34 ? -19  DT  Y O4    1 
ATOM   29917 C  C5    . DT  J 10 6    ? 145.998 134.787 144.925 1.00 107.71 ? -19  DT  Y C5    1 
ATOM   29918 C  C7    . DT  J 10 6    ? 146.727 135.215 146.166 1.00 107.02 ? -19  DT  Y C7    1 
ATOM   29919 C  C6    . DT  J 10 6    ? 146.463 133.809 144.134 1.00 106.97 ? -19  DT  Y C6    1 
ATOM   29920 P  P     . DC  J 10 7    ? 149.681 131.289 139.513 1.00 108.17 ? -18  DC  Y P     1 
ATOM   29921 O  OP1   . DC  J 10 7    ? 150.217 130.174 138.699 1.00 104.26 ? -18  DC  Y OP1   1 
ATOM   29922 O  OP2   . DC  J 10 7    ? 150.586 132.009 140.440 1.00 103.95 ? -18  DC  Y OP2   1 
ATOM   29923 O  "O5'" . DC  J 10 7    ? 149.014 132.372 138.540 1.00 105.03 ? -18  DC  Y "O5'" 1 
ATOM   29924 C  "C5'" . DC  J 10 7    ? 148.368 131.946 137.345 1.00 103.58 ? -18  DC  Y "C5'" 1 
ATOM   29925 C  "C4'" . DC  J 10 7    ? 147.705 133.111 136.626 1.00 103.76 ? -18  DC  Y "C4'" 1 
ATOM   29926 O  "O4'" . DC  J 10 7    ? 146.939 133.899 137.575 1.00 104.89 ? -18  DC  Y "O4'" 1 
ATOM   29927 C  "C3'" . DC  J 10 7    ? 148.662 134.083 135.934 1.00 102.78 ? -18  DC  Y "C3'" 1 
ATOM   29928 O  "O3'" . DC  J 10 7    ? 148.136 134.467 134.669 1.00 101.73 ? -18  DC  Y "O3'" 1 
ATOM   29929 C  "C2'" . DC  J 10 7    ? 148.721 135.265 136.898 1.00 103.31 ? -18  DC  Y "C2'" 1 
ATOM   29930 C  "C1'" . DC  J 10 7    ? 147.319 135.255 137.490 1.00 104.45 ? -18  DC  Y "C1'" 1 
ATOM   29931 N  N1    . DC  J 10 7    ? 147.252 135.847 138.853 1.00 104.92 ? -18  DC  Y N1    1 
ATOM   29932 C  C2    . DC  J 10 7    ? 146.327 136.861 139.121 1.00 104.76 ? -18  DC  Y C2    1 
ATOM   29933 O  O2    . DC  J 10 7    ? 145.575 137.245 138.216 1.00 103.50 ? -18  DC  Y O2    1 
ATOM   29934 N  N3    . DC  J 10 7    ? 146.280 137.393 140.370 1.00 104.93 ? -18  DC  Y N3    1 
ATOM   29935 C  C4    . DC  J 10 7    ? 147.107 136.947 141.317 1.00 104.07 ? -18  DC  Y C4    1 
ATOM   29936 N  N4    . DC  J 10 7    ? 147.024 137.501 142.531 1.00 103.60 ? -18  DC  Y N4    1 
ATOM   29937 C  C5    . DC  J 10 7    ? 148.057 135.914 141.061 1.00 103.26 ? -18  DC  Y C5    1 
ATOM   29938 C  C6    . DC  J 10 7    ? 148.093 135.399 139.828 1.00 103.56 ? -18  DC  Y C6    1 
HETATM 29939 MG MG    . MG  K 11 .    ? 128.906 141.025 119.199 1.00 17.57  ? 1501 MG  A MG    1 
HETATM 29940 ZN ZN    . ZN  L 12 .    ? 165.677 108.087 124.751 1.00 64.77  ? 1502 ZN  A ZN    1 
HETATM 29941 ZN ZN    . ZN  M 12 .    ? 157.969 93.185  127.270 1.00 66.81  ? 1301 ZN  B ZN    1 
HETATM 29942 ZN ZN    . ZN  N 12 .    ? 97.065  168.693 167.095 1.00 76.21  ? 201  ZN  G ZN    1 
HETATM 29943 ZN ZN    . ZN  O 12 .    ? 131.318 169.940 102.353 1.00 37.39  ? 101  ZN  H ZN    1 
# 
