data_9CJI
# 
_entry.id   9CJI 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9CJI         pdb_00009cji 10.2210/pdb9cji/pdb 
WWPDB D_1000285687 ?            ?                   
EMDB  EMD-45632    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1  'Structure model' 1 0 2025-01-08 ? 
2  'EM metadata'     1 0 2025-01-08 ? 
3  'Additional map'  1 0 2025-01-08 ? 
4  FSC               1 0 2025-01-08 ? 
5  'Half map'        1 0 2025-01-08 1 
6  'Half map'        1 0 2025-01-08 2 
7  Image             1 0 2025-01-08 ? 
8  Mask              1 0 2025-01-08 ? 
9  'Primary map'     1 0 2025-01-08 ? 
10 'Structure model' 1 1 2025-02-12 ? 
11 'Additional map'  1 0 2025-01-08 ? 
12 FSC               1 0 2025-01-08 ? 
13 'Half map'        1 0 2025-01-08 1 
14 'Half map'        1 0 2025-01-08 2 
15 Image             1 0 2025-01-08 ? 
16 Mask              1 0 2025-01-08 ? 
17 'Primary map'     1 0 2025-01-08 ? 
18 'Structure model' 2 0 2025-06-18 ? 
19 'EM metadata'     2 0 2025-06-18 ? 
20 'Additional map'  2 0 2025-06-18 2 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1  1  'Structure model' repository 'Initial release' ? ? 
2  2  'EM metadata'     repository 'Initial release' ? ? 
3  3  'Additional map'  repository 'Initial release' ? ? 
4  4  FSC               repository 'Initial release' ? ? 
5  5  'Half map'        repository 'Initial release' ? ? 
6  6  'Half map'        repository 'Initial release' ? ? 
7  7  Image             repository 'Initial release' ? ? 
8  8  Mask              repository 'Initial release' ? ? 
9  9  'Primary map'     repository 'Initial release' ? ? 
10 11 'Additional map'  repository 'Initial release' ? ? 
11 12 FSC               repository 'Initial release' ? ? 
12 13 'Half map'        repository 'Initial release' ? ? 
13 14 'Half map'        repository 'Initial release' ? ? 
14 15 Image             repository 'Initial release' ? ? 
15 16 Mask              repository 'Initial release' ? ? 
16 17 'Primary map'     repository 'Initial release' ? ? 
17 20 'Additional map'  repository 'Data updated'    ? ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1  10 'Structure model' 'Data collection'        
2  10 'Structure model' 'Database references'    
3  10 'Structure model' 'Derived calculations'   
4  10 'Structure model' 'Structure summary'      
5  18 'Structure model' Advisory                 
6  18 'Structure model' 'Atomic model'           
7  18 'Structure model' 'Data collection'        
8  18 'Structure model' 'Derived calculations'   
9  18 'Structure model' 'Refinement description' 
10 18 'Structure model' 'Structure summary'      
11 19 'EM metadata'     'Experimental summary'   
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1  10 'Structure model' citation                    
2  10 'Structure model' citation_author             
3  10 'Structure model' em_admin                    
4  10 'Structure model' pdbx_contact_author         
5  10 'Structure model' pdbx_struct_assembly        
6  18 'Structure model' atom_site                   
7  18 'Structure model' database_PDB_caveat         
8  18 'Structure model' em_admin                    
9  18 'Structure model' pdbx_poly_seq_scheme        
10 18 'Structure model' pdbx_struct_assembly        
11 18 'Structure model' pdbx_validate_close_contact 
12 18 'Structure model' pdbx_validate_torsion       
13 18 'Structure model' refine                      
14 18 'Structure model' refine_ls_restr             
15 18 'Structure model' software                    
16 18 'Structure model' struct_conf                 
17 19 'EM metadata'     em_admin                    
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  10 'Structure model' '_citation.journal_volume'                   
2  10 'Structure model' '_citation.year'                             
3  10 'Structure model' '_citation_author.identifier_ORCID'          
4  10 'Structure model' '_em_admin.last_update'                      
5  10 'Structure model' '_pdbx_struct_assembly.details'              
6  18 'Structure model' '_atom_site.Cartn_x'                         
7  18 'Structure model' '_atom_site.Cartn_y'                         
8  18 'Structure model' '_atom_site.Cartn_z'                         
9  18 'Structure model' '_em_admin.last_update'                      
10 18 'Structure model' '_pdbx_poly_seq_scheme.auth_mon_id'          
11 18 'Structure model' '_pdbx_struct_assembly.details'              
12 18 'Structure model' '_pdbx_validate_torsion.auth_comp_id'        
13 18 'Structure model' '_pdbx_validate_torsion.auth_seq_id'         
14 18 'Structure model' '_pdbx_validate_torsion.phi'                 
15 18 'Structure model' '_pdbx_validate_torsion.psi'                 
16 18 'Structure model' '_refine.ls_d_res_high'                      
17 18 'Structure model' '_refine.pdbx_stereochemistry_target_values' 
18 18 'Structure model' '_refine_ls_restr.dev_ideal'                 
19 18 'Structure model' '_refine_ls_restr.number'                    
20 19 'EM metadata'     '_em_admin.last_update'                      
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CJI 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-06 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
EMDB .                                                                              EMD-45631 'other EM volume'      
PDB  .                                                                              9CJH      unspecified            
EMDB 'Cas12a:gRNA:DNA (Acidaminococcus sp.) with 0 RNA:DNA base pairs, structure 2' EMD-45632 'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              doudna@berkeley.edu 
_pdbx_contact_author.name_first         Jennifer 
_pdbx_contact_author.name_last          Doudna 
_pdbx_contact_author.name_mi            A 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9161-999X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Soczek, K.M.' 1 0000-0003-3803-6079 
'Doudna, J.A.' 2 0000-0001-9161-999X 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nucleic Acids Res.' 
_citation.journal_id_ASTM           NARHAD 
_citation.journal_id_CSD            0389 
_citation.journal_id_ISSN           1362-4962 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            53 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'CRISPR-Cas12a bends DNA to destabilize base pairs during target interrogation.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1093/nar/gkae1192 
_citation.pdbx_database_id_PubMed   39698811 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Soczek, K.M.' 1 ? 
primary 'Cofsky, J.C.' 2 ? 
primary 'Tuck, O.T.'   3 ? 
primary 'Shi, H.'      4 ? 
primary 'Doudna, J.A.' 5 ? 
# 
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 syn 'Non-target DNA strand'                 9567.206   1 ?                 ?     ? 
;cytidine in position 7 is covalently modified, forming N4-cystamine-2'-deoxycytidine (2YR); the modified base is forming a disulfide bond with cysteine 551 in the protein
;
2 polymer syn 'guide RNA (25-MER)'                    13418.956  1 ?                 ?     ? ? 
3 polymer syn 'Target DNA strand'                     9557.205   1 ?                 ?     ? ? 
4 polymer man 'CRISPR-associated endonuclease Cas12a' 151680.250 1 3.1.21.1,4.6.1.22 N551C ? ? 
# 
_entity_name_com.entity_id   4 
_entity_name_com.name        'AsCpf1,CRISPR-associated endonuclease Cpf1' 
# 
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 polydeoxyribonucleotide no yes 
;(DG)(DT)(DA)(DG)(DT)(DG)(2YR)(DT)(DT)(DT)(DG)(DT)(DC)(DG)(DT)(DC)(DT)(DC)(DA)
(DT)(DC)(DT)(DG)(DT)(DA)(DT)(DG)(DC)(DG)(DT)(DC)
;
GTAGTGXTTTGTCGTCTCATCTGTATGCGTC C ? 
2 polyribonucleotide      no no  UUUAAUUUCUACUCUUGUAGAUAGCAGAGUAGACAUACGCAG UUUAAUUUCUACUCUUGUAGAUAGCAGAGUAGACAUACGCAG B ? 
3 polydeoxyribonucleotide no no  
;(DG)(DA)(DC)(DG)(DC)(DA)(DT)(DA)(DC)(DA)(DG)(DA)(DT)(DG)(DA)(DG)(DA)(DC)(DG)(DA)
(DC)(DA)(DA)(DA)(DG)(DC)(DA)(DC)(DT)(DA)(DC)
;
GACGCATACAGATGAGACGACAAAGCACTAC D ? 
4 'polypeptide(L)'        no no  
;SNAMTQFEGFTNLYQVSKTLRFELIPQGKTLKHIQEQGFIEEDKARNDHYKELKPIIDRIYKTYADQCLQLVQLDWENLS
AAIDSYRKEKTEETRNALIEEQATYRNAIHDYFIGRTDNLTDAINKRHAEIYKGLFKAELFNGKVLKQLGTVTTTEHENA
LLRSFDKFTTYFSGFYENRKNVFSAEDISTAIPHRIVQDNFPKFKENCHIFTRLITAVPSLREHFENVKKAIGIFVSTSI
EEVFSFPFYNQLLTQTQIDLYNQLLGGISREAGTEKIKGLNEVLNLAIQKNDETAHIIASLPHRFIPLFKQILSDRNTLS
FILEEFKSDEEVIQSFCKYKTLLRNENVLETAEALFNELNSIDLTHIFISHKKLETISSALCDHWDTLRNALYERRISEL
TGKITKSAKEKVQRSLKHEDINLQEIISAAGKELSEAFKQKTSEILSHAHAALDQPLPTTLKKQEEKEILKSQLDSLLGL
YHLLDWFAVDESNEVDPEFSARLTGIKLEMEPSLSFYNKARNYATKKPYSVEKFKLNFQMPTLASGWDVNKEKCNGAILF
VKNGLYYLGIMPKQKGRYKALSFEPTEKTSEGFDKMYYDYFPDAAKMIPKCSTQLKAVTAHFQTHTTPILLSNNFIEPLE
ITKEIYDLNNPEKEPKKFQTAYAKKTGDQKGYREALCKWIDFTRDFLSKYTKTTSIDLSSLRPSSQYKDLGEYYAELNPL
LYHISFQRIAEKEIMDAVETGKLYLFQIYNKDFAKGHHGKPNLHTLYWTGLFSPENLAKTSIKLNGQAELFYRPKSRMKR
MAHRLGEKMLNKKLKDQKTPIPDTLYQELYDYVNHRLSHDLSDEARALLPNVITKEVSHEIIKDRRFTSDKFFFHVPITL
NYQAANSPSKFNQRVNAYLKEHPETPIIGIDRGERNLIYITVIDSTGKILEQRSLNTIQQFDYQKKLDNREKERVAARQA
WSVVGTIKDLKQGYLSQVIHEIVDLMIHYQAVVVLENLNFGFKSKRTGIAEKAVYQQFEKMLIDKLNCLVLKDYPAEKVG
GVLNPYQLTDQFTSFAKMGTQSGFLFYVPAPYTSKIDPLTGFVDPFVWKTIKNHESRKHFLEGFDFLHYDVKTGDFILHF
KMNRNLSFQRGLPGFMPAWDIVFEKNETQFDAKGTPFIAGKRIVPVIENHRFTGRYRDLYPANELIALLEEKGIVFRDGS
NILPKLLENDDSHAIDTMVALIRSVLQMRNSNAATGEDYINSPVRDLNGVCFDSRFQNPEWPMDADANGAYHIALKGQLL
LNHLKESKDLKLQNGISNQDWLAYIQELRN
;
;SNAMTQFEGFTNLYQVSKTLRFELIPQGKTLKHIQEQGFIEEDKARNDHYKELKPIIDRIYKTYADQCLQLVQLDWENLS
AAIDSYRKEKTEETRNALIEEQATYRNAIHDYFIGRTDNLTDAINKRHAEIYKGLFKAELFNGKVLKQLGTVTTTEHENA
LLRSFDKFTTYFSGFYENRKNVFSAEDISTAIPHRIVQDNFPKFKENCHIFTRLITAVPSLREHFENVKKAIGIFVSTSI
EEVFSFPFYNQLLTQTQIDLYNQLLGGISREAGTEKIKGLNEVLNLAIQKNDETAHIIASLPHRFIPLFKQILSDRNTLS
FILEEFKSDEEVIQSFCKYKTLLRNENVLETAEALFNELNSIDLTHIFISHKKLETISSALCDHWDTLRNALYERRISEL
TGKITKSAKEKVQRSLKHEDINLQEIISAAGKELSEAFKQKTSEILSHAHAALDQPLPTTLKKQEEKEILKSQLDSLLGL
YHLLDWFAVDESNEVDPEFSARLTGIKLEMEPSLSFYNKARNYATKKPYSVEKFKLNFQMPTLASGWDVNKEKCNGAILF
VKNGLYYLGIMPKQKGRYKALSFEPTEKTSEGFDKMYYDYFPDAAKMIPKCSTQLKAVTAHFQTHTTPILLSNNFIEPLE
ITKEIYDLNNPEKEPKKFQTAYAKKTGDQKGYREALCKWIDFTRDFLSKYTKTTSIDLSSLRPSSQYKDLGEYYAELNPL
LYHISFQRIAEKEIMDAVETGKLYLFQIYNKDFAKGHHGKPNLHTLYWTGLFSPENLAKTSIKLNGQAELFYRPKSRMKR
MAHRLGEKMLNKKLKDQKTPIPDTLYQELYDYVNHRLSHDLSDEARALLPNVITKEVSHEIIKDRRFTSDKFFFHVPITL
NYQAANSPSKFNQRVNAYLKEHPETPIIGIDRGERNLIYITVIDSTGKILEQRSLNTIQQFDYQKKLDNREKERVAARQA
WSVVGTIKDLKQGYLSQVIHEIVDLMIHYQAVVVLENLNFGFKSKRTGIAEKAVYQQFEKMLIDKLNCLVLKDYPAEKVG
GVLNPYQLTDQFTSFAKMGTQSGFLFYVPAPYTSKIDPLTGFVDPFVWKTIKNHESRKHFLEGFDFLHYDVKTGDFILHF
KMNRNLSFQRGLPGFMPAWDIVFEKNETQFDAKGTPFIAGKRIVPVIENHRFTGRYRDLYPANELIALLEEKGIVFRDGS
NILPKLLENDDSHAIDTMVALIRSVLQMRNSNAATGEDYINSPVRDLNGVCFDSRFQNPEWPMDADANGAYHIALKGQLL
LNHLKESKDLKLQNGISNQDWLAYIQELRN
;
A ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    DG  n 
1 2    DT  n 
1 3    DA  n 
1 4    DG  n 
1 5    DT  n 
1 6    DG  n 
1 7    2YR n 
1 8    DT  n 
1 9    DT  n 
1 10   DT  n 
1 11   DG  n 
1 12   DT  n 
1 13   DC  n 
1 14   DG  n 
1 15   DT  n 
1 16   DC  n 
1 17   DT  n 
1 18   DC  n 
1 19   DA  n 
1 20   DT  n 
1 21   DC  n 
1 22   DT  n 
1 23   DG  n 
1 24   DT  n 
1 25   DA  n 
1 26   DT  n 
1 27   DG  n 
1 28   DC  n 
1 29   DG  n 
1 30   DT  n 
1 31   DC  n 
2 1    U   n 
2 2    U   n 
2 3    U   n 
2 4    A   n 
2 5    A   n 
2 6    U   n 
2 7    U   n 
2 8    U   n 
2 9    C   n 
2 10   U   n 
2 11   A   n 
2 12   C   n 
2 13   U   n 
2 14   C   n 
2 15   U   n 
2 16   U   n 
2 17   G   n 
2 18   U   n 
2 19   A   n 
2 20   G   n 
2 21   A   n 
2 22   U   n 
2 23   A   n 
2 24   G   n 
2 25   C   n 
2 26   A   n 
2 27   G   n 
2 28   A   n 
2 29   G   n 
2 30   U   n 
2 31   A   n 
2 32   G   n 
2 33   A   n 
2 34   C   n 
2 35   A   n 
2 36   U   n 
2 37   A   n 
2 38   C   n 
2 39   G   n 
2 40   C   n 
2 41   A   n 
2 42   G   n 
3 1    DG  n 
3 2    DA  n 
3 3    DC  n 
3 4    DG  n 
3 5    DC  n 
3 6    DA  n 
3 7    DT  n 
3 8    DA  n 
3 9    DC  n 
3 10   DA  n 
3 11   DG  n 
3 12   DA  n 
3 13   DT  n 
3 14   DG  n 
3 15   DA  n 
3 16   DG  n 
3 17   DA  n 
3 18   DC  n 
3 19   DG  n 
3 20   DA  n 
3 21   DC  n 
3 22   DA  n 
3 23   DA  n 
3 24   DA  n 
3 25   DG  n 
3 26   DC  n 
3 27   DA  n 
3 28   DC  n 
3 29   DT  n 
3 30   DA  n 
3 31   DC  n 
4 1    SER n 
4 2    ASN n 
4 3    ALA n 
4 4    MET n 
4 5    THR n 
4 6    GLN n 
4 7    PHE n 
4 8    GLU n 
4 9    GLY n 
4 10   PHE n 
4 11   THR n 
4 12   ASN n 
4 13   LEU n 
4 14   TYR n 
4 15   GLN n 
4 16   VAL n 
4 17   SER n 
4 18   LYS n 
4 19   THR n 
4 20   LEU n 
4 21   ARG n 
4 22   PHE n 
4 23   GLU n 
4 24   LEU n 
4 25   ILE n 
4 26   PRO n 
4 27   GLN n 
4 28   GLY n 
4 29   LYS n 
4 30   THR n 
4 31   LEU n 
4 32   LYS n 
4 33   HIS n 
4 34   ILE n 
4 35   GLN n 
4 36   GLU n 
4 37   GLN n 
4 38   GLY n 
4 39   PHE n 
4 40   ILE n 
4 41   GLU n 
4 42   GLU n 
4 43   ASP n 
4 44   LYS n 
4 45   ALA n 
4 46   ARG n 
4 47   ASN n 
4 48   ASP n 
4 49   HIS n 
4 50   TYR n 
4 51   LYS n 
4 52   GLU n 
4 53   LEU n 
4 54   LYS n 
4 55   PRO n 
4 56   ILE n 
4 57   ILE n 
4 58   ASP n 
4 59   ARG n 
4 60   ILE n 
4 61   TYR n 
4 62   LYS n 
4 63   THR n 
4 64   TYR n 
4 65   ALA n 
4 66   ASP n 
4 67   GLN n 
4 68   CYS n 
4 69   LEU n 
4 70   GLN n 
4 71   LEU n 
4 72   VAL n 
4 73   GLN n 
4 74   LEU n 
4 75   ASP n 
4 76   TRP n 
4 77   GLU n 
4 78   ASN n 
4 79   LEU n 
4 80   SER n 
4 81   ALA n 
4 82   ALA n 
4 83   ILE n 
4 84   ASP n 
4 85   SER n 
4 86   TYR n 
4 87   ARG n 
4 88   LYS n 
4 89   GLU n 
4 90   LYS n 
4 91   THR n 
4 92   GLU n 
4 93   GLU n 
4 94   THR n 
4 95   ARG n 
4 96   ASN n 
4 97   ALA n 
4 98   LEU n 
4 99   ILE n 
4 100  GLU n 
4 101  GLU n 
4 102  GLN n 
4 103  ALA n 
4 104  THR n 
4 105  TYR n 
4 106  ARG n 
4 107  ASN n 
4 108  ALA n 
4 109  ILE n 
4 110  HIS n 
4 111  ASP n 
4 112  TYR n 
4 113  PHE n 
4 114  ILE n 
4 115  GLY n 
4 116  ARG n 
4 117  THR n 
4 118  ASP n 
4 119  ASN n 
4 120  LEU n 
4 121  THR n 
4 122  ASP n 
4 123  ALA n 
4 124  ILE n 
4 125  ASN n 
4 126  LYS n 
4 127  ARG n 
4 128  HIS n 
4 129  ALA n 
4 130  GLU n 
4 131  ILE n 
4 132  TYR n 
4 133  LYS n 
4 134  GLY n 
4 135  LEU n 
4 136  PHE n 
4 137  LYS n 
4 138  ALA n 
4 139  GLU n 
4 140  LEU n 
4 141  PHE n 
4 142  ASN n 
4 143  GLY n 
4 144  LYS n 
4 145  VAL n 
4 146  LEU n 
4 147  LYS n 
4 148  GLN n 
4 149  LEU n 
4 150  GLY n 
4 151  THR n 
4 152  VAL n 
4 153  THR n 
4 154  THR n 
4 155  THR n 
4 156  GLU n 
4 157  HIS n 
4 158  GLU n 
4 159  ASN n 
4 160  ALA n 
4 161  LEU n 
4 162  LEU n 
4 163  ARG n 
4 164  SER n 
4 165  PHE n 
4 166  ASP n 
4 167  LYS n 
4 168  PHE n 
4 169  THR n 
4 170  THR n 
4 171  TYR n 
4 172  PHE n 
4 173  SER n 
4 174  GLY n 
4 175  PHE n 
4 176  TYR n 
4 177  GLU n 
4 178  ASN n 
4 179  ARG n 
4 180  LYS n 
4 181  ASN n 
4 182  VAL n 
4 183  PHE n 
4 184  SER n 
4 185  ALA n 
4 186  GLU n 
4 187  ASP n 
4 188  ILE n 
4 189  SER n 
4 190  THR n 
4 191  ALA n 
4 192  ILE n 
4 193  PRO n 
4 194  HIS n 
4 195  ARG n 
4 196  ILE n 
4 197  VAL n 
4 198  GLN n 
4 199  ASP n 
4 200  ASN n 
4 201  PHE n 
4 202  PRO n 
4 203  LYS n 
4 204  PHE n 
4 205  LYS n 
4 206  GLU n 
4 207  ASN n 
4 208  CYS n 
4 209  HIS n 
4 210  ILE n 
4 211  PHE n 
4 212  THR n 
4 213  ARG n 
4 214  LEU n 
4 215  ILE n 
4 216  THR n 
4 217  ALA n 
4 218  VAL n 
4 219  PRO n 
4 220  SER n 
4 221  LEU n 
4 222  ARG n 
4 223  GLU n 
4 224  HIS n 
4 225  PHE n 
4 226  GLU n 
4 227  ASN n 
4 228  VAL n 
4 229  LYS n 
4 230  LYS n 
4 231  ALA n 
4 232  ILE n 
4 233  GLY n 
4 234  ILE n 
4 235  PHE n 
4 236  VAL n 
4 237  SER n 
4 238  THR n 
4 239  SER n 
4 240  ILE n 
4 241  GLU n 
4 242  GLU n 
4 243  VAL n 
4 244  PHE n 
4 245  SER n 
4 246  PHE n 
4 247  PRO n 
4 248  PHE n 
4 249  TYR n 
4 250  ASN n 
4 251  GLN n 
4 252  LEU n 
4 253  LEU n 
4 254  THR n 
4 255  GLN n 
4 256  THR n 
4 257  GLN n 
4 258  ILE n 
4 259  ASP n 
4 260  LEU n 
4 261  TYR n 
4 262  ASN n 
4 263  GLN n 
4 264  LEU n 
4 265  LEU n 
4 266  GLY n 
4 267  GLY n 
4 268  ILE n 
4 269  SER n 
4 270  ARG n 
4 271  GLU n 
4 272  ALA n 
4 273  GLY n 
4 274  THR n 
4 275  GLU n 
4 276  LYS n 
4 277  ILE n 
4 278  LYS n 
4 279  GLY n 
4 280  LEU n 
4 281  ASN n 
4 282  GLU n 
4 283  VAL n 
4 284  LEU n 
4 285  ASN n 
4 286  LEU n 
4 287  ALA n 
4 288  ILE n 
4 289  GLN n 
4 290  LYS n 
4 291  ASN n 
4 292  ASP n 
4 293  GLU n 
4 294  THR n 
4 295  ALA n 
4 296  HIS n 
4 297  ILE n 
4 298  ILE n 
4 299  ALA n 
4 300  SER n 
4 301  LEU n 
4 302  PRO n 
4 303  HIS n 
4 304  ARG n 
4 305  PHE n 
4 306  ILE n 
4 307  PRO n 
4 308  LEU n 
4 309  PHE n 
4 310  LYS n 
4 311  GLN n 
4 312  ILE n 
4 313  LEU n 
4 314  SER n 
4 315  ASP n 
4 316  ARG n 
4 317  ASN n 
4 318  THR n 
4 319  LEU n 
4 320  SER n 
4 321  PHE n 
4 322  ILE n 
4 323  LEU n 
4 324  GLU n 
4 325  GLU n 
4 326  PHE n 
4 327  LYS n 
4 328  SER n 
4 329  ASP n 
4 330  GLU n 
4 331  GLU n 
4 332  VAL n 
4 333  ILE n 
4 334  GLN n 
4 335  SER n 
4 336  PHE n 
4 337  CYS n 
4 338  LYS n 
4 339  TYR n 
4 340  LYS n 
4 341  THR n 
4 342  LEU n 
4 343  LEU n 
4 344  ARG n 
4 345  ASN n 
4 346  GLU n 
4 347  ASN n 
4 348  VAL n 
4 349  LEU n 
4 350  GLU n 
4 351  THR n 
4 352  ALA n 
4 353  GLU n 
4 354  ALA n 
4 355  LEU n 
4 356  PHE n 
4 357  ASN n 
4 358  GLU n 
4 359  LEU n 
4 360  ASN n 
4 361  SER n 
4 362  ILE n 
4 363  ASP n 
4 364  LEU n 
4 365  THR n 
4 366  HIS n 
4 367  ILE n 
4 368  PHE n 
4 369  ILE n 
4 370  SER n 
4 371  HIS n 
4 372  LYS n 
4 373  LYS n 
4 374  LEU n 
4 375  GLU n 
4 376  THR n 
4 377  ILE n 
4 378  SER n 
4 379  SER n 
4 380  ALA n 
4 381  LEU n 
4 382  CYS n 
4 383  ASP n 
4 384  HIS n 
4 385  TRP n 
4 386  ASP n 
4 387  THR n 
4 388  LEU n 
4 389  ARG n 
4 390  ASN n 
4 391  ALA n 
4 392  LEU n 
4 393  TYR n 
4 394  GLU n 
4 395  ARG n 
4 396  ARG n 
4 397  ILE n 
4 398  SER n 
4 399  GLU n 
4 400  LEU n 
4 401  THR n 
4 402  GLY n 
4 403  LYS n 
4 404  ILE n 
4 405  THR n 
4 406  LYS n 
4 407  SER n 
4 408  ALA n 
4 409  LYS n 
4 410  GLU n 
4 411  LYS n 
4 412  VAL n 
4 413  GLN n 
4 414  ARG n 
4 415  SER n 
4 416  LEU n 
4 417  LYS n 
4 418  HIS n 
4 419  GLU n 
4 420  ASP n 
4 421  ILE n 
4 422  ASN n 
4 423  LEU n 
4 424  GLN n 
4 425  GLU n 
4 426  ILE n 
4 427  ILE n 
4 428  SER n 
4 429  ALA n 
4 430  ALA n 
4 431  GLY n 
4 432  LYS n 
4 433  GLU n 
4 434  LEU n 
4 435  SER n 
4 436  GLU n 
4 437  ALA n 
4 438  PHE n 
4 439  LYS n 
4 440  GLN n 
4 441  LYS n 
4 442  THR n 
4 443  SER n 
4 444  GLU n 
4 445  ILE n 
4 446  LEU n 
4 447  SER n 
4 448  HIS n 
4 449  ALA n 
4 450  HIS n 
4 451  ALA n 
4 452  ALA n 
4 453  LEU n 
4 454  ASP n 
4 455  GLN n 
4 456  PRO n 
4 457  LEU n 
4 458  PRO n 
4 459  THR n 
4 460  THR n 
4 461  LEU n 
4 462  LYS n 
4 463  LYS n 
4 464  GLN n 
4 465  GLU n 
4 466  GLU n 
4 467  LYS n 
4 468  GLU n 
4 469  ILE n 
4 470  LEU n 
4 471  LYS n 
4 472  SER n 
4 473  GLN n 
4 474  LEU n 
4 475  ASP n 
4 476  SER n 
4 477  LEU n 
4 478  LEU n 
4 479  GLY n 
4 480  LEU n 
4 481  TYR n 
4 482  HIS n 
4 483  LEU n 
4 484  LEU n 
4 485  ASP n 
4 486  TRP n 
4 487  PHE n 
4 488  ALA n 
4 489  VAL n 
4 490  ASP n 
4 491  GLU n 
4 492  SER n 
4 493  ASN n 
4 494  GLU n 
4 495  VAL n 
4 496  ASP n 
4 497  PRO n 
4 498  GLU n 
4 499  PHE n 
4 500  SER n 
4 501  ALA n 
4 502  ARG n 
4 503  LEU n 
4 504  THR n 
4 505  GLY n 
4 506  ILE n 
4 507  LYS n 
4 508  LEU n 
4 509  GLU n 
4 510  MET n 
4 511  GLU n 
4 512  PRO n 
4 513  SER n 
4 514  LEU n 
4 515  SER n 
4 516  PHE n 
4 517  TYR n 
4 518  ASN n 
4 519  LYS n 
4 520  ALA n 
4 521  ARG n 
4 522  ASN n 
4 523  TYR n 
4 524  ALA n 
4 525  THR n 
4 526  LYS n 
4 527  LYS n 
4 528  PRO n 
4 529  TYR n 
4 530  SER n 
4 531  VAL n 
4 532  GLU n 
4 533  LYS n 
4 534  PHE n 
4 535  LYS n 
4 536  LEU n 
4 537  ASN n 
4 538  PHE n 
4 539  GLN n 
4 540  MET n 
4 541  PRO n 
4 542  THR n 
4 543  LEU n 
4 544  ALA n 
4 545  SER n 
4 546  GLY n 
4 547  TRP n 
4 548  ASP n 
4 549  VAL n 
4 550  ASN n 
4 551  LYS n 
4 552  GLU n 
4 553  LYS n 
4 554  CYS n 
4 555  ASN n 
4 556  GLY n 
4 557  ALA n 
4 558  ILE n 
4 559  LEU n 
4 560  PHE n 
4 561  VAL n 
4 562  LYS n 
4 563  ASN n 
4 564  GLY n 
4 565  LEU n 
4 566  TYR n 
4 567  TYR n 
4 568  LEU n 
4 569  GLY n 
4 570  ILE n 
4 571  MET n 
4 572  PRO n 
4 573  LYS n 
4 574  GLN n 
4 575  LYS n 
4 576  GLY n 
4 577  ARG n 
4 578  TYR n 
4 579  LYS n 
4 580  ALA n 
4 581  LEU n 
4 582  SER n 
4 583  PHE n 
4 584  GLU n 
4 585  PRO n 
4 586  THR n 
4 587  GLU n 
4 588  LYS n 
4 589  THR n 
4 590  SER n 
4 591  GLU n 
4 592  GLY n 
4 593  PHE n 
4 594  ASP n 
4 595  LYS n 
4 596  MET n 
4 597  TYR n 
4 598  TYR n 
4 599  ASP n 
4 600  TYR n 
4 601  PHE n 
4 602  PRO n 
4 603  ASP n 
4 604  ALA n 
4 605  ALA n 
4 606  LYS n 
4 607  MET n 
4 608  ILE n 
4 609  PRO n 
4 610  LYS n 
4 611  CYS n 
4 612  SER n 
4 613  THR n 
4 614  GLN n 
4 615  LEU n 
4 616  LYS n 
4 617  ALA n 
4 618  VAL n 
4 619  THR n 
4 620  ALA n 
4 621  HIS n 
4 622  PHE n 
4 623  GLN n 
4 624  THR n 
4 625  HIS n 
4 626  THR n 
4 627  THR n 
4 628  PRO n 
4 629  ILE n 
4 630  LEU n 
4 631  LEU n 
4 632  SER n 
4 633  ASN n 
4 634  ASN n 
4 635  PHE n 
4 636  ILE n 
4 637  GLU n 
4 638  PRO n 
4 639  LEU n 
4 640  GLU n 
4 641  ILE n 
4 642  THR n 
4 643  LYS n 
4 644  GLU n 
4 645  ILE n 
4 646  TYR n 
4 647  ASP n 
4 648  LEU n 
4 649  ASN n 
4 650  ASN n 
4 651  PRO n 
4 652  GLU n 
4 653  LYS n 
4 654  GLU n 
4 655  PRO n 
4 656  LYS n 
4 657  LYS n 
4 658  PHE n 
4 659  GLN n 
4 660  THR n 
4 661  ALA n 
4 662  TYR n 
4 663  ALA n 
4 664  LYS n 
4 665  LYS n 
4 666  THR n 
4 667  GLY n 
4 668  ASP n 
4 669  GLN n 
4 670  LYS n 
4 671  GLY n 
4 672  TYR n 
4 673  ARG n 
4 674  GLU n 
4 675  ALA n 
4 676  LEU n 
4 677  CYS n 
4 678  LYS n 
4 679  TRP n 
4 680  ILE n 
4 681  ASP n 
4 682  PHE n 
4 683  THR n 
4 684  ARG n 
4 685  ASP n 
4 686  PHE n 
4 687  LEU n 
4 688  SER n 
4 689  LYS n 
4 690  TYR n 
4 691  THR n 
4 692  LYS n 
4 693  THR n 
4 694  THR n 
4 695  SER n 
4 696  ILE n 
4 697  ASP n 
4 698  LEU n 
4 699  SER n 
4 700  SER n 
4 701  LEU n 
4 702  ARG n 
4 703  PRO n 
4 704  SER n 
4 705  SER n 
4 706  GLN n 
4 707  TYR n 
4 708  LYS n 
4 709  ASP n 
4 710  LEU n 
4 711  GLY n 
4 712  GLU n 
4 713  TYR n 
4 714  TYR n 
4 715  ALA n 
4 716  GLU n 
4 717  LEU n 
4 718  ASN n 
4 719  PRO n 
4 720  LEU n 
4 721  LEU n 
4 722  TYR n 
4 723  HIS n 
4 724  ILE n 
4 725  SER n 
4 726  PHE n 
4 727  GLN n 
4 728  ARG n 
4 729  ILE n 
4 730  ALA n 
4 731  GLU n 
4 732  LYS n 
4 733  GLU n 
4 734  ILE n 
4 735  MET n 
4 736  ASP n 
4 737  ALA n 
4 738  VAL n 
4 739  GLU n 
4 740  THR n 
4 741  GLY n 
4 742  LYS n 
4 743  LEU n 
4 744  TYR n 
4 745  LEU n 
4 746  PHE n 
4 747  GLN n 
4 748  ILE n 
4 749  TYR n 
4 750  ASN n 
4 751  LYS n 
4 752  ASP n 
4 753  PHE n 
4 754  ALA n 
4 755  LYS n 
4 756  GLY n 
4 757  HIS n 
4 758  HIS n 
4 759  GLY n 
4 760  LYS n 
4 761  PRO n 
4 762  ASN n 
4 763  LEU n 
4 764  HIS n 
4 765  THR n 
4 766  LEU n 
4 767  TYR n 
4 768  TRP n 
4 769  THR n 
4 770  GLY n 
4 771  LEU n 
4 772  PHE n 
4 773  SER n 
4 774  PRO n 
4 775  GLU n 
4 776  ASN n 
4 777  LEU n 
4 778  ALA n 
4 779  LYS n 
4 780  THR n 
4 781  SER n 
4 782  ILE n 
4 783  LYS n 
4 784  LEU n 
4 785  ASN n 
4 786  GLY n 
4 787  GLN n 
4 788  ALA n 
4 789  GLU n 
4 790  LEU n 
4 791  PHE n 
4 792  TYR n 
4 793  ARG n 
4 794  PRO n 
4 795  LYS n 
4 796  SER n 
4 797  ARG n 
4 798  MET n 
4 799  LYS n 
4 800  ARG n 
4 801  MET n 
4 802  ALA n 
4 803  HIS n 
4 804  ARG n 
4 805  LEU n 
4 806  GLY n 
4 807  GLU n 
4 808  LYS n 
4 809  MET n 
4 810  LEU n 
4 811  ASN n 
4 812  LYS n 
4 813  LYS n 
4 814  LEU n 
4 815  LYS n 
4 816  ASP n 
4 817  GLN n 
4 818  LYS n 
4 819  THR n 
4 820  PRO n 
4 821  ILE n 
4 822  PRO n 
4 823  ASP n 
4 824  THR n 
4 825  LEU n 
4 826  TYR n 
4 827  GLN n 
4 828  GLU n 
4 829  LEU n 
4 830  TYR n 
4 831  ASP n 
4 832  TYR n 
4 833  VAL n 
4 834  ASN n 
4 835  HIS n 
4 836  ARG n 
4 837  LEU n 
4 838  SER n 
4 839  HIS n 
4 840  ASP n 
4 841  LEU n 
4 842  SER n 
4 843  ASP n 
4 844  GLU n 
4 845  ALA n 
4 846  ARG n 
4 847  ALA n 
4 848  LEU n 
4 849  LEU n 
4 850  PRO n 
4 851  ASN n 
4 852  VAL n 
4 853  ILE n 
4 854  THR n 
4 855  LYS n 
4 856  GLU n 
4 857  VAL n 
4 858  SER n 
4 859  HIS n 
4 860  GLU n 
4 861  ILE n 
4 862  ILE n 
4 863  LYS n 
4 864  ASP n 
4 865  ARG n 
4 866  ARG n 
4 867  PHE n 
4 868  THR n 
4 869  SER n 
4 870  ASP n 
4 871  LYS n 
4 872  PHE n 
4 873  PHE n 
4 874  PHE n 
4 875  HIS n 
4 876  VAL n 
4 877  PRO n 
4 878  ILE n 
4 879  THR n 
4 880  LEU n 
4 881  ASN n 
4 882  TYR n 
4 883  GLN n 
4 884  ALA n 
4 885  ALA n 
4 886  ASN n 
4 887  SER n 
4 888  PRO n 
4 889  SER n 
4 890  LYS n 
4 891  PHE n 
4 892  ASN n 
4 893  GLN n 
4 894  ARG n 
4 895  VAL n 
4 896  ASN n 
4 897  ALA n 
4 898  TYR n 
4 899  LEU n 
4 900  LYS n 
4 901  GLU n 
4 902  HIS n 
4 903  PRO n 
4 904  GLU n 
4 905  THR n 
4 906  PRO n 
4 907  ILE n 
4 908  ILE n 
4 909  GLY n 
4 910  ILE n 
4 911  ASP n 
4 912  ARG n 
4 913  GLY n 
4 914  GLU n 
4 915  ARG n 
4 916  ASN n 
4 917  LEU n 
4 918  ILE n 
4 919  TYR n 
4 920  ILE n 
4 921  THR n 
4 922  VAL n 
4 923  ILE n 
4 924  ASP n 
4 925  SER n 
4 926  THR n 
4 927  GLY n 
4 928  LYS n 
4 929  ILE n 
4 930  LEU n 
4 931  GLU n 
4 932  GLN n 
4 933  ARG n 
4 934  SER n 
4 935  LEU n 
4 936  ASN n 
4 937  THR n 
4 938  ILE n 
4 939  GLN n 
4 940  GLN n 
4 941  PHE n 
4 942  ASP n 
4 943  TYR n 
4 944  GLN n 
4 945  LYS n 
4 946  LYS n 
4 947  LEU n 
4 948  ASP n 
4 949  ASN n 
4 950  ARG n 
4 951  GLU n 
4 952  LYS n 
4 953  GLU n 
4 954  ARG n 
4 955  VAL n 
4 956  ALA n 
4 957  ALA n 
4 958  ARG n 
4 959  GLN n 
4 960  ALA n 
4 961  TRP n 
4 962  SER n 
4 963  VAL n 
4 964  VAL n 
4 965  GLY n 
4 966  THR n 
4 967  ILE n 
4 968  LYS n 
4 969  ASP n 
4 970  LEU n 
4 971  LYS n 
4 972  GLN n 
4 973  GLY n 
4 974  TYR n 
4 975  LEU n 
4 976  SER n 
4 977  GLN n 
4 978  VAL n 
4 979  ILE n 
4 980  HIS n 
4 981  GLU n 
4 982  ILE n 
4 983  VAL n 
4 984  ASP n 
4 985  LEU n 
4 986  MET n 
4 987  ILE n 
4 988  HIS n 
4 989  TYR n 
4 990  GLN n 
4 991  ALA n 
4 992  VAL n 
4 993  VAL n 
4 994  VAL n 
4 995  LEU n 
4 996  GLU n 
4 997  ASN n 
4 998  LEU n 
4 999  ASN n 
4 1000 PHE n 
4 1001 GLY n 
4 1002 PHE n 
4 1003 LYS n 
4 1004 SER n 
4 1005 LYS n 
4 1006 ARG n 
4 1007 THR n 
4 1008 GLY n 
4 1009 ILE n 
4 1010 ALA n 
4 1011 GLU n 
4 1012 LYS n 
4 1013 ALA n 
4 1014 VAL n 
4 1015 TYR n 
4 1016 GLN n 
4 1017 GLN n 
4 1018 PHE n 
4 1019 GLU n 
4 1020 LYS n 
4 1021 MET n 
4 1022 LEU n 
4 1023 ILE n 
4 1024 ASP n 
4 1025 LYS n 
4 1026 LEU n 
4 1027 ASN n 
4 1028 CYS n 
4 1029 LEU n 
4 1030 VAL n 
4 1031 LEU n 
4 1032 LYS n 
4 1033 ASP n 
4 1034 TYR n 
4 1035 PRO n 
4 1036 ALA n 
4 1037 GLU n 
4 1038 LYS n 
4 1039 VAL n 
4 1040 GLY n 
4 1041 GLY n 
4 1042 VAL n 
4 1043 LEU n 
4 1044 ASN n 
4 1045 PRO n 
4 1046 TYR n 
4 1047 GLN n 
4 1048 LEU n 
4 1049 THR n 
4 1050 ASP n 
4 1051 GLN n 
4 1052 PHE n 
4 1053 THR n 
4 1054 SER n 
4 1055 PHE n 
4 1056 ALA n 
4 1057 LYS n 
4 1058 MET n 
4 1059 GLY n 
4 1060 THR n 
4 1061 GLN n 
4 1062 SER n 
4 1063 GLY n 
4 1064 PHE n 
4 1065 LEU n 
4 1066 PHE n 
4 1067 TYR n 
4 1068 VAL n 
4 1069 PRO n 
4 1070 ALA n 
4 1071 PRO n 
4 1072 TYR n 
4 1073 THR n 
4 1074 SER n 
4 1075 LYS n 
4 1076 ILE n 
4 1077 ASP n 
4 1078 PRO n 
4 1079 LEU n 
4 1080 THR n 
4 1081 GLY n 
4 1082 PHE n 
4 1083 VAL n 
4 1084 ASP n 
4 1085 PRO n 
4 1086 PHE n 
4 1087 VAL n 
4 1088 TRP n 
4 1089 LYS n 
4 1090 THR n 
4 1091 ILE n 
4 1092 LYS n 
4 1093 ASN n 
4 1094 HIS n 
4 1095 GLU n 
4 1096 SER n 
4 1097 ARG n 
4 1098 LYS n 
4 1099 HIS n 
4 1100 PHE n 
4 1101 LEU n 
4 1102 GLU n 
4 1103 GLY n 
4 1104 PHE n 
4 1105 ASP n 
4 1106 PHE n 
4 1107 LEU n 
4 1108 HIS n 
4 1109 TYR n 
4 1110 ASP n 
4 1111 VAL n 
4 1112 LYS n 
4 1113 THR n 
4 1114 GLY n 
4 1115 ASP n 
4 1116 PHE n 
4 1117 ILE n 
4 1118 LEU n 
4 1119 HIS n 
4 1120 PHE n 
4 1121 LYS n 
4 1122 MET n 
4 1123 ASN n 
4 1124 ARG n 
4 1125 ASN n 
4 1126 LEU n 
4 1127 SER n 
4 1128 PHE n 
4 1129 GLN n 
4 1130 ARG n 
4 1131 GLY n 
4 1132 LEU n 
4 1133 PRO n 
4 1134 GLY n 
4 1135 PHE n 
4 1136 MET n 
4 1137 PRO n 
4 1138 ALA n 
4 1139 TRP n 
4 1140 ASP n 
4 1141 ILE n 
4 1142 VAL n 
4 1143 PHE n 
4 1144 GLU n 
4 1145 LYS n 
4 1146 ASN n 
4 1147 GLU n 
4 1148 THR n 
4 1149 GLN n 
4 1150 PHE n 
4 1151 ASP n 
4 1152 ALA n 
4 1153 LYS n 
4 1154 GLY n 
4 1155 THR n 
4 1156 PRO n 
4 1157 PHE n 
4 1158 ILE n 
4 1159 ALA n 
4 1160 GLY n 
4 1161 LYS n 
4 1162 ARG n 
4 1163 ILE n 
4 1164 VAL n 
4 1165 PRO n 
4 1166 VAL n 
4 1167 ILE n 
4 1168 GLU n 
4 1169 ASN n 
4 1170 HIS n 
4 1171 ARG n 
4 1172 PHE n 
4 1173 THR n 
4 1174 GLY n 
4 1175 ARG n 
4 1176 TYR n 
4 1177 ARG n 
4 1178 ASP n 
4 1179 LEU n 
4 1180 TYR n 
4 1181 PRO n 
4 1182 ALA n 
4 1183 ASN n 
4 1184 GLU n 
4 1185 LEU n 
4 1186 ILE n 
4 1187 ALA n 
4 1188 LEU n 
4 1189 LEU n 
4 1190 GLU n 
4 1191 GLU n 
4 1192 LYS n 
4 1193 GLY n 
4 1194 ILE n 
4 1195 VAL n 
4 1196 PHE n 
4 1197 ARG n 
4 1198 ASP n 
4 1199 GLY n 
4 1200 SER n 
4 1201 ASN n 
4 1202 ILE n 
4 1203 LEU n 
4 1204 PRO n 
4 1205 LYS n 
4 1206 LEU n 
4 1207 LEU n 
4 1208 GLU n 
4 1209 ASN n 
4 1210 ASP n 
4 1211 ASP n 
4 1212 SER n 
4 1213 HIS n 
4 1214 ALA n 
4 1215 ILE n 
4 1216 ASP n 
4 1217 THR n 
4 1218 MET n 
4 1219 VAL n 
4 1220 ALA n 
4 1221 LEU n 
4 1222 ILE n 
4 1223 ARG n 
4 1224 SER n 
4 1225 VAL n 
4 1226 LEU n 
4 1227 GLN n 
4 1228 MET n 
4 1229 ARG n 
4 1230 ASN n 
4 1231 SER n 
4 1232 ASN n 
4 1233 ALA n 
4 1234 ALA n 
4 1235 THR n 
4 1236 GLY n 
4 1237 GLU n 
4 1238 ASP n 
4 1239 TYR n 
4 1240 ILE n 
4 1241 ASN n 
4 1242 SER n 
4 1243 PRO n 
4 1244 VAL n 
4 1245 ARG n 
4 1246 ASP n 
4 1247 LEU n 
4 1248 ASN n 
4 1249 GLY n 
4 1250 VAL n 
4 1251 CYS n 
4 1252 PHE n 
4 1253 ASP n 
4 1254 SER n 
4 1255 ARG n 
4 1256 PHE n 
4 1257 GLN n 
4 1258 ASN n 
4 1259 PRO n 
4 1260 GLU n 
4 1261 TRP n 
4 1262 PRO n 
4 1263 MET n 
4 1264 ASP n 
4 1265 ALA n 
4 1266 ASP n 
4 1267 ALA n 
4 1268 ASN n 
4 1269 GLY n 
4 1270 ALA n 
4 1271 TYR n 
4 1272 HIS n 
4 1273 ILE n 
4 1274 ALA n 
4 1275 LEU n 
4 1276 LYS n 
4 1277 GLY n 
4 1278 GLN n 
4 1279 LEU n 
4 1280 LEU n 
4 1281 LEU n 
4 1282 ASN n 
4 1283 HIS n 
4 1284 LEU n 
4 1285 LYS n 
4 1286 GLU n 
4 1287 SER n 
4 1288 LYS n 
4 1289 ASP n 
4 1290 LEU n 
4 1291 LYS n 
4 1292 LEU n 
4 1293 GLN n 
4 1294 ASN n 
4 1295 GLY n 
4 1296 ILE n 
4 1297 SER n 
4 1298 ASN n 
4 1299 GLN n 
4 1300 ASP n 
4 1301 TRP n 
4 1302 LEU n 
4 1303 ALA n 
4 1304 TYR n 
4 1305 ILE n 
4 1306 GLN n 
4 1307 GLU n 
4 1308 LEU n 
4 1309 ARG n 
4 1310 ASN n 
# 
_entity_src_gen.entity_id                          4 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   1310 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'cas12a, cpf1, HMPREF1246_0236' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Acidaminococcus sp. BV3L6' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1111120 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_pdbx_entity_src_syn.entity_id 
_pdbx_entity_src_syn.pdbx_src_id 
_pdbx_entity_src_syn.pdbx_alt_source_flag 
_pdbx_entity_src_syn.pdbx_beg_seq_num 
_pdbx_entity_src_syn.pdbx_end_seq_num 
_pdbx_entity_src_syn.organism_scientific 
_pdbx_entity_src_syn.organism_common_name 
_pdbx_entity_src_syn.ncbi_taxonomy_id 
_pdbx_entity_src_syn.details 
1 1 sample 1 31 'synthetic construct' ? 32630 ? 
2 1 sample 1 42 'synthetic construct' ? 32630 ? 
3 1 sample 1 31 'synthetic construct' ? 32630 ? 
# 
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 
2YR non-polymer         . 
;2'-deoxy-N-(2-sulfanylethyl)cytidine 5'-(dihydrogen phosphate)
;
? 'C11 H18 N3 O7 P S' 367.315 
A   'RNA linking'       y "ADENOSINE-5'-MONOPHOSPHATE"                                     ? 'C10 H14 N5 O7 P'   347.221 
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 
C   'RNA linking'       y "CYTIDINE-5'-MONOPHOSPHATE"                                      ? 'C9 H14 N3 O8 P'    323.197 
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 
G   'RNA linking'       y "GUANOSINE-5'-MONOPHOSPHATE"                                     ? 'C10 H14 N5 O8 P'   363.221 
GLN 'L-peptide linking' y GLUTAMINE                                                        ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                  ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                                          ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                                                        ? 'C6 H10 N3 O2 1'    156.162 
ILE 'L-peptide linking' y ISOLEUCINE                                                       ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                                                          ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                                                           ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                                                       ? 'C5 H11 N O2 S'     149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                    ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                                                          ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                                                           ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                                                        ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                       ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                                                         ? 'C9 H11 N O3'       181.189 
U   'RNA linking'       y "URIDINE-5'-MONOPHOSPHATE"                                       ? 'C9 H13 N2 O9 P'    324.181 
VAL 'L-peptide linking' y VALINE                                                           ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    DG  1    1    ?    ?   ?   C . n 
A 1 2    DT  2    2    2    DT  DT  C . n 
A 1 3    DA  3    3    3    DA  DA  C . n 
A 1 4    DG  4    4    4    DG  DG  C . n 
A 1 5    DT  5    5    5    DT  DT  C . n 
A 1 6    DG  6    6    6    DG  DG  C . n 
A 1 7    2YR 7    7    7    2YR 2YR C . n 
A 1 8    DT  8    8    8    DT  DT  C . n 
A 1 9    DT  9    9    9    DT  DT  C . n 
A 1 10   DT  10   10   10   DT  DT  C . n 
A 1 11   DG  11   11   11   DG  DG  C . n 
A 1 12   DT  12   12   12   DT  DT  C . n 
A 1 13   DC  13   13   13   DC  DC  C . n 
A 1 14   DG  14   14   14   DG  DG  C . n 
A 1 15   DT  15   15   15   DT  DT  C . n 
A 1 16   DC  16   16   16   DC  DC  C . n 
A 1 17   DT  17   17   17   DT  DT  C . n 
A 1 18   DC  18   18   18   DC  DC  C . n 
A 1 19   DA  19   19   19   DA  DA  C . n 
A 1 20   DT  20   20   20   DT  DT  C . n 
A 1 21   DC  21   21   21   DC  DC  C . n 
A 1 22   DT  22   22   22   DT  DT  C . n 
A 1 23   DG  23   23   ?    ?   ?   C . n 
A 1 24   DT  24   24   ?    ?   ?   C . n 
A 1 25   DA  25   25   ?    ?   ?   C . n 
A 1 26   DT  26   26   ?    ?   ?   C . n 
A 1 27   DG  27   27   ?    ?   ?   C . n 
A 1 28   DC  28   28   ?    ?   ?   C . n 
A 1 29   DG  29   29   ?    ?   ?   C . n 
A 1 30   DT  30   30   ?    ?   ?   C . n 
A 1 31   DC  31   31   ?    ?   ?   C . n 
B 2 1    U   1    1    ?    ?   ?   B . n 
B 2 2    U   2    2    ?    ?   ?   B . n 
B 2 3    U   3    3    ?    ?   ?   B . n 
B 2 4    A   4    4    4    A   A   B . n 
B 2 5    A   5    5    5    A   A   B . n 
B 2 6    U   6    6    6    U   U   B . n 
B 2 7    U   7    7    7    U   U   B . n 
B 2 8    U   8    8    8    U   U   B . n 
B 2 9    C   9    9    9    C   C   B . n 
B 2 10   U   10   10   10   U   U   B . n 
B 2 11   A   11   11   11   A   A   B . n 
B 2 12   C   12   12   12   C   C   B . n 
B 2 13   U   13   13   13   U   U   B . n 
B 2 14   C   14   14   14   C   C   B . n 
B 2 15   U   15   15   15   U   U   B . n 
B 2 16   U   16   16   16   U   U   B . n 
B 2 17   G   17   17   17   G   G   B . n 
B 2 18   U   18   18   18   U   U   B . n 
B 2 19   A   19   19   19   A   A   B . n 
B 2 20   G   20   20   20   G   G   B . n 
B 2 21   A   21   21   21   A   A   B . n 
B 2 22   U   22   22   22   U   U   B . n 
B 2 23   A   23   23   23   A   A   B . n 
B 2 24   G   24   24   24   G   G   B . n 
B 2 25   C   25   25   25   C   C   B . n 
B 2 26   A   26   26   26   A   A   B . n 
B 2 27   G   27   27   27   G   G   B . n 
B 2 28   A   28   28   28   A   A   B . n 
B 2 29   G   29   29   ?    ?   ?   B . n 
B 2 30   U   30   30   ?    ?   ?   B . n 
B 2 31   A   31   31   ?    ?   ?   B . n 
B 2 32   G   32   32   ?    ?   ?   B . n 
B 2 33   A   33   33   ?    ?   ?   B . n 
B 2 34   C   34   34   ?    ?   ?   B . n 
B 2 35   A   35   35   ?    ?   ?   B . n 
B 2 36   U   36   36   ?    ?   ?   B . n 
B 2 37   A   37   37   ?    ?   ?   B . n 
B 2 38   C   38   38   ?    ?   ?   B . n 
B 2 39   G   39   39   ?    ?   ?   B . n 
B 2 40   C   40   40   ?    ?   ?   B . n 
B 2 41   A   41   41   ?    ?   ?   B . n 
B 2 42   G   42   42   ?    ?   ?   B . n 
C 3 1    DG  1    1    ?    ?   ?   D . n 
C 3 2    DA  2    2    ?    ?   ?   D . n 
C 3 3    DC  3    3    ?    ?   ?   D . n 
C 3 4    DG  4    4    ?    ?   ?   D . n 
C 3 5    DC  5    5    ?    ?   ?   D . n 
C 3 6    DA  6    6    ?    ?   ?   D . n 
C 3 7    DT  7    7    ?    ?   ?   D . n 
C 3 8    DA  8    8    ?    ?   ?   D . n 
C 3 9    DC  9    9    ?    ?   ?   D . n 
C 3 10   DA  10   10   10   DA  DA  D . n 
C 3 11   DG  11   11   11   DG  DG  D . n 
C 3 12   DA  12   12   12   DA  DA  D . n 
C 3 13   DT  13   13   13   DT  DT  D . n 
C 3 14   DG  14   14   14   DG  DG  D . n 
C 3 15   DA  15   15   15   DA  DA  D . n 
C 3 16   DG  16   16   16   DG  DG  D . n 
C 3 17   DA  17   17   17   DA  DA  D . n 
C 3 18   DC  18   18   18   DC  DC  D . n 
C 3 19   DG  19   19   19   DG  DG  D . n 
C 3 20   DA  20   20   20   DA  DA  D . n 
C 3 21   DC  21   21   21   DC  DC  D . n 
C 3 22   DA  22   22   22   DA  DA  D . n 
C 3 23   DA  23   23   23   DA  DA  D . n 
C 3 24   DA  24   24   24   DA  DA  D . n 
C 3 25   DG  25   25   25   DG  DG  D . n 
C 3 26   DC  26   26   26   DC  DC  D . n 
C 3 27   DA  27   27   27   DA  DA  D . n 
C 3 28   DC  28   28   28   DC  DC  D . n 
C 3 29   DT  29   29   29   DT  DT  D . n 
C 3 30   DA  30   30   30   DA  DA  D . n 
C 3 31   DC  31   31   ?    ?   ?   D . n 
D 4 1    SER 1    -2   ?    ?   ?   A . n 
D 4 2    ASN 2    -1   ?    ?   ?   A . n 
D 4 3    ALA 3    0    ?    ?   ?   A . n 
D 4 4    MET 4    1    ?    ?   ?   A . n 
D 4 5    THR 5    2    2    THR THR A . n 
D 4 6    GLN 6    3    3    GLN GLN A . n 
D 4 7    PHE 7    4    4    PHE PHE A . n 
D 4 8    GLU 8    5    5    GLU GLU A . n 
D 4 9    GLY 9    6    6    GLY GLY A . n 
D 4 10   PHE 10   7    7    PHE PHE A . n 
D 4 11   THR 11   8    8    THR THR A . n 
D 4 12   ASN 12   9    9    ASN ASN A . n 
D 4 13   LEU 13   10   10   LEU LEU A . n 
D 4 14   TYR 14   11   11   TYR TYR A . n 
D 4 15   GLN 15   12   12   GLN GLN A . n 
D 4 16   VAL 16   13   13   VAL VAL A . n 
D 4 17   SER 17   14   14   SER SER A . n 
D 4 18   LYS 18   15   15   LYS LYS A . n 
D 4 19   THR 19   16   16   THR THR A . n 
D 4 20   LEU 20   17   17   LEU LEU A . n 
D 4 21   ARG 21   18   18   ARG ARG A . n 
D 4 22   PHE 22   19   19   PHE PHE A . n 
D 4 23   GLU 23   20   20   GLU GLU A . n 
D 4 24   LEU 24   21   21   LEU LEU A . n 
D 4 25   ILE 25   22   22   ILE ILE A . n 
D 4 26   PRO 26   23   23   PRO PRO A . n 
D 4 27   GLN 27   24   24   GLN GLN A . n 
D 4 28   GLY 28   25   25   GLY GLY A . n 
D 4 29   LYS 29   26   26   LYS LYS A . n 
D 4 30   THR 30   27   27   THR THR A . n 
D 4 31   LEU 31   28   28   LEU LEU A . n 
D 4 32   LYS 32   29   29   LYS LYS A . n 
D 4 33   HIS 33   30   30   HIS HIS A . n 
D 4 34   ILE 34   31   31   ILE ILE A . n 
D 4 35   GLN 35   32   32   GLN GLN A . n 
D 4 36   GLU 36   33   33   GLU GLU A . n 
D 4 37   GLN 37   34   34   GLN GLN A . n 
D 4 38   GLY 38   35   35   GLY GLY A . n 
D 4 39   PHE 39   36   36   PHE PHE A . n 
D 4 40   ILE 40   37   37   ILE ILE A . n 
D 4 41   GLU 41   38   38   GLU GLU A . n 
D 4 42   GLU 42   39   39   GLU GLU A . n 
D 4 43   ASP 43   40   40   ASP ASP A . n 
D 4 44   LYS 44   41   41   LYS LYS A . n 
D 4 45   ALA 45   42   42   ALA ALA A . n 
D 4 46   ARG 46   43   43   ARG ARG A . n 
D 4 47   ASN 47   44   44   ASN ASN A . n 
D 4 48   ASP 48   45   45   ASP ASP A . n 
D 4 49   HIS 49   46   46   HIS HIS A . n 
D 4 50   TYR 50   47   47   TYR TYR A . n 
D 4 51   LYS 51   48   48   LYS LYS A . n 
D 4 52   GLU 52   49   49   GLU GLU A . n 
D 4 53   LEU 53   50   50   LEU LEU A . n 
D 4 54   LYS 54   51   51   LYS LYS A . n 
D 4 55   PRO 55   52   52   PRO PRO A . n 
D 4 56   ILE 56   53   53   ILE ILE A . n 
D 4 57   ILE 57   54   54   ILE ILE A . n 
D 4 58   ASP 58   55   55   ASP ASP A . n 
D 4 59   ARG 59   56   56   ARG ARG A . n 
D 4 60   ILE 60   57   57   ILE ILE A . n 
D 4 61   TYR 61   58   58   TYR TYR A . n 
D 4 62   LYS 62   59   59   LYS LYS A . n 
D 4 63   THR 63   60   60   THR THR A . n 
D 4 64   TYR 64   61   61   TYR TYR A . n 
D 4 65   ALA 65   62   62   ALA ALA A . n 
D 4 66   ASP 66   63   63   ASP ASP A . n 
D 4 67   GLN 67   64   64   GLN GLN A . n 
D 4 68   CYS 68   65   65   CYS CYS A . n 
D 4 69   LEU 69   66   66   LEU LEU A . n 
D 4 70   GLN 70   67   67   GLN GLN A . n 
D 4 71   LEU 71   68   68   LEU LEU A . n 
D 4 72   VAL 72   69   69   VAL VAL A . n 
D 4 73   GLN 73   70   70   GLN GLN A . n 
D 4 74   LEU 74   71   71   LEU LEU A . n 
D 4 75   ASP 75   72   72   ASP ASP A . n 
D 4 76   TRP 76   73   73   TRP TRP A . n 
D 4 77   GLU 77   74   74   GLU GLU A . n 
D 4 78   ASN 78   75   75   ASN ASN A . n 
D 4 79   LEU 79   76   76   LEU LEU A . n 
D 4 80   SER 80   77   77   SER SER A . n 
D 4 81   ALA 81   78   78   ALA ALA A . n 
D 4 82   ALA 82   79   79   ALA ALA A . n 
D 4 83   ILE 83   80   80   ILE ILE A . n 
D 4 84   ASP 84   81   81   ASP ASP A . n 
D 4 85   SER 85   82   82   SER SER A . n 
D 4 86   TYR 86   83   83   TYR TYR A . n 
D 4 87   ARG 87   84   84   ARG ARG A . n 
D 4 88   LYS 88   85   85   LYS LYS A . n 
D 4 89   GLU 89   86   86   GLU GLU A . n 
D 4 90   LYS 90   87   87   LYS LYS A . n 
D 4 91   THR 91   88   88   THR THR A . n 
D 4 92   GLU 92   89   89   GLU GLU A . n 
D 4 93   GLU 93   90   90   GLU GLU A . n 
D 4 94   THR 94   91   91   THR THR A . n 
D 4 95   ARG 95   92   92   ARG ARG A . n 
D 4 96   ASN 96   93   93   ASN ASN A . n 
D 4 97   ALA 97   94   94   ALA ALA A . n 
D 4 98   LEU 98   95   95   LEU LEU A . n 
D 4 99   ILE 99   96   96   ILE ILE A . n 
D 4 100  GLU 100  97   97   GLU GLU A . n 
D 4 101  GLU 101  98   98   GLU GLU A . n 
D 4 102  GLN 102  99   99   GLN GLN A . n 
D 4 103  ALA 103  100  100  ALA ALA A . n 
D 4 104  THR 104  101  101  THR THR A . n 
D 4 105  TYR 105  102  102  TYR TYR A . n 
D 4 106  ARG 106  103  103  ARG ARG A . n 
D 4 107  ASN 107  104  104  ASN ASN A . n 
D 4 108  ALA 108  105  105  ALA ALA A . n 
D 4 109  ILE 109  106  106  ILE ILE A . n 
D 4 110  HIS 110  107  107  HIS HIS A . n 
D 4 111  ASP 111  108  108  ASP ASP A . n 
D 4 112  TYR 112  109  109  TYR TYR A . n 
D 4 113  PHE 113  110  110  PHE PHE A . n 
D 4 114  ILE 114  111  111  ILE ILE A . n 
D 4 115  GLY 115  112  112  GLY GLY A . n 
D 4 116  ARG 116  113  113  ARG ARG A . n 
D 4 117  THR 117  114  114  THR THR A . n 
D 4 118  ASP 118  115  115  ASP ASP A . n 
D 4 119  ASN 119  116  116  ASN ASN A . n 
D 4 120  LEU 120  117  117  LEU LEU A . n 
D 4 121  THR 121  118  118  THR THR A . n 
D 4 122  ASP 122  119  119  ASP ASP A . n 
D 4 123  ALA 123  120  120  ALA ALA A . n 
D 4 124  ILE 124  121  121  ILE ILE A . n 
D 4 125  ASN 125  122  122  ASN ASN A . n 
D 4 126  LYS 126  123  123  LYS LYS A . n 
D 4 127  ARG 127  124  124  ARG ARG A . n 
D 4 128  HIS 128  125  125  HIS HIS A . n 
D 4 129  ALA 129  126  126  ALA ALA A . n 
D 4 130  GLU 130  127  127  GLU GLU A . n 
D 4 131  ILE 131  128  128  ILE ILE A . n 
D 4 132  TYR 132  129  129  TYR TYR A . n 
D 4 133  LYS 133  130  130  LYS LYS A . n 
D 4 134  GLY 134  131  131  GLY GLY A . n 
D 4 135  LEU 135  132  132  LEU LEU A . n 
D 4 136  PHE 136  133  133  PHE PHE A . n 
D 4 137  LYS 137  134  134  LYS LYS A . n 
D 4 138  ALA 138  135  135  ALA ALA A . n 
D 4 139  GLU 139  136  136  GLU GLU A . n 
D 4 140  LEU 140  137  137  LEU LEU A . n 
D 4 141  PHE 141  138  138  PHE PHE A . n 
D 4 142  ASN 142  139  139  ASN ASN A . n 
D 4 143  GLY 143  140  140  GLY GLY A . n 
D 4 144  LYS 144  141  141  LYS LYS A . n 
D 4 145  VAL 145  142  142  VAL VAL A . n 
D 4 146  LEU 146  143  143  LEU LEU A . n 
D 4 147  LYS 147  144  144  LYS LYS A . n 
D 4 148  GLN 148  145  145  GLN GLN A . n 
D 4 149  LEU 149  146  146  LEU LEU A . n 
D 4 150  GLY 150  147  ?    ?   ?   A . n 
D 4 151  THR 151  148  ?    ?   ?   A . n 
D 4 152  VAL 152  149  ?    ?   ?   A . n 
D 4 153  THR 153  150  150  THR THR A . n 
D 4 154  THR 154  151  151  THR THR A . n 
D 4 155  THR 155  152  152  THR THR A . n 
D 4 156  GLU 156  153  153  GLU GLU A . n 
D 4 157  HIS 157  154  154  HIS HIS A . n 
D 4 158  GLU 158  155  155  GLU GLU A . n 
D 4 159  ASN 159  156  156  ASN ASN A . n 
D 4 160  ALA 160  157  157  ALA ALA A . n 
D 4 161  LEU 161  158  158  LEU LEU A . n 
D 4 162  LEU 162  159  159  LEU LEU A . n 
D 4 163  ARG 163  160  160  ARG ARG A . n 
D 4 164  SER 164  161  161  SER SER A . n 
D 4 165  PHE 165  162  162  PHE PHE A . n 
D 4 166  ASP 166  163  163  ASP ASP A . n 
D 4 167  LYS 167  164  164  LYS LYS A . n 
D 4 168  PHE 168  165  165  PHE PHE A . n 
D 4 169  THR 169  166  166  THR THR A . n 
D 4 170  THR 170  167  167  THR THR A . n 
D 4 171  TYR 171  168  168  TYR TYR A . n 
D 4 172  PHE 172  169  169  PHE PHE A . n 
D 4 173  SER 173  170  170  SER SER A . n 
D 4 174  GLY 174  171  171  GLY GLY A . n 
D 4 175  PHE 175  172  172  PHE PHE A . n 
D 4 176  TYR 176  173  173  TYR TYR A . n 
D 4 177  GLU 177  174  174  GLU GLU A . n 
D 4 178  ASN 178  175  175  ASN ASN A . n 
D 4 179  ARG 179  176  176  ARG ARG A . n 
D 4 180  LYS 180  177  177  LYS LYS A . n 
D 4 181  ASN 181  178  178  ASN ASN A . n 
D 4 182  VAL 182  179  179  VAL VAL A . n 
D 4 183  PHE 183  180  180  PHE PHE A . n 
D 4 184  SER 184  181  181  SER SER A . n 
D 4 185  ALA 185  182  182  ALA ALA A . n 
D 4 186  GLU 186  183  183  GLU GLU A . n 
D 4 187  ASP 187  184  184  ASP ASP A . n 
D 4 188  ILE 188  185  185  ILE ILE A . n 
D 4 189  SER 189  186  186  SER SER A . n 
D 4 190  THR 190  187  187  THR THR A . n 
D 4 191  ALA 191  188  188  ALA ALA A . n 
D 4 192  ILE 192  189  189  ILE ILE A . n 
D 4 193  PRO 193  190  190  PRO PRO A . n 
D 4 194  HIS 194  191  191  HIS HIS A . n 
D 4 195  ARG 195  192  192  ARG ARG A . n 
D 4 196  ILE 196  193  193  ILE ILE A . n 
D 4 197  VAL 197  194  194  VAL VAL A . n 
D 4 198  GLN 198  195  195  GLN GLN A . n 
D 4 199  ASP 199  196  196  ASP ASP A . n 
D 4 200  ASN 200  197  197  ASN ASN A . n 
D 4 201  PHE 201  198  198  PHE PHE A . n 
D 4 202  PRO 202  199  199  PRO PRO A . n 
D 4 203  LYS 203  200  200  LYS LYS A . n 
D 4 204  PHE 204  201  201  PHE PHE A . n 
D 4 205  LYS 205  202  202  LYS LYS A . n 
D 4 206  GLU 206  203  203  GLU GLU A . n 
D 4 207  ASN 207  204  204  ASN ASN A . n 
D 4 208  CYS 208  205  205  CYS CYS A . n 
D 4 209  HIS 209  206  206  HIS HIS A . n 
D 4 210  ILE 210  207  207  ILE ILE A . n 
D 4 211  PHE 211  208  208  PHE PHE A . n 
D 4 212  THR 212  209  209  THR THR A . n 
D 4 213  ARG 213  210  210  ARG ARG A . n 
D 4 214  LEU 214  211  211  LEU LEU A . n 
D 4 215  ILE 215  212  212  ILE ILE A . n 
D 4 216  THR 216  213  213  THR THR A . n 
D 4 217  ALA 217  214  214  ALA ALA A . n 
D 4 218  VAL 218  215  215  VAL VAL A . n 
D 4 219  PRO 219  216  216  PRO PRO A . n 
D 4 220  SER 220  217  217  SER SER A . n 
D 4 221  LEU 221  218  218  LEU LEU A . n 
D 4 222  ARG 222  219  219  ARG ARG A . n 
D 4 223  GLU 223  220  220  GLU GLU A . n 
D 4 224  HIS 224  221  221  HIS HIS A . n 
D 4 225  PHE 225  222  222  PHE PHE A . n 
D 4 226  GLU 226  223  223  GLU GLU A . n 
D 4 227  ASN 227  224  224  ASN ASN A . n 
D 4 228  VAL 228  225  225  VAL VAL A . n 
D 4 229  LYS 229  226  226  LYS LYS A . n 
D 4 230  LYS 230  227  227  LYS LYS A . n 
D 4 231  ALA 231  228  228  ALA ALA A . n 
D 4 232  ILE 232  229  229  ILE ILE A . n 
D 4 233  GLY 233  230  230  GLY GLY A . n 
D 4 234  ILE 234  231  231  ILE ILE A . n 
D 4 235  PHE 235  232  232  PHE PHE A . n 
D 4 236  VAL 236  233  233  VAL VAL A . n 
D 4 237  SER 237  234  234  SER SER A . n 
D 4 238  THR 238  235  235  THR THR A . n 
D 4 239  SER 239  236  236  SER SER A . n 
D 4 240  ILE 240  237  237  ILE ILE A . n 
D 4 241  GLU 241  238  238  GLU GLU A . n 
D 4 242  GLU 242  239  239  GLU GLU A . n 
D 4 243  VAL 243  240  240  VAL VAL A . n 
D 4 244  PHE 244  241  241  PHE PHE A . n 
D 4 245  SER 245  242  242  SER SER A . n 
D 4 246  PHE 246  243  243  PHE PHE A . n 
D 4 247  PRO 247  244  244  PRO PRO A . n 
D 4 248  PHE 248  245  245  PHE PHE A . n 
D 4 249  TYR 249  246  246  TYR TYR A . n 
D 4 250  ASN 250  247  247  ASN ASN A . n 
D 4 251  GLN 251  248  248  GLN GLN A . n 
D 4 252  LEU 252  249  249  LEU LEU A . n 
D 4 253  LEU 253  250  250  LEU LEU A . n 
D 4 254  THR 254  251  251  THR THR A . n 
D 4 255  GLN 255  252  252  GLN GLN A . n 
D 4 256  THR 256  253  253  THR THR A . n 
D 4 257  GLN 257  254  254  GLN GLN A . n 
D 4 258  ILE 258  255  255  ILE ILE A . n 
D 4 259  ASP 259  256  256  ASP ASP A . n 
D 4 260  LEU 260  257  257  LEU LEU A . n 
D 4 261  TYR 261  258  258  TYR TYR A . n 
D 4 262  ASN 262  259  259  ASN ASN A . n 
D 4 263  GLN 263  260  260  GLN GLN A . n 
D 4 264  LEU 264  261  261  LEU LEU A . n 
D 4 265  LEU 265  262  262  LEU LEU A . n 
D 4 266  GLY 266  263  263  GLY GLY A . n 
D 4 267  GLY 267  264  264  GLY GLY A . n 
D 4 268  ILE 268  265  ?    ?   ?   A . n 
D 4 269  SER 269  266  ?    ?   ?   A . n 
D 4 270  ARG 270  267  ?    ?   ?   A . n 
D 4 271  GLU 271  268  ?    ?   ?   A . n 
D 4 272  ALA 272  269  ?    ?   ?   A . n 
D 4 273  GLY 273  270  ?    ?   ?   A . n 
D 4 274  THR 274  271  ?    ?   ?   A . n 
D 4 275  GLU 275  272  ?    ?   ?   A . n 
D 4 276  LYS 276  273  ?    ?   ?   A . n 
D 4 277  ILE 277  274  ?    ?   ?   A . n 
D 4 278  LYS 278  275  ?    ?   ?   A . n 
D 4 279  GLY 279  276  ?    ?   ?   A . n 
D 4 280  LEU 280  277  ?    ?   ?   A . n 
D 4 281  ASN 281  278  ?    ?   ?   A . n 
D 4 282  GLU 282  279  ?    ?   ?   A . n 
D 4 283  VAL 283  280  ?    ?   ?   A . n 
D 4 284  LEU 284  281  ?    ?   ?   A . n 
D 4 285  ASN 285  282  ?    ?   ?   A . n 
D 4 286  LEU 286  283  ?    ?   ?   A . n 
D 4 287  ALA 287  284  ?    ?   ?   A . n 
D 4 288  ILE 288  285  ?    ?   ?   A . n 
D 4 289  GLN 289  286  ?    ?   ?   A . n 
D 4 290  LYS 290  287  ?    ?   ?   A . n 
D 4 291  ASN 291  288  ?    ?   ?   A . n 
D 4 292  ASP 292  289  ?    ?   ?   A . n 
D 4 293  GLU 293  290  ?    ?   ?   A . n 
D 4 294  THR 294  291  ?    ?   ?   A . n 
D 4 295  ALA 295  292  ?    ?   ?   A . n 
D 4 296  HIS 296  293  ?    ?   ?   A . n 
D 4 297  ILE 297  294  ?    ?   ?   A . n 
D 4 298  ILE 298  295  ?    ?   ?   A . n 
D 4 299  ALA 299  296  ?    ?   ?   A . n 
D 4 300  SER 300  297  ?    ?   ?   A . n 
D 4 301  LEU 301  298  ?    ?   ?   A . n 
D 4 302  PRO 302  299  ?    ?   ?   A . n 
D 4 303  HIS 303  300  ?    ?   ?   A . n 
D 4 304  ARG 304  301  ?    ?   ?   A . n 
D 4 305  PHE 305  302  ?    ?   ?   A . n 
D 4 306  ILE 306  303  ?    ?   ?   A . n 
D 4 307  PRO 307  304  ?    ?   ?   A . n 
D 4 308  LEU 308  305  ?    ?   ?   A . n 
D 4 309  PHE 309  306  ?    ?   ?   A . n 
D 4 310  LYS 310  307  ?    ?   ?   A . n 
D 4 311  GLN 311  308  ?    ?   ?   A . n 
D 4 312  ILE 312  309  ?    ?   ?   A . n 
D 4 313  LEU 313  310  ?    ?   ?   A . n 
D 4 314  SER 314  311  ?    ?   ?   A . n 
D 4 315  ASP 315  312  ?    ?   ?   A . n 
D 4 316  ARG 316  313  ?    ?   ?   A . n 
D 4 317  ASN 317  314  ?    ?   ?   A . n 
D 4 318  THR 318  315  ?    ?   ?   A . n 
D 4 319  LEU 319  316  ?    ?   ?   A . n 
D 4 320  SER 320  317  ?    ?   ?   A . n 
D 4 321  PHE 321  318  ?    ?   ?   A . n 
D 4 322  ILE 322  319  ?    ?   ?   A . n 
D 4 323  LEU 323  320  ?    ?   ?   A . n 
D 4 324  GLU 324  321  ?    ?   ?   A . n 
D 4 325  GLU 325  322  ?    ?   ?   A . n 
D 4 326  PHE 326  323  ?    ?   ?   A . n 
D 4 327  LYS 327  324  324  LYS LYS A . n 
D 4 328  SER 328  325  325  SER SER A . n 
D 4 329  ASP 329  326  326  ASP ASP A . n 
D 4 330  GLU 330  327  327  GLU GLU A . n 
D 4 331  GLU 331  328  328  GLU GLU A . n 
D 4 332  VAL 332  329  329  VAL VAL A . n 
D 4 333  ILE 333  330  330  ILE ILE A . n 
D 4 334  GLN 334  331  331  GLN GLN A . n 
D 4 335  SER 335  332  332  SER SER A . n 
D 4 336  PHE 336  333  333  PHE PHE A . n 
D 4 337  CYS 337  334  334  CYS CYS A . n 
D 4 338  LYS 338  335  335  LYS LYS A . n 
D 4 339  TYR 339  336  336  TYR TYR A . n 
D 4 340  LYS 340  337  337  LYS LYS A . n 
D 4 341  THR 341  338  338  THR THR A . n 
D 4 342  LEU 342  339  339  LEU LEU A . n 
D 4 343  LEU 343  340  340  LEU LEU A . n 
D 4 344  ARG 344  341  341  ARG ARG A . n 
D 4 345  ASN 345  342  342  ASN ASN A . n 
D 4 346  GLU 346  343  343  GLU GLU A . n 
D 4 347  ASN 347  344  344  ASN ASN A . n 
D 4 348  VAL 348  345  345  VAL VAL A . n 
D 4 349  LEU 349  346  346  LEU LEU A . n 
D 4 350  GLU 350  347  347  GLU GLU A . n 
D 4 351  THR 351  348  348  THR THR A . n 
D 4 352  ALA 352  349  349  ALA ALA A . n 
D 4 353  GLU 353  350  350  GLU GLU A . n 
D 4 354  ALA 354  351  351  ALA ALA A . n 
D 4 355  LEU 355  352  352  LEU LEU A . n 
D 4 356  PHE 356  353  353  PHE PHE A . n 
D 4 357  ASN 357  354  354  ASN ASN A . n 
D 4 358  GLU 358  355  355  GLU GLU A . n 
D 4 359  LEU 359  356  356  LEU LEU A . n 
D 4 360  ASN 360  357  357  ASN ASN A . n 
D 4 361  SER 361  358  358  SER SER A . n 
D 4 362  ILE 362  359  359  ILE ILE A . n 
D 4 363  ASP 363  360  360  ASP ASP A . n 
D 4 364  LEU 364  361  361  LEU LEU A . n 
D 4 365  THR 365  362  362  THR THR A . n 
D 4 366  HIS 366  363  363  HIS HIS A . n 
D 4 367  ILE 367  364  364  ILE ILE A . n 
D 4 368  PHE 368  365  365  PHE PHE A . n 
D 4 369  ILE 369  366  366  ILE ILE A . n 
D 4 370  SER 370  367  367  SER SER A . n 
D 4 371  HIS 371  368  368  HIS HIS A . n 
D 4 372  LYS 372  369  369  LYS LYS A . n 
D 4 373  LYS 373  370  370  LYS LYS A . n 
D 4 374  LEU 374  371  371  LEU LEU A . n 
D 4 375  GLU 375  372  372  GLU GLU A . n 
D 4 376  THR 376  373  373  THR THR A . n 
D 4 377  ILE 377  374  374  ILE ILE A . n 
D 4 378  SER 378  375  375  SER SER A . n 
D 4 379  SER 379  376  376  SER SER A . n 
D 4 380  ALA 380  377  377  ALA ALA A . n 
D 4 381  LEU 381  378  378  LEU LEU A . n 
D 4 382  CYS 382  379  379  CYS CYS A . n 
D 4 383  ASP 383  380  380  ASP ASP A . n 
D 4 384  HIS 384  381  381  HIS HIS A . n 
D 4 385  TRP 385  382  382  TRP TRP A . n 
D 4 386  ASP 386  383  383  ASP ASP A . n 
D 4 387  THR 387  384  384  THR THR A . n 
D 4 388  LEU 388  385  385  LEU LEU A . n 
D 4 389  ARG 389  386  386  ARG ARG A . n 
D 4 390  ASN 390  387  387  ASN ASN A . n 
D 4 391  ALA 391  388  388  ALA ALA A . n 
D 4 392  LEU 392  389  389  LEU LEU A . n 
D 4 393  TYR 393  390  390  TYR TYR A . n 
D 4 394  GLU 394  391  391  GLU GLU A . n 
D 4 395  ARG 395  392  392  ARG ARG A . n 
D 4 396  ARG 396  393  393  ARG ARG A . n 
D 4 397  ILE 397  394  394  ILE ILE A . n 
D 4 398  SER 398  395  395  SER SER A . n 
D 4 399  GLU 399  396  396  GLU GLU A . n 
D 4 400  LEU 400  397  397  LEU LEU A . n 
D 4 401  THR 401  398  398  THR THR A . n 
D 4 402  GLY 402  399  399  GLY GLY A . n 
D 4 403  LYS 403  400  400  LYS LYS A . n 
D 4 404  ILE 404  401  401  ILE ILE A . n 
D 4 405  THR 405  402  402  THR THR A . n 
D 4 406  LYS 406  403  403  LYS LYS A . n 
D 4 407  SER 407  404  404  SER SER A . n 
D 4 408  ALA 408  405  405  ALA ALA A . n 
D 4 409  LYS 409  406  406  LYS LYS A . n 
D 4 410  GLU 410  407  407  GLU GLU A . n 
D 4 411  LYS 411  408  408  LYS LYS A . n 
D 4 412  VAL 412  409  409  VAL VAL A . n 
D 4 413  GLN 413  410  410  GLN GLN A . n 
D 4 414  ARG 414  411  411  ARG ARG A . n 
D 4 415  SER 415  412  412  SER SER A . n 
D 4 416  LEU 416  413  413  LEU LEU A . n 
D 4 417  LYS 417  414  414  LYS LYS A . n 
D 4 418  HIS 418  415  415  HIS HIS A . n 
D 4 419  GLU 419  416  416  GLU GLU A . n 
D 4 420  ASP 420  417  417  ASP ASP A . n 
D 4 421  ILE 421  418  418  ILE ILE A . n 
D 4 422  ASN 422  419  419  ASN ASN A . n 
D 4 423  LEU 423  420  420  LEU LEU A . n 
D 4 424  GLN 424  421  421  GLN GLN A . n 
D 4 425  GLU 425  422  422  GLU GLU A . n 
D 4 426  ILE 426  423  423  ILE ILE A . n 
D 4 427  ILE 427  424  424  ILE ILE A . n 
D 4 428  SER 428  425  425  SER SER A . n 
D 4 429  ALA 429  426  426  ALA ALA A . n 
D 4 430  ALA 430  427  427  ALA ALA A . n 
D 4 431  GLY 431  428  428  GLY GLY A . n 
D 4 432  LYS 432  429  429  LYS LYS A . n 
D 4 433  GLU 433  430  430  GLU GLU A . n 
D 4 434  LEU 434  431  431  LEU LEU A . n 
D 4 435  SER 435  432  432  SER SER A . n 
D 4 436  GLU 436  433  433  GLU GLU A . n 
D 4 437  ALA 437  434  434  ALA ALA A . n 
D 4 438  PHE 438  435  435  PHE PHE A . n 
D 4 439  LYS 439  436  436  LYS LYS A . n 
D 4 440  GLN 440  437  437  GLN GLN A . n 
D 4 441  LYS 441  438  438  LYS LYS A . n 
D 4 442  THR 442  439  439  THR THR A . n 
D 4 443  SER 443  440  440  SER SER A . n 
D 4 444  GLU 444  441  441  GLU GLU A . n 
D 4 445  ILE 445  442  442  ILE ILE A . n 
D 4 446  LEU 446  443  443  LEU LEU A . n 
D 4 447  SER 447  444  444  SER SER A . n 
D 4 448  HIS 448  445  445  HIS HIS A . n 
D 4 449  ALA 449  446  446  ALA ALA A . n 
D 4 450  HIS 450  447  447  HIS HIS A . n 
D 4 451  ALA 451  448  448  ALA ALA A . n 
D 4 452  ALA 452  449  449  ALA ALA A . n 
D 4 453  LEU 453  450  450  LEU LEU A . n 
D 4 454  ASP 454  451  451  ASP ASP A . n 
D 4 455  GLN 455  452  452  GLN GLN A . n 
D 4 456  PRO 456  453  453  PRO PRO A . n 
D 4 457  LEU 457  454  454  LEU LEU A . n 
D 4 458  PRO 458  455  455  PRO PRO A . n 
D 4 459  THR 459  456  456  THR THR A . n 
D 4 460  THR 460  457  457  THR THR A . n 
D 4 461  LEU 461  458  458  LEU LEU A . n 
D 4 462  LYS 462  459  459  LYS LYS A . n 
D 4 463  LYS 463  460  460  LYS LYS A . n 
D 4 464  GLN 464  461  461  GLN GLN A . n 
D 4 465  GLU 465  462  462  GLU GLU A . n 
D 4 466  GLU 466  463  463  GLU GLU A . n 
D 4 467  LYS 467  464  464  LYS LYS A . n 
D 4 468  GLU 468  465  465  GLU GLU A . n 
D 4 469  ILE 469  466  466  ILE ILE A . n 
D 4 470  LEU 470  467  467  LEU LEU A . n 
D 4 471  LYS 471  468  468  LYS LYS A . n 
D 4 472  SER 472  469  469  SER SER A . n 
D 4 473  GLN 473  470  470  GLN GLN A . n 
D 4 474  LEU 474  471  471  LEU LEU A . n 
D 4 475  ASP 475  472  472  ASP ASP A . n 
D 4 476  SER 476  473  473  SER SER A . n 
D 4 477  LEU 477  474  474  LEU LEU A . n 
D 4 478  LEU 478  475  475  LEU LEU A . n 
D 4 479  GLY 479  476  476  GLY GLY A . n 
D 4 480  LEU 480  477  477  LEU LEU A . n 
D 4 481  TYR 481  478  478  TYR TYR A . n 
D 4 482  HIS 482  479  479  HIS HIS A . n 
D 4 483  LEU 483  480  480  LEU LEU A . n 
D 4 484  LEU 484  481  481  LEU LEU A . n 
D 4 485  ASP 485  482  482  ASP ASP A . n 
D 4 486  TRP 486  483  483  TRP TRP A . n 
D 4 487  PHE 487  484  484  PHE PHE A . n 
D 4 488  ALA 488  485  485  ALA ALA A . n 
D 4 489  VAL 489  486  486  VAL VAL A . n 
D 4 490  ASP 490  487  487  ASP ASP A . n 
D 4 491  GLU 491  488  488  GLU GLU A . n 
D 4 492  SER 492  489  489  SER SER A . n 
D 4 493  ASN 493  490  490  ASN ASN A . n 
D 4 494  GLU 494  491  491  GLU GLU A . n 
D 4 495  VAL 495  492  492  VAL VAL A . n 
D 4 496  ASP 496  493  493  ASP ASP A . n 
D 4 497  PRO 497  494  494  PRO PRO A . n 
D 4 498  GLU 498  495  495  GLU GLU A . n 
D 4 499  PHE 499  496  496  PHE PHE A . n 
D 4 500  SER 500  497  497  SER SER A . n 
D 4 501  ALA 501  498  498  ALA ALA A . n 
D 4 502  ARG 502  499  499  ARG ARG A . n 
D 4 503  LEU 503  500  500  LEU LEU A . n 
D 4 504  THR 504  501  501  THR THR A . n 
D 4 505  GLY 505  502  502  GLY GLY A . n 
D 4 506  ILE 506  503  503  ILE ILE A . n 
D 4 507  LYS 507  504  504  LYS LYS A . n 
D 4 508  LEU 508  505  505  LEU LEU A . n 
D 4 509  GLU 509  506  506  GLU GLU A . n 
D 4 510  MET 510  507  507  MET MET A . n 
D 4 511  GLU 511  508  508  GLU GLU A . n 
D 4 512  PRO 512  509  509  PRO PRO A . n 
D 4 513  SER 513  510  510  SER SER A . n 
D 4 514  LEU 514  511  511  LEU LEU A . n 
D 4 515  SER 515  512  512  SER SER A . n 
D 4 516  PHE 516  513  513  PHE PHE A . n 
D 4 517  TYR 517  514  514  TYR TYR A . n 
D 4 518  ASN 518  515  515  ASN ASN A . n 
D 4 519  LYS 519  516  516  LYS LYS A . n 
D 4 520  ALA 520  517  517  ALA ALA A . n 
D 4 521  ARG 521  518  518  ARG ARG A . n 
D 4 522  ASN 522  519  519  ASN ASN A . n 
D 4 523  TYR 523  520  520  TYR TYR A . n 
D 4 524  ALA 524  521  521  ALA ALA A . n 
D 4 525  THR 525  522  522  THR THR A . n 
D 4 526  LYS 526  523  523  LYS LYS A . n 
D 4 527  LYS 527  524  524  LYS LYS A . n 
D 4 528  PRO 528  525  525  PRO PRO A . n 
D 4 529  TYR 529  526  526  TYR TYR A . n 
D 4 530  SER 530  527  527  SER SER A . n 
D 4 531  VAL 531  528  528  VAL VAL A . n 
D 4 532  GLU 532  529  529  GLU GLU A . n 
D 4 533  LYS 533  530  530  LYS LYS A . n 
D 4 534  PHE 534  531  531  PHE PHE A . n 
D 4 535  LYS 535  532  532  LYS LYS A . n 
D 4 536  LEU 536  533  533  LEU LEU A . n 
D 4 537  ASN 537  534  534  ASN ASN A . n 
D 4 538  PHE 538  535  535  PHE PHE A . n 
D 4 539  GLN 539  536  536  GLN GLN A . n 
D 4 540  MET 540  537  537  MET MET A . n 
D 4 541  PRO 541  538  538  PRO PRO A . n 
D 4 542  THR 542  539  539  THR THR A . n 
D 4 543  LEU 543  540  540  LEU LEU A . n 
D 4 544  ALA 544  541  541  ALA ALA A . n 
D 4 545  SER 545  542  542  SER SER A . n 
D 4 546  GLY 546  543  543  GLY GLY A . n 
D 4 547  TRP 547  544  544  TRP TRP A . n 
D 4 548  ASP 548  545  545  ASP ASP A . n 
D 4 549  VAL 549  546  546  VAL VAL A . n 
D 4 550  ASN 550  547  547  ASN ASN A . n 
D 4 551  LYS 551  548  548  LYS LYS A . n 
D 4 552  GLU 552  549  549  GLU GLU A . n 
D 4 553  LYS 553  550  550  LYS LYS A . n 
D 4 554  CYS 554  551  551  CYS CYS A . n 
D 4 555  ASN 555  552  552  ASN ASN A . n 
D 4 556  GLY 556  553  553  GLY GLY A . n 
D 4 557  ALA 557  554  554  ALA ALA A . n 
D 4 558  ILE 558  555  555  ILE ILE A . n 
D 4 559  LEU 559  556  556  LEU LEU A . n 
D 4 560  PHE 560  557  557  PHE PHE A . n 
D 4 561  VAL 561  558  558  VAL VAL A . n 
D 4 562  LYS 562  559  559  LYS LYS A . n 
D 4 563  ASN 563  560  560  ASN ASN A . n 
D 4 564  GLY 564  561  561  GLY GLY A . n 
D 4 565  LEU 565  562  562  LEU LEU A . n 
D 4 566  TYR 566  563  563  TYR TYR A . n 
D 4 567  TYR 567  564  564  TYR TYR A . n 
D 4 568  LEU 568  565  565  LEU LEU A . n 
D 4 569  GLY 569  566  566  GLY GLY A . n 
D 4 570  ILE 570  567  567  ILE ILE A . n 
D 4 571  MET 571  568  568  MET MET A . n 
D 4 572  PRO 572  569  569  PRO PRO A . n 
D 4 573  LYS 573  570  570  LYS LYS A . n 
D 4 574  GLN 574  571  571  GLN GLN A . n 
D 4 575  LYS 575  572  572  LYS LYS A . n 
D 4 576  GLY 576  573  573  GLY GLY A . n 
D 4 577  ARG 577  574  574  ARG ARG A . n 
D 4 578  TYR 578  575  575  TYR TYR A . n 
D 4 579  LYS 579  576  576  LYS LYS A . n 
D 4 580  ALA 580  577  577  ALA ALA A . n 
D 4 581  LEU 581  578  578  LEU LEU A . n 
D 4 582  SER 582  579  579  SER SER A . n 
D 4 583  PHE 583  580  580  PHE PHE A . n 
D 4 584  GLU 584  581  581  GLU GLU A . n 
D 4 585  PRO 585  582  582  PRO PRO A . n 
D 4 586  THR 586  583  583  THR THR A . n 
D 4 587  GLU 587  584  584  GLU GLU A . n 
D 4 588  LYS 588  585  585  LYS LYS A . n 
D 4 589  THR 589  586  586  THR THR A . n 
D 4 590  SER 590  587  587  SER SER A . n 
D 4 591  GLU 591  588  588  GLU GLU A . n 
D 4 592  GLY 592  589  589  GLY GLY A . n 
D 4 593  PHE 593  590  590  PHE PHE A . n 
D 4 594  ASP 594  591  591  ASP ASP A . n 
D 4 595  LYS 595  592  592  LYS LYS A . n 
D 4 596  MET 596  593  593  MET MET A . n 
D 4 597  TYR 597  594  594  TYR TYR A . n 
D 4 598  TYR 598  595  595  TYR TYR A . n 
D 4 599  ASP 599  596  596  ASP ASP A . n 
D 4 600  TYR 600  597  597  TYR TYR A . n 
D 4 601  PHE 601  598  598  PHE PHE A . n 
D 4 602  PRO 602  599  599  PRO PRO A . n 
D 4 603  ASP 603  600  600  ASP ASP A . n 
D 4 604  ALA 604  601  601  ALA ALA A . n 
D 4 605  ALA 605  602  602  ALA ALA A . n 
D 4 606  LYS 606  603  603  LYS LYS A . n 
D 4 607  MET 607  604  604  MET MET A . n 
D 4 608  ILE 608  605  605  ILE ILE A . n 
D 4 609  PRO 609  606  606  PRO PRO A . n 
D 4 610  LYS 610  607  607  LYS LYS A . n 
D 4 611  CYS 611  608  608  CYS CYS A . n 
D 4 612  SER 612  609  609  SER SER A . n 
D 4 613  THR 613  610  610  THR THR A . n 
D 4 614  GLN 614  611  611  GLN GLN A . n 
D 4 615  LEU 615  612  612  LEU LEU A . n 
D 4 616  LYS 616  613  613  LYS LYS A . n 
D 4 617  ALA 617  614  614  ALA ALA A . n 
D 4 618  VAL 618  615  615  VAL VAL A . n 
D 4 619  THR 619  616  616  THR THR A . n 
D 4 620  ALA 620  617  617  ALA ALA A . n 
D 4 621  HIS 621  618  618  HIS HIS A . n 
D 4 622  PHE 622  619  619  PHE PHE A . n 
D 4 623  GLN 623  620  620  GLN GLN A . n 
D 4 624  THR 624  621  621  THR THR A . n 
D 4 625  HIS 625  622  622  HIS HIS A . n 
D 4 626  THR 626  623  623  THR THR A . n 
D 4 627  THR 627  624  624  THR THR A . n 
D 4 628  PRO 628  625  625  PRO PRO A . n 
D 4 629  ILE 629  626  626  ILE ILE A . n 
D 4 630  LEU 630  627  627  LEU LEU A . n 
D 4 631  LEU 631  628  628  LEU LEU A . n 
D 4 632  SER 632  629  629  SER SER A . n 
D 4 633  ASN 633  630  630  ASN ASN A . n 
D 4 634  ASN 634  631  631  ASN ASN A . n 
D 4 635  PHE 635  632  632  PHE PHE A . n 
D 4 636  ILE 636  633  633  ILE ILE A . n 
D 4 637  GLU 637  634  634  GLU GLU A . n 
D 4 638  PRO 638  635  635  PRO PRO A . n 
D 4 639  LEU 639  636  636  LEU LEU A . n 
D 4 640  GLU 640  637  637  GLU GLU A . n 
D 4 641  ILE 641  638  638  ILE ILE A . n 
D 4 642  THR 642  639  639  THR THR A . n 
D 4 643  LYS 643  640  640  LYS LYS A . n 
D 4 644  GLU 644  641  641  GLU GLU A . n 
D 4 645  ILE 645  642  642  ILE ILE A . n 
D 4 646  TYR 646  643  643  TYR TYR A . n 
D 4 647  ASP 647  644  644  ASP ASP A . n 
D 4 648  LEU 648  645  645  LEU LEU A . n 
D 4 649  ASN 649  646  646  ASN ASN A . n 
D 4 650  ASN 650  647  647  ASN ASN A . n 
D 4 651  PRO 651  648  648  PRO PRO A . n 
D 4 652  GLU 652  649  649  GLU GLU A . n 
D 4 653  LYS 653  650  650  LYS LYS A . n 
D 4 654  GLU 654  651  651  GLU GLU A . n 
D 4 655  PRO 655  652  652  PRO PRO A . n 
D 4 656  LYS 656  653  653  LYS LYS A . n 
D 4 657  LYS 657  654  654  LYS LYS A . n 
D 4 658  PHE 658  655  655  PHE PHE A . n 
D 4 659  GLN 659  656  656  GLN GLN A . n 
D 4 660  THR 660  657  657  THR THR A . n 
D 4 661  ALA 661  658  658  ALA ALA A . n 
D 4 662  TYR 662  659  659  TYR TYR A . n 
D 4 663  ALA 663  660  660  ALA ALA A . n 
D 4 664  LYS 664  661  661  LYS LYS A . n 
D 4 665  LYS 665  662  662  LYS LYS A . n 
D 4 666  THR 666  663  663  THR THR A . n 
D 4 667  GLY 667  664  664  GLY GLY A . n 
D 4 668  ASP 668  665  665  ASP ASP A . n 
D 4 669  GLN 669  666  666  GLN GLN A . n 
D 4 670  LYS 670  667  667  LYS LYS A . n 
D 4 671  GLY 671  668  668  GLY GLY A . n 
D 4 672  TYR 672  669  669  TYR TYR A . n 
D 4 673  ARG 673  670  670  ARG ARG A . n 
D 4 674  GLU 674  671  671  GLU GLU A . n 
D 4 675  ALA 675  672  672  ALA ALA A . n 
D 4 676  LEU 676  673  673  LEU LEU A . n 
D 4 677  CYS 677  674  674  CYS CYS A . n 
D 4 678  LYS 678  675  675  LYS LYS A . n 
D 4 679  TRP 679  676  676  TRP TRP A . n 
D 4 680  ILE 680  677  677  ILE ILE A . n 
D 4 681  ASP 681  678  678  ASP ASP A . n 
D 4 682  PHE 682  679  679  PHE PHE A . n 
D 4 683  THR 683  680  680  THR THR A . n 
D 4 684  ARG 684  681  681  ARG ARG A . n 
D 4 685  ASP 685  682  682  ASP ASP A . n 
D 4 686  PHE 686  683  683  PHE PHE A . n 
D 4 687  LEU 687  684  684  LEU LEU A . n 
D 4 688  SER 688  685  685  SER SER A . n 
D 4 689  LYS 689  686  686  LYS LYS A . n 
D 4 690  TYR 690  687  687  TYR TYR A . n 
D 4 691  THR 691  688  688  THR THR A . n 
D 4 692  LYS 692  689  689  LYS LYS A . n 
D 4 693  THR 693  690  690  THR THR A . n 
D 4 694  THR 694  691  691  THR THR A . n 
D 4 695  SER 695  692  692  SER SER A . n 
D 4 696  ILE 696  693  693  ILE ILE A . n 
D 4 697  ASP 697  694  694  ASP ASP A . n 
D 4 698  LEU 698  695  695  LEU LEU A . n 
D 4 699  SER 699  696  696  SER SER A . n 
D 4 700  SER 700  697  697  SER SER A . n 
D 4 701  LEU 701  698  698  LEU LEU A . n 
D 4 702  ARG 702  699  699  ARG ARG A . n 
D 4 703  PRO 703  700  700  PRO PRO A . n 
D 4 704  SER 704  701  701  SER SER A . n 
D 4 705  SER 705  702  702  SER SER A . n 
D 4 706  GLN 706  703  703  GLN GLN A . n 
D 4 707  TYR 707  704  704  TYR TYR A . n 
D 4 708  LYS 708  705  705  LYS LYS A . n 
D 4 709  ASP 709  706  706  ASP ASP A . n 
D 4 710  LEU 710  707  707  LEU LEU A . n 
D 4 711  GLY 711  708  708  GLY GLY A . n 
D 4 712  GLU 712  709  709  GLU GLU A . n 
D 4 713  TYR 713  710  710  TYR TYR A . n 
D 4 714  TYR 714  711  711  TYR TYR A . n 
D 4 715  ALA 715  712  712  ALA ALA A . n 
D 4 716  GLU 716  713  713  GLU GLU A . n 
D 4 717  LEU 717  714  714  LEU LEU A . n 
D 4 718  ASN 718  715  715  ASN ASN A . n 
D 4 719  PRO 719  716  716  PRO PRO A . n 
D 4 720  LEU 720  717  717  LEU LEU A . n 
D 4 721  LEU 721  718  718  LEU LEU A . n 
D 4 722  TYR 722  719  719  TYR TYR A . n 
D 4 723  HIS 723  720  720  HIS HIS A . n 
D 4 724  ILE 724  721  721  ILE ILE A . n 
D 4 725  SER 725  722  722  SER SER A . n 
D 4 726  PHE 726  723  723  PHE PHE A . n 
D 4 727  GLN 727  724  724  GLN GLN A . n 
D 4 728  ARG 728  725  725  ARG ARG A . n 
D 4 729  ILE 729  726  726  ILE ILE A . n 
D 4 730  ALA 730  727  727  ALA ALA A . n 
D 4 731  GLU 731  728  728  GLU GLU A . n 
D 4 732  LYS 732  729  729  LYS LYS A . n 
D 4 733  GLU 733  730  730  GLU GLU A . n 
D 4 734  ILE 734  731  731  ILE ILE A . n 
D 4 735  MET 735  732  732  MET MET A . n 
D 4 736  ASP 736  733  733  ASP ASP A . n 
D 4 737  ALA 737  734  734  ALA ALA A . n 
D 4 738  VAL 738  735  735  VAL VAL A . n 
D 4 739  GLU 739  736  736  GLU GLU A . n 
D 4 740  THR 740  737  737  THR THR A . n 
D 4 741  GLY 741  738  738  GLY GLY A . n 
D 4 742  LYS 742  739  739  LYS LYS A . n 
D 4 743  LEU 743  740  740  LEU LEU A . n 
D 4 744  TYR 744  741  741  TYR TYR A . n 
D 4 745  LEU 745  742  742  LEU LEU A . n 
D 4 746  PHE 746  743  743  PHE PHE A . n 
D 4 747  GLN 747  744  744  GLN GLN A . n 
D 4 748  ILE 748  745  745  ILE ILE A . n 
D 4 749  TYR 749  746  746  TYR TYR A . n 
D 4 750  ASN 750  747  747  ASN ASN A . n 
D 4 751  LYS 751  748  748  LYS LYS A . n 
D 4 752  ASP 752  749  749  ASP ASP A . n 
D 4 753  PHE 753  750  750  PHE PHE A . n 
D 4 754  ALA 754  751  751  ALA ALA A . n 
D 4 755  LYS 755  752  752  LYS LYS A . n 
D 4 756  GLY 756  753  753  GLY GLY A . n 
D 4 757  HIS 757  754  754  HIS HIS A . n 
D 4 758  HIS 758  755  755  HIS HIS A . n 
D 4 759  GLY 759  756  756  GLY GLY A . n 
D 4 760  LYS 760  757  757  LYS LYS A . n 
D 4 761  PRO 761  758  758  PRO PRO A . n 
D 4 762  ASN 762  759  759  ASN ASN A . n 
D 4 763  LEU 763  760  760  LEU LEU A . n 
D 4 764  HIS 764  761  761  HIS HIS A . n 
D 4 765  THR 765  762  762  THR THR A . n 
D 4 766  LEU 766  763  763  LEU LEU A . n 
D 4 767  TYR 767  764  764  TYR TYR A . n 
D 4 768  TRP 768  765  765  TRP TRP A . n 
D 4 769  THR 769  766  766  THR THR A . n 
D 4 770  GLY 770  767  767  GLY GLY A . n 
D 4 771  LEU 771  768  768  LEU LEU A . n 
D 4 772  PHE 772  769  769  PHE PHE A . n 
D 4 773  SER 773  770  770  SER SER A . n 
D 4 774  PRO 774  771  771  PRO PRO A . n 
D 4 775  GLU 775  772  772  GLU GLU A . n 
D 4 776  ASN 776  773  773  ASN ASN A . n 
D 4 777  LEU 777  774  774  LEU LEU A . n 
D 4 778  ALA 778  775  775  ALA ALA A . n 
D 4 779  LYS 779  776  776  LYS LYS A . n 
D 4 780  THR 780  777  777  THR THR A . n 
D 4 781  SER 781  778  778  SER SER A . n 
D 4 782  ILE 782  779  779  ILE ILE A . n 
D 4 783  LYS 783  780  780  LYS LYS A . n 
D 4 784  LEU 784  781  781  LEU LEU A . n 
D 4 785  ASN 785  782  782  ASN ASN A . n 
D 4 786  GLY 786  783  783  GLY GLY A . n 
D 4 787  GLN 787  784  784  GLN GLN A . n 
D 4 788  ALA 788  785  785  ALA ALA A . n 
D 4 789  GLU 789  786  786  GLU GLU A . n 
D 4 790  LEU 790  787  787  LEU LEU A . n 
D 4 791  PHE 791  788  788  PHE PHE A . n 
D 4 792  TYR 792  789  789  TYR TYR A . n 
D 4 793  ARG 793  790  790  ARG ARG A . n 
D 4 794  PRO 794  791  791  PRO PRO A . n 
D 4 795  LYS 795  792  792  LYS LYS A . n 
D 4 796  SER 796  793  793  SER SER A . n 
D 4 797  ARG 797  794  794  ARG ARG A . n 
D 4 798  MET 798  795  795  MET MET A . n 
D 4 799  LYS 799  796  796  LYS LYS A . n 
D 4 800  ARG 800  797  797  ARG ARG A . n 
D 4 801  MET 801  798  798  MET MET A . n 
D 4 802  ALA 802  799  799  ALA ALA A . n 
D 4 803  HIS 803  800  800  HIS HIS A . n 
D 4 804  ARG 804  801  801  ARG ARG A . n 
D 4 805  LEU 805  802  802  LEU LEU A . n 
D 4 806  GLY 806  803  803  GLY GLY A . n 
D 4 807  GLU 807  804  804  GLU GLU A . n 
D 4 808  LYS 808  805  805  LYS LYS A . n 
D 4 809  MET 809  806  806  MET MET A . n 
D 4 810  LEU 810  807  807  LEU LEU A . n 
D 4 811  ASN 811  808  808  ASN ASN A . n 
D 4 812  LYS 812  809  809  LYS LYS A . n 
D 4 813  LYS 813  810  810  LYS LYS A . n 
D 4 814  LEU 814  811  811  LEU LEU A . n 
D 4 815  LYS 815  812  812  LYS LYS A . n 
D 4 816  ASP 816  813  813  ASP ASP A . n 
D 4 817  GLN 817  814  814  GLN GLN A . n 
D 4 818  LYS 818  815  815  LYS LYS A . n 
D 4 819  THR 819  816  816  THR THR A . n 
D 4 820  PRO 820  817  817  PRO PRO A . n 
D 4 821  ILE 821  818  818  ILE ILE A . n 
D 4 822  PRO 822  819  819  PRO PRO A . n 
D 4 823  ASP 823  820  820  ASP ASP A . n 
D 4 824  THR 824  821  821  THR THR A . n 
D 4 825  LEU 825  822  822  LEU LEU A . n 
D 4 826  TYR 826  823  823  TYR TYR A . n 
D 4 827  GLN 827  824  824  GLN GLN A . n 
D 4 828  GLU 828  825  825  GLU GLU A . n 
D 4 829  LEU 829  826  826  LEU LEU A . n 
D 4 830  TYR 830  827  827  TYR TYR A . n 
D 4 831  ASP 831  828  828  ASP ASP A . n 
D 4 832  TYR 832  829  829  TYR TYR A . n 
D 4 833  VAL 833  830  830  VAL VAL A . n 
D 4 834  ASN 834  831  831  ASN ASN A . n 
D 4 835  HIS 835  832  832  HIS HIS A . n 
D 4 836  ARG 836  833  833  ARG ARG A . n 
D 4 837  LEU 837  834  834  LEU LEU A . n 
D 4 838  SER 838  835  835  SER SER A . n 
D 4 839  HIS 839  836  836  HIS HIS A . n 
D 4 840  ASP 840  837  837  ASP ASP A . n 
D 4 841  LEU 841  838  838  LEU LEU A . n 
D 4 842  SER 842  839  839  SER SER A . n 
D 4 843  ASP 843  840  840  ASP ASP A . n 
D 4 844  GLU 844  841  841  GLU GLU A . n 
D 4 845  ALA 845  842  842  ALA ALA A . n 
D 4 846  ARG 846  843  843  ARG ARG A . n 
D 4 847  ALA 847  844  844  ALA ALA A . n 
D 4 848  LEU 848  845  845  LEU LEU A . n 
D 4 849  LEU 849  846  846  LEU LEU A . n 
D 4 850  PRO 850  847  847  PRO PRO A . n 
D 4 851  ASN 851  848  848  ASN ASN A . n 
D 4 852  VAL 852  849  849  VAL VAL A . n 
D 4 853  ILE 853  850  850  ILE ILE A . n 
D 4 854  THR 854  851  851  THR THR A . n 
D 4 855  LYS 855  852  852  LYS LYS A . n 
D 4 856  GLU 856  853  853  GLU GLU A . n 
D 4 857  VAL 857  854  854  VAL VAL A . n 
D 4 858  SER 858  855  855  SER SER A . n 
D 4 859  HIS 859  856  856  HIS HIS A . n 
D 4 860  GLU 860  857  857  GLU GLU A . n 
D 4 861  ILE 861  858  858  ILE ILE A . n 
D 4 862  ILE 862  859  859  ILE ILE A . n 
D 4 863  LYS 863  860  860  LYS LYS A . n 
D 4 864  ASP 864  861  861  ASP ASP A . n 
D 4 865  ARG 865  862  862  ARG ARG A . n 
D 4 866  ARG 866  863  863  ARG ARG A . n 
D 4 867  PHE 867  864  864  PHE PHE A . n 
D 4 868  THR 868  865  865  THR THR A . n 
D 4 869  SER 869  866  866  SER SER A . n 
D 4 870  ASP 870  867  867  ASP ASP A . n 
D 4 871  LYS 871  868  868  LYS LYS A . n 
D 4 872  PHE 872  869  869  PHE PHE A . n 
D 4 873  PHE 873  870  870  PHE PHE A . n 
D 4 874  PHE 874  871  871  PHE PHE A . n 
D 4 875  HIS 875  872  872  HIS HIS A . n 
D 4 876  VAL 876  873  873  VAL VAL A . n 
D 4 877  PRO 877  874  874  PRO PRO A . n 
D 4 878  ILE 878  875  875  ILE ILE A . n 
D 4 879  THR 879  876  876  THR THR A . n 
D 4 880  LEU 880  877  877  LEU LEU A . n 
D 4 881  ASN 881  878  878  ASN ASN A . n 
D 4 882  TYR 882  879  879  TYR TYR A . n 
D 4 883  GLN 883  880  880  GLN GLN A . n 
D 4 884  ALA 884  881  881  ALA ALA A . n 
D 4 885  ALA 885  882  882  ALA ALA A . n 
D 4 886  ASN 886  883  883  ASN ASN A . n 
D 4 887  SER 887  884  884  SER SER A . n 
D 4 888  PRO 888  885  885  PRO PRO A . n 
D 4 889  SER 889  886  886  SER SER A . n 
D 4 890  LYS 890  887  887  LYS LYS A . n 
D 4 891  PHE 891  888  888  PHE PHE A . n 
D 4 892  ASN 892  889  889  ASN ASN A . n 
D 4 893  GLN 893  890  890  GLN GLN A . n 
D 4 894  ARG 894  891  891  ARG ARG A . n 
D 4 895  VAL 895  892  892  VAL VAL A . n 
D 4 896  ASN 896  893  893  ASN ASN A . n 
D 4 897  ALA 897  894  894  ALA ALA A . n 
D 4 898  TYR 898  895  895  TYR TYR A . n 
D 4 899  LEU 899  896  896  LEU LEU A . n 
D 4 900  LYS 900  897  897  LYS LYS A . n 
D 4 901  GLU 901  898  898  GLU GLU A . n 
D 4 902  HIS 902  899  899  HIS HIS A . n 
D 4 903  PRO 903  900  900  PRO PRO A . n 
D 4 904  GLU 904  901  901  GLU GLU A . n 
D 4 905  THR 905  902  902  THR THR A . n 
D 4 906  PRO 906  903  903  PRO PRO A . n 
D 4 907  ILE 907  904  904  ILE ILE A . n 
D 4 908  ILE 908  905  905  ILE ILE A . n 
D 4 909  GLY 909  906  906  GLY GLY A . n 
D 4 910  ILE 910  907  907  ILE ILE A . n 
D 4 911  ASP 911  908  908  ASP ASP A . n 
D 4 912  ARG 912  909  909  ARG ARG A . n 
D 4 913  GLY 913  910  910  GLY GLY A . n 
D 4 914  GLU 914  911  911  GLU GLU A . n 
D 4 915  ARG 915  912  912  ARG ARG A . n 
D 4 916  ASN 916  913  913  ASN ASN A . n 
D 4 917  LEU 917  914  914  LEU LEU A . n 
D 4 918  ILE 918  915  915  ILE ILE A . n 
D 4 919  TYR 919  916  916  TYR TYR A . n 
D 4 920  ILE 920  917  917  ILE ILE A . n 
D 4 921  THR 921  918  918  THR THR A . n 
D 4 922  VAL 922  919  919  VAL VAL A . n 
D 4 923  ILE 923  920  920  ILE ILE A . n 
D 4 924  ASP 924  921  921  ASP ASP A . n 
D 4 925  SER 925  922  922  SER SER A . n 
D 4 926  THR 926  923  923  THR THR A . n 
D 4 927  GLY 927  924  924  GLY GLY A . n 
D 4 928  LYS 928  925  925  LYS LYS A . n 
D 4 929  ILE 929  926  926  ILE ILE A . n 
D 4 930  LEU 930  927  927  LEU LEU A . n 
D 4 931  GLU 931  928  928  GLU GLU A . n 
D 4 932  GLN 932  929  929  GLN GLN A . n 
D 4 933  ARG 933  930  930  ARG ARG A . n 
D 4 934  SER 934  931  931  SER SER A . n 
D 4 935  LEU 935  932  932  LEU LEU A . n 
D 4 936  ASN 936  933  933  ASN ASN A . n 
D 4 937  THR 937  934  934  THR THR A . n 
D 4 938  ILE 938  935  935  ILE ILE A . n 
D 4 939  GLN 939  936  936  GLN GLN A . n 
D 4 940  GLN 940  937  937  GLN GLN A . n 
D 4 941  PHE 941  938  938  PHE PHE A . n 
D 4 942  ASP 942  939  939  ASP ASP A . n 
D 4 943  TYR 943  940  940  TYR TYR A . n 
D 4 944  GLN 944  941  941  GLN GLN A . n 
D 4 945  LYS 945  942  942  LYS LYS A . n 
D 4 946  LYS 946  943  943  LYS LYS A . n 
D 4 947  LEU 947  944  944  LEU LEU A . n 
D 4 948  ASP 948  945  945  ASP ASP A . n 
D 4 949  ASN 949  946  946  ASN ASN A . n 
D 4 950  ARG 950  947  947  ARG ARG A . n 
D 4 951  GLU 951  948  948  GLU GLU A . n 
D 4 952  LYS 952  949  949  LYS LYS A . n 
D 4 953  GLU 953  950  950  GLU GLU A . n 
D 4 954  ARG 954  951  951  ARG ARG A . n 
D 4 955  VAL 955  952  952  VAL VAL A . n 
D 4 956  ALA 956  953  953  ALA ALA A . n 
D 4 957  ALA 957  954  954  ALA ALA A . n 
D 4 958  ARG 958  955  955  ARG ARG A . n 
D 4 959  GLN 959  956  956  GLN GLN A . n 
D 4 960  ALA 960  957  957  ALA ALA A . n 
D 4 961  TRP 961  958  958  TRP TRP A . n 
D 4 962  SER 962  959  959  SER SER A . n 
D 4 963  VAL 963  960  960  VAL VAL A . n 
D 4 964  VAL 964  961  961  VAL VAL A . n 
D 4 965  GLY 965  962  962  GLY GLY A . n 
D 4 966  THR 966  963  963  THR THR A . n 
D 4 967  ILE 967  964  964  ILE ILE A . n 
D 4 968  LYS 968  965  965  LYS LYS A . n 
D 4 969  ASP 969  966  966  ASP ASP A . n 
D 4 970  LEU 970  967  967  LEU LEU A . n 
D 4 971  LYS 971  968  968  LYS LYS A . n 
D 4 972  GLN 972  969  969  GLN GLN A . n 
D 4 973  GLY 973  970  970  GLY GLY A . n 
D 4 974  TYR 974  971  971  TYR TYR A . n 
D 4 975  LEU 975  972  972  LEU LEU A . n 
D 4 976  SER 976  973  973  SER SER A . n 
D 4 977  GLN 977  974  974  GLN GLN A . n 
D 4 978  VAL 978  975  975  VAL VAL A . n 
D 4 979  ILE 979  976  976  ILE ILE A . n 
D 4 980  HIS 980  977  977  HIS HIS A . n 
D 4 981  GLU 981  978  978  GLU GLU A . n 
D 4 982  ILE 982  979  979  ILE ILE A . n 
D 4 983  VAL 983  980  980  VAL VAL A . n 
D 4 984  ASP 984  981  981  ASP ASP A . n 
D 4 985  LEU 985  982  982  LEU LEU A . n 
D 4 986  MET 986  983  983  MET MET A . n 
D 4 987  ILE 987  984  984  ILE ILE A . n 
D 4 988  HIS 988  985  985  HIS HIS A . n 
D 4 989  TYR 989  986  986  TYR TYR A . n 
D 4 990  GLN 990  987  987  GLN GLN A . n 
D 4 991  ALA 991  988  988  ALA ALA A . n 
D 4 992  VAL 992  989  989  VAL VAL A . n 
D 4 993  VAL 993  990  990  VAL VAL A . n 
D 4 994  VAL 994  991  991  VAL VAL A . n 
D 4 995  LEU 995  992  992  LEU LEU A . n 
D 4 996  GLU 996  993  993  GLU GLU A . n 
D 4 997  ASN 997  994  994  ASN ASN A . n 
D 4 998  LEU 998  995  995  LEU LEU A . n 
D 4 999  ASN 999  996  996  ASN ASN A . n 
D 4 1000 PHE 1000 997  997  PHE PHE A . n 
D 4 1001 GLY 1001 998  998  GLY GLY A . n 
D 4 1002 PHE 1002 999  999  PHE PHE A . n 
D 4 1003 LYS 1003 1000 1000 LYS LYS A . n 
D 4 1004 SER 1004 1001 1001 SER SER A . n 
D 4 1005 LYS 1005 1002 1002 LYS LYS A . n 
D 4 1006 ARG 1006 1003 1003 ARG ARG A . n 
D 4 1007 THR 1007 1004 1004 THR THR A . n 
D 4 1008 GLY 1008 1005 1005 GLY GLY A . n 
D 4 1009 ILE 1009 1006 1006 ILE ILE A . n 
D 4 1010 ALA 1010 1007 1007 ALA ALA A . n 
D 4 1011 GLU 1011 1008 1008 GLU GLU A . n 
D 4 1012 LYS 1012 1009 1009 LYS LYS A . n 
D 4 1013 ALA 1013 1010 1010 ALA ALA A . n 
D 4 1014 VAL 1014 1011 1011 VAL VAL A . n 
D 4 1015 TYR 1015 1012 1012 TYR TYR A . n 
D 4 1016 GLN 1016 1013 1013 GLN GLN A . n 
D 4 1017 GLN 1017 1014 1014 GLN GLN A . n 
D 4 1018 PHE 1018 1015 1015 PHE PHE A . n 
D 4 1019 GLU 1019 1016 1016 GLU GLU A . n 
D 4 1020 LYS 1020 1017 1017 LYS LYS A . n 
D 4 1021 MET 1021 1018 1018 MET MET A . n 
D 4 1022 LEU 1022 1019 1019 LEU LEU A . n 
D 4 1023 ILE 1023 1020 1020 ILE ILE A . n 
D 4 1024 ASP 1024 1021 1021 ASP ASP A . n 
D 4 1025 LYS 1025 1022 1022 LYS LYS A . n 
D 4 1026 LEU 1026 1023 1023 LEU LEU A . n 
D 4 1027 ASN 1027 1024 1024 ASN ASN A . n 
D 4 1028 CYS 1028 1025 1025 CYS CYS A . n 
D 4 1029 LEU 1029 1026 1026 LEU LEU A . n 
D 4 1030 VAL 1030 1027 1027 VAL VAL A . n 
D 4 1031 LEU 1031 1028 1028 LEU LEU A . n 
D 4 1032 LYS 1032 1029 1029 LYS LYS A . n 
D 4 1033 ASP 1033 1030 1030 ASP ASP A . n 
D 4 1034 TYR 1034 1031 1031 TYR TYR A . n 
D 4 1035 PRO 1035 1032 1032 PRO PRO A . n 
D 4 1036 ALA 1036 1033 1033 ALA ALA A . n 
D 4 1037 GLU 1037 1034 1034 GLU GLU A . n 
D 4 1038 LYS 1038 1035 1035 LYS LYS A . n 
D 4 1039 VAL 1039 1036 1036 VAL VAL A . n 
D 4 1040 GLY 1040 1037 1037 GLY GLY A . n 
D 4 1041 GLY 1041 1038 1038 GLY GLY A . n 
D 4 1042 VAL 1042 1039 1039 VAL VAL A . n 
D 4 1043 LEU 1043 1040 1040 LEU LEU A . n 
D 4 1044 ASN 1044 1041 1041 ASN ASN A . n 
D 4 1045 PRO 1045 1042 1042 PRO PRO A . n 
D 4 1046 TYR 1046 1043 1043 TYR TYR A . n 
D 4 1047 GLN 1047 1044 1044 GLN GLN A . n 
D 4 1048 LEU 1048 1045 1045 LEU LEU A . n 
D 4 1049 THR 1049 1046 1046 THR THR A . n 
D 4 1050 ASP 1050 1047 1047 ASP ASP A . n 
D 4 1051 GLN 1051 1048 1048 GLN GLN A . n 
D 4 1052 PHE 1052 1049 1049 PHE PHE A . n 
D 4 1053 THR 1053 1050 1050 THR THR A . n 
D 4 1054 SER 1054 1051 1051 SER SER A . n 
D 4 1055 PHE 1055 1052 1052 PHE PHE A . n 
D 4 1056 ALA 1056 1053 1053 ALA ALA A . n 
D 4 1057 LYS 1057 1054 1054 LYS LYS A . n 
D 4 1058 MET 1058 1055 1055 MET MET A . n 
D 4 1059 GLY 1059 1056 1056 GLY GLY A . n 
D 4 1060 THR 1060 1057 1057 THR THR A . n 
D 4 1061 GLN 1061 1058 1058 GLN GLN A . n 
D 4 1062 SER 1062 1059 1059 SER SER A . n 
D 4 1063 GLY 1063 1060 1060 GLY GLY A . n 
D 4 1064 PHE 1064 1061 1061 PHE PHE A . n 
D 4 1065 LEU 1065 1062 1062 LEU LEU A . n 
D 4 1066 PHE 1066 1063 1063 PHE PHE A . n 
D 4 1067 TYR 1067 1064 1064 TYR TYR A . n 
D 4 1068 VAL 1068 1065 1065 VAL VAL A . n 
D 4 1069 PRO 1069 1066 1066 PRO PRO A . n 
D 4 1070 ALA 1070 1067 1067 ALA ALA A . n 
D 4 1071 PRO 1071 1068 1068 PRO PRO A . n 
D 4 1072 TYR 1072 1069 1069 TYR TYR A . n 
D 4 1073 THR 1073 1070 1070 THR THR A . n 
D 4 1074 SER 1074 1071 1071 SER SER A . n 
D 4 1075 LYS 1075 1072 1072 LYS LYS A . n 
D 4 1076 ILE 1076 1073 1073 ILE ILE A . n 
D 4 1077 ASP 1077 1074 1074 ASP ASP A . n 
D 4 1078 PRO 1078 1075 1075 PRO PRO A . n 
D 4 1079 LEU 1079 1076 1076 LEU LEU A . n 
D 4 1080 THR 1080 1077 1077 THR THR A . n 
D 4 1081 GLY 1081 1078 1078 GLY GLY A . n 
D 4 1082 PHE 1082 1079 1079 PHE PHE A . n 
D 4 1083 VAL 1083 1080 1080 VAL VAL A . n 
D 4 1084 ASP 1084 1081 1081 ASP ASP A . n 
D 4 1085 PRO 1085 1082 1082 PRO PRO A . n 
D 4 1086 PHE 1086 1083 1083 PHE PHE A . n 
D 4 1087 VAL 1087 1084 1084 VAL VAL A . n 
D 4 1088 TRP 1088 1085 1085 TRP TRP A . n 
D 4 1089 LYS 1089 1086 1086 LYS LYS A . n 
D 4 1090 THR 1090 1087 1087 THR THR A . n 
D 4 1091 ILE 1091 1088 1088 ILE ILE A . n 
D 4 1092 LYS 1092 1089 1089 LYS LYS A . n 
D 4 1093 ASN 1093 1090 1090 ASN ASN A . n 
D 4 1094 HIS 1094 1091 1091 HIS HIS A . n 
D 4 1095 GLU 1095 1092 1092 GLU GLU A . n 
D 4 1096 SER 1096 1093 1093 SER SER A . n 
D 4 1097 ARG 1097 1094 1094 ARG ARG A . n 
D 4 1098 LYS 1098 1095 1095 LYS LYS A . n 
D 4 1099 HIS 1099 1096 1096 HIS HIS A . n 
D 4 1100 PHE 1100 1097 1097 PHE PHE A . n 
D 4 1101 LEU 1101 1098 1098 LEU LEU A . n 
D 4 1102 GLU 1102 1099 1099 GLU GLU A . n 
D 4 1103 GLY 1103 1100 1100 GLY GLY A . n 
D 4 1104 PHE 1104 1101 1101 PHE PHE A . n 
D 4 1105 ASP 1105 1102 1102 ASP ASP A . n 
D 4 1106 PHE 1106 1103 1103 PHE PHE A . n 
D 4 1107 LEU 1107 1104 1104 LEU LEU A . n 
D 4 1108 HIS 1108 1105 1105 HIS HIS A . n 
D 4 1109 TYR 1109 1106 1106 TYR TYR A . n 
D 4 1110 ASP 1110 1107 1107 ASP ASP A . n 
D 4 1111 VAL 1111 1108 1108 VAL VAL A . n 
D 4 1112 LYS 1112 1109 1109 LYS LYS A . n 
D 4 1113 THR 1113 1110 1110 THR THR A . n 
D 4 1114 GLY 1114 1111 1111 GLY GLY A . n 
D 4 1115 ASP 1115 1112 1112 ASP ASP A . n 
D 4 1116 PHE 1116 1113 1113 PHE PHE A . n 
D 4 1117 ILE 1117 1114 1114 ILE ILE A . n 
D 4 1118 LEU 1118 1115 1115 LEU LEU A . n 
D 4 1119 HIS 1119 1116 1116 HIS HIS A . n 
D 4 1120 PHE 1120 1117 1117 PHE PHE A . n 
D 4 1121 LYS 1121 1118 1118 LYS LYS A . n 
D 4 1122 MET 1122 1119 1119 MET MET A . n 
D 4 1123 ASN 1123 1120 1120 ASN ASN A . n 
D 4 1124 ARG 1124 1121 1121 ARG ARG A . n 
D 4 1125 ASN 1125 1122 1122 ASN ASN A . n 
D 4 1126 LEU 1126 1123 1123 LEU LEU A . n 
D 4 1127 SER 1127 1124 1124 SER SER A . n 
D 4 1128 PHE 1128 1125 1125 PHE PHE A . n 
D 4 1129 GLN 1129 1126 1126 GLN GLN A . n 
D 4 1130 ARG 1130 1127 1127 ARG ARG A . n 
D 4 1131 GLY 1131 1128 1128 GLY GLY A . n 
D 4 1132 LEU 1132 1129 1129 LEU LEU A . n 
D 4 1133 PRO 1133 1130 1130 PRO PRO A . n 
D 4 1134 GLY 1134 1131 1131 GLY GLY A . n 
D 4 1135 PHE 1135 1132 1132 PHE PHE A . n 
D 4 1136 MET 1136 1133 1133 MET MET A . n 
D 4 1137 PRO 1137 1134 1134 PRO PRO A . n 
D 4 1138 ALA 1138 1135 1135 ALA ALA A . n 
D 4 1139 TRP 1139 1136 1136 TRP TRP A . n 
D 4 1140 ASP 1140 1137 1137 ASP ASP A . n 
D 4 1141 ILE 1141 1138 1138 ILE ILE A . n 
D 4 1142 VAL 1142 1139 1139 VAL VAL A . n 
D 4 1143 PHE 1143 1140 1140 PHE PHE A . n 
D 4 1144 GLU 1144 1141 1141 GLU GLU A . n 
D 4 1145 LYS 1145 1142 1142 LYS LYS A . n 
D 4 1146 ASN 1146 1143 1143 ASN ASN A . n 
D 4 1147 GLU 1147 1144 1144 GLU GLU A . n 
D 4 1148 THR 1148 1145 1145 THR THR A . n 
D 4 1149 GLN 1149 1146 1146 GLN GLN A . n 
D 4 1150 PHE 1150 1147 1147 PHE PHE A . n 
D 4 1151 ASP 1151 1148 1148 ASP ASP A . n 
D 4 1152 ALA 1152 1149 1149 ALA ALA A . n 
D 4 1153 LYS 1153 1150 1150 LYS LYS A . n 
D 4 1154 GLY 1154 1151 1151 GLY GLY A . n 
D 4 1155 THR 1155 1152 1152 THR THR A . n 
D 4 1156 PRO 1156 1153 1153 PRO PRO A . n 
D 4 1157 PHE 1157 1154 1154 PHE PHE A . n 
D 4 1158 ILE 1158 1155 1155 ILE ILE A . n 
D 4 1159 ALA 1159 1156 1156 ALA ALA A . n 
D 4 1160 GLY 1160 1157 1157 GLY GLY A . n 
D 4 1161 LYS 1161 1158 1158 LYS LYS A . n 
D 4 1162 ARG 1162 1159 1159 ARG ARG A . n 
D 4 1163 ILE 1163 1160 1160 ILE ILE A . n 
D 4 1164 VAL 1164 1161 1161 VAL VAL A . n 
D 4 1165 PRO 1165 1162 1162 PRO PRO A . n 
D 4 1166 VAL 1166 1163 1163 VAL VAL A . n 
D 4 1167 ILE 1167 1164 1164 ILE ILE A . n 
D 4 1168 GLU 1168 1165 1165 GLU GLU A . n 
D 4 1169 ASN 1169 1166 1166 ASN ASN A . n 
D 4 1170 HIS 1170 1167 1167 HIS HIS A . n 
D 4 1171 ARG 1171 1168 1168 ARG ARG A . n 
D 4 1172 PHE 1172 1169 1169 PHE PHE A . n 
D 4 1173 THR 1173 1170 1170 THR THR A . n 
D 4 1174 GLY 1174 1171 1171 GLY GLY A . n 
D 4 1175 ARG 1175 1172 1172 ARG ARG A . n 
D 4 1176 TYR 1176 1173 1173 TYR TYR A . n 
D 4 1177 ARG 1177 1174 1174 ARG ARG A . n 
D 4 1178 ASP 1178 1175 1175 ASP ASP A . n 
D 4 1179 LEU 1179 1176 1176 LEU LEU A . n 
D 4 1180 TYR 1180 1177 1177 TYR TYR A . n 
D 4 1181 PRO 1181 1178 1178 PRO PRO A . n 
D 4 1182 ALA 1182 1179 1179 ALA ALA A . n 
D 4 1183 ASN 1183 1180 1180 ASN ASN A . n 
D 4 1184 GLU 1184 1181 1181 GLU GLU A . n 
D 4 1185 LEU 1185 1182 1182 LEU LEU A . n 
D 4 1186 ILE 1186 1183 1183 ILE ILE A . n 
D 4 1187 ALA 1187 1184 1184 ALA ALA A . n 
D 4 1188 LEU 1188 1185 1185 LEU LEU A . n 
D 4 1189 LEU 1189 1186 1186 LEU LEU A . n 
D 4 1190 GLU 1190 1187 1187 GLU GLU A . n 
D 4 1191 GLU 1191 1188 1188 GLU GLU A . n 
D 4 1192 LYS 1192 1189 1189 LYS LYS A . n 
D 4 1193 GLY 1193 1190 1190 GLY GLY A . n 
D 4 1194 ILE 1194 1191 1191 ILE ILE A . n 
D 4 1195 VAL 1195 1192 1192 VAL VAL A . n 
D 4 1196 PHE 1196 1193 1193 PHE PHE A . n 
D 4 1197 ARG 1197 1194 1194 ARG ARG A . n 
D 4 1198 ASP 1198 1195 1195 ASP ASP A . n 
D 4 1199 GLY 1199 1196 1196 GLY GLY A . n 
D 4 1200 SER 1200 1197 1197 SER SER A . n 
D 4 1201 ASN 1201 1198 1198 ASN ASN A . n 
D 4 1202 ILE 1202 1199 1199 ILE ILE A . n 
D 4 1203 LEU 1203 1200 1200 LEU LEU A . n 
D 4 1204 PRO 1204 1201 1201 PRO PRO A . n 
D 4 1205 LYS 1205 1202 1202 LYS LYS A . n 
D 4 1206 LEU 1206 1203 1203 LEU LEU A . n 
D 4 1207 LEU 1207 1204 1204 LEU LEU A . n 
D 4 1208 GLU 1208 1205 1205 GLU GLU A . n 
D 4 1209 ASN 1209 1206 1206 ASN ASN A . n 
D 4 1210 ASP 1210 1207 1207 ASP ASP A . n 
D 4 1211 ASP 1211 1208 1208 ASP ASP A . n 
D 4 1212 SER 1212 1209 1209 SER SER A . n 
D 4 1213 HIS 1213 1210 1210 HIS HIS A . n 
D 4 1214 ALA 1214 1211 1211 ALA ALA A . n 
D 4 1215 ILE 1215 1212 1212 ILE ILE A . n 
D 4 1216 ASP 1216 1213 1213 ASP ASP A . n 
D 4 1217 THR 1217 1214 1214 THR THR A . n 
D 4 1218 MET 1218 1215 1215 MET MET A . n 
D 4 1219 VAL 1219 1216 1216 VAL VAL A . n 
D 4 1220 ALA 1220 1217 1217 ALA ALA A . n 
D 4 1221 LEU 1221 1218 1218 LEU LEU A . n 
D 4 1222 ILE 1222 1219 1219 ILE ILE A . n 
D 4 1223 ARG 1223 1220 1220 ARG ARG A . n 
D 4 1224 SER 1224 1221 1221 SER SER A . n 
D 4 1225 VAL 1225 1222 1222 VAL VAL A . n 
D 4 1226 LEU 1226 1223 1223 LEU LEU A . n 
D 4 1227 GLN 1227 1224 1224 GLN GLN A . n 
D 4 1228 MET 1228 1225 1225 MET MET A . n 
D 4 1229 ARG 1229 1226 1226 ARG ARG A . n 
D 4 1230 ASN 1230 1227 1227 ASN ASN A . n 
D 4 1231 SER 1231 1228 1228 SER SER A . n 
D 4 1232 ASN 1232 1229 1229 ASN ASN A . n 
D 4 1233 ALA 1233 1230 1230 ALA ALA A . n 
D 4 1234 ALA 1234 1231 1231 ALA ALA A . n 
D 4 1235 THR 1235 1232 1232 THR THR A . n 
D 4 1236 GLY 1236 1233 1233 GLY GLY A . n 
D 4 1237 GLU 1237 1234 1234 GLU GLU A . n 
D 4 1238 ASP 1238 1235 1235 ASP ASP A . n 
D 4 1239 TYR 1239 1236 1236 TYR TYR A . n 
D 4 1240 ILE 1240 1237 1237 ILE ILE A . n 
D 4 1241 ASN 1241 1238 1238 ASN ASN A . n 
D 4 1242 SER 1242 1239 1239 SER SER A . n 
D 4 1243 PRO 1243 1240 1240 PRO PRO A . n 
D 4 1244 VAL 1244 1241 1241 VAL VAL A . n 
D 4 1245 ARG 1245 1242 1242 ARG ARG A . n 
D 4 1246 ASP 1246 1243 1243 ASP ASP A . n 
D 4 1247 LEU 1247 1244 1244 LEU LEU A . n 
D 4 1248 ASN 1248 1245 1245 ASN ASN A . n 
D 4 1249 GLY 1249 1246 1246 GLY GLY A . n 
D 4 1250 VAL 1250 1247 1247 VAL VAL A . n 
D 4 1251 CYS 1251 1248 1248 CYS CYS A . n 
D 4 1252 PHE 1252 1249 1249 PHE PHE A . n 
D 4 1253 ASP 1253 1250 1250 ASP ASP A . n 
D 4 1254 SER 1254 1251 1251 SER SER A . n 
D 4 1255 ARG 1255 1252 1252 ARG ARG A . n 
D 4 1256 PHE 1256 1253 1253 PHE PHE A . n 
D 4 1257 GLN 1257 1254 1254 GLN GLN A . n 
D 4 1258 ASN 1258 1255 1255 ASN ASN A . n 
D 4 1259 PRO 1259 1256 1256 PRO PRO A . n 
D 4 1260 GLU 1260 1257 1257 GLU GLU A . n 
D 4 1261 TRP 1261 1258 1258 TRP TRP A . n 
D 4 1262 PRO 1262 1259 1259 PRO PRO A . n 
D 4 1263 MET 1263 1260 1260 MET MET A . n 
D 4 1264 ASP 1264 1261 1261 ASP ASP A . n 
D 4 1265 ALA 1265 1262 1262 ALA ALA A . n 
D 4 1266 ASP 1266 1263 1263 ASP ASP A . n 
D 4 1267 ALA 1267 1264 1264 ALA ALA A . n 
D 4 1268 ASN 1268 1265 1265 ASN ASN A . n 
D 4 1269 GLY 1269 1266 1266 GLY GLY A . n 
D 4 1270 ALA 1270 1267 1267 ALA ALA A . n 
D 4 1271 TYR 1271 1268 1268 TYR TYR A . n 
D 4 1272 HIS 1272 1269 1269 HIS HIS A . n 
D 4 1273 ILE 1273 1270 1270 ILE ILE A . n 
D 4 1274 ALA 1274 1271 1271 ALA ALA A . n 
D 4 1275 LEU 1275 1272 1272 LEU LEU A . n 
D 4 1276 LYS 1276 1273 1273 LYS LYS A . n 
D 4 1277 GLY 1277 1274 1274 GLY GLY A . n 
D 4 1278 GLN 1278 1275 1275 GLN GLN A . n 
D 4 1279 LEU 1279 1276 1276 LEU LEU A . n 
D 4 1280 LEU 1280 1277 1277 LEU LEU A . n 
D 4 1281 LEU 1281 1278 1278 LEU LEU A . n 
D 4 1282 ASN 1282 1279 1279 ASN ASN A . n 
D 4 1283 HIS 1283 1280 1280 HIS HIS A . n 
D 4 1284 LEU 1284 1281 1281 LEU LEU A . n 
D 4 1285 LYS 1285 1282 1282 LYS LYS A . n 
D 4 1286 GLU 1286 1283 1283 GLU GLU A . n 
D 4 1287 SER 1287 1284 1284 SER SER A . n 
D 4 1288 LYS 1288 1285 1285 LYS LYS A . n 
D 4 1289 ASP 1289 1286 1286 ASP ASP A . n 
D 4 1290 LEU 1290 1287 1287 LEU LEU A . n 
D 4 1291 LYS 1291 1288 1288 LYS LYS A . n 
D 4 1292 LEU 1292 1289 1289 LEU LEU A . n 
D 4 1293 GLN 1293 1290 1290 GLN GLN A . n 
D 4 1294 ASN 1294 1291 1291 ASN ASN A . n 
D 4 1295 GLY 1295 1292 1292 GLY GLY A . n 
D 4 1296 ILE 1296 1293 1293 ILE ILE A . n 
D 4 1297 SER 1297 1294 1294 SER SER A . n 
D 4 1298 ASN 1298 1295 1295 ASN ASN A . n 
D 4 1299 GLN 1299 1296 1296 GLN GLN A . n 
D 4 1300 ASP 1300 1297 1297 ASP ASP A . n 
D 4 1301 TRP 1301 1298 1298 TRP TRP A . n 
D 4 1302 LEU 1302 1299 1299 LEU LEU A . n 
D 4 1303 ALA 1303 1300 1300 ALA ALA A . n 
D 4 1304 TYR 1304 1301 1301 TYR TYR A . n 
D 4 1305 ILE 1305 1302 1302 ILE ILE A . n 
D 4 1306 GLN 1306 1303 1303 GLN GLN A . n 
D 4 1307 GLU 1307 1304 1304 GLU GLU A . n 
D 4 1308 LEU 1308 1305 1305 LEU LEU A . n 
D 4 1309 ARG 1309 1306 1306 ARG ARG A . n 
D 4 1310 ASN 1310 1307 1307 ASN ASN A . n 
# 
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 GLU 89  ? CG  ? D GLU 92  CG  
2  1 Y 1 A GLU 89  ? CD  ? D GLU 92  CD  
3  1 Y 1 A GLU 89  ? OE1 ? D GLU 92  OE1 
4  1 Y 1 A GLU 89  ? OE2 ? D GLU 92  OE2 
5  1 Y 1 A LYS 123 ? CG  ? D LYS 126 CG  
6  1 Y 1 A LYS 123 ? CD  ? D LYS 126 CD  
7  1 Y 1 A LYS 123 ? CE  ? D LYS 126 CE  
8  1 Y 1 A LYS 123 ? NZ  ? D LYS 126 NZ  
9  1 Y 1 A ARG 124 ? CG  ? D ARG 127 CG  
10 1 Y 1 A ARG 124 ? CD  ? D ARG 127 CD  
11 1 Y 1 A ARG 124 ? NE  ? D ARG 127 NE  
12 1 Y 1 A ARG 124 ? CZ  ? D ARG 127 CZ  
13 1 Y 1 A ARG 124 ? NH1 ? D ARG 127 NH1 
14 1 Y 1 A ARG 124 ? NH2 ? D ARG 127 NH2 
15 1 Y 1 A GLU 127 ? CG  ? D GLU 130 CG  
16 1 Y 1 A GLU 127 ? CD  ? D GLU 130 CD  
17 1 Y 1 A GLU 127 ? OE1 ? D GLU 130 OE1 
18 1 Y 1 A GLU 127 ? OE2 ? D GLU 130 OE2 
19 1 Y 1 A LYS 130 ? CG  ? D LYS 133 CG  
20 1 Y 1 A LYS 130 ? CD  ? D LYS 133 CD  
21 1 Y 1 A LYS 130 ? CE  ? D LYS 133 CE  
22 1 Y 1 A LYS 130 ? NZ  ? D LYS 133 NZ  
23 1 Y 1 A LYS 141 ? CG  ? D LYS 144 CG  
24 1 Y 1 A LYS 141 ? CD  ? D LYS 144 CD  
25 1 Y 1 A LYS 141 ? CE  ? D LYS 144 CE  
26 1 Y 1 A LYS 141 ? NZ  ? D LYS 144 NZ  
27 1 Y 1 A LYS 144 ? CG  ? D LYS 147 CG  
28 1 Y 1 A LYS 144 ? CD  ? D LYS 147 CD  
29 1 Y 1 A LYS 144 ? CE  ? D LYS 147 CE  
30 1 Y 1 A LYS 144 ? NZ  ? D LYS 147 NZ  
31 1 Y 1 A GLU 153 ? CG  ? D GLU 156 CG  
32 1 Y 1 A GLU 153 ? CD  ? D GLU 156 CD  
33 1 Y 1 A GLU 153 ? OE1 ? D GLU 156 OE1 
34 1 Y 1 A GLU 153 ? OE2 ? D GLU 156 OE2 
35 1 Y 1 A ASP 163 ? CG  ? D ASP 166 CG  
36 1 Y 1 A ASP 163 ? OD1 ? D ASP 166 OD1 
37 1 Y 1 A ASP 163 ? OD2 ? D ASP 166 OD2 
38 1 Y 1 A LYS 164 ? CG  ? D LYS 167 CG  
39 1 Y 1 A LYS 164 ? CD  ? D LYS 167 CD  
40 1 Y 1 A LYS 164 ? CE  ? D LYS 167 CE  
41 1 Y 1 A LYS 164 ? NZ  ? D LYS 167 NZ  
42 1 Y 1 A GLU 220 ? CG  ? D GLU 223 CG  
43 1 Y 1 A GLU 220 ? CD  ? D GLU 223 CD  
44 1 Y 1 A GLU 220 ? OE1 ? D GLU 223 OE1 
45 1 Y 1 A GLU 220 ? OE2 ? D GLU 223 OE2 
46 1 Y 1 A GLU 327 ? CG  ? D GLU 330 CG  
47 1 Y 1 A GLU 327 ? CD  ? D GLU 330 CD  
48 1 Y 1 A GLU 327 ? OE1 ? D GLU 330 OE1 
49 1 Y 1 A GLU 327 ? OE2 ? D GLU 330 OE2 
50 1 Y 1 A GLN 331 ? CG  ? D GLN 334 CG  
51 1 Y 1 A GLN 331 ? CD  ? D GLN 334 CD  
52 1 Y 1 A GLN 331 ? OE1 ? D GLN 334 OE1 
53 1 Y 1 A GLN 331 ? NE2 ? D GLN 334 NE2 
54 1 Y 1 A LYS 335 ? CG  ? D LYS 338 CG  
55 1 Y 1 A LYS 335 ? CD  ? D LYS 338 CD  
56 1 Y 1 A LYS 335 ? CE  ? D LYS 338 CE  
57 1 Y 1 A LYS 335 ? NZ  ? D LYS 338 NZ  
58 1 Y 1 A ASN 344 ? CG  ? D ASN 347 CG  
59 1 Y 1 A ASN 344 ? OD1 ? D ASN 347 OD1 
60 1 Y 1 A ASN 344 ? ND2 ? D ASN 347 ND2 
61 1 Y 1 A GLU 347 ? CG  ? D GLU 350 CG  
62 1 Y 1 A GLU 347 ? CD  ? D GLU 350 CD  
63 1 Y 1 A GLU 347 ? OE1 ? D GLU 350 OE1 
64 1 Y 1 A GLU 347 ? OE2 ? D GLU 350 OE2 
65 1 Y 1 A LYS 400 ? CG  ? D LYS 403 CG  
66 1 Y 1 A LYS 400 ? CD  ? D LYS 403 CD  
67 1 Y 1 A LYS 400 ? CE  ? D LYS 403 CE  
68 1 Y 1 A LYS 400 ? NZ  ? D LYS 403 NZ  
69 1 Y 1 A GLN 437 ? CG  ? D GLN 440 CG  
70 1 Y 1 A GLN 437 ? CD  ? D GLN 440 CD  
71 1 Y 1 A GLN 437 ? OE1 ? D GLN 440 OE1 
72 1 Y 1 A GLN 437 ? NE2 ? D GLN 440 NE2 
73 1 Y 1 A LYS 459 ? CG  ? D LYS 462 CG  
74 1 Y 1 A LYS 459 ? CD  ? D LYS 462 CD  
75 1 Y 1 A LYS 459 ? CE  ? D LYS 462 CE  
76 1 Y 1 A LYS 459 ? NZ  ? D LYS 462 NZ  
77 1 Y 1 A LYS 460 ? CG  ? D LYS 463 CG  
78 1 Y 1 A LYS 460 ? CD  ? D LYS 463 CD  
79 1 Y 1 A LYS 460 ? CE  ? D LYS 463 CE  
80 1 Y 1 A LYS 460 ? NZ  ? D LYS 463 NZ  
81 1 Y 1 A GLU 462 ? CG  ? D GLU 465 CG  
82 1 Y 1 A GLU 462 ? CD  ? D GLU 465 CD  
83 1 Y 1 A GLU 462 ? OE1 ? D GLU 465 OE1 
84 1 Y 1 A GLU 462 ? OE2 ? D GLU 465 OE2 
85 1 Y 1 A ASP 487 ? CG  ? D ASP 490 CG  
86 1 Y 1 A ASP 487 ? OD1 ? D ASP 490 OD1 
87 1 Y 1 A ASP 487 ? OD2 ? D ASP 490 OD2 
88 1 Y 1 A GLU 488 ? CG  ? D GLU 491 CG  
89 1 Y 1 A GLU 488 ? CD  ? D GLU 491 CD  
90 1 Y 1 A GLU 488 ? OE1 ? D GLU 491 OE1 
91 1 Y 1 A GLU 488 ? OE2 ? D GLU 491 OE2 
92 1 Y 1 A GLU 495 ? CG  ? D GLU 498 CG  
93 1 Y 1 A GLU 495 ? CD  ? D GLU 498 CD  
94 1 Y 1 A GLU 495 ? OE1 ? D GLU 498 OE1 
95 1 Y 1 A GLU 495 ? OE2 ? D GLU 498 OE2 
96 1 Y 1 A LYS 796 ? CG  ? D LYS 799 CG  
97 1 Y 1 A LYS 796 ? CD  ? D LYS 799 CD  
98 1 Y 1 A LYS 796 ? CE  ? D LYS 799 CE  
99 1 Y 1 A LYS 796 ? NZ  ? D LYS 799 NZ  
# 
_software.classification   refinement 
_software.name             PHENIX 
_software.version          1.19.2_4158 
_software.citation_id      ? 
_software.pdbx_ordinal     1 
# 
_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                     9CJI 
_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                         9CJI 
_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                   9CJI 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9CJI 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            3.40 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
f_bond_d           0.005  ? ? 11872 'ELECTRON MICROSCOPY' ? 
f_angle_d          0.606  ? ? 16346 'ELECTRON MICROSCOPY' ? 
f_dihedral_angle_d 17.757 ? ? 4548  'ELECTRON MICROSCOPY' ? 
f_chiral_restr     0.041  ? ? 1819  'ELECTRON MICROSCOPY' ? 
f_plane_restr      0.006  ? ? 1861  'ELECTRON MICROSCOPY' ? 
# 
_struct.entry_id                     9CJI 
_struct.title                        'Cas12a:gRNA:DNA (Acidaminococcus sp.) with 0 RNA:DNA base pairs, structure 2' 
_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        9CJI 
_struct_keywords.text            
'DNase, complex, ribonucleoprotein, genome editor, HYDROLASE-RNA complex, HYDROLASE, HYDROLASE-RNA-DNA complex' 
_struct_keywords.pdbx_keywords   HYDROLASE/RNA/DNA 
# 
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 ? 
# 
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 PDB 9CJI        9CJI   ? 1 ? 1 
2 PDB 9CJI        9CJI   ? 2 ? 1 
3 PDB 9CJI        9CJI   ? 3 ? 1 
4 UNP CS12A_ACISB U2UMQ6 ? 4 
;MTQFEGFTNLYQVSKTLRFELIPQGKTLKHIQEQGFIEEDKARNDHYKELKPIIDRIYKTYADQCLQLVQLDWENLSAAI
DSYRKEKTEETRNALIEEQATYRNAIHDYFIGRTDNLTDAINKRHAEIYKGLFKAELFNGKVLKQLGTVTTTEHENALLR
SFDKFTTYFSGFYENRKNVFSAEDISTAIPHRIVQDNFPKFKENCHIFTRLITAVPSLREHFENVKKAIGIFVSTSIEEV
FSFPFYNQLLTQTQIDLYNQLLGGISREAGTEKIKGLNEVLNLAIQKNDETAHIIASLPHRFIPLFKQILSDRNTLSFIL
EEFKSDEEVIQSFCKYKTLLRNENVLETAEALFNELNSIDLTHIFISHKKLETISSALCDHWDTLRNALYERRISELTGK
ITKSAKEKVQRSLKHEDINLQEIISAAGKELSEAFKQKTSEILSHAHAALDQPLPTTLKKQEEKEILKSQLDSLLGLYHL
LDWFAVDESNEVDPEFSARLTGIKLEMEPSLSFYNKARNYATKKPYSVEKFKLNFQMPTLASGWDVNKEKNNGAILFVKN
GLYYLGIMPKQKGRYKALSFEPTEKTSEGFDKMYYDYFPDAAKMIPKCSTQLKAVTAHFQTHTTPILLSNNFIEPLEITK
EIYDLNNPEKEPKKFQTAYAKKTGDQKGYREALCKWIDFTRDFLSKYTKTTSIDLSSLRPSSQYKDLGEYYAELNPLLYH
ISFQRIAEKEIMDAVETGKLYLFQIYNKDFAKGHHGKPNLHTLYWTGLFSPENLAKTSIKLNGQAELFYRPKSRMKRMAH
RLGEKMLNKKLKDQKTPIPDTLYQELYDYVNHRLSHDLSDEARALLPNVITKEVSHEIIKDRRFTSDKFFFHVPITLNYQ
AANSPSKFNQRVNAYLKEHPETPIIGIDRGERNLIYITVIDSTGKILEQRSLNTIQQFDYQKKLDNREKERVAARQAWSV
VGTIKDLKQGYLSQVIHEIVDLMIHYQAVVVLENLNFGFKSKRTGIAEKAVYQQFEKMLIDKLNCLVLKDYPAEKVGGVL
NPYQLTDQFTSFAKMGTQSGFLFYVPAPYTSKIDPLTGFVDPFVWKTIKNHESRKHFLEGFDFLHYDVKTGDFILHFKMN
RNLSFQRGLPGFMPAWDIVFEKNETQFDAKGTPFIAGKRIVPVIENHRFTGRYRDLYPANELIALLEEKGIVFRDGSNIL
PKLLENDDSHAIDTMVALIRSVLQMRNSNAATGEDYINSPVRDLNGVCFDSRFQNPEWPMDADANGAYHIALKGQLLLNH
LKESKDLKLQNGISNQDWLAYIQELRN
;
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 9CJI C 1 ? 31   ? 9CJI   1 ? 31   ? 1 31   
2 2 9CJI B 1 ? 42   ? 9CJI   1 ? 42   ? 1 42   
3 3 9CJI D 1 ? 31   ? 9CJI   1 ? 31   ? 1 31   
4 4 9CJI A 4 ? 1310 ? U2UMQ6 1 ? 1307 ? 1 1307 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
4 9CJI SER A 1   ? UNP U2UMQ6 ?   ?   'expression tag'      -2  1 
4 9CJI ASN A 2   ? UNP U2UMQ6 ?   ?   'expression tag'      -1  2 
4 9CJI ALA A 3   ? UNP U2UMQ6 ?   ?   'expression tag'      0   3 
4 9CJI CYS A 554 ? UNP U2UMQ6 ASN 551 'engineered mutation' 551 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLN D 6    ? PHE D 10   ? GLN A 3    PHE A 7    5 ? 5  
HELX_P HELX_P2  AA2 LYS D 29   ? GLY D 38   ? LYS A 26   GLY A 35   1 ? 10 
HELX_P HELX_P3  AA3 GLY D 38   ? LEU D 71   ? GLY A 35   LEU A 68   1 ? 34 
HELX_P HELX_P4  AA4 TRP D 76   ? GLU D 89   ? TRP A 73   GLU A 86   1 ? 14 
HELX_P HELX_P5  AA5 THR D 91   ? GLY D 115  ? THR A 88   GLY A 112  1 ? 25 
HELX_P HELX_P6  AA6 THR D 121  ? GLY D 134  ? THR A 118  GLY A 131  1 ? 14 
HELX_P HELX_P7  AA7 LEU D 135  ? PHE D 136  ? LEU A 132  PHE A 133  5 ? 2  
HELX_P HELX_P8  AA8 LYS D 137  ? PHE D 141  ? LYS A 134  PHE A 138  5 ? 5  
HELX_P HELX_P9  AA9 GLY D 143  ? LEU D 149  ? GLY A 140  LEU A 146  1 ? 7  
HELX_P HELX_P10 AB1 THR D 155  ? SER D 164  ? THR A 152  SER A 161  1 ? 10 
HELX_P HELX_P11 AB2 PHE D 172  ? SER D 184  ? PHE A 169  SER A 181  1 ? 13 
HELX_P HELX_P12 AB3 ALA D 191  ? ASP D 199  ? ALA A 188  ASP A 196  1 ? 9  
HELX_P HELX_P13 AB4 ASP D 199  ? VAL D 218  ? ASP A 196  VAL A 215  1 ? 20 
HELX_P HELX_P14 AB5 PRO D 219  ? GLY D 233  ? PRO A 216  GLY A 230  1 ? 15 
HELX_P HELX_P15 AB6 SER D 245  ? LEU D 252  ? SER A 242  LEU A 249  5 ? 8  
HELX_P HELX_P16 AB7 THR D 254  ? GLY D 267  ? THR A 251  GLY A 264  1 ? 14 
HELX_P HELX_P17 AB8 SER D 328  ? ASN D 347  ? SER A 325  ASN A 344  1 ? 20 
HELX_P HELX_P18 AB9 ASN D 347  ? LEU D 359  ? ASN A 344  LEU A 356  1 ? 13 
HELX_P HELX_P19 AC1 ASP D 363  ? HIS D 366  ? ASP A 360  HIS A 363  5 ? 4  
HELX_P HELX_P20 AC2 SER D 370  ? CYS D 382  ? SER A 367  CYS A 379  1 ? 13 
HELX_P HELX_P21 AC3 TRP D 385  ? SER D 398  ? TRP A 382  SER A 395  1 ? 14 
HELX_P HELX_P22 AC4 THR D 405  ? HIS D 418  ? THR A 402  HIS A 415  1 ? 14 
HELX_P HELX_P23 AC5 LEU D 423  ? GLY D 431  ? LEU A 420  GLY A 428  1 ? 9  
HELX_P HELX_P24 AC6 GLY D 431  ? ASP D 454  ? GLY A 428  ASP A 451  1 ? 24 
HELX_P HELX_P25 AC7 LYS D 463  ? ASP D 485  ? LYS A 460  ASP A 482  1 ? 23 
HELX_P HELX_P26 AC8 ASP D 496  ? MET D 510  ? ASP A 493  MET A 507  1 ? 15 
HELX_P HELX_P27 AC9 GLU D 511  ? THR D 525  ? GLU A 508  THR A 522  1 ? 15 
HELX_P HELX_P28 AD1 LYS D 551  ? GLY D 556  ? LYS A 548  GLY A 553  1 ? 6  
HELX_P HELX_P29 AD2 ASP D 603  ? THR D 613  ? ASP A 600  THR A 610  1 ? 11 
HELX_P HELX_P30 AD3 LEU D 615  ? HIS D 625  ? LEU A 612  HIS A 622  1 ? 11 
HELX_P HELX_P31 AD4 THR D 642  ? ASN D 650  ? THR A 639  ASN A 647  1 ? 9  
HELX_P HELX_P32 AD5 GLN D 659  ? GLY D 667  ? GLN A 656  GLY A 664  1 ? 9  
HELX_P HELX_P33 AD6 ASP D 668  ? TYR D 690  ? ASP A 665  TYR A 687  1 ? 23 
HELX_P HELX_P34 AD7 ASP D 697  ? LEU D 701  ? ASP A 694  LEU A 698  5 ? 5  
HELX_P HELX_P35 AD8 ASP D 709  ? TYR D 722  ? ASP A 706  TYR A 719  1 ? 14 
HELX_P HELX_P36 AD9 GLU D 731  ? THR D 740  ? GLU A 728  THR A 737  1 ? 10 
HELX_P HELX_P37 AE1 ASN D 762  ? PHE D 772  ? ASN A 759  PHE A 769  1 ? 11 
HELX_P HELX_P38 AE2 SER D 773  ? LYS D 779  ? SER A 770  LYS A 776  1 ? 7  
HELX_P HELX_P39 AE3 PRO D 822  ? ASN D 834  ? PRO A 819  ASN A 831  1 ? 13 
HELX_P HELX_P40 AE4 SER D 842  ? LEU D 849  ? SER A 839  LEU A 846  1 ? 8  
HELX_P HELX_P41 AE5 ASP D 864  ? THR D 868  ? ASP A 861  THR A 865  5 ? 5  
HELX_P HELX_P42 AE6 LYS D 890  ? HIS D 902  ? LYS A 887  HIS A 899  1 ? 13 
HELX_P HELX_P43 AE7 LYS D 946  ? GLN D 959  ? LYS A 943  GLN A 956  1 ? 14 
HELX_P HELX_P44 AE8 TRP D 961  ? GLN D 990  ? TRP A 958  GLN A 987  1 ? 30 
HELX_P HELX_P45 AE9 ALA D 1013 ? CYS D 1028 ? ALA A 1010 CYS A 1025 1 ? 16 
HELX_P HELX_P46 AF1 ASN D 1093 ? PHE D 1104 ? ASN A 1090 PHE A 1101 1 ? 12 
HELX_P HELX_P47 AF2 TYR D 1180 ? LYS D 1192 ? TYR A 1177 LYS A 1189 1 ? 13 
HELX_P HELX_P48 AF3 ILE D 1202 ? ASP D 1210 ? ILE A 1199 ASP A 1207 1 ? 9  
HELX_P HELX_P49 AF4 ASP D 1211 ? GLN D 1227 ? ASP A 1208 GLN A 1224 1 ? 17 
HELX_P HELX_P50 AF5 ARG D 1255 ? GLN D 1257 ? ARG A 1252 GLN A 1254 5 ? 3  
HELX_P HELX_P51 AF6 ASP D 1264 ? SER D 1287 ? ASP A 1261 SER A 1284 1 ? 24 
HELX_P HELX_P52 AF7 SER D 1297 ? ASN D 1310 ? SER A 1294 ASN A 1307 1 ? 14 
# 
_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 
covale1  covale both ? A DG  6  "O3'" ? ? ? 1_555 A 2YR 7   P  ? ? C DG  6  C 2YR 7   1_555 ? ? ? ? ? ? ?                    1.607 
? ? 
covale2  covale both ? A 2YR 7  "O3'" ? ? ? 1_555 A DT  8   P  ? ? C 2YR 7  C DT  8   1_555 ? ? ? ? ? ? ?                    1.605 
? ? 
covale3  covale one  ? A 2YR 7  S     ? ? ? 1_555 D CYS 554 SG ? ? C 2YR 7  A CYS 551 1_555 ? ? ? ? ? ? ?                    2.034 
? ? 
hydrog1  hydrog ?    ? B A   5  N6    ? ? ? 1_555 B U   13  O2 ? ? B A   5  B U   13  1_555 ? ? ? ? ? ? 'REVERSED HOOGSTEEN' ?     
? ? 
hydrog2  hydrog ?    ? B A   5  N7    ? ? ? 1_555 B U   13  N3 ? ? B A   5  B U   13  1_555 ? ? ? ? ? ? 'REVERSED HOOGSTEEN' ?     
? ? 
hydrog3  hydrog ?    ? B U   7  N3    ? ? ? 1_555 B U   22  O2 ? ? B U   7  B U   22  1_555 ? ? ? ? ? ? TYPE_16_PAIR         ?     
? ? 
hydrog4  hydrog ?    ? B U   7  O4    ? ? ? 1_555 B U   22  N3 ? ? B U   7  B U   22  1_555 ? ? ? ? ? ? TYPE_16_PAIR         ?     
? ? 
hydrog5  hydrog ?    ? B U   8  N3    ? ? ? 1_555 B A   21  N1 ? ? B U   8  B A   21  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog6  hydrog ?    ? B U   8  O4    ? ? ? 1_555 B A   21  N6 ? ? B U   8  B A   21  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog7  hydrog ?    ? B C   9  N3    ? ? ? 1_555 B G   20  N1 ? ? B C   9  B G   20  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog8  hydrog ?    ? B C   9  N4    ? ? ? 1_555 B G   20  O6 ? ? B C   9  B G   20  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog9  hydrog ?    ? B C   9  O2    ? ? ? 1_555 B G   20  N2 ? ? B C   9  B G   20  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog10 hydrog ?    ? B U   10 N3    ? ? ? 1_555 B A   19  N1 ? ? B U   10 B A   19  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog11 hydrog ?    ? B U   10 O4    ? ? ? 1_555 B A   19  N6 ? ? B U   10 B A   19  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog12 hydrog ?    ? B A   11 N1    ? ? ? 1_555 B U   18  N3 ? ? B A   11 B U   18  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog13 hydrog ?    ? B A   11 N6    ? ? ? 1_555 B U   18  O4 ? ? B A   11 B U   18  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog14 hydrog ?    ? B C   12 N3    ? ? ? 1_555 B G   17  N1 ? ? B C   12 B G   17  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog15 hydrog ?    ? B C   12 N4    ? ? ? 1_555 B G   17  O6 ? ? B C   12 B G   17  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog16 hydrog ?    ? B C   12 O2    ? ? ? 1_555 B G   17  N2 ? ? B C   12 B G   17  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog17 hydrog ?    ? A DT  2  N3    ? ? ? 1_555 C DA  30  N1 ? ? C DT  2  D DA  30  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog18 hydrog ?    ? A DT  2  O4    ? ? ? 1_555 C DA  30  N6 ? ? C DT  2  D DA  30  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog19 hydrog ?    ? A DA  3  N1    ? ? ? 1_555 C DT  29  N3 ? ? C DA  3  D DT  29  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog20 hydrog ?    ? A DA  3  N6    ? ? ? 1_555 C DT  29  O4 ? ? C DA  3  D DT  29  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog21 hydrog ?    ? A DG  4  N1    ? ? ? 1_555 C DC  28  N3 ? ? C DG  4  D DC  28  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog22 hydrog ?    ? A DG  4  N2    ? ? ? 1_555 C DC  28  O2 ? ? C DG  4  D DC  28  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog23 hydrog ?    ? A DG  4  O6    ? ? ? 1_555 C DC  28  N4 ? ? C DG  4  D DC  28  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog24 hydrog ?    ? A DT  5  N3    ? ? ? 1_555 C DA  27  N1 ? ? C DT  5  D DA  27  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog25 hydrog ?    ? A DT  5  O4    ? ? ? 1_555 C DA  27  N6 ? ? C DT  5  D DA  27  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog26 hydrog ?    ? A DG  6  N1    ? ? ? 1_555 C DC  26  N3 ? ? C DG  6  D DC  26  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog27 hydrog ?    ? A DG  6  N2    ? ? ? 1_555 C DC  26  O2 ? ? C DG  6  D DC  26  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog28 hydrog ?    ? A DG  6  O6    ? ? ? 1_555 C DC  26  N4 ? ? C DG  6  D DC  26  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog29 hydrog ?    ? A DT  8  N3    ? ? ? 1_555 C DA  24  N1 ? ? C DT  8  D DA  24  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog30 hydrog ?    ? A DT  8  O4    ? ? ? 1_555 C DA  24  N6 ? ? C DT  8  D DA  24  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog31 hydrog ?    ? A DT  9  N3    ? ? ? 1_555 C DA  23  N1 ? ? C DT  9  D DA  23  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog32 hydrog ?    ? A DT  9  O4    ? ? ? 1_555 C DA  23  N6 ? ? C DT  9  D DA  23  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog33 hydrog ?    ? A DT  10 N3    ? ? ? 1_555 C DA  22  N1 ? ? C DT  10 D DA  22  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog34 hydrog ?    ? A DT  10 O4    ? ? ? 1_555 C DA  22  N6 ? ? C DT  10 D DA  22  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog35 hydrog ?    ? A DG  11 N1    ? ? ? 1_555 C DC  21  N3 ? ? C DG  11 D DC  21  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog36 hydrog ?    ? A DG  11 N2    ? ? ? 1_555 C DC  21  O2 ? ? C DG  11 D DC  21  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog37 hydrog ?    ? A DG  11 O6    ? ? ? 1_555 C DC  21  N4 ? ? C DG  11 D DC  21  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog38 hydrog ?    ? A DT  12 N3    ? ? ? 1_555 C DA  20  N1 ? ? C DT  12 D DA  20  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog39 hydrog ?    ? A DT  12 O4    ? ? ? 1_555 C DA  20  N6 ? ? C DT  12 D DA  20  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog40 hydrog ?    ? A DC  13 N3    ? ? ? 1_555 C DG  19  N1 ? ? C DC  13 D DG  19  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog41 hydrog ?    ? A DC  13 N4    ? ? ? 1_555 C DG  19  O6 ? ? C DC  13 D DG  19  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog42 hydrog ?    ? A DC  13 O2    ? ? ? 1_555 C DG  19  N2 ? ? C DC  13 D DG  19  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog43 hydrog ?    ? A DG  14 N1    ? ? ? 1_555 C DC  18  N3 ? ? C DG  14 D DC  18  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog44 hydrog ?    ? A DG  14 N2    ? ? ? 1_555 C DC  18  O2 ? ? C DG  14 D DC  18  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog45 hydrog ?    ? A DG  14 O6    ? ? ? 1_555 C DC  18  N4 ? ? C DG  14 D DC  18  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog46 hydrog ?    ? A DT  15 N3    ? ? ? 1_555 C DA  17  N1 ? ? C DT  15 D DA  17  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog47 hydrog ?    ? A DT  15 O4    ? ? ? 1_555 C DA  17  N6 ? ? C DT  15 D DA  17  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog48 hydrog ?    ? A DC  16 N3    ? ? ? 1_555 C DG  16  N1 ? ? C DC  16 D DG  16  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog49 hydrog ?    ? A DC  16 N4    ? ? ? 1_555 C DG  16  O6 ? ? C DC  16 D DG  16  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog50 hydrog ?    ? A DC  16 O2    ? ? ? 1_555 C DG  16  N2 ? ? C DC  16 D DG  16  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog51 hydrog ?    ? A DT  17 N3    ? ? ? 1_555 C DA  15  N1 ? ? C DT  17 D DA  15  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog52 hydrog ?    ? A DT  17 O4    ? ? ? 1_555 C DA  15  N6 ? ? C DT  17 D DA  15  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog53 hydrog ?    ? A DC  18 N3    ? ? ? 1_555 C DG  14  N1 ? ? C DC  18 D DG  14  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog54 hydrog ?    ? A DC  18 N4    ? ? ? 1_555 C DG  14  O6 ? ? C DC  18 D DG  14  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog55 hydrog ?    ? A DC  18 O2    ? ? ? 1_555 C DG  14  N2 ? ? C DC  18 D DG  14  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog56 hydrog ?    ? A DA  19 N1    ? ? ? 1_555 C DT  13  N3 ? ? C DA  19 D DT  13  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog57 hydrog ?    ? A DA  19 N6    ? ? ? 1_555 C DT  13  O4 ? ? C DA  19 D DT  13  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog58 hydrog ?    ? A DT  20 N3    ? ? ? 1_555 C DA  12  N1 ? ? C DT  20 D DA  12  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog59 hydrog ?    ? A DT  20 O4    ? ? ? 1_555 C DA  12  N6 ? ? C DT  20 D DA  12  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog60 hydrog ?    ? A DC  21 N3    ? ? ? 1_555 C DG  11  N1 ? ? C DC  21 D DG  11  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog61 hydrog ?    ? A DC  21 N4    ? ? ? 1_555 C DG  11  O6 ? ? C DC  21 D DG  11  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog62 hydrog ?    ? A DC  21 O2    ? ? ? 1_555 C DG  11  N2 ? ? C DC  21 D DG  11  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog63 hydrog ?    ? A DT  22 N3    ? ? ? 1_555 C DA  10  N1 ? ? C DT  22 D DA  10  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
hydrog64 hydrog ?    ? A DT  22 O4    ? ? ? 1_555 C DA  10  N6 ? ? C DT  22 D DA  10  1_555 ? ? ? ? ? ? WATSON-CRICK         ?     
? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
hydrog ? ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      2YR 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       7 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     D 
_pdbx_modification_feature.modified_residue_label_seq_id      554 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       2YR 
_pdbx_modification_feature.auth_asym_id                       C 
_pdbx_modification_feature.auth_seq_id                        7 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       551 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               S 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                CYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        2YR 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
AA8 ? 6 ? 
AA9 ? 3 ? 
AB1 ? 2 ? 
AB2 ? 2 ? 
AB3 ? 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 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? parallel      
AA8 4 5 ? parallel      
AA8 5 6 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 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 PHE D 534  ? LYS D 535  ? PHE A 531  LYS A 532  
AA1 2 GLU D 789  ? ARG D 793  ? GLU A 786  ARG A 790  
AA1 3 LYS D 871  ? LEU D 880  ? LYS A 868  LEU A 877  
AA1 4 VAL D 16   ? PRO D 26   ? VAL A 13   PRO A 23   
AA1 5 TYR D 744  ? TYR D 749  ? TYR A 741  TYR A 746  
AA1 6 LEU D 565  ? ILE D 570  ? LEU A 562  ILE A 567  
AA1 7 ILE D 558  ? LYS D 562  ? ILE A 555  LYS A 559  
AA2 1 PHE D 534  ? LYS D 535  ? PHE A 531  LYS A 532  
AA2 2 GLU D 789  ? ARG D 793  ? GLU A 786  ARG A 790  
AA2 3 LYS D 871  ? LEU D 880  ? LYS A 868  LEU A 877  
AA2 4 ILE D 782  ? LEU D 784  ? ILE A 779  LEU A 781  
AA3 1 PHE D 368  ? ILE D 369  ? PHE A 365  ILE A 366  
AA3 2 ILE D 421  ? ASN D 422  ? ILE A 418  ASN A 419  
AA4 1 GLY D 592  ? ASP D 599  ? GLY A 589  ASP A 596  
AA4 2 HIS D 723  ? ALA D 730  ? HIS A 720  ALA A 727  
AA5 1 ILE D 629  ? LEU D 631  ? ILE A 626  LEU A 628  
AA5 2 LEU D 639  ? ILE D 641  ? LEU A 636  ILE A 638  
AA6 1 ALA D 802  ? HIS D 803  ? ALA A 799  HIS A 800  
AA6 2 ILE D 861  ? ILE D 862  ? ILE A 858  ILE A 859  
AA7 1 LYS D 808  ? LEU D 814  ? LYS A 805  LEU A 811  
AA7 2 VAL D 852  ? GLU D 856  ? VAL A 849  GLU A 853  
AA8 1 ILE D 929  ? SER D 934  ? ILE A 926  SER A 931  
AA8 2 TYR D 919  ? ILE D 923  ? TYR A 916  ILE A 920  
AA8 3 ILE D 907  ? ASP D 911  ? ILE A 904  ASP A 908  
AA8 4 VAL D 992  ? ASN D 997  ? VAL A 989  ASN A 994  
AA8 5 LEU D 1065 ? PRO D 1069 ? LEU A 1062 PRO A 1066 
AA8 6 GLN D 1061 ? SER D 1062 ? GLN A 1058 SER A 1059 
AA9 1 PHE D 1106 ? ASP D 1110 ? PHE A 1103 ASP A 1107 
AA9 2 ASP D 1115 ? LYS D 1121 ? ASP A 1112 LYS A 1118 
AA9 3 ALA D 1138 ? PHE D 1143 ? ALA A 1135 PHE A 1140 
AB1 1 THR D 1148 ? PHE D 1150 ? THR A 1145 PHE A 1147 
AB1 2 PRO D 1156 ? ILE D 1158 ? PRO A 1153 ILE A 1155 
AB2 1 ARG D 1162 ? VAL D 1164 ? ARG A 1159 VAL A 1161 
AB2 2 ARG D 1177 ? LEU D 1179 ? ARG A 1174 LEU A 1176 
AB3 1 ARG D 1229 ? ASN D 1232 ? ARG A 1226 ASN A 1229 
AB3 2 GLU D 1237 ? ARG D 1245 ? GLU A 1234 ARG A 1242 
AB3 3 CYS D 1251 ? ASP D 1253 ? CYS A 1248 ASP A 1250 
# 
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 PHE D 534  ? N PHE A 531  O TYR D 792  ? O TYR A 789  
AA1 2 3 N GLU D 789  ? N GLU A 786  O HIS D 875  ? O HIS A 872  
AA1 3 4 O ILE D 878  ? O ILE A 875  N LYS D 18   ? N LYS A 15   
AA1 4 5 N GLU D 23   ? N GLU A 20   O TYR D 749  ? O TYR A 746  
AA1 5 6 O PHE D 746  ? O PHE A 743  N LEU D 568  ? N LEU A 565  
AA1 6 7 O GLY D 569  ? O GLY A 566  N ILE D 558  ? N ILE A 555  
AA2 1 2 N PHE D 534  ? N PHE A 531  O TYR D 792  ? O TYR A 789  
AA2 2 3 N GLU D 789  ? N GLU A 786  O HIS D 875  ? O HIS A 872  
AA2 3 4 O THR D 879  ? O THR A 876  N LYS D 783  ? N LYS A 780  
AA3 1 2 N ILE D 369  ? N ILE A 366  O ILE D 421  ? O ILE A 418  
AA4 1 2 N TYR D 597  ? N TYR A 594  O SER D 725  ? O SER A 722  
AA5 1 2 N ILE D 629  ? N ILE A 626  O ILE D 641  ? O ILE A 638  
AA6 1 2 N HIS D 803  ? N HIS A 800  O ILE D 861  ? O ILE A 858  
AA7 1 2 N MET D 809  ? N MET A 806  O LYS D 855  ? O LYS A 852  
AA8 1 2 O LEU D 930  ? O LEU A 927  N VAL D 922  ? N VAL A 919  
AA8 2 3 O ILE D 923  ? O ILE A 920  N ILE D 907  ? N ILE A 904  
AA8 3 4 N ILE D 908  ? N ILE A 905  O VAL D 994  ? O VAL A 991  
AA8 4 5 N LEU D 995  ? N LEU A 992  O PHE D 1066 ? O PHE A 1063 
AA8 5 6 O LEU D 1065 ? O LEU A 1062 N SER D 1062 ? N SER A 1059 
AA9 1 2 N ASP D 1110 ? N ASP A 1107 O ASP D 1115 ? O ASP A 1112 
AA9 2 3 N PHE D 1120 ? N PHE A 1117 O TRP D 1139 ? O TRP A 1136 
AB1 1 2 N GLN D 1149 ? N GLN A 1146 O PHE D 1157 ? O PHE A 1154 
AB2 1 2 N ARG D 1162 ? N ARG A 1159 O LEU D 1179 ? O LEU A 1176 
AB3 1 2 N ASN D 1232 ? N ASN A 1229 O GLU D 1237 ? O GLU A 1234 
AB3 2 3 N SER D 1242 ? N SER A 1239 O PHE D 1252 ? O PHE A 1249 
# 
_pdbx_entry_details.entry_id                   9CJI 
_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     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             "C3'" 
_pdbx_validate_rmsd_angle.auth_asym_id_1             C 
_pdbx_validate_rmsd_angle.auth_comp_id_1             DG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              4 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             "C2'" 
_pdbx_validate_rmsd_angle.auth_asym_id_2             C 
_pdbx_validate_rmsd_angle.auth_comp_id_2             DG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              4 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             "C1'" 
_pdbx_validate_rmsd_angle.auth_asym_id_3             C 
_pdbx_validate_rmsd_angle.auth_comp_id_3             DG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              4 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                97.53 
_pdbx_validate_rmsd_angle.angle_target_value         102.40 
_pdbx_validate_rmsd_angle.angle_deviation            -4.87 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.80 
_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 LYS A 87   ? ? -91.73  49.51   
2  1 ARG A 113  ? ? -144.54 36.90   
3  1 LYS A 134  ? ? -153.84 -159.72 
4  1 SER A 170  ? ? -54.97  -71.15  
5  1 PRO A 525  ? ? -69.63  5.27    
6  1 ASP A 694  ? ? 33.23   55.56   
7  1 ASN A 747  ? ? -142.51 32.34   
8  1 LYS A 748  ? ? 71.99   -8.83   
9  1 LYS A 796  ? ? -160.36 112.66  
10 1 ALA A 1007 ? ? -68.42  -179.89 
11 1 LYS A 1009 ? ? 68.16   -5.74   
12 1 MET A 1133 ? ? 57.27   73.78   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9CJI 
_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                    9CJI 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.4 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               27147 
_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 
# 
loop_
_em_entity_assembly.id 
_em_entity_assembly.parent_id 
_em_entity_assembly.source 
_em_entity_assembly.type 
_em_entity_assembly.name 
_em_entity_assembly.details 
_em_entity_assembly.synonym 
_em_entity_assembly.oligomeric_details 
_em_entity_assembly.entity_id_list 
1 0 'MULTIPLE SOURCES' COMPLEX 'Cas12a:gRNA:DNA (Acidaminococcus sp.) with 0 RNA:DNA base pairs, structure 2' ? ? ? 2,3,4 
2 1 RECOMBINANT        COMPLEX Cas12a                                                                         ? ? ? 4     
3 1 SYNTHETIC          COMPLEX gRNA:DNA                                                                       ? ? ? 2,3   
# 
_em_imaging.entry_id                        9CJI 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TALOS ARCTICA' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            200 
_em_imaging.illumination_mode               OTHER 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             800 
_em_imaging.nominal_defocus_max             2000 
_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                         NITROGEN 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    COPPER 
_em_sample_support.grid_mesh_size   400 
_em_sample_support.grid_type        C-flat-1.2/1.3 
_em_sample_support.details          '25 mA' 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9CJI 
_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   281 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9CJI 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
_em_single_particle_entity.entry_id              9CJI 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C1 
# 
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 C DG  1   ? A DG  1   
2   1 Y 1 C DG  23  ? A DG  23  
3   1 Y 1 C DT  24  ? A DT  24  
4   1 Y 1 C DA  25  ? A DA  25  
5   1 Y 1 C DT  26  ? A DT  26  
6   1 Y 1 C DG  27  ? A DG  27  
7   1 Y 1 C DC  28  ? A DC  28  
8   1 Y 1 C DG  29  ? A DG  29  
9   1 Y 1 C DT  30  ? A DT  30  
10  1 Y 1 C DC  31  ? A DC  31  
11  1 Y 1 B U   1   ? B U   1   
12  1 Y 1 B U   2   ? B U   2   
13  1 Y 1 B U   3   ? B U   3   
14  1 Y 1 B G   29  ? B G   29  
15  1 Y 1 B U   30  ? B U   30  
16  1 Y 1 B A   31  ? B A   31  
17  1 Y 1 B G   32  ? B G   32  
18  1 Y 1 B A   33  ? B A   33  
19  1 Y 1 B C   34  ? B C   34  
20  1 Y 1 B A   35  ? B A   35  
21  1 Y 1 B U   36  ? B U   36  
22  1 Y 1 B A   37  ? B A   37  
23  1 Y 1 B C   38  ? B C   38  
24  1 Y 1 B G   39  ? B G   39  
25  1 Y 1 B C   40  ? B C   40  
26  1 Y 1 B A   41  ? B A   41  
27  1 Y 1 B G   42  ? B G   42  
28  1 Y 1 D DG  1   ? C DG  1   
29  1 Y 1 D DA  2   ? C DA  2   
30  1 Y 1 D DC  3   ? C DC  3   
31  1 Y 1 D DG  4   ? C DG  4   
32  1 Y 1 D DC  5   ? C DC  5   
33  1 Y 1 D DA  6   ? C DA  6   
34  1 Y 1 D DT  7   ? C DT  7   
35  1 Y 1 D DA  8   ? C DA  8   
36  1 Y 1 D DC  9   ? C DC  9   
37  1 Y 1 D DC  31  ? C DC  31  
38  1 Y 1 A SER -2  ? D SER 1   
39  1 Y 1 A ASN -1  ? D ASN 2   
40  1 Y 1 A ALA 0   ? D ALA 3   
41  1 Y 1 A MET 1   ? D MET 4   
42  1 Y 1 A GLY 147 ? D GLY 150 
43  1 Y 1 A THR 148 ? D THR 151 
44  1 Y 1 A VAL 149 ? D VAL 152 
45  1 Y 1 A ILE 265 ? D ILE 268 
46  1 Y 1 A SER 266 ? D SER 269 
47  1 Y 1 A ARG 267 ? D ARG 270 
48  1 Y 1 A GLU 268 ? D GLU 271 
49  1 Y 1 A ALA 269 ? D ALA 272 
50  1 Y 1 A GLY 270 ? D GLY 273 
51  1 Y 1 A THR 271 ? D THR 274 
52  1 Y 1 A GLU 272 ? D GLU 275 
53  1 Y 1 A LYS 273 ? D LYS 276 
54  1 Y 1 A ILE 274 ? D ILE 277 
55  1 Y 1 A LYS 275 ? D LYS 278 
56  1 Y 1 A GLY 276 ? D GLY 279 
57  1 Y 1 A LEU 277 ? D LEU 280 
58  1 Y 1 A ASN 278 ? D ASN 281 
59  1 Y 1 A GLU 279 ? D GLU 282 
60  1 Y 1 A VAL 280 ? D VAL 283 
61  1 Y 1 A LEU 281 ? D LEU 284 
62  1 Y 1 A ASN 282 ? D ASN 285 
63  1 Y 1 A LEU 283 ? D LEU 286 
64  1 Y 1 A ALA 284 ? D ALA 287 
65  1 Y 1 A ILE 285 ? D ILE 288 
66  1 Y 1 A GLN 286 ? D GLN 289 
67  1 Y 1 A LYS 287 ? D LYS 290 
68  1 Y 1 A ASN 288 ? D ASN 291 
69  1 Y 1 A ASP 289 ? D ASP 292 
70  1 Y 1 A GLU 290 ? D GLU 293 
71  1 Y 1 A THR 291 ? D THR 294 
72  1 Y 1 A ALA 292 ? D ALA 295 
73  1 Y 1 A HIS 293 ? D HIS 296 
74  1 Y 1 A ILE 294 ? D ILE 297 
75  1 Y 1 A ILE 295 ? D ILE 298 
76  1 Y 1 A ALA 296 ? D ALA 299 
77  1 Y 1 A SER 297 ? D SER 300 
78  1 Y 1 A LEU 298 ? D LEU 301 
79  1 Y 1 A PRO 299 ? D PRO 302 
80  1 Y 1 A HIS 300 ? D HIS 303 
81  1 Y 1 A ARG 301 ? D ARG 304 
82  1 Y 1 A PHE 302 ? D PHE 305 
83  1 Y 1 A ILE 303 ? D ILE 306 
84  1 Y 1 A PRO 304 ? D PRO 307 
85  1 Y 1 A LEU 305 ? D LEU 308 
86  1 Y 1 A PHE 306 ? D PHE 309 
87  1 Y 1 A LYS 307 ? D LYS 310 
88  1 Y 1 A GLN 308 ? D GLN 311 
89  1 Y 1 A ILE 309 ? D ILE 312 
90  1 Y 1 A LEU 310 ? D LEU 313 
91  1 Y 1 A SER 311 ? D SER 314 
92  1 Y 1 A ASP 312 ? D ASP 315 
93  1 Y 1 A ARG 313 ? D ARG 316 
94  1 Y 1 A ASN 314 ? D ASN 317 
95  1 Y 1 A THR 315 ? D THR 318 
96  1 Y 1 A LEU 316 ? D LEU 319 
97  1 Y 1 A SER 317 ? D SER 320 
98  1 Y 1 A PHE 318 ? D PHE 321 
99  1 Y 1 A ILE 319 ? D ILE 322 
100 1 Y 1 A LEU 320 ? D LEU 323 
101 1 Y 1 A GLU 321 ? D GLU 324 
102 1 Y 1 A GLU 322 ? D GLU 325 
103 1 Y 1 A PHE 323 ? D PHE 326 
# 
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 
2YR P      P N N 1   
2YR OP1    O N N 2   
2YR OP2    O N N 3   
2YR "O5'"  O N N 4   
2YR "C5'"  C N N 5   
2YR "C4'"  C N R 6   
2YR "O4'"  O N N 7   
2YR "C3'"  C N S 8   
2YR "O3'"  O N N 9   
2YR "C2'"  C N N 10  
2YR "C1'"  C N R 11  
2YR N1     N N N 12  
2YR C2     C N N 13  
2YR O2     O N N 14  
2YR N3     N N N 15  
2YR C4     C N N 16  
2YR N4     N N N 17  
2YR C5     C N N 18  
2YR C6     C N N 19  
2YR S      S N N 20  
2YR C8     C N N 21  
2YR C9     C N N 22  
2YR H2     H N N 23  
2YR H3     H N N 24  
2YR H4     H N N 25  
2YR H5     H N N 26  
2YR H6     H N N 27  
2YR H7     H N N 28  
2YR H8     H N N 29  
2YR H9     H N N 30  
2YR H10    H N N 31  
2YR H11    H N N 32  
2YR H12    H N N 33  
2YR H13    H N N 34  
2YR H14    H N N 35  
2YR H15    H N N 36  
2YR H16    H N N 37  
2YR H17    H N N 38  
2YR H18    H N N 39  
2YR OP3    O N N 40  
2YR H20    H N N 41  
A   OP3    O N N 42  
A   P      P N N 43  
A   OP1    O N N 44  
A   OP2    O N N 45  
A   "O5'"  O N N 46  
A   "C5'"  C N N 47  
A   "C4'"  C N R 48  
A   "O4'"  O N N 49  
A   "C3'"  C N S 50  
A   "O3'"  O N N 51  
A   "C2'"  C N R 52  
A   "O2'"  O N N 53  
A   "C1'"  C N R 54  
A   N9     N Y N 55  
A   C8     C Y N 56  
A   N7     N Y N 57  
A   C5     C Y N 58  
A   C6     C Y N 59  
A   N6     N N N 60  
A   N1     N Y N 61  
A   C2     C Y N 62  
A   N3     N Y N 63  
A   C4     C Y N 64  
A   HOP3   H N N 65  
A   HOP2   H N N 66  
A   "H5'"  H N N 67  
A   "H5''" H N N 68  
A   "H4'"  H N N 69  
A   "H3'"  H N N 70  
A   "HO3'" H N N 71  
A   "H2'"  H N N 72  
A   "HO2'" H N N 73  
A   "H1'"  H N N 74  
A   H8     H N N 75  
A   H61    H N N 76  
A   H62    H N N 77  
A   H2     H N N 78  
ALA N      N N N 79  
ALA CA     C N S 80  
ALA C      C N N 81  
ALA O      O N N 82  
ALA CB     C N N 83  
ALA OXT    O N N 84  
ALA H      H N N 85  
ALA H2     H N N 86  
ALA HA     H N N 87  
ALA HB1    H N N 88  
ALA HB2    H N N 89  
ALA HB3    H N N 90  
ALA HXT    H N N 91  
ARG N      N N N 92  
ARG CA     C N S 93  
ARG C      C N N 94  
ARG O      O N N 95  
ARG CB     C N N 96  
ARG CG     C N N 97  
ARG CD     C N N 98  
ARG NE     N N N 99  
ARG CZ     C N N 100 
ARG NH1    N N N 101 
ARG NH2    N N N 102 
ARG OXT    O N N 103 
ARG H      H N N 104 
ARG H2     H N N 105 
ARG HA     H N N 106 
ARG HB2    H N N 107 
ARG HB3    H N N 108 
ARG HG2    H N N 109 
ARG HG3    H N N 110 
ARG HD2    H N N 111 
ARG HD3    H N N 112 
ARG HE     H N N 113 
ARG HH11   H N N 114 
ARG HH12   H N N 115 
ARG HH21   H N N 116 
ARG HH22   H N N 117 
ARG HXT    H N N 118 
ASN N      N N N 119 
ASN CA     C N S 120 
ASN C      C N N 121 
ASN O      O N N 122 
ASN CB     C N N 123 
ASN CG     C N N 124 
ASN OD1    O N N 125 
ASN ND2    N N N 126 
ASN OXT    O N N 127 
ASN H      H N N 128 
ASN H2     H N N 129 
ASN HA     H N N 130 
ASN HB2    H N N 131 
ASN HB3    H N N 132 
ASN HD21   H N N 133 
ASN HD22   H N N 134 
ASN HXT    H N N 135 
ASP N      N N N 136 
ASP CA     C N S 137 
ASP C      C N N 138 
ASP O      O N N 139 
ASP CB     C N N 140 
ASP CG     C N N 141 
ASP OD1    O N N 142 
ASP OD2    O N N 143 
ASP OXT    O N N 144 
ASP H      H N N 145 
ASP H2     H N N 146 
ASP HA     H N N 147 
ASP HB2    H N N 148 
ASP HB3    H N N 149 
ASP HD2    H N N 150 
ASP HXT    H N N 151 
C   OP3    O N N 152 
C   P      P N N 153 
C   OP1    O N N 154 
C   OP2    O N N 155 
C   "O5'"  O N N 156 
C   "C5'"  C N N 157 
C   "C4'"  C N R 158 
C   "O4'"  O N N 159 
C   "C3'"  C N S 160 
C   "O3'"  O N N 161 
C   "C2'"  C N R 162 
C   "O2'"  O N N 163 
C   "C1'"  C N R 164 
C   N1     N N N 165 
C   C2     C N N 166 
C   O2     O N N 167 
C   N3     N N N 168 
C   C4     C N N 169 
C   N4     N N N 170 
C   C5     C N N 171 
C   C6     C N N 172 
C   HOP3   H N N 173 
C   HOP2   H N N 174 
C   "H5'"  H N N 175 
C   "H5''" H N N 176 
C   "H4'"  H N N 177 
C   "H3'"  H N N 178 
C   "HO3'" H N N 179 
C   "H2'"  H N N 180 
C   "HO2'" H N N 181 
C   "H1'"  H N N 182 
C   H41    H N N 183 
C   H42    H N N 184 
C   H5     H N N 185 
C   H6     H N N 186 
CYS N      N N N 187 
CYS CA     C N R 188 
CYS C      C N N 189 
CYS O      O N N 190 
CYS CB     C N N 191 
CYS SG     S N N 192 
CYS OXT    O N N 193 
CYS H      H N N 194 
CYS H2     H N N 195 
CYS HA     H N N 196 
CYS HB2    H N N 197 
CYS HB3    H N N 198 
CYS HG     H N N 199 
CYS HXT    H N N 200 
DA  OP3    O N N 201 
DA  P      P N N 202 
DA  OP1    O N N 203 
DA  OP2    O N N 204 
DA  "O5'"  O N N 205 
DA  "C5'"  C N N 206 
DA  "C4'"  C N R 207 
DA  "O4'"  O N N 208 
DA  "C3'"  C N S 209 
DA  "O3'"  O N N 210 
DA  "C2'"  C N N 211 
DA  "C1'"  C N R 212 
DA  N9     N Y N 213 
DA  C8     C Y N 214 
DA  N7     N Y N 215 
DA  C5     C Y N 216 
DA  C6     C Y N 217 
DA  N6     N N N 218 
DA  N1     N Y N 219 
DA  C2     C Y N 220 
DA  N3     N Y N 221 
DA  C4     C Y N 222 
DA  HOP3   H N N 223 
DA  HOP2   H N N 224 
DA  "H5'"  H N N 225 
DA  "H5''" H N N 226 
DA  "H4'"  H N N 227 
DA  "H3'"  H N N 228 
DA  "HO3'" H N N 229 
DA  "H2'"  H N N 230 
DA  "H2''" H N N 231 
DA  "H1'"  H N N 232 
DA  H8     H N N 233 
DA  H61    H N N 234 
DA  H62    H N N 235 
DA  H2     H N N 236 
DC  OP3    O N N 237 
DC  P      P N N 238 
DC  OP1    O N N 239 
DC  OP2    O N N 240 
DC  "O5'"  O N N 241 
DC  "C5'"  C N N 242 
DC  "C4'"  C N R 243 
DC  "O4'"  O N N 244 
DC  "C3'"  C N S 245 
DC  "O3'"  O N N 246 
DC  "C2'"  C N N 247 
DC  "C1'"  C N R 248 
DC  N1     N N N 249 
DC  C2     C N N 250 
DC  O2     O N N 251 
DC  N3     N N N 252 
DC  C4     C N N 253 
DC  N4     N N N 254 
DC  C5     C N N 255 
DC  C6     C N N 256 
DC  HOP3   H N N 257 
DC  HOP2   H N N 258 
DC  "H5'"  H N N 259 
DC  "H5''" H N N 260 
DC  "H4'"  H N N 261 
DC  "H3'"  H N N 262 
DC  "HO3'" H N N 263 
DC  "H2'"  H N N 264 
DC  "H2''" H N N 265 
DC  "H1'"  H N N 266 
DC  H41    H N N 267 
DC  H42    H N N 268 
DC  H5     H N N 269 
DC  H6     H N N 270 
DG  OP3    O N N 271 
DG  P      P N N 272 
DG  OP1    O N N 273 
DG  OP2    O N N 274 
DG  "O5'"  O N N 275 
DG  "C5'"  C N N 276 
DG  "C4'"  C N R 277 
DG  "O4'"  O N N 278 
DG  "C3'"  C N S 279 
DG  "O3'"  O N N 280 
DG  "C2'"  C N N 281 
DG  "C1'"  C N R 282 
DG  N9     N Y N 283 
DG  C8     C Y N 284 
DG  N7     N Y N 285 
DG  C5     C Y N 286 
DG  C6     C N N 287 
DG  O6     O N N 288 
DG  N1     N N N 289 
DG  C2     C N N 290 
DG  N2     N N N 291 
DG  N3     N N N 292 
DG  C4     C Y N 293 
DG  HOP3   H N N 294 
DG  HOP2   H N N 295 
DG  "H5'"  H N N 296 
DG  "H5''" H N N 297 
DG  "H4'"  H N N 298 
DG  "H3'"  H N N 299 
DG  "HO3'" H N N 300 
DG  "H2'"  H N N 301 
DG  "H2''" H N N 302 
DG  "H1'"  H N N 303 
DG  H8     H N N 304 
DG  H1     H N N 305 
DG  H21    H N N 306 
DG  H22    H N N 307 
DT  OP3    O N N 308 
DT  P      P N N 309 
DT  OP1    O N N 310 
DT  OP2    O N N 311 
DT  "O5'"  O N N 312 
DT  "C5'"  C N N 313 
DT  "C4'"  C N R 314 
DT  "O4'"  O N N 315 
DT  "C3'"  C N S 316 
DT  "O3'"  O N N 317 
DT  "C2'"  C N N 318 
DT  "C1'"  C N R 319 
DT  N1     N N N 320 
DT  C2     C N N 321 
DT  O2     O N N 322 
DT  N3     N N N 323 
DT  C4     C N N 324 
DT  O4     O N N 325 
DT  C5     C N N 326 
DT  C7     C N N 327 
DT  C6     C N N 328 
DT  HOP3   H N N 329 
DT  HOP2   H N N 330 
DT  "H5'"  H N N 331 
DT  "H5''" H N N 332 
DT  "H4'"  H N N 333 
DT  "H3'"  H N N 334 
DT  "HO3'" H N N 335 
DT  "H2'"  H N N 336 
DT  "H2''" H N N 337 
DT  "H1'"  H N N 338 
DT  H3     H N N 339 
DT  H71    H N N 340 
DT  H72    H N N 341 
DT  H73    H N N 342 
DT  H6     H N N 343 
G   OP3    O N N 344 
G   P      P N N 345 
G   OP1    O N N 346 
G   OP2    O N N 347 
G   "O5'"  O N N 348 
G   "C5'"  C N N 349 
G   "C4'"  C N R 350 
G   "O4'"  O N N 351 
G   "C3'"  C N S 352 
G   "O3'"  O N N 353 
G   "C2'"  C N R 354 
G   "O2'"  O N N 355 
G   "C1'"  C N R 356 
G   N9     N Y N 357 
G   C8     C Y N 358 
G   N7     N Y N 359 
G   C5     C Y N 360 
G   C6     C N N 361 
G   O6     O N N 362 
G   N1     N N N 363 
G   C2     C N N 364 
G   N2     N N N 365 
G   N3     N N N 366 
G   C4     C Y N 367 
G   HOP3   H N N 368 
G   HOP2   H N N 369 
G   "H5'"  H N N 370 
G   "H5''" H N N 371 
G   "H4'"  H N N 372 
G   "H3'"  H N N 373 
G   "HO3'" H N N 374 
G   "H2'"  H N N 375 
G   "HO2'" H N N 376 
G   "H1'"  H N N 377 
G   H8     H N N 378 
G   H1     H N N 379 
G   H21    H N N 380 
G   H22    H N N 381 
GLN N      N N N 382 
GLN CA     C N S 383 
GLN C      C N N 384 
GLN O      O N N 385 
GLN CB     C N N 386 
GLN CG     C N N 387 
GLN CD     C N N 388 
GLN OE1    O N N 389 
GLN NE2    N N N 390 
GLN OXT    O N N 391 
GLN H      H N N 392 
GLN H2     H N N 393 
GLN HA     H N N 394 
GLN HB2    H N N 395 
GLN HB3    H N N 396 
GLN HG2    H N N 397 
GLN HG3    H N N 398 
GLN HE21   H N N 399 
GLN HE22   H N N 400 
GLN HXT    H N N 401 
GLU N      N N N 402 
GLU CA     C N S 403 
GLU C      C N N 404 
GLU O      O N N 405 
GLU CB     C N N 406 
GLU CG     C N N 407 
GLU CD     C N N 408 
GLU OE1    O N N 409 
GLU OE2    O N N 410 
GLU OXT    O N N 411 
GLU H      H N N 412 
GLU H2     H N N 413 
GLU HA     H N N 414 
GLU HB2    H N N 415 
GLU HB3    H N N 416 
GLU HG2    H N N 417 
GLU HG3    H N N 418 
GLU HE2    H N N 419 
GLU HXT    H N N 420 
GLY N      N N N 421 
GLY CA     C N N 422 
GLY C      C N N 423 
GLY O      O N N 424 
GLY OXT    O N N 425 
GLY H      H N N 426 
GLY H2     H N N 427 
GLY HA2    H N N 428 
GLY HA3    H N N 429 
GLY HXT    H N N 430 
HIS N      N N N 431 
HIS CA     C N S 432 
HIS C      C N N 433 
HIS O      O N N 434 
HIS CB     C N N 435 
HIS CG     C Y N 436 
HIS ND1    N Y N 437 
HIS CD2    C Y N 438 
HIS CE1    C Y N 439 
HIS NE2    N Y N 440 
HIS OXT    O N N 441 
HIS H      H N N 442 
HIS H2     H N N 443 
HIS HA     H N N 444 
HIS HB2    H N N 445 
HIS HB3    H N N 446 
HIS HD1    H N N 447 
HIS HD2    H N N 448 
HIS HE1    H N N 449 
HIS HE2    H N N 450 
HIS HXT    H N N 451 
ILE N      N N N 452 
ILE CA     C N S 453 
ILE C      C N N 454 
ILE O      O N N 455 
ILE CB     C N S 456 
ILE CG1    C N N 457 
ILE CG2    C N N 458 
ILE CD1    C N N 459 
ILE OXT    O N N 460 
ILE H      H N N 461 
ILE H2     H N N 462 
ILE HA     H N N 463 
ILE HB     H N N 464 
ILE HG12   H N N 465 
ILE HG13   H N N 466 
ILE HG21   H N N 467 
ILE HG22   H N N 468 
ILE HG23   H N N 469 
ILE HD11   H N N 470 
ILE HD12   H N N 471 
ILE HD13   H N N 472 
ILE HXT    H N N 473 
LEU N      N N N 474 
LEU CA     C N S 475 
LEU C      C N N 476 
LEU O      O N N 477 
LEU CB     C N N 478 
LEU CG     C N N 479 
LEU CD1    C N N 480 
LEU CD2    C N N 481 
LEU OXT    O N N 482 
LEU H      H N N 483 
LEU H2     H N N 484 
LEU HA     H N N 485 
LEU HB2    H N N 486 
LEU HB3    H N N 487 
LEU HG     H N N 488 
LEU HD11   H N N 489 
LEU HD12   H N N 490 
LEU HD13   H N N 491 
LEU HD21   H N N 492 
LEU HD22   H N N 493 
LEU HD23   H N N 494 
LEU HXT    H N N 495 
LYS N      N N N 496 
LYS CA     C N S 497 
LYS C      C N N 498 
LYS O      O N N 499 
LYS CB     C N N 500 
LYS CG     C N N 501 
LYS CD     C N N 502 
LYS CE     C N N 503 
LYS NZ     N N N 504 
LYS OXT    O N N 505 
LYS H      H N N 506 
LYS H2     H N N 507 
LYS HA     H N N 508 
LYS HB2    H N N 509 
LYS HB3    H N N 510 
LYS HG2    H N N 511 
LYS HG3    H N N 512 
LYS HD2    H N N 513 
LYS HD3    H N N 514 
LYS HE2    H N N 515 
LYS HE3    H N N 516 
LYS HZ1    H N N 517 
LYS HZ2    H N N 518 
LYS HZ3    H N N 519 
LYS HXT    H N N 520 
MET N      N N N 521 
MET CA     C N S 522 
MET C      C N N 523 
MET O      O N N 524 
MET CB     C N N 525 
MET CG     C N N 526 
MET SD     S N N 527 
MET CE     C N N 528 
MET OXT    O N N 529 
MET H      H N N 530 
MET H2     H N N 531 
MET HA     H N N 532 
MET HB2    H N N 533 
MET HB3    H N N 534 
MET HG2    H N N 535 
MET HG3    H N N 536 
MET HE1    H N N 537 
MET HE2    H N N 538 
MET HE3    H N N 539 
MET HXT    H N N 540 
PHE N      N N N 541 
PHE CA     C N S 542 
PHE C      C N N 543 
PHE O      O N N 544 
PHE CB     C N N 545 
PHE CG     C Y N 546 
PHE CD1    C Y N 547 
PHE CD2    C Y N 548 
PHE CE1    C Y N 549 
PHE CE2    C Y N 550 
PHE CZ     C Y N 551 
PHE OXT    O N N 552 
PHE H      H N N 553 
PHE H2     H N N 554 
PHE HA     H N N 555 
PHE HB2    H N N 556 
PHE HB3    H N N 557 
PHE HD1    H N N 558 
PHE HD2    H N N 559 
PHE HE1    H N N 560 
PHE HE2    H N N 561 
PHE HZ     H N N 562 
PHE HXT    H N N 563 
PRO N      N N N 564 
PRO CA     C N S 565 
PRO C      C N N 566 
PRO O      O N N 567 
PRO CB     C N N 568 
PRO CG     C N N 569 
PRO CD     C N N 570 
PRO OXT    O N N 571 
PRO H      H N N 572 
PRO HA     H N N 573 
PRO HB2    H N N 574 
PRO HB3    H N N 575 
PRO HG2    H N N 576 
PRO HG3    H N N 577 
PRO HD2    H N N 578 
PRO HD3    H N N 579 
PRO HXT    H N N 580 
SER N      N N N 581 
SER CA     C N S 582 
SER C      C N N 583 
SER O      O N N 584 
SER CB     C N N 585 
SER OG     O N N 586 
SER OXT    O N N 587 
SER H      H N N 588 
SER H2     H N N 589 
SER HA     H N N 590 
SER HB2    H N N 591 
SER HB3    H N N 592 
SER HG     H N N 593 
SER HXT    H N N 594 
THR N      N N N 595 
THR CA     C N S 596 
THR C      C N N 597 
THR O      O N N 598 
THR CB     C N R 599 
THR OG1    O N N 600 
THR CG2    C N N 601 
THR OXT    O N N 602 
THR H      H N N 603 
THR H2     H N N 604 
THR HA     H N N 605 
THR HB     H N N 606 
THR HG1    H N N 607 
THR HG21   H N N 608 
THR HG22   H N N 609 
THR HG23   H N N 610 
THR HXT    H N N 611 
TRP N      N N N 612 
TRP CA     C N S 613 
TRP C      C N N 614 
TRP O      O N N 615 
TRP CB     C N N 616 
TRP CG     C Y N 617 
TRP CD1    C Y N 618 
TRP CD2    C Y N 619 
TRP NE1    N Y N 620 
TRP CE2    C Y N 621 
TRP CE3    C Y N 622 
TRP CZ2    C Y N 623 
TRP CZ3    C Y N 624 
TRP CH2    C Y N 625 
TRP OXT    O N N 626 
TRP H      H N N 627 
TRP H2     H N N 628 
TRP HA     H N N 629 
TRP HB2    H N N 630 
TRP HB3    H N N 631 
TRP HD1    H N N 632 
TRP HE1    H N N 633 
TRP HE3    H N N 634 
TRP HZ2    H N N 635 
TRP HZ3    H N N 636 
TRP HH2    H N N 637 
TRP HXT    H N N 638 
TYR N      N N N 639 
TYR CA     C N S 640 
TYR C      C N N 641 
TYR O      O N N 642 
TYR CB     C N N 643 
TYR CG     C Y N 644 
TYR CD1    C Y N 645 
TYR CD2    C Y N 646 
TYR CE1    C Y N 647 
TYR CE2    C Y N 648 
TYR CZ     C Y N 649 
TYR OH     O N N 650 
TYR OXT    O N N 651 
TYR H      H N N 652 
TYR H2     H N N 653 
TYR HA     H N N 654 
TYR HB2    H N N 655 
TYR HB3    H N N 656 
TYR HD1    H N N 657 
TYR HD2    H N N 658 
TYR HE1    H N N 659 
TYR HE2    H N N 660 
TYR HH     H N N 661 
TYR HXT    H N N 662 
U   OP3    O N N 663 
U   P      P N N 664 
U   OP1    O N N 665 
U   OP2    O N N 666 
U   "O5'"  O N N 667 
U   "C5'"  C N N 668 
U   "C4'"  C N R 669 
U   "O4'"  O N N 670 
U   "C3'"  C N S 671 
U   "O3'"  O N N 672 
U   "C2'"  C N R 673 
U   "O2'"  O N N 674 
U   "C1'"  C N R 675 
U   N1     N N N 676 
U   C2     C N N 677 
U   O2     O N N 678 
U   N3     N N N 679 
U   C4     C N N 680 
U   O4     O N N 681 
U   C5     C N N 682 
U   C6     C N N 683 
U   HOP3   H N N 684 
U   HOP2   H N N 685 
U   "H5'"  H N N 686 
U   "H5''" H N N 687 
U   "H4'"  H N N 688 
U   "H3'"  H N N 689 
U   "HO3'" H N N 690 
U   "H2'"  H N N 691 
U   "HO2'" H N N 692 
U   "H1'"  H N N 693 
U   H3     H N N 694 
U   H5     H N N 695 
U   H6     H N N 696 
VAL N      N N N 697 
VAL CA     C N S 698 
VAL C      C N N 699 
VAL O      O N N 700 
VAL CB     C N N 701 
VAL CG1    C N N 702 
VAL CG2    C N N 703 
VAL OXT    O N N 704 
VAL H      H N N 705 
VAL H2     H N N 706 
VAL HA     H N N 707 
VAL HB     H N N 708 
VAL HG11   H N N 709 
VAL HG12   H N N 710 
VAL HG13   H N N 711 
VAL HG21   H N N 712 
VAL HG22   H N N 713 
VAL HG23   H N N 714 
VAL HXT    H N N 715 
# 
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 
2YR S     C8     sing N N 1   
2YR C8    C9     sing N N 2   
2YR N4    C9     sing N N 3   
2YR N4    C4     sing N N 4   
2YR C4    N3     doub N N 5   
2YR C4    C5     sing N N 6   
2YR N3    C2     sing N N 7   
2YR C5    C6     doub N N 8   
2YR C2    O2     doub N N 9   
2YR C2    N1     sing N N 10  
2YR C6    N1     sing N N 11  
2YR N1    "C1'"  sing N N 12  
2YR "C2'" "C3'"  sing N N 13  
2YR "C2'" "C1'"  sing N N 14  
2YR "C3'" "O3'"  sing N N 15  
2YR "C3'" "C4'"  sing N N 16  
2YR "C1'" "O4'"  sing N N 17  
2YR "O4'" "C4'"  sing N N 18  
2YR "C4'" "C5'"  sing N N 19  
2YR "C5'" "O5'"  sing N N 20  
2YR "O5'" P      sing N N 21  
2YR OP2   P      sing N N 22  
2YR P     OP1    doub N N 23  
2YR OP2   H2     sing N N 24  
2YR "C5'" H3     sing N N 25  
2YR "C5'" H4     sing N N 26  
2YR "C4'" H5     sing N N 27  
2YR "C3'" H6     sing N N 28  
2YR "O3'" H7     sing N N 29  
2YR "C2'" H8     sing N N 30  
2YR "C2'" H9     sing N N 31  
2YR "C1'" H10    sing N N 32  
2YR N4    H11    sing N N 33  
2YR C5    H12    sing N N 34  
2YR C6    H13    sing N N 35  
2YR S     H14    sing N N 36  
2YR C8    H15    sing N N 37  
2YR C8    H16    sing N N 38  
2YR C9    H17    sing N N 39  
2YR C9    H18    sing N N 40  
2YR P     OP3    sing N N 41  
2YR OP3   H20    sing N N 42  
A   OP3   P      sing N N 43  
A   OP3   HOP3   sing N N 44  
A   P     OP1    doub N N 45  
A   P     OP2    sing N N 46  
A   P     "O5'"  sing N N 47  
A   OP2   HOP2   sing N N 48  
A   "O5'" "C5'"  sing N N 49  
A   "C5'" "C4'"  sing N N 50  
A   "C5'" "H5'"  sing N N 51  
A   "C5'" "H5''" sing N N 52  
A   "C4'" "O4'"  sing N N 53  
A   "C4'" "C3'"  sing N N 54  
A   "C4'" "H4'"  sing N N 55  
A   "O4'" "C1'"  sing N N 56  
A   "C3'" "O3'"  sing N N 57  
A   "C3'" "C2'"  sing N N 58  
A   "C3'" "H3'"  sing N N 59  
A   "O3'" "HO3'" sing N N 60  
A   "C2'" "O2'"  sing N N 61  
A   "C2'" "C1'"  sing N N 62  
A   "C2'" "H2'"  sing N N 63  
A   "O2'" "HO2'" sing N N 64  
A   "C1'" N9     sing N N 65  
A   "C1'" "H1'"  sing N N 66  
A   N9    C8     sing Y N 67  
A   N9    C4     sing Y N 68  
A   C8    N7     doub Y N 69  
A   C8    H8     sing N N 70  
A   N7    C5     sing Y N 71  
A   C5    C6     sing Y N 72  
A   C5    C4     doub Y N 73  
A   C6    N6     sing N N 74  
A   C6    N1     doub Y N 75  
A   N6    H61    sing N N 76  
A   N6    H62    sing N N 77  
A   N1    C2     sing Y N 78  
A   C2    N3     doub Y N 79  
A   C2    H2     sing N N 80  
A   N3    C4     sing Y N 81  
ALA N     CA     sing N N 82  
ALA N     H      sing N N 83  
ALA N     H2     sing N N 84  
ALA CA    C      sing N N 85  
ALA CA    CB     sing N N 86  
ALA CA    HA     sing N N 87  
ALA C     O      doub N N 88  
ALA C     OXT    sing N N 89  
ALA CB    HB1    sing N N 90  
ALA CB    HB2    sing N N 91  
ALA CB    HB3    sing N N 92  
ALA OXT   HXT    sing N N 93  
ARG N     CA     sing N N 94  
ARG N     H      sing N N 95  
ARG N     H2     sing N N 96  
ARG CA    C      sing N N 97  
ARG CA    CB     sing N N 98  
ARG CA    HA     sing N N 99  
ARG C     O      doub N N 100 
ARG C     OXT    sing N N 101 
ARG CB    CG     sing N N 102 
ARG CB    HB2    sing N N 103 
ARG CB    HB3    sing N N 104 
ARG CG    CD     sing N N 105 
ARG CG    HG2    sing N N 106 
ARG CG    HG3    sing N N 107 
ARG CD    NE     sing N N 108 
ARG CD    HD2    sing N N 109 
ARG CD    HD3    sing N N 110 
ARG NE    CZ     sing N N 111 
ARG NE    HE     sing N N 112 
ARG CZ    NH1    sing N N 113 
ARG CZ    NH2    doub N N 114 
ARG NH1   HH11   sing N N 115 
ARG NH1   HH12   sing N N 116 
ARG NH2   HH21   sing N N 117 
ARG NH2   HH22   sing N N 118 
ARG OXT   HXT    sing N N 119 
ASN N     CA     sing N N 120 
ASN N     H      sing N N 121 
ASN N     H2     sing N N 122 
ASN CA    C      sing N N 123 
ASN CA    CB     sing N N 124 
ASN CA    HA     sing N N 125 
ASN C     O      doub N N 126 
ASN C     OXT    sing N N 127 
ASN CB    CG     sing N N 128 
ASN CB    HB2    sing N N 129 
ASN CB    HB3    sing N N 130 
ASN CG    OD1    doub N N 131 
ASN CG    ND2    sing N N 132 
ASN ND2   HD21   sing N N 133 
ASN ND2   HD22   sing N N 134 
ASN OXT   HXT    sing N N 135 
ASP N     CA     sing N N 136 
ASP N     H      sing N N 137 
ASP N     H2     sing N N 138 
ASP CA    C      sing N N 139 
ASP CA    CB     sing N N 140 
ASP CA    HA     sing N N 141 
ASP C     O      doub N N 142 
ASP C     OXT    sing N N 143 
ASP CB    CG     sing N N 144 
ASP CB    HB2    sing N N 145 
ASP CB    HB3    sing N N 146 
ASP CG    OD1    doub N N 147 
ASP CG    OD2    sing N N 148 
ASP OD2   HD2    sing N N 149 
ASP OXT   HXT    sing N N 150 
C   OP3   P      sing N N 151 
C   OP3   HOP3   sing N N 152 
C   P     OP1    doub N N 153 
C   P     OP2    sing N N 154 
C   P     "O5'"  sing N N 155 
C   OP2   HOP2   sing N N 156 
C   "O5'" "C5'"  sing N N 157 
C   "C5'" "C4'"  sing N N 158 
C   "C5'" "H5'"  sing N N 159 
C   "C5'" "H5''" sing N N 160 
C   "C4'" "O4'"  sing N N 161 
C   "C4'" "C3'"  sing N N 162 
C   "C4'" "H4'"  sing N N 163 
C   "O4'" "C1'"  sing N N 164 
C   "C3'" "O3'"  sing N N 165 
C   "C3'" "C2'"  sing N N 166 
C   "C3'" "H3'"  sing N N 167 
C   "O3'" "HO3'" sing N N 168 
C   "C2'" "O2'"  sing N N 169 
C   "C2'" "C1'"  sing N N 170 
C   "C2'" "H2'"  sing N N 171 
C   "O2'" "HO2'" sing N N 172 
C   "C1'" N1     sing N N 173 
C   "C1'" "H1'"  sing N N 174 
C   N1    C2     sing N N 175 
C   N1    C6     sing N N 176 
C   C2    O2     doub N N 177 
C   C2    N3     sing N N 178 
C   N3    C4     doub N N 179 
C   C4    N4     sing N N 180 
C   C4    C5     sing N N 181 
C   N4    H41    sing N N 182 
C   N4    H42    sing N N 183 
C   C5    C6     doub N N 184 
C   C5    H5     sing N N 185 
C   C6    H6     sing N N 186 
CYS N     CA     sing N N 187 
CYS N     H      sing N N 188 
CYS N     H2     sing N N 189 
CYS CA    C      sing N N 190 
CYS CA    CB     sing N N 191 
CYS CA    HA     sing N N 192 
CYS C     O      doub N N 193 
CYS C     OXT    sing N N 194 
CYS CB    SG     sing N N 195 
CYS CB    HB2    sing N N 196 
CYS CB    HB3    sing N N 197 
CYS SG    HG     sing N N 198 
CYS OXT   HXT    sing N N 199 
DA  OP3   P      sing N N 200 
DA  OP3   HOP3   sing N N 201 
DA  P     OP1    doub N N 202 
DA  P     OP2    sing N N 203 
DA  P     "O5'"  sing N N 204 
DA  OP2   HOP2   sing N N 205 
DA  "O5'" "C5'"  sing N N 206 
DA  "C5'" "C4'"  sing N N 207 
DA  "C5'" "H5'"  sing N N 208 
DA  "C5'" "H5''" sing N N 209 
DA  "C4'" "O4'"  sing N N 210 
DA  "C4'" "C3'"  sing N N 211 
DA  "C4'" "H4'"  sing N N 212 
DA  "O4'" "C1'"  sing N N 213 
DA  "C3'" "O3'"  sing N N 214 
DA  "C3'" "C2'"  sing N N 215 
DA  "C3'" "H3'"  sing N N 216 
DA  "O3'" "HO3'" sing N N 217 
DA  "C2'" "C1'"  sing N N 218 
DA  "C2'" "H2'"  sing N N 219 
DA  "C2'" "H2''" sing N N 220 
DA  "C1'" N9     sing N N 221 
DA  "C1'" "H1'"  sing N N 222 
DA  N9    C8     sing Y N 223 
DA  N9    C4     sing Y N 224 
DA  C8    N7     doub Y N 225 
DA  C8    H8     sing N N 226 
DA  N7    C5     sing Y N 227 
DA  C5    C6     sing Y N 228 
DA  C5    C4     doub Y N 229 
DA  C6    N6     sing N N 230 
DA  C6    N1     doub Y N 231 
DA  N6    H61    sing N N 232 
DA  N6    H62    sing N N 233 
DA  N1    C2     sing Y N 234 
DA  C2    N3     doub Y N 235 
DA  C2    H2     sing N N 236 
DA  N3    C4     sing Y N 237 
DC  OP3   P      sing N N 238 
DC  OP3   HOP3   sing N N 239 
DC  P     OP1    doub N N 240 
DC  P     OP2    sing N N 241 
DC  P     "O5'"  sing N N 242 
DC  OP2   HOP2   sing N N 243 
DC  "O5'" "C5'"  sing N N 244 
DC  "C5'" "C4'"  sing N N 245 
DC  "C5'" "H5'"  sing N N 246 
DC  "C5'" "H5''" sing N N 247 
DC  "C4'" "O4'"  sing N N 248 
DC  "C4'" "C3'"  sing N N 249 
DC  "C4'" "H4'"  sing N N 250 
DC  "O4'" "C1'"  sing N N 251 
DC  "C3'" "O3'"  sing N N 252 
DC  "C3'" "C2'"  sing N N 253 
DC  "C3'" "H3'"  sing N N 254 
DC  "O3'" "HO3'" sing N N 255 
DC  "C2'" "C1'"  sing N N 256 
DC  "C2'" "H2'"  sing N N 257 
DC  "C2'" "H2''" sing N N 258 
DC  "C1'" N1     sing N N 259 
DC  "C1'" "H1'"  sing N N 260 
DC  N1    C2     sing N N 261 
DC  N1    C6     sing N N 262 
DC  C2    O2     doub N N 263 
DC  C2    N3     sing N N 264 
DC  N3    C4     doub N N 265 
DC  C4    N4     sing N N 266 
DC  C4    C5     sing N N 267 
DC  N4    H41    sing N N 268 
DC  N4    H42    sing N N 269 
DC  C5    C6     doub N N 270 
DC  C5    H5     sing N N 271 
DC  C6    H6     sing N N 272 
DG  OP3   P      sing N N 273 
DG  OP3   HOP3   sing N N 274 
DG  P     OP1    doub N N 275 
DG  P     OP2    sing N N 276 
DG  P     "O5'"  sing N N 277 
DG  OP2   HOP2   sing N N 278 
DG  "O5'" "C5'"  sing N N 279 
DG  "C5'" "C4'"  sing N N 280 
DG  "C5'" "H5'"  sing N N 281 
DG  "C5'" "H5''" sing N N 282 
DG  "C4'" "O4'"  sing N N 283 
DG  "C4'" "C3'"  sing N N 284 
DG  "C4'" "H4'"  sing N N 285 
DG  "O4'" "C1'"  sing N N 286 
DG  "C3'" "O3'"  sing N N 287 
DG  "C3'" "C2'"  sing N N 288 
DG  "C3'" "H3'"  sing N N 289 
DG  "O3'" "HO3'" sing N N 290 
DG  "C2'" "C1'"  sing N N 291 
DG  "C2'" "H2'"  sing N N 292 
DG  "C2'" "H2''" sing N N 293 
DG  "C1'" N9     sing N N 294 
DG  "C1'" "H1'"  sing N N 295 
DG  N9    C8     sing Y N 296 
DG  N9    C4     sing Y N 297 
DG  C8    N7     doub Y N 298 
DG  C8    H8     sing N N 299 
DG  N7    C5     sing Y N 300 
DG  C5    C6     sing N N 301 
DG  C5    C4     doub Y N 302 
DG  C6    O6     doub N N 303 
DG  C6    N1     sing N N 304 
DG  N1    C2     sing N N 305 
DG  N1    H1     sing N N 306 
DG  C2    N2     sing N N 307 
DG  C2    N3     doub N N 308 
DG  N2    H21    sing N N 309 
DG  N2    H22    sing N N 310 
DG  N3    C4     sing N N 311 
DT  OP3   P      sing N N 312 
DT  OP3   HOP3   sing N N 313 
DT  P     OP1    doub N N 314 
DT  P     OP2    sing N N 315 
DT  P     "O5'"  sing N N 316 
DT  OP2   HOP2   sing N N 317 
DT  "O5'" "C5'"  sing N N 318 
DT  "C5'" "C4'"  sing N N 319 
DT  "C5'" "H5'"  sing N N 320 
DT  "C5'" "H5''" sing N N 321 
DT  "C4'" "O4'"  sing N N 322 
DT  "C4'" "C3'"  sing N N 323 
DT  "C4'" "H4'"  sing N N 324 
DT  "O4'" "C1'"  sing N N 325 
DT  "C3'" "O3'"  sing N N 326 
DT  "C3'" "C2'"  sing N N 327 
DT  "C3'" "H3'"  sing N N 328 
DT  "O3'" "HO3'" sing N N 329 
DT  "C2'" "C1'"  sing N N 330 
DT  "C2'" "H2'"  sing N N 331 
DT  "C2'" "H2''" sing N N 332 
DT  "C1'" N1     sing N N 333 
DT  "C1'" "H1'"  sing N N 334 
DT  N1    C2     sing N N 335 
DT  N1    C6     sing N N 336 
DT  C2    O2     doub N N 337 
DT  C2    N3     sing N N 338 
DT  N3    C4     sing N N 339 
DT  N3    H3     sing N N 340 
DT  C4    O4     doub N N 341 
DT  C4    C5     sing N N 342 
DT  C5    C7     sing N N 343 
DT  C5    C6     doub N N 344 
DT  C7    H71    sing N N 345 
DT  C7    H72    sing N N 346 
DT  C7    H73    sing N N 347 
DT  C6    H6     sing N N 348 
G   OP3   P      sing N N 349 
G   OP3   HOP3   sing N N 350 
G   P     OP1    doub N N 351 
G   P     OP2    sing N N 352 
G   P     "O5'"  sing N N 353 
G   OP2   HOP2   sing N N 354 
G   "O5'" "C5'"  sing N N 355 
G   "C5'" "C4'"  sing N N 356 
G   "C5'" "H5'"  sing N N 357 
G   "C5'" "H5''" sing N N 358 
G   "C4'" "O4'"  sing N N 359 
G   "C4'" "C3'"  sing N N 360 
G   "C4'" "H4'"  sing N N 361 
G   "O4'" "C1'"  sing N N 362 
G   "C3'" "O3'"  sing N N 363 
G   "C3'" "C2'"  sing N N 364 
G   "C3'" "H3'"  sing N N 365 
G   "O3'" "HO3'" sing N N 366 
G   "C2'" "O2'"  sing N N 367 
G   "C2'" "C1'"  sing N N 368 
G   "C2'" "H2'"  sing N N 369 
G   "O2'" "HO2'" sing N N 370 
G   "C1'" N9     sing N N 371 
G   "C1'" "H1'"  sing N N 372 
G   N9    C8     sing Y N 373 
G   N9    C4     sing Y N 374 
G   C8    N7     doub Y N 375 
G   C8    H8     sing N N 376 
G   N7    C5     sing Y N 377 
G   C5    C6     sing N N 378 
G   C5    C4     doub Y N 379 
G   C6    O6     doub N N 380 
G   C6    N1     sing N N 381 
G   N1    C2     sing N N 382 
G   N1    H1     sing N N 383 
G   C2    N2     sing N N 384 
G   C2    N3     doub N N 385 
G   N2    H21    sing N N 386 
G   N2    H22    sing N N 387 
G   N3    C4     sing N N 388 
GLN N     CA     sing N N 389 
GLN N     H      sing N N 390 
GLN N     H2     sing N N 391 
GLN CA    C      sing N N 392 
GLN CA    CB     sing N N 393 
GLN CA    HA     sing N N 394 
GLN C     O      doub N N 395 
GLN C     OXT    sing N N 396 
GLN CB    CG     sing N N 397 
GLN CB    HB2    sing N N 398 
GLN CB    HB3    sing N N 399 
GLN CG    CD     sing N N 400 
GLN CG    HG2    sing N N 401 
GLN CG    HG3    sing N N 402 
GLN CD    OE1    doub N N 403 
GLN CD    NE2    sing N N 404 
GLN NE2   HE21   sing N N 405 
GLN NE2   HE22   sing N N 406 
GLN OXT   HXT    sing N N 407 
GLU N     CA     sing N N 408 
GLU N     H      sing N N 409 
GLU N     H2     sing N N 410 
GLU CA    C      sing N N 411 
GLU CA    CB     sing N N 412 
GLU CA    HA     sing N N 413 
GLU C     O      doub N N 414 
GLU C     OXT    sing N N 415 
GLU CB    CG     sing N N 416 
GLU CB    HB2    sing N N 417 
GLU CB    HB3    sing N N 418 
GLU CG    CD     sing N N 419 
GLU CG    HG2    sing N N 420 
GLU CG    HG3    sing N N 421 
GLU CD    OE1    doub N N 422 
GLU CD    OE2    sing N N 423 
GLU OE2   HE2    sing N N 424 
GLU OXT   HXT    sing N N 425 
GLY N     CA     sing N N 426 
GLY N     H      sing N N 427 
GLY N     H2     sing N N 428 
GLY CA    C      sing N N 429 
GLY CA    HA2    sing N N 430 
GLY CA    HA3    sing N N 431 
GLY C     O      doub N N 432 
GLY C     OXT    sing N N 433 
GLY OXT   HXT    sing N N 434 
HIS N     CA     sing N N 435 
HIS N     H      sing N N 436 
HIS N     H2     sing N N 437 
HIS CA    C      sing N N 438 
HIS CA    CB     sing N N 439 
HIS CA    HA     sing N N 440 
HIS C     O      doub N N 441 
HIS C     OXT    sing N N 442 
HIS CB    CG     sing N N 443 
HIS CB    HB2    sing N N 444 
HIS CB    HB3    sing N N 445 
HIS CG    ND1    sing Y N 446 
HIS CG    CD2    doub Y N 447 
HIS ND1   CE1    doub Y N 448 
HIS ND1   HD1    sing N N 449 
HIS CD2   NE2    sing Y N 450 
HIS CD2   HD2    sing N N 451 
HIS CE1   NE2    sing Y N 452 
HIS CE1   HE1    sing N N 453 
HIS NE2   HE2    sing N N 454 
HIS OXT   HXT    sing N N 455 
ILE N     CA     sing N N 456 
ILE N     H      sing N N 457 
ILE N     H2     sing N N 458 
ILE CA    C      sing N N 459 
ILE CA    CB     sing N N 460 
ILE CA    HA     sing N N 461 
ILE C     O      doub N N 462 
ILE C     OXT    sing N N 463 
ILE CB    CG1    sing N N 464 
ILE CB    CG2    sing N N 465 
ILE CB    HB     sing N N 466 
ILE CG1   CD1    sing N N 467 
ILE CG1   HG12   sing N N 468 
ILE CG1   HG13   sing N N 469 
ILE CG2   HG21   sing N N 470 
ILE CG2   HG22   sing N N 471 
ILE CG2   HG23   sing N N 472 
ILE CD1   HD11   sing N N 473 
ILE CD1   HD12   sing N N 474 
ILE CD1   HD13   sing N N 475 
ILE OXT   HXT    sing N N 476 
LEU N     CA     sing N N 477 
LEU N     H      sing N N 478 
LEU N     H2     sing N N 479 
LEU CA    C      sing N N 480 
LEU CA    CB     sing N N 481 
LEU CA    HA     sing N N 482 
LEU C     O      doub N N 483 
LEU C     OXT    sing N N 484 
LEU CB    CG     sing N N 485 
LEU CB    HB2    sing N N 486 
LEU CB    HB3    sing N N 487 
LEU CG    CD1    sing N N 488 
LEU CG    CD2    sing N N 489 
LEU CG    HG     sing N N 490 
LEU CD1   HD11   sing N N 491 
LEU CD1   HD12   sing N N 492 
LEU CD1   HD13   sing N N 493 
LEU CD2   HD21   sing N N 494 
LEU CD2   HD22   sing N N 495 
LEU CD2   HD23   sing N N 496 
LEU OXT   HXT    sing N N 497 
LYS N     CA     sing N N 498 
LYS N     H      sing N N 499 
LYS N     H2     sing N N 500 
LYS CA    C      sing N N 501 
LYS CA    CB     sing N N 502 
LYS CA    HA     sing N N 503 
LYS C     O      doub N N 504 
LYS C     OXT    sing N N 505 
LYS CB    CG     sing N N 506 
LYS CB    HB2    sing N N 507 
LYS CB    HB3    sing N N 508 
LYS CG    CD     sing N N 509 
LYS CG    HG2    sing N N 510 
LYS CG    HG3    sing N N 511 
LYS CD    CE     sing N N 512 
LYS CD    HD2    sing N N 513 
LYS CD    HD3    sing N N 514 
LYS CE    NZ     sing N N 515 
LYS CE    HE2    sing N N 516 
LYS CE    HE3    sing N N 517 
LYS NZ    HZ1    sing N N 518 
LYS NZ    HZ2    sing N N 519 
LYS NZ    HZ3    sing N N 520 
LYS OXT   HXT    sing N N 521 
MET N     CA     sing N N 522 
MET N     H      sing N N 523 
MET N     H2     sing N N 524 
MET CA    C      sing N N 525 
MET CA    CB     sing N N 526 
MET CA    HA     sing N N 527 
MET C     O      doub N N 528 
MET C     OXT    sing N N 529 
MET CB    CG     sing N N 530 
MET CB    HB2    sing N N 531 
MET CB    HB3    sing N N 532 
MET CG    SD     sing N N 533 
MET CG    HG2    sing N N 534 
MET CG    HG3    sing N N 535 
MET SD    CE     sing N N 536 
MET CE    HE1    sing N N 537 
MET CE    HE2    sing N N 538 
MET CE    HE3    sing N N 539 
MET OXT   HXT    sing N N 540 
PHE N     CA     sing N N 541 
PHE N     H      sing N N 542 
PHE N     H2     sing N N 543 
PHE CA    C      sing N N 544 
PHE CA    CB     sing N N 545 
PHE CA    HA     sing N N 546 
PHE C     O      doub N N 547 
PHE C     OXT    sing N N 548 
PHE CB    CG     sing N N 549 
PHE CB    HB2    sing N N 550 
PHE CB    HB3    sing N N 551 
PHE CG    CD1    doub Y N 552 
PHE CG    CD2    sing Y N 553 
PHE CD1   CE1    sing Y N 554 
PHE CD1   HD1    sing N N 555 
PHE CD2   CE2    doub Y N 556 
PHE CD2   HD2    sing N N 557 
PHE CE1   CZ     doub Y N 558 
PHE CE1   HE1    sing N N 559 
PHE CE2   CZ     sing Y N 560 
PHE CE2   HE2    sing N N 561 
PHE CZ    HZ     sing N N 562 
PHE OXT   HXT    sing N N 563 
PRO N     CA     sing N N 564 
PRO N     CD     sing N N 565 
PRO N     H      sing N N 566 
PRO CA    C      sing N N 567 
PRO CA    CB     sing N N 568 
PRO CA    HA     sing N N 569 
PRO C     O      doub N N 570 
PRO C     OXT    sing N N 571 
PRO CB    CG     sing N N 572 
PRO CB    HB2    sing N N 573 
PRO CB    HB3    sing N N 574 
PRO CG    CD     sing N N 575 
PRO CG    HG2    sing N N 576 
PRO CG    HG3    sing N N 577 
PRO CD    HD2    sing N N 578 
PRO CD    HD3    sing N N 579 
PRO OXT   HXT    sing N N 580 
SER N     CA     sing N N 581 
SER N     H      sing N N 582 
SER N     H2     sing N N 583 
SER CA    C      sing N N 584 
SER CA    CB     sing N N 585 
SER CA    HA     sing N N 586 
SER C     O      doub N N 587 
SER C     OXT    sing N N 588 
SER CB    OG     sing N N 589 
SER CB    HB2    sing N N 590 
SER CB    HB3    sing N N 591 
SER OG    HG     sing N N 592 
SER OXT   HXT    sing N N 593 
THR N     CA     sing N N 594 
THR N     H      sing N N 595 
THR N     H2     sing N N 596 
THR CA    C      sing N N 597 
THR CA    CB     sing N N 598 
THR CA    HA     sing N N 599 
THR C     O      doub N N 600 
THR C     OXT    sing N N 601 
THR CB    OG1    sing N N 602 
THR CB    CG2    sing N N 603 
THR CB    HB     sing N N 604 
THR OG1   HG1    sing N N 605 
THR CG2   HG21   sing N N 606 
THR CG2   HG22   sing N N 607 
THR CG2   HG23   sing N N 608 
THR OXT   HXT    sing N N 609 
TRP N     CA     sing N N 610 
TRP N     H      sing N N 611 
TRP N     H2     sing N N 612 
TRP CA    C      sing N N 613 
TRP CA    CB     sing N N 614 
TRP CA    HA     sing N N 615 
TRP C     O      doub N N 616 
TRP C     OXT    sing N N 617 
TRP CB    CG     sing N N 618 
TRP CB    HB2    sing N N 619 
TRP CB    HB3    sing N N 620 
TRP CG    CD1    doub Y N 621 
TRP CG    CD2    sing Y N 622 
TRP CD1   NE1    sing Y N 623 
TRP CD1   HD1    sing N N 624 
TRP CD2   CE2    doub Y N 625 
TRP CD2   CE3    sing Y N 626 
TRP NE1   CE2    sing Y N 627 
TRP NE1   HE1    sing N N 628 
TRP CE2   CZ2    sing Y N 629 
TRP CE3   CZ3    doub Y N 630 
TRP CE3   HE3    sing N N 631 
TRP CZ2   CH2    doub Y N 632 
TRP CZ2   HZ2    sing N N 633 
TRP CZ3   CH2    sing Y N 634 
TRP CZ3   HZ3    sing N N 635 
TRP CH2   HH2    sing N N 636 
TRP OXT   HXT    sing N N 637 
TYR N     CA     sing N N 638 
TYR N     H      sing N N 639 
TYR N     H2     sing N N 640 
TYR CA    C      sing N N 641 
TYR CA    CB     sing N N 642 
TYR CA    HA     sing N N 643 
TYR C     O      doub N N 644 
TYR C     OXT    sing N N 645 
TYR CB    CG     sing N N 646 
TYR CB    HB2    sing N N 647 
TYR CB    HB3    sing N N 648 
TYR CG    CD1    doub Y N 649 
TYR CG    CD2    sing Y N 650 
TYR CD1   CE1    sing Y N 651 
TYR CD1   HD1    sing N N 652 
TYR CD2   CE2    doub Y N 653 
TYR CD2   HD2    sing N N 654 
TYR CE1   CZ     doub Y N 655 
TYR CE1   HE1    sing N N 656 
TYR CE2   CZ     sing Y N 657 
TYR CE2   HE2    sing N N 658 
TYR CZ    OH     sing N N 659 
TYR OH    HH     sing N N 660 
TYR OXT   HXT    sing N N 661 
U   OP3   P      sing N N 662 
U   OP3   HOP3   sing N N 663 
U   P     OP1    doub N N 664 
U   P     OP2    sing N N 665 
U   P     "O5'"  sing N N 666 
U   OP2   HOP2   sing N N 667 
U   "O5'" "C5'"  sing N N 668 
U   "C5'" "C4'"  sing N N 669 
U   "C5'" "H5'"  sing N N 670 
U   "C5'" "H5''" sing N N 671 
U   "C4'" "O4'"  sing N N 672 
U   "C4'" "C3'"  sing N N 673 
U   "C4'" "H4'"  sing N N 674 
U   "O4'" "C1'"  sing N N 675 
U   "C3'" "O3'"  sing N N 676 
U   "C3'" "C2'"  sing N N 677 
U   "C3'" "H3'"  sing N N 678 
U   "O3'" "HO3'" sing N N 679 
U   "C2'" "O2'"  sing N N 680 
U   "C2'" "C1'"  sing N N 681 
U   "C2'" "H2'"  sing N N 682 
U   "O2'" "HO2'" sing N N 683 
U   "C1'" N1     sing N N 684 
U   "C1'" "H1'"  sing N N 685 
U   N1    C2     sing N N 686 
U   N1    C6     sing N N 687 
U   C2    O2     doub N N 688 
U   C2    N3     sing N N 689 
U   N3    C4     sing N N 690 
U   N3    H3     sing N N 691 
U   C4    O4     doub N N 692 
U   C4    C5     sing N N 693 
U   C5    C6     doub N N 694 
U   C5    H5     sing N N 695 
U   C6    H6     sing N N 696 
VAL N     CA     sing N N 697 
VAL N     H      sing N N 698 
VAL N     H2     sing N N 699 
VAL CA    C      sing N N 700 
VAL CA    CB     sing N N 701 
VAL CA    HA     sing N N 702 
VAL C     O      doub N N 703 
VAL C     OXT    sing N N 704 
VAL CB    CG1    sing N N 705 
VAL CB    CG2    sing N N 706 
VAL CB    HB     sing N N 707 
VAL CG1   HG11   sing N N 708 
VAL CG1   HG12   sing N N 709 
VAL CG1   HG13   sing N N 710 
VAL CG2   HG21   sing N N 711 
VAL CG2   HG22   sing N N 712 
VAL CG2   HG23   sing N N 713 
VAL OXT   HXT    sing N N 714 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-07-06 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9CJI 
_em_admin.last_update        2025-06-18 
_em_admin.map_release_date   2025-01-08 
_em_admin.title              'Cas12a:gRNA:DNA (Acidaminococcus sp.) with 0 RNA:DNA base pairs, structure 2' 
# 
loop_
_em_buffer_component.buffer_id 
_em_buffer_component.concentration 
_em_buffer_component.concentration_units 
_em_buffer_component.formula 
_em_buffer_component.id 
_em_buffer_component.name 
1 20   mM ?     1 Tris-Cl              
1 200  mM KCl   2 'potassium chloride' 
1 0.1  mM ?     3 dithiothreitol       
1 5    mM MgCl2 4 'magnesium chloride' 
1 0.25 %  ?     5 glycerol             
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                0.185 
# 
loop_
_em_entity_assembly_naturalsource.cell 
_em_entity_assembly_naturalsource.cellular_location 
_em_entity_assembly_naturalsource.entity_assembly_id 
_em_entity_assembly_naturalsource.id 
_em_entity_assembly_naturalsource.ncbi_tax_id 
_em_entity_assembly_naturalsource.organism 
_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 
? ? 2 2 1111120 'Acidaminococcus sp. BV3L6' ? ? ? ? ? 
? ? 3 3 32630   'synthetic construct'       ? ? ? ? ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   2 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          469008 
_em_entity_assembly_recombinant.organism             'Escherichia coli BL21(DE3)' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ?           1  1 ? ? cryoSPARC 4      
'IMAGE ACQUISITION'             ?           2  ? ? 1 SerialEM  3.8.7  
MASKING                         ?           3  ? ? ? ?         ?      
'CTF CORRECTION'                'patch ctf' 4  1 ? ? cryoSPARC 4      
'LAYERLINE INDEXING'            ?           5  ? ? ? ?         ?      
'DIFFRACTION INDEXING'          ?           6  ? ? ? ?         ?      
'MODEL FITTING'                 ?           7  ? ? ? ?         ?      
'MODEL REFINEMENT'              ?           8  ? ? ? ?         ?      
OTHER                           ?           9  ? ? ? ?         ?      
'INITIAL EULER ASSIGNMENT'      ?           10 1 ? ? cryoSPARC 4      
'FINAL EULER ASSIGNMENT'        ?           11 1 ? ? RELION    5-beta 
CLASSIFICATION                  ?           12 1 ? ? RELION    5-beta 
RECONSTRUCTION                  ?           13 1 ? ? RELION    5-beta 
'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 
# 
loop_
_ndb_struct_conf_na.entry_id 
_ndb_struct_conf_na.feature 
9CJI 'double helix'        
9CJI 'a-form double helix' 
9CJI '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 A DT 2  1_555 C DA 30 1_555 -0.287 -0.583 -1.636 1.982   1.439   -3.183   1  C_DT2:DA30_D  C 2  ? D 30 ? 20 1 
1 A DA 3  1_555 C DT 29 1_555 0.159  -0.440 1.330  3.234   2.329   1.147    2  C_DA3:DT29_D  C 3  ? D 29 ? 20 1 
1 A DG 4  1_555 C DC 28 1_555 -0.157 -0.317 1.071  3.345   1.092   1.774    3  C_DG4:DC28_D  C 4  ? D 28 ? 19 1 
1 A DT 5  1_555 C DA 27 1_555 -0.193 -0.243 0.793  3.068   -3.518  -2.753   4  C_DT5:DA27_D  C 5  ? D 27 ? 20 1 
1 A DG 6  1_555 C DC 26 1_555 -0.176 -0.154 0.428  5.338   -4.298  -0.203   5  C_DG6:DC26_D  C 6  ? D 26 ? 19 1 
1 A DT 8  1_555 C DA 24 1_555 -0.062 -0.132 -0.382 2.156   -12.941 0.788    6  C_DT8:DA24_D  C 8  ? D 24 ? 20 1 
1 A DT 9  1_555 C DA 23 1_555 -0.049 -0.241 -0.486 -7.492  -15.455 6.289    7  C_DT9:DA23_D  C 9  ? D 23 ? 20 1 
1 A DT 10 1_555 C DA 22 1_555 -0.122 -0.295 -0.927 -10.795 -5.008  -2.009   8  C_DT10:DA22_D C 10 ? D 22 ? 20 1 
1 A DG 11 1_555 C DC 21 1_555 -0.060 -0.299 -1.126 -10.159 10.015  -4.709   9  C_DG11:DC21_D C 11 ? D 21 ? 19 1 
1 A DT 12 1_555 C DA 20 1_555 -0.120 -0.110 0.001  0.336   16.276  0.154    10 C_DT12:DA20_D C 12 ? D 20 ? 20 1 
1 A DC 13 1_555 C DG 19 1_555 0.182  -0.154 0.059  6.058   12.765  -0.121   11 C_DC13:DG19_D C 13 ? D 19 ? 19 1 
1 A DG 14 1_555 C DC 18 1_555 -0.217 -0.201 -0.658 -5.940  -4.035  2.111    12 C_DG14:DC18_D C 14 ? D 18 ? 19 1 
1 A DT 15 1_555 C DA 17 1_555 -0.098 -0.106 -0.140 -0.850  -0.613  -0.594   13 C_DT15:DA17_D C 15 ? D 17 ? 20 1 
1 A DC 16 1_555 C DG 16 1_555 0.184  -0.134 -0.099 0.294   0.606   0.298    14 C_DC16:DG16_D C 16 ? D 16 ? 19 1 
1 A DT 17 1_555 C DA 15 1_555 -0.067 -0.132 -0.007 0.868   0.472   1.104    15 C_DT17:DA15_D C 17 ? D 15 ? 20 1 
1 A DC 18 1_555 C DG 14 1_555 0.204  -0.156 0.189  1.996   1.152   1.213    16 C_DC18:DG14_D C 18 ? D 14 ? 19 1 
1 A DA 19 1_555 C DT 13 1_555 0.086  -0.440 -1.297 4.967   -7.964  1.716    17 C_DA19:DT13_D C 19 ? D 13 ? 20 1 
1 A DT 20 1_555 C DA 12 1_555 -0.196 -1.292 -2.447 6.972   -15.532 34.277   18 C_DT20:DA12_D C 20 ? D 12 ? 20 1 
1 A DC 21 1_555 C DG 11 1_555 0.148  -0.435 -1.311 -2.150  -0.478  -0.368   19 C_DC21:DG11_D C 21 ? D 11 ? 19 1 
1 A DT 22 1_555 C DA 10 1_555 -0.131 -0.368 -1.115 -0.943  0.529   1.492    20 C_DT22:DA10_D C 22 ? D 10 ? 20 1 
1 B A  5  1_555 B U  13 1_555 -3.535 -0.984 0.158  -7.867  -0.946  -104.244 21 B_A5:U13_B    B 5  ? B 13 ? 24 4 
1 B G  17 1_555 B C  12 1_555 -0.190 -0.123 -0.149 4.856   -3.973  2.565    22 B_G17:C12_B   B 17 ? B 12 ? 19 1 
1 B U  18 1_555 B A  11 1_555 -0.069 -0.100 0.108  2.373   -7.583  0.774    23 B_U18:A11_B   B 18 ? B 11 ? 20 1 
1 B A  19 1_555 B U  10 1_555 0.046  -0.089 0.462  -0.061  15.425  0.311    24 B_A19:U10_B   B 19 ? B 10 ? 20 1 
1 B G  20 1_555 B C  9  1_555 -0.174 -0.163 0.013  5.946   7.662   0.258    25 B_G20:C9_B    B 20 ? B 9  ? 19 1 
1 B A  21 1_555 B U  8  1_555 0.039  -0.144 -0.462 1.817   4.469   0.417    26 B_A21:U8_B    B 21 ? B 8  ? 20 1 
1 B U  22 1_555 B U  7  1_555 2.378  -1.942 -0.477 0.488   -21.328 2.183    27 B_U22:U7_B    B 22 ? B 7  ? 16 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 A DT 2  1_555 C DA 30 1_555 A DA 3  1_555 C DT 29 1_555 0.504  -1.658 4.742 1.735  1.020  38.457 -2.697 -0.453 4.715 1.547  
-2.631  38.507 1  CC_DT2DA3:DT29DA30_DD   C 2  ? D 30 ? C 3  ? D 29 ? 
1 A DA 3  1_555 C DT 29 1_555 A DG 4  1_555 C DC 28 1_555 0.269  -1.257 3.368 0.762  -0.061 29.812 -2.429 -0.359 3.376 -0.118 
-1.480  29.822 2  CC_DA3DG4:DC28DT29_DD   C 3  ? D 29 ? C 4  ? D 28 ? 
1 A DG 4  1_555 C DC 28 1_555 A DT 5  1_555 C DA 27 1_555 -0.560 -0.394 3.500 -0.161 -0.138 35.063 -0.631 0.904  3.504 -0.230 
0.268   35.064 3  CC_DG4DT5:DA27DC28_DD   C 4  ? D 28 ? C 5  ? D 27 ? 
1 A DT 5  1_555 C DA 27 1_555 A DG 6  1_555 C DC 26 1_555 1.015  -0.142 3.104 3.067  1.531  42.137 -0.348 -1.106 3.160 2.126  
-4.258  42.270 4  CC_DT5DG6:DC26DA27_DD   C 5  ? D 27 ? C 6  ? D 26 ? 
1 A DG 6  1_555 C DC 26 1_555 A DT 8  1_555 C DA 24 1_555 -0.502 -0.565 6.915 2.908  -2.100 65.726 -0.339 0.711  6.904 -1.934 
-2.677  65.813 5  CC_DG6DT8:DA24DC26_DD   C 6  ? D 26 ? C 8  ? D 24 ? 
1 A DT 8  1_555 C DA 24 1_555 A DT 9  1_555 C DA 23 1_555 0.105  0.722  3.302 0.856  -0.199 44.716 0.967  -0.059 3.301 -0.262 
-1.125  44.724 6  CC_DT8DT9:DA23DA24_DD   C 8  ? D 24 ? C 9  ? D 23 ? 
1 A DT 9  1_555 C DA 23 1_555 A DT 10 1_555 C DA 22 1_555 -0.657 0.524  3.610 -2.515 2.848  35.093 0.393  0.668  3.676 4.706  
4.157   35.292 7  CC_DT9DT10:DA22DA23_DD  C 9  ? D 23 ? C 10 ? D 22 ? 
1 A DT 10 1_555 C DA 22 1_555 A DG 11 1_555 C DC 21 1_555 0.230  1.933  3.437 -2.568 4.736  39.679 2.237  -0.655 3.614 6.938  
3.762   40.029 8  CC_DT10DG11:DC21DA22_DD C 10 ? D 22 ? C 11 ? D 21 ? 
1 A DG 11 1_555 C DC 21 1_555 A DT 12 1_555 C DA 20 1_555 1.073  1.255  3.937 -4.881 12.019 10.850 -6.084 -7.858 3.114 46.561 
18.909  16.897 9  CC_DG11DT12:DA20DC21_DD C 11 ? D 21 ? C 12 ? D 20 ? 
1 A DT 12 1_555 C DA 20 1_555 A DC 13 1_555 C DG 19 1_555 0.819  -0.568 3.226 2.067  8.088  32.728 -2.256 -1.083 3.047 14.069 
-3.596  33.747 10 CC_DT12DC13:DG19DA20_DD C 12 ? D 20 ? C 13 ? D 19 ? 
1 A DC 13 1_555 C DG 19 1_555 A DG 14 1_555 C DC 18 1_555 0.763  -0.262 3.216 11.075 16.251 40.579 -1.822 0.010  3.009 21.946 
-14.956 44.912 11 CC_DC13DG14:DC18DG19_DD C 13 ? D 19 ? C 14 ? D 18 ? 
1 A DG 14 1_555 C DC 18 1_555 A DT 15 1_555 C DA 17 1_555 0.128  -0.411 3.411 0.829  0.497  33.586 -0.796 -0.081 3.407 0.859  
-1.434  33.599 12 CC_DG14DT15:DA17DC18_DD C 14 ? D 18 ? C 15 ? D 17 ? 
1 A DT 15 1_555 C DA 17 1_555 A DC 16 1_555 C DG 16 1_555 0.016  -0.699 3.185 -0.513 1.386  36.019 -1.320 -0.097 3.156 2.240  
0.830   36.048 13 CC_DT15DC16:DG16DA17_DD C 15 ? D 17 ? C 16 ? D 16 ? 
1 A DC 16 1_555 C DG 16 1_555 A DT 17 1_555 C DA 15 1_555 0.019  -0.871 3.267 1.865  2.226  29.033 -2.208 0.365  3.188 4.426  
-3.708  29.174 14 CC_DC16DT17:DA15DG16_DD C 16 ? D 16 ? C 17 ? D 15 ? 
1 A DT 17 1_555 C DA 15 1_555 A DC 18 1_555 C DG 14 1_555 0.468  0.893  3.368 2.845  2.205  39.963 1.040  -0.344 3.435 3.219  
-4.152  40.119 15 CC_DT17DC18:DG14DA15_DD C 17 ? D 15 ? C 18 ? D 14 ? 
1 A DC 18 1_555 C DG 14 1_555 A DA 19 1_555 C DT 13 1_555 -0.647 -0.294 3.150 13.801 19.479 34.913 -2.261 2.213  2.294 28.698 
-20.333 42.084 16 CC_DC18DA19:DT13DG14_DD C 18 ? D 14 ? C 19 ? D 13 ? 
1 A DA 19 1_555 C DT 13 1_555 A DT 20 1_555 C DA 12 1_555 1.918  0.986  3.884 5.001  -0.873 33.366 1.872  -2.309 4.093 -1.510 
-8.648  33.739 17 CC_DA19DT20:DA12DT13_DD C 19 ? D 13 ? C 20 ? D 12 ? 
1 A DT 20 1_555 C DA 12 1_555 A DC 21 1_555 C DG 11 1_555 -2.036 1.450  4.090 -7.184 5.414  46.026 1.230  1.772  4.476 6.848  
9.085   46.850 18 CC_DT20DC21:DG11DA12_DD C 20 ? D 12 ? C 21 ? D 11 ? 
1 A DC 21 1_555 C DG 11 1_555 A DT 22 1_555 C DA 10 1_555 1.333  0.302  3.474 1.792  -0.137 37.050 0.494  -1.838 3.531 -0.216 
-2.818  37.092 19 CC_DC21DT22:DA10DG11_DD C 21 ? D 11 ? C 22 ? D 10 ? 
1 B A  5  1_555 B U  13 1_555 B G  17 1_555 B C  12 1_555 3.412  -2.082 3.276 6.734  2.920  81.183 -1.672 -2.439 3.439 2.240  
-5.165  81.457 20 BB_A5G17:C12U13_BB      B 5  ? B 13 ? B 17 ? B 12 ? 
1 B G  17 1_555 B C  12 1_555 B U  18 1_555 B A  11 1_555 -0.684 -2.370 3.529 0.732  0.527  28.074 -5.015 1.594  3.467 1.086  
-1.508  28.088 21 BB_G17U18:A11C12_BB     B 17 ? B 12 ? B 18 ? B 11 ? 
1 B U  18 1_555 B A  11 1_555 B A  19 1_555 B U  10 1_555 -0.329 -1.401 2.882 -2.673 25.684 36.697 -3.651 0.245  1.630 35.869 
3.733   44.614 22 BB_U18A19:U10A11_BB     B 18 ? B 11 ? B 19 ? B 10 ? 
1 B A  19 1_555 B U  10 1_555 B G  20 1_555 B C  9  1_555 -0.009 -1.618 3.093 3.134  9.487  26.241 -5.268 0.655  2.359 19.998 
-6.606  28.047 23 BB_A19G20:C9U10_BB      B 19 ? B 10 ? B 20 ? B 9  ? 
1 B G  20 1_555 B C  9  1_555 B A  21 1_555 B U  8  1_555 0.690  -1.292 3.370 5.071  2.669  37.029 -2.373 -0.389 3.334 4.172  
-7.927  37.454 24 BB_G20A21:U8C9_BB       B 20 ? B 9  ? B 21 ? B 8  ? 
1 B A  21 1_555 B U  8  1_555 B U  22 1_555 B U  7  1_555 0.103  -0.736 3.521 3.178  13.978 42.778 -2.281 0.165  3.144 18.551 
-4.217  45.009 25 BB_A21U22:U7U8_BB       B 21 ? B 8  ? B 22 ? B 7  ? 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Howard Hughes Medical Institute (HHMI)'                                                            'United States' ? 1 
'National Science Foundation (NSF, United States)'                                                  'United States' 2334028 2 
'National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)'               'United States' R21HL173710 3 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)'   'United States' 
'U19AI171110, U54AI170792, U19AI135990, UH3AI150552, U01AI142817' 4 
'National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS)' 'United States' U19NS132303 5 
'Department of Energy (DOE, United States)'                                                         'United States' 
'DE-AC02-05CH11231, 2553571, B656358'                             6 
# 
_atom_sites.entry_id                    9CJI 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     P P     . DT  A 1 2    ? 142.498 136.054 198.230 1.00 195.29 ? 2    DT  C P     1 
ATOM   2     O OP1   . DT  A 1 2    ? 143.562 135.684 197.270 1.00 195.29 ? 2    DT  C OP1   1 
ATOM   3     O OP2   . DT  A 1 2    ? 142.036 135.075 199.239 1.00 195.29 ? 2    DT  C OP2   1 
ATOM   4     O "O5'" . DT  A 1 2    ? 142.939 137.384 199.001 1.00 195.29 ? 2    DT  C "O5'" 1 
ATOM   5     C "C5'" . DT  A 1 2    ? 142.114 137.917 200.031 1.00 195.29 ? 2    DT  C "C5'" 1 
ATOM   6     C "C4'" . DT  A 1 2    ? 142.932 138.760 200.992 1.00 195.29 ? 2    DT  C "C4'" 1 
ATOM   7     O "O4'" . DT  A 1 2    ? 143.730 137.890 201.844 1.00 195.29 ? 2    DT  C "O4'" 1 
ATOM   8     C "C3'" . DT  A 1 2    ? 143.916 139.721 200.326 1.00 195.29 ? 2    DT  C "C3'" 1 
ATOM   9     O "O3'" . DT  A 1 2    ? 143.330 141.023 200.220 1.00 195.29 ? 2    DT  C "O3'" 1 
ATOM   10    C "C2'" . DT  A 1 2    ? 145.092 139.714 201.296 1.00 195.29 ? 2    DT  C "C2'" 1 
ATOM   11    C "C1'" . DT  A 1 2    ? 145.089 138.269 201.782 1.00 195.29 ? 2    DT  C "C1'" 1 
ATOM   12    N N1    . DT  A 1 2    ? 145.814 137.277 200.886 1.00 195.29 ? 2    DT  C N1    1 
ATOM   13    C C2    . DT  A 1 2    ? 147.050 137.584 200.334 1.00 195.29 ? 2    DT  C C2    1 
ATOM   14    O O2    . DT  A 1 2    ? 147.631 138.642 200.501 1.00 195.29 ? 2    DT  C O2    1 
ATOM   15    N N3    . DT  A 1 2    ? 147.587 136.594 199.553 1.00 195.29 ? 2    DT  C N3    1 
ATOM   16    C C4    . DT  A 1 2    ? 147.045 135.350 199.288 1.00 195.29 ? 2    DT  C C4    1 
ATOM   17    O O4    . DT  A 1 2    ? 147.610 134.529 198.575 1.00 195.29 ? 2    DT  C O4    1 
ATOM   18    C C5    . DT  A 1 2    ? 145.766 135.090 199.897 1.00 195.29 ? 2    DT  C C5    1 
ATOM   19    C C7    . DT  A 1 2    ? 145.078 133.775 199.674 1.00 195.29 ? 2    DT  C C7    1 
ATOM   20    C C6    . DT  A 1 2    ? 145.223 136.049 200.660 1.00 195.29 ? 2    DT  C C6    1 
ATOM   21    P P     . DA  A 1 3    ? 144.062 142.199 199.399 1.00 154.22 ? 3    DA  C P     1 
ATOM   22    O OP1   . DA  A 1 3    ? 145.478 141.826 199.188 1.00 154.22 ? 3    DA  C OP1   1 
ATOM   23    O OP2   . DA  A 1 3    ? 143.739 143.470 200.084 1.00 154.22 ? 3    DA  C OP2   1 
ATOM   24    O "O5'" . DA  A 1 3    ? 143.312 142.213 197.985 1.00 154.22 ? 3    DA  C "O5'" 1 
ATOM   25    C "C5'" . DA  A 1 3    ? 143.312 143.396 197.179 1.00 154.22 ? 3    DA  C "C5'" 1 
ATOM   26    C "C4'" . DA  A 1 3    ? 144.726 143.804 196.802 1.00 154.22 ? 3    DA  C "C4'" 1 
ATOM   27    O "O4'" . DA  A 1 3    ? 145.524 142.613 196.572 1.00 154.22 ? 3    DA  C "O4'" 1 
ATOM   28    C "C3'" . DA  A 1 3    ? 144.840 144.617 195.519 1.00 154.22 ? 3    DA  C "C3'" 1 
ATOM   29    O "O3'" . DA  A 1 3    ? 146.003 145.443 195.565 1.00 154.22 ? 3    DA  C "O3'" 1 
ATOM   30    C "C2'" . DA  A 1 3    ? 144.980 143.523 194.472 1.00 154.22 ? 3    DA  C "C2'" 1 
ATOM   31    C "C1'" . DA  A 1 3    ? 145.870 142.525 195.204 1.00 154.22 ? 3    DA  C "C1'" 1 
ATOM   32    N N9    . DA  A 1 3    ? 145.676 141.149 194.764 1.00 154.22 ? 3    DA  C N9    1 
ATOM   33    C C8    . DA  A 1 3    ? 144.604 140.343 195.024 1.00 154.22 ? 3    DA  C C8    1 
ATOM   34    N N7    . DA  A 1 3    ? 144.700 139.148 194.491 1.00 154.22 ? 3    DA  C N7    1 
ATOM   35    C C5    . DA  A 1 3    ? 145.919 139.174 193.836 1.00 154.22 ? 3    DA  C C5    1 
ATOM   36    C C6    . DA  A 1 3    ? 146.607 138.212 193.073 1.00 154.22 ? 3    DA  C C6    1 
ATOM   37    N N6    . DA  A 1 3    ? 146.132 136.985 192.839 1.00 154.22 ? 3    DA  C N6    1 
ATOM   38    N N1    . DA  A 1 3    ? 147.807 138.560 192.561 1.00 154.22 ? 3    DA  C N1    1 
ATOM   39    C C2    . DA  A 1 3    ? 148.273 139.791 192.797 1.00 154.22 ? 3    DA  C C2    1 
ATOM   40    N N3    . DA  A 1 3    ? 147.719 140.778 193.497 1.00 154.22 ? 3    DA  C N3    1 
ATOM   41    C C4    . DA  A 1 3    ? 146.532 140.401 193.993 1.00 154.22 ? 3    DA  C C4    1 
ATOM   42    P P     . DG  A 1 4    ? 146.193 146.647 194.514 1.00 132.75 ? 4    DG  C P     1 
ATOM   43    O OP1   . DG  A 1 4    ? 146.233 147.906 195.289 1.00 132.75 ? 4    DG  C OP1   1 
ATOM   44    O OP2   . DG  A 1 4    ? 145.196 146.486 193.433 1.00 132.75 ? 4    DG  C OP2   1 
ATOM   45    O "O5'" . DG  A 1 4    ? 147.642 146.385 193.886 1.00 132.75 ? 4    DG  C "O5'" 1 
ATOM   46    C "C5'" . DG  A 1 4    ? 148.090 145.053 193.662 1.00 132.75 ? 4    DG  C "C5'" 1 
ATOM   47    C "C4'" . DG  A 1 4    ? 148.618 144.882 192.250 1.00 132.75 ? 4    DG  C "C4'" 1 
ATOM   48    O "O4'" . DG  A 1 4    ? 148.380 143.511 191.819 1.00 132.75 ? 4    DG  C "O4'" 1 
ATOM   49    C "C3'" . DG  A 1 4    ? 147.920 145.732 191.192 1.00 132.75 ? 4    DG  C "C3'" 1 
ATOM   50    O "O3'" . DG  A 1 4    ? 148.748 145.811 190.043 1.00 132.75 ? 4    DG  C "O3'" 1 
ATOM   51    C "C2'" . DG  A 1 4    ? 146.731 144.849 190.890 1.00 132.75 ? 4    DG  C "C2'" 1 
ATOM   52    C "C1'" . DG  A 1 4    ? 147.488 143.546 190.725 1.00 132.75 ? 4    DG  C "C1'" 1 
ATOM   53    N N9    . DG  A 1 4    ? 146.661 142.347 190.718 1.00 132.75 ? 4    DG  C N9    1 
ATOM   54    C C8    . DG  A 1 4    ? 145.435 142.166 191.309 1.00 132.75 ? 4    DG  C C8    1 
ATOM   55    N N7    . DG  A 1 4    ? 144.938 140.974 191.113 1.00 132.75 ? 4    DG  C N7    1 
ATOM   56    C C5    . DG  A 1 4    ? 145.897 140.331 190.339 1.00 132.75 ? 4    DG  C C5    1 
ATOM   57    C C6    . DG  A 1 4    ? 145.921 139.018 189.812 1.00 132.75 ? 4    DG  C C6    1 
ATOM   58    O O6    . DG  A 1 4    ? 145.070 138.125 189.928 1.00 132.75 ? 4    DG  C O6    1 
ATOM   59    N N1    . DG  A 1 4    ? 147.084 138.775 189.085 1.00 132.75 ? 4    DG  C N1    1 
ATOM   60    C C2    . DG  A 1 4    ? 148.094 139.688 188.892 1.00 132.75 ? 4    DG  C C2    1 
ATOM   61    N N2    . DG  A 1 4    ? 149.140 139.277 188.162 1.00 132.75 ? 4    DG  C N2    1 
ATOM   62    N N3    . DG  A 1 4    ? 148.082 140.916 189.380 1.00 132.75 ? 4    DG  C N3    1 
ATOM   63    C C4    . DG  A 1 4    ? 146.958 141.167 190.088 1.00 132.75 ? 4    DG  C C4    1 
ATOM   64    P P     . DT  A 1 5    ? 149.608 147.125 189.713 1.00 107.48 ? 5    DT  C P     1 
ATOM   65    O OP1   . DT  A 1 5    ? 150.637 147.259 190.768 1.00 107.48 ? 5    DT  C OP1   1 
ATOM   66    O OP2   . DT  A 1 5    ? 148.667 148.236 189.452 1.00 107.48 ? 5    DT  C OP2   1 
ATOM   67    O "O5'" . DT  A 1 5    ? 150.324 146.753 188.329 1.00 107.48 ? 5    DT  C "O5'" 1 
ATOM   68    C "C5'" . DT  A 1 5    ? 151.071 145.539 188.217 1.00 107.48 ? 5    DT  C "C5'" 1 
ATOM   69    C "C4'" . DT  A 1 5    ? 150.797 144.843 186.890 1.00 107.48 ? 5    DT  C "C4'" 1 
ATOM   70    O "O4'" . DT  A 1 5    ? 149.872 143.759 187.090 1.00 107.48 ? 5    DT  C "O4'" 1 
ATOM   71    C "C3'" . DT  A 1 5    ? 150.180 145.729 185.808 1.00 107.48 ? 5    DT  C "C3'" 1 
ATOM   72    O "O3'" . DT  A 1 5    ? 151.144 146.057 184.758 1.00 107.48 ? 5    DT  C "O3'" 1 
ATOM   73    C "C2'" . DT  A 1 5    ? 148.963 144.938 185.283 1.00 107.48 ? 5    DT  C "C2'" 1 
ATOM   74    C "C1'" . DT  A 1 5    ? 149.142 143.557 185.908 1.00 107.48 ? 5    DT  C "C1'" 1 
ATOM   75    N N1    . DT  A 1 5    ? 147.863 142.881 186.273 1.00 107.48 ? 5    DT  C N1    1 
ATOM   76    C C2    . DT  A 1 5    ? 147.652 141.579 185.881 1.00 107.48 ? 5    DT  C C2    1 
ATOM   77    O O2    . DT  A 1 5    ? 148.453 140.941 185.223 1.00 107.48 ? 5    DT  C O2    1 
ATOM   78    N N3    . DT  A 1 5    ? 146.453 141.049 186.283 1.00 107.48 ? 5    DT  C N3    1 
ATOM   79    C C4    . DT  A 1 5    ? 145.473 141.673 187.028 1.00 107.48 ? 5    DT  C C4    1 
ATOM   80    O O4    . DT  A 1 5    ? 144.429 141.115 187.340 1.00 107.48 ? 5    DT  C O4    1 
ATOM   81    C C5    . DT  A 1 5    ? 145.760 143.031 187.411 1.00 107.48 ? 5    DT  C C5    1 
ATOM   82    C C7    . DT  A 1 5    ? 144.764 143.807 188.218 1.00 107.48 ? 5    DT  C C7    1 
ATOM   83    C C6    . DT  A 1 5    ? 146.929 143.563 187.024 1.00 107.48 ? 5    DT  C C6    1 
ATOM   84    P P     . DG  A 1 6    ? 152.218 144.998 184.177 1.00 87.31  ? 6    DG  C P     1 
ATOM   85    O OP1   . DG  A 1 6    ? 153.165 144.528 185.211 1.00 87.31  ? 6    DG  C OP1   1 
ATOM   86    O OP2   . DG  A 1 6    ? 152.792 145.658 182.987 1.00 87.31  ? 6    DG  C OP2   1 
ATOM   87    O "O5'" . DG  A 1 6    ? 151.340 143.788 183.618 1.00 87.31  ? 6    DG  C "O5'" 1 
ATOM   88    C "C5'" . DG  A 1 6    ? 150.670 143.930 182.375 1.00 87.31  ? 6    DG  C "C5'" 1 
ATOM   89    C "C4'" . DG  A 1 6    ? 150.574 142.607 181.643 1.00 87.31  ? 6    DG  C "C4'" 1 
ATOM   90    O "O4'" . DG  A 1 6    ? 149.557 141.791 182.273 1.00 87.31  ? 6    DG  C "O4'" 1 
ATOM   91    C "C3'" . DG  A 1 6    ? 150.134 142.727 180.196 1.00 87.31  ? 6    DG  C "C3'" 1 
ATOM   92    O "O3'" . DG  A 1 6    ? 150.554 141.591 179.455 1.00 87.31  ? 6    DG  C "O3'" 1 
ATOM   93    C "C2'" . DG  A 1 6    ? 148.622 142.770 180.338 1.00 87.31  ? 6    DG  C "C2'" 1 
ATOM   94    C "C1'" . DG  A 1 6    ? 148.392 141.769 181.466 1.00 87.31  ? 6    DG  C "C1'" 1 
ATOM   95    N N9    . DG  A 1 6    ? 147.242 142.095 182.303 1.00 87.31  ? 6    DG  C N9    1 
ATOM   96    C C8    . DG  A 1 6    ? 146.960 143.307 182.882 1.00 87.31  ? 6    DG  C C8    1 
ATOM   97    N N7    . DG  A 1 6    ? 145.859 143.304 183.579 1.00 87.31  ? 6    DG  C N7    1 
ATOM   98    C C5    . DG  A 1 6    ? 145.380 142.008 183.453 1.00 87.31  ? 6    DG  C C5    1 
ATOM   99    C C6    . DG  A 1 6    ? 144.217 141.411 183.993 1.00 87.31  ? 6    DG  C C6    1 
ATOM   100   O O6    . DG  A 1 6    ? 143.354 141.928 184.713 1.00 87.31  ? 6    DG  C O6    1 
ATOM   101   N N1    . DG  A 1 6    ? 144.105 140.075 183.621 1.00 87.31  ? 6    DG  C N1    1 
ATOM   102   C C2    . DG  A 1 6    ? 145.003 139.401 182.828 1.00 87.31  ? 6    DG  C C2    1 
ATOM   103   N N2    . DG  A 1 6    ? 144.731 138.114 182.573 1.00 87.31  ? 6    DG  C N2    1 
ATOM   104   N N3    . DG  A 1 6    ? 146.096 139.951 182.317 1.00 87.31  ? 6    DG  C N3    1 
ATOM   105   C C4    . DG  A 1 6    ? 146.219 141.252 182.670 1.00 87.31  ? 6    DG  C C4    1 
HETATM 106   P P     . 2YR A 1 7    ? 150.414 141.578 177.854 1.00 72.25  ? 7    2YR C P     1 
HETATM 107   O OP1   . 2YR A 1 7    ? 151.632 140.947 177.301 1.00 72.25  ? 7    2YR C OP1   1 
HETATM 108   O OP2   . 2YR A 1 7    ? 150.034 142.940 177.424 1.00 72.25  ? 7    2YR C OP2   1 
HETATM 109   O "O5'" . 2YR A 1 7    ? 149.165 140.618 177.583 1.00 72.25  ? 7    2YR C "O5'" 1 
HETATM 110   C "C5'" . 2YR A 1 7    ? 149.281 139.216 177.804 1.00 72.25  ? 7    2YR C "C5'" 1 
HETATM 111   C "C4'" . 2YR A 1 7    ? 147.923 138.532 177.770 1.00 72.25  ? 7    2YR C "C4'" 1 
HETATM 112   O "O4'" . 2YR A 1 7    ? 147.030 139.167 178.725 1.00 72.25  ? 7    2YR C "O4'" 1 
HETATM 113   C "C3'" . 2YR A 1 7    ? 147.178 138.605 176.434 1.00 72.25  ? 7    2YR C "C3'" 1 
HETATM 114   O "O3'" . 2YR A 1 7    ? 146.277 137.511 176.338 1.00 72.25  ? 7    2YR C "O3'" 1 
HETATM 115   C "C2'" . 2YR A 1 7    ? 146.384 139.880 176.628 1.00 72.25  ? 7    2YR C "C2'" 1 
HETATM 116   C "C1'" . 2YR A 1 7    ? 145.884 139.594 178.026 1.00 72.25  ? 7    2YR C "C1'" 1 
HETATM 117   N N1    . 2YR A 1 7    ? 145.268 140.736 178.736 1.00 72.25  ? 7    2YR C N1    1 
HETATM 118   C C2    . 2YR A 1 7    ? 144.135 140.500 179.503 1.00 72.25  ? 7    2YR C C2    1 
HETATM 119   O O2    . 2YR A 1 7    ? 143.694 139.349 179.555 1.00 72.25  ? 7    2YR C O2    1 
HETATM 120   N N3    . 2YR A 1 7    ? 143.559 141.527 180.167 1.00 72.25  ? 7    2YR C N3    1 
HETATM 121   C C4    . 2YR A 1 7    ? 144.086 142.749 180.080 1.00 72.25  ? 7    2YR C C4    1 
HETATM 122   N N4    . 2YR A 1 7    ? 143.481 143.740 180.743 1.00 72.25  ? 7    2YR C N4    1 
HETATM 123   C C5    . 2YR A 1 7    ? 145.248 143.012 179.296 1.00 72.25  ? 7    2YR C C5    1 
HETATM 124   C C6    . 2YR A 1 7    ? 145.803 141.983 178.646 1.00 72.25  ? 7    2YR C C6    1 
HETATM 125   S S     . 2YR A 1 7    ? 145.017 147.236 180.606 1.00 76.23  ? 7    2YR C S     1 
HETATM 126   C C8    . 2YR A 1 7    ? 143.641 146.123 181.033 1.00 76.23  ? 7    2YR C C8    1 
HETATM 127   C C9    . 2YR A 1 7    ? 143.352 145.008 180.028 1.00 76.23  ? 7    2YR C C9    1 
ATOM   128   P P     . DT  A 1 8    ? 146.754 136.051 175.872 1.00 60.46  ? 8    DT  C P     1 
ATOM   129   O OP1   . DT  A 1 8    ? 147.790 135.562 176.808 1.00 60.46  ? 8    DT  C OP1   1 
ATOM   130   O OP2   . DT  A 1 8    ? 147.044 136.123 174.424 1.00 60.46  ? 8    DT  C OP2   1 
ATOM   131   O "O5'" . DT  A 1 8    ? 145.435 135.166 176.068 1.00 60.46  ? 8    DT  C "O5'" 1 
ATOM   132   C "C5'" . DT  A 1 8    ? 144.524 135.468 177.133 1.00 60.46  ? 8    DT  C "C5'" 1 
ATOM   133   C "C4'" . DT  A 1 8    ? 143.086 135.412 176.648 1.00 60.46  ? 8    DT  C "C4'" 1 
ATOM   134   O "O4'" . DT  A 1 8    ? 142.349 136.557 177.168 1.00 60.46  ? 8    DT  C "O4'" 1 
ATOM   135   C "C3'" . DT  A 1 8    ? 142.927 135.508 175.134 1.00 60.46  ? 8    DT  C "C3'" 1 
ATOM   136   O "O3'" . DT  A 1 8    ? 141.662 134.961 174.730 1.00 60.46  ? 8    DT  C "O3'" 1 
ATOM   137   C "C2'" . DT  A 1 8    ? 142.910 137.017 174.968 1.00 60.46  ? 8    DT  C "C2'" 1 
ATOM   138   C "C1'" . DT  A 1 8    ? 141.922 137.342 176.074 1.00 60.46  ? 8    DT  C "C1'" 1 
ATOM   139   N N1    . DT  A 1 8    ? 141.859 138.778 176.484 1.00 60.46  ? 8    DT  C N1    1 
ATOM   140   C C2    . DT  A 1 8    ? 140.869 139.171 177.351 1.00 60.46  ? 8    DT  C C2    1 
ATOM   141   O O2    . DT  A 1 8    ? 140.045 138.404 177.811 1.00 60.46  ? 8    DT  C O2    1 
ATOM   142   N N3    . DT  A 1 8    ? 140.882 140.499 177.676 1.00 60.46  ? 8    DT  C N3    1 
ATOM   143   C C4    . DT  A 1 8    ? 141.763 141.458 177.222 1.00 60.46  ? 8    DT  C C4    1 
ATOM   144   O O4    . DT  A 1 8    ? 141.692 142.631 177.572 1.00 60.46  ? 8    DT  C O4    1 
ATOM   145   C C5    . DT  A 1 8    ? 142.774 140.987 176.309 1.00 60.46  ? 8    DT  C C5    1 
ATOM   146   C C7    . DT  A 1 8    ? 143.781 141.945 175.751 1.00 60.46  ? 8    DT  C C7    1 
ATOM   147   C C6    . DT  A 1 8    ? 142.774 139.682 175.983 1.00 60.46  ? 8    DT  C C6    1 
ATOM   148   P P     . DT  A 1 9    ? 141.274 133.412 174.946 1.00 53.23  ? 9    DT  C P     1 
ATOM   149   O OP1   . DT  A 1 9    ? 142.309 132.696 175.722 1.00 53.23  ? 9    DT  C OP1   1 
ATOM   150   O OP2   . DT  A 1 9    ? 140.910 132.894 173.611 1.00 53.23  ? 9    DT  C OP2   1 
ATOM   151   O "O5'" . DT  A 1 9    ? 139.922 133.492 175.802 1.00 53.23  ? 9    DT  C "O5'" 1 
ATOM   152   C "C5'" . DT  A 1 9    ? 139.419 134.769 176.190 1.00 53.23  ? 9    DT  C "C5'" 1 
ATOM   153   C "C4'" . DT  A 1 9    ? 137.986 134.693 176.691 1.00 53.23  ? 9    DT  C "C4'" 1 
ATOM   154   O "O4'" . DT  A 1 9    ? 137.514 136.034 176.950 1.00 53.23  ? 9    DT  C "O4'" 1 
ATOM   155   C "C3'" . DT  A 1 9    ? 136.976 134.187 175.694 1.00 53.23  ? 9    DT  C "C3'" 1 
ATOM   156   O "O3'" . DT  A 1 9    ? 135.737 133.990 176.381 1.00 53.23  ? 9    DT  C "O3'" 1 
ATOM   157   C "C2'" . DT  A 1 9    ? 136.908 135.389 174.761 1.00 53.23  ? 9    DT  C "C2'" 1 
ATOM   158   C "C1'" . DT  A 1 9    ? 136.900 136.540 175.769 1.00 53.23  ? 9    DT  C "C1'" 1 
ATOM   159   N N1    . DT  A 1 9    ? 137.668 137.747 175.349 1.00 53.23  ? 9    DT  C N1    1 
ATOM   160   C C2    . DT  A 1 9    ? 137.364 138.951 175.927 1.00 53.23  ? 9    DT  C C2    1 
ATOM   161   O O2    . DT  A 1 9    ? 136.473 139.093 176.743 1.00 53.23  ? 9    DT  C O2    1 
ATOM   162   N N3    . DT  A 1 9    ? 138.136 139.997 175.511 1.00 53.23  ? 9    DT  C N3    1 
ATOM   163   C C4    . DT  A 1 9    ? 139.167 139.963 174.599 1.00 53.23  ? 9    DT  C C4    1 
ATOM   164   O O4    . DT  A 1 9    ? 139.800 140.966 174.292 1.00 53.23  ? 9    DT  C O4    1 
ATOM   165   C C5    . DT  A 1 9    ? 139.445 138.668 174.032 1.00 53.23  ? 9    DT  C C5    1 
ATOM   166   C C7    . DT  A 1 9    ? 140.542 138.512 173.022 1.00 53.23  ? 9    DT  C C7    1 
ATOM   167   C C6    . DT  A 1 9    ? 138.695 137.629 174.435 1.00 53.23  ? 9    DT  C C6    1 
ATOM   168   P P     . DT  A 1 10   ? 134.431 133.413 175.642 1.00 49.77  ? 10   DT  C P     1 
ATOM   169   O OP1   . DT  A 1 10   ? 134.211 132.050 176.170 1.00 49.77  ? 10   DT  C OP1   1 
ATOM   170   O OP2   . DT  A 1 10   ? 134.536 133.615 174.181 1.00 49.77  ? 10   DT  C OP2   1 
ATOM   171   O "O5'" . DT  A 1 10   ? 133.255 134.352 176.189 1.00 49.77  ? 10   DT  C "O5'" 1 
ATOM   172   C "C5'" . DT  A 1 10   ? 133.562 135.649 176.703 1.00 49.77  ? 10   DT  C "C5'" 1 
ATOM   173   C "C4'" . DT  A 1 10   ? 132.312 136.505 176.810 1.00 49.77  ? 10   DT  C "C4'" 1 
ATOM   174   O "O4'" . DT  A 1 10   ? 132.646 137.881 176.493 1.00 49.77  ? 10   DT  C "O4'" 1 
ATOM   175   C "C3'" . DT  A 1 10   ? 131.223 136.156 175.822 1.00 49.77  ? 10   DT  C "C3'" 1 
ATOM   176   O "O3'" . DT  A 1 10   ? 129.994 136.713 176.257 1.00 49.77  ? 10   DT  C "O3'" 1 
ATOM   177   C "C2'" . DT  A 1 10   ? 131.733 136.859 174.575 1.00 49.77  ? 10   DT  C "C2'" 1 
ATOM   178   C "C1'" . DT  A 1 10   ? 132.232 138.177 175.168 1.00 49.77  ? 10   DT  C "C1'" 1 
ATOM   179   N N1    . DT  A 1 10   ? 133.392 138.765 174.440 1.00 49.77  ? 10   DT  C N1    1 
ATOM   180   C C2    . DT  A 1 10   ? 133.646 140.112 174.553 1.00 49.77  ? 10   DT  C C2    1 
ATOM   181   O O2    . DT  A 1 10   ? 132.961 140.867 175.217 1.00 49.77  ? 10   DT  C O2    1 
ATOM   182   N N3    . DT  A 1 10   ? 134.740 140.549 173.853 1.00 49.77  ? 10   DT  C N3    1 
ATOM   183   C C4    . DT  A 1 10   ? 135.587 139.786 173.072 1.00 49.77  ? 10   DT  C C4    1 
ATOM   184   O O4    . DT  A 1 10   ? 136.547 140.264 172.482 1.00 49.77  ? 10   DT  C O4    1 
ATOM   185   C C5    . DT  A 1 10   ? 135.265 138.385 172.999 1.00 49.77  ? 10   DT  C C5    1 
ATOM   186   C C7    . DT  A 1 10   ? 136.112 137.467 172.172 1.00 49.77  ? 10   DT  C C7    1 
ATOM   187   C C6    . DT  A 1 10   ? 134.197 137.946 173.678 1.00 49.77  ? 10   DT  C C6    1 
ATOM   188   P P     . DG  A 1 11   ? 128.632 135.870 176.141 1.00 52.87  ? 11   DG  C P     1 
ATOM   189   O OP1   . DG  A 1 11   ? 128.291 135.376 177.492 1.00 52.87  ? 11   DG  C OP1   1 
ATOM   190   O OP2   . DG  A 1 11   ? 128.789 134.915 175.023 1.00 52.87  ? 11   DG  C OP2   1 
ATOM   191   O "O5'" . DG  A 1 11   ? 127.549 136.962 175.705 1.00 52.87  ? 11   DG  C "O5'" 1 
ATOM   192   C "C5'" . DG  A 1 11   ? 127.337 138.118 176.509 1.00 52.87  ? 11   DG  C "C5'" 1 
ATOM   193   C "C4'" . DG  A 1 11   ? 127.001 139.317 175.642 1.00 52.87  ? 11   DG  C "C4'" 1 
ATOM   194   O "O4'" . DG  A 1 11   ? 128.220 139.962 175.232 1.00 52.87  ? 11   DG  C "O4'" 1 
ATOM   195   C "C3'" . DG  A 1 11   ? 126.255 138.978 174.366 1.00 52.87  ? 11   DG  C "C3'" 1 
ATOM   196   O "O3'" . DG  A 1 11   ? 124.857 139.111 174.594 1.00 52.87  ? 11   DG  C "O3'" 1 
ATOM   197   C "C2'" . DG  A 1 11   ? 126.757 140.012 173.353 1.00 52.87  ? 11   DG  C "C2'" 1 
ATOM   198   C "C1'" . DG  A 1 11   ? 128.088 140.497 173.933 1.00 52.87  ? 11   DG  C "C1'" 1 
ATOM   199   N N9    . DG  A 1 11   ? 129.260 140.086 173.170 1.00 52.87  ? 11   DG  C N9    1 
ATOM   200   C C8    . DG  A 1 11   ? 129.640 138.803 172.878 1.00 52.87  ? 11   DG  C C8    1 
ATOM   201   N N7    . DG  A 1 11   ? 130.752 138.732 172.203 1.00 52.87  ? 11   DG  C N7    1 
ATOM   202   C C5    . DG  A 1 11   ? 131.141 140.053 172.047 1.00 52.87  ? 11   DG  C C5    1 
ATOM   203   C C6    . DG  A 1 11   ? 132.272 140.596 171.400 1.00 52.87  ? 11   DG  C C6    1 
ATOM   204   O O6    . DG  A 1 11   ? 133.182 139.999 170.811 1.00 52.87  ? 11   DG  C O6    1 
ATOM   205   N N1    . DG  A 1 11   ? 132.287 141.985 171.467 1.00 52.87  ? 11   DG  C N1    1 
ATOM   206   C C2    . DG  A 1 11   ? 131.331 142.752 172.085 1.00 52.87  ? 11   DG  C C2    1 
ATOM   207   N N2    . DG  A 1 11   ? 131.518 144.081 172.048 1.00 52.87  ? 11   DG  C N2    1 
ATOM   208   N N3    . DG  A 1 11   ? 130.265 142.254 172.700 1.00 52.87  ? 11   DG  C N3    1 
ATOM   209   C C4    . DG  A 1 11   ? 130.236 140.901 172.641 1.00 52.87  ? 11   DG  C C4    1 
ATOM   210   P P     . DT  A 1 12   ? 123.831 138.005 174.047 1.00 70.28  ? 12   DT  C P     1 
ATOM   211   O OP1   . DT  A 1 12   ? 122.690 137.956 174.987 1.00 70.28  ? 12   DT  C OP1   1 
ATOM   212   O OP2   . DT  A 1 12   ? 124.597 136.774 173.755 1.00 70.28  ? 12   DT  C OP2   1 
ATOM   213   O "O5'" . DT  A 1 12   ? 123.330 138.613 172.658 1.00 70.28  ? 12   DT  C "O5'" 1 
ATOM   214   C "C5'" . DT  A 1 12   ? 122.850 139.946 172.610 1.00 70.28  ? 12   DT  C "C5'" 1 
ATOM   215   C "C4'" . DT  A 1 12   ? 123.244 140.613 171.307 1.00 70.28  ? 12   DT  C "C4'" 1 
ATOM   216   O "O4'" . DT  A 1 12   ? 124.648 140.412 171.071 1.00 70.28  ? 12   DT  C "O4'" 1 
ATOM   217   C "C3'" . DT  A 1 12   ? 122.557 140.058 170.065 1.00 70.28  ? 12   DT  C "C3'" 1 
ATOM   218   O "O3'" . DT  A 1 12   ? 121.443 140.873 169.711 1.00 70.28  ? 12   DT  C "O3'" 1 
ATOM   219   C "C2'" . DT  A 1 12   ? 123.645 140.098 168.981 1.00 70.28  ? 12   DT  C "C2'" 1 
ATOM   220   C "C1'" . DT  A 1 12   ? 124.883 140.620 169.708 1.00 70.28  ? 12   DT  C "C1'" 1 
ATOM   221   N N1    . DT  A 1 12   ? 126.131 139.911 169.308 1.00 70.28  ? 12   DT  C N1    1 
ATOM   222   C C2    . DT  A 1 12   ? 127.141 140.617 168.695 1.00 70.28  ? 12   DT  C C2    1 
ATOM   223   O O2    . DT  A 1 12   ? 127.083 141.813 168.478 1.00 70.28  ? 12   DT  C O2    1 
ATOM   224   N N3    . DT  A 1 12   ? 128.235 139.868 168.351 1.00 70.28  ? 12   DT  C N3    1 
ATOM   225   C C4    . DT  A 1 12   ? 128.413 138.514 168.545 1.00 70.28  ? 12   DT  C C4    1 
ATOM   226   O O4    . DT  A 1 12   ? 129.435 137.932 168.199 1.00 70.28  ? 12   DT  C O4    1 
ATOM   227   C C5    . DT  A 1 12   ? 127.312 137.831 169.184 1.00 70.28  ? 12   DT  C C5    1 
ATOM   228   C C7    . DT  A 1 12   ? 127.389 136.358 169.448 1.00 70.28  ? 12   DT  C C7    1 
ATOM   229   C C6    . DT  A 1 12   ? 126.235 138.554 169.525 1.00 70.28  ? 12   DT  C C6    1 
ATOM   230   P P     . DC  A 1 13   ? 120.613 140.577 168.365 1.00 88.82  ? 13   DC  C P     1 
ATOM   231   O OP1   . DC  A 1 13   ? 119.279 141.196 168.519 1.00 88.82  ? 13   DC  C OP1   1 
ATOM   232   O OP2   . DC  A 1 13   ? 120.718 139.131 168.071 1.00 88.82  ? 13   DC  C OP2   1 
ATOM   233   O "O5'" . DC  A 1 13   ? 121.416 141.372 167.231 1.00 88.82  ? 13   DC  C "O5'" 1 
ATOM   234   C "C5'" . DC  A 1 13   ? 121.664 142.763 167.386 1.00 88.82  ? 13   DC  C "C5'" 1 
ATOM   235   C "C4'" . DC  A 1 13   ? 122.681 143.260 166.371 1.00 88.82  ? 13   DC  C "C4'" 1 
ATOM   236   O "O4'" . DC  A 1 13   ? 123.920 142.524 166.515 1.00 88.82  ? 13   DC  C "O4'" 1 
ATOM   237   C "C3'" . DC  A 1 13   ? 122.257 143.116 164.907 1.00 88.82  ? 13   DC  C "C3'" 1 
ATOM   238   O "O3'" . DC  A 1 13   ? 122.278 144.386 164.265 1.00 88.82  ? 13   DC  C "O3'" 1 
ATOM   239   C "C2'" . DC  A 1 13   ? 123.291 142.158 164.304 1.00 88.82  ? 13   DC  C "C2'" 1 
ATOM   240   C "C1'" . DC  A 1 13   ? 124.477 142.304 165.244 1.00 88.82  ? 13   DC  C "C1'" 1 
ATOM   241   N N1    . DC  A 1 13   ? 125.327 141.077 165.312 1.00 88.82  ? 13   DC  C N1    1 
ATOM   242   C C2    . DC  A 1 13   ? 126.620 141.077 164.766 1.00 88.82  ? 13   DC  C C2    1 
ATOM   243   O O2    . DC  A 1 13   ? 127.061 142.102 164.233 1.00 88.82  ? 13   DC  C O2    1 
ATOM   244   N N3    . DC  A 1 13   ? 127.361 139.943 164.845 1.00 88.82  ? 13   DC  C N3    1 
ATOM   245   C C4    . DC  A 1 13   ? 126.860 138.854 165.429 1.00 88.82  ? 13   DC  C C4    1 
ATOM   246   N N4    . DC  A 1 13   ? 127.627 137.761 165.482 1.00 88.82  ? 13   DC  C N4    1 
ATOM   247   C C5    . DC  A 1 13   ? 125.550 138.837 165.985 1.00 88.82  ? 13   DC  C C5    1 
ATOM   248   C C6    . DC  A 1 13   ? 124.827 139.955 165.899 1.00 88.82  ? 13   DC  C C6    1 
ATOM   249   P P     . DG  A 1 14   ? 121.697 144.556 162.776 1.00 109.11 ? 14   DG  C P     1 
ATOM   250   O OP1   . DG  A 1 14   ? 120.951 145.833 162.730 1.00 109.11 ? 14   DG  C OP1   1 
ATOM   251   O OP2   . DG  A 1 14   ? 121.013 143.298 162.403 1.00 109.11 ? 14   DG  C OP2   1 
ATOM   252   O "O5'" . DG  A 1 14   ? 123.009 144.693 161.873 1.00 109.11 ? 14   DG  C "O5'" 1 
ATOM   253   C "C5'" . DG  A 1 14   ? 122.923 144.585 160.458 1.00 109.11 ? 14   DG  C "C5'" 1 
ATOM   254   C "C4'" . DG  A 1 14   ? 124.295 144.325 159.866 1.00 109.11 ? 14   DG  C "C4'" 1 
ATOM   255   O "O4'" . DG  A 1 14   ? 125.112 143.678 160.860 1.00 109.11 ? 14   DG  C "O4'" 1 
ATOM   256   C "C3'" . DG  A 1 14   ? 124.306 143.402 158.659 1.00 109.11 ? 14   DG  C "C3'" 1 
ATOM   257   O "O3'" . DG  A 1 14   ? 124.234 144.174 157.462 1.00 109.11 ? 14   DG  C "O3'" 1 
ATOM   258   C "C2'" . DG  A 1 14   ? 125.652 142.683 158.768 1.00 109.11 ? 14   DG  C "C2'" 1 
ATOM   259   C "C1'" . DG  A 1 14   ? 126.005 142.774 160.249 1.00 109.11 ? 14   DG  C "C1'" 1 
ATOM   260   N N9    . DG  A 1 14   ? 125.931 141.502 160.957 1.00 109.11 ? 14   DG  C N9    1 
ATOM   261   C C8    . DG  A 1 14   ? 124.870 141.019 161.679 1.00 109.11 ? 14   DG  C C8    1 
ATOM   262   N N7    . DG  A 1 14   ? 125.096 139.857 162.223 1.00 109.11 ? 14   DG  C N7    1 
ATOM   263   C C5    . DG  A 1 14   ? 126.392 139.549 161.834 1.00 109.11 ? 14   DG  C C5    1 
ATOM   264   C C6    . DG  A 1 14   ? 127.183 138.413 162.118 1.00 109.11 ? 14   DG  C C6    1 
ATOM   265   O O6    . DG  A 1 14   ? 126.885 137.418 162.793 1.00 109.11 ? 14   DG  C O6    1 
ATOM   266   N N1    . DG  A 1 14   ? 128.440 138.502 161.529 1.00 109.11 ? 14   DG  C N1    1 
ATOM   267   C C2    . DG  A 1 14   ? 128.877 139.557 160.760 1.00 109.11 ? 14   DG  C C2    1 
ATOM   268   N N2    . DG  A 1 14   ? 130.122 139.475 160.274 1.00 109.11 ? 14   DG  C N2    1 
ATOM   269   N N3    . DG  A 1 14   ? 128.144 140.626 160.489 1.00 109.11 ? 14   DG  C N3    1 
ATOM   270   C C4    . DG  A 1 14   ? 126.919 140.554 161.056 1.00 109.11 ? 14   DG  C C4    1 
ATOM   271   P P     . DT  A 1 15   ? 123.906 143.470 156.054 1.00 122.76 ? 15   DT  C P     1 
ATOM   272   O OP1   . DT  A 1 15   ? 123.648 144.543 155.069 1.00 122.76 ? 15   DT  C OP1   1 
ATOM   273   O OP2   . DT  A 1 15   ? 122.879 142.434 156.300 1.00 122.76 ? 15   DT  C OP2   1 
ATOM   274   O "O5'" . DT  A 1 15   ? 125.269 142.728 155.657 1.00 122.76 ? 15   DT  C "O5'" 1 
ATOM   275   C "C5'" . DT  A 1 15   ? 126.474 143.473 155.513 1.00 122.76 ? 15   DT  C "C5'" 1 
ATOM   276   C "C4'" . DT  A 1 15   ? 127.673 142.548 155.390 1.00 122.76 ? 15   DT  C "C4'" 1 
ATOM   277   O "O4'" . DT  A 1 15   ? 127.671 141.588 156.483 1.00 122.76 ? 15   DT  C "O4'" 1 
ATOM   278   C "C3'" . DT  A 1 15   ? 127.719 141.722 154.107 1.00 122.76 ? 15   DT  C "C3'" 1 
ATOM   279   O "O3'" . DT  A 1 15   ? 129.059 141.624 153.647 1.00 122.76 ? 15   DT  C "O3'" 1 
ATOM   280   C "C2'" . DT  A 1 15   ? 127.180 140.368 154.557 1.00 122.76 ? 15   DT  C "C2'" 1 
ATOM   281   C "C1'" . DT  A 1 15   ? 127.750 140.278 155.961 1.00 122.76 ? 15   DT  C "C1'" 1 
ATOM   282   N N1    . DT  A 1 15   ? 126.989 139.363 156.863 1.00 122.76 ? 15   DT  C N1    1 
ATOM   283   C C2    . DT  A 1 15   ? 127.597 138.227 157.347 1.00 122.76 ? 15   DT  C C2    1 
ATOM   284   O O2    . DT  A 1 15   ? 128.740 137.912 157.071 1.00 122.76 ? 15   DT  C O2    1 
ATOM   285   N N3    . DT  A 1 15   ? 126.809 137.462 158.167 1.00 122.76 ? 15   DT  C N3    1 
ATOM   286   C C4    . DT  A 1 15   ? 125.505 137.717 158.545 1.00 122.76 ? 15   DT  C C4    1 
ATOM   287   O O4    . DT  A 1 15   ? 124.877 136.970 159.289 1.00 122.76 ? 15   DT  C O4    1 
ATOM   288   C C5    . DT  A 1 15   ? 124.931 138.923 158.005 1.00 122.76 ? 15   DT  C C5    1 
ATOM   289   C C7    . DT  A 1 15   ? 123.521 139.305 158.346 1.00 122.76 ? 15   DT  C C7    1 
ATOM   290   C C6    . DT  A 1 15   ? 125.690 139.677 157.199 1.00 122.76 ? 15   DT  C C6    1 
ATOM   291   P P     . DC  A 1 16   ? 129.392 141.814 152.087 1.00 144.62 ? 16   DC  C P     1 
ATOM   292   O OP1   . DC  A 1 16   ? 130.406 142.887 151.974 1.00 144.62 ? 16   DC  C OP1   1 
ATOM   293   O OP2   . DC  A 1 16   ? 128.106 141.933 151.365 1.00 144.62 ? 16   DC  C OP2   1 
ATOM   294   O "O5'" . DC  A 1 16   ? 130.063 140.424 151.670 1.00 144.62 ? 16   DC  C "O5'" 1 
ATOM   295   C "C5'" . DC  A 1 16   ? 129.438 139.202 152.034 1.00 144.62 ? 16   DC  C "C5'" 1 
ATOM   296   C "C4'" . DC  A 1 16   ? 130.471 138.173 152.450 1.00 144.62 ? 16   DC  C "C4'" 1 
ATOM   297   O "O4'" . DC  A 1 16   ? 130.093 137.596 153.725 1.00 144.62 ? 16   DC  C "O4'" 1 
ATOM   298   C "C3'" . DC  A 1 16   ? 130.614 136.998 151.500 1.00 144.62 ? 16   DC  C "C3'" 1 
ATOM   299   O "O3'" . DC  A 1 16   ? 131.930 136.474 151.568 1.00 144.62 ? 16   DC  C "O3'" 1 
ATOM   300   C "C2'" . DC  A 1 16   ? 129.588 136.013 152.046 1.00 144.62 ? 16   DC  C "C2'" 1 
ATOM   301   C "C1'" . DC  A 1 16   ? 129.691 136.250 153.550 1.00 144.62 ? 16   DC  C "C1'" 1 
ATOM   302   N N1    . DC  A 1 16   ? 128.404 136.053 154.269 1.00 144.62 ? 16   DC  C N1    1 
ATOM   303   C C2    . DC  A 1 16   ? 128.225 134.928 155.082 1.00 144.62 ? 16   DC  C C2    1 
ATOM   304   O O2    . DC  A 1 16   ? 129.149 134.115 155.186 1.00 144.62 ? 16   DC  C O2    1 
ATOM   305   N N3    . DC  A 1 16   ? 127.042 134.771 155.731 1.00 144.62 ? 16   DC  C N3    1 
ATOM   306   C C4    . DC  A 1 16   ? 126.075 135.680 155.585 1.00 144.62 ? 16   DC  C C4    1 
ATOM   307   N N4    . DC  A 1 16   ? 124.925 135.490 156.240 1.00 144.62 ? 16   DC  C N4    1 
ATOM   308   C C5    . DC  A 1 16   ? 126.244 136.828 154.759 1.00 144.62 ? 16   DC  C C5    1 
ATOM   309   C C6    . DC  A 1 16   ? 127.412 136.974 154.130 1.00 144.62 ? 16   DC  C C6    1 
ATOM   310   P P     . DT  A 1 17   ? 132.488 135.548 150.380 1.00 163.38 ? 17   DT  C P     1 
ATOM   311   O OP1   . DT  A 1 17   ? 133.965 135.558 150.455 1.00 163.38 ? 17   DT  C OP1   1 
ATOM   312   O OP2   . DT  A 1 17   ? 131.812 135.965 149.132 1.00 163.38 ? 17   DT  C OP2   1 
ATOM   313   O "O5'" . DT  A 1 17   ? 131.961 134.087 150.755 1.00 163.38 ? 17   DT  C "O5'" 1 
ATOM   314   C "C5'" . DT  A 1 17   ? 132.341 133.489 151.989 1.00 163.38 ? 17   DT  C "C5'" 1 
ATOM   315   C "C4'" . DT  A 1 17   ? 131.795 132.077 152.091 1.00 163.38 ? 17   DT  C "C4'" 1 
ATOM   316   O "O4'" . DT  A 1 17   ? 130.564 132.080 152.866 1.00 163.38 ? 17   DT  C "O4'" 1 
ATOM   317   C "C3'" . DT  A 1 17   ? 131.447 131.424 150.751 1.00 163.38 ? 17   DT  C "C3'" 1 
ATOM   318   O "O3'" . DT  A 1 17   ? 131.846 130.059 150.755 1.00 163.38 ? 17   DT  C "O3'" 1 
ATOM   319   C "C2'" . DT  A 1 17   ? 129.929 131.559 150.698 1.00 163.38 ? 17   DT  C "C2'" 1 
ATOM   320   C "C1'" . DT  A 1 17   ? 129.581 131.361 152.160 1.00 163.38 ? 17   DT  C "C1'" 1 
ATOM   321   N N1    . DT  A 1 17   ? 128.236 131.881 152.539 1.00 163.38 ? 17   DT  C N1    1 
ATOM   322   C C2    . DT  A 1 17   ? 127.466 131.166 153.425 1.00 163.38 ? 17   DT  C C2    1 
ATOM   323   O O2    . DT  A 1 17   ? 127.827 130.117 153.928 1.00 163.38 ? 17   DT  C O2    1 
ATOM   324   N N3    . DT  A 1 17   ? 126.250 131.725 153.709 1.00 163.38 ? 17   DT  C N3    1 
ATOM   325   C C4    . DT  A 1 17   ? 125.735 132.903 153.202 1.00 163.38 ? 17   DT  C C4    1 
ATOM   326   O O4    . DT  A 1 17   ? 124.628 133.324 153.518 1.00 163.38 ? 17   DT  C O4    1 
ATOM   327   C C5    . DT  A 1 17   ? 126.593 133.603 152.275 1.00 163.38 ? 17   DT  C C5    1 
ATOM   328   C C7    . DT  A 1 17   ? 126.141 134.893 151.658 1.00 163.38 ? 17   DT  C C7    1 
ATOM   329   C C6    . DT  A 1 17   ? 127.787 133.063 151.990 1.00 163.38 ? 17   DT  C C6    1 
ATOM   330   P P     . DC  A 1 18   ? 132.141 129.298 149.371 1.00 180.22 ? 18   DC  C P     1 
ATOM   331   O OP1   . DC  A 1 18   ? 133.406 129.838 148.826 1.00 180.22 ? 18   DC  C OP1   1 
ATOM   332   O OP2   . DC  A 1 18   ? 130.910 129.349 148.553 1.00 180.22 ? 18   DC  C OP2   1 
ATOM   333   O "O5'" . DC  A 1 18   ? 132.375 127.777 149.809 1.00 180.22 ? 18   DC  C "O5'" 1 
ATOM   334   C "C5'" . DC  A 1 18   ? 131.601 126.735 149.217 1.00 180.22 ? 18   DC  C "C5'" 1 
ATOM   335   C "C4'" . DC  A 1 18   ? 130.647 126.128 150.231 1.00 180.22 ? 18   DC  C "C4'" 1 
ATOM   336   O "O4'" . DC  A 1 18   ? 129.784 127.167 150.765 1.00 180.22 ? 18   DC  C "O4'" 1 
ATOM   337   C "C3'" . DC  A 1 18   ? 129.716 125.045 149.676 1.00 180.22 ? 18   DC  C "C3'" 1 
ATOM   338   O "O3'" . DC  A 1 18   ? 129.599 123.974 150.606 1.00 180.22 ? 18   DC  C "O3'" 1 
ATOM   339   C "C2'" . DC  A 1 18   ? 128.392 125.781 149.509 1.00 180.22 ? 18   DC  C "C2'" 1 
ATOM   340   C "C1'" . DC  A 1 18   ? 128.443 126.748 150.679 1.00 180.22 ? 18   DC  C "C1'" 1 
ATOM   341   N N1    . DC  A 1 18   ? 127.578 127.941 150.492 1.00 180.22 ? 18   DC  C N1    1 
ATOM   342   C C2    . DC  A 1 18   ? 126.373 128.032 151.193 1.00 180.22 ? 18   DC  C C2    1 
ATOM   343   O O2    . DC  A 1 18   ? 126.064 127.113 151.960 1.00 180.22 ? 18   DC  C O2    1 
ATOM   344   N N3    . DC  A 1 18   ? 125.587 129.121 151.008 1.00 180.22 ? 18   DC  C N3    1 
ATOM   345   C C4    . DC  A 1 18   ? 125.972 130.084 150.166 1.00 180.22 ? 18   DC  C C4    1 
ATOM   346   N N4    . DC  A 1 18   ? 125.171 131.144 150.011 1.00 180.22 ? 18   DC  C N4    1 
ATOM   347   C C5    . DC  A 1 18   ? 127.195 130.002 149.439 1.00 180.22 ? 18   DC  C C5    1 
ATOM   348   C C6    . DC  A 1 18   ? 127.958 128.924 149.631 1.00 180.22 ? 18   DC  C C6    1 
ATOM   349   P P     . DA  A 1 19   ? 129.009 122.555 150.134 1.00 193.97 ? 19   DA  C P     1 
ATOM   350   O OP1   . DA  A 1 19   ? 129.426 121.543 151.129 1.00 193.97 ? 19   DA  C OP1   1 
ATOM   351   O OP2   . DA  A 1 19   ? 129.364 122.374 148.709 1.00 193.97 ? 19   DA  C OP2   1 
ATOM   352   O "O5'" . DA  A 1 19   ? 127.421 122.740 150.223 1.00 193.97 ? 19   DA  C "O5'" 1 
ATOM   353   C "C5'" . DA  A 1 19   ? 126.571 121.996 149.354 1.00 193.97 ? 19   DA  C "C5'" 1 
ATOM   354   C "C4'" . DA  A 1 19   ? 125.276 121.613 150.052 1.00 193.97 ? 19   DA  C "C4'" 1 
ATOM   355   O "O4'" . DA  A 1 19   ? 124.646 122.801 150.588 1.00 193.97 ? 19   DA  C "O4'" 1 
ATOM   356   C "C3'" . DA  A 1 19   ? 124.223 121.000 149.149 1.00 193.97 ? 19   DA  C "C3'" 1 
ATOM   357   O "O3'" . DA  A 1 19   ? 123.301 120.253 149.934 1.00 193.97 ? 19   DA  C "O3'" 1 
ATOM   358   C "C2'" . DA  A 1 19   ? 123.573 122.245 148.558 1.00 193.97 ? 19   DA  C "C2'" 1 
ATOM   359   C "C1'" . DA  A 1 19   ? 123.543 123.168 149.773 1.00 193.97 ? 19   DA  C "C1'" 1 
ATOM   360   N N9    . DA  A 1 19   ? 123.681 124.584 149.450 1.00 193.97 ? 19   DA  C N9    1 
ATOM   361   C C8    . DA  A 1 19   ? 124.619 125.156 148.637 1.00 193.97 ? 19   DA  C C8    1 
ATOM   362   N N7    . DA  A 1 19   ? 124.515 126.461 148.548 1.00 193.97 ? 19   DA  C N7    1 
ATOM   363   C C5    . DA  A 1 19   ? 123.441 126.766 149.367 1.00 193.97 ? 19   DA  C C5    1 
ATOM   364   C C6    . DA  A 1 19   ? 122.821 127.984 149.704 1.00 193.97 ? 19   DA  C C6    1 
ATOM   365   N N6    . DA  A 1 19   ? 123.220 129.164 149.227 1.00 193.97 ? 19   DA  C N6    1 
ATOM   366   N N1    . DA  A 1 19   ? 121.767 127.940 150.547 1.00 193.97 ? 19   DA  C N1    1 
ATOM   367   C C2    . DA  A 1 19   ? 121.376 126.752 151.022 1.00 193.97 ? 19   DA  C C2    1 
ATOM   368   N N3    . DA  A 1 19   ? 121.879 125.543 150.778 1.00 193.97 ? 19   DA  C N3    1 
ATOM   369   C C4    . DA  A 1 19   ? 122.919 125.621 149.935 1.00 193.97 ? 19   DA  C C4    1 
ATOM   370   P P     . DT  A 1 20   ? 122.058 119.506 149.243 1.00 204.31 ? 20   DT  C P     1 
ATOM   371   O OP1   . DT  A 1 20   ? 121.670 118.382 150.123 1.00 204.31 ? 20   DT  C OP1   1 
ATOM   372   O OP2   . DT  A 1 20   ? 122.415 119.245 147.831 1.00 204.31 ? 20   DT  C OP2   1 
ATOM   373   O "O5'" . DT  A 1 20   ? 120.892 120.602 149.265 1.00 204.31 ? 20   DT  C "O5'" 1 
ATOM   374   C "C5'" . DT  A 1 20   ? 120.485 121.179 150.500 1.00 204.31 ? 20   DT  C "C5'" 1 
ATOM   375   C "C4'" . DT  A 1 20   ? 119.440 122.259 150.277 1.00 204.31 ? 20   DT  C "C4'" 1 
ATOM   376   O "O4'" . DT  A 1 20   ? 120.074 123.457 149.758 1.00 204.31 ? 20   DT  C "O4'" 1 
ATOM   377   C "C3'" . DT  A 1 20   ? 118.334 121.895 149.283 1.00 204.31 ? 20   DT  C "C3'" 1 
ATOM   378   O "O3'" . DT  A 1 20   ? 117.074 122.299 149.796 1.00 204.31 ? 20   DT  C "O3'" 1 
ATOM   379   C "C2'" . DT  A 1 20   ? 118.708 122.695 148.037 1.00 204.31 ? 20   DT  C "C2'" 1 
ATOM   380   C "C1'" . DT  A 1 20   ? 119.337 123.930 148.657 1.00 204.31 ? 20   DT  C "C1'" 1 
ATOM   381   N N1    . DT  A 1 20   ? 120.263 124.653 147.744 1.00 204.31 ? 20   DT  C N1    1 
ATOM   382   C C2    . DT  A 1 20   ? 120.288 126.027 147.762 1.00 204.31 ? 20   DT  C C2    1 
ATOM   383   O O2    . DT  A 1 20   ? 119.583 126.698 148.493 1.00 204.31 ? 20   DT  C O2    1 
ATOM   384   N N3    . DT  A 1 20   ? 121.175 126.594 146.887 1.00 204.31 ? 20   DT  C N3    1 
ATOM   385   C C4    . DT  A 1 20   ? 122.020 125.938 146.012 1.00 204.31 ? 20   DT  C C4    1 
ATOM   386   O O4    . DT  A 1 20   ? 122.783 126.538 145.261 1.00 204.31 ? 20   DT  C O4    1 
ATOM   387   C C5    . DT  A 1 20   ? 121.943 124.497 146.043 1.00 204.31 ? 20   DT  C C5    1 
ATOM   388   C C7    . DT  A 1 20   ? 122.812 123.674 145.140 1.00 204.31 ? 20   DT  C C7    1 
ATOM   389   C C6    . DT  A 1 20   ? 121.076 123.931 146.897 1.00 204.31 ? 20   DT  C C6    1 
ATOM   390   P P     . DC  A 1 21   ? 116.188 121.277 150.663 1.00 219.81 ? 21   DC  C P     1 
ATOM   391   O OP1   . DC  A 1 21   ? 116.628 121.385 152.071 1.00 219.81 ? 21   DC  C OP1   1 
ATOM   392   O OP2   . DC  A 1 21   ? 116.220 119.964 149.983 1.00 219.81 ? 21   DC  C OP2   1 
ATOM   393   O "O5'" . DC  A 1 21   ? 114.706 121.863 150.539 1.00 219.81 ? 21   DC  C "O5'" 1 
ATOM   394   C "C5'" . DC  A 1 21   ? 114.049 121.869 149.277 1.00 219.81 ? 21   DC  C "C5'" 1 
ATOM   395   C "C4'" . DC  A 1 21   ? 113.088 123.039 149.176 1.00 219.81 ? 21   DC  C "C4'" 1 
ATOM   396   O "O4'" . DC  A 1 21   ? 113.770 124.173 148.586 1.00 219.81 ? 21   DC  C "O4'" 1 
ATOM   397   C "C3'" . DC  A 1 21   ? 111.886 122.801 148.282 1.00 219.81 ? 21   DC  C "C3'" 1 
ATOM   398   O "O3'" . DC  A 1 21   ? 110.821 123.658 148.669 1.00 219.81 ? 21   DC  C "O3'" 1 
ATOM   399   C "C2'" . DC  A 1 21   ? 112.433 123.169 146.907 1.00 219.81 ? 21   DC  C "C2'" 1 
ATOM   400   C "C1'" . DC  A 1 21   ? 113.365 124.336 147.236 1.00 219.81 ? 21   DC  C "C1'" 1 
ATOM   401   N N1    . DC  A 1 21   ? 114.590 124.377 146.387 1.00 219.81 ? 21   DC  C N1    1 
ATOM   402   C C2    . DC  A 1 21   ? 115.023 125.594 145.846 1.00 219.81 ? 21   DC  C C2    1 
ATOM   403   O O2    . DC  A 1 21   ? 114.371 126.624 146.058 1.00 219.81 ? 21   DC  C O2    1 
ATOM   404   N N3    . DC  A 1 21   ? 116.138 125.610 145.074 1.00 219.81 ? 21   DC  C N3    1 
ATOM   405   C C4    . DC  A 1 21   ? 116.815 124.480 144.856 1.00 219.81 ? 21   DC  C C4    1 
ATOM   406   N N4    . DC  A 1 21   ? 117.911 124.547 144.094 1.00 219.81 ? 21   DC  C N4    1 
ATOM   407   C C5    . DC  A 1 21   ? 116.392 123.233 145.402 1.00 219.81 ? 21   DC  C C5    1 
ATOM   408   C C6    . DC  A 1 21   ? 115.287 123.229 146.155 1.00 219.81 ? 21   DC  C C6    1 
ATOM   409   P P     . DT  A 1 22   ? 109.379 123.522 147.975 1.00 222.85 ? 22   DT  C P     1 
ATOM   410   O OP1   . DT  A 1 22   ? 108.364 123.929 148.973 1.00 222.85 ? 22   DT  C OP1   1 
ATOM   411   O OP2   . DT  A 1 22   ? 109.304 122.182 147.351 1.00 222.85 ? 22   DT  C OP2   1 
ATOM   412   O "O5'" . DT  A 1 22   ? 109.416 124.608 146.803 1.00 222.85 ? 22   DT  C "O5'" 1 
ATOM   413   C "C5'" . DT  A 1 22   ? 109.691 125.970 147.110 1.00 222.85 ? 22   DT  C "C5'" 1 
ATOM   414   C "C4'" . DT  A 1 22   ? 109.864 126.786 145.842 1.00 222.85 ? 22   DT  C "C4'" 1 
ATOM   415   O "O4'" . DT  A 1 22   ? 111.146 126.481 145.235 1.00 222.85 ? 22   DT  C "O4'" 1 
ATOM   416   C "C3'" . DT  A 1 22   ? 108.806 126.535 144.762 1.00 222.85 ? 22   DT  C "C3'" 1 
ATOM   417   O "O3'" . DT  A 1 22   ? 108.316 127.774 144.263 1.00 222.85 ? 22   DT  C "O3'" 1 
ATOM   418   C "C2'" . DT  A 1 22   ? 109.569 125.761 143.687 1.00 222.85 ? 22   DT  C "C2'" 1 
ATOM   419   C "C1'" . DT  A 1 22   ? 110.969 126.323 143.850 1.00 222.85 ? 22   DT  C "C1'" 1 
ATOM   420   N N1    . DT  A 1 22   ? 112.039 125.428 143.330 1.00 222.85 ? 22   DT  C N1    1 
ATOM   421   C C2    . DT  A 1 22   ? 113.058 125.969 142.589 1.00 222.85 ? 22   DT  C C2    1 
ATOM   422   O O2    . DT  A 1 22   ? 113.137 127.156 142.332 1.00 222.85 ? 22   DT  C O2    1 
ATOM   423   N N3    . DT  A 1 22   ? 113.991 125.068 142.151 1.00 222.85 ? 22   DT  C N3    1 
ATOM   424   C C4    . DT  A 1 22   ? 114.005 123.705 142.381 1.00 222.85 ? 22   DT  C C4    1 
ATOM   425   O O4    . DT  A 1 22   ? 114.890 122.978 141.944 1.00 222.85 ? 22   DT  C O4    1 
ATOM   426   C C5    . DT  A 1 22   ? 112.904 123.200 143.165 1.00 222.85 ? 22   DT  C C5    1 
ATOM   427   C C7    . DT  A 1 22   ? 112.810 121.736 143.477 1.00 222.85 ? 22   DT  C C7    1 
ATOM   428   C C6    . DT  A 1 22   ? 111.983 124.076 143.596 1.00 222.85 ? 22   DT  C C6    1 
ATOM   429   P P     . A   B 2 4    ? 166.825 160.703 135.780 1.00 49.23  ? 4    A   B P     1 
ATOM   430   O OP1   . A   B 2 4    ? 165.580 160.594 134.978 1.00 49.23  ? 4    A   B OP1   1 
ATOM   431   O OP2   . A   B 2 4    ? 167.973 161.482 135.249 1.00 49.23  ? 4    A   B OP2   1 
ATOM   432   O "O5'" . A   B 2 4    ? 166.437 161.304 137.202 1.00 49.23  ? 4    A   B "O5'" 1 
ATOM   433   C "C5'" . A   B 2 4    ? 165.089 161.304 137.648 1.00 49.23  ? 4    A   B "C5'" 1 
ATOM   434   C "C4'" . A   B 2 4    ? 164.903 162.194 138.851 1.00 49.23  ? 4    A   B "C4'" 1 
ATOM   435   O "O4'" . A   B 2 4    ? 165.494 163.493 138.595 1.00 49.23  ? 4    A   B "O4'" 1 
ATOM   436   C "C3'" . A   B 2 4    ? 163.462 162.499 139.234 1.00 49.23  ? 4    A   B "C3'" 1 
ATOM   437   O "O3'" . A   B 2 4    ? 162.894 161.448 140.006 1.00 49.23  ? 4    A   B "O3'" 1 
ATOM   438   C "C2'" . A   B 2 4    ? 163.579 163.836 139.957 1.00 49.23  ? 4    A   B "C2'" 1 
ATOM   439   O "O2'" . A   B 2 4    ? 164.009 163.643 141.295 1.00 49.23  ? 4    A   B "O2'" 1 
ATOM   440   C "C1'" . A   B 2 4    ? 164.713 164.508 139.182 1.00 49.23  ? 4    A   B "C1'" 1 
ATOM   441   N N9    . A   B 2 4    ? 164.239 165.393 138.101 1.00 49.23  ? 4    A   B N9    1 
ATOM   442   C C8    . A   B 2 4    ? 164.114 165.073 136.773 1.00 49.23  ? 4    A   B C8    1 
ATOM   443   N N7    . A   B 2 4    ? 163.690 166.059 136.022 1.00 49.23  ? 4    A   B N7    1 
ATOM   444   C C5    . A   B 2 4    ? 163.533 167.107 136.914 1.00 49.23  ? 4    A   B C5    1 
ATOM   445   C C6    . A   B 2 4    ? 163.107 168.434 136.742 1.00 49.23  ? 4    A   B C6    1 
ATOM   446   N N6    . A   B 2 4    ? 162.747 168.951 135.567 1.00 49.23  ? 4    A   B N6    1 
ATOM   447   N N1    . A   B 2 4    ? 163.059 169.227 137.832 1.00 49.23  ? 4    A   B N1    1 
ATOM   448   C C2    . A   B 2 4    ? 163.419 168.705 139.009 1.00 49.23  ? 4    A   B C2    1 
ATOM   449   N N3    . A   B 2 4    ? 163.839 167.477 139.299 1.00 49.23  ? 4    A   B N3    1 
ATOM   450   C C4    . A   B 2 4    ? 163.873 166.715 138.196 1.00 49.23  ? 4    A   B C4    1 
ATOM   451   P P     . A   B 2 5    ? 161.609 161.662 140.951 1.00 43.55  ? 5    A   B P     1 
ATOM   452   O OP1   . A   B 2 5    ? 160.977 160.331 141.116 1.00 43.55  ? 5    A   B OP1   1 
ATOM   453   O OP2   . A   B 2 5    ? 160.778 162.789 140.457 1.00 43.55  ? 5    A   B OP2   1 
ATOM   454   O "O5'" . A   B 2 5    ? 162.238 162.044 142.362 1.00 43.55  ? 5    A   B "O5'" 1 
ATOM   455   C "C5'" . A   B 2 5    ? 161.438 162.118 143.532 1.00 43.55  ? 5    A   B "C5'" 1 
ATOM   456   C "C4'" . A   B 2 5    ? 162.094 162.989 144.571 1.00 43.55  ? 5    A   B "C4'" 1 
ATOM   457   O "O4'" . A   B 2 5    ? 162.686 164.134 143.920 1.00 43.55  ? 5    A   B "O4'" 1 
ATOM   458   C "C3'" . A   B 2 5    ? 161.182 163.577 145.641 1.00 43.55  ? 5    A   B "C3'" 1 
ATOM   459   O "O3'" . A   B 2 5    ? 160.994 162.660 146.713 1.00 43.55  ? 5    A   B "O3'" 1 
ATOM   460   C "C2'" . A   B 2 5    ? 161.904 164.860 146.050 1.00 43.55  ? 5    A   B "C2'" 1 
ATOM   461   O "O2'" . A   B 2 5    ? 162.880 164.588 147.045 1.00 43.55  ? 5    A   B "O2'" 1 
ATOM   462   C "C1'" . A   B 2 5    ? 162.630 165.257 144.764 1.00 43.55  ? 5    A   B "C1'" 1 
ATOM   463   N N9    . A   B 2 5    ? 162.018 166.380 144.027 1.00 43.55  ? 5    A   B N9    1 
ATOM   464   C C8    . A   B 2 5    ? 161.557 166.351 142.736 1.00 43.55  ? 5    A   B C8    1 
ATOM   465   N N7    . A   B 2 5    ? 161.101 167.498 142.303 1.00 43.55  ? 5    A   B N7    1 
ATOM   466   C C5    . A   B 2 5    ? 161.294 168.352 143.376 1.00 43.55  ? 5    A   B C5    1 
ATOM   467   C C6    . A   B 2 5    ? 161.015 169.716 143.550 1.00 43.55  ? 5    A   B C6    1 
ATOM   468   N N6    . A   B 2 5    ? 160.463 170.484 142.607 1.00 43.55  ? 5    A   B N6    1 
ATOM   469   N N1    . A   B 2 5    ? 161.327 170.270 144.739 1.00 43.55  ? 5    A   B N1    1 
ATOM   470   C C2    . A   B 2 5    ? 161.880 169.496 145.681 1.00 43.55  ? 5    A   B C2    1 
ATOM   471   N N3    . A   B 2 5    ? 162.190 168.204 145.636 1.00 43.55  ? 5    A   B N3    1 
ATOM   472   C C4    . A   B 2 5    ? 161.869 167.682 144.441 1.00 43.55  ? 5    A   B C4    1 
ATOM   473   P P     . U   B 2 6    ? 160.207 163.043 148.068 1.00 50.27  ? 6    U   B P     1 
ATOM   474   O OP1   . U   B 2 6    ? 160.370 164.458 148.476 1.00 50.27  ? 6    U   B OP1   1 
ATOM   475   O OP2   . U   B 2 6    ? 160.567 161.998 149.052 1.00 50.27  ? 6    U   B OP2   1 
ATOM   476   O "O5'" . U   B 2 6    ? 158.674 162.840 147.705 1.00 50.27  ? 6    U   B "O5'" 1 
ATOM   477   C "C5'" . U   B 2 6    ? 157.662 163.370 148.553 1.00 50.27  ? 6    U   B "C5'" 1 
ATOM   478   C "C4'" . U   B 2 6    ? 156.388 162.568 148.487 1.00 50.27  ? 6    U   B "C4'" 1 
ATOM   479   O "O4'" . U   B 2 6    ? 155.879 162.597 147.128 1.00 50.27  ? 6    U   B "O4'" 1 
ATOM   480   C "C3'" . U   B 2 6    ? 156.515 161.097 148.869 1.00 50.27  ? 6    U   B "C3'" 1 
ATOM   481   O "O3'" . U   B 2 6    ? 155.327 160.677 149.537 1.00 50.27  ? 6    U   B "O3'" 1 
ATOM   482   C "C2'" . U   B 2 6    ? 156.613 160.401 147.515 1.00 50.27  ? 6    U   B "C2'" 1 
ATOM   483   O "O2'" . U   B 2 6    ? 156.180 159.058 147.517 1.00 50.27  ? 6    U   B "O2'" 1 
ATOM   484   C "C1'" . U   B 2 6    ? 155.717 161.279 146.647 1.00 50.27  ? 6    U   B "C1'" 1 
ATOM   485   N N1    . U   B 2 6    ? 156.082 161.279 145.224 1.00 50.27  ? 6    U   B N1    1 
ATOM   486   C C2    . U   B 2 6    ? 155.118 160.919 144.308 1.00 50.27  ? 6    U   B C2    1 
ATOM   487   O O2    . U   B 2 6    ? 153.989 160.599 144.629 1.00 50.27  ? 6    U   B O2    1 
ATOM   488   N N3    . U   B 2 6    ? 155.524 160.945 142.999 1.00 50.27  ? 6    U   B N3    1 
ATOM   489   C C4    . U   B 2 6    ? 156.771 161.290 142.526 1.00 50.27  ? 6    U   B C4    1 
ATOM   490   O O4    . U   B 2 6    ? 156.987 161.265 141.314 1.00 50.27  ? 6    U   B O4    1 
ATOM   491   C C5    . U   B 2 6    ? 157.713 161.653 143.538 1.00 50.27  ? 6    U   B C5    1 
ATOM   492   C C6    . U   B 2 6    ? 157.344 161.636 144.820 1.00 50.27  ? 6    U   B C6    1 
ATOM   493   P P     . U   B 2 7    ? 154.779 161.499 150.805 1.00 41.77  ? 7    U   B P     1 
ATOM   494   O OP1   . U   B 2 7    ? 153.779 162.473 150.311 1.00 41.77  ? 7    U   B OP1   1 
ATOM   495   O OP2   . U   B 2 7    ? 155.934 161.950 151.618 1.00 41.77  ? 7    U   B OP2   1 
ATOM   496   O "O5'" . U   B 2 7    ? 153.977 160.421 151.652 1.00 41.77  ? 7    U   B "O5'" 1 
ATOM   497   C "C5'" . U   B 2 7    ? 154.602 159.691 152.695 1.00 41.77  ? 7    U   B "C5'" 1 
ATOM   498   C "C4'" . U   B 2 7    ? 153.933 158.357 152.881 1.00 41.77  ? 7    U   B "C4'" 1 
ATOM   499   O "O4'" . U   B 2 7    ? 152.516 158.560 153.101 1.00 41.77  ? 7    U   B "O4'" 1 
ATOM   500   C "C3'" . U   B 2 7    ? 154.004 157.428 151.680 1.00 41.77  ? 7    U   B "C3'" 1 
ATOM   501   O "O3'" . U   B 2 7    ? 155.203 156.673 151.667 1.00 41.77  ? 7    U   B "O3'" 1 
ATOM   502   C "C2'" . U   B 2 7    ? 152.758 156.564 151.832 1.00 41.77  ? 7    U   B "C2'" 1 
ATOM   503   O "O2'" . U   B 2 7    ? 152.995 155.501 152.742 1.00 41.77  ? 7    U   B "O2'" 1 
ATOM   504   C "C1'" . U   B 2 7    ? 151.773 157.538 152.479 1.00 41.77  ? 7    U   B "C1'" 1 
ATOM   505   N N1    . U   B 2 7    ? 150.834 158.162 151.518 1.00 41.77  ? 7    U   B N1    1 
ATOM   506   C C2    . U   B 2 7    ? 149.899 157.381 150.863 1.00 41.77  ? 7    U   B C2    1 
ATOM   507   O O2    . U   B 2 7    ? 149.807 156.174 150.996 1.00 41.77  ? 7    U   B O2    1 
ATOM   508   N N3    . U   B 2 7    ? 149.066 158.066 150.017 1.00 41.77  ? 7    U   B N3    1 
ATOM   509   C C4    . U   B 2 7    ? 149.056 159.420 149.773 1.00 41.77  ? 7    U   B C4    1 
ATOM   510   O O4    . U   B 2 7    ? 148.240 159.884 148.977 1.00 41.77  ? 7    U   B O4    1 
ATOM   511   C C5    . U   B 2 7    ? 150.040 160.161 150.495 1.00 41.77  ? 7    U   B C5    1 
ATOM   512   C C6    . U   B 2 7    ? 150.866 159.522 151.325 1.00 41.77  ? 7    U   B C6    1 
ATOM   513   P P     . U   B 2 8    ? 156.249 156.809 150.457 1.00 50.27  ? 8    U   B P     1 
ATOM   514   O OP1   . U   B 2 8    ? 157.596 156.997 151.049 1.00 50.27  ? 8    U   B OP1   1 
ATOM   515   O OP2   . U   B 2 8    ? 155.740 157.809 149.491 1.00 50.27  ? 8    U   B OP2   1 
ATOM   516   O "O5'" . U   B 2 8    ? 156.212 155.377 149.764 1.00 50.27  ? 8    U   B "O5'" 1 
ATOM   517   C "C5'" . U   B 2 8    ? 155.152 154.461 150.023 1.00 50.27  ? 8    U   B "C5'" 1 
ATOM   518   C "C4'" . U   B 2 8    ? 154.457 154.044 148.752 1.00 50.27  ? 8    U   B "C4'" 1 
ATOM   519   O "O4'" . U   B 2 8    ? 153.222 154.806 148.606 1.00 50.27  ? 8    U   B "O4'" 1 
ATOM   520   C "C3'" . U   B 2 8    ? 155.265 154.288 147.476 1.00 50.27  ? 8    U   B "C3'" 1 
ATOM   521   O "O3'" . U   B 2 8    ? 155.028 153.252 146.523 1.00 50.27  ? 8    U   B "O3'" 1 
ATOM   522   C "C2'" . U   B 2 8    ? 154.677 155.593 146.960 1.00 50.27  ? 8    U   B "C2'" 1 
ATOM   523   O "O2'" . U   B 2 8    ? 154.847 155.819 145.578 1.00 50.27  ? 8    U   B "O2'" 1 
ATOM   524   C "C1'" . U   B 2 8    ? 153.211 155.437 147.345 1.00 50.27  ? 8    U   B "C1'" 1 
ATOM   525   N N1    . U   B 2 8    ? 152.517 156.728 147.423 1.00 50.27  ? 8    U   B N1    1 
ATOM   526   C C2    . U   B 2 8    ? 151.420 156.914 146.611 1.00 50.27  ? 8    U   B C2    1 
ATOM   527   O O2    . U   B 2 8    ? 150.984 156.039 145.886 1.00 50.27  ? 8    U   B O2    1 
ATOM   528   N N3    . U   B 2 8    ? 150.849 158.158 146.673 1.00 50.27  ? 8    U   B N3    1 
ATOM   529   C C4    . U   B 2 8    ? 151.267 159.215 147.452 1.00 50.27  ? 8    U   B C4    1 
ATOM   530   O O4    . U   B 2 8    ? 150.653 160.282 147.418 1.00 50.27  ? 8    U   B O4    1 
ATOM   531   C C5    . U   B 2 8    ? 152.418 158.948 148.254 1.00 50.27  ? 8    U   B C5    1 
ATOM   532   C C6    . U   B 2 8    ? 152.995 157.747 148.203 1.00 50.27  ? 8    U   B C6    1 
ATOM   533   P P     . C   B 2 9    ? 155.993 153.103 145.243 1.00 50.27  ? 9    C   B P     1 
ATOM   534   O OP1   . C   B 2 9    ? 156.384 151.678 145.126 1.00 50.27  ? 9    C   B OP1   1 
ATOM   535   O OP2   . C   B 2 9    ? 157.046 154.145 145.321 1.00 50.27  ? 9    C   B OP2   1 
ATOM   536   O "O5'" . C   B 2 9    ? 155.053 153.450 144.003 1.00 50.27  ? 9    C   B "O5'" 1 
ATOM   537   C "C5'" . C   B 2 9    ? 154.377 152.413 143.311 1.00 50.27  ? 9    C   B "C5'" 1 
ATOM   538   C "C4'" . C   B 2 9    ? 153.489 152.927 142.203 1.00 50.27  ? 9    C   B "C4'" 1 
ATOM   539   O "O4'" . C   B 2 9    ? 152.367 153.670 142.743 1.00 50.27  ? 9    C   B "O4'" 1 
ATOM   540   C "C3'" . C   B 2 9    ? 154.102 153.894 141.205 1.00 50.27  ? 9    C   B "C3'" 1 
ATOM   541   O "O3'" . C   B 2 9    ? 154.949 153.271 140.257 1.00 50.27  ? 9    C   B "O3'" 1 
ATOM   542   C "C2'" . C   B 2 9    ? 152.866 154.530 140.586 1.00 50.27  ? 9    C   B "C2'" 1 
ATOM   543   O "O2'" . C   B 2 9    ? 152.268 153.650 139.646 1.00 50.27  ? 9    C   B "O2'" 1 
ATOM   544   C "C1'" . C   B 2 9    ? 151.940 154.632 141.797 1.00 50.27  ? 9    C   B "C1'" 1 
ATOM   545   N N1    . C   B 2 9    ? 151.979 155.979 142.405 1.00 50.27  ? 9    C   B N1    1 
ATOM   546   C C2    . C   B 2 9    ? 151.147 156.966 141.877 1.00 50.27  ? 9    C   B C2    1 
ATOM   547   O O2    . C   B 2 9    ? 150.411 156.673 140.927 1.00 50.27  ? 9    C   B O2    1 
ATOM   548   N N3    . C   B 2 9    ? 151.170 158.208 142.412 1.00 50.27  ? 9    C   B N3    1 
ATOM   549   C C4    . C   B 2 9    ? 151.981 158.479 143.429 1.00 50.27  ? 9    C   B C4    1 
ATOM   550   N N4    . C   B 2 9    ? 151.981 159.712 143.936 1.00 50.27  ? 9    C   B N4    1 
ATOM   551   C C5    . C   B 2 9    ? 152.846 157.494 143.971 1.00 50.27  ? 9    C   B C5    1 
ATOM   552   C C6    . C   B 2 9    ? 152.810 156.268 143.442 1.00 50.27  ? 9    C   B C6    1 
ATOM   553   P P     . U   B 2 10   ? 156.029 154.147 139.450 1.00 50.27  ? 10   U   B P     1 
ATOM   554   O OP1   . U   B 2 10   ? 156.880 153.219 138.666 1.00 50.27  ? 10   U   B OP1   1 
ATOM   555   O OP2   . U   B 2 10   ? 156.664 155.087 140.404 1.00 50.27  ? 10   U   B OP2   1 
ATOM   556   O "O5'" . U   B 2 10   ? 155.156 155.000 138.426 1.00 50.27  ? 10   U   B "O5'" 1 
ATOM   557   C "C5'" . U   B 2 10   ? 154.388 154.360 137.419 1.00 50.27  ? 10   U   B "C5'" 1 
ATOM   558   C "C4'" . U   B 2 10   ? 153.506 155.332 136.674 1.00 50.27  ? 10   U   B "C4'" 1 
ATOM   559   O "O4'" . U   B 2 10   ? 152.503 155.897 137.559 1.00 50.27  ? 10   U   B "O4'" 1 
ATOM   560   C "C3'" . U   B 2 10   ? 154.194 156.549 136.086 1.00 50.27  ? 10   U   B "C3'" 1 
ATOM   561   O "O3'" . U   B 2 10   ? 154.891 156.266 134.888 1.00 50.27  ? 10   U   B "O3'" 1 
ATOM   562   C "C2'" . U   B 2 10   ? 153.036 157.522 135.910 1.00 50.27  ? 10   U   B "C2'" 1 
ATOM   563   O "O2'" . U   B 2 10   ? 152.273 157.193 134.759 1.00 50.27  ? 10   U   B "O2'" 1 
ATOM   564   C "C1'" . U   B 2 10   ? 152.193 157.215 137.148 1.00 50.27  ? 10   U   B "C1'" 1 
ATOM   565   N N1    . U   B 2 10   ? 152.480 158.147 138.263 1.00 50.27  ? 10   U   B N1    1 
ATOM   566   C C2    . U   B 2 10   ? 151.984 159.436 138.193 1.00 50.27  ? 10   U   B C2    1 
ATOM   567   O O2    . U   B 2 10   ? 151.336 159.847 137.247 1.00 50.27  ? 10   U   B O2    1 
ATOM   568   N N3    . U   B 2 10   ? 152.296 160.242 139.262 1.00 50.27  ? 10   U   B N3    1 
ATOM   569   C C4    . U   B 2 10   ? 153.027 159.887 140.376 1.00 50.27  ? 10   U   B C4    1 
ATOM   570   O O4    . U   B 2 10   ? 153.232 160.707 141.272 1.00 50.27  ? 10   U   B O4    1 
ATOM   571   C C5    . U   B 2 10   ? 153.498 158.539 140.373 1.00 50.27  ? 10   U   B C5    1 
ATOM   572   C C6    . U   B 2 10   ? 153.211 157.738 139.347 1.00 50.27  ? 10   U   B C6    1 
ATOM   573   P P     . A   B 2 11   ? 156.297 156.978 134.592 1.00 50.27  ? 11   A   B P     1 
ATOM   574   O OP1   . A   B 2 11   ? 156.934 156.279 133.449 1.00 50.27  ? 11   A   B OP1   1 
ATOM   575   O OP2   . A   B 2 11   ? 157.031 157.103 135.874 1.00 50.27  ? 11   A   B OP2   1 
ATOM   576   O "O5'" . A   B 2 11   ? 155.887 158.440 134.116 1.00 50.27  ? 11   A   B "O5'" 1 
ATOM   577   C "C5'" . A   B 2 11   ? 155.062 158.623 132.978 1.00 50.27  ? 11   A   B "C5'" 1 
ATOM   578   C "C4'" . A   B 2 11   ? 154.528 160.030 132.898 1.00 50.27  ? 11   A   B "C4'" 1 
ATOM   579   O "O4'" . A   B 2 11   ? 153.516 160.240 133.918 1.00 50.27  ? 11   A   B "O4'" 1 
ATOM   580   C "C3'" . A   B 2 11   ? 155.528 161.142 133.151 1.00 50.27  ? 11   A   B "C3'" 1 
ATOM   581   O "O3'" . A   B 2 11   ? 156.362 161.414 132.041 1.00 50.27  ? 11   A   B "O3'" 1 
ATOM   582   C "C2'" . A   B 2 11   ? 154.625 162.301 133.541 1.00 50.27  ? 11   A   B "C2'" 1 
ATOM   583   O "O2'" . A   B 2 11   ? 153.998 162.855 132.395 1.00 50.27  ? 11   A   B "O2'" 1 
ATOM   584   C "C1'" . A   B 2 11   ? 153.564 161.580 134.368 1.00 50.27  ? 11   A   B "C1'" 1 
ATOM   585   N N9    . A   B 2 11   ? 153.915 161.586 135.798 1.00 50.27  ? 11   A   B N9    1 
ATOM   586   C C8    . A   B 2 11   ? 154.380 160.543 136.552 1.00 50.27  ? 11   A   B C8    1 
ATOM   587   N N7    . A   B 2 11   ? 154.614 160.854 137.801 1.00 50.27  ? 11   A   B N7    1 
ATOM   588   C C5    . A   B 2 11   ? 154.293 162.198 137.868 1.00 50.27  ? 11   A   B C5    1 
ATOM   589   C C6    . A   B 2 11   ? 154.329 163.118 138.923 1.00 50.27  ? 11   A   B C6    1 
ATOM   590   N N6    . A   B 2 11   ? 154.724 162.800 140.156 1.00 50.27  ? 11   A   B N6    1 
ATOM   591   N N1    . A   B 2 11   ? 153.949 164.388 138.668 1.00 50.27  ? 11   A   B N1    1 
ATOM   592   C C2    . A   B 2 11   ? 153.558 164.696 137.426 1.00 50.27  ? 11   A   B C2    1 
ATOM   593   N N3    . A   B 2 11   ? 153.481 163.918 136.350 1.00 50.27  ? 11   A   B N3    1 
ATOM   594   C C4    . A   B 2 11   ? 153.867 162.666 136.642 1.00 50.27  ? 11   A   B C4    1 
ATOM   595   P P     . C   B 2 12   ? 157.883 161.872 132.279 1.00 50.27  ? 12   C   B P     1 
ATOM   596   O OP1   . C   B 2 12   ? 158.519 162.043 130.950 1.00 50.27  ? 12   C   B OP1   1 
ATOM   597   O OP2   . C   B 2 12   ? 158.495 160.955 133.272 1.00 50.27  ? 12   C   B OP2   1 
ATOM   598   O "O5'" . C   B 2 12   ? 157.749 163.311 132.947 1.00 50.27  ? 12   C   B "O5'" 1 
ATOM   599   C "C5'" . C   B 2 12   ? 157.138 164.374 132.234 1.00 50.27  ? 12   C   B "C5'" 1 
ATOM   600   C "C4'" . C   B 2 12   ? 156.712 165.503 133.139 1.00 50.27  ? 12   C   B "C4'" 1 
ATOM   601   O "O4'" . C   B 2 12   ? 156.074 164.999 134.337 1.00 50.27  ? 12   C   B "O4'" 1 
ATOM   602   C "C3'" . C   B 2 12   ? 157.811 166.400 133.671 1.00 50.27  ? 12   C   B "C3'" 1 
ATOM   603   O "O3'" . C   B 2 12   ? 158.256 167.333 132.707 1.00 50.27  ? 12   C   B "O3'" 1 
ATOM   604   C "C2'" . C   B 2 12   ? 157.148 167.056 134.876 1.00 50.27  ? 12   C   B "C2'" 1 
ATOM   605   O "O2'" . C   B 2 12   ? 156.329 168.141 134.468 1.00 50.27  ? 12   C   B "O2'" 1 
ATOM   606   C "C1'" . C   B 2 12   ? 156.229 165.939 135.380 1.00 50.27  ? 12   C   B "C1'" 1 
ATOM   607   N N1    . C   B 2 12   ? 156.714 165.268 136.612 1.00 50.27  ? 12   C   B N1    1 
ATOM   608   C C2    . C   B 2 12   ? 156.823 166.012 137.795 1.00 50.27  ? 12   C   B C2    1 
ATOM   609   O O2    . C   B 2 12   ? 156.540 167.218 137.767 1.00 50.27  ? 12   C   B O2    1 
ATOM   610   N N3    . C   B 2 12   ? 157.240 165.408 138.929 1.00 50.27  ? 12   C   B N3    1 
ATOM   611   C C4    . C   B 2 12   ? 157.530 164.110 138.923 1.00 50.27  ? 12   C   B C4    1 
ATOM   612   N N4    . C   B 2 12   ? 157.939 163.551 140.064 1.00 50.27  ? 12   C   B N4    1 
ATOM   613   C C5    . C   B 2 12   ? 157.415 163.325 137.741 1.00 50.27  ? 12   C   B C5    1 
ATOM   614   C C6    . C   B 2 12   ? 157.001 163.934 136.623 1.00 50.27  ? 12   C   B C6    1 
ATOM   615   P P     . U   B 2 13   ? 159.713 167.990 132.831 1.00 48.21  ? 13   U   B P     1 
ATOM   616   O OP1   . U   B 2 13   ? 160.047 168.560 131.505 1.00 48.21  ? 13   U   B OP1   1 
ATOM   617   O OP2   . U   B 2 13   ? 160.618 166.995 133.459 1.00 48.21  ? 13   U   B OP2   1 
ATOM   618   O "O5'" . U   B 2 13   ? 159.511 169.190 133.856 1.00 48.21  ? 13   U   B "O5'" 1 
ATOM   619   C "C5'" . U   B 2 13   ? 158.496 170.165 133.646 1.00 48.21  ? 13   U   B "C5'" 1 
ATOM   620   C "C4'" . U   B 2 13   ? 158.395 171.127 134.804 1.00 48.21  ? 13   U   B "C4'" 1 
ATOM   621   O "O4'" . U   B 2 13   ? 158.221 170.382 136.040 1.00 48.21  ? 13   U   B "O4'" 1 
ATOM   622   C "C3'" . U   B 2 13   ? 159.614 172.018 135.011 1.00 48.21  ? 13   U   B "C3'" 1 
ATOM   623   O "O3'" . U   B 2 13   ? 159.189 173.299 135.463 1.00 48.21  ? 13   U   B "O3'" 1 
ATOM   624   C "C2'" . U   B 2 13   ? 160.375 171.305 136.124 1.00 48.21  ? 13   U   B "C2'" 1 
ATOM   625   O "O2'" . U   B 2 13   ? 161.215 172.142 136.890 1.00 48.21  ? 13   U   B "O2'" 1 
ATOM   626   C "C1'" . U   B 2 13   ? 159.237 170.733 136.959 1.00 48.21  ? 13   U   B "C1'" 1 
ATOM   627   N N1    . U   B 2 13   ? 159.606 169.529 137.716 1.00 48.21  ? 13   U   B N1    1 
ATOM   628   C C2    . U   B 2 13   ? 159.949 169.664 139.047 1.00 48.21  ? 13   U   B C2    1 
ATOM   629   O O2    . U   B 2 13   ? 159.963 170.734 139.629 1.00 48.21  ? 13   U   B O2    1 
ATOM   630   N N3    . U   B 2 13   ? 160.278 168.493 139.679 1.00 48.21  ? 13   U   B N3    1 
ATOM   631   C C4    . U   B 2 13   ? 160.298 167.230 139.128 1.00 48.21  ? 13   U   B C4    1 
ATOM   632   O O4    . U   B 2 13   ? 160.617 166.269 139.825 1.00 48.21  ? 13   U   B O4    1 
ATOM   633   C C5    . U   B 2 13   ? 159.932 167.175 137.750 1.00 48.21  ? 13   U   B C5    1 
ATOM   634   C C6    . U   B 2 13   ? 159.606 168.299 137.110 1.00 48.21  ? 13   U   B C6    1 
ATOM   635   P P     . C   B 2 14   ? 159.569 174.607 134.617 1.00 55.65  ? 14   C   B P     1 
ATOM   636   O OP1   . C   B 2 14   ? 158.347 175.431 134.461 1.00 55.65  ? 14   C   B OP1   1 
ATOM   637   O OP2   . C   B 2 14   ? 160.307 174.168 133.407 1.00 55.65  ? 14   C   B OP2   1 
ATOM   638   O "O5'" . C   B 2 14   ? 160.591 175.380 135.560 1.00 55.65  ? 14   C   B "O5'" 1 
ATOM   639   C "C5'" . C   B 2 14   ? 160.235 175.722 136.890 1.00 55.65  ? 14   C   B "C5'" 1 
ATOM   640   C "C4'" . C   B 2 14   ? 160.101 177.213 137.048 1.00 55.65  ? 14   C   B "C4'" 1 
ATOM   641   O "O4'" . C   B 2 14   ? 159.125 177.714 136.098 1.00 55.65  ? 14   C   B "O4'" 1 
ATOM   642   C "C3'" . C   B 2 14   ? 159.593 177.704 138.395 1.00 55.65  ? 14   C   B "C3'" 1 
ATOM   643   O "O3'" . C   B 2 14   ? 160.612 177.730 139.388 1.00 55.65  ? 14   C   B "O3'" 1 
ATOM   644   C "C2'" . C   B 2 14   ? 159.001 179.062 138.046 1.00 55.65  ? 14   C   B "C2'" 1 
ATOM   645   O "O2'" . C   B 2 14   ? 160.024 180.035 137.886 1.00 55.65  ? 14   C   B "O2'" 1 
ATOM   646   C "C1'" . C   B 2 14   ? 158.404 178.784 136.669 1.00 55.65  ? 14   C   B "C1'" 1 
ATOM   647   N N1    . C   B 2 14   ? 156.965 178.419 136.697 1.00 55.65  ? 14   C   B N1    1 
ATOM   648   C C2    . C   B 2 14   ? 155.984 179.234 137.287 1.00 55.65  ? 14   C   B C2    1 
ATOM   649   O O2    . C   B 2 14   ? 156.291 180.292 137.857 1.00 55.65  ? 14   C   B O2    1 
ATOM   650   N N3    . C   B 2 14   ? 154.690 178.840 137.242 1.00 55.65  ? 14   C   B N3    1 
ATOM   651   C C4    . C   B 2 14   ? 154.344 177.707 136.633 1.00 55.65  ? 14   C   B C4    1 
ATOM   652   N N4    . C   B 2 14   ? 153.052 177.369 136.617 1.00 55.65  ? 14   C   B N4    1 
ATOM   653   C C5    . C   B 2 14   ? 155.310 176.870 136.011 1.00 55.65  ? 14   C   B C5    1 
ATOM   654   C C6    . C   B 2 14   ? 156.585 177.269 136.065 1.00 55.65  ? 14   C   B C6    1 
ATOM   655   P P     . U   B 2 15   ? 160.661 178.852 140.546 1.00 55.85  ? 15   U   B P     1 
ATOM   656   O OP1   . U   B 2 15   ? 159.310 179.334 140.938 1.00 55.85  ? 15   U   B OP1   1 
ATOM   657   O OP2   . U   B 2 15   ? 161.676 179.844 140.118 1.00 55.85  ? 15   U   B OP2   1 
ATOM   658   O "O5'" . U   B 2 15   ? 161.259 178.069 141.796 1.00 55.85  ? 15   U   B "O5'" 1 
ATOM   659   C "C5'" . U   B 2 15   ? 160.754 176.795 142.170 1.00 55.85  ? 15   U   B "C5'" 1 
ATOM   660   C "C4'" . U   B 2 15   ? 159.345 176.890 142.699 1.00 55.85  ? 15   U   B "C4'" 1 
ATOM   661   O "O4'" . U   B 2 15   ? 158.407 176.762 141.601 1.00 55.85  ? 15   U   B "O4'" 1 
ATOM   662   C "C3'" . U   B 2 15   ? 158.914 175.815 143.681 1.00 55.85  ? 15   U   B "C3'" 1 
ATOM   663   O "O3'" . U   B 2 15   ? 159.341 176.085 145.003 1.00 55.85  ? 15   U   B "O3'" 1 
ATOM   664   C "C2'" . U   B 2 15   ? 157.396 175.819 143.536 1.00 55.85  ? 15   U   B "C2'" 1 
ATOM   665   O "O2'" . U   B 2 15   ? 156.826 176.881 144.285 1.00 55.85  ? 15   U   B "O2'" 1 
ATOM   666   C "C1'" . U   B 2 15   ? 157.226 176.134 142.048 1.00 55.85  ? 15   U   B "C1'" 1 
ATOM   667   N N1    . U   B 2 15   ? 156.985 174.918 141.239 1.00 55.85  ? 15   U   B N1    1 
ATOM   668   C C2    . U   B 2 15   ? 155.668 174.558 141.048 1.00 55.85  ? 15   U   B C2    1 
ATOM   669   O O2    . U   B 2 15   ? 154.741 175.198 141.508 1.00 55.85  ? 15   U   B O2    1 
ATOM   670   N N3    . U   B 2 15   ? 155.475 173.430 140.295 1.00 55.85  ? 15   U   B N3    1 
ATOM   671   C C4    . U   B 2 15   ? 156.447 172.637 139.729 1.00 55.85  ? 15   U   B C4    1 
ATOM   672   O O4    . U   B 2 15   ? 156.114 171.647 139.078 1.00 55.85  ? 15   U   B O4    1 
ATOM   673   C C5    . U   B 2 15   ? 157.787 173.073 139.974 1.00 55.85  ? 15   U   B C5    1 
ATOM   674   C C6    . U   B 2 15   ? 158.006 174.172 140.702 1.00 55.85  ? 15   U   B C6    1 
ATOM   675   P P     . U   B 2 16   ? 160.818 175.683 145.486 1.00 50.24  ? 16   U   B P     1 
ATOM   676   O OP1   . U   B 2 16   ? 161.486 176.913 145.979 1.00 50.24  ? 16   U   B OP1   1 
ATOM   677   O OP2   . U   B 2 16   ? 161.459 174.861 144.431 1.00 50.24  ? 16   U   B OP2   1 
ATOM   678   O "O5'" . U   B 2 16   ? 160.564 174.708 146.716 1.00 50.24  ? 16   U   B "O5'" 1 
ATOM   679   C "C5'" . U   B 2 16   ? 160.216 173.349 146.490 1.00 50.24  ? 16   U   B "C5'" 1 
ATOM   680   C "C4'" . U   B 2 16   ? 160.781 172.438 147.550 1.00 50.24  ? 16   U   B "C4'" 1 
ATOM   681   O "O4'" . U   B 2 16   ? 162.233 172.548 147.571 1.00 50.24  ? 16   U   B "O4'" 1 
ATOM   682   C "C3'" . U   B 2 16   ? 160.309 172.712 148.978 1.00 50.24  ? 16   U   B "C3'" 1 
ATOM   683   O "O3'" . U   B 2 16   ? 160.130 171.472 149.656 1.00 50.24  ? 16   U   B "O3'" 1 
ATOM   684   C "C2'" . U   B 2 16   ? 161.490 173.459 149.592 1.00 50.24  ? 16   U   B "C2'" 1 
ATOM   685   O "O2'" . U   B 2 16   ? 161.584 173.356 150.996 1.00 50.24  ? 16   U   B "O2'" 1 
ATOM   686   C "C1'" . U   B 2 16   ? 162.664 172.782 148.895 1.00 50.24  ? 16   U   B "C1'" 1 
ATOM   687   N N1    . U   B 2 16   ? 163.914 173.561 148.878 1.00 50.24  ? 16   U   B N1    1 
ATOM   688   C C2    . U   B 2 16   ? 163.975 174.798 148.261 1.00 50.24  ? 16   U   B C2    1 
ATOM   689   O O2    . U   B 2 16   ? 163.038 175.326 147.694 1.00 50.24  ? 16   U   B O2    1 
ATOM   690   N N3    . U   B 2 16   ? 165.198 175.417 148.322 1.00 50.24  ? 16   U   B N3    1 
ATOM   691   C C4    . U   B 2 16   ? 166.343 174.946 148.925 1.00 50.24  ? 16   U   B C4    1 
ATOM   692   O O4    . U   B 2 16   ? 167.370 175.625 148.893 1.00 50.24  ? 16   U   B O4    1 
ATOM   693   C C5    . U   B 2 16   ? 166.204 173.665 149.542 1.00 50.24  ? 16   U   B C5    1 
ATOM   694   C C6    . U   B 2 16   ? 165.026 173.039 149.496 1.00 50.24  ? 16   U   B C6    1 
ATOM   695   P P     . G   B 2 17   ? 158.651 170.895 149.884 1.00 45.51  ? 17   G   B P     1 
ATOM   696   O OP1   . G   B 2 17   ? 158.216 171.337 151.230 1.00 45.51  ? 17   G   B OP1   1 
ATOM   697   O OP2   . G   B 2 17   ? 158.638 169.455 149.525 1.00 45.51  ? 17   G   B OP2   1 
ATOM   698   O "O5'" . G   B 2 17   ? 157.770 171.680 148.816 1.00 45.51  ? 17   G   B "O5'" 1 
ATOM   699   C "C5'" . G   B 2 17   ? 156.656 171.066 148.187 1.00 45.51  ? 17   G   B "C5'" 1 
ATOM   700   C "C4'" . G   B 2 17   ? 156.523 171.529 146.760 1.00 45.51  ? 17   G   B "C4'" 1 
ATOM   701   O "O4'" . G   B 2 17   ? 157.695 171.121 146.008 1.00 45.51  ? 17   G   B "O4'" 1 
ATOM   702   C "C3'" . G   B 2 17   ? 155.365 170.951 145.965 1.00 45.51  ? 17   G   B "C3'" 1 
ATOM   703   O "O3'" . G   B 2 17   ? 154.126 171.583 146.225 1.00 45.51  ? 17   G   B "O3'" 1 
ATOM   704   C "C2'" . G   B 2 17   ? 155.844 171.117 144.534 1.00 45.51  ? 17   G   B "C2'" 1 
ATOM   705   O "O2'" . G   B 2 17   ? 155.727 172.471 144.126 1.00 45.51  ? 17   G   B "O2'" 1 
ATOM   706   C "C1'" . G   B 2 17   ? 157.325 170.792 144.687 1.00 45.51  ? 17   G   B "C1'" 1 
ATOM   707   N N9    . G   B 2 17   ? 157.581 169.358 144.472 1.00 45.51  ? 17   G   B N9    1 
ATOM   708   C C8    . G   B 2 17   ? 157.884 168.402 145.408 1.00 45.51  ? 17   G   B C8    1 
ATOM   709   N N7    . G   B 2 17   ? 158.045 167.214 144.888 1.00 45.51  ? 17   G   B N7    1 
ATOM   710   C C5    . G   B 2 17   ? 157.831 167.401 143.530 1.00 45.51  ? 17   G   B C5    1 
ATOM   711   C C6    . G   B 2 17   ? 157.869 166.483 142.451 1.00 45.51  ? 17   G   B C6    1 
ATOM   712   O O6    . G   B 2 17   ? 158.107 165.270 142.473 1.00 45.51  ? 17   G   B O6    1 
ATOM   713   N N1    . G   B 2 17   ? 157.590 167.107 141.241 1.00 45.51  ? 17   G   B N1    1 
ATOM   714   C C2    . G   B 2 17   ? 157.311 168.441 141.089 1.00 45.51  ? 17   G   B C2    1 
ATOM   715   N N2    . G   B 2 17   ? 157.067 168.876 139.849 1.00 45.51  ? 17   G   B N2    1 
ATOM   716   N N3    . G   B 2 17   ? 157.274 169.305 142.083 1.00 45.51  ? 17   G   B N3    1 
ATOM   717   C C4    . G   B 2 17   ? 157.541 168.719 143.263 1.00 45.51  ? 17   G   B C4    1 
ATOM   718   P P     . U   B 2 18   ? 152.755 170.785 145.973 1.00 50.27  ? 18   U   B P     1 
ATOM   719   O OP1   . U   B 2 18   ? 151.641 171.587 146.531 1.00 50.27  ? 18   U   B OP1   1 
ATOM   720   O OP2   . U   B 2 18   ? 152.947 169.387 146.429 1.00 50.27  ? 18   U   B OP2   1 
ATOM   721   O "O5'" . U   B 2 18   ? 152.607 170.760 144.388 1.00 50.27  ? 18   U   B "O5'" 1 
ATOM   722   C "C5'" . U   B 2 18   ? 152.491 171.965 143.648 1.00 50.27  ? 18   U   B "C5'" 1 
ATOM   723   C "C4'" . U   B 2 18   ? 152.310 171.695 142.176 1.00 50.27  ? 18   U   B "C4'" 1 
ATOM   724   O "O4'" . U   B 2 18   ? 153.456 170.967 141.664 1.00 50.27  ? 18   U   B "O4'" 1 
ATOM   725   C "C3'" . U   B 2 18   ? 151.126 170.821 141.802 1.00 50.27  ? 18   U   B "C3'" 1 
ATOM   726   O "O3'" . U   B 2 18   ? 149.899 171.527 141.774 1.00 50.27  ? 18   U   B "O3'" 1 
ATOM   727   C "C2'" . U   B 2 18   ? 151.543 170.261 140.450 1.00 50.27  ? 18   U   B "C2'" 1 
ATOM   728   O "O2'" . U   B 2 18   ? 151.357 171.230 139.430 1.00 50.27  ? 18   U   B "O2'" 1 
ATOM   729   C "C1'" . U   B 2 18   ? 153.044 170.065 140.659 1.00 50.27  ? 18   U   B "C1'" 1 
ATOM   730   N N1    . U   B 2 18   ? 153.368 168.689 141.098 1.00 50.27  ? 18   U   B N1    1 
ATOM   731   C C2    . U   B 2 18   ? 153.454 167.706 140.134 1.00 50.27  ? 18   U   B C2    1 
ATOM   732   O O2    . U   B 2 18   ? 153.274 167.926 138.950 1.00 50.27  ? 18   U   B O2    1 
ATOM   733   N N3    . U   B 2 18   ? 153.756 166.453 140.608 1.00 50.27  ? 18   U   B N3    1 
ATOM   734   C C4    . U   B 2 18   ? 153.977 166.095 141.921 1.00 50.27  ? 18   U   B C4    1 
ATOM   735   O O4    . U   B 2 18   ? 154.242 164.927 142.207 1.00 50.27  ? 18   U   B O4    1 
ATOM   736   C C5    . U   B 2 18   ? 153.870 167.169 142.855 1.00 50.27  ? 18   U   B C5    1 
ATOM   737   C C6    . U   B 2 18   ? 153.578 168.397 142.422 1.00 50.27  ? 18   U   B C6    1 
ATOM   738   P P     . A   B 2 19   ? 148.566 170.837 142.342 1.00 50.27  ? 19   A   B P     1 
ATOM   739   O OP1   . A   B 2 19   ? 147.509 171.873 142.416 1.00 50.27  ? 19   A   B OP1   1 
ATOM   740   O OP2   . A   B 2 19   ? 148.923 170.060 143.555 1.00 50.27  ? 19   A   B OP2   1 
ATOM   741   O "O5'" . A   B 2 19   ? 148.161 169.797 141.208 1.00 50.27  ? 19   A   B "O5'" 1 
ATOM   742   C "C5'" . A   B 2 19   ? 147.548 170.234 140.006 1.00 50.27  ? 19   A   B "C5'" 1 
ATOM   743   C "C4'" . A   B 2 19   ? 147.151 169.067 139.139 1.00 50.27  ? 19   A   B "C4'" 1 
ATOM   744   O "O4'" . A   B 2 19   ? 148.334 168.461 138.561 1.00 50.27  ? 19   A   B "O4'" 1 
ATOM   745   C "C3'" . A   B 2 19   ? 146.454 167.919 139.852 1.00 50.27  ? 19   A   B "C3'" 1 
ATOM   746   O "O3'" . A   B 2 19   ? 145.069 168.156 140.040 1.00 50.27  ? 19   A   B "O3'" 1 
ATOM   747   C "C2'" . A   B 2 19   ? 146.754 166.731 138.947 1.00 50.27  ? 19   A   B "C2'" 1 
ATOM   748   O "O2'" . A   B 2 19   ? 145.886 166.726 137.825 1.00 50.27  ? 19   A   B "O2'" 1 
ATOM   749   C "C1'" . A   B 2 19   ? 148.164 167.064 138.462 1.00 50.27  ? 19   A   B "C1'" 1 
ATOM   750   N N9    . A   B 2 19   ? 149.204 166.414 139.278 1.00 50.27  ? 19   A   B N9    1 
ATOM   751   C C8    . A   B 2 19   ? 149.955 167.004 140.260 1.00 50.27  ? 19   A   B C8    1 
ATOM   752   N N7    . A   B 2 19   ? 150.814 166.196 140.825 1.00 50.27  ? 19   A   B N7    1 
ATOM   753   C C5    . A   B 2 19   ? 150.615 164.993 140.169 1.00 50.27  ? 19   A   B C5    1 
ATOM   754   C C6    . A   B 2 19   ? 151.226 163.740 140.314 1.00 50.27  ? 19   A   B C6    1 
ATOM   755   N N6    . A   B 2 19   ? 152.188 163.502 141.201 1.00 50.27  ? 19   A   B N6    1 
ATOM   756   N N1    . A   B 2 19   ? 150.813 162.735 139.514 1.00 50.27  ? 19   A   B N1    1 
ATOM   757   C C2    . A   B 2 19   ? 149.844 162.992 138.627 1.00 50.27  ? 19   A   B C2    1 
ATOM   758   N N3    . A   B 2 19   ? 149.189 164.130 138.400 1.00 50.27  ? 19   A   B N3    1 
ATOM   759   C C4    . A   B 2 19   ? 149.627 165.107 139.213 1.00 50.27  ? 19   A   B C4    1 
ATOM   760   P P     . G   B 2 20   ? 144.265 167.418 141.217 1.00 50.27  ? 20   G   B P     1 
ATOM   761   O OP1   . G   B 2 20   ? 142.875 167.934 141.196 1.00 50.27  ? 20   G   B OP1   1 
ATOM   762   O OP2   . G   B 2 20   ? 145.060 167.488 142.465 1.00 50.27  ? 20   G   B OP2   1 
ATOM   763   O "O5'" . G   B 2 20   ? 144.203 165.901 140.749 1.00 50.27  ? 20   G   B "O5'" 1 
ATOM   764   C "C5'" . G   B 2 20   ? 143.413 165.523 139.635 1.00 50.27  ? 20   G   B "C5'" 1 
ATOM   765   C "C4'" . G   B 2 20   ? 143.652 164.087 139.253 1.00 50.27  ? 20   G   B "C4'" 1 
ATOM   766   O "O4'" . G   B 2 20   ? 145.041 163.899 138.893 1.00 50.27  ? 20   G   B "O4'" 1 
ATOM   767   C "C3'" . G   B 2 20   ? 143.418 163.059 140.345 1.00 50.27  ? 20   G   B "C3'" 1 
ATOM   768   O "O3'" . G   B 2 20   ? 142.053 162.737 140.522 1.00 50.27  ? 20   G   B "O3'" 1 
ATOM   769   C "C2'" . G   B 2 20   ? 144.264 161.885 139.879 1.00 50.27  ? 20   G   B "C2'" 1 
ATOM   770   O "O2'" . G   B 2 20   ? 143.603 161.160 138.854 1.00 50.27  ? 20   G   B "O2'" 1 
ATOM   771   C "C1'" . G   B 2 20   ? 145.458 162.603 139.260 1.00 50.27  ? 20   G   B "C1'" 1 
ATOM   772   N N9    . G   B 2 20   ? 146.591 162.712 140.194 1.00 50.27  ? 20   G   B N9    1 
ATOM   773   C C8    . G   B 2 20   ? 147.009 163.810 140.899 1.00 50.27  ? 20   G   B C8    1 
ATOM   774   N N7    . G   B 2 20   ? 148.061 163.569 141.632 1.00 50.27  ? 20   G   B N7    1 
ATOM   775   C C5    . G   B 2 20   ? 148.347 162.234 141.392 1.00 50.27  ? 20   G   B C5    1 
ATOM   776   C C6    . G   B 2 20   ? 149.375 161.403 141.899 1.00 50.27  ? 20   G   B C6    1 
ATOM   777   O O6    . G   B 2 20   ? 150.272 161.695 142.697 1.00 50.27  ? 20   G   B O6    1 
ATOM   778   N N1    . G   B 2 20   ? 149.291 160.115 141.381 1.00 50.27  ? 20   G   B N1    1 
ATOM   779   C C2    . G   B 2 20   ? 148.345 159.674 140.491 1.00 50.27  ? 20   G   B C2    1 
ATOM   780   N N2    . G   B 2 20   ? 148.415 158.394 140.099 1.00 50.27  ? 20   G   B N2    1 
ATOM   781   N N3    . G   B 2 20   ? 147.385 160.441 140.013 1.00 50.27  ? 20   G   B N3    1 
ATOM   782   C C4    . G   B 2 20   ? 147.450 161.694 140.503 1.00 50.27  ? 20   G   B C4    1 
ATOM   783   P P     . A   B 2 21   ? 141.534 162.229 141.951 1.00 31.04  ? 21   A   B P     1 
ATOM   784   O OP1   . A   B 2 21   ? 140.051 162.231 141.932 1.00 31.04  ? 21   A   B OP1   1 
ATOM   785   O OP2   . A   B 2 21   ? 142.262 162.998 142.990 1.00 31.04  ? 21   A   B OP2   1 
ATOM   786   O "O5'" . A   B 2 21   ? 142.034 160.720 142.031 1.00 31.04  ? 21   A   B "O5'" 1 
ATOM   787   C "C5'" . A   B 2 21   ? 141.629 159.761 141.066 1.00 31.04  ? 21   A   B "C5'" 1 
ATOM   788   C "C4'" . A   B 2 21   ? 142.492 158.527 141.126 1.00 31.04  ? 21   A   B "C4'" 1 
ATOM   789   O "O4'" . A   B 2 21   ? 143.869 158.884 140.850 1.00 31.04  ? 21   A   B "O4'" 1 
ATOM   790   C "C3'" . A   B 2 21   ? 142.548 157.829 142.474 1.00 31.04  ? 21   A   B "C3'" 1 
ATOM   791   O "O3'" . A   B 2 21   ? 141.452 156.957 142.676 1.00 31.04  ? 21   A   B "O3'" 1 
ATOM   792   C "C2'" . A   B 2 21   ? 143.891 157.114 142.432 1.00 31.04  ? 21   A   B "C2'" 1 
ATOM   793   O "O2'" . A   B 2 21   ? 143.792 155.911 141.685 1.00 31.04  ? 21   A   B "O2'" 1 
ATOM   794   C "C1'" . A   B 2 21   ? 144.740 158.103 141.637 1.00 31.04  ? 21   A   B "C1'" 1 
ATOM   795   N N9    . A   B 2 21   ? 145.522 159.008 142.499 1.00 31.04  ? 21   A   B N9    1 
ATOM   796   C C8    . A   B 2 21   ? 145.282 160.337 142.732 1.00 31.04  ? 21   A   B C8    1 
ATOM   797   N N7    . A   B 2 21   ? 146.152 160.905 143.528 1.00 31.04  ? 21   A   B N7    1 
ATOM   798   C C5    . A   B 2 21   ? 147.029 159.880 143.837 1.00 31.04  ? 21   A   B C5    1 
ATOM   799   C C6    . A   B 2 21   ? 148.175 159.839 144.644 1.00 31.04  ? 21   A   B C6    1 
ATOM   800   N N6    . A   B 2 21   ? 148.647 160.894 145.306 1.00 31.04  ? 21   A   B N6    1 
ATOM   801   N N1    . A   B 2 21   ? 148.829 158.664 144.748 1.00 31.04  ? 21   A   B N1    1 
ATOM   802   C C2    . A   B 2 21   ? 148.351 157.607 144.080 1.00 31.04  ? 21   A   B C2    1 
ATOM   803   N N3    . A   B 2 21   ? 147.284 157.521 143.290 1.00 31.04  ? 21   A   B N3    1 
ATOM   804   C C4    . A   B 2 21   ? 146.658 158.706 143.210 1.00 31.04  ? 21   A   B C4    1 
ATOM   805   P P     . U   B 2 22   ? 140.801 156.799 144.133 1.00 50.27  ? 22   U   B P     1 
ATOM   806   O OP1   . U   B 2 22   ? 139.646 155.875 144.023 1.00 50.27  ? 22   U   B OP1   1 
ATOM   807   O OP2   . U   B 2 22   ? 140.607 158.157 144.698 1.00 50.27  ? 22   U   B OP2   1 
ATOM   808   O "O5'" . U   B 2 22   ? 141.933 156.067 144.978 1.00 50.27  ? 22   U   B "O5'" 1 
ATOM   809   C "C5'" . U   B 2 22   ? 142.371 154.762 144.632 1.00 50.27  ? 22   U   B "C5'" 1 
ATOM   810   C "C4'" . U   B 2 22   ? 143.606 154.380 145.404 1.00 50.27  ? 22   U   B "C4'" 1 
ATOM   811   O "O4'" . U   B 2 22   ? 144.705 155.254 145.032 1.00 50.27  ? 22   U   B "O4'" 1 
ATOM   812   C "C3'" . U   B 2 22   ? 143.513 154.534 146.911 1.00 50.27  ? 22   U   B "C3'" 1 
ATOM   813   O "O3'" . U   B 2 22   ? 142.839 153.461 147.540 1.00 50.27  ? 22   U   B "O3'" 1 
ATOM   814   C "C2'" . U   B 2 22   ? 144.973 154.676 147.317 1.00 50.27  ? 22   U   B "C2'" 1 
ATOM   815   O "O2'" . U   B 2 22   ? 145.621 153.414 147.307 1.00 50.27  ? 22   U   B "O2'" 1 
ATOM   816   C "C1'" . U   B 2 22   ? 145.521 155.505 146.157 1.00 50.27  ? 22   U   B "C1'" 1 
ATOM   817   N N1    . U   B 2 22   ? 145.482 156.954 146.454 1.00 50.27  ? 22   U   B N1    1 
ATOM   818   C C2    . U   B 2 22   ? 146.528 157.477 147.181 1.00 50.27  ? 22   U   B C2    1 
ATOM   819   O O2    . U   B 2 22   ? 147.461 156.800 147.570 1.00 50.27  ? 22   U   B O2    1 
ATOM   820   N N3    . U   B 2 22   ? 146.445 158.821 147.434 1.00 50.27  ? 22   U   B N3    1 
ATOM   821   C C4    . U   B 2 22   ? 145.439 159.677 147.043 1.00 50.27  ? 22   U   B C4    1 
ATOM   822   O O4    . U   B 2 22   ? 145.506 160.867 147.348 1.00 50.27  ? 22   U   B O4    1 
ATOM   823   C C5    . U   B 2 22   ? 144.389 159.062 146.296 1.00 50.27  ? 22   U   B C5    1 
ATOM   824   C C6    . U   B 2 22   ? 144.447 157.754 146.035 1.00 50.27  ? 22   U   B C6    1 
ATOM   825   P P     . A   B 2 23   ? 141.407 153.710 148.221 1.00 38.85  ? 23   A   B P     1 
ATOM   826   O OP1   . A   B 2 23   ? 140.370 153.074 147.371 1.00 38.85  ? 23   A   B OP1   1 
ATOM   827   O OP2   . A   B 2 23   ? 141.306 155.152 148.551 1.00 38.85  ? 23   A   B OP2   1 
ATOM   828   O "O5'" . A   B 2 23   ? 141.487 152.899 149.587 1.00 38.85  ? 23   A   B "O5'" 1 
ATOM   829   C "C5'" . A   B 2 23   ? 142.510 153.176 150.536 1.00 38.85  ? 23   A   B "C5'" 1 
ATOM   830   C "C4'" . A   B 2 23   ? 143.193 151.917 151.006 1.00 38.85  ? 23   A   B "C4'" 1 
ATOM   831   O "O4'" . A   B 2 23   ? 142.310 151.195 151.907 1.00 38.85  ? 23   A   B "O4'" 1 
ATOM   832   C "C3'" . A   B 2 23   ? 143.580 150.931 149.905 1.00 38.85  ? 23   A   B "C3'" 1 
ATOM   833   O "O3'" . A   B 2 23   ? 144.810 150.298 150.252 1.00 38.85  ? 23   A   B "O3'" 1 
ATOM   834   C "C2'" . A   B 2 23   ? 142.451 149.907 149.956 1.00 38.85  ? 23   A   B "C2'" 1 
ATOM   835   O "O2'" . A   B 2 23   ? 142.792 148.631 149.459 1.00 38.85  ? 23   A   B "O2'" 1 
ATOM   836   C "C1'" . A   B 2 23   ? 142.146 149.869 151.448 1.00 38.85  ? 23   A   B "C1'" 1 
ATOM   837   N N9    . A   B 2 23   ? 140.787 149.433 151.774 1.00 38.85  ? 23   A   B N9    1 
ATOM   838   C C8    . A   B 2 23   ? 139.693 149.396 150.950 1.00 38.85  ? 23   A   B C8    1 
ATOM   839   N N7    . A   B 2 23   ? 138.609 148.952 151.537 1.00 38.85  ? 23   A   B N7    1 
ATOM   840   C C5    . A   B 2 23   ? 139.019 148.680 152.833 1.00 38.85  ? 23   A   B C5    1 
ATOM   841   C C6    . A   B 2 23   ? 138.339 148.183 153.958 1.00 38.85  ? 23   A   B C6    1 
ATOM   842   N N6    . A   B 2 23   ? 137.045 147.858 153.955 1.00 38.85  ? 23   A   B N6    1 
ATOM   843   N N1    . A   B 2 23   ? 139.040 148.029 155.101 1.00 38.85  ? 23   A   B N1    1 
ATOM   844   C C2    . A   B 2 23   ? 140.337 148.355 155.104 1.00 38.85  ? 23   A   B C2    1 
ATOM   845   N N3    . A   B 2 23   ? 141.086 148.831 154.113 1.00 38.85  ? 23   A   B N3    1 
ATOM   846   C C4    . A   B 2 23   ? 140.358 148.972 152.993 1.00 38.85  ? 23   A   B C4    1 
ATOM   847   P P     . G   B 2 24   ? 146.205 150.928 149.768 1.00 47.08  ? 24   G   B P     1 
ATOM   848   O OP1   . G   B 2 24   ? 145.984 152.358 149.441 1.00 47.08  ? 24   G   B OP1   1 
ATOM   849   O OP2   . G   B 2 24   ? 146.780 150.024 148.741 1.00 47.08  ? 24   G   B OP2   1 
ATOM   850   O "O5'" . G   B 2 24   ? 147.132 150.852 151.060 1.00 47.08  ? 24   G   B "O5'" 1 
ATOM   851   C "C5'" . G   B 2 24   ? 147.943 149.714 151.304 1.00 47.08  ? 24   G   B "C5'" 1 
ATOM   852   C "C4'" . G   B 2 24   ? 147.908 149.304 152.754 1.00 47.08  ? 24   G   B "C4'" 1 
ATOM   853   O "O4'" . G   B 2 24   ? 146.562 149.442 153.267 1.00 47.08  ? 24   G   B "O4'" 1 
ATOM   854   C "C3'" . G   B 2 24   ? 148.276 147.856 153.033 1.00 47.08  ? 24   G   B "C3'" 1 
ATOM   855   O "O3'" . G   B 2 24   ? 149.676 147.670 153.124 1.00 47.08  ? 24   G   B "O3'" 1 
ATOM   856   C "C2'" . G   B 2 24   ? 147.540 147.554 154.332 1.00 47.08  ? 24   G   B "C2'" 1 
ATOM   857   O "O2'" . G   B 2 24   ? 148.278 148.032 155.446 1.00 47.08  ? 24   G   B "O2'" 1 
ATOM   858   C "C1'" . G   B 2 24   ? 146.284 148.413 154.189 1.00 47.08  ? 24   G   B "C1'" 1 
ATOM   859   N N9    . G   B 2 24   ? 145.108 147.669 153.703 1.00 47.08  ? 24   G   B N9    1 
ATOM   860   C C8    . G   B 2 24   ? 144.701 147.551 152.398 1.00 47.08  ? 24   G   B C8    1 
ATOM   861   N N7    . G   B 2 24   ? 143.602 146.862 152.265 1.00 47.08  ? 24   G   B N7    1 
ATOM   862   C C5    . G   B 2 24   ? 143.256 146.515 153.561 1.00 47.08  ? 24   G   B C5    1 
ATOM   863   C C6    . G   B 2 24   ? 142.155 145.766 154.045 1.00 47.08  ? 24   G   B C6    1 
ATOM   864   O O6    . G   B 2 24   ? 141.236 145.243 153.403 1.00 47.08  ? 24   G   B O6    1 
ATOM   865   N N1    . G   B 2 24   ? 142.184 145.652 155.430 1.00 47.08  ? 24   G   B N1    1 
ATOM   866   C C2    . G   B 2 24   ? 143.150 146.188 156.244 1.00 47.08  ? 24   G   B C2    1 
ATOM   867   N N2    . G   B 2 24   ? 143.002 145.968 157.558 1.00 47.08  ? 24   G   B N2    1 
ATOM   868   N N3    . G   B 2 24   ? 144.182 146.890 155.805 1.00 47.08  ? 24   G   B N3    1 
ATOM   869   C C4    . G   B 2 24   ? 144.172 147.012 154.463 1.00 47.08  ? 24   G   B C4    1 
ATOM   870   P P     . C   B 2 25   ? 150.335 146.264 152.721 1.00 66.24  ? 25   C   B P     1 
ATOM   871   O OP1   . C   B 2 25   ? 151.807 146.449 152.671 1.00 66.24  ? 25   C   B OP1   1 
ATOM   872   O OP2   . C   B 2 25   ? 149.616 145.748 151.530 1.00 66.24  ? 25   C   B OP2   1 
ATOM   873   O "O5'" . C   B 2 25   ? 150.000 145.318 153.956 1.00 66.24  ? 25   C   B "O5'" 1 
ATOM   874   C "C5'" . C   B 2 25   ? 150.464 145.628 155.261 1.00 66.24  ? 25   C   B "C5'" 1 
ATOM   875   C "C4'" . C   B 2 25   ? 149.763 144.789 156.299 1.00 66.24  ? 25   C   B "C4'" 1 
ATOM   876   O "O4'" . C   B 2 25   ? 148.345 145.082 156.276 1.00 66.24  ? 25   C   B "O4'" 1 
ATOM   877   C "C3'" . C   B 2 25   ? 149.840 143.284 156.094 1.00 66.24  ? 25   C   B "C3'" 1 
ATOM   878   O "O3'" . C   B 2 25   ? 151.043 142.730 156.599 1.00 66.24  ? 25   C   B "O3'" 1 
ATOM   879   C "C2'" . C   B 2 25   ? 148.595 142.779 156.814 1.00 66.24  ? 25   C   B "C2'" 1 
ATOM   880   O "O2'" . C   B 2 25   ? 148.828 142.684 158.211 1.00 66.24  ? 25   C   B "O2'" 1 
ATOM   881   C "C1'" . C   B 2 25   ? 147.604 143.919 156.567 1.00 66.24  ? 25   C   B "C1'" 1 
ATOM   882   N N1    . C   B 2 25   ? 146.682 143.648 155.441 1.00 66.24  ? 25   C   B N1    1 
ATOM   883   C C2    . C   B 2 25   ? 145.433 143.096 155.732 1.00 66.24  ? 25   C   B C2    1 
ATOM   884   O O2    . C   B 2 25   ? 145.150 142.852 156.914 1.00 66.24  ? 25   C   B O2    1 
ATOM   885   N N3    . C   B 2 25   ? 144.566 142.845 154.726 1.00 66.24  ? 25   C   B N3    1 
ATOM   886   C C4    . C   B 2 25   ? 144.908 143.125 153.470 1.00 66.24  ? 25   C   B C4    1 
ATOM   887   N N4    . C   B 2 25   ? 144.020 142.860 152.510 1.00 66.24  ? 25   C   B N4    1 
ATOM   888   C C5    . C   B 2 25   ? 146.174 143.690 153.141 1.00 66.24  ? 25   C   B C5    1 
ATOM   889   C C6    . C   B 2 25   ? 147.021 143.934 154.149 1.00 66.24  ? 25   C   B C6    1 
ATOM   890   P P     . A   B 2 26   ? 152.244 142.332 155.608 1.00 107.24 ? 26   A   B P     1 
ATOM   891   O OP1   . A   B 2 26   ? 153.514 142.460 156.365 1.00 107.24 ? 26   A   B OP1   1 
ATOM   892   O OP2   . A   B 2 26   ? 152.078 143.068 154.330 1.00 107.24 ? 26   A   B OP2   1 
ATOM   893   O "O5'" . A   B 2 26   ? 151.999 140.788 155.306 1.00 107.24 ? 26   A   B "O5'" 1 
ATOM   894   C "C5'" . A   B 2 26   ? 152.075 139.817 156.338 1.00 107.24 ? 26   A   B "C5'" 1 
ATOM   895   C "C4'" . A   B 2 26   ? 151.360 138.551 155.942 1.00 107.24 ? 26   A   B "C4'" 1 
ATOM   896   O "O4'" . A   B 2 26   ? 149.931 138.786 155.939 1.00 107.24 ? 26   A   B "O4'" 1 
ATOM   897   C "C3'" . A   B 2 26   ? 151.666 138.037 154.543 1.00 107.24 ? 26   A   B "C3'" 1 
ATOM   898   O "O3'" . A   B 2 26   ? 152.841 137.247 154.506 1.00 107.24 ? 26   A   B "O3'" 1 
ATOM   899   C "C2'" . A   B 2 26   ? 150.405 137.267 154.172 1.00 107.24 ? 26   A   B "C2'" 1 
ATOM   900   O "O2'" . A   B 2 26   ? 150.429 135.965 154.738 1.00 107.24 ? 26   A   B "O2'" 1 
ATOM   901   C "C1'" . A   B 2 26   ? 149.322 138.080 154.881 1.00 107.24 ? 26   A   B "C1'" 1 
ATOM   902   N N9    . A   B 2 26   ? 148.651 139.057 154.004 1.00 107.24 ? 26   A   B N9    1 
ATOM   903   C C8    . A   B 2 26   ? 148.893 140.406 153.933 1.00 107.24 ? 26   A   B C8    1 
ATOM   904   N N7    . A   B 2 26   ? 148.125 141.039 153.082 1.00 107.24 ? 26   A   B N7    1 
ATOM   905   C C5    . A   B 2 26   ? 147.313 140.041 152.564 1.00 107.24 ? 26   A   B C5    1 
ATOM   906   C C6    . A   B 2 26   ? 146.282 140.065 151.610 1.00 107.24 ? 26   A   B C6    1 
ATOM   907   N N6    . A   B 2 26   ? 145.879 141.172 150.984 1.00 107.24 ? 26   A   B N6    1 
ATOM   908   N N1    . A   B 2 26   ? 145.672 138.897 151.315 1.00 107.24 ? 26   A   B N1    1 
ATOM   909   C C2    . A   B 2 26   ? 146.080 137.787 151.943 1.00 107.24 ? 26   A   B C2    1 
ATOM   910   N N3    . A   B 2 26   ? 147.036 137.638 152.857 1.00 107.24 ? 26   A   B N3    1 
ATOM   911   C C4    . A   B 2 26   ? 147.622 138.816 153.126 1.00 107.24 ? 26   A   B C4    1 
ATOM   912   P P     . G   B 2 27   ? 153.775 137.230 153.200 1.00 133.70 ? 27   G   B P     1 
ATOM   913   O OP1   . G   B 2 27   ? 155.026 136.508 153.544 1.00 133.70 ? 27   G   B OP1   1 
ATOM   914   O OP2   . G   B 2 27   ? 153.847 138.613 152.664 1.00 133.70 ? 27   G   B OP2   1 
ATOM   915   O "O5'" . G   B 2 27   ? 152.966 136.336 152.161 1.00 133.70 ? 27   G   B "O5'" 1 
ATOM   916   C "C5'" . G   B 2 27   ? 152.646 134.983 152.453 1.00 133.70 ? 27   G   B "C5'" 1 
ATOM   917   C "C4'" . G   B 2 27   ? 151.633 134.444 151.476 1.00 133.70 ? 27   G   B "C4'" 1 
ATOM   918   O "O4'" . G   B 2 27   ? 150.374 135.143 151.648 1.00 133.70 ? 27   G   B "O4'" 1 
ATOM   919   C "C3'" . G   B 2 27   ? 151.977 134.639 150.007 1.00 133.70 ? 27   G   B "C3'" 1 
ATOM   920   O "O3'" . G   B 2 27   ? 152.849 133.635 149.516 1.00 133.70 ? 27   G   B "O3'" 1 
ATOM   921   C "C2'" . G   B 2 27   ? 150.609 134.653 149.337 1.00 133.70 ? 27   G   B "C2'" 1 
ATOM   922   O "O2'" . G   B 2 27   ? 150.113 133.332 149.179 1.00 133.70 ? 27   G   B "O2'" 1 
ATOM   923   C "C1'" . G   B 2 27   ? 149.763 135.362 150.395 1.00 133.70 ? 27   G   B "C1'" 1 
ATOM   924   N N9    . G   B 2 27   ? 149.689 136.819 150.175 1.00 133.70 ? 27   G   B N9    1 
ATOM   925   C C8    . G   B 2 27   ? 150.524 137.766 150.717 1.00 133.70 ? 27   G   B C8    1 
ATOM   926   N N7    . G   B 2 27   ? 150.223 138.985 150.364 1.00 133.70 ? 27   G   B N7    1 
ATOM   927   C C5    . G   B 2 27   ? 149.118 138.837 149.539 1.00 133.70 ? 27   G   B C5    1 
ATOM   928   C C6    . G   B 2 27   ? 148.351 139.815 148.856 1.00 133.70 ? 27   G   B C6    1 
ATOM   929   O O6    . G   B 2 27   ? 148.501 141.043 148.845 1.00 133.70 ? 27   G   B O6    1 
ATOM   930   N N1    . G   B 2 27   ? 147.317 139.235 148.130 1.00 133.70 ? 27   G   B N1    1 
ATOM   931   C C2    . G   B 2 27   ? 147.055 137.889 148.068 1.00 133.70 ? 27   G   B C2    1 
ATOM   932   N N2    . G   B 2 27   ? 146.009 137.528 147.311 1.00 133.70 ? 27   G   B N2    1 
ATOM   933   N N3    . G   B 2 27   ? 147.762 136.966 148.701 1.00 133.70 ? 27   G   B N3    1 
ATOM   934   C C4    . G   B 2 27   ? 148.773 137.506 149.412 1.00 133.70 ? 27   G   B C4    1 
ATOM   935   P P     . A   B 2 28   ? 153.527 133.781 148.067 1.00 154.69 ? 28   A   B P     1 
ATOM   936   O OP1   . A   B 2 28   ? 154.845 133.099 148.110 1.00 154.69 ? 28   A   B OP1   1 
ATOM   937   O OP2   . A   B 2 28   ? 153.453 135.206 147.658 1.00 154.69 ? 28   A   B OP2   1 
ATOM   938   O "O5'" . A   B 2 28   ? 152.568 132.938 147.114 1.00 154.69 ? 28   A   B "O5'" 1 
ATOM   939   C "C5'" . A   B 2 28   ? 152.691 133.012 145.703 1.00 154.69 ? 28   A   B "C5'" 1 
ATOM   940   C "C4'" . A   B 2 28   ? 151.367 132.768 145.026 1.00 154.69 ? 28   A   B "C4'" 1 
ATOM   941   O "O4'" . A   B 2 28   ? 150.330 133.529 145.698 1.00 154.69 ? 28   A   B "O4'" 1 
ATOM   942   C "C3'" . A   B 2 28   ? 151.272 133.211 143.573 1.00 154.69 ? 28   A   B "C3'" 1 
ATOM   943   O "O3'" . A   B 2 28   ? 151.817 132.265 142.670 1.00 154.69 ? 28   A   B "O3'" 1 
ATOM   944   C "C2'" . A   B 2 28   ? 149.779 133.442 143.391 1.00 154.69 ? 28   A   B "C2'" 1 
ATOM   945   O "O2'" . A   B 2 28   ? 149.099 132.208 143.214 1.00 154.69 ? 28   A   B "O2'" 1 
ATOM   946   C "C1'" . A   B 2 28   ? 149.396 134.013 144.756 1.00 154.69 ? 28   A   B "C1'" 1 
ATOM   947   N N9    . A   B 2 28   ? 149.448 135.486 144.770 1.00 154.69 ? 28   A   B N9    1 
ATOM   948   C C8    . A   B 2 28   ? 150.357 136.285 145.418 1.00 154.69 ? 28   A   B C8    1 
ATOM   949   N N7    . A   B 2 28   ? 150.151 137.567 145.246 1.00 154.69 ? 28   A   B N7    1 
ATOM   950   C C5    . A   B 2 28   ? 149.030 137.616 144.429 1.00 154.69 ? 28   A   B C5    1 
ATOM   951   C C6    . A   B 2 28   ? 148.304 138.688 143.881 1.00 154.69 ? 28   A   B C6    1 
ATOM   952   N N6    . A   B 2 28   ? 148.612 139.971 144.083 1.00 154.69 ? 28   A   B N6    1 
ATOM   953   N N1    . A   B 2 28   ? 147.235 138.393 143.108 1.00 154.69 ? 28   A   B N1    1 
ATOM   954   C C2    . A   B 2 28   ? 146.926 137.106 142.905 1.00 154.69 ? 28   A   B C2    1 
ATOM   955   N N3    . A   B 2 28   ? 147.530 136.013 143.364 1.00 154.69 ? 28   A   B N3    1 
ATOM   956   C C4    . A   B 2 28   ? 148.586 136.341 144.128 1.00 154.69 ? 28   A   B C4    1 
ATOM   957   P P     . DA  C 3 10   ? 122.549 128.337 133.967 1.00 210.12 ? 10   DA  D P     1 
ATOM   958   O OP1   . DA  C 3 10   ? 122.319 126.892 133.748 1.00 210.12 ? 10   DA  D OP1   1 
ATOM   959   O OP2   . DA  C 3 10   ? 122.622 129.258 132.811 1.00 210.12 ? 10   DA  D OP2   1 
ATOM   960   O "O5'" . DA  C 3 10   ? 121.439 128.896 134.976 1.00 210.12 ? 10   DA  D "O5'" 1 
ATOM   961   C "C5'" . DA  C 3 10   ? 120.506 129.874 134.534 1.00 210.12 ? 10   DA  D "C5'" 1 
ATOM   962   C "C4'" . DA  C 3 10   ? 119.535 130.238 135.644 1.00 210.12 ? 10   DA  D "C4'" 1 
ATOM   963   O "O4'" . DA  C 3 10   ? 118.714 129.087 135.970 1.00 210.12 ? 10   DA  D "O4'" 1 
ATOM   964   C "C3'" . DA  C 3 10   ? 120.189 130.685 136.959 1.00 210.12 ? 10   DA  D "C3'" 1 
ATOM   965   O "O3'" . DA  C 3 10   ? 119.603 131.904 137.411 1.00 210.12 ? 10   DA  D "O3'" 1 
ATOM   966   C "C2'" . DA  C 3 10   ? 119.890 129.533 137.918 1.00 210.12 ? 10   DA  D "C2'" 1 
ATOM   967   C "C1'" . DA  C 3 10   ? 118.575 129.017 137.365 1.00 210.12 ? 10   DA  D "C1'" 1 
ATOM   968   N N9    . DA  C 3 10   ? 118.284 127.639 137.748 1.00 210.12 ? 10   DA  D N9    1 
ATOM   969   C C8    . DA  C 3 10   ? 119.026 126.526 137.466 1.00 210.12 ? 10   DA  D C8    1 
ATOM   970   N N7    . DA  C 3 10   ? 118.519 125.417 137.950 1.00 210.12 ? 10   DA  D N7    1 
ATOM   971   C C5    . DA  C 3 10   ? 117.365 125.833 138.596 1.00 210.12 ? 10   DA  D C5    1 
ATOM   972   C C6    . DA  C 3 10   ? 116.372 125.136 139.314 1.00 210.12 ? 10   DA  D C6    1 
ATOM   973   N N6    . DA  C 3 10   ? 116.394 123.813 139.506 1.00 210.12 ? 10   DA  D N6    1 
ATOM   974   N N1    . DA  C 3 10   ? 115.354 125.856 139.833 1.00 210.12 ? 10   DA  D N1    1 
ATOM   975   C C2    . DA  C 3 10   ? 115.336 127.179 139.634 1.00 210.12 ? 10   DA  D C2    1 
ATOM   976   N N3    . DA  C 3 10   ? 116.210 127.941 138.982 1.00 210.12 ? 10   DA  D N3    1 
ATOM   977   C C4    . DA  C 3 10   ? 117.209 127.200 138.482 1.00 210.12 ? 10   DA  D C4    1 
ATOM   978   P P     . DG  C 3 11   ? 120.414 132.871 138.408 1.00 211.63 ? 11   DG  D P     1 
ATOM   979   O OP1   . DG  C 3 11   ? 120.849 134.050 137.628 1.00 211.63 ? 11   DG  D OP1   1 
ATOM   980   O OP2   . DG  C 3 11   ? 121.418 132.054 139.124 1.00 211.63 ? 11   DG  D OP2   1 
ATOM   981   O "O5'" . DG  C 3 11   ? 119.319 133.332 139.478 1.00 211.63 ? 11   DG  D "O5'" 1 
ATOM   982   C "C5'" . DG  C 3 11   ? 118.319 134.278 139.115 1.00 211.63 ? 11   DG  D "C5'" 1 
ATOM   983   C "C4'" . DG  C 3 11   ? 117.195 134.312 140.141 1.00 211.63 ? 11   DG  D "C4'" 1 
ATOM   984   O "O4'" . DG  C 3 11   ? 116.682 132.971 140.349 1.00 211.63 ? 11   DG  D "O4'" 1 
ATOM   985   C "C3'" . DG  C 3 11   ? 117.585 134.818 141.524 1.00 211.63 ? 11   DG  D "C3'" 1 
ATOM   986   O "O3'" . DG  C 3 11   ? 116.464 135.462 142.130 1.00 211.63 ? 11   DG  D "O3'" 1 
ATOM   987   C "C2'" . DG  C 3 11   ? 117.958 133.530 142.248 1.00 211.63 ? 11   DG  D "C2'" 1 
ATOM   988   C "C1'" . DG  C 3 11   ? 116.946 132.548 141.675 1.00 211.63 ? 11   DG  D "C1'" 1 
ATOM   989   N N9    . DG  C 3 11   ? 117.431 131.172 141.619 1.00 211.63 ? 11   DG  D N9    1 
ATOM   990   C C8    . DG  C 3 11   ? 118.556 130.721 140.973 1.00 211.63 ? 11   DG  D C8    1 
ATOM   991   N N7    . DG  C 3 11   ? 118.739 129.436 141.082 1.00 211.63 ? 11   DG  D N7    1 
ATOM   992   C C5    . DG  C 3 11   ? 117.663 129.003 141.845 1.00 211.63 ? 11   DG  D C5    1 
ATOM   993   C C6    . DG  C 3 11   ? 117.325 127.702 142.284 1.00 211.63 ? 11   DG  D C6    1 
ATOM   994   O O6    . DG  C 3 11   ? 117.931 126.641 142.090 1.00 211.63 ? 11   DG  D O6    1 
ATOM   995   N N1    . DG  C 3 11   ? 116.155 127.700 143.038 1.00 211.63 ? 11   DG  D N1    1 
ATOM   996   C C2    . DG  C 3 11   ? 115.400 128.813 143.320 1.00 211.63 ? 11   DG  D C2    1 
ATOM   997   N N2    . DG  C 3 11   ? 114.305 128.605 144.067 1.00 211.63 ? 11   DG  D N2    1 
ATOM   998   N N3    . DG  C 3 11   ? 115.704 130.041 142.915 1.00 211.63 ? 11   DG  D N3    1 
ATOM   999   C C4    . DG  C 3 11   ? 116.846 130.059 142.182 1.00 211.63 ? 11   DG  D C4    1 
ATOM   1000  P P     . DA  C 3 12   ? 116.479 135.849 143.691 1.00 205.85 ? 12   DA  D P     1 
ATOM   1001  O OP1   . DA  C 3 12   ? 115.514 136.955 143.876 1.00 205.85 ? 12   DA  D OP1   1 
ATOM   1002  O OP2   . DA  C 3 12   ? 117.884 136.032 144.117 1.00 205.85 ? 12   DA  D OP2   1 
ATOM   1003  O "O5'" . DA  C 3 12   ? 115.898 134.543 144.410 1.00 205.85 ? 12   DA  D "O5'" 1 
ATOM   1004  C "C5'" . DA  C 3 12   ? 115.762 134.504 145.823 1.00 205.85 ? 12   DA  D "C5'" 1 
ATOM   1005  C "C4'" . DA  C 3 12   ? 115.030 133.246 146.254 1.00 205.85 ? 12   DA  D "C4'" 1 
ATOM   1006  O "O4'" . DA  C 3 12   ? 115.548 132.113 145.515 1.00 205.85 ? 12   DA  D "O4'" 1 
ATOM   1007  C "C3'" . DA  C 3 12   ? 115.203 132.873 147.714 1.00 205.85 ? 12   DA  D "C3'" 1 
ATOM   1008  O "O3'" . DA  C 3 12   ? 114.116 132.062 148.135 1.00 205.85 ? 12   DA  D "O3'" 1 
ATOM   1009  C "C2'" . DA  C 3 12   ? 116.503 132.081 147.678 1.00 205.85 ? 12   DA  D "C2'" 1 
ATOM   1010  C "C1'" . DA  C 3 12   ? 116.362 131.320 146.361 1.00 205.85 ? 12   DA  D "C1'" 1 
ATOM   1011  N N9    . DA  C 3 12   ? 117.632 131.087 145.684 1.00 205.85 ? 12   DA  D N9    1 
ATOM   1012  C C8    . DA  C 3 12   ? 118.472 132.031 145.166 1.00 205.85 ? 12   DA  D C8    1 
ATOM   1013  N N7    . DA  C 3 12   ? 119.547 131.532 144.604 1.00 205.85 ? 12   DA  D N7    1 
ATOM   1014  C C5    . DA  C 3 12   ? 119.402 130.165 144.765 1.00 205.85 ? 12   DA  D C5    1 
ATOM   1015  C C6    . DA  C 3 12   ? 120.208 129.074 144.387 1.00 205.85 ? 12   DA  D C6    1 
ATOM   1016  N N6    . DA  C 3 12   ? 121.370 129.207 143.741 1.00 205.85 ? 12   DA  D N6    1 
ATOM   1017  N N1    . DA  C 3 12   ? 119.771 127.837 144.700 1.00 205.85 ? 12   DA  D N1    1 
ATOM   1018  C C2    . DA  C 3 12   ? 118.606 127.708 145.347 1.00 205.85 ? 12   DA  D C2    1 
ATOM   1019  N N3    . DA  C 3 12   ? 117.764 128.656 145.753 1.00 205.85 ? 12   DA  D N3    1 
ATOM   1020  C C4    . DA  C 3 12   ? 118.225 129.873 145.428 1.00 205.85 ? 12   DA  D C4    1 
ATOM   1021  P P     . DT  C 3 13   ? 112.766 132.740 148.682 1.00 189.96 ? 13   DT  D P     1 
ATOM   1022  O OP1   . DT  C 3 13   ? 111.637 132.163 147.917 1.00 189.96 ? 13   DT  D OP1   1 
ATOM   1023  O OP2   . DT  C 3 13   ? 112.971 134.205 148.701 1.00 189.96 ? 13   DT  D OP2   1 
ATOM   1024  O "O5'" . DT  C 3 13   ? 112.670 132.240 150.197 1.00 189.96 ? 13   DT  D "O5'" 1 
ATOM   1025  C "C5'" . DT  C 3 13   ? 113.736 132.497 151.101 1.00 189.96 ? 13   DT  D "C5'" 1 
ATOM   1026  C "C4'" . DT  C 3 13   ? 114.235 131.206 151.724 1.00 189.96 ? 13   DT  D "C4'" 1 
ATOM   1027  O "O4'" . DT  C 3 13   ? 115.350 130.687 150.946 1.00 189.96 ? 13   DT  D "O4'" 1 
ATOM   1028  C "C3'" . DT  C 3 13   ? 114.746 131.338 153.160 1.00 189.96 ? 13   DT  D "C3'" 1 
ATOM   1029  O "O3'" . DT  C 3 13   ? 114.331 130.211 153.925 1.00 189.96 ? 13   DT  D "O3'" 1 
ATOM   1030  C "C2'" . DT  C 3 13   ? 116.259 131.364 152.978 1.00 189.96 ? 13   DT  D "C2'" 1 
ATOM   1031  C "C1'" . DT  C 3 13   ? 116.429 130.413 151.809 1.00 189.96 ? 13   DT  D "C1'" 1 
ATOM   1032  N N1    . DT  C 3 13   ? 117.705 130.609 151.065 1.00 189.96 ? 13   DT  D N1    1 
ATOM   1033  C C2    . DT  C 3 13   ? 118.463 129.511 150.729 1.00 189.96 ? 13   DT  D C2    1 
ATOM   1034  O O2    . DT  C 3 13   ? 118.142 128.369 151.004 1.00 189.96 ? 13   DT  D O2    1 
ATOM   1035  N N3    . DT  C 3 13   ? 119.621 129.798 150.056 1.00 189.96 ? 13   DT  D N3    1 
ATOM   1036  C C4    . DT  C 3 13   ? 120.083 131.050 149.690 1.00 189.96 ? 13   DT  D C4    1 
ATOM   1037  O O4    . DT  C 3 13   ? 121.136 131.209 149.083 1.00 189.96 ? 13   DT  D O4    1 
ATOM   1038  C C5    . DT  C 3 13   ? 119.242 132.157 150.077 1.00 189.96 ? 13   DT  D C5    1 
ATOM   1039  C C7    . DT  C 3 13   ? 119.642 133.562 149.738 1.00 189.96 ? 13   DT  D C7    1 
ATOM   1040  C C6    . DT  C 3 13   ? 118.109 131.886 150.741 1.00 189.96 ? 13   DT  D C6    1 
ATOM   1041  P P     . DG  C 3 14   ? 114.408 130.234 155.531 1.00 179.25 ? 14   DG  D P     1 
ATOM   1042  O OP1   . DG  C 3 14   ? 113.023 130.339 156.038 1.00 179.25 ? 14   DG  D OP1   1 
ATOM   1043  O OP2   . DG  C 3 14   ? 115.415 131.233 155.952 1.00 179.25 ? 14   DG  D OP2   1 
ATOM   1044  O "O5'" . DG  C 3 14   ? 114.981 128.787 155.894 1.00 179.25 ? 14   DG  D "O5'" 1 
ATOM   1045  C "C5'" . DG  C 3 14   ? 115.835 128.119 154.974 1.00 179.25 ? 14   DG  D "C5'" 1 
ATOM   1046  C "C4'" . DG  C 3 14   ? 117.026 127.508 155.685 1.00 179.25 ? 14   DG  D "C4'" 1 
ATOM   1047  O "O4'" . DG  C 3 14   ? 118.215 127.683 154.866 1.00 179.25 ? 14   DG  D "O4'" 1 
ATOM   1048  C "C3'" . DG  C 3 14   ? 117.367 128.145 157.027 1.00 179.25 ? 14   DG  D "C3'" 1 
ATOM   1049  O "O3'" . DG  C 3 14   ? 117.997 127.186 157.865 1.00 179.25 ? 14   DG  D "O3'" 1 
ATOM   1050  C "C2'" . DG  C 3 14   ? 118.340 129.236 156.613 1.00 179.25 ? 14   DG  D "C2'" 1 
ATOM   1051  C "C1'" . DG  C 3 14   ? 119.143 128.501 155.552 1.00 179.25 ? 14   DG  D "C1'" 1 
ATOM   1052  N N9    . DG  C 3 14   ? 119.795 129.384 154.592 1.00 179.25 ? 14   DG  D N9    1 
ATOM   1053  C C8    . DG  C 3 14   ? 119.316 130.572 154.100 1.00 179.25 ? 14   DG  D C8    1 
ATOM   1054  N N7    . DG  C 3 14   ? 120.121 131.146 153.251 1.00 179.25 ? 14   DG  D N7    1 
ATOM   1055  C C5    . DG  C 3 14   ? 121.206 130.284 153.179 1.00 179.25 ? 14   DG  D C5    1 
ATOM   1056  C C6    . DG  C 3 14   ? 122.396 130.379 152.420 1.00 179.25 ? 14   DG  D C6    1 
ATOM   1057  O O6    . DG  C 3 14   ? 122.735 131.274 151.636 1.00 179.25 ? 14   DG  D O6    1 
ATOM   1058  N N1    . DG  C 3 14   ? 123.234 129.291 152.641 1.00 179.25 ? 14   DG  D N1    1 
ATOM   1059  C C2    . DG  C 3 14   ? 122.957 128.243 153.488 1.00 179.25 ? 14   DG  D C2    1 
ATOM   1060  N N2    . DG  C 3 14   ? 123.881 127.277 153.580 1.00 179.25 ? 14   DG  D N2    1 
ATOM   1061  N N3    . DG  C 3 14   ? 121.846 128.145 154.203 1.00 179.25 ? 14   DG  D N3    1 
ATOM   1062  C C4    . DG  C 3 14   ? 121.021 129.196 153.999 1.00 179.25 ? 14   DG  D C4    1 
ATOM   1063  P P     . DA  C 3 15   ? 118.037 127.392 159.458 1.00 166.14 ? 15   DA  D P     1 
ATOM   1064  O OP1   . DA  C 3 15   ? 116.927 126.604 160.037 1.00 166.14 ? 15   DA  D OP1   1 
ATOM   1065  O OP2   . DA  C 3 15   ? 118.136 128.841 159.739 1.00 166.14 ? 15   DA  D OP2   1 
ATOM   1066  O "O5'" . DA  C 3 15   ? 119.423 126.721 159.888 1.00 166.14 ? 15   DA  D "O5'" 1 
ATOM   1067  C "C5'" . DA  C 3 15   ? 119.701 125.376 159.522 1.00 166.14 ? 15   DA  D "C5'" 1 
ATOM   1068  C "C4'" . DA  C 3 15   ? 121.199 125.130 159.445 1.00 166.14 ? 15   DA  D "C4'" 1 
ATOM   1069  O "O4'" . DA  C 3 15   ? 121.759 125.872 158.332 1.00 166.14 ? 15   DA  D "O4'" 1 
ATOM   1070  C "C3'" . DA  C 3 15   ? 121.989 125.548 160.679 1.00 166.14 ? 15   DA  D "C3'" 1 
ATOM   1071  O "O3'" . DA  C 3 15   ? 123.031 124.616 160.924 1.00 166.14 ? 15   DA  D "O3'" 1 
ATOM   1072  C "C2'" . DA  C 3 15   ? 122.537 126.923 160.300 1.00 166.14 ? 15   DA  D "C2'" 1 
ATOM   1073  C "C1'" . DA  C 3 15   ? 122.722 126.800 158.791 1.00 166.14 ? 15   DA  D "C1'" 1 
ATOM   1074  N N9    . DA  C 3 15   ? 122.505 128.057 158.081 1.00 166.14 ? 15   DA  D N9    1 
ATOM   1075  C C8    . DA  C 3 15   ? 121.390 128.844 158.133 1.00 166.14 ? 15   DA  D C8    1 
ATOM   1076  N N7    . DA  C 3 15   ? 121.466 129.920 157.388 1.00 166.14 ? 15   DA  D N7    1 
ATOM   1077  C C5    . DA  C 3 15   ? 122.716 129.833 156.804 1.00 166.14 ? 15   DA  D C5    1 
ATOM   1078  C C6    . DA  C 3 15   ? 123.399 130.670 155.904 1.00 166.14 ? 15   DA  D C6    1 
ATOM   1079  N N6    . DA  C 3 15   ? 122.885 131.805 155.421 1.00 166.14 ? 15   DA  D N6    1 
ATOM   1080  N N1    . DA  C 3 15   ? 124.635 130.295 155.518 1.00 166.14 ? 15   DA  D N1    1 
ATOM   1081  C C2    . DA  C 3 15   ? 125.145 129.157 156.003 1.00 166.14 ? 15   DA  D C2    1 
ATOM   1082  N N3    . DA  C 3 15   ? 124.599 128.290 156.855 1.00 166.14 ? 15   DA  D N3    1 
ATOM   1083  C C4    . DA  C 3 15   ? 123.372 128.690 157.219 1.00 166.14 ? 15   DA  D C4    1 
ATOM   1084  P P     . DG  C 3 16   ? 123.761 124.581 162.354 1.00 154.12 ? 16   DG  D P     1 
ATOM   1085  O OP1   . DG  C 3 16   ? 123.995 123.162 162.703 1.00 154.12 ? 16   DG  D OP1   1 
ATOM   1086  O OP2   . DG  C 3 16   ? 122.993 125.449 163.274 1.00 154.12 ? 16   DG  D OP2   1 
ATOM   1087  O "O5'" . DG  C 3 16   ? 125.168 125.284 162.075 1.00 154.12 ? 16   DG  D "O5'" 1 
ATOM   1088  C "C5'" . DG  C 3 16   ? 126.006 124.790 161.041 1.00 154.12 ? 16   DG  D "C5'" 1 
ATOM   1089  C "C4'" . DG  C 3 16   ? 127.014 125.839 160.614 1.00 154.12 ? 16   DG  D "C4'" 1 
ATOM   1090  O "O4'" . DG  C 3 16   ? 126.359 126.860 159.838 1.00 154.12 ? 16   DG  D "O4'" 1 
ATOM   1091  C "C3'" . DG  C 3 16   ? 127.710 126.573 161.762 1.00 154.12 ? 16   DG  D "C3'" 1 
ATOM   1092  O "O3'" . DG  C 3 16   ? 129.060 126.134 161.863 1.00 154.12 ? 16   DG  D "O3'" 1 
ATOM   1093  C "C2'" . DG  C 3 16   ? 127.618 128.065 161.383 1.00 154.12 ? 16   DG  D "C2'" 1 
ATOM   1094  C "C1'" . DG  C 3 16   ? 127.115 128.032 159.945 1.00 154.12 ? 16   DG  D "C1'" 1 
ATOM   1095  N N9    . DG  C 3 16   ? 126.266 129.168 159.592 1.00 154.12 ? 16   DG  D N9    1 
ATOM   1096  C C8    . DG  C 3 16   ? 124.979 129.401 160.011 1.00 154.12 ? 16   DG  D C8    1 
ATOM   1097  N N7    . DG  C 3 16   ? 124.467 130.499 159.529 1.00 154.12 ? 16   DG  D N7    1 
ATOM   1098  C C5    . DG  C 3 16   ? 125.478 131.028 158.739 1.00 154.12 ? 16   DG  D C5    1 
ATOM   1099  C C6    . DG  C 3 16   ? 125.504 132.210 157.963 1.00 154.12 ? 16   DG  D C6    1 
ATOM   1100  O O6    . DG  C 3 16   ? 124.606 133.049 157.819 1.00 154.12 ? 16   DG  D O6    1 
ATOM   1101  N N1    . DG  C 3 16   ? 126.724 132.375 157.313 1.00 154.12 ? 16   DG  D N1    1 
ATOM   1102  C C2    . DG  C 3 16   ? 127.786 131.507 157.404 1.00 154.12 ? 16   DG  D C2    1 
ATOM   1103  N N2    . DG  C 3 16   ? 128.889 131.823 156.710 1.00 154.12 ? 16   DG  D N2    1 
ATOM   1104  N N3    . DG  C 3 16   ? 127.773 130.395 158.128 1.00 154.12 ? 16   DG  D N3    1 
ATOM   1105  C C4    . DG  C 3 16   ? 126.592 130.221 158.767 1.00 154.12 ? 16   DG  D C4    1 
ATOM   1106  P P     . DA  C 3 17   ? 130.051 126.780 162.950 1.00 140.21 ? 17   DA  D P     1 
ATOM   1107  O OP1   . DA  C 3 17   ? 131.067 125.758 163.285 1.00 140.21 ? 17   DA  D OP1   1 
ATOM   1108  O OP2   . DA  C 3 17   ? 129.232 127.377 164.028 1.00 140.21 ? 17   DA  D OP2   1 
ATOM   1109  O "O5'" . DA  C 3 17   ? 130.767 127.963 162.149 1.00 140.21 ? 17   DA  D "O5'" 1 
ATOM   1110  C "C5'" . DA  C 3 17   ? 131.328 127.709 160.867 1.00 140.21 ? 17   DA  D "C5'" 1 
ATOM   1111  C "C4'" . DA  C 3 17   ? 131.968 128.962 160.296 1.00 140.21 ? 17   DA  D "C4'" 1 
ATOM   1112  O "O4'" . DA  C 3 17   ? 130.937 129.855 159.796 1.00 140.21 ? 17   DA  D "O4'" 1 
ATOM   1113  C "C3'" . DA  C 3 17   ? 132.788 129.778 161.293 1.00 140.21 ? 17   DA  D "C3'" 1 
ATOM   1114  O "O3'" . DA  C 3 17   ? 133.964 130.267 160.665 1.00 140.21 ? 17   DA  D "O3'" 1 
ATOM   1115  C "C2'" . DA  C 3 17   ? 131.840 130.912 161.672 1.00 140.21 ? 17   DA  D "C2'" 1 
ATOM   1116  C "C1'" . DA  C 3 17   ? 131.102 131.135 160.362 1.00 140.21 ? 17   DA  D "C1'" 1 
ATOM   1117  N N9    . DA  C 3 17   ? 129.781 131.736 160.530 1.00 140.21 ? 17   DA  D N9    1 
ATOM   1118  C C8    . DA  C 3 17   ? 128.752 131.258 161.290 1.00 140.21 ? 17   DA  D C8    1 
ATOM   1119  N N7    . DA  C 3 17   ? 127.673 132.001 161.250 1.00 140.21 ? 17   DA  D N7    1 
ATOM   1120  C C5    . DA  C 3 17   ? 128.016 133.040 160.403 1.00 140.21 ? 17   DA  D C5    1 
ATOM   1121  C C6    . DA  C 3 17   ? 127.304 134.167 159.950 1.00 140.21 ? 17   DA  D C6    1 
ATOM   1122  N N6    . DA  C 3 17   ? 126.045 134.432 160.310 1.00 140.21 ? 17   DA  D N6    1 
ATOM   1123  N N1    . DA  C 3 17   ? 127.937 135.011 159.110 1.00 140.21 ? 17   DA  D N1    1 
ATOM   1124  C C2    . DA  C 3 17   ? 129.198 134.741 158.752 1.00 140.21 ? 17   DA  D C2    1 
ATOM   1125  N N3    . DA  C 3 17   ? 129.970 133.715 159.113 1.00 140.21 ? 17   DA  D N3    1 
ATOM   1126  C C4    . DA  C 3 17   ? 129.312 132.894 159.948 1.00 140.21 ? 17   DA  D C4    1 
ATOM   1127  P P     . DC  C 3 18   ? 135.235 130.696 161.549 1.00 119.53 ? 18   DC  D P     1 
ATOM   1128  O OP1   . DC  C 3 18   ? 136.412 129.974 161.020 1.00 119.53 ? 18   DC  D OP1   1 
ATOM   1129  O OP2   . DC  C 3 18   ? 134.867 130.556 162.974 1.00 119.53 ? 18   DC  D OP2   1 
ATOM   1130  O "O5'" . DC  C 3 18   ? 135.404 132.254 161.238 1.00 119.53 ? 18   DC  D "O5'" 1 
ATOM   1131  C "C5'" . DC  C 3 18   ? 135.641 132.686 159.906 1.00 119.53 ? 18   DC  D "C5'" 1 
ATOM   1132  C "C4'" . DC  C 3 18   ? 135.296 134.153 159.747 1.00 119.53 ? 18   DC  D "C4'" 1 
ATOM   1133  O "O4'" . DC  C 3 18   ? 133.857 134.328 159.856 1.00 119.53 ? 18   DC  D "O4'" 1 
ATOM   1134  C "C3'" . DC  C 3 18   ? 135.919 135.081 160.799 1.00 119.53 ? 18   DC  D "C3'" 1 
ATOM   1135  O "O3'" . DC  C 3 18   ? 136.480 136.234 160.174 1.00 119.53 ? 18   DC  D "O3'" 1 
ATOM   1136  C "C2'" . DC  C 3 18   ? 134.733 135.451 161.684 1.00 119.53 ? 18   DC  D "C2'" 1 
ATOM   1137  C "C1'" . DC  C 3 18   ? 133.603 135.440 160.673 1.00 119.53 ? 18   DC  D "C1'" 1 
ATOM   1138  N N1    . DC  C 3 18   ? 132.258 135.303 161.293 1.00 119.53 ? 18   DC  D N1    1 
ATOM   1139  C C2    . DC  C 3 18   ? 131.276 136.249 161.008 1.00 119.53 ? 18   DC  D C2    1 
ATOM   1140  O O2    . DC  C 3 18   ? 131.546 137.174 160.236 1.00 119.53 ? 18   DC  D O2    1 
ATOM   1141  N N3    . DC  C 3 18   ? 130.061 136.134 161.591 1.00 119.53 ? 18   DC  D N3    1 
ATOM   1142  C C4    . DC  C 3 18   ? 129.816 135.120 162.422 1.00 119.53 ? 18   DC  D C4    1 
ATOM   1143  N N4    . DC  C 3 18   ? 128.600 135.041 162.970 1.00 119.53 ? 18   DC  D N4    1 
ATOM   1144  C C5    . DC  C 3 18   ? 130.807 134.144 162.727 1.00 119.53 ? 18   DC  D C5    1 
ATOM   1145  C C6    . DC  C 3 18   ? 132.004 134.276 162.149 1.00 119.53 ? 18   DC  D C6    1 
ATOM   1146  P P     . DG  C 3 19   ? 137.511 137.170 160.978 1.00 97.77  ? 19   DG  D P     1 
ATOM   1147  O OP1   . DG  C 3 19   ? 138.760 137.228 160.188 1.00 97.77  ? 19   DG  D OP1   1 
ATOM   1148  O OP2   . DG  C 3 19   ? 137.557 136.704 162.381 1.00 97.77  ? 19   DG  D OP2   1 
ATOM   1149  O "O5'" . DG  C 3 19   ? 136.825 138.618 160.962 1.00 97.77  ? 19   DG  D "O5'" 1 
ATOM   1150  C "C5'" . DG  C 3 19   ? 137.043 139.497 159.860 1.00 97.77  ? 19   DG  D "C5'" 1 
ATOM   1151  C "C4'" . DG  C 3 19   ? 136.329 140.829 160.056 1.00 97.77  ? 19   DG  D "C4'" 1 
ATOM   1152  O "O4'" . DG  C 3 19   ? 134.907 140.608 160.241 1.00 97.77  ? 19   DG  D "O4'" 1 
ATOM   1153  C "C3'" . DG  C 3 19   ? 136.778 141.650 161.257 1.00 97.77  ? 19   DG  D "C3'" 1 
ATOM   1154  O "O3'" . DG  C 3 19   ? 136.660 143.033 160.955 1.00 97.77  ? 19   DG  D "O3'" 1 
ATOM   1155  C "C2'" . DG  C 3 19   ? 135.784 141.228 162.335 1.00 97.77  ? 19   DG  D "C2'" 1 
ATOM   1156  C "C1'" . DG  C 3 19   ? 134.506 141.050 161.525 1.00 97.77  ? 19   DG  D "C1'" 1 
ATOM   1157  N N9    . DG  C 3 19   ? 133.610 140.043 162.073 1.00 97.77  ? 19   DG  D N9    1 
ATOM   1158  C C8    . DG  C 3 19   ? 133.815 138.689 162.070 1.00 97.77  ? 19   DG  D C8    1 
ATOM   1159  N N7    . DG  C 3 19   ? 132.852 138.016 162.620 1.00 97.77  ? 19   DG  D N7    1 
ATOM   1160  C C5    . DG  C 3 19   ? 131.935 138.980 163.003 1.00 97.77  ? 19   DG  D C5    1 
ATOM   1161  C C6    . DG  C 3 19   ? 130.687 138.835 163.647 1.00 97.77  ? 19   DG  D C6    1 
ATOM   1162  O O6    . DG  C 3 19   ? 130.132 137.792 164.014 1.00 97.77  ? 19   DG  D O6    1 
ATOM   1163  N N1    . DG  C 3 19   ? 130.075 140.062 163.866 1.00 97.77  ? 19   DG  D N1    1 
ATOM   1164  C C2    . DG  C 3 19   ? 130.597 141.280 163.503 1.00 97.77  ? 19   DG  D C2    1 
ATOM   1165  N N2    . DG  C 3 19   ? 129.850 142.354 163.801 1.00 97.77  ? 19   DG  D N2    1 
ATOM   1166  N N3    . DG  C 3 19   ? 131.772 141.433 162.895 1.00 97.77  ? 19   DG  D N3    1 
ATOM   1167  C C4    . DG  C 3 19   ? 132.382 140.240 162.675 1.00 97.77  ? 19   DG  D C4    1 
ATOM   1168  P P     . DA  C 3 20   ? 137.454 144.130 161.818 1.00 74.02  ? 20   DA  D P     1 
ATOM   1169  O OP1   . DA  C 3 20   ? 138.455 144.755 160.927 1.00 74.02  ? 20   DA  D OP1   1 
ATOM   1170  O OP2   . DA  C 3 20   ? 137.893 143.501 163.082 1.00 74.02  ? 20   DA  D OP2   1 
ATOM   1171  O "O5'" . DA  C 3 20   ? 136.334 145.216 162.169 1.00 74.02  ? 20   DA  D "O5'" 1 
ATOM   1172  C "C5'" . DA  C 3 20   ? 135.059 144.796 162.644 1.00 74.02  ? 20   DA  D "C5'" 1 
ATOM   1173  C "C4'" . DA  C 3 20   ? 134.457 145.845 163.558 1.00 74.02  ? 20   DA  D "C4'" 1 
ATOM   1174  O "O4'" . DA  C 3 20   ? 133.324 145.280 164.255 1.00 74.02  ? 20   DA  D "O4'" 1 
ATOM   1175  C "C3'" . DA  C 3 20   ? 135.371 146.308 164.666 1.00 74.02  ? 20   DA  D "C3'" 1 
ATOM   1176  O "O3'" . DA  C 3 20   ? 134.892 147.535 165.194 1.00 74.02  ? 20   DA  D "O3'" 1 
ATOM   1177  C "C2'" . DA  C 3 20   ? 135.219 145.170 165.671 1.00 74.02  ? 20   DA  D "C2'" 1 
ATOM   1178  C "C1'" . DA  C 3 20   ? 133.732 144.835 165.540 1.00 74.02  ? 20   DA  D "C1'" 1 
ATOM   1179  N N9    . DA  C 3 20   ? 133.432 143.410 165.629 1.00 74.02  ? 20   DA  D N9    1 
ATOM   1180  C C8    . DA  C 3 20   ? 134.148 142.381 165.089 1.00 74.02  ? 20   DA  D C8    1 
ATOM   1181  N N7    . DA  C 3 20   ? 133.623 141.199 165.308 1.00 74.02  ? 20   DA  D N7    1 
ATOM   1182  C C5    . DA  C 3 20   ? 132.478 141.474 166.036 1.00 74.02  ? 20   DA  D C5    1 
ATOM   1183  C C6    . DA  C 3 20   ? 131.473 140.646 166.578 1.00 74.02  ? 20   DA  D C6    1 
ATOM   1184  N N6    . DA  C 3 20   ? 131.473 139.315 166.463 1.00 74.02  ? 20   DA  D N6    1 
ATOM   1185  N N1    . DA  C 3 20   ? 130.466 141.241 167.245 1.00 74.02  ? 20   DA  D N1    1 
ATOM   1186  C C2    . DA  C 3 20   ? 130.469 142.572 167.359 1.00 74.02  ? 20   DA  D C2    1 
ATOM   1187  N N3    . DA  C 3 20   ? 131.354 143.453 166.896 1.00 74.02  ? 20   DA  D N3    1 
ATOM   1188  C C4    . DA  C 3 20   ? 132.342 142.832 166.236 1.00 74.02  ? 20   DA  D C4    1 
ATOM   1189  P P     . DC  C 3 21   ? 135.661 148.909 164.871 1.00 54.62  ? 21   DC  D P     1 
ATOM   1190  O OP1   . DC  C 3 21   ? 134.660 149.889 164.399 1.00 54.62  ? 21   DC  D OP1   1 
ATOM   1191  O OP2   . DC  C 3 21   ? 136.828 148.582 164.025 1.00 54.62  ? 21   DC  D OP2   1 
ATOM   1192  O "O5'" . DC  C 3 21   ? 136.204 149.380 166.296 1.00 54.62  ? 21   DC  D "O5'" 1 
ATOM   1193  C "C5'" . DC  C 3 21   ? 136.917 148.468 167.114 1.00 54.62  ? 21   DC  D "C5'" 1 
ATOM   1194  C "C4'" . DC  C 3 21   ? 136.386 148.488 168.533 1.00 54.62  ? 21   DC  D "C4'" 1 
ATOM   1195  O "O4'" . DC  C 3 21   ? 135.466 147.377 168.730 1.00 54.62  ? 21   DC  D "O4'" 1 
ATOM   1196  C "C3'" . DC  C 3 21   ? 137.452 148.333 169.607 1.00 54.62  ? 21   DC  D "C3'" 1 
ATOM   1197  O "O3'" . DC  C 3 21   ? 137.078 149.064 170.751 1.00 54.62  ? 21   DC  D "O3'" 1 
ATOM   1198  C "C2'" . DC  C 3 21   ? 137.422 146.836 169.876 1.00 54.62  ? 21   DC  D "C2'" 1 
ATOM   1199  C "C1'" . DC  C 3 21   ? 135.931 146.565 169.788 1.00 54.62  ? 21   DC  D "C1'" 1 
ATOM   1200  N N1    . DC  C 3 21   ? 135.601 145.146 169.480 1.00 54.62  ? 21   DC  D N1    1 
ATOM   1201  C C2    . DC  C 3 21   ? 134.399 144.595 169.940 1.00 54.62  ? 21   DC  D C2    1 
ATOM   1202  O O2    . DC  C 3 21   ? 133.623 145.294 170.600 1.00 54.62  ? 21   DC  D O2    1 
ATOM   1203  N N3    . DC  C 3 21   ? 134.117 143.304 169.651 1.00 54.62  ? 21   DC  D N3    1 
ATOM   1204  C C4    . DC  C 3 21   ? 134.974 142.577 168.935 1.00 54.62  ? 21   DC  D C4    1 
ATOM   1205  N N4    . DC  C 3 21   ? 134.649 141.307 168.684 1.00 54.62  ? 21   DC  D N4    1 
ATOM   1206  C C5    . DC  C 3 21   ? 136.205 143.116 168.461 1.00 54.62  ? 21   DC  D C5    1 
ATOM   1207  C C6    . DC  C 3 21   ? 136.476 144.392 168.756 1.00 54.62  ? 21   DC  D C6    1 
ATOM   1208  P P     . DA  C 3 22   ? 137.577 150.577 170.940 1.00 46.73  ? 22   DA  D P     1 
ATOM   1209  O OP1   . DA  C 3 22   ? 137.192 151.350 169.740 1.00 46.73  ? 22   DA  D OP1   1 
ATOM   1210  O OP2   . DA  C 3 22   ? 138.993 150.525 171.358 1.00 46.73  ? 22   DA  D OP2   1 
ATOM   1211  O "O5'" . DA  C 3 22   ? 136.735 151.088 172.193 1.00 46.73  ? 22   DA  D "O5'" 1 
ATOM   1212  C "C5'" . DA  C 3 22   ? 137.065 150.620 173.481 1.00 46.73  ? 22   DA  D "C5'" 1 
ATOM   1213  C "C4'" . DA  C 3 22   ? 135.834 150.491 174.351 1.00 46.73  ? 22   DA  D "C4'" 1 
ATOM   1214  O "O4'" . DA  C 3 22   ? 135.112 149.297 173.977 1.00 46.73  ? 22   DA  D "O4'" 1 
ATOM   1215  C "C3'" . DA  C 3 22   ? 136.139 150.318 175.823 1.00 46.73  ? 22   DA  D "C3'" 1 
ATOM   1216  O "O3'" . DA  C 3 22   ? 135.054 150.750 176.615 1.00 46.73  ? 22   DA  D "O3'" 1 
ATOM   1217  C "C2'" . DA  C 3 22   ? 136.355 148.816 175.941 1.00 46.73  ? 22   DA  D "C2'" 1 
ATOM   1218  C "C1'" . DA  C 3 22   ? 135.404 148.250 174.887 1.00 46.73  ? 22   DA  D "C1'" 1 
ATOM   1219  N N9    . DA  C 3 22   ? 135.982 147.139 174.138 1.00 46.73  ? 22   DA  D N9    1 
ATOM   1220  C C8    . DA  C 3 22   ? 137.185 147.126 173.495 1.00 46.73  ? 22   DA  D C8    1 
ATOM   1221  N N7    . DA  C 3 22   ? 137.457 145.989 172.905 1.00 46.73  ? 22   DA  D N7    1 
ATOM   1222  C C5    . DA  C 3 22   ? 136.356 145.201 173.177 1.00 46.73  ? 22   DA  D C5    1 
ATOM   1223  C C6    . DA  C 3 22   ? 136.033 143.879 172.827 1.00 46.73  ? 22   DA  D C6    1 
ATOM   1224  N N6    . DA  C 3 22   ? 136.831 143.104 172.092 1.00 46.73  ? 22   DA  D N6    1 
ATOM   1225  N N1    . DA  C 3 22   ? 134.856 143.384 173.262 1.00 46.73  ? 22   DA  D N1    1 
ATOM   1226  C C2    . DA  C 3 22   ? 134.062 144.172 173.996 1.00 46.73  ? 22   DA  D C2    1 
ATOM   1227  N N3    . DA  C 3 22   ? 134.260 145.431 174.387 1.00 46.73  ? 22   DA  D N3    1 
ATOM   1228  C C4    . DA  C 3 22   ? 135.437 145.890 173.940 1.00 46.73  ? 22   DA  D C4    1 
ATOM   1229  P P     . DA  C 3 23   ? 135.263 150.931 178.195 1.00 49.77  ? 23   DA  D P     1 
ATOM   1230  O OP1   . DA  C 3 23   ? 134.375 152.009 178.670 1.00 49.77  ? 23   DA  D OP1   1 
ATOM   1231  O OP2   . DA  C 3 23   ? 136.718 151.014 178.433 1.00 49.77  ? 23   DA  D OP2   1 
ATOM   1232  O "O5'" . DA  C 3 23   ? 134.775 149.543 178.807 1.00 49.77  ? 23   DA  D "O5'" 1 
ATOM   1233  C "C5'" . DA  C 3 23   ? 133.455 149.094 178.574 1.00 49.77  ? 23   DA  D "C5'" 1 
ATOM   1234  C "C4'" . DA  C 3 23   ? 133.256 147.699 179.135 1.00 49.77  ? 23   DA  D "C4'" 1 
ATOM   1235  O "O4'" . DA  C 3 23   ? 133.966 146.735 178.315 1.00 49.77  ? 23   DA  D "O4'" 1 
ATOM   1236  C "C3'" . DA  C 3 23   ? 133.768 147.492 180.557 1.00 49.77  ? 23   DA  D "C3'" 1 
ATOM   1237  O "O3'" . DA  C 3 23   ? 132.907 146.598 181.228 1.00 49.77  ? 23   DA  D "O3'" 1 
ATOM   1238  C "C2'" . DA  C 3 23   ? 135.141 146.870 180.325 1.00 49.77  ? 23   DA  D "C2'" 1 
ATOM   1239  C "C1'" . DA  C 3 23   ? 134.853 145.992 179.123 1.00 49.77  ? 23   DA  D "C1'" 1 
ATOM   1240  N N9    . DA  C 3 23   ? 136.031 145.669 178.329 1.00 49.77  ? 23   DA  D N9    1 
ATOM   1241  C C8    . DA  C 3 23   ? 137.124 146.456 178.112 1.00 49.77  ? 23   DA  D C8    1 
ATOM   1242  N N7    . DA  C 3 23   ? 138.030 145.903 177.341 1.00 49.77  ? 23   DA  D N7    1 
ATOM   1243  C C5    . DA  C 3 23   ? 137.492 144.666 177.034 1.00 49.77  ? 23   DA  D C5    1 
ATOM   1244  C C6    . DA  C 3 23   ? 137.961 143.593 176.254 1.00 49.77  ? 23   DA  D C6    1 
ATOM   1245  N N6    . DA  C 3 23   ? 139.134 143.603 175.614 1.00 49.77  ? 23   DA  D N6    1 
ATOM   1246  N N1    . DA  C 3 23   ? 137.173 142.504 176.156 1.00 49.77  ? 23   DA  D N1    1 
ATOM   1247  C C2    . DA  C 3 23   ? 136.000 142.497 176.795 1.00 49.77  ? 23   DA  D C2    1 
ATOM   1248  N N3    . DA  C 3 23   ? 135.456 143.440 177.555 1.00 49.77  ? 23   DA  D N3    1 
ATOM   1249  C C4    . DA  C 3 23   ? 136.259 144.509 177.634 1.00 49.77  ? 23   DA  D C4    1 
ATOM   1250  P P     . DA  C 3 24   ? 132.954 146.444 182.824 1.00 56.97  ? 24   DA  D P     1 
ATOM   1251  O OP1   . DA  C 3 24   ? 131.785 147.165 183.370 1.00 56.97  ? 24   DA  D OP1   1 
ATOM   1252  O OP2   . DA  C 3 24   ? 134.311 146.782 183.306 1.00 56.97  ? 24   DA  D OP2   1 
ATOM   1253  O "O5'" . DA  C 3 24   ? 132.724 144.880 183.033 1.00 56.97  ? 24   DA  D "O5'" 1 
ATOM   1254  C "C5'" . DA  C 3 24   ? 131.715 144.223 182.286 1.00 56.97  ? 24   DA  D "C5'" 1 
ATOM   1255  C "C4'" . DA  C 3 24   ? 132.059 142.763 182.057 1.00 56.97  ? 24   DA  D "C4'" 1 
ATOM   1256  O "O4'" . DA  C 3 24   ? 133.185 142.652 181.153 1.00 56.97  ? 24   DA  D "O4'" 1 
ATOM   1257  C "C3'" . DA  C 3 24   ? 132.441 141.981 183.304 1.00 56.97  ? 24   DA  D "C3'" 1 
ATOM   1258  O "O3'" . DA  C 3 24   ? 131.915 140.674 183.206 1.00 56.97  ? 24   DA  D "O3'" 1 
ATOM   1259  C "C2'" . DA  C 3 24   ? 133.969 141.985 183.262 1.00 56.97  ? 24   DA  D "C2'" 1 
ATOM   1260  C "C1'" . DA  C 3 24   ? 134.234 141.931 181.766 1.00 56.97  ? 24   DA  D "C1'" 1 
ATOM   1261  N N9    . DA  C 3 24   ? 135.484 142.559 181.359 1.00 56.97  ? 24   DA  D N9    1 
ATOM   1262  C C8    . DA  C 3 24   ? 135.912 143.814 181.680 1.00 56.97  ? 24   DA  D C8    1 
ATOM   1263  N N7    . DA  C 3 24   ? 137.068 144.131 181.150 1.00 56.97  ? 24   DA  D N7    1 
ATOM   1264  C C5    . DA  C 3 24   ? 137.418 143.009 180.422 1.00 56.97  ? 24   DA  D C5    1 
ATOM   1265  C C6    . DA  C 3 24   ? 138.537 142.708 179.625 1.00 56.97  ? 24   DA  D C6    1 
ATOM   1266  N N6    . DA  C 3 24   ? 139.550 143.559 179.429 1.00 56.97  ? 24   DA  D N6    1 
ATOM   1267  N N1    . DA  C 3 24   ? 138.578 141.497 179.036 1.00 56.97  ? 24   DA  D N1    1 
ATOM   1268  C C2    . DA  C 3 24   ? 137.563 140.648 179.235 1.00 56.97  ? 24   DA  D C2    1 
ATOM   1269  N N3    . DA  C 3 24   ? 136.458 140.820 179.960 1.00 56.97  ? 24   DA  D N3    1 
ATOM   1270  C C4    . DA  C 3 24   ? 136.449 142.032 180.533 1.00 56.97  ? 24   DA  D C4    1 
ATOM   1271  P P     . DG  C 3 25   ? 131.855 139.723 184.494 1.00 66.00  ? 25   DG  D P     1 
ATOM   1272  O OP1   . DG  C 3 25   ? 130.600 138.942 184.421 1.00 66.00  ? 25   DG  D OP1   1 
ATOM   1273  O OP2   . DG  C 3 25   ? 132.137 140.555 185.684 1.00 66.00  ? 25   DG  D OP2   1 
ATOM   1274  O "O5'" . DG  C 3 25   ? 133.091 138.743 184.275 1.00 66.00  ? 25   DG  D "O5'" 1 
ATOM   1275  C "C5'" . DG  C 3 25   ? 133.448 138.345 182.960 1.00 66.00  ? 25   DG  D "C5'" 1 
ATOM   1276  C "C4'" . DG  C 3 25   ? 134.837 137.747 182.952 1.00 66.00  ? 25   DG  D "C4'" 1 
ATOM   1277  O "O4'" . DG  C 3 25   ? 135.799 138.742 182.515 1.00 66.00  ? 25   DG  D "O4'" 1 
ATOM   1278  C "C3'" . DG  C 3 25   ? 135.323 137.261 184.323 1.00 66.00  ? 25   DG  D "C3'" 1 
ATOM   1279  O "O3'" . DG  C 3 25   ? 135.835 135.946 184.219 1.00 66.00  ? 25   DG  D "O3'" 1 
ATOM   1280  C "C2'" . DG  C 3 25   ? 136.421 138.260 184.684 1.00 66.00  ? 25   DG  D "C2'" 1 
ATOM   1281  C "C1'" . DG  C 3 25   ? 136.945 138.608 183.308 1.00 66.00  ? 25   DG  D "C1'" 1 
ATOM   1282  N N9    . DG  C 3 25   ? 137.730 139.839 183.263 1.00 66.00  ? 25   DG  D N9    1 
ATOM   1283  C C8    . DG  C 3 25   ? 137.495 141.011 183.940 1.00 66.00  ? 25   DG  D C8    1 
ATOM   1284  N N7    . DG  C 3 25   ? 138.393 141.932 183.705 1.00 66.00  ? 25   DG  D N7    1 
ATOM   1285  C C5    . DG  C 3 25   ? 139.277 141.326 182.821 1.00 66.00  ? 25   DG  D C5    1 
ATOM   1286  C C6    . DG  C 3 25   ? 140.456 141.826 182.208 1.00 66.00  ? 25   DG  D C6    1 
ATOM   1287  O O6    . DG  C 3 25   ? 140.977 142.947 182.322 1.00 66.00  ? 25   DG  D O6    1 
ATOM   1288  N N1    . DG  C 3 25   ? 141.044 140.873 181.383 1.00 66.00  ? 25   DG  D N1    1 
ATOM   1289  C C2    . DG  C 3 25   ? 140.559 139.603 181.180 1.00 66.00  ? 25   DG  D C2    1 
ATOM   1290  N N2    . DG  C 3 25   ? 141.254 138.820 180.351 1.00 66.00  ? 25   DG  D N2    1 
ATOM   1291  N N3    . DG  C 3 25   ? 139.466 139.129 181.744 1.00 66.00  ? 25   DG  D N3    1 
ATOM   1292  C C4    . DG  C 3 25   ? 138.880 140.038 182.548 1.00 66.00  ? 25   DG  D C4    1 
ATOM   1293  P P     . DC  C 3 26   ? 135.347 134.814 185.246 1.00 84.16  ? 26   DC  D P     1 
ATOM   1294  O OP1   . DC  C 3 26   ? 133.959 134.461 184.889 1.00 84.16  ? 26   DC  D OP1   1 
ATOM   1295  O OP2   . DC  C 3 26   ? 135.657 135.281 186.614 1.00 84.16  ? 26   DC  D OP2   1 
ATOM   1296  O "O5'" . DC  C 3 26   ? 136.295 133.571 184.927 1.00 84.16  ? 26   DC  D "O5'" 1 
ATOM   1297  C "C5'" . DC  C 3 26   ? 137.611 133.535 185.453 1.00 84.16  ? 26   DC  D "C5'" 1 
ATOM   1298  C "C4'" . DC  C 3 26   ? 138.641 133.651 184.346 1.00 84.16  ? 26   DC  D "C4'" 1 
ATOM   1299  O "O4'" . DC  C 3 26   ? 138.912 135.054 184.082 1.00 84.16  ? 26   DC  D "O4'" 1 
ATOM   1300  C "C3'" . DC  C 3 26   ? 139.990 133.011 184.667 1.00 84.16  ? 26   DC  D "C3'" 1 
ATOM   1301  O "O3'" . DC  C 3 26   ? 140.501 132.337 183.527 1.00 84.16  ? 26   DC  D "O3'" 1 
ATOM   1302  C "C2'" . DC  C 3 26   ? 140.858 134.203 185.049 1.00 84.16  ? 26   DC  D "C2'" 1 
ATOM   1303  C "C1'" . DC  C 3 26   ? 140.302 135.284 184.141 1.00 84.16  ? 26   DC  D "C1'" 1 
ATOM   1304  N N1    . DC  C 3 26   ? 140.537 136.661 184.655 1.00 84.16  ? 26   DC  D N1    1 
ATOM   1305  C C2    . DC  C 3 26   ? 141.699 137.345 184.288 1.00 84.16  ? 26   DC  D C2    1 
ATOM   1306  O O2    . DC  C 3 26   ? 142.508 136.789 183.537 1.00 84.16  ? 26   DC  D O2    1 
ATOM   1307  N N3    . DC  C 3 26   ? 141.903 138.596 184.766 1.00 84.16  ? 26   DC  D N3    1 
ATOM   1308  C C4    . DC  C 3 26   ? 141.002 139.155 185.574 1.00 84.16  ? 26   DC  D C4    1 
ATOM   1309  N N4    . DC  C 3 26   ? 141.243 140.391 186.023 1.00 84.16  ? 26   DC  D N4    1 
ATOM   1310  C C5    . DC  C 3 26   ? 139.812 138.471 185.961 1.00 84.16  ? 26   DC  D C5    1 
ATOM   1311  C C6    . DC  C 3 26   ? 139.625 137.238 185.484 1.00 84.16  ? 26   DC  D C6    1 
ATOM   1312  P P     . DA  C 3 27   ? 141.513 131.104 183.714 1.00 113.61 ? 27   DA  D P     1 
ATOM   1313  O OP1   . DA  C 3 27   ? 141.092 130.026 182.792 1.00 113.61 ? 27   DA  D OP1   1 
ATOM   1314  O OP2   . DA  C 3 27   ? 141.617 130.835 185.166 1.00 113.61 ? 27   DA  D OP2   1 
ATOM   1315  O "O5'" . DA  C 3 27   ? 142.923 131.681 183.231 1.00 113.61 ? 27   DA  D "O5'" 1 
ATOM   1316  C "C5'" . DA  C 3 27   ? 144.098 130.898 183.389 1.00 113.61 ? 27   DA  D "C5'" 1 
ATOM   1317  C "C4'" . DA  C 3 27   ? 145.317 131.640 182.872 1.00 113.61 ? 27   DA  D "C4'" 1 
ATOM   1318  O "O4'" . DA  C 3 27   ? 145.124 133.068 183.053 1.00 113.61 ? 27   DA  D "O4'" 1 
ATOM   1319  C "C3'" . DA  C 3 27   ? 146.613 131.318 183.601 1.00 113.61 ? 27   DA  D "C3'" 1 
ATOM   1320  O "O3'" . DA  C 3 27   ? 147.724 131.545 182.740 1.00 113.61 ? 27   DA  D "O3'" 1 
ATOM   1321  C "C2'" . DA  C 3 27   ? 146.578 132.330 184.735 1.00 113.61 ? 27   DA  D "C2'" 1 
ATOM   1322  C "C1'" . DA  C 3 27   ? 146.054 133.555 184.003 1.00 113.61 ? 27   DA  D "C1'" 1 
ATOM   1323  N N9    . DA  C 3 27   ? 145.376 134.511 184.869 1.00 113.61 ? 27   DA  D N9    1 
ATOM   1324  C C8    . DA  C 3 27   ? 144.173 134.347 185.492 1.00 113.61 ? 27   DA  D C8    1 
ATOM   1325  N N7    . DA  C 3 27   ? 143.803 135.381 186.210 1.00 113.61 ? 27   DA  D N7    1 
ATOM   1326  C C5    . DA  C 3 27   ? 144.836 136.286 186.044 1.00 113.61 ? 27   DA  D C5    1 
ATOM   1327  C C6    . DA  C 3 27   ? 145.051 137.583 186.548 1.00 113.61 ? 27   DA  D C6    1 
ATOM   1328  N N6    . DA  C 3 27   ? 144.189 138.206 187.355 1.00 113.61 ? 27   DA  D N6    1 
ATOM   1329  N N1    . DA  C 3 27   ? 146.188 138.216 186.189 1.00 113.61 ? 27   DA  D N1    1 
ATOM   1330  C C2    . DA  C 3 27   ? 147.047 137.584 185.381 1.00 113.61 ? 27   DA  D C2    1 
ATOM   1331  N N3    . DA  C 3 27   ? 146.954 136.367 184.845 1.00 113.61 ? 27   DA  D N3    1 
ATOM   1332  C C4    . DA  C 3 27   ? 145.814 135.767 185.220 1.00 113.61 ? 27   DA  D C4    1 
ATOM   1333  P P     . DC  C 3 28   ? 149.142 130.848 183.038 1.00 139.22 ? 28   DC  D P     1 
ATOM   1334  O OP1   . DC  C 3 28   ? 150.168 131.581 182.263 1.00 139.22 ? 28   DC  D OP1   1 
ATOM   1335  O OP2   . DC  C 3 28   ? 148.974 129.392 182.840 1.00 139.22 ? 28   DC  D OP2   1 
ATOM   1336  O "O5'" . DC  C 3 28   ? 149.382 131.107 184.600 1.00 139.22 ? 28   DC  D "O5'" 1 
ATOM   1337  C "C5'" . DC  C 3 28   ? 150.701 131.222 185.116 1.00 139.22 ? 28   DC  D "C5'" 1 
ATOM   1338  C "C4'" . DC  C 3 28   ? 151.140 132.675 185.149 1.00 139.22 ? 28   DC  D "C4'" 1 
ATOM   1339  O "O4'" . DC  C 3 28   ? 150.002 133.519 185.470 1.00 139.22 ? 28   DC  D "O4'" 1 
ATOM   1340  C "C3'" . DC  C 3 28   ? 152.217 133.001 186.184 1.00 139.22 ? 28   DC  D "C3'" 1 
ATOM   1341  O "O3'" . DC  C 3 28   ? 153.148 133.929 185.641 1.00 139.22 ? 28   DC  D "O3'" 1 
ATOM   1342  C "C2'" . DC  C 3 28   ? 151.416 133.619 187.326 1.00 139.22 ? 28   DC  D "C2'" 1 
ATOM   1343  C "C1'" . DC  C 3 28   ? 150.326 134.351 186.561 1.00 139.22 ? 28   DC  D "C1'" 1 
ATOM   1344  N N1    . DC  C 3 28   ? 149.092 134.588 187.360 1.00 139.22 ? 28   DC  D N1    1 
ATOM   1345  C C2    . DC  C 3 28   ? 148.928 135.802 188.031 1.00 139.22 ? 28   DC  D C2    1 
ATOM   1346  O O2    . DC  C 3 28   ? 149.807 136.662 187.944 1.00 139.22 ? 28   DC  D O2    1 
ATOM   1347  N N3    . DC  C 3 28   ? 147.800 136.008 188.751 1.00 139.22 ? 28   DC  D N3    1 
ATOM   1348  C C4    . DC  C 3 28   ? 146.869 135.056 188.821 1.00 139.22 ? 28   DC  D C4    1 
ATOM   1349  N N4    . DC  C 3 28   ? 145.774 135.306 189.547 1.00 139.22 ? 28   DC  D N4    1 
ATOM   1350  C C5    . DC  C 3 28   ? 147.019 133.810 188.146 1.00 139.22 ? 28   DC  D C5    1 
ATOM   1351  C C6    . DC  C 3 28   ? 148.136 133.621 187.436 1.00 139.22 ? 28   DC  D C6    1 
ATOM   1352  P P     . DT  C 3 29   ? 154.727 133.691 185.822 1.00 161.53 ? 29   DT  D P     1 
ATOM   1353  O OP1   . DT  C 3 29   ? 155.367 133.948 184.514 1.00 161.53 ? 29   DT  D OP1   1 
ATOM   1354  O OP2   . DT  C 3 29   ? 154.912 132.383 186.489 1.00 161.53 ? 29   DT  D OP2   1 
ATOM   1355  O "O5'" . DT  C 3 29   ? 155.176 134.835 186.847 1.00 161.53 ? 29   DT  D "O5'" 1 
ATOM   1356  C "C5'" . DT  C 3 29   ? 154.740 134.793 188.202 1.00 161.53 ? 29   DT  D "C5'" 1 
ATOM   1357  C "C4'" . DT  C 3 29   ? 154.607 136.195 188.767 1.00 161.53 ? 29   DT  D "C4'" 1 
ATOM   1358  O "O4'" . DT  C 3 29   ? 153.208 136.471 189.051 1.00 161.53 ? 29   DT  D "O4'" 1 
ATOM   1359  C "C3'" . DT  C 3 29   ? 155.358 136.440 190.075 1.00 161.53 ? 29   DT  D "C3'" 1 
ATOM   1360  O "O3'" . DT  C 3 29   ? 155.907 137.752 190.082 1.00 161.53 ? 29   DT  D "O3'" 1 
ATOM   1361  C "C2'" . DT  C 3 29   ? 154.266 136.287 191.126 1.00 161.53 ? 29   DT  D "C2'" 1 
ATOM   1362  C "C1'" . DT  C 3 29   ? 153.072 136.877 190.394 1.00 161.53 ? 29   DT  D "C1'" 1 
ATOM   1363  N N1    . DT  C 3 29   ? 151.765 136.390 190.908 1.00 161.53 ? 29   DT  D N1    1 
ATOM   1364  C C2    . DT  C 3 29   ? 151.030 137.199 191.739 1.00 161.53 ? 29   DT  D C2    1 
ATOM   1365  O O2    . DT  C 3 29   ? 151.392 138.312 192.077 1.00 161.53 ? 29   DT  D O2    1 
ATOM   1366  N N3    . DT  C 3 29   ? 149.844 136.664 192.158 1.00 161.53 ? 29   DT  D N3    1 
ATOM   1367  C C4    . DT  C 3 29   ? 149.334 135.418 191.843 1.00 161.53 ? 29   DT  D C4    1 
ATOM   1368  O O4    . DT  C 3 29   ? 148.256 135.025 192.273 1.00 161.53 ? 29   DT  D O4    1 
ATOM   1369  C C5    . DT  C 3 29   ? 150.155 134.617 190.968 1.00 161.53 ? 29   DT  D C5    1 
ATOM   1370  C C7    . DT  C 3 29   ? 149.704 133.248 190.556 1.00 161.53 ? 29   DT  D C7    1 
ATOM   1371  C C6    . DT  C 3 29   ? 151.319 135.135 190.548 1.00 161.53 ? 29   DT  D C6    1 
ATOM   1372  P P     . DA  C 3 30   ? 156.848 138.229 191.295 1.00 177.49 ? 30   DA  D P     1 
ATOM   1373  O OP1   . DA  C 3 30   ? 157.696 139.333 190.795 1.00 177.49 ? 30   DA  D OP1   1 
ATOM   1374  O OP2   . DA  C 3 30   ? 157.475 137.023 191.880 1.00 177.49 ? 30   DA  D OP2   1 
ATOM   1375  O "O5'" . DA  C 3 30   ? 155.822 138.816 192.371 1.00 177.49 ? 30   DA  D "O5'" 1 
ATOM   1376  C "C5'" . DA  C 3 30   ? 156.276 139.158 193.674 1.00 177.49 ? 30   DA  D "C5'" 1 
ATOM   1377  C "C4'" . DA  C 3 30   ? 155.314 140.123 194.343 1.00 177.49 ? 30   DA  D "C4'" 1 
ATOM   1378  O "O4'" . DA  C 3 30   ? 153.954 139.636 194.189 1.00 177.49 ? 30   DA  D "O4'" 1 
ATOM   1379  C "C3'" . DA  C 3 30   ? 155.530 140.313 195.844 1.00 177.49 ? 30   DA  D "C3'" 1 
ATOM   1380  O "O3'" . DA  C 3 30   ? 155.314 141.673 196.198 1.00 177.49 ? 30   DA  D "O3'" 1 
ATOM   1381  C "C2'" . DA  C 3 30   ? 154.473 139.401 196.459 1.00 177.49 ? 30   DA  D "C2'" 1 
ATOM   1382  C "C1'" . DA  C 3 30   ? 153.340 139.538 195.454 1.00 177.49 ? 30   DA  D "C1'" 1 
ATOM   1383  N N9    . DA  C 3 30   ? 152.431 138.395 195.440 1.00 177.49 ? 30   DA  D N9    1 
ATOM   1384  C C8    . DA  C 3 30   ? 152.586 137.226 194.749 1.00 177.49 ? 30   DA  D C8    1 
ATOM   1385  N N7    . DA  C 3 30   ? 151.605 136.373 194.928 1.00 177.49 ? 30   DA  D N7    1 
ATOM   1386  C C5    . DA  C 3 30   ? 150.749 137.028 195.798 1.00 177.49 ? 30   DA  D C5    1 
ATOM   1387  C C6    . DA  C 3 30   ? 149.520 136.658 196.379 1.00 177.49 ? 30   DA  D C6    1 
ATOM   1388  N N6    . DA  C 3 30   ? 148.926 135.482 196.153 1.00 177.49 ? 30   DA  D N6    1 
ATOM   1389  N N1    . DA  C 3 30   ? 148.927 137.545 197.211 1.00 177.49 ? 30   DA  D N1    1 
ATOM   1390  C C2    . DA  C 3 30   ? 149.527 138.722 197.422 1.00 177.49 ? 30   DA  D C2    1 
ATOM   1391  N N3    . DA  C 3 30   ? 150.679 139.178 196.937 1.00 177.49 ? 30   DA  D N3    1 
ATOM   1392  C C4    . DA  C 3 30   ? 151.244 138.275 196.123 1.00 177.49 ? 30   DA  D C4    1 
ATOM   1393  N N     . THR D 4 5    ? 113.646 162.950 142.717 1.00 31.44  ? 2    THR A N     1 
ATOM   1394  C CA    . THR D 4 5    ? 114.899 162.269 143.018 1.00 31.44  ? 2    THR A CA    1 
ATOM   1395  C C     . THR D 4 5    ? 116.073 162.962 142.337 1.00 31.44  ? 2    THR A C     1 
ATOM   1396  O O     . THR D 4 5    ? 116.408 162.654 141.195 1.00 31.44  ? 2    THR A O     1 
ATOM   1397  C CB    . THR D 4 5    ? 114.860 160.796 142.580 1.00 31.44  ? 2    THR A CB    1 
ATOM   1398  O OG1   . THR D 4 5    ? 113.595 160.224 142.935 1.00 31.44  ? 2    THR A OG1   1 
ATOM   1399  C CG2   . THR D 4 5    ? 115.972 160.012 143.257 1.00 31.44  ? 2    THR A CG2   1 
ATOM   1400  N N     . GLN D 4 6    ? 116.695 163.899 143.046 1.00 29.96  ? 3    GLN A N     1 
ATOM   1401  C CA    . GLN D 4 6    ? 117.806 164.650 142.485 1.00 29.96  ? 3    GLN A CA    1 
ATOM   1402  C C     . GLN D 4 6    ? 119.029 163.759 142.301 1.00 29.96  ? 3    GLN A C     1 
ATOM   1403  O O     . GLN D 4 6    ? 119.212 162.761 143.003 1.00 29.96  ? 3    GLN A O     1 
ATOM   1404  C CB    . GLN D 4 6    ? 118.158 165.833 143.387 1.00 29.96  ? 3    GLN A CB    1 
ATOM   1405  C CG    . GLN D 4 6    ? 117.063 166.877 143.497 1.00 29.96  ? 3    GLN A CG    1 
ATOM   1406  C CD    . GLN D 4 6    ? 116.852 167.637 142.203 1.00 29.96  ? 3    GLN A CD    1 
ATOM   1407  O OE1   . GLN D 4 6    ? 115.881 167.403 141.484 1.00 29.96  ? 3    GLN A OE1   1 
ATOM   1408  N NE2   . GLN D 4 6    ? 117.762 168.555 141.902 1.00 29.96  ? 3    GLN A NE2   1 
ATOM   1409  N N     . PHE D 4 7    ? 119.869 164.130 141.330 1.00 26.80  ? 4    PHE A N     1 
ATOM   1410  C CA    . PHE D 4 7    ? 121.141 163.440 141.147 1.00 26.80  ? 4    PHE A CA    1 
ATOM   1411  C C     . PHE D 4 7    ? 122.036 163.605 142.365 1.00 26.80  ? 4    PHE A C     1 
ATOM   1412  O O     . PHE D 4 7    ? 122.864 162.734 142.651 1.00 26.80  ? 4    PHE A O     1 
ATOM   1413  C CB    . PHE D 4 7    ? 121.841 163.961 139.890 1.00 26.80  ? 4    PHE A CB    1 
ATOM   1414  C CG    . PHE D 4 7    ? 123.249 163.458 139.717 1.00 26.80  ? 4    PHE A CG    1 
ATOM   1415  C CD1   . PHE D 4 7    ? 123.495 162.249 139.091 1.00 26.80  ? 4    PHE A CD1   1 
ATOM   1416  C CD2   . PHE D 4 7    ? 124.326 164.204 140.159 1.00 26.80  ? 4    PHE A CD2   1 
ATOM   1417  C CE1   . PHE D 4 7    ? 124.786 161.791 138.922 1.00 26.80  ? 4    PHE A CE1   1 
ATOM   1418  C CE2   . PHE D 4 7    ? 125.618 163.747 139.994 1.00 26.80  ? 4    PHE A CE2   1 
ATOM   1419  C CZ    . PHE D 4 7    ? 125.847 162.539 139.375 1.00 26.80  ? 4    PHE A CZ    1 
ATOM   1420  N N     . GLU D 4 8    ? 121.880 164.709 143.095 1.00 28.37  ? 5    GLU A N     1 
ATOM   1421  C CA    . GLU D 4 8    ? 122.658 164.942 144.303 1.00 28.37  ? 5    GLU A CA    1 
ATOM   1422  C C     . GLU D 4 8    ? 122.201 164.077 145.468 1.00 28.37  ? 5    GLU A C     1 
ATOM   1423  O O     . GLU D 4 8    ? 122.857 164.083 146.514 1.00 28.37  ? 5    GLU A O     1 
ATOM   1424  C CB    . GLU D 4 8    ? 122.586 166.419 144.689 1.00 28.37  ? 5    GLU A CB    1 
ATOM   1425  C CG    . GLU D 4 8    ? 123.577 167.297 143.946 1.00 28.37  ? 5    GLU A CG    1 
ATOM   1426  C CD    . GLU D 4 8    ? 122.977 167.943 142.714 1.00 28.37  ? 5    GLU A CD    1 
ATOM   1427  O OE1   . GLU D 4 8    ? 121.743 167.865 142.539 1.00 28.37  ? 5    GLU A OE1   1 
ATOM   1428  O OE2   . GLU D 4 8    ? 123.741 168.530 141.918 1.00 28.37  ? 5    GLU A OE2   1 
ATOM   1429  N N     . GLY D 4 9    ? 121.097 163.346 145.318 1.00 26.51  ? 6    GLY A N     1 
ATOM   1430  C CA    . GLY D 4 9    ? 120.618 162.470 146.370 1.00 26.51  ? 6    GLY A CA    1 
ATOM   1431  C C     . GLY D 4 9    ? 121.338 161.147 146.481 1.00 26.51  ? 6    GLY A C     1 
ATOM   1432  O O     . GLY D 4 9    ? 121.049 160.378 147.402 1.00 26.51  ? 6    GLY A O     1 
ATOM   1433  N N     . PHE D 4 10   ? 122.265 160.860 145.567 1.00 25.90  ? 7    PHE A N     1 
ATOM   1434  C CA    . PHE D 4 10   ? 123.045 159.625 145.608 1.00 25.90  ? 7    PHE A CA    1 
ATOM   1435  C C     . PHE D 4 10   ? 124.260 159.793 146.523 1.00 25.90  ? 7    PHE A C     1 
ATOM   1436  O O     . PHE D 4 10   ? 125.415 159.689 146.112 1.00 25.90  ? 7    PHE A O     1 
ATOM   1437  C CB    . PHE D 4 10   ? 123.466 159.219 144.203 1.00 25.90  ? 7    PHE A CB    1 
ATOM   1438  C CG    . PHE D 4 10   ? 122.352 158.654 143.378 1.00 25.90  ? 7    PHE A CG    1 
ATOM   1439  C CD1   . PHE D 4 10   ? 122.091 157.298 143.385 1.00 25.90  ? 7    PHE A CD1   1 
ATOM   1440  C CD2   . PHE D 4 10   ? 121.567 159.479 142.595 1.00 25.90  ? 7    PHE A CD2   1 
ATOM   1441  C CE1   . PHE D 4 10   ? 121.068 156.775 142.626 1.00 25.90  ? 7    PHE A CE1   1 
ATOM   1442  C CE2   . PHE D 4 10   ? 120.542 158.962 141.834 1.00 25.90  ? 7    PHE A CE2   1 
ATOM   1443  C CZ    . PHE D 4 10   ? 120.292 157.608 141.850 1.00 25.90  ? 7    PHE A CZ    1 
ATOM   1444  N N     . THR D 4 11   ? 123.973 160.060 147.794 1.00 26.01  ? 8    THR A N     1 
ATOM   1445  C CA    . THR D 4 11   ? 125.010 160.246 148.795 1.00 26.01  ? 8    THR A CA    1 
ATOM   1446  C C     . THR D 4 11   ? 124.551 159.637 150.110 1.00 26.01  ? 8    THR A C     1 
ATOM   1447  O O     . THR D 4 11   ? 123.354 159.478 150.360 1.00 26.01  ? 8    THR A O     1 
ATOM   1448  C CB    . THR D 4 11   ? 125.350 161.727 148.993 1.00 26.01  ? 8    THR A CB    1 
ATOM   1449  O OG1   . THR D 4 11   ? 126.352 161.854 150.009 1.00 26.01  ? 8    THR A OG1   1 
ATOM   1450  C CG2   . THR D 4 11   ? 124.113 162.503 149.411 1.00 26.01  ? 8    THR A CG2   1 
ATOM   1451  N N     . ASN D 4 12   ? 125.529 159.298 150.951 1.00 26.93  ? 9    ASN A N     1 
ATOM   1452  C CA    . ASN D 4 12   ? 125.270 158.738 152.277 1.00 26.93  ? 9    ASN A CA    1 
ATOM   1453  C C     . ASN D 4 12   ? 124.384 157.498 152.190 1.00 26.93  ? 9    ASN A C     1 
ATOM   1454  O O     . ASN D 4 12   ? 123.451 157.322 152.975 1.00 26.93  ? 9    ASN A O     1 
ATOM   1455  C CB    . ASN D 4 12   ? 124.652 159.788 153.202 1.00 26.93  ? 9    ASN A CB    1 
ATOM   1456  C CG    . ASN D 4 12   ? 125.054 159.601 154.648 1.00 26.93  ? 9    ASN A CG    1 
ATOM   1457  O OD1   . ASN D 4 12   ? 124.840 158.541 155.231 1.00 26.93  ? 9    ASN A OD1   1 
ATOM   1458  N ND2   . ASN D 4 12   ? 125.648 160.634 155.236 1.00 26.93  ? 9    ASN A ND2   1 
ATOM   1459  N N     . LEU D 4 13   ? 124.677 156.630 151.222 1.00 26.32  ? 10   LEU A N     1 
ATOM   1460  C CA    . LEU D 4 13   ? 123.860 155.445 150.996 1.00 26.32  ? 10   LEU A CA    1 
ATOM   1461  C C     . LEU D 4 13   ? 124.397 154.215 151.715 1.00 26.32  ? 10   LEU A C     1 
ATOM   1462  O O     . LEU D 4 13   ? 123.619 153.458 152.304 1.00 26.32  ? 10   LEU A O     1 
ATOM   1463  C CB    . LEU D 4 13   ? 123.745 155.164 149.496 1.00 26.32  ? 10   LEU A CB    1 
ATOM   1464  C CG    . LEU D 4 13   ? 122.826 156.120 148.734 1.00 26.32  ? 10   LEU A CG    1 
ATOM   1465  C CD1   . LEU D 4 13   ? 122.689 155.698 147.286 1.00 26.32  ? 10   LEU A CD1   1 
ATOM   1466  C CD2   . LEU D 4 13   ? 121.464 156.194 149.401 1.00 26.32  ? 10   LEU A CD2   1 
ATOM   1467  N N     . TYR D 4 14   ? 125.709 153.991 151.682 1.00 29.04  ? 11   TYR A N     1 
ATOM   1468  C CA    . TYR D 4 14   ? 126.298 152.873 152.404 1.00 29.04  ? 11   TYR A CA    1 
ATOM   1469  C C     . TYR D 4 14   ? 127.697 153.251 152.866 1.00 29.04  ? 11   TYR A C     1 
ATOM   1470  O O     . TYR D 4 14   ? 128.369 154.079 152.248 1.00 29.04  ? 11   TYR A O     1 
ATOM   1471  C CB    . TYR D 4 14   ? 126.336 151.601 151.549 1.00 29.04  ? 11   TYR A CB    1 
ATOM   1472  C CG    . TYR D 4 14   ? 127.088 151.735 150.244 1.00 29.04  ? 11   TYR A CG    1 
ATOM   1473  C CD1   . TYR D 4 14   ? 128.448 151.481 150.175 1.00 29.04  ? 11   TYR A CD1   1 
ATOM   1474  C CD2   . TYR D 4 14   ? 126.432 152.101 149.080 1.00 29.04  ? 11   TYR A CD2   1 
ATOM   1475  C CE1   . TYR D 4 14   ? 129.135 151.597 148.986 1.00 29.04  ? 11   TYR A CE1   1 
ATOM   1476  C CE2   . TYR D 4 14   ? 127.110 152.218 147.886 1.00 29.04  ? 11   TYR A CE2   1 
ATOM   1477  C CZ    . TYR D 4 14   ? 128.461 151.965 147.845 1.00 29.04  ? 11   TYR A CZ    1 
ATOM   1478  O OH    . TYR D 4 14   ? 129.143 152.081 146.657 1.00 29.04  ? 11   TYR A OH    1 
ATOM   1479  N N     . GLN D 4 15   ? 128.124 152.634 153.964 1.00 25.81  ? 12   GLN A N     1 
ATOM   1480  C CA    . GLN D 4 15   ? 129.437 152.914 154.524 1.00 25.81  ? 12   GLN A CA    1 
ATOM   1481  C C     . GLN D 4 15   ? 130.539 152.348 153.638 1.00 25.81  ? 12   GLN A C     1 
ATOM   1482  O O     . GLN D 4 15   ? 130.398 151.283 153.032 1.00 25.81  ? 12   GLN A O     1 
ATOM   1483  C CB    . GLN D 4 15   ? 129.560 152.327 155.929 1.00 25.81  ? 12   GLN A CB    1 
ATOM   1484  C CG    . GLN D 4 15   ? 128.557 152.865 156.928 1.00 25.81  ? 12   GLN A CG    1 
ATOM   1485  C CD    . GLN D 4 15   ? 128.666 152.188 158.276 1.00 25.81  ? 12   GLN A CD    1 
ATOM   1486  O OE1   . GLN D 4 15   ? 129.414 151.226 158.440 1.00 25.81  ? 12   GLN A OE1   1 
ATOM   1487  N NE2   . GLN D 4 15   ? 127.918 152.688 159.251 1.00 25.81  ? 12   GLN A NE2   1 
ATOM   1488  N N     . VAL D 4 16   ? 131.650 153.074 153.573 1.00 24.67  ? 13   VAL A N     1 
ATOM   1489  C CA    . VAL D 4 16   ? 132.837 152.637 152.851 1.00 24.67  ? 13   VAL A CA    1 
ATOM   1490  C C     . VAL D 4 16   ? 134.055 152.901 153.727 1.00 24.67  ? 13   VAL A C     1 
ATOM   1491  O O     . VAL D 4 16   ? 134.168 153.960 154.354 1.00 24.67  ? 13   VAL A O     1 
ATOM   1492  C CB    . VAL D 4 16   ? 132.954 153.330 151.476 1.00 24.67  ? 13   VAL A CB    1 
ATOM   1493  C CG1   . VAL D 4 16   ? 133.157 154.821 151.636 1.00 24.67  ? 13   VAL A CG1   1 
ATOM   1494  C CG2   . VAL D 4 16   ? 134.085 152.718 150.670 1.00 24.67  ? 13   VAL A CG2   1 
ATOM   1495  N N     . SER D 4 17   ? 134.951 151.922 153.797 1.00 28.72  ? 14   SER A N     1 
ATOM   1496  C CA    . SER D 4 17   ? 136.123 151.986 154.658 1.00 28.72  ? 14   SER A CA    1 
ATOM   1497  C C     . SER D 4 17   ? 137.377 152.126 153.810 1.00 28.72  ? 14   SER A C     1 
ATOM   1498  O O     . SER D 4 17   ? 137.573 151.368 152.855 1.00 28.72  ? 14   SER A O     1 
ATOM   1499  C CB    . SER D 4 17   ? 136.218 150.741 155.541 1.00 28.72  ? 14   SER A CB    1 
ATOM   1500  O OG    . SER D 4 17   ? 134.989 150.486 156.196 1.00 28.72  ? 14   SER A OG    1 
ATOM   1501  N N     . LYS D 4 18   ? 138.222 153.091 154.162 1.00 28.36  ? 15   LYS A N     1 
ATOM   1502  C CA    . LYS D 4 18   ? 139.484 153.318 153.477 1.00 28.36  ? 15   LYS A CA    1 
ATOM   1503  C C     . LYS D 4 18   ? 140.605 153.400 154.500 1.00 28.36  ? 15   LYS A C     1 
ATOM   1504  O O     . LYS D 4 18   ? 140.408 153.870 155.623 1.00 28.36  ? 15   LYS A O     1 
ATOM   1505  C CB    . LYS D 4 18   ? 139.448 154.599 152.635 1.00 28.36  ? 15   LYS A CB    1 
ATOM   1506  C CG    . LYS D 4 18   ? 138.351 154.619 151.587 1.00 28.36  ? 15   LYS A CG    1 
ATOM   1507  C CD    . LYS D 4 18   ? 138.578 155.721 150.571 1.00 28.36  ? 15   LYS A CD    1 
ATOM   1508  C CE    . LYS D 4 18   ? 137.457 155.764 149.550 1.00 28.36  ? 15   LYS A CE    1 
ATOM   1509  N NZ    . LYS D 4 18   ? 137.350 154.488 148.791 1.00 28.36  ? 15   LYS A NZ    1 
ATOM   1510  N N     . THR D 4 19   ? 141.786 152.936 154.103 1.00 31.47  ? 16   THR A N     1 
ATOM   1511  C CA    . THR D 4 19   ? 142.960 152.915 154.968 1.00 31.47  ? 16   THR A CA    1 
ATOM   1512  C C     . THR D 4 19   ? 143.945 153.965 154.472 1.00 31.47  ? 16   THR A C     1 
ATOM   1513  O O     . THR D 4 19   ? 144.582 153.784 153.429 1.00 31.47  ? 16   THR A O     1 
ATOM   1514  C CB    . THR D 4 19   ? 143.603 151.531 154.985 1.00 31.47  ? 16   THR A CB    1 
ATOM   1515  O OG1   . THR D 4 19   ? 142.693 150.587 155.561 1.00 31.47  ? 16   THR A OG1   1 
ATOM   1516  C CG2   . THR D 4 19   ? 144.882 151.553 155.802 1.00 31.47  ? 16   THR A CG2   1 
ATOM   1517  N N     . LEU D 4 20   ? 144.067 155.058 155.216 1.00 30.95  ? 17   LEU A N     1 
ATOM   1518  C CA    . LEU D 4 20   ? 145.029 156.094 154.880 1.00 30.95  ? 17   LEU A CA    1 
ATOM   1519  C C     . LEU D 4 20   ? 146.414 155.717 155.390 1.00 30.95  ? 17   LEU A C     1 
ATOM   1520  O O     . LEU D 4 20   ? 146.561 155.039 156.410 1.00 30.95  ? 17   LEU A O     1 
ATOM   1521  C CB    . LEU D 4 20   ? 144.606 157.439 155.469 1.00 30.95  ? 17   LEU A CB    1 
ATOM   1522  C CG    . LEU D 4 20   ? 143.113 157.764 155.456 1.00 30.95  ? 17   LEU A CG    1 
ATOM   1523  C CD1   . LEU D 4 20   ? 142.859 159.099 156.129 1.00 30.95  ? 17   LEU A CD1   1 
ATOM   1524  C CD2   . LEU D 4 20   ? 142.570 157.770 154.040 1.00 30.95  ? 17   LEU A CD2   1 
ATOM   1525  N N     . ARG D 4 21   ? 147.435 156.164 154.666 1.00 39.60  ? 18   ARG A N     1 
ATOM   1526  C CA    . ARG D 4 21   ? 148.819 155.927 155.040 1.00 39.60  ? 18   ARG A CA    1 
ATOM   1527  C C     . ARG D 4 21   ? 149.537 157.257 155.198 1.00 39.60  ? 18   ARG A C     1 
ATOM   1528  O O     . ARG D 4 21   ? 149.244 158.226 154.494 1.00 39.60  ? 18   ARG A O     1 
ATOM   1529  C CB    . ARG D 4 21   ? 149.551 155.071 154.003 1.00 39.60  ? 18   ARG A CB    1 
ATOM   1530  C CG    . ARG D 4 21   ? 149.072 153.639 153.914 1.00 39.60  ? 18   ARG A CG    1 
ATOM   1531  C CD    . ARG D 4 21   ? 149.777 152.911 152.788 1.00 39.60  ? 18   ARG A CD    1 
ATOM   1532  N NE    . ARG D 4 21   ? 149.380 153.423 151.483 1.00 39.60  ? 18   ARG A NE    1 
ATOM   1533  C CZ    . ARG D 4 21   ? 149.789 152.921 150.326 1.00 39.60  ? 18   ARG A CZ    1 
ATOM   1534  N NH1   . ARG D 4 21   ? 150.619 151.893 150.274 1.00 39.60  ? 18   ARG A NH1   1 
ATOM   1535  N NH2   . ARG D 4 21   ? 149.356 153.466 149.194 1.00 39.60  ? 18   ARG A NH2   1 
ATOM   1536  N N     . PHE D 4 22   ? 150.481 157.294 156.134 1.00 50.27  ? 19   PHE A N     1 
ATOM   1537  C CA    . PHE D 4 22   ? 151.276 158.486 156.378 1.00 50.27  ? 19   PHE A CA    1 
ATOM   1538  C C     . PHE D 4 22   ? 152.676 158.067 156.794 1.00 50.27  ? 19   PHE A C     1 
ATOM   1539  O O     . PHE D 4 22   ? 152.903 156.937 157.232 1.00 50.27  ? 19   PHE A O     1 
ATOM   1540  C CB    . PHE D 4 22   ? 150.657 159.380 157.459 1.00 50.27  ? 19   PHE A CB    1 
ATOM   1541  C CG    . PHE D 4 22   ? 149.257 159.822 157.159 1.00 50.27  ? 19   PHE A CG    1 
ATOM   1542  C CD1   . PHE D 4 22   ? 149.017 160.839 156.254 1.00 50.27  ? 19   PHE A CD1   1 
ATOM   1543  C CD2   . PHE D 4 22   ? 148.181 159.230 157.792 1.00 50.27  ? 19   PHE A CD2   1 
ATOM   1544  C CE1   . PHE D 4 22   ? 147.732 161.250 155.980 1.00 50.27  ? 19   PHE A CE1   1 
ATOM   1545  C CE2   . PHE D 4 22   ? 146.893 159.637 157.522 1.00 50.27  ? 19   PHE A CE2   1 
ATOM   1546  C CZ    . PHE D 4 22   ? 146.668 160.649 156.614 1.00 50.27  ? 19   PHE A CZ    1 
ATOM   1547  N N     . GLU D 4 23   ? 153.614 158.994 156.648 1.00 50.27  ? 20   GLU A N     1 
ATOM   1548  C CA    . GLU D 4 23   ? 154.985 158.794 157.091 1.00 50.27  ? 20   GLU A CA    1 
ATOM   1549  C C     . GLU D 4 23   ? 155.187 159.506 158.418 1.00 50.27  ? 20   GLU A C     1 
ATOM   1550  O O     . GLU D 4 23   ? 154.901 160.702 158.535 1.00 50.27  ? 20   GLU A O     1 
ATOM   1551  C CB    . GLU D 4 23   ? 155.981 159.317 156.057 1.00 50.27  ? 20   GLU A CB    1 
ATOM   1552  C CG    . GLU D 4 23   ? 157.427 159.244 156.509 1.00 50.27  ? 20   GLU A CG    1 
ATOM   1553  C CD    . GLU D 4 23   ? 158.297 160.294 155.853 1.00 50.27  ? 20   GLU A CD    1 
ATOM   1554  O OE1   . GLU D 4 23   ? 157.917 160.793 154.774 1.00 50.27  ? 20   GLU A OE1   1 
ATOM   1555  O OE2   . GLU D 4 23   ? 159.361 160.621 156.415 1.00 50.27  ? 20   GLU A OE2   1 
ATOM   1556  N N     . LEU D 4 24   ? 155.675 158.773 159.412 1.00 37.65  ? 21   LEU A N     1 
ATOM   1557  C CA    . LEU D 4 24   ? 155.902 159.324 160.740 1.00 37.65  ? 21   LEU A CA    1 
ATOM   1558  C C     . LEU D 4 24   ? 157.301 159.921 160.804 1.00 37.65  ? 21   LEU A C     1 
ATOM   1559  O O     . LEU D 4 24   ? 158.288 159.234 160.522 1.00 37.65  ? 21   LEU A O     1 
ATOM   1560  C CB    . LEU D 4 24   ? 155.731 158.246 161.807 1.00 37.65  ? 21   LEU A CB    1 
ATOM   1561  C CG    . LEU D 4 24   ? 154.358 157.583 161.867 1.00 37.65  ? 21   LEU A CG    1 
ATOM   1562  C CD1   . LEU D 4 24   ? 154.323 156.546 162.971 1.00 37.65  ? 21   LEU A CD1   1 
ATOM   1563  C CD2   . LEU D 4 24   ? 153.283 158.630 162.079 1.00 37.65  ? 21   LEU A CD2   1 
ATOM   1564  N N     . ILE D 4 25   ? 157.384 161.195 161.172 1.00 37.62  ? 22   ILE A N     1 
ATOM   1565  C CA    . ILE D 4 25   ? 158.658 161.881 161.358 1.00 37.62  ? 22   ILE A CA    1 
ATOM   1566  C C     . ILE D 4 25   ? 158.894 162.010 162.860 1.00 37.62  ? 22   ILE A C     1 
ATOM   1567  O O     . ILE D 4 25   ? 158.143 162.736 163.532 1.00 37.62  ? 22   ILE A O     1 
ATOM   1568  C CB    . ILE D 4 25   ? 158.669 163.251 160.672 1.00 37.62  ? 22   ILE A CB    1 
ATOM   1569  C CG1   . ILE D 4 25   ? 158.329 163.103 159.190 1.00 37.62  ? 22   ILE A CG1   1 
ATOM   1570  C CG2   . ILE D 4 25   ? 160.021 163.917 160.846 1.00 37.62  ? 22   ILE A CG2   1 
ATOM   1571  C CD1   . ILE D 4 25   ? 158.550 164.361 158.384 1.00 37.62  ? 22   ILE A CD1   1 
ATOM   1572  N N     . PRO D 4 26   ? 159.890 161.330 163.425 1.00 50.27  ? 23   PRO A N     1 
ATOM   1573  C CA    . PRO D 4 26   ? 160.128 161.430 164.869 1.00 50.27  ? 23   PRO A CA    1 
ATOM   1574  C C     . PRO D 4 26   ? 160.409 162.865 165.287 1.00 50.27  ? 23   PRO A C     1 
ATOM   1575  O O     . PRO D 4 26   ? 161.090 163.615 164.585 1.00 50.27  ? 23   PRO A O     1 
ATOM   1576  C CB    . PRO D 4 26   ? 161.345 160.524 165.093 1.00 50.27  ? 23   PRO A CB    1 
ATOM   1577  C CG    . PRO D 4 26   ? 161.947 160.323 163.743 1.00 50.27  ? 23   PRO A CG    1 
ATOM   1578  C CD    . PRO D 4 26   ? 160.822 160.399 162.771 1.00 50.27  ? 23   PRO A CD    1 
ATOM   1579  N N     . GLN D 4 27   ? 159.874 163.243 166.444 1.00 37.78  ? 24   GLN A N     1 
ATOM   1580  C CA    . GLN D 4 27   ? 159.955 164.607 166.946 1.00 37.78  ? 24   GLN A CA    1 
ATOM   1581  C C     . GLN D 4 27   ? 160.747 164.628 168.244 1.00 37.78  ? 24   GLN A C     1 
ATOM   1582  O O     . GLN D 4 27   ? 160.492 163.823 169.144 1.00 37.78  ? 24   GLN A O     1 
ATOM   1583  C CB    . GLN D 4 27   ? 158.559 165.192 167.172 1.00 37.78  ? 24   GLN A CB    1 
ATOM   1584  C CG    . GLN D 4 27   ? 157.767 165.407 165.897 1.00 37.78  ? 24   GLN A CG    1 
ATOM   1585  C CD    . GLN D 4 27   ? 158.328 166.527 165.047 1.00 37.78  ? 24   GLN A CD    1 
ATOM   1586  O OE1   . GLN D 4 27   ? 158.415 167.672 165.488 1.00 37.78  ? 24   GLN A OE1   1 
ATOM   1587  N NE2   . GLN D 4 27   ? 158.713 166.202 163.819 1.00 37.78  ? 24   GLN A NE2   1 
ATOM   1588  N N     . GLY D 4 28   ? 161.698 165.554 168.340 1.00 37.41  ? 25   GLY A N     1 
ATOM   1589  C CA    . GLY D 4 28   ? 162.508 165.634 169.538 1.00 37.41  ? 25   GLY A CA    1 
ATOM   1590  C C     . GLY D 4 28   ? 163.475 164.468 169.643 1.00 37.41  ? 25   GLY A C     1 
ATOM   1591  O O     . GLY D 4 28   ? 163.995 163.957 168.646 1.00 37.41  ? 25   GLY A O     1 
ATOM   1592  N N     . LYS D 4 29   ? 163.719 164.038 170.880 1.00 50.26  ? 26   LYS A N     1 
ATOM   1593  C CA    . LYS D 4 29   ? 164.640 162.946 171.158 1.00 50.26  ? 26   LYS A CA    1 
ATOM   1594  C C     . LYS D 4 29   ? 163.955 161.586 171.186 1.00 50.26  ? 26   LYS A C     1 
ATOM   1595  O O     . LYS D 4 29   ? 164.465 160.663 171.830 1.00 50.26  ? 26   LYS A O     1 
ATOM   1596  C CB    . LYS D 4 29   ? 165.364 163.187 172.484 1.00 36.41  ? 26   LYS A CB    1 
ATOM   1597  C CG    . LYS D 4 29   ? 166.381 164.310 172.440 1.00 36.41  ? 26   LYS A CG    1 
ATOM   1598  C CD    . LYS D 4 29   ? 167.176 164.373 173.731 1.00 36.41  ? 26   LYS A CD    1 
ATOM   1599  C CE    . LYS D 4 29   ? 168.190 165.503 173.703 1.00 36.41  ? 26   LYS A CE    1 
ATOM   1600  N NZ    . LYS D 4 29   ? 168.994 165.553 174.956 1.00 36.41  ? 26   LYS A NZ    1 
ATOM   1601  N N     . THR D 4 30   ? 162.813 161.439 170.511 1.00 50.26  ? 27   THR A N     1 
ATOM   1602  C CA    . THR D 4 30   ? 162.127 160.152 170.521 1.00 50.26  ? 27   THR A CA    1 
ATOM   1603  C C     . THR D 4 30   ? 162.893 159.089 169.741 1.00 50.26  ? 27   THR A C     1 
ATOM   1604  O O     . THR D 4 30   ? 162.886 157.917 170.134 1.00 50.26  ? 27   THR A O     1 
ATOM   1605  C CB    . THR D 4 30   ? 160.704 160.302 169.979 1.00 50.26  ? 27   THR A CB    1 
ATOM   1606  O OG1   . THR D 4 30   ? 160.018 159.050 170.093 1.00 50.26  ? 27   THR A OG1   1 
ATOM   1607  C CG2   . THR D 4 30   ? 160.708 160.739 168.533 1.00 50.26  ? 27   THR A CG2   1 
ATOM   1608  N N     . LEU D 4 31   ? 163.564 159.469 168.651 1.00 50.26  ? 28   LEU A N     1 
ATOM   1609  C CA    . LEU D 4 31   ? 164.339 158.493 167.893 1.00 50.26  ? 28   LEU A CA    1 
ATOM   1610  C C     . LEU D 4 31   ? 165.506 157.964 168.714 1.00 50.26  ? 28   LEU A C     1 
ATOM   1611  O O     . LEU D 4 31   ? 165.820 156.768 168.662 1.00 50.26  ? 28   LEU A O     1 
ATOM   1612  C CB    . LEU D 4 31   ? 164.838 159.110 166.588 1.00 50.26  ? 28   LEU A CB    1 
ATOM   1613  C CG    . LEU D 4 31   ? 165.621 158.164 165.676 1.00 50.26  ? 28   LEU A CG    1 
ATOM   1614  C CD1   . LEU D 4 31   ? 164.838 156.886 165.430 1.00 50.26  ? 28   LEU A CD1   1 
ATOM   1615  C CD2   . LEU D 4 31   ? 165.962 158.847 164.362 1.00 50.26  ? 28   LEU A CD2   1 
ATOM   1616  N N     . LYS D 4 32   ? 166.158 158.841 169.480 1.00 50.26  ? 29   LYS A N     1 
ATOM   1617  C CA    . LYS D 4 32   ? 167.243 158.398 170.346 1.00 50.26  ? 29   LYS A CA    1 
ATOM   1618  C C     . LYS D 4 32   ? 166.743 157.401 171.382 1.00 50.26  ? 29   LYS A C     1 
ATOM   1619  O O     . LYS D 4 32   ? 167.398 156.387 171.641 1.00 50.26  ? 29   LYS A O     1 
ATOM   1620  C CB    . LYS D 4 32   ? 167.893 159.602 171.025 1.00 50.26  ? 29   LYS A CB    1 
ATOM   1621  C CG    . LYS D 4 32   ? 168.862 159.245 172.137 1.00 50.26  ? 29   LYS A CG    1 
ATOM   1622  C CD    . LYS D 4 32   ? 169.506 160.490 172.725 1.00 50.26  ? 29   LYS A CD    1 
ATOM   1623  C CE    . LYS D 4 32   ? 170.338 160.157 173.951 1.00 50.26  ? 29   LYS A CE    1 
ATOM   1624  N NZ    . LYS D 4 32   ? 169.485 159.862 175.134 1.00 50.26  ? 29   LYS A NZ    1 
ATOM   1625  N N     . HIS D 4 33   ? 165.578 157.666 171.976 1.00 50.26  ? 30   HIS A N     1 
ATOM   1626  C CA    . HIS D 4 33   ? 165.027 156.742 172.962 1.00 50.26  ? 30   HIS A CA    1 
ATOM   1627  C C     . HIS D 4 33   ? 164.644 155.410 172.329 1.00 50.26  ? 30   HIS A C     1 
ATOM   1628  O O     . HIS D 4 33   ? 164.868 154.350 172.925 1.00 50.26  ? 30   HIS A O     1 
ATOM   1629  C CB    . HIS D 4 33   ? 163.824 157.372 173.660 1.00 50.26  ? 30   HIS A CB    1 
ATOM   1630  C CG    . HIS D 4 33   ? 164.186 158.470 174.611 1.00 50.26  ? 30   HIS A CG    1 
ATOM   1631  N ND1   . HIS D 4 33   ? 165.061 158.285 175.660 1.00 50.26  ? 30   HIS A ND1   1 
ATOM   1632  C CD2   . HIS D 4 33   ? 163.791 159.763 174.673 1.00 50.26  ? 30   HIS A CD2   1 
ATOM   1633  C CE1   . HIS D 4 33   ? 165.191 159.419 176.325 1.00 50.26  ? 30   HIS A CE1   1 
ATOM   1634  N NE2   . HIS D 4 33   ? 164.431 160.331 175.747 1.00 50.26  ? 30   HIS A NE2   1 
ATOM   1635  N N     . ILE D 4 34   ? 164.062 155.439 171.127 1.00 50.26  ? 31   ILE A N     1 
ATOM   1636  C CA    . ILE D 4 34   ? 163.703 154.192 170.454 1.00 50.26  ? 31   ILE A CA    1 
ATOM   1637  C C     . ILE D 4 34   ? 164.948 153.372 170.147 1.00 50.26  ? 31   ILE A C     1 
ATOM   1638  O O     . ILE D 4 34   ? 164.972 152.153 170.357 1.00 50.26  ? 31   ILE A O     1 
ATOM   1639  C CB    . ILE D 4 34   ? 162.883 154.473 169.182 1.00 50.26  ? 31   ILE A CB    1 
ATOM   1640  C CG1   . ILE D 4 34   ? 161.558 155.145 169.538 1.00 50.26  ? 31   ILE A CG1   1 
ATOM   1641  C CG2   . ILE D 4 34   ? 162.638 153.191 168.410 1.00 50.26  ? 31   ILE A CG2   1 
ATOM   1642  C CD1   . ILE D 4 34   ? 160.815 155.683 168.343 1.00 50.26  ? 31   ILE A CD1   1 
ATOM   1643  N N     . GLN D 4 35   ? 166.000 154.020 169.645 1.00 50.26  ? 32   GLN A N     1 
ATOM   1644  C CA    . GLN D 4 35   ? 167.237 153.298 169.366 1.00 50.26  ? 32   GLN A CA    1 
ATOM   1645  C C     . GLN D 4 35   ? 167.865 152.760 170.646 1.00 50.26  ? 32   GLN A C     1 
ATOM   1646  O O     . GLN D 4 35   ? 168.401 151.645 170.659 1.00 50.26  ? 32   GLN A O     1 
ATOM   1647  C CB    . GLN D 4 35   ? 168.217 154.202 168.621 1.00 50.26  ? 32   GLN A CB    1 
ATOM   1648  C CG    . GLN D 4 35   ? 167.835 154.455 167.175 1.00 50.26  ? 32   GLN A CG    1 
ATOM   1649  C CD    . GLN D 4 35   ? 168.813 155.367 166.467 1.00 50.26  ? 32   GLN A CD    1 
ATOM   1650  O OE1   . GLN D 4 35   ? 169.506 156.163 167.099 1.00 50.26  ? 32   GLN A OE1   1 
ATOM   1651  N NE2   . GLN D 4 35   ? 168.875 155.255 165.146 1.00 50.26  ? 32   GLN A NE2   1 
ATOM   1652  N N     . GLU D 4 36   ? 167.816 153.538 171.730 1.00 50.26  ? 33   GLU A N     1 
ATOM   1653  C CA    . GLU D 4 36   ? 168.374 153.085 172.999 1.00 50.26  ? 33   GLU A CA    1 
ATOM   1654  C C     . GLU D 4 36   ? 167.633 151.863 173.526 1.00 50.26  ? 33   GLU A C     1 
ATOM   1655  O O     . GLU D 4 36   ? 168.256 150.907 174.000 1.00 50.26  ? 33   GLU A O     1 
ATOM   1656  C CB    . GLU D 4 36   ? 168.331 154.224 174.017 1.00 50.26  ? 33   GLU A CB    1 
ATOM   1657  C CG    . GLU D 4 36   ? 168.562 153.796 175.454 1.00 50.26  ? 33   GLU A CG    1 
ATOM   1658  C CD    . GLU D 4 36   ? 168.412 154.946 176.429 1.00 50.26  ? 33   GLU A CD    1 
ATOM   1659  O OE1   . GLU D 4 36   ? 169.134 155.953 176.276 1.00 50.26  ? 33   GLU A OE1   1 
ATOM   1660  O OE2   . GLU D 4 36   ? 167.570 154.844 177.346 1.00 50.26  ? 33   GLU A OE2   1 
ATOM   1661  N N     . GLN D 4 37   ? 166.303 151.874 173.448 1.00 50.26  ? 34   GLN A N     1 
ATOM   1662  C CA    . GLN D 4 37   ? 165.516 150.727 173.880 1.00 50.26  ? 34   GLN A CA    1 
ATOM   1663  C C     . GLN D 4 37   ? 165.530 149.588 172.870 1.00 50.26  ? 34   GLN A C     1 
ATOM   1664  O O     . GLN D 4 37   ? 165.110 148.476 173.210 1.00 50.26  ? 34   GLN A O     1 
ATOM   1665  C CB    . GLN D 4 37   ? 164.075 151.154 174.157 1.00 50.26  ? 34   GLN A CB    1 
ATOM   1666  C CG    . GLN D 4 37   ? 163.889 151.883 175.475 1.00 50.26  ? 34   GLN A CG    1 
ATOM   1667  C CD    . GLN D 4 37   ? 164.145 150.990 176.670 1.00 50.26  ? 34   GLN A CD    1 
ATOM   1668  O OE1   . GLN D 4 37   ? 163.818 149.803 176.654 1.00 50.26  ? 34   GLN A OE1   1 
ATOM   1669  N NE2   . GLN D 4 37   ? 164.735 151.556 177.717 1.00 50.26  ? 34   GLN A NE2   1 
ATOM   1670  N N     . GLY D 4 38   ? 165.996 149.835 171.652 1.00 50.26  ? 35   GLY A N     1 
ATOM   1671  C CA    . GLY D 4 38   ? 166.106 148.791 170.649 1.00 50.26  ? 35   GLY A CA    1 
ATOM   1672  C C     . GLY D 4 38   ? 164.790 148.219 170.171 1.00 50.26  ? 35   GLY A C     1 
ATOM   1673  O O     . GLY D 4 38   ? 164.702 147.012 169.919 1.00 50.26  ? 35   GLY A O     1 
ATOM   1674  N N     . PHE D 4 39   ? 163.759 149.056 170.037 1.00 50.26  ? 36   PHE A N     1 
ATOM   1675  C CA    . PHE D 4 39   ? 162.479 148.560 169.541 1.00 50.26  ? 36   PHE A CA    1 
ATOM   1676  C C     . PHE D 4 39   ? 162.571 148.154 168.076 1.00 50.26  ? 36   PHE A C     1 
ATOM   1677  O O     . PHE D 4 39   ? 161.941 147.177 167.657 1.00 50.26  ? 36   PHE A O     1 
ATOM   1678  C CB    . PHE D 4 39   ? 161.391 149.614 169.736 1.00 50.26  ? 36   PHE A CB    1 
ATOM   1679  C CG    . PHE D 4 39   ? 161.018 149.846 171.170 1.00 50.26  ? 36   PHE A CG    1 
ATOM   1680  C CD1   . PHE D 4 39   ? 160.509 148.819 171.942 1.00 50.26  ? 36   PHE A CD1   1 
ATOM   1681  C CD2   . PHE D 4 39   ? 161.166 151.096 171.743 1.00 50.26  ? 36   PHE A CD2   1 
ATOM   1682  C CE1   . PHE D 4 39   ? 160.161 149.034 173.260 1.00 50.26  ? 36   PHE A CE1   1 
ATOM   1683  C CE2   . PHE D 4 39   ? 160.817 151.315 173.059 1.00 50.26  ? 36   PHE A CE2   1 
ATOM   1684  C CZ    . PHE D 4 39   ? 160.317 150.282 173.819 1.00 50.26  ? 36   PHE A CZ    1 
ATOM   1685  N N     . ILE D 4 40   ? 163.342 148.897 167.280 1.00 50.26  ? 37   ILE A N     1 
ATOM   1686  C CA    . ILE D 4 40   ? 163.442 148.600 165.854 1.00 50.26  ? 37   ILE A CA    1 
ATOM   1687  C C     . ILE D 4 40   ? 164.173 147.283 165.630 1.00 50.26  ? 37   ILE A C     1 
ATOM   1688  O O     . ILE D 4 40   ? 163.737 146.439 164.838 1.00 50.26  ? 37   ILE A O     1 
ATOM   1689  C CB    . ILE D 4 40   ? 164.132 149.758 165.112 1.00 50.26  ? 37   ILE A CB    1 
ATOM   1690  C CG1   . ILE D 4 40   ? 163.412 151.075 165.397 1.00 50.26  ? 37   ILE A CG1   1 
ATOM   1691  C CG2   . ILE D 4 40   ? 164.169 149.484 163.623 1.00 50.26  ? 37   ILE A CG2   1 
ATOM   1692  C CD1   . ILE D 4 40   ? 161.950 151.058 165.020 1.00 50.26  ? 37   ILE A CD1   1 
ATOM   1693  N N     . GLU D 4 41   ? 165.300 147.089 166.318 1.00 50.26  ? 38   GLU A N     1 
ATOM   1694  C CA    . GLU D 4 41   ? 166.069 145.864 166.137 1.00 50.26  ? 38   GLU A CA    1 
ATOM   1695  C C     . GLU D 4 41   ? 165.299 144.645 166.633 1.00 50.26  ? 38   GLU A C     1 
ATOM   1696  O O     . GLU D 4 41   ? 165.361 143.574 166.018 1.00 50.26  ? 38   GLU A O     1 
ATOM   1697  C CB    . GLU D 4 41   ? 167.425 145.986 166.836 1.00 50.26  ? 38   GLU A CB    1 
ATOM   1698  C CG    . GLU D 4 41   ? 167.359 146.136 168.345 1.00 50.26  ? 38   GLU A CG    1 
ATOM   1699  C CD    . GLU D 4 41   ? 168.726 146.328 168.971 1.00 50.26  ? 38   GLU A CD    1 
ATOM   1700  O OE1   . GLU D 4 41   ? 169.723 146.367 168.221 1.00 50.26  ? 38   GLU A OE1   1 
ATOM   1701  O OE2   . GLU D 4 41   ? 168.804 146.437 170.213 1.00 50.26  ? 38   GLU A OE2   1 
ATOM   1702  N N     . GLU D 4 42   ? 164.553 144.789 167.731 1.00 50.26  ? 39   GLU A N     1 
ATOM   1703  C CA    . GLU D 4 42   ? 163.756 143.670 168.222 1.00 50.26  ? 39   GLU A CA    1 
ATOM   1704  C C     . GLU D 4 42   ? 162.635 143.321 167.252 1.00 50.26  ? 39   GLU A C     1 
ATOM   1705  O O     . GLU D 4 42   ? 162.312 142.145 167.069 1.00 50.26  ? 39   GLU A O     1 
ATOM   1706  C CB    . GLU D 4 42   ? 163.195 143.982 169.610 1.00 50.26  ? 39   GLU A CB    1 
ATOM   1707  C CG    . GLU D 4 42   ? 164.234 144.034 170.740 1.00 50.26  ? 39   GLU A CG    1 
ATOM   1708  C CD    . GLU D 4 42   ? 165.030 142.744 170.932 1.00 50.26  ? 39   GLU A CD    1 
ATOM   1709  O OE1   . GLU D 4 42   ? 164.741 141.725 170.269 1.00 50.26  ? 39   GLU A OE1   1 
ATOM   1710  O OE2   . GLU D 4 42   ? 165.936 142.743 171.792 1.00 50.26  ? 39   GLU A OE2   1 
ATOM   1711  N N     . ASP D 4 43   ? 162.039 144.324 166.606 1.00 50.26  ? 40   ASP A N     1 
ATOM   1712  C CA    . ASP D 4 43   ? 160.998 144.038 165.623 1.00 50.26  ? 40   ASP A CA    1 
ATOM   1713  C C     . ASP D 4 43   ? 161.572 143.429 164.349 1.00 50.26  ? 40   ASP A C     1 
ATOM   1714  O O     . ASP D 4 43   ? 160.929 142.576 163.727 1.00 50.26  ? 40   ASP A O     1 
ATOM   1715  C CB    . ASP D 4 43   ? 160.209 145.308 165.316 1.00 50.26  ? 40   ASP A CB    1 
ATOM   1716  C CG    . ASP D 4 43   ? 159.364 145.762 166.491 1.00 50.26  ? 40   ASP A CG    1 
ATOM   1717  O OD1   . ASP D 4 43   ? 158.941 144.897 167.285 1.00 50.26  ? 40   ASP A OD1   1 
ATOM   1718  O OD2   . ASP D 4 43   ? 159.134 146.980 166.631 1.00 50.26  ? 40   ASP A OD2   1 
ATOM   1719  N N     . LYS D 4 44   ? 162.775 143.845 163.944 1.00 50.26  ? 41   LYS A N     1 
ATOM   1720  C CA    . LYS D 4 44   ? 163.440 143.179 162.827 1.00 50.26  ? 41   LYS A CA    1 
ATOM   1721  C C     . LYS D 4 44   ? 163.738 141.724 163.164 1.00 50.26  ? 41   LYS A C     1 
ATOM   1722  O O     . LYS D 4 44   ? 163.565 140.830 162.324 1.00 50.26  ? 41   LYS A O     1 
ATOM   1723  C CB    . LYS D 4 44   ? 164.724 143.922 162.461 1.00 50.26  ? 41   LYS A CB    1 
ATOM   1724  C CG    . LYS D 4 44   ? 165.306 143.523 161.118 1.00 50.26  ? 41   LYS A CG    1 
ATOM   1725  C CD    . LYS D 4 44   ? 166.746 143.990 160.980 1.00 50.26  ? 41   LYS A CD    1 
ATOM   1726  C CE    . LYS D 4 44   ? 167.711 143.024 161.648 1.00 50.26  ? 41   LYS A CE    1 
ATOM   1727  N NZ    . LYS D 4 44   ? 168.127 141.924 160.732 1.00 50.26  ? 41   LYS A NZ    1 
ATOM   1728  N N     . ALA D 4 45   ? 164.182 141.468 164.396 1.00 52.33  ? 42   ALA A N     1 
ATOM   1729  C CA    . ALA D 4 45   ? 164.386 140.094 164.840 1.00 52.33  ? 42   ALA A CA    1 
ATOM   1730  C C     . ALA D 4 45   ? 163.075 139.322 164.854 1.00 52.33  ? 42   ALA A C     1 
ATOM   1731  O O     . ALA D 4 45   ? 163.049 138.130 164.538 1.00 52.33  ? 42   ALA A O     1 
ATOM   1732  C CB    . ALA D 4 45   ? 165.036 140.079 166.223 1.00 52.33  ? 42   ALA A CB    1 
ATOM   1733  N N     . ARG D 4 46   ? 161.976 139.982 165.227 1.00 52.55  ? 43   ARG A N     1 
ATOM   1734  C CA    . ARG D 4 46   ? 160.670 139.330 165.203 1.00 52.55  ? 43   ARG A CA    1 
ATOM   1735  C C     . ARG D 4 46   ? 160.262 138.956 163.784 1.00 52.55  ? 43   ARG A C     1 
ATOM   1736  O O     . ARG D 4 46   ? 159.714 137.873 163.551 1.00 52.55  ? 43   ARG A O     1 
ATOM   1737  C CB    . ARG D 4 46   ? 159.618 140.240 165.835 1.00 52.55  ? 43   ARG A CB    1 
ATOM   1738  C CG    . ARG D 4 46   ? 158.362 139.520 166.287 1.00 52.55  ? 43   ARG A CG    1 
ATOM   1739  C CD    . ARG D 4 46   ? 158.336 139.368 167.795 1.00 52.55  ? 43   ARG A CD    1 
ATOM   1740  N NE    . ARG D 4 46   ? 158.152 140.652 168.461 1.00 52.55  ? 43   ARG A NE    1 
ATOM   1741  C CZ    . ARG D 4 46   ? 158.304 140.848 169.764 1.00 52.55  ? 43   ARG A CZ    1 
ATOM   1742  N NH1   . ARG D 4 46   ? 158.643 139.860 170.576 1.00 52.55  ? 43   ARG A NH1   1 
ATOM   1743  N NH2   . ARG D 4 46   ? 158.112 142.065 170.263 1.00 52.55  ? 43   ARG A NH2   1 
ATOM   1744  N N     . ASN D 4 47   ? 160.280 139.869 162.822 1.00 52.56  ? 44   ASN A N     1 
ATOM   1745  C CA    . ASN D 4 47   ? 159.749 139.482 161.482 1.00 52.56  ? 44   ASN A CA    1 
ATOM   1746  C C     . ASN D 4 47   ? 160.663 138.434 160.851 1.00 52.56  ? 44   ASN A C     1 
ATOM   1747  O O     . ASN D 4 47   ? 160.204 137.713 159.958 1.00 52.56  ? 44   ASN A O     1 
ATOM   1748  C CB    . ASN D 4 47   ? 159.582 140.681 160.554 1.00 52.56  ? 44   ASN A CB    1 
ATOM   1749  C CG    . ASN D 4 47   ? 159.239 140.318 159.127 1.00 52.56  ? 44   ASN A CG    1 
ATOM   1750  O OD1   . ASN D 4 47   ? 158.414 139.441 158.884 1.00 52.56  ? 44   ASN A OD1   1 
ATOM   1751  N ND2   . ASN D 4 47   ? 159.851 141.003 158.176 1.00 52.56  ? 44   ASN A ND2   1 
ATOM   1752  N N     . ASP D 4 48   ? 161.915 138.350 161.293 1.00 58.37  ? 45   ASP A N     1 
ATOM   1753  C CA    . ASP D 4 48   ? 162.857 137.400 160.657 1.00 58.37  ? 45   ASP A CA    1 
ATOM   1754  C C     . ASP D 4 48   ? 162.719 136.066 161.372 1.00 58.37  ? 45   ASP A C     1 
ATOM   1755  O O     . ASP D 4 48   ? 163.086 135.040 160.787 1.00 58.37  ? 45   ASP A O     1 
ATOM   1756  C CB    . ASP D 4 48   ? 164.283 137.944 160.676 1.00 58.37  ? 45   ASP A CB    1 
ATOM   1757  C CG    . ASP D 4 48   ? 164.444 139.224 159.876 1.00 58.37  ? 45   ASP A CG    1 
ATOM   1758  O OD1   . ASP D 4 48   ? 163.458 139.641 159.236 1.00 58.37  ? 45   ASP A OD1   1 
ATOM   1759  O OD2   . ASP D 4 48   ? 165.550 139.798 159.905 1.00 58.37  ? 45   ASP A OD2   1 
ATOM   1760  N N     . HIS D 4 49   ? 162.193 136.089 162.581 1.00 63.39  ? 46   HIS A N     1 
ATOM   1761  C CA    . HIS D 4 49   ? 161.939 134.827 163.302 1.00 63.39  ? 46   HIS A CA    1 
ATOM   1762  C C     . HIS D 4 49   ? 160.690 134.249 162.707 1.00 63.39  ? 46   HIS A C     1 
ATOM   1763  O O     . HIS D 4 49   ? 160.237 133.243 163.180 1.00 63.39  ? 46   HIS A O     1 
ATOM   1764  C CB    . HIS D 4 49   ? 161.654 135.082 164.770 1.00 63.39  ? 46   HIS A CB    1 
ATOM   1765  C CG    . HIS D 4 49   ? 162.806 135.610 165.554 1.00 63.39  ? 46   HIS A CG    1 
ATOM   1766  N ND1   . HIS D 4 49   ? 164.113 135.348 165.210 1.00 63.39  ? 46   HIS A ND1   1 
ATOM   1767  C CD2   . HIS D 4 49   ? 162.850 136.320 166.702 1.00 63.39  ? 46   HIS A CD2   1 
ATOM   1768  C CE1   . HIS D 4 49   ? 164.918 135.912 166.086 1.00 63.39  ? 46   HIS A CE1   1 
ATOM   1769  N NE2   . HIS D 4 49   ? 164.167 136.516 167.012 1.00 63.39  ? 46   HIS A NE2   1 
ATOM   1770  N N     . TYR D 4 50   ? 160.126 134.970 161.764 1.00 78.22  ? 47   TYR A N     1 
ATOM   1771  C CA    . TYR D 4 50   ? 158.851 134.507 161.197 1.00 73.90  ? 47   TYR A CA    1 
ATOM   1772  C C     . TYR D 4 50   ? 159.230 133.343 160.327 1.00 72.72  ? 47   TYR A C     1 
ATOM   1773  O O     . TYR D 4 50   ? 158.742 132.223 160.523 1.00 72.10  ? 47   TYR A O     1 
ATOM   1774  C CB    . TYR D 4 50   ? 158.210 135.602 160.355 1.00 71.19  ? 47   TYR A CB    1 
ATOM   1775  C CG    . TYR D 4 50   ? 156.781 135.346 159.957 1.00 67.71  ? 47   TYR A CG    1 
ATOM   1776  C CD1   . TYR D 4 50   ? 155.770 135.361 160.899 1.00 65.48  ? 47   TYR A CD1   1 
ATOM   1777  C CD2   . TYR D 4 50   ? 156.438 135.099 158.639 1.00 66.53  ? 47   TYR A CD2   1 
ATOM   1778  C CE1   . TYR D 4 50   ? 154.454 135.136 160.543 1.00 64.09  ? 47   TYR A CE1   1 
ATOM   1779  C CE2   . TYR D 4 50   ? 155.124 134.868 158.268 1.00 64.91  ? 47   TYR A CE2   1 
ATOM   1780  C CZ    . TYR D 4 50   ? 154.129 134.887 159.226 1.00 64.34  ? 47   TYR A CZ    1 
ATOM   1781  O OH    . TYR D 4 50   ? 152.832 134.661 158.874 1.00 60.55  ? 47   TYR A OH    1 
ATOM   1782  N N     . LYS D 4 51   ? 160.098 133.620 159.387 1.00 72.22  ? 48   LYS A N     1 
ATOM   1783  C CA    . LYS D 4 51   ? 160.631 132.499 158.603 1.00 69.41  ? 48   LYS A CA    1 
ATOM   1784  C C     . LYS D 4 51   ? 161.360 131.535 159.542 1.00 70.71  ? 48   LYS A C     1 
ATOM   1785  O O     . LYS D 4 51   ? 161.289 130.345 159.278 1.00 69.55  ? 48   LYS A O     1 
ATOM   1786  C CB    . LYS D 4 51   ? 161.565 133.032 157.515 1.00 68.43  ? 48   LYS A CB    1 
ATOM   1787  C CG    . LYS D 4 51   ? 160.998 134.173 156.682 1.00 68.21  ? 48   LYS A CG    1 
ATOM   1788  C CD    . LYS D 4 51   ? 161.996 134.755 155.705 1.00 69.74  ? 48   LYS A CD    1 
ATOM   1789  C CE    . LYS D 4 51   ? 161.438 135.917 154.911 1.00 69.49  ? 48   LYS A CE    1 
ATOM   1790  N NZ    . LYS D 4 51   ? 162.432 136.452 153.951 1.00 69.69  ? 48   LYS A NZ    1 
ATOM   1791  N N     . GLU D 4 52   ? 162.063 132.003 160.603 1.00 71.98  ? 49   GLU A N     1 
ATOM   1792  C CA    . GLU D 4 52   ? 162.678 130.922 161.366 1.00 74.88  ? 49   GLU A CA    1 
ATOM   1793  C C     . GLU D 4 52   ? 161.620 130.049 162.030 1.00 76.15  ? 49   GLU A C     1 
ATOM   1794  O O     . GLU D 4 52   ? 161.789 128.828 162.135 1.00 78.41  ? 49   GLU A O     1 
ATOM   1795  C CB    . GLU D 4 52   ? 163.631 131.492 162.418 1.00 79.05  ? 49   GLU A CB    1 
ATOM   1796  C CG    . GLU D 4 52   ? 164.920 132.073 161.862 1.00 80.27  ? 49   GLU A CG    1 
ATOM   1797  C CD    . GLU D 4 52   ? 165.707 132.835 162.912 1.00 82.96  ? 49   GLU A CD    1 
ATOM   1798  O OE1   . GLU D 4 52   ? 165.403 134.028 163.135 1.00 82.09  ? 49   GLU A OE1   1 
ATOM   1799  O OE2   . GLU D 4 52   ? 166.618 132.240 163.525 1.00 86.24  ? 49   GLU A OE2   1 
ATOM   1800  N N     . LEU D 4 53   ? 160.520 130.657 162.477 1.00 74.85  ? 50   LEU A N     1 
ATOM   1801  C CA    . LEU D 4 53   ? 159.509 129.931 163.233 1.00 73.79  ? 50   LEU A CA    1 
ATOM   1802  C C     . LEU D 4 53   ? 158.550 129.159 162.333 1.00 74.49  ? 50   LEU A C     1 
ATOM   1803  O O     . LEU D 4 53   ? 158.010 128.129 162.756 1.00 76.10  ? 50   LEU A O     1 
ATOM   1804  C CB    . LEU D 4 53   ? 158.734 130.905 164.121 1.00 72.32  ? 50   LEU A CB    1 
ATOM   1805  C CG    . LEU D 4 53   ? 157.624 130.342 165.005 1.00 73.52  ? 50   LEU A CG    1 
ATOM   1806  C CD1   . LEU D 4 53   ? 158.159 129.246 165.911 1.00 76.56  ? 50   LEU A CD1   1 
ATOM   1807  C CD2   . LEU D 4 53   ? 156.987 131.454 165.819 1.00 76.16  ? 50   LEU A CD2   1 
ATOM   1808  N N     . LYS D 4 54   ? 158.330 129.630 161.105 1.00 72.11  ? 51   LYS A N     1 
ATOM   1809  C CA    . LYS D 4 54   ? 157.394 128.975 160.191 1.00 67.69  ? 51   LYS A CA    1 
ATOM   1810  C C     . LYS D 4 54   ? 157.672 127.488 159.988 1.00 63.77  ? 51   LYS A C     1 
ATOM   1811  O O     . LYS D 4 54   ? 156.725 126.692 160.097 1.00 60.79  ? 51   LYS A O     1 
ATOM   1812  C CB    . LYS D 4 54   ? 157.387 129.723 158.850 1.00 69.19  ? 51   LYS A CB    1 
ATOM   1813  C CG    . LYS D 4 54   ? 156.730 128.953 157.714 1.00 69.43  ? 51   LYS A CG    1 
ATOM   1814  C CD    . LYS D 4 54   ? 157.130 129.517 156.362 1.00 69.55  ? 51   LYS A CD    1 
ATOM   1815  C CE    . LYS D 4 54   ? 156.673 128.609 155.229 1.00 69.75  ? 51   LYS A CE    1 
ATOM   1816  N NZ    . LYS D 4 54   ? 157.236 129.028 153.915 1.00 68.75  ? 51   LYS A NZ    1 
ATOM   1817  N N     . PRO D 4 55   ? 158.902 127.040 159.700 1.00 63.44  ? 52   PRO A N     1 
ATOM   1818  C CA    . PRO D 4 55   ? 159.117 125.590 159.568 1.00 62.36  ? 52   PRO A CA    1 
ATOM   1819  C C     . PRO D 4 55   ? 158.918 124.837 160.870 1.00 67.62  ? 52   PRO A C     1 
ATOM   1820  O O     . PRO D 4 55   ? 158.513 123.669 160.839 1.00 66.54  ? 52   PRO A O     1 
ATOM   1821  C CB    . PRO D 4 55   ? 160.569 125.487 159.075 1.00 62.28  ? 52   PRO A CB    1 
ATOM   1822  C CG    . PRO D 4 55   ? 160.889 126.836 158.523 1.00 63.28  ? 52   PRO A CG    1 
ATOM   1823  C CD    . PRO D 4 55   ? 160.131 127.791 159.386 1.00 64.75  ? 52   PRO A CD    1 
ATOM   1824  N N     . ILE D 4 56   ? 159.190 125.470 162.013 1.00 72.56  ? 53   ILE A N     1 
ATOM   1825  C CA    . ILE D 4 56   ? 158.966 124.816 163.298 1.00 65.78  ? 53   ILE A CA    1 
ATOM   1826  C C     . ILE D 4 56   ? 157.476 124.583 163.521 1.00 82.29  ? 53   ILE A C     1 
ATOM   1827  O O     . ILE D 4 56   ? 157.055 123.495 163.932 1.00 65.42  ? 53   ILE A O     1 
ATOM   1828  C CB    . ILE D 4 56   ? 159.583 125.650 164.437 1.00 85.92  ? 53   ILE A CB    1 
ATOM   1829  C CG1   . ILE D 4 56   ? 161.072 125.881 164.171 1.00 86.54  ? 53   ILE A CG1   1 
ATOM   1830  C CG2   . ILE D 4 56   ? 159.370 124.965 165.779 1.00 70.77  ? 53   ILE A CG2   1 
ATOM   1831  C CD1   . ILE D 4 56   ? 161.714 126.867 165.117 1.00 71.87  ? 53   ILE A CD1   1 
ATOM   1832  N N     . ILE D 4 57   ? 156.657 125.603 163.253 1.00 74.06  ? 54   ILE A N     1 
ATOM   1833  C CA    . ILE D 4 57   ? 155.211 125.462 163.408 1.00 73.58  ? 54   ILE A CA    1 
ATOM   1834  C C     . ILE D 4 57   ? 154.671 124.419 162.437 1.00 73.04  ? 54   ILE A C     1 
ATOM   1835  O O     . ILE D 4 57   ? 153.743 123.667 162.764 1.00 73.12  ? 54   ILE A O     1 
ATOM   1836  C CB    . ILE D 4 57   ? 154.518 126.825 163.218 1.00 73.25  ? 54   ILE A CB    1 
ATOM   1837  C CG1   . ILE D 4 57   ? 154.978 127.813 164.289 1.00 76.27  ? 54   ILE A CG1   1 
ATOM   1838  C CG2   . ILE D 4 57   ? 153.004 126.671 163.252 1.00 72.59  ? 54   ILE A CG2   1 
ATOM   1839  C CD1   . ILE D 4 57   ? 154.271 129.150 164.223 1.00 76.34  ? 54   ILE A CD1   1 
ATOM   1840  N N     . ASP D 4 58   ? 155.249 124.349 161.236 1.00 72.26  ? 55   ASP A N     1 
ATOM   1841  C CA    . ASP D 4 58   ? 154.793 123.385 160.242 1.00 73.17  ? 55   ASP A CA    1 
ATOM   1842  C C     . ASP D 4 58   ? 154.965 121.945 160.705 1.00 75.72  ? 55   ASP A C     1 
ATOM   1843  O O     . ASP D 4 58   ? 154.261 121.062 160.205 1.00 74.53  ? 55   ASP A O     1 
ATOM   1844  C CB    . ASP D 4 58   ? 155.531 123.600 158.921 1.00 74.50  ? 55   ASP A CB    1 
ATOM   1845  C CG    . ASP D 4 58   ? 155.023 124.810 158.162 1.00 74.93  ? 55   ASP A CG    1 
ATOM   1846  O OD1   . ASP D 4 58   ? 153.828 125.141 158.306 1.00 75.35  ? 55   ASP A OD1   1 
ATOM   1847  O OD2   . ASP D 4 58   ? 155.818 125.429 157.422 1.00 74.56  ? 55   ASP A OD2   1 
ATOM   1848  N N     . ARG D 4 59   ? 155.878 121.686 161.645 1.00 80.59  ? 56   ARG A N     1 
ATOM   1849  C CA    . ARG D 4 59   ? 156.015 120.334 162.177 1.00 84.18  ? 56   ARG A CA    1 
ATOM   1850  C C     . ARG D 4 59   ? 154.715 119.847 162.800 1.00 85.42  ? 56   ARG A C     1 
ATOM   1851  O O     . ARG D 4 59   ? 154.401 118.654 162.727 1.00 86.16  ? 56   ARG A O     1 
ATOM   1852  C CB    . ARG D 4 59   ? 157.142 120.276 163.207 1.00 87.61  ? 56   ARG A CB    1 
ATOM   1853  C CG    . ARG D 4 59   ? 158.498 120.727 162.692 1.00 88.35  ? 56   ARG A CG    1 
ATOM   1854  C CD    . ARG D 4 59   ? 159.617 120.048 163.464 1.00 91.36  ? 56   ARG A CD    1 
ATOM   1855  N NE    . ARG D 4 59   ? 160.899 120.725 163.301 1.00 92.31  ? 56   ARG A NE    1 
ATOM   1856  C CZ    . ARG D 4 59   ? 161.450 121.507 164.225 1.00 93.28  ? 56   ARG A CZ    1 
ATOM   1857  N NH1   . ARG D 4 59   ? 160.833 121.705 165.383 1.00 93.28  ? 56   ARG A NH1   1 
ATOM   1858  N NH2   . ARG D 4 59   ? 162.621 122.086 163.995 1.00 93.93  ? 56   ARG A NH2   1 
ATOM   1859  N N     . ILE D 4 60   ? 153.946 120.750 163.410 1.00 87.19  ? 57   ILE A N     1 
ATOM   1860  C CA    . ILE D 4 60   ? 152.666 120.367 163.997 1.00 87.35  ? 57   ILE A CA    1 
ATOM   1861  C C     . ILE D 4 60   ? 151.687 119.943 162.909 1.00 85.46  ? 57   ILE A C     1 
ATOM   1862  O O     . ILE D 4 60   ? 151.014 118.913 163.023 1.00 87.46  ? 57   ILE A O     1 
ATOM   1863  C CB    . ILE D 4 60   ? 152.100 121.518 164.847 1.00 88.27  ? 57   ILE A CB    1 
ATOM   1864  C CG1   . ILE D 4 60   ? 153.104 121.924 165.926 1.00 91.73  ? 57   ILE A CG1   1 
ATOM   1865  C CG2   . ILE D 4 60   ? 150.773 121.117 165.471 1.00 89.37  ? 57   ILE A CG2   1 
ATOM   1866  C CD1   . ILE D 4 60   ? 152.643 123.079 166.783 1.00 93.85  ? 57   ILE A CD1   1 
ATOM   1867  N N     . TYR D 4 61   ? 151.593 120.734 161.837 1.00 76.75  ? 58   TYR A N     1 
ATOM   1868  C CA    . TYR D 4 61   ? 150.712 120.379 160.730 1.00 70.22  ? 58   TYR A CA    1 
ATOM   1869  C C     . TYR D 4 61   ? 151.175 119.097 160.050 1.00 67.48  ? 58   TYR A C     1 
ATOM   1870  O O     . TYR D 4 61   ? 150.378 118.182 159.818 1.00 64.94  ? 58   TYR A O     1 
ATOM   1871  C CB    . TYR D 4 61   ? 150.648 121.523 159.717 1.00 67.06  ? 58   TYR A CB    1 
ATOM   1872  C CG    . TYR D 4 61   ? 150.013 122.789 160.243 1.00 68.31  ? 58   TYR A CG    1 
ATOM   1873  C CD1   . TYR D 4 61   ? 148.642 122.869 160.444 1.00 70.21  ? 58   TYR A CD1   1 
ATOM   1874  C CD2   . TYR D 4 61   ? 150.785 123.909 160.522 1.00 69.10  ? 58   TYR A CD2   1 
ATOM   1875  C CE1   . TYR D 4 61   ? 148.056 124.027 160.919 1.00 70.75  ? 58   TYR A CE1   1 
ATOM   1876  C CE2   . TYR D 4 61   ? 150.208 125.071 160.998 1.00 70.85  ? 58   TYR A CE2   1 
ATOM   1877  C CZ    . TYR D 4 61   ? 148.843 125.123 161.194 1.00 71.54  ? 58   TYR A CZ    1 
ATOM   1878  O OH    . TYR D 4 61   ? 148.262 126.277 161.665 1.00 72.82  ? 58   TYR A OH    1 
ATOM   1879  N N     . LYS D 4 62   ? 152.469 119.016 159.724 1.00 66.76  ? 59   LYS A N     1 
ATOM   1880  C CA    . LYS D 4 62   ? 152.989 117.851 159.016 1.00 64.88  ? 59   LYS A CA    1 
ATOM   1881  C C     . LYS D 4 62   ? 152.775 116.574 159.820 1.00 69.08  ? 59   LYS A C     1 
ATOM   1882  O O     . LYS D 4 62   ? 152.313 115.561 159.286 1.00 70.16  ? 59   LYS A O     1 
ATOM   1883  C CB    . LYS D 4 62   ? 154.472 118.046 158.699 1.00 64.02  ? 59   LYS A CB    1 
ATOM   1884  C CG    . LYS D 4 62   ? 154.761 119.169 157.714 1.00 62.74  ? 59   LYS A CG    1 
ATOM   1885  C CD    . LYS D 4 62   ? 156.248 119.267 157.405 1.00 63.27  ? 59   LYS A CD    1 
ATOM   1886  C CE    . LYS D 4 62   ? 157.064 119.543 158.658 1.00 66.52  ? 59   LYS A CE    1 
ATOM   1887  N NZ    . LYS D 4 62   ? 158.521 119.642 158.367 1.00 66.37  ? 59   LYS A NZ    1 
ATOM   1888  N N     . THR D 4 63   ? 153.101 116.609 161.114 1.00 73.25  ? 60   THR A N     1 
ATOM   1889  C CA    . THR D 4 63   ? 152.956 115.417 161.944 1.00 76.55  ? 60   THR A CA    1 
ATOM   1890  C C     . THR D 4 63   ? 151.491 115.029 162.095 1.00 78.91  ? 60   THR A C     1 
ATOM   1891  O O     . THR D 4 63   ? 151.124 113.866 161.892 1.00 79.19  ? 60   THR A O     1 
ATOM   1892  C CB    . THR D 4 63   ? 153.596 115.647 163.313 1.00 80.26  ? 60   THR A CB    1 
ATOM   1893  O OG1   . THR D 4 63   ? 154.917 116.177 163.139 1.00 82.54  ? 60   THR A OG1   1 
ATOM   1894  C CG2   . THR D 4 63   ? 153.680 114.341 164.089 1.00 81.68  ? 60   THR A CG2   1 
ATOM   1895  N N     . TYR D 4 64   ? 150.635 115.992 162.447 1.00 81.09  ? 61   TYR A N     1 
ATOM   1896  C CA    . TYR D 4 64   ? 149.225 115.684 162.660 1.00 83.09  ? 61   TYR A CA    1 
ATOM   1897  C C     . TYR D 4 64   ? 148.561 115.204 161.377 1.00 83.80  ? 61   TYR A C     1 
ATOM   1898  O O     . TYR D 4 64   ? 147.777 114.247 161.396 1.00 84.04  ? 61   TYR A O     1 
ATOM   1899  C CB    . TYR D 4 64   ? 148.496 116.903 163.219 1.00 81.79  ? 61   TYR A CB    1 
ATOM   1900  C CG    . TYR D 4 64   ? 147.003 116.706 163.347 1.00 79.80  ? 61   TYR A CG    1 
ATOM   1901  C CD1   . TYR D 4 64   ? 146.468 115.977 164.401 1.00 80.90  ? 61   TYR A CD1   1 
ATOM   1902  C CD2   . TYR D 4 64   ? 146.130 117.247 162.414 1.00 77.87  ? 61   TYR A CD2   1 
ATOM   1903  C CE1   . TYR D 4 64   ? 145.104 115.791 164.519 1.00 81.09  ? 61   TYR A CE1   1 
ATOM   1904  C CE2   . TYR D 4 64   ? 144.767 117.069 162.523 1.00 77.99  ? 61   TYR A CE2   1 
ATOM   1905  C CZ    . TYR D 4 64   ? 144.259 116.340 163.579 1.00 79.63  ? 61   TYR A CZ    1 
ATOM   1906  O OH    . TYR D 4 64   ? 142.899 116.162 163.688 1.00 79.57  ? 61   TYR A OH    1 
ATOM   1907  N N     . ALA D 4 65   ? 148.858 115.855 160.249 1.00 84.26  ? 62   ALA A N     1 
ATOM   1908  C CA    . ALA D 4 65   ? 148.285 115.417 158.979 1.00 84.02  ? 62   ALA A CA    1 
ATOM   1909  C C     . ALA D 4 65   ? 148.791 114.033 158.600 1.00 85.43  ? 62   ALA A C     1 
ATOM   1910  O O     . ALA D 4 65   ? 148.015 113.183 158.146 1.00 86.51  ? 62   ALA A O     1 
ATOM   1911  C CB    . ALA D 4 65   ? 148.601 116.426 157.875 1.00 82.50  ? 62   ALA A CB    1 
ATOM   1912  N N     . ASP D 4 66   ? 150.089 113.784 158.784 1.00 86.48  ? 63   ASP A N     1 
ATOM   1913  C CA    . ASP D 4 66   ? 150.638 112.470 158.468 1.00 88.87  ? 63   ASP A CA    1 
ATOM   1914  C C     . ASP D 4 66   ? 150.031 111.395 159.361 1.00 90.28  ? 63   ASP A C     1 
ATOM   1915  O O     . ASP D 4 66   ? 149.727 110.292 158.895 1.00 91.39  ? 63   ASP A O     1 
ATOM   1916  C CB    . ASP D 4 66   ? 152.162 112.495 158.603 1.00 93.16  ? 63   ASP A CB    1 
ATOM   1917  C CG    . ASP D 4 66   ? 152.836 111.361 157.856 1.00 97.49  ? 63   ASP A CG    1 
ATOM   1918  O OD1   . ASP D 4 66   ? 152.429 110.194 158.035 1.00 100.21 ? 63   ASP A OD1   1 
ATOM   1919  O OD2   . ASP D 4 66   ? 153.775 111.641 157.081 1.00 98.07  ? 63   ASP A OD2   1 
ATOM   1920  N N     . GLN D 4 67   ? 149.836 111.704 160.645 1.00 89.86  ? 64   GLN A N     1 
ATOM   1921  C CA    . GLN D 4 67   ? 149.250 110.726 161.559 1.00 88.06  ? 64   GLN A CA    1 
ATOM   1922  C C     . GLN D 4 67   ? 147.805 110.415 161.187 1.00 83.49  ? 64   GLN A C     1 
ATOM   1923  O O     . GLN D 4 67   ? 147.377 109.257 161.262 1.00 83.81  ? 64   GLN A O     1 
ATOM   1924  C CB    . GLN D 4 67   ? 149.336 111.234 162.998 1.00 88.84  ? 64   GLN A CB    1 
ATOM   1925  C CG    . GLN D 4 67   ? 150.738 111.205 163.583 1.00 90.92  ? 64   GLN A CG    1 
ATOM   1926  C CD    . GLN D 4 67   ? 150.811 111.856 164.950 1.00 94.52  ? 64   GLN A CD    1 
ATOM   1927  O OE1   . GLN D 4 67   ? 150.690 113.072 165.077 1.00 97.42  ? 64   GLN A OE1   1 
ATOM   1928  N NE2   . GLN D 4 67   ? 151.007 111.043 165.982 1.00 94.55  ? 64   GLN A NE2   1 
ATOM   1929  N N     . CYS D 4 68   ? 147.040 111.431 160.780 1.00 79.56  ? 65   CYS A N     1 
ATOM   1930  C CA    . CYS D 4 68   ? 145.650 111.200 160.399 1.00 77.17  ? 65   CYS A CA    1 
ATOM   1931  C C     . CYS D 4 68   ? 145.539 110.401 159.107 1.00 74.34  ? 65   CYS A C     1 
ATOM   1932  O O     . CYS D 4 68   ? 144.595 109.621 158.943 1.00 71.82  ? 65   CYS A O     1 
ATOM   1933  C CB    . CYS D 4 68   ? 144.910 112.530 160.263 1.00 77.04  ? 65   CYS A CB    1 
ATOM   1934  S SG    . CYS D 4 68   ? 144.631 113.391 161.826 1.00 81.69  ? 65   CYS A SG    1 
ATOM   1935  N N     . LEU D 4 69   ? 146.483 110.577 158.183 1.00 73.22  ? 66   LEU A N     1 
ATOM   1936  C CA    . LEU D 4 69   ? 146.447 109.852 156.920 1.00 71.15  ? 66   LEU A CA    1 
ATOM   1937  C C     . LEU D 4 69   ? 146.896 108.404 157.051 1.00 75.33  ? 66   LEU A C     1 
ATOM   1938  O O     . LEU D 4 69   ? 146.710 107.630 156.107 1.00 77.12  ? 66   LEU A O     1 
ATOM   1939  C CB    . LEU D 4 69   ? 147.311 110.569 155.877 1.00 65.00  ? 66   LEU A CB    1 
ATOM   1940  C CG    . LEU D 4 69   ? 146.822 111.956 155.452 1.00 58.74  ? 66   LEU A CG    1 
ATOM   1941  C CD1   . LEU D 4 69   ? 147.762 112.588 154.436 1.00 54.64  ? 66   LEU A CD1   1 
ATOM   1942  C CD2   . LEU D 4 69   ? 145.405 111.887 154.905 1.00 56.42  ? 66   LEU A CD2   1 
ATOM   1943  N N     . GLN D 4 70   ? 147.478 108.013 158.188 1.00 78.16  ? 67   GLN A N     1 
ATOM   1944  C CA    . GLN D 4 70   ? 147.919 106.633 158.354 1.00 82.42  ? 67   GLN A CA    1 
ATOM   1945  C C     . GLN D 4 70   ? 146.758 105.690 158.644 1.00 85.59  ? 67   GLN A C     1 
ATOM   1946  O O     . GLN D 4 70   ? 146.856 104.490 158.362 1.00 87.67  ? 67   GLN A O     1 
ATOM   1947  C CB    . GLN D 4 70   ? 148.960 106.537 159.471 1.00 85.82  ? 67   GLN A CB    1 
ATOM   1948  C CG    . GLN D 4 70   ? 150.284 107.214 159.154 1.00 85.53  ? 67   GLN A CG    1 
ATOM   1949  C CD    . GLN D 4 70   ? 151.281 107.102 160.291 1.00 87.69  ? 67   GLN A CD    1 
ATOM   1950  O OE1   . GLN D 4 70   ? 151.612 106.002 160.732 1.00 89.72  ? 67   GLN A OE1   1 
ATOM   1951  N NE2   . GLN D 4 70   ? 151.759 108.244 160.779 1.00 87.30  ? 67   GLN A NE2   1 
ATOM   1952  N N     . LEU D 4 71   ? 145.662 106.201 159.202 1.00 86.89  ? 68   LEU A N     1 
ATOM   1953  C CA    . LEU D 4 71   ? 144.509 105.378 159.540 1.00 90.18  ? 68   LEU A CA    1 
ATOM   1954  C C     . LEU D 4 71   ? 143.453 105.349 158.443 1.00 90.06  ? 68   LEU A C     1 
ATOM   1955  O O     . LEU D 4 71   ? 142.401 104.730 158.635 1.00 91.05  ? 68   LEU A O     1 
ATOM   1956  C CB    . LEU D 4 71   ? 143.868 105.870 160.841 1.00 92.47  ? 68   LEU A CB    1 
ATOM   1957  C CG    . LEU D 4 71   ? 144.734 105.904 162.101 1.00 94.87  ? 68   LEU A CG    1 
ATOM   1958  C CD1   . LEU D 4 71   ? 145.154 107.326 162.419 1.00 93.49  ? 68   LEU A CD1   1 
ATOM   1959  C CD2   . LEU D 4 71   ? 143.988 105.288 163.274 1.00 98.14  ? 68   LEU A CD2   1 
ATOM   1960  N N     . VAL D 4 72   ? 143.697 106.000 157.307 1.00 88.71  ? 69   VAL A N     1 
ATOM   1961  C CA    . VAL D 4 72   ? 142.678 106.101 156.268 1.00 86.66  ? 69   VAL A CA    1 
ATOM   1962  C C     . VAL D 4 72   ? 142.555 104.763 155.549 1.00 86.87  ? 69   VAL A C     1 
ATOM   1963  O O     . VAL D 4 72   ? 143.523 104.262 154.965 1.00 87.21  ? 69   VAL A O     1 
ATOM   1964  C CB    . VAL D 4 72   ? 143.005 107.230 155.284 1.00 81.61  ? 69   VAL A CB    1 
ATOM   1965  C CG1   . VAL D 4 72   ? 141.927 107.324 154.217 1.00 79.70  ? 69   VAL A CG1   1 
ATOM   1966  C CG2   . VAL D 4 72   ? 143.144 108.552 156.022 1.00 80.65  ? 69   VAL A CG2   1 
ATOM   1967  N N     . GLN D 4 73   ? 141.358 104.183 155.588 1.00 88.38  ? 70   GLN A N     1 
ATOM   1968  C CA    . GLN D 4 73   ? 141.034 102.959 154.859 1.00 88.49  ? 70   GLN A CA    1 
ATOM   1969  C C     . GLN D 4 73   ? 139.694 103.172 154.167 1.00 85.74  ? 70   GLN A C     1 
ATOM   1970  O O     . GLN D 4 73   ? 138.661 103.277 154.835 1.00 87.42  ? 70   GLN A O     1 
ATOM   1971  C CB    . GLN D 4 73   ? 140.980 101.747 155.791 1.00 94.00  ? 70   GLN A CB    1 
ATOM   1972  C CG    . GLN D 4 73   ? 142.238 100.889 155.792 1.00 99.61  ? 70   GLN A CG    1 
ATOM   1973  C CD    . GLN D 4 73   ? 143.406 101.549 156.500 1.00 102.76 ? 70   GLN A CD    1 
ATOM   1974  O OE1   . GLN D 4 73   ? 144.383 101.954 155.868 1.00 104.11 ? 70   GLN A OE1   1 
ATOM   1975  N NE2   . GLN D 4 73   ? 143.310 101.662 157.820 1.00 102.05 ? 70   GLN A NE2   1 
ATOM   1976  N N     . LEU D 4 74   ? 139.711 103.240 152.838 1.00 83.59  ? 71   LEU A N     1 
ATOM   1977  C CA    . LEU D 4 74   ? 138.506 103.484 152.061 1.00 80.35  ? 71   LEU A CA    1 
ATOM   1978  C C     . LEU D 4 74   ? 138.413 102.491 150.912 1.00 78.91  ? 71   LEU A C     1 
ATOM   1979  O O     . LEU D 4 74   ? 139.405 101.889 150.495 1.00 79.78  ? 71   LEU A O     1 
ATOM   1980  C CB    . LEU D 4 74   ? 138.471 104.914 151.506 1.00 74.28  ? 71   LEU A CB    1 
ATOM   1981  C CG    . LEU D 4 74   ? 138.408 106.050 152.523 1.00 71.19  ? 71   LEU A CG    1 
ATOM   1982  C CD1   . LEU D 4 74   ? 138.339 107.385 151.804 1.00 67.32  ? 71   LEU A CD1   1 
ATOM   1983  C CD2   . LEU D 4 74   ? 137.218 105.873 153.451 1.00 71.98  ? 71   LEU A CD2   1 
ATOM   1984  N N     . ASP D 4 75   ? 137.192 102.332 150.404 1.00 78.75  ? 72   ASP A N     1 
ATOM   1985  C CA    . ASP D 4 75   ? 136.920 101.507 149.234 1.00 80.11  ? 72   ASP A CA    1 
ATOM   1986  C C     . ASP D 4 75   ? 136.772 102.436 148.036 1.00 78.86  ? 72   ASP A C     1 
ATOM   1987  O O     . ASP D 4 75   ? 135.764 103.137 147.904 1.00 79.00  ? 72   ASP A O     1 
ATOM   1988  C CB    . ASP D 4 75   ? 135.663 100.663 149.441 1.00 83.64  ? 72   ASP A CB    1 
ATOM   1989  C CG    . ASP D 4 75   ? 135.529 99.549  148.419 1.00 87.93  ? 72   ASP A CG    1 
ATOM   1990  O OD1   . ASP D 4 75   ? 136.121 99.658  147.325 1.00 89.44  ? 72   ASP A OD1   1 
ATOM   1991  O OD2   . ASP D 4 75   ? 134.828 98.558  148.712 1.00 91.11  ? 72   ASP A OD2   1 
ATOM   1992  N N     . TRP D 4 76   ? 137.778 102.442 147.165 1.00 77.19  ? 73   TRP A N     1 
ATOM   1993  C CA    . TRP D 4 76   ? 137.835 103.358 146.035 1.00 74.62  ? 73   TRP A CA    1 
ATOM   1994  C C     . TRP D 4 76   ? 137.110 102.829 144.803 1.00 76.79  ? 73   TRP A C     1 
ATOM   1995  O O     . TRP D 4 76   ? 137.268 103.397 143.718 1.00 76.14  ? 73   TRP A O     1 
ATOM   1996  C CB    . TRP D 4 76   ? 139.292 103.663 145.685 1.00 70.57  ? 73   TRP A CB    1 
ATOM   1997  C CG    . TRP D 4 76   ? 140.098 104.151 146.849 1.00 67.54  ? 73   TRP A CG    1 
ATOM   1998  C CD1   . TRP D 4 76   ? 140.755 103.387 147.770 1.00 67.81  ? 73   TRP A CD1   1 
ATOM   1999  C CD2   . TRP D 4 76   ? 140.336 105.515 147.217 1.00 65.75  ? 73   TRP A CD2   1 
ATOM   2000  N NE1   . TRP D 4 76   ? 141.385 104.188 148.689 1.00 67.17  ? 73   TRP A NE1   1 
ATOM   2001  C CE2   . TRP D 4 76   ? 141.144 105.500 148.372 1.00 66.42  ? 73   TRP A CE2   1 
ATOM   2002  C CE3   . TRP D 4 76   ? 139.945 106.746 146.684 1.00 63.59  ? 73   TRP A CE3   1 
ATOM   2003  C CZ2   . TRP D 4 76   ? 141.568 106.669 149.003 1.00 65.46  ? 73   TRP A CZ2   1 
ATOM   2004  C CZ3   . TRP D 4 76   ? 140.365 107.905 147.311 1.00 61.89  ? 73   TRP A CZ3   1 
ATOM   2005  C CH2   . TRP D 4 76   ? 141.168 107.858 148.457 1.00 63.01  ? 73   TRP A CH2   1 
ATOM   2006  N N     . GLU D 4 77   ? 136.320 101.761 144.944 1.00 83.38  ? 74   GLU A N     1 
ATOM   2007  C CA    . GLU D 4 77   ? 135.653 101.181 143.782 1.00 87.04  ? 74   GLU A CA    1 
ATOM   2008  C C     . GLU D 4 77   ? 134.592 102.121 143.221 1.00 85.01  ? 74   GLU A C     1 
ATOM   2009  O O     . GLU D 4 77   ? 134.417 102.209 142.000 1.00 83.95  ? 74   GLU A O     1 
ATOM   2010  C CB    . GLU D 4 77   ? 135.035 99.832  144.153 1.00 93.55  ? 74   GLU A CB    1 
ATOM   2011  C CG    . GLU D 4 77   ? 134.408 99.095  142.981 1.00 99.07  ? 74   GLU A CG    1 
ATOM   2012  C CD    . GLU D 4 77   ? 135.425 98.700  141.927 1.00 103.74 ? 74   GLU A CD    1 
ATOM   2013  O OE1   . GLU D 4 77   ? 136.592 98.440  142.291 1.00 105.48 ? 74   GLU A OE1   1 
ATOM   2014  O OE2   . GLU D 4 77   ? 135.059 98.653  140.733 1.00 105.20 ? 74   GLU A OE2   1 
ATOM   2015  N N     . ASN D 4 78   ? 133.876 102.833 144.094 1.00 83.74  ? 75   ASN A N     1 
ATOM   2016  C CA    . ASN D 4 78   ? 132.842 103.751 143.625 1.00 81.18  ? 75   ASN A CA    1 
ATOM   2017  C C     . ASN D 4 78   ? 133.448 104.923 142.866 1.00 76.47  ? 75   ASN A C     1 
ATOM   2018  O O     . ASN D 4 78   ? 132.896 105.364 141.851 1.00 75.05  ? 75   ASN A O     1 
ATOM   2019  C CB    . ASN D 4 78   ? 132.006 104.246 144.803 1.00 83.59  ? 75   ASN A CB    1 
ATOM   2020  C CG    . ASN D 4 78   ? 131.196 103.140 145.447 1.00 87.54  ? 75   ASN A CG    1 
ATOM   2021  O OD1   . ASN D 4 78   ? 130.011 102.975 145.160 1.00 88.15  ? 75   ASN A OD1   1 
ATOM   2022  N ND2   . ASN D 4 78   ? 131.836 102.370 146.321 1.00 89.66  ? 75   ASN A ND2   1 
ATOM   2023  N N     . LEU D 4 79   ? 134.581 105.442 143.343 1.00 73.26  ? 76   LEU A N     1 
ATOM   2024  C CA    . LEU D 4 79   ? 135.230 106.555 142.658 1.00 66.85  ? 76   LEU A CA    1 
ATOM   2025  C C     . LEU D 4 79   ? 135.736 106.137 141.283 1.00 62.54  ? 76   LEU A C     1 
ATOM   2026  O O     . LEU D 4 79   ? 135.662 106.914 140.325 1.00 61.31  ? 76   LEU A O     1 
ATOM   2027  C CB    . LEU D 4 79   ? 136.373 107.102 143.513 1.00 62.16  ? 76   LEU A CB    1 
ATOM   2028  C CG    . LEU D 4 79   ? 137.105 108.336 142.984 1.00 54.99  ? 76   LEU A CG    1 
ATOM   2029  C CD1   . LEU D 4 79   ? 136.127 109.472 142.731 1.00 50.61  ? 76   LEU A CD1   1 
ATOM   2030  C CD2   . LEU D 4 79   ? 138.185 108.768 143.962 1.00 53.62  ? 76   LEU A CD2   1 
ATOM   2031  N N     . SER D 4 80   ? 136.246 104.908 141.164 1.00 62.07  ? 77   SER A N     1 
ATOM   2032  C CA    . SER D 4 80   ? 136.719 104.427 139.870 1.00 61.99  ? 77   SER A CA    1 
ATOM   2033  C C     . SER D 4 80   ? 135.574 104.310 138.873 1.00 63.06  ? 77   SER A C     1 
ATOM   2034  O O     . SER D 4 80   ? 135.740 104.624 137.687 1.00 62.63  ? 77   SER A O     1 
ATOM   2035  C CB    . SER D 4 80   ? 137.419 103.079 140.036 1.00 64.84  ? 77   SER A CB    1 
ATOM   2036  O OG    . SER D 4 80   ? 137.786 102.535 138.780 1.00 66.14  ? 77   SER A OG    1 
ATOM   2037  N N     . ALA D 4 81   ? 134.404 103.860 139.333 1.00 63.69  ? 78   ALA A N     1 
ATOM   2038  C CA    . ALA D 4 81   ? 133.270 103.702 138.429 1.00 63.04  ? 78   ALA A CA    1 
ATOM   2039  C C     . ALA D 4 81   ? 132.769 105.053 137.932 1.00 59.75  ? 78   ALA A C     1 
ATOM   2040  O O     . ALA D 4 81   ? 132.323 105.170 136.784 1.00 61.45  ? 78   ALA A O     1 
ATOM   2041  C CB    . ALA D 4 81   ? 132.146 102.934 139.121 1.00 64.74  ? 78   ALA A CB    1 
ATOM   2042  N N     . ALA D 4 82   ? 132.823 106.080 138.784 1.00 56.33  ? 79   ALA A N     1 
ATOM   2043  C CA    . ALA D 4 82   ? 132.421 107.415 138.355 1.00 56.08  ? 79   ALA A CA    1 
ATOM   2044  C C     . ALA D 4 82   ? 133.413 108.005 137.359 1.00 58.12  ? 79   ALA A C     1 
ATOM   2045  O O     . ALA D 4 82   ? 133.016 108.757 136.462 1.00 57.56  ? 79   ALA A O     1 
ATOM   2046  C CB    . ALA D 4 82   ? 132.269 108.333 139.567 1.00 55.90  ? 79   ALA A CB    1 
ATOM   2047  N N     . ILE D 4 83   ? 134.698 107.681 137.502 1.00 60.17  ? 80   ILE A N     1 
ATOM   2048  C CA    . ILE D 4 83   ? 135.688 108.121 136.526 1.00 60.66  ? 80   ILE A CA    1 
ATOM   2049  C C     . ILE D 4 83   ? 135.481 107.403 135.198 1.00 57.88  ? 80   ILE A C     1 
ATOM   2050  O O     . ILE D 4 83   ? 135.559 108.016 134.126 1.00 56.54  ? 80   ILE A O     1 
ATOM   2051  C CB    . ILE D 4 83   ? 137.111 107.904 137.074 1.00 64.17  ? 80   ILE A CB    1 
ATOM   2052  C CG1   . ILE D 4 83   ? 137.331 108.741 138.336 1.00 41.39  ? 80   ILE A CG1   1 
ATOM   2053  C CG2   . ILE D 4 83   ? 138.154 108.251 136.023 1.00 40.42  ? 80   ILE A CG2   1 
ATOM   2054  C CD1   . ILE D 4 83   ? 138.700 108.562 138.954 1.00 41.07  ? 80   ILE A CD1   1 
ATOM   2055  N N     . ASP D 4 84   ? 135.205 106.097 135.248 1.00 57.17  ? 81   ASP A N     1 
ATOM   2056  C CA    . ASP D 4 84   ? 134.990 105.333 134.023 1.00 57.86  ? 81   ASP A CA    1 
ATOM   2057  C C     . ASP D 4 84   ? 133.754 105.817 133.275 1.00 57.68  ? 81   ASP A C     1 
ATOM   2058  O O     . ASP D 4 84   ? 133.776 105.949 132.046 1.00 55.78  ? 81   ASP A O     1 
ATOM   2059  C CB    . ASP D 4 84   ? 134.867 103.844 134.345 1.00 62.59  ? 81   ASP A CB    1 
ATOM   2060  C CG    . ASP D 4 84   ? 136.200 103.207 134.671 1.00 67.37  ? 81   ASP A CG    1 
ATOM   2061  O OD1   . ASP D 4 84   ? 137.171 103.952 134.913 1.00 66.53  ? 81   ASP A OD1   1 
ATOM   2062  O OD2   . ASP D 4 84   ? 136.277 101.960 134.689 1.00 71.57  ? 81   ASP A OD2   1 
ATOM   2063  N N     . SER D 4 85   ? 132.665 106.086 134.001 1.00 60.14  ? 82   SER A N     1 
ATOM   2064  C CA    . SER D 4 85   ? 131.428 106.500 133.348 1.00 61.49  ? 82   SER A CA    1 
ATOM   2065  C C     . SER D 4 85   ? 131.564 107.864 132.683 1.00 60.13  ? 82   SER A C     1 
ATOM   2066  O O     . SER D 4 85   ? 130.949 108.104 131.638 1.00 60.87  ? 82   SER A O     1 
ATOM   2067  C CB    . SER D 4 85   ? 130.278 106.516 134.356 1.00 61.30  ? 82   SER A CB    1 
ATOM   2068  O OG    . SER D 4 85   ? 129.905 105.198 134.727 1.00 61.66  ? 82   SER A OG    1 
ATOM   2069  N N     . TYR D 4 86   ? 132.359 108.766 133.262 1.00 58.96  ? 83   TYR A N     1 
ATOM   2070  C CA    . TYR D 4 86   ? 132.539 110.077 132.647 1.00 59.49  ? 83   TYR A CA    1 
ATOM   2071  C C     . TYR D 4 86   ? 133.408 109.982 131.397 1.00 60.01  ? 83   TYR A C     1 
ATOM   2072  O O     . TYR D 4 86   ? 133.155 110.678 130.407 1.00 60.47  ? 83   TYR A O     1 
ATOM   2073  C CB    . TYR D 4 86   ? 133.140 111.060 133.652 1.00 59.79  ? 83   TYR A CB    1 
ATOM   2074  C CG    . TYR D 4 86   ? 133.308 112.456 133.096 1.00 59.83  ? 83   TYR A CG    1 
ATOM   2075  C CD1   . TYR D 4 86   ? 132.263 113.088 132.435 1.00 61.96  ? 83   TYR A CD1   1 
ATOM   2076  C CD2   . TYR D 4 86   ? 134.506 113.143 133.236 1.00 56.76  ? 83   TYR A CD2   1 
ATOM   2077  C CE1   . TYR D 4 86   ? 132.408 114.363 131.920 1.00 61.29  ? 83   TYR A CE1   1 
ATOM   2078  C CE2   . TYR D 4 86   ? 134.660 114.420 132.728 1.00 56.87  ? 83   TYR A CE2   1 
ATOM   2079  C CZ    . TYR D 4 86   ? 133.608 115.024 132.071 1.00 60.40  ? 83   TYR A CZ    1 
ATOM   2080  O OH    . TYR D 4 86   ? 133.753 116.295 131.563 1.00 61.83  ? 83   TYR A OH    1 
ATOM   2081  N N     . ARG D 4 87   ? 134.437 109.131 131.426 1.00 60.14  ? 84   ARG A N     1 
ATOM   2082  C CA    . ARG D 4 87   ? 135.228 108.899 130.223 1.00 60.01  ? 84   ARG A CA    1 
ATOM   2083  C C     . ARG D 4 87   ? 134.441 108.113 129.181 1.00 61.04  ? 84   ARG A C     1 
ATOM   2084  O O     . ARG D 4 87   ? 134.686 108.263 127.978 1.00 55.45  ? 84   ARG A O     1 
ATOM   2085  C CB    . ARG D 4 87   ? 136.522 108.164 130.575 1.00 59.11  ? 84   ARG A CB    1 
ATOM   2086  C CG    . ARG D 4 87   ? 137.441 108.927 131.516 1.00 59.11  ? 84   ARG A CG    1 
ATOM   2087  C CD    . ARG D 4 87   ? 138.642 108.083 131.907 1.00 59.60  ? 84   ARG A CD    1 
ATOM   2088  N NE    . ARG D 4 87   ? 139.509 108.766 132.861 1.00 59.81  ? 84   ARG A NE    1 
ATOM   2089  C CZ    . ARG D 4 87   ? 140.539 108.194 133.477 1.00 60.93  ? 84   ARG A CZ    1 
ATOM   2090  N NH1   . ARG D 4 87   ? 140.829 106.922 133.241 1.00 61.84  ? 84   ARG A NH1   1 
ATOM   2091  N NH2   . ARG D 4 87   ? 141.276 108.891 134.332 1.00 59.37  ? 84   ARG A NH2   1 
ATOM   2092  N N     . LYS D 4 88   ? 133.501 107.277 129.621 1.00 66.49  ? 85   LYS A N     1 
ATOM   2093  C CA    . LYS D 4 88   ? 132.666 106.496 128.717 1.00 73.50  ? 85   LYS A CA    1 
ATOM   2094  C C     . LYS D 4 88   ? 131.686 107.413 127.992 1.00 78.32  ? 85   LYS A C     1 
ATOM   2095  O O     . LYS D 4 88   ? 131.795 107.610 126.777 1.00 77.46  ? 85   LYS A O     1 
ATOM   2096  C CB    . LYS D 4 88   ? 131.923 105.407 129.495 1.00 74.93  ? 85   LYS A CB    1 
ATOM   2097  C CG    . LYS D 4 88   ? 131.804 104.063 128.785 1.00 73.49  ? 85   LYS A CG    1 
ATOM   2098  C CD    . LYS D 4 88   ? 130.722 104.077 127.720 1.00 74.66  ? 85   LYS A CD    1 
ATOM   2099  C CE    . LYS D 4 88   ? 130.285 102.664 127.360 1.00 77.90  ? 85   LYS A CE    1 
ATOM   2100  N NZ    . LYS D 4 88   ? 131.434 101.801 126.965 1.00 78.09  ? 85   LYS A NZ    1 
ATOM   2101  N N     . GLU D 4 89   ? 130.731 107.975 128.726 1.00 85.09  ? 86   GLU A N     1 
ATOM   2102  C CA    . GLU D 4 89   ? 129.797 108.956 128.190 1.00 87.26  ? 86   GLU A CA    1 
ATOM   2103  C C     . GLU D 4 89   ? 130.225 110.352 128.626 1.00 86.95  ? 86   GLU A C     1 
ATOM   2104  O O     . GLU D 4 89   ? 130.405 110.606 129.821 1.00 87.92  ? 86   GLU A O     1 
ATOM   2105  C CB    . GLU D 4 89   ? 128.367 108.677 128.658 1.00 89.93  ? 86   GLU A CB    1 
ATOM   2106  C CG    . GLU D 4 89   ? 127.560 107.766 127.738 1.00 94.70  ? 86   GLU A CG    1 
ATOM   2107  C CD    . GLU D 4 89   ? 127.583 106.311 128.172 1.00 98.50  ? 86   GLU A CD    1 
ATOM   2108  O OE1   . GLU D 4 89   ? 128.328 105.981 129.118 1.00 99.08  ? 86   GLU A OE1   1 
ATOM   2109  O OE2   . GLU D 4 89   ? 126.848 105.500 127.568 1.00 100.51 ? 86   GLU A OE2   1 
ATOM   2110  N N     . LYS D 4 90   ? 130.386 111.250 127.658 1.00 85.57  ? 87   LYS A N     1 
ATOM   2111  C CA    . LYS D 4 90   ? 130.795 112.627 127.934 1.00 82.07  ? 87   LYS A CA    1 
ATOM   2112  C C     . LYS D 4 90   ? 129.587 113.542 128.123 1.00 81.28  ? 87   LYS A C     1 
ATOM   2113  O O     . LYS D 4 90   ? 129.493 114.613 127.526 1.00 82.27  ? 87   LYS A O     1 
ATOM   2114  C CB    . LYS D 4 90   ? 131.697 113.141 126.816 1.00 79.64  ? 87   LYS A CB    1 
ATOM   2115  C CG    . LYS D 4 90   ? 133.009 112.384 126.647 1.00 77.99  ? 87   LYS A CG    1 
ATOM   2116  C CD    . LYS D 4 90   ? 132.884 111.250 125.639 1.00 80.07  ? 87   LYS A CD    1 
ATOM   2117  C CE    . LYS D 4 90   ? 134.243 110.657 125.298 1.00 81.40  ? 87   LYS A CE    1 
ATOM   2118  N NZ    . LYS D 4 90   ? 134.946 110.141 126.505 1.00 82.33  ? 87   LYS A NZ    1 
ATOM   2119  N N     . THR D 4 91   ? 128.650 113.120 128.963 1.00 82.09  ? 88   THR A N     1 
ATOM   2120  C CA    . THR D 4 91   ? 127.440 113.882 129.229 1.00 83.14  ? 88   THR A CA    1 
ATOM   2121  C C     . THR D 4 91   ? 127.567 114.642 130.543 1.00 82.62  ? 88   THR A C     1 
ATOM   2122  O O     . THR D 4 91   ? 128.330 114.266 131.438 1.00 83.80  ? 88   THR A O     1 
ATOM   2123  C CB    . THR D 4 91   ? 126.211 112.967 129.265 1.00 87.46  ? 88   THR A CB    1 
ATOM   2124  O OG1   . THR D 4 91   ? 125.064 113.719 129.681 1.00 91.55  ? 88   THR A OG1   1 
ATOM   2125  C CG2   . THR D 4 91   ? 126.430 111.808 130.226 1.00 87.64  ? 88   THR A CG2   1 
ATOM   2126  N N     . GLU D 4 92   ? 126.803 115.734 130.646 1.00 81.31  ? 89   GLU A N     1 
ATOM   2127  C CA    . GLU D 4 92   ? 126.832 116.568 131.842 1.00 79.08  ? 89   GLU A CA    1 
ATOM   2128  C C     . GLU D 4 92   ? 126.298 115.843 133.071 1.00 78.11  ? 89   GLU A C     1 
ATOM   2129  O O     . GLU D 4 92   ? 126.585 116.264 134.197 1.00 77.47  ? 89   GLU A O     1 
ATOM   2130  C CB    . GLU D 4 92   ? 126.036 117.853 131.606 1.00 78.95  ? 89   GLU A CB    1 
ATOM   2131  N N     . GLU D 4 93   ? 125.526 114.771 132.883 1.00 76.90  ? 90   GLU A N     1 
ATOM   2132  C CA    . GLU D 4 93   ? 125.040 114.008 134.027 1.00 75.54  ? 90   GLU A CA    1 
ATOM   2133  C C     . GLU D 4 93   ? 126.166 113.208 134.670 1.00 73.52  ? 90   GLU A C     1 
ATOM   2134  O O     . GLU D 4 93   ? 126.252 113.127 135.901 1.00 71.81  ? 90   GLU A O     1 
ATOM   2135  C CB    . GLU D 4 93   ? 123.895 113.090 133.598 1.00 75.97  ? 90   GLU A CB    1 
ATOM   2136  C CG    . GLU D 4 93   ? 123.260 112.294 134.734 1.00 77.60  ? 90   GLU A CG    1 
ATOM   2137  C CD    . GLU D 4 93   ? 123.984 110.991 135.016 1.00 80.21  ? 90   GLU A CD    1 
ATOM   2138  O OE1   . GLU D 4 93   ? 124.508 110.380 134.060 1.00 79.93  ? 90   GLU A OE1   1 
ATOM   2139  O OE2   . GLU D 4 93   ? 124.038 110.584 136.195 1.00 82.82  ? 90   GLU A OE2   1 
ATOM   2140  N N     . THR D 4 94   ? 127.040 112.613 133.855 1.00 73.51  ? 91   THR A N     1 
ATOM   2141  C CA    . THR D 4 94   ? 128.161 111.858 134.404 1.00 73.44  ? 91   THR A CA    1 
ATOM   2142  C C     . THR D 4 94   ? 129.227 112.779 134.984 1.00 71.42  ? 91   THR A C     1 
ATOM   2143  O O     . THR D 4 94   ? 129.984 112.363 135.869 1.00 71.30  ? 91   THR A O     1 
ATOM   2144  C CB    . THR D 4 94   ? 128.767 110.953 133.332 1.00 75.50  ? 91   THR A CB    1 
ATOM   2145  O OG1   . THR D 4 94   ? 129.060 111.726 132.161 1.00 76.80  ? 91   THR A OG1   1 
ATOM   2146  C CG2   . THR D 4 94   ? 127.800 109.835 132.972 1.00 77.65  ? 91   THR A CG2   1 
ATOM   2147  N N     . ARG D 4 95   ? 129.304 114.021 134.504 1.00 72.07  ? 92   ARG A N     1 
ATOM   2148  C CA    . ARG D 4 95   ? 130.242 114.976 135.085 1.00 71.33  ? 92   ARG A CA    1 
ATOM   2149  C C     . ARG D 4 95   ? 129.809 115.373 136.490 1.00 69.67  ? 92   ARG A C     1 
ATOM   2150  O O     . ARG D 4 95   ? 130.611 115.341 137.430 1.00 70.46  ? 92   ARG A O     1 
ATOM   2151  C CB    . ARG D 4 95   ? 130.366 116.210 134.192 1.00 77.35  ? 92   ARG A CB    1 
ATOM   2152  C CG    . ARG D 4 95   ? 131.675 116.969 134.371 1.00 83.35  ? 92   ARG A CG    1 
ATOM   2153  C CD    . ARG D 4 95   ? 131.473 118.479 134.398 1.00 89.54  ? 92   ARG A CD    1 
ATOM   2154  N NE    . ARG D 4 95   ? 130.602 118.953 133.326 1.00 95.56  ? 92   ARG A NE    1 
ATOM   2155  C CZ    . ARG D 4 95   ? 129.374 119.423 133.517 1.00 100.09 ? 92   ARG A CZ    1 
ATOM   2156  N NH1   . ARG D 4 95   ? 128.871 119.494 134.743 1.00 102.26 ? 92   ARG A NH1   1 
ATOM   2157  N NH2   . ARG D 4 95   ? 128.649 119.831 132.483 1.00 100.52 ? 92   ARG A NH2   1 
ATOM   2158  N N     . ASN D 4 96   ? 128.536 115.748 136.651 1.00 67.36  ? 93   ASN A N     1 
ATOM   2159  C CA    . ASN D 4 96   ? 128.029 116.112 137.969 1.00 65.01  ? 93   ASN A CA    1 
ATOM   2160  C C     . ASN D 4 96   ? 128.058 114.928 138.925 1.00 60.28  ? 93   ASN A C     1 
ATOM   2161  O O     . ASN D 4 96   ? 128.221 115.112 140.137 1.00 58.84  ? 93   ASN A O     1 
ATOM   2162  C CB    . ASN D 4 96   ? 126.609 116.666 137.854 1.00 68.48  ? 93   ASN A CB    1 
ATOM   2163  C CG    . ASN D 4 96   ? 126.555 117.972 137.087 1.00 72.30  ? 93   ASN A CG    1 
ATOM   2164  O OD1   . ASN D 4 96   ? 127.537 118.385 136.470 1.00 72.69  ? 93   ASN A OD1   1 
ATOM   2165  N ND2   . ASN D 4 96   ? 125.401 118.628 137.120 1.00 75.13  ? 93   ASN A ND2   1 
ATOM   2166  N N     . ALA D 4 97   ? 127.894 113.710 138.405 1.00 58.13  ? 94   ALA A N     1 
ATOM   2167  C CA    . ALA D 4 97   ? 128.004 112.531 139.254 1.00 56.83  ? 94   ALA A CA    1 
ATOM   2168  C C     . ALA D 4 97   ? 129.428 112.352 139.761 1.00 56.60  ? 94   ALA A C     1 
ATOM   2169  O O     . ALA D 4 97   ? 129.639 111.970 140.918 1.00 57.66  ? 94   ALA A O     1 
ATOM   2170  C CB    . ALA D 4 97   ? 127.542 111.290 138.489 1.00 55.85  ? 94   ALA A CB    1 
ATOM   2171  N N     . LEU D 4 98   ? 130.420 112.632 138.913 1.00 55.31  ? 95   LEU A N     1 
ATOM   2172  C CA    . LEU D 4 98   ? 131.811 112.533 139.345 1.00 55.64  ? 95   LEU A CA    1 
ATOM   2173  C C     . LEU D 4 98   ? 132.169 113.654 140.313 1.00 56.49  ? 95   LEU A C     1 
ATOM   2174  O O     . LEU D 4 98   ? 132.911 113.433 141.276 1.00 57.90  ? 95   LEU A O     1 
ATOM   2175  C CB    . LEU D 4 98   ? 132.738 112.551 138.130 1.00 55.45  ? 95   LEU A CB    1 
ATOM   2176  C CG    . LEU D 4 98   ? 134.239 112.510 138.420 1.00 40.33  ? 95   LEU A CG    1 
ATOM   2177  C CD1   . LEU D 4 98   ? 134.593 111.306 139.276 1.00 43.74  ? 95   LEU A CD1   1 
ATOM   2178  C CD2   . LEU D 4 98   ? 135.033 112.499 137.124 1.00 39.45  ? 95   LEU A CD2   1 
ATOM   2179  N N     . ILE D 4 99   ? 131.650 114.861 140.075 1.00 55.24  ? 96   ILE A N     1 
ATOM   2180  C CA    . ILE D 4 99   ? 131.939 115.988 140.960 1.00 54.80  ? 96   ILE A CA    1 
ATOM   2181  C C     . ILE D 4 99   ? 131.395 115.722 142.357 1.00 57.37  ? 96   ILE A C     1 
ATOM   2182  O O     . ILE D 4 99   ? 132.051 116.020 143.362 1.00 57.51  ? 96   ILE A O     1 
ATOM   2183  C CB    . ILE D 4 99   ? 131.372 117.291 140.365 1.00 52.47  ? 96   ILE A CB    1 
ATOM   2184  C CG1   . ILE D 4 99   ? 132.110 117.651 139.074 1.00 48.58  ? 96   ILE A CG1   1 
ATOM   2185  C CG2   . ILE D 4 99   ? 131.468 118.428 141.371 1.00 52.51  ? 96   ILE A CG2   1 
ATOM   2186  C CD1   . ILE D 4 99   ? 131.589 118.902 138.401 1.00 46.40  ? 96   ILE A CD1   1 
ATOM   2187  N N     . GLU D 4 100  ? 130.191 115.153 142.446 1.00 61.07  ? 97   GLU A N     1 
ATOM   2188  C CA    . GLU D 4 100  ? 129.642 114.802 143.751 1.00 63.16  ? 97   GLU A CA    1 
ATOM   2189  C C     . GLU D 4 100  ? 130.406 113.642 144.378 1.00 61.32  ? 97   GLU A C     1 
ATOM   2190  O O     . GLU D 4 100  ? 130.640 113.630 145.592 1.00 61.31  ? 97   GLU A O     1 
ATOM   2191  C CB    . GLU D 4 100  ? 128.158 114.461 143.631 1.00 70.39  ? 97   GLU A CB    1 
ATOM   2192  C CG    . GLU D 4 100  ? 127.271 115.642 143.280 1.00 76.09  ? 97   GLU A CG    1 
ATOM   2193  C CD    . GLU D 4 100  ? 125.799 115.320 143.429 1.00 82.26  ? 97   GLU A CD    1 
ATOM   2194  O OE1   . GLU D 4 100  ? 125.479 114.213 143.910 1.00 84.96  ? 97   GLU A OE1   1 
ATOM   2195  O OE2   . GLU D 4 100  ? 124.962 116.173 143.065 1.00 83.79  ? 97   GLU A OE2   1 
ATOM   2196  N N     . GLU D 4 101  ? 130.798 112.657 143.566 1.00 60.35  ? 98   GLU A N     1 
ATOM   2197  C CA    . GLU D 4 101  ? 131.542 111.518 144.097 1.00 62.79  ? 98   GLU A CA    1 
ATOM   2198  C C     . GLU D 4 101  ? 132.894 111.953 144.644 1.00 60.33  ? 98   GLU A C     1 
ATOM   2199  O O     . GLU D 4 101  ? 133.350 111.442 145.674 1.00 59.75  ? 98   GLU A O     1 
ATOM   2200  C CB    . GLU D 4 101  ? 131.717 110.453 143.015 1.00 66.23  ? 98   GLU A CB    1 
ATOM   2201  C CG    . GLU D 4 101  ? 132.149 109.099 143.553 1.00 69.85  ? 98   GLU A CG    1 
ATOM   2202  C CD    . GLU D 4 101  ? 131.058 108.427 144.362 1.00 75.65  ? 98   GLU A CD    1 
ATOM   2203  O OE1   . GLU D 4 101  ? 129.877 108.543 143.974 1.00 78.48  ? 98   GLU A OE1   1 
ATOM   2204  O OE2   . GLU D 4 101  ? 131.377 107.788 145.386 1.00 78.09  ? 98   GLU A OE2   1 
ATOM   2205  N N     . GLN D 4 102  ? 133.552 112.898 143.966 1.00 57.89  ? 99   GLN A N     1 
ATOM   2206  C CA    . GLN D 4 102  ? 134.816 113.422 144.470 1.00 53.92  ? 99   GLN A CA    1 
ATOM   2207  C C     . GLN D 4 102  ? 134.614 114.191 145.771 1.00 53.36  ? 99   GLN A C     1 
ATOM   2208  O O     . GLN D 4 102  ? 135.409 114.055 146.708 1.00 53.06  ? 99   GLN A O     1 
ATOM   2209  C CB    . GLN D 4 102  ? 135.473 114.312 143.417 1.00 50.83  ? 99   GLN A CB    1 
ATOM   2210  C CG    . GLN D 4 102  ? 135.928 113.570 142.172 1.00 48.83  ? 99   GLN A CG    1 
ATOM   2211  C CD    . GLN D 4 102  ? 136.265 114.506 141.031 1.00 44.98  ? 99   GLN A CD    1 
ATOM   2212  O OE1   . GLN D 4 102  ? 135.996 115.706 141.098 1.00 46.87  ? 99   GLN A OE1   1 
ATOM   2213  N NE2   . GLN D 4 102  ? 136.854 113.964 139.972 1.00 42.28  ? 99   GLN A NE2   1 
ATOM   2214  N N     . ALA D 4 103  ? 133.553 114.999 145.846 1.00 53.05  ? 100  ALA A N     1 
ATOM   2215  C CA    . ALA D 4 103  ? 133.275 115.743 147.071 1.00 54.63  ? 100  ALA A CA    1 
ATOM   2216  C C     . ALA D 4 103  ? 132.979 114.811 148.238 1.00 57.18  ? 100  ALA A C     1 
ATOM   2217  O O     . ALA D 4 103  ? 133.317 115.128 149.384 1.00 58.73  ? 100  ALA A O     1 
ATOM   2218  C CB    . ALA D 4 103  ? 132.107 116.704 146.850 1.00 53.32  ? 100  ALA A CB    1 
ATOM   2219  N N     . THR D 4 104  ? 132.354 113.664 147.970 1.00 57.84  ? 101  THR A N     1 
ATOM   2220  C CA    . THR D 4 104  ? 132.099 112.696 149.031 1.00 60.57  ? 101  THR A CA    1 
ATOM   2221  C C     . THR D 4 104  ? 133.401 112.101 149.555 1.00 62.07  ? 101  THR A C     1 
ATOM   2222  O O     . THR D 4 104  ? 133.582 111.960 150.771 1.00 63.41  ? 101  THR A O     1 
ATOM   2223  C CB    . THR D 4 104  ? 131.168 111.591 148.525 1.00 61.73  ? 101  THR A CB    1 
ATOM   2224  O OG1   . THR D 4 104  ? 129.914 112.163 148.133 1.00 62.40  ? 101  THR A OG1   1 
ATOM   2225  C CG2   . THR D 4 104  ? 130.927 110.551 149.610 1.00 62.46  ? 101  THR A CG2   1 
ATOM   2226  N N     . TYR D 4 105  ? 134.323 111.756 148.654 1.00 61.96  ? 102  TYR A N     1 
ATOM   2227  C CA    . TYR D 4 105  ? 135.598 111.189 149.084 1.00 63.27  ? 102  TYR A CA    1 
ATOM   2228  C C     . TYR D 4 105  ? 136.461 112.227 149.791 1.00 62.70  ? 102  TYR A C     1 
ATOM   2229  O O     . TYR D 4 105  ? 137.171 111.900 150.748 1.00 63.79  ? 102  TYR A O     1 
ATOM   2230  C CB    . TYR D 4 105  ? 136.341 110.594 147.887 1.00 63.32  ? 102  TYR A CB    1 
ATOM   2231  C CG    . TYR D 4 105  ? 135.969 109.160 147.589 1.00 64.22  ? 102  TYR A CG    1 
ATOM   2232  C CD1   . TYR D 4 105  ? 134.902 108.855 146.755 1.00 64.37  ? 102  TYR A CD1   1 
ATOM   2233  C CD2   . TYR D 4 105  ? 136.687 108.109 148.144 1.00 64.75  ? 102  TYR A CD2   1 
ATOM   2234  C CE1   . TYR D 4 105  ? 134.560 107.544 146.481 1.00 65.84  ? 102  TYR A CE1   1 
ATOM   2235  C CE2   . TYR D 4 105  ? 136.353 106.794 147.875 1.00 66.56  ? 102  TYR A CE2   1 
ATOM   2236  C CZ    . TYR D 4 105  ? 135.290 106.518 147.043 1.00 66.41  ? 102  TYR A CZ    1 
ATOM   2237  O OH    . TYR D 4 105  ? 134.953 105.211 146.773 1.00 66.14  ? 102  TYR A OH    1 
ATOM   2238  N N     . ARG D 4 106  ? 136.417 113.483 149.334 1.00 60.46  ? 103  ARG A N     1 
ATOM   2239  C CA    . ARG D 4 106  ? 137.182 114.531 150.003 1.00 59.30  ? 103  ARG A CA    1 
ATOM   2240  C C     . ARG D 4 106  ? 136.706 114.728 151.437 1.00 61.36  ? 103  ARG A C     1 
ATOM   2241  O O     . ARG D 4 106  ? 137.518 114.948 152.344 1.00 62.56  ? 103  ARG A O     1 
ATOM   2242  C CB    . ARG D 4 106  ? 137.090 115.844 149.222 1.00 56.63  ? 103  ARG A CB    1 
ATOM   2243  C CG    . ARG D 4 106  ? 137.771 115.820 147.862 1.00 51.75  ? 103  ARG A CG    1 
ATOM   2244  C CD    . ARG D 4 106  ? 137.944 117.225 147.305 1.00 47.67  ? 103  ARG A CD    1 
ATOM   2245  N NE    . ARG D 4 106  ? 136.693 117.979 147.295 1.00 49.19  ? 103  ARG A NE    1 
ATOM   2246  C CZ    . ARG D 4 106  ? 135.871 118.053 146.254 1.00 50.08  ? 103  ARG A CZ    1 
ATOM   2247  N NH1   . ARG D 4 106  ? 136.165 117.421 145.125 1.00 50.40  ? 103  ARG A NH1   1 
ATOM   2248  N NH2   . ARG D 4 106  ? 134.755 118.764 146.337 1.00 49.39  ? 103  ARG A NH2   1 
ATOM   2249  N N     . ASN D 4 107  ? 135.393 114.647 151.661 1.00 61.62  ? 104  ASN A N     1 
ATOM   2250  C CA    . ASN D 4 107  ? 134.870 114.753 153.021 1.00 63.17  ? 104  ASN A CA    1 
ATOM   2251  C C     . ASN D 4 107  ? 135.236 113.535 153.857 1.00 65.54  ? 104  ASN A C     1 
ATOM   2252  O O     . ASN D 4 107  ? 135.441 113.660 155.071 1.00 68.30  ? 104  ASN A O     1 
ATOM   2253  C CB    . ASN D 4 107  ? 133.352 114.941 152.991 1.00 65.58  ? 104  ASN A CB    1 
ATOM   2254  C CG    . ASN D 4 107  ? 132.943 116.292 152.438 1.00 68.26  ? 104  ASN A CG    1 
ATOM   2255  O OD1   . ASN D 4 107  ? 133.595 117.305 152.692 1.00 70.18  ? 104  ASN A OD1   1 
ATOM   2256  N ND2   . ASN D 4 107  ? 131.854 116.314 151.675 1.00 68.13  ? 104  ASN A ND2   1 
ATOM   2257  N N     . ALA D 4 108  ? 135.323 112.356 153.235 1.00 67.05  ? 105  ALA A N     1 
ATOM   2258  C CA    . ALA D 4 108  ? 135.730 111.161 153.967 1.00 70.46  ? 105  ALA A CA    1 
ATOM   2259  C C     . ALA D 4 108  ? 137.147 111.303 154.504 1.00 71.65  ? 105  ALA A C     1 
ATOM   2260  O O     . ALA D 4 108  ? 137.444 110.859 155.621 1.00 74.61  ? 105  ALA A O     1 
ATOM   2261  C CB    . ALA D 4 108  ? 135.615 109.929 153.070 1.00 70.09  ? 105  ALA A CB    1 
ATOM   2262  N N     . ILE D 4 109  ? 138.039 111.917 153.723 1.00 68.34  ? 106  ILE A N     1 
ATOM   2263  C CA    . ILE D 4 109  ? 139.378 112.217 154.219 1.00 66.72  ? 106  ILE A CA    1 
ATOM   2264  C C     . ILE D 4 109  ? 139.322 113.337 155.250 1.00 70.90  ? 106  ILE A C     1 
ATOM   2265  O O     . ILE D 4 109  ? 140.041 113.312 156.256 1.00 72.92  ? 106  ILE A O     1 
ATOM   2266  C CB    . ILE D 4 109  ? 140.310 112.577 153.047 1.00 60.73  ? 106  ILE A CB    1 
ATOM   2267  C CG1   . ILE D 4 109  ? 140.198 111.540 151.927 1.00 59.82  ? 106  ILE A CG1   1 
ATOM   2268  C CG2   . ILE D 4 109  ? 141.750 112.696 153.528 1.00 58.67  ? 106  ILE A CG2   1 
ATOM   2269  C CD1   . ILE D 4 109  ? 140.671 110.162 152.316 1.00 61.82  ? 106  ILE A CD1   1 
ATOM   2270  N N     . HIS D 4 110  ? 138.461 114.333 155.018 1.00 71.32  ? 107  HIS A N     1 
ATOM   2271  C CA    . HIS D 4 110  ? 138.355 115.464 155.933 1.00 72.60  ? 107  HIS A CA    1 
ATOM   2272  C C     . HIS D 4 110  ? 137.852 115.036 157.304 1.00 76.50  ? 107  HIS A C     1 
ATOM   2273  O O     . HIS D 4 110  ? 138.241 115.625 158.319 1.00 78.56  ? 107  HIS A O     1 
ATOM   2274  C CB    . HIS D 4 110  ? 137.428 116.524 155.334 1.00 70.77  ? 107  HIS A CB    1 
ATOM   2275  C CG    . HIS D 4 110  ? 137.402 117.813 156.097 1.00 71.02  ? 107  HIS A CG    1 
ATOM   2276  N ND1   . HIS D 4 110  ? 138.459 118.697 156.102 1.00 71.06  ? 107  HIS A ND1   1 
ATOM   2277  C CD2   . HIS D 4 110  ? 136.441 118.371 156.870 1.00 71.82  ? 107  HIS A CD2   1 
ATOM   2278  C CE1   . HIS D 4 110  ? 138.152 119.743 156.849 1.00 71.62  ? 107  HIS A CE1   1 
ATOM   2279  N NE2   . HIS D 4 110  ? 136.932 119.570 157.326 1.00 72.27  ? 107  HIS A NE2   1 
ATOM   2280  N N     . ASP D 4 111  ? 136.991 114.017 157.357 1.00 78.28  ? 108  ASP A N     1 
ATOM   2281  C CA    . ASP D 4 111  ? 136.473 113.548 158.637 1.00 80.94  ? 108  ASP A CA    1 
ATOM   2282  C C     . ASP D 4 111  ? 137.553 112.900 159.495 1.00 84.57  ? 108  ASP A C     1 
ATOM   2283  O O     . ASP D 4 111  ? 137.387 112.821 160.716 1.00 86.53  ? 108  ASP A O     1 
ATOM   2284  C CB    . ASP D 4 111  ? 135.318 112.569 158.411 1.00 81.41  ? 108  ASP A CB    1 
ATOM   2285  C CG    . ASP D 4 111  ? 134.098 113.238 157.799 1.00 80.91  ? 108  ASP A CG    1 
ATOM   2286  O OD1   . ASP D 4 111  ? 133.958 114.472 157.940 1.00 80.12  ? 108  ASP A OD1   1 
ATOM   2287  O OD2   . ASP D 4 111  ? 133.276 112.528 157.182 1.00 81.63  ? 108  ASP A OD2   1 
ATOM   2288  N N     . TYR D 4 112  ? 138.649 112.434 158.890 1.00 84.67  ? 109  TYR A N     1 
ATOM   2289  C CA    . TYR D 4 112  ? 139.785 111.978 159.683 1.00 84.08  ? 109  TYR A CA    1 
ATOM   2290  C C     . TYR D 4 112  ? 140.486 113.142 160.372 1.00 81.45  ? 109  TYR A C     1 
ATOM   2291  O O     . TYR D 4 112  ? 140.998 112.986 161.486 1.00 82.19  ? 109  TYR A O     1 
ATOM   2292  C CB    . TYR D 4 112  ? 140.772 111.210 158.802 1.00 82.25  ? 109  TYR A CB    1 
ATOM   2293  C CG    . TYR D 4 112  ? 140.435 109.746 158.624 1.00 83.64  ? 109  TYR A CG    1 
ATOM   2294  C CD1   . TYR D 4 112  ? 139.465 109.339 157.718 1.00 83.07  ? 109  TYR A CD1   1 
ATOM   2295  C CD2   . TYR D 4 112  ? 141.093 108.769 159.359 1.00 86.48  ? 109  TYR A CD2   1 
ATOM   2296  C CE1   . TYR D 4 112  ? 139.156 108.000 157.553 1.00 84.08  ? 109  TYR A CE1   1 
ATOM   2297  C CE2   . TYR D 4 112  ? 140.793 107.429 159.201 1.00 87.75  ? 109  TYR A CE2   1 
ATOM   2298  C CZ    . TYR D 4 112  ? 139.823 107.050 158.297 1.00 86.17  ? 109  TYR A CZ    1 
ATOM   2299  O OH    . TYR D 4 112  ? 139.522 105.716 158.137 1.00 86.77  ? 109  TYR A OH    1 
ATOM   2300  N N     . PHE D 4 113  ? 140.516 114.310 159.727 1.00 78.56  ? 110  PHE A N     1 
ATOM   2301  C CA    . PHE D 4 113  ? 141.143 115.482 160.330 1.00 74.76  ? 110  PHE A CA    1 
ATOM   2302  C C     . PHE D 4 113  ? 140.291 116.041 161.462 1.00 74.35  ? 110  PHE A C     1 
ATOM   2303  O O     . PHE D 4 113  ? 140.778 116.232 162.584 1.00 73.98  ? 110  PHE A O     1 
ATOM   2304  C CB    . PHE D 4 113  ? 141.382 116.554 159.265 1.00 72.17  ? 110  PHE A CB    1 
ATOM   2305  C CG    . PHE D 4 113  ? 142.400 116.169 158.230 1.00 70.91  ? 110  PHE A CG    1 
ATOM   2306  C CD1   . PHE D 4 113  ? 143.560 115.507 158.592 1.00 72.33  ? 110  PHE A CD1   1 
ATOM   2307  C CD2   . PHE D 4 113  ? 142.195 116.471 156.893 1.00 69.41  ? 110  PHE A CD2   1 
ATOM   2308  C CE1   . PHE D 4 113  ? 144.499 115.153 157.641 1.00 70.99  ? 110  PHE A CE1   1 
ATOM   2309  C CE2   . PHE D 4 113  ? 143.129 116.120 155.937 1.00 68.24  ? 110  PHE A CE2   1 
ATOM   2310  C CZ    . PHE D 4 113  ? 144.283 115.460 156.312 1.00 69.17  ? 110  PHE A CZ    1 
ATOM   2311  N N     . ILE D 4 114  ? 139.013 116.310 161.186 1.00 74.31  ? 111  ILE A N     1 
ATOM   2312  C CA    . ILE D 4 114  ? 138.144 116.944 162.173 1.00 74.06  ? 111  ILE A CA    1 
ATOM   2313  C C     . ILE D 4 114  ? 137.562 115.949 163.167 1.00 75.11  ? 111  ILE A C     1 
ATOM   2314  O O     . ILE D 4 114  ? 137.073 116.359 164.227 1.00 75.36  ? 111  ILE A O     1 
ATOM   2315  C CB    . ILE D 4 114  ? 137.003 117.710 161.484 1.00 69.34  ? 111  ILE A CB    1 
ATOM   2316  C CG1   . ILE D 4 114  ? 136.069 116.742 160.754 1.00 67.28  ? 111  ILE A CG1   1 
ATOM   2317  C CG2   . ILE D 4 114  ? 137.562 118.739 160.516 1.00 65.32  ? 111  ILE A CG2   1 
ATOM   2318  C CD1   . ILE D 4 114  ? 134.882 117.416 160.096 1.00 64.89  ? 111  ILE A CD1   1 
ATOM   2319  N N     . GLY D 4 115  ? 137.590 114.655 162.856 1.00 76.02  ? 112  GLY A N     1 
ATOM   2320  C CA    . GLY D 4 115  ? 137.059 113.655 163.761 1.00 78.49  ? 112  GLY A CA    1 
ATOM   2321  C C     . GLY D 4 115  ? 135.557 113.484 163.666 1.00 81.82  ? 112  GLY A C     1 
ATOM   2322  O O     . GLY D 4 115  ? 134.841 113.704 164.647 1.00 84.29  ? 112  GLY A O     1 
ATOM   2323  N N     . ARG D 4 116  ? 135.067 113.084 162.493 1.00 84.28  ? 113  ARG A N     1 
ATOM   2324  C CA    . ARG D 4 116  ? 133.652 112.781 162.288 1.00 87.18  ? 113  ARG A CA    1 
ATOM   2325  C C     . ARG D 4 116  ? 133.493 111.623 161.313 1.00 88.25  ? 113  ARG A C     1 
ATOM   2326  O O     . ARG D 4 116  ? 132.569 111.601 160.492 1.00 87.26  ? 113  ARG A O     1 
ATOM   2327  C CB    . ARG D 4 116  ? 132.881 114.004 161.790 1.00 86.81  ? 113  ARG A CB    1 
ATOM   2328  C CG    . ARG D 4 116  ? 132.478 114.991 162.873 1.00 89.08  ? 113  ARG A CG    1 
ATOM   2329  C CD    . ARG D 4 116  ? 131.318 115.860 162.410 1.00 90.55  ? 113  ARG A CD    1 
ATOM   2330  N NE    . ARG D 4 116  ? 131.027 116.943 163.344 1.00 94.37  ? 113  ARG A NE    1 
ATOM   2331  C CZ    . ARG D 4 116  ? 130.239 116.827 164.407 1.00 99.89  ? 113  ARG A CZ    1 
ATOM   2332  N NH1   . ARG D 4 116  ? 129.657 115.667 164.683 1.00 102.79 ? 113  ARG A NH1   1 
ATOM   2333  N NH2   . ARG D 4 116  ? 130.034 117.871 165.199 1.00 100.99 ? 113  ARG A NH2   1 
ATOM   2334  N N     . THR D 4 117  ? 134.393 110.648 161.388 1.00 90.66  ? 114  THR A N     1 
ATOM   2335  C CA    . THR D 4 117  ? 134.338 109.460 160.548 1.00 93.05  ? 114  THR A CA    1 
ATOM   2336  C C     . THR D 4 117  ? 133.897 108.263 161.380 1.00 97.06  ? 114  THR A C     1 
ATOM   2337  O O     . THR D 4 117  ? 134.317 108.104 162.531 1.00 97.34  ? 114  THR A O     1 
ATOM   2338  C CB    . THR D 4 117  ? 135.695 109.179 159.893 1.00 93.92  ? 114  THR A CB    1 
ATOM   2339  O OG1   . THR D 4 117  ? 135.652 107.916 159.214 1.00 95.05  ? 114  THR A OG1   1 
ATOM   2340  C CG2   . THR D 4 117  ? 136.809 109.159 160.932 1.00 95.80  ? 114  THR A CG2   1 
ATOM   2341  N N     . ASP D 4 118  ? 133.042 107.425 160.793 1.00 100.12 ? 115  ASP A N     1 
ATOM   2342  C CA    . ASP D 4 118  ? 132.537 106.250 161.491 1.00 104.58 ? 115  ASP A CA    1 
ATOM   2343  C C     . ASP D 4 118  ? 133.573 105.138 161.606 1.00 105.97 ? 115  ASP A C     1 
ATOM   2344  O O     . ASP D 4 118  ? 133.300 104.129 162.264 1.00 107.71 ? 115  ASP A O     1 
ATOM   2345  C CB    . ASP D 4 118  ? 131.288 105.715 160.787 1.00 104.27 ? 115  ASP A CB    1 
ATOM   2346  C CG    . ASP D 4 118  ? 130.154 106.721 160.763 1.00 103.27 ? 115  ASP A CG    1 
ATOM   2347  O OD1   . ASP D 4 118  ? 130.073 107.552 161.692 1.00 103.23 ? 115  ASP A OD1   1 
ATOM   2348  O OD2   . ASP D 4 118  ? 129.340 106.680 159.815 1.00 102.66 ? 115  ASP A OD2   1 
ATOM   2349  N N     . ASN D 4 119  ? 134.745 105.297 160.991 1.00 106.41 ? 116  ASN A N     1 
ATOM   2350  C CA    . ASN D 4 119  ? 135.759 104.251 161.008 1.00 110.52 ? 116  ASN A CA    1 
ATOM   2351  C C     . ASN D 4 119  ? 136.579 104.239 162.292 1.00 114.11 ? 116  ASN A C     1 
ATOM   2352  O O     . ASN D 4 119  ? 137.219 103.225 162.589 1.00 116.13 ? 116  ASN A O     1 
ATOM   2353  C CB    . ASN D 4 119  ? 136.693 104.406 159.806 1.00 110.84 ? 116  ASN A CB    1 
ATOM   2354  C CG    . ASN D 4 119  ? 135.943 104.464 158.488 1.00 111.20 ? 116  ASN A CG    1 
ATOM   2355  O OD1   . ASN D 4 119  ? 134.879 103.862 158.340 1.00 113.05 ? 116  ASN A OD1   1 
ATOM   2356  N ND2   . ASN D 4 119  ? 136.495 105.191 157.523 1.00 108.73 ? 116  ASN A ND2   1 
ATOM   2357  N N     . LEU D 4 120  ? 136.577 105.330 163.051 1.00 114.46 ? 117  LEU A N     1 
ATOM   2358  C CA    . LEU D 4 120  ? 137.358 105.439 164.274 1.00 115.36 ? 117  LEU A CA    1 
ATOM   2359  C C     . LEU D 4 120  ? 136.441 105.554 165.486 1.00 117.05 ? 117  LEU A C     1 
ATOM   2360  O O     . LEU D 4 120  ? 135.330 106.084 165.399 1.00 114.30 ? 117  LEU A O     1 
ATOM   2361  C CB    . LEU D 4 120  ? 138.301 106.644 164.218 1.00 113.00 ? 117  LEU A CB    1 
ATOM   2362  C CG    . LEU D 4 120  ? 139.402 106.573 163.160 1.00 110.16 ? 117  LEU A CG    1 
ATOM   2363  C CD1   . LEU D 4 120  ? 140.295 107.800 163.229 1.00 108.32 ? 117  LEU A CD1   1 
ATOM   2364  C CD2   . LEU D 4 120  ? 140.217 105.300 163.326 1.00 111.92 ? 117  LEU A CD2   1 
ATOM   2365  N N     . THR D 4 121  ? 136.924 105.052 166.620 1.00 120.81 ? 118  THR A N     1 
ATOM   2366  C CA    . THR D 4 121  ? 136.146 105.057 167.849 1.00 122.13 ? 118  THR A CA    1 
ATOM   2367  C C     . THR D 4 121  ? 136.091 106.459 168.452 1.00 120.17 ? 118  THR A C     1 
ATOM   2368  O O     . THR D 4 121  ? 136.885 107.342 168.119 1.00 119.17 ? 118  THR A O     1 
ATOM   2369  C CB    . THR D 4 121  ? 136.733 104.077 168.863 1.00 123.23 ? 118  THR A CB    1 
ATOM   2370  O OG1   . THR D 4 121  ? 138.146 104.300 168.984 1.00 121.30 ? 118  THR A OG1   1 
ATOM   2371  C CG2   . THR D 4 121  ? 136.482 102.641 168.425 1.00 123.88 ? 118  THR A CG2   1 
ATOM   2372  N N     . ASP D 4 122  ? 135.142 106.643 169.377 1.00 120.85 ? 119  ASP A N     1 
ATOM   2373  C CA    . ASP D 4 122  ? 134.873 107.971 169.926 1.00 120.25 ? 119  ASP A CA    1 
ATOM   2374  C C     . ASP D 4 122  ? 136.089 108.537 170.649 1.00 120.86 ? 119  ASP A C     1 
ATOM   2375  O O     . ASP D 4 122  ? 136.344 109.746 170.592 1.00 116.86 ? 119  ASP A O     1 
ATOM   2376  C CB    . ASP D 4 122  ? 133.673 107.910 170.871 1.00 123.00 ? 119  ASP A CB    1 
ATOM   2377  C CG    . ASP D 4 122  ? 132.489 107.189 170.262 1.00 123.51 ? 119  ASP A CG    1 
ATOM   2378  O OD1   . ASP D 4 122  ? 132.709 106.261 169.457 1.00 123.76 ? 119  ASP A OD1   1 
ATOM   2379  O OD2   . ASP D 4 122  ? 131.338 107.547 170.589 1.00 123.23 ? 119  ASP A OD2   1 
ATOM   2380  N N     . ALA D 4 123  ? 136.848 107.684 171.341 1.00 124.96 ? 120  ALA A N     1 
ATOM   2381  C CA    . ALA D 4 123  ? 138.025 108.158 172.062 1.00 125.52 ? 120  ALA A CA    1 
ATOM   2382  C C     . ALA D 4 123  ? 139.059 108.737 171.104 1.00 122.28 ? 120  ALA A C     1 
ATOM   2383  O O     . ALA D 4 123  ? 139.613 109.816 171.346 1.00 123.01 ? 120  ALA A O     1 
ATOM   2384  C CB    . ALA D 4 123  ? 138.627 107.022 172.888 1.00 127.62 ? 120  ALA A CB    1 
ATOM   2385  N N     . ILE D 4 124  ? 139.328 108.031 170.005 1.00 118.43 ? 121  ILE A N     1 
ATOM   2386  C CA    . ILE D 4 124  ? 140.269 108.536 169.011 1.00 113.10 ? 121  ILE A CA    1 
ATOM   2387  C C     . ILE D 4 124  ? 139.629 109.649 168.188 1.00 108.01 ? 121  ILE A C     1 
ATOM   2388  O O     . ILE D 4 124  ? 140.290 110.626 167.817 1.00 106.68 ? 121  ILE A O     1 
ATOM   2389  C CB    . ILE D 4 124  ? 140.765 107.385 168.117 1.00 114.71 ? 121  ILE A CB    1 
ATOM   2390  C CG1   . ILE D 4 124  ? 141.334 106.252 168.973 1.00 118.87 ? 121  ILE A CG1   1 
ATOM   2391  C CG2   . ILE D 4 124  ? 141.807 107.882 167.127 1.00 113.27 ? 121  ILE A CG2   1 
ATOM   2392  C CD1   . ILE D 4 124  ? 141.767 105.043 168.174 1.00 119.43 ? 121  ILE A CD1   1 
ATOM   2393  N N     . ASN D 4 125  ? 138.332 109.523 167.900 1.00 102.76 ? 122  ASN A N     1 
ATOM   2394  C CA    . ASN D 4 125  ? 137.657 110.496 167.050 1.00 97.74  ? 122  ASN A CA    1 
ATOM   2395  C C     . ASN D 4 125  ? 137.555 111.858 167.727 1.00 96.00  ? 122  ASN A C     1 
ATOM   2396  O O     . ASN D 4 125  ? 137.705 112.895 167.072 1.00 96.25  ? 122  ASN A O     1 
ATOM   2397  C CB    . ASN D 4 125  ? 136.270 109.975 166.671 1.00 98.17  ? 122  ASN A CB    1 
ATOM   2398  C CG    . ASN D 4 125  ? 135.595 110.820 165.619 1.00 97.33  ? 122  ASN A CG    1 
ATOM   2399  O OD1   . ASN D 4 125  ? 135.804 110.623 164.420 1.00 95.67  ? 122  ASN A OD1   1 
ATOM   2400  N ND2   . ASN D 4 125  ? 134.768 111.761 166.057 1.00 98.25  ? 122  ASN A ND2   1 
ATOM   2401  N N     . LYS D 4 126  ? 137.301 111.878 169.037 1.00 95.44  ? 123  LYS A N     1 
ATOM   2402  C CA    . LYS D 4 126  ? 137.177 113.147 169.749 1.00 92.61  ? 123  LYS A CA    1 
ATOM   2403  C C     . LYS D 4 126  ? 138.532 113.787 170.020 1.00 91.88  ? 123  LYS A C     1 
ATOM   2404  O O     . LYS D 4 126  ? 138.617 115.014 170.143 1.00 86.71  ? 123  LYS A O     1 
ATOM   2405  C CB    . LYS D 4 126  ? 136.422 112.943 171.064 1.00 94.32  ? 123  LYS A CB    1 
ATOM   2406  N N     . ARG D 4 127  ? 139.594 112.983 170.117 1.00 95.36  ? 124  ARG A N     1 
ATOM   2407  C CA    . ARG D 4 127  ? 140.922 113.538 170.368 1.00 94.83  ? 124  ARG A CA    1 
ATOM   2408  C C     . ARG D 4 127  ? 141.403 114.394 169.204 1.00 92.57  ? 124  ARG A C     1 
ATOM   2409  O O     . ARG D 4 127  ? 142.127 115.374 169.416 1.00 93.81  ? 124  ARG A O     1 
ATOM   2410  C CB    . ARG D 4 127  ? 141.918 112.412 170.646 1.00 94.10  ? 124  ARG A CB    1 
ATOM   2411  N N     . HIS D 4 128  ? 141.015 114.045 167.974 1.00 90.07  ? 125  HIS A N     1 
ATOM   2412  C CA    . HIS D 4 128  ? 141.400 114.850 166.822 1.00 87.44  ? 125  HIS A CA    1 
ATOM   2413  C C     . HIS D 4 128  ? 140.670 116.188 166.800 1.00 88.43  ? 125  HIS A C     1 
ATOM   2414  O O     . HIS D 4 128  ? 141.235 117.191 166.350 1.00 86.28  ? 125  HIS A O     1 
ATOM   2415  C CB    . HIS D 4 128  ? 141.128 114.082 165.529 1.00 88.75  ? 125  HIS A CB    1 
ATOM   2416  C CG    . HIS D 4 128  ? 142.002 112.880 165.345 1.00 93.75  ? 125  HIS A CG    1 
ATOM   2417  N ND1   . HIS D 4 128  ? 141.640 111.812 164.552 1.00 94.52  ? 125  HIS A ND1   1 
ATOM   2418  C CD2   . HIS D 4 128  ? 143.223 112.579 165.848 1.00 96.27  ? 125  HIS A CD2   1 
ATOM   2419  C CE1   . HIS D 4 128  ? 142.598 110.903 164.576 1.00 94.82  ? 125  HIS A CE1   1 
ATOM   2420  N NE2   . HIS D 4 128  ? 143.570 111.344 165.356 1.00 95.91  ? 125  HIS A NE2   1 
ATOM   2421  N N     . ALA D 4 129  ? 139.423 116.223 167.277 1.00 91.97  ? 126  ALA A N     1 
ATOM   2422  C CA    . ALA D 4 129  ? 138.668 117.471 167.281 1.00 92.28  ? 126  ALA A CA    1 
ATOM   2423  C C     . ALA D 4 129  ? 139.272 118.482 168.245 1.00 94.29  ? 126  ALA A C     1 
ATOM   2424  O O     . ALA D 4 129  ? 139.265 119.689 167.973 1.00 91.61  ? 126  ALA A O     1 
ATOM   2425  C CB    . ALA D 4 129  ? 137.206 117.199 167.632 1.00 92.60  ? 126  ALA A CB    1 
ATOM   2426  N N     . GLU D 4 130  ? 139.797 118.014 169.381 1.00 99.36  ? 127  GLU A N     1 
ATOM   2427  C CA    . GLU D 4 130  ? 140.444 118.913 170.328 1.00 103.55 ? 127  GLU A CA    1 
ATOM   2428  C C     . GLU D 4 130  ? 141.718 119.523 169.759 1.00 104.67 ? 127  GLU A C     1 
ATOM   2429  O O     . GLU D 4 130  ? 142.152 120.579 170.230 1.00 104.69 ? 127  GLU A O     1 
ATOM   2430  C CB    . GLU D 4 130  ? 140.754 118.174 171.631 1.00 107.12 ? 127  GLU A CB    1 
ATOM   2431  N N     . ILE D 4 131  ? 142.317 118.880 168.762 1.00 107.27 ? 128  ILE A N     1 
ATOM   2432  C CA    . ILE D 4 131  ? 143.509 119.411 168.106 1.00 105.30 ? 128  ILE A CA    1 
ATOM   2433  C C     . ILE D 4 131  ? 143.139 120.312 166.937 1.00 100.49 ? 128  ILE A C     1 
ATOM   2434  O O     . ILE D 4 131  ? 143.690 121.403 166.782 1.00 100.10 ? 128  ILE A O     1 
ATOM   2435  C CB    . ILE D 4 131  ? 144.417 118.250 167.653 1.00 106.95 ? 128  ILE A CB    1 
ATOM   2436  C CG1   . ILE D 4 131  ? 144.790 117.372 168.847 1.00 110.84 ? 128  ILE A CG1   1 
ATOM   2437  C CG2   . ILE D 4 131  ? 145.659 118.785 166.957 1.00 106.26 ? 128  ILE A CG2   1 
ATOM   2438  C CD1   . ILE D 4 131  ? 145.615 116.163 168.475 1.00 111.75 ? 128  ILE A CD1   1 
ATOM   2439  N N     . TYR D 4 132  ? 142.200 119.868 166.096 1.00 94.08  ? 129  TYR A N     1 
ATOM   2440  C CA    . TYR D 4 132  ? 141.807 120.653 164.932 1.00 86.96  ? 129  TYR A CA    1 
ATOM   2441  C C     . TYR D 4 132  ? 141.127 121.958 165.324 1.00 82.73  ? 129  TYR A C     1 
ATOM   2442  O O     . TYR D 4 132  ? 141.152 122.914 164.542 1.00 81.42  ? 129  TYR A O     1 
ATOM   2443  C CB    . TYR D 4 132  ? 140.886 119.826 164.032 1.00 84.76  ? 129  TYR A CB    1 
ATOM   2444  C CG    . TYR D 4 132  ? 140.632 120.436 162.669 1.00 81.18  ? 129  TYR A CG    1 
ATOM   2445  C CD1   . TYR D 4 132  ? 141.493 120.193 161.607 1.00 78.83  ? 129  TYR A CD1   1 
ATOM   2446  C CD2   . TYR D 4 132  ? 139.525 121.244 162.443 1.00 79.94  ? 129  TYR A CD2   1 
ATOM   2447  C CE1   . TYR D 4 132  ? 141.263 120.743 160.360 1.00 77.71  ? 129  TYR A CE1   1 
ATOM   2448  C CE2   . TYR D 4 132  ? 139.288 121.800 161.199 1.00 77.78  ? 129  TYR A CE2   1 
ATOM   2449  C CZ    . TYR D 4 132  ? 140.158 121.545 160.161 1.00 77.28  ? 129  TYR A CZ    1 
ATOM   2450  O OH    . TYR D 4 132  ? 139.925 122.095 158.920 1.00 75.16  ? 129  TYR A OH    1 
ATOM   2451  N N     . LYS D 4 133  ? 140.529 122.021 166.514 1.00 83.28  ? 130  LYS A N     1 
ATOM   2452  C CA    . LYS D 4 133  ? 139.895 123.257 166.962 1.00 82.82  ? 130  LYS A CA    1 
ATOM   2453  C C     . LYS D 4 133  ? 140.931 124.353 167.184 1.00 83.85  ? 130  LYS A C     1 
ATOM   2454  O O     . LYS D 4 133  ? 140.815 125.451 166.628 1.00 83.27  ? 130  LYS A O     1 
ATOM   2455  C CB    . LYS D 4 133  ? 139.096 123.001 168.240 1.00 84.76  ? 130  LYS A CB    1 
ATOM   2456  N N     . GLY D 4 134  ? 141.954 124.070 167.987 1.00 84.65  ? 131  GLY A N     1 
ATOM   2457  C CA    . GLY D 4 134  ? 143.005 125.034 168.239 1.00 84.56  ? 131  GLY A CA    1 
ATOM   2458  C C     . GLY D 4 134  ? 144.179 124.890 167.292 1.00 81.10  ? 131  GLY A C     1 
ATOM   2459  O O     . GLY D 4 134  ? 145.325 125.157 167.665 1.00 81.11  ? 131  GLY A O     1 
ATOM   2460  N N     . LEU D 4 135  ? 143.902 124.470 166.061 1.00 78.28  ? 132  LEU A N     1 
ATOM   2461  C CA    . LEU D 4 135  ? 144.942 124.257 165.064 1.00 75.48  ? 132  LEU A CA    1 
ATOM   2462  C C     . LEU D 4 135  ? 145.185 125.478 164.188 1.00 73.01  ? 132  LEU A C     1 
ATOM   2463  O O     . LEU D 4 135  ? 146.179 125.505 163.452 1.00 69.06  ? 132  LEU A O     1 
ATOM   2464  C CB    . LEU D 4 135  ? 144.578 123.058 164.180 1.00 72.22  ? 132  LEU A CB    1 
ATOM   2465  C CG    . LEU D 4 135  ? 145.717 122.348 163.449 1.00 70.29  ? 132  LEU A CG    1 
ATOM   2466  C CD1   . LEU D 4 135  ? 146.710 121.767 164.442 1.00 71.12  ? 132  LEU A CD1   1 
ATOM   2467  C CD2   . LEU D 4 135  ? 145.162 121.264 162.540 1.00 69.68  ? 132  LEU A CD2   1 
ATOM   2468  N N     . PHE D 4 136  ? 144.315 126.487 164.252 1.00 77.39  ? 133  PHE A N     1 
ATOM   2469  C CA    . PHE D 4 136  ? 144.423 127.664 163.397 1.00 78.23  ? 133  PHE A CA    1 
ATOM   2470  C C     . PHE D 4 136  ? 144.303 128.951 164.204 1.00 80.21  ? 133  PHE A C     1 
ATOM   2471  O O     . PHE D 4 136  ? 143.791 129.956 163.704 1.00 78.46  ? 133  PHE A O     1 
ATOM   2472  C CB    . PHE D 4 136  ? 143.371 127.625 162.289 1.00 77.98  ? 133  PHE A CB    1 
ATOM   2473  C CG    . PHE D 4 136  ? 143.342 126.331 161.532 1.00 79.56  ? 133  PHE A CG    1 
ATOM   2474  C CD1   . PHE D 4 136  ? 144.243 126.091 160.509 1.00 80.67  ? 133  PHE A CD1   1 
ATOM   2475  C CD2   . PHE D 4 136  ? 142.415 125.351 161.847 1.00 80.49  ? 133  PHE A CD2   1 
ATOM   2476  C CE1   . PHE D 4 136  ? 144.221 124.898 159.812 1.00 80.62  ? 133  PHE A CE1   1 
ATOM   2477  C CE2   . PHE D 4 136  ? 142.388 124.156 161.154 1.00 80.79  ? 133  PHE A CE2   1 
ATOM   2478  C CZ    . PHE D 4 136  ? 143.291 123.929 160.134 1.00 80.86  ? 133  PHE A CZ    1 
ATOM   2479  N N     . LYS D 4 137  ? 144.769 128.938 165.447 1.00 80.68  ? 134  LYS A N     1 
ATOM   2480  C CA    . LYS D 4 137  ? 144.786 130.138 166.274 1.00 82.22  ? 134  LYS A CA    1 
ATOM   2481  C C     . LYS D 4 137  ? 145.905 129.991 167.303 1.00 84.97  ? 134  LYS A C     1 
ATOM   2482  O O     . LYS D 4 137  ? 146.827 129.189 167.125 1.00 86.22  ? 134  LYS A O     1 
ATOM   2483  C CB    . LYS D 4 137  ? 143.398 130.386 166.893 1.00 82.22  ? 134  LYS A CB    1 
ATOM   2484  C CG    . LYS D 4 137  ? 142.661 129.140 167.350 1.00 80.69  ? 134  LYS A CG    1 
ATOM   2485  C CD    . LYS D 4 137  ? 141.242 129.496 167.771 1.00 77.48  ? 134  LYS A CD    1 
ATOM   2486  C CE    . LYS D 4 137  ? 140.439 128.265 168.146 1.00 76.40  ? 134  LYS A CE    1 
ATOM   2487  N NZ    . LYS D 4 137  ? 139.040 128.615 168.512 1.00 75.88  ? 134  LYS A NZ    1 
ATOM   2488  N N     . ALA D 4 138  ? 145.820 130.763 168.390 1.00 86.78  ? 135  ALA A N     1 
ATOM   2489  C CA    . ALA D 4 138  ? 146.924 130.886 169.336 1.00 93.94  ? 135  ALA A CA    1 
ATOM   2490  C C     . ALA D 4 138  ? 147.257 129.591 170.065 1.00 112.24 ? 135  ALA A C     1 
ATOM   2491  O O     . ALA D 4 138  ? 148.287 129.539 170.747 1.00 129.30 ? 135  ALA A O     1 
ATOM   2492  C CB    . ALA D 4 138  ? 146.615 131.980 170.359 1.00 116.29 ? 135  ALA A CB    1 
ATOM   2493  N N     . GLU D 4 139  ? 146.431 128.550 169.945 1.00 109.33 ? 136  GLU A N     1 
ATOM   2494  C CA    . GLU D 4 139  ? 146.709 127.306 170.656 1.00 113.99 ? 136  GLU A CA    1 
ATOM   2495  C C     . GLU D 4 139  ? 147.890 126.539 170.074 1.00 114.10 ? 136  GLU A C     1 
ATOM   2496  O O     . GLU D 4 139  ? 148.363 125.594 170.715 1.00 116.37 ? 136  GLU A O     1 
ATOM   2497  C CB    . GLU D 4 139  ? 145.465 126.416 170.669 1.00 116.25 ? 136  GLU A CB    1 
ATOM   2498  C CG    . GLU D 4 139  ? 144.274 127.037 171.382 1.00 119.26 ? 136  GLU A CG    1 
ATOM   2499  C CD    . GLU D 4 139  ? 143.166 126.038 171.651 1.00 121.80 ? 136  GLU A CD    1 
ATOM   2500  O OE1   . GLU D 4 139  ? 143.459 124.825 171.710 1.00 123.52 ? 136  GLU A OE1   1 
ATOM   2501  O OE2   . GLU D 4 139  ? 142.003 126.465 171.801 1.00 121.83 ? 136  GLU A OE2   1 
ATOM   2502  N N     . LEU D 4 140  ? 148.370 126.910 168.885 1.00 107.02 ? 137  LEU A N     1 
ATOM   2503  C CA    . LEU D 4 140  ? 149.603 126.320 168.370 1.00 101.61 ? 137  LEU A CA    1 
ATOM   2504  C C     . LEU D 4 140  ? 150.784 126.645 169.275 1.00 103.71 ? 137  LEU A C     1 
ATOM   2505  O O     . LEU D 4 140  ? 151.680 125.814 169.465 1.00 107.16 ? 137  LEU A O     1 
ATOM   2506  C CB    . LEU D 4 140  ? 149.880 126.825 166.954 1.00 94.93  ? 137  LEU A CB    1 
ATOM   2507  C CG    . LEU D 4 140  ? 149.036 126.316 165.786 1.00 89.43  ? 137  LEU A CG    1 
ATOM   2508  C CD1   . LEU D 4 140  ? 149.383 127.096 164.532 1.00 86.10  ? 137  LEU A CD1   1 
ATOM   2509  C CD2   . LEU D 4 140  ? 149.259 124.828 165.572 1.00 87.84  ? 137  LEU A CD2   1 
ATOM   2510  N N     . PHE D 4 141  ? 150.796 127.849 169.844 1.00 103.02 ? 138  PHE A N     1 
ATOM   2511  C CA    . PHE D 4 141  ? 151.920 128.341 170.627 1.00 105.69 ? 138  PHE A CA    1 
ATOM   2512  C C     . PHE D 4 141  ? 151.878 127.890 172.079 1.00 110.93 ? 138  PHE A C     1 
ATOM   2513  O O     . PHE D 4 141  ? 152.892 128.007 172.776 1.00 112.12 ? 138  PHE A O     1 
ATOM   2514  C CB    . PHE D 4 141  ? 151.963 129.870 170.561 1.00 105.68 ? 138  PHE A CB    1 
ATOM   2515  C CG    . PHE D 4 141  ? 151.964 130.419 169.158 1.00 103.39 ? 138  PHE A CG    1 
ATOM   2516  C CD1   . PHE D 4 141  ? 150.781 130.538 168.444 1.00 100.97 ? 138  PHE A CD1   1 
ATOM   2517  C CD2   . PHE D 4 141  ? 153.145 130.819 168.557 1.00 103.07 ? 138  PHE A CD2   1 
ATOM   2518  C CE1   . PHE D 4 141  ? 150.778 131.038 167.157 1.00 97.47  ? 138  PHE A CE1   1 
ATOM   2519  C CE2   . PHE D 4 141  ? 153.147 131.324 167.270 1.00 100.07 ? 138  PHE A CE2   1 
ATOM   2520  C CZ    . PHE D 4 141  ? 151.962 131.431 166.569 1.00 96.94  ? 138  PHE A CZ    1 
ATOM   2521  N N     . ASN D 4 142  ? 150.736 127.381 172.550 1.00 114.51 ? 139  ASN A N     1 
ATOM   2522  C CA    . ASN D 4 142  ? 150.644 126.875 173.912 1.00 118.97 ? 139  ASN A CA    1 
ATOM   2523  C C     . ASN D 4 142  ? 151.562 125.687 174.151 1.00 121.33 ? 139  ASN A C     1 
ATOM   2524  O O     . ASN D 4 142  ? 151.858 125.368 175.308 1.00 123.03 ? 139  ASN A O     1 
ATOM   2525  C CB    . ASN D 4 142  ? 149.208 126.455 174.227 1.00 118.90 ? 139  ASN A CB    1 
ATOM   2526  C CG    . ASN D 4 142  ? 148.213 127.574 174.020 1.00 117.27 ? 139  ASN A CG    1 
ATOM   2527  O OD1   . ASN D 4 142  ? 148.582 128.689 173.656 1.00 115.83 ? 139  ASN A OD1   1 
ATOM   2528  N ND2   . ASN D 4 142  ? 146.938 127.279 174.246 1.00 117.24 ? 139  ASN A ND2   1 
ATOM   2529  N N     . GLY D 4 143  ? 152.018 125.030 173.089 1.00 121.35 ? 140  GLY A N     1 
ATOM   2530  C CA    . GLY D 4 143  ? 152.569 123.701 173.219 1.00 124.23 ? 140  GLY A CA    1 
ATOM   2531  C C     . GLY D 4 143  ? 151.539 122.638 173.514 1.00 125.94 ? 140  GLY A C     1 
ATOM   2532  O O     . GLY D 4 143  ? 151.899 121.460 173.603 1.00 127.20 ? 140  GLY A O     1 
ATOM   2533  N N     . LYS D 4 144  ? 150.267 123.021 173.666 1.00 126.32 ? 141  LYS A N     1 
ATOM   2534  C CA    . LYS D 4 144  ? 149.217 122.051 173.949 1.00 127.37 ? 141  LYS A CA    1 
ATOM   2535  C C     . LYS D 4 144  ? 149.054 121.072 172.795 1.00 126.44 ? 141  LYS A C     1 
ATOM   2536  O O     . LYS D 4 144  ? 149.055 119.855 173.000 1.00 128.10 ? 141  LYS A O     1 
ATOM   2537  C CB    . LYS D 4 144  ? 147.899 122.775 174.236 1.00 126.48 ? 141  LYS A CB    1 
ATOM   2538  N N     . VAL D 4 145  ? 148.922 121.587 171.570 1.00 123.65 ? 142  VAL A N     1 
ATOM   2539  C CA    . VAL D 4 145  ? 148.805 120.715 170.404 1.00 121.53 ? 142  VAL A CA    1 
ATOM   2540  C C     . VAL D 4 145  ? 150.044 119.837 170.273 1.00 123.73 ? 142  VAL A C     1 
ATOM   2541  O O     . VAL D 4 145  ? 149.946 118.638 169.984 1.00 122.20 ? 142  VAL A O     1 
ATOM   2542  C CB    . VAL D 4 145  ? 148.546 121.550 169.135 1.00 118.95 ? 142  VAL A CB    1 
ATOM   2543  C CG1   . VAL D 4 145  ? 147.129 122.102 169.151 1.00 118.40 ? 142  VAL A CG1   1 
ATOM   2544  C CG2   . VAL D 4 145  ? 149.544 122.691 169.032 1.00 119.55 ? 142  VAL A CG2   1 
ATOM   2545  N N     . LEU D 4 146  ? 151.224 120.411 170.511 1.00 126.87 ? 143  LEU A N     1 
ATOM   2546  C CA    . LEU D 4 146  ? 152.442 119.615 170.563 1.00 128.66 ? 143  LEU A CA    1 
ATOM   2547  C C     . LEU D 4 146  ? 152.474 118.701 171.782 1.00 134.39 ? 143  LEU A C     1 
ATOM   2548  O O     . LEU D 4 146  ? 153.137 117.659 171.742 1.00 133.38 ? 143  LEU A O     1 
ATOM   2549  C CB    . LEU D 4 146  ? 153.661 120.542 170.532 1.00 125.15 ? 143  LEU A CB    1 
ATOM   2550  C CG    . LEU D 4 146  ? 154.983 120.123 171.174 1.00 124.33 ? 143  LEU A CG    1 
ATOM   2551  C CD1   . LEU D 4 146  ? 156.119 120.223 170.172 1.00 121.41 ? 143  LEU A CD1   1 
ATOM   2552  C CD2   . LEU D 4 146  ? 155.262 120.999 172.383 1.00 126.05 ? 143  LEU A CD2   1 
ATOM   2553  N N     . LYS D 4 147  ? 151.759 119.053 172.853 1.00 142.81 ? 144  LYS A N     1 
ATOM   2554  C CA    . LYS D 4 147  ? 151.649 118.137 173.983 1.00 146.04 ? 144  LYS A CA    1 
ATOM   2555  C C     . LYS D 4 147  ? 150.781 116.930 173.644 1.00 145.97 ? 144  LYS A C     1 
ATOM   2556  O O     . LYS D 4 147  ? 151.014 115.840 174.177 1.00 149.19 ? 144  LYS A O     1 
ATOM   2557  C CB    . LYS D 4 147  ? 151.098 118.860 175.213 1.00 147.77 ? 144  LYS A CB    1 
ATOM   2558  N N     . GLN D 4 148  ? 149.780 117.099 172.771 1.00 137.88 ? 145  GLN A N     1 
ATOM   2559  C CA    . GLN D 4 148  ? 149.024 115.938 172.308 1.00 130.71 ? 145  GLN A CA    1 
ATOM   2560  C C     . GLN D 4 148  ? 149.883 115.038 171.429 1.00 127.34 ? 145  GLN A C     1 
ATOM   2561  O O     . GLN D 4 148  ? 149.633 113.832 171.346 1.00 129.20 ? 145  GLN A O     1 
ATOM   2562  C CB    . GLN D 4 148  ? 147.766 116.359 171.538 1.00 123.13 ? 145  GLN A CB    1 
ATOM   2563  C CG    . GLN D 4 148  ? 147.277 117.772 171.808 1.00 119.79 ? 145  GLN A CG    1 
ATOM   2564  C CD    . GLN D 4 148  ? 145.833 117.834 172.273 1.00 119.01 ? 145  GLN A CD    1 
ATOM   2565  O OE1   . GLN D 4 148  ? 145.193 116.801 172.486 1.00 117.50 ? 145  GLN A OE1   1 
ATOM   2566  N NE2   . GLN D 4 148  ? 145.309 119.044 172.425 1.00 120.01 ? 145  GLN A NE2   1 
ATOM   2567  N N     . LEU D 4 149  ? 150.895 115.605 170.780 1.00 122.10 ? 146  LEU A N     1 
ATOM   2568  C CA    . LEU D 4 149  ? 151.762 114.850 169.886 1.00 117.84 ? 146  LEU A CA    1 
ATOM   2569  C C     . LEU D 4 149  ? 153.023 114.388 170.610 1.00 118.91 ? 146  LEU A C     1 
ATOM   2570  O O     . LEU D 4 149  ? 153.354 113.202 170.609 1.00 119.01 ? 146  LEU A O     1 
ATOM   2571  C CB    . LEU D 4 149  ? 152.133 115.696 168.664 1.00 113.63 ? 146  LEU A CB    1 
ATOM   2572  C CG    . LEU D 4 149  ? 151.179 115.768 167.463 1.00 110.55 ? 146  LEU A CG    1 
ATOM   2573  C CD1   . LEU D 4 149  ? 149.737 115.452 167.834 1.00 111.34 ? 146  LEU A CD1   1 
ATOM   2574  C CD2   . LEU D 4 149  ? 151.268 117.139 166.800 1.00 107.90 ? 146  LEU A CD2   1 
ATOM   2575  N N     . THR D 4 153  ? 158.846 114.825 168.438 1.00 113.34 ? 150  THR A N     1 
ATOM   2576  C CA    . THR D 4 153  ? 158.261 115.283 167.161 1.00 118.25 ? 150  THR A CA    1 
ATOM   2577  C C     . THR D 4 153  ? 158.800 116.654 166.788 1.00 117.75 ? 150  THR A C     1 
ATOM   2578  O O     . THR D 4 153  ? 158.248 117.239 165.830 1.00 116.11 ? 150  THR A O     1 
ATOM   2579  C CB    . THR D 4 153  ? 156.765 115.538 167.310 1.00 122.60 ? 150  THR A CB    1 
ATOM   2580  O OG1   . THR D 4 153  ? 156.601 116.723 168.089 1.00 122.26 ? 150  THR A OG1   1 
ATOM   2581  C CG2   . THR D 4 153  ? 156.037 114.386 167.968 1.00 124.04 ? 150  THR A CG2   1 
ATOM   2582  N N     . THR D 4 154  ? 159.841 117.141 167.477 1.00 119.02 ? 151  THR A N     1 
ATOM   2583  C CA    . THR D 4 154  ? 160.282 118.541 167.251 1.00 118.47 ? 151  THR A CA    1 
ATOM   2584  C C     . THR D 4 154  ? 161.631 118.769 167.918 1.00 121.21 ? 151  THR A C     1 
ATOM   2585  O O     . THR D 4 154  ? 161.981 117.945 168.770 1.00 122.91 ? 151  THR A O     1 
ATOM   2586  C CB    . THR D 4 154  ? 159.172 119.458 167.791 1.00 118.38 ? 151  THR A CB    1 
ATOM   2587  O OG1   . THR D 4 154  ? 158.968 119.192 169.179 1.00 116.23 ? 151  THR A OG1   1 
ATOM   2588  C CG2   . THR D 4 154  ? 157.851 119.338 167.064 1.00 116.75 ? 151  THR A CG2   1 
ATOM   2589  N N     . THR D 4 155  ? 162.341 119.847 167.572 1.00 121.09 ? 152  THR A N     1 
ATOM   2590  C CA    . THR D 4 155  ? 163.642 120.226 168.195 1.00 121.57 ? 152  THR A CA    1 
ATOM   2591  C C     . THR D 4 155  ? 163.374 120.993 169.487 1.00 121.81 ? 152  THR A C     1 
ATOM   2592  O O     . THR D 4 155  ? 162.249 121.473 169.668 1.00 120.92 ? 152  THR A O     1 
ATOM   2593  C CB    . THR D 4 155  ? 164.511 121.078 167.266 1.00 116.03 ? 152  THR A CB    1 
ATOM   2594  O OG1   . THR D 4 155  ? 163.797 122.263 166.926 1.00 112.08 ? 152  THR A OG1   1 
ATOM   2595  C CG2   . THR D 4 155  ? 164.894 120.349 165.997 1.00 112.06 ? 152  THR A CG2   1 
ATOM   2596  N N     . GLU D 4 156  ? 164.375 121.410 170.275 1.00 123.10 ? 153  GLU A N     1 
ATOM   2597  C CA    . GLU D 4 156  ? 164.075 122.292 171.463 1.00 121.92 ? 153  GLU A CA    1 
ATOM   2598  C C     . GLU D 4 156  ? 163.951 123.769 171.025 1.00 118.78 ? 153  GLU A C     1 
ATOM   2599  O O     . GLU D 4 156  ? 163.214 124.641 171.706 1.00 118.51 ? 153  GLU A O     1 
ATOM   2600  C CB    . GLU D 4 156  ? 165.152 122.127 172.537 1.00 124.48 ? 153  GLU A CB    1 
ATOM   2601  N N     . HIS D 4 157  ? 164.646 124.092 169.931 1.00 116.04 ? 154  HIS A N     1 
ATOM   2602  C CA    . HIS D 4 157  ? 164.520 125.465 169.387 1.00 111.24 ? 154  HIS A CA    1 
ATOM   2603  C C     . HIS D 4 157  ? 163.032 125.725 169.177 1.00 109.05 ? 154  HIS A C     1 
ATOM   2604  O O     . HIS D 4 157  ? 162.626 126.877 169.328 1.00 108.24 ? 154  HIS A O     1 
ATOM   2605  C CB    . HIS D 4 157  ? 165.332 125.630 168.098 1.00 106.23 ? 154  HIS A CB    1 
ATOM   2606  C CG    . HIS D 4 157  ? 165.152 126.961 167.449 1.00 101.74 ? 154  HIS A CG    1 
ATOM   2607  N ND1   . HIS D 4 157  ? 165.080 127.113 166.078 1.00 98.32  ? 154  HIS A ND1   1 
ATOM   2608  C CD2   . HIS D 4 157  ? 165.015 128.198 167.976 1.00 101.44 ? 154  HIS A CD2   1 
ATOM   2609  C CE1   . HIS D 4 157  ? 164.917 128.388 165.788 1.00 97.09  ? 154  HIS A CE1   1 
ATOM   2610  N NE2   . HIS D 4 157  ? 164.871 129.074 166.935 1.00 99.06  ? 154  HIS A NE2   1 
ATOM   2611  N N     . GLU D 4 158  ? 162.255 124.684 168.862 1.00 108.15 ? 155  GLU A N     1 
ATOM   2612  C CA    . GLU D 4 158  ? 160.789 124.818 168.678 1.00 106.08 ? 155  GLU A CA    1 
ATOM   2613  C C     . GLU D 4 158  ? 160.167 125.383 169.938 1.00 108.19 ? 155  GLU A C     1 
ATOM   2614  O O     . GLU D 4 158  ? 159.633 126.465 169.849 1.00 108.29 ? 155  GLU A O     1 
ATOM   2615  C CB    . GLU D 4 158  ? 160.129 123.476 168.387 1.00 105.31 ? 155  GLU A CB    1 
ATOM   2616  C CG    . GLU D 4 158  ? 158.623 123.488 168.106 1.00 103.75 ? 155  GLU A CG    1 
ATOM   2617  C CD    . GLU D 4 158  ? 157.657 123.564 169.268 1.00 102.52 ? 155  GLU A CD    1 
ATOM   2618  O OE1   . GLU D 4 158  ? 158.050 123.145 170.374 1.00 102.99 ? 155  GLU A OE1   1 
ATOM   2619  O OE2   . GLU D 4 158  ? 156.535 124.041 169.067 1.00 100.59 ? 155  GLU A OE2   1 
ATOM   2620  N N     . ASN D 4 159  ? 160.136 124.627 171.028 1.00 114.27 ? 156  ASN A N     1 
ATOM   2621  C CA    . ASN D 4 159  ? 159.651 125.181 172.310 1.00 115.87 ? 156  ASN A CA    1 
ATOM   2622  C C     . ASN D 4 159  ? 160.053 126.657 172.317 1.00 114.15 ? 156  ASN A C     1 
ATOM   2623  O O     . ASN D 4 159  ? 159.138 127.515 172.249 1.00 113.05 ? 156  ASN A O     1 
ATOM   2624  C CB    . ASN D 4 159  ? 160.209 124.418 173.512 1.00 123.27 ? 156  ASN A CB    1 
ATOM   2625  C CG    . ASN D 4 159  ? 159.953 122.928 173.437 1.00 125.57 ? 156  ASN A CG    1 
ATOM   2626  O OD1   . ASN D 4 159  ? 158.806 122.488 173.468 1.00 124.81 ? 156  ASN A OD1   1 
ATOM   2627  N ND2   . ASN D 4 159  ? 161.015 122.147 173.328 1.00 127.74 ? 156  ASN A ND2   1 
ATOM   2628  N N     . ALA D 4 160  ? 161.362 126.949 172.248 1.00 114.07 ? 157  ALA A N     1 
ATOM   2629  C CA    . ALA D 4 160  ? 161.755 128.382 172.406 1.00 111.66 ? 157  ALA A CA    1 
ATOM   2630  C C     . ALA D 4 160  ? 160.979 129.357 171.490 1.00 104.25 ? 157  ALA A C     1 
ATOM   2631  O O     . ALA D 4 160  ? 160.259 130.268 172.007 1.00 103.00 ? 157  ALA A O     1 
ATOM   2632  C CB    . ALA D 4 160  ? 163.244 128.514 172.189 1.00 113.69 ? 157  ALA A CB    1 
ATOM   2633  N N     . LEU D 4 161  ? 161.122 129.219 170.174 1.00 98.50  ? 158  LEU A N     1 
ATOM   2634  C CA    . LEU D 4 161  ? 160.503 130.160 169.199 1.00 94.06  ? 158  LEU A CA    1 
ATOM   2635  C C     . LEU D 4 161  ? 158.957 130.121 169.194 1.00 93.31  ? 158  LEU A C     1 
ATOM   2636  O O     . LEU D 4 161  ? 158.369 131.159 168.829 1.00 93.33  ? 158  LEU A O     1 
ATOM   2637  C CB    . LEU D 4 161  ? 161.104 129.812 167.832 1.00 90.41  ? 158  LEU A CB    1 
ATOM   2638  C CG    . LEU D 4 161  ? 160.562 130.607 166.646 1.00 89.99  ? 158  LEU A CG    1 
ATOM   2639  C CD1   . LEU D 4 161  ? 160.879 132.085 166.797 1.00 88.47  ? 158  LEU A CD1   1 
ATOM   2640  C CD2   . LEU D 4 161  ? 161.101 130.080 165.328 1.00 88.47  ? 158  LEU A CD2   1 
ATOM   2641  N N     . LEU D 4 162  ? 158.279 129.027 169.568 1.00 91.16  ? 159  LEU A N     1 
ATOM   2642  C CA    . LEU D 4 162  ? 156.784 129.056 169.638 1.00 86.84  ? 159  LEU A CA    1 
ATOM   2643  C C     . LEU D 4 162  ? 156.396 129.818 170.906 1.00 88.43  ? 159  LEU A C     1 
ATOM   2644  O O     . LEU D 4 162  ? 155.393 130.556 170.873 1.00 84.71  ? 159  LEU A O     1 
ATOM   2645  C CB    . LEU D 4 162  ? 156.169 127.652 169.612 1.00 86.53  ? 159  LEU A CB    1 
ATOM   2646  C CG    . LEU D 4 162  ? 155.491 127.247 168.296 1.00 85.36  ? 159  LEU A CG    1 
ATOM   2647  C CD1   . LEU D 4 162  ? 154.832 125.881 168.402 1.00 86.84  ? 159  LEU A CD1   1 
ATOM   2648  C CD2   . LEU D 4 162  ? 154.452 128.258 167.863 1.00 81.82  ? 159  LEU A CD2   1 
ATOM   2649  N N     . ARG D 4 163  ? 157.152 129.656 171.992 1.00 93.93  ? 160  ARG A N     1 
ATOM   2650  C CA    . ARG D 4 163  ? 156.919 130.473 173.209 1.00 84.24  ? 160  ARG A CA    1 
ATOM   2651  C C     . ARG D 4 163  ? 157.122 131.936 172.804 1.00 83.30  ? 160  ARG A C     1 
ATOM   2652  O O     . ARG D 4 163  ? 156.454 132.817 173.410 1.00 84.04  ? 160  ARG A O     1 
ATOM   2653  C CB    . ARG D 4 163  ? 157.870 130.081 174.343 1.00 96.86  ? 160  ARG A CB    1 
ATOM   2654  C CG    . ARG D 4 163  ? 157.605 128.711 174.947 1.00 98.39  ? 160  ARG A CG    1 
ATOM   2655  C CD    . ARG D 4 163  ? 158.363 128.522 176.247 1.00 93.33  ? 160  ARG A CD    1 
ATOM   2656  N NE    . ARG D 4 163  ? 159.734 129.010 176.161 1.00 101.10 ? 160  ARG A NE    1 
ATOM   2657  C CZ    . ARG D 4 163  ? 160.778 128.311 175.722 1.00 101.24 ? 160  ARG A CZ    1 
ATOM   2658  N NH1   . ARG D 4 163  ? 160.641 127.061 175.315 1.00 96.15  ? 160  ARG A NH1   1 
ATOM   2659  N NH2   . ARG D 4 163  ? 161.972 128.874 175.693 1.00 101.73 ? 160  ARG A NH2   1 
ATOM   2660  N N     . SER D 4 164  ? 157.989 132.194 171.812 1.00 84.68  ? 161  SER A N     1 
ATOM   2661  C CA    . SER D 4 164  ? 158.295 133.585 171.357 1.00 80.84  ? 161  SER A CA    1 
ATOM   2662  C C     . SER D 4 164  ? 157.092 134.361 170.762 1.00 81.53  ? 161  SER A C     1 
ATOM   2663  O O     . SER D 4 164  ? 157.200 135.591 170.820 1.00 77.86  ? 161  SER A O     1 
ATOM   2664  C CB    . SER D 4 164  ? 159.463 133.612 170.395 1.00 79.73  ? 161  SER A CB    1 
ATOM   2665  O OG    . SER D 4 164  ? 160.614 133.013 170.972 1.00 79.34  ? 161  SER A OG    1 
ATOM   2666  N N     . PHE D 4 165  ? 156.025 133.757 170.195 1.00 79.65  ? 162  PHE A N     1 
ATOM   2667  C CA    . PHE D 4 165  ? 154.871 134.494 169.701 1.00 77.85  ? 162  PHE A CA    1 
ATOM   2668  C C     . PHE D 4 165  ? 153.625 134.161 170.513 1.00 78.98  ? 162  PHE A C     1 
ATOM   2669  O O     . PHE D 4 165  ? 152.513 134.093 169.984 1.00 77.33  ? 162  PHE A O     1 
ATOM   2670  C CB    . PHE D 4 165  ? 154.642 134.216 168.218 1.00 76.31  ? 162  PHE A CB    1 
ATOM   2671  C CG    . PHE D 4 165  ? 155.656 134.863 167.319 1.00 76.35  ? 162  PHE A CG    1 
ATOM   2672  C CD1   . PHE D 4 165  ? 155.615 136.226 167.083 1.00 76.27  ? 162  PHE A CD1   1 
ATOM   2673  C CD2   . PHE D 4 165  ? 156.650 134.111 166.715 1.00 76.20  ? 162  PHE A CD2   1 
ATOM   2674  C CE1   . PHE D 4 165  ? 156.544 136.829 166.259 1.00 74.11  ? 162  PHE A CE1   1 
ATOM   2675  C CE2   . PHE D 4 165  ? 157.582 134.708 165.888 1.00 75.44  ? 162  PHE A CE2   1 
ATOM   2676  C CZ    . PHE D 4 165  ? 157.530 136.070 165.661 1.00 74.23  ? 162  PHE A CZ    1 
ATOM   2677  N N     . ASP D 4 166  ? 153.800 133.938 171.813 1.00 82.48  ? 163  ASP A N     1 
ATOM   2678  C CA    . ASP D 4 166  ? 152.655 133.787 172.700 1.00 84.23  ? 163  ASP A CA    1 
ATOM   2679  C C     . ASP D 4 166  ? 151.979 135.140 172.883 1.00 85.21  ? 163  ASP A C     1 
ATOM   2680  O O     . ASP D 4 166  ? 152.650 136.151 173.118 1.00 86.32  ? 163  ASP A O     1 
ATOM   2681  C CB    . ASP D 4 166  ? 153.093 133.215 174.048 1.00 88.02  ? 163  ASP A CB    1 
ATOM   2682  N N     . LYS D 4 167  ? 150.652 135.175 172.721 1.00 84.41  ? 164  LYS A N     1 
ATOM   2683  C CA    . LYS D 4 167  ? 149.915 136.469 172.785 1.00 81.83  ? 164  LYS A CA    1 
ATOM   2684  C C     . LYS D 4 167  ? 150.418 137.379 171.657 1.00 80.33  ? 164  LYS A C     1 
ATOM   2685  O O     . LYS D 4 167  ? 150.188 138.602 171.743 1.00 78.15  ? 164  LYS A O     1 
ATOM   2686  C CB    . LYS D 4 167  ? 150.072 137.131 174.160 1.00 83.32  ? 164  LYS A CB    1 
ATOM   2687  N N     . PHE D 4 168  ? 151.075 136.802 170.644 1.00 83.02  ? 165  PHE A N     1 
ATOM   2688  C CA    . PHE D 4 168  ? 151.586 137.591 169.491 1.00 84.45  ? 165  PHE A CA    1 
ATOM   2689  C C     . PHE D 4 168  ? 151.415 136.787 168.197 1.00 82.33  ? 165  PHE A C     1 
ATOM   2690  O O     . PHE D 4 168  ? 152.436 136.404 167.598 1.00 85.33  ? 165  PHE A O     1 
ATOM   2691  C CB    . PHE D 4 168  ? 153.058 137.956 169.698 1.00 86.22  ? 165  PHE A CB    1 
ATOM   2692  C CG    . PHE D 4 168  ? 153.305 139.317 170.298 1.00 84.41  ? 165  PHE A CG    1 
ATOM   2693  C CD1   . PHE D 4 168  ? 153.341 140.448 169.498 1.00 67.98  ? 165  PHE A CD1   1 
ATOM   2694  C CD2   . PHE D 4 168  ? 153.518 139.467 171.659 1.00 72.30  ? 165  PHE A CD2   1 
ATOM   2695  C CE1   . PHE D 4 168  ? 153.574 141.699 170.047 1.00 67.25  ? 165  PHE A CE1   1 
ATOM   2696  C CE2   . PHE D 4 168  ? 153.753 140.719 172.206 1.00 71.57  ? 165  PHE A CE2   1 
ATOM   2697  C CZ    . PHE D 4 168  ? 153.781 141.832 171.400 1.00 69.05  ? 165  PHE A CZ    1 
ATOM   2698  N N     . THR D 4 169  ? 150.169 136.548 167.776 1.00 77.76  ? 166  THR A N     1 
ATOM   2699  C CA    . THR D 4 169  ? 149.915 135.718 166.566 1.00 76.86  ? 166  THR A CA    1 
ATOM   2700  C C     . THR D 4 169  ? 149.354 136.593 165.440 1.00 75.42  ? 166  THR A C     1 
ATOM   2701  O O     . THR D 4 169  ? 148.769 136.026 164.496 1.00 75.41  ? 166  THR A O     1 
ATOM   2702  C CB    . THR D 4 169  ? 148.963 134.561 166.892 1.00 80.29  ? 166  THR A CB    1 
ATOM   2703  O OG1   . THR D 4 169  ? 147.627 135.065 166.872 1.00 82.78  ? 166  THR A OG1   1 
ATOM   2704  C CG2   . THR D 4 169  ? 149.252 133.925 168.233 1.00 83.41  ? 166  THR A CG2   1 
ATOM   2705  N N     . THR D 4 170  ? 149.529 137.914 165.534 1.00 73.83  ? 167  THR A N     1 
ATOM   2706  C CA    . THR D 4 170  ? 148.955 138.845 164.524 1.00 70.13  ? 167  THR A CA    1 
ATOM   2707  C C     . THR D 4 170  ? 149.541 138.556 163.137 1.00 66.91  ? 167  THR A C     1 
ATOM   2708  O O     . THR D 4 170  ? 148.752 138.480 162.175 1.00 63.17  ? 167  THR A O     1 
ATOM   2709  C CB    . THR D 4 170  ? 149.197 140.304 164.931 1.00 67.72  ? 167  THR A CB    1 
ATOM   2710  O OG1   . THR D 4 170  ? 148.649 140.494 166.236 1.00 67.15  ? 167  THR A OG1   1 
ATOM   2711  C CG2   . THR D 4 170  ? 148.585 141.297 163.968 1.00 63.29  ? 167  THR A CG2   1 
ATOM   2712  N N     . TYR D 4 171  ? 150.866 138.409 163.037 1.00 68.68  ? 168  TYR A N     1 
ATOM   2713  C CA    . TYR D 4 171  ? 151.529 138.174 161.727 1.00 69.23  ? 168  TYR A CA    1 
ATOM   2714  C C     . TYR D 4 171  ? 151.028 136.872 161.102 1.00 64.81  ? 168  TYR A C     1 
ATOM   2715  O O     . TYR D 4 171  ? 151.049 136.763 159.860 1.00 65.00  ? 168  TYR A O     1 
ATOM   2716  C CB    . TYR D 4 171  ? 153.039 138.004 161.896 1.00 73.94  ? 168  TYR A CB    1 
ATOM   2717  C CG    . TYR D 4 171  ? 153.775 139.114 162.601 1.00 61.61  ? 168  TYR A CG    1 
ATOM   2718  C CD1   . TYR D 4 171  ? 153.896 139.130 163.981 1.00 61.69  ? 168  TYR A CD1   1 
ATOM   2719  C CD2   . TYR D 4 171  ? 154.393 140.125 161.885 1.00 61.30  ? 168  TYR A CD2   1 
ATOM   2720  C CE1   . TYR D 4 171  ? 154.588 140.137 164.633 1.00 61.52  ? 168  TYR A CE1   1 
ATOM   2721  C CE2   . TYR D 4 171  ? 155.091 141.138 162.521 1.00 61.05  ? 168  TYR A CE2   1 
ATOM   2722  C CZ    . TYR D 4 171  ? 155.188 141.145 163.901 1.00 61.19  ? 168  TYR A CZ    1 
ATOM   2723  O OH    . TYR D 4 171  ? 155.874 142.141 164.533 1.00 61.09  ? 168  TYR A OH    1 
ATOM   2724  N N     . PHE D 4 172  ? 150.598 135.917 161.927 1.00 62.69  ? 169  PHE A N     1 
ATOM   2725  C CA    . PHE D 4 172  ? 150.211 134.575 161.416 1.00 63.52  ? 169  PHE A CA    1 
ATOM   2726  C C     . PHE D 4 172  ? 148.762 134.587 160.914 1.00 63.33  ? 169  PHE A C     1 
ATOM   2727  O O     . PHE D 4 172  ? 148.231 133.500 160.622 1.00 61.82  ? 169  PHE A O     1 
ATOM   2728  C CB    . PHE D 4 172  ? 150.409 133.518 162.506 1.00 64.12  ? 169  PHE A CB    1 
ATOM   2729  C CG    . PHE D 4 172  ? 151.812 133.451 163.055 1.00 65.56  ? 169  PHE A CG    1 
ATOM   2730  C CD1   . PHE D 4 172  ? 152.191 134.233 164.134 1.00 66.96  ? 169  PHE A CD1   1 
ATOM   2731  C CD2   . PHE D 4 172  ? 152.756 132.612 162.486 1.00 64.94  ? 169  PHE A CD2   1 
ATOM   2732  C CE1   . PHE D 4 172  ? 153.482 134.175 164.634 1.00 67.82  ? 169  PHE A CE1   1 
ATOM   2733  C CE2   . PHE D 4 172  ? 154.047 132.554 162.988 1.00 65.91  ? 169  PHE A CE2   1 
ATOM   2734  C CZ    . PHE D 4 172  ? 154.407 133.335 164.060 1.00 67.72  ? 169  PHE A CZ    1 
ATOM   2735  N N     . SER D 4 173  ? 148.152 135.773 160.811 1.00 63.36  ? 170  SER A N     1 
ATOM   2736  C CA    . SER D 4 173  ? 146.750 135.881 160.323 1.00 61.26  ? 170  SER A CA    1 
ATOM   2737  C C     . SER D 4 173  ? 146.614 135.205 158.954 1.00 59.08  ? 170  SER A C     1 
ATOM   2738  O O     . SER D 4 173  ? 145.969 134.142 158.883 1.00 58.26  ? 170  SER A O     1 
ATOM   2739  C CB    . SER D 4 173  ? 146.308 137.319 160.267 1.00 61.06  ? 170  SER A CB    1 
ATOM   2740  O OG    . SER D 4 173  ? 144.989 137.419 159.750 1.00 61.66  ? 170  SER A OG    1 
ATOM   2741  N N     . GLY D 4 174  ? 147.181 135.811 157.906 1.00 58.91  ? 171  GLY A N     1 
ATOM   2742  C CA    . GLY D 4 174  ? 147.110 135.223 156.580 1.00 59.54  ? 171  GLY A CA    1 
ATOM   2743  C C     . GLY D 4 174  ? 147.683 133.825 156.517 1.00 62.71  ? 171  GLY A C     1 
ATOM   2744  O O     . GLY D 4 174  ? 147.226 132.997 155.721 1.00 63.50  ? 171  GLY A O     1 
ATOM   2745  N N     . PHE D 4 175  ? 148.688 133.537 157.350 1.00 65.06  ? 172  PHE A N     1 
ATOM   2746  C CA    . PHE D 4 175  ? 149.240 132.189 157.422 1.00 64.17  ? 172  PHE A CA    1 
ATOM   2747  C C     . PHE D 4 175  ? 148.209 131.186 157.926 1.00 62.49  ? 172  PHE A C     1 
ATOM   2748  O O     . PHE D 4 175  ? 148.214 130.027 157.493 1.00 60.51  ? 172  PHE A O     1 
ATOM   2749  C CB    . PHE D 4 175  ? 150.480 132.183 158.319 1.00 67.89  ? 172  PHE A CB    1 
ATOM   2750  C CG    . PHE D 4 175  ? 150.990 130.805 158.645 1.00 69.08  ? 172  PHE A CG    1 
ATOM   2751  C CD1   . PHE D 4 175  ? 151.717 130.080 157.714 1.00 68.91  ? 172  PHE A CD1   1 
ATOM   2752  C CD2   . PHE D 4 175  ? 150.755 130.240 159.889 1.00 69.15  ? 172  PHE A CD2   1 
ATOM   2753  C CE1   . PHE D 4 175  ? 152.188 128.815 158.014 1.00 68.25  ? 172  PHE A CE1   1 
ATOM   2754  C CE2   . PHE D 4 175  ? 151.223 128.976 160.194 1.00 68.95  ? 172  PHE A CE2   1 
ATOM   2755  C CZ    . PHE D 4 175  ? 151.942 128.263 159.254 1.00 69.03  ? 172  PHE A CZ    1 
ATOM   2756  N N     . TYR D 4 176  ? 147.327 131.607 158.838 1.00 60.81  ? 173  TYR A N     1 
ATOM   2757  C CA    . TYR D 4 176  ? 146.263 130.719 159.298 1.00 58.36  ? 173  TYR A CA    1 
ATOM   2758  C C     . TYR D 4 176  ? 145.357 130.307 158.147 1.00 53.40  ? 173  TYR A C     1 
ATOM   2759  O O     . TYR D 4 176  ? 144.899 129.161 158.087 1.00 50.06  ? 173  TYR A O     1 
ATOM   2760  C CB    . TYR D 4 176  ? 145.445 131.393 160.401 1.00 60.04  ? 173  TYR A CB    1 
ATOM   2761  C CG    . TYR D 4 176  ? 146.139 131.469 161.743 1.00 63.74  ? 173  TYR A CG    1 
ATOM   2762  C CD1   . TYR D 4 176  ? 147.094 130.529 162.108 1.00 65.55  ? 173  TYR A CD1   1 
ATOM   2763  C CD2   . TYR D 4 176  ? 145.834 132.477 162.648 1.00 64.67  ? 173  TYR A CD2   1 
ATOM   2764  C CE1   . TYR D 4 176  ? 147.729 130.594 163.334 1.00 67.78  ? 173  TYR A CE1   1 
ATOM   2765  C CE2   . TYR D 4 176  ? 146.464 132.552 163.877 1.00 66.57  ? 173  TYR A CE2   1 
ATOM   2766  C CZ    . TYR D 4 176  ? 147.410 131.607 164.214 1.00 69.82  ? 173  TYR A CZ    1 
ATOM   2767  O OH    . TYR D 4 176  ? 148.040 131.677 165.435 1.00 75.30  ? 173  TYR A OH    1 
ATOM   2768  N N     . GLU D 4 177  ? 145.083 131.232 157.223 1.00 54.59  ? 174  GLU A N     1 
ATOM   2769  C CA    . GLU D 4 177  ? 144.252 130.902 156.070 1.00 55.64  ? 174  GLU A CA    1 
ATOM   2770  C C     . GLU D 4 177  ? 144.966 129.938 155.130 1.00 53.07  ? 174  GLU A C     1 
ATOM   2771  O O     . GLU D 4 177  ? 144.338 129.036 154.561 1.00 49.50  ? 174  GLU A O     1 
ATOM   2772  C CB    . GLU D 4 177  ? 143.852 132.179 155.331 1.00 59.70  ? 174  GLU A CB    1 
ATOM   2773  C CG    . GLU D 4 177  ? 142.807 133.006 156.057 1.00 64.70  ? 174  GLU A CG    1 
ATOM   2774  C CD    . GLU D 4 177  ? 141.459 132.316 156.112 1.00 67.31  ? 174  GLU A CD    1 
ATOM   2775  O OE1   . GLU D 4 177  ? 141.143 131.549 155.177 1.00 67.21  ? 174  GLU A OE1   1 
ATOM   2776  O OE2   . GLU D 4 177  ? 140.716 132.536 157.091 1.00 68.49  ? 174  GLU A OE2   1 
ATOM   2777  N N     . ASN D 4 178  ? 146.278 130.111 154.959 1.00 53.77  ? 175  ASN A N     1 
ATOM   2778  C CA    . ASN D 4 178  ? 147.034 129.211 154.094 1.00 52.60  ? 175  ASN A CA    1 
ATOM   2779  C C     . ASN D 4 178  ? 147.048 127.790 154.641 1.00 54.41  ? 175  ASN A C     1 
ATOM   2780  O O     . ASN D 4 178  ? 147.124 126.828 153.867 1.00 54.14  ? 175  ASN A O     1 
ATOM   2781  C CB    . ASN D 4 178  ? 148.460 129.729 153.923 1.00 54.12  ? 175  ASN A CB    1 
ATOM   2782  C CG    . ASN D 4 178  ? 148.504 131.128 153.344 1.00 55.02  ? 175  ASN A CG    1 
ATOM   2783  O OD1   . ASN D 4 178  ? 149.166 132.013 153.884 1.00 58.84  ? 175  ASN A OD1   1 
ATOM   2784  N ND2   . ASN D 4 178  ? 147.809 131.331 152.231 1.00 52.67  ? 175  ASN A ND2   1 
ATOM   2785  N N     . ARG D 4 179  ? 146.970 127.636 155.965 1.00 57.14  ? 176  ARG A N     1 
ATOM   2786  C CA    . ARG D 4 179  ? 146.939 126.303 156.551 1.00 60.11  ? 176  ARG A CA    1 
ATOM   2787  C C     . ARG D 4 179  ? 145.534 125.713 156.559 1.00 62.20  ? 176  ARG A C     1 
ATOM   2788  O O     . ARG D 4 179  ? 145.386 124.485 156.547 1.00 64.76  ? 176  ARG A O     1 
ATOM   2789  C CB    . ARG D 4 179  ? 147.516 126.339 157.966 1.00 61.46  ? 176  ARG A CB    1 
ATOM   2790  C CG    . ARG D 4 179  ? 149.028 126.484 157.990 1.00 61.19  ? 176  ARG A CG    1 
ATOM   2791  C CD    . ARG D 4 179  ? 149.687 125.357 157.207 1.00 58.79  ? 176  ARG A CD    1 
ATOM   2792  N NE    . ARG D 4 179  ? 151.117 125.577 157.006 1.00 57.40  ? 176  ARG A NE    1 
ATOM   2793  C CZ    . ARG D 4 179  ? 151.641 126.155 155.929 1.00 56.21  ? 176  ARG A CZ    1 
ATOM   2794  N NH1   . ARG D 4 179  ? 150.854 126.576 154.949 1.00 57.40  ? 176  ARG A NH1   1 
ATOM   2795  N NH2   . ARG D 4 179  ? 152.955 126.312 155.833 1.00 53.53  ? 176  ARG A NH2   1 
ATOM   2796  N N     . LYS D 4 180  ? 144.498 126.555 156.582 1.00 61.87  ? 177  LYS A N     1 
ATOM   2797  C CA    . LYS D 4 180  ? 143.151 126.044 156.356 1.00 60.62  ? 177  LYS A CA    1 
ATOM   2798  C C     . LYS D 4 180  ? 142.995 125.524 154.935 1.00 58.13  ? 177  LYS A C     1 
ATOM   2799  O O     . LYS D 4 180  ? 142.251 124.564 154.703 1.00 57.87  ? 177  LYS A O     1 
ATOM   2800  C CB    . LYS D 4 180  ? 142.105 127.123 156.636 1.00 62.74  ? 177  LYS A CB    1 
ATOM   2801  C CG    . LYS D 4 180  ? 142.059 127.612 158.071 1.00 67.60  ? 177  LYS A CG    1 
ATOM   2802  C CD    . LYS D 4 180  ? 140.645 128.017 158.454 1.00 69.76  ? 177  LYS A CD    1 
ATOM   2803  C CE    . LYS D 4 180  ? 140.636 129.201 159.404 1.00 70.84  ? 177  LYS A CE    1 
ATOM   2804  N NZ    . LYS D 4 180  ? 141.040 130.455 158.708 1.00 70.07  ? 177  LYS A NZ    1 
ATOM   2805  N N     . ASN D 4 181  ? 143.691 126.138 153.975 1.00 53.03  ? 178  ASN A N     1 
ATOM   2806  C CA    . ASN D 4 181  ? 143.671 125.652 152.601 1.00 51.79  ? 178  ASN A CA    1 
ATOM   2807  C C     . ASN D 4 181  ? 144.321 124.284 152.462 1.00 51.12  ? 178  ASN A C     1 
ATOM   2808  O O     . ASN D 4 181  ? 144.096 123.607 151.455 1.00 49.58  ? 178  ASN A O     1 
ATOM   2809  C CB    . ASN D 4 181  ? 144.374 126.648 151.678 1.00 49.23  ? 178  ASN A CB    1 
ATOM   2810  C CG    . ASN D 4 181  ? 143.690 127.998 151.650 1.00 41.02  ? 178  ASN A CG    1 
ATOM   2811  O OD1   . ASN D 4 181  ? 142.492 128.106 151.911 1.00 47.20  ? 178  ASN A OD1   1 
ATOM   2812  N ND2   . ASN D 4 181  ? 144.449 129.040 151.329 1.00 40.88  ? 178  ASN A ND2   1 
ATOM   2813  N N     . VAL D 4 182  ? 145.120 123.865 153.444 1.00 52.49  ? 179  VAL A N     1 
ATOM   2814  C CA    . VAL D 4 182  ? 145.772 122.562 153.375 1.00 49.03  ? 179  VAL A CA    1 
ATOM   2815  C C     . VAL D 4 182  ? 144.824 121.457 153.824 1.00 51.77  ? 179  VAL A C     1 
ATOM   2816  O O     . VAL D 4 182  ? 144.785 120.376 153.224 1.00 52.43  ? 179  VAL A O     1 
ATOM   2817  C CB    . VAL D 4 182  ? 147.064 122.575 154.212 1.00 47.28  ? 179  VAL A CB    1 
ATOM   2818  C CG1   . VAL D 4 182  ? 147.701 121.194 154.236 1.00 46.11  ? 179  VAL A CG1   1 
ATOM   2819  C CG2   . VAL D 4 182  ? 148.039 123.608 153.669 1.00 44.97  ? 179  VAL A CG2   1 
ATOM   2820  N N     . PHE D 4 183  ? 144.046 121.706 154.875 1.00 52.46  ? 180  PHE A N     1 
ATOM   2821  C CA    . PHE D 4 183  ? 143.144 120.711 155.438 1.00 52.58  ? 180  PHE A CA    1 
ATOM   2822  C C     . PHE D 4 183  ? 141.713 120.850 154.937 1.00 52.59  ? 180  PHE A C     1 
ATOM   2823  O O     . PHE D 4 183  ? 140.851 120.066 155.345 1.00 54.53  ? 180  PHE A O     1 
ATOM   2824  C CB    . PHE D 4 183  ? 143.157 120.795 156.970 1.00 53.74  ? 180  PHE A CB    1 
ATOM   2825  C CG    . PHE D 4 183  ? 144.472 120.412 157.587 1.00 53.51  ? 180  PHE A CG    1 
ATOM   2826  C CD1   . PHE D 4 183  ? 145.486 121.346 157.731 1.00 53.04  ? 180  PHE A CD1   1 
ATOM   2827  C CD2   . PHE D 4 183  ? 144.693 119.119 158.033 1.00 55.35  ? 180  PHE A CD2   1 
ATOM   2828  C CE1   . PHE D 4 183  ? 146.695 120.996 158.300 1.00 54.23  ? 180  PHE A CE1   1 
ATOM   2829  C CE2   . PHE D 4 183  ? 145.900 118.763 158.605 1.00 57.39  ? 180  PHE A CE2   1 
ATOM   2830  C CZ    . PHE D 4 183  ? 146.902 119.702 158.739 1.00 52.39  ? 180  PHE A CZ    1 
ATOM   2831  N N     . SER D 4 184  ? 141.441 121.821 154.068 1.00 52.07  ? 181  SER A N     1 
ATOM   2832  C CA    . SER D 4 184  ? 140.084 122.048 153.593 1.00 50.03  ? 181  SER A CA    1 
ATOM   2833  C C     . SER D 4 184  ? 139.571 120.847 152.809 1.00 51.68  ? 181  SER A C     1 
ATOM   2834  O O     . SER D 4 184  ? 140.333 120.118 152.170 1.00 52.15  ? 181  SER A O     1 
ATOM   2835  C CB    . SER D 4 184  ? 140.031 123.301 152.717 1.00 47.24  ? 181  SER A CB    1 
ATOM   2836  O OG    . SER D 4 184  ? 138.753 123.457 152.124 1.00 46.86  ? 181  SER A OG    1 
ATOM   2837  N N     . ALA D 4 185  ? 138.257 120.643 152.868 1.00 53.19  ? 182  ALA A N     1 
ATOM   2838  C CA    . ALA D 4 185  ? 137.597 119.604 152.091 1.00 53.44  ? 182  ALA A CA    1 
ATOM   2839  C C     . ALA D 4 185  ? 137.054 120.120 150.767 1.00 53.95  ? 182  ALA A C     1 
ATOM   2840  O O     . ALA D 4 185  ? 136.520 119.329 149.983 1.00 55.53  ? 182  ALA A O     1 
ATOM   2841  C CB    . ALA D 4 185  ? 136.461 118.977 152.902 1.00 52.24  ? 182  ALA A CB    1 
ATOM   2842  N N     . GLU D 4 186  ? 137.177 121.416 150.501 1.00 54.32  ? 183  GLU A N     1 
ATOM   2843  C CA    . GLU D 4 186  ? 136.674 121.986 149.262 1.00 55.61  ? 183  GLU A CA    1 
ATOM   2844  C C     . GLU D 4 186  ? 137.515 121.513 148.077 1.00 52.94  ? 183  GLU A C     1 
ATOM   2845  O O     . GLU D 4 186  ? 138.596 120.937 148.227 1.00 50.73  ? 183  GLU A O     1 
ATOM   2846  C CB    . GLU D 4 186  ? 136.674 123.513 149.340 1.00 59.72  ? 183  GLU A CB    1 
ATOM   2847  C CG    . GLU D 4 186  ? 135.782 124.071 150.432 1.00 65.56  ? 183  GLU A CG    1 
ATOM   2848  C CD    . GLU D 4 186  ? 134.314 123.785 150.183 1.00 72.08  ? 183  GLU A CD    1 
ATOM   2849  O OE1   . GLU D 4 186  ? 133.915 123.717 149.002 1.00 75.13  ? 183  GLU A OE1   1 
ATOM   2850  O OE2   . GLU D 4 186  ? 133.562 123.624 151.166 1.00 74.22  ? 183  GLU A OE2   1 
ATOM   2851  N N     . ASP D 4 187  ? 136.997 121.772 146.875 1.00 52.32  ? 184  ASP A N     1 
ATOM   2852  C CA    . ASP D 4 187  ? 137.662 121.371 145.636 1.00 50.47  ? 184  ASP A CA    1 
ATOM   2853  C C     . ASP D 4 187  ? 138.712 122.419 145.265 1.00 47.17  ? 184  ASP A C     1 
ATOM   2854  O O     . ASP D 4 187  ? 138.623 123.124 144.257 1.00 45.93  ? 184  ASP A O     1 
ATOM   2855  C CB    . ASP D 4 187  ? 136.640 121.175 144.525 1.00 51.81  ? 184  ASP A CB    1 
ATOM   2856  C CG    . ASP D 4 187  ? 137.262 120.653 143.247 1.00 53.38  ? 184  ASP A CG    1 
ATOM   2857  O OD1   . ASP D 4 187  ? 138.336 120.023 143.324 1.00 53.32  ? 184  ASP A OD1   1 
ATOM   2858  O OD2   . ASP D 4 187  ? 136.675 120.871 142.166 1.00 55.72  ? 184  ASP A OD2   1 
ATOM   2859  N N     . ILE D 4 188  ? 139.731 122.514 146.118 1.00 46.62  ? 185  ILE A N     1 
ATOM   2860  C CA    . ILE D 4 188  ? 140.838 123.444 145.933 1.00 44.22  ? 185  ILE A CA    1 
ATOM   2861  C C     . ILE D 4 188  ? 142.135 122.650 145.896 1.00 46.68  ? 185  ILE A C     1 
ATOM   2862  O O     . ILE D 4 188  ? 142.324 121.713 146.681 1.00 49.42  ? 185  ILE A O     1 
ATOM   2863  C CB    . ILE D 4 188  ? 140.873 124.520 147.039 1.00 42.86  ? 185  ILE A CB    1 
ATOM   2864  C CG1   . ILE D 4 188  ? 141.016 123.879 148.420 1.00 46.57  ? 185  ILE A CG1   1 
ATOM   2865  C CG2   . ILE D 4 188  ? 139.614 125.373 146.987 1.00 39.40  ? 185  ILE A CG2   1 
ATOM   2866  C CD1   . ILE D 4 188  ? 141.051 124.879 149.554 1.00 39.19  ? 185  ILE A CD1   1 
ATOM   2867  N N     . SER D 4 189  ? 143.029 123.025 144.978 1.00 45.17  ? 186  SER A N     1 
ATOM   2868  C CA    . SER D 4 189  ? 144.245 122.254 144.749 1.00 42.99  ? 186  SER A CA    1 
ATOM   2869  C C     . SER D 4 189  ? 145.278 122.411 145.856 1.00 42.86  ? 186  SER A C     1 
ATOM   2870  O O     . SER D 4 189  ? 146.252 121.650 145.882 1.00 44.80  ? 186  SER A O     1 
ATOM   2871  C CB    . SER D 4 189  ? 144.856 122.647 143.403 1.00 35.22  ? 186  SER A CB    1 
ATOM   2872  O OG    . SER D 4 189  ? 144.692 124.031 143.164 1.00 34.87  ? 186  SER A OG    1 
ATOM   2873  N N     . THR D 4 190  ? 145.096 123.361 146.771 1.00 42.71  ? 187  THR A N     1 
ATOM   2874  C CA    . THR D 4 190  ? 146.017 123.517 147.888 1.00 43.97  ? 187  THR A CA    1 
ATOM   2875  C C     . THR D 4 190  ? 145.809 122.479 148.983 1.00 45.91  ? 187  THR A C     1 
ATOM   2876  O O     . THR D 4 190  ? 146.622 122.412 149.910 1.00 52.52  ? 187  THR A O     1 
ATOM   2877  C CB    . THR D 4 190  ? 145.879 124.916 148.495 1.00 38.89  ? 187  THR A CB    1 
ATOM   2878  O OG1   . THR D 4 190  ? 144.509 125.149 148.850 1.00 38.93  ? 187  THR A OG1   1 
ATOM   2879  C CG2   . THR D 4 190  ? 146.326 125.978 147.505 1.00 41.00  ? 187  THR A CG2   1 
ATOM   2880  N N     . ALA D 4 191  ? 144.760 121.668 148.897 1.00 42.48  ? 188  ALA A N     1 
ATOM   2881  C CA    . ALA D 4 191  ? 144.326 120.834 150.006 1.00 43.86  ? 188  ALA A CA    1 
ATOM   2882  C C     . ALA D 4 191  ? 144.840 119.404 149.880 1.00 47.01  ? 188  ALA A C     1 
ATOM   2883  O O     . ALA D 4 191  ? 145.169 118.922 148.793 1.00 48.54  ? 188  ALA A O     1 
ATOM   2884  C CB    . ALA D 4 191  ? 142.799 120.829 150.108 1.00 44.48  ? 188  ALA A CB    1 
ATOM   2885  N N     . ILE D 4 192  ? 144.895 118.730 151.025 1.00 47.89  ? 189  ILE A N     1 
ATOM   2886  C CA    . ILE D 4 192  ? 145.312 117.333 151.118 1.00 47.84  ? 189  ILE A CA    1 
ATOM   2887  C C     . ILE D 4 192  ? 144.218 116.409 150.585 1.00 50.65  ? 189  ILE A C     1 
ATOM   2888  O O     . ILE D 4 192  ? 144.533 115.493 149.810 1.00 51.63  ? 189  ILE A O     1 
ATOM   2889  C CB    . ILE D 4 192  ? 145.703 116.970 152.562 1.00 46.17  ? 189  ILE A CB    1 
ATOM   2890  C CG1   . ILE D 4 192  ? 146.981 117.706 152.968 1.00 46.62  ? 189  ILE A CG1   1 
ATOM   2891  C CG2   . ILE D 4 192  ? 145.875 115.467 152.714 1.00 46.31  ? 189  ILE A CG2   1 
ATOM   2892  C CD1   . ILE D 4 192  ? 147.450 117.386 154.370 1.00 50.06  ? 189  ILE A CD1   1 
ATOM   2893  N N     . PRO D 4 193  ? 142.938 116.578 150.959 1.00 51.02  ? 190  PRO A N     1 
ATOM   2894  C CA    . PRO D 4 193  ? 141.909 115.700 150.370 1.00 51.20  ? 190  PRO A CA    1 
ATOM   2895  C C     . PRO D 4 193  ? 141.831 115.787 148.856 1.00 51.02  ? 190  PRO A C     1 
ATOM   2896  O O     . PRO D 4 193  ? 141.629 114.764 148.192 1.00 51.30  ? 190  PRO A O     1 
ATOM   2897  C CB    . PRO D 4 193  ? 140.615 116.185 151.036 1.00 52.45  ? 190  PRO A CB    1 
ATOM   2898  C CG    . PRO D 4 193  ? 141.056 116.772 152.319 1.00 53.13  ? 190  PRO A CG    1 
ATOM   2899  C CD    . PRO D 4 193  ? 142.361 117.437 152.010 1.00 52.18  ? 190  PRO A CD    1 
ATOM   2900  N N     . HIS D 4 194  ? 141.991 116.988 148.289 1.00 50.66  ? 191  HIS A N     1 
ATOM   2901  C CA    . HIS D 4 194  ? 141.963 117.124 146.835 1.00 47.97  ? 191  HIS A CA    1 
ATOM   2902  C C     . HIS D 4 194  ? 143.148 116.414 146.188 1.00 46.90  ? 191  HIS A C     1 
ATOM   2903  O O     . HIS D 4 194  ? 142.996 115.766 145.145 1.00 47.43  ? 191  HIS A O     1 
ATOM   2904  C CB    . HIS D 4 194  ? 141.950 118.600 146.445 1.00 47.26  ? 191  HIS A CB    1 
ATOM   2905  C CG    . HIS D 4 194  ? 142.180 118.840 144.986 1.00 48.28  ? 191  HIS A CG    1 
ATOM   2906  N ND1   . HIS D 4 194  ? 143.437 118.996 144.445 1.00 50.95  ? 191  HIS A ND1   1 
ATOM   2907  C CD2   . HIS D 4 194  ? 141.309 118.967 143.955 1.00 46.40  ? 191  HIS A CD2   1 
ATOM   2908  C CE1   . HIS D 4 194  ? 143.334 119.198 143.144 1.00 48.86  ? 191  HIS A CE1   1 
ATOM   2909  N NE2   . HIS D 4 194  ? 142.053 119.186 142.821 1.00 46.58  ? 191  HIS A NE2   1 
ATOM   2910  N N     . ARG D 4 195  ? 144.335 116.533 146.788 1.00 44.20  ? 192  ARG A N     1 
ATOM   2911  C CA    . ARG D 4 195  ? 145.509 115.849 146.257 1.00 42.29  ? 192  ARG A CA    1 
ATOM   2912  C C     . ARG D 4 195  ? 145.323 114.338 146.259 1.00 42.52  ? 192  ARG A C     1 
ATOM   2913  O O     . ARG D 4 195  ? 145.800 113.650 145.348 1.00 44.01  ? 192  ARG A O     1 
ATOM   2914  C CB    . ARG D 4 195  ? 146.746 116.242 147.069 1.00 42.33  ? 192  ARG A CB    1 
ATOM   2915  C CG    . ARG D 4 195  ? 148.026 115.501 146.706 1.00 43.26  ? 192  ARG A CG    1 
ATOM   2916  C CD    . ARG D 4 195  ? 148.376 115.650 145.232 1.00 43.42  ? 192  ARG A CD    1 
ATOM   2917  N NE    . ARG D 4 195  ? 148.448 117.048 144.809 1.00 43.74  ? 192  ARG A NE    1 
ATOM   2918  C CZ    . ARG D 4 195  ? 149.561 117.775 144.815 1.00 37.72  ? 192  ARG A CZ    1 
ATOM   2919  N NH1   . ARG D 4 195  ? 150.703 117.240 145.224 1.00 57.88  ? 192  ARG A NH1   1 
ATOM   2920  N NH2   . ARG D 4 195  ? 149.533 119.036 144.412 1.00 37.06  ? 192  ARG A NH2   1 
ATOM   2921  N N     . ILE D 4 196  ? 144.618 113.803 147.253 1.00 42.60  ? 193  ILE A N     1 
ATOM   2922  C CA    . ILE D 4 196  ? 144.428 112.358 147.344 1.00 44.76  ? 193  ILE A CA    1 
ATOM   2923  C C     . ILE D 4 196  ? 143.368 111.887 146.358 1.00 46.28  ? 193  ILE A C     1 
ATOM   2924  O O     . ILE D 4 196  ? 143.552 110.890 145.652 1.00 48.93  ? 193  ILE A O     1 
ATOM   2925  C CB    . ILE D 4 196  ? 144.071 111.959 148.786 1.00 47.51  ? 193  ILE A CB    1 
ATOM   2926  C CG1   . ILE D 4 196  ? 145.254 112.219 149.718 1.00 47.66  ? 193  ILE A CG1   1 
ATOM   2927  C CG2   . ILE D 4 196  ? 143.636 110.500 148.850 1.00 50.84  ? 193  ILE A CG2   1 
ATOM   2928  C CD1   . ILE D 4 196  ? 144.977 111.882 151.169 1.00 49.08  ? 193  ILE A CD1   1 
ATOM   2929  N N     . VAL D 4 197  ? 142.243 112.601 146.289 1.00 45.11  ? 194  VAL A N     1 
ATOM   2930  C CA    . VAL D 4 197  ? 141.098 112.115 145.530 1.00 45.99  ? 194  VAL A CA    1 
ATOM   2931  C C     . VAL D 4 197  ? 141.238 112.433 144.045 1.00 46.95  ? 194  VAL A C     1 
ATOM   2932  O O     . VAL D 4 197  ? 140.988 111.576 143.192 1.00 51.34  ? 194  VAL A O     1 
ATOM   2933  C CB    . VAL D 4 197  ? 139.800 112.698 146.117 1.00 47.44  ? 194  VAL A CB    1 
ATOM   2934  C CG1   . VAL D 4 197  ? 138.602 112.274 145.284 1.00 46.92  ? 194  VAL A CG1   1 
ATOM   2935  C CG2   . VAL D 4 197  ? 139.632 112.263 147.566 1.00 49.10  ? 194  VAL A CG2   1 
ATOM   2936  N N     . GLN D 4 198  ? 141.640 113.658 143.705 1.00 45.02  ? 195  GLN A N     1 
ATOM   2937  C CA    . GLN D 4 198  ? 141.562 114.127 142.329 1.00 45.99  ? 195  GLN A CA    1 
ATOM   2938  C C     . GLN D 4 198  ? 142.907 114.236 141.623 1.00 51.42  ? 195  GLN A C     1 
ATOM   2939  O O     . GLN D 4 198  ? 142.928 114.501 140.416 1.00 54.12  ? 195  GLN A O     1 
ATOM   2940  C CB    . GLN D 4 198  ? 140.856 115.490 142.282 1.00 42.70  ? 195  GLN A CB    1 
ATOM   2941  C CG    . GLN D 4 198  ? 139.497 115.487 142.964 1.00 42.95  ? 195  GLN A CG    1 
ATOM   2942  C CD    . GLN D 4 198  ? 138.860 116.859 143.013 1.00 43.57  ? 195  GLN A CD    1 
ATOM   2943  O OE1   . GLN D 4 198  ? 138.343 117.277 144.048 1.00 42.98  ? 195  GLN A OE1   1 
ATOM   2944  N NE2   . GLN D 4 198  ? 138.887 117.566 141.889 1.00 44.95  ? 195  GLN A NE2   1 
ATOM   2945  N N     . ASP D 4 199  ? 144.022 114.035 142.325 1.00 52.81  ? 196  ASP A N     1 
ATOM   2946  C CA    . ASP D 4 199  ? 145.343 114.110 141.714 1.00 53.13  ? 196  ASP A CA    1 
ATOM   2947  C C     . ASP D 4 199  ? 146.033 112.753 141.664 1.00 52.75  ? 196  ASP A C     1 
ATOM   2948  O O     . ASP D 4 199  ? 146.390 112.282 140.581 1.00 53.41  ? 196  ASP A O     1 
ATOM   2949  C CB    . ASP D 4 199  ? 146.220 115.123 142.464 1.00 57.35  ? 196  ASP A CB    1 
ATOM   2950  C CG    . ASP D 4 199  ? 146.035 116.542 141.960 1.00 61.57  ? 196  ASP A CG    1 
ATOM   2951  O OD1   . ASP D 4 199  ? 145.668 116.714 140.779 1.00 61.13  ? 196  ASP A OD1   1 
ATOM   2952  O OD2   . ASP D 4 199  ? 146.270 117.488 142.743 1.00 63.77  ? 196  ASP A OD2   1 
ATOM   2953  N N     . ASN D 4 200  ? 146.226 112.103 142.813 1.00 52.35  ? 197  ASN A N     1 
ATOM   2954  C CA    . ASN D 4 200  ? 147.042 110.893 142.843 1.00 50.77  ? 197  ASN A CA    1 
ATOM   2955  C C     . ASN D 4 200  ? 146.245 109.647 142.471 1.00 50.48  ? 197  ASN A C     1 
ATOM   2956  O O     . ASN D 4 200  ? 146.774 108.758 141.794 1.00 50.23  ? 197  ASN A O     1 
ATOM   2957  C CB    . ASN D 4 200  ? 147.682 110.727 144.222 1.00 49.95  ? 197  ASN A CB    1 
ATOM   2958  C CG    . ASN D 4 200  ? 148.874 111.643 144.423 1.00 46.83  ? 197  ASN A CG    1 
ATOM   2959  O OD1   . ASN D 4 200  ? 149.430 112.175 143.461 1.00 40.29  ? 197  ASN A OD1   1 
ATOM   2960  N ND2   . ASN D 4 200  ? 149.281 111.821 145.675 1.00 46.84  ? 197  ASN A ND2   1 
ATOM   2961  N N     . PHE D 4 201  ? 144.986 109.553 142.901 1.00 49.23  ? 198  PHE A N     1 
ATOM   2962  C CA    . PHE D 4 201  ? 144.219 108.341 142.615 1.00 50.96  ? 198  PHE A CA    1 
ATOM   2963  C C     . PHE D 4 201  ? 143.977 108.129 141.125 1.00 48.80  ? 198  PHE A C     1 
ATOM   2964  O O     . PHE D 4 201  ? 144.154 106.992 140.654 1.00 48.44  ? 198  PHE A O     1 
ATOM   2965  C CB    . PHE D 4 201  ? 142.899 108.344 143.392 1.00 51.80  ? 198  PHE A CB    1 
ATOM   2966  C CG    . PHE D 4 201  ? 142.010 107.178 143.061 1.00 53.76  ? 198  PHE A CG    1 
ATOM   2967  C CD1   . PHE D 4 201  ? 142.295 105.914 143.550 1.00 55.29  ? 198  PHE A CD1   1 
ATOM   2968  C CD2   . PHE D 4 201  ? 140.903 107.341 142.244 1.00 55.12  ? 198  PHE A CD2   1 
ATOM   2969  C CE1   . PHE D 4 201  ? 141.488 104.836 143.239 1.00 57.04  ? 198  PHE A CE1   1 
ATOM   2970  C CE2   . PHE D 4 201  ? 140.089 106.266 141.932 1.00 56.41  ? 198  PHE A CE2   1 
ATOM   2971  C CZ    . PHE D 4 201  ? 140.381 105.012 142.431 1.00 57.31  ? 198  PHE A CZ    1 
ATOM   2972  N N     . PRO D 4 202  ? 143.565 109.130 140.335 1.00 45.03  ? 199  PRO A N     1 
ATOM   2973  C CA    . PRO D 4 202  ? 143.500 108.906 138.880 1.00 43.90  ? 199  PRO A CA    1 
ATOM   2974  C C     . PRO D 4 202  ? 144.831 108.484 138.285 1.00 44.03  ? 199  PRO A C     1 
ATOM   2975  O O     . PRO D 4 202  ? 144.850 107.738 137.297 1.00 44.03  ? 199  PRO A O     1 
ATOM   2976  C CB    . PRO D 4 202  ? 143.037 110.266 138.338 1.00 40.33  ? 199  PRO A CB    1 
ATOM   2977  C CG    . PRO D 4 202  ? 142.279 110.868 139.459 1.00 39.75  ? 199  PRO A CG    1 
ATOM   2978  C CD    . PRO D 4 202  ? 143.008 110.447 140.702 1.00 42.11  ? 199  PRO A CD    1 
ATOM   2979  N N     . LYS D 4 203  ? 145.947 108.938 138.859 1.00 41.78  ? 200  LYS A N     1 
ATOM   2980  C CA    . LYS D 4 203  ? 147.251 108.442 138.435 1.00 41.65  ? 200  LYS A CA    1 
ATOM   2981  C C     . LYS D 4 203  ? 147.450 106.997 138.870 1.00 46.11  ? 200  LYS A C     1 
ATOM   2982  O O     . LYS D 4 203  ? 147.889 106.154 138.077 1.00 47.39  ? 200  LYS A O     1 
ATOM   2983  C CB    . LYS D 4 203  ? 148.361 109.333 139.000 1.00 40.83  ? 200  LYS A CB    1 
ATOM   2984  C CG    . LYS D 4 203  ? 148.309 110.772 138.513 1.00 41.28  ? 200  LYS A CG    1 
ATOM   2985  C CD    . LYS D 4 203  ? 149.391 111.619 139.165 1.00 40.85  ? 200  LYS A CD    1 
ATOM   2986  C CE    . LYS D 4 203  ? 149.277 113.077 138.745 1.00 41.63  ? 200  LYS A CE    1 
ATOM   2987  N NZ    . LYS D 4 203  ? 149.346 113.237 137.264 1.00 44.33  ? 200  LYS A NZ    1 
ATOM   2988  N N     . PHE D 4 204  ? 147.127 106.689 140.128 1.00 47.99  ? 201  PHE A N     1 
ATOM   2989  C CA    . PHE D 4 204  ? 147.265 105.319 140.612 1.00 46.10  ? 201  PHE A CA    1 
ATOM   2990  C C     . PHE D 4 204  ? 146.292 104.381 139.904 1.00 46.55  ? 201  PHE A C     1 
ATOM   2991  O O     . PHE D 4 204  ? 146.651 103.248 139.567 1.00 46.01  ? 201  PHE A O     1 
ATOM   2992  C CB    . PHE D 4 204  ? 147.051 105.272 142.125 1.00 43.93  ? 201  PHE A CB    1 
ATOM   2993  C CG    . PHE D 4 204  ? 147.092 103.885 142.697 1.00 46.69  ? 201  PHE A CG    1 
ATOM   2994  C CD1   . PHE D 4 204  ? 148.302 103.271 142.969 1.00 48.40  ? 201  PHE A CD1   1 
ATOM   2995  C CD2   . PHE D 4 204  ? 145.920 103.196 142.965 1.00 48.37  ? 201  PHE A CD2   1 
ATOM   2996  C CE1   . PHE D 4 204  ? 148.342 101.993 143.493 1.00 49.32  ? 201  PHE A CE1   1 
ATOM   2997  C CE2   . PHE D 4 204  ? 145.956 101.918 143.488 1.00 48.68  ? 201  PHE A CE2   1 
ATOM   2998  C CZ    . PHE D 4 204  ? 147.168 101.318 143.754 1.00 48.93  ? 201  PHE A CZ    1 
ATOM   2999  N N     . LYS D 4 205  ? 145.059 104.838 139.679 1.00 47.92  ? 202  LYS A N     1 
ATOM   3000  C CA    . LYS D 4 205  ? 144.081 104.026 138.960 1.00 50.01  ? 202  LYS A CA    1 
ATOM   3001  C C     . LYS D 4 205  ? 144.548 103.729 137.539 1.00 50.96  ? 202  LYS A C     1 
ATOM   3002  O O     . LYS D 4 205  ? 144.365 102.614 137.037 1.00 51.99  ? 202  LYS A O     1 
ATOM   3003  C CB    . LYS D 4 205  ? 142.728 104.737 138.952 1.00 49.07  ? 202  LYS A CB    1 
ATOM   3004  C CG    . LYS D 4 205  ? 141.707 104.163 137.990 1.00 47.14  ? 202  LYS A CG    1 
ATOM   3005  C CD    . LYS D 4 205  ? 140.432 104.989 138.014 1.00 44.43  ? 202  LYS A CD    1 
ATOM   3006  C CE    . LYS D 4 205  ? 139.540 104.665 136.832 1.00 45.83  ? 202  LYS A CE    1 
ATOM   3007  N NZ    . LYS D 4 205  ? 139.112 103.240 136.819 1.00 49.36  ? 202  LYS A NZ    1 
ATOM   3008  N N     . GLU D 4 206  ? 145.161 104.715 136.879 1.00 50.24  ? 203  GLU A N     1 
ATOM   3009  C CA    . GLU D 4 206  ? 145.718 104.477 135.551 1.00 48.73  ? 203  GLU A CA    1 
ATOM   3010  C C     . GLU D 4 206  ? 146.903 103.521 135.604 1.00 48.01  ? 203  GLU A C     1 
ATOM   3011  O O     . GLU D 4 206  ? 147.089 102.717 134.685 1.00 47.75  ? 203  GLU A O     1 
ATOM   3012  C CB    . GLU D 4 206  ? 146.129 105.804 134.912 1.00 48.35  ? 203  GLU A CB    1 
ATOM   3013  C CG    . GLU D 4 206  ? 146.833 105.674 133.568 1.00 51.03  ? 203  GLU A CG    1 
ATOM   3014  C CD    . GLU D 4 206  ? 145.933 105.123 132.476 1.00 55.86  ? 203  GLU A CD    1 
ATOM   3015  O OE1   . GLU D 4 206  ? 144.695 105.161 132.637 1.00 59.20  ? 203  GLU A OE1   1 
ATOM   3016  O OE2   . GLU D 4 206  ? 146.466 104.652 131.448 1.00 56.88  ? 203  GLU A OE2   1 
ATOM   3017  N N     . ASN D 4 207  ? 147.703 103.582 136.672 1.00 49.86  ? 204  ASN A N     1 
ATOM   3018  C CA    . ASN D 4 207  ? 148.842 102.676 136.795 1.00 49.74  ? 204  ASN A CA    1 
ATOM   3019  C C     . ASN D 4 207  ? 148.388 101.223 136.862 1.00 50.71  ? 204  ASN A C     1 
ATOM   3020  O O     . ASN D 4 207  ? 149.027 100.339 136.281 1.00 51.39  ? 204  ASN A O     1 
ATOM   3021  C CB    . ASN D 4 207  ? 149.674 103.035 138.028 1.00 50.18  ? 204  ASN A CB    1 
ATOM   3022  C CG    . ASN D 4 207  ? 150.551 104.256 137.806 1.00 49.25  ? 204  ASN A CG    1 
ATOM   3023  O OD1   . ASN D 4 207  ? 150.494 104.897 136.755 1.00 51.01  ? 204  ASN A OD1   1 
ATOM   3024  N ND2   . ASN D 4 207  ? 151.367 104.585 138.802 1.00 45.34  ? 204  ASN A ND2   1 
ATOM   3025  N N     . CYS D 4 208  ? 147.286 100.959 137.566 1.00 51.88  ? 205  CYS A N     1 
ATOM   3026  C CA    . CYS D 4 208  ? 146.770 99.597  137.645 1.00 54.00  ? 205  CYS A CA    1 
ATOM   3027  C C     . CYS D 4 208  ? 146.299 99.095  136.286 1.00 56.69  ? 205  CYS A C     1 
ATOM   3028  O O     . CYS D 4 208  ? 146.434 97.904  135.985 1.00 60.05  ? 205  CYS A O     1 
ATOM   3029  C CB    . CYS D 4 208  ? 145.628 99.525  138.658 1.00 56.49  ? 205  CYS A CB    1 
ATOM   3030  S SG    . CYS D 4 208  ? 146.048 100.154 140.299 1.00 58.59  ? 205  CYS A SG    1 
ATOM   3031  N N     . HIS D 4 209  ? 145.749 99.984  135.457 1.00 54.86  ? 206  HIS A N     1 
ATOM   3032  C CA    . HIS D 4 209  ? 145.287 99.572  134.136 1.00 53.39  ? 206  HIS A CA    1 
ATOM   3033  C C     . HIS D 4 209  ? 146.458 99.334  133.192 1.00 53.76  ? 206  HIS A C     1 
ATOM   3034  O O     . HIS D 4 209  ? 146.431 98.396  132.386 1.00 55.26  ? 206  HIS A O     1 
ATOM   3035  C CB    . HIS D 4 209  ? 144.334 100.622 133.567 1.00 53.68  ? 206  HIS A CB    1 
ATOM   3036  C CG    . HIS D 4 209  ? 143.698 100.220 132.273 1.00 59.22  ? 206  HIS A CG    1 
ATOM   3037  N ND1   . HIS D 4 209  ? 144.002 100.827 131.073 1.00 62.09  ? 206  HIS A ND1   1 
ATOM   3038  C CD2   . HIS D 4 209  ? 142.774 99.271  131.991 1.00 64.63  ? 206  HIS A CD2   1 
ATOM   3039  C CE1   . HIS D 4 209  ? 143.292 100.270 130.109 1.00 65.48  ? 206  HIS A CE1   1 
ATOM   3040  N NE2   . HIS D 4 209  ? 142.540 99.321  130.638 1.00 66.67  ? 206  HIS A NE2   1 
ATOM   3041  N N     . ILE D 4 210  ? 147.493 100.174 133.273 1.00 50.80  ? 207  ILE A N     1 
ATOM   3042  C CA    . ILE D 4 210  ? 148.693 99.957  132.468 1.00 52.06  ? 207  ILE A CA    1 
ATOM   3043  C C     . ILE D 4 210  ? 149.363 98.648  132.861 1.00 54.26  ? 207  ILE A C     1 
ATOM   3044  O O     . ILE D 4 210  ? 149.900 97.924  132.013 1.00 52.97  ? 207  ILE A O     1 
ATOM   3045  C CB    . ILE D 4 210  ? 149.655 101.151 132.611 1.00 50.86  ? 207  ILE A CB    1 
ATOM   3046  C CG1   . ILE D 4 210  ? 148.991 102.438 132.121 1.00 51.17  ? 207  ILE A CG1   1 
ATOM   3047  C CG2   . ILE D 4 210  ? 150.949 100.900 131.853 1.00 48.81  ? 207  ILE A CG2   1 
ATOM   3048  C CD1   . ILE D 4 210  ? 149.853 103.667 132.293 1.00 50.14  ? 207  ILE A CD1   1 
ATOM   3049  N N     . PHE D 4 211  ? 149.327 98.316  134.154 1.00 56.95  ? 208  PHE A N     1 
ATOM   3050  C CA    . PHE D 4 211  ? 149.980 97.103  134.636 1.00 58.13  ? 208  PHE A CA    1 
ATOM   3051  C C     . PHE D 4 211  ? 149.319 95.854  134.062 1.00 63.71  ? 208  PHE A C     1 
ATOM   3052  O O     . PHE D 4 211  ? 149.988 95.010  133.455 1.00 66.74  ? 208  PHE A O     1 
ATOM   3053  C CB    . PHE D 4 211  ? 149.954 97.080  136.164 1.00 56.09  ? 208  PHE A CB    1 
ATOM   3054  C CG    . PHE D 4 211  ? 150.469 95.803  136.765 1.00 56.86  ? 208  PHE A CG    1 
ATOM   3055  C CD1   . PHE D 4 211  ? 151.829 95.590  136.912 1.00 56.92  ? 208  PHE A CD1   1 
ATOM   3056  C CD2   . PHE D 4 211  ? 149.592 94.822  137.197 1.00 58.33  ? 208  PHE A CD2   1 
ATOM   3057  C CE1   . PHE D 4 211  ? 152.305 94.417  137.471 1.00 58.89  ? 208  PHE A CE1   1 
ATOM   3058  C CE2   . PHE D 4 211  ? 150.060 93.647  137.754 1.00 59.39  ? 208  PHE A CE2   1 
ATOM   3059  C CZ    . PHE D 4 211  ? 151.419 93.444  137.893 1.00 59.60  ? 208  PHE A CZ    1 
ATOM   3060  N N     . THR D 4 212  ? 148.001 95.726  134.234 1.00 65.50  ? 209  THR A N     1 
ATOM   3061  C CA    . THR D 4 212  ? 147.323 94.499  133.824 1.00 66.58  ? 209  THR A CA    1 
ATOM   3062  C C     . THR D 4 212  ? 147.334 94.316  132.310 1.00 64.64  ? 209  THR A C     1 
ATOM   3063  O O     . THR D 4 212  ? 147.324 93.178  131.828 1.00 67.48  ? 209  THR A O     1 
ATOM   3064  C CB    . THR D 4 212  ? 145.887 94.484  134.348 1.00 68.88  ? 209  THR A CB    1 
ATOM   3065  O OG1   . THR D 4 212  ? 145.148 95.562  133.760 1.00 70.87  ? 209  THR A OG1   1 
ATOM   3066  C CG2   . THR D 4 212  ? 145.872 94.632  135.862 1.00 69.33  ? 209  THR A CG2   1 
ATOM   3067  N N     . ARG D 4 213  ? 147.354 95.410  131.545 1.00 61.32  ? 210  ARG A N     1 
ATOM   3068  C CA    . ARG D 4 213  ? 147.419 95.280  130.092 1.00 62.46  ? 210  ARG A CA    1 
ATOM   3069  C C     . ARG D 4 213  ? 148.766 94.724  129.647 1.00 64.13  ? 210  ARG A C     1 
ATOM   3070  O O     . ARG D 4 213  ? 148.830 93.904  128.722 1.00 66.76  ? 210  ARG A O     1 
ATOM   3071  C CB    . ARG D 4 213  ? 147.150 96.624  129.419 1.00 61.76  ? 210  ARG A CB    1 
ATOM   3072  C CG    . ARG D 4 213  ? 145.696 97.056  129.451 1.00 66.62  ? 210  ARG A CG    1 
ATOM   3073  C CD    . ARG D 4 213  ? 145.426 98.117  128.398 1.00 69.61  ? 210  ARG A CD    1 
ATOM   3074  N NE    . ARG D 4 213  ? 145.582 97.590  127.047 1.00 73.49  ? 210  ARG A NE    1 
ATOM   3075  C CZ    . ARG D 4 213  ? 145.487 98.322  125.941 1.00 75.30  ? 210  ARG A CZ    1 
ATOM   3076  N NH1   . ARG D 4 213  ? 145.239 99.622  126.024 1.00 74.58  ? 210  ARG A NH1   1 
ATOM   3077  N NH2   . ARG D 4 213  ? 145.643 97.755  124.752 1.00 75.78  ? 210  ARG A NH2   1 
ATOM   3078  N N     . LEU D 4 214  ? 149.854 95.156  130.290 1.00 60.40  ? 211  LEU A N     1 
ATOM   3079  C CA    . LEU D 4 214  ? 151.172 94.635  129.943 1.00 56.19  ? 211  LEU A CA    1 
ATOM   3080  C C     . LEU D 4 214  ? 151.325 93.181  130.375 1.00 58.63  ? 211  LEU A C     1 
ATOM   3081  O O     . LEU D 4 214  ? 151.866 92.359  129.625 1.00 58.47  ? 211  LEU A O     1 
ATOM   3082  C CB    . LEU D 4 214  ? 152.264 95.499  130.574 1.00 51.00  ? 211  LEU A CB    1 
ATOM   3083  C CG    . LEU D 4 214  ? 152.421 96.930  130.053 1.00 46.48  ? 211  LEU A CG    1 
ATOM   3084  C CD1   . LEU D 4 214  ? 153.471 97.682  130.859 1.00 43.47  ? 211  LEU A CD1   1 
ATOM   3085  C CD2   . LEU D 4 214  ? 152.777 96.933  128.576 1.00 43.76  ? 211  LEU A CD2   1 
ATOM   3086  N N     . ILE D 4 215  ? 150.849 92.844  131.576 1.00 61.06  ? 212  ILE A N     1 
ATOM   3087  C CA    . ILE D 4 215  ? 151.011 91.486  132.086 1.00 64.53  ? 212  ILE A CA    1 
ATOM   3088  C C     . ILE D 4 215  ? 150.187 90.497  131.273 1.00 67.37  ? 212  ILE A C     1 
ATOM   3089  O O     . ILE D 4 215  ? 150.594 89.344  131.086 1.00 71.35  ? 212  ILE A O     1 
ATOM   3090  C CB    . ILE D 4 215  ? 150.648 91.433  133.582 1.00 67.42  ? 212  ILE A CB    1 
ATOM   3091  C CG1   . ILE D 4 215  ? 151.499 92.429  134.374 1.00 67.04  ? 212  ILE A CG1   1 
ATOM   3092  C CG2   . ILE D 4 215  ? 150.828 90.030  134.138 1.00 70.25  ? 212  ILE A CG2   1 
ATOM   3093  C CD1   . ILE D 4 215  ? 152.978 92.360  134.063 1.00 64.77  ? 212  ILE A CD1   1 
ATOM   3094  N N     . THR D 4 216  ? 149.025 90.919  130.772 1.00 67.19  ? 213  THR A N     1 
ATOM   3095  C CA    . THR D 4 216  ? 148.207 90.016  129.970 1.00 69.20  ? 213  THR A CA    1 
ATOM   3096  C C     . THR D 4 216  ? 148.845 89.756  128.610 1.00 68.66  ? 213  THR A C     1 
ATOM   3097  O O     . THR D 4 216  ? 148.867 88.615  128.136 1.00 71.03  ? 213  THR A O     1 
ATOM   3098  C CB    . THR D 4 216  ? 146.798 90.584  129.806 1.00 69.13  ? 213  THR A CB    1 
ATOM   3099  O OG1   . THR D 4 216  ? 146.217 90.796  131.099 1.00 69.23  ? 213  THR A OG1   1 
ATOM   3100  C CG2   . THR D 4 216  ? 145.921 89.620  129.020 1.00 70.97  ? 213  THR A CG2   1 
ATOM   3101  N N     . ALA D 4 217  ? 149.382 90.798  127.974 1.00 66.99  ? 214  ALA A N     1 
ATOM   3102  C CA    . ALA D 4 217  ? 150.019 90.624  126.673 1.00 67.93  ? 214  ALA A CA    1 
ATOM   3103  C C     . ALA D 4 217  ? 151.382 89.955  126.807 1.00 68.20  ? 214  ALA A C     1 
ATOM   3104  O O     . ALA D 4 217  ? 151.697 89.019  126.065 1.00 70.74  ? 214  ALA A O     1 
ATOM   3105  C CB    . ALA D 4 217  ? 150.148 91.973  125.966 1.00 65.45  ? 214  ALA A CB    1 
ATOM   3106  N N     . VAL D 4 218  ? 152.202 90.420  127.746 1.00 64.72  ? 215  VAL A N     1 
ATOM   3107  C CA    . VAL D 4 218  ? 153.528 89.845  127.970 1.00 61.88  ? 215  VAL A CA    1 
ATOM   3108  C C     . VAL D 4 218  ? 153.592 89.309  129.396 1.00 63.91  ? 215  VAL A C     1 
ATOM   3109  O O     . VAL D 4 218  ? 154.004 90.037  130.311 1.00 62.67  ? 215  VAL A O     1 
ATOM   3110  C CB    . VAL D 4 218  ? 154.635 90.879  127.706 1.00 57.65  ? 215  VAL A CB    1 
ATOM   3111  C CG1   . VAL D 4 218  ? 156.005 90.223  127.791 1.00 57.44  ? 215  VAL A CG1   1 
ATOM   3112  C CG2   . VAL D 4 218  ? 154.436 91.537  126.349 1.00 54.60  ? 215  VAL A CG2   1 
ATOM   3113  N N     . PRO D 4 219  ? 153.193 88.057  129.633 1.00 67.37  ? 216  PRO A N     1 
ATOM   3114  C CA    . PRO D 4 219  ? 153.189 87.537  131.011 1.00 70.11  ? 216  PRO A CA    1 
ATOM   3115  C C     . PRO D 4 219  ? 154.569 87.456  131.641 1.00 70.60  ? 216  PRO A C     1 
ATOM   3116  O O     . PRO D 4 219  ? 154.677 87.496  132.874 1.00 72.10  ? 216  PRO A O     1 
ATOM   3117  C CB    . PRO D 4 219  ? 152.556 86.147  130.859 1.00 71.86  ? 216  PRO A CB    1 
ATOM   3118  C CG    . PRO D 4 219  ? 151.779 86.218  129.583 1.00 71.81  ? 216  PRO A CG    1 
ATOM   3119  C CD    . PRO D 4 219  ? 152.569 87.118  128.685 1.00 69.31  ? 216  PRO A CD    1 
ATOM   3120  N N     . SER D 4 220  ? 155.628 87.336  130.837 1.00 70.69  ? 217  SER A N     1 
ATOM   3121  C CA    . SER D 4 220  ? 156.977 87.305  131.390 1.00 70.11  ? 217  SER A CA    1 
ATOM   3122  C C     . SER D 4 220  ? 157.332 88.602  132.104 1.00 72.13  ? 217  SER A C     1 
ATOM   3123  O O     . SER D 4 220  ? 158.231 88.606  132.952 1.00 73.31  ? 217  SER A O     1 
ATOM   3124  C CB    . SER D 4 220  ? 157.995 87.024  130.283 1.00 66.62  ? 217  SER A CB    1 
ATOM   3125  O OG    . SER D 4 220  ? 157.976 88.046  129.301 1.00 64.23  ? 217  SER A OG    1 
ATOM   3126  N N     . LEU D 4 221  ? 156.642 89.697  131.780 1.00 72.36  ? 218  LEU A N     1 
ATOM   3127  C CA    . LEU D 4 221  ? 156.888 90.975  132.434 1.00 70.08  ? 218  LEU A CA    1 
ATOM   3128  C C     . LEU D 4 221  ? 156.429 90.981  133.886 1.00 69.70  ? 218  LEU A C     1 
ATOM   3129  O O     . LEU D 4 221  ? 156.850 91.856  134.652 1.00 66.73  ? 218  LEU A O     1 
ATOM   3130  C CB    . LEU D 4 221  ? 156.189 92.091  131.660 1.00 67.60  ? 218  LEU A CB    1 
ATOM   3131  C CG    . LEU D 4 221  ? 157.034 93.284  131.217 1.00 66.01  ? 218  LEU A CG    1 
ATOM   3132  C CD1   . LEU D 4 221  ? 158.346 92.819  130.608 1.00 65.68  ? 218  LEU A CD1   1 
ATOM   3133  C CD2   . LEU D 4 221  ? 156.250 94.117  130.220 1.00 65.72  ? 218  LEU A CD2   1 
ATOM   3134  N N     . ARG D 4 222  ? 155.578 90.031  134.282 1.00 72.45  ? 219  ARG A N     1 
ATOM   3135  C CA    . ARG D 4 222  ? 155.109 89.974  135.662 1.00 73.88  ? 219  ARG A CA    1 
ATOM   3136  C C     . ARG D 4 222  ? 156.241 89.599  136.607 1.00 74.85  ? 219  ARG A C     1 
ATOM   3137  O O     . ARG D 4 222  ? 156.524 90.315  137.574 1.00 74.50  ? 219  ARG A O     1 
ATOM   3138  C CB    . ARG D 4 222  ? 153.945 88.983  135.780 1.00 75.00  ? 219  ARG A CB    1 
ATOM   3139  C CG    . ARG D 4 222  ? 153.289 88.929  137.157 1.00 77.38  ? 219  ARG A CG    1 
ATOM   3140  C CD    . ARG D 4 222  ? 153.904 87.847  138.036 1.00 81.80  ? 219  ARG A CD    1 
ATOM   3141  N NE    . ARG D 4 222  ? 153.525 87.988  139.437 1.00 85.67  ? 219  ARG A NE    1 
ATOM   3142  C CZ    . ARG D 4 222  ? 154.067 87.291  140.430 1.00 89.55  ? 219  ARG A CZ    1 
ATOM   3143  N NH1   . ARG D 4 222  ? 155.017 86.400  140.175 1.00 90.84  ? 219  ARG A NH1   1 
ATOM   3144  N NH2   . ARG D 4 222  ? 153.662 87.484  141.678 1.00 91.28  ? 219  ARG A NH2   1 
ATOM   3145  N N     . GLU D 4 223  ? 156.899 88.467  136.345 1.00 76.59  ? 220  GLU A N     1 
ATOM   3146  C CA    . GLU D 4 223  ? 158.030 88.067  137.176 1.00 78.48  ? 220  GLU A CA    1 
ATOM   3147  C C     . GLU D 4 223  ? 159.163 89.080  137.094 1.00 78.70  ? 220  GLU A C     1 
ATOM   3148  O O     . GLU D 4 223  ? 159.927 89.235  138.054 1.00 80.10  ? 220  GLU A O     1 
ATOM   3149  C CB    . GLU D 4 223  ? 158.524 86.681  136.762 1.00 80.03  ? 220  GLU A CB    1 
ATOM   3150  N N     . HIS D 4 224  ? 159.280 89.787  135.967 1.00 78.14  ? 221  HIS A N     1 
ATOM   3151  C CA    . HIS D 4 224  ? 160.334 90.785  135.826 1.00 78.04  ? 221  HIS A CA    1 
ATOM   3152  C C     . HIS D 4 224  ? 160.058 92.005  136.699 1.00 76.03  ? 221  HIS A C     1 
ATOM   3153  O O     . HIS D 4 224  ? 160.977 92.546  137.324 1.00 74.48  ? 221  HIS A O     1 
ATOM   3154  C CB    . HIS D 4 224  ? 160.476 91.188  134.358 1.00 79.31  ? 221  HIS A CB    1 
ATOM   3155  C CG    . HIS D 4 224  ? 161.821 91.745  134.012 1.00 81.77  ? 221  HIS A CG    1 
ATOM   3156  N ND1   . HIS D 4 224  ? 162.393 91.589  132.767 1.00 81.94  ? 221  HIS A ND1   1 
ATOM   3157  C CD2   . HIS D 4 224  ? 162.707 92.460  134.746 1.00 82.42  ? 221  HIS A CD2   1 
ATOM   3158  C CE1   . HIS D 4 224  ? 163.574 92.181  132.750 1.00 81.01  ? 221  HIS A CE1   1 
ATOM   3159  N NE2   . HIS D 4 224  ? 163.788 92.718  133.938 1.00 81.38  ? 221  HIS A NE2   1 
ATOM   3160  N N     . PHE D 4 225  ? 158.801 92.454  136.751 1.00 74.16  ? 222  PHE A N     1 
ATOM   3161  C CA    . PHE D 4 225  ? 158.445 93.542  137.657 1.00 70.75  ? 222  PHE A CA    1 
ATOM   3162  C C     . PHE D 4 225  ? 158.626 93.124  139.111 1.00 71.71  ? 222  PHE A C     1 
ATOM   3163  O O     . PHE D 4 225  ? 159.062 93.925  139.947 1.00 69.46  ? 222  PHE A O     1 
ATOM   3164  C CB    . PHE D 4 225  ? 157.003 93.991  137.409 1.00 67.25  ? 222  PHE A CB    1 
ATOM   3165  C CG    . PHE D 4 225  ? 156.801 94.715  136.107 1.00 63.41  ? 222  PHE A CG    1 
ATOM   3166  C CD1   . PHE D 4 225  ? 157.853 95.364  135.482 1.00 62.19  ? 222  PHE A CD1   1 
ATOM   3167  C CD2   . PHE D 4 225  ? 155.550 94.753  135.511 1.00 61.50  ? 222  PHE A CD2   1 
ATOM   3168  C CE1   . PHE D 4 225  ? 157.664 96.033  134.283 1.00 58.48  ? 222  PHE A CE1   1 
ATOM   3169  C CE2   . PHE D 4 225  ? 155.354 95.419  134.312 1.00 58.65  ? 222  PHE A CE2   1 
ATOM   3170  C CZ    . PHE D 4 225  ? 156.412 96.059  133.699 1.00 56.90  ? 222  PHE A CZ    1 
ATOM   3171  N N     . GLU D 4 226  ? 158.290 91.871  139.432 1.00 76.18  ? 223  GLU A N     1 
ATOM   3172  C CA    . GLU D 4 226  ? 158.436 91.384  140.801 1.00 80.68  ? 223  GLU A CA    1 
ATOM   3173  C C     . GLU D 4 226  ? 159.897 91.372  141.232 1.00 81.80  ? 223  GLU A C     1 
ATOM   3174  O O     . GLU D 4 226  ? 160.212 91.659  142.393 1.00 82.47  ? 223  GLU A O     1 
ATOM   3175  C CB    . GLU D 4 226  ? 157.830 89.984  140.925 1.00 85.00  ? 223  GLU A CB    1 
ATOM   3176  C CG    . GLU D 4 226  ? 157.975 89.352  142.303 1.00 90.35  ? 223  GLU A CG    1 
ATOM   3177  C CD    . GLU D 4 226  ? 156.932 89.842  143.289 1.00 94.27  ? 223  GLU A CD    1 
ATOM   3178  O OE1   . GLU D 4 226  ? 155.753 89.962  142.899 1.00 94.85  ? 223  GLU A OE1   1 
ATOM   3179  O OE2   . GLU D 4 226  ? 157.292 90.109  144.456 1.00 96.61  ? 223  GLU A OE2   1 
ATOM   3180  N N     . ASN D 4 227  ? 160.806 91.047  140.309 1.00 84.12  ? 224  ASN A N     1 
ATOM   3181  C CA    . ASN D 4 227  ? 162.226 91.034  140.646 1.00 84.83  ? 224  ASN A CA    1 
ATOM   3182  C C     . ASN D 4 227  ? 162.738 92.438  140.938 1.00 81.88  ? 224  ASN A C     1 
ATOM   3183  O O     . ASN D 4 227  ? 163.587 92.622  141.818 1.00 83.93  ? 224  ASN A O     1 
ATOM   3184  C CB    . ASN D 4 227  ? 163.032 90.392  139.516 1.00 86.11  ? 224  ASN A CB    1 
ATOM   3185  C CG    . ASN D 4 227  ? 162.684 88.933  139.305 1.00 89.01  ? 224  ASN A CG    1 
ATOM   3186  O OD1   . ASN D 4 227  ? 162.426 88.201  140.260 1.00 88.84  ? 224  ASN A OD1   1 
ATOM   3187  N ND2   . ASN D 4 227  ? 162.685 88.499  138.049 1.00 91.13  ? 224  ASN A ND2   1 
ATOM   3188  N N     . VAL D 4 228  ? 162.238 93.439  140.210 1.00 77.14  ? 225  VAL A N     1 
ATOM   3189  C CA    . VAL D 4 228  ? 162.658 94.816  140.456 1.00 73.62  ? 225  VAL A CA    1 
ATOM   3190  C C     . VAL D 4 228  ? 162.216 95.266  141.842 1.00 72.48  ? 225  VAL A C     1 
ATOM   3191  O O     . VAL D 4 228  ? 162.953 95.963  142.551 1.00 72.08  ? 225  VAL A O     1 
ATOM   3192  C CB    . VAL D 4 228  ? 162.115 95.745  139.355 1.00 70.02  ? 225  VAL A CB    1 
ATOM   3193  C CG1   . VAL D 4 228  ? 162.509 97.189  139.631 1.00 67.54  ? 225  VAL A CG1   1 
ATOM   3194  C CG2   . VAL D 4 228  ? 162.624 95.306  137.992 1.00 68.30  ? 225  VAL A CG2   1 
ATOM   3195  N N     . LYS D 4 229  ? 161.011 94.870  142.256 1.00 71.50  ? 226  LYS A N     1 
ATOM   3196  C CA    . LYS D 4 229  ? 160.525 95.249  143.579 1.00 70.90  ? 226  LYS A CA    1 
ATOM   3197  C C     . LYS D 4 229  ? 161.324 94.562  144.678 1.00 74.76  ? 226  LYS A C     1 
ATOM   3198  O O     . LYS D 4 229  ? 161.636 95.178  145.704 1.00 75.26  ? 226  LYS A O     1 
ATOM   3199  C CB    . LYS D 4 229  ? 159.039 94.916  143.709 1.00 68.59  ? 226  LYS A CB    1 
ATOM   3200  C CG    . LYS D 4 229  ? 158.339 95.655  144.837 1.00 67.33  ? 226  LYS A CG    1 
ATOM   3201  C CD    . LYS D 4 229  ? 157.333 94.767  145.546 1.00 68.21  ? 226  LYS A CD    1 
ATOM   3202  C CE    . LYS D 4 229  ? 158.034 93.648  146.298 1.00 72.35  ? 226  LYS A CE    1 
ATOM   3203  N NZ    . LYS D 4 229  ? 157.082 92.827  147.092 1.00 76.36  ? 226  LYS A NZ    1 
ATOM   3204  N N     . LYS D 4 230  ? 161.666 93.285  144.483 1.00 78.69  ? 227  LYS A N     1 
ATOM   3205  C CA    . LYS D 4 230  ? 162.437 92.561  145.487 1.00 82.93  ? 227  LYS A CA    1 
ATOM   3206  C C     . LYS D 4 230  ? 163.889 93.020  145.528 1.00 84.30  ? 227  LYS A C     1 
ATOM   3207  O O     . LYS D 4 230  ? 164.507 93.016  146.599 1.00 82.57  ? 227  LYS A O     1 
ATOM   3208  C CB    . LYS D 4 230  ? 162.368 91.056  145.224 1.00 85.07  ? 227  LYS A CB    1 
ATOM   3209  C CG    . LYS D 4 230  ? 160.997 90.435  145.450 1.00 87.04  ? 227  LYS A CG    1 
ATOM   3210  C CD    . LYS D 4 230  ? 161.031 88.929  145.224 1.00 89.07  ? 227  LYS A CD    1 
ATOM   3211  C CE    . LYS D 4 230  ? 159.701 88.281  145.578 1.00 90.62  ? 227  LYS A CE    1 
ATOM   3212  N NZ    . LYS D 4 230  ? 159.726 86.804  145.380 1.00 91.59  ? 227  LYS A NZ    1 
ATOM   3213  N N     . ALA D 4 231  ? 164.448 93.417  144.382 1.00 89.28  ? 228  ALA A N     1 
ATOM   3214  C CA    . ALA D 4 231  ? 165.846 93.829  144.340 1.00 88.26  ? 228  ALA A CA    1 
ATOM   3215  C C     . ALA D 4 231  ? 166.081 95.173  145.016 1.00 88.39  ? 228  ALA A C     1 
ATOM   3216  O O     . ALA D 4 231  ? 167.221 95.473  145.387 1.00 89.54  ? 228  ALA A O     1 
ATOM   3217  C CB    . ALA D 4 231  ? 166.337 93.888  142.893 1.00 85.51  ? 228  ALA A CB    1 
ATOM   3218  N N     . ILE D 4 232  ? 165.042 95.986  145.182 1.00 87.16  ? 229  ILE A N     1 
ATOM   3219  C CA    . ILE D 4 232  ? 165.195 97.282  145.837 1.00 86.15  ? 229  ILE A CA    1 
ATOM   3220  C C     . ILE D 4 232  ? 164.925 97.185  147.333 1.00 89.54  ? 229  ILE A C     1 
ATOM   3221  O O     . ILE D 4 232  ? 165.660 97.759  148.140 1.00 92.63  ? 229  ILE A O     1 
ATOM   3222  C CB    . ILE D 4 232  ? 164.277 98.321  145.166 1.00 81.39  ? 229  ILE A CB    1 
ATOM   3223  C CG1   . ILE D 4 232  ? 164.661 98.505  143.697 1.00 79.22  ? 229  ILE A CG1   1 
ATOM   3224  C CG2   . ILE D 4 232  ? 164.353 99.648  145.897 1.00 80.39  ? 229  ILE A CG2   1 
ATOM   3225  C CD1   . ILE D 4 232  ? 163.865 99.582  142.993 1.00 75.42  ? 229  ILE A CD1   1 
ATOM   3226  N N     . GLY D 4 233  ? 163.880 96.461  147.724 1.00 88.21  ? 230  GLY A N     1 
ATOM   3227  C CA    . GLY D 4 233  ? 163.517 96.317  149.116 1.00 89.36  ? 230  GLY A CA    1 
ATOM   3228  C C     . GLY D 4 233  ? 162.266 97.058  149.537 1.00 88.96  ? 230  GLY A C     1 
ATOM   3229  O O     . GLY D 4 233  ? 161.962 97.088  150.735 1.00 92.02  ? 230  GLY A O     1 
ATOM   3230  N N     . ILE D 4 234  ? 161.537 97.649  148.602 1.00 85.71  ? 231  ILE A N     1 
ATOM   3231  C CA    . ILE D 4 234  ? 160.328 98.404  148.901 1.00 84.82  ? 231  ILE A CA    1 
ATOM   3232  C C     . ILE D 4 234  ? 159.138 97.457  148.908 1.00 86.47  ? 231  ILE A C     1 
ATOM   3233  O O     . ILE D 4 234  ? 159.038 96.560  148.061 1.00 86.60  ? 231  ILE A O     1 
ATOM   3234  C CB    . ILE D 4 234  ? 160.130 99.539  147.878 1.00 80.76  ? 231  ILE A CB    1 
ATOM   3235  C CG1   . ILE D 4 234  ? 161.371 100.431 147.826 1.00 79.01  ? 231  ILE A CG1   1 
ATOM   3236  C CG2   . ILE D 4 234  ? 158.901 100.363 148.219 1.00 80.92  ? 231  ILE A CG2   1 
ATOM   3237  C CD1   . ILE D 4 234  ? 161.293 101.514 146.775 1.00 76.03  ? 231  ILE A CD1   1 
ATOM   3238  N N     . PHE D 4 235  ? 158.235 97.655  149.869 1.00 87.34  ? 232  PHE A N     1 
ATOM   3239  C CA    . PHE D 4 235  ? 156.982 96.904  149.962 1.00 88.25  ? 232  PHE A CA    1 
ATOM   3240  C C     . PHE D 4 235  ? 157.250 95.400  150.035 1.00 92.75  ? 232  PHE A C     1 
ATOM   3241  O O     . PHE D 4 235  ? 156.815 94.617  149.189 1.00 91.88  ? 232  PHE A O     1 
ATOM   3242  C CB    . PHE D 4 235  ? 156.054 97.243  148.789 1.00 83.62  ? 232  PHE A CB    1 
ATOM   3243  C CG    . PHE D 4 235  ? 155.787 98.715  148.624 1.00 79.27  ? 232  PHE A CG    1 
ATOM   3244  C CD1   . PHE D 4 235  ? 155.711 99.553  149.725 1.00 79.06  ? 232  PHE A CD1   1 
ATOM   3245  C CD2   . PHE D 4 235  ? 155.611 99.261  147.362 1.00 75.89  ? 232  PHE A CD2   1 
ATOM   3246  C CE1   . PHE D 4 235  ? 155.466 100.906 149.570 1.00 76.80  ? 232  PHE A CE1   1 
ATOM   3247  C CE2   . PHE D 4 235  ? 155.366 100.612 147.202 1.00 73.89  ? 232  PHE A CE2   1 
ATOM   3248  C CZ    . PHE D 4 235  ? 155.293 101.434 148.307 1.00 74.14  ? 232  PHE A CZ    1 
ATOM   3249  N N     . VAL D 4 236  ? 157.988 95.006  151.076 1.00 100.14 ? 233  VAL A N     1 
ATOM   3250  C CA    . VAL D 4 236  ? 158.369 93.604  151.216 1.00 101.71 ? 233  VAL A CA    1 
ATOM   3251  C C     . VAL D 4 236  ? 157.160 92.738  151.545 1.00 102.99 ? 233  VAL A C     1 
ATOM   3252  O O     . VAL D 4 236  ? 157.121 91.554  151.187 1.00 104.72 ? 233  VAL A O     1 
ATOM   3253  C CB    . VAL D 4 236  ? 159.477 93.457  152.275 1.00 102.91 ? 233  VAL A CB    1 
ATOM   3254  C CG1   . VAL D 4 236  ? 160.752 94.138  151.804 1.00 100.26 ? 233  VAL A CG1   1 
ATOM   3255  C CG2   . VAL D 4 236  ? 159.024 94.036  153.608 1.00 105.70 ? 233  VAL A CG2   1 
ATOM   3256  N N     . SER D 4 237  ? 156.156 93.300  152.214 1.00 101.44 ? 234  SER A N     1 
ATOM   3257  C CA    . SER D 4 237  ? 154.965 92.558  152.603 1.00 100.90 ? 234  SER A CA    1 
ATOM   3258  C C     . SER D 4 237  ? 153.863 92.615  151.554 1.00 95.14  ? 234  SER A C     1 
ATOM   3259  O O     . SER D 4 237  ? 152.742 92.171  151.824 1.00 92.91  ? 234  SER A O     1 
ATOM   3260  C CB    . SER D 4 237  ? 154.433 93.083  153.939 1.00 104.06 ? 234  SER A CB    1 
ATOM   3261  O OG    . SER D 4 237  ? 153.215 92.449  154.288 1.00 106.64 ? 234  SER A OG    1 
ATOM   3262  N N     . THR D 4 238  ? 154.152 93.143  150.366 1.00 91.81  ? 235  THR A N     1 
ATOM   3263  C CA    . THR D 4 238  ? 153.146 93.342  149.331 1.00 87.05  ? 235  THR A CA    1 
ATOM   3264  C C     . THR D 4 238  ? 153.692 92.858  147.997 1.00 83.66  ? 235  THR A C     1 
ATOM   3265  O O     . THR D 4 238  ? 154.789 93.256  147.592 1.00 86.08  ? 235  THR A O     1 
ATOM   3266  C CB    . THR D 4 238  ? 152.746 94.817  149.234 1.00 82.71  ? 235  THR A CB    1 
ATOM   3267  O OG1   . THR D 4 238  ? 152.655 95.377  150.550 1.00 82.34  ? 235  THR A OG1   1 
ATOM   3268  C CG2   . THR D 4 238  ? 151.402 94.957  148.547 1.00 81.03  ? 235  THR A CG2   1 
ATOM   3269  N N     . SER D 4 239  ? 152.928 92.005  147.319 1.00 80.10  ? 236  SER A N     1 
ATOM   3270  C CA    . SER D 4 239  ? 153.334 91.511  146.012 1.00 78.19  ? 236  SER A CA    1 
ATOM   3271  C C     . SER D 4 239  ? 153.158 92.602  144.956 1.00 77.76  ? 236  SER A C     1 
ATOM   3272  O O     . SER D 4 239  ? 152.625 93.685  145.218 1.00 79.26  ? 236  SER A O     1 
ATOM   3273  C CB    . SER D 4 239  ? 152.532 90.268  145.632 1.00 79.97  ? 236  SER A CB    1 
ATOM   3274  O OG    . SER D 4 239  ? 151.170 90.590  145.416 1.00 81.28  ? 236  SER A OG    1 
ATOM   3275  N N     . ILE D 4 240  ? 153.611 92.301  143.736 1.00 77.51  ? 237  ILE A N     1 
ATOM   3276  C CA    . ILE D 4 240  ? 153.570 93.304  142.677 1.00 75.15  ? 237  ILE A CA    1 
ATOM   3277  C C     . ILE D 4 240  ? 152.151 93.478  142.144 1.00 76.51  ? 237  ILE A C     1 
ATOM   3278  O O     . ILE D 4 240  ? 151.790 94.556  141.660 1.00 75.56  ? 237  ILE A O     1 
ATOM   3279  C CB    . ILE D 4 240  ? 154.562 92.945  141.554 1.00 71.86  ? 237  ILE A CB    1 
ATOM   3280  C CG1   . ILE D 4 240  ? 154.744 94.129  140.599 1.00 67.73  ? 237  ILE A CG1   1 
ATOM   3281  C CG2   . ILE D 4 240  ? 154.095 91.721  140.783 1.00 72.83  ? 237  ILE A CG2   1 
ATOM   3282  C CD1   . ILE D 4 240  ? 155.251 95.385  141.272 1.00 65.15  ? 237  ILE A CD1   1 
ATOM   3283  N N     . GLU D 4 241  ? 151.323 92.435  142.223 1.00 79.70  ? 238  GLU A N     1 
ATOM   3284  C CA    . GLU D 4 241  ? 149.939 92.575  141.780 1.00 79.90  ? 238  GLU A CA    1 
ATOM   3285  C C     . GLU D 4 241  ? 149.119 93.400  142.763 1.00 78.03  ? 238  GLU A C     1 
ATOM   3286  O O     . GLU D 4 241  ? 148.184 94.098  142.354 1.00 76.17  ? 238  GLU A O     1 
ATOM   3287  C CB    . GLU D 4 241  ? 149.300 91.201  141.580 1.00 84.76  ? 238  GLU A CB    1 
ATOM   3288  C CG    . GLU D 4 241  ? 149.760 90.472  140.328 1.00 86.48  ? 238  GLU A CG    1 
ATOM   3289  C CD    . GLU D 4 241  ? 150.946 89.563  140.577 1.00 87.95  ? 238  GLU A CD    1 
ATOM   3290  O OE1   . GLU D 4 241  ? 151.639 89.751  141.597 1.00 86.69  ? 238  GLU A OE1   1 
ATOM   3291  O OE2   . GLU D 4 241  ? 151.179 88.653  139.754 1.00 89.96  ? 238  GLU A OE2   1 
ATOM   3292  N N     . GLU D 4 242  ? 149.455 93.339  144.053 1.00 80.65  ? 239  GLU A N     1 
ATOM   3293  C CA    . GLU D 4 242  ? 148.677 94.058  145.057 1.00 79.11  ? 239  GLU A CA    1 
ATOM   3294  C C     . GLU D 4 242  ? 148.980 95.551  145.043 1.00 76.49  ? 239  GLU A C     1 
ATOM   3295  O O     . GLU D 4 242  ? 148.077 96.367  145.262 1.00 75.59  ? 239  GLU A O     1 
ATOM   3296  C CB    . GLU D 4 242  ? 148.939 93.471  146.444 1.00 82.69  ? 239  GLU A CB    1 
ATOM   3297  C CG    . GLU D 4 242  ? 148.511 92.020  146.594 1.00 87.57  ? 239  GLU A CG    1 
ATOM   3298  C CD    . GLU D 4 242  ? 148.804 91.464  147.973 1.00 91.24  ? 239  GLU A CD    1 
ATOM   3299  O OE1   . GLU D 4 242  ? 149.135 92.260  148.876 1.00 92.19  ? 239  GLU A OE1   1 
ATOM   3300  O OE2   . GLU D 4 242  ? 148.707 90.231  148.151 1.00 93.10  ? 239  GLU A OE2   1 
ATOM   3301  N N     . VAL D 4 243  ? 150.235 95.935  144.786 1.00 75.42  ? 240  VAL A N     1 
ATOM   3302  C CA    . VAL D 4 243  ? 150.554 97.356  144.693 1.00 71.59  ? 240  VAL A CA    1 
ATOM   3303  C C     . VAL D 4 243  ? 149.887 97.992  143.482 1.00 70.55  ? 240  VAL A C     1 
ATOM   3304  O O     . VAL D 4 243  ? 149.798 99.222  143.400 1.00 70.93  ? 240  VAL A O     1 
ATOM   3305  C CB    . VAL D 4 243  ? 152.076 97.591  144.653 1.00 65.07  ? 240  VAL A CB    1 
ATOM   3306  C CG1   . VAL D 4 243  ? 152.759 96.891  145.816 1.00 66.03  ? 240  VAL A CG1   1 
ATOM   3307  C CG2   . VAL D 4 243  ? 152.658 97.136  143.329 1.00 61.88  ? 240  VAL A CG2   1 
ATOM   3308  N N     . PHE D 4 244  ? 149.417 97.182  142.533 1.00 69.97  ? 241  PHE A N     1 
ATOM   3309  C CA    . PHE D 4 244  ? 148.600 97.653  141.423 1.00 68.63  ? 241  PHE A CA    1 
ATOM   3310  C C     . PHE D 4 244  ? 147.143 97.233  141.585 1.00 71.87  ? 241  PHE A C     1 
ATOM   3311  O O     . PHE D 4 244  ? 146.441 96.998  140.598 1.00 74.43  ? 241  PHE A O     1 
ATOM   3312  C CB    . PHE D 4 244  ? 149.165 97.160  140.093 1.00 64.96  ? 241  PHE A CB    1 
ATOM   3313  C CG    . PHE D 4 244  ? 150.450 97.830  139.700 1.00 62.76  ? 241  PHE A CG    1 
ATOM   3314  C CD1   . PHE D 4 244  ? 150.439 99.067  139.075 1.00 60.66  ? 241  PHE A CD1   1 
ATOM   3315  C CD2   . PHE D 4 244  ? 151.670 97.227  139.958 1.00 63.65  ? 241  PHE A CD2   1 
ATOM   3316  C CE1   . PHE D 4 244  ? 151.620 99.689  138.713 1.00 58.22  ? 241  PHE A CE1   1 
ATOM   3317  C CE2   . PHE D 4 244  ? 152.855 97.844  139.599 1.00 61.98  ? 241  PHE A CE2   1 
ATOM   3318  C CZ    . PHE D 4 244  ? 152.830 99.075  138.974 1.00 58.93  ? 241  PHE A CZ    1 
ATOM   3319  N N     . SER D 4 245  ? 146.684 97.128  142.829 1.00 73.77  ? 242  SER A N     1 
ATOM   3320  C CA    . SER D 4 245  ? 145.281 96.918  143.148 1.00 75.29  ? 242  SER A CA    1 
ATOM   3321  C C     . SER D 4 245  ? 144.797 98.066  144.022 1.00 73.80  ? 242  SER A C     1 
ATOM   3322  O O     . SER D 4 245  ? 145.584 98.705  144.725 1.00 72.07  ? 242  SER A O     1 
ATOM   3323  C CB    . SER D 4 245  ? 145.056 95.579  143.862 1.00 82.38  ? 242  SER A CB    1 
ATOM   3324  O OG    . SER D 4 245  ? 145.662 95.575  145.145 1.00 87.41  ? 242  SER A OG    1 
ATOM   3325  N N     . PHE D 4 246  ? 143.490 98.320  143.969 1.00 70.61  ? 243  PHE A N     1 
ATOM   3326  C CA    . PHE D 4 246  ? 142.931 99.477  144.666 1.00 66.42  ? 243  PHE A CA    1 
ATOM   3327  C C     . PHE D 4 246  ? 143.193 99.500  146.170 1.00 66.23  ? 243  PHE A C     1 
ATOM   3328  O O     . PHE D 4 246  ? 143.516 100.584 146.686 1.00 63.91  ? 243  PHE A O     1 
ATOM   3329  C CB    . PHE D 4 246  ? 141.425 99.569  144.384 1.00 64.18  ? 243  PHE A CB    1 
ATOM   3330  C CG    . PHE D 4 246  ? 141.097 100.084 143.013 1.00 60.48  ? 243  PHE A CG    1 
ATOM   3331  C CD1   . PHE D 4 246  ? 142.082 100.638 142.211 1.00 57.82  ? 243  PHE A CD1   1 
ATOM   3332  C CD2   . PHE D 4 246  ? 139.802 100.022 142.528 1.00 60.79  ? 243  PHE A CD2   1 
ATOM   3333  C CE1   . PHE D 4 246  ? 141.782 101.115 140.950 1.00 56.81  ? 243  PHE A CE1   1 
ATOM   3334  C CE2   . PHE D 4 246  ? 139.496 100.497 141.269 1.00 60.39  ? 243  PHE A CE2   1 
ATOM   3335  C CZ    . PHE D 4 246  ? 140.488 101.044 140.478 1.00 58.12  ? 243  PHE A CZ    1 
ATOM   3336  N N     . PRO D 4 247  ? 143.068 98.399  146.925 1.00 68.96  ? 244  PRO A N     1 
ATOM   3337  C CA    . PRO D 4 247  ? 143.265 98.496  148.383 1.00 69.74  ? 244  PRO A CA    1 
ATOM   3338  C C     . PRO D 4 247  ? 144.630 99.022  148.799 1.00 67.62  ? 244  PRO A C     1 
ATOM   3339  O O     . PRO D 4 247  ? 144.754 99.553  149.909 1.00 69.29  ? 244  PRO A O     1 
ATOM   3340  C CB    . PRO D 4 247  ? 143.055 97.053  148.862 1.00 71.56  ? 244  PRO A CB    1 
ATOM   3341  C CG    . PRO D 4 247  ? 142.162 96.457  147.847 1.00 71.35  ? 244  PRO A CG    1 
ATOM   3342  C CD    . PRO D 4 247  ? 142.591 97.056  146.542 1.00 69.97  ? 244  PRO A CD    1 
ATOM   3343  N N     . PHE D 4 248  ? 145.655 98.902  147.952 1.00 64.63  ? 245  PHE A N     1 
ATOM   3344  C CA    . PHE D 4 248  ? 146.981 99.369  148.342 1.00 64.24  ? 245  PHE A CA    1 
ATOM   3345  C C     . PHE D 4 248  ? 147.092 100.888 148.321 1.00 61.40  ? 245  PHE A C     1 
ATOM   3346  O O     . PHE D 4 248  ? 148.000 101.438 148.954 1.00 61.08  ? 245  PHE A O     1 
ATOM   3347  C CB    . PHE D 4 248  ? 148.047 98.754  147.437 1.00 65.73  ? 245  PHE A CB    1 
ATOM   3348  C CG    . PHE D 4 248  ? 149.455 99.033  147.885 1.00 67.57  ? 245  PHE A CG    1 
ATOM   3349  C CD1   . PHE D 4 248  ? 149.970 98.423  149.017 1.00 69.47  ? 245  PHE A CD1   1 
ATOM   3350  C CD2   . PHE D 4 248  ? 150.264 99.903  147.172 1.00 65.14  ? 245  PHE A CD2   1 
ATOM   3351  C CE1   . PHE D 4 248  ? 151.264 98.677  149.433 1.00 68.94  ? 245  PHE A CE1   1 
ATOM   3352  C CE2   . PHE D 4 248  ? 151.561 100.161 147.581 1.00 64.62  ? 245  PHE A CE2   1 
ATOM   3353  C CZ    . PHE D 4 248  ? 152.060 99.546  148.714 1.00 66.68  ? 245  PHE A CZ    1 
ATOM   3354  N N     . TYR D 4 249  ? 146.192 101.581 147.618 1.00 60.14  ? 246  TYR A N     1 
ATOM   3355  C CA    . TYR D 4 249  ? 146.260 103.036 147.559 1.00 58.45  ? 246  TYR A CA    1 
ATOM   3356  C C     . TYR D 4 249  ? 146.021 103.681 148.917 1.00 59.05  ? 246  TYR A C     1 
ATOM   3357  O O     . TYR D 4 249  ? 146.445 104.824 149.131 1.00 58.91  ? 246  TYR A O     1 
ATOM   3358  C CB    . TYR D 4 249  ? 145.255 103.570 146.536 1.00 55.97  ? 246  TYR A CB    1 
ATOM   3359  C CG    . TYR D 4 249  ? 145.297 105.072 146.359 1.00 46.90  ? 246  TYR A CG    1 
ATOM   3360  C CD1   . TYR D 4 249  ? 146.439 105.702 145.882 1.00 45.62  ? 246  TYR A CD1   1 
ATOM   3361  C CD2   . TYR D 4 249  ? 144.194 105.857 146.664 1.00 46.79  ? 246  TYR A CD2   1 
ATOM   3362  C CE1   . TYR D 4 249  ? 146.484 107.074 145.719 1.00 44.34  ? 246  TYR A CE1   1 
ATOM   3363  C CE2   . TYR D 4 249  ? 144.227 107.229 146.504 1.00 45.45  ? 246  TYR A CE2   1 
ATOM   3364  C CZ    . TYR D 4 249  ? 145.375 107.832 146.031 1.00 50.46  ? 246  TYR A CZ    1 
ATOM   3365  O OH    . TYR D 4 249  ? 145.411 109.198 145.871 1.00 49.71  ? 246  TYR A OH    1 
ATOM   3366  N N     . ASN D 4 250  ? 145.361 102.977 149.841 1.00 60.91  ? 247  ASN A N     1 
ATOM   3367  C CA    . ASN D 4 250  ? 145.210 103.498 151.195 1.00 64.66  ? 247  ASN A CA    1 
ATOM   3368  C C     . ASN D 4 250  ? 146.557 103.649 151.888 1.00 69.90  ? 247  ASN A C     1 
ATOM   3369  O O     . ASN D 4 250  ? 146.707 104.498 152.775 1.00 72.91  ? 247  ASN A O     1 
ATOM   3370  C CB    . ASN D 4 250  ? 144.290 102.588 152.009 1.00 67.39  ? 247  ASN A CB    1 
ATOM   3371  C CG    . ASN D 4 250  ? 142.844 102.673 151.562 1.00 69.64  ? 247  ASN A CG    1 
ATOM   3372  O OD1   . ASN D 4 250  ? 142.362 103.739 151.183 1.00 69.29  ? 247  ASN A OD1   1 
ATOM   3373  N ND2   . ASN D 4 250  ? 142.144 101.544 151.602 1.00 72.35  ? 247  ASN A ND2   1 
ATOM   3374  N N     . GLN D 4 251  ? 147.546 102.844 151.499 1.00 73.18  ? 248  GLN A N     1 
ATOM   3375  C CA    . GLN D 4 251  ? 148.903 102.953 152.014 1.00 74.55  ? 248  GLN A CA    1 
ATOM   3376  C C     . GLN D 4 251  ? 149.803 103.785 151.107 1.00 69.59  ? 248  GLN A C     1 
ATOM   3377  O O     . GLN D 4 251  ? 151.028 103.634 151.152 1.00 69.26  ? 248  GLN A O     1 
ATOM   3378  C CB    . GLN D 4 251  ? 149.504 101.564 152.228 1.00 80.28  ? 248  GLN A CB    1 
ATOM   3379  C CG    . GLN D 4 251  ? 149.229 100.984 153.603 1.00 88.93  ? 248  GLN A CG    1 
ATOM   3380  C CD    . GLN D 4 251  ? 149.841 101.820 154.712 1.00 95.38  ? 248  GLN A CD    1 
ATOM   3381  O OE1   . GLN D 4 251  ? 151.063 101.932 154.819 1.00 96.87  ? 248  GLN A OE1   1 
ATOM   3382  N NE2   . GLN D 4 251  ? 148.992 102.419 155.541 1.00 97.77  ? 248  GLN A NE2   1 
ATOM   3383  N N     . LEU D 4 252  ? 149.219 104.651 150.284 1.00 67.16  ? 249  LEU A N     1 
ATOM   3384  C CA    . LEU D 4 252  ? 149.958 105.572 149.428 1.00 63.82  ? 249  LEU A CA    1 
ATOM   3385  C C     . LEU D 4 252  ? 149.484 106.997 149.655 1.00 61.36  ? 249  LEU A C     1 
ATOM   3386  O O     . LEU D 4 252  ? 149.406 107.807 148.727 1.00 58.60  ? 249  LEU A O     1 
ATOM   3387  C CB    . LEU D 4 252  ? 149.820 105.185 147.957 1.00 60.70  ? 249  LEU A CB    1 
ATOM   3388  C CG    . LEU D 4 252  ? 150.413 103.838 147.544 1.00 59.57  ? 249  LEU A CG    1 
ATOM   3389  C CD1   . LEU D 4 252  ? 150.232 103.619 146.051 1.00 58.03  ? 249  LEU A CD1   1 
ATOM   3390  C CD2   . LEU D 4 252  ? 151.882 103.757 147.930 1.00 57.69  ? 249  LEU A CD2   1 
ATOM   3391  N N     . LEU D 4 253  ? 149.159 107.324 150.905 1.00 60.30  ? 250  LEU A N     1 
ATOM   3392  C CA    . LEU D 4 253  ? 148.624 108.631 151.255 1.00 56.71  ? 250  LEU A CA    1 
ATOM   3393  C C     . LEU D 4 253  ? 149.608 109.490 152.036 1.00 58.98  ? 250  LEU A C     1 
ATOM   3394  O O     . LEU D 4 253  ? 149.298 110.649 152.329 1.00 60.11  ? 250  LEU A O     1 
ATOM   3395  C CB    . LEU D 4 253  ? 147.328 108.468 152.058 1.00 54.27  ? 250  LEU A CB    1 
ATOM   3396  C CG    . LEU D 4 253  ? 146.298 107.538 151.417 1.00 54.37  ? 250  LEU A CG    1 
ATOM   3397  C CD1   . LEU D 4 253  ? 145.034 107.479 152.251 1.00 55.48  ? 250  LEU A CD1   1 
ATOM   3398  C CD2   . LEU D 4 253  ? 145.984 107.975 149.994 1.00 54.61  ? 250  LEU A CD2   1 
ATOM   3399  N N     . THR D 4 254  ? 150.777 108.959 152.381 1.00 60.37  ? 251  THR A N     1 
ATOM   3400  C CA    . THR D 4 254  ? 151.804 109.714 153.079 1.00 64.42  ? 251  THR A CA    1 
ATOM   3401  C C     . THR D 4 254  ? 153.029 109.855 152.184 1.00 67.03  ? 251  THR A C     1 
ATOM   3402  O O     . THR D 4 254  ? 153.250 109.055 151.270 1.00 70.78  ? 251  THR A O     1 
ATOM   3403  C CB    . THR D 4 254  ? 152.188 109.048 154.406 1.00 65.68  ? 251  THR A CB    1 
ATOM   3404  O OG1   . THR D 4 254  ? 152.668 107.721 154.161 1.00 65.55  ? 251  THR A OG1   1 
ATOM   3405  C CG2   . THR D 4 254  ? 150.982 108.979 155.332 1.00 65.39  ? 251  THR A CG2   1 
ATOM   3406  N N     . GLN D 4 255  ? 153.829 110.886 152.464 1.00 66.58  ? 252  GLN A N     1 
ATOM   3407  C CA    . GLN D 4 255  ? 154.949 111.217 151.586 1.00 67.12  ? 252  GLN A CA    1 
ATOM   3408  C C     . GLN D 4 255  ? 155.983 110.097 151.550 1.00 71.85  ? 252  GLN A C     1 
ATOM   3409  O O     . GLN D 4 255  ? 156.522 109.779 150.483 1.00 70.80  ? 252  GLN A O     1 
ATOM   3410  C CB    . GLN D 4 255  ? 155.595 112.527 152.029 1.00 65.99  ? 252  GLN A CB    1 
ATOM   3411  C CG    . GLN D 4 255  ? 156.732 112.996 151.134 1.00 65.94  ? 252  GLN A CG    1 
ATOM   3412  C CD    . GLN D 4 255  ? 156.282 113.298 149.718 1.00 67.74  ? 252  GLN A CD    1 
ATOM   3413  O OE1   . GLN D 4 255  ? 155.114 113.604 149.476 1.00 68.38  ? 252  GLN A OE1   1 
ATOM   3414  N NE2   . GLN D 4 255  ? 157.208 113.213 148.770 1.00 68.41  ? 252  GLN A NE2   1 
ATOM   3415  N N     . THR D 4 256  ? 156.282 109.497 152.704 1.00 73.58  ? 253  THR A N     1 
ATOM   3416  C CA    . THR D 4 256  ? 157.258 108.412 152.735 1.00 73.69  ? 253  THR A CA    1 
ATOM   3417  C C     . THR D 4 256  ? 156.806 107.241 151.875 1.00 71.78  ? 253  THR A C     1 
ATOM   3418  O O     . THR D 4 256  ? 157.622 106.604 151.199 1.00 73.59  ? 253  THR A O     1 
ATOM   3419  C CB    . THR D 4 256  ? 157.504 107.959 154.174 1.00 75.01  ? 253  THR A CB    1 
ATOM   3420  O OG1   . THR D 4 256  ? 156.260 107.591 154.782 1.00 75.45  ? 253  THR A OG1   1 
ATOM   3421  C CG2   . THR D 4 256  ? 158.150 109.076 154.982 1.00 75.47  ? 253  THR A CG2   1 
ATOM   3422  N N     . GLN D 4 257  ? 155.504 106.949 151.875 1.00 69.16  ? 254  GLN A N     1 
ATOM   3423  C CA    . GLN D 4 257  ? 154.977 105.895 151.017 1.00 68.31  ? 254  GLN A CA    1 
ATOM   3424  C C     . GLN D 4 257  ? 154.905 106.344 149.562 1.00 67.81  ? 254  GLN A C     1 
ATOM   3425  O O     . GLN D 4 257  ? 155.151 105.545 148.651 1.00 66.41  ? 254  GLN A O     1 
ATOM   3426  C CB    . GLN D 4 257  ? 153.600 105.456 151.514 1.00 69.43  ? 254  GLN A CB    1 
ATOM   3427  C CG    . GLN D 4 257  ? 153.610 104.851 152.911 1.00 75.54  ? 254  GLN A CG    1 
ATOM   3428  C CD    . GLN D 4 257  ? 154.485 103.616 153.007 1.00 79.16  ? 254  GLN A CD    1 
ATOM   3429  O OE1   . GLN D 4 257  ? 155.501 103.615 153.703 1.00 80.83  ? 254  GLN A OE1   1 
ATOM   3430  N NE2   . GLN D 4 257  ? 154.092 102.555 152.312 1.00 79.30  ? 254  GLN A NE2   1 
ATOM   3431  N N     . ILE D 4 258  ? 154.569 107.614 149.325 1.00 65.99  ? 255  ILE A N     1 
ATOM   3432  C CA    . ILE D 4 258  ? 154.556 108.132 147.960 1.00 61.25  ? 255  ILE A CA    1 
ATOM   3433  C C     . ILE D 4 258  ? 155.970 108.163 147.389 1.00 63.78  ? 255  ILE A C     1 
ATOM   3434  O O     . ILE D 4 258  ? 156.181 107.863 146.207 1.00 63.80  ? 255  ILE A O     1 
ATOM   3435  C CB    . ILE D 4 258  ? 153.893 109.521 147.921 1.00 53.09  ? 255  ILE A CB    1 
ATOM   3436  C CG1   . ILE D 4 258  ? 152.395 109.406 148.218 1.00 50.59  ? 255  ILE A CG1   1 
ATOM   3437  C CG2   . ILE D 4 258  ? 154.112 110.193 146.573 1.00 49.91  ? 255  ILE A CG2   1 
ATOM   3438  C CD1   . ILE D 4 258  ? 151.675 110.736 148.254 1.00 44.29  ? 255  ILE A CD1   1 
ATOM   3439  N N     . ASP D 4 259  ? 156.957 108.515 148.215 1.00 67.25  ? 256  ASP A N     1 
ATOM   3440  C CA    . ASP D 4 259  ? 158.342 108.510 147.754 1.00 68.61  ? 256  ASP A CA    1 
ATOM   3441  C C     . ASP D 4 259  ? 158.806 107.099 147.414 1.00 67.87  ? 256  ASP A C     1 
ATOM   3442  O O     . ASP D 4 259  ? 159.453 106.887 146.380 1.00 67.13  ? 256  ASP A O     1 
ATOM   3443  C CB    . ASP D 4 259  ? 159.252 109.134 148.811 1.00 73.38  ? 256  ASP A CB    1 
ATOM   3444  C CG    . ASP D 4 259  ? 159.104 110.639 148.893 1.00 79.68  ? 256  ASP A CG    1 
ATOM   3445  O OD1   . ASP D 4 259  ? 158.819 111.269 147.852 1.00 80.20  ? 256  ASP A OD1   1 
ATOM   3446  O OD2   . ASP D 4 259  ? 159.276 111.195 149.999 1.00 84.04  ? 256  ASP A OD2   1 
ATOM   3447  N N     . LEU D 4 260  ? 158.490 106.124 148.268 1.00 67.44  ? 257  LEU A N     1 
ATOM   3448  C CA    . LEU D 4 260  ? 158.862 104.743 147.979 1.00 64.71  ? 257  LEU A CA    1 
ATOM   3449  C C     . LEU D 4 260  ? 158.161 104.234 146.726 1.00 59.16  ? 257  LEU A C     1 
ATOM   3450  O O     . LEU D 4 260  ? 158.751 103.488 145.936 1.00 57.24  ? 257  LEU A O     1 
ATOM   3451  C CB    . LEU D 4 260  ? 158.538 103.851 149.177 1.00 65.29  ? 257  LEU A CB    1 
ATOM   3452  C CG    . LEU D 4 260  ? 159.437 104.019 150.402 1.00 67.07  ? 257  LEU A CG    1 
ATOM   3453  C CD1   . LEU D 4 260  ? 158.932 103.165 151.552 1.00 69.56  ? 257  LEU A CD1   1 
ATOM   3454  C CD2   . LEU D 4 260  ? 160.875 103.664 150.055 1.00 66.65  ? 257  LEU A CD2   1 
ATOM   3455  N N     . TYR D 4 261  ? 156.902 104.628 146.528 1.00 56.17  ? 258  TYR A N     1 
ATOM   3456  C CA    . TYR D 4 261  ? 156.184 104.241 145.319 1.00 54.41  ? 258  TYR A CA    1 
ATOM   3457  C C     . TYR D 4 261  ? 156.818 104.860 144.080 1.00 56.04  ? 258  TYR A C     1 
ATOM   3458  O O     . TYR D 4 261  ? 156.976 104.187 143.054 1.00 57.15  ? 258  TYR A O     1 
ATOM   3459  C CB    . TYR D 4 261  ? 154.714 104.644 145.436 1.00 51.85  ? 258  TYR A CB    1 
ATOM   3460  C CG    . TYR D 4 261  ? 153.840 104.184 144.291 1.00 51.15  ? 258  TYR A CG    1 
ATOM   3461  C CD1   . TYR D 4 261  ? 153.299 102.905 144.278 1.00 53.44  ? 258  TYR A CD1   1 
ATOM   3462  C CD2   . TYR D 4 261  ? 153.541 105.032 143.233 1.00 49.86  ? 258  TYR A CD2   1 
ATOM   3463  C CE1   . TYR D 4 261  ? 152.493 102.480 143.238 1.00 53.30  ? 258  TYR A CE1   1 
ATOM   3464  C CE2   . TYR D 4 261  ? 152.735 104.615 142.187 1.00 47.62  ? 258  TYR A CE2   1 
ATOM   3465  C CZ    . TYR D 4 261  ? 152.214 103.339 142.196 1.00 49.77  ? 258  TYR A CZ    1 
ATOM   3466  O OH    . TYR D 4 261  ? 151.412 102.917 141.161 1.00 50.05  ? 258  TYR A OH    1 
ATOM   3467  N N     . ASN D 4 262  ? 157.194 106.139 144.156 1.00 54.59  ? 259  ASN A N     1 
ATOM   3468  C CA    . ASN D 4 262  ? 157.833 106.787 143.015 1.00 52.61  ? 259  ASN A CA    1 
ATOM   3469  C C     . ASN D 4 262  ? 159.221 106.221 142.747 1.00 53.01  ? 259  ASN A C     1 
ATOM   3470  O O     . ASN D 4 262  ? 159.660 106.186 141.590 1.00 51.79  ? 259  ASN A O     1 
ATOM   3471  C CB    . ASN D 4 262  ? 157.912 108.298 143.237 1.00 51.60  ? 259  ASN A CB    1 
ATOM   3472  C CG    . ASN D 4 262  ? 156.571 108.986 143.062 1.00 51.57  ? 259  ASN A CG    1 
ATOM   3473  O OD1   . ASN D 4 262  ? 155.650 108.431 142.464 1.00 53.47  ? 259  ASN A OD1   1 
ATOM   3474  N ND2   . ASN D 4 262  ? 156.460 110.206 143.575 1.00 50.65  ? 259  ASN A ND2   1 
ATOM   3475  N N     . GLN D 4 263  ? 159.927 105.774 143.788 1.00 54.76  ? 260  GLN A N     1 
ATOM   3476  C CA    . GLN D 4 263  ? 161.257 105.210 143.586 1.00 54.41  ? 260  GLN A CA    1 
ATOM   3477  C C     . GLN D 4 263  ? 161.197 103.786 143.048 1.00 54.43  ? 260  GLN A C     1 
ATOM   3478  O O     . GLN D 4 263  ? 162.148 103.335 142.400 1.00 53.01  ? 260  GLN A O     1 
ATOM   3479  C CB    . GLN D 4 263  ? 162.058 105.262 144.887 1.00 53.89  ? 260  GLN A CB    1 
ATOM   3480  C CG    . GLN D 4 263  ? 162.439 106.675 145.303 1.00 54.92  ? 260  GLN A CG    1 
ATOM   3481  C CD    . GLN D 4 263  ? 163.466 106.703 146.414 1.00 61.21  ? 260  GLN A CD    1 
ATOM   3482  O OE1   . GLN D 4 263  ? 163.122 106.818 147.590 1.00 64.38  ? 260  GLN A OE1   1 
ATOM   3483  N NE2   . GLN D 4 263  ? 164.738 106.605 146.046 1.00 63.27  ? 260  GLN A NE2   1 
ATOM   3484  N N     . LEU D 4 264  ? 160.103 103.065 143.304 1.00 54.91  ? 261  LEU A N     1 
ATOM   3485  C CA    . LEU D 4 264  ? 159.880 101.804 142.607 1.00 55.07  ? 261  LEU A CA    1 
ATOM   3486  C C     . LEU D 4 264  ? 159.725 102.029 141.110 1.00 53.74  ? 261  LEU A C     1 
ATOM   3487  O O     . LEU D 4 264  ? 160.142 101.187 140.306 1.00 52.88  ? 261  LEU A O     1 
ATOM   3488  C CB    . LEU D 4 264  ? 158.643 101.102 143.170 1.00 56.87  ? 261  LEU A CB    1 
ATOM   3489  C CG    . LEU D 4 264  ? 158.198 99.810  142.481 1.00 56.59  ? 261  LEU A CG    1 
ATOM   3490  C CD1   . LEU D 4 264  ? 159.214 98.699  142.700 1.00 57.02  ? 261  LEU A CD1   1 
ATOM   3491  C CD2   . LEU D 4 264  ? 156.818 99.385  142.961 1.00 56.90  ? 261  LEU A CD2   1 
ATOM   3492  N N     . LEU D 4 265  ? 159.141 103.164 140.719 1.00 55.18  ? 262  LEU A N     1 
ATOM   3493  C CA    . LEU D 4 265  ? 158.975 103.487 139.306 1.00 52.92  ? 262  LEU A CA    1 
ATOM   3494  C C     . LEU D 4 265  ? 160.240 104.099 138.718 1.00 51.37  ? 262  LEU A C     1 
ATOM   3495  O O     . LEU D 4 265  ? 160.555 103.867 137.544 1.00 50.02  ? 262  LEU A O     1 
ATOM   3496  C CB    . LEU D 4 265  ? 157.799 104.449 139.122 1.00 53.02  ? 262  LEU A CB    1 
ATOM   3497  C CG    . LEU D 4 265  ? 156.367 103.917 139.014 1.00 53.63  ? 262  LEU A CG    1 
ATOM   3498  C CD1   . LEU D 4 265  ? 155.988 103.056 140.206 1.00 56.55  ? 262  LEU A CD1   1 
ATOM   3499  C CD2   . LEU D 4 265  ? 155.398 105.081 138.870 1.00 53.02  ? 262  LEU A CD2   1 
ATOM   3500  N N     . GLY D 4 266  ? 160.974 104.878 139.510 1.00 48.62  ? 263  GLY A N     1 
ATOM   3501  C CA    . GLY D 4 266  ? 162.088 105.647 138.993 1.00 49.22  ? 263  GLY A CA    1 
ATOM   3502  C C     . GLY D 4 266  ? 163.461 105.088 139.304 1.00 51.70  ? 263  GLY A C     1 
ATOM   3503  O O     . GLY D 4 266  ? 164.444 105.457 138.654 1.00 50.97  ? 263  GLY A O     1 
ATOM   3504  N N     . GLY D 4 267  ? 163.551 104.205 140.296 1.00 53.73  ? 264  GLY A N     1 
ATOM   3505  C CA    . GLY D 4 267  ? 164.826 103.626 140.660 1.00 56.95  ? 264  GLY A CA    1 
ATOM   3506  C C     . GLY D 4 267  ? 165.608 104.498 141.622 1.00 59.64  ? 264  GLY A C     1 
ATOM   3507  O O     . GLY D 4 267  ? 165.178 105.572 142.045 1.00 62.18  ? 264  GLY A O     1 
ATOM   3508  N N     . LYS D 4 327  ? 167.447 137.219 144.435 1.00 105.25 ? 324  LYS A N     1 
ATOM   3509  C CA    . LYS D 4 327  ? 167.888 138.254 145.359 1.00 105.46 ? 324  LYS A CA    1 
ATOM   3510  C C     . LYS D 4 327  ? 169.107 139.038 144.890 1.00 106.48 ? 324  LYS A C     1 
ATOM   3511  O O     . LYS D 4 327  ? 169.382 140.105 145.450 1.00 106.46 ? 324  LYS A O     1 
ATOM   3512  C CB    . LYS D 4 327  ? 168.185 137.637 146.733 1.00 106.73 ? 324  LYS A CB    1 
ATOM   3513  C CG    . LYS D 4 327  ? 166.955 137.089 147.444 1.00 105.20 ? 324  LYS A CG    1 
ATOM   3514  C CD    . LYS D 4 327  ? 165.929 138.186 147.692 1.00 103.53 ? 324  LYS A CD    1 
ATOM   3515  C CE    . LYS D 4 327  ? 164.695 137.651 148.401 1.00 102.73 ? 324  LYS A CE    1 
ATOM   3516  N NZ    . LYS D 4 327  ? 163.686 138.725 148.639 1.00 99.75  ? 324  LYS A NZ    1 
ATOM   3517  N N     . SER D 4 328  ? 169.845 138.557 143.892 1.00 108.92 ? 325  SER A N     1 
ATOM   3518  C CA    . SER D 4 328  ? 171.047 139.256 143.458 1.00 112.73 ? 325  SER A CA    1 
ATOM   3519  C C     . SER D 4 328  ? 171.211 139.104 141.951 1.00 112.17 ? 325  SER A C     1 
ATOM   3520  O O     . SER D 4 328  ? 170.438 138.410 141.284 1.00 110.18 ? 325  SER A O     1 
ATOM   3521  C CB    . SER D 4 328  ? 172.285 138.747 144.207 1.00 117.56 ? 325  SER A CB    1 
ATOM   3522  O OG    . SER D 4 328  ? 172.641 137.441 143.790 1.00 118.93 ? 325  SER A OG    1 
ATOM   3523  N N     . ASP D 4 329  ? 172.238 139.768 141.420 1.00 114.71 ? 326  ASP A N     1 
ATOM   3524  C CA    . ASP D 4 329  ? 172.489 139.766 139.983 1.00 115.09 ? 326  ASP A CA    1 
ATOM   3525  C C     . ASP D 4 329  ? 173.103 138.448 139.528 1.00 117.19 ? 326  ASP A C     1 
ATOM   3526  O O     . ASP D 4 329  ? 172.667 137.862 138.531 1.00 116.07 ? 326  ASP A O     1 
ATOM   3527  C CB    . ASP D 4 329  ? 173.398 140.941 139.616 1.00 117.35 ? 326  ASP A CB    1 
ATOM   3528  C CG    . ASP D 4 329  ? 173.345 141.283 138.142 1.00 116.26 ? 326  ASP A CG    1 
ATOM   3529  O OD1   . ASP D 4 329  ? 174.133 140.701 137.366 1.00 118.06 ? 326  ASP A OD1   1 
ATOM   3530  O OD2   . ASP D 4 329  ? 172.516 142.136 137.762 1.00 113.92 ? 326  ASP A OD2   1 
ATOM   3531  N N     . GLU D 4 330  ? 174.116 137.966 140.248 1.00 120.49 ? 327  GLU A N     1 
ATOM   3532  C CA    . GLU D 4 330  ? 174.769 136.711 139.902 1.00 122.30 ? 327  GLU A CA    1 
ATOM   3533  C C     . GLU D 4 330  ? 173.954 135.488 140.298 1.00 122.50 ? 327  GLU A C     1 
ATOM   3534  O O     . GLU D 4 330  ? 174.265 134.385 139.834 1.00 122.41 ? 327  GLU A O     1 
ATOM   3535  C CB    . GLU D 4 330  ? 176.152 136.641 140.554 1.00 124.73 ? 327  GLU A CB    1 
ATOM   3536  N N     . GLU D 4 331  ? 172.929 135.649 141.140 1.00 121.40 ? 328  GLU A N     1 
ATOM   3537  C CA    . GLU D 4 331  ? 172.115 134.503 141.533 1.00 119.35 ? 328  GLU A CA    1 
ATOM   3538  C C     . GLU D 4 331  ? 171.344 133.943 140.344 1.00 116.34 ? 328  GLU A C     1 
ATOM   3539  O O     . GLU D 4 331  ? 171.158 132.726 140.237 1.00 115.25 ? 328  GLU A O     1 
ATOM   3540  C CB    . GLU D 4 331  ? 171.155 134.894 142.656 1.00 116.65 ? 328  GLU A CB    1 
ATOM   3541  C CG    . GLU D 4 331  ? 170.355 133.729 143.223 1.00 115.81 ? 328  GLU A CG    1 
ATOM   3542  C CD    . GLU D 4 331  ? 169.336 134.168 144.259 1.00 115.55 ? 328  GLU A CD    1 
ATOM   3543  O OE1   . GLU D 4 331  ? 169.174 135.390 144.457 1.00 114.69 ? 328  GLU A OE1   1 
ATOM   3544  O OE2   . GLU D 4 331  ? 168.695 133.290 144.876 1.00 116.52 ? 328  GLU A OE2   1 
ATOM   3545  N N     . VAL D 4 332  ? 170.891 134.813 139.440 1.00 118.09 ? 329  VAL A N     1 
ATOM   3546  C CA    . VAL D 4 332  ? 170.174 134.331 138.266 1.00 114.87 ? 329  VAL A CA    1 
ATOM   3547  C C     . VAL D 4 332  ? 171.135 133.690 137.276 1.00 116.01 ? 329  VAL A C     1 
ATOM   3548  O O     . VAL D 4 332  ? 170.740 132.821 136.492 1.00 116.94 ? 329  VAL A O     1 
ATOM   3549  C CB    . VAL D 4 332  ? 169.367 135.472 137.614 1.00 113.17 ? 329  VAL A CB    1 
ATOM   3550  C CG1   . VAL D 4 332  ? 168.601 136.248 138.670 1.00 112.44 ? 329  VAL A CG1   1 
ATOM   3551  C CG2   . VAL D 4 332  ? 170.275 136.399 136.818 1.00 114.05 ? 329  VAL A CG2   1 
ATOM   3552  N N     . ILE D 4 333  ? 172.407 134.092 137.293 1.00 116.48 ? 330  ILE A N     1 
ATOM   3553  C CA    . ILE D 4 333  ? 173.373 133.508 136.371 1.00 110.83 ? 330  ILE A CA    1 
ATOM   3554  C C     . ILE D 4 333  ? 173.891 132.179 136.905 1.00 108.13 ? 330  ILE A C     1 
ATOM   3555  O O     . ILE D 4 333  ? 174.023 131.209 136.155 1.00 107.26 ? 330  ILE A O     1 
ATOM   3556  C CB    . ILE D 4 333  ? 174.522 134.496 136.104 1.00 104.58 ? 330  ILE A CB    1 
ATOM   3557  C CG1   . ILE D 4 333  ? 173.970 135.853 135.668 1.00 96.96  ? 330  ILE A CG1   1 
ATOM   3558  C CG2   . ILE D 4 333  ? 175.460 133.945 135.042 1.00 103.21 ? 330  ILE A CG2   1 
ATOM   3559  C CD1   . ILE D 4 333  ? 175.042 136.889 135.417 1.00 95.34  ? 330  ILE A CD1   1 
ATOM   3560  N N     . GLN D 4 334  ? 174.186 132.114 138.205 1.00 108.13 ? 331  GLN A N     1 
ATOM   3561  C CA    . GLN D 4 334  ? 174.703 130.878 138.783 1.00 111.56 ? 331  GLN A CA    1 
ATOM   3562  C C     . GLN D 4 334  ? 173.633 129.793 138.819 1.00 112.21 ? 331  GLN A C     1 
ATOM   3563  O O     . GLN D 4 334  ? 173.928 128.615 138.589 1.00 113.89 ? 331  GLN A O     1 
ATOM   3564  C CB    . GLN D 4 334  ? 175.249 131.143 140.185 1.00 113.13 ? 331  GLN A CB    1 
ATOM   3565  N N     . SER D 4 335  ? 172.383 130.171 139.102 1.00 110.88 ? 332  SER A N     1 
ATOM   3566  C CA    . SER D 4 335  ? 171.315 129.178 139.186 1.00 109.08 ? 332  SER A CA    1 
ATOM   3567  C C     . SER D 4 335  ? 170.898 128.693 137.804 1.00 106.57 ? 332  SER A C     1 
ATOM   3568  O O     . SER D 4 335  ? 170.687 127.492 137.599 1.00 105.31 ? 332  SER A O     1 
ATOM   3569  C CB    . SER D 4 335  ? 170.115 129.757 139.935 1.00 107.27 ? 332  SER A CB    1 
ATOM   3570  O OG    . SER D 4 335  ? 169.077 128.800 140.051 1.00 107.23 ? 332  SER A OG    1 
ATOM   3571  N N     . PHE D 4 336  ? 170.765 129.613 136.843 1.00 104.19 ? 333  PHE A N     1 
ATOM   3572  C CA    . PHE D 4 336  ? 170.380 129.213 135.493 1.00 100.04 ? 333  PHE A CA    1 
ATOM   3573  C C     . PHE D 4 336  ? 171.471 128.376 134.842 1.00 102.92 ? 333  PHE A C     1 
ATOM   3574  O O     . PHE D 4 336  ? 171.192 127.316 134.270 1.00 103.05 ? 333  PHE A O     1 
ATOM   3575  C CB    . PHE D 4 336  ? 170.063 130.447 134.647 1.00 94.00  ? 333  PHE A CB    1 
ATOM   3576  C CG    . PHE D 4 336  ? 169.583 130.127 133.259 1.00 90.46  ? 333  PHE A CG    1 
ATOM   3577  C CD1   . PHE D 4 336  ? 168.507 129.282 133.064 1.00 87.98  ? 333  PHE A CD1   1 
ATOM   3578  C CD2   . PHE D 4 336  ? 170.200 130.688 132.152 1.00 90.37  ? 333  PHE A CD2   1 
ATOM   3579  C CE1   . PHE D 4 336  ? 168.060 128.987 131.789 1.00 86.69  ? 333  PHE A CE1   1 
ATOM   3580  C CE2   . PHE D 4 336  ? 169.757 130.400 130.874 1.00 88.66  ? 333  PHE A CE2   1 
ATOM   3581  C CZ    . PHE D 4 336  ? 168.684 129.547 130.693 1.00 86.79  ? 333  PHE A CZ    1 
ATOM   3582  N N     . CYS D 4 337  ? 172.725 128.828 134.931 1.00 107.47 ? 334  CYS A N     1 
ATOM   3583  C CA    . CYS D 4 337  ? 173.831 128.059 134.369 1.00 110.44 ? 334  CYS A CA    1 
ATOM   3584  C C     . CYS D 4 337  ? 173.963 126.698 135.037 1.00 113.43 ? 334  CYS A C     1 
ATOM   3585  O O     . CYS D 4 337  ? 174.417 125.738 134.402 1.00 114.52 ? 334  CYS A O     1 
ATOM   3586  C CB    . CYS D 4 337  ? 175.138 128.844 134.494 1.00 113.73 ? 334  CYS A CB    1 
ATOM   3587  S SG    . CYS D 4 337  ? 176.573 128.052 133.733 1.00 118.68 ? 334  CYS A SG    1 
ATOM   3588  N N     . LYS D 4 338  ? 173.576 126.590 136.310 1.00 115.22 ? 335  LYS A N     1 
ATOM   3589  C CA    . LYS D 4 338  ? 173.556 125.284 136.964 1.00 117.67 ? 335  LYS A CA    1 
ATOM   3590  C C     . LYS D 4 338  ? 172.439 124.411 136.406 1.00 115.38 ? 335  LYS A C     1 
ATOM   3591  O O     . LYS D 4 338  ? 172.641 123.218 136.158 1.00 116.32 ? 335  LYS A O     1 
ATOM   3592  C CB    . LYS D 4 338  ? 173.406 125.452 138.476 1.00 118.16 ? 335  LYS A CB    1 
ATOM   3593  N N     . TYR D 4 339  ? 171.252 124.989 136.205 1.00 111.45 ? 336  TYR A N     1 
ATOM   3594  C CA    . TYR D 4 339  ? 170.180 124.258 135.540 1.00 107.89 ? 336  TYR A CA    1 
ATOM   3595  C C     . TYR D 4 339  ? 170.466 124.083 134.055 1.00 102.25 ? 336  TYR A C     1 
ATOM   3596  O O     . TYR D 4 339  ? 170.062 123.077 133.461 1.00 101.75 ? 336  TYR A O     1 
ATOM   3597  C CB    . TYR D 4 339  ? 168.847 124.979 135.747 1.00 108.02 ? 336  TYR A CB    1 
ATOM   3598  C CG    . TYR D 4 339  ? 167.735 124.515 134.832 1.00 107.66 ? 336  TYR A CG    1 
ATOM   3599  C CD1   . TYR D 4 339  ? 167.038 123.342 135.092 1.00 108.62 ? 336  TYR A CD1   1 
ATOM   3600  C CD2   . TYR D 4 339  ? 167.376 125.255 133.712 1.00 105.60 ? 336  TYR A CD2   1 
ATOM   3601  C CE1   . TYR D 4 339  ? 166.019 122.918 134.260 1.00 106.67 ? 336  TYR A CE1   1 
ATOM   3602  C CE2   . TYR D 4 339  ? 166.361 124.838 132.874 1.00 103.47 ? 336  TYR A CE2   1 
ATOM   3603  C CZ    . TYR D 4 339  ? 165.684 123.670 133.153 1.00 104.20 ? 336  TYR A CZ    1 
ATOM   3604  O OH    . TYR D 4 339  ? 164.671 123.249 132.321 1.00 102.33 ? 336  TYR A OH    1 
ATOM   3605  N N     . LYS D 4 340  ? 171.160 125.045 133.447 1.00 97.81  ? 337  LYS A N     1 
ATOM   3606  C CA    . LYS D 4 340  ? 171.498 124.938 132.033 1.00 94.74  ? 337  LYS A CA    1 
ATOM   3607  C C     . LYS D 4 340  ? 172.504 123.816 131.794 1.00 98.35  ? 337  LYS A C     1 
ATOM   3608  O O     . LYS D 4 340  ? 172.335 123.007 130.876 1.00 98.39  ? 337  LYS A O     1 
ATOM   3609  C CB    . LYS D 4 340  ? 172.038 126.277 131.532 1.00 92.46  ? 337  LYS A CB    1 
ATOM   3610  C CG    . LYS D 4 340  ? 172.398 126.321 130.066 1.00 90.58  ? 337  LYS A CG    1 
ATOM   3611  C CD    . LYS D 4 340  ? 172.571 127.758 129.619 1.00 88.48  ? 337  LYS A CD    1 
ATOM   3612  C CE    . LYS D 4 340  ? 173.447 127.848 128.390 1.00 89.72  ? 337  LYS A CE    1 
ATOM   3613  N NZ    . LYS D 4 340  ? 173.549 129.238 127.873 1.00 88.85  ? 337  LYS A NZ    1 
ATOM   3614  N N     . THR D 4 341  ? 173.549 123.744 132.624 1.00 100.96 ? 338  THR A N     1 
ATOM   3615  C CA    . THR D 4 341  ? 174.528 122.671 132.486 1.00 101.82 ? 338  THR A CA    1 
ATOM   3616  C C     . THR D 4 341  ? 173.949 121.313 132.860 1.00 101.52 ? 338  THR A C     1 
ATOM   3617  O O     . THR D 4 341  ? 174.520 120.283 132.481 1.00 102.56 ? 338  THR A O     1 
ATOM   3618  C CB    . THR D 4 341  ? 175.769 122.964 133.337 1.00 103.05 ? 338  THR A CB    1 
ATOM   3619  O OG1   . THR D 4 341  ? 176.847 122.116 132.920 1.00 106.87 ? 338  THR A OG1   1 
ATOM   3620  C CG2   . THR D 4 341  ? 175.490 122.710 134.812 1.00 102.09 ? 338  THR A CG2   1 
ATOM   3621  N N     . LEU D 4 342  ? 172.829 121.288 133.588 1.00 102.17 ? 339  LEU A N     1 
ATOM   3622  C CA    . LEU D 4 342  ? 172.155 120.032 133.893 1.00 103.53 ? 339  LEU A CA    1 
ATOM   3623  C C     . LEU D 4 342  ? 171.425 119.474 132.678 1.00 102.63 ? 339  LEU A C     1 
ATOM   3624  O O     . LEU D 4 342  ? 171.257 118.254 132.566 1.00 101.63 ? 339  LEU A O     1 
ATOM   3625  C CB    . LEU D 4 342  ? 171.182 120.236 135.058 1.00 104.21 ? 339  LEU A CB    1 
ATOM   3626  C CG    . LEU D 4 342  ? 170.439 119.025 135.626 1.00 106.12 ? 339  LEU A CG    1 
ATOM   3627  C CD1   . LEU D 4 342  ? 170.353 119.130 137.137 1.00 108.19 ? 339  LEU A CD1   1 
ATOM   3628  C CD2   . LEU D 4 342  ? 169.048 118.914 135.029 1.00 104.03 ? 339  LEU A CD2   1 
ATOM   3629  N N     . LEU D 4 343  ? 170.996 120.342 131.758 1.00 102.68 ? 340  LEU A N     1 
ATOM   3630  C CA    . LEU D 4 343  ? 170.318 119.884 130.553 1.00 102.74 ? 340  LEU A CA    1 
ATOM   3631  C C     . LEU D 4 343  ? 171.265 119.192 129.584 1.00 104.95 ? 340  LEU A C     1 
ATOM   3632  O O     . LEU D 4 343  ? 170.815 118.369 128.782 1.00 104.96 ? 340  LEU A O     1 
ATOM   3633  C CB    . LEU D 4 343  ? 169.627 121.061 129.862 1.00 101.14 ? 340  LEU A CB    1 
ATOM   3634  C CG    . LEU D 4 343  ? 168.570 121.799 130.688 1.00 98.30  ? 340  LEU A CG    1 
ATOM   3635  C CD1   . LEU D 4 343  ? 168.112 123.058 129.974 1.00 94.25  ? 340  LEU A CD1   1 
ATOM   3636  C CD2   . LEU D 4 343  ? 167.387 120.892 130.989 1.00 96.62  ? 340  LEU A CD2   1 
ATOM   3637  N N     . ARG D 4 344  ? 172.562 119.506 129.636 1.00 107.33 ? 341  ARG A N     1 
ATOM   3638  C CA    . ARG D 4 344  ? 173.521 118.806 128.788 1.00 110.50 ? 341  ARG A CA    1 
ATOM   3639  C C     . ARG D 4 344  ? 173.769 117.390 129.292 1.00 113.25 ? 341  ARG A C     1 
ATOM   3640  O O     . ARG D 4 344  ? 173.809 116.441 128.501 1.00 113.74 ? 341  ARG A O     1 
ATOM   3641  C CB    . ARG D 4 344  ? 174.841 119.577 128.716 1.00 113.99 ? 341  ARG A CB    1 
ATOM   3642  C CG    . ARG D 4 344  ? 174.817 120.850 127.883 1.00 113.53 ? 341  ARG A CG    1 
ATOM   3643  C CD    . ARG D 4 344  ? 174.333 122.036 128.698 1.00 113.95 ? 341  ARG A CD    1 
ATOM   3644  N NE    . ARG D 4 344  ? 175.014 123.275 128.333 1.00 115.55 ? 341  ARG A NE    1 
ATOM   3645  C CZ    . ARG D 4 344  ? 176.118 123.719 128.923 1.00 118.46 ? 341  ARG A CZ    1 
ATOM   3646  N NH1   . ARG D 4 344  ? 176.674 123.025 129.906 1.00 121.22 ? 341  ARG A NH1   1 
ATOM   3647  N NH2   . ARG D 4 344  ? 176.671 124.859 128.530 1.00 118.53 ? 341  ARG A NH2   1 
ATOM   3648  N N     . ASN D 4 345  ? 173.939 117.232 130.608 1.00 114.62 ? 342  ASN A N     1 
ATOM   3649  C CA    . ASN D 4 345  ? 174.245 115.918 131.166 1.00 116.13 ? 342  ASN A CA    1 
ATOM   3650  C C     . ASN D 4 345  ? 173.081 114.951 130.985 1.00 115.20 ? 342  ASN A C     1 
ATOM   3651  O O     . ASN D 4 345  ? 173.288 113.771 130.684 1.00 116.25 ? 342  ASN A O     1 
ATOM   3652  C CB    . ASN D 4 345  ? 174.613 116.050 132.643 1.00 116.22 ? 342  ASN A CB    1 
ATOM   3653  C CG    . ASN D 4 345  ? 175.770 117.008 132.873 1.00 116.84 ? 342  ASN A CG    1 
ATOM   3654  O OD1   . ASN D 4 345  ? 176.627 117.183 132.009 1.00 117.55 ? 342  ASN A OD1   1 
ATOM   3655  N ND2   . ASN D 4 345  ? 175.795 117.633 134.044 1.00 116.72 ? 342  ASN A ND2   1 
ATOM   3656  N N     . GLU D 4 346  ? 171.848 115.433 131.164 1.00 111.92 ? 343  GLU A N     1 
ATOM   3657  C CA    . GLU D 4 346  ? 170.681 114.595 130.912 1.00 109.11 ? 343  GLU A CA    1 
ATOM   3658  C C     . GLU D 4 346  ? 170.444 114.375 129.425 1.00 107.79 ? 343  GLU A C     1 
ATOM   3659  O O     . GLU D 4 346  ? 169.691 113.464 129.060 1.00 105.60 ? 343  GLU A O     1 
ATOM   3660  C CB    . GLU D 4 346  ? 169.436 115.213 131.549 1.00 104.32 ? 343  GLU A CB    1 
ATOM   3661  C CG    . GLU D 4 346  ? 169.430 115.185 133.068 1.00 103.95 ? 343  GLU A CG    1 
ATOM   3662  C CD    . GLU D 4 346  ? 168.211 115.866 133.661 1.00 101.05 ? 343  GLU A CD    1 
ATOM   3663  O OE1   . GLU D 4 346  ? 167.624 116.735 132.982 1.00 98.91  ? 343  GLU A OE1   1 
ATOM   3664  O OE2   . GLU D 4 346  ? 167.839 115.532 134.806 1.00 101.42 ? 343  GLU A OE2   1 
ATOM   3665  N N     . ASN D 4 347  ? 171.065 115.186 128.565 1.00 109.45 ? 344  ASN A N     1 
ATOM   3666  C CA    . ASN D 4 347  ? 170.912 115.086 127.114 1.00 109.06 ? 344  ASN A CA    1 
ATOM   3667  C C     . ASN D 4 347  ? 169.439 115.169 126.712 1.00 105.87 ? 344  ASN A C     1 
ATOM   3668  O O     . ASN D 4 347  ? 168.941 114.380 125.907 1.00 104.52 ? 344  ASN A O     1 
ATOM   3669  C CB    . ASN D 4 347  ? 171.560 113.804 126.579 1.00 111.26 ? 344  ASN A CB    1 
ATOM   3670  N N     . VAL D 4 348  ? 168.737 116.146 127.290 1.00 105.13 ? 345  VAL A N     1 
ATOM   3671  C CA    . VAL D 4 348  ? 167.314 116.297 127.006 1.00 103.11 ? 345  VAL A CA    1 
ATOM   3672  C C     . VAL D 4 348  ? 167.092 116.795 125.586 1.00 101.24 ? 345  VAL A C     1 
ATOM   3673  O O     . VAL D 4 348  ? 166.055 116.505 124.976 1.00 97.55  ? 345  VAL A O     1 
ATOM   3674  C CB    . VAL D 4 348  ? 166.650 117.224 128.043 1.00 102.40 ? 345  VAL A CB    1 
ATOM   3675  C CG1   . VAL D 4 348  ? 166.738 116.612 129.430 1.00 104.27 ? 345  VAL A CG1   1 
ATOM   3676  C CG2   . VAL D 4 348  ? 167.296 118.600 128.022 1.00 103.47 ? 345  VAL A CG2   1 
ATOM   3677  N N     . LEU D 4 349  ? 168.045 117.547 125.030 1.00 103.31 ? 346  LEU A N     1 
ATOM   3678  C CA    . LEU D 4 349  ? 167.930 117.953 123.633 1.00 101.76 ? 346  LEU A CA    1 
ATOM   3679  C C     . LEU D 4 349  ? 168.039 116.752 122.704 1.00 100.10 ? 346  LEU A C     1 
ATOM   3680  O O     . LEU D 4 349  ? 167.233 116.594 121.782 1.00 97.78  ? 346  LEU A O     1 
ATOM   3681  C CB    . LEU D 4 349  ? 168.988 119.008 123.284 1.00 105.30 ? 346  LEU A CB    1 
ATOM   3682  C CG    . LEU D 4 349  ? 170.318 119.177 124.033 1.00 110.95 ? 346  LEU A CG    1 
ATOM   3683  C CD1   . LEU D 4 349  ? 171.128 117.892 124.137 1.00 113.43 ? 346  LEU A CD1   1 
ATOM   3684  C CD2   . LEU D 4 349  ? 171.139 120.251 123.337 1.00 112.56 ? 346  LEU A CD2   1 
ATOM   3685  N N     . GLU D 4 350  ? 169.026 115.884 122.943 1.00 102.06 ? 347  GLU A N     1 
ATOM   3686  C CA    . GLU D 4 350  ? 169.186 114.700 122.105 1.00 100.49 ? 347  GLU A CA    1 
ATOM   3687  C C     . GLU D 4 350  ? 167.992 113.765 122.244 1.00 96.96  ? 347  GLU A C     1 
ATOM   3688  O O     . GLU D 4 350  ? 167.574 113.130 121.269 1.00 93.08  ? 347  GLU A O     1 
ATOM   3689  C CB    . GLU D 4 350  ? 170.483 113.975 122.464 1.00 102.99 ? 347  GLU A CB    1 
ATOM   3690  N N     . THR D 4 351  ? 167.428 113.671 123.449 1.00 98.00  ? 348  THR A N     1 
ATOM   3691  C CA    . THR D 4 351  ? 166.235 112.854 123.640 1.00 96.48  ? 348  THR A CA    1 
ATOM   3692  C C     . THR D 4 351  ? 165.029 113.473 122.945 1.00 93.15  ? 348  THR A C     1 
ATOM   3693  O O     . THR D 4 351  ? 164.207 112.759 122.360 1.00 92.60  ? 348  THR A O     1 
ATOM   3694  C CB    . THR D 4 351  ? 165.955 112.669 125.132 1.00 95.65  ? 348  THR A CB    1 
ATOM   3695  O OG1   . THR D 4 351  ? 167.155 112.253 125.797 1.00 98.29  ? 348  THR A OG1   1 
ATOM   3696  C CG2   . THR D 4 351  ? 164.877 111.619 125.347 1.00 93.45  ? 348  THR A CG2   1 
ATOM   3697  N N     . ALA D 4 352  ? 164.910 114.802 122.996 1.00 91.33  ? 349  ALA A N     1 
ATOM   3698  C CA    . ALA D 4 352  ? 163.802 115.472 122.323 1.00 88.04  ? 349  ALA A CA    1 
ATOM   3699  C C     . ALA D 4 352  ? 163.954 115.413 120.809 1.00 88.99  ? 349  ALA A C     1 
ATOM   3700  O O     . ALA D 4 352  ? 162.980 115.165 120.090 1.00 86.44  ? 349  ALA A O     1 
ATOM   3701  C CB    . ALA D 4 352  ? 163.697 116.922 122.796 1.00 87.74  ? 349  ALA A CB    1 
ATOM   3702  N N     . GLU D 4 353  ? 165.172 115.637 120.305 1.00 92.33  ? 350  GLU A N     1 
ATOM   3703  C CA    . GLU D 4 353  ? 165.403 115.546 118.866 1.00 92.52  ? 350  GLU A CA    1 
ATOM   3704  C C     . GLU D 4 353  ? 165.153 114.135 118.349 1.00 91.73  ? 350  GLU A C     1 
ATOM   3705  O O     . GLU D 4 353  ? 164.769 113.958 117.188 1.00 90.57  ? 350  GLU A O     1 
ATOM   3706  C CB    . GLU D 4 353  ? 166.826 115.997 118.530 1.00 94.61  ? 350  GLU A CB    1 
ATOM   3707  C CG    . GLU D 4 353  ? 167.097 117.470 118.808 1.00 95.40  ? 350  GLU A CG    1 
ATOM   3708  C CD    . GLU D 4 353  ? 168.574 117.815 118.762 1.00 99.29  ? 350  GLU A CD    1 
ATOM   3709  O OE1   . GLU D 4 353  ? 169.299 117.234 117.924 1.00 100.83 ? 350  GLU A OE1   1 
ATOM   3710  O OE2   . GLU D 4 353  ? 169.016 118.663 119.568 1.00 100.16 ? 350  GLU A OE2   1 
ATOM   3711  N N     . ALA D 4 354  ? 165.358 113.122 119.195 1.00 92.39  ? 351  ALA A N     1 
ATOM   3712  C CA    . ALA D 4 354  ? 165.098 111.746 118.789 1.00 91.05  ? 351  ALA A CA    1 
ATOM   3713  C C     . ALA D 4 354  ? 163.611 111.415 118.803 1.00 87.24  ? 351  ALA A C     1 
ATOM   3714  O O     . ALA D 4 354  ? 163.155 110.607 117.985 1.00 87.35  ? 351  ALA A O     1 
ATOM   3715  C CB    . ALA D 4 354  ? 165.858 110.776 119.695 1.00 94.16  ? 351  ALA A CB    1 
ATOM   3716  N N     . LEU D 4 355  ? 162.845 112.020 119.713 1.00 84.23  ? 352  LEU A N     1 
ATOM   3717  C CA    . LEU D 4 355  ? 161.410 111.758 119.765 1.00 77.51  ? 352  LEU A CA    1 
ATOM   3718  C C     . LEU D 4 355  ? 160.704 112.320 118.539 1.00 73.06  ? 352  LEU A C     1 
ATOM   3719  O O     . LEU D 4 355  ? 159.888 111.634 117.912 1.00 72.80  ? 352  LEU A O     1 
ATOM   3720  C CB    . LEU D 4 355  ? 160.809 112.345 121.042 1.00 73.00  ? 352  LEU A CB    1 
ATOM   3721  C CG    . LEU D 4 355  ? 160.895 111.472 122.291 1.00 73.05  ? 352  LEU A CG    1 
ATOM   3722  C CD1   . LEU D 4 355  ? 160.141 112.123 123.436 1.00 72.47  ? 352  LEU A CD1   1 
ATOM   3723  C CD2   . LEU D 4 355  ? 160.352 110.081 122.006 1.00 72.02  ? 352  LEU A CD2   1 
ATOM   3724  N N     . PHE D 4 356  ? 160.994 113.574 118.188 1.00 71.29  ? 353  PHE A N     1 
ATOM   3725  C CA    . PHE D 4 356  ? 160.363 114.170 117.018 1.00 71.33  ? 353  PHE A CA    1 
ATOM   3726  C C     . PHE D 4 356  ? 160.831 113.524 115.721 1.00 74.85  ? 353  PHE A C     1 
ATOM   3727  O O     . PHE D 4 356  ? 160.111 113.585 114.719 1.00 74.54  ? 353  PHE A O     1 
ATOM   3728  C CB    . PHE D 4 356  ? 160.622 115.676 116.990 1.00 70.58  ? 353  PHE A CB    1 
ATOM   3729  C CG    . PHE D 4 356  ? 159.883 116.433 118.056 1.00 71.19  ? 353  PHE A CG    1 
ATOM   3730  C CD1   . PHE D 4 356  ? 158.558 116.795 117.874 1.00 70.15  ? 353  PHE A CD1   1 
ATOM   3731  C CD2   . PHE D 4 356  ? 160.511 116.779 119.240 1.00 72.74  ? 353  PHE A CD2   1 
ATOM   3732  C CE1   . PHE D 4 356  ? 157.874 117.487 118.855 1.00 69.49  ? 353  PHE A CE1   1 
ATOM   3733  C CE2   . PHE D 4 356  ? 159.833 117.473 120.224 1.00 71.46  ? 353  PHE A CE2   1 
ATOM   3734  C CZ    . PHE D 4 356  ? 158.514 117.827 120.031 1.00 70.08  ? 353  PHE A CZ    1 
ATOM   3735  N N     . ASN D 4 357  ? 162.012 112.907 115.719 1.00 78.80  ? 354  ASN A N     1 
ATOM   3736  C CA    . ASN D 4 357  ? 162.442 112.130 114.564 1.00 80.91  ? 354  ASN A CA    1 
ATOM   3737  C C     . ASN D 4 357  ? 161.736 110.785 114.479 1.00 81.70  ? 354  ASN A C     1 
ATOM   3738  O O     . ASN D 4 357  ? 161.624 110.226 113.381 1.00 80.63  ? 354  ASN A O     1 
ATOM   3739  C CB    . ASN D 4 357  ? 163.957 111.926 114.596 1.00 85.48  ? 354  ASN A CB    1 
ATOM   3740  C CG    . ASN D 4 357  ? 164.487 111.295 113.325 1.00 88.53  ? 354  ASN A CG    1 
ATOM   3741  O OD1   . ASN D 4 357  ? 164.756 110.095 113.279 1.00 90.33  ? 354  ASN A OD1   1 
ATOM   3742  N ND2   . ASN D 4 357  ? 164.633 112.101 112.280 1.00 88.81  ? 354  ASN A ND2   1 
ATOM   3743  N N     . GLU D 4 358  ? 161.250 110.257 115.607 1.00 82.95  ? 355  GLU A N     1 
ATOM   3744  C CA    . GLU D 4 358  ? 160.464 109.028 115.575 1.00 82.30  ? 355  GLU A CA    1 
ATOM   3745  C C     . GLU D 4 358  ? 159.153 109.220 114.827 1.00 75.99  ? 355  GLU A C     1 
ATOM   3746  O O     . GLU D 4 358  ? 158.625 108.264 114.244 1.00 72.20  ? 355  GLU A O     1 
ATOM   3747  C CB    . GLU D 4 358  ? 160.178 108.541 116.998 1.00 85.13  ? 355  GLU A CB    1 
ATOM   3748  C CG    . GLU D 4 358  ? 161.254 107.656 117.601 1.00 89.31  ? 355  GLU A CG    1 
ATOM   3749  C CD    . GLU D 4 358  ? 160.867 107.138 118.972 1.00 91.80  ? 355  GLU A CD    1 
ATOM   3750  O OE1   . GLU D 4 358  ? 159.912 106.335 119.057 1.00 94.59  ? 355  GLU A OE1   1 
ATOM   3751  O OE2   . GLU D 4 358  ? 161.506 107.539 119.968 1.00 90.93  ? 355  GLU A OE2   1 
ATOM   3752  N N     . LEU D 4 359  ? 158.616 110.441 114.822 1.00 75.35  ? 356  LEU A N     1 
ATOM   3753  C CA    . LEU D 4 359  ? 157.312 110.696 114.219 1.00 72.72  ? 356  LEU A CA    1 
ATOM   3754  C C     . LEU D 4 359  ? 157.299 110.483 112.712 1.00 75.05  ? 356  LEU A C     1 
ATOM   3755  O O     . LEU D 4 359  ? 156.218 110.495 112.113 1.00 75.40  ? 356  LEU A O     1 
ATOM   3756  C CB    . LEU D 4 359  ? 156.864 112.124 114.544 1.00 66.63  ? 356  LEU A CB    1 
ATOM   3757  C CG    . LEU D 4 359  ? 156.801 112.483 116.030 1.00 61.22  ? 356  LEU A CG    1 
ATOM   3758  C CD1   . LEU D 4 359  ? 156.495 113.958 116.208 1.00 58.93  ? 356  LEU A CD1   1 
ATOM   3759  C CD2   . LEU D 4 359  ? 155.768 111.628 116.750 1.00 58.90  ? 356  LEU A CD2   1 
ATOM   3760  N N     . ASN D 4 360  ? 158.460 110.284 112.085 1.00 79.90  ? 357  ASN A N     1 
ATOM   3761  C CA    . ASN D 4 360  ? 158.510 110.056 110.647 1.00 80.98  ? 357  ASN A CA    1 
ATOM   3762  C C     . ASN D 4 360  ? 158.223 108.610 110.268 1.00 81.94  ? 357  ASN A C     1 
ATOM   3763  O O     . ASN D 4 360  ? 157.928 108.339 109.099 1.00 83.54  ? 357  ASN A O     1 
ATOM   3764  C CB    . ASN D 4 360  ? 159.879 110.458 110.096 1.00 85.08  ? 357  ASN A CB    1 
ATOM   3765  C CG    . ASN D 4 360  ? 160.286 111.854 110.509 1.00 89.55  ? 357  ASN A CG    1 
ATOM   3766  O OD1   . ASN D 4 360  ? 159.854 112.840 109.918 1.00 90.12  ? 357  ASN A OD1   1 
ATOM   3767  N ND2   . ASN D 4 360  ? 161.125 111.944 111.535 1.00 92.49  ? 357  ASN A ND2   1 
ATOM   3768  N N     . SER D 4 361  ? 158.298 107.681 111.219 1.00 81.07  ? 358  SER A N     1 
ATOM   3769  C CA    . SER D 4 361  ? 158.128 106.264 110.922 1.00 79.32  ? 358  SER A CA    1 
ATOM   3770  C C     . SER D 4 361  ? 157.161 105.534 111.843 1.00 78.85  ? 358  SER A C     1 
ATOM   3771  O O     . SER D 4 361  ? 156.620 104.502 111.430 1.00 76.86  ? 358  SER A O     1 
ATOM   3772  C CB    . SER D 4 361  ? 159.483 105.543 110.966 1.00 80.39  ? 358  SER A CB    1 
ATOM   3773  O OG    . SER D 4 361  ? 160.115 105.720 112.222 1.00 81.35  ? 358  SER A OG    1 
ATOM   3774  N N     . ILE D 4 362  ? 156.919 106.020 113.059 1.00 79.87  ? 359  ILE A N     1 
ATOM   3775  C CA    . ILE D 4 362  ? 156.055 105.312 113.997 1.00 79.86  ? 359  ILE A CA    1 
ATOM   3776  C C     . ILE D 4 362  ? 154.595 105.551 113.639 1.00 80.13  ? 359  ILE A C     1 
ATOM   3777  O O     . ILE D 4 362  ? 154.278 106.397 112.795 1.00 81.13  ? 359  ILE A O     1 
ATOM   3778  C CB    . ILE D 4 362  ? 156.339 105.732 115.451 1.00 74.89  ? 359  ILE A CB    1 
ATOM   3779  C CG1   . ILE D 4 362  ? 155.934 107.189 115.677 1.00 68.22  ? 359  ILE A CG1   1 
ATOM   3780  C CG2   . ILE D 4 362  ? 157.806 105.512 115.792 1.00 76.10  ? 359  ILE A CG2   1 
ATOM   3781  C CD1   . ILE D 4 362  ? 156.108 107.657 117.104 1.00 64.70  ? 359  ILE A CD1   1 
ATOM   3782  N N     . ASP D 4 363  ? 153.700 104.804 114.282 1.00 78.63  ? 360  ASP A N     1 
ATOM   3783  C CA    . ASP D 4 363  ? 152.267 104.914 114.028 1.00 75.85  ? 360  ASP A CA    1 
ATOM   3784  C C     . ASP D 4 363  ? 151.741 106.211 114.634 1.00 73.17  ? 360  ASP A C     1 
ATOM   3785  O O     . ASP D 4 363  ? 151.736 106.376 115.857 1.00 72.35  ? 360  ASP A O     1 
ATOM   3786  C CB    . ASP D 4 363  ? 151.544 103.702 114.608 1.00 78.71  ? 360  ASP A CB    1 
ATOM   3787  C CG    . ASP D 4 363  ? 150.049 103.736 114.355 1.00 80.24  ? 360  ASP A CG    1 
ATOM   3788  O OD1   . ASP D 4 363  ? 149.618 104.403 113.392 1.00 81.36  ? 360  ASP A OD1   1 
ATOM   3789  O OD2   . ASP D 4 363  ? 149.307 103.086 115.120 1.00 80.57  ? 360  ASP A OD2   1 
ATOM   3790  N N     . LEU D 4 364  ? 151.291 107.127 113.779 1.00 71.76  ? 361  LEU A N     1 
ATOM   3791  C CA    . LEU D 4 364  ? 150.842 108.443 114.215 1.00 69.00  ? 361  LEU A CA    1 
ATOM   3792  C C     . LEU D 4 364  ? 149.379 108.472 114.639 1.00 67.77  ? 361  LEU A C     1 
ATOM   3793  O O     . LEU D 4 364  ? 148.899 109.525 115.071 1.00 65.72  ? 361  LEU A O     1 
ATOM   3794  C CB    . LEU D 4 364  ? 151.074 109.473 113.104 1.00 65.30  ? 361  LEU A CB    1 
ATOM   3795  C CG    . LEU D 4 364  ? 152.538 109.760 112.768 1.00 64.67  ? 361  LEU A CG    1 
ATOM   3796  C CD1   . LEU D 4 364  ? 152.647 110.872 111.739 1.00 62.82  ? 361  LEU A CD1   1 
ATOM   3797  C CD2   . LEU D 4 364  ? 153.320 110.110 114.028 1.00 65.38  ? 361  LEU A CD2   1 
ATOM   3798  N N     . THR D 4 365  ? 148.660 107.354 114.532 1.00 67.42  ? 362  THR A N     1 
ATOM   3799  C CA    . THR D 4 365  ? 147.287 107.306 115.016 1.00 64.12  ? 362  THR A CA    1 
ATOM   3800  C C     . THR D 4 365  ? 147.203 107.224 116.534 1.00 64.41  ? 362  THR A C     1 
ATOM   3801  O O     . THR D 4 365  ? 146.097 107.288 117.081 1.00 65.92  ? 362  THR A O     1 
ATOM   3802  C CB    . THR D 4 365  ? 146.540 106.117 114.403 1.00 61.78  ? 362  THR A CB    1 
ATOM   3803  O OG1   . THR D 4 365  ? 147.054 104.894 114.949 1.00 63.34  ? 362  THR A OG1   1 
ATOM   3804  C CG2   . THR D 4 365  ? 146.711 106.101 112.895 1.00 60.52  ? 362  THR A CG2   1 
ATOM   3805  N N     . HIS D 4 366  ? 148.338 107.081 117.221 1.00 65.75  ? 363  HIS A N     1 
ATOM   3806  C CA    . HIS D 4 366  ? 148.372 107.039 118.677 1.00 67.74  ? 363  HIS A CA    1 
ATOM   3807  C C     . HIS D 4 366  ? 149.185 108.181 119.275 1.00 67.04  ? 363  HIS A C     1 
ATOM   3808  O O     . HIS D 4 366  ? 149.434 108.185 120.487 1.00 69.17  ? 363  HIS A O     1 
ATOM   3809  C CB    . HIS D 4 366  ? 148.920 105.691 119.156 1.00 71.85  ? 363  HIS A CB    1 
ATOM   3810  C CG    . HIS D 4 366  ? 148.007 104.536 118.873 1.00 75.11  ? 363  HIS A CG    1 
ATOM   3811  N ND1   . HIS D 4 366  ? 146.966 104.189 119.708 1.00 77.47  ? 363  HIS A ND1   1 
ATOM   3812  C CD2   . HIS D 4 366  ? 147.978 103.653 117.848 1.00 76.03  ? 363  HIS A CD2   1 
ATOM   3813  C CE1   . HIS D 4 366  ? 146.338 103.140 119.210 1.00 77.53  ? 363  HIS A CE1   1 
ATOM   3814  N NE2   . HIS D 4 366  ? 146.930 102.795 118.082 1.00 76.67  ? 363  HIS A NE2   1 
ATOM   3815  N N     . ILE D 4 367  ? 149.608 109.144 118.461 1.00 64.34  ? 364  ILE A N     1 
ATOM   3816  C CA    . ILE D 4 367  ? 150.235 110.372 118.937 1.00 62.36  ? 364  ILE A CA    1 
ATOM   3817  C C     . ILE D 4 367  ? 149.166 111.455 118.896 1.00 57.80  ? 364  ILE A C     1 
ATOM   3818  O O     . ILE D 4 367  ? 148.723 111.863 117.818 1.00 58.18  ? 364  ILE A O     1 
ATOM   3819  C CB    . ILE D 4 367  ? 151.456 110.753 118.091 1.00 61.75  ? 364  ILE A CB    1 
ATOM   3820  C CG1   . ILE D 4 367  ? 152.474 109.614 118.079 1.00 63.65  ? 364  ILE A CG1   1 
ATOM   3821  C CG2   . ILE D 4 367  ? 152.095 112.024 118.623 1.00 58.79  ? 364  ILE A CG2   1 
ATOM   3822  C CD1   . ILE D 4 367  ? 153.011 109.268 119.449 1.00 64.31  ? 364  ILE A CD1   1 
ATOM   3823  N N     . PHE D 4 368  ? 148.745 111.925 120.066 1.00 54.96  ? 365  PHE A N     1 
ATOM   3824  C CA    . PHE D 4 368  ? 147.588 112.798 120.185 1.00 52.26  ? 365  PHE A CA    1 
ATOM   3825  C C     . PHE D 4 368  ? 148.006 114.234 120.468 1.00 52.41  ? 365  PHE A C     1 
ATOM   3826  O O     . PHE D 4 368  ? 148.942 114.484 121.235 1.00 51.82  ? 365  PHE A O     1 
ATOM   3827  C CB    . PHE D 4 368  ? 146.648 112.307 121.287 1.00 52.55  ? 365  PHE A CB    1 
ATOM   3828  C CG    . PHE D 4 368  ? 145.997 110.991 120.977 1.00 56.23  ? 365  PHE A CG    1 
ATOM   3829  C CD1   . PHE D 4 368  ? 146.608 109.799 121.331 1.00 57.64  ? 365  PHE A CD1   1 
ATOM   3830  C CD2   . PHE D 4 368  ? 144.780 110.945 120.319 1.00 56.80  ? 365  PHE A CD2   1 
ATOM   3831  C CE1   . PHE D 4 368  ? 146.014 108.588 121.042 1.00 59.25  ? 365  PHE A CE1   1 
ATOM   3832  C CE2   . PHE D 4 368  ? 144.179 109.737 120.027 1.00 58.05  ? 365  PHE A CE2   1 
ATOM   3833  C CZ    . PHE D 4 368  ? 144.797 108.556 120.390 1.00 60.16  ? 365  PHE A CZ    1 
ATOM   3834  N N     . ILE D 4 369  ? 147.299 115.171 119.842 1.00 52.31  ? 366  ILE A N     1 
ATOM   3835  C CA    . ILE D 4 369  ? 147.480 116.602 120.063 1.00 52.49  ? 366  ILE A CA    1 
ATOM   3836  C C     . ILE D 4 369  ? 146.372 117.092 120.982 1.00 53.71  ? 366  ILE A C     1 
ATOM   3837  O O     . ILE D 4 369  ? 145.201 116.729 120.810 1.00 54.44  ? 366  ILE A O     1 
ATOM   3838  C CB    . ILE D 4 369  ? 147.478 117.372 118.728 1.00 51.28  ? 366  ILE A CB    1 
ATOM   3839  C CG1   . ILE D 4 369  ? 148.646 116.922 117.849 1.00 50.67  ? 366  ILE A CG1   1 
ATOM   3840  C CG2   . ILE D 4 369  ? 147.539 118.868 118.973 1.00 50.77  ? 366  ILE A CG2   1 
ATOM   3841  C CD1   . ILE D 4 369  ? 150.003 117.139 118.480 1.00 49.77  ? 366  ILE A CD1   1 
ATOM   3842  N N     . SER D 4 370  ? 146.736 117.915 121.959 1.00 54.71  ? 367  SER A N     1 
ATOM   3843  C CA    . SER D 4 370  ? 145.757 118.429 122.907 1.00 54.34  ? 367  SER A CA    1 
ATOM   3844  C C     . SER D 4 370  ? 144.830 119.434 122.235 1.00 55.91  ? 367  SER A C     1 
ATOM   3845  O O     . SER D 4 370  ? 145.265 120.266 121.435 1.00 55.68  ? 367  SER A O     1 
ATOM   3846  C CB    . SER D 4 370  ? 146.462 119.079 124.096 1.00 54.51  ? 367  SER A CB    1 
ATOM   3847  O OG    . SER D 4 370  ? 145.520 119.629 125.001 1.00 55.35  ? 367  SER A OG    1 
ATOM   3848  N N     . HIS D 4 371  ? 143.538 119.354 122.572 1.00 57.17  ? 368  HIS A N     1 
ATOM   3849  C CA    . HIS D 4 371  ? 142.571 120.291 122.009 1.00 56.25  ? 368  HIS A CA    1 
ATOM   3850  C C     . HIS D 4 371  ? 142.805 121.709 122.509 1.00 55.12  ? 368  HIS A C     1 
ATOM   3851  O O     . HIS D 4 371  ? 142.471 122.674 121.814 1.00 54.89  ? 368  HIS A O     1 
ATOM   3852  C CB    . HIS D 4 371  ? 141.145 119.841 122.334 1.00 59.84  ? 368  HIS A CB    1 
ATOM   3853  C CG    . HIS D 4 371  ? 140.846 119.783 123.801 1.00 65.77  ? 368  HIS A CG    1 
ATOM   3854  N ND1   . HIS D 4 371  ? 140.857 118.606 124.518 1.00 69.98  ? 368  HIS A ND1   1 
ATOM   3855  C CD2   . HIS D 4 371  ? 140.521 120.757 124.684 1.00 66.18  ? 368  HIS A CD2   1 
ATOM   3856  C CE1   . HIS D 4 371  ? 140.555 118.857 125.777 1.00 68.93  ? 368  HIS A CE1   1 
ATOM   3857  N NE2   . HIS D 4 371  ? 140.346 120.154 125.906 1.00 67.13  ? 368  HIS A NE2   1 
ATOM   3858  N N     . LYS D 4 372  ? 143.380 121.853 123.706 1.00 56.01  ? 369  LYS A N     1 
ATOM   3859  C CA    . LYS D 4 372  ? 143.705 123.171 124.239 1.00 57.47  ? 369  LYS A CA    1 
ATOM   3860  C C     . LYS D 4 372  ? 144.824 123.857 123.467 1.00 58.23  ? 369  LYS A C     1 
ATOM   3861  O O     . LYS D 4 372  ? 145.028 125.062 123.649 1.00 59.14  ? 369  LYS A O     1 
ATOM   3862  C CB    . LYS D 4 372  ? 144.097 123.054 125.714 1.00 58.16  ? 369  LYS A CB    1 
ATOM   3863  C CG    . LYS D 4 372  ? 143.020 122.446 126.598 1.00 58.45  ? 369  LYS A CG    1 
ATOM   3864  C CD    . LYS D 4 372  ? 143.522 122.254 128.022 1.00 59.54  ? 369  LYS A CD    1 
ATOM   3865  C CE    . LYS D 4 372  ? 142.446 121.658 128.912 1.00 58.62  ? 369  LYS A CE    1 
ATOM   3866  N NZ    . LYS D 4 372  ? 142.951 121.398 130.288 1.00 60.64  ? 369  LYS A NZ    1 
ATOM   3867  N N     . LYS D 4 373  ? 145.548 123.127 122.616 1.00 57.16  ? 370  LYS A N     1 
ATOM   3868  C CA    . LYS D 4 373  ? 146.650 123.680 121.846 1.00 53.66  ? 370  LYS A CA    1 
ATOM   3869  C C     . LYS D 4 373  ? 146.420 123.624 120.343 1.00 50.19  ? 370  LYS A C     1 
ATOM   3870  O O     . LYS D 4 373  ? 147.253 124.137 119.588 1.00 51.70  ? 370  LYS A O     1 
ATOM   3871  C CB    . LYS D 4 373  ? 147.956 122.944 122.181 1.00 53.51  ? 370  LYS A CB    1 
ATOM   3872  C CG    . LYS D 4 373  ? 148.238 122.797 123.668 1.00 55.98  ? 370  LYS A CG    1 
ATOM   3873  C CD    . LYS D 4 373  ? 148.496 124.142 124.329 1.00 59.11  ? 370  LYS A CD    1 
ATOM   3874  C CE    . LYS D 4 373  ? 148.820 123.972 125.807 1.00 62.87  ? 370  LYS A CE    1 
ATOM   3875  N NZ    . LYS D 4 373  ? 149.083 125.277 126.477 1.00 65.60  ? 370  LYS A NZ    1 
ATOM   3876  N N     . LEU D 4 374  ? 145.318 123.022 119.885 1.00 46.07  ? 371  LEU A N     1 
ATOM   3877  C CA    . LEU D 4 374  ? 145.122 122.829 118.450 1.00 46.14  ? 371  LEU A CA    1 
ATOM   3878  C C     . LEU D 4 374  ? 145.024 124.159 117.713 1.00 42.45  ? 371  LEU A C     1 
ATOM   3879  O O     . LEU D 4 374  ? 145.578 124.312 116.618 1.00 41.17  ? 371  LEU A O     1 
ATOM   3880  C CB    . LEU D 4 374  ? 143.873 121.986 118.195 1.00 46.66  ? 371  LEU A CB    1 
ATOM   3881  C CG    . LEU D 4 374  ? 143.547 121.718 116.725 1.00 43.67  ? 371  LEU A CG    1 
ATOM   3882  C CD1   . LEU D 4 374  ? 144.682 120.960 116.052 1.00 43.80  ? 371  LEU A CD1   1 
ATOM   3883  C CD2   . LEU D 4 374  ? 142.238 120.957 116.589 1.00 42.51  ? 371  LEU A CD2   1 
ATOM   3884  N N     . GLU D 4 375  ? 144.323 125.135 118.293 1.00 41.71  ? 372  GLU A N     1 
ATOM   3885  C CA    . GLU D 4 375  ? 144.195 126.431 117.636 1.00 45.20  ? 372  GLU A CA    1 
ATOM   3886  C C     . GLU D 4 375  ? 145.521 127.181 117.631 1.00 47.19  ? 372  GLU A C     1 
ATOM   3887  O O     . GLU D 4 375  ? 145.837 127.889 116.667 1.00 48.35  ? 372  GLU A O     1 
ATOM   3888  C CB    . GLU D 4 375  ? 143.103 127.261 118.310 1.00 47.18  ? 372  GLU A CB    1 
ATOM   3889  C CG    . GLU D 4 375  ? 141.704 126.981 117.780 1.00 50.70  ? 372  GLU A CG    1 
ATOM   3890  C CD    . GLU D 4 375  ? 141.276 125.540 117.977 1.00 55.36  ? 372  GLU A CD    1 
ATOM   3891  O OE1   . GLU D 4 375  ? 141.405 125.032 119.112 1.00 59.66  ? 372  GLU A OE1   1 
ATOM   3892  O OE2   . GLU D 4 375  ? 140.821 124.913 116.998 1.00 54.43  ? 372  GLU A OE2   1 
ATOM   3893  N N     . THR D 4 376  ? 146.311 127.039 118.698 1.00 48.75  ? 373  THR A N     1 
ATOM   3894  C CA    . THR D 4 376  ? 147.627 127.669 118.725 1.00 51.15  ? 373  THR A CA    1 
ATOM   3895  C C     . THR D 4 376  ? 148.547 127.060 117.673 1.00 52.59  ? 373  THR A C     1 
ATOM   3896  O O     . THR D 4 376  ? 149.292 127.780 117.000 1.00 53.75  ? 373  THR A O     1 
ATOM   3897  C CB    . THR D 4 376  ? 148.241 127.542 120.119 1.00 53.69  ? 373  THR A CB    1 
ATOM   3898  O OG1   . THR D 4 376  ? 147.354 128.114 121.089 1.00 55.64  ? 373  THR A OG1   1 
ATOM   3899  C CG2   . THR D 4 376  ? 149.580 128.261 120.183 1.00 53.21  ? 373  THR A CG2   1 
ATOM   3900  N N     . ILE D 4 377  ? 148.499 125.737 117.512 1.00 53.59  ? 374  ILE A N     1 
ATOM   3901  C CA    . ILE D 4 377  ? 149.318 125.074 116.501 1.00 53.18  ? 374  ILE A CA    1 
ATOM   3902  C C     . ILE D 4 377  ? 148.881 125.486 115.103 1.00 54.37  ? 374  ILE A C     1 
ATOM   3903  O O     . ILE D 4 377  ? 149.713 125.682 114.208 1.00 55.41  ? 374  ILE A O     1 
ATOM   3904  C CB    . ILE D 4 377  ? 149.257 123.548 116.686 1.00 49.88  ? 374  ILE A CB    1 
ATOM   3905  C CG1   . ILE D 4 377  ? 149.830 123.157 118.047 1.00 49.44  ? 374  ILE A CG1   1 
ATOM   3906  C CG2   . ILE D 4 377  ? 150.004 122.836 115.569 1.00 49.72  ? 374  ILE A CG2   1 
ATOM   3907  C CD1   . ILE D 4 377  ? 149.656 121.696 118.373 1.00 50.33  ? 374  ILE A CD1   1 
ATOM   3908  N N     . SER D 4 378  ? 147.569 125.626 114.889 1.00 54.70  ? 375  SER A N     1 
ATOM   3909  C CA    . SER D 4 378  ? 147.070 126.037 113.581 1.00 53.71  ? 375  SER A CA    1 
ATOM   3910  C C     . SER D 4 378  ? 147.595 127.416 113.202 1.00 53.81  ? 375  SER A C     1 
ATOM   3911  O O     . SER D 4 378  ? 147.965 127.650 112.045 1.00 55.04  ? 375  SER A O     1 
ATOM   3912  C CB    . SER D 4 378  ? 145.544 126.026 113.577 1.00 52.66  ? 375  SER A CB    1 
ATOM   3913  O OG    . SER D 4 378  ? 145.037 126.209 112.266 1.00 52.00  ? 375  SER A OG    1 
ATOM   3914  N N     . SER D 4 379  ? 147.641 128.338 114.163 1.00 55.60  ? 376  SER A N     1 
ATOM   3915  C CA    . SER D 4 379  ? 148.123 129.683 113.880 1.00 56.79  ? 376  SER A CA    1 
ATOM   3916  C C     . SER D 4 379  ? 149.634 129.731 113.690 1.00 56.92  ? 376  SER A C     1 
ATOM   3917  O O     . SER D 4 379  ? 150.131 130.639 113.017 1.00 58.36  ? 376  SER A O     1 
ATOM   3918  C CB    . SER D 4 379  ? 147.706 130.636 115.002 1.00 58.68  ? 376  SER A CB    1 
ATOM   3919  O OG    . SER D 4 379  ? 148.033 131.978 114.683 1.00 62.48  ? 376  SER A OG    1 
ATOM   3920  N N     . ALA D 4 380  ? 150.369 128.775 114.256 1.00 57.39  ? 377  ALA A N     1 
ATOM   3921  C CA    . ALA D 4 380  ? 151.821 128.763 114.146 1.00 61.15  ? 377  ALA A CA    1 
ATOM   3922  C C     . ALA D 4 380  ? 152.324 128.022 112.917 1.00 62.37  ? 377  ALA A C     1 
ATOM   3923  O O     . ALA D 4 380  ? 153.451 128.278 112.475 1.00 65.68  ? 377  ALA A O     1 
ATOM   3924  C CB    . ALA D 4 380  ? 152.442 128.136 115.400 1.00 61.93  ? 377  ALA A CB    1 
ATOM   3925  N N     . LEU D 4 381  ? 151.524 127.116 112.354 1.00 60.26  ? 378  LEU A N     1 
ATOM   3926  C CA    . LEU D 4 381  ? 151.942 126.322 111.211 1.00 59.72  ? 378  LEU A CA    1 
ATOM   3927  C C     . LEU D 4 381  ? 151.139 126.588 109.948 1.00 63.33  ? 378  LEU A C     1 
ATOM   3928  O O     . LEU D 4 381  ? 151.572 126.175 108.867 1.00 64.33  ? 378  LEU A O     1 
ATOM   3929  C CB    . LEU D 4 381  ? 151.856 124.824 111.539 1.00 59.49  ? 378  LEU A CB    1 
ATOM   3930  C CG    . LEU D 4 381  ? 152.599 124.358 112.790 1.00 62.36  ? 378  LEU A CG    1 
ATOM   3931  C CD1   . LEU D 4 381  ? 152.567 122.843 112.898 1.00 62.95  ? 378  LEU A CD1   1 
ATOM   3932  C CD2   . LEU D 4 381  ? 154.027 124.867 112.778 1.00 65.54  ? 378  LEU A CD2   1 
ATOM   3933  N N     . CYS D 4 382  ? 149.990 127.255 110.045 1.00 67.35  ? 379  CYS A N     1 
ATOM   3934  C CA    . CYS D 4 382  ? 149.140 127.448 108.877 1.00 71.16  ? 379  CYS A CA    1 
ATOM   3935  C C     . CYS D 4 382  ? 148.765 128.913 108.693 1.00 73.73  ? 379  CYS A C     1 
ATOM   3936  O O     . CYS D 4 382  ? 149.310 129.794 109.367 1.00 72.71  ? 379  CYS A O     1 
ATOM   3937  C CB    . CYS D 4 382  ? 147.879 126.593 108.995 1.00 69.33  ? 379  CYS A CB    1 
ATOM   3938  S SG    . CYS D 4 382  ? 148.185 124.854 109.374 1.00 67.69  ? 379  CYS A SG    1 
ATOM   3939  N N     . ASP D 4 383  ? 147.830 129.177 107.777 1.00 80.10  ? 380  ASP A N     1 
ATOM   3940  C CA    . ASP D 4 383  ? 147.427 130.549 107.493 1.00 85.60  ? 380  ASP A CA    1 
ATOM   3941  C C     . ASP D 4 383  ? 146.774 131.193 108.709 1.00 85.11  ? 380  ASP A C     1 
ATOM   3942  O O     . ASP D 4 383  ? 147.164 132.287 109.134 1.00 85.73  ? 380  ASP A O     1 
ATOM   3943  C CB    . ASP D 4 383  ? 146.482 130.580 106.291 1.00 89.96  ? 380  ASP A CB    1 
ATOM   3944  C CG    . ASP D 4 383  ? 147.089 129.948 105.052 1.00 94.25  ? 380  ASP A CG    1 
ATOM   3945  O OD1   . ASP D 4 383  ? 146.958 128.717 104.885 1.00 96.19  ? 380  ASP A OD1   1 
ATOM   3946  O OD2   . ASP D 4 383  ? 147.691 130.683 104.241 1.00 95.77  ? 380  ASP A OD2   1 
ATOM   3947  N N     . HIS D 4 384  ? 145.773 130.528 109.285 1.00 80.78  ? 381  HIS A N     1 
ATOM   3948  C CA    . HIS D 4 384  ? 145.031 131.072 110.410 1.00 78.81  ? 381  HIS A CA    1 
ATOM   3949  C C     . HIS D 4 384  ? 144.833 129.989 111.461 1.00 74.26  ? 381  HIS A C     1 
ATOM   3950  O O     . HIS D 4 384  ? 145.166 128.818 111.259 1.00 73.43  ? 381  HIS A O     1 
ATOM   3951  C CB    . HIS D 4 384  ? 143.669 131.630 109.975 1.00 79.52  ? 381  HIS A CB    1 
ATOM   3952  C CG    . HIS D 4 384  ? 143.669 132.219 108.600 1.00 82.73  ? 381  HIS A CG    1 
ATOM   3953  N ND1   . HIS D 4 384  ? 143.090 131.586 107.522 1.00 83.94  ? 381  HIS A ND1   1 
ATOM   3954  C CD2   . HIS D 4 384  ? 144.182 133.379 108.125 1.00 84.55  ? 381  HIS A CD2   1 
ATOM   3955  C CE1   . HIS D 4 384  ? 143.242 132.332 106.442 1.00 84.94  ? 381  HIS A CE1   1 
ATOM   3956  N NE2   . HIS D 4 384  ? 143.902 133.425 106.780 1.00 85.18  ? 381  HIS A NE2   1 
ATOM   3957  N N     . TRP D 4 385  ? 144.274 130.405 112.599 1.00 69.68  ? 382  TRP A N     1 
ATOM   3958  C CA    . TRP D 4 385  ? 143.861 129.461 113.630 1.00 66.96  ? 382  TRP A CA    1 
ATOM   3959  C C     . TRP D 4 385  ? 142.715 128.574 113.163 1.00 69.37  ? 382  TRP A C     1 
ATOM   3960  O O     . TRP D 4 385  ? 142.481 127.514 113.755 1.00 71.19  ? 382  TRP A O     1 
ATOM   3961  C CB    . TRP D 4 385  ? 143.435 130.224 114.880 1.00 61.32  ? 382  TRP A CB    1 
ATOM   3962  C CG    . TRP D 4 385  ? 142.215 131.049 114.633 1.00 55.72  ? 382  TRP A CG    1 
ATOM   3963  C CD1   . TRP D 4 385  ? 142.163 132.287 114.062 1.00 53.57  ? 382  TRP A CD1   1 
ATOM   3964  C CD2   . TRP D 4 385  ? 140.861 130.683 114.922 1.00 54.55  ? 382  TRP A CD2   1 
ATOM   3965  N NE1   . TRP D 4 385  ? 140.861 132.719 113.988 1.00 53.29  ? 382  TRP A NE1   1 
ATOM   3966  C CE2   . TRP D 4 385  ? 140.043 131.751 114.511 1.00 53.40  ? 382  TRP A CE2   1 
ATOM   3967  C CE3   . TRP D 4 385  ? 140.264 129.556 115.496 1.00 54.39  ? 382  TRP A CE3   1 
ATOM   3968  C CZ2   . TRP D 4 385  ? 138.658 131.727 114.654 1.00 53.68  ? 382  TRP A CZ2   1 
ATOM   3969  C CZ3   . TRP D 4 385  ? 138.889 129.534 115.638 1.00 52.80  ? 382  TRP A CZ3   1 
ATOM   3970  C CH2   . TRP D 4 385  ? 138.101 130.613 115.219 1.00 53.54  ? 382  TRP A CH2   1 
ATOM   3971  N N     . ASP D 4 386  ? 141.998 128.988 112.117 1.00 71.11  ? 383  ASP A N     1 
ATOM   3972  C CA    . ASP D 4 386  ? 140.813 128.273 111.659 1.00 67.80  ? 383  ASP A CA    1 
ATOM   3973  C C     . ASP D 4 386  ? 141.148 127.008 110.884 1.00 65.87  ? 383  ASP A C     1 
ATOM   3974  O O     . ASP D 4 386  ? 140.400 126.027 110.963 1.00 65.70  ? 383  ASP A O     1 
ATOM   3975  C CB    . ASP D 4 386  ? 139.966 129.189 110.774 1.00 70.79  ? 383  ASP A CB    1 
ATOM   3976  C CG    . ASP D 4 386  ? 138.752 129.727 111.487 1.00 77.68  ? 383  ASP A CG    1 
ATOM   3977  O OD1   . ASP D 4 386  ? 138.242 129.034 112.393 1.00 81.17  ? 383  ASP A OD1   1 
ATOM   3978  O OD2   . ASP D 4 386  ? 138.305 130.841 111.140 1.00 81.25  ? 383  ASP A OD2   1 
ATOM   3979  N N     . THR D 4 387  ? 142.261 127.009 110.146 1.00 62.87  ? 384  THR A N     1 
ATOM   3980  C CA    . THR D 4 387  ? 142.457 126.030 109.081 1.00 61.57  ? 384  THR A CA    1 
ATOM   3981  C C     . THR D 4 387  ? 142.439 124.598 109.603 1.00 59.61  ? 384  THR A C     1 
ATOM   3982  O O     . THR D 4 387  ? 141.852 123.712 108.970 1.00 59.56  ? 384  THR A O     1 
ATOM   3983  C CB    . THR D 4 387  ? 143.764 126.314 108.345 1.00 63.09  ? 384  THR A CB    1 
ATOM   3984  O OG1   . THR D 4 387  ? 144.816 126.484 109.301 1.00 66.51  ? 384  THR A OG1   1 
ATOM   3985  C CG2   . THR D 4 387  ? 143.637 127.577 107.504 1.00 61.17  ? 384  THR A CG2   1 
ATOM   3986  N N     . LEU D 4 388  ? 143.070 124.348 110.752 1.00 56.51  ? 385  LEU A N     1 
ATOM   3987  C CA    . LEU D 4 388  ? 143.135 122.980 111.261 1.00 53.86  ? 385  LEU A CA    1 
ATOM   3988  C C     . LEU D 4 388  ? 141.768 122.490 111.718 1.00 52.80  ? 385  LEU A C     1 
ATOM   3989  O O     . LEU D 4 388  ? 141.318 121.415 111.305 1.00 53.82  ? 385  LEU A O     1 
ATOM   3990  C CB    . LEU D 4 388  ? 144.149 122.882 112.400 1.00 53.86  ? 385  LEU A CB    1 
ATOM   3991  C CG    . LEU D 4 388  ? 145.608 122.864 111.947 1.00 55.35  ? 385  LEU A CG    1 
ATOM   3992  C CD1   . LEU D 4 388  ? 146.486 122.198 112.994 1.00 53.69  ? 385  LEU A CD1   1 
ATOM   3993  C CD2   . LEU D 4 388  ? 145.730 122.170 110.602 1.00 57.18  ? 385  LEU A CD2   1 
ATOM   3994  N N     . ARG D 4 389  ? 141.096 123.260 112.577 1.00 51.99  ? 386  ARG A N     1 
ATOM   3995  C CA    . ARG D 4 389  ? 139.773 122.862 113.043 1.00 52.98  ? 386  ARG A CA    1 
ATOM   3996  C C     . ARG D 4 389  ? 138.803 122.705 111.880 1.00 55.75  ? 386  ARG A C     1 
ATOM   3997  O O     . ARG D 4 389  ? 137.943 121.819 111.890 1.00 58.06  ? 386  ARG A O     1 
ATOM   3998  C CB    . ARG D 4 389  ? 139.244 123.884 114.048 1.00 55.21  ? 386  ARG A CB    1 
ATOM   3999  C CG    . ARG D 4 389  ? 137.900 123.522 114.655 1.00 57.31  ? 386  ARG A CG    1 
ATOM   4000  C CD    . ARG D 4 389  ? 137.195 124.756 115.187 1.00 59.90  ? 386  ARG A CD    1 
ATOM   4001  N NE    . ARG D 4 389  ? 136.899 125.706 114.119 1.00 62.20  ? 386  ARG A NE    1 
ATOM   4002  C CZ    . ARG D 4 389  ? 136.241 126.846 114.295 1.00 63.82  ? 386  ARG A CZ    1 
ATOM   4003  N NH1   . ARG D 4 389  ? 135.803 127.184 115.501 1.00 64.52  ? 386  ARG A NH1   1 
ATOM   4004  N NH2   . ARG D 4 389  ? 136.015 127.651 113.265 1.00 63.16  ? 386  ARG A NH2   1 
ATOM   4005  N N     . ASN D 4 390  ? 138.937 123.554 110.857 1.00 56.16  ? 387  ASN A N     1 
ATOM   4006  C CA    . ASN D 4 390  ? 138.058 123.463 109.696 1.00 56.50  ? 387  ASN A CA    1 
ATOM   4007  C C     . ASN D 4 390  ? 138.392 122.246 108.841 1.00 57.90  ? 387  ASN A C     1 
ATOM   4008  O O     . ASN D 4 390  ? 137.487 121.561 108.349 1.00 58.95  ? 387  ASN A O     1 
ATOM   4009  C CB    . ASN D 4 390  ? 138.149 124.746 108.870 1.00 58.12  ? 387  ASN A CB    1 
ATOM   4010  C CG    . ASN D 4 390  ? 137.504 125.933 109.562 1.00 59.62  ? 387  ASN A CG    1 
ATOM   4011  O OD1   . ASN D 4 390  ? 136.482 126.447 109.110 1.00 60.93  ? 387  ASN A OD1   1 
ATOM   4012  N ND2   . ASN D 4 390  ? 138.096 126.367 110.667 1.00 60.40  ? 387  ASN A ND2   1 
ATOM   4013  N N     . ALA D 4 391  ? 139.684 121.960 108.654 1.00 57.69  ? 388  ALA A N     1 
ATOM   4014  C CA    . ALA D 4 391  ? 140.076 120.804 107.852 1.00 54.96  ? 388  ALA A CA    1 
ATOM   4015  C C     . ALA D 4 391  ? 139.621 119.503 108.500 1.00 56.87  ? 388  ALA A C     1 
ATOM   4016  O O     . ALA D 4 391  ? 139.157 118.588 107.810 1.00 58.11  ? 388  ALA A O     1 
ATOM   4017  C CB    . ALA D 4 391  ? 141.590 120.798 107.640 1.00 51.53  ? 388  ALA A CB    1 
ATOM   4018  N N     . LEU D 4 392  ? 139.750 119.401 109.824 1.00 55.66  ? 389  LEU A N     1 
ATOM   4019  C CA    . LEU D 4 392  ? 139.239 118.229 110.526 1.00 53.61  ? 389  LEU A CA    1 
ATOM   4020  C C     . LEU D 4 392  ? 137.724 118.146 110.421 1.00 53.06  ? 389  LEU A C     1 
ATOM   4021  O O     . LEU D 4 392  ? 137.156 117.050 110.337 1.00 52.01  ? 389  LEU A O     1 
ATOM   4022  C CB    . LEU D 4 392  ? 139.672 118.260 111.993 1.00 51.97  ? 389  LEU A CB    1 
ATOM   4023  C CG    . LEU D 4 392  ? 141.172 118.187 112.276 1.00 52.74  ? 389  LEU A CG    1 
ATOM   4024  C CD1   . LEU D 4 392  ? 141.432 118.321 113.767 1.00 55.03  ? 389  LEU A CD1   1 
ATOM   4025  C CD2   . LEU D 4 392  ? 141.756 116.890 111.741 1.00 52.55  ? 389  LEU A CD2   1 
ATOM   4026  N N     . TYR D 4 393  ? 137.051 119.299 110.423 1.00 53.69  ? 390  TYR A N     1 
ATOM   4027  C CA    . TYR D 4 393  ? 135.597 119.314 110.304 1.00 51.99  ? 390  TYR A CA    1 
ATOM   4028  C C     . TYR D 4 393  ? 135.150 118.754 108.960 1.00 52.12  ? 390  TYR A C     1 
ATOM   4029  O O     . TYR D 4 393  ? 134.229 117.934 108.890 1.00 53.37  ? 390  TYR A O     1 
ATOM   4030  C CB    . TYR D 4 393  ? 135.070 120.737 110.495 1.00 48.18  ? 390  TYR A CB    1 
ATOM   4031  C CG    . TYR D 4 393  ? 133.600 120.890 110.170 1.00 48.90  ? 390  TYR A CG    1 
ATOM   4032  C CD1   . TYR D 4 393  ? 132.626 120.531 111.090 1.00 49.62  ? 390  TYR A CD1   1 
ATOM   4033  C CD2   . TYR D 4 393  ? 133.188 121.395 108.942 1.00 48.46  ? 390  TYR A CD2   1 
ATOM   4034  C CE1   . TYR D 4 393  ? 131.282 120.666 110.797 1.00 49.58  ? 390  TYR A CE1   1 
ATOM   4035  C CE2   . TYR D 4 393  ? 131.847 121.533 108.640 1.00 47.26  ? 390  TYR A CE2   1 
ATOM   4036  C CZ    . TYR D 4 393  ? 130.897 121.168 109.572 1.00 47.49  ? 390  TYR A CZ    1 
ATOM   4037  O OH    . TYR D 4 393  ? 129.560 121.305 109.283 1.00 46.61  ? 390  TYR A OH    1 
ATOM   4038  N N     . GLU D 4 394  ? 135.802 119.185 107.878 1.00 52.24  ? 391  GLU A N     1 
ATOM   4039  C CA    . GLU D 4 394  ? 135.391 118.740 106.550 1.00 53.91  ? 391  GLU A CA    1 
ATOM   4040  C C     . GLU D 4 394  ? 135.646 117.251 106.358 1.00 54.96  ? 391  GLU A C     1 
ATOM   4041  O O     . GLU D 4 394  ? 134.831 116.554 105.741 1.00 57.69  ? 391  GLU A O     1 
ATOM   4042  C CB    . GLU D 4 394  ? 136.112 119.558 105.478 1.00 55.46  ? 391  GLU A CB    1 
ATOM   4043  C CG    . GLU D 4 394  ? 135.767 121.041 105.498 1.00 57.86  ? 391  GLU A CG    1 
ATOM   4044  C CD    . GLU D 4 394  ? 134.304 121.308 105.189 1.00 60.24  ? 391  GLU A CD    1 
ATOM   4045  O OE1   . GLU D 4 394  ? 133.687 120.502 104.460 1.00 59.38  ? 391  GLU A OE1   1 
ATOM   4046  O OE2   . GLU D 4 394  ? 133.769 122.326 105.679 1.00 62.65  ? 391  GLU A OE2   1 
ATOM   4047  N N     . ARG D 4 395  ? 136.761 116.739 106.881 1.00 54.30  ? 392  ARG A N     1 
ATOM   4048  C CA    . ARG D 4 395  ? 137.060 115.322 106.699 1.00 53.47  ? 392  ARG A CA    1 
ATOM   4049  C C     . ARG D 4 395  ? 136.142 114.443 107.537 1.00 53.15  ? 392  ARG A C     1 
ATOM   4050  O O     . ARG D 4 395  ? 135.835 113.314 107.136 1.00 54.84  ? 392  ARG A O     1 
ATOM   4051  C CB    . ARG D 4 395  ? 138.520 115.031 107.041 1.00 55.02  ? 392  ARG A CB    1 
ATOM   4052  C CG    . ARG D 4 395  ? 139.025 113.720 106.461 1.00 57.39  ? 392  ARG A CG    1 
ATOM   4053  C CD    . ARG D 4 395  ? 140.457 113.440 106.872 1.00 61.93  ? 392  ARG A CD    1 
ATOM   4054  N NE    . ARG D 4 395  ? 140.533 112.489 107.976 1.00 66.40  ? 392  ARG A NE    1 
ATOM   4055  C CZ    . ARG D 4 395  ? 140.746 111.187 107.820 1.00 69.75  ? 392  ARG A CZ    1 
ATOM   4056  N NH1   . ARG D 4 395  ? 140.908 110.680 106.605 1.00 69.57  ? 392  ARG A NH1   1 
ATOM   4057  N NH2   . ARG D 4 395  ? 140.801 110.389 108.880 1.00 70.91  ? 392  ARG A NH2   1 
ATOM   4058  N N     . ARG D 4 396  ? 135.695 114.933 108.696 1.00 52.22  ? 393  ARG A N     1 
ATOM   4059  C CA    . ARG D 4 396  ? 134.781 114.151 109.517 1.00 54.26  ? 393  ARG A CA    1 
ATOM   4060  C C     . ARG D 4 396  ? 133.367 114.164 108.945 1.00 55.70  ? 393  ARG A C     1 
ATOM   4061  O O     . ARG D 4 396  ? 132.669 113.145 108.987 1.00 57.36  ? 393  ARG A O     1 
ATOM   4062  C CB    . ARG D 4 396  ? 134.790 114.666 110.958 1.00 54.41  ? 393  ARG A CB    1 
ATOM   4063  C CG    . ARG D 4 396  ? 136.074 114.333 111.707 1.00 56.79  ? 393  ARG A CG    1 
ATOM   4064  C CD    . ARG D 4 396  ? 135.953 114.606 113.196 1.00 60.52  ? 393  ARG A CD    1 
ATOM   4065  N NE    . ARG D 4 396  ? 137.117 114.110 113.928 1.00 64.57  ? 393  ARG A NE    1 
ATOM   4066  C CZ    . ARG D 4 396  ? 137.235 114.133 115.253 1.00 65.42  ? 393  ARG A CZ    1 
ATOM   4067  N NH1   . ARG D 4 396  ? 136.259 114.626 116.001 1.00 65.57  ? 393  ARG A NH1   1 
ATOM   4068  N NH2   . ARG D 4 396  ? 138.331 113.657 115.829 1.00 64.56  ? 393  ARG A NH2   1 
ATOM   4069  N N     . ILE D 4 397  ? 132.930 115.306 108.407 1.00 54.07  ? 394  ILE A N     1 
ATOM   4070  C CA    . ILE D 4 397  ? 131.673 115.335 107.664 1.00 53.38  ? 394  ILE A CA    1 
ATOM   4071  C C     . ILE D 4 397  ? 131.767 114.433 106.442 1.00 53.15  ? 394  ILE A C     1 
ATOM   4072  O O     . ILE D 4 397  ? 130.768 113.840 106.013 1.00 52.69  ? 394  ILE A O     1 
ATOM   4073  C CB    . ILE D 4 397  ? 131.314 116.786 107.280 1.00 53.94  ? 394  ILE A CB    1 
ATOM   4074  C CG1   . ILE D 4 397  ? 131.133 117.638 108.535 1.00 54.47  ? 394  ILE A CG1   1 
ATOM   4075  C CG2   . ILE D 4 397  ? 130.046 116.831 106.444 1.00 55.30  ? 394  ILE A CG2   1 
ATOM   4076  C CD1   . ILE D 4 397  ? 130.031 117.156 109.439 1.00 56.02  ? 394  ILE A CD1   1 
ATOM   4077  N N     . SER D 4 398  ? 132.969 114.293 105.878 1.00 52.75  ? 395  SER A N     1 
ATOM   4078  C CA    . SER D 4 398  ? 133.180 113.434 104.719 1.00 52.50  ? 395  SER A CA    1 
ATOM   4079  C C     . SER D 4 398  ? 132.955 111.960 105.025 1.00 54.01  ? 395  SER A C     1 
ATOM   4080  O O     . SER D 4 398  ? 132.803 111.167 104.090 1.00 55.81  ? 395  SER A O     1 
ATOM   4081  C CB    . SER D 4 398  ? 134.597 113.637 104.177 1.00 50.75  ? 395  SER A CB    1 
ATOM   4082  O OG    . SER D 4 398  ? 134.976 112.575 103.319 1.00 53.05  ? 395  SER A OG    1 
ATOM   4083  N N     . GLU D 4 399  ? 132.931 111.570 106.299 1.00 55.21  ? 396  GLU A N     1 
ATOM   4084  C CA    . GLU D 4 399  ? 132.806 110.168 106.678 1.00 57.39  ? 396  GLU A CA    1 
ATOM   4085  C C     . GLU D 4 399  ? 131.603 109.926 107.588 1.00 59.41  ? 396  GLU A C     1 
ATOM   4086  O O     . GLU D 4 399  ? 131.605 108.994 108.397 1.00 61.15  ? 396  GLU A O     1 
ATOM   4087  C CB    . GLU D 4 399  ? 134.094 109.674 107.336 1.00 60.42  ? 396  GLU A CB    1 
ATOM   4088  C CG    . GLU D 4 399  ? 134.673 110.611 108.381 1.00 64.28  ? 396  GLU A CG    1 
ATOM   4089  C CD    . GLU D 4 399  ? 136.157 110.379 108.613 1.00 67.07  ? 396  GLU A CD    1 
ATOM   4090  O OE1   . GLU D 4 399  ? 136.794 109.707 107.773 1.00 65.64  ? 396  GLU A OE1   1 
ATOM   4091  O OE2   . GLU D 4 399  ? 136.689 110.869 109.632 1.00 69.02  ? 396  GLU A OE2   1 
ATOM   4092  N N     . LEU D 4 400  ? 130.565 110.748 107.463 1.00 60.34  ? 397  LEU A N     1 
ATOM   4093  C CA    . LEU D 4 400  ? 129.310 110.484 108.147 1.00 61.52  ? 397  LEU A CA    1 
ATOM   4094  C C     . LEU D 4 400  ? 128.457 109.516 107.331 1.00 66.17  ? 397  LEU A C     1 
ATOM   4095  O O     . LEU D 4 400  ? 128.686 109.297 106.139 1.00 67.89  ? 397  LEU A O     1 
ATOM   4096  C CB    . LEU D 4 400  ? 128.542 111.780 108.401 1.00 58.33  ? 397  LEU A CB    1 
ATOM   4097  C CG    . LEU D 4 400  ? 129.044 112.713 109.505 1.00 56.07  ? 397  LEU A CG    1 
ATOM   4098  C CD1   . LEU D 4 400  ? 128.184 113.964 109.570 1.00 52.93  ? 397  LEU A CD1   1 
ATOM   4099  C CD2   . LEU D 4 400  ? 129.051 112.005 110.848 1.00 56.87  ? 397  LEU A CD2   1 
ATOM   4100  N N     . THR D 4 401  ? 127.455 108.942 107.990 1.00 67.17  ? 398  THR A N     1 
ATOM   4101  C CA    . THR D 4 401  ? 126.613 107.909 107.401 1.00 68.26  ? 398  THR A CA    1 
ATOM   4102  C C     . THR D 4 401  ? 125.226 108.463 107.103 1.00 70.42  ? 398  THR A C     1 
ATOM   4103  O O     . THR D 4 401  ? 124.622 109.126 107.954 1.00 69.99  ? 398  THR A O     1 
ATOM   4104  C CB    . THR D 4 401  ? 126.497 106.700 108.330 1.00 69.51  ? 398  THR A CB    1 
ATOM   4105  O OG1   . THR D 4 401  ? 127.805 106.222 108.660 1.00 71.09  ? 398  THR A OG1   1 
ATOM   4106  C CG2   . THR D 4 401  ? 125.711 105.586 107.661 1.00 69.04  ? 398  THR A CG2   1 
ATOM   4107  N N     . GLY D 4 402  ? 124.727 108.185 105.899 1.00 72.94  ? 399  GLY A N     1 
ATOM   4108  C CA    . GLY D 4 402  ? 123.362 108.513 105.545 1.00 73.38  ? 399  GLY A CA    1 
ATOM   4109  C C     . GLY D 4 402  ? 123.131 109.999 105.329 1.00 71.54  ? 399  GLY A C     1 
ATOM   4110  O O     . GLY D 4 402  ? 124.045 110.779 105.040 1.00 68.17  ? 399  GLY A O     1 
ATOM   4111  N N     . LYS D 4 403  ? 121.863 110.387 105.473 1.00 73.98  ? 400  LYS A N     1 
ATOM   4112  C CA    . LYS D 4 403  ? 121.448 111.771 105.293 1.00 75.40  ? 400  LYS A CA    1 
ATOM   4113  C C     . LYS D 4 403  ? 122.107 112.670 106.333 1.00 76.42  ? 400  LYS A C     1 
ATOM   4114  O O     . LYS D 4 403  ? 121.693 112.693 107.494 1.00 78.29  ? 400  LYS A O     1 
ATOM   4115  C CB    . LYS D 4 403  ? 119.924 111.889 105.373 1.00 75.22  ? 400  LYS A CB    1 
ATOM   4116  N N     . ILE D 4 404  ? 123.137 113.407 105.919 1.00 77.32  ? 401  ILE A N     1 
ATOM   4117  C CA    . ILE D 4 404  ? 123.875 114.277 106.826 1.00 79.60  ? 401  ILE A CA    1 
ATOM   4118  C C     . ILE D 4 404  ? 123.027 115.496 107.171 1.00 80.05  ? 401  ILE A C     1 
ATOM   4119  O O     . ILE D 4 404  ? 123.005 116.488 106.435 1.00 81.20  ? 401  ILE A O     1 
ATOM   4120  C CB    . ILE D 4 404  ? 125.233 114.686 106.221 1.00 81.75  ? 401  ILE A CB    1 
ATOM   4121  C CG1   . ILE D 4 404  ? 125.090 115.061 104.743 1.00 84.74  ? 401  ILE A CG1   1 
ATOM   4122  C CG2   . ILE D 4 404  ? 126.235 113.555 106.362 1.00 81.77  ? 401  ILE A CG2   1 
ATOM   4123  C CD1   . ILE D 4 404  ? 126.379 115.552 104.113 1.00 85.76  ? 401  ILE A CD1   1 
ATOM   4124  N N     . THR D 4 405  ? 122.316 115.425 108.294 1.00 82.99  ? 402  THR A N     1 
ATOM   4125  C CA    . THR D 4 405  ? 121.499 116.545 108.730 1.00 83.36  ? 402  THR A CA    1 
ATOM   4126  C C     . THR D 4 405  ? 122.386 117.664 109.276 1.00 80.94  ? 402  THR A C     1 
ATOM   4127  O O     . THR D 4 405  ? 123.597 117.510 109.453 1.00 81.11  ? 402  THR A O     1 
ATOM   4128  C CB    . THR D 4 405  ? 120.506 116.101 109.803 1.00 81.38  ? 402  THR A CB    1 
ATOM   4129  O OG1   . THR D 4 405  ? 121.197 115.903 111.042 1.00 80.24  ? 402  THR A OG1   1 
ATOM   4130  C CG2   . THR D 4 405  ? 119.829 114.800 109.396 1.00 79.79  ? 402  THR A CG2   1 
ATOM   4131  N N     . LYS D 4 406  ? 121.761 118.812 109.546 1.00 78.98  ? 403  LYS A N     1 
ATOM   4132  C CA    . LYS D 4 406  ? 122.486 119.887 110.210 1.00 77.98  ? 403  LYS A CA    1 
ATOM   4133  C C     . LYS D 4 406  ? 122.732 119.573 111.680 1.00 78.45  ? 403  LYS A C     1 
ATOM   4134  O O     . LYS D 4 406  ? 123.604 120.196 112.297 1.00 78.31  ? 403  LYS A O     1 
ATOM   4135  C CB    . LYS D 4 406  ? 121.732 121.213 110.072 1.00 79.48  ? 403  LYS A CB    1 
ATOM   4136  C CG    . LYS D 4 406  ? 120.821 121.548 111.242 1.00 83.78  ? 403  LYS A CG    1 
ATOM   4137  C CD    . LYS D 4 406  ? 120.989 123.001 111.658 1.00 85.62  ? 403  LYS A CD    1 
ATOM   4138  C CE    . LYS D 4 406  ? 120.199 123.319 112.916 1.00 86.78  ? 403  LYS A CE    1 
ATOM   4139  N NZ    . LYS D 4 406  ? 120.475 124.698 113.405 1.00 86.12  ? 403  LYS A NZ    1 
ATOM   4140  N N     . SER D 4 407  ? 121.983 118.626 112.249 1.00 74.71  ? 404  SER A N     1 
ATOM   4141  C CA    . SER D 4 407  ? 122.260 118.178 113.609 1.00 71.62  ? 404  SER A CA    1 
ATOM   4142  C C     . SER D 4 407  ? 123.544 117.364 113.667 1.00 65.44  ? 404  SER A C     1 
ATOM   4143  O O     . SER D 4 407  ? 124.324 117.489 114.619 1.00 60.62  ? 404  SER A O     1 
ATOM   4144  C CB    . SER D 4 407  ? 121.082 117.361 114.141 1.00 74.39  ? 404  SER A CB    1 
ATOM   4145  O OG    . SER D 4 407  ? 121.392 116.782 115.397 1.00 75.44  ? 404  SER A OG    1 
ATOM   4146  N N     . ALA D 4 408  ? 123.783 116.526 112.654 1.00 63.23  ? 405  ALA A N     1 
ATOM   4147  C CA    . ALA D 4 408  ? 125.015 115.748 112.612 1.00 61.48  ? 405  ALA A CA    1 
ATOM   4148  C C     . ALA D 4 408  ? 126.237 116.639 112.429 1.00 58.53  ? 405  ALA A C     1 
ATOM   4149  O O     . ALA D 4 408  ? 127.323 116.305 112.915 1.00 58.67  ? 405  ALA A O     1 
ATOM   4150  C CB    . ALA D 4 408  ? 124.945 114.709 111.491 1.00 62.47  ? 405  ALA A CB    1 
ATOM   4151  N N     . LYS D 4 409  ? 126.083 117.770 111.738 1.00 57.00  ? 406  LYS A N     1 
ATOM   4152  C CA    . LYS D 4 409  ? 127.205 118.688 111.578 1.00 56.36  ? 406  LYS A CA    1 
ATOM   4153  C C     . LYS D 4 409  ? 127.533 119.387 112.890 1.00 54.87  ? 406  LYS A C     1 
ATOM   4154  O O     . LYS D 4 409  ? 128.710 119.569 113.226 1.00 53.77  ? 406  LYS A O     1 
ATOM   4155  C CB    . LYS D 4 409  ? 126.901 119.707 110.481 1.00 61.01  ? 406  LYS A CB    1 
ATOM   4156  C CG    . LYS D 4 409  ? 126.692 119.090 109.108 1.00 65.36  ? 406  LYS A CG    1 
ATOM   4157  C CD    . LYS D 4 409  ? 126.679 120.151 108.019 1.00 67.88  ? 406  LYS A CD    1 
ATOM   4158  C CE    . LYS D 4 409  ? 126.590 119.520 106.640 1.00 71.70  ? 406  LYS A CE    1 
ATOM   4159  N NZ    . LYS D 4 409  ? 126.743 120.531 105.555 1.00 73.84  ? 406  LYS A NZ    1 
ATOM   4160  N N     . GLU D 4 410  ? 126.509 119.782 113.649 1.00 55.94  ? 407  GLU A N     1 
ATOM   4161  C CA    . GLU D 4 410  ? 126.751 120.421 114.936 1.00 57.70  ? 407  GLU A CA    1 
ATOM   4162  C C     . GLU D 4 410  ? 127.379 119.456 115.933 1.00 55.32  ? 407  GLU A C     1 
ATOM   4163  O O     . GLU D 4 410  ? 128.140 119.883 116.809 1.00 52.80  ? 407  GLU A O     1 
ATOM   4164  C CB    . GLU D 4 410  ? 125.446 120.994 115.490 1.00 63.55  ? 407  GLU A CB    1 
ATOM   4165  C CG    . GLU D 4 410  ? 124.854 122.098 114.631 1.00 70.51  ? 407  GLU A CG    1 
ATOM   4166  C CD    . GLU D 4 410  ? 123.543 122.623 115.178 1.00 77.80  ? 407  GLU A CD    1 
ATOM   4167  O OE1   . GLU D 4 410  ? 123.043 122.055 116.173 1.00 80.15  ? 407  GLU A OE1   1 
ATOM   4168  O OE2   . GLU D 4 410  ? 123.014 123.604 114.614 1.00 80.58  ? 407  GLU A OE2   1 
ATOM   4169  N N     . LYS D 4 411  ? 127.076 118.160 115.816 1.00 54.41  ? 408  LYS A N     1 
ATOM   4170  C CA    . LYS D 4 411  ? 127.728 117.172 116.671 1.00 49.77  ? 408  LYS A CA    1 
ATOM   4171  C C     . LYS D 4 411  ? 129.211 117.057 116.342 1.00 48.18  ? 408  LYS A C     1 
ATOM   4172  O O     . LYS D 4 411  ? 130.040 116.887 117.245 1.00 49.97  ? 408  LYS A O     1 
ATOM   4173  C CB    . LYS D 4 411  ? 127.038 115.814 116.526 1.00 48.74  ? 408  LYS A CB    1 
ATOM   4174  C CG    . LYS D 4 411  ? 125.615 115.778 117.056 1.00 47.76  ? 408  LYS A CG    1 
ATOM   4175  C CD    . LYS D 4 411  ? 125.030 114.379 116.960 1.00 45.74  ? 408  LYS A CD    1 
ATOM   4176  C CE    . LYS D 4 411  ? 123.630 114.324 117.552 1.00 44.65  ? 408  LYS A CE    1 
ATOM   4177  N NZ    . LYS D 4 411  ? 123.072 112.943 117.529 1.00 44.18  ? 408  LYS A NZ    1 
ATOM   4178  N N     . VAL D 4 412  ? 129.564 117.150 115.059 1.00 46.81  ? 409  VAL A N     1 
ATOM   4179  C CA    . VAL D 4 412  ? 130.971 117.123 114.673 1.00 44.92  ? 409  VAL A CA    1 
ATOM   4180  C C     . VAL D 4 412  ? 131.681 118.382 115.162 1.00 46.96  ? 409  VAL A C     1 
ATOM   4181  O O     . VAL D 4 412  ? 132.844 118.334 115.579 1.00 48.55  ? 409  VAL A O     1 
ATOM   4182  C CB    . VAL D 4 412  ? 131.101 116.945 113.150 1.00 41.72  ? 409  VAL A CB    1 
ATOM   4183  C CG1   . VAL D 4 412  ? 132.555 117.054 112.714 1.00 39.72  ? 409  VAL A CG1   1 
ATOM   4184  C CG2   . VAL D 4 412  ? 130.518 115.604 112.722 1.00 40.35  ? 409  VAL A CG2   1 
ATOM   4185  N N     . GLN D 4 413  ? 130.988 119.524 115.138 1.00 50.27  ? 410  GLN A N     1 
ATOM   4186  C CA    . GLN D 4 413  ? 131.579 120.764 115.635 1.00 54.59  ? 410  GLN A CA    1 
ATOM   4187  C C     . GLN D 4 413  ? 131.876 120.671 117.125 1.00 56.91  ? 410  GLN A C     1 
ATOM   4188  O O     . GLN D 4 413  ? 132.990 120.973 117.570 1.00 58.31  ? 410  GLN A O     1 
ATOM   4189  C CB    . GLN D 4 413  ? 130.646 121.944 115.353 1.00 60.84  ? 410  GLN A CB    1 
ATOM   4190  C CG    . GLN D 4 413  ? 130.461 122.276 113.885 1.00 66.82  ? 410  GLN A CG    1 
ATOM   4191  C CD    . GLN D 4 413  ? 129.666 123.552 113.676 1.00 70.48  ? 410  GLN A CD    1 
ATOM   4192  O OE1   . GLN D 4 413  ? 129.578 124.397 114.566 1.00 73.35  ? 410  GLN A OE1   1 
ATOM   4193  N NE2   . GLN D 4 413  ? 129.076 123.695 112.493 1.00 69.47  ? 410  GLN A NE2   1 
ATOM   4194  N N     . ARG D 4 414  ? 130.883 120.256 117.919 1.00 58.45  ? 411  ARG A N     1 
ATOM   4195  C CA    . ARG D 4 414  ? 131.075 120.180 119.363 1.00 62.08  ? 411  ARG A CA    1 
ATOM   4196  C C     . ARG D 4 414  ? 132.125 119.143 119.740 1.00 60.96  ? 411  ARG A C     1 
ATOM   4197  O O     . ARG D 4 414  ? 132.815 119.301 120.754 1.00 62.33  ? 411  ARG A O     1 
ATOM   4198  C CB    . ARG D 4 414  ? 129.745 119.869 120.053 1.00 68.98  ? 411  ARG A CB    1 
ATOM   4199  C CG    . ARG D 4 414  ? 128.868 121.092 120.293 1.00 74.07  ? 411  ARG A CG    1 
ATOM   4200  C CD    . ARG D 4 414  ? 127.433 120.851 119.854 1.00 77.19  ? 411  ARG A CD    1 
ATOM   4201  N NE    . ARG D 4 414  ? 126.861 119.652 120.457 1.00 80.01  ? 411  ARG A NE    1 
ATOM   4202  C CZ    . ARG D 4 414  ? 125.650 119.179 120.175 1.00 82.13  ? 411  ARG A CZ    1 
ATOM   4203  N NH1   . ARG D 4 414  ? 124.882 119.806 119.295 1.00 82.60  ? 411  ARG A NH1   1 
ATOM   4204  N NH2   . ARG D 4 414  ? 125.212 118.079 120.770 1.00 82.76  ? 411  ARG A NH2   1 
ATOM   4205  N N     . SER D 4 415  ? 132.268 118.084 118.940 1.00 59.70  ? 412  SER A N     1 
ATOM   4206  C CA    . SER D 4 415  ? 133.268 117.066 119.241 1.00 60.25  ? 412  SER A CA    1 
ATOM   4207  C C     . SER D 4 415  ? 134.681 117.619 119.099 1.00 59.40  ? 412  SER A C     1 
ATOM   4208  O O     . SER D 4 415  ? 135.577 117.255 119.871 1.00 59.22  ? 412  SER A O     1 
ATOM   4209  C CB    . SER D 4 415  ? 133.071 115.850 118.336 1.00 59.64  ? 412  SER A CB    1 
ATOM   4210  O OG    . SER D 4 415  ? 133.227 116.196 116.971 1.00 57.95  ? 412  SER A OG    1 
ATOM   4211  N N     . LEU D 4 416  ? 134.899 118.507 118.128 1.00 57.65  ? 413  LEU A N     1 
ATOM   4212  C CA    . LEU D 4 416  ? 136.226 119.066 117.894 1.00 56.59  ? 413  LEU A CA    1 
ATOM   4213  C C     . LEU D 4 416  ? 136.649 120.068 118.960 1.00 56.85  ? 413  LEU A C     1 
ATOM   4214  O O     . LEU D 4 416  ? 137.830 120.428 119.008 1.00 57.64  ? 413  LEU A O     1 
ATOM   4215  C CB    . LEU D 4 416  ? 136.277 119.731 116.517 1.00 55.53  ? 413  LEU A CB    1 
ATOM   4216  C CG    . LEU D 4 416  ? 136.124 118.800 115.313 1.00 56.32  ? 413  LEU A CG    1 
ATOM   4217  C CD1   . LEU D 4 416  ? 136.110 119.592 114.015 1.00 56.37  ? 413  LEU A CD1   1 
ATOM   4218  C CD2   . LEU D 4 416  ? 137.238 117.763 115.297 1.00 57.40  ? 413  LEU A CD2   1 
ATOM   4219  N N     . LYS D 4 417  ? 135.729 120.528 119.809 1.00 58.81  ? 414  LYS A N     1 
ATOM   4220  C CA    . LYS D 4 417  ? 136.094 121.507 120.826 1.00 62.96  ? 414  LYS A CA    1 
ATOM   4221  C C     . LYS D 4 417  ? 136.762 120.867 122.035 1.00 70.32  ? 414  LYS A C     1 
ATOM   4222  O O     . LYS D 4 417  ? 137.656 121.474 122.634 1.00 74.45  ? 414  LYS A O     1 
ATOM   4223  C CB    . LYS D 4 417  ? 134.864 122.295 121.279 1.00 64.17  ? 414  LYS A CB    1 
ATOM   4224  C CG    . LYS D 4 417  ? 134.349 123.303 120.268 1.00 65.36  ? 414  LYS A CG    1 
ATOM   4225  C CD    . LYS D 4 417  ? 133.263 124.169 120.882 1.00 68.65  ? 414  LYS A CD    1 
ATOM   4226  C CE    . LYS D 4 417  ? 132.671 125.129 119.866 1.00 71.61  ? 414  LYS A CE    1 
ATOM   4227  N NZ    . LYS D 4 417  ? 131.669 126.037 120.491 1.00 73.27  ? 414  LYS A NZ    1 
ATOM   4228  N N     . HIS D 4 418  ? 136.353 119.653 122.411 1.00 73.22  ? 415  HIS A N     1 
ATOM   4229  C CA    . HIS D 4 418  ? 136.829 119.023 123.639 1.00 78.11  ? 415  HIS A CA    1 
ATOM   4230  C C     . HIS D 4 418  ? 137.172 117.549 123.409 1.00 80.86  ? 415  HIS A C     1 
ATOM   4231  O O     . HIS D 4 418  ? 136.625 116.646 124.035 1.00 82.13  ? 415  HIS A O     1 
ATOM   4232  C CB    . HIS D 4 418  ? 135.797 119.184 124.756 1.00 82.40  ? 415  HIS A CB    1 
ATOM   4233  C CG    . HIS D 4 418  ? 134.439 118.654 124.413 1.00 85.61  ? 415  HIS A CG    1 
ATOM   4234  N ND1   . HIS D 4 418  ? 134.207 117.326 124.124 1.00 86.50  ? 415  HIS A ND1   1 
ATOM   4235  C CD2   . HIS D 4 418  ? 133.237 119.272 124.323 1.00 87.03  ? 415  HIS A CD2   1 
ATOM   4236  C CE1   . HIS D 4 418  ? 132.922 117.150 123.865 1.00 87.72  ? 415  HIS A CE1   1 
ATOM   4237  N NE2   . HIS D 4 418  ? 132.312 118.317 123.979 1.00 88.00  ? 415  HIS A NE2   1 
ATOM   4238  N N     . GLU D 4 419  ? 138.109 117.293 122.500 1.00 83.95  ? 416  GLU A N     1 
ATOM   4239  C CA    . GLU D 4 419  ? 138.669 115.955 122.360 1.00 83.79  ? 416  GLU A CA    1 
ATOM   4240  C C     . GLU D 4 419  ? 140.052 116.072 121.737 1.00 78.53  ? 416  GLU A C     1 
ATOM   4241  O O     . GLU D 4 419  ? 140.330 117.007 120.982 1.00 77.95  ? 416  GLU A O     1 
ATOM   4242  C CB    . GLU D 4 419  ? 137.779 115.032 121.518 1.00 87.67  ? 416  GLU A CB    1 
ATOM   4243  C CG    . GLU D 4 419  ? 137.944 115.177 120.014 1.00 90.17  ? 416  GLU A CG    1 
ATOM   4244  C CD    . GLU D 4 419  ? 137.590 113.904 119.268 1.00 93.38  ? 416  GLU A CD    1 
ATOM   4245  O OE1   . GLU D 4 419  ? 138.481 113.043 119.105 1.00 94.41  ? 416  GLU A OE1   1 
ATOM   4246  O OE2   . GLU D 4 419  ? 136.420 113.757 118.857 1.00 94.47  ? 416  GLU A OE2   1 
ATOM   4247  N N     . ASP D 4 420  ? 140.916 115.116 122.068 1.00 71.23  ? 417  ASP A N     1 
ATOM   4248  C CA    . ASP D 4 420  ? 142.273 115.113 121.544 1.00 65.54  ? 417  ASP A CA    1 
ATOM   4249  C C     . ASP D 4 420  ? 142.299 114.431 120.184 1.00 63.16  ? 417  ASP A C     1 
ATOM   4250  O O     . ASP D 4 420  ? 141.766 113.331 120.021 1.00 65.36  ? 417  ASP A O     1 
ATOM   4251  C CB    . ASP D 4 420  ? 143.220 114.408 122.513 1.00 65.54  ? 417  ASP A CB    1 
ATOM   4252  C CG    . ASP D 4 420  ? 143.259 115.073 123.872 1.00 66.13  ? 417  ASP A CG    1 
ATOM   4253  O OD1   . ASP D 4 420  ? 143.188 116.320 123.930 1.00 63.56  ? 417  ASP A OD1   1 
ATOM   4254  O OD2   . ASP D 4 420  ? 143.354 114.349 124.884 1.00 69.64  ? 417  ASP A OD2   1 
ATOM   4255  N N     . ILE D 4 421  ? 142.911 115.094 119.205 1.00 60.55  ? 418  ILE A N     1 
ATOM   4256  C CA    . ILE D 4 421  ? 143.010 114.582 117.846 1.00 60.91  ? 418  ILE A CA    1 
ATOM   4257  C C     . ILE D 4 421  ? 144.360 113.898 117.688 1.00 63.56  ? 418  ILE A C     1 
ATOM   4258  O O     . ILE D 4 421  ? 145.391 114.439 118.105 1.00 67.57  ? 418  ILE A O     1 
ATOM   4259  C CB    . ILE D 4 421  ? 142.846 115.707 116.811 1.00 62.30  ? 418  ILE A CB    1 
ATOM   4260  C CG1   . ILE D 4 421  ? 141.708 116.651 117.210 1.00 60.60  ? 418  ILE A CG1   1 
ATOM   4261  C CG2   . ILE D 4 421  ? 142.596 115.120 115.427 1.00 64.15  ? 418  ILE A CG2   1 
ATOM   4262  C CD1   . ILE D 4 421  ? 140.339 116.010 117.192 1.00 59.92  ? 418  ILE A CD1   1 
ATOM   4263  N N     . ASN D 4 422  ? 144.360 112.708 117.090 1.00 63.00  ? 419  ASN A N     1 
ATOM   4264  C CA    . ASN D 4 422  ? 145.619 112.040 116.803 1.00 62.27  ? 419  ASN A CA    1 
ATOM   4265  C C     . ASN D 4 422  ? 146.310 112.715 115.624 1.00 59.36  ? 419  ASN A C     1 
ATOM   4266  O O     . ASN D 4 422  ? 145.668 113.319 114.759 1.00 57.11  ? 419  ASN A O     1 
ATOM   4267  C CB    . ASN D 4 422  ? 145.398 110.553 116.518 1.00 65.14  ? 419  ASN A CB    1 
ATOM   4268  C CG    . ASN D 4 422  ? 144.549 110.311 115.287 1.00 67.96  ? 419  ASN A CG    1 
ATOM   4269  O OD1   . ASN D 4 422  ? 145.026 110.422 114.157 1.00 67.95  ? 419  ASN A OD1   1 
ATOM   4270  N ND2   . ASN D 4 422  ? 143.286 109.958 115.500 1.00 70.51  ? 419  ASN A ND2   1 
ATOM   4271  N N     . LEU D 4 423  ? 147.641 112.609 115.597 1.00 59.65  ? 420  LEU A N     1 
ATOM   4272  C CA    . LEU D 4 423  ? 148.424 113.324 114.596 1.00 57.46  ? 420  LEU A CA    1 
ATOM   4273  C C     . LEU D 4 423  ? 148.126 112.835 113.180 1.00 55.20  ? 420  LEU A C     1 
ATOM   4274  O O     . LEU D 4 423  ? 148.260 113.605 112.224 1.00 55.83  ? 420  LEU A O     1 
ATOM   4275  C CB    . LEU D 4 423  ? 149.916 113.188 114.905 1.00 55.94  ? 420  LEU A CB    1 
ATOM   4276  C CG    . LEU D 4 423  ? 150.876 114.038 114.070 1.00 52.83  ? 420  LEU A CG    1 
ATOM   4277  C CD1   . LEU D 4 423  ? 150.495 115.509 114.144 1.00 50.48  ? 420  LEU A CD1   1 
ATOM   4278  C CD2   . LEU D 4 423  ? 152.313 113.832 114.527 1.00 53.36  ? 420  LEU A CD2   1 
ATOM   4279  N N     . GLN D 4 424  ? 147.715 111.574 113.026 1.00 54.17  ? 421  GLN A N     1 
ATOM   4280  C CA    . GLN D 4 424  ? 147.450 111.055 111.688 1.00 57.88  ? 421  GLN A CA    1 
ATOM   4281  C C     . GLN D 4 424  ? 146.206 111.694 111.080 1.00 57.24  ? 421  GLN A C     1 
ATOM   4282  O O     . GLN D 4 424  ? 146.199 112.039 109.893 1.00 58.01  ? 421  GLN A O     1 
ATOM   4283  C CB    . GLN D 4 424  ? 147.304 109.534 111.729 1.00 62.21  ? 421  GLN A CB    1 
ATOM   4284  C CG    . GLN D 4 424  ? 147.161 108.901 110.353 1.00 66.03  ? 421  GLN A CG    1 
ATOM   4285  C CD    . GLN D 4 424  ? 148.313 109.250 109.431 1.00 70.27  ? 421  GLN A CD    1 
ATOM   4286  O OE1   . GLN D 4 424  ? 149.481 109.154 109.814 1.00 74.17  ? 421  GLN A OE1   1 
ATOM   4287  N NE2   . GLN D 4 424  ? 147.992 109.670 108.213 1.00 67.95  ? 421  GLN A NE2   1 
ATOM   4288  N N     . GLU D 4 425  ? 145.146 111.861 111.875 1.00 54.96  ? 422  GLU A N     1 
ATOM   4289  C CA    . GLU D 4 425  ? 143.936 112.493 111.362 1.00 53.95  ? 422  GLU A CA    1 
ATOM   4290  C C     . GLU D 4 425  ? 144.181 113.950 110.990 1.00 52.50  ? 422  GLU A C     1 
ATOM   4291  O O     . GLU D 4 425  ? 143.509 114.483 110.099 1.00 50.75  ? 422  GLU A O     1 
ATOM   4292  C CB    . GLU D 4 425  ? 142.806 112.389 112.387 1.00 56.69  ? 422  GLU A CB    1 
ATOM   4293  C CG    . GLU D 4 425  ? 141.441 112.790 111.843 1.00 60.25  ? 422  GLU A CG    1 
ATOM   4294  C CD    . GLU D 4 425  ? 140.344 112.707 112.889 1.00 65.93  ? 422  GLU A CD    1 
ATOM   4295  O OE1   . GLU D 4 425  ? 140.670 112.656 114.094 1.00 70.77  ? 422  GLU A OE1   1 
ATOM   4296  O OE2   . GLU D 4 425  ? 139.155 112.694 112.504 1.00 65.23  ? 422  GLU A OE2   1 
ATOM   4297  N N     . ILE D 4 426  ? 145.139 114.605 111.648 1.00 52.90  ? 423  ILE A N     1 
ATOM   4298  C CA    . ILE D 4 426  ? 145.474 115.978 111.286 1.00 54.91  ? 423  ILE A CA    1 
ATOM   4299  C C     . ILE D 4 426  ? 146.178 116.016 109.936 1.00 58.00  ? 423  ILE A C     1 
ATOM   4300  O O     . ILE D 4 426  ? 145.864 116.851 109.079 1.00 59.25  ? 423  ILE A O     1 
ATOM   4301  C CB    . ILE D 4 426  ? 146.327 116.629 112.389 1.00 51.61  ? 423  ILE A CB    1 
ATOM   4302  C CG1   . ILE D 4 426  ? 145.592 116.586 113.730 1.00 51.48  ? 423  ILE A CG1   1 
ATOM   4303  C CG2   . ILE D 4 426  ? 146.674 118.064 112.023 1.00 47.13  ? 423  ILE A CG2   1 
ATOM   4304  C CD1   . ILE D 4 426  ? 146.355 117.240 114.862 1.00 51.56  ? 423  ILE A CD1   1 
ATOM   4305  N N     . ILE D 4 427  ? 147.134 115.108 109.720 1.00 59.00  ? 424  ILE A N     1 
ATOM   4306  C CA    . ILE D 4 427  ? 147.872 115.085 108.462 1.00 60.20  ? 424  ILE A CA    1 
ATOM   4307  C C     . ILE D 4 427  ? 146.959 114.681 107.311 1.00 60.59  ? 424  ILE A C     1 
ATOM   4308  O O     . ILE D 4 427  ? 147.022 115.257 106.219 1.00 61.13  ? 424  ILE A O     1 
ATOM   4309  C CB    . ILE D 4 427  ? 149.089 114.148 108.577 1.00 61.48  ? 424  ILE A CB    1 
ATOM   4310  C CG1   . ILE D 4 427  ? 150.054 114.659 109.647 1.00 60.61  ? 424  ILE A CG1   1 
ATOM   4311  C CG2   . ILE D 4 427  ? 149.794 114.012 107.236 1.00 63.62  ? 424  ILE A CG2   1 
ATOM   4312  C CD1   . ILE D 4 427  ? 151.273 113.785 109.837 1.00 60.75  ? 424  ILE A CD1   1 
ATOM   4313  N N     . SER D 4 428  ? 146.089 113.694 107.537 1.00 59.87  ? 425  SER A N     1 
ATOM   4314  C CA    . SER D 4 428  ? 145.182 113.240 106.489 1.00 60.24  ? 425  SER A CA    1 
ATOM   4315  C C     . SER D 4 428  ? 144.145 114.291 106.117 1.00 60.39  ? 425  SER A C     1 
ATOM   4316  O O     . SER D 4 428  ? 143.552 114.201 105.038 1.00 61.34  ? 425  SER A O     1 
ATOM   4317  C CB    . SER D 4 428  ? 144.478 111.954 106.924 1.00 61.33  ? 425  SER A CB    1 
ATOM   4318  O OG    . SER D 4 428  ? 145.412 110.924 107.189 1.00 64.10  ? 425  SER A OG    1 
ATOM   4319  N N     . ALA D 4 429  ? 143.917 115.282 106.978 1.00 58.46  ? 426  ALA A N     1 
ATOM   4320  C CA    . ALA D 4 429  ? 142.914 116.309 106.725 1.00 56.73  ? 426  ALA A CA    1 
ATOM   4321  C C     . ALA D 4 429  ? 143.503 117.631 106.257 1.00 56.81  ? 426  ALA A C     1 
ATOM   4322  O O     . ALA D 4 429  ? 142.811 118.397 105.578 1.00 54.87  ? 426  ALA A O     1 
ATOM   4323  C CB    . ALA D 4 429  ? 142.078 116.554 107.985 1.00 55.01  ? 426  ALA A CB    1 
ATOM   4324  N N     . ALA D 4 430  ? 144.756 117.921 106.601 1.00 58.19  ? 427  ALA A N     1 
ATOM   4325  C CA    . ALA D 4 430  ? 145.364 119.204 106.273 1.00 60.00  ? 427  ALA A CA    1 
ATOM   4326  C C     . ALA D 4 430  ? 146.246 119.160 105.034 1.00 63.25  ? 427  ALA A C     1 
ATOM   4327  O O     . ALA D 4 430  ? 146.417 120.192 104.379 1.00 64.89  ? 427  ALA A O     1 
ATOM   4328  C CB    . ALA D 4 430  ? 146.192 119.715 107.457 1.00 60.15  ? 427  ALA A CB    1 
ATOM   4329  N N     . GLY D 4 431  ? 146.803 118.007 104.701 1.00 64.73  ? 428  GLY A N     1 
ATOM   4330  C CA    . GLY D 4 431  ? 147.666 117.866 103.546 1.00 66.84  ? 428  GLY A CA    1 
ATOM   4331  C C     . GLY D 4 431  ? 149.128 117.730 103.939 1.00 70.62  ? 428  GLY A C     1 
ATOM   4332  O O     . GLY D 4 431  ? 149.516 117.868 105.099 1.00 71.44  ? 428  GLY A O     1 
ATOM   4333  N N     . LYS D 4 432  ? 149.948 117.458 102.921 1.00 75.03  ? 429  LYS A N     1 
ATOM   4334  C CA    . LYS D 4 432  ? 151.373 117.248 103.150 1.00 78.06  ? 429  LYS A CA    1 
ATOM   4335  C C     . LYS D 4 432  ? 152.095 118.529 103.546 1.00 81.83  ? 429  LYS A C     1 
ATOM   4336  O O     . LYS D 4 432  ? 153.202 118.456 104.090 1.00 84.59  ? 429  LYS A O     1 
ATOM   4337  C CB    . LYS D 4 432  ? 152.026 116.651 101.902 1.00 77.14  ? 429  LYS A CB    1 
ATOM   4338  C CG    . LYS D 4 432  ? 152.072 117.592 100.708 1.00 75.93  ? 429  LYS A CG    1 
ATOM   4339  C CD    . LYS D 4 432  ? 152.768 116.937 99.524  1.00 76.10  ? 429  LYS A CD    1 
ATOM   4340  C CE    . LYS D 4 432  ? 152.910 117.906 98.360  1.00 75.72  ? 429  LYS A CE    1 
ATOM   4341  N NZ    . LYS D 4 432  ? 153.564 117.269 97.183  1.00 75.64  ? 429  LYS A NZ    1 
ATOM   4342  N N     . GLU D 4 433  ? 151.501 119.696 103.292 1.00 83.67  ? 430  GLU A N     1 
ATOM   4343  C CA    . GLU D 4 433  ? 152.151 120.952 103.642 1.00 84.17  ? 430  GLU A CA    1 
ATOM   4344  C C     . GLU D 4 433  ? 152.147 121.225 105.140 1.00 80.64  ? 430  GLU A C     1 
ATOM   4345  O O     . GLU D 4 433  ? 152.888 122.105 105.590 1.00 80.72  ? 430  GLU A O     1 
ATOM   4346  C CB    . GLU D 4 433  ? 151.491 122.115 102.897 1.00 88.06  ? 430  GLU A CB    1 
ATOM   4347  C CG    . GLU D 4 433  ? 151.846 122.183 101.418 1.00 93.19  ? 430  GLU A CG    1 
ATOM   4348  C CD    . GLU D 4 433  ? 153.348 122.186 101.175 1.00 97.69  ? 430  GLU A CD    1 
ATOM   4349  O OE1   . GLU D 4 433  ? 153.975 123.256 101.330 1.00 98.64  ? 430  GLU A OE1   1 
ATOM   4350  O OE2   . GLU D 4 433  ? 153.902 121.119 100.840 1.00 99.47  ? 430  GLU A OE2   1 
ATOM   4351  N N     . LEU D 4 434  ? 151.338 120.504 105.919 1.00 76.25  ? 431  LEU A N     1 
ATOM   4352  C CA    . LEU D 4 434  ? 151.438 120.620 107.368 1.00 73.45  ? 431  LEU A CA    1 
ATOM   4353  C C     . LEU D 4 434  ? 152.652 119.870 107.895 1.00 75.00  ? 431  LEU A C     1 
ATOM   4354  O O     . LEU D 4 434  ? 153.327 120.345 108.816 1.00 73.35  ? 431  LEU A O     1 
ATOM   4355  C CB    . LEU D 4 434  ? 150.163 120.100 108.037 1.00 69.31  ? 431  LEU A CB    1 
ATOM   4356  C CG    . LEU D 4 434  ? 150.121 120.157 109.567 1.00 66.05  ? 431  LEU A CG    1 
ATOM   4357  C CD1   . LEU D 4 434  ? 148.732 120.510 110.028 1.00 63.30  ? 431  LEU A CD1   1 
ATOM   4358  C CD2   . LEU D 4 434  ? 150.551 118.837 110.199 1.00 66.91  ? 431  LEU A CD2   1 
ATOM   4359  N N     . SER D 4 435  ? 152.937 118.695 107.329 1.00 77.08  ? 432  SER A N     1 
ATOM   4360  C CA    . SER D 4 435  ? 154.117 117.943 107.739 1.00 78.73  ? 432  SER A CA    1 
ATOM   4361  C C     . SER D 4 435  ? 155.385 118.756 107.521 1.00 80.79  ? 432  SER A C     1 
ATOM   4362  O O     . SER D 4 435  ? 156.279 118.766 108.376 1.00 83.35  ? 432  SER A O     1 
ATOM   4363  C CB    . SER D 4 435  ? 154.185 116.620 106.977 1.00 77.43  ? 432  SER A CB    1 
ATOM   4364  O OG    . SER D 4 435  ? 152.977 115.891 107.116 1.00 74.11  ? 432  SER A OG    1 
ATOM   4365  N N     . GLU D 4 436  ? 155.477 119.455 106.387 1.00 81.23  ? 433  GLU A N     1 
ATOM   4366  C CA    . GLU D 4 436  ? 156.630 120.317 106.143 1.00 83.87  ? 433  GLU A CA    1 
ATOM   4367  C C     . GLU D 4 436  ? 156.673 121.471 107.137 1.00 81.75  ? 433  GLU A C     1 
ATOM   4368  O O     . GLU D 4 436  ? 157.751 121.874 107.583 1.00 84.25  ? 433  GLU A O     1 
ATOM   4369  C CB    . GLU D 4 436  ? 156.602 120.842 104.709 1.00 87.14  ? 433  GLU A CB    1 
ATOM   4370  C CG    . GLU D 4 436  ? 156.779 119.768 103.648 1.00 92.14  ? 433  GLU A CG    1 
ATOM   4371  C CD    . GLU D 4 436  ? 158.028 118.934 103.867 1.00 98.50  ? 433  GLU A CD    1 
ATOM   4372  O OE1   . GLU D 4 436  ? 159.137 119.441 103.597 1.00 99.42  ? 433  GLU A OE1   1 
ATOM   4373  O OE2   . GLU D 4 436  ? 157.900 117.776 104.317 1.00 101.10 ? 433  GLU A OE2   1 
ATOM   4374  N N     . ALA D 4 437  ? 155.507 122.013 107.497 1.00 78.11  ? 434  ALA A N     1 
ATOM   4375  C CA    . ALA D 4 437  ? 155.463 123.050 108.523 1.00 73.42  ? 434  ALA A CA    1 
ATOM   4376  C C     . ALA D 4 437  ? 155.805 122.479 109.892 1.00 70.08  ? 434  ALA A C     1 
ATOM   4377  O O     . ALA D 4 437  ? 156.479 123.137 110.695 1.00 72.44  ? 434  ALA A O     1 
ATOM   4378  C CB    . ALA D 4 437  ? 154.086 123.713 108.544 1.00 68.60  ? 434  ALA A CB    1 
ATOM   4379  N N     . PHE D 4 438  ? 155.351 121.257 110.174 1.00 65.40  ? 435  PHE A N     1 
ATOM   4380  C CA    . PHE D 4 438  ? 155.671 120.621 111.450 1.00 64.44  ? 435  PHE A CA    1 
ATOM   4381  C C     . PHE D 4 438  ? 157.155 120.296 111.542 1.00 67.81  ? 435  PHE A C     1 
ATOM   4382  O O     . PHE D 4 438  ? 157.772 120.486 112.596 1.00 72.12  ? 435  PHE A O     1 
ATOM   4383  C CB    . PHE D 4 438  ? 154.827 119.359 111.631 1.00 66.88  ? 435  PHE A CB    1 
ATOM   4384  C CG    . PHE D 4 438  ? 154.729 118.891 113.057 1.00 70.76  ? 435  PHE A CG    1 
ATOM   4385  C CD1   . PHE D 4 438  ? 155.726 118.110 113.619 1.00 73.90  ? 435  PHE A CD1   1 
ATOM   4386  C CD2   . PHE D 4 438  ? 153.629 119.225 113.832 1.00 70.82  ? 435  PHE A CD2   1 
ATOM   4387  C CE1   . PHE D 4 438  ? 155.633 117.677 114.929 1.00 74.01  ? 435  PHE A CE1   1 
ATOM   4388  C CE2   . PHE D 4 438  ? 153.531 118.794 115.144 1.00 71.95  ? 435  PHE A CE2   1 
ATOM   4389  C CZ    . PHE D 4 438  ? 154.535 118.019 115.692 1.00 73.00  ? 435  PHE A CZ    1 
ATOM   4390  N N     . LYS D 4 439  ? 157.745 119.799 110.451 1.00 68.66  ? 436  LYS A N     1 
ATOM   4391  C CA    . LYS D 4 439  ? 159.174 119.500 110.449 1.00 71.97  ? 436  LYS A CA    1 
ATOM   4392  C C     . LYS D 4 439  ? 160.001 120.771 110.598 1.00 75.23  ? 436  LYS A C     1 
ATOM   4393  O O     . LYS D 4 439  ? 160.950 120.820 111.390 1.00 78.49  ? 436  LYS A O     1 
ATOM   4394  C CB    . LYS D 4 439  ? 159.559 118.764 109.166 1.00 74.40  ? 436  LYS A CB    1 
ATOM   4395  C CG    . LYS D 4 439  ? 159.005 117.356 109.036 1.00 75.85  ? 436  LYS A CG    1 
ATOM   4396  C CD    . LYS D 4 439  ? 159.367 116.764 107.681 1.00 77.22  ? 436  LYS A CD    1 
ATOM   4397  C CE    . LYS D 4 439  ? 158.678 115.432 107.449 1.00 77.04  ? 436  LYS A CE    1 
ATOM   4398  N NZ    . LYS D 4 439  ? 159.051 114.437 108.488 1.00 78.26  ? 436  LYS A NZ    1 
ATOM   4399  N N     . GLN D 4 440  ? 159.654 121.813 109.839 1.00 74.16  ? 437  GLN A N     1 
ATOM   4400  C CA    . GLN D 4 440  ? 160.439 123.043 109.863 1.00 73.05  ? 437  GLN A CA    1 
ATOM   4401  C C     . GLN D 4 440  ? 160.345 123.738 111.215 1.00 71.98  ? 437  GLN A C     1 
ATOM   4402  O O     . GLN D 4 440  ? 161.351 124.234 111.735 1.00 71.92  ? 437  GLN A O     1 
ATOM   4403  C CB    . GLN D 4 440  ? 159.984 123.980 108.744 1.00 70.87  ? 437  GLN A CB    1 
ATOM   4404  N N     . LYS D 4 441  ? 159.147 123.784 111.804 1.00 71.57  ? 438  LYS A N     1 
ATOM   4405  C CA    . LYS D 4 441  ? 158.989 124.441 113.098 1.00 73.43  ? 438  LYS A CA    1 
ATOM   4406  C C     . LYS D 4 441  ? 159.683 123.658 114.203 1.00 76.29  ? 438  LYS A C     1 
ATOM   4407  O O     . LYS D 4 441  ? 160.233 124.250 115.140 1.00 78.76  ? 438  LYS A O     1 
ATOM   4408  C CB    . LYS D 4 441  ? 157.506 124.616 113.424 1.00 72.83  ? 438  LYS A CB    1 
ATOM   4409  C CG    . LYS D 4 441  ? 157.222 125.586 114.563 1.00 72.88  ? 438  LYS A CG    1 
ATOM   4410  C CD    . LYS D 4 441  ? 157.170 127.023 114.061 1.00 73.60  ? 438  LYS A CD    1 
ATOM   4411  C CE    . LYS D 4 441  ? 156.964 128.011 115.200 1.00 75.06  ? 438  LYS A CE    1 
ATOM   4412  N NZ    . LYS D 4 441  ? 158.158 128.095 116.088 1.00 78.59  ? 438  LYS A NZ    1 
ATOM   4413  N N     . THR D 4 442  ? 159.668 122.325 114.113 1.00 78.54  ? 439  THR A N     1 
ATOM   4414  C CA    . THR D 4 442  ? 160.300 121.507 115.142 1.00 81.90  ? 439  THR A CA    1 
ATOM   4415  C C     . THR D 4 442  ? 161.815 121.678 115.130 1.00 85.48  ? 439  THR A C     1 
ATOM   4416  O O     . THR D 4 442  ? 162.434 121.886 116.178 1.00 86.85  ? 439  THR A O     1 
ATOM   4417  C CB    . THR D 4 442  ? 159.919 120.038 114.953 1.00 83.01  ? 439  THR A CB    1 
ATOM   4418  O OG1   . THR D 4 442  ? 158.498 119.895 115.062 1.00 82.75  ? 439  THR A OG1   1 
ATOM   4419  C CG2   . THR D 4 442  ? 160.592 119.177 116.005 1.00 84.91  ? 439  THR A CG2   1 
ATOM   4420  N N     . SER D 4 443  ? 162.430 121.591 113.948 1.00 86.01  ? 440  SER A N     1 
ATOM   4421  C CA    . SER D 4 443  ? 163.873 121.780 113.859 1.00 87.83  ? 440  SER A CA    1 
ATOM   4422  C C     . SER D 4 443  ? 164.268 123.215 114.185 1.00 85.40  ? 440  SER A C     1 
ATOM   4423  O O     . SER D 4 443  ? 165.351 123.446 114.733 1.00 87.95  ? 440  SER A O     1 
ATOM   4424  C CB    . SER D 4 443  ? 164.374 121.400 112.465 1.00 89.67  ? 440  SER A CB    1 
ATOM   4425  O OG    . SER D 4 443  ? 163.922 122.323 111.490 1.00 89.22  ? 440  SER A OG    1 
ATOM   4426  N N     . GLU D 4 444  ? 163.412 124.184 113.858 1.00 81.24  ? 441  GLU A N     1 
ATOM   4427  C CA    . GLU D 4 444  ? 163.704 125.578 114.174 1.00 80.45  ? 441  GLU A CA    1 
ATOM   4428  C C     . GLU D 4 444  ? 163.773 125.789 115.683 1.00 77.42  ? 441  GLU A C     1 
ATOM   4429  O O     . GLU D 4 444  ? 164.683 126.455 116.189 1.00 74.97  ? 441  GLU A O     1 
ATOM   4430  C CB    . GLU D 4 444  ? 162.643 126.488 113.551 1.00 83.37  ? 441  GLU A CB    1 
ATOM   4431  C CG    . GLU D 4 444  ? 162.962 127.972 113.611 1.00 89.14  ? 441  GLU A CG    1 
ATOM   4432  C CD    . GLU D 4 444  ? 161.793 128.831 113.163 1.00 91.57  ? 441  GLU A CD    1 
ATOM   4433  O OE1   . GLU D 4 444  ? 160.791 128.909 113.906 1.00 90.05  ? 441  GLU A OE1   1 
ATOM   4434  O OE2   . GLU D 4 444  ? 161.872 129.419 112.065 1.00 93.69  ? 441  GLU A OE2   1 
ATOM   4435  N N     . ILE D 4 445  ? 162.813 125.223 116.418 1.00 77.37  ? 442  ILE A N     1 
ATOM   4436  C CA    . ILE D 4 445  ? 162.818 125.344 117.871 1.00 77.48  ? 442  ILE A CA    1 
ATOM   4437  C C     . ILE D 4 445  ? 163.960 124.536 118.474 1.00 81.29  ? 442  ILE A C     1 
ATOM   4438  O O     . ILE D 4 445  ? 164.654 125.000 119.388 1.00 83.89  ? 442  ILE A O     1 
ATOM   4439  C CB    . ILE D 4 445  ? 161.454 124.916 118.444 1.00 71.65  ? 442  ILE A CB    1 
ATOM   4440  C CG1   . ILE D 4 445  ? 160.356 125.871 117.976 1.00 68.15  ? 442  ILE A CG1   1 
ATOM   4441  C CG2   . ILE D 4 445  ? 161.503 124.861 119.963 1.00 70.36  ? 442  ILE A CG2   1 
ATOM   4442  C CD1   . ILE D 4 445  ? 158.971 125.487 118.452 1.00 65.90  ? 442  ILE A CD1   1 
ATOM   4443  N N     . LEU D 4 446  ? 164.179 123.317 117.969 1.00 83.47  ? 443  LEU A N     1 
ATOM   4444  C CA    . LEU D 4 446  ? 165.236 122.467 118.510 1.00 85.31  ? 443  LEU A CA    1 
ATOM   4445  C C     . LEU D 4 446  ? 166.616 123.058 118.252 1.00 86.32  ? 443  LEU A C     1 
ATOM   4446  O O     . LEU D 4 446  ? 167.510 122.948 119.100 1.00 86.56  ? 443  LEU A O     1 
ATOM   4447  C CB    . LEU D 4 446  ? 165.133 121.062 117.918 1.00 86.70  ? 443  LEU A CB    1 
ATOM   4448  C CG    . LEU D 4 446  ? 163.996 120.184 118.447 1.00 87.22  ? 443  LEU A CG    1 
ATOM   4449  C CD1   . LEU D 4 446  ? 163.916 118.877 117.673 1.00 88.01  ? 443  LEU A CD1   1 
ATOM   4450  C CD2   . LEU D 4 446  ? 164.176 119.921 119.933 1.00 88.52  ? 443  LEU A CD2   1 
ATOM   4451  N N     . SER D 4 447  ? 166.813 123.688 117.092 1.00 88.14  ? 444  SER A N     1 
ATOM   4452  C CA    . SER D 4 447  ? 168.106 124.297 116.800 1.00 91.13  ? 444  SER A CA    1 
ATOM   4453  C C     . SER D 4 447  ? 168.366 125.499 117.700 1.00 90.72  ? 444  SER A C     1 
ATOM   4454  O O     . SER D 4 447  ? 169.495 125.701 118.162 1.00 92.77  ? 444  SER A O     1 
ATOM   4455  C CB    . SER D 4 447  ? 168.183 124.703 115.328 1.00 93.47  ? 444  SER A CB    1 
ATOM   4456  O OG    . SER D 4 447  ? 167.189 125.663 115.010 1.00 94.40  ? 444  SER A OG    1 
ATOM   4457  N N     . HIS D 4 448  ? 167.335 126.306 117.963 1.00 87.50  ? 445  HIS A N     1 
ATOM   4458  C CA    . HIS D 4 448  ? 167.507 127.458 118.843 1.00 87.46  ? 445  HIS A CA    1 
ATOM   4459  C C     . HIS D 4 448  ? 167.811 127.025 120.272 1.00 89.75  ? 445  HIS A C     1 
ATOM   4460  O O     . HIS D 4 448  ? 168.645 127.638 120.947 1.00 85.95  ? 445  HIS A O     1 
ATOM   4461  C CB    . HIS D 4 448  ? 166.261 128.342 118.803 1.00 85.74  ? 445  HIS A CB    1 
ATOM   4462  C CG    . HIS D 4 448  ? 166.185 129.220 117.592 1.00 85.36  ? 445  HIS A CG    1 
ATOM   4463  N ND1   . HIS D 4 448  ? 165.010 129.439 116.904 1.00 83.08  ? 445  HIS A ND1   1 
ATOM   4464  C CD2   . HIS D 4 448  ? 167.136 129.939 116.950 1.00 86.80  ? 445  HIS A CD2   1 
ATOM   4465  C CE1   . HIS D 4 448  ? 165.243 130.252 115.889 1.00 82.91  ? 445  HIS A CE1   1 
ATOM   4466  N NE2   . HIS D 4 448  ? 166.525 130.570 115.896 1.00 85.21  ? 445  HIS A NE2   1 
ATOM   4467  N N     . ALA D 4 449  ? 167.145 125.972 120.752 1.00 100.67 ? 446  ALA A N     1 
ATOM   4468  C CA    . ALA D 4 449  ? 167.456 125.451 122.078 1.00 107.66 ? 446  ALA A CA    1 
ATOM   4469  C C     . ALA D 4 449  ? 168.826 124.787 122.095 1.00 112.85 ? 446  ALA A C     1 
ATOM   4470  O O     . ALA D 4 449  ? 169.553 124.874 123.093 1.00 115.14 ? 446  ALA A O     1 
ATOM   4471  C CB    . ALA D 4 449  ? 166.373 124.471 122.527 1.00 102.88 ? 446  ALA A CB    1 
ATOM   4472  N N     . HIS D 4 450  ? 169.197 124.118 121.002 1.00 115.10 ? 447  HIS A N     1 
ATOM   4473  C CA    . HIS D 4 450  ? 170.529 123.530 120.910 1.00 118.19 ? 447  HIS A CA    1 
ATOM   4474  C C     . HIS D 4 450  ? 171.599 124.608 120.800 1.00 118.55 ? 447  HIS A C     1 
ATOM   4475  O O     . HIS D 4 450  ? 172.684 124.474 121.378 1.00 121.24 ? 447  HIS A O     1 
ATOM   4476  C CB    . HIS D 4 450  ? 170.597 122.573 119.719 1.00 121.14 ? 447  HIS A CB    1 
ATOM   4477  C CG    . HIS D 4 450  ? 171.983 122.339 119.206 1.00 128.20 ? 447  HIS A CG    1 
ATOM   4478  N ND1   . HIS D 4 450  ? 173.004 121.869 120.004 1.00 133.27 ? 447  HIS A ND1   1 
ATOM   4479  C CD2   . HIS D 4 450  ? 172.516 122.509 117.973 1.00 130.97 ? 447  HIS A CD2   1 
ATOM   4480  C CE1   . HIS D 4 450  ? 174.107 121.762 119.285 1.00 136.11 ? 447  HIS A CE1   1 
ATOM   4481  N NE2   . HIS D 4 450  ? 173.838 122.144 118.048 1.00 135.00 ? 447  HIS A NE2   1 
ATOM   4482  N N     . ALA D 4 451  ? 171.313 125.686 120.068 1.00 114.33 ? 448  ALA A N     1 
ATOM   4483  C CA    . ALA D 4 451  ? 172.258 126.789 119.939 1.00 111.04 ? 448  ALA A CA    1 
ATOM   4484  C C     . ALA D 4 451  ? 172.321 127.668 121.180 1.00 106.42 ? 448  ALA A C     1 
ATOM   4485  O O     . ALA D 4 451  ? 173.220 128.509 121.279 1.00 109.27 ? 448  ALA A O     1 
ATOM   4486  C CB    . ALA D 4 451  ? 171.906 127.651 118.724 1.00 106.97 ? 448  ALA A CB    1 
ATOM   4487  N N     . ALA D 4 452  ? 171.395 127.496 122.122 1.00 100.07 ? 449  ALA A N     1 
ATOM   4488  C CA    . ALA D 4 452  ? 171.395 128.275 123.353 1.00 97.80  ? 449  ALA A CA    1 
ATOM   4489  C C     . ALA D 4 452  ? 172.033 127.548 124.527 1.00 99.67  ? 449  ALA A C     1 
ATOM   4490  O O     . ALA D 4 452  ? 172.563 128.204 125.426 1.00 99.07  ? 449  ALA A O     1 
ATOM   4491  C CB    . ALA D 4 452  ? 169.964 128.675 123.732 1.00 95.05  ? 449  ALA A CB    1 
ATOM   4492  N N     . LEU D 4 453  ? 171.999 126.212 124.539 1.00 102.48 ? 450  LEU A N     1 
ATOM   4493  C CA    . LEU D 4 453  ? 172.593 125.473 125.648 1.00 105.44 ? 450  LEU A CA    1 
ATOM   4494  C C     . LEU D 4 453  ? 174.112 125.551 125.637 1.00 113.03 ? 450  LEU A C     1 
ATOM   4495  O O     . LEU D 4 453  ? 174.740 125.511 126.700 1.00 115.75 ? 450  LEU A O     1 
ATOM   4496  C CB    . LEU D 4 453  ? 172.141 124.012 125.616 1.00 102.11 ? 450  LEU A CB    1 
ATOM   4497  C CG    . LEU D 4 453  ? 170.765 123.713 126.210 1.00 96.49  ? 450  LEU A CG    1 
ATOM   4498  C CD1   . LEU D 4 453  ? 170.521 122.216 126.257 1.00 95.71  ? 450  LEU A CD1   1 
ATOM   4499  C CD2   . LEU D 4 453  ? 170.643 124.317 127.597 1.00 95.06  ? 450  LEU A CD2   1 
ATOM   4500  N N     . ASP D 4 454  ? 174.721 125.653 124.456 1.00 121.03 ? 451  ASP A N     1 
ATOM   4501  C CA    . ASP D 4 454  ? 176.170 125.772 124.366 1.00 126.47 ? 451  ASP A CA    1 
ATOM   4502  C C     . ASP D 4 454  ? 176.648 127.218 124.394 1.00 127.80 ? 451  ASP A C     1 
ATOM   4503  O O     . ASP D 4 454  ? 177.834 127.457 124.643 1.00 131.43 ? 451  ASP A O     1 
ATOM   4504  C CB    . ASP D 4 454  ? 176.680 125.083 123.096 1.00 128.65 ? 451  ASP A CB    1 
ATOM   4505  C CG    . ASP D 4 454  ? 175.976 125.566 121.845 1.00 129.79 ? 451  ASP A CG    1 
ATOM   4506  O OD1   . ASP D 4 454  ? 174.902 126.190 121.970 1.00 130.11 ? 451  ASP A OD1   1 
ATOM   4507  O OD2   . ASP D 4 454  ? 176.492 125.316 120.735 1.00 131.16 ? 451  ASP A OD2   1 
ATOM   4508  N N     . GLN D 4 455  ? 175.762 128.175 124.152 1.00 119.27 ? 452  GLN A N     1 
ATOM   4509  C CA    . GLN D 4 455  ? 176.128 129.585 124.237 1.00 117.23 ? 452  GLN A CA    1 
ATOM   4510  C C     . GLN D 4 455  ? 176.282 129.982 125.698 1.00 117.40 ? 452  GLN A C     1 
ATOM   4511  O O     . GLN D 4 455  ? 175.322 129.851 126.471 1.00 115.47 ? 452  GLN A O     1 
ATOM   4512  C CB    . GLN D 4 455  ? 175.071 130.449 123.558 1.00 113.66 ? 452  GLN A CB    1 
ATOM   4513  C CG    . GLN D 4 455  ? 175.418 131.929 123.497 1.00 114.16 ? 452  GLN A CG    1 
ATOM   4514  C CD    . GLN D 4 455  ? 174.245 132.786 123.058 1.00 111.69 ? 452  GLN A CD    1 
ATOM   4515  O OE1   . GLN D 4 455  ? 173.104 132.553 123.463 1.00 109.11 ? 452  GLN A OE1   1 
ATOM   4516  N NE2   . GLN D 4 455  ? 174.517 133.782 122.224 1.00 112.62 ? 452  GLN A NE2   1 
ATOM   4517  N N     . PRO D 4 456  ? 177.445 130.464 126.125 1.00 119.43 ? 453  PRO A N     1 
ATOM   4518  C CA    . PRO D 4 456  ? 177.640 130.782 127.541 1.00 120.27 ? 453  PRO A CA    1 
ATOM   4519  C C     . PRO D 4 456  ? 176.968 132.085 127.943 1.00 117.33 ? 453  PRO A C     1 
ATOM   4520  O O     . PRO D 4 456  ? 176.855 133.030 127.160 1.00 117.36 ? 453  PRO A O     1 
ATOM   4521  C CB    . PRO D 4 456  ? 179.164 130.889 127.666 1.00 123.73 ? 453  PRO A CB    1 
ATOM   4522  C CG    . PRO D 4 456  ? 179.603 131.342 126.315 1.00 123.50 ? 453  PRO A CG    1 
ATOM   4523  C CD    . PRO D 4 456  ? 178.669 130.684 125.332 1.00 120.99 ? 453  PRO A CD    1 
ATOM   4524  N N     . LEU D 4 457  ? 176.520 132.122 129.197 1.00 114.91 ? 454  LEU A N     1 
ATOM   4525  C CA    . LEU D 4 457  ? 175.929 133.325 129.753 1.00 113.11 ? 454  LEU A CA    1 
ATOM   4526  C C     . LEU D 4 457  ? 177.005 134.382 129.992 1.00 115.46 ? 454  LEU A C     1 
ATOM   4527  O O     . LEU D 4 457  ? 178.188 134.061 130.120 1.00 118.75 ? 454  LEU A O     1 
ATOM   4528  C CB    . LEU D 4 457  ? 175.203 133.009 131.061 1.00 114.30 ? 454  LEU A CB    1 
ATOM   4529  C CG    . LEU D 4 457  ? 173.765 132.498 130.974 1.00 113.38 ? 454  LEU A CG    1 
ATOM   4530  C CD1   . LEU D 4 457  ? 172.957 133.316 129.972 1.00 110.47 ? 454  LEU A CD1   1 
ATOM   4531  C CD2   . LEU D 4 457  ? 173.725 131.021 130.633 1.00 115.64 ? 454  LEU A CD2   1 
ATOM   4532  N N     . PRO D 4 458  ? 176.616 135.665 130.055 1.00 114.32 ? 455  PRO A N     1 
ATOM   4533  C CA    . PRO D 4 458  ? 177.604 136.714 130.336 1.00 116.61 ? 455  PRO A CA    1 
ATOM   4534  C C     . PRO D 4 458  ? 178.062 136.699 131.786 1.00 118.12 ? 455  PRO A C     1 
ATOM   4535  O O     . PRO D 4 458  ? 177.601 135.878 132.583 1.00 119.72 ? 455  PRO A O     1 
ATOM   4536  C CB    . PRO D 4 458  ? 176.849 138.003 129.997 1.00 112.98 ? 455  PRO A CB    1 
ATOM   4537  C CG    . PRO D 4 458  ? 175.423 137.662 130.242 1.00 108.76 ? 455  PRO A CG    1 
ATOM   4538  C CD    . PRO D 4 458  ? 175.274 136.227 129.818 1.00 109.94 ? 455  PRO A CD    1 
ATOM   4539  N N     . THR D 4 459  ? 178.968 137.611 132.138 1.00 118.19 ? 456  THR A N     1 
ATOM   4540  C CA    . THR D 4 459  ? 179.482 137.654 133.503 1.00 119.56 ? 456  THR A CA    1 
ATOM   4541  C C     . THR D 4 459  ? 178.540 138.407 134.436 1.00 117.71 ? 456  THR A C     1 
ATOM   4542  O O     . THR D 4 459  ? 178.357 138.004 135.591 1.00 117.84 ? 456  THR A O     1 
ATOM   4543  C CB    . THR D 4 459  ? 180.872 138.291 133.522 1.00 123.08 ? 456  THR A CB    1 
ATOM   4544  O OG1   . THR D 4 459  ? 180.811 139.596 132.933 1.00 122.90 ? 456  THR A OG1   1 
ATOM   4545  C CG2   . THR D 4 459  ? 181.860 137.432 132.743 1.00 125.17 ? 456  THR A CG2   1 
ATOM   4546  N N     . THR D 4 460  ? 177.935 139.495 133.962 1.00 116.18 ? 457  THR A N     1 
ATOM   4547  C CA    . THR D 4 460  ? 177.026 140.296 134.767 1.00 114.36 ? 457  THR A CA    1 
ATOM   4548  C C     . THR D 4 460  ? 175.831 140.714 133.920 1.00 111.03 ? 457  THR A C     1 
ATOM   4549  O O     . THR D 4 460  ? 175.806 140.532 132.701 1.00 108.59 ? 457  THR A O     1 
ATOM   4550  C CB    . THR D 4 460  ? 177.718 141.539 135.344 1.00 115.73 ? 457  THR A CB    1 
ATOM   4551  O OG1   . THR D 4 460  ? 178.432 142.220 134.304 1.00 117.12 ? 457  THR A OG1   1 
ATOM   4552  C CG2   . THR D 4 460  ? 178.683 141.157 136.459 1.00 119.14 ? 457  THR A CG2   1 
ATOM   4553  N N     . LEU D 4 461  ? 174.826 141.280 134.593 1.00 109.57 ? 458  LEU A N     1 
ATOM   4554  C CA    . LEU D 4 461  ? 173.653 141.851 133.945 1.00 104.67 ? 458  LEU A CA    1 
ATOM   4555  C C     . LEU D 4 461  ? 173.701 143.375 133.917 1.00 104.08 ? 458  LEU A C     1 
ATOM   4556  O O     . LEU D 4 461  ? 172.654 144.032 133.896 1.00 102.62 ? 458  LEU A O     1 
ATOM   4557  C CB    . LEU D 4 461  ? 172.378 141.375 134.642 1.00 100.50 ? 458  LEU A CB    1 
ATOM   4558  C CG    . LEU D 4 461  ? 171.617 140.188 134.048 1.00 97.36  ? 458  LEU A CG    1 
ATOM   4559  C CD1   . LEU D 4 461  ? 172.533 138.995 133.835 1.00 99.18  ? 458  LEU A CD1   1 
ATOM   4560  C CD2   . LEU D 4 461  ? 170.450 139.815 134.947 1.00 94.91  ? 458  LEU A CD2   1 
ATOM   4561  N N     . LYS D 4 462  ? 174.905 143.954 133.922 1.00 107.06 ? 459  LYS A N     1 
ATOM   4562  C CA    . LYS D 4 462  ? 175.035 145.405 133.982 1.00 106.37 ? 459  LYS A CA    1 
ATOM   4563  C C     . LYS D 4 462  ? 174.580 146.054 132.680 1.00 104.15 ? 459  LYS A C     1 
ATOM   4564  O O     . LYS D 4 462  ? 173.829 147.038 132.694 1.00 100.03 ? 459  LYS A O     1 
ATOM   4565  C CB    . LYS D 4 462  ? 176.480 145.787 134.302 1.00 110.59 ? 459  LYS A CB    1 
ATOM   4566  N N     . LYS D 4 463  ? 175.026 145.523 131.546 1.00 106.81 ? 460  LYS A N     1 
ATOM   4567  C CA    . LYS D 4 463  ? 174.677 146.082 130.249 1.00 106.37 ? 460  LYS A CA    1 
ATOM   4568  C C     . LYS D 4 463  ? 173.395 145.452 129.718 1.00 103.79 ? 460  LYS A C     1 
ATOM   4569  O O     . LYS D 4 463  ? 173.061 144.306 130.039 1.00 105.94 ? 460  LYS A O     1 
ATOM   4570  C CB    . LYS D 4 463  ? 175.812 145.872 129.247 1.00 107.92 ? 460  LYS A CB    1 
ATOM   4571  N N     . GLN D 4 464  ? 172.670 146.220 128.900 1.00 99.44  ? 461  GLN A N     1 
ATOM   4572  C CA    . GLN D 4 464  ? 171.453 145.702 128.284 1.00 94.74  ? 461  GLN A CA    1 
ATOM   4573  C C     . GLN D 4 464  ? 171.763 144.618 127.259 1.00 94.89  ? 461  GLN A C     1 
ATOM   4574  O O     . GLN D 4 464  ? 170.957 143.701 127.066 1.00 91.32  ? 461  GLN A O     1 
ATOM   4575  C CB    . GLN D 4 464  ? 170.665 146.839 127.633 1.00 94.02  ? 461  GLN A CB    1 
ATOM   4576  C CG    . GLN D 4 464  ? 169.317 146.422 127.062 1.00 93.35  ? 461  GLN A CG    1 
ATOM   4577  C CD    . GLN D 4 464  ? 168.318 146.036 128.137 1.00 93.30  ? 461  GLN A CD    1 
ATOM   4578  O OE1   . GLN D 4 464  ? 168.243 146.672 129.189 1.00 93.98  ? 461  GLN A OE1   1 
ATOM   4579  N NE2   . GLN D 4 464  ? 167.542 144.988 127.877 1.00 91.14  ? 461  GLN A NE2   1 
ATOM   4580  N N     . GLU D 4 465  ? 172.921 144.705 126.599 1.00 100.41 ? 462  GLU A N     1 
ATOM   4581  C CA    . GLU D 4 465  ? 173.318 143.659 125.661 1.00 99.85  ? 462  GLU A CA    1 
ATOM   4582  C C     . GLU D 4 465  ? 173.519 142.326 126.369 1.00 98.56  ? 462  GLU A C     1 
ATOM   4583  O O     . GLU D 4 465  ? 173.352 141.266 125.756 1.00 99.86  ? 462  GLU A O     1 
ATOM   4584  C CB    . GLU D 4 465  ? 174.594 144.069 124.926 1.00 99.10  ? 462  GLU A CB    1 
ATOM   4585  N N     . GLU D 4 466  ? 173.872 142.359 127.655 1.00 95.50  ? 463  GLU A N     1 
ATOM   4586  C CA    . GLU D 4 466  ? 173.991 141.134 128.435 1.00 98.40  ? 463  GLU A CA    1 
ATOM   4587  C C     . GLU D 4 466  ? 172.640 140.663 128.962 1.00 97.71  ? 463  GLU A C     1 
ATOM   4588  O O     . GLU D 4 466  ? 172.456 139.463 129.195 1.00 94.71  ? 463  GLU A O     1 
ATOM   4589  C CB    . GLU D 4 466  ? 174.975 141.340 129.589 1.00 103.30 ? 463  GLU A CB    1 
ATOM   4590  C CG    . GLU D 4 466  ? 176.414 141.552 129.136 1.00 108.98 ? 463  GLU A CG    1 
ATOM   4591  C CD    . GLU D 4 466  ? 177.338 141.945 130.274 1.00 112.74 ? 463  GLU A CD    1 
ATOM   4592  O OE1   . GLU D 4 466  ? 176.895 142.691 131.171 1.00 111.64 ? 463  GLU A OE1   1 
ATOM   4593  O OE2   . GLU D 4 466  ? 178.508 141.506 130.269 1.00 115.84 ? 463  GLU A OE2   1 
ATOM   4594  N N     . LYS D 4 467  ? 171.693 141.583 129.161 1.00 100.66 ? 464  LYS A N     1 
ATOM   4595  C CA    . LYS D 4 467  ? 170.335 141.177 129.507 1.00 99.79  ? 464  LYS A CA    1 
ATOM   4596  C C     . LYS D 4 467  ? 169.634 140.523 128.325 1.00 99.19  ? 464  LYS A C     1 
ATOM   4597  O O     . LYS D 4 467  ? 168.803 139.629 128.515 1.00 96.31  ? 464  LYS A O     1 
ATOM   4598  C CB    . LYS D 4 467  ? 169.523 142.380 129.990 1.00 96.47  ? 464  LYS A CB    1 
ATOM   4599  C CG    . LYS D 4 467  ? 169.996 142.993 131.297 1.00 96.26  ? 464  LYS A CG    1 
ATOM   4600  C CD    . LYS D 4 467  ? 169.052 144.102 131.745 1.00 92.50  ? 464  LYS A CD    1 
ATOM   4601  C CE    . LYS D 4 467  ? 169.506 144.735 133.050 1.00 93.21  ? 464  LYS A CE    1 
ATOM   4602  N NZ    . LYS D 4 467  ? 168.559 145.788 133.511 1.00 91.33  ? 464  LYS A NZ    1 
ATOM   4603  N N     . GLU D 4 468  ? 169.959 140.952 127.103 1.00 104.32 ? 465  GLU A N     1 
ATOM   4604  C CA    . GLU D 4 468  ? 169.267 140.438 125.925 1.00 104.58 ? 465  GLU A CA    1 
ATOM   4605  C C     . GLU D 4 468  ? 169.594 138.972 125.679 1.00 102.27 ? 465  GLU A C     1 
ATOM   4606  O O     . GLU D 4 468  ? 168.703 138.181 125.346 1.00 100.21 ? 465  GLU A O     1 
ATOM   4607  C CB    . GLU D 4 468  ? 169.629 141.281 124.703 1.00 109.72 ? 465  GLU A CB    1 
ATOM   4608  C CG    . GLU D 4 468  ? 168.892 140.886 123.437 1.00 112.31 ? 465  GLU A CG    1 
ATOM   4609  C CD    . GLU D 4 468  ? 169.348 141.685 122.232 1.00 116.62 ? 465  GLU A CD    1 
ATOM   4610  O OE1   . GLU D 4 468  ? 170.429 142.306 122.305 1.00 119.43 ? 465  GLU A OE1   1 
ATOM   4611  O OE2   . GLU D 4 468  ? 168.623 141.693 121.216 1.00 116.64 ? 465  GLU A OE2   1 
ATOM   4612  N N     . ILE D 4 469  ? 170.863 138.588 125.836 1.00 100.52 ? 466  ILE A N     1 
ATOM   4613  C CA    . ILE D 4 469  ? 171.243 137.204 125.572 1.00 98.57  ? 466  ILE A CA    1 
ATOM   4614  C C     . ILE D 4 469  ? 170.680 136.271 126.638 1.00 93.64  ? 466  ILE A C     1 
ATOM   4615  O O     . ILE D 4 469  ? 170.415 135.094 126.361 1.00 92.53  ? 466  ILE A O     1 
ATOM   4616  C CB    . ILE D 4 469  ? 172.774 137.075 125.456 1.00 103.21 ? 466  ILE A CB    1 
ATOM   4617  C CG1   . ILE D 4 469  ? 173.466 137.708 126.665 1.00 105.63 ? 466  ILE A CG1   1 
ATOM   4618  C CG2   . ILE D 4 469  ? 173.264 137.713 124.164 1.00 104.37 ? 466  ILE A CG2   1 
ATOM   4619  C CD1   . ILE D 4 469  ? 174.974 137.734 126.553 1.00 109.15 ? 466  ILE A CD1   1 
ATOM   4620  N N     . LEU D 4 470  ? 170.482 136.768 127.861 1.00 89.71  ? 467  LEU A N     1 
ATOM   4621  C CA    . LEU D 4 470  ? 169.814 135.956 128.874 1.00 86.53  ? 467  LEU A CA    1 
ATOM   4622  C C     . LEU D 4 470  ? 168.355 135.715 128.504 1.00 79.99  ? 467  LEU A C     1 
ATOM   4623  O O     . LEU D 4 470  ? 167.846 134.599 128.658 1.00 78.87  ? 467  LEU A O     1 
ATOM   4624  C CB    . LEU D 4 470  ? 169.918 136.625 130.245 1.00 87.22  ? 467  LEU A CB    1 
ATOM   4625  C CG    . LEU D 4 470  ? 169.147 135.936 131.378 1.00 86.75  ? 467  LEU A CG    1 
ATOM   4626  C CD1   . LEU D 4 470  ? 169.642 134.512 131.582 1.00 65.94  ? 467  LEU A CD1   1 
ATOM   4627  C CD2   . LEU D 4 470  ? 169.242 136.732 132.671 1.00 64.76  ? 467  LEU A CD2   1 
ATOM   4628  N N     . LYS D 4 471  ? 167.671 136.750 128.010 1.00 74.89  ? 468  LYS A N     1 
ATOM   4629  C CA    . LYS D 4 471  ? 166.294 136.574 127.559 1.00 70.96  ? 468  LYS A CA    1 
ATOM   4630  C C     . LYS D 4 471  ? 166.233 135.698 126.314 1.00 67.59  ? 468  LYS A C     1 
ATOM   4631  O O     . LYS D 4 471  ? 165.315 134.881 126.167 1.00 65.01  ? 468  LYS A O     1 
ATOM   4632  C CB    . LYS D 4 471  ? 165.650 137.932 127.285 1.00 73.91  ? 468  LYS A CB    1 
ATOM   4633  C CG    . LYS D 4 471  ? 164.209 137.843 126.803 1.00 75.39  ? 468  LYS A CG    1 
ATOM   4634  C CD    . LYS D 4 471  ? 163.811 139.068 125.994 1.00 75.19  ? 468  LYS A CD    1 
ATOM   4635  C CE    . LYS D 4 471  ? 162.483 138.845 125.288 1.00 72.68  ? 468  LYS A CE    1 
ATOM   4636  N NZ    . LYS D 4 471  ? 162.199 139.902 124.278 1.00 71.46  ? 468  LYS A NZ    1 
ATOM   4637  N N     . SER D 4 472  ? 167.205 135.847 125.410 1.00 68.41  ? 469  SER A N     1 
ATOM   4638  C CA    . SER D 4 472  ? 167.199 135.071 124.173 1.00 67.77  ? 469  SER A CA    1 
ATOM   4639  C C     . SER D 4 472  ? 167.314 133.580 124.453 1.00 66.87  ? 469  SER A C     1 
ATOM   4640  O O     . SER D 4 472  ? 166.628 132.767 123.822 1.00 66.10  ? 469  SER A O     1 
ATOM   4641  C CB    . SER D 4 472  ? 168.333 135.535 123.260 1.00 69.74  ? 469  SER A CB    1 
ATOM   4642  O OG    . SER D 4 472  ? 168.370 134.779 122.063 1.00 69.95  ? 469  SER A OG    1 
ATOM   4643  N N     . GLN D 4 473  ? 168.179 133.198 125.396 1.00 68.20  ? 470  GLN A N     1 
ATOM   4644  C CA    . GLN D 4 473  ? 168.315 131.786 125.737 1.00 70.57  ? 470  GLN A CA    1 
ATOM   4645  C C     . GLN D 4 473  ? 167.090 131.269 126.482 1.00 72.83  ? 470  GLN A C     1 
ATOM   4646  O O     . GLN D 4 473  ? 166.715 130.102 126.318 1.00 72.14  ? 470  GLN A O     1 
ATOM   4647  C CB    . GLN D 4 473  ? 169.577 131.565 126.569 1.00 74.11  ? 470  GLN A CB    1 
ATOM   4648  C CG    . GLN D 4 473  ? 170.860 131.940 125.846 1.00 76.56  ? 470  GLN A CG    1 
ATOM   4649  C CD    . GLN D 4 473  ? 172.088 131.780 126.720 1.00 77.40  ? 470  GLN A CD    1 
ATOM   4650  O OE1   . GLN D 4 473  ? 172.060 131.072 127.724 1.00 75.67  ? 470  GLN A OE1   1 
ATOM   4651  N NE2   . GLN D 4 473  ? 173.173 132.445 126.341 1.00 79.94  ? 470  GLN A NE2   1 
ATOM   4652  N N     . LEU D 4 474  ? 166.457 132.114 127.298 1.00 75.55  ? 471  LEU A N     1 
ATOM   4653  C CA    . LEU D 4 474  ? 165.229 131.706 127.972 1.00 77.12  ? 471  LEU A CA    1 
ATOM   4654  C C     . LEU D 4 474  ? 164.074 131.555 126.993 1.00 71.75  ? 471  LEU A C     1 
ATOM   4655  O O     . LEU D 4 474  ? 163.211 130.691 127.184 1.00 71.07  ? 471  LEU A O     1 
ATOM   4656  C CB    . LEU D 4 474  ? 164.871 132.710 129.069 1.00 80.44  ? 471  LEU A CB    1 
ATOM   4657  C CG    . LEU D 4 474  ? 165.728 132.662 130.334 1.00 58.88  ? 471  LEU A CG    1 
ATOM   4658  C CD1   . LEU D 4 474  ? 165.396 133.827 131.246 1.00 60.52  ? 471  LEU A CD1   1 
ATOM   4659  C CD2   . LEU D 4 474  ? 165.522 131.343 131.059 1.00 59.54  ? 471  LEU A CD2   1 
ATOM   4660  N N     . ASP D 4 475  ? 164.036 132.383 125.945 1.00 68.64  ? 472  ASP A N     1 
ATOM   4661  C CA    . ASP D 4 475  ? 163.006 132.229 124.922 1.00 66.28  ? 472  ASP A CA    1 
ATOM   4662  C C     . ASP D 4 475  ? 163.154 130.902 124.190 1.00 66.04  ? 472  ASP A C     1 
ATOM   4663  O O     . ASP D 4 475  ? 162.158 130.247 123.863 1.00 64.97  ? 472  ASP A O     1 
ATOM   4664  C CB    . ASP D 4 475  ? 163.063 133.395 123.933 1.00 68.60  ? 472  ASP A CB    1 
ATOM   4665  C CG    . ASP D 4 475  ? 162.737 134.728 124.579 1.00 73.49  ? 472  ASP A CG    1 
ATOM   4666  O OD1   . ASP D 4 475  ? 161.986 134.745 125.577 1.00 74.30  ? 472  ASP A OD1   1 
ATOM   4667  O OD2   . ASP D 4 475  ? 163.234 135.765 124.087 1.00 76.76  ? 472  ASP A OD2   1 
ATOM   4668  N N     . SER D 4 476  ? 164.397 130.488 123.927 1.00 67.57  ? 473  SER A N     1 
ATOM   4669  C CA    . SER D 4 476  ? 164.625 129.197 123.285 1.00 67.93  ? 473  SER A CA    1 
ATOM   4670  C C     . SER D 4 476  ? 164.235 128.049 124.206 1.00 66.79  ? 473  SER A C     1 
ATOM   4671  O O     . SER D 4 476  ? 163.691 127.037 123.751 1.00 65.37  ? 473  SER A O     1 
ATOM   4672  C CB    . SER D 4 476  ? 166.086 129.077 122.859 1.00 68.89  ? 473  SER A CB    1 
ATOM   4673  O OG    . SER D 4 476  ? 166.469 130.172 122.044 1.00 68.08  ? 473  SER A OG    1 
ATOM   4674  N N     . LEU D 4 477  ? 164.506 128.188 125.506 1.00 67.29  ? 474  LEU A N     1 
ATOM   4675  C CA    . LEU D 4 477  ? 164.109 127.159 126.460 1.00 68.69  ? 474  LEU A CA    1 
ATOM   4676  C C     . LEU D 4 477  ? 162.594 127.109 126.619 1.00 65.97  ? 474  LEU A C     1 
ATOM   4677  O O     . LEU D 4 477  ? 162.009 126.022 126.700 1.00 66.56  ? 474  LEU A O     1 
ATOM   4678  C CB    . LEU D 4 477  ? 164.780 127.401 127.811 1.00 73.32  ? 474  LEU A CB    1 
ATOM   4679  C CG    . LEU D 4 477  ? 166.075 126.632 128.081 1.00 77.31  ? 474  LEU A CG    1 
ATOM   4680  C CD1   . LEU D 4 477  ? 165.797 125.139 128.116 1.00 79.38  ? 474  LEU A CD1   1 
ATOM   4681  C CD2   . LEU D 4 477  ? 167.133 126.952 127.037 1.00 77.75  ? 474  LEU A CD2   1 
ATOM   4682  N N     . LEU D 4 478  ? 161.941 128.274 126.670 1.00 64.71  ? 475  LEU A N     1 
ATOM   4683  C CA    . LEU D 4 478  ? 160.487 128.293 126.757 1.00 62.41  ? 475  LEU A CA    1 
ATOM   4684  C C     . LEU D 4 478  ? 159.847 127.847 125.448 1.00 62.51  ? 475  LEU A C     1 
ATOM   4685  O O     . LEU D 4 478  ? 158.736 127.304 125.456 1.00 62.11  ? 475  LEU A O     1 
ATOM   4686  C CB    . LEU D 4 478  ? 159.999 129.691 127.142 1.00 59.61  ? 475  LEU A CB    1 
ATOM   4687  C CG    . LEU D 4 478  ? 158.532 129.800 127.570 1.00 56.12  ? 475  LEU A CG    1 
ATOM   4688  C CD1   . LEU D 4 478  ? 158.284 128.987 128.830 1.00 57.41  ? 475  LEU A CD1   1 
ATOM   4689  C CD2   . LEU D 4 478  ? 158.127 131.251 127.774 1.00 53.35  ? 475  LEU A CD2   1 
ATOM   4690  N N     . GLY D 4 479  ? 160.526 128.068 124.320 1.00 62.12  ? 476  GLY A N     1 
ATOM   4691  C CA    . GLY D 4 479  ? 160.001 127.600 123.049 1.00 61.59  ? 476  GLY A CA    1 
ATOM   4692  C C     . GLY D 4 479  ? 159.938 126.088 122.971 1.00 64.11  ? 476  GLY A C     1 
ATOM   4693  O O     . GLY D 4 479  ? 158.959 125.520 122.484 1.00 64.88  ? 476  GLY A O     1 
ATOM   4694  N N     . LEU D 4 480  ? 160.986 125.414 123.450 1.00 66.05  ? 477  LEU A N     1 
ATOM   4695  C CA    . LEU D 4 480  ? 160.956 123.956 123.513 1.00 65.05  ? 477  LEU A CA    1 
ATOM   4696  C C     . LEU D 4 480  ? 159.943 123.472 124.540 1.00 64.78  ? 477  LEU A C     1 
ATOM   4697  O O     . LEU D 4 480  ? 159.261 122.464 124.321 1.00 64.93  ? 477  LEU A O     1 
ATOM   4698  C CB    . LEU D 4 480  ? 162.351 123.418 123.832 1.00 64.07  ? 477  LEU A CB    1 
ATOM   4699  C CG    . LEU D 4 480  ? 162.467 121.903 123.994 1.00 63.64  ? 477  LEU A CG    1 
ATOM   4700  C CD1   . LEU D 4 480  ? 161.999 121.190 122.735 1.00 63.27  ? 477  LEU A CD1   1 
ATOM   4701  C CD2   . LEU D 4 480  ? 163.896 121.519 124.333 1.00 66.18  ? 477  LEU A CD2   1 
ATOM   4702  N N     . TYR D 4 481  ? 159.829 124.180 125.668 1.00 65.27  ? 478  TYR A N     1 
ATOM   4703  C CA    . TYR D 4 481  ? 158.821 123.831 126.665 1.00 66.19  ? 478  TYR A CA    1 
ATOM   4704  C C     . TYR D 4 481  ? 157.415 124.015 126.108 1.00 62.10  ? 478  TYR A C     1 
ATOM   4705  O O     . TYR D 4 481  ? 156.510 123.231 126.417 1.00 60.52  ? 478  TYR A O     1 
ATOM   4706  C CB    . TYR D 4 481  ? 159.019 124.674 127.926 1.00 72.60  ? 478  TYR A CB    1 
ATOM   4707  C CG    . TYR D 4 481  ? 157.914 124.526 128.951 1.00 79.32  ? 478  TYR A CG    1 
ATOM   4708  C CD1   . TYR D 4 481  ? 157.885 123.443 129.817 1.00 83.61  ? 478  TYR A CD1   1 
ATOM   4709  C CD2   . TYR D 4 481  ? 156.907 125.478 129.056 1.00 81.64  ? 478  TYR A CD2   1 
ATOM   4710  C CE1   . TYR D 4 481  ? 156.879 123.306 130.756 1.00 85.19  ? 478  TYR A CE1   1 
ATOM   4711  C CE2   . TYR D 4 481  ? 155.897 125.349 129.991 1.00 82.85  ? 478  TYR A CE2   1 
ATOM   4712  C CZ    . TYR D 4 481  ? 155.888 124.263 130.838 1.00 84.32  ? 478  TYR A CZ    1 
ATOM   4713  O OH    . TYR D 4 481  ? 154.884 124.132 131.772 1.00 84.24  ? 478  TYR A OH    1 
ATOM   4714  N N     . HIS D 4 482  ? 157.215 125.048 125.286 1.00 59.93  ? 479  HIS A N     1 
ATOM   4715  C CA    . HIS D 4 482  ? 155.923 125.236 124.634 1.00 57.10  ? 479  HIS A CA    1 
ATOM   4716  C C     . HIS D 4 482  ? 155.635 124.119 123.642 1.00 57.22  ? 479  HIS A C     1 
ATOM   4717  O O     . HIS D 4 482  ? 154.492 123.666 123.520 1.00 57.45  ? 479  HIS A O     1 
ATOM   4718  C CB    . HIS D 4 482  ? 155.881 126.592 123.932 1.00 54.21  ? 479  HIS A CB    1 
ATOM   4719  C CG    . HIS D 4 482  ? 155.624 127.742 124.852 1.00 54.70  ? 479  HIS A CG    1 
ATOM   4720  N ND1   . HIS D 4 482  ? 154.951 127.606 126.047 1.00 55.09  ? 479  HIS A ND1   1 
ATOM   4721  C CD2   . HIS D 4 482  ? 155.957 129.050 124.754 1.00 54.58  ? 479  HIS A CD2   1 
ATOM   4722  C CE1   . HIS D 4 482  ? 154.877 128.781 126.644 1.00 55.29  ? 479  HIS A CE1   1 
ATOM   4723  N NE2   . HIS D 4 482  ? 155.480 129.675 125.881 1.00 54.99  ? 479  HIS A NE2   1 
ATOM   4724  N N     . LEU D 4 483  ? 156.664 123.665 122.924 1.00 58.11  ? 480  LEU A N     1 
ATOM   4725  C CA    . LEU D 4 483  ? 156.463 122.639 121.906 1.00 57.89  ? 480  LEU A CA    1 
ATOM   4726  C C     . LEU D 4 483  ? 156.023 121.319 122.525 1.00 59.17  ? 480  LEU A C     1 
ATOM   4727  O O     . LEU D 4 483  ? 155.165 120.621 121.971 1.00 59.88  ? 480  LEU A O     1 
ATOM   4728  C CB    . LEU D 4 483  ? 157.745 122.455 121.095 1.00 57.68  ? 480  LEU A CB    1 
ATOM   4729  C CG    . LEU D 4 483  ? 157.741 121.365 120.021 1.00 55.56  ? 480  LEU A CG    1 
ATOM   4730  C CD1   . LEU D 4 483  ? 156.641 121.616 119.006 1.00 54.20  ? 480  LEU A CD1   1 
ATOM   4731  C CD2   . LEU D 4 483  ? 159.094 121.284 119.338 1.00 55.50  ? 480  LEU A CD2   1 
ATOM   4732  N N     . LEU D 4 484  ? 156.590 120.962 123.680 1.00 60.00  ? 481  LEU A N     1 
ATOM   4733  C CA    . LEU D 4 484  ? 156.274 119.673 124.289 1.00 60.84  ? 481  LEU A CA    1 
ATOM   4734  C C     . LEU D 4 484  ? 154.842 119.624 124.807 1.00 61.91  ? 481  LEU A C     1 
ATOM   4735  O O     . LEU D 4 484  ? 154.244 118.544 124.861 1.00 65.30  ? 481  LEU A O     1 
ATOM   4736  C CB    . LEU D 4 484  ? 157.260 119.368 125.416 1.00 61.05  ? 481  LEU A CB    1 
ATOM   4737  C CG    . LEU D 4 484  ? 158.724 119.213 124.999 1.00 62.36  ? 481  LEU A CG    1 
ATOM   4738  C CD1   . LEU D 4 484  ? 159.588 118.839 126.194 1.00 65.84  ? 481  LEU A CD1   1 
ATOM   4739  C CD2   . LEU D 4 484  ? 158.866 118.185 123.885 1.00 59.89  ? 481  LEU A CD2   1 
ATOM   4740  N N     . ASP D 4 485  ? 154.277 120.768 125.185 1.00 59.93  ? 482  ASP A N     1 
ATOM   4741  C CA    . ASP D 4 485  ? 152.901 120.824 125.669 1.00 59.54  ? 482  ASP A CA    1 
ATOM   4742  C C     . ASP D 4 485  ? 151.872 120.706 124.550 1.00 59.21  ? 482  ASP A C     1 
ATOM   4743  O O     . ASP D 4 485  ? 150.672 120.838 124.817 1.00 56.86  ? 482  ASP A O     1 
ATOM   4744  C CB    . ASP D 4 485  ? 152.671 122.114 126.456 1.00 60.17  ? 482  ASP A CB    1 
ATOM   4745  C CG    . ASP D 4 485  ? 153.052 121.979 127.918 1.00 64.91  ? 482  ASP A CG    1 
ATOM   4746  O OD1   . ASP D 4 485  ? 153.974 121.194 128.224 1.00 68.43  ? 482  ASP A OD1   1 
ATOM   4747  O OD2   . ASP D 4 485  ? 152.426 122.652 128.763 1.00 66.76  ? 482  ASP A OD2   1 
ATOM   4748  N N     . TRP D 4 486  ? 152.309 120.465 123.312 1.00 59.22  ? 483  TRP A N     1 
ATOM   4749  C CA    . TRP D 4 486  ? 151.365 120.239 122.222 1.00 56.64  ? 483  TRP A CA    1 
ATOM   4750  C C     . TRP D 4 486  ? 150.664 118.894 122.352 1.00 58.54  ? 483  TRP A C     1 
ATOM   4751  O O     . TRP D 4 486  ? 149.532 118.739 121.882 1.00 58.97  ? 483  TRP A O     1 
ATOM   4752  C CB    . TRP D 4 486  ? 152.083 120.322 120.877 1.00 55.98  ? 483  TRP A CB    1 
ATOM   4753  C CG    . TRP D 4 486  ? 152.457 121.709 120.454 1.00 56.90  ? 483  TRP A CG    1 
ATOM   4754  C CD1   . TRP D 4 486  ? 152.376 122.847 121.202 1.00 56.59  ? 483  TRP A CD1   1 
ATOM   4755  C CD2   . TRP D 4 486  ? 152.960 122.105 119.173 1.00 55.97  ? 483  TRP A CD2   1 
ATOM   4756  N NE1   . TRP D 4 486  ? 152.804 123.928 120.469 1.00 54.32  ? 483  TRP A NE1   1 
ATOM   4757  C CE2   . TRP D 4 486  ? 153.168 123.498 119.217 1.00 54.76  ? 483  TRP A CE2   1 
ATOM   4758  C CE3   . TRP D 4 486  ? 153.256 121.416 117.992 1.00 55.78  ? 483  TRP A CE3   1 
ATOM   4759  C CZ2   . TRP D 4 486  ? 153.657 124.216 118.128 1.00 55.30  ? 483  TRP A CZ2   1 
ATOM   4760  C CZ3   . TRP D 4 486  ? 153.743 122.130 116.912 1.00 56.83  ? 483  TRP A CZ3   1 
ATOM   4761  C CH2   . TRP D 4 486  ? 153.939 123.514 116.988 1.00 56.14  ? 483  TRP A CH2   1 
ATOM   4762  N N     . PHE D 4 487  ? 151.313 117.918 122.980 1.00 61.90  ? 484  PHE A N     1 
ATOM   4763  C CA    . PHE D 4 487  ? 150.801 116.557 123.027 1.00 66.86  ? 484  PHE A CA    1 
ATOM   4764  C C     . PHE D 4 487  ? 149.911 116.350 124.245 1.00 74.18  ? 484  PHE A C     1 
ATOM   4765  O O     . PHE D 4 487  ? 150.178 116.889 125.324 1.00 71.55  ? 484  PHE A O     1 
ATOM   4766  C CB    . PHE D 4 487  ? 151.957 115.555 123.043 1.00 67.09  ? 484  PHE A CB    1 
ATOM   4767  C CG    . PHE D 4 487  ? 152.903 115.709 121.886 1.00 65.91  ? 484  PHE A CG    1 
ATOM   4768  C CD1   . PHE D 4 487  ? 152.580 115.205 120.638 1.00 62.18  ? 484  PHE A CD1   1 
ATOM   4769  C CD2   . PHE D 4 487  ? 154.116 116.360 122.049 1.00 67.70  ? 484  PHE A CD2   1 
ATOM   4770  C CE1   . PHE D 4 487  ? 153.449 115.346 119.572 1.00 61.39  ? 484  PHE A CE1   1 
ATOM   4771  C CE2   . PHE D 4 487  ? 154.989 116.503 120.985 1.00 67.20  ? 484  PHE A CE2   1 
ATOM   4772  C CZ    . PHE D 4 487  ? 154.654 115.995 119.745 1.00 63.97  ? 484  PHE A CZ    1 
ATOM   4773  N N     . ALA D 4 488  ? 148.855 115.562 124.063 1.00 83.31  ? 485  ALA A N     1 
ATOM   4774  C CA    . ALA D 4 488  ? 147.922 115.286 125.145 1.00 90.72  ? 485  ALA A CA    1 
ATOM   4775  C C     . ALA D 4 488  ? 148.593 114.468 126.242 1.00 96.80  ? 485  ALA A C     1 
ATOM   4776  O O     . ALA D 4 488  ? 149.347 113.530 125.969 1.00 95.35  ? 485  ALA A O     1 
ATOM   4777  C CB    . ALA D 4 488  ? 146.695 114.545 124.613 1.00 89.57  ? 485  ALA A CB    1 
ATOM   4778  N N     . VAL D 4 489  ? 148.304 114.826 127.491 1.00 105.19 ? 486  VAL A N     1 
ATOM   4779  C CA    . VAL D 4 489  ? 148.946 114.203 128.643 1.00 109.76 ? 486  VAL A CA    1 
ATOM   4780  C C     . VAL D 4 489  ? 147.984 113.221 129.301 1.00 109.59 ? 486  VAL A C     1 
ATOM   4781  O O     . VAL D 4 489  ? 148.412 112.240 129.923 1.00 111.37 ? 486  VAL A O     1 
ATOM   4782  C CB    . VAL D 4 489  ? 149.420 115.269 129.649 1.00 112.13 ? 486  VAL A CB    1 
ATOM   4783  C CG1   . VAL D 4 489  ? 150.339 114.654 130.695 1.00 115.35 ? 486  VAL A CG1   1 
ATOM   4784  C CG2   . VAL D 4 489  ? 150.114 116.410 128.921 1.00 111.13 ? 486  VAL A CG2   1 
ATOM   4785  N N     . ASP D 4 490  ? 146.684 113.473 129.165 1.00 105.19 ? 487  ASP A N     1 
ATOM   4786  C CA    . ASP D 4 490  ? 145.686 112.634 129.816 1.00 105.27 ? 487  ASP A CA    1 
ATOM   4787  C C     . ASP D 4 490  ? 145.752 111.206 129.289 1.00 105.98 ? 487  ASP A C     1 
ATOM   4788  O O     . ASP D 4 490  ? 145.972 110.973 128.097 1.00 106.07 ? 487  ASP A O     1 
ATOM   4789  C CB    . ASP D 4 490  ? 144.286 113.211 129.600 1.00 103.54 ? 487  ASP A CB    1 
ATOM   4790  N N     . GLU D 4 491  ? 145.562 110.246 130.192 1.00 105.09 ? 488  GLU A N     1 
ATOM   4791  C CA    . GLU D 4 491  ? 145.578 108.831 129.846 1.00 101.99 ? 488  GLU A CA    1 
ATOM   4792  C C     . GLU D 4 491  ? 144.272 108.360 129.215 1.00 97.73  ? 488  GLU A C     1 
ATOM   4793  O O     . GLU D 4 491  ? 144.089 107.152 129.031 1.00 97.66  ? 488  GLU A O     1 
ATOM   4794  C CB    . GLU D 4 491  ? 145.887 107.989 131.086 1.00 102.24 ? 488  GLU A CB    1 
ATOM   4795  N N     . SER D 4 492  ? 143.365 109.282 128.890 1.00 93.83  ? 489  SER A N     1 
ATOM   4796  C CA    . SER D 4 492  ? 142.114 108.898 128.243 1.00 90.65  ? 489  SER A CA    1 
ATOM   4797  C C     . SER D 4 492  ? 142.346 108.406 126.819 1.00 89.67  ? 489  SER A C     1 
ATOM   4798  O O     . SER D 4 492  ? 141.541 107.624 126.298 1.00 90.05  ? 489  SER A O     1 
ATOM   4799  C CB    . SER D 4 492  ? 141.139 110.074 128.251 1.00 87.23  ? 489  SER A CB    1 
ATOM   4800  O OG    . SER D 4 492  ? 141.740 111.241 127.715 1.00 83.94  ? 489  SER A OG    1 
ATOM   4801  N N     . ASN D 4 493  ? 143.428 108.839 126.181 1.00 88.83  ? 490  ASN A N     1 
ATOM   4802  C CA    . ASN D 4 493  ? 143.754 108.421 124.827 1.00 87.07  ? 490  ASN A CA    1 
ATOM   4803  C C     . ASN D 4 493  ? 144.707 107.229 124.851 1.00 89.27  ? 490  ASN A C     1 
ATOM   4804  O O     . ASN D 4 493  ? 145.402 106.975 125.838 1.00 88.67  ? 490  ASN A O     1 
ATOM   4805  C CB    . ASN D 4 493  ? 144.383 109.573 124.042 1.00 84.17  ? 490  ASN A CB    1 
ATOM   4806  C CG    . ASN D 4 493  ? 143.683 110.897 124.283 1.00 81.82  ? 490  ASN A CG    1 
ATOM   4807  O OD1   . ASN D 4 493  ? 142.656 111.191 123.670 1.00 80.56  ? 490  ASN A OD1   1 
ATOM   4808  N ND2   . ASN D 4 493  ? 144.242 111.711 125.173 1.00 81.05  ? 490  ASN A ND2   1 
ATOM   4809  N N     . GLU D 4 494  ? 144.733 106.495 123.738 1.00 91.56  ? 491  GLU A N     1 
ATOM   4810  C CA    . GLU D 4 494  ? 145.631 105.351 123.580 1.00 92.54  ? 491  GLU A CA    1 
ATOM   4811  C C     . GLU D 4 494  ? 147.015 105.875 123.208 1.00 94.62  ? 491  GLU A C     1 
ATOM   4812  O O     . GLU D 4 494  ? 147.401 105.949 122.039 1.00 92.87  ? 491  GLU A O     1 
ATOM   4813  C CB    . GLU D 4 494  ? 145.100 104.382 122.534 1.00 88.15  ? 491  GLU A CB    1 
ATOM   4814  C CG    . GLU D 4 494  ? 143.923 103.547 123.004 1.00 85.16  ? 491  GLU A CG    1 
ATOM   4815  C CD    . GLU D 4 494  ? 143.532 102.478 122.002 1.00 83.10  ? 491  GLU A CD    1 
ATOM   4816  O OE1   . GLU D 4 494  ? 143.444 102.799 120.799 1.00 81.29  ? 491  GLU A OE1   1 
ATOM   4817  O OE2   . GLU D 4 494  ? 143.319 101.319 122.415 1.00 84.13  ? 491  GLU A OE2   1 
ATOM   4818  N N     . VAL D 4 495  ? 147.778 106.243 124.237 1.00 100.90 ? 492  VAL A N     1 
ATOM   4819  C CA    . VAL D 4 495  ? 149.109 106.803 124.044 1.00 99.65  ? 492  VAL A CA    1 
ATOM   4820  C C     . VAL D 4 495  ? 150.106 105.683 123.782 1.00 98.55  ? 492  VAL A C     1 
ATOM   4821  O O     . VAL D 4 495  ? 149.936 104.542 124.231 1.00 98.98  ? 492  VAL A O     1 
ATOM   4822  C CB    . VAL D 4 495  ? 149.523 107.651 125.265 1.00 101.24 ? 492  VAL A CB    1 
ATOM   4823  C CG1   . VAL D 4 495  ? 148.641 108.886 125.370 1.00 99.94  ? 492  VAL A CG1   1 
ATOM   4824  C CG2   . VAL D 4 495  ? 149.441 106.820 126.538 1.00 104.30 ? 492  VAL A CG2   1 
ATOM   4825  N N     . ASP D 4 496  ? 151.157 106.013 123.040 1.00 97.18  ? 493  ASP A N     1 
ATOM   4826  C CA    . ASP D 4 496  ? 152.198 105.045 122.738 1.00 96.99  ? 493  ASP A CA    1 
ATOM   4827  C C     . ASP D 4 496  ? 152.941 104.664 124.017 1.00 98.87  ? 493  ASP A C     1 
ATOM   4828  O O     . ASP D 4 496  ? 153.158 105.513 124.885 1.00 100.36 ? 493  ASP A O     1 
ATOM   4829  C CB    . ASP D 4 496  ? 153.172 105.622 121.712 1.00 94.48  ? 493  ASP A CB    1 
ATOM   4830  C CG    . ASP D 4 496  ? 154.164 104.598 121.201 1.00 95.54  ? 493  ASP A CG    1 
ATOM   4831  O OD1   . ASP D 4 496  ? 153.856 103.924 120.197 1.00 94.90  ? 493  ASP A OD1   1 
ATOM   4832  O OD2   . ASP D 4 496  ? 155.253 104.471 121.798 1.00 97.72  ? 493  ASP A OD2   1 
ATOM   4833  N N     . PRO D 4 497  ? 153.324 103.391 124.174 1.00 99.80  ? 494  PRO A N     1 
ATOM   4834  C CA    . PRO D 4 497  ? 154.057 102.984 125.382 1.00 100.18 ? 494  PRO A CA    1 
ATOM   4835  C C     . PRO D 4 497  ? 155.365 103.738 125.563 1.00 97.70  ? 494  PRO A C     1 
ATOM   4836  O O     . PRO D 4 497  ? 155.551 104.441 126.560 1.00 96.91  ? 494  PRO A O     1 
ATOM   4837  C CB    . PRO D 4 497  ? 154.303 101.487 125.152 1.00 103.34 ? 494  PRO A CB    1 
ATOM   4838  C CG    . PRO D 4 497  ? 153.223 101.065 124.217 1.00 101.94 ? 494  PRO A CG    1 
ATOM   4839  C CD    . PRO D 4 497  ? 152.986 102.241 123.318 1.00 99.88  ? 494  PRO A CD    1 
ATOM   4840  N N     . GLU D 4 498  ? 156.275 103.605 124.595 1.00 96.41  ? 495  GLU A N     1 
ATOM   4841  C CA    . GLU D 4 498  ? 157.595 104.209 124.733 1.00 95.14  ? 495  GLU A CA    1 
ATOM   4842  C C     . GLU D 4 498  ? 157.539 105.724 124.579 1.00 92.29  ? 495  GLU A C     1 
ATOM   4843  O O     . GLU D 4 498  ? 158.207 106.453 125.322 1.00 93.51  ? 495  GLU A O     1 
ATOM   4844  C CB    . GLU D 4 498  ? 158.559 103.601 123.714 1.00 95.44  ? 495  GLU A CB    1 
ATOM   4845  N N     . PHE D 4 499  ? 156.744 106.221 123.626 1.00 86.17  ? 496  PHE A N     1 
ATOM   4846  C CA    . PHE D 4 499  ? 156.741 107.652 123.338 1.00 79.92  ? 496  PHE A CA    1 
ATOM   4847  C C     . PHE D 4 499  ? 156.203 108.458 124.514 1.00 76.77  ? 496  PHE A C     1 
ATOM   4848  O O     . PHE D 4 499  ? 156.785 109.486 124.882 1.00 77.69  ? 496  PHE A O     1 
ATOM   4849  C CB    . PHE D 4 499  ? 155.924 107.936 122.079 1.00 75.12  ? 496  PHE A CB    1 
ATOM   4850  C CG    . PHE D 4 499  ? 156.059 109.348 121.572 1.00 72.57  ? 496  PHE A CG    1 
ATOM   4851  C CD1   . PHE D 4 499  ? 155.221 110.351 122.033 1.00 70.92  ? 496  PHE A CD1   1 
ATOM   4852  C CD2   . PHE D 4 499  ? 157.030 109.670 120.636 1.00 73.09  ? 496  PHE A CD2   1 
ATOM   4853  C CE1   . PHE D 4 499  ? 155.347 111.648 121.569 1.00 69.17  ? 496  PHE A CE1   1 
ATOM   4854  C CE2   . PHE D 4 499  ? 157.158 110.966 120.169 1.00 71.51  ? 496  PHE A CE2   1 
ATOM   4855  C CZ    . PHE D 4 499  ? 156.316 111.956 120.637 1.00 69.31  ? 496  PHE A CZ    1 
ATOM   4856  N N     . SER D 4 500  ? 155.094 108.016 125.110 1.00 74.04  ? 497  SER A N     1 
ATOM   4857  C CA    . SER D 4 500  ? 154.518 108.758 126.227 1.00 73.44  ? 497  SER A CA    1 
ATOM   4858  C C     . SER D 4 500  ? 155.438 108.755 127.440 1.00 78.22  ? 497  SER A C     1 
ATOM   4859  O O     . SER D 4 500  ? 155.431 109.712 128.222 1.00 75.81  ? 497  SER A O     1 
ATOM   4860  C CB    . SER D 4 500  ? 153.153 108.181 126.600 1.00 72.94  ? 497  SER A CB    1 
ATOM   4861  O OG    . SER D 4 500  ? 152.567 108.901 127.669 1.00 74.00  ? 497  SER A OG    1 
ATOM   4862  N N     . ALA D 4 501  ? 156.235 107.699 127.615 1.00 83.05  ? 498  ALA A N     1 
ATOM   4863  C CA    . ALA D 4 501  ? 157.151 107.653 128.751 1.00 85.02  ? 498  ALA A CA    1 
ATOM   4864  C C     . ALA D 4 501  ? 158.350 108.566 128.528 1.00 84.98  ? 498  ALA A C     1 
ATOM   4865  O O     . ALA D 4 501  ? 158.760 109.291 129.442 1.00 85.84  ? 498  ALA A O     1 
ATOM   4866  C CB    . ALA D 4 501  ? 157.606 106.215 129.003 1.00 86.72  ? 498  ALA A CB    1 
ATOM   4867  N N     . ARG D 4 502  ? 158.925 108.545 127.323 1.00 85.52  ? 499  ARG A N     1 
ATOM   4868  C CA    . ARG D 4 502  ? 160.071 109.403 127.035 1.00 88.02  ? 499  ARG A CA    1 
ATOM   4869  C C     . ARG D 4 502  ? 159.670 110.870 126.957 1.00 87.53  ? 499  ARG A C     1 
ATOM   4870  O O     . ARG D 4 502  ? 160.461 111.746 127.330 1.00 89.00  ? 499  ARG A O     1 
ATOM   4871  C CB    . ARG D 4 502  ? 160.742 108.967 125.733 1.00 91.14  ? 499  ARG A CB    1 
ATOM   4872  C CG    . ARG D 4 502  ? 161.184 107.514 125.709 1.00 98.39  ? 499  ARG A CG    1 
ATOM   4873  C CD    . ARG D 4 502  ? 162.034 107.227 124.483 1.00 103.76 ? 499  ARG A CD    1 
ATOM   4874  N NE    . ARG D 4 502  ? 163.335 107.883 124.567 1.00 109.77 ? 499  ARG A NE    1 
ATOM   4875  C CZ    . ARG D 4 502  ? 164.202 107.960 123.562 1.00 113.65 ? 499  ARG A CZ    1 
ATOM   4876  N NH1   . ARG D 4 502  ? 163.905 107.427 122.385 1.00 113.83 ? 499  ARG A NH1   1 
ATOM   4877  N NH2   . ARG D 4 502  ? 165.364 108.577 123.734 1.00 115.95 ? 499  ARG A NH2   1 
ATOM   4878  N N     . LEU D 4 503  ? 158.461 111.158 126.472 1.00 86.59  ? 500  LEU A N     1 
ATOM   4879  C CA    . LEU D 4 503  ? 158.005 112.542 126.398 1.00 83.48  ? 500  LEU A CA    1 
ATOM   4880  C C     . LEU D 4 503  ? 157.728 113.102 127.787 1.00 82.48  ? 500  LEU A C     1 
ATOM   4881  O O     . LEU D 4 503  ? 158.147 114.220 128.111 1.00 82.34  ? 500  LEU A O     1 
ATOM   4882  C CB    . LEU D 4 503  ? 156.756 112.638 125.521 1.00 78.20  ? 500  LEU A CB    1 
ATOM   4883  C CG    . LEU D 4 503  ? 156.100 114.016 125.436 1.00 74.84  ? 500  LEU A CG    1 
ATOM   4884  C CD1   . LEU D 4 503  ? 157.065 115.035 124.848 1.00 75.31  ? 500  LEU A CD1   1 
ATOM   4885  C CD2   . LEU D 4 503  ? 154.822 113.950 124.618 1.00 72.65  ? 500  LEU A CD2   1 
ATOM   4886  N N     . THR D 4 504  ? 157.026 112.335 128.625 1.00 82.46  ? 501  THR A N     1 
ATOM   4887  C CA    . THR D 4 504  ? 156.722 112.797 129.976 1.00 83.03  ? 501  THR A CA    1 
ATOM   4888  C C     . THR D 4 504  ? 157.990 112.988 130.799 1.00 83.95  ? 501  THR A C     1 
ATOM   4889  O O     . THR D 4 504  ? 158.015 113.816 131.716 1.00 84.42  ? 501  THR A O     1 
ATOM   4890  C CB    . THR D 4 504  ? 155.783 111.809 130.671 1.00 85.10  ? 501  THR A CB    1 
ATOM   4891  O OG1   . THR D 4 504  ? 154.776 111.374 129.748 1.00 84.13  ? 501  THR A OG1   1 
ATOM   4892  C CG2   . THR D 4 504  ? 155.108 112.464 131.868 1.00 87.44  ? 501  THR A CG2   1 
ATOM   4893  N N     . GLY D 4 505  ? 159.047 112.239 130.485 1.00 85.49  ? 502  GLY A N     1 
ATOM   4894  C CA    . GLY D 4 505  ? 160.297 112.408 131.210 1.00 87.05  ? 502  GLY A CA    1 
ATOM   4895  C C     . GLY D 4 505  ? 160.963 113.738 130.911 1.00 83.65  ? 502  GLY A C     1 
ATOM   4896  O O     . GLY D 4 505  ? 161.319 114.488 131.824 1.00 84.50  ? 502  GLY A O     1 
ATOM   4897  N N     . ILE D 4 506  ? 161.137 114.054 129.624 1.00 80.70  ? 503  ILE A N     1 
ATOM   4898  C CA    . ILE D 4 506  ? 161.765 115.316 129.254 1.00 80.89  ? 503  ILE A CA    1 
ATOM   4899  C C     . ILE D 4 506  ? 160.821 116.494 129.452 1.00 83.11  ? 503  ILE A C     1 
ATOM   4900  O O     . ILE D 4 506  ? 161.283 117.636 129.562 1.00 83.07  ? 503  ILE A O     1 
ATOM   4901  C CB    . ILE D 4 506  ? 162.273 115.262 127.802 1.00 78.19  ? 503  ILE A CB    1 
ATOM   4902  C CG1   . ILE D 4 506  ? 161.107 115.084 126.830 1.00 75.43  ? 503  ILE A CG1   1 
ATOM   4903  C CG2   . ILE D 4 506  ? 163.281 114.139 127.632 1.00 80.82  ? 503  ILE A CG2   1 
ATOM   4904  C CD1   . ILE D 4 506  ? 161.532 115.020 125.379 1.00 74.34  ? 503  ILE A CD1   1 
ATOM   4905  N N     . LYS D 4 507  ? 159.510 116.254 129.498 1.00 85.24  ? 504  LYS A N     1 
ATOM   4906  C CA    . LYS D 4 507  ? 158.575 117.340 129.775 1.00 85.52  ? 504  LYS A CA    1 
ATOM   4907  C C     . LYS D 4 507  ? 158.682 117.799 131.222 1.00 90.70  ? 504  LYS A C     1 
ATOM   4908  O O     . LYS D 4 507  ? 158.611 119.003 131.507 1.00 87.62  ? 504  LYS A O     1 
ATOM   4909  C CB    . LYS D 4 507  ? 157.145 116.904 129.449 1.00 82.62  ? 504  LYS A CB    1 
ATOM   4910  C CG    . LYS D 4 507  ? 156.086 117.948 129.775 1.00 81.76  ? 504  LYS A CG    1 
ATOM   4911  C CD    . LYS D 4 507  ? 154.689 117.474 129.398 1.00 81.05  ? 504  LYS A CD    1 
ATOM   4912  C CE    . LYS D 4 507  ? 154.543 117.313 127.893 1.00 80.65  ? 504  LYS A CE    1 
ATOM   4913  N NZ    . LYS D 4 507  ? 153.147 116.978 127.497 1.00 78.56  ? 504  LYS A NZ    1 
ATOM   4914  N N     . LEU D 4 508  ? 158.856 116.858 132.152 1.00 102.75 ? 505  LEU A N     1 
ATOM   4915  C CA    . LEU D 4 508  ? 159.039 117.209 133.556 1.00 105.40 ? 505  LEU A CA    1 
ATOM   4916  C C     . LEU D 4 508  ? 160.437 117.733 133.850 1.00 107.48 ? 505  LEU A C     1 
ATOM   4917  O O     . LEU D 4 508  ? 160.618 118.460 134.833 1.00 108.38 ? 505  LEU A O     1 
ATOM   4918  C CB    . LEU D 4 508  ? 158.743 116.001 134.450 1.00 107.96 ? 505  LEU A CB    1 
ATOM   4919  C CG    . LEU D 4 508  ? 157.318 115.869 135.000 1.00 110.35 ? 505  LEU A CG    1 
ATOM   4920  C CD1   . LEU D 4 508  ? 156.287 115.798 133.883 1.00 109.49 ? 505  LEU A CD1   1 
ATOM   4921  C CD2   . LEU D 4 508  ? 157.209 114.656 135.914 1.00 113.18 ? 505  LEU A CD2   1 
ATOM   4922  N N     . GLU D 4 509  ? 161.427 117.382 133.028 1.00 102.75 ? 506  GLU A N     1 
ATOM   4923  C CA    . GLU D 4 509  ? 162.772 117.915 133.197 1.00 103.00 ? 506  GLU A CA    1 
ATOM   4924  C C     . GLU D 4 509  ? 162.933 119.294 132.571 1.00 102.90 ? 506  GLU A C     1 
ATOM   4925  O O     . GLU D 4 509  ? 163.900 119.996 132.889 1.00 104.27 ? 506  GLU A O     1 
ATOM   4926  C CB    . GLU D 4 509  ? 163.796 116.941 132.612 1.00 104.08 ? 506  GLU A CB    1 
ATOM   4927  C CG    . GLU D 4 509  ? 163.937 115.659 133.420 1.00 107.41 ? 506  GLU A CG    1 
ATOM   4928  C CD    . GLU D 4 509  ? 164.694 114.573 132.681 1.00 110.86 ? 506  GLU A CD    1 
ATOM   4929  O OE1   . GLU D 4 509  ? 165.673 114.899 131.977 1.00 111.82 ? 506  GLU A OE1   1 
ATOM   4930  O OE2   . GLU D 4 509  ? 164.308 113.391 132.800 1.00 112.85 ? 506  GLU A OE2   1 
ATOM   4931  N N     . MET D 4 510  ? 162.016 119.691 131.692 1.00 101.52 ? 507  MET A N     1 
ATOM   4932  C CA    . MET D 4 510  ? 161.942 121.053 131.181 1.00 100.24 ? 507  MET A CA    1 
ATOM   4933  C C     . MET D 4 510  ? 160.964 121.916 131.966 1.00 102.99 ? 507  MET A C     1 
ATOM   4934  O O     . MET D 4 510  ? 160.848 123.113 131.685 1.00 101.13 ? 507  MET A O     1 
ATOM   4935  C CB    . MET D 4 510  ? 161.542 121.039 129.701 1.00 95.44  ? 507  MET A CB    1 
ATOM   4936  C CG    . MET D 4 510  ? 162.602 120.484 128.763 1.00 94.68  ? 507  MET A CG    1 
ATOM   4937  S SD    . MET D 4 510  ? 163.871 121.694 128.348 1.00 94.39  ? 507  MET A SD    1 
ATOM   4938  C CE    . MET D 4 510  ? 162.872 122.968 127.583 1.00 91.88  ? 507  MET A CE    1 
ATOM   4939  N N     . GLU D 4 511  ? 160.262 121.332 132.936 1.00 112.46 ? 508  GLU A N     1 
ATOM   4940  C CA    . GLU D 4 511  ? 159.281 122.089 133.711 1.00 113.12 ? 508  GLU A CA    1 
ATOM   4941  C C     . GLU D 4 511  ? 159.882 123.233 134.523 1.00 112.73 ? 508  GLU A C     1 
ATOM   4942  O O     . GLU D 4 511  ? 159.269 124.315 134.548 1.00 111.84 ? 508  GLU A O     1 
ATOM   4943  C CB    . GLU D 4 511  ? 158.500 121.122 134.616 1.00 117.39 ? 508  GLU A CB    1 
ATOM   4944  C CG    . GLU D 4 511  ? 157.565 121.790 135.608 1.00 119.48 ? 508  GLU A CG    1 
ATOM   4945  C CD    . GLU D 4 511  ? 156.779 120.783 136.425 1.00 123.38 ? 508  GLU A CD    1 
ATOM   4946  O OE1   . GLU D 4 511  ? 156.352 119.756 135.854 1.00 123.82 ? 508  GLU A OE1   1 
ATOM   4947  O OE2   . GLU D 4 511  ? 156.599 121.010 137.641 1.00 125.81 ? 508  GLU A OE2   1 
ATOM   4948  N N     . PRO D 4 512  ? 161.029 123.088 135.202 1.00 104.02 ? 509  PRO A N     1 
ATOM   4949  C CA    . PRO D 4 512  ? 161.577 124.233 135.952 1.00 99.69  ? 509  PRO A CA    1 
ATOM   4950  C C     . PRO D 4 512  ? 161.963 125.421 135.082 1.00 97.05  ? 509  PRO A C     1 
ATOM   4951  O O     . PRO D 4 512  ? 162.216 126.502 135.631 1.00 98.09  ? 509  PRO A O     1 
ATOM   4952  C CB    . PRO D 4 512  ? 162.807 123.639 136.651 1.00 100.65 ? 509  PRO A CB    1 
ATOM   4953  C CG    . PRO D 4 512  ? 162.520 122.189 136.744 1.00 102.25 ? 509  PRO A CG    1 
ATOM   4954  C CD    . PRO D 4 512  ? 161.789 121.855 135.481 1.00 102.74 ? 509  PRO A CD    1 
ATOM   4955  N N     . SER D 4 513  ? 162.016 125.266 133.757 1.00 91.01  ? 510  SER A N     1 
ATOM   4956  C CA    . SER D 4 513  ? 162.384 126.386 132.896 1.00 83.19  ? 510  SER A CA    1 
ATOM   4957  C C     . SER D 4 513  ? 161.292 127.444 132.820 1.00 75.65  ? 510  SER A C     1 
ATOM   4958  O O     . SER D 4 513  ? 161.591 128.604 132.513 1.00 74.11  ? 510  SER A O     1 
ATOM   4959  C CB    . SER D 4 513  ? 162.725 125.882 131.492 1.00 80.27  ? 510  SER A CB    1 
ATOM   4960  O OG    . SER D 4 513  ? 161.615 125.235 130.896 1.00 77.09  ? 510  SER A OG    1 
ATOM   4961  N N     . LEU D 4 514  ? 160.037 127.077 133.087 1.00 72.35  ? 511  LEU A N     1 
ATOM   4962  C CA    . LEU D 4 514  ? 158.959 128.063 133.064 1.00 69.78  ? 511  LEU A CA    1 
ATOM   4963  C C     . LEU D 4 514  ? 159.090 129.043 134.222 1.00 72.78  ? 511  LEU A C     1 
ATOM   4964  O O     . LEU D 4 514  ? 158.982 130.261 134.033 1.00 73.23  ? 511  LEU A O     1 
ATOM   4965  C CB    . LEU D 4 514  ? 157.601 127.360 133.101 1.00 66.82  ? 511  LEU A CB    1 
ATOM   4966  C CG    . LEU D 4 514  ? 156.376 128.269 133.217 1.00 64.21  ? 511  LEU A CG    1 
ATOM   4967  C CD1   . LEU D 4 514  ? 156.286 129.222 132.032 1.00 62.52  ? 511  LEU A CD1   1 
ATOM   4968  C CD2   . LEU D 4 514  ? 155.106 127.442 133.341 1.00 63.30  ? 511  LEU A CD2   1 
ATOM   4969  N N     . SER D 4 515  ? 159.319 128.530 135.435 1.00 76.44  ? 512  SER A N     1 
ATOM   4970  C CA    . SER D 4 515  ? 159.502 129.415 136.581 1.00 76.70  ? 512  SER A CA    1 
ATOM   4971  C C     . SER D 4 515  ? 160.791 130.214 136.466 1.00 76.20  ? 512  SER A C     1 
ATOM   4972  O O     . SER D 4 515  ? 160.862 131.345 136.964 1.00 76.35  ? 512  SER A O     1 
ATOM   4973  C CB    . SER D 4 515  ? 159.493 128.608 137.880 1.00 79.55  ? 512  SER A CB    1 
ATOM   4974  O OG    . SER D 4 515  ? 160.640 127.783 137.976 1.00 84.44  ? 512  SER A OG    1 
ATOM   4975  N N     . PHE D 4 516  ? 161.814 129.654 135.818 1.00 75.39  ? 513  PHE A N     1 
ATOM   4976  C CA    . PHE D 4 516  ? 163.052 130.401 135.618 1.00 77.38  ? 513  PHE A CA    1 
ATOM   4977  C C     . PHE D 4 516  ? 162.849 131.582 134.682 1.00 75.58  ? 513  PHE A C     1 
ATOM   4978  O O     . PHE D 4 516  ? 163.526 132.608 134.826 1.00 76.28  ? 513  PHE A O     1 
ATOM   4979  C CB    . PHE D 4 516  ? 164.149 129.484 135.083 1.00 80.06  ? 513  PHE A CB    1 
ATOM   4980  C CG    . PHE D 4 516  ? 165.030 128.912 136.153 1.00 84.69  ? 513  PHE A CG    1 
ATOM   4981  C CD1   . PHE D 4 516  ? 164.739 129.119 137.492 1.00 86.32  ? 513  PHE A CD1   1 
ATOM   4982  C CD2   . PHE D 4 516  ? 166.160 128.187 135.824 1.00 86.89  ? 513  PHE A CD2   1 
ATOM   4983  C CE1   . PHE D 4 516  ? 165.550 128.600 138.482 1.00 88.99  ? 513  PHE A CE1   1 
ATOM   4984  C CE2   . PHE D 4 516  ? 166.977 127.667 136.808 1.00 90.26  ? 513  PHE A CE2   1 
ATOM   4985  C CZ    . PHE D 4 516  ? 166.672 127.873 138.139 1.00 91.57  ? 513  PHE A CZ    1 
ATOM   4986  N N     . TYR D 4 517  ? 161.932 131.465 133.719 1.00 74.45  ? 514  TYR A N     1 
ATOM   4987  C CA    . TYR D 4 517  ? 161.612 132.605 132.867 1.00 71.64  ? 514  TYR A CA    1 
ATOM   4988  C C     . TYR D 4 517  ? 160.958 133.718 133.678 1.00 71.61  ? 514  TYR A C     1 
ATOM   4989  O O     . TYR D 4 517  ? 161.336 134.889 133.563 1.00 72.45  ? 514  TYR A O     1 
ATOM   4990  C CB    . TYR D 4 517  ? 160.703 132.167 131.718 1.00 68.42  ? 514  TYR A CB    1 
ATOM   4991  C CG    . TYR D 4 517  ? 160.510 133.227 130.654 1.00 66.16  ? 514  TYR A CG    1 
ATOM   4992  C CD1   . TYR D 4 517  ? 159.540 134.212 130.792 1.00 63.57  ? 514  TYR A CD1   1 
ATOM   4993  C CD2   . TYR D 4 517  ? 161.295 133.239 129.508 1.00 66.60  ? 514  TYR A CD2   1 
ATOM   4994  C CE1   . TYR D 4 517  ? 159.364 135.182 129.824 1.00 62.72  ? 514  TYR A CE1   1 
ATOM   4995  C CE2   . TYR D 4 517  ? 161.125 134.202 128.534 1.00 64.16  ? 514  TYR A CE2   1 
ATOM   4996  C CZ    . TYR D 4 517  ? 160.159 135.171 128.696 1.00 63.61  ? 514  TYR A CZ    1 
ATOM   4997  O OH    . TYR D 4 517  ? 159.987 136.133 127.726 1.00 65.35  ? 514  TYR A OH    1 
ATOM   4998  N N     . ASN D 4 518  ? 159.972 133.367 134.507 1.00 72.31  ? 515  ASN A N     1 
ATOM   4999  C CA    . ASN D 4 518  ? 159.285 134.376 135.302 1.00 73.99  ? 515  ASN A CA    1 
ATOM   5000  C C     . ASN D 4 518  ? 160.187 134.931 136.399 1.00 77.54  ? 515  ASN A C     1 
ATOM   5001  O O     . ASN D 4 518  ? 160.175 136.137 136.666 1.00 79.60  ? 515  ASN A O     1 
ATOM   5002  C CB    . ASN D 4 518  ? 158.002 133.797 135.896 1.00 74.88  ? 515  ASN A CB    1 
ATOM   5003  C CG    . ASN D 4 518  ? 156.911 133.614 134.858 1.00 73.59  ? 515  ASN A CG    1 
ATOM   5004  O OD1   . ASN D 4 518  ? 156.791 134.405 133.923 1.00 72.82  ? 515  ASN A OD1   1 
ATOM   5005  N ND2   . ASN D 4 518  ? 156.107 132.568 135.019 1.00 73.12  ? 515  ASN A ND2   1 
ATOM   5006  N N     . LYS D 4 519  ? 160.976 134.068 137.046 1.00 78.53  ? 516  LYS A N     1 
ATOM   5007  C CA    . LYS D 4 519  ? 161.888 134.545 138.084 1.00 78.99  ? 516  LYS A CA    1 
ATOM   5008  C C     . LYS D 4 519  ? 162.929 135.497 137.512 1.00 77.73  ? 516  LYS A C     1 
ATOM   5009  O O     . LYS D 4 519  ? 163.291 136.490 138.154 1.00 76.91  ? 516  LYS A O     1 
ATOM   5010  C CB    . LYS D 4 519  ? 162.571 133.364 138.775 1.00 83.53  ? 516  LYS A CB    1 
ATOM   5011  C CG    . LYS D 4 519  ? 161.719 132.644 139.809 1.00 86.21  ? 516  LYS A CG    1 
ATOM   5012  C CD    . LYS D 4 519  ? 162.541 131.588 140.540 1.00 92.12  ? 516  LYS A CD    1 
ATOM   5013  C CE    . LYS D 4 519  ? 161.730 130.890 141.620 1.00 93.79  ? 516  LYS A CE    1 
ATOM   5014  N NZ    . LYS D 4 519  ? 162.554 129.913 142.387 1.00 96.57  ? 516  LYS A NZ    1 
ATOM   5015  N N     . ALA D 4 520  ? 163.420 135.215 136.302 1.00 76.46  ? 517  ALA A N     1 
ATOM   5016  C CA    . ALA D 4 520  ? 164.447 136.064 135.707 1.00 74.11  ? 517  ALA A CA    1 
ATOM   5017  C C     . ALA D 4 520  ? 163.868 137.388 135.228 1.00 71.48  ? 517  ALA A C     1 
ATOM   5018  O O     . ALA D 4 520  ? 164.499 138.440 135.389 1.00 73.72  ? 517  ALA A O     1 
ATOM   5019  C CB    . ALA D 4 520  ? 165.135 135.331 134.556 1.00 71.01  ? 517  ALA A CB    1 
ATOM   5020  N N     . ARG D 4 521  ? 162.671 137.360 134.635 1.00 67.81  ? 518  ARG A N     1 
ATOM   5021  C CA    . ARG D 4 521  ? 162.048 138.600 134.181 1.00 68.16  ? 518  ARG A CA    1 
ATOM   5022  C C     . ARG D 4 521  ? 161.700 139.506 135.356 1.00 70.46  ? 518  ARG A C     1 
ATOM   5023  O O     . ARG D 4 521  ? 161.847 140.731 135.268 1.00 69.87  ? 518  ARG A O     1 
ATOM   5024  C CB    . ARG D 4 521  ? 160.801 138.292 133.353 1.00 66.18  ? 518  ARG A CB    1 
ATOM   5025  C CG    . ARG D 4 521  ? 159.996 139.526 132.970 1.00 64.38  ? 518  ARG A CG    1 
ATOM   5026  C CD    . ARG D 4 521  ? 158.716 139.153 132.241 1.00 63.99  ? 518  ARG A CD    1 
ATOM   5027  N NE    . ARG D 4 521  ? 158.040 138.025 132.875 1.00 65.04  ? 518  ARG A NE    1 
ATOM   5028  C CZ    . ARG D 4 521  ? 157.302 138.115 133.975 1.00 64.65  ? 518  ARG A CZ    1 
ATOM   5029  N NH1   . ARG D 4 521  ? 157.144 139.286 134.579 1.00 66.10  ? 518  ARG A NH1   1 
ATOM   5030  N NH2   . ARG D 4 521  ? 156.728 137.032 134.479 1.00 62.87  ? 518  ARG A NH2   1 
ATOM   5031  N N     . ASN D 4 522  ? 161.441 138.890 136.505 1.00 72.91  ? 519  ASN A N     1 
ATOM   5032  C CA    . ASN D 4 522  ? 161.101 139.675 137.708 1.00 73.38  ? 519  ASN A CA    1 
ATOM   5033  C C     . ASN D 4 522  ? 162.383 140.170 138.313 1.00 76.71  ? 519  ASN A C     1 
ATOM   5034  O O     . ASN D 4 522  ? 162.371 141.259 138.877 1.00 78.91  ? 519  ASN A O     1 
ATOM   5035  C CB    . ASN D 4 522  ? 160.324 138.858 138.728 1.00 72.27  ? 519  ASN A CB    1 
ATOM   5036  C CG    . ASN D 4 522  ? 158.951 138.465 138.227 1.00 67.56  ? 519  ASN A CG    1 
ATOM   5037  O OD1   . ASN D 4 522  ? 158.475 138.998 137.226 1.00 64.67  ? 519  ASN A OD1   1 
ATOM   5038  N ND2   . ASN D 4 522  ? 158.307 137.535 138.913 1.00 66.76  ? 519  ASN A ND2   1 
ATOM   5039  N N     . TYR D 4 523  ? 163.447 139.411 138.186 1.00 80.05  ? 520  TYR A N     1 
ATOM   5040  C CA    . TYR D 4 523  ? 164.714 139.976 138.701 1.00 83.54  ? 520  TYR A CA    1 
ATOM   5041  C C     . TYR D 4 523  ? 165.045 141.295 138.005 1.00 83.60  ? 520  TYR A C     1 
ATOM   5042  O O     . TYR D 4 523  ? 165.530 142.212 138.698 1.00 85.26  ? 520  TYR A O     1 
ATOM   5043  C CB    . TYR D 4 523  ? 165.931 139.090 138.469 1.00 87.59  ? 520  TYR A CB    1 
ATOM   5044  C CG    . TYR D 4 523  ? 167.209 139.848 138.717 1.00 94.34  ? 520  TYR A CG    1 
ATOM   5045  C CD1   . TYR D 4 523  ? 167.572 140.202 140.003 1.00 97.25  ? 520  TYR A CD1   1 
ATOM   5046  C CD2   . TYR D 4 523  ? 168.013 140.272 137.674 1.00 97.66  ? 520  TYR A CD2   1 
ATOM   5047  C CE1   . TYR D 4 523  ? 168.720 140.928 140.254 1.00 100.33 ? 520  TYR A CE1   1 
ATOM   5048  C CE2   . TYR D 4 523  ? 169.168 140.994 137.908 1.00 101.02 ? 520  TYR A CE2   1 
ATOM   5049  C CZ    . TYR D 4 523  ? 169.521 141.323 139.202 1.00 102.05 ? 520  TYR A CZ    1 
ATOM   5050  O OH    . TYR D 4 523  ? 170.643 142.051 139.451 1.00 104.34 ? 520  TYR A OH    1 
ATOM   5051  N N     . ALA D 4 524  ? 164.782 141.426 136.702 1.00 64.94  ? 521  ALA A N     1 
ATOM   5052  C CA    . ALA D 4 524  ? 165.227 142.640 135.982 1.00 64.94  ? 521  ALA A CA    1 
ATOM   5053  C C     . ALA D 4 524  ? 164.078 143.576 135.565 1.00 64.94  ? 521  ALA A C     1 
ATOM   5054  O O     . ALA D 4 524  ? 164.366 144.497 134.809 1.00 64.94  ? 521  ALA A O     1 
ATOM   5055  C CB    . ALA D 4 524  ? 166.031 142.155 134.818 1.00 64.94  ? 521  ALA A CB    1 
ATOM   5056  N N     . THR D 4 525  ? 162.836 143.353 136.009 1.00 61.87  ? 522  THR A N     1 
ATOM   5057  C CA    . THR D 4 525  ? 161.679 144.248 135.706 1.00 61.87  ? 522  THR A CA    1 
ATOM   5058  C C     . THR D 4 525  ? 161.239 144.905 137.010 1.00 61.87  ? 522  THR A C     1 
ATOM   5059  O O     . THR D 4 525  ? 160.138 145.487 137.031 1.00 61.87  ? 522  THR A O     1 
ATOM   5060  C CB    . THR D 4 525  ? 160.516 143.509 135.046 1.00 61.87  ? 522  THR A CB    1 
ATOM   5061  O OG1   . THR D 4 525  ? 160.207 142.376 135.856 1.00 61.87  ? 522  THR A OG1   1 
ATOM   5062  C CG2   . THR D 4 525  ? 160.814 143.079 133.628 1.00 61.87  ? 522  THR A CG2   1 
ATOM   5063  N N     . LYS D 4 526  ? 162.057 144.813 138.043 1.00 55.29  ? 523  LYS A N     1 
ATOM   5064  C CA    . LYS D 4 526  ? 161.877 145.340 139.388 1.00 55.29  ? 523  LYS A CA    1 
ATOM   5065  C C     . LYS D 4 526  ? 162.641 146.648 139.555 1.00 55.29  ? 523  LYS A C     1 
ATOM   5066  O O     . LYS D 4 526  ? 163.732 146.829 139.007 1.00 55.29  ? 523  LYS A O     1 
ATOM   5067  C CB    . LYS D 4 526  ? 162.332 144.323 140.436 1.00 55.29  ? 523  LYS A CB    1 
ATOM   5068  C CG    . LYS D 4 526  ? 163.836 144.120 140.512 1.00 55.29  ? 523  LYS A CG    1 
ATOM   5069  C CD    . LYS D 4 526  ? 164.279 143.752 141.918 1.00 55.29  ? 523  LYS A CD    1 
ATOM   5070  C CE    . LYS D 4 526  ? 165.788 143.856 142.061 1.00 55.29  ? 523  LYS A CE    1 
ATOM   5071  N NZ    . LYS D 4 526  ? 166.293 145.185 141.619 1.00 55.29  ? 523  LYS A NZ    1 
ATOM   5072  N N     . LYS D 4 527  ? 162.047 147.570 140.306 1.00 50.26  ? 524  LYS A N     1 
ATOM   5073  C CA    . LYS D 4 527  ? 162.677 148.848 140.567 1.00 50.26  ? 524  LYS A CA    1 
ATOM   5074  C C     . LYS D 4 527  ? 163.829 148.675 141.555 1.00 50.26  ? 524  LYS A C     1 
ATOM   5075  O O     . LYS D 4 527  ? 163.876 147.698 142.305 1.00 50.26  ? 524  LYS A O     1 
ATOM   5076  C CB    . LYS D 4 527  ? 161.651 149.836 141.111 1.00 43.74  ? 524  LYS A CB    1 
ATOM   5077  C CG    . LYS D 4 527  ? 160.361 149.904 140.317 1.00 43.74  ? 524  LYS A CG    1 
ATOM   5078  C CD    . LYS D 4 527  ? 159.215 150.399 141.182 1.00 43.74  ? 524  LYS A CD    1 
ATOM   5079  C CE    . LYS D 4 527  ? 157.915 150.458 140.400 1.00 43.74  ? 524  LYS A CE    1 
ATOM   5080  N NZ    . LYS D 4 527  ? 157.225 149.140 140.380 1.00 43.74  ? 524  LYS A NZ    1 
ATOM   5081  N N     . PRO D 4 528  ? 164.779 149.617 141.575 1.00 50.26  ? 525  PRO A N     1 
ATOM   5082  C CA    . PRO D 4 528  ? 165.930 149.480 142.480 1.00 50.26  ? 525  PRO A CA    1 
ATOM   5083  C C     . PRO D 4 528  ? 165.575 149.644 143.951 1.00 50.26  ? 525  PRO A C     1 
ATOM   5084  O O     . PRO D 4 528  ? 166.468 149.647 144.804 1.00 50.26  ? 525  PRO A O     1 
ATOM   5085  C CB    . PRO D 4 528  ? 166.876 150.597 142.016 1.00 50.26  ? 525  PRO A CB    1 
ATOM   5086  C CG    . PRO D 4 528  ? 166.425 150.950 140.641 1.00 50.26  ? 525  PRO A CG    1 
ATOM   5087  C CD    . PRO D 4 528  ? 164.949 150.741 140.641 1.00 50.26  ? 525  PRO A CD    1 
ATOM   5088  N N     . TYR D 4 529  ? 164.291 149.779 144.266 1.00 50.26  ? 526  TYR A N     1 
ATOM   5089  C CA    . TYR D 4 529  ? 163.873 150.028 145.638 1.00 50.26  ? 526  TYR A CA    1 
ATOM   5090  C C     . TYR D 4 529  ? 163.897 148.723 146.429 1.00 50.26  ? 526  TYR A C     1 
ATOM   5091  O O     . TYR D 4 529  ? 164.286 147.663 145.931 1.00 50.26  ? 526  TYR A O     1 
ATOM   5092  C CB    . TYR D 4 529  ? 162.474 150.635 145.681 1.00 50.26  ? 526  TYR A CB    1 
ATOM   5093  C CG    . TYR D 4 529  ? 162.295 151.884 144.862 1.00 50.26  ? 526  TYR A CG    1 
ATOM   5094  C CD1   . TYR D 4 529  ? 162.865 153.080 145.247 1.00 50.26  ? 526  TYR A CD1   1 
ATOM   5095  C CD2   . TYR D 4 529  ? 161.494 151.877 143.733 1.00 50.26  ? 526  TYR A CD2   1 
ATOM   5096  C CE1   . TYR D 4 529  ? 162.684 154.225 144.505 1.00 50.26  ? 526  TYR A CE1   1 
ATOM   5097  C CE2   . TYR D 4 529  ? 161.304 153.012 142.983 1.00 50.26  ? 526  TYR A CE2   1 
ATOM   5098  C CZ    . TYR D 4 529  ? 161.901 154.187 143.372 1.00 50.26  ? 526  TYR A CZ    1 
ATOM   5099  O OH    . TYR D 4 529  ? 161.710 155.327 142.626 1.00 50.26  ? 526  TYR A OH    1 
ATOM   5100  N N     . SER D 4 530  ? 163.474 148.798 147.689 1.00 50.26  ? 527  SER A N     1 
ATOM   5101  C CA    . SER D 4 530  ? 163.086 147.619 148.463 1.00 50.26  ? 527  SER A CA    1 
ATOM   5102  C C     . SER D 4 530  ? 161.988 148.086 149.418 1.00 50.26  ? 527  SER A C     1 
ATOM   5103  O O     . SER D 4 530  ? 162.266 148.579 150.513 1.00 50.26  ? 527  SER A O     1 
ATOM   5104  C CB    . SER D 4 530  ? 164.261 147.000 149.205 1.00 50.26  ? 527  SER A CB    1 
ATOM   5105  O OG    . SER D 4 530  ? 163.989 145.656 149.559 1.00 50.26  ? 527  SER A OG    1 
ATOM   5106  N N     . VAL D 4 531  ? 160.735 147.924 148.982 1.00 50.26  ? 528  VAL A N     1 
ATOM   5107  C CA    . VAL D 4 531  ? 159.590 148.442 149.728 1.00 50.26  ? 528  VAL A CA    1 
ATOM   5108  C C     . VAL D 4 531  ? 159.223 147.552 150.906 1.00 50.26  ? 528  VAL A C     1 
ATOM   5109  O O     . VAL D 4 531  ? 158.256 147.846 151.621 1.00 50.26  ? 528  VAL A O     1 
ATOM   5110  C CB    . VAL D 4 531  ? 158.428 148.634 148.729 1.00 50.26  ? 528  VAL A CB    1 
ATOM   5111  C CG1   . VAL D 4 531  ? 157.256 149.392 149.348 1.00 50.26  ? 528  VAL A CG1   1 
ATOM   5112  C CG2   . VAL D 4 531  ? 158.922 149.346 147.481 1.00 50.26  ? 528  VAL A CG2   1 
ATOM   5113  N N     . GLU D 4 532  ? 159.977 146.481 151.146 1.00 50.26  ? 529  GLU A N     1 
ATOM   5114  C CA    . GLU D 4 532  ? 159.669 145.581 152.248 1.00 50.26  ? 529  GLU A CA    1 
ATOM   5115  C C     . GLU D 4 532  ? 159.710 146.325 153.577 1.00 50.26  ? 529  GLU A C     1 
ATOM   5116  O O     . GLU D 4 532  ? 160.614 147.126 153.831 1.00 50.26  ? 529  GLU A O     1 
ATOM   5117  C CB    . GLU D 4 532  ? 160.638 144.393 152.249 1.00 50.26  ? 529  GLU A CB    1 
ATOM   5118  C CG    . GLU D 4 532  ? 162.115 144.732 152.429 1.00 50.26  ? 529  GLU A CG    1 
ATOM   5119  C CD    . GLU D 4 532  ? 162.532 144.847 153.885 1.00 50.26  ? 529  GLU A CD    1 
ATOM   5120  O OE1   . GLU D 4 532  ? 161.728 144.487 154.770 1.00 50.26  ? 529  GLU A OE1   1 
ATOM   5121  O OE2   . GLU D 4 532  ? 163.669 145.294 154.145 1.00 50.26  ? 529  GLU A OE2   1 
ATOM   5122  N N     . LYS D 4 533  ? 158.704 146.078 154.411 1.00 50.26  ? 530  LYS A N     1 
ATOM   5123  C CA    . LYS D 4 533  ? 158.582 146.724 155.708 1.00 50.26  ? 530  LYS A CA    1 
ATOM   5124  C C     . LYS D 4 533  ? 158.061 145.712 156.716 1.00 50.26  ? 530  LYS A C     1 
ATOM   5125  O O     . LYS D 4 533  ? 157.380 144.749 156.356 1.00 50.26  ? 530  LYS A O     1 
ATOM   5126  C CB    . LYS D 4 533  ? 157.646 147.937 155.642 1.00 50.26  ? 530  LYS A CB    1 
ATOM   5127  C CG    . LYS D 4 533  ? 156.182 147.575 155.459 1.00 50.26  ? 530  LYS A CG    1 
ATOM   5128  C CD    . LYS D 4 533  ? 155.338 148.799 155.166 1.00 50.26  ? 530  LYS A CD    1 
ATOM   5129  C CE    . LYS D 4 533  ? 155.430 149.190 153.706 1.00 50.26  ? 530  LYS A CE    1 
ATOM   5130  N NZ    . LYS D 4 533  ? 154.760 148.187 152.836 1.00 50.26  ? 530  LYS A NZ    1 
ATOM   5131  N N     . PHE D 4 534  ? 158.391 145.935 157.984 1.00 50.26  ? 531  PHE A N     1 
ATOM   5132  C CA    . PHE D 4 534  ? 157.926 145.080 159.065 1.00 50.26  ? 531  PHE A CA    1 
ATOM   5133  C C     . PHE D 4 534  ? 157.240 145.931 160.120 1.00 50.26  ? 531  PHE A C     1 
ATOM   5134  O O     . PHE D 4 534  ? 157.689 147.039 160.425 1.00 50.26  ? 531  PHE A O     1 
ATOM   5135  C CB    . PHE D 4 534  ? 159.074 144.280 159.690 1.00 50.26  ? 531  PHE A CB    1 
ATOM   5136  C CG    . PHE D 4 534  ? 160.294 145.097 159.995 1.00 50.26  ? 531  PHE A CG    1 
ATOM   5137  C CD1   . PHE D 4 534  ? 160.446 145.706 161.228 1.00 50.26  ? 531  PHE A CD1   1 
ATOM   5138  C CD2   . PHE D 4 534  ? 161.298 145.242 159.054 1.00 50.26  ? 531  PHE A CD2   1 
ATOM   5139  C CE1   . PHE D 4 534  ? 161.569 146.450 161.512 1.00 50.26  ? 531  PHE A CE1   1 
ATOM   5140  C CE2   . PHE D 4 534  ? 162.422 145.986 159.333 1.00 50.26  ? 531  PHE A CE2   1 
ATOM   5141  C CZ    . PHE D 4 534  ? 162.559 146.590 160.564 1.00 50.26  ? 531  PHE A CZ    1 
ATOM   5142  N N     . LYS D 4 535  ? 156.148 145.409 160.669 1.00 50.26  ? 532  LYS A N     1 
ATOM   5143  C CA    . LYS D 4 535  ? 155.360 146.170 161.624 1.00 50.26  ? 532  LYS A CA    1 
ATOM   5144  C C     . LYS D 4 535  ? 156.100 146.313 162.949 1.00 50.26  ? 532  LYS A C     1 
ATOM   5145  O O     . LYS D 4 535  ? 156.888 145.451 163.347 1.00 50.26  ? 532  LYS A O     1 
ATOM   5146  C CB    . LYS D 4 535  ? 153.998 145.510 161.839 1.00 50.26  ? 532  LYS A CB    1 
ATOM   5147  C CG    . LYS D 4 535  ? 153.977 144.409 162.878 1.00 50.26  ? 532  LYS A CG    1 
ATOM   5148  C CD    . LYS D 4 535  ? 152.562 143.909 163.108 1.00 50.26  ? 532  LYS A CD    1 
ATOM   5149  C CE    . LYS D 4 535  ? 151.724 144.948 163.831 1.00 50.26  ? 532  LYS A CE    1 
ATOM   5150  N NZ    . LYS D 4 535  ? 150.326 144.484 164.035 1.00 50.26  ? 532  LYS A NZ    1 
ATOM   5151  N N     . LEU D 4 536  ? 155.849 147.429 163.625 1.00 50.26  ? 533  LEU A N     1 
ATOM   5152  C CA    . LEU D 4 536  ? 156.459 147.726 164.913 1.00 50.26  ? 533  LEU A CA    1 
ATOM   5153  C C     . LEU D 4 536  ? 155.431 147.521 166.016 1.00 50.26  ? 533  LEU A C     1 
ATOM   5154  O O     . LEU D 4 536  ? 154.321 148.058 165.943 1.00 50.26  ? 533  LEU A O     1 
ATOM   5155  C CB    . LEU D 4 536  ? 156.994 149.157 164.953 1.00 50.26  ? 533  LEU A CB    1 
ATOM   5156  C CG    . LEU D 4 536  ? 157.964 149.563 163.845 1.00 50.26  ? 533  LEU A CG    1 
ATOM   5157  C CD1   . LEU D 4 536  ? 158.330 151.029 163.979 1.00 50.26  ? 533  LEU A CD1   1 
ATOM   5158  C CD2   . LEU D 4 536  ? 159.207 148.696 163.878 1.00 50.26  ? 533  LEU A CD2   1 
ATOM   5159  N N     . ASN D 4 537  ? 155.805 146.749 167.033 1.00 50.26  ? 534  ASN A N     1 
ATOM   5160  C CA    . ASN D 4 537  ? 154.909 146.439 168.137 1.00 50.26  ? 534  ASN A CA    1 
ATOM   5161  C C     . ASN D 4 537  ? 155.281 147.122 169.441 1.00 50.26  ? 534  ASN A C     1 
ATOM   5162  O O     . ASN D 4 537  ? 154.403 147.325 170.280 1.00 50.26  ? 534  ASN A O     1 
ATOM   5163  C CB    . ASN D 4 537  ? 154.859 144.925 168.372 1.00 50.26  ? 534  ASN A CB    1 
ATOM   5164  C CG    . ASN D 4 537  ? 154.140 144.189 167.263 1.00 50.26  ? 534  ASN A CG    1 
ATOM   5165  O OD1   . ASN D 4 537  ? 154.768 143.650 166.353 1.00 50.26  ? 534  ASN A OD1   1 
ATOM   5166  N ND2   . ASN D 4 537  ? 152.816 144.162 167.333 1.00 50.26  ? 534  ASN A ND2   1 
ATOM   5167  N N     . PHE D 4 538  ? 156.553 147.476 169.634 1.00 50.26  ? 535  PHE A N     1 
ATOM   5168  C CA    . PHE D 4 538  ? 157.025 148.099 170.872 1.00 50.26  ? 535  PHE A CA    1 
ATOM   5169  C C     . PHE D 4 538  ? 156.714 147.234 172.090 1.00 50.26  ? 535  PHE A C     1 
ATOM   5170  O O     . PHE D 4 538  ? 156.464 147.751 173.181 1.00 50.26  ? 535  PHE A O     1 
ATOM   5171  C CB    . PHE D 4 538  ? 156.435 149.501 171.053 1.00 50.26  ? 535  PHE A CB    1 
ATOM   5172  C CG    . PHE D 4 538  ? 156.897 150.492 170.027 1.00 50.26  ? 535  PHE A CG    1 
ATOM   5173  C CD1   . PHE D 4 538  ? 156.270 150.579 168.797 1.00 50.26  ? 535  PHE A CD1   1 
ATOM   5174  C CD2   . PHE D 4 538  ? 157.955 151.341 170.294 1.00 50.26  ? 535  PHE A CD2   1 
ATOM   5175  C CE1   . PHE D 4 538  ? 156.693 151.491 167.852 1.00 50.26  ? 535  PHE A CE1   1 
ATOM   5176  C CE2   . PHE D 4 538  ? 158.382 152.255 169.353 1.00 50.26  ? 535  PHE A CE2   1 
ATOM   5177  C CZ    . PHE D 4 538  ? 157.750 152.330 168.131 1.00 50.26  ? 535  PHE A CZ    1 
ATOM   5178  N N     . GLN D 4 539  ? 156.729 145.912 171.907 1.00 50.26  ? 536  GLN A N     1 
ATOM   5179  C CA    . GLN D 4 539  ? 156.324 144.956 172.939 1.00 50.26  ? 536  GLN A CA    1 
ATOM   5180  C C     . GLN D 4 539  ? 154.901 145.220 173.422 1.00 50.26  ? 536  GLN A C     1 
ATOM   5181  O O     . GLN D 4 539  ? 154.548 144.896 174.558 1.00 50.26  ? 536  GLN A O     1 
ATOM   5182  C CB    . GLN D 4 539  ? 157.302 144.949 174.119 1.00 50.26  ? 536  GLN A CB    1 
ATOM   5183  C CG    . GLN D 4 539  ? 158.505 144.041 173.916 1.00 50.26  ? 536  GLN A CG    1 
ATOM   5184  C CD    . GLN D 4 539  ? 159.720 144.788 173.409 1.00 50.26  ? 536  GLN A CD    1 
ATOM   5185  O OE1   . GLN D 4 539  ? 159.776 146.014 173.466 1.00 50.26  ? 536  GLN A OE1   1 
ATOM   5186  N NE2   . GLN D 4 539  ? 160.702 144.049 172.905 1.00 50.26  ? 536  GLN A NE2   1 
ATOM   5187  N N     . MET D 4 540  ? 154.078 145.808 172.561 1.00 50.26  ? 537  MET A N     1 
ATOM   5188  C CA    . MET D 4 540  ? 152.674 146.053 172.862 1.00 50.26  ? 537  MET A CA    1 
ATOM   5189  C C     . MET D 4 540  ? 151.830 145.114 172.016 1.00 50.26  ? 537  MET A C     1 
ATOM   5190  O O     . MET D 4 540  ? 151.720 145.323 170.797 1.00 50.26  ? 537  MET A O     1 
ATOM   5191  C CB    . MET D 4 540  ? 152.306 147.509 172.573 1.00 50.26  ? 537  MET A CB    1 
ATOM   5192  C CG    . MET D 4 540  ? 153.272 148.523 173.161 1.00 50.26  ? 537  MET A CG    1 
ATOM   5193  S SD    . MET D 4 540  ? 152.458 150.035 173.698 1.00 50.26  ? 537  MET A SD    1 
ATOM   5194  C CE    . MET D 4 540  ? 151.736 149.497 175.237 1.00 50.26  ? 537  MET A CE    1 
ATOM   5195  N N     . PRO D 4 541  ? 151.234 144.071 172.595 1.00 50.26  ? 538  PRO A N     1 
ATOM   5196  C CA    . PRO D 4 541  ? 150.438 143.140 171.780 1.00 50.26  ? 538  PRO A CA    1 
ATOM   5197  C C     . PRO D 4 541  ? 149.282 143.803 171.053 1.00 50.26  ? 538  PRO A C     1 
ATOM   5198  O O     . PRO D 4 541  ? 148.937 143.382 169.942 1.00 50.26  ? 538  PRO A O     1 
ATOM   5199  C CB    . PRO D 4 541  ? 149.945 142.114 172.808 1.00 50.26  ? 538  PRO A CB    1 
ATOM   5200  C CG    . PRO D 4 541  ? 150.947 142.178 173.910 1.00 50.26  ? 538  PRO A CG    1 
ATOM   5201  C CD    . PRO D 4 541  ? 151.368 143.615 173.988 1.00 50.26  ? 538  PRO A CD    1 
ATOM   5202  N N     . THR D 4 542  ? 148.673 144.831 171.642 1.00 50.26  ? 539  THR A N     1 
ATOM   5203  C CA    . THR D 4 542  ? 147.532 145.492 171.023 1.00 50.26  ? 539  THR A CA    1 
ATOM   5204  C C     . THR D 4 542  ? 147.819 146.967 170.781 1.00 50.26  ? 539  THR A C     1 
ATOM   5205  O O     . THR D 4 542  ? 146.985 147.824 171.089 1.00 50.26  ? 539  THR A O     1 
ATOM   5206  C CB    . THR D 4 542  ? 146.284 145.336 171.894 1.00 50.26  ? 539  THR A CB    1 
ATOM   5207  O OG1   . THR D 4 542  ? 146.538 145.878 173.195 1.00 50.26  ? 539  THR A OG1   1 
ATOM   5208  C CG2   . THR D 4 542  ? 145.906 143.871 172.028 1.00 50.26  ? 539  THR A CG2   1 
ATOM   5209  N N     . LEU D 4 543  ? 148.997 147.274 170.240 1.00 50.26  ? 540  LEU A N     1 
ATOM   5210  C CA    . LEU D 4 543  ? 149.352 148.658 169.956 1.00 50.26  ? 540  LEU A CA    1 
ATOM   5211  C C     . LEU D 4 543  ? 148.407 149.251 168.921 1.00 50.26  ? 540  LEU A C     1 
ATOM   5212  O O     . LEU D 4 543  ? 148.181 148.664 167.859 1.00 50.26  ? 540  LEU A O     1 
ATOM   5213  C CB    . LEU D 4 543  ? 150.794 148.741 169.459 1.00 50.26  ? 540  LEU A CB    1 
ATOM   5214  C CG    . LEU D 4 543  ? 151.284 150.135 169.064 1.00 50.26  ? 540  LEU A CG    1 
ATOM   5215  C CD1   . LEU D 4 543  ? 151.603 150.960 170.295 1.00 50.26  ? 540  LEU A CD1   1 
ATOM   5216  C CD2   . LEU D 4 543  ? 152.495 150.040 168.154 1.00 50.26  ? 540  LEU A CD2   1 
ATOM   5217  N N     . ALA D 4 544  ? 147.854 150.422 169.243 1.00 50.26  ? 541  ALA A N     1 
ATOM   5218  C CA    . ALA D 4 544  ? 146.948 151.154 168.357 1.00 50.26  ? 541  ALA A CA    1 
ATOM   5219  C C     . ALA D 4 544  ? 145.734 150.320 167.958 1.00 50.26  ? 541  ALA A C     1 
ATOM   5220  O O     . ALA D 4 544  ? 145.136 150.543 166.904 1.00 50.26  ? 541  ALA A O     1 
ATOM   5221  C CB    . ALA D 4 544  ? 147.678 151.662 167.111 1.00 50.26  ? 541  ALA A CB    1 
ATOM   5222  N N     . SER D 4 545  ? 145.364 149.344 168.790 1.00 50.26  ? 542  SER A N     1 
ATOM   5223  C CA    . SER D 4 545  ? 144.172 148.552 168.506 1.00 50.26  ? 542  SER A CA    1 
ATOM   5224  C C     . SER D 4 545  ? 142.912 149.401 168.597 1.00 50.26  ? 542  SER A C     1 
ATOM   5225  O O     . SER D 4 545  ? 142.003 149.265 167.772 1.00 50.26  ? 542  SER A O     1 
ATOM   5226  C CB    . SER D 4 545  ? 144.089 147.366 169.465 1.00 50.26  ? 542  SER A CB    1 
ATOM   5227  O OG    . SER D 4 545  ? 142.776 146.837 169.501 1.00 50.26  ? 542  SER A OG    1 
ATOM   5228  N N     . GLY D 4 546  ? 142.842 150.274 169.590 1.00 50.26  ? 543  GLY A N     1 
ATOM   5229  C CA    . GLY D 4 546  ? 141.711 151.173 169.737 1.00 50.26  ? 543  GLY A CA    1 
ATOM   5230  C C     . GLY D 4 546  ? 142.169 152.484 170.329 1.00 50.26  ? 543  GLY A C     1 
ATOM   5231  O O     . GLY D 4 546  ? 143.127 152.533 171.105 1.00 50.26  ? 543  GLY A O     1 
ATOM   5232  N N     . TRP D 4 547  ? 141.478 153.557 169.958 1.00 50.26  ? 544  TRP A N     1 
ATOM   5233  C CA    . TRP D 4 547  ? 141.863 154.896 170.377 1.00 50.26  ? 544  TRP A CA    1 
ATOM   5234  C C     . TRP D 4 547  ? 141.165 155.354 171.649 1.00 50.26  ? 544  TRP A C     1 
ATOM   5235  O O     . TRP D 4 547  ? 141.435 156.466 172.112 1.00 50.26  ? 544  TRP A O     1 
ATOM   5236  C CB    . TRP D 4 547  ? 141.583 155.902 169.257 1.00 50.26  ? 544  TRP A CB    1 
ATOM   5237  C CG    . TRP D 4 547  ? 142.264 155.580 167.969 1.00 50.26  ? 544  TRP A CG    1 
ATOM   5238  C CD1   . TRP D 4 547  ? 141.674 155.160 166.815 1.00 50.26  ? 544  TRP A CD1   1 
ATOM   5239  C CD2   . TRP D 4 547  ? 143.667 155.644 167.703 1.00 50.26  ? 544  TRP A CD2   1 
ATOM   5240  N NE1   . TRP D 4 547  ? 142.623 154.965 165.843 1.00 50.26  ? 544  TRP A NE1   1 
ATOM   5241  C CE2   . TRP D 4 547  ? 143.856 155.253 166.364 1.00 50.26  ? 544  TRP A CE2   1 
ATOM   5242  C CE3   . TRP D 4 547  ? 144.783 155.994 168.466 1.00 50.26  ? 544  TRP A CE3   1 
ATOM   5243  C CZ2   . TRP D 4 547  ? 145.113 155.204 165.773 1.00 50.26  ? 544  TRP A CZ2   1 
ATOM   5244  C CZ3   . TRP D 4 547  ? 146.030 155.940 167.878 1.00 50.26  ? 544  TRP A CZ3   1 
ATOM   5245  C CH2   . TRP D 4 547  ? 146.185 155.552 166.544 1.00 50.26  ? 544  TRP A CH2   1 
ATOM   5246  N N     . ASP D 4 548  ? 140.294 154.530 172.227 1.00 50.26  ? 545  ASP A N     1 
ATOM   5247  C CA    . ASP D 4 548  ? 139.495 154.958 173.368 1.00 50.26  ? 545  ASP A CA    1 
ATOM   5248  C C     . ASP D 4 548  ? 140.386 155.341 174.544 1.00 50.26  ? 545  ASP A C     1 
ATOM   5249  O O     . ASP D 4 548  ? 141.428 154.726 174.785 1.00 50.26  ? 545  ASP A O     1 
ATOM   5250  C CB    . ASP D 4 548  ? 138.529 153.850 173.779 1.00 50.26  ? 545  ASP A CB    1 
ATOM   5251  C CG    . ASP D 4 548  ? 137.384 154.359 174.630 1.00 50.26  ? 545  ASP A CG    1 
ATOM   5252  O OD1   . ASP D 4 548  ? 137.636 155.125 175.582 1.00 50.26  ? 545  ASP A OD1   1 
ATOM   5253  O OD2   . ASP D 4 548  ? 136.226 153.988 174.348 1.00 50.26  ? 545  ASP A OD2   1 
ATOM   5254  N N     . VAL D 4 549  ? 139.963 156.373 175.277 1.00 50.26  ? 546  VAL A N     1 
ATOM   5255  C CA    . VAL D 4 549  ? 140.775 156.900 176.370 1.00 50.26  ? 546  VAL A CA    1 
ATOM   5256  C C     . VAL D 4 549  ? 140.894 155.881 177.497 1.00 50.26  ? 546  VAL A C     1 
ATOM   5257  O O     . VAL D 4 549  ? 141.932 155.792 178.163 1.00 50.26  ? 546  VAL A O     1 
ATOM   5258  C CB    . VAL D 4 549  ? 140.199 158.241 176.862 1.00 50.26  ? 546  VAL A CB    1 
ATOM   5259  C CG1   . VAL D 4 549  ? 138.758 158.078 177.316 1.00 50.26  ? 546  VAL A CG1   1 
ATOM   5260  C CG2   . VAL D 4 549  ? 141.058 158.817 177.976 1.00 50.26  ? 546  VAL A CG2   1 
ATOM   5261  N N     . ASN D 4 550  ? 139.838 155.103 177.740 1.00 50.26  ? 547  ASN A N     1 
ATOM   5262  C CA    . ASN D 4 550  ? 139.911 154.077 178.774 1.00 50.26  ? 547  ASN A CA    1 
ATOM   5263  C C     . ASN D 4 550  ? 140.922 152.997 178.412 1.00 50.26  ? 547  ASN A C     1 
ATOM   5264  O O     . ASN D 4 550  ? 141.680 152.531 179.270 1.00 50.26  ? 547  ASN A O     1 
ATOM   5265  C CB    . ASN D 4 550  ? 138.531 153.469 179.007 1.00 50.26  ? 547  ASN A CB    1 
ATOM   5266  C CG    . ASN D 4 550  ? 137.640 154.356 179.847 1.00 50.26  ? 547  ASN A CG    1 
ATOM   5267  O OD1   . ASN D 4 550  ? 138.108 155.296 180.488 1.00 50.26  ? 547  ASN A OD1   1 
ATOM   5268  N ND2   . ASN D 4 550  ? 136.346 154.061 179.850 1.00 50.26  ? 547  ASN A ND2   1 
ATOM   5269  N N     . LYS D 4 551  ? 140.953 152.590 177.145 1.00 50.26  ? 548  LYS A N     1 
ATOM   5270  C CA    . LYS D 4 551  ? 141.906 151.602 176.662 1.00 50.26  ? 548  LYS A CA    1 
ATOM   5271  C C     . LYS D 4 551  ? 143.213 152.232 176.204 1.00 50.26  ? 548  LYS A C     1 
ATOM   5272  O O     . LYS D 4 551  ? 144.054 151.538 175.625 1.00 50.26  ? 548  LYS A O     1 
ATOM   5273  C CB    . LYS D 4 551  ? 141.291 150.788 175.523 1.00 50.26  ? 548  LYS A CB    1 
ATOM   5274  C CG    . LYS D 4 551  ? 139.885 150.296 175.809 1.00 50.26  ? 548  LYS A CG    1 
ATOM   5275  C CD    . LYS D 4 551  ? 139.862 149.363 177.005 1.00 50.26  ? 548  LYS A CD    1 
ATOM   5276  C CE    . LYS D 4 551  ? 140.579 148.062 176.702 1.00 50.26  ? 548  LYS A CE    1 
ATOM   5277  N NZ    . LYS D 4 551  ? 140.134 147.478 175.410 1.00 50.26  ? 548  LYS A NZ    1 
ATOM   5278  N N     . GLU D 4 552  ? 143.390 153.532 176.444 1.00 50.26  ? 549  GLU A N     1 
ATOM   5279  C CA    . GLU D 4 552  ? 144.628 154.207 176.071 1.00 50.26  ? 549  GLU A CA    1 
ATOM   5280  C C     . GLU D 4 552  ? 145.828 153.601 176.787 1.00 50.26  ? 549  GLU A C     1 
ATOM   5281  O O     . GLU D 4 552  ? 146.886 153.402 176.181 1.00 50.26  ? 549  GLU A O     1 
ATOM   5282  C CB    . GLU D 4 552  ? 144.509 155.695 176.389 1.00 50.26  ? 549  GLU A CB    1 
ATOM   5283  C CG    . GLU D 4 552  ? 145.812 156.459 176.411 1.00 50.26  ? 549  GLU A CG    1 
ATOM   5284  C CD    . GLU D 4 552  ? 145.589 157.952 176.530 1.00 50.26  ? 549  GLU A CD    1 
ATOM   5285  O OE1   . GLU D 4 552  ? 144.425 158.389 176.419 1.00 50.26  ? 549  GLU A OE1   1 
ATOM   5286  O OE2   . GLU D 4 552  ? 146.575 158.689 176.737 1.00 50.26  ? 549  GLU A OE2   1 
ATOM   5287  N N     . LYS D 4 553  ? 145.684 153.308 178.080 1.00 50.26  ? 550  LYS A N     1 
ATOM   5288  C CA    . LYS D 4 553  ? 146.785 152.715 178.830 1.00 50.26  ? 550  LYS A CA    1 
ATOM   5289  C C     . LYS D 4 553  ? 147.131 151.326 178.305 1.00 50.26  ? 550  LYS A C     1 
ATOM   5290  O O     . LYS D 4 553  ? 148.311 150.983 178.169 1.00 50.26  ? 550  LYS A O     1 
ATOM   5291  C CB    . LYS D 4 553  ? 146.430 152.658 180.316 1.00 50.26  ? 550  LYS A CB    1 
ATOM   5292  C CG    . LYS D 4 553  ? 147.503 152.042 181.196 1.00 50.26  ? 550  LYS A CG    1 
ATOM   5293  C CD    . LYS D 4 553  ? 147.079 150.679 181.718 1.00 50.26  ? 550  LYS A CD    1 
ATOM   5294  C CE    . LYS D 4 553  ? 148.105 150.118 182.687 1.00 50.26  ? 550  LYS A CE    1 
ATOM   5295  N NZ    . LYS D 4 553  ? 147.837 148.692 183.017 1.00 50.26  ? 550  LYS A NZ    1 
ATOM   5296  N N     . CYS D 4 554  ? 146.116 150.514 178.003 1.00 50.26  ? 551  CYS A N     1 
ATOM   5297  C CA    . CYS D 4 554  ? 146.362 149.144 177.567 1.00 50.26  ? 551  CYS A CA    1 
ATOM   5298  C C     . CYS D 4 554  ? 146.869 149.077 176.131 1.00 50.26  ? 551  CYS A C     1 
ATOM   5299  O O     . CYS D 4 554  ? 147.571 148.125 175.775 1.00 50.26  ? 551  CYS A O     1 
ATOM   5300  C CB    . CYS D 4 554  ? 145.088 148.308 177.730 1.00 37.31  ? 551  CYS A CB    1 
ATOM   5301  S SG    . CYS D 4 554  ? 144.232 148.591 179.308 1.00 37.31  ? 551  CYS A SG    1 
ATOM   5302  N N     . ASN D 4 555  ? 146.534 150.062 175.297 1.00 50.26  ? 552  ASN A N     1 
ATOM   5303  C CA    . ASN D 4 555  ? 147.004 150.100 173.916 1.00 50.26  ? 552  ASN A CA    1 
ATOM   5304  C C     . ASN D 4 555  ? 148.206 151.012 173.714 1.00 50.26  ? 552  ASN A C     1 
ATOM   5305  O O     . ASN D 4 555  ? 149.132 150.651 172.984 1.00 50.26  ? 552  ASN A O     1 
ATOM   5306  C CB    . ASN D 4 555  ? 145.877 150.543 172.978 1.00 50.26  ? 552  ASN A CB    1 
ATOM   5307  C CG    . ASN D 4 555  ? 144.685 149.615 173.023 1.00 50.26  ? 552  ASN A CG    1 
ATOM   5308  O OD1   . ASN D 4 555  ? 143.550 150.054 173.201 1.00 50.26  ? 552  ASN A OD1   1 
ATOM   5309  N ND2   . ASN D 4 555  ? 144.935 148.324 172.855 1.00 50.26  ? 552  ASN A ND2   1 
ATOM   5310  N N     . GLY D 4 556  ? 148.214 152.187 174.336 1.00 50.26  ? 553  GLY A N     1 
ATOM   5311  C CA    . GLY D 4 556  ? 149.345 153.087 174.227 1.00 50.26  ? 553  GLY A CA    1 
ATOM   5312  C C     . GLY D 4 556  ? 149.492 153.737 172.867 1.00 50.26  ? 553  GLY A C     1 
ATOM   5313  O O     . GLY D 4 556  ? 150.508 153.545 172.195 1.00 50.26  ? 553  GLY A O     1 
ATOM   5314  N N     . ALA D 4 557  ? 148.488 154.506 172.449 1.00 50.26  ? 554  ALA A N     1 
ATOM   5315  C CA    . ALA D 4 557  ? 148.549 155.226 171.183 1.00 50.26  ? 554  ALA A CA    1 
ATOM   5316  C C     . ALA D 4 557  ? 147.520 156.346 171.200 1.00 50.26  ? 554  ALA A C     1 
ATOM   5317  O O     . ALA D 4 557  ? 146.333 156.093 171.421 1.00 50.26  ? 554  ALA A O     1 
ATOM   5318  C CB    . ALA D 4 557  ? 148.298 154.289 169.999 1.00 50.26  ? 554  ALA A CB    1 
ATOM   5319  N N     . ILE D 4 558  ? 147.978 157.578 170.966 1.00 50.26  ? 555  ILE A N     1 
ATOM   5320  C CA    . ILE D 4 558  ? 147.117 158.754 170.987 1.00 50.26  ? 555  ILE A CA    1 
ATOM   5321  C C     . ILE D 4 558  ? 147.493 159.678 169.838 1.00 50.26  ? 555  ILE A C     1 
ATOM   5322  O O     . ILE D 4 558  ? 148.562 159.560 169.238 1.00 50.26  ? 555  ILE A O     1 
ATOM   5323  C CB    . ILE D 4 558  ? 147.205 159.518 172.324 1.00 50.26  ? 555  ILE A CB    1 
ATOM   5324  C CG1   . ILE D 4 558  ? 148.667 159.698 172.736 1.00 50.26  ? 555  ILE A CG1   1 
ATOM   5325  C CG2   . ILE D 4 558  ? 146.430 158.794 173.395 1.00 50.26  ? 555  ILE A CG2   1 
ATOM   5326  C CD1   . ILE D 4 558  ? 148.847 160.427 174.043 1.00 50.26  ? 555  ILE A CD1   1 
ATOM   5327  N N     . LEU D 4 559  ? 146.593 160.613 169.543 1.00 50.26  ? 556  LEU A N     1 
ATOM   5328  C CA    . LEU D 4 559  ? 146.808 161.615 168.511 1.00 50.26  ? 556  LEU A CA    1 
ATOM   5329  C C     . LEU D 4 559  ? 146.822 163.008 169.123 1.00 50.26  ? 556  LEU A C     1 
ATOM   5330  O O     . LEU D 4 559  ? 146.159 163.271 170.129 1.00 50.26  ? 556  LEU A O     1 
ATOM   5331  C CB    . LEU D 4 559  ? 145.733 161.563 167.419 1.00 50.26  ? 556  LEU A CB    1 
ATOM   5332  C CG    . LEU D 4 559  ? 145.817 160.483 166.343 1.00 50.26  ? 556  LEU A CG    1 
ATOM   5333  C CD1   . LEU D 4 559  ? 145.475 159.129 166.904 1.00 50.26  ? 556  LEU A CD1   1 
ATOM   5334  C CD2   . LEU D 4 559  ? 144.898 160.825 165.192 1.00 50.26  ? 556  LEU A CD2   1 
ATOM   5335  N N     . PHE D 4 560  ? 147.585 163.894 168.498 1.00 50.26  ? 557  PHE A N     1 
ATOM   5336  C CA    . PHE D 4 560  ? 147.658 165.299 168.858 1.00 50.26  ? 557  PHE A CA    1 
ATOM   5337  C C     . PHE D 4 560  ? 147.374 166.148 167.625 1.00 50.26  ? 557  PHE A C     1 
ATOM   5338  O O     . PHE D 4 560  ? 147.248 165.641 166.508 1.00 50.26  ? 557  PHE A O     1 
ATOM   5339  C CB    . PHE D 4 560  ? 149.029 165.647 169.445 1.00 50.26  ? 557  PHE A CB    1 
ATOM   5340  C CG    . PHE D 4 560  ? 149.318 164.977 170.754 1.00 50.26  ? 557  PHE A CG    1 
ATOM   5341  C CD1   . PHE D 4 560  ? 148.811 165.489 171.933 1.00 50.26  ? 557  PHE A CD1   1 
ATOM   5342  C CD2   . PHE D 4 560  ? 150.104 163.842 170.806 1.00 50.26  ? 557  PHE A CD2   1 
ATOM   5343  C CE1   . PHE D 4 560  ? 149.077 164.879 173.138 1.00 50.26  ? 557  PHE A CE1   1 
ATOM   5344  C CE2   . PHE D 4 560  ? 150.373 163.228 172.009 1.00 50.26  ? 557  PHE A CE2   1 
ATOM   5345  C CZ    . PHE D 4 560  ? 149.859 163.748 173.176 1.00 50.26  ? 557  PHE A CZ    1 
ATOM   5346  N N     . VAL D 4 561  ? 147.268 167.456 167.839 1.00 50.26  ? 558  VAL A N     1 
ATOM   5347  C CA    . VAL D 4 561  ? 147.177 168.413 166.743 1.00 50.26  ? 558  VAL A CA    1 
ATOM   5348  C C     . VAL D 4 561  ? 147.650 169.769 167.250 1.00 50.26  ? 558  VAL A C     1 
ATOM   5349  O O     . VAL D 4 561  ? 147.252 170.217 168.331 1.00 50.26  ? 558  VAL A O     1 
ATOM   5350  C CB    . VAL D 4 561  ? 145.752 168.478 166.161 1.00 50.26  ? 558  VAL A CB    1 
ATOM   5351  C CG1   . VAL D 4 561  ? 144.734 168.761 167.246 1.00 50.26  ? 558  VAL A CG1   1 
ATOM   5352  C CG2   . VAL D 4 561  ? 145.672 169.527 165.067 1.00 50.26  ? 558  VAL A CG2   1 
ATOM   5353  N N     . LYS D 4 562  ? 148.521 170.419 166.484 1.00 50.26  ? 559  LYS A N     1 
ATOM   5354  C CA    . LYS D 4 562  ? 149.132 171.674 166.909 1.00 50.26  ? 559  LYS A CA    1 
ATOM   5355  C C     . LYS D 4 562  ? 149.453 172.501 165.677 1.00 50.26  ? 559  LYS A C     1 
ATOM   5356  O O     . LYS D 4 562  ? 150.258 172.076 164.842 1.00 50.26  ? 559  LYS A O     1 
ATOM   5357  C CB    . LYS D 4 562  ? 150.396 171.415 167.727 1.00 50.26  ? 559  LYS A CB    1 
ATOM   5358  C CG    . LYS D 4 562  ? 151.146 172.670 168.128 1.00 50.26  ? 559  LYS A CG    1 
ATOM   5359  C CD    . LYS D 4 562  ? 152.422 172.327 168.873 1.00 50.26  ? 559  LYS A CD    1 
ATOM   5360  C CE    . LYS D 4 562  ? 153.070 173.568 169.456 1.00 50.26  ? 559  LYS A CE    1 
ATOM   5361  N NZ    . LYS D 4 562  ? 154.436 173.279 169.969 1.00 50.26  ? 559  LYS A NZ    1 
ATOM   5362  N N     . ASN D 4 563  ? 148.828 173.675 165.570 1.00 50.26  ? 560  ASN A N     1 
ATOM   5363  C CA    . ASN D 4 563  ? 149.052 174.592 164.452 1.00 50.26  ? 560  ASN A CA    1 
ATOM   5364  C C     . ASN D 4 563  ? 148.801 173.905 163.112 1.00 50.26  ? 560  ASN A C     1 
ATOM   5365  O O     . ASN D 4 563  ? 149.523 174.121 162.137 1.00 50.26  ? 560  ASN A O     1 
ATOM   5366  C CB    . ASN D 4 563  ? 150.459 175.189 164.501 1.00 50.26  ? 560  ASN A CB    1 
ATOM   5367  C CG    . ASN D 4 563  ? 150.734 175.926 165.795 1.00 50.26  ? 560  ASN A CG    1 
ATOM   5368  O OD1   . ASN D 4 563  ? 149.815 176.230 166.555 1.00 50.26  ? 560  ASN A OD1   1 
ATOM   5369  N ND2   . ASN D 4 563  ? 152.003 176.217 166.054 1.00 50.26  ? 560  ASN A ND2   1 
ATOM   5370  N N     . GLY D 4 564  ? 147.768 173.068 163.063 1.00 50.26  ? 561  GLY A N     1 
ATOM   5371  C CA    . GLY D 4 564  ? 147.427 172.361 161.847 1.00 50.26  ? 561  GLY A CA    1 
ATOM   5372  C C     . GLY D 4 564  ? 148.292 171.164 161.533 1.00 50.26  ? 561  GLY A C     1 
ATOM   5373  O O     . GLY D 4 564  ? 148.177 170.610 160.434 1.00 50.26  ? 561  GLY A O     1 
ATOM   5374  N N     . LEU D 4 565  ? 149.156 170.748 162.453 1.00 50.26  ? 562  LEU A N     1 
ATOM   5375  C CA    . LEU D 4 565  ? 150.017 169.589 162.265 1.00 50.26  ? 562  LEU A CA    1 
ATOM   5376  C C     . LEU D 4 565  ? 149.595 168.493 163.233 1.00 50.26  ? 562  LEU A C     1 
ATOM   5377  O O     . LEU D 4 565  ? 149.499 168.730 164.441 1.00 50.26  ? 562  LEU A O     1 
ATOM   5378  C CB    . LEU D 4 565  ? 151.486 169.954 162.482 1.00 50.26  ? 562  LEU A CB    1 
ATOM   5379  C CG    . LEU D 4 565  ? 152.303 170.280 161.232 1.00 50.26  ? 562  LEU A CG    1 
ATOM   5380  C CD1   . LEU D 4 565  ? 151.672 171.417 160.449 1.00 50.26  ? 562  LEU A CD1   1 
ATOM   5381  C CD2   . LEU D 4 565  ? 153.734 170.617 161.610 1.00 50.26  ? 562  LEU A CD2   1 
ATOM   5382  N N     . TYR D 4 566  ? 149.351 167.300 162.703 1.00 50.26  ? 563  TYR A N     1 
ATOM   5383  C CA    . TYR D 4 566  ? 148.853 166.181 163.489 1.00 50.26  ? 563  TYR A CA    1 
ATOM   5384  C C     . TYR D 4 566  ? 150.017 165.312 163.940 1.00 50.26  ? 563  TYR A C     1 
ATOM   5385  O O     . TYR D 4 566  ? 150.836 164.887 163.119 1.00 50.26  ? 563  TYR A O     1 
ATOM   5386  C CB    . TYR D 4 566  ? 147.851 165.355 162.683 1.00 50.26  ? 563  TYR A CB    1 
ATOM   5387  C CG    . TYR D 4 566  ? 146.658 166.152 162.213 1.00 50.26  ? 563  TYR A CG    1 
ATOM   5388  C CD1   . TYR D 4 566  ? 146.692 166.849 161.014 1.00 50.26  ? 563  TYR A CD1   1 
ATOM   5389  C CD2   . TYR D 4 566  ? 145.501 166.217 162.975 1.00 50.26  ? 563  TYR A CD2   1 
ATOM   5390  C CE1   . TYR D 4 566  ? 145.606 167.582 160.585 1.00 50.26  ? 563  TYR A CE1   1 
ATOM   5391  C CE2   . TYR D 4 566  ? 144.410 166.948 162.553 1.00 50.26  ? 563  TYR A CE2   1 
ATOM   5392  C CZ    . TYR D 4 566  ? 144.468 167.628 161.358 1.00 50.26  ? 563  TYR A CZ    1 
ATOM   5393  O OH    . TYR D 4 566  ? 143.383 168.358 160.936 1.00 50.26  ? 563  TYR A OH    1 
ATOM   5394  N N     . TYR D 4 567  ? 150.085 165.051 165.242 1.00 50.26  ? 564  TYR A N     1 
ATOM   5395  C CA    . TYR D 4 567  ? 151.151 164.262 165.839 1.00 50.26  ? 564  TYR A CA    1 
ATOM   5396  C C     . TYR D 4 567  ? 150.581 162.980 166.425 1.00 50.26  ? 564  TYR A C     1 
ATOM   5397  O O     . TYR D 4 567  ? 149.545 162.999 167.094 1.00 50.26  ? 564  TYR A O     1 
ATOM   5398  C CB    . TYR D 4 567  ? 151.877 165.049 166.931 1.00 50.26  ? 564  TYR A CB    1 
ATOM   5399  C CG    . TYR D 4 567  ? 152.590 166.283 166.435 1.00 50.26  ? 564  TYR A CG    1 
ATOM   5400  C CD1   . TYR D 4 567  ? 151.916 167.484 166.288 1.00 50.26  ? 564  TYR A CD1   1 
ATOM   5401  C CD2   . TYR D 4 567  ? 153.939 166.247 166.120 1.00 50.26  ? 564  TYR A CD2   1 
ATOM   5402  C CE1   . TYR D 4 567  ? 152.564 168.614 165.837 1.00 50.26  ? 564  TYR A CE1   1 
ATOM   5403  C CE2   . TYR D 4 567  ? 154.595 167.370 165.669 1.00 50.26  ? 564  TYR A CE2   1 
ATOM   5404  C CZ    . TYR D 4 567  ? 153.903 168.551 165.529 1.00 50.26  ? 564  TYR A CZ    1 
ATOM   5405  O OH    . TYR D 4 567  ? 154.553 169.676 165.079 1.00 50.26  ? 564  TYR A OH    1 
ATOM   5406  N N     . LEU D 4 568  ? 151.265 161.870 166.173 1.00 50.26  ? 565  LEU A N     1 
ATOM   5407  C CA    . LEU D 4 568  ? 150.904 160.578 166.741 1.00 50.26  ? 565  LEU A CA    1 
ATOM   5408  C C     . LEU D 4 568  ? 151.854 160.270 167.890 1.00 50.26  ? 565  LEU A C     1 
ATOM   5409  O O     . LEU D 4 568  ? 153.075 160.281 167.709 1.00 50.26  ? 565  LEU A O     1 
ATOM   5410  C CB    . LEU D 4 568  ? 150.966 159.476 165.685 1.00 50.26  ? 565  LEU A CB    1 
ATOM   5411  C CG    . LEU D 4 568  ? 151.090 158.047 166.218 1.00 50.26  ? 565  LEU A CG    1 
ATOM   5412  C CD1   . LEU D 4 568  ? 149.823 157.626 166.938 1.00 50.26  ? 565  LEU A CD1   1 
ATOM   5413  C CD2   . LEU D 4 568  ? 151.411 157.079 165.098 1.00 50.26  ? 565  LEU A CD2   1 
ATOM   5414  N N     . GLY D 4 569  ? 151.297 160.002 169.059 1.00 50.26  ? 566  GLY A N     1 
ATOM   5415  C CA    . GLY D 4 569  ? 152.084 159.666 170.235 1.00 50.26  ? 566  GLY A CA    1 
ATOM   5416  C C     . GLY D 4 569  ? 151.718 158.290 170.753 1.00 50.26  ? 566  GLY A C     1 
ATOM   5417  O O     . GLY D 4 569  ? 150.540 157.937 170.817 1.00 50.26  ? 566  GLY A O     1 
ATOM   5418  N N     . ILE D 4 570  ? 152.737 157.514 171.112 1.00 50.26  ? 567  ILE A N     1 
ATOM   5419  C CA    . ILE D 4 570  ? 152.554 156.191 171.695 1.00 50.26  ? 567  ILE A CA    1 
ATOM   5420  C C     . ILE D 4 570  ? 153.368 156.117 172.979 1.00 50.26  ? 567  ILE A C     1 
ATOM   5421  O O     . ILE D 4 570  ? 154.461 156.686 173.069 1.00 50.26  ? 567  ILE A O     1 
ATOM   5422  C CB    . ILE D 4 570  ? 152.951 155.062 170.716 1.00 50.26  ? 567  ILE A CB    1 
ATOM   5423  C CG1   . ILE D 4 570  ? 154.468 154.947 170.589 1.00 50.26  ? 567  ILE A CG1   1 
ATOM   5424  C CG2   . ILE D 4 570  ? 152.321 155.281 169.349 1.00 50.26  ? 567  ILE A CG2   1 
ATOM   5425  C CD1   . ILE D 4 570  ? 154.904 154.016 169.493 1.00 50.26  ? 567  ILE A CD1   1 
ATOM   5426  N N     . MET D 4 571  ? 152.815 155.449 173.987 1.00 50.26  ? 568  MET A N     1 
ATOM   5427  C CA    . MET D 4 571  ? 153.490 155.310 175.271 1.00 50.26  ? 568  MET A CA    1 
ATOM   5428  C C     . MET D 4 571  ? 153.939 153.870 175.465 1.00 50.26  ? 568  MET A C     1 
ATOM   5429  O O     . MET D 4 571  ? 153.092 152.987 175.673 1.00 50.26  ? 568  MET A O     1 
ATOM   5430  C CB    . MET D 4 571  ? 152.571 155.741 176.414 1.00 50.26  ? 568  MET A CB    1 
ATOM   5431  C CG    . MET D 4 571  ? 152.088 157.173 176.307 1.00 50.26  ? 568  MET A CG    1 
ATOM   5432  S SD    . MET D 4 571  ? 150.473 157.299 175.525 1.00 50.26  ? 568  MET A SD    1 
ATOM   5433  C CE    . MET D 4 571  ? 149.409 157.108 176.950 1.00 50.26  ? 568  MET A CE    1 
ATOM   5434  N N     . PRO D 4 572  ? 155.233 153.583 175.411 1.00 50.26  ? 569  PRO A N     1 
ATOM   5435  C CA    . PRO D 4 572  ? 155.703 152.208 175.595 1.00 50.26  ? 569  PRO A CA    1 
ATOM   5436  C C     . PRO D 4 572  ? 155.667 151.799 177.061 1.00 50.26  ? 569  PRO A C     1 
ATOM   5437  O O     . PRO D 4 572  ? 155.511 152.619 177.966 1.00 50.26  ? 569  PRO A O     1 
ATOM   5438  C CB    . PRO D 4 572  ? 157.139 152.264 175.074 1.00 50.26  ? 569  PRO A CB    1 
ATOM   5439  C CG    . PRO D 4 572  ? 157.567 153.658 175.375 1.00 50.26  ? 569  PRO A CG    1 
ATOM   5440  C CD    . PRO D 4 572  ? 156.346 154.520 175.181 1.00 50.26  ? 569  PRO A CD    1 
ATOM   5441  N N     . LYS D 4 573  ? 155.810 150.495 177.279 1.00 55.07  ? 570  LYS A N     1 
ATOM   5442  C CA    . LYS D 4 573  ? 155.897 149.968 178.634 1.00 55.07  ? 570  LYS A CA    1 
ATOM   5443  C C     . LYS D 4 573  ? 157.144 150.507 179.322 1.00 55.07  ? 570  LYS A C     1 
ATOM   5444  O O     . LYS D 4 573  ? 158.227 150.544 178.731 1.00 55.07  ? 570  LYS A O     1 
ATOM   5445  C CB    . LYS D 4 573  ? 155.921 148.441 178.603 1.00 55.07  ? 570  LYS A CB    1 
ATOM   5446  C CG    . LYS D 4 573  ? 154.796 147.827 177.789 1.00 55.07  ? 570  LYS A CG    1 
ATOM   5447  C CD    . LYS D 4 573  ? 155.058 146.363 177.487 1.00 55.07  ? 570  LYS A CD    1 
ATOM   5448  C CE    . LYS D 4 573  ? 154.824 145.500 178.711 1.00 55.07  ? 570  LYS A CE    1 
ATOM   5449  N NZ    . LYS D 4 573  ? 154.985 144.053 178.403 1.00 55.07  ? 570  LYS A NZ    1 
ATOM   5450  N N     . GLN D 4 574  ? 156.991 150.928 180.574 1.00 64.07  ? 571  GLN A N     1 
ATOM   5451  C CA    . GLN D 4 574  ? 158.072 151.573 181.312 1.00 64.07  ? 571  GLN A CA    1 
ATOM   5452  C C     . GLN D 4 574  ? 158.867 150.516 182.069 1.00 64.07  ? 571  GLN A C     1 
ATOM   5453  O O     . GLN D 4 574  ? 158.362 149.915 183.024 1.00 64.07  ? 571  GLN A O     1 
ATOM   5454  C CB    . GLN D 4 574  ? 157.518 152.631 182.261 1.00 64.07  ? 571  GLN A CB    1 
ATOM   5455  C CG    . GLN D 4 574  ? 157.176 153.943 181.579 1.00 64.07  ? 571  GLN A CG    1 
ATOM   5456  C CD    . GLN D 4 574  ? 158.403 154.762 181.231 1.00 64.07  ? 571  GLN A CD    1 
ATOM   5457  O OE1   . GLN D 4 574  ? 159.533 154.365 181.516 1.00 64.07  ? 571  GLN A OE1   1 
ATOM   5458  N NE2   . GLN D 4 574  ? 158.186 155.910 180.605 1.00 64.07  ? 571  GLN A NE2   1 
ATOM   5459  N N     . LYS D 4 575  ? 160.114 150.301 181.644 1.00 73.69  ? 572  LYS A N     1 
ATOM   5460  C CA    . LYS D 4 575  ? 161.028 149.356 182.287 1.00 73.69  ? 572  LYS A CA    1 
ATOM   5461  C C     . LYS D 4 575  ? 160.402 147.969 182.408 1.00 73.69  ? 572  LYS A C     1 
ATOM   5462  O O     . LYS D 4 575  ? 160.535 147.287 183.426 1.00 73.69  ? 572  LYS A O     1 
ATOM   5463  C CB    . LYS D 4 575  ? 161.478 149.873 183.656 1.00 73.69  ? 572  LYS A CB    1 
ATOM   5464  C CG    . LYS D 4 575  ? 162.120 151.254 183.625 1.00 73.69  ? 572  LYS A CG    1 
ATOM   5465  C CD    . LYS D 4 575  ? 163.227 151.347 182.583 1.00 73.69  ? 572  LYS A CD    1 
ATOM   5466  C CE    . LYS D 4 575  ? 164.369 150.387 182.882 1.00 73.69  ? 572  LYS A CE    1 
ATOM   5467  N NZ    . LYS D 4 575  ? 165.340 150.317 181.755 1.00 73.69  ? 572  LYS A NZ    1 
ATOM   5468  N N     . GLY D 4 576  ? 159.706 147.549 181.355 1.00 75.64  ? 573  GLY A N     1 
ATOM   5469  C CA    . GLY D 4 576  ? 159.030 146.271 181.350 1.00 75.64  ? 573  GLY A CA    1 
ATOM   5470  C C     . GLY D 4 576  ? 157.700 146.250 182.068 1.00 75.64  ? 573  GLY A C     1 
ATOM   5471  O O     . GLY D 4 576  ? 157.057 145.194 182.112 1.00 75.64  ? 573  GLY A O     1 
ATOM   5472  N N     . ARG D 4 577  ? 157.266 147.376 182.626 1.00 73.85  ? 574  ARG A N     1 
ATOM   5473  C CA    . ARG D 4 577  ? 156.003 147.475 183.337 1.00 73.85  ? 574  ARG A CA    1 
ATOM   5474  C C     . ARG D 4 577  ? 155.128 148.533 182.680 1.00 73.85  ? 574  ARG A C     1 
ATOM   5475  O O     . ARG D 4 577  ? 155.603 149.375 181.913 1.00 73.85  ? 574  ARG A O     1 
ATOM   5476  C CB    . ARG D 4 577  ? 156.219 147.816 184.817 1.00 73.85  ? 574  ARG A CB    1 
ATOM   5477  C CG    . ARG D 4 577  ? 157.102 146.826 185.561 1.00 73.85  ? 574  ARG A CG    1 
ATOM   5478  C CD    . ARG D 4 577  ? 157.291 147.232 187.018 1.00 73.85  ? 574  ARG A CD    1 
ATOM   5479  N NE    . ARG D 4 577  ? 157.516 148.665 187.179 1.00 73.85  ? 574  ARG A NE    1 
ATOM   5480  C CZ    . ARG D 4 577  ? 158.609 149.309 186.789 1.00 73.85  ? 574  ARG A CZ    1 
ATOM   5481  N NH1   . ARG D 4 577  ? 159.620 148.674 186.217 1.00 73.85  ? 574  ARG A NH1   1 
ATOM   5482  N NH2   . ARG D 4 577  ? 158.692 150.622 186.982 1.00 73.85  ? 574  ARG A NH2   1 
ATOM   5483  N N     . TYR D 4 578  ? 153.837 148.481 182.991 1.00 67.74  ? 575  TYR A N     1 
ATOM   5484  C CA    . TYR D 4 578  ? 152.860 149.398 182.413 1.00 67.74  ? 575  TYR A CA    1 
ATOM   5485  C C     . TYR D 4 578  ? 152.697 150.603 183.331 1.00 67.74  ? 575  TYR A C     1 
ATOM   5486  O O     . TYR D 4 578  ? 152.160 150.484 184.437 1.00 67.74  ? 575  TYR A O     1 
ATOM   5487  C CB    . TYR D 4 578  ? 151.527 148.692 182.191 1.00 67.74  ? 575  TYR A CB    1 
ATOM   5488  C CG    . TYR D 4 578  ? 151.365 148.139 180.797 1.00 67.74  ? 575  TYR A CG    1 
ATOM   5489  C CD1   . TYR D 4 578  ? 151.405 148.975 179.693 1.00 67.74  ? 575  TYR A CD1   1 
ATOM   5490  C CD2   . TYR D 4 578  ? 151.178 146.783 180.583 1.00 67.74  ? 575  TYR A CD2   1 
ATOM   5491  C CE1   . TYR D 4 578  ? 151.259 148.475 178.419 1.00 67.74  ? 575  TYR A CE1   1 
ATOM   5492  C CE2   . TYR D 4 578  ? 151.032 146.273 179.310 1.00 67.74  ? 575  TYR A CE2   1 
ATOM   5493  C CZ    . TYR D 4 578  ? 151.074 147.125 178.231 1.00 67.74  ? 575  TYR A CZ    1 
ATOM   5494  O OH    . TYR D 4 578  ? 150.928 146.623 176.959 1.00 67.74  ? 575  TYR A OH    1 
ATOM   5495  N N     . LYS D 4 579  ? 153.161 151.760 182.872 1.00 66.46  ? 576  LYS A N     1 
ATOM   5496  C CA    . LYS D 4 579  ? 152.979 153.024 183.571 1.00 66.46  ? 576  LYS A CA    1 
ATOM   5497  C C     . LYS D 4 579  ? 152.100 153.929 182.722 1.00 66.46  ? 576  LYS A C     1 
ATOM   5498  O O     . LYS D 4 579  ? 152.406 154.177 181.551 1.00 66.46  ? 576  LYS A O     1 
ATOM   5499  C CB    . LYS D 4 579  ? 154.322 153.698 183.856 1.00 66.46  ? 576  LYS A CB    1 
ATOM   5500  C CG    . LYS D 4 579  ? 154.219 154.960 184.698 1.00 66.46  ? 576  LYS A CG    1 
ATOM   5501  C CD    . LYS D 4 579  ? 155.594 155.483 185.079 1.00 66.46  ? 576  LYS A CD    1 
ATOM   5502  C CE    . LYS D 4 579  ? 156.250 154.598 186.126 1.00 66.46  ? 576  LYS A CE    1 
ATOM   5503  N NZ    . LYS D 4 579  ? 157.720 154.823 186.202 1.00 66.46  ? 576  LYS A NZ    1 
ATOM   5504  N N     . ALA D 4 580  ? 151.013 154.417 183.310 1.00 55.23  ? 577  ALA A N     1 
ATOM   5505  C CA    . ALA D 4 580  ? 150.049 155.236 182.590 1.00 55.23  ? 577  ALA A CA    1 
ATOM   5506  C C     . ALA D 4 580  ? 150.418 156.708 182.713 1.00 55.23  ? 577  ALA A C     1 
ATOM   5507  O O     . ALA D 4 580  ? 150.643 157.209 183.819 1.00 55.23  ? 577  ALA A O     1 
ATOM   5508  C CB    . ALA D 4 580  ? 148.636 154.997 183.122 1.00 55.23  ? 577  ALA A CB    1 
ATOM   5509  N N     . LEU D 4 581  ? 150.482 157.393 181.575 1.00 50.26  ? 578  LEU A N     1 
ATOM   5510  C CA    . LEU D 4 581  ? 150.720 158.830 181.560 1.00 50.26  ? 578  LEU A CA    1 
ATOM   5511  C C     . LEU D 4 581  ? 149.393 159.557 181.721 1.00 50.26  ? 578  LEU A C     1 
ATOM   5512  O O     . LEU D 4 581  ? 148.508 159.442 180.867 1.00 50.26  ? 578  LEU A O     1 
ATOM   5513  C CB    . LEU D 4 581  ? 151.406 159.249 180.263 1.00 43.42  ? 578  LEU A CB    1 
ATOM   5514  C CG    . LEU D 4 581  ? 152.928 159.372 180.294 1.00 43.42  ? 578  LEU A CG    1 
ATOM   5515  C CD1   . LEU D 4 581  ? 153.478 159.447 178.882 1.00 43.42  ? 578  LEU A CD1   1 
ATOM   5516  C CD2   . LEU D 4 581  ? 153.349 160.586 181.103 1.00 43.42  ? 578  LEU A CD2   1 
ATOM   5517  N N     . SER D 4 582  ? 149.253 160.302 182.812 1.00 50.26  ? 579  SER A N     1 
ATOM   5518  C CA    . SER D 4 582  ? 148.030 161.049 183.099 1.00 50.26  ? 579  SER A CA    1 
ATOM   5519  C C     . SER D 4 582  ? 148.290 162.512 182.759 1.00 50.26  ? 579  SER A C     1 
ATOM   5520  O O     . SER D 4 582  ? 148.720 163.299 183.602 1.00 50.26  ? 579  SER A O     1 
ATOM   5521  C CB    . SER D 4 582  ? 147.610 160.869 184.553 1.00 50.26  ? 579  SER A CB    1 
ATOM   5522  O OG    . SER D 4 582  ? 147.280 159.518 184.825 1.00 50.26  ? 579  SER A OG    1 
ATOM   5523  N N     . PHE D 4 583  ? 148.032 162.872 181.506 1.00 50.26  ? 580  PHE A N     1 
ATOM   5524  C CA    . PHE D 4 583  ? 148.185 164.254 181.082 1.00 50.26  ? 580  PHE A CA    1 
ATOM   5525  C C     . PHE D 4 583  ? 147.155 165.140 181.772 1.00 50.26  ? 580  PHE A C     1 
ATOM   5526  O O     . PHE D 4 583  ? 146.025 164.725 182.043 1.00 50.26  ? 580  PHE A O     1 
ATOM   5527  C CB    . PHE D 4 583  ? 148.038 164.373 179.567 1.00 50.26  ? 580  PHE A CB    1 
ATOM   5528  C CG    . PHE D 4 583  ? 149.148 163.720 178.796 1.00 50.26  ? 580  PHE A CG    1 
ATOM   5529  C CD1   . PHE D 4 583  ? 150.468 164.056 179.039 1.00 50.26  ? 580  PHE A CD1   1 
ATOM   5530  C CD2   . PHE D 4 583  ? 148.870 162.781 177.819 1.00 50.26  ? 580  PHE A CD2   1 
ATOM   5531  C CE1   . PHE D 4 583  ? 151.489 163.460 178.330 1.00 50.26  ? 580  PHE A CE1   1 
ATOM   5532  C CE2   . PHE D 4 583  ? 149.886 162.183 177.106 1.00 50.26  ? 580  PHE A CE2   1 
ATOM   5533  C CZ    . PHE D 4 583  ? 151.198 162.523 177.361 1.00 50.26  ? 580  PHE A CZ    1 
ATOM   5534  N N     . GLU D 4 584  ? 147.557 166.377 182.057 1.00 50.26  ? 581  GLU A N     1 
ATOM   5535  C CA    . GLU D 4 584  ? 146.686 167.316 182.743 1.00 50.26  ? 581  GLU A CA    1 
ATOM   5536  C C     . GLU D 4 584  ? 146.122 168.308 181.740 1.00 50.26  ? 581  GLU A C     1 
ATOM   5537  O O     . GLU D 4 584  ? 146.880 169.135 181.211 1.00 50.26  ? 581  GLU A O     1 
ATOM   5538  C CB    . GLU D 4 584  ? 147.447 168.049 183.846 1.00 40.89  ? 581  GLU A CB    1 
ATOM   5539  C CG    . GLU D 4 584  ? 146.610 169.057 184.620 1.00 40.89  ? 581  GLU A CG    1 
ATOM   5540  C CD    . GLU D 4 584  ? 145.384 168.437 185.266 1.00 40.89  ? 581  GLU A CD    1 
ATOM   5541  O OE1   . GLU D 4 584  ? 145.439 167.246 185.641 1.00 40.89  ? 581  GLU A OE1   1 
ATOM   5542  O OE2   . GLU D 4 584  ? 144.363 169.143 185.400 1.00 40.89  ? 581  GLU A OE2   1 
ATOM   5543  N N     . PRO D 4 585  ? 144.827 168.262 181.435 1.00 50.26  ? 582  PRO A N     1 
ATOM   5544  C CA    . PRO D 4 585  ? 144.252 169.252 180.517 1.00 50.26  ? 582  PRO A CA    1 
ATOM   5545  C C     . PRO D 4 585  ? 144.356 170.659 181.086 1.00 50.26  ? 582  PRO A C     1 
ATOM   5546  O O     . PRO D 4 585  ? 144.241 170.872 182.294 1.00 50.26  ? 582  PRO A O     1 
ATOM   5547  C CB    . PRO D 4 585  ? 142.791 168.806 180.382 1.00 50.26  ? 582  PRO A CB    1 
ATOM   5548  C CG    . PRO D 4 585  ? 142.783 167.372 180.804 1.00 50.26  ? 582  PRO A CG    1 
ATOM   5549  C CD    . PRO D 4 585  ? 143.842 167.250 181.849 1.00 50.26  ? 582  PRO A CD    1 
ATOM   5550  N N     . THR D 4 586  ? 144.577 171.625 180.196 1.00 50.26  ? 583  THR A N     1 
ATOM   5551  C CA    . THR D 4 586  ? 144.672 173.023 180.594 1.00 50.26  ? 583  THR A CA    1 
ATOM   5552  C C     . THR D 4 586  ? 143.683 173.868 179.803 1.00 50.26  ? 583  THR A C     1 
ATOM   5553  O O     . THR D 4 586  ? 142.852 173.331 179.064 1.00 50.26  ? 583  THR A O     1 
ATOM   5554  C CB    . THR D 4 586  ? 146.092 173.558 180.390 1.00 50.26  ? 583  THR A CB    1 
ATOM   5555  O OG1   . THR D 4 586  ? 146.342 173.729 178.989 1.00 50.26  ? 583  THR A OG1   1 
ATOM   5556  C CG2   . THR D 4 586  ? 147.122 172.602 180.975 1.00 50.26  ? 583  THR A CG2   1 
ATOM   5557  N N     . GLU D 4 587  ? 143.762 175.185 179.954 1.00 52.82  ? 584  GLU A N     1 
ATOM   5558  C CA    . GLU D 4 587  ? 142.906 176.082 179.196 1.00 52.82  ? 584  GLU A CA    1 
ATOM   5559  C C     . GLU D 4 587  ? 143.470 176.299 177.797 1.00 52.82  ? 584  GLU A C     1 
ATOM   5560  O O     . GLU D 4 587  ? 144.674 176.163 177.562 1.00 52.82  ? 584  GLU A O     1 
ATOM   5561  C CB    . GLU D 4 587  ? 142.758 177.422 179.916 1.00 52.82  ? 584  GLU A CB    1 
ATOM   5562  C CG    . GLU D 4 587  ? 142.453 177.298 181.401 1.00 52.82  ? 584  GLU A CG    1 
ATOM   5563  C CD    . GLU D 4 587  ? 141.087 176.696 181.676 1.00 52.82  ? 584  GLU A CD    1 
ATOM   5564  O OE1   . GLU D 4 587  ? 140.217 176.749 180.781 1.00 52.82  ? 584  GLU A OE1   1 
ATOM   5565  O OE2   . GLU D 4 587  ? 140.882 176.170 182.790 1.00 52.82  ? 584  GLU A OE2   1 
ATOM   5566  N N     . LYS D 4 588  ? 142.580 176.640 176.862 1.00 56.27  ? 585  LYS A N     1 
ATOM   5567  C CA    . LYS D 4 588  ? 142.995 176.850 175.479 1.00 56.27  ? 585  LYS A CA    1 
ATOM   5568  C C     . LYS D 4 588  ? 143.961 178.017 175.333 1.00 56.27  ? 585  LYS A C     1 
ATOM   5569  O O     . LYS D 4 588  ? 144.728 178.054 174.365 1.00 56.27  ? 585  LYS A O     1 
ATOM   5570  C CB    . LYS D 4 588  ? 141.773 177.074 174.589 1.00 56.28  ? 585  LYS A CB    1 
ATOM   5571  C CG    . LYS D 4 588  ? 141.031 175.800 174.227 1.00 56.28  ? 585  LYS A CG    1 
ATOM   5572  C CD    . LYS D 4 588  ? 139.932 176.074 173.216 1.00 56.28  ? 585  LYS A CD    1 
ATOM   5573  C CE    . LYS D 4 588  ? 140.513 176.376 171.845 1.00 56.28  ? 585  LYS A CE    1 
ATOM   5574  N NZ    . LYS D 4 588  ? 141.327 175.243 171.326 1.00 56.28  ? 585  LYS A NZ    1 
ATOM   5575  N N     . THR D 4 589  ? 143.939 178.973 176.264 1.00 58.48  ? 586  THR A N     1 
ATOM   5576  C CA    . THR D 4 589  ? 144.884 180.081 176.204 1.00 58.48  ? 586  THR A CA    1 
ATOM   5577  C C     . THR D 4 589  ? 146.319 179.605 176.394 1.00 58.48  ? 586  THR A C     1 
ATOM   5578  O O     . THR D 4 589  ? 147.253 180.244 175.898 1.00 58.48  ? 586  THR A O     1 
ATOM   5579  C CB    . THR D 4 589  ? 144.532 181.134 177.254 1.00 58.48  ? 586  THR A CB    1 
ATOM   5580  O OG1   . THR D 4 589  ? 144.713 180.584 178.565 1.00 58.48  ? 586  THR A OG1   1 
ATOM   5581  C CG2   . THR D 4 589  ? 143.087 181.582 177.093 1.00 58.48  ? 586  THR A CG2   1 
ATOM   5582  N N     . SER D 4 590  ? 146.514 178.496 177.104 1.00 51.99  ? 587  SER A N     1 
ATOM   5583  C CA    . SER D 4 590  ? 147.851 177.953 177.291 1.00 51.99  ? 587  SER A CA    1 
ATOM   5584  C C     . SER D 4 590  ? 148.349 177.328 175.994 1.00 51.99  ? 587  SER A C     1 
ATOM   5585  O O     . SER D 4 590  ? 147.626 176.573 175.338 1.00 51.99  ? 587  SER A O     1 
ATOM   5586  C CB    . SER D 4 590  ? 147.853 176.920 178.417 1.00 51.99  ? 587  SER A CB    1 
ATOM   5587  O OG    . SER D 4 590  ? 147.002 175.830 178.112 1.00 51.99  ? 587  SER A OG    1 
ATOM   5588  N N     . GLU D 4 591  ? 149.585 177.647 175.625 1.00 50.26  ? 588  GLU A N     1 
ATOM   5589  C CA    . GLU D 4 591  ? 150.165 177.148 174.387 1.00 50.26  ? 588  GLU A CA    1 
ATOM   5590  C C     . GLU D 4 591  ? 150.579 175.692 174.550 1.00 50.26  ? 588  GLU A C     1 
ATOM   5591  O O     . GLU D 4 591  ? 151.215 175.326 175.544 1.00 50.26  ? 588  GLU A O     1 
ATOM   5592  C CB    . GLU D 4 591  ? 151.367 178.003 173.987 1.00 50.26  ? 588  GLU A CB    1 
ATOM   5593  C CG    . GLU D 4 591  ? 151.968 177.652 172.640 1.00 50.26  ? 588  GLU A CG    1 
ATOM   5594  C CD    . GLU D 4 591  ? 153.348 178.250 172.451 1.00 50.26  ? 588  GLU A CD    1 
ATOM   5595  O OE1   . GLU D 4 591  ? 153.521 179.452 172.743 1.00 50.26  ? 588  GLU A OE1   1 
ATOM   5596  O OE2   . GLU D 4 591  ? 154.260 177.522 172.006 1.00 50.26  ? 588  GLU A OE2   1 
ATOM   5597  N N     . GLY D 4 592  ? 150.218 174.863 173.579 1.00 50.26  ? 589  GLY A N     1 
ATOM   5598  C CA    . GLY D 4 592  ? 150.583 173.463 173.632 1.00 50.26  ? 589  GLY A CA    1 
ATOM   5599  C C     . GLY D 4 592  ? 149.782 172.651 172.635 1.00 50.26  ? 589  GLY A C     1 
ATOM   5600  O O     . GLY D 4 592  ? 149.059 173.193 171.796 1.00 50.26  ? 589  GLY A O     1 
ATOM   5601  N N     . PHE D 4 593  ? 149.931 171.335 172.750 1.00 50.26  ? 590  PHE A N     1 
ATOM   5602  C CA    . PHE D 4 593  ? 149.267 170.399 171.859 1.00 50.26  ? 590  PHE A CA    1 
ATOM   5603  C C     . PHE D 4 593  ? 147.798 170.242 172.236 1.00 50.26  ? 590  PHE A C     1 
ATOM   5604  O O     . PHE D 4 593  ? 147.354 170.659 173.308 1.00 50.26  ? 590  PHE A O     1 
ATOM   5605  C CB    . PHE D 4 593  ? 149.955 169.033 171.897 1.00 50.26  ? 590  PHE A CB    1 
ATOM   5606  C CG    . PHE D 4 593  ? 151.347 169.033 171.333 1.00 50.26  ? 590  PHE A CG    1 
ATOM   5607  C CD1   . PHE D 4 593  ? 152.397 169.601 172.035 1.00 50.26  ? 590  PHE A CD1   1 
ATOM   5608  C CD2   . PHE D 4 593  ? 151.607 168.454 170.104 1.00 50.26  ? 590  PHE A CD2   1 
ATOM   5609  C CE1   . PHE D 4 593  ? 153.675 169.598 171.518 1.00 50.26  ? 590  PHE A CE1   1 
ATOM   5610  C CE2   . PHE D 4 593  ? 152.884 168.448 169.583 1.00 50.26  ? 590  PHE A CE2   1 
ATOM   5611  C CZ    . PHE D 4 593  ? 153.919 169.021 170.291 1.00 50.26  ? 590  PHE A CZ    1 
ATOM   5612  N N     . ASP D 4 594  ? 147.041 169.625 171.333 1.00 50.26  ? 591  ASP A N     1 
ATOM   5613  C CA    . ASP D 4 594  ? 145.631 169.321 171.549 1.00 50.26  ? 591  ASP A CA    1 
ATOM   5614  C C     . ASP D 4 594  ? 145.447 167.819 171.386 1.00 50.26  ? 591  ASP A C     1 
ATOM   5615  O O     . ASP D 4 594  ? 145.524 167.299 170.268 1.00 50.26  ? 591  ASP A O     1 
ATOM   5616  C CB    . ASP D 4 594  ? 144.745 170.090 170.572 1.00 50.26  ? 591  ASP A CB    1 
ATOM   5617  C CG    . ASP D 4 594  ? 144.736 171.577 170.841 1.00 50.26  ? 591  ASP A CG    1 
ATOM   5618  O OD1   . ASP D 4 594  ? 144.915 171.972 172.011 1.00 50.26  ? 591  ASP A OD1   1 
ATOM   5619  O OD2   . ASP D 4 594  ? 144.550 172.354 169.881 1.00 50.26  ? 591  ASP A OD2   1 
ATOM   5620  N N     . LYS D 4 595  ? 145.201 167.125 172.492 1.00 50.26  ? 592  LYS A N     1 
ATOM   5621  C CA    . LYS D 4 595  ? 145.095 165.674 172.480 1.00 50.26  ? 592  LYS A CA    1 
ATOM   5622  C C     . LYS D 4 595  ? 143.677 165.242 172.135 1.00 50.26  ? 592  LYS A C     1 
ATOM   5623  O O     . LYS D 4 595  ? 142.702 165.788 172.659 1.00 50.26  ? 592  LYS A O     1 
ATOM   5624  C CB    . LYS D 4 595  ? 145.503 165.094 173.834 1.00 50.26  ? 592  LYS A CB    1 
ATOM   5625  C CG    . LYS D 4 595  ? 145.101 163.645 174.039 1.00 50.26  ? 592  LYS A CG    1 
ATOM   5626  C CD    . LYS D 4 595  ? 145.868 163.014 175.186 1.00 50.26  ? 592  LYS A CD    1 
ATOM   5627  C CE    . LYS D 4 595  ? 144.986 162.067 175.979 1.00 50.26  ? 592  LYS A CE    1 
ATOM   5628  N NZ    . LYS D 4 595  ? 144.196 161.174 175.090 1.00 50.26  ? 592  LYS A NZ    1 
ATOM   5629  N N     . MET D 4 596  ? 143.571 164.258 171.248 1.00 50.26  ? 593  MET A N     1 
ATOM   5630  C CA    . MET D 4 596  ? 142.281 163.700 170.867 1.00 50.26  ? 593  MET A CA    1 
ATOM   5631  C C     . MET D 4 596  ? 141.769 162.796 171.981 1.00 50.26  ? 593  MET A C     1 
ATOM   5632  O O     . MET D 4 596  ? 142.432 161.820 172.349 1.00 50.26  ? 593  MET A O     1 
ATOM   5633  C CB    . MET D 4 596  ? 142.405 162.923 169.559 1.00 50.26  ? 593  MET A CB    1 
ATOM   5634  C CG    . MET D 4 596  ? 141.176 162.108 169.203 1.00 50.26  ? 593  MET A CG    1 
ATOM   5635  S SD    . MET D 4 596  ? 141.561 160.660 168.204 1.00 50.26  ? 593  MET A SD    1 
ATOM   5636  C CE    . MET D 4 596  ? 142.580 159.724 169.339 1.00 50.26  ? 593  MET A CE    1 
ATOM   5637  N N     . TYR D 4 597  ? 140.596 163.118 172.518 1.00 50.26  ? 594  TYR A N     1 
ATOM   5638  C CA    . TYR D 4 597  ? 139.960 162.310 173.557 1.00 50.26  ? 594  TYR A CA    1 
ATOM   5639  C C     . TYR D 4 597  ? 138.905 161.443 172.880 1.00 50.26  ? 594  TYR A C     1 
ATOM   5640  O O     . TYR D 4 597  ? 137.724 161.786 172.830 1.00 50.26  ? 594  TYR A O     1 
ATOM   5641  C CB    . TYR D 4 597  ? 139.366 163.190 174.649 1.00 50.26  ? 594  TYR A CB    1 
ATOM   5642  C CG    . TYR D 4 597  ? 140.379 163.629 175.678 1.00 50.26  ? 594  TYR A CG    1 
ATOM   5643  C CD1   . TYR D 4 597  ? 141.301 164.623 175.389 1.00 50.26  ? 594  TYR A CD1   1 
ATOM   5644  C CD2   . TYR D 4 597  ? 140.419 163.045 176.934 1.00 50.26  ? 594  TYR A CD2   1 
ATOM   5645  C CE1   . TYR D 4 597  ? 142.232 165.026 176.322 1.00 50.26  ? 594  TYR A CE1   1 
ATOM   5646  C CE2   . TYR D 4 597  ? 141.346 163.442 177.876 1.00 50.26  ? 594  TYR A CE2   1 
ATOM   5647  C CZ    . TYR D 4 597  ? 142.250 164.434 177.564 1.00 50.26  ? 594  TYR A CZ    1 
ATOM   5648  O OH    . TYR D 4 597  ? 143.178 164.835 178.497 1.00 50.26  ? 594  TYR A OH    1 
ATOM   5649  N N     . TYR D 4 598  ? 139.348 160.306 172.355 1.00 50.26  ? 595  TYR A N     1 
ATOM   5650  C CA    . TYR D 4 598  ? 138.473 159.383 171.646 1.00 50.26  ? 595  TYR A CA    1 
ATOM   5651  C C     . TYR D 4 598  ? 137.582 158.657 172.645 1.00 50.26  ? 595  TYR A C     1 
ATOM   5652  O O     . TYR D 4 598  ? 138.069 157.870 173.462 1.00 50.26  ? 595  TYR A O     1 
ATOM   5653  C CB    . TYR D 4 598  ? 139.316 158.392 170.851 1.00 50.26  ? 595  TYR A CB    1 
ATOM   5654  C CG    . TYR D 4 598  ? 138.567 157.551 169.846 1.00 50.26  ? 595  TYR A CG    1 
ATOM   5655  C CD1   . TYR D 4 598  ? 138.359 158.003 168.553 1.00 50.26  ? 595  TYR A CD1   1 
ATOM   5656  C CD2   . TYR D 4 598  ? 138.091 156.294 170.184 1.00 50.26  ? 595  TYR A CD2   1 
ATOM   5657  C CE1   . TYR D 4 598  ? 137.690 157.231 167.629 1.00 50.26  ? 595  TYR A CE1   1 
ATOM   5658  C CE2   . TYR D 4 598  ? 137.419 155.517 169.268 1.00 50.26  ? 595  TYR A CE2   1 
ATOM   5659  C CZ    . TYR D 4 598  ? 137.220 155.990 167.993 1.00 50.26  ? 595  TYR A CZ    1 
ATOM   5660  O OH    . TYR D 4 598  ? 136.550 155.215 167.076 1.00 50.26  ? 595  TYR A OH    1 
ATOM   5661  N N     . ASP D 4 599  ? 136.281 158.926 172.585 1.00 50.26  ? 596  ASP A N     1 
ATOM   5662  C CA    . ASP D 4 599  ? 135.298 158.267 173.433 1.00 50.26  ? 596  ASP A CA    1 
ATOM   5663  C C     . ASP D 4 599  ? 134.374 157.440 172.555 1.00 50.26  ? 596  ASP A C     1 
ATOM   5664  O O     . ASP D 4 599  ? 133.762 157.969 171.622 1.00 50.26  ? 596  ASP A O     1 
ATOM   5665  C CB    . ASP D 4 599  ? 134.497 159.287 174.244 1.00 50.26  ? 596  ASP A CB    1 
ATOM   5666  C CG    . ASP D 4 599  ? 133.889 158.688 175.492 1.00 50.26  ? 596  ASP A CG    1 
ATOM   5667  O OD1   . ASP D 4 599  ? 134.647 158.399 176.442 1.00 50.26  ? 596  ASP A OD1   1 
ATOM   5668  O OD2   . ASP D 4 599  ? 132.654 158.509 175.526 1.00 50.26  ? 596  ASP A OD2   1 
ATOM   5669  N N     . TYR D 4 600  ? 134.270 156.149 172.854 1.00 50.26  ? 597  TYR A N     1 
ATOM   5670  C CA    . TYR D 4 600  ? 133.529 155.240 171.995 1.00 50.26  ? 597  TYR A CA    1 
ATOM   5671  C C     . TYR D 4 600  ? 132.788 154.225 172.850 1.00 50.26  ? 597  TYR A C     1 
ATOM   5672  O O     . TYR D 4 600  ? 133.155 153.957 173.996 1.00 50.26  ? 597  TYR A O     1 
ATOM   5673  C CB    . TYR D 4 600  ? 134.462 154.532 171.006 1.00 50.26  ? 597  TYR A CB    1 
ATOM   5674  C CG    . TYR D 4 600  ? 133.757 153.792 169.892 1.00 50.26  ? 597  TYR A CG    1 
ATOM   5675  C CD1   . TYR D 4 600  ? 132.562 154.257 169.367 1.00 50.26  ? 597  TYR A CD1   1 
ATOM   5676  C CD2   . TYR D 4 600  ? 134.293 152.627 169.365 1.00 50.26  ? 597  TYR A CD2   1 
ATOM   5677  C CE1   . TYR D 4 600  ? 131.918 153.580 168.351 1.00 50.26  ? 597  TYR A CE1   1 
ATOM   5678  C CE2   . TYR D 4 600  ? 133.658 151.946 168.349 1.00 50.26  ? 597  TYR A CE2   1 
ATOM   5679  C CZ    . TYR D 4 600  ? 132.472 152.426 167.846 1.00 50.26  ? 597  TYR A CZ    1 
ATOM   5680  O OH    . TYR D 4 600  ? 131.838 151.745 166.834 1.00 50.26  ? 597  TYR A OH    1 
ATOM   5681  N N     . PHE D 4 601  ? 131.731 153.672 172.275 1.00 50.26  ? 598  PHE A N     1 
ATOM   5682  C CA    . PHE D 4 601  ? 130.962 152.599 172.902 1.00 50.26  ? 598  PHE A CA    1 
ATOM   5683  C C     . PHE D 4 601  ? 130.430 151.763 171.748 1.00 50.26  ? 598  PHE A C     1 
ATOM   5684  O O     . PHE D 4 601  ? 129.443 152.141 171.097 1.00 50.26  ? 598  PHE A O     1 
ATOM   5685  C CB    . PHE D 4 601  ? 129.836 153.144 173.775 1.00 50.26  ? 598  PHE A CB    1 
ATOM   5686  C CG    . PHE D 4 601  ? 129.265 152.141 174.734 1.00 50.26  ? 598  PHE A CG    1 
ATOM   5687  C CD1   . PHE D 4 601  ? 130.002 151.716 175.825 1.00 50.26  ? 598  PHE A CD1   1 
ATOM   5688  C CD2   . PHE D 4 601  ? 127.983 151.653 174.569 1.00 50.26  ? 598  PHE A CD2   1 
ATOM   5689  C CE1   . PHE D 4 601  ? 129.481 150.805 176.718 1.00 50.26  ? 598  PHE A CE1   1 
ATOM   5690  C CE2   . PHE D 4 601  ? 127.455 150.744 175.461 1.00 50.26  ? 598  PHE A CE2   1 
ATOM   5691  C CZ    . PHE D 4 601  ? 128.206 150.320 176.537 1.00 50.26  ? 598  PHE A CZ    1 
ATOM   5692  N N     . PRO D 4 602  ? 131.057 150.609 171.464 1.00 50.26  ? 599  PRO A N     1 
ATOM   5693  C CA    . PRO D 4 602  ? 130.961 149.995 170.128 1.00 50.26  ? 599  PRO A CA    1 
ATOM   5694  C C     . PRO D 4 602  ? 129.560 149.857 169.552 1.00 50.26  ? 599  PRO A C     1 
ATOM   5695  O O     . PRO D 4 602  ? 129.275 150.396 168.478 1.00 50.26  ? 599  PRO A O     1 
ATOM   5696  C CB    . PRO D 4 602  ? 131.594 148.615 170.345 1.00 50.26  ? 599  PRO A CB    1 
ATOM   5697  C CG    . PRO D 4 602  ? 132.554 148.822 171.455 1.00 50.26  ? 599  PRO A CG    1 
ATOM   5698  C CD    . PRO D 4 602  ? 131.933 149.844 172.365 1.00 50.26  ? 599  PRO A CD    1 
ATOM   5699  N N     . ASP D 4 603  ? 128.678 149.147 170.248 1.00 52.06  ? 600  ASP A N     1 
ATOM   5700  C CA    . ASP D 4 603  ? 127.329 148.925 169.746 1.00 52.06  ? 600  ASP A CA    1 
ATOM   5701  C C     . ASP D 4 603  ? 126.440 148.558 170.920 1.00 52.06  ? 600  ASP A C     1 
ATOM   5702  O O     . ASP D 4 603  ? 126.764 147.639 171.676 1.00 52.06  ? 600  ASP A O     1 
ATOM   5703  C CB    . ASP D 4 603  ? 127.306 147.818 168.686 1.00 52.06  ? 600  ASP A CB    1 
ATOM   5704  C CG    . ASP D 4 603  ? 125.968 147.709 167.980 1.00 52.06  ? 600  ASP A CG    1 
ATOM   5705  O OD1   . ASP D 4 603  ? 125.043 148.475 168.321 1.00 52.06  ? 600  ASP A OD1   1 
ATOM   5706  O OD2   . ASP D 4 603  ? 125.841 146.851 167.081 1.00 52.06  ? 600  ASP A OD2   1 
ATOM   5707  N N     . ALA D 4 604  ? 125.321 149.270 171.062 1.00 50.33  ? 601  ALA A N     1 
ATOM   5708  C CA    . ALA D 4 604  ? 124.443 149.038 172.202 1.00 50.33  ? 601  ALA A CA    1 
ATOM   5709  C C     . ALA D 4 604  ? 123.916 147.610 172.212 1.00 50.33  ? 601  ALA A C     1 
ATOM   5710  O O     . ALA D 4 604  ? 123.885 146.961 173.264 1.00 50.33  ? 601  ALA A O     1 
ATOM   5711  C CB    . ALA D 4 604  ? 123.288 150.038 172.185 1.00 50.33  ? 601  ALA A CB    1 
ATOM   5712  N N     . ALA D 4 605  ? 123.538 147.091 171.040 1.00 54.83  ? 602  ALA A N     1 
ATOM   5713  C CA    . ALA D 4 605  ? 122.902 145.781 170.961 1.00 54.83  ? 602  ALA A CA    1 
ATOM   5714  C C     . ALA D 4 605  ? 123.723 144.696 171.642 1.00 54.83  ? 602  ALA A C     1 
ATOM   5715  O O     . ALA D 4 605  ? 123.158 143.775 172.242 1.00 54.83  ? 602  ALA A O     1 
ATOM   5716  C CB    . ALA D 4 605  ? 122.656 145.414 169.498 1.00 54.83  ? 602  ALA A CB    1 
ATOM   5717  N N     . LYS D 4 606  ? 125.049 144.787 171.571 1.00 54.12  ? 603  LYS A N     1 
ATOM   5718  C CA    . LYS D 4 606  ? 125.916 143.811 172.216 1.00 54.12  ? 603  LYS A CA    1 
ATOM   5719  C C     . LYS D 4 606  ? 126.500 144.298 173.533 1.00 54.12  ? 603  LYS A C     1 
ATOM   5720  O O     . LYS D 4 606  ? 126.773 143.479 174.415 1.00 54.12  ? 603  LYS A O     1 
ATOM   5721  C CB    . LYS D 4 606  ? 127.060 143.416 171.277 1.00 54.12  ? 603  LYS A CB    1 
ATOM   5722  C CG    . LYS D 4 606  ? 128.104 144.497 171.072 1.00 54.12  ? 603  LYS A CG    1 
ATOM   5723  C CD    . LYS D 4 606  ? 128.862 144.282 169.781 1.00 54.12  ? 603  LYS A CD    1 
ATOM   5724  C CE    . LYS D 4 606  ? 129.850 145.404 169.518 1.00 54.12  ? 603  LYS A CE    1 
ATOM   5725  N NZ    . LYS D 4 606  ? 129.958 145.719 168.068 1.00 54.12  ? 603  LYS A NZ    1 
ATOM   5726  N N     . MET D 4 607  ? 126.696 145.607 173.692 1.00 51.56  ? 604  MET A N     1 
ATOM   5727  C CA    . MET D 4 607  ? 127.364 146.111 174.885 1.00 51.56  ? 604  MET A CA    1 
ATOM   5728  C C     . MET D 4 607  ? 126.420 146.204 176.078 1.00 51.56  ? 604  MET A C     1 
ATOM   5729  O O     . MET D 4 607  ? 126.812 145.870 177.201 1.00 51.56  ? 604  MET A O     1 
ATOM   5730  C CB    . MET D 4 607  ? 127.994 147.471 174.597 1.00 51.56  ? 604  MET A CB    1 
ATOM   5731  C CG    . MET D 4 607  ? 129.203 147.420 173.679 1.00 51.56  ? 604  MET A CG    1 
ATOM   5732  S SD    . MET D 4 607  ? 130.395 146.158 174.155 1.00 51.56  ? 604  MET A SD    1 
ATOM   5733  C CE    . MET D 4 607  ? 131.505 147.125 175.173 1.00 51.56  ? 604  MET A CE    1 
ATOM   5734  N N     . ILE D 4 608  ? 125.181 146.663 175.867 1.00 55.66  ? 605  ILE A N     1 
ATOM   5735  C CA    . ILE D 4 608  ? 124.250 146.808 176.989 1.00 55.66  ? 605  ILE A CA    1 
ATOM   5736  C C     . ILE D 4 608  ? 123.966 145.479 177.680 1.00 55.66  ? 605  ILE A C     1 
ATOM   5737  O O     . ILE D 4 608  ? 124.080 145.416 178.915 1.00 55.66  ? 605  ILE A O     1 
ATOM   5738  C CB    . ILE D 4 608  ? 122.967 147.525 176.529 1.00 55.66  ? 605  ILE A CB    1 
ATOM   5739  C CG1   . ILE D 4 608  ? 123.304 148.710 175.624 1.00 55.66  ? 605  ILE A CG1   1 
ATOM   5740  C CG2   . ILE D 4 608  ? 122.142 147.964 177.727 1.00 55.66  ? 605  ILE A CG2   1 
ATOM   5741  C CD1   . ILE D 4 608  ? 124.054 149.818 176.307 1.00 55.66  ? 605  ILE A CD1   1 
ATOM   5742  N N     . PRO D 4 609  ? 123.594 144.399 176.978 1.00 53.79  ? 606  PRO A N     1 
ATOM   5743  C CA    . PRO D 4 609  ? 123.415 143.124 177.693 1.00 53.79  ? 606  PRO A CA    1 
ATOM   5744  C C     . PRO D 4 609  ? 124.685 142.636 178.362 1.00 53.79  ? 606  PRO A C     1 
ATOM   5745  O O     . PRO D 4 609  ? 124.633 142.122 179.485 1.00 53.79  ? 606  PRO A O     1 
ATOM   5746  C CB    . PRO D 4 609  ? 122.944 142.162 176.592 1.00 53.79  ? 606  PRO A CB    1 
ATOM   5747  C CG    . PRO D 4 609  ? 122.468 143.032 175.487 1.00 53.79  ? 606  PRO A CG    1 
ATOM   5748  C CD    . PRO D 4 609  ? 123.325 144.248 175.538 1.00 53.79  ? 606  PRO A CD    1 
ATOM   5749  N N     . LYS D 4 610  ? 125.834 142.803 177.703 1.00 51.95  ? 607  LYS A N     1 
ATOM   5750  C CA    . LYS D 4 610  ? 127.093 142.328 178.269 1.00 51.95  ? 607  LYS A CA    1 
ATOM   5751  C C     . LYS D 4 610  ? 127.450 143.082 179.541 1.00 51.95  ? 607  LYS A C     1 
ATOM   5752  O O     . LYS D 4 610  ? 127.854 142.474 180.538 1.00 51.95  ? 607  LYS A O     1 
ATOM   5753  C CB    . LYS D 4 610  ? 128.211 142.462 177.236 1.00 51.95  ? 607  LYS A CB    1 
ATOM   5754  C CG    . LYS D 4 610  ? 129.603 142.590 177.829 1.00 51.95  ? 607  LYS A CG    1 
ATOM   5755  C CD    . LYS D 4 610  ? 130.573 143.173 176.818 1.00 51.95  ? 607  LYS A CD    1 
ATOM   5756  C CE    . LYS D 4 610  ? 131.921 143.462 177.447 1.00 51.95  ? 607  LYS A CE    1 
ATOM   5757  N NZ    . LYS D 4 610  ? 132.527 142.235 178.028 1.00 51.95  ? 607  LYS A NZ    1 
ATOM   5758  N N     . CYS D 4 611  ? 127.302 144.405 179.531 1.00 57.58  ? 608  CYS A N     1 
ATOM   5759  C CA    . CYS D 4 611  ? 127.702 145.206 180.678 1.00 57.58  ? 608  CYS A CA    1 
ATOM   5760  C C     . CYS D 4 611  ? 126.625 145.290 181.749 1.00 57.58  ? 608  CYS A C     1 
ATOM   5761  O O     . CYS D 4 611  ? 126.914 145.754 182.857 1.00 57.58  ? 608  CYS A O     1 
ATOM   5762  C CB    . CYS D 4 611  ? 128.085 146.616 180.227 1.00 57.58  ? 608  CYS A CB    1 
ATOM   5763  S SG    . CYS D 4 611  ? 129.447 146.677 179.042 1.00 57.58  ? 608  CYS A SG    1 
ATOM   5764  N N     . SER D 4 612  ? 125.397 144.862 181.455 1.00 61.44  ? 609  SER A N     1 
ATOM   5765  C CA    . SER D 4 612  ? 124.302 144.988 182.407 1.00 61.44  ? 609  SER A CA    1 
ATOM   5766  C C     . SER D 4 612  ? 123.757 143.644 182.870 1.00 61.44  ? 609  SER A C     1 
ATOM   5767  O O     . SER D 4 612  ? 123.766 143.356 184.070 1.00 61.44  ? 609  SER A O     1 
ATOM   5768  C CB    . SER D 4 612  ? 123.178 145.829 181.789 1.00 61.44  ? 609  SER A CB    1 
ATOM   5769  O OG    . SER D 4 612  ? 122.592 145.160 180.686 1.00 61.44  ? 609  SER A OG    1 
ATOM   5770  N N     . THR D 4 613  ? 123.288 142.800 181.950 1.00 61.40  ? 610  THR A N     1 
ATOM   5771  C CA    . THR D 4 613  ? 122.512 141.626 182.323 1.00 61.40  ? 610  THR A CA    1 
ATOM   5772  C C     . THR D 4 613  ? 123.157 140.302 181.943 1.00 61.40  ? 610  THR A C     1 
ATOM   5773  O O     . THR D 4 613  ? 122.666 139.253 182.372 1.00 61.40  ? 610  THR A O     1 
ATOM   5774  C CB    . THR D 4 613  ? 121.112 141.695 181.697 1.00 61.40  ? 610  THR A CB    1 
ATOM   5775  O OG1   . THR D 4 613  ? 120.280 140.677 182.266 1.00 61.40  ? 610  THR A OG1   1 
ATOM   5776  C CG2   . THR D 4 613  ? 121.195 141.497 180.197 1.00 61.40  ? 610  THR A CG2   1 
ATOM   5777  N N     . GLN D 4 614  ? 124.229 140.311 181.153 1.00 58.07  ? 611  GLN A N     1 
ATOM   5778  C CA    . GLN D 4 614  ? 124.962 139.092 180.838 1.00 58.07  ? 611  GLN A CA    1 
ATOM   5779  C C     . GLN D 4 614  ? 126.214 138.943 181.693 1.00 58.07  ? 611  GLN A C     1 
ATOM   5780  O O     . GLN D 4 614  ? 127.075 138.112 181.388 1.00 58.07  ? 611  GLN A O     1 
ATOM   5781  C CB    . GLN D 4 614  ? 125.314 139.043 179.353 1.00 58.07  ? 611  GLN A CB    1 
ATOM   5782  C CG    . GLN D 4 614  ? 124.102 139.097 178.444 1.00 58.07  ? 611  GLN A CG    1 
ATOM   5783  C CD    . GLN D 4 614  ? 123.032 138.105 178.854 1.00 58.07  ? 611  GLN A CD    1 
ATOM   5784  O OE1   . GLN D 4 614  ? 121.941 138.489 179.273 1.00 58.07  ? 611  GLN A OE1   1 
ATOM   5785  N NE2   . GLN D 4 614  ? 123.341 136.820 178.736 1.00 58.07  ? 611  GLN A NE2   1 
ATOM   5786  N N     . LEU D 4 615  ? 126.335 139.742 182.749 1.00 61.11  ? 612  LEU A N     1 
ATOM   5787  C CA    . LEU D 4 615  ? 127.405 139.543 183.714 1.00 61.11  ? 612  LEU A CA    1 
ATOM   5788  C C     . LEU D 4 615  ? 127.254 138.179 184.372 1.00 61.11  ? 612  LEU A C     1 
ATOM   5789  O O     . LEU D 4 615  ? 126.143 137.745 184.689 1.00 61.11  ? 612  LEU A O     1 
ATOM   5790  C CB    . LEU D 4 615  ? 127.374 140.644 184.774 1.00 61.11  ? 612  LEU A CB    1 
ATOM   5791  C CG    . LEU D 4 615  ? 127.443 142.087 184.277 1.00 61.11  ? 612  LEU A CG    1 
ATOM   5792  C CD1   . LEU D 4 615  ? 127.099 143.053 185.397 1.00 61.11  ? 612  LEU A CD1   1 
ATOM   5793  C CD2   . LEU D 4 615  ? 128.816 142.389 183.718 1.00 61.11  ? 612  LEU A CD2   1 
ATOM   5794  N N     . LYS D 4 616  ? 128.382 137.493 184.570 1.00 62.21  ? 613  LYS A N     1 
ATOM   5795  C CA    . LYS D 4 616  ? 128.328 136.165 185.172 1.00 62.21  ? 613  LYS A CA    1 
ATOM   5796  C C     . LYS D 4 616  ? 127.777 136.228 186.590 1.00 62.21  ? 613  LYS A C     1 
ATOM   5797  O O     . LYS D 4 616  ? 127.006 135.354 187.003 1.00 62.21  ? 613  LYS A O     1 
ATOM   5798  C CB    . LYS D 4 616  ? 129.711 135.516 185.159 1.00 62.21  ? 613  LYS A CB    1 
ATOM   5799  C CG    . LYS D 4 616  ? 129.665 134.002 185.289 1.00 62.21  ? 613  LYS A CG    1 
ATOM   5800  C CD    . LYS D 4 616  ? 131.007 133.367 184.975 1.00 62.21  ? 613  LYS A CD    1 
ATOM   5801  C CE    . LYS D 4 616  ? 131.275 133.352 183.479 1.00 62.21  ? 613  LYS A CE    1 
ATOM   5802  N NZ    . LYS D 4 616  ? 130.341 132.449 182.755 1.00 62.21  ? 613  LYS A NZ    1 
ATOM   5803  N N     . ALA D 4 617  ? 128.159 137.256 187.350 1.00 64.72  ? 614  ALA A N     1 
ATOM   5804  C CA    . ALA D 4 617  ? 127.618 137.418 188.695 1.00 64.72  ? 614  ALA A CA    1 
ATOM   5805  C C     . ALA D 4 617  ? 126.112 137.645 188.660 1.00 64.72  ? 614  ALA A C     1 
ATOM   5806  O O     . ALA D 4 617  ? 125.370 137.059 189.457 1.00 64.72  ? 614  ALA A O     1 
ATOM   5807  C CB    . ALA D 4 617  ? 128.320 138.573 189.408 1.00 64.72  ? 614  ALA A CB    1 
ATOM   5808  N N     . VAL D 4 618  ? 125.643 138.486 187.737 1.00 68.07  ? 615  VAL A N     1 
ATOM   5809  C CA    . VAL D 4 618  ? 124.212 138.765 187.633 1.00 68.07  ? 615  VAL A CA    1 
ATOM   5810  C C     . VAL D 4 618  ? 123.450 137.503 187.251 1.00 68.07  ? 615  VAL A C     1 
ATOM   5811  O O     . VAL D 4 618  ? 122.400 137.188 187.827 1.00 68.07  ? 615  VAL A O     1 
ATOM   5812  C CB    . VAL D 4 618  ? 123.963 139.904 186.627 1.00 68.07  ? 615  VAL A CB    1 
ATOM   5813  C CG1   . VAL D 4 618  ? 122.511 139.917 186.182 1.00 68.07  ? 615  VAL A CG1   1 
ATOM   5814  C CG2   . VAL D 4 618  ? 124.353 141.243 187.234 1.00 68.07  ? 615  VAL A CG2   1 
ATOM   5815  N N     . THR D 4 619  ? 123.967 136.763 186.267 1.00 66.96  ? 616  THR A N     1 
ATOM   5816  C CA    . THR D 4 619  ? 123.304 135.538 185.835 1.00 66.96  ? 616  THR A CA    1 
ATOM   5817  C C     . THR D 4 619  ? 123.267 134.507 186.955 1.00 66.96  ? 616  THR A C     1 
ATOM   5818  O O     . THR D 4 619  ? 122.245 133.845 187.165 1.00 66.96  ? 616  THR A O     1 
ATOM   5819  C CB    . THR D 4 619  ? 124.007 134.968 184.602 1.00 66.96  ? 616  THR A CB    1 
ATOM   5820  O OG1   . THR D 4 619  ? 123.886 135.892 183.514 1.00 66.96  ? 616  THR A OG1   1 
ATOM   5821  C CG2   . THR D 4 619  ? 123.386 133.640 184.198 1.00 66.96  ? 616  THR A CG2   1 
ATOM   5822  N N     . ALA D 4 620  ? 124.373 134.358 187.689 1.00 69.96  ? 617  ALA A N     1 
ATOM   5823  C CA    . ALA D 4 620  ? 124.398 133.421 188.806 1.00 69.96  ? 617  ALA A CA    1 
ATOM   5824  C C     . ALA D 4 620  ? 123.409 133.829 189.890 1.00 69.96  ? 617  ALA A C     1 
ATOM   5825  O O     . ALA D 4 620  ? 122.696 132.982 190.442 1.00 69.96  ? 617  ALA A O     1 
ATOM   5826  C CB    . ALA D 4 620  ? 125.812 133.321 189.377 1.00 69.96  ? 617  ALA A CB    1 
ATOM   5827  N N     . HIS D 4 621  ? 123.350 135.125 190.207 1.00 77.93  ? 618  HIS A N     1 
ATOM   5828  C CA    . HIS D 4 621  ? 122.419 135.595 191.226 1.00 77.93  ? 618  HIS A CA    1 
ATOM   5829  C C     . HIS D 4 621  ? 120.977 135.342 190.811 1.00 77.93  ? 618  HIS A C     1 
ATOM   5830  O O     . HIS D 4 621  ? 120.152 134.926 191.632 1.00 77.93  ? 618  HIS A O     1 
ATOM   5831  C CB    . HIS D 4 621  ? 122.647 137.081 191.500 1.00 77.93  ? 618  HIS A CB    1 
ATOM   5832  C CG    . HIS D 4 621  ? 121.610 137.701 192.385 1.00 77.93  ? 618  HIS A CG    1 
ATOM   5833  N ND1   . HIS D 4 621  ? 121.797 137.878 193.739 1.00 77.93  ? 618  HIS A ND1   1 
ATOM   5834  C CD2   . HIS D 4 621  ? 120.379 138.194 192.108 1.00 77.93  ? 618  HIS A CD2   1 
ATOM   5835  C CE1   . HIS D 4 621  ? 120.724 138.447 194.259 1.00 77.93  ? 618  HIS A CE1   1 
ATOM   5836  N NE2   . HIS D 4 621  ? 119.849 138.650 193.291 1.00 77.93  ? 618  HIS A NE2   1 
ATOM   5837  N N     . PHE D 4 622  ? 120.651 135.589 189.541 1.00 80.86  ? 619  PHE A N     1 
ATOM   5838  C CA    . PHE D 4 622  ? 119.285 135.359 189.082 1.00 80.86  ? 619  PHE A CA    1 
ATOM   5839  C C     . PHE D 4 622  ? 118.951 133.872 189.041 1.00 80.86  ? 619  PHE A C     1 
ATOM   5840  O O     . PHE D 4 622  ? 117.818 133.478 189.338 1.00 80.86  ? 619  PHE A O     1 
ATOM   5841  C CB    . PHE D 4 622  ? 119.073 136.005 187.714 1.00 80.86  ? 619  PHE A CB    1 
ATOM   5842  C CG    . PHE D 4 622  ? 118.853 137.488 187.780 1.00 80.86  ? 619  PHE A CG    1 
ATOM   5843  C CD1   . PHE D 4 622  ? 118.256 138.059 188.891 1.00 80.86  ? 619  PHE A CD1   1 
ATOM   5844  C CD2   . PHE D 4 622  ? 119.241 138.309 186.737 1.00 80.86  ? 619  PHE A CD2   1 
ATOM   5845  C CE1   . PHE D 4 622  ? 118.051 139.422 188.961 1.00 80.86  ? 619  PHE A CE1   1 
ATOM   5846  C CE2   . PHE D 4 622  ? 119.036 139.674 186.801 1.00 80.86  ? 619  PHE A CE2   1 
ATOM   5847  C CZ    . PHE D 4 622  ? 118.441 140.230 187.915 1.00 80.86  ? 619  PHE A CZ    1 
ATOM   5848  N N     . GLN D 4 623  ? 119.919 133.032 188.668 1.00 78.77  ? 620  GLN A N     1 
ATOM   5849  C CA    . GLN D 4 623  ? 119.682 131.594 188.663 1.00 78.77  ? 620  GLN A CA    1 
ATOM   5850  C C     . GLN D 4 623  ? 119.451 131.067 190.074 1.00 78.77  ? 620  GLN A C     1 
ATOM   5851  O O     . GLN D 4 623  ? 118.582 130.216 190.293 1.00 78.77  ? 620  GLN A O     1 
ATOM   5852  C CB    . GLN D 4 623  ? 120.857 130.872 188.004 1.00 78.77  ? 620  GLN A CB    1 
ATOM   5853  C CG    . GLN D 4 623  ? 120.694 129.363 187.921 1.00 78.77  ? 620  GLN A CG    1 
ATOM   5854  C CD    . GLN D 4 623  ? 119.450 128.950 187.158 1.00 78.77  ? 620  GLN A CD    1 
ATOM   5855  O OE1   . GLN D 4 623  ? 119.079 129.577 186.166 1.00 78.77  ? 620  GLN A OE1   1 
ATOM   5856  N NE2   . GLN D 4 623  ? 118.799 127.888 187.618 1.00 78.77  ? 620  GLN A NE2   1 
ATOM   5857  N N     . THR D 4 624  ? 120.218 131.563 191.044 1.00 82.51  ? 621  THR A N     1 
ATOM   5858  C CA    . THR D 4 624  ? 120.115 131.082 192.416 1.00 82.51  ? 621  THR A CA    1 
ATOM   5859  C C     . THR D 4 624  ? 119.060 131.831 193.224 1.00 82.51  ? 621  THR A C     1 
ATOM   5860  O O     . THR D 4 624  ? 118.413 131.239 194.095 1.00 82.51  ? 621  THR A O     1 
ATOM   5861  C CB    . THR D 4 624  ? 121.477 131.189 193.110 1.00 82.51  ? 621  THR A CB    1 
ATOM   5862  O OG1   . THR D 4 624  ? 122.486 130.611 192.273 1.00 82.51  ? 621  THR A OG1   1 
ATOM   5863  C CG2   . THR D 4 624  ? 121.461 130.456 194.443 1.00 82.51  ? 621  THR A CG2   1 
ATOM   5864  N N     . HIS D 4 625  ? 118.858 133.118 192.946 1.00 84.87  ? 622  HIS A N     1 
ATOM   5865  C CA    . HIS D 4 625  ? 117.982 133.952 193.754 1.00 84.87  ? 622  HIS A CA    1 
ATOM   5866  C C     . HIS D 4 625  ? 117.047 134.731 192.838 1.00 84.87  ? 622  HIS A C     1 
ATOM   5867  O O     . HIS D 4 625  ? 117.374 135.000 191.680 1.00 84.87  ? 622  HIS A O     1 
ATOM   5868  C CB    . HIS D 4 625  ? 118.805 134.895 194.642 1.00 84.87  ? 622  HIS A CB    1 
ATOM   5869  C CG    . HIS D 4 625  ? 117.980 135.761 195.539 1.00 84.87  ? 622  HIS A CG    1 
ATOM   5870  N ND1   . HIS D 4 625  ? 117.341 135.275 196.659 1.00 84.87  ? 622  HIS A ND1   1 
ATOM   5871  C CD2   . HIS D 4 625  ? 117.703 137.085 195.492 1.00 84.87  ? 622  HIS A CD2   1 
ATOM   5872  C CE1   . HIS D 4 625  ? 116.699 136.261 197.259 1.00 84.87  ? 622  HIS A CE1   1 
ATOM   5873  N NE2   . HIS D 4 625  ? 116.904 137.370 196.572 1.00 84.87  ? 622  HIS A NE2   1 
ATOM   5874  N N     . THR D 4 626  ? 115.877 135.092 193.365 1.00 88.33  ? 623  THR A N     1 
ATOM   5875  C CA    . THR D 4 626  ? 114.793 135.630 192.549 1.00 88.33  ? 623  THR A CA    1 
ATOM   5876  C C     . THR D 4 626  ? 114.636 137.143 192.643 1.00 88.33  ? 623  THR A C     1 
ATOM   5877  O O     . THR D 4 626  ? 114.285 137.780 191.645 1.00 88.33  ? 623  THR A O     1 
ATOM   5878  C CB    . THR D 4 626  ? 113.466 134.967 192.933 1.00 88.33  ? 623  THR A CB    1 
ATOM   5879  O OG1   . THR D 4 626  ? 113.248 135.109 194.343 1.00 88.33  ? 623  THR A OG1   1 
ATOM   5880  C CG2   . THR D 4 626  ? 113.485 133.489 192.574 1.00 88.33  ? 623  THR A CG2   1 
ATOM   5881  N N     . THR D 4 627  ? 114.873 137.738 193.809 1.00 89.88  ? 624  THR A N     1 
ATOM   5882  C CA    . THR D 4 627  ? 114.636 139.164 193.971 1.00 89.88  ? 624  THR A CA    1 
ATOM   5883  C C     . THR D 4 627  ? 115.651 139.975 193.162 1.00 89.88  ? 624  THR A C     1 
ATOM   5884  O O     . THR D 4 627  ? 116.753 139.499 192.878 1.00 89.88  ? 624  THR A O     1 
ATOM   5885  C CB    . THR D 4 627  ? 114.704 139.557 195.446 1.00 89.88  ? 624  THR A CB    1 
ATOM   5886  O OG1   . THR D 4 627  ? 116.066 139.539 195.891 1.00 89.88  ? 624  THR A OG1   1 
ATOM   5887  C CG2   . THR D 4 627  ? 113.876 138.599 196.292 1.00 89.88  ? 624  THR A CG2   1 
ATOM   5888  N N     . PRO D 4 628  ? 115.295 141.201 192.769 1.00 87.91  ? 625  PRO A N     1 
ATOM   5889  C CA    . PRO D 4 628  ? 116.193 141.996 191.922 1.00 87.91  ? 625  PRO A CA    1 
ATOM   5890  C C     . PRO D 4 628  ? 117.510 142.317 192.616 1.00 87.91  ? 625  PRO A C     1 
ATOM   5891  O O     . PRO D 4 628  ? 117.586 142.428 193.841 1.00 87.91  ? 625  PRO A O     1 
ATOM   5892  C CB    . PRO D 4 628  ? 115.385 143.271 191.646 1.00 87.91  ? 625  PRO A CB    1 
ATOM   5893  C CG    . PRO D 4 628  ? 114.353 143.316 192.726 1.00 87.91  ? 625  PRO A CG    1 
ATOM   5894  C CD    . PRO D 4 628  ? 114.011 141.887 192.993 1.00 87.91  ? 625  PRO A CD    1 
ATOM   5895  N N     . ILE D 4 629  ? 118.555 142.468 191.804 1.00 81.05  ? 626  ILE A N     1 
ATOM   5896  C CA    . ILE D 4 629  ? 119.909 142.710 192.286 1.00 81.05  ? 626  ILE A CA    1 
ATOM   5897  C C     . ILE D 4 629  ? 120.324 144.128 191.915 1.00 81.05  ? 626  ILE A C     1 
ATOM   5898  O O     . ILE D 4 629  ? 119.866 144.693 190.915 1.00 81.05  ? 626  ILE A O     1 
ATOM   5899  C CB    . ILE D 4 629  ? 120.897 141.670 191.711 1.00 81.05  ? 626  ILE A CB    1 
ATOM   5900  C CG1   . ILE D 4 629  ? 122.256 141.759 192.411 1.00 81.05  ? 626  ILE A CG1   1 
ATOM   5901  C CG2   . ILE D 4 629  ? 121.051 141.846 190.207 1.00 81.05  ? 626  ILE A CG2   1 
ATOM   5902  C CD1   . ILE D 4 629  ? 123.297 140.821 191.841 1.00 81.05  ? 626  ILE A CD1   1 
ATOM   5903  N N     . LEU D 4 630  ? 121.191 144.707 192.740 1.00 80.82  ? 627  LEU A N     1 
ATOM   5904  C CA    . LEU D 4 630  ? 121.725 146.045 192.528 1.00 80.82  ? 627  LEU A CA    1 
ATOM   5905  C C     . LEU D 4 630  ? 123.215 145.961 192.227 1.00 80.82  ? 627  LEU A C     1 
ATOM   5906  O O     . LEU D 4 630  ? 123.936 145.162 192.833 1.00 80.82  ? 627  LEU A O     1 
ATOM   5907  C CB    . LEU D 4 630  ? 121.491 146.933 193.754 1.00 80.82  ? 627  LEU A CB    1 
ATOM   5908  C CG    . LEU D 4 630  ? 120.187 147.733 193.839 1.00 80.82  ? 627  LEU A CG    1 
ATOM   5909  C CD1   . LEU D 4 630  ? 120.133 148.784 192.743 1.00 80.82  ? 627  LEU A CD1   1 
ATOM   5910  C CD2   . LEU D 4 630  ? 118.963 146.828 193.778 1.00 80.82  ? 627  LEU A CD2   1 
ATOM   5911  N N     . LEU D 4 631  ? 123.674 146.787 191.289 1.00 72.48  ? 628  LEU A N     1 
ATOM   5912  C CA    . LEU D 4 631  ? 125.068 146.804 190.865 1.00 72.48  ? 628  LEU A CA    1 
ATOM   5913  C C     . LEU D 4 631  ? 125.693 148.142 191.234 1.00 72.48  ? 628  LEU A C     1 
ATOM   5914  O O     . LEU D 4 631  ? 125.206 149.197 190.811 1.00 72.48  ? 628  LEU A O     1 
ATOM   5915  C CB    . LEU D 4 631  ? 125.184 146.556 189.362 1.00 72.48  ? 628  LEU A CB    1 
ATOM   5916  C CG    . LEU D 4 631  ? 124.703 145.189 188.880 1.00 72.48  ? 628  LEU A CG    1 
ATOM   5917  C CD1   . LEU D 4 631  ? 124.690 145.136 187.364 1.00 72.48  ? 628  LEU A CD1   1 
ATOM   5918  C CD2   . LEU D 4 631  ? 125.580 144.089 189.451 1.00 72.48  ? 628  LEU A CD2   1 
ATOM   5919  N N     . SER D 4 632  ? 126.773 148.095 192.012 1.00 82.34  ? 629  SER A N     1 
ATOM   5920  C CA    . SER D 4 632  ? 127.513 149.286 192.408 1.00 82.34  ? 629  SER A CA    1 
ATOM   5921  C C     . SER D 4 632  ? 128.906 149.337 191.792 1.00 82.34  ? 629  SER A C     1 
ATOM   5922  O O     . SER D 4 632  ? 129.711 150.194 192.173 1.00 82.34  ? 629  SER A O     1 
ATOM   5923  C CB    . SER D 4 632  ? 127.611 149.365 193.933 1.00 82.34  ? 629  SER A CB    1 
ATOM   5924  O OG    . SER D 4 632  ? 128.434 148.333 194.447 1.00 82.34  ? 629  SER A OG    1 
ATOM   5925  N N     . ASN D 4 633  ? 129.209 148.445 190.854 1.00 75.26  ? 630  ASN A N     1 
ATOM   5926  C CA    . ASN D 4 633  ? 130.509 148.400 190.199 1.00 75.26  ? 630  ASN A CA    1 
ATOM   5927  C C     . ASN D 4 633  ? 130.395 148.996 188.804 1.00 75.26  ? 630  ASN A C     1 
ATOM   5928  O O     . ASN D 4 633  ? 129.532 148.588 188.019 1.00 75.26  ? 630  ASN A O     1 
ATOM   5929  C CB    . ASN D 4 633  ? 131.029 146.964 190.120 1.00 75.26  ? 630  ASN A CB    1 
ATOM   5930  C CG    . ASN D 4 633  ? 132.478 146.892 189.680 1.00 75.26  ? 630  ASN A CG    1 
ATOM   5931  O OD1   . ASN D 4 633  ? 133.128 147.917 189.472 1.00 75.26  ? 630  ASN A OD1   1 
ATOM   5932  N ND2   . ASN D 4 633  ? 132.991 145.677 189.533 1.00 75.26  ? 630  ASN A ND2   1 
ATOM   5933  N N     . ASN D 4 634  ? 131.272 149.955 188.499 1.00 69.96  ? 631  ASN A N     1 
ATOM   5934  C CA    . ASN D 4 634  ? 131.269 150.659 187.216 1.00 69.96  ? 631  ASN A CA    1 
ATOM   5935  C C     . ASN D 4 634  ? 129.920 151.330 186.963 1.00 69.96  ? 631  ASN A C     1 
ATOM   5936  O O     . ASN D 4 634  ? 129.308 151.174 185.904 1.00 69.96  ? 631  ASN A O     1 
ATOM   5937  C CB    . ASN D 4 634  ? 131.641 149.718 186.067 1.00 69.96  ? 631  ASN A CB    1 
ATOM   5938  C CG    . ASN D 4 634  ? 133.126 149.726 185.764 1.00 69.96  ? 631  ASN A CG    1 
ATOM   5939  O OD1   . ASN D 4 634  ? 133.754 150.783 185.704 1.00 69.96  ? 631  ASN A OD1   1 
ATOM   5940  N ND2   . ASN D 4 634  ? 133.697 148.543 185.570 1.00 69.96  ? 631  ASN A ND2   1 
ATOM   5941  N N     . PHE D 4 635  ? 129.456 152.086 187.955 1.00 67.97  ? 632  PHE A N     1 
ATOM   5942  C CA    . PHE D 4 635  ? 128.207 152.829 187.845 1.00 67.97  ? 632  PHE A CA    1 
ATOM   5943  C C     . PHE D 4 635  ? 128.284 154.049 188.749 1.00 67.97  ? 632  PHE A C     1 
ATOM   5944  O O     . PHE D 4 635  ? 128.626 153.924 189.928 1.00 67.97  ? 632  PHE A O     1 
ATOM   5945  C CB    . PHE D 4 635  ? 127.004 151.961 188.229 1.00 67.97  ? 632  PHE A CB    1 
ATOM   5946  C CG    . PHE D 4 635  ? 126.564 151.020 187.145 1.00 67.97  ? 632  PHE A CG    1 
ATOM   5947  C CD1   . PHE D 4 635  ? 125.971 151.500 185.992 1.00 67.97  ? 632  PHE A CD1   1 
ATOM   5948  C CD2   . PHE D 4 635  ? 126.741 149.654 187.281 1.00 67.97  ? 632  PHE A CD2   1 
ATOM   5949  C CE1   . PHE D 4 635  ? 125.566 150.637 184.994 1.00 67.97  ? 632  PHE A CE1   1 
ATOM   5950  C CE2   . PHE D 4 635  ? 126.338 148.786 186.285 1.00 67.97  ? 632  PHE A CE2   1 
ATOM   5951  C CZ    . PHE D 4 635  ? 125.750 149.278 185.142 1.00 67.97  ? 632  PHE A CZ    1 
ATOM   5952  N N     . ILE D 4 636  ? 127.975 155.223 188.192 1.00 73.60  ? 633  ILE A N     1 
ATOM   5953  C CA    . ILE D 4 636  ? 127.971 156.444 188.993 1.00 73.60  ? 633  ILE A CA    1 
ATOM   5954  C C     . ILE D 4 636  ? 126.917 156.355 190.089 1.00 73.60  ? 633  ILE A C     1 
ATOM   5955  O O     . ILE D 4 636  ? 127.182 156.669 191.256 1.00 73.60  ? 633  ILE A O     1 
ATOM   5956  C CB    . ILE D 4 636  ? 127.753 157.674 188.093 1.00 73.60  ? 633  ILE A CB    1 
ATOM   5957  C CG1   . ILE D 4 636  ? 128.972 157.899 187.197 1.00 73.60  ? 633  ILE A CG1   1 
ATOM   5958  C CG2   . ILE D 4 636  ? 127.463 158.909 188.931 1.00 73.60  ? 633  ILE A CG2   1 
ATOM   5959  C CD1   . ILE D 4 636  ? 130.254 158.137 187.964 1.00 73.60  ? 633  ILE A CD1   1 
ATOM   5960  N N     . GLU D 4 637  ? 125.712 155.921 189.732 1.00 74.17  ? 634  GLU A N     1 
ATOM   5961  C CA    . GLU D 4 637  ? 124.658 155.646 190.686 1.00 74.17  ? 634  GLU A CA    1 
ATOM   5962  C C     . GLU D 4 637  ? 124.165 154.218 190.479 1.00 74.17  ? 634  GLU A C     1 
ATOM   5963  O O     . GLU D 4 637  ? 124.028 153.780 189.332 1.00 74.17  ? 634  GLU A O     1 
ATOM   5964  C CB    . GLU D 4 637  ? 123.501 156.649 190.520 1.00 74.17  ? 634  GLU A CB    1 
ATOM   5965  C CG    . GLU D 4 637  ? 122.441 156.616 191.614 1.00 74.17  ? 634  GLU A CG    1 
ATOM   5966  C CD    . GLU D 4 637  ? 121.396 155.548 191.390 1.00 74.17  ? 634  GLU A CD    1 
ATOM   5967  O OE1   . GLU D 4 637  ? 121.141 155.211 190.218 1.00 74.17  ? 634  GLU A OE1   1 
ATOM   5968  O OE2   . GLU D 4 637  ? 120.834 155.044 192.385 1.00 74.17  ? 634  GLU A OE2   1 
ATOM   5969  N N     . PRO D 4 638  ? 123.910 153.469 191.554 1.00 74.68  ? 635  PRO A N     1 
ATOM   5970  C CA    . PRO D 4 638  ? 123.634 152.032 191.405 1.00 74.68  ? 635  PRO A CA    1 
ATOM   5971  C C     . PRO D 4 638  ? 122.475 151.754 190.458 1.00 74.68  ? 635  PRO A C     1 
ATOM   5972  O O     . PRO D 4 638  ? 121.457 152.448 190.467 1.00 74.68  ? 635  PRO A O     1 
ATOM   5973  C CB    . PRO D 4 638  ? 123.307 151.585 192.833 1.00 74.68  ? 635  PRO A CB    1 
ATOM   5974  C CG    . PRO D 4 638  ? 124.016 152.555 193.706 1.00 74.68  ? 635  PRO A CG    1 
ATOM   5975  C CD    . PRO D 4 638  ? 124.086 153.860 192.964 1.00 74.68  ? 635  PRO A CD    1 
ATOM   5976  N N     . LEU D 4 639  ? 122.646 150.722 189.636 1.00 74.50  ? 636  LEU A N     1 
ATOM   5977  C CA    . LEU D 4 639  ? 121.660 150.353 188.630 1.00 74.50  ? 636  LEU A CA    1 
ATOM   5978  C C     . LEU D 4 639  ? 120.740 149.269 189.170 1.00 74.50  ? 636  LEU A C     1 
ATOM   5979  O O     . LEU D 4 639  ? 121.205 148.239 189.667 1.00 74.50  ? 636  LEU A O     1 
ATOM   5980  C CB    . LEU D 4 639  ? 122.344 149.872 187.351 1.00 74.50  ? 636  LEU A CB    1 
ATOM   5981  C CG    . LEU D 4 639  ? 121.438 149.159 186.344 1.00 74.50  ? 636  LEU A CG    1 
ATOM   5982  C CD1   . LEU D 4 639  ? 120.449 150.134 185.729 1.00 74.50  ? 636  LEU A CD1   1 
ATOM   5983  C CD2   . LEU D 4 639  ? 122.260 148.478 185.263 1.00 74.50  ? 636  LEU A CD2   1 
ATOM   5984  N N     . GLU D 4 640  ? 119.437 149.504 189.064 1.00 81.33  ? 637  GLU A N     1 
ATOM   5985  C CA    . GLU D 4 640  ? 118.433 148.555 189.523 1.00 81.33  ? 637  GLU A CA    1 
ATOM   5986  C C     . GLU D 4 640  ? 118.068 147.652 188.351 1.00 81.33  ? 637  GLU A C     1 
ATOM   5987  O O     . GLU D 4 640  ? 117.582 148.130 187.320 1.00 81.33  ? 637  GLU A O     1 
ATOM   5988  C CB    . GLU D 4 640  ? 117.220 149.308 190.084 1.00 81.33  ? 637  GLU A CB    1 
ATOM   5989  C CG    . GLU D 4 640  ? 116.168 148.494 190.870 1.00 81.33  ? 637  GLU A CG    1 
ATOM   5990  C CD    . GLU D 4 640  ? 115.405 147.451 190.065 1.00 81.33  ? 637  GLU A CD    1 
ATOM   5991  O OE1   . GLU D 4 640  ? 115.351 147.552 188.824 1.00 81.33  ? 637  GLU A OE1   1 
ATOM   5992  O OE2   . GLU D 4 640  ? 114.848 146.523 190.687 1.00 81.33  ? 637  GLU A OE2   1 
ATOM   5993  N N     . ILE D 4 641  ? 118.321 146.356 188.502 1.00 79.94  ? 638  ILE A N     1 
ATOM   5994  C CA    . ILE D 4 641  ? 117.999 145.358 187.489 1.00 79.94  ? 638  ILE A CA    1 
ATOM   5995  C C     . ILE D 4 641  ? 116.969 144.407 188.080 1.00 79.94  ? 638  ILE A C     1 
ATOM   5996  O O     . ILE D 4 641  ? 117.213 143.789 189.124 1.00 79.94  ? 638  ILE A O     1 
ATOM   5997  C CB    . ILE D 4 641  ? 119.248 144.597 187.023 1.00 79.94  ? 638  ILE A CB    1 
ATOM   5998  C CG1   . ILE D 4 641  ? 120.149 145.513 186.196 1.00 79.94  ? 638  ILE A CG1   1 
ATOM   5999  C CG2   . ILE D 4 641  ? 118.858 143.364 186.223 1.00 79.94  ? 638  ILE A CG2   1 
ATOM   6000  C CD1   . ILE D 4 641  ? 121.424 144.851 185.739 1.00 79.94  ? 638  ILE A CD1   1 
ATOM   6001  N N     . THR D 4 642  ? 115.826 144.286 187.415 1.00 82.79  ? 639  THR A N     1 
ATOM   6002  C CA    . THR D 4 642  ? 114.753 143.429 187.888 1.00 82.79  ? 639  THR A CA    1 
ATOM   6003  C C     . THR D 4 642  ? 114.906 142.013 187.340 1.00 82.79  ? 639  THR A C     1 
ATOM   6004  O O     . THR D 4 642  ? 115.713 141.740 186.450 1.00 82.79  ? 639  THR A O     1 
ATOM   6005  C CB    . THR D 4 642  ? 113.392 143.995 187.490 1.00 82.79  ? 639  THR A CB    1 
ATOM   6006  O OG1   . THR D 4 642  ? 113.296 144.054 186.061 1.00 82.79  ? 639  THR A OG1   1 
ATOM   6007  C CG2   . THR D 4 642  ? 113.194 145.385 188.068 1.00 82.79  ? 639  THR A CG2   1 
ATOM   6008  N N     . LYS D 4 643  ? 114.110 141.101 187.899 1.00 83.22  ? 640  LYS A N     1 
ATOM   6009  C CA    . LYS D 4 643  ? 114.089 139.732 187.397 1.00 83.22  ? 640  LYS A CA    1 
ATOM   6010  C C     . LYS D 4 643  ? 113.402 139.652 186.040 1.00 83.22  ? 640  LYS A C     1 
ATOM   6011  O O     . LYS D 4 643  ? 113.817 138.874 185.173 1.00 83.22  ? 640  LYS A O     1 
ATOM   6012  C CB    . LYS D 4 643  ? 113.393 138.819 188.407 1.00 83.22  ? 640  LYS A CB    1 
ATOM   6013  C CG    . LYS D 4 643  ? 113.321 137.359 187.990 1.00 83.22  ? 640  LYS A CG    1 
ATOM   6014  C CD    . LYS D 4 643  ? 112.414 136.565 188.917 1.00 83.22  ? 640  LYS A CD    1 
ATOM   6015  C CE    . LYS D 4 643  ? 111.026 136.398 188.320 1.00 83.22  ? 640  LYS A CE    1 
ATOM   6016  N NZ    . LYS D 4 643  ? 110.451 135.055 188.610 1.00 83.22  ? 640  LYS A NZ    1 
ATOM   6017  N N     . GLU D 4 644  ? 112.352 140.452 185.837 1.00 84.08  ? 641  GLU A N     1 
ATOM   6018  C CA    . GLU D 4 644  ? 111.548 140.331 184.624 1.00 84.08  ? 641  GLU A CA    1 
ATOM   6019  C C     . GLU D 4 644  ? 112.333 140.727 183.379 1.00 84.08  ? 641  GLU A C     1 
ATOM   6020  O O     . GLU D 4 644  ? 112.181 140.101 182.325 1.00 84.08  ? 641  GLU A O     1 
ATOM   6021  C CB    . GLU D 4 644  ? 110.270 141.162 184.750 1.00 84.08  ? 641  GLU A CB    1 
ATOM   6022  C CG    . GLU D 4 644  ? 110.484 142.610 185.147 1.00 84.08  ? 641  GLU A CG    1 
ATOM   6023  C CD    . GLU D 4 644  ? 110.320 142.826 186.638 1.00 84.08  ? 641  GLU A CD    1 
ATOM   6024  O OE1   . GLU D 4 644  ? 110.329 141.828 187.389 1.00 84.08  ? 641  GLU A OE1   1 
ATOM   6025  O OE2   . GLU D 4 644  ? 110.178 143.993 187.060 1.00 84.08  ? 641  GLU A OE2   1 
ATOM   6026  N N     . ILE D 4 645  ? 113.166 141.766 183.465 1.00 77.92  ? 642  ILE A N     1 
ATOM   6027  C CA    . ILE D 4 645  ? 113.938 142.168 182.292 1.00 77.92  ? 642  ILE A CA    1 
ATOM   6028  C C     . ILE D 4 645  ? 114.915 141.068 181.895 1.00 77.92  ? 642  ILE A C     1 
ATOM   6029  O O     . ILE D 4 645  ? 115.092 140.775 180.705 1.00 77.92  ? 642  ILE A O     1 
ATOM   6030  C CB    . ILE D 4 645  ? 114.648 143.512 182.541 1.00 77.92  ? 642  ILE A CB    1 
ATOM   6031  C CG1   . ILE D 4 645  ? 115.530 143.449 183.786 1.00 77.92  ? 642  ILE A CG1   1 
ATOM   6032  C CG2   . ILE D 4 645  ? 113.630 144.635 182.669 1.00 77.92  ? 642  ILE A CG2   1 
ATOM   6033  C CD1   . ILE D 4 645  ? 116.232 144.750 184.094 1.00 77.92  ? 642  ILE A CD1   1 
ATOM   6034  N N     . TYR D 4 646  ? 115.552 140.430 182.880 1.00 76.32  ? 643  TYR A N     1 
ATOM   6035  C CA    . TYR D 4 646  ? 116.425 139.300 182.585 1.00 76.32  ? 643  TYR A CA    1 
ATOM   6036  C C     . TYR D 4 646  ? 115.640 138.139 181.987 1.00 76.32  ? 643  TYR A C     1 
ATOM   6037  O O     . TYR D 4 646  ? 116.104 137.486 181.045 1.00 76.32  ? 643  TYR A O     1 
ATOM   6038  C CB    . TYR D 4 646  ? 117.158 138.862 183.854 1.00 76.32  ? 643  TYR A CB    1 
ATOM   6039  C CG    . TYR D 4 646  ? 117.993 137.612 183.687 1.00 76.32  ? 643  TYR A CG    1 
ATOM   6040  C CD1   . TYR D 4 646  ? 119.296 137.684 183.215 1.00 76.32  ? 643  TYR A CD1   1 
ATOM   6041  C CD2   . TYR D 4 646  ? 117.482 136.362 184.011 1.00 76.32  ? 643  TYR A CD2   1 
ATOM   6042  C CE1   . TYR D 4 646  ? 120.062 136.546 183.062 1.00 76.32  ? 643  TYR A CE1   1 
ATOM   6043  C CE2   . TYR D 4 646  ? 118.240 135.219 183.861 1.00 76.32  ? 643  TYR A CE2   1 
ATOM   6044  C CZ    . TYR D 4 646  ? 119.529 135.317 183.386 1.00 76.32  ? 643  TYR A CZ    1 
ATOM   6045  O OH    . TYR D 4 646  ? 120.288 134.179 183.237 1.00 76.32  ? 643  TYR A OH    1 
ATOM   6046  N N     . ASP D 4 647  ? 114.447 137.866 182.524 1.00 81.32  ? 644  ASP A N     1 
ATOM   6047  C CA    . ASP D 4 647  ? 113.639 136.763 182.009 1.00 81.32  ? 644  ASP A CA    1 
ATOM   6048  C C     . ASP D 4 647  ? 113.242 136.999 180.558 1.00 81.32  ? 644  ASP A C     1 
ATOM   6049  O O     . ASP D 4 647  ? 113.280 136.075 179.737 1.00 81.32  ? 644  ASP A O     1 
ATOM   6050  C CB    . ASP D 4 647  ? 112.397 136.568 182.878 1.00 81.32  ? 644  ASP A CB    1 
ATOM   6051  C CG    . ASP D 4 647  ? 112.738 136.153 184.294 1.00 81.32  ? 644  ASP A CG    1 
ATOM   6052  O OD1   . ASP D 4 647  ? 113.933 135.935 184.580 1.00 81.32  ? 644  ASP A OD1   1 
ATOM   6053  O OD2   . ASP D 4 647  ? 111.809 136.042 185.122 1.00 81.32  ? 644  ASP A OD2   1 
ATOM   6054  N N     . LEU D 4 648  ? 112.849 138.229 180.224 1.00 79.64  ? 645  LEU A N     1 
ATOM   6055  C CA    . LEU D 4 648  ? 112.556 138.556 178.831 1.00 79.64  ? 645  LEU A CA    1 
ATOM   6056  C C     . LEU D 4 648  ? 113.804 138.456 177.964 1.00 79.64  ? 645  LEU A C     1 
ATOM   6057  O O     . LEU D 4 648  ? 113.737 137.985 176.823 1.00 79.64  ? 645  LEU A O     1 
ATOM   6058  C CB    . LEU D 4 648  ? 111.926 139.946 178.724 1.00 79.64  ? 645  LEU A CB    1 
ATOM   6059  C CG    . LEU D 4 648  ? 110.414 140.088 178.954 1.00 79.64  ? 645  LEU A CG    1 
ATOM   6060  C CD1   . LEU D 4 648  ? 109.665 139.326 177.876 1.00 79.64  ? 645  LEU A CD1   1 
ATOM   6061  C CD2   . LEU D 4 648  ? 109.953 139.621 180.324 1.00 79.64  ? 645  LEU A CD2   1 
ATOM   6062  N N     . ASN D 4 649  ? 114.954 138.891 178.482 1.00 72.59  ? 646  ASN A N     1 
ATOM   6063  C CA    . ASN D 4 649  ? 116.191 138.749 177.726 1.00 72.59  ? 646  ASN A CA    1 
ATOM   6064  C C     . ASN D 4 649  ? 116.745 137.331 177.755 1.00 72.59  ? 646  ASN A C     1 
ATOM   6065  O O     . ASN D 4 649  ? 117.627 137.012 176.950 1.00 72.59  ? 646  ASN A O     1 
ATOM   6066  C CB    . ASN D 4 649  ? 117.252 139.719 178.246 1.00 72.59  ? 646  ASN A CB    1 
ATOM   6067  C CG    . ASN D 4 649  ? 118.340 139.989 177.225 1.00 72.59  ? 646  ASN A CG    1 
ATOM   6068  O OD1   . ASN D 4 649  ? 118.253 139.549 176.079 1.00 72.59  ? 646  ASN A OD1   1 
ATOM   6069  N ND2   . ASN D 4 649  ? 119.369 140.715 177.634 1.00 72.59  ? 646  ASN A ND2   1 
ATOM   6070  N N     . ASN D 4 650  ? 116.256 136.476 178.650 1.00 75.10  ? 647  ASN A N     1 
ATOM   6071  C CA    . ASN D 4 650  ? 116.679 135.078 178.729 1.00 75.10  ? 647  ASN A CA    1 
ATOM   6072  C C     . ASN D 4 650  ? 115.448 134.182 178.779 1.00 75.10  ? 647  ASN A C     1 
ATOM   6073  O O     . ASN D 4 650  ? 115.120 133.610 179.825 1.00 75.10  ? 647  ASN A O     1 
ATOM   6074  C CB    . ASN D 4 650  ? 117.577 134.846 179.944 1.00 75.10  ? 647  ASN A CB    1 
ATOM   6075  C CG    . ASN D 4 650  ? 118.870 135.627 179.865 1.00 75.10  ? 647  ASN A CG    1 
ATOM   6076  O OD1   . ASN D 4 650  ? 118.910 136.815 180.181 1.00 75.10  ? 647  ASN A OD1   1 
ATOM   6077  N ND2   . ASN D 4 650  ? 119.940 134.961 179.445 1.00 75.10  ? 647  ASN A ND2   1 
ATOM   6078  N N     . PRO D 4 651  ? 114.741 134.040 177.665 1.00 85.59  ? 648  PRO A N     1 
ATOM   6079  C CA    . PRO D 4 651  ? 113.558 133.179 177.629 1.00 85.59  ? 648  PRO A CA    1 
ATOM   6080  C C     . PRO D 4 651  ? 113.958 131.726 177.394 1.00 85.59  ? 648  PRO A C     1 
ATOM   6081  O O     . PRO D 4 651  ? 115.135 131.385 177.293 1.00 85.59  ? 648  PRO A O     1 
ATOM   6082  C CB    . PRO D 4 651  ? 112.763 133.743 176.454 1.00 85.59  ? 648  PRO A CB    1 
ATOM   6083  C CG    . PRO D 4 651  ? 113.818 134.224 175.513 1.00 85.59  ? 648  PRO A CG    1 
ATOM   6084  C CD    . PRO D 4 651  ? 114.997 134.666 176.355 1.00 85.59  ? 648  PRO A CD    1 
ATOM   6085  N N     . GLU D 4 652  ? 112.948 130.867 177.307 1.00 92.62  ? 649  GLU A N     1 
ATOM   6086  C CA    . GLU D 4 652  ? 113.155 129.451 177.037 1.00 92.62  ? 649  GLU A CA    1 
ATOM   6087  C C     . GLU D 4 652  ? 113.067 129.112 175.555 1.00 92.62  ? 649  GLU A C     1 
ATOM   6088  O O     . GLU D 4 652  ? 113.198 127.937 175.195 1.00 92.62  ? 649  GLU A O     1 
ATOM   6089  C CB    . GLU D 4 652  ? 112.142 128.611 177.821 1.00 92.62  ? 649  GLU A CB    1 
ATOM   6090  C CG    . GLU D 4 652  ? 112.025 128.993 179.288 1.00 92.62  ? 649  GLU A CG    1 
ATOM   6091  C CD    . GLU D 4 652  ? 113.370 129.059 179.986 1.00 92.62  ? 649  GLU A CD    1 
ATOM   6092  O OE1   . GLU D 4 652  ? 114.195 128.143 179.783 1.00 92.62  ? 649  GLU A OE1   1 
ATOM   6093  O OE2   . GLU D 4 652  ? 113.604 130.029 180.738 1.00 92.62  ? 649  GLU A OE2   1 
ATOM   6094  N N     . LYS D 4 653  ? 112.853 130.101 174.693 1.00 96.67  ? 650  LYS A N     1 
ATOM   6095  C CA    . LYS D 4 653  ? 112.755 129.889 173.258 1.00 96.67  ? 650  LYS A CA    1 
ATOM   6096  C C     . LYS D 4 653  ? 113.811 130.717 172.538 1.00 96.67  ? 650  LYS A C     1 
ATOM   6097  O O     . LYS D 4 653  ? 114.248 131.762 173.031 1.00 96.67  ? 650  LYS A O     1 
ATOM   6098  C CB    . LYS D 4 653  ? 111.361 130.253 172.733 1.00 96.67  ? 650  LYS A CB    1 
ATOM   6099  C CG    . LYS D 4 653  ? 110.233 129.453 173.360 1.00 96.67  ? 650  LYS A CG    1 
ATOM   6100  C CD    . LYS D 4 653  ? 108.873 129.985 172.934 1.00 96.67  ? 650  LYS A CD    1 
ATOM   6101  C CE    . LYS D 4 653  ? 107.752 129.336 173.730 1.00 96.67  ? 650  LYS A CE    1 
ATOM   6102  N NZ    . LYS D 4 653  ? 106.427 129.943 173.421 1.00 96.67  ? 650  LYS A NZ    1 
ATOM   6103  N N     . GLU D 4 654  ? 114.224 130.230 171.368 1.00 100.20 ? 651  GLU A N     1 
ATOM   6104  C CA    . GLU D 4 654  ? 115.217 130.952 170.574 1.00 100.20 ? 651  GLU A CA    1 
ATOM   6105  C C     . GLU D 4 654  ? 114.745 132.342 170.161 1.00 100.20 ? 651  GLU A C     1 
ATOM   6106  O O     . GLU D 4 654  ? 115.516 133.302 170.329 1.00 100.20 ? 651  GLU A O     1 
ATOM   6107  C CB    . GLU D 4 654  ? 115.620 130.104 169.361 1.00 100.20 ? 651  GLU A CB    1 
ATOM   6108  C CG    . GLU D 4 654  ? 116.699 130.728 168.489 1.00 100.20 ? 651  GLU A CG    1 
ATOM   6109  C CD    . GLU D 4 654  ? 118.064 130.713 169.148 1.00 100.20 ? 651  GLU A CD    1 
ATOM   6110  O OE1   . GLU D 4 654  ? 118.316 129.811 169.975 1.00 100.20 ? 651  GLU A OE1   1 
ATOM   6111  O OE2   . GLU D 4 654  ? 118.885 131.602 168.839 1.00 100.20 ? 651  GLU A OE2   1 
ATOM   6112  N N     . PRO D 4 655  ? 113.521 132.539 169.625 1.00 96.94  ? 652  PRO A N     1 
ATOM   6113  C CA    . PRO D 4 655  ? 113.073 133.904 169.310 1.00 96.94  ? 652  PRO A CA    1 
ATOM   6114  C C     . PRO D 4 655  ? 112.655 134.647 170.570 1.00 96.94  ? 652  PRO A C     1 
ATOM   6115  O O     . PRO D 4 655  ? 111.613 134.356 171.166 1.00 96.94  ? 652  PRO A O     1 
ATOM   6116  C CB    . PRO D 4 655  ? 111.889 133.670 168.361 1.00 96.94  ? 652  PRO A CB    1 
ATOM   6117  C CG    . PRO D 4 655  ? 111.369 132.342 168.736 1.00 96.94  ? 652  PRO A CG    1 
ATOM   6118  C CD    . PRO D 4 655  ? 112.561 131.530 169.136 1.00 96.94  ? 652  PRO A CD    1 
ATOM   6119  N N     . LYS D 4 656  ? 113.473 135.612 170.979 1.00 87.14  ? 653  LYS A N     1 
ATOM   6120  C CA    . LYS D 4 656  ? 113.143 136.420 172.141 1.00 87.14  ? 653  LYS A CA    1 
ATOM   6121  C C     . LYS D 4 656  ? 111.990 137.367 171.821 1.00 87.14  ? 653  LYS A C     1 
ATOM   6122  O O     . LYS D 4 656  ? 111.729 137.705 170.663 1.00 87.14  ? 653  LYS A O     1 
ATOM   6123  C CB    . LYS D 4 656  ? 114.361 137.218 172.607 1.00 87.14  ? 653  LYS A CB    1 
ATOM   6124  C CG    . LYS D 4 656  ? 115.613 136.383 172.814 1.00 87.14  ? 653  LYS A CG    1 
ATOM   6125  C CD    . LYS D 4 656  ? 116.556 137.043 173.807 1.00 87.14  ? 653  LYS A CD    1 
ATOM   6126  C CE    . LYS D 4 656  ? 117.422 138.096 173.136 1.00 87.14  ? 653  LYS A CE    1 
ATOM   6127  N NZ    . LYS D 4 656  ? 118.587 137.494 172.429 1.00 87.14  ? 653  LYS A NZ    1 
ATOM   6128  N N     . LYS D 4 657  ? 111.294 137.799 172.875 1.00 86.54  ? 654  LYS A N     1 
ATOM   6129  C CA    . LYS D 4 657  ? 110.202 138.751 172.703 1.00 86.54  ? 654  LYS A CA    1 
ATOM   6130  C C     . LYS D 4 657  ? 110.695 140.101 172.203 1.00 86.54  ? 654  LYS A C     1 
ATOM   6131  O O     . LYS D 4 657  ? 109.885 140.922 171.761 1.00 86.54  ? 654  LYS A O     1 
ATOM   6132  C CB    . LYS D 4 657  ? 109.445 138.928 174.020 1.00 86.54  ? 654  LYS A CB    1 
ATOM   6133  C CG    . LYS D 4 657  ? 108.810 137.650 174.544 1.00 86.54  ? 654  LYS A CG    1 
ATOM   6134  C CD    . LYS D 4 657  ? 107.553 137.941 175.348 1.00 86.54  ? 654  LYS A CD    1 
ATOM   6135  C CE    . LYS D 4 657  ? 107.166 136.753 176.212 1.00 86.54  ? 654  LYS A CE    1 
ATOM   6136  N NZ    . LYS D 4 657  ? 106.889 135.541 175.394 1.00 86.54  ? 654  LYS A NZ    1 
ATOM   6137  N N     . PHE D 4 658  ? 112.003 140.351 172.275 1.00 77.16  ? 655  PHE A N     1 
ATOM   6138  C CA    . PHE D 4 658  ? 112.565 141.606 171.793 1.00 77.16  ? 655  PHE A CA    1 
ATOM   6139  C C     . PHE D 4 658  ? 112.622 141.646 170.272 1.00 77.16  ? 655  PHE A C     1 
ATOM   6140  O O     . PHE D 4 658  ? 112.345 142.685 169.663 1.00 77.16  ? 655  PHE A O     1 
ATOM   6141  C CB    . PHE D 4 658  ? 113.961 141.801 172.382 1.00 77.16  ? 655  PHE A CB    1 
ATOM   6142  C CG    . PHE D 4 658  ? 113.969 141.990 173.869 1.00 77.16  ? 655  PHE A CG    1 
ATOM   6143  C CD1   . PHE D 4 658  ? 112.790 142.207 174.564 1.00 77.16  ? 655  PHE A CD1   1 
ATOM   6144  C CD2   . PHE D 4 658  ? 115.152 141.915 174.578 1.00 77.16  ? 655  PHE A CD2   1 
ATOM   6145  C CE1   . PHE D 4 658  ? 112.796 142.370 175.932 1.00 77.16  ? 655  PHE A CE1   1 
ATOM   6146  C CE2   . PHE D 4 658  ? 115.164 142.072 175.947 1.00 77.16  ? 655  PHE A CE2   1 
ATOM   6147  C CZ    . PHE D 4 658  ? 113.985 142.302 176.626 1.00 77.16  ? 655  PHE A CZ    1 
ATOM   6148  N N     . GLN D 4 659  ? 112.981 140.529 169.648 1.00 86.21  ? 656  GLN A N     1 
ATOM   6149  C CA    . GLN D 4 659  ? 113.107 140.462 168.203 1.00 86.21  ? 656  GLN A CA    1 
ATOM   6150  C C     . GLN D 4 659  ? 111.736 140.332 167.547 1.00 86.21  ? 656  GLN A C     1 
ATOM   6151  O O     . GLN D 4 659  ? 110.771 139.852 168.148 1.00 86.21  ? 656  GLN A O     1 
ATOM   6152  C CB    . GLN D 4 659  ? 113.995 139.285 167.797 1.00 86.21  ? 656  GLN A CB    1 
ATOM   6153  C CG    . GLN D 4 659  ? 115.426 139.384 168.300 1.00 86.21  ? 656  GLN A CG    1 
ATOM   6154  C CD    . GLN D 4 659  ? 116.198 138.092 168.113 1.00 86.21  ? 656  GLN A CD    1 
ATOM   6155  O OE1   . GLN D 4 659  ? 115.617 137.007 168.090 1.00 86.21  ? 656  GLN A OE1   1 
ATOM   6156  N NE2   . GLN D 4 659  ? 117.515 138.202 167.979 1.00 86.21  ? 656  GLN A NE2   1 
ATOM   6157  N N     . THR D 4 660  ? 111.664 140.760 166.284 1.00 92.42  ? 657  THR A N     1 
ATOM   6158  C CA    . THR D 4 660  ? 110.424 140.684 165.521 1.00 92.42  ? 657  THR A CA    1 
ATOM   6159  C C     . THR D 4 660  ? 109.980 139.253 165.252 1.00 92.42  ? 657  THR A C     1 
ATOM   6160  O O     . THR D 4 660  ? 108.831 139.049 164.844 1.00 92.42  ? 657  THR A O     1 
ATOM   6161  C CB    . THR D 4 660  ? 110.575 141.423 164.189 1.00 92.42  ? 657  THR A CB    1 
ATOM   6162  O OG1   . THR D 4 660  ? 111.796 141.023 163.555 1.00 92.42  ? 657  THR A OG1   1 
ATOM   6163  C CG2   . THR D 4 660  ? 110.593 142.926 164.410 1.00 92.42  ? 657  THR A CG2   1 
ATOM   6164  N N     . ALA D 4 661  ? 110.857 138.268 165.460 1.00 95.99  ? 658  ALA A N     1 
ATOM   6165  C CA    . ALA D 4 661  ? 110.487 136.879 165.211 1.00 95.99  ? 658  ALA A CA    1 
ATOM   6166  C C     . ALA D 4 661  ? 109.351 136.436 166.123 1.00 95.99  ? 658  ALA A C     1 
ATOM   6167  O O     . ALA D 4 661  ? 108.460 135.691 165.697 1.00 95.99  ? 658  ALA A O     1 
ATOM   6168  C CB    . ALA D 4 661  ? 111.703 135.972 165.389 1.00 95.99  ? 658  ALA A CB    1 
ATOM   6169  N N     . TYR D 4 662  ? 109.371 136.873 167.384 1.00 96.17  ? 659  TYR A N     1 
ATOM   6170  C CA    . TYR D 4 662  ? 108.306 136.504 168.311 1.00 96.17  ? 659  TYR A CA    1 
ATOM   6171  C C     . TYR D 4 662  ? 106.955 137.019 167.831 1.00 96.17  ? 659  TYR A C     1 
ATOM   6172  O O     . TYR D 4 662  ? 105.964 136.280 167.822 1.00 96.17  ? 659  TYR A O     1 
ATOM   6173  C CB    . TYR D 4 662  ? 108.611 137.041 169.709 1.00 96.17  ? 659  TYR A CB    1 
ATOM   6174  C CG    . TYR D 4 662  ? 107.533 136.718 170.715 1.00 96.17  ? 659  TYR A CG    1 
ATOM   6175  C CD1   . TYR D 4 662  ? 107.103 135.412 170.905 1.00 96.17  ? 659  TYR A CD1   1 
ATOM   6176  C CD2   . TYR D 4 662  ? 106.926 137.721 171.458 1.00 96.17  ? 659  TYR A CD2   1 
ATOM   6177  C CE1   . TYR D 4 662  ? 106.112 135.111 171.818 1.00 96.17  ? 659  TYR A CE1   1 
ATOM   6178  C CE2   . TYR D 4 662  ? 105.932 137.431 172.370 1.00 96.17  ? 659  TYR A CE2   1 
ATOM   6179  C CZ    . TYR D 4 662  ? 105.530 136.125 172.548 1.00 96.17  ? 659  TYR A CZ    1 
ATOM   6180  O OH    . TYR D 4 662  ? 104.541 135.831 173.458 1.00 96.17  ? 659  TYR A OH    1 
ATOM   6181  N N     . ALA D 4 663  ? 106.898 138.288 167.424 1.00 99.68  ? 660  ALA A N     1 
ATOM   6182  C CA    . ALA D 4 663  ? 105.642 138.850 166.938 1.00 99.68  ? 660  ALA A CA    1 
ATOM   6183  C C     . ALA D 4 663  ? 105.218 138.202 165.627 1.00 99.68  ? 660  ALA A C     1 
ATOM   6184  O O     . ALA D 4 663  ? 104.021 138.008 165.382 1.00 99.68  ? 660  ALA A O     1 
ATOM   6185  C CB    . ALA D 4 663  ? 105.773 140.364 166.773 1.00 99.68  ? 660  ALA A CB    1 
ATOM   6186  N N     . LYS D 4 664  ? 106.184 137.866 164.769 1.00 101.51 ? 661  LYS A N     1 
ATOM   6187  C CA    . LYS D 4 664  ? 105.861 137.238 163.492 1.00 101.51 ? 661  LYS A CA    1 
ATOM   6188  C C     . LYS D 4 664  ? 105.268 135.848 163.691 1.00 101.51 ? 661  LYS A C     1 
ATOM   6189  O O     . LYS D 4 664  ? 104.280 135.485 163.043 1.00 101.51 ? 661  LYS A O     1 
ATOM   6190  C CB    . LYS D 4 664  ? 107.112 137.171 162.616 1.00 101.51 ? 661  LYS A CB    1 
ATOM   6191  C CG    . LYS D 4 664  ? 106.846 136.767 161.176 1.00 101.51 ? 661  LYS A CG    1 
ATOM   6192  C CD    . LYS D 4 664  ? 108.128 136.336 160.481 1.00 101.51 ? 661  LYS A CD    1 
ATOM   6193  C CE    . LYS D 4 664  ? 109.118 137.487 160.386 1.00 101.51 ? 661  LYS A CE    1 
ATOM   6194  N NZ    . LYS D 4 664  ? 110.360 137.094 159.667 1.00 101.51 ? 661  LYS A NZ    1 
ATOM   6195  N N     . LYS D 4 665  ? 105.857 135.053 164.587 1.00 100.26 ? 662  LYS A N     1 
ATOM   6196  C CA    . LYS D 4 665  ? 105.407 133.681 164.780 1.00 100.26 ? 662  LYS A CA    1 
ATOM   6197  C C     . LYS D 4 665  ? 104.286 133.557 165.802 1.00 100.26 ? 662  LYS A C     1 
ATOM   6198  O O     . LYS D 4 665  ? 103.700 132.476 165.928 1.00 100.26 ? 662  LYS A O     1 
ATOM   6199  C CB    . LYS D 4 665  ? 106.580 132.796 165.206 1.00 100.26 ? 662  LYS A CB    1 
ATOM   6200  C CG    . LYS D 4 665  ? 107.003 132.982 166.653 1.00 100.26 ? 662  LYS A CG    1 
ATOM   6201  C CD    . LYS D 4 665  ? 108.010 131.925 167.074 1.00 100.26 ? 662  LYS A CD    1 
ATOM   6202  C CE    . LYS D 4 665  ? 107.341 130.575 167.267 1.00 100.26 ? 662  LYS A CE    1 
ATOM   6203  N NZ    . LYS D 4 665  ? 108.256 129.584 167.897 1.00 100.26 ? 662  LYS A NZ    1 
ATOM   6204  N N     . THR D 4 666  ? 103.974 134.624 166.532 1.00 100.36 ? 663  THR A N     1 
ATOM   6205  C CA    . THR D 4 666  ? 102.950 134.586 167.570 1.00 100.36 ? 663  THR A CA    1 
ATOM   6206  C C     . THR D 4 666  ? 101.783 135.521 167.307 1.00 100.36 ? 663  THR A C     1 
ATOM   6207  O O     . THR D 4 666  ? 100.629 135.122 167.475 1.00 100.36 ? 663  THR A O     1 
ATOM   6208  C CB    . THR D 4 666  ? 103.568 134.930 168.931 1.00 100.36 ? 663  THR A CB    1 
ATOM   6209  O OG1   . THR D 4 666  ? 104.738 134.130 169.142 1.00 100.36 ? 663  THR A OG1   1 
ATOM   6210  C CG2   . THR D 4 666  ? 102.573 134.669 170.052 1.00 100.36 ? 663  THR A CG2   1 
ATOM   6211  N N     . GLY D 4 667  ? 102.050 136.756 166.891 1.00 98.21  ? 664  GLY A N     1 
ATOM   6212  C CA    . GLY D 4 667  ? 101.005 137.739 166.715 1.00 98.21  ? 664  GLY A CA    1 
ATOM   6213  C C     . GLY D 4 667  ? 100.621 138.491 167.969 1.00 98.21  ? 664  GLY A C     1 
ATOM   6214  O O     . GLY D 4 667  ? 99.744  139.363 167.903 1.00 98.21  ? 664  GLY A O     1 
ATOM   6215  N N     . ASP D 4 668  ? 101.246 138.189 169.107 1.00 98.85  ? 665  ASP A N     1 
ATOM   6216  C CA    . ASP D 4 668  ? 100.970 138.888 170.361 1.00 98.85  ? 665  ASP A CA    1 
ATOM   6217  C C     . ASP D 4 668  ? 101.638 140.258 170.296 1.00 98.85  ? 665  ASP A C     1 
ATOM   6218  O O     . ASP D 4 668  ? 102.726 140.488 170.828 1.00 98.85  ? 665  ASP A O     1 
ATOM   6219  C CB    . ASP D 4 668  ? 101.461 138.074 171.551 1.00 98.85  ? 665  ASP A CB    1 
ATOM   6220  C CG    . ASP D 4 668  ? 101.075 138.692 172.880 1.00 98.85  ? 665  ASP A CG    1 
ATOM   6221  O OD1   . ASP D 4 668  ? 100.209 139.592 172.891 1.00 98.85  ? 665  ASP A OD1   1 
ATOM   6222  O OD2   . ASP D 4 668  ? 101.640 138.279 173.914 1.00 98.85  ? 665  ASP A OD2   1 
ATOM   6223  N N     . GLN D 4 669  ? 100.960 141.187 169.619 1.00 94.54  ? 666  GLN A N     1 
ATOM   6224  C CA    . GLN D 4 669  ? 101.532 142.512 169.411 1.00 94.54  ? 666  GLN A CA    1 
ATOM   6225  C C     . GLN D 4 669  ? 101.565 143.319 170.704 1.00 94.54  ? 666  GLN A C     1 
ATOM   6226  O O     . GLN D 4 669  ? 102.496 144.101 170.926 1.00 94.54  ? 666  GLN A O     1 
ATOM   6227  C CB    . GLN D 4 669  ? 100.749 143.258 168.333 1.00 94.54  ? 666  GLN A CB    1 
ATOM   6228  C CG    . GLN D 4 669  ? 101.471 144.474 167.775 1.00 94.54  ? 666  GLN A CG    1 
ATOM   6229  C CD    . GLN D 4 669  ? 102.771 144.111 167.084 1.00 94.54  ? 666  GLN A CD    1 
ATOM   6230  O OE1   . GLN D 4 669  ? 103.856 144.435 167.567 1.00 94.54  ? 666  GLN A OE1   1 
ATOM   6231  N NE2   . GLN D 4 669  ? 102.668 143.433 165.947 1.00 94.54  ? 666  GLN A NE2   1 
ATOM   6232  N N     . LYS D 4 670  ? 100.558 143.152 171.565 1.00 93.54  ? 667  LYS A N     1 
ATOM   6233  C CA    . LYS D 4 670  ? 100.511 143.928 172.802 1.00 93.54  ? 667  LYS A CA    1 
ATOM   6234  C C     . LYS D 4 670  ? 101.642 143.534 173.747 1.00 93.54  ? 667  LYS A C     1 
ATOM   6235  O O     . LYS D 4 670  ? 102.348 144.399 174.281 1.00 93.54  ? 667  LYS A O     1 
ATOM   6236  C CB    . LYS D 4 670  ? 99.149  143.760 173.479 1.00 93.54  ? 667  LYS A CB    1 
ATOM   6237  C CG    . LYS D 4 670  ? 98.649  142.326 173.551 1.00 93.54  ? 667  LYS A CG    1 
ATOM   6238  C CD    . LYS D 4 670  ? 97.239  142.262 174.115 1.00 93.54  ? 667  LYS A CD    1 
ATOM   6239  C CE    . LYS D 4 670  ? 97.169  142.895 175.496 1.00 93.54  ? 667  LYS A CE    1 
ATOM   6240  N NZ    . LYS D 4 670  ? 98.213  142.354 176.408 1.00 93.54  ? 667  LYS A NZ    1 
ATOM   6241  N N     . GLY D 4 671  ? 101.831 142.230 173.964 1.00 90.32  ? 668  GLY A N     1 
ATOM   6242  C CA    . GLY D 4 671  ? 102.942 141.783 174.787 1.00 90.32  ? 668  GLY A CA    1 
ATOM   6243  C C     . GLY D 4 671  ? 104.286 142.115 174.169 1.00 90.32  ? 668  GLY A C     1 
ATOM   6244  O O     . GLY D 4 671  ? 105.230 142.484 174.872 1.00 90.32  ? 668  GLY A O     1 
ATOM   6245  N N     . TYR D 4 672  ? 104.388 141.986 172.844 1.00 87.93  ? 669  TYR A N     1 
ATOM   6246  C CA    . TYR D 4 672  ? 105.592 142.398 172.130 1.00 87.93  ? 669  TYR A CA    1 
ATOM   6247  C C     . TYR D 4 672  ? 105.938 143.851 172.422 1.00 87.93  ? 669  TYR A C     1 
ATOM   6248  O O     . TYR D 4 672  ? 107.075 144.173 172.787 1.00 87.93  ? 669  TYR A O     1 
ATOM   6249  C CB    . TYR D 4 672  ? 105.392 142.189 170.629 1.00 87.93  ? 669  TYR A CB    1 
ATOM   6250  C CG    . TYR D 4 672  ? 106.587 142.550 169.783 1.00 87.93  ? 669  TYR A CG    1 
ATOM   6251  C CD1   . TYR D 4 672  ? 107.695 141.721 169.717 1.00 87.93  ? 669  TYR A CD1   1 
ATOM   6252  C CD2   . TYR D 4 672  ? 106.604 143.728 169.047 1.00 87.93  ? 669  TYR A CD2   1 
ATOM   6253  C CE1   . TYR D 4 672  ? 108.788 142.055 168.942 1.00 87.93  ? 669  TYR A CE1   1 
ATOM   6254  C CE2   . TYR D 4 672  ? 107.690 144.069 168.270 1.00 87.93  ? 669  TYR A CE2   1 
ATOM   6255  C CZ    . TYR D 4 672  ? 108.780 143.230 168.220 1.00 87.93  ? 669  TYR A CZ    1 
ATOM   6256  O OH    . TYR D 4 672  ? 109.865 143.568 167.447 1.00 87.93  ? 669  TYR A OH    1 
ATOM   6257  N N     . ARG D 4 673  ? 104.959 144.745 172.273 1.00 83.15  ? 670  ARG A N     1 
ATOM   6258  C CA    . ARG D 4 673  ? 105.220 146.166 172.467 1.00 83.15  ? 670  ARG A CA    1 
ATOM   6259  C C     . ARG D 4 673  ? 105.520 146.482 173.925 1.00 83.15  ? 670  ARG A C     1 
ATOM   6260  O O     . ARG D 4 673  ? 106.371 147.329 174.215 1.00 83.15  ? 670  ARG A O     1 
ATOM   6261  C CB    . ARG D 4 673  ? 104.036 146.992 171.969 1.00 83.15  ? 670  ARG A CB    1 
ATOM   6262  C CG    . ARG D 4 673  ? 104.333 148.476 171.849 1.00 83.15  ? 670  ARG A CG    1 
ATOM   6263  C CD    . ARG D 4 673  ? 105.604 148.714 171.048 1.00 83.15  ? 670  ARG A CD    1 
ATOM   6264  N NE    . ARG D 4 673  ? 105.498 148.204 169.686 1.00 83.15  ? 670  ARG A NE    1 
ATOM   6265  C CZ    . ARG D 4 673  ? 104.819 148.795 168.713 1.00 83.15  ? 670  ARG A CZ    1 
ATOM   6266  N NH1   . ARG D 4 673  ? 104.173 149.933 168.912 1.00 83.15  ? 670  ARG A NH1   1 
ATOM   6267  N NH2   . ARG D 4 673  ? 104.788 148.232 167.508 1.00 83.15  ? 670  ARG A NH2   1 
ATOM   6268  N N     . GLU D 4 674  ? 104.833 145.819 174.859 1.00 80.95  ? 671  GLU A N     1 
ATOM   6269  C CA    . GLU D 4 674  ? 105.112 146.062 176.271 1.00 80.95  ? 671  GLU A CA    1 
ATOM   6270  C C     . GLU D 4 674  ? 106.523 145.616 176.642 1.00 80.95  ? 671  GLU A C     1 
ATOM   6271  O O     . GLU D 4 674  ? 107.244 146.336 177.346 1.00 80.95  ? 671  GLU A O     1 
ATOM   6272  C CB    . GLU D 4 674  ? 104.074 145.355 177.142 1.00 80.95  ? 671  GLU A CB    1 
ATOM   6273  C CG    . GLU D 4 674  ? 104.011 145.874 178.571 1.00 80.95  ? 671  GLU A CG    1 
ATOM   6274  C CD    . GLU D 4 674  ? 103.727 147.364 178.645 1.00 80.95  ? 671  GLU A CD    1 
ATOM   6275  O OE1   . GLU D 4 674  ? 102.987 147.878 177.779 1.00 80.95  ? 671  GLU A OE1   1 
ATOM   6276  O OE2   . GLU D 4 674  ? 104.247 148.023 179.570 1.00 80.95  ? 671  GLU A OE2   1 
ATOM   6277  N N     . ALA D 4 675  ? 106.938 144.437 176.170 1.00 76.97  ? 672  ALA A N     1 
ATOM   6278  C CA    . ALA D 4 675  ? 108.296 143.973 176.430 1.00 76.97  ? 672  ALA A CA    1 
ATOM   6279  C C     . ALA D 4 675  ? 109.323 144.895 175.786 1.00 76.97  ? 672  ALA A C     1 
ATOM   6280  O O     . ALA D 4 675  ? 110.365 145.189 176.383 1.00 76.97  ? 672  ALA A O     1 
ATOM   6281  C CB    . ALA D 4 675  ? 108.467 142.541 175.926 1.00 76.97  ? 672  ALA A CB    1 
ATOM   6282  N N     . LEU D 4 676  ? 109.046 145.359 174.565 1.00 74.94  ? 673  LEU A N     1 
ATOM   6283  C CA    . LEU D 4 676  ? 109.959 146.283 173.902 1.00 74.94  ? 673  LEU A CA    1 
ATOM   6284  C C     . LEU D 4 676  ? 110.086 147.584 174.683 1.00 74.94  ? 673  LEU A C     1 
ATOM   6285  O O     . LEU D 4 676  ? 111.191 148.108 174.851 1.00 74.94  ? 673  LEU A O     1 
ATOM   6286  C CB    . LEU D 4 676  ? 109.477 146.553 172.477 1.00 74.94  ? 673  LEU A CB    1 
ATOM   6287  C CG    . LEU D 4 676  ? 110.447 147.223 171.505 1.00 74.94  ? 673  LEU A CG    1 
ATOM   6288  C CD1   . LEU D 4 676  ? 110.261 146.644 170.114 1.00 74.94  ? 673  LEU A CD1   1 
ATOM   6289  C CD2   . LEU D 4 676  ? 110.249 148.731 171.486 1.00 74.94  ? 673  LEU A CD2   1 
ATOM   6290  N N     . CYS D 4 677  ? 108.963 148.119 175.166 1.00 71.83  ? 674  CYS A N     1 
ATOM   6291  C CA    . CYS D 4 677  ? 109.003 149.351 175.946 1.00 71.83  ? 674  CYS A CA    1 
ATOM   6292  C C     . CYS D 4 677  ? 109.787 149.157 177.236 1.00 71.83  ? 674  CYS A C     1 
ATOM   6293  O O     . CYS D 4 677  ? 110.580 150.022 177.625 1.00 71.83  ? 674  CYS A O     1 
ATOM   6294  C CB    . CYS D 4 677  ? 107.583 149.829 176.248 1.00 71.83  ? 674  CYS A CB    1 
ATOM   6295  S SG    . CYS D 4 677  ? 106.724 150.564 174.838 1.00 71.83  ? 674  CYS A SG    1 
ATOM   6296  N N     . LYS D 4 678  ? 109.580 148.024 177.913 1.00 73.71  ? 675  LYS A N     1 
ATOM   6297  C CA    . LYS D 4 678  ? 110.332 147.753 179.135 1.00 73.71  ? 675  LYS A CA    1 
ATOM   6298  C C     . LYS D 4 678  ? 111.826 147.658 178.851 1.00 73.71  ? 675  LYS A C     1 
ATOM   6299  O O     . LYS D 4 678  ? 112.645 148.207 179.599 1.00 73.71  ? 675  LYS A O     1 
ATOM   6300  C CB    . LYS D 4 678  ? 109.828 146.467 179.789 1.00 73.71  ? 675  LYS A CB    1 
ATOM   6301  C CG    . LYS D 4 678  ? 108.426 146.569 180.364 1.00 73.71  ? 675  LYS A CG    1 
ATOM   6302  C CD    . LYS D 4 678  ? 108.090 145.354 181.212 1.00 73.71  ? 675  LYS A CD    1 
ATOM   6303  C CE    . LYS D 4 678  ? 107.944 144.105 180.358 1.00 73.71  ? 675  LYS A CE    1 
ATOM   6304  N NZ    . LYS D 4 678  ? 106.752 144.174 179.471 1.00 73.71  ? 675  LYS A NZ    1 
ATOM   6305  N N     . TRP D 4 679  ? 112.199 146.972 177.769 1.00 67.31  ? 676  TRP A N     1 
ATOM   6306  C CA    . TRP D 4 679  ? 113.611 146.835 177.429 1.00 67.31  ? 676  TRP A CA    1 
ATOM   6307  C C     . TRP D 4 679  ? 114.233 148.180 177.074 1.00 67.31  ? 676  TRP A C     1 
ATOM   6308  O O     . TRP D 4 679  ? 115.370 148.463 177.465 1.00 67.31  ? 676  TRP A O     1 
ATOM   6309  C CB    . TRP D 4 679  ? 113.782 145.842 176.282 1.00 67.31  ? 676  TRP A CB    1 
ATOM   6310  C CG    . TRP D 4 679  ? 115.201 145.677 175.833 1.00 67.31  ? 676  TRP A CG    1 
ATOM   6311  C CD1   . TRP D 4 679  ? 115.726 146.055 174.635 1.00 67.31  ? 676  TRP A CD1   1 
ATOM   6312  C CD2   . TRP D 4 679  ? 116.278 145.095 176.577 1.00 67.31  ? 676  TRP A CD2   1 
ATOM   6313  N NE1   . TRP D 4 679  ? 117.061 145.740 174.582 1.00 67.31  ? 676  TRP A NE1   1 
ATOM   6314  C CE2   . TRP D 4 679  ? 117.425 145.150 175.763 1.00 67.31  ? 676  TRP A CE2   1 
ATOM   6315  C CE3   . TRP D 4 679  ? 116.383 144.530 177.852 1.00 67.31  ? 676  TRP A CE3   1 
ATOM   6316  C CZ2   . TRP D 4 679  ? 118.661 144.663 176.180 1.00 67.31  ? 676  TRP A CZ2   1 
ATOM   6317  C CZ3   . TRP D 4 679  ? 117.611 144.045 178.262 1.00 67.31  ? 676  TRP A CZ3   1 
ATOM   6318  C CH2   . TRP D 4 679  ? 118.733 144.117 177.430 1.00 67.31  ? 676  TRP A CH2   1 
ATOM   6319  N N     . ILE D 4 680  ? 113.509 149.023 176.335 1.00 67.06  ? 677  ILE A N     1 
ATOM   6320  C CA    . ILE D 4 680  ? 114.051 150.329 175.975 1.00 67.06  ? 677  ILE A CA    1 
ATOM   6321  C C     . ILE D 4 680  ? 114.176 151.216 177.208 1.00 67.06  ? 677  ILE A C     1 
ATOM   6322  O O     . ILE D 4 680  ? 115.137 151.982 177.340 1.00 67.06  ? 677  ILE A O     1 
ATOM   6323  C CB    . ILE D 4 680  ? 113.195 150.993 174.882 1.00 67.06  ? 677  ILE A CB    1 
ATOM   6324  C CG1   . ILE D 4 680  ? 113.155 150.119 173.631 1.00 67.06  ? 677  ILE A CG1   1 
ATOM   6325  C CG2   . ILE D 4 680  ? 113.758 152.352 174.522 1.00 67.06  ? 677  ILE A CG2   1 
ATOM   6326  C CD1   . ILE D 4 680  ? 114.503 149.895 173.009 1.00 67.06  ? 677  ILE A CD1   1 
ATOM   6327  N N     . ASP D 4 681  ? 113.213 151.131 178.129 1.00 71.23  ? 678  ASP A N     1 
ATOM   6328  C CA    . ASP D 4 681  ? 113.324 151.885 179.373 1.00 71.23  ? 678  ASP A CA    1 
ATOM   6329  C C     . ASP D 4 681  ? 114.532 151.432 180.180 1.00 71.23  ? 678  ASP A C     1 
ATOM   6330  O O     . ASP D 4 681  ? 115.267 152.259 180.735 1.00 71.23  ? 678  ASP A O     1 
ATOM   6331  C CB    . ASP D 4 681  ? 112.043 151.737 180.193 1.00 71.23  ? 678  ASP A CB    1 
ATOM   6332  C CG    . ASP D 4 681  ? 110.920 152.616 179.681 1.00 71.23  ? 678  ASP A CG    1 
ATOM   6333  O OD1   . ASP D 4 681  ? 111.203 153.755 179.255 1.00 71.23  ? 678  ASP A OD1   1 
ATOM   6334  O OD2   . ASP D 4 681  ? 109.755 152.167 179.704 1.00 71.23  ? 678  ASP A OD2   1 
ATOM   6335  N N     . PHE D 4 682  ? 114.758 150.118 180.251 1.00 66.42  ? 679  PHE A N     1 
ATOM   6336  C CA    . PHE D 4 682  ? 115.932 149.611 180.952 1.00 66.42  ? 679  PHE A CA    1 
ATOM   6337  C C     . PHE D 4 682  ? 117.216 150.067 180.271 1.00 66.42  ? 679  PHE A C     1 
ATOM   6338  O O     . PHE D 4 682  ? 118.201 150.391 180.941 1.00 66.42  ? 679  PHE A O     1 
ATOM   6339  C CB    . PHE D 4 682  ? 115.879 148.087 181.034 1.00 66.42  ? 679  PHE A CB    1 
ATOM   6340  C CG    . PHE D 4 682  ? 117.206 147.453 181.330 1.00 66.42  ? 679  PHE A CG    1 
ATOM   6341  C CD1   . PHE D 4 682  ? 117.790 147.593 182.576 1.00 66.42  ? 679  PHE A CD1   1 
ATOM   6342  C CD2   . PHE D 4 682  ? 117.869 146.720 180.363 1.00 66.42  ? 679  PHE A CD2   1 
ATOM   6343  C CE1   . PHE D 4 682  ? 119.009 147.012 182.854 1.00 66.42  ? 679  PHE A CE1   1 
ATOM   6344  C CE2   . PHE D 4 682  ? 119.090 146.137 180.634 1.00 66.42  ? 679  PHE A CE2   1 
ATOM   6345  C CZ    . PHE D 4 682  ? 119.660 146.282 181.881 1.00 66.42  ? 679  PHE A CZ    1 
ATOM   6346  N N     . THR D 4 683  ? 117.225 150.089 178.936 1.00 64.25  ? 680  THR A N     1 
ATOM   6347  C CA    . THR D 4 683  ? 118.399 150.554 178.205 1.00 64.25  ? 680  THR A CA    1 
ATOM   6348  C C     . THR D 4 683  ? 118.681 152.024 178.490 1.00 64.25  ? 680  THR A C     1 
ATOM   6349  O O     . THR D 4 683  ? 119.835 152.412 178.703 1.00 64.25  ? 680  THR A O     1 
ATOM   6350  C CB    . THR D 4 683  ? 118.206 150.327 176.705 1.00 64.25  ? 680  THR A CB    1 
ATOM   6351  O OG1   . THR D 4 683  ? 118.090 148.923 176.445 1.00 64.25  ? 680  THR A OG1   1 
ATOM   6352  C CG2   . THR D 4 683  ? 119.384 150.880 175.925 1.00 64.25  ? 680  THR A CG2   1 
ATOM   6353  N N     . ARG D 4 684  ? 117.639 152.858 178.499 1.00 68.46  ? 681  ARG A N     1 
ATOM   6354  C CA    . ARG D 4 684  ? 117.823 154.269 178.825 1.00 68.46  ? 681  ARG A CA    1 
ATOM   6355  C C     . ARG D 4 684  ? 118.333 154.443 180.250 1.00 68.46  ? 681  ARG A C     1 
ATOM   6356  O O     . ARG D 4 684  ? 119.216 155.272 180.507 1.00 68.46  ? 681  ARG A O     1 
ATOM   6357  C CB    . ARG D 4 684  ? 116.513 155.033 178.631 1.00 68.46  ? 681  ARG A CB    1 
ATOM   6358  C CG    . ARG D 4 684  ? 115.983 155.023 177.209 1.00 68.46  ? 681  ARG A CG    1 
ATOM   6359  C CD    . ARG D 4 684  ? 116.923 155.754 176.265 1.00 68.46  ? 681  ARG A CD    1 
ATOM   6360  N NE    . ARG D 4 684  ? 116.871 157.200 176.447 1.00 68.46  ? 681  ARG A NE    1 
ATOM   6361  C CZ    . ARG D 4 684  ? 115.873 157.973 176.042 1.00 68.46  ? 681  ARG A CZ    1 
ATOM   6362  N NH1   . ARG D 4 684  ? 114.821 157.474 175.415 1.00 68.46  ? 681  ARG A NH1   1 
ATOM   6363  N NH2   . ARG D 4 684  ? 115.933 159.282 176.270 1.00 68.46  ? 681  ARG A NH2   1 
ATOM   6364  N N     . ASP D 4 685  ? 117.789 153.668 181.190 1.00 67.60  ? 682  ASP A N     1 
ATOM   6365  C CA    . ASP D 4 685  ? 118.258 153.746 182.569 1.00 67.60  ? 682  ASP A CA    1 
ATOM   6366  C C     . ASP D 4 685  ? 119.723 153.338 182.672 1.00 67.60  ? 682  ASP A C     1 
ATOM   6367  O O     . ASP D 4 685  ? 120.507 153.979 183.381 1.00 67.60  ? 682  ASP A O     1 
ATOM   6368  C CB    . ASP D 4 685  ? 117.388 152.865 183.465 1.00 67.60  ? 682  ASP A CB    1 
ATOM   6369  C CG    . ASP D 4 685  ? 117.456 153.271 184.922 1.00 67.60  ? 682  ASP A CG    1 
ATOM   6370  O OD1   . ASP D 4 685  ? 117.939 154.387 185.203 1.00 67.60  ? 682  ASP A OD1   1 
ATOM   6371  O OD2   . ASP D 4 685  ? 117.026 152.475 185.783 1.00 67.60  ? 682  ASP A OD2   1 
ATOM   6372  N N     . PHE D 4 686  ? 120.109 152.275 181.963 1.00 60.70  ? 683  PHE A N     1 
ATOM   6373  C CA    . PHE D 4 686  ? 121.498 151.830 181.968 1.00 60.70  ? 683  PHE A CA    1 
ATOM   6374  C C     . PHE D 4 686  ? 122.416 152.888 181.373 1.00 60.70  ? 683  PHE A C     1 
ATOM   6375  O O     . PHE D 4 686  ? 123.513 153.132 181.889 1.00 60.70  ? 683  PHE A O     1 
ATOM   6376  C CB    . PHE D 4 686  ? 121.619 150.516 181.199 1.00 60.70  ? 683  PHE A CB    1 
ATOM   6377  C CG    . PHE D 4 686  ? 123.032 150.053 181.002 1.00 60.70  ? 683  PHE A CG    1 
ATOM   6378  C CD1   . PHE D 4 686  ? 123.686 149.348 181.996 1.00 60.70  ? 683  PHE A CD1   1 
ATOM   6379  C CD2   . PHE D 4 686  ? 123.705 150.315 179.823 1.00 60.70  ? 683  PHE A CD2   1 
ATOM   6380  C CE1   . PHE D 4 686  ? 124.983 148.917 181.816 1.00 60.70  ? 683  PHE A CE1   1 
ATOM   6381  C CE2   . PHE D 4 686  ? 125.002 149.888 179.641 1.00 60.70  ? 683  PHE A CE2   1 
ATOM   6382  C CZ    . PHE D 4 686  ? 125.641 149.187 180.636 1.00 60.70  ? 683  PHE A CZ    1 
ATOM   6383  N N     . LEU D 4 687  ? 121.987 153.522 180.279 1.00 61.12  ? 684  LEU A N     1 
ATOM   6384  C CA    . LEU D 4 687  ? 122.781 154.588 179.679 1.00 61.12  ? 684  LEU A CA    1 
ATOM   6385  C C     . LEU D 4 687  ? 122.952 155.750 180.646 1.00 61.12  ? 684  LEU A C     1 
ATOM   6386  O O     . LEU D 4 687  ? 124.040 156.327 180.751 1.00 61.12  ? 684  LEU A O     1 
ATOM   6387  C CB    . LEU D 4 687  ? 122.127 155.065 178.381 1.00 61.12  ? 684  LEU A CB    1 
ATOM   6388  C CG    . LEU D 4 687  ? 122.592 154.460 177.053 1.00 61.12  ? 684  LEU A CG    1 
ATOM   6389  C CD1   . LEU D 4 687  ? 124.018 154.867 176.747 1.00 61.12  ? 684  LEU A CD1   1 
ATOM   6390  C CD2   . LEU D 4 687  ? 122.464 152.951 177.055 1.00 61.12  ? 684  LEU A CD2   1 
ATOM   6391  N N     . SER D 4 688  ? 121.885 156.107 181.362 1.00 64.54  ? 685  SER A N     1 
ATOM   6392  C CA    . SER D 4 688  ? 121.981 157.183 182.343 1.00 64.54  ? 685  SER A CA    1 
ATOM   6393  C C     . SER D 4 688  ? 122.925 156.816 183.480 1.00 64.54  ? 685  SER A C     1 
ATOM   6394  O O     . SER D 4 688  ? 123.704 157.656 183.947 1.00 64.54  ? 685  SER A O     1 
ATOM   6395  C CB    . SER D 4 688  ? 120.595 157.515 182.892 1.00 64.54  ? 685  SER A CB    1 
ATOM   6396  O OG    . SER D 4 688  ? 120.217 156.593 183.899 1.00 64.54  ? 685  SER A OG    1 
ATOM   6397  N N     . LYS D 4 689  ? 122.873 155.567 183.938 1.00 67.68  ? 686  LYS A N     1 
ATOM   6398  C CA    . LYS D 4 689  ? 123.570 155.169 185.153 1.00 67.68  ? 686  LYS A CA    1 
ATOM   6399  C C     . LYS D 4 689  ? 124.997 154.692 184.915 1.00 67.68  ? 686  LYS A C     1 
ATOM   6400  O O     . LYS D 4 689  ? 125.774 154.619 185.875 1.00 67.68  ? 686  LYS A O     1 
ATOM   6401  C CB    . LYS D 4 689  ? 122.779 154.067 185.863 1.00 67.68  ? 686  LYS A CB    1 
ATOM   6402  C CG    . LYS D 4 689  ? 121.409 154.510 186.353 1.00 67.68  ? 686  LYS A CG    1 
ATOM   6403  C CD    . LYS D 4 689  ? 120.789 153.473 187.269 1.00 67.68  ? 686  LYS A CD    1 
ATOM   6404  C CE    . LYS D 4 689  ? 119.512 153.978 187.916 1.00 67.68  ? 686  LYS A CE    1 
ATOM   6405  N NZ    . LYS D 4 689  ? 119.081 153.103 189.042 1.00 67.68  ? 686  LYS A NZ    1 
ATOM   6406  N N     . TYR D 4 690  ? 125.366 154.371 183.678 1.00 58.97  ? 687  TYR A N     1 
ATOM   6407  C CA    . TYR D 4 690  ? 126.709 153.873 183.410 1.00 58.97  ? 687  TYR A CA    1 
ATOM   6408  C C     . TYR D 4 690  ? 127.744 154.978 183.594 1.00 58.97  ? 687  TYR A C     1 
ATOM   6409  O O     . TYR D 4 690  ? 127.453 156.165 183.438 1.00 58.97  ? 687  TYR A O     1 
ATOM   6410  C CB    . TYR D 4 690  ? 126.800 153.296 181.999 1.00 58.97  ? 687  TYR A CB    1 
ATOM   6411  C CG    . TYR D 4 690  ? 127.925 152.302 181.830 1.00 58.97  ? 687  TYR A CG    1 
ATOM   6412  C CD1   . TYR D 4 690  ? 127.838 151.030 182.374 1.00 58.97  ? 687  TYR A CD1   1 
ATOM   6413  C CD2   . TYR D 4 690  ? 129.074 152.635 181.129 1.00 58.97  ? 687  TYR A CD2   1 
ATOM   6414  C CE1   . TYR D 4 690  ? 128.860 150.117 182.225 1.00 58.97  ? 687  TYR A CE1   1 
ATOM   6415  C CE2   . TYR D 4 690  ? 130.103 151.727 180.974 1.00 58.97  ? 687  TYR A CE2   1 
ATOM   6416  C CZ    . TYR D 4 690  ? 129.990 150.471 181.525 1.00 58.97  ? 687  TYR A CZ    1 
ATOM   6417  O OH    . TYR D 4 690  ? 131.011 149.563 181.374 1.00 58.97  ? 687  TYR A OH    1 
ATOM   6418  N N     . THR D 4 691  ? 128.968 154.567 183.934 1.00 59.48  ? 688  THR A N     1 
ATOM   6419  C CA    . THR D 4 691  ? 130.008 155.531 184.282 1.00 59.48  ? 688  THR A CA    1 
ATOM   6420  C C     . THR D 4 691  ? 130.363 156.434 183.106 1.00 59.48  ? 688  THR A C     1 
ATOM   6421  O O     . THR D 4 691  ? 130.486 157.654 183.268 1.00 59.48  ? 688  THR A O     1 
ATOM   6422  C CB    . THR D 4 691  ? 131.255 154.800 184.781 1.00 59.48  ? 688  THR A CB    1 
ATOM   6423  O OG1   . THR D 4 691  ? 130.912 153.981 185.905 1.00 59.48  ? 688  THR A OG1   1 
ATOM   6424  C CG2   . THR D 4 691  ? 132.327 155.794 185.196 1.00 59.48  ? 688  THR A CG2   1 
ATOM   6425  N N     . LYS D 4 692  ? 130.527 155.859 181.916 1.00 53.26  ? 689  LYS A N     1 
ATOM   6426  C CA    . LYS D 4 692  ? 131.024 156.621 180.778 1.00 53.26  ? 689  LYS A CA    1 
ATOM   6427  C C     . LYS D 4 692  ? 129.922 157.270 179.952 1.00 53.26  ? 689  LYS A C     1 
ATOM   6428  O O     . LYS D 4 692  ? 130.191 158.259 179.261 1.00 53.26  ? 689  LYS A O     1 
ATOM   6429  C CB    . LYS D 4 692  ? 131.874 155.724 179.873 1.00 53.26  ? 689  LYS A CB    1 
ATOM   6430  C CG    . LYS D 4 692  ? 131.067 154.792 178.995 1.00 53.26  ? 689  LYS A CG    1 
ATOM   6431  C CD    . LYS D 4 692  ? 131.966 153.890 178.181 1.00 53.26  ? 689  LYS A CD    1 
ATOM   6432  C CE    . LYS D 4 692  ? 132.701 154.670 177.108 1.00 53.26  ? 689  LYS A CE    1 
ATOM   6433  N NZ    . LYS D 4 692  ? 131.782 155.130 176.031 1.00 53.26  ? 689  LYS A NZ    1 
ATOM   6434  N N     . THR D 4 693  ? 128.700 156.746 179.999 1.00 60.90  ? 690  THR A N     1 
ATOM   6435  C CA    . THR D 4 693  ? 127.596 157.277 179.214 1.00 60.90  ? 690  THR A CA    1 
ATOM   6436  C C     . THR D 4 693  ? 126.608 158.082 180.049 1.00 60.90  ? 690  THR A C     1 
ATOM   6437  O O     . THR D 4 693  ? 125.507 158.376 179.573 1.00 60.90  ? 690  THR A O     1 
ATOM   6438  C CB    . THR D 4 693  ? 126.862 156.143 178.498 1.00 60.90  ? 690  THR A CB    1 
ATOM   6439  O OG1   . THR D 4 693  ? 126.263 155.274 179.466 1.00 60.90  ? 690  THR A OG1   1 
ATOM   6440  C CG2   . THR D 4 693  ? 127.821 155.347 177.633 1.00 60.90  ? 690  THR A CG2   1 
ATOM   6441  N N     . THR D 4 694  ? 126.975 158.446 181.279 1.00 64.02  ? 691  THR A N     1 
ATOM   6442  C CA    . THR D 4 694  ? 126.039 159.143 182.155 1.00 64.02  ? 691  THR A CA    1 
ATOM   6443  C C     . THR D 4 694  ? 125.719 160.546 181.656 1.00 64.02  ? 691  THR A C     1 
ATOM   6444  O O     . THR D 4 694  ? 124.694 161.118 182.045 1.00 64.02  ? 691  THR A O     1 
ATOM   6445  C CB    . THR D 4 694  ? 126.599 159.218 183.574 1.00 64.02  ? 691  THR A CB    1 
ATOM   6446  O OG1   . THR D 4 694  ? 125.702 159.965 184.405 1.00 64.02  ? 691  THR A OG1   1 
ATOM   6447  C CG2   . THR D 4 694  ? 127.962 159.893 183.574 1.00 64.02  ? 691  THR A CG2   1 
ATOM   6448  N N     . SER D 4 695  ? 126.568 161.117 180.804 1.00 67.01  ? 692  SER A N     1 
ATOM   6449  C CA    . SER D 4 695  ? 126.446 162.516 180.426 1.00 67.01  ? 692  SER A CA    1 
ATOM   6450  C C     . SER D 4 695  ? 126.306 162.741 178.927 1.00 67.01  ? 692  SER A C     1 
ATOM   6451  O O     . SER D 4 695  ? 126.128 163.889 178.507 1.00 67.01  ? 692  SER A O     1 
ATOM   6452  C CB    . SER D 4 695  ? 127.655 163.302 180.945 1.00 67.01  ? 692  SER A CB    1 
ATOM   6453  O OG    . SER D 4 695  ? 127.701 163.290 182.360 1.00 67.01  ? 692  SER A OG    1 
ATOM   6454  N N     . ILE D 4 696  ? 126.376 161.696 178.109 1.00 62.56  ? 693  ILE A N     1 
ATOM   6455  C CA    . ILE D 4 696  ? 126.457 161.875 176.648 1.00 62.56  ? 693  ILE A CA    1 
ATOM   6456  C C     . ILE D 4 696  ? 125.025 161.919 176.122 1.00 62.56  ? 693  ILE A C     1 
ATOM   6457  O O     . ILE D 4 696  ? 124.460 160.936 175.635 1.00 62.56  ? 693  ILE A O     1 
ATOM   6458  C CB    . ILE D 4 696  ? 127.339 160.805 175.982 1.00 62.56  ? 693  ILE A CB    1 
ATOM   6459  C CG1   . ILE D 4 696  ? 127.606 161.152 174.513 1.00 62.56  ? 693  ILE A CG1   1 
ATOM   6460  C CG2   . ILE D 4 696  ? 126.825 159.374 176.218 1.00 62.56  ? 693  ILE A CG2   1 
ATOM   6461  C CD1   . ILE D 4 696  ? 128.712 160.333 173.887 1.00 62.56  ? 693  ILE A CD1   1 
ATOM   6462  N N     . ASP D 4 697  ? 124.424 163.108 176.227 1.00 70.82  ? 694  ASP A N     1 
ATOM   6463  C CA    . ASP D 4 697  ? 123.214 163.525 175.501 1.00 70.82  ? 694  ASP A CA    1 
ATOM   6464  C C     . ASP D 4 697  ? 122.238 162.377 175.246 1.00 70.82  ? 694  ASP A C     1 
ATOM   6465  O O     . ASP D 4 697  ? 121.847 162.096 174.112 1.00 70.82  ? 694  ASP A O     1 
ATOM   6466  C CB    . ASP D 4 697  ? 123.588 164.214 174.190 1.00 70.82  ? 694  ASP A CB    1 
ATOM   6467  C CG    . ASP D 4 697  ? 124.100 165.626 174.402 1.00 70.82  ? 694  ASP A CG    1 
ATOM   6468  O OD1   . ASP D 4 697  ? 124.706 165.887 175.462 1.00 70.82  ? 694  ASP A OD1   1 
ATOM   6469  O OD2   . ASP D 4 697  ? 123.892 166.476 173.510 1.00 70.82  ? 694  ASP A OD2   1 
ATOM   6470  N N     . LEU D 4 698  ? 121.838 161.704 176.325 1.00 73.72  ? 695  LEU A N     1 
ATOM   6471  C CA    . LEU D 4 698  ? 120.903 160.594 176.186 1.00 73.72  ? 695  LEU A CA    1 
ATOM   6472  C C     . LEU D 4 698  ? 119.478 161.063 175.924 1.00 73.72  ? 695  LEU A C     1 
ATOM   6473  O O     . LEU D 4 698  ? 118.668 160.284 175.411 1.00 73.72  ? 695  LEU A O     1 
ATOM   6474  C CB    . LEU D 4 698  ? 120.924 159.709 177.436 1.00 73.72  ? 695  LEU A CB    1 
ATOM   6475  C CG    . LEU D 4 698  ? 120.269 160.229 178.720 1.00 73.72  ? 695  LEU A CG    1 
ATOM   6476  C CD1   . LEU D 4 698  ? 120.049 159.079 179.685 1.00 73.72  ? 695  LEU A CD1   1 
ATOM   6477  C CD2   . LEU D 4 698  ? 121.100 161.318 179.386 1.00 73.72  ? 695  LEU A CD2   1 
ATOM   6478  N N     . SER D 4 699  ? 119.155 162.315 176.257 1.00 79.19  ? 696  SER A N     1 
ATOM   6479  C CA    . SER D 4 699  ? 117.780 162.790 176.148 1.00 79.19  ? 696  SER A CA    1 
ATOM   6480  C C     . SER D 4 699  ? 117.364 163.078 174.712 1.00 79.19  ? 696  SER A C     1 
ATOM   6481  O O     . SER D 4 699  ? 116.176 163.306 174.461 1.00 79.19  ? 696  SER A O     1 
ATOM   6482  C CB    . SER D 4 699  ? 117.592 164.045 177.001 1.00 79.19  ? 696  SER A CB    1 
ATOM   6483  O OG    . SER D 4 699  ? 118.401 165.108 176.526 1.00 79.19  ? 696  SER A OG    1 
ATOM   6484  N N     . SER D 4 700  ? 118.306 163.075 173.766 1.00 76.52  ? 697  SER A N     1 
ATOM   6485  C CA    . SER D 4 700  ? 117.975 163.403 172.384 1.00 76.52  ? 697  SER A CA    1 
ATOM   6486  C C     . SER D 4 700  ? 117.125 162.332 171.711 1.00 76.52  ? 697  SER A C     1 
ATOM   6487  O O     . SER D 4 700  ? 116.583 162.581 170.630 1.00 76.52  ? 697  SER A O     1 
ATOM   6488  C CB    . SER D 4 700  ? 119.253 163.631 171.577 1.00 76.52  ? 697  SER A CB    1 
ATOM   6489  O OG    . SER D 4 700  ? 118.958 163.842 170.207 1.00 76.52  ? 697  SER A OG    1 
ATOM   6490  N N     . LEU D 4 701  ? 117.001 161.154 172.316 1.00 70.93  ? 698  LEU A N     1 
ATOM   6491  C CA    . LEU D 4 701  ? 116.220 160.084 171.714 1.00 70.93  ? 698  LEU A CA    1 
ATOM   6492  C C     . LEU D 4 701  ? 114.726 160.374 171.804 1.00 70.93  ? 698  LEU A C     1 
ATOM   6493  O O     . LEU D 4 701  ? 114.261 161.121 172.669 1.00 70.93  ? 698  LEU A O     1 
ATOM   6494  C CB    . LEU D 4 701  ? 116.530 158.748 172.388 1.00 70.93  ? 698  LEU A CB    1 
ATOM   6495  C CG    . LEU D 4 701  ? 117.947 158.206 172.201 1.00 70.93  ? 698  LEU A CG    1 
ATOM   6496  C CD1   . LEU D 4 701  ? 118.154 156.956 173.034 1.00 70.93  ? 698  LEU A CD1   1 
ATOM   6497  C CD2   . LEU D 4 701  ? 118.204 157.916 170.732 1.00 70.93  ? 698  LEU A CD2   1 
ATOM   6498  N N     . ARG D 4 702  ? 113.974 159.770 170.888 1.00 69.72  ? 699  ARG A N     1 
ATOM   6499  C CA    . ARG D 4 702  ? 112.529 159.891 170.887 1.00 69.72  ? 699  ARG A CA    1 
ATOM   6500  C C     . ARG D 4 702  ? 111.932 159.081 172.036 1.00 69.72  ? 699  ARG A C     1 
ATOM   6501  O O     . ARG D 4 702  ? 112.601 158.220 172.613 1.00 69.72  ? 699  ARG A O     1 
ATOM   6502  C CB    . ARG D 4 702  ? 111.964 159.420 169.549 1.00 69.72  ? 699  ARG A CB    1 
ATOM   6503  C CG    . ARG D 4 702  ? 112.512 160.172 168.347 1.00 69.72  ? 699  ARG A CG    1 
ATOM   6504  C CD    . ARG D 4 702  ? 111.582 160.057 167.149 1.00 69.72  ? 699  ARG A CD    1 
ATOM   6505  N NE    . ARG D 4 702  ? 111.879 158.887 166.332 1.00 69.72  ? 699  ARG A NE    1 
ATOM   6506  C CZ    . ARG D 4 702  ? 111.152 157.779 166.317 1.00 69.72  ? 699  ARG A CZ    1 
ATOM   6507  N NH1   . ARG D 4 702  ? 110.071 157.652 167.071 1.00 69.72  ? 699  ARG A NH1   1 
ATOM   6508  N NH2   . ARG D 4 702  ? 111.517 156.773 165.528 1.00 69.72  ? 699  ARG A NH2   1 
ATOM   6509  N N     . PRO D 4 703  ? 110.678 159.355 172.403 1.00 70.35  ? 700  PRO A N     1 
ATOM   6510  C CA    . PRO D 4 703  ? 110.032 158.569 173.460 1.00 70.35  ? 700  PRO A CA    1 
ATOM   6511  C C     . PRO D 4 703  ? 110.015 157.083 173.125 1.00 70.35  ? 700  PRO A C     1 
ATOM   6512  O O     . PRO D 4 703  ? 109.923 156.684 171.963 1.00 70.35  ? 700  PRO A O     1 
ATOM   6513  C CB    . PRO D 4 703  ? 108.616 159.150 173.516 1.00 70.35  ? 700  PRO A CB    1 
ATOM   6514  C CG    . PRO D 4 703  ? 108.782 160.557 173.074 1.00 70.35  ? 700  PRO A CG    1 
ATOM   6515  C CD    . PRO D 4 703  ? 109.904 160.565 172.067 1.00 70.35  ? 700  PRO A CD    1 
ATOM   6516  N N     . SER D 4 704  ? 110.119 156.262 174.172 1.00 69.58  ? 701  SER A N     1 
ATOM   6517  C CA    . SER D 4 704  ? 110.309 154.828 173.987 1.00 69.58  ? 701  SER A CA    1 
ATOM   6518  C C     . SER D 4 704  ? 109.048 154.135 173.487 1.00 69.58  ? 701  SER A C     1 
ATOM   6519  O O     . SER D 4 704  ? 109.134 153.062 172.880 1.00 69.58  ? 701  SER A O     1 
ATOM   6520  C CB    . SER D 4 704  ? 110.764 154.196 175.301 1.00 69.58  ? 701  SER A CB    1 
ATOM   6521  O OG    . SER D 4 704  ? 111.978 154.773 175.746 1.00 69.58  ? 701  SER A OG    1 
ATOM   6522  N N     . SER D 4 705  ? 107.876 154.723 173.735 1.00 70.02  ? 702  SER A N     1 
ATOM   6523  C CA    . SER D 4 705  ? 106.622 154.019 173.481 1.00 70.02  ? 702  SER A CA    1 
ATOM   6524  C C     . SER D 4 705  ? 106.410 153.739 171.996 1.00 70.02  ? 702  SER A C     1 
ATOM   6525  O O     . SER D 4 705  ? 105.987 152.638 171.624 1.00 70.02  ? 702  SER A O     1 
ATOM   6526  C CB    . SER D 4 705  ? 105.451 154.824 174.045 1.00 70.02  ? 702  SER A CB    1 
ATOM   6527  O OG    . SER D 4 705  ? 105.702 155.213 175.384 1.00 70.02  ? 702  SER A OG    1 
ATOM   6528  N N     . GLN D 4 706  ? 106.700 154.711 171.133 1.00 66.86  ? 703  GLN A N     1 
ATOM   6529  C CA    . GLN D 4 706  ? 106.332 154.601 169.727 1.00 66.86  ? 703  GLN A CA    1 
ATOM   6530  C C     . GLN D 4 706  ? 107.380 153.899 168.873 1.00 66.86  ? 703  GLN A C     1 
ATOM   6531  O O     . GLN D 4 706  ? 107.176 153.778 167.660 1.00 66.86  ? 703  GLN A O     1 
ATOM   6532  C CB    . GLN D 4 706  ? 106.050 155.989 169.145 1.00 66.86  ? 703  GLN A CB    1 
ATOM   6533  C CG    . GLN D 4 706  ? 107.296 156.797 168.835 1.00 66.86  ? 703  GLN A CG    1 
ATOM   6534  C CD    . GLN D 4 706  ? 107.805 157.558 170.038 1.00 66.86  ? 703  GLN A CD    1 
ATOM   6535  O OE1   . GLN D 4 706  ? 107.309 157.386 171.151 1.00 66.86  ? 703  GLN A OE1   1 
ATOM   6536  N NE2   . GLN D 4 706  ? 108.807 158.401 169.823 1.00 66.86  ? 703  GLN A NE2   1 
ATOM   6537  N N     . TYR D 4 707  ? 108.486 153.443 169.456 1.00 69.28  ? 704  TYR A N     1 
ATOM   6538  C CA    . TYR D 4 707  ? 109.505 152.758 168.671 1.00 69.28  ? 704  TYR A CA    1 
ATOM   6539  C C     . TYR D 4 707  ? 108.951 151.462 168.093 1.00 69.28  ? 704  TYR A C     1 
ATOM   6540  O O     . TYR D 4 707  ? 108.348 150.654 168.805 1.00 69.28  ? 704  TYR A O     1 
ATOM   6541  C CB    . TYR D 4 707  ? 110.736 152.477 169.531 1.00 69.28  ? 704  TYR A CB    1 
ATOM   6542  C CG    . TYR D 4 707  ? 111.677 153.656 169.634 1.00 69.28  ? 704  TYR A CG    1 
ATOM   6543  C CD1   . TYR D 4 707  ? 112.329 154.146 168.510 1.00 69.28  ? 704  TYR A CD1   1 
ATOM   6544  C CD2   . TYR D 4 707  ? 111.908 154.281 170.850 1.00 69.28  ? 704  TYR A CD2   1 
ATOM   6545  C CE1   . TYR D 4 707  ? 113.186 155.224 168.597 1.00 69.28  ? 704  TYR A CE1   1 
ATOM   6546  C CE2   . TYR D 4 707  ? 112.764 155.360 170.946 1.00 69.28  ? 704  TYR A CE2   1 
ATOM   6547  C CZ    . TYR D 4 707  ? 113.400 155.827 169.817 1.00 69.28  ? 704  TYR A CZ    1 
ATOM   6548  O OH    . TYR D 4 707  ? 114.254 156.901 169.907 1.00 69.28  ? 704  TYR A OH    1 
ATOM   6549  N N     . LYS D 4 708  ? 109.159 151.268 166.788 1.00 71.27  ? 705  LYS A N     1 
ATOM   6550  C CA    . LYS D 4 708  ? 108.606 150.095 166.118 1.00 71.27  ? 705  LYS A CA    1 
ATOM   6551  C C     . LYS D 4 708  ? 109.354 148.825 166.503 1.00 71.27  ? 705  LYS A C     1 
ATOM   6552  O O     . LYS D 4 708  ? 108.731 147.794 166.784 1.00 71.27  ? 705  LYS A O     1 
ATOM   6553  C CB    . LYS D 4 708  ? 108.635 150.295 164.602 1.00 71.27  ? 705  LYS A CB    1 
ATOM   6554  C CG    . LYS D 4 708  ? 108.138 151.656 164.145 1.00 71.27  ? 705  LYS A CG    1 
ATOM   6555  C CD    . LYS D 4 708  ? 108.581 151.957 162.723 1.00 71.27  ? 705  LYS A CD    1 
ATOM   6556  C CE    . LYS D 4 708  ? 108.553 153.451 162.440 1.00 71.27  ? 705  LYS A CE    1 
ATOM   6557  N NZ    . LYS D 4 708  ? 108.205 153.743 161.022 1.00 71.27  ? 705  LYS A NZ    1 
ATOM   6558  N N     . ASP D 4 709  ? 110.683 148.875 166.524 1.00 70.75  ? 706  ASP A N     1 
ATOM   6559  C CA    . ASP D 4 709  ? 111.482 147.688 166.794 1.00 70.75  ? 706  ASP A CA    1 
ATOM   6560  C C     . ASP D 4 709  ? 112.844 148.118 167.317 1.00 70.75  ? 706  ASP A C     1 
ATOM   6561  O O     . ASP D 4 709  ? 113.203 149.298 167.284 1.00 70.75  ? 706  ASP A O     1 
ATOM   6562  C CB    . ASP D 4 709  ? 111.624 146.816 165.543 1.00 70.75  ? 706  ASP A CB    1 
ATOM   6563  C CG    . ASP D 4 709  ? 111.936 147.627 164.301 1.00 70.75  ? 706  ASP A CG    1 
ATOM   6564  O OD1   . ASP D 4 709  ? 112.144 148.852 164.425 1.00 70.75  ? 706  ASP A OD1   1 
ATOM   6565  O OD2   . ASP D 4 709  ? 111.975 147.037 163.201 1.00 70.75  ? 706  ASP A OD2   1 
ATOM   6566  N N     . LEU D 4 710  ? 113.601 147.133 167.807 1.00 66.80  ? 707  LEU A N     1 
ATOM   6567  C CA    . LEU D 4 710  ? 114.944 147.406 168.309 1.00 66.80  ? 707  LEU A CA    1 
ATOM   6568  C C     . LEU D 4 710  ? 115.869 147.910 167.211 1.00 66.80  ? 707  LEU A C     1 
ATOM   6569  O O     . LEU D 4 710  ? 116.839 148.619 167.499 1.00 66.80  ? 707  LEU A O     1 
ATOM   6570  C CB    . LEU D 4 710  ? 115.541 146.153 168.952 1.00 66.80  ? 707  LEU A CB    1 
ATOM   6571  C CG    . LEU D 4 710  ? 115.190 145.815 170.403 1.00 66.80  ? 707  LEU A CG    1 
ATOM   6572  C CD1   . LEU D 4 710  ? 115.716 146.902 171.324 1.00 66.80  ? 707  LEU A CD1   1 
ATOM   6573  C CD2   . LEU D 4 710  ? 113.699 145.601 170.611 1.00 66.80  ? 707  LEU A CD2   1 
ATOM   6574  N N     . GLY D 4 711  ? 115.599 147.547 165.955 1.00 66.92  ? 708  GLY A N     1 
ATOM   6575  C CA    . GLY D 4 711  ? 116.502 147.927 164.881 1.00 66.92  ? 708  GLY A CA    1 
ATOM   6576  C C     . GLY D 4 711  ? 116.630 149.430 164.729 1.00 66.92  ? 708  GLY A C     1 
ATOM   6577  O O     . GLY D 4 711  ? 117.738 149.970 164.684 1.00 66.92  ? 708  GLY A O     1 
ATOM   6578  N N     . GLU D 4 712  ? 115.495 150.132 164.676 1.00 67.05  ? 709  GLU A N     1 
ATOM   6579  C CA    . GLU D 4 712  ? 115.543 151.581 164.522 1.00 67.05  ? 709  GLU A CA    1 
ATOM   6580  C C     . GLU D 4 712  ? 116.102 152.249 165.772 1.00 67.05  ? 709  GLU A C     1 
ATOM   6581  O O     . GLU D 4 712  ? 116.845 153.233 165.675 1.00 67.05  ? 709  GLU A O     1 
ATOM   6582  C CB    . GLU D 4 712  ? 114.156 152.131 164.184 1.00 67.05  ? 709  GLU A CB    1 
ATOM   6583  C CG    . GLU D 4 712  ? 113.121 151.994 165.288 1.00 67.05  ? 709  GLU A CG    1 
ATOM   6584  C CD    . GLU D 4 712  ? 111.762 152.524 164.877 1.00 67.05  ? 709  GLU A CD    1 
ATOM   6585  O OE1   . GLU D 4 712  ? 111.619 152.964 163.717 1.00 67.05  ? 709  GLU A OE1   1 
ATOM   6586  O OE2   . GLU D 4 712  ? 110.839 152.509 165.717 1.00 67.05  ? 709  GLU A OE2   1 
ATOM   6587  N N     . TYR D 4 713  ? 115.771 151.721 166.953 1.00 59.86  ? 710  TYR A N     1 
ATOM   6588  C CA    . TYR D 4 713  ? 116.291 152.306 168.183 1.00 59.86  ? 710  TYR A CA    1 
ATOM   6589  C C     . TYR D 4 713  ? 117.808 152.206 168.239 1.00 59.86  ? 710  TYR A C     1 
ATOM   6590  O O     . TYR D 4 713  ? 118.486 153.170 168.607 1.00 59.86  ? 710  TYR A O     1 
ATOM   6591  C CB    . TYR D 4 713  ? 115.675 151.625 169.402 1.00 59.86  ? 710  TYR A CB    1 
ATOM   6592  C CG    . TYR D 4 713  ? 116.280 152.093 170.704 1.00 59.86  ? 710  TYR A CG    1 
ATOM   6593  C CD1   . TYR D 4 713  ? 115.926 153.316 171.255 1.00 59.86  ? 710  TYR A CD1   1 
ATOM   6594  C CD2   . TYR D 4 713  ? 117.217 151.319 171.375 1.00 59.86  ? 710  TYR A CD2   1 
ATOM   6595  C CE1   . TYR D 4 713  ? 116.478 153.750 172.442 1.00 59.86  ? 710  TYR A CE1   1 
ATOM   6596  C CE2   . TYR D 4 713  ? 117.773 151.745 172.563 1.00 59.86  ? 710  TYR A CE2   1 
ATOM   6597  C CZ    . TYR D 4 713  ? 117.401 152.961 173.091 1.00 59.86  ? 710  TYR A CZ    1 
ATOM   6598  O OH    . TYR D 4 713  ? 117.955 153.390 174.274 1.00 59.86  ? 710  TYR A OH    1 
ATOM   6599  N N     . TYR D 4 714  ? 118.360 151.051 167.869 1.00 54.95  ? 711  TYR A N     1 
ATOM   6600  C CA    . TYR D 4 714  ? 119.810 150.900 167.891 1.00 54.95  ? 711  TYR A CA    1 
ATOM   6601  C C     . TYR D 4 714  ? 120.466 151.707 166.778 1.00 54.95  ? 711  TYR A C     1 
ATOM   6602  O O     . TYR D 4 714  ? 121.544 152.278 166.975 1.00 54.95  ? 711  TYR A O     1 
ATOM   6603  C CB    . TYR D 4 714  ? 120.186 149.424 167.798 1.00 54.95  ? 711  TYR A CB    1 
ATOM   6604  C CG    . TYR D 4 714  ? 119.942 148.678 169.089 1.00 54.95  ? 711  TYR A CG    1 
ATOM   6605  C CD1   . TYR D 4 714  ? 120.101 149.311 170.314 1.00 54.95  ? 711  TYR A CD1   1 
ATOM   6606  C CD2   . TYR D 4 714  ? 119.544 147.350 169.085 1.00 54.95  ? 711  TYR A CD2   1 
ATOM   6607  C CE1   . TYR D 4 714  ? 119.876 148.641 171.498 1.00 54.95  ? 711  TYR A CE1   1 
ATOM   6608  C CE2   . TYR D 4 714  ? 119.317 146.671 170.266 1.00 54.95  ? 711  TYR A CE2   1 
ATOM   6609  C CZ    . TYR D 4 714  ? 119.485 147.322 171.469 1.00 54.95  ? 711  TYR A CZ    1 
ATOM   6610  O OH    . TYR D 4 714  ? 119.260 146.651 172.647 1.00 54.95  ? 711  TYR A OH    1 
ATOM   6611  N N     . ALA D 4 715  ? 119.827 151.781 165.606 1.00 55.67  ? 712  ALA A N     1 
ATOM   6612  C CA    . ALA D 4 715  ? 120.362 152.612 164.534 1.00 55.67  ? 712  ALA A CA    1 
ATOM   6613  C C     . ALA D 4 715  ? 120.390 154.081 164.929 1.00 55.67  ? 712  ALA A C     1 
ATOM   6614  O O     . ALA D 4 715  ? 121.245 154.836 164.453 1.00 55.67  ? 712  ALA A O     1 
ATOM   6615  C CB    . ALA D 4 715  ? 119.543 152.420 163.259 1.00 55.67  ? 712  ALA A CB    1 
ATOM   6616  N N     . GLU D 4 716  ? 119.457 154.508 165.781 1.00 56.70  ? 713  GLU A N     1 
ATOM   6617  C CA    . GLU D 4 716  ? 119.469 155.879 166.275 1.00 56.70  ? 713  GLU A CA    1 
ATOM   6618  C C     . GLU D 4 716  ? 120.443 156.067 167.433 1.00 56.70  ? 713  GLU A C     1 
ATOM   6619  O O     . GLU D 4 716  ? 121.016 157.151 167.584 1.00 56.70  ? 713  GLU A O     1 
ATOM   6620  C CB    . GLU D 4 716  ? 118.061 156.291 166.706 1.00 56.70  ? 713  GLU A CB    1 
ATOM   6621  C CG    . GLU D 4 716  ? 117.888 157.784 166.928 1.00 56.70  ? 713  GLU A CG    1 
ATOM   6622  C CD    . GLU D 4 716  ? 116.433 158.187 167.073 1.00 56.70  ? 713  GLU A CD    1 
ATOM   6623  O OE1   . GLU D 4 716  ? 115.570 157.547 166.438 1.00 56.70  ? 713  GLU A OE1   1 
ATOM   6624  O OE2   . GLU D 4 716  ? 116.153 159.146 167.823 1.00 56.70  ? 713  GLU A OE2   1 
ATOM   6625  N N     . LEU D 4 717  ? 120.643 155.034 168.252 1.00 50.26  ? 714  LEU A N     1 
ATOM   6626  C CA    . LEU D 4 717  ? 121.445 155.182 169.461 1.00 50.26  ? 714  LEU A CA    1 
ATOM   6627  C C     . LEU D 4 717  ? 122.939 155.056 169.183 1.00 50.26  ? 714  LEU A C     1 
ATOM   6628  O O     . LEU D 4 717  ? 123.746 155.735 169.826 1.00 50.26  ? 714  LEU A O     1 
ATOM   6629  C CB    . LEU D 4 717  ? 121.012 154.149 170.501 1.00 50.26  ? 714  LEU A CB    1 
ATOM   6630  C CG    . LEU D 4 717  ? 121.759 154.170 171.833 1.00 50.26  ? 714  LEU A CG    1 
ATOM   6631  C CD1   . LEU D 4 717  ? 121.655 155.541 172.478 1.00 50.26  ? 714  LEU A CD1   1 
ATOM   6632  C CD2   . LEU D 4 717  ? 121.226 153.095 172.763 1.00 50.26  ? 714  LEU A CD2   1 
ATOM   6633  N N     . ASN D 4 718  ? 123.325 154.195 168.241 1.00 50.26  ? 715  ASN A N     1 
ATOM   6634  C CA    . ASN D 4 718  ? 124.746 153.976 167.981 1.00 50.26  ? 715  ASN A CA    1 
ATOM   6635  C C     . ASN D 4 718  ? 125.506 155.237 167.576 1.00 50.26  ? 715  ASN A C     1 
ATOM   6636  O O     . ASN D 4 718  ? 126.616 155.440 168.098 1.00 50.26  ? 715  ASN A O     1 
ATOM   6637  C CB    . ASN D 4 718  ? 124.915 152.878 166.924 1.00 50.26  ? 715  ASN A CB    1 
ATOM   6638  C CG    . ASN D 4 718  ? 124.413 151.532 167.401 1.00 50.26  ? 715  ASN A CG    1 
ATOM   6639  O OD1   . ASN D 4 718  ? 124.270 151.302 168.601 1.00 50.26  ? 715  ASN A OD1   1 
ATOM   6640  N ND2   . ASN D 4 718  ? 124.142 150.634 166.462 1.00 50.26  ? 715  ASN A ND2   1 
ATOM   6641  N N     . PRO D 4 719  ? 125.011 156.096 166.676 1.00 50.26  ? 716  PRO A N     1 
ATOM   6642  C CA    . PRO D 4 719  ? 125.774 157.314 166.356 1.00 50.26  ? 716  PRO A CA    1 
ATOM   6643  C C     . PRO D 4 719  ? 125.991 158.229 167.547 1.00 50.26  ? 716  PRO A C     1 
ATOM   6644  O O     . PRO D 4 719  ? 126.993 158.953 167.584 1.00 50.26  ? 716  PRO A O     1 
ATOM   6645  C CB    . PRO D 4 719  ? 124.919 157.990 165.275 1.00 50.26  ? 716  PRO A CB    1 
ATOM   6646  C CG    . PRO D 4 719  ? 124.112 156.895 164.692 1.00 50.26  ? 716  PRO A CG    1 
ATOM   6647  C CD    . PRO D 4 719  ? 123.809 155.983 165.832 1.00 50.26  ? 716  PRO A CD    1 
ATOM   6648  N N     . LEU D 4 720  ? 125.082 158.224 168.523 1.00 50.26  ? 717  LEU A N     1 
ATOM   6649  C CA    . LEU D 4 720  ? 125.223 159.112 169.670 1.00 50.26  ? 717  LEU A CA    1 
ATOM   6650  C C     . LEU D 4 720  ? 126.312 158.658 170.631 1.00 50.26  ? 717  LEU A C     1 
ATOM   6651  O O     . LEU D 4 720  ? 126.828 159.482 171.393 1.00 50.26  ? 717  LEU A O     1 
ATOM   6652  C CB    . LEU D 4 720  ? 123.894 159.224 170.415 1.00 50.26  ? 717  LEU A CB    1 
ATOM   6653  C CG    . LEU D 4 720  ? 122.660 159.520 169.562 1.00 50.26  ? 717  LEU A CG    1 
ATOM   6654  C CD1   . LEU D 4 720  ? 121.425 159.625 170.439 1.00 50.26  ? 717  LEU A CD1   1 
ATOM   6655  C CD2   . LEU D 4 720  ? 122.854 160.790 168.752 1.00 50.26  ? 717  LEU A CD2   1 
ATOM   6656  N N     . LEU D 4 721  ? 126.671 157.374 170.617 1.00 50.26  ? 718  LEU A N     1 
ATOM   6657  C CA    . LEU D 4 721  ? 127.658 156.867 171.563 1.00 50.26  ? 718  LEU A CA    1 
ATOM   6658  C C     . LEU D 4 721  ? 129.077 157.264 171.174 1.00 50.26  ? 718  LEU A C     1 
ATOM   6659  O O     . LEU D 4 721  ? 129.918 157.506 172.047 1.00 50.26  ? 718  LEU A O     1 
ATOM   6660  C CB    . LEU D 4 721  ? 127.538 155.348 171.673 1.00 50.26  ? 718  LEU A CB    1 
ATOM   6661  C CG    . LEU D 4 721  ? 126.205 154.853 172.235 1.00 50.26  ? 718  LEU A CG    1 
ATOM   6662  C CD1   . LEU D 4 721  ? 126.082 153.348 172.092 1.00 50.26  ? 718  LEU A CD1   1 
ATOM   6663  C CD2   . LEU D 4 721  ? 126.053 155.271 173.686 1.00 50.26  ? 718  LEU A CD2   1 
ATOM   6664  N N     . TYR D 4 722  ? 129.362 157.335 169.878 1.00 50.26  ? 719  TYR A N     1 
ATOM   6665  C CA    . TYR D 4 722  ? 130.699 157.660 169.401 1.00 50.26  ? 719  TYR A CA    1 
ATOM   6666  C C     . TYR D 4 722  ? 130.902 159.170 169.387 1.00 50.26  ? 719  TYR A C     1 
ATOM   6667  O O     . TYR D 4 722  ? 130.043 159.915 168.906 1.00 50.26  ? 719  TYR A O     1 
ATOM   6668  C CB    . TYR D 4 722  ? 130.905 157.073 168.005 1.00 50.26  ? 719  TYR A CB    1 
ATOM   6669  C CG    . TYR D 4 722  ? 132.094 157.613 167.249 1.00 50.26  ? 719  TYR A CG    1 
ATOM   6670  C CD1   . TYR D 4 722  ? 133.354 157.062 167.416 1.00 50.26  ? 719  TYR A CD1   1 
ATOM   6671  C CD2   . TYR D 4 722  ? 131.952 158.656 166.346 1.00 50.26  ? 719  TYR A CD2   1 
ATOM   6672  C CE1   . TYR D 4 722  ? 134.439 157.545 166.720 1.00 50.26  ? 719  TYR A CE1   1 
ATOM   6673  C CE2   . TYR D 4 722  ? 133.033 159.145 165.649 1.00 50.26  ? 719  TYR A CE2   1 
ATOM   6674  C CZ    . TYR D 4 722  ? 134.273 158.586 165.837 1.00 50.26  ? 719  TYR A CZ    1 
ATOM   6675  O OH    . TYR D 4 722  ? 135.350 159.073 165.137 1.00 50.26  ? 719  TYR A OH    1 
ATOM   6676  N N     . HIS D 4 723  ? 132.040 159.621 169.912 1.00 50.26  ? 720  HIS A N     1 
ATOM   6677  C CA    . HIS D 4 723  ? 132.326 161.048 169.981 1.00 50.26  ? 720  HIS A CA    1 
ATOM   6678  C C     . HIS D 4 723  ? 133.827 161.259 170.106 1.00 50.26  ? 720  HIS A C     1 
ATOM   6679  O O     . HIS D 4 723  ? 134.527 160.466 170.739 1.00 50.26  ? 720  HIS A O     1 
ATOM   6680  C CB    . HIS D 4 723  ? 131.596 161.705 171.157 1.00 50.26  ? 720  HIS A CB    1 
ATOM   6681  C CG    . HIS D 4 723  ? 131.609 163.201 171.115 1.00 50.26  ? 720  HIS A CG    1 
ATOM   6682  N ND1   . HIS D 4 723  ? 131.672 163.976 172.253 1.00 50.26  ? 720  HIS A ND1   1 
ATOM   6683  C CD2   . HIS D 4 723  ? 131.570 164.064 170.073 1.00 50.26  ? 720  HIS A CD2   1 
ATOM   6684  C CE1   . HIS D 4 723  ? 131.669 165.253 171.913 1.00 50.26  ? 720  HIS A CE1   1 
ATOM   6685  N NE2   . HIS D 4 723  ? 131.607 165.334 170.597 1.00 50.26  ? 720  HIS A NE2   1 
ATOM   6686  N N     . ILE D 4 724  ? 134.311 162.340 169.497 1.00 50.26  ? 721  ILE A N     1 
ATOM   6687  C CA    . ILE D 4 724  ? 135.709 162.743 169.587 1.00 50.26  ? 721  ILE A CA    1 
ATOM   6688  C C     . ILE D 4 724  ? 135.763 164.176 170.093 1.00 50.26  ? 721  ILE A C     1 
ATOM   6689  O O     . ILE D 4 724  ? 135.058 165.049 169.575 1.00 50.26  ? 721  ILE A O     1 
ATOM   6690  C CB    . ILE D 4 724  ? 136.438 162.626 168.234 1.00 50.26  ? 721  ILE A CB    1 
ATOM   6691  C CG1   . ILE D 4 724  ? 136.623 161.162 167.845 1.00 50.26  ? 721  ILE A CG1   1 
ATOM   6692  C CG2   . ILE D 4 724  ? 137.791 163.310 168.295 1.00 50.26  ? 721  ILE A CG2   1 
ATOM   6693  C CD1   . ILE D 4 724  ? 137.433 160.979 166.585 1.00 50.26  ? 721  ILE A CD1   1 
ATOM   6694  N N     . SER D 4 725  ? 136.596 164.417 171.101 1.00 50.26  ? 722  SER A N     1 
ATOM   6695  C CA    . SER D 4 725  ? 136.782 165.743 171.664 1.00 50.26  ? 722  SER A CA    1 
ATOM   6696  C C     . SER D 4 725  ? 138.269 166.026 171.811 1.00 50.26  ? 722  SER A C     1 
ATOM   6697  O O     . SER D 4 725  ? 139.090 165.111 171.914 1.00 50.26  ? 722  SER A O     1 
ATOM   6698  C CB    . SER D 4 725  ? 136.082 165.882 173.022 1.00 50.26  ? 722  SER A CB    1 
ATOM   6699  O OG    . SER D 4 725  ? 136.446 164.824 173.890 1.00 50.26  ? 722  SER A OG    1 
ATOM   6700  N N     . PHE D 4 726  ? 138.609 167.311 171.814 1.00 50.26  ? 723  PHE A N     1 
ATOM   6701  C CA    . PHE D 4 726  ? 139.985 167.763 171.947 1.00 50.26  ? 723  PHE A CA    1 
ATOM   6702  C C     . PHE D 4 726  ? 140.119 168.642 173.182 1.00 50.26  ? 723  PHE A C     1 
ATOM   6703  O O     . PHE D 4 726  ? 139.251 169.476 173.458 1.00 50.26  ? 723  PHE A O     1 
ATOM   6704  C CB    . PHE D 4 726  ? 140.434 168.539 170.707 1.00 50.26  ? 723  PHE A CB    1 
ATOM   6705  C CG    . PHE D 4 726  ? 140.728 167.669 169.521 1.00 50.26  ? 723  PHE A CG    1 
ATOM   6706  C CD1   . PHE D 4 726  ? 141.977 167.095 169.360 1.00 50.26  ? 723  PHE A CD1   1 
ATOM   6707  C CD2   . PHE D 4 726  ? 139.758 167.427 168.566 1.00 50.26  ? 723  PHE A CD2   1 
ATOM   6708  C CE1   . PHE D 4 726  ? 142.251 166.295 168.270 1.00 50.26  ? 723  PHE A CE1   1 
ATOM   6709  C CE2   . PHE D 4 726  ? 140.027 166.629 167.473 1.00 50.26  ? 723  PHE A CE2   1 
ATOM   6710  C CZ    . PHE D 4 726  ? 141.275 166.063 167.325 1.00 50.26  ? 723  PHE A CZ    1 
ATOM   6711  N N     . GLN D 4 727  ? 141.207 168.449 173.923 1.00 50.26  ? 724  GLN A N     1 
ATOM   6712  C CA    . GLN D 4 727  ? 141.498 169.242 175.109 1.00 50.26  ? 724  GLN A CA    1 
ATOM   6713  C C     . GLN D 4 727  ? 142.931 169.743 175.031 1.00 50.26  ? 724  GLN A C     1 
ATOM   6714  O O     . GLN D 4 727  ? 143.840 168.979 174.694 1.00 50.26  ? 724  GLN A O     1 
ATOM   6715  C CB    . GLN D 4 727  ? 141.289 168.428 176.389 1.00 50.26  ? 724  GLN A CB    1 
ATOM   6716  C CG    . GLN D 4 727  ? 139.845 168.041 176.648 1.00 50.26  ? 724  GLN A CG    1 
ATOM   6717  C CD    . GLN D 4 727  ? 139.574 167.754 178.109 1.00 50.26  ? 724  GLN A CD    1 
ATOM   6718  O OE1   . GLN D 4 727  ? 139.376 168.669 178.907 1.00 50.26  ? 724  GLN A OE1   1 
ATOM   6719  N NE2   . GLN D 4 727  ? 139.563 166.476 178.468 1.00 50.26  ? 724  GLN A NE2   1 
ATOM   6720  N N     . ARG D 4 728  ? 143.126 171.020 175.341 1.00 50.26  ? 725  ARG A N     1 
ATOM   6721  C CA    . ARG D 4 728  ? 144.455 171.610 175.281 1.00 50.26  ? 725  ARG A CA    1 
ATOM   6722  C C     . ARG D 4 728  ? 145.345 171.050 176.382 1.00 50.26  ? 725  ARG A C     1 
ATOM   6723  O O     . ARG D 4 728  ? 144.931 170.925 177.538 1.00 50.26  ? 725  ARG A O     1 
ATOM   6724  C CB    . ARG D 4 728  ? 144.367 173.130 175.398 1.00 50.26  ? 725  ARG A CB    1 
ATOM   6725  C CG    . ARG D 4 728  ? 145.709 173.825 175.545 1.00 50.26  ? 725  ARG A CG    1 
ATOM   6726  C CD    . ARG D 4 728  ? 146.579 173.610 174.322 1.00 50.26  ? 725  ARG A CD    1 
ATOM   6727  N NE    . ARG D 4 728  ? 145.853 173.878 173.087 1.00 50.26  ? 725  ARG A NE    1 
ATOM   6728  C CZ    . ARG D 4 728  ? 146.064 174.929 172.308 1.00 50.26  ? 725  ARG A CZ    1 
ATOM   6729  N NH1   . ARG D 4 728  ? 146.981 175.835 172.605 1.00 50.26  ? 725  ARG A NH1   1 
ATOM   6730  N NH2   . ARG D 4 728  ? 145.338 175.075 171.204 1.00 50.26  ? 725  ARG A NH2   1 
ATOM   6731  N N     . ILE D 4 729  ? 146.578 170.711 176.014 1.00 50.26  ? 726  ILE A N     1 
ATOM   6732  C CA    . ILE D 4 729  ? 147.579 170.204 176.942 1.00 50.26  ? 726  ILE A CA    1 
ATOM   6733  C C     . ILE D 4 729  ? 148.827 171.061 176.810 1.00 50.26  ? 726  ILE A C     1 
ATOM   6734  O O     . ILE D 4 729  ? 149.255 171.378 175.695 1.00 50.26  ? 726  ILE A O     1 
ATOM   6735  C CB    . ILE D 4 729  ? 147.900 168.719 176.677 1.00 50.26  ? 726  ILE A CB    1 
ATOM   6736  C CG1   . ILE D 4 729  ? 146.659 167.863 176.919 1.00 50.26  ? 726  ILE A CG1   1 
ATOM   6737  C CG2   . ILE D 4 729  ? 149.046 168.251 177.554 1.00 50.26  ? 726  ILE A CG2   1 
ATOM   6738  C CD1   . ILE D 4 729  ? 146.921 166.386 176.839 1.00 50.26  ? 726  ILE A CD1   1 
ATOM   6739  N N     . ALA D 4 730  ? 149.401 171.445 177.948 1.00 50.26  ? 727  ALA A N     1 
ATOM   6740  C CA    . ALA D 4 730  ? 150.555 172.333 177.945 1.00 50.26  ? 727  ALA A CA    1 
ATOM   6741  C C     . ALA D 4 730  ? 151.710 171.720 177.164 1.00 50.26  ? 727  ALA A C     1 
ATOM   6742  O O     . ALA D 4 730  ? 151.961 170.515 177.236 1.00 50.26  ? 727  ALA A O     1 
ATOM   6743  C CB    . ALA D 4 730  ? 150.992 172.637 179.378 1.00 50.26  ? 727  ALA A CB    1 
ATOM   6744  N N     . GLU D 4 731  ? 152.408 172.566 176.403 1.00 50.26  ? 728  GLU A N     1 
ATOM   6745  C CA    . GLU D 4 731  ? 153.522 172.089 175.590 1.00 50.26  ? 728  GLU A CA    1 
ATOM   6746  C C     . GLU D 4 731  ? 154.642 171.530 176.456 1.00 50.26  ? 728  GLU A C     1 
ATOM   6747  O O     . GLU D 4 731  ? 155.278 170.533 176.092 1.00 50.26  ? 728  GLU A O     1 
ATOM   6748  C CB    . GLU D 4 731  ? 154.054 173.219 174.710 1.00 50.26  ? 728  GLU A CB    1 
ATOM   6749  C CG    . GLU D 4 731  ? 155.168 172.788 173.772 1.00 50.26  ? 728  GLU A CG    1 
ATOM   6750  C CD    . GLU D 4 731  ? 155.645 173.912 172.877 1.00 50.26  ? 728  GLU A CD    1 
ATOM   6751  O OE1   . GLU D 4 731  ? 155.118 175.037 173.004 1.00 50.26  ? 728  GLU A OE1   1 
ATOM   6752  O OE2   . GLU D 4 731  ? 156.546 173.671 172.048 1.00 50.26  ? 728  GLU A OE2   1 
ATOM   6753  N N     . LYS D 4 732  ? 154.901 172.163 177.601 1.00 50.26  ? 729  LYS A N     1 
ATOM   6754  C CA    . LYS D 4 732  ? 156.027 171.756 178.433 1.00 50.26  ? 729  LYS A CA    1 
ATOM   6755  C C     . LYS D 4 732  ? 155.880 170.315 178.901 1.00 50.26  ? 729  LYS A C     1 
ATOM   6756  O O     . LYS D 4 732  ? 156.860 169.564 178.924 1.00 50.26  ? 729  LYS A O     1 
ATOM   6757  C CB    . LYS D 4 732  ? 156.172 172.706 179.624 1.00 38.20  ? 729  LYS A CB    1 
ATOM   6758  C CG    . LYS D 4 732  ? 154.943 172.797 180.514 1.00 38.20  ? 729  LYS A CG    1 
ATOM   6759  C CD    . LYS D 4 732  ? 155.067 173.928 181.520 1.00 38.20  ? 729  LYS A CD    1 
ATOM   6760  C CE    . LYS D 4 732  ? 154.012 173.810 182.604 1.00 38.20  ? 729  LYS A CE    1 
ATOM   6761  N NZ    . LYS D 4 732  ? 153.856 172.403 183.063 1.00 38.20  ? 729  LYS A NZ    1 
ATOM   6762  N N     . GLU D 4 733  ? 154.664 169.906 179.269 1.00 50.26  ? 730  GLU A N     1 
ATOM   6763  C CA    . GLU D 4 733  ? 154.459 168.538 179.734 1.00 50.26  ? 730  GLU A CA    1 
ATOM   6764  C C     . GLU D 4 733  ? 154.736 167.526 178.630 1.00 50.26  ? 730  GLU A C     1 
ATOM   6765  O O     . GLU D 4 733  ? 155.405 166.512 178.865 1.00 50.26  ? 730  GLU A O     1 
ATOM   6766  C CB    . GLU D 4 733  ? 153.038 168.373 180.269 1.00 50.26  ? 730  GLU A CB    1 
ATOM   6767  C CG    . GLU D 4 733  ? 152.757 166.997 180.841 1.00 50.26  ? 730  GLU A CG    1 
ATOM   6768  C CD    . GLU D 4 733  ? 151.400 166.912 181.505 1.00 50.26  ? 730  GLU A CD    1 
ATOM   6769  O OE1   . GLU D 4 733  ? 150.680 167.931 181.518 1.00 50.26  ? 730  GLU A OE1   1 
ATOM   6770  O OE2   . GLU D 4 733  ? 151.054 165.825 182.013 1.00 50.26  ? 730  GLU A OE2   1 
ATOM   6771  N N     . ILE D 4 734  ? 154.240 167.785 177.418 1.00 50.26  ? 731  ILE A N     1 
ATOM   6772  C CA    . ILE D 4 734  ? 154.468 166.860 176.310 1.00 50.26  ? 731  ILE A CA    1 
ATOM   6773  C C     . ILE D 4 734  ? 155.950 166.790 175.969 1.00 50.26  ? 731  ILE A C     1 
ATOM   6774  O O     . ILE D 4 734  ? 156.502 165.705 175.745 1.00 50.26  ? 731  ILE A O     1 
ATOM   6775  C CB    . ILE D 4 734  ? 153.628 167.270 175.087 1.00 50.26  ? 731  ILE A CB    1 
ATOM   6776  C CG1   . ILE D 4 734  ? 152.146 167.340 175.452 1.00 50.26  ? 731  ILE A CG1   1 
ATOM   6777  C CG2   . ILE D 4 734  ? 153.843 166.293 173.946 1.00 50.26  ? 731  ILE A CG2   1 
ATOM   6778  C CD1   . ILE D 4 734  ? 151.548 166.007 175.821 1.00 50.26  ? 731  ILE A CD1   1 
ATOM   6779  N N     . MET D 4 735  ? 156.619 167.945 175.920 1.00 50.26  ? 732  MET A N     1 
ATOM   6780  C CA    . MET D 4 735  ? 158.039 167.951 175.586 1.00 50.26  ? 732  MET A CA    1 
ATOM   6781  C C     . MET D 4 735  ? 158.864 167.249 176.656 1.00 50.26  ? 732  MET A C     1 
ATOM   6782  O O     . MET D 4 735  ? 159.823 166.540 176.336 1.00 50.26  ? 732  MET A O     1 
ATOM   6783  C CB    . MET D 4 735  ? 158.530 169.383 175.372 1.00 50.26  ? 732  MET A CB    1 
ATOM   6784  C CG    . MET D 4 735  ? 157.807 170.159 174.268 1.00 50.26  ? 732  MET A CG    1 
ATOM   6785  S SD    . MET D 4 735  ? 157.265 169.241 172.804 1.00 50.26  ? 732  MET A SD    1 
ATOM   6786  C CE    . MET D 4 735  ? 158.765 168.408 172.275 1.00 50.26  ? 732  MET A CE    1 
ATOM   6787  N N     . ASP D 4 736  ? 158.510 167.427 177.931 1.00 50.26  ? 733  ASP A N     1 
ATOM   6788  C CA    . ASP D 4 736  ? 159.227 166.733 178.994 1.00 50.26  ? 733  ASP A CA    1 
ATOM   6789  C C     . ASP D 4 736  ? 158.971 165.233 178.960 1.00 50.26  ? 733  ASP A C     1 
ATOM   6790  O O     . ASP D 4 736  ? 159.876 164.446 179.257 1.00 50.26  ? 733  ASP A O     1 
ATOM   6791  C CB    . ASP D 4 736  ? 158.841 167.309 180.355 1.00 50.26  ? 733  ASP A CB    1 
ATOM   6792  C CG    . ASP D 4 736  ? 159.297 168.744 180.530 1.00 50.26  ? 733  ASP A CG    1 
ATOM   6793  O OD1   . ASP D 4 736  ? 160.247 169.155 179.831 1.00 50.26  ? 733  ASP A OD1   1 
ATOM   6794  O OD2   . ASP D 4 736  ? 158.707 169.460 181.365 1.00 50.26  ? 733  ASP A OD2   1 
ATOM   6795  N N     . ALA D 4 737  ? 157.752 164.818 178.607 1.00 50.26  ? 734  ALA A N     1 
ATOM   6796  C CA    . ALA D 4 737  ? 157.477 163.394 178.456 1.00 50.26  ? 734  ALA A CA    1 
ATOM   6797  C C     . ALA D 4 737  ? 158.281 162.800 177.308 1.00 50.26  ? 734  ALA A C     1 
ATOM   6798  O O     . ALA D 4 737  ? 158.776 161.670 177.404 1.00 50.26  ? 734  ALA A O     1 
ATOM   6799  C CB    . ALA D 4 737  ? 155.981 163.167 178.241 1.00 50.26  ? 734  ALA A CB    1 
ATOM   6800  N N     . VAL D 4 738  ? 158.411 163.542 176.207 1.00 50.26  ? 735  VAL A N     1 
ATOM   6801  C CA    . VAL D 4 738  ? 159.230 163.078 175.090 1.00 50.26  ? 735  VAL A CA    1 
ATOM   6802  C C     . VAL D 4 738  ? 160.696 162.996 175.498 1.00 50.26  ? 735  VAL A C     1 
ATOM   6803  O O     . VAL D 4 738  ? 161.389 162.020 175.187 1.00 50.26  ? 735  VAL A O     1 
ATOM   6804  C CB    . VAL D 4 738  ? 159.028 163.992 173.869 1.00 50.26  ? 735  VAL A CB    1 
ATOM   6805  C CG1   . VAL D 4 738  ? 160.151 163.800 172.865 1.00 50.26  ? 735  VAL A CG1   1 
ATOM   6806  C CG2   . VAL D 4 738  ? 157.683 163.719 173.223 1.00 50.26  ? 735  VAL A CG2   1 
ATOM   6807  N N     . GLU D 4 739  ? 161.189 164.016 176.205 1.00 50.26  ? 736  GLU A N     1 
ATOM   6808  C CA    . GLU D 4 739  ? 162.585 164.036 176.630 1.00 50.26  ? 736  GLU A CA    1 
ATOM   6809  C C     . GLU D 4 739  ? 162.897 162.886 177.578 1.00 50.26  ? 736  GLU A C     1 
ATOM   6810  O O     . GLU D 4 739  ? 163.942 162.236 177.455 1.00 50.26  ? 736  GLU A O     1 
ATOM   6811  C CB    . GLU D 4 739  ? 162.901 165.376 177.294 1.00 50.26  ? 736  GLU A CB    1 
ATOM   6812  C CG    . GLU D 4 739  ? 164.346 165.545 177.716 1.00 50.26  ? 736  GLU A CG    1 
ATOM   6813  C CD    . GLU D 4 739  ? 165.276 165.753 176.542 1.00 50.26  ? 736  GLU A CD    1 
ATOM   6814  O OE1   . GLU D 4 739  ? 164.824 166.301 175.515 1.00 50.26  ? 736  GLU A OE1   1 
ATOM   6815  O OE2   . GLU D 4 739  ? 166.461 165.375 176.650 1.00 50.26  ? 736  GLU A OE2   1 
ATOM   6816  N N     . THR D 4 740  ? 162.004 162.620 178.533 1.00 50.26  ? 737  THR A N     1 
ATOM   6817  C CA    . THR D 4 740  ? 162.219 161.531 179.477 1.00 50.26  ? 737  THR A CA    1 
ATOM   6818  C C     . THR D 4 740  ? 162.136 160.168 178.803 1.00 50.26  ? 737  THR A C     1 
ATOM   6819  O O     . THR D 4 740  ? 162.741 159.206 179.289 1.00 50.26  ? 737  THR A O     1 
ATOM   6820  C CB    . THR D 4 740  ? 161.197 161.630 180.615 1.00 50.26  ? 737  THR A CB    1 
ATOM   6821  O OG1   . THR D 4 740  ? 161.311 162.912 181.244 1.00 50.26  ? 737  THR A OG1   1 
ATOM   6822  C CG2   . THR D 4 740  ? 161.438 160.556 181.665 1.00 50.26  ? 737  THR A CG2   1 
ATOM   6823  N N     . GLY D 4 741  ? 161.438 160.073 177.677 1.00 50.26  ? 738  GLY A N     1 
ATOM   6824  C CA    . GLY D 4 741  ? 161.220 158.805 177.017 1.00 50.26  ? 738  GLY A CA    1 
ATOM   6825  C C     . GLY D 4 741  ? 159.892 158.155 177.319 1.00 50.26  ? 738  GLY A C     1 
ATOM   6826  O O     . GLY D 4 741  ? 159.683 157.001 176.926 1.00 50.26  ? 738  GLY A O     1 
ATOM   6827  N N     . LYS D 4 742  ? 158.989 158.853 178.008 1.00 50.26  ? 739  LYS A N     1 
ATOM   6828  C CA    . LYS D 4 742  ? 157.678 158.302 178.315 1.00 50.26  ? 739  LYS A CA    1 
ATOM   6829  C C     . LYS D 4 742  ? 156.734 158.327 177.121 1.00 50.26  ? 739  LYS A C     1 
ATOM   6830  O O     . LYS D 4 742  ? 155.826 157.493 177.050 1.00 50.26  ? 739  LYS A O     1 
ATOM   6831  C CB    . LYS D 4 742  ? 157.050 159.064 179.483 1.00 37.53  ? 739  LYS A CB    1 
ATOM   6832  C CG    . LYS D 4 742  ? 157.950 159.182 180.702 1.00 37.53  ? 739  LYS A CG    1 
ATOM   6833  C CD    . LYS D 4 742  ? 157.147 159.500 181.952 1.00 37.53  ? 739  LYS A CD    1 
ATOM   6834  C CE    . LYS D 4 742  ? 157.969 160.302 182.946 1.00 37.53  ? 739  LYS A CE    1 
ATOM   6835  N NZ    . LYS D 4 742  ? 157.777 161.768 182.773 1.00 37.53  ? 739  LYS A NZ    1 
ATOM   6836  N N     . LEU D 4 743  ? 156.925 159.256 176.188 1.00 50.26  ? 740  LEU A N     1 
ATOM   6837  C CA    . LEU D 4 743  ? 156.061 159.378 175.024 1.00 50.26  ? 740  LEU A CA    1 
ATOM   6838  C C     . LEU D 4 743  ? 156.915 159.455 173.769 1.00 50.26  ? 740  LEU A C     1 
ATOM   6839  O O     . LEU D 4 743  ? 157.964 160.103 173.763 1.00 50.26  ? 740  LEU A O     1 
ATOM   6840  C CB    . LEU D 4 743  ? 155.165 160.618 175.124 1.00 50.26  ? 740  LEU A CB    1 
ATOM   6841  C CG    . LEU D 4 743  ? 154.229 160.896 173.949 1.00 50.26  ? 740  LEU A CG    1 
ATOM   6842  C CD1   . LEU D 4 743  ? 153.089 159.897 173.932 1.00 50.26  ? 740  LEU A CD1   1 
ATOM   6843  C CD2   . LEU D 4 743  ? 153.699 162.316 174.014 1.00 50.26  ? 740  LEU A CD2   1 
ATOM   6844  N N     . TYR D 4 744  ? 156.461 158.792 172.710 1.00 50.26  ? 741  TYR A N     1 
ATOM   6845  C CA    . TYR D 4 744  ? 157.134 158.810 171.414 1.00 50.26  ? 741  TYR A CA    1 
ATOM   6846  C C     . TYR D 4 744  ? 156.284 159.628 170.449 1.00 50.26  ? 741  TYR A C     1 
ATOM   6847  O O     . TYR D 4 744  ? 155.299 159.129 169.899 1.00 50.26  ? 741  TYR A O     1 
ATOM   6848  C CB    . TYR D 4 744  ? 157.359 157.395 170.888 1.00 50.26  ? 741  TYR A CB    1 
ATOM   6849  C CG    . TYR D 4 744  ? 158.327 156.578 171.708 1.00 50.26  ? 741  TYR A CG    1 
ATOM   6850  C CD1   . TYR D 4 744  ? 159.260 157.190 172.531 1.00 50.26  ? 741  TYR A CD1   1 
ATOM   6851  C CD2   . TYR D 4 744  ? 158.318 155.193 171.646 1.00 50.26  ? 741  TYR A CD2   1 
ATOM   6852  C CE1   . TYR D 4 744  ? 160.148 156.446 173.278 1.00 50.26  ? 741  TYR A CE1   1 
ATOM   6853  C CE2   . TYR D 4 744  ? 159.203 154.441 172.387 1.00 50.26  ? 741  TYR A CE2   1 
ATOM   6854  C CZ    . TYR D 4 744  ? 160.115 155.072 173.202 1.00 50.26  ? 741  TYR A CZ    1 
ATOM   6855  O OH    . TYR D 4 744  ? 160.999 154.328 173.945 1.00 50.26  ? 741  TYR A OH    1 
ATOM   6856  N N     . LEU D 4 745  ? 156.666 160.885 170.246 1.00 50.26  ? 742  LEU A N     1 
ATOM   6857  C CA    . LEU D 4 745  ? 155.947 161.735 169.311 1.00 50.26  ? 742  LEU A CA    1 
ATOM   6858  C C     . LEU D 4 745  ? 156.282 161.356 167.874 1.00 50.26  ? 742  LEU A C     1 
ATOM   6859  O O     . LEU D 4 745  ? 157.398 160.938 167.560 1.00 50.26  ? 742  LEU A O     1 
ATOM   6860  C CB    . LEU D 4 745  ? 156.280 163.205 169.554 1.00 50.26  ? 742  LEU A CB    1 
ATOM   6861  C CG    . LEU D 4 745  ? 155.256 163.992 170.370 1.00 50.26  ? 742  LEU A CG    1 
ATOM   6862  C CD1   . LEU D 4 745  ? 155.678 165.444 170.498 1.00 50.26  ? 742  LEU A CD1   1 
ATOM   6863  C CD2   . LEU D 4 745  ? 153.882 163.887 169.739 1.00 50.26  ? 742  LEU A CD2   1 
ATOM   6864  N N     . PHE D 4 746  ? 155.293 161.505 166.997 1.00 50.26  ? 743  PHE A N     1 
ATOM   6865  C CA    . PHE D 4 746  ? 155.471 161.221 165.576 1.00 50.26  ? 743  PHE A CA    1 
ATOM   6866  C C     . PHE D 4 746  ? 154.563 162.159 164.797 1.00 50.26  ? 743  PHE A C     1 
ATOM   6867  O O     . PHE D 4 746  ? 153.340 162.002 164.829 1.00 50.26  ? 743  PHE A O     1 
ATOM   6868  C CB    . PHE D 4 746  ? 155.144 159.765 165.251 1.00 50.26  ? 743  PHE A CB    1 
ATOM   6869  C CG    . PHE D 4 746  ? 156.195 158.790 165.686 1.00 50.26  ? 743  PHE A CG    1 
ATOM   6870  C CD1   . PHE D 4 746  ? 157.435 158.774 165.077 1.00 50.26  ? 743  PHE A CD1   1 
ATOM   6871  C CD2   . PHE D 4 746  ? 155.936 157.875 166.689 1.00 50.26  ? 743  PHE A CD2   1 
ATOM   6872  C CE1   . PHE D 4 746  ? 158.401 157.875 165.470 1.00 50.26  ? 743  PHE A CE1   1 
ATOM   6873  C CE2   . PHE D 4 746  ? 156.897 156.973 167.084 1.00 50.26  ? 743  PHE A CE2   1 
ATOM   6874  C CZ    . PHE D 4 746  ? 158.130 156.972 166.474 1.00 50.26  ? 743  PHE A CZ    1 
ATOM   6875  N N     . GLN D 4 747  ? 155.153 163.128 164.104 1.00 50.26  ? 744  GLN A N     1 
ATOM   6876  C CA    . GLN D 4 747  ? 154.367 163.999 163.243 1.00 50.26  ? 744  GLN A CA    1 
ATOM   6877  C C     . GLN D 4 747  ? 153.892 163.224 162.023 1.00 50.26  ? 744  GLN A C     1 
ATOM   6878  O O     . GLN D 4 747  ? 154.666 162.494 161.398 1.00 50.26  ? 744  GLN A O     1 
ATOM   6879  C CB    . GLN D 4 747  ? 155.186 165.212 162.811 1.00 50.26  ? 744  GLN A CB    1 
ATOM   6880  C CG    . GLN D 4 747  ? 154.436 166.151 161.884 1.00 50.26  ? 744  GLN A CG    1 
ATOM   6881  C CD    . GLN D 4 747  ? 155.358 167.056 161.100 1.00 50.26  ? 744  GLN A CD    1 
ATOM   6882  O OE1   . GLN D 4 747  ? 156.515 167.250 161.468 1.00 50.26  ? 744  GLN A OE1   1 
ATOM   6883  N NE2   . GLN D 4 747  ? 154.850 167.616 160.009 1.00 50.26  ? 744  GLN A NE2   1 
ATOM   6884  N N     . ILE D 4 748  ? 152.618 163.381 161.685 1.00 50.26  ? 745  ILE A N     1 
ATOM   6885  C CA    . ILE D 4 748  ? 152.039 162.736 160.515 1.00 50.26  ? 745  ILE A CA    1 
ATOM   6886  C C     . ILE D 4 748  ? 152.327 163.612 159.303 1.00 50.26  ? 745  ILE A C     1 
ATOM   6887  O O     . ILE D 4 748  ? 151.928 164.781 159.261 1.00 50.26  ? 745  ILE A O     1 
ATOM   6888  C CB    . ILE D 4 748  ? 150.532 162.508 160.698 1.00 50.26  ? 745  ILE A CB    1 
ATOM   6889  C CG1   . ILE D 4 748  ? 150.293 161.265 161.553 1.00 50.26  ? 745  ILE A CG1   1 
ATOM   6890  C CG2   . ILE D 4 748  ? 149.842 162.376 159.359 1.00 50.26  ? 745  ILE A CG2   1 
ATOM   6891  C CD1   . ILE D 4 748  ? 148.916 161.200 162.164 1.00 50.26  ? 745  ILE A CD1   1 
ATOM   6892  N N     . TYR D 4 749  ? 153.030 163.052 158.320 1.00 50.26  ? 746  TYR A N     1 
ATOM   6893  C CA    . TYR D 4 749  ? 153.533 163.811 157.183 1.00 50.26  ? 746  TYR A CA    1 
ATOM   6894  C C     . TYR D 4 749  ? 153.199 163.082 155.891 1.00 50.26  ? 746  TYR A C     1 
ATOM   6895  O O     . TYR D 4 749  ? 153.434 161.876 155.780 1.00 50.26  ? 746  TYR A O     1 
ATOM   6896  C CB    . TYR D 4 749  ? 155.046 164.017 157.303 1.00 50.26  ? 746  TYR A CB    1 
ATOM   6897  C CG    . TYR D 4 749  ? 155.667 164.809 156.177 1.00 50.26  ? 746  TYR A CG    1 
ATOM   6898  C CD1   . TYR D 4 749  ? 156.129 164.178 155.031 1.00 50.26  ? 746  TYR A CD1   1 
ATOM   6899  C CD2   . TYR D 4 749  ? 155.803 166.186 156.264 1.00 50.26  ? 746  TYR A CD2   1 
ATOM   6900  C CE1   . TYR D 4 749  ? 156.699 164.895 154.003 1.00 50.26  ? 746  TYR A CE1   1 
ATOM   6901  C CE2   . TYR D 4 749  ? 156.373 166.912 155.240 1.00 50.26  ? 746  TYR A CE2   1 
ATOM   6902  C CZ    . TYR D 4 749  ? 156.819 166.261 154.112 1.00 50.26  ? 746  TYR A CZ    1 
ATOM   6903  O OH    . TYR D 4 749  ? 157.390 166.978 153.086 1.00 50.26  ? 746  TYR A OH    1 
ATOM   6904  N N     . ASN D 4 750  ? 152.647 163.815 154.918 1.00 50.26  ? 747  ASN A N     1 
ATOM   6905  C CA    . ASN D 4 750  ? 152.405 163.260 153.591 1.00 50.26  ? 747  ASN A CA    1 
ATOM   6906  C C     . ASN D 4 750  ? 152.664 164.283 152.487 1.00 50.26  ? 747  ASN A C     1 
ATOM   6907  O O     . ASN D 4 750  ? 151.970 164.279 151.464 1.00 50.26  ? 747  ASN A O     1 
ATOM   6908  C CB    . ASN D 4 750  ? 150.985 162.696 153.475 1.00 50.26  ? 747  ASN A CB    1 
ATOM   6909  C CG    . ASN D 4 750  ? 149.910 163.755 153.628 1.00 50.26  ? 747  ASN A CG    1 
ATOM   6910  O OD1   . ASN D 4 750  ? 150.194 164.949 153.704 1.00 50.26  ? 747  ASN A OD1   1 
ATOM   6911  N ND2   . ASN D 4 750  ? 148.658 163.317 153.658 1.00 50.26  ? 747  ASN A ND2   1 
ATOM   6912  N N     . LYS D 4 751  ? 153.621 165.190 152.700 1.00 50.26  ? 748  LYS A N     1 
ATOM   6913  C CA    . LYS D 4 751  ? 154.066 166.177 151.715 1.00 50.26  ? 748  LYS A CA    1 
ATOM   6914  C C     . LYS D 4 751  ? 153.019 167.267 151.504 1.00 50.26  ? 748  LYS A C     1 
ATOM   6915  O O     . LYS D 4 751  ? 153.294 168.289 150.866 1.00 50.26  ? 748  LYS A O     1 
ATOM   6916  C CB    . LYS D 4 751  ? 154.423 165.495 150.387 1.00 37.94  ? 748  LYS A CB    1 
ATOM   6917  C CG    . LYS D 4 751  ? 154.975 166.406 149.299 1.00 37.94  ? 748  LYS A CG    1 
ATOM   6918  C CD    . LYS D 4 751  ? 154.839 165.763 147.929 1.00 37.94  ? 748  LYS A CD    1 
ATOM   6919  C CE    . LYS D 4 751  ? 153.455 165.976 147.348 1.00 37.94  ? 748  LYS A CE    1 
ATOM   6920  N NZ    . LYS D 4 751  ? 153.311 165.312 146.025 1.00 37.94  ? 748  LYS A NZ    1 
ATOM   6921  N N     . ASP D 4 752  ? 151.830 167.087 152.067 1.00 50.26  ? 749  ASP A N     1 
ATOM   6922  C CA    . ASP D 4 752  ? 150.832 168.145 152.062 1.00 50.26  ? 749  ASP A CA    1 
ATOM   6923  C C     . ASP D 4 752  ? 150.888 168.998 153.319 1.00 50.26  ? 749  ASP A C     1 
ATOM   6924  O O     . ASP D 4 752  ? 150.210 170.028 153.384 1.00 50.26  ? 749  ASP A O     1 
ATOM   6925  C CB    . ASP D 4 752  ? 149.431 167.553 151.894 1.00 50.26  ? 749  ASP A CB    1 
ATOM   6926  C CG    . ASP D 4 752  ? 149.147 167.139 150.465 1.00 50.26  ? 749  ASP A CG    1 
ATOM   6927  O OD1   . ASP D 4 752  ? 149.798 167.682 149.549 1.00 50.26  ? 749  ASP A OD1   1 
ATOM   6928  O OD2   . ASP D 4 752  ? 148.277 166.269 150.256 1.00 50.26  ? 749  ASP A OD2   1 
ATOM   6929  N N     . PHE D 4 753  ? 151.678 168.592 154.311 1.00 50.26  ? 750  PHE A N     1 
ATOM   6930  C CA    . PHE D 4 753  ? 151.945 169.395 155.493 1.00 50.26  ? 750  PHE A CA    1 
ATOM   6931  C C     . PHE D 4 753  ? 153.313 170.059 155.439 1.00 50.26  ? 750  PHE A C     1 
ATOM   6932  O O     . PHE D 4 753  ? 153.730 170.681 156.420 1.00 50.26  ? 750  PHE A O     1 
ATOM   6933  C CB    . PHE D 4 753  ? 151.829 168.533 156.750 1.00 50.26  ? 750  PHE A CB    1 
ATOM   6934  C CG    . PHE D 4 753  ? 150.517 167.818 156.874 1.00 50.26  ? 750  PHE A CG    1 
ATOM   6935  C CD1   . PHE D 4 753  ? 149.343 168.526 157.061 1.00 50.26  ? 750  PHE A CD1   1 
ATOM   6936  C CD2   . PHE D 4 753  ? 150.456 166.440 156.799 1.00 50.26  ? 750  PHE A CD2   1 
ATOM   6937  C CE1   . PHE D 4 753  ? 148.134 167.872 157.174 1.00 50.26  ? 750  PHE A CE1   1 
ATOM   6938  C CE2   . PHE D 4 753  ? 149.249 165.780 156.911 1.00 50.26  ? 750  PHE A CE2   1 
ATOM   6939  C CZ    . PHE D 4 753  ? 148.087 166.496 157.099 1.00 50.26  ? 750  PHE A CZ    1 
ATOM   6940  N N     . ALA D 4 754  ? 154.018 169.939 154.319 1.00 50.26  ? 751  ALA A N     1 
ATOM   6941  C CA    . ALA D 4 754  ? 155.337 170.531 154.184 1.00 50.26  ? 751  ALA A CA    1 
ATOM   6942  C C     . ALA D 4 754  ? 155.239 172.050 154.071 1.00 50.26  ? 751  ALA A C     1 
ATOM   6943  O O     . ALA D 4 754  ? 154.217 172.607 153.662 1.00 50.26  ? 751  ALA A O     1 
ATOM   6944  C CB    . ALA D 4 754  ? 156.057 169.955 152.968 1.00 50.26  ? 751  ALA A CB    1 
ATOM   6945  N N     . LYS D 4 755  ? 156.329 172.724 154.445 1.00 50.26  ? 752  LYS A N     1 
ATOM   6946  C CA    . LYS D 4 755  ? 156.325 174.183 154.444 1.00 50.26  ? 752  LYS A CA    1 
ATOM   6947  C C     . LYS D 4 755  ? 156.329 174.750 153.031 1.00 50.26  ? 752  LYS A C     1 
ATOM   6948  O O     . LYS D 4 755  ? 155.871 175.877 152.817 1.00 50.26  ? 752  LYS A O     1 
ATOM   6949  C CB    . LYS D 4 755  ? 157.520 174.715 155.234 1.00 48.36  ? 752  LYS A CB    1 
ATOM   6950  C CG    . LYS D 4 755  ? 158.874 174.375 154.636 1.00 48.36  ? 752  LYS A CG    1 
ATOM   6951  C CD    . LYS D 4 755  ? 159.960 175.273 155.205 1.00 48.36  ? 752  LYS A CD    1 
ATOM   6952  C CE    . LYS D 4 755  ? 161.066 175.519 154.194 1.00 48.36  ? 752  LYS A CE    1 
ATOM   6953  N NZ    . LYS D 4 755  ? 162.266 176.130 154.830 1.00 48.36  ? 752  LYS A NZ    1 
ATOM   6954  N N     . GLY D 4 756  ? 156.835 173.996 152.062 1.00 50.26  ? 753  GLY A N     1 
ATOM   6955  C CA    . GLY D 4 756  ? 156.825 174.410 150.677 1.00 50.26  ? 753  GLY A CA    1 
ATOM   6956  C C     . GLY D 4 756  ? 155.546 174.092 149.937 1.00 50.26  ? 753  GLY A C     1 
ATOM   6957  O O     . GLY D 4 756  ? 155.464 174.332 148.728 1.00 50.26  ? 753  GLY A O     1 
ATOM   6958  N N     . HIS D 4 757  ? 154.546 173.557 150.630 1.00 50.26  ? 754  HIS A N     1 
ATOM   6959  C CA    . HIS D 4 757  ? 153.298 173.170 149.990 1.00 50.26  ? 754  HIS A CA    1 
ATOM   6960  C C     . HIS D 4 757  ? 152.523 174.384 149.496 1.00 50.26  ? 754  HIS A C     1 
ATOM   6961  O O     . HIS D 4 757  ? 152.388 175.388 150.201 1.00 50.26  ? 754  HIS A O     1 
ATOM   6962  C CB    . HIS D 4 757  ? 152.440 172.368 150.967 1.00 50.26  ? 754  HIS A CB    1 
ATOM   6963  C CG    . HIS D 4 757  ? 151.093 172.003 150.430 1.00 50.26  ? 754  HIS A CG    1 
ATOM   6964  N ND1   . HIS D 4 757  ? 149.981 172.796 150.616 1.00 50.26  ? 754  HIS A ND1   1 
ATOM   6965  C CD2   . HIS D 4 757  ? 150.677 170.934 149.711 1.00 50.26  ? 754  HIS A CD2   1 
ATOM   6966  C CE1   . HIS D 4 757  ? 148.937 172.228 150.039 1.00 50.26  ? 754  HIS A CE1   1 
ATOM   6967  N NE2   . HIS D 4 757  ? 149.333 171.099 149.480 1.00 50.26  ? 754  HIS A NE2   1 
ATOM   6968  N N     . HIS D 4 758  ? 152.012 174.283 148.271 1.00 50.26  ? 755  HIS A N     1 
ATOM   6969  C CA    . HIS D 4 758  ? 151.099 175.283 147.725 1.00 50.26  ? 755  HIS A CA    1 
ATOM   6970  C C     . HIS D 4 758  ? 150.334 174.635 146.582 1.00 50.26  ? 755  HIS A C     1 
ATOM   6971  O O     . HIS D 4 758  ? 150.945 174.108 145.648 1.00 50.26  ? 755  HIS A O     1 
ATOM   6972  C CB    . HIS D 4 758  ? 151.851 176.535 147.257 1.00 50.26  ? 755  HIS A CB    1 
ATOM   6973  C CG    . HIS D 4 758  ? 152.660 176.336 146.014 1.00 50.26  ? 755  HIS A CG    1 
ATOM   6974  N ND1   . HIS D 4 758  ? 152.103 176.359 144.753 1.00 50.26  ? 755  HIS A ND1   1 
ATOM   6975  C CD2   . HIS D 4 758  ? 153.982 176.111 145.837 1.00 50.26  ? 755  HIS A CD2   1 
ATOM   6976  C CE1   . HIS D 4 758  ? 153.048 176.157 143.853 1.00 50.26  ? 755  HIS A CE1   1 
ATOM   6977  N NE2   . HIS D 4 758  ? 154.198 176.004 144.484 1.00 50.26  ? 755  HIS A NE2   1 
ATOM   6978  N N     . GLY D 4 759  ? 149.011 174.655 146.663 1.00 50.26  ? 756  GLY A N     1 
ATOM   6979  C CA    . GLY D 4 759  ? 148.166 173.984 145.697 1.00 50.26  ? 756  GLY A CA    1 
ATOM   6980  C C     . GLY D 4 759  ? 147.242 172.984 146.364 1.00 50.26  ? 756  GLY A C     1 
ATOM   6981  O O     . GLY D 4 759  ? 147.364 172.663 147.544 1.00 50.26  ? 756  GLY A O     1 
ATOM   6982  N N     . LYS D 4 760  ? 146.300 172.497 145.567 1.00 50.26  ? 757  LYS A N     1 
ATOM   6983  C CA    . LYS D 4 760  ? 145.294 171.585 146.087 1.00 50.26  ? 757  LYS A CA    1 
ATOM   6984  C C     . LYS D 4 760  ? 145.937 170.268 146.522 1.00 50.26  ? 757  LYS A C     1 
ATOM   6985  O O     . LYS D 4 760  ? 146.833 169.757 145.843 1.00 50.26  ? 757  LYS A O     1 
ATOM   6986  C CB    . LYS D 4 760  ? 144.206 171.351 145.040 1.00 50.26  ? 757  LYS A CB    1 
ATOM   6987  C CG    . LYS D 4 760  ? 144.685 170.725 143.748 1.00 50.26  ? 757  LYS A CG    1 
ATOM   6988  C CD    . LYS D 4 760  ? 143.535 170.577 142.771 1.00 50.26  ? 757  LYS A CD    1 
ATOM   6989  C CE    . LYS D 4 760  ? 143.103 171.922 142.213 1.00 50.26  ? 757  LYS A CE    1 
ATOM   6990  N NZ    . LYS D 4 760  ? 144.158 172.535 141.360 1.00 50.26  ? 757  LYS A NZ    1 
ATOM   6991  N N     . PRO D 4 761  ? 145.516 169.708 147.661 1.00 50.26  ? 758  PRO A N     1 
ATOM   6992  C CA    . PRO D 4 761  ? 146.209 168.540 148.221 1.00 50.26  ? 758  PRO A CA    1 
ATOM   6993  C C     . PRO D 4 761  ? 145.649 167.209 147.746 1.00 50.26  ? 758  PRO A C     1 
ATOM   6994  O O     . PRO D 4 761  ? 144.700 167.166 146.959 1.00 50.26  ? 758  PRO A O     1 
ATOM   6995  C CB    . PRO D 4 761  ? 146.010 168.718 149.729 1.00 50.26  ? 758  PRO A CB    1 
ATOM   6996  C CG    . PRO D 4 761  ? 144.718 169.479 149.853 1.00 50.26  ? 758  PRO A CG    1 
ATOM   6997  C CD    . PRO D 4 761  ? 144.445 170.190 148.548 1.00 50.26  ? 758  PRO A CD    1 
ATOM   6998  N N     . ASN D 4 762  ? 146.241 166.117 148.224 1.00 50.26  ? 759  ASN A N     1 
ATOM   6999  C CA    . ASN D 4 762  ? 145.783 164.784 147.870 1.00 50.26  ? 759  ASN A CA    1 
ATOM   7000  C C     . ASN D 4 762  ? 144.436 164.485 148.522 1.00 50.26  ? 759  ASN A C     1 
ATOM   7001  O O     . ASN D 4 762  ? 144.006 165.157 149.462 1.00 50.26  ? 759  ASN A O     1 
ATOM   7002  C CB    . ASN D 4 762  ? 146.805 163.731 148.296 1.00 50.26  ? 759  ASN A CB    1 
ATOM   7003  C CG    . ASN D 4 762  ? 148.191 164.016 147.765 1.00 50.26  ? 759  ASN A CG    1 
ATOM   7004  O OD1   . ASN D 4 762  ? 148.394 164.959 147.004 1.00 50.26  ? 759  ASN A OD1   1 
ATOM   7005  N ND2   . ASN D 4 762  ? 149.156 163.199 148.167 1.00 50.26  ? 759  ASN A ND2   1 
ATOM   7006  N N     . LEU D 4 763  ? 143.766 163.456 148.001 1.00 50.26  ? 760  LEU A N     1 
ATOM   7007  C CA    . LEU D 4 763  ? 142.469 163.071 148.546 1.00 50.26  ? 760  LEU A CA    1 
ATOM   7008  C C     . LEU D 4 763  ? 142.596 162.526 149.962 1.00 50.26  ? 760  LEU A C     1 
ATOM   7009  O O     . LEU D 4 763  ? 141.734 162.783 150.808 1.00 50.26  ? 760  LEU A O     1 
ATOM   7010  C CB    . LEU D 4 763  ? 141.800 162.042 147.639 1.00 50.26  ? 760  LEU A CB    1 
ATOM   7011  C CG    . LEU D 4 763  ? 141.225 162.587 146.334 1.00 50.26  ? 760  LEU A CG    1 
ATOM   7012  C CD1   . LEU D 4 763  ? 140.523 161.484 145.568 1.00 50.26  ? 760  LEU A CD1   1 
ATOM   7013  C CD2   . LEU D 4 763  ? 140.283 163.743 146.609 1.00 50.26  ? 760  LEU A CD2   1 
ATOM   7014  N N     . HIS D 4 764  ? 143.650 161.754 150.234 1.00 50.26  ? 761  HIS A N     1 
ATOM   7015  C CA    . HIS D 4 764  ? 143.836 161.205 151.574 1.00 50.26  ? 761  HIS A CA    1 
ATOM   7016  C C     . HIS D 4 764  ? 144.101 162.308 152.591 1.00 50.26  ? 761  HIS A C     1 
ATOM   7017  O O     . HIS D 4 764  ? 143.633 162.234 153.734 1.00 50.26  ? 761  HIS A O     1 
ATOM   7018  C CB    . HIS D 4 764  ? 144.971 160.186 151.565 1.00 50.26  ? 761  HIS A CB    1 
ATOM   7019  C CG    . HIS D 4 764  ? 144.580 158.860 150.993 1.00 50.26  ? 761  HIS A CG    1 
ATOM   7020  N ND1   . HIS D 4 764  ? 143.828 158.739 149.845 1.00 50.26  ? 761  HIS A ND1   1 
ATOM   7021  C CD2   . HIS D 4 764  ? 144.836 157.597 151.410 1.00 50.26  ? 761  HIS A CD2   1 
ATOM   7022  C CE1   . HIS D 4 764  ? 143.635 157.460 149.580 1.00 50.26  ? 761  HIS A CE1   1 
ATOM   7023  N NE2   . HIS D 4 764  ? 144.237 156.746 150.514 1.00 50.26  ? 761  HIS A NE2   1 
ATOM   7024  N N     . THR D 4 765  ? 144.851 163.337 152.195 1.00 50.26  ? 762  THR A N     1 
ATOM   7025  C CA    . THR D 4 765  ? 145.034 164.491 153.067 1.00 50.26  ? 762  THR A CA    1 
ATOM   7026  C C     . THR D 4 765  ? 143.701 165.163 153.362 1.00 50.26  ? 762  THR A C     1 
ATOM   7027  O O     . THR D 4 765  ? 143.450 165.589 154.495 1.00 50.26  ? 762  THR A O     1 
ATOM   7028  C CB    . THR D 4 765  ? 146.010 165.480 152.430 1.00 50.26  ? 762  THR A CB    1 
ATOM   7029  O OG1   . THR D 4 765  ? 147.323 164.909 152.407 1.00 50.26  ? 762  THR A OG1   1 
ATOM   7030  C CG2   . THR D 4 765  ? 146.047 166.781 153.214 1.00 50.26  ? 762  THR A CG2   1 
ATOM   7031  N N     . LEU D 4 766  ? 142.832 165.265 152.355 1.00 50.26  ? 763  LEU A N     1 
ATOM   7032  C CA    . LEU D 4 766  ? 141.510 165.839 152.578 1.00 50.26  ? 763  LEU A CA    1 
ATOM   7033  C C     . LEU D 4 766  ? 140.680 164.979 153.521 1.00 50.26  ? 763  LEU A C     1 
ATOM   7034  O O     . LEU D 4 766  ? 139.964 165.509 154.375 1.00 50.26  ? 763  LEU A O     1 
ATOM   7035  C CB    . LEU D 4 766  ? 140.784 166.025 151.252 1.00 50.26  ? 763  LEU A CB    1 
ATOM   7036  C CG    . LEU D 4 766  ? 140.926 167.415 150.646 1.00 50.26  ? 763  LEU A CG    1 
ATOM   7037  C CD1   . LEU D 4 766  ? 140.290 167.435 149.285 1.00 50.26  ? 763  LEU A CD1   1 
ATOM   7038  C CD2   . LEU D 4 766  ? 140.293 168.455 151.551 1.00 50.26  ? 763  LEU A CD2   1 
ATOM   7039  N N     . TYR D 4 767  ? 140.749 163.655 153.371 1.00 50.26  ? 764  TYR A N     1 
ATOM   7040  C CA    . TYR D 4 767  ? 140.048 162.769 154.295 1.00 50.26  ? 764  TYR A CA    1 
ATOM   7041  C C     . TYR D 4 767  ? 140.529 162.989 155.721 1.00 50.26  ? 764  TYR A C     1 
ATOM   7042  O O     . TYR D 4 767  ? 139.726 163.110 156.653 1.00 50.26  ? 764  TYR A O     1 
ATOM   7043  C CB    . TYR D 4 767  ? 140.256 161.308 153.894 1.00 50.26  ? 764  TYR A CB    1 
ATOM   7044  C CG    . TYR D 4 767  ? 139.587 160.885 152.607 1.00 50.26  ? 764  TYR A CG    1 
ATOM   7045  C CD1   . TYR D 4 767  ? 138.384 161.444 152.206 1.00 50.26  ? 764  TYR A CD1   1 
ATOM   7046  C CD2   . TYR D 4 767  ? 140.154 159.908 151.803 1.00 50.26  ? 764  TYR A CD2   1 
ATOM   7047  C CE1   . TYR D 4 767  ? 137.771 161.049 151.033 1.00 50.26  ? 764  TYR A CE1   1 
ATOM   7048  C CE2   . TYR D 4 767  ? 139.551 159.507 150.632 1.00 50.26  ? 764  TYR A CE2   1 
ATOM   7049  C CZ    . TYR D 4 767  ? 138.361 160.079 150.251 1.00 50.26  ? 764  TYR A CZ    1 
ATOM   7050  O OH    . TYR D 4 767  ? 137.761 159.677 149.081 1.00 50.26  ? 764  TYR A OH    1 
ATOM   7051  N N     . TRP D 4 768  ? 141.849 163.052 155.905 1.00 50.26  ? 765  TRP A N     1 
ATOM   7052  C CA    . TRP D 4 768  ? 142.407 163.242 157.239 1.00 50.26  ? 765  TRP A CA    1 
ATOM   7053  C C     . TRP D 4 768  ? 142.000 164.587 157.825 1.00 50.26  ? 765  TRP A C     1 
ATOM   7054  O O     . TRP D 4 768  ? 141.646 164.677 159.006 1.00 50.26  ? 765  TRP A O     1 
ATOM   7055  C CB    . TRP D 4 768  ? 143.928 163.118 157.186 1.00 50.26  ? 765  TRP A CB    1 
ATOM   7056  C CG    . TRP D 4 768  ? 144.567 163.084 158.526 1.00 50.26  ? 765  TRP A CG    1 
ATOM   7057  C CD1   . TRP D 4 768  ? 145.338 164.053 159.091 1.00 50.26  ? 765  TRP A CD1   1 
ATOM   7058  C CD2   . TRP D 4 768  ? 144.495 162.021 159.479 1.00 50.26  ? 765  TRP A CD2   1 
ATOM   7059  N NE1   . TRP D 4 768  ? 145.752 163.661 160.339 1.00 50.26  ? 765  TRP A NE1   1 
ATOM   7060  C CE2   . TRP D 4 768  ? 145.246 162.415 160.601 1.00 50.26  ? 765  TRP A CE2   1 
ATOM   7061  C CE3   . TRP D 4 768  ? 143.867 160.773 159.493 1.00 50.26  ? 765  TRP A CE3   1 
ATOM   7062  C CZ2   . TRP D 4 768  ? 145.387 161.607 161.723 1.00 50.26  ? 765  TRP A CZ2   1 
ATOM   7063  C CZ3   . TRP D 4 768  ? 144.008 159.974 160.607 1.00 50.26  ? 765  TRP A CZ3   1 
ATOM   7064  C CH2   . TRP D 4 768  ? 144.762 160.393 161.706 1.00 50.26  ? 765  TRP A CH2   1 
ATOM   7065  N N     . THR D 4 769  ? 142.049 165.647 157.016 1.00 50.26  ? 766  THR A N     1 
ATOM   7066  C CA    . THR D 4 769  ? 141.689 166.974 157.504 1.00 50.26  ? 766  THR A CA    1 
ATOM   7067  C C     . THR D 4 769  ? 140.207 167.059 157.845 1.00 50.26  ? 766  THR A C     1 
ATOM   7068  O O     . THR D 4 769  ? 139.833 167.637 158.872 1.00 50.26  ? 766  THR A O     1 
ATOM   7069  C CB    . THR D 4 769  ? 142.063 168.030 156.465 1.00 50.26  ? 766  THR A CB    1 
ATOM   7070  O OG1   . THR D 4 769  ? 143.480 168.008 156.252 1.00 50.26  ? 766  THR A OG1   1 
ATOM   7071  C CG2   . THR D 4 769  ? 141.651 169.414 156.937 1.00 50.26  ? 766  THR A CG2   1 
ATOM   7072  N N     . GLY D 4 770  ? 139.346 166.484 157.003 1.00 50.26  ? 767  GLY A N     1 
ATOM   7073  C CA    . GLY D 4 770  ? 137.919 166.522 157.254 1.00 50.26  ? 767  GLY A CA    1 
ATOM   7074  C C     . GLY D 4 770  ? 137.463 165.581 158.345 1.00 50.26  ? 767  GLY A C     1 
ATOM   7075  O O     . GLY D 4 770  ? 136.349 165.735 158.854 1.00 50.26  ? 767  GLY A O     1 
ATOM   7076  N N     . LEU D 4 771  ? 138.294 164.604 158.711 1.00 50.26  ? 768  LEU A N     1 
ATOM   7077  C CA    . LEU D 4 771  ? 137.953 163.740 159.835 1.00 50.26  ? 768  LEU A CA    1 
ATOM   7078  C C     . LEU D 4 771  ? 137.899 164.534 161.133 1.00 50.26  ? 768  LEU A C     1 
ATOM   7079  O O     . LEU D 4 771  ? 137.037 164.291 161.984 1.00 50.26  ? 768  LEU A O     1 
ATOM   7080  C CB    . LEU D 4 771  ? 138.960 162.596 159.940 1.00 50.26  ? 768  LEU A CB    1 
ATOM   7081  C CG    . LEU D 4 771  ? 138.601 161.408 160.835 1.00 50.26  ? 768  LEU A CG    1 
ATOM   7082  C CD1   . LEU D 4 771  ? 139.263 160.158 160.303 1.00 50.26  ? 768  LEU A CD1   1 
ATOM   7083  C CD2   . LEU D 4 771  ? 139.016 161.640 162.274 1.00 50.26  ? 768  LEU A CD2   1 
ATOM   7084  N N     . PHE D 4 772  ? 138.815 165.484 161.303 1.00 50.26  ? 769  PHE A N     1 
ATOM   7085  C CA    . PHE D 4 772  ? 138.894 166.297 162.506 1.00 50.26  ? 769  PHE A CA    1 
ATOM   7086  C C     . PHE D 4 772  ? 138.319 167.692 162.313 1.00 50.26  ? 769  PHE A C     1 
ATOM   7087  O O     . PHE D 4 772  ? 138.568 168.573 163.141 1.00 50.26  ? 769  PHE A O     1 
ATOM   7088  C CB    . PHE D 4 772  ? 140.344 166.388 162.979 1.00 50.26  ? 769  PHE A CB    1 
ATOM   7089  C CG    . PHE D 4 772  ? 140.955 165.059 163.306 1.00 50.26  ? 769  PHE A CG    1 
ATOM   7090  C CD1   . PHE D 4 772  ? 140.544 164.350 164.420 1.00 50.26  ? 769  PHE A CD1   1 
ATOM   7091  C CD2   . PHE D 4 772  ? 141.933 164.513 162.495 1.00 50.26  ? 769  PHE A CD2   1 
ATOM   7092  C CE1   . PHE D 4 772  ? 141.102 163.128 164.724 1.00 50.26  ? 769  PHE A CE1   1 
ATOM   7093  C CE2   . PHE D 4 772  ? 142.492 163.289 162.794 1.00 50.26  ? 769  PHE A CE2   1 
ATOM   7094  C CZ    . PHE D 4 772  ? 142.075 162.596 163.909 1.00 50.26  ? 769  PHE A CZ    1 
ATOM   7095  N N     . SER D 4 773  ? 137.568 167.916 161.239 1.00 50.26  ? 770  SER A N     1 
ATOM   7096  C CA    . SER D 4 773  ? 136.942 169.208 161.026 1.00 50.26  ? 770  SER A CA    1 
ATOM   7097  C C     . SER D 4 773  ? 135.898 169.473 162.109 1.00 50.26  ? 770  SER A C     1 
ATOM   7098  O O     . SER D 4 773  ? 135.278 168.539 162.625 1.00 50.26  ? 770  SER A O     1 
ATOM   7099  C CB    . SER D 4 773  ? 136.288 169.264 159.650 1.00 50.26  ? 770  SER A CB    1 
ATOM   7100  O OG    . SER D 4 773  ? 137.258 169.437 158.633 1.00 50.26  ? 770  SER A OG    1 
ATOM   7101  N N     . PRO D 4 774  ? 135.697 170.740 162.483 1.00 50.26  ? 771  PRO A N     1 
ATOM   7102  C CA    . PRO D 4 774  ? 134.696 171.039 163.521 1.00 50.26  ? 771  PRO A CA    1 
ATOM   7103  C C     . PRO D 4 774  ? 133.300 170.554 163.173 1.00 50.26  ? 771  PRO A C     1 
ATOM   7104  O O     . PRO D 4 774  ? 132.570 170.094 164.059 1.00 50.26  ? 771  PRO A O     1 
ATOM   7105  C CB    . PRO D 4 774  ? 134.757 172.568 163.629 1.00 50.26  ? 771  PRO A CB    1 
ATOM   7106  C CG    . PRO D 4 774  ? 136.117 172.927 163.143 1.00 50.26  ? 771  PRO A CG    1 
ATOM   7107  C CD    . PRO D 4 774  ? 136.438 171.940 162.064 1.00 50.26  ? 771  PRO A CD    1 
ATOM   7108  N N     . GLU D 4 775  ? 132.908 170.637 161.900 1.00 50.26  ? 772  GLU A N     1 
ATOM   7109  C CA    . GLU D 4 775  ? 131.589 170.152 161.509 1.00 50.26  ? 772  GLU A CA    1 
ATOM   7110  C C     . GLU D 4 775  ? 131.503 168.634 161.613 1.00 50.26  ? 772  GLU A C     1 
ATOM   7111  O O     . GLU D 4 775  ? 130.444 168.091 161.947 1.00 50.26  ? 772  GLU A O     1 
ATOM   7112  C CB    . GLU D 4 775  ? 131.247 170.624 160.096 1.00 50.26  ? 772  GLU A CB    1 
ATOM   7113  C CG    . GLU D 4 775  ? 132.218 170.169 159.023 1.00 50.26  ? 772  GLU A CG    1 
ATOM   7114  C CD    . GLU D 4 775  ? 133.325 171.176 158.780 1.00 50.26  ? 772  GLU A CD    1 
ATOM   7115  O OE1   . GLU D 4 775  ? 133.513 172.072 159.629 1.00 50.26  ? 772  GLU A OE1   1 
ATOM   7116  O OE2   . GLU D 4 775  ? 134.006 171.073 157.738 1.00 50.26  ? 772  GLU A OE2   1 
ATOM   7117  N N     . ASN D 4 776  ? 132.601 167.932 161.326 1.00 50.26  ? 773  ASN A N     1 
ATOM   7118  C CA    . ASN D 4 776  ? 132.599 166.481 161.482 1.00 50.26  ? 773  ASN A CA    1 
ATOM   7119  C C     . ASN D 4 776  ? 132.599 166.086 162.952 1.00 50.26  ? 773  ASN A C     1 
ATOM   7120  O O     . ASN D 4 776  ? 131.970 165.093 163.332 1.00 50.26  ? 773  ASN A O     1 
ATOM   7121  C CB    . ASN D 4 776  ? 133.797 165.867 160.764 1.00 50.26  ? 773  ASN A CB    1 
ATOM   7122  C CG    . ASN D 4 776  ? 133.802 164.356 160.837 1.00 50.26  ? 773  ASN A CG    1 
ATOM   7123  O OD1   . ASN D 4 776  ? 132.956 163.692 160.241 1.00 50.26  ? 773  ASN A OD1   1 
ATOM   7124  N ND2   . ASN D 4 776  ? 134.753 163.802 161.577 1.00 50.26  ? 773  ASN A ND2   1 
ATOM   7125  N N     . LEU D 4 777  ? 133.309 166.840 163.791 1.00 50.26  ? 774  LEU A N     1 
ATOM   7126  C CA    . LEU D 4 777  ? 133.279 166.567 165.224 1.00 50.26  ? 774  LEU A CA    1 
ATOM   7127  C C     . LEU D 4 777  ? 131.886 166.798 165.796 1.00 50.26  ? 774  LEU A C     1 
ATOM   7128  O O     . LEU D 4 777  ? 131.410 166.014 166.624 1.00 50.26  ? 774  LEU A O     1 
ATOM   7129  C CB    . LEU D 4 777  ? 134.308 167.436 165.947 1.00 50.26  ? 774  LEU A CB    1 
ATOM   7130  C CG    . LEU D 4 777  ? 135.777 167.174 165.617 1.00 50.26  ? 774  LEU A CG    1 
ATOM   7131  C CD1   . LEU D 4 777  ? 136.662 168.239 166.237 1.00 50.26  ? 774  LEU A CD1   1 
ATOM   7132  C CD2   . LEU D 4 777  ? 136.192 165.794 166.086 1.00 50.26  ? 774  LEU A CD2   1 
ATOM   7133  N N     . ALA D 4 778  ? 131.220 167.873 165.368 1.00 50.26  ? 775  ALA A N     1 
ATOM   7134  C CA    . ALA D 4 778  ? 129.874 168.153 165.857 1.00 50.26  ? 775  ALA A CA    1 
ATOM   7135  C C     . ALA D 4 778  ? 128.884 167.083 165.414 1.00 50.26  ? 775  ALA A C     1 
ATOM   7136  O O     . ALA D 4 778  ? 128.050 166.635 166.209 1.00 50.26  ? 775  ALA A O     1 
ATOM   7137  C CB    . ALA D 4 778  ? 129.422 169.533 165.382 1.00 50.26  ? 775  ALA A CB    1 
ATOM   7138  N N     . LYS D 4 779  ? 128.959 166.662 164.154 1.00 50.26  ? 776  LYS A N     1 
ATOM   7139  C CA    . LYS D 4 779  ? 128.088 165.616 163.621 1.00 50.26  ? 776  LYS A CA    1 
ATOM   7140  C C     . LYS D 4 779  ? 128.954 164.662 162.814 1.00 50.26  ? 776  LYS A C     1 
ATOM   7141  O O     . LYS D 4 779  ? 129.455 165.030 161.747 1.00 50.26  ? 776  LYS A O     1 
ATOM   7142  C CB    . LYS D 4 779  ? 126.970 166.203 162.762 1.00 50.26  ? 776  LYS A CB    1 
ATOM   7143  C CG    . LYS D 4 779  ? 126.100 165.156 162.088 1.00 50.26  ? 776  LYS A CG    1 
ATOM   7144  C CD    . LYS D 4 779  ? 124.655 165.617 161.990 1.00 50.26  ? 776  LYS A CD    1 
ATOM   7145  C CE    . LYS D 4 779  ? 123.753 164.498 161.501 1.00 50.26  ? 776  LYS A CE    1 
ATOM   7146  N NZ    . LYS D 4 779  ? 124.195 163.965 160.183 1.00 50.26  ? 776  LYS A NZ    1 
ATOM   7147  N N     . THR D 4 780  ? 129.127 163.443 163.318 1.00 50.26  ? 777  THR A N     1 
ATOM   7148  C CA    . THR D 4 780  ? 130.077 162.514 162.723 1.00 50.26  ? 777  THR A CA    1 
ATOM   7149  C C     . THR D 4 780  ? 129.655 162.111 161.317 1.00 50.26  ? 777  THR A C     1 
ATOM   7150  O O     . THR D 4 780  ? 128.509 161.718 161.084 1.00 50.26  ? 777  THR A O     1 
ATOM   7151  C CB    . THR D 4 780  ? 130.219 161.270 163.597 1.00 50.26  ? 777  THR A CB    1 
ATOM   7152  O OG1   . THR D 4 780  ? 130.722 161.642 164.886 1.00 50.26  ? 777  THR A OG1   1 
ATOM   7153  C CG2   . THR D 4 780  ? 131.166 160.275 162.952 1.00 50.26  ? 777  THR A CG2   1 
ATOM   7154  N N     . SER D 4 781  ? 130.595 162.214 160.380 1.00 50.26  ? 778  SER A N     1 
ATOM   7155  C CA    . SER D 4 781  ? 130.437 161.659 159.044 1.00 50.26  ? 778  SER A CA    1 
ATOM   7156  C C     . SER D 4 781  ? 131.616 160.809 158.603 1.00 50.26  ? 778  SER A C     1 
ATOM   7157  O O     . SER D 4 781  ? 131.433 159.940 157.742 1.00 50.26  ? 778  SER A O     1 
ATOM   7158  C CB    . SER D 4 781  ? 130.218 162.776 158.015 1.00 50.26  ? 778  SER A CB    1 
ATOM   7159  O OG    . SER D 4 781  ? 129.733 162.249 156.794 1.00 50.26  ? 778  SER A OG    1 
ATOM   7160  N N     . ILE D 4 782  ? 132.808 161.026 159.151 1.00 50.26  ? 779  ILE A N     1 
ATOM   7161  C CA    . ILE D 4 782  ? 133.968 160.174 158.925 1.00 50.26  ? 779  ILE A CA    1 
ATOM   7162  C C     . ILE D 4 782  ? 134.405 159.639 160.280 1.00 50.26  ? 779  ILE A C     1 
ATOM   7163  O O     . ILE D 4 782  ? 134.714 160.421 161.188 1.00 50.26  ? 779  ILE A O     1 
ATOM   7164  C CB    . ILE D 4 782  ? 135.115 160.933 158.243 1.00 50.26  ? 779  ILE A CB    1 
ATOM   7165  C CG1   . ILE D 4 782  ? 134.610 161.678 157.009 1.00 50.26  ? 779  ILE A CG1   1 
ATOM   7166  C CG2   . ILE D 4 782  ? 136.232 159.979 157.867 1.00 50.26  ? 779  ILE A CG2   1 
ATOM   7167  C CD1   . ILE D 4 782  ? 135.681 162.474 156.303 1.00 50.26  ? 779  ILE A CD1   1 
ATOM   7168  N N     . LYS D 4 783  ? 134.431 158.319 160.419 1.00 50.26  ? 780  LYS A N     1 
ATOM   7169  C CA    . LYS D 4 783  ? 134.766 157.682 161.683 1.00 50.26  ? 780  LYS A CA    1 
ATOM   7170  C C     . LYS D 4 783  ? 136.234 157.282 161.696 1.00 50.26  ? 780  LYS A C     1 
ATOM   7171  O O     . LYS D 4 783  ? 136.786 156.868 160.674 1.00 50.26  ? 780  LYS A O     1 
ATOM   7172  C CB    . LYS D 4 783  ? 133.892 156.451 161.929 1.00 50.26  ? 780  LYS A CB    1 
ATOM   7173  C CG    . LYS D 4 783  ? 134.131 155.793 163.278 1.00 50.26  ? 780  LYS A CG    1 
ATOM   7174  C CD    . LYS D 4 783  ? 133.366 154.494 163.416 1.00 50.26  ? 780  LYS A CD    1 
ATOM   7175  C CE    . LYS D 4 783  ? 133.889 153.674 164.581 1.00 50.26  ? 780  LYS A CE    1 
ATOM   7176  N NZ    . LYS D 4 783  ? 133.540 152.234 164.448 1.00 50.26  ? 780  LYS A NZ    1 
ATOM   7177  N N     . LEU D 4 784  ? 136.861 157.413 162.861 1.00 50.26  ? 781  LEU A N     1 
ATOM   7178  C CA    . LEU D 4 784  ? 138.247 157.005 163.067 1.00 50.26  ? 781  LEU A CA    1 
ATOM   7179  C C     . LEU D 4 784  ? 138.232 155.604 163.667 1.00 50.26  ? 781  LEU A C     1 
ATOM   7180  O O     . LEU D 4 784  ? 138.038 155.434 164.873 1.00 50.26  ? 781  LEU A O     1 
ATOM   7181  C CB    . LEU D 4 784  ? 138.970 157.996 163.972 1.00 50.26  ? 781  LEU A CB    1 
ATOM   7182  C CG    . LEU D 4 784  ? 140.412 157.655 164.335 1.00 50.26  ? 781  LEU A CG    1 
ATOM   7183  C CD1   . LEU D 4 784  ? 141.191 157.330 163.083 1.00 50.26  ? 781  LEU A CD1   1 
ATOM   7184  C CD2   . LEU D 4 784  ? 141.058 158.804 165.083 1.00 50.26  ? 781  LEU A CD2   1 
ATOM   7185  N N     . ASN D 4 785  ? 138.431 154.598 162.821 1.00 50.26  ? 782  ASN A N     1 
ATOM   7186  C CA    . ASN D 4 785  ? 138.391 153.220 163.281 1.00 50.26  ? 782  ASN A CA    1 
ATOM   7187  C C     . ASN D 4 785  ? 139.679 152.855 164.010 1.00 50.26  ? 782  ASN A C     1 
ATOM   7188  O O     . ASN D 4 785  ? 140.704 153.534 163.905 1.00 50.26  ? 782  ASN A O     1 
ATOM   7189  C CB    . ASN D 4 785  ? 138.175 152.267 162.108 1.00 50.26  ? 782  ASN A CB    1 
ATOM   7190  C CG    . ASN D 4 785  ? 136.909 152.568 161.342 1.00 50.26  ? 782  ASN A CG    1 
ATOM   7191  O OD1   . ASN D 4 785  ? 136.949 152.872 160.151 1.00 50.26  ? 782  ASN A OD1   1 
ATOM   7192  N ND2   . ASN D 4 785  ? 135.773 152.488 162.022 1.00 50.26  ? 782  ASN A ND2   1 
ATOM   7193  N N     . GLY D 4 786  ? 139.615 151.760 164.759 1.00 50.26  ? 783  GLY A N     1 
ATOM   7194  C CA    . GLY D 4 786  ? 140.769 151.240 165.459 1.00 50.26  ? 783  GLY A CA    1 
ATOM   7195  C C     . GLY D 4 786  ? 141.598 150.336 164.571 1.00 50.26  ? 783  GLY A C     1 
ATOM   7196  O O     . GLY D 4 786  ? 141.560 150.418 163.341 1.00 50.26  ? 783  GLY A O     1 
ATOM   7197  N N     . GLN D 4 787  ? 142.363 149.455 165.217 1.00 50.26  ? 784  GLN A N     1 
ATOM   7198  C CA    . GLN D 4 787  ? 143.208 148.481 164.525 1.00 50.26  ? 784  GLN A CA    1 
ATOM   7199  C C     . GLN D 4 787  ? 144.210 149.164 163.597 1.00 50.26  ? 784  GLN A C     1 
ATOM   7200  O O     . GLN D 4 787  ? 144.476 148.696 162.489 1.00 50.26  ? 784  GLN A O     1 
ATOM   7201  C CB    . GLN D 4 787  ? 142.364 147.464 163.754 1.00 50.26  ? 784  GLN A CB    1 
ATOM   7202  C CG    . GLN D 4 787  ? 141.558 146.534 164.638 1.00 50.26  ? 784  GLN A CG    1 
ATOM   7203  C CD    . GLN D 4 787  ? 142.408 145.447 165.262 1.00 50.26  ? 784  GLN A CD    1 
ATOM   7204  O OE1   . GLN D 4 787  ? 142.722 144.445 164.622 1.00 50.26  ? 784  GLN A OE1   1 
ATOM   7205  N NE2   . GLN D 4 787  ? 142.786 145.641 166.519 1.00 50.26  ? 784  GLN A NE2   1 
ATOM   7206  N N     . ALA D 4 788  ? 144.768 150.282 164.051 1.00 50.26  ? 785  ALA A N     1 
ATOM   7207  C CA    . ALA D 4 788  ? 145.819 150.944 163.297 1.00 50.26  ? 785  ALA A CA    1 
ATOM   7208  C C     . ALA D 4 788  ? 147.114 150.139 163.384 1.00 50.26  ? 785  ALA A C     1 
ATOM   7209  O O     . ALA D 4 788  ? 147.290 149.282 164.254 1.00 50.26  ? 785  ALA A O     1 
ATOM   7210  C CB    . ALA D 4 788  ? 146.037 152.364 163.813 1.00 50.26  ? 785  ALA A CB    1 
ATOM   7211  N N     . GLU D 4 789  ? 148.030 150.421 162.462 1.00 50.26  ? 786  GLU A N     1 
ATOM   7212  C CA    . GLU D 4 789  ? 149.297 149.708 162.406 1.00 50.26  ? 786  GLU A CA    1 
ATOM   7213  C C     . GLU D 4 789  ? 150.433 150.688 162.158 1.00 50.26  ? 786  GLU A C     1 
ATOM   7214  O O     . GLU D 4 789  ? 150.250 151.731 161.527 1.00 50.26  ? 786  GLU A O     1 
ATOM   7215  C CB    . GLU D 4 789  ? 149.291 148.631 161.316 1.00 50.26  ? 786  GLU A CB    1 
ATOM   7216  C CG    . GLU D 4 789  ? 148.565 147.357 161.709 1.00 50.26  ? 786  GLU A CG    1 
ATOM   7217  C CD    . GLU D 4 789  ? 147.852 146.707 160.541 1.00 50.26  ? 786  GLU A CD    1 
ATOM   7218  O OE1   . GLU D 4 789  ? 147.921 147.255 159.421 1.00 50.26  ? 786  GLU A OE1   1 
ATOM   7219  O OE2   . GLU D 4 789  ? 147.223 145.647 160.743 1.00 50.26  ? 786  GLU A OE2   1 
ATOM   7220  N N     . LEU D 4 790  ? 151.610 150.336 162.664 1.00 50.26  ? 787  LEU A N     1 
ATOM   7221  C CA    . LEU D 4 790  ? 152.832 151.090 162.442 1.00 50.26  ? 787  LEU A CA    1 
ATOM   7222  C C     . LEU D 4 790  ? 153.848 150.196 161.748 1.00 50.26  ? 787  LEU A C     1 
ATOM   7223  O O     . LEU D 4 790  ? 153.911 148.991 162.004 1.00 50.26  ? 787  LEU A O     1 
ATOM   7224  C CB    . LEU D 4 790  ? 153.417 151.617 163.756 1.00 50.26  ? 787  LEU A CB    1 
ATOM   7225  C CG    . LEU D 4 790  ? 152.801 152.880 164.358 1.00 50.26  ? 787  LEU A CG    1 
ATOM   7226  C CD1   . LEU D 4 790  ? 151.477 152.580 165.036 1.00 50.26  ? 787  LEU A CD1   1 
ATOM   7227  C CD2   . LEU D 4 790  ? 153.771 153.515 165.336 1.00 50.26  ? 787  LEU A CD2   1 
ATOM   7228  N N     . PHE D 4 791  ? 154.645 150.791 160.866 1.00 50.26  ? 788  PHE A N     1 
ATOM   7229  C CA    . PHE D 4 791  ? 155.620 150.050 160.082 1.00 50.26  ? 788  PHE A CA    1 
ATOM   7230  C C     . PHE D 4 791  ? 156.958 150.775 160.100 1.00 50.26  ? 788  PHE A C     1 
ATOM   7231  O O     . PHE D 4 791  ? 157.090 151.879 160.634 1.00 50.26  ? 788  PHE A O     1 
ATOM   7232  C CB    . PHE D 4 791  ? 155.144 149.853 158.638 1.00 50.26  ? 788  PHE A CB    1 
ATOM   7233  C CG    . PHE D 4 791  ? 153.948 148.958 158.511 1.00 50.26  ? 788  PHE A CG    1 
ATOM   7234  C CD1   . PHE D 4 791  ? 154.099 147.585 158.448 1.00 50.26  ? 788  PHE A CD1   1 
ATOM   7235  C CD2   . PHE D 4 791  ? 152.674 149.488 158.449 1.00 50.26  ? 788  PHE A CD2   1 
ATOM   7236  C CE1   . PHE D 4 791  ? 153.003 146.759 158.330 1.00 50.26  ? 788  PHE A CE1   1 
ATOM   7237  C CE2   . PHE D 4 791  ? 151.574 148.665 158.330 1.00 50.26  ? 788  PHE A CE2   1 
ATOM   7238  C CZ    . PHE D 4 791  ? 151.739 147.299 158.272 1.00 50.26  ? 788  PHE A CZ    1 
ATOM   7239  N N     . TYR D 4 792  ? 157.958 150.132 159.503 1.00 50.26  ? 789  TYR A N     1 
ATOM   7240  C CA    . TYR D 4 792  ? 159.305 150.677 159.430 1.00 50.26  ? 789  TYR A CA    1 
ATOM   7241  C C     . TYR D 4 792  ? 159.982 150.097 158.200 1.00 50.26  ? 789  TYR A C     1 
ATOM   7242  O O     . TYR D 4 792  ? 159.986 148.877 158.012 1.00 50.26  ? 789  TYR A O     1 
ATOM   7243  C CB    . TYR D 4 792  ? 160.097 150.348 160.699 1.00 50.26  ? 789  TYR A CB    1 
ATOM   7244  C CG    . TYR D 4 792  ? 161.553 150.755 160.680 1.00 50.26  ? 789  TYR A CG    1 
ATOM   7245  C CD1   . TYR D 4 792  ? 162.522 149.920 160.143 1.00 50.26  ? 789  TYR A CD1   1 
ATOM   7246  C CD2   . TYR D 4 792  ? 161.962 151.964 161.221 1.00 50.26  ? 789  TYR A CD2   1 
ATOM   7247  C CE1   . TYR D 4 792  ? 163.850 150.281 160.133 1.00 50.26  ? 789  TYR A CE1   1 
ATOM   7248  C CE2   . TYR D 4 792  ? 163.291 152.335 161.215 1.00 50.26  ? 789  TYR A CE2   1 
ATOM   7249  C CZ    . TYR D 4 792  ? 164.229 151.489 160.670 1.00 50.26  ? 789  TYR A CZ    1 
ATOM   7250  O OH    . TYR D 4 792  ? 165.554 151.847 160.663 1.00 50.26  ? 789  TYR A OH    1 
ATOM   7251  N N     . ARG D 4 793  ? 160.545 150.964 157.371 1.00 50.26  ? 790  ARG A N     1 
ATOM   7252  C CA    . ARG D 4 793  ? 161.175 150.550 156.118 1.00 50.26  ? 790  ARG A CA    1 
ATOM   7253  C C     . ARG D 4 793  ? 162.661 150.861 156.155 1.00 50.26  ? 790  ARG A C     1 
ATOM   7254  O O     . ARG D 4 793  ? 163.044 152.043 156.063 1.00 50.26  ? 790  ARG A O     1 
ATOM   7255  C CB    . ARG D 4 793  ? 160.516 151.251 154.932 1.00 50.26  ? 790  ARG A CB    1 
ATOM   7256  C CG    . ARG D 4 793  ? 161.108 150.880 153.591 1.00 50.26  ? 790  ARG A CG    1 
ATOM   7257  C CD    . ARG D 4 793  ? 160.407 151.621 152.474 1.00 50.26  ? 790  ARG A CD    1 
ATOM   7258  N NE    . ARG D 4 793  ? 160.768 153.032 152.453 1.00 50.26  ? 790  ARG A NE    1 
ATOM   7259  C CZ    . ARG D 4 793  ? 159.994 153.994 151.973 1.00 50.26  ? 790  ARG A CZ    1 
ATOM   7260  N NH1   . ARG D 4 793  ? 158.801 153.733 151.467 1.00 50.26  ? 790  ARG A NH1   1 
ATOM   7261  N NH2   . ARG D 4 793  ? 160.429 155.250 152.000 1.00 50.26  ? 790  ARG A NH2   1 
ATOM   7262  N N     . PRO D 4 794  ? 163.531 149.862 156.297 1.00 50.26  ? 791  PRO A N     1 
ATOM   7263  C CA    . PRO D 4 794  ? 164.971 150.134 156.273 1.00 50.26  ? 791  PRO A CA    1 
ATOM   7264  C C     . PRO D 4 794  ? 165.392 150.732 154.942 1.00 50.26  ? 791  PRO A C     1 
ATOM   7265  O O     . PRO D 4 794  ? 164.843 150.403 153.888 1.00 50.26  ? 791  PRO A O     1 
ATOM   7266  C CB    . PRO D 4 794  ? 165.598 148.751 156.488 1.00 50.26  ? 791  PRO A CB    1 
ATOM   7267  C CG    . PRO D 4 794  ? 164.515 147.929 157.106 1.00 50.26  ? 791  PRO A CG    1 
ATOM   7268  C CD    . PRO D 4 794  ? 163.239 148.438 156.519 1.00 50.26  ? 791  PRO A CD    1 
ATOM   7269  N N     . LYS D 4 795  ? 166.370 151.632 155.001 1.00 50.26  ? 792  LYS A N     1 
ATOM   7270  C CA    . LYS D 4 795  ? 166.855 152.280 153.790 1.00 50.26  ? 792  LYS A CA    1 
ATOM   7271  C C     . LYS D 4 795  ? 167.435 151.242 152.842 1.00 50.26  ? 792  LYS A C     1 
ATOM   7272  O O     . LYS D 4 795  ? 168.161 150.336 153.263 1.00 50.26  ? 792  LYS A O     1 
ATOM   7273  C CB    . LYS D 4 795  ? 167.900 153.343 154.130 1.00 35.84  ? 792  LYS A CB    1 
ATOM   7274  C CG    . LYS D 4 795  ? 169.166 152.813 154.778 1.00 35.84  ? 792  LYS A CG    1 
ATOM   7275  C CD    . LYS D 4 795  ? 170.158 153.932 155.037 1.00 35.84  ? 792  LYS A CD    1 
ATOM   7276  C CE    . LYS D 4 795  ? 171.452 153.396 155.619 1.00 35.84  ? 792  LYS A CE    1 
ATOM   7277  N NZ    . LYS D 4 795  ? 172.195 152.569 154.630 1.00 35.84  ? 792  LYS A NZ    1 
ATOM   7278  N N     . SER D 4 796  ? 167.091 151.358 151.568 1.00 50.26  ? 793  SER A N     1 
ATOM   7279  C CA    . SER D 4 796  ? 167.552 150.437 150.537 1.00 50.26  ? 793  SER A CA    1 
ATOM   7280  C C     . SER D 4 796  ? 168.170 151.273 149.424 1.00 50.26  ? 793  SER A C     1 
ATOM   7281  O O     . SER D 4 796  ? 167.491 151.664 148.474 1.00 50.26  ? 793  SER A O     1 
ATOM   7282  C CB    . SER D 4 796  ? 166.409 149.584 150.018 1.00 50.26  ? 793  SER A CB    1 
ATOM   7283  O OG    . SER D 4 796  ? 165.499 150.364 149.261 1.00 50.26  ? 793  SER A OG    1 
ATOM   7284  N N     . ARG D 4 797  ? 169.464 151.549 149.546 1.00 63.53  ? 794  ARG A N     1 
ATOM   7285  C CA    . ARG D 4 797  ? 170.171 152.351 148.559 1.00 63.53  ? 794  ARG A CA    1 
ATOM   7286  C C     . ARG D 4 797  ? 171.276 151.502 147.950 1.00 63.53  ? 794  ARG A C     1 
ATOM   7287  O O     . ARG D 4 797  ? 172.093 150.927 148.676 1.00 63.53  ? 794  ARG A O     1 
ATOM   7288  C CB    . ARG D 4 797  ? 170.756 153.621 149.180 1.00 63.53  ? 794  ARG A CB    1 
ATOM   7289  C CG    . ARG D 4 797  ? 171.527 154.477 148.184 1.00 63.53  ? 794  ARG A CG    1 
ATOM   7290  C CD    . ARG D 4 797  ? 170.547 155.122 147.203 1.00 63.53  ? 794  ARG A CD    1 
ATOM   7291  N NE    . ARG D 4 797  ? 170.211 154.262 146.073 1.00 63.53  ? 794  ARG A NE    1 
ATOM   7292  C CZ    . ARG D 4 797  ? 169.265 154.533 145.184 1.00 63.53  ? 794  ARG A CZ    1 
ATOM   7293  N NH1   . ARG D 4 797  ? 168.535 155.632 145.265 1.00 63.53  ? 794  ARG A NH1   1 
ATOM   7294  N NH2   . ARG D 4 797  ? 169.041 153.674 144.194 1.00 63.53  ? 794  ARG A NH2   1 
ATOM   7295  N N     . MET D 4 798  ? 171.293 151.419 146.619 1.00 74.73  ? 795  MET A N     1 
ATOM   7296  C CA    . MET D 4 798  ? 172.344 150.708 145.907 1.00 74.73  ? 795  MET A CA    1 
ATOM   7297  C C     . MET D 4 798  ? 173.181 151.605 145.008 1.00 74.73  ? 795  MET A C     1 
ATOM   7298  O O     . MET D 4 798  ? 174.315 151.239 144.685 1.00 74.73  ? 795  MET A O     1 
ATOM   7299  C CB    . MET D 4 798  ? 171.743 149.569 145.069 1.00 74.73  ? 795  MET A CB    1 
ATOM   7300  C CG    . MET D 4 798  ? 170.831 150.029 143.945 1.00 74.73  ? 795  MET A CG    1 
ATOM   7301  S SD    . MET D 4 798  ? 170.168 148.654 142.986 1.00 74.73  ? 795  MET A SD    1 
ATOM   7302  C CE    . MET D 4 798  ? 171.627 148.133 142.089 1.00 74.73  ? 795  MET A CE    1 
ATOM   7303  N N     . LYS D 4 799  ? 172.658 152.760 144.603 1.00 67.13  ? 796  LYS A N     1 
ATOM   7304  C CA    . LYS D 4 799  ? 173.419 153.716 143.802 1.00 67.13  ? 796  LYS A CA    1 
ATOM   7305  C C     . LYS D 4 799  ? 172.745 155.070 143.932 1.00 67.13  ? 796  LYS A C     1 
ATOM   7306  O O     . LYS D 4 799  ? 171.628 155.251 143.437 1.00 67.13  ? 796  LYS A O     1 
ATOM   7307  C CB    . LYS D 4 799  ? 173.489 153.280 142.338 1.00 67.13  ? 796  LYS A CB    1 
ATOM   7308  N N     . ARG D 4 800  ? 173.418 156.018 144.575 1.00 59.04  ? 797  ARG A N     1 
ATOM   7309  C CA    . ARG D 4 800  ? 172.831 157.313 144.894 1.00 59.04  ? 797  ARG A CA    1 
ATOM   7310  C C     . ARG D 4 800  ? 173.172 158.310 143.796 1.00 59.04  ? 797  ARG A C     1 
ATOM   7311  O O     . ARG D 4 800  ? 174.350 158.573 143.533 1.00 59.04  ? 797  ARG A O     1 
ATOM   7312  C CB    . ARG D 4 800  ? 173.329 157.817 146.248 1.00 59.04  ? 797  ARG A CB    1 
ATOM   7313  C CG    . ARG D 4 800  ? 172.459 158.900 146.864 1.00 59.04  ? 797  ARG A CG    1 
ATOM   7314  C CD    . ARG D 4 800  ? 172.714 159.030 148.356 1.00 59.04  ? 797  ARG A CD    1 
ATOM   7315  N NE    . ARG D 4 800  ? 172.422 157.792 149.068 1.00 59.04  ? 797  ARG A NE    1 
ATOM   7316  C CZ    . ARG D 4 800  ? 172.332 157.691 150.387 1.00 59.04  ? 797  ARG A CZ    1 
ATOM   7317  N NH1   . ARG D 4 800  ? 172.504 158.739 151.174 1.00 59.04  ? 797  ARG A NH1   1 
ATOM   7318  N NH2   . ARG D 4 800  ? 172.064 156.506 150.929 1.00 59.04  ? 797  ARG A NH2   1 
ATOM   7319  N N     . MET D 4 801  ? 172.141 158.862 143.163 1.00 53.44  ? 798  MET A N     1 
ATOM   7320  C CA    . MET D 4 801  ? 172.298 159.883 142.139 1.00 53.44  ? 798  MET A CA    1 
ATOM   7321  C C     . MET D 4 801  ? 171.402 161.059 142.491 1.00 53.44  ? 798  MET A C     1 
ATOM   7322  O O     . MET D 4 801  ? 170.255 160.873 142.909 1.00 53.44  ? 798  MET A O     1 
ATOM   7323  C CB    . MET D 4 801  ? 171.962 159.324 140.740 1.00 53.44  ? 798  MET A CB    1 
ATOM   7324  C CG    . MET D 4 801  ? 171.890 160.345 139.597 1.00 53.44  ? 798  MET A CG    1 
ATOM   7325  S SD    . MET D 4 801  ? 170.429 161.406 139.527 1.00 53.44  ? 798  MET A SD    1 
ATOM   7326  C CE    . MET D 4 801  ? 169.500 160.611 138.222 1.00 53.44  ? 798  MET A CE    1 
ATOM   7327  N N     . ALA D 4 802  ? 171.928 162.268 142.317 1.00 49.38  ? 799  ALA A N     1 
ATOM   7328  C CA    . ALA D 4 802  ? 171.197 163.475 142.663 1.00 49.38  ? 799  ALA A CA    1 
ATOM   7329  C C     . ALA D 4 802  ? 171.590 164.588 141.706 1.00 49.38  ? 799  ALA A C     1 
ATOM   7330  O O     . ALA D 4 802  ? 172.627 164.528 141.042 1.00 49.38  ? 799  ALA A O     1 
ATOM   7331  C CB    . ALA D 4 802  ? 171.460 163.897 144.112 1.00 49.38  ? 799  ALA A CB    1 
ATOM   7332  N N     . HIS D 4 803  ? 170.740 165.612 141.642 1.00 48.34  ? 800  HIS A N     1 
ATOM   7333  C CA    . HIS D 4 803  ? 170.987 166.782 140.804 1.00 48.34  ? 800  HIS A CA    1 
ATOM   7334  C C     . HIS D 4 803  ? 171.620 167.854 141.686 1.00 48.34  ? 800  HIS A C     1 
ATOM   7335  O O     . HIS D 4 803  ? 170.958 168.757 142.197 1.00 48.34  ? 800  HIS A O     1 
ATOM   7336  C CB    . HIS D 4 803  ? 169.696 167.264 140.148 1.00 48.34  ? 800  HIS A CB    1 
ATOM   7337  C CG    . HIS D 4 803  ? 169.037 166.240 139.276 1.00 48.34  ? 800  HIS A CG    1 
ATOM   7338  N ND1   . HIS D 4 803  ? 168.164 166.577 138.264 1.00 48.34  ? 800  HIS A ND1   1 
ATOM   7339  C CD2   . HIS D 4 803  ? 169.118 164.888 139.266 1.00 48.34  ? 800  HIS A CD2   1 
ATOM   7340  C CE1   . HIS D 4 803  ? 167.740 165.479 137.666 1.00 48.34  ? 800  HIS A CE1   1 
ATOM   7341  N NE2   . HIS D 4 803  ? 168.303 164.440 138.255 1.00 48.34  ? 800  HIS A NE2   1 
ATOM   7342  N N     . ARG D 4 804  ? 172.934 167.741 141.858 1.00 52.38  ? 801  ARG A N     1 
ATOM   7343  C CA    . ARG D 4 804  ? 173.661 168.597 142.781 1.00 52.38  ? 801  ARG A CA    1 
ATOM   7344  C C     . ARG D 4 804  ? 173.696 170.038 142.272 1.00 52.38  ? 801  ARG A C     1 
ATOM   7345  O O     . ARG D 4 804  ? 173.369 170.332 141.120 1.00 52.38  ? 801  ARG A O     1 
ATOM   7346  C CB    . ARG D 4 804  ? 175.080 168.070 142.988 1.00 52.38  ? 801  ARG A CB    1 
ATOM   7347  C CG    . ARG D 4 804  ? 175.133 166.654 143.532 1.00 52.38  ? 801  ARG A CG    1 
ATOM   7348  C CD    . ARG D 4 804  ? 176.441 165.972 143.172 1.00 52.38  ? 801  ARG A CD    1 
ATOM   7349  N NE    . ARG D 4 804  ? 176.426 164.553 143.508 1.00 52.38  ? 801  ARG A NE    1 
ATOM   7350  C CZ    . ARG D 4 804  ? 175.879 163.610 142.752 1.00 52.38  ? 801  ARG A CZ    1 
ATOM   7351  N NH1   . ARG D 4 804  ? 175.295 163.898 141.601 1.00 52.38  ? 801  ARG A NH1   1 
ATOM   7352  N NH2   . ARG D 4 804  ? 175.922 162.345 143.161 1.00 52.38  ? 801  ARG A NH2   1 
ATOM   7353  N N     . LEU D 4 805  ? 174.094 170.944 143.162 1.00 52.39  ? 802  LEU A N     1 
ATOM   7354  C CA    . LEU D 4 805  ? 174.182 172.354 142.811 1.00 52.39  ? 802  LEU A CA    1 
ATOM   7355  C C     . LEU D 4 805  ? 175.276 172.578 141.775 1.00 52.39  ? 802  LEU A C     1 
ATOM   7356  O O     . LEU D 4 805  ? 176.330 171.938 141.811 1.00 52.39  ? 802  LEU A O     1 
ATOM   7357  C CB    . LEU D 4 805  ? 174.460 173.198 144.054 1.00 52.39  ? 802  LEU A CB    1 
ATOM   7358  C CG    . LEU D 4 805  ? 173.382 173.251 145.138 1.00 52.39  ? 802  LEU A CG    1 
ATOM   7359  C CD1   . LEU D 4 805  ? 173.564 172.129 146.150 1.00 52.39  ? 802  LEU A CD1   1 
ATOM   7360  C CD2   . LEU D 4 805  ? 173.386 174.604 145.831 1.00 52.39  ? 802  LEU A CD2   1 
ATOM   7361  N N     . GLY D 4 806  ? 175.019 173.496 140.846 1.00 49.68  ? 803  GLY A N     1 
ATOM   7362  C CA    . GLY D 4 806  ? 175.956 173.805 139.791 1.00 49.68  ? 803  GLY A CA    1 
ATOM   7363  C C     . GLY D 4 806  ? 175.813 172.969 138.539 1.00 49.68  ? 803  GLY A C     1 
ATOM   7364  O O     . GLY D 4 806  ? 176.481 173.261 137.539 1.00 49.68  ? 803  GLY A O     1 
ATOM   7365  N N     . GLU D 4 807  ? 174.969 171.941 138.557 1.00 53.00  ? 804  GLU A N     1 
ATOM   7366  C CA    . GLU D 4 807  ? 174.711 171.139 137.375 1.00 53.00  ? 804  GLU A CA    1 
ATOM   7367  C C     . GLU D 4 807  ? 173.586 171.771 136.560 1.00 53.00  ? 804  GLU A C     1 
ATOM   7368  O O     . GLU D 4 807  ? 173.040 172.819 136.911 1.00 53.00  ? 804  GLU A O     1 
ATOM   7369  C CB    . GLU D 4 807  ? 174.376 169.700 137.767 1.00 53.00  ? 804  GLU A CB    1 
ATOM   7370  C CG    . GLU D 4 807  ? 175.265 169.138 138.863 1.00 53.00  ? 804  GLU A CG    1 
ATOM   7371  C CD    . GLU D 4 807  ? 175.363 167.627 138.818 1.00 53.00  ? 804  GLU A CD    1 
ATOM   7372  O OE1   . GLU D 4 807  ? 174.615 167.003 138.037 1.00 53.00  ? 804  GLU A OE1   1 
ATOM   7373  O OE2   . GLU D 4 807  ? 176.186 167.062 139.568 1.00 53.00  ? 804  GLU A OE2   1 
ATOM   7374  N N     . LYS D 4 808  ? 173.236 171.129 135.449 1.00 51.20  ? 805  LYS A N     1 
ATOM   7375  C CA    . LYS D 4 808  ? 172.203 171.626 134.548 1.00 51.20  ? 805  LYS A CA    1 
ATOM   7376  C C     . LYS D 4 808  ? 171.124 170.561 134.410 1.00 51.20  ? 805  LYS A C     1 
ATOM   7377  O O     . LYS D 4 808  ? 171.371 169.487 133.851 1.00 51.20  ? 805  LYS A O     1 
ATOM   7378  C CB    . LYS D 4 808  ? 172.796 171.991 133.189 1.00 51.20  ? 805  LYS A CB    1 
ATOM   7379  C CG    . LYS D 4 808  ? 173.450 173.362 133.150 1.00 51.20  ? 805  LYS A CG    1 
ATOM   7380  C CD    . LYS D 4 808  ? 173.174 174.070 131.835 1.00 51.20  ? 805  LYS A CD    1 
ATOM   7381  C CE    . LYS D 4 808  ? 174.227 175.126 131.547 1.00 51.20  ? 805  LYS A CE    1 
ATOM   7382  N NZ    . LYS D 4 808  ? 174.222 175.539 130.117 1.00 51.20  ? 805  LYS A NZ    1 
ATOM   7383  N N     . MET D 4 809  ? 169.934 170.859 134.920 1.00 50.26  ? 806  MET A N     1 
ATOM   7384  C CA    . MET D 4 809  ? 168.790 169.969 134.805 1.00 50.26  ? 806  MET A CA    1 
ATOM   7385  C C     . MET D 4 809  ? 168.082 170.200 133.478 1.00 50.26  ? 806  MET A C     1 
ATOM   7386  O O     . MET D 4 809  ? 167.932 171.340 133.031 1.00 50.26  ? 806  MET A O     1 
ATOM   7387  C CB    . MET D 4 809  ? 167.820 170.194 135.964 1.00 50.26  ? 806  MET A CB    1 
ATOM   7388  C CG    . MET D 4 809  ? 168.440 169.973 137.329 1.00 50.26  ? 806  MET A CG    1 
ATOM   7389  S SD    . MET D 4 809  ? 167.229 169.533 138.584 1.00 50.26  ? 806  MET A SD    1 
ATOM   7390  C CE    . MET D 4 809  ? 166.055 170.867 138.371 1.00 50.26  ? 806  MET A CE    1 
ATOM   7391  N N     . LEU D 4 810  ? 167.645 169.111 132.853 1.00 50.26  ? 807  LEU A N     1 
ATOM   7392  C CA    . LEU D 4 810  ? 166.981 169.162 131.559 1.00 50.26  ? 807  LEU A CA    1 
ATOM   7393  C C     . LEU D 4 810  ? 165.524 168.760 131.719 1.00 50.26  ? 807  LEU A C     1 
ATOM   7394  O O     . LEU D 4 810  ? 165.220 167.754 132.368 1.00 50.26  ? 807  LEU A O     1 
ATOM   7395  C CB    . LEU D 4 810  ? 167.670 168.247 130.546 1.00 50.26  ? 807  LEU A CB    1 
ATOM   7396  C CG    . LEU D 4 810  ? 167.145 168.365 129.116 1.00 50.26  ? 807  LEU A CG    1 
ATOM   7397  C CD1   . LEU D 4 810  ? 167.429 169.748 128.562 1.00 50.26  ? 807  LEU A CD1   1 
ATOM   7398  C CD2   . LEU D 4 810  ? 167.755 167.294 128.231 1.00 50.26  ? 807  LEU A CD2   1 
ATOM   7399  N N     . ASN D 4 811  ? 164.631 169.548 131.130 1.00 50.26  ? 808  ASN A N     1 
ATOM   7400  C CA    . ASN D 4 811  ? 163.210 169.236 131.170 1.00 50.26  ? 808  ASN A CA    1 
ATOM   7401  C C     . ASN D 4 811  ? 162.892 168.078 130.233 1.00 50.26  ? 808  ASN A C     1 
ATOM   7402  O O     . ASN D 4 811  ? 163.452 167.971 129.140 1.00 50.26  ? 808  ASN A O     1 
ATOM   7403  C CB    . ASN D 4 811  ? 162.389 170.464 130.783 1.00 50.26  ? 808  ASN A CB    1 
ATOM   7404  C CG    . ASN D 4 811  ? 162.101 171.365 131.961 1.00 50.26  ? 808  ASN A CG    1 
ATOM   7405  O OD1   . ASN D 4 811  ? 162.603 171.146 133.062 1.00 50.26  ? 808  ASN A OD1   1 
ATOM   7406  N ND2   . ASN D 4 811  ? 161.285 172.387 131.737 1.00 50.26  ? 808  ASN A ND2   1 
ATOM   7407  N N     . LYS D 4 812  ? 161.982 167.208 130.666 1.00 50.26  ? 809  LYS A N     1 
ATOM   7408  C CA    . LYS D 4 812  ? 161.534 166.088 129.848 1.00 50.26  ? 809  LYS A CA    1 
ATOM   7409  C C     . LYS D 4 812  ? 160.452 166.484 128.855 1.00 50.26  ? 809  LYS A C     1 
ATOM   7410  O O     . LYS D 4 812  ? 159.864 165.605 128.217 1.00 50.26  ? 809  LYS A O     1 
ATOM   7411  C CB    . LYS D 4 812  ? 161.028 164.950 130.736 1.00 50.26  ? 809  LYS A CB    1 
ATOM   7412  C CG    . LYS D 4 812  ? 162.109 164.276 131.560 1.00 50.26  ? 809  LYS A CG    1 
ATOM   7413  C CD    . LYS D 4 812  ? 161.539 163.144 132.398 1.00 50.26  ? 809  LYS A CD    1 
ATOM   7414  C CE    . LYS D 4 812  ? 162.607 162.509 133.271 1.00 50.26  ? 809  LYS A CE    1 
ATOM   7415  N NZ    . LYS D 4 812  ? 162.059 161.409 134.109 1.00 50.26  ? 809  LYS A NZ    1 
ATOM   7416  N N     . LYS D 4 813  ? 160.174 167.777 128.719 1.00 50.26  ? 810  LYS A N     1 
ATOM   7417  C CA    . LYS D 4 813  ? 159.215 168.287 127.753 1.00 50.26  ? 810  LYS A CA    1 
ATOM   7418  C C     . LYS D 4 813  ? 159.889 169.347 126.897 1.00 50.26  ? 810  LYS A C     1 
ATOM   7419  O O     . LYS D 4 813  ? 160.865 169.979 127.308 1.00 50.26  ? 810  LYS A O     1 
ATOM   7420  C CB    . LYS D 4 813  ? 157.982 168.891 128.435 1.00 46.81  ? 810  LYS A CB    1 
ATOM   7421  C CG    . LYS D 4 813  ? 157.311 167.993 129.454 1.00 46.81  ? 810  LYS A CG    1 
ATOM   7422  C CD    . LYS D 4 813  ? 156.245 168.764 130.214 1.00 46.81  ? 810  LYS A CD    1 
ATOM   7423  C CE    . LYS D 4 813  ? 155.043 167.898 130.528 1.00 46.81  ? 810  LYS A CE    1 
ATOM   7424  N NZ    . LYS D 4 813  ? 153.803 168.712 130.618 1.00 46.81  ? 810  LYS A NZ    1 
ATOM   7425  N N     . LEU D 4 814  ? 159.356 169.538 125.696 1.00 52.85  ? 811  LEU A N     1 
ATOM   7426  C CA    . LEU D 4 814  ? 159.857 170.576 124.807 1.00 52.85  ? 811  LEU A CA    1 
ATOM   7427  C C     . LEU D 4 814  ? 159.295 171.922 125.267 1.00 52.85  ? 811  LEU A C     1 
ATOM   7428  O O     . LEU D 4 814  ? 158.672 172.029 126.327 1.00 52.85  ? 811  LEU A O     1 
ATOM   7429  C CB    . LEU D 4 814  ? 159.503 170.254 123.356 1.00 52.85  ? 811  LEU A CB    1 
ATOM   7430  C CG    . LEU D 4 814  ? 160.393 169.263 122.592 1.00 52.85  ? 811  LEU A CG    1 
ATOM   7431  C CD1   . LEU D 4 814  ? 161.822 169.765 122.511 1.00 52.85  ? 811  LEU A CD1   1 
ATOM   7432  C CD2   . LEU D 4 814  ? 160.352 167.859 123.170 1.00 52.85  ? 811  LEU A CD2   1 
ATOM   7433  N N     . LYS D 4 815  ? 159.512 172.977 124.477 1.00 56.26  ? 812  LYS A N     1 
ATOM   7434  C CA    . LYS D 4 815  ? 159.041 174.297 124.887 1.00 56.26  ? 812  LYS A CA    1 
ATOM   7435  C C     . LYS D 4 815  ? 157.519 174.381 124.890 1.00 56.26  ? 812  LYS A C     1 
ATOM   7436  O O     . LYS D 4 815  ? 156.949 175.205 125.614 1.00 56.26  ? 812  LYS A O     1 
ATOM   7437  C CB    . LYS D 4 815  ? 159.626 175.380 123.982 1.00 56.26  ? 812  LYS A CB    1 
ATOM   7438  C CG    . LYS D 4 815  ? 159.439 175.130 122.500 1.00 56.26  ? 812  LYS A CG    1 
ATOM   7439  C CD    . LYS D 4 815  ? 160.083 176.235 121.677 1.00 56.26  ? 812  LYS A CD    1 
ATOM   7440  C CE    . LYS D 4 815  ? 161.592 176.249 121.853 1.00 56.26  ? 812  LYS A CE    1 
ATOM   7441  N NZ    . LYS D 4 815  ? 162.269 177.007 120.765 1.00 56.26  ? 812  LYS A NZ    1 
ATOM   7442  N N     . ASP D 4 816  ? 156.847 173.545 124.097 1.00 54.84  ? 813  ASP A N     1 
ATOM   7443  C CA    . ASP D 4 816  ? 155.389 173.537 124.079 1.00 54.84  ? 813  ASP A CA    1 
ATOM   7444  C C     . ASP D 4 816  ? 154.790 172.940 125.345 1.00 54.84  ? 813  ASP A C     1 
ATOM   7445  O O     . ASP D 4 816  ? 153.571 173.028 125.530 1.00 54.84  ? 813  ASP A O     1 
ATOM   7446  C CB    . ASP D 4 816  ? 154.883 172.769 122.859 1.00 54.84  ? 813  ASP A CB    1 
ATOM   7447  C CG    . ASP D 4 816  ? 155.437 171.363 122.787 1.00 54.84  ? 813  ASP A CG    1 
ATOM   7448  O OD1   . ASP D 4 816  ? 156.412 171.072 123.509 1.00 54.84  ? 813  ASP A OD1   1 
ATOM   7449  O OD2   . ASP D 4 816  ? 154.898 170.548 122.011 1.00 54.84  ? 813  ASP A OD2   1 
ATOM   7450  N N     . GLN D 4 817  ? 155.608 172.322 126.198 1.00 52.30  ? 814  GLN A N     1 
ATOM   7451  C CA    . GLN D 4 817  ? 155.222 171.749 127.485 1.00 52.30  ? 814  GLN A CA    1 
ATOM   7452  C C     . GLN D 4 817  ? 154.282 170.558 127.356 1.00 52.30  ? 814  GLN A C     1 
ATOM   7453  O O     . GLN D 4 817  ? 153.728 170.111 128.366 1.00 52.30  ? 814  GLN A O     1 
ATOM   7454  C CB    . GLN D 4 817  ? 154.582 172.795 128.407 1.00 52.30  ? 814  GLN A CB    1 
ATOM   7455  C CG    . GLN D 4 817  ? 155.418 174.048 128.606 1.00 52.30  ? 814  GLN A CG    1 
ATOM   7456  C CD    . GLN D 4 817  ? 155.208 174.674 129.970 1.00 52.30  ? 814  GLN A CD    1 
ATOM   7457  O OE1   . GLN D 4 817  ? 155.428 174.036 130.999 1.00 52.30  ? 814  GLN A OE1   1 
ATOM   7458  N NE2   . GLN D 4 817  ? 154.780 175.931 129.984 1.00 52.30  ? 814  GLN A NE2   1 
ATOM   7459  N N     . LYS D 4 818  ? 154.092 170.020 126.151 1.00 50.26  ? 815  LYS A N     1 
ATOM   7460  C CA    . LYS D 4 818  ? 153.179 168.907 125.945 1.00 50.26  ? 815  LYS A CA    1 
ATOM   7461  C C     . LYS D 4 818  ? 153.807 167.701 125.264 1.00 50.26  ? 815  LYS A C     1 
ATOM   7462  O O     . LYS D 4 818  ? 153.274 166.594 125.402 1.00 50.26  ? 815  LYS A O     1 
ATOM   7463  C CB    . LYS D 4 818  ? 151.961 169.357 125.123 1.00 48.20  ? 815  LYS A CB    1 
ATOM   7464  C CG    . LYS D 4 818  ? 150.736 169.687 125.958 1.00 48.20  ? 815  LYS A CG    1 
ATOM   7465  C CD    . LYS D 4 818  ? 149.607 170.226 125.096 1.00 48.20  ? 815  LYS A CD    1 
ATOM   7466  C CE    . LYS D 4 818  ? 149.304 169.290 123.939 1.00 48.20  ? 815  LYS A CE    1 
ATOM   7467  N NZ    . LYS D 4 818  ? 148.600 168.060 124.392 1.00 48.20  ? 815  LYS A NZ    1 
ATOM   7468  N N     . THR D 4 819  ? 154.911 167.871 124.543 1.00 50.26  ? 816  THR A N     1 
ATOM   7469  C CA    . THR D 4 819  ? 155.525 166.767 123.815 1.00 50.26  ? 816  THR A CA    1 
ATOM   7470  C C     . THR D 4 819  ? 156.740 166.263 124.579 1.00 50.26  ? 816  THR A C     1 
ATOM   7471  O O     . THR D 4 819  ? 157.754 166.973 124.653 1.00 50.26  ? 816  THR A O     1 
ATOM   7472  C CB    . THR D 4 819  ? 155.928 167.206 122.407 1.00 50.26  ? 816  THR A CB    1 
ATOM   7473  O OG1   . THR D 4 819  ? 156.614 168.462 122.475 1.00 50.26  ? 816  THR A OG1   1 
ATOM   7474  C CG2   . THR D 4 819  ? 154.700 167.359 121.525 1.00 50.26  ? 816  THR A CG2   1 
ATOM   7475  N N     . PRO D 4 820  ? 156.689 165.074 125.172 1.00 50.26  ? 817  PRO A N     1 
ATOM   7476  C CA    . PRO D 4 820  ? 157.869 164.547 125.863 1.00 50.26  ? 817  PRO A CA    1 
ATOM   7477  C C     . PRO D 4 820  ? 158.980 164.181 124.892 1.00 50.26  ? 817  PRO A C     1 
ATOM   7478  O O     . PRO D 4 820  ? 158.739 163.808 123.742 1.00 50.26  ? 817  PRO A O     1 
ATOM   7479  C CB    . PRO D 4 820  ? 157.332 163.306 126.585 1.00 50.26  ? 817  PRO A CB    1 
ATOM   7480  C CG    . PRO D 4 820  ? 156.123 162.915 125.808 1.00 50.26  ? 817  PRO A CG    1 
ATOM   7481  C CD    . PRO D 4 820  ? 155.518 164.199 125.336 1.00 50.26  ? 817  PRO A CD    1 
ATOM   7482  N N     . ILE D 4 821  ? 160.212 164.298 125.376 1.00 50.26  ? 818  ILE A N     1 
ATOM   7483  C CA    . ILE D 4 821  ? 161.400 163.905 124.623 1.00 50.26  ? 818  ILE A CA    1 
ATOM   7484  C C     . ILE D 4 821  ? 161.475 162.383 124.607 1.00 50.26  ? 818  ILE A C     1 
ATOM   7485  O O     . ILE D 4 821  ? 161.057 161.739 125.580 1.00 50.26  ? 818  ILE A O     1 
ATOM   7486  C CB    . ILE D 4 821  ? 162.670 164.516 125.235 1.00 50.26  ? 818  ILE A CB    1 
ATOM   7487  C CG1   . ILE D 4 821  ? 162.502 166.020 125.429 1.00 50.26  ? 818  ILE A CG1   1 
ATOM   7488  C CG2   . ILE D 4 821  ? 163.886 164.253 124.366 1.00 50.26  ? 818  ILE A CG2   1 
ATOM   7489  C CD1   . ILE D 4 821  ? 163.609 166.637 126.236 1.00 50.26  ? 818  ILE A CD1   1 
ATOM   7490  N N     . PRO D 4 822  ? 161.972 161.765 123.536 1.00 50.97  ? 819  PRO A N     1 
ATOM   7491  C CA    . PRO D 4 822  ? 162.273 160.331 123.596 1.00 50.97  ? 819  PRO A CA    1 
ATOM   7492  C C     . PRO D 4 822  ? 163.277 160.039 124.702 1.00 50.97  ? 819  PRO A C     1 
ATOM   7493  O O     . PRO D 4 822  ? 164.173 160.839 124.978 1.00 50.97  ? 819  PRO A O     1 
ATOM   7494  C CB    . PRO D 4 822  ? 162.851 160.035 122.210 1.00 50.97  ? 819  PRO A CB    1 
ATOM   7495  C CG    . PRO D 4 822  ? 162.204 161.043 121.328 1.00 50.97  ? 819  PRO A CG    1 
ATOM   7496  C CD    . PRO D 4 822  ? 162.055 162.287 122.160 1.00 50.97  ? 819  PRO A CD    1 
ATOM   7497  N N     . ASP D 4 823  ? 163.111 158.878 125.341 1.00 57.88  ? 820  ASP A N     1 
ATOM   7498  C CA    . ASP D 4 823  ? 163.865 158.579 126.556 1.00 57.88  ? 820  ASP A CA    1 
ATOM   7499  C C     . ASP D 4 823  ? 165.367 158.568 126.297 1.00 57.88  ? 820  ASP A C     1 
ATOM   7500  O O     . ASP D 4 823  ? 166.135 159.225 127.011 1.00 57.88  ? 820  ASP A O     1 
ATOM   7501  C CB    . ASP D 4 823  ? 163.407 157.241 127.134 1.00 57.88  ? 820  ASP A CB    1 
ATOM   7502  C CG    . ASP D 4 823  ? 162.000 157.300 127.695 1.00 57.88  ? 820  ASP A CG    1 
ATOM   7503  O OD1   . ASP D 4 823  ? 161.589 158.384 128.159 1.00 57.88  ? 820  ASP A OD1   1 
ATOM   7504  O OD2   . ASP D 4 823  ? 161.304 156.263 127.672 1.00 57.88  ? 820  ASP A OD2   1 
ATOM   7505  N N     . THR D 4 824  ? 165.807 157.825 125.280 1.00 56.98  ? 821  THR A N     1 
ATOM   7506  C CA    . THR D 4 824  ? 167.236 157.764 124.987 1.00 56.98  ? 821  THR A CA    1 
ATOM   7507  C C     . THR D 4 824  ? 167.769 159.123 124.549 1.00 56.98  ? 821  THR A C     1 
ATOM   7508  O O     . THR D 4 824  ? 168.862 159.532 124.961 1.00 56.98  ? 821  THR A O     1 
ATOM   7509  C CB    . THR D 4 824  ? 167.517 156.694 123.928 1.00 56.98  ? 821  THR A CB    1 
ATOM   7510  O OG1   . THR D 4 824  ? 168.914 156.690 123.605 1.00 56.98  ? 821  THR A OG1   1 
ATOM   7511  C CG2   . THR D 4 824  ? 166.693 156.924 122.665 1.00 56.98  ? 821  THR A CG2   1 
ATOM   7512  N N     . LEU D 4 825  ? 167.003 159.845 123.729 1.00 57.77  ? 822  LEU A N     1 
ATOM   7513  C CA    . LEU D 4 825  ? 167.423 161.177 123.314 1.00 57.77  ? 822  LEU A CA    1 
ATOM   7514  C C     . LEU D 4 825  ? 167.464 162.132 124.498 1.00 57.77  ? 822  LEU A C     1 
ATOM   7515  O O     . LEU D 4 825  ? 168.366 162.971 124.594 1.00 57.77  ? 822  LEU A O     1 
ATOM   7516  C CB    . LEU D 4 825  ? 166.496 161.705 122.221 1.00 57.77  ? 822  LEU A CB    1 
ATOM   7517  C CG    . LEU D 4 825  ? 166.561 160.928 120.906 1.00 57.77  ? 822  LEU A CG    1 
ATOM   7518  C CD1   . LEU D 4 825  ? 165.515 161.429 119.924 1.00 57.77  ? 822  LEU A CD1   1 
ATOM   7519  C CD2   . LEU D 4 825  ? 167.956 161.014 120.308 1.00 57.77  ? 822  LEU A CD2   1 
ATOM   7520  N N     . TYR D 4 826  ? 166.495 162.021 125.411 1.00 53.35  ? 823  TYR A N     1 
ATOM   7521  C CA    . TYR D 4 826  ? 166.511 162.864 126.602 1.00 53.35  ? 823  TYR A CA    1 
ATOM   7522  C C     . TYR D 4 826  ? 167.737 162.587 127.458 1.00 53.35  ? 823  TYR A C     1 
ATOM   7523  O O     . TYR D 4 826  ? 168.382 163.520 127.949 1.00 53.35  ? 823  TYR A O     1 
ATOM   7524  C CB    . TYR D 4 826  ? 165.240 162.657 127.423 1.00 53.35  ? 823  TYR A CB    1 
ATOM   7525  C CG    . TYR D 4 826  ? 165.375 163.118 128.858 1.00 53.35  ? 823  TYR A CG    1 
ATOM   7526  C CD1   . TYR D 4 826  ? 165.524 164.463 129.165 1.00 53.35  ? 823  TYR A CD1   1 
ATOM   7527  C CD2   . TYR D 4 826  ? 165.363 162.206 129.904 1.00 53.35  ? 823  TYR A CD2   1 
ATOM   7528  C CE1   . TYR D 4 826  ? 165.652 164.887 130.473 1.00 53.35  ? 823  TYR A CE1   1 
ATOM   7529  C CE2   . TYR D 4 826  ? 165.491 162.621 131.214 1.00 53.35  ? 823  TYR A CE2   1 
ATOM   7530  C CZ    . TYR D 4 826  ? 165.634 163.962 131.493 1.00 53.35  ? 823  TYR A CZ    1 
ATOM   7531  O OH    . TYR D 4 826  ? 165.761 164.378 132.798 1.00 53.35  ? 823  TYR A OH    1 
ATOM   7532  N N     . GLN D 4 827  ? 168.073 161.310 127.656 1.00 57.65  ? 824  GLN A N     1 
ATOM   7533  C CA    . GLN D 4 827  ? 169.245 160.984 128.462 1.00 57.65  ? 824  GLN A CA    1 
ATOM   7534  C C     . GLN D 4 827  ? 170.522 161.483 127.798 1.00 57.65  ? 824  GLN A C     1 
ATOM   7535  O O     . GLN D 4 827  ? 171.403 162.035 128.468 1.00 57.65  ? 824  GLN A O     1 
ATOM   7536  C CB    . GLN D 4 827  ? 169.314 159.476 128.707 1.00 57.65  ? 824  GLN A CB    1 
ATOM   7537  C CG    . GLN D 4 827  ? 170.387 159.047 129.701 1.00 57.65  ? 824  GLN A CG    1 
ATOM   7538  C CD    . GLN D 4 827  ? 171.746 158.854 129.060 1.00 57.65  ? 824  GLN A CD    1 
ATOM   7539  O OE1   . GLN D 4 827  ? 171.848 158.508 127.883 1.00 57.65  ? 824  GLN A OE1   1 
ATOM   7540  N NE2   . GLN D 4 827  ? 172.802 159.078 129.834 1.00 57.65  ? 824  GLN A NE2   1 
ATOM   7541  N N     . GLU D 4 828  ? 170.636 161.304 126.479 1.00 63.05  ? 825  GLU A N     1 
ATOM   7542  C CA    . GLU D 4 828  ? 171.818 161.784 125.772 1.00 63.05  ? 825  GLU A CA    1 
ATOM   7543  C C     . GLU D 4 828  ? 171.937 163.300 125.860 1.00 63.05  ? 825  GLU A C     1 
ATOM   7544  O O     . GLU D 4 828  ? 173.030 163.832 126.089 1.00 63.05  ? 825  GLU A O     1 
ATOM   7545  C CB    . GLU D 4 828  ? 171.774 161.334 124.313 1.00 63.05  ? 825  GLU A CB    1 
ATOM   7546  C CG    . GLU D 4 828  ? 173.012 161.702 123.517 1.00 63.05  ? 825  GLU A CG    1 
ATOM   7547  C CD    . GLU D 4 828  ? 172.870 161.384 122.044 1.00 63.05  ? 825  GLU A CD    1 
ATOM   7548  O OE1   . GLU D 4 828  ? 171.851 160.770 121.664 1.00 63.05  ? 825  GLU A OE1   1 
ATOM   7549  O OE2   . GLU D 4 828  ? 173.776 161.749 121.265 1.00 63.05  ? 825  GLU A OE2   1 
ATOM   7550  N N     . LEU D 4 829  ? 170.823 164.015 125.683 1.00 61.00  ? 826  LEU A N     1 
ATOM   7551  C CA    . LEU D 4 829  ? 170.856 165.471 125.763 1.00 61.00  ? 826  LEU A CA    1 
ATOM   7552  C C     . LEU D 4 829  ? 171.201 165.940 127.170 1.00 61.00  ? 826  LEU A C     1 
ATOM   7553  O O     . LEU D 4 829  ? 171.956 166.903 127.338 1.00 61.00  ? 826  LEU A O     1 
ATOM   7554  C CB    . LEU D 4 829  ? 169.516 166.049 125.313 1.00 61.00  ? 826  LEU A CB    1 
ATOM   7555  C CG    . LEU D 4 829  ? 169.282 166.100 123.803 1.00 61.00  ? 826  LEU A CG    1 
ATOM   7556  C CD1   . LEU D 4 829  ? 167.798 166.201 123.497 1.00 61.00  ? 826  LEU A CD1   1 
ATOM   7557  C CD2   . LEU D 4 829  ? 170.038 167.263 123.185 1.00 61.00  ? 826  LEU A CD2   1 
ATOM   7558  N N     . TYR D 4 830  ? 170.657 165.276 128.192 1.00 58.44  ? 827  TYR A N     1 
ATOM   7559  C CA    . TYR D 4 830  ? 170.988 165.635 129.567 1.00 58.44  ? 827  TYR A CA    1 
ATOM   7560  C C     . TYR D 4 830  ? 172.466 165.412 129.849 1.00 58.44  ? 827  TYR A C     1 
ATOM   7561  O O     . TYR D 4 830  ? 173.108 166.226 130.523 1.00 58.44  ? 827  TYR A O     1 
ATOM   7562  C CB    . TYR D 4 830  ? 170.125 164.833 130.541 1.00 58.44  ? 827  TYR A CB    1 
ATOM   7563  C CG    . TYR D 4 830  ? 170.590 164.896 131.977 1.00 58.44  ? 827  TYR A CG    1 
ATOM   7564  C CD1   . TYR D 4 830  ? 170.287 165.988 132.777 1.00 58.44  ? 827  TYR A CD1   1 
ATOM   7565  C CD2   . TYR D 4 830  ? 171.325 163.859 132.536 1.00 58.44  ? 827  TYR A CD2   1 
ATOM   7566  C CE1   . TYR D 4 830  ? 170.708 166.050 134.090 1.00 58.44  ? 827  TYR A CE1   1 
ATOM   7567  C CE2   . TYR D 4 830  ? 171.750 163.913 133.848 1.00 58.44  ? 827  TYR A CE2   1 
ATOM   7568  C CZ    . TYR D 4 830  ? 171.439 165.010 134.621 1.00 58.44  ? 827  TYR A CZ    1 
ATOM   7569  O OH    . TYR D 4 830  ? 171.859 165.068 135.929 1.00 58.44  ? 827  TYR A OH    1 
ATOM   7570  N N     . ASP D 4 831  ? 173.025 164.309 129.346 1.00 63.47  ? 828  ASP A N     1 
ATOM   7571  C CA    . ASP D 4 831  ? 174.456 164.075 129.503 1.00 63.47  ? 828  ASP A CA    1 
ATOM   7572  C C     . ASP D 4 831  ? 175.272 165.143 128.786 1.00 63.47  ? 828  ASP A C     1 
ATOM   7573  O O     . ASP D 4 831  ? 176.291 165.610 129.306 1.00 63.47  ? 828  ASP A O     1 
ATOM   7574  C CB    . ASP D 4 831  ? 174.820 162.684 128.986 1.00 63.47  ? 828  ASP A CB    1 
ATOM   7575  C CG    . ASP D 4 831  ? 174.771 161.626 130.071 1.00 63.47  ? 828  ASP A CG    1 
ATOM   7576  O OD1   . ASP D 4 831  ? 174.701 161.996 131.261 1.00 63.47  ? 828  ASP A OD1   1 
ATOM   7577  O OD2   . ASP D 4 831  ? 174.802 160.425 129.732 1.00 63.47  ? 828  ASP A OD2   1 
ATOM   7578  N N     . TYR D 4 832  ? 174.841 165.539 127.587 1.00 67.34  ? 829  TYR A N     1 
ATOM   7579  C CA    . TYR D 4 832  ? 175.605 166.511 126.810 1.00 67.34  ? 829  TYR A CA    1 
ATOM   7580  C C     . TYR D 4 832  ? 175.566 167.897 127.442 1.00 67.34  ? 829  TYR A C     1 
ATOM   7581  O O     . TYR D 4 832  ? 176.574 168.614 127.433 1.00 67.34  ? 829  TYR A O     1 
ATOM   7582  C CB    . TYR D 4 832  ? 175.081 166.568 125.376 1.00 67.34  ? 829  TYR A CB    1 
ATOM   7583  C CG    . TYR D 4 832  ? 175.550 167.785 124.611 1.00 67.34  ? 829  TYR A CG    1 
ATOM   7584  C CD1   . TYR D 4 832  ? 176.819 167.829 124.051 1.00 67.34  ? 829  TYR A CD1   1 
ATOM   7585  C CD2   . TYR D 4 832  ? 174.727 168.893 124.455 1.00 67.34  ? 829  TYR A CD2   1 
ATOM   7586  C CE1   . TYR D 4 832  ? 177.254 168.939 123.353 1.00 67.34  ? 829  TYR A CE1   1 
ATOM   7587  C CE2   . TYR D 4 832  ? 175.154 170.007 123.760 1.00 67.34  ? 829  TYR A CE2   1 
ATOM   7588  C CZ    . TYR D 4 832  ? 176.417 170.025 123.210 1.00 67.34  ? 829  TYR A CZ    1 
ATOM   7589  O OH    . TYR D 4 832  ? 176.844 171.134 122.517 1.00 67.34  ? 829  TYR A OH    1 
ATOM   7590  N N     . VAL D 4 833  ? 174.412 168.299 127.980 1.00 62.31  ? 830  VAL A N     1 
ATOM   7591  C CA    . VAL D 4 833  ? 174.259 169.663 128.480 1.00 62.31  ? 830  VAL A CA    1 
ATOM   7592  C C     . VAL D 4 833  ? 175.216 169.922 129.638 1.00 62.31  ? 830  VAL A C     1 
ATOM   7593  O O     . VAL D 4 833  ? 175.790 171.012 129.757 1.00 62.31  ? 830  VAL A O     1 
ATOM   7594  C CB    . VAL D 4 833  ? 172.793 169.927 128.876 1.00 62.31  ? 830  VAL A CB    1 
ATOM   7595  C CG1   . VAL D 4 833  ? 172.676 171.212 129.667 1.00 62.31  ? 830  VAL A CG1   1 
ATOM   7596  C CG2   . VAL D 4 833  ? 171.922 170.006 127.636 1.00 62.31  ? 830  VAL A CG2   1 
ATOM   7597  N N     . ASN D 4 834  ? 175.422 168.924 130.494 1.00 62.34  ? 831  ASN A N     1 
ATOM   7598  C CA    . ASN D 4 834  ? 176.363 169.045 131.600 1.00 62.34  ? 831  ASN A CA    1 
ATOM   7599  C C     . ASN D 4 834  ? 177.817 168.930 131.159 1.00 62.34  ? 831  ASN A C     1 
ATOM   7600  O O     . ASN D 4 834  ? 178.704 168.891 132.019 1.00 62.34  ? 831  ASN A O     1 
ATOM   7601  C CB    . ASN D 4 834  ? 176.061 167.988 132.664 1.00 62.34  ? 831  ASN A CB    1 
ATOM   7602  C CG    . ASN D 4 834  ? 174.613 168.000 133.100 1.00 62.34  ? 831  ASN A CG    1 
ATOM   7603  O OD1   . ASN D 4 834  ? 173.824 168.825 132.644 1.00 62.34  ? 831  ASN A OD1   1 
ATOM   7604  N ND2   . ASN D 4 834  ? 174.255 167.081 133.989 1.00 62.34  ? 831  ASN A ND2   1 
ATOM   7605  N N     . HIS D 4 835  ? 178.074 168.876 129.850 1.00 65.69  ? 832  HIS A N     1 
ATOM   7606  C CA    . HIS D 4 835  ? 179.429 168.790 129.304 1.00 65.69  ? 832  HIS A CA    1 
ATOM   7607  C C     . HIS D 4 835  ? 180.177 167.577 129.852 1.00 65.69  ? 832  HIS A C     1 
ATOM   7608  O O     . HIS D 4 835  ? 181.371 167.642 130.151 1.00 65.69  ? 832  HIS A O     1 
ATOM   7609  C CB    . HIS D 4 835  ? 180.213 170.078 129.566 1.00 65.69  ? 832  HIS A CB    1 
ATOM   7610  C CG    . HIS D 4 835  ? 179.390 171.321 129.433 1.00 65.69  ? 832  HIS A CG    1 
ATOM   7611  N ND1   . HIS D 4 835  ? 178.736 171.660 128.268 1.00 65.69  ? 832  HIS A ND1   1 
ATOM   7612  C CD2   . HIS D 4 835  ? 179.113 172.307 130.319 1.00 65.69  ? 832  HIS A CD2   1 
ATOM   7613  C CE1   . HIS D 4 835  ? 178.093 172.800 128.442 1.00 65.69  ? 832  HIS A CE1   1 
ATOM   7614  N NE2   . HIS D 4 835  ? 178.305 173.214 129.678 1.00 65.69  ? 832  HIS A NE2   1 
ATOM   7615  N N     . ARG D 4 836  ? 179.465 166.458 129.986 1.00 68.70  ? 833  ARG A N     1 
ATOM   7616  C CA    . ARG D 4 836  ? 180.055 165.212 130.460 1.00 68.70  ? 833  ARG A CA    1 
ATOM   7617  C C     . ARG D 4 836  ? 179.825 164.055 129.496 1.00 68.70  ? 833  ARG A C     1 
ATOM   7618  O O     . ARG D 4 836  ? 179.976 162.893 129.892 1.00 68.70  ? 833  ARG A O     1 
ATOM   7619  C CB    . ARG D 4 836  ? 179.505 164.855 131.844 1.00 68.70  ? 833  ARG A CB    1 
ATOM   7620  C CG    . ARG D 4 836  ? 178.015 164.564 131.863 1.00 68.70  ? 833  ARG A CG    1 
ATOM   7621  C CD    . ARG D 4 836  ? 177.540 164.207 133.260 1.00 68.70  ? 833  ARG A CD    1 
ATOM   7622  N NE    . ARG D 4 836  ? 177.580 165.352 134.162 1.00 68.70  ? 833  ARG A NE    1 
ATOM   7623  C CZ    . ARG D 4 836  ? 176.974 165.398 135.340 1.00 68.70  ? 833  ARG A CZ    1 
ATOM   7624  N NH1   . ARG D 4 836  ? 176.268 164.376 135.795 1.00 68.70  ? 833  ARG A NH1   1 
ATOM   7625  N NH2   . ARG D 4 836  ? 177.081 166.497 136.081 1.00 68.70  ? 833  ARG A NH2   1 
ATOM   7626  N N     . LEU D 4 837  ? 179.468 164.337 128.246 1.00 79.18  ? 834  LEU A N     1 
ATOM   7627  C CA    . LEU D 4 837  ? 179.200 163.296 127.261 1.00 79.18  ? 834  LEU A CA    1 
ATOM   7628  C C     . LEU D 4 837  ? 180.401 163.155 126.333 1.00 79.18  ? 834  LEU A C     1 
ATOM   7629  O O     . LEU D 4 837  ? 180.814 164.127 125.692 1.00 79.18  ? 834  LEU A O     1 
ATOM   7630  C CB    . LEU D 4 837  ? 177.937 163.622 126.465 1.00 79.18  ? 834  LEU A CB    1 
ATOM   7631  C CG    . LEU D 4 837  ? 177.534 162.618 125.384 1.00 79.18  ? 834  LEU A CG    1 
ATOM   7632  C CD1   . LEU D 4 837  ? 177.359 161.229 125.978 1.00 79.18  ? 834  LEU A CD1   1 
ATOM   7633  C CD2   . LEU D 4 837  ? 176.263 163.070 124.681 1.00 79.18  ? 834  LEU A CD2   1 
ATOM   7634  N N     . SER D 4 838  ? 180.958 161.943 126.265 1.00 85.74  ? 835  SER A N     1 
ATOM   7635  C CA    . SER D 4 838  ? 182.110 161.709 125.400 1.00 85.74  ? 835  SER A CA    1 
ATOM   7636  C C     . SER D 4 838  ? 181.704 161.658 123.933 1.00 85.74  ? 835  SER A C     1 
ATOM   7637  O O     . SER D 4 838  ? 182.391 162.222 123.073 1.00 85.74  ? 835  SER A O     1 
ATOM   7638  C CB    . SER D 4 838  ? 182.817 160.416 125.806 1.00 85.74  ? 835  SER A CB    1 
ATOM   7639  O OG    . SER D 4 838  ? 182.042 159.281 125.461 1.00 85.74  ? 835  SER A OG    1 
ATOM   7640  N N     . HIS D 4 839  ? 180.596 160.989 123.629 1.00 93.99  ? 836  HIS A N     1 
ATOM   7641  C CA    . HIS D 4 839  ? 180.141 160.858 122.255 1.00 93.99  ? 836  HIS A CA    1 
ATOM   7642  C C     . HIS D 4 839  ? 179.575 162.179 121.743 1.00 93.99  ? 836  HIS A C     1 
ATOM   7643  O O     . HIS D 4 839  ? 179.064 163.006 122.503 1.00 93.99  ? 836  HIS A O     1 
ATOM   7644  C CB    . HIS D 4 839  ? 179.080 159.764 122.139 1.00 93.99  ? 836  HIS A CB    1 
ATOM   7645  C CG    . HIS D 4 839  ? 179.592 158.391 122.444 1.00 93.99  ? 836  HIS A CG    1 
ATOM   7646  N ND1   . HIS D 4 839  ? 180.384 157.681 121.568 1.00 93.99  ? 836  HIS A ND1   1 
ATOM   7647  C CD2   . HIS D 4 839  ? 179.424 157.597 123.528 1.00 93.99  ? 836  HIS A CD2   1 
ATOM   7648  C CE1   . HIS D 4 839  ? 180.683 156.509 122.099 1.00 93.99  ? 836  HIS A CE1   1 
ATOM   7649  N NE2   . HIS D 4 839  ? 180.112 156.433 123.288 1.00 93.99  ? 836  HIS A NE2   1 
ATOM   7650  N N     . ASP D 4 840  ? 179.677 162.371 120.432 1.00 89.38  ? 837  ASP A N     1 
ATOM   7651  C CA    . ASP D 4 840  ? 179.079 163.533 119.798 1.00 89.38  ? 837  ASP A CA    1 
ATOM   7652  C C     . ASP D 4 840  ? 177.572 163.344 119.672 1.00 89.38  ? 837  ASP A C     1 
ATOM   7653  O O     . ASP D 4 840  ? 177.068 162.219 119.612 1.00 89.38  ? 837  ASP A O     1 
ATOM   7654  C CB    . ASP D 4 840  ? 179.695 163.776 118.420 1.00 89.38  ? 837  ASP A CB    1 
ATOM   7655  C CG    . ASP D 4 840  ? 179.265 165.098 117.816 1.00 89.38  ? 837  ASP A CG    1 
ATOM   7656  O OD1   . ASP D 4 840  ? 179.771 166.150 118.262 1.00 89.38  ? 837  ASP A OD1   1 
ATOM   7657  O OD2   . ASP D 4 840  ? 178.419 165.087 116.898 1.00 89.38  ? 837  ASP A OD2   1 
ATOM   7658  N N     . LEU D 4 841  ? 176.854 164.463 119.642 1.00 80.61  ? 838  LEU A N     1 
ATOM   7659  C CA    . LEU D 4 841  ? 175.403 164.415 119.542 1.00 80.61  ? 838  LEU A CA    1 
ATOM   7660  C C     . LEU D 4 841  ? 174.972 163.802 118.216 1.00 80.61  ? 838  LEU A C     1 
ATOM   7661  O O     . LEU D 4 841  ? 175.557 164.074 117.164 1.00 80.61  ? 838  LEU A O     1 
ATOM   7662  C CB    . LEU D 4 841  ? 174.820 165.820 119.681 1.00 80.61  ? 838  LEU A CB    1 
ATOM   7663  C CG    . LEU D 4 841  ? 174.805 166.393 121.097 1.00 80.61  ? 838  LEU A CG    1 
ATOM   7664  C CD1   . LEU D 4 841  ? 174.156 167.763 121.100 1.00 80.61  ? 838  LEU A CD1   1 
ATOM   7665  C CD2   . LEU D 4 841  ? 174.082 165.449 122.041 1.00 80.61  ? 838  LEU A CD2   1 
ATOM   7666  N N     . SER D 4 842  ? 173.939 162.965 118.273 1.00 75.88  ? 839  SER A N     1 
ATOM   7667  C CA    . SER D 4 842  ? 173.369 162.402 117.062 1.00 75.88  ? 839  SER A CA    1 
ATOM   7668  C C     . SER D 4 842  ? 172.646 163.486 116.268 1.00 75.88  ? 839  SER A C     1 
ATOM   7669  O O     . SER D 4 842  ? 172.326 164.562 116.782 1.00 75.88  ? 839  SER A O     1 
ATOM   7670  C CB    . SER D 4 842  ? 172.409 161.262 117.399 1.00 75.88  ? 839  SER A CB    1 
ATOM   7671  O OG    . SER D 4 842  ? 173.033 160.298 118.230 1.00 75.88  ? 839  SER A OG    1 
ATOM   7672  N N     . ASP D 4 843  ? 172.398 163.192 114.989 1.00 73.60  ? 840  ASP A N     1 
ATOM   7673  C CA    . ASP D 4 843  ? 171.772 164.180 114.116 1.00 73.60  ? 840  ASP A CA    1 
ATOM   7674  C C     . ASP D 4 843  ? 170.383 164.560 114.615 1.00 73.60  ? 840  ASP A C     1 
ATOM   7675  O O     . ASP D 4 843  ? 170.035 165.747 114.659 1.00 73.60  ? 840  ASP A O     1 
ATOM   7676  C CB    . ASP D 4 843  ? 171.703 163.644 112.686 1.00 73.60  ? 840  ASP A CB    1 
ATOM   7677  C CG    . ASP D 4 843  ? 172.987 163.881 111.912 1.00 73.60  ? 840  ASP A CG    1 
ATOM   7678  O OD1   . ASP D 4 843  ? 174.065 163.913 112.542 1.00 73.60  ? 840  ASP A OD1   1 
ATOM   7679  O OD2   . ASP D 4 843  ? 172.918 164.035 110.675 1.00 73.60  ? 840  ASP A OD2   1 
ATOM   7680  N N     . GLU D 4 844  ? 169.578 163.568 115.002 1.00 73.10  ? 841  GLU A N     1 
ATOM   7681  C CA    . GLU D 4 844  ? 168.251 163.865 115.532 1.00 73.10  ? 841  GLU A CA    1 
ATOM   7682  C C     . GLU D 4 844  ? 168.339 164.615 116.856 1.00 73.10  ? 841  GLU A C     1 
ATOM   7683  O O     . GLU D 4 844  ? 167.570 165.553 117.096 1.00 73.10  ? 841  GLU A O     1 
ATOM   7684  C CB    . GLU D 4 844  ? 167.438 162.574 115.671 1.00 73.10  ? 841  GLU A CB    1 
ATOM   7685  C CG    . GLU D 4 844  ? 167.923 161.602 116.736 1.00 73.10  ? 841  GLU A CG    1 
ATOM   7686  C CD    . GLU D 4 844  ? 169.018 160.678 116.236 1.00 73.10  ? 841  GLU A CD    1 
ATOM   7687  O OE1   . GLU D 4 844  ? 169.611 160.970 115.176 1.00 73.10  ? 841  GLU A OE1   1 
ATOM   7688  O OE2   . GLU D 4 844  ? 169.285 159.656 116.903 1.00 73.10  ? 841  GLU A OE2   1 
ATOM   7689  N N     . ALA D 4 845  ? 169.280 164.231 117.722 1.00 68.74  ? 842  ALA A N     1 
ATOM   7690  C CA    . ALA D 4 845  ? 169.468 164.958 118.974 1.00 68.74  ? 842  ALA A CA    1 
ATOM   7691  C C     . ALA D 4 845  ? 169.942 166.383 118.718 1.00 68.74  ? 842  ALA A C     1 
ATOM   7692  O O     . ALA D 4 845  ? 169.500 167.322 119.390 1.00 68.74  ? 842  ALA A O     1 
ATOM   7693  C CB    . ALA D 4 845  ? 170.455 164.214 119.871 1.00 68.74  ? 842  ALA A CB    1 
ATOM   7694  N N     . ARG D 4 846  ? 170.848 166.561 117.753 1.00 71.49  ? 843  ARG A N     1 
ATOM   7695  C CA    . ARG D 4 846  ? 171.324 167.900 117.423 1.00 71.49  ? 843  ARG A CA    1 
ATOM   7696  C C     . ARG D 4 846  ? 170.192 168.769 116.893 1.00 71.49  ? 843  ARG A C     1 
ATOM   7697  O O     . ARG D 4 846  ? 170.109 169.960 117.217 1.00 71.49  ? 843  ARG A O     1 
ATOM   7698  C CB    . ARG D 4 846  ? 172.461 167.816 116.406 1.00 71.49  ? 843  ARG A CB    1 
ATOM   7699  C CG    . ARG D 4 846  ? 173.134 169.147 116.118 1.00 71.49  ? 843  ARG A CG    1 
ATOM   7700  C CD    . ARG D 4 846  ? 174.602 168.956 115.771 1.00 71.49  ? 843  ARG A CD    1 
ATOM   7701  N NE    . ARG D 4 846  ? 175.395 168.578 116.935 1.00 71.49  ? 843  ARG A NE    1 
ATOM   7702  C CZ    . ARG D 4 846  ? 175.771 169.416 117.891 1.00 71.49  ? 843  ARG A CZ    1 
ATOM   7703  N NH1   . ARG D 4 846  ? 175.448 170.699 117.854 1.00 71.49  ? 843  ARG A NH1   1 
ATOM   7704  N NH2   . ARG D 4 846  ? 176.492 168.957 118.910 1.00 71.49  ? 843  ARG A NH2   1 
ATOM   7705  N N     . ALA D 4 847  ? 169.313 168.194 116.070 1.00 67.96  ? 844  ALA A N     1 
ATOM   7706  C CA    . ALA D 4 847  ? 168.166 168.948 115.575 1.00 67.96  ? 844  ALA A CA    1 
ATOM   7707  C C     . ALA D 4 847  ? 167.165 169.246 116.684 1.00 67.96  ? 844  ALA A C     1 
ATOM   7708  O O     . ALA D 4 847  ? 166.507 170.292 116.659 1.00 67.96  ? 844  ALA A O     1 
ATOM   7709  C CB    . ALA D 4 847  ? 167.487 168.187 114.437 1.00 67.96  ? 844  ALA A CB    1 
ATOM   7710  N N     . LEU D 4 848  ? 167.026 168.339 117.652 1.00 61.03  ? 845  LEU A N     1 
ATOM   7711  C CA    . LEU D 4 848  ? 166.081 168.541 118.744 1.00 61.03  ? 845  LEU A CA    1 
ATOM   7712  C C     . LEU D 4 848  ? 166.584 169.549 119.769 1.00 61.03  ? 845  LEU A C     1 
ATOM   7713  O O     . LEU D 4 848  ? 165.772 170.178 120.457 1.00 61.03  ? 845  LEU A O     1 
ATOM   7714  C CB    . LEU D 4 848  ? 165.787 167.204 119.426 1.00 61.03  ? 845  LEU A CB    1 
ATOM   7715  C CG    . LEU D 4 848  ? 164.582 167.140 120.363 1.00 61.03  ? 845  LEU A CG    1 
ATOM   7716  C CD1   . LEU D 4 848  ? 163.305 167.472 119.611 1.00 61.03  ? 845  LEU A CD1   1 
ATOM   7717  C CD2   . LEU D 4 848  ? 164.488 165.767 121.006 1.00 61.03  ? 845  LEU A CD2   1 
ATOM   7718  N N     . LEU D 4 849  ? 167.900 169.707 119.889 1.00 62.16  ? 846  LEU A N     1 
ATOM   7719  C CA    . LEU D 4 849  ? 168.466 170.578 120.918 1.00 62.16  ? 846  LEU A CA    1 
ATOM   7720  C C     . LEU D 4 849  ? 167.915 172.003 120.916 1.00 62.16  ? 846  LEU A C     1 
ATOM   7721  O O     . LEU D 4 849  ? 167.623 172.515 122.009 1.00 62.16  ? 846  LEU A O     1 
ATOM   7722  C CB    . LEU D 4 849  ? 169.998 170.588 120.790 1.00 62.16  ? 846  LEU A CB    1 
ATOM   7723  C CG    . LEU D 4 849  ? 170.835 171.290 121.867 1.00 62.16  ? 846  LEU A CG    1 
ATOM   7724  C CD1   . LEU D 4 849  ? 172.208 170.657 121.937 1.00 62.16  ? 846  LEU A CD1   1 
ATOM   7725  C CD2   . LEU D 4 849  ? 170.978 172.785 121.606 1.00 62.16  ? 846  LEU A CD2   1 
ATOM   7726  N N     . PRO D 4 850  ? 167.766 172.699 119.783 1.00 60.47  ? 847  PRO A N     1 
ATOM   7727  C CA    . PRO D 4 850  ? 167.228 174.069 119.848 1.00 60.47  ? 847  PRO A CA    1 
ATOM   7728  C C     . PRO D 4 850  ? 165.817 174.147 120.400 1.00 60.47  ? 847  PRO A C     1 
ATOM   7729  O O     . PRO D 4 850  ? 165.405 175.221 120.854 1.00 60.47  ? 847  PRO A O     1 
ATOM   7730  C CB    . PRO D 4 850  ? 167.281 174.542 118.388 1.00 60.47  ? 847  PRO A CB    1 
ATOM   7731  C CG    . PRO D 4 850  ? 167.385 173.298 117.577 1.00 60.47  ? 847  PRO A CG    1 
ATOM   7732  C CD    . PRO D 4 850  ? 168.185 172.356 118.413 1.00 60.47  ? 847  PRO A CD    1 
ATOM   7733  N N     . ASN D 4 851  ? 165.066 173.050 120.378 1.00 56.58  ? 848  ASN A N     1 
ATOM   7734  C CA    . ASN D 4 851  ? 163.676 173.053 120.809 1.00 56.58  ? 848  ASN A CA    1 
ATOM   7735  C C     . ASN D 4 851  ? 163.497 172.766 122.296 1.00 56.58  ? 848  ASN A C     1 
ATOM   7736  O O     . ASN D 4 851  ? 162.382 172.920 122.806 1.00 56.58  ? 848  ASN A O     1 
ATOM   7737  C CB    . ASN D 4 851  ? 162.883 172.026 119.992 1.00 56.58  ? 848  ASN A CB    1 
ATOM   7738  C CG    . ASN D 4 851  ? 161.443 172.439 119.771 1.00 56.58  ? 848  ASN A CG    1 
ATOM   7739  O OD1   . ASN D 4 851  ? 160.999 173.471 120.268 1.00 56.58  ? 848  ASN A OD1   1 
ATOM   7740  N ND2   . ASN D 4 851  ? 160.705 171.632 119.018 1.00 56.58  ? 848  ASN A ND2   1 
ATOM   7741  N N     . VAL D 4 852  ? 164.554 172.369 123.004 1.00 51.65  ? 849  VAL A N     1 
ATOM   7742  C CA    . VAL D 4 852  ? 164.434 171.950 124.395 1.00 51.65  ? 849  VAL A CA    1 
ATOM   7743  C C     . VAL D 4 852  ? 164.870 173.089 125.310 1.00 51.65  ? 849  VAL A C     1 
ATOM   7744  O O     . VAL D 4 852  ? 165.594 174.004 124.909 1.00 51.65  ? 849  VAL A O     1 
ATOM   7745  C CB    . VAL D 4 852  ? 165.252 170.669 124.666 1.00 51.65  ? 849  VAL A CB    1 
ATOM   7746  C CG1   . VAL D 4 852  ? 166.741 170.974 124.678 1.00 51.65  ? 849  VAL A CG1   1 
ATOM   7747  C CG2   . VAL D 4 852  ? 164.815 170.003 125.960 1.00 51.65  ? 849  VAL A CG2   1 
ATOM   7748  N N     . ILE D 4 853  ? 164.420 173.032 126.563 1.00 50.26  ? 850  ILE A N     1 
ATOM   7749  C CA    . ILE D 4 853  ? 164.729 174.035 127.575 1.00 50.26  ? 850  ILE A CA    1 
ATOM   7750  C C     . ILE D 4 853  ? 165.467 173.358 128.723 1.00 50.26  ? 850  ILE A C     1 
ATOM   7751  O O     . ILE D 4 853  ? 165.030 172.314 129.221 1.00 50.26  ? 850  ILE A O     1 
ATOM   7752  C CB    . ILE D 4 853  ? 163.455 174.742 128.077 1.00 50.26  ? 850  ILE A CB    1 
ATOM   7753  C CG1   . ILE D 4 853  ? 163.770 175.630 129.281 1.00 50.26  ? 850  ILE A CG1   1 
ATOM   7754  C CG2   . ILE D 4 853  ? 162.367 173.731 128.408 1.00 50.26  ? 850  ILE A CG2   1 
ATOM   7755  C CD1   . ILE D 4 853  ? 162.651 176.581 129.642 1.00 50.26  ? 850  ILE A CD1   1 
ATOM   7756  N N     . THR D 4 854  ? 166.587 173.947 129.133 1.00 50.26  ? 851  THR A N     1 
ATOM   7757  C CA    . THR D 4 854  ? 167.392 173.445 130.235 1.00 50.26  ? 851  THR A CA    1 
ATOM   7758  C C     . THR D 4 854  ? 167.224 174.342 131.455 1.00 50.26  ? 851  THR A C     1 
ATOM   7759  O O     . THR D 4 854  ? 166.917 175.532 131.334 1.00 50.26  ? 851  THR A O     1 
ATOM   7760  C CB    . THR D 4 854  ? 168.872 173.361 129.848 1.00 50.26  ? 851  THR A CB    1 
ATOM   7761  O OG1   . THR D 4 854  ? 169.631 172.868 130.958 1.00 50.26  ? 851  THR A OG1   1 
ATOM   7762  C CG2   . THR D 4 854  ? 169.399 174.728 129.445 1.00 50.26  ? 851  THR A CG2   1 
ATOM   7763  N N     . LYS D 4 855  ? 167.423 173.761 132.636 1.00 50.26  ? 852  LYS A N     1 
ATOM   7764  C CA    . LYS D 4 855  ? 167.180 174.451 133.895 1.00 50.26  ? 852  LYS A CA    1 
ATOM   7765  C C     . LYS D 4 855  ? 168.398 174.357 134.801 1.00 50.26  ? 852  LYS A C     1 
ATOM   7766  O O     . LYS D 4 855  ? 169.042 173.308 134.885 1.00 50.26  ? 852  LYS A O     1 
ATOM   7767  C CB    . LYS D 4 855  ? 165.960 173.872 134.615 1.00 50.26  ? 852  LYS A CB    1 
ATOM   7768  C CG    . LYS D 4 855  ? 164.657 174.582 134.301 1.00 50.26  ? 852  LYS A CG    1 
ATOM   7769  C CD    . LYS D 4 855  ? 163.527 174.043 135.156 1.00 50.26  ? 852  LYS A CD    1 
ATOM   7770  C CE    . LYS D 4 855  ? 163.842 174.190 136.633 1.00 50.26  ? 852  LYS A CE    1 
ATOM   7771  N NZ    . LYS D 4 855  ? 164.369 175.544 136.957 1.00 50.26  ? 852  LYS A NZ    1 
ATOM   7772  N N     . GLU D 4 856  ? 168.702 175.460 135.479 1.00 50.26  ? 853  GLU A N     1 
ATOM   7773  C CA    . GLU D 4 856  ? 169.770 175.483 136.467 1.00 50.26  ? 853  GLU A CA    1 
ATOM   7774  C C     . GLU D 4 856  ? 169.294 174.869 137.778 1.00 50.26  ? 853  GLU A C     1 
ATOM   7775  O O     . GLU D 4 856  ? 168.098 174.844 138.079 1.00 50.26  ? 853  GLU A O     1 
ATOM   7776  C CB    . GLU D 4 856  ? 170.250 176.914 136.710 1.00 50.26  ? 853  GLU A CB    1 
ATOM   7777  C CG    . GLU D 4 856  ? 170.986 177.535 135.535 1.00 50.26  ? 853  GLU A CG    1 
ATOM   7778  C CD    . GLU D 4 856  ? 171.902 176.554 134.833 1.00 50.26  ? 853  GLU A CD    1 
ATOM   7779  O OE1   . GLU D 4 856  ? 172.806 176.002 135.495 1.00 50.26  ? 853  GLU A OE1   1 
ATOM   7780  O OE2   . GLU D 4 856  ? 171.716 176.333 133.619 1.00 50.26  ? 853  GLU A OE2   1 
ATOM   7781  N N     . VAL D 4 857  ? 170.248 174.376 138.562 1.00 50.76  ? 854  VAL A N     1 
ATOM   7782  C CA    . VAL D 4 857  ? 169.937 173.715 139.826 1.00 50.76  ? 854  VAL A CA    1 
ATOM   7783  C C     . VAL D 4 857  ? 169.847 174.778 140.916 1.00 50.76  ? 854  VAL A C     1 
ATOM   7784  O O     . VAL D 4 857  ? 170.866 175.291 141.382 1.00 50.76  ? 854  VAL A O     1 
ATOM   7785  C CB    . VAL D 4 857  ? 170.983 172.654 140.179 1.00 50.76  ? 854  VAL A CB    1 
ATOM   7786  C CG1   . VAL D 4 857  ? 170.677 172.046 141.537 1.00 50.76  ? 854  VAL A CG1   1 
ATOM   7787  C CG2   . VAL D 4 857  ? 171.034 171.583 139.112 1.00 50.76  ? 854  VAL A CG2   1 
ATOM   7788  N N     . SER D 4 858  ? 168.622 175.114 141.323 1.00 50.77  ? 855  SER A N     1 
ATOM   7789  C CA    . SER D 4 858  ? 168.450 176.009 142.461 1.00 50.77  ? 855  SER A CA    1 
ATOM   7790  C C     . SER D 4 858  ? 168.744 175.290 143.771 1.00 50.77  ? 855  SER A C     1 
ATOM   7791  O O     . SER D 4 858  ? 169.389 175.850 144.665 1.00 50.77  ? 855  SER A O     1 
ATOM   7792  C CB    . SER D 4 858  ? 167.035 176.585 142.470 1.00 50.77  ? 855  SER A CB    1 
ATOM   7793  O OG    . SER D 4 858  ? 166.650 177.014 141.176 1.00 50.77  ? 855  SER A OG    1 
ATOM   7794  N N     . HIS D 4 859  ? 168.283 174.049 143.900 1.00 50.26  ? 856  HIS A N     1 
ATOM   7795  C CA    . HIS D 4 859  ? 168.501 173.251 145.095 1.00 50.26  ? 856  HIS A CA    1 
ATOM   7796  C C     . HIS D 4 859  ? 168.693 171.798 144.690 1.00 50.26  ? 856  HIS A C     1 
ATOM   7797  O O     . HIS D 4 859  ? 168.271 171.374 143.612 1.00 50.26  ? 856  HIS A O     1 
ATOM   7798  C CB    . HIS D 4 859  ? 167.335 173.379 146.082 1.00 50.26  ? 856  HIS A CB    1 
ATOM   7799  C CG    . HIS D 4 859  ? 165.987 173.278 145.439 1.00 50.26  ? 856  HIS A CG    1 
ATOM   7800  N ND1   . HIS D 4 859  ? 165.431 172.076 145.060 1.00 50.26  ? 856  HIS A ND1   1 
ATOM   7801  C CD2   . HIS D 4 859  ? 165.083 174.231 145.110 1.00 50.26  ? 856  HIS A CD2   1 
ATOM   7802  C CE1   . HIS D 4 859  ? 164.243 172.291 144.524 1.00 50.26  ? 856  HIS A CE1   1 
ATOM   7803  N NE2   . HIS D 4 859  ? 164.008 173.591 144.542 1.00 50.26  ? 856  HIS A NE2   1 
ATOM   7804  N N     . GLU D 4 860  ? 169.339 171.037 145.569 1.00 50.26  ? 857  GLU A N     1 
ATOM   7805  C CA    . GLU D 4 860  ? 169.591 169.633 145.282 1.00 50.26  ? 857  GLU A CA    1 
ATOM   7806  C C     . GLU D 4 860  ? 168.282 168.857 145.210 1.00 50.26  ? 857  GLU A C     1 
ATOM   7807  O O     . GLU D 4 860  ? 167.347 169.105 145.977 1.00 50.26  ? 857  GLU A O     1 
ATOM   7808  C CB    . GLU D 4 860  ? 170.515 169.030 146.342 1.00 50.26  ? 857  GLU A CB    1 
ATOM   7809  C CG    . GLU D 4 860  ? 169.916 168.951 147.735 1.00 50.26  ? 857  GLU A CG    1 
ATOM   7810  C CD    . GLU D 4 860  ? 170.803 168.198 148.707 1.00 50.26  ? 857  GLU A CD    1 
ATOM   7811  O OE1   . GLU D 4 860  ? 171.423 167.197 148.292 1.00 50.26  ? 857  GLU A OE1   1 
ATOM   7812  O OE2   . GLU D 4 860  ? 170.880 168.609 149.884 1.00 50.26  ? 857  GLU A OE2   1 
ATOM   7813  N N     . ILE D 4 861  ? 168.213 167.925 144.264 1.00 50.26  ? 858  ILE A N     1 
ATOM   7814  C CA    . ILE D 4 861  ? 167.035 167.086 144.083 1.00 50.26  ? 858  ILE A CA    1 
ATOM   7815  C C     . ILE D 4 861  ? 167.493 165.640 143.958 1.00 50.26  ? 858  ILE A C     1 
ATOM   7816  O O     . ILE D 4 861  ? 167.963 165.212 142.898 1.00 50.26  ? 858  ILE A O     1 
ATOM   7817  C CB    . ILE D 4 861  ? 166.213 167.533 142.860 1.00 50.26  ? 858  ILE A CB    1 
ATOM   7818  C CG1   . ILE D 4 861  ? 165.541 168.876 143.140 1.00 50.26  ? 858  ILE A CG1   1 
ATOM   7819  C CG2   . ILE D 4 861  ? 165.163 166.499 142.506 1.00 50.26  ? 858  ILE A CG2   1 
ATOM   7820  C CD1   . ILE D 4 861  ? 165.114 169.615 141.901 1.00 50.26  ? 858  ILE A CD1   1 
ATOM   7821  N N     . ILE D 4 862  ? 167.380 164.886 145.045 1.00 50.26  ? 859  ILE A N     1 
ATOM   7822  C CA    . ILE D 4 862  ? 167.864 163.511 145.074 1.00 50.26  ? 859  ILE A CA    1 
ATOM   7823  C C     . ILE D 4 862  ? 166.828 162.604 144.431 1.00 50.26  ? 859  ILE A C     1 
ATOM   7824  O O     . ILE D 4 862  ? 165.649 162.625 144.803 1.00 50.26  ? 859  ILE A O     1 
ATOM   7825  C CB    . ILE D 4 862  ? 168.168 163.070 146.514 1.00 50.26  ? 859  ILE A CB    1 
ATOM   7826  C CG1   . ILE D 4 862  ? 169.251 163.956 147.128 1.00 50.26  ? 859  ILE A CG1   1 
ATOM   7827  C CG2   . ILE D 4 862  ? 168.593 161.614 146.543 1.00 50.26  ? 859  ILE A CG2   1 
ATOM   7828  C CD1   . ILE D 4 862  ? 169.571 163.612 148.565 1.00 50.26  ? 859  ILE A CD1   1 
ATOM   7829  N N     . LYS D 4 863  ? 167.263 161.808 143.458 1.00 50.26  ? 860  LYS A N     1 
ATOM   7830  C CA    . LYS D 4 863  ? 166.380 160.817 142.862 1.00 50.26  ? 860  LYS A CA    1 
ATOM   7831  C C     . LYS D 4 863  ? 166.104 159.705 143.864 1.00 50.26  ? 860  LYS A C     1 
ATOM   7832  O O     . LYS D 4 863  ? 167.028 159.185 144.497 1.00 50.26  ? 860  LYS A O     1 
ATOM   7833  C CB    . LYS D 4 863  ? 167.002 160.239 141.594 1.00 50.26  ? 860  LYS A CB    1 
ATOM   7834  C CG    . LYS D 4 863  ? 166.128 159.208 140.906 1.00 50.26  ? 860  LYS A CG    1 
ATOM   7835  C CD    . LYS D 4 863  ? 166.830 158.589 139.714 1.00 50.26  ? 860  LYS A CD    1 
ATOM   7836  C CE    . LYS D 4 863  ? 166.012 157.454 139.128 1.00 50.26  ? 860  LYS A CE    1 
ATOM   7837  N NZ    . LYS D 4 863  ? 164.747 157.950 138.521 1.00 50.26  ? 860  LYS A NZ    1 
ATOM   7838  N N     . ASP D 4 864  ? 164.829 159.343 144.004 1.00 50.26  ? 861  ASP A N     1 
ATOM   7839  C CA    . ASP D 4 864  ? 164.400 158.292 144.925 1.00 50.26  ? 861  ASP A CA    1 
ATOM   7840  C C     . ASP D 4 864  ? 164.853 158.593 146.352 1.00 50.26  ? 861  ASP A C     1 
ATOM   7841  O O     . ASP D 4 864  ? 165.367 157.729 147.064 1.00 50.26  ? 861  ASP A O     1 
ATOM   7842  C CB    . ASP D 4 864  ? 164.905 156.924 144.462 1.00 42.29  ? 861  ASP A CB    1 
ATOM   7843  C CG    . ASP D 4 864  ? 164.427 156.570 143.070 1.00 42.29  ? 861  ASP A CG    1 
ATOM   7844  O OD1   . ASP D 4 864  ? 163.397 157.127 142.637 1.00 42.29  ? 861  ASP A OD1   1 
ATOM   7845  O OD2   . ASP D 4 864  ? 165.076 155.733 142.408 1.00 42.29  ? 861  ASP A OD2   1 
ATOM   7846  N N     . ARG D 4 865  ? 164.659 159.846 146.767 1.00 50.26  ? 862  ARG A N     1 
ATOM   7847  C CA    . ARG D 4 865  ? 165.023 160.256 148.118 1.00 50.26  ? 862  ARG A CA    1 
ATOM   7848  C C     . ARG D 4 865  ? 164.196 159.541 149.178 1.00 50.26  ? 862  ARG A C     1 
ATOM   7849  O O     . ARG D 4 865  ? 164.638 159.436 150.327 1.00 50.26  ? 862  ARG A O     1 
ATOM   7850  C CB    . ARG D 4 865  ? 164.864 161.772 148.257 1.00 38.77  ? 862  ARG A CB    1 
ATOM   7851  C CG    . ARG D 4 865  ? 165.315 162.339 149.589 1.00 38.77  ? 862  ARG A CG    1 
ATOM   7852  C CD    . ARG D 4 865  ? 165.229 163.849 149.596 1.00 38.77  ? 862  ARG A CD    1 
ATOM   7853  N NE    . ARG D 4 865  ? 163.860 164.310 149.411 1.00 38.77  ? 862  ARG A NE    1 
ATOM   7854  C CZ    . ARG D 4 865  ? 163.331 165.350 150.040 1.00 38.77  ? 862  ARG A CZ    1 
ATOM   7855  N NH1   . ARG D 4 865  ? 164.029 166.058 150.913 1.00 38.77  ? 862  ARG A NH1   1 
ATOM   7856  N NH2   . ARG D 4 865  ? 162.070 165.688 149.788 1.00 38.77  ? 862  ARG A NH2   1 
ATOM   7857  N N     . ARG D 4 866  ? 163.014 159.037 148.813 1.00 50.26  ? 863  ARG A N     1 
ATOM   7858  C CA    . ARG D 4 866  ? 162.160 158.345 149.773 1.00 50.26  ? 863  ARG A CA    1 
ATOM   7859  C C     . ARG D 4 866  ? 162.874 157.168 150.419 1.00 50.26  ? 863  ARG A C     1 
ATOM   7860  O O     . ARG D 4 866  ? 162.589 156.825 151.572 1.00 50.26  ? 863  ARG A O     1 
ATOM   7861  C CB    . ARG D 4 866  ? 160.888 157.852 149.084 1.00 50.26  ? 863  ARG A CB    1 
ATOM   7862  C CG    . ARG D 4 866  ? 159.909 158.932 148.679 1.00 50.26  ? 863  ARG A CG    1 
ATOM   7863  C CD    . ARG D 4 866  ? 160.166 159.402 147.255 1.00 50.26  ? 863  ARG A CD    1 
ATOM   7864  N NE    . ARG D 4 866  ? 160.335 158.295 146.320 1.00 50.26  ? 863  ARG A NE    1 
ATOM   7865  C CZ    . ARG D 4 866  ? 159.358 157.502 145.902 1.00 50.26  ? 863  ARG A CZ    1 
ATOM   7866  N NH1   . ARG D 4 866  ? 158.114 157.656 146.323 1.00 50.26  ? 863  ARG A NH1   1 
ATOM   7867  N NH2   . ARG D 4 866  ? 159.635 156.533 145.037 1.00 50.26  ? 863  ARG A NH2   1 
ATOM   7868  N N     . PHE D 4 867  ? 163.801 156.540 149.696 1.00 50.26  ? 864  PHE A N     1 
ATOM   7869  C CA    . PHE D 4 867  ? 164.436 155.303 150.126 1.00 50.26  ? 864  PHE A CA    1 
ATOM   7870  C C     . PHE D 4 867  ? 165.918 155.482 150.430 1.00 50.26  ? 864  PHE A C     1 
ATOM   7871  O O     . PHE D 4 867  ? 166.668 154.501 150.439 1.00 50.26  ? 864  PHE A O     1 
ATOM   7872  C CB    . PHE D 4 867  ? 164.232 154.220 149.067 1.00 50.26  ? 864  PHE A CB    1 
ATOM   7873  C CG    . PHE D 4 867  ? 162.791 153.976 148.720 1.00 50.26  ? 864  PHE A CG    1 
ATOM   7874  C CD1   . PHE D 4 867  ? 162.122 154.810 147.843 1.00 50.26  ? 864  PHE A CD1   1 
ATOM   7875  C CD2   . PHE D 4 867  ? 162.100 152.923 149.289 1.00 50.26  ? 864  PHE A CD2   1 
ATOM   7876  C CE1   . PHE D 4 867  ? 160.800 154.589 147.526 1.00 50.26  ? 864  PHE A CE1   1 
ATOM   7877  C CE2   . PHE D 4 867  ? 160.776 152.697 148.973 1.00 50.26  ? 864  PHE A CE2   1 
ATOM   7878  C CZ    . PHE D 4 867  ? 160.126 153.533 148.093 1.00 50.26  ? 864  PHE A CZ    1 
ATOM   7879  N N     . THR D 4 868  ? 166.358 156.712 150.673 1.00 50.26  ? 865  THR A N     1 
ATOM   7880  C CA    . THR D 4 868  ? 167.730 156.970 151.081 1.00 50.26  ? 865  THR A CA    1 
ATOM   7881  C C     . THR D 4 868  ? 167.894 157.012 152.594 1.00 50.26  ? 865  THR A C     1 
ATOM   7882  O O     . THR D 4 868  ? 169.007 157.238 153.076 1.00 50.26  ? 865  THR A O     1 
ATOM   7883  C CB    . THR D 4 868  ? 168.227 158.286 150.475 1.00 50.26  ? 865  THR A CB    1 
ATOM   7884  O OG1   . THR D 4 868  ? 167.415 159.368 150.948 1.00 50.26  ? 865  THR A OG1   1 
ATOM   7885  C CG2   . THR D 4 868  ? 168.158 158.232 148.958 1.00 50.26  ? 865  THR A CG2   1 
ATOM   7886  N N     . SER D 4 869  ? 166.818 156.800 153.347 1.00 50.26  ? 866  SER A N     1 
ATOM   7887  C CA    . SER D 4 869  ? 166.882 156.809 154.801 1.00 50.26  ? 866  SER A CA    1 
ATOM   7888  C C     . SER D 4 869  ? 165.751 155.950 155.343 1.00 50.26  ? 866  SER A C     1 
ATOM   7889  O O     . SER D 4 869  ? 164.774 155.666 154.646 1.00 50.26  ? 866  SER A O     1 
ATOM   7890  C CB    . SER D 4 869  ? 166.797 158.232 155.358 1.00 50.26  ? 866  SER A CB    1 
ATOM   7891  O OG    . SER D 4 869  ? 165.537 158.813 155.075 1.00 50.26  ? 866  SER A OG    1 
ATOM   7892  N N     . ASP D 4 870  ? 165.899 155.538 156.599 1.00 50.26  ? 867  ASP A N     1 
ATOM   7893  C CA    . ASP D 4 870  ? 164.878 154.728 157.247 1.00 50.26  ? 867  ASP A CA    1 
ATOM   7894  C C     . ASP D 4 870  ? 163.644 155.571 157.537 1.00 50.26  ? 867  ASP A C     1 
ATOM   7895  O O     . ASP D 4 870  ? 163.746 156.670 158.088 1.00 50.26  ? 867  ASP A O     1 
ATOM   7896  C CB    . ASP D 4 870  ? 165.424 154.129 158.539 1.00 50.26  ? 867  ASP A CB    1 
ATOM   7897  C CG    . ASP D 4 870  ? 166.695 153.336 158.322 1.00 50.26  ? 867  ASP A CG    1 
ATOM   7898  O OD1   . ASP D 4 870  ? 166.886 152.813 157.205 1.00 50.26  ? 867  ASP A OD1   1 
ATOM   7899  O OD2   . ASP D 4 870  ? 167.502 153.234 159.268 1.00 50.26  ? 867  ASP A OD2   1 
ATOM   7900  N N     . LYS D 4 871  ? 162.473 155.053 157.173 1.00 50.26  ? 868  LYS A N     1 
ATOM   7901  C CA    . LYS D 4 871  ? 161.225 155.793 157.293 1.00 50.26  ? 868  LYS A CA    1 
ATOM   7902  C C     . LYS D 4 871  ? 160.215 154.983 158.088 1.00 50.26  ? 868  LYS A C     1 
ATOM   7903  O O     . LYS D 4 871  ? 160.023 153.793 157.823 1.00 50.26  ? 868  LYS A O     1 
ATOM   7904  C CB    . LYS D 4 871  ? 160.653 156.131 155.913 1.00 50.26  ? 868  LYS A CB    1 
ATOM   7905  C CG    . LYS D 4 871  ? 161.570 156.975 155.048 1.00 50.26  ? 868  LYS A CG    1 
ATOM   7906  C CD    . LYS D 4 871  ? 161.695 158.385 155.592 1.00 50.26  ? 868  LYS A CD    1 
ATOM   7907  C CE    . LYS D 4 871  ? 162.263 159.326 154.548 1.00 50.26  ? 868  LYS A CE    1 
ATOM   7908  N NZ    . LYS D 4 871  ? 161.255 159.665 153.509 1.00 50.26  ? 868  LYS A NZ    1 
ATOM   7909  N N     . PHE D 4 872  ? 159.575 155.629 159.058 1.00 50.26  ? 869  PHE A N     1 
ATOM   7910  C CA    . PHE D 4 872  ? 158.449 155.034 159.757 1.00 50.26  ? 869  PHE A CA    1 
ATOM   7911  C C     . PHE D 4 872  ? 157.167 155.269 158.967 1.00 50.26  ? 869  PHE A C     1 
ATOM   7912  O O     . PHE D 4 872  ? 157.090 156.151 158.109 1.00 50.26  ? 869  PHE A O     1 
ATOM   7913  C CB    . PHE D 4 872  ? 158.307 155.619 161.162 1.00 50.26  ? 869  PHE A CB    1 
ATOM   7914  C CG    . PHE D 4 872  ? 159.472 155.332 162.064 1.00 50.26  ? 869  PHE A CG    1 
ATOM   7915  C CD1   . PHE D 4 872  ? 160.651 156.045 161.946 1.00 50.26  ? 869  PHE A CD1   1 
ATOM   7916  C CD2   . PHE D 4 872  ? 159.381 154.356 163.039 1.00 50.26  ? 869  PHE A CD2   1 
ATOM   7917  C CE1   . PHE D 4 872  ? 161.719 155.784 162.777 1.00 50.26  ? 869  PHE A CE1   1 
ATOM   7918  C CE2   . PHE D 4 872  ? 160.446 154.092 163.873 1.00 50.26  ? 869  PHE A CE2   1 
ATOM   7919  C CZ    . PHE D 4 872  ? 161.616 154.807 163.741 1.00 50.26  ? 869  PHE A CZ    1 
ATOM   7920  N N     . PHE D 4 873  ? 156.147 154.467 159.265 1.00 50.26  ? 870  PHE A N     1 
ATOM   7921  C CA    . PHE D 4 873  ? 154.884 154.585 158.552 1.00 50.26  ? 870  PHE A CA    1 
ATOM   7922  C C     . PHE D 4 873  ? 153.735 154.282 159.499 1.00 50.26  ? 870  PHE A C     1 
ATOM   7923  O O     . PHE D 4 873  ? 153.897 153.592 160.508 1.00 50.26  ? 870  PHE A O     1 
ATOM   7924  C CB    . PHE D 4 873  ? 154.847 153.661 157.331 1.00 50.26  ? 870  PHE A CB    1 
ATOM   7925  C CG    . PHE D 4 873  ? 155.809 154.060 156.253 1.00 50.26  ? 870  PHE A CG    1 
ATOM   7926  C CD1   . PHE D 4 873  ? 155.511 155.103 155.397 1.00 50.26  ? 870  PHE A CD1   1 
ATOM   7927  C CD2   . PHE D 4 873  ? 157.019 153.409 156.110 1.00 50.26  ? 870  PHE A CD2   1 
ATOM   7928  C CE1   . PHE D 4 873  ? 156.397 155.480 154.413 1.00 50.26  ? 870  PHE A CE1   1 
ATOM   7929  C CE2   . PHE D 4 873  ? 157.908 153.782 155.127 1.00 50.26  ? 870  PHE A CE2   1 
ATOM   7930  C CZ    . PHE D 4 873  ? 157.596 154.820 154.278 1.00 50.26  ? 870  PHE A CZ    1 
ATOM   7931  N N     . PHE D 4 874  ? 152.563 154.812 159.155 1.00 50.26  ? 871  PHE A N     1 
ATOM   7932  C CA    . PHE D 4 874  ? 151.377 154.712 159.997 1.00 50.26  ? 871  PHE A CA    1 
ATOM   7933  C C     . PHE D 4 874  ? 150.173 154.444 159.111 1.00 50.26  ? 871  PHE A C     1 
ATOM   7934  O O     . PHE D 4 874  ? 149.798 155.295 158.301 1.00 50.26  ? 871  PHE A O     1 
ATOM   7935  C CB    . PHE D 4 874  ? 151.179 155.996 160.807 1.00 50.26  ? 871  PHE A CB    1 
ATOM   7936  C CG    . PHE D 4 874  ? 149.934 156.007 161.644 1.00 50.26  ? 871  PHE A CG    1 
ATOM   7937  C CD1   . PHE D 4 874  ? 149.635 154.948 162.482 1.00 50.26  ? 871  PHE A CD1   1 
ATOM   7938  C CD2   . PHE D 4 874  ? 149.070 157.086 161.604 1.00 50.26  ? 871  PHE A CD2   1 
ATOM   7939  C CE1   . PHE D 4 874  ? 148.494 154.963 163.255 1.00 50.26  ? 871  PHE A CE1   1 
ATOM   7940  C CE2   . PHE D 4 874  ? 147.928 157.106 162.374 1.00 50.26  ? 871  PHE A CE2   1 
ATOM   7941  C CZ    . PHE D 4 874  ? 147.639 156.043 163.201 1.00 50.26  ? 871  PHE A CZ    1 
ATOM   7942  N N     . HIS D 4 875  ? 149.573 153.266 159.261 1.00 50.26  ? 872  HIS A N     1 
ATOM   7943  C CA    . HIS D 4 875  ? 148.386 152.882 158.504 1.00 50.26  ? 872  HIS A CA    1 
ATOM   7944  C C     . HIS D 4 875  ? 147.177 153.011 159.420 1.00 50.26  ? 872  HIS A C     1 
ATOM   7945  O O     . HIS D 4 875  ? 147.046 152.262 160.393 1.00 50.26  ? 872  HIS A O     1 
ATOM   7946  C CB    . HIS D 4 875  ? 148.512 151.460 157.964 1.00 50.26  ? 872  HIS A CB    1 
ATOM   7947  C CG    . HIS D 4 875  ? 149.607 151.286 156.960 1.00 50.26  ? 872  HIS A CG    1 
ATOM   7948  N ND1   . HIS D 4 875  ? 149.517 150.398 155.911 1.00 50.26  ? 872  HIS A ND1   1 
ATOM   7949  C CD2   . HIS D 4 875  ? 150.818 151.882 156.846 1.00 50.26  ? 872  HIS A CD2   1 
ATOM   7950  C CE1   . HIS D 4 875  ? 150.624 150.456 155.192 1.00 50.26  ? 872  HIS A CE1   1 
ATOM   7951  N NE2   . HIS D 4 875  ? 151.429 151.349 155.738 1.00 50.26  ? 872  HIS A NE2   1 
ATOM   7952  N N     . VAL D 4 876  ? 146.296 153.955 159.109 1.00 50.26  ? 873  VAL A N     1 
ATOM   7953  C CA    . VAL D 4 876  ? 145.119 154.243 159.916 1.00 50.26  ? 873  VAL A CA    1 
ATOM   7954  C C     . VAL D 4 876  ? 143.886 154.074 159.040 1.00 50.26  ? 873  VAL A C     1 
ATOM   7955  O O     . VAL D 4 876  ? 143.848 154.611 157.931 1.00 50.26  ? 873  VAL A O     1 
ATOM   7956  C CB    . VAL D 4 876  ? 145.160 155.652 160.536 1.00 50.26  ? 873  VAL A CB    1 
ATOM   7957  C CG1   . VAL D 4 876  ? 145.298 156.729 159.467 1.00 50.26  ? 873  VAL A CG1   1 
ATOM   7958  C CG2   . VAL D 4 876  ? 143.928 155.890 161.378 1.00 50.26  ? 873  VAL A CG2   1 
ATOM   7959  N N     . PRO D 4 877  ? 142.885 153.309 159.466 1.00 50.26  ? 874  PRO A N     1 
ATOM   7960  C CA    . PRO D 4 877  ? 141.660 153.172 158.678 1.00 50.26  ? 874  PRO A CA    1 
ATOM   7961  C C     . PRO D 4 877  ? 140.581 154.154 159.104 1.00 50.26  ? 874  PRO A C     1 
ATOM   7962  O O     . PRO D 4 877  ? 140.477 154.553 160.264 1.00 50.26  ? 874  PRO A O     1 
ATOM   7963  C CB    . PRO D 4 877  ? 141.233 151.729 158.976 1.00 50.26  ? 874  PRO A CB    1 
ATOM   7964  C CG    . PRO D 4 877  ? 141.693 151.505 160.376 1.00 50.26  ? 874  PRO A CG    1 
ATOM   7965  C CD    . PRO D 4 877  ? 142.904 152.386 160.612 1.00 50.26  ? 874  PRO A CD    1 
ATOM   7966  N N     . ILE D 4 878  ? 139.765 154.544 158.126 1.00 50.26  ? 875  ILE A N     1 
ATOM   7967  C CA    . ILE D 4 878  ? 138.642 155.442 158.348 1.00 50.26  ? 875  ILE A CA    1 
ATOM   7968  C C     . ILE D 4 878  ? 137.406 154.828 157.710 1.00 50.26  ? 875  ILE A C     1 
ATOM   7969  O O     . ILE D 4 878  ? 137.493 153.954 156.846 1.00 50.26  ? 875  ILE A O     1 
ATOM   7970  C CB    . ILE D 4 878  ? 138.894 156.857 157.782 1.00 50.26  ? 875  ILE A CB    1 
ATOM   7971  C CG1   . ILE D 4 878  ? 138.829 156.843 156.256 1.00 50.26  ? 875  ILE A CG1   1 
ATOM   7972  C CG2   . ILE D 4 878  ? 140.239 157.388 158.241 1.00 50.26  ? 875  ILE A CG2   1 
ATOM   7973  C CD1   . ILE D 4 878  ? 138.989 158.205 155.630 1.00 50.26  ? 875  ILE A CD1   1 
ATOM   7974  N N     . THR D 4 879  ? 136.242 155.293 158.153 1.00 50.26  ? 876  THR A N     1 
ATOM   7975  C CA    . THR D 4 879  ? 134.958 154.838 157.624 1.00 50.26  ? 876  THR A CA    1 
ATOM   7976  C C     . THR D 4 879  ? 134.200 156.053 157.104 1.00 50.26  ? 876  THR A C     1 
ATOM   7977  O O     . THR D 4 879  ? 133.548 156.765 157.874 1.00 50.26  ? 876  THR A O     1 
ATOM   7978  C CB    . THR D 4 879  ? 134.151 154.094 158.684 1.00 50.26  ? 876  THR A CB    1 
ATOM   7979  O OG1   . THR D 4 879  ? 134.898 152.965 159.149 1.00 50.26  ? 876  THR A OG1   1 
ATOM   7980  C CG2   . THR D 4 879  ? 132.836 153.608 158.103 1.00 50.26  ? 876  THR A CG2   1 
ATOM   7981  N N     . LEU D 4 880  ? 134.293 156.292 155.801 1.00 50.26  ? 877  LEU A N     1 
ATOM   7982  C CA    . LEU D 4 880  ? 133.541 157.369 155.180 1.00 50.26  ? 877  LEU A CA    1 
ATOM   7983  C C     . LEU D 4 880  ? 132.063 157.005 155.113 1.00 50.26  ? 877  LEU A C     1 
ATOM   7984  O O     . LEU D 4 880  ? 131.695 155.831 155.033 1.00 50.26  ? 877  LEU A O     1 
ATOM   7985  C CB    . LEU D 4 880  ? 134.081 157.652 153.782 1.00 50.26  ? 877  LEU A CB    1 
ATOM   7986  C CG    . LEU D 4 880  ? 135.521 158.160 153.738 1.00 50.26  ? 877  LEU A CG    1 
ATOM   7987  C CD1   . LEU D 4 880  ? 136.156 157.851 152.399 1.00 50.26  ? 877  LEU A CD1   1 
ATOM   7988  C CD2   . LEU D 4 880  ? 135.555 159.650 154.006 1.00 50.26  ? 877  LEU A CD2   1 
ATOM   7989  N N     . ASN D 4 881  ? 131.213 158.033 155.146 1.00 50.26  ? 878  ASN A N     1 
ATOM   7990  C CA    . ASN D 4 881  ? 129.761 157.863 155.168 1.00 50.26  ? 878  ASN A CA    1 
ATOM   7991  C C     . ASN D 4 881  ? 129.340 156.978 156.343 1.00 50.26  ? 878  ASN A C     1 
ATOM   7992  O O     . ASN D 4 881  ? 128.676 155.953 156.183 1.00 50.26  ? 878  ASN A O     1 
ATOM   7993  C CB    . ASN D 4 881  ? 129.251 157.297 153.839 1.00 50.26  ? 878  ASN A CB    1 
ATOM   7994  C CG    . ASN D 4 881  ? 129.111 158.359 152.772 1.00 50.26  ? 878  ASN A CG    1 
ATOM   7995  O OD1   . ASN D 4 881  ? 129.571 158.186 151.644 1.00 50.26  ? 878  ASN A OD1   1 
ATOM   7996  N ND2   . ASN D 4 881  ? 128.474 159.469 153.123 1.00 50.26  ? 878  ASN A ND2   1 
ATOM   7997  N N     . TYR D 4 882  ? 129.751 157.400 157.540 1.00 50.26  ? 879  TYR A N     1 
ATOM   7998  C CA    . TYR D 4 882  ? 129.512 156.599 158.736 1.00 50.26  ? 879  TYR A CA    1 
ATOM   7999  C C     . TYR D 4 882  ? 128.024 156.460 159.031 1.00 50.26  ? 879  TYR A C     1 
ATOM   8000  O O     . TYR D 4 882  ? 127.564 155.390 159.445 1.00 50.26  ? 879  TYR A O     1 
ATOM   8001  C CB    . TYR D 4 882  ? 130.239 157.215 159.930 1.00 50.26  ? 879  TYR A CB    1 
ATOM   8002  C CG    . TYR D 4 882  ? 129.944 156.532 161.243 1.00 50.26  ? 879  TYR A CG    1 
ATOM   8003  C CD1   . TYR D 4 882  ? 130.279 155.201 161.445 1.00 50.26  ? 879  TYR A CD1   1 
ATOM   8004  C CD2   . TYR D 4 882  ? 129.337 157.220 162.283 1.00 50.26  ? 879  TYR A CD2   1 
ATOM   8005  C CE1   . TYR D 4 882  ? 130.010 154.574 162.645 1.00 50.26  ? 879  TYR A CE1   1 
ATOM   8006  C CE2   . TYR D 4 882  ? 129.067 156.602 163.487 1.00 50.26  ? 879  TYR A CE2   1 
ATOM   8007  C CZ    . TYR D 4 882  ? 129.406 155.279 163.662 1.00 50.26  ? 879  TYR A CZ    1 
ATOM   8008  O OH    . TYR D 4 882  ? 129.140 154.657 164.859 1.00 50.26  ? 879  TYR A OH    1 
ATOM   8009  N N     . GLN D 4 883  ? 127.255 157.528 158.824 1.00 50.26  ? 880  GLN A N     1 
ATOM   8010  C CA    . GLN D 4 883  ? 125.838 157.510 159.165 1.00 50.26  ? 880  GLN A CA    1 
ATOM   8011  C C     . GLN D 4 883  ? 125.006 156.643 158.228 1.00 50.26  ? 880  GLN A C     1 
ATOM   8012  O O     . GLN D 4 883  ? 123.827 156.413 158.515 1.00 50.26  ? 880  GLN A O     1 
ATOM   8013  C CB    . GLN D 4 883  ? 125.286 158.936 159.175 1.00 50.26  ? 880  GLN A CB    1 
ATOM   8014  C CG    . GLN D 4 883  ? 125.924 159.839 160.218 1.00 50.26  ? 880  GLN A CG    1 
ATOM   8015  C CD    . GLN D 4 883  ? 125.563 159.445 161.638 1.00 50.26  ? 880  GLN A CD    1 
ATOM   8016  O OE1   . GLN D 4 883  ? 124.644 158.657 161.864 1.00 50.26  ? 880  GLN A OE1   1 
ATOM   8017  N NE2   . GLN D 4 883  ? 126.288 159.994 162.605 1.00 50.26  ? 880  GLN A NE2   1 
ATOM   8018  N N     . ALA D 4 884  ? 125.578 156.163 157.128 1.00 50.26  ? 881  ALA A N     1 
ATOM   8019  C CA    . ALA D 4 884  ? 124.828 155.375 156.165 1.00 50.26  ? 881  ALA A CA    1 
ATOM   8020  C C     . ALA D 4 884  ? 124.702 153.928 156.636 1.00 50.26  ? 881  ALA A C     1 
ATOM   8021  O O     . ALA D 4 884  ? 125.154 153.553 157.721 1.00 50.26  ? 881  ALA A O     1 
ATOM   8022  C CB    . ALA D 4 884  ? 125.492 155.447 154.794 1.00 50.26  ? 881  ALA A CB    1 
ATOM   8023  N N     . ALA D 4 885  ? 124.074 153.102 155.803 1.00 50.26  ? 882  ALA A N     1 
ATOM   8024  C CA    . ALA D 4 885  ? 123.891 151.694 156.109 1.00 50.26  ? 882  ALA A CA    1 
ATOM   8025  C C     . ALA D 4 885  ? 125.200 150.930 155.925 1.00 50.26  ? 882  ALA A C     1 
ATOM   8026  O O     . ALA D 4 885  ? 126.157 151.415 155.316 1.00 50.26  ? 882  ALA A O     1 
ATOM   8027  C CB    . ALA D 4 885  ? 122.794 151.094 155.232 1.00 50.26  ? 882  ALA A CB    1 
ATOM   8028  N N     . ASN D 4 886  ? 125.236 149.711 156.469 1.00 50.26  ? 883  ASN A N     1 
ATOM   8029  C CA    . ASN D 4 886  ? 126.446 148.900 156.384 1.00 50.26  ? 883  ASN A CA    1 
ATOM   8030  C C     . ASN D 4 886  ? 126.769 148.524 154.943 1.00 50.26  ? 883  ASN A C     1 
ATOM   8031  O O     . ASN D 4 886  ? 127.935 148.557 154.534 1.00 50.26  ? 883  ASN A O     1 
ATOM   8032  C CB    . ASN D 4 886  ? 126.300 147.644 157.242 1.00 50.26  ? 883  ASN A CB    1 
ATOM   8033  C CG    . ASN D 4 886  ? 126.516 147.917 158.715 1.00 50.26  ? 883  ASN A CG    1 
ATOM   8034  O OD1   . ASN D 4 886  ? 125.730 148.618 159.350 1.00 50.26  ? 883  ASN A OD1   1 
ATOM   8035  N ND2   . ASN D 4 886  ? 127.589 147.364 159.267 1.00 50.26  ? 883  ASN A ND2   1 
ATOM   8036  N N     . SER D 4 887  ? 125.757 148.162 154.162 1.00 50.26  ? 884  SER A N     1 
ATOM   8037  C CA    . SER D 4 887  ? 125.947 147.732 152.787 1.00 50.26  ? 884  SER A CA    1 
ATOM   8038  C C     . SER D 4 887  ? 124.829 148.291 151.921 1.00 50.26  ? 884  SER A C     1 
ATOM   8039  O O     . SER D 4 887  ? 123.737 148.582 152.425 1.00 50.26  ? 884  SER A O     1 
ATOM   8040  C CB    . SER D 4 887  ? 125.970 146.199 152.681 1.00 50.26  ? 884  SER A CB    1 
ATOM   8041  O OG    . SER D 4 887  ? 127.159 145.672 153.242 1.00 50.26  ? 884  SER A OG    1 
ATOM   8042  N N     . PRO D 4 888  ? 125.072 148.461 150.623 1.00 50.26  ? 885  PRO A N     1 
ATOM   8043  C CA    . PRO D 4 888  ? 124.012 148.949 149.736 1.00 50.26  ? 885  PRO A CA    1 
ATOM   8044  C C     . PRO D 4 888  ? 122.864 147.958 149.641 1.00 50.26  ? 885  PRO A C     1 
ATOM   8045  O O     . PRO D 4 888  ? 123.049 146.742 149.736 1.00 50.26  ? 885  PRO A O     1 
ATOM   8046  C CB    . PRO D 4 888  ? 124.720 149.106 148.386 1.00 50.26  ? 885  PRO A CB    1 
ATOM   8047  C CG    . PRO D 4 888  ? 125.902 148.203 148.472 1.00 50.26  ? 885  PRO A CG    1 
ATOM   8048  C CD    . PRO D 4 888  ? 126.337 148.244 149.901 1.00 50.26  ? 885  PRO A CD    1 
ATOM   8049  N N     . SER D 4 889  ? 121.664 148.496 149.448 1.00 50.26  ? 886  SER A N     1 
ATOM   8050  C CA    . SER D 4 889  ? 120.440 147.703 149.371 1.00 50.26  ? 886  SER A CA    1 
ATOM   8051  C C     . SER D 4 889  ? 119.740 148.029 148.056 1.00 50.26  ? 886  SER A C     1 
ATOM   8052  O O     . SER D 4 889  ? 119.069 149.060 147.943 1.00 50.26  ? 886  SER A O     1 
ATOM   8053  C CB    . SER D 4 889  ? 119.535 147.978 150.568 1.00 50.26  ? 886  SER A CB    1 
ATOM   8054  O OG    . SER D 4 889  ? 120.273 147.960 151.778 1.00 50.26  ? 886  SER A OG    1 
ATOM   8055  N N     . LYS D 4 890  ? 119.897 147.144 147.070 1.00 50.26  ? 887  LYS A N     1 
ATOM   8056  C CA    . LYS D 4 890  ? 119.282 147.290 145.751 1.00 50.26  ? 887  LYS A CA    1 
ATOM   8057  C C     . LYS D 4 890  ? 119.658 148.631 145.117 1.00 50.26  ? 887  LYS A C     1 
ATOM   8058  O O     . LYS D 4 890  ? 118.810 149.466 144.796 1.00 50.26  ? 887  LYS A O     1 
ATOM   8059  C CB    . LYS D 4 890  ? 117.760 147.119 145.832 1.00 50.26  ? 887  LYS A CB    1 
ATOM   8060  C CG    . LYS D 4 890  ? 117.304 145.885 146.601 1.00 50.26  ? 887  LYS A CG    1 
ATOM   8061  C CD    . LYS D 4 890  ? 118.063 144.635 146.175 1.00 50.26  ? 887  LYS A CD    1 
ATOM   8062  C CE    . LYS D 4 890  ? 117.703 144.213 144.760 1.00 50.26  ? 887  LYS A CE    1 
ATOM   8063  N NZ    . LYS D 4 890  ? 118.566 143.096 144.284 1.00 50.26  ? 887  LYS A NZ    1 
ATOM   8064  N N     . PHE D 4 891  ? 120.968 148.822 144.951 1.00 50.26  ? 888  PHE A N     1 
ATOM   8065  C CA    . PHE D 4 891  ? 121.473 150.056 144.360 1.00 50.26  ? 888  PHE A CA    1 
ATOM   8066  C C     . PHE D 4 891  ? 121.004 150.214 142.920 1.00 50.26  ? 888  PHE A C     1 
ATOM   8067  O O     . PHE D 4 891  ? 120.608 151.310 142.500 1.00 50.26  ? 888  PHE A O     1 
ATOM   8068  C CB    . PHE D 4 891  ? 122.999 150.072 144.435 1.00 50.26  ? 888  PHE A CB    1 
ATOM   8069  C CG    . PHE D 4 891  ? 123.602 151.428 144.248 1.00 50.26  ? 888  PHE A CG    1 
ATOM   8070  C CD1   . PHE D 4 891  ? 123.933 151.884 142.987 1.00 50.26  ? 888  PHE A CD1   1 
ATOM   8071  C CD2   . PHE D 4 891  ? 123.838 152.248 145.334 1.00 50.26  ? 888  PHE A CD2   1 
ATOM   8072  C CE1   . PHE D 4 891  ? 124.489 153.130 142.814 1.00 50.26  ? 888  PHE A CE1   1 
ATOM   8073  C CE2   . PHE D 4 891  ? 124.393 153.495 145.165 1.00 50.26  ? 888  PHE A CE2   1 
ATOM   8074  C CZ    . PHE D 4 891  ? 124.718 153.937 143.904 1.00 50.26  ? 888  PHE A CZ    1 
ATOM   8075  N N     . ASN D 4 892  ? 121.041 149.126 142.147 1.00 50.26  ? 889  ASN A N     1 
ATOM   8076  C CA    . ASN D 4 892  ? 120.652 149.199 140.744 1.00 50.26  ? 889  ASN A CA    1 
ATOM   8077  C C     . ASN D 4 892  ? 119.189 149.582 140.585 1.00 50.26  ? 889  ASN A C     1 
ATOM   8078  O O     . ASN D 4 892  ? 118.835 150.277 139.629 1.00 50.26  ? 889  ASN A O     1 
ATOM   8079  C CB    . ASN D 4 892  ? 120.932 147.867 140.051 1.00 50.26  ? 889  ASN A CB    1 
ATOM   8080  C CG    . ASN D 4 892  ? 122.411 147.560 139.960 1.00 50.26  ? 889  ASN A CG    1 
ATOM   8081  O OD1   . ASN D 4 892  ? 123.251 148.416 140.232 1.00 50.26  ? 889  ASN A OD1   1 
ATOM   8082  N ND2   . ASN D 4 892  ? 122.738 146.333 139.575 1.00 50.26  ? 889  ASN A ND2   1 
ATOM   8083  N N     . GLN D 4 893  ? 118.324 149.140 141.500 1.00 50.26  ? 890  GLN A N     1 
ATOM   8084  C CA    . GLN D 4 893  ? 116.917 149.519 141.418 1.00 50.26  ? 890  GLN A CA    1 
ATOM   8085  C C     . GLN D 4 893  ? 116.737 151.021 141.607 1.00 50.26  ? 890  GLN A C     1 
ATOM   8086  O O     . GLN D 4 893  ? 115.957 151.655 140.887 1.00 50.26  ? 890  GLN A O     1 
ATOM   8087  C CB    . GLN D 4 893  ? 116.104 148.741 142.451 1.00 50.26  ? 890  GLN A CB    1 
ATOM   8088  C CG    . GLN D 4 893  ? 115.826 147.302 142.053 1.00 50.26  ? 890  GLN A CG    1 
ATOM   8089  C CD    . GLN D 4 893  ? 114.395 146.889 142.328 1.00 50.26  ? 890  GLN A CD    1 
ATOM   8090  O OE1   . GLN D 4 893  ? 113.821 147.244 143.357 1.00 50.26  ? 890  GLN A OE1   1 
ATOM   8091  N NE2   . GLN D 4 893  ? 113.808 146.136 141.404 1.00 50.26  ? 890  GLN A NE2   1 
ATOM   8092  N N     . ARG D 4 894  ? 117.454 151.608 142.567 1.00 50.26  ? 891  ARG A N     1 
ATOM   8093  C CA    . ARG D 4 894  ? 117.394 153.054 142.760 1.00 50.26  ? 891  ARG A CA    1 
ATOM   8094  C C     . ARG D 4 894  ? 117.948 153.794 141.549 1.00 50.26  ? 891  ARG A C     1 
ATOM   8095  O O     . ARG D 4 894  ? 117.395 154.818 141.125 1.00 50.26  ? 891  ARG A O     1 
ATOM   8096  C CB    . ARG D 4 894  ? 118.157 153.437 144.027 1.00 50.26  ? 891  ARG A CB    1 
ATOM   8097  C CG    . ARG D 4 894  ? 118.441 154.920 144.175 1.00 50.26  ? 891  ARG A CG    1 
ATOM   8098  C CD    . ARG D 4 894  ? 119.303 155.181 145.397 1.00 50.26  ? 891  ARG A CD    1 
ATOM   8099  N NE    . ARG D 4 894  ? 119.203 156.562 145.853 1.00 50.26  ? 891  ARG A NE    1 
ATOM   8100  C CZ    . ARG D 4 894  ? 118.414 156.969 146.838 1.00 50.26  ? 891  ARG A CZ    1 
ATOM   8101  N NH1   . ARG D 4 894  ? 117.635 156.124 147.493 1.00 50.26  ? 891  ARG A NH1   1 
ATOM   8102  N NH2   . ARG D 4 894  ? 118.407 158.256 147.174 1.00 50.26  ? 891  ARG A NH2   1 
ATOM   8103  N N     . VAL D 4 895  ? 119.043 153.287 140.979 1.00 50.26  ? 892  VAL A N     1 
ATOM   8104  C CA    . VAL D 4 895  ? 119.604 153.881 139.767 1.00 50.26  ? 892  VAL A CA    1 
ATOM   8105  C C     . VAL D 4 895  ? 118.580 153.865 138.640 1.00 50.26  ? 892  VAL A C     1 
ATOM   8106  O O     . VAL D 4 895  ? 118.380 154.867 137.942 1.00 50.26  ? 892  VAL A O     1 
ATOM   8107  C CB    . VAL D 4 895  ? 120.893 153.146 139.365 1.00 50.26  ? 892  VAL A CB    1 
ATOM   8108  C CG1   . VAL D 4 895  ? 121.331 153.573 137.986 1.00 50.26  ? 892  VAL A CG1   1 
ATOM   8109  C CG2   . VAL D 4 895  ? 121.987 153.432 140.370 1.00 50.26  ? 892  VAL A CG2   1 
ATOM   8110  N N     . ASN D 4 896  ? 117.924 152.722 138.440 1.00 50.26  ? 893  ASN A N     1 
ATOM   8111  C CA    . ASN D 4 896  ? 116.943 152.602 137.370 1.00 50.26  ? 893  ASN A CA    1 
ATOM   8112  C C     . ASN D 4 896  ? 115.746 153.510 137.614 1.00 50.26  ? 893  ASN A C     1 
ATOM   8113  O O     . ASN D 4 896  ? 115.200 154.088 136.670 1.00 50.26  ? 893  ASN A O     1 
ATOM   8114  C CB    . ASN D 4 896  ? 116.501 151.148 137.228 1.00 50.26  ? 893  ASN A CB    1 
ATOM   8115  C CG    . ASN D 4 896  ? 117.647 150.227 136.871 1.00 50.26  ? 893  ASN A CG    1 
ATOM   8116  O OD1   . ASN D 4 896  ? 118.755 150.679 136.586 1.00 50.26  ? 893  ASN A OD1   1 
ATOM   8117  N ND2   . ASN D 4 896  ? 117.387 148.925 136.886 1.00 50.26  ? 893  ASN A ND2   1 
ATOM   8118  N N     . ALA D 4 897  ? 115.321 153.644 138.872 1.00 50.26  ? 894  ALA A N     1 
ATOM   8119  C CA    . ALA D 4 897  ? 114.222 154.551 139.185 1.00 50.26  ? 894  ALA A CA    1 
ATOM   8120  C C     . ALA D 4 897  ? 114.592 155.991 138.851 1.00 50.26  ? 894  ALA A C     1 
ATOM   8121  O O     . ALA D 4 897  ? 113.800 156.725 138.245 1.00 50.26  ? 894  ALA A O     1 
ATOM   8122  C CB    . ALA D 4 897  ? 113.838 154.420 140.658 1.00 50.26  ? 894  ALA A CB    1 
ATOM   8123  N N     . TYR D 4 898  ? 115.803 156.408 139.229 1.00 50.26  ? 895  TYR A N     1 
ATOM   8124  C CA    . TYR D 4 898  ? 116.241 157.764 138.909 1.00 50.26  ? 895  TYR A CA    1 
ATOM   8125  C C     . TYR D 4 898  ? 116.317 157.978 137.404 1.00 50.26  ? 895  TYR A C     1 
ATOM   8126  O O     . TYR D 4 898  ? 115.906 159.028 136.897 1.00 50.26  ? 895  TYR A O     1 
ATOM   8127  C CB    . TYR D 4 898  ? 117.596 158.052 139.552 1.00 50.26  ? 895  TYR A CB    1 
ATOM   8128  C CG    . TYR D 4 898  ? 118.281 159.273 138.980 1.00 50.26  ? 895  TYR A CG    1 
ATOM   8129  C CD1   . TYR D 4 898  ? 117.872 160.550 139.334 1.00 50.26  ? 895  TYR A CD1   1 
ATOM   8130  C CD2   . TYR D 4 898  ? 119.333 159.149 138.084 1.00 50.26  ? 895  TYR A CD2   1 
ATOM   8131  C CE1   . TYR D 4 898  ? 118.492 161.668 138.814 1.00 50.26  ? 895  TYR A CE1   1 
ATOM   8132  C CE2   . TYR D 4 898  ? 119.957 160.262 137.558 1.00 50.26  ? 895  TYR A CE2   1 
ATOM   8133  C CZ    . TYR D 4 898  ? 119.532 161.518 137.927 1.00 50.26  ? 895  TYR A CZ    1 
ATOM   8134  O OH    . TYR D 4 898  ? 120.151 162.630 137.407 1.00 50.26  ? 895  TYR A OH    1 
ATOM   8135  N N     . LEU D 4 899  ? 116.848 156.996 136.673 1.00 50.26  ? 896  LEU A N     1 
ATOM   8136  C CA    . LEU D 4 899  ? 116.961 157.131 135.225 1.00 50.26  ? 896  LEU A CA    1 
ATOM   8137  C C     . LEU D 4 899  ? 115.590 157.196 134.564 1.00 50.26  ? 896  LEU A C     1 
ATOM   8138  O O     . LEU D 4 899  ? 115.385 157.974 133.625 1.00 50.26  ? 896  LEU A O     1 
ATOM   8139  C CB    . LEU D 4 899  ? 117.782 155.976 134.654 1.00 50.26  ? 896  LEU A CB    1 
ATOM   8140  C CG    . LEU D 4 899  ? 119.286 156.044 134.918 1.00 50.26  ? 896  LEU A CG    1 
ATOM   8141  C CD1   . LEU D 4 899  ? 119.952 154.730 134.560 1.00 50.26  ? 896  LEU A CD1   1 
ATOM   8142  C CD2   . LEU D 4 899  ? 119.912 157.190 134.145 1.00 50.26  ? 896  LEU A CD2   1 
ATOM   8143  N N     . LYS D 4 900  ? 114.642 156.382 135.032 1.00 50.26  ? 897  LYS A N     1 
ATOM   8144  C CA    . LYS D 4 900  ? 113.293 156.415 134.479 1.00 50.26  ? 897  LYS A CA    1 
ATOM   8145  C C     . LYS D 4 900  ? 112.612 157.747 134.759 1.00 50.26  ? 897  LYS A C     1 
ATOM   8146  O O     . LYS D 4 900  ? 111.917 158.288 133.892 1.00 50.26  ? 897  LYS A O     1 
ATOM   8147  C CB    . LYS D 4 900  ? 112.465 155.262 135.042 1.00 50.26  ? 897  LYS A CB    1 
ATOM   8148  C CG    . LYS D 4 900  ? 112.289 154.100 134.084 1.00 50.26  ? 897  LYS A CG    1 
ATOM   8149  C CD    . LYS D 4 900  ? 111.533 152.958 134.740 1.00 50.26  ? 897  LYS A CD    1 
ATOM   8150  C CE    . LYS D 4 900  ? 110.075 153.321 134.969 1.00 50.26  ? 897  LYS A CE    1 
ATOM   8151  N NZ    . LYS D 4 900  ? 109.363 152.287 135.771 1.00 50.26  ? 897  LYS A NZ    1 
ATOM   8152  N N     . GLU D 4 901  ? 112.793 158.290 135.962 1.00 50.26  ? 898  GLU A N     1 
ATOM   8153  C CA    . GLU D 4 901  ? 112.182 159.573 136.283 1.00 50.26  ? 898  GLU A CA    1 
ATOM   8154  C C     . GLU D 4 901  ? 112.900 160.744 135.619 1.00 50.26  ? 898  GLU A C     1 
ATOM   8155  O O     . GLU D 4 901  ? 112.355 161.852 135.595 1.00 50.26  ? 898  GLU A O     1 
ATOM   8156  C CB    . GLU D 4 901  ? 112.139 159.759 137.803 1.00 50.26  ? 898  GLU A CB    1 
ATOM   8157  C CG    . GLU D 4 901  ? 111.052 160.704 138.304 1.00 50.26  ? 898  GLU A CG    1 
ATOM   8158  C CD    . GLU D 4 901  ? 111.499 162.148 138.369 1.00 50.26  ? 898  GLU A CD    1 
ATOM   8159  O OE1   . GLU D 4 901  ? 112.707 162.384 138.558 1.00 50.26  ? 898  GLU A OE1   1 
ATOM   8160  O OE2   . GLU D 4 901  ? 110.643 163.046 138.232 1.00 50.26  ? 898  GLU A OE2   1 
ATOM   8161  N N     . HIS D 4 902  ? 114.089 160.521 135.057 1.00 50.26  ? 899  HIS A N     1 
ATOM   8162  C CA    . HIS D 4 902  ? 114.850 161.547 134.342 1.00 50.26  ? 899  HIS A CA    1 
ATOM   8163  C C     . HIS D 4 902  ? 115.176 161.021 132.952 1.00 50.26  ? 899  HIS A C     1 
ATOM   8164  O O     . HIS D 4 902  ? 116.297 160.560 132.696 1.00 50.26  ? 899  HIS A O     1 
ATOM   8165  C CB    . HIS D 4 902  ? 116.133 161.918 135.086 1.00 50.26  ? 899  HIS A CB    1 
ATOM   8166  C CG    . HIS D 4 902  ? 115.914 162.782 136.288 1.00 50.26  ? 899  HIS A CG    1 
ATOM   8167  N ND1   . HIS D 4 902  ? 115.618 162.268 137.531 1.00 50.26  ? 899  HIS A ND1   1 
ATOM   8168  C CD2   . HIS D 4 902  ? 115.960 164.127 136.437 1.00 50.26  ? 899  HIS A CD2   1 
ATOM   8169  C CE1   . HIS D 4 902  ? 115.490 163.259 138.395 1.00 50.26  ? 899  HIS A CE1   1 
ATOM   8170  N NE2   . HIS D 4 902  ? 115.689 164.397 137.756 1.00 50.26  ? 899  HIS A NE2   1 
ATOM   8171  N N     . PRO D 4 903  ? 114.218 161.076 132.022 1.00 50.26  ? 900  PRO A N     1 
ATOM   8172  C CA    . PRO D 4 903  ? 114.455 160.512 130.683 1.00 50.26  ? 900  PRO A CA    1 
ATOM   8173  C C     . PRO D 4 903  ? 115.478 161.275 129.858 1.00 50.26  ? 900  PRO A C     1 
ATOM   8174  O O     . PRO D 4 903  ? 115.908 160.759 128.819 1.00 50.26  ? 900  PRO A O     1 
ATOM   8175  C CB    . PRO D 4 903  ? 113.068 160.570 130.025 1.00 50.26  ? 900  PRO A CB    1 
ATOM   8176  C CG    . PRO D 4 903  ? 112.100 160.782 131.153 1.00 50.26  ? 900  PRO A CG    1 
ATOM   8177  C CD    . PRO D 4 903  ? 112.845 161.577 132.172 1.00 50.26  ? 900  PRO A CD    1 
ATOM   8178  N N     . GLU D 4 904  ? 115.882 162.473 130.276 1.00 50.26  ? 901  GLU A N     1 
ATOM   8179  C CA    . GLU D 4 904  ? 116.801 163.300 129.507 1.00 50.26  ? 901  GLU A CA    1 
ATOM   8180  C C     . GLU D 4 904  ? 118.246 163.173 129.972 1.00 50.26  ? 901  GLU A C     1 
ATOM   8181  O O     . GLU D 4 904  ? 119.086 163.983 129.570 1.00 50.26  ? 901  GLU A O     1 
ATOM   8182  C CB    . GLU D 4 904  ? 116.365 164.765 129.567 1.00 50.26  ? 901  GLU A CB    1 
ATOM   8183  C CG    . GLU D 4 904  ? 116.285 165.328 130.973 1.00 50.26  ? 901  GLU A CG    1 
ATOM   8184  C CD    . GLU D 4 904  ? 116.172 166.838 130.988 1.00 50.26  ? 901  GLU A CD    1 
ATOM   8185  O OE1   . GLU D 4 904  ? 115.921 167.427 129.916 1.00 50.26  ? 901  GLU A OE1   1 
ATOM   8186  O OE2   . GLU D 4 904  ? 116.333 167.437 132.072 1.00 50.26  ? 901  GLU A OE2   1 
ATOM   8187  N N     . THR D 4 905  ? 118.551 162.190 130.806 1.00 50.26  ? 902  THR A N     1 
ATOM   8188  C CA    . THR D 4 905  ? 119.917 162.003 131.285 1.00 50.26  ? 902  THR A CA    1 
ATOM   8189  C C     . THR D 4 905  ? 120.826 161.614 130.127 1.00 50.26  ? 902  THR A C     1 
ATOM   8190  O O     . THR D 4 905  ? 120.539 160.632 129.431 1.00 50.26  ? 902  THR A O     1 
ATOM   8191  C CB    . THR D 4 905  ? 119.957 160.932 132.371 1.00 50.26  ? 902  THR A CB    1 
ATOM   8192  O OG1   . THR D 4 905  ? 119.214 161.380 133.511 1.00 50.26  ? 902  THR A OG1   1 
ATOM   8193  C CG2   . THR D 4 905  ? 121.389 160.650 132.787 1.00 50.26  ? 902  THR A CG2   1 
ATOM   8194  N N     . PRO D 4 906  ? 121.913 162.339 129.882 1.00 50.26  ? 903  PRO A N     1 
ATOM   8195  C CA    . PRO D 4 906  ? 122.780 162.013 128.745 1.00 50.26  ? 903  PRO A CA    1 
ATOM   8196  C C     . PRO D 4 906  ? 123.592 160.754 129.005 1.00 50.26  ? 903  PRO A C     1 
ATOM   8197  O O     . PRO D 4 906  ? 123.603 160.189 130.099 1.00 50.26  ? 903  PRO A O     1 
ATOM   8198  C CB    . PRO D 4 906  ? 123.679 163.245 128.614 1.00 50.26  ? 903  PRO A CB    1 
ATOM   8199  C CG    . PRO D 4 906  ? 123.667 163.870 129.956 1.00 50.26  ? 903  PRO A CG    1 
ATOM   8200  C CD    . PRO D 4 906  ? 122.339 163.564 130.577 1.00 50.26  ? 903  PRO A CD    1 
ATOM   8201  N N     . ILE D 4 907  ? 124.284 160.316 127.956 1.00 50.26  ? 904  ILE A N     1 
ATOM   8202  C CA    . ILE D 4 907  ? 125.062 159.086 127.968 1.00 50.26  ? 904  ILE A CA    1 
ATOM   8203  C C     . ILE D 4 907  ? 126.522 159.444 127.731 1.00 50.26  ? 904  ILE A C     1 
ATOM   8204  O O     . ILE D 4 907  ? 126.836 160.344 126.946 1.00 50.26  ? 904  ILE A O     1 
ATOM   8205  C CB    . ILE D 4 907  ? 124.570 158.096 126.889 1.00 50.26  ? 904  ILE A CB    1 
ATOM   8206  C CG1   . ILE D 4 907  ? 123.065 157.856 127.009 1.00 50.26  ? 904  ILE A CG1   1 
ATOM   8207  C CG2   . ILE D 4 907  ? 125.306 156.776 127.001 1.00 50.26  ? 904  ILE A CG2   1 
ATOM   8208  C CD1   . ILE D 4 907  ? 122.642 157.237 128.300 1.00 50.26  ? 904  ILE A CD1   1 
ATOM   8209  N N     . ILE D 4 908  ? 127.419 158.737 128.414 1.00 50.26  ? 905  ILE A N     1 
ATOM   8210  C CA    . ILE D 4 908  ? 128.857 158.880 128.213 1.00 50.26  ? 905  ILE A CA    1 
ATOM   8211  C C     . ILE D 4 908  ? 129.405 157.549 127.723 1.00 50.26  ? 905  ILE A C     1 
ATOM   8212  O O     . ILE D 4 908  ? 129.222 156.518 128.380 1.00 50.26  ? 905  ILE A O     1 
ATOM   8213  C CB    . ILE D 4 908  ? 129.579 159.324 129.498 1.00 50.26  ? 905  ILE A CB    1 
ATOM   8214  C CG1   . ILE D 4 908  ? 129.005 160.645 130.005 1.00 50.26  ? 905  ILE A CG1   1 
ATOM   8215  C CG2   . ILE D 4 908  ? 131.070 159.452 129.250 1.00 50.26  ? 905  ILE A CG2   1 
ATOM   8216  C CD1   . ILE D 4 908  ? 129.784 161.249 131.146 1.00 50.26  ? 905  ILE A CD1   1 
ATOM   8217  N N     . GLY D 4 909  ? 130.076 157.572 126.576 1.00 50.26  ? 906  GLY A N     1 
ATOM   8218  C CA    . GLY D 4 909  ? 130.651 156.380 125.980 1.00 50.26  ? 906  GLY A CA    1 
ATOM   8219  C C     . GLY D 4 909  ? 132.165 156.495 125.911 1.00 50.26  ? 906  GLY A C     1 
ATOM   8220  O O     . GLY D 4 909  ? 132.699 157.504 125.449 1.00 50.26  ? 906  GLY A O     1 
ATOM   8221  N N     . ILE D 4 910  ? 132.840 155.449 126.377 1.00 50.26  ? 907  ILE A N     1 
ATOM   8222  C CA    . ILE D 4 910  ? 134.297 155.400 126.422 1.00 50.26  ? 907  ILE A CA    1 
ATOM   8223  C C     . ILE D 4 910  ? 134.759 154.226 125.575 1.00 50.26  ? 907  ILE A C     1 
ATOM   8224  O O     . ILE D 4 910  ? 134.326 153.088 125.793 1.00 50.26  ? 907  ILE A O     1 
ATOM   8225  C CB    . ILE D 4 910  ? 134.818 155.272 127.859 1.00 50.26  ? 907  ILE A CB    1 
ATOM   8226  C CG1   . ILE D 4 910  ? 134.326 156.444 128.701 1.00 50.26  ? 907  ILE A CG1   1 
ATOM   8227  C CG2   . ILE D 4 910  ? 136.333 155.206 127.873 1.00 50.26  ? 907  ILE A CG2   1 
ATOM   8228  C CD1   . ILE D 4 910  ? 134.158 156.100 130.144 1.00 50.26  ? 907  ILE A CD1   1 
ATOM   8229  N N     . ASP D 4 911  ? 135.638 154.500 124.616 1.00 50.26  ? 908  ASP A N     1 
ATOM   8230  C CA    . ASP D 4 911  ? 136.206 153.472 123.761 1.00 50.26  ? 908  ASP A CA    1 
ATOM   8231  C C     . ASP D 4 911  ? 137.710 153.669 123.658 1.00 50.26  ? 908  ASP A C     1 
ATOM   8232  O O     . ASP D 4 911  ? 138.206 154.798 123.658 1.00 50.26  ? 908  ASP A O     1 
ATOM   8233  C CB    . ASP D 4 911  ? 135.584 153.495 122.361 1.00 50.26  ? 908  ASP A CB    1 
ATOM   8234  C CG    . ASP D 4 911  ? 135.880 152.236 121.571 1.00 50.26  ? 908  ASP A CG    1 
ATOM   8235  O OD1   . ASP D 4 911  ? 136.219 151.208 122.193 1.00 50.26  ? 908  ASP A OD1   1 
ATOM   8236  O OD2   . ASP D 4 911  ? 135.777 152.273 120.327 1.00 50.26  ? 908  ASP A OD2   1 
ATOM   8237  N N     . ARG D 4 912  ? 138.431 152.556 123.570 1.00 50.26  ? 909  ARG A N     1 
ATOM   8238  C CA    . ARG D 4 912  ? 139.877 152.576 123.389 1.00 50.26  ? 909  ARG A CA    1 
ATOM   8239  C C     . ARG D 4 912  ? 140.172 152.698 121.901 1.00 50.26  ? 909  ARG A C     1 
ATOM   8240  O O     . ARG D 4 912  ? 139.951 151.754 121.136 1.00 50.26  ? 909  ARG A O     1 
ATOM   8241  C CB    . ARG D 4 912  ? 140.513 151.317 123.969 1.00 50.26  ? 909  ARG A CB    1 
ATOM   8242  C CG    . ARG D 4 912  ? 140.285 151.127 125.451 1.00 50.26  ? 909  ARG A CG    1 
ATOM   8243  C CD    . ARG D 4 912  ? 140.599 149.702 125.861 1.00 50.26  ? 909  ARG A CD    1 
ATOM   8244  N NE    . ARG D 4 912  ? 139.502 148.794 125.556 1.00 50.26  ? 909  ARG A NE    1 
ATOM   8245  C CZ    . ARG D 4 912  ? 139.582 147.473 125.635 1.00 50.26  ? 909  ARG A CZ    1 
ATOM   8246  N NH1   . ARG D 4 912  ? 140.702 146.870 125.997 1.00 50.26  ? 909  ARG A NH1   1 
ATOM   8247  N NH2   . ARG D 4 912  ? 138.513 146.740 125.341 1.00 50.26  ? 909  ARG A NH2   1 
ATOM   8248  N N     . GLY D 4 913  ? 140.671 153.858 121.488 1.00 50.26  ? 910  GLY A N     1 
ATOM   8249  C CA    . GLY D 4 913  ? 140.991 154.085 120.099 1.00 50.26  ? 910  GLY A CA    1 
ATOM   8250  C C     . GLY D 4 913  ? 142.343 153.521 119.716 1.00 50.26  ? 910  GLY A C     1 
ATOM   8251  O O     . GLY D 4 913  ? 143.048 152.896 120.508 1.00 50.26  ? 910  GLY A O     1 
ATOM   8252  N N     . GLU D 4 914  ? 142.707 153.751 118.457 1.00 50.26  ? 911  GLU A N     1 
ATOM   8253  C CA    . GLU D 4 914  ? 143.997 153.329 117.932 1.00 50.26  ? 911  GLU A CA    1 
ATOM   8254  C C     . GLU D 4 914  ? 144.963 154.479 117.712 1.00 50.26  ? 911  GLU A C     1 
ATOM   8255  O O     . GLU D 4 914  ? 146.169 154.296 117.889 1.00 50.26  ? 911  GLU A O     1 
ATOM   8256  C CB    . GLU D 4 914  ? 143.811 152.569 116.614 1.00 50.26  ? 911  GLU A CB    1 
ATOM   8257  C CG    . GLU D 4 914  ? 142.890 151.365 116.734 1.00 50.26  ? 911  GLU A CG    1 
ATOM   8258  C CD    . GLU D 4 914  ? 142.817 150.551 115.460 1.00 50.26  ? 911  GLU A CD    1 
ATOM   8259  O OE1   . GLU D 4 914  ? 143.614 150.815 114.536 1.00 50.26  ? 911  GLU A OE1   1 
ATOM   8260  O OE2   . GLU D 4 914  ? 141.961 149.645 115.382 1.00 50.26  ? 911  GLU A OE2   1 
ATOM   8261  N N     . ARG D 4 915  ? 144.467 155.654 117.331 1.00 50.26  ? 912  ARG A N     1 
ATOM   8262  C CA    . ARG D 4 915  ? 145.280 156.858 117.262 1.00 50.26  ? 912  ARG A CA    1 
ATOM   8263  C C     . ARG D 4 915  ? 145.227 157.666 118.550 1.00 50.26  ? 912  ARG A C     1 
ATOM   8264  O O     . ARG D 4 915  ? 145.852 158.727 118.629 1.00 50.26  ? 912  ARG A O     1 
ATOM   8265  C CB    . ARG D 4 915  ? 144.842 157.731 116.083 1.00 50.26  ? 912  ARG A CB    1 
ATOM   8266  C CG    . ARG D 4 915  ? 145.396 157.280 114.740 1.00 50.26  ? 912  ARG A CG    1 
ATOM   8267  C CD    . ARG D 4 915  ? 146.693 157.997 114.390 1.00 50.26  ? 912  ARG A CD    1 
ATOM   8268  N NE    . ARG D 4 915  ? 147.784 157.654 115.295 1.00 50.26  ? 912  ARG A NE    1 
ATOM   8269  C CZ    . ARG D 4 915  ? 148.451 156.507 115.269 1.00 50.26  ? 912  ARG A CZ    1 
ATOM   8270  N NH1   . ARG D 4 915  ? 148.164 155.559 114.391 1.00 50.26  ? 912  ARG A NH1   1 
ATOM   8271  N NH2   . ARG D 4 915  ? 149.430 156.306 116.146 1.00 50.26  ? 912  ARG A NH2   1 
ATOM   8272  N N     . ASN D 4 916  ? 144.484 157.196 119.549 1.00 50.26  ? 913  ASN A N     1 
ATOM   8273  C CA    . ASN D 4 916  ? 144.467 157.798 120.873 1.00 50.26  ? 913  ASN A CA    1 
ATOM   8274  C C     . ASN D 4 916  ? 144.074 156.727 121.879 1.00 50.26  ? 913  ASN A C     1 
ATOM   8275  O O     . ASN D 4 916  ? 143.298 155.820 121.566 1.00 50.26  ? 913  ASN A O     1 
ATOM   8276  C CB    . ASN D 4 916  ? 143.516 158.999 120.938 1.00 50.26  ? 913  ASN A CB    1 
ATOM   8277  C CG    . ASN D 4 916  ? 142.199 158.742 120.240 1.00 50.26  ? 913  ASN A CG    1 
ATOM   8278  O OD1   . ASN D 4 916  ? 141.573 157.701 120.430 1.00 50.26  ? 913  ASN A OD1   1 
ATOM   8279  N ND2   . ASN D 4 916  ? 141.770 159.695 119.423 1.00 50.26  ? 913  ASN A ND2   1 
ATOM   8280  N N     . LEU D 4 917  ? 144.628 156.831 123.088 1.00 50.26  ? 914  LEU A N     1 
ATOM   8281  C CA    . LEU D 4 917  ? 144.448 155.775 124.080 1.00 50.26  ? 914  LEU A CA    1 
ATOM   8282  C C     . LEU D 4 917  ? 142.989 155.642 124.501 1.00 50.26  ? 914  LEU A C     1 
ATOM   8283  O O     . LEU D 4 917  ? 142.419 154.546 124.465 1.00 50.26  ? 914  LEU A O     1 
ATOM   8284  C CB    . LEU D 4 917  ? 145.339 156.038 125.295 1.00 50.26  ? 914  LEU A CB    1 
ATOM   8285  C CG    . LEU D 4 917  ? 146.850 155.966 125.085 1.00 50.26  ? 914  LEU A CG    1 
ATOM   8286  C CD1   . LEU D 4 917  ? 147.608 156.382 126.326 1.00 50.26  ? 914  LEU A CD1   1 
ATOM   8287  C CD2   . LEU D 4 917  ? 147.249 154.565 124.670 1.00 50.26  ? 914  LEU A CD2   1 
ATOM   8288  N N     . ILE D 4 918  ? 142.368 156.743 124.910 1.00 50.26  ? 915  ILE A N     1 
ATOM   8289  C CA    . ILE D 4 918  ? 140.981 156.741 125.357 1.00 50.26  ? 915  ILE A CA    1 
ATOM   8290  C C     . ILE D 4 918  ? 140.257 157.881 124.660 1.00 50.26  ? 915  ILE A C     1 
ATOM   8291  O O     . ILE D 4 918  ? 140.722 159.026 124.693 1.00 50.26  ? 915  ILE A O     1 
ATOM   8292  C CB    . ILE D 4 918  ? 140.866 156.881 126.884 1.00 50.26  ? 915  ILE A CB    1 
ATOM   8293  C CG1   . ILE D 4 918  ? 141.369 155.615 127.577 1.00 50.26  ? 915  ILE A CG1   1 
ATOM   8294  C CG2   . ILE D 4 918  ? 139.431 157.164 127.288 1.00 50.26  ? 915  ILE A CG2   1 
ATOM   8295  C CD1   . ILE D 4 918  ? 140.499 154.409 127.338 1.00 50.26  ? 915  ILE A CD1   1 
ATOM   8296  N N     . TYR D 4 919  ? 139.125 157.574 124.034 1.00 50.26  ? 916  TYR A N     1 
ATOM   8297  C CA    . TYR D 4 919  ? 138.310 158.583 123.380 1.00 50.26  ? 916  TYR A CA    1 
ATOM   8298  C C     . TYR D 4 919  ? 136.909 158.521 123.967 1.00 50.26  ? 916  TYR A C     1 
ATOM   8299  O O     . TYR D 4 919  ? 136.384 157.433 124.220 1.00 50.26  ? 916  TYR A O     1 
ATOM   8300  C CB    . TYR D 4 919  ? 138.245 158.369 121.869 1.00 50.26  ? 916  TYR A CB    1 
ATOM   8301  C CG    . TYR D 4 919  ? 137.996 159.644 121.103 1.00 50.26  ? 916  TYR A CG    1 
ATOM   8302  C CD1   . TYR D 4 919  ? 138.824 160.738 121.269 1.00 50.26  ? 916  TYR A CD1   1 
ATOM   8303  C CD2   . TYR D 4 919  ? 136.979 159.737 120.175 1.00 50.26  ? 916  TYR A CD2   1 
ATOM   8304  C CE1   . TYR D 4 919  ? 138.621 161.904 120.563 1.00 50.26  ? 916  TYR A CE1   1 
ATOM   8305  C CE2   . TYR D 4 919  ? 136.765 160.905 119.472 1.00 50.26  ? 916  TYR A CE2   1 
ATOM   8306  C CZ    . TYR D 4 919  ? 137.591 161.981 119.665 1.00 50.26  ? 916  TYR A CZ    1 
ATOM   8307  O OH    . TYR D 4 919  ? 137.384 163.142 118.958 1.00 50.26  ? 916  TYR A OH    1 
ATOM   8308  N N     . ILE D 4 920  ? 136.304 159.686 124.183 1.00 50.26  ? 917  ILE A N     1 
ATOM   8309  C CA    . ILE D 4 920  ? 135.008 159.788 124.841 1.00 50.26  ? 917  ILE A CA    1 
ATOM   8310  C C     . ILE D 4 920  ? 134.093 160.701 124.037 1.00 50.26  ? 917  ILE A C     1 
ATOM   8311  O O     . ILE D 4 920  ? 134.522 161.744 123.531 1.00 50.26  ? 917  ILE A O     1 
ATOM   8312  C CB    . ILE D 4 920  ? 135.148 160.294 126.293 1.00 50.26  ? 917  ILE A CB    1 
ATOM   8313  C CG1   . ILE D 4 920  ? 135.757 161.696 126.318 1.00 50.26  ? 917  ILE A CG1   1 
ATOM   8314  C CG2   . ILE D 4 920  ? 135.962 159.322 127.126 1.00 50.26  ? 917  ILE A CG2   1 
ATOM   8315  C CD1   . ILE D 4 920  ? 135.719 162.353 127.668 1.00 50.26  ? 917  ILE A CD1   1 
ATOM   8316  N N     . THR D 4 921  ? 132.836 160.287 123.897 1.00 50.26  ? 918  THR A N     1 
ATOM   8317  C CA    . THR D 4 921  ? 131.782 161.113 123.327 1.00 50.26  ? 918  THR A CA    1 
ATOM   8318  C C     . THR D 4 921  ? 130.553 161.023 124.218 1.00 50.26  ? 918  THR A C     1 
ATOM   8319  O O     . THR D 4 921  ? 130.246 159.965 124.771 1.00 50.26  ? 918  THR A O     1 
ATOM   8320  C CB    . THR D 4 921  ? 131.397 160.686 121.902 1.00 50.26  ? 918  THR A CB    1 
ATOM   8321  O OG1   . THR D 4 921  ? 130.601 159.497 121.958 1.00 50.26  ? 918  THR A OG1   1 
ATOM   8322  C CG2   . THR D 4 921  ? 132.631 160.432 121.051 1.00 50.26  ? 918  THR A CG2   1 
ATOM   8323  N N     . VAL D 4 922  ? 129.848 162.143 124.350 1.00 50.26  ? 919  VAL A N     1 
ATOM   8324  C CA    . VAL D 4 922  ? 128.642 162.224 125.164 1.00 50.26  ? 919  VAL A CA    1 
ATOM   8325  C C     . VAL D 4 922  ? 127.469 162.555 124.253 1.00 50.26  ? 919  VAL A C     1 
ATOM   8326  O O     . VAL D 4 922  ? 127.566 163.451 123.406 1.00 50.26  ? 919  VAL A O     1 
ATOM   8327  C CB    . VAL D 4 922  ? 128.783 163.261 126.294 1.00 50.26  ? 919  VAL A CB    1 
ATOM   8328  C CG1   . VAL D 4 922  ? 129.802 162.790 127.306 1.00 50.26  ? 919  VAL A CG1   1 
ATOM   8329  C CG2   . VAL D 4 922  ? 129.199 164.605 125.745 1.00 50.26  ? 919  VAL A CG2   1 
ATOM   8330  N N     . ILE D 4 923  ? 126.374 161.819 124.411 1.00 50.26  ? 920  ILE A N     1 
ATOM   8331  C CA    . ILE D 4 923  ? 125.184 162.016 123.596 1.00 50.26  ? 920  ILE A CA    1 
ATOM   8332  C C     . ILE D 4 923  ? 124.006 162.316 124.509 1.00 50.26  ? 920  ILE A C     1 
ATOM   8333  O O     . ILE D 4 923  ? 123.914 161.805 125.629 1.00 50.26  ? 920  ILE A O     1 
ATOM   8334  C CB    . ILE D 4 923  ? 124.880 160.796 122.702 1.00 50.26  ? 920  ILE A CB    1 
ATOM   8335  C CG1   . ILE D 4 923  ? 124.732 159.535 123.550 1.00 50.26  ? 920  ILE A CG1   1 
ATOM   8336  C CG2   . ILE D 4 923  ? 125.975 160.608 121.672 1.00 50.26  ? 920  ILE A CG2   1 
ATOM   8337  C CD1   . ILE D 4 923  ? 124.149 158.367 122.796 1.00 50.26  ? 920  ILE A CD1   1 
ATOM   8338  N N     . ASP D 4 924  ? 123.101 163.157 124.020 1.00 50.26  ? 921  ASP A N     1 
ATOM   8339  C CA    . ASP D 4 924  ? 121.910 163.524 124.771 1.00 50.26  ? 921  ASP A CA    1 
ATOM   8340  C C     . ASP D 4 924  ? 120.835 162.456 124.573 1.00 50.26  ? 921  ASP A C     1 
ATOM   8341  O O     . ASP D 4 924  ? 121.095 161.361 124.067 1.00 50.26  ? 921  ASP A O     1 
ATOM   8342  C CB    . ASP D 4 924  ? 121.435 164.915 124.359 1.00 50.26  ? 921  ASP A CB    1 
ATOM   8343  C CG    . ASP D 4 924  ? 121.255 165.051 122.862 1.00 50.26  ? 921  ASP A CG    1 
ATOM   8344  O OD1   . ASP D 4 924  ? 121.532 164.076 122.134 1.00 50.26  ? 921  ASP A OD1   1 
ATOM   8345  O OD2   . ASP D 4 924  ? 120.839 166.139 122.411 1.00 50.26  ? 921  ASP A OD2   1 
ATOM   8346  N N     . SER D 4 925  ? 119.603 162.767 124.983 1.00 50.26  ? 922  SER A N     1 
ATOM   8347  C CA    . SER D 4 925  ? 118.521 161.793 124.883 1.00 50.26  ? 922  SER A CA    1 
ATOM   8348  C C     . SER D 4 925  ? 118.193 161.452 123.435 1.00 50.26  ? 922  SER A C     1 
ATOM   8349  O O     . SER D 4 925  ? 117.772 160.327 123.145 1.00 50.26  ? 922  SER A O     1 
ATOM   8350  C CB    . SER D 4 925  ? 117.277 162.320 125.597 1.00 50.26  ? 922  SER A CB    1 
ATOM   8351  O OG    . SER D 4 925  ? 116.122 161.600 125.203 1.00 50.26  ? 922  SER A OG    1 
ATOM   8352  N N     . THR D 4 926  ? 118.375 162.398 122.517 1.00 50.26  ? 923  THR A N     1 
ATOM   8353  C CA    . THR D 4 926  ? 118.025 162.194 121.118 1.00 50.26  ? 923  THR A CA    1 
ATOM   8354  C C     . THR D 4 926  ? 119.174 161.640 120.286 1.00 50.26  ? 923  THR A C     1 
ATOM   8355  O O     . THR D 4 926  ? 119.013 161.469 119.074 1.00 50.26  ? 923  THR A O     1 
ATOM   8356  C CB    . THR D 4 926  ? 117.534 163.505 120.497 1.00 50.26  ? 923  THR A CB    1 
ATOM   8357  O OG1   . THR D 4 926  ? 117.189 163.285 119.124 1.00 50.26  ? 923  THR A OG1   1 
ATOM   8358  C CG2   . THR D 4 926  ? 118.616 164.567 120.576 1.00 50.26  ? 923  THR A CG2   1 
ATOM   8359  N N     . GLY D 4 927  ? 120.322 161.358 120.897 1.00 50.26  ? 924  GLY A N     1 
ATOM   8360  C CA    . GLY D 4 927  ? 121.442 160.778 120.188 1.00 50.26  ? 924  GLY A CA    1 
ATOM   8361  C C     . GLY D 4 927  ? 122.419 161.764 119.587 1.00 50.26  ? 924  GLY A C     1 
ATOM   8362  O O     . GLY D 4 927  ? 123.446 161.336 119.046 1.00 50.26  ? 924  GLY A O     1 
ATOM   8363  N N     . LYS D 4 928  ? 122.137 163.062 119.656 1.00 50.26  ? 925  LYS A N     1 
ATOM   8364  C CA    . LYS D 4 928  ? 123.067 164.056 119.139 1.00 50.26  ? 925  LYS A CA    1 
ATOM   8365  C C     . LYS D 4 928  ? 124.326 164.102 119.995 1.00 50.26  ? 925  LYS A C     1 
ATOM   8366  O O     . LYS D 4 928  ? 124.264 164.003 121.222 1.00 50.26  ? 925  LYS A O     1 
ATOM   8367  C CB    . LYS D 4 928  ? 122.409 165.433 119.105 1.00 27.29  ? 925  LYS A CB    1 
ATOM   8368  C CG    . LYS D 4 928  ? 121.280 165.561 118.097 1.00 27.29  ? 925  LYS A CG    1 
ATOM   8369  C CD    . LYS D 4 928  ? 120.661 166.948 118.144 1.00 27.29  ? 925  LYS A CD    1 
ATOM   8370  C CE    . LYS D 4 928  ? 119.539 167.088 117.130 1.00 27.29  ? 925  LYS A CE    1 
ATOM   8371  N NZ    . LYS D 4 928  ? 118.904 168.433 117.193 1.00 27.29  ? 925  LYS A NZ    1 
ATOM   8372  N N     . ILE D 4 929  ? 125.474 164.259 119.341 1.00 50.26  ? 926  ILE A N     1 
ATOM   8373  C CA    . ILE D 4 929  ? 126.747 164.302 120.055 1.00 50.26  ? 926  ILE A CA    1 
ATOM   8374  C C     . ILE D 4 929  ? 126.839 165.637 120.785 1.00 50.26  ? 926  ILE A C     1 
ATOM   8375  O O     . ILE D 4 929  ? 126.893 166.696 120.155 1.00 50.26  ? 926  ILE A O     1 
ATOM   8376  C CB    . ILE D 4 929  ? 127.934 164.109 119.107 1.00 50.26  ? 926  ILE A CB    1 
ATOM   8377  C CG1   . ILE D 4 929  ? 127.889 162.725 118.469 1.00 50.26  ? 926  ILE A CG1   1 
ATOM   8378  C CG2   . ILE D 4 929  ? 129.241 164.297 119.850 1.00 50.26  ? 926  ILE A CG2   1 
ATOM   8379  C CD1   . ILE D 4 929  ? 128.578 162.655 117.132 1.00 50.26  ? 926  ILE A CD1   1 
ATOM   8380  N N     . LEU D 4 930  ? 126.854 165.591 122.117 1.00 50.26  ? 927  LEU A N     1 
ATOM   8381  C CA    . LEU D 4 930  ? 127.033 166.816 122.886 1.00 50.26  ? 927  LEU A CA    1 
ATOM   8382  C C     . LEU D 4 930  ? 128.484 167.275 122.871 1.00 50.26  ? 927  LEU A C     1 
ATOM   8383  O O     . LEU D 4 930  ? 128.755 168.479 122.807 1.00 50.26  ? 927  LEU A O     1 
ATOM   8384  C CB    . LEU D 4 930  ? 126.552 166.613 124.322 1.00 50.26  ? 927  LEU A CB    1 
ATOM   8385  C CG    . LEU D 4 930  ? 125.043 166.691 124.552 1.00 50.26  ? 927  LEU A CG    1 
ATOM   8386  C CD1   . LEU D 4 930  ? 124.728 166.672 126.037 1.00 50.26  ? 927  LEU A CD1   1 
ATOM   8387  C CD2   . LEU D 4 930  ? 124.465 167.933 123.896 1.00 50.26  ? 927  LEU A CD2   1 
ATOM   8388  N N     . GLU D 4 931  ? 129.426 166.334 122.917 1.00 50.26  ? 928  GLU A N     1 
ATOM   8389  C CA    . GLU D 4 931  ? 130.843 166.662 122.964 1.00 50.26  ? 928  GLU A CA    1 
ATOM   8390  C C     . GLU D 4 931  ? 131.653 165.402 122.706 1.00 50.26  ? 928  GLU A C     1 
ATOM   8391  O O     . GLU D 4 931  ? 131.342 164.341 123.250 1.00 50.26  ? 928  GLU A O     1 
ATOM   8392  C CB    . GLU D 4 931  ? 131.224 167.268 124.321 1.00 50.26  ? 928  GLU A CB    1 
ATOM   8393  C CG    . GLU D 4 931  ? 132.700 167.179 124.660 1.00 50.26  ? 928  GLU A CG    1 
ATOM   8394  C CD    . GLU D 4 931  ? 133.002 167.672 126.059 1.00 50.26  ? 928  GLU A CD    1 
ATOM   8395  O OE1   . GLU D 4 931  ? 132.052 168.060 126.771 1.00 50.26  ? 928  GLU A OE1   1 
ATOM   8396  O OE2   . GLU D 4 931  ? 134.189 167.675 126.448 1.00 50.26  ? 928  GLU A OE2   1 
ATOM   8397  N N     . GLN D 4 932  ? 132.684 165.527 121.876 1.00 50.26  ? 929  GLN A N     1 
ATOM   8398  C CA    . GLN D 4 932  ? 133.655 164.465 121.650 1.00 50.26  ? 929  GLN A CA    1 
ATOM   8399  C C     . GLN D 4 932  ? 135.040 164.997 121.983 1.00 50.26  ? 929  GLN A C     1 
ATOM   8400  O O     . GLN D 4 932  ? 135.462 166.023 121.440 1.00 50.26  ? 929  GLN A O     1 
ATOM   8401  C CB    . GLN D 4 932  ? 133.603 163.962 120.207 1.00 50.26  ? 929  GLN A CB    1 
ATOM   8402  C CG    . GLN D 4 932  ? 133.359 165.052 119.183 1.00 50.26  ? 929  GLN A CG    1 
ATOM   8403  C CD    . GLN D 4 932  ? 133.241 164.509 117.778 1.00 50.26  ? 929  GLN A CD    1 
ATOM   8404  O OE1   . GLN D 4 932  ? 133.803 163.465 117.456 1.00 50.26  ? 929  GLN A OE1   1 
ATOM   8405  N NE2   . GLN D 4 932  ? 132.508 165.218 116.930 1.00 50.26  ? 929  GLN A NE2   1 
ATOM   8406  N N     . ARG D 4 933  ? 135.743 164.302 122.873 1.00 50.26  ? 930  ARG A N     1 
ATOM   8407  C CA    . ARG D 4 933  ? 137.029 164.762 123.372 1.00 50.26  ? 930  ARG A CA    1 
ATOM   8408  C C     . ARG D 4 933  ? 138.013 163.605 123.390 1.00 50.26  ? 930  ARG A C     1 
ATOM   8409  O O     . ARG D 4 933  ? 137.625 162.442 123.524 1.00 50.26  ? 930  ARG A O     1 
ATOM   8410  C CB    . ARG D 4 933  ? 136.904 165.354 124.780 1.00 50.26  ? 930  ARG A CB    1 
ATOM   8411  C CG    . ARG D 4 933  ? 138.072 166.225 125.199 1.00 50.26  ? 930  ARG A CG    1 
ATOM   8412  C CD    . ARG D 4 933  ? 137.619 167.327 126.133 1.00 50.26  ? 930  ARG A CD    1 
ATOM   8413  N NE    . ARG D 4 933  ? 137.037 166.790 127.356 1.00 50.26  ? 930  ARG A NE    1 
ATOM   8414  C CZ    . ARG D 4 933  ? 137.740 166.357 128.392 1.00 50.26  ? 930  ARG A CZ    1 
ATOM   8415  N NH1   . ARG D 4 933  ? 139.063 166.374 128.385 1.00 50.26  ? 930  ARG A NH1   1 
ATOM   8416  N NH2   . ARG D 4 933  ? 137.101 165.897 129.464 1.00 50.26  ? 930  ARG A NH2   1 
ATOM   8417  N N     . SER D 4 934  ? 139.293 163.937 123.265 1.00 50.26  ? 931  SER A N     1 
ATOM   8418  C CA    . SER D 4 934  ? 140.374 162.964 123.329 1.00 50.26  ? 931  SER A CA    1 
ATOM   8419  C C     . SER D 4 934  ? 141.035 163.057 124.695 1.00 50.26  ? 931  SER A C     1 
ATOM   8420  O O     . SER D 4 934  ? 141.528 164.123 125.078 1.00 50.26  ? 931  SER A O     1 
ATOM   8421  C CB    . SER D 4 934  ? 141.397 163.201 122.219 1.00 50.26  ? 931  SER A CB    1 
ATOM   8422  O OG    . SER D 4 934  ? 142.204 162.055 122.022 1.00 50.26  ? 931  SER A OG    1 
ATOM   8423  N N     . LEU D 4 935  ? 141.046 161.944 125.423 1.00 50.26  ? 932  LEU A N     1 
ATOM   8424  C CA    . LEU D 4 935  ? 141.681 161.883 126.728 1.00 50.26  ? 932  LEU A CA    1 
ATOM   8425  C C     . LEU D 4 935  ? 143.123 161.405 126.652 1.00 50.26  ? 932  LEU A C     1 
ATOM   8426  O O     . LEU D 4 935  ? 143.674 160.965 127.667 1.00 50.26  ? 932  LEU A O     1 
ATOM   8427  C CB    . LEU D 4 935  ? 140.879 160.980 127.666 1.00 50.26  ? 932  LEU A CB    1 
ATOM   8428  C CG    . LEU D 4 935  ? 139.497 161.488 128.073 1.00 50.26  ? 932  LEU A CG    1 
ATOM   8429  C CD1   . LEU D 4 935  ? 138.823 160.491 128.994 1.00 50.26  ? 932  LEU A CD1   1 
ATOM   8430  C CD2   . LEU D 4 935  ? 139.602 162.848 128.736 1.00 50.26  ? 932  LEU A CD2   1 
ATOM   8431  N N     . ASN D 4 936  ? 143.747 161.475 125.477 1.00 50.26  ? 933  ASN A N     1 
ATOM   8432  C CA    . ASN D 4 936  ? 145.139 161.070 125.352 1.00 50.26  ? 933  ASN A CA    1 
ATOM   8433  C C     . ASN D 4 936  ? 146.109 162.138 125.835 1.00 50.26  ? 933  ASN A C     1 
ATOM   8434  O O     . ASN D 4 936  ? 147.298 161.846 125.994 1.00 50.26  ? 933  ASN A O     1 
ATOM   8435  C CB    . ASN D 4 936  ? 145.455 160.693 123.901 1.00 50.26  ? 933  ASN A CB    1 
ATOM   8436  C CG    . ASN D 4 936  ? 145.399 161.878 122.963 1.00 50.26  ? 933  ASN A CG    1 
ATOM   8437  O OD1   . ASN D 4 936  ? 144.850 162.928 123.297 1.00 50.26  ? 933  ASN A OD1   1 
ATOM   8438  N ND2   . ASN D 4 936  ? 145.969 161.715 121.776 1.00 50.26  ? 933  ASN A ND2   1 
ATOM   8439  N N     . THR D 4 937  ? 145.636 163.359 126.069 1.00 50.26  ? 934  THR A N     1 
ATOM   8440  C CA    . THR D 4 937  ? 146.435 164.416 126.674 1.00 50.26  ? 934  THR A CA    1 
ATOM   8441  C C     . THR D 4 937  ? 145.773 164.845 127.977 1.00 50.26  ? 934  THR A C     1 
ATOM   8442  O O     . THR D 4 937  ? 144.630 165.315 127.976 1.00 50.26  ? 934  THR A O     1 
ATOM   8443  C CB    . THR D 4 937  ? 146.615 165.597 125.712 1.00 50.26  ? 934  THR A CB    1 
ATOM   8444  O OG1   . THR D 4 937  ? 147.324 166.656 126.368 1.00 50.26  ? 934  THR A OG1   1 
ATOM   8445  C CG2   . THR D 4 937  ? 145.279 166.105 125.171 1.00 50.26  ? 934  THR A CG2   1 
ATOM   8446  N N     . ILE D 4 938  ? 146.480 164.656 129.088 1.00 50.26  ? 935  ILE A N     1 
ATOM   8447  C CA    . ILE D 4 938  ? 145.958 164.950 130.417 1.00 50.26  ? 935  ILE A CA    1 
ATOM   8448  C C     . ILE D 4 938  ? 146.935 165.871 131.129 1.00 50.26  ? 935  ILE A C     1 
ATOM   8449  O O     . ILE D 4 938  ? 148.120 165.546 131.253 1.00 50.26  ? 935  ILE A O     1 
ATOM   8450  C CB    . ILE D 4 938  ? 145.735 163.670 131.245 1.00 50.26  ? 935  ILE A CB    1 
ATOM   8451  C CG1   . ILE D 4 938  ? 144.918 162.649 130.455 1.00 50.26  ? 935  ILE A CG1   1 
ATOM   8452  C CG2   . ILE D 4 938  ? 145.034 164.004 132.547 1.00 50.26  ? 935  ILE A CG2   1 
ATOM   8453  C CD1   . ILE D 4 938  ? 143.541 163.133 130.089 1.00 50.26  ? 935  ILE A CD1   1 
ATOM   8454  N N     . GLN D 4 939  ? 146.432 167.009 131.605 1.00 50.26  ? 936  GLN A N     1 
ATOM   8455  C CA    . GLN D 4 939  ? 147.223 167.973 132.367 1.00 50.26  ? 936  GLN A CA    1 
ATOM   8456  C C     . GLN D 4 939  ? 148.476 168.386 131.597 1.00 50.26  ? 936  GLN A C     1 
ATOM   8457  O O     . GLN D 4 939  ? 149.603 168.285 132.086 1.00 50.26  ? 936  GLN A O     1 
ATOM   8458  C CB    . GLN D 4 939  ? 147.580 167.416 133.747 1.00 50.26  ? 936  GLN A CB    1 
ATOM   8459  C CG    . GLN D 4 939  ? 147.984 168.472 134.764 1.00 50.26  ? 936  GLN A CG    1 
ATOM   8460  C CD    . GLN D 4 939  ? 146.978 169.599 134.870 1.00 50.26  ? 936  GLN A CD    1 
ATOM   8461  O OE1   . GLN D 4 939  ? 145.769 169.369 134.897 1.00 50.26  ? 936  GLN A OE1   1 
ATOM   8462  N NE2   . GLN D 4 939  ? 147.473 170.828 134.931 1.00 50.26  ? 936  GLN A NE2   1 
ATOM   8463  N N     . GLN D 4 940  ? 148.261 168.850 130.366 1.00 50.26  ? 937  GLN A N     1 
ATOM   8464  C CA    . GLN D 4 940  ? 149.334 169.368 129.517 1.00 50.26  ? 937  GLN A CA    1 
ATOM   8465  C C     . GLN D 4 940  ? 150.438 168.332 129.309 1.00 50.26  ? 937  GLN A C     1 
ATOM   8466  O O     . GLN D 4 940  ? 151.627 168.635 129.417 1.00 50.26  ? 937  GLN A O     1 
ATOM   8467  C CB    . GLN D 4 940  ? 149.907 170.666 130.090 1.00 44.99  ? 937  GLN A CB    1 
ATOM   8468  C CG    . GLN D 4 940  ? 150.469 171.614 129.049 1.00 44.99  ? 937  GLN A CG    1 
ATOM   8469  C CD    . GLN D 4 940  ? 150.814 172.969 129.629 1.00 44.99  ? 937  GLN A CD    1 
ATOM   8470  O OE1   . GLN D 4 940  ? 150.630 173.211 130.821 1.00 44.99  ? 937  GLN A OE1   1 
ATOM   8471  N NE2   . GLN D 4 940  ? 151.321 173.861 128.787 1.00 44.99  ? 937  GLN A NE2   1 
ATOM   8472  N N     . PHE D 4 941  ? 150.045 167.095 129.019 1.00 50.26  ? 938  PHE A N     1 
ATOM   8473  C CA    . PHE D 4 941  ? 151.008 166.048 128.705 1.00 50.26  ? 938  PHE A CA    1 
ATOM   8474  C C     . PHE D 4 941  ? 150.386 165.077 127.716 1.00 50.26  ? 938  PHE A C     1 
ATOM   8475  O O     . PHE D 4 941  ? 149.303 164.543 127.970 1.00 50.26  ? 938  PHE A O     1 
ATOM   8476  C CB    . PHE D 4 941  ? 151.454 165.302 129.963 1.00 50.26  ? 938  PHE A CB    1 
ATOM   8477  C CG    . PHE D 4 941  ? 152.553 164.315 129.716 1.00 50.26  ? 938  PHE A CG    1 
ATOM   8478  C CD1   . PHE D 4 941  ? 153.856 164.743 129.538 1.00 50.26  ? 938  PHE A CD1   1 
ATOM   8479  C CD2   . PHE D 4 941  ? 152.284 162.961 129.648 1.00 50.26  ? 938  PHE A CD2   1 
ATOM   8480  C CE1   . PHE D 4 941  ? 154.870 163.841 129.306 1.00 50.26  ? 938  PHE A CE1   1 
ATOM   8481  C CE2   . PHE D 4 941  ? 153.294 162.054 129.414 1.00 50.26  ? 938  PHE A CE2   1 
ATOM   8482  C CZ    . PHE D 4 941  ? 154.589 162.495 129.244 1.00 50.26  ? 938  PHE A CZ    1 
ATOM   8483  N N     . ASP D 4 942  ? 151.076 164.840 126.604 1.00 50.26  ? 939  ASP A N     1 
ATOM   8484  C CA    . ASP D 4 942  ? 150.593 163.944 125.559 1.00 50.26  ? 939  ASP A CA    1 
ATOM   8485  C C     . ASP D 4 942  ? 151.059 162.528 125.876 1.00 50.26  ? 939  ASP A C     1 
ATOM   8486  O O     . ASP D 4 942  ? 152.263 162.255 125.905 1.00 50.26  ? 939  ASP A O     1 
ATOM   8487  C CB    . ASP D 4 942  ? 151.096 164.396 124.191 1.00 50.26  ? 939  ASP A CB    1 
ATOM   8488  C CG    . ASP D 4 942  ? 150.236 163.883 123.055 1.00 50.26  ? 939  ASP A CG    1 
ATOM   8489  O OD1   . ASP D 4 942  ? 149.653 162.788 123.195 1.00 50.26  ? 939  ASP A OD1   1 
ATOM   8490  O OD2   . ASP D 4 942  ? 150.141 164.575 122.021 1.00 50.26  ? 939  ASP A OD2   1 
ATOM   8491  N N     . TYR D 4 943  ? 150.107 161.627 126.112 1.00 50.26  ? 940  TYR A N     1 
ATOM   8492  C CA    . TYR D 4 943  ? 150.434 160.244 126.442 1.00 50.26  ? 940  TYR A CA    1 
ATOM   8493  C C     . TYR D 4 943  ? 150.528 159.375 125.190 1.00 50.26  ? 940  TYR A C     1 
ATOM   8494  O O     . TYR D 4 943  ? 151.563 158.753 124.935 1.00 50.26  ? 940  TYR A O     1 
ATOM   8495  C CB    . TYR D 4 943  ? 149.397 159.675 127.417 1.00 50.26  ? 940  TYR A CB    1 
ATOM   8496  C CG    . TYR D 4 943  ? 149.572 160.148 128.842 1.00 50.26  ? 940  TYR A CG    1 
ATOM   8497  C CD1   . TYR D 4 943  ? 148.950 161.304 129.290 1.00 50.26  ? 940  TYR A CD1   1 
ATOM   8498  C CD2   . TYR D 4 943  ? 150.360 159.442 129.738 1.00 50.26  ? 940  TYR A CD2   1 
ATOM   8499  C CE1   . TYR D 4 943  ? 149.106 161.741 130.589 1.00 50.26  ? 940  TYR A CE1   1 
ATOM   8500  C CE2   . TYR D 4 943  ? 150.523 159.873 131.040 1.00 50.26  ? 940  TYR A CE2   1 
ATOM   8501  C CZ    . TYR D 4 943  ? 149.893 161.023 131.459 1.00 50.26  ? 940  TYR A CZ    1 
ATOM   8502  O OH    . TYR D 4 943  ? 150.050 161.457 132.754 1.00 50.26  ? 940  TYR A OH    1 
ATOM   8503  N N     . GLN D 4 944  ? 149.455 159.327 124.397 1.00 50.26  ? 941  GLN A N     1 
ATOM   8504  C CA    . GLN D 4 944  ? 149.443 158.453 123.228 1.00 50.26  ? 941  GLN A CA    1 
ATOM   8505  C C     . GLN D 4 944  ? 150.298 159.020 122.107 1.00 50.26  ? 941  GLN A C     1 
ATOM   8506  O O     . GLN D 4 944  ? 151.283 158.403 121.686 1.00 50.26  ? 941  GLN A O     1 
ATOM   8507  C CB    . GLN D 4 944  ? 148.014 158.243 122.731 1.00 50.26  ? 941  GLN A CB    1 
ATOM   8508  C CG    . GLN D 4 944  ? 147.838 156.984 121.891 1.00 50.26  ? 941  GLN A CG    1 
ATOM   8509  C CD    . GLN D 4 944  ? 148.360 157.138 120.481 1.00 50.26  ? 941  GLN A CD    1 
ATOM   8510  O OE1   . GLN D 4 944  ? 148.295 158.218 119.897 1.00 50.26  ? 941  GLN A OE1   1 
ATOM   8511  N NE2   . GLN D 4 944  ? 148.889 156.055 119.925 1.00 50.26  ? 941  GLN A NE2   1 
ATOM   8512  N N     . LYS D 4 945  ? 149.927 160.200 121.607 1.00 50.26  ? 942  LYS A N     1 
ATOM   8513  C CA    . LYS D 4 945  ? 150.520 160.706 120.375 1.00 50.26  ? 942  LYS A CA    1 
ATOM   8514  C C     . LYS D 4 945  ? 152.027 160.872 120.493 1.00 50.26  ? 942  LYS A C     1 
ATOM   8515  O O     . LYS D 4 945  ? 152.734 160.808 119.481 1.00 50.26  ? 942  LYS A O     1 
ATOM   8516  C CB    . LYS D 4 945  ? 149.862 162.028 119.979 1.00 46.85  ? 942  LYS A CB    1 
ATOM   8517  C CG    . LYS D 4 945  ? 148.436 161.872 119.469 1.00 46.85  ? 942  LYS A CG    1 
ATOM   8518  C CD    . LYS D 4 945  ? 147.792 163.217 119.174 1.00 46.85  ? 942  LYS A CD    1 
ATOM   8519  C CE    . LYS D 4 945  ? 146.374 163.043 118.656 1.00 46.85  ? 942  LYS A CE    1 
ATOM   8520  N NZ    . LYS D 4 945  ? 145.715 164.349 118.383 1.00 46.85  ? 942  LYS A NZ    1 
ATOM   8521  N N     . LYS D 4 946  ? 152.544 161.079 121.704 1.00 50.26  ? 943  LYS A N     1 
ATOM   8522  C CA    . LYS D 4 946  ? 153.986 161.209 121.870 1.00 50.26  ? 943  LYS A CA    1 
ATOM   8523  C C     . LYS D 4 946  ? 154.591 160.101 122.722 1.00 50.26  ? 943  LYS A C     1 
ATOM   8524  O O     . LYS D 4 946  ? 155.314 159.260 122.186 1.00 50.26  ? 943  LYS A O     1 
ATOM   8525  C CB    . LYS D 4 946  ? 154.308 162.585 122.469 1.00 50.26  ? 943  LYS A CB    1 
ATOM   8526  C CG    . LYS D 4 946  ? 153.995 163.833 121.608 1.00 50.26  ? 943  LYS A CG    1 
ATOM   8527  C CD    . LYS D 4 946  ? 154.024 163.702 120.069 1.00 50.26  ? 943  LYS A CD    1 
ATOM   8528  C CE    . LYS D 4 946  ? 155.279 163.035 119.495 1.00 50.26  ? 943  LYS A CE    1 
ATOM   8529  N NZ    . LYS D 4 946  ? 155.258 163.011 118.007 1.00 50.26  ? 943  LYS A NZ    1 
ATOM   8530  N N     . LEU D 4 947  ? 154.259 160.018 124.013 1.00 50.26  ? 944  LEU A N     1 
ATOM   8531  C CA    . LEU D 4 947  ? 155.097 159.244 124.928 1.00 50.26  ? 944  LEU A CA    1 
ATOM   8532  C C     . LEU D 4 947  ? 154.976 157.745 124.685 1.00 50.26  ? 944  LEU A C     1 
ATOM   8533  O O     . LEU D 4 947  ? 155.989 157.035 124.611 1.00 50.26  ? 944  LEU A O     1 
ATOM   8534  C CB    . LEU D 4 947  ? 154.746 159.576 126.378 1.00 50.26  ? 944  LEU A CB    1 
ATOM   8535  C CG    . LEU D 4 947  ? 155.639 158.891 127.413 1.00 50.26  ? 944  LEU A CG    1 
ATOM   8536  C CD1   . LEU D 4 947  ? 157.030 159.499 127.406 1.00 50.26  ? 944  LEU A CD1   1 
ATOM   8537  C CD2   . LEU D 4 947  ? 155.028 158.981 128.796 1.00 50.26  ? 944  LEU A CD2   1 
ATOM   8538  N N     . ASP D 4 948  ? 153.747 157.243 124.562 1.00 50.26  ? 945  ASP A N     1 
ATOM   8539  C CA    . ASP D 4 948  ? 153.570 155.823 124.290 1.00 50.26  ? 945  ASP A CA    1 
ATOM   8540  C C     . ASP D 4 948  ? 154.166 155.443 122.944 1.00 50.26  ? 945  ASP A C     1 
ATOM   8541  O O     . ASP D 4 948  ? 154.636 154.314 122.770 1.00 50.26  ? 945  ASP A O     1 
ATOM   8542  C CB    . ASP D 4 948  ? 152.088 155.456 124.347 1.00 50.26  ? 945  ASP A CB    1 
ATOM   8543  C CG    . ASP D 4 948  ? 151.862 153.963 124.453 1.00 50.26  ? 945  ASP A CG    1 
ATOM   8544  O OD1   . ASP D 4 948  ? 152.090 153.405 125.546 1.00 50.26  ? 945  ASP A OD1   1 
ATOM   8545  O OD2   . ASP D 4 948  ? 151.458 153.346 123.446 1.00 50.26  ? 945  ASP A OD2   1 
ATOM   8546  N N     . ASN D 4 949  ? 154.176 156.373 121.986 1.00 50.26  ? 946  ASN A N     1 
ATOM   8547  C CA    . ASN D 4 949  ? 154.796 156.094 120.695 1.00 50.26  ? 946  ASN A CA    1 
ATOM   8548  C C     . ASN D 4 949  ? 156.301 155.895 120.830 1.00 50.26  ? 946  ASN A C     1 
ATOM   8549  O O     . ASN D 4 949  ? 156.863 154.963 120.243 1.00 50.26  ? 946  ASN A O     1 
ATOM   8550  C CB    . ASN D 4 949  ? 154.485 157.218 119.708 1.00 50.26  ? 946  ASN A CB    1 
ATOM   8551  C CG    . ASN D 4 949  ? 153.044 157.194 119.235 1.00 50.26  ? 946  ASN A CG    1 
ATOM   8552  O OD1   . ASN D 4 949  ? 152.393 156.150 119.245 1.00 50.26  ? 946  ASN A OD1   1 
ATOM   8553  N ND2   . ASN D 4 949  ? 152.544 158.345 118.805 1.00 50.26  ? 946  ASN A ND2   1 
ATOM   8554  N N     . ARG D 4 950  ? 156.976 156.755 121.599 1.00 50.26  ? 947  ARG A N     1 
ATOM   8555  C CA    . ARG D 4 950  ? 158.401 156.544 121.837 1.00 50.26  ? 947  ARG A CA    1 
ATOM   8556  C C     . ARG D 4 950  ? 158.654 155.262 122.618 1.00 50.26  ? 947  ARG A C     1 
ATOM   8557  O O     . ARG D 4 950  ? 159.650 154.573 122.375 1.00 50.26  ? 947  ARG A O     1 
ATOM   8558  C CB    . ARG D 4 950  ? 159.032 157.738 122.557 1.00 50.26  ? 947  ARG A CB    1 
ATOM   8559  C CG    . ARG D 4 950  ? 159.303 158.958 121.684 1.00 50.26  ? 947  ARG A CG    1 
ATOM   8560  C CD    . ARG D 4 950  ? 158.110 159.863 121.536 1.00 50.26  ? 947  ARG A CD    1 
ATOM   8561  N NE    . ARG D 4 950  ? 158.457 161.125 120.895 1.00 50.26  ? 947  ARG A NE    1 
ATOM   8562  C CZ    . ARG D 4 950  ? 158.362 161.351 119.592 1.00 50.26  ? 947  ARG A CZ    1 
ATOM   8563  N NH1   . ARG D 4 950  ? 157.933 160.418 118.759 1.00 50.26  ? 947  ARG A NH1   1 
ATOM   8564  N NH2   . ARG D 4 950  ? 158.707 162.542 119.113 1.00 50.26  ? 947  ARG A NH2   1 
ATOM   8565  N N     . GLU D 4 951  ? 157.779 154.925 123.567 1.00 50.26  ? 948  GLU A N     1 
ATOM   8566  C CA    . GLU D 4 951  ? 157.957 153.667 124.287 1.00 50.26  ? 948  GLU A CA    1 
ATOM   8567  C C     . GLU D 4 951  ? 157.839 152.470 123.347 1.00 50.26  ? 948  GLU A C     1 
ATOM   8568  O O     . GLU D 4 951  ? 158.631 151.522 123.432 1.00 50.26  ? 948  GLU A O     1 
ATOM   8569  C CB    . GLU D 4 951  ? 156.949 153.564 125.430 1.00 50.26  ? 948  GLU A CB    1 
ATOM   8570  C CG    . GLU D 4 951  ? 157.180 154.567 126.551 1.00 50.26  ? 948  GLU A CG    1 
ATOM   8571  C CD    . GLU D 4 951  ? 158.298 154.156 127.493 1.00 50.26  ? 948  GLU A CD    1 
ATOM   8572  O OE1   . GLU D 4 951  ? 159.461 154.074 127.048 1.00 50.26  ? 948  GLU A OE1   1 
ATOM   8573  O OE2   . GLU D 4 951  ? 158.012 153.916 128.684 1.00 50.26  ? 948  GLU A OE2   1 
ATOM   8574  N N     . LYS D 4 952  ? 156.863 152.498 122.436 1.00 50.26  ? 949  LYS A N     1 
ATOM   8575  C CA    . LYS D 4 952  ? 156.729 151.418 121.463 1.00 50.26  ? 949  LYS A CA    1 
ATOM   8576  C C     . LYS D 4 952  ? 157.922 151.371 120.516 1.00 50.26  ? 949  LYS A C     1 
ATOM   8577  O O     . LYS D 4 952  ? 158.368 150.286 120.125 1.00 50.26  ? 949  LYS A O     1 
ATOM   8578  C CB    . LYS D 4 952  ? 155.426 151.568 120.680 1.00 50.26  ? 949  LYS A CB    1 
ATOM   8579  C CG    . LYS D 4 952  ? 154.174 151.477 121.535 1.00 50.26  ? 949  LYS A CG    1 
ATOM   8580  C CD    . LYS D 4 952  ? 154.221 150.275 122.464 1.00 50.26  ? 949  LYS A CD    1 
ATOM   8581  C CE    . LYS D 4 952  ? 152.933 149.471 122.394 1.00 50.26  ? 949  LYS A CE    1 
ATOM   8582  N NZ    . LYS D 4 952  ? 152.878 148.412 123.439 1.00 50.26  ? 949  LYS A NZ    1 
ATOM   8583  N N     . GLU D 4 953  ? 158.446 152.535 120.126 1.00 51.39  ? 950  GLU A N     1 
ATOM   8584  C CA    . GLU D 4 953  ? 159.640 152.561 119.287 1.00 51.39  ? 950  GLU A CA    1 
ATOM   8585  C C     . GLU D 4 953  ? 160.831 151.947 120.011 1.00 51.39  ? 950  GLU A C     1 
ATOM   8586  O O     . GLU D 4 953  ? 161.622 151.209 119.410 1.00 51.39  ? 950  GLU A O     1 
ATOM   8587  C CB    . GLU D 4 953  ? 159.950 153.994 118.859 1.00 51.39  ? 950  GLU A CB    1 
ATOM   8588  C CG    . GLU D 4 953  ? 159.037 154.523 117.765 1.00 51.39  ? 950  GLU A CG    1 
ATOM   8589  C CD    . GLU D 4 953  ? 159.312 155.975 117.426 1.00 51.39  ? 950  GLU A CD    1 
ATOM   8590  O OE1   . GLU D 4 953  ? 160.492 156.383 117.465 1.00 51.39  ? 950  GLU A OE1   1 
ATOM   8591  O OE2   . GLU D 4 953  ? 158.348 156.708 117.119 1.00 51.39  ? 950  GLU A OE2   1 
ATOM   8592  N N     . ARG D 4 954  ? 160.976 152.242 121.304 1.00 50.26  ? 951  ARG A N     1 
ATOM   8593  C CA    . ARG D 4 954  ? 162.050 151.642 122.088 1.00 50.26  ? 951  ARG A CA    1 
ATOM   8594  C C     . ARG D 4 954  ? 161.875 150.133 122.199 1.00 50.26  ? 951  ARG A C     1 
ATOM   8595  O O     . ARG D 4 954  ? 162.857 149.383 122.151 1.00 50.26  ? 951  ARG A O     1 
ATOM   8596  C CB    . ARG D 4 954  ? 162.105 152.279 123.475 1.00 50.26  ? 951  ARG A CB    1 
ATOM   8597  C CG    . ARG D 4 954  ? 162.801 153.626 123.508 1.00 50.26  ? 951  ARG A CG    1 
ATOM   8598  C CD    . ARG D 4 954  ? 163.659 153.771 124.752 1.00 50.26  ? 951  ARG A CD    1 
ATOM   8599  N NE    . ARG D 4 954  ? 162.881 153.595 125.973 1.00 50.26  ? 951  ARG A NE    1 
ATOM   8600  C CZ    . ARG D 4 954  ? 163.398 153.256 127.146 1.00 50.26  ? 951  ARG A CZ    1 
ATOM   8601  N NH1   . ARG D 4 954  ? 164.695 153.048 127.295 1.00 50.26  ? 951  ARG A NH1   1 
ATOM   8602  N NH2   . ARG D 4 954  ? 162.592 153.124 128.196 1.00 50.26  ? 951  ARG A NH2   1 
ATOM   8603  N N     . VAL D 4 955  ? 160.633 149.670 122.360 1.00 50.26  ? 952  VAL A N     1 
ATOM   8604  C CA    . VAL D 4 955  ? 160.377 148.230 122.385 1.00 50.26  ? 952  VAL A CA    1 
ATOM   8605  C C     . VAL D 4 955  ? 160.788 147.597 121.062 1.00 50.26  ? 952  VAL A C     1 
ATOM   8606  O O     . VAL D 4 955  ? 161.452 146.554 121.029 1.00 50.26  ? 952  VAL A O     1 
ATOM   8607  C CB    . VAL D 4 955  ? 158.899 147.947 122.703 1.00 50.26  ? 952  VAL A CB    1 
ATOM   8608  C CG1   . VAL D 4 955  ? 158.572 146.487 122.444 1.00 50.26  ? 952  VAL A CG1   1 
ATOM   8609  C CG2   . VAL D 4 955  ? 158.602 148.289 124.137 1.00 50.26  ? 952  VAL A CG2   1 
ATOM   8610  N N     . ALA D 4 956  ? 160.403 148.222 119.949 1.00 54.24  ? 953  ALA A N     1 
ATOM   8611  C CA    . ALA D 4 956  ? 160.762 147.685 118.641 1.00 54.24  ? 953  ALA A CA    1 
ATOM   8612  C C     . ALA D 4 956  ? 162.270 147.684 118.432 1.00 54.24  ? 953  ALA A C     1 
ATOM   8613  O O     . ALA D 4 956  ? 162.804 146.791 117.764 1.00 54.24  ? 953  ALA A O     1 
ATOM   8614  C CB    . ALA D 4 956  ? 160.070 148.482 117.536 1.00 54.24  ? 953  ALA A CB    1 
ATOM   8615  N N     . ALA D 4 957  ? 162.972 148.669 118.994 1.00 57.42  ? 954  ALA A N     1 
ATOM   8616  C CA    . ALA D 4 957  ? 164.417 148.753 118.817 1.00 57.42  ? 954  ALA A CA    1 
ATOM   8617  C C     . ALA D 4 957  ? 165.174 147.749 119.678 1.00 57.42  ? 954  ALA A C     1 
ATOM   8618  O O     . ALA D 4 957  ? 166.236 147.269 119.267 1.00 57.42  ? 954  ALA A O     1 
ATOM   8619  C CB    . ALA D 4 957  ? 164.902 150.170 119.124 1.00 57.42  ? 954  ALA A CB    1 
ATOM   8620  N N     . ARG D 4 958  ? 164.663 147.424 120.866 1.00 67.27  ? 955  ARG A N     1 
ATOM   8621  C CA    . ARG D 4 958  ? 165.386 146.569 121.800 1.00 67.27  ? 955  ARG A CA    1 
ATOM   8622  C C     . ARG D 4 958  ? 164.643 145.286 122.137 1.00 67.27  ? 955  ARG A C     1 
ATOM   8623  O O     . ARG D 4 958  ? 165.257 144.212 122.154 1.00 67.27  ? 955  ARG A O     1 
ATOM   8624  C CB    . ARG D 4 958  ? 165.694 147.345 123.089 1.00 67.27  ? 955  ARG A CB    1 
ATOM   8625  C CG    . ARG D 4 958  ? 166.680 148.486 122.904 1.00 67.27  ? 955  ARG A CG    1 
ATOM   8626  C CD    . ARG D 4 958  ? 166.973 149.174 124.223 1.00 67.27  ? 955  ARG A CD    1 
ATOM   8627  N NE    . ARG D 4 958  ? 167.864 150.313 124.040 1.00 67.27  ? 955  ARG A NE    1 
ATOM   8628  C CZ    . ARG D 4 958  ? 168.199 151.167 124.997 1.00 67.27  ? 955  ARG A CZ    1 
ATOM   8629  N NH1   . ARG D 4 958  ? 167.746 151.033 126.233 1.00 67.27  ? 955  ARG A NH1   1 
ATOM   8630  N NH2   . ARG D 4 958  ? 169.005 152.184 124.706 1.00 67.27  ? 955  ARG A NH2   1 
ATOM   8631  N N     . GLN D 4 959  ? 163.340 145.368 122.417 1.00 63.96  ? 956  GLN A N     1 
ATOM   8632  C CA    . GLN D 4 959  ? 162.531 144.213 122.819 1.00 63.96  ? 956  GLN A CA    1 
ATOM   8633  C C     . GLN D 4 959  ? 163.055 143.596 124.116 1.00 63.96  ? 956  GLN A C     1 
ATOM   8634  O O     . GLN D 4 959  ? 163.353 142.403 124.191 1.00 63.96  ? 956  GLN A O     1 
ATOM   8635  C CB    . GLN D 4 959  ? 162.457 143.169 121.700 1.00 63.96  ? 956  GLN A CB    1 
ATOM   8636  C CG    . GLN D 4 959  ? 161.229 142.277 121.760 1.00 63.96  ? 956  GLN A CG    1 
ATOM   8637  C CD    . GLN D 4 959  ? 159.951 143.018 121.420 1.00 63.96  ? 956  GLN A CD    1 
ATOM   8638  O OE1   . GLN D 4 959  ? 159.912 143.812 120.481 1.00 63.96  ? 956  GLN A OE1   1 
ATOM   8639  N NE2   . GLN D 4 959  ? 158.896 142.760 122.183 1.00 63.96  ? 956  GLN A NE2   1 
ATOM   8640  N N     . ALA D 4 960  ? 163.167 144.430 125.146 1.00 65.40  ? 957  ALA A N     1 
ATOM   8641  C CA    . ALA D 4 960  ? 163.629 143.997 126.456 1.00 65.40  ? 957  ALA A CA    1 
ATOM   8642  C C     . ALA D 4 960  ? 162.432 143.747 127.373 1.00 65.40  ? 957  ALA A C     1 
ATOM   8643  O O     . ALA D 4 960  ? 161.277 143.751 126.942 1.00 65.40  ? 957  ALA A O     1 
ATOM   8644  C CB    . ALA D 4 960  ? 164.589 145.029 127.043 1.00 65.40  ? 957  ALA A CB    1 
ATOM   8645  N N     . TRP D 4 961  ? 162.705 143.520 128.659 1.00 63.05  ? 958  TRP A N     1 
ATOM   8646  C CA    . TRP D 4 961  ? 161.677 143.318 129.676 1.00 63.05  ? 958  TRP A CA    1 
ATOM   8647  C C     . TRP D 4 961  ? 161.367 144.588 130.459 1.00 63.05  ? 958  TRP A C     1 
ATOM   8648  O O     . TRP D 4 961  ? 160.194 144.902 130.700 1.00 63.05  ? 958  TRP A O     1 
ATOM   8649  C CB    . TRP D 4 961  ? 162.109 142.207 130.641 1.00 63.05  ? 958  TRP A CB    1 
ATOM   8650  C CG    . TRP D 4 961  ? 162.083 140.834 130.045 1.00 63.05  ? 958  TRP A CG    1 
ATOM   8651  C CD1   . TRP D 4 961  ? 161.530 140.468 128.854 1.00 63.05  ? 958  TRP A CD1   1 
ATOM   8652  C CD2   . TRP D 4 961  ? 162.649 139.643 130.606 1.00 63.05  ? 958  TRP A CD2   1 
ATOM   8653  N NE1   . TRP D 4 961  ? 161.704 139.122 128.645 1.00 63.05  ? 958  TRP A NE1   1 
ATOM   8654  C CE2   . TRP D 4 961  ? 162.392 138.593 129.705 1.00 63.05  ? 958  TRP A CE2   1 
ATOM   8655  C CE3   . TRP D 4 961  ? 163.345 139.363 131.785 1.00 63.05  ? 958  TRP A CE3   1 
ATOM   8656  C CZ2   . TRP D 4 961  ? 162.805 137.286 129.944 1.00 63.05  ? 958  TRP A CZ2   1 
ATOM   8657  C CZ3   . TRP D 4 961  ? 163.756 138.064 132.021 1.00 63.05  ? 958  TRP A CZ3   1 
ATOM   8658  C CH2   . TRP D 4 961  ? 163.484 137.042 131.105 1.00 63.05  ? 958  TRP A CH2   1 
ATOM   8659  N N     . SER D 4 962  ? 162.403 145.324 130.869 1.00 54.80  ? 959  SER A N     1 
ATOM   8660  C CA    . SER D 4 962  ? 162.191 146.534 131.655 1.00 54.80  ? 959  SER A CA    1 
ATOM   8661  C C     . SER D 4 962  ? 161.374 147.564 130.890 1.00 54.80  ? 959  SER A C     1 
ATOM   8662  O O     . SER D 4 962  ? 160.574 148.290 131.489 1.00 54.80  ? 959  SER A O     1 
ATOM   8663  C CB    . SER D 4 962  ? 163.536 147.125 132.078 1.00 54.80  ? 959  SER A CB    1 
ATOM   8664  O OG    . SER D 4 962  ? 164.462 147.102 131.006 1.00 54.80  ? 959  SER A OG    1 
ATOM   8665  N N     . VAL D 4 963  ? 161.555 147.639 129.570 1.00 50.26  ? 960  VAL A N     1 
ATOM   8666  C CA    . VAL D 4 963  ? 160.772 148.573 128.768 1.00 50.26  ? 960  VAL A CA    1 
ATOM   8667  C C     . VAL D 4 963  ? 159.296 148.198 128.808 1.00 50.26  ? 960  VAL A C     1 
ATOM   8668  O O     . VAL D 4 963  ? 158.421 149.066 128.922 1.00 50.26  ? 960  VAL A O     1 
ATOM   8669  C CB    . VAL D 4 963  ? 161.309 148.620 127.327 1.00 50.26  ? 960  VAL A CB    1 
ATOM   8670  C CG1   . VAL D 4 963  ? 160.694 149.784 126.576 1.00 50.26  ? 960  VAL A CG1   1 
ATOM   8671  C CG2   . VAL D 4 963  ? 162.825 148.716 127.330 1.00 50.26  ? 960  VAL A CG2   1 
ATOM   8672  N N     . VAL D 4 964  ? 158.996 146.900 128.723 1.00 50.26  ? 961  VAL A N     1 
ATOM   8673  C CA    . VAL D 4 964  ? 157.609 146.447 128.796 1.00 50.26  ? 961  VAL A CA    1 
ATOM   8674  C C     . VAL D 4 964  ? 157.018 146.753 130.168 1.00 50.26  ? 961  VAL A C     1 
ATOM   8675  O O     . VAL D 4 964  ? 155.857 147.170 130.284 1.00 50.26  ? 961  VAL A O     1 
ATOM   8676  C CB    . VAL D 4 964  ? 157.520 144.948 128.460 1.00 50.26  ? 961  VAL A CB    1 
ATOM   8677  C CG1   . VAL D 4 964  ? 156.085 144.460 128.575 1.00 50.26  ? 961  VAL A CG1   1 
ATOM   8678  C CG2   . VAL D 4 964  ? 158.068 144.685 127.068 1.00 50.26  ? 961  VAL A CG2   1 
ATOM   8679  N N     . GLY D 4 965  ? 157.801 146.546 131.229 1.00 50.26  ? 962  GLY A N     1 
ATOM   8680  C CA    . GLY D 4 965  ? 157.318 146.882 132.560 1.00 50.26  ? 962  GLY A CA    1 
ATOM   8681  C C     . GLY D 4 965  ? 157.026 148.363 132.719 1.00 50.26  ? 962  GLY A C     1 
ATOM   8682  O O     . GLY D 4 965  ? 156.012 148.749 133.312 1.00 50.26  ? 962  GLY A O     1 
ATOM   8683  N N     . THR D 4 966  ? 157.910 149.212 132.190 1.00 50.26  ? 963  THR A N     1 
ATOM   8684  C CA    . THR D 4 966  ? 157.672 150.651 132.240 1.00 50.26  ? 963  THR A CA    1 
ATOM   8685  C C     . THR D 4 966  ? 156.437 151.030 131.436 1.00 50.26  ? 963  THR A C     1 
ATOM   8686  O O     . THR D 4 966  ? 155.684 151.926 131.830 1.00 50.26  ? 963  THR A O     1 
ATOM   8687  C CB    . THR D 4 966  ? 158.894 151.413 131.729 1.00 50.26  ? 963  THR A CB    1 
ATOM   8688  O OG1   . THR D 4 966  ? 159.250 150.933 130.427 1.00 50.26  ? 963  THR A OG1   1 
ATOM   8689  C CG2   . THR D 4 966  ? 160.069 151.236 132.678 1.00 50.26  ? 963  THR A CG2   1 
ATOM   8690  N N     . ILE D 4 967  ? 156.213 150.360 130.303 1.00 50.26  ? 964  ILE A N     1 
ATOM   8691  C CA    . ILE D 4 967  ? 155.007 150.614 129.520 1.00 50.26  ? 964  ILE A CA    1 
ATOM   8692  C C     . ILE D 4 967  ? 153.763 150.255 130.322 1.00 50.26  ? 964  ILE A C     1 
ATOM   8693  O O     . ILE D 4 967  ? 152.771 150.993 130.319 1.00 50.26  ? 964  ILE A O     1 
ATOM   8694  C CB    . ILE D 4 967  ? 155.061 149.851 128.184 1.00 50.26  ? 964  ILE A CB    1 
ATOM   8695  C CG1   . ILE D 4 967  ? 155.959 150.586 127.195 1.00 50.26  ? 964  ILE A CG1   1 
ATOM   8696  C CG2   . ILE D 4 967  ? 153.671 149.674 127.604 1.00 50.26  ? 964  ILE A CG2   1 
ATOM   8697  C CD1   . ILE D 4 967  ? 156.013 149.940 125.843 1.00 50.26  ? 964  ILE A CD1   1 
ATOM   8698  N N     . LYS D 4 968  ? 153.794 149.119 131.020 1.00 50.26  ? 965  LYS A N     1 
ATOM   8699  C CA    . LYS D 4 968  ? 152.646 148.723 131.834 1.00 50.26  ? 965  LYS A CA    1 
ATOM   8700  C C     . LYS D 4 968  ? 152.382 149.739 132.941 1.00 50.26  ? 965  LYS A C     1 
ATOM   8701  O O     . LYS D 4 968  ? 151.230 150.120 133.197 1.00 50.26  ? 965  LYS A O     1 
ATOM   8702  C CB    . LYS D 4 968  ? 152.878 147.331 132.420 1.00 50.26  ? 965  LYS A CB    1 
ATOM   8703  C CG    . LYS D 4 968  ? 151.850 146.914 133.457 1.00 50.26  ? 965  LYS A CG    1 
ATOM   8704  C CD    . LYS D 4 968  ? 150.845 145.933 132.878 1.00 50.26  ? 965  LYS A CD    1 
ATOM   8705  C CE    . LYS D 4 968  ? 150.315 144.993 133.948 1.00 50.26  ? 965  LYS A CE    1 
ATOM   8706  N NZ    . LYS D 4 968  ? 149.221 144.124 133.436 1.00 50.26  ? 965  LYS A NZ    1 
ATOM   8707  N N     . ASP D 4 969  ? 153.444 150.194 133.609 1.00 50.26  ? 966  ASP A N     1 
ATOM   8708  C CA    . ASP D 4 969  ? 153.277 151.182 134.673 1.00 50.26  ? 966  ASP A CA    1 
ATOM   8709  C C     . ASP D 4 969  ? 152.730 152.498 134.127 1.00 50.26  ? 966  ASP A C     1 
ATOM   8710  O O     . ASP D 4 969  ? 151.854 153.124 134.744 1.00 50.26  ? 966  ASP A O     1 
ATOM   8711  C CB    . ASP D 4 969  ? 154.607 151.404 135.390 1.00 50.26  ? 966  ASP A CB    1 
ATOM   8712  C CG    . ASP D 4 969  ? 154.958 150.266 136.330 1.00 50.26  ? 966  ASP A CG    1 
ATOM   8713  O OD1   . ASP D 4 969  ? 154.030 149.579 136.805 1.00 50.26  ? 966  ASP A OD1   1 
ATOM   8714  O OD2   . ASP D 4 969  ? 156.161 150.058 136.593 1.00 50.26  ? 966  ASP A OD2   1 
ATOM   8715  N N     . LEU D 4 970  ? 153.236 152.934 132.971 1.00 50.26  ? 967  LEU A N     1 
ATOM   8716  C CA    . LEU D 4 970  ? 152.736 154.154 132.350 1.00 50.26  ? 967  LEU A CA    1 
ATOM   8717  C C     . LEU D 4 970  ? 151.268 154.014 131.978 1.00 50.26  ? 967  LEU A C     1 
ATOM   8718  O O     . LEU D 4 970  ? 150.486 154.959 132.135 1.00 50.26  ? 967  LEU A O     1 
ATOM   8719  C CB    . LEU D 4 970  ? 153.574 154.492 131.118 1.00 50.26  ? 967  LEU A CB    1 
ATOM   8720  C CG    . LEU D 4 970  ? 152.947 155.437 130.093 1.00 50.26  ? 967  LEU A CG    1 
ATOM   8721  C CD1   . LEU D 4 970  ? 152.788 156.829 130.676 1.00 50.26  ? 967  LEU A CD1   1 
ATOM   8722  C CD2   . LEU D 4 970  ? 153.780 155.476 128.824 1.00 50.26  ? 967  LEU A CD2   1 
ATOM   8723  N N     . LYS D 4 971  ? 150.876 152.840 131.479 1.00 50.26  ? 968  LYS A N     1 
ATOM   8724  C CA    . LYS D 4 971  ? 149.472 152.605 131.168 1.00 50.26  ? 968  LYS A CA    1 
ATOM   8725  C C     . LYS D 4 971  ? 148.610 152.711 132.417 1.00 50.26  ? 968  LYS A C     1 
ATOM   8726  O O     . LYS D 4 971  ? 147.537 153.322 132.387 1.00 50.26  ? 968  LYS A O     1 
ATOM   8727  C CB    . LYS D 4 971  ? 149.301 151.236 130.515 1.00 50.26  ? 968  LYS A CB    1 
ATOM   8728  C CG    . LYS D 4 971  ? 149.714 151.185 129.059 1.00 50.26  ? 968  LYS A CG    1 
ATOM   8729  C CD    . LYS D 4 971  ? 149.410 149.826 128.462 1.00 50.26  ? 968  LYS A CD    1 
ATOM   8730  C CE    . LYS D 4 971  ? 150.051 149.665 127.098 1.00 50.26  ? 968  LYS A CE    1 
ATOM   8731  N NZ    . LYS D 4 971  ? 149.688 148.364 126.475 1.00 50.26  ? 968  LYS A NZ    1 
ATOM   8732  N N     . GLN D 4 972  ? 149.064 152.128 133.529 1.00 50.26  ? 969  GLN A N     1 
ATOM   8733  C CA    . GLN D 4 972  ? 148.281 152.216 134.760 1.00 50.26  ? 969  GLN A CA    1 
ATOM   8734  C C     . GLN D 4 972  ? 148.127 153.663 135.219 1.00 50.26  ? 969  GLN A C     1 
ATOM   8735  O O     . GLN D 4 972  ? 147.025 154.096 135.588 1.00 50.26  ? 969  GLN A O     1 
ATOM   8736  C CB    . GLN D 4 972  ? 148.920 151.365 135.855 1.00 37.80  ? 969  GLN A CB    1 
ATOM   8737  C CG    . GLN D 4 972  ? 148.622 149.881 135.729 1.00 37.80  ? 969  GLN A CG    1 
ATOM   8738  C CD    . GLN D 4 972  ? 149.157 149.077 136.896 1.00 37.80  ? 969  GLN A CD    1 
ATOM   8739  O OE1   . GLN D 4 972  ? 150.092 149.497 137.577 1.00 37.80  ? 969  GLN A OE1   1 
ATOM   8740  N NE2   . GLN D 4 972  ? 148.565 147.913 137.133 1.00 37.80  ? 969  GLN A NE2   1 
ATOM   8741  N N     . GLY D 4 973  ? 149.217 154.433 135.189 1.00 50.26  ? 970  GLY A N     1 
ATOM   8742  C CA    . GLY D 4 973  ? 149.118 155.835 135.572 1.00 50.26  ? 970  GLY A CA    1 
ATOM   8743  C C     . GLY D 4 973  ? 148.180 156.620 134.673 1.00 50.26  ? 970  GLY A C     1 
ATOM   8744  O O     . GLY D 4 973  ? 147.343 157.402 135.149 1.00 50.26  ? 970  GLY A O     1 
ATOM   8745  N N     . TYR D 4 974  ? 148.295 156.410 133.360 1.00 50.26  ? 971  TYR A N     1 
ATOM   8746  C CA    . TYR D 4 974  ? 147.424 157.106 132.424 1.00 50.26  ? 971  TYR A CA    1 
ATOM   8747  C C     . TYR D 4 974  ? 145.965 156.760 132.672 1.00 50.26  ? 971  TYR A C     1 
ATOM   8748  O O     . TYR D 4 974  ? 145.097 157.636 132.618 1.00 50.26  ? 971  TYR A O     1 
ATOM   8749  C CB    . TYR D 4 974  ? 147.807 156.764 130.989 1.00 50.26  ? 971  TYR A CB    1 
ATOM   8750  C CG    . TYR D 4 974  ? 146.773 157.224 129.999 1.00 50.26  ? 971  TYR A CG    1 
ATOM   8751  C CD1   . TYR D 4 974  ? 146.649 158.564 129.676 1.00 50.26  ? 971  TYR A CD1   1 
ATOM   8752  C CD2   . TYR D 4 974  ? 145.895 156.325 129.417 1.00 50.26  ? 971  TYR A CD2   1 
ATOM   8753  C CE1   . TYR D 4 974  ? 145.698 158.993 128.783 1.00 50.26  ? 971  TYR A CE1   1 
ATOM   8754  C CE2   . TYR D 4 974  ? 144.936 156.746 128.529 1.00 50.26  ? 971  TYR A CE2   1 
ATOM   8755  C CZ    . TYR D 4 974  ? 144.846 158.081 128.209 1.00 50.26  ? 971  TYR A CZ    1 
ATOM   8756  O OH    . TYR D 4 974  ? 143.890 158.505 127.319 1.00 50.26  ? 971  TYR A OH    1 
ATOM   8757  N N     . LEU D 4 975  ? 145.671 155.484 132.931 1.00 50.26  ? 972  LEU A N     1 
ATOM   8758  C CA    . LEU D 4 975  ? 144.294 155.113 133.236 1.00 50.26  ? 972  LEU A CA    1 
ATOM   8759  C C     . LEU D 4 975  ? 143.817 155.733 134.542 1.00 50.26  ? 972  LEU A C     1 
ATOM   8760  O O     . LEU D 4 975  ? 142.625 156.009 134.684 1.00 50.26  ? 972  LEU A O     1 
ATOM   8761  C CB    . LEU D 4 975  ? 144.132 153.592 133.263 1.00 50.26  ? 972  LEU A CB    1 
ATOM   8762  C CG    . LEU D 4 975  ? 143.856 152.882 131.928 1.00 50.26  ? 972  LEU A CG    1 
ATOM   8763  C CD1   . LEU D 4 975  ? 142.517 153.328 131.378 1.00 50.26  ? 972  LEU A CD1   1 
ATOM   8764  C CD2   . LEU D 4 975  ? 144.928 153.109 130.887 1.00 50.26  ? 972  LEU A CD2   1 
ATOM   8765  N N     . SER D 4 976  ? 144.716 155.979 135.496 1.00 50.26  ? 973  SER A N     1 
ATOM   8766  C CA    . SER D 4 976  ? 144.312 156.718 136.694 1.00 50.26  ? 973  SER A CA    1 
ATOM   8767  C C     . SER D 4 976  ? 143.873 158.141 136.345 1.00 50.26  ? 973  SER A C     1 
ATOM   8768  O O     . SER D 4 976  ? 142.815 158.620 136.795 1.00 50.26  ? 973  SER A O     1 
ATOM   8769  C CB    . SER D 4 976  ? 145.456 156.739 137.706 1.00 50.26  ? 973  SER A CB    1 
ATOM   8770  O OG    . SER D 4 976  ? 146.373 157.776 137.409 1.00 50.26  ? 973  SER A OG    1 
ATOM   8771  N N     . GLN D 4 977  ? 144.675 158.836 135.534 1.00 50.26  ? 974  GLN A N     1 
ATOM   8772  C CA    . GLN D 4 977  ? 144.260 160.170 135.098 1.00 50.26  ? 974  GLN A CA    1 
ATOM   8773  C C     . GLN D 4 977  ? 142.953 160.113 134.311 1.00 50.26  ? 974  GLN A C     1 
ATOM   8774  O O     . GLN D 4 977  ? 142.111 161.018 134.408 1.00 50.26  ? 974  GLN A O     1 
ATOM   8775  C CB    . GLN D 4 977  ? 145.352 160.848 134.268 1.00 50.26  ? 974  GLN A CB    1 
ATOM   8776  C CG    . GLN D 4 977  ? 146.378 161.612 135.092 1.00 50.26  ? 974  GLN A CG    1 
ATOM   8777  C CD    . GLN D 4 977  ? 147.607 160.802 135.415 1.00 50.26  ? 974  GLN A CD    1 
ATOM   8778  O OE1   . GLN D 4 977  ? 147.957 159.878 134.691 1.00 50.26  ? 974  GLN A OE1   1 
ATOM   8779  N NE2   . GLN D 4 977  ? 148.271 161.145 136.510 1.00 50.26  ? 974  GLN A NE2   1 
ATOM   8780  N N     . VAL D 4 978  ? 142.765 159.050 133.530 1.00 50.26  ? 975  VAL A N     1 
ATOM   8781  C CA    . VAL D 4 978  ? 141.528 158.881 132.777 1.00 50.26  ? 975  VAL A CA    1 
ATOM   8782  C C     . VAL D 4 978  ? 140.349 158.689 133.721 1.00 50.26  ? 975  VAL A C     1 
ATOM   8783  O O     . VAL D 4 978  ? 139.242 159.164 133.453 1.00 50.26  ? 975  VAL A O     1 
ATOM   8784  C CB    . VAL D 4 978  ? 141.675 157.712 131.788 1.00 50.26  ? 975  VAL A CB    1 
ATOM   8785  C CG1   . VAL D 4 978  ? 140.330 157.275 131.259 1.00 50.26  ? 975  VAL A CG1   1 
ATOM   8786  C CG2   . VAL D 4 978  ? 142.567 158.123 130.647 1.00 50.26  ? 975  VAL A CG2   1 
ATOM   8787  N N     . ILE D 4 979  ? 140.563 157.987 134.836 1.00 50.26  ? 976  ILE A N     1 
ATOM   8788  C CA    . ILE D 4 979  ? 139.524 157.867 135.858 1.00 50.26  ? 976  ILE A CA    1 
ATOM   8789  C C     . ILE D 4 979  ? 139.117 159.244 136.355 1.00 50.26  ? 976  ILE A C     1 
ATOM   8790  O O     . ILE D 4 979  ? 137.924 159.552 136.488 1.00 50.26  ? 976  ILE A O     1 
ATOM   8791  C CB    . ILE D 4 979  ? 140.006 156.984 137.022 1.00 50.26  ? 976  ILE A CB    1 
ATOM   8792  C CG1   . ILE D 4 979  ? 140.278 155.561 136.550 1.00 50.26  ? 976  ILE A CG1   1 
ATOM   8793  C CG2   . ILE D 4 979  ? 138.995 156.996 138.155 1.00 50.26  ? 976  ILE A CG2   1 
ATOM   8794  C CD1   . ILE D 4 979  ? 140.991 154.727 137.569 1.00 50.26  ? 976  ILE A CD1   1 
ATOM   8795  N N     . HIS D 4 980  ? 140.105 160.089 136.653 1.00 50.26  ? 977  HIS A N     1 
ATOM   8796  C CA    . HIS D 4 980  ? 139.769 161.436 137.114 1.00 50.26  ? 977  HIS A CA    1 
ATOM   8797  C C     . HIS D 4 980  ? 138.954 162.190 136.071 1.00 50.26  ? 977  HIS A C     1 
ATOM   8798  O O     . HIS D 4 980  ? 137.944 162.828 136.393 1.00 50.26  ? 977  HIS A O     1 
ATOM   8799  C CB    . HIS D 4 980  ? 141.016 162.239 137.453 1.00 50.26  ? 977  HIS A CB    1 
ATOM   8800  C CG    . HIS D 4 980  ? 140.741 163.702 137.621 1.00 50.26  ? 977  HIS A CG    1 
ATOM   8801  N ND1   . HIS D 4 980  ? 141.309 164.666 136.818 1.00 50.26  ? 977  HIS A ND1   1 
ATOM   8802  C CD2   . HIS D 4 980  ? 139.933 164.360 138.486 1.00 50.26  ? 977  HIS A CD2   1 
ATOM   8803  C CE1   . HIS D 4 980  ? 140.875 165.857 137.190 1.00 50.26  ? 977  HIS A CE1   1 
ATOM   8804  N NE2   . HIS D 4 980  ? 140.039 165.699 138.201 1.00 50.26  ? 977  HIS A NE2   1 
ATOM   8805  N N     . GLU D 4 981  ? 139.392 162.142 134.812 1.00 50.26  ? 978  GLU A N     1 
ATOM   8806  C CA    . GLU D 4 981  ? 138.680 162.870 133.764 1.00 50.26  ? 978  GLU A CA    1 
ATOM   8807  C C     . GLU D 4 981  ? 137.259 162.346 133.599 1.00 50.26  ? 978  GLU A C     1 
ATOM   8808  O O     . GLU D 4 981  ? 136.316 163.125 133.406 1.00 50.26  ? 978  GLU A O     1 
ATOM   8809  C CB    . GLU D 4 981  ? 139.445 162.777 132.445 1.00 50.26  ? 978  GLU A CB    1 
ATOM   8810  C CG    . GLU D 4 981  ? 140.858 163.323 132.514 1.00 50.26  ? 978  GLU A CG    1 
ATOM   8811  C CD    . GLU D 4 981  ? 140.927 164.806 132.217 1.00 50.26  ? 978  GLU A CD    1 
ATOM   8812  O OE1   . GLU D 4 981  ? 140.391 165.228 131.172 1.00 50.26  ? 978  GLU A OE1   1 
ATOM   8813  O OE2   . GLU D 4 981  ? 141.518 165.550 133.027 1.00 50.26  ? 978  GLU A OE2   1 
ATOM   8814  N N     . ILE D 4 982  ? 137.087 161.026 133.680 1.00 50.26  ? 979  ILE A N     1 
ATOM   8815  C CA    . ILE D 4 982  ? 135.769 160.424 133.510 1.00 50.26  ? 979  ILE A CA    1 
ATOM   8816  C C     . ILE D 4 982  ? 134.835 160.864 134.627 1.00 50.26  ? 979  ILE A C     1 
ATOM   8817  O O     . ILE D 4 982  ? 133.680 161.226 134.381 1.00 50.26  ? 979  ILE A O     1 
ATOM   8818  C CB    . ILE D 4 982  ? 135.884 158.891 133.450 1.00 50.26  ? 979  ILE A CB    1 
ATOM   8819  C CG1   . ILE D 4 982  ? 136.400 158.448 132.086 1.00 50.26  ? 979  ILE A CG1   1 
ATOM   8820  C CG2   . ILE D 4 982  ? 134.544 158.242 133.736 1.00 50.26  ? 979  ILE A CG2   1 
ATOM   8821  C CD1   . ILE D 4 982  ? 136.924 157.046 132.089 1.00 50.26  ? 979  ILE A CD1   1 
ATOM   8822  N N     . VAL D 4 983  ? 135.314 160.831 135.874 1.00 50.26  ? 980  VAL A N     1 
ATOM   8823  C CA    . VAL D 4 983  ? 134.433 161.231 136.970 1.00 50.26  ? 980  VAL A CA    1 
ATOM   8824  C C     . VAL D 4 983  ? 134.123 162.721 136.896 1.00 50.26  ? 980  VAL A C     1 
ATOM   8825  O O     . VAL D 4 983  ? 133.001 163.142 137.207 1.00 50.26  ? 980  VAL A O     1 
ATOM   8826  C CB    . VAL D 4 983  ? 135.018 160.828 138.338 1.00 50.26  ? 980  VAL A CB    1 
ATOM   8827  C CG1   . VAL D 4 983  ? 135.377 159.353 138.345 1.00 50.26  ? 980  VAL A CG1   1 
ATOM   8828  C CG2   . VAL D 4 983  ? 136.220 161.677 138.706 1.00 50.26  ? 980  VAL A CG2   1 
ATOM   8829  N N     . ASP D 4 984  ? 135.084 163.542 136.464 1.00 50.26  ? 981  ASP A N     1 
ATOM   8830  C CA    . ASP D 4 984  ? 134.817 164.968 136.311 1.00 50.26  ? 981  ASP A CA    1 
ATOM   8831  C C     . ASP D 4 984  ? 133.727 165.206 135.272 1.00 50.26  ? 981  ASP A C     1 
ATOM   8832  O O     . ASP D 4 984  ? 132.785 165.975 135.503 1.00 50.26  ? 981  ASP A O     1 
ATOM   8833  C CB    . ASP D 4 984  ? 136.106 165.696 135.927 1.00 50.26  ? 981  ASP A CB    1 
ATOM   8834  C CG    . ASP D 4 984  ? 135.995 167.205 136.053 1.00 50.26  ? 981  ASP A CG    1 
ATOM   8835  O OD1   . ASP D 4 984  ? 134.864 167.730 136.115 1.00 50.26  ? 981  ASP A OD1   1 
ATOM   8836  O OD2   . ASP D 4 984  ? 137.050 167.871 136.101 1.00 50.26  ? 981  ASP A OD2   1 
ATOM   8837  N N     . LEU D 4 985  ? 133.836 164.542 134.119 1.00 50.26  ? 982  LEU A N     1 
ATOM   8838  C CA    . LEU D 4 985  ? 132.833 164.713 133.073 1.00 50.26  ? 982  LEU A CA    1 
ATOM   8839  C C     . LEU D 4 985  ? 131.476 164.194 133.531 1.00 50.26  ? 982  LEU A C     1 
ATOM   8840  O O     . LEU D 4 985  ? 130.437 164.809 133.256 1.00 50.26  ? 982  LEU A O     1 
ATOM   8841  C CB    . LEU D 4 985  ? 133.280 163.997 131.802 1.00 50.26  ? 982  LEU A CB    1 
ATOM   8842  C CG    . LEU D 4 985  ? 132.410 164.253 130.577 1.00 50.26  ? 982  LEU A CG    1 
ATOM   8843  C CD1   . LEU D 4 985  ? 132.528 165.711 130.188 1.00 50.26  ? 982  LEU A CD1   1 
ATOM   8844  C CD2   . LEU D 4 985  ? 132.807 163.357 129.427 1.00 50.26  ? 982  LEU A CD2   1 
ATOM   8845  N N     . MET D 4 986  ? 131.473 163.057 134.230 1.00 50.26  ? 983  MET A N     1 
ATOM   8846  C CA    . MET D 4 986  ? 130.254 162.518 134.822 1.00 50.26  ? 983  MET A CA    1 
ATOM   8847  C C     . MET D 4 986  ? 129.559 163.547 135.697 1.00 50.26  ? 983  MET A C     1 
ATOM   8848  O O     . MET D 4 986  ? 128.357 163.793 135.555 1.00 50.26  ? 983  MET A O     1 
ATOM   8849  C CB    . MET D 4 986  ? 130.600 161.287 135.654 1.00 50.26  ? 983  MET A CB    1 
ATOM   8850  C CG    . MET D 4 986  ? 129.413 160.512 136.150 1.00 50.26  ? 983  MET A CG    1 
ATOM   8851  S SD    . MET D 4 986  ? 129.747 158.754 136.238 1.00 50.26  ? 983  MET A SD    1 
ATOM   8852  C CE    . MET D 4 986  ? 128.472 158.277 137.384 1.00 50.26  ? 983  MET A CE    1 
ATOM   8853  N N     . ILE D 4 987  ? 130.305 164.154 136.619 1.00 50.26  ? 984  ILE A N     1 
ATOM   8854  C CA    . ILE D 4 987  ? 129.691 165.084 137.557 1.00 50.26  ? 984  ILE A CA    1 
ATOM   8855  C C     . ILE D 4 987  ? 129.219 166.336 136.832 1.00 50.26  ? 984  ILE A C     1 
ATOM   8856  O O     . ILE D 4 987  ? 128.173 166.906 137.167 1.00 50.26  ? 984  ILE A O     1 
ATOM   8857  C CB    . ILE D 4 987  ? 130.666 165.412 138.701 1.00 50.26  ? 984  ILE A CB    1 
ATOM   8858  C CG1   . ILE D 4 987  ? 131.013 164.139 139.474 1.00 50.26  ? 984  ILE A CG1   1 
ATOM   8859  C CG2   . ILE D 4 987  ? 130.069 166.445 139.636 1.00 50.26  ? 984  ILE A CG2   1 
ATOM   8860  C CD1   . ILE D 4 987  ? 129.854 163.178 139.635 1.00 50.26  ? 984  ILE A CD1   1 
ATOM   8861  N N     . HIS D 4 988  ? 129.972 166.783 135.824 1.00 50.26  ? 985  HIS A N     1 
ATOM   8862  C CA    . HIS D 4 988  ? 129.559 167.971 135.083 1.00 50.26  ? 985  HIS A CA    1 
ATOM   8863  C C     . HIS D 4 988  ? 128.257 167.734 134.327 1.00 50.26  ? 985  HIS A C     1 
ATOM   8864  O O     . HIS D 4 988  ? 127.362 168.585 134.342 1.00 50.26  ? 985  HIS A O     1 
ATOM   8865  C CB    . HIS D 4 988  ? 130.660 168.407 134.119 1.00 50.26  ? 985  HIS A CB    1 
ATOM   8866  C CG    . HIS D 4 988  ? 130.205 169.411 133.108 1.00 50.26  ? 985  HIS A CG    1 
ATOM   8867  N ND1   . HIS D 4 988  ? 130.036 169.104 131.776 1.00 50.26  ? 985  HIS A ND1   1 
ATOM   8868  C CD2   . HIS D 4 988  ? 129.874 170.718 133.237 1.00 50.26  ? 985  HIS A CD2   1 
ATOM   8869  C CE1   . HIS D 4 988  ? 129.625 170.178 131.127 1.00 50.26  ? 985  HIS A CE1   1 
ATOM   8870  N NE2   . HIS D 4 988  ? 129.519 171.171 131.990 1.00 50.26  ? 985  HIS A NE2   1 
ATOM   8871  N N     . TYR D 4 989  ? 128.130 166.588 133.658 1.00 50.26  ? 986  TYR A N     1 
ATOM   8872  C CA    . TYR D 4 989  ? 126.937 166.317 132.864 1.00 50.26  ? 986  TYR A CA    1 
ATOM   8873  C C     . TYR D 4 989  ? 125.852 165.566 133.622 1.00 50.26  ? 986  TYR A C     1 
ATOM   8874  O O     . TYR D 4 989  ? 124.746 165.421 133.091 1.00 50.26  ? 986  TYR A O     1 
ATOM   8875  C CB    . TYR D 4 989  ? 127.296 165.523 131.604 1.00 50.26  ? 986  TYR A CB    1 
ATOM   8876  C CG    . TYR D 4 989  ? 127.787 166.375 130.459 1.00 50.26  ? 986  TYR A CG    1 
ATOM   8877  C CD1   . TYR D 4 989  ? 126.897 167.081 129.663 1.00 50.26  ? 986  TYR A CD1   1 
ATOM   8878  C CD2   . TYR D 4 989  ? 129.138 166.470 130.170 1.00 50.26  ? 986  TYR A CD2   1 
ATOM   8879  C CE1   . TYR D 4 989  ? 127.340 167.861 128.615 1.00 50.26  ? 986  TYR A CE1   1 
ATOM   8880  C CE2   . TYR D 4 989  ? 129.591 167.248 129.124 1.00 50.26  ? 986  TYR A CE2   1 
ATOM   8881  C CZ    . TYR D 4 989  ? 128.689 167.940 128.350 1.00 50.26  ? 986  TYR A CZ    1 
ATOM   8882  O OH    . TYR D 4 989  ? 129.142 168.715 127.308 1.00 50.26  ? 986  TYR A OH    1 
ATOM   8883  N N     . GLN D 4 990  ? 126.133 165.090 134.837 1.00 50.26  ? 987  GLN A N     1 
ATOM   8884  C CA    . GLN D 4 990  ? 125.187 164.270 135.599 1.00 50.26  ? 987  GLN A CA    1 
ATOM   8885  C C     . GLN D 4 990  ? 124.726 163.066 134.784 1.00 50.26  ? 987  GLN A C     1 
ATOM   8886  O O     . GLN D 4 990  ? 123.588 162.610 134.906 1.00 50.26  ? 987  GLN A O     1 
ATOM   8887  C CB    . GLN D 4 990  ? 123.987 165.094 136.071 1.00 50.26  ? 987  GLN A CB    1 
ATOM   8888  C CG    . GLN D 4 990  ? 124.326 166.128 137.127 1.00 50.26  ? 987  GLN A CG    1 
ATOM   8889  C CD    . GLN D 4 990  ? 123.094 166.741 137.755 1.00 50.26  ? 987  GLN A CD    1 
ATOM   8890  O OE1   . GLN D 4 990  ? 121.993 166.645 137.213 1.00 50.26  ? 987  GLN A OE1   1 
ATOM   8891  N NE2   . GLN D 4 990  ? 123.271 167.376 138.907 1.00 50.26  ? 987  GLN A NE2   1 
ATOM   8892  N N     . ALA D 4 991  ? 125.617 162.544 133.949 1.00 50.26  ? 988  ALA A N     1 
ATOM   8893  C CA    . ALA D 4 991  ? 125.272 161.516 132.984 1.00 50.26  ? 988  ALA A CA    1 
ATOM   8894  C C     . ALA D 4 991  ? 125.612 160.127 133.512 1.00 50.26  ? 988  ALA A C     1 
ATOM   8895  O O     . ALA D 4 991  ? 126.313 159.961 134.511 1.00 50.26  ? 988  ALA A O     1 
ATOM   8896  C CB    . ALA D 4 991  ? 125.994 161.767 131.662 1.00 50.26  ? 988  ALA A CB    1 
ATOM   8897  N N     . VAL D 4 992  ? 125.103 159.117 132.814 1.00 50.26  ? 989  VAL A N     1 
ATOM   8898  C CA    . VAL D 4 992  ? 125.403 157.720 133.093 1.00 50.26  ? 989  VAL A CA    1 
ATOM   8899  C C     . VAL D 4 992  ? 126.478 157.268 132.115 1.00 50.26  ? 989  VAL A C     1 
ATOM   8900  O O     . VAL D 4 992  ? 126.373 157.514 130.908 1.00 50.26  ? 989  VAL A O     1 
ATOM   8901  C CB    . VAL D 4 992  ? 124.140 156.844 133.010 1.00 50.26  ? 989  VAL A CB    1 
ATOM   8902  C CG1   . VAL D 4 992  ? 123.451 157.013 131.678 1.00 50.26  ? 989  VAL A CG1   1 
ATOM   8903  C CG2   . VAL D 4 992  ? 124.487 155.388 133.232 1.00 50.26  ? 989  VAL A CG2   1 
ATOM   8904  N N     . VAL D 4 993  ? 127.520 156.637 132.639 1.00 50.26  ? 990  VAL A N     1 
ATOM   8905  C CA    . VAL D 4 993  ? 128.706 156.305 131.860 1.00 50.26  ? 990  VAL A CA    1 
ATOM   8906  C C     . VAL D 4 993  ? 128.608 154.863 131.386 1.00 50.26  ? 990  VAL A C     1 
ATOM   8907  O O     . VAL D 4 993  ? 128.283 153.961 132.167 1.00 50.26  ? 990  VAL A O     1 
ATOM   8908  C CB    . VAL D 4 993  ? 129.980 156.534 132.686 1.00 50.26  ? 990  VAL A CB    1 
ATOM   8909  C CG1   . VAL D 4 993  ? 131.173 155.967 131.975 1.00 50.26  ? 990  VAL A CG1   1 
ATOM   8910  C CG2   . VAL D 4 993  ? 130.184 158.012 132.916 1.00 50.26  ? 990  VAL A CG2   1 
ATOM   8911  N N     . VAL D 4 994  ? 128.891 154.643 130.104 1.00 50.26  ? 991  VAL A N     1 
ATOM   8912  C CA    . VAL D 4 994  ? 128.768 153.335 129.473 1.00 50.26  ? 991  VAL A CA    1 
ATOM   8913  C C     . VAL D 4 994  ? 130.158 152.884 129.047 1.00 50.26  ? 991  VAL A C     1 
ATOM   8914  O O     . VAL D 4 994  ? 130.742 153.448 128.114 1.00 50.26  ? 991  VAL A O     1 
ATOM   8915  C CB    . VAL D 4 994  ? 127.813 153.368 128.275 1.00 50.26  ? 991  VAL A CB    1 
ATOM   8916  C CG1   . VAL D 4 994  ? 127.803 152.025 127.570 1.00 50.26  ? 991  VAL A CG1   1 
ATOM   8917  C CG2   . VAL D 4 994  ? 126.419 153.754 128.726 1.00 50.26  ? 991  VAL A CG2   1 
ATOM   8918  N N     . LEU D 4 995  ? 130.686 151.869 129.723 1.00 50.26  ? 992  LEU A N     1 
ATOM   8919  C CA    . LEU D 4 995  ? 131.944 151.249 129.339 1.00 50.26  ? 992  LEU A CA    1 
ATOM   8920  C C     . LEU D 4 995  ? 131.665 150.105 128.368 1.00 50.26  ? 992  LEU A C     1 
ATOM   8921  O O     . LEU D 4 995  ? 130.555 149.951 127.854 1.00 50.26  ? 992  LEU A O     1 
ATOM   8922  C CB    . LEU D 4 995  ? 132.706 150.751 130.566 1.00 50.26  ? 992  LEU A CB    1 
ATOM   8923  C CG    . LEU D 4 995  ? 133.583 151.707 131.379 1.00 50.26  ? 992  LEU A CG    1 
ATOM   8924  C CD1   . LEU D 4 995  ? 134.725 152.236 130.530 1.00 50.26  ? 992  LEU A CD1   1 
ATOM   8925  C CD2   . LEU D 4 995  ? 132.784 152.840 131.982 1.00 50.26  ? 992  LEU A CD2   1 
ATOM   8926  N N     . GLU D 4 996  ? 132.680 149.288 128.106 1.00 50.26  ? 993  GLU A N     1 
ATOM   8927  C CA    . GLU D 4 996  ? 132.536 148.070 127.322 1.00 50.26  ? 993  GLU A CA    1 
ATOM   8928  C C     . GLU D 4 996  ? 132.986 146.888 128.166 1.00 50.26  ? 993  GLU A C     1 
ATOM   8929  O O     . GLU D 4 996  ? 134.084 146.909 128.732 1.00 50.26  ? 993  GLU A O     1 
ATOM   8930  C CB    . GLU D 4 996  ? 133.347 148.149 126.026 1.00 50.26  ? 993  GLU A CB    1 
ATOM   8931  C CG    . GLU D 4 996  ? 134.787 148.588 126.222 1.00 50.26  ? 993  GLU A CG    1 
ATOM   8932  C CD    . GLU D 4 996  ? 135.653 148.301 125.014 1.00 50.26  ? 993  GLU A CD    1 
ATOM   8933  O OE1   . GLU D 4 996  ? 136.045 147.130 124.826 1.00 50.26  ? 993  GLU A OE1   1 
ATOM   8934  O OE2   . GLU D 4 996  ? 135.947 149.248 124.256 1.00 50.26  ? 993  GLU A OE2   1 
ATOM   8935  N N     . ASN D 4 997  ? 132.139 145.867 128.265 1.00 50.26  ? 994  ASN A N     1 
ATOM   8936  C CA    . ASN D 4 997  ? 132.507 144.684 129.031 1.00 50.26  ? 994  ASN A CA    1 
ATOM   8937  C C     . ASN D 4 997  ? 133.542 143.875 128.263 1.00 50.26  ? 994  ASN A C     1 
ATOM   8938  O O     . ASN D 4 997  ? 133.406 143.652 127.057 1.00 50.26  ? 994  ASN A O     1 
ATOM   8939  C CB    . ASN D 4 997  ? 131.277 143.833 129.346 1.00 50.26  ? 994  ASN A CB    1 
ATOM   8940  C CG    . ASN D 4 997  ? 130.425 143.558 128.129 1.00 50.26  ? 994  ASN A CG    1 
ATOM   8941  O OD1   . ASN D 4 997  ? 130.722 144.020 127.031 1.00 50.26  ? 994  ASN A OD1   1 
ATOM   8942  N ND2   . ASN D 4 997  ? 129.354 142.798 128.320 1.00 50.26  ? 994  ASN A ND2   1 
ATOM   8943  N N     . LEU D 4 998  ? 134.587 143.439 128.966 1.00 50.26  ? 995  LEU A N     1 
ATOM   8944  C CA    . LEU D 4 998  ? 135.696 142.754 128.318 1.00 50.26  ? 995  LEU A CA    1 
ATOM   8945  C C     . LEU D 4 998  ? 135.367 141.317 127.941 1.00 50.26  ? 995  LEU A C     1 
ATOM   8946  O O     . LEU D 4 998  ? 136.188 140.666 127.287 1.00 50.26  ? 995  LEU A O     1 
ATOM   8947  C CB    . LEU D 4 998  ? 136.932 142.783 129.219 1.00 50.26  ? 995  LEU A CB    1 
ATOM   8948  C CG    . LEU D 4 998  ? 137.817 144.034 129.191 1.00 50.26  ? 995  LEU A CG    1 
ATOM   8949  C CD1   . LEU D 4 998  ? 138.435 144.216 127.813 1.00 50.26  ? 995  LEU A CD1   1 
ATOM   8950  C CD2   . LEU D 4 998  ? 137.068 145.287 129.618 1.00 50.26  ? 995  LEU A CD2   1 
ATOM   8951  N N     . ASN D 4 999  ? 134.200 140.808 128.343 1.00 35.06  ? 996  ASN A N     1 
ATOM   8952  C CA    . ASN D 4 999  ? 133.854 139.423 128.042 1.00 35.06  ? 996  ASN A CA    1 
ATOM   8953  C C     . ASN D 4 999  ? 133.739 139.188 126.541 1.00 35.06  ? 996  ASN A C     1 
ATOM   8954  O O     . ASN D 4 999  ? 134.194 138.157 126.031 1.00 35.06  ? 996  ASN A O     1 
ATOM   8955  C CB    . ASN D 4 999  ? 132.549 139.047 128.743 1.00 35.06  ? 996  ASN A CB    1 
ATOM   8956  C CG    . ASN D 4 999  ? 132.647 139.155 130.251 1.00 35.06  ? 996  ASN A CG    1 
ATOM   8957  O OD1   . ASN D 4 999  ? 133.695 138.886 130.837 1.00 35.06  ? 996  ASN A OD1   1 
ATOM   8958  N ND2   . ASN D 4 999  ? 131.551 139.549 130.888 1.00 35.06  ? 996  ASN A ND2   1 
ATOM   8959  N N     . PHE D 4 1000 ? 133.142 140.129 125.818 1.00 37.92  ? 997  PHE A N     1 
ATOM   8960  C CA    . PHE D 4 1000 ? 132.865 139.966 124.397 1.00 37.92  ? 997  PHE A CA    1 
ATOM   8961  C C     . PHE D 4 1000 ? 133.897 140.717 123.567 1.00 37.92  ? 997  PHE A C     1 
ATOM   8962  O O     . PHE D 4 1000 ? 134.187 141.887 123.834 1.00 37.92  ? 997  PHE A O     1 
ATOM   8963  C CB    . PHE D 4 1000 ? 131.459 140.463 124.060 1.00 37.92  ? 997  PHE A CB    1 
ATOM   8964  C CG    . PHE D 4 1000 ? 130.374 139.781 124.839 1.00 37.92  ? 997  PHE A CG    1 
ATOM   8965  C CD1   . PHE D 4 1000 ? 129.948 138.511 124.491 1.00 37.92  ? 997  PHE A CD1   1 
ATOM   8966  C CD2   . PHE D 4 1000 ? 129.778 140.409 125.918 1.00 37.92  ? 997  PHE A CD2   1 
ATOM   8967  C CE1   . PHE D 4 1000 ? 128.949 137.881 125.204 1.00 37.92  ? 997  PHE A CE1   1 
ATOM   8968  C CE2   . PHE D 4 1000 ? 128.779 139.784 126.636 1.00 37.92  ? 997  PHE A CE2   1 
ATOM   8969  C CZ    . PHE D 4 1000 ? 128.364 138.518 126.278 1.00 37.92  ? 997  PHE A CZ    1 
ATOM   8970  N N     . GLY D 4 1001 ? 134.448 140.039 122.564 1.00 49.31  ? 998  GLY A N     1 
ATOM   8971  C CA    . GLY D 4 1001 ? 135.345 140.663 121.617 1.00 49.31  ? 998  GLY A CA    1 
ATOM   8972  C C     . GLY D 4 1001 ? 136.745 140.864 122.165 1.00 49.31  ? 998  GLY A C     1 
ATOM   8973  O O     . GLY D 4 1001 ? 137.047 140.597 123.329 1.00 49.31  ? 998  GLY A O     1 
ATOM   8974  N N     . PHE D 4 1002 ? 137.621 141.345 121.286 1.00 59.04  ? 999  PHE A N     1 
ATOM   8975  C CA    . PHE D 4 1002 ? 138.982 141.694 121.662 1.00 59.04  ? 999  PHE A CA    1 
ATOM   8976  C C     . PHE D 4 1002 ? 139.446 142.854 120.795 1.00 59.04  ? 999  PHE A C     1 
ATOM   8977  O O     . PHE D 4 1002 ? 138.911 143.089 119.708 1.00 59.04  ? 999  PHE A O     1 
ATOM   8978  C CB    . PHE D 4 1002 ? 139.935 140.493 121.544 1.00 59.04  ? 999  PHE A CB    1 
ATOM   8979  C CG    . PHE D 4 1002 ? 139.917 139.813 120.196 1.00 59.04  ? 999  PHE A CG    1 
ATOM   8980  C CD1   . PHE D 4 1002 ? 140.450 140.429 119.073 1.00 59.04  ? 999  PHE A CD1   1 
ATOM   8981  C CD2   . PHE D 4 1002 ? 139.375 138.545 120.060 1.00 59.04  ? 999  PHE A CD2   1 
ATOM   8982  C CE1   . PHE D 4 1002 ? 140.434 139.798 117.843 1.00 59.04  ? 999  PHE A CE1   1 
ATOM   8983  C CE2   . PHE D 4 1002 ? 139.358 137.908 118.833 1.00 59.04  ? 999  PHE A CE2   1 
ATOM   8984  C CZ    . PHE D 4 1002 ? 139.887 138.535 117.723 1.00 59.04  ? 999  PHE A CZ    1 
ATOM   8985  N N     . LYS D 4 1003 ? 140.444 143.580 121.288 1.00 50.87  ? 1000 LYS A N     1 
ATOM   8986  C CA    . LYS D 4 1003 ? 140.984 144.727 120.576 1.00 50.87  ? 1000 LYS A CA    1 
ATOM   8987  C C     . LYS D 4 1003 ? 142.217 144.323 119.781 1.00 50.87  ? 1000 LYS A C     1 
ATOM   8988  O O     . LYS D 4 1003 ? 143.015 143.493 120.225 1.00 50.87  ? 1000 LYS A O     1 
ATOM   8989  C CB    . LYS D 4 1003 ? 141.335 145.853 121.549 1.00 50.87  ? 1000 LYS A CB    1 
ATOM   8990  C CG    . LYS D 4 1003 ? 140.156 146.360 122.360 1.00 50.87  ? 1000 LYS A CG    1 
ATOM   8991  C CD    . LYS D 4 1003 ? 139.046 146.882 121.462 1.00 50.87  ? 1000 LYS A CD    1 
ATOM   8992  C CE    . LYS D 4 1003 ? 139.480 148.128 120.710 1.00 50.87  ? 1000 LYS A CE    1 
ATOM   8993  N NZ    . LYS D 4 1003 ? 138.313 148.926 120.242 1.00 50.87  ? 1000 LYS A NZ    1 
ATOM   8994  N N     . SER D 4 1004 ? 142.365 144.917 118.600 1.00 55.59  ? 1001 SER A N     1 
ATOM   8995  C CA    . SER D 4 1004 ? 143.518 144.636 117.762 1.00 55.59  ? 1001 SER A CA    1 
ATOM   8996  C C     . SER D 4 1004 ? 144.791 145.174 118.407 1.00 55.59  ? 1001 SER A C     1 
ATOM   8997  O O     . SER D 4 1004 ? 144.759 146.007 119.316 1.00 55.59  ? 1001 SER A O     1 
ATOM   8998  C CB    . SER D 4 1004 ? 143.333 145.249 116.375 1.00 55.59  ? 1001 SER A CB    1 
ATOM   8999  O OG    . SER D 4 1004 ? 144.544 145.228 115.641 1.00 55.59  ? 1001 SER A OG    1 
ATOM   9000  N N     . LYS D 4 1005 ? 145.931 144.681 117.921 1.00 56.43  ? 1002 LYS A N     1 
ATOM   9001  C CA    . LYS D 4 1005 ? 147.222 145.108 118.445 1.00 56.43  ? 1002 LYS A CA    1 
ATOM   9002  C C     . LYS D 4 1005 ? 147.514 146.578 118.177 1.00 56.43  ? 1002 LYS A C     1 
ATOM   9003  O O     . LYS D 4 1005 ? 148.422 147.133 118.804 1.00 56.43  ? 1002 LYS A O     1 
ATOM   9004  C CB    . LYS D 4 1005 ? 148.338 144.245 117.853 1.00 56.43  ? 1002 LYS A CB    1 
ATOM   9005  C CG    . LYS D 4 1005 ? 148.549 144.441 116.360 1.00 56.43  ? 1002 LYS A CG    1 
ATOM   9006  C CD    . LYS D 4 1005 ? 149.663 143.547 115.839 1.00 56.43  ? 1002 LYS A CD    1 
ATOM   9007  C CE    . LYS D 4 1005 ? 149.857 143.721 114.340 1.00 56.43  ? 1002 LYS A CE    1 
ATOM   9008  N NZ    . LYS D 4 1005 ? 150.376 145.073 113.997 1.00 56.43  ? 1002 LYS A NZ    1 
ATOM   9009  N N     . ARG D 4 1006 ? 146.776 147.218 117.266 1.00 52.66  ? 1003 ARG A N     1 
ATOM   9010  C CA    . ARG D 4 1006 ? 147.007 148.626 116.974 1.00 52.66  ? 1003 ARG A CA    1 
ATOM   9011  C C     . ARG D 4 1006 ? 146.571 149.537 118.112 1.00 52.66  ? 1003 ARG A C     1 
ATOM   9012  O O     . ARG D 4 1006 ? 147.074 150.660 118.215 1.00 52.66  ? 1003 ARG A O     1 
ATOM   9013  C CB    . ARG D 4 1006 ? 146.281 149.021 115.688 1.00 52.66  ? 1003 ARG A CB    1 
ATOM   9014  C CG    . ARG D 4 1006 ? 146.903 148.453 114.425 1.00 52.66  ? 1003 ARG A CG    1 
ATOM   9015  C CD    . ARG D 4 1006 ? 146.088 148.819 113.196 1.00 52.66  ? 1003 ARG A CD    1 
ATOM   9016  N NE    . ARG D 4 1006 ? 144.697 148.400 113.319 1.00 52.66  ? 1003 ARG A NE    1 
ATOM   9017  C CZ    . ARG D 4 1006 ? 144.271 147.152 113.177 1.00 52.66  ? 1003 ARG A CZ    1 
ATOM   9018  N NH1   . ARG D 4 1006 ? 145.106 146.164 112.900 1.00 52.66  ? 1003 ARG A NH1   1 
ATOM   9019  N NH2   . ARG D 4 1006 ? 142.975 146.889 113.317 1.00 52.66  ? 1003 ARG A NH2   1 
ATOM   9020  N N     . THR D 4 1007 ? 145.649 149.088 118.959 1.00 46.30  ? 1004 THR A N     1 
ATOM   9021  C CA    . THR D 4 1007 ? 145.198 149.907 120.073 1.00 46.30  ? 1004 THR A CA    1 
ATOM   9022  C C     . THR D 4 1007 ? 146.305 150.064 121.109 1.00 46.30  ? 1004 THR A C     1 
ATOM   9023  O O     . THR D 4 1007 ? 147.111 149.158 121.334 1.00 46.30  ? 1004 THR A O     1 
ATOM   9024  C CB    . THR D 4 1007 ? 143.960 149.296 120.728 1.00 46.30  ? 1004 THR A CB    1 
ATOM   9025  O OG1   . THR D 4 1007 ? 144.289 148.008 121.262 1.00 46.30  ? 1004 THR A OG1   1 
ATOM   9026  C CG2   . THR D 4 1007 ? 142.845 149.144 119.711 1.00 46.30  ? 1004 THR A CG2   1 
ATOM   9027  N N     . GLY D 4 1008 ? 146.340 151.238 121.739 1.00 39.95  ? 1005 GLY A N     1 
ATOM   9028  C CA    . GLY D 4 1008 ? 147.358 151.495 122.743 1.00 39.95  ? 1005 GLY A CA    1 
ATOM   9029  C C     . GLY D 4 1008 ? 147.197 150.635 123.982 1.00 39.95  ? 1005 GLY A C     1 
ATOM   9030  O O     . GLY D 4 1008 ? 148.185 150.188 124.569 1.00 39.95  ? 1005 GLY A O     1 
ATOM   9031  N N     . ILE D 4 1009 ? 145.962 150.392 124.393 1.00 36.24  ? 1006 ILE A N     1 
ATOM   9032  C CA    . ILE D 4 1009 ? 145.675 149.652 125.616 1.00 36.24  ? 1006 ILE A CA    1 
ATOM   9033  C C     . ILE D 4 1009 ? 145.579 148.167 125.298 1.00 36.24  ? 1006 ILE A C     1 
ATOM   9034  O O     . ILE D 4 1009 ? 144.985 147.767 124.290 1.00 36.24  ? 1006 ILE A O     1 
ATOM   9035  C CB    . ILE D 4 1009 ? 144.383 150.171 126.274 1.00 36.24  ? 1006 ILE A CB    1 
ATOM   9036  C CG1   . ILE D 4 1009 ? 144.542 151.639 126.674 1.00 36.24  ? 1006 ILE A CG1   1 
ATOM   9037  C CG2   . ILE D 4 1009 ? 144.025 149.337 127.490 1.00 36.24  ? 1006 ILE A CG2   1 
ATOM   9038  C CD1   . ILE D 4 1009 ? 145.845 151.945 127.377 1.00 36.24  ? 1006 ILE A CD1   1 
ATOM   9039  N N     . ALA D 4 1010 ? 146.168 147.345 126.165 1.00 42.45  ? 1007 ALA A N     1 
ATOM   9040  C CA    . ALA D 4 1010 ? 146.162 145.901 125.986 1.00 42.45  ? 1007 ALA A CA    1 
ATOM   9041  C C     . ALA D 4 1010 ? 144.749 145.347 126.169 1.00 42.45  ? 1007 ALA A C     1 
ATOM   9042  O O     . ALA D 4 1010 ? 143.789 146.075 126.436 1.00 42.45  ? 1007 ALA A O     1 
ATOM   9043  C CB    . ALA D 4 1010 ? 147.136 145.242 126.959 1.00 42.45  ? 1007 ALA A CB    1 
ATOM   9044  N N     . GLU D 4 1011 ? 144.626 144.030 126.029 1.00 49.56  ? 1008 GLU A N     1 
ATOM   9045  C CA    . GLU D 4 1011 ? 143.335 143.351 126.056 1.00 49.56  ? 1008 GLU A CA    1 
ATOM   9046  C C     . GLU D 4 1011 ? 143.138 142.692 127.417 1.00 49.56  ? 1008 GLU A C     1 
ATOM   9047  O O     . GLU D 4 1011 ? 143.875 141.770 127.781 1.00 49.56  ? 1008 GLU A O     1 
ATOM   9048  C CB    . GLU D 4 1011 ? 143.246 142.322 124.931 1.00 49.56  ? 1008 GLU A CB    1 
ATOM   9049  C CG    . GLU D 4 1011 ? 141.849 141.767 124.698 1.00 49.56  ? 1008 GLU A CG    1 
ATOM   9050  C CD    . GLU D 4 1011 ? 141.647 140.404 125.333 1.00 49.56  ? 1008 GLU A CD    1 
ATOM   9051  O OE1   . GLU D 4 1011 ? 142.612 139.612 125.364 1.00 49.56  ? 1008 GLU A OE1   1 
ATOM   9052  O OE2   . GLU D 4 1011 ? 140.523 140.126 125.801 1.00 49.56  ? 1008 GLU A OE2   1 
ATOM   9053  N N     . LYS D 4 1012 ? 142.156 143.183 128.174 1.00 40.51  ? 1009 LYS A N     1 
ATOM   9054  C CA    . LYS D 4 1012 ? 141.629 142.579 129.395 1.00 40.51  ? 1009 LYS A CA    1 
ATOM   9055  C C     . LYS D 4 1012 ? 142.628 142.600 130.549 1.00 40.51  ? 1009 LYS A C     1 
ATOM   9056  O O     . LYS D 4 1012 ? 142.261 142.250 131.676 1.00 40.51  ? 1009 LYS A O     1 
ATOM   9057  C CB    . LYS D 4 1012 ? 141.153 141.136 129.150 1.00 40.51  ? 1009 LYS A CB    1 
ATOM   9058  C CG    . LYS D 4 1012 ? 140.315 140.515 130.260 1.00 40.51  ? 1009 LYS A CG    1 
ATOM   9059  C CD    . LYS D 4 1012 ? 139.962 139.073 129.938 1.00 40.51  ? 1009 LYS A CD    1 
ATOM   9060  C CE    . LYS D 4 1012 ? 138.920 138.990 128.838 1.00 40.51  ? 1009 LYS A CE    1 
ATOM   9061  N NZ    . LYS D 4 1012 ? 137.593 139.472 129.305 1.00 40.51  ? 1009 LYS A NZ    1 
ATOM   9062  N N     . ALA D 4 1013 ? 143.867 143.032 130.324 1.00 38.18  ? 1010 ALA A N     1 
ATOM   9063  C CA    . ALA D 4 1013 ? 144.866 143.024 131.388 1.00 38.18  ? 1010 ALA A CA    1 
ATOM   9064  C C     . ALA D 4 1013 ? 144.863 144.338 132.163 1.00 38.18  ? 1010 ALA A C     1 
ATOM   9065  O O     . ALA D 4 1013 ? 144.648 144.351 133.379 1.00 38.18  ? 1010 ALA A O     1 
ATOM   9066  C CB    . ALA D 4 1013 ? 146.254 142.741 130.804 1.00 38.18  ? 1010 ALA A CB    1 
ATOM   9067  N N     . VAL D 4 1014 ? 145.094 145.448 131.469 1.00 50.26  ? 1011 VAL A N     1 
ATOM   9068  C CA    . VAL D 4 1014 ? 145.116 146.757 132.110 1.00 50.26  ? 1011 VAL A CA    1 
ATOM   9069  C C     . VAL D 4 1014 ? 143.724 147.369 132.169 1.00 50.26  ? 1011 VAL A C     1 
ATOM   9070  O O     . VAL D 4 1014 ? 143.334 147.936 133.192 1.00 50.26  ? 1011 VAL A O     1 
ATOM   9071  C CB    . VAL D 4 1014 ? 146.106 147.681 131.374 1.00 50.26  ? 1011 VAL A CB    1 
ATOM   9072  C CG1   . VAL D 4 1014 ? 146.008 149.098 131.906 1.00 50.26  ? 1011 VAL A CG1   1 
ATOM   9073  C CG2   . VAL D 4 1014 ? 147.523 147.155 131.511 1.00 50.26  ? 1011 VAL A CG2   1 
ATOM   9074  N N     . TYR D 4 1015 ? 142.961 147.260 131.080 1.00 50.26  ? 1012 TYR A N     1 
ATOM   9075  C CA    . TYR D 4 1015 ? 141.652 147.903 131.024 1.00 50.26  ? 1012 TYR A CA    1 
ATOM   9076  C C     . TYR D 4 1015 ? 140.698 147.324 132.060 1.00 50.26  ? 1012 TYR A C     1 
ATOM   9077  O O     . TYR D 4 1015 ? 139.920 148.061 132.675 1.00 50.26  ? 1012 TYR A O     1 
ATOM   9078  C CB    . TYR D 4 1015 ? 141.061 147.771 129.624 1.00 50.26  ? 1012 TYR A CB    1 
ATOM   9079  C CG    . TYR D 4 1015 ? 140.016 148.814 129.315 1.00 50.26  ? 1012 TYR A CG    1 
ATOM   9080  C CD1   . TYR D 4 1015 ? 140.344 150.161 129.281 1.00 50.26  ? 1012 TYR A CD1   1 
ATOM   9081  C CD2   . TYR D 4 1015 ? 138.701 148.453 129.064 1.00 50.26  ? 1012 TYR A CD2   1 
ATOM   9082  C CE1   . TYR D 4 1015 ? 139.393 151.119 128.999 1.00 50.26  ? 1012 TYR A CE1   1 
ATOM   9083  C CE2   . TYR D 4 1015 ? 137.743 149.403 128.782 1.00 50.26  ? 1012 TYR A CE2   1 
ATOM   9084  C CZ    . TYR D 4 1015 ? 138.094 150.734 128.751 1.00 50.26  ? 1012 TYR A CZ    1 
ATOM   9085  O OH    . TYR D 4 1015 ? 137.143 151.685 128.469 1.00 50.26  ? 1012 TYR A OH    1 
ATOM   9086  N N     . GLN D 4 1016 ? 140.737 146.006 132.264 1.00 50.26  ? 1013 GLN A N     1 
ATOM   9087  C CA    . GLN D 4 1016 ? 139.843 145.390 133.238 1.00 50.26  ? 1013 GLN A CA    1 
ATOM   9088  C C     . GLN D 4 1016 ? 140.112 145.918 134.640 1.00 50.26  ? 1013 GLN A C     1 
ATOM   9089  O O     . GLN D 4 1016 ? 139.178 146.141 135.418 1.00 50.26  ? 1013 GLN A O     1 
ATOM   9090  C CB    . GLN D 4 1016 ? 139.988 143.871 133.196 1.00 50.26  ? 1013 GLN A CB    1 
ATOM   9091  C CG    . GLN D 4 1016 ? 138.934 143.127 133.989 1.00 50.26  ? 1013 GLN A CG    1 
ATOM   9092  C CD    . GLN D 4 1016 ? 138.671 141.739 133.444 1.00 50.26  ? 1013 GLN A CD    1 
ATOM   9093  O OE1   . GLN D 4 1016 ? 137.724 141.527 132.687 1.00 50.26  ? 1013 GLN A OE1   1 
ATOM   9094  N NE2   . GLN D 4 1016 ? 139.510 140.785 133.825 1.00 50.26  ? 1013 GLN A NE2   1 
ATOM   9095  N N     . GLN D 4 1017 ? 141.385 146.120 134.983 1.00 50.26  ? 1014 GLN A N     1 
ATOM   9096  C CA    . GLN D 4 1017 ? 141.713 146.752 136.255 1.00 50.26  ? 1014 GLN A CA    1 
ATOM   9097  C C     . GLN D 4 1017 ? 141.232 148.196 136.299 1.00 50.26  ? 1014 GLN A C     1 
ATOM   9098  O O     . GLN D 4 1017 ? 140.853 148.689 137.367 1.00 50.26  ? 1014 GLN A O     1 
ATOM   9099  C CB    . GLN D 4 1017 ? 143.220 146.687 136.502 1.00 50.26  ? 1014 GLN A CB    1 
ATOM   9100  C CG    . GLN D 4 1017 ? 143.647 147.168 137.877 1.00 50.26  ? 1014 GLN A CG    1 
ATOM   9101  C CD    . GLN D 4 1017 ? 143.408 146.134 138.959 1.00 50.26  ? 1014 GLN A CD    1 
ATOM   9102  O OE1   . GLN D 4 1017 ? 142.914 145.039 138.691 1.00 50.26  ? 1014 GLN A OE1   1 
ATOM   9103  N NE2   . GLN D 4 1017 ? 143.757 146.479 140.193 1.00 50.26  ? 1014 GLN A NE2   1 
ATOM   9104  N N     . PHE D 4 1018 ? 141.242 148.884 135.156 1.00 50.26  ? 1015 PHE A N     1 
ATOM   9105  C CA    . PHE D 4 1018 ? 140.767 150.262 135.113 1.00 50.26  ? 1015 PHE A CA    1 
ATOM   9106  C C     . PHE D 4 1018 ? 139.285 150.349 135.456 1.00 50.26  ? 1015 PHE A C     1 
ATOM   9107  O O     . PHE D 4 1018 ? 138.856 151.279 136.146 1.00 50.26  ? 1015 PHE A O     1 
ATOM   9108  C CB    . PHE D 4 1018 ? 141.037 150.865 133.736 1.00 50.26  ? 1015 PHE A CB    1 
ATOM   9109  C CG    . PHE D 4 1018 ? 140.063 151.932 133.340 1.00 50.26  ? 1015 PHE A CG    1 
ATOM   9110  C CD1   . PHE D 4 1018 ? 140.111 153.185 133.921 1.00 50.26  ? 1015 PHE A CD1   1 
ATOM   9111  C CD2   . PHE D 4 1018 ? 139.099 151.682 132.381 1.00 50.26  ? 1015 PHE A CD2   1 
ATOM   9112  C CE1   . PHE D 4 1018 ? 139.216 154.164 133.552 1.00 50.26  ? 1015 PHE A CE1   1 
ATOM   9113  C CE2   . PHE D 4 1018 ? 138.202 152.658 132.012 1.00 50.26  ? 1015 PHE A CE2   1 
ATOM   9114  C CZ    . PHE D 4 1018 ? 138.260 153.899 132.599 1.00 50.26  ? 1015 PHE A CZ    1 
ATOM   9115  N N     . GLU D 4 1019 ? 138.484 149.397 134.973 1.00 50.26  ? 1016 GLU A N     1 
ATOM   9116  C CA    . GLU D 4 1019 ? 137.062 149.396 135.303 1.00 50.26  ? 1016 GLU A CA    1 
ATOM   9117  C C     . GLU D 4 1019 ? 136.844 149.183 136.795 1.00 50.26  ? 1016 GLU A C     1 
ATOM   9118  O O     . GLU D 4 1019 ? 135.988 149.836 137.406 1.00 50.26  ? 1016 GLU A O     1 
ATOM   9119  C CB    . GLU D 4 1019 ? 136.342 148.321 134.491 1.00 50.26  ? 1016 GLU A CB    1 
ATOM   9120  C CG    . GLU D 4 1019 ? 136.760 148.279 133.034 1.00 50.26  ? 1016 GLU A CG    1 
ATOM   9121  C CD    . GLU D 4 1019 ? 135.661 147.784 132.120 1.00 50.26  ? 1016 GLU A CD    1 
ATOM   9122  O OE1   . GLU D 4 1019 ? 134.736 147.107 132.613 1.00 50.26  ? 1016 GLU A OE1   1 
ATOM   9123  O OE2   . GLU D 4 1019 ? 135.723 148.071 130.907 1.00 50.26  ? 1016 GLU A OE2   1 
ATOM   9124  N N     . LYS D 4 1020 ? 137.611 148.273 137.400 1.00 50.26  ? 1017 LYS A N     1 
ATOM   9125  C CA    . LYS D 4 1020 ? 137.515 148.061 138.840 1.00 50.26  ? 1017 LYS A CA    1 
ATOM   9126  C C     . LYS D 4 1020 ? 137.909 149.316 139.606 1.00 50.26  ? 1017 LYS A C     1 
ATOM   9127  O O     . LYS D 4 1020 ? 137.263 149.679 140.597 1.00 50.26  ? 1017 LYS A O     1 
ATOM   9128  C CB    . LYS D 4 1020 ? 138.396 146.884 139.254 1.00 50.26  ? 1017 LYS A CB    1 
ATOM   9129  C CG    . LYS D 4 1020 ? 138.165 146.398 140.672 1.00 50.26  ? 1017 LYS A CG    1 
ATOM   9130  C CD    . LYS D 4 1020 ? 139.195 145.352 141.067 1.00 50.26  ? 1017 LYS A CD    1 
ATOM   9131  C CE    . LYS D 4 1020 ? 140.414 145.990 141.709 1.00 50.26  ? 1017 LYS A CE    1 
ATOM   9132  N NZ    . LYS D 4 1020 ? 140.283 146.065 143.189 1.00 50.26  ? 1017 LYS A NZ    1 
ATOM   9133  N N     . MET D 4 1021 ? 138.971 149.991 139.162 1.00 50.26  ? 1018 MET A N     1 
ATOM   9134  C CA    . MET D 4 1021 ? 139.394 151.217 139.828 1.00 50.26  ? 1018 MET A CA    1 
ATOM   9135  C C     . MET D 4 1021 ? 138.342 152.309 139.693 1.00 50.26  ? 1018 MET A C     1 
ATOM   9136  O O     . MET D 4 1021 ? 138.108 153.072 140.636 1.00 50.26  ? 1018 MET A O     1 
ATOM   9137  C CB    . MET D 4 1021 ? 140.736 151.683 139.268 1.00 50.26  ? 1018 MET A CB    1 
ATOM   9138  C CG    . MET D 4 1021 ? 141.905 150.784 139.622 1.00 50.26  ? 1018 MET A CG    1 
ATOM   9139  S SD    . MET D 4 1021 ? 143.477 151.665 139.611 1.00 50.26  ? 1018 MET A SD    1 
ATOM   9140  C CE    . MET D 4 1021 ? 143.869 151.640 137.863 1.00 50.26  ? 1018 MET A CE    1 
ATOM   9141  N N     . LEU D 4 1022 ? 137.698 152.404 138.528 1.00 50.26  ? 1019 LEU A N     1 
ATOM   9142  C CA    . LEU D 4 1022 ? 136.631 153.385 138.351 1.00 50.26  ? 1019 LEU A CA    1 
ATOM   9143  C C     . LEU D 4 1022 ? 135.443 153.080 139.254 1.00 50.26  ? 1019 LEU A C     1 
ATOM   9144  O O     . LEU D 4 1022 ? 134.853 153.995 139.842 1.00 50.26  ? 1019 LEU A O     1 
ATOM   9145  C CB    . LEU D 4 1022 ? 136.193 153.429 136.888 1.00 50.26  ? 1019 LEU A CB    1 
ATOM   9146  C CG    . LEU D 4 1022 ? 135.112 154.453 136.544 1.00 50.26  ? 1019 LEU A CG    1 
ATOM   9147  C CD1   . LEU D 4 1022 ? 135.535 155.842 136.983 1.00 50.26  ? 1019 LEU A CD1   1 
ATOM   9148  C CD2   . LEU D 4 1022 ? 134.813 154.431 135.057 1.00 50.26  ? 1019 LEU A CD2   1 
ATOM   9149  N N     . ILE D 4 1023 ? 135.076 151.803 139.374 1.00 50.26  ? 1020 ILE A N     1 
ATOM   9150  C CA    . ILE D 4 1023 ? 133.984 151.428 140.270 1.00 50.26  ? 1020 ILE A CA    1 
ATOM   9151  C C     . ILE D 4 1023 ? 134.331 151.788 141.708 1.00 50.26  ? 1020 ILE A C     1 
ATOM   9152  O O     . ILE D 4 1023 ? 133.504 152.341 142.444 1.00 50.26  ? 1020 ILE A O     1 
ATOM   9153  C CB    . ILE D 4 1023 ? 133.659 149.931 140.125 1.00 50.26  ? 1020 ILE A CB    1 
ATOM   9154  C CG1   . ILE D 4 1023 ? 132.964 149.660 138.793 1.00 50.26  ? 1020 ILE A CG1   1 
ATOM   9155  C CG2   . ILE D 4 1023 ? 132.788 149.459 141.273 1.00 50.26  ? 1020 ILE A CG2   1 
ATOM   9156  C CD1   . ILE D 4 1023 ? 132.748 148.193 138.517 1.00 50.26  ? 1020 ILE A CD1   1 
ATOM   9157  N N     . ASP D 4 1024 ? 135.562 151.486 142.130 1.00 50.26  ? 1021 ASP A N     1 
ATOM   9158  C CA    . ASP D 4 1024 ? 135.980 151.819 143.488 1.00 50.26  ? 1021 ASP A CA    1 
ATOM   9159  C C     . ASP D 4 1024 ? 135.974 153.325 143.715 1.00 50.26  ? 1021 ASP A C     1 
ATOM   9160  O O     . ASP D 4 1024 ? 135.565 153.799 144.781 1.00 50.26  ? 1021 ASP A O     1 
ATOM   9161  C CB    . ASP D 4 1024 ? 137.365 151.238 143.766 1.00 50.26  ? 1021 ASP A CB    1 
ATOM   9162  C CG    . ASP D 4 1024 ? 137.370 149.725 143.771 1.00 50.26  ? 1021 ASP A CG    1 
ATOM   9163  O OD1   . ASP D 4 1024 ? 136.283 149.127 143.904 1.00 50.26  ? 1021 ASP A OD1   1 
ATOM   9164  O OD2   . ASP D 4 1024 ? 138.462 149.132 143.641 1.00 50.26  ? 1021 ASP A OD2   1 
ATOM   9165  N N     . LYS D 4 1025 ? 136.429 154.093 142.723 1.00 50.26  ? 1022 LYS A N     1 
ATOM   9166  C CA    . LYS D 4 1025 ? 136.422 155.546 142.843 1.00 50.26  ? 1022 LYS A CA    1 
ATOM   9167  C C     . LYS D 4 1025 ? 135.004 156.079 142.980 1.00 50.26  ? 1022 LYS A C     1 
ATOM   9168  O O     . LYS D 4 1025 ? 134.743 156.970 143.797 1.00 50.26  ? 1022 LYS A O     1 
ATOM   9169  C CB    . LYS D 4 1025 ? 137.118 156.170 141.633 1.00 50.26  ? 1022 LYS A CB    1 
ATOM   9170  C CG    . LYS D 4 1025 ? 136.839 157.648 141.435 1.00 50.26  ? 1022 LYS A CG    1 
ATOM   9171  C CD    . LYS D 4 1025 ? 137.366 158.477 142.592 1.00 50.26  ? 1022 LYS A CD    1 
ATOM   9172  C CE    . LYS D 4 1025 ? 137.887 159.816 142.108 1.00 50.26  ? 1022 LYS A CE    1 
ATOM   9173  N NZ    . LYS D 4 1025 ? 138.289 160.691 143.239 1.00 50.26  ? 1022 LYS A NZ    1 
ATOM   9174  N N     . LEU D 4 1026 ? 134.071 155.543 142.197 1.00 50.26  ? 1023 LEU A N     1 
ATOM   9175  C CA    . LEU D 4 1026 ? 132.697 156.023 142.249 1.00 50.26  ? 1023 LEU A CA    1 
ATOM   9176  C C     . LEU D 4 1026 ? 131.912 155.468 143.429 1.00 50.26  ? 1023 LEU A C     1 
ATOM   9177  O O     . LEU D 4 1026 ? 130.811 155.959 143.699 1.00 50.26  ? 1023 LEU A O     1 
ATOM   9178  C CB    . LEU D 4 1026 ? 131.981 155.693 140.941 1.00 50.26  ? 1023 LEU A CB    1 
ATOM   9179  C CG    . LEU D 4 1026 ? 132.399 156.585 139.773 1.00 50.26  ? 1023 LEU A CG    1 
ATOM   9180  C CD1   . LEU D 4 1026 ? 131.365 156.538 138.680 1.00 50.26  ? 1023 LEU A CD1   1 
ATOM   9181  C CD2   . LEU D 4 1026 ? 132.598 158.010 140.246 1.00 50.26  ? 1023 LEU A CD2   1 
ATOM   9182  N N     . ASN D 4 1027 ? 132.440 154.464 144.133 1.00 50.26  ? 1024 ASN A N     1 
ATOM   9183  C CA    . ASN D 4 1027 ? 131.797 154.020 145.366 1.00 50.26  ? 1024 ASN A CA    1 
ATOM   9184  C C     . ASN D 4 1027 ? 131.783 155.135 146.402 1.00 50.26  ? 1024 ASN A C     1 
ATOM   9185  O O     . ASN D 4 1027 ? 130.812 155.288 147.152 1.00 50.26  ? 1024 ASN A O     1 
ATOM   9186  C CB    . ASN D 4 1027 ? 132.508 152.786 145.920 1.00 50.26  ? 1024 ASN A CB    1 
ATOM   9187  C CG    . ASN D 4 1027 ? 132.154 151.525 145.167 1.00 50.26  ? 1024 ASN A CG    1 
ATOM   9188  O OD1   . ASN D 4 1027 ? 131.305 151.538 144.277 1.00 50.26  ? 1024 ASN A OD1   1 
ATOM   9189  N ND2   . ASN D 4 1027 ? 132.803 150.423 145.521 1.00 50.26  ? 1024 ASN A ND2   1 
ATOM   9190  N N     . CYS D 4 1028 ? 132.858 155.919 146.461 1.00 50.26  ? 1025 CYS A N     1 
ATOM   9191  C CA    . CYS D 4 1028 ? 132.941 157.086 147.340 1.00 50.26  ? 1025 CYS A CA    1 
ATOM   9192  C C     . CYS D 4 1028 ? 133.758 158.142 146.595 1.00 50.26  ? 1025 CYS A C     1 
ATOM   9193  O O     . CYS D 4 1028 ? 134.989 158.153 146.662 1.00 50.26  ? 1025 CYS A O     1 
ATOM   9194  C CB    . CYS D 4 1028 ? 133.566 156.733 148.680 1.00 50.26  ? 1025 CYS A CB    1 
ATOM   9195  S SG    . CYS D 4 1028 ? 133.747 158.126 149.805 1.00 50.26  ? 1025 CYS A SG    1 
ATOM   9196  N N     . LEU D 4 1029 ? 133.058 159.025 145.892 1.00 50.26  ? 1026 LEU A N     1 
ATOM   9197  C CA    . LEU D 4 1029 ? 133.687 160.025 145.041 1.00 50.26  ? 1026 LEU A CA    1 
ATOM   9198  C C     . LEU D 4 1029 ? 133.681 161.368 145.756 1.00 50.26  ? 1026 LEU A C     1 
ATOM   9199  O O     . LEU D 4 1029 ? 132.618 161.872 146.132 1.00 50.26  ? 1026 LEU A O     1 
ATOM   9200  C CB    . LEU D 4 1029 ? 132.962 160.127 143.700 1.00 50.26  ? 1026 LEU A CB    1 
ATOM   9201  C CG    . LEU D 4 1029 ? 133.189 161.397 142.880 1.00 50.26  ? 1026 LEU A CG    1 
ATOM   9202  C CD1   . LEU D 4 1029 ? 134.645 161.532 142.474 1.00 50.26  ? 1026 LEU A CD1   1 
ATOM   9203  C CD2   . LEU D 4 1029 ? 132.294 161.398 141.659 1.00 50.26  ? 1026 LEU A CD2   1 
ATOM   9204  N N     . VAL D 4 1030 ? 134.865 161.945 145.935 1.00 50.26  ? 1027 VAL A N     1 
ATOM   9205  C CA    . VAL D 4 1030 ? 135.027 163.263 146.533 1.00 50.26  ? 1027 VAL A CA    1 
ATOM   9206  C C     . VAL D 4 1030 ? 135.828 164.130 145.572 1.00 50.26  ? 1027 VAL A C     1 
ATOM   9207  O O     . VAL D 4 1030 ? 136.847 163.689 145.026 1.00 50.26  ? 1027 VAL A O     1 
ATOM   9208  C CB    . VAL D 4 1030 ? 135.700 163.182 147.917 1.00 50.26  ? 1027 VAL A CB    1 
ATOM   9209  C CG1   . VAL D 4 1030 ? 137.071 162.550 147.821 1.00 50.26  ? 1027 VAL A CG1   1 
ATOM   9210  C CG2   . VAL D 4 1030 ? 135.812 164.562 148.524 1.00 50.26  ? 1027 VAL A CG2   1 
ATOM   9211  N N     . LEU D 4 1031 ? 135.347 165.345 145.337 1.00 50.26  ? 1028 LEU A N     1 
ATOM   9212  C CA    . LEU D 4 1031 ? 136.019 166.300 144.468 1.00 50.26  ? 1028 LEU A CA    1 
ATOM   9213  C C     . LEU D 4 1031 ? 136.694 167.351 145.338 1.00 50.26  ? 1028 LEU A C     1 
ATOM   9214  O O     . LEU D 4 1031 ? 136.038 167.993 146.165 1.00 50.26  ? 1028 LEU A O     1 
ATOM   9215  C CB    . LEU D 4 1031 ? 135.030 166.941 143.496 1.00 50.26  ? 1028 LEU A CB    1 
ATOM   9216  C CG    . LEU D 4 1031 ? 134.169 165.938 142.727 1.00 50.26  ? 1028 LEU A CG    1 
ATOM   9217  C CD1   . LEU D 4 1031 ? 132.904 166.592 142.212 1.00 50.26  ? 1028 LEU A CD1   1 
ATOM   9218  C CD2   . LEU D 4 1031 ? 134.955 165.322 141.585 1.00 50.26  ? 1028 LEU A CD2   1 
ATOM   9219  N N     . LYS D 4 1032 ? 138.001 167.527 145.148 1.00 50.26  ? 1029 LYS A N     1 
ATOM   9220  C CA    . LYS D 4 1032 ? 138.775 168.366 146.053 1.00 50.26  ? 1029 LYS A CA    1 
ATOM   9221  C C     . LYS D 4 1032 ? 138.491 169.851 145.877 1.00 50.26  ? 1029 LYS A C     1 
ATOM   9222  O O     . LYS D 4 1032 ? 138.769 170.632 146.793 1.00 50.26  ? 1029 LYS A O     1 
ATOM   9223  C CB    . LYS D 4 1032 ? 140.266 168.078 145.878 1.00 50.26  ? 1029 LYS A CB    1 
ATOM   9224  C CG    . LYS D 4 1032 ? 140.762 168.108 144.454 1.00 50.26  ? 1029 LYS A CG    1 
ATOM   9225  C CD    . LYS D 4 1032 ? 142.225 167.718 144.411 1.00 50.26  ? 1029 LYS A CD    1 
ATOM   9226  C CE    . LYS D 4 1032 ? 142.414 166.261 144.786 1.00 50.26  ? 1029 LYS A CE    1 
ATOM   9227  N NZ    . LYS D 4 1032 ? 143.836 165.845 144.653 1.00 50.26  ? 1029 LYS A NZ    1 
ATOM   9228  N N     . ASP D 4 1033 ? 137.949 170.264 144.731 1.00 50.26  ? 1030 ASP A N     1 
ATOM   9229  C CA    . ASP D 4 1033 ? 137.568 171.663 144.573 1.00 50.26  ? 1030 ASP A CA    1 
ATOM   9230  C C     . ASP D 4 1033 ? 136.252 171.970 145.277 1.00 50.26  ? 1030 ASP A C     1 
ATOM   9231  O O     . ASP D 4 1033 ? 135.991 173.129 145.620 1.00 50.26  ? 1030 ASP A O     1 
ATOM   9232  C CB    . ASP D 4 1033 ? 137.475 172.020 143.091 1.00 50.26  ? 1030 ASP A CB    1 
ATOM   9233  C CG    . ASP D 4 1033 ? 138.836 172.206 142.450 1.00 50.26  ? 1030 ASP A CG    1 
ATOM   9234  O OD1   . ASP D 4 1033 ? 139.853 172.041 143.156 1.00 50.26  ? 1030 ASP A OD1   1 
ATOM   9235  O OD2   . ASP D 4 1033 ? 138.891 172.516 141.242 1.00 50.26  ? 1030 ASP A OD2   1 
ATOM   9236  N N     . TYR D 4 1034 ? 135.421 170.958 145.501 1.00 50.26  ? 1031 TYR A N     1 
ATOM   9237  C CA    . TYR D 4 1034 ? 134.126 171.180 146.126 1.00 50.26  ? 1031 TYR A CA    1 
ATOM   9238  C C     . TYR D 4 1034 ? 134.299 171.529 147.603 1.00 50.26  ? 1031 TYR A C     1 
ATOM   9239  O O     . TYR D 4 1034 ? 135.219 171.028 148.257 1.00 50.26  ? 1031 TYR A O     1 
ATOM   9240  C CB    . TYR D 4 1034 ? 133.244 169.940 145.991 1.00 50.26  ? 1031 TYR A CB    1 
ATOM   9241  C CG    . TYR D 4 1034 ? 132.497 169.843 144.682 1.00 50.26  ? 1031 TYR A CG    1 
ATOM   9242  C CD1   . TYR D 4 1034 ? 132.957 170.491 143.546 1.00 50.26  ? 1031 TYR A CD1   1 
ATOM   9243  C CD2   . TYR D 4 1034 ? 131.329 169.100 144.583 1.00 50.26  ? 1031 TYR A CD2   1 
ATOM   9244  C CE1   . TYR D 4 1034 ? 132.275 170.402 142.349 1.00 50.26  ? 1031 TYR A CE1   1 
ATOM   9245  C CE2   . TYR D 4 1034 ? 130.641 169.007 143.393 1.00 50.26  ? 1031 TYR A CE2   1 
ATOM   9246  C CZ    . TYR D 4 1034 ? 131.118 169.658 142.279 1.00 50.26  ? 1031 TYR A CZ    1 
ATOM   9247  O OH    . TYR D 4 1034 ? 130.436 169.568 141.088 1.00 50.26  ? 1031 TYR A OH    1 
ATOM   9248  N N     . PRO D 4 1035 ? 133.438 172.381 148.154 1.00 50.26  ? 1032 PRO A N     1 
ATOM   9249  C CA    . PRO D 4 1035 ? 133.468 172.621 149.599 1.00 50.26  ? 1032 PRO A CA    1 
ATOM   9250  C C     . PRO D 4 1035 ? 132.981 171.403 150.367 1.00 50.26  ? 1032 PRO A C     1 
ATOM   9251  O O     . PRO D 4 1035 ? 132.245 170.562 149.846 1.00 50.26  ? 1032 PRO A O     1 
ATOM   9252  C CB    . PRO D 4 1035 ? 132.524 173.813 149.783 1.00 50.26  ? 1032 PRO A CB    1 
ATOM   9253  C CG    . PRO D 4 1035 ? 131.606 173.743 148.617 1.00 50.26  ? 1032 PRO A CG    1 
ATOM   9254  C CD    . PRO D 4 1035 ? 132.413 173.193 147.478 1.00 50.26  ? 1032 PRO A CD    1 
ATOM   9255  N N     . ALA D 4 1036 ? 133.410 171.316 151.628 1.00 50.26  ? 1033 ALA A N     1 
ATOM   9256  C CA    . ALA D 4 1036 ? 133.090 170.149 152.443 1.00 50.26  ? 1033 ALA A CA    1 
ATOM   9257  C C     . ALA D 4 1036 ? 131.592 170.031 152.696 1.00 50.26  ? 1033 ALA A C     1 
ATOM   9258  O O     . ALA D 4 1036 ? 131.036 168.926 152.669 1.00 50.26  ? 1033 ALA A O     1 
ATOM   9259  C CB    . ALA D 4 1036 ? 133.854 170.213 153.764 1.00 50.26  ? 1033 ALA A CB    1 
ATOM   9260  N N     . GLU D 4 1037 ? 130.922 171.156 152.955 1.00 50.26  ? 1034 GLU A N     1 
ATOM   9261  C CA    . GLU D 4 1037 ? 129.496 171.118 153.268 1.00 50.26  ? 1034 GLU A CA    1 
ATOM   9262  C C     . GLU D 4 1037 ? 128.672 170.633 152.082 1.00 50.26  ? 1034 GLU A C     1 
ATOM   9263  O O     . GLU D 4 1037 ? 127.740 169.839 152.251 1.00 50.26  ? 1034 GLU A O     1 
ATOM   9264  C CB    . GLU D 4 1037 ? 129.021 172.499 153.716 1.00 29.58  ? 1034 GLU A CB    1 
ATOM   9265  C CG    . GLU D 4 1037 ? 129.637 172.972 155.021 1.00 29.58  ? 1034 GLU A CG    1 
ATOM   9266  C CD    . GLU D 4 1037 ? 129.613 171.909 156.101 1.00 29.58  ? 1034 GLU A CD    1 
ATOM   9267  O OE1   . GLU D 4 1037 ? 128.558 171.268 156.291 1.00 29.58  ? 1034 GLU A OE1   1 
ATOM   9268  O OE2   . GLU D 4 1037 ? 130.655 171.711 156.757 1.00 29.58  ? 1034 GLU A OE2   1 
ATOM   9269  N N     . LYS D 4 1038 ? 128.994 171.103 150.880 1.00 50.26  ? 1035 LYS A N     1 
ATOM   9270  C CA    . LYS D 4 1038 ? 128.238 170.725 149.695 1.00 50.26  ? 1035 LYS A CA    1 
ATOM   9271  C C     . LYS D 4 1038 ? 128.419 169.242 149.397 1.00 50.26  ? 1035 LYS A C     1 
ATOM   9272  O O     . LYS D 4 1038 ? 129.501 168.682 149.590 1.00 50.26  ? 1035 LYS A O     1 
ATOM   9273  C CB    . LYS D 4 1038 ? 128.683 171.572 148.501 1.00 27.73  ? 1035 LYS A CB    1 
ATOM   9274  C CG    . LYS D 4 1038 ? 128.488 170.923 147.141 1.00 27.73  ? 1035 LYS A CG    1 
ATOM   9275  C CD    . LYS D 4 1038 ? 129.298 171.630 146.070 1.00 27.73  ? 1035 LYS A CD    1 
ATOM   9276  C CE    . LYS D 4 1038 ? 128.507 172.759 145.437 1.00 27.73  ? 1035 LYS A CE    1 
ATOM   9277  N NZ    . LYS D 4 1038 ? 129.345 173.568 144.512 1.00 27.73  ? 1035 LYS A NZ    1 
ATOM   9278  N N     . VAL D 4 1039 ? 127.339 168.602 148.939 1.00 50.26  ? 1036 VAL A N     1 
ATOM   9279  C CA    . VAL D 4 1039 ? 127.410 167.194 148.571 1.00 50.26  ? 1036 VAL A CA    1 
ATOM   9280  C C     . VAL D 4 1039 ? 128.447 167.004 147.472 1.00 50.26  ? 1036 VAL A C     1 
ATOM   9281  O O     . VAL D 4 1039 ? 128.543 167.798 146.528 1.00 50.26  ? 1036 VAL A O     1 
ATOM   9282  C CB    . VAL D 4 1039 ? 126.023 166.679 148.148 1.00 50.26  ? 1036 VAL A CB    1 
ATOM   9283  C CG1   . VAL D 4 1039 ? 125.521 167.423 146.925 1.00 50.26  ? 1036 VAL A CG1   1 
ATOM   9284  C CG2   . VAL D 4 1039 ? 126.069 165.184 147.885 1.00 50.26  ? 1036 VAL A CG2   1 
ATOM   9285  N N     . GLY D 4 1040 ? 129.245 165.950 147.605 1.00 50.26  ? 1037 GLY A N     1 
ATOM   9286  C CA    . GLY D 4 1040 ? 130.417 165.758 146.784 1.00 50.26  ? 1037 GLY A CA    1 
ATOM   9287  C C     . GLY D 4 1040 ? 131.713 166.140 147.463 1.00 50.26  ? 1037 GLY A C     1 
ATOM   9288  O O     . GLY D 4 1040 ? 132.786 165.800 146.952 1.00 50.26  ? 1037 GLY A O     1 
ATOM   9289  N N     . GLY D 4 1041 ? 131.643 166.835 148.594 1.00 50.26  ? 1038 GLY A N     1 
ATOM   9290  C CA    . GLY D 4 1041 ? 132.816 167.152 149.375 1.00 50.26  ? 1038 GLY A CA    1 
ATOM   9291  C C     . GLY D 4 1041 ? 133.228 165.992 150.260 1.00 50.26  ? 1038 GLY A C     1 
ATOM   9292  O O     . GLY D 4 1041 ? 132.708 164.879 150.173 1.00 50.26  ? 1038 GLY A O     1 
ATOM   9293  N N     . VAL D 4 1042 ? 134.192 166.272 151.139 1.00 50.26  ? 1039 VAL A N     1 
ATOM   9294  C CA    . VAL D 4 1042 ? 134.747 165.222 151.983 1.00 50.26  ? 1039 VAL A CA    1 
ATOM   9295  C C     . VAL D 4 1042 ? 133.762 164.765 153.053 1.00 50.26  ? 1039 VAL A C     1 
ATOM   9296  O O     . VAL D 4 1042 ? 133.928 163.676 153.614 1.00 50.26  ? 1039 VAL A O     1 
ATOM   9297  C CB    . VAL D 4 1042 ? 136.078 165.697 152.600 1.00 50.26  ? 1039 VAL A CB    1 
ATOM   9298  C CG1   . VAL D 4 1042 ? 135.833 166.695 153.711 1.00 50.26  ? 1039 VAL A CG1   1 
ATOM   9299  C CG2   . VAL D 4 1042 ? 136.892 164.515 153.098 1.00 50.26  ? 1039 VAL A CG2   1 
ATOM   9300  N N     . LEU D 4 1043 ? 132.728 165.555 153.347 1.00 50.26  ? 1040 LEU A N     1 
ATOM   9301  C CA    . LEU D 4 1043 ? 131.719 165.132 154.312 1.00 50.26  ? 1040 LEU A CA    1 
ATOM   9302  C C     . LEU D 4 1043 ? 130.595 164.324 153.674 1.00 50.26  ? 1040 LEU A C     1 
ATOM   9303  O O     . LEU D 4 1043 ? 130.102 163.369 154.284 1.00 50.26  ? 1040 LEU A O     1 
ATOM   9304  C CB    . LEU D 4 1043 ? 131.123 166.343 155.040 1.00 50.26  ? 1040 LEU A CB    1 
ATOM   9305  C CG    . LEU D 4 1043 ? 131.828 166.936 156.266 1.00 50.26  ? 1040 LEU A CG    1 
ATOM   9306  C CD1   . LEU D 4 1043 ? 131.868 165.924 157.396 1.00 50.26  ? 1040 LEU A CD1   1 
ATOM   9307  C CD2   . LEU D 4 1043 ? 133.219 167.439 155.959 1.00 50.26  ? 1040 LEU A CD2   1 
ATOM   9308  N N     . ASN D 4 1044 ? 130.176 164.679 152.462 1.00 50.26  ? 1041 ASN A N     1 
ATOM   9309  C CA    . ASN D 4 1044 ? 129.056 164.024 151.785 1.00 50.26  ? 1041 ASN A CA    1 
ATOM   9310  C C     . ASN D 4 1044 ? 129.480 163.607 150.383 1.00 50.26  ? 1041 ASN A C     1 
ATOM   9311  O O     . ASN D 4 1044 ? 129.095 164.234 149.389 1.00 50.26  ? 1041 ASN A O     1 
ATOM   9312  C CB    . ASN D 4 1044 ? 127.838 164.945 151.733 1.00 50.26  ? 1041 ASN A CB    1 
ATOM   9313  C CG    . ASN D 4 1044 ? 127.436 165.453 153.099 1.00 50.26  ? 1041 ASN A CG    1 
ATOM   9314  O OD1   . ASN D 4 1044 ? 127.420 164.701 154.072 1.00 50.26  ? 1041 ASN A OD1   1 
ATOM   9315  N ND2   . ASN D 4 1044 ? 127.109 166.737 153.180 1.00 50.26  ? 1041 ASN A ND2   1 
ATOM   9316  N N     . PRO D 4 1045 ? 130.275 162.548 150.267 1.00 50.26  ? 1042 PRO A N     1 
ATOM   9317  C CA    . PRO D 4 1045 ? 130.725 162.107 148.944 1.00 50.26  ? 1042 PRO A CA    1 
ATOM   9318  C C     . PRO D 4 1045 ? 129.591 161.492 148.141 1.00 50.26  ? 1042 PRO A C     1 
ATOM   9319  O O     . PRO D 4 1045 ? 128.603 160.991 148.682 1.00 50.26  ? 1042 PRO A O     1 
ATOM   9320  C CB    . PRO D 4 1045 ? 131.803 161.063 149.260 1.00 50.26  ? 1042 PRO A CB    1 
ATOM   9321  C CG    . PRO D 4 1045 ? 132.079 161.195 150.731 1.00 50.26  ? 1042 PRO A CG    1 
ATOM   9322  C CD    . PRO D 4 1045 ? 130.819 161.701 151.337 1.00 50.26  ? 1042 PRO A CD    1 
ATOM   9323  N N     . TYR D 4 1046 ? 129.746 161.544 146.821 1.00 50.26  ? 1043 TYR A N     1 
ATOM   9324  C CA    . TYR D 4 1046 ? 128.821 160.854 145.933 1.00 50.26  ? 1043 TYR A CA    1 
ATOM   9325  C C     . TYR D 4 1046 ? 128.963 159.345 146.063 1.00 50.26  ? 1043 TYR A C     1 
ATOM   9326  O O     . TYR D 4 1046 ? 130.071 158.812 146.166 1.00 50.26  ? 1043 TYR A O     1 
ATOM   9327  C CB    . TYR D 4 1046 ? 129.052 161.271 144.481 1.00 50.26  ? 1043 TYR A CB    1 
ATOM   9328  C CG    . TYR D 4 1046 ? 128.542 162.647 144.127 1.00 50.26  ? 1043 TYR A CG    1 
ATOM   9329  C CD1   . TYR D 4 1046 ? 127.621 163.298 144.933 1.00 50.26  ? 1043 TYR A CD1   1 
ATOM   9330  C CD2   . TYR D 4 1046 ? 128.975 163.291 142.981 1.00 50.26  ? 1043 TYR A CD2   1 
ATOM   9331  C CE1   . TYR D 4 1046 ? 127.147 164.551 144.604 1.00 50.26  ? 1043 TYR A CE1   1 
ATOM   9332  C CE2   . TYR D 4 1046 ? 128.509 164.544 142.646 1.00 50.26  ? 1043 TYR A CE2   1 
ATOM   9333  C CZ    . TYR D 4 1046 ? 127.597 165.170 143.460 1.00 50.26  ? 1043 TYR A CZ    1 
ATOM   9334  O OH    . TYR D 4 1046 ? 127.133 166.421 143.126 1.00 50.26  ? 1043 TYR A OH    1 
ATOM   9335  N N     . GLN D 4 1047 ? 127.826 158.657 146.054 1.00 50.26  ? 1044 GLN A N     1 
ATOM   9336  C CA    . GLN D 4 1047 ? 127.756 157.199 146.058 1.00 50.26  ? 1044 GLN A CA    1 
ATOM   9337  C C     . GLN D 4 1047 ? 126.994 156.813 144.795 1.00 50.26  ? 1044 GLN A C     1 
ATOM   9338  O O     . GLN D 4 1047 ? 125.762 156.753 144.798 1.00 50.26  ? 1044 GLN A O     1 
ATOM   9339  C CB    . GLN D 4 1047 ? 127.068 156.680 147.316 1.00 50.26  ? 1044 GLN A CB    1 
ATOM   9340  C CG    . GLN D 4 1047 ? 127.701 157.145 148.615 1.00 50.26  ? 1044 GLN A CG    1 
ATOM   9341  C CD    . GLN D 4 1047 ? 128.479 156.052 149.311 1.00 50.26  ? 1044 GLN A CD    1 
ATOM   9342  O OE1   . GLN D 4 1047 ? 128.162 154.872 149.181 1.00 50.26  ? 1044 GLN A OE1   1 
ATOM   9343  N NE2   . GLN D 4 1047 ? 129.501 156.439 150.061 1.00 50.26  ? 1044 GLN A NE2   1 
ATOM   9344  N N     . LEU D 4 1048 ? 127.725 156.556 143.711 1.00 50.26  ? 1045 LEU A N     1 
ATOM   9345  C CA    . LEU D 4 1048 ? 127.112 156.351 142.408 1.00 50.26  ? 1045 LEU A CA    1 
ATOM   9346  C C     . LEU D 4 1048 ? 127.210 154.923 141.891 1.00 50.26  ? 1045 LEU A C     1 
ATOM   9347  O O     . LEU D 4 1048 ? 126.579 154.611 140.876 1.00 50.26  ? 1045 LEU A O     1 
ATOM   9348  C CB    . LEU D 4 1048 ? 127.736 157.299 141.374 1.00 50.26  ? 1045 LEU A CB    1 
ATOM   9349  C CG    . LEU D 4 1048 ? 127.608 158.789 141.682 1.00 50.26  ? 1045 LEU A CG    1 
ATOM   9350  C CD1   . LEU D 4 1048 ? 128.514 159.605 140.780 1.00 50.26  ? 1045 LEU A CD1   1 
ATOM   9351  C CD2   . LEU D 4 1048 ? 126.166 159.235 141.547 1.00 50.26  ? 1045 LEU A CD2   1 
ATOM   9352  N N     . THR D 4 1049 ? 127.973 154.051 142.546 1.00 50.26  ? 1046 THR A N     1 
ATOM   9353  C CA    . THR D 4 1049 ? 128.112 152.675 142.096 1.00 50.26  ? 1046 THR A CA    1 
ATOM   9354  C C     . THR D 4 1049 ? 128.012 151.728 143.282 1.00 50.26  ? 1046 THR A C     1 
ATOM   9355  O O     . THR D 4 1049 ? 128.304 152.098 144.421 1.00 50.26  ? 1046 THR A O     1 
ATOM   9356  C CB    . THR D 4 1049 ? 129.441 152.439 141.368 1.00 50.26  ? 1046 THR A CB    1 
ATOM   9357  O OG1   . THR D 4 1049 ? 130.524 152.881 142.194 1.00 50.26  ? 1046 THR A OG1   1 
ATOM   9358  C CG2   . THR D 4 1049 ? 129.472 153.189 140.049 1.00 50.26  ? 1046 THR A CG2   1 
ATOM   9359  N N     . ASP D 4 1050 ? 127.590 150.501 142.998 1.00 50.26  ? 1047 ASP A N     1 
ATOM   9360  C CA    . ASP D 4 1050 ? 127.558 149.447 143.996 1.00 50.26  ? 1047 ASP A CA    1 
ATOM   9361  C C     . ASP D 4 1050 ? 128.973 148.942 144.263 1.00 50.26  ? 1047 ASP A C     1 
ATOM   9362  O O     . ASP D 4 1050 ? 129.879 149.090 143.439 1.00 50.26  ? 1047 ASP A O     1 
ATOM   9363  C CB    . ASP D 4 1050 ? 126.655 148.301 143.533 1.00 50.26  ? 1047 ASP A CB    1 
ATOM   9364  C CG    . ASP D 4 1050 ? 126.350 147.300 144.638 1.00 50.26  ? 1047 ASP A CG    1 
ATOM   9365  O OD1   . ASP D 4 1050 ? 127.064 147.286 145.662 1.00 50.26  ? 1047 ASP A OD1   1 
ATOM   9366  O OD2   . ASP D 4 1050 ? 125.386 146.521 144.479 1.00 50.26  ? 1047 ASP A OD2   1 
ATOM   9367  N N     . GLN D 4 1051 ? 129.156 148.347 145.439 1.00 50.26  ? 1048 GLN A N     1 
ATOM   9368  C CA    . GLN D 4 1051 ? 130.459 147.813 145.812 1.00 50.26  ? 1048 GLN A CA    1 
ATOM   9369  C C     . GLN D 4 1051 ? 130.887 146.725 144.837 1.00 50.26  ? 1048 GLN A C     1 
ATOM   9370  O O     . GLN D 4 1051 ? 130.101 145.841 144.487 1.00 50.26  ? 1048 GLN A O     1 
ATOM   9371  C CB    . GLN D 4 1051 ? 130.418 147.259 147.235 1.00 50.26  ? 1048 GLN A CB    1 
ATOM   9372  C CG    . GLN D 4 1051 ? 130.101 148.295 148.294 1.00 50.26  ? 1048 GLN A CG    1 
ATOM   9373  C CD    . GLN D 4 1051 ? 130.990 148.172 149.512 1.00 50.26  ? 1048 GLN A CD    1 
ATOM   9374  O OE1   . GLN D 4 1051 ? 132.192 147.937 149.396 1.00 50.26  ? 1048 GLN A OE1   1 
ATOM   9375  N NE2   . GLN D 4 1051 ? 130.403 148.331 150.692 1.00 50.26  ? 1048 GLN A NE2   1 
ATOM   9376  N N     . PHE D 4 1052 ? 132.138 146.797 144.395 1.00 50.26  ? 1049 PHE A N     1 
ATOM   9377  C CA    . PHE D 4 1052 ? 132.663 145.798 143.476 1.00 50.26  ? 1049 PHE A CA    1 
ATOM   9378  C C     . PHE D 4 1052 ? 132.786 144.449 144.172 1.00 50.26  ? 1049 PHE A C     1 
ATOM   9379  O O     . PHE D 4 1052 ? 133.226 144.362 145.321 1.00 50.26  ? 1049 PHE A O     1 
ATOM   9380  C CB    . PHE D 4 1052 ? 134.022 146.240 142.938 1.00 50.26  ? 1049 PHE A CB    1 
ATOM   9381  C CG    . PHE D 4 1052 ? 134.692 145.217 142.071 1.00 50.26  ? 1049 PHE A CG    1 
ATOM   9382  C CD1   . PHE D 4 1052 ? 134.300 145.042 140.757 1.00 50.26  ? 1049 PHE A CD1   1 
ATOM   9383  C CD2   . PHE D 4 1052 ? 135.716 144.432 142.570 1.00 50.26  ? 1049 PHE A CD2   1 
ATOM   9384  C CE1   . PHE D 4 1052 ? 134.915 144.103 139.959 1.00 50.26  ? 1049 PHE A CE1   1 
ATOM   9385  C CE2   . PHE D 4 1052 ? 136.332 143.490 141.776 1.00 50.26  ? 1049 PHE A CE2   1 
ATOM   9386  C CZ    . PHE D 4 1052 ? 135.933 143.328 140.468 1.00 50.26  ? 1049 PHE A CZ    1 
ATOM   9387  N N     . THR D 4 1053 ? 132.391 143.390 143.467 1.00 50.26  ? 1050 THR A N     1 
ATOM   9388  C CA    . THR D 4 1053 ? 132.458 142.035 143.998 1.00 50.26  ? 1050 THR A CA    1 
ATOM   9389  C C     . THR D 4 1053 ? 133.453 141.171 143.233 1.00 50.26  ? 1050 THR A C     1 
ATOM   9390  O O     . THR D 4 1053 ? 134.388 140.627 143.827 1.00 50.26  ? 1050 THR A O     1 
ATOM   9391  C CB    . THR D 4 1053 ? 131.066 141.390 143.973 1.00 50.26  ? 1050 THR A CB    1 
ATOM   9392  O OG1   . THR D 4 1053 ? 130.094 142.331 144.445 1.00 50.26  ? 1050 THR A OG1   1 
ATOM   9393  C CG2   . THR D 4 1053 ? 131.039 140.158 144.860 1.00 50.26  ? 1050 THR A CG2   1 
ATOM   9394  N N     . SER D 4 1054 ? 133.276 141.034 141.922 1.00 50.26  ? 1051 SER A N     1 
ATOM   9395  C CA    . SER D 4 1054 ? 134.190 140.254 141.101 1.00 50.26  ? 1051 SER A CA    1 
ATOM   9396  C C     . SER D 4 1054 ? 134.021 140.678 139.651 1.00 50.26  ? 1051 SER A C     1 
ATOM   9397  O O     . SER D 4 1054 ? 132.993 141.240 139.265 1.00 50.26  ? 1051 SER A O     1 
ATOM   9398  C CB    . SER D 4 1054 ? 133.947 138.750 141.257 1.00 50.26  ? 1051 SER A CB    1 
ATOM   9399  O OG    . SER D 4 1054 ? 134.847 138.005 140.457 1.00 50.26  ? 1051 SER A OG    1 
ATOM   9400  N N     . PHE D 4 1055 ? 135.053 140.401 138.850 1.00 50.26  ? 1052 PHE A N     1 
ATOM   9401  C CA    . PHE D 4 1055 ? 134.999 140.745 137.433 1.00 50.26  ? 1052 PHE A CA    1 
ATOM   9402  C C     . PHE D 4 1055 ? 133.898 139.970 136.720 1.00 50.26  ? 1052 PHE A C     1 
ATOM   9403  O O     . PHE D 4 1055 ? 133.180 140.527 135.881 1.00 50.26  ? 1052 PHE A O     1 
ATOM   9404  C CB    . PHE D 4 1055 ? 136.353 140.485 136.777 1.00 50.26  ? 1052 PHE A CB    1 
ATOM   9405  C CG    . PHE D 4 1055 ? 137.431 141.430 137.221 1.00 50.26  ? 1052 PHE A CG    1 
ATOM   9406  C CD1   . PHE D 4 1055 ? 137.244 142.799 137.144 1.00 50.26  ? 1052 PHE A CD1   1 
ATOM   9407  C CD2   . PHE D 4 1055 ? 138.632 140.949 137.715 1.00 50.26  ? 1052 PHE A CD2   1 
ATOM   9408  C CE1   . PHE D 4 1055 ? 138.234 143.671 137.551 1.00 50.26  ? 1052 PHE A CE1   1 
ATOM   9409  C CE2   . PHE D 4 1055 ? 139.626 141.817 138.123 1.00 50.26  ? 1052 PHE A CE2   1 
ATOM   9410  C CZ    . PHE D 4 1055 ? 139.427 143.179 138.041 1.00 50.26  ? 1052 PHE A CZ    1 
ATOM   9411  N N     . ALA D 4 1056 ? 133.754 138.682 137.035 1.00 50.26  ? 1053 ALA A N     1 
ATOM   9412  C CA    . ALA D 4 1056 ? 132.689 137.893 136.427 1.00 50.26  ? 1053 ALA A CA    1 
ATOM   9413  C C     . ALA D 4 1056 ? 131.335 138.195 137.055 1.00 50.26  ? 1053 ALA A C     1 
ATOM   9414  O O     . ALA D 4 1056 ? 130.306 138.112 136.375 1.00 50.26  ? 1053 ALA A O     1 
ATOM   9415  C CB    . ALA D 4 1056 ? 133.007 136.403 136.544 1.00 50.26  ? 1053 ALA A CB    1 
ATOM   9416  N N     . LYS D 4 1057 ? 131.313 138.547 138.343 1.00 50.26  ? 1054 LYS A N     1 
ATOM   9417  C CA    . LYS D 4 1057 ? 130.043 138.724 139.037 1.00 50.26  ? 1054 LYS A CA    1 
ATOM   9418  C C     . LYS D 4 1057 ? 129.331 140.004 138.619 1.00 50.26  ? 1054 LYS A C     1 
ATOM   9419  O O     . LYS D 4 1057 ? 128.097 140.060 138.657 1.00 50.26  ? 1054 LYS A O     1 
ATOM   9420  C CB    . LYS D 4 1057 ? 130.263 138.709 140.549 1.00 50.26  ? 1054 LYS A CB    1 
ATOM   9421  C CG    . LYS D 4 1057 ? 130.339 137.312 141.143 1.00 50.26  ? 1054 LYS A CG    1 
ATOM   9422  C CD    . LYS D 4 1057 ? 130.345 137.353 142.660 1.00 50.26  ? 1054 LYS A CD    1 
ATOM   9423  C CE    . LYS D 4 1057 ? 129.639 136.142 143.248 1.00 50.26  ? 1054 LYS A CE    1 
ATOM   9424  N NZ    . LYS D 4 1057 ? 129.860 134.918 142.431 1.00 50.26  ? 1054 LYS A NZ    1 
ATOM   9425  N N     . MET D 4 1058 ? 130.073 141.037 138.226 1.00 50.26  ? 1055 MET A N     1 
ATOM   9426  C CA    . MET D 4 1058 ? 129.437 142.283 137.821 1.00 50.26  ? 1055 MET A CA    1 
ATOM   9427  C C     . MET D 4 1058 ? 128.713 142.092 136.494 1.00 50.26  ? 1055 MET A C     1 
ATOM   9428  O O     . MET D 4 1058 ? 129.254 141.500 135.555 1.00 50.26  ? 1055 MET A O     1 
ATOM   9429  C CB    . MET D 4 1058 ? 130.465 143.412 137.719 1.00 50.26  ? 1055 MET A CB    1 
ATOM   9430  C CG    . MET D 4 1058 ? 131.570 143.196 136.700 1.00 50.26  ? 1055 MET A CG    1 
ATOM   9431  S SD    . MET D 4 1058 ? 132.467 144.720 136.346 1.00 50.26  ? 1055 MET A SD    1 
ATOM   9432  C CE    . MET D 4 1058 ? 134.108 144.087 136.015 1.00 50.26  ? 1055 MET A CE    1 
ATOM   9433  N N     . GLY D 4 1059 ? 127.483 142.578 136.424 1.00 50.26  ? 1056 GLY A N     1 
ATOM   9434  C CA    . GLY D 4 1059 ? 126.649 142.426 135.250 1.00 50.26  ? 1056 GLY A CA    1 
ATOM   9435  C C     . GLY D 4 1059 ? 126.828 143.553 134.259 1.00 50.26  ? 1056 GLY A C     1 
ATOM   9436  O O     . GLY D 4 1059 ? 127.875 144.204 134.200 1.00 50.26  ? 1056 GLY A O     1 
ATOM   9437  N N     . THR D 4 1060 ? 125.786 143.783 133.461 1.00 50.26  ? 1057 THR A N     1 
ATOM   9438  C CA    . THR D 4 1060 ? 125.813 144.862 132.483 1.00 50.26  ? 1057 THR A CA    1 
ATOM   9439  C C     . THR D 4 1060 ? 125.654 146.235 133.118 1.00 50.26  ? 1057 THR A C     1 
ATOM   9440  O O     . THR D 4 1060 ? 125.869 147.241 132.434 1.00 50.26  ? 1057 THR A O     1 
ATOM   9441  C CB    . THR D 4 1060 ? 124.719 144.649 131.436 1.00 50.26  ? 1057 THR A CB    1 
ATOM   9442  O OG1   . THR D 4 1060 ? 125.017 145.420 130.266 1.00 50.26  ? 1057 THR A OG1   1 
ATOM   9443  C CG2   . THR D 4 1060 ? 123.367 145.074 131.984 1.00 50.26  ? 1057 THR A CG2   1 
ATOM   9444  N N     . GLN D 4 1061 ? 125.286 146.306 134.395 1.00 50.26  ? 1058 GLN A N     1 
ATOM   9445  C CA    . GLN D 4 1061 ? 125.098 147.576 135.078 1.00 50.26  ? 1058 GLN A CA    1 
ATOM   9446  C C     . GLN D 4 1061 ? 125.752 147.520 136.448 1.00 50.26  ? 1058 GLN A C     1 
ATOM   9447  O O     . GLN D 4 1061 ? 125.656 146.510 137.150 1.00 50.26  ? 1058 GLN A O     1 
ATOM   9448  C CB    . GLN D 4 1061 ? 123.611 147.917 135.232 1.00 50.26  ? 1058 GLN A CB    1 
ATOM   9449  C CG    . GLN D 4 1061 ? 123.342 149.085 136.165 1.00 50.26  ? 1058 GLN A CG    1 
ATOM   9450  C CD    . GLN D 4 1061 ? 121.868 149.341 136.372 1.00 50.26  ? 1058 GLN A CD    1 
ATOM   9451  O OE1   . GLN D 4 1061 ? 121.075 148.408 136.479 1.00 50.26  ? 1058 GLN A OE1   1 
ATOM   9452  N NE2   . GLN D 4 1061 ? 121.490 150.611 136.425 1.00 50.26  ? 1058 GLN A NE2   1 
ATOM   9453  N N     . SER D 4 1062 ? 126.417 148.613 136.823 1.00 50.26  ? 1059 SER A N     1 
ATOM   9454  C CA    . SER D 4 1062 ? 126.968 148.787 138.169 1.00 50.26  ? 1059 SER A CA    1 
ATOM   9455  C C     . SER D 4 1062 ? 126.748 150.252 138.542 1.00 50.26  ? 1059 SER A C     1 
ATOM   9456  O O     . SER D 4 1062 ? 127.582 151.110 138.243 1.00 50.26  ? 1059 SER A O     1 
ATOM   9457  C CB    . SER D 4 1062 ? 128.438 148.398 138.227 1.00 50.26  ? 1059 SER A CB    1 
ATOM   9458  O OG    . SER D 4 1062 ? 129.038 148.862 139.422 1.00 50.26  ? 1059 SER A OG    1 
ATOM   9459  N N     . GLY D 4 1063 ? 125.631 150.526 139.203 1.00 50.26  ? 1060 GLY A N     1 
ATOM   9460  C CA    . GLY D 4 1063 ? 125.271 151.904 139.490 1.00 50.26  ? 1060 GLY A CA    1 
ATOM   9461  C C     . GLY D 4 1063 ? 125.047 152.664 138.198 1.00 50.26  ? 1060 GLY A C     1 
ATOM   9462  O O     . GLY D 4 1063 ? 124.276 152.243 137.329 1.00 50.26  ? 1060 GLY A O     1 
ATOM   9463  N N     . PHE D 4 1064 ? 125.725 153.800 138.055 1.00 50.26  ? 1061 PHE A N     1 
ATOM   9464  C CA    . PHE D 4 1064 ? 125.701 154.573 136.821 1.00 50.26  ? 1061 PHE A CA    1 
ATOM   9465  C C     . PHE D 4 1064 ? 126.737 154.106 135.809 1.00 50.26  ? 1061 PHE A C     1 
ATOM   9466  O O     . PHE D 4 1064 ? 127.081 154.867 134.901 1.00 50.26  ? 1061 PHE A O     1 
ATOM   9467  C CB    . PHE D 4 1064 ? 125.920 156.057 137.113 1.00 50.26  ? 1061 PHE A CB    1 
ATOM   9468  C CG    . PHE D 4 1064 ? 124.750 156.741 137.753 1.00 50.26  ? 1061 PHE A CG    1 
ATOM   9469  C CD1   . PHE D 4 1064 ? 123.502 156.159 137.754 1.00 50.26  ? 1061 PHE A CD1   1 
ATOM   9470  C CD2   . PHE D 4 1064 ? 124.901 157.980 138.343 1.00 50.26  ? 1061 PHE A CD2   1 
ATOM   9471  C CE1   . PHE D 4 1064 ? 122.427 156.797 138.340 1.00 50.26  ? 1061 PHE A CE1   1 
ATOM   9472  C CE2   . PHE D 4 1064 ? 123.829 158.618 138.929 1.00 50.26  ? 1061 PHE A CE2   1 
ATOM   9473  C CZ    . PHE D 4 1064 ? 122.593 158.026 138.927 1.00 50.26  ? 1061 PHE A CZ    1 
ATOM   9474  N N     . LEU D 4 1065 ? 127.256 152.893 135.950 1.00 50.26  ? 1062 LEU A N     1 
ATOM   9475  C CA    . LEU D 4 1065 ? 128.186 152.329 134.982 1.00 50.26  ? 1062 LEU A CA    1 
ATOM   9476  C C     . LEU D 4 1065 ? 127.479 151.232 134.201 1.00 50.26  ? 1062 LEU A C     1 
ATOM   9477  O O     . LEU D 4 1065 ? 127.032 150.238 134.783 1.00 50.26  ? 1062 LEU A O     1 
ATOM   9478  C CB    . LEU D 4 1065 ? 129.435 151.778 135.668 1.00 50.26  ? 1062 LEU A CB    1 
ATOM   9479  C CG    . LEU D 4 1065 ? 130.658 152.691 135.628 1.00 50.26  ? 1062 LEU A CG    1 
ATOM   9480  C CD1   . LEU D 4 1065 ? 130.439 153.893 136.515 1.00 50.26  ? 1062 LEU A CD1   1 
ATOM   9481  C CD2   . LEU D 4 1065 ? 131.905 151.933 136.043 1.00 50.26  ? 1062 LEU A CD2   1 
ATOM   9482  N N     . PHE D 4 1066 ? 127.380 151.413 132.891 1.00 50.26  ? 1063 PHE A N     1 
ATOM   9483  C CA    . PHE D 4 1066 ? 126.802 150.418 132.004 1.00 50.26  ? 1063 PHE A CA    1 
ATOM   9484  C C     . PHE D 4 1066 ? 127.906 149.763 131.189 1.00 50.26  ? 1063 PHE A C     1 
ATOM   9485  O O     . PHE D 4 1066 ? 128.944 150.372 130.915 1.00 50.26  ? 1063 PHE A O     1 
ATOM   9486  C CB    . PHE D 4 1066 ? 125.763 151.040 131.069 1.00 50.26  ? 1063 PHE A CB    1 
ATOM   9487  C CG    . PHE D 4 1066 ? 124.532 151.535 131.769 1.00 50.26  ? 1063 PHE A CG    1 
ATOM   9488  C CD1   . PHE D 4 1066 ? 124.251 151.145 133.065 1.00 50.26  ? 1063 PHE A CD1   1 
ATOM   9489  C CD2   . PHE D 4 1066 ? 123.654 152.387 131.127 1.00 50.26  ? 1063 PHE A CD2   1 
ATOM   9490  C CE1   . PHE D 4 1066 ? 123.120 151.600 133.708 1.00 50.26  ? 1063 PHE A CE1   1 
ATOM   9491  C CE2   . PHE D 4 1066 ? 122.521 152.842 131.765 1.00 50.26  ? 1063 PHE A CE2   1 
ATOM   9492  C CZ    . PHE D 4 1066 ? 122.254 152.448 133.057 1.00 50.26  ? 1063 PHE A CZ    1 
ATOM   9493  N N     . TYR D 4 1067 ? 127.678 148.511 130.809 1.00 50.26  ? 1064 TYR A N     1 
ATOM   9494  C CA    . TYR D 4 1067 ? 128.630 147.759 130.007 1.00 50.26  ? 1064 TYR A CA    1 
ATOM   9495  C C     . TYR D 4 1067 ? 127.910 147.180 128.802 1.00 50.26  ? 1064 TYR A C     1 
ATOM   9496  O O     . TYR D 4 1067 ? 126.890 146.500 128.950 1.00 50.26  ? 1064 TYR A O     1 
ATOM   9497  C CB    . TYR D 4 1067 ? 129.287 146.654 130.833 1.00 50.26  ? 1064 TYR A CB    1 
ATOM   9498  C CG    . TYR D 4 1067 ? 129.973 147.180 132.069 1.00 50.26  ? 1064 TYR A CG    1 
ATOM   9499  C CD1   . TYR D 4 1067 ? 131.222 147.777 131.989 1.00 50.26  ? 1064 TYR A CD1   1 
ATOM   9500  C CD2   . TYR D 4 1067 ? 129.367 147.095 133.313 1.00 50.26  ? 1064 TYR A CD2   1 
ATOM   9501  C CE1   . TYR D 4 1067 ? 131.850 148.267 133.113 1.00 50.26  ? 1064 TYR A CE1   1 
ATOM   9502  C CE2   . TYR D 4 1067 ? 129.989 147.582 134.443 1.00 50.26  ? 1064 TYR A CE2   1 
ATOM   9503  C CZ    . TYR D 4 1067 ? 131.231 148.167 134.337 1.00 50.26  ? 1064 TYR A CZ    1 
ATOM   9504  O OH    . TYR D 4 1067 ? 131.856 148.654 135.458 1.00 50.26  ? 1064 TYR A OH    1 
ATOM   9505  N N     . VAL D 4 1068 ? 128.442 147.450 127.616 1.00 50.26  ? 1065 VAL A N     1 
ATOM   9506  C CA    . VAL D 4 1068 ? 127.828 147.012 126.368 1.00 50.26  ? 1065 VAL A CA    1 
ATOM   9507  C C     . VAL D 4 1068 ? 128.853 146.186 125.602 1.00 50.26  ? 1065 VAL A C     1 
ATOM   9508  O O     . VAL D 4 1068 ? 130.062 146.385 125.788 1.00 50.26  ? 1065 VAL A O     1 
ATOM   9509  C CB    . VAL D 4 1068 ? 127.337 148.210 125.541 1.00 50.26  ? 1065 VAL A CB    1 
ATOM   9510  C CG1   . VAL D 4 1068 ? 126.194 148.909 126.254 1.00 50.26  ? 1065 VAL A CG1   1 
ATOM   9511  C CG2   . VAL D 4 1068 ? 128.480 149.177 125.285 1.00 50.26  ? 1065 VAL A CG2   1 
ATOM   9512  N N     . PRO D 4 1069 ? 128.429 145.251 124.753 1.00 50.26  ? 1066 PRO A N     1 
ATOM   9513  C CA    . PRO D 4 1069 ? 129.398 144.407 124.045 1.00 50.26  ? 1066 PRO A CA    1 
ATOM   9514  C C     . PRO D 4 1069 ? 130.368 145.232 123.213 1.00 50.26  ? 1066 PRO A C     1 
ATOM   9515  O O     . PRO D 4 1069 ? 129.985 146.186 122.534 1.00 50.26  ? 1066 PRO A O     1 
ATOM   9516  C CB    . PRO D 4 1069 ? 128.515 143.520 123.162 1.00 50.26  ? 1066 PRO A CB    1 
ATOM   9517  C CG    . PRO D 4 1069 ? 127.208 143.481 123.861 1.00 50.26  ? 1066 PRO A CG    1 
ATOM   9518  C CD    . PRO D 4 1069 ? 127.042 144.824 124.506 1.00 50.26  ? 1066 PRO A CD    1 
ATOM   9519  N N     . ALA D 4 1070 ? 131.641 144.849 123.282 1.00 50.26  ? 1067 ALA A N     1 
ATOM   9520  C CA    . ALA D 4 1070 ? 132.675 145.535 122.511 1.00 50.26  ? 1067 ALA A CA    1 
ATOM   9521  C C     . ALA D 4 1070 ? 132.486 145.436 121.000 1.00 50.26  ? 1067 ALA A C     1 
ATOM   9522  O O     . ALA D 4 1070 ? 132.547 146.482 120.331 1.00 50.26  ? 1067 ALA A O     1 
ATOM   9523  C CB    . ALA D 4 1070 ? 134.052 145.009 122.927 1.00 50.26  ? 1067 ALA A CB    1 
ATOM   9524  N N     . PRO D 4 1071 ? 132.264 144.265 120.398 1.00 50.26  ? 1068 PRO A N     1 
ATOM   9525  C CA    . PRO D 4 1071 ? 132.308 144.188 118.935 1.00 50.26  ? 1068 PRO A CA    1 
ATOM   9526  C C     . PRO D 4 1071 ? 131.116 144.879 118.294 1.00 50.26  ? 1068 PRO A C     1 
ATOM   9527  O O     . PRO D 4 1071 ? 130.073 145.093 118.915 1.00 50.26  ? 1068 PRO A O     1 
ATOM   9528  C CB    . PRO D 4 1071 ? 132.302 142.684 118.643 1.00 50.26  ? 1068 PRO A CB    1 
ATOM   9529  C CG    . PRO D 4 1071 ? 131.779 142.034 119.856 1.00 50.26  ? 1068 PRO A CG    1 
ATOM   9530  C CD    . PRO D 4 1071 ? 131.750 143.014 120.987 1.00 50.26  ? 1068 PRO A CD    1 
ATOM   9531  N N     . TYR D 4 1072 ? 131.299 145.231 117.021 1.00 50.26  ? 1069 TYR A N     1 
ATOM   9532  C CA    . TYR D 4 1072 ? 130.314 145.978 116.243 1.00 50.26  ? 1069 TYR A CA    1 
ATOM   9533  C C     . TYR D 4 1072 ? 130.012 147.325 116.901 1.00 50.26  ? 1069 TYR A C     1 
ATOM   9534  O O     . TYR D 4 1072 ? 128.880 147.627 117.284 1.00 50.26  ? 1069 TYR A O     1 
ATOM   9535  C CB    . TYR D 4 1072 ? 129.036 145.160 116.036 1.00 50.26  ? 1069 TYR A CB    1 
ATOM   9536  C CG    . TYR D 4 1072 ? 129.140 144.161 114.914 1.00 50.26  ? 1069 TYR A CG    1 
ATOM   9537  C CD1   . TYR D 4 1072 ? 129.086 144.572 113.592 1.00 50.26  ? 1069 TYR A CD1   1 
ATOM   9538  C CD2   . TYR D 4 1072 ? 129.306 142.810 115.174 1.00 50.26  ? 1069 TYR A CD2   1 
ATOM   9539  C CE1   . TYR D 4 1072 ? 129.184 143.666 112.562 1.00 50.26  ? 1069 TYR A CE1   1 
ATOM   9540  C CE2   . TYR D 4 1072 ? 129.407 141.896 114.150 1.00 50.26  ? 1069 TYR A CE2   1 
ATOM   9541  C CZ    . TYR D 4 1072 ? 129.344 142.330 112.846 1.00 50.26  ? 1069 TYR A CZ    1 
ATOM   9542  O OH    . TYR D 4 1072 ? 129.440 141.426 111.817 1.00 50.26  ? 1069 TYR A OH    1 
ATOM   9543  N N     . THR D 4 1073 ? 131.066 148.123 117.054 1.00 50.26  ? 1070 THR A N     1 
ATOM   9544  C CA    . THR D 4 1073 ? 130.915 149.498 117.505 1.00 50.26  ? 1070 THR A CA    1 
ATOM   9545  C C     . THR D 4 1073 ? 131.802 150.487 116.765 1.00 50.26  ? 1070 THR A C     1 
ATOM   9546  O O     . THR D 4 1073 ? 131.564 151.691 116.881 1.00 50.26  ? 1070 THR A O     1 
ATOM   9547  C CB    . THR D 4 1073 ? 131.199 149.606 119.010 1.00 50.26  ? 1070 THR A CB    1 
ATOM   9548  O OG1   . THR D 4 1073 ? 130.737 150.872 119.493 1.00 50.26  ? 1070 THR A OG1   1 
ATOM   9549  C CG2   . THR D 4 1073 ? 132.689 149.487 119.278 1.00 50.26  ? 1070 THR A CG2   1 
ATOM   9550  N N     . SER D 4 1074 ? 132.803 150.036 116.012 1.00 50.26  ? 1071 SER A N     1 
ATOM   9551  C CA    . SER D 4 1074 ? 133.733 150.923 115.326 1.00 50.26  ? 1071 SER A CA    1 
ATOM   9552  C C     . SER D 4 1074 ? 133.567 150.897 113.815 1.00 50.26  ? 1071 SER A C     1 
ATOM   9553  O O     . SER D 4 1074 ? 133.535 151.953 113.177 1.00 50.26  ? 1071 SER A O     1 
ATOM   9554  C CB    . SER D 4 1074 ? 135.176 150.556 115.697 1.00 50.26  ? 1071 SER A CB    1 
ATOM   9555  O OG    . SER D 4 1074 ? 136.097 151.461 115.117 1.00 50.26  ? 1071 SER A OG    1 
ATOM   9556  N N     . LYS D 4 1075 ? 133.463 149.710 113.220 1.00 50.26  ? 1072 LYS A N     1 
ATOM   9557  C CA    . LYS D 4 1075 ? 133.279 149.592 111.780 1.00 50.26  ? 1072 LYS A CA    1 
ATOM   9558  C C     . LYS D 4 1075 ? 131.805 149.700 111.416 1.00 50.26  ? 1072 LYS A C     1 
ATOM   9559  O O     . LYS D 4 1075 ? 131.259 148.815 110.750 1.00 50.26  ? 1072 LYS A O     1 
ATOM   9560  C CB    . LYS D 4 1075 ? 133.851 148.267 111.273 1.00 50.26  ? 1072 LYS A CB    1 
ATOM   9561  C CG    . LYS D 4 1075 ? 135.219 147.920 111.832 1.00 50.26  ? 1072 LYS A CG    1 
ATOM   9562  C CD    . LYS D 4 1075 ? 136.291 148.847 111.290 1.00 50.26  ? 1072 LYS A CD    1 
ATOM   9563  C CE    . LYS D 4 1075 ? 137.677 148.257 111.484 1.00 50.26  ? 1072 LYS A CE    1 
ATOM   9564  N NZ    . LYS D 4 1075 ? 137.999 148.064 112.924 1.00 50.26  ? 1072 LYS A NZ    1 
ATOM   9565  N N     . ILE D 4 1076 ? 131.152 150.776 111.846 1.00 50.26  ? 1073 ILE A N     1 
ATOM   9566  C CA    . ILE D 4 1076 ? 129.738 151.003 111.579 1.00 50.26  ? 1073 ILE A CA    1 
ATOM   9567  C C     . ILE D 4 1076 ? 129.573 152.396 110.996 1.00 50.26  ? 1073 ILE A C     1 
ATOM   9568  O O     . ILE D 4 1076 ? 130.192 153.355 111.470 1.00 50.26  ? 1073 ILE A O     1 
ATOM   9569  C CB    . ILE D 4 1076 ? 128.874 150.854 112.848 1.00 50.26  ? 1073 ILE A CB    1 
ATOM   9570  C CG1   . ILE D 4 1076 ? 128.949 149.435 113.392 1.00 50.26  ? 1073 ILE A CG1   1 
ATOM   9571  C CG2   . ILE D 4 1076 ? 127.427 151.203 112.563 1.00 50.26  ? 1073 ILE A CG2   1 
ATOM   9572  C CD1   . ILE D 4 1076 ? 128.339 149.308 114.749 1.00 50.26  ? 1073 ILE A CD1   1 
ATOM   9573  N N     . ASP D 4 1077 ? 128.750 152.505 109.968 1.00 50.26  ? 1074 ASP A N     1 
ATOM   9574  C CA    . ASP D 4 1077 ? 128.419 153.806 109.411 1.00 50.26  ? 1074 ASP A CA    1 
ATOM   9575  C C     . ASP D 4 1077 ? 127.539 154.560 110.397 1.00 50.26  ? 1074 ASP A C     1 
ATOM   9576  O O     . ASP D 4 1077 ? 126.424 154.107 110.687 1.00 50.26  ? 1074 ASP A O     1 
ATOM   9577  C CB    . ASP D 4 1077 ? 127.700 153.632 108.080 1.00 50.26  ? 1074 ASP A CB    1 
ATOM   9578  C CG    . ASP D 4 1077 ? 127.500 154.938 107.351 1.00 50.26  ? 1074 ASP A CG    1 
ATOM   9579  O OD1   . ASP D 4 1077 ? 128.077 155.957 107.778 1.00 50.26  ? 1074 ASP A OD1   1 
ATOM   9580  O OD2   . ASP D 4 1077 ? 126.759 154.946 106.347 1.00 50.26  ? 1074 ASP A OD2   1 
ATOM   9581  N N     . PRO D 4 1078 ? 127.982 155.699 110.935 1.00 50.26  ? 1075 PRO A N     1 
ATOM   9582  C CA    . PRO D 4 1078 ? 127.122 156.444 111.864 1.00 50.26  ? 1075 PRO A CA    1 
ATOM   9583  C C     . PRO D 4 1078 ? 125.892 157.035 111.206 1.00 50.26  ? 1075 PRO A C     1 
ATOM   9584  O O     . PRO D 4 1078 ? 124.936 157.372 111.913 1.00 50.26  ? 1075 PRO A O     1 
ATOM   9585  C CB    . PRO D 4 1078 ? 128.051 157.539 112.403 1.00 50.26  ? 1075 PRO A CB    1 
ATOM   9586  C CG    . PRO D 4 1078 ? 129.070 157.715 111.347 1.00 50.26  ? 1075 PRO A CG    1 
ATOM   9587  C CD    . PRO D 4 1078 ? 129.274 156.369 110.716 1.00 50.26  ? 1075 PRO A CD    1 
ATOM   9588  N N     . LEU D 4 1079 ? 125.885 157.174 109.880 1.00 50.26  ? 1076 LEU A N     1 
ATOM   9589  C CA    . LEU D 4 1079 ? 124.725 157.730 109.196 1.00 50.26  ? 1076 LEU A CA    1 
ATOM   9590  C C     . LEU D 4 1079 ? 123.678 156.671 108.880 1.00 50.26  ? 1076 LEU A C     1 
ATOM   9591  O O     . LEU D 4 1079 ? 122.483 156.983 108.842 1.00 50.26  ? 1076 LEU A O     1 
ATOM   9592  C CB    . LEU D 4 1079 ? 125.159 158.427 107.906 1.00 50.26  ? 1076 LEU A CB    1 
ATOM   9593  C CG    . LEU D 4 1079 ? 125.719 159.841 108.050 1.00 50.26  ? 1076 LEU A CG    1 
ATOM   9594  C CD1   . LEU D 4 1079 ? 125.839 160.510 106.693 1.00 50.26  ? 1076 LEU A CD1   1 
ATOM   9595  C CD2   . LEU D 4 1079 ? 124.839 160.658 108.966 1.00 50.26  ? 1076 LEU A CD2   1 
ATOM   9596  N N     . THR D 4 1080 ? 124.096 155.428 108.648 1.00 50.26  ? 1077 THR A N     1 
ATOM   9597  C CA    . THR D 4 1080 ? 123.181 154.374 108.228 1.00 50.26  ? 1077 THR A CA    1 
ATOM   9598  C C     . THR D 4 1080 ? 123.213 153.123 109.092 1.00 50.26  ? 1077 THR A C     1 
ATOM   9599  O O     . THR D 4 1080 ? 122.248 152.352 109.048 1.00 50.26  ? 1077 THR A O     1 
ATOM   9600  C CB    . THR D 4 1080 ? 123.470 153.955 106.778 1.00 50.26  ? 1077 THR A CB    1 
ATOM   9601  O OG1   . THR D 4 1080 ? 124.767 153.352 106.705 1.00 50.26  ? 1077 THR A OG1   1 
ATOM   9602  C CG2   . THR D 4 1080 ? 123.428 155.156 105.855 1.00 50.26  ? 1077 THR A CG2   1 
ATOM   9603  N N     . GLY D 4 1081 ? 124.268 152.890 109.866 1.00 50.26  ? 1078 GLY A N     1 
ATOM   9604  C CA    . GLY D 4 1081 ? 124.398 151.639 110.582 1.00 50.26  ? 1078 GLY A CA    1 
ATOM   9605  C C     . GLY D 4 1081 ? 124.875 150.483 109.737 1.00 50.26  ? 1078 GLY A C     1 
ATOM   9606  O O     . GLY D 4 1081 ? 124.852 149.340 110.207 1.00 50.26  ? 1078 GLY A O     1 
ATOM   9607  N N     . PHE D 4 1082 ? 125.301 150.743 108.505 1.00 50.26  ? 1079 PHE A N     1 
ATOM   9608  C CA    . PHE D 4 1082 ? 125.754 149.686 107.615 1.00 50.26  ? 1079 PHE A CA    1 
ATOM   9609  C C     . PHE D 4 1082 ? 127.062 149.084 108.111 1.00 50.26  ? 1079 PHE A C     1 
ATOM   9610  O O     . PHE D 4 1082 ? 127.944 149.791 108.604 1.00 50.26  ? 1079 PHE A O     1 
ATOM   9611  C CB    . PHE D 4 1082 ? 125.933 150.239 106.202 1.00 50.26  ? 1079 PHE A CB    1 
ATOM   9612  C CG    . PHE D 4 1082 ? 126.522 149.258 105.234 1.00 50.26  ? 1079 PHE A CG    1 
ATOM   9613  C CD1   . PHE D 4 1082 ? 125.916 148.036 105.011 1.00 50.26  ? 1079 PHE A CD1   1 
ATOM   9614  C CD2   . PHE D 4 1082 ? 127.680 149.562 104.543 1.00 50.26  ? 1079 PHE A CD2   1 
ATOM   9615  C CE1   . PHE D 4 1082 ? 126.454 147.136 104.117 1.00 50.26  ? 1079 PHE A CE1   1 
ATOM   9616  C CE2   . PHE D 4 1082 ? 128.223 148.665 103.650 1.00 50.26  ? 1079 PHE A CE2   1 
ATOM   9617  C CZ    . PHE D 4 1082 ? 127.610 147.450 103.437 1.00 50.26  ? 1079 PHE A CZ    1 
ATOM   9618  N N     . VAL D 4 1083 ? 127.182 147.766 107.979 1.00 50.26  ? 1080 VAL A N     1 
ATOM   9619  C CA    . VAL D 4 1083 ? 128.396 147.047 108.338 1.00 50.26  ? 1080 VAL A CA    1 
ATOM   9620  C C     . VAL D 4 1083 ? 128.780 146.141 107.180 1.00 50.26  ? 1080 VAL A C     1 
ATOM   9621  O O     . VAL D 4 1083 ? 127.926 145.696 106.408 1.00 50.26  ? 1080 VAL A O     1 
ATOM   9622  C CB    . VAL D 4 1083 ? 128.225 146.220 109.628 1.00 50.26  ? 1080 VAL A CB    1 
ATOM   9623  C CG1   . VAL D 4 1083 ? 128.150 147.131 110.831 1.00 50.26  ? 1080 VAL A CG1   1 
ATOM   9624  C CG2   . VAL D 4 1083 ? 126.986 145.348 109.536 1.00 50.26  ? 1080 VAL A CG2   1 
ATOM   9625  N N     . ASP D 4 1084 ? 130.077 145.870 107.064 1.00 50.26  ? 1081 ASP A N     1 
ATOM   9626  C CA    . ASP D 4 1084 ? 130.578 144.949 106.053 1.00 50.26  ? 1081 ASP A CA    1 
ATOM   9627  C C     . ASP D 4 1084 ? 130.056 143.552 106.366 1.00 50.26  ? 1081 ASP A C     1 
ATOM   9628  O O     . ASP D 4 1084 ? 130.459 142.949 107.369 1.00 50.26  ? 1081 ASP A O     1 
ATOM   9629  C CB    . ASP D 4 1084 ? 132.108 144.967 106.020 1.00 50.26  ? 1081 ASP A CB    1 
ATOM   9630  C CG    . ASP D 4 1084 ? 132.679 144.257 104.807 1.00 50.26  ? 1081 ASP A CG    1 
ATOM   9631  O OD1   . ASP D 4 1084 ? 131.993 143.387 104.233 1.00 50.26  ? 1081 ASP A OD1   1 
ATOM   9632  O OD2   . ASP D 4 1084 ? 133.827 144.570 104.427 1.00 50.26  ? 1081 ASP A OD2   1 
ATOM   9633  N N     . PRO D 4 1085 ? 129.162 143.003 105.538 1.00 50.26  ? 1082 PRO A N     1 
ATOM   9634  C CA    . PRO D 4 1085 ? 128.569 141.701 105.869 1.00 50.26  ? 1082 PRO A CA    1 
ATOM   9635  C C     . PRO D 4 1085 ? 129.403 140.514 105.427 1.00 50.26  ? 1082 PRO A C     1 
ATOM   9636  O O     . PRO D 4 1085 ? 129.254 139.430 106.005 1.00 50.26  ? 1082 PRO A O     1 
ATOM   9637  C CB    . PRO D 4 1085 ? 127.229 141.736 105.126 1.00 50.26  ? 1082 PRO A CB    1 
ATOM   9638  C CG    . PRO D 4 1085 ? 127.510 142.586 103.921 1.00 50.26  ? 1082 PRO A CG    1 
ATOM   9639  C CD    . PRO D 4 1085 ? 128.629 143.546 104.276 1.00 50.26  ? 1082 PRO A CD    1 
ATOM   9640  N N     . PHE D 4 1086 ? 130.276 140.681 104.440 1.00 50.26  ? 1083 PHE A N     1 
ATOM   9641  C CA    . PHE D 4 1086 ? 131.008 139.567 103.860 1.00 50.26  ? 1083 PHE A CA    1 
ATOM   9642  C C     . PHE D 4 1086 ? 132.233 139.223 104.694 1.00 50.26  ? 1083 PHE A C     1 
ATOM   9643  O O     . PHE D 4 1086 ? 132.965 140.108 105.143 1.00 50.26  ? 1083 PHE A O     1 
ATOM   9644  C CB    . PHE D 4 1086 ? 131.433 139.896 102.430 1.00 50.26  ? 1083 PHE A CB    1 
ATOM   9645  C CG    . PHE D 4 1086 ? 130.322 140.431 101.581 1.00 50.26  ? 1083 PHE A CG    1 
ATOM   9646  C CD1   . PHE D 4 1086 ? 129.281 139.612 101.187 1.00 50.26  ? 1083 PHE A CD1   1 
ATOM   9647  C CD2   . PHE D 4 1086 ? 130.314 141.754 101.182 1.00 50.26  ? 1083 PHE A CD2   1 
ATOM   9648  C CE1   . PHE D 4 1086 ? 128.256 140.102 100.407 1.00 50.26  ? 1083 PHE A CE1   1 
ATOM   9649  C CE2   . PHE D 4 1086 ? 129.292 142.249 100.403 1.00 50.26  ? 1083 PHE A CE2   1 
ATOM   9650  C CZ    . PHE D 4 1086 ? 128.262 141.422 100.016 1.00 50.26  ? 1083 PHE A CZ    1 
ATOM   9651  N N     . VAL D 4 1087 ? 132.449 137.925 104.896 1.00 50.26  ? 1084 VAL A N     1 
ATOM   9652  C CA    . VAL D 4 1087 ? 133.663 137.423 105.528 1.00 50.26  ? 1084 VAL A CA    1 
ATOM   9653  C C     . VAL D 4 1087 ? 134.643 137.119 104.400 1.00 50.26  ? 1084 VAL A C     1 
ATOM   9654  O O     . VAL D 4 1087 ? 134.565 136.073 103.754 1.00 50.26  ? 1084 VAL A O     1 
ATOM   9655  C CB    . VAL D 4 1087 ? 133.389 136.194 106.395 1.00 50.26  ? 1084 VAL A CB    1 
ATOM   9656  C CG1   . VAL D 4 1087 ? 134.651 135.774 107.127 1.00 50.26  ? 1084 VAL A CG1   1 
ATOM   9657  C CG2   . VAL D 4 1087 ? 132.267 136.483 107.378 1.00 50.26  ? 1084 VAL A CG2   1 
ATOM   9658  N N     . TRP D 4 1088 ? 135.574 138.044 104.163 1.00 50.26  ? 1085 TRP A N     1 
ATOM   9659  C CA    . TRP D 4 1088 ? 136.455 137.943 103.006 1.00 50.26  ? 1085 TRP A CA    1 
ATOM   9660  C C     . TRP D 4 1088 ? 137.422 136.771 103.102 1.00 50.26  ? 1085 TRP A C     1 
ATOM   9661  O O     . TRP D 4 1088 ? 138.001 136.380 102.083 1.00 50.26  ? 1085 TRP A O     1 
ATOM   9662  C CB    . TRP D 4 1088 ? 137.221 139.252 102.828 1.00 50.26  ? 1085 TRP A CB    1 
ATOM   9663  C CG    . TRP D 4 1088 ? 136.309 140.425 102.676 1.00 50.26  ? 1085 TRP A CG    1 
ATOM   9664  C CD1   . TRP D 4 1088 ? 135.993 141.345 103.630 1.00 50.26  ? 1085 TRP A CD1   1 
ATOM   9665  C CD2   . TRP D 4 1088 ? 135.573 140.791 101.505 1.00 50.26  ? 1085 TRP A CD2   1 
ATOM   9666  N NE1   . TRP D 4 1088 ? 135.113 142.268 103.123 1.00 50.26  ? 1085 TRP A NE1   1 
ATOM   9667  C CE2   . TRP D 4 1088 ? 134.839 141.950 101.819 1.00 50.26  ? 1085 TRP A CE2   1 
ATOM   9668  C CE3   . TRP D 4 1088 ? 135.467 140.254 100.220 1.00 50.26  ? 1085 TRP A CE3   1 
ATOM   9669  C CZ2   . TRP D 4 1088 ? 134.010 142.580 100.897 1.00 50.26  ? 1085 TRP A CZ2   1 
ATOM   9670  C CZ3   . TRP D 4 1088 ? 134.646 140.882 99.305  1.00 50.26  ? 1085 TRP A CZ3   1 
ATOM   9671  C CH2   . TRP D 4 1088 ? 133.928 142.033 99.647  1.00 50.26  ? 1085 TRP A CH2   1 
ATOM   9672  N N     . LYS D 4 1089 ? 137.612 136.203 104.293 1.00 57.08  ? 1086 LYS A N     1 
ATOM   9673  C CA    . LYS D 4 1089 ? 138.450 135.019 104.425 1.00 57.08  ? 1086 LYS A CA    1 
ATOM   9674  C C     . LYS D 4 1089 ? 137.798 133.772 103.844 1.00 57.08  ? 1086 LYS A C     1 
ATOM   9675  O O     . LYS D 4 1089 ? 138.492 132.770 103.642 1.00 57.08  ? 1086 LYS A O     1 
ATOM   9676  C CB    . LYS D 4 1089 ? 138.799 134.784 105.896 1.00 57.08  ? 1086 LYS A CB    1 
ATOM   9677  C CG    . LYS D 4 1089 ? 139.698 135.854 106.496 1.00 57.08  ? 1086 LYS A CG    1 
ATOM   9678  C CD    . LYS D 4 1089 ? 139.989 135.578 107.963 1.00 57.08  ? 1086 LYS A CD    1 
ATOM   9679  C CE    . LYS D 4 1089 ? 140.907 136.636 108.554 1.00 57.08  ? 1086 LYS A CE    1 
ATOM   9680  N NZ    . LYS D 4 1089 ? 141.183 136.394 109.997 1.00 57.08  ? 1086 LYS A NZ    1 
ATOM   9681  N N     . THR D 4 1090 ? 136.491 133.806 103.579 1.00 53.66  ? 1087 THR A N     1 
ATOM   9682  C CA    . THR D 4 1090 ? 135.821 132.639 103.015 1.00 53.66  ? 1087 THR A CA    1 
ATOM   9683  C C     . THR D 4 1090 ? 136.157 132.462 101.540 1.00 53.66  ? 1087 THR A C     1 
ATOM   9684  O O     . THR D 4 1090 ? 136.378 131.335 101.080 1.00 53.66  ? 1087 THR A O     1 
ATOM   9685  C CB    . THR D 4 1090 ? 134.310 132.755 103.203 1.00 53.66  ? 1087 THR A CB    1 
ATOM   9686  O OG1   . THR D 4 1090 ? 133.825 133.890 102.476 1.00 53.66  ? 1087 THR A OG1   1 
ATOM   9687  C CG2   . THR D 4 1090 ? 133.969 132.918 104.675 1.00 53.66  ? 1087 THR A CG2   1 
ATOM   9688  N N     . ILE D 4 1091 ? 136.199 133.555 100.784 1.00 55.42  ? 1088 ILE A N     1 
ATOM   9689  C CA    . ILE D 4 1091 ? 136.455 133.482 99.349  1.00 55.42  ? 1088 ILE A CA    1 
ATOM   9690  C C     . ILE D 4 1091 ? 137.951 133.299 99.117  1.00 55.42  ? 1088 ILE A C     1 
ATOM   9691  O O     . ILE D 4 1091 ? 138.766 134.126 99.539  1.00 55.42  ? 1088 ILE A O     1 
ATOM   9692  C CB    . ILE D 4 1091 ? 135.923 134.728 98.627  1.00 55.42  ? 1088 ILE A CB    1 
ATOM   9693  C CG1   . ILE D 4 1091 ? 136.419 136.005 99.305  1.00 55.42  ? 1088 ILE A CG1   1 
ATOM   9694  C CG2   . ILE D 4 1091 ? 134.407 134.714 98.593  1.00 55.42  ? 1088 ILE A CG2   1 
ATOM   9695  C CD1   . ILE D 4 1091 ? 136.201 137.245 98.487  1.00 55.42  ? 1088 ILE A CD1   1 
ATOM   9696  N N     . LYS D 4 1092 ? 138.315 132.204 98.468  1.00 59.55  ? 1089 LYS A N     1 
ATOM   9697  C CA    . LYS D 4 1092 ? 139.716 131.904 98.199  1.00 59.55  ? 1089 LYS A CA    1 
ATOM   9698  C C     . LYS D 4 1092 ? 139.990 131.570 96.741  1.00 59.55  ? 1089 LYS A C     1 
ATOM   9699  O O     . LYS D 4 1092 ? 141.046 131.938 96.222  1.00 59.55  ? 1089 LYS A O     1 
ATOM   9700  C CB    . LYS D 4 1092 ? 140.185 130.742 99.092  1.00 59.55  ? 1089 LYS A CB    1 
ATOM   9701  C CG    . LYS D 4 1092 ? 139.988 130.977 100.580 1.00 59.55  ? 1089 LYS A CG    1 
ATOM   9702  C CD    . LYS D 4 1092 ? 139.845 129.664 101.332 1.00 59.55  ? 1089 LYS A CD    1 
ATOM   9703  C CE    . LYS D 4 1092 ? 138.669 128.853 100.810 1.00 59.55  ? 1089 LYS A CE    1 
ATOM   9704  N NZ    . LYS D 4 1092 ? 137.398 129.200 101.504 1.00 59.55  ? 1089 LYS A NZ    1 
ATOM   9705  N N     . ASN D 4 1093 ? 139.071 130.886 96.069  1.00 60.56  ? 1090 ASN A N     1 
ATOM   9706  C CA    . ASN D 4 1093 ? 139.285 130.401 94.714  1.00 60.56  ? 1090 ASN A CA    1 
ATOM   9707  C C     . ASN D 4 1093 ? 138.517 131.250 93.709  1.00 60.56  ? 1090 ASN A C     1 
ATOM   9708  O O     . ASN D 4 1093 ? 137.700 132.102 94.066  1.00 60.56  ? 1090 ASN A O     1 
ATOM   9709  C CB    . ASN D 4 1093 ? 138.880 128.926 94.597  1.00 60.56  ? 1090 ASN A CB    1 
ATOM   9710  C CG    . ASN D 4 1093 ? 137.418 128.690 94.928  1.00 60.56  ? 1090 ASN A CG    1 
ATOM   9711  O OD1   . ASN D 4 1093 ? 136.524 129.140 94.211  1.00 60.56  ? 1090 ASN A OD1   1 
ATOM   9712  N ND2   . ASN D 4 1093 ? 137.168 127.978 96.020  1.00 60.56  ? 1090 ASN A ND2   1 
ATOM   9713  N N     . HIS D 4 1094 ? 138.802 130.998 92.429  1.00 60.39  ? 1091 HIS A N     1 
ATOM   9714  C CA    . HIS D 4 1094 ? 138.172 131.761 91.356  1.00 60.39  ? 1091 HIS A CA    1 
ATOM   9715  C C     . HIS D 4 1094 ? 136.672 131.501 91.292  1.00 60.39  ? 1091 HIS A C     1 
ATOM   9716  O O     . HIS D 4 1094 ? 135.888 132.424 91.041  1.00 60.39  ? 1091 HIS A O     1 
ATOM   9717  C CB    . HIS D 4 1094 ? 138.833 131.423 90.022  1.00 60.39  ? 1091 HIS A CB    1 
ATOM   9718  C CG    . HIS D 4 1094 ? 138.608 132.451 88.959  1.00 60.39  ? 1091 HIS A CG    1 
ATOM   9719  N ND1   . HIS D 4 1094 ? 138.774 132.182 87.617  1.00 60.39  ? 1091 HIS A ND1   1 
ATOM   9720  C CD2   . HIS D 4 1094 ? 138.235 133.750 89.039  1.00 60.39  ? 1091 HIS A CD2   1 
ATOM   9721  C CE1   . HIS D 4 1094 ? 138.511 133.270 86.917  1.00 60.39  ? 1091 HIS A CE1   1 
ATOM   9722  N NE2   . HIS D 4 1094 ? 138.182 134.236 87.755  1.00 60.39  ? 1091 HIS A NE2   1 
ATOM   9723  N N     . GLU D 4 1095 ? 136.254 130.250 91.499  1.00 62.19  ? 1092 GLU A N     1 
ATOM   9724  C CA    . GLU D 4 1095 ? 134.828 129.937 91.479  1.00 62.19  ? 1092 GLU A CA    1 
ATOM   9725  C C     . GLU D 4 1095 ? 134.097 130.625 92.625  1.00 62.19  ? 1092 GLU A C     1 
ATOM   9726  O O     . GLU D 4 1095 ? 132.955 131.074 92.461  1.00 62.19  ? 1092 GLU A O     1 
ATOM   9727  C CB    . GLU D 4 1095 ? 134.622 128.424 91.536  1.00 62.19  ? 1092 GLU A CB    1 
ATOM   9728  C CG    . GLU D 4 1095 ? 134.789 127.728 90.194  1.00 62.19  ? 1092 GLU A CG    1 
ATOM   9729  C CD    . GLU D 4 1095 ? 133.756 128.166 89.172  1.00 62.19  ? 1092 GLU A CD    1 
ATOM   9730  O OE1   . GLU D 4 1095 ? 132.637 128.545 89.577  1.00 62.19  ? 1092 GLU A OE1   1 
ATOM   9731  O OE2   . GLU D 4 1095 ? 134.064 128.134 87.962  1.00 62.19  ? 1092 GLU A OE2   1 
ATOM   9732  N N     . SER D 4 1096 ? 134.734 130.708 93.795  1.00 59.89  ? 1093 SER A N     1 
ATOM   9733  C CA    . SER D 4 1096 ? 134.148 131.458 94.900  1.00 59.89  ? 1093 SER A CA    1 
ATOM   9734  C C     . SER D 4 1096 ? 133.984 132.927 94.535  1.00 59.89  ? 1093 SER A C     1 
ATOM   9735  O O     . SER D 4 1096 ? 132.965 133.544 94.861  1.00 59.89  ? 1093 SER A O     1 
ATOM   9736  C CB    . SER D 4 1096 ? 135.008 131.305 96.154  1.00 59.89  ? 1093 SER A CB    1 
ATOM   9737  O OG    . SER D 4 1096 ? 136.244 131.983 96.009  1.00 59.89  ? 1093 SER A OG    1 
ATOM   9738  N N     . ARG D 4 1097 ? 134.978 133.503 93.854  1.00 55.69  ? 1094 ARG A N     1 
ATOM   9739  C CA    . ARG D 4 1097 ? 134.858 134.884 93.400  1.00 55.69  ? 1094 ARG A CA    1 
ATOM   9740  C C     . ARG D 4 1097 ? 133.707 135.041 92.416  1.00 55.69  ? 1094 ARG A C     1 
ATOM   9741  O O     . ARG D 4 1097 ? 132.963 136.027 92.472  1.00 55.69  ? 1094 ARG A O     1 
ATOM   9742  C CB    . ARG D 4 1097 ? 136.165 135.350 92.761  1.00 55.69  ? 1094 ARG A CB    1 
ATOM   9743  C CG    . ARG D 4 1097 ? 137.333 135.476 93.720  1.00 55.69  ? 1094 ARG A CG    1 
ATOM   9744  C CD    . ARG D 4 1097 ? 138.488 136.214 93.063  1.00 55.69  ? 1094 ARG A CD    1 
ATOM   9745  N NE    . ARG D 4 1097 ? 139.744 136.014 93.773  1.00 55.69  ? 1094 ARG A NE    1 
ATOM   9746  C CZ    . ARG D 4 1097 ? 140.567 134.996 93.563  1.00 55.69  ? 1094 ARG A CZ    1 
ATOM   9747  N NH1   . ARG D 4 1097 ? 140.298 134.064 92.665  1.00 55.69  ? 1094 ARG A NH1   1 
ATOM   9748  N NH2   . ARG D 4 1097 ? 141.690 134.913 94.271  1.00 55.69  ? 1094 ARG A NH2   1 
ATOM   9749  N N     . LYS D 4 1098 ? 133.549 134.082 91.501  1.00 57.39  ? 1095 LYS A N     1 
ATOM   9750  C CA    . LYS D 4 1098 ? 132.452 134.146 90.540  1.00 57.39  ? 1095 LYS A CA    1 
ATOM   9751  C C     . LYS D 4 1098 ? 131.104 134.107 91.248  1.00 57.39  ? 1095 LYS A C     1 
ATOM   9752  O O     . LYS D 4 1098 ? 130.203 134.897 90.943  1.00 57.39  ? 1095 LYS A O     1 
ATOM   9753  C CB    . LYS D 4 1098 ? 132.558 132.992 89.544  1.00 57.39  ? 1095 LYS A CB    1 
ATOM   9754  C CG    . LYS D 4 1098 ? 133.594 133.183 88.457  1.00 57.39  ? 1095 LYS A CG    1 
ATOM   9755  C CD    . LYS D 4 1098 ? 133.255 132.330 87.247  1.00 57.39  ? 1095 LYS A CD    1 
ATOM   9756  C CE    . LYS D 4 1098 ? 134.327 132.430 86.183  1.00 57.39  ? 1095 LYS A CE    1 
ATOM   9757  N NZ    . LYS D 4 1098 ? 135.671 132.141 86.746  1.00 57.39  ? 1095 LYS A NZ    1 
ATOM   9758  N N     . HIS D 4 1099 ? 130.952 133.187 92.202  1.00 58.70  ? 1096 HIS A N     1 
ATOM   9759  C CA    . HIS D 4 1099 ? 129.690 133.077 92.927  1.00 58.70  ? 1096 HIS A CA    1 
ATOM   9760  C C     . HIS D 4 1099 ? 129.416 134.328 93.751  1.00 58.70  ? 1096 HIS A C     1 
ATOM   9761  O O     . HIS D 4 1099 ? 128.269 134.782 93.841  1.00 58.70  ? 1096 HIS A O     1 
ATOM   9762  C CB    . HIS D 4 1099 ? 129.702 131.833 93.815  1.00 58.70  ? 1096 HIS A CB    1 
ATOM   9763  C CG    . HIS D 4 1099 ? 129.747 130.548 93.049  1.00 58.70  ? 1096 HIS A CG    1 
ATOM   9764  N ND1   . HIS D 4 1099 ? 130.929 129.952 92.665  1.00 58.70  ? 1096 HIS A ND1   1 
ATOM   9765  C CD2   . HIS D 4 1099 ? 128.756 129.749 92.589  1.00 58.70  ? 1096 HIS A CD2   1 
ATOM   9766  C CE1   . HIS D 4 1099 ? 130.665 128.839 92.005  1.00 58.70  ? 1096 HIS A CE1   1 
ATOM   9767  N NE2   . HIS D 4 1099 ? 129.353 128.692 91.945  1.00 58.70  ? 1096 HIS A NE2   1 
ATOM   9768  N N     . PHE D 4 1100 ? 130.455 134.896 94.368  1.00 50.26  ? 1097 PHE A N     1 
ATOM   9769  C CA    . PHE D 4 1100 ? 130.278 136.120 95.141  1.00 50.26  ? 1097 PHE A CA    1 
ATOM   9770  C C     . PHE D 4 1100 ? 129.871 137.284 94.249  1.00 50.26  ? 1097 PHE A C     1 
ATOM   9771  O O     . PHE D 4 1100 ? 128.990 138.073 94.608  1.00 50.26  ? 1097 PHE A O     1 
ATOM   9772  C CB    . PHE D 4 1100 ? 131.563 136.446 95.902  1.00 50.26  ? 1097 PHE A CB    1 
ATOM   9773  C CG    . PHE D 4 1100 ? 131.652 137.871 96.364  1.00 50.26  ? 1097 PHE A CG    1 
ATOM   9774  C CD1   . PHE D 4 1100 ? 131.002 138.280 97.513  1.00 50.26  ? 1097 PHE A CD1   1 
ATOM   9775  C CD2   . PHE D 4 1100 ? 132.398 138.798 95.657  1.00 50.26  ? 1097 PHE A CD2   1 
ATOM   9776  C CE1   . PHE D 4 1100 ? 131.083 139.590 97.943  1.00 50.26  ? 1097 PHE A CE1   1 
ATOM   9777  C CE2   . PHE D 4 1100 ? 132.483 140.109 96.081  1.00 50.26  ? 1097 PHE A CE2   1 
ATOM   9778  C CZ    . PHE D 4 1100 ? 131.826 140.504 97.226  1.00 50.26  ? 1097 PHE A CZ    1 
ATOM   9779  N N     . LEU D 4 1101 ? 130.501 137.409 93.079  1.00 51.65  ? 1098 LEU A N     1 
ATOM   9780  C CA    . LEU D 4 1101 ? 130.218 138.543 92.208  1.00 51.65  ? 1098 LEU A CA    1 
ATOM   9781  C C     . LEU D 4 1101 ? 128.857 138.416 91.538  1.00 51.65  ? 1098 LEU A C     1 
ATOM   9782  O O     . LEU D 4 1101 ? 128.194 139.431 91.294  1.00 51.65  ? 1098 LEU A O     1 
ATOM   9783  C CB    . LEU D 4 1101 ? 131.318 138.686 91.158  1.00 51.65  ? 1098 LEU A CB    1 
ATOM   9784  C CG    . LEU D 4 1101 ? 131.536 140.102 90.626  1.00 51.65  ? 1098 LEU A CG    1 
ATOM   9785  C CD1   . LEU D 4 1101 ? 131.889 141.046 91.762  1.00 51.65  ? 1098 LEU A CD1   1 
ATOM   9786  C CD2   . LEU D 4 1101 ? 132.619 140.114 89.563  1.00 51.65  ? 1098 LEU A CD2   1 
ATOM   9787  N N     . GLU D 4 1102 ? 128.423 137.193 91.228  1.00 56.48  ? 1099 GLU A N     1 
ATOM   9788  C CA    . GLU D 4 1102 ? 127.113 137.017 90.615  1.00 56.48  ? 1099 GLU A CA    1 
ATOM   9789  C C     . GLU D 4 1102 ? 125.972 137.201 91.606  1.00 56.48  ? 1099 GLU A C     1 
ATOM   9790  O O     . GLU D 4 1102 ? 124.815 137.286 91.181  1.00 56.48  ? 1099 GLU A O     1 
ATOM   9791  C CB    . GLU D 4 1102 ? 127.015 135.636 89.963  1.00 56.48  ? 1099 GLU A CB    1 
ATOM   9792  C CG    . GLU D 4 1102 ? 126.846 134.491 90.946  1.00 56.48  ? 1099 GLU A CG    1 
ATOM   9793  C CD    . GLU D 4 1102 ? 126.660 133.154 90.255  1.00 56.48  ? 1099 GLU A CD    1 
ATOM   9794  O OE1   . GLU D 4 1102 ? 127.089 133.021 89.090  1.00 56.48  ? 1099 GLU A OE1   1 
ATOM   9795  O OE2   . GLU D 4 1102 ? 126.086 132.236 90.877  1.00 56.48  ? 1099 GLU A OE2   1 
ATOM   9796  N N     . GLY D 4 1103 ? 126.265 137.260 92.906  1.00 50.33  ? 1100 GLY A N     1 
ATOM   9797  C CA    . GLY D 4 1103 ? 125.210 137.464 93.885  1.00 50.33  ? 1100 GLY A CA    1 
ATOM   9798  C C     . GLY D 4 1103 ? 124.573 138.837 93.792  1.00 50.33  ? 1100 GLY A C     1 
ATOM   9799  O O     . GLY D 4 1103 ? 123.363 138.983 93.983  1.00 50.33  ? 1100 GLY A O     1 
ATOM   9800  N N     . PHE D 4 1104 ? 125.374 139.860 93.504  1.00 50.26  ? 1101 PHE A N     1 
ATOM   9801  C CA    . PHE D 4 1104 ? 124.862 141.221 93.440  1.00 50.26  ? 1101 PHE A CA    1 
ATOM   9802  C C     . PHE D 4 1104 ? 123.911 141.387 92.261  1.00 50.26  ? 1101 PHE A C     1 
ATOM   9803  O O     . PHE D 4 1104 ? 124.008 140.685 91.251  1.00 50.26  ? 1101 PHE A O     1 
ATOM   9804  C CB    . PHE D 4 1104 ? 126.013 142.219 93.326  1.00 50.26  ? 1101 PHE A CB    1 
ATOM   9805  C CG    . PHE D 4 1104 ? 126.925 142.228 94.516  1.00 50.26  ? 1101 PHE A CG    1 
ATOM   9806  C CD1   . PHE D 4 1104 ? 127.953 141.310 94.623  1.00 50.26  ? 1101 PHE A CD1   1 
ATOM   9807  C CD2   . PHE D 4 1104 ? 126.749 143.149 95.531  1.00 50.26  ? 1101 PHE A CD2   1 
ATOM   9808  C CE1   . PHE D 4 1104 ? 128.791 141.314 95.717  1.00 50.26  ? 1101 PHE A CE1   1 
ATOM   9809  C CE2   . PHE D 4 1104 ? 127.583 143.158 96.627  1.00 50.26  ? 1101 PHE A CE2   1 
ATOM   9810  C CZ    . PHE D 4 1104 ? 128.606 142.239 96.720  1.00 50.26  ? 1101 PHE A CZ    1 
ATOM   9811  N N     . ASP D 4 1105 ? 122.979 142.330 92.401  1.00 50.26  ? 1102 ASP A N     1 
ATOM   9812  C CA    . ASP D 4 1105 ? 121.975 142.538 91.361  1.00 50.26  ? 1102 ASP A CA    1 
ATOM   9813  C C     . ASP D 4 1105 ? 122.590 143.168 90.119  1.00 50.26  ? 1102 ASP A C     1 
ATOM   9814  O O     . ASP D 4 1105 ? 122.590 142.568 89.038  1.00 50.26  ? 1102 ASP A O     1 
ATOM   9815  C CB    . ASP D 4 1105 ? 120.834 143.402 91.897  1.00 50.26  ? 1102 ASP A CB    1 
ATOM   9816  C CG    . ASP D 4 1105 ? 119.913 142.639 92.825  1.00 50.26  ? 1102 ASP A CG    1 
ATOM   9817  O OD1   . ASP D 4 1105 ? 119.803 141.404 92.670  1.00 50.26  ? 1102 ASP A OD1   1 
ATOM   9818  O OD2   . ASP D 4 1105 ? 119.293 143.272 93.704  1.00 50.26  ? 1102 ASP A OD2   1 
ATOM   9819  N N     . PHE D 4 1106 ? 123.126 144.378 90.251  1.00 50.26  ? 1103 PHE A N     1 
ATOM   9820  C CA    . PHE D 4 1106 ? 123.673 145.084 89.102  1.00 50.26  ? 1103 PHE A CA    1 
ATOM   9821  C C     . PHE D 4 1106 ? 124.694 146.102 89.584  1.00 50.26  ? 1103 PHE A C     1 
ATOM   9822  O O     . PHE D 4 1106 ? 124.766 146.431 90.770  1.00 50.26  ? 1103 PHE A O     1 
ATOM   9823  C CB    . PHE D 4 1106 ? 122.569 145.764 88.283  1.00 50.26  ? 1103 PHE A CB    1 
ATOM   9824  C CG    . PHE D 4 1106 ? 121.633 146.610 89.101  1.00 50.26  ? 1103 PHE A CG    1 
ATOM   9825  C CD1   . PHE D 4 1106 ? 122.011 147.870 89.535  1.00 50.26  ? 1103 PHE A CD1   1 
ATOM   9826  C CD2   . PHE D 4 1106 ? 120.371 146.147 89.429  1.00 50.26  ? 1103 PHE A CD2   1 
ATOM   9827  C CE1   . PHE D 4 1106 ? 121.152 148.648 90.285  1.00 50.26  ? 1103 PHE A CE1   1 
ATOM   9828  C CE2   . PHE D 4 1106 ? 119.506 146.921 90.178  1.00 50.26  ? 1103 PHE A CE2   1 
ATOM   9829  C CZ    . PHE D 4 1106 ? 119.898 148.173 90.606  1.00 50.26  ? 1103 PHE A CZ    1 
ATOM   9830  N N     . LEU D 4 1107 ? 125.489 146.597 88.637  1.00 50.26  ? 1104 LEU A N     1 
ATOM   9831  C CA    . LEU D 4 1107 ? 126.441 147.677 88.889  1.00 50.26  ? 1104 LEU A CA    1 
ATOM   9832  C C     . LEU D 4 1107 ? 126.380 148.615 87.689  1.00 50.26  ? 1104 LEU A C     1 
ATOM   9833  O O     . LEU D 4 1107 ? 127.032 148.372 86.670  1.00 50.26  ? 1104 LEU A O     1 
ATOM   9834  C CB    . LEU D 4 1107 ? 127.851 147.144 89.105  1.00 50.26  ? 1104 LEU A CB    1 
ATOM   9835  C CG    . LEU D 4 1107 ? 128.932 148.220 89.200  1.00 50.26  ? 1104 LEU A CG    1 
ATOM   9836  C CD1   . LEU D 4 1107 ? 128.795 149.001 90.495  1.00 50.26  ? 1104 LEU A CD1   1 
ATOM   9837  C CD2   . LEU D 4 1107 ? 130.310 147.611 89.081  1.00 50.26  ? 1104 LEU A CD2   1 
ATOM   9838  N N     . HIS D 4 1108 ? 125.592 149.679 87.807  1.00 50.26  ? 1105 HIS A N     1 
ATOM   9839  C CA    . HIS D 4 1108 ? 125.416 150.645 86.733  1.00 50.26  ? 1105 HIS A CA    1 
ATOM   9840  C C     . HIS D 4 1108 ? 126.130 151.940 87.092  1.00 50.26  ? 1105 HIS A C     1 
ATOM   9841  O O     . HIS D 4 1108 ? 126.032 152.416 88.227  1.00 50.26  ? 1105 HIS A O     1 
ATOM   9842  C CB    . HIS D 4 1108 ? 123.930 150.897 86.455  1.00 50.26  ? 1105 HIS A CB    1 
ATOM   9843  C CG    . HIS D 4 1108 ? 123.245 151.726 87.496  1.00 50.26  ? 1105 HIS A CG    1 
ATOM   9844  N ND1   . HIS D 4 1108 ? 122.625 151.175 88.596  1.00 50.26  ? 1105 HIS A ND1   1 
ATOM   9845  C CD2   . HIS D 4 1108 ? 123.071 153.065 87.597  1.00 50.26  ? 1105 HIS A CD2   1 
ATOM   9846  C CE1   . HIS D 4 1108 ? 122.104 152.140 89.334  1.00 50.26  ? 1105 HIS A CE1   1 
ATOM   9847  N NE2   . HIS D 4 1108 ? 122.361 153.296 88.750  1.00 50.26  ? 1105 HIS A NE2   1 
ATOM   9848  N N     . TYR D 4 1109 ? 126.857 152.494 86.126  1.00 50.30  ? 1106 TYR A N     1 
ATOM   9849  C CA    . TYR D 4 1109 ? 127.632 153.712 86.336  1.00 50.30  ? 1106 TYR A CA    1 
ATOM   9850  C C     . TYR D 4 1109 ? 126.734 154.922 86.113  1.00 50.30  ? 1106 TYR A C     1 
ATOM   9851  O O     . TYR D 4 1109 ? 126.310 155.190 84.985  1.00 50.30  ? 1106 TYR A O     1 
ATOM   9852  C CB    . TYR D 4 1109 ? 128.831 153.739 85.394  1.00 50.30  ? 1106 TYR A CB    1 
ATOM   9853  C CG    . TYR D 4 1109 ? 129.498 155.088 85.281  1.00 50.30  ? 1106 TYR A CG    1 
ATOM   9854  C CD1   . TYR D 4 1109 ? 130.244 155.605 86.329  1.00 50.30  ? 1106 TYR A CD1   1 
ATOM   9855  C CD2   . TYR D 4 1109 ? 129.381 155.846 84.124  1.00 50.30  ? 1106 TYR A CD2   1 
ATOM   9856  C CE1   . TYR D 4 1109 ? 130.857 156.837 86.228  1.00 50.30  ? 1106 TYR A CE1   1 
ATOM   9857  C CE2   . TYR D 4 1109 ? 129.989 157.080 84.015  1.00 50.30  ? 1106 TYR A CE2   1 
ATOM   9858  C CZ    . TYR D 4 1109 ? 130.725 157.571 85.070  1.00 50.30  ? 1106 TYR A CZ    1 
ATOM   9859  O OH    . TYR D 4 1109 ? 131.333 158.800 84.965  1.00 50.30  ? 1106 TYR A OH    1 
ATOM   9860  N N     . ASP D 4 1110 ? 126.444 155.654 87.186  1.00 53.24  ? 1107 ASP A N     1 
ATOM   9861  C CA    . ASP D 4 1110 ? 125.649 156.873 87.083  1.00 53.24  ? 1107 ASP A CA    1 
ATOM   9862  C C     . ASP D 4 1110 ? 126.463 157.937 86.358  1.00 53.24  ? 1107 ASP A C     1 
ATOM   9863  O O     . ASP D 4 1110 ? 127.401 158.506 86.925  1.00 53.24  ? 1107 ASP A O     1 
ATOM   9864  C CB    . ASP D 4 1110 ? 125.232 157.352 88.470  1.00 53.24  ? 1107 ASP A CB    1 
ATOM   9865  C CG    . ASP D 4 1110 ? 124.182 158.443 88.418  1.00 53.24  ? 1107 ASP A CG    1 
ATOM   9866  O OD1   . ASP D 4 1110 ? 123.468 158.534 87.398  1.00 53.24  ? 1107 ASP A OD1   1 
ATOM   9867  O OD2   . ASP D 4 1110 ? 124.071 159.210 89.397  1.00 53.24  ? 1107 ASP A OD2   1 
ATOM   9868  N N     . VAL D 4 1111 ? 126.107 158.205 85.101  1.00 52.54  ? 1108 VAL A N     1 
ATOM   9869  C CA    . VAL D 4 1111 ? 126.888 159.132 84.287  1.00 52.54  ? 1108 VAL A CA    1 
ATOM   9870  C C     . VAL D 4 1111 ? 126.786 160.551 84.835  1.00 52.54  ? 1108 VAL A C     1 
ATOM   9871  O O     . VAL D 4 1111 ? 127.754 161.320 84.785  1.00 52.54  ? 1108 VAL A O     1 
ATOM   9872  C CB    . VAL D 4 1111 ? 126.445 159.047 82.814  1.00 52.54  ? 1108 VAL A CB    1 
ATOM   9873  C CG1   . VAL D 4 1111 ? 124.954 159.326 82.678  1.00 52.54  ? 1108 VAL A CG1   1 
ATOM   9874  C CG2   . VAL D 4 1111 ? 127.259 160.002 81.951  1.00 52.54  ? 1108 VAL A CG2   1 
ATOM   9875  N N     . LYS D 4 1112 ? 125.619 160.921 85.368  1.00 53.60  ? 1109 LYS A N     1 
ATOM   9876  C CA    . LYS D 4 1112 ? 125.423 162.287 85.845  1.00 53.60  ? 1109 LYS A CA    1 
ATOM   9877  C C     . LYS D 4 1112 ? 126.330 162.605 87.029  1.00 53.60  ? 1109 LYS A C     1 
ATOM   9878  O O     . LYS D 4 1112 ? 126.920 163.690 87.089  1.00 53.60  ? 1109 LYS A O     1 
ATOM   9879  C CB    . LYS D 4 1112 ? 123.955 162.505 86.211  1.00 53.60  ? 1109 LYS A CB    1 
ATOM   9880  C CG    . LYS D 4 1112 ? 123.662 163.852 86.853  1.00 53.60  ? 1109 LYS A CG    1 
ATOM   9881  C CD    . LYS D 4 1112 ? 122.191 163.993 87.238  1.00 53.60  ? 1109 LYS A CD    1 
ATOM   9882  C CE    . LYS D 4 1112 ? 121.619 162.723 87.855  1.00 53.60  ? 1109 LYS A CE    1 
ATOM   9883  N NZ    . LYS D 4 1112 ? 122.419 162.223 89.009  1.00 53.60  ? 1109 LYS A NZ    1 
ATOM   9884  N N     . THR D 4 1113 ? 126.460 161.675 87.976  1.00 51.11  ? 1110 THR A N     1 
ATOM   9885  C CA    . THR D 4 1113 ? 127.261 161.911 89.170  1.00 51.11  ? 1110 THR A CA    1 
ATOM   9886  C C     . THR D 4 1113 ? 128.652 161.298 89.104  1.00 51.11  ? 1110 THR A C     1 
ATOM   9887  O O     . THR D 4 1113 ? 129.527 161.708 89.874  1.00 51.11  ? 1110 THR A O     1 
ATOM   9888  C CB    . THR D 4 1113 ? 126.544 161.367 90.412  1.00 51.11  ? 1110 THR A CB    1 
ATOM   9889  O OG1   . THR D 4 1113 ? 126.222 159.985 90.214  1.00 51.11  ? 1110 THR A OG1   1 
ATOM   9890  C CG2   . THR D 4 1113 ? 125.270 162.149 90.677  1.00 51.11  ? 1110 THR A CG2   1 
ATOM   9891  N N     . GLY D 4 1114 ? 128.880 160.337 88.214  1.00 50.26  ? 1111 GLY A N     1 
ATOM   9892  C CA    . GLY D 4 1114 ? 130.169 159.681 88.153  1.00 50.26  ? 1111 GLY A CA    1 
ATOM   9893  C C     . GLY D 4 1114 ? 130.395 158.632 89.214  1.00 50.26  ? 1111 GLY A C     1 
ATOM   9894  O O     . GLY D 4 1114 ? 131.539 158.219 89.427  1.00 50.26  ? 1111 GLY A O     1 
ATOM   9895  N N     . ASP D 4 1115 ? 129.340 158.186 89.889  1.00 50.26  ? 1112 ASP A N     1 
ATOM   9896  C CA    . ASP D 4 1115 ? 129.438 157.210 90.964  1.00 50.26  ? 1112 ASP A CA    1 
ATOM   9897  C C     . ASP D 4 1115 ? 128.834 155.887 90.518  1.00 50.26  ? 1112 ASP A C     1 
ATOM   9898  O O     . ASP D 4 1115 ? 127.742 155.861 89.941  1.00 50.26  ? 1112 ASP A O     1 
ATOM   9899  C CB    . ASP D 4 1115 ? 128.728 157.708 92.225  1.00 50.26  ? 1112 ASP A CB    1 
ATOM   9900  C CG    . ASP D 4 1115 ? 129.360 158.961 92.795  1.00 50.26  ? 1112 ASP A CG    1 
ATOM   9901  O OD1   . ASP D 4 1115 ? 130.543 159.221 92.492  1.00 50.26  ? 1112 ASP A OD1   1 
ATOM   9902  O OD2   . ASP D 4 1115 ? 128.676 159.683 93.550  1.00 50.26  ? 1112 ASP A OD2   1 
ATOM   9903  N N     . PHE D 4 1116 ? 129.545 154.795 90.785  1.00 50.26  ? 1113 PHE A N     1 
ATOM   9904  C CA    . PHE D 4 1116 ? 129.018 153.463 90.529  1.00 50.26  ? 1113 PHE A CA    1 
ATOM   9905  C C     . PHE D 4 1116 ? 128.095 153.050 91.668  1.00 50.26  ? 1113 PHE A C     1 
ATOM   9906  O O     . PHE D 4 1116 ? 128.410 153.268 92.841  1.00 50.26  ? 1113 PHE A O     1 
ATOM   9907  C CB    . PHE D 4 1116 ? 130.155 152.454 90.386  1.00 50.26  ? 1113 PHE A CB    1 
ATOM   9908  C CG    . PHE D 4 1116 ? 130.990 152.647 89.157  1.00 50.26  ? 1113 PHE A CG    1 
ATOM   9909  C CD1   . PHE D 4 1116 ? 132.037 153.550 89.151  1.00 50.26  ? 1113 PHE A CD1   1 
ATOM   9910  C CD2   . PHE D 4 1116 ? 130.738 151.914 88.011  1.00 50.26  ? 1113 PHE A CD2   1 
ATOM   9911  C CE1   . PHE D 4 1116 ? 132.809 153.726 88.022  1.00 50.26  ? 1113 PHE A CE1   1 
ATOM   9912  C CE2   . PHE D 4 1116 ? 131.508 152.083 86.881  1.00 50.26  ? 1113 PHE A CE2   1 
ATOM   9913  C CZ    . PHE D 4 1116 ? 132.544 152.990 86.886  1.00 50.26  ? 1113 PHE A CZ    1 
ATOM   9914  N N     . ILE D 4 1117 ? 126.959 152.452 91.323  1.00 50.26  ? 1114 ILE A N     1 
ATOM   9915  C CA    . ILE D 4 1117 ? 125.988 151.977 92.301  1.00 50.26  ? 1114 ILE A CA    1 
ATOM   9916  C C     . ILE D 4 1117 ? 125.908 150.463 92.183  1.00 50.26  ? 1114 ILE A C     1 
ATOM   9917  O O     . ILE D 4 1117 ? 125.606 149.932 91.108  1.00 50.26  ? 1114 ILE A O     1 
ATOM   9918  C CB    . ILE D 4 1117 ? 124.610 152.622 92.092  1.00 50.26  ? 1114 ILE A CB    1 
ATOM   9919  C CG1   . ILE D 4 1117 ? 124.654 154.101 92.479  1.00 50.26  ? 1114 ILE A CG1   1 
ATOM   9920  C CG2   . ILE D 4 1117 ? 123.551 151.885 92.894  1.00 50.26  ? 1114 ILE A CG2   1 
ATOM   9921  C CD1   . ILE D 4 1117 ? 123.328 154.812 92.323  1.00 50.26  ? 1114 ILE A CD1   1 
ATOM   9922  N N     . LEU D 4 1118 ? 126.172 149.769 93.286  1.00 50.26  ? 1115 LEU A N     1 
ATOM   9923  C CA    . LEU D 4 1118 ? 126.183 148.309 93.331  1.00 50.26  ? 1115 LEU A CA    1 
ATOM   9924  C C     . LEU D 4 1118 ? 125.087 147.863 94.294  1.00 50.26  ? 1115 LEU A C     1 
ATOM   9925  O O     . LEU D 4 1118 ? 125.315 147.740 95.499  1.00 50.26  ? 1115 LEU A O     1 
ATOM   9926  C CB    . LEU D 4 1118 ? 127.551 147.789 93.753  1.00 50.26  ? 1115 LEU A CB    1 
ATOM   9927  C CG    . LEU D 4 1118 ? 127.708 146.274 93.874  1.00 50.26  ? 1115 LEU A CG    1 
ATOM   9928  C CD1   . LEU D 4 1118 ? 127.877 145.641 92.505  1.00 50.26  ? 1115 LEU A CD1   1 
ATOM   9929  C CD2   . LEU D 4 1118 ? 128.884 145.938 94.771  1.00 50.26  ? 1115 LEU A CD2   1 
ATOM   9930  N N     . HIS D 4 1119 ? 123.893 147.628 93.757  1.00 50.26  ? 1116 HIS A N     1 
ATOM   9931  C CA    . HIS D 4 1119 ? 122.766 147.223 94.586  1.00 50.26  ? 1116 HIS A CA    1 
ATOM   9932  C C     . HIS D 4 1119 ? 122.983 145.812 95.115  1.00 50.26  ? 1116 HIS A C     1 
ATOM   9933  O O     . HIS D 4 1119 ? 123.322 144.898 94.358  1.00 50.26  ? 1116 HIS A O     1 
ATOM   9934  C CB    . HIS D 4 1119 ? 121.468 147.299 93.788  1.00 50.26  ? 1116 HIS A CB    1 
ATOM   9935  C CG    . HIS D 4 1119 ? 120.235 147.149 94.623  1.00 50.26  ? 1116 HIS A CG    1 
ATOM   9936  N ND1   . HIS D 4 1119 ? 119.477 148.226 95.030  1.00 50.26  ? 1116 HIS A ND1   1 
ATOM   9937  C CD2   . HIS D 4 1119 ? 119.628 146.049 95.127  1.00 50.26  ? 1116 HIS A CD2   1 
ATOM   9938  C CE1   . HIS D 4 1119 ? 118.456 147.795 95.750  1.00 50.26  ? 1116 HIS A CE1   1 
ATOM   9939  N NE2   . HIS D 4 1119 ? 118.524 146.479 95.823  1.00 50.26  ? 1116 HIS A NE2   1 
ATOM   9940  N N     . PHE D 4 1120 ? 122.784 145.636 96.418  1.00 50.26  ? 1117 PHE A N     1 
ATOM   9941  C CA    . PHE D 4 1120 ? 122.995 144.358 97.080  1.00 50.26  ? 1117 PHE A CA    1 
ATOM   9942  C C     . PHE D 4 1120 ? 121.827 144.069 98.008  1.00 50.26  ? 1117 PHE A C     1 
ATOM   9943  O O     . PHE D 4 1120 ? 121.332 144.967 98.695  1.00 50.26  ? 1117 PHE A O     1 
ATOM   9944  C CB    . PHE D 4 1120 ? 124.304 144.359 97.875  1.00 50.26  ? 1117 PHE A CB    1 
ATOM   9945  C CG    . PHE D 4 1120 ? 124.505 143.132 98.713  1.00 50.26  ? 1117 PHE A CG    1 
ATOM   9946  C CD1   . PHE D 4 1120 ? 124.443 141.873 98.145  1.00 50.26  ? 1117 PHE A CD1   1 
ATOM   9947  C CD2   . PHE D 4 1120 ? 124.750 143.238 100.070 1.00 50.26  ? 1117 PHE A CD2   1 
ATOM   9948  C CE1   . PHE D 4 1120 ? 124.628 140.742 98.914  1.00 50.26  ? 1117 PHE A CE1   1 
ATOM   9949  C CE2   . PHE D 4 1120 ? 124.934 142.111 100.844 1.00 50.26  ? 1117 PHE A CE2   1 
ATOM   9950  C CZ    . PHE D 4 1120 ? 124.872 140.862 100.265 1.00 50.26  ? 1117 PHE A CZ    1 
ATOM   9951  N N     . LYS D 4 1121 ? 121.389 142.814 98.024  1.00 50.26  ? 1118 LYS A N     1 
ATOM   9952  C CA    . LYS D 4 1121 ? 120.304 142.366 98.885  1.00 50.26  ? 1118 LYS A CA    1 
ATOM   9953  C C     . LYS D 4 1121 ? 120.840 141.348 99.880  1.00 50.26  ? 1118 LYS A C     1 
ATOM   9954  O O     . LYS D 4 1121 ? 121.581 140.435 99.501  1.00 50.26  ? 1118 LYS A O     1 
ATOM   9955  C CB    . LYS D 4 1121 ? 119.168 141.760 98.060  1.00 50.26  ? 1118 LYS A CB    1 
ATOM   9956  C CG    . LYS D 4 1121 ? 118.719 142.626 96.897  1.00 50.26  ? 1118 LYS A CG    1 
ATOM   9957  C CD    . LYS D 4 1121 ? 117.351 142.206 96.396  1.00 50.26  ? 1118 LYS A CD    1 
ATOM   9958  C CE    . LYS D 4 1121 ? 117.380 140.791 95.841  1.00 50.26  ? 1118 LYS A CE    1 
ATOM   9959  N NZ    . LYS D 4 1121 ? 118.181 140.694 94.591  1.00 50.26  ? 1118 LYS A NZ    1 
ATOM   9960  N N     . MET D 4 1122 ? 120.459 141.501 101.151 1.00 50.26  ? 1119 MET A N     1 
ATOM   9961  C CA    . MET D 4 1122 ? 120.957 140.617 102.199 1.00 50.26  ? 1119 MET A CA    1 
ATOM   9962  C C     . MET D 4 1122 ? 120.444 139.188 102.084 1.00 50.26  ? 1119 MET A C     1 
ATOM   9963  O O     . MET D 4 1122 ? 120.958 138.313 102.788 1.00 50.26  ? 1119 MET A O     1 
ATOM   9964  C CB    . MET D 4 1122 ? 120.605 141.177 103.578 1.00 50.26  ? 1119 MET A CB    1 
ATOM   9965  C CG    . MET D 4 1122 ? 121.167 142.558 103.848 1.00 50.26  ? 1119 MET A CG    1 
ATOM   9966  S SD    . MET D 4 1122 ? 122.969 142.514 103.884 1.00 50.26  ? 1119 MET A SD    1 
ATOM   9967  C CE    . MET D 4 1122 ? 123.318 143.671 105.202 1.00 50.26  ? 1119 MET A CE    1 
ATOM   9968  N N     . ASN D 4 1123 ? 119.456 138.922 101.231 1.00 50.26  ? 1120 ASN A N     1 
ATOM   9969  C CA    . ASN D 4 1123 ? 118.972 137.566 101.022 1.00 50.26  ? 1120 ASN A CA    1 
ATOM   9970  C C     . ASN D 4 1123 ? 119.798 136.802 99.993  1.00 50.26  ? 1120 ASN A C     1 
ATOM   9971  O O     . ASN D 4 1123 ? 119.318 135.806 99.440  1.00 50.26  ? 1120 ASN A O     1 
ATOM   9972  C CB    . ASN D 4 1123 ? 117.496 137.583 100.613 1.00 50.26  ? 1120 ASN A CB    1 
ATOM   9973  C CG    . ASN D 4 1123 ? 117.256 138.311 99.304  1.00 50.26  ? 1120 ASN A CG    1 
ATOM   9974  O OD1   . ASN D 4 1123 ? 118.184 138.820 98.679  1.00 50.26  ? 1120 ASN A OD1   1 
ATOM   9975  N ND2   . ASN D 4 1123 ? 115.998 138.361 98.882  1.00 50.26  ? 1120 ASN A ND2   1 
ATOM   9976  N N     . ARG D 4 1124 ? 121.024 137.247 99.726  1.00 50.26  ? 1121 ARG A N     1 
ATOM   9977  C CA    . ARG D 4 1124 ? 121.901 136.615 98.754  1.00 50.26  ? 1121 ARG A CA    1 
ATOM   9978  C C     . ARG D 4 1124 ? 123.290 136.450 99.353  1.00 50.26  ? 1121 ARG A C     1 
ATOM   9979  O O     . ARG D 4 1124 ? 123.666 137.143 100.301 1.00 50.26  ? 1121 ARG A O     1 
ATOM   9980  C CB    . ARG D 4 1124 ? 121.985 137.428 97.457  1.00 50.26  ? 1121 ARG A CB    1 
ATOM   9981  C CG    . ARG D 4 1124 ? 120.661 137.580 96.732  1.00 50.26  ? 1121 ARG A CG    1 
ATOM   9982  C CD    . ARG D 4 1124 ? 120.248 136.281 96.068  1.00 50.26  ? 1121 ARG A CD    1 
ATOM   9983  N NE    . ARG D 4 1124 ? 121.144 135.923 94.975  1.00 50.26  ? 1121 ARG A NE    1 
ATOM   9984  C CZ    . ARG D 4 1124 ? 121.083 136.442 93.757  1.00 50.26  ? 1121 ARG A CZ    1 
ATOM   9985  N NH1   . ARG D 4 1124 ? 120.178 137.352 93.437  1.00 50.26  ? 1121 ARG A NH1   1 
ATOM   9986  N NH2   . ARG D 4 1124 ? 121.953 136.037 92.836  1.00 50.26  ? 1121 ARG A NH2   1 
ATOM   9987  N N     . ASN D 4 1125 ? 124.049 135.513 98.780  1.00 50.26  ? 1122 ASN A N     1 
ATOM   9988  C CA    . ASN D 4 1125 ? 125.428 135.246 99.192  1.00 50.26  ? 1122 ASN A CA    1 
ATOM   9989  C C     . ASN D 4 1125 ? 125.514 134.907 100.678 1.00 50.26  ? 1122 ASN A C     1 
ATOM   9990  O O     . ASN D 4 1125 ? 126.454 135.304 101.367 1.00 50.26  ? 1122 ASN A O     1 
ATOM   9991  C CB    . ASN D 4 1125 ? 126.344 136.424 98.855  1.00 50.26  ? 1122 ASN A CB    1 
ATOM   9992  C CG    . ASN D 4 1125 ? 126.820 136.400 97.419  1.00 50.26  ? 1122 ASN A CG    1 
ATOM   9993  O OD1   . ASN D 4 1125 ? 126.966 135.336 96.819  1.00 50.26  ? 1122 ASN A OD1   1 
ATOM   9994  N ND2   . ASN D 4 1125 ? 127.063 137.578 96.857  1.00 50.26  ? 1122 ASN A ND2   1 
ATOM   9995  N N     . LEU D 4 1126 ? 124.530 134.149 101.171 1.00 50.26  ? 1123 LEU A N     1 
ATOM   9996  C CA    . LEU D 4 1126 ? 124.479 133.832 102.595 1.00 50.26  ? 1123 LEU A CA    1 
ATOM   9997  C C     . LEU D 4 1126 ? 125.711 133.062 103.052 1.00 50.26  ? 1123 LEU A C     1 
ATOM   9998  O O     . LEU D 4 1126 ? 126.082 133.132 104.229 1.00 50.26  ? 1123 LEU A O     1 
ATOM   9999  C CB    . LEU D 4 1126 ? 123.215 133.034 102.920 1.00 50.26  ? 1123 LEU A CB    1 
ATOM   10000 C CG    . LEU D 4 1126 ? 121.907 133.793 103.164 1.00 50.26  ? 1123 LEU A CG    1 
ATOM   10001 C CD1   . LEU D 4 1126 ? 122.028 134.680 104.395 1.00 50.26  ? 1123 LEU A CD1   1 
ATOM   10002 C CD2   . LEU D 4 1126 ? 121.476 134.604 101.954 1.00 50.26  ? 1123 LEU A CD2   1 
ATOM   10003 N N     . SER D 4 1127 ? 126.353 132.323 102.145 1.00 51.28  ? 1124 SER A N     1 
ATOM   10004 C CA    . SER D 4 1127 ? 127.554 131.585 102.517 1.00 51.28  ? 1124 SER A CA    1 
ATOM   10005 C C     . SER D 4 1127 ? 128.692 132.521 102.899 1.00 51.28  ? 1124 SER A C     1 
ATOM   10006 O O     . SER D 4 1127 ? 129.556 132.152 103.703 1.00 51.28  ? 1124 SER A O     1 
ATOM   10007 C CB    . SER D 4 1127 ? 127.982 130.666 101.374 1.00 51.28  ? 1124 SER A CB    1 
ATOM   10008 O OG    . SER D 4 1127 ? 128.106 131.386 100.161 1.00 51.28  ? 1124 SER A OG    1 
ATOM   10009 N N     . PHE D 4 1128 ? 128.713 133.730 102.341 1.00 50.26  ? 1125 PHE A N     1 
ATOM   10010 C CA    . PHE D 4 1128 ? 129.770 134.691 102.621 1.00 50.26  ? 1125 PHE A CA    1 
ATOM   10011 C C     . PHE D 4 1128 ? 129.393 135.710 103.687 1.00 50.26  ? 1125 PHE A C     1 
ATOM   10012 O O     . PHE D 4 1128 ? 130.283 136.384 104.214 1.00 50.26  ? 1125 PHE A O     1 
ATOM   10013 C CB    . PHE D 4 1128 ? 130.170 135.420 101.334 1.00 50.26  ? 1125 PHE A CB    1 
ATOM   10014 C CG    . PHE D 4 1128 ? 130.507 134.497 100.200 1.00 50.26  ? 1125 PHE A CG    1 
ATOM   10015 C CD1   . PHE D 4 1128 ? 131.389 133.446 100.387 1.00 50.26  ? 1125 PHE A CD1   1 
ATOM   10016 C CD2   . PHE D 4 1128 ? 129.941 134.676 98.951  1.00 50.26  ? 1125 PHE A CD2   1 
ATOM   10017 C CE1   . PHE D 4 1128 ? 131.699 132.592 99.348  1.00 50.26  ? 1125 PHE A CE1   1 
ATOM   10018 C CE2   . PHE D 4 1128 ? 130.249 133.824 97.908  1.00 50.26  ? 1125 PHE A CE2   1 
ATOM   10019 C CZ    . PHE D 4 1128 ? 131.129 132.782 98.107  1.00 50.26  ? 1125 PHE A CZ    1 
ATOM   10020 N N     . GLN D 4 1129 ? 128.110 135.838 104.018 1.00 50.26  ? 1126 GLN A N     1 
ATOM   10021 C CA    . GLN D 4 1129 ? 127.698 136.764 105.060 1.00 50.26  ? 1126 GLN A CA    1 
ATOM   10022 C C     . GLN D 4 1129 ? 128.160 136.267 106.428 1.00 50.26  ? 1126 GLN A C     1 
ATOM   10023 O O     . GLN D 4 1129 ? 128.587 135.122 106.598 1.00 50.26  ? 1126 GLN A O     1 
ATOM   10024 C CB    . GLN D 4 1129 ? 126.181 136.942 105.062 1.00 50.26  ? 1126 GLN A CB    1 
ATOM   10025 C CG    . GLN D 4 1129 ? 125.568 137.171 103.698 1.00 50.26  ? 1126 GLN A CG    1 
ATOM   10026 C CD    . GLN D 4 1129 ? 125.638 138.615 103.263 1.00 50.26  ? 1126 GLN A CD    1 
ATOM   10027 O OE1   . GLN D 4 1129 ? 126.719 139.154 103.034 1.00 50.26  ? 1126 GLN A OE1   1 
ATOM   10028 N NE2   . GLN D 4 1129 ? 124.481 139.253 103.148 1.00 50.26  ? 1126 GLN A NE2   1 
ATOM   10029 N N     . ARG D 4 1130 ? 128.073 137.154 107.415 1.00 50.26  ? 1127 ARG A N     1 
ATOM   10030 C CA    . ARG D 4 1130 ? 128.399 136.808 108.790 1.00 50.26  ? 1127 ARG A CA    1 
ATOM   10031 C C     . ARG D 4 1130 ? 127.180 136.364 109.588 1.00 50.26  ? 1127 ARG A C     1 
ATOM   10032 O O     . ARG D 4 1130 ? 127.311 136.073 110.781 1.00 50.26  ? 1127 ARG A O     1 
ATOM   10033 C CB    . ARG D 4 1130 ? 129.073 137.992 109.488 1.00 50.26  ? 1127 ARG A CB    1 
ATOM   10034 C CG    . ARG D 4 1130 ? 130.193 137.587 110.434 1.00 50.26  ? 1127 ARG A CG    1 
ATOM   10035 C CD    . ARG D 4 1130 ? 130.908 138.802 110.996 1.00 50.26  ? 1127 ARG A CD    1 
ATOM   10036 N NE    . ARG D 4 1130 ? 131.771 139.444 110.012 1.00 50.26  ? 1127 ARG A NE    1 
ATOM   10037 C CZ    . ARG D 4 1130 ? 131.493 140.590 109.407 1.00 50.26  ? 1127 ARG A CZ    1 
ATOM   10038 N NH1   . ARG D 4 1130 ? 130.366 141.242 109.644 1.00 50.26  ? 1127 ARG A NH1   1 
ATOM   10039 N NH2   . ARG D 4 1130 ? 132.366 141.095 108.541 1.00 50.26  ? 1127 ARG A NH2   1 
ATOM   10040 N N     . GLY D 4 1131 ? 126.008 136.301 108.963 1.00 50.26  ? 1128 GLY A N     1 
ATOM   10041 C CA    . GLY D 4 1131 ? 124.814 135.851 109.647 1.00 50.26  ? 1128 GLY A CA    1 
ATOM   10042 C C     . GLY D 4 1131 ? 124.084 136.905 110.443 1.00 50.26  ? 1128 GLY A C     1 
ATOM   10043 O O     . GLY D 4 1131 ? 123.376 136.564 111.397 1.00 50.26  ? 1128 GLY A O     1 
ATOM   10044 N N     . LEU D 4 1132 ? 124.233 138.180 110.089 1.00 50.26  ? 1129 LEU A N     1 
ATOM   10045 C CA    . LEU D 4 1132 ? 123.576 139.281 110.792 1.00 50.26  ? 1129 LEU A CA    1 
ATOM   10046 C C     . LEU D 4 1132 ? 122.821 140.127 109.777 1.00 50.26  ? 1129 LEU A C     1 
ATOM   10047 O O     . LEU D 4 1132 ? 123.344 141.132 109.277 1.00 50.26  ? 1129 LEU A O     1 
ATOM   10048 C CB    . LEU D 4 1132 ? 124.585 140.123 111.569 1.00 50.26  ? 1129 LEU A CB    1 
ATOM   10049 C CG    . LEU D 4 1132 ? 125.405 139.375 112.618 1.00 50.26  ? 1129 LEU A CG    1 
ATOM   10050 C CD1   . LEU D 4 1132 ? 126.447 140.291 113.223 1.00 50.26  ? 1129 LEU A CD1   1 
ATOM   10051 C CD2   . LEU D 4 1132 ? 124.503 138.801 113.697 1.00 50.26  ? 1129 LEU A CD2   1 
ATOM   10052 N N     . PRO D 4 1133 ? 121.591 139.744 109.438 1.00 50.26  ? 1130 PRO A N     1 
ATOM   10053 C CA    . PRO D 4 1133 ? 120.817 140.530 108.467 1.00 50.26  ? 1130 PRO A CA    1 
ATOM   10054 C C     . PRO D 4 1133 ? 120.437 141.906 108.990 1.00 50.26  ? 1130 PRO A C     1 
ATOM   10055 O O     . PRO D 4 1133 ? 120.688 142.918 108.328 1.00 50.26  ? 1130 PRO A O     1 
ATOM   10056 C CB    . PRO D 4 1133 ? 119.576 139.661 108.222 1.00 50.26  ? 1130 PRO A CB    1 
ATOM   10057 C CG    . PRO D 4 1133 ? 119.461 138.804 109.436 1.00 50.26  ? 1130 PRO A CG    1 
ATOM   10058 C CD    . PRO D 4 1133 ? 120.862 138.553 109.905 1.00 50.26  ? 1130 PRO A CD    1 
ATOM   10059 N N     . GLY D 4 1134 ? 119.840 141.956 110.179 1.00 50.26  ? 1131 GLY A N     1 
ATOM   10060 C CA    . GLY D 4 1134 ? 119.386 143.223 110.714 1.00 50.26  ? 1131 GLY A CA    1 
ATOM   10061 C C     . GLY D 4 1134 ? 118.265 143.815 109.875 1.00 50.26  ? 1131 GLY A C     1 
ATOM   10062 O O     . GLY D 4 1134 ? 117.526 143.111 109.180 1.00 50.26  ? 1131 GLY A O     1 
ATOM   10063 N N     . PHE D 4 1135 ? 118.141 145.135 109.943 1.00 50.26  ? 1132 PHE A N     1 
ATOM   10064 C CA    . PHE D 4 1135 ? 117.178 145.861 109.127 1.00 50.26  ? 1132 PHE A CA    1 
ATOM   10065 C C     . PHE D 4 1135 ? 117.772 146.064 107.734 1.00 50.26  ? 1132 PHE A C     1 
ATOM   10066 O O     . PHE D 4 1135 ? 118.799 145.477 107.384 1.00 50.26  ? 1132 PHE A O     1 
ATOM   10067 C CB    . PHE D 4 1135 ? 116.807 147.177 109.804 1.00 50.26  ? 1132 PHE A CB    1 
ATOM   10068 C CG    . PHE D 4 1135 ? 115.417 147.648 109.498 1.00 50.26  ? 1132 PHE A CG    1 
ATOM   10069 C CD1   . PHE D 4 1135 ? 114.317 146.956 109.974 1.00 50.26  ? 1132 PHE A CD1   1 
ATOM   10070 C CD2   . PHE D 4 1135 ? 115.208 148.790 108.745 1.00 50.26  ? 1132 PHE A CD2   1 
ATOM   10071 C CE1   . PHE D 4 1135 ? 113.036 147.389 109.698 1.00 50.26  ? 1132 PHE A CE1   1 
ATOM   10072 C CE2   . PHE D 4 1135 ? 113.930 149.229 108.465 1.00 50.26  ? 1132 PHE A CE2   1 
ATOM   10073 C CZ    . PHE D 4 1135 ? 112.842 148.527 108.943 1.00 50.26  ? 1132 PHE A CZ    1 
ATOM   10074 N N     . MET D 4 1136 ? 117.121 146.897 106.915 1.00 50.26  ? 1133 MET A N     1 
ATOM   10075 C CA    . MET D 4 1136 ? 117.644 147.288 105.609 1.00 50.26  ? 1133 MET A CA    1 
ATOM   10076 C C     . MET D 4 1136 ? 117.908 146.076 104.723 1.00 50.26  ? 1133 MET A C     1 
ATOM   10077 O O     . MET D 4 1136 ? 119.068 145.693 104.529 1.00 50.26  ? 1133 MET A O     1 
ATOM   10078 C CB    . MET D 4 1136 ? 118.922 148.113 105.768 1.00 50.26  ? 1133 MET A CB    1 
ATOM   10079 C CG    . MET D 4 1136 ? 118.702 149.486 106.372 1.00 50.26  ? 1133 MET A CG    1 
ATOM   10080 S SD    . MET D 4 1136 ? 117.134 150.208 105.861 1.00 50.26  ? 1133 MET A SD    1 
ATOM   10081 C CE    . MET D 4 1136 ? 117.653 151.133 104.419 1.00 50.26  ? 1133 MET A CE    1 
ATOM   10082 N N     . PRO D 4 1137 ? 116.865 145.436 104.191 1.00 50.26  ? 1134 PRO A N     1 
ATOM   10083 C CA    . PRO D 4 1137 ? 117.090 144.249 103.349 1.00 50.26  ? 1134 PRO A CA    1 
ATOM   10084 C C     . PRO D 4 1137 ? 117.931 144.523 102.114 1.00 50.26  ? 1134 PRO A C     1 
ATOM   10085 O O     . PRO D 4 1137 ? 118.603 143.608 101.621 1.00 50.26  ? 1134 PRO A O     1 
ATOM   10086 C CB    . PRO D 4 1137 ? 115.666 143.814 102.976 1.00 50.26  ? 1134 PRO A CB    1 
ATOM   10087 C CG    . PRO D 4 1137 ? 114.850 145.059 103.091 1.00 50.26  ? 1134 PRO A CG    1 
ATOM   10088 C CD    . PRO D 4 1137 ? 115.447 145.831 104.229 1.00 50.26  ? 1134 PRO A CD    1 
ATOM   10089 N N     . ALA D 4 1138 ? 117.919 145.748 101.596 1.00 50.26  ? 1135 ALA A N     1 
ATOM   10090 C CA    . ALA D 4 1138 ? 118.664 146.098 100.398 1.00 50.26  ? 1135 ALA A CA    1 
ATOM   10091 C C     . ALA D 4 1138 ? 119.608 147.259 100.680 1.00 50.26  ? 1135 ALA A C     1 
ATOM   10092 O O     . ALA D 4 1138 ? 119.293 148.165 101.456 1.00 50.26  ? 1135 ALA A O     1 
ATOM   10093 C CB    . ALA D 4 1138 ? 117.723 146.465 99.245  1.00 50.26  ? 1135 ALA A CB    1 
ATOM   10094 N N     . TRP D 4 1139 ? 120.772 147.221 100.035 1.00 50.26  ? 1136 TRP A N     1 
ATOM   10095 C CA    . TRP D 4 1139 ? 121.786 148.255 100.167 1.00 50.26  ? 1136 TRP A CA    1 
ATOM   10096 C C     . TRP D 4 1139 ? 122.217 148.721 98.783  1.00 50.26  ? 1136 TRP A C     1 
ATOM   10097 O O     . TRP D 4 1139 ? 122.082 148.000 97.792  1.00 50.26  ? 1136 TRP A O     1 
ATOM   10098 C CB    . TRP D 4 1139 ? 123.007 147.755 100.948 1.00 50.26  ? 1136 TRP A CB    1 
ATOM   10099 C CG    . TRP D 4 1139 ? 122.782 147.614 102.419 1.00 50.26  ? 1136 TRP A CG    1 
ATOM   10100 C CD1   . TRP D 4 1139 ? 122.684 146.454 103.123 1.00 50.26  ? 1136 TRP A CD1   1 
ATOM   10101 C CD2   . TRP D 4 1139 ? 122.650 148.674 103.373 1.00 50.26  ? 1136 TRP A CD2   1 
ATOM   10102 N NE1   . TRP D 4 1139 ? 122.488 146.723 104.455 1.00 50.26  ? 1136 TRP A NE1   1 
ATOM   10103 C CE2   . TRP D 4 1139 ? 122.464 148.080 104.634 1.00 50.26  ? 1136 TRP A CE2   1 
ATOM   10104 C CE3   . TRP D 4 1139 ? 122.663 150.068 103.281 1.00 50.26  ? 1136 TRP A CE3   1 
ATOM   10105 C CZ2   . TRP D 4 1139 ? 122.296 148.829 105.794 1.00 50.26  ? 1136 TRP A CZ2   1 
ATOM   10106 C CZ3   . TRP D 4 1139 ? 122.496 150.810 104.433 1.00 50.26  ? 1136 TRP A CZ3   1 
ATOM   10107 C CH2   . TRP D 4 1139 ? 122.314 150.190 105.673 1.00 50.26  ? 1136 TRP A CH2   1 
ATOM   10108 N N     . ASP D 4 1140 ? 122.743 149.945 98.726  1.00 50.26  ? 1137 ASP A N     1 
ATOM   10109 C CA    . ASP D 4 1140 ? 123.213 150.553 97.479  1.00 50.26  ? 1137 ASP A CA    1 
ATOM   10110 C C     . ASP D 4 1140 ? 124.644 151.038 97.691  1.00 50.26  ? 1137 ASP A C     1 
ATOM   10111 O O     . ASP D 4 1140 ? 124.867 152.201 98.035  1.00 50.26  ? 1137 ASP A O     1 
ATOM   10112 C CB    . ASP D 4 1140 ? 122.293 151.691 97.045  1.00 50.26  ? 1137 ASP A CB    1 
ATOM   10113 C CG    . ASP D 4 1140 ? 121.205 151.232 96.095  1.00 50.26  ? 1137 ASP A CG    1 
ATOM   10114 O OD1   . ASP D 4 1140 ? 121.513 150.464 95.160  1.00 50.26  ? 1137 ASP A OD1   1 
ATOM   10115 O OD2   . ASP D 4 1140 ? 120.040 151.640 96.282  1.00 50.26  ? 1137 ASP A OD2   1 
ATOM   10116 N N     . ILE D 4 1141 ? 125.612 150.146 97.475  1.00 50.26  ? 1138 ILE A N     1 
ATOM   10117 C CA    . ILE D 4 1141 ? 127.015 150.515 97.613  1.00 50.26  ? 1138 ILE A CA    1 
ATOM   10118 C C     . ILE D 4 1141 ? 127.390 151.502 96.518  1.00 50.26  ? 1138 ILE A C     1 
ATOM   10119 O O     . ILE D 4 1141 ? 127.032 151.325 95.346  1.00 50.26  ? 1138 ILE A O     1 
ATOM   10120 C CB    . ILE D 4 1141 ? 127.909 149.265 97.567  1.00 50.26  ? 1138 ILE A CB    1 
ATOM   10121 C CG1   . ILE D 4 1141 ? 127.331 148.161 98.453  1.00 50.26  ? 1138 ILE A CG1   1 
ATOM   10122 C CG2   . ILE D 4 1141 ? 129.319 149.606 98.007  1.00 50.26  ? 1138 ILE A CG2   1 
ATOM   10123 C CD1   . ILE D 4 1141 ? 127.150 148.568 99.897  1.00 50.26  ? 1138 ILE A CD1   1 
ATOM   10124 N N     . VAL D 4 1142 ? 128.117 152.551 96.893  1.00 50.26  ? 1139 VAL A N     1 
ATOM   10125 C CA    . VAL D 4 1142 ? 128.421 153.663 96.001  1.00 50.26  ? 1139 VAL A CA    1 
ATOM   10126 C C     . VAL D 4 1142 ? 129.931 153.822 95.907  1.00 50.26  ? 1139 VAL A C     1 
ATOM   10127 O O     . VAL D 4 1142 ? 130.624 153.827 96.931  1.00 50.26  ? 1139 VAL A O     1 
ATOM   10128 C CB    . VAL D 4 1142 ? 127.768 154.969 96.488  1.00 50.26  ? 1139 VAL A CB    1 
ATOM   10129 C CG1   . VAL D 4 1142 ? 128.172 156.132 95.599  1.00 50.26  ? 1139 VAL A CG1   1 
ATOM   10130 C CG2   . VAL D 4 1142 ? 126.258 154.820 96.523  1.00 50.26  ? 1139 VAL A CG2   1 
ATOM   10131 N N     . PHE D 4 1143 ? 130.438 153.949 94.682  1.00 50.26  ? 1140 PHE A N     1 
ATOM   10132 C CA    . PHE D 4 1143 ? 131.844 154.262 94.439  1.00 50.26  ? 1140 PHE A CA    1 
ATOM   10133 C C     . PHE D 4 1143 ? 131.928 155.767 94.222  1.00 50.26  ? 1140 PHE A C     1 
ATOM   10134 O O     . PHE D 4 1143 ? 131.602 156.265 93.142  1.00 50.26  ? 1140 PHE A O     1 
ATOM   10135 C CB    . PHE D 4 1143 ? 132.393 153.509 93.231  1.00 50.26  ? 1140 PHE A CB    1 
ATOM   10136 C CG    . PHE D 4 1143 ? 132.430 152.018 93.400  1.00 50.26  ? 1140 PHE A CG    1 
ATOM   10137 C CD1   . PHE D 4 1143 ? 132.211 151.432 94.629  1.00 50.26  ? 1140 PHE A CD1   1 
ATOM   10138 C CD2   . PHE D 4 1143 ? 132.711 151.202 92.321  1.00 50.26  ? 1140 PHE A CD2   1 
ATOM   10139 C CE1   . PHE D 4 1143 ? 132.244 150.063 94.768  1.00 50.26  ? 1140 PHE A CE1   1 
ATOM   10140 C CE2   . PHE D 4 1143 ? 132.752 149.833 92.460  1.00 50.26  ? 1140 PHE A CE2   1 
ATOM   10141 C CZ    . PHE D 4 1143 ? 132.521 149.264 93.685  1.00 50.26  ? 1140 PHE A CZ    1 
ATOM   10142 N N     . GLU D 4 1144 ? 132.358 156.493 95.249  1.00 50.26  ? 1141 GLU A N     1 
ATOM   10143 C CA    . GLU D 4 1144 ? 132.428 157.945 95.151  1.00 50.26  ? 1141 GLU A CA    1 
ATOM   10144 C C     . GLU D 4 1144 ? 133.381 158.369 94.043  1.00 50.26  ? 1141 GLU A C     1 
ATOM   10145 O O     . GLU D 4 1144 ? 134.493 157.848 93.924  1.00 50.26  ? 1141 GLU A O     1 
ATOM   10146 C CB    . GLU D 4 1144 ? 132.882 158.548 96.479  1.00 50.26  ? 1141 GLU A CB    1 
ATOM   10147 C CG    . GLU D 4 1144 ? 132.110 158.070 97.689  1.00 50.26  ? 1141 GLU A CG    1 
ATOM   10148 C CD    . GLU D 4 1144 ? 130.977 159.006 98.051  1.00 50.26  ? 1141 GLU A CD    1 
ATOM   10149 O OE1   . GLU D 4 1144 ? 130.419 159.650 97.139  1.00 50.26  ? 1141 GLU A OE1   1 
ATOM   10150 O OE2   . GLU D 4 1144 ? 130.657 159.112 99.251  1.00 50.26  ? 1141 GLU A OE2   1 
ATOM   10151 N N     . LYS D 4 1145 ? 132.937 159.317 93.222  1.00 50.26  ? 1142 LYS A N     1 
ATOM   10152 C CA    . LYS D 4 1145 ? 133.834 159.928 92.253  1.00 50.26  ? 1142 LYS A CA    1 
ATOM   10153 C C     . LYS D 4 1145 ? 134.910 160.705 92.995  1.00 50.26  ? 1142 LYS A C     1 
ATOM   10154 O O     . LYS D 4 1145 ? 134.611 161.495 93.895  1.00 50.26  ? 1142 LYS A O     1 
ATOM   10155 C CB    . LYS D 4 1145 ? 133.066 160.845 91.304  1.00 50.26  ? 1142 LYS A CB    1 
ATOM   10156 C CG    . LYS D 4 1145 ? 133.807 161.144 90.011  1.00 50.26  ? 1142 LYS A CG    1 
ATOM   10157 C CD    . LYS D 4 1145 ? 132.985 162.025 89.086  1.00 50.26  ? 1142 LYS A CD    1 
ATOM   10158 C CE    . LYS D 4 1145 ? 133.319 163.494 89.280  1.00 50.26  ? 1142 LYS A CE    1 
ATOM   10159 N NZ    . LYS D 4 1145 ? 134.667 163.831 88.747  1.00 50.26  ? 1142 LYS A NZ    1 
ATOM   10160 N N     . ASN D 4 1146 ? 136.165 160.484 92.617  1.00 50.26  ? 1143 ASN A N     1 
ATOM   10161 C CA    . ASN D 4 1146 ? 137.282 161.008 93.390  1.00 50.26  ? 1143 ASN A CA    1 
ATOM   10162 C C     . ASN D 4 1146 ? 137.442 162.509 93.194  1.00 50.26  ? 1143 ASN A C     1 
ATOM   10163 O O     . ASN D 4 1146 ? 138.417 162.966 92.589  1.00 50.26  ? 1143 ASN A O     1 
ATOM   10164 C CB    . ASN D 4 1146 ? 138.566 160.269 93.019  1.00 50.26  ? 1143 ASN A CB    1 
ATOM   10165 C CG    . ASN D 4 1146 ? 138.425 158.768 93.159  1.00 50.26  ? 1143 ASN A CG    1 
ATOM   10166 O OD1   . ASN D 4 1146 ? 138.752 158.014 92.246  1.00 50.26  ? 1143 ASN A OD1   1 
ATOM   10167 N ND2   . ASN D 4 1146 ? 137.931 158.327 94.308  1.00 50.26  ? 1143 ASN A ND2   1 
ATOM   10168 N N     . GLU D 4 1147 ? 136.487 163.277 93.707  1.00 50.26  ? 1144 GLU A N     1 
ATOM   10169 C CA    . GLU D 4 1147 ? 136.568 164.728 93.711  1.00 50.26  ? 1144 GLU A CA    1 
ATOM   10170 C C     . GLU D 4 1147 ? 137.242 165.206 94.990  1.00 50.26  ? 1144 GLU A C     1 
ATOM   10171 O O     . GLU D 4 1147 ? 137.204 164.534 96.024  1.00 50.26  ? 1144 GLU A O     1 
ATOM   10172 C CB    . GLU D 4 1147 ? 135.177 165.351 93.593  1.00 50.26  ? 1144 GLU A CB    1 
ATOM   10173 C CG    . GLU D 4 1147 ? 134.537 165.199 92.226  1.00 50.26  ? 1144 GLU A CG    1 
ATOM   10174 C CD    . GLU D 4 1147 ? 135.301 165.924 91.136  1.00 50.26  ? 1144 GLU A CD    1 
ATOM   10175 O OE1   . GLU D 4 1147 ? 136.207 165.311 90.533  1.00 50.26  ? 1144 GLU A OE1   1 
ATOM   10176 O OE2   . GLU D 4 1147 ? 134.996 167.108 90.882  1.00 50.26  ? 1144 GLU A OE2   1 
ATOM   10177 N N     . THR D 4 1148 ? 137.862 166.379 94.911  1.00 53.80  ? 1145 THR A N     1 
ATOM   10178 C CA    . THR D 4 1148 ? 138.557 166.964 96.055  1.00 53.80  ? 1145 THR A CA    1 
ATOM   10179 C C     . THR D 4 1148 ? 137.552 167.754 96.890  1.00 53.80  ? 1145 THR A C     1 
ATOM   10180 O O     . THR D 4 1148 ? 137.152 168.865 96.531  1.00 53.80  ? 1145 THR A O     1 
ATOM   10181 C CB    . THR D 4 1148 ? 139.737 167.815 95.591  1.00 53.80  ? 1145 THR A CB    1 
ATOM   10182 O OG1   . THR D 4 1148 ? 140.328 168.485 96.713  1.00 53.80  ? 1145 THR A OG1   1 
ATOM   10183 C CG2   . THR D 4 1148 ? 139.332 168.820 94.510  1.00 53.80  ? 1145 THR A CG2   1 
ATOM   10184 N N     . GLN D 4 1149 ? 137.126 167.167 98.004  1.00 54.61  ? 1146 GLN A N     1 
ATOM   10185 C CA    . GLN D 4 1149 ? 136.211 167.839 98.910  1.00 54.61  ? 1146 GLN A CA    1 
ATOM   10186 C C     . GLN D 4 1149 ? 136.984 168.678 99.922  1.00 54.61  ? 1146 GLN A C     1 
ATOM   10187 O O     . GLN D 4 1149 ? 138.180 168.480 100.151 1.00 54.61  ? 1146 GLN A O     1 
ATOM   10188 C CB    . GLN D 4 1149 ? 135.329 166.825 99.638  1.00 54.61  ? 1146 GLN A CB    1 
ATOM   10189 C CG    . GLN D 4 1149 ? 134.663 165.808 98.729  1.00 54.61  ? 1146 GLN A CG    1 
ATOM   10190 C CD    . GLN D 4 1149 ? 133.779 166.453 97.684  1.00 54.61  ? 1146 GLN A CD    1 
ATOM   10191 O OE1   . GLN D 4 1149 ? 133.959 166.240 96.486  1.00 54.61  ? 1146 GLN A OE1   1 
ATOM   10192 N NE2   . GLN D 4 1149 ? 132.819 167.251 98.133  1.00 54.61  ? 1146 GLN A NE2   1 
ATOM   10193 N N     . PHE D 4 1150 ? 136.281 169.626 100.533 1.00 55.83  ? 1147 PHE A N     1 
ATOM   10194 C CA    . PHE D 4 1150 ? 136.861 170.519 101.525 1.00 55.83  ? 1147 PHE A CA    1 
ATOM   10195 C C     . PHE D 4 1150 ? 136.072 170.431 102.822 1.00 55.83  ? 1147 PHE A C     1 
ATOM   10196 O O     . PHE D 4 1150 ? 134.837 170.421 102.811 1.00 55.83  ? 1147 PHE A O     1 
ATOM   10197 C CB    . PHE D 4 1150 ? 136.885 171.964 101.019 1.00 55.83  ? 1147 PHE A CB    1 
ATOM   10198 C CG    . PHE D 4 1150 ? 137.518 172.120 99.668  1.00 55.83  ? 1147 PHE A CG    1 
ATOM   10199 C CD1   . PHE D 4 1150 ? 138.890 172.265 99.544  1.00 55.83  ? 1147 PHE A CD1   1 
ATOM   10200 C CD2   . PHE D 4 1150 ? 136.743 172.122 98.521  1.00 55.83  ? 1147 PHE A CD2   1 
ATOM   10201 C CE1   . PHE D 4 1150 ? 139.476 172.408 98.301  1.00 55.83  ? 1147 PHE A CE1   1 
ATOM   10202 C CE2   . PHE D 4 1150 ? 137.324 172.264 97.275  1.00 55.83  ? 1147 PHE A CE2   1 
ATOM   10203 C CZ    . PHE D 4 1150 ? 138.692 172.408 97.166  1.00 55.83  ? 1147 PHE A CZ    1 
ATOM   10204 N N     . ASP D 4 1151 ? 136.791 170.368 103.938 1.00 57.02  ? 1148 ASP A N     1 
ATOM   10205 C CA    . ASP D 4 1151 ? 136.177 170.269 105.251 1.00 57.02  ? 1148 ASP A CA    1 
ATOM   10206 C C     . ASP D 4 1151 ? 135.924 171.668 105.810 1.00 57.02  ? 1148 ASP A C     1 
ATOM   10207 O O     . ASP D 4 1151 ? 136.042 172.674 105.105 1.00 57.02  ? 1148 ASP A O     1 
ATOM   10208 C CB    . ASP D 4 1151 ? 137.057 169.436 106.181 1.00 57.02  ? 1148 ASP A CB    1 
ATOM   10209 C CG    . ASP D 4 1151 ? 138.430 170.042 106.378 1.00 57.02  ? 1148 ASP A CG    1 
ATOM   10210 O OD1   . ASP D 4 1151 ? 138.832 170.889 105.554 1.00 57.02  ? 1148 ASP A OD1   1 
ATOM   10211 O OD2   . ASP D 4 1151 ? 139.108 169.673 107.360 1.00 57.02  ? 1148 ASP A OD2   1 
ATOM   10212 N N     . ALA D 4 1152 ? 135.566 171.741 107.094 1.00 60.69  ? 1149 ALA A N     1 
ATOM   10213 C CA    . ALA D 4 1152 ? 135.337 173.035 107.727 1.00 60.69  ? 1149 ALA A CA    1 
ATOM   10214 C C     . ALA D 4 1152 ? 136.612 173.870 107.752 1.00 60.69  ? 1149 ALA A C     1 
ATOM   10215 O O     . ALA D 4 1152 ? 136.575 175.081 107.507 1.00 60.69  ? 1149 ALA A O     1 
ATOM   10216 C CB    . ALA D 4 1152 ? 134.795 172.838 109.142 1.00 60.69  ? 1149 ALA A CB    1 
ATOM   10217 N N     . LYS D 4 1153 ? 137.750 173.239 108.046 1.00 65.38  ? 1150 LYS A N     1 
ATOM   10218 C CA    . LYS D 4 1153 ? 139.027 173.940 108.033 1.00 65.38  ? 1150 LYS A CA    1 
ATOM   10219 C C     . LYS D 4 1153 ? 139.495 174.288 106.627 1.00 65.38  ? 1150 LYS A C     1 
ATOM   10220 O O     . LYS D 4 1153 ? 140.452 175.057 106.486 1.00 65.38  ? 1150 LYS A O     1 
ATOM   10221 C CB    . LYS D 4 1153 ? 140.095 173.101 108.736 1.00 65.39  ? 1150 LYS A CB    1 
ATOM   10222 C CG    . LYS D 4 1153 ? 140.181 173.333 110.236 1.00 65.39  ? 1150 LYS A CG    1 
ATOM   10223 C CD    . LYS D 4 1153 ? 141.446 172.726 110.829 1.00 65.39  ? 1150 LYS A CD    1 
ATOM   10224 C CE    . LYS D 4 1153 ? 142.616 172.798 109.859 1.00 65.39  ? 1150 LYS A CE    1 
ATOM   10225 N NZ    . LYS D 4 1153 ? 143.922 172.593 110.544 1.00 65.39  ? 1150 LYS A NZ    1 
ATOM   10226 N N     . GLY D 4 1154 ? 138.854 173.747 105.594 1.00 62.90  ? 1151 GLY A N     1 
ATOM   10227 C CA    . GLY D 4 1154 ? 139.241 174.012 104.227 1.00 62.90  ? 1151 GLY A CA    1 
ATOM   10228 C C     . GLY D 4 1154 ? 140.315 173.104 103.671 1.00 62.90  ? 1151 GLY A C     1 
ATOM   10229 O O     . GLY D 4 1154 ? 140.669 173.243 102.493 1.00 62.90  ? 1151 GLY A O     1 
ATOM   10230 N N     . THR D 4 1155 ? 140.844 172.187 104.470 1.00 63.24  ? 1152 THR A N     1 
ATOM   10231 C CA    . THR D 4 1155 ? 141.881 171.286 103.982 1.00 63.24  ? 1152 THR A CA    1 
ATOM   10232 C C     . THR D 4 1155 ? 141.285 170.315 102.969 1.00 63.24  ? 1152 THR A C     1 
ATOM   10233 O O     . THR D 4 1155 ? 140.310 169.622 103.280 1.00 63.24  ? 1152 THR A O     1 
ATOM   10234 C CB    . THR D 4 1155 ? 142.515 170.518 105.139 1.00 63.24  ? 1152 THR A CB    1 
ATOM   10235 O OG1   . THR D 4 1155 ? 141.492 169.864 105.899 1.00 63.24  ? 1152 THR A OG1   1 
ATOM   10236 C CG2   . THR D 4 1155 ? 143.285 171.464 106.046 1.00 63.24  ? 1152 THR A CG2   1 
ATOM   10237 N N     . PRO D 4 1156 ? 141.831 170.237 101.758 1.00 59.04  ? 1153 PRO A N     1 
ATOM   10238 C CA    . PRO D 4 1156 ? 141.252 169.347 100.748 1.00 59.04  ? 1153 PRO A CA    1 
ATOM   10239 C C     . PRO D 4 1156 ? 141.538 167.885 101.052 1.00 59.04  ? 1153 PRO A C     1 
ATOM   10240 O O     . PRO D 4 1156 ? 142.516 167.541 101.718 1.00 59.04  ? 1153 PRO A O     1 
ATOM   10241 C CB    . PRO D 4 1156 ? 141.937 169.785 99.445  1.00 59.04  ? 1153 PRO A CB    1 
ATOM   10242 C CG    . PRO D 4 1156 ? 142.754 171.010 99.792  1.00 59.04  ? 1153 PRO A CG    1 
ATOM   10243 C CD    . PRO D 4 1156 ? 143.016 170.945 101.255 1.00 59.04  ? 1153 PRO A CD    1 
ATOM   10244 N N     . PHE D 4 1157 ? 140.658 167.022 100.549 1.00 50.26  ? 1154 PHE A N     1 
ATOM   10245 C CA    . PHE D 4 1157 ? 140.849 165.583 100.633 1.00 50.26  ? 1154 PHE A CA    1 
ATOM   10246 C C     . PHE D 4 1157 ? 140.086 164.926 99.494  1.00 50.26  ? 1154 PHE A C     1 
ATOM   10247 O O     . PHE D 4 1157 ? 139.031 165.409 99.076  1.00 50.26  ? 1154 PHE A O     1 
ATOM   10248 C CB    . PHE D 4 1157 ? 140.397 165.023 101.990 1.00 50.26  ? 1154 PHE A CB    1 
ATOM   10249 C CG    . PHE D 4 1157 ? 138.932 165.205 102.273 1.00 50.26  ? 1154 PHE A CG    1 
ATOM   10250 C CD1   . PHE D 4 1157 ? 138.007 164.258 101.867 1.00 50.26  ? 1154 PHE A CD1   1 
ATOM   10251 C CD2   . PHE D 4 1157 ? 138.482 166.318 102.960 1.00 50.26  ? 1154 PHE A CD2   1 
ATOM   10252 C CE1   . PHE D 4 1157 ? 136.663 164.424 102.131 1.00 50.26  ? 1154 PHE A CE1   1 
ATOM   10253 C CE2   . PHE D 4 1157 ? 137.138 166.488 103.228 1.00 50.26  ? 1154 PHE A CE2   1 
ATOM   10254 C CZ    . PHE D 4 1157 ? 136.228 165.539 102.813 1.00 50.26  ? 1154 PHE A CZ    1 
ATOM   10255 N N     . ILE D 4 1158 ? 140.629 163.819 98.997  1.00 50.26  ? 1155 ILE A N     1 
ATOM   10256 C CA    . ILE D 4 1158 ? 140.037 163.123 97.860  1.00 50.26  ? 1155 ILE A CA    1 
ATOM   10257 C C     . ILE D 4 1158 ? 138.892 162.251 98.358  1.00 50.26  ? 1155 ILE A C     1 
ATOM   10258 O O     . ILE D 4 1158 ? 139.083 161.392 99.225  1.00 50.26  ? 1155 ILE A O     1 
ATOM   10259 C CB    . ILE D 4 1158 ? 141.085 162.287 97.113  1.00 50.26  ? 1155 ILE A CB    1 
ATOM   10260 C CG1   . ILE D 4 1158 ? 142.301 163.144 96.758  1.00 50.26  ? 1155 ILE A CG1   1 
ATOM   10261 C CG2   . ILE D 4 1158 ? 140.482 161.690 95.855  1.00 50.26  ? 1155 ILE A CG2   1 
ATOM   10262 C CD1   . ILE D 4 1158 ? 143.509 162.886 97.633  1.00 50.26  ? 1155 ILE A CD1   1 
ATOM   10263 N N     . ALA D 4 1159 ? 137.700 162.470 97.810  1.00 50.26  ? 1156 ALA A N     1 
ATOM   10264 C CA    . ALA D 4 1159 ? 136.539 161.686 98.203  1.00 50.26  ? 1156 ALA A CA    1 
ATOM   10265 C C     . ALA D 4 1159 ? 136.687 160.241 97.745  1.00 50.26  ? 1156 ALA A C     1 
ATOM   10266 O O     . ALA D 4 1159 ? 137.189 159.966 96.653  1.00 50.26  ? 1156 ALA A O     1 
ATOM   10267 C CB    . ALA D 4 1159 ? 135.265 162.293 97.618  1.00 50.26  ? 1156 ALA A CB    1 
ATOM   10268 N N     . GLY D 4 1160 ? 136.247 159.314 98.592  1.00 50.26  ? 1157 GLY A N     1 
ATOM   10269 C CA    . GLY D 4 1160 ? 136.318 157.907 98.263  1.00 50.26  ? 1157 GLY A CA    1 
ATOM   10270 C C     . GLY D 4 1160 ? 137.678 157.274 98.437  1.00 50.26  ? 1157 GLY A C     1 
ATOM   10271 O O     . GLY D 4 1160 ? 137.848 156.106 98.070  1.00 50.26  ? 1157 GLY A O     1 
ATOM   10272 N N     . LYS D 4 1161 ? 138.650 158.003 98.978  1.00 50.26  ? 1158 LYS A N     1 
ATOM   10273 C CA    . LYS D 4 1161 ? 139.986 157.455 99.165  1.00 50.26  ? 1158 LYS A CA    1 
ATOM   10274 C C     . LYS D 4 1161 ? 139.952 156.284 100.138 1.00 50.26  ? 1158 LYS A C     1 
ATOM   10275 O O     . LYS D 4 1161 ? 139.256 156.319 101.155 1.00 50.26  ? 1158 LYS A O     1 
ATOM   10276 C CB    . LYS D 4 1161 ? 140.932 158.541 99.679  1.00 50.26  ? 1158 LYS A CB    1 
ATOM   10277 C CG    . LYS D 4 1161 ? 142.401 158.161 99.661  1.00 50.26  ? 1158 LYS A CG    1 
ATOM   10278 C CD    . LYS D 4 1161 ? 143.232 159.200 100.395 1.00 50.26  ? 1158 LYS A CD    1 
ATOM   10279 C CE    . LYS D 4 1161 ? 144.704 159.086 100.045 1.00 50.26  ? 1158 LYS A CE    1 
ATOM   10280 N NZ    . LYS D 4 1161 ? 145.331 157.892 100.669 1.00 50.26  ? 1158 LYS A NZ    1 
ATOM   10281 N N     . ARG D 4 1162 ? 140.710 155.240 99.817  1.00 50.26  ? 1159 ARG A N     1 
ATOM   10282 C CA    . ARG D 4 1162 ? 140.778 154.040 100.637 1.00 50.26  ? 1159 ARG A CA    1 
ATOM   10283 C C     . ARG D 4 1162 ? 142.231 153.675 100.892 1.00 50.26  ? 1159 ARG A C     1 
ATOM   10284 O O     . ARG D 4 1162 ? 143.082 153.825 100.011 1.00 50.26  ? 1159 ARG A O     1 
ATOM   10285 C CB    . ARG D 4 1162 ? 140.057 152.866 99.969  1.00 50.26  ? 1159 ARG A CB    1 
ATOM   10286 C CG    . ARG D 4 1162 ? 138.547 152.999 99.948  1.00 50.26  ? 1159 ARG A CG    1 
ATOM   10287 C CD    . ARG D 4 1162 ? 137.977 152.974 101.353 1.00 50.26  ? 1159 ARG A CD    1 
ATOM   10288 N NE    . ARG D 4 1162 ? 136.537 152.756 101.353 1.00 50.26  ? 1159 ARG A NE    1 
ATOM   10289 C CZ    . ARG D 4 1162 ? 135.638 153.688 101.071 1.00 50.26  ? 1159 ARG A CZ    1 
ATOM   10290 N NH1   . ARG D 4 1162 ? 135.996 154.924 100.767 1.00 50.26  ? 1159 ARG A NH1   1 
ATOM   10291 N NH2   . ARG D 4 1162 ? 134.347 153.372 101.095 1.00 50.26  ? 1159 ARG A NH2   1 
ATOM   10292 N N     . ILE D 4 1163 ? 142.506 153.197 102.100 1.00 50.26  ? 1160 ILE A N     1 
ATOM   10293 C CA    . ILE D 4 1163 ? 143.828 152.722 102.488 1.00 50.26  ? 1160 ILE A CA    1 
ATOM   10294 C C     . ILE D 4 1163 ? 143.742 151.213 102.657 1.00 50.26  ? 1160 ILE A C     1 
ATOM   10295 O O     . ILE D 4 1163 ? 142.988 150.719 103.505 1.00 50.26  ? 1160 ILE A O     1 
ATOM   10296 C CB    . ILE D 4 1163 ? 144.318 153.395 103.777 1.00 50.26  ? 1160 ILE A CB    1 
ATOM   10297 C CG1   . ILE D 4 1163 ? 144.543 154.889 103.546 1.00 50.26  ? 1160 ILE A CG1   1 
ATOM   10298 C CG2   . ILE D 4 1163 ? 145.588 152.731 104.272 1.00 50.26  ? 1160 ILE A CG2   1 
ATOM   10299 C CD1   . ILE D 4 1163 ? 145.657 155.187 102.572 1.00 50.26  ? 1160 ILE A CD1   1 
ATOM   10300 N N     . VAL D 4 1164 ? 144.511 150.480 101.859 1.00 55.14  ? 1161 VAL A N     1 
ATOM   10301 C CA    . VAL D 4 1164 ? 144.471 149.021 101.897 1.00 55.14  ? 1161 VAL A CA    1 
ATOM   10302 C C     . VAL D 4 1164 ? 145.877 148.473 102.112 1.00 55.14  ? 1161 VAL A C     1 
ATOM   10303 O O     . VAL D 4 1164 ? 146.849 149.024 101.577 1.00 55.14  ? 1161 VAL A O     1 
ATOM   10304 C CB    . VAL D 4 1164 ? 143.849 148.449 100.614 1.00 55.14  ? 1161 VAL A CB    1 
ATOM   10305 C CG1   . VAL D 4 1164 ? 142.370 148.770 100.561 1.00 55.14  ? 1161 VAL A CG1   1 
ATOM   10306 C CG2   . VAL D 4 1164 ? 144.558 148.999 99.395  1.00 55.14  ? 1161 VAL A CG2   1 
ATOM   10307 N N     . PRO D 4 1165 ? 146.034 147.407 102.895 1.00 76.20  ? 1162 PRO A N     1 
ATOM   10308 C CA    . PRO D 4 1165 ? 147.354 146.785 103.082 1.00 76.20  ? 1162 PRO A CA    1 
ATOM   10309 C C     . PRO D 4 1165 ? 147.632 145.577 102.195 1.00 76.20  ? 1162 PRO A C     1 
ATOM   10310 O O     . PRO D 4 1165 ? 148.744 145.041 102.258 1.00 76.20  ? 1162 PRO A O     1 
ATOM   10311 C CB    . PRO D 4 1165 ? 147.287 146.359 104.551 1.00 76.20  ? 1162 PRO A CB    1 
ATOM   10312 C CG    . PRO D 4 1165 ? 145.846 145.988 104.751 1.00 76.20  ? 1162 PRO A CG    1 
ATOM   10313 C CD    . PRO D 4 1165 ? 145.024 146.834 103.800 1.00 76.20  ? 1162 PRO A CD    1 
ATOM   10314 N N     . VAL D 4 1166 ? 146.672 145.155 101.375 1.00 94.55  ? 1163 VAL A N     1 
ATOM   10315 C CA    . VAL D 4 1166 ? 146.844 143.951 100.572 1.00 94.55  ? 1163 VAL A CA    1 
ATOM   10316 C C     . VAL D 4 1166 ? 147.915 144.208 99.522  1.00 94.55  ? 1163 VAL A C     1 
ATOM   10317 O O     . VAL D 4 1166 ? 147.725 145.009 98.600  1.00 94.55  ? 1163 VAL A O     1 
ATOM   10318 C CB    . VAL D 4 1166 ? 145.517 143.529 99.926  1.00 94.55  ? 1163 VAL A CB    1 
ATOM   10319 C CG1   . VAL D 4 1166 ? 145.734 142.402 98.926  1.00 94.55  ? 1163 VAL A CG1   1 
ATOM   10320 C CG2   . VAL D 4 1166 ? 144.515 143.111 100.988 1.00 94.55  ? 1163 VAL A CG2   1 
ATOM   10321 N N     . ILE D 4 1167 ? 149.051 143.529 99.663  1.00 102.77 ? 1164 ILE A N     1 
ATOM   10322 C CA    . ILE D 4 1167 ? 150.126 143.597 98.680  1.00 102.77 ? 1164 ILE A CA    1 
ATOM   10323 C C     . ILE D 4 1167 ? 150.409 142.181 98.191  1.00 102.77 ? 1164 ILE A C     1 
ATOM   10324 O O     . ILE D 4 1167 ? 150.491 141.928 96.985  1.00 102.77 ? 1164 ILE A O     1 
ATOM   10325 C CB    . ILE D 4 1167 ? 151.393 144.248 99.269  1.00 102.77 ? 1164 ILE A CB    1 
ATOM   10326 C CG1   . ILE D 4 1167 ? 151.060 145.558 99.990  1.00 102.77 ? 1164 ILE A CG1   1 
ATOM   10327 C CG2   . ILE D 4 1167 ? 152.402 144.525 98.164  1.00 102.77 ? 1164 ILE A CG2   1 
ATOM   10328 C CD1   . ILE D 4 1167 ? 150.560 146.655 99.079  1.00 102.77 ? 1164 ILE A CD1   1 
ATOM   10329 N N     . GLU D 4 1168 ? 150.575 141.250 99.128  1.00 114.03 ? 1165 GLU A N     1 
ATOM   10330 C CA    . GLU D 4 1168 ? 150.796 139.846 98.819  1.00 114.03 ? 1165 GLU A CA    1 
ATOM   10331 C C     . GLU D 4 1168 ? 149.857 139.011 99.678  1.00 114.03 ? 1165 GLU A C     1 
ATOM   10332 O O     . GLU D 4 1168 ? 149.364 139.472 100.708 1.00 114.03 ? 1165 GLU A O     1 
ATOM   10333 C CB    . GLU D 4 1168 ? 152.266 139.447 99.044  1.00 114.03 ? 1165 GLU A CB    1 
ATOM   10334 C CG    . GLU D 4 1168 ? 152.649 138.040 98.595  1.00 114.03 ? 1165 GLU A CG    1 
ATOM   10335 C CD    . GLU D 4 1168 ? 152.351 137.784 97.125  1.00 114.03 ? 1165 GLU A CD    1 
ATOM   10336 O OE1   . GLU D 4 1168 ? 151.196 137.432 96.800  1.00 114.03 ? 1165 GLU A OE1   1 
ATOM   10337 O OE2   . GLU D 4 1168 ? 153.259 137.951 96.288  1.00 114.03 ? 1165 GLU A OE2   1 
ATOM   10338 N N     . ASN D 4 1169 ? 149.598 137.778 99.233  1.00 119.24 ? 1166 ASN A N     1 
ATOM   10339 C CA    . ASN D 4 1169 ? 148.611 136.930 99.900  1.00 119.24 ? 1166 ASN A CA    1 
ATOM   10340 C C     . ASN D 4 1169 ? 148.964 136.703 101.368 1.00 119.24 ? 1166 ASN A C     1 
ATOM   10341 O O     . ASN D 4 1169 ? 148.135 136.927 102.259 1.00 119.24 ? 1166 ASN A O     1 
ATOM   10342 C CB    . ASN D 4 1169 ? 148.492 135.597 99.158  1.00 119.24 ? 1166 ASN A CB    1 
ATOM   10343 C CG    . ASN D 4 1169 ? 149.846 134.986 98.828  1.00 119.24 ? 1166 ASN A CG    1 
ATOM   10344 O OD1   . ASN D 4 1169 ? 150.856 135.311 99.454  1.00 119.24 ? 1166 ASN A OD1   1 
ATOM   10345 N ND2   . ASN D 4 1169 ? 149.873 134.101 97.837  1.00 119.24 ? 1166 ASN A ND2   1 
ATOM   10346 N N     . HIS D 4 1170 ? 150.194 136.262 101.641 1.00 118.74 ? 1167 HIS A N     1 
ATOM   10347 C CA    . HIS D 4 1170 ? 150.607 136.018 103.020 1.00 118.74 ? 1167 HIS A CA    1 
ATOM   10348 C C     . HIS D 4 1170 ? 150.969 137.313 103.738 1.00 118.74 ? 1167 HIS A C     1 
ATOM   10349 O O     . HIS D 4 1170 ? 150.436 137.598 104.817 1.00 118.74 ? 1167 HIS A O     1 
ATOM   10350 C CB    . HIS D 4 1170 ? 151.788 135.045 103.049 1.00 118.74 ? 1167 HIS A CB    1 
ATOM   10351 C CG    . HIS D 4 1170 ? 151.385 133.602 103.061 1.00 118.74 ? 1167 HIS A CG    1 
ATOM   10352 N ND1   . HIS D 4 1170 ? 150.889 132.959 101.948 1.00 118.74 ? 1167 HIS A ND1   1 
ATOM   10353 C CD2   . HIS D 4 1170 ? 151.406 132.678 104.050 1.00 118.74 ? 1167 HIS A CD2   1 
ATOM   10354 C CE1   . HIS D 4 1170 ? 150.622 131.701 102.249 1.00 118.74 ? 1167 HIS A CE1   1 
ATOM   10355 N NE2   . HIS D 4 1170 ? 150.925 131.504 103.520 1.00 118.74 ? 1167 HIS A NE2   1 
ATOM   10356 N N     . ARG D 4 1171 ? 151.859 138.114 103.155 1.00 110.63 ? 1168 ARG A N     1 
ATOM   10357 C CA    . ARG D 4 1171 ? 152.266 139.382 103.760 1.00 110.63 ? 1168 ARG A CA    1 
ATOM   10358 C C     . ARG D 4 1171 ? 151.413 140.533 103.214 1.00 110.63 ? 1168 ARG A C     1 
ATOM   10359 O O     . ARG D 4 1171 ? 151.848 141.441 102.514 1.00 110.63 ? 1168 ARG A O     1 
ATOM   10360 C CB    . ARG D 4 1171 ? 153.779 139.570 103.609 1.00 110.63 ? 1168 ARG A CB    1 
ATOM   10361 C CG    . ARG D 4 1171 ? 154.418 139.574 102.208 1.00 110.63 ? 1168 ARG A CG    1 
ATOM   10362 C CD    . ARG D 4 1171 ? 154.506 140.903 101.477 1.00 110.63 ? 1168 ARG A CD    1 
ATOM   10363 N NE    . ARG D 4 1171 ? 155.271 140.752 100.245 1.00 110.63 ? 1168 ARG A NE    1 
ATOM   10364 C CZ    . ARG D 4 1171 ? 155.423 141.697 99.328  1.00 110.63 ? 1168 ARG A CZ    1 
ATOM   10365 N NH1   . ARG D 4 1171 ? 154.910 142.905 99.488  1.00 110.63 ? 1168 ARG A NH1   1 
ATOM   10366 N NH2   . ARG D 4 1171 ? 156.127 141.428 98.230  1.00 110.63 ? 1168 ARG A NH2   1 
ATOM   10367 N N     . PHE D 4 1172 ? 150.138 140.465 103.604 1.00 105.87 ? 1169 PHE A N     1 
ATOM   10368 C CA    . PHE D 4 1172 ? 149.110 141.438 103.263 1.00 105.87 ? 1169 PHE A CA    1 
ATOM   10369 C C     . PHE D 4 1172 ? 148.999 142.567 104.281 1.00 105.87 ? 1169 PHE A C     1 
ATOM   10370 O O     . PHE D 4 1172 ? 147.991 143.281 104.292 1.00 105.87 ? 1169 PHE A O     1 
ATOM   10371 C CB    . PHE D 4 1172 ? 147.761 140.730 103.107 1.00 105.87 ? 1169 PHE A CB    1 
ATOM   10372 C CG    . PHE D 4 1172 ? 147.144 140.310 104.412 1.00 105.87 ? 1169 PHE A CG    1 
ATOM   10373 C CD1   . PHE D 4 1172 ? 147.659 139.230 105.110 1.00 105.87 ? 1169 PHE A CD1   1 
ATOM   10374 C CD2   . PHE D 4 1172 ? 146.042 140.971 104.935 1.00 105.87 ? 1169 PHE A CD2   1 
ATOM   10375 C CE1   . PHE D 4 1172 ? 147.109 138.826 106.305 1.00 105.87 ? 1169 PHE A CE1   1 
ATOM   10376 C CE2   . PHE D 4 1172 ? 145.483 140.569 106.135 1.00 105.87 ? 1169 PHE A CE2   1 
ATOM   10377 C CZ    . PHE D 4 1172 ? 146.020 139.494 106.820 1.00 105.87 ? 1169 PHE A CZ    1 
ATOM   10378 N N     . THR D 4 1173 ? 150.008 142.738 105.143 1.00 96.12  ? 1170 THR A N     1 
ATOM   10379 C CA    . THR D 4 1173 ? 150.023 143.843 106.095 1.00 96.12  ? 1170 THR A CA    1 
ATOM   10380 C C     . THR D 4 1173 ? 151.402 144.505 106.125 1.00 96.12  ? 1170 THR A C     1 
ATOM   10381 O O     . THR D 4 1173 ? 151.712 145.249 107.064 1.00 96.12  ? 1170 THR A O     1 
ATOM   10382 C CB    . THR D 4 1173 ? 149.608 143.347 107.493 1.00 96.12  ? 1170 THR A CB    1 
ATOM   10383 O OG1   . THR D 4 1173 ? 148.470 142.488 107.366 1.00 96.12  ? 1170 THR A OG1   1 
ATOM   10384 C CG2   . THR D 4 1173 ? 149.199 144.511 108.394 1.00 96.12  ? 1170 THR A CG2   1 
ATOM   10385 N N     . GLY D 4 1174 ? 152.233 144.257 105.109 1.00 86.60  ? 1171 GLY A N     1 
ATOM   10386 C CA    . GLY D 4 1174 ? 153.578 144.811 105.108 1.00 86.60  ? 1171 GLY A CA    1 
ATOM   10387 C C     . GLY D 4 1174 ? 153.592 146.327 105.065 1.00 86.60  ? 1171 GLY A C     1 
ATOM   10388 O O     . GLY D 4 1174 ? 154.348 146.974 105.794 1.00 86.60  ? 1171 GLY A O     1 
ATOM   10389 N N     . ARG D 4 1175 ? 152.761 146.914 104.208 1.00 78.85  ? 1172 ARG A N     1 
ATOM   10390 C CA    . ARG D 4 1175 ? 152.704 148.363 104.091 1.00 78.85  ? 1172 ARG A CA    1 
ATOM   10391 C C     . ARG D 4 1175 ? 151.372 148.764 103.477 1.00 78.85  ? 1172 ARG A C     1 
ATOM   10392 O O     . ARG D 4 1175 ? 150.853 148.074 102.596 1.00 78.85  ? 1172 ARG A O     1 
ATOM   10393 C CB    . ARG D 4 1175 ? 153.866 148.905 103.249 1.00 78.85  ? 1172 ARG A CB    1 
ATOM   10394 C CG    . ARG D 4 1175 ? 154.173 148.089 102.009 1.00 78.85  ? 1172 ARG A CG    1 
ATOM   10395 C CD    . ARG D 4 1175 ? 154.737 148.969 100.907 1.00 78.85  ? 1172 ARG A CD    1 
ATOM   10396 N NE    . ARG D 4 1175 ? 154.828 148.263 99.635  1.00 78.85  ? 1172 ARG A NE    1 
ATOM   10397 C CZ    . ARG D 4 1175 ? 155.852 147.505 99.271  1.00 78.85  ? 1172 ARG A CZ    1 
ATOM   10398 N NH1   . ARG D 4 1175 ? 156.895 147.325 100.065 1.00 78.85  ? 1172 ARG A NH1   1 
ATOM   10399 N NH2   . ARG D 4 1175 ? 155.830 146.911 98.081  1.00 78.85  ? 1172 ARG A NH2   1 
ATOM   10400 N N     . TYR D 4 1176 ? 150.831 149.882 103.950 1.00 63.85  ? 1173 TYR A N     1 
ATOM   10401 C CA    . TYR D 4 1176 ? 149.564 150.388 103.447 1.00 63.85  ? 1173 TYR A CA    1 
ATOM   10402 C C     . TYR D 4 1176 ? 149.732 150.976 102.050 1.00 63.85  ? 1173 TYR A C     1 
ATOM   10403 O O     . TYR D 4 1176 ? 150.793 151.495 101.692 1.00 63.85  ? 1173 TYR A O     1 
ATOM   10404 C CB    . TYR D 4 1176 ? 149.004 151.442 104.398 1.00 63.85  ? 1173 TYR A CB    1 
ATOM   10405 C CG    . TYR D 4 1176 ? 148.538 150.875 105.718 1.00 63.85  ? 1173 TYR A CG    1 
ATOM   10406 C CD1   . TYR D 4 1176 ? 148.003 149.597 105.794 1.00 63.85  ? 1173 TYR A CD1   1 
ATOM   10407 C CD2   . TYR D 4 1176 ? 148.634 151.616 106.888 1.00 63.85  ? 1173 TYR A CD2   1 
ATOM   10408 C CE1   . TYR D 4 1176 ? 147.573 149.074 106.997 1.00 63.85  ? 1173 TYR A CE1   1 
ATOM   10409 C CE2   . TYR D 4 1176 ? 148.207 151.101 108.096 1.00 63.85  ? 1173 TYR A CE2   1 
ATOM   10410 C CZ    . TYR D 4 1176 ? 147.678 149.830 108.144 1.00 63.85  ? 1173 TYR A CZ    1 
ATOM   10411 O OH    . TYR D 4 1176 ? 147.252 149.313 109.345 1.00 63.85  ? 1173 TYR A OH    1 
ATOM   10412 N N     . ARG D 4 1177 ? 148.666 150.893 101.257 1.00 54.03  ? 1174 ARG A N     1 
ATOM   10413 C CA    . ARG D 4 1177 ? 148.674 151.372 99.883  1.00 54.03  ? 1174 ARG A CA    1 
ATOM   10414 C C     . ARG D 4 1177 ? 147.465 152.260 99.630  1.00 54.03  ? 1174 ARG A C     1 
ATOM   10415 O O     . ARG D 4 1177 ? 146.353 151.949 100.066 1.00 54.03  ? 1174 ARG A O     1 
ATOM   10416 C CB    . ARG D 4 1177 ? 148.679 150.206 98.891  1.00 54.03  ? 1174 ARG A CB    1 
ATOM   10417 C CG    . ARG D 4 1177 ? 148.929 150.623 97.456  1.00 54.03  ? 1174 ARG A CG    1 
ATOM   10418 C CD    . ARG D 4 1177 ? 149.063 149.416 96.545  1.00 54.03  ? 1174 ARG A CD    1 
ATOM   10419 N NE    . ARG D 4 1177 ? 147.768 148.836 96.211  1.00 54.03  ? 1174 ARG A NE    1 
ATOM   10420 C CZ    . ARG D 4 1177 ? 146.912 149.357 95.342  1.00 54.03  ? 1174 ARG A CZ    1 
ATOM   10421 N NH1   . ARG D 4 1177 ? 147.180 150.479 94.695  1.00 54.03  ? 1174 ARG A NH1   1 
ATOM   10422 N NH2   . ARG D 4 1177 ? 145.760 148.734 95.115  1.00 54.03  ? 1174 ARG A NH2   1 
ATOM   10423 N N     . ASP D 4 1178 ? 147.691 153.363 98.924  1.00 50.26  ? 1175 ASP A N     1 
ATOM   10424 C CA    . ASP D 4 1178 ? 146.609 154.261 98.552  1.00 50.26  ? 1175 ASP A CA    1 
ATOM   10425 C C     . ASP D 4 1178 ? 145.745 153.627 97.466  1.00 50.26  ? 1175 ASP A C     1 
ATOM   10426 O O     . ASP D 4 1178 ? 146.224 152.851 96.634  1.00 50.26  ? 1175 ASP A O     1 
ATOM   10427 C CB    . ASP D 4 1178 ? 147.179 155.595 98.070  1.00 50.26  ? 1175 ASP A CB    1 
ATOM   10428 C CG    . ASP D 4 1178 ? 146.115 156.651 97.865  1.00 50.26  ? 1175 ASP A CG    1 
ATOM   10429 O OD1   . ASP D 4 1178 ? 144.919 156.352 98.065  1.00 50.26  ? 1175 ASP A OD1   1 
ATOM   10430 O OD2   . ASP D 4 1178 ? 146.479 157.789 97.504  1.00 50.26  ? 1175 ASP A OD2   1 
ATOM   10431 N N     . LEU D 4 1179 ? 144.457 153.967 97.475  1.00 50.26  ? 1176 LEU A N     1 
ATOM   10432 C CA    . LEU D 4 1179 ? 143.506 153.344 96.562  1.00 50.26  ? 1176 LEU A CA    1 
ATOM   10433 C C     . LEU D 4 1179 ? 142.266 154.218 96.442  1.00 50.26  ? 1176 LEU A C     1 
ATOM   10434 O O     . LEU D 4 1179 ? 141.696 154.631 97.456  1.00 50.26  ? 1176 LEU A O     1 
ATOM   10435 C CB    . LEU D 4 1179 ? 143.146 151.933 97.054  1.00 50.26  ? 1176 LEU A CB    1 
ATOM   10436 C CG    . LEU D 4 1179 ? 142.298 151.007 96.182  1.00 50.26  ? 1176 LEU A CG    1 
ATOM   10437 C CD1   . LEU D 4 1179 ? 142.601 149.557 96.491  1.00 50.26  ? 1176 LEU A CD1   1 
ATOM   10438 C CD2   . LEU D 4 1179 ? 140.826 151.268 96.421  1.00 50.26  ? 1176 LEU A CD2   1 
ATOM   10439 N N     . TYR D 4 1180 ? 141.849 154.487 95.201  1.00 50.26  ? 1177 TYR A N     1 
ATOM   10440 C CA    . TYR D 4 1180 ? 140.633 155.242 94.896  1.00 50.26  ? 1177 TYR A CA    1 
ATOM   10441 C C     . TYR D 4 1180 ? 139.758 154.380 93.995  1.00 50.26  ? 1177 TYR A C     1 
ATOM   10442 O O     . TYR D 4 1180 ? 139.874 154.457 92.763  1.00 50.26  ? 1177 TYR A O     1 
ATOM   10443 C CB    . TYR D 4 1180 ? 140.953 156.565 94.203  1.00 50.26  ? 1177 TYR A CB    1 
ATOM   10444 C CG    . TYR D 4 1180 ? 142.089 157.361 94.802  1.00 50.26  ? 1177 TYR A CG    1 
ATOM   10445 C CD1   . TYR D 4 1180 ? 143.403 157.113 94.439  1.00 50.26  ? 1177 TYR A CD1   1 
ATOM   10446 C CD2   . TYR D 4 1180 ? 141.842 158.384 95.708  1.00 50.26  ? 1177 TYR A CD2   1 
ATOM   10447 C CE1   . TYR D 4 1180 ? 144.441 157.845 94.973  1.00 50.26  ? 1177 TYR A CE1   1 
ATOM   10448 C CE2   . TYR D 4 1180 ? 142.875 159.122 96.246  1.00 50.26  ? 1177 TYR A CE2   1 
ATOM   10449 C CZ    . TYR D 4 1180 ? 144.170 158.848 95.875  1.00 50.26  ? 1177 TYR A CZ    1 
ATOM   10450 O OH    . TYR D 4 1180 ? 145.203 159.580 96.410  1.00 50.26  ? 1177 TYR A OH    1 
ATOM   10451 N N     . PRO D 4 1181 ? 138.814 153.614 94.555  1.00 50.26  ? 1178 PRO A N     1 
ATOM   10452 C CA    . PRO D 4 1181 ? 138.215 152.497 93.798  1.00 50.26  ? 1178 PRO A CA    1 
ATOM   10453 C C     . PRO D 4 1181 ? 137.650 152.877 92.440  1.00 50.26  ? 1178 PRO A C     1 
ATOM   10454 O O     . PRO D 4 1181 ? 137.764 152.089 91.491  1.00 50.26  ? 1178 PRO A O     1 
ATOM   10455 C CB    . PRO D 4 1181 ? 137.113 151.991 94.737  1.00 50.26  ? 1178 PRO A CB    1 
ATOM   10456 C CG    . PRO D 4 1181 ? 137.498 152.480 96.088  1.00 50.26  ? 1178 PRO A CG    1 
ATOM   10457 C CD    . PRO D 4 1181 ? 138.194 153.783 95.877  1.00 50.26  ? 1178 PRO A CD    1 
ATOM   10458 N N     . ALA D 4 1182 ? 137.061 154.064 92.310  1.00 50.26  ? 1179 ALA A N     1 
ATOM   10459 C CA    . ALA D 4 1182 ? 136.477 154.459 91.034  1.00 50.26  ? 1179 ALA A CA    1 
ATOM   10460 C C     . ALA D 4 1182 ? 137.536 154.584 89.943  1.00 50.26  ? 1179 ALA A C     1 
ATOM   10461 O O     . ALA D 4 1182 ? 137.303 154.185 88.795  1.00 50.26  ? 1179 ALA A O     1 
ATOM   10462 C CB    . ALA D 4 1182 ? 135.715 155.773 91.196  1.00 50.26  ? 1179 ALA A CB    1 
ATOM   10463 N N     . ASN D 4 1183 ? 138.706 155.136 90.279  1.00 50.26  ? 1180 ASN A N     1 
ATOM   10464 C CA    . ASN D 4 1183 ? 139.718 155.405 89.260  1.00 50.26  ? 1180 ASN A CA    1 
ATOM   10465 C C     . ASN D 4 1183 ? 140.231 154.118 88.625  1.00 50.26  ? 1180 ASN A C     1 
ATOM   10466 O O     . ASN D 4 1183 ? 140.198 153.966 87.400  1.00 50.26  ? 1180 ASN A O     1 
ATOM   10467 C CB    . ASN D 4 1183 ? 140.875 156.202 89.864  1.00 50.26  ? 1180 ASN A CB    1 
ATOM   10468 C CG    . ASN D 4 1183 ? 140.594 157.688 89.914  1.00 50.26  ? 1180 ASN A CG    1 
ATOM   10469 O OD1   . ASN D 4 1183 ? 139.584 158.155 89.390  1.00 50.26  ? 1180 ASN A OD1   1 
ATOM   10470 N ND2   . ASN D 4 1183 ? 141.485 158.439 90.549  1.00 50.26  ? 1180 ASN A ND2   1 
ATOM   10471 N N     . GLU D 4 1184 ? 140.696 153.167 89.437  1.00 50.26  ? 1181 GLU A N     1 
ATOM   10472 C CA    . GLU D 4 1184 ? 141.147 151.911 88.848  1.00 50.26  ? 1181 GLU A CA    1 
ATOM   10473 C C     . GLU D 4 1184 ? 139.987 151.047 88.372  1.00 50.26  ? 1181 GLU A C     1 
ATOM   10474 O O     . GLU D 4 1184 ? 140.186 150.198 87.501  1.00 50.26  ? 1181 GLU A O     1 
ATOM   10475 C CB    . GLU D 4 1184 ? 142.062 151.138 89.802  1.00 50.26  ? 1181 GLU A CB    1 
ATOM   10476 C CG    . GLU D 4 1184 ? 141.403 150.588 91.029  1.00 50.26  ? 1181 GLU A CG    1 
ATOM   10477 C CD    . GLU D 4 1184 ? 141.360 151.623 92.120  1.00 50.26  ? 1181 GLU A CD    1 
ATOM   10478 O OE1   . GLU D 4 1184 ? 141.570 152.808 91.804  1.00 50.26  ? 1181 GLU A OE1   1 
ATOM   10479 O OE2   . GLU D 4 1184 ? 141.125 151.259 93.286  1.00 50.26  ? 1181 GLU A OE2   1 
ATOM   10480 N N     . LEU D 4 1185 ? 138.772 151.246 88.889  1.00 50.26  ? 1182 LEU A N     1 
ATOM   10481 C CA    . LEU D 4 1185 ? 137.631 150.547 88.303  1.00 50.26  ? 1182 LEU A CA    1 
ATOM   10482 C C     . LEU D 4 1185 ? 137.429 150.959 86.850  1.00 50.26  ? 1182 LEU A C     1 
ATOM   10483 O O     . LEU D 4 1185 ? 137.339 150.107 85.955  1.00 50.26  ? 1182 LEU A O     1 
ATOM   10484 C CB    . LEU D 4 1185 ? 136.361 150.813 89.106  1.00 50.26  ? 1182 LEU A CB    1 
ATOM   10485 C CG    . LEU D 4 1185 ? 135.181 149.989 88.581  1.00 50.26  ? 1182 LEU A CG    1 
ATOM   10486 C CD1   . LEU D 4 1185 ? 135.405 148.506 88.836  1.00 50.26  ? 1182 LEU A CD1   1 
ATOM   10487 C CD2   . LEU D 4 1185 ? 133.863 150.455 89.162  1.00 50.26  ? 1182 LEU A CD2   1 
ATOM   10488 N N     . ILE D 4 1186 ? 137.368 152.268 86.592  1.00 50.26  ? 1183 ILE A N     1 
ATOM   10489 C CA    . ILE D 4 1186 ? 137.201 152.724 85.215  1.00 50.26  ? 1183 ILE A CA    1 
ATOM   10490 C C     . ILE D 4 1186 ? 138.443 152.405 84.393  1.00 50.26  ? 1183 ILE A C     1 
ATOM   10491 O O     . ILE D 4 1186 ? 138.341 152.141 83.191  1.00 50.26  ? 1183 ILE A O     1 
ATOM   10492 C CB    . ILE D 4 1186 ? 136.846 154.223 85.152  1.00 50.26  ? 1183 ILE A CB    1 
ATOM   10493 C CG1   . ILE D 4 1186 ? 137.972 155.089 85.710  1.00 50.26  ? 1183 ILE A CG1   1 
ATOM   10494 C CG2   . ILE D 4 1186 ? 135.553 154.497 85.895  1.00 50.26  ? 1183 ILE A CG2   1 
ATOM   10495 C CD1   . ILE D 4 1186 ? 137.749 156.571 85.526  1.00 50.26  ? 1183 ILE A CD1   1 
ATOM   10496 N N     . ALA D 4 1187 ? 139.628 152.415 85.012  1.00 51.00  ? 1184 ALA A N     1 
ATOM   10497 C CA    . ALA D 4 1187 ? 140.837 152.037 84.287  1.00 51.00  ? 1184 ALA A CA    1 
ATOM   10498 C C     . ALA D 4 1187 ? 140.779 150.585 83.829  1.00 51.00  ? 1184 ALA A C     1 
ATOM   10499 O O     . ALA D 4 1187 ? 141.102 150.278 82.676  1.00 51.00  ? 1184 ALA A O     1 
ATOM   10500 C CB    . ALA D 4 1187 ? 142.067 152.276 85.161  1.00 51.00  ? 1184 ALA A CB    1 
ATOM   10501 N N     . LEU D 4 1188 ? 140.364 149.679 84.716  1.00 52.40  ? 1185 LEU A N     1 
ATOM   10502 C CA    . LEU D 4 1188 ? 140.224 148.276 84.344  1.00 52.40  ? 1185 LEU A CA    1 
ATOM   10503 C C     . LEU D 4 1188 ? 139.159 148.099 83.275  1.00 52.40  ? 1185 LEU A C     1 
ATOM   10504 O O     . LEU D 4 1188 ? 139.334 147.312 82.338  1.00 52.40  ? 1185 LEU A O     1 
ATOM   10505 C CB    . LEU D 4 1188 ? 139.891 147.439 85.581  1.00 52.40  ? 1185 LEU A CB    1 
ATOM   10506 C CG    . LEU D 4 1188 ? 139.866 145.912 85.473  1.00 52.40  ? 1185 LEU A CG    1 
ATOM   10507 C CD1   . LEU D 4 1188 ? 140.193 145.306 86.818  1.00 52.40  ? 1185 LEU A CD1   1 
ATOM   10508 C CD2   . LEU D 4 1188 ? 138.515 145.398 84.997  1.00 52.40  ? 1185 LEU A CD2   1 
ATOM   10509 N N     . LEU D 4 1189 ? 138.040 148.812 83.405  1.00 56.75  ? 1186 LEU A N     1 
ATOM   10510 C CA    . LEU D 4 1189 ? 136.977 148.681 82.416  1.00 56.75  ? 1186 LEU A CA    1 
ATOM   10511 C C     . LEU D 4 1189 ? 137.431 149.180 81.048  1.00 56.75  ? 1186 LEU A C     1 
ATOM   10512 O O     . LEU D 4 1189 ? 137.117 148.569 80.020  1.00 56.75  ? 1186 LEU A O     1 
ATOM   10513 C CB    . LEU D 4 1189 ? 135.729 149.422 82.893  1.00 56.75  ? 1186 LEU A CB    1 
ATOM   10514 C CG    . LEU D 4 1189 ? 134.692 148.522 83.570  1.00 56.75  ? 1186 LEU A CG    1 
ATOM   10515 C CD1   . LEU D 4 1189 ? 135.248 147.903 84.840  1.00 56.75  ? 1186 LEU A CD1   1 
ATOM   10516 C CD2   . LEU D 4 1189 ? 133.430 149.298 83.878  1.00 56.75  ? 1186 LEU A CD2   1 
ATOM   10517 N N     . GLU D 4 1190 ? 138.176 150.285 81.014  1.00 58.65  ? 1187 GLU A N     1 
ATOM   10518 C CA    . GLU D 4 1190 ? 138.710 150.782 79.752  1.00 58.65  ? 1187 GLU A CA    1 
ATOM   10519 C C     . GLU D 4 1190 ? 139.742 149.823 79.172  1.00 58.65  ? 1187 GLU A C     1 
ATOM   10520 O O     . GLU D 4 1190 ? 139.777 149.599 77.956  1.00 58.65  ? 1187 GLU A O     1 
ATOM   10521 C CB    . GLU D 4 1190 ? 139.316 152.169 79.955  1.00 58.65  ? 1187 GLU A CB    1 
ATOM   10522 C CG    . GLU D 4 1190 ? 138.351 153.312 79.693  1.00 58.65  ? 1187 GLU A CG    1 
ATOM   10523 C CD    . GLU D 4 1190 ? 138.926 154.659 80.086  1.00 58.65  ? 1187 GLU A CD    1 
ATOM   10524 O OE1   . GLU D 4 1190 ? 140.164 154.765 80.210  1.00 58.65  ? 1187 GLU A OE1   1 
ATOM   10525 O OE2   . GLU D 4 1190 ? 138.139 155.611 80.273  1.00 58.65  ? 1187 GLU A OE2   1 
ATOM   10526 N N     . GLU D 4 1191 ? 140.592 149.246 80.025  1.00 58.73  ? 1188 GLU A N     1 
ATOM   10527 C CA    . GLU D 4 1191 ? 141.622 148.331 79.546  1.00 58.73  ? 1188 GLU A CA    1 
ATOM   10528 C C     . GLU D 4 1191 ? 141.027 147.033 79.020  1.00 58.73  ? 1188 GLU A C     1 
ATOM   10529 O O     . GLU D 4 1191 ? 141.561 146.446 78.073  1.00 58.73  ? 1188 GLU A O     1 
ATOM   10530 C CB    . GLU D 4 1191 ? 142.622 148.040 80.665  1.00 58.73  ? 1188 GLU A CB    1 
ATOM   10531 C CG    . GLU D 4 1191 ? 143.797 147.171 80.249  1.00 58.73  ? 1188 GLU A CG    1 
ATOM   10532 C CD    . GLU D 4 1191 ? 144.928 147.196 81.259  1.00 58.73  ? 1188 GLU A CD    1 
ATOM   10533 O OE1   . GLU D 4 1191 ? 144.642 147.201 82.475  1.00 58.73  ? 1188 GLU A OE1   1 
ATOM   10534 O OE2   . GLU D 4 1191 ? 146.103 147.211 80.838  1.00 58.73  ? 1188 GLU A OE2   1 
ATOM   10535 N N     . LYS D 4 1192 ? 139.927 146.574 79.609  1.00 60.42  ? 1189 LYS A N     1 
ATOM   10536 C CA    . LYS D 4 1192 ? 139.330 145.296 79.252  1.00 60.42  ? 1189 LYS A CA    1 
ATOM   10537 C C     . LYS D 4 1192 ? 138.398 145.390 78.053  1.00 60.42  ? 1189 LYS A C     1 
ATOM   10538 O O     . LYS D 4 1192 ? 137.829 144.370 77.649  1.00 60.42  ? 1189 LYS A O     1 
ATOM   10539 C CB    . LYS D 4 1192 ? 138.572 144.719 80.451  1.00 60.42  ? 1189 LYS A CB    1 
ATOM   10540 C CG    . LYS D 4 1192 ? 139.310 143.601 81.172  1.00 60.42  ? 1189 LYS A CG    1 
ATOM   10541 C CD    . LYS D 4 1192 ? 140.774 143.956 81.388  1.00 60.42  ? 1189 LYS A CD    1 
ATOM   10542 C CE    . LYS D 4 1192 ? 141.516 142.844 82.109  1.00 60.42  ? 1189 LYS A CE    1 
ATOM   10543 N NZ    . LYS D 4 1192 ? 142.873 143.274 82.547  1.00 60.42  ? 1189 LYS A NZ    1 
ATOM   10544 N N     . GLY D 4 1193 ? 138.230 146.575 77.476  1.00 62.10  ? 1190 GLY A N     1 
ATOM   10545 C CA    . GLY D 4 1193 ? 137.363 146.723 76.318  1.00 62.10  ? 1190 GLY A CA    1 
ATOM   10546 C C     . GLY D 4 1193 ? 135.901 146.469 76.608  1.00 62.10  ? 1190 GLY A C     1 
ATOM   10547 O O     . GLY D 4 1193 ? 135.217 145.810 75.815  1.00 62.10  ? 1190 GLY A O     1 
ATOM   10548 N N     . ILE D 4 1194 ? 135.404 146.976 77.732  1.00 59.96  ? 1191 ILE A N     1 
ATOM   10549 C CA    . ILE D 4 1194 ? 134.005 146.843 78.118  1.00 59.96  ? 1191 ILE A CA    1 
ATOM   10550 C C     . ILE D 4 1194 ? 133.413 148.237 78.269  1.00 59.96  ? 1191 ILE A C     1 
ATOM   10551 O O     . ILE D 4 1194 ? 134.000 149.100 78.933  1.00 59.96  ? 1191 ILE A O     1 
ATOM   10552 C CB    . ILE D 4 1194 ? 133.849 146.024 79.415  1.00 59.96  ? 1191 ILE A CB    1 
ATOM   10553 C CG1   . ILE D 4 1194 ? 132.401 146.048 79.904  1.00 59.96  ? 1191 ILE A CG1   1 
ATOM   10554 C CG2   . ILE D 4 1194 ? 134.805 146.504 80.490  1.00 59.96  ? 1191 ILE A CG2   1 
ATOM   10555 C CD1   . ILE D 4 1194 ? 132.173 145.194 81.123  1.00 59.96  ? 1191 ILE A CD1   1 
ATOM   10556 N N     . VAL D 4 1195 ? 132.263 148.458 77.643  1.00 64.73  ? 1192 VAL A N     1 
ATOM   10557 C CA    . VAL D 4 1195 ? 131.599 149.756 77.658  1.00 64.73  ? 1192 VAL A CA    1 
ATOM   10558 C C     . VAL D 4 1195 ? 130.724 149.855 78.900  1.00 64.73  ? 1192 VAL A C     1 
ATOM   10559 O O     . VAL D 4 1195 ? 130.026 148.903 79.270  1.00 64.73  ? 1192 VAL A O     1 
ATOM   10560 C CB    . VAL D 4 1195 ? 130.782 149.970 76.368  1.00 64.73  ? 1192 VAL A CB    1 
ATOM   10561 C CG1   . VAL D 4 1195 ? 129.762 148.856 76.180  1.00 64.73  ? 1192 VAL A CG1   1 
ATOM   10562 C CG2   . VAL D 4 1195 ? 130.103 151.331 76.383  1.00 64.73  ? 1192 VAL A CG2   1 
ATOM   10563 N N     . PHE D 4 1196 ? 130.780 151.009 79.564  1.00 61.01  ? 1193 PHE A N     1 
ATOM   10564 C CA    . PHE D 4 1196 ? 130.014 151.221 80.785  1.00 61.01  ? 1193 PHE A CA    1 
ATOM   10565 C C     . PHE D 4 1196 ? 129.306 152.564 80.855  1.00 61.01  ? 1193 PHE A C     1 
ATOM   10566 O O     . PHE D 4 1196 ? 128.445 152.729 81.725  1.00 61.01  ? 1193 PHE A O     1 
ATOM   10567 C CB    . PHE D 4 1196 ? 130.924 151.080 82.013  1.00 61.01  ? 1193 PHE A CB    1 
ATOM   10568 C CG    . PHE D 4 1196 ? 132.093 152.024 82.015  1.00 61.01  ? 1193 PHE A CG    1 
ATOM   10569 C CD1   . PHE D 4 1196 ? 133.268 151.697 81.359  1.00 61.01  ? 1193 PHE A CD1   1 
ATOM   10570 C CD2   . PHE D 4 1196 ? 132.018 153.238 82.676  1.00 61.01  ? 1193 PHE A CD2   1 
ATOM   10571 C CE1   . PHE D 4 1196 ? 134.343 152.562 81.360  1.00 61.01  ? 1193 PHE A CE1   1 
ATOM   10572 C CE2   . PHE D 4 1196 ? 133.090 154.107 82.680  1.00 61.01  ? 1193 PHE A CE2   1 
ATOM   10573 C CZ    . PHE D 4 1196 ? 134.254 153.768 82.022  1.00 61.01  ? 1193 PHE A CZ    1 
ATOM   10574 N N     . ARG D 4 1197 ? 129.628 153.526 79.987  1.00 61.32  ? 1194 ARG A N     1 
ATOM   10575 C CA    . ARG D 4 1197 ? 128.999 154.839 80.061  1.00 61.32  ? 1194 ARG A CA    1 
ATOM   10576 C C     . ARG D 4 1197 ? 127.507 154.784 79.766  1.00 61.32  ? 1194 ARG A C     1 
ATOM   10577 O O     . ARG D 4 1197 ? 126.775 155.701 80.155  1.00 61.32  ? 1194 ARG A O     1 
ATOM   10578 C CB    . ARG D 4 1197 ? 129.685 155.805 79.095  1.00 61.32  ? 1194 ARG A CB    1 
ATOM   10579 C CG    . ARG D 4 1197 ? 130.588 156.817 79.774  1.00 61.32  ? 1194 ARG A CG    1 
ATOM   10580 C CD    . ARG D 4 1197 ? 131.966 156.232 80.024  1.00 61.32  ? 1194 ARG A CD    1 
ATOM   10581 N NE    . ARG D 4 1197 ? 132.876 157.205 80.614  1.00 61.32  ? 1194 ARG A NE    1 
ATOM   10582 C CZ    . ARG D 4 1197 ? 134.197 157.145 80.520  1.00 61.32  ? 1194 ARG A CZ    1 
ATOM   10583 N NH1   . ARG D 4 1197 ? 134.799 156.168 79.863  1.00 61.32  ? 1194 ARG A NH1   1 
ATOM   10584 N NH2   . ARG D 4 1197 ? 134.933 158.089 81.100  1.00 61.32  ? 1194 ARG A NH2   1 
ATOM   10585 N N     . ASP D 4 1198 ? 127.039 153.733 79.091  1.00 65.01  ? 1195 ASP A N     1 
ATOM   10586 C CA    . ASP D 4 1198 ? 125.617 153.590 78.809  1.00 65.01  ? 1195 ASP A CA    1 
ATOM   10587 C C     . ASP D 4 1198 ? 124.799 153.266 80.051  1.00 65.01  ? 1195 ASP A C     1 
ATOM   10588 O O     . ASP D 4 1198 ? 123.566 153.299 79.983  1.00 65.01  ? 1195 ASP A O     1 
ATOM   10589 C CB    . ASP D 4 1198 ? 125.400 152.510 77.748  1.00 65.01  ? 1195 ASP A CB    1 
ATOM   10590 C CG    . ASP D 4 1198 ? 126.078 151.201 78.100  1.00 65.01  ? 1195 ASP A CG    1 
ATOM   10591 O OD1   . ASP D 4 1198 ? 126.836 151.170 79.093  1.00 65.01  ? 1195 ASP A OD1   1 
ATOM   10592 O OD2   . ASP D 4 1198 ? 125.856 150.203 77.383  1.00 65.01  ? 1195 ASP A OD2   1 
ATOM   10593 N N     . GLY D 4 1199 ? 125.446 152.953 81.172  1.00 59.70  ? 1196 GLY A N     1 
ATOM   10594 C CA    . GLY D 4 1199 ? 124.726 152.644 82.390  1.00 59.70  ? 1196 GLY A CA    1 
ATOM   10595 C C     . GLY D 4 1199 ? 124.155 151.248 82.458  1.00 59.70  ? 1196 GLY A C     1 
ATOM   10596 O O     . GLY D 4 1199 ? 123.267 150.995 83.278  1.00 59.70  ? 1196 GLY A O     1 
ATOM   10597 N N     . SER D 4 1200 ? 124.630 150.334 81.620  1.00 54.84  ? 1197 SER A N     1 
ATOM   10598 C CA    . SER D 4 1200 ? 124.150 148.963 81.646  1.00 54.84  ? 1197 SER A CA    1 
ATOM   10599 C C     . SER D 4 1200 ? 124.858 148.169 82.739  1.00 54.84  ? 1197 SER A C     1 
ATOM   10600 O O     . SER D 4 1200 ? 125.877 148.589 83.293  1.00 54.84  ? 1197 SER A O     1 
ATOM   10601 C CB    . SER D 4 1200 ? 124.363 148.292 80.290  1.00 54.84  ? 1197 SER A CB    1 
ATOM   10602 O OG    . SER D 4 1200 ? 125.713 147.895 80.129  1.00 54.84  ? 1197 SER A OG    1 
ATOM   10603 N N     . ASN D 4 1201 ? 124.295 147.003 83.049  1.00 53.29  ? 1198 ASN A N     1 
ATOM   10604 C CA    . ASN D 4 1201 ? 124.888 146.130 84.051  1.00 53.29  ? 1198 ASN A CA    1 
ATOM   10605 C C     . ASN D 4 1201 ? 126.269 145.672 83.599  1.00 53.29  ? 1198 ASN A C     1 
ATOM   10606 O O     . ASN D 4 1201 ? 126.494 145.389 82.419  1.00 53.29  ? 1198 ASN A O     1 
ATOM   10607 C CB    . ASN D 4 1201 ? 123.982 144.925 84.300  1.00 53.29  ? 1198 ASN A CB    1 
ATOM   10608 C CG    . ASN D 4 1201 ? 124.273 144.240 85.617  1.00 53.29  ? 1198 ASN A CG    1 
ATOM   10609 O OD1   . ASN D 4 1201 ? 125.292 144.502 86.255  1.00 53.29  ? 1198 ASN A OD1   1 
ATOM   10610 N ND2   . ASN D 4 1201 ? 123.379 143.351 86.030  1.00 53.29  ? 1198 ASN A ND2   1 
ATOM   10611 N N     . ILE D 4 1202 ? 127.201 145.605 84.547  1.00 52.70  ? 1199 ILE A N     1 
ATOM   10612 C CA    . ILE D 4 1202 ? 128.595 145.316 84.254  1.00 52.70  ? 1199 ILE A CA    1 
ATOM   10613 C C     . ILE D 4 1202 ? 128.995 143.920 84.719  1.00 52.70  ? 1199 ILE A C     1 
ATOM   10614 O O     . ILE D 4 1202 ? 129.789 143.249 84.056  1.00 52.70  ? 1199 ILE A O     1 
ATOM   10615 C CB    . ILE D 4 1202 ? 129.511 146.393 84.877  1.00 52.70  ? 1199 ILE A CB    1 
ATOM   10616 C CG1   . ILE D 4 1202 ? 129.272 147.743 84.199  1.00 52.70  ? 1199 ILE A CG1   1 
ATOM   10617 C CG2   . ILE D 4 1202 ? 130.975 146.005 84.760  1.00 52.70  ? 1199 ILE A CG2   1 
ATOM   10618 C CD1   . ILE D 4 1202 ? 129.915 148.908 84.912  1.00 52.70  ? 1199 ILE A CD1   1 
ATOM   10619 N N     . LEU D 4 1203 ? 128.443 143.459 85.842  1.00 54.99  ? 1200 LEU A N     1 
ATOM   10620 C CA    . LEU D 4 1203 ? 128.843 142.164 86.392  1.00 54.99  ? 1200 LEU A CA    1 
ATOM   10621 C C     . LEU D 4 1203 ? 128.624 141.002 85.429  1.00 54.99  ? 1200 LEU A C     1 
ATOM   10622 O O     . LEU D 4 1203 ? 129.548 140.183 85.271  1.00 54.99  ? 1200 LEU A O     1 
ATOM   10623 C CB    . LEU D 4 1203 ? 128.122 141.930 87.723  1.00 54.99  ? 1200 LEU A CB    1 
ATOM   10624 C CG    . LEU D 4 1203 ? 128.208 143.067 88.740  1.00 54.99  ? 1200 LEU A CG    1 
ATOM   10625 C CD1   . LEU D 4 1203 ? 127.415 142.723 89.986  1.00 54.99  ? 1200 LEU A CD1   1 
ATOM   10626 C CD2   . LEU D 4 1203 ? 129.657 143.363 89.087  1.00 54.99  ? 1200 LEU A CD2   1 
ATOM   10627 N N     . PRO D 4 1204 ? 127.462 140.845 84.777  1.00 57.41  ? 1201 PRO A N     1 
ATOM   10628 C CA    . PRO D 4 1204 ? 127.339 139.745 83.805  1.00 57.41  ? 1201 PRO A CA    1 
ATOM   10629 C C     . PRO D 4 1204 ? 128.354 139.834 82.682  1.00 57.41  ? 1201 PRO A C     1 
ATOM   10630 O O     . PRO D 4 1204 ? 128.857 138.802 82.222  1.00 57.41  ? 1201 PRO A O     1 
ATOM   10631 C CB    . PRO D 4 1204 ? 125.900 139.886 83.289  1.00 57.41  ? 1201 PRO A CB    1 
ATOM   10632 C CG    . PRO D 4 1204 ? 125.191 140.667 84.329  1.00 57.41  ? 1201 PRO A CG    1 
ATOM   10633 C CD    . PRO D 4 1204 ? 126.205 141.603 84.893  1.00 57.41  ? 1201 PRO A CD    1 
ATOM   10634 N N     . LYS D 4 1205 ? 128.682 141.047 82.236  1.00 59.02  ? 1202 LYS A N     1 
ATOM   10635 C CA    . LYS D 4 1205 ? 129.720 141.205 81.224  1.00 59.02  ? 1202 LYS A CA    1 
ATOM   10636 C C     . LYS D 4 1205 ? 131.078 140.765 81.756  1.00 59.02  ? 1202 LYS A C     1 
ATOM   10637 O O     . LYS D 4 1205 ? 131.866 140.145 81.031  1.00 59.02  ? 1202 LYS A O     1 
ATOM   10638 C CB    . LYS D 4 1205 ? 129.770 142.654 80.748  1.00 59.02  ? 1202 LYS A CB    1 
ATOM   10639 C CG    . LYS D 4 1205 ? 128.433 143.206 80.290  1.00 59.02  ? 1202 LYS A CG    1 
ATOM   10640 C CD    . LYS D 4 1205 ? 128.542 144.681 79.944  1.00 59.02  ? 1202 LYS A CD    1 
ATOM   10641 C CE    . LYS D 4 1205 ? 127.300 145.169 79.221  1.00 59.02  ? 1202 LYS A CE    1 
ATOM   10642 N NZ    . LYS D 4 1205 ? 127.422 146.598 78.826  1.00 59.02  ? 1202 LYS A NZ    1 
ATOM   10643 N N     . LEU D 4 1206 ? 131.372 141.081 83.020  1.00 57.98  ? 1203 LEU A N     1 
ATOM   10644 C CA    . LEU D 4 1206 ? 132.627 140.640 83.619  1.00 57.98  ? 1203 LEU A CA    1 
ATOM   10645 C C     . LEU D 4 1206 ? 132.699 139.121 83.691  1.00 57.98  ? 1203 LEU A C     1 
ATOM   10646 O O     . LEU D 4 1206 ? 133.751 138.529 83.424  1.00 57.98  ? 1203 LEU A O     1 
ATOM   10647 C CB    . LEU D 4 1206 ? 132.791 141.251 85.009  1.00 57.98  ? 1203 LEU A CB    1 
ATOM   10648 C CG    . LEU D 4 1206 ? 133.458 142.624 85.072  1.00 57.98  ? 1203 LEU A CG    1 
ATOM   10649 C CD1   . LEU D 4 1206 ? 133.600 143.083 86.513  1.00 57.98  ? 1203 LEU A CD1   1 
ATOM   10650 C CD2   . LEU D 4 1206 ? 134.812 142.590 84.384  1.00 57.98  ? 1203 LEU A CD2   1 
ATOM   10651 N N     . LEU D 4 1207 ? 131.591 138.471 84.056  1.00 60.55  ? 1204 LEU A N     1 
ATOM   10652 C CA    . LEU D 4 1207 ? 131.571 137.010 84.066  1.00 60.55  ? 1204 LEU A CA    1 
ATOM   10653 C C     . LEU D 4 1207 ? 131.734 136.444 82.660  1.00 60.55  ? 1204 LEU A C     1 
ATOM   10654 O O     . LEU D 4 1207 ? 132.417 135.432 82.465  1.00 60.55  ? 1204 LEU A O     1 
ATOM   10655 C CB    . LEU D 4 1207 ? 130.283 136.496 84.710  1.00 60.55  ? 1204 LEU A CB    1 
ATOM   10656 C CG    . LEU D 4 1207 ? 130.301 136.302 86.230  1.00 60.55  ? 1204 LEU A CG    1 
ATOM   10657 C CD1   . LEU D 4 1207 ? 130.259 137.627 86.973  1.00 60.55  ? 1204 LEU A CD1   1 
ATOM   10658 C CD2   . LEU D 4 1207 ? 129.155 135.403 86.669  1.00 60.55  ? 1204 LEU A CD2   1 
ATOM   10659 N N     . GLU D 4 1208 ? 131.109 137.082 81.667  1.00 62.70  ? 1205 GLU A N     1 
ATOM   10660 C CA    . GLU D 4 1208 ? 131.250 136.626 80.287  1.00 62.70  ? 1205 GLU A CA    1 
ATOM   10661 C C     . GLU D 4 1208 ? 132.692 136.745 79.811  1.00 62.70  ? 1205 GLU A C     1 
ATOM   10662 O O     . GLU D 4 1208 ? 133.172 135.899 79.048  1.00 62.70  ? 1205 GLU A O     1 
ATOM   10663 C CB    . GLU D 4 1208 ? 130.317 137.417 79.372  1.00 62.70  ? 1205 GLU A CB    1 
ATOM   10664 C CG    . GLU D 4 1208 ? 128.848 137.076 79.540  1.00 62.70  ? 1205 GLU A CG    1 
ATOM   10665 C CD    . GLU D 4 1208 ? 127.950 137.933 78.670  1.00 62.70  ? 1205 GLU A CD    1 
ATOM   10666 O OE1   . GLU D 4 1208 ? 128.471 138.848 77.999  1.00 62.70  ? 1205 GLU A OE1   1 
ATOM   10667 O OE2   . GLU D 4 1208 ? 126.725 137.692 78.659  1.00 62.70  ? 1205 GLU A OE2   1 
ATOM   10668 N N     . ASN D 4 1209 ? 133.394 137.796 80.241  1.00 68.15  ? 1206 ASN A N     1 
ATOM   10669 C CA    . ASN D 4 1209 ? 134.796 137.951 79.864  1.00 68.15  ? 1206 ASN A CA    1 
ATOM   10670 C C     . ASN D 4 1209 ? 135.645 136.791 80.368  1.00 68.15  ? 1206 ASN A C     1 
ATOM   10671 O O     . ASN D 4 1209 ? 136.615 136.402 79.708  1.00 68.15  ? 1206 ASN A O     1 
ATOM   10672 C CB    . ASN D 4 1209 ? 135.341 139.277 80.394  1.00 68.15  ? 1206 ASN A CB    1 
ATOM   10673 C CG    . ASN D 4 1209 ? 135.074 140.434 79.453  1.00 68.15  ? 1206 ASN A CG    1 
ATOM   10674 O OD1   . ASN D 4 1209 ? 134.097 140.429 78.706  1.00 68.15  ? 1206 ASN A OD1   1 
ATOM   10675 N ND2   . ASN D 4 1209 ? 135.947 141.434 79.484  1.00 68.15  ? 1206 ASN A ND2   1 
ATOM   10676 N N     . ASP D 4 1210 ? 135.296 136.231 81.528  1.00 72.38  ? 1207 ASP A N     1 
ATOM   10677 C CA    . ASP D 4 1210 ? 135.976 135.064 82.093  1.00 72.38  ? 1207 ASP A CA    1 
ATOM   10678 C C     . ASP D 4 1210 ? 137.471 135.306 82.280  1.00 72.38  ? 1207 ASP A C     1 
ATOM   10679 O O     . ASP D 4 1210 ? 138.288 134.410 82.056  1.00 72.38  ? 1207 ASP A O     1 
ATOM   10680 C CB    . ASP D 4 1210 ? 135.741 133.816 81.236  1.00 72.38  ? 1207 ASP A CB    1 
ATOM   10681 C CG    . ASP D 4 1210 ? 135.687 132.545 82.060  1.00 72.38  ? 1207 ASP A CG    1 
ATOM   10682 O OD1   . ASP D 4 1210 ? 135.734 132.640 83.304  1.00 72.38  ? 1207 ASP A OD1   1 
ATOM   10683 O OD2   . ASP D 4 1210 ? 135.597 131.452 81.464  1.00 72.38  ? 1207 ASP A OD2   1 
ATOM   10684 N N     . ASP D 4 1211 ? 137.841 136.515 82.690  1.00 65.86  ? 1208 ASP A N     1 
ATOM   10685 C CA    . ASP D 4 1211 ? 139.236 136.857 82.933  1.00 65.86  ? 1208 ASP A CA    1 
ATOM   10686 C C     . ASP D 4 1211 ? 139.516 136.766 84.428  1.00 65.86  ? 1208 ASP A C     1 
ATOM   10687 O O     . ASP D 4 1211 ? 138.870 137.451 85.227  1.00 65.86  ? 1208 ASP A O     1 
ATOM   10688 C CB    . ASP D 4 1211 ? 139.550 138.256 82.405  1.00 65.86  ? 1208 ASP A CB    1 
ATOM   10689 C CG    . ASP D 4 1211 ? 141.038 138.507 82.268  1.00 65.86  ? 1208 ASP A CG    1 
ATOM   10690 O OD1   . ASP D 4 1211 ? 141.829 137.588 82.569  1.00 65.86  ? 1208 ASP A OD1   1 
ATOM   10691 O OD2   . ASP D 4 1211 ? 141.419 139.622 81.856  1.00 65.86  ? 1208 ASP A OD2   1 
ATOM   10692 N N     . SER D 4 1212 ? 140.474 135.915 84.802  1.00 62.94  ? 1209 SER A N     1 
ATOM   10693 C CA    . SER D 4 1212 ? 140.780 135.723 86.216  1.00 62.94  ? 1209 SER A CA    1 
ATOM   10694 C C     . SER D 4 1212 ? 141.333 136.994 86.845  1.00 62.94  ? 1209 SER A C     1 
ATOM   10695 O O     . SER D 4 1212 ? 140.958 137.355 87.967  1.00 62.94  ? 1209 SER A O     1 
ATOM   10696 C CB    . SER D 4 1212 ? 141.765 134.567 86.386  1.00 62.94  ? 1209 SER A CB    1 
ATOM   10697 O OG    . SER D 4 1212 ? 142.993 134.845 85.736  1.00 62.94  ? 1209 SER A OG    1 
ATOM   10698 N N     . HIS D 4 1213 ? 142.230 137.686 86.138  1.00 60.93  ? 1210 HIS A N     1 
ATOM   10699 C CA    . HIS D 4 1213 ? 142.833 138.898 86.683  1.00 60.93  ? 1210 HIS A CA    1 
ATOM   10700 C C     . HIS D 4 1213 ? 141.778 139.968 86.933  1.00 60.93  ? 1210 HIS A C     1 
ATOM   10701 O O     . HIS D 4 1213 ? 141.755 140.599 87.997  1.00 60.93  ? 1210 HIS A O     1 
ATOM   10702 C CB    . HIS D 4 1213 ? 143.911 139.411 85.728  1.00 60.93  ? 1210 HIS A CB    1 
ATOM   10703 C CG    . HIS D 4 1213 ? 144.621 140.636 86.214  1.00 60.93  ? 1210 HIS A CG    1 
ATOM   10704 N ND1   . HIS D 4 1213 ? 145.550 140.604 87.232  1.00 60.93  ? 1210 HIS A ND1   1 
ATOM   10705 C CD2   . HIS D 4 1213 ? 144.542 141.929 85.818  1.00 60.93  ? 1210 HIS A CD2   1 
ATOM   10706 C CE1   . HIS D 4 1213 ? 146.012 141.823 87.443  1.00 60.93  ? 1210 HIS A CE1   1 
ATOM   10707 N NE2   . HIS D 4 1213 ? 145.416 142.646 86.599  1.00 60.93  ? 1210 HIS A NE2   1 
ATOM   10708 N N     . ALA D 4 1214 ? 140.884 140.173 85.964  1.00 55.59  ? 1211 ALA A N     1 
ATOM   10709 C CA    . ALA D 4 1214 ? 139.848 141.189 86.115  1.00 55.59  ? 1211 ALA A CA    1 
ATOM   10710 C C     . ALA D 4 1214 ? 138.897 140.849 87.254  1.00 55.59  ? 1211 ALA A C     1 
ATOM   10711 O O     . ALA D 4 1214 ? 138.523 141.726 88.039  1.00 55.59  ? 1211 ALA A O     1 
ATOM   10712 C CB    . ALA D 4 1214 ? 139.079 141.351 84.804  1.00 55.59  ? 1211 ALA A CB    1 
ATOM   10713 N N     . ILE D 4 1215 ? 138.494 139.581 87.363  1.00 52.55  ? 1212 ILE A N     1 
ATOM   10714 C CA    . ILE D 4 1215 ? 137.569 139.183 88.420  1.00 52.55  ? 1212 ILE A CA    1 
ATOM   10715 C C     . ILE D 4 1215 ? 138.217 139.339 89.791  1.00 52.55  ? 1212 ILE A C     1 
ATOM   10716 O O     . ILE D 4 1215 ? 137.589 139.829 90.738  1.00 52.55  ? 1212 ILE A O     1 
ATOM   10717 C CB    . ILE D 4 1215 ? 137.077 137.744 88.183  1.00 52.55  ? 1212 ILE A CB    1 
ATOM   10718 C CG1   . ILE D 4 1215 ? 136.150 137.692 86.967  1.00 52.55  ? 1212 ILE A CG1   1 
ATOM   10719 C CG2   . ILE D 4 1215 ? 136.371 137.206 89.417  1.00 52.55  ? 1212 ILE A CG2   1 
ATOM   10720 C CD1   . ILE D 4 1215 ? 134.767 138.242 87.226  1.00 52.55  ? 1212 ILE A CD1   1 
ATOM   10721 N N     . ASP D 4 1216 ? 139.478 138.919 89.922  1.00 52.39  ? 1213 ASP A N     1 
ATOM   10722 C CA    . ASP D 4 1216 ? 140.169 139.057 91.199  1.00 52.39  ? 1213 ASP A CA    1 
ATOM   10723 C C     . ASP D 4 1216 ? 140.338 140.523 91.577  1.00 52.39  ? 1213 ASP A C     1 
ATOM   10724 O O     . ASP D 4 1216 ? 140.147 140.898 92.741  1.00 52.39  ? 1213 ASP A O     1 
ATOM   10725 C CB    . ASP D 4 1216 ? 141.526 138.355 91.141  1.00 52.39  ? 1213 ASP A CB    1 
ATOM   10726 C CG    . ASP D 4 1216 ? 142.297 138.467 92.441  1.00 52.39  ? 1213 ASP A CG    1 
ATOM   10727 O OD1   . ASP D 4 1216 ? 141.678 138.315 93.515  1.00 52.39  ? 1213 ASP A OD1   1 
ATOM   10728 O OD2   . ASP D 4 1216 ? 143.522 138.705 92.388  1.00 52.39  ? 1213 ASP A OD2   1 
ATOM   10729 N N     . THR D 4 1217 ? 140.682 141.371 90.605  1.00 50.26  ? 1214 THR A N     1 
ATOM   10730 C CA    . THR D 4 1217 ? 140.818 142.794 90.893  1.00 50.26  ? 1214 THR A CA    1 
ATOM   10731 C C     . THR D 4 1217 ? 139.476 143.410 91.268  1.00 50.26  ? 1214 THR A C     1 
ATOM   10732 O O     . THR D 4 1217 ? 139.411 144.281 92.141  1.00 50.26  ? 1214 THR A O     1 
ATOM   10733 C CB    . THR D 4 1217 ? 141.430 143.518 89.696  1.00 50.26  ? 1214 THR A CB    1 
ATOM   10734 O OG1   . THR D 4 1217 ? 142.614 142.830 89.276  1.00 50.26  ? 1214 THR A OG1   1 
ATOM   10735 C CG2   . THR D 4 1217 ? 141.793 144.945 90.069  1.00 50.26  ? 1214 THR A CG2   1 
ATOM   10736 N N     . MET D 4 1218 ? 138.393 142.969 90.624  1.00 50.26  ? 1215 MET A N     1 
ATOM   10737 C CA    . MET D 4 1218 ? 137.066 143.461 90.979  1.00 50.26  ? 1215 MET A CA    1 
ATOM   10738 C C     . MET D 4 1218 ? 136.685 143.066 92.400  1.00 50.26  ? 1215 MET A C     1 
ATOM   10739 O O     . MET D 4 1218 ? 136.128 143.876 93.152  1.00 50.26  ? 1215 MET A O     1 
ATOM   10740 C CB    . MET D 4 1218 ? 136.034 142.935 89.985  1.00 50.26  ? 1215 MET A CB    1 
ATOM   10741 C CG    . MET D 4 1218 ? 134.630 143.404 90.272  1.00 50.26  ? 1215 MET A CG    1 
ATOM   10742 S SD    . MET D 4 1218 ? 134.526 145.196 90.361  1.00 50.26  ? 1215 MET A SD    1 
ATOM   10743 C CE    . MET D 4 1218 ? 132.753 145.406 90.339  1.00 50.26  ? 1215 MET A CE    1 
ATOM   10744 N N     . VAL D 4 1219 ? 136.963 141.818 92.782  1.00 50.26  ? 1216 VAL A N     1 
ATOM   10745 C CA    . VAL D 4 1219 ? 136.664 141.376 94.141  1.00 50.26  ? 1216 VAL A CA    1 
ATOM   10746 C C     . VAL D 4 1219 ? 137.485 142.173 95.146  1.00 50.26  ? 1216 VAL A C     1 
ATOM   10747 O O     . VAL D 4 1219 ? 136.979 142.586 96.199  1.00 50.26  ? 1216 VAL A O     1 
ATOM   10748 C CB    . VAL D 4 1219 ? 136.908 139.862 94.278  1.00 50.26  ? 1216 VAL A CB    1 
ATOM   10749 C CG1   . VAL D 4 1219 ? 136.876 139.449 95.736  1.00 50.26  ? 1216 VAL A CG1   1 
ATOM   10750 C CG2   . VAL D 4 1219 ? 135.875 139.091 93.487  1.00 50.26  ? 1216 VAL A CG2   1 
ATOM   10751 N N     . ALA D 4 1220 ? 138.761 142.410 94.832  1.00 50.26  ? 1217 ALA A N     1 
ATOM   10752 C CA    . ALA D 4 1220 ? 139.600 143.224 95.705  1.00 50.26  ? 1217 ALA A CA    1 
ATOM   10753 C C     . ALA D 4 1220 ? 139.063 144.645 95.819  1.00 50.26  ? 1217 ALA A C     1 
ATOM   10754 O O     . ALA D 4 1220 ? 139.106 145.246 96.897  1.00 50.26  ? 1217 ALA A O     1 
ATOM   10755 C CB    . ALA D 4 1220 ? 141.040 143.233 95.192  1.00 50.26  ? 1217 ALA A CB    1 
ATOM   10756 N N     . LEU D 4 1221 ? 138.561 145.203 94.715  1.00 50.26  ? 1218 LEU A N     1 
ATOM   10757 C CA    . LEU D 4 1221 ? 137.986 146.544 94.753  1.00 50.26  ? 1218 LEU A CA    1 
ATOM   10758 C C     . LEU D 4 1221 ? 136.737 146.588 95.623  1.00 50.26  ? 1218 LEU A C     1 
ATOM   10759 O O     . LEU D 4 1221 ? 136.524 147.551 96.367  1.00 50.26  ? 1218 LEU A O     1 
ATOM   10760 C CB    . LEU D 4 1221 ? 137.660 147.015 93.338  1.00 50.26  ? 1218 LEU A CB    1 
ATOM   10761 C CG    . LEU D 4 1221 ? 138.845 147.522 92.523  1.00 50.26  ? 1218 LEU A CG    1 
ATOM   10762 C CD1   . LEU D 4 1221 ? 138.365 148.194 91.252  1.00 50.26  ? 1218 LEU A CD1   1 
ATOM   10763 C CD2   . LEU D 4 1221 ? 139.686 148.461 93.352  1.00 50.26  ? 1218 LEU A CD2   1 
ATOM   10764 N N     . ILE D 4 1222 ? 135.888 145.566 95.525  1.00 50.26  ? 1219 ILE A N     1 
ATOM   10765 C CA    . ILE D 4 1222 ? 134.705 145.510 96.378  1.00 50.26  ? 1219 ILE A CA    1 
ATOM   10766 C C     . ILE D 4 1222 ? 135.116 145.437 97.843  1.00 50.26  ? 1219 ILE A C     1 
ATOM   10767 O O     . ILE D 4 1222 ? 134.549 146.125 98.702  1.00 50.26  ? 1219 ILE A O     1 
ATOM   10768 C CB    . ILE D 4 1222 ? 133.811 144.325 95.975  1.00 50.26  ? 1219 ILE A CB    1 
ATOM   10769 C CG1   . ILE D 4 1222 ? 133.317 144.503 94.540  1.00 50.26  ? 1219 ILE A CG1   1 
ATOM   10770 C CG2   . ILE D 4 1222 ? 132.640 144.196 96.926  1.00 50.26  ? 1219 ILE A CG2   1 
ATOM   10771 C CD1   . ILE D 4 1222 ? 132.524 145.759 94.325  1.00 50.26  ? 1219 ILE A CD1   1 
ATOM   10772 N N     . ARG D 4 1223 ? 136.122 144.614 98.148  1.00 50.26  ? 1220 ARG A N     1 
ATOM   10773 C CA    . ARG D 4 1223 ? 136.609 144.522 99.521  1.00 50.26  ? 1220 ARG A CA    1 
ATOM   10774 C C     . ARG D 4 1223 ? 137.167 145.857 100.001 1.00 50.26  ? 1220 ARG A C     1 
ATOM   10775 O O     . ARG D 4 1223 ? 136.940 146.258 101.148 1.00 50.26  ? 1220 ARG A O     1 
ATOM   10776 C CB    . ARG D 4 1223 ? 137.672 143.430 99.626  1.00 50.26  ? 1220 ARG A CB    1 
ATOM   10777 C CG    . ARG D 4 1223 ? 138.257 143.266 101.017 1.00 50.26  ? 1220 ARG A CG    1 
ATOM   10778 C CD    . ARG D 4 1223 ? 139.029 141.965 101.140 1.00 50.26  ? 1220 ARG A CD    1 
ATOM   10779 N NE    . ARG D 4 1223 ? 139.850 141.925 102.343 1.00 50.26  ? 1220 ARG A NE    1 
ATOM   10780 C CZ    . ARG D 4 1223 ? 140.671 140.932 102.655 1.00 50.26  ? 1220 ARG A CZ    1 
ATOM   10781 N NH1   . ARG D 4 1223 ? 140.806 139.875 101.872 1.00 50.26  ? 1220 ARG A NH1   1 
ATOM   10782 N NH2   . ARG D 4 1223 ? 141.373 141.000 103.783 1.00 50.26  ? 1220 ARG A NH2   1 
ATOM   10783 N N     . SER D 4 1224 ? 137.904 146.555 99.136  1.00 50.26  ? 1221 SER A N     1 
ATOM   10784 C CA    . SER D 4 1224 ? 138.504 147.829 99.518  1.00 50.26  ? 1221 SER A CA    1 
ATOM   10785 C C     . SER D 4 1224 ? 137.446 148.897 99.755  1.00 50.26  ? 1221 SER A C     1 
ATOM   10786 O O     . SER D 4 1224 ? 137.527 149.651 100.731 1.00 50.26  ? 1221 SER A O     1 
ATOM   10787 C CB    . SER D 4 1224 ? 139.483 148.285 98.440  1.00 50.26  ? 1221 SER A CB    1 
ATOM   10788 O OG    . SER D 4 1224 ? 138.804 148.971 97.405  1.00 50.26  ? 1221 SER A OG    1 
ATOM   10789 N N     . VAL D 4 1225 ? 136.455 148.991 98.868  1.00 50.26  ? 1222 VAL A N     1 
ATOM   10790 C CA    . VAL D 4 1225 ? 135.425 150.010 99.028  1.00 50.26  ? 1222 VAL A CA    1 
ATOM   10791 C C     . VAL D 4 1225 ? 134.561 149.706 100.244 1.00 50.26  ? 1222 VAL A C     1 
ATOM   10792 O O     . VAL D 4 1225 ? 134.125 150.620 100.954 1.00 50.26  ? 1222 VAL A O     1 
ATOM   10793 C CB    . VAL D 4 1225 ? 134.586 150.146 97.744  1.00 50.26  ? 1222 VAL A CB    1 
ATOM   10794 C CG1   . VAL D 4 1225 ? 133.812 148.877 97.469  1.00 50.26  ? 1222 VAL A CG1   1 
ATOM   10795 C CG2   . VAL D 4 1225 ? 133.640 151.327 97.859  1.00 50.26  ? 1222 VAL A CG2   1 
ATOM   10796 N N     . LEU D 4 1226 ? 134.305 148.424 100.513 1.00 50.26  ? 1223 LEU A N     1 
ATOM   10797 C CA    . LEU D 4 1226 ? 133.545 148.070 101.704 1.00 50.26  ? 1223 LEU A CA    1 
ATOM   10798 C C     . LEU D 4 1226 ? 134.356 148.233 102.981 1.00 50.26  ? 1223 LEU A C     1 
ATOM   10799 O O     . LEU D 4 1226 ? 133.772 148.217 104.069 1.00 50.26  ? 1223 LEU A O     1 
ATOM   10800 C CB    . LEU D 4 1226 ? 133.023 146.640 101.587 1.00 50.26  ? 1223 LEU A CB    1 
ATOM   10801 C CG    . LEU D 4 1226 ? 131.772 146.516 100.718 1.00 50.26  ? 1223 LEU A CG    1 
ATOM   10802 C CD1   . LEU D 4 1226 ? 131.471 145.065 100.397 1.00 50.26  ? 1223 LEU A CD1   1 
ATOM   10803 C CD2   . LEU D 4 1226 ? 130.589 147.174 101.401 1.00 50.26  ? 1223 LEU A CD2   1 
ATOM   10804 N N     . GLN D 4 1227 ? 135.673 148.392 102.876 1.00 50.26  ? 1224 GLN A N     1 
ATOM   10805 C CA    . GLN D 4 1227 ? 136.503 148.701 104.034 1.00 50.26  ? 1224 GLN A CA    1 
ATOM   10806 C C     . GLN D 4 1227 ? 136.314 150.166 104.398 1.00 50.26  ? 1224 GLN A C     1 
ATOM   10807 O O     . GLN D 4 1227 ? 136.721 151.058 103.647 1.00 50.26  ? 1224 GLN A O     1 
ATOM   10808 C CB    . GLN D 4 1227 ? 137.966 148.398 103.733 1.00 50.26  ? 1224 GLN A CB    1 
ATOM   10809 C CG    . GLN D 4 1227 ? 138.913 148.730 104.870 1.00 50.26  ? 1224 GLN A CG    1 
ATOM   10810 C CD    . GLN D 4 1227 ? 140.326 148.980 104.391 1.00 50.26  ? 1224 GLN A CD    1 
ATOM   10811 O OE1   . GLN D 4 1227 ? 140.822 148.291 103.501 1.00 50.26  ? 1224 GLN A OE1   1 
ATOM   10812 N NE2   . GLN D 4 1227 ? 140.984 149.971 104.979 1.00 50.26  ? 1224 GLN A NE2   1 
ATOM   10813 N N     . MET D 4 1228 ? 135.703 150.422 105.551 1.00 50.26  ? 1225 MET A N     1 
ATOM   10814 C CA    . MET D 4 1228 ? 135.334 151.779 105.927 1.00 50.26  ? 1225 MET A CA    1 
ATOM   10815 C C     . MET D 4 1228 ? 136.446 152.492 106.686 1.00 50.26  ? 1225 MET A C     1 
ATOM   10816 O O     . MET D 4 1228 ? 136.825 153.611 106.329 1.00 50.26  ? 1225 MET A O     1 
ATOM   10817 C CB    . MET D 4 1228 ? 134.053 151.751 106.760 1.00 50.26  ? 1225 MET A CB    1 
ATOM   10818 C CG    . MET D 4 1228 ? 132.829 151.343 105.967 1.00 50.26  ? 1225 MET A CG    1 
ATOM   10819 S SD    . MET D 4 1228 ? 131.550 150.638 107.013 1.00 50.26  ? 1225 MET A SD    1 
ATOM   10820 C CE    . MET D 4 1228 ? 131.519 151.859 108.314 1.00 50.26  ? 1225 MET A CE    1 
ATOM   10821 N N     . ARG D 4 1229 ? 136.977 151.863 107.730 1.00 50.26  ? 1226 ARG A N     1 
ATOM   10822 C CA    . ARG D 4 1229 ? 138.017 152.479 108.547 1.00 50.26  ? 1226 ARG A CA    1 
ATOM   10823 C C     . ARG D 4 1229 ? 139.340 152.429 107.794 1.00 50.26  ? 1226 ARG A C     1 
ATOM   10824 O O     . ARG D 4 1229 ? 139.925 151.356 107.620 1.00 50.26  ? 1226 ARG A O     1 
ATOM   10825 C CB    . ARG D 4 1229 ? 138.129 151.771 109.892 1.00 50.26  ? 1226 ARG A CB    1 
ATOM   10826 C CG    . ARG D 4 1229 ? 139.211 152.340 110.786 1.00 50.26  ? 1226 ARG A CG    1 
ATOM   10827 C CD    . ARG D 4 1229 ? 139.128 151.765 112.184 1.00 50.26  ? 1226 ARG A CD    1 
ATOM   10828 N NE    . ARG D 4 1229 ? 139.990 152.487 113.110 1.00 50.26  ? 1226 ARG A NE    1 
ATOM   10829 C CZ    . ARG D 4 1229 ? 139.861 152.456 114.429 1.00 50.26  ? 1226 ARG A CZ    1 
ATOM   10830 N NH1   . ARG D 4 1229 ? 138.923 151.731 115.014 1.00 50.26  ? 1226 ARG A NH1   1 
ATOM   10831 N NH2   . ARG D 4 1229 ? 140.690 153.176 115.178 1.00 50.26  ? 1226 ARG A NH2   1 
ATOM   10832 N N     . ASN D 4 1230 ? 139.815 153.589 107.352 1.00 50.26  ? 1227 ASN A N     1 
ATOM   10833 C CA    . ASN D 4 1230 ? 141.092 153.710 106.661 1.00 50.26  ? 1227 ASN A CA    1 
ATOM   10834 C C     . ASN D 4 1230 ? 142.029 154.538 107.526 1.00 50.26  ? 1227 ASN A C     1 
ATOM   10835 O O     . ASN D 4 1230 ? 141.706 155.676 107.882 1.00 50.26  ? 1227 ASN A O     1 
ATOM   10836 C CB    . ASN D 4 1230 ? 140.911 154.352 105.286 1.00 50.26  ? 1227 ASN A CB    1 
ATOM   10837 C CG    . ASN D 4 1230 ? 139.866 153.645 104.451 1.00 50.26  ? 1227 ASN A CG    1 
ATOM   10838 O OD1   . ASN D 4 1230 ? 140.169 152.689 103.737 1.00 50.26  ? 1227 ASN A OD1   1 
ATOM   10839 N ND2   . ASN D 4 1230 ? 138.626 154.108 104.539 1.00 50.26  ? 1227 ASN A ND2   1 
ATOM   10840 N N     . SER D 4 1231 ? 143.183 153.969 107.862 1.00 50.26  ? 1228 SER A N     1 
ATOM   10841 C CA    . SER D 4 1231 ? 144.142 154.617 108.740 1.00 50.26  ? 1228 SER A CA    1 
ATOM   10842 C C     . SER D 4 1231 ? 145.544 154.489 108.166 1.00 50.26  ? 1228 SER A C     1 
ATOM   10843 O O     . SER D 4 1231 ? 145.879 153.497 107.513 1.00 50.26  ? 1228 SER A O     1 
ATOM   10844 C CB    . SER D 4 1231 ? 144.100 154.019 110.152 1.00 50.26  ? 1228 SER A CB    1 
ATOM   10845 O OG    . SER D 4 1231 ? 144.011 152.606 110.103 1.00 50.26  ? 1228 SER A OG    1 
ATOM   10846 N N     . ASN D 4 1232 ? 146.363 155.509 108.420 1.00 57.59  ? 1229 ASN A N     1 
ATOM   10847 C CA    . ASN D 4 1232 ? 147.755 155.512 107.972 1.00 57.59  ? 1229 ASN A CA    1 
ATOM   10848 C C     . ASN D 4 1232 ? 148.545 156.359 108.965 1.00 57.59  ? 1229 ASN A C     1 
ATOM   10849 O O     . ASN D 4 1232 ? 148.514 157.591 108.895 1.00 57.59  ? 1229 ASN A O     1 
ATOM   10850 C CB    . ASN D 4 1232 ? 147.878 156.046 106.552 1.00 57.59  ? 1229 ASN A CB    1 
ATOM   10851 C CG    . ASN D 4 1232 ? 149.221 155.736 105.930 1.00 57.59  ? 1229 ASN A CG    1 
ATOM   10852 O OD1   . ASN D 4 1232 ? 150.033 155.015 106.509 1.00 57.59  ? 1229 ASN A OD1   1 
ATOM   10853 N ND2   . ASN D 4 1232 ? 149.463 156.276 104.742 1.00 57.59  ? 1229 ASN A ND2   1 
ATOM   10854 N N     . ALA D 4 1233 ? 149.248 155.690 109.882 1.00 59.57  ? 1230 ALA A N     1 
ATOM   10855 C CA    . ALA D 4 1233 ? 149.975 156.403 110.927 1.00 59.57  ? 1230 ALA A CA    1 
ATOM   10856 C C     . ALA D 4 1233 ? 151.117 157.236 110.361 1.00 59.57  ? 1230 ALA A C     1 
ATOM   10857 O O     . ALA D 4 1233 ? 151.477 158.264 110.945 1.00 59.57  ? 1230 ALA A O     1 
ATOM   10858 C CB    . ALA D 4 1233 ? 150.507 155.414 111.963 1.00 59.57  ? 1230 ALA A CB    1 
ATOM   10859 N N     . ALA D 4 1234 ? 151.700 156.810 109.238 1.00 61.38  ? 1231 ALA A N     1 
ATOM   10860 C CA    . ALA D 4 1234 ? 152.842 157.528 108.680 1.00 61.38  ? 1231 ALA A CA    1 
ATOM   10861 C C     . ALA D 4 1234 ? 152.464 158.946 108.271 1.00 61.38  ? 1231 ALA A C     1 
ATOM   10862 O O     . ALA D 4 1234 ? 153.211 159.896 108.531 1.00 61.38  ? 1231 ALA A O     1 
ATOM   10863 C CB    . ALA D 4 1234 ? 153.413 156.759 107.489 1.00 61.38  ? 1231 ALA A CB    1 
ATOM   10864 N N     . THR D 4 1235 ? 151.307 159.111 107.634 1.00 63.33  ? 1232 THR A N     1 
ATOM   10865 C CA    . THR D 4 1235 ? 150.839 160.416 107.193 1.00 63.33  ? 1232 THR A CA    1 
ATOM   10866 C C     . THR D 4 1235 ? 149.826 161.031 108.150 1.00 63.33  ? 1232 THR A C     1 
ATOM   10867 O O     . THR D 4 1235 ? 149.241 162.071 107.832 1.00 63.33  ? 1232 THR A O     1 
ATOM   10868 C CB    . THR D 4 1235 ? 150.238 160.317 105.789 1.00 63.33  ? 1232 THR A CB    1 
ATOM   10869 O OG1   . THR D 4 1235 ? 149.909 161.628 105.314 1.00 63.33  ? 1232 THR A OG1   1 
ATOM   10870 C CG2   . THR D 4 1235 ? 148.985 159.461 105.806 1.00 63.33  ? 1232 THR A CG2   1 
ATOM   10871 N N     . GLY D 4 1236 ? 149.610 160.418 109.310 1.00 61.55  ? 1233 GLY A N     1 
ATOM   10872 C CA    . GLY D 4 1236 ? 148.658 160.952 110.271 1.00 61.55  ? 1233 GLY A CA    1 
ATOM   10873 C C     . GLY D 4 1236 ? 147.230 160.963 109.774 1.00 61.55  ? 1233 GLY A C     1 
ATOM   10874 O O     . GLY D 4 1236 ? 146.520 161.961 109.949 1.00 61.55  ? 1233 GLY A O     1 
ATOM   10875 N N     . GLU D 4 1237 ? 146.790 159.871 109.154 1.00 55.59  ? 1234 GLU A N     1 
ATOM   10876 C CA    . GLU D 4 1237 ? 145.457 159.769 108.579 1.00 55.59  ? 1234 GLU A CA    1 
ATOM   10877 C C     . GLU D 4 1237 ? 144.675 158.686 109.306 1.00 55.59  ? 1234 GLU A C     1 
ATOM   10878 O O     . GLU D 4 1237 ? 145.174 157.571 109.489 1.00 55.59  ? 1234 GLU A O     1 
ATOM   10879 C CB    . GLU D 4 1237 ? 145.532 159.459 107.082 1.00 55.59  ? 1234 GLU A CB    1 
ATOM   10880 C CG    . GLU D 4 1237 ? 144.217 159.610 106.344 1.00 55.59  ? 1234 GLU A CG    1 
ATOM   10881 C CD    . GLU D 4 1237 ? 144.414 159.936 104.877 1.00 55.59  ? 1234 GLU A CD    1 
ATOM   10882 O OE1   . GLU D 4 1237 ? 145.413 159.466 104.293 1.00 55.59  ? 1234 GLU A OE1   1 
ATOM   10883 O OE2   . GLU D 4 1237 ? 143.571 160.661 104.308 1.00 55.59  ? 1234 GLU A OE2   1 
ATOM   10884 N N     . ASP D 4 1238 ? 143.454 159.018 109.721 1.00 50.26  ? 1235 ASP A N     1 
ATOM   10885 C CA    . ASP D 4 1238 ? 142.577 158.052 110.380 1.00 50.26  ? 1235 ASP A CA    1 
ATOM   10886 C C     . ASP D 4 1238 ? 141.148 158.545 110.212 1.00 50.26  ? 1235 ASP A C     1 
ATOM   10887 O O     . ASP D 4 1238 ? 140.784 159.583 110.773 1.00 50.26  ? 1235 ASP A O     1 
ATOM   10888 C CB    . ASP D 4 1238 ? 142.938 157.897 111.851 1.00 50.26  ? 1235 ASP A CB    1 
ATOM   10889 C CG    . ASP D 4 1238 ? 142.061 156.888 112.561 1.00 50.26  ? 1235 ASP A CG    1 
ATOM   10890 O OD1   . ASP D 4 1238 ? 142.343 155.676 112.460 1.00 50.26  ? 1235 ASP A OD1   1 
ATOM   10891 O OD2   . ASP D 4 1238 ? 141.086 157.305 113.219 1.00 50.26  ? 1235 ASP A OD2   1 
ATOM   10892 N N     . TYR D 4 1239 ? 140.348 157.810 109.447 1.00 50.26  ? 1236 TYR A N     1 
ATOM   10893 C CA    . TYR D 4 1239 ? 139.003 158.252 109.112 1.00 50.26  ? 1236 TYR A CA    1 
ATOM   10894 C C     . TYR D 4 1239 ? 138.175 157.044 108.705 1.00 50.26  ? 1236 TYR A C     1 
ATOM   10895 O O     . TYR D 4 1239 ? 138.705 155.963 108.436 1.00 50.26  ? 1236 TYR A O     1 
ATOM   10896 C CB    . TYR D 4 1239 ? 139.027 159.294 107.990 1.00 50.26  ? 1236 TYR A CB    1 
ATOM   10897 C CG    . TYR D 4 1239 ? 139.448 158.735 106.651 1.00 50.26  ? 1236 TYR A CG    1 
ATOM   10898 C CD1   . TYR D 4 1239 ? 140.785 158.504 106.364 1.00 50.26  ? 1236 TYR A CD1   1 
ATOM   10899 C CD2   . TYR D 4 1239 ? 138.508 158.436 105.676 1.00 50.26  ? 1236 TYR A CD2   1 
ATOM   10900 C CE1   . TYR D 4 1239 ? 141.174 157.992 105.144 1.00 50.26  ? 1236 TYR A CE1   1 
ATOM   10901 C CE2   . TYR D 4 1239 ? 138.889 157.924 104.453 1.00 50.26  ? 1236 TYR A CE2   1 
ATOM   10902 C CZ    . TYR D 4 1239 ? 140.222 157.704 104.194 1.00 50.26  ? 1236 TYR A CZ    1 
ATOM   10903 O OH    . TYR D 4 1239 ? 140.606 157.194 102.978 1.00 50.26  ? 1236 TYR A OH    1 
ATOM   10904 N N     . ILE D 4 1240 ? 136.861 157.244 108.662 1.00 50.26  ? 1237 ILE A N     1 
ATOM   10905 C CA    . ILE D 4 1240 ? 135.925 156.248 108.159 1.00 50.26  ? 1237 ILE A CA    1 
ATOM   10906 C C     . ILE D 4 1240 ? 135.100 156.884 107.051 1.00 50.26  ? 1237 ILE A C     1 
ATOM   10907 O O     . ILE D 4 1240 ? 134.643 158.025 107.177 1.00 50.26  ? 1237 ILE A O     1 
ATOM   10908 C CB    . ILE D 4 1240 ? 135.012 155.690 109.271 1.00 50.26  ? 1237 ILE A CB    1 
ATOM   10909 C CG1   . ILE D 4 1240 ? 134.251 156.815 109.965 1.00 50.26  ? 1237 ILE A CG1   1 
ATOM   10910 C CG2   . ILE D 4 1240 ? 135.824 154.907 110.286 1.00 50.26  ? 1237 ILE A CG2   1 
ATOM   10911 C CD1   . ILE D 4 1240 ? 133.131 156.326 110.833 1.00 50.26  ? 1237 ILE A CD1   1 
ATOM   10912 N N     . ASN D 4 1241 ? 134.935 156.155 105.952 1.00 50.26  ? 1238 ASN A N     1 
ATOM   10913 C CA    . ASN D 4 1241 ? 134.143 156.609 104.820 1.00 50.26  ? 1238 ASN A CA    1 
ATOM   10914 C C     . ASN D 4 1241 ? 133.022 155.612 104.573 1.00 50.26  ? 1238 ASN A C     1 
ATOM   10915 O O     . ASN D 4 1241 ? 133.272 154.410 104.441 1.00 50.26  ? 1238 ASN A O     1 
ATOM   10916 C CB    . ASN D 4 1241 ? 135.008 156.767 103.568 1.00 50.26  ? 1238 ASN A CB    1 
ATOM   10917 C CG    . ASN D 4 1241 ? 134.288 157.492 102.450 1.00 50.26  ? 1238 ASN A CG    1 
ATOM   10918 O OD1   . ASN D 4 1241 ? 133.119 157.851 102.578 1.00 50.26  ? 1238 ASN A OD1   1 
ATOM   10919 N ND2   . ASN D 4 1241 ? 134.987 157.716 101.345 1.00 50.26  ? 1238 ASN A ND2   1 
ATOM   10920 N N     . SER D 4 1242 ? 131.799 156.110 104.518 1.00 50.26  ? 1239 SER A N     1 
ATOM   10921 C CA    . SER D 4 1242 ? 130.646 155.250 104.293 1.00 50.26  ? 1239 SER A CA    1 
ATOM   10922 C C     . SER D 4 1242 ? 130.554 154.869 102.821 1.00 50.26  ? 1239 SER A C     1 
ATOM   10923 O O     . SER D 4 1242 ? 130.593 155.749 101.956 1.00 50.26  ? 1239 SER A O     1 
ATOM   10924 C CB    . SER D 4 1242 ? 129.365 155.946 104.724 1.00 50.26  ? 1239 SER A CB    1 
ATOM   10925 O OG    . SER D 4 1242 ? 128.241 155.123 104.474 1.00 50.26  ? 1239 SER A OG    1 
ATOM   10926 N N     . PRO D 4 1243 ? 130.435 153.581 102.497 1.00 50.26  ? 1240 PRO A N     1 
ATOM   10927 C CA    . PRO D 4 1243 ? 130.236 153.179 101.102 1.00 50.26  ? 1240 PRO A CA    1 
ATOM   10928 C C     . PRO D 4 1243 ? 128.786 153.213 100.649 1.00 50.26  ? 1240 PRO A C     1 
ATOM   10929 O O     . PRO D 4 1243 ? 128.508 152.839 99.505  1.00 50.26  ? 1240 PRO A O     1 
ATOM   10930 C CB    . PRO D 4 1243 ? 130.780 151.747 101.089 1.00 50.26  ? 1240 PRO A CB    1 
ATOM   10931 C CG    . PRO D 4 1243 ? 130.481 151.239 102.455 1.00 50.26  ? 1240 PRO A CG    1 
ATOM   10932 C CD    . PRO D 4 1243 ? 130.540 152.420 103.396 1.00 50.26  ? 1240 PRO A CD    1 
ATOM   10933 N N     . VAL D 4 1244 ? 127.858 153.646 101.501 1.00 50.26  ? 1241 VAL A N     1 
ATOM   10934 C CA    . VAL D 4 1244 ? 126.440 153.656 101.175 1.00 50.26  ? 1241 VAL A CA    1 
ATOM   10935 C C     . VAL D 4 1244 ? 125.851 155.008 101.552 1.00 50.26  ? 1241 VAL A C     1 
ATOM   10936 O O     . VAL D 4 1244 ? 126.371 155.714 102.421 1.00 50.26  ? 1241 VAL A O     1 
ATOM   10937 C CB    . VAL D 4 1244 ? 125.688 152.506 101.884 1.00 50.26  ? 1241 VAL A CB    1 
ATOM   10938 C CG1   . VAL D 4 1244 ? 125.501 152.817 103.359 1.00 50.26  ? 1241 VAL A CG1   1 
ATOM   10939 C CG2   . VAL D 4 1244 ? 124.356 152.236 101.207 1.00 50.26  ? 1241 VAL A CG2   1 
ATOM   10940 N N     . ARG D 4 1245 ? 124.760 155.370 100.883 1.00 50.26  ? 1242 ARG A N     1 
ATOM   10941 C CA    . ARG D 4 1245 ? 124.099 156.648 101.101 1.00 50.26  ? 1242 ARG A CA    1 
ATOM   10942 C C     . ARG D 4 1245 ? 122.984 156.512 102.129 1.00 50.26  ? 1242 ARG A C     1 
ATOM   10943 O O     . ARG D 4 1245 ? 122.347 155.462 102.250 1.00 50.26  ? 1242 ARG A O     1 
ATOM   10944 C CB    . ARG D 4 1245 ? 123.523 157.190 99.792  1.00 50.26  ? 1242 ARG A CB    1 
ATOM   10945 C CG    . ARG D 4 1245 ? 124.527 157.296 98.660  1.00 50.26  ? 1242 ARG A CG    1 
ATOM   10946 C CD    . ARG D 4 1245 ? 123.831 157.496 97.325  1.00 50.26  ? 1242 ARG A CD    1 
ATOM   10947 N NE    . ARG D 4 1245 ? 124.769 157.860 96.271  1.00 50.26  ? 1242 ARG A NE    1 
ATOM   10948 C CZ    . ARG D 4 1245 ? 125.233 159.085 96.070  1.00 50.26  ? 1242 ARG A CZ    1 
ATOM   10949 N NH1   . ARG D 4 1245 ? 124.869 160.097 96.840  1.00 50.26  ? 1242 ARG A NH1   1 
ATOM   10950 N NH2   . ARG D 4 1245 ? 126.084 159.301 95.071  1.00 50.26  ? 1242 ARG A NH2   1 
ATOM   10951 N N     . ASP D 4 1246 ? 122.750 157.591 102.868 1.00 50.26  ? 1243 ASP A N     1 
ATOM   10952 C CA    . ASP D 4 1246 ? 121.663 157.645 103.832 1.00 50.26  ? 1243 ASP A CA    1 
ATOM   10953 C C     . ASP D 4 1246 ? 120.418 158.222 103.159 1.00 50.26  ? 1243 ASP A C     1 
ATOM   10954 O O     . ASP D 4 1246 ? 120.372 158.399 101.939 1.00 50.26  ? 1243 ASP A O     1 
ATOM   10955 C CB    . ASP D 4 1246 ? 122.085 158.450 105.059 1.00 50.26  ? 1243 ASP A CB    1 
ATOM   10956 C CG    . ASP D 4 1246 ? 122.044 159.945 104.819 1.00 50.26  ? 1243 ASP A CG    1 
ATOM   10957 O OD1   . ASP D 4 1246 ? 122.542 160.394 103.767 1.00 50.26  ? 1243 ASP A OD1   1 
ATOM   10958 O OD2   . ASP D 4 1246 ? 121.512 160.671 105.685 1.00 50.26  ? 1243 ASP A OD2   1 
ATOM   10959 N N     . LEU D 4 1247 ? 119.385 158.519 103.953 1.00 50.26  ? 1244 LEU A N     1 
ATOM   10960 C CA    . LEU D 4 1247 ? 118.165 159.087 103.388 1.00 50.26  ? 1244 LEU A CA    1 
ATOM   10961 C C     . LEU D 4 1247 ? 118.408 160.473 102.806 1.00 50.26  ? 1244 LEU A C     1 
ATOM   10962 O O     . LEU D 4 1247 ? 117.715 160.882 101.868 1.00 50.26  ? 1244 LEU A O     1 
ATOM   10963 C CB    . LEU D 4 1247 ? 117.061 159.126 104.449 1.00 50.26  ? 1244 LEU A CB    1 
ATOM   10964 C CG    . LEU D 4 1247 ? 117.271 159.901 105.754 1.00 50.26  ? 1244 LEU A CG    1 
ATOM   10965 C CD1   . LEU D 4 1247 ? 116.887 161.369 105.618 1.00 50.26  ? 1244 LEU A CD1   1 
ATOM   10966 C CD2   . LEU D 4 1247 ? 116.491 159.247 106.883 1.00 50.26  ? 1244 LEU A CD2   1 
ATOM   10967 N N     . ASN D 4 1248 ? 119.381 161.209 103.347 1.00 50.26  ? 1245 ASN A N     1 
ATOM   10968 C CA    . ASN D 4 1248 ? 119.731 162.510 102.790 1.00 50.26  ? 1245 ASN A CA    1 
ATOM   10969 C C     . ASN D 4 1248 ? 120.345 162.394 101.401 1.00 50.26  ? 1245 ASN A C     1 
ATOM   10970 O O     . ASN D 4 1248 ? 120.333 163.373 100.647 1.00 50.26  ? 1245 ASN A O     1 
ATOM   10971 C CB    . ASN D 4 1248 ? 120.693 163.240 103.730 1.00 50.26  ? 1245 ASN A CB    1 
ATOM   10972 C CG    . ASN D 4 1248 ? 120.931 164.680 103.320 1.00 50.26  ? 1245 ASN A CG    1 
ATOM   10973 O OD1   . ASN D 4 1248 ? 121.823 164.971 102.524 1.00 50.26  ? 1245 ASN A OD1   1 
ATOM   10974 N ND2   . ASN D 4 1248 ? 120.134 165.590 103.865 1.00 50.26  ? 1245 ASN A ND2   1 
ATOM   10975 N N     . GLY D 4 1249 ? 120.870 161.226 101.045 1.00 50.26  ? 1246 GLY A N     1 
ATOM   10976 C CA    . GLY D 4 1249 ? 121.456 161.018 99.739  1.00 50.26  ? 1246 GLY A CA    1 
ATOM   10977 C C     . GLY D 4 1249 ? 122.947 161.243 99.650  1.00 50.26  ? 1246 GLY A C     1 
ATOM   10978 O O     . GLY D 4 1249 ? 123.474 161.341 98.536  1.00 50.26  ? 1246 GLY A O     1 
ATOM   10979 N N     . VAL D 4 1250 ? 123.646 161.328 100.779 1.00 50.26  ? 1247 VAL A N     1 
ATOM   10980 C CA    . VAL D 4 1250 ? 125.086 161.543 100.801 1.00 50.26  ? 1247 VAL A CA    1 
ATOM   10981 C C     . VAL D 4 1250 ? 125.722 160.521 101.734 1.00 50.26  ? 1247 VAL A C     1 
ATOM   10982 O O     . VAL D 4 1250 ? 125.158 160.185 102.782 1.00 50.26  ? 1247 VAL A O     1 
ATOM   10983 C CB    . VAL D 4 1250 ? 125.441 162.986 101.225 1.00 50.26  ? 1247 VAL A CB    1 
ATOM   10984 C CG1   . VAL D 4 1250 ? 125.025 163.252 102.666 1.00 50.26  ? 1247 VAL A CG1   1 
ATOM   10985 C CG2   . VAL D 4 1250 ? 126.927 163.255 101.027 1.00 50.26  ? 1247 VAL A CG2   1 
ATOM   10986 N N     . CYS D 4 1251 ? 126.880 160.004 101.337 1.00 50.26  ? 1248 CYS A N     1 
ATOM   10987 C CA    . CYS D 4 1251 ? 127.612 159.062 102.168 1.00 50.26  ? 1248 CYS A CA    1 
ATOM   10988 C C     . CYS D 4 1251 ? 128.403 159.799 103.240 1.00 50.26  ? 1248 CYS A C     1 
ATOM   10989 O O     . CYS D 4 1251 ? 128.898 160.909 103.025 1.00 50.26  ? 1248 CYS A O     1 
ATOM   10990 C CB    . CYS D 4 1251 ? 128.563 158.217 101.323 1.00 50.26  ? 1248 CYS A CB    1 
ATOM   10991 S SG    . CYS D 4 1251 ? 127.790 157.321 99.964  1.00 50.26  ? 1248 CYS A SG    1 
ATOM   10992 N N     . PHE D 4 1252 ? 128.521 159.167 104.403 1.00 50.26  ? 1249 PHE A N     1 
ATOM   10993 C CA    . PHE D 4 1252 ? 129.280 159.758 105.492 1.00 50.26  ? 1249 PHE A CA    1 
ATOM   10994 C C     . PHE D 4 1252 ? 130.761 159.829 105.145 1.00 50.26  ? 1249 PHE A C     1 
ATOM   10995 O O     . PHE D 4 1252 ? 131.310 158.954 104.472 1.00 50.26  ? 1249 PHE A O     1 
ATOM   10996 C CB    . PHE D 4 1252 ? 129.099 158.955 106.778 1.00 50.26  ? 1249 PHE A CB    1 
ATOM   10997 C CG    . PHE D 4 1252 ? 129.896 159.485 107.932 1.00 50.26  ? 1249 PHE A CG    1 
ATOM   10998 C CD1   . PHE D 4 1252 ? 129.635 160.739 108.449 1.00 50.26  ? 1249 PHE A CD1   1 
ATOM   10999 C CD2   . PHE D 4 1252 ? 130.919 158.740 108.485 1.00 50.26  ? 1249 PHE A CD2   1 
ATOM   11000 C CE1   . PHE D 4 1252 ? 130.369 161.233 109.504 1.00 50.26  ? 1249 PHE A CE1   1 
ATOM   11001 C CE2   . PHE D 4 1252 ? 131.656 159.232 109.539 1.00 50.26  ? 1249 PHE A CE2   1 
ATOM   11002 C CZ    . PHE D 4 1252 ? 131.381 160.478 110.050 1.00 50.26  ? 1249 PHE A CZ    1 
ATOM   11003 N N     . ASP D 4 1253 ? 131.407 160.892 105.614 1.00 50.26  ? 1250 ASP A N     1 
ATOM   11004 C CA    . ASP D 4 1253 ? 132.851 161.044 105.466 1.00 50.26  ? 1250 ASP A CA    1 
ATOM   11005 C C     . ASP D 4 1253 ? 133.350 161.824 106.672 1.00 50.26  ? 1250 ASP A C     1 
ATOM   11006 O O     . ASP D 4 1253 ? 133.130 163.036 106.759 1.00 50.26  ? 1250 ASP A O     1 
ATOM   11007 C CB    . ASP D 4 1253 ? 133.205 161.751 104.163 1.00 50.26  ? 1250 ASP A CB    1 
ATOM   11008 C CG    . ASP D 4 1253 ? 134.523 161.279 103.585 1.00 50.26  ? 1250 ASP A CG    1 
ATOM   11009 O OD1   . ASP D 4 1253 ? 135.218 160.489 104.256 1.00 50.26  ? 1250 ASP A OD1   1 
ATOM   11010 O OD2   . ASP D 4 1253 ? 134.864 161.696 102.458 1.00 50.26  ? 1250 ASP A OD2   1 
ATOM   11011 N N     . SER D 4 1254 ? 134.013 161.130 107.599 1.00 50.26  ? 1251 SER A N     1 
ATOM   11012 C CA    . SER D 4 1254 ? 134.483 161.774 108.820 1.00 50.26  ? 1251 SER A CA    1 
ATOM   11013 C C     . SER D 4 1254 ? 135.519 162.851 108.541 1.00 50.26  ? 1251 SER A C     1 
ATOM   11014 O O     . SER D 4 1254 ? 135.772 163.692 109.410 1.00 50.26  ? 1251 SER A O     1 
ATOM   11015 C CB    . SER D 4 1254 ? 135.063 160.732 109.774 1.00 50.26  ? 1251 SER A CB    1 
ATOM   11016 O OG    . SER D 4 1254 ? 136.344 160.312 109.345 1.00 50.26  ? 1251 SER A OG    1 
ATOM   11017 N N     . ARG D 4 1255 ? 136.126 162.844 107.354 1.00 50.26  ? 1252 ARG A N     1 
ATOM   11018 C CA    . ARG D 4 1255 ? 137.072 163.891 106.994 1.00 50.26  ? 1252 ARG A CA    1 
ATOM   11019 C C     . ARG D 4 1255 ? 136.400 165.248 106.841 1.00 50.26  ? 1252 ARG A C     1 
ATOM   11020 O O     . ARG D 4 1255 ? 137.086 166.273 106.894 1.00 50.26  ? 1252 ARG A O     1 
ATOM   11021 C CB    . ARG D 4 1255 ? 137.800 163.508 105.707 1.00 50.26  ? 1252 ARG A CB    1 
ATOM   11022 C CG    . ARG D 4 1255 ? 138.459 162.141 105.775 1.00 50.26  ? 1252 ARG A CG    1 
ATOM   11023 C CD    . ARG D 4 1255 ? 139.107 161.760 104.458 1.00 50.26  ? 1252 ARG A CD    1 
ATOM   11024 N NE    . ARG D 4 1255 ? 138.119 161.421 103.442 1.00 50.26  ? 1252 ARG A NE    1 
ATOM   11025 C CZ    . ARG D 4 1255 ? 138.415 160.924 102.250 1.00 50.26  ? 1252 ARG A CZ    1 
ATOM   11026 N NH1   . ARG D 4 1255 ? 139.665 160.691 101.890 1.00 50.26  ? 1252 ARG A NH1   1 
ATOM   11027 N NH2   . ARG D 4 1255 ? 137.431 160.657 101.396 1.00 50.26  ? 1252 ARG A NH2   1 
ATOM   11028 N N     . PHE D 4 1256 ? 135.077 165.279 106.656 1.00 50.26  ? 1253 PHE A N     1 
ATOM   11029 C CA    . PHE D 4 1256 ? 134.357 166.546 106.618 1.00 50.26  ? 1253 PHE A CA    1 
ATOM   11030 C C     . PHE D 4 1256 ? 134.362 167.250 107.967 1.00 50.26  ? 1253 PHE A C     1 
ATOM   11031 O O     . PHE D 4 1256 ? 134.119 168.460 108.019 1.00 50.26  ? 1253 PHE A O     1 
ATOM   11032 C CB    . PHE D 4 1256 ? 132.916 166.322 106.160 1.00 50.26  ? 1253 PHE A CB    1 
ATOM   11033 C CG    . PHE D 4 1256 ? 132.765 166.200 104.673 1.00 50.26  ? 1253 PHE A CG    1 
ATOM   11034 C CD1   . PHE D 4 1256 ? 133.232 167.195 103.833 1.00 50.26  ? 1253 PHE A CD1   1 
ATOM   11035 C CD2   . PHE D 4 1256 ? 132.151 165.094 104.114 1.00 50.26  ? 1253 PHE A CD2   1 
ATOM   11036 C CE1   . PHE D 4 1256 ? 133.094 167.086 102.465 1.00 50.26  ? 1253 PHE A CE1   1 
ATOM   11037 C CE2   . PHE D 4 1256 ? 132.010 164.979 102.747 1.00 50.26  ? 1253 PHE A CE2   1 
ATOM   11038 C CZ    . PHE D 4 1256 ? 132.482 165.977 101.921 1.00 50.26  ? 1253 PHE A CZ    1 
ATOM   11039 N N     . GLN D 4 1257 ? 134.630 166.518 109.050 1.00 50.26  ? 1254 GLN A N     1 
ATOM   11040 C CA    . GLN D 4 1257 ? 134.724 167.084 110.396 1.00 50.26  ? 1254 GLN A CA    1 
ATOM   11041 C C     . GLN D 4 1257 ? 133.448 167.826 110.788 1.00 50.26  ? 1254 GLN A C     1 
ATOM   11042 O O     . GLN D 4 1257 ? 133.492 168.918 111.356 1.00 50.26  ? 1254 GLN A O     1 
ATOM   11043 C CB    . GLN D 4 1257 ? 135.946 167.994 110.527 1.00 50.26  ? 1254 GLN A CB    1 
ATOM   11044 C CG    . GLN D 4 1257 ? 137.260 167.313 110.182 1.00 50.26  ? 1254 GLN A CG    1 
ATOM   11045 C CD    . GLN D 4 1257 ? 137.791 166.457 111.316 1.00 50.26  ? 1254 GLN A CD    1 
ATOM   11046 O OE1   . GLN D 4 1257 ? 138.665 166.881 112.070 1.00 50.26  ? 1254 GLN A OE1   1 
ATOM   11047 N NE2   . GLN D 4 1257 ? 137.268 165.243 111.438 1.00 50.26  ? 1254 GLN A NE2   1 
ATOM   11048 N N     . ASN D 4 1258 ? 132.305 167.230 110.480 1.00 50.26  ? 1255 ASN A N     1 
ATOM   11049 C CA    . ASN D 4 1258 ? 131.032 167.804 110.895 1.00 50.26  ? 1255 ASN A CA    1 
ATOM   11050 C C     . ASN D 4 1258 ? 130.895 167.695 112.410 1.00 50.26  ? 1255 ASN A C     1 
ATOM   11051 O O     . ASN D 4 1258 ? 131.054 166.601 112.962 1.00 50.26  ? 1255 ASN A O     1 
ATOM   11052 C CB    . ASN D 4 1258 ? 129.875 167.089 110.202 1.00 50.26  ? 1255 ASN A CB    1 
ATOM   11053 C CG    . ASN D 4 1258 ? 128.650 167.965 110.059 1.00 50.26  ? 1255 ASN A CG    1 
ATOM   11054 O OD1   . ASN D 4 1258 ? 128.739 169.190 110.111 1.00 50.26  ? 1255 ASN A OD1   1 
ATOM   11055 N ND2   . ASN D 4 1258 ? 127.494 167.340 109.873 1.00 50.26  ? 1255 ASN A ND2   1 
ATOM   11056 N N     . PRO D 4 1259 ? 130.616 168.795 113.113 1.00 50.26  ? 1256 PRO A N     1 
ATOM   11057 C CA    . PRO D 4 1259 ? 130.561 168.728 114.584 1.00 50.26  ? 1256 PRO A CA    1 
ATOM   11058 C C     . PRO D 4 1259 ? 129.503 167.782 115.118 1.00 50.26  ? 1256 PRO A C     1 
ATOM   11059 O O     . PRO D 4 1259 ? 129.667 167.243 116.220 1.00 50.26  ? 1256 PRO A O     1 
ATOM   11060 C CB    . PRO D 4 1259 ? 130.274 170.181 114.989 1.00 50.26  ? 1256 PRO A CB    1 
ATOM   11061 C CG    . PRO D 4 1259 ? 130.687 171.004 113.813 1.00 50.26  ? 1256 PRO A CG    1 
ATOM   11062 C CD    . PRO D 4 1259 ? 130.411 170.162 112.611 1.00 50.26  ? 1256 PRO A CD    1 
ATOM   11063 N N     . GLU D 4 1260 ? 128.421 167.562 114.378 1.00 50.26  ? 1257 GLU A N     1 
ATOM   11064 C CA    . GLU D 4 1260 ? 127.317 166.735 114.842 1.00 50.26  ? 1257 GLU A CA    1 
ATOM   11065 C C     . GLU D 4 1260 ? 127.535 165.251 114.568 1.00 50.26  ? 1257 GLU A C     1 
ATOM   11066 O O     . GLU D 4 1260 ? 126.707 164.431 114.974 1.00 50.26  ? 1257 GLU A O     1 
ATOM   11067 C CB    . GLU D 4 1260 ? 126.010 167.210 114.195 1.00 50.26  ? 1257 GLU A CB    1 
ATOM   11068 C CG    . GLU D 4 1260 ? 124.746 166.847 114.960 1.00 50.26  ? 1257 GLU A CG    1 
ATOM   11069 C CD    . GLU D 4 1260 ? 124.042 165.636 114.385 1.00 50.26  ? 1257 GLU A CD    1 
ATOM   11070 O OE1   . GLU D 4 1260 ? 124.113 165.437 113.155 1.00 50.26  ? 1257 GLU A OE1   1 
ATOM   11071 O OE2   . GLU D 4 1260 ? 123.420 164.882 115.162 1.00 50.26  ? 1257 GLU A OE2   1 
ATOM   11072 N N     . TRP D 4 1261 ? 128.627 164.888 113.913 1.00 50.26  ? 1258 TRP A N     1 
ATOM   11073 C CA    . TRP D 4 1261 ? 128.938 163.512 113.567 1.00 50.26  ? 1258 TRP A CA    1 
ATOM   11074 C C     . TRP D 4 1261 ? 130.353 163.187 114.017 1.00 50.26  ? 1258 TRP A C     1 
ATOM   11075 O O     . TRP D 4 1261 ? 131.165 164.093 114.232 1.00 50.26  ? 1258 TRP A O     1 
ATOM   11076 C CB    . TRP D 4 1261 ? 128.784 163.284 112.055 1.00 50.26  ? 1258 TRP A CB    1 
ATOM   11077 C CG    . TRP D 4 1261 ? 127.370 163.441 111.596 1.00 50.26  ? 1258 TRP A CG    1 
ATOM   11078 C CD1   . TRP D 4 1261 ? 126.903 164.325 110.671 1.00 50.26  ? 1258 TRP A CD1   1 
ATOM   11079 C CD2   . TRP D 4 1261 ? 126.231 162.702 112.056 1.00 50.26  ? 1258 TRP A CD2   1 
ATOM   11080 N NE1   . TRP D 4 1261 ? 125.546 164.179 110.520 1.00 50.26  ? 1258 TRP A NE1   1 
ATOM   11081 C CE2   . TRP D 4 1261 ? 125.110 163.189 111.359 1.00 50.26  ? 1258 TRP A CE2   1 
ATOM   11082 C CE3   . TRP D 4 1261 ? 126.053 161.672 112.985 1.00 50.26  ? 1258 TRP A CE3   1 
ATOM   11083 C CZ2   . TRP D 4 1261 ? 123.828 162.685 111.565 1.00 50.26  ? 1258 TRP A CZ2   1 
ATOM   11084 C CZ3   . TRP D 4 1261 ? 124.781 161.173 113.186 1.00 50.26  ? 1258 TRP A CZ3   1 
ATOM   11085 C CH2   . TRP D 4 1261 ? 123.685 161.678 112.479 1.00 50.26  ? 1258 TRP A CH2   1 
ATOM   11086 N N     . PRO D 4 1262 ? 130.673 161.904 114.196 1.00 50.26  ? 1259 PRO A N     1 
ATOM   11087 C CA    . PRO D 4 1262 ? 131.988 161.542 114.738 1.00 50.26  ? 1259 PRO A CA    1 
ATOM   11088 C C     . PRO D 4 1262 ? 133.132 162.097 113.901 1.00 50.26  ? 1259 PRO A C     1 
ATOM   11089 O O     . PRO D 4 1262 ? 133.066 162.146 112.671 1.00 50.26  ? 1259 PRO A O     1 
ATOM   11090 C CB    . PRO D 4 1262 ? 131.967 160.011 114.716 1.00 50.26  ? 1259 PRO A CB    1 
ATOM   11091 C CG    . PRO D 4 1262 ? 130.536 159.663 114.825 1.00 50.26  ? 1259 PRO A CG    1 
ATOM   11092 C CD    . PRO D 4 1262 ? 129.787 160.732 114.087 1.00 50.26  ? 1259 PRO A CD    1 
ATOM   11093 N N     . MET D 4 1263 ? 134.189 162.528 114.593 1.00 50.26  ? 1260 MET A N     1 
ATOM   11094 C CA    . MET D 4 1263 ? 135.327 163.147 113.920 1.00 50.26  ? 1260 MET A CA    1 
ATOM   11095 C C     . MET D 4 1263 ? 136.182 162.117 113.195 1.00 50.26  ? 1260 MET A C     1 
ATOM   11096 O O     . MET D 4 1263 ? 136.648 162.368 112.077 1.00 50.26  ? 1260 MET A O     1 
ATOM   11097 C CB    . MET D 4 1263 ? 136.174 163.920 114.930 1.00 50.26  ? 1260 MET A CB    1 
ATOM   11098 C CG    . MET D 4 1263 ? 135.617 165.281 115.305 1.00 50.26  ? 1260 MET A CG    1 
ATOM   11099 S SD    . MET D 4 1263 ? 135.050 166.213 113.874 1.00 50.26  ? 1260 MET A SD    1 
ATOM   11100 C CE    . MET D 4 1263 ? 133.923 167.362 114.654 1.00 50.26  ? 1260 MET A CE    1 
ATOM   11101 N N     . ASP D 4 1264 ? 136.413 160.962 113.811 1.00 50.26  ? 1261 ASP A N     1 
ATOM   11102 C CA    . ASP D 4 1264 ? 137.280 159.946 113.227 1.00 50.26  ? 1261 ASP A CA    1 
ATOM   11103 C C     . ASP D 4 1264 ? 136.785 158.570 113.658 1.00 50.26  ? 1261 ASP A C     1 
ATOM   11104 O O     . ASP D 4 1264 ? 135.667 158.421 114.159 1.00 50.26  ? 1261 ASP A O     1 
ATOM   11105 C CB    . ASP D 4 1264 ? 138.741 160.192 113.624 1.00 50.26  ? 1261 ASP A CB    1 
ATOM   11106 C CG    . ASP D 4 1264 ? 138.896 160.551 115.085 1.00 50.26  ? 1261 ASP A CG    1 
ATOM   11107 O OD1   . ASP D 4 1264 ? 137.868 160.794 115.748 1.00 50.26  ? 1261 ASP A OD1   1 
ATOM   11108 O OD2   . ASP D 4 1264 ? 140.045 160.588 115.571 1.00 50.26  ? 1261 ASP A OD2   1 
ATOM   11109 N N     . ALA D 4 1265 ? 137.625 157.554 113.448 1.00 50.26  ? 1262 ALA A N     1 
ATOM   11110 C CA    . ALA D 4 1265 ? 137.213 156.180 113.716 1.00 50.26  ? 1262 ALA A CA    1 
ATOM   11111 C C     . ALA D 4 1265 ? 137.030 155.927 115.207 1.00 50.26  ? 1262 ALA A C     1 
ATOM   11112 O O     . ALA D 4 1265 ? 136.080 155.247 115.615 1.00 50.26  ? 1262 ALA A O     1 
ATOM   11113 C CB    . ALA D 4 1265 ? 138.231 155.209 113.127 1.00 50.26  ? 1262 ALA A CB    1 
ATOM   11114 N N     . ASP D 4 1266 ? 137.935 156.450 116.037 1.00 50.26  ? 1263 ASP A N     1 
ATOM   11115 C CA    . ASP D 4 1266 ? 137.755 156.336 117.479 1.00 50.26  ? 1263 ASP A CA    1 
ATOM   11116 C C     . ASP D 4 1266 ? 136.502 157.070 117.932 1.00 50.26  ? 1263 ASP A C     1 
ATOM   11117 O O     . ASP D 4 1266 ? 135.809 156.617 118.854 1.00 50.26  ? 1263 ASP A O     1 
ATOM   11118 C CB    . ASP D 4 1266 ? 138.988 156.872 118.203 1.00 50.26  ? 1263 ASP A CB    1 
ATOM   11119 C CG    . ASP D 4 1266 ? 140.280 156.375 117.590 1.00 50.26  ? 1263 ASP A CG    1 
ATOM   11120 O OD1   . ASP D 4 1266 ? 140.304 155.227 117.101 1.00 50.26  ? 1263 ASP A OD1   1 
ATOM   11121 O OD2   . ASP D 4 1266 ? 141.273 157.132 117.596 1.00 50.26  ? 1263 ASP A OD2   1 
ATOM   11122 N N     . ALA D 4 1267 ? 136.194 158.199 117.291 1.00 50.26  ? 1264 ALA A N     1 
ATOM   11123 C CA    . ALA D 4 1267 ? 134.930 158.873 117.552 1.00 50.26  ? 1264 ALA A CA    1 
ATOM   11124 C C     . ALA D 4 1267 ? 133.757 157.976 117.202 1.00 50.26  ? 1264 ALA A C     1 
ATOM   11125 O O     . ALA D 4 1267 ? 132.768 157.926 117.937 1.00 50.26  ? 1264 ALA A O     1 
ATOM   11126 C CB    . ALA D 4 1267 ? 134.858 160.181 116.769 1.00 50.26  ? 1264 ALA A CB    1 
ATOM   11127 N N     . ASN D 4 1268 ? 133.851 157.255 116.085 1.00 50.26  ? 1265 ASN A N     1 
ATOM   11128 C CA    . ASN D 4 1268 ? 132.792 156.324 115.718 1.00 50.26  ? 1265 ASN A CA    1 
ATOM   11129 C C     . ASN D 4 1268 ? 132.622 155.245 116.778 1.00 50.26  ? 1265 ASN A C     1 
ATOM   11130 O O     . ASN D 4 1268 ? 131.494 154.921 117.169 1.00 50.26  ? 1265 ASN A O     1 
ATOM   11131 C CB    . ASN D 4 1268 ? 133.099 155.697 114.361 1.00 50.26  ? 1265 ASN A CB    1 
ATOM   11132 C CG    . ASN D 4 1268 ? 131.889 155.045 113.737 1.00 50.26  ? 1265 ASN A CG    1 
ATOM   11133 O OD1   . ASN D 4 1268 ? 130.846 155.675 113.578 1.00 50.26  ? 1265 ASN A OD1   1 
ATOM   11134 N ND2   . ASN D 4 1268 ? 132.023 153.776 113.374 1.00 50.26  ? 1265 ASN A ND2   1 
ATOM   11135 N N     . GLY D 4 1269 ? 133.733 154.688 117.263 1.00 50.26  ? 1266 GLY A N     1 
ATOM   11136 C CA    . GLY D 4 1269 ? 133.641 153.641 118.269 1.00 50.26  ? 1266 GLY A CA    1 
ATOM   11137 C C     . GLY D 4 1269 ? 133.017 154.125 119.563 1.00 50.26  ? 1266 GLY A C     1 
ATOM   11138 O O     . GLY D 4 1269 ? 132.111 153.489 120.110 1.00 50.26  ? 1266 GLY A O     1 
ATOM   11139 N N     . ALA D 4 1270 ? 133.482 155.273 120.063 1.00 50.26  ? 1267 ALA A N     1 
ATOM   11140 C CA    . ALA D 4 1270 ? 132.926 155.812 121.300 1.00 50.26  ? 1267 ALA A CA    1 
ATOM   11141 C C     . ALA D 4 1270 ? 131.462 156.196 121.127 1.00 50.26  ? 1267 ALA A C     1 
ATOM   11142 O O     . ALA D 4 1270 ? 130.633 155.938 122.010 1.00 50.26  ? 1267 ALA A O     1 
ATOM   11143 C CB    . ALA D 4 1270 ? 133.748 157.012 121.764 1.00 50.26  ? 1267 ALA A CB    1 
ATOM   11144 N N     . TYR D 4 1271 ? 131.124 156.802 119.988 1.00 50.26  ? 1268 TYR A N     1 
ATOM   11145 C CA    . TYR D 4 1271 ? 129.752 157.215 119.728 1.00 50.26  ? 1268 TYR A CA    1 
ATOM   11146 C C     . TYR D 4 1271 ? 128.821 156.013 119.674 1.00 50.26  ? 1268 TYR A C     1 
ATOM   11147 O O     . TYR D 4 1271 ? 127.721 156.046 120.235 1.00 50.26  ? 1268 TYR A O     1 
ATOM   11148 C CB    . TYR D 4 1271 ? 129.715 158.009 118.422 1.00 50.26  ? 1268 TYR A CB    1 
ATOM   11149 C CG    . TYR D 4 1271 ? 128.344 158.342 117.891 1.00 50.26  ? 1268 TYR A CG    1 
ATOM   11150 C CD1   . TYR D 4 1271 ? 127.557 159.302 118.504 1.00 50.26  ? 1268 TYR A CD1   1 
ATOM   11151 C CD2   . TYR D 4 1271 ? 127.851 157.721 116.755 1.00 50.26  ? 1268 TYR A CD2   1 
ATOM   11152 C CE1   . TYR D 4 1271 ? 126.312 159.624 118.011 1.00 50.26  ? 1268 TYR A CE1   1 
ATOM   11153 C CE2   . TYR D 4 1271 ? 126.606 158.033 116.256 1.00 50.26  ? 1268 TYR A CE2   1 
ATOM   11154 C CZ    . TYR D 4 1271 ? 125.840 158.984 116.888 1.00 50.26  ? 1268 TYR A CZ    1 
ATOM   11155 O OH    . TYR D 4 1271 ? 124.596 159.299 116.396 1.00 50.26  ? 1268 TYR A OH    1 
ATOM   11156 N N     . HIS D 4 1272 ? 129.250 154.927 119.034 1.00 50.26  ? 1269 HIS A N     1 
ATOM   11157 C CA    . HIS D 4 1272 ? 128.378 153.763 118.958 1.00 50.26  ? 1269 HIS A CA    1 
ATOM   11158 C C     . HIS D 4 1272 ? 128.321 152.998 120.273 1.00 50.26  ? 1269 HIS A C     1 
ATOM   11159 O O     . HIS D 4 1272 ? 127.306 152.357 120.562 1.00 50.26  ? 1269 HIS A O     1 
ATOM   11160 C CB    . HIS D 4 1272 ? 128.815 152.857 117.812 1.00 50.26  ? 1269 HIS A CB    1 
ATOM   11161 C CG    . HIS D 4 1272 ? 128.302 153.302 116.481 1.00 50.26  ? 1269 HIS A CG    1 
ATOM   11162 N ND1   . HIS D 4 1272 ? 129.067 154.024 115.592 1.00 50.26  ? 1269 HIS A ND1   1 
ATOM   11163 C CD2   . HIS D 4 1272 ? 127.090 153.151 115.898 1.00 50.26  ? 1269 HIS A CD2   1 
ATOM   11164 C CE1   . HIS D 4 1272 ? 128.353 154.287 114.514 1.00 50.26  ? 1269 HIS A CE1   1 
ATOM   11165 N NE2   . HIS D 4 1272 ? 127.149 153.769 114.674 1.00 50.26  ? 1269 HIS A NE2   1 
ATOM   11166 N N     . ILE D 4 1273 ? 129.371 153.067 121.095 1.00 50.26  ? 1270 ILE A N     1 
ATOM   11167 C CA    . ILE D 4 1273 ? 129.251 152.557 122.459 1.00 50.26  ? 1270 ILE A CA    1 
ATOM   11168 C C     . ILE D 4 1273 ? 128.198 153.351 123.224 1.00 50.26  ? 1270 ILE A C     1 
ATOM   11169 O O     . ILE D 4 1273 ? 127.386 152.788 123.972 1.00 50.26  ? 1270 ILE A O     1 
ATOM   11170 C CB    . ILE D 4 1273 ? 130.618 152.588 123.166 1.00 50.26  ? 1270 ILE A CB    1 
ATOM   11171 C CG1   . ILE D 4 1273 ? 131.498 151.445 122.661 1.00 50.26  ? 1270 ILE A CG1   1 
ATOM   11172 C CG2   . ILE D 4 1273 ? 130.447 152.493 124.669 1.00 50.26  ? 1270 ILE A CG2   1 
ATOM   11173 C CD1   . ILE D 4 1273 ? 132.794 151.295 123.415 1.00 50.26  ? 1270 ILE A CD1   1 
ATOM   11174 N N     . ALA D 4 1274 ? 128.189 154.673 123.039 1.00 50.26  ? 1271 ALA A N     1 
ATOM   11175 C CA    . ALA D 4 1274 ? 127.165 155.499 123.671 1.00 50.26  ? 1271 ALA A CA    1 
ATOM   11176 C C     . ALA D 4 1274 ? 125.769 155.132 123.176 1.00 50.26  ? 1271 ALA A C     1 
ATOM   11177 O O     . ALA D 4 1274 ? 124.817 155.093 123.961 1.00 50.26  ? 1271 ALA A O     1 
ATOM   11178 C CB    . ALA D 4 1274 ? 127.456 156.977 123.420 1.00 50.26  ? 1271 ALA A CB    1 
ATOM   11179 N N     . LEU D 4 1275 ? 125.623 154.868 121.875 1.00 50.26  ? 1272 LEU A N     1 
ATOM   11180 C CA    . LEU D 4 1275 ? 124.326 154.428 121.356 1.00 50.26  ? 1272 LEU A CA    1 
ATOM   11181 C C     . LEU D 4 1275 ? 123.922 153.060 121.897 1.00 50.26  ? 1272 LEU A C     1 
ATOM   11182 O O     . LEU D 4 1275 ? 122.733 152.806 122.103 1.00 50.26  ? 1272 LEU A O     1 
ATOM   11183 C CB    . LEU D 4 1275 ? 124.306 154.424 119.827 1.00 50.26  ? 1272 LEU A CB    1 
ATOM   11184 C CG    . LEU D 4 1275 ? 124.003 155.734 119.095 1.00 50.26  ? 1272 LEU A CG    1 
ATOM   11185 C CD1   . LEU D 4 1275 ? 122.586 156.165 119.429 1.00 50.26  ? 1272 LEU A CD1   1 
ATOM   11186 C CD2   . LEU D 4 1275 ? 124.952 156.838 119.450 1.00 50.26  ? 1272 LEU A CD2   1 
ATOM   11187 N N     . LYS D 4 1276 ? 124.878 152.155 122.109 1.00 50.26  ? 1273 LYS A N     1 
ATOM   11188 C CA    . LYS D 4 1276 ? 124.533 150.881 122.737 1.00 50.26  ? 1273 LYS A CA    1 
ATOM   11189 C C     . LYS D 4 1276 ? 124.041 151.093 124.165 1.00 50.26  ? 1273 LYS A C     1 
ATOM   11190 O O     . LYS D 4 1276 ? 123.061 150.468 124.601 1.00 50.26  ? 1273 LYS A O     1 
ATOM   11191 C CB    . LYS D 4 1276 ? 125.732 149.936 122.715 1.00 50.26  ? 1273 LYS A CB    1 
ATOM   11192 C CG    . LYS D 4 1276 ? 125.723 148.952 121.562 1.00 50.26  ? 1273 LYS A CG    1 
ATOM   11193 C CD    . LYS D 4 1276 ? 126.996 148.129 121.534 1.00 50.26  ? 1273 LYS A CD    1 
ATOM   11194 C CE    . LYS D 4 1276 ? 126.980 147.135 120.388 1.00 50.26  ? 1273 LYS A CE    1 
ATOM   11195 N NZ    . LYS D 4 1276 ? 128.189 146.272 120.391 1.00 50.26  ? 1273 LYS A NZ    1 
ATOM   11196 N N     . GLY D 4 1277 ? 124.706 151.978 124.907 1.00 50.26  ? 1274 GLY A N     1 
ATOM   11197 C CA    . GLY D 4 1277 ? 124.217 152.325 126.232 1.00 50.26  ? 1274 GLY A CA    1 
ATOM   11198 C C     . GLY D 4 1277 ? 122.834 152.946 126.192 1.00 50.26  ? 1274 GLY A C     1 
ATOM   11199 O O     . GLY D 4 1277 ? 121.996 152.683 127.059 1.00 50.26  ? 1274 GLY A O     1 
ATOM   11200 N N     . GLN D 4 1278 ? 122.578 153.782 125.185 1.00 50.26  ? 1275 GLN A N     1 
ATOM   11201 C CA    . GLN D 4 1278 ? 121.253 154.372 125.022 1.00 50.26  ? 1275 GLN A CA    1 
ATOM   11202 C C     . GLN D 4 1278 ? 120.215 153.308 124.694 1.00 50.26  ? 1275 GLN A C     1 
ATOM   11203 O O     . GLN D 4 1278 ? 119.067 153.395 125.138 1.00 50.26  ? 1275 GLN A O     1 
ATOM   11204 C CB    . GLN D 4 1278 ? 121.288 155.445 123.935 1.00 50.26  ? 1275 GLN A CB    1 
ATOM   11205 C CG    . GLN D 4 1278 ? 119.933 156.050 123.621 1.00 50.26  ? 1275 GLN A CG    1 
ATOM   11206 C CD    . GLN D 4 1278 ? 120.022 157.518 123.269 1.00 50.26  ? 1275 GLN A CD    1 
ATOM   11207 O OE1   . GLN D 4 1278 ? 120.411 158.344 124.095 1.00 50.26  ? 1275 GLN A OE1   1 
ATOM   11208 N NE2   . GLN D 4 1278 ? 119.660 157.854 122.037 1.00 50.26  ? 1275 GLN A NE2   1 
ATOM   11209 N N     . LEU D 4 1279 ? 120.596 152.305 123.903 1.00 50.26  ? 1276 LEU A N     1 
ATOM   11210 C CA    . LEU D 4 1279 ? 119.714 151.172 123.643 1.00 50.26  ? 1276 LEU A CA    1 
ATOM   11211 C C     . LEU D 4 1279 ? 119.336 150.480 124.943 1.00 50.26  ? 1276 LEU A C     1 
ATOM   11212 O O     . LEU D 4 1279 ? 118.162 150.173 125.184 1.00 50.26  ? 1276 LEU A O     1 
ATOM   11213 C CB    . LEU D 4 1279 ? 120.400 150.188 122.691 1.00 50.26  ? 1276 LEU A CB    1 
ATOM   11214 C CG    . LEU D 4 1279 ? 119.674 148.928 122.206 1.00 50.26  ? 1276 LEU A CG    1 
ATOM   11215 C CD1   . LEU D 4 1279 ? 120.222 148.506 120.860 1.00 50.26  ? 1276 LEU A CD1   1 
ATOM   11216 C CD2   . LEU D 4 1279 ? 119.810 147.776 123.190 1.00 50.26  ? 1276 LEU A CD2   1 
ATOM   11217 N N     . LEU D 4 1280 ? 120.332 150.219 125.790 1.00 50.26  ? 1277 LEU A N     1 
ATOM   11218 C CA    . LEU D 4 1280 ? 120.061 149.578 127.074 1.00 50.26  ? 1277 LEU A CA    1 
ATOM   11219 C C     . LEU D 4 1280 ? 119.141 150.439 127.935 1.00 50.26  ? 1277 LEU A C     1 
ATOM   11220 O O     . LEU D 4 1280 ? 118.191 149.933 128.549 1.00 50.26  ? 1277 LEU A O     1 
ATOM   11221 C CB    . LEU D 4 1280 ? 121.376 149.300 127.800 1.00 50.26  ? 1277 LEU A CB    1 
ATOM   11222 C CG    . LEU D 4 1280 ? 121.456 148.023 128.631 1.00 50.26  ? 1277 LEU A CG    1 
ATOM   11223 C CD1   . LEU D 4 1280 ? 121.122 146.814 127.778 1.00 50.26  ? 1277 LEU A CD1   1 
ATOM   11224 C CD2   . LEU D 4 1280 ? 122.836 147.884 129.246 1.00 50.26  ? 1277 LEU A CD2   1 
ATOM   11225 N N     . LEU D 4 1281 ? 119.399 151.747 127.976 1.00 50.26  ? 1278 LEU A N     1 
ATOM   11226 C CA    . LEU D 4 1281 ? 118.578 152.647 128.780 1.00 50.26  ? 1278 LEU A CA    1 
ATOM   11227 C C     . LEU D 4 1281 ? 117.145 152.705 128.262 1.00 50.26  ? 1278 LEU A C     1 
ATOM   11228 O O     . LEU D 4 1281 ? 116.195 152.744 129.049 1.00 50.26  ? 1278 LEU A O     1 
ATOM   11229 C CB    . LEU D 4 1281 ? 119.202 154.043 128.802 1.00 50.26  ? 1278 LEU A CB    1 
ATOM   11230 C CG    . LEU D 4 1281 ? 118.340 155.186 129.342 1.00 50.26  ? 1278 LEU A CG    1 
ATOM   11231 C CD1   . LEU D 4 1281 ? 117.937 154.924 130.785 1.00 50.26  ? 1278 LEU A CD1   1 
ATOM   11232 C CD2   . LEU D 4 1281 ? 119.068 156.515 129.218 1.00 50.26  ? 1278 LEU A CD2   1 
ATOM   11233 N N     . ASN D 4 1282 ? 116.969 152.718 126.940 1.00 50.26  ? 1279 ASN A N     1 
ATOM   11234 C CA    . ASN D 4 1282 ? 115.626 152.749 126.371 1.00 50.26  ? 1279 ASN A CA    1 
ATOM   11235 C C     . ASN D 4 1282 ? 114.886 151.445 126.631 1.00 50.26  ? 1279 ASN A C     1 
ATOM   11236 O O     . ASN D 4 1282 ? 113.675 151.451 126.883 1.00 50.26  ? 1279 ASN A O     1 
ATOM   11237 C CB    . ASN D 4 1282 ? 115.696 153.039 124.873 1.00 50.26  ? 1279 ASN A CB    1 
ATOM   11238 C CG    . ASN D 4 1282 ? 115.693 154.522 124.570 1.00 50.26  ? 1279 ASN A CG    1 
ATOM   11239 O OD1   . ASN D 4 1282 ? 115.548 155.349 125.469 1.00 50.26  ? 1279 ASN A OD1   1 
ATOM   11240 N ND2   . ASN D 4 1282 ? 115.855 154.866 123.298 1.00 50.26  ? 1279 ASN A ND2   1 
ATOM   11241 N N     . HIS D 4 1283 ? 115.593 150.314 126.564 1.00 50.26  ? 1280 HIS A N     1 
ATOM   11242 C CA    . HIS D 4 1283 ? 114.974 149.042 126.918 1.00 50.26  ? 1280 HIS A CA    1 
ATOM   11243 C C     . HIS D 4 1283 ? 114.523 149.046 128.371 1.00 50.26  ? 1280 HIS A C     1 
ATOM   11244 O O     . HIS D 4 1283 ? 113.446 148.536 128.697 1.00 50.26  ? 1280 HIS A O     1 
ATOM   11245 C CB    . HIS D 4 1283 ? 115.947 147.892 126.661 1.00 50.26  ? 1280 HIS A CB    1 
ATOM   11246 C CG    . HIS D 4 1283 ? 115.964 147.419 125.242 1.00 50.26  ? 1280 HIS A CG    1 
ATOM   11247 N ND1   . HIS D 4 1283 ? 116.101 146.091 124.902 1.00 50.26  ? 1280 HIS A ND1   1 
ATOM   11248 C CD2   . HIS D 4 1283 ? 115.866 148.098 124.075 1.00 50.26  ? 1280 HIS A CD2   1 
ATOM   11249 C CE1   . HIS D 4 1283 ? 116.085 145.972 123.587 1.00 50.26  ? 1280 HIS A CE1   1 
ATOM   11250 N NE2   . HIS D 4 1283 ? 115.944 147.175 123.061 1.00 50.26  ? 1280 HIS A NE2   1 
ATOM   11251 N N     . LEU D 4 1284 ? 115.342 149.615 129.259 1.00 54.99  ? 1281 LEU A N     1 
ATOM   11252 C CA    . LEU D 4 1284 ? 114.931 149.774 130.652 1.00 54.99  ? 1281 LEU A CA    1 
ATOM   11253 C C     . LEU D 4 1284 ? 113.696 150.659 130.769 1.00 54.99  ? 1281 LEU A C     1 
ATOM   11254 O O     . LEU D 4 1284 ? 112.754 150.340 131.504 1.00 54.99  ? 1281 LEU A O     1 
ATOM   11255 C CB    . LEU D 4 1284 ? 116.078 150.365 131.468 1.00 54.99  ? 1281 LEU A CB    1 
ATOM   11256 C CG    . LEU D 4 1284 ? 115.802 150.532 132.961 1.00 54.99  ? 1281 LEU A CG    1 
ATOM   11257 C CD1   . LEU D 4 1284 ? 115.551 149.189 133.630 1.00 54.99  ? 1281 LEU A CD1   1 
ATOM   11258 C CD2   . LEU D 4 1284 ? 116.942 151.281 133.628 1.00 54.99  ? 1281 LEU A CD2   1 
ATOM   11259 N N     . LYS D 4 1285 ? 113.691 151.785 130.055 1.00 57.30  ? 1282 LYS A N     1 
ATOM   11260 C CA    . LYS D 4 1285 ? 112.608 152.754 130.182 1.00 57.30  ? 1282 LYS A CA    1 
ATOM   11261 C C     . LYS D 4 1285 ? 111.283 152.181 129.697 1.00 57.30  ? 1282 LYS A C     1 
ATOM   11262 O O     . LYS D 4 1285 ? 110.248 152.361 130.348 1.00 57.30  ? 1282 LYS A O     1 
ATOM   11263 C CB    . LYS D 4 1285 ? 112.958 154.024 129.408 1.00 57.30  ? 1282 LYS A CB    1 
ATOM   11264 C CG    . LYS D 4 1285 ? 111.970 155.160 129.584 1.00 57.30  ? 1282 LYS A CG    1 
ATOM   11265 C CD    . LYS D 4 1285 ? 112.145 156.207 128.497 1.00 57.30  ? 1282 LYS A CD    1 
ATOM   11266 C CE    . LYS D 4 1285 ? 113.589 156.678 128.399 1.00 57.30  ? 1282 LYS A CE    1 
ATOM   11267 N NZ    . LYS D 4 1285 ? 114.151 157.065 129.724 1.00 57.30  ? 1282 LYS A NZ    1 
ATOM   11268 N N     . GLU D 4 1286 ? 111.293 151.494 128.554 1.00 70.23  ? 1283 GLU A N     1 
ATOM   11269 C CA    . GLU D 4 1286 ? 110.056 150.925 128.030 1.00 70.23  ? 1283 GLU A CA    1 
ATOM   11270 C C     . GLU D 4 1286 ? 109.581 149.753 128.880 1.00 70.23  ? 1283 GLU A C     1 
ATOM   11271 O O     . GLU D 4 1286 ? 108.374 149.572 129.078 1.00 70.23  ? 1283 GLU A O     1 
ATOM   11272 C CB    . GLU D 4 1286 ? 110.249 150.497 126.575 1.00 70.23  ? 1283 GLU A CB    1 
ATOM   11273 C CG    . GLU D 4 1286 ? 110.589 151.642 125.630 1.00 70.23  ? 1283 GLU A CG    1 
ATOM   11274 C CD    . GLU D 4 1286 ? 109.362 152.384 125.127 1.00 70.23  ? 1283 GLU A CD    1 
ATOM   11275 O OE1   . GLU D 4 1286 ? 108.322 152.370 125.818 1.00 70.23  ? 1283 GLU A OE1   1 
ATOM   11276 O OE2   . GLU D 4 1286 ? 109.439 152.985 124.035 1.00 70.23  ? 1283 GLU A OE2   1 
ATOM   11277 N N     . SER D 4 1287 ? 110.511 148.950 129.389 1.00 73.06  ? 1284 SER A N     1 
ATOM   11278 C CA    . SER D 4 1287 ? 110.144 147.833 130.247 1.00 73.06  ? 1284 SER A CA    1 
ATOM   11279 C C     . SER D 4 1287 ? 109.601 148.339 131.577 1.00 73.06  ? 1284 SER A C     1 
ATOM   11280 O O     . SER D 4 1287 ? 110.078 149.338 132.124 1.00 73.06  ? 1284 SER A O     1 
ATOM   11281 C CB    . SER D 4 1287 ? 111.349 146.924 130.483 1.00 73.06  ? 1284 SER A CB    1 
ATOM   11282 O OG    . SER D 4 1287 ? 111.141 146.080 131.601 1.00 73.06  ? 1284 SER A OG    1 
ATOM   11283 N N     . LYS D 4 1288 ? 108.587 147.645 132.095 1.00 78.94  ? 1285 LYS A N     1 
ATOM   11284 C CA    . LYS D 4 1288 ? 108.010 148.030 133.379 1.00 78.94  ? 1285 LYS A CA    1 
ATOM   11285 C C     . LYS D 4 1288 ? 108.963 147.726 134.528 1.00 78.94  ? 1285 LYS A C     1 
ATOM   11286 O O     . LYS D 4 1288 ? 109.130 148.546 135.437 1.00 78.94  ? 1285 LYS A O     1 
ATOM   11287 C CB    . LYS D 4 1288 ? 106.674 147.317 133.586 1.00 78.94  ? 1285 LYS A CB    1 
ATOM   11288 C CG    . LYS D 4 1288 ? 105.603 147.703 132.580 1.00 78.94  ? 1285 LYS A CG    1 
ATOM   11289 C CD    . LYS D 4 1288 ? 104.311 146.945 132.836 1.00 78.94  ? 1285 LYS A CD    1 
ATOM   11290 C CE    . LYS D 4 1288 ? 103.227 147.351 131.852 1.00 78.94  ? 1285 LYS A CE    1 
ATOM   11291 N NZ    . LYS D 4 1288 ? 101.968 146.586 132.070 1.00 78.94  ? 1285 LYS A NZ    1 
ATOM   11292 N N     . ASP D 4 1289 ? 109.596 146.556 134.504 1.00 72.41  ? 1286 ASP A N     1 
ATOM   11293 C CA    . ASP D 4 1289 ? 110.498 146.167 135.578 1.00 72.41  ? 1286 ASP A CA    1 
ATOM   11294 C C     . ASP D 4 1289 ? 111.800 146.957 135.505 1.00 72.41  ? 1286 ASP A C     1 
ATOM   11295 O O     . ASP D 4 1289 ? 112.239 147.381 134.433 1.00 72.41  ? 1286 ASP A O     1 
ATOM   11296 C CB    . ASP D 4 1289 ? 110.789 144.668 135.510 1.00 72.41  ? 1286 ASP A CB    1 
ATOM   11297 C CG    . ASP D 4 1289 ? 111.345 144.121 136.812 1.00 72.41  ? 1286 ASP A CG    1 
ATOM   11298 O OD1   . ASP D 4 1289 ? 111.595 144.920 137.739 1.00 72.41  ? 1286 ASP A OD1   1 
ATOM   11299 O OD2   . ASP D 4 1289 ? 111.530 142.890 136.908 1.00 72.41  ? 1286 ASP A OD2   1 
ATOM   11300 N N     . LEU D 4 1290 ? 112.419 147.150 136.666 1.00 61.70  ? 1287 LEU A N     1 
ATOM   11301 C CA    . LEU D 4 1290 ? 113.683 147.878 136.771 1.00 61.70  ? 1287 LEU A CA    1 
ATOM   11302 C C     . LEU D 4 1290 ? 114.880 146.949 136.592 1.00 61.70  ? 1287 LEU A C     1 
ATOM   11303 O O     . LEU D 4 1290 ? 115.788 146.899 137.421 1.00 61.70  ? 1287 LEU A O     1 
ATOM   11304 C CB    . LEU D 4 1290 ? 113.751 148.606 138.108 1.00 61.70  ? 1287 LEU A CB    1 
ATOM   11305 C CG    . LEU D 4 1290 ? 112.602 149.567 138.411 1.00 61.70  ? 1287 LEU A CG    1 
ATOM   11306 C CD1   . LEU D 4 1290 ? 112.711 150.110 139.827 1.00 61.70  ? 1287 LEU A CD1   1 
ATOM   11307 C CD2   . LEU D 4 1290 ? 112.582 150.701 137.402 1.00 61.70  ? 1287 LEU A CD2   1 
ATOM   11308 N N     . LYS D 4 1291 ? 114.886 146.202 135.491 1.00 65.11  ? 1288 LYS A N     1 
ATOM   11309 C CA    . LYS D 4 1291 ? 115.950 145.256 135.189 1.00 65.11  ? 1288 LYS A CA    1 
ATOM   11310 C C     . LYS D 4 1291 ? 116.526 145.561 133.815 1.00 65.11  ? 1288 LYS A C     1 
ATOM   11311 O O     . LYS D 4 1291 ? 115.790 145.906 132.885 1.00 65.11  ? 1288 LYS A O     1 
ATOM   11312 C CB    . LYS D 4 1291 ? 115.441 143.810 135.237 1.00 65.11  ? 1288 LYS A CB    1 
ATOM   11313 C CG    . LYS D 4 1291 ? 114.156 143.578 134.457 1.00 65.11  ? 1288 LYS A CG    1 
ATOM   11314 C CD    . LYS D 4 1291 ? 113.975 142.111 134.108 1.00 65.11  ? 1288 LYS A CD    1 
ATOM   11315 C CE    . LYS D 4 1291 ? 114.001 141.238 135.352 1.00 65.11  ? 1288 LYS A CE    1 
ATOM   11316 N NZ    . LYS D 4 1291 ? 113.743 139.808 135.030 1.00 65.11  ? 1288 LYS A NZ    1 
ATOM   11317 N N     . LEU D 4 1292 ? 117.843 145.437 133.695 1.00 55.85  ? 1289 LEU A N     1 
ATOM   11318 C CA    . LEU D 4 1292 ? 118.544 145.676 132.441 1.00 55.85  ? 1289 LEU A CA    1 
ATOM   11319 C C     . LEU D 4 1292 ? 118.786 144.345 131.743 1.00 55.85  ? 1289 LEU A C     1 
ATOM   11320 O O     . LEU D 4 1292 ? 119.168 143.363 132.388 1.00 55.85  ? 1289 LEU A O     1 
ATOM   11321 C CB    . LEU D 4 1292 ? 119.873 146.396 132.676 1.00 55.85  ? 1289 LEU A CB    1 
ATOM   11322 C CG    . LEU D 4 1292 ? 119.855 147.922 132.804 1.00 55.85  ? 1289 LEU A CG    1 
ATOM   11323 C CD1   . LEU D 4 1292 ? 119.329 148.567 131.535 1.00 55.85  ? 1289 LEU A CD1   1 
ATOM   11324 C CD2   . LEU D 4 1292 ? 119.054 148.372 134.011 1.00 55.85  ? 1289 LEU A CD2   1 
ATOM   11325 N N     . GLN D 4 1293 ? 118.554 144.315 130.433 1.00 58.87  ? 1290 GLN A N     1 
ATOM   11326 C CA    . GLN D 4 1293 ? 118.755 143.092 129.670 1.00 58.87  ? 1290 GLN A CA    1 
ATOM   11327 C C     . GLN D 4 1293 ? 120.216 142.666 129.719 1.00 58.87  ? 1290 GLN A C     1 
ATOM   11328 O O     . GLN D 4 1293 ? 121.127 143.488 129.590 1.00 58.87  ? 1290 GLN A O     1 
ATOM   11329 C CB    . GLN D 4 1293 ? 118.309 143.292 128.221 1.00 58.87  ? 1290 GLN A CB    1 
ATOM   11330 C CG    . GLN D 4 1293 ? 116.802 143.229 128.020 1.00 58.87  ? 1290 GLN A CG    1 
ATOM   11331 C CD    . GLN D 4 1293 ? 116.093 144.479 128.504 1.00 58.87  ? 1290 GLN A CD    1 
ATOM   11332 O OE1   . GLN D 4 1293 ? 116.717 145.520 128.709 1.00 58.87  ? 1290 GLN A OE1   1 
ATOM   11333 N NE2   . GLN D 4 1293 ? 114.783 144.380 128.692 1.00 58.87  ? 1290 GLN A NE2   1 
ATOM   11334 N N     . ASN D 4 1294 ? 120.435 141.369 129.911 1.00 63.40  ? 1291 ASN A N     1 
ATOM   11335 C CA    . ASN D 4 1294 ? 121.785 140.822 130.026 1.00 63.40  ? 1291 ASN A CA    1 
ATOM   11336 C C     . ASN D 4 1294 ? 122.429 140.798 128.647 1.00 63.40  ? 1291 ASN A C     1 
ATOM   11337 O O     . ASN D 4 1294 ? 122.250 139.851 127.878 1.00 63.40  ? 1291 ASN A O     1 
ATOM   11338 C CB    . ASN D 4 1294 ? 121.740 139.428 130.641 1.00 63.40  ? 1291 ASN A CB    1 
ATOM   11339 C CG    . ASN D 4 1294 ? 121.006 139.400 131.968 1.00 63.40  ? 1291 ASN A CG    1 
ATOM   11340 O OD1   . ASN D 4 1294 ? 121.225 140.252 132.829 1.00 63.40  ? 1291 ASN A OD1   1 
ATOM   11341 N ND2   . ASN D 4 1294 ? 120.128 138.420 132.138 1.00 63.40  ? 1291 ASN A ND2   1 
ATOM   11342 N N     . GLY D 4 1295 ? 123.179 141.844 128.329 1.00 53.34  ? 1292 GLY A N     1 
ATOM   11343 C CA    . GLY D 4 1295 ? 123.884 141.927 127.069 1.00 53.34  ? 1292 GLY A CA    1 
ATOM   11344 C C     . GLY D 4 1295 ? 122.969 142.259 125.903 1.00 53.34  ? 1292 GLY A C     1 
ATOM   11345 O O     . GLY D 4 1295 ? 121.753 142.073 125.944 1.00 53.34  ? 1292 GLY A O     1 
ATOM   11346 N N     . ILE D 4 1296 ? 123.583 142.762 124.836 1.00 50.26  ? 1293 ILE A N     1 
ATOM   11347 C CA    . ILE D 4 1296 ? 122.883 143.119 123.608 1.00 50.26  ? 1293 ILE A CA    1 
ATOM   11348 C C     . ILE D 4 1296 ? 123.426 142.242 122.491 1.00 50.26  ? 1293 ILE A C     1 
ATOM   11349 O O     . ILE D 4 1296 ? 124.636 142.234 122.234 1.00 50.26  ? 1293 ILE A O     1 
ATOM   11350 C CB    . ILE D 4 1296 ? 123.050 144.606 123.262 1.00 50.26  ? 1293 ILE A CB    1 
ATOM   11351 C CG1   . ILE D 4 1296 ? 122.563 145.484 124.414 1.00 50.26  ? 1293 ILE A CG1   1 
ATOM   11352 C CG2   . ILE D 4 1296 ? 122.302 144.937 121.985 1.00 50.26  ? 1293 ILE A CG2   1 
ATOM   11353 C CD1   . ILE D 4 1296 ? 123.679 146.051 125.259 1.00 50.26  ? 1293 ILE A CD1   1 
ATOM   11354 N N     . SER D 4 1297 ? 122.537 141.507 121.831 1.00 50.26  ? 1294 SER A N     1 
ATOM   11355 C CA    . SER D 4 1297 ? 122.947 140.678 120.709 1.00 50.26  ? 1294 SER A CA    1 
ATOM   11356 C C     . SER D 4 1297 ? 123.403 141.549 119.545 1.00 50.26  ? 1294 SER A C     1 
ATOM   11357 O O     . SER D 4 1297 ? 122.896 142.653 119.330 1.00 50.26  ? 1294 SER A O     1 
ATOM   11358 C CB    . SER D 4 1297 ? 121.800 139.771 120.267 1.00 50.26  ? 1294 SER A CB    1 
ATOM   11359 O OG    . SER D 4 1297 ? 121.293 139.024 121.359 1.00 50.26  ? 1294 SER A OG    1 
ATOM   11360 N N     . ASN D 4 1298 ? 124.383 141.042 118.794 1.00 50.26  ? 1295 ASN A N     1 
ATOM   11361 C CA    . ASN D 4 1298 ? 124.882 141.782 117.639 1.00 50.26  ? 1295 ASN A CA    1 
ATOM   11362 C C     . ASN D 4 1298 ? 123.782 141.993 116.608 1.00 50.26  ? 1295 ASN A C     1 
ATOM   11363 O O     . ASN D 4 1298 ? 123.648 143.088 116.049 1.00 50.26  ? 1295 ASN A O     1 
ATOM   11364 C CB    . ASN D 4 1298 ? 126.067 141.047 117.016 1.00 50.26  ? 1295 ASN A CB    1 
ATOM   11365 C CG    . ASN D 4 1298 ? 127.137 140.705 118.029 1.00 50.26  ? 1295 ASN A CG    1 
ATOM   11366 O OD1   . ASN D 4 1298 ? 127.953 141.549 118.396 1.00 50.26  ? 1295 ASN A OD1   1 
ATOM   11367 N ND2   . ASN D 4 1298 ? 127.138 139.461 118.489 1.00 50.26  ? 1295 ASN A ND2   1 
ATOM   11368 N N     . GLN D 4 1299 ? 122.983 140.957 116.347 1.00 50.26  ? 1296 GLN A N     1 
ATOM   11369 C CA    . GLN D 4 1299 ? 121.869 141.101 115.417 1.00 50.26  ? 1296 GLN A CA    1 
ATOM   11370 C C     . GLN D 4 1299 ? 120.852 142.114 115.929 1.00 50.26  ? 1296 GLN A C     1 
ATOM   11371 O O     . GLN D 4 1299 ? 120.359 142.950 115.163 1.00 50.26  ? 1296 GLN A O     1 
ATOM   11372 C CB    . GLN D 4 1299 ? 121.207 139.744 115.181 1.00 50.26  ? 1296 GLN A CB    1 
ATOM   11373 C CG    . GLN D 4 1299 ? 119.744 139.818 114.774 1.00 50.26  ? 1296 GLN A CG    1 
ATOM   11374 C CD    . GLN D 4 1299 ? 119.543 140.477 113.425 1.00 50.26  ? 1296 GLN A CD    1 
ATOM   11375 O OE1   . GLN D 4 1299 ? 120.420 140.436 112.564 1.00 50.26  ? 1296 GLN A OE1   1 
ATOM   11376 N NE2   . GLN D 4 1299 ? 118.383 141.091 113.235 1.00 50.26  ? 1296 GLN A NE2   1 
ATOM   11377 N N     . ASP D 4 1300 ? 120.532 142.058 117.224 1.00 50.26  ? 1297 ASP A N     1 
ATOM   11378 C CA    . ASP D 4 1300 ? 119.569 142.997 117.791 1.00 50.26  ? 1297 ASP A CA    1 
ATOM   11379 C C     . ASP D 4 1300 ? 120.088 144.429 117.727 1.00 50.26  ? 1297 ASP A C     1 
ATOM   11380 O O     . ASP D 4 1300 ? 119.347 145.350 117.364 1.00 50.26  ? 1297 ASP A O     1 
ATOM   11381 C CB    . ASP D 4 1300 ? 119.248 142.602 119.232 1.00 50.26  ? 1297 ASP A CB    1 
ATOM   11382 C CG    . ASP D 4 1300 ? 118.012 143.297 119.766 1.00 50.26  ? 1297 ASP A CG    1 
ATOM   11383 O OD1   . ASP D 4 1300 ? 117.341 144.009 118.989 1.00 50.26  ? 1297 ASP A OD1   1 
ATOM   11384 O OD2   . ASP D 4 1300 ? 117.710 143.128 120.966 1.00 50.26  ? 1297 ASP A OD2   1 
ATOM   11385 N N     . TRP D 4 1301 ? 121.360 144.634 118.075 1.00 50.26  ? 1298 TRP A N     1 
ATOM   11386 C CA    . TRP D 4 1301 ? 121.942 145.970 118.010 1.00 50.26  ? 1298 TRP A CA    1 
ATOM   11387 C C     . TRP D 4 1301 ? 121.957 146.495 116.581 1.00 50.26  ? 1298 TRP A C     1 
ATOM   11388 O O     . TRP D 4 1301 ? 121.635 147.665 116.338 1.00 50.26  ? 1298 TRP A O     1 
ATOM   11389 C CB    . TRP D 4 1301 ? 123.355 145.948 118.592 1.00 50.26  ? 1298 TRP A CB    1 
ATOM   11390 C CG    . TRP D 4 1301 ? 124.283 146.970 118.008 1.00 50.26  ? 1298 TRP A CG    1 
ATOM   11391 C CD1   . TRP D 4 1301 ? 125.389 146.729 117.247 1.00 50.26  ? 1298 TRP A CD1   1 
ATOM   11392 C CD2   . TRP D 4 1301 ? 124.201 148.392 118.155 1.00 50.26  ? 1298 TRP A CD2   1 
ATOM   11393 N NE1   . TRP D 4 1301 ? 125.994 147.912 116.902 1.00 50.26  ? 1298 TRP A NE1   1 
ATOM   11394 C CE2   . TRP D 4 1301 ? 125.283 148.948 117.447 1.00 50.26  ? 1298 TRP A CE2   1 
ATOM   11395 C CE3   . TRP D 4 1301 ? 123.314 149.249 118.811 1.00 50.26  ? 1298 TRP A CE3   1 
ATOM   11396 C CZ2   . TRP D 4 1301 ? 125.502 150.320 117.378 1.00 50.26  ? 1298 TRP A CZ2   1 
ATOM   11397 C CZ3   . TRP D 4 1301 ? 123.534 150.610 118.740 1.00 50.26  ? 1298 TRP A CZ3   1 
ATOM   11398 C CH2   . TRP D 4 1301 ? 124.619 151.132 118.030 1.00 50.26  ? 1298 TRP A CH2   1 
ATOM   11399 N N     . LEU D 4 1302 ? 122.330 145.644 115.621 1.00 50.26  ? 1299 LEU A N     1 
ATOM   11400 C CA    . LEU D 4 1302 ? 122.347 146.070 114.227 1.00 50.26  ? 1299 LEU A CA    1 
ATOM   11401 C C     . LEU D 4 1302 ? 120.950 146.426 113.743 1.00 50.26  ? 1299 LEU A C     1 
ATOM   11402 O O     . LEU D 4 1302 ? 120.762 147.440 113.061 1.00 50.26  ? 1299 LEU A O     1 
ATOM   11403 C CB    . LEU D 4 1302 ? 122.958 144.978 113.351 1.00 50.26  ? 1299 LEU A CB    1 
ATOM   11404 C CG    . LEU D 4 1302 ? 124.482 145.002 113.251 1.00 50.26  ? 1299 LEU A CG    1 
ATOM   11405 C CD1   . LEU D 4 1302 ? 124.987 143.803 112.469 1.00 50.26  ? 1299 LEU A CD1   1 
ATOM   11406 C CD2   . LEU D 4 1302 ? 124.949 146.297 112.615 1.00 50.26  ? 1299 LEU A CD2   1 
ATOM   11407 N N     . ALA D 4 1303 ? 119.953 145.609 114.092 1.00 50.26  ? 1300 ALA A N     1 
ATOM   11408 C CA    . ALA D 4 1303 ? 118.583 145.912 113.696 1.00 50.26  ? 1300 ALA A CA    1 
ATOM   11409 C C     . ALA D 4 1303 ? 118.119 147.230 114.296 1.00 50.26  ? 1300 ALA A C     1 
ATOM   11410 O O     . ALA D 4 1303 ? 117.510 148.055 113.604 1.00 50.26  ? 1300 ALA A O     1 
ATOM   11411 C CB    . ALA D 4 1303 ? 117.651 144.774 114.110 1.00 50.26  ? 1300 ALA A CB    1 
ATOM   11412 N N     . TYR D 4 1304 ? 118.419 147.459 115.576 1.00 50.26  ? 1301 TYR A N     1 
ATOM   11413 C CA    . TYR D 4 1304 ? 118.005 148.700 116.222 1.00 50.26  ? 1301 TYR A CA    1 
ATOM   11414 C C     . TYR D 4 1304 ? 118.651 149.907 115.557 1.00 50.26  ? 1301 TYR A C     1 
ATOM   11415 O O     . TYR D 4 1304 ? 117.975 150.896 115.251 1.00 50.26  ? 1301 TYR A O     1 
ATOM   11416 C CB    . TYR D 4 1304 ? 118.349 148.658 117.711 1.00 50.26  ? 1301 TYR A CB    1 
ATOM   11417 C CG    . TYR D 4 1304 ? 118.219 149.992 118.418 1.00 50.26  ? 1301 TYR A CG    1 
ATOM   11418 C CD1   . TYR D 4 1304 ? 117.016 150.382 118.986 1.00 50.26  ? 1301 TYR A CD1   1 
ATOM   11419 C CD2   . TYR D 4 1304 ? 119.303 150.856 118.526 1.00 50.26  ? 1301 TYR A CD2   1 
ATOM   11420 C CE1   . TYR D 4 1304 ? 116.892 151.595 119.634 1.00 50.26  ? 1301 TYR A CE1   1 
ATOM   11421 C CE2   . TYR D 4 1304 ? 119.188 152.070 119.172 1.00 50.26  ? 1301 TYR A CE2   1 
ATOM   11422 C CZ    . TYR D 4 1304 ? 117.980 152.434 119.724 1.00 50.26  ? 1301 TYR A CZ    1 
ATOM   11423 O OH    . TYR D 4 1304 ? 117.860 153.643 120.369 1.00 50.26  ? 1301 TYR A OH    1 
ATOM   11424 N N     . ILE D 4 1305 ? 119.964 149.848 115.323 1.00 50.26  ? 1302 ILE A N     1 
ATOM   11425 C CA    . ILE D 4 1305 ? 120.657 151.014 114.784 1.00 50.26  ? 1302 ILE A CA    1 
ATOM   11426 C C     . ILE D 4 1305 ? 120.236 151.272 113.341 1.00 50.26  ? 1302 ILE A C     1 
ATOM   11427 O O     . ILE D 4 1305 ? 120.084 152.427 112.925 1.00 50.26  ? 1302 ILE A O     1 
ATOM   11428 C CB    . ILE D 4 1305 ? 122.184 150.859 114.925 1.00 50.26  ? 1302 ILE A CB    1 
ATOM   11429 C CG1   . ILE D 4 1305 ? 122.884 152.171 114.572 1.00 50.26  ? 1302 ILE A CG1   1 
ATOM   11430 C CG2   . ILE D 4 1305 ? 122.714 149.730 114.064 1.00 50.26  ? 1302 ILE A CG2   1 
ATOM   11431 C CD1   . ILE D 4 1305 ? 122.409 153.351 115.384 1.00 50.26  ? 1302 ILE A CD1   1 
ATOM   11432 N N     . GLN D 4 1306 ? 120.017 150.211 112.560 1.00 50.26  ? 1303 GLN A N     1 
ATOM   11433 C CA    . GLN D 4 1306 ? 119.619 150.403 111.172 1.00 50.26  ? 1303 GLN A CA    1 
ATOM   11434 C C     . GLN D 4 1306 ? 118.176 150.877 111.061 1.00 50.26  ? 1303 GLN A C     1 
ATOM   11435 O O     . GLN D 4 1306 ? 117.840 151.611 110.125 1.00 50.26  ? 1303 GLN A O     1 
ATOM   11436 C CB    . GLN D 4 1306 ? 119.831 149.112 110.385 1.00 50.26  ? 1303 GLN A CB    1 
ATOM   11437 C CG    . GLN D 4 1306 ? 121.295 148.779 110.151 1.00 50.26  ? 1303 GLN A CG    1 
ATOM   11438 C CD    . GLN D 4 1306 ? 121.490 147.438 109.479 1.00 50.26  ? 1303 GLN A CD    1 
ATOM   11439 O OE1   . GLN D 4 1306 ? 120.536 146.692 109.270 1.00 50.26  ? 1303 GLN A OE1   1 
ATOM   11440 N NE2   . GLN D 4 1306 ? 122.732 147.122 109.139 1.00 50.26  ? 1303 GLN A NE2   1 
ATOM   11441 N N     . GLU D 4 1307 ? 117.311 150.477 111.996 1.00 50.26  ? 1304 GLU A N     1 
ATOM   11442 C CA    . GLU D 4 1307 ? 115.955 151.011 112.002 1.00 50.26  ? 1304 GLU A CA    1 
ATOM   11443 C C     . GLU D 4 1307 ? 115.927 152.454 112.483 1.00 50.26  ? 1304 GLU A C     1 
ATOM   11444 O O     . GLU D 4 1307 ? 115.106 153.247 112.011 1.00 50.26  ? 1304 GLU A O     1 
ATOM   11445 C CB    . GLU D 4 1307 ? 115.052 150.140 112.874 1.00 50.26  ? 1304 GLU A CB    1 
ATOM   11446 C CG    . GLU D 4 1307 ? 113.570 150.444 112.734 1.00 50.26  ? 1304 GLU A CG    1 
ATOM   11447 C CD    . GLU D 4 1307 ? 112.695 149.381 113.368 1.00 50.26  ? 1304 GLU A CD    1 
ATOM   11448 O OE1   . GLU D 4 1307 ? 113.078 148.851 114.432 1.00 50.26  ? 1304 GLU A OE1   1 
ATOM   11449 O OE2   . GLU D 4 1307 ? 111.626 149.073 112.802 1.00 50.26  ? 1304 GLU A OE2   1 
ATOM   11450 N N     . LEU D 4 1308 ? 116.808 152.813 113.418 1.00 50.26  ? 1305 LEU A N     1 
ATOM   11451 C CA    . LEU D 4 1308 ? 116.855 154.187 113.903 1.00 50.26  ? 1305 LEU A CA    1 
ATOM   11452 C C     . LEU D 4 1308 ? 117.393 155.129 112.834 1.00 50.26  ? 1305 LEU A C     1 
ATOM   11453 O O     . LEU D 4 1308 ? 116.862 156.228 112.636 1.00 50.26  ? 1305 LEU A O     1 
ATOM   11454 C CB    . LEU D 4 1308 ? 117.708 154.265 115.169 1.00 50.26  ? 1305 LEU A CB    1 
ATOM   11455 C CG    . LEU D 4 1308 ? 118.039 155.667 115.680 1.00 50.26  ? 1305 LEU A CG    1 
ATOM   11456 C CD1   . LEU D 4 1308 ? 116.771 156.404 116.076 1.00 50.26  ? 1305 LEU A CD1   1 
ATOM   11457 C CD2   . LEU D 4 1308 ? 119.011 155.598 116.846 1.00 50.26  ? 1305 LEU A CD2   1 
ATOM   11458 N N     . ARG D 4 1309 ? 118.449 154.716 112.132 1.00 50.26  ? 1306 ARG A N     1 
ATOM   11459 C CA    . ARG D 4 1309 ? 119.066 155.596 111.145 1.00 50.26  ? 1306 ARG A CA    1 
ATOM   11460 C C     . ARG D 4 1309 ? 118.195 155.745 109.904 1.00 50.26  ? 1306 ARG A C     1 
ATOM   11461 O O     . ARG D 4 1309 ? 118.166 156.814 109.285 1.00 50.26  ? 1306 ARG A O     1 
ATOM   11462 C CB    . ARG D 4 1309 ? 120.450 155.072 110.771 1.00 50.26  ? 1306 ARG A CB    1 
ATOM   11463 C CG    . ARG D 4 1309 ? 121.469 155.223 111.878 1.00 50.26  ? 1306 ARG A CG    1 
ATOM   11464 C CD    . ARG D 4 1309 ? 121.821 156.681 112.090 1.00 50.26  ? 1306 ARG A CD    1 
ATOM   11465 N NE    . ARG D 4 1309 ? 122.870 156.845 113.087 1.00 50.26  ? 1306 ARG A NE    1 
ATOM   11466 C CZ    . ARG D 4 1309 ? 122.657 157.215 114.341 1.00 50.26  ? 1306 ARG A CZ    1 
ATOM   11467 N NH1   . ARG D 4 1309 ? 121.440 157.485 114.785 1.00 50.26  ? 1306 ARG A NH1   1 
ATOM   11468 N NH2   . ARG D 4 1309 ? 123.690 157.320 115.171 1.00 50.26  ? 1306 ARG A NH2   1 
ATOM   11469 N N     . ASN D 4 1310 ? 117.486 154.689 109.521 1.00 50.26  ? 1307 ASN A N     1 
ATOM   11470 C CA    . ASN D 4 1310 ? 116.642 154.731 108.333 1.00 50.26  ? 1307 ASN A CA    1 
ATOM   11471 C C     . ASN D 4 1310 ? 115.218 155.154 108.679 1.00 50.26  ? 1307 ASN A C     1 
ATOM   11472 O O     . ASN D 4 1310 ? 114.714 154.864 109.762 1.00 50.26  ? 1307 ASN A O     1 
ATOM   11473 C CB    . ASN D 4 1310 ? 116.632 153.369 107.637 1.00 50.26  ? 1307 ASN A CB    1 
ATOM   11474 C CG    . ASN D 4 1310 ? 115.546 153.260 106.588 1.00 50.26  ? 1307 ASN A CG    1 
ATOM   11475 O OD1   . ASN D 4 1310 ? 114.459 152.747 106.855 1.00 50.26  ? 1307 ASN A OD1   1 
ATOM   11476 N ND2   . ASN D 4 1310 ? 115.831 153.751 105.388 1.00 50.26  ? 1307 ASN A ND2   1 
ATOM   11477 O OXT   . ASN D 4 1310 ? 114.535 155.798 107.882 1.00 35.92  ? 1307 ASN A OXT   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1592  N N   . LYS D 29   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  26   LYS A N   
1593  C CA  . LYS D 29   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  26   LYS A CA  
1594  C C   . LYS D 29   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  26   LYS A C   
1595  O O   . LYS D 29   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  26   LYS A O   
1601  N N   . THR D 30   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  27   THR A N   
1602  C CA  . THR D 30   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  27   THR A CA  
1603  C C   . THR D 30   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  27   THR A C   
1604  O O   . THR D 30   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  27   THR A O   
1605  C CB  . THR D 30   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  27   THR A CB  
1606  O OG1 . THR D 30   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  27   THR A OG1 
1607  C CG2 . THR D 30   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  27   THR A CG2 
1608  N N   . LEU D 31   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  28   LEU A N   
1609  C CA  . LEU D 31   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  28   LEU A CA  
1610  C C   . LEU D 31   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  28   LEU A C   
1611  O O   . LEU D 31   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  28   LEU A O   
1612  C CB  . LEU D 31   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  28   LEU A CB  
1613  C CG  . LEU D 31   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  28   LEU A CG  
1614  C CD1 . LEU D 31   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  28   LEU A CD1 
1615  C CD2 . LEU D 31   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  28   LEU A CD2 
1616  N N   . LYS D 32   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  29   LYS A N   
1617  C CA  . LYS D 32   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  29   LYS A CA  
1618  C C   . LYS D 32   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  29   LYS A C   
1619  O O   . LYS D 32   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  29   LYS A O   
1620  C CB  . LYS D 32   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  29   LYS A CB  
1621  C CG  . LYS D 32   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  29   LYS A CG  
1622  C CD  . LYS D 32   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  29   LYS A CD  
1623  C CE  . LYS D 32   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  29   LYS A CE  
1624  N NZ  . LYS D 32   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  29   LYS A NZ  
1625  N N   . HIS D 33   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  30   HIS A N   
1626  C CA  . HIS D 33   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  30   HIS A CA  
1627  C C   . HIS D 33   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  30   HIS A C   
1628  O O   . HIS D 33   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  30   HIS A O   
1629  C CB  . HIS D 33   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  30   HIS A CB  
1630  C CG  . HIS D 33   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  30   HIS A CG  
1631  N ND1 . HIS D 33   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  30   HIS A ND1 
1632  C CD2 . HIS D 33   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  30   HIS A CD2 
1633  C CE1 . HIS D 33   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  30   HIS A CE1 
1634  N NE2 . HIS D 33   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  30   HIS A NE2 
1635  N N   . ILE D 34   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  31   ILE A N   
1636  C CA  . ILE D 34   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  31   ILE A CA  
1637  C C   . ILE D 34   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  31   ILE A C   
1638  O O   . ILE D 34   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  31   ILE A O   
1639  C CB  . ILE D 34   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  31   ILE A CB  
1640  C CG1 . ILE D 34   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  31   ILE A CG1 
1641  C CG2 . ILE D 34   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  31   ILE A CG2 
1642  C CD1 . ILE D 34   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  31   ILE A CD1 
1643  N N   . GLN D 35   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  32   GLN A N   
1644  C CA  . GLN D 35   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  32   GLN A CA  
1645  C C   . GLN D 35   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  32   GLN A C   
1646  O O   . GLN D 35   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  32   GLN A O   
1647  C CB  . GLN D 35   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  32   GLN A CB  
1648  C CG  . GLN D 35   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  32   GLN A CG  
1649  C CD  . GLN D 35   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  32   GLN A CD  
1650  O OE1 . GLN D 35   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  32   GLN A OE1 
1651  N NE2 . GLN D 35   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  32   GLN A NE2 
1652  N N   . GLU D 36   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  33   GLU A N   
1653  C CA  . GLU D 36   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  33   GLU A CA  
1654  C C   . GLU D 36   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  33   GLU A C   
1655  O O   . GLU D 36   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  33   GLU A O   
1656  C CB  . GLU D 36   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  33   GLU A CB  
1657  C CG  . GLU D 36   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  33   GLU A CG  
1658  C CD  . GLU D 36   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  33   GLU A CD  
1659  O OE1 . GLU D 36   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  33   GLU A OE1 
1660  O OE2 . GLU D 36   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  33   GLU A OE2 
1661  N N   . GLN D 37   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  34   GLN A N   
1662  C CA  . GLN D 37   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  34   GLN A CA  
1663  C C   . GLN D 37   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  34   GLN A C   
1664  O O   . GLN D 37   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  34   GLN A O   
1665  C CB  . GLN D 37   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  34   GLN A CB  
1666  C CG  . GLN D 37   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  34   GLN A CG  
1667  C CD  . GLN D 37   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  34   GLN A CD  
1668  O OE1 . GLN D 37   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  34   GLN A OE1 
1669  N NE2 . GLN D 37   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  34   GLN A NE2 
1670  N N   . GLY D 38   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  35   GLY A N   
1671  C CA  . GLY D 38   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  35   GLY A CA  
1672  C C   . GLY D 38   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  35   GLY A C   
1673  O O   . GLY D 38   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  35   GLY A O   
1674  N N   . PHE D 39   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  36   PHE A N   
1675  C CA  . PHE D 39   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  36   PHE A CA  
1676  C C   . PHE D 39   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  36   PHE A C   
1677  O O   . PHE D 39   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  36   PHE A O   
1678  C CB  . PHE D 39   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  36   PHE A CB  
1679  C CG  . PHE D 39   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  36   PHE A CG  
1680  C CD1 . PHE D 39   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  36   PHE A CD1 
1681  C CD2 . PHE D 39   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  36   PHE A CD2 
1682  C CE1 . PHE D 39   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  36   PHE A CE1 
1683  C CE2 . PHE D 39   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  36   PHE A CE2 
1684  C CZ  . PHE D 39   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  36   PHE A CZ  
1685  N N   . ILE D 40   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  37   ILE A N   
1686  C CA  . ILE D 40   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  37   ILE A CA  
1687  C C   . ILE D 40   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  37   ILE A C   
1688  O O   . ILE D 40   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  37   ILE A O   
1689  C CB  . ILE D 40   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  37   ILE A CB  
1690  C CG1 . ILE D 40   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  37   ILE A CG1 
1691  C CG2 . ILE D 40   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  37   ILE A CG2 
1692  C CD1 . ILE D 40   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  37   ILE A CD1 
1693  N N   . GLU D 41   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  38   GLU A N   
1694  C CA  . GLU D 41   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  38   GLU A CA  
1695  C C   . GLU D 41   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  38   GLU A C   
1696  O O   . GLU D 41   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  38   GLU A O   
1697  C CB  . GLU D 41   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  38   GLU A CB  
1698  C CG  . GLU D 41   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  38   GLU A CG  
1699  C CD  . GLU D 41   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  38   GLU A CD  
1700  O OE1 . GLU D 41   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  38   GLU A OE1 
1701  O OE2 . GLU D 41   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  38   GLU A OE2 
1702  N N   . GLU D 42   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  39   GLU A N   
1703  C CA  . GLU D 42   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  39   GLU A CA  
1704  C C   . GLU D 42   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  39   GLU A C   
1705  O O   . GLU D 42   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  39   GLU A O   
1706  C CB  . GLU D 42   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  39   GLU A CB  
1707  C CG  . GLU D 42   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  39   GLU A CG  
1708  C CD  . GLU D 42   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  39   GLU A CD  
1709  O OE1 . GLU D 42   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  39   GLU A OE1 
1710  O OE2 . GLU D 42   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  39   GLU A OE2 
1711  N N   . ASP D 43   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  40   ASP A N   
1712  C CA  . ASP D 43   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  40   ASP A CA  
1713  C C   . ASP D 43   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  40   ASP A C   
1714  O O   . ASP D 43   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  40   ASP A O   
1715  C CB  . ASP D 43   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  40   ASP A CB  
1716  C CG  . ASP D 43   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  40   ASP A CG  
1717  O OD1 . ASP D 43   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  40   ASP A OD1 
1718  O OD2 . ASP D 43   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  40   ASP A OD2 
1719  N N   . LYS D 44   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  41   LYS A N   
1720  C CA  . LYS D 44   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  41   LYS A CA  
1721  C C   . LYS D 44   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  41   LYS A C   
1722  O O   . LYS D 44   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  41   LYS A O   
1723  C CB  . LYS D 44   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  41   LYS A CB  
1724  C CG  . LYS D 44   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  41   LYS A CG  
1725  C CD  . LYS D 44   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  41   LYS A CD  
1726  C CE  . LYS D 44   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  41   LYS A CE  
1727  N NZ  . LYS D 44   ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  41   LYS A NZ  
1728  N N   . ALA D 45   ? 0.6628 0.6628 0.6628 0.0000  0.0000  0.0000  42   ALA A N   
1729  C CA  . ALA D 45   ? 0.6628 0.6628 0.6628 0.0000  0.0000  0.0000  42   ALA A CA  
1730  C C   . ALA D 45   ? 0.6628 0.6628 0.6628 0.0000  0.0000  0.0000  42   ALA A C   
1731  O O   . ALA D 45   ? 0.6628 0.6628 0.6628 0.0000  0.0000  0.0000  42   ALA A O   
1732  C CB  . ALA D 45   ? 0.6628 0.6628 0.6628 0.0000  0.0000  0.0000  42   ALA A CB  
1733  N N   . ARG D 46   ? 0.6655 0.6655 0.6655 0.0000  0.0000  0.0000  43   ARG A N   
1734  C CA  . ARG D 46   ? 0.6655 0.6655 0.6655 0.0000  0.0000  0.0000  43   ARG A CA  
1735  C C   . ARG D 46   ? 0.6655 0.6655 0.6655 0.0000  0.0000  0.0000  43   ARG A C   
1736  O O   . ARG D 46   ? 0.6655 0.6655 0.6655 0.0000  0.0000  0.0000  43   ARG A O   
1737  C CB  . ARG D 46   ? 0.6655 0.6655 0.6655 0.0000  0.0000  0.0000  43   ARG A CB  
1738  C CG  . ARG D 46   ? 0.6655 0.6655 0.6655 0.0000  0.0000  0.0000  43   ARG A CG  
1739  C CD  . ARG D 46   ? 0.6655 0.6655 0.6655 0.0000  0.0000  0.0000  43   ARG A CD  
1740  N NE  . ARG D 46   ? 0.6655 0.6655 0.6655 0.0000  0.0000  0.0000  43   ARG A NE  
1741  C CZ  . ARG D 46   ? 0.6655 0.6655 0.6655 0.0000  0.0000  0.0000  43   ARG A CZ  
1742  N NH1 . ARG D 46   ? 0.6655 0.6655 0.6655 0.0000  0.0000  0.0000  43   ARG A NH1 
1743  N NH2 . ARG D 46   ? 0.6655 0.6655 0.6655 0.0000  0.0000  0.0000  43   ARG A NH2 
1744  N N   . ASN D 47   ? 0.6657 0.6657 0.6657 0.0000  0.0000  0.0000  44   ASN A N   
1745  C CA  . ASN D 47   ? 0.6657 0.6657 0.6657 0.0000  0.0000  0.0000  44   ASN A CA  
1746  C C   . ASN D 47   ? 0.6657 0.6657 0.6657 0.0000  0.0000  0.0000  44   ASN A C   
1747  O O   . ASN D 47   ? 0.6657 0.6657 0.6657 0.0000  0.0000  0.0000  44   ASN A O   
1748  C CB  . ASN D 47   ? 0.6657 0.6657 0.6657 0.0000  0.0000  0.0000  44   ASN A CB  
1749  C CG  . ASN D 47   ? 0.6657 0.6657 0.6657 0.0000  0.0000  0.0000  44   ASN A CG  
1750  O OD1 . ASN D 47   ? 0.6657 0.6657 0.6657 0.0000  0.0000  0.0000  44   ASN A OD1 
1751  N ND2 . ASN D 47   ? 0.6657 0.6657 0.6657 0.0000  0.0000  0.0000  44   ASN A ND2 
1752  N N   . ASP D 48   ? 0.7393 0.7393 0.7393 0.0000  0.0000  0.0000  45   ASP A N   
1753  C CA  . ASP D 48   ? 0.7393 0.7393 0.7393 0.0000  0.0000  0.0000  45   ASP A CA  
1754  C C   . ASP D 48   ? 0.7393 0.7393 0.7393 0.0000  0.0000  0.0000  45   ASP A C   
1755  O O   . ASP D 48   ? 0.7393 0.7393 0.7393 0.0000  0.0000  0.0000  45   ASP A O   
1756  C CB  . ASP D 48   ? 0.7393 0.7393 0.7393 0.0000  0.0000  0.0000  45   ASP A CB  
1757  C CG  . ASP D 48   ? 0.7393 0.7393 0.7393 0.0000  0.0000  0.0000  45   ASP A CG  
1758  O OD1 . ASP D 48   ? 0.7393 0.7393 0.7393 0.0000  0.0000  0.0000  45   ASP A OD1 
1759  O OD2 . ASP D 48   ? 0.7393 0.7393 0.7393 0.0000  0.0000  0.0000  45   ASP A OD2 
1760  N N   . HIS D 49   ? 0.8028 0.8028 0.8028 0.0000  0.0000  0.0000  46   HIS A N   
1761  C CA  . HIS D 49   ? 0.8028 0.8028 0.8028 0.0000  0.0000  0.0000  46   HIS A CA  
1762  C C   . HIS D 49   ? 0.8028 0.8028 0.8028 0.0000  0.0000  0.0000  46   HIS A C   
1763  O O   . HIS D 49   ? 0.8028 0.8028 0.8028 0.0000  0.0000  0.0000  46   HIS A O   
1764  C CB  . HIS D 49   ? 0.8028 0.8028 0.8028 0.0000  0.0000  0.0000  46   HIS A CB  
1765  C CG  . HIS D 49   ? 0.8028 0.8028 0.8028 0.0000  0.0000  0.0000  46   HIS A CG  
1766  N ND1 . HIS D 49   ? 0.8028 0.8028 0.8028 0.0000  0.0000  0.0000  46   HIS A ND1 
1767  C CD2 . HIS D 49   ? 0.8028 0.8028 0.8028 0.0000  0.0000  0.0000  46   HIS A CD2 
1768  C CE1 . HIS D 49   ? 0.8028 0.8028 0.8028 0.0000  0.0000  0.0000  46   HIS A CE1 
1769  N NE2 . HIS D 49   ? 0.8028 0.8028 0.8028 0.0000  0.0000  0.0000  46   HIS A NE2 
1770  N N   . TYR D 50   ? 1.3546 0.7167 0.9007 -0.3343 -0.2415 0.2361  47   TYR A N   
1771  C CA  . TYR D 50   ? 1.2889 0.6603 0.8585 -0.3042 -0.2271 0.2296  47   TYR A CA  
1772  C C   . TYR D 50   ? 1.2695 0.6436 0.8498 -0.2941 -0.2219 0.2205  47   TYR A C   
1773  O O   . TYR D 50   ? 1.2735 0.6189 0.8470 -0.2652 -0.2184 0.2106  47   TYR A O   
1774  C CB  . TYR D 50   ? 1.2189 0.6547 0.8314 -0.3077 -0.2133 0.2386  47   TYR A CB  
1775  C CG  . TYR D 50   ? 1.1554 0.6174 0.7999 -0.2840 -0.1980 0.2333  47   TYR A CG  
1776  C CD1 . TYR D 50   ? 1.1334 0.5781 0.7764 -0.2499 -0.1923 0.2230  47   TYR A CD1 
1777  C CD2 . TYR D 50   ? 1.1067 0.6302 0.7909 -0.2871 -0.1861 0.2303  47   TYR A CD2 
1778  C CE1 . TYR D 50   ? 1.0891 0.5768 0.7693 -0.2226 -0.1757 0.2108  47   TYR A CE1 
1779  C CE2 . TYR D 50   ? 1.0616 0.6237 0.7810 -0.2587 -0.1698 0.2175  47   TYR A CE2 
1780  C CZ  . TYR D 50   ? 1.0611 0.6052 0.7785 -0.2279 -0.1649 0.2081  47   TYR A CZ  
1781  O OH  . TYR D 50   ? 0.9889 0.5718 0.7399 -0.2025 -0.1497 0.1967  47   TYR A OH  
1782  N N   . LYS D 51   ? 1.2457 0.6560 0.8423 -0.3165 -0.2216 0.2239  48   LYS A N   
1783  C CA  . LYS D 51   ? 1.2040 0.6205 0.8127 -0.3084 -0.2162 0.2158  48   LYS A CA  
1784  C C   . LYS D 51   ? 1.2563 0.6071 0.8232 -0.2981 -0.2282 0.2052  48   LYS A C   
1785  O O   . LYS D 51   ? 1.2446 0.5834 0.8144 -0.2786 -0.2235 0.1954  48   LYS A O   
1786  C CB  . LYS D 51   ? 1.1629 0.6380 0.7991 -0.3346 -0.2129 0.2226  48   LYS A CB  
1787  C CG  . LYS D 51   ? 1.1223 0.6678 0.8015 -0.3402 -0.1994 0.2315  48   LYS A CG  
1788  C CD  . LYS D 51   ? 1.1123 0.7181 0.8194 -0.3589 -0.1943 0.2359  48   LYS A CD  
1789  C CE  . LYS D 51   ? 1.0719 0.7478 0.8206 -0.3588 -0.1798 0.2429  48   LYS A CE  
1790  N NZ  . LYS D 51   ? 1.0450 0.7818 0.8210 -0.3713 -0.1736 0.2457  48   LYS A NZ  
1791  N N   . GLU D 52   ? 1.3000 0.6081 0.8267 -0.3105 -0.2442 0.2068  49   GLU A N   
1792  C CA  . GLU D 52   ? 1.3737 0.6156 0.8557 -0.2980 -0.2565 0.1962  49   GLU A CA  
1793  C C   . GLU D 52   ? 1.4109 0.6089 0.8735 -0.2616 -0.2548 0.1869  49   GLU A C   
1794  O O   . GLU D 52   ? 1.4586 0.6196 0.9011 -0.2379 -0.2567 0.1751  49   GLU A O   
1795  C CB  . GLU D 52   ? 1.4509 0.6600 0.8928 -0.3237 -0.2753 0.2014  49   GLU A CB  
1796  C CG  . GLU D 52   ? 1.4519 0.6951 0.9030 -0.3569 -0.2802 0.2088  49   GLU A CG  
1797  C CD  . GLU D 52   ? 1.5070 0.7246 0.9204 -0.3850 -0.2992 0.2169  49   GLU A CD  
1798  O OE1 . GLU D 52   ? 1.4826 0.7301 0.9065 -0.4034 -0.2998 0.2285  49   GLU A OE1 
1799  O OE2 . GLU D 52   ? 1.5795 0.7464 0.9510 -0.3884 -0.3141 0.2120  49   GLU A OE2 
1800  N N   . LEU D 53   ? 1.3904 0.5948 0.8587 -0.2553 -0.2512 0.1921  50   LEU A N   
1801  C CA  . LEU D 53   ? 1.3974 0.5618 0.8443 -0.2209 -0.2508 0.1844  50   LEU A CA  
1802  C C   . LEU D 53   ? 1.3875 0.5772 0.8655 -0.1914 -0.2352 0.1790  50   LEU A C   
1803  O O   . LEU D 53   ? 1.4252 0.5821 0.8840 -0.1579 -0.2349 0.1691  50   LEU A O   
1804  C CB  . LEU D 53   ? 1.3831 0.5431 0.8216 -0.2265 -0.2541 0.1926  50   LEU A CB  
1805  C CG  . LEU D 53   ? 1.4183 0.5410 0.8341 -0.1923 -0.2542 0.1862  50   LEU A CG  
1806  C CD1 . LEU D 53   ? 1.4953 0.5527 0.8608 -0.1728 -0.2664 0.1740  50   LEU A CD1 
1807  C CD2 . LEU D 53   ? 1.4539 0.5763 0.8634 -0.2035 -0.2578 0.1957  50   LEU A CD2 
1808  N N   . LYS D 54   ? 1.3221 0.5712 0.8464 -0.2026 -0.2226 0.1853  51   LYS A N   
1809  C CA  . LYS D 54   ? 1.2362 0.5343 0.8015 -0.1727 -0.2042 0.1748  51   LYS A CA  
1810  C C   . LYS D 54   ? 1.1966 0.4744 0.7520 -0.1455 -0.2025 0.1601  51   LYS A C   
1811  O O   . LYS D 54   ? 1.1565 0.4373 0.7161 -0.1119 -0.1951 0.1511  51   LYS A O   
1812  C CB  . LYS D 54   ? 1.2110 0.5878 0.8300 -0.1889 -0.1901 0.1786  51   LYS A CB  
1813  C CG  . LYS D 54   ? 1.1834 0.6109 0.8436 -0.1628 -0.1723 0.1665  51   LYS A CG  
1814  C CD  . LYS D 54   ? 1.1498 0.6408 0.8518 -0.1798 -0.1620 0.1688  51   LYS A CD  
1815  C CE  . LYS D 54   ? 1.1280 0.6587 0.8633 -0.1557 -0.1470 0.1565  51   LYS A CE  
1816  N NZ  . LYS D 54   ? 1.0867 0.6701 0.8554 -0.1706 -0.1389 0.1575  51   LYS A NZ  
1817  N N   . PRO D 55   ? 1.2026 0.4624 0.7453 -0.1572 -0.2090 0.1574  52   PRO A N   
1818  C CA  . PRO D 55   ? 1.1997 0.4390 0.7308 -0.1287 -0.2076 0.1432  52   PRO A CA  
1819  C C   . PRO D 55   ? 1.3083 0.4750 0.7859 -0.1041 -0.2199 0.1382  52   PRO A C   
1820  O O   . PRO D 55   ? 1.2966 0.4601 0.7715 -0.0697 -0.2145 0.1265  52   PRO A O   
1821  C CB  . PRO D 55   ? 1.2031 0.4350 0.7281 -0.1523 -0.2142 0.1437  52   PRO A CB  
1822  C CG  . PRO D 55   ? 1.1917 0.4681 0.7444 -0.1885 -0.2122 0.1565  52   PRO A CG  
1823  C CD  . PRO D 55   ? 1.2180 0.4827 0.7596 -0.1958 -0.2167 0.1668  52   PRO A CD  
1824  N N   . ILE D 56   ? 1.3999 0.5190 0.8382 -0.1192 -0.2349 0.1449  53   ILE A N   
1825  C CA  . ILE D 56   ? 1.3477 0.4122 0.7395 -0.0931 -0.2443 0.1365  53   ILE A CA  
1826  C C   . ILE D 56   ? 1.5505 0.6250 0.9511 -0.0610 -0.2355 0.1353  53   ILE A C   
1827  O O   . ILE D 56   ? 1.3506 0.4037 0.7315 -0.0243 -0.2348 0.1249  53   ILE A O   
1828  C CB  . ILE D 56   ? 1.6272 0.6551 0.9823 -0.1181 -0.2602 0.1416  53   ILE A CB  
1829  C CG1 . ILE D 56   ? 1.6393 0.6626 0.9864 -0.1505 -0.2694 0.1437  53   ILE A CG1 
1830  C CG2 . ILE D 56   ? 1.4723 0.4410 0.7757 -0.0906 -0.2707 0.1324  53   ILE A CG2 
1831  C CD1 . ILE D 56   ? 1.4720 0.4700 0.7888 -0.1813 -0.2851 0.1516  53   ILE A CD1 
1832  N N   . ILE D 57   ? 1.4244 0.5350 0.8547 -0.0736 -0.2285 0.1463  54   ILE A N   
1833  C CA  . ILE D 57   ? 1.4045 0.5400 0.8511 -0.0448 -0.2182 0.1441  54   ILE A CA  
1834  C C   . ILE D 57   ? 1.3669 0.5562 0.8521 -0.0166 -0.2012 0.1323  54   ILE A C   
1835  O O   . ILE D 57   ? 1.3679 0.5606 0.8498 0.0178  -0.1961 0.1256  54   ILE A O   
1836  C CB  . ILE D 57   ? 1.3754 0.5539 0.8540 -0.0666 -0.2119 0.1557  54   ILE A CB  
1837  C CG1 . ILE D 57   ? 1.4415 0.5737 0.8829 -0.0927 -0.2278 0.1662  54   ILE A CG1 
1838  C CG2 . ILE D 57   ? 1.3475 0.5615 0.8491 -0.0378 -0.1996 0.1525  54   ILE A CG2 
1839  C CD1 . ILE D 57   ? 1.4224 0.5895 0.8885 -0.1124 -0.2235 0.1793  54   ILE A CD1 
1840  N N   . ASP D 58   ? 1.3305 0.5635 0.8516 -0.0310 -0.1926 0.1302  55   ASP A N   
1841  C CA  . ASP D 58   ? 1.3129 0.5970 0.8703 -0.0080 -0.1771 0.1200  55   ASP A CA  
1842  C C   . ASP D 58   ? 1.3680 0.6158 0.8934 0.0253  -0.1812 0.1088  55   ASP A C   
1843  O O   . ASP D 58   ? 1.3323 0.6188 0.8808 0.0517  -0.1692 0.1011  55   ASP A O   
1844  C CB  . ASP D 58   ? 1.3024 0.6311 0.8971 -0.0308 -0.1694 0.1201  55   ASP A CB  
1845  C CG  . ASP D 58   ? 1.2744 0.6602 0.9124 -0.0525 -0.1597 0.1285  55   ASP A CG  
1846  O OD1 . ASP D 58   ? 1.2668 0.6762 0.9201 -0.0417 -0.1530 0.1306  55   ASP A OD1 
1847  O OD2 . ASP D 58   ? 1.2565 0.6643 0.9120 -0.0793 -0.1589 0.1330  55   ASP A OD2 
1848  N N   . ARG D 59   ? 1.4721 0.6469 0.9431 0.0245  -0.1983 0.1079  56   ARG A N   
1849  C CA  . ARG D 59   ? 1.5424 0.6788 0.9773 0.0597  -0.2032 0.0970  56   ARG A CA  
1850  C C   . ARG D 59   ? 1.5579 0.7009 0.9867 0.0968  -0.1984 0.0936  56   ARG A C   
1851  O O   . ARG D 59   ? 1.5641 0.7186 0.9910 0.1306  -0.1929 0.0842  56   ARG A O   
1852  C CB  . ARG D 59   ? 1.6364 0.6854 1.0071 0.0520  -0.2247 0.0974  56   ARG A CB  
1853  C CG  . ARG D 59   ? 1.6466 0.6901 1.0202 0.0141  -0.2307 0.1007  56   ARG A CG  
1854  C CD  . ARG D 59   ? 1.7183 0.7093 1.0437 0.0176  -0.2444 0.0912  56   ARG A CD  
1855  N NE  . ARG D 59   ? 1.7357 0.7160 1.0557 -0.0229 -0.2538 0.0964  56   ARG A NE  
1856  C CZ  . ARG D 59   ? 1.7696 0.7163 1.0583 -0.0472 -0.2680 0.1014  56   ARG A CZ  
1857  N NH1 . ARG D 59   ? 1.7898 0.7061 1.0484 -0.0350 -0.2744 0.1011  56   ARG A NH1 
1858  N NH2 . ARG D 59   ? 1.7791 0.7241 1.0657 -0.0837 -0.2760 0.1068  56   ARG A NH2 
1859  N N   . ILE D 60   ? 1.5824 0.7217 1.0087 0.0912  -0.2003 0.1017  57   ILE A N   
1860  C CA  . ILE D 60   ? 1.5822 0.7322 1.0046 0.1254  -0.1955 0.0994  57   ILE A CA  
1861  C C   . ILE D 60   ? 1.5106 0.7455 0.9911 0.1381  -0.1753 0.0959  57   ILE A C   
1862  O O   . ILE D 60   ? 1.5302 0.7831 1.0098 0.1733  -0.1695 0.0891  57   ILE A O   
1863  C CB  . ILE D 60   ? 1.6060 0.7337 1.0140 0.1133  -0.2021 0.1095  57   ILE A CB  
1864  C CG1 . ILE D 60   ? 1.6932 0.7454 1.0467 0.0963  -0.2212 0.1115  57   ILE A CG1 
1865  C CG2 . ILE D 60   ? 1.6175 0.7573 1.0207 0.1495  -0.1973 0.1072  57   ILE A CG2 
1866  C CD1 . ILE D 60   ? 1.7286 0.7664 1.0710 0.0804  -0.2268 0.1201  57   ILE A CD1 
1867  N N   . TYR D 61   ? 1.3658 0.6545 0.8959 0.1096  -0.1651 0.1011  58   TYR A N   
1868  C CA  . TYR D 61   ? 1.2400 0.6052 0.8228 0.1179  -0.1474 0.0983  58   TYR A CA  
1869  C C   . TYR D 61   ? 1.1975 0.5790 0.7873 0.1340  -0.1421 0.0888  58   TYR A C   
1870  O O   . TYR D 61   ? 1.1482 0.5667 0.7525 0.1608  -0.1330 0.0838  58   TYR A O   
1871  C CB  . TYR D 61   ? 1.1697 0.5809 0.7974 0.0842  -0.1393 0.1054  58   TYR A CB  
1872  C CG  . TYR D 61   ? 1.1859 0.5949 0.8145 0.0698  -0.1418 0.1151  58   TYR A CG  
1873  C CD1 . TYR D 61   ? 1.1949 0.6342 0.8385 0.0866  -0.1347 0.1165  58   TYR A CD1 
1874  C CD2 . TYR D 61   ? 1.2101 0.5899 0.8254 0.0384  -0.1512 0.1235  58   TYR A CD2 
1875  C CE1 . TYR D 61   ? 1.2019 0.6397 0.8464 0.0738  -0.1368 0.1254  58   TYR A CE1 
1876  C CE2 . TYR D 61   ? 1.2319 0.6119 0.8482 0.0250  -0.1534 0.1331  58   TYR A CE2 
1877  C CZ  . TYR D 61   ? 1.2265 0.6345 0.8573 0.0434  -0.1460 0.1336  58   TYR A CZ  
1878  O OH  . TYR D 61   ? 1.2421 0.6507 0.8739 0.0306  -0.1480 0.1430  58   TYR A OH  
1879  N N   . LYS D 62   ? 1.2002 0.5566 0.7797 0.1169  -0.1480 0.0867  59   LYS A N   
1880  C CA  . LYS D 62   ? 1.1685 0.5408 0.7558 0.1297  -0.1430 0.0780  59   LYS A CA  
1881  C C   . LYS D 62   ? 1.2421 0.5887 0.7939 0.1701  -0.1468 0.0701  59   LYS A C   
1882  O O   . LYS D 62   ? 1.2350 0.6242 0.8064 0.1924  -0.1366 0.0645  59   LYS A O   
1883  C CB  . LYS D 62   ? 1.1718 0.5133 0.7473 0.1043  -0.1509 0.0776  59   LYS A CB  
1884  C CG  . LYS D 62   ? 1.1307 0.5084 0.7447 0.0672  -0.1454 0.0846  59   LYS A CG  
1885  C CD  . LYS D 62   ? 1.1502 0.5016 0.7521 0.0439  -0.1533 0.0843  59   LYS A CD  
1886  C CE  . LYS D 62   ? 1.2359 0.5098 0.7819 0.0360  -0.1725 0.0873  59   LYS A CE  
1887  N NZ  . LYS D 62   ? 1.2466 0.4956 0.7796 0.0111  -0.1811 0.0878  59   LYS A NZ  
1888  N N   . THR D 63   ? 1.3362 0.6134 0.8336 0.1806  -0.1619 0.0700  60   THR A N   
1889  C CA  . THR D 63   ? 1.4012 0.6489 0.8584 0.2221  -0.1669 0.0622  60   THR A CA  
1890  C C   . THR D 63   ? 1.4092 0.7048 0.8843 0.2514  -0.1565 0.0622  60   THR A C   
1891  O O   . THR D 63   ? 1.4004 0.7276 0.8809 0.2815  -0.1494 0.0559  60   THR A O   
1892  C CB  . THR D 63   ? 1.5007 0.6577 0.8912 0.2259  -0.1869 0.0626  60   THR A CB  
1893  O OG1 . THR D 63   ? 1.5475 0.6644 0.9243 0.1919  -0.1971 0.0648  60   THR A OG1 
1894  C CG2 . THR D 63   ? 1.5445 0.6690 0.8899 0.2689  -0.1926 0.0524  60   THR A CG2 
1895  N N   . TYR D 64   ? 1.4305 0.7351 0.9156 0.2423  -0.1554 0.0698  61   TYR A N   
1896  C CA  . TYR D 64   ? 1.4359 0.7849 0.9361 0.2689  -0.1466 0.0706  61   TYR A CA  
1897  C C   . TYR D 64   ? 1.3978 0.8313 0.9550 0.2684  -0.1292 0.0698  61   TYR A C   
1898  O O   . TYR D 64   ? 1.3861 0.8577 0.9495 0.2988  -0.1222 0.0666  61   TYR A O   
1899  C CB  . TYR D 64   ? 1.4215 0.7632 0.9228 0.2553  -0.1490 0.0794  61   TYR A CB  
1900  C CG  . TYR D 64   ? 1.3724 0.7655 0.8943 0.2784  -0.1394 0.0812  61   TYR A CG  
1901  C CD1 . TYR D 64   ? 1.4050 0.7789 0.8899 0.3184  -0.1439 0.0779  61   TYR A CD1 
1902  C CD2 . TYR D 64   ? 1.3073 0.7680 0.8835 0.2607  -0.1262 0.0863  61   TYR A CD2 
1903  C CE1 . TYR D 64   ? 1.3839 0.8089 0.8881 0.3390  -0.1352 0.0802  61   TYR A CE1 
1904  C CE2 . TYR D 64   ? 1.2870 0.7950 0.8813 0.2798  -0.1182 0.0884  61   TYR A CE2 
1905  C CZ  . TYR D 64   ? 1.3246 0.8168 0.8841 0.3183  -0.1225 0.0857  61   TYR A CZ  
1906  O OH  . TYR D 64   ? 1.3005 0.8440 0.8788 0.3368  -0.1145 0.0885  61   TYR A OH  
1907  N N   . ALA D 65   ? 1.3798 0.8442 0.9775 0.2342  -0.1225 0.0730  62   ALA A N   
1908  C CA  . ALA D 65   ? 1.3353 0.8738 0.9834 0.2316  -0.1075 0.0722  62   ALA A CA  
1909  C C   . ALA D 65   ? 1.3513 0.9001 0.9947 0.2518  -0.1048 0.0643  62   ALA A C   
1910  O O   . ALA D 65   ? 1.3395 0.9424 1.0050 0.2698  -0.0949 0.0629  62   ALA A O   
1911  C CB  . ALA D 65   ? 1.2958 0.8574 0.9815 0.1926  -0.1024 0.0767  62   ALA A CB  
1912  N N   . ASP D 66   ? 1.3912 0.8896 1.0050 0.2484  -0.1139 0.0595  63   ASP A N   
1913  C CA  . ASP D 66   ? 1.4220 0.9265 1.0282 0.2685  -0.1121 0.0517  63   ASP A CA  
1914  C C   . ASP D 66   ? 1.4499 0.9532 1.0271 0.3127  -0.1135 0.0475  63   ASP A C   
1915  O O   . ASP D 66   ? 1.4442 0.9927 1.0356 0.3333  -0.1052 0.0440  63   ASP A O   
1916  C CB  . ASP D 66   ? 1.5066 0.9510 1.0820 0.2558  -0.1234 0.0476  63   ASP A CB  
1917  C CG  . ASP D 66   ? 1.5533 1.0153 1.1354 0.2650  -0.1190 0.0404  63   ASP A CG  
1918  O OD1 . ASP D 66   ? 1.5839 1.0658 1.1579 0.2987  -0.1154 0.0357  63   ASP A OD1 
1919  O OD2 . ASP D 66   ? 1.5575 1.0158 1.1530 0.2387  -0.1191 0.0399  63   ASP A OD2 
1920  N N   . GLN D 67   ? 1.4751 0.9288 1.0105 0.3282  -0.1241 0.0484  64   GLN A N   
1921  C CA  . GLN D 67   ? 1.4636 0.9148 0.9674 0.3734  -0.1260 0.0445  64   GLN A CA  
1922  C C   . GLN D 67   ? 1.3661 0.8972 0.9089 0.3868  -0.1123 0.0485  64   GLN A C   
1923  O O   . GLN D 67   ? 1.3598 0.9254 0.8992 0.4201  -0.1075 0.0452  64   GLN A O   
1924  C CB  . GLN D 67   ? 1.5167 0.8936 0.9654 0.3853  -0.1411 0.0451  64   GLN A CB  
1925  C CG  . GLN D 67   ? 1.5889 0.8804 0.9852 0.3819  -0.1573 0.0401  64   GLN A CG  
1926  C CD  . GLN D 67   ? 1.6702 0.9001 1.0209 0.3793  -0.1699 0.0396  64   GLN A CD  
1927  O OE1 . GLN D 67   ? 1.7312 0.9316 1.0386 0.4025  -0.1760 0.0304  64   GLN A OE1 
1928  N NE2 . GLN D 67   ? 1.6734 0.8860 1.0330 0.3496  -0.1738 0.0493  64   GLN A NE2 
1929  N N   . CYS D 68   ? 1.2937 0.8565 0.8727 0.3612  -0.1063 0.0561  65   CYS A N   
1930  C CA  . CYS D 68   ? 1.2263 0.8638 0.8419 0.3702  -0.0943 0.0607  65   CYS A CA  
1931  C C   . CYS D 68   ? 1.1545 0.8584 0.8116 0.3648  -0.0822 0.0598  65   CYS A C   
1932  O O   . CYS D 68   ? 1.0974 0.8603 0.7711 0.3846  -0.0742 0.0615  65   CYS A O   
1933  C CB  . CYS D 68   ? 1.2118 0.8620 0.8534 0.3429  -0.0919 0.0687  65   CYS A CB  
1934  S SG  . CYS D 68   ? 1.3062 0.8943 0.9033 0.3535  -0.1042 0.0718  65   CYS A SG  
1935  N N   . LEU D 69   ? 1.1375 0.8340 0.8107 0.3379  -0.0811 0.0579  66   LEU A N   
1936  C CA  . LEU D 69   ? 1.0796 0.8339 0.7897 0.3309  -0.0705 0.0572  66   LEU A CA  
1937  C C   . LEU D 69   ? 1.1376 0.8968 0.8277 0.3618  -0.0705 0.0507  66   LEU A C   
1938  O O   . LEU D 69   ? 1.1327 0.9463 0.8513 0.3613  -0.0614 0.0509  66   LEU A O   
1939  C CB  . LEU D 69   ? 0.9974 0.7420 0.7302 0.2928  -0.0694 0.0573  66   LEU A CB  
1940  C CG  . LEU D 69   ? 0.9057 0.6600 0.6661 0.2608  -0.0670 0.0641  66   LEU A CG  
1941  C CD1 . LEU D 69   ? 0.8503 0.5963 0.6294 0.2275  -0.0662 0.0637  66   LEU A CD1 
1942  C CD2 . LEU D 69   ? 0.8420 0.6636 0.6380 0.2609  -0.0569 0.0696  66   LEU A CD2 
1943  N N   . GLN D 70   ? 1.2088 0.9121 0.8489 0.3890  -0.0810 0.0451  67   GLN A N   
1944  C CA  . GLN D 70   ? 1.2692 0.9756 0.8867 0.4215  -0.0815 0.0384  67   GLN A CA  
1945  C C   . GLN D 70   ? 1.2879 1.0544 0.9098 0.4563  -0.0746 0.0407  67   GLN A C   
1946  O O   . GLN D 70   ? 1.3027 1.1035 0.9250 0.4779  -0.0701 0.0377  67   GLN A O   
1947  C CB  . GLN D 70   ? 1.3608 0.9819 0.9182 0.4398  -0.0963 0.0313  67   GLN A CB  
1948  C CG  . GLN D 70   ? 1.3784 0.9433 0.9280 0.4074  -0.1039 0.0288  67   GLN A CG  
1949  C CD  . GLN D 70   ? 1.4561 0.9334 0.9422 0.4240  -0.1203 0.0223  67   GLN A CD  
1950  O OE1 . GLN D 70   ? 1.4977 0.9607 0.9506 0.4584  -0.1239 0.0154  67   GLN A OE1 
1951  N NE2 . GLN D 70   ? 1.4776 0.8952 0.9442 0.3995  -0.1309 0.0250  67   GLN A NE2 
1952  N N   . LEU D 71   ? 1.2979 1.0805 0.9231 0.4621  -0.0737 0.0463  68   LEU A N   
1953  C CA  . LEU D 71   ? 1.3182 1.1609 0.9472 0.4947  -0.0677 0.0495  68   LEU A CA  
1954  C C   . LEU D 71   ? 1.2693 1.1982 0.9543 0.4744  -0.0548 0.0578  68   LEU A C   
1955  O O   . LEU D 71   ? 1.2594 1.2472 0.9528 0.4965  -0.0493 0.0623  68   LEU A O   
1956  C CB  . LEU D 71   ? 1.3679 1.1806 0.9651 0.5162  -0.0747 0.0511  68   LEU A CB  
1957  C CG  . LEU D 71   ? 1.4480 1.1733 0.9835 0.5356  -0.0882 0.0428  68   LEU A CG  
1958  C CD1 . LEU D 71   ? 1.4574 1.1142 0.9807 0.5086  -0.0981 0.0455  68   LEU A CD1 
1959  C CD2 . LEU D 71   ? 1.4949 1.2327 1.0012 0.5669  -0.0871 0.0383  68   LEU A CD2 
1960  N N   . VAL D 72   ? 1.2372 1.1748 0.9584 0.4335  -0.0505 0.0602  69   VAL A N   
1961  C CA  . VAL D 72   ? 1.1709 1.1809 0.9408 0.4115  -0.0402 0.0682  69   VAL A CA  
1962  C C   . VAL D 72   ? 1.1472 1.2195 0.9338 0.4229  -0.0326 0.0690  69   VAL A C   
1963  O O   . VAL D 72   ? 1.1555 1.2164 0.9415 0.4179  -0.0322 0.0641  69   VAL A O   
1964  C CB  . VAL D 72   ? 1.1023 1.0979 0.9007 0.3667  -0.0389 0.0700  69   VAL A CB  
1965  C CG1 . VAL D 72   ? 1.0400 1.1048 0.8835 0.3450  -0.0297 0.0779  69   VAL A CG1 
1966  C CG2 . VAL D 72   ? 1.1150 1.0528 0.8966 0.3554  -0.0465 0.0702  69   VAL A CG2 
1967  N N   . GLN D 73   ? 1.1387 1.2791 0.9402 0.4374  -0.0267 0.0758  70   GLN A N   
1968  C CA  . GLN D 73   ? 1.1096 1.3213 0.9314 0.4445  -0.0189 0.0794  70   GLN A CA  
1969  C C   . GLN D 73   ? 1.0385 1.3195 0.8998 0.4232  -0.0121 0.0903  70   GLN A C   
1970  O O   . GLN D 73   ? 1.0511 1.3597 0.9106 0.4375  -0.0119 0.0955  70   GLN A O   
1971  C CB  . GLN D 73   ? 1.1836 1.4135 0.9745 0.4927  -0.0199 0.0770  70   GLN A CB  
1972  C CG  . GLN D 73   ? 1.2730 1.4725 1.0393 0.5102  -0.0225 0.0682  70   GLN A CG  
1973  C CD  . GLN D 73   ? 1.3579 1.4606 1.0860 0.5124  -0.0330 0.0585  70   GLN A CD  
1974  O OE1 . GLN D 73   ? 1.4020 1.4626 1.0912 0.5402  -0.0405 0.0549  70   GLN A OE1 
1975  N NE2 . GLN D 73   ? 1.3579 1.4245 1.0951 0.4828  -0.0343 0.0545  70   GLN A NE2 
1976  N N   . LEU D 74   ? 0.9914 1.2987 0.8859 0.3893  -0.0073 0.0937  71   LEU A N   
1977  C CA  . LEU D 74   ? 0.9190 1.2851 0.8487 0.3644  -0.0023 0.1040  71   LEU A CA  
1978  C C   . LEU D 74   ? 0.8734 1.2981 0.8267 0.3525  0.0036  0.1089  71   LEU A C   
1979  O O   . LEU D 74   ? 0.8908 1.3017 0.8387 0.3546  0.0042  0.1037  71   LEU A O   
1980  C CB  . LEU D 74   ? 0.8485 1.1795 0.7944 0.3273  -0.0040 0.1044  71   LEU A CB  
1981  C CG  . LEU D 74   ? 0.8328 1.1118 0.7603 0.3320  -0.0096 0.1018  71   LEU A CG  
1982  C CD1 . LEU D 74   ? 0.7848 1.0408 0.7321 0.2944  -0.0102 0.1033  71   LEU A CD1 
1983  C CD2 . LEU D 74   ? 0.8327 1.1481 0.7543 0.3555  -0.0094 0.1075  71   LEU A CD2 
1984  N N   . ASP D 75   ? 0.8411 1.3312 0.8197 0.3387  0.0074  0.1196  72   ASP A N   
1985  C CA  . ASP D 75   ? 0.8308 1.3794 0.8335 0.3206  0.0121  0.1268  72   ASP A CA  
1986  C C   . ASP D 75   ? 0.8118 1.3464 0.8380 0.2764  0.0117  0.1293  72   ASP A C   
1987  O O   . ASP D 75   ? 0.8038 1.3544 0.8434 0.2590  0.0110  0.1357  72   ASP A O   
1988  C CB  . ASP D 75   ? 0.8443 1.4768 0.8568 0.3330  0.0153  0.1383  72   ASP A CB  
1989  C CG  . ASP D 75   ? 0.8717 1.5670 0.9024 0.3211  0.0195  0.1460  72   ASP A CG  
1990  O OD1 . ASP D 75   ? 0.8934 1.5696 0.9354 0.2935  0.0199  0.1443  72   ASP A OD1 
1991  O OD2 . ASP D 75   ? 0.8878 1.6533 0.9206 0.3397  0.0223  0.1543  72   ASP A OD2 
1992  N N   . TRP D 76   ? 0.7997 1.3040 0.8290 0.2597  0.0120  0.1240  73   TRP A N   
1993  C CA  . TRP D 76   ? 0.7692 1.2508 0.8154 0.2216  0.0111  0.1244  73   TRP A CA  
1994  C C   . TRP D 76   ? 0.7708 1.3074 0.8395 0.1960  0.0134  0.1343  73   TRP A C   
1995  O O   . TRP D 76   ? 0.7653 1.2829 0.8448 0.1659  0.0124  0.1342  73   TRP A O   
1996  C CB  . TRP D 76   ? 0.7409 1.1625 0.7780 0.2163  0.0098  0.1141  73   TRP A CB  
1997  C CG  . TRP D 76   ? 0.7302 1.0939 0.7423 0.2381  0.0060  0.1050  73   TRP A CG  
1998  C CD1 . TRP D 76   ? 0.7459 1.0967 0.7340 0.2708  0.0049  0.0993  73   TRP A CD1 
1999  C CD2 . TRP D 76   ? 0.7277 1.0371 0.7335 0.2280  0.0020  0.1009  73   TRP A CD2 
2000  N NE1 . TRP D 76   ? 0.7662 1.0543 0.7318 0.2803  -0.0004 0.0922  73   TRP A NE1 
2001  C CE2 . TRP D 76   ? 0.7608 1.0248 0.7380 0.2537  -0.0020 0.0935  73   TRP A CE2 
2002  C CE3 . TRP D 76   ? 0.7005 0.9953 0.7203 0.2001  0.0009  0.1032  73   TRP A CE3 
2003  C CZ2 . TRP D 76   ? 0.7725 0.9789 0.7357 0.2497  -0.0072 0.0892  73   TRP A CZ2 
2004  C CZ3 . TRP D 76   ? 0.7007 0.9422 0.7085 0.1982  -0.0032 0.0987  73   TRP A CZ3 
2005  C CH2 . TRP D 76   ? 0.7384 0.9370 0.7187 0.2216  -0.0073 0.0923  73   TRP A CH2 
2006  N N   . GLU D 77   ? 0.8300 1.4342 0.9040 0.2071  0.0159  0.1433  74   GLU A N   
2007  C CA  . GLU D 77   ? 0.8522 1.5098 0.9452 0.1808  0.0170  0.1540  74   GLU A CA  
2008  C C   . GLU D 77   ? 0.8205 1.4826 0.9270 0.1495  0.0139  0.1608  74   GLU A C   
2009  O O   . GLU D 77   ? 0.8021 1.4684 0.9192 0.1180  0.0123  0.1652  74   GLU A O   
2010  C CB  . GLU D 77   ? 0.9083 1.6427 1.0033 0.2005  0.0201  0.1633  74   GLU A CB  
2011  C CG  . GLU D 77   ? 0.9528 1.7461 1.0653 0.1728  0.0207  0.1757  74   GLU A CG  
2012  C CD  . GLU D 77   ? 1.0187 1.7905 1.1324 0.1583  0.0215  0.1719  74   GLU A CD  
2013  O OE1 . GLU D 77   ? 1.0565 1.7938 1.1575 0.1803  0.0233  0.1614  74   GLU A OE1 
2014  O OE2 . GLU D 77   ? 1.0280 1.8155 1.1535 0.1246  0.0196  0.1793  74   GLU A OE2 
2015  N N   . ASN D 78   ? 0.8064 1.4652 0.9101 0.1582  0.0124  0.1617  75   ASN A N   
2016  C CA  . ASN D 78   ? 0.7692 1.4312 0.8839 0.1302  0.0090  0.1678  75   ASN A CA  
2017  C C   . ASN D 78   ? 0.7312 1.3288 0.8457 0.1067  0.0063  0.1604  75   ASN A C   
2018  O O   . ASN D 78   ? 0.7096 1.3092 0.8328 0.0762  0.0034  0.1653  75   ASN A O   
2019  C CB  . ASN D 78   ? 0.7979 1.4694 0.9087 0.1475  0.0082  0.1698  75   ASN A CB  
2020  C CG  . ASN D 78   ? 0.8229 1.5677 0.9354 0.1685  0.0105  0.1790  75   ASN A CG  
2021  O OD1 . ASN D 78   ? 0.8088 1.6069 0.9335 0.1530  0.0092  0.1906  75   ASN A OD1 
2022  N ND2 . ASN D 78   ? 0.8532 1.6016 0.9517 0.2042  0.0134  0.1742  75   ASN A ND2 
2023  N N   . LEU D 79   ? 0.7135 1.2538 0.8161 0.1206  0.0068  0.1490  76   LEU A N   
2024  C CA  . LEU D 79   ? 0.6514 1.1349 0.7536 0.1004  0.0046  0.1422  76   LEU A CA  
2025  C C   . LEU D 79   ? 0.5951 1.0782 0.7031 0.0791  0.0048  0.1424  76   LEU A C   
2026  O O   . LEU D 79   ? 0.5858 1.0460 0.6976 0.0539  0.0022  0.1421  76   LEU A O   
2027  C CB  . LEU D 79   ? 0.6157 1.0432 0.7030 0.1195  0.0045  0.1313  76   LEU A CB  
2028  C CG  . LEU D 79   ? 0.5441 0.9151 0.6300 0.1017  0.0024  0.1246  76   LEU A CG  
2029  C CD1 . LEU D 79   ? 0.4870 0.8555 0.5803 0.0827  -0.0002 0.1287  76   LEU A CD1 
2030  C CD2 . LEU D 79   ? 0.5486 0.8703 0.6183 0.1203  0.0014  0.1157  76   LEU A CD2 
2031  N N   . SER D 80   ? 0.5812 1.0891 0.6882 0.0900  0.0077  0.1429  77   SER A N   
2032  C CA  . SER D 80   ? 0.5781 1.0875 0.6897 0.0704  0.0078  0.1437  77   SER A CA  
2033  C C   . SER D 80   ? 0.5761 1.1222 0.6977 0.0416  0.0048  0.1549  77   SER A C   
2034  O O   . SER D 80   ? 0.5772 1.1029 0.6996 0.0168  0.0022  0.1548  77   SER A O   
2035  C CB  . SER D 80   ? 0.6072 1.1410 0.7154 0.0897  0.0115  0.1427  77   SER A CB  
2036  O OG  . SER D 80   ? 0.6199 1.1603 0.7327 0.0702  0.0116  0.1448  77   SER A OG  
2037  N N   . ALA D 81   ? 0.5644 1.1640 0.6917 0.0443  0.0046  0.1650  78   ALA A N   
2038  C CA  . ALA D 81   ? 0.5413 1.1777 0.6762 0.0149  0.0005  0.1770  78   ALA A CA  
2039  C C   . ALA D 81   ? 0.5130 1.1109 0.6465 -0.0079 -0.0047 0.1758  78   ALA A C   
2040  O O   . ALA D 81   ? 0.5349 1.1318 0.6680 -0.0370 -0.0096 0.1811  78   ALA A O   
2041  C CB  . ALA D 81   ? 0.5374 1.2437 0.6787 0.0239  0.0013  0.1886  78   ALA A CB  
2042  N N   . ALA D 82   ? 0.4816 1.0467 0.6119 0.0053  -0.0043 0.1690  79   ALA A N   
2043  C CA  . ALA D 82   ? 0.4918 1.0193 0.6197 -0.0134 -0.0088 0.1671  79   ALA A CA  
2044  C C   . ALA D 82   ? 0.5373 1.0119 0.6592 -0.0260 -0.0100 0.1589  79   ALA A C   
2045  O O   . ALA D 82   ? 0.5385 0.9917 0.6567 -0.0485 -0.0150 0.1598  79   ALA A O   
2046  C CB  . ALA D 82   ? 0.4965 1.0050 0.6226 0.0048  -0.0078 0.1626  79   ALA A CB  
2047  N N   . ILE D 83   ? 0.5715 1.0242 0.6904 -0.0109 -0.0060 0.1507  80   ILE A N   
2048  C CA  . ILE D 83   ? 0.5942 1.0028 0.7078 -0.0219 -0.0068 0.1434  80   ILE A CA  
2049  C C   . ILE D 83   ? 0.5536 0.9789 0.6666 -0.0443 -0.0097 0.1495  80   ILE A C   
2050  O O   . ILE D 83   ? 0.5490 0.9439 0.6554 -0.0634 -0.0137 0.1478  80   ILE A O   
2051  C CB  . ILE D 83   ? 0.6483 1.0317 0.7582 -0.0005 -0.0024 0.1338  80   ILE A CB  
2052  C CG1 . ILE D 83   ? 0.3693 0.7279 0.4756 0.0180  -0.0014 0.1282  80   ILE A CG1 
2053  C CG2 . ILE D 83   ? 0.3620 0.7064 0.4672 -0.0117 -0.0030 0.1270  80   ILE A CG2 
2054  C CD1 . ILE D 83   ? 0.3771 0.7072 0.4761 0.0377  0.0014  0.1192  80   ILE A CD1 
2055  N N   . ASP D 84   ? 0.5267 1.0007 0.6447 -0.0418 -0.0080 0.1570  81   ASP A N   
2056  C CA  . ASP D 84   ? 0.5298 1.0225 0.6463 -0.0644 -0.0112 0.1643  81   ASP A CA  
2057  C C   . ASP D 84   ? 0.5273 1.0245 0.6399 -0.0927 -0.0189 0.1729  81   ASP A C   
2058  O O   . ASP D 84   ? 0.5138 0.9887 0.6170 -0.1152 -0.0242 0.1740  81   ASP A O   
2059  C CB  . ASP D 84   ? 0.5679 1.1191 0.6911 -0.0552 -0.0078 0.1721  81   ASP A CB  
2060  C CG  . ASP D 84   ? 0.6319 1.1735 0.7544 -0.0324 -0.0017 0.1638  81   ASP A CG  
2061  O OD1 . ASP D 84   ? 0.6393 1.1314 0.7570 -0.0212 0.0000  0.1521  81   ASP A OD1 
2062  O OD2 . ASP D 84   ? 0.6694 1.2544 0.7954 -0.0260 0.0010  0.1693  81   ASP A OD2 
2063  N N   . SER D 85   ? 0.5480 1.0717 0.6654 -0.0916 -0.0203 0.1788  82   SER A N   
2064  C CA  . SER D 85   ? 0.5647 1.0945 0.6770 -0.1189 -0.0285 0.1876  82   SER A CA  
2065  C C   . SER D 85   ? 0.5718 1.0407 0.6721 -0.1302 -0.0332 0.1799  82   SER A C   
2066  O O   . SER D 85   ? 0.5894 1.0456 0.6779 -0.1561 -0.0414 0.1848  82   SER A O   
2067  C CB  . SER D 85   ? 0.5453 1.1180 0.6660 -0.1129 -0.0286 0.1951  82   SER A CB  
2068  O OG  . SER D 85   ? 0.5251 1.1630 0.6547 -0.1079 -0.0260 0.2052  82   SER A OG  
2069  N N   . TYR D 86   ? 0.5696 1.0003 0.6705 -0.1112 -0.0289 0.1685  83   TYR A N   
2070  C CA  . TYR D 86   ? 0.5978 0.9751 0.6874 -0.1195 -0.0328 0.1614  83   TYR A CA  
2071  C C   . TYR D 86   ? 0.6191 0.9635 0.6975 -0.1297 -0.0347 0.1568  83   TYR A C   
2072  O O   . TYR D 86   ? 0.6407 0.9527 0.7043 -0.1462 -0.0414 0.1559  83   TYR A O   
2073  C CB  . TYR D 86   ? 0.6090 0.9601 0.7027 -0.0977 -0.0278 0.1520  83   TYR A CB  
2074  C CG  . TYR D 86   ? 0.6292 0.9319 0.7123 -0.1041 -0.0313 0.1454  83   TYR A CG  
2075  C CD1 . TYR D 86   ? 0.6624 0.9566 0.7352 -0.1229 -0.0389 0.1496  83   TYR A CD1 
2076  C CD2 . TYR D 86   ? 0.6027 0.8695 0.6844 -0.0912 -0.0274 0.1352  83   TYR A CD2 
2077  C CE1 . TYR D 86   ? 0.6721 0.9235 0.7331 -0.1261 -0.0421 0.1434  83   TYR A CE1 
2078  C CE2 . TYR D 86   ? 0.6201 0.8485 0.6922 -0.0956 -0.0302 0.1299  83   TYR A CE2 
2079  C CZ  . TYR D 86   ? 0.6708 0.8918 0.7323 -0.1118 -0.0373 0.1337  83   TYR A CZ  
2080  O OH  . TYR D 86   ? 0.7051 0.8891 0.7550 -0.1136 -0.0402 0.1282  83   TYR A OH  
2081  N N   . ARG D 87   ? 0.6169 0.9678 0.7003 -0.1188 -0.0293 0.1537  84   ARG A N   
2082  C CA  . ARG D 87   ? 0.6275 0.9521 0.7004 -0.1286 -0.0311 0.1503  84   ARG A CA  
2083  C C   . ARG D 87   ? 0.6371 0.9810 0.7012 -0.1544 -0.0382 0.1611  84   ARG A C   
2084  O O   . ARG D 87   ? 0.5822 0.8944 0.6304 -0.1692 -0.0435 0.1597  84   ARG A O   
2085  C CB  . ARG D 87   ? 0.6125 0.9405 0.6930 -0.1101 -0.0236 0.1444  84   ARG A CB  
2086  C CG  . ARG D 87   ? 0.6193 0.9220 0.7046 -0.0874 -0.0180 0.1339  84   ARG A CG  
2087  C CD  . ARG D 87   ? 0.6223 0.9298 0.7125 -0.0700 -0.0118 0.1288  84   ARG A CD  
2088  N NE  . ARG D 87   ? 0.6326 0.9150 0.7248 -0.0503 -0.0079 0.1198  84   ARG A NE  
2089  C CZ  . ARG D 87   ? 0.6465 0.9278 0.7407 -0.0323 -0.0033 0.1146  84   ARG A CZ  
2090  N NH1 . ARG D 87   ? 0.6491 0.9554 0.7450 -0.0294 -0.0012 0.1170  84   ARG A NH1 
2091  N NH2 . ARG D 87   ? 0.6361 0.8907 0.7288 -0.0177 -0.0014 0.1073  84   ARG A NH2 
2092  N N   . LYS D 88   ? 0.6860 1.0817 0.7585 -0.1601 -0.0390 0.1723  85   LYS A N   
2093  C CA  . LYS D 88   ? 0.7694 1.1894 0.8337 -0.1874 -0.0466 0.1848  85   LYS A CA  
2094  C C   . LYS D 88   ? 0.8461 1.2372 0.8926 -0.2105 -0.0572 0.1878  85   LYS A C   
2095  O O   . LYS D 88   ? 0.8543 1.2082 0.8806 -0.2282 -0.0646 0.1872  85   LYS A O   
2096  C CB  . LYS D 88   ? 0.7593 1.2491 0.8387 -0.1856 -0.0441 0.1966  85   LYS A CB  
2097  C CG  . LYS D 88   ? 0.7288 1.2567 0.8068 -0.2028 -0.0466 0.2078  85   LYS A CG  
2098  C CD  . LYS D 88   ? 0.7498 1.2761 0.8110 -0.2394 -0.0590 0.2194  85   LYS A CD  
2099  C CE  . LYS D 88   ? 0.7705 1.3548 0.8346 -0.2574 -0.0615 0.2348  85   LYS A CE  
2100  N NZ  . LYS D 88   ? 0.7723 1.3567 0.8380 -0.2493 -0.0561 0.2316  85   LYS A NZ  
2101  N N   . GLU D 89   ? 0.9252 1.3311 0.9769 -0.2096 -0.0586 0.1910  86   GLU A N   
2102  C CA  . GLU D 89   ? 0.9682 1.3447 1.0027 -0.2280 -0.0685 0.1926  86   GLU A CA  
2103  C C   . GLU D 89   ? 0.9787 1.3125 1.0125 -0.2096 -0.0653 0.1801  86   GLU A C   
2104  O O   . GLU D 89   ? 0.9802 1.3294 1.0309 -0.1879 -0.0575 0.1764  86   GLU A O   
2105  C CB  . GLU D 89   ? 0.9846 1.4079 1.0243 -0.2417 -0.0733 0.2055  86   GLU A CB  
2106  C CG  . GLU D 89   ? 1.0409 1.4887 1.0686 -0.2742 -0.0833 0.2199  86   GLU A CG  
2107  C CD  . GLU D 89   ? 1.0606 1.5756 1.1062 -0.2720 -0.0778 0.2299  86   GLU A CD  
2108  O OE1 . GLU D 89   ? 1.0544 1.5908 1.1192 -0.2433 -0.0664 0.2242  86   GLU A OE1 
2109  O OE2 . GLU D 89   ? 1.0778 1.6245 1.1166 -0.2992 -0.0856 0.2439  86   GLU A OE2 
2110  N N   . LYS D 90   ? 0.9862 1.2667 0.9985 -0.2179 -0.0716 0.1742  87   LYS A N   
2111  C CA  . LYS D 90   ? 0.9559 1.1969 0.9653 -0.2021 -0.0692 0.1631  87   LYS A CA  
2112  C C   . LYS D 90   ? 0.9504 1.1859 0.9521 -0.2103 -0.0758 0.1662  87   LYS A C   
2113  O O   . LYS D 90   ? 0.9836 1.1760 0.9664 -0.2131 -0.0814 0.1608  87   LYS A O   
2114  C CB  . LYS D 90   ? 0.9489 1.1383 0.9389 -0.2023 -0.0717 0.1544  87   LYS A CB  
2115  C CG  . LYS D 90   ? 0.9251 1.1155 0.9226 -0.1920 -0.0647 0.1497  87   LYS A CG  
2116  C CD  . LYS D 90   ? 0.9526 1.1509 0.9387 -0.2121 -0.0704 0.1573  87   LYS A CD  
2117  C CE  . LYS D 90   ? 0.9709 1.1616 0.9605 -0.2019 -0.0643 0.1514  87   LYS A CE  
2118  N NZ  . LYS D 90   ? 0.9627 1.1866 0.9789 -0.1803 -0.0528 0.1487  87   LYS A NZ  
2119  N N   . THR D 91   ? 0.9410 1.2217 0.9565 -0.2131 -0.0753 0.1749  88   THR A N   
2120  C CA  . THR D 91   ? 0.9557 1.2374 0.9657 -0.2213 -0.0815 0.1789  88   THR A CA  
2121  C C   . THR D 91   ? 0.9410 1.2297 0.9685 -0.1973 -0.0732 0.1734  88   THR A C   
2122  O O   . THR D 91   ? 0.9436 1.2508 0.9895 -0.1769 -0.0635 0.1701  88   THR A O   
2123  C CB  . THR D 91   ? 0.9939 1.3233 1.0060 -0.2423 -0.0876 0.1934  88   THR A CB  
2124  O OG1 . THR D 91   ? 1.0451 1.3789 1.0544 -0.2479 -0.0927 0.1969  88   THR A OG1 
2125  C CG2 . THR D 91   ? 0.9681 1.3561 1.0058 -0.2296 -0.0784 0.1986  88   THR A CG2 
2126  N N   . GLU D 92   ? 0.9332 1.2041 0.9522 -0.2001 -0.0781 0.1725  89   GLU A N   
2127  C CA  . GLU D 92   ? 0.8993 1.1733 0.9319 -0.1797 -0.0715 0.1680  89   GLU A CA  
2128  C C   . GLU D 92   ? 0.8622 1.1900 0.9156 -0.1714 -0.0665 0.1752  89   GLU A C   
2129  O O   . GLU D 92   ? 0.8482 1.1808 0.9144 -0.1505 -0.0595 0.1712  89   GLU A O   
2130  C CB  . GLU D 92   ? 0.9123 1.1579 0.9296 -0.1860 -0.0786 0.1665  89   GLU A CB  
2131  N N   . GLU D 93   ? 0.8325 1.2012 0.8880 -0.1871 -0.0705 0.1862  90   GLU A N   
2132  C CA  . GLU D 93   ? 0.7902 1.2154 0.8647 -0.1768 -0.0654 0.1934  90   GLU A CA  
2133  C C   . GLU D 93   ? 0.7547 1.1953 0.8433 -0.1542 -0.0553 0.1893  90   GLU A C   
2134  O O   . GLU D 93   ? 0.7215 1.1839 0.8229 -0.1320 -0.0486 0.1884  90   GLU A O   
2135  C CB  . GLU D 93   ? 0.7815 1.2511 0.8538 -0.2013 -0.0730 0.2075  90   GLU A CB  
2136  C CG  . GLU D 93   ? 0.7742 1.3094 0.8649 -0.1908 -0.0684 0.2164  90   GLU A CG  
2137  C CD  . GLU D 93   ? 0.7908 1.3630 0.8938 -0.1782 -0.0611 0.2184  90   GLU A CD  
2138  O OE1 . GLU D 93   ? 0.7923 1.3558 0.8887 -0.1909 -0.0630 0.2192  90   GLU A OE1 
2139  O OE2 . GLU D 93   ? 0.8071 1.4152 0.9244 -0.1542 -0.0536 0.2191  90   GLU A OE2 
2140  N N   . THR D 94   ? 0.7605 1.1879 0.8446 -0.1588 -0.0546 0.1868  91   THR A N   
2141  C CA  . THR D 94   ? 0.7524 1.1906 0.8475 -0.1375 -0.0456 0.1823  91   THR A CA  
2142  C C   . THR D 94   ? 0.7402 1.1371 0.8365 -0.1157 -0.0396 0.1699  91   THR A C   
2143  O O   . THR D 94   ? 0.7328 1.1384 0.8378 -0.0937 -0.0325 0.1660  91   THR A O   
2144  C CB  . THR D 94   ? 0.7809 1.2175 0.8704 -0.1498 -0.0469 0.1836  91   THR A CB  
2145  O OG1 . THR D 94   ? 0.8203 1.2052 0.8926 -0.1644 -0.0527 0.1782  91   THR A OG1 
2146  C CG2 . THR D 94   ? 0.7905 1.2786 0.8814 -0.1694 -0.0517 0.1976  91   THR A CG2 
2147  N N   . ARG D 95   ? 0.7668 1.1191 0.8526 -0.1216 -0.0431 0.1639  92   ARG A N   
2148  C CA  . ARG D 95   ? 0.7685 1.0862 0.8556 -0.1033 -0.0380 0.1538  92   ARG A CA  
2149  C C   . ARG D 95   ? 0.7393 1.0723 0.8354 -0.0868 -0.0347 0.1548  92   ARG A C   
2150  O O   . ARG D 95   ? 0.7489 1.0774 0.8507 -0.0665 -0.0288 0.1499  92   ARG A O   
2151  C CB  . ARG D 95   ? 0.8646 1.1368 0.9376 -0.1130 -0.0427 0.1483  92   ARG A CB  
2152  C CG  . ARG D 95   ? 0.9524 1.1896 1.0251 -0.0984 -0.0377 0.1382  92   ARG A CG  
2153  C CD  . ARG D 95   ? 1.0426 1.2511 1.1083 -0.0976 -0.0399 0.1344  92   ARG A CD  
2154  N NE  . ARG D 95   ? 1.1287 1.3235 1.1786 -0.1153 -0.0482 0.1366  92   ARG A NE  
2155  C CZ  . ARG D 95   ? 1.1844 1.3875 1.2309 -0.1226 -0.0531 0.1416  92   ARG A CZ  
2156  N NH1 . ARG D 95   ? 1.2241 1.4092 1.2522 -0.1389 -0.0618 0.1431  92   ARG A NH1 
2157  N NH2 . ARG D 95   ? 1.1775 1.4048 1.2369 -0.1131 -0.0498 0.1448  92   ARG A NH2 
2158  N N   . ASN D 96   ? 0.7048 1.0541 0.8003 -0.0957 -0.0393 0.1611  93   ASN A N   
2159  C CA  . ASN D 96   ? 0.6672 1.0325 0.7702 -0.0804 -0.0366 0.1626  93   ASN A CA  
2160  C C   . ASN D 96   ? 0.5899 0.9973 0.7030 -0.0637 -0.0316 0.1666  93   ASN A C   
2161  O O   . ASN D 96   ? 0.5699 0.9792 0.6866 -0.0427 -0.0275 0.1645  93   ASN A O   
2162  C CB  . ASN D 96   ? 0.7083 1.0857 0.8080 -0.0948 -0.0430 0.1692  93   ASN A CB  
2163  C CG  . ASN D 96   ? 0.7754 1.1090 0.8625 -0.1060 -0.0479 0.1644  93   ASN A CG  
2164  O OD1 . ASN D 96   ? 0.7945 1.0922 0.8750 -0.1053 -0.0469 0.1570  93   ASN A OD1 
2165  N ND2 . ASN D 96   ? 0.8114 1.1492 0.8941 -0.1153 -0.0533 0.1686  93   ASN A ND2 
2166  N N   . ALA D 97   ? 0.5506 0.9918 0.6664 -0.0721 -0.0323 0.1727  94   ALA A N   
2167  C CA  . ALA D 97   ? 0.5172 1.0007 0.6412 -0.0538 -0.0272 0.1763  94   ALA A CA  
2168  C C   . ALA D 97   ? 0.5232 0.9810 0.6462 -0.0317 -0.0211 0.1668  94   ALA A C   
2169  O O   . ALA D 97   ? 0.5315 1.0031 0.6563 -0.0075 -0.0169 0.1658  94   ALA A O   
2170  C CB  . ALA D 97   ? 0.4892 1.0168 0.6160 -0.0697 -0.0296 0.1857  94   ALA A CB  
2171  N N   . LEU D 98   ? 0.5217 0.9405 0.6395 -0.0392 -0.0212 0.1599  95   LEU A N   
2172  C CA  . LEU D 98   ? 0.5356 0.9273 0.6513 -0.0208 -0.0163 0.1510  95   LEU A CA  
2173  C C   . LEU D 98   ? 0.5589 0.9166 0.6710 -0.0068 -0.0150 0.1449  95   LEU A C   
2174  O O   . LEU D 98   ? 0.5808 0.9293 0.6900 0.0144  -0.0117 0.1405  95   LEU A O   
2175  C CB  . LEU D 98   ? 0.5444 0.9067 0.6556 -0.0337 -0.0170 0.1459  95   LEU A CB  
2176  C CG  . LEU D 98   ? 0.3641 0.6958 0.4723 -0.0184 -0.0128 0.1367  95   LEU A CG  
2177  C CD1 . LEU D 98   ? 0.3977 0.7562 0.5080 0.0026  -0.0086 0.1373  95   LEU A CD1 
2178  C CD2 . LEU D 98   ? 0.3623 0.6703 0.4664 -0.0323 -0.0137 0.1327  95   LEU A CD2 
2179  N N   . ILE D 99   ? 0.5503 0.8881 0.6603 -0.0184 -0.0184 0.1447  96   ILE A N   
2180  C CA  . ILE D 99   ? 0.5559 0.8636 0.6625 -0.0074 -0.0176 0.1402  96   ILE A CA  
2181  C C   . ILE D 99   ? 0.5807 0.9105 0.6885 0.0119  -0.0161 0.1435  96   ILE A C   
2182  O O   . ILE D 99   ? 0.5917 0.8994 0.6939 0.0292  -0.0143 0.1392  96   ILE A O   
2183  C CB  . ILE D 99   ? 0.5339 0.8217 0.6379 -0.0235 -0.0216 0.1403  96   ILE A CB  
2184  C CG1 . ILE D 99   ? 0.4960 0.7552 0.5948 -0.0373 -0.0230 0.1354  96   ILE A CG1 
2185  C CG2 . ILE D 99   ? 0.5427 0.8081 0.6442 -0.0130 -0.0209 0.1378  96   ILE A CG2 
2186  C CD1 . ILE D 99   ? 0.4771 0.7159 0.5698 -0.0508 -0.0273 0.1349  96   ILE A CD1 
2187  N N   . GLU D 100  ? 0.6112 0.9846 0.7245 0.0091  -0.0173 0.1516  97   GLU A N   
2188  C CA  . GLU D 100  ? 0.6290 1.0283 0.7425 0.0298  -0.0158 0.1551  97   GLU A CA  
2189  C C   . GLU D 100  ? 0.6029 1.0138 0.7130 0.0521  -0.0120 0.1530  97   GLU A C   
2190  O O   . GLU D 100  ? 0.6080 1.0110 0.7104 0.0757  -0.0106 0.1507  97   GLU A O   
2191  C CB  . GLU D 100  ? 0.7019 1.1502 0.8224 0.0202  -0.0183 0.1651  97   GLU A CB  
2192  C CG  . GLU D 100  ? 0.7778 1.2146 0.8986 0.0025  -0.0227 0.1673  97   GLU A CG  
2193  C CD  . GLU D 100  ? 0.8379 1.3235 0.9642 -0.0040 -0.0256 0.1775  97   GLU A CD  
2194  O OE1 . GLU D 100  ? 0.8553 1.3867 0.9861 0.0075  -0.0235 0.1830  97   GLU A OE1 
2195  O OE2 . GLU D 100  ? 0.8594 1.3393 0.9850 -0.0202 -0.0301 0.1801  97   GLU A OE2 
2196  N N   . GLU D 101  ? 0.5840 1.0117 0.6974 0.0459  -0.0108 0.1537  98   GLU A N   
2197  C CA  . GLU D 101  ? 0.6123 1.0520 0.7215 0.0678  -0.0072 0.1514  98   GLU A CA  
2198  C C   . GLU D 101  ? 0.6026 0.9893 0.7002 0.0820  -0.0062 0.1414  98   GLU A C   
2199  O O   . GLU D 101  ? 0.5998 0.9833 0.6871 0.1075  -0.0048 0.1385  98   GLU A O   
2200  C CB  . GLU D 101  ? 0.6448 1.1116 0.7601 0.0555  -0.0063 0.1545  98   GLU A CB  
2201  C CG  . GLU D 101  ? 0.6817 1.1781 0.7942 0.0786  -0.0027 0.1548  98   GLU A CG  
2202  C CD  . GLU D 101  ? 0.7354 1.2883 0.8508 0.0936  -0.0019 0.1633  98   GLU A CD  
2203  O OE1 . GLU D 101  ? 0.7567 1.3440 0.8812 0.0759  -0.0043 0.1722  98   GLU A OE1 
2204  O OE2 . GLU D 101  ? 0.7660 1.3285 0.8726 0.1236  0.0006  0.1612  98   GLU A OE2 
2205  N N   . GLN D 102  ? 0.5859 0.9307 0.6829 0.0659  -0.0075 0.1362  99   GLN A N   
2206  C CA  . GLN D 102  ? 0.5556 0.8514 0.6416 0.0757  -0.0074 0.1279  99   GLN A CA  
2207  C C   . GLN D 102  ? 0.5582 0.8343 0.6348 0.0900  -0.0090 0.1273  99   GLN A C   
2208  O O   . GLN D 102  ? 0.5677 0.8180 0.6302 0.1087  -0.0094 0.1228  99   GLN A O   
2209  C CB  . GLN D 102  ? 0.5267 0.7895 0.6150 0.0547  -0.0084 0.1237  99   GLN A CB  
2210  C CG  . GLN D 102  ? 0.4967 0.7687 0.5901 0.0426  -0.0073 0.1229  99   GLN A CG  
2211  C CD  . GLN D 102  ? 0.4561 0.7018 0.5510 0.0218  -0.0089 0.1201  99   GLN A CD  
2212  O OE1 . GLN D 102  ? 0.4866 0.7136 0.5805 0.0151  -0.0108 0.1198  99   GLN A OE1 
2213  N NE2 . GLN D 102  ? 0.4218 0.6666 0.5179 0.0126  -0.0083 0.1181  99   GLN A NE2 
2214  N N   . ALA D 103  ? 0.5493 0.8350 0.6314 0.0813  -0.0106 0.1320  100  ALA A N   
2215  C CA  . ALA D 103  ? 0.5780 0.8466 0.6510 0.0943  -0.0123 0.1323  100  ALA A CA  
2216  C C   . ALA D 103  ? 0.6063 0.8960 0.6701 0.1218  -0.0116 0.1340  100  ALA A C   
2217  O O   . ALA D 103  ? 0.6407 0.9020 0.6886 0.1393  -0.0134 0.1315  100  ALA A O   
2218  C CB  . ALA D 103  ? 0.5548 0.8349 0.6364 0.0796  -0.0140 0.1374  100  ALA A CB  
2219  N N   . THR D 104  ? 0.5956 0.9351 0.6670 0.1262  -0.0095 0.1388  101  THR A N   
2220  C CA  . THR D 104  ? 0.6248 0.9900 0.6865 0.1554  -0.0084 0.1405  101  THR A CA  
2221  C C   . THR D 104  ? 0.6602 0.9938 0.7042 0.1758  -0.0083 0.1330  101  THR A C   
2222  O O   . THR D 104  ? 0.6892 1.0064 0.7138 0.2021  -0.0099 0.1307  101  THR A O   
2223  C CB  . THR D 104  ? 0.6128 1.0447 0.6880 0.1533  -0.0062 0.1484  101  THR A CB  
2224  O OG1 . THR D 104  ? 0.6079 1.0666 0.6963 0.1341  -0.0077 0.1557  101  THR A OG1 
2225  C CG2 . THR D 104  ? 0.6148 1.0789 0.6794 0.1864  -0.0047 0.1504  101  THR A CG2 
2226  N N   . TYR D 105  ? 0.6615 0.9833 0.7093 0.1645  -0.0071 0.1290  102  TYR A N   
2227  C CA  . TYR D 105  ? 0.6944 0.9849 0.7248 0.1823  -0.0075 0.1217  102  TYR A CA  
2228  C C   . TYR D 105  ? 0.7142 0.9410 0.7270 0.1842  -0.0116 0.1158  102  TYR A C   
2229  O O   . TYR D 105  ? 0.7457 0.9428 0.7353 0.2066  -0.0143 0.1111  102  TYR A O   
2230  C CB  . TYR D 105  ? 0.6902 0.9857 0.7301 0.1681  -0.0052 0.1194  102  TYR A CB  
2231  C CG  . TYR D 105  ? 0.6812 1.0314 0.7274 0.1778  -0.0018 0.1236  102  TYR A CG  
2232  C CD1 . TYR D 105  ? 0.6593 1.0615 0.7250 0.1606  0.0000  0.1321  102  TYR A CD1 
2233  C CD2 . TYR D 105  ? 0.6930 1.0430 0.7241 0.2038  -0.0009 0.1195  102  TYR A CD2 
2234  C CE1 . TYR D 105  ? 0.6579 1.1142 0.7295 0.1675  0.0028  0.1374  102  TYR A CE1 
2235  C CE2 . TYR D 105  ? 0.6957 1.1003 0.7328 0.2135  0.0025  0.1241  102  TYR A CE2 
2236  C CZ  . TYR D 105  ? 0.6685 1.1280 0.7268 0.1945  0.0045  0.1335  102  TYR A CZ  
2237  O OH  . TYR D 105  ? 0.6436 1.1615 0.7081 0.2021  0.0075  0.1394  102  TYR A OH  
2238  N N   . ARG D 106  ? 0.6902 0.8953 0.7117 0.1608  -0.0129 0.1162  103  ARG A N   
2239  C CA  . ARG D 106  ? 0.6992 0.8490 0.7049 0.1598  -0.0172 0.1124  103  ARG A CA  
2240  C C   . ARG D 106  ? 0.7355 0.8733 0.7226 0.1814  -0.0205 0.1139  103  ARG A C   
2241  O O   . ARG D 106  ? 0.7741 0.8657 0.7371 0.1930  -0.0251 0.1100  103  ARG A O   
2242  C CB  . ARG D 106  ? 0.6646 0.8026 0.6844 0.1320  -0.0174 0.1137  103  ARG A CB  
2243  C CG  . ARG D 106  ? 0.5988 0.7363 0.6312 0.1119  -0.0153 0.1110  103  ARG A CG  
2244  C CD  . ARG D 106  ? 0.5522 0.6679 0.5910 0.0899  -0.0165 0.1111  103  ARG A CD  
2245  N NE  . ARG D 106  ? 0.5622 0.6966 0.6103 0.0824  -0.0166 0.1165  103  ARG A NE  
2246  C CZ  . ARG D 106  ? 0.5588 0.7217 0.6222 0.0674  -0.0150 0.1197  103  ARG A CZ  
2247  N NH1 . ARG D 106  ? 0.5562 0.7317 0.6272 0.0578  -0.0132 0.1182  103  ARG A NH1 
2248  N NH2 . ARG D 106  ? 0.5438 0.7201 0.6128 0.0615  -0.0160 0.1243  103  ARG A NH2 
2249  N N   . ASN D 107  ? 0.7225 0.9002 0.7185 0.1867  -0.0188 0.1199  104  ASN A N   
2250  C CA  . ASN D 107  ? 0.7508 0.9211 0.7284 0.2098  -0.0217 0.1216  104  ASN A CA  
2251  C C   . ASN D 107  ? 0.7880 0.9588 0.7433 0.2426  -0.0226 0.1185  104  ASN A C   
2252  O O   . ASN D 107  ? 0.8434 0.9801 0.7714 0.2640  -0.0273 0.1164  104  ASN A O   
2253  C CB  . ASN D 107  ? 0.7601 0.9776 0.7539 0.2069  -0.0196 0.1291  104  ASN A CB  
2254  C CG  . ASN D 107  ? 0.7922 1.0004 0.8008 0.1796  -0.0202 0.1318  104  ASN A CG  
2255  O OD1 . ASN D 107  ? 0.8350 0.9971 0.8346 0.1715  -0.0233 0.1292  104  ASN A OD1 
2256  N ND2 . ASN D 107  ? 0.7686 1.0214 0.7985 0.1650  -0.0178 0.1373  104  ASN A ND2 
2257  N N   . ALA D 108  ? 0.7918 0.9998 0.7561 0.2476  -0.0187 0.1182  105  ALA A N   
2258  C CA  . ALA D 108  ? 0.8416 1.0519 0.7837 0.2804  -0.0193 0.1148  105  ALA A CA  
2259  C C   . ALA D 108  ? 0.8887 1.0312 0.8023 0.2884  -0.0248 0.1065  105  ALA A C   
2260  O O   . ALA D 108  ? 0.9451 1.0625 0.8273 0.3184  -0.0291 0.1031  105  ALA A O   
2261  C CB  . ALA D 108  ? 0.8129 1.0778 0.7723 0.2803  -0.0139 0.1167  105  ALA A CB  
2262  N N   . ILE D 109  ? 0.8545 0.9660 0.7762 0.2622  -0.0255 0.1034  106  ILE A N   
2263  C CA  . ILE D 109  ? 0.8648 0.9106 0.7598 0.2644  -0.0318 0.0968  106  ILE A CA  
2264  C C   . ILE D 109  ? 0.9396 0.9396 0.8147 0.2648  -0.0383 0.0978  106  ILE A C   
2265  O O   . ILE D 109  ? 0.9939 0.9426 0.8342 0.2811  -0.0456 0.0938  106  ILE A O   
2266  C CB  . ILE D 109  ? 0.7879 0.8204 0.6991 0.2355  -0.0303 0.0941  106  ILE A CB  
2267  C CG1 . ILE D 109  ? 0.7525 0.8343 0.6859 0.2319  -0.0236 0.0944  106  ILE A CG1 
2268  C CG2 . ILE D 109  ? 0.7920 0.7622 0.6751 0.2382  -0.0371 0.0875  106  ILE A CG2 
2269  C CD1 . ILE D 109  ? 0.7819 0.8697 0.6974 0.2601  -0.0236 0.0903  106  ILE A CD1 
2270  N N   . HIS D 110  ? 0.9331 0.9490 0.8278 0.2465  -0.0365 0.1034  107  HIS A N   
2271  C CA  . HIS D 110  ? 0.9680 0.9441 0.8462 0.2443  -0.0423 0.1055  107  HIS A CA  
2272  C C   . HIS D 110  ? 1.0302 0.9972 0.8793 0.2776  -0.0464 0.1058  107  HIS A C   
2273  O O   . HIS D 110  ? 1.0838 0.9978 0.9032 0.2839  -0.0541 0.1050  107  HIS A O   
2274  C CB  . HIS D 110  ? 0.9266 0.9291 0.8331 0.2201  -0.0388 0.1115  107  HIS A CB  
2275  C CG  . HIS D 110  ? 0.9472 0.9106 0.8407 0.2125  -0.0442 0.1142  107  HIS A CG  
2276  N ND1 . HIS D 110  ? 0.9668 0.8828 0.8505 0.1943  -0.0490 0.1129  107  HIS A ND1 
2277  C CD2 . HIS D 110  ? 0.9576 0.9248 0.8465 0.2197  -0.0457 0.1189  107  HIS A CD2 
2278  C CE1 . HIS D 110  ? 0.9852 0.8775 0.8586 0.1901  -0.0534 0.1170  107  HIS A CE1 
2279  N NE2 . HIS D 110  ? 0.9830 0.9041 0.8590 0.2058  -0.0514 0.1203  107  HIS A NE2 
2280  N N   . ASP D 111  ? 1.0335 1.0519 0.8890 0.2993  -0.0418 0.1075  108  ASP A N   
2281  C CA  . ASP D 111  ? 1.0775 1.0929 0.9048 0.3346  -0.0452 0.1078  108  ASP A CA  
2282  C C   . ASP D 111  ? 1.1552 1.1179 0.9401 0.3607  -0.0523 0.1007  108  ASP A C   
2283  O O   . ASP D 111  ? 1.2007 1.1356 0.9513 0.3884  -0.0583 0.0998  108  ASP A O   
2284  C CB  . ASP D 111  ? 1.0521 1.1431 0.8980 0.3509  -0.0383 0.1122  108  ASP A CB  
2285  C CG  . ASP D 111  ? 1.0187 1.1567 0.8990 0.3284  -0.0334 0.1199  108  ASP A CG  
2286  O OD1 . ASP D 111  ? 1.0173 1.1271 0.8997 0.3106  -0.0360 0.1218  108  ASP A OD1 
2287  O OD2 . ASP D 111  ? 0.9980 1.2015 0.9020 0.3282  -0.0274 0.1244  108  ASP A OD2 
2288  N N   . TYR D 112  ? 1.1622 1.1087 0.9462 0.3533  -0.0524 0.0954  109  TYR A N   
2289  C CA  . TYR D 112  ? 1.1892 1.0756 0.9300 0.3738  -0.0608 0.0882  109  TYR A CA  
2290  C C   . TYR D 112  ? 1.1896 1.0013 0.9037 0.3598  -0.0708 0.0876  109  TYR A C   
2291  O O   . TYR D 112  ? 1.2329 0.9886 0.9013 0.3819  -0.0805 0.0839  109  TYR A O   
2292  C CB  . TYR D 112  ? 1.1621 1.0524 0.9106 0.3672  -0.0582 0.0830  109  TYR A CB  
2293  C CG  . TYR D 112  ? 1.1609 1.1040 0.9130 0.3949  -0.0525 0.0817  109  TYR A CG  
2294  C CD1 . TYR D 112  ? 1.1146 1.1349 0.9067 0.3868  -0.0425 0.0874  109  TYR A CD1 
2295  C CD2 . TYR D 112  ? 1.2188 1.1345 0.9324 0.4289  -0.0576 0.0752  109  TYR A CD2 
2296  C CE1 . TYR D 112  ? 1.1085 1.1818 0.9043 0.4105  -0.0374 0.0877  109  TYR A CE1 
2297  C CE2 . TYR D 112  ? 1.2164 1.1847 0.9331 0.4554  -0.0520 0.0745  109  TYR A CE2 
2298  C CZ  . TYR D 112  ? 1.1552 1.2045 0.9142 0.4454  -0.0417 0.0812  109  TYR A CZ  
2299  O OH  . TYR D 112  ? 1.1427 1.2489 0.9052 0.4702  -0.0363 0.0819  109  TYR A OH  
2300  N N   . PHE D 113  ? 1.1451 0.9549 0.8849 0.3234  -0.0692 0.0916  110  PHE A N   
2301  C CA  . PHE D 113  ? 1.1256 0.8717 0.8431 0.3066  -0.0785 0.0929  110  PHE A CA  
2302  C C   . PHE D 113  ? 1.1320 0.8630 0.8298 0.3206  -0.0830 0.0972  110  PHE A C   
2303  O O   . PHE D 113  ? 1.1627 0.8316 0.8165 0.3330  -0.0939 0.0957  110  PHE A O   
2304  C CB  . PHE D 113  ? 1.0778 0.8344 0.8298 0.2656  -0.0747 0.0964  110  PHE A CB  
2305  C CG  . PHE D 113  ? 1.0563 0.8158 0.8221 0.2500  -0.0720 0.0921  110  PHE A CG  
2306  C CD1 . PHE D 113  ? 1.0992 0.8152 0.8338 0.2611  -0.0787 0.0859  110  PHE A CD1 
2307  C CD2 . PHE D 113  ? 1.0086 0.8123 0.8163 0.2249  -0.0635 0.0941  110  PHE A CD2 
2308  C CE1 . PHE D 113  ? 1.0768 0.7963 0.8241 0.2470  -0.0763 0.0820  110  PHE A CE1 
2309  C CE2 . PHE D 113  ? 0.9892 0.7952 0.8083 0.2116  -0.0612 0.0902  110  PHE A CE2 
2310  C CZ  . PHE D 113  ? 1.0242 0.7896 0.8144 0.2224  -0.0673 0.0842  110  PHE A CZ  
2311  N N   . ILE D 114  ? 1.1035 0.8886 0.8313 0.3183  -0.0755 0.1027  111  ILE A N   
2312  C CA  . ILE D 114  ? 1.1085 0.8836 0.8219 0.3288  -0.0791 0.1074  111  ILE A CA  
2313  C C   . ILE D 114  ? 1.1287 0.9111 0.8140 0.3721  -0.0809 0.1055  111  ILE A C   
2314  O O   . ILE D 114  ? 1.1486 0.9062 0.8084 0.3873  -0.0865 0.1079  111  ILE A O   
2315  C CB  . ILE D 114  ? 1.0167 0.8455 0.7725 0.3079  -0.0710 0.1142  111  ILE A CB  
2316  C CG1 . ILE D 114  ? 0.9552 0.8595 0.7418 0.3180  -0.0611 0.1150  111  ILE A CG1 
2317  C CG2 . ILE D 114  ? 0.9598 0.7816 0.7405 0.2681  -0.0695 0.1159  111  ILE A CG2 
2318  C CD1 . ILE D 114  ? 0.8953 0.8508 0.7196 0.2985  -0.0544 0.1216  111  ILE A CD1 
2319  N N   . GLY D 115  ? 1.1277 0.9449 0.8159 0.3934  -0.0763 0.1015  112  GLY A N   
2320  C CA  . GLY D 115  ? 1.1636 0.9938 0.8249 0.4373  -0.0776 0.0997  112  GLY A CA  
2321  C C   . GLY D 115  ? 1.1719 1.0759 0.8608 0.4468  -0.0694 0.1061  112  GLY A C   
2322  O O   . GLY D 115  ? 1.2119 1.1098 0.8808 0.4677  -0.0728 0.1086  112  GLY A O   
2323  N N   . ARG D 116  ? 1.1653 1.1387 0.8984 0.4312  -0.0594 0.1090  113  ARG A N   
2324  C CA  . ARG D 116  ? 1.1672 1.2174 0.9279 0.4379  -0.0519 0.1157  113  ARG A CA  
2325  C C   . ARG D 116  ? 1.1494 1.2664 0.9372 0.4388  -0.0437 0.1164  113  ARG A C   
2326  O O   . ARG D 116  ? 1.1030 1.2840 0.9284 0.4215  -0.0367 0.1228  113  ARG A O   
2327  C CB  . ARG D 116  ? 1.1466 1.2129 0.9390 0.4045  -0.0491 0.1222  113  ARG A CB  
2328  C CG  . ARG D 116  ? 1.1957 1.2233 0.9658 0.4107  -0.0553 0.1246  113  ARG A CG  
2329  C CD  . ARG D 116  ? 1.1890 1.2580 0.9935 0.3875  -0.0507 0.1321  113  ARG A CD  
2330  N NE  . ARG D 116  ? 1.2571 1.2857 1.0427 0.3882  -0.0565 0.1347  113  ARG A NE  
2331  C CZ  . ARG D 116  ? 1.3319 1.3663 1.0971 0.4170  -0.0589 0.1371  113  ARG A CZ  
2332  N NH1 . ARG D 116  ? 1.3540 1.4362 1.1152 0.4486  -0.0558 0.1374  113  ARG A NH1 
2333  N NH2 . ARG D 116  ? 1.3649 1.3592 1.1130 0.4146  -0.0645 0.1396  113  ARG A NH2 
2334  N N   . THR D 117  ? 1.1917 1.2937 0.9592 0.4581  -0.0452 0.1101  114  THR A N   
2335  C CA  . THR D 117  ? 1.1945 1.3576 0.9833 0.4619  -0.0380 0.1108  114  THR A CA  
2336  C C   . THR D 117  ? 1.2414 1.4395 1.0071 0.5085  -0.0376 0.1108  114  THR A C   
2337  O O   . THR D 117  ? 1.2761 1.4246 0.9978 0.5386  -0.0441 0.1046  114  THR A O   
2338  C CB  . THR D 117  ? 1.2184 1.3461 1.0042 0.4490  -0.0390 0.1040  114  THR A CB  
2339  O OG1 . THR D 117  ? 1.2080 1.3942 1.0094 0.4579  -0.0326 0.1046  114  THR A OG1 
2340  C CG2 . THR D 117  ? 1.2855 1.3329 1.0215 0.4716  -0.0488 0.0956  114  THR A CG2 
2341  N N   . ASP D 118  ? 1.2422 1.5256 1.0363 0.5114  -0.0297 0.1172  115  ASP A N   
2342  C CA  . ASP D 118  ? 1.2913 1.6149 1.0673 0.5420  -0.0247 0.1144  115  ASP A CA  
2343  C C   . ASP D 118  ? 1.3238 1.6287 1.0740 0.5609  -0.0241 0.1049  115  ASP A C   
2344  O O   . ASP D 118  ? 1.3450 1.6745 1.0728 0.5870  -0.0198 0.1006  115  ASP A O   
2345  C CB  . ASP D 118  ? 1.2423 1.6629 1.0564 0.5306  -0.0155 0.1243  115  ASP A CB  
2346  C CG  . ASP D 118  ? 1.2147 1.6579 1.0513 0.5137  -0.0160 0.1332  115  ASP A CG  
2347  O OD1 . ASP D 118  ? 1.2380 1.6321 1.0523 0.5227  -0.0213 0.1308  115  ASP A OD1 
2348  O OD2 . ASP D 118  ? 1.1724 1.6809 1.0474 0.4902  -0.0114 0.1428  115  ASP A OD2 
2349  N N   . ASN D 119  ? 1.3431 1.6057 1.0942 0.5491  -0.0284 0.1016  116  ASN A N   
2350  C CA  . ASN D 119  ? 1.4084 1.6540 1.1368 0.5650  -0.0281 0.0927  116  ASN A CA  
2351  C C   . ASN D 119  ? 1.4996 1.6641 1.1720 0.5895  -0.0362 0.0809  116  ASN A C   
2352  O O   . ASN D 119  ? 1.5375 1.6925 1.1825 0.6099  -0.0356 0.0726  116  ASN A O   
2353  C CB  . ASN D 119  ? 1.4087 1.6425 1.1604 0.5418  -0.0295 0.0939  116  ASN A CB  
2354  C CG  . ASN D 119  ? 1.3717 1.6773 1.1760 0.5091  -0.0216 0.1037  116  ASN A CG  
2355  O OD1 . ASN D 119  ? 1.3634 1.7454 1.1866 0.5158  -0.0156 0.1115  116  ASN A OD1 
2356  N ND2 . ASN D 119  ? 1.3420 1.6209 1.1682 0.4688  -0.0211 0.1025  116  ASN A ND2 
2357  N N   . LEU D 120  ? 1.5302 1.6358 1.1830 0.5870  -0.0440 0.0801  117  LEU A N   
2358  C CA  . LEU D 120  ? 1.5877 1.6102 1.1853 0.6055  -0.0533 0.0695  117  LEU A CA  
2359  C C   . LEU D 120  ? 1.6171 1.6405 1.1899 0.6265  -0.0536 0.0685  117  LEU A C   
2360  O O   . LEU D 120  ? 1.5594 1.6248 1.1587 0.6185  -0.0496 0.0770  117  LEU A O   
2361  C CB  . LEU D 120  ? 1.5878 1.5293 1.1762 0.5826  -0.0640 0.0691  117  LEU A CB  
2362  C CG  . LEU D 120  ? 1.5521 1.4779 1.1556 0.5638  -0.0653 0.0684  117  LEU A CG  
2363  C CD1 . LEU D 120  ? 1.5606 1.4051 1.1500 0.5410  -0.0761 0.0685  117  LEU A CD1 
2364  C CD2 . LEU D 120  ? 1.5859 1.5042 1.1625 0.5847  -0.0648 0.0581  117  LEU A CD2 
2365  N N   . THR D 121  ? 1.6984 1.6738 1.2180 0.6536  -0.0587 0.0578  118  THR A N   
2366  C CA  . THR D 121  ? 1.7267 1.6982 1.2156 0.6777  -0.0594 0.0553  118  THR A CA  
2367  C C   . THR D 121  ? 1.7263 1.6360 1.2036 0.6637  -0.0685 0.0575  118  THR A C   
2368  O O   . THR D 121  ? 1.7308 1.5860 1.2112 0.6390  -0.0761 0.0588  118  THR A O   
2369  C CB  . THR D 121  ? 1.7717 1.7077 1.2029 0.7117  -0.0629 0.0426  118  THR A CB  
2370  O OG1 . THR D 121  ? 1.7853 1.6376 1.1860 0.7042  -0.0740 0.0349  118  THR A OG1 
2371  C CG2 . THR D 121  ? 1.7518 1.7624 1.1926 0.7300  -0.0522 0.0419  118  THR A CG2 
2372  N N   . ASP D 122  ? 1.7368 1.6560 1.1989 0.6802  -0.0676 0.0581  119  ASP A N   
2373  C CA  . ASP D 122  ? 1.7467 1.6197 1.2025 0.6668  -0.0749 0.0619  119  ASP A CA  
2374  C C   . ASP D 122  ? 1.8049 1.5737 1.2135 0.6622  -0.0889 0.0545  119  ASP A C   
2375  O O   . ASP D 122  ? 1.7675 1.4914 1.1813 0.6364  -0.0960 0.0595  119  ASP A O   
2376  C CB  . ASP D 122  ? 1.7763 1.6781 1.2191 0.6895  -0.0712 0.0625  119  ASP A CB  
2377  C CG  . ASP D 122  ? 1.7344 1.7409 1.2175 0.6953  -0.0576 0.0694  119  ASP A CG  
2378  O OD1 . ASP D 122  ? 1.7157 1.7685 1.2180 0.6956  -0.0510 0.0695  119  ASP A OD1 
2379  O OD2 . ASP D 122  ? 1.7147 1.7577 1.2098 0.6983  -0.0537 0.0751  119  ASP A OD2 
2380  N N   . ALA D 123  ? 1.8858 1.6158 1.2462 0.6859  -0.0935 0.0429  120  ALA A N   
2381  C CA  . ALA D 123  ? 1.9424 1.5728 1.2539 0.6802  -0.1080 0.0356  120  ALA A CA  
2382  C C   . ALA D 123  ? 1.9047 1.5038 1.2377 0.6457  -0.1126 0.0390  120  ALA A C   
2383  O O   . ALA D 123  ? 1.9398 1.4742 1.2598 0.6222  -0.1228 0.0411  120  ALA A O   
2384  C CB  . ALA D 123  ? 1.9975 1.5983 1.2533 0.7130  -0.1119 0.0223  120  ALA A CB  
2385  N N   . ILE D 124  ? 1.8295 1.4754 1.1949 0.6415  -0.1051 0.0399  121  ILE A N   
2386  C CA  . ILE D 124  ? 1.7621 1.3848 1.1503 0.6098  -0.1083 0.0433  121  ILE A CA  
2387  C C   . ILE D 124  ? 1.6710 1.3239 1.1088 0.5807  -0.1045 0.0562  121  ILE A C   
2388  O O   . ILE D 124  ? 1.6671 1.2760 1.1104 0.5514  -0.1111 0.0604  121  ILE A O   
2389  C CB  . ILE D 124  ? 1.7638 1.4264 1.1684 0.6162  -0.1015 0.0398  121  ILE A CB  
2390  C CG1 . ILE D 124  ? 1.8429 1.4782 1.1953 0.6477  -0.1051 0.0270  121  ILE A CG1 
2391  C CG2 . ILE D 124  ? 1.7485 1.3828 1.1725 0.5849  -0.1053 0.0423  121  ILE A CG2 
2392  C CD1 . ILE D 124  ? 1.8313 1.5092 1.1973 0.6567  -0.0980 0.0235  121  ILE A CD1 
2393  N N   . ASN D 125  ? 1.5676 1.2967 1.0403 0.5877  -0.0942 0.0630  122  ASN A N   
2394  C CA  . ASN D 125  ? 1.4761 1.2409 0.9965 0.5614  -0.0903 0.0753  122  ASN A CA  
2395  C C   . ASN D 125  ? 1.4778 1.1872 0.9824 0.5463  -0.0989 0.0795  122  ASN A C   
2396  O O   . ASN D 125  ? 1.4772 1.1749 1.0049 0.5171  -0.1010 0.0876  122  ASN A O   
2397  C CB  . ASN D 125  ? 1.4376 1.2974 0.9950 0.5721  -0.0782 0.0812  122  ASN A CB  
2398  C CG  . ASN D 125  ? 1.3949 1.2996 1.0035 0.5447  -0.0737 0.0935  122  ASN A CG  
2399  O OD1 . ASN D 125  ? 1.3503 1.2909 0.9940 0.5276  -0.0688 0.0970  122  ASN A OD1 
2400  N ND2 . ASN D 125  ? 1.4058 1.3091 1.0183 0.5389  -0.0752 0.0996  122  ASN A ND2 
2401  N N   . LYS D 126  ? 1.4958 1.1708 0.9596 0.5658  -0.1039 0.0743  123  LYS A N   
2402  C CA  . LYS D 126  ? 1.4829 1.1059 0.9298 0.5516  -0.1122 0.0785  123  LYS A CA  
2403  C C   . LYS D 126  ? 1.5142 1.0485 0.9284 0.5307  -0.1250 0.0756  123  LYS A C   
2404  O O   . LYS D 126  ? 1.4610 0.9586 0.8750 0.5058  -0.1313 0.0824  123  LYS A O   
2405  C CB  . LYS D 126  ? 1.5177 1.1349 0.9310 0.5797  -0.1133 0.0740  123  LYS A CB  
2406  N N   . ARG D 127  ? 1.5787 1.0797 0.9648 0.5388  -0.1293 0.0660  124  ARG A N   
2407  C CA  . ARG D 127  ? 1.6099 1.0290 0.9642 0.5168  -0.1420 0.0633  124  ARG A CA  
2408  C C   . ARG D 127  ? 1.5687 0.9888 0.9597 0.4793  -0.1417 0.0724  124  ARG A C   
2409  O O   . ARG D 127  ? 1.6094 0.9707 0.9841 0.4518  -0.1516 0.0755  124  ARG A O   
2410  C CB  . ARG D 127  ? 1.6227 1.0121 0.9405 0.5345  -0.1461 0.0509  124  ARG A CB  
2411  N N   . HIS D 128  ? 1.4986 0.9860 0.9377 0.4769  -0.1307 0.0770  125  HIS A N   
2412  C CA  . HIS D 128  ? 1.4506 0.9454 0.9263 0.4405  -0.1288 0.0846  125  HIS A CA  
2413  C C   . HIS D 128  ? 1.4513 0.9574 0.9513 0.4132  -0.1268 0.0934  125  HIS A C   
2414  O O   . HIS D 128  ? 1.4257 0.9124 0.9401 0.3749  -0.1286 0.0970  125  HIS A O   
2415  C CB  . HIS D 128  ? 1.4235 0.9984 0.9501 0.4361  -0.1144 0.0833  125  HIS A CB  
2416  C CG  . HIS D 128  ? 1.4958 1.0615 1.0047 0.4550  -0.1156 0.0752  125  HIS A CG  
2417  N ND1 . HIS D 128  ? 1.4723 1.1076 1.0115 0.4677  -0.1044 0.0733  125  HIS A ND1 
2418  C CD2 . HIS D 128  ? 1.5663 1.0618 1.0297 0.4619  -0.1271 0.0686  125  HIS A CD2 
2419  C CE1 . HIS D 128  ? 1.4933 1.1025 1.0070 0.4837  -0.1084 0.0659  125  HIS A CE1 
2420  N NE2 . HIS D 128  ? 1.5500 1.0756 1.0187 0.4786  -0.1216 0.0619  125  HIS A NE2 
2421  N N   . ALA D 129  ? 1.4833 1.0231 0.9881 0.4330  -0.1230 0.0971  126  ALA A N   
2422  C CA  . ALA D 129  ? 1.4756 1.0279 1.0029 0.4093  -0.1209 0.1053  126  ALA A CA  
2423  C C   . ALA D 129  ? 1.5426 1.0124 1.0275 0.3972  -0.1351 0.1082  126  ALA A C   
2424  O O   . ALA D 129  ? 1.5034 0.9694 1.0078 0.3627  -0.1350 0.1147  126  ALA A O   
2425  C CB  . ALA D 129  ? 1.4578 1.0641 0.9965 0.4354  -0.1144 0.1085  126  ALA A CB  
2426  N N   . GLU D 130  ? 1.6452 1.0547 1.0753 0.4203  -0.1459 0.1018  127  GLU A N   
2427  C CA  . GLU D 130  ? 1.7363 1.0708 1.1273 0.4019  -0.1587 0.1024  127  GLU A CA  
2428  C C   . GLU D 130  ? 1.7645 1.0580 1.1546 0.3656  -0.1656 0.1054  127  GLU A C   
2429  O O   . GLU D 130  ? 1.7863 1.0327 1.1589 0.3391  -0.1747 0.1106  127  GLU A O   
2430  C CB  . GLU D 130  ? 1.8144 1.1038 1.1517 0.4284  -0.1662 0.0906  127  GLU A CB  
2431  N N   . ILE D 131  ? 1.7845 1.0978 1.1936 0.3630  -0.1613 0.1027  128  ILE A N   
2432  C CA  . ILE D 131  ? 1.7652 1.0538 1.1821 0.3251  -0.1650 0.1041  128  ILE A CA  
2433  C C   . ILE D 131  ? 1.6630 1.0133 1.1419 0.2884  -0.1528 0.1103  128  ILE A C   
2434  O O   . ILE D 131  ? 1.6637 0.9925 1.1470 0.2530  -0.1572 0.1165  128  ILE A O   
2435  C CB  . ILE D 131  ? 1.7904 1.0741 1.1993 0.3369  -0.1650 0.0951  128  ILE A CB  
2436  C CG1 . ILE D 131  ? 1.8721 1.1110 1.2282 0.3656  -0.1731 0.0838  128  ILE A CG1 
2437  C CG2 . ILE D 131  ? 1.7854 1.0480 1.2039 0.2971  -0.1684 0.0963  128  ILE A CG2 
2438  C CD1 . ILE D 131  ? 1.8866 1.1252 1.2341 0.3795  -0.1723 0.0737  128  ILE A CD1 
2439  N N   . TYR D 132  ? 1.5404 0.9682 1.0660 0.2964  -0.1379 0.1093  129  TYR A N   
2440  C CA  . TYR D 132  ? 1.4126 0.8975 0.9941 0.2644  -0.1267 0.1143  129  TYR A CA  
2441  C C   . TYR D 132  ? 1.3576 0.8407 0.9450 0.2479  -0.1281 0.1231  129  TYR A C   
2442  O O   . TYR D 132  ? 1.3217 0.8292 0.9427 0.2157  -0.1233 0.1281  129  TYR A O   
2443  C CB  . TYR D 132  ? 1.3444 0.9078 0.9682 0.2779  -0.1123 0.1116  129  TYR A CB  
2444  C CG  . TYR D 132  ? 1.2628 0.8810 0.9405 0.2464  -0.1015 0.1149  129  TYR A CG  
2445  C CD1 . TYR D 132  ? 1.2228 0.8522 0.9203 0.2284  -0.0978 0.1115  129  TYR A CD1 
2446  C CD2 . TYR D 132  ? 1.2246 0.8817 0.9310 0.2360  -0.0955 0.1211  129  TYR A CD2 
2447  C CE1 . TYR D 132  ? 1.1780 0.8540 0.9205 0.2019  -0.0887 0.1141  129  TYR A CE1 
2448  C CE2 . TYR D 132  ? 1.1672 0.8700 0.9180 0.2092  -0.0866 0.1236  129  TYR A CE2 
2449  C CZ  . TYR D 132  ? 1.1524 0.8637 0.9202 0.1928  -0.0834 0.1200  129  TYR A CZ  
2450  O OH  . TYR D 132  ? 1.0981 0.8516 0.9062 0.1684  -0.0753 0.1222  129  TYR A OH  
2451  N N   . LYS D 133  ? 1.3851 0.8398 0.9392 0.2705  -0.1347 0.1250  130  LYS A N   
2452  C CA  . LYS D 133  ? 1.3802 0.8299 0.9367 0.2557  -0.1367 0.1336  130  LYS A CA  
2453  C C   . LYS D 133  ? 1.4174 0.8133 0.9554 0.2219  -0.1471 0.1394  130  LYS A C   
2454  O O   . LYS D 133  ? 1.3920 0.8117 0.9603 0.1912  -0.1431 0.1462  130  LYS A O   
2455  C CB  . LYS D 133  ? 1.4246 0.8513 0.9447 0.2898  -0.1424 0.1341  130  LYS A CB  
2456  N N   . GLY D 134  ? 1.4684 0.7925 0.9553 0.2269  -0.1611 0.1372  131  GLY A N   
2457  C CA  . GLY D 134  ? 1.4920 0.7635 0.9574 0.1933  -0.1726 0.1435  131  GLY A CA  
2458  C C   . GLY D 134  ? 1.4416 0.7172 0.9227 0.1695  -0.1715 0.1409  131  GLY A C   
2459  O O   . GLY D 134  ? 1.4719 0.6904 0.9196 0.1515  -0.1843 0.1430  131  GLY A O   
2460  N N   . LEU D 135  ? 1.3671 0.7096 0.8977 0.1685  -0.1569 0.1366  132  LEU A N   
2461  C CA  . LEU D 135  ? 1.3219 0.6750 0.8709 0.1487  -0.1543 0.1334  132  LEU A CA  
2462  C C   . LEU D 135  ? 1.2680 0.6523 0.8539 0.1092  -0.1496 0.1410  132  LEU A C   
2463  O O   . LEU D 135  ? 1.2136 0.6003 0.8101 0.0889  -0.1495 0.1399  132  LEU A O   
2464  C CB  . LEU D 135  ? 1.2530 0.6590 0.8319 0.1699  -0.1419 0.1246  132  LEU A CB  
2465  C CG  . LEU D 135  ? 1.2290 0.6311 0.8107 0.1636  -0.1416 0.1182  132  LEU A CG  
2466  C CD1 . LEU D 135  ? 1.2840 0.6106 0.8076 0.1766  -0.1568 0.1141  132  LEU A CD1 
2467  C CD2 . LEU D 135  ? 1.1899 0.6523 0.8055 0.1828  -0.1283 0.1113  132  LEU A CD2 
2468  N N   . PHE D 136  ? 1.3090 0.7179 0.9135 0.0992  -0.1459 0.1485  133  PHE A N   
2469  C CA  . PHE D 136  ? 1.2958 0.7406 0.9360 0.0657  -0.1405 0.1556  133  PHE A CA  
2470  C C   . PHE D 136  ? 1.3352 0.7540 0.9584 0.0474  -0.1486 0.1668  133  PHE A C   
2471  O O   . PHE D 136  ? 1.2894 0.7482 0.9436 0.0302  -0.1420 0.1732  133  PHE A O   
2472  C CB  . PHE D 136  ? 1.2509 0.7695 0.9424 0.0700  -0.1245 0.1534  133  PHE A CB  
2473  C CG  . PHE D 136  ? 1.2559 0.8031 0.9640 0.0885  -0.1166 0.1435  133  PHE A CG  
2474  C CD1 . PHE D 136  ? 1.2595 0.8206 0.9851 0.0739  -0.1132 0.1400  133  PHE A CD1 
2475  C CD2 . PHE D 136  ? 1.2634 0.8257 0.9691 0.1204  -0.1126 0.1384  133  PHE A CD2 
2476  C CE1 . PHE D 136  ? 1.2453 0.8325 0.9853 0.0901  -0.1061 0.1316  133  PHE A CE1 
2477  C CE2 . PHE D 136  ? 1.2523 0.8443 0.9731 0.1363  -0.1054 0.1306  133  PHE A CE2 
2478  C CZ  . PHE D 136  ? 1.2439 0.8470 0.9816 0.1207  -0.1022 0.1271  133  PHE A CZ  
2479  N N   . LYS D 137  ? 1.3810 0.7318 0.9528 0.0511  -0.1634 0.1694  134  LYS A N   
2480  C CA  . LYS D 137  ? 1.4182 0.7375 0.9682 0.0310  -0.1731 0.1810  134  LYS A CA  
2481  C C   . LYS D 137  ? 1.5000 0.7372 0.9912 0.0248  -0.1917 0.1830  134  LYS A C   
2482  O O   . LYS D 137  ? 1.5289 0.7423 1.0049 0.0275  -0.1959 0.1764  134  LYS A O   
2483  C CB  . LYS D 137  ? 1.4138 0.7453 0.9649 0.0509  -0.1697 0.1833  134  LYS A CB  
2484  C CG  . LYS D 137  ? 1.4006 0.7278 0.9376 0.0929  -0.1674 0.1737  134  LYS A CG  
2485  C CD  . LYS D 137  ? 1.3481 0.7008 0.8950 0.1089  -0.1622 0.1768  134  LYS A CD  
2486  C CE  . LYS D 137  ? 1.3351 0.6954 0.8725 0.1511  -0.1587 0.1681  134  LYS A CE  
2487  N NZ  . LYS D 137  ? 1.3145 0.7049 0.8638 0.1658  -0.1533 0.1716  134  LYS A NZ  
2488  N N   . ALA D 138  ? 1.5500 0.7415 1.0057 0.0162  -0.2037 0.1922  135  ALA A N   
2489  C CA  . ALA D 138  ? 1.6782 0.8050 1.0861 0.0010  -0.2198 0.1927  135  ALA A CA  
2490  C C   . ALA D 138  ? 1.9382 1.0199 1.3066 0.0316  -0.2261 0.1785  135  ALA A C   
2491  O O   . ALA D 138  ? 2.1817 1.2170 1.5141 0.0194  -0.2383 0.1747  135  ALA A O   
2492  C CB  . ALA D 138  ? 1.9733 1.0817 1.3634 -0.0135 -0.2268 0.2006  135  ALA A CB  
2493  N N   . GLU D 139  ? 1.8948 0.9912 1.2679 0.0710  -0.2186 0.1706  136  GLU A N   
2494  C CA  . GLU D 139  ? 1.9788 1.0380 1.3144 0.1025  -0.2238 0.1568  136  GLU A CA  
2495  C C   . GLU D 139  ? 1.9852 1.0333 1.3168 0.0972  -0.2259 0.1496  136  GLU A C   
2496  O O   . GLU D 139  ? 2.0386 1.0493 1.3335 0.1179  -0.2325 0.1382  136  GLU A O   
2497  C CB  . GLU D 139  ? 1.9945 1.0830 1.3396 0.1463  -0.2141 0.1509  136  GLU A CB  
2498  C CG  . GLU D 139  ? 2.0304 1.1267 1.3741 0.1564  -0.2127 0.1563  136  GLU A CG  
2499  C CD  . GLU D 139  ? 2.0547 1.1748 1.3983 0.2021  -0.2053 0.1487  136  GLU A CD  
2500  O OE1 . GLU D 139  ? 2.0835 1.1974 1.4122 0.2281  -0.2048 0.1373  136  GLU A OE1 
2501  O OE2 . GLU D 139  ? 2.0406 1.1890 1.3994 0.2119  -0.1998 0.1541  136  GLU A OE2 
2502  N N   . LEU D 140  ? 1.8731 0.9531 1.2402 0.0710  -0.2207 0.1557  137  LEU A N   
2503  C CA  . LEU D 140  ? 1.8105 0.8777 1.1726 0.0610  -0.2239 0.1498  137  LEU A CA  
2504  C C   . LEU D 140  ? 1.8697 0.8817 1.1891 0.0385  -0.2397 0.1484  137  LEU A C   
2505  O O   . LEU D 140  ? 1.9332 0.9131 1.2253 0.0452  -0.2465 0.1389  137  LEU A O   
2506  C CB  . LEU D 140  ? 1.6946 0.8090 1.1033 0.0339  -0.2154 0.1576  137  LEU A CB  
2507  C CG  . LEU D 140  ? 1.5783 0.7742 1.0453 0.0503  -0.1949 0.1505  137  LEU A CG  
2508  C CD1 . LEU D 140  ? 1.5008 0.7532 1.0175 0.0173  -0.1854 0.1553  137  LEU A CD1 
2509  C CD2 . LEU D 140  ? 1.5620 0.7546 1.0211 0.0808  -0.1922 0.1377  137  LEU A CD2 
2510  N N   . PHE D 141  ? 1.8668 0.8684 1.1790 0.0115  -0.2462 0.1581  138  PHE A N   
2511  C CA  . PHE D 141  ? 1.9286 0.8838 1.2032 -0.0161 -0.2620 0.1592  138  PHE A CA  
2512  C C   . PHE D 141  ? 2.0341 0.9288 1.2520 0.0053  -0.2745 0.1509  138  PHE A C   
2513  O O   . PHE D 141  ? 2.0783 0.9258 1.2559 -0.0121 -0.2896 0.1491  138  PHE A O   
2514  C CB  . PHE D 141  ? 1.9153 0.8916 1.2084 -0.0557 -0.2636 0.1741  138  PHE A CB  
2515  C CG  . PHE D 141  ? 1.8475 0.8860 1.1949 -0.0769 -0.2514 0.1827  138  PHE A CG  
2516  C CD1 . PHE D 141  ? 1.7876 0.8740 1.1747 -0.0630 -0.2371 0.1868  138  PHE A CD1 
2517  C CD2 . PHE D 141  ? 1.8363 0.8863 1.1936 -0.1105 -0.2548 0.1868  138  PHE A CD2 
2518  C CE1 . PHE D 141  ? 1.7094 0.8509 1.1431 -0.0819 -0.2266 0.1943  138  PHE A CE1 
2519  C CE2 . PHE D 141  ? 1.7625 0.8712 1.1684 -0.1286 -0.2435 0.1942  138  PHE A CE2 
2520  C CZ  . PHE D 141  ? 1.6957 0.8488 1.1389 -0.1142 -0.2295 0.1978  138  PHE A CZ  
2521  N N   . ASN D 142  ? 2.0808 0.9769 1.2931 0.0424  -0.2690 0.1459  139  ASN A N   
2522  C CA  . ASN D 142  ? 2.1742 1.0149 1.3314 0.0667  -0.2800 0.1369  139  ASN A CA  
2523  C C   . ASN D 142  ? 2.2295 1.0311 1.3494 0.0832  -0.2878 0.1234  139  ASN A C   
2524  O O   . ASN D 142  ? 2.2882 1.0333 1.3532 0.0947  -0.3011 0.1161  139  ASN A O   
2525  C CB  . ASN D 142  ? 2.1642 1.0252 1.3282 0.1064  -0.2704 0.1337  139  ASN A CB  
2526  C CG  . ASN D 142  ? 2.1191 1.0184 1.3181 0.0935  -0.2627 0.1465  139  ASN A CG  
2527  O OD1 . ASN D 142  ? 2.0903 1.0021 1.3085 0.0552  -0.2641 0.1579  139  ASN A OD1 
2528  N ND2 . ASN D 142  ? 2.1083 1.0301 1.3161 0.1258  -0.2542 0.1448  139  ASN A ND2 
2529  N N   . GLY D 143  ? 2.2117 1.0409 1.3580 0.0848  -0.2803 0.1200  140  GLY A N   
2530  C CA  . GLY D 143  ? 2.2662 1.0703 1.3837 0.1115  -0.2837 0.1061  140  GLY A CA  
2531  C C   . GLY D 143  ? 2.2854 1.1021 1.3977 0.1611  -0.2753 0.0964  140  GLY A C   
2532  O O   . GLY D 143  ? 2.3136 1.1161 1.4035 0.1875  -0.2765 0.0844  140  GLY A O   
2533  N N   . LYS D 144  ? 2.2737 1.1198 1.4061 0.1747  -0.2669 0.1014  141  LYS A N   
2534  C CA  . LYS D 144  ? 2.2810 1.1475 1.4111 0.2216  -0.2584 0.0931  141  LYS A CA  
2535  C C   . LYS D 144  ? 2.2392 1.1576 1.4072 0.2408  -0.2447 0.0888  141  LYS A C   
2536  O O   . LYS D 144  ? 2.2673 1.1839 1.4162 0.2749  -0.2432 0.0773  141  LYS A O   
2537  C CB  . LYS D 144  ? 2.2544 1.1478 1.4035 0.2276  -0.2519 0.1011  141  LYS A CB  
2538  N N   . VAL D 145  ? 2.1706 1.1365 1.3911 0.2191  -0.2348 0.0982  142  VAL A N   
2539  C CA  . VAL D 145  ? 2.1153 1.1302 1.3722 0.2342  -0.2225 0.0949  142  VAL A CA  
2540  C C   . VAL D 145  ? 2.1605 1.1467 1.3941 0.2354  -0.2285 0.0851  142  VAL A C   
2541  O O   . VAL D 145  ? 2.1337 1.1402 1.3693 0.2659  -0.2222 0.0761  142  VAL A O   
2542  C CB  . VAL D 145  ? 2.0483 1.1114 1.3599 0.2065  -0.2131 0.1071  142  VAL A CB  
2543  C CG1 . VAL D 145  ? 2.0198 1.1218 1.3569 0.2158  -0.2048 0.1148  142  VAL A CG1 
2544  C CG2 . VAL D 145  ? 2.0658 1.1019 1.3748 0.1597  -0.2219 0.1154  142  VAL A CG2 
2545  N N   . LEU D 146  ? 2.2233 1.1639 1.4334 0.2024  -0.2410 0.0870  143  LEU A N   
2546  C CA  . LEU D 146  ? 2.2676 1.1734 1.4476 0.2032  -0.2492 0.0774  143  LEU A CA  
2547  C C   . LEU D 146  ? 2.3736 1.2355 1.4972 0.2374  -0.2579 0.0649  143  LEU A C   
2548  O O   . LEU D 146  ? 2.3726 1.2202 1.4752 0.2540  -0.2604 0.0546  143  LEU A O   
2549  C CB  . LEU D 146  ? 2.2378 1.1103 1.4072 0.1570  -0.2611 0.0838  143  LEU A CB  
2550  C CG  . LEU D 146  ? 2.2646 1.0774 1.3821 0.1500  -0.2773 0.0759  143  LEU A CG  
2551  C CD1 . LEU D 146  ? 2.2174 1.0402 1.3555 0.1196  -0.2779 0.0786  143  LEU A CD1 
2552  C CD2 . LEU D 146  ? 2.3186 1.0783 1.3924 0.1302  -0.2935 0.0798  143  LEU A CD2 
2553  N N   . LYS D 147  ? 2.4958 1.3368 1.5934 0.2493  -0.2623 0.0654  144  LYS A N   
2554  C CA  . LYS D 147  ? 2.5667 1.3712 1.6110 0.2862  -0.2692 0.0530  144  LYS A CA  
2555  C C   . LYS D 147  ? 2.5429 1.3976 1.6056 0.3306  -0.2549 0.0455  144  LYS A C   
2556  O O   . LYS D 147  ? 2.6029 1.4379 1.6277 0.3615  -0.2584 0.0335  144  LYS A O   
2557  C CB  . LYS D 147  ? 2.6116 1.3806 1.6225 0.2869  -0.2778 0.0557  144  LYS A CB  
2558  N N   . GLN D 148  ? 2.3995 1.3209 1.5185 0.3342  -0.2393 0.0527  145  GLN A N   
2559  C CA  . GLN D 148  ? 2.2825 1.2601 1.4239 0.3724  -0.2255 0.0468  145  GLN A CA  
2560  C C   . GLN D 148  ? 2.2322 1.2223 1.3840 0.3740  -0.2224 0.0409  145  GLN A C   
2561  O O   . GLN D 148  ? 2.2472 1.2651 1.3967 0.4083  -0.2157 0.0324  145  GLN A O   
2562  C CB  . GLN D 148  ? 2.1442 1.1913 1.3429 0.3732  -0.2106 0.0566  145  GLN A CB  
2563  C CG  . GLN D 148  ? 2.1014 1.1400 1.3102 0.3471  -0.2134 0.0683  145  GLN A CG  
2564  C CD  . GLN D 148  ? 2.0767 1.1499 1.2951 0.3720  -0.2061 0.0707  145  GLN A CD  
2565  O OE1 . GLN D 148  ? 2.0531 1.1279 1.2835 0.3548  -0.2066 0.0803  145  GLN A OE1 
2566  N NE2 . GLN D 148  ? 2.0809 1.1849 1.2939 0.4123  -0.1991 0.0622  145  GLN A NE2 
2567  N N   . LEU D 149  ? 2.1680 1.1402 1.3310 0.3372  -0.2272 0.0455  146  LEU A N   
2568  C CA  . LEU D 149  ? 2.1066 1.0896 1.2813 0.3352  -0.2245 0.0407  146  LEU A CA  
2569  C C   . LEU D 149  ? 2.1607 1.0784 1.2790 0.3341  -0.2398 0.0312  146  LEU A C   
2570  O O   . LEU D 149  ? 2.1675 1.0860 1.2682 0.3605  -0.2389 0.0208  146  LEU A O   
2571  C CB  . LEU D 149  ? 2.0299 1.0363 1.2513 0.2962  -0.2202 0.0513  146  LEU A CB  
2572  C CG  . LEU D 149  ? 1.9464 1.0254 1.2286 0.2989  -0.2037 0.0586  146  LEU A CG  
2573  C CD1 . LEU D 149  ? 1.9398 1.0589 1.2319 0.3321  -0.1948 0.0586  146  LEU A CD1 
2574  C CD2 . LEU D 149  ? 1.9000 0.9860 1.2137 0.2569  -0.2035 0.0718  146  LEU A CD2 
2575  N N   . THR D 153  ? 2.2153 0.8898 1.2014 0.1511  -0.3156 0.0498  150  THR A N   
2576  C CA  . THR D 153  ? 2.3110 0.9300 1.2520 0.1242  -0.3343 0.0543  150  THR A CA  
2577  C C   . THR D 153  ? 2.2914 0.9234 1.2591 0.0724  -0.3378 0.0672  150  THR A C   
2578  O O   . THR D 153  ? 2.2585 0.9072 1.2460 0.0564  -0.3359 0.0676  150  THR A O   
2579  C CB  . THR D 153  ? 2.4124 0.9635 1.2822 0.1371  -0.3525 0.0431  150  THR A CB  
2580  O OG1 . THR D 153  ? 2.4047 0.9610 1.2798 0.1342  -0.3523 0.0383  150  THR A OG1 
2581  C CG2 . THR D 153  ? 2.4481 0.9819 1.2828 0.1873  -0.3512 0.0312  150  THR A CG2 
2582  N N   . THR D 154  ? 2.3091 0.9360 1.2772 0.0469  -0.3427 0.0778  151  THR A N   
2583  C CA  . THR D 154  ? 2.2871 0.9331 1.2811 -0.0021 -0.3456 0.0913  151  THR A CA  
2584  C C   . THR D 154  ? 2.3554 0.9492 1.3007 -0.0298 -0.3667 0.0916  151  THR A C   
2585  O O   . THR D 154  ? 2.4179 0.9503 1.3017 -0.0177 -0.3825 0.0847  151  THR A O   
2586  C CB  . THR D 154  ? 2.2755 0.9368 1.2855 -0.0176 -0.3435 0.1028  151  THR A CB  
2587  O OG1 . THR D 154  ? 2.2208 0.9258 1.2697 0.0115  -0.3254 0.1020  151  THR A OG1 
2588  C CG2 . THR D 154  ? 2.2315 0.9274 1.2769 -0.0657 -0.3432 0.1174  151  THR A CG2 
2589  N N   . THR D 155  ? 2.3365 0.9562 1.3083 -0.0667 -0.3672 0.0997  152  THR A N   
2590  C CA  . THR D 155  ? 2.3685 0.9493 1.3013 -0.0999 -0.3870 0.1033  152  THR A CA  
2591  C C   . THR D 155  ? 2.3681 0.9555 1.3047 -0.1404 -0.3945 0.1183  152  THR A C   
2592  O O   . THR D 155  ? 2.3268 0.9602 1.3074 -0.1468 -0.3819 0.1266  152  THR A O   
2593  C CB  . THR D 155  ? 2.2811 0.8888 1.2389 -0.1159 -0.3837 0.1034  152  THR A CB  
2594  O OG1 . THR D 155  ? 2.1923 0.8605 1.2058 -0.1501 -0.3741 0.1167  152  THR A OG1 
2595  C CG2 . THR D 155  ? 2.2177 0.8445 1.1957 -0.0768 -0.3690 0.0911  152  THR A CG2 
2596  N N   . GLU D 156  ? 2.4157 0.9574 1.3042 -0.1681 -0.4159 0.1221  153  GLU A N   
2597  C CA  . GLU D 156  ? 2.4039 0.9435 1.2850 -0.2047 -0.4262 0.1358  153  GLU A CA  
2598  C C   . GLU D 156  ? 2.3172 0.9322 1.2636 -0.2369 -0.4133 0.1497  153  GLU A C   
2599  O O   . GLU D 156  ? 2.2981 0.9388 1.2658 -0.2500 -0.4091 0.1596  153  GLU A O   
2600  C CB  . GLU D 156  ? 2.4770 0.9574 1.2951 -0.2307 -0.4523 0.1380  153  GLU A CB  
2601  N N   . HIS D 157  ? 2.2596 0.9117 1.2376 -0.2494 -0.4070 0.1508  154  HIS A N   
2602  C CA  . HIS D 157  ? 2.1538 0.8801 1.1929 -0.2778 -0.3943 0.1633  154  HIS A CA  
2603  C C   . HIS D 157  ? 2.0916 0.8677 1.1840 -0.2552 -0.3718 0.1630  154  HIS A C   
2604  O O   . HIS D 157  ? 2.0522 0.8773 1.1830 -0.2746 -0.3637 0.1746  154  HIS A O   
2605  C CB  . HIS D 157  ? 2.0748 0.8281 1.1333 -0.2932 -0.3925 0.1635  154  HIS A CB  
2606  C CG  . HIS D 157  ? 1.9720 0.8030 1.0907 -0.3207 -0.3798 0.1757  154  HIS A CG  
2607  N ND1 . HIS D 157  ? 1.8928 0.7776 1.0654 -0.3081 -0.3598 0.1729  154  HIS A ND1 
2608  C CD2 . HIS D 157  ? 1.9522 0.8175 1.0844 -0.3591 -0.3844 0.1908  154  HIS A CD2 
2609  C CE1 . HIS D 157  ? 1.8418 0.7896 1.0574 -0.3367 -0.3526 0.1853  154  HIS A CE1 
2610  N NE2 . HIS D 157  ? 1.8771 0.8167 1.0702 -0.3674 -0.3669 0.1963  154  HIS A NE2 
2611  N N   . GLU D 158  ? 2.0832 0.8487 1.1773 -0.2138 -0.3619 0.1502  155  GLU A N   
2612  C CA  . GLU D 158  ? 2.0286 0.8355 1.1665 -0.1902 -0.3425 0.1500  155  GLU A CA  
2613  C C   . GLU D 158  ? 2.0648 0.8571 1.1890 -0.1869 -0.3453 0.1549  155  GLU A C   
2614  O O   . GLU D 158  ? 2.0368 0.8756 1.2022 -0.1921 -0.3331 0.1634  155  GLU A O   
2615  C CB  . GLU D 158  ? 2.0222 0.8196 1.1594 -0.1458 -0.3333 0.1354  155  GLU A CB  
2616  C CG  . GLU D 158  ? 1.9853 0.8088 1.1479 -0.1458 -0.3260 0.1308  155  GLU A CG  
2617  C CD  . GLU D 158  ? 1.9811 0.7844 1.1297 -0.1021 -0.3213 0.1156  155  GLU A CD  
2618  O OE1 . GLU D 158  ? 2.0008 0.7826 1.1299 -0.0696 -0.3201 0.1093  155  GLU A OE1 
2619  O OE2 . GLU D 158  ? 1.9512 0.7625 1.1081 -0.0998 -0.3188 0.1101  155  GLU A OE2 
2620  N N   . ASN D 159  ? 2.1835 0.9103 1.2481 -0.1780 -0.3617 0.1496  156  ASN A N   
2621  C CA  . ASN D 159  ? 2.2158 0.9241 1.2626 -0.1776 -0.3664 0.1545  156  ASN A CA  
2622  C C   . ASN D 159  ? 2.1778 0.9162 1.2432 -0.2221 -0.3703 0.1709  156  ASN A C   
2623  O O   . ASN D 159  ? 2.1483 0.9118 1.2354 -0.2245 -0.3635 0.1786  156  ASN A O   
2624  C CB  . ASN D 159  ? 2.3604 0.9891 1.3343 -0.1631 -0.3856 0.1459  156  ASN A CB  
2625  C CG  . ASN D 159  ? 2.4020 1.0090 1.3602 -0.1131 -0.3790 0.1332  156  ASN A CG  
2626  O OD1 . ASN D 159  ? 2.3700 1.0111 1.3613 -0.0956 -0.3645 0.1352  156  ASN A OD1 
2627  N ND2 . ASN D 159  ? 2.4653 1.0170 1.3712 -0.0894 -0.3899 0.1204  156  ASN A ND2 
2628  N N   . ALA D 160  ? 2.1789 0.9187 1.2366 -0.2571 -0.3813 0.1769  157  ALA A N   
2629  C CA  . ALA D 160  ? 2.1285 0.9067 1.2072 -0.2992 -0.3842 0.1930  157  ALA A CA  
2630  C C   . ALA D 160  ? 1.9840 0.8438 1.1334 -0.3043 -0.3629 0.2003  157  ALA A C   
2631  O O   . ALA D 160  ? 1.9473 0.8457 1.1205 -0.3273 -0.3602 0.2129  157  ALA A O   
2632  C CB  . ALA D 160  ? 2.1668 0.9320 1.2210 -0.3340 -0.4008 0.1978  157  ALA A CB  
2633  N N   . LEU D 161  ? 1.8914 0.7782 1.0731 -0.2829 -0.3480 0.1927  158  LEU A N   
2634  C CA  . LEU D 161  ? 1.7894 0.7498 1.0347 -0.2845 -0.3280 0.1987  158  LEU A CA  
2635  C C   . LEU D 161  ? 1.7695 0.7426 1.0334 -0.2598 -0.3159 0.1988  158  LEU A C   
2636  O O   . LEU D 161  ? 1.7369 0.7657 1.0437 -0.2706 -0.3043 0.2085  158  LEU A O   
2637  C CB  . LEU D 161  ? 1.7270 0.7097 0.9983 -0.2706 -0.3172 0.1906  158  LEU A CB  
2638  C CG  . LEU D 161  ? 1.7039 0.7216 0.9937 -0.3022 -0.3189 0.1964  158  LEU A CG  
2639  C CD1 . LEU D 161  ? 1.6682 0.7079 0.9855 -0.2848 -0.3066 0.1878  158  LEU A CD1 
2640  C CD2 . LEU D 161  ? 1.6504 0.7319 0.9793 -0.3325 -0.3129 0.2115  158  LEU A CD2 
2641  N N   . LEU D 162  ? 1.7692 0.6936 1.0008 -0.2257 -0.3185 0.1885  159  LEU A N   
2642  C CA  . LEU D 162  ? 1.7062 0.6415 0.9520 -0.2014 -0.3082 0.1889  159  LEU A CA  
2643  C C   . LEU D 162  ? 1.7281 0.6645 0.9672 -0.2236 -0.3144 0.2006  159  LEU A C   
2644  O O   . LEU D 162  ? 1.6546 0.6344 0.9297 -0.2236 -0.3026 0.2082  159  LEU A O   
2645  C CB  . LEU D 162  ? 1.7316 0.6157 0.9404 -0.1592 -0.3108 0.1751  159  LEU A CB  
2646  C CG  . LEU D 162  ? 1.7119 0.6006 0.9307 -0.1286 -0.3019 0.1630  159  LEU A CG  
2647  C CD1 . LEU D 162  ? 1.7620 0.6000 0.9376 -0.0878 -0.3067 0.1498  159  LEU A CD1 
2648  C CD2 . LEU D 162  ? 1.6261 0.5791 0.9036 -0.1189 -0.2819 0.1664  159  LEU A CD2 
2649  N N   . ARG D 163  ? 1.8293 0.7182 1.0214 -0.2431 -0.3334 0.2025  160  ARG A N   
2650  C CA  . ARG D 163  ? 1.7113 0.5970 0.8924 -0.2649 -0.3411 0.2135  160  ARG A CA  
2651  C C   . ARG D 163  ? 1.6639 0.6142 0.8871 -0.3023 -0.3362 0.2285  160  ARG A C   
2652  O O   . ARG D 163  ? 1.6679 0.6312 0.8942 -0.3182 -0.3383 0.2388  160  ARG A O   
2653  C CB  . ARG D 163  ? 1.9164 0.7317 1.0323 -0.2769 -0.3644 0.2116  160  ARG A CB  
2654  C CG  . ARG D 163  ? 1.9740 0.7228 1.0416 -0.2397 -0.3712 0.1962  160  ARG A CG  
2655  C CD  . ARG D 163  ? 1.9557 0.6339 0.9564 -0.2509 -0.3944 0.1957  160  ARG A CD  
2656  N NE  . ARG D 163  ? 2.0575 0.7370 1.0467 -0.2960 -0.4089 0.2058  160  ARG A NE  
2657  C CZ  . ARG D 163  ? 2.0764 0.7306 1.0395 -0.3076 -0.4206 0.2019  160  ARG A CZ  
2658  N NH1 . ARG D 163  ? 2.0276 0.6524 0.9733 -0.2769 -0.4193 0.1876  160  ARG A NH1 
2659  N NH2 . ARG D 163  ? 2.0836 0.7441 1.0376 -0.3496 -0.4339 0.2128  160  ARG A NH2 
2660  N N   . SER D 164  ? 1.6564 0.6493 0.9116 -0.3156 -0.3297 0.2298  161  SER A N   
2661  C CA  . SER D 164  ? 1.5706 0.6324 0.8684 -0.3470 -0.3232 0.2434  161  SER A CA  
2662  C C   . SER D 164  ? 1.5465 0.6610 0.8904 -0.3353 -0.3051 0.2484  161  SER A C   
2663  O O   . SER D 164  ? 1.4713 0.6409 0.8462 -0.3588 -0.3004 0.2604  161  SER A O   
2664  C CB  . SER D 164  ? 1.5374 0.6333 0.8587 -0.3593 -0.3193 0.2424  161  SER A CB  
2665  O OG  . SER D 164  ? 1.5228 0.6261 0.8658 -0.3288 -0.3054 0.2317  161  SER A OG  
2666  N N   . PHE D 165  ? 1.5261 0.6264 0.8739 -0.2989 -0.2954 0.2398  162  PHE A N   
2667  C CA  . PHE D 165  ? 1.4764 0.6195 0.8621 -0.2846 -0.2796 0.2440  162  PHE A CA  
2668  C C   . PHE D 165  ? 1.5134 0.6161 0.8714 -0.2642 -0.2834 0.2423  162  PHE A C   
2669  O O   . PHE D 165  ? 1.4833 0.5970 0.8580 -0.2361 -0.2720 0.2393  162  PHE A O   
2670  C CB  . PHE D 165  ? 1.4358 0.6078 0.8558 -0.2596 -0.2637 0.2368  162  PHE A CB  
2671  C CG  . PHE D 165  ? 1.4055 0.6322 0.8631 -0.2796 -0.2562 0.2407  162  PHE A CG  
2672  C CD1 . PHE D 165  ? 1.3691 0.6613 0.8675 -0.2982 -0.2468 0.2520  162  PHE A CD1 
2673  C CD2 . PHE D 165  ? 1.4099 0.6240 0.8615 -0.2784 -0.2585 0.2327  162  PHE A CD2 
2674  C CE1 . PHE D 165  ? 1.3130 0.6578 0.8449 -0.3145 -0.2397 0.2551  162  PHE A CE1 
2675  C CE2 . PHE D 165  ? 1.3717 0.6372 0.8576 -0.2960 -0.2515 0.2362  162  PHE A CE2 
2676  C CZ  . PHE D 165  ? 1.3211 0.6523 0.8469 -0.3136 -0.2421 0.2473  162  PHE A CZ  
2677  N N   . ASP D 166  ? 1.5883 0.6435 0.9021 -0.2779 -0.3002 0.2442  163  ASP A N   
2678  C CA  . ASP D 166  ? 1.6308 0.6511 0.9184 -0.2627 -0.3045 0.2443  163  ASP A CA  
2679  C C   . ASP D 166  ? 1.6145 0.6864 0.9366 -0.2764 -0.2958 0.2573  163  ASP A C   
2680  O O   . ASP D 166  ? 1.6094 0.7204 0.9499 -0.3098 -0.2973 0.2683  163  ASP A O   
2681  C CB  . ASP D 166  ? 1.7206 0.6748 0.9489 -0.2761 -0.3260 0.2431  163  ASP A CB  
2682  N N   . LYS D 167  ? 1.6007 0.6753 0.9312 -0.2493 -0.2868 0.2560  164  LYS A N   
2683  C CA  . LYS D 167  ? 1.5392 0.6650 0.9048 -0.2564 -0.2766 0.2672  164  LYS A CA  
2684  C C   . LYS D 167  ? 1.4780 0.6773 0.8969 -0.2715 -0.2632 0.2735  164  LYS A C   
2685  O O   . LYS D 167  ? 1.4261 0.6728 0.8705 -0.2931 -0.2592 0.2851  164  LYS A O   
2686  C CB  . LYS D 167  ? 1.5697 0.6826 0.9134 -0.2831 -0.2886 0.2776  164  LYS A CB  
2687  N N   . PHE D 168  ? 1.5032 0.7129 0.9381 -0.2591 -0.2562 0.2656  165  PHE A N   
2688  C CA  . PHE D 168  ? 1.4827 0.7600 0.9659 -0.2717 -0.2437 0.2704  165  PHE A CA  
2689  C C   . PHE D 168  ? 1.4467 0.7327 0.9489 -0.2457 -0.2330 0.2607  165  PHE A C   
2690  O O   . PHE D 168  ? 1.4609 0.7884 0.9930 -0.2567 -0.2260 0.2617  165  PHE A O   
2691  C CB  . PHE D 168  ? 1.5006 0.7927 0.9826 -0.3070 -0.2518 0.2755  165  PHE A CB  
2692  C CG  . PHE D 168  ? 1.4388 0.8055 0.9628 -0.3306 -0.2433 0.2872  165  PHE A CG  
2693  C CD1 . PHE D 168  ? 1.1981 0.6197 0.7650 -0.3250 -0.2284 0.2866  165  PHE A CD1 
2694  C CD2 . PHE D 168  ? 1.2818 0.6645 0.8009 -0.3576 -0.2506 0.2987  165  PHE A CD2 
2695  C CE1 . PHE D 168  ? 1.1535 0.6448 0.7568 -0.3438 -0.2206 0.2965  165  PHE A CE1 
2696  C CE2 . PHE D 168  ? 1.2360 0.6907 0.7928 -0.3767 -0.2428 0.3091  165  PHE A CE2 
2697  C CZ  . PHE D 168  ? 1.1720 0.6812 0.7705 -0.3688 -0.2276 0.3076  165  PHE A CZ  
2698  N N   . THR D 169  ? 1.4059 0.6567 0.8918 -0.2113 -0.2316 0.2515  166  THR A N   
2699  C CA  . THR D 169  ? 1.3865 0.6454 0.8883 -0.1859 -0.2225 0.2425  166  THR A CA  
2700  C C   . THR D 169  ? 1.3313 0.6530 0.8815 -0.1820 -0.2070 0.2478  166  THR A C   
2701  O O   . THR D 169  ? 1.3144 0.6618 0.8891 -0.1627 -0.1966 0.2371  166  THR A O   
2702  C CB  . THR D 169  ? 1.4569 0.6665 0.9274 -0.1482 -0.2256 0.2316  166  THR A CB  
2703  O OG1 . THR D 169  ? 1.4861 0.7009 0.9583 -0.1337 -0.2222 0.2358  166  THR A OG1 
2704  C CG2 . THR D 169  ? 1.5348 0.6800 0.9543 -0.1503 -0.2415 0.2251  166  THR A CG2 
2705  N N   . THR D 170  ? 1.2918 0.6512 0.8623 -0.1968 -0.2028 0.2588  167  THR A N   
2706  C CA  . THR D 170  ? 1.2019 0.6371 0.8258 -0.1928 -0.1857 0.2580  167  THR A CA  
2707  C C   . THR D 170  ? 1.1363 0.6162 0.7896 -0.2115 -0.1799 0.2579  167  THR A C   
2708  O O   . THR D 170  ? 1.0540 0.5955 0.7507 -0.2039 -0.1652 0.2531  167  THR A O   
2709  C CB  . THR D 170  ? 1.1587 0.6211 0.7932 -0.2045 -0.1839 0.2702  167  THR A CB  
2710  O OG1 . THR D 170  ? 1.1826 0.5904 0.7785 -0.1947 -0.1939 0.2735  167  THR A OG1 
2711  C CG2 . THR D 170  ? 1.0638 0.5940 0.7469 -0.1868 -0.1660 0.2642  167  THR A CG2 
2712  N N   . TYR D 171  ? 1.1773 0.6263 0.8059 -0.2355 -0.1917 0.2631  168  TYR A N   
2713  C CA  . TYR D 171  ? 1.1627 0.6513 0.8166 -0.2506 -0.1867 0.2619  168  TYR A CA  
2714  C C   . TYR D 171  ? 1.0950 0.5978 0.7697 -0.2230 -0.1759 0.2448  168  TYR A C   
2715  O O   . TYR D 171  ? 1.0701 0.6218 0.7777 -0.2275 -0.1665 0.2416  168  TYR A O   
2716  C CB  . TYR D 171  ? 1.2421 0.7001 0.8672 -0.2760 -0.2007 0.2643  168  TYR A CB  
2717  C CG  . TYR D 171  ? 1.0606 0.5690 0.7113 -0.3002 -0.1973 0.2684  168  TYR A CG  
2718  C CD1 . TYR D 171  ? 1.0342 0.6003 0.7095 -0.3211 -0.1932 0.2795  168  TYR A CD1 
2719  C CD2 . TYR D 171  ? 1.0601 0.5598 0.7092 -0.3006 -0.1984 0.2612  168  TYR A CD2 
2720  C CE1 . TYR D 171  ? 1.0080 0.6237 0.7056 -0.3404 -0.1902 0.2831  168  TYR A CE1 
2721  C CE2 . TYR D 171  ? 1.0334 0.5809 0.7052 -0.3215 -0.1954 0.2650  168  TYR A CE2 
2722  C CZ  . TYR D 171  ? 1.0077 0.6137 0.7035 -0.3407 -0.1913 0.2759  168  TYR A CZ  
2723  O OH  . TYR D 171  ? 0.9823 0.6391 0.6997 -0.3586 -0.1883 0.2795  168  TYR A OH  
2724  N N   . PHE D 172  ? 1.0882 0.5504 0.7434 -0.1941 -0.1773 0.2341  169  PHE A N   
2725  C CA  . PHE D 172  ? 1.0872 0.5649 0.7615 -0.1660 -0.1669 0.2186  169  PHE A CA  
2726  C C   . PHE D 172  ? 1.0579 0.5817 0.7666 -0.1422 -0.1522 0.2129  169  PHE A C   
2727  O O   . PHE D 172  ? 1.0365 0.5613 0.7510 -0.1144 -0.1460 0.2012  169  PHE A O   
2728  C CB  . PHE D 172  ? 1.1306 0.5423 0.7633 -0.1466 -0.1768 0.2104  169  PHE A CB  
2729  C CG  . PHE D 172  ? 1.1768 0.5399 0.7741 -0.1679 -0.1915 0.2138  169  PHE A CG  
2730  C CD1 . PHE D 172  ? 1.2265 0.5365 0.7811 -0.1894 -0.2083 0.2254  169  PHE A CD1 
2731  C CD2 . PHE D 172  ? 1.1646 0.5334 0.7695 -0.1673 -0.1894 0.2057  169  PHE A CD2 
2732  C CE1 . PHE D 172  ? 1.2565 0.5357 0.7848 -0.2071 -0.2199 0.2231  169  PHE A CE1 
2733  C CE2 . PHE D 172  ? 1.2032 0.5267 0.7744 -0.1875 -0.2036 0.2088  169  PHE A CE2 
2734  C CZ  . PHE D 172  ? 1.2525 0.5340 0.7867 -0.2072 -0.2185 0.2165  169  PHE A CZ  
2735  N N   . SER D 173  ? 1.0379 0.6010 0.7684 -0.1528 -0.1469 0.2213  170  SER A N   
2736  C CA  . SER D 173  ? 0.9884 0.5914 0.7478 -0.1320 -0.1346 0.2166  170  SER A CA  
2737  C C   . SER D 173  ? 0.9334 0.5824 0.7289 -0.1200 -0.1215 0.2059  170  SER A C   
2738  O O   . SER D 173  ? 0.9184 0.5730 0.7221 -0.0947 -0.1152 0.1962  170  SER A O   
2739  C CB  . SER D 173  ? 0.9704 0.6055 0.7441 -0.1477 -0.1324 0.2282  170  SER A CB  
2740  O OG  . SER D 173  ? 0.9600 0.6266 0.7563 -0.1278 -0.1223 0.2241  170  SER A OG  
2741  N N   . GLY D 174  ? 0.9128 0.5964 0.7293 -0.1382 -0.1176 0.2082  171  GLY A N   
2742  C CA  . GLY D 174  ? 0.8975 0.6202 0.7445 -0.1281 -0.1064 0.1984  171  GLY A CA  
2743  C C   . GLY D 174  ? 0.9505 0.6461 0.7861 -0.1152 -0.1081 0.1880  171  GLY A C   
2744  O O   . GLY D 174  ? 0.9465 0.6647 0.8017 -0.0979 -0.0992 0.1783  171  GLY A O   
2745  N N   . PHE D 175  ? 1.0079 0.6542 0.8100 -0.1240 -0.1200 0.1903  172  PHE A N   
2746  C CA  . PHE D 175  ? 1.0121 0.6275 0.7984 -0.1098 -0.1228 0.1804  172  PHE A CA  
2747  C C   . PHE D 175  ? 0.9981 0.5995 0.7769 -0.0785 -0.1202 0.1723  172  PHE A C   
2748  O O   . PHE D 175  ? 0.9701 0.5749 0.7541 -0.0604 -0.1156 0.1623  172  PHE A O   
2749  C CB  . PHE D 175  ? 1.0912 0.6509 0.8376 -0.1263 -0.1380 0.1853  172  PHE A CB  
2750  C CG  . PHE D 175  ? 1.1286 0.6462 0.8500 -0.1088 -0.1431 0.1753  172  PHE A CG  
2751  C CD1 . PHE D 175  ? 1.1168 0.6496 0.8519 -0.1079 -0.1386 0.1677  172  PHE A CD1 
2752  C CD2 . PHE D 175  ? 1.1610 0.6233 0.8432 -0.0920 -0.1526 0.1735  172  PHE A CD2 
2753  C CE1 . PHE D 175  ? 1.1288 0.6241 0.8403 -0.0909 -0.1432 0.1585  172  PHE A CE1 
2754  C CE2 . PHE D 175  ? 1.1797 0.6037 0.8365 -0.0734 -0.1574 0.1640  172  PHE A CE2 
2755  C CZ  . PHE D 175  ? 1.1698 0.6112 0.8419 -0.0731 -0.1526 0.1566  172  PHE A CZ  
2756  N N   . TYR D 176  ? 0.9854 0.5733 0.7519 -0.0715 -0.1230 0.1771  173  TYR A N   
2757  C CA  . TYR D 176  ? 0.9580 0.5402 0.7193 -0.0409 -0.1200 0.1703  173  TYR A CA  
2758  C C   . TYR D 176  ? 0.8627 0.5019 0.6642 -0.0278 -0.1056 0.1636  173  TYR A C   
2759  O O   . TYR D 176  ? 0.8188 0.4618 0.6213 -0.0042 -0.1017 0.1554  173  TYR A O   
2760  C CB  . TYR D 176  ? 0.9914 0.5546 0.7351 -0.0375 -0.1250 0.1775  173  TYR A CB  
2761  C CG  . TYR D 176  ? 1.0774 0.5726 0.7718 -0.0423 -0.1408 0.1824  173  TYR A CG  
2762  C CD1 . TYR D 176  ? 1.1260 0.5753 0.7894 -0.0361 -0.1493 0.1768  173  TYR A CD1 
2763  C CD2 . TYR D 176  ? 1.1021 0.5766 0.7785 -0.0531 -0.1481 0.1929  173  TYR A CD2 
2764  C CE1 . TYR D 176  ? 1.1936 0.5749 0.8070 -0.0408 -0.1653 0.1812  173  TYR A CE1 
2765  C CE2 . TYR D 176  ? 1.1648 0.5724 0.7920 -0.0589 -0.1639 0.1979  173  TYR A CE2 
2766  C CZ  . TYR D 176  ? 1.2329 0.5924 0.8276 -0.0527 -0.1729 0.1919  173  TYR A CZ  
2767  O OH  . TYR D 176  ? 1.3442 0.6314 0.8853 -0.0586 -0.1902 0.1967  173  TYR A OH  
2768  N N   . GLU D 177  ? 0.8525 0.5363 0.6853 -0.0429 -0.0982 0.1675  174  GLU A N   
2769  C CA  . GLU D 177  ? 0.8376 0.5712 0.7051 -0.0331 -0.0861 0.1616  174  GLU A CA  
2770  C C   . GLU D 177  ? 0.7987 0.5416 0.6761 -0.0304 -0.0822 0.1533  174  GLU A C   
2771  O O   . GLU D 177  ? 0.7410 0.5066 0.6333 -0.0142 -0.0752 0.1463  174  GLU A O   
2772  C CB  . GLU D 177  ? 0.8673 0.6406 0.7603 -0.0489 -0.0806 0.1675  174  GLU A CB  
2773  C CG  . GLU D 177  ? 0.9307 0.7064 0.8211 -0.0470 -0.0815 0.1742  174  GLU A CG  
2774  C CD  . GLU D 177  ? 0.9556 0.7471 0.8547 -0.0240 -0.0760 0.1691  174  GLU A CD  
2775  O OE1 . GLU D 177  ? 0.9390 0.7574 0.8573 -0.0151 -0.0688 0.1619  174  GLU A OE1 
2776  O OE2 . GLU D 177  ? 0.9796 0.7573 0.8655 -0.0155 -0.0792 0.1729  174  GLU A OE2 
2777  N N   . ASN D 178  ? 0.8158 0.5427 0.6847 -0.0471 -0.0871 0.1546  175  ASN A N   
2778  C CA  . ASN D 178  ? 0.7961 0.5298 0.6728 -0.0450 -0.0839 0.1469  175  ASN A CA  
2779  C C   . ASN D 178  ? 0.8345 0.5408 0.6922 -0.0225 -0.0863 0.1392  175  ASN A C   
2780  O O   . ASN D 178  ? 0.8210 0.5446 0.6914 -0.0126 -0.0805 0.1316  175  ASN A O   
2781  C CB  . ASN D 178  ? 0.8223 0.5429 0.6910 -0.0682 -0.0898 0.1509  175  ASN A CB  
2782  C CG  . ASN D 178  ? 0.8164 0.5702 0.7039 -0.0890 -0.0870 0.1590  175  ASN A CG  
2783  O OD1 . ASN D 178  ? 0.8414 0.6376 0.7567 -0.0866 -0.0777 0.1571  175  ASN A OD1 
2784  N ND2 . ASN D 178  ? 0.7989 0.5332 0.6691 -0.1095 -0.0958 0.1684  175  ASN A ND2 
2785  N N   . ARG D 179  ? 0.8938 0.5576 0.7195 -0.0132 -0.0950 0.1411  176  ARG A N   
2786  C CA  . ARG D 179  ? 0.9473 0.5853 0.7514 0.0120  -0.0977 0.1338  176  ARG A CA  
2787  C C   . ARG D 179  ? 0.9594 0.6268 0.7770 0.0361  -0.0901 0.1306  176  ARG A C   
2788  O O   . ARG D 179  ? 0.9923 0.6624 0.8060 0.0577  -0.0878 0.1236  176  ARG A O   
2789  C CB  . ARG D 179  ? 1.0007 0.5756 0.7590 0.0138  -0.1116 0.1366  176  ARG A CB  
2790  C CG  . ARG D 179  ? 1.0152 0.5556 0.7540 -0.0065 -0.1207 0.1379  176  ARG A CG  
2791  C CD  . ARG D 179  ? 0.9796 0.5284 0.7258 0.0017  -0.1168 0.1286  176  ARG A CD  
2792  N NE  . ARG D 179  ? 0.9734 0.4997 0.7080 -0.0206 -0.1239 0.1301  176  ARG A NE  
2793  C CZ  . ARG D 179  ? 0.9374 0.4984 0.6998 -0.0423 -0.1187 0.1324  176  ARG A CZ  
2794  N NH1 . ARG D 179  ? 0.9637 0.5041 0.7133 -0.0620 -0.1260 0.1342  176  ARG A NH1 
2795  N NH2 . ARG D 179  ? 0.8723 0.4881 0.6735 -0.0438 -0.1067 0.1330  176  ARG A NH2 
2796  N N   . LYS D 180  ? 0.9419 0.6338 0.7751 0.0327  -0.0863 0.1360  177  LYS A N   
2797  C CA  . LYS D 180  ? 0.9075 0.6367 0.7592 0.0514  -0.0783 0.1335  177  LYS A CA  
2798  C C   . LYS D 180  ? 0.8500 0.6245 0.7342 0.0494  -0.0685 0.1286  177  LYS A C   
2799  O O   . LYS D 180  ? 0.8353 0.6348 0.7287 0.0670  -0.0632 0.1246  177  LYS A O   
2800  C CB  . LYS D 180  ? 0.9260 0.6710 0.7870 0.0462  -0.0769 0.1405  177  LYS A CB  
2801  C CG  . LYS D 180  ? 1.0126 0.7147 0.8412 0.0500  -0.0864 0.1459  177  LYS A CG  
2802  C CD  . LYS D 180  ? 1.0298 0.7538 0.8668 0.0598  -0.0832 0.1497  177  LYS A CD  
2803  C CE  . LYS D 180  ? 1.0595 0.7545 0.8777 0.0485  -0.0906 0.1584  177  LYS A CE  
2804  N NZ  . LYS D 180  ? 1.0381 0.7496 0.8748 0.0200  -0.0891 0.1643  177  LYS A NZ  
2805  N N   . ASN D 181  ? 0.7762 0.5623 0.6764 0.0282  -0.0663 0.1295  178  ASN A N   
2806  C CA  . ASN D 181  ? 0.7396 0.5621 0.6660 0.0257  -0.0582 0.1246  178  ASN A CA  
2807  C C   . ASN D 181  ? 0.7369 0.5503 0.6553 0.0382  -0.0582 0.1174  178  ASN A C   
2808  O O   . ASN D 181  ? 0.7006 0.5447 0.6384 0.0412  -0.0515 0.1133  178  ASN A O   
2809  C CB  . ASN D 181  ? 0.6987 0.5323 0.6394 0.0024  -0.0568 0.1271  178  ASN A CB  
2810  C CG  . ASN D 181  ? 0.5859 0.4357 0.5370 -0.0089 -0.0557 0.1340  178  ASN A CG  
2811  O OD1 . ASN D 181  ? 0.6575 0.5216 0.6141 0.0000  -0.0534 0.1357  178  ASN A OD1 
2812  N ND2 . ASN D 181  ? 0.5832 0.4332 0.5368 -0.0281 -0.0574 0.1384  178  ASN A ND2 
2813  N N   . VAL D 182  ? 0.7786 0.5489 0.6668 0.0454  -0.0662 0.1161  179  VAL A N   
2814  C CA  . VAL D 182  ? 0.7420 0.5014 0.6195 0.0592  -0.0668 0.1090  179  VAL A CA  
2815  C C   . VAL D 182  ? 0.7737 0.5464 0.6470 0.0868  -0.0641 0.1059  179  VAL A C   
2816  O O   . VAL D 182  ? 0.7712 0.5667 0.6542 0.0977  -0.0591 0.1009  179  VAL A O   
2817  C CB  . VAL D 182  ? 0.7494 0.4542 0.5929 0.0553  -0.0776 0.1085  179  VAL A CB  
2818  C CG1 . VAL D 182  ? 0.7442 0.4348 0.5730 0.0726  -0.0789 0.1007  179  VAL A CG1 
2819  C CG2 . VAL D 182  ? 0.7193 0.4197 0.5696 0.0265  -0.0798 0.1124  179  VAL A CG2 
2820  N N   . PHE D 183  ? 0.7911 0.5523 0.6497 0.0988  -0.0675 0.1093  180  PHE A N   
2821  C CA  . PHE D 183  ? 0.7905 0.5652 0.6420 0.1270  -0.0657 0.1072  180  PHE A CA  
2822  C C   . PHE D 183  ? 0.7637 0.5904 0.6442 0.1282  -0.0576 0.1105  180  PHE A C   
2823  O O   . PHE D 183  ? 0.7822 0.6293 0.6603 0.1503  -0.0555 0.1100  180  PHE A O   
2824  C CB  . PHE D 183  ? 0.8338 0.5617 0.6465 0.1432  -0.0752 0.1086  180  PHE A CB  
2825  C CG  . PHE D 183  ? 0.8613 0.5336 0.6381 0.1469  -0.0848 0.1047  180  PHE A CG  
2826  C CD1 . PHE D 183  ? 0.8725 0.5062 0.6365 0.1227  -0.0923 0.1078  180  PHE A CD1 
2827  C CD2 . PHE D 183  ? 0.8964 0.5559 0.6506 0.1745  -0.0869 0.0983  180  PHE A CD2 
2828  C CE1 . PHE D 183  ? 0.9172 0.4974 0.6458 0.1241  -0.1025 0.1047  180  PHE A CE1 
2829  C CE2 . PHE D 183  ? 0.9529 0.5572 0.6706 0.1784  -0.0968 0.0943  180  PHE A CE2 
2830  C CZ  . PHE D 183  ? 0.9077 0.4708 0.6121 0.1522  -0.1050 0.0975  180  PHE A CZ  
2831  N N   . SER D 184  ? 0.7411 0.5903 0.6472 0.1056  -0.0536 0.1140  181  SER A N   
2832  C CA  . SER D 184  ? 0.6923 0.5859 0.6228 0.1046  -0.0473 0.1173  181  SER A CA  
2833  C C   . SER D 184  ? 0.6937 0.6289 0.6411 0.1141  -0.0409 0.1143  181  SER A C   
2834  O O   . SER D 184  ? 0.6982 0.6348 0.6483 0.1131  -0.0393 0.1098  181  SER A O   
2835  C CB  . SER D 184  ? 0.6461 0.5517 0.5971 0.0792  -0.0449 0.1207  181  SER A CB  
2836  O OG  . SER D 184  ? 0.6203 0.5670 0.5933 0.0773  -0.0396 0.1232  181  SER A OG  
2837  N N   . ALA D 185  ? 0.6973 0.6680 0.6557 0.1226  -0.0376 0.1174  182  ALA A N   
2838  C CA  . ALA D 185  ? 0.6793 0.6959 0.6554 0.1277  -0.0319 0.1168  182  ALA A CA  
2839  C C   . ALA D 185  ? 0.6666 0.7136 0.6695 0.1056  -0.0275 0.1189  182  ALA A C   
2840  O O   . ALA D 185  ? 0.6695 0.7534 0.6870 0.1049  -0.0236 0.1192  182  ALA A O   
2841  C CB  . ALA D 185  ? 0.6570 0.6994 0.6285 0.1498  -0.0313 0.1198  182  ALA A CB  
2842  N N   . GLU D 186  ? 0.6747 0.7069 0.6823 0.0878  -0.0287 0.1206  183  GLU A N   
2843  C CA  . GLU D 186  ? 0.6764 0.7321 0.7045 0.0688  -0.0256 0.1221  183  GLU A CA  
2844  C C   . GLU D 186  ? 0.6391 0.6973 0.6750 0.0590  -0.0233 0.1177  183  GLU A C   
2845  O O   . GLU D 186  ? 0.6207 0.6597 0.6471 0.0643  -0.0242 0.1137  183  GLU A O   
2846  C CB  . GLU D 186  ? 0.7339 0.7730 0.7623 0.0553  -0.0276 0.1249  183  GLU A CB  
2847  C CG  . GLU D 186  ? 0.8106 0.8480 0.8322 0.0633  -0.0298 0.1297  183  GLU A CG  
2848  C CD  . GLU D 186  ? 0.8761 0.9522 0.9103 0.0663  -0.0274 0.1328  183  GLU A CD  
2849  O OE1 . GLU D 186  ? 0.9019 1.0015 0.9511 0.0543  -0.0249 0.1325  183  GLU A OE1 
2850  O OE2 . GLU D 186  ? 0.9034 0.9857 0.9309 0.0803  -0.0286 0.1358  183  GLU A OE2 
2851  N N   . ASP D 187  ? 0.6188 0.6989 0.6701 0.0447  -0.0210 0.1185  184  ASP A N   
2852  C CA  . ASP D 187  ? 0.5919 0.6755 0.6501 0.0348  -0.0190 0.1148  184  ASP A CA  
2853  C C   . ASP D 187  ? 0.5596 0.6172 0.6153 0.0229  -0.0200 0.1127  184  ASP A C   
2854  O O   . ASP D 187  ? 0.5399 0.6025 0.6029 0.0100  -0.0193 0.1126  184  ASP A O   
2855  C CB  . ASP D 187  ? 0.5945 0.7087 0.6653 0.0249  -0.0174 0.1169  184  ASP A CB  
2856  C CG  . ASP D 187  ? 0.6119 0.7289 0.6873 0.0158  -0.0159 0.1133  184  ASP A CG  
2857  O OD1 . ASP D 187  ? 0.6168 0.7215 0.6877 0.0213  -0.0150 0.1094  184  ASP A OD1 
2858  O OD2 . ASP D 187  ? 0.6356 0.7647 0.7169 0.0033  -0.0161 0.1144  184  ASP A OD2 
2859  N N   . ILE D 188  ? 0.5662 0.5957 0.6093 0.0280  -0.0225 0.1112  185  ILE A N   
2860  C CA  . ILE D 188  ? 0.5446 0.5515 0.5839 0.0166  -0.0242 0.1104  185  ILE A CA  
2861  C C   . ILE D 188  ? 0.5842 0.5738 0.6156 0.0195  -0.0249 0.1057  185  ILE A C   
2862  O O   . ILE D 188  ? 0.6258 0.6057 0.6462 0.0334  -0.0264 0.1040  185  ILE A O   
2863  C CB  . ILE D 188  ? 0.5377 0.5241 0.5666 0.0154  -0.0281 0.1147  185  ILE A CB  
2864  C CG1 . ILE D 188  ? 0.5979 0.5628 0.6088 0.0307  -0.0318 0.1148  185  ILE A CG1 
2865  C CG2 . ILE D 188  ? 0.4852 0.4895 0.5225 0.0120  -0.0271 0.1192  185  ILE A CG2 
2866  C CD1 . ILE D 188  ? 0.5171 0.4577 0.5142 0.0290  -0.0367 0.1197  185  ILE A CD1 
2867  N N   . SER D 189  ? 0.5647 0.5510 0.6005 0.0075  -0.0241 0.1035  186  SER A N   
2868  C CA  . SER D 189  ? 0.5433 0.5167 0.5736 0.0088  -0.0245 0.0987  186  SER A CA  
2869  C C   . SER D 189  ? 0.5591 0.4984 0.5708 0.0104  -0.0300 0.0989  186  SER A C   
2870  O O   . SER D 189  ? 0.5914 0.5161 0.5947 0.0139  -0.0313 0.0948  186  SER A O   
2871  C CB  . SER D 189  ? 0.4389 0.4205 0.4788 -0.0040 -0.0221 0.0966  186  SER A CB  
2872  O OG  . SER D 189  ? 0.4320 0.4169 0.4759 -0.0148 -0.0226 0.1002  186  SER A OG  
2873  N N   . THR D 190  ? 0.5649 0.4895 0.5682 0.0073  -0.0338 0.1038  187  THR A N   
2874  C CA  . THR D 190  ? 0.6005 0.4884 0.5818 0.0073  -0.0407 0.1049  187  THR A CA  
2875  C C   . THR D 190  ? 0.6374 0.5066 0.6003 0.0271  -0.0438 0.1028  187  THR A C   
2876  O O   . THR D 190  ? 0.7413 0.5737 0.6807 0.0293  -0.0508 0.1026  187  THR A O   
2877  C CB  . THR D 190  ? 0.5409 0.4192 0.5177 -0.0040 -0.0444 0.1118  187  THR A CB  
2878  O OG1 . THR D 190  ? 0.5344 0.4278 0.5168 0.0036  -0.0424 0.1148  187  THR A OG1 
2879  C CG2 . THR D 190  ? 0.5573 0.4524 0.5480 -0.0222 -0.0422 0.1141  187  THR A CG2 
2880  N N   . ALA D 191  ? 0.5831 0.4767 0.5541 0.0417  -0.0395 0.1014  188  ALA A N   
2881  C CA  . ALA D 191  ? 0.6100 0.4926 0.5637 0.0633  -0.0421 0.1006  188  ALA A CA  
2882  C C   . ALA D 191  ? 0.6522 0.5348 0.5992 0.0780  -0.0412 0.0947  188  ALA A C   
2883  O O   . ALA D 191  ? 0.6602 0.5621 0.6219 0.0723  -0.0367 0.0916  188  ALA A O   
2884  C CB  . ALA D 191  ? 0.6034 0.5177 0.5690 0.0715  -0.0383 0.1041  188  ALA A CB  
2885  N N   . ILE D 192  ? 0.6791 0.5388 0.6016 0.0985  -0.0457 0.0931  189  ILE A N   
2886  C CA  . ILE D 192  ? 0.6827 0.5411 0.5940 0.1175  -0.0455 0.0875  189  ILE A CA  
2887  C C   . ILE D 192  ? 0.6949 0.6040 0.6256 0.1294  -0.0380 0.0879  189  ILE A C   
2888  O O   . ILE D 192  ? 0.6979 0.6264 0.6375 0.1315  -0.0341 0.0845  189  ILE A O   
2889  C CB  . ILE D 192  ? 0.6887 0.5030 0.5627 0.1379  -0.0539 0.0856  189  ILE A CB  
2890  C CG1 . ILE D 192  ? 0.7189 0.4813 0.5713 0.1229  -0.0625 0.0852  189  ILE A CG1 
2891  C CG2 . ILE D 192  ? 0.6923 0.5128 0.5545 0.1631  -0.0529 0.0800  189  ILE A CG2 
2892  C CD1 . ILE D 192  ? 0.7942 0.5039 0.6039 0.1409  -0.0728 0.0833  189  ILE A CD1 
2893  N N   . PRO D 193  ? 0.6893 0.6227 0.6265 0.1365  -0.0361 0.0924  190  PRO A N   
2894  C CA  . PRO D 193  ? 0.6677 0.6534 0.6241 0.1440  -0.0296 0.0941  190  PRO A CA  
2895  C C   . PRO D 193  ? 0.6466 0.6618 0.6301 0.1226  -0.0242 0.0946  190  PRO A C   
2896  O O   . PRO D 193  ? 0.6360 0.6833 0.6299 0.1266  -0.0201 0.0940  190  PRO A O   
2897  C CB  . PRO D 193  ? 0.6775 0.6794 0.6359 0.1500  -0.0297 0.0997  190  PRO A CB  
2898  C CG  . PRO D 193  ? 0.7114 0.6653 0.6421 0.1585  -0.0368 0.0992  190  PRO A CG  
2899  C CD  . PRO D 193  ? 0.7141 0.6294 0.6391 0.1400  -0.0404 0.0966  190  PRO A CD  
2900  N N   . HIS D 194  ? 0.6422 0.6471 0.6356 0.1006  -0.0245 0.0961  191  HIS A N   
2901  C CA  . HIS D 194  ? 0.5937 0.6209 0.6082 0.0819  -0.0204 0.0960  191  HIS A CA  
2902  C C   . HIS D 194  ? 0.5837 0.6020 0.5964 0.0803  -0.0195 0.0907  191  HIS A C   
2903  O O   . HIS D 194  ? 0.5771 0.6218 0.6031 0.0753  -0.0157 0.0901  191  HIS A O   
2904  C CB  . HIS D 194  ? 0.5859 0.6023 0.6075 0.0624  -0.0213 0.0983  191  HIS A CB  
2905  C CG  . HIS D 194  ? 0.5896 0.6185 0.6263 0.0452  -0.0184 0.0970  191  HIS A CG  
2906  N ND1 . HIS D 194  ? 0.6086 0.6670 0.6602 0.0366  -0.0157 0.0997  191  HIS A ND1 
2907  C CD2 . HIS D 194  ? 0.5705 0.5850 0.6074 0.0355  -0.0183 0.0933  191  HIS A CD2 
2908  C CE1 . HIS D 194  ? 0.5798 0.6385 0.6382 0.0236  -0.0143 0.0974  191  HIS A CE1 
2909  N NE2 . HIS D 194  ? 0.5615 0.5959 0.6123 0.0232  -0.0154 0.0936  191  HIS A NE2 
2910  N N   . ARG D 195  ? 0.5681 0.5482 0.5632 0.0832  -0.0238 0.0871  192  ARG A N   
2911  C CA  . ARG D 195  ? 0.5485 0.5183 0.5400 0.0825  -0.0236 0.0818  192  ARG A CA  
2912  C C   . ARG D 195  ? 0.5447 0.5364 0.5345 0.1008  -0.0209 0.0796  192  ARG A C   
2913  O O   . ARG D 195  ? 0.5568 0.5610 0.5544 0.0973  -0.0179 0.0769  192  ARG A O   
2914  C CB  . ARG D 195  ? 0.5721 0.4949 0.5412 0.0826  -0.0302 0.0791  192  ARG A CB  
2915  C CG  . ARG D 195  ? 0.5916 0.4991 0.5529 0.0837  -0.0312 0.0733  192  ARG A CG  
2916  C CD  . ARG D 195  ? 0.5801 0.5075 0.5622 0.0664  -0.0265 0.0723  192  ARG A CD  
2917  N NE  . ARG D 195  ? 0.5824 0.5062 0.5735 0.0464  -0.0270 0.0755  192  ARG A NE  
2918  C CZ  . ARG D 195  ? 0.5166 0.4158 0.5006 0.0340  -0.0308 0.0749  192  ARG A CZ  
2919  N NH1 . ARG D 195  ? 0.7868 0.6588 0.7536 0.0381  -0.0352 0.0710  192  ARG A NH1 
2920  N NH2 . ARG D 195  ? 0.5039 0.4071 0.4970 0.0175  -0.0307 0.0785  192  ARG A NH2 
2921  N N   . ILE D 196  ? 0.5467 0.5458 0.5261 0.1211  -0.0218 0.0812  193  ILE A N   
2922  C CA  . ILE D 196  ? 0.5666 0.5910 0.5430 0.1412  -0.0192 0.0799  193  ILE A CA  
2923  C C   . ILE D 196  ? 0.5600 0.6378 0.5607 0.1340  -0.0132 0.0846  193  ILE A C   
2924  O O   . ILE D 196  ? 0.5833 0.6848 0.5909 0.1356  -0.0099 0.0836  193  ILE A O   
2925  C CB  . ILE D 196  ? 0.6125 0.6266 0.5660 0.1681  -0.0228 0.0800  193  ILE A CB  
2926  C CG1 . ILE D 196  ? 0.6440 0.5996 0.5674 0.1754  -0.0303 0.0749  193  ILE A CG1 
2927  C CG2 . ILE D 196  ? 0.6421 0.6947 0.5950 0.1905  -0.0192 0.0801  193  ILE A CG2 
2928  C CD1 . ILE D 196  ? 0.6781 0.6142 0.5726 0.2032  -0.0353 0.0743  193  ILE A CD1 
2929  N N   . VAL D 197  ? 0.5349 0.6314 0.5477 0.1249  -0.0124 0.0902  194  VAL A N   
2930  C CA  . VAL D 197  ? 0.5231 0.6697 0.5548 0.1187  -0.0083 0.0958  194  VAL A CA  
2931  C C   . VAL D 197  ? 0.5276 0.6807 0.5754 0.0938  -0.0064 0.0960  194  VAL A C   
2932  O O   . VAL D 197  ? 0.5697 0.7538 0.6273 0.0891  -0.0037 0.0980  194  VAL A O   
2933  C CB  . VAL D 197  ? 0.5346 0.6979 0.5700 0.1202  -0.0090 0.1017  194  VAL A CB  
2934  C CG1 . VAL D 197  ? 0.5050 0.7188 0.5588 0.1097  -0.0061 0.1083  194  VAL A CG1 
2935  C CG2 . VAL D 197  ? 0.5632 0.7220 0.5803 0.1478  -0.0110 0.1015  194  VAL A CG2 
2936  N N   . GLN D 198  ? 0.5123 0.6368 0.5615 0.0780  -0.0082 0.0943  195  GLN A N   
2937  C CA  . GLN D 198  ? 0.5182 0.6489 0.5802 0.0562  -0.0070 0.0950  195  GLN A CA  
2938  C C   . GLN D 198  ? 0.5961 0.7021 0.6557 0.0486  -0.0069 0.0893  195  GLN A C   
2939  O O   . GLN D 198  ? 0.6261 0.7365 0.6937 0.0331  -0.0060 0.0892  195  GLN A O   
2940  C CB  . GLN D 198  ? 0.4772 0.6017 0.5436 0.0440  -0.0087 0.0980  195  GLN A CB  
2941  C CG  . GLN D 198  ? 0.4714 0.6201 0.5404 0.0502  -0.0090 0.1038  195  GLN A CG  
2942  C CD  . GLN D 198  ? 0.4813 0.6212 0.5530 0.0397  -0.0109 0.1064  195  GLN A CD  
2943  O OE1 . GLN D 198  ? 0.4763 0.6134 0.5434 0.0483  -0.0123 0.1089  195  GLN A OE1 
2944  N NE2 . GLN D 198  ? 0.4985 0.6336 0.5759 0.0223  -0.0112 0.1059  195  GLN A NE2 
2945  N N   . ASP D 199  ? 0.6268 0.7059 0.6737 0.0592  -0.0085 0.0846  196  ASP A N   
2946  C CA  . ASP D 199  ? 0.6392 0.6963 0.6833 0.0521  -0.0088 0.0794  196  ASP A CA  
2947  C C   . ASP D 199  ? 0.6347 0.6961 0.6735 0.0639  -0.0074 0.0757  196  ASP A C   
2948  O O   . ASP D 199  ? 0.6372 0.7091 0.6832 0.0562  -0.0051 0.0742  196  ASP A O   
2949  C CB  . ASP D 199  ? 0.7092 0.7283 0.7415 0.0501  -0.0129 0.0774  196  ASP A CB  
2950  C CG  . ASP D 199  ? 0.7616 0.7763 0.8015 0.0329  -0.0134 0.0797  196  ASP A CG  
2951  O OD1 . ASP D 199  ? 0.7463 0.7784 0.7980 0.0218  -0.0108 0.0805  196  ASP A OD1 
2952  O OD2 . ASP D 199  ? 0.7992 0.7924 0.8314 0.0309  -0.0167 0.0810  196  ASP A OD2 
2953  N N   . ASN D 200  ? 0.6373 0.6900 0.6617 0.0837  -0.0092 0.0741  197  ASN A N   
2954  C CA  . ASN D 200  ? 0.6206 0.6720 0.6363 0.0968  -0.0086 0.0697  197  ASN A CA  
2955  C C   . ASN D 200  ? 0.5991 0.6953 0.6237 0.1053  -0.0044 0.0729  197  ASN A C   
2956  O O   . ASN D 200  ? 0.5914 0.6987 0.6185 0.1060  -0.0021 0.0708  197  ASN A O   
2957  C CB  . ASN D 200  ? 0.6297 0.6473 0.6209 0.1157  -0.0135 0.0660  197  ASN A CB  
2958  C CG  . ASN D 200  ? 0.6091 0.5814 0.5887 0.1051  -0.0185 0.0624  197  ASN A CG  
2959  O OD1 . ASN D 200  ? 0.5237 0.4933 0.5140 0.0868  -0.0174 0.0615  197  ASN A OD1 
2960  N ND2 . ASN D 200  ? 0.6291 0.5657 0.5850 0.1167  -0.0247 0.0607  197  ASN A ND2 
2961  N N   . PHE D 201  ? 0.5722 0.6969 0.6016 0.1113  -0.0034 0.0787  198  PHE A N   
2962  C CA  . PHE D 201  ? 0.5754 0.7481 0.6128 0.1189  0.0002  0.0832  198  PHE A CA  
2963  C C   . PHE D 201  ? 0.5340 0.7316 0.5884 0.0977  0.0029  0.0863  198  PHE A C   
2964  O O   . PHE D 201  ? 0.5205 0.7428 0.5773 0.1018  0.0054  0.0870  198  PHE A O   
2965  C CB  . PHE D 201  ? 0.5761 0.7769 0.6151 0.1286  0.0002  0.0894  198  PHE A CB  
2966  C CG  . PHE D 201  ? 0.5788 0.8361 0.6278 0.1333  0.0037  0.0960  198  PHE A CG  
2967  C CD1 . PHE D 201  ? 0.5947 0.8714 0.6345 0.1569  0.0053  0.0949  198  PHE A CD1 
2968  C CD2 . PHE D 201  ? 0.5789 0.8706 0.6447 0.1138  0.0047  0.1036  198  PHE A CD2 
2969  C CE1 . PHE D 201  ? 0.5943 0.9289 0.6439 0.1605  0.0085  0.1022  198  PHE A CE1 
2970  C CE2 . PHE D 201  ? 0.5742 0.9206 0.6487 0.1151  0.0070  0.1111  198  PHE A CE2 
2971  C CZ  . PHE D 201  ? 0.5798 0.9503 0.6473 0.1383  0.0093  0.1108  198  PHE A CZ  
2972  N N   . PRO D 202  ? 0.4848 0.6771 0.5490 0.0757  0.0021  0.0885  199  PRO A N   
2973  C CA  . PRO D 202  ? 0.4623 0.6690 0.5367 0.0565  0.0034  0.0905  199  PRO A CA  
2974  C C   . PRO D 202  ? 0.4715 0.6594 0.5419 0.0561  0.0044  0.0842  199  PRO A C   
2975  O O   . PRO D 202  ? 0.4634 0.6705 0.5390 0.0481  0.0059  0.0861  199  PRO A O   
2976  C CB  . PRO D 202  ? 0.4208 0.6119 0.4997 0.0377  0.0012  0.0917  199  PRO A CB  
2977  C CG  . PRO D 202  ? 0.4140 0.6054 0.4911 0.0458  -0.0001 0.0943  199  PRO A CG  
2978  C CD  . PRO D 202  ? 0.4528 0.6292 0.5180 0.0682  -0.0002 0.0901  199  PRO A CD  
2979  N N   . LYS D 203  ? 0.4589 0.6095 0.5191 0.0634  0.0029  0.0775  200  LYS A N   
2980  C CA  . LYS D 203  ? 0.4645 0.5984 0.5196 0.0652  0.0035  0.0715  200  LYS A CA  
2981  C C   . LYS D 203  ? 0.5163 0.6699 0.5657 0.0844  0.0053  0.0708  200  LYS A C   
2982  O O   . LYS D 203  ? 0.5273 0.6936 0.5797 0.0822  0.0074  0.0700  200  LYS A O   
2983  C CB  . LYS D 203  ? 0.4723 0.5624 0.5166 0.0663  0.0003  0.0655  200  LYS A CB  
2984  C CG  . LYS D 203  ? 0.4817 0.5555 0.5313 0.0483  -0.0012 0.0661  200  LYS A CG  
2985  C CD  . LYS D 203  ? 0.4925 0.5283 0.5312 0.0483  -0.0047 0.0619  200  LYS A CD  
2986  C CE  . LYS D 203  ? 0.5038 0.5298 0.5480 0.0321  -0.0059 0.0636  200  LYS A CE  
2987  N NZ  . LYS D 203  ? 0.5314 0.5678 0.5851 0.0185  -0.0036 0.0632  200  LYS A NZ  
2988  N N   . PHE D 204  ? 0.5423 0.6989 0.5821 0.1045  0.0043  0.0713  201  PHE A N   
2989  C CA  . PHE D 204  ? 0.5140 0.6917 0.5460 0.1266  0.0059  0.0707  201  PHE A CA  
2990  C C   . PHE D 204  ? 0.4966 0.7293 0.5428 0.1225  0.0098  0.0785  201  PHE A C   
2991  O O   . PHE D 204  ? 0.4829 0.7367 0.5286 0.1300  0.0122  0.0783  201  PHE A O   
2992  C CB  . PHE D 204  ? 0.4955 0.6629 0.5108 0.1509  0.0033  0.0695  201  PHE A CB  
2993  C CG  . PHE D 204  ? 0.5260 0.7175 0.5305 0.1777  0.0048  0.0690  201  PHE A CG  
2994  C CD1 . PHE D 204  ? 0.5620 0.7276 0.5492 0.1925  0.0032  0.0616  201  PHE A CD1 
2995  C CD2 . PHE D 204  ? 0.5284 0.7704 0.5391 0.1888  0.0076  0.0763  201  PHE A CD2 
2996  C CE1 . PHE D 204  ? 0.5701 0.7583 0.5454 0.2196  0.0045  0.0608  201  PHE A CE1 
2997  C CE2 . PHE D 204  ? 0.5268 0.7958 0.5271 0.2157  0.0092  0.0762  201  PHE A CE2 
2998  C CZ  . PHE D 204  ? 0.5453 0.7866 0.5273 0.2321  0.0077  0.0682  201  PHE A CZ  
2999  N N   . LYS D 205  ? 0.5020 0.7589 0.5599 0.1099  0.0099  0.0858  202  LYS A N   
3000  C CA  . LYS D 205  ? 0.5068 0.8160 0.5773 0.1012  0.0123  0.0947  202  LYS A CA  
3001  C C   . LYS D 205  ? 0.5163 0.8267 0.5934 0.0817  0.0132  0.0949  202  LYS A C   
3002  O O   . LYS D 205  ? 0.5155 0.8630 0.5970 0.0813  0.0153  0.0998  202  LYS A O   
3003  C CB  . LYS D 205  ? 0.4859 0.8131 0.5654 0.0881  0.0108  0.1021  202  LYS A CB  
3004  C CG  . LYS D 205  ? 0.4419 0.8156 0.5335 0.0700  0.0113  0.1122  202  LYS A CG  
3005  C CD  . LYS D 205  ? 0.4019 0.7863 0.4999 0.0563  0.0087  0.1187  202  LYS A CD  
3006  C CE  . LYS D 205  ? 0.4062 0.8227 0.5126 0.0309  0.0070  0.1280  202  LYS A CE  
3007  N NZ  . LYS D 205  ? 0.4304 0.9036 0.5413 0.0362  0.0091  0.1363  202  LYS A NZ  
3008  N N   . GLU D 206  ? 0.5203 0.7915 0.5972 0.0660  0.0114  0.0899  203  GLU A N   
3009  C CA  . GLU D 206  ? 0.5017 0.7682 0.5816 0.0500  0.0119  0.0890  203  GLU A CA  
3010  C C   . GLU D 206  ? 0.4962 0.7581 0.5698 0.0641  0.0140  0.0834  203  GLU A C   
3011  O O   . GLU D 206  ? 0.4859 0.7655 0.5627 0.0568  0.0155  0.0856  203  GLU A O   
3012  C CB  . GLU D 206  ? 0.5104 0.7371 0.5895 0.0339  0.0095  0.0846  203  GLU A CB  
3013  C CG  . GLU D 206  ? 0.5481 0.7636 0.6271 0.0200  0.0096  0.0823  203  GLU A CG  
3014  C CD  . GLU D 206  ? 0.5982 0.8425 0.6816 0.0029  0.0087  0.0905  203  GLU A CD  
3015  O OE1 . GLU D 206  ? 0.6310 0.8999 0.7186 -0.0032 0.0073  0.0981  203  GLU A OE1 
3016  O OE2 . GLU D 206  ? 0.6127 0.8543 0.6942 -0.0055 0.0089  0.0898  203  GLU A OE2 
3017  N N   . ASN D 207  ? 0.5317 0.7684 0.5942 0.0838  0.0135  0.0764  204  ASN A N   
3018  C CA  . ASN D 207  ? 0.5357 0.7649 0.5893 0.0986  0.0147  0.0705  204  ASN A CA  
3019  C C   . ASN D 207  ? 0.5313 0.8088 0.5868 0.1116  0.0178  0.0759  204  ASN A C   
3020  O O   . ASN D 207  ? 0.5369 0.8239 0.5918 0.1133  0.0198  0.0746  204  ASN A O   
3021  C CB  . ASN D 207  ? 0.5598 0.7500 0.5969 0.1171  0.0119  0.0628  204  ASN A CB  
3022  C CG  . ASN D 207  ? 0.5645 0.7081 0.5985 0.1036  0.0089  0.0570  204  ASN A CG  
3023  O OD1 . ASN D 207  ? 0.5842 0.7254 0.6286 0.0828  0.0093  0.0584  204  ASN A OD1 
3024  N ND2 . ASN D 207  ? 0.5328 0.6395 0.5506 0.1155  0.0052  0.0509  204  ASN A ND2 
3025  N N   . CYS D 208  ? 0.5342 0.8452 0.5918 0.1212  0.0184  0.0823  205  CYS A N   
3026  C CA  . CYS D 208  ? 0.5421 0.9073 0.6024 0.1337  0.0215  0.0889  205  CYS A CA  
3027  C C   . CYS D 208  ? 0.5600 0.9600 0.6340 0.1099  0.0230  0.0972  205  CYS A C   
3028  O O   . CYS D 208  ? 0.5906 1.0254 0.6657 0.1160  0.0256  0.1007  205  CYS A O   
3029  C CB  . CYS D 208  ? 0.5632 0.9598 0.6233 0.1479  0.0216  0.0949  205  CYS A CB  
3030  S SG  . CYS D 208  ? 0.6113 0.9636 0.6511 0.1755  0.0185  0.0861  205  CYS A SG  
3031  N N   . HIS D 209  ? 0.5374 0.9273 0.6196 0.0830  0.0207  0.1008  206  HIS A N   
3032  C CA  . HIS D 209  ? 0.5075 0.9229 0.5981 0.0586  0.0204  0.1088  206  HIS A CA  
3033  C C   . HIS D 209  ? 0.5217 0.9122 0.6088 0.0519  0.0210  0.1030  206  HIS A C   
3034  O O   . HIS D 209  ? 0.5303 0.9491 0.6202 0.0436  0.0220  0.1087  206  HIS A O   
3035  C CB  . HIS D 209  ? 0.5125 0.9191 0.6081 0.0337  0.0166  0.1136  206  HIS A CB  
3036  C CG  . HIS D 209  ? 0.5734 1.0036 0.6730 0.0074  0.0143  0.1231  206  HIS A CG  
3037  N ND1 . HIS D 209  ? 0.6224 1.0188 0.7181 -0.0140 0.0112  0.1209  206  HIS A ND1 
3038  C CD2 . HIS D 209  ? 0.6223 1.1060 0.7272 -0.0015 0.0140  0.1352  206  HIS A CD2 
3039  C CE1 . HIS D 209  ? 0.6563 1.0792 0.7526 -0.0352 0.0084  0.1310  206  HIS A CE1 
3040  N NE2 . HIS D 209  ? 0.6511 1.1284 0.7538 -0.0296 0.0100  0.1403  206  HIS A NE2 
3041  N N   . ILE D 210  ? 0.5034 0.8427 0.5841 0.0548  0.0201  0.0925  207  ILE A N   
3042  C CA  . ILE D 210  ? 0.5284 0.8442 0.6053 0.0511  0.0207  0.0863  207  ILE A CA  
3043  C C   . ILE D 210  ? 0.5511 0.8870 0.6236 0.0717  0.0239  0.0844  207  ILE A C   
3044  O O   . ILE D 210  ? 0.5322 0.8757 0.6049 0.0665  0.0252  0.0848  207  ILE A O   
3045  C CB  . ILE D 210  ? 0.5332 0.7950 0.6042 0.0510  0.0188  0.0762  207  ILE A CB  
3046  C CG1 . ILE D 210  ? 0.5416 0.7864 0.6162 0.0314  0.0159  0.0783  207  ILE A CG1 
3047  C CG2 . ILE D 210  ? 0.5161 0.7559 0.5827 0.0490  0.0195  0.0697  207  ILE A CG2 
3048  C CD1 . ILE D 210  ? 0.5455 0.7445 0.6152 0.0309  0.0142  0.0699  207  ILE A CD1 
3049  N N   . PHE D 211  ? 0.5844 0.9286 0.6509 0.0966  0.0248  0.0824  208  PHE A N   
3050  C CA  . PHE D 211  ? 0.5965 0.9571 0.6551 0.1205  0.0273  0.0797  208  PHE A CA  
3051  C C   . PHE D 211  ? 0.6444 1.0649 0.7112 0.1172  0.0303  0.0902  208  PHE A C   
3052  O O   . PHE D 211  ? 0.6801 1.1100 0.7458 0.1181  0.0322  0.0895  208  PHE A O   
3053  C CB  . PHE D 211  ? 0.5768 0.9312 0.6232 0.1491  0.0266  0.0756  208  PHE A CB  
3054  C CG  . PHE D 211  ? 0.5839 0.9579 0.6186 0.1778  0.0286  0.0731  208  PHE A CG  
3055  C CD1 . PHE D 211  ? 0.6019 0.9385 0.6223 0.1900  0.0275  0.0629  208  PHE A CD1 
3056  C CD2 . PHE D 211  ? 0.5827 1.0139 0.6195 0.1934  0.0313  0.0812  208  PHE A CD2 
3057  C CE1 . PHE D 211  ? 0.6261 0.9784 0.6330 0.2182  0.0288  0.0600  208  PHE A CE1 
3058  C CE2 . PHE D 211  ? 0.5937 1.0448 0.6179 0.2226  0.0333  0.0788  208  PHE A CE2 
3059  C CZ  . PHE D 211  ? 0.6155 1.0251 0.6239 0.2355  0.0319  0.0678  208  PHE A CZ  
3060  N N   . THR D 212  ? 0.6500 1.1136 0.7251 0.1124  0.0305  0.1007  209  THR A N   
3061  C CA  . THR D 212  ? 0.6400 1.1675 0.7223 0.1097  0.0329  0.1124  209  THR A CA  
3062  C C   . THR D 212  ? 0.6117 1.1438 0.7005 0.0796  0.0319  0.1181  209  THR A C   
3063  O O   . THR D 212  ? 0.6331 1.2065 0.7245 0.0784  0.0340  0.1250  209  THR A O   
3064  C CB  . THR D 212  ? 0.6514 1.2248 0.7410 0.1089  0.0326  0.1231  209  THR A CB  
3065  O OG1 . THR D 212  ? 0.6803 1.2360 0.7765 0.0806  0.0288  0.1268  209  THR A OG1 
3066  C CG2 . THR D 212  ? 0.6622 1.2296 0.7425 0.1409  0.0332  0.1174  209  THR A CG2 
3067  N N   . ARG D 213  ? 0.5832 1.0738 0.6730 0.0560  0.0284  0.1156  210  ARG A N   
3068  C CA  . ARG D 213  ? 0.5982 1.0856 0.6893 0.0292  0.0265  0.1201  210  ARG A CA  
3069  C C   . ARG D 213  ? 0.6275 1.0961 0.7130 0.0369  0.0287  0.1126  210  ARG A C   
3070  O O   . ARG D 213  ? 0.6534 1.1437 0.7396 0.0248  0.0290  0.1187  210  ARG A O   
3071  C CB  . ARG D 213  ? 0.6041 1.0487 0.6938 0.0063  0.0218  0.1182  210  ARG A CB  
3072  C CG  . ARG D 213  ? 0.6569 1.1233 0.7512 -0.0096 0.0183  0.1282  210  ARG A CG  
3073  C CD  . ARG D 213  ? 0.7091 1.1373 0.7984 -0.0358 0.0128  0.1281  210  ARG A CD  
3074  N NE  . ARG D 213  ? 0.7602 1.1883 0.8439 -0.0562 0.0103  0.1329  210  ARG A NE  
3075  C CZ  . ARG D 213  ? 0.7981 1.1905 0.8724 -0.0777 0.0049  0.1326  210  ARG A CZ  
3076  N NH1 . ARG D 213  ? 0.8019 1.1590 0.8729 -0.0813 0.0020  0.1277  210  ARG A NH1 
3077  N NH2 . ARG D 213  ? 0.8071 1.1986 0.8735 -0.0948 0.0020  0.1372  210  ARG A NH2 
3078  N N   . LEU D 214  ? 0.5960 1.0239 0.6749 0.0557  0.0298  0.0997  211  LEU A N   
3079  C CA  . LEU D 214  ? 0.5509 0.9604 0.6237 0.0641  0.0316  0.0921  211  LEU A CA  
3080  C C   . LEU D 214  ? 0.5675 1.0214 0.6389 0.0846  0.0355  0.0952  211  LEU A C   
3081  O O   . LEU D 214  ? 0.5617 1.0274 0.6324 0.0814  0.0371  0.0964  211  LEU A O   
3082  C CB  . LEU D 214  ? 0.5060 0.8613 0.5706 0.0772  0.0307  0.0785  211  LEU A CB  
3083  C CG  . LEU D 214  ? 0.4638 0.7738 0.5286 0.0589  0.0274  0.0741  211  LEU A CG  
3084  C CD1 . LEU D 214  ? 0.4434 0.7082 0.4999 0.0726  0.0262  0.0625  211  LEU A CD1 
3085  C CD2 . LEU D 214  ? 0.4326 0.7324 0.4978 0.0383  0.0265  0.0752  211  LEU A CD2 
3086  N N   . ILE D 215  ? 0.5902 1.0699 0.6600 0.1071  0.0369  0.0965  212  ILE A N   
3087  C CA  . ILE D 215  ? 0.6210 1.1439 0.6870 0.1316  0.0405  0.0987  212  ILE A CA  
3088  C C   . ILE D 215  ? 0.6326 1.2182 0.7088 0.1160  0.0422  0.1135  212  ILE A C   
3089  O O   . ILE D 215  ? 0.6730 1.2904 0.7475 0.1263  0.0453  0.1159  212  ILE A O   
3090  C CB  . ILE D 215  ? 0.6564 1.1901 0.7150 0.1613  0.0410  0.0965  212  ILE A CB  
3091  C CG1 . ILE D 215  ? 0.6781 1.1455 0.7237 0.1737  0.0380  0.0827  212  ILE A CG1 
3092  C CG2 . ILE D 215  ? 0.6796 1.2583 0.7312 0.1906  0.0446  0.0983  212  ILE A CG2 
3093  C CD1 . ILE D 215  ? 0.6671 1.0913 0.7027 0.1778  0.0374  0.0717  212  ILE A CD1 
3094  N N   . THR D 216  ? 0.6208 1.2255 0.7066 0.0902  0.0398  0.1242  213  THR A N   
3095  C CA  . THR D 216  ? 0.6242 1.2873 0.7179 0.0710  0.0399  0.1398  213  THR A CA  
3096  C C   . THR D 216  ? 0.6234 1.2699 0.7155 0.0495  0.0388  0.1405  213  THR A C   
3097  O O   . THR D 216  ? 0.6384 1.3282 0.7321 0.0470  0.0407  0.1488  213  THR A O   
3098  C CB  . THR D 216  ? 0.6141 1.2970 0.7154 0.0475  0.0361  0.1509  213  THR A CB  
3099  O OG1 . THR D 216  ? 0.6093 1.3093 0.7119 0.0693  0.0374  0.1503  213  THR A OG1 
3100  C CG2 . THR D 216  ? 0.6144 1.3599 0.7221 0.0252  0.0350  0.1686  213  THR A CG2 
3101  N N   . ALA D 217  ? 0.6241 1.2094 0.7119 0.0347  0.0356  0.1321  214  ALA A N   
3102  C CA  . ALA D 217  ? 0.6442 1.2090 0.7280 0.0160  0.0342  0.1319  214  ALA A CA  
3103  C C   . ALA D 217  ? 0.6529 1.2069 0.7315 0.0378  0.0382  0.1223  214  ALA A C   
3104  O O   . ALA D 217  ? 0.6781 1.2540 0.7557 0.0320  0.0394  0.1273  214  ALA A O   
3105  C CB  . ALA D 217  ? 0.6342 1.1393 0.7133 -0.0037 0.0295  0.1259  214  ALA A CB  
3106  N N   . VAL D 218  ? 0.6221 1.1413 0.6957 0.0621  0.0397  0.1089  215  VAL A N   
3107  C CA  . VAL D 218  ? 0.5938 1.0976 0.6597 0.0837  0.0425  0.0988  215  VAL A CA  
3108  C C   . VAL D 218  ? 0.6144 1.1383 0.6755 0.1178  0.0452  0.0952  215  VAL A C   
3109  O O   . VAL D 218  ? 0.6140 1.0993 0.6677 0.1334  0.0438  0.0849  215  VAL A O   
3110  C CB  . VAL D 218  ? 0.5645 1.0018 0.6242 0.0807  0.0404  0.0855  215  VAL A CB  
3111  C CG1 . VAL D 218  ? 0.5695 0.9923 0.6207 0.0992  0.0425  0.0761  215  VAL A CG1 
3112  C CG2 . VAL D 218  ? 0.5322 0.9484 0.5940 0.0495  0.0372  0.0891  215  VAL A CG2 
3113  N N   . PRO D 219  ? 0.6378 1.2212 0.7006 0.1308  0.0485  0.1036  216  PRO A N   
3114  C CA  . PRO D 219  ? 0.6686 1.2721 0.7233 0.1666  0.0506  0.1001  216  PRO A CA  
3115  C C   . PRO D 219  ? 0.6950 1.2542 0.7331 0.1935  0.0505  0.0848  216  PRO A C   
3116  O O   . PRO D 219  ? 0.7217 1.2703 0.7474 0.2216  0.0498  0.0783  216  PRO A O   
3117  C CB  . PRO D 219  ? 0.6628 1.3443 0.7232 0.1719  0.0544  0.1136  216  PRO A CB  
3118  C CG  . PRO D 219  ? 0.6503 1.3542 0.7239 0.1329  0.0528  0.1268  216  PRO A CG  
3119  C CD  . PRO D 219  ? 0.6413 1.2798 0.7125 0.1122  0.0498  0.1182  216  PRO A CD  
3120  N N   . SER D 220  ? 0.7064 1.2378 0.7418 0.1857  0.0505  0.0790  217  SER A N   
3121  C CA  . SER D 220  ? 0.7197 1.2060 0.7382 0.2083  0.0493  0.0646  217  SER A CA  
3122  C C   . SER D 220  ? 0.7684 1.1936 0.7787 0.2099  0.0447  0.0542  217  SER A C   
3123  O O   . SER D 220  ? 0.8013 1.1907 0.7934 0.2326  0.0423  0.0431  217  SER A O   
3124  C CB  . SER D 220  ? 0.6810 1.1502 0.6999 0.1957  0.0499  0.0612  217  SER A CB  
3125  O OG  . SER D 220  ? 0.6580 1.0964 0.6861 0.1643  0.0477  0.0617  217  SER A OG  
3126  N N   . LEU D 221  ? 0.7720 1.1839 0.7933 0.1859  0.0429  0.0578  218  LEU A N   
3127  C CA  . LEU D 221  ? 0.7629 1.1219 0.7778 0.1853  0.0387  0.0497  218  LEU A CA  
3128  C C   . LEU D 221  ? 0.7610 1.1226 0.7647 0.2110  0.0373  0.0481  218  LEU A C   
3129  O O   . LEU D 221  ? 0.7431 1.0571 0.7354 0.2167  0.0331  0.0400  218  LEU A O   
3130  C CB  . LEU D 221  ? 0.7298 1.0795 0.7591 0.1541  0.0373  0.0549  218  LEU A CB  
3131  C CG  . LEU D 221  ? 0.7290 1.0226 0.7565 0.1387  0.0341  0.0466  218  LEU A CG  
3132  C CD1 . LEU D 221  ? 0.7329 1.0083 0.7543 0.1404  0.0346  0.0398  218  LEU A CD1 
3133  C CD2 . LEU D 221  ? 0.7206 1.0155 0.7611 0.1094  0.0334  0.0534  218  LEU A CD2 
3134  N N   . ARG D 222  ? 0.7766 1.1938 0.7823 0.2264  0.0404  0.0562  219  ARG A N   
3135  C CA  . ARG D 222  ? 0.7973 1.2197 0.7902 0.2539  0.0391  0.0548  219  ARG A CA  
3136  C C   . ARG D 222  ? 0.8311 1.2159 0.7970 0.2855  0.0362  0.0425  219  ARG A C   
3137  O O   . ARG D 222  ? 0.8478 1.1859 0.7969 0.2968  0.0312  0.0348  219  ARG A O   
3138  C CB  . ARG D 222  ? 0.7834 1.2813 0.7850 0.2634  0.0435  0.0673  219  ARG A CB  
3139  C CG  . ARG D 222  ? 0.8134 1.3241 0.8027 0.2923  0.0425  0.0674  219  ARG A CG  
3140  C CD  . ARG D 222  ? 0.8747 1.3931 0.8404 0.3334  0.0428  0.0613  219  ARG A CD  
3141  N NE  . ARG D 222  ? 0.9330 1.4427 0.8794 0.3637  0.0401  0.0580  219  ARG A NE  
3142  C CZ  . ARG D 222  ? 0.9948 1.4947 0.9129 0.4033  0.0382  0.0503  219  ARG A CZ  
3143  N NH1 . ARG D 222  ? 1.0152 1.5140 0.9222 0.4170  0.0391  0.0452  219  ARG A NH1 
3144  N NH2 . ARG D 222  ? 1.0270 1.5159 0.9255 0.4302  0.0350  0.0476  219  ARG A NH2 
3145  N N   . GLU D 223  ? 0.8491 1.2525 0.8083 0.2999  0.0385  0.0408  220  GLU A N   
3146  C CA  . GLU D 223  ? 0.8956 1.2601 0.8261 0.3297  0.0348  0.0286  220  GLU A CA  
3147  C C   . GLU D 223  ? 0.9260 1.2171 0.8473 0.3157  0.0290  0.0178  220  GLU A C   
3148  O O   . GLU D 223  ? 0.9689 1.2115 0.8632 0.3355  0.0230  0.0077  220  GLU A O   
3149  C CB  . GLU D 223  ? 0.9045 1.3050 0.8313 0.3451  0.0387  0.0293  220  GLU A CB  
3150  N N   . HIS D 224  ? 0.9151 1.1970 0.8567 0.2818  0.0302  0.0201  221  HIS A N   
3151  C CA  . HIS D 224  ? 0.9368 1.1564 0.8719 0.2672  0.0251  0.0111  221  HIS A CA  
3152  C C   . HIS D 224  ? 0.9266 1.1075 0.8546 0.2641  0.0198  0.0087  221  HIS A C   
3153  O O   . HIS D 224  ? 0.9317 1.0582 0.8399 0.2686  0.0133  -0.0002 221  HIS A O   
3154  C CB  . HIS D 224  ? 0.9439 1.1685 0.9012 0.2346  0.0279  0.0147  221  HIS A CB  
3155  C CG  . HIS D 224  ? 0.9943 1.1685 0.9440 0.2247  0.0241  0.0055  221  HIS A CG  
3156  N ND1 . HIS D 224  ? 0.9916 1.1699 0.9520 0.2076  0.0266  0.0057  221  HIS A ND1 
3157  C CD2 . HIS D 224  ? 1.0268 1.1465 0.9584 0.2286  0.0175  -0.0036 221  HIS A CD2 
3158  C CE1 . HIS D 224  ? 0.9986 1.1302 0.9493 0.2025  0.0222  -0.0030 221  HIS A CE1 
3159  N NE2 . HIS D 224  ? 1.0209 1.1169 0.9542 0.2138  0.0164  -0.0084 221  HIS A NE2 
3160  N N   . PHE D 225  ? 0.8888 1.0969 0.8320 0.2552  0.0220  0.0171  222  PHE A N   
3161  C CA  . PHE D 225  ? 0.8589 1.0346 0.7948 0.2547  0.0173  0.0156  222  PHE A CA  
3162  C C   . PHE D 225  ? 0.8877 1.0435 0.7936 0.2888  0.0127  0.0098  222  PHE A C   
3163  O O   . PHE D 225  ? 0.8827 0.9866 0.7700 0.2916  0.0058  0.0038  222  PHE A O   
3164  C CB  . PHE D 225  ? 0.7948 1.0081 0.7523 0.2400  0.0208  0.0261  222  PHE A CB  
3165  C CG  . PHE D 225  ? 0.7370 0.9545 0.7178 0.2057  0.0229  0.0307  222  PHE A CG  
3166  C CD1 . PHE D 225  ? 0.7350 0.9127 0.7153 0.1895  0.0206  0.0245  222  PHE A CD1 
3167  C CD2 . PHE D 225  ? 0.6919 0.9524 0.6925 0.1901  0.0264  0.0413  222  PHE A CD2 
3168  C CE1 . PHE D 225  ? 0.6810 0.8615 0.6793 0.1612  0.0223  0.0283  222  PHE A CE1 
3169  C CE2 . PHE D 225  ? 0.6508 0.9099 0.6678 0.1602  0.0272  0.0451  222  PHE A CE2 
3170  C CZ  . PHE D 225  ? 0.6427 0.8613 0.6578 0.1471  0.0253  0.0383  222  PHE A CZ  
3171  N N   . GLU D 226  ? 0.9329 1.1297 0.8319 0.3154  0.0159  0.0120  223  GLU A N   
3172  C CA  . GLU D 226  ? 1.0066 1.1856 0.8732 0.3523  0.0113  0.0063  223  GLU A CA  
3173  C C   . GLU D 226  ? 1.0519 1.1677 0.8883 0.3628  0.0038  -0.0059 223  GLU A C   
3174  O O   . GLU D 226  ? 1.0866 1.1551 0.8919 0.3811  -0.0041 -0.0125 223  GLU A O   
3175  C CB  . GLU D 226  ? 1.0403 1.2830 0.9064 0.3793  0.0169  0.0116  223  GLU A CB  
3176  C CG  . GLU D 226  ? 1.1251 1.3533 0.9544 0.4227  0.0123  0.0054  223  GLU A CG  
3177  C CD  . GLU D 226  ? 1.1754 1.4079 0.9986 0.4345  0.0105  0.0090  223  GLU A CD  
3178  O OE1 . GLU D 226  ? 1.1557 1.4416 1.0066 0.4209  0.0163  0.0200  223  GLU A OE1 
3179  O OE2 . GLU D 226  ? 1.2335 1.4145 1.0226 0.4569  0.0027  0.0012  223  GLU A OE2 
3180  N N   . ASN D 227  ? 1.0802 1.1926 0.9233 0.3508  0.0054  -0.0089 224  ASN A N   
3181  C CA  . ASN D 227  ? 1.1182 1.1718 0.9331 0.3581  -0.0022 -0.0202 224  ASN A CA  
3182  C C   . ASN D 227  ? 1.1034 1.0962 0.9115 0.3365  -0.0099 -0.0241 224  ASN A C   
3183  O O   . ASN D 227  ? 1.1594 1.0952 0.9342 0.3479  -0.0194 -0.0324 224  ASN A O   
3184  C CB  . ASN D 227  ? 1.1257 1.1940 0.9520 0.3484  0.0017  -0.0217 224  ASN A CB  
3185  C CG  . ASN D 227  ? 1.1424 1.2684 0.9711 0.3715  0.0084  -0.0180 224  ASN A CG  
3186  O OD1 . ASN D 227  ? 1.1194 1.2850 0.9712 0.3574  0.0150  -0.0130 224  ASN A OD1 
3187  N ND2 . ASN D 227  ? 1.1758 1.3076 0.9790 0.4076  0.0063  -0.0202 224  ASN A ND2 
3188  N N   . VAL D 228  ? 1.0299 1.0336 0.8673 0.3051  -0.0066 -0.0179 225  VAL A N   
3189  C CA  . VAL D 228  ? 1.0035 0.9570 0.8367 0.2839  -0.0132 -0.0203 225  VAL A CA  
3190  C C   . VAL D 228  ? 1.0070 0.9305 0.8163 0.2994  -0.0199 -0.0212 225  VAL A C   
3191  O O   . VAL D 228  ? 1.0291 0.8952 0.8143 0.2962  -0.0294 -0.0264 225  VAL A O   
3192  C CB  . VAL D 228  ? 0.9383 0.9150 0.8071 0.2504  -0.0077 -0.0131 225  VAL A CB  
3193  C CG1 . VAL D 228  ? 0.9234 0.8543 0.7884 0.2297  -0.0141 -0.0146 225  VAL A CG1 
3194  C CG2 . VAL D 228  ? 0.9026 0.9023 0.7901 0.2361  -0.0022 -0.0127 225  VAL A CG2 
3195  N N   . LYS D 229  ? 0.9800 0.9423 0.7943 0.3160  -0.0156 -0.0156 226  LYS A N   
3196  C CA  . LYS D 229  ? 0.9891 0.9251 0.7796 0.3333  -0.0217 -0.0163 226  LYS A CA  
3197  C C   . LYS D 229  ? 1.0678 0.9599 0.8128 0.3658  -0.0305 -0.0254 226  LYS A C   
3198  O O   . LYS D 229  ? 1.1030 0.9389 0.8178 0.3709  -0.0405 -0.0295 226  LYS A O   
3199  C CB  . LYS D 229  ? 0.9350 0.9287 0.7423 0.3445  -0.0147 -0.0078 226  LYS A CB  
3200  C CG  . LYS D 229  ? 0.9312 0.9029 0.7242 0.3525  -0.0197 -0.0063 226  LYS A CG  
3201  C CD  . LYS D 229  ? 0.9313 0.9446 0.7159 0.3857  -0.0166 -0.0029 226  LYS A CD  
3202  C CE  . LYS D 229  ? 1.0024 0.9975 0.7490 0.4237  -0.0211 -0.0109 226  LYS A CE  
3203  N NZ  . LYS D 229  ? 1.0439 1.0789 0.7785 0.4600  -0.0187 -0.0078 226  LYS A NZ  
3204  N N   . LYS D 230  ? 1.1125 1.0277 0.8496 0.3880  -0.0276 -0.0285 227  LYS A N   
3205  C CA  . LYS D 230  ? 1.1958 1.0686 0.8864 0.4216  -0.0363 -0.0378 227  LYS A CA  
3206  C C   . LYS D 230  ? 1.2436 1.0481 0.9115 0.4076  -0.0463 -0.0462 227  LYS A C   
3207  O O   . LYS D 230  ? 1.2566 1.0010 0.8798 0.4257  -0.0580 -0.0535 227  LYS A O   
3208  C CB  . LYS D 230  ? 1.2068 1.1289 0.8964 0.4500  -0.0298 -0.0383 227  LYS A CB  
3209  C CG  . LYS D 230  ? 1.2055 1.1941 0.9077 0.4712  -0.0219 -0.0303 227  LYS A CG  
3210  C CD  . LYS D 230  ? 1.2158 1.2541 0.9143 0.4999  -0.0161 -0.0303 227  LYS A CD  
3211  C CE  . LYS D 230  ? 1.2099 1.3164 0.9168 0.5237  -0.0093 -0.0219 227  LYS A CE  
3212  N NZ  . LYS D 230  ? 1.2061 1.3653 0.9085 0.5473  -0.0038 -0.0206 227  LYS A NZ  
3213  N N   . ALA D 231  ? 1.2949 1.1067 0.9906 0.3757  -0.0427 -0.0450 228  ALA A N   
3214  C CA  . ALA D 231  ? 1.3075 1.0617 0.9843 0.3607  -0.0518 -0.0520 228  ALA A CA  
3215  C C   . ALA D 231  ? 1.3327 1.0310 0.9948 0.3411  -0.0619 -0.0520 228  ALA A C   
3216  O O   . ALA D 231  ? 1.3761 1.0166 1.0096 0.3344  -0.0730 -0.0579 228  ALA A O   
3217  C CB  . ALA D 231  ? 1.2517 1.0341 0.9631 0.3332  -0.0446 -0.0501 228  ALA A CB  
3218  N N   . ILE D 232  ? 1.3056 1.0202 0.9858 0.3309  -0.0588 -0.0449 229  ILE A N   
3219  C CA  . ILE D 232  ? 1.3135 0.9791 0.9807 0.3120  -0.0681 -0.0437 229  ILE A CA  
3220  C C   . ILE D 232  ? 1.3850 1.0082 1.0089 0.3394  -0.0779 -0.0466 229  ILE A C   
3221  O O   . ILE D 232  ? 1.4576 1.0155 1.0463 0.3342  -0.0911 -0.0501 229  ILE A O   
3222  C CB  . ILE D 232  ? 1.2267 0.9295 0.9361 0.2842  -0.0600 -0.0346 229  ILE A CB  
3223  C CG1 . ILE D 232  ? 1.1765 0.9113 0.9223 0.2573  -0.0522 -0.0325 229  ILE A CG1 
3224  C CG2 . ILE D 232  ? 1.2338 0.8907 0.9298 0.2664  -0.0691 -0.0325 229  ILE A CG2 
3225  C CD1 . ILE D 232  ? 1.1060 0.8709 0.8886 0.2300  -0.0457 -0.0244 229  ILE A CD1 
3226  N N   . GLY D 233  ? 1.3561 1.0155 0.9798 0.3686  -0.0722 -0.0447 230  GLY A N   
3227  C CA  . GLY D 233  ? 1.3962 1.0205 0.9786 0.3986  -0.0807 -0.0473 230  GLY A CA  
3228  C C   . GLY D 233  ? 1.3803 1.0231 0.9768 0.3955  -0.0777 -0.0398 230  GLY A C   
3229  O O   . GLY D 233  ? 1.4423 1.0510 1.0030 0.4186  -0.0856 -0.0416 230  GLY A O   
3230  N N   . ILE D 234  ? 1.3061 0.9995 0.9509 0.3689  -0.0672 -0.0318 231  ILE A N   
3231  C CA  . ILE D 234  ? 1.2826 0.9964 0.9439 0.3632  -0.0640 -0.0243 231  ILE A CA  
3232  C C   . ILE D 234  ? 1.2776 1.0556 0.9523 0.3899  -0.0545 -0.0203 231  ILE A C   
3233  O O   . ILE D 234  ? 1.2549 1.0842 0.9514 0.3941  -0.0456 -0.0191 231  ILE A O   
3234  C CB  . ILE D 234  ? 1.2101 0.9447 0.9139 0.3216  -0.0583 -0.0177 231  ILE A CB  
3235  C CG1 . ILE D 234  ? 1.2107 0.8893 0.9022 0.2952  -0.0674 -0.0209 231  ILE A CG1 
3236  C CG2 . ILE D 234  ? 1.2012 0.9535 0.9200 0.3155  -0.0557 -0.0103 231  ILE A CG2 
3237  C CD1 . ILE D 234  ? 1.1526 0.8529 0.8834 0.2571  -0.0618 -0.0150 231  ILE A CD1 
3238  N N   . PHE D 235  ? 1.2936 1.0703 0.9546 0.4078  -0.0566 -0.0177 232  PHE A N   
3239  C CA  . PHE D 235  ? 1.2790 1.1204 0.9536 0.4315  -0.0480 -0.0123 232  PHE A CA  
3240  C C   . PHE D 235  ? 1.3336 1.1993 0.9911 0.4667  -0.0459 -0.0167 232  PHE A C   
3241  O O   . PHE D 235  ? 1.2906 1.2230 0.9776 0.4674  -0.0355 -0.0121 232  PHE A O   
3242  C CB  . PHE D 235  ? 1.1804 1.0880 0.9087 0.4028  -0.0362 -0.0026 232  PHE A CB  
3243  C CG  . PHE D 235  ? 1.1259 1.0138 0.8721 0.3691  -0.0377 0.0017  232  PHE A CG  
3244  C CD1 . PHE D 235  ? 1.1486 0.9868 0.8687 0.3729  -0.0465 0.0007  232  PHE A CD1 
3245  C CD2 . PHE D 235  ? 1.0594 0.9779 0.8463 0.3345  -0.0306 0.0069  232  PHE A CD2 
3246  C CE1 . PHE D 235  ? 1.1192 0.9428 0.8561 0.3423  -0.0476 0.0051  232  PHE A CE1 
3247  C CE2 . PHE D 235  ? 1.0343 0.9369 0.8364 0.3059  -0.0319 0.0107  232  PHE A CE2 
3248  C CZ  . PHE D 235  ? 1.0605 0.9176 0.8387 0.3095  -0.0400 0.0100  232  PHE A CZ  
3249  N N   . VAL D 236  ? 1.4632 1.2718 1.0699 0.4960  -0.0566 -0.0255 233  VAL A N   
3250  C CA  . VAL D 236  ? 1.4854 1.3094 1.0697 0.5322  -0.0559 -0.0310 233  VAL A CA  
3251  C C   . VAL D 236  ? 1.4767 1.3699 1.0667 0.5599  -0.0478 -0.0256 233  VAL A C   
3252  O O   . VAL D 236  ? 1.4802 1.4238 1.0750 0.5731  -0.0408 -0.0253 233  VAL A O   
3253  C CB  . VAL D 236  ? 1.5477 1.2897 1.0727 0.5478  -0.0702 -0.0422 233  VAL A CB  
3254  C CG1 . VAL D 236  ? 1.5353 1.2175 1.0565 0.5212  -0.0779 -0.0468 233  VAL A CG1 
3255  C CG2 . VAL D 236  ? 1.6083 1.3086 1.0991 0.5566  -0.0787 -0.0430 233  VAL A CG2 
3256  N N   . SER D 237  ? 1.4549 1.3546 1.0447 0.5637  -0.0481 -0.0207 234  SER A N   
3257  C CA  . SER D 237  ? 1.4248 1.3903 1.0185 0.5837  -0.0404 -0.0153 234  SER A CA  
3258  C C   . SER D 237  ? 1.3049 1.3547 0.9551 0.5686  -0.0283 -0.0027 234  SER A C   
3259  O O   . SER D 237  ? 1.2547 1.3625 0.9128 0.5797  -0.0220 0.0038  234  SER A O   
3260  C CB  . SER D 237  ? 1.4878 1.4172 1.0487 0.5969  -0.0473 -0.0169 234  SER A CB  
3261  O OG  . SER D 237  ? 1.4966 1.4921 1.0631 0.6150  -0.0395 -0.0111 234  SER A OG  
3262  N N   . THR D 238  ? 1.2480 1.3051 0.9352 0.5336  -0.0246 0.0006  235  THR A N   
3263  C CA  . THR D 238  ? 1.1477 1.2744 0.8855 0.5046  -0.0141 0.0121  235  THR A CA  
3264  C C   . THR D 238  ? 1.0864 1.2413 0.8511 0.4824  -0.0079 0.0133  235  THR A C   
3265  O O   . THR D 238  ? 1.1349 1.2405 0.8954 0.4640  -0.0119 0.0068  235  THR A O   
3266  C CB  . THR D 238  ? 1.0956 1.1958 0.8511 0.4704  -0.0160 0.0156  235  THR A CB  
3267  O OG1 . THR D 238  ? 1.1194 1.1686 0.8404 0.4894  -0.0247 0.0117  235  THR A OG1 
3268  C CG2 . THR D 238  ? 1.0364 1.2088 0.8337 0.4515  -0.0070 0.0277  235  THR A CG2 
3269  N N   . SER D 239  ? 1.0057 1.2405 0.7974 0.4835  0.0013  0.0221  236  SER A N   
3270  C CA  . SER D 239  ? 0.9625 1.2282 0.7801 0.4616  0.0073  0.0247  236  SER A CA  
3271  C C   . SER D 239  ? 0.9476 1.2077 0.7994 0.4144  0.0094  0.0294  236  SER A C   
3272  O O   . SER D 239  ? 0.9710 1.2116 0.8290 0.3992  0.0072  0.0315  236  SER A O   
3273  C CB  . SER D 239  ? 0.9500 1.3043 0.7841 0.4756  0.0157  0.0342  236  SER A CB  
3274  O OG  . SER D 239  ? 0.9396 1.3472 0.8013 0.4602  0.0203  0.0461  236  SER A OG  
3275  N N   . ILE D 240  ? 0.9317 1.2089 0.8043 0.3922  0.0137  0.0309  237  ILE A N   
3276  C CA  . ILE D 240  ? 0.8960 1.1629 0.7963 0.3500  0.0150  0.0341  237  ILE A CA  
3277  C C   . ILE D 240  ? 0.8839 1.2092 0.8141 0.3316  0.0204  0.0467  237  ILE A C   
3278  O O   . ILE D 240  ? 0.8707 1.1823 0.8180 0.3022  0.0199  0.0496  237  ILE A O   
3279  C CB  . ILE D 240  ? 0.8533 1.1146 0.7624 0.3337  0.0170  0.0311  237  ILE A CB  
3280  C CG1 . ILE D 240  ? 0.8029 1.0381 0.7323 0.2945  0.0165  0.0318  237  ILE A CG1 
3281  C CG2 . ILE D 240  ? 0.8364 1.1685 0.7623 0.3361  0.0242  0.0393  237  ILE A CG2 
3282  C CD1 . ILE D 240  ? 0.7970 0.9666 0.7119 0.2885  0.0094  0.0250  237  ILE A CD1 
3283  N N   . GLU D 241  ? 0.9001 1.2921 0.8361 0.3480  0.0252  0.0548  238  GLU A N   
3284  C CA  . GLU D 241  ? 0.8751 1.3236 0.8372 0.3297  0.0291  0.0676  238  GLU A CA  
3285  C C   . GLU D 241  ? 0.8570 1.2940 0.8136 0.3367  0.0262  0.0687  238  GLU A C   
3286  O O   . GLU D 241  ? 0.8208 1.2753 0.7979 0.3119  0.0271  0.0764  238  GLU A O   
3287  C CB  . GLU D 241  ? 0.9073 1.4359 0.8774 0.3437  0.0347  0.0773  238  GLU A CB  
3288  C CG  . GLU D 241  ? 0.9159 1.4698 0.9001 0.3261  0.0384  0.0806  238  GLU A CG  
3289  C CD  . GLU D 241  ? 0.9468 1.4851 0.9099 0.3532  0.0383  0.0716  238  GLU A CD  
3290  O OE1 . GLU D 241  ? 0.9154 1.4907 0.8877 0.3481  0.0423  0.0759  238  GLU A OE1 
3291  O OE2 . GLU D 241  ? 0.9982 1.4860 0.9338 0.3793  0.0338  0.0605  238  GLU A OE2 
3292  N N   . GLU D 242  ? 0.9109 1.3160 0.8376 0.3702  0.0220  0.0612  239  GLU A N   
3293  C CA  . GLU D 242  ? 0.8978 1.2918 0.8162 0.3798  0.0189  0.0624  239  GLU A CA  
3294  C C   . GLU D 242  ? 0.8856 1.2156 0.8052 0.3544  0.0141  0.0578  239  GLU A C   
3295  O O   . GLU D 242  ? 0.8691 1.2041 0.7987 0.3433  0.0136  0.0629  239  GLU A O   
3296  C CB  . GLU D 242  ? 0.9608 1.3387 0.8424 0.4257  0.0152  0.0558  239  GLU A CB  
3297  C CG  . GLU D 242  ? 1.0000 1.4484 0.8788 0.4558  0.0202  0.0611  239  GLU A CG  
3298  C CD  . GLU D 242  ? 1.0671 1.4948 0.9047 0.5048  0.0157  0.0536  239  GLU A CD  
3299  O OE1 . GLU D 242  ? 1.1101 1.4709 0.9217 0.5136  0.0083  0.0458  239  GLU A OE1 
3300  O OE2 . GLU D 242  ? 1.0812 1.5503 0.9060 0.5250  0.0195  0.0547  239  GLU A OE2 
3301  N N   . VAL D 243  ? 0.8944 1.1670 0.8042 0.3447  0.0104  0.0489  240  VAL A N   
3302  C CA  . VAL D 243  ? 0.8631 1.0815 0.7756 0.3189  0.0061  0.0457  240  VAL A CA  
3303  C C   . VAL D 243  ? 0.8293 1.0752 0.7762 0.2820  0.0104  0.0535  240  VAL A C   
3304  O O   . VAL D 243  ? 0.8422 1.0573 0.7954 0.2611  0.0078  0.0533  240  VAL A O   
3305  C CB  . VAL D 243  ? 0.8074 0.9632 0.7018 0.3156  0.0009  0.0353  240  VAL A CB  
3306  C CG1 . VAL D 243  ? 0.8428 0.9675 0.6986 0.3525  -0.0046 0.0273  240  VAL A CG1 
3307  C CG2 . VAL D 243  ? 0.7549 0.9285 0.6678 0.2971  0.0053  0.0355  240  VAL A CG2 
3308  N N   . PHE D 244  ? 0.7963 1.0985 0.7636 0.2734  0.0162  0.0606  241  PHE A N   
3309  C CA  . PHE D 244  ? 0.7601 1.0918 0.7558 0.2406  0.0192  0.0692  241  PHE A CA  
3310  C C   . PHE D 244  ? 0.7761 1.1708 0.7840 0.2441  0.0222  0.0804  241  PHE A C   
3311  O O   . PHE D 244  ? 0.7873 1.2249 0.8158 0.2224  0.0252  0.0895  241  PHE A O   
3312  C CB  . PHE D 244  ? 0.7055 1.0489 0.7138 0.2219  0.0221  0.0699  241  PHE A CB  
3313  C CG  . PHE D 244  ? 0.6991 0.9844 0.7012 0.2101  0.0193  0.0606  241  PHE A CG  
3314  C CD1 . PHE D 244  ? 0.6780 0.9359 0.6909 0.1824  0.0176  0.0605  241  PHE A CD1 
3315  C CD2 . PHE D 244  ? 0.7248 0.9844 0.7092 0.2271  0.0179  0.0521  241  PHE A CD2 
3316  C CE1 . PHE D 244  ? 0.6647 0.8749 0.6724 0.1719  0.0151  0.0527  241  PHE A CE1 
3317  C CE2 . PHE D 244  ? 0.7222 0.9315 0.7012 0.2151  0.0149  0.0443  241  PHE A CE2 
3318  C CZ  . PHE D 244  ? 0.6869 0.8737 0.6783 0.1873  0.0137  0.0449  241  PHE A CZ  
3319  N N   . SER D 245  ? 0.8033 1.2032 0.7965 0.2713  0.0209  0.0802  242  SER A N   
3320  C CA  . SER D 245  ? 0.8004 1.2564 0.8037 0.2757  0.0230  0.0906  242  SER A CA  
3321  C C   . SER D 245  ? 0.7945 1.2183 0.7912 0.2772  0.0192  0.0890  242  SER A C   
3322  O O   . SER D 245  ? 0.7995 1.1624 0.7764 0.2866  0.0147  0.0798  242  SER A O   
3323  C CB  . SER D 245  ? 0.8780 1.3827 0.8694 0.3116  0.0255  0.0931  242  SER A CB  
3324  O OG  . SER D 245  ? 0.9660 1.4284 0.9266 0.3459  0.0216  0.0835  242  SER A OG  
3325  N N   . PHE D 246  ? 0.7351 1.2004 0.7475 0.2668  0.0205  0.0988  243  PHE A N   
3326  C CA  . PHE D 246  ? 0.6920 1.1303 0.7014 0.2643  0.0172  0.0984  243  PHE A CA  
3327  C C   . PHE D 246  ? 0.7094 1.1170 0.6902 0.2998  0.0137  0.0919  243  PHE A C   
3328  O O   . PHE D 246  ? 0.7024 1.0536 0.6723 0.2960  0.0092  0.0864  243  PHE A O   
3329  C CB  . PHE D 246  ? 0.6378 1.1330 0.6678 0.2497  0.0191  0.1107  243  PHE A CB  
3330  C CG  . PHE D 246  ? 0.5813 1.0828 0.6337 0.2096  0.0195  0.1159  243  PHE A CG  
3331  C CD1 . PHE D 246  ? 0.5632 1.0169 0.6167 0.1904  0.0183  0.1091  243  PHE A CD1 
3332  C CD2 . PHE D 246  ? 0.5619 1.1160 0.6320 0.1916  0.0203  0.1277  243  PHE A CD2 
3333  C CE1 . PHE D 246  ? 0.5441 1.0004 0.6141 0.1564  0.0180  0.1134  243  PHE A CE1 
3334  C CE2 . PHE D 246  ? 0.5517 1.1055 0.6374 0.1555  0.0192  0.1322  243  PHE A CE2 
3335  C CZ  . PHE D 246  ? 0.5400 1.0437 0.6247 0.1391  0.0181  0.1248  243  PHE A CZ  
3336  N N   . PRO D 247  ? 0.7383 1.1780 0.7039 0.3346  0.0150  0.0925  244  PRO A N   
3337  C CA  . PRO D 247  ? 0.7708 1.1747 0.7043 0.3695  0.0104  0.0860  244  PRO A CA  
3338  C C   . PRO D 247  ? 0.7802 1.1011 0.6878 0.3735  0.0042  0.0739  244  PRO A C   
3339  O O   . PRO D 247  ? 0.8252 1.1006 0.7070 0.3907  -0.0016 0.0691  244  PRO A O   
3340  C CB  . PRO D 247  ? 0.7801 1.2371 0.7017 0.4062  0.0133  0.0883  244  PRO A CB  
3341  C CG  . PRO D 247  ? 0.7402 1.2767 0.6942 0.3867  0.0197  0.1005  244  PRO A CG  
3342  C CD  . PRO D 247  ? 0.7227 1.2373 0.6986 0.3447  0.0203  0.1003  244  PRO A CD  
3343  N N   . PHE D 248  ? 0.7481 1.0472 0.6603 0.3574  0.0046  0.0692  245  PHE A N   
3344  C CA  . PHE D 248  ? 0.7770 0.9999 0.6640 0.3598  -0.0019 0.0584  245  PHE A CA  
3345  C C   . PHE D 248  ? 0.7559 0.9297 0.6474 0.3324  -0.0060 0.0573  245  PHE A C   
3346  O O   . PHE D 248  ? 0.7816 0.8912 0.6481 0.3360  -0.0130 0.0499  245  PHE A O   
3347  C CB  . PHE D 248  ? 0.7962 1.0143 0.6871 0.3514  -0.0002 0.0540  245  PHE A CB  
3348  C CG  . PHE D 248  ? 0.8536 0.9982 0.7156 0.3569  -0.0074 0.0431  245  PHE A CG  
3349  C CD1 . PHE D 248  ? 0.9005 1.0151 0.7240 0.3932  -0.0130 0.0362  245  PHE A CD1 
3350  C CD2 . PHE D 248  ? 0.8327 0.9383 0.7040 0.3260  -0.0093 0.0400  245  PHE A CD2 
3351  C CE1 . PHE D 248  ? 0.9271 0.9712 0.7210 0.3961  -0.0211 0.0267  245  PHE A CE1 
3352  C CE2 . PHE D 248  ? 0.8566 0.8975 0.7012 0.3287  -0.0167 0.0310  245  PHE A CE2 
3353  C CZ  . PHE D 248  ? 0.9065 0.9151 0.7120 0.3625  -0.0229 0.0245  245  PHE A CZ  
3354  N N   . TYR D 249  ? 0.7204 0.9232 0.6416 0.3051  -0.0024 0.0648  246  TYR A N   
3355  C CA  . TYR D 249  ? 0.7111 0.8725 0.6374 0.2801  -0.0058 0.0643  246  TYR A CA  
3356  C C   . TYR D 249  ? 0.7387 0.8640 0.6409 0.2966  -0.0118 0.0628  246  TYR A C   
3357  O O   . TYR D 249  ? 0.7552 0.8319 0.6513 0.2813  -0.0166 0.0604  246  TYR A O   
3358  C CB  . TYR D 249  ? 0.6551 0.8566 0.6150 0.2507  -0.0011 0.0726  246  TYR A CB  
3359  C CG  . TYR D 249  ? 0.5504 0.7147 0.5169 0.2252  -0.0040 0.0724  246  TYR A CG  
3360  C CD1 . TYR D 249  ? 0.5497 0.6699 0.5138 0.2081  -0.0064 0.0668  246  TYR A CD1 
3361  C CD2 . TYR D 249  ? 0.5421 0.7185 0.5171 0.2187  -0.0041 0.0782  246  TYR A CD2 
3362  C CE1 . TYR D 249  ? 0.5411 0.6326 0.5112 0.1859  -0.0088 0.0672  246  TYR A CE1 
3363  C CE2 . TYR D 249  ? 0.5337 0.6788 0.5143 0.1967  -0.0066 0.0782  246  TYR A CE2 
3364  C CZ  . TYR D 249  ? 0.6117 0.7157 0.5898 0.1807  -0.0088 0.0729  246  TYR A CZ  
3365  O OH  . TYR D 249  ? 0.6090 0.6871 0.5926 0.1599  -0.0110 0.0736  246  TYR A OH  
3366  N N   . ASN D 250  ? 0.7592 0.9084 0.6466 0.3280  -0.0118 0.0645  247  ASN A N   
3367  C CA  . ASN D 250  ? 0.8294 0.9392 0.6882 0.3474  -0.0183 0.0624  247  ASN A CA  
3368  C C   . ASN D 250  ? 0.9327 0.9680 0.7550 0.3575  -0.0270 0.0530  247  ASN A C   
3369  O O   . ASN D 250  ? 0.9953 0.9796 0.7954 0.3590  -0.0342 0.0511  247  ASN A O   
3370  C CB  . ASN D 250  ? 0.8532 1.0064 0.7010 0.3829  -0.0165 0.0658  247  ASN A CB  
3371  C CG  . ASN D 250  ? 0.8485 1.0692 0.7283 0.3712  -0.0101 0.0763  247  ASN A CG  
3372  O OD1 . ASN D 250  ? 0.8390 1.0555 0.7382 0.3435  -0.0098 0.0802  247  ASN A OD1 
3373  N ND2 . ASN D 250  ? 0.8598 1.1447 0.7445 0.3923  -0.0054 0.0813  247  ASN A ND2 
3374  N N   . GLN D 251  ? 0.9796 1.0068 0.7941 0.3632  -0.0270 0.0473  248  GLN A N   
3375  C CA  . GLN D 251  ? 1.0319 0.9884 0.8123 0.3686  -0.0358 0.0385  248  GLN A CA  
3376  C C   . GLN D 251  ? 0.9733 0.9014 0.7695 0.3317  -0.0366 0.0369  248  GLN A C   
3377  O O   . GLN D 251  ? 0.9906 0.8747 0.7664 0.3317  -0.0421 0.0301  248  GLN A O   
3378  C CB  . GLN D 251  ? 1.1107 1.0715 0.8682 0.4000  -0.0363 0.0326  248  GLN A CB  
3379  C CG  . GLN D 251  ? 1.2387 1.1845 0.9559 0.4430  -0.0417 0.0297  248  GLN A CG  
3380  C CD  . GLN D 251  ? 1.3617 1.2241 1.0381 0.4466  -0.0542 0.0246  248  GLN A CD  
3381  O OE1 . GLN D 251  ? 1.4082 1.2121 1.0605 0.4413  -0.0619 0.0179  248  GLN A OE1 
3382  N NE2 . GLN D 251  ? 1.3970 1.2533 1.0646 0.4544  -0.0568 0.0284  248  GLN A NE2 
3383  N N   . LEU D 252  ? 0.9227 0.8757 0.7532 0.3013  -0.0317 0.0430  249  LEU A N   
3384  C CA  . LEU D 252  ? 0.8829 0.8131 0.7289 0.2673  -0.0323 0.0423  249  LEU A CA  
3385  C C   . LEU D 252  ? 0.8551 0.7681 0.7082 0.2472  -0.0346 0.0467  249  LEU A C   
3386  O O   . LEU D 252  ? 0.8076 0.7320 0.6869 0.2186  -0.0313 0.0499  249  LEU A O   
3387  C CB  . LEU D 252  ? 0.8155 0.7944 0.6963 0.2491  -0.0236 0.0449  249  LEU A CB  
3388  C CG  . LEU D 252  ? 0.7966 0.7934 0.6735 0.2639  -0.0208 0.0409  249  LEU A CG  
3389  C CD1 . LEU D 252  ? 0.7511 0.7919 0.6619 0.2416  -0.0131 0.0446  249  LEU A CD1 
3390  C CD2 . LEU D 252  ? 0.8015 0.7408 0.6497 0.2690  -0.0282 0.0324  249  LEU A CD2 
3391  N N   . LEU D 253  ? 0.8594 0.7443 0.6873 0.2632  -0.0407 0.0471  250  LEU A N   
3392  C CA  . LEU D 253  ? 0.8173 0.6876 0.6497 0.2472  -0.0431 0.0519  250  LEU A CA  
3393  C C   . LEU D 253  ? 0.8788 0.6804 0.6816 0.2395  -0.0537 0.0492  250  LEU A C   
3394  O O   . LEU D 253  ? 0.8975 0.6837 0.7026 0.2240  -0.0564 0.0535  250  LEU A O   
3395  C CB  . LEU D 253  ? 0.7792 0.6747 0.6081 0.2683  -0.0418 0.0562  250  LEU A CB  
3396  C CG  . LEU D 253  ? 0.7480 0.7148 0.6029 0.2770  -0.0325 0.0602  250  LEU A CG  
3397  C CD1 . LEU D 253  ? 0.7548 0.7472 0.6059 0.2966  -0.0318 0.0651  250  LEU A CD1 
3398  C CD2 . LEU D 253  ? 0.7260 0.7290 0.6201 0.2450  -0.0256 0.0645  250  LEU A CD2 
3399  N N   . THR D 254  ? 0.9199 0.6800 0.6937 0.2490  -0.0604 0.0426  251  THR A N   
3400  C CA  . THR D 254  ? 1.0038 0.6970 0.7469 0.2386  -0.0718 0.0407  251  THR A CA  
3401  C C   . THR D 254  ? 1.0379 0.7192 0.7896 0.2152  -0.0724 0.0378  251  THR A C   
3402  O O   . THR D 254  ? 1.0688 0.7821 0.8385 0.2168  -0.0657 0.0350  251  THR A O   
3403  C CB  . THR D 254  ? 1.0531 0.6965 0.7458 0.2698  -0.0821 0.0354  251  THR A CB  
3404  O OG1 . THR D 254  ? 1.0509 0.7045 0.7352 0.2911  -0.0802 0.0290  251  THR A OG1 
3405  C CG2 . THR D 254  ? 1.0493 0.7037 0.7316 0.2941  -0.0820 0.0385  251  THR A CG2 
3406  N N   . GLN D 255  ? 1.0518 0.6881 0.7899 0.1930  -0.0808 0.0392  252  GLN A N   
3407  C CA  . GLN D 255  ? 1.0571 0.6870 0.8063 0.1675  -0.0813 0.0380  252  GLN A CA  
3408  C C   . GLN D 255  ? 1.1308 0.7401 0.8590 0.1813  -0.0847 0.0302  252  GLN A C   
3409  O O   . GLN D 255  ? 1.1028 0.7353 0.8518 0.1709  -0.0792 0.0280  252  GLN A O   
3410  C CB  . GLN D 255  ? 1.0615 0.6489 0.7968 0.1418  -0.0907 0.0422  252  GLN A CB  
3411  C CG  . GLN D 255  ? 1.0573 0.6430 0.8052 0.1139  -0.0913 0.0422  252  GLN A CG  
3412  C CD  . GLN D 255  ? 1.0451 0.6892 0.8396 0.0988  -0.0788 0.0447  252  GLN A CD  
3413  O OE1 . GLN D 255  ? 1.0337 0.7134 0.8511 0.1001  -0.0715 0.0487  252  GLN A OE1 
3414  N NE2 . GLN D 255  ? 1.0469 0.6992 0.8533 0.0846  -0.0768 0.0423  252  GLN A NE2 
3415  N N   . THR D 256  ? 1.1824 0.7463 0.8670 0.2057  -0.0943 0.0257  253  THR A N   
3416  C CA  . THR D 256  ? 1.1995 0.7406 0.8599 0.2214  -0.0984 0.0178  253  THR A CA  
3417  C C   . THR D 256  ? 1.1471 0.7465 0.8339 0.2384  -0.0862 0.0151  253  THR A C   
3418  O O   . THR D 256  ? 1.1672 0.7712 0.8577 0.2367  -0.0846 0.0105  253  THR A O   
3419  C CB  . THR D 256  ? 1.2545 0.7358 0.8596 0.2489  -0.1112 0.0134  253  THR A CB  
3420  O OG1 . THR D 256  ? 1.2533 0.7574 0.8559 0.2768  -0.1072 0.0149  253  THR A OG1 
3421  C CG2 . THR D 256  ? 1.2920 0.7090 0.8664 0.2280  -0.1253 0.0165  253  THR A CG2 
3422  N N   . GLN D 257  ? 1.0921 0.7381 0.7974 0.2536  -0.0779 0.0185  254  GLN A N   
3423  C CA  . GLN D 257  ? 1.0520 0.7590 0.7845 0.2658  -0.0664 0.0181  254  GLN A CA  
3424  C C   . GLN D 257  ? 1.0165 0.7659 0.7940 0.2354  -0.0572 0.0219  254  GLN A C   
3425  O O   . GLN D 257  ? 0.9830 0.7634 0.7768 0.2361  -0.0508 0.0198  254  GLN A O   
3426  C CB  . GLN D 257  ? 1.0521 0.7973 0.7885 0.2902  -0.0615 0.0217  254  GLN A CB  
3427  C CG  . GLN D 257  ? 1.1572 0.8657 0.8471 0.3265  -0.0699 0.0174  254  GLN A CG  
3428  C CD  . GLN D 257  ? 1.2165 0.9106 0.8807 0.3504  -0.0727 0.0095  254  GLN A CD  
3429  O OE1 . GLN D 257  ? 1.2725 0.9026 0.8962 0.3567  -0.0842 0.0035  254  GLN A OE1 
3430  N NE2 . GLN D 257  ? 1.1911 0.9445 0.8773 0.3634  -0.0628 0.0098  254  GLN A NE2 
3431  N N   . ILE D 258  ? 0.9872 0.7374 0.7828 0.2097  -0.0566 0.0274  255  ILE A N   
3432  C CA  . ILE D 258  ? 0.9033 0.6874 0.7365 0.1821  -0.0491 0.0305  255  ILE A CA  
3433  C C   . ILE D 258  ? 0.9448 0.7046 0.7738 0.1672  -0.0523 0.0261  255  ILE A C   
3434  O O   . ILE D 258  ? 0.9272 0.7172 0.7798 0.1571  -0.0456 0.0254  255  ILE A O   
3435  C CB  . ILE D 258  ? 0.7931 0.5813 0.6426 0.1609  -0.0486 0.0371  255  ILE A CB  
3436  C CG1 . ILE D 258  ? 0.7459 0.5695 0.6066 0.1737  -0.0436 0.0419  255  ILE A CG1 
3437  C CG2 . ILE D 258  ? 0.7349 0.5463 0.6153 0.1330  -0.0431 0.0393  255  ILE A CG2 
3438  C CD1 . ILE D 258  ? 0.6604 0.4876 0.5350 0.1554  -0.0433 0.0482  255  ILE A CD1 
3439  N N   . ASP D 259  ? 1.0180 0.7221 0.8150 0.1652  -0.0632 0.0233  256  ASP A N   
3440  C CA  . ASP D 259  ? 1.0455 0.7258 0.8357 0.1512  -0.0673 0.0193  256  ASP A CA  
3441  C C   . ASP D 259  ? 1.0348 0.7248 0.8191 0.1705  -0.0647 0.0127  256  ASP A C   
3442  O O   . ASP D 259  ? 1.0145 0.7205 0.8155 0.1587  -0.0606 0.0108  256  ASP A O   
3443  C CB  . ASP D 259  ? 1.1395 0.7562 0.8925 0.1444  -0.0812 0.0186  256  ASP A CB  
3444  C CG  . ASP D 259  ? 1.2184 0.8284 0.9808 0.1176  -0.0838 0.0259  256  ASP A CG  
3445  O OD1 . ASP D 259  ? 1.2001 0.8492 0.9978 0.0987  -0.0756 0.0298  256  ASP A OD1 
3446  O OD2 . ASP D 259  ? 1.2986 0.8635 1.0311 0.1160  -0.0944 0.0279  256  ASP A OD2 
3447  N N   . LEU D 260  ? 1.0403 0.7221 0.8002 0.2016  -0.0669 0.0093  257  LEU A N   
3448  C CA  . LEU D 260  ? 1.0030 0.6986 0.7569 0.2227  -0.0640 0.0034  257  LEU A CA  
3449  C C   . LEU D 260  ? 0.8971 0.6593 0.6916 0.2190  -0.0508 0.0065  257  LEU A C   
3450  O O   . LEU D 260  ? 0.8649 0.6426 0.6672 0.2193  -0.0471 0.0032  257  LEU A O   
3451  C CB  . LEU D 260  ? 1.0279 0.7061 0.7468 0.2595  -0.0687 -0.0002 257  LEU A CB  
3452  C CG  . LEU D 260  ? 1.0922 0.6956 0.7606 0.2682  -0.0837 -0.0052 257  LEU A CG  
3453  C CD1 . LEU D 260  ? 1.1399 0.7299 0.7732 0.3082  -0.0877 -0.0085 257  LEU A CD1 
3454  C CD2 . LEU D 260  ? 1.1023 0.6745 0.7555 0.2609  -0.0893 -0.0115 257  LEU A CD2 
3455  N N   . TYR D 261  ? 0.8382 0.6388 0.6572 0.2147  -0.0442 0.0131  258  TYR A N   
3456  C CA  . TYR D 261  ? 0.7839 0.6442 0.6391 0.2072  -0.0332 0.0172  258  TYR A CA  
3457  C C   . TYR D 261  ? 0.7958 0.6600 0.6734 0.1779  -0.0305 0.0175  258  TYR A C   
3458  O O   . TYR D 261  ? 0.7945 0.6883 0.6886 0.1748  -0.0245 0.0169  258  TYR A O   
3459  C CB  . TYR D 261  ? 0.7340 0.6288 0.6071 0.2066  -0.0286 0.0245  258  TYR A CB  
3460  C CG  . TYR D 261  ? 0.6941 0.6492 0.6000 0.1993  -0.0188 0.0297  258  TYR A CG  
3461  C CD1 . TYR D 261  ? 0.7091 0.7047 0.6166 0.2202  -0.0142 0.0309  258  TYR A CD1 
3462  C CD2 . TYR D 261  ? 0.6635 0.6348 0.5963 0.1715  -0.0150 0.0338  258  TYR A CD2 
3463  C CE1 . TYR D 261  ? 0.6799 0.7300 0.6154 0.2106  -0.0064 0.0369  258  TYR A CE1 
3464  C CE2 . TYR D 261  ? 0.6101 0.6308 0.5683 0.1635  -0.0077 0.0389  258  TYR A CE2 
3465  C CZ  . TYR D 261  ? 0.6240 0.6836 0.5836 0.1816  -0.0037 0.0408  258  TYR A CZ  
3466  O OH  . TYR D 261  ? 0.6035 0.7116 0.5864 0.1707  0.0024  0.0470  258  TYR A OH  
3467  N N   . ASN D 262  ? 0.7869 0.6227 0.6644 0.1567  -0.0350 0.0189  259  ASN A N   
3468  C CA  . ASN D 262  ? 0.7541 0.5944 0.6506 0.1310  -0.0328 0.0193  259  ASN A CA  
3469  C C   . ASN D 262  ? 0.7706 0.5892 0.6542 0.1314  -0.0360 0.0129  259  ASN A C   
3470  O O   . ASN D 262  ? 0.7433 0.5797 0.6447 0.1182  -0.0316 0.0123  259  ASN A O   
3471  C CB  . ASN D 262  ? 0.7479 0.5669 0.6459 0.1099  -0.0371 0.0230  259  ASN A CB  
3472  C CG  . ASN D 262  ? 0.7309 0.5790 0.6495 0.1036  -0.0322 0.0296  259  ASN A CG  
3473  O OD1 . ASN D 262  ? 0.7357 0.6234 0.6725 0.1086  -0.0250 0.0318  259  ASN A OD1 
3474  N ND2 . ASN D 262  ? 0.7267 0.5558 0.6420 0.0914  -0.0365 0.0332  259  ASN A ND2 
3475  N N   . GLN D 263  ? 0.8173 0.5955 0.6679 0.1467  -0.0443 0.0080  260  GLN A N   
3476  C CA  . GLN D 263  ? 0.8256 0.5807 0.6612 0.1476  -0.0483 0.0017  260  GLN A CA  
3477  C C   . GLN D 263  ? 0.8138 0.5995 0.6548 0.1663  -0.0418 -0.0017 260  GLN A C   
3478  O O   . GLN D 263  ? 0.7965 0.5798 0.6377 0.1624  -0.0415 -0.0058 260  GLN A O   
3479  C CB  . GLN D 263  ? 0.8525 0.5483 0.6466 0.1563  -0.0610 -0.0024 260  GLN A CB  
3480  C CG  . GLN D 263  ? 0.8789 0.5417 0.6660 0.1322  -0.0688 0.0015  260  GLN A CG  
3481  C CD  . GLN D 263  ? 0.9942 0.5939 0.7376 0.1350  -0.0831 -0.0022 260  GLN A CD  
3482  O OE1 . GLN D 263  ? 1.0544 0.6215 0.7703 0.1471  -0.0905 -0.0018 260  GLN A OE1 
3483  N NE2 . GLN D 263  ? 1.0296 0.6098 0.7645 0.1235  -0.0879 -0.0058 260  GLN A NE2 
3484  N N   . LEU D 264  ? 0.8080 0.6251 0.6533 0.1863  -0.0367 0.0005  261  LEU A N   
3485  C CA  . LEU D 264  ? 0.7922 0.6509 0.6494 0.1995  -0.0291 -0.0002 261  LEU A CA  
3486  C C   . LEU D 264  ? 0.7517 0.6472 0.6431 0.1765  -0.0211 0.0035  261  LEU A C   
3487  O O   . LEU D 264  ? 0.7319 0.6469 0.6304 0.1784  -0.0170 0.0016  261  LEU A O   
3488  C CB  . LEU D 264  ? 0.8040 0.6958 0.6610 0.2229  -0.0252 0.0033  261  LEU A CB  
3489  C CG  . LEU D 264  ? 0.7778 0.7228 0.6494 0.2356  -0.0169 0.0052  261  LEU A CG  
3490  C CD1 . LEU D 264  ? 0.7962 0.7258 0.6445 0.2564  -0.0196 -0.0022 261  LEU A CD1 
3491  C CD2 . LEU D 264  ? 0.7665 0.7522 0.6434 0.2525  -0.0129 0.0112  261  LEU A CD2 
3492  N N   . LEU D 265  ? 0.7609 0.6643 0.6713 0.1555  -0.0193 0.0088  262  LEU A N   
3493  C CA  . LEU D 265  ? 0.7134 0.6456 0.6517 0.1344  -0.0130 0.0121  262  LEU A CA  
3494  C C   . LEU D 265  ? 0.7024 0.6095 0.6399 0.1169  -0.0159 0.0084  262  LEU A C   
3495  O O   . LEU D 265  ? 0.6744 0.5997 0.6263 0.1074  -0.0115 0.0080  262  LEU A O   
3496  C CB  . LEU D 265  ? 0.7026 0.6531 0.6589 0.1211  -0.0104 0.0190  262  LEU A CB  
3497  C CG  . LEU D 265  ? 0.6915 0.6851 0.6612 0.1283  -0.0049 0.0251  262  LEU A CG  
3498  C CD1 . LEU D 265  ? 0.7333 0.7296 0.6857 0.1553  -0.0064 0.0244  262  LEU A CD1 
3499  C CD2 . LEU D 265  ? 0.6764 0.6777 0.6604 0.1126  -0.0041 0.0309  262  LEU A CD2 
3500  N N   . GLY D 266  ? 0.6871 0.5533 0.6069 0.1121  -0.0237 0.0062  263  GLY A N   
3501  C CA  . GLY D 266  ? 0.7007 0.5481 0.6214 0.0926  -0.0269 0.0044  263  GLY A CA  
3502  C C   . GLY D 266  ? 0.7500 0.5659 0.6483 0.0980  -0.0331 -0.0021 263  GLY A C   
3503  O O   . GLY D 266  ? 0.7420 0.5512 0.6436 0.0831  -0.0344 -0.0038 263  GLY A O   
3504  N N   . GLY D 267  ? 0.7905 0.5867 0.6643 0.1200  -0.0374 -0.0060 264  GLY A N   
3505  C CA  . GLY D 267  ? 0.8512 0.6132 0.6993 0.1269  -0.0444 -0.0127 264  GLY A CA  
3506  C C   . GLY D 267  ? 0.9110 0.6221 0.7331 0.1166  -0.0563 -0.0134 264  GLY A C   
3507  O O   . GLY D 267  ? 0.9451 0.6481 0.7692 0.1044  -0.0590 -0.0083 264  GLY A O   
3508  N N   . LYS D 327  ? 1.7072 1.0924 1.1996 -0.4513 -0.2941 0.1632  324  LYS A N   
3509  C CA  . LYS D 327  ? 1.7159 1.0935 1.1975 -0.4586 -0.2988 0.1720  324  LYS A CA  
3510  C C   . LYS D 327  ? 1.7057 1.1400 1.2000 -0.4907 -0.3017 0.1897  324  LYS A C   
3511  O O   . LYS D 327  ? 1.7014 1.1455 1.1982 -0.4963 -0.3019 0.1975  324  LYS A O   
3512  C CB  . LYS D 327  ? 1.7789 1.0740 1.2023 -0.4543 -0.3171 0.1686  324  LYS A CB  
3513  C CG  . LYS D 327  ? 1.7836 1.0224 1.1913 -0.4177 -0.3141 0.1518  324  LYS A CG  
3514  C CD  . LYS D 327  ? 1.7458 1.0029 1.1849 -0.3964 -0.2987 0.1484  324  LYS A CD  
3515  C CE  . LYS D 327  ? 1.7582 0.9637 1.1814 -0.3585 -0.2955 0.1326  324  LYS A CE  
3516  N NZ  . LYS D 327  ? 1.7044 0.9285 1.1573 -0.3381 -0.2808 0.1305  324  LYS A NZ  
3517  N N   . SER D 328  ? 1.7211 1.1945 1.2229 -0.5111 -0.3038 0.1964  325  SER A N   
3518  C CA  . SER D 328  ? 1.7478 1.2769 1.2584 -0.5407 -0.3073 0.2139  325  SER A CA  
3519  C C   . SER D 328  ? 1.7045 1.3058 1.2515 -0.5486 -0.2971 0.2174  325  SER A C   
3520  O O   . SER D 328  ? 1.6733 1.2769 1.2360 -0.5333 -0.2887 0.2062  325  SER A O   
3521  C CB  . SER D 328  ? 1.8407 1.3266 1.2996 -0.5657 -0.3299 0.2236  325  SER A CB  
3522  O OG  . SER D 328  ? 1.8720 1.3379 1.3089 -0.5740 -0.3388 0.2216  325  SER A OG  
3523  N N   . ASP D 329  ? 1.7126 1.3745 1.2715 -0.5722 -0.2981 0.2332  326  ASP A N   
3524  C CA  . ASP D 329  ? 1.6805 1.4188 1.2736 -0.5791 -0.2881 0.2382  326  ASP A CA  
3525  C C   . ASP D 329  ? 1.7192 1.4441 1.2892 -0.5938 -0.2987 0.2394  326  ASP A C   
3526  O O   . ASP D 329  ? 1.6890 1.4405 1.2808 -0.5855 -0.2898 0.2326  326  ASP A O   
3527  C CB  . ASP D 329  ? 1.6798 1.4883 1.2905 -0.5969 -0.2859 0.2551  326  ASP A CB  
3528  C CG  . ASP D 329  ? 1.6225 1.5180 1.2770 -0.5936 -0.2705 0.2580  326  ASP A CG  
3529  O OD1 . ASP D 329  ? 1.6359 1.5635 1.2865 -0.6101 -0.2748 0.2655  326  ASP A OD1 
3530  O OD2 . ASP D 329  ? 1.5686 1.5001 1.2597 -0.5738 -0.2542 0.2529  326  ASP A OD2 
3531  N N   . GLU D 330  ? 1.7901 1.4732 1.3146 -0.6161 -0.3183 0.2481  327  GLU A N   
3532  C CA  . GLU D 330  ? 1.8279 1.4936 1.3254 -0.6322 -0.3302 0.2506  327  GLU A CA  
3533  C C   . GLU D 330  ? 1.8622 1.4553 1.3369 -0.6131 -0.3340 0.2336  327  GLU A C   
3534  O O   . GLU D 330  ? 1.8696 1.4523 1.3292 -0.6210 -0.3404 0.2327  327  GLU A O   
3535  C CB  . GLU D 330  ? 1.8804 1.5249 1.3338 -0.6640 -0.3511 0.2669  327  GLU A CB  
3536  N N   . GLU D 331  ? 1.8659 1.4098 1.3369 -0.5875 -0.3303 0.2204  328  GLU A N   
3537  C CA  . GLU D 331  ? 1.8699 1.3468 1.3182 -0.5661 -0.3335 0.2040  328  GLU A CA  
3538  C C   . GLU D 331  ? 1.8085 1.3201 1.2916 -0.5520 -0.3193 0.1938  328  GLU A C   
3539  O O   . GLU D 331  ? 1.8137 1.2884 1.2768 -0.5462 -0.3249 0.1852  328  GLU A O   
3540  C CB  . GLU D 331  ? 1.8562 1.2808 1.2952 -0.5397 -0.3311 0.1929  328  GLU A CB  
3541  C CG  . GLU D 331  ? 1.8800 1.2315 1.2889 -0.5151 -0.3360 0.1763  328  GLU A CG  
3542  C CD  . GLU D 331  ? 1.8930 1.2014 1.2961 -0.4861 -0.3316 0.1655  328  GLU A CD  
3543  O OE1 . GLU D 331  ? 1.8644 1.2019 1.2913 -0.4850 -0.3233 0.1703  328  GLU A OE1 
3544  O OE2 . GLU D 331  ? 1.9354 1.1823 1.3096 -0.4632 -0.3362 0.1523  328  GLU A OE2 
3545  N N   . VAL D 332  ? 1.7903 1.3726 1.3241 -0.5458 -0.3014 0.1945  329  VAL A N   
3546  C CA  . VAL D 332  ? 1.7263 1.3448 1.2933 -0.5331 -0.2884 0.1852  329  VAL A CA  
3547  C C   . VAL D 332  ? 1.7275 1.3860 1.2944 -0.5557 -0.2929 0.1942  329  VAL A C   
3548  O O   . VAL D 332  ? 1.7337 1.3992 1.3103 -0.5484 -0.2887 0.1857  329  VAL A O   
3549  C CB  . VAL D 332  ? 1.6674 1.3471 1.2856 -0.5184 -0.2685 0.1832  329  VAL A CB  
3550  C CG1 . VAL D 332  ? 1.6710 1.3144 1.2869 -0.5006 -0.2653 0.1780  329  VAL A CG1 
3551  C CG2 . VAL D 332  ? 1.6429 1.4040 1.2866 -0.5379 -0.2638 0.1993  329  VAL A CG2 
3552  N N   . ILE D 333  ? 1.7283 1.4139 1.2834 -0.5832 -0.3018 0.2117  330  ILE A N   
3553  C CA  . ILE D 333  ? 1.6439 1.3699 1.1972 -0.6055 -0.3064 0.2219  330  ILE A CA  
3554  C C   . ILE D 333  ? 1.6489 1.3070 1.1524 -0.6172 -0.3250 0.2211  330  ILE A C   
3555  O O   . ILE D 333  ? 1.6354 1.3019 1.1381 -0.6213 -0.3260 0.2188  330  ILE A O   
3556  C CB  . ILE D 333  ? 1.5413 1.3298 1.1023 -0.6299 -0.3079 0.2419  330  ILE A CB  
3557  C CG1 . ILE D 333  ? 1.4087 1.2594 1.0158 -0.6153 -0.2899 0.2420  330  ILE A CG1 
3558  C CG2 . ILE D 333  ? 1.5064 1.3457 1.0693 -0.6508 -0.3105 0.2528  330  ILE A CG2 
3559  C CD1 . ILE D 333  ? 1.3643 1.2787 0.9794 -0.6356 -0.2906 0.2610  330  ILE A CD1 
3560  N N   . GLN D 334  ? 1.6863 1.2759 1.1464 -0.6219 -0.3402 0.2228  331  GLN A N   
3561  C CA  . GLN D 334  ? 1.7701 1.2910 1.1778 -0.6322 -0.3593 0.2224  331  GLN A CA  
3562  C C   . GLN D 334  ? 1.7970 1.2680 1.1983 -0.6051 -0.3566 0.2027  331  GLN A C   
3563  O O   . GLN D 334  ? 1.8350 1.2800 1.2122 -0.6113 -0.3656 0.2008  331  GLN A O   
3564  C CB  . GLN D 334  ? 1.8258 1.2857 1.1869 -0.6418 -0.3765 0.2287  331  GLN A CB  
3565  N N   . SER D 335  ? 1.7778 1.2356 1.1996 -0.5748 -0.3443 0.1882  332  SER A N   
3566  C CA  . SER D 335  ? 1.7730 1.1841 1.1876 -0.5470 -0.3416 0.1694  332  SER A CA  
3567  C C   . SER D 335  ? 1.7116 1.1741 1.1633 -0.5424 -0.3291 0.1634  332  SER A C   
3568  O O   . SER D 335  ? 1.7117 1.1431 1.1466 -0.5355 -0.3336 0.1544  332  SER A O   
3569  C CB  . SER D 335  ? 1.7564 1.1394 1.1799 -0.5164 -0.3326 0.1569  332  SER A CB  
3570  O OG  . SER D 335  ? 1.7737 1.1124 1.1881 -0.4881 -0.3302 0.1390  332  SER A OG  
3571  N N   . PHE D 336  ? 1.6388 1.1802 1.1399 -0.5449 -0.3135 0.1680  333  PHE A N   
3572  C CA  . PHE D 336  ? 1.5568 1.1509 1.0933 -0.5401 -0.3016 0.1626  333  PHE A CA  
3573  C C   . PHE D 336  ? 1.5923 1.2042 1.1139 -0.5650 -0.3111 0.1723  333  PHE A C   
3574  O O   . PHE D 336  ? 1.5973 1.2010 1.1173 -0.5590 -0.3112 0.1635  333  PHE A O   
3575  C CB  . PHE D 336  ? 1.4359 1.1110 1.0248 -0.5365 -0.2838 0.1665  333  PHE A CB  
3576  C CG  . PHE D 336  ? 1.3600 1.0912 0.9858 -0.5287 -0.2712 0.1601  333  PHE A CG  
3577  C CD1 . PHE D 336  ? 1.3378 1.0390 0.9661 -0.5066 -0.2671 0.1426  333  PHE A CD1 
3578  C CD2 . PHE D 336  ? 1.3208 1.1358 0.9772 -0.5418 -0.2634 0.1716  333  PHE A CD2 
3579  C CE1 . PHE D 336  ? 1.2936 1.0459 0.9544 -0.4996 -0.2563 0.1366  333  PHE A CE1 
3580  C CE2 . PHE D 336  ? 1.2710 1.1381 0.9597 -0.5328 -0.2521 0.1654  333  PHE A CE2 
3581  C CZ  . PHE D 336  ? 1.2571 1.0924 0.9482 -0.5125 -0.2489 0.1479  333  PHE A CZ  
3582  N N   . CYS D 337  ? 1.6460 1.2819 1.1553 -0.5933 -0.3197 0.1908  334  CYS A N   
3583  C CA  . CYS D 337  ? 1.6840 1.3363 1.1760 -0.6193 -0.3298 0.2021  334  CYS A CA  
3584  C C   . CYS D 337  ? 1.7659 1.3362 1.2079 -0.6205 -0.3465 0.1960  334  CYS A C   
3585  O O   . CYS D 337  ? 1.7807 1.3570 1.2136 -0.6319 -0.3515 0.1980  334  CYS A O   
3586  C CB  . CYS D 337  ? 1.7169 1.4046 1.1998 -0.6494 -0.3373 0.2239  334  CYS A CB  
3587  S SG  . CYS D 337  ? 1.7755 1.4948 1.2391 -0.6842 -0.3487 0.2410  334  CYS A SG  
3588  N N   . LYS D 338  ? 1.8254 1.3192 1.2334 -0.6075 -0.3553 0.1887  335  LYS A N   
3589  C CA  . LYS D 338  ? 1.8993 1.3128 1.2588 -0.6022 -0.3704 0.1807  335  LYS A CA  
3590  C C   . LYS D 338  ? 1.8680 1.2723 1.2436 -0.5751 -0.3608 0.1617  335  LYS A C   
3591  O O   . LYS D 338  ? 1.8960 1.2743 1.2493 -0.5780 -0.3688 0.1582  335  LYS A O   
3592  C CB  . LYS D 338  ? 1.9446 1.2819 1.2629 -0.5920 -0.3817 0.1775  335  LYS A CB  
3593  N N   . TYR D 339  ? 1.7989 1.2238 1.2120 -0.5488 -0.3440 0.1494  336  TYR A N   
3594  C CA  . TYR D 339  ? 1.7466 1.1732 1.1795 -0.5244 -0.3338 0.1322  336  TYR A CA  
3595  C C   . TYR D 339  ? 1.6386 1.1392 1.1072 -0.5373 -0.3253 0.1363  336  TYR A C   
3596  O O   . TYR D 339  ? 1.6336 1.1288 1.1036 -0.5278 -0.3239 0.1258  336  TYR A O   
3597  C CB  . TYR D 339  ? 1.7381 1.1670 1.1993 -0.4946 -0.3191 0.1194  336  TYR A CB  
3598  C CG  . TYR D 339  ? 1.7157 1.1669 1.2078 -0.4726 -0.3057 0.1039  336  TYR A CG  
3599  C CD1 . TYR D 339  ? 1.7542 1.1504 1.2224 -0.4504 -0.3095 0.0884  336  TYR A CD1 
3600  C CD2 . TYR D 339  ? 1.6470 1.1748 1.1905 -0.4728 -0.2897 0.1049  336  TYR A CD2 
3601  C CE1 . TYR D 339  ? 1.7140 1.1303 1.2086 -0.4306 -0.2979 0.0743  336  TYR A CE1 
3602  C CE2 . TYR D 339  ? 1.6050 1.1521 1.1743 -0.4535 -0.2788 0.0910  336  TYR A CE2 
3603  C CZ  . TYR D 339  ? 1.6412 1.1320 1.1859 -0.4332 -0.2830 0.0757  336  TYR A CZ  
3604  O OH  . TYR D 339  ? 1.6025 1.1139 1.1717 -0.4126 -0.2718 0.0620  336  TYR A OH  
3605  N N   . LYS D 340  ? 1.5494 1.1207 1.0461 -0.5574 -0.3195 0.1512  337  LYS A N   
3606  C CA  . LYS D 340  ? 1.4745 1.1214 1.0039 -0.5684 -0.3113 0.1563  337  LYS A CA  
3607  C C   . LYS D 340  ? 1.5351 1.1681 1.0338 -0.5905 -0.3251 0.1638  337  LYS A C   
3608  O O   . LYS D 340  ? 1.5246 1.1786 1.0350 -0.5875 -0.3215 0.1577  337  LYS A O   
3609  C CB  . LYS D 340  ? 1.4086 1.1335 0.9710 -0.5818 -0.3022 0.1712  337  LYS A CB  
3610  C CG  . LYS D 340  ? 1.3446 1.1551 0.9418 -0.5899 -0.2923 0.1773  337  LYS A CG  
3611  C CD  . LYS D 340  ? 1.2812 1.1664 0.9144 -0.5917 -0.2801 0.1877  337  LYS A CD  
3612  C CE  . LYS D 340  ? 1.2629 1.2305 0.9157 -0.6075 -0.2755 0.2007  337  LYS A CE  
3613  N NZ  . LYS D 340  ? 1.2149 1.2583 0.9027 -0.6043 -0.2624 0.2095  337  LYS A NZ  
3614  N N   . THR D 341  ? 1.5942 1.1904 1.0515 -0.6133 -0.3416 0.1771  338  THR A N   
3615  C CA  . THR D 341  ? 1.6230 1.1997 1.0461 -0.6361 -0.3565 0.1853  338  THR A CA  
3616  C C   . THR D 341  ? 1.6541 1.1572 1.0460 -0.6191 -0.3644 0.1693  338  THR A C   
3617  O O   . THR D 341  ? 1.6772 1.1708 1.0490 -0.6326 -0.3734 0.1723  338  THR A O   
3618  C CB  . THR D 341  ? 1.6603 1.2122 1.0430 -0.6652 -0.3736 0.2039  338  THR A CB  
3619  O OG1 . THR D 341  ? 1.7153 1.2716 1.0737 -0.6927 -0.3857 0.2160  338  THR A OG1 
3620  C CG2 . THR D 341  ? 1.6951 1.1527 1.0313 -0.6540 -0.3870 0.1970  338  THR A CG2 
3621  N N   . LEU D 342  ? 1.6809 1.1334 1.0678 -0.5889 -0.3612 0.1528  339  LEU A N   
3622  C CA  . LEU D 342  ? 1.7285 1.1165 1.0885 -0.5673 -0.3666 0.1363  339  LEU A CA  
3623  C C   . LEU D 342  ? 1.6916 1.1206 1.0873 -0.5532 -0.3536 0.1241  339  LEU A C   
3624  O O   . LEU D 342  ? 1.6980 1.0911 1.0725 -0.5455 -0.3597 0.1150  339  LEU A O   
3625  C CB  . LEU D 342  ? 1.7633 1.0896 1.1065 -0.5375 -0.3664 0.1232  339  LEU A CB  
3626  C CG  . LEU D 342  ? 1.8235 1.0761 1.1323 -0.5101 -0.3727 0.1061  339  LEU A CG  
3627  C CD1 . LEU D 342  ? 1.8896 1.0676 1.1537 -0.4975 -0.3840 0.1043  339  LEU A CD1 
3628  C CD2 . LEU D 342  ? 1.7783 1.0509 1.1235 -0.4784 -0.3557 0.0877  339  LEU A CD2 
3629  N N   . LEU D 343  ? 1.6499 1.1535 1.0979 -0.5492 -0.3364 0.1238  340  LEU A N   
3630  C CA  . LEU D 343  ? 1.6248 1.1718 1.1069 -0.5364 -0.3244 0.1128  340  LEU A CA  
3631  C C   . LEU D 343  ? 1.6397 1.2255 1.1224 -0.5598 -0.3287 0.1223  340  LEU A C   
3632  O O   . LEU D 343  ? 1.6320 1.2299 1.1260 -0.5496 -0.3245 0.1118  340  LEU A O   
3633  C CB  . LEU D 343  ? 1.5640 1.1798 1.0989 -0.5256 -0.3058 0.1110  340  LEU A CB  
3634  C CG  . LEU D 343  ? 1.5366 1.1216 1.0767 -0.5013 -0.2993 0.1011  340  LEU A CG  
3635  C CD1 . LEU D 343  ? 1.4442 1.1023 1.0346 -0.4965 -0.2825 0.1033  340  LEU A CD1 
3636  C CD2 . LEU D 343  ? 1.5385 1.0676 1.0650 -0.4711 -0.2986 0.0806  340  LEU A CD2 
3637  N N   . ARG D 344  ? 1.6672 1.2737 1.1372 -0.5909 -0.3371 0.1421  341  ARG A N   
3638  C CA  . ARG D 344  ? 1.6974 1.3375 1.1636 -0.6143 -0.3424 0.1523  341  ARG A CA  
3639  C C   . ARG D 344  ? 1.7731 1.3387 1.1910 -0.6175 -0.3589 0.1477  341  ARG A C   
3640  O O   . ARG D 344  ? 1.7742 1.3525 1.1949 -0.6186 -0.3590 0.1433  341  ARG A O   
3641  C CB  . ARG D 344  ? 1.7271 1.4123 1.1916 -0.6468 -0.3468 0.1759  341  ARG A CB  
3642  C CG  . ARG D 344  ? 1.6743 1.4509 1.1885 -0.6463 -0.3299 0.1830  341  ARG A CG  
3643  C CD  . ARG D 344  ? 1.6806 1.4459 1.2029 -0.6349 -0.3251 0.1819  341  ARG A CD  
3644  N NE  . ARG D 344  ? 1.6691 1.5062 1.2152 -0.6495 -0.3183 0.1987  341  ARG A NE  
3645  C CZ  . ARG D 344  ? 1.7155 1.5488 1.2365 -0.6754 -0.3294 0.2168  341  ARG A CZ  
3646  N NH1 . ARG D 344  ? 1.7919 1.5515 1.2623 -0.6903 -0.3483 0.2207  341  ARG A NH1 
3647  N NH2 . ARG D 344  ? 1.6854 1.5885 1.2297 -0.6858 -0.3221 0.2311  341  ARG A NH2 
3648  N N   . ASN D 345  ? 1.8318 1.3193 1.2038 -0.6179 -0.3732 0.1485  342  ASN A N   
3649  C CA  . ASN D 345  ? 1.8930 1.3061 1.2135 -0.6205 -0.3904 0.1454  342  ASN A CA  
3650  C C   . ASN D 345  ? 1.8910 1.2724 1.2136 -0.5881 -0.3853 0.1230  342  ASN A C   
3651  O O   . ASN D 345  ? 1.9185 1.2777 1.2207 -0.5908 -0.3930 0.1196  342  ASN A O   
3652  C CB  . ASN D 345  ? 1.9362 1.2734 1.2061 -0.6243 -0.4065 0.1506  342  ASN A CB  
3653  C CG  . ASN D 345  ? 1.9362 1.3024 1.2009 -0.6568 -0.4126 0.1729  342  ASN A CG  
3654  O OD1 . ASN D 345  ? 1.9185 1.3475 1.2005 -0.6832 -0.4110 0.1876  342  ASN A OD1 
3655  N ND2 . ASN D 345  ? 1.9576 1.2798 1.1976 -0.6542 -0.4197 0.1757  342  ASN A ND2 
3656  N N   . GLU D 346  ? 1.8425 1.2216 1.1885 -0.5572 -0.3726 0.1080  343  GLU A N   
3657  C CA  . GLU D 346  ? 1.8124 1.1697 1.1636 -0.5254 -0.3662 0.0871  343  GLU A CA  
3658  C C   . GLU D 346  ? 1.7575 1.1861 1.1518 -0.5260 -0.3538 0.0831  343  GLU A C   
3659  O O   . GLU D 346  ? 1.7349 1.1482 1.1292 -0.5053 -0.3510 0.0676  343  GLU A O   
3660  C CB  . GLU D 346  ? 1.7552 1.0910 1.1175 -0.4930 -0.3564 0.0734  343  GLU A CB  
3661  C CG  . GLU D 346  ? 1.7928 1.0488 1.1081 -0.4827 -0.3685 0.0726  343  GLU A CG  
3662  C CD  . GLU D 346  ? 1.7562 0.9982 1.0852 -0.4509 -0.3576 0.0602  343  GLU A CD  
3663  O OE1 . GLU D 346  ? 1.6937 0.9940 1.0703 -0.4460 -0.3416 0.0580  343  GLU A OE1 
3664  O OE2 . GLU D 346  ? 1.7963 0.9698 1.0874 -0.4301 -0.3651 0.0531  343  GLU A OE2 
3665  N N   . ASN D 347  ? 1.7408 1.2478 1.1701 -0.5478 -0.3465 0.0968  344  ASN A N   
3666  C CA  . ASN D 347  ? 1.6969 1.2793 1.1677 -0.5483 -0.3345 0.0947  344  ASN A CA  
3667  C C   . ASN D 347  ? 1.6430 1.2360 1.1436 -0.5148 -0.3202 0.0751  344  ASN A C   
3668  O O   . ASN D 347  ? 1.6178 1.2245 1.1291 -0.5030 -0.3160 0.0640  344  ASN A O   
3669  C CB  . ASN D 347  ? 1.7334 1.3094 1.1844 -0.5620 -0.3440 0.0964  344  ASN A CB  
3670  N N   . VAL D 348  ? 1.6318 1.2180 1.1446 -0.4998 -0.3129 0.0713  345  VAL A N   
3671  C CA  . VAL D 348  ? 1.5959 1.1882 1.1337 -0.4689 -0.3000 0.0537  345  VAL A CA  
3672  C C   . VAL D 348  ? 1.5262 1.2075 1.1130 -0.4696 -0.2859 0.0546  345  VAL A C   
3673  O O   . VAL D 348  ? 1.4681 1.1636 1.0748 -0.4431 -0.2743 0.0408  345  VAL A O   
3674  C CB  . VAL D 348  ? 1.5981 1.1585 1.1342 -0.4536 -0.2965 0.0505  345  VAL A CB  
3675  C CG1 . VAL D 348  ? 1.6687 1.1394 1.1538 -0.4463 -0.3102 0.0473  345  VAL A CG1 
3676  C CG2 . VAL D 348  ? 1.5871 1.1979 1.1463 -0.4729 -0.2921 0.0671  345  VAL A CG2 
3677  N N   . LEU D 349  ? 1.5240 1.2698 1.1316 -0.4929 -0.2832 0.0718  346  LEU A N   
3678  C CA  . LEU D 349  ? 1.4606 1.2942 1.1118 -0.4915 -0.2703 0.0735  346  LEU A CA  
3679  C C   . LEU D 349  ? 1.4355 1.2832 1.0846 -0.4918 -0.2724 0.0681  346  LEU A C   
3680  O O   . LEU D 349  ? 1.3854 1.2690 1.0609 -0.4699 -0.2601 0.0578  346  LEU A O   
3681  C CB  . LEU D 349  ? 1.4769 1.3768 1.1472 -0.5137 -0.2668 0.0938  346  LEU A CB  
3682  C CG  . LEU D 349  ? 1.5643 1.4453 1.2061 -0.5426 -0.2789 0.1121  346  LEU A CG  
3683  C CD1 . LEU D 349  ? 1.6203 1.4638 1.2259 -0.5600 -0.2935 0.1156  346  LEU A CD1 
3684  C CD2 . LEU D 349  ? 1.5470 1.5128 1.2169 -0.5579 -0.2711 0.1298  346  LEU A CD2 
3685  N N   . GLU D 350  ? 1.4803 1.2993 1.0982 -0.5118 -0.2854 0.0756  347  GLU A N   
3686  C CA  . GLU D 350  ? 1.4583 1.2878 1.0721 -0.5133 -0.2882 0.0710  347  GLU A CA  
3687  C C   . GLU D 350  ? 1.4349 1.2125 1.0365 -0.4857 -0.2883 0.0494  347  GLU A C   
3688  O O   . GLU D 350  ? 1.3715 1.1779 0.9872 -0.4753 -0.2834 0.0406  347  GLU A O   
3689  C CB  . GLU D 350  ? 1.5110 1.3126 1.0894 -0.5415 -0.3036 0.0841  347  GLU A CB  
3690  N N   . THR D 351  ? 1.4824 1.1845 1.0565 -0.4718 -0.2936 0.0408  348  THR A N   
3691  C CA  . THR D 351  ? 1.4836 1.1372 1.0450 -0.4419 -0.2925 0.0203  348  THR A CA  
3692  C C   . THR D 351  ? 1.4085 1.1135 1.0171 -0.4041 -0.2660 0.0130  348  THR A C   
3693  O O   . THR D 351  ? 1.3965 1.1067 1.0151 -0.3770 -0.2558 0.0012  348  THR A O   
3694  C CB  . THR D 351  ? 1.5153 1.0815 1.0374 -0.4298 -0.3011 0.0150  348  THR A CB  
3695  O OG1 . THR D 351  ? 1.5730 1.1022 1.0592 -0.4532 -0.3163 0.0276  348  THR A OG1 
3696  C CG2 . THR D 351  ? 1.5104 1.0261 1.0141 -0.3967 -0.2999 -0.0045 348  THR A CG2 
3697  N N   . ALA D 352  ? 1.3638 1.1061 1.0001 -0.4021 -0.2551 0.0204  349  ALA A N   
3698  C CA  . ALA D 352  ? 1.2923 1.0819 0.9709 -0.3683 -0.2312 0.0146  349  ALA A CA  
3699  C C   . ALA D 352  ? 1.2687 1.1337 0.9788 -0.3681 -0.2211 0.0173  349  ALA A C   
3700  O O   . ALA D 352  ? 1.2231 1.1075 0.9538 -0.3380 -0.2059 0.0073  349  ALA A O   
3701  C CB  . ALA D 352  ? 1.2767 1.0837 0.9732 -0.3676 -0.2238 0.0220  349  ALA A CB  
3702  N N   . GLU D 353  ? 1.2952 1.2046 1.0083 -0.4013 -0.2296 0.0312  350  GLU A N   
3703  C CA  . GLU D 353  ? 1.2640 1.2473 1.0042 -0.4009 -0.2211 0.0343  350  GLU A CA  
3704  C C   . GLU D 353  ? 1.2639 1.2297 0.9919 -0.3920 -0.2238 0.0238  350  GLU A C   
3705  O O   . GLU D 353  ? 1.2249 1.2391 0.9773 -0.3747 -0.2112 0.0199  350  GLU A O   
3706  C CB  . GLU D 353  ? 1.2726 1.3073 1.0148 -0.4405 -0.2317 0.0526  350  GLU A CB  
3707  C CG  . GLU D 353  ? 1.2654 1.3338 1.0254 -0.4478 -0.2266 0.0642  350  GLU A CG  
3708  C CD  . GLU D 353  ? 1.3038 1.4109 1.0577 -0.4907 -0.2403 0.0836  350  GLU A CD  
3709  O OE1 . GLU D 353  ? 1.3099 1.4556 1.0657 -0.5012 -0.2413 0.0900  350  GLU A OE1 
3710  O OE2 . GLU D 353  ? 1.3208 1.4160 1.0690 -0.5022 -0.2424 0.0939  350  GLU A OE2 
3711  N N   . ALA D 354  ? 1.3088 1.2040 0.9975 -0.4023 -0.2404 0.0187  351  ALA A N   
3712  C CA  . ALA D 354  ? 1.3040 1.1772 0.9781 -0.3927 -0.2437 0.0079  351  ALA A CA  
3713  C C   . ALA D 354  ? 1.2608 1.1102 0.9439 -0.3490 -0.2282 -0.0084 351  ALA A C   
3714  O O   . ALA D 354  ? 1.2550 1.1186 0.9454 -0.3326 -0.2217 -0.0166 351  ALA A O   
3715  C CB  . ALA D 354  ? 1.3834 1.1863 1.0080 -0.4187 -0.2682 0.0082  351  ALA A CB  
3716  N N   . LEU D 355  ? 1.2343 1.0495 0.9165 -0.3306 -0.2224 -0.0127 352  LEU A N   
3717  C CA  . LEU D 355  ? 1.1523 0.9493 0.8435 -0.2906 -0.2078 -0.0267 352  LEU A CA  
3718  C C   . LEU D 355  ? 1.0594 0.9233 0.7933 -0.2696 -0.1869 -0.0276 352  LEU A C   
3719  O O   . LEU D 355  ? 1.0515 0.9210 0.7934 -0.2460 -0.1777 -0.0373 352  LEU A O   
3720  C CB  . LEU D 355  ? 1.1142 0.8644 0.7949 -0.2776 -0.2070 -0.0295 352  LEU A CB  
3721  C CG  . LEU D 355  ? 1.1579 0.8259 0.7918 -0.2785 -0.2236 -0.0360 352  LEU A CG  
3722  C CD1 . LEU D 355  ? 1.1644 0.7959 0.7931 -0.2594 -0.2194 -0.0393 352  LEU A CD1 
3723  C CD2 . LEU D 355  ? 1.1579 0.8016 0.7770 -0.2593 -0.2241 -0.0487 352  LEU A CD2 
3724  N N   . PHE D 356  ? 1.0119 0.9255 0.7714 -0.2772 -0.1797 -0.0176 353  PHE A N   
3725  C CA  . PHE D 356  ? 0.9804 0.9540 0.7759 -0.2568 -0.1612 -0.0183 353  PHE A CA  
3726  C C   . PHE D 356  ? 1.0069 1.0264 0.8106 -0.2620 -0.1607 -0.0171 353  PHE A C   
3727  O O   . PHE D 356  ? 0.9840 1.0385 0.8096 -0.2389 -0.1464 -0.0218 353  PHE A O   
3728  C CB  . PHE D 356  ? 0.9505 0.9640 0.7674 -0.2630 -0.1549 -0.0078 353  PHE A CB  
3729  C CG  . PHE D 356  ? 0.9703 0.9481 0.7864 -0.2502 -0.1506 -0.0103 353  PHE A CG  
3730  C CD1 . PHE D 356  ? 0.9506 0.9305 0.7844 -0.2185 -0.1347 -0.0183 353  PHE A CD1 
3731  C CD2 . PHE D 356  ? 1.0085 0.9504 0.8048 -0.2705 -0.1631 -0.0042 353  PHE A CD2 
3732  C CE1 . PHE D 356  ? 0.9522 0.9025 0.7857 -0.2073 -0.1309 -0.0201 353  PHE A CE1 
3733  C CE2 . PHE D 356  ? 1.0031 0.9136 0.7984 -0.2578 -0.1590 -0.0064 353  PHE A CE2 
3734  C CZ  . PHE D 356  ? 0.9772 0.8937 0.7920 -0.2260 -0.1428 -0.0144 353  PHE A CZ  
3735  N N   . ASN D 357  ? 1.0631 1.0825 0.8484 -0.2921 -0.1767 -0.0106 354  ASN A N   
3736  C CA  . ASN D 357  ? 1.0753 1.1339 0.8652 -0.2969 -0.1775 -0.0103 354  ASN A CA  
3737  C C   . ASN D 357  ? 1.1032 1.1226 0.8784 -0.2786 -0.1777 -0.0240 354  ASN A C   
3738  O O   . ASN D 357  ? 1.0746 1.1284 0.8606 -0.2696 -0.1721 -0.0271 354  ASN A O   
3739  C CB  . ASN D 357  ? 1.1331 1.2073 0.9075 -0.3379 -0.1955 0.0024  354  ASN A CB  
3740  C CG  . ASN D 357  ? 1.1510 1.2788 0.9341 -0.3443 -0.1957 0.0049  354  ASN A CG  
3741  O OD1 . ASN D 357  ? 1.1892 1.2917 0.9513 -0.3531 -0.2063 0.0005  354  ASN A OD1 
3742  N ND2 . ASN D 357  ? 1.1199 1.3220 0.9326 -0.3386 -0.1841 0.0118  354  ASN A ND2 
3743  N N   . GLU D 358  ? 1.1507 1.1004 0.9006 -0.2714 -0.1841 -0.0323 355  GLU A N   
3744  C CA  . GLU D 358  ? 1.1590 1.0726 0.8955 -0.2498 -0.1828 -0.0457 355  GLU A CA  
3745  C C   . GLU D 358  ? 1.0611 1.0010 0.8253 -0.2145 -0.1623 -0.0534 355  GLU A C   
3746  O O   . GLU D 358  ? 1.0140 0.9524 0.7770 -0.1984 -0.1583 -0.0619 355  GLU A O   
3747  C CB  . GLU D 358  ? 1.2321 1.0677 0.9347 -0.2459 -0.1932 -0.0525 355  GLU A CB  
3748  C CG  . GLU D 358  ? 1.3135 1.1038 0.9759 -0.2741 -0.2161 -0.0506 355  GLU A CG  
3749  C CD  . GLU D 358  ? 1.3843 1.0940 1.0095 -0.2639 -0.2259 -0.0590 355  GLU A CD  
3750  O OE1 . GLU D 358  ? 1.4395 1.1128 1.0417 -0.2836 -0.2391 -0.0530 355  GLU A OE1 
3751  O OE2 . GLU D 358  ? 1.3844 1.0680 1.0026 -0.2352 -0.2204 -0.0714 355  GLU A OE2 
3752  N N   . LEU D 359  ? 1.0374 1.0004 0.8251 -0.2030 -0.1498 -0.0503 356  LEU A N   
3753  C CA  . LEU D 359  ? 0.9907 0.9715 0.8008 -0.1711 -0.1317 -0.0570 356  LEU A CA  
3754  C C   . LEU D 359  ? 0.9963 1.0303 0.8248 -0.1638 -0.1233 -0.0569 356  LEU A C   
3755  O O   . LEU D 359  ? 0.9926 1.0371 0.8351 -0.1379 -0.1098 -0.0630 356  LEU A O   
3756  C CB  . LEU D 359  ? 0.9032 0.8968 0.7318 -0.1641 -0.1222 -0.0524 356  LEU A CB  
3757  C CG  . LEU D 359  ? 0.8564 0.8007 0.6688 -0.1688 -0.1289 -0.0521 356  LEU A CG  
3758  C CD1 . LEU D 359  ? 0.8136 0.7790 0.6464 -0.1646 -0.1197 -0.0462 356  LEU A CD1 
3759  C CD2 . LEU D 359  ? 0.8492 0.7430 0.6457 -0.1469 -0.1280 -0.0635 356  LEU A CD2 
3760  N N   . ASN D 360  ? 1.0468 1.1147 0.8743 -0.1860 -0.1313 -0.0498 357  ASN A N   
3761  C CA  . ASN D 360  ? 1.0379 1.1581 0.8809 -0.1781 -0.1240 -0.0496 357  ASN A CA  
3762  C C   . ASN D 360  ? 1.0606 1.1621 0.8908 -0.1696 -0.1265 -0.0589 357  ASN A C   
3763  O O   . ASN D 360  ? 1.0649 1.2016 0.9075 -0.1555 -0.1180 -0.0613 357  ASN A O   
3764  C CB  . ASN D 360  ? 1.0707 1.2429 0.9190 -0.2047 -0.1311 -0.0372 357  ASN A CB  
3765  C CG  . ASN D 360  ? 1.1170 1.3094 0.9762 -0.2155 -0.1301 -0.0270 357  ASN A CG  
3766  O OD1 . ASN D 360  ? 1.1051 1.3337 0.9853 -0.1991 -0.1173 -0.0250 357  ASN A OD1 
3767  N ND2 . ASN D 360  ? 1.1682 1.3351 1.0109 -0.2432 -0.1442 -0.0203 357  ASN A ND2 
3768  N N   . SER D 361  ? 1.0769 1.1227 0.8807 -0.1766 -0.1382 -0.0642 358  SER A N   
3769  C CA  . SER D 361  ? 1.0664 1.0925 0.8549 -0.1701 -0.1422 -0.0729 358  SER A CA  
3770  C C   . SER D 361  ? 1.0868 1.0522 0.8570 -0.1511 -0.1425 -0.0841 358  SER A C   
3771  O O   . SER D 361  ? 1.0665 1.0229 0.8310 -0.1355 -0.1400 -0.0925 358  SER A O   
3772  C CB  . SER D 361  ? 1.0878 1.1114 0.8554 -0.2017 -0.1605 -0.0678 358  SER A CB  
3773  O OG  . SER D 361  ? 1.1221 1.1021 0.8667 -0.2235 -0.1750 -0.0638 358  SER A OG  
3774  N N   . ILE D 362  ? 1.1162 1.0421 0.8764 -0.1507 -0.1454 -0.0842 359  ILE A N   
3775  C CA  . ILE D 362  ? 1.1413 1.0115 0.8814 -0.1315 -0.1465 -0.0943 359  ILE A CA  
3776  C C   . ILE D 362  ? 1.1330 1.0170 0.8946 -0.0998 -0.1282 -0.0999 359  ILE A C   
3777  O O   . ILE D 362  ? 1.1214 1.0504 0.9107 -0.0940 -0.1158 -0.0957 359  ILE A O   
3778  C CB  . ILE D 362  ? 1.1013 0.9237 0.8204 -0.1414 -0.1569 -0.0923 359  ILE A CB  
3779  C CG1 . ILE D 362  ? 1.0018 0.8454 0.7449 -0.1370 -0.1461 -0.0863 359  ILE A CG1 
3780  C CG2 . ILE D 362  ? 1.1300 0.9366 0.8250 -0.1761 -0.1765 -0.0855 359  ILE A CG2 
3781  C CD1 . ILE D 362  ? 0.9789 0.7768 0.7027 -0.1438 -0.1548 -0.0845 359  ILE A CD1 
3782  N N   . ASP D 363  ? 1.1319 0.9770 0.8787 -0.0791 -0.1271 -0.1091 360  ASP A N   
3783  C CA  . ASP D 363  ? 1.0873 0.9433 0.8513 -0.0505 -0.1111 -0.1138 360  ASP A CA  
3784  C C   . ASP D 363  ? 1.0476 0.9063 0.8261 -0.0460 -0.1036 -0.1093 360  ASP A C   
3785  O O   . ASP D 363  ? 1.0549 0.8765 0.8175 -0.0464 -0.1098 -0.1100 360  ASP A O   
3786  C CB  . ASP D 363  ? 1.1439 0.9607 0.8859 -0.0308 -0.1133 -0.1239 360  ASP A CB  
3787  C CG  . ASP D 363  ? 1.1531 0.9838 0.9117 -0.0032 -0.0975 -0.1277 360  ASP A CG  
3788  O OD1 . ASP D 363  ? 1.1449 1.0163 0.9300 0.0004  -0.0856 -0.1238 360  ASP A OD1 
3789  O OD2 . ASP D 363  ? 1.1724 0.9732 0.9156 0.0151  -0.0976 -0.1342 360  ASP A OD2 
3790  N N   . LEU D 364  ? 1.0064 0.9073 0.8129 -0.0407 -0.0908 -0.1049 361  LEU A N   
3791  C CA  . LEU D 364  ? 0.9640 0.8720 0.7856 -0.0379 -0.0837 -0.1000 361  LEU A CA  
3792  C C   . LEU D 364  ? 0.9510 0.8469 0.7771 -0.0136 -0.0735 -0.1045 361  LEU A C   
3793  O O   . LEU D 364  ? 0.9200 0.8195 0.7575 -0.0103 -0.0677 -0.1008 361  LEU A O   
3794  C CB  . LEU D 364  ? 0.8927 0.8497 0.7387 -0.0434 -0.0759 -0.0930 361  LEU A CB  
3795  C CG  . LEU D 364  ? 0.8776 0.8564 0.7230 -0.0687 -0.0850 -0.0857 361  LEU A CG  
3796  C CD1 . LEU D 364  ? 0.8298 0.8585 0.6984 -0.0688 -0.0761 -0.0791 361  LEU A CD1 
3797  C CD2 . LEU D 364  ? 0.9016 0.8504 0.7320 -0.0875 -0.0969 -0.0816 361  LEU A CD2 
3798  N N   . THR D 365  ? 0.9533 0.8375 0.7708 0.0029  -0.0713 -0.1118 362  THR A N   
3799  C CA  . THR D 365  ? 0.9136 0.7890 0.7338 0.0248  -0.0626 -0.1151 362  THR A CA  
3800  C C   . THR D 365  ? 0.9369 0.7725 0.7379 0.0292  -0.0694 -0.1174 362  THR A C   
3801  O O   . THR D 365  ? 0.9568 0.7878 0.7600 0.0470  -0.0626 -0.1190 362  THR A O   
3802  C CB  . THR D 365  ? 0.8838 0.7630 0.7006 0.0414  -0.0580 -0.1215 362  THR A CB  
3803  O OG1 . THR D 365  ? 0.9232 0.7699 0.7136 0.0417  -0.0692 -0.1279 362  THR A OG1 
3804  C CG2 . THR D 365  ? 0.8510 0.7659 0.6825 0.0377  -0.0527 -0.1197 362  THR A CG2 
3805  N N   . HIS D 366  ? 0.9701 0.7773 0.7509 0.0133  -0.0831 -0.1171 363  HIS A N   
3806  C CA  . HIS D 366  ? 1.0171 0.7816 0.7750 0.0172  -0.0913 -0.1192 363  HIS A CA  
3807  C C   . HIS D 366  ? 1.0102 0.7682 0.7690 -0.0021 -0.0971 -0.1119 363  HIS A C   
3808  O O   . HIS D 366  ? 1.0578 0.7765 0.7940 -0.0024 -0.1062 -0.1129 363  HIS A O   
3809  C CB  . HIS D 366  ? 1.0946 0.8176 0.8176 0.0181  -0.1049 -0.1264 363  HIS A CB  
3810  C CG  . HIS D 366  ? 1.1377 0.8607 0.8554 0.0414  -0.0996 -0.1342 363  HIS A CG  
3811  N ND1 . HIS D 366  ? 1.1763 0.8831 0.8842 0.0666  -0.0957 -0.1390 363  HIS A ND1 
3812  C CD2 . HIS D 366  ? 1.1428 0.8826 0.8635 0.0438  -0.0975 -0.1377 363  HIS A CD2 
3813  C CE1 . HIS D 366  ? 1.1754 0.8897 0.8807 0.0830  -0.0914 -0.1447 363  HIS A CE1 
3814  N NE2 . HIS D 366  ? 1.1559 0.8885 0.8687 0.0694  -0.0925 -0.1443 363  HIS A NE2 
3815  N N   . ILE D 367  ? 0.9556 0.7508 0.7381 -0.0172 -0.0924 -0.1045 364  ILE A N   
3816  C CA  . ILE D 367  ? 0.9279 0.7254 0.7162 -0.0337 -0.0954 -0.0967 364  ILE A CA  
3817  C C   . ILE D 367  ? 0.8539 0.6752 0.6670 -0.0205 -0.0814 -0.0939 364  ILE A C   
3818  O O   . ILE D 367  ? 0.8385 0.6976 0.6744 -0.0165 -0.0708 -0.0919 364  ILE A O   
3819  C CB  . ILE D 367  ? 0.9079 0.7339 0.7046 -0.0587 -0.1000 -0.0896 364  ILE A CB  
3820  C CG1 . ILE D 367  ? 0.9478 0.7516 0.7191 -0.0735 -0.1146 -0.0920 364  ILE A CG1 
3821  C CG2 . ILE D 367  ? 0.8671 0.6973 0.6693 -0.0756 -0.1031 -0.0809 364  ILE A CG2 
3822  C CD1 . ILE D 367  ? 0.9858 0.7340 0.7235 -0.0814 -0.1298 -0.0934 364  ILE A CD1 
3823  N N   . PHE D 368  ? 0.8280 0.6258 0.6345 -0.0135 -0.0819 -0.0936 365  PHE A N   
3824  C CA  . PHE D 368  ? 0.7814 0.5968 0.6076 0.0008  -0.0695 -0.0918 365  PHE A CA  
3825  C C   . PHE D 368  ? 0.7757 0.6017 0.6140 -0.0125 -0.0690 -0.0839 365  PHE A C   
3826  O O   . PHE D 368  ? 0.7804 0.5839 0.6045 -0.0271 -0.0795 -0.0809 365  PHE A O   
3827  C CB  . PHE D 368  ? 0.7989 0.5869 0.6108 0.0217  -0.0690 -0.0970 365  PHE A CB  
3828  C CG  . PHE D 368  ? 0.8497 0.6341 0.6528 0.0388  -0.0669 -0.1044 365  PHE A CG  
3829  C CD1 . PHE D 368  ? 0.8880 0.6393 0.6629 0.0391  -0.0782 -0.1104 365  PHE A CD1 
3830  C CD2 . PHE D 368  ? 0.8412 0.6545 0.6626 0.0538  -0.0542 -0.1049 365  PHE A CD2 
3831  C CE1 . PHE D 368  ? 0.9120 0.6610 0.6784 0.0558  -0.0762 -0.1173 365  PHE A CE1 
3832  C CE2 . PHE D 368  ? 0.8598 0.6722 0.6735 0.0691  -0.0521 -0.1109 365  PHE A CE2 
3833  C CZ  . PHE D 368  ? 0.9059 0.6872 0.6928 0.0710  -0.0627 -0.1174 365  PHE A CZ  
3834  N N   . ILE D 369  ? 0.7554 0.6140 0.6182 -0.0075 -0.0574 -0.0802 366  ILE A N   
3835  C CA  . ILE D 369  ? 0.7489 0.6205 0.6250 -0.0162 -0.0550 -0.0731 366  ILE A CA  
3836  C C   . ILE D 369  ? 0.7669 0.6283 0.6457 -0.0015 -0.0494 -0.0735 366  ILE A C   
3837  O O   . ILE D 369  ? 0.7722 0.6401 0.6561 0.0154  -0.0416 -0.0767 366  ILE A O   
3838  C CB  . ILE D 369  ? 0.7125 0.6256 0.6104 -0.0198 -0.0469 -0.0689 366  ILE A CB  
3839  C CG1 . ILE D 369  ? 0.7004 0.6289 0.5958 -0.0343 -0.0527 -0.0677 366  ILE A CG1 
3840  C CG2 . ILE D 369  ? 0.6975 0.6236 0.6081 -0.0257 -0.0438 -0.0621 366  ILE A CG2 
3841  C CD1 . ILE D 369  ? 0.6966 0.6136 0.5808 -0.0561 -0.0645 -0.0627 366  ILE A CD1 
3842  N N   . SER D 370  ? 0.7855 0.6327 0.6607 -0.0084 -0.0536 -0.0695 367  SER A N   
3843  C CA  . SER D 370  ? 0.7829 0.6218 0.6600 0.0049  -0.0490 -0.0692 367  SER A CA  
3844  C C   . SER D 370  ? 0.7836 0.6555 0.6851 0.0097  -0.0372 -0.0654 367  SER A C   
3845  O O   . SER D 370  ? 0.7687 0.6635 0.6835 -0.0009 -0.0348 -0.0609 367  SER A O   
3846  C CB  . SER D 370  ? 0.7970 0.6115 0.6627 -0.0045 -0.0572 -0.0656 367  SER A CB  
3847  O OG  . SER D 370  ? 0.8084 0.6180 0.6768 0.0088  -0.0525 -0.0650 367  SER A OG  
3848  N N   . HIS D 371  ? 0.7975 0.6719 0.7027 0.0261  -0.0304 -0.0670 368  HIS A N   
3849  C CA  . HIS D 371  ? 0.7706 0.6716 0.6952 0.0296  -0.0205 -0.0630 368  HIS A CA  
3850  C C   . HIS D 371  ? 0.7526 0.6566 0.6851 0.0214  -0.0204 -0.0571 368  HIS A C   
3851  O O   . HIS D 371  ? 0.7378 0.6631 0.6847 0.0185  -0.0146 -0.0531 368  HIS A O   
3852  C CB  . HIS D 371  ? 0.8146 0.7192 0.7399 0.0467  -0.0143 -0.0648 368  HIS A CB  
3853  C CG  . HIS D 371  ? 0.8993 0.7854 0.8142 0.0559  -0.0172 -0.0654 368  HIS A CG  
3854  N ND1 . HIS D 371  ? 0.9661 0.8309 0.8621 0.0677  -0.0220 -0.0710 368  HIS A ND1 
3855  C CD2 . HIS D 371  ? 0.9033 0.7889 0.8223 0.0568  -0.0161 -0.0613 368  HIS A CD2 
3856  C CE1 . HIS D 371  ? 0.9597 0.8117 0.8477 0.0765  -0.0238 -0.0704 368  HIS A CE1 
3857  N NE2 . HIS D 371  ? 0.9276 0.7927 0.8302 0.0696  -0.0202 -0.0643 368  HIS A NE2 
3858  N N   . LYS D 372  ? 0.7754 0.6563 0.6966 0.0180  -0.0274 -0.0565 369  LYS A N   
3859  C CA  . LYS D 372  ? 0.7912 0.6736 0.7187 0.0094  -0.0281 -0.0507 369  LYS A CA  
3860  C C   . LYS D 372  ? 0.7937 0.6906 0.7281 -0.0078 -0.0304 -0.0463 369  LYS A C   
3861  O O   . LYS D 372  ? 0.7996 0.7052 0.7424 -0.0146 -0.0294 -0.0410 369  LYS A O   
3862  C CB  . LYS D 372  ? 0.8164 0.6669 0.7264 0.0105  -0.0361 -0.0512 369  LYS A CB  
3863  C CG  . LYS D 372  ? 0.8268 0.6657 0.7283 0.0302  -0.0340 -0.0550 369  LYS A CG  
3864  C CD  . LYS D 372  ? 0.8602 0.6630 0.7390 0.0332  -0.0433 -0.0563 369  LYS A CD  
3865  C CE  . LYS D 372  ? 0.8543 0.6496 0.7234 0.0561  -0.0410 -0.0600 369  LYS A CE  
3866  N NZ  . LYS D 372  ? 0.9021 0.6579 0.7439 0.0622  -0.0509 -0.0621 369  LYS A NZ  
3867  N N   . LYS D 373  ? 0.7795 0.6818 0.7104 -0.0144 -0.0335 -0.0482 370  LYS A N   
3868  C CA  . LYS D 373  ? 0.7267 0.6486 0.6635 -0.0300 -0.0359 -0.0436 370  LYS A CA  
3869  C C   . LYS D 373  ? 0.6691 0.6207 0.6171 -0.0264 -0.0293 -0.0444 370  LYS A C   
3870  O O   . LYS D 373  ? 0.6787 0.6531 0.6325 -0.0362 -0.0301 -0.0404 370  LYS A O   
3871  C CB  . LYS D 373  ? 0.7361 0.6406 0.6566 -0.0447 -0.0474 -0.0435 370  LYS A CB  
3872  C CG  . LYS D 373  ? 0.7861 0.6526 0.6883 -0.0475 -0.0560 -0.0437 370  LYS A CG  
3873  C CD  . LYS D 373  ? 0.8230 0.6917 0.7311 -0.0552 -0.0564 -0.0369 370  LYS A CD  
3874  C CE  . LYS D 373  ? 0.8915 0.7193 0.7781 -0.0574 -0.0659 -0.0370 370  LYS A CE  
3875  N NZ  . LYS D 373  ? 0.9238 0.7531 0.8155 -0.0652 -0.0664 -0.0302 370  LYS A NZ  
3876  N N   . LEU D 374  ? 0.6158 0.5689 0.5657 -0.0121 -0.0231 -0.0490 371  LEU A N   
3877  C CA  . LEU D 374  ? 0.6069 0.5831 0.5631 -0.0080 -0.0180 -0.0502 371  LEU A CA  
3878  C C   . LEU D 374  ? 0.5486 0.5482 0.5160 -0.0084 -0.0128 -0.0455 371  LEU A C   
3879  O O   . LEU D 374  ? 0.5242 0.5458 0.4944 -0.0106 -0.0121 -0.0444 371  LEU A O   
3880  C CB  . LEU D 374  ? 0.6156 0.5868 0.5703 0.0067  -0.0126 -0.0551 371  LEU A CB  
3881  C CG  . LEU D 374  ? 0.5701 0.5607 0.5285 0.0123  -0.0076 -0.0566 371  LEU A CG  
3882  C CD1 . LEU D 374  ? 0.5707 0.5692 0.5244 0.0053  -0.0125 -0.0584 371  LEU A CD1 
3883  C CD2 . LEU D 374  ? 0.5578 0.5431 0.5144 0.0252  -0.0026 -0.0601 371  LEU A CD2 
3884  N N   . GLU D 375  ? 0.5388 0.5346 0.5114 -0.0052 -0.0095 -0.0428 372  GLU A N   
3885  C CA  . GLU D 375  ? 0.5744 0.5885 0.5544 -0.0045 -0.0054 -0.0387 372  GLU A CA  
3886  C C   . GLU D 375  ? 0.5939 0.6226 0.5764 -0.0166 -0.0096 -0.0338 372  GLU A C   
3887  O O   . GLU D 375  ? 0.5997 0.6515 0.5857 -0.0155 -0.0073 -0.0314 372  GLU A O   
3888  C CB  . GLU D 375  ? 0.6012 0.6066 0.5850 0.0006  -0.0017 -0.0368 372  GLU A CB  
3889  C CG  . GLU D 375  ? 0.6464 0.6503 0.6295 0.0115  0.0039  -0.0389 372  GLU A CG  
3890  C CD  . GLU D 375  ? 0.7106 0.7043 0.6887 0.0169  0.0037  -0.0436 372  GLU A CD  
3891  O OE1 . GLU D 375  ? 0.7708 0.7502 0.7457 0.0163  0.0005  -0.0448 372  GLU A OE1 
3892  O OE2 . GLU D 375  ? 0.6979 0.6969 0.6734 0.0227  0.0064  -0.0461 372  GLU A OE2 
3893  N N   . THR D 376  ? 0.6192 0.6350 0.5980 -0.0278 -0.0161 -0.0320 373  THR A N   
3894  C CA  . THR D 376  ? 0.6439 0.6753 0.6242 -0.0421 -0.0211 -0.0261 373  THR A CA  
3895  C C   . THR D 376  ? 0.6552 0.7090 0.6341 -0.0476 -0.0235 -0.0259 373  THR A C   
3896  O O   . THR D 376  ? 0.6582 0.7420 0.6421 -0.0525 -0.0233 -0.0209 373  THR A O   
3897  C CB  . THR D 376  ? 0.6867 0.6939 0.6594 -0.0540 -0.0289 -0.0239 373  THR A CB  
3898  O OG1 . THR D 376  ? 0.7169 0.7060 0.6910 -0.0470 -0.0263 -0.0241 373  THR A OG1 
3899  C CG2 . THR D 376  ? 0.6745 0.6990 0.6484 -0.0713 -0.0345 -0.0162 373  THR A CG2 
3900  N N   . ILE D 377  ? 0.6741 0.7163 0.6458 -0.0462 -0.0258 -0.0311 374  ILE A N   
3901  C CA  . ILE D 377  ? 0.6621 0.7262 0.6322 -0.0511 -0.0282 -0.0312 374  ILE A CA  
3902  C C   . ILE D 377  ? 0.6656 0.7578 0.6423 -0.0380 -0.0205 -0.0319 374  ILE A C   
3903  O O   . ILE D 377  ? 0.6674 0.7915 0.6464 -0.0415 -0.0212 -0.0286 374  ILE A O   
3904  C CB  . ILE D 377  ? 0.6313 0.6731 0.5907 -0.0510 -0.0324 -0.0373 374  ILE A CB  
3905  C CG1 . ILE D 377  ? 0.6402 0.6507 0.5875 -0.0637 -0.0420 -0.0365 374  ILE A CG1 
3906  C CG2 . ILE D 377  ? 0.6217 0.6877 0.5799 -0.0551 -0.0345 -0.0376 374  ILE A CG2 
3907  C CD1 . ILE D 377  ? 0.6656 0.6480 0.5987 -0.0605 -0.0466 -0.0433 374  ILE A CD1 
3908  N N   . SER D 378  ? 0.6732 0.7542 0.6510 -0.0226 -0.0136 -0.0358 375  SER A N   
3909  C CA  . SER D 378  ? 0.6539 0.7539 0.6329 -0.0093 -0.0074 -0.0367 375  SER A CA  
3910  C C   . SER D 378  ? 0.6454 0.7705 0.6286 -0.0097 -0.0062 -0.0310 375  SER A C   
3911  O O   . SER D 378  ? 0.6526 0.8044 0.6344 -0.0031 -0.0045 -0.0302 375  SER A O   
3912  C CB  . SER D 378  ? 0.6480 0.7276 0.6252 0.0037  -0.0018 -0.0404 375  SER A CB  
3913  O OG  . SER D 378  ? 0.6372 0.7280 0.6104 0.0163  0.0027  -0.0419 375  SER A OG  
3914  N N   . SER D 379  ? 0.6693 0.7869 0.6564 -0.0159 -0.0073 -0.0270 376  SER A N   
3915  C CA  . SER D 379  ? 0.6753 0.8166 0.6659 -0.0157 -0.0062 -0.0215 376  SER A CA  
3916  C C   . SER D 379  ? 0.6654 0.8387 0.6587 -0.0286 -0.0110 -0.0157 376  SER A C   
3917  O O   . SER D 379  ? 0.6727 0.8770 0.6676 -0.0247 -0.0094 -0.0115 376  SER A O   
3918  C CB  . SER D 379  ? 0.7038 0.8278 0.6980 -0.0190 -0.0060 -0.0188 376  SER A CB  
3919  O OG  . SER D 379  ? 0.7441 0.8895 0.7405 -0.0164 -0.0044 -0.0140 376  SER A OG  
3920  N N   . ALA D 380  ? 0.6740 0.8408 0.6659 -0.0438 -0.0174 -0.0151 377  ALA A N   
3921  C CA  . ALA D 380  ? 0.7111 0.9080 0.7043 -0.0602 -0.0235 -0.0083 377  ALA A CA  
3922  C C   . ALA D 380  ? 0.7172 0.9436 0.7088 -0.0573 -0.0235 -0.0093 377  ALA A C   
3923  O O   . ALA D 380  ? 0.7454 1.0106 0.7395 -0.0667 -0.0266 -0.0025 377  ALA A O   
3924  C CB  . ALA D 380  ? 0.7309 0.9028 0.7193 -0.0806 -0.0324 -0.0063 377  ALA A CB  
3925  N N   . LEU D 381  ? 0.6969 0.9084 0.6843 -0.0447 -0.0203 -0.0170 378  LEU A N   
3926  C CA  . LEU D 381  ? 0.6825 0.9192 0.6674 -0.0409 -0.0204 -0.0186 378  LEU A CA  
3927  C C   . LEU D 381  ? 0.7255 0.9730 0.7078 -0.0174 -0.0126 -0.0228 378  LEU A C   
3928  O O   . LEU D 381  ? 0.7294 1.0054 0.7095 -0.0117 -0.0121 -0.0231 378  LEU A O   
3929  C CB  . LEU D 381  ? 0.6903 0.9009 0.6693 -0.0474 -0.0247 -0.0240 378  LEU A CB  
3930  C CG  . LEU D 381  ? 0.7349 0.9247 0.7099 -0.0696 -0.0342 -0.0212 378  LEU A CG  
3931  C CD1 . LEU D 381  ? 0.7531 0.9199 0.7188 -0.0729 -0.0388 -0.0271 378  LEU A CD1 
3932  C CD2 . LEU D 381  ? 0.7626 0.9876 0.7402 -0.0888 -0.0404 -0.0113 378  LEU A CD2 
3933  N N   . CYS D 382  ? 0.7845 1.0094 0.7651 -0.0040 -0.0073 -0.0258 379  CYS A N   
3934  C CA  . CYS D 382  ? 0.8348 1.0611 0.8079 0.0174  -0.0015 -0.0300 379  CYS A CA  
3935  C C   . CYS D 382  ? 0.8670 1.0970 0.8375 0.0282  0.0019  -0.0275 379  CYS A C   
3936  O O   . CYS D 382  ? 0.8487 1.0885 0.8255 0.0194  0.0002  -0.0221 379  CYS A O   
3937  C CB  . CYS D 382  ? 0.8256 1.0148 0.7940 0.0240  0.0009  -0.0368 379  CYS A CB  
3938  S SG  . CYS D 382  ? 0.8082 0.9862 0.7774 0.0130  -0.0034 -0.0406 379  CYS A SG  
3939  N N   . ASP D 383  ? 0.9548 1.1747 0.9140 0.0472  0.0060  -0.0315 380  ASP A N   
3940  C CA  . ASP D 383  ? 1.0271 1.2464 0.9789 0.0594  0.0083  -0.0299 380  ASP A CA  
3941  C C   . ASP D 383  ? 1.0285 1.2197 0.9857 0.0511  0.0082  -0.0286 380  ASP A C   
3942  O O   . ASP D 383  ? 1.0317 1.2333 0.9924 0.0483  0.0077  -0.0240 380  ASP A O   
3943  C CB  . ASP D 383  ? 1.0929 1.2984 1.0266 0.0803  0.0110  -0.0347 380  ASP A CB  
3944  C CG  . ASP D 383  ? 1.1402 1.3736 1.0671 0.0910  0.0112  -0.0364 380  ASP A CG  
3945  O OD1 . ASP D 383  ? 1.1665 1.3935 1.0948 0.0878  0.0110  -0.0398 380  ASP A OD1 
3946  O OD2 . ASP D 383  ? 1.1522 1.4151 1.0715 0.1038  0.0116  -0.0342 380  ASP A OD2 
3947  N N   . HIS D 384  ? 0.9846 1.1425 0.9423 0.0476  0.0089  -0.0321 381  HIS A N   
3948  C CA  . HIS D 384  ? 0.9666 1.0992 0.9286 0.0413  0.0090  -0.0309 381  HIS A CA  
3949  C C   . HIS D 384  ? 0.9123 1.0268 0.8825 0.0296  0.0076  -0.0326 381  HIS A C   
3950  O O   . HIS D 384  ? 0.9005 1.0182 0.8713 0.0270  0.0064  -0.0352 381  HIS A O   
3951  C CB  . HIS D 384  ? 0.9878 1.0963 0.9373 0.0531  0.0115  -0.0329 381  HIS A CB  
3952  C CG  . HIS D 384  ? 1.0308 1.1486 0.9640 0.0697  0.0123  -0.0339 381  HIS A CG  
3953  N ND1 . HIS D 384  ? 1.0538 1.1626 0.9730 0.0813  0.0131  -0.0379 381  HIS A ND1 
3954  C CD2 . HIS D 384  ? 1.0503 1.1852 0.9769 0.0784  0.0119  -0.0314 381  HIS A CD2 
3955  C CE1 . HIS D 384  ? 1.0690 1.1863 0.9719 0.0970  0.0130  -0.0382 381  HIS A CE1 
3956  N NE2 . HIS D 384  ? 1.0652 1.1993 0.9721 0.0963  0.0124  -0.0344 381  HIS A NE2 
3957  N N   . TRP D 385  ? 0.8591 0.9543 0.8340 0.0238  0.0075  -0.0311 382  TRP A N   
3958  C CA  . TRP D 385  ? 0.8300 0.9050 0.8091 0.0170  0.0064  -0.0331 382  TRP A CA  
3959  C C   . TRP D 385  ? 0.8675 0.9277 0.8406 0.0254  0.0092  -0.0375 382  TRP A C   
3960  O O   . TRP D 385  ? 0.8938 0.9426 0.8686 0.0227  0.0084  -0.0400 382  TRP A O   
3961  C CB  . TRP D 385  ? 0.7616 0.8223 0.7458 0.0118  0.0061  -0.0302 382  TRP A CB  
3962  C CG  . TRP D 385  ? 0.6957 0.7460 0.6753 0.0196  0.0094  -0.0296 382  TRP A CG  
3963  C CD1 . TRP D 385  ? 0.6679 0.7247 0.6428 0.0247  0.0103  -0.0273 382  TRP A CD1 
3964  C CD2 . TRP D 385  ? 0.6878 0.7197 0.6650 0.0228  0.0115  -0.0309 382  TRP A CD2 
3965  N NE1 . TRP D 385  ? 0.6723 0.7118 0.6405 0.0294  0.0120  -0.0272 382  TRP A NE1 
3966  C CE2 . TRP D 385  ? 0.6774 0.7037 0.6479 0.0273  0.0129  -0.0289 382  TRP A CE2 
3967  C CE3 . TRP D 385  ? 0.6888 0.7099 0.6678 0.0223  0.0120  -0.0333 382  TRP A CE3 
3968  C CZ2 . TRP D 385  ? 0.6874 0.6986 0.6536 0.0286  0.0143  -0.0282 382  TRP A CZ2 
3969  C CZ3 . TRP D 385  ? 0.6733 0.6835 0.6495 0.0253  0.0143  -0.0326 382  TRP A CZ3 
3970  C CH2 . TRP D 385  ? 0.6861 0.6919 0.6564 0.0271  0.0152  -0.0296 382  TRP A CH2 
3971  N N   . ASP D 386  ? 0.8929 0.9520 0.8569 0.0357  0.0118  -0.0382 383  ASP A N   
3972  C CA  . ASP D 386  ? 0.8585 0.9026 0.8150 0.0421  0.0140  -0.0409 383  ASP A CA  
3973  C C   . ASP D 386  ? 0.8327 0.8838 0.7862 0.0458  0.0141  -0.0450 383  ASP A C   
3974  O O   . ASP D 386  ? 0.8348 0.8748 0.7866 0.0473  0.0153  -0.0474 383  ASP A O   
3975  C CB  . ASP D 386  ? 0.9036 0.9394 0.8468 0.0507  0.0153  -0.0398 383  ASP A CB  
3976  C CG  . ASP D 386  ? 0.9971 1.0146 0.9396 0.0472  0.0158  -0.0370 383  ASP A CG  
3977  O OD1 . ASP D 386  ? 1.0408 1.0522 0.9910 0.0419  0.0165  -0.0369 383  ASP A OD1 
3978  O OD2 . ASP D 386  ? 1.0482 1.0579 0.9809 0.0503  0.0152  -0.0348 383  ASP A OD2 
3979  N N   . THR D 387  ? 0.7881 0.8601 0.7407 0.0475  0.0128  -0.0454 384  THR A N   
3980  C CA  . THR D 387  ? 0.7709 0.8512 0.7172 0.0542  0.0132  -0.0490 384  THR A CA  
3981  C C   . THR D 387  ? 0.7469 0.8202 0.6978 0.0489  0.0123  -0.0522 384  THR A C   
3982  O O   . THR D 387  ? 0.7503 0.8178 0.6949 0.0554  0.0139  -0.0555 384  THR A O   
3983  C CB  . THR D 387  ? 0.7802 0.8903 0.7266 0.0556  0.0116  -0.0477 384  THR A CB  
3984  O OG1 . THR D 387  ? 0.8158 0.9376 0.7737 0.0418  0.0083  -0.0445 384  THR A OG1 
3985  C CG2 . THR D 387  ? 0.7570 0.8738 0.6932 0.0673  0.0130  -0.0459 384  THR A CG2 
3986  N N   . LEU D 388  ? 0.7054 0.7769 0.6649 0.0377  0.0091  -0.0514 385  LEU A N   
3987  C CA  . LEU D 388  ? 0.6748 0.7370 0.6348 0.0341  0.0071  -0.0551 385  LEU A CA  
3988  C C   . LEU D 388  ? 0.6687 0.7108 0.6267 0.0396  0.0101  -0.0569 385  LEU A C   
3989  O O   . LEU D 388  ? 0.6843 0.7227 0.6379 0.0450  0.0113  -0.0604 385  LEU A O   
3990  C CB  . LEU D 388  ? 0.6741 0.7338 0.6386 0.0211  0.0016  -0.0536 385  LEU A CB  
3991  C CG  . LEU D 388  ? 0.6850 0.7675 0.6504 0.0125  -0.0029 -0.0517 385  LEU A CG  
3992  C CD1 . LEU D 388  ? 0.6681 0.7398 0.6320 -0.0014 -0.0101 -0.0516 385  LEU A CD1 
3993  C CD2 . LEU D 388  ? 0.7042 0.8031 0.6653 0.0200  -0.0013 -0.0546 385  LEU A CD2 
3994  N N   . ARG D 389  ? 0.6607 0.6924 0.6221 0.0380  0.0112  -0.0539 386  ARG A N   
3995  C CA  . ARG D 389  ? 0.6781 0.6967 0.6383 0.0424  0.0141  -0.0542 386  ARG A CA  
3996  C C   . ARG D 389  ? 0.7156 0.7344 0.6682 0.0501  0.0175  -0.0544 386  ARG A C   
3997  O O   . ARG D 389  ? 0.7474 0.7612 0.6974 0.0539  0.0194  -0.0557 386  ARG A O   
3998  C CB  . ARG D 389  ? 0.7069 0.7189 0.6719 0.0391  0.0146  -0.0500 386  ARG A CB  
3999  C CG  . ARG D 389  ? 0.7361 0.7405 0.7011 0.0426  0.0172  -0.0490 386  ARG A CG  
4000  C CD  . ARG D 389  ? 0.7686 0.7706 0.7366 0.0397  0.0184  -0.0438 386  ARG A CD  
4001  N NE  . ARG D 389  ? 0.7994 0.8024 0.7616 0.0400  0.0193  -0.0414 386  ARG A NE  
4002  C CZ  . ARG D 389  ? 0.8215 0.8205 0.7827 0.0374  0.0196  -0.0369 386  ARG A CZ  
4003  N NH1 . ARG D 389  ? 0.8286 0.8262 0.7967 0.0337  0.0198  -0.0339 386  ARG A NH1 
4004  N NH2 . ARG D 389  ? 0.8177 0.8132 0.7690 0.0392  0.0194  -0.0355 386  ARG A NH2 
4005  N N   . ASN D 390  ? 0.7209 0.7450 0.6680 0.0529  0.0180  -0.0530 387  ASN A N   
4006  C CA  . ASN D 390  ? 0.7309 0.7500 0.6660 0.0604  0.0200  -0.0531 387  ASN A CA  
4007  C C   . ASN D 390  ? 0.7480 0.7733 0.6786 0.0658  0.0202  -0.0575 387  ASN A C   
4008  O O   . ASN D 390  ? 0.7660 0.7844 0.6894 0.0701  0.0220  -0.0582 387  ASN A O   
4009  C CB  . ASN D 390  ? 0.7544 0.7737 0.6803 0.0643  0.0195  -0.0510 387  ASN A CB  
4010  C CG  . ASN D 390  ? 0.7765 0.7857 0.7032 0.0597  0.0193  -0.0465 387  ASN A CG  
4011  O OD1 . ASN D 390  ? 0.8017 0.7970 0.7162 0.0617  0.0192  -0.0441 387  ASN A OD1 
4012  N ND2 . ASN D 390  ? 0.7804 0.7950 0.7196 0.0528  0.0184  -0.0451 387  ASN A ND2 
4013  N N   . ALA D 391  ? 0.7391 0.7790 0.6737 0.0646  0.0182  -0.0599 388  ALA A N   
4014  C CA  . ALA D 391  ? 0.7033 0.7511 0.6339 0.0691  0.0180  -0.0639 388  ALA A CA  
4015  C C   . ALA D 391  ? 0.7295 0.7686 0.6627 0.0679  0.0182  -0.0667 388  ALA A C   
4016  O O   . ALA D 391  ? 0.7478 0.7856 0.6746 0.0741  0.0197  -0.0692 388  ALA A O   
4017  C CB  . ALA D 391  ? 0.6516 0.7197 0.5865 0.0653  0.0148  -0.0647 388  ALA A CB  
4018  N N   . LEU D 392  ? 0.7139 0.7465 0.6546 0.0614  0.0165  -0.0664 389  LEU A N   
4019  C CA  . LEU D 392  ? 0.6909 0.7145 0.6315 0.0631  0.0167  -0.0691 389  LEU A CA  
4020  C C   . LEU D 392  ? 0.6869 0.7047 0.6243 0.0685  0.0209  -0.0669 389  LEU A C   
4021  O O   . LEU D 392  ? 0.6751 0.6917 0.6092 0.0735  0.0223  -0.0690 389  LEU A O   
4022  C CB  . LEU D 392  ? 0.6713 0.6866 0.6168 0.0571  0.0133  -0.0691 389  LEU A CB  
4023  C CG  . LEU D 392  ? 0.6800 0.6976 0.6262 0.0486  0.0075  -0.0705 389  LEU A CG  
4024  C CD1 . LEU D 392  ? 0.7135 0.7167 0.6606 0.0433  0.0036  -0.0699 389  LEU A CD1 
4025  C CD2 . LEU D 392  ? 0.6787 0.6989 0.6191 0.0498  0.0048  -0.0754 389  LEU A CD2 
4026  N N   . TYR D 393  ? 0.6959 0.7108 0.6333 0.0666  0.0225  -0.0620 390  TYR A N   
4027  C CA  . TYR D 393  ? 0.6774 0.6876 0.6103 0.0683  0.0254  -0.0582 390  TYR A CA  
4028  C C   . TYR D 393  ? 0.6830 0.6925 0.6047 0.0738  0.0267  -0.0592 390  TYR A C   
4029  O O   . TYR D 393  ? 0.7001 0.7094 0.6185 0.0761  0.0286  -0.0583 390  TYR A O   
4030  C CB  . TYR D 393  ? 0.6310 0.6362 0.5636 0.0635  0.0255  -0.0527 390  TYR A CB  
4031  C CG  . TYR D 393  ? 0.6445 0.6442 0.5692 0.0624  0.0271  -0.0475 390  TYR A CG  
4032  C CD1 . TYR D 393  ? 0.6507 0.6544 0.5803 0.0599  0.0287  -0.0439 390  TYR A CD1 
4033  C CD2 . TYR D 393  ? 0.6470 0.6374 0.5569 0.0636  0.0262  -0.0457 390  TYR A CD2 
4034  C CE1 . TYR D 393  ? 0.6532 0.6552 0.5754 0.0561  0.0294  -0.0377 390  TYR A CE1 
4035  C CE2 . TYR D 393  ? 0.6381 0.6202 0.5375 0.0598  0.0262  -0.0401 390  TYR A CE2 
4036  C CZ  . TYR D 393  ? 0.6362 0.6256 0.5427 0.0547  0.0278  -0.0356 390  TYR A CZ  
4037  O OH  . TYR D 393  ? 0.6301 0.6146 0.5261 0.0482  0.0271  -0.0285 390  TYR A OH  
4038  N N   . GLU D 394  ? 0.6864 0.6971 0.6012 0.0768  0.0256  -0.0607 391  GLU A N   
4039  C CA  . GLU D 394  ? 0.7132 0.7208 0.6143 0.0835  0.0263  -0.0615 391  GLU A CA  
4040  C C   . GLU D 394  ? 0.7238 0.7383 0.6263 0.0877  0.0271  -0.0662 391  GLU A C   
4041  O O   . GLU D 394  ? 0.7625 0.7732 0.6564 0.0915  0.0286  -0.0658 391  GLU A O   
4042  C CB  . GLU D 394  ? 0.7355 0.7446 0.6273 0.0888  0.0248  -0.0625 391  GLU A CB  
4043  C CG  . GLU D 394  ? 0.7713 0.7704 0.6569 0.0868  0.0236  -0.0582 391  GLU A CG  
4044  C CD  . GLU D 394  ? 0.8125 0.7924 0.6838 0.0852  0.0234  -0.0536 391  GLU A CD  
4045  O OE1 . GLU D 394  ? 0.8072 0.7811 0.6677 0.0887  0.0238  -0.0538 391  GLU A OE1 
4046  O OE2 . GLU D 394  ? 0.8466 0.8172 0.7166 0.0793  0.0222  -0.0492 391  GLU A OE2 
4047  N N   . ARG D 395  ? 0.7094 0.7327 0.6210 0.0863  0.0254  -0.0704 392  ARG A N   
4048  C CA  . ARG D 395  ? 0.6975 0.7255 0.6085 0.0901  0.0252  -0.0752 392  ARG A CA  
4049  C C   . ARG D 395  ? 0.6942 0.7179 0.6073 0.0911  0.0269  -0.0750 392  ARG A C   
4050  O O   . ARG D 395  ? 0.7165 0.7420 0.6250 0.0966  0.0280  -0.0776 392  ARG A O   
4051  C CB  . ARG D 395  ? 0.7124 0.7486 0.6295 0.0862  0.0214  -0.0791 392  ARG A CB  
4052  C CG  . ARG D 395  ? 0.7417 0.7840 0.6548 0.0902  0.0201  -0.0842 392  ARG A CG  
4053  C CD  . ARG D 395  ? 0.7957 0.8446 0.7128 0.0831  0.0149  -0.0870 392  ARG A CD  
4054  N NE  . ARG D 395  ? 0.8561 0.8936 0.7733 0.0809  0.0120  -0.0903 392  ARG A NE  
4055  C CZ  . ARG D 395  ? 0.9008 0.9368 0.8124 0.0841  0.0100  -0.0952 392  ARG A CZ  
4056  N NH1 . ARG D 395  ? 0.8960 0.9436 0.8036 0.0887  0.0111  -0.0970 392  ARG A NH1 
4057  N NH2 . ARG D 395  ? 0.9213 0.9434 0.8294 0.0839  0.0066  -0.0984 392  ARG A NH2 
4058  N N   . ARG D 396  ? 0.6815 0.7016 0.6010 0.0871  0.0272  -0.0719 393  ARG A N   
4059  C CA  . ARG D 396  ? 0.7067 0.7273 0.6276 0.0902  0.0291  -0.0710 393  ARG A CA  
4060  C C   . ARG D 396  ? 0.7263 0.7488 0.6414 0.0909  0.0325  -0.0654 393  ARG A C   
4061  O O   . ARG D 396  ? 0.7461 0.7743 0.6589 0.0956  0.0345  -0.0653 393  ARG A O   
4062  C CB  . ARG D 396  ? 0.7069 0.7252 0.6354 0.0870  0.0281  -0.0693 393  ARG A CB  
4063  C CG  . ARG D 396  ? 0.7384 0.7509 0.6686 0.0862  0.0236  -0.0747 393  ARG A CG  
4064  C CD  . ARG D 396  ? 0.7861 0.7933 0.7200 0.0860  0.0224  -0.0734 393  ARG A CD  
4065  N NE  . ARG D 396  ? 0.8423 0.8383 0.7727 0.0854  0.0167  -0.0787 393  ARG A NE  
4066  C CZ  . ARG D 396  ? 0.8570 0.8429 0.7857 0.0872  0.0140  -0.0793 393  ARG A CZ  
4067  N NH1 . ARG D 396  ? 0.8560 0.8465 0.7888 0.0905  0.0172  -0.0749 393  ARG A NH1 
4068  N NH2 . ARG D 396  ? 0.8536 0.8245 0.7747 0.0853  0.0074  -0.0840 393  ARG A NH2 
4069  N N   . ILE D 397  ? 0.7088 0.7260 0.6197 0.0859  0.0326  -0.0604 394  ILE A N   
4070  C CA  . ILE D 397  ? 0.7045 0.7188 0.6050 0.0843  0.0340  -0.0547 394  ILE A CA  
4071  C C   . ILE D 397  ? 0.7054 0.7185 0.5956 0.0906  0.0344  -0.0580 394  ILE A C   
4072  O O   . ILE D 397  ? 0.7018 0.7157 0.5843 0.0909  0.0358  -0.0545 394  ILE A O   
4073  C CB  . ILE D 397  ? 0.7178 0.7206 0.6111 0.0778  0.0323  -0.0494 394  ILE A CB  
4074  C CG1 . ILE D 397  ? 0.7200 0.7255 0.6240 0.0714  0.0321  -0.0457 394  ILE A CG1 
4075  C CG2 . ILE D 397  ? 0.7432 0.7373 0.6208 0.0743  0.0319  -0.0431 394  ILE A CG2 
4076  C CD1 . ILE D 397  ? 0.7340 0.7510 0.6434 0.0686  0.0343  -0.0406 394  ILE A CD1 
4077  N N   . SER D 398  ? 0.7005 0.7137 0.5902 0.0953  0.0329  -0.0642 395  SER A N   
4078  C CA  . SER D 398  ? 0.7001 0.7141 0.5804 0.1023  0.0331  -0.0679 395  SER A CA  
4079  C C   . SER D 398  ? 0.7156 0.7378 0.5989 0.1066  0.0348  -0.0707 395  SER A C   
4080  O O   . SER D 398  ? 0.7410 0.7638 0.6156 0.1121  0.0355  -0.0724 395  SER A O   
4081  C CB  . SER D 398  ? 0.6763 0.6947 0.5574 0.1057  0.0309  -0.0733 395  SER A CB  
4082  O OG  . SER D 398  ? 0.7054 0.7294 0.5810 0.1128  0.0310  -0.0779 395  SER A OG  
4083  N N   . GLU D 399  ? 0.7255 0.7533 0.6191 0.1058  0.0352  -0.0715 396  GLU A N   
4084  C CA  . GLU D 399  ? 0.7504 0.7852 0.6449 0.1123  0.0363  -0.0750 396  GLU A CA  
4085  C C   . GLU D 399  ? 0.7724 0.8150 0.6699 0.1125  0.0390  -0.0697 396  GLU A C   
4086  O O   . GLU D 399  ? 0.7915 0.8404 0.6914 0.1191  0.0394  -0.0728 396  GLU A O   
4087  C CB  . GLU D 399  ? 0.7875 0.8212 0.6869 0.1144  0.0330  -0.0825 396  GLU A CB  
4088  C CG  . GLU D 399  ? 0.8354 0.8643 0.7425 0.1084  0.0305  -0.0819 396  GLU A CG  
4089  C CD  . GLU D 399  ? 0.8717 0.8966 0.7799 0.1064  0.0256  -0.0881 396  GLU A CD  
4090  O OE1 . GLU D 399  ? 0.8542 0.8820 0.7579 0.1084  0.0241  -0.0923 396  GLU A OE1 
4091  O OE2 . GLU D 399  ? 0.8971 0.9160 0.8095 0.1019  0.0227  -0.0883 396  GLU A OE2 
4092  N N   . LEU D 400  ? 0.7847 0.8277 0.6803 0.1056  0.0403  -0.0614 397  LEU A N   
4093  C CA  . LEU D 400  ? 0.7944 0.8509 0.6921 0.1046  0.0430  -0.0545 397  LEU A CA  
4094  C C   . LEU D 400  ? 0.8537 0.9177 0.7426 0.1070  0.0450  -0.0516 397  LEU A C   
4095  O O   . LEU D 400  ? 0.8819 0.9365 0.7613 0.1080  0.0442  -0.0538 397  LEU A O   
4096  C CB  . LEU D 400  ? 0.7543 0.8093 0.6528 0.0936  0.0426  -0.0458 397  LEU A CB  
4097  C CG  . LEU D 400  ? 0.7229 0.7759 0.6316 0.0909  0.0414  -0.0464 397  LEU A CG  
4098  C CD1 . LEU D 400  ? 0.6842 0.7353 0.5915 0.0794  0.0407  -0.0373 397  LEU A CD1 
4099  C CD2 . LEU D 400  ? 0.7258 0.7923 0.6427 0.0989  0.0427  -0.0485 397  LEU A CD2 
4100  N N   . THR D 401  ? 0.8592 0.9421 0.7507 0.1085  0.0477  -0.0462 398  THR A N   
4101  C CA  . THR D 401  ? 0.8714 0.9665 0.7558 0.1111  0.0499  -0.0427 398  THR A CA  
4102  C C   . THR D 401  ? 0.8983 1.0004 0.7769 0.0982  0.0503  -0.0299 398  THR A C   
4103  O O   . THR D 401  ? 0.8871 1.0003 0.7720 0.0915  0.0505  -0.0230 398  THR A O   
4104  C CB  . THR D 401  ? 0.8787 0.9942 0.7682 0.1238  0.0525  -0.0456 398  THR A CB  
4105  O OG1 . THR D 401  ? 0.9019 1.0058 0.7933 0.1340  0.0505  -0.0573 398  THR A OG1 
4106  C CG2 . THR D 401  ? 0.8705 1.0000 0.7527 0.1274  0.0550  -0.0424 398  THR A CG2 
4107  N N   . GLY D 402  ? 0.9371 1.0319 0.8023 0.0939  0.0496  -0.0263 399  GLY A N   
4108  C CA  . GLY D 402  ? 0.9442 1.0441 0.7998 0.0800  0.0487  -0.0133 399  GLY A CA  
4109  C C   . GLY D 402  ? 0.9301 1.0097 0.7785 0.0660  0.0445  -0.0077 399  GLY A C   
4110  O O   . GLY D 402  ? 0.8954 0.9525 0.7421 0.0680  0.0422  -0.0142 399  GLY A O   
4111  N N   . LYS D 403  ? 0.9596 1.0488 0.8026 0.0512  0.0431  0.0053  400  LYS A N   
4112  C CA  . LYS D 403  ? 0.9875 1.0568 0.8205 0.0359  0.0381  0.0121  400  LYS A CA  
4113  C C   . LYS D 403  ? 0.9948 1.0655 0.8433 0.0380  0.0386  0.0080  400  LYS A C   
4114  O O   . LYS D 403  ? 1.0049 1.1020 0.8676 0.0363  0.0409  0.0124  400  LYS A O   
4115  C CB  . LYS D 403  ? 0.9830 1.0671 0.8079 0.0175  0.0359  0.0280  400  LYS A CB  
4116  N N   . ILE D 404  ? 1.0162 1.0604 0.8613 0.0426  0.0364  -0.0003 401  ILE A N   
4117  C CA  . ILE D 404  ? 1.0408 1.0842 0.8996 0.0446  0.0365  -0.0046 401  ILE A CA  
4118  C C   . ILE D 404  ? 1.0493 1.0888 0.9036 0.0288  0.0331  0.0055  401  ILE A C   
4119  O O   . ILE D 404  ? 1.0785 1.0902 0.9166 0.0218  0.0282  0.0071  401  ILE A O   
4120  C CB  . ILE D 404  ? 1.0765 1.0972 0.9326 0.0536  0.0351  -0.0153 401  ILE A CB  
4121  C CG1 . ILE D 404  ? 1.1318 1.1245 0.9636 0.0511  0.0309  -0.0143 401  ILE A CG1 
4122  C CG2 . ILE D 404  ? 1.0697 1.1006 0.9364 0.0680  0.0384  -0.0254 401  ILE A CG2 
4123  C CD1 . ILE D 404  ? 1.1517 1.1271 0.9798 0.0609  0.0295  -0.0237 401  ILE A CD1 
4124  N N   . THR D 405  ? 1.0728 1.1405 0.9399 0.0239  0.0352  0.0125  402  THR A N   
4125  C CA  . THR D 405  ? 1.0780 1.1466 0.9427 0.0080  0.0319  0.0226  402  THR A CA  
4126  C C   . THR D 405  ? 1.0492 1.1044 0.9217 0.0107  0.0308  0.0168  402  THR A C   
4127  O O   . THR D 405  ? 1.0501 1.1000 0.9318 0.0240  0.0330  0.0059  402  THR A O   
4128  C CB  . THR D 405  ? 1.0353 1.1444 0.9124 0.0034  0.0348  0.0321  402  THR A CB  
4129  O OG1 . THR D 405  ? 1.0078 1.1357 0.9052 0.0173  0.0392  0.0254  402  THR A OG1 
4130  C CG2 . THR D 405  ? 1.0098 1.1389 0.8830 0.0049  0.0372  0.0363  402  THR A CG2 
4131  N N   . LYS D 406  ? 1.0277 1.0777 0.8955 -0.0035 0.0270  0.0248  403  LYS A N   
4132  C CA  . LYS D 406  ? 1.0148 1.0567 0.8915 -0.0016 0.0264  0.0207  403  LYS A CA  
4133  C C   . LYS D 406  ? 1.0028 1.0750 0.9029 0.0064  0.0312  0.0190  403  LYS A C   
4134  O O   . LYS D 406  ? 0.9998 1.0662 0.9095 0.0119  0.0316  0.0131  403  LYS A O   
4135  C CB  . LYS D 406  ? 1.0435 1.0697 0.9068 -0.0188 0.0203  0.0296  403  LYS A CB  
4136  C CG  . LYS D 406  ? 1.0845 1.1396 0.9593 -0.0297 0.0207  0.0398  403  LYS A CG  
4137  C CD  . LYS D 406  ? 1.1127 1.1535 0.9869 -0.0366 0.0170  0.0409  403  LYS A CD  
4138  C CE  . LYS D 406  ? 1.1120 1.1853 1.0000 -0.0454 0.0180  0.0502  403  LYS A CE  
4139  N NZ  . LYS D 406  ? 1.1073 1.1678 0.9969 -0.0503 0.0150  0.0502  403  LYS A NZ  
4140  N N   . SER D 407  ? 0.9423 1.0464 0.8498 0.0079  0.0346  0.0242  404  SER A N   
4141  C CA  . SER D 407  ? 0.8883 1.0191 0.8139 0.0200  0.0389  0.0213  404  SER A CA  
4142  C C   . SER D 407  ? 0.8113 0.9330 0.7421 0.0381  0.0414  0.0080  404  SER A C   
4143  O O   . SER D 407  ? 0.7466 0.8691 0.6875 0.0474  0.0424  0.0020  404  SER A O   
4144  C CB  . SER D 407  ? 0.9088 1.0790 0.8386 0.0189  0.0418  0.0309  404  SER A CB  
4145  O OG  . SER D 407  ? 0.9096 1.1039 0.8530 0.0352  0.0458  0.0268  404  SER A OG  
4146  N N   . ALA D 408  ? 0.7893 0.9012 0.7119 0.0424  0.0417  0.0036  405  ALA A N   
4147  C CA  . ALA D 408  ? 0.7693 0.8717 0.6950 0.0573  0.0430  -0.0086 405  ALA A CA  
4148  C C   . ALA D 408  ? 0.7403 0.8171 0.6666 0.0574  0.0404  -0.0159 405  ALA A C   
4149  O O   . ALA D 408  ? 0.7414 0.8139 0.6739 0.0672  0.0406  -0.0245 405  ALA A O   
4150  C CB  . ALA D 408  ? 0.7863 0.8850 0.7024 0.0608  0.0437  -0.0109 405  ALA A CB  
4151  N N   . LYS D 409  ? 0.7293 0.7889 0.6474 0.0466  0.0374  -0.0122 406  LYS A N   
4152  C CA  . LYS D 409  ? 0.7276 0.7675 0.6462 0.0474  0.0351  -0.0181 406  LYS A CA  
4153  C C   . LYS D 409  ? 0.7024 0.7485 0.6338 0.0471  0.0352  -0.0180 406  LYS A C   
4154  O O   . LYS D 409  ? 0.6891 0.7277 0.6263 0.0524  0.0346  -0.0249 406  LYS A O   
4155  C CB  . LYS D 409  ? 0.7987 0.8176 0.7017 0.0384  0.0314  -0.0144 406  LYS A CB  
4156  C CG  . LYS D 409  ? 0.8630 0.8706 0.7498 0.0401  0.0304  -0.0152 406  LYS A CG  
4157  C CD  . LYS D 409  ? 0.9104 0.8910 0.7777 0.0356  0.0258  -0.0140 406  LYS A CD  
4158  C CE  . LYS D 409  ? 0.9694 0.9363 0.8184 0.0400  0.0245  -0.0158 406  LYS A CE  
4159  N NZ  . LYS D 409  ? 1.0137 0.9516 0.8402 0.0403  0.0196  -0.0162 406  LYS A NZ  
4160  N N   . GLU D 410  ? 0.7098 0.7706 0.6450 0.0404  0.0357  -0.0096 407  GLU A N   
4161  C CA  . GLU D 410  ? 0.7260 0.7939 0.6726 0.0413  0.0359  -0.0091 407  GLU A CA  
4162  C C   . GLU D 410  ? 0.6897 0.7675 0.6447 0.0552  0.0380  -0.0156 407  GLU A C   
4163  O O   . GLU D 410  ? 0.6574 0.7302 0.6187 0.0588  0.0370  -0.0192 407  GLU A O   
4164  C CB  . GLU D 410  ? 0.7937 0.8790 0.7418 0.0311  0.0358  0.0020  407  GLU A CB  
4165  C CG  . GLU D 410  ? 0.8912 0.9607 0.8273 0.0159  0.0318  0.0086  407  GLU A CG  
4166  C CD  . GLU D 410  ? 0.9772 1.0652 0.9137 0.0031  0.0307  0.0206  407  GLU A CD  
4167  O OE1 . GLU D 410  ? 0.9933 1.1115 0.9406 0.0074  0.0339  0.0243  407  GLU A OE1 
4168  O OE2 . GLU D 410  ? 1.0214 1.0942 0.9460 -0.0107 0.0262  0.0266  407  GLU A OE2 
4169  N N   . LYS D 411  ? 0.6749 0.7647 0.6279 0.0633  0.0402  -0.0171 408  LYS A N   
4170  C CA  . LYS D 411  ? 0.6139 0.7073 0.5698 0.0781  0.0410  -0.0243 408  LYS A CA  
4171  C C   . LYS D 411  ? 0.6024 0.6722 0.5562 0.0815  0.0383  -0.0343 408  LYS A C   
4172  O O   . LYS D 411  ? 0.6269 0.6894 0.5822 0.0886  0.0365  -0.0398 408  LYS A O   
4173  C CB  . LYS D 411  ? 0.5959 0.7077 0.5483 0.0866  0.0438  -0.0236 408  LYS A CB  
4174  C CG  . LYS D 411  ? 0.5721 0.7151 0.5275 0.0846  0.0465  -0.0130 408  LYS A CG  
4175  C CD  . LYS D 411  ? 0.5406 0.7048 0.4926 0.0949  0.0495  -0.0126 408  LYS A CD  
4176  C CE  . LYS D 411  ? 0.5128 0.7151 0.4685 0.0930  0.0522  -0.0009 408  LYS A CE  
4177  N NZ  . LYS D 411  ? 0.4997 0.7267 0.4521 0.1047  0.0554  -0.0001 408  LYS A NZ  
4178  N N   . VAL D 412  ? 0.5907 0.6485 0.5394 0.0763  0.0375  -0.0362 409  VAL A N   
4179  C CA  . VAL D 412  ? 0.5728 0.6137 0.5201 0.0778  0.0347  -0.0442 409  VAL A CA  
4180  C C   . VAL D 412  ? 0.6002 0.6316 0.5525 0.0717  0.0323  -0.0439 409  VAL A C   
4181  O O   . VAL D 412  ? 0.6230 0.6452 0.5766 0.0735  0.0296  -0.0494 409  VAL A O   
4182  C CB  . VAL D 412  ? 0.5369 0.5715 0.4766 0.0755  0.0347  -0.0457 409  VAL A CB  
4183  C CG1 . VAL D 412  ? 0.5156 0.5387 0.4547 0.0760  0.0318  -0.0525 409  VAL A CG1 
4184  C CG2 . VAL D 412  ? 0.5184 0.5618 0.4531 0.0821  0.0369  -0.0465 409  VAL A CG2 
4185  N N   . GLN D 413  ? 0.6410 0.6742 0.5948 0.0636  0.0328  -0.0371 410  GLN A N   
4186  C CA  . GLN D 413  ? 0.6967 0.7224 0.6552 0.0582  0.0307  -0.0363 410  GLN A CA  
4187  C C   . GLN D 413  ? 0.7231 0.7513 0.6880 0.0628  0.0300  -0.0375 410  GLN A C   
4188  O O   . GLN D 413  ? 0.7437 0.7616 0.7103 0.0624  0.0272  -0.0414 410  GLN A O   
4189  C CB  . GLN D 413  ? 0.7763 0.8025 0.7329 0.0490  0.0308  -0.0286 410  GLN A CB  
4190  C CG  . GLN D 413  ? 0.8592 0.8752 0.8044 0.0450  0.0298  -0.0276 410  GLN A CG  
4191  C CD  . GLN D 413  ? 0.9096 0.9194 0.8488 0.0354  0.0280  -0.0205 410  GLN A CD  
4192  O OE1 . GLN D 413  ? 0.9540 0.9537 0.8794 0.0316  0.0264  -0.0177 410  GLN A OE1 
4193  N NE2 . GLN D 413  ? 0.8930 0.9062 0.8402 0.0316  0.0275  -0.0176 410  GLN A NE2 
4194  N N   . ARG D 414  ? 0.7372 0.7798 0.7040 0.0673  0.0322  -0.0337 411  ARG A N   
4195  C CA  . ARG D 414  ? 0.7815 0.8260 0.7511 0.0745  0.0314  -0.0348 411  ARG A CA  
4196  C C   . ARG D 414  ? 0.7737 0.8052 0.7374 0.0841  0.0286  -0.0433 411  ARG A C   
4197  O O   . ARG D 414  ? 0.7952 0.8157 0.7574 0.0875  0.0255  -0.0460 411  ARG A O   
4198  C CB  . ARG D 414  ? 0.8604 0.9285 0.8321 0.0796  0.0346  -0.0285 411  ARG A CB  
4199  C CG  . ARG D 414  ? 0.9191 0.9986 0.8967 0.0694  0.0354  -0.0195 411  ARG A CG  
4200  C CD  . ARG D 414  ? 0.9511 1.0535 0.9282 0.0646  0.0381  -0.0111 411  ARG A CD  
4201  N NE  . ARG D 414  ? 0.9797 1.1041 0.9562 0.0774  0.0408  -0.0107 411  ARG A NE  
4202  C CZ  . ARG D 414  ? 0.9983 1.1480 0.9743 0.0750  0.0433  -0.0032 411  ARG A CZ  
4203  N NH1 . ARG D 414  ? 1.0042 1.1560 0.9784 0.0587  0.0427  0.0045  411  ARG A NH1 
4204  N NH2 . ARG D 414  ? 0.9990 1.1713 0.9743 0.0890  0.0459  -0.0032 411  ARG A NH2 
4205  N N   . SER D 415  ? 0.7598 0.7902 0.7182 0.0880  0.0290  -0.0476 412  SER A N   
4206  C CA  . SER D 415  ? 0.7744 0.7902 0.7247 0.0959  0.0253  -0.0557 412  SER A CA  
4207  C C   . SER D 415  ? 0.7700 0.7672 0.7196 0.0873  0.0204  -0.0593 412  SER A C   
4208  O O   . SER D 415  ? 0.7756 0.7566 0.7180 0.0902  0.0154  -0.0639 412  SER A O   
4209  C CB  . SER D 415  ? 0.7668 0.7873 0.7118 0.1011  0.0268  -0.0591 412  SER A CB  
4210  O OG  . SER D 415  ? 0.7447 0.7653 0.6919 0.0919  0.0278  -0.0582 412  SER A OG  
4211  N N   . LEU D 416  ? 0.7453 0.7447 0.7004 0.0767  0.0213  -0.0567 413  LEU A N   
4212  C CA  . LEU D 416  ? 0.7352 0.7241 0.6907 0.0684  0.0171  -0.0589 413  LEU A CA  
4213  C C   . LEU D 416  ? 0.7399 0.7215 0.6986 0.0638  0.0145  -0.0564 413  LEU A C   
4214  O O   . LEU D 416  ? 0.7531 0.7261 0.7109 0.0566  0.0102  -0.0578 413  LEU A O   
4215  C CB  . LEU D 416  ? 0.7185 0.7144 0.6768 0.0618  0.0190  -0.0568 413  LEU A CB  
4216  C CG  . LEU D 416  ? 0.7287 0.7292 0.6821 0.0656  0.0207  -0.0596 413  LEU A CG  
4217  C CD1 . LEU D 416  ? 0.7281 0.7330 0.6808 0.0615  0.0221  -0.0573 413  LEU A CD1 
4218  C CD2 . LEU D 416  ? 0.7463 0.7403 0.6945 0.0671  0.0166  -0.0661 413  LEU A CD2 
4219  N N   . LYS D 417  ? 0.7618 0.7487 0.7240 0.0671  0.0169  -0.0523 414  LYS A N   
4220  C CA  . LYS D 417  ? 0.8157 0.7958 0.7806 0.0633  0.0145  -0.0498 414  LYS A CA  
4221  C C   . LYS D 417  ? 0.9180 0.8808 0.8732 0.0695  0.0093  -0.0540 414  LYS A C   
4222  O O   . LYS D 417  ? 0.9752 0.9249 0.9286 0.0634  0.0048  -0.0537 414  LYS A O   
4223  C CB  . LYS D 417  ? 0.8243 0.8179 0.7961 0.0640  0.0185  -0.0433 414  LYS A CB  
4224  C CG  . LYS D 417  ? 0.8344 0.8369 0.8120 0.0551  0.0213  -0.0384 414  LYS A CG  
4225  C CD  . LYS D 417  ? 0.8708 0.8840 0.8536 0.0532  0.0236  -0.0315 414  LYS A CD  
4226  C CE  . LYS D 417  ? 0.9067 0.9237 0.8904 0.0442  0.0250  -0.0266 414  LYS A CE  
4227  N NZ  . LYS D 417  ? 0.9233 0.9497 0.9111 0.0399  0.0260  -0.0195 414  LYS A NZ  
4228  N N   . HIS D 418  ? 0.9582 0.9192 0.9047 0.0820  0.0093  -0.0577 415  HIS A N   
4229  C CA  . HIS D 418  ? 1.0316 0.9724 0.9638 0.0913  0.0037  -0.0619 415  HIS A CA  
4230  C C   . HIS D 418  ? 1.0748 1.0044 0.9933 0.0994  0.0006  -0.0689 415  HIS A C   
4231  O O   . HIS D 418  ? 1.0947 1.0230 1.0030 0.1151  0.0007  -0.0716 415  HIS A O   
4232  C CB  . HIS D 418  ? 1.0827 1.0331 1.0149 0.1037  0.0065  -0.0588 415  HIS A CB  
4233  C CG  . HIS D 418  ? 1.1127 1.0899 1.0503 0.1125  0.0132  -0.0562 415  HIS A CG  
4234  N ND1 . HIS D 418  ? 1.1260 1.1054 1.0551 0.1233  0.0137  -0.0606 415  HIS A ND1 
4235  C CD2 . HIS D 418  ? 1.1178 1.1215 1.0673 0.1109  0.0191  -0.0489 415  HIS A CD2 
4236  C CE1 . HIS D 418  ? 1.1295 1.1373 1.0660 0.1280  0.0201  -0.0557 415  HIS A CE1 
4237  N NE2 . HIS D 418  ? 1.1242 1.1468 1.0727 0.1197  0.0231  -0.0483 415  HIS A NE2 
4238  N N   . GLU D 419  ? 1.1167 1.0393 1.0339 0.0893  -0.0025 -0.0716 416  GLU A N   
4239  C CA  . GLU D 419  ? 1.1248 1.0320 1.0268 0.0944  -0.0074 -0.0785 416  GLU A CA  
4240  C C   . GLU D 419  ? 1.0624 0.9589 0.9623 0.0784  -0.0135 -0.0798 416  GLU A C   
4241  O O   . GLU D 419  ? 1.0459 0.9565 0.9592 0.0662  -0.0111 -0.0757 416  GLU A O   
4242  C CB  . GLU D 419  ? 1.1670 1.0924 1.0718 0.1035  -0.0016 -0.0800 416  GLU A CB  
4243  C CG  . GLU D 419  ? 1.1903 1.1303 1.1056 0.0930  0.0016  -0.0789 416  GLU A CG  
4244  C CD  . GLU D 419  ? 1.2305 1.1766 1.1408 0.1012  0.0035  -0.0830 416  GLU A CD  
4245  O OE1 . GLU D 419  ? 1.2523 1.1835 1.1512 0.1005  -0.0023 -0.0887 416  GLU A OE1 
4246  O OE2 . GLU D 419  ? 1.2357 1.2012 1.1524 0.1074  0.0102  -0.0801 416  GLU A OE2 
4247  N N   . ASP D 420  ? 0.9844 0.8563 0.8656 0.0789  -0.0219 -0.0854 417  ASP A N   
4248  C CA  . ASP D 420  ? 0.9165 0.7799 0.7938 0.0621  -0.0290 -0.0859 417  ASP A CA  
4249  C C   . ASP D 420  ? 0.8789 0.7595 0.7615 0.0606  -0.0260 -0.0881 417  ASP A C   
4250  O O   . ASP D 420  ? 0.9096 0.7888 0.7850 0.0729  -0.0246 -0.0928 417  ASP A O   
4251  C CB  . ASP D 420  ? 0.9377 0.7636 0.7891 0.0605  -0.0411 -0.0902 417  ASP A CB  
4252  C CG  . ASP D 420  ? 0.9547 0.7602 0.7976 0.0626  -0.0450 -0.0881 417  ASP A CG  
4253  O OD1 . ASP D 420  ? 0.9124 0.7318 0.7709 0.0549  -0.0411 -0.0821 417  ASP A OD1 
4254  O OD2 . ASP D 420  ? 1.0178 0.7918 0.8363 0.0732  -0.0522 -0.0927 417  ASP A OD2 
4255  N N   . ILE D 421  ? 0.8359 0.7343 0.7305 0.0469  -0.0249 -0.0846 418  ILE A N   
4256  C CA  . ILE D 421  ? 0.8327 0.7494 0.7323 0.0456  -0.0221 -0.0861 418  ILE A CA  
4257  C C   . ILE D 421  ? 0.8741 0.7796 0.7614 0.0339  -0.0318 -0.0886 418  ILE A C   
4258  O O   . ILE D 421  ? 0.9286 0.8265 0.8124 0.0193  -0.0388 -0.0855 418  ILE A O   
4259  C CB  . ILE D 421  ? 0.8353 0.7794 0.7525 0.0403  -0.0154 -0.0808 418  ILE A CB  
4260  C CG1 . ILE D 421  ? 0.8087 0.7584 0.7356 0.0466  -0.0085 -0.0768 418  ILE A CG1 
4261  C CG2 . ILE D 421  ? 0.8517 0.8136 0.7721 0.0446  -0.0111 -0.0827 418  ILE A CG2 
4262  C CD1 . ILE D 421  ? 0.7989 0.7522 0.7257 0.0609  -0.0025 -0.0783 418  ILE A CD1 
4263  N N   . ASN D 422  ? 0.8695 0.7747 0.7494 0.0390  -0.0328 -0.0937 419  ASN A N   
4264  C CA  . ASN D 422  ? 0.8666 0.7645 0.7350 0.0264  -0.0422 -0.0956 419  ASN A CA  
4265  C C   . ASN D 422  ? 0.8145 0.7438 0.6971 0.0137  -0.0403 -0.0908 419  ASN A C   
4266  O O   . ASN D 422  ? 0.7726 0.7269 0.6705 0.0197  -0.0311 -0.0885 419  ASN A O   
4267  C CB  . ASN D 422  ? 0.9103 0.7988 0.7659 0.0365  -0.0440 -0.1027 419  ASN A CB  
4268  C CG  . ASN D 422  ? 0.9324 0.8485 0.8013 0.0467  -0.0338 -0.1034 419  ASN A CG  
4269  O OD1 . ASN D 422  ? 0.9222 0.8605 0.7990 0.0396  -0.0325 -0.1018 419  ASN A OD1 
4270  N ND2 . ASN D 422  ? 0.9646 0.8801 0.8345 0.0636  -0.0270 -0.1054 419  ASN A ND2 
4271  N N   . LEU D 423  ? 0.8213 0.7488 0.6964 -0.0038 -0.0499 -0.0890 420  LEU A N   
4272  C CA  . LEU D 423  ? 0.7780 0.7394 0.6657 -0.0161 -0.0489 -0.0833 420  LEU A CA  
4273  C C   . LEU D 423  ? 0.7380 0.7262 0.6330 -0.0077 -0.0426 -0.0856 420  LEU A C   
4274  O O   . LEU D 423  ? 0.7313 0.7510 0.6391 -0.0084 -0.0374 -0.0815 420  LEU A O   
4275  C CB  . LEU D 423  ? 0.7642 0.7204 0.6408 -0.0385 -0.0615 -0.0799 420  LEU A CB  
4276  C CG  . LEU D 423  ? 0.7076 0.7030 0.5967 -0.0533 -0.0617 -0.0722 420  LEU A CG  
4277  C CD1 . LEU D 423  ? 0.6673 0.6786 0.5721 -0.0501 -0.0542 -0.0669 420  LEU A CD1 
4278  C CD2 . LEU D 423  ? 0.7210 0.7096 0.5969 -0.0781 -0.0755 -0.0677 420  LEU A CD2 
4279  N N   . GLN D 424  ? 0.7324 0.7081 0.6179 0.0018  -0.0430 -0.0921 421  GLN A N   
4280  C CA  . GLN D 424  ? 0.7696 0.7690 0.6604 0.0099  -0.0375 -0.0942 421  GLN A CA  
4281  C C   . GLN D 424  ? 0.7528 0.7661 0.6560 0.0250  -0.0257 -0.0932 421  GLN A C   
4282  O O   . GLN D 424  ? 0.7513 0.7909 0.6621 0.0281  -0.0208 -0.0914 421  GLN A O   
4283  C CB  . GLN D 424  ? 0.8353 0.8167 0.7117 0.0163  -0.0412 -0.1014 421  GLN A CB  
4284  C CG  . GLN D 424  ? 0.8746 0.8796 0.7548 0.0233  -0.0367 -0.1037 421  GLN A CG  
4285  C CD  . GLN D 424  ? 0.9162 0.9521 0.8017 0.0101  -0.0399 -0.0994 421  GLN A CD  
4286  O OE1 . GLN D 424  ? 0.9687 1.0021 0.8473 -0.0075 -0.0498 -0.0971 421  GLN A OE1 
4287  N NE2 . GLN D 424  ? 0.8735 0.9388 0.7695 0.0185  -0.0319 -0.0976 421  GLN A NE2 
4288  N N   . GLU D 425  ? 0.7296 0.7255 0.6332 0.0346  -0.0216 -0.0941 422  GLU A N   
4289  C CA  . GLU D 425  ? 0.7099 0.7167 0.6231 0.0460  -0.0117 -0.0920 422  GLU A CA  
4290  C C   . GLU D 425  ? 0.6823 0.7064 0.6059 0.0404  -0.0091 -0.0860 422  GLU A C   
4291  O O   . GLU D 425  ? 0.6543 0.6914 0.5826 0.0479  -0.0026 -0.0842 422  GLU A O   
4292  C CB  . GLU D 425  ? 0.7513 0.7398 0.6627 0.0553  -0.0088 -0.0929 422  GLU A CB  
4293  C CG  . GLU D 425  ? 0.7908 0.7892 0.7092 0.0656  0.0003  -0.0906 422  GLU A CG  
4294  C CD  . GLU D 425  ? 0.8669 0.8538 0.7845 0.0735  0.0030  -0.0901 422  GLU A CD  
4295  O OE1 . GLU D 425  ? 0.9351 0.9060 0.8479 0.0719  -0.0016 -0.0912 422  GLU A OE1 
4296  O OE2 . GLU D 425  ? 0.8546 0.8489 0.7750 0.0812  0.0094  -0.0882 422  GLU A OE2 
4297  N N   . ILE D 426  ? 0.6874 0.7102 0.6122 0.0275  -0.0147 -0.0827 423  ILE A N   
4298  C CA  . ILE D 426  ? 0.7035 0.7454 0.6375 0.0226  -0.0125 -0.0769 423  ILE A CA  
4299  C C   . ILE D 426  ? 0.7322 0.8036 0.6681 0.0218  -0.0121 -0.0757 423  ILE A C   
4300  O O   . ILE D 426  ? 0.7409 0.8292 0.6811 0.0289  -0.0067 -0.0733 423  ILE A O   
4301  C CB  . ILE D 426  ? 0.6643 0.6981 0.5986 0.0084  -0.0189 -0.0730 423  ILE A CB  
4302  C CG1 . ILE D 426  ? 0.6735 0.6783 0.6042 0.0121  -0.0192 -0.0744 423  ILE A CG1 
4303  C CG2 . ILE D 426  ? 0.5970 0.6529 0.5408 0.0043  -0.0164 -0.0668 423  ILE A CG2 
4304  C CD1 . ILE D 426  ? 0.6793 0.6719 0.6079 -0.0007 -0.0257 -0.0707 423  ILE A CD1 
4305  N N   . ILE D 427  ? 0.7446 0.8221 0.6752 0.0138  -0.0183 -0.0774 424  ILE A N   
4306  C CA  . ILE D 427  ? 0.7483 0.8583 0.6806 0.0131  -0.0183 -0.0759 424  ILE A CA  
4307  C C   . ILE D 427  ? 0.7518 0.8679 0.6824 0.0305  -0.0112 -0.0795 424  ILE A C   
4308  O O   . ILE D 427  ? 0.7500 0.8902 0.6823 0.0378  -0.0074 -0.0775 424  ILE A O   
4309  C CB  . ILE D 427  ? 0.7651 0.8796 0.6911 -0.0017 -0.0276 -0.0763 424  ILE A CB  
4310  C CG1 . ILE D 427  ? 0.7565 0.8647 0.6816 -0.0211 -0.0357 -0.0712 424  ILE A CG1 
4311  C CG2 . ILE D 427  ? 0.7789 0.9316 0.7069 -0.0012 -0.0273 -0.0746 424  ILE A CG2 
4312  C CD1 . ILE D 427  ? 0.7615 0.8699 0.6770 -0.0393 -0.0469 -0.0705 424  ILE A CD1 
4313  N N   . SER D 428  ? 0.7518 0.8459 0.6771 0.0382  -0.0095 -0.0847 425  SER A N   
4314  C CA  . SER D 428  ? 0.7565 0.8539 0.6786 0.0532  -0.0034 -0.0877 425  SER A CA  
4315  C C   . SER D 428  ? 0.7583 0.8541 0.6822 0.0632  0.0035  -0.0850 425  SER A C   
4316  O O   . SER D 428  ? 0.7702 0.8713 0.6891 0.0746  0.0077  -0.0859 425  SER A O   
4317  C CB  . SER D 428  ? 0.7796 0.8553 0.6955 0.0584  -0.0034 -0.0930 425  SER A CB  
4318  O OG  . SER D 428  ? 0.8173 0.8907 0.7276 0.0502  -0.0107 -0.0962 425  SER A OG  
4319  N N   . ALA D 429  ? 0.7352 0.8218 0.6641 0.0587  0.0039  -0.0815 426  ALA A N   
4320  C CA  . ALA D 429  ? 0.7150 0.7967 0.6438 0.0663  0.0092  -0.0786 426  ALA A CA  
4321  C C   . ALA D 429  ? 0.7095 0.8086 0.6403 0.0655  0.0093  -0.0744 426  ALA A C   
4322  O O   . ALA D 429  ? 0.6873 0.7849 0.6127 0.0747  0.0130  -0.0729 426  ALA A O   
4323  C CB  . ALA D 429  ? 0.6991 0.7596 0.6313 0.0636  0.0102  -0.0775 426  ALA A CB  
4324  N N   . ALA D 430  ? 0.7199 0.8349 0.6563 0.0548  0.0049  -0.0721 427  ALA A N   
4325  C CA  . ALA D 430  ? 0.7352 0.8704 0.6743 0.0541  0.0050  -0.0674 427  ALA A CA  
4326  C C   . ALA D 430  ? 0.7665 0.9343 0.7025 0.0590  0.0044  -0.0668 427  ALA A C   
4327  O O   . ALA D 430  ? 0.7823 0.9674 0.7159 0.0665  0.0062  -0.0638 427  ALA A O   
4328  C CB  . ALA D 430  ? 0.7341 0.8702 0.6812 0.0383  0.0004  -0.0636 427  ALA A CB  
4329  N N   . GLY D 431  ? 0.7823 0.9600 0.7171 0.0559  0.0016  -0.0694 428  GLY A N   
4330  C CA  . GLY D 431  ? 0.7982 1.0108 0.7305 0.0603  0.0008  -0.0685 428  GLY A CA  
4331  C C   . GLY D 431  ? 0.8352 1.0738 0.7743 0.0423  -0.0058 -0.0644 428  GLY A C   
4332  O O   . GLY D 431  ? 0.8477 1.0747 0.7920 0.0263  -0.0102 -0.0620 428  GLY A O   
4333  N N   . LYS D 432  ? 0.8794 1.1544 0.8170 0.0448  -0.0070 -0.0631 429  LYS A N   
4334  C CA  . LYS D 432  ? 0.9060 1.2111 0.8489 0.0259  -0.0141 -0.0580 429  LYS A CA  
4335  C C   . LYS D 432  ? 0.9439 1.2716 0.8936 0.0170  -0.0156 -0.0502 429  LYS A C   
4336  O O   . LYS D 432  ? 0.9718 1.3165 0.9259 -0.0039 -0.0227 -0.0446 429  LYS A O   
4337  C CB  . LYS D 432  ? 0.8824 1.2262 0.8222 0.0317  -0.0147 -0.0579 429  LYS A CB  
4338  C CG  . LYS D 432  ? 0.8564 1.2352 0.7933 0.0512  -0.0094 -0.0554 429  LYS A CG  
4339  C CD  . LYS D 432  ? 0.8459 1.2659 0.7795 0.0574  -0.0103 -0.0550 429  LYS A CD  
4340  C CE  . LYS D 432  ? 0.8306 1.2880 0.7586 0.0791  -0.0057 -0.0523 429  LYS A CE  
4341  N NZ  . LYS D 432  ? 0.8165 1.3168 0.7405 0.0875  -0.0063 -0.0519 429  LYS A NZ  
4342  N N   . GLU D 433  ? 0.9675 1.2948 0.9166 0.0317  -0.0098 -0.0492 430  GLU A N   
4343  C CA  . GLU D 433  ? 0.9643 1.3143 0.9196 0.0251  -0.0107 -0.0418 430  GLU A CA  
4344  C C   . GLU D 433  ? 0.9274 1.2481 0.8883 0.0069  -0.0144 -0.0397 430  GLU A C   
4345  O O   . GLU D 433  ? 0.9200 1.2602 0.8868 -0.0040 -0.0169 -0.0327 430  GLU A O   
4346  C CB  . GLU D 433  ? 1.0137 1.3687 0.9633 0.0479  -0.0040 -0.0421 430  GLU A CB  
4347  C CG  . GLU D 433  ? 1.0680 1.4627 1.0100 0.0664  -0.0015 -0.0419 430  GLU A CG  
4348  C CD  . GLU D 433  ? 1.1039 1.5548 1.0531 0.0543  -0.0059 -0.0343 430  GLU A CD  
4349  O OE1 . GLU D 433  ? 1.1100 1.5777 1.0601 0.0469  -0.0093 -0.0347 430  GLU A OE1 
4350  O OE2 . GLU D 433  ? 1.1154 1.5950 1.0691 0.0515  -0.0064 -0.0274 430  GLU A OE2 
4351  N N   . LEU D 434  ? 0.8873 1.1637 0.8460 0.0045  -0.0148 -0.0453 431  LEU A N   
4352  C CA  . LEU D 434  ? 0.8601 1.1089 0.8216 -0.0122 -0.0195 -0.0435 431  LEU A CA  
4353  C C   . LEU D 434  ? 0.8779 1.1336 0.8382 -0.0353 -0.0292 -0.0402 431  LEU A C   
4354  O O   . LEU D 434  ? 0.8571 1.1105 0.8192 -0.0527 -0.0348 -0.0345 431  LEU A O   
4355  C CB  . LEU D 434  ? 0.8244 1.0267 0.7822 -0.0050 -0.0168 -0.0503 431  LEU A CB  
4356  C CG  . LEU D 434  ? 0.7938 0.9640 0.7519 -0.0180 -0.0213 -0.0495 431  LEU A CG  
4357  C CD1 . LEU D 434  ? 0.7686 0.9094 0.7270 -0.0054 -0.0152 -0.0529 431  LEU A CD1 
4358  C CD2 . LEU D 434  ? 0.8141 0.9637 0.7645 -0.0299 -0.0290 -0.0526 431  LEU A CD2 
4359  N N   . SER D 435  ? 0.9037 1.1658 0.8591 -0.0365 -0.0320 -0.0435 432  SER A N   
4360  C CA  . SER D 435  ? 0.9241 1.1921 0.8752 -0.0599 -0.0426 -0.0400 432  SER A CA  
4361  C C   . SER D 435  ? 0.9326 1.2474 0.8897 -0.0750 -0.0466 -0.0294 432  SER A C   
4362  O O   . SER D 435  ? 0.9671 1.2783 0.9216 -0.0990 -0.0559 -0.0234 432  SER A O   
4363  C CB  . SER D 435  ? 0.9081 1.1808 0.8532 -0.0565 -0.0442 -0.0451 432  SER A CB  
4364  O OG  . SER D 435  ? 0.8806 1.1145 0.8206 -0.0414 -0.0398 -0.0542 432  SER A OG  
4365  N N   . GLU D 436  ? 0.9214 1.2804 0.8847 -0.0608 -0.0401 -0.0266 433  GLU A N   
4366  C CA  . GLU D 436  ? 0.9357 1.3457 0.9054 -0.0723 -0.0429 -0.0159 433  GLU A CA  
4367  C C   . GLU D 436  ? 0.9110 1.3099 0.8851 -0.0804 -0.0433 -0.0107 433  GLU A C   
4368  O O   . GLU D 436  ? 0.9339 1.3566 0.9105 -0.1022 -0.0502 -0.0011 433  GLU A O   
4369  C CB  . GLU D 436  ? 0.9603 1.4179 0.9328 -0.0498 -0.0352 -0.0151 433  GLU A CB  
4370  C CG  . GLU D 436  ? 1.0180 1.4966 0.9863 -0.0430 -0.0354 -0.0185 433  GLU A CG  
4371  C CD  . GLU D 436  ? 1.0913 1.5921 1.0592 -0.0710 -0.0461 -0.0125 433  GLU A CD  
4372  O OE1 . GLU D 436  ? 1.1170 1.5824 1.0782 -0.0811 -0.0515 -0.0177 433  GLU A OE1 
4373  O OE2 . GLU D 436  ? 1.1049 1.6587 1.0779 -0.0831 -0.0497 -0.0022 433  GLU A OE2 
4374  N N   . ALA D 437  ? 0.8766 1.2404 0.8510 -0.0643 -0.0366 -0.0162 434  ALA A N   
4375  C CA  . ALA D 437  ? 0.8210 1.1697 0.7991 -0.0717 -0.0371 -0.0120 434  ALA A CA  
4376  C C   . ALA D 437  ? 0.7931 1.1039 0.7658 -0.0949 -0.0465 -0.0111 434  ALA A C   
4377  O O   . ALA D 437  ? 0.8216 1.1352 0.7956 -0.1124 -0.0517 -0.0035 434  ALA A O   
4378  C CB  . ALA D 437  ? 0.7691 1.0897 0.7478 -0.0492 -0.0281 -0.0181 434  ALA A CB  
4379  N N   . PHE D 438  ? 0.7489 1.0228 0.7132 -0.0946 -0.0491 -0.0187 435  PHE A N   
4380  C CA  . PHE D 438  ? 0.7538 0.9872 0.7076 -0.1139 -0.0591 -0.0188 435  PHE A CA  
4381  C C   . PHE D 438  ? 0.7907 1.0466 0.7392 -0.1420 -0.0708 -0.0103 435  PHE A C   
4382  O O   . PHE D 438  ? 0.8539 1.0909 0.7953 -0.1628 -0.0798 -0.0048 435  PHE A O   
4383  C CB  . PHE D 438  ? 0.8017 0.9937 0.7459 -0.1039 -0.0590 -0.0293 435  PHE A CB  
4384  C CG  . PHE D 438  ? 0.8725 1.0126 0.8036 -0.1138 -0.0667 -0.0318 435  PHE A CG  
4385  C CD1 . PHE D 438  ? 0.9224 1.0469 0.8385 -0.1363 -0.0799 -0.0294 435  PHE A CD1 
4386  C CD2 . PHE D 438  ? 0.8844 0.9906 0.8159 -0.1001 -0.0614 -0.0364 435  PHE A CD2 
4387  C CE1 . PHE D 438  ? 0.9468 1.0192 0.8461 -0.1429 -0.0878 -0.0322 435  PHE A CE1 
4388  C CE2 . PHE D 438  ? 0.9189 0.9785 0.8362 -0.1060 -0.0685 -0.0389 435  PHE A CE2 
4389  C CZ  . PHE D 438  ? 0.9443 0.9851 0.8444 -0.1264 -0.0818 -0.0372 435  PHE A CZ  
4390  N N   . LYS D 439  ? 0.7873 1.0837 0.7377 -0.1436 -0.0716 -0.0084 436  LYS A N   
4391  C CA  . LYS D 439  ? 0.8214 1.1460 0.7671 -0.1722 -0.0831 0.0011  436  LYS A CA  
4392  C C   . LYS D 439  ? 0.8468 1.2106 0.8011 -0.1857 -0.0844 0.0135  436  LYS A C   
4393  O O   . LYS D 439  ? 0.8919 1.2514 0.8388 -0.2141 -0.0957 0.0220  436  LYS A O   
4394  C CB  . LYS D 439  ? 0.8377 1.2039 0.7854 -0.1685 -0.0824 0.0007  436  LYS A CB  
4395  C CG  . LYS D 439  ? 0.8712 1.2023 0.8084 -0.1610 -0.0838 -0.0099 436  LYS A CG  
4396  C CD  . LYS D 439  ? 0.8720 1.2494 0.8127 -0.1552 -0.0820 -0.0099 436  LYS A CD  
4397  C CE  . LYS D 439  ? 0.8838 1.2280 0.8154 -0.1436 -0.0814 -0.0211 436  LYS A CE  
4398  N NZ  . LYS D 439  ? 0.9207 1.2182 0.8346 -0.1649 -0.0944 -0.0230 436  LYS A NZ  
4399  N N   . GLN D 440  ? 0.8162 1.2174 0.7840 -0.1655 -0.0734 0.0148  437  GLN A N   
4400  C CA  . GLN D 440  ? 0.7846 1.2299 0.7609 -0.1753 -0.0737 0.0267  437  GLN A CA  
4401  C C   . GLN D 440  ? 0.7846 1.1921 0.7584 -0.1868 -0.0771 0.0295  437  GLN A C   
4402  O O   . GLN D 440  ? 0.7777 1.2040 0.7510 -0.2112 -0.0848 0.0409  437  GLN A O   
4403  C CB  . GLN D 440  ? 0.7393 1.2267 0.7266 -0.1467 -0.0613 0.0259  437  GLN A CB  
4404  N N   . LYS D 441  ? 0.7973 1.1530 0.7690 -0.1700 -0.0716 0.0198  438  LYS A N   
4405  C CA  . LYS D 441  ? 0.8339 1.1533 0.8028 -0.1784 -0.0744 0.0219  438  LYS A CA  
4406  C C   . LYS D 441  ? 0.8882 1.1697 0.8407 -0.2063 -0.0887 0.0246  438  LYS A C   
4407  O O   . LYS D 441  ? 0.9244 1.1955 0.8726 -0.2247 -0.0953 0.0322  438  LYS A O   
4408  C CB  . LYS D 441  ? 0.8399 1.1170 0.8103 -0.1533 -0.0653 0.0112  438  LYS A CB  
4409  C CG  . LYS D 441  ? 0.8490 1.1000 0.8202 -0.1559 -0.0651 0.0137  438  LYS A CG  
4410  C CD  . LYS D 441  ? 0.8406 1.1309 0.8249 -0.1451 -0.0571 0.0188  438  LYS A CD  
4411  C CE  . LYS D 441  ? 0.8665 1.1335 0.8518 -0.1493 -0.0574 0.0220  438  LYS A CE  
4412  N NZ  . LYS D 441  ? 0.9136 1.1801 0.8925 -0.1790 -0.0689 0.0321  438  LYS A NZ  
4413  N N   . THR D 442  ? 0.9286 1.1864 0.8693 -0.2095 -0.0941 0.0185  439  THR A N   
4414  C CA  . THR D 442  ? 0.9924 1.2073 0.9120 -0.2344 -0.1091 0.0200  439  THR A CA  
4415  C C   . THR D 442  ? 1.0274 1.2776 0.9428 -0.2679 -0.1209 0.0342  439  THR A C   
4416  O O   . THR D 442  ? 1.0579 1.2822 0.9599 -0.2912 -0.1319 0.0410  439  THR A O   
4417  C CB  . THR D 442  ? 1.0211 1.2049 0.9279 -0.2280 -0.1120 0.0098  439  THR A CB  
4418  O OG1 . THR D 442  ? 1.0274 1.1791 0.9375 -0.1987 -0.1016 -0.0021 439  THR A OG1 
4419  C CG2 . THR D 442  ? 1.0704 1.2054 0.9505 -0.2527 -0.1288 0.0109  439  THR A CG2 
4420  N N   . SER D 443  ? 1.0105 1.3212 0.9361 -0.2711 -0.1192 0.0395  440  SER A N   
4421  C CA  . SER D 443  ? 1.0200 1.3740 0.9433 -0.3038 -0.1301 0.0546  440  SER A CA  
4422  C C   . SER D 443  ? 0.9755 1.3597 0.9096 -0.3107 -0.1278 0.0657  440  SER A C   
4423  O O   . SER D 443  ? 1.0072 1.4013 0.9333 -0.3427 -0.1397 0.0785  440  SER A O   
4424  C CB  . SER D 443  ? 1.0184 1.4370 0.9516 -0.3021 -0.1275 0.0578  440  SER A CB  
4425  O OG  . SER D 443  ? 0.9891 1.4580 0.9430 -0.2748 -0.1126 0.0573  440  SER A OG  
4426  N N   . GLU D 444  ? 0.9127 1.3108 0.8634 -0.2820 -0.1133 0.0614  441  GLU A N   
4427  C CA  . GLU D 444  ? 0.8905 1.3152 0.8510 -0.2856 -0.1104 0.0709  441  GLU A CA  
4428  C C   . GLU D 444  ? 0.8755 1.2437 0.8223 -0.3034 -0.1193 0.0732  441  GLU A C   
4429  O O   . GLU D 444  ? 0.8391 1.2254 0.7841 -0.3277 -0.1266 0.0861  441  GLU A O   
4430  C CB  . GLU D 444  ? 0.9169 1.3572 0.8936 -0.2494 -0.0940 0.0639  441  GLU A CB  
4431  C CG  . GLU D 444  ? 0.9733 1.4525 0.9613 -0.2488 -0.0896 0.0736  441  GLU A CG  
4432  C CD  . GLU D 444  ? 1.0007 1.4793 0.9991 -0.2132 -0.0751 0.0652  441  GLU A CD  
4433  O OE1 . GLU D 444  ? 1.0008 1.4245 0.9960 -0.2021 -0.0720 0.0566  441  GLU A OE1 
4434  O OE2 . GLU D 444  ? 1.0064 1.5391 1.0142 -0.1962 -0.0674 0.0673  441  GLU A OE2 
4435  N N   . ILE D 445  ? 0.9011 1.2016 0.8371 -0.2908 -0.1189 0.0610  442  ILE A N   
4436  C CA  . ILE D 445  ? 0.9272 1.1698 0.8469 -0.3042 -0.1275 0.0619  442  ILE A CA  
4437  C C   . ILE D 445  ? 0.9907 1.2113 0.8865 -0.3402 -0.1463 0.0694  442  ILE A C   
4438  O O   . ILE D 445  ? 1.0327 1.2380 0.9168 -0.3642 -0.1564 0.0791  442  ILE A O   
4439  C CB  . ILE D 445  ? 0.8757 1.0571 0.7896 -0.2783 -0.1217 0.0468  442  ILE A CB  
4440  C CG1 . ILE D 445  ? 0.8180 1.0183 0.7532 -0.2473 -0.1050 0.0414  442  ILE A CG1 
4441  C CG2 . ILE D 445  ? 0.8874 1.0060 0.7800 -0.2908 -0.1321 0.0471  442  ILE A CG2 
4442  C CD1 . ILE D 445  ? 0.8077 0.9568 0.7394 -0.2225 -0.0986 0.0280  442  ILE A CD1 
4443  N N   . LEU D 446  ? 1.0229 1.2397 0.9089 -0.3454 -0.1519 0.0655  443  LEU A N   
4444  C CA  . LEU D 446  ? 1.0637 1.2545 0.9231 -0.3803 -0.1711 0.0721  443  LEU A CA  
4445  C C   . LEU D 446  ? 1.0561 1.3045 0.9191 -0.4138 -0.1793 0.0906  443  LEU A C   
4446  O O   . LEU D 446  ? 1.0753 1.2977 0.9159 -0.4471 -0.1958 0.1003  443  LEU A O   
4447  C CB  . LEU D 446  ? 1.0885 1.2676 0.9380 -0.3768 -0.1745 0.0636  443  LEU A CB  
4448  C CG  . LEU D 446  ? 1.1227 1.2329 0.9583 -0.3525 -0.1723 0.0469  443  LEU A CG  
4449  C CD1 . LEU D 446  ? 1.1345 1.2451 0.9643 -0.3475 -0.1739 0.0392  443  LEU A CD1 
4450  C CD2 . LEU D 446  ? 1.1746 1.2104 0.9782 -0.3675 -0.1869 0.0465  443  LEU A CD2 
4451  N N   . SER D 447  ? 1.0442 1.3714 0.9335 -0.4055 -0.1687 0.0964  444  SER A N   
4452  C CA  . SER D 447  ? 1.0587 1.4505 0.9535 -0.4354 -0.1754 0.1150  444  SER A CA  
4453  C C   . SER D 447  ? 1.0546 1.4422 0.9501 -0.4466 -0.1770 0.1245  444  SER A C   
4454  O O   . SER D 447  ? 1.0832 1.4764 0.9651 -0.4761 -0.1866 0.1397  444  SER A O   
4455  C CB  . SER D 447  ? 1.0506 1.5290 0.9720 -0.4182 -0.1626 0.1179  444  SER A CB  
4456  O OG  . SER D 447  ? 1.0518 1.5420 0.9929 -0.3819 -0.1452 0.1105  444  SER A OG  
4457  N N   . HIS D 448  ? 1.0156 1.3856 0.9233 -0.4167 -0.1638 0.1161  445  HIS A N   
4458  C CA  . HIS D 448  ? 1.0170 1.3807 0.9255 -0.4251 -0.1647 0.1242  445  HIS A CA  
4459  C C   . HIS D 448  ? 1.0814 1.3695 0.9593 -0.4501 -0.1812 0.1259  445  HIS A C   
4460  O O   . HIS D 448  ? 1.0351 1.3263 0.9044 -0.4773 -0.1905 0.1396  445  HIS A O   
4461  C CB  . HIS D 448  ? 0.9912 1.3488 0.9177 -0.3868 -0.1474 0.1138  445  HIS A CB  
4462  C CG  . HIS D 448  ? 0.9521 1.3864 0.9049 -0.3667 -0.1334 0.1167  445  HIS A CG  
4463  N ND1 . HIS D 448  ? 0.9175 1.3546 0.8845 -0.3282 -0.1178 0.1040  445  HIS A ND1 
4464  C CD2 . HIS D 448  ? 0.9410 1.4513 0.9058 -0.3789 -0.1331 0.1312  445  HIS A CD2 
4465  C CE1 . HIS D 448  ? 0.8862 1.3935 0.8706 -0.3163 -0.1090 0.1096  445  HIS A CE1 
4466  N NE2 . HIS D 448  ? 0.8993 1.4545 0.8837 -0.3455 -0.1175 0.1260  445  HIS A NE2 
4467  N N   . ALA D 449  ? 1.2491 1.4678 1.1081 -0.4400 -0.1849 0.1122  446  ALA A N   
4468  C CA  . ALA D 449  ? 1.3746 1.5172 1.1988 -0.4616 -0.2020 0.1129  446  ALA A CA  
4469  C C   . ALA D 449  ? 1.4471 1.5927 1.2481 -0.4989 -0.2187 0.1259  446  ALA A C   
4470  O O   . ALA D 449  ? 1.4986 1.6035 1.2726 -0.5174 -0.2290 0.1353  446  ALA A O   
4471  C CB  . ALA D 449  ? 1.3430 1.4143 1.1517 -0.4363 -0.2006 0.0947  446  ALA A CB  
4472  N N   . HIS D 450  ? 1.4583 1.6479 1.2670 -0.5011 -0.2170 0.1271  447  HIS A N   
4473  C CA  . HIS D 450  ? 1.5024 1.6986 1.2898 -0.5274 -0.2266 0.1410  447  HIS A CA  
4474  C C   . HIS D 450  ? 1.4859 1.7382 1.2804 -0.5434 -0.2237 0.1611  447  HIS A C   
4475  O O   . HIS D 450  ? 1.5353 1.7687 1.3027 -0.5694 -0.2350 0.1750  447  HIS A O   
4476  C CB  . HIS D 450  ? 1.5248 1.7574 1.3205 -0.5239 -0.2243 0.1369  447  HIS A CB  
4477  C CG  . HIS D 450  ? 1.6029 1.8779 1.3904 -0.5481 -0.2285 0.1543  447  HIS A CG  
4478  N ND1 . HIS D 450  ? 1.6933 1.9254 1.4450 -0.5765 -0.2434 0.1658  447  HIS A ND1 
4479  C CD2 . HIS D 450  ? 1.6038 1.9604 1.4120 -0.5477 -0.2198 0.1627  447  HIS A CD2 
4480  C CE1 . HIS D 450  ? 1.7111 1.9977 1.4628 -0.5946 -0.2438 0.1810  447  HIS A CE1 
4481  N NE2 . HIS D 450  ? 1.6600 2.0233 1.4460 -0.5771 -0.2293 0.1793  447  HIS A NE2 
4482  N N   . ALA D 451  ? 1.3983 1.7191 1.2265 -0.5274 -0.2092 0.1631  448  ALA A N   
4483  C CA  . ALA D 451  ? 1.3358 1.7125 1.1707 -0.5386 -0.2054 0.1813  448  ALA A CA  
4484  C C   . ALA D 451  ? 1.2941 1.6320 1.1173 -0.5461 -0.2098 0.1866  448  ALA A C   
4485  O O   . ALA D 451  ? 1.3190 1.6926 1.1403 -0.5597 -0.2099 0.2029  448  ALA A O   
4486  C CB  . ALA D 451  ? 1.2439 1.7048 1.1157 -0.5149 -0.1882 0.1808  448  ALA A CB  
4487  N N   . ALA D 452  ? 1.2404 1.5075 1.0544 -0.5368 -0.2136 0.1735  449  ALA A N   
4488  C CA  . ALA D 452  ? 1.2300 1.4550 1.0311 -0.5421 -0.2181 0.1774  449  ALA A CA  
4489  C C   . ALA D 452  ? 1.2938 1.4423 1.0508 -0.5642 -0.2360 0.1817  449  ALA A C   
4490  O O   . ALA D 452  ? 1.2983 1.4269 1.0390 -0.5771 -0.2422 0.1920  449  ALA A O   
4491  C CB  . ALA D 452  ? 1.1998 1.3950 1.0167 -0.5165 -0.2105 0.1612  449  ALA A CB  
4492  N N   . LEU D 453  ? 1.3513 1.4558 1.0868 -0.5680 -0.2449 0.1742  450  LEU A N   
4493  C CA  . LEU D 453  ? 1.4296 1.4576 1.1191 -0.5866 -0.2627 0.1778  450  LEU A CA  
4494  C C   . LEU D 453  ? 1.5237 1.5772 1.1936 -0.6182 -0.2721 0.1993  450  LEU A C   
4495  O O   . LEU D 453  ? 1.5873 1.5891 1.2214 -0.6357 -0.2861 0.2075  450  LEU A O   
4496  C CB  . LEU D 453  ? 1.4112 1.3868 1.0818 -0.5801 -0.2695 0.1637  450  LEU A CB  
4497  C CG  . LEU D 453  ? 1.3614 1.2756 1.0293 -0.5534 -0.2675 0.1433  450  LEU A CG  
4498  C CD1 . LEU D 453  ? 1.3785 1.2380 1.0202 -0.5492 -0.2765 0.1314  450  LEU A CD1 
4499  C CD2 . LEU D 453  ? 1.3697 1.2262 1.0160 -0.5524 -0.2735 0.1444  450  LEU A CD2 
4500  N N   . ASP D 454  ? 1.5919 1.7241 1.2826 -0.6254 -0.2652 0.2089  451  ASP A N   
4501  C CA  . ASP D 454  ? 1.6560 1.8202 1.3290 -0.6558 -0.2733 0.2305  451  ASP A CA  
4502  C C   . ASP D 454  ? 1.6497 1.8683 1.3377 -0.6602 -0.2669 0.2447  451  ASP A C   
4503  O O   . ASP D 454  ? 1.6981 1.9308 1.3650 -0.6869 -0.2761 0.2635  451  ASP A O   
4504  C CB  . ASP D 454  ? 1.6610 1.8827 1.3444 -0.6623 -0.2698 0.2350  451  ASP A CB  
4505  C CG  . ASP D 454  ? 1.6353 1.9318 1.3645 -0.6361 -0.2506 0.2273  451  ASP A CG  
4506  O OD1 . ASP D 454  ? 1.6336 1.9250 1.3850 -0.6113 -0.2409 0.2148  451  ASP A OD1 
4507  O OD2 . ASP D 454  ? 1.6274 1.9872 1.3687 -0.6397 -0.2454 0.2338  451  ASP A OD2 
4508  N N   . GLN D 455  ? 1.5203 1.7692 1.2422 -0.6352 -0.2522 0.2365  452  GLN A N   
4509  C CA  . GLN D 455  ? 1.4741 1.7705 1.2095 -0.6364 -0.2461 0.2485  452  GLN A CA  
4510  C C   . GLN D 455  ? 1.5073 1.7385 1.2149 -0.6476 -0.2578 0.2522  452  GLN A C   
4511  O O   . GLN D 455  ? 1.5052 1.6735 1.2086 -0.6325 -0.2587 0.2377  452  GLN A O   
4512  C CB  . GLN D 455  ? 1.3993 1.7422 1.1771 -0.6046 -0.2274 0.2377  452  GLN A CB  
4513  C CG  . GLN D 455  ? 1.3815 1.7807 1.1755 -0.6023 -0.2196 0.2494  452  GLN A CG  
4514  C CD  . GLN D 455  ? 1.3285 1.7564 1.1590 -0.5698 -0.2030 0.2371  452  GLN A CD  
4515  O OE1 . GLN D 455  ? 1.3100 1.6893 1.1464 -0.5531 -0.2009 0.2209  452  GLN A OE1 
4516  N NE2 . GLN D 455  ? 1.3064 1.8132 1.1593 -0.5599 -0.1915 0.2452  452  GLN A NE2 
4517  N N   . PRO D 456  ? 1.5359 1.7794 1.2225 -0.6730 -0.2671 0.2712  453  PRO A N   
4518  C CA  . PRO D 456  ? 1.5784 1.7567 1.2346 -0.6843 -0.2799 0.2749  453  PRO A CA  
4519  C C   . PRO D 456  ? 1.5301 1.7187 1.2092 -0.6658 -0.2698 0.2709  453  PRO A C   
4520  O O   . PRO D 456  ? 1.4949 1.7563 1.2078 -0.6538 -0.2556 0.2740  453  PRO A O   
4521  C CB  . PRO D 456  ? 1.6239 1.8249 1.2524 -0.7188 -0.2928 0.2981  453  PRO A CB  
4522  C CG  . PRO D 456  ? 1.5776 1.8785 1.2362 -0.7176 -0.2801 0.3075  453  PRO A CG  
4523  C CD  . PRO D 456  ? 1.5311 1.8481 1.2178 -0.6933 -0.2674 0.2907  453  PRO A CD  
4524  N N   . LEU D 457  ? 1.5316 1.6446 1.1899 -0.6625 -0.2776 0.2640  454  LEU A N   
4525  C CA  . LEU D 457  ? 1.5031 1.6166 1.1781 -0.6475 -0.2701 0.2610  454  LEU A CA  
4526  C C   . LEU D 457  ? 1.5215 1.6752 1.1903 -0.6672 -0.2743 0.2807  454  LEU A C   
4527  O O   . LEU D 457  ? 1.5720 1.7278 1.2122 -0.6953 -0.2877 0.2961  454  LEU A O   
4528  C CB  . LEU D 457  ? 1.5574 1.5776 1.2080 -0.6386 -0.2781 0.2487  454  LEU A CB  
4529  C CG  . LEU D 457  ? 1.5517 1.5379 1.2182 -0.6096 -0.2691 0.2270  454  LEU A CG  
4530  C CD1 . LEU D 457  ? 1.4754 1.5304 1.1914 -0.5874 -0.2489 0.2212  454  LEU A CD1 
4531  C CD2 . LEU D 457  ? 1.5965 1.5513 1.2461 -0.6117 -0.2756 0.2193  454  LEU A CD2 
4532  N N   . PRO D 458  ? 1.4875 1.6743 1.1818 -0.6532 -0.2635 0.2809  455  PRO A N   
4533  C CA  . PRO D 458  ? 1.5063 1.7302 1.1942 -0.6706 -0.2679 0.2991  455  PRO A CA  
4534  C C   . PRO D 458  ? 1.5629 1.7151 1.2102 -0.6889 -0.2857 0.3045  455  PRO A C   
4535  O O   . PRO D 458  ? 1.6179 1.6903 1.2408 -0.6860 -0.2943 0.2937  455  PRO A O   
4536  C CB  . PRO D 458  ? 1.4311 1.7029 1.1586 -0.6455 -0.2504 0.2944  455  PRO A CB  
4537  C CG  . PRO D 458  ? 1.3897 1.6122 1.1303 -0.6196 -0.2428 0.2736  455  PRO A CG  
4538  C CD  . PRO D 458  ? 1.4173 1.6127 1.1474 -0.6213 -0.2469 0.2654  455  PRO A CD  
4539  N N   . THR D 459  ? 1.5574 1.7375 1.1956 -0.7065 -0.2916 0.3210  456  THR A N   
4540  C CA  . THR D 459  ? 1.6099 1.7251 1.2077 -0.7250 -0.3096 0.3272  456  THR A CA  
4541  C C   . THR D 459  ? 1.5975 1.6717 1.2032 -0.7045 -0.3047 0.3160  456  THR A C   
4542  O O   . THR D 459  ? 1.6367 1.6304 1.2103 -0.7063 -0.3167 0.3104  456  THR A O   
4543  C CB  . THR D 459  ? 1.6444 1.8055 1.2266 -0.7543 -0.3195 0.3503  456  THR A CB  
4544  O OG1 . THR D 459  ? 1.6038 1.8429 1.2228 -0.7425 -0.3049 0.3552  456  THR A OG1 
4545  C CG2 . THR D 459  ? 1.6655 1.8578 1.2325 -0.7778 -0.3269 0.3626  456  THR A CG2 
4546  N N   . THR D 460  ? 1.5468 1.6745 1.1930 -0.6840 -0.2875 0.3128  457  THR A N   
4547  C CA  . THR D 460  ? 1.5306 1.6270 1.1875 -0.6644 -0.2813 0.3032  457  THR A CA  
4548  C C   . THR D 460  ? 1.4601 1.5956 1.1628 -0.6333 -0.2600 0.2900  457  THR A C   
4549  O O   . THR D 460  ? 1.4020 1.5954 1.1285 -0.6272 -0.2501 0.2898  457  THR A O   
4550  C CB  . THR D 460  ? 1.5415 1.6613 1.1943 -0.6766 -0.2856 0.3172  457  THR A CB  
4551  O OG1 . THR D 460  ? 1.5212 1.7328 1.1959 -0.6832 -0.2787 0.3307  457  THR A OG1 
4552  C CG2 . THR D 460  ? 1.6202 1.6829 1.2235 -0.7047 -0.3081 0.3274  457  THR A CG2 
4553  N N   . LEU D 461  ? 1.4492 1.5516 1.1624 -0.6133 -0.2534 0.2793  458  LEU A N   
4554  C CA  . LEU D 461  ? 1.3624 1.4979 1.1168 -0.5844 -0.2341 0.2679  458  LEU A CA  
4555  C C   . LEU D 461  ? 1.3302 1.5171 1.1073 -0.5780 -0.2250 0.2753  458  LEU A C   
4556  O O   . LEU D 461  ? 1.3018 1.4931 1.1043 -0.5548 -0.2120 0.2659  458  LEU A O   
4557  C CB  . LEU D 461  ? 1.3345 1.3985 1.0855 -0.5647 -0.2319 0.2502  458  LEU A CB  
4558  C CG  . LEU D 461  ? 1.2996 1.3441 1.0557 -0.5525 -0.2281 0.2361  458  LEU A CG  
4559  C CD1 . LEU D 461  ? 1.3366 1.3672 1.0647 -0.5735 -0.2414 0.2412  458  LEU A CD1 
4560  C CD2 . LEU D 461  ? 1.2969 1.2662 1.0432 -0.5342 -0.2282 0.2206  458  LEU A CD2 
4561  N N   . LYS D 462  ? 1.3581 1.5843 1.1254 -0.5985 -0.2322 0.2924  459  LYS A N   
4562  C CA  . LYS D 462  ? 1.3280 1.6005 1.1131 -0.5933 -0.2253 0.3001  459  LYS A CA  
4563  C C   . LYS D 462  ? 1.2607 1.6112 1.0854 -0.5712 -0.2069 0.2976  459  LYS A C   
4564  O O   . LYS D 462  ? 1.1955 1.5618 1.0435 -0.5508 -0.1951 0.2926  459  LYS A O   
4565  C CB  . LYS D 462  ? 1.3817 1.6769 1.1435 -0.6220 -0.2391 0.3195  459  LYS A CB  
4566  N N   . LYS D 463  ? 1.2760 1.6753 1.1069 -0.5740 -0.2044 0.3011  460  LYS A N   
4567  C CA  . LYS D 463  ? 1.2344 1.7087 1.0983 -0.5518 -0.1880 0.2990  460  LYS A CA  
4568  C C   . LYS D 463  ? 1.2012 1.6575 1.0847 -0.5281 -0.1770 0.2809  460  LYS A C   
4569  O O   . LYS D 463  ? 1.2518 1.6516 1.1217 -0.5332 -0.1832 0.2723  460  LYS A O   
4570  C CB  . LYS D 463  ? 1.2333 1.7739 1.0932 -0.5648 -0.1904 0.3124  460  LYS A CB  
4571  N N   . GLN D 464  ? 1.1198 1.6244 1.0339 -0.5014 -0.1610 0.2750  461  GLN A N   
4572  C CA  . GLN D 464  ? 1.0567 1.5524 0.9905 -0.4783 -0.1503 0.2586  461  GLN A CA  
4573  C C   . GLN D 464  ? 1.0510 1.5705 0.9840 -0.4813 -0.1509 0.2573  461  GLN A C   
4574  O O   . GLN D 464  ? 1.0149 1.5026 0.9521 -0.4729 -0.1489 0.2443  461  GLN A O   
4575  C CB  . GLN D 464  ? 1.0219 1.5650 0.9853 -0.4490 -0.1341 0.2538  461  GLN A CB  
4576  C CG  . GLN D 464  ? 1.0103 1.5429 0.9938 -0.4246 -0.1233 0.2370  461  GLN A CG  
4577  C CD  . GLN D 464  ? 1.0372 1.4919 1.0157 -0.4241 -0.1260 0.2261  461  GLN A CD  
4578  O OE1 . GLN D 464  ? 1.0592 1.4812 1.0303 -0.4287 -0.1291 0.2289  461  GLN A OE1 
4579  N NE2 . GLN D 464  ? 1.0190 1.4438 1.0001 -0.4177 -0.1251 0.2138  461  GLN A NE2 
4580  N N   . GLU D 465  ? 1.1040 1.6803 1.0309 -0.4930 -0.1536 0.2710  462  GLU A N   
4581  C CA  . GLU D 465  ? 1.0902 1.6897 1.0138 -0.4980 -0.1548 0.2713  462  GLU A CA  
4582  C C   . GLU D 465  ? 1.1054 1.6361 1.0032 -0.5205 -0.1689 0.2689  462  GLU A C   
4583  O O   . GLU D 465  ? 1.1232 1.6499 1.0211 -0.5193 -0.1688 0.2624  462  GLU A O   
4584  C CB  . GLU D 465  ? 1.0580 1.7310 0.9764 -0.5082 -0.1559 0.2884  462  GLU A CB  
4585  N N   . GLU D 466  ? 1.0934 1.5682 0.9671 -0.5398 -0.1814 0.2739  463  GLU A N   
4586  C CA  . GLU D 466  ? 1.1645 1.5651 1.0090 -0.5579 -0.1956 0.2705  463  GLU A CA  
4587  C C   . GLU D 466  ? 1.1761 1.5112 1.0252 -0.5405 -0.1925 0.2518  463  GLU A C   
4588  O O   . GLU D 466  ? 1.1612 1.4445 0.9930 -0.5460 -0.2002 0.2443  463  GLU A O   
4589  C CB  . GLU D 466  ? 1.2488 1.6153 1.0609 -0.5848 -0.2116 0.2837  463  GLU A CB  
4590  C CG  . GLU D 466  ? 1.3055 1.7294 1.1058 -0.6077 -0.2181 0.3035  463  GLU A CG  
4591  C CD  . GLU D 466  ? 1.3728 1.7682 1.1427 -0.6333 -0.2336 0.3172  463  GLU A CD  
4592  O OE1 . GLU D 466  ? 1.3691 1.7332 1.1397 -0.6266 -0.2334 0.3139  463  GLU A OE1 
4593  O OE2 . GLU D 466  ? 1.4176 1.8219 1.1620 -0.6605 -0.2464 0.3316  463  GLU A OE2 
4594  N N   . LYS D 467  ? 1.2059 1.5424 1.0765 -0.5195 -0.1817 0.2446  464  LYS A N   
4595  C CA  . LYS D 467  ? 1.2099 1.4939 1.0877 -0.5011 -0.1771 0.2273  464  LYS A CA  
4596  C C   . LYS D 467  ? 1.1860 1.4975 1.0853 -0.4843 -0.1675 0.2163  464  LYS A C   
4597  O O   . LYS D 467  ? 1.1673 1.4294 1.0625 -0.4772 -0.1689 0.2031  464  LYS A O   
4598  C CB  . LYS D 467  ? 1.1627 1.4451 1.0578 -0.4841 -0.1679 0.2240  464  LYS A CB  
4599  C CG  . LYS D 467  ? 1.1798 1.4241 1.0535 -0.4974 -0.1772 0.2320  464  LYS A CG  
4600  C CD  . LYS D 467  ? 1.1275 1.3676 1.0195 -0.4786 -0.1671 0.2272  464  LYS A CD  
4601  C CE  . LYS D 467  ? 1.1559 1.3589 1.0268 -0.4907 -0.1763 0.2349  464  LYS A CE  
4602  N NZ  . LYS D 467  ? 1.1284 1.3253 1.0164 -0.4722 -0.1664 0.2302  464  LYS A NZ  
4603  N N   . GLU D 468  ? 1.2179 1.6076 1.1382 -0.4767 -0.1582 0.2215  465  GLU A N   
4604  C CA  . GLU D 468  ? 1.2038 1.6244 1.1452 -0.4578 -0.1485 0.2109  465  GLU A CA  
4605  C C   . GLU D 468  ? 1.1882 1.5846 1.1129 -0.4708 -0.1574 0.2079  465  GLU A C   
4606  O O   . GLU D 468  ? 1.1667 1.5422 1.0986 -0.4585 -0.1546 0.1942  465  GLU A O   
4607  C CB  . GLU D 468  ? 1.2324 1.7414 1.1951 -0.4444 -0.1372 0.2177  465  GLU A CB  
4608  C CG  . GLU D 468  ? 1.2460 1.7910 1.2302 -0.4210 -0.1266 0.2068  465  GLU A CG  
4609  C CD  . GLU D 468  ? 1.2676 1.8970 1.2664 -0.4056 -0.1165 0.2138  465  GLU A CD  
4610  O OE1 . GLU D 468  ? 1.2952 1.9579 1.2846 -0.4183 -0.1195 0.2286  465  GLU A OE1 
4611  O OE2 . GLU D 468  ? 1.2508 1.9127 1.2682 -0.3798 -0.1060 0.2044  465  GLU A OE2 
4612  N N   . ILE D 469  ? 1.1730 1.5721 1.0742 -0.4960 -0.1686 0.2209  466  ILE A N   
4613  C CA  . ILE D 469  ? 1.1610 1.5393 1.0450 -0.5092 -0.1774 0.2192  466  ILE A CA  
4614  C C   . ILE D 469  ? 1.1367 1.4235 0.9976 -0.5135 -0.1877 0.2082  466  ILE A C   
4615  O O   . ILE D 469  ? 1.1337 1.3948 0.9872 -0.5132 -0.1913 0.1994  466  ILE A O   
4616  C CB  . ILE D 469  ? 1.2170 1.6241 1.0803 -0.5362 -0.1870 0.2374  466  ILE A CB  
4617  C CG1 . ILE D 469  ? 1.2655 1.6421 1.1057 -0.5554 -0.1975 0.2491  466  ILE A CG1 
4618  C CG2 . ILE D 469  ? 1.1935 1.6940 1.0781 -0.5280 -0.1760 0.2461  466  ILE A CG2 
4619  C CD1 . ILE D 469  ? 1.3055 1.7162 1.1254 -0.5829 -0.2072 0.2688  466  ILE A CD1 
4620  N N   . LEU D 470  ? 1.1084 1.3445 0.9558 -0.5161 -0.1926 0.2083  467  LEU A N   
4621  C CA  . LEU D 470  ? 1.1049 1.2535 0.9295 -0.5140 -0.2010 0.1964  467  LEU A CA  
4622  C C   . LEU D 470  ? 1.0181 1.1563 0.8649 -0.4880 -0.1904 0.1788  467  LEU A C   
4623  O O   . LEU D 470  ? 1.0250 1.1136 0.8580 -0.4842 -0.1955 0.1672  467  LEU A O   
4624  C CB  . LEU D 470  ? 1.1361 1.2366 0.9413 -0.5196 -0.2078 0.2007  467  LEU A CB  
4625  C CG  . LEU D 470  ? 1.1689 1.1783 0.9489 -0.5121 -0.2154 0.1880  467  LEU A CG  
4626  C CD1 . LEU D 470  ? 0.9331 0.8938 0.6785 -0.5251 -0.2297 0.1860  467  LEU A CD1 
4627  C CD2 . LEU D 470  ? 0.9093 0.8790 0.6723 -0.5149 -0.2208 0.1927  467  LEU A CD2 
4628  N N   . LYS D 471  ? 0.9273 1.1115 0.8068 -0.4698 -0.1761 0.1766  468  LYS A N   
4629  C CA  . LYS D 471  ? 0.8756 1.0494 0.7711 -0.4302 -0.1612 0.1586  468  LYS A CA  
4630  C C   . LYS D 471  ? 0.8188 1.0253 0.7240 -0.4224 -0.1569 0.1529  468  LYS A C   
4631  O O   . LYS D 471  ? 0.7983 0.9705 0.7014 -0.4004 -0.1523 0.1379  468  LYS A O   
4632  C CB  . LYS D 471  ? 0.8915 1.1033 0.8133 -0.4052 -0.1454 0.1574  468  LYS A CB  
4633  C CG  . LYS D 471  ? 0.9088 1.1102 0.8455 -0.3654 -0.1303 0.1400  468  LYS A CG  
4634  C CD  . LYS D 471  ? 0.8782 1.1371 0.8415 -0.3435 -0.1154 0.1406  468  LYS A CD  
4635  C CE  . LYS D 471  ? 0.8443 1.0974 0.8198 -0.3078 -0.1021 0.1245  468  LYS A CE  
4636  N NZ  . LYS D 471  ? 0.8025 1.1132 0.7994 -0.2871 -0.0893 0.1251  468  LYS A NZ  
4637  N N   . SER D 472  ? 0.8028 1.0780 0.7184 -0.4401 -0.1583 0.1651  469  SER A N   
4638  C CA  . SER D 472  ? 0.7791 1.0914 0.7045 -0.4321 -0.1540 0.1606  469  SER A CA  
4639  C C   . SER D 472  ? 0.7937 1.0525 0.6946 -0.4453 -0.1662 0.1547  469  SER A C   
4640  O O   . SER D 472  ? 0.7853 1.0359 0.6902 -0.4246 -0.1601 0.1419  469  SER A O   
4641  C CB  . SER D 472  ? 0.7714 1.1691 0.7094 -0.4497 -0.1544 0.1766  469  SER A CB  
4642  O OG  . SER D 472  ? 0.7582 1.1945 0.7051 -0.4429 -0.1510 0.1728  469  SER A OG  
4643  N N   . GLN D 473  ? 0.8333 1.0521 0.7058 -0.4776 -0.1834 0.1637  470  GLN A N   
4644  C CA  . GLN D 473  ? 0.8925 1.0528 0.7360 -0.4877 -0.1958 0.1577  470  GLN A CA  
4645  C C   . GLN D 473  ? 0.9498 1.0354 0.7821 -0.4640 -0.1943 0.1402  470  GLN A C   
4646  O O   . GLN D 473  ? 0.9560 1.0085 0.7765 -0.4557 -0.1968 0.1293  470  GLN A O   
4647  C CB  . GLN D 473  ? 0.9596 1.0884 0.7678 -0.5148 -0.2105 0.1714  470  GLN A CB  
4648  C CG  . GLN D 473  ? 0.9661 1.1641 0.7786 -0.5325 -0.2103 0.1891  470  GLN A CG  
4649  C CD  . GLN D 473  ? 0.9999 1.1657 0.7754 -0.5611 -0.2260 0.2036  470  GLN A CD  
4650  O OE1 . GLN D 473  ? 1.0144 1.1034 0.7574 -0.5682 -0.2386 0.1994  470  GLN A OE1 
4651  N NE2 . GLN D 473  ? 1.0116 1.2360 0.7898 -0.5768 -0.2258 0.2211  470  GLN A NE2 
4652  N N   . LEU D 474  ? 0.9922 1.0514 0.8269 -0.4487 -0.1887 0.1372  471  LEU A N   
4653  C CA  . LEU D 474  ? 1.0362 1.0319 0.8620 -0.4194 -0.1840 0.1208  471  LEU A CA  
4654  C C   . LEU D 474  ? 0.9509 0.9725 0.8029 -0.3834 -0.1663 0.1073  471  LEU A C   
4655  O O   . LEU D 474  ? 0.9599 0.9376 0.8027 -0.3636 -0.1645 0.0936  471  LEU A O   
4656  C CB  . LEU D 474  ? 1.0887 1.0561 0.9117 -0.4128 -0.1824 0.1223  471  LEU A CB  
4657  C CG  . LEU D 474  ? 0.8450 0.7595 0.6326 -0.4424 -0.2014 0.1317  471  LEU A CG  
4658  C CD1 . LEU D 474  ? 0.8693 0.7701 0.6599 -0.4345 -0.1975 0.1343  471  LEU A CD1 
4659  C CD2 . LEU D 474  ? 0.8918 0.7276 0.6427 -0.4409 -0.2137 0.1217  471  LEU A CD2 
4660  N N   . ASP D 475  ? 0.8781 0.9694 0.7604 -0.3741 -0.1536 0.1110  472  ASP A N   
4661  C CA  . ASP D 475  ? 0.8332 0.9484 0.7369 -0.3420 -0.1381 0.0991  472  ASP A CA  
4662  C C   . ASP D 475  ? 0.8323 0.9477 0.7293 -0.3446 -0.1419 0.0938  472  ASP A C   
4663  O O   . ASP D 475  ? 0.8240 0.9205 0.7240 -0.3198 -0.1344 0.0805  472  ASP A O   
4664  C CB  . ASP D 475  ? 0.8289 1.0168 0.7608 -0.3324 -0.1258 0.1049  472  ASP A CB  
4665  C CG  . ASP D 475  ? 0.8881 1.0757 0.8283 -0.3248 -0.1203 0.1081  472  ASP A CG  
4666  O OD1 . ASP D 475  ? 0.9197 1.0529 0.8506 -0.3145 -0.1204 0.1011  472  ASP A OD1 
4667  O OD2 . ASP D 475  ? 0.9058 1.1495 0.8612 -0.3282 -0.1158 0.1178  472  ASP A OD2 
4668  N N   . SER D 476  ? 0.8472 0.9853 0.7347 -0.3753 -0.1537 0.1048  473  SER A N   
4669  C CA  . SER D 476  ? 0.8550 0.9920 0.7340 -0.3806 -0.1589 0.1006  473  SER A CA  
4670  C C   . SER D 476  ? 0.8772 0.9339 0.7268 -0.3796 -0.1687 0.0904  473  SER A C   
4671  O O   . SER D 476  ? 0.8648 0.9069 0.7119 -0.3647 -0.1662 0.0794  473  SER A O   
4672  C CB  . SER D 476  ? 0.8538 1.0355 0.7282 -0.4168 -0.1706 0.1164  473  SER A CB  
4673  O OG  . SER D 476  ? 0.8090 1.0684 0.7092 -0.4158 -0.1615 0.1263  473  SER A OG  
4674  N N   . LEU D 477  ? 0.9093 0.9127 0.7348 -0.3939 -0.1802 0.0939  474  LEU A N   
4675  C CA  . LEU D 477  ? 0.9641 0.8880 0.7579 -0.3892 -0.1898 0.0838  474  LEU A CA  
4676  C C   . LEU D 477  ? 0.9343 0.8339 0.7382 -0.3493 -0.1757 0.0682  474  LEU A C   
4677  O O   . LEU D 477  ? 0.9591 0.8206 0.7493 -0.3347 -0.1770 0.0565  474  LEU A O   
4678  C CB  . LEU D 477  ? 1.0503 0.9227 0.8130 -0.4129 -0.2059 0.0919  474  LEU A CB  
4679  C CG  . LEU D 477  ? 1.1199 0.9683 0.8492 -0.4521 -0.2277 0.1015  474  LEU A CG  
4680  C CD1 . LEU D 477  ? 1.1715 0.9692 0.8752 -0.4449 -0.2352 0.0895  474  LEU A CD1 
4681  C CD2 . LEU D 477  ? 1.0938 1.0188 0.8417 -0.4790 -0.2287 0.1161  474  LEU A CD2 
4682  N N   . LEU D 478  ? 0.9032 0.8253 0.7301 -0.3319 -0.1627 0.0682  475  LEU A N   
4683  C CA  . LEU D 478  ? 0.8759 0.7815 0.7140 -0.2961 -0.1493 0.0549  475  LEU A CA  
4684  C C   . LEU D 478  ? 0.8576 0.8006 0.7170 -0.2767 -0.1371 0.0472  475  LEU A C   
4685  O O   . LEU D 478  ? 0.8597 0.7800 0.7201 -0.2515 -0.1300 0.0352  475  LEU A O   
4686  C CB  . LEU D 478  ? 0.8297 0.7498 0.6853 -0.2852 -0.1398 0.0579  475  LEU A CB  
4687  C CG  . LEU D 478  ? 0.7921 0.6864 0.6538 -0.2527 -0.1289 0.0461  475  LEU A CG  
4688  C CD1 . LEU D 478  ? 0.8422 0.6666 0.6727 -0.2490 -0.1389 0.0398  475  LEU A CD1 
4689  C CD2 . LEU D 478  ? 0.7429 0.6600 0.6240 -0.2442 -0.1194 0.0501  475  LEU A CD2 
4690  N N   . GLY D 479  ? 0.8277 0.8293 0.7033 -0.2877 -0.1346 0.0543  476  GLY A N   
4691  C CA  . GLY D 479  ? 0.8043 0.8394 0.6965 -0.2698 -0.1243 0.0473  476  GLY A CA  
4692  C C   . GLY D 479  ? 0.8531 0.8554 0.7272 -0.2698 -0.1311 0.0392  476  GLY A C   
4693  O O   . GLY D 479  ? 0.8623 0.8598 0.7429 -0.2459 -0.1223 0.0283  476  GLY A O   
4694  N N   . LEU D 480  ? 0.8939 0.8723 0.7434 -0.2974 -0.1475 0.0448  477  LEU A N   
4695  C CA  . LEU D 480  ? 0.9017 0.8409 0.7290 -0.2979 -0.1559 0.0368  477  LEU A CA  
4696  C C   . LEU D 480  ? 0.9255 0.8003 0.7355 -0.2764 -0.1558 0.0251  477  LEU A C   
4697  O O   . LEU D 480  ? 0.9359 0.7909 0.7403 -0.2588 -0.1533 0.0141  477  LEU A O   
4698  C CB  . LEU D 480  ? 0.9027 0.8279 0.7039 -0.3347 -0.1752 0.0464  477  LEU A CB  
4699  C CG  . LEU D 480  ? 0.9225 0.8009 0.6947 -0.3388 -0.1869 0.0389  477  LEU A CG  
4700  C CD1 . LEU D 480  ? 0.9005 0.8134 0.6900 -0.3221 -0.1771 0.0313  477  LEU A CD1 
4701  C CD2 . LEU D 480  ? 0.9686 0.8329 0.7130 -0.3790 -0.2075 0.0503  477  LEU A CD2 
4702  N N   . TYR D 481  ? 0.9449 0.7889 0.7461 -0.2767 -0.1585 0.0275  478  TYR A N   
4703  C CA  . TYR D 481  ? 0.9800 0.7691 0.7660 -0.2535 -0.1574 0.0170  478  TYR A CA  
4704  C C   . TYR D 481  ? 0.9118 0.7235 0.7243 -0.2205 -0.1391 0.0077  478  TYR A C   
4705  O O   . TYR D 481  ? 0.9054 0.6856 0.7086 -0.1990 -0.1367 -0.0029 478  TYR A O   
4706  C CB  . TYR D 481  ? 1.0760 0.8338 0.8488 -0.2604 -0.1634 0.0225  478  TYR A CB  
4707  C CG  . TYR D 481  ? 1.1807 0.8915 0.9417 -0.2334 -0.1603 0.0127  478  TYR A CG  
4708  C CD1 . TYR D 481  ? 1.2683 0.9162 0.9924 -0.2288 -0.1722 0.0057  478  TYR A CD1 
4709  C CD2 . TYR D 481  ? 1.1956 0.9258 0.9807 -0.2121 -0.1459 0.0106  478  TYR A CD2 
4710  C CE1 . TYR D 481  ? 1.3049 0.9146 1.0175 -0.2020 -0.1692 -0.0030 478  TYR A CE1 
4711  C CE2 . TYR D 481  ? 1.2267 0.9197 1.0017 -0.1878 -0.1431 0.0026  478  TYR A CE2 
4712  C CZ  . TYR D 481  ? 1.2765 0.9114 1.0159 -0.1821 -0.1544 -0.0041 478  TYR A CZ  
4713  O OH  . TYR D 481  ? 1.2898 0.8923 1.0186 -0.1558 -0.1513 -0.0117 478  TYR A OH  
4714  N N   . HIS D 482  ? 0.8559 0.7218 0.6995 -0.2162 -0.1268 0.0121  479  HIS A N   
4715  C CA  . HIS D 482  ? 0.8051 0.6927 0.6716 -0.1879 -0.1106 0.0043  479  HIS A CA  
4716  C C   . HIS D 482  ? 0.8025 0.7007 0.6710 -0.1789 -0.1076 -0.0029 479  HIS A C   
4717  O O   . HIS D 482  ? 0.8074 0.6956 0.6799 -0.1555 -0.0994 -0.0122 479  HIS A O   
4718  C CB  . HIS D 482  ? 0.7420 0.6816 0.6360 -0.1864 -0.1001 0.0108  479  HIS A CB  
4719  C CG  . HIS D 482  ? 0.7505 0.6800 0.6477 -0.1843 -0.0981 0.0146  479  HIS A CG  
4720  N ND1 . HIS D 482  ? 0.7374 0.7051 0.6508 -0.1918 -0.0942 0.0235  479  HIS A ND1 
4721  C CD2 . HIS D 482  ? 0.7669 0.6540 0.6528 -0.1743 -0.0994 0.0107  479  HIS A CD2 
4722  C CE1 . HIS D 482  ? 0.7469 0.6946 0.6591 -0.1877 -0.0933 0.0249  479  HIS A CE1 
4723  N NE2 . HIS D 482  ? 0.7647 0.6641 0.6606 -0.1771 -0.0964 0.0173  479  HIS A NE2 
4724  N N   . LEU D 483  ? 0.8073 0.7276 0.6729 -0.1980 -0.1143 0.0018  480  LEU A N   
4725  C CA  . LEU D 483  ? 0.7989 0.7334 0.6673 -0.1903 -0.1114 -0.0045 480  LEU A CA  
4726  C C   . LEU D 483  ? 0.8405 0.7226 0.6850 -0.1812 -0.1176 -0.0143 480  LEU A C   
4727  O O   . LEU D 483  ? 0.8472 0.7310 0.6969 -0.1615 -0.1101 -0.0230 480  LEU A O   
4728  C CB  . LEU D 483  ? 0.7839 0.7548 0.6528 -0.2146 -0.1185 0.0038  480  LEU A CB  
4729  C CG  . LEU D 483  ? 0.7510 0.7389 0.6210 -0.2101 -0.1173 -0.0015 480  LEU A CG  
4730  C CD1 . LEU D 483  ? 0.7158 0.7344 0.6090 -0.1827 -0.1009 -0.0077 480  LEU A CD1 
4731  C CD2 . LEU D 483  ? 0.7371 0.7644 0.6071 -0.2367 -0.1255 0.0085  480  LEU A CD2 
4732  N N   . LEU D 484  ? 0.8766 0.7105 0.6927 -0.1946 -0.1316 -0.0131 481  LEU A N   
4733  C CA  . LEU D 484  ? 0.9138 0.6955 0.7022 -0.1853 -0.1392 -0.0225 481  LEU A CA  
4734  C C   . LEU D 484  ? 0.9330 0.6947 0.7246 -0.1539 -0.1291 -0.0318 481  LEU A C   
4735  O O   . LEU D 484  ? 0.9878 0.7261 0.7672 -0.1376 -0.1291 -0.0411 481  LEU A O   
4736  C CB  . LEU D 484  ? 0.9457 0.6761 0.6979 -0.2069 -0.1581 -0.0186 481  LEU A CB  
4737  C CG  . LEU D 484  ? 0.9606 0.7054 0.7035 -0.2418 -0.1712 -0.0088 481  LEU A CG  
4738  C CD1 . LEU D 484  ? 1.0389 0.7228 0.7400 -0.2628 -0.1914 -0.0055 481  LEU A CD1 
4739  C CD2 . LEU D 484  ? 0.9206 0.6877 0.6671 -0.2425 -0.1707 -0.0127 481  LEU A CD2 
4740  N N   . ASP D 485  ? 0.8988 0.6717 0.7067 -0.1453 -0.1206 -0.0291 482  ASP A N   
4741  C CA  . ASP D 485  ? 0.8961 0.6569 0.7091 -0.1173 -0.1108 -0.0362 482  ASP A CA  
4742  C C   . ASP D 485  ? 0.8713 0.6691 0.7093 -0.0989 -0.0961 -0.0409 482  ASP A C   
4743  O O   . ASP D 485  ? 0.8396 0.6357 0.6853 -0.0775 -0.0870 -0.0454 482  ASP A O   
4744  C CB  . ASP D 485  ? 0.9016 0.6622 0.7225 -0.1162 -0.1075 -0.0310 482  ASP A CB  
4745  C CG  . ASP D 485  ? 0.9898 0.6969 0.7795 -0.1201 -0.1201 -0.0308 482  ASP A CG  
4746  O OD1 . ASP D 485  ? 1.0546 0.7291 0.8164 -0.1352 -0.1344 -0.0306 482  ASP A OD1 
4747  O OD2 . ASP D 485  ? 1.0164 0.7124 0.8076 -0.1080 -0.1163 -0.0308 482  ASP A OD2 
4748  N N   . TRP D 486  ? 0.8563 0.6878 0.7059 -0.1070 -0.0940 -0.0395 483  TRP A N   
4749  C CA  . TRP D 486  ? 0.8074 0.6686 0.6759 -0.0896 -0.0816 -0.0443 483  TRP A CA  
4750  C C   . TRP D 486  ? 0.8446 0.6804 0.6993 -0.0731 -0.0819 -0.0538 483  TRP A C   
4751  O O   . TRP D 486  ? 0.8415 0.6907 0.7084 -0.0541 -0.0713 -0.0583 483  TRP A O   
4752  C CB  . TRP D 486  ? 0.7805 0.6841 0.6622 -0.1013 -0.0800 -0.0402 483  TRP A CB  
4753  C CG  . TRP D 486  ? 0.7736 0.7144 0.6741 -0.1095 -0.0754 -0.0317 483  TRP A CG  
4754  C CD1 . TRP D 486  ? 0.7692 0.7065 0.6745 -0.1115 -0.0741 -0.0269 483  TRP A CD1 
4755  C CD2 . TRP D 486  ? 0.7408 0.7292 0.6566 -0.1150 -0.0713 -0.0272 483  TRP A CD2 
4756  N NE1 . TRP D 486  ? 0.7207 0.7000 0.6432 -0.1180 -0.0696 -0.0198 483  TRP A NE1 
4757  C CE2 . TRP D 486  ? 0.7135 0.7252 0.6421 -0.1194 -0.0678 -0.0198 483  TRP A CE2 
4758  C CE3 . TRP D 486  ? 0.7286 0.7431 0.6475 -0.1152 -0.0703 -0.0287 483  TRP A CE3 
4759  C CZ2 . TRP D 486  ? 0.6994 0.7595 0.6424 -0.1226 -0.0634 -0.0141 483  TRP A CZ2 
4760  C CZ3 . TRP D 486  ? 0.7208 0.7840 0.6544 -0.1184 -0.0659 -0.0229 483  TRP A CZ3 
4761  C CH2 . TRP D 486  ? 0.7008 0.7865 0.6458 -0.1214 -0.0625 -0.0157 483  TRP A CH2 
4762  N N   . PHE D 487  ? 0.9087 0.7071 0.7361 -0.0803 -0.0946 -0.0566 484  PHE A N   
4763  C CA  . PHE D 487  ? 0.9846 0.7597 0.7961 -0.0652 -0.0962 -0.0658 484  PHE A CA  
4764  C C   . PHE D 487  ? 1.0938 0.8340 0.8908 -0.0450 -0.0960 -0.0710 484  PHE A C   
4765  O O   . PHE D 487  ? 1.0731 0.7876 0.8577 -0.0489 -0.1020 -0.0682 484  PHE A O   
4766  C CB  . PHE D 487  ? 1.0041 0.7548 0.7901 -0.0824 -0.1111 -0.0667 484  PHE A CB  
4767  C CG  . PHE D 487  ? 0.9723 0.7609 0.7712 -0.1032 -0.1123 -0.0607 484  PHE A CG  
4768  C CD1 . PHE D 487  ? 0.9091 0.7304 0.7230 -0.0958 -0.1045 -0.0637 484  PHE A CD1 
4769  C CD2 . PHE D 487  ? 0.9943 0.7883 0.7898 -0.1298 -0.1214 -0.0514 484  PHE A CD2 
4770  C CE1 . PHE D 487  ? 0.8827 0.7422 0.7078 -0.1128 -0.1055 -0.0582 484  PHE A CE1 
4771  C CE2 . PHE D 487  ? 0.9701 0.8054 0.7779 -0.1481 -0.1223 -0.0450 484  PHE A CE2 
4772  C CZ  . PHE D 487  ? 0.9131 0.7816 0.7357 -0.1386 -0.1143 -0.0487 484  PHE A CZ  
4773  N N   . ALA D 488  ? 1.2088 0.9500 1.0067 -0.0229 -0.0891 -0.0781 485  ALA A N   
4774  C CA  . ALA D 488  ? 1.3154 1.0312 1.1004 -0.0006 -0.0877 -0.0829 485  ALA A CA  
4775  C C   . ALA D 488  ? 1.4235 1.0851 1.1692 -0.0010 -0.1031 -0.0871 485  ALA A C   
4776  O O   . ALA D 488  ? 1.4177 1.0606 1.1444 -0.0100 -0.1129 -0.0901 485  ALA A O   
4777  C CB  . ALA D 488  ? 1.2917 1.0256 1.0859 0.0216  -0.0774 -0.0887 485  ALA A CB  
4778  N N   . VAL D 489  ? 1.5436 1.1781 1.2750 0.0094  -0.1060 -0.0873 486  VAL A N   
4779  C CA  . VAL D 489  ? 1.6347 1.2116 1.3242 0.0102  -0.1217 -0.0909 486  VAL A CA  
4780  C C   . VAL D 489  ? 1.6463 1.2019 1.3157 0.0418  -0.1207 -0.0998 486  VAL A C   
4781  O O   . VAL D 489  ? 1.6974 1.2057 1.3283 0.0477  -0.1335 -0.1059 486  VAL A O   
4782  C CB  . VAL D 489  ? 1.6741 1.2308 1.3557 0.0003  -0.1275 -0.0847 486  VAL A CB  
4783  C CG1 . VAL D 489  ? 1.7521 1.2445 1.3861 -0.0053 -0.1467 -0.0872 486  VAL A CG1 
4784  C CG2 . VAL D 489  ? 1.6404 1.2322 1.3497 -0.0267 -0.1246 -0.0750 486  VAL A CG2 
4785  N N   . ASP D 490  ? 1.5708 1.1615 1.2645 0.0622  -0.1059 -0.1004 487  ASP A N   
4786  C CA  . ASP D 490  ? 1.5809 1.1606 1.2584 0.0935  -0.1035 -0.1075 487  ASP A CA  
4787  C C   . ASP D 490  ? 1.5989 1.1677 1.2600 0.1009  -0.1073 -0.1150 487  ASP A C   
4788  O O   . ASP D 490  ? 1.5858 1.1797 1.2648 0.0878  -0.1037 -0.1143 487  ASP A O   
4789  C CB  . ASP D 490  ? 1.5319 1.1598 1.2422 0.1090  -0.0867 -0.1047 487  ASP A CB  
4790  N N   . GLU D 491  ? 1.6124 1.1431 1.2374 0.1236  -0.1149 -0.1226 488  GLU A N   
4791  C CA  . GLU D 491  ? 1.5851 1.1007 1.1895 0.1344  -0.1195 -0.1306 488  GLU A CA  
4792  C C   . GLU D 491  ? 1.5081 1.0692 1.1361 0.1554  -0.1044 -0.1327 488  GLU A C   
4793  O O   . GLU D 491  ? 1.5161 1.0677 1.1268 0.1699  -0.1068 -0.1397 488  GLU A O   
4794  C CB  . GLU D 491  ? 1.6263 1.0799 1.1783 0.1527  -0.1345 -0.1383 488  GLU A CB  
4795  N N   . SER D 492  ? 1.4303 1.0395 1.0954 0.1567  -0.0898 -0.1264 489  SER A N   
4796  C CA  . SER D 492  ? 1.3676 1.0213 1.0552 0.1728  -0.0760 -0.1267 489  SER A CA  
4797  C C   . SER D 492  ? 1.3431 1.0176 1.0465 0.1591  -0.0728 -0.1272 489  SER A C   
4798  O O   . SER D 492  ? 1.3384 1.0354 1.0476 0.1735  -0.0658 -0.1300 489  SER A O   
4799  C CB  . SER D 492  ? 1.2993 0.9953 1.0197 0.1739  -0.0630 -0.1188 489  SER A CB  
4800  O OG  . SER D 492  ? 1.2465 0.9535 0.9892 0.1474  -0.0618 -0.1121 489  SER A OG  
4801  N N   . ASN D 493  ? 1.3319 1.0015 1.0419 0.1320  -0.0779 -0.1243 490  ASN A N   
4802  C CA  . ASN D 493  ? 1.2982 0.9880 1.0220 0.1187  -0.0757 -0.1246 490  ASN A CA  
4803  C C   . ASN D 493  ? 1.3496 1.0011 1.0412 0.1152  -0.0893 -0.1315 490  ASN A C   
4804  O O   . ASN D 493  ? 1.3685 0.9735 1.0272 0.1150  -0.1026 -0.1345 490  ASN A O   
4805  C CB  . ASN D 493  ? 1.2453 0.9580 0.9948 0.0922  -0.0731 -0.1170 490  ASN A CB  
4806  C CG  . ASN D 493  ? 1.1991 0.9369 0.9728 0.0929  -0.0635 -0.1101 490  ASN A CG  
4807  O OD1 . ASN D 493  ? 1.1632 0.9371 0.9606 0.0999  -0.0513 -0.1075 490  ASN A OD1 
4808  N ND2 . ASN D 493  ? 1.1987 0.9161 0.9649 0.0845  -0.0696 -0.1069 490  ASN A ND2 
4809  N N   . GLU D 494  ? 1.3700 1.0395 1.0694 0.1122  -0.0866 -0.1338 491  GLU A N   
4810  C CA  . GLU D 494  ? 1.4022 1.0402 1.0736 0.1067  -0.0992 -0.1400 491  GLU A CA  
4811  C C   . GLU D 494  ? 1.4309 1.0615 1.1026 0.0746  -0.1085 -0.1351 491  GLU A C   
4812  O O   . GLU D 494  ? 1.3924 1.0525 1.0836 0.0589  -0.1053 -0.1321 491  GLU A O   
4813  C CB  . GLU D 494  ? 1.3354 0.9983 1.0157 0.1162  -0.0923 -0.1440 491  GLU A CB  
4814  C CG  . GLU D 494  ? 1.3008 0.9640 0.9710 0.1477  -0.0868 -0.1497 491  GLU A CG  
4815  C CD  . GLU D 494  ? 1.2667 0.9496 0.9412 0.1557  -0.0820 -0.1538 491  GLU A CD  
4816  O OE1 . GLU D 494  ? 1.2222 0.9414 0.9249 0.1435  -0.0738 -0.1496 491  GLU A OE1 
4817  O OE2 . GLU D 494  ? 1.2959 0.9568 0.9438 0.1753  -0.0868 -0.1614 491  GLU A OE2 
4818  N N   . VAL D 495  ? 1.5313 1.1227 1.1796 0.0651  -0.1207 -0.1337 492  VAL A N   
4819  C CA  . VAL D 495  ? 1.5186 1.1028 1.1650 0.0331  -0.1307 -0.1275 492  VAL A CA  
4820  C C   . VAL D 495  ? 1.5240 1.0790 1.1416 0.0202  -0.1454 -0.1316 492  VAL A C   
4821  O O   . VAL D 495  ? 1.5515 1.0710 1.1381 0.0366  -0.1525 -0.1401 492  VAL A O   
4822  C CB  . VAL D 495  ? 1.5544 1.1068 1.1854 0.0265  -0.1386 -0.1235 492  VAL A CB  
4823  C CG1 . VAL D 495  ? 1.5153 1.1030 1.1790 0.0346  -0.1239 -0.1181 492  VAL A CG1 
4824  C CG2 . VAL D 495  ? 1.6277 1.1214 1.2138 0.0455  -0.1502 -0.1313 492  VAL A CG2 
4825  N N   . ASP D 496  ? 1.4977 1.0697 1.1250 -0.0093 -0.1503 -0.1252 493  ASP A N   
4826  C CA  . ASP D 496  ? 1.5117 1.0603 1.1133 -0.0266 -0.1651 -0.1273 493  ASP A CA  
4827  C C   . ASP D 496  ? 1.5745 1.0545 1.1276 -0.0331 -0.1850 -0.1296 493  ASP A C   
4828  O O   . ASP D 496  ? 1.6017 1.0631 1.1484 -0.0392 -0.1888 -0.1249 493  ASP A O   
4829  C CB  . ASP D 496  ? 1.4591 1.0475 1.0832 -0.0578 -0.1657 -0.1181 493  ASP A CB  
4830  C CG  . ASP D 496  ? 1.4838 1.0597 1.0866 -0.0763 -0.1793 -0.1195 493  ASP A CG  
4831  O OD1 . ASP D 496  ? 1.4621 1.0659 1.0778 -0.0687 -0.1726 -0.1233 493  ASP A OD1 
4832  O OD2 . ASP D 496  ? 1.5343 1.0720 1.1065 -0.0994 -0.1973 -0.1164 493  ASP A OD2 
4833  N N   . PRO D 497  ? 1.6125 1.0511 1.1284 -0.0312 -0.1984 -0.1369 494  PRO A N   
4834  C CA  . PRO D 497  ? 1.6591 1.0249 1.1222 -0.0373 -0.2194 -0.1394 494  PRO A CA  
4835  C C   . PRO D 497  ? 1.6340 0.9888 1.0894 -0.0760 -0.2327 -0.1287 494  PRO A C   
4836  O O   . PRO D 497  ? 1.6387 0.9638 1.0795 -0.0794 -0.2385 -0.1252 494  PRO A O   
4837  C CB  . PRO D 497  ? 1.7207 1.0550 1.1507 -0.0325 -0.2305 -0.1483 494  PRO A CB  
4838  C CG  . PRO D 497  ? 1.6755 1.0593 1.1385 -0.0087 -0.2119 -0.1532 494  PRO A CG  
4839  C CD  . PRO D 497  ? 1.6084 1.0608 1.1256 -0.0195 -0.1949 -0.1440 494  PRO A CD  
4840  N N   . GLU D 498  ? 1.6055 0.9869 1.0709 -0.1055 -0.2376 -0.1229 495  GLU A N   
4841  C CA  . GLU D 498  ? 1.5952 0.9688 1.0508 -0.1451 -0.2519 -0.1117 495  GLU A CA  
4842  C C   . GLU D 498  ? 1.5294 0.9517 1.0255 -0.1543 -0.2394 -0.1012 495  GLU A C   
4843  O O   . GLU D 498  ? 1.5569 0.9567 1.0394 -0.1738 -0.2492 -0.0936 495  GLU A O   
4844  C CB  . GLU D 498  ? 1.5919 0.9868 1.0474 -0.1733 -0.2603 -0.1078 495  GLU A CB  
4845  N N   . PHE D 499  ? 1.4145 0.9012 0.9585 -0.1405 -0.2184 -0.1006 496  PHE A N   
4846  C CA  . PHE D 499  ? 1.3064 0.8419 0.8884 -0.1499 -0.2070 -0.0907 496  PHE A CA  
4847  C C   . PHE D 499  ? 1.2769 0.7860 0.8539 -0.1363 -0.2044 -0.0905 496  PHE A C   
4848  O O   . PHE D 499  ? 1.2856 0.7990 0.8673 -0.1555 -0.2077 -0.0812 496  PHE A O   
4849  C CB  . PHE D 499  ? 1.2080 0.8103 0.8361 -0.1350 -0.1861 -0.0912 496  PHE A CB  
4850  C CG  . PHE D 499  ? 1.1456 0.8011 0.8107 -0.1464 -0.1757 -0.0809 496  PHE A CG  
4851  C CD1 . PHE D 499  ? 1.1158 0.7796 0.7994 -0.1303 -0.1639 -0.0800 496  PHE A CD1 
4852  C CD2 . PHE D 499  ? 1.1326 0.8314 0.8130 -0.1724 -0.1778 -0.0720 496  PHE A CD2 
4853  C CE1 . PHE D 499  ? 1.0676 0.7779 0.7826 -0.1397 -0.1549 -0.0710 496  PHE A CE1 
4854  C CE2 . PHE D 499  ? 1.0855 0.8339 0.7977 -0.1804 -0.1683 -0.0627 496  PHE A CE2 
4855  C CZ  . PHE D 499  ? 1.0509 0.8030 0.7797 -0.1638 -0.1570 -0.0626 496  PHE A CZ  
4856  N N   . SER D 500  ? 1.2536 0.7383 0.8214 -0.1029 -0.1984 -0.1003 497  SER A N   
4857  C CA  . SER D 500  ? 1.2545 0.7178 0.8180 -0.0875 -0.1954 -0.1003 497  SER A CA  
4858  C C   . SER D 500  ? 1.3516 0.7504 0.8699 -0.1032 -0.2159 -0.0981 497  SER A C   
4859  O O   . SER D 500  ? 1.3242 0.7135 0.8429 -0.1047 -0.2158 -0.0932 497  SER A O   
4860  C CB  . SER D 500  ? 1.2520 0.7064 0.8130 -0.0481 -0.1855 -0.1108 497  SER A CB  
4861  O OG  . SER D 500  ? 1.2719 0.7102 0.8297 -0.0323 -0.1822 -0.1105 497  SER A OG  
4862  N N   . ALA D 501  ? 1.4421 0.7942 0.9192 -0.1153 -0.2342 -0.1013 498  ALA A N   
4863  C CA  . ALA D 501  ? 1.5059 0.7903 0.9342 -0.1321 -0.2558 -0.0989 498  ALA A CA  
4864  C C   . ALA D 501  ? 1.4961 0.7992 0.9337 -0.1739 -0.2634 -0.0846 498  ALA A C   
4865  O O   . ALA D 501  ? 1.5223 0.7960 0.9434 -0.1848 -0.2716 -0.0787 498  ALA A O   
4866  C CB  . ALA D 501  ? 1.5644 0.7888 0.9416 -0.1321 -0.2743 -0.1070 498  ALA A CB  
4867  N N   . ARG D 502  ? 1.4772 0.8312 0.9408 -0.1970 -0.2608 -0.0785 499  ARG A N   
4868  C CA  . ARG D 502  ? 1.4963 0.8775 0.9707 -0.2364 -0.2674 -0.0639 499  ARG A CA  
4869  C C   . ARG D 502  ? 1.4594 0.8901 0.9761 -0.2330 -0.2510 -0.0567 499  ARG A C   
4870  O O   . ARG D 502  ? 1.4785 0.9100 0.9930 -0.2587 -0.2581 -0.0455 499  ARG A O   
4871  C CB  . ARG D 502  ? 1.5143 0.9428 1.0058 -0.2588 -0.2681 -0.0594 499  ARG A CB  
4872  C CG  . ARG D 502  ? 1.6346 1.0182 1.0857 -0.2647 -0.2845 -0.0661 499  ARG A CG  
4873  C CD  . ARG D 502  ? 1.6806 1.1139 1.1478 -0.2929 -0.2872 -0.0589 499  ARG A CD  
4874  N NE  . ARG D 502  ? 1.7556 1.1987 1.2165 -0.3359 -0.3008 -0.0435 499  ARG A NE  
4875  C CZ  . ARG D 502  ? 1.7802 1.2785 1.2596 -0.3652 -0.3029 -0.0332 499  ARG A CZ  
4876  N NH1 . ARG D 502  ? 1.7581 1.3042 1.2629 -0.3549 -0.2921 -0.0375 499  ARG A NH1 
4877  N NH2 . ARG D 502  ? 1.8060 1.3176 1.2819 -0.4005 -0.3125 -0.0169 499  ARG A NH2 
4878  N N   . LEU D 503  ? 1.4217 0.8931 0.9754 -0.2027 -0.2298 -0.0624 500  LEU A N   
4879  C CA  . LEU D 503  ? 1.3550 0.8702 0.9465 -0.1977 -0.2146 -0.0563 500  LEU A CA  
4880  C C   . LEU D 503  ? 1.3643 0.8338 0.9358 -0.1880 -0.2186 -0.0566 500  LEU A C   
4881  O O   . LEU D 503  ? 1.3555 0.8366 0.9366 -0.2036 -0.2189 -0.0471 500  LEU A O   
4882  C CB  . LEU D 503  ? 1.2583 0.8232 0.8896 -0.1690 -0.1926 -0.0623 500  LEU A CB  
4883  C CG  . LEU D 503  ? 1.1896 0.7959 0.8579 -0.1597 -0.1764 -0.0575 500  LEU A CG  
4884  C CD1 . LEU D 503  ? 1.1739 0.8243 0.8631 -0.1887 -0.1768 -0.0447 500  LEU A CD1 
4885  C CD2 . LEU D 503  ? 1.1385 0.7838 0.8382 -0.1317 -0.1573 -0.0640 500  LEU A CD2 
4886  N N   . THR D 504  ? 1.3906 0.8093 0.9332 -0.1611 -0.2216 -0.0675 501  THR A N   
4887  C CA  . THR D 504  ? 1.4200 0.7941 0.9405 -0.1482 -0.2257 -0.0686 501  THR A CA  
4888  C C   . THR D 504  ? 1.4611 0.7856 0.9429 -0.1787 -0.2470 -0.0608 501  THR A C   
4889  O O   . THR D 504  ? 1.4765 0.7807 0.9504 -0.1789 -0.2494 -0.0566 501  THR A O   
4890  C CB  . THR D 504  ? 1.4698 0.8007 0.9629 -0.1120 -0.2260 -0.0819 501  THR A CB  
4891  O OG1 . THR D 504  ? 1.4319 0.8080 0.9565 -0.0896 -0.2091 -0.0883 501  THR A OG1 
4892  C CG2 . THR D 504  ? 1.5102 0.8172 0.9950 -0.0901 -0.2229 -0.0833 501  THR A CG2 
4893  N N   . GLY D 505  ? 1.4958 0.8002 0.9522 -0.2058 -0.2633 -0.0582 502  GLY A N   
4894  C CA  . GLY D 505  ? 1.5440 0.8016 0.9618 -0.2392 -0.2852 -0.0492 502  GLY A CA  
4895  C C   . GLY D 505  ? 1.4747 0.7806 0.9232 -0.2685 -0.2816 -0.0342 502  GLY A C   
4896  O O   . GLY D 505  ? 1.5000 0.7781 0.9327 -0.2786 -0.2890 -0.0277 502  GLY A O   
4897  N N   . ILE D 506  ? 1.3983 0.7779 0.8900 -0.2810 -0.2702 -0.0283 503  ILE A N   
4898  C CA  . ILE D 506  ? 1.3730 0.8053 0.8950 -0.3065 -0.2659 -0.0140 503  ILE A CA  
4899  C C   . ILE D 506  ? 1.3795 0.8423 0.9361 -0.2832 -0.2473 -0.0143 503  ILE A C   
4900  O O   . ILE D 506  ? 1.3653 0.8538 0.9372 -0.3005 -0.2460 -0.0031 503  ILE A O   
4901  C CB  . ILE D 506  ? 1.3046 0.8073 0.8589 -0.3249 -0.2602 -0.0078 503  ILE A CB  
4902  C CG1 . ILE D 506  ? 1.2414 0.7907 0.8339 -0.2922 -0.2387 -0.0174 503  ILE A CG1 
4903  C CG2 . ILE D 506  ? 1.3591 0.8332 0.8784 -0.3518 -0.2800 -0.0060 503  ILE A CG2 
4904  C CD1 . ILE D 506  ? 1.1947 0.8124 0.8174 -0.3056 -0.2323 -0.0124 503  ILE A CD1 
4905  N N   . LYS D 507  ? 1.4025 0.8647 0.9714 -0.2451 -0.2331 -0.0262 504  LYS A N   
4906  C CA  . LYS D 507  ? 1.3885 0.8747 0.9863 -0.2236 -0.2169 -0.0265 504  LYS A CA  
4907  C C   . LYS D 507  ? 1.4823 0.9138 1.0499 -0.2227 -0.2268 -0.0247 504  LYS A C   
4908  O O   . LYS D 507  ? 1.4299 0.8823 1.0168 -0.2254 -0.2203 -0.0179 504  LYS A O   
4909  C CB  . LYS D 507  ? 1.3405 0.8413 0.9572 -0.1855 -0.2005 -0.0385 504  LYS A CB  
4910  C CG  . LYS D 507  ? 1.3133 0.8362 0.9571 -0.1629 -0.1846 -0.0391 504  LYS A CG  
4911  C CD  . LYS D 507  ? 1.2926 0.8329 0.9542 -0.1288 -0.1693 -0.0496 504  LYS A CD  
4912  C CE  . LYS D 507  ? 1.2579 0.8545 0.9521 -0.1311 -0.1583 -0.0495 504  LYS A CE  
4913  N NZ  . LYS D 507  ? 1.2185 0.8349 0.9316 -0.1000 -0.1430 -0.0580 504  LYS A NZ  
4914  N N   . LEU D 508  ? 1.6755 1.0350 1.1937 -0.2180 -0.2428 -0.0310 505  LEU A N   
4915  C CA  . LEU D 508  ? 1.7407 1.0410 1.2232 -0.2170 -0.2545 -0.0296 505  LEU A CA  
4916  C C   . LEU D 508  ? 1.7788 1.0632 1.2419 -0.2587 -0.2714 -0.0158 505  LEU A C   
4917  O O   . LEU D 508  ? 1.8052 1.0602 1.2525 -0.2623 -0.2772 -0.0109 505  LEU A O   
4918  C CB  . LEU D 508  ? 1.8151 1.0406 1.2464 -0.1949 -0.2669 -0.0415 505  LEU A CB  
4919  C CG  . LEU D 508  ? 1.8461 1.0651 1.2815 -0.1494 -0.2539 -0.0530 505  LEU A CG  
4920  C CD1 . LEU D 508  ? 1.7963 1.0827 1.2810 -0.1298 -0.2320 -0.0579 505  LEU A CD1 
4921  C CD2 . LEU D 508  ? 1.9265 1.0690 1.3049 -0.1289 -0.2688 -0.0639 505  LEU A CD2 
4922  N N   . GLU D 509  ? 1.7118 1.0167 1.1755 -0.2908 -0.2797 -0.0087 506  GLU A N   
4923  C CA  . GLU D 509  ? 1.7207 1.0223 1.1705 -0.3333 -0.2948 0.0066  506  GLU A CA  
4924  C C   . GLU D 509  ? 1.6780 1.0550 1.1766 -0.3469 -0.2812 0.0183  506  GLU A C   
4925  O O   . GLU D 509  ? 1.6965 1.0769 1.1884 -0.3763 -0.2901 0.0323  506  GLU A O   
4926  C CB  . GLU D 509  ? 1.7380 1.0439 1.1726 -0.3563 -0.3054 0.0126  506  GLU A CB  
4927  C CG  . GLU D 509  ? 1.8218 1.0550 1.2044 -0.3436 -0.3191 0.0066  506  GLU A CG  
4928  C CD  . GLU D 509  ? 1.8673 1.1064 1.2386 -0.3614 -0.3274 0.0092  506  GLU A CD  
4929  O OE1 . GLU D 509  ? 1.9012 1.1006 1.2470 -0.3417 -0.3317 -0.0022 506  GLU A OE1 
4930  O OE2 . GLU D 509  ? 1.8714 1.1570 1.2593 -0.3940 -0.3293 0.0231  506  GLU A OE2 
4931  N N   . MET D 510  ? 1.6233 1.0633 1.1706 -0.3235 -0.2588 0.0139  507  MET A N   
4932  C CA  . MET D 510  ? 1.5698 1.0770 1.1619 -0.3272 -0.2439 0.0227  507  MET A CA  
4933  C C   . MET D 510  ? 1.6041 1.1022 1.2070 -0.3002 -0.2327 0.0188  507  MET A C   
4934  O O   . MET D 510  ? 1.5531 1.0998 1.1896 -0.3014 -0.2211 0.0256  507  MET A O   
4935  C CB  . MET D 510  ? 1.4699 1.0502 1.1060 -0.3183 -0.2269 0.0207  507  MET A CB  
4936  C CG  . MET D 510  ? 1.4509 1.0604 1.0860 -0.3479 -0.2355 0.0277  507  MET A CG  
4937  S SD  . MET D 510  ? 1.4212 1.0901 1.0751 -0.3867 -0.2388 0.0479  507  MET A SD  
4938  C CE  . MET D 510  ? 1.3473 1.0878 1.0561 -0.3587 -0.2123 0.0466  507  MET A CE  
4939  N N   . GLU D 511  ? 1.7534 1.1919 1.3276 -0.2752 -0.2362 0.0080  508  GLU A N   
4940  C CA  . GLU D 511  ? 1.7611 1.1925 1.3446 -0.2481 -0.2257 0.0041  508  GLU A CA  
4941  C C   . GLU D 511  ? 1.7617 1.1829 1.3386 -0.2660 -0.2319 0.0152  508  GLU A C   
4942  O O   . GLU D 511  ? 1.7285 1.1846 1.3365 -0.2537 -0.2178 0.0172  508  GLU A O   
4943  C CB  . GLU D 511  ? 1.8471 1.2169 1.3963 -0.2176 -0.2301 -0.0091 508  GLU A CB  
4944  C CG  . GLU D 511  ? 1.8781 1.2330 1.4285 -0.1901 -0.2225 -0.0128 508  GLU A CG  
4945  C CD  . GLU D 511  ? 1.9565 1.2580 1.4734 -0.1574 -0.2261 -0.0257 508  GLU A CD  
4946  O OE1 . GLU D 511  ? 1.9606 1.2662 1.4778 -0.1437 -0.2230 -0.0343 508  GLU A OE1 
4947  O OE2 . GLU D 511  ? 2.0115 1.2679 1.5009 -0.1444 -0.2323 -0.0272 508  GLU A OE2 
4948  N N   . PRO D 512  ? 1.6802 1.0546 1.2174 -0.2950 -0.2525 0.0231  509  PRO A N   
4949  C CA  . PRO D 512  ? 1.6292 0.9970 1.1616 -0.3124 -0.2577 0.0345  509  PRO A CA  
4950  C C   . PRO D 512  ? 1.5548 1.0001 1.1325 -0.3311 -0.2467 0.0467  509  PRO A C   
4951  O O   . PRO D 512  ? 1.5651 1.0150 1.1468 -0.3401 -0.2469 0.0554  509  PRO A O   
4952  C CB  . PRO D 512  ? 1.6799 0.9854 1.1590 -0.3423 -0.2830 0.0413  509  PRO A CB  
4953  C CG  . PRO D 512  ? 1.7256 0.9857 1.1738 -0.3248 -0.2896 0.0291  509  PRO A CG  
4954  C CD  . PRO D 512  ? 1.6999 1.0154 1.1885 -0.3108 -0.2734 0.0212  509  PRO A CD  
4955  N N   . SER D 513  ? 1.4472 0.9533 1.0574 -0.3358 -0.2373 0.0475  510  SER A N   
4956  C CA  . SER D 513  ? 1.3097 0.8909 0.9604 -0.3504 -0.2268 0.0586  510  SER A CA  
4957  C C   . SER D 513  ? 1.1901 0.8068 0.8774 -0.3223 -0.2069 0.0549  510  SER A C   
4958  O O   . SER D 513  ? 1.1464 0.8106 0.8590 -0.3325 -0.2005 0.0647  510  SER A O   
4959  C CB  . SER D 513  ? 1.2476 0.8826 0.9196 -0.3602 -0.2227 0.0599  510  SER A CB  
4960  O OG  . SER D 513  ? 1.1990 0.8429 0.8870 -0.3285 -0.2096 0.0460  510  SER A OG  
4961  N N   . LEU D 514  ? 1.1545 0.7506 0.8440 -0.2875 -0.1975 0.0415  511  LEU A N   
4962  C CA  . LEU D 514  ? 1.1010 0.7277 0.8225 -0.2624 -0.1800 0.0384  511  LEU A CA  
4963  C C   . LEU D 514  ? 1.1507 0.7531 0.8615 -0.2658 -0.1840 0.0445  511  LEU A C   
4964  O O   . LEU D 514  ? 1.1336 0.7770 0.8719 -0.2664 -0.1744 0.0507  511  LEU A O   
4965  C CB  . LEU D 514  ? 1.0676 0.6793 0.7919 -0.2268 -0.1703 0.0239  511  LEU A CB  
4966  C CG  . LEU D 514  ? 1.0173 0.6529 0.7694 -0.2005 -0.1537 0.0202  511  LEU A CG  
4967  C CD1 . LEU D 514  ? 0.9593 0.6637 0.7524 -0.2037 -0.1401 0.0253  511  LEU A CD1 
4968  C CD2 . LEU D 514  ? 1.0121 0.6309 0.7621 -0.1685 -0.1466 0.0072  511  LEU A CD2 
4969  N N   . SER D 515  ? 1.2339 0.7678 0.9027 -0.2670 -0.1987 0.0426  512  SER A N   
4970  C CA  . SER D 515  ? 1.2512 0.7574 0.9058 -0.2708 -0.2040 0.0486  512  SER A CA  
4971  C C   . SER D 515  ? 1.2373 0.7650 0.8930 -0.3081 -0.2124 0.0646  512  SER A C   
4972  O O   . SER D 515  ? 1.2332 0.7705 0.8972 -0.3115 -0.2099 0.0717  512  SER A O   
4973  C CB  . SER D 515  ? 1.3316 0.7555 0.9355 -0.2623 -0.2193 0.0425  512  SER A CB  
4974  O OG  . SER D 515  ? 1.4191 0.8038 0.9856 -0.2903 -0.2389 0.0470  512  SER A OG  
4975  N N   . PHE D 516  ? 1.2263 0.7645 0.8738 -0.3365 -0.2223 0.0711  513  PHE A N   
4976  C CA  . PHE D 516  ? 1.2402 0.8087 0.8911 -0.3734 -0.2298 0.0878  513  PHE A CA  
4977  C C   . PHE D 516  ? 1.1738 0.8238 0.8740 -0.3699 -0.2121 0.0933  513  PHE A C   
4978  O O   . PHE D 516  ? 1.1719 0.8472 0.8793 -0.3897 -0.2140 0.1062  513  PHE A O   
4979  C CB  . PHE D 516  ? 1.2812 0.8478 0.9131 -0.4047 -0.2444 0.0938  513  PHE A CB  
4980  C CG  . PHE D 516  ? 1.3794 0.8787 0.9596 -0.4222 -0.2652 0.0987  513  PHE A CG  
4981  C CD1 . PHE D 516  ? 1.4295 0.8691 0.9810 -0.4083 -0.2708 0.0957  513  PHE A CD1 
4982  C CD2 . PHE D 516  ? 1.4123 0.9156 0.9734 -0.4454 -0.2764 0.1069  513  PHE A CD2 
4983  C CE1 . PHE D 516  ? 1.4980 0.8818 1.0015 -0.4169 -0.2878 0.1002  513  PHE A CE1 
4984  C CE2 . PHE D 516  ? 1.4901 0.9363 1.0032 -0.4558 -0.2936 0.1120  513  PHE A CE2 
4985  C CZ  . PHE D 516  ? 1.5367 0.9225 1.0202 -0.4414 -0.2996 0.1084  513  PHE A CZ  
4986  N N   . TYR D 517  ? 1.1354 0.8259 0.8676 -0.3448 -0.1954 0.0840  514  TYR A N   
4987  C CA  . TYR D 517  ? 1.0622 0.8229 0.8368 -0.3367 -0.1787 0.0876  514  TYR A CA  
4988  C C   . TYR D 517  ? 1.0617 0.8146 0.8444 -0.3209 -0.1715 0.0874  514  TYR A C   
4989  O O   . TYR D 517  ? 1.0537 0.8451 0.8538 -0.3307 -0.1676 0.0973  514  TYR A O   
4990  C CB  . TYR D 517  ? 1.0011 0.7966 0.8021 -0.3121 -0.1640 0.0768  514  TYR A CB  
4991  C CG  . TYR D 517  ? 0.9356 0.8029 0.7752 -0.3055 -0.1488 0.0807  514  TYR A CG  
4992  C CD1 . TYR D 517  ? 0.8918 0.7717 0.7517 -0.2826 -0.1357 0.0771  514  TYR A CD1 
4993  C CD2 . TYR D 517  ? 0.9181 0.8405 0.7720 -0.3213 -0.1482 0.0881  514  TYR A CD2 
4994  C CE1 . TYR D 517  ? 0.8508 0.7910 0.7413 -0.2753 -0.1231 0.0802  514  TYR A CE1 
4995  C CE2 . TYR D 517  ? 0.8555 0.8414 0.7407 -0.3122 -0.1349 0.0911  514  TYR A CE2 
4996  C CZ  . TYR D 517  ? 0.8408 0.8330 0.7430 -0.2890 -0.1227 0.0869  514  TYR A CZ  
4997  O OH  . TYR D 517  ? 0.8345 0.8850 0.7635 -0.2788 -0.1107 0.0894  514  TYR A OH  
4998  N N   . ASN D 518  ? 1.0907 0.7961 0.8605 -0.2958 -0.1698 0.0763  515  ASN A N   
4999  C CA  . ASN D 518  ? 1.1120 0.8103 0.8891 -0.2796 -0.1630 0.0757  515  ASN A CA  
5000  C C   . ASN D 518  ? 1.1761 0.8420 0.9280 -0.3017 -0.1766 0.0865  515  ASN A C   
5001  O O   . ASN D 518  ? 1.1901 0.8776 0.9567 -0.3026 -0.1714 0.0930  515  ASN A O   
5002  C CB  . ASN D 518  ? 1.1385 0.7990 0.9076 -0.2469 -0.1580 0.0618  515  ASN A CB  
5003  C CG  . ASN D 518  ? 1.0988 0.7985 0.8986 -0.2232 -0.1417 0.0526  515  ASN A CG  
5004  O OD1 . ASN D 518  ? 1.0604 0.8148 0.8917 -0.2232 -0.1306 0.0559  515  ASN A OD1 
5005  N ND2 . ASN D 518  ? 1.1062 0.7772 0.8949 -0.2025 -0.1407 0.0411  515  ASN A ND2 
5006  N N   . LYS D 519  ? 1.2200 0.8320 0.9319 -0.3200 -0.1947 0.0887  516  LYS A N   
5007  C CA  . LYS D 519  ? 1.2473 0.8236 0.9305 -0.3435 -0.2095 0.0998  516  LYS A CA  
5008  C C   . LYS D 519  ? 1.2065 0.8383 0.9086 -0.3742 -0.2101 0.1160  516  LYS A C   
5009  O O   . LYS D 519  ? 1.1970 0.8284 0.8968 -0.3847 -0.2127 0.1255  516  LYS A O   
5010  C CB  . LYS D 519  ? 1.3453 0.8506 0.9779 -0.3590 -0.2304 0.0992  516  LYS A CB  
5011  C CG  . LYS D 519  ? 1.4126 0.8490 1.0141 -0.3297 -0.2341 0.0859  516  LYS A CG  
5012  C CD  . LYS D 519  ? 1.5312 0.8924 1.0764 -0.3473 -0.2573 0.0866  516  LYS A CD  
5013  C CE  . LYS D 519  ? 1.5875 0.8788 1.0974 -0.3152 -0.2617 0.0734  516  LYS A CE  
5014  N NZ  . LYS D 519  ? 1.6601 0.8923 1.1170 -0.3218 -0.2806 0.0737  516  LYS A NZ  
5015  N N   . ALA D 520  ? 1.1674 0.8497 0.8879 -0.3881 -0.2076 0.1198  517  ALA A N   
5016  C CA  . ALA D 520  ? 1.1122 0.8537 0.8501 -0.4166 -0.2083 0.1359  517  ALA A CA  
5017  C C   . ALA D 520  ? 1.0455 0.8466 0.8238 -0.3989 -0.1900 0.1369  517  ALA A C   
5018  O O   . ALA D 520  ? 1.0620 0.8916 0.8474 -0.4154 -0.1911 0.1497  517  ALA A O   
5019  C CB  . ALA D 520  ? 1.0579 0.8381 0.8021 -0.4348 -0.2112 0.1396  517  ALA A CB  
5020  N N   . ARG D 521  ? 0.9843 0.8043 0.7877 -0.3658 -0.1739 0.1240  518  ARG A N   
5021  C CA  . ARG D 521  ? 0.9605 0.8308 0.7983 -0.3478 -0.1575 0.1240  518  ARG A CA  
5022  C C   . ARG D 521  ? 1.0014 0.8429 0.8329 -0.3407 -0.1574 0.1255  518  ARG A C   
5023  O O   . ARG D 521  ? 0.9751 0.8549 0.8249 -0.3429 -0.1513 0.1332  518  ARG A O   
5024  C CB  . ARG D 521  ? 0.9221 0.8099 0.7825 -0.3156 -0.1423 0.1099  518  ARG A CB  
5025  C CG  . ARG D 521  ? 0.8758 0.8039 0.7663 -0.2944 -0.1265 0.1082  518  ARG A CG  
5026  C CD  . ARG D 521  ? 0.8625 0.7990 0.7699 -0.2644 -0.1134 0.0945  518  ARG A CD  
5027  N NE  . ARG D 521  ? 0.9003 0.7821 0.7887 -0.2521 -0.1172 0.0836  518  ARG A NE  
5028  C CZ  . ARG D 521  ? 0.9129 0.7529 0.7905 -0.2377 -0.1174 0.0784  518  ARG A CZ  
5029  N NH1 . ARG D 521  ? 0.9275 0.7722 0.8117 -0.2351 -0.1143 0.0830  518  ARG A NH1 
5030  N NH2 . ARG D 521  ? 0.9114 0.7065 0.7707 -0.2248 -0.1208 0.0687  518  ARG A NH2 
5031  N N   . ASN D 522  ? 1.0637 0.8385 0.8681 -0.3310 -0.1644 0.1182  519  ASN A N   
5032  C CA  . ASN D 522  ? 1.0821 0.8274 0.8785 -0.3219 -0.1645 0.1189  519  ASN A CA  
5033  C C   . ASN D 522  ? 1.1309 0.8718 0.9120 -0.3524 -0.1764 0.1346  519  ASN A C   
5034  O O   . ASN D 522  ? 1.1617 0.8938 0.9429 -0.3472 -0.1747 0.1377  519  ASN A O   
5035  C CB  . ASN D 522  ? 1.1012 0.7765 0.8683 -0.3034 -0.1703 0.1077  519  ASN A CB  
5036  C CG  . ASN D 522  ? 1.0336 0.7158 0.8175 -0.2710 -0.1574 0.0928  519  ASN A CG  
5037  O OD1 . ASN D 522  ? 0.9684 0.7021 0.7866 -0.2585 -0.1427 0.0904  519  ASN A OD1 
5038  N ND2 . ASN D 522  ? 1.0499 0.6793 0.8075 -0.2571 -0.1633 0.0831  519  ASN A ND2 
5039  N N   . TYR D 523  ? 1.1754 0.9234 0.9429 -0.3849 -0.1886 0.1453  520  TYR A N   
5040  C CA  . TYR D 523  ? 1.2227 0.9744 0.9769 -0.4176 -0.2001 0.1623  520  TYR A CA  
5041  C C   . TYR D 523  ? 1.1852 1.0199 0.9712 -0.4332 -0.1930 0.1745  520  TYR A C   
5042  O O   . TYR D 523  ? 1.1955 1.0547 0.9892 -0.4430 -0.1920 0.1854  520  TYR A O   
5043  C CB  . TYR D 523  ? 1.3044 1.0075 1.0160 -0.4415 -0.2199 0.1669  520  TYR A CB  
5044  C CG  . TYR D 523  ? 1.3878 1.1098 1.0869 -0.4656 -0.2289 0.1826  520  TYR A CG  
5045  C CD1 . TYR D 523  ? 1.4407 1.1318 1.1227 -0.4656 -0.2341 0.1869  520  TYR A CD1 
5046  C CD2 . TYR D 523  ? 1.4114 1.1838 1.1153 -0.4878 -0.2324 0.1934  520  TYR A CD2 
5047  C CE1 . TYR D 523  ? 1.4779 1.1864 1.1477 -0.4883 -0.2429 0.2014  520  TYR A CE1 
5048  C CE2 . TYR D 523  ? 1.4520 1.2431 1.1432 -0.5102 -0.2411 0.2085  520  TYR A CE2 
5049  C CZ  . TYR D 523  ? 1.4816 1.2400 1.1558 -0.5109 -0.2466 0.2124  520  TYR A CZ  
5050  O OH  . TYR D 523  ? 1.5091 1.2858 1.1697 -0.5338 -0.2559 0.2275  520  TYR A OH  
5051  N N   . ALA D 524  ? 0.8225 0.8225 0.8225 0.0000  0.0000  0.0000  521  ALA A N   
5052  C CA  . ALA D 524  ? 0.8225 0.8225 0.8225 0.0000  0.0000  0.0000  521  ALA A CA  
5053  C C   . ALA D 524  ? 0.8225 0.8225 0.8225 0.0000  0.0000  0.0000  521  ALA A C   
5054  O O   . ALA D 524  ? 0.8225 0.8225 0.8225 0.0000  0.0000  0.0000  521  ALA A O   
5055  C CB  . ALA D 524  ? 0.8225 0.8225 0.8225 0.0000  0.0000  0.0000  521  ALA A CB  
5056  N N   . THR D 525  ? 0.7836 0.7836 0.7836 0.0000  0.0000  0.0000  522  THR A N   
5057  C CA  . THR D 525  ? 0.7836 0.7836 0.7836 0.0000  0.0000  0.0000  522  THR A CA  
5058  C C   . THR D 525  ? 0.7836 0.7836 0.7836 0.0000  0.0000  0.0000  522  THR A C   
5059  O O   . THR D 525  ? 0.7836 0.7836 0.7836 0.0000  0.0000  0.0000  522  THR A O   
5060  C CB  . THR D 525  ? 0.7836 0.7836 0.7836 0.0000  0.0000  0.0000  522  THR A CB  
5061  O OG1 . THR D 525  ? 0.7836 0.7836 0.7836 0.0000  0.0000  0.0000  522  THR A OG1 
5062  C CG2 . THR D 525  ? 0.7836 0.7836 0.7836 0.0000  0.0000  0.0000  522  THR A CG2 
5063  N N   . LYS D 526  ? 0.7003 0.7003 0.7003 0.0000  0.0000  0.0000  523  LYS A N   
5064  C CA  . LYS D 526  ? 0.7003 0.7003 0.7003 0.0000  0.0000  0.0000  523  LYS A CA  
5065  C C   . LYS D 526  ? 0.7003 0.7003 0.7003 0.0000  0.0000  0.0000  523  LYS A C   
5066  O O   . LYS D 526  ? 0.7003 0.7003 0.7003 0.0000  0.0000  0.0000  523  LYS A O   
5067  C CB  . LYS D 526  ? 0.7003 0.7003 0.7003 0.0000  0.0000  0.0000  523  LYS A CB  
5068  C CG  . LYS D 526  ? 0.7003 0.7003 0.7003 0.0000  0.0000  0.0000  523  LYS A CG  
5069  C CD  . LYS D 526  ? 0.7003 0.7003 0.7003 0.0000  0.0000  0.0000  523  LYS A CD  
5070  C CE  . LYS D 526  ? 0.7003 0.7003 0.7003 0.0000  0.0000  0.0000  523  LYS A CE  
5071  N NZ  . LYS D 526  ? 0.7003 0.7003 0.7003 0.0000  0.0000  0.0000  523  LYS A NZ  
5072  N N   . LYS D 527  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  524  LYS A N   
5073  C CA  . LYS D 527  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  524  LYS A CA  
5074  C C   . LYS D 527  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  524  LYS A C   
5075  O O   . LYS D 527  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  524  LYS A O   
5081  N N   . PRO D 528  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  525  PRO A N   
5082  C CA  . PRO D 528  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  525  PRO A CA  
5083  C C   . PRO D 528  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  525  PRO A C   
5084  O O   . PRO D 528  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  525  PRO A O   
5085  C CB  . PRO D 528  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  525  PRO A CB  
5086  C CG  . PRO D 528  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  525  PRO A CG  
5087  C CD  . PRO D 528  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  525  PRO A CD  
5088  N N   . TYR D 529  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  526  TYR A N   
5089  C CA  . TYR D 529  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  526  TYR A CA  
5090  C C   . TYR D 529  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  526  TYR A C   
5091  O O   . TYR D 529  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  526  TYR A O   
5092  C CB  . TYR D 529  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  526  TYR A CB  
5093  C CG  . TYR D 529  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  526  TYR A CG  
5094  C CD1 . TYR D 529  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  526  TYR A CD1 
5095  C CD2 . TYR D 529  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  526  TYR A CD2 
5096  C CE1 . TYR D 529  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  526  TYR A CE1 
5097  C CE2 . TYR D 529  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  526  TYR A CE2 
5098  C CZ  . TYR D 529  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  526  TYR A CZ  
5099  O OH  . TYR D 529  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  526  TYR A OH  
5100  N N   . SER D 530  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  527  SER A N   
5101  C CA  . SER D 530  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  527  SER A CA  
5102  C C   . SER D 530  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  527  SER A C   
5103  O O   . SER D 530  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  527  SER A O   
5104  C CB  . SER D 530  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  527  SER A CB  
5105  O OG  . SER D 530  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  527  SER A OG  
5106  N N   . VAL D 531  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  528  VAL A N   
5107  C CA  . VAL D 531  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  528  VAL A CA  
5108  C C   . VAL D 531  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  528  VAL A C   
5109  O O   . VAL D 531  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  528  VAL A O   
5110  C CB  . VAL D 531  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  528  VAL A CB  
5111  C CG1 . VAL D 531  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  528  VAL A CG1 
5112  C CG2 . VAL D 531  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  528  VAL A CG2 
5113  N N   . GLU D 532  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  529  GLU A N   
5114  C CA  . GLU D 532  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  529  GLU A CA  
5115  C C   . GLU D 532  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  529  GLU A C   
5116  O O   . GLU D 532  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  529  GLU A O   
5117  C CB  . GLU D 532  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  529  GLU A CB  
5118  C CG  . GLU D 532  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  529  GLU A CG  
5119  C CD  . GLU D 532  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  529  GLU A CD  
5120  O OE1 . GLU D 532  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  529  GLU A OE1 
5121  O OE2 . GLU D 532  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  529  GLU A OE2 
5122  N N   . LYS D 533  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  530  LYS A N   
5123  C CA  . LYS D 533  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  530  LYS A CA  
5124  C C   . LYS D 533  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  530  LYS A C   
5125  O O   . LYS D 533  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  530  LYS A O   
5126  C CB  . LYS D 533  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  530  LYS A CB  
5127  C CG  . LYS D 533  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  530  LYS A CG  
5128  C CD  . LYS D 533  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  530  LYS A CD  
5129  C CE  . LYS D 533  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  530  LYS A CE  
5130  N NZ  . LYS D 533  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  530  LYS A NZ  
5131  N N   . PHE D 534  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  531  PHE A N   
5132  C CA  . PHE D 534  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  531  PHE A CA  
5133  C C   . PHE D 534  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  531  PHE A C   
5134  O O   . PHE D 534  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  531  PHE A O   
5135  C CB  . PHE D 534  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  531  PHE A CB  
5136  C CG  . PHE D 534  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  531  PHE A CG  
5137  C CD1 . PHE D 534  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  531  PHE A CD1 
5138  C CD2 . PHE D 534  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  531  PHE A CD2 
5139  C CE1 . PHE D 534  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  531  PHE A CE1 
5140  C CE2 . PHE D 534  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  531  PHE A CE2 
5141  C CZ  . PHE D 534  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  531  PHE A CZ  
5142  N N   . LYS D 535  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  532  LYS A N   
5143  C CA  . LYS D 535  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  532  LYS A CA  
5144  C C   . LYS D 535  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  532  LYS A C   
5145  O O   . LYS D 535  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  532  LYS A O   
5146  C CB  . LYS D 535  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  532  LYS A CB  
5147  C CG  . LYS D 535  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  532  LYS A CG  
5148  C CD  . LYS D 535  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  532  LYS A CD  
5149  C CE  . LYS D 535  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  532  LYS A CE  
5150  N NZ  . LYS D 535  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  532  LYS A NZ  
5151  N N   . LEU D 536  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  533  LEU A N   
5152  C CA  . LEU D 536  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  533  LEU A CA  
5153  C C   . LEU D 536  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  533  LEU A C   
5154  O O   . LEU D 536  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  533  LEU A O   
5155  C CB  . LEU D 536  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  533  LEU A CB  
5156  C CG  . LEU D 536  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  533  LEU A CG  
5157  C CD1 . LEU D 536  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  533  LEU A CD1 
5158  C CD2 . LEU D 536  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  533  LEU A CD2 
5159  N N   . ASN D 537  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  534  ASN A N   
5160  C CA  . ASN D 537  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  534  ASN A CA  
5161  C C   . ASN D 537  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  534  ASN A C   
5162  O O   . ASN D 537  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  534  ASN A O   
5163  C CB  . ASN D 537  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  534  ASN A CB  
5164  C CG  . ASN D 537  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  534  ASN A CG  
5165  O OD1 . ASN D 537  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  534  ASN A OD1 
5166  N ND2 . ASN D 537  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  534  ASN A ND2 
5167  N N   . PHE D 538  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  535  PHE A N   
5168  C CA  . PHE D 538  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  535  PHE A CA  
5169  C C   . PHE D 538  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  535  PHE A C   
5170  O O   . PHE D 538  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  535  PHE A O   
5171  C CB  . PHE D 538  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  535  PHE A CB  
5172  C CG  . PHE D 538  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  535  PHE A CG  
5173  C CD1 . PHE D 538  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  535  PHE A CD1 
5174  C CD2 . PHE D 538  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  535  PHE A CD2 
5175  C CE1 . PHE D 538  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  535  PHE A CE1 
5176  C CE2 . PHE D 538  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  535  PHE A CE2 
5177  C CZ  . PHE D 538  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  535  PHE A CZ  
5178  N N   . GLN D 539  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  536  GLN A N   
5179  C CA  . GLN D 539  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  536  GLN A CA  
5180  C C   . GLN D 539  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  536  GLN A C   
5181  O O   . GLN D 539  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  536  GLN A O   
5182  C CB  . GLN D 539  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  536  GLN A CB  
5183  C CG  . GLN D 539  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  536  GLN A CG  
5184  C CD  . GLN D 539  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  536  GLN A CD  
5185  O OE1 . GLN D 539  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  536  GLN A OE1 
5186  N NE2 . GLN D 539  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  536  GLN A NE2 
5187  N N   . MET D 540  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  537  MET A N   
5188  C CA  . MET D 540  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  537  MET A CA  
5189  C C   . MET D 540  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  537  MET A C   
5190  O O   . MET D 540  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  537  MET A O   
5191  C CB  . MET D 540  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  537  MET A CB  
5192  C CG  . MET D 540  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  537  MET A CG  
5193  S SD  . MET D 540  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  537  MET A SD  
5194  C CE  . MET D 540  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  537  MET A CE  
5195  N N   . PRO D 541  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  538  PRO A N   
5196  C CA  . PRO D 541  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  538  PRO A CA  
5197  C C   . PRO D 541  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  538  PRO A C   
5198  O O   . PRO D 541  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  538  PRO A O   
5199  C CB  . PRO D 541  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  538  PRO A CB  
5200  C CG  . PRO D 541  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  538  PRO A CG  
5201  C CD  . PRO D 541  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  538  PRO A CD  
5202  N N   . THR D 542  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  539  THR A N   
5203  C CA  . THR D 542  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  539  THR A CA  
5204  C C   . THR D 542  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  539  THR A C   
5205  O O   . THR D 542  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  539  THR A O   
5206  C CB  . THR D 542  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  539  THR A CB  
5207  O OG1 . THR D 542  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  539  THR A OG1 
5208  C CG2 . THR D 542  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  539  THR A CG2 
5209  N N   . LEU D 543  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  540  LEU A N   
5210  C CA  . LEU D 543  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  540  LEU A CA  
5211  C C   . LEU D 543  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  540  LEU A C   
5212  O O   . LEU D 543  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  540  LEU A O   
5213  C CB  . LEU D 543  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  540  LEU A CB  
5214  C CG  . LEU D 543  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  540  LEU A CG  
5215  C CD1 . LEU D 543  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  540  LEU A CD1 
5216  C CD2 . LEU D 543  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  540  LEU A CD2 
5217  N N   . ALA D 544  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  541  ALA A N   
5218  C CA  . ALA D 544  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  541  ALA A CA  
5219  C C   . ALA D 544  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  541  ALA A C   
5220  O O   . ALA D 544  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  541  ALA A O   
5221  C CB  . ALA D 544  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  541  ALA A CB  
5222  N N   . SER D 545  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  542  SER A N   
5223  C CA  . SER D 545  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  542  SER A CA  
5224  C C   . SER D 545  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  542  SER A C   
5225  O O   . SER D 545  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  542  SER A O   
5226  C CB  . SER D 545  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  542  SER A CB  
5227  O OG  . SER D 545  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  542  SER A OG  
5228  N N   . GLY D 546  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  543  GLY A N   
5229  C CA  . GLY D 546  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  543  GLY A CA  
5230  C C   . GLY D 546  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  543  GLY A C   
5231  O O   . GLY D 546  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  543  GLY A O   
5232  N N   . TRP D 547  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  544  TRP A N   
5233  C CA  . TRP D 547  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  544  TRP A CA  
5234  C C   . TRP D 547  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  544  TRP A C   
5235  O O   . TRP D 547  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  544  TRP A O   
5236  C CB  . TRP D 547  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  544  TRP A CB  
5237  C CG  . TRP D 547  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  544  TRP A CG  
5238  C CD1 . TRP D 547  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  544  TRP A CD1 
5239  C CD2 . TRP D 547  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  544  TRP A CD2 
5240  N NE1 . TRP D 547  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  544  TRP A NE1 
5241  C CE2 . TRP D 547  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  544  TRP A CE2 
5242  C CE3 . TRP D 547  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  544  TRP A CE3 
5243  C CZ2 . TRP D 547  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  544  TRP A CZ2 
5244  C CZ3 . TRP D 547  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  544  TRP A CZ3 
5245  C CH2 . TRP D 547  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  544  TRP A CH2 
5246  N N   . ASP D 548  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  545  ASP A N   
5247  C CA  . ASP D 548  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  545  ASP A CA  
5248  C C   . ASP D 548  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  545  ASP A C   
5249  O O   . ASP D 548  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  545  ASP A O   
5250  C CB  . ASP D 548  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  545  ASP A CB  
5251  C CG  . ASP D 548  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  545  ASP A CG  
5252  O OD1 . ASP D 548  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  545  ASP A OD1 
5253  O OD2 . ASP D 548  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  545  ASP A OD2 
5254  N N   . VAL D 549  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  546  VAL A N   
5255  C CA  . VAL D 549  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  546  VAL A CA  
5256  C C   . VAL D 549  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  546  VAL A C   
5257  O O   . VAL D 549  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  546  VAL A O   
5258  C CB  . VAL D 549  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  546  VAL A CB  
5259  C CG1 . VAL D 549  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  546  VAL A CG1 
5260  C CG2 . VAL D 549  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  546  VAL A CG2 
5261  N N   . ASN D 550  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  547  ASN A N   
5262  C CA  . ASN D 550  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  547  ASN A CA  
5263  C C   . ASN D 550  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  547  ASN A C   
5264  O O   . ASN D 550  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  547  ASN A O   
5265  C CB  . ASN D 550  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  547  ASN A CB  
5266  C CG  . ASN D 550  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  547  ASN A CG  
5267  O OD1 . ASN D 550  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  547  ASN A OD1 
5268  N ND2 . ASN D 550  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  547  ASN A ND2 
5269  N N   . LYS D 551  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  548  LYS A N   
5270  C CA  . LYS D 551  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  548  LYS A CA  
5271  C C   . LYS D 551  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  548  LYS A C   
5272  O O   . LYS D 551  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  548  LYS A O   
5273  C CB  . LYS D 551  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  548  LYS A CB  
5274  C CG  . LYS D 551  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  548  LYS A CG  
5275  C CD  . LYS D 551  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  548  LYS A CD  
5276  C CE  . LYS D 551  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  548  LYS A CE  
5277  N NZ  . LYS D 551  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  548  LYS A NZ  
5278  N N   . GLU D 552  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  549  GLU A N   
5279  C CA  . GLU D 552  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  549  GLU A CA  
5280  C C   . GLU D 552  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  549  GLU A C   
5281  O O   . GLU D 552  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  549  GLU A O   
5282  C CB  . GLU D 552  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  549  GLU A CB  
5283  C CG  . GLU D 552  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  549  GLU A CG  
5284  C CD  . GLU D 552  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  549  GLU A CD  
5285  O OE1 . GLU D 552  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  549  GLU A OE1 
5286  O OE2 . GLU D 552  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  549  GLU A OE2 
5287  N N   . LYS D 553  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  550  LYS A N   
5288  C CA  . LYS D 553  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  550  LYS A CA  
5289  C C   . LYS D 553  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  550  LYS A C   
5290  O O   . LYS D 553  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  550  LYS A O   
5291  C CB  . LYS D 553  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  550  LYS A CB  
5292  C CG  . LYS D 553  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  550  LYS A CG  
5293  C CD  . LYS D 553  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  550  LYS A CD  
5294  C CE  . LYS D 553  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  550  LYS A CE  
5295  N NZ  . LYS D 553  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  550  LYS A NZ  
5296  N N   . CYS D 554  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  551  CYS A N   
5297  C CA  . CYS D 554  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  551  CYS A CA  
5298  C C   . CYS D 554  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  551  CYS A C   
5299  O O   . CYS D 554  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  551  CYS A O   
5302  N N   . ASN D 555  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  552  ASN A N   
5303  C CA  . ASN D 555  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  552  ASN A CA  
5304  C C   . ASN D 555  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  552  ASN A C   
5305  O O   . ASN D 555  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  552  ASN A O   
5306  C CB  . ASN D 555  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  552  ASN A CB  
5307  C CG  . ASN D 555  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  552  ASN A CG  
5308  O OD1 . ASN D 555  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  552  ASN A OD1 
5309  N ND2 . ASN D 555  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  552  ASN A ND2 
5310  N N   . GLY D 556  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  553  GLY A N   
5311  C CA  . GLY D 556  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  553  GLY A CA  
5312  C C   . GLY D 556  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  553  GLY A C   
5313  O O   . GLY D 556  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  553  GLY A O   
5314  N N   . ALA D 557  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  554  ALA A N   
5315  C CA  . ALA D 557  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  554  ALA A CA  
5316  C C   . ALA D 557  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  554  ALA A C   
5317  O O   . ALA D 557  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  554  ALA A O   
5318  C CB  . ALA D 557  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  554  ALA A CB  
5319  N N   . ILE D 558  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  555  ILE A N   
5320  C CA  . ILE D 558  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  555  ILE A CA  
5321  C C   . ILE D 558  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  555  ILE A C   
5322  O O   . ILE D 558  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  555  ILE A O   
5323  C CB  . ILE D 558  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  555  ILE A CB  
5324  C CG1 . ILE D 558  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  555  ILE A CG1 
5325  C CG2 . ILE D 558  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  555  ILE A CG2 
5326  C CD1 . ILE D 558  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  555  ILE A CD1 
5327  N N   . LEU D 559  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  556  LEU A N   
5328  C CA  . LEU D 559  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  556  LEU A CA  
5329  C C   . LEU D 559  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  556  LEU A C   
5330  O O   . LEU D 559  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  556  LEU A O   
5331  C CB  . LEU D 559  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  556  LEU A CB  
5332  C CG  . LEU D 559  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  556  LEU A CG  
5333  C CD1 . LEU D 559  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  556  LEU A CD1 
5334  C CD2 . LEU D 559  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  556  LEU A CD2 
5335  N N   . PHE D 560  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  557  PHE A N   
5336  C CA  . PHE D 560  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  557  PHE A CA  
5337  C C   . PHE D 560  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  557  PHE A C   
5338  O O   . PHE D 560  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  557  PHE A O   
5339  C CB  . PHE D 560  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  557  PHE A CB  
5340  C CG  . PHE D 560  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  557  PHE A CG  
5341  C CD1 . PHE D 560  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  557  PHE A CD1 
5342  C CD2 . PHE D 560  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  557  PHE A CD2 
5343  C CE1 . PHE D 560  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  557  PHE A CE1 
5344  C CE2 . PHE D 560  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  557  PHE A CE2 
5345  C CZ  . PHE D 560  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  557  PHE A CZ  
5346  N N   . VAL D 561  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  558  VAL A N   
5347  C CA  . VAL D 561  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  558  VAL A CA  
5348  C C   . VAL D 561  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  558  VAL A C   
5349  O O   . VAL D 561  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  558  VAL A O   
5350  C CB  . VAL D 561  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  558  VAL A CB  
5351  C CG1 . VAL D 561  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  558  VAL A CG1 
5352  C CG2 . VAL D 561  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  558  VAL A CG2 
5353  N N   . LYS D 562  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  559  LYS A N   
5354  C CA  . LYS D 562  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  559  LYS A CA  
5355  C C   . LYS D 562  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  559  LYS A C   
5356  O O   . LYS D 562  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  559  LYS A O   
5357  C CB  . LYS D 562  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  559  LYS A CB  
5358  C CG  . LYS D 562  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  559  LYS A CG  
5359  C CD  . LYS D 562  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  559  LYS A CD  
5360  C CE  . LYS D 562  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  559  LYS A CE  
5361  N NZ  . LYS D 562  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  559  LYS A NZ  
5362  N N   . ASN D 563  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  560  ASN A N   
5363  C CA  . ASN D 563  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  560  ASN A CA  
5364  C C   . ASN D 563  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  560  ASN A C   
5365  O O   . ASN D 563  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  560  ASN A O   
5366  C CB  . ASN D 563  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  560  ASN A CB  
5367  C CG  . ASN D 563  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  560  ASN A CG  
5368  O OD1 . ASN D 563  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  560  ASN A OD1 
5369  N ND2 . ASN D 563  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  560  ASN A ND2 
5370  N N   . GLY D 564  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  561  GLY A N   
5371  C CA  . GLY D 564  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  561  GLY A CA  
5372  C C   . GLY D 564  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  561  GLY A C   
5373  O O   . GLY D 564  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  561  GLY A O   
5374  N N   . LEU D 565  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  562  LEU A N   
5375  C CA  . LEU D 565  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  562  LEU A CA  
5376  C C   . LEU D 565  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  562  LEU A C   
5377  O O   . LEU D 565  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  562  LEU A O   
5378  C CB  . LEU D 565  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  562  LEU A CB  
5379  C CG  . LEU D 565  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  562  LEU A CG  
5380  C CD1 . LEU D 565  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  562  LEU A CD1 
5381  C CD2 . LEU D 565  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  562  LEU A CD2 
5382  N N   . TYR D 566  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  563  TYR A N   
5383  C CA  . TYR D 566  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  563  TYR A CA  
5384  C C   . TYR D 566  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  563  TYR A C   
5385  O O   . TYR D 566  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  563  TYR A O   
5386  C CB  . TYR D 566  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  563  TYR A CB  
5387  C CG  . TYR D 566  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  563  TYR A CG  
5388  C CD1 . TYR D 566  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  563  TYR A CD1 
5389  C CD2 . TYR D 566  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  563  TYR A CD2 
5390  C CE1 . TYR D 566  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  563  TYR A CE1 
5391  C CE2 . TYR D 566  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  563  TYR A CE2 
5392  C CZ  . TYR D 566  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  563  TYR A CZ  
5393  O OH  . TYR D 566  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  563  TYR A OH  
5394  N N   . TYR D 567  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  564  TYR A N   
5395  C CA  . TYR D 567  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  564  TYR A CA  
5396  C C   . TYR D 567  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  564  TYR A C   
5397  O O   . TYR D 567  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  564  TYR A O   
5398  C CB  . TYR D 567  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  564  TYR A CB  
5399  C CG  . TYR D 567  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  564  TYR A CG  
5400  C CD1 . TYR D 567  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  564  TYR A CD1 
5401  C CD2 . TYR D 567  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  564  TYR A CD2 
5402  C CE1 . TYR D 567  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  564  TYR A CE1 
5403  C CE2 . TYR D 567  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  564  TYR A CE2 
5404  C CZ  . TYR D 567  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  564  TYR A CZ  
5405  O OH  . TYR D 567  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  564  TYR A OH  
5406  N N   . LEU D 568  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  565  LEU A N   
5407  C CA  . LEU D 568  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  565  LEU A CA  
5408  C C   . LEU D 568  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  565  LEU A C   
5409  O O   . LEU D 568  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  565  LEU A O   
5410  C CB  . LEU D 568  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  565  LEU A CB  
5411  C CG  . LEU D 568  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  565  LEU A CG  
5412  C CD1 . LEU D 568  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  565  LEU A CD1 
5413  C CD2 . LEU D 568  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  565  LEU A CD2 
5414  N N   . GLY D 569  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  566  GLY A N   
5415  C CA  . GLY D 569  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  566  GLY A CA  
5416  C C   . GLY D 569  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  566  GLY A C   
5417  O O   . GLY D 569  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  566  GLY A O   
5418  N N   . ILE D 570  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  567  ILE A N   
5419  C CA  . ILE D 570  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  567  ILE A CA  
5420  C C   . ILE D 570  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  567  ILE A C   
5421  O O   . ILE D 570  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  567  ILE A O   
5422  C CB  . ILE D 570  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  567  ILE A CB  
5423  C CG1 . ILE D 570  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  567  ILE A CG1 
5424  C CG2 . ILE D 570  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  567  ILE A CG2 
5425  C CD1 . ILE D 570  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  567  ILE A CD1 
5426  N N   . MET D 571  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  568  MET A N   
5427  C CA  . MET D 571  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  568  MET A CA  
5428  C C   . MET D 571  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  568  MET A C   
5429  O O   . MET D 571  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  568  MET A O   
5430  C CB  . MET D 571  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  568  MET A CB  
5431  C CG  . MET D 571  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  568  MET A CG  
5432  S SD  . MET D 571  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  568  MET A SD  
5433  C CE  . MET D 571  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  568  MET A CE  
5434  N N   . PRO D 572  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  569  PRO A N   
5435  C CA  . PRO D 572  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  569  PRO A CA  
5436  C C   . PRO D 572  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  569  PRO A C   
5437  O O   . PRO D 572  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  569  PRO A O   
5438  C CB  . PRO D 572  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  569  PRO A CB  
5439  C CG  . PRO D 572  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  569  PRO A CG  
5440  C CD  . PRO D 572  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  569  PRO A CD  
5441  N N   . LYS D 573  ? 0.6975 0.6975 0.6975 0.0000  0.0000  0.0000  570  LYS A N   
5442  C CA  . LYS D 573  ? 0.6975 0.6975 0.6975 0.0000  0.0000  0.0000  570  LYS A CA  
5443  C C   . LYS D 573  ? 0.6975 0.6975 0.6975 0.0000  0.0000  0.0000  570  LYS A C   
5444  O O   . LYS D 573  ? 0.6975 0.6975 0.6975 0.0000  0.0000  0.0000  570  LYS A O   
5445  C CB  . LYS D 573  ? 0.6975 0.6975 0.6975 0.0000  0.0000  0.0000  570  LYS A CB  
5446  C CG  . LYS D 573  ? 0.6975 0.6975 0.6975 0.0000  0.0000  0.0000  570  LYS A CG  
5447  C CD  . LYS D 573  ? 0.6975 0.6975 0.6975 0.0000  0.0000  0.0000  570  LYS A CD  
5448  C CE  . LYS D 573  ? 0.6975 0.6975 0.6975 0.0000  0.0000  0.0000  570  LYS A CE  
5449  N NZ  . LYS D 573  ? 0.6975 0.6975 0.6975 0.0000  0.0000  0.0000  570  LYS A NZ  
5450  N N   . GLN D 574  ? 0.8114 0.8114 0.8114 0.0000  0.0000  0.0000  571  GLN A N   
5451  C CA  . GLN D 574  ? 0.8114 0.8114 0.8114 0.0000  0.0000  0.0000  571  GLN A CA  
5452  C C   . GLN D 574  ? 0.8114 0.8114 0.8114 0.0000  0.0000  0.0000  571  GLN A C   
5453  O O   . GLN D 574  ? 0.8114 0.8114 0.8114 0.0000  0.0000  0.0000  571  GLN A O   
5454  C CB  . GLN D 574  ? 0.8114 0.8114 0.8114 0.0000  0.0000  0.0000  571  GLN A CB  
5455  C CG  . GLN D 574  ? 0.8114 0.8114 0.8114 0.0000  0.0000  0.0000  571  GLN A CG  
5456  C CD  . GLN D 574  ? 0.8114 0.8114 0.8114 0.0000  0.0000  0.0000  571  GLN A CD  
5457  O OE1 . GLN D 574  ? 0.8114 0.8114 0.8114 0.0000  0.0000  0.0000  571  GLN A OE1 
5458  N NE2 . GLN D 574  ? 0.8114 0.8114 0.8114 0.0000  0.0000  0.0000  571  GLN A NE2 
5459  N N   . LYS D 575  ? 0.9333 0.9333 0.9333 0.0000  0.0000  0.0000  572  LYS A N   
5460  C CA  . LYS D 575  ? 0.9333 0.9333 0.9333 0.0000  0.0000  0.0000  572  LYS A CA  
5461  C C   . LYS D 575  ? 0.9333 0.9333 0.9333 0.0000  0.0000  0.0000  572  LYS A C   
5462  O O   . LYS D 575  ? 0.9333 0.9333 0.9333 0.0000  0.0000  0.0000  572  LYS A O   
5468  N N   . GLY D 576  ? 0.9580 0.9580 0.9580 0.0000  0.0000  0.0000  573  GLY A N   
5469  C CA  . GLY D 576  ? 0.9580 0.9580 0.9580 0.0000  0.0000  0.0000  573  GLY A CA  
5470  C C   . GLY D 576  ? 0.9580 0.9580 0.9580 0.0000  0.0000  0.0000  573  GLY A C   
5471  O O   . GLY D 576  ? 0.9580 0.9580 0.9580 0.0000  0.0000  0.0000  573  GLY A O   
5472  N N   . ARG D 577  ? 0.9353 0.9353 0.9353 0.0000  0.0000  0.0000  574  ARG A N   
5473  C CA  . ARG D 577  ? 0.9353 0.9353 0.9353 0.0000  0.0000  0.0000  574  ARG A CA  
5474  C C   . ARG D 577  ? 0.9353 0.9353 0.9353 0.0000  0.0000  0.0000  574  ARG A C   
5475  O O   . ARG D 577  ? 0.9353 0.9353 0.9353 0.0000  0.0000  0.0000  574  ARG A O   
5483  N N   . TYR D 578  ? 0.8579 0.8579 0.8579 0.0000  0.0000  0.0000  575  TYR A N   
5484  C CA  . TYR D 578  ? 0.8579 0.8579 0.8579 0.0000  0.0000  0.0000  575  TYR A CA  
5485  C C   . TYR D 578  ? 0.8579 0.8579 0.8579 0.0000  0.0000  0.0000  575  TYR A C   
5486  O O   . TYR D 578  ? 0.8579 0.8579 0.8579 0.0000  0.0000  0.0000  575  TYR A O   
5487  C CB  . TYR D 578  ? 0.8579 0.8579 0.8579 0.0000  0.0000  0.0000  575  TYR A CB  
5488  C CG  . TYR D 578  ? 0.8579 0.8579 0.8579 0.0000  0.0000  0.0000  575  TYR A CG  
5489  C CD1 . TYR D 578  ? 0.8579 0.8579 0.8579 0.0000  0.0000  0.0000  575  TYR A CD1 
5490  C CD2 . TYR D 578  ? 0.8579 0.8579 0.8579 0.0000  0.0000  0.0000  575  TYR A CD2 
5491  C CE1 . TYR D 578  ? 0.8579 0.8579 0.8579 0.0000  0.0000  0.0000  575  TYR A CE1 
5492  C CE2 . TYR D 578  ? 0.8579 0.8579 0.8579 0.0000  0.0000  0.0000  575  TYR A CE2 
5493  C CZ  . TYR D 578  ? 0.8579 0.8579 0.8579 0.0000  0.0000  0.0000  575  TYR A CZ  
5494  O OH  . TYR D 578  ? 0.8579 0.8579 0.8579 0.0000  0.0000  0.0000  575  TYR A OH  
5495  N N   . LYS D 579  ? 0.8417 0.8417 0.8417 0.0000  0.0000  0.0000  576  LYS A N   
5496  C CA  . LYS D 579  ? 0.8417 0.8417 0.8417 0.0000  0.0000  0.0000  576  LYS A CA  
5497  C C   . LYS D 579  ? 0.8417 0.8417 0.8417 0.0000  0.0000  0.0000  576  LYS A C   
5498  O O   . LYS D 579  ? 0.8417 0.8417 0.8417 0.0000  0.0000  0.0000  576  LYS A O   
5504  N N   . ALA D 580  ? 0.6995 0.6995 0.6995 0.0000  0.0000  0.0000  577  ALA A N   
5505  C CA  . ALA D 580  ? 0.6995 0.6995 0.6995 0.0000  0.0000  0.0000  577  ALA A CA  
5506  C C   . ALA D 580  ? 0.6995 0.6995 0.6995 0.0000  0.0000  0.0000  577  ALA A C   
5507  O O   . ALA D 580  ? 0.6995 0.6995 0.6995 0.0000  0.0000  0.0000  577  ALA A O   
5508  C CB  . ALA D 580  ? 0.6995 0.6995 0.6995 0.0000  0.0000  0.0000  577  ALA A CB  
5509  N N   . LEU D 581  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  578  LEU A N   
5510  C CA  . LEU D 581  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  578  LEU A CA  
5511  C C   . LEU D 581  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  578  LEU A C   
5512  O O   . LEU D 581  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  578  LEU A O   
5517  N N   . SER D 582  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  579  SER A N   
5518  C CA  . SER D 582  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  579  SER A CA  
5519  C C   . SER D 582  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  579  SER A C   
5520  O O   . SER D 582  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  579  SER A O   
5521  C CB  . SER D 582  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  579  SER A CB  
5522  O OG  . SER D 582  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  579  SER A OG  
5523  N N   . PHE D 583  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  580  PHE A N   
5524  C CA  . PHE D 583  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  580  PHE A CA  
5525  C C   . PHE D 583  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  580  PHE A C   
5526  O O   . PHE D 583  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  580  PHE A O   
5527  C CB  . PHE D 583  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  580  PHE A CB  
5528  C CG  . PHE D 583  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  580  PHE A CG  
5529  C CD1 . PHE D 583  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  580  PHE A CD1 
5530  C CD2 . PHE D 583  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  580  PHE A CD2 
5531  C CE1 . PHE D 583  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  580  PHE A CE1 
5532  C CE2 . PHE D 583  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  580  PHE A CE2 
5533  C CZ  . PHE D 583  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  580  PHE A CZ  
5534  N N   . GLU D 584  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  581  GLU A N   
5535  C CA  . GLU D 584  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  581  GLU A CA  
5536  C C   . GLU D 584  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  581  GLU A C   
5537  O O   . GLU D 584  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  581  GLU A O   
5543  N N   . PRO D 585  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  582  PRO A N   
5544  C CA  . PRO D 585  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  582  PRO A CA  
5545  C C   . PRO D 585  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  582  PRO A C   
5546  O O   . PRO D 585  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  582  PRO A O   
5547  C CB  . PRO D 585  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  582  PRO A CB  
5548  C CG  . PRO D 585  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  582  PRO A CG  
5549  C CD  . PRO D 585  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  582  PRO A CD  
5550  N N   . THR D 586  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  583  THR A N   
5551  C CA  . THR D 586  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  583  THR A CA  
5552  C C   . THR D 586  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  583  THR A C   
5553  O O   . THR D 586  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  583  THR A O   
5554  C CB  . THR D 586  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  583  THR A CB  
5555  O OG1 . THR D 586  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  583  THR A OG1 
5556  C CG2 . THR D 586  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  583  THR A CG2 
5557  N N   . GLU D 587  ? 0.6690 0.6690 0.6690 0.0000  0.0000  0.0000  584  GLU A N   
5558  C CA  . GLU D 587  ? 0.6690 0.6690 0.6690 0.0000  0.0000  0.0000  584  GLU A CA  
5559  C C   . GLU D 587  ? 0.6690 0.6690 0.6690 0.0000  0.0000  0.0000  584  GLU A C   
5560  O O   . GLU D 587  ? 0.6690 0.6690 0.6690 0.0000  0.0000  0.0000  584  GLU A O   
5561  C CB  . GLU D 587  ? 0.6690 0.6690 0.6690 0.0000  0.0000  0.0000  584  GLU A CB  
5562  C CG  . GLU D 587  ? 0.6690 0.6690 0.6690 0.0000  0.0000  0.0000  584  GLU A CG  
5563  C CD  . GLU D 587  ? 0.6690 0.6690 0.6690 0.0000  0.0000  0.0000  584  GLU A CD  
5564  O OE1 . GLU D 587  ? 0.6690 0.6690 0.6690 0.0000  0.0000  0.0000  584  GLU A OE1 
5565  O OE2 . GLU D 587  ? 0.6690 0.6690 0.6690 0.0000  0.0000  0.0000  584  GLU A OE2 
5566  N N   . LYS D 588  ? 0.7127 0.7127 0.7127 0.0000  0.0000  0.0000  585  LYS A N   
5567  C CA  . LYS D 588  ? 0.7127 0.7127 0.7127 0.0000  0.0000  0.0000  585  LYS A CA  
5568  C C   . LYS D 588  ? 0.7127 0.7127 0.7127 0.0000  0.0000  0.0000  585  LYS A C   
5569  O O   . LYS D 588  ? 0.7127 0.7127 0.7127 0.0000  0.0000  0.0000  585  LYS A O   
5575  N N   . THR D 589  ? 0.7407 0.7407 0.7407 0.0000  0.0000  0.0000  586  THR A N   
5576  C CA  . THR D 589  ? 0.7407 0.7407 0.7407 0.0000  0.0000  0.0000  586  THR A CA  
5577  C C   . THR D 589  ? 0.7407 0.7407 0.7407 0.0000  0.0000  0.0000  586  THR A C   
5578  O O   . THR D 589  ? 0.7407 0.7407 0.7407 0.0000  0.0000  0.0000  586  THR A O   
5579  C CB  . THR D 589  ? 0.7407 0.7407 0.7407 0.0000  0.0000  0.0000  586  THR A CB  
5580  O OG1 . THR D 589  ? 0.7407 0.7407 0.7407 0.0000  0.0000  0.0000  586  THR A OG1 
5581  C CG2 . THR D 589  ? 0.7407 0.7407 0.7407 0.0000  0.0000  0.0000  586  THR A CG2 
5582  N N   . SER D 590  ? 0.6584 0.6584 0.6584 0.0000  0.0000  0.0000  587  SER A N   
5583  C CA  . SER D 590  ? 0.6584 0.6584 0.6584 0.0000  0.0000  0.0000  587  SER A CA  
5584  C C   . SER D 590  ? 0.6584 0.6584 0.6584 0.0000  0.0000  0.0000  587  SER A C   
5585  O O   . SER D 590  ? 0.6584 0.6584 0.6584 0.0000  0.0000  0.0000  587  SER A O   
5586  C CB  . SER D 590  ? 0.6584 0.6584 0.6584 0.0000  0.0000  0.0000  587  SER A CB  
5587  O OG  . SER D 590  ? 0.6584 0.6584 0.6584 0.0000  0.0000  0.0000  587  SER A OG  
5588  N N   . GLU D 591  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  588  GLU A N   
5589  C CA  . GLU D 591  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  588  GLU A CA  
5590  C C   . GLU D 591  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  588  GLU A C   
5591  O O   . GLU D 591  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  588  GLU A O   
5592  C CB  . GLU D 591  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  588  GLU A CB  
5593  C CG  . GLU D 591  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  588  GLU A CG  
5594  C CD  . GLU D 591  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  588  GLU A CD  
5595  O OE1 . GLU D 591  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  588  GLU A OE1 
5596  O OE2 . GLU D 591  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  588  GLU A OE2 
5597  N N   . GLY D 592  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  589  GLY A N   
5598  C CA  . GLY D 592  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  589  GLY A CA  
5599  C C   . GLY D 592  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  589  GLY A C   
5600  O O   . GLY D 592  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  589  GLY A O   
5601  N N   . PHE D 593  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  590  PHE A N   
5602  C CA  . PHE D 593  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  590  PHE A CA  
5603  C C   . PHE D 593  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  590  PHE A C   
5604  O O   . PHE D 593  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  590  PHE A O   
5605  C CB  . PHE D 593  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  590  PHE A CB  
5606  C CG  . PHE D 593  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  590  PHE A CG  
5607  C CD1 . PHE D 593  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  590  PHE A CD1 
5608  C CD2 . PHE D 593  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  590  PHE A CD2 
5609  C CE1 . PHE D 593  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  590  PHE A CE1 
5610  C CE2 . PHE D 593  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  590  PHE A CE2 
5611  C CZ  . PHE D 593  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  590  PHE A CZ  
5612  N N   . ASP D 594  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  591  ASP A N   
5613  C CA  . ASP D 594  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  591  ASP A CA  
5614  C C   . ASP D 594  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  591  ASP A C   
5615  O O   . ASP D 594  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  591  ASP A O   
5616  C CB  . ASP D 594  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  591  ASP A CB  
5617  C CG  . ASP D 594  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  591  ASP A CG  
5618  O OD1 . ASP D 594  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  591  ASP A OD1 
5619  O OD2 . ASP D 594  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  591  ASP A OD2 
5620  N N   . LYS D 595  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  592  LYS A N   
5621  C CA  . LYS D 595  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  592  LYS A CA  
5622  C C   . LYS D 595  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  592  LYS A C   
5623  O O   . LYS D 595  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  592  LYS A O   
5624  C CB  . LYS D 595  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  592  LYS A CB  
5625  C CG  . LYS D 595  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  592  LYS A CG  
5626  C CD  . LYS D 595  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  592  LYS A CD  
5627  C CE  . LYS D 595  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  592  LYS A CE  
5628  N NZ  . LYS D 595  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  592  LYS A NZ  
5629  N N   . MET D 596  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  593  MET A N   
5630  C CA  . MET D 596  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  593  MET A CA  
5631  C C   . MET D 596  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  593  MET A C   
5632  O O   . MET D 596  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  593  MET A O   
5633  C CB  . MET D 596  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  593  MET A CB  
5634  C CG  . MET D 596  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  593  MET A CG  
5635  S SD  . MET D 596  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  593  MET A SD  
5636  C CE  . MET D 596  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  593  MET A CE  
5637  N N   . TYR D 597  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  594  TYR A N   
5638  C CA  . TYR D 597  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  594  TYR A CA  
5639  C C   . TYR D 597  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  594  TYR A C   
5640  O O   . TYR D 597  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  594  TYR A O   
5641  C CB  . TYR D 597  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  594  TYR A CB  
5642  C CG  . TYR D 597  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  594  TYR A CG  
5643  C CD1 . TYR D 597  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  594  TYR A CD1 
5644  C CD2 . TYR D 597  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  594  TYR A CD2 
5645  C CE1 . TYR D 597  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  594  TYR A CE1 
5646  C CE2 . TYR D 597  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  594  TYR A CE2 
5647  C CZ  . TYR D 597  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  594  TYR A CZ  
5648  O OH  . TYR D 597  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  594  TYR A OH  
5649  N N   . TYR D 598  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  595  TYR A N   
5650  C CA  . TYR D 598  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  595  TYR A CA  
5651  C C   . TYR D 598  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  595  TYR A C   
5652  O O   . TYR D 598  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  595  TYR A O   
5653  C CB  . TYR D 598  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  595  TYR A CB  
5654  C CG  . TYR D 598  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  595  TYR A CG  
5655  C CD1 . TYR D 598  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  595  TYR A CD1 
5656  C CD2 . TYR D 598  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  595  TYR A CD2 
5657  C CE1 . TYR D 598  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  595  TYR A CE1 
5658  C CE2 . TYR D 598  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  595  TYR A CE2 
5659  C CZ  . TYR D 598  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  595  TYR A CZ  
5660  O OH  . TYR D 598  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  595  TYR A OH  
5661  N N   . ASP D 599  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  596  ASP A N   
5662  C CA  . ASP D 599  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  596  ASP A CA  
5663  C C   . ASP D 599  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  596  ASP A C   
5664  O O   . ASP D 599  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  596  ASP A O   
5665  C CB  . ASP D 599  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  596  ASP A CB  
5666  C CG  . ASP D 599  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  596  ASP A CG  
5667  O OD1 . ASP D 599  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  596  ASP A OD1 
5668  O OD2 . ASP D 599  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  596  ASP A OD2 
5669  N N   . TYR D 600  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  597  TYR A N   
5670  C CA  . TYR D 600  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  597  TYR A CA  
5671  C C   . TYR D 600  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  597  TYR A C   
5672  O O   . TYR D 600  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  597  TYR A O   
5673  C CB  . TYR D 600  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  597  TYR A CB  
5674  C CG  . TYR D 600  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  597  TYR A CG  
5675  C CD1 . TYR D 600  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  597  TYR A CD1 
5676  C CD2 . TYR D 600  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  597  TYR A CD2 
5677  C CE1 . TYR D 600  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  597  TYR A CE1 
5678  C CE2 . TYR D 600  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  597  TYR A CE2 
5679  C CZ  . TYR D 600  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  597  TYR A CZ  
5680  O OH  . TYR D 600  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  597  TYR A OH  
5681  N N   . PHE D 601  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  598  PHE A N   
5682  C CA  . PHE D 601  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  598  PHE A CA  
5683  C C   . PHE D 601  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  598  PHE A C   
5684  O O   . PHE D 601  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  598  PHE A O   
5685  C CB  . PHE D 601  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  598  PHE A CB  
5686  C CG  . PHE D 601  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  598  PHE A CG  
5687  C CD1 . PHE D 601  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  598  PHE A CD1 
5688  C CD2 . PHE D 601  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  598  PHE A CD2 
5689  C CE1 . PHE D 601  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  598  PHE A CE1 
5690  C CE2 . PHE D 601  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  598  PHE A CE2 
5691  C CZ  . PHE D 601  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  598  PHE A CZ  
5692  N N   . PRO D 602  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  599  PRO A N   
5693  C CA  . PRO D 602  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  599  PRO A CA  
5694  C C   . PRO D 602  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  599  PRO A C   
5695  O O   . PRO D 602  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  599  PRO A O   
5696  C CB  . PRO D 602  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  599  PRO A CB  
5697  C CG  . PRO D 602  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  599  PRO A CG  
5698  C CD  . PRO D 602  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  599  PRO A CD  
5699  N N   . ASP D 603  ? 0.6593 0.6593 0.6593 0.0000  0.0000  0.0000  600  ASP A N   
5700  C CA  . ASP D 603  ? 0.6593 0.6593 0.6593 0.0000  0.0000  0.0000  600  ASP A CA  
5701  C C   . ASP D 603  ? 0.6593 0.6593 0.6593 0.0000  0.0000  0.0000  600  ASP A C   
5702  O O   . ASP D 603  ? 0.6593 0.6593 0.6593 0.0000  0.0000  0.0000  600  ASP A O   
5703  C CB  . ASP D 603  ? 0.6593 0.6593 0.6593 0.0000  0.0000  0.0000  600  ASP A CB  
5704  C CG  . ASP D 603  ? 0.6593 0.6593 0.6593 0.0000  0.0000  0.0000  600  ASP A CG  
5705  O OD1 . ASP D 603  ? 0.6593 0.6593 0.6593 0.0000  0.0000  0.0000  600  ASP A OD1 
5706  O OD2 . ASP D 603  ? 0.6593 0.6593 0.6593 0.0000  0.0000  0.0000  600  ASP A OD2 
5707  N N   . ALA D 604  ? 0.6375 0.6375 0.6375 0.0000  0.0000  0.0000  601  ALA A N   
5708  C CA  . ALA D 604  ? 0.6375 0.6375 0.6375 0.0000  0.0000  0.0000  601  ALA A CA  
5709  C C   . ALA D 604  ? 0.6375 0.6375 0.6375 0.0000  0.0000  0.0000  601  ALA A C   
5710  O O   . ALA D 604  ? 0.6375 0.6375 0.6375 0.0000  0.0000  0.0000  601  ALA A O   
5711  C CB  . ALA D 604  ? 0.6375 0.6375 0.6375 0.0000  0.0000  0.0000  601  ALA A CB  
5712  N N   . ALA D 605  ? 0.6944 0.6944 0.6944 0.0000  0.0000  0.0000  602  ALA A N   
5713  C CA  . ALA D 605  ? 0.6944 0.6944 0.6944 0.0000  0.0000  0.0000  602  ALA A CA  
5714  C C   . ALA D 605  ? 0.6944 0.6944 0.6944 0.0000  0.0000  0.0000  602  ALA A C   
5715  O O   . ALA D 605  ? 0.6944 0.6944 0.6944 0.0000  0.0000  0.0000  602  ALA A O   
5716  C CB  . ALA D 605  ? 0.6944 0.6944 0.6944 0.0000  0.0000  0.0000  602  ALA A CB  
5717  N N   . LYS D 606  ? 0.6855 0.6855 0.6855 0.0000  0.0000  0.0000  603  LYS A N   
5718  C CA  . LYS D 606  ? 0.6855 0.6855 0.6855 0.0000  0.0000  0.0000  603  LYS A CA  
5719  C C   . LYS D 606  ? 0.6855 0.6855 0.6855 0.0000  0.0000  0.0000  603  LYS A C   
5720  O O   . LYS D 606  ? 0.6855 0.6855 0.6855 0.0000  0.0000  0.0000  603  LYS A O   
5721  C CB  . LYS D 606  ? 0.6855 0.6855 0.6855 0.0000  0.0000  0.0000  603  LYS A CB  
5722  C CG  . LYS D 606  ? 0.6855 0.6855 0.6855 0.0000  0.0000  0.0000  603  LYS A CG  
5723  C CD  . LYS D 606  ? 0.6855 0.6855 0.6855 0.0000  0.0000  0.0000  603  LYS A CD  
5724  C CE  . LYS D 606  ? 0.6855 0.6855 0.6855 0.0000  0.0000  0.0000  603  LYS A CE  
5725  N NZ  . LYS D 606  ? 0.6855 0.6855 0.6855 0.0000  0.0000  0.0000  603  LYS A NZ  
5726  N N   . MET D 607  ? 0.6530 0.6530 0.6530 0.0000  0.0000  0.0000  604  MET A N   
5727  C CA  . MET D 607  ? 0.6530 0.6530 0.6530 0.0000  0.0000  0.0000  604  MET A CA  
5728  C C   . MET D 607  ? 0.6530 0.6530 0.6530 0.0000  0.0000  0.0000  604  MET A C   
5729  O O   . MET D 607  ? 0.6530 0.6530 0.6530 0.0000  0.0000  0.0000  604  MET A O   
5730  C CB  . MET D 607  ? 0.6530 0.6530 0.6530 0.0000  0.0000  0.0000  604  MET A CB  
5731  C CG  . MET D 607  ? 0.6530 0.6530 0.6530 0.0000  0.0000  0.0000  604  MET A CG  
5732  S SD  . MET D 607  ? 0.6530 0.6530 0.6530 0.0000  0.0000  0.0000  604  MET A SD  
5733  C CE  . MET D 607  ? 0.6530 0.6530 0.6530 0.0000  0.0000  0.0000  604  MET A CE  
5734  N N   . ILE D 608  ? 0.7050 0.7050 0.7050 0.0000  0.0000  0.0000  605  ILE A N   
5735  C CA  . ILE D 608  ? 0.7050 0.7050 0.7050 0.0000  0.0000  0.0000  605  ILE A CA  
5736  C C   . ILE D 608  ? 0.7050 0.7050 0.7050 0.0000  0.0000  0.0000  605  ILE A C   
5737  O O   . ILE D 608  ? 0.7050 0.7050 0.7050 0.0000  0.0000  0.0000  605  ILE A O   
5738  C CB  . ILE D 608  ? 0.7050 0.7050 0.7050 0.0000  0.0000  0.0000  605  ILE A CB  
5739  C CG1 . ILE D 608  ? 0.7050 0.7050 0.7050 0.0000  0.0000  0.0000  605  ILE A CG1 
5740  C CG2 . ILE D 608  ? 0.7050 0.7050 0.7050 0.0000  0.0000  0.0000  605  ILE A CG2 
5741  C CD1 . ILE D 608  ? 0.7050 0.7050 0.7050 0.0000  0.0000  0.0000  605  ILE A CD1 
5742  N N   . PRO D 609  ? 0.6813 0.6813 0.6813 0.0000  0.0000  0.0000  606  PRO A N   
5743  C CA  . PRO D 609  ? 0.6813 0.6813 0.6813 0.0000  0.0000  0.0000  606  PRO A CA  
5744  C C   . PRO D 609  ? 0.6813 0.6813 0.6813 0.0000  0.0000  0.0000  606  PRO A C   
5745  O O   . PRO D 609  ? 0.6813 0.6813 0.6813 0.0000  0.0000  0.0000  606  PRO A O   
5746  C CB  . PRO D 609  ? 0.6813 0.6813 0.6813 0.0000  0.0000  0.0000  606  PRO A CB  
5747  C CG  . PRO D 609  ? 0.6813 0.6813 0.6813 0.0000  0.0000  0.0000  606  PRO A CG  
5748  C CD  . PRO D 609  ? 0.6813 0.6813 0.6813 0.0000  0.0000  0.0000  606  PRO A CD  
5749  N N   . LYS D 610  ? 0.6580 0.6580 0.6580 0.0000  0.0000  0.0000  607  LYS A N   
5750  C CA  . LYS D 610  ? 0.6580 0.6580 0.6580 0.0000  0.0000  0.0000  607  LYS A CA  
5751  C C   . LYS D 610  ? 0.6580 0.6580 0.6580 0.0000  0.0000  0.0000  607  LYS A C   
5752  O O   . LYS D 610  ? 0.6580 0.6580 0.6580 0.0000  0.0000  0.0000  607  LYS A O   
5753  C CB  . LYS D 610  ? 0.6580 0.6580 0.6580 0.0000  0.0000  0.0000  607  LYS A CB  
5754  C CG  . LYS D 610  ? 0.6580 0.6580 0.6580 0.0000  0.0000  0.0000  607  LYS A CG  
5755  C CD  . LYS D 610  ? 0.6580 0.6580 0.6580 0.0000  0.0000  0.0000  607  LYS A CD  
5756  C CE  . LYS D 610  ? 0.6580 0.6580 0.6580 0.0000  0.0000  0.0000  607  LYS A CE  
5757  N NZ  . LYS D 610  ? 0.6580 0.6580 0.6580 0.0000  0.0000  0.0000  607  LYS A NZ  
5758  N N   . CYS D 611  ? 0.7292 0.7292 0.7292 0.0000  0.0000  0.0000  608  CYS A N   
5759  C CA  . CYS D 611  ? 0.7292 0.7292 0.7292 0.0000  0.0000  0.0000  608  CYS A CA  
5760  C C   . CYS D 611  ? 0.7292 0.7292 0.7292 0.0000  0.0000  0.0000  608  CYS A C   
5761  O O   . CYS D 611  ? 0.7292 0.7292 0.7292 0.0000  0.0000  0.0000  608  CYS A O   
5762  C CB  . CYS D 611  ? 0.7292 0.7292 0.7292 0.0000  0.0000  0.0000  608  CYS A CB  
5763  S SG  . CYS D 611  ? 0.7292 0.7292 0.7292 0.0000  0.0000  0.0000  608  CYS A SG  
5764  N N   . SER D 612  ? 0.7782 0.7782 0.7782 0.0000  0.0000  0.0000  609  SER A N   
5765  C CA  . SER D 612  ? 0.7782 0.7782 0.7782 0.0000  0.0000  0.0000  609  SER A CA  
5766  C C   . SER D 612  ? 0.7782 0.7782 0.7782 0.0000  0.0000  0.0000  609  SER A C   
5767  O O   . SER D 612  ? 0.7782 0.7782 0.7782 0.0000  0.0000  0.0000  609  SER A O   
5768  C CB  . SER D 612  ? 0.7782 0.7782 0.7782 0.0000  0.0000  0.0000  609  SER A CB  
5769  O OG  . SER D 612  ? 0.7782 0.7782 0.7782 0.0000  0.0000  0.0000  609  SER A OG  
5770  N N   . THR D 613  ? 0.7776 0.7776 0.7776 0.0000  0.0000  0.0000  610  THR A N   
5771  C CA  . THR D 613  ? 0.7776 0.7776 0.7776 0.0000  0.0000  0.0000  610  THR A CA  
5772  C C   . THR D 613  ? 0.7776 0.7776 0.7776 0.0000  0.0000  0.0000  610  THR A C   
5773  O O   . THR D 613  ? 0.7776 0.7776 0.7776 0.0000  0.0000  0.0000  610  THR A O   
5774  C CB  . THR D 613  ? 0.7776 0.7776 0.7776 0.0000  0.0000  0.0000  610  THR A CB  
5775  O OG1 . THR D 613  ? 0.7776 0.7776 0.7776 0.0000  0.0000  0.0000  610  THR A OG1 
5776  C CG2 . THR D 613  ? 0.7776 0.7776 0.7776 0.0000  0.0000  0.0000  610  THR A CG2 
5777  N N   . GLN D 614  ? 0.7355 0.7355 0.7355 0.0000  0.0000  0.0000  611  GLN A N   
5778  C CA  . GLN D 614  ? 0.7355 0.7355 0.7355 0.0000  0.0000  0.0000  611  GLN A CA  
5779  C C   . GLN D 614  ? 0.7355 0.7355 0.7355 0.0000  0.0000  0.0000  611  GLN A C   
5780  O O   . GLN D 614  ? 0.7355 0.7355 0.7355 0.0000  0.0000  0.0000  611  GLN A O   
5781  C CB  . GLN D 614  ? 0.7355 0.7355 0.7355 0.0000  0.0000  0.0000  611  GLN A CB  
5782  C CG  . GLN D 614  ? 0.7355 0.7355 0.7355 0.0000  0.0000  0.0000  611  GLN A CG  
5783  C CD  . GLN D 614  ? 0.7355 0.7355 0.7355 0.0000  0.0000  0.0000  611  GLN A CD  
5784  O OE1 . GLN D 614  ? 0.7355 0.7355 0.7355 0.0000  0.0000  0.0000  611  GLN A OE1 
5785  N NE2 . GLN D 614  ? 0.7355 0.7355 0.7355 0.0000  0.0000  0.0000  611  GLN A NE2 
5786  N N   . LEU D 615  ? 0.7740 0.7740 0.7740 0.0000  0.0000  0.0000  612  LEU A N   
5787  C CA  . LEU D 615  ? 0.7740 0.7740 0.7740 0.0000  0.0000  0.0000  612  LEU A CA  
5788  C C   . LEU D 615  ? 0.7740 0.7740 0.7740 0.0000  0.0000  0.0000  612  LEU A C   
5789  O O   . LEU D 615  ? 0.7740 0.7740 0.7740 0.0000  0.0000  0.0000  612  LEU A O   
5790  C CB  . LEU D 615  ? 0.7740 0.7740 0.7740 0.0000  0.0000  0.0000  612  LEU A CB  
5791  C CG  . LEU D 615  ? 0.7740 0.7740 0.7740 0.0000  0.0000  0.0000  612  LEU A CG  
5792  C CD1 . LEU D 615  ? 0.7740 0.7740 0.7740 0.0000  0.0000  0.0000  612  LEU A CD1 
5793  C CD2 . LEU D 615  ? 0.7740 0.7740 0.7740 0.0000  0.0000  0.0000  612  LEU A CD2 
5794  N N   . LYS D 616  ? 0.7879 0.7879 0.7879 0.0000  0.0000  0.0000  613  LYS A N   
5795  C CA  . LYS D 616  ? 0.7879 0.7879 0.7879 0.0000  0.0000  0.0000  613  LYS A CA  
5796  C C   . LYS D 616  ? 0.7879 0.7879 0.7879 0.0000  0.0000  0.0000  613  LYS A C   
5797  O O   . LYS D 616  ? 0.7879 0.7879 0.7879 0.0000  0.0000  0.0000  613  LYS A O   
5798  C CB  . LYS D 616  ? 0.7879 0.7879 0.7879 0.0000  0.0000  0.0000  613  LYS A CB  
5799  C CG  . LYS D 616  ? 0.7879 0.7879 0.7879 0.0000  0.0000  0.0000  613  LYS A CG  
5800  C CD  . LYS D 616  ? 0.7879 0.7879 0.7879 0.0000  0.0000  0.0000  613  LYS A CD  
5801  C CE  . LYS D 616  ? 0.7879 0.7879 0.7879 0.0000  0.0000  0.0000  613  LYS A CE  
5802  N NZ  . LYS D 616  ? 0.7879 0.7879 0.7879 0.0000  0.0000  0.0000  613  LYS A NZ  
5803  N N   . ALA D 617  ? 0.8197 0.8197 0.8197 0.0000  0.0000  0.0000  614  ALA A N   
5804  C CA  . ALA D 617  ? 0.8197 0.8197 0.8197 0.0000  0.0000  0.0000  614  ALA A CA  
5805  C C   . ALA D 617  ? 0.8197 0.8197 0.8197 0.0000  0.0000  0.0000  614  ALA A C   
5806  O O   . ALA D 617  ? 0.8197 0.8197 0.8197 0.0000  0.0000  0.0000  614  ALA A O   
5807  C CB  . ALA D 617  ? 0.8197 0.8197 0.8197 0.0000  0.0000  0.0000  614  ALA A CB  
5808  N N   . VAL D 618  ? 0.8621 0.8621 0.8621 0.0000  0.0000  0.0000  615  VAL A N   
5809  C CA  . VAL D 618  ? 0.8621 0.8621 0.8621 0.0000  0.0000  0.0000  615  VAL A CA  
5810  C C   . VAL D 618  ? 0.8621 0.8621 0.8621 0.0000  0.0000  0.0000  615  VAL A C   
5811  O O   . VAL D 618  ? 0.8621 0.8621 0.8621 0.0000  0.0000  0.0000  615  VAL A O   
5812  C CB  . VAL D 618  ? 0.8621 0.8621 0.8621 0.0000  0.0000  0.0000  615  VAL A CB  
5813  C CG1 . VAL D 618  ? 0.8621 0.8621 0.8621 0.0000  0.0000  0.0000  615  VAL A CG1 
5814  C CG2 . VAL D 618  ? 0.8621 0.8621 0.8621 0.0000  0.0000  0.0000  615  VAL A CG2 
5815  N N   . THR D 619  ? 0.8481 0.8481 0.8481 0.0000  0.0000  0.0000  616  THR A N   
5816  C CA  . THR D 619  ? 0.8481 0.8481 0.8481 0.0000  0.0000  0.0000  616  THR A CA  
5817  C C   . THR D 619  ? 0.8481 0.8481 0.8481 0.0000  0.0000  0.0000  616  THR A C   
5818  O O   . THR D 619  ? 0.8481 0.8481 0.8481 0.0000  0.0000  0.0000  616  THR A O   
5819  C CB  . THR D 619  ? 0.8481 0.8481 0.8481 0.0000  0.0000  0.0000  616  THR A CB  
5820  O OG1 . THR D 619  ? 0.8481 0.8481 0.8481 0.0000  0.0000  0.0000  616  THR A OG1 
5821  C CG2 . THR D 619  ? 0.8481 0.8481 0.8481 0.0000  0.0000  0.0000  616  THR A CG2 
5822  N N   . ALA D 620  ? 0.8861 0.8861 0.8861 0.0000  0.0000  0.0000  617  ALA A N   
5823  C CA  . ALA D 620  ? 0.8861 0.8861 0.8861 0.0000  0.0000  0.0000  617  ALA A CA  
5824  C C   . ALA D 620  ? 0.8861 0.8861 0.8861 0.0000  0.0000  0.0000  617  ALA A C   
5825  O O   . ALA D 620  ? 0.8861 0.8861 0.8861 0.0000  0.0000  0.0000  617  ALA A O   
5826  C CB  . ALA D 620  ? 0.8861 0.8861 0.8861 0.0000  0.0000  0.0000  617  ALA A CB  
5827  N N   . HIS D 621  ? 0.9870 0.9870 0.9870 0.0000  0.0000  0.0000  618  HIS A N   
5828  C CA  . HIS D 621  ? 0.9870 0.9870 0.9870 0.0000  0.0000  0.0000  618  HIS A CA  
5829  C C   . HIS D 621  ? 0.9870 0.9870 0.9870 0.0000  0.0000  0.0000  618  HIS A C   
5830  O O   . HIS D 621  ? 0.9870 0.9870 0.9870 0.0000  0.0000  0.0000  618  HIS A O   
5831  C CB  . HIS D 621  ? 0.9870 0.9870 0.9870 0.0000  0.0000  0.0000  618  HIS A CB  
5832  C CG  . HIS D 621  ? 0.9870 0.9870 0.9870 0.0000  0.0000  0.0000  618  HIS A CG  
5833  N ND1 . HIS D 621  ? 0.9870 0.9870 0.9870 0.0000  0.0000  0.0000  618  HIS A ND1 
5834  C CD2 . HIS D 621  ? 0.9870 0.9870 0.9870 0.0000  0.0000  0.0000  618  HIS A CD2 
5835  C CE1 . HIS D 621  ? 0.9870 0.9870 0.9870 0.0000  0.0000  0.0000  618  HIS A CE1 
5836  N NE2 . HIS D 621  ? 0.9870 0.9870 0.9870 0.0000  0.0000  0.0000  618  HIS A NE2 
5837  N N   . PHE D 622  ? 1.0241 1.0241 1.0241 0.0000  0.0000  0.0000  619  PHE A N   
5838  C CA  . PHE D 622  ? 1.0241 1.0241 1.0241 0.0000  0.0000  0.0000  619  PHE A CA  
5839  C C   . PHE D 622  ? 1.0241 1.0241 1.0241 0.0000  0.0000  0.0000  619  PHE A C   
5840  O O   . PHE D 622  ? 1.0241 1.0241 1.0241 0.0000  0.0000  0.0000  619  PHE A O   
5841  C CB  . PHE D 622  ? 1.0241 1.0241 1.0241 0.0000  0.0000  0.0000  619  PHE A CB  
5842  C CG  . PHE D 622  ? 1.0241 1.0241 1.0241 0.0000  0.0000  0.0000  619  PHE A CG  
5843  C CD1 . PHE D 622  ? 1.0241 1.0241 1.0241 0.0000  0.0000  0.0000  619  PHE A CD1 
5844  C CD2 . PHE D 622  ? 1.0241 1.0241 1.0241 0.0000  0.0000  0.0000  619  PHE A CD2 
5845  C CE1 . PHE D 622  ? 1.0241 1.0241 1.0241 0.0000  0.0000  0.0000  619  PHE A CE1 
5846  C CE2 . PHE D 622  ? 1.0241 1.0241 1.0241 0.0000  0.0000  0.0000  619  PHE A CE2 
5847  C CZ  . PHE D 622  ? 1.0241 1.0241 1.0241 0.0000  0.0000  0.0000  619  PHE A CZ  
5848  N N   . GLN D 623  ? 0.9976 0.9976 0.9976 0.0000  0.0000  0.0000  620  GLN A N   
5849  C CA  . GLN D 623  ? 0.9976 0.9976 0.9976 0.0000  0.0000  0.0000  620  GLN A CA  
5850  C C   . GLN D 623  ? 0.9976 0.9976 0.9976 0.0000  0.0000  0.0000  620  GLN A C   
5851  O O   . GLN D 623  ? 0.9976 0.9976 0.9976 0.0000  0.0000  0.0000  620  GLN A O   
5852  C CB  . GLN D 623  ? 0.9976 0.9976 0.9976 0.0000  0.0000  0.0000  620  GLN A CB  
5853  C CG  . GLN D 623  ? 0.9976 0.9976 0.9976 0.0000  0.0000  0.0000  620  GLN A CG  
5854  C CD  . GLN D 623  ? 0.9976 0.9976 0.9976 0.0000  0.0000  0.0000  620  GLN A CD  
5855  O OE1 . GLN D 623  ? 0.9976 0.9976 0.9976 0.0000  0.0000  0.0000  620  GLN A OE1 
5856  N NE2 . GLN D 623  ? 0.9976 0.9976 0.9976 0.0000  0.0000  0.0000  620  GLN A NE2 
5857  N N   . THR D 624  ? 1.0450 1.0450 1.0450 0.0000  0.0000  0.0000  621  THR A N   
5858  C CA  . THR D 624  ? 1.0450 1.0450 1.0450 0.0000  0.0000  0.0000  621  THR A CA  
5859  C C   . THR D 624  ? 1.0450 1.0450 1.0450 0.0000  0.0000  0.0000  621  THR A C   
5860  O O   . THR D 624  ? 1.0450 1.0450 1.0450 0.0000  0.0000  0.0000  621  THR A O   
5861  C CB  . THR D 624  ? 1.0450 1.0450 1.0450 0.0000  0.0000  0.0000  621  THR A CB  
5862  O OG1 . THR D 624  ? 1.0450 1.0450 1.0450 0.0000  0.0000  0.0000  621  THR A OG1 
5863  C CG2 . THR D 624  ? 1.0450 1.0450 1.0450 0.0000  0.0000  0.0000  621  THR A CG2 
5864  N N   . HIS D 625  ? 1.0749 1.0749 1.0749 0.0000  0.0000  0.0000  622  HIS A N   
5865  C CA  . HIS D 625  ? 1.0749 1.0749 1.0749 0.0000  0.0000  0.0000  622  HIS A CA  
5866  C C   . HIS D 625  ? 1.0749 1.0749 1.0749 0.0000  0.0000  0.0000  622  HIS A C   
5867  O O   . HIS D 625  ? 1.0749 1.0749 1.0749 0.0000  0.0000  0.0000  622  HIS A O   
5868  C CB  . HIS D 625  ? 1.0749 1.0749 1.0749 0.0000  0.0000  0.0000  622  HIS A CB  
5869  C CG  . HIS D 625  ? 1.0749 1.0749 1.0749 0.0000  0.0000  0.0000  622  HIS A CG  
5870  N ND1 . HIS D 625  ? 1.0749 1.0749 1.0749 0.0000  0.0000  0.0000  622  HIS A ND1 
5871  C CD2 . HIS D 625  ? 1.0749 1.0749 1.0749 0.0000  0.0000  0.0000  622  HIS A CD2 
5872  C CE1 . HIS D 625  ? 1.0749 1.0749 1.0749 0.0000  0.0000  0.0000  622  HIS A CE1 
5873  N NE2 . HIS D 625  ? 1.0749 1.0749 1.0749 0.0000  0.0000  0.0000  622  HIS A NE2 
5874  N N   . THR D 626  ? 1.1187 1.1187 1.1187 0.0000  0.0000  0.0000  623  THR A N   
5875  C CA  . THR D 626  ? 1.1187 1.1187 1.1187 0.0000  0.0000  0.0000  623  THR A CA  
5876  C C   . THR D 626  ? 1.1187 1.1187 1.1187 0.0000  0.0000  0.0000  623  THR A C   
5877  O O   . THR D 626  ? 1.1187 1.1187 1.1187 0.0000  0.0000  0.0000  623  THR A O   
5878  C CB  . THR D 626  ? 1.1187 1.1187 1.1187 0.0000  0.0000  0.0000  623  THR A CB  
5879  O OG1 . THR D 626  ? 1.1187 1.1187 1.1187 0.0000  0.0000  0.0000  623  THR A OG1 
5880  C CG2 . THR D 626  ? 1.1187 1.1187 1.1187 0.0000  0.0000  0.0000  623  THR A CG2 
5881  N N   . THR D 627  ? 1.1384 1.1384 1.1384 0.0000  0.0000  0.0000  624  THR A N   
5882  C CA  . THR D 627  ? 1.1384 1.1384 1.1384 0.0000  0.0000  0.0000  624  THR A CA  
5883  C C   . THR D 627  ? 1.1384 1.1384 1.1384 0.0000  0.0000  0.0000  624  THR A C   
5884  O O   . THR D 627  ? 1.1384 1.1384 1.1384 0.0000  0.0000  0.0000  624  THR A O   
5885  C CB  . THR D 627  ? 1.1384 1.1384 1.1384 0.0000  0.0000  0.0000  624  THR A CB  
5886  O OG1 . THR D 627  ? 1.1384 1.1384 1.1384 0.0000  0.0000  0.0000  624  THR A OG1 
5887  C CG2 . THR D 627  ? 1.1384 1.1384 1.1384 0.0000  0.0000  0.0000  624  THR A CG2 
5888  N N   . PRO D 628  ? 1.1134 1.1134 1.1134 0.0000  0.0000  0.0000  625  PRO A N   
5889  C CA  . PRO D 628  ? 1.1134 1.1134 1.1134 0.0000  0.0000  0.0000  625  PRO A CA  
5890  C C   . PRO D 628  ? 1.1134 1.1134 1.1134 0.0000  0.0000  0.0000  625  PRO A C   
5891  O O   . PRO D 628  ? 1.1134 1.1134 1.1134 0.0000  0.0000  0.0000  625  PRO A O   
5892  C CB  . PRO D 628  ? 1.1134 1.1134 1.1134 0.0000  0.0000  0.0000  625  PRO A CB  
5893  C CG  . PRO D 628  ? 1.1134 1.1134 1.1134 0.0000  0.0000  0.0000  625  PRO A CG  
5894  C CD  . PRO D 628  ? 1.1134 1.1134 1.1134 0.0000  0.0000  0.0000  625  PRO A CD  
5895  N N   . ILE D 629  ? 1.0265 1.0265 1.0265 0.0000  0.0000  0.0000  626  ILE A N   
5896  C CA  . ILE D 629  ? 1.0265 1.0265 1.0265 0.0000  0.0000  0.0000  626  ILE A CA  
5897  C C   . ILE D 629  ? 1.0265 1.0265 1.0265 0.0000  0.0000  0.0000  626  ILE A C   
5898  O O   . ILE D 629  ? 1.0265 1.0265 1.0265 0.0000  0.0000  0.0000  626  ILE A O   
5899  C CB  . ILE D 629  ? 1.0265 1.0265 1.0265 0.0000  0.0000  0.0000  626  ILE A CB  
5900  C CG1 . ILE D 629  ? 1.0265 1.0265 1.0265 0.0000  0.0000  0.0000  626  ILE A CG1 
5901  C CG2 . ILE D 629  ? 1.0265 1.0265 1.0265 0.0000  0.0000  0.0000  626  ILE A CG2 
5902  C CD1 . ILE D 629  ? 1.0265 1.0265 1.0265 0.0000  0.0000  0.0000  626  ILE A CD1 
5903  N N   . LEU D 630  ? 1.0236 1.0236 1.0236 0.0000  0.0000  0.0000  627  LEU A N   
5904  C CA  . LEU D 630  ? 1.0236 1.0236 1.0236 0.0000  0.0000  0.0000  627  LEU A CA  
5905  C C   . LEU D 630  ? 1.0236 1.0236 1.0236 0.0000  0.0000  0.0000  627  LEU A C   
5906  O O   . LEU D 630  ? 1.0236 1.0236 1.0236 0.0000  0.0000  0.0000  627  LEU A O   
5907  C CB  . LEU D 630  ? 1.0236 1.0236 1.0236 0.0000  0.0000  0.0000  627  LEU A CB  
5908  C CG  . LEU D 630  ? 1.0236 1.0236 1.0236 0.0000  0.0000  0.0000  627  LEU A CG  
5909  C CD1 . LEU D 630  ? 1.0236 1.0236 1.0236 0.0000  0.0000  0.0000  627  LEU A CD1 
5910  C CD2 . LEU D 630  ? 1.0236 1.0236 1.0236 0.0000  0.0000  0.0000  627  LEU A CD2 
5911  N N   . LEU D 631  ? 0.9180 0.9180 0.9180 0.0000  0.0000  0.0000  628  LEU A N   
5912  C CA  . LEU D 631  ? 0.9180 0.9180 0.9180 0.0000  0.0000  0.0000  628  LEU A CA  
5913  C C   . LEU D 631  ? 0.9180 0.9180 0.9180 0.0000  0.0000  0.0000  628  LEU A C   
5914  O O   . LEU D 631  ? 0.9180 0.9180 0.9180 0.0000  0.0000  0.0000  628  LEU A O   
5915  C CB  . LEU D 631  ? 0.9180 0.9180 0.9180 0.0000  0.0000  0.0000  628  LEU A CB  
5916  C CG  . LEU D 631  ? 0.9180 0.9180 0.9180 0.0000  0.0000  0.0000  628  LEU A CG  
5917  C CD1 . LEU D 631  ? 0.9180 0.9180 0.9180 0.0000  0.0000  0.0000  628  LEU A CD1 
5918  C CD2 . LEU D 631  ? 0.9180 0.9180 0.9180 0.0000  0.0000  0.0000  628  LEU A CD2 
5919  N N   . SER D 632  ? 1.0429 1.0429 1.0429 0.0000  0.0000  0.0000  629  SER A N   
5920  C CA  . SER D 632  ? 1.0429 1.0429 1.0429 0.0000  0.0000  0.0000  629  SER A CA  
5921  C C   . SER D 632  ? 1.0429 1.0429 1.0429 0.0000  0.0000  0.0000  629  SER A C   
5922  O O   . SER D 632  ? 1.0429 1.0429 1.0429 0.0000  0.0000  0.0000  629  SER A O   
5923  C CB  . SER D 632  ? 1.0429 1.0429 1.0429 0.0000  0.0000  0.0000  629  SER A CB  
5924  O OG  . SER D 632  ? 1.0429 1.0429 1.0429 0.0000  0.0000  0.0000  629  SER A OG  
5925  N N   . ASN D 633  ? 0.9532 0.9532 0.9532 0.0000  0.0000  0.0000  630  ASN A N   
5926  C CA  . ASN D 633  ? 0.9532 0.9532 0.9532 0.0000  0.0000  0.0000  630  ASN A CA  
5927  C C   . ASN D 633  ? 0.9532 0.9532 0.9532 0.0000  0.0000  0.0000  630  ASN A C   
5928  O O   . ASN D 633  ? 0.9532 0.9532 0.9532 0.0000  0.0000  0.0000  630  ASN A O   
5929  C CB  . ASN D 633  ? 0.9532 0.9532 0.9532 0.0000  0.0000  0.0000  630  ASN A CB  
5930  C CG  . ASN D 633  ? 0.9532 0.9532 0.9532 0.0000  0.0000  0.0000  630  ASN A CG  
5931  O OD1 . ASN D 633  ? 0.9532 0.9532 0.9532 0.0000  0.0000  0.0000  630  ASN A OD1 
5932  N ND2 . ASN D 633  ? 0.9532 0.9532 0.9532 0.0000  0.0000  0.0000  630  ASN A ND2 
5933  N N   . ASN D 634  ? 0.8860 0.8860 0.8860 0.0000  0.0000  0.0000  631  ASN A N   
5934  C CA  . ASN D 634  ? 0.8860 0.8860 0.8860 0.0000  0.0000  0.0000  631  ASN A CA  
5935  C C   . ASN D 634  ? 0.8860 0.8860 0.8860 0.0000  0.0000  0.0000  631  ASN A C   
5936  O O   . ASN D 634  ? 0.8860 0.8860 0.8860 0.0000  0.0000  0.0000  631  ASN A O   
5937  C CB  . ASN D 634  ? 0.8860 0.8860 0.8860 0.0000  0.0000  0.0000  631  ASN A CB  
5938  C CG  . ASN D 634  ? 0.8860 0.8860 0.8860 0.0000  0.0000  0.0000  631  ASN A CG  
5939  O OD1 . ASN D 634  ? 0.8860 0.8860 0.8860 0.0000  0.0000  0.0000  631  ASN A OD1 
5940  N ND2 . ASN D 634  ? 0.8860 0.8860 0.8860 0.0000  0.0000  0.0000  631  ASN A ND2 
5941  N N   . PHE D 635  ? 0.8609 0.8609 0.8609 0.0000  0.0000  0.0000  632  PHE A N   
5942  C CA  . PHE D 635  ? 0.8609 0.8609 0.8609 0.0000  0.0000  0.0000  632  PHE A CA  
5943  C C   . PHE D 635  ? 0.8609 0.8609 0.8609 0.0000  0.0000  0.0000  632  PHE A C   
5944  O O   . PHE D 635  ? 0.8609 0.8609 0.8609 0.0000  0.0000  0.0000  632  PHE A O   
5945  C CB  . PHE D 635  ? 0.8609 0.8609 0.8609 0.0000  0.0000  0.0000  632  PHE A CB  
5946  C CG  . PHE D 635  ? 0.8609 0.8609 0.8609 0.0000  0.0000  0.0000  632  PHE A CG  
5947  C CD1 . PHE D 635  ? 0.8609 0.8609 0.8609 0.0000  0.0000  0.0000  632  PHE A CD1 
5948  C CD2 . PHE D 635  ? 0.8609 0.8609 0.8609 0.0000  0.0000  0.0000  632  PHE A CD2 
5949  C CE1 . PHE D 635  ? 0.8609 0.8609 0.8609 0.0000  0.0000  0.0000  632  PHE A CE1 
5950  C CE2 . PHE D 635  ? 0.8609 0.8609 0.8609 0.0000  0.0000  0.0000  632  PHE A CE2 
5951  C CZ  . PHE D 635  ? 0.8609 0.8609 0.8609 0.0000  0.0000  0.0000  632  PHE A CZ  
5952  N N   . ILE D 636  ? 0.9322 0.9322 0.9322 0.0000  0.0000  0.0000  633  ILE A N   
5953  C CA  . ILE D 636  ? 0.9322 0.9322 0.9322 0.0000  0.0000  0.0000  633  ILE A CA  
5954  C C   . ILE D 636  ? 0.9322 0.9322 0.9322 0.0000  0.0000  0.0000  633  ILE A C   
5955  O O   . ILE D 636  ? 0.9322 0.9322 0.9322 0.0000  0.0000  0.0000  633  ILE A O   
5956  C CB  . ILE D 636  ? 0.9322 0.9322 0.9322 0.0000  0.0000  0.0000  633  ILE A CB  
5957  C CG1 . ILE D 636  ? 0.9322 0.9322 0.9322 0.0000  0.0000  0.0000  633  ILE A CG1 
5958  C CG2 . ILE D 636  ? 0.9322 0.9322 0.9322 0.0000  0.0000  0.0000  633  ILE A CG2 
5959  C CD1 . ILE D 636  ? 0.9322 0.9322 0.9322 0.0000  0.0000  0.0000  633  ILE A CD1 
5960  N N   . GLU D 637  ? 0.9394 0.9394 0.9394 0.0000  0.0000  0.0000  634  GLU A N   
5961  C CA  . GLU D 637  ? 0.9394 0.9394 0.9394 0.0000  0.0000  0.0000  634  GLU A CA  
5962  C C   . GLU D 637  ? 0.9394 0.9394 0.9394 0.0000  0.0000  0.0000  634  GLU A C   
5963  O O   . GLU D 637  ? 0.9394 0.9394 0.9394 0.0000  0.0000  0.0000  634  GLU A O   
5964  C CB  . GLU D 637  ? 0.9394 0.9394 0.9394 0.0000  0.0000  0.0000  634  GLU A CB  
5965  C CG  . GLU D 637  ? 0.9394 0.9394 0.9394 0.0000  0.0000  0.0000  634  GLU A CG  
5966  C CD  . GLU D 637  ? 0.9394 0.9394 0.9394 0.0000  0.0000  0.0000  634  GLU A CD  
5967  O OE1 . GLU D 637  ? 0.9394 0.9394 0.9394 0.0000  0.0000  0.0000  634  GLU A OE1 
5968  O OE2 . GLU D 637  ? 0.9394 0.9394 0.9394 0.0000  0.0000  0.0000  634  GLU A OE2 
5969  N N   . PRO D 638  ? 0.9458 0.9458 0.9458 0.0000  0.0000  0.0000  635  PRO A N   
5970  C CA  . PRO D 638  ? 0.9458 0.9458 0.9458 0.0000  0.0000  0.0000  635  PRO A CA  
5971  C C   . PRO D 638  ? 0.9458 0.9458 0.9458 0.0000  0.0000  0.0000  635  PRO A C   
5972  O O   . PRO D 638  ? 0.9458 0.9458 0.9458 0.0000  0.0000  0.0000  635  PRO A O   
5973  C CB  . PRO D 638  ? 0.9458 0.9458 0.9458 0.0000  0.0000  0.0000  635  PRO A CB  
5974  C CG  . PRO D 638  ? 0.9458 0.9458 0.9458 0.0000  0.0000  0.0000  635  PRO A CG  
5975  C CD  . PRO D 638  ? 0.9458 0.9458 0.9458 0.0000  0.0000  0.0000  635  PRO A CD  
5976  N N   . LEU D 639  ? 0.9435 0.9435 0.9435 0.0000  0.0000  0.0000  636  LEU A N   
5977  C CA  . LEU D 639  ? 0.9435 0.9435 0.9435 0.0000  0.0000  0.0000  636  LEU A CA  
5978  C C   . LEU D 639  ? 0.9435 0.9435 0.9435 0.0000  0.0000  0.0000  636  LEU A C   
5979  O O   . LEU D 639  ? 0.9435 0.9435 0.9435 0.0000  0.0000  0.0000  636  LEU A O   
5980  C CB  . LEU D 639  ? 0.9435 0.9435 0.9435 0.0000  0.0000  0.0000  636  LEU A CB  
5981  C CG  . LEU D 639  ? 0.9435 0.9435 0.9435 0.0000  0.0000  0.0000  636  LEU A CG  
5982  C CD1 . LEU D 639  ? 0.9435 0.9435 0.9435 0.0000  0.0000  0.0000  636  LEU A CD1 
5983  C CD2 . LEU D 639  ? 0.9435 0.9435 0.9435 0.0000  0.0000  0.0000  636  LEU A CD2 
5984  N N   . GLU D 640  ? 1.0300 1.0300 1.0300 0.0000  0.0000  0.0000  637  GLU A N   
5985  C CA  . GLU D 640  ? 1.0300 1.0300 1.0300 0.0000  0.0000  0.0000  637  GLU A CA  
5986  C C   . GLU D 640  ? 1.0300 1.0300 1.0300 0.0000  0.0000  0.0000  637  GLU A C   
5987  O O   . GLU D 640  ? 1.0300 1.0300 1.0300 0.0000  0.0000  0.0000  637  GLU A O   
5988  C CB  . GLU D 640  ? 1.0300 1.0300 1.0300 0.0000  0.0000  0.0000  637  GLU A CB  
5989  C CG  . GLU D 640  ? 1.0300 1.0300 1.0300 0.0000  0.0000  0.0000  637  GLU A CG  
5990  C CD  . GLU D 640  ? 1.0300 1.0300 1.0300 0.0000  0.0000  0.0000  637  GLU A CD  
5991  O OE1 . GLU D 640  ? 1.0300 1.0300 1.0300 0.0000  0.0000  0.0000  637  GLU A OE1 
5992  O OE2 . GLU D 640  ? 1.0300 1.0300 1.0300 0.0000  0.0000  0.0000  637  GLU A OE2 
5993  N N   . ILE D 641  ? 1.0124 1.0124 1.0124 0.0000  0.0000  0.0000  638  ILE A N   
5994  C CA  . ILE D 641  ? 1.0124 1.0124 1.0124 0.0000  0.0000  0.0000  638  ILE A CA  
5995  C C   . ILE D 641  ? 1.0124 1.0124 1.0124 0.0000  0.0000  0.0000  638  ILE A C   
5996  O O   . ILE D 641  ? 1.0124 1.0124 1.0124 0.0000  0.0000  0.0000  638  ILE A O   
5997  C CB  . ILE D 641  ? 1.0124 1.0124 1.0124 0.0000  0.0000  0.0000  638  ILE A CB  
5998  C CG1 . ILE D 641  ? 1.0124 1.0124 1.0124 0.0000  0.0000  0.0000  638  ILE A CG1 
5999  C CG2 . ILE D 641  ? 1.0124 1.0124 1.0124 0.0000  0.0000  0.0000  638  ILE A CG2 
6000  C CD1 . ILE D 641  ? 1.0124 1.0124 1.0124 0.0000  0.0000  0.0000  638  ILE A CD1 
6001  N N   . THR D 642  ? 1.0486 1.0486 1.0486 0.0000  0.0000  0.0000  639  THR A N   
6002  C CA  . THR D 642  ? 1.0486 1.0486 1.0486 0.0000  0.0000  0.0000  639  THR A CA  
6003  C C   . THR D 642  ? 1.0486 1.0486 1.0486 0.0000  0.0000  0.0000  639  THR A C   
6004  O O   . THR D 642  ? 1.0486 1.0486 1.0486 0.0000  0.0000  0.0000  639  THR A O   
6005  C CB  . THR D 642  ? 1.0486 1.0486 1.0486 0.0000  0.0000  0.0000  639  THR A CB  
6006  O OG1 . THR D 642  ? 1.0486 1.0486 1.0486 0.0000  0.0000  0.0000  639  THR A OG1 
6007  C CG2 . THR D 642  ? 1.0486 1.0486 1.0486 0.0000  0.0000  0.0000  639  THR A CG2 
6008  N N   . LYS D 643  ? 1.0540 1.0540 1.0540 0.0000  0.0000  0.0000  640  LYS A N   
6009  C CA  . LYS D 643  ? 1.0540 1.0540 1.0540 0.0000  0.0000  0.0000  640  LYS A CA  
6010  C C   . LYS D 643  ? 1.0540 1.0540 1.0540 0.0000  0.0000  0.0000  640  LYS A C   
6011  O O   . LYS D 643  ? 1.0540 1.0540 1.0540 0.0000  0.0000  0.0000  640  LYS A O   
6012  C CB  . LYS D 643  ? 1.0540 1.0540 1.0540 0.0000  0.0000  0.0000  640  LYS A CB  
6013  C CG  . LYS D 643  ? 1.0540 1.0540 1.0540 0.0000  0.0000  0.0000  640  LYS A CG  
6014  C CD  . LYS D 643  ? 1.0540 1.0540 1.0540 0.0000  0.0000  0.0000  640  LYS A CD  
6015  C CE  . LYS D 643  ? 1.0540 1.0540 1.0540 0.0000  0.0000  0.0000  640  LYS A CE  
6016  N NZ  . LYS D 643  ? 1.0540 1.0540 1.0540 0.0000  0.0000  0.0000  640  LYS A NZ  
6017  N N   . GLU D 644  ? 1.0649 1.0649 1.0649 0.0000  0.0000  0.0000  641  GLU A N   
6018  C CA  . GLU D 644  ? 1.0649 1.0649 1.0649 0.0000  0.0000  0.0000  641  GLU A CA  
6019  C C   . GLU D 644  ? 1.0649 1.0649 1.0649 0.0000  0.0000  0.0000  641  GLU A C   
6020  O O   . GLU D 644  ? 1.0649 1.0649 1.0649 0.0000  0.0000  0.0000  641  GLU A O   
6021  C CB  . GLU D 644  ? 1.0649 1.0649 1.0649 0.0000  0.0000  0.0000  641  GLU A CB  
6022  C CG  . GLU D 644  ? 1.0649 1.0649 1.0649 0.0000  0.0000  0.0000  641  GLU A CG  
6023  C CD  . GLU D 644  ? 1.0649 1.0649 1.0649 0.0000  0.0000  0.0000  641  GLU A CD  
6024  O OE1 . GLU D 644  ? 1.0649 1.0649 1.0649 0.0000  0.0000  0.0000  641  GLU A OE1 
6025  O OE2 . GLU D 644  ? 1.0649 1.0649 1.0649 0.0000  0.0000  0.0000  641  GLU A OE2 
6026  N N   . ILE D 645  ? 0.9869 0.9869 0.9869 0.0000  0.0000  0.0000  642  ILE A N   
6027  C CA  . ILE D 645  ? 0.9869 0.9869 0.9869 0.0000  0.0000  0.0000  642  ILE A CA  
6028  C C   . ILE D 645  ? 0.9869 0.9869 0.9869 0.0000  0.0000  0.0000  642  ILE A C   
6029  O O   . ILE D 645  ? 0.9869 0.9869 0.9869 0.0000  0.0000  0.0000  642  ILE A O   
6030  C CB  . ILE D 645  ? 0.9869 0.9869 0.9869 0.0000  0.0000  0.0000  642  ILE A CB  
6031  C CG1 . ILE D 645  ? 0.9869 0.9869 0.9869 0.0000  0.0000  0.0000  642  ILE A CG1 
6032  C CG2 . ILE D 645  ? 0.9869 0.9869 0.9869 0.0000  0.0000  0.0000  642  ILE A CG2 
6033  C CD1 . ILE D 645  ? 0.9869 0.9869 0.9869 0.0000  0.0000  0.0000  642  ILE A CD1 
6034  N N   . TYR D 646  ? 0.9666 0.9666 0.9666 0.0000  0.0000  0.0000  643  TYR A N   
6035  C CA  . TYR D 646  ? 0.9666 0.9666 0.9666 0.0000  0.0000  0.0000  643  TYR A CA  
6036  C C   . TYR D 646  ? 0.9666 0.9666 0.9666 0.0000  0.0000  0.0000  643  TYR A C   
6037  O O   . TYR D 646  ? 0.9666 0.9666 0.9666 0.0000  0.0000  0.0000  643  TYR A O   
6038  C CB  . TYR D 646  ? 0.9666 0.9666 0.9666 0.0000  0.0000  0.0000  643  TYR A CB  
6039  C CG  . TYR D 646  ? 0.9666 0.9666 0.9666 0.0000  0.0000  0.0000  643  TYR A CG  
6040  C CD1 . TYR D 646  ? 0.9666 0.9666 0.9666 0.0000  0.0000  0.0000  643  TYR A CD1 
6041  C CD2 . TYR D 646  ? 0.9666 0.9666 0.9666 0.0000  0.0000  0.0000  643  TYR A CD2 
6042  C CE1 . TYR D 646  ? 0.9666 0.9666 0.9666 0.0000  0.0000  0.0000  643  TYR A CE1 
6043  C CE2 . TYR D 646  ? 0.9666 0.9666 0.9666 0.0000  0.0000  0.0000  643  TYR A CE2 
6044  C CZ  . TYR D 646  ? 0.9666 0.9666 0.9666 0.0000  0.0000  0.0000  643  TYR A CZ  
6045  O OH  . TYR D 646  ? 0.9666 0.9666 0.9666 0.0000  0.0000  0.0000  643  TYR A OH  
6046  N N   . ASP D 647  ? 1.0299 1.0299 1.0299 0.0000  0.0000  0.0000  644  ASP A N   
6047  C CA  . ASP D 647  ? 1.0299 1.0299 1.0299 0.0000  0.0000  0.0000  644  ASP A CA  
6048  C C   . ASP D 647  ? 1.0299 1.0299 1.0299 0.0000  0.0000  0.0000  644  ASP A C   
6049  O O   . ASP D 647  ? 1.0299 1.0299 1.0299 0.0000  0.0000  0.0000  644  ASP A O   
6050  C CB  . ASP D 647  ? 1.0299 1.0299 1.0299 0.0000  0.0000  0.0000  644  ASP A CB  
6051  C CG  . ASP D 647  ? 1.0299 1.0299 1.0299 0.0000  0.0000  0.0000  644  ASP A CG  
6052  O OD1 . ASP D 647  ? 1.0299 1.0299 1.0299 0.0000  0.0000  0.0000  644  ASP A OD1 
6053  O OD2 . ASP D 647  ? 1.0299 1.0299 1.0299 0.0000  0.0000  0.0000  644  ASP A OD2 
6054  N N   . LEU D 648  ? 1.0087 1.0087 1.0087 0.0000  0.0000  0.0000  645  LEU A N   
6055  C CA  . LEU D 648  ? 1.0087 1.0087 1.0087 0.0000  0.0000  0.0000  645  LEU A CA  
6056  C C   . LEU D 648  ? 1.0087 1.0087 1.0087 0.0000  0.0000  0.0000  645  LEU A C   
6057  O O   . LEU D 648  ? 1.0087 1.0087 1.0087 0.0000  0.0000  0.0000  645  LEU A O   
6058  C CB  . LEU D 648  ? 1.0087 1.0087 1.0087 0.0000  0.0000  0.0000  645  LEU A CB  
6059  C CG  . LEU D 648  ? 1.0087 1.0087 1.0087 0.0000  0.0000  0.0000  645  LEU A CG  
6060  C CD1 . LEU D 648  ? 1.0087 1.0087 1.0087 0.0000  0.0000  0.0000  645  LEU A CD1 
6061  C CD2 . LEU D 648  ? 1.0087 1.0087 1.0087 0.0000  0.0000  0.0000  645  LEU A CD2 
6062  N N   . ASN D 649  ? 0.9194 0.9194 0.9194 0.0000  0.0000  0.0000  646  ASN A N   
6063  C CA  . ASN D 649  ? 0.9194 0.9194 0.9194 0.0000  0.0000  0.0000  646  ASN A CA  
6064  C C   . ASN D 649  ? 0.9194 0.9194 0.9194 0.0000  0.0000  0.0000  646  ASN A C   
6065  O O   . ASN D 649  ? 0.9194 0.9194 0.9194 0.0000  0.0000  0.0000  646  ASN A O   
6066  C CB  . ASN D 649  ? 0.9194 0.9194 0.9194 0.0000  0.0000  0.0000  646  ASN A CB  
6067  C CG  . ASN D 649  ? 0.9194 0.9194 0.9194 0.0000  0.0000  0.0000  646  ASN A CG  
6068  O OD1 . ASN D 649  ? 0.9194 0.9194 0.9194 0.0000  0.0000  0.0000  646  ASN A OD1 
6069  N ND2 . ASN D 649  ? 0.9194 0.9194 0.9194 0.0000  0.0000  0.0000  646  ASN A ND2 
6070  N N   . ASN D 650  ? 0.9512 0.9512 0.9512 0.0000  0.0000  0.0000  647  ASN A N   
6071  C CA  . ASN D 650  ? 0.9512 0.9512 0.9512 0.0000  0.0000  0.0000  647  ASN A CA  
6072  C C   . ASN D 650  ? 0.9512 0.9512 0.9512 0.0000  0.0000  0.0000  647  ASN A C   
6073  O O   . ASN D 650  ? 0.9512 0.9512 0.9512 0.0000  0.0000  0.0000  647  ASN A O   
6074  C CB  . ASN D 650  ? 0.9512 0.9512 0.9512 0.0000  0.0000  0.0000  647  ASN A CB  
6075  C CG  . ASN D 650  ? 0.9512 0.9512 0.9512 0.0000  0.0000  0.0000  647  ASN A CG  
6076  O OD1 . ASN D 650  ? 0.9512 0.9512 0.9512 0.0000  0.0000  0.0000  647  ASN A OD1 
6077  N ND2 . ASN D 650  ? 0.9512 0.9512 0.9512 0.0000  0.0000  0.0000  647  ASN A ND2 
6078  N N   . PRO D 651  ? 1.0840 1.0840 1.0840 0.0000  0.0000  0.0000  648  PRO A N   
6079  C CA  . PRO D 651  ? 1.0840 1.0840 1.0840 0.0000  0.0000  0.0000  648  PRO A CA  
6080  C C   . PRO D 651  ? 1.0840 1.0840 1.0840 0.0000  0.0000  0.0000  648  PRO A C   
6081  O O   . PRO D 651  ? 1.0840 1.0840 1.0840 0.0000  0.0000  0.0000  648  PRO A O   
6082  C CB  . PRO D 651  ? 1.0840 1.0840 1.0840 0.0000  0.0000  0.0000  648  PRO A CB  
6083  C CG  . PRO D 651  ? 1.0840 1.0840 1.0840 0.0000  0.0000  0.0000  648  PRO A CG  
6084  C CD  . PRO D 651  ? 1.0840 1.0840 1.0840 0.0000  0.0000  0.0000  648  PRO A CD  
6085  N N   . GLU D 652  ? 1.1731 1.1731 1.1731 0.0000  0.0000  0.0000  649  GLU A N   
6086  C CA  . GLU D 652  ? 1.1731 1.1731 1.1731 0.0000  0.0000  0.0000  649  GLU A CA  
6087  C C   . GLU D 652  ? 1.1731 1.1731 1.1731 0.0000  0.0000  0.0000  649  GLU A C   
6088  O O   . GLU D 652  ? 1.1731 1.1731 1.1731 0.0000  0.0000  0.0000  649  GLU A O   
6094  N N   . LYS D 653  ? 1.2243 1.2243 1.2243 0.0000  0.0000  0.0000  650  LYS A N   
6095  C CA  . LYS D 653  ? 1.2243 1.2243 1.2243 0.0000  0.0000  0.0000  650  LYS A CA  
6096  C C   . LYS D 653  ? 1.2243 1.2243 1.2243 0.0000  0.0000  0.0000  650  LYS A C   
6097  O O   . LYS D 653  ? 1.2243 1.2243 1.2243 0.0000  0.0000  0.0000  650  LYS A O   
6103  N N   . GLU D 654  ? 1.2690 1.2690 1.2690 0.0000  0.0000  0.0000  651  GLU A N   
6104  C CA  . GLU D 654  ? 1.2690 1.2690 1.2690 0.0000  0.0000  0.0000  651  GLU A CA  
6105  C C   . GLU D 654  ? 1.2690 1.2690 1.2690 0.0000  0.0000  0.0000  651  GLU A C   
6106  O O   . GLU D 654  ? 1.2690 1.2690 1.2690 0.0000  0.0000  0.0000  651  GLU A O   
6112  N N   . PRO D 655  ? 1.2278 1.2278 1.2278 0.0000  0.0000  0.0000  652  PRO A N   
6113  C CA  . PRO D 655  ? 1.2278 1.2278 1.2278 0.0000  0.0000  0.0000  652  PRO A CA  
6114  C C   . PRO D 655  ? 1.2278 1.2278 1.2278 0.0000  0.0000  0.0000  652  PRO A C   
6115  O O   . PRO D 655  ? 1.2278 1.2278 1.2278 0.0000  0.0000  0.0000  652  PRO A O   
6116  C CB  . PRO D 655  ? 1.2278 1.2278 1.2278 0.0000  0.0000  0.0000  652  PRO A CB  
6117  C CG  . PRO D 655  ? 1.2278 1.2278 1.2278 0.0000  0.0000  0.0000  652  PRO A CG  
6118  C CD  . PRO D 655  ? 1.2278 1.2278 1.2278 0.0000  0.0000  0.0000  652  PRO A CD  
6119  N N   . LYS D 656  ? 1.1036 1.1036 1.1036 0.0000  0.0000  0.0000  653  LYS A N   
6120  C CA  . LYS D 656  ? 1.1036 1.1036 1.1036 0.0000  0.0000  0.0000  653  LYS A CA  
6121  C C   . LYS D 656  ? 1.1036 1.1036 1.1036 0.0000  0.0000  0.0000  653  LYS A C   
6122  O O   . LYS D 656  ? 1.1036 1.1036 1.1036 0.0000  0.0000  0.0000  653  LYS A O   
6123  C CB  . LYS D 656  ? 1.1036 1.1036 1.1036 0.0000  0.0000  0.0000  653  LYS A CB  
6124  C CG  . LYS D 656  ? 1.1036 1.1036 1.1036 0.0000  0.0000  0.0000  653  LYS A CG  
6125  C CD  . LYS D 656  ? 1.1036 1.1036 1.1036 0.0000  0.0000  0.0000  653  LYS A CD  
6126  C CE  . LYS D 656  ? 1.1036 1.1036 1.1036 0.0000  0.0000  0.0000  653  LYS A CE  
6127  N NZ  . LYS D 656  ? 1.1036 1.1036 1.1036 0.0000  0.0000  0.0000  653  LYS A NZ  
6128  N N   . LYS D 657  ? 1.0961 1.0961 1.0961 0.0000  0.0000  0.0000  654  LYS A N   
6129  C CA  . LYS D 657  ? 1.0961 1.0961 1.0961 0.0000  0.0000  0.0000  654  LYS A CA  
6130  C C   . LYS D 657  ? 1.0961 1.0961 1.0961 0.0000  0.0000  0.0000  654  LYS A C   
6131  O O   . LYS D 657  ? 1.0961 1.0961 1.0961 0.0000  0.0000  0.0000  654  LYS A O   
6132  C CB  . LYS D 657  ? 1.0961 1.0961 1.0961 0.0000  0.0000  0.0000  654  LYS A CB  
6133  C CG  . LYS D 657  ? 1.0961 1.0961 1.0961 0.0000  0.0000  0.0000  654  LYS A CG  
6134  C CD  . LYS D 657  ? 1.0961 1.0961 1.0961 0.0000  0.0000  0.0000  654  LYS A CD  
6135  C CE  . LYS D 657  ? 1.0961 1.0961 1.0961 0.0000  0.0000  0.0000  654  LYS A CE  
6136  N NZ  . LYS D 657  ? 1.0961 1.0961 1.0961 0.0000  0.0000  0.0000  654  LYS A NZ  
6137  N N   . PHE D 658  ? 0.9773 0.9773 0.9773 0.0000  0.0000  0.0000  655  PHE A N   
6138  C CA  . PHE D 658  ? 0.9773 0.9773 0.9773 0.0000  0.0000  0.0000  655  PHE A CA  
6139  C C   . PHE D 658  ? 0.9773 0.9773 0.9773 0.0000  0.0000  0.0000  655  PHE A C   
6140  O O   . PHE D 658  ? 0.9773 0.9773 0.9773 0.0000  0.0000  0.0000  655  PHE A O   
6141  C CB  . PHE D 658  ? 0.9773 0.9773 0.9773 0.0000  0.0000  0.0000  655  PHE A CB  
6142  C CG  . PHE D 658  ? 0.9773 0.9773 0.9773 0.0000  0.0000  0.0000  655  PHE A CG  
6143  C CD1 . PHE D 658  ? 0.9773 0.9773 0.9773 0.0000  0.0000  0.0000  655  PHE A CD1 
6144  C CD2 . PHE D 658  ? 0.9773 0.9773 0.9773 0.0000  0.0000  0.0000  655  PHE A CD2 
6145  C CE1 . PHE D 658  ? 0.9773 0.9773 0.9773 0.0000  0.0000  0.0000  655  PHE A CE1 
6146  C CE2 . PHE D 658  ? 0.9773 0.9773 0.9773 0.0000  0.0000  0.0000  655  PHE A CE2 
6147  C CZ  . PHE D 658  ? 0.9773 0.9773 0.9773 0.0000  0.0000  0.0000  655  PHE A CZ  
6148  N N   . GLN D 659  ? 1.0919 1.0919 1.0919 0.0000  0.0000  0.0000  656  GLN A N   
6149  C CA  . GLN D 659  ? 1.0919 1.0919 1.0919 0.0000  0.0000  0.0000  656  GLN A CA  
6150  C C   . GLN D 659  ? 1.0919 1.0919 1.0919 0.0000  0.0000  0.0000  656  GLN A C   
6151  O O   . GLN D 659  ? 1.0919 1.0919 1.0919 0.0000  0.0000  0.0000  656  GLN A O   
6152  C CB  . GLN D 659  ? 1.0919 1.0919 1.0919 0.0000  0.0000  0.0000  656  GLN A CB  
6153  C CG  . GLN D 659  ? 1.0919 1.0919 1.0919 0.0000  0.0000  0.0000  656  GLN A CG  
6154  C CD  . GLN D 659  ? 1.0919 1.0919 1.0919 0.0000  0.0000  0.0000  656  GLN A CD  
6155  O OE1 . GLN D 659  ? 1.0919 1.0919 1.0919 0.0000  0.0000  0.0000  656  GLN A OE1 
6156  N NE2 . GLN D 659  ? 1.0919 1.0919 1.0919 0.0000  0.0000  0.0000  656  GLN A NE2 
6157  N N   . THR D 660  ? 1.1705 1.1705 1.1705 0.0000  0.0000  0.0000  657  THR A N   
6158  C CA  . THR D 660  ? 1.1705 1.1705 1.1705 0.0000  0.0000  0.0000  657  THR A CA  
6159  C C   . THR D 660  ? 1.1705 1.1705 1.1705 0.0000  0.0000  0.0000  657  THR A C   
6160  O O   . THR D 660  ? 1.1705 1.1705 1.1705 0.0000  0.0000  0.0000  657  THR A O   
6161  C CB  . THR D 660  ? 1.1705 1.1705 1.1705 0.0000  0.0000  0.0000  657  THR A CB  
6162  O OG1 . THR D 660  ? 1.1705 1.1705 1.1705 0.0000  0.0000  0.0000  657  THR A OG1 
6163  C CG2 . THR D 660  ? 1.1705 1.1705 1.1705 0.0000  0.0000  0.0000  657  THR A CG2 
6164  N N   . ALA D 661  ? 1.2157 1.2157 1.2157 0.0000  0.0000  0.0000  658  ALA A N   
6165  C CA  . ALA D 661  ? 1.2157 1.2157 1.2157 0.0000  0.0000  0.0000  658  ALA A CA  
6166  C C   . ALA D 661  ? 1.2157 1.2157 1.2157 0.0000  0.0000  0.0000  658  ALA A C   
6167  O O   . ALA D 661  ? 1.2157 1.2157 1.2157 0.0000  0.0000  0.0000  658  ALA A O   
6168  C CB  . ALA D 661  ? 1.2157 1.2157 1.2157 0.0000  0.0000  0.0000  658  ALA A CB  
6169  N N   . TYR D 662  ? 1.2180 1.2180 1.2180 0.0000  0.0000  0.0000  659  TYR A N   
6170  C CA  . TYR D 662  ? 1.2180 1.2180 1.2180 0.0000  0.0000  0.0000  659  TYR A CA  
6171  C C   . TYR D 662  ? 1.2180 1.2180 1.2180 0.0000  0.0000  0.0000  659  TYR A C   
6172  O O   . TYR D 662  ? 1.2180 1.2180 1.2180 0.0000  0.0000  0.0000  659  TYR A O   
6173  C CB  . TYR D 662  ? 1.2180 1.2180 1.2180 0.0000  0.0000  0.0000  659  TYR A CB  
6174  C CG  . TYR D 662  ? 1.2180 1.2180 1.2180 0.0000  0.0000  0.0000  659  TYR A CG  
6175  C CD1 . TYR D 662  ? 1.2180 1.2180 1.2180 0.0000  0.0000  0.0000  659  TYR A CD1 
6176  C CD2 . TYR D 662  ? 1.2180 1.2180 1.2180 0.0000  0.0000  0.0000  659  TYR A CD2 
6177  C CE1 . TYR D 662  ? 1.2180 1.2180 1.2180 0.0000  0.0000  0.0000  659  TYR A CE1 
6178  C CE2 . TYR D 662  ? 1.2180 1.2180 1.2180 0.0000  0.0000  0.0000  659  TYR A CE2 
6179  C CZ  . TYR D 662  ? 1.2180 1.2180 1.2180 0.0000  0.0000  0.0000  659  TYR A CZ  
6180  O OH  . TYR D 662  ? 1.2180 1.2180 1.2180 0.0000  0.0000  0.0000  659  TYR A OH  
6181  N N   . ALA D 663  ? 1.2625 1.2625 1.2625 0.0000  0.0000  0.0000  660  ALA A N   
6182  C CA  . ALA D 663  ? 1.2625 1.2625 1.2625 0.0000  0.0000  0.0000  660  ALA A CA  
6183  C C   . ALA D 663  ? 1.2625 1.2625 1.2625 0.0000  0.0000  0.0000  660  ALA A C   
6184  O O   . ALA D 663  ? 1.2625 1.2625 1.2625 0.0000  0.0000  0.0000  660  ALA A O   
6185  C CB  . ALA D 663  ? 1.2625 1.2625 1.2625 0.0000  0.0000  0.0000  660  ALA A CB  
6186  N N   . LYS D 664  ? 1.2857 1.2857 1.2857 0.0000  0.0000  0.0000  661  LYS A N   
6187  C CA  . LYS D 664  ? 1.2857 1.2857 1.2857 0.0000  0.0000  0.0000  661  LYS A CA  
6188  C C   . LYS D 664  ? 1.2857 1.2857 1.2857 0.0000  0.0000  0.0000  661  LYS A C   
6189  O O   . LYS D 664  ? 1.2857 1.2857 1.2857 0.0000  0.0000  0.0000  661  LYS A O   
6190  C CB  . LYS D 664  ? 1.2857 1.2857 1.2857 0.0000  0.0000  0.0000  661  LYS A CB  
6191  C CG  . LYS D 664  ? 1.2857 1.2857 1.2857 0.0000  0.0000  0.0000  661  LYS A CG  
6192  C CD  . LYS D 664  ? 1.2857 1.2857 1.2857 0.0000  0.0000  0.0000  661  LYS A CD  
6193  C CE  . LYS D 664  ? 1.2857 1.2857 1.2857 0.0000  0.0000  0.0000  661  LYS A CE  
6194  N NZ  . LYS D 664  ? 1.2857 1.2857 1.2857 0.0000  0.0000  0.0000  661  LYS A NZ  
6195  N N   . LYS D 665  ? 1.2698 1.2698 1.2698 0.0000  0.0000  0.0000  662  LYS A N   
6196  C CA  . LYS D 665  ? 1.2698 1.2698 1.2698 0.0000  0.0000  0.0000  662  LYS A CA  
6197  C C   . LYS D 665  ? 1.2698 1.2698 1.2698 0.0000  0.0000  0.0000  662  LYS A C   
6198  O O   . LYS D 665  ? 1.2698 1.2698 1.2698 0.0000  0.0000  0.0000  662  LYS A O   
6199  C CB  . LYS D 665  ? 1.2698 1.2698 1.2698 0.0000  0.0000  0.0000  662  LYS A CB  
6200  C CG  . LYS D 665  ? 1.2698 1.2698 1.2698 0.0000  0.0000  0.0000  662  LYS A CG  
6201  C CD  . LYS D 665  ? 1.2698 1.2698 1.2698 0.0000  0.0000  0.0000  662  LYS A CD  
6202  C CE  . LYS D 665  ? 1.2698 1.2698 1.2698 0.0000  0.0000  0.0000  662  LYS A CE  
6203  N NZ  . LYS D 665  ? 1.2698 1.2698 1.2698 0.0000  0.0000  0.0000  662  LYS A NZ  
6204  N N   . THR D 666  ? 1.2711 1.2711 1.2711 0.0000  0.0000  0.0000  663  THR A N   
6205  C CA  . THR D 666  ? 1.2711 1.2711 1.2711 0.0000  0.0000  0.0000  663  THR A CA  
6206  C C   . THR D 666  ? 1.2711 1.2711 1.2711 0.0000  0.0000  0.0000  663  THR A C   
6207  O O   . THR D 666  ? 1.2711 1.2711 1.2711 0.0000  0.0000  0.0000  663  THR A O   
6208  C CB  . THR D 666  ? 1.2711 1.2711 1.2711 0.0000  0.0000  0.0000  663  THR A CB  
6209  O OG1 . THR D 666  ? 1.2711 1.2711 1.2711 0.0000  0.0000  0.0000  663  THR A OG1 
6210  C CG2 . THR D 666  ? 1.2711 1.2711 1.2711 0.0000  0.0000  0.0000  663  THR A CG2 
6211  N N   . GLY D 667  ? 1.2438 1.2438 1.2438 0.0000  0.0000  0.0000  664  GLY A N   
6212  C CA  . GLY D 667  ? 1.2438 1.2438 1.2438 0.0000  0.0000  0.0000  664  GLY A CA  
6213  C C   . GLY D 667  ? 1.2438 1.2438 1.2438 0.0000  0.0000  0.0000  664  GLY A C   
6214  O O   . GLY D 667  ? 1.2438 1.2438 1.2438 0.0000  0.0000  0.0000  664  GLY A O   
6215  N N   . ASP D 668  ? 1.2520 1.2520 1.2520 0.0000  0.0000  0.0000  665  ASP A N   
6216  C CA  . ASP D 668  ? 1.2520 1.2520 1.2520 0.0000  0.0000  0.0000  665  ASP A CA  
6217  C C   . ASP D 668  ? 1.2520 1.2520 1.2520 0.0000  0.0000  0.0000  665  ASP A C   
6218  O O   . ASP D 668  ? 1.2520 1.2520 1.2520 0.0000  0.0000  0.0000  665  ASP A O   
6219  C CB  . ASP D 668  ? 1.2520 1.2520 1.2520 0.0000  0.0000  0.0000  665  ASP A CB  
6220  C CG  . ASP D 668  ? 1.2520 1.2520 1.2520 0.0000  0.0000  0.0000  665  ASP A CG  
6221  O OD1 . ASP D 668  ? 1.2520 1.2520 1.2520 0.0000  0.0000  0.0000  665  ASP A OD1 
6222  O OD2 . ASP D 668  ? 1.2520 1.2520 1.2520 0.0000  0.0000  0.0000  665  ASP A OD2 
6223  N N   . GLN D 669  ? 1.1973 1.1973 1.1973 0.0000  0.0000  0.0000  666  GLN A N   
6224  C CA  . GLN D 669  ? 1.1973 1.1973 1.1973 0.0000  0.0000  0.0000  666  GLN A CA  
6225  C C   . GLN D 669  ? 1.1973 1.1973 1.1973 0.0000  0.0000  0.0000  666  GLN A C   
6226  O O   . GLN D 669  ? 1.1973 1.1973 1.1973 0.0000  0.0000  0.0000  666  GLN A O   
6227  C CB  . GLN D 669  ? 1.1973 1.1973 1.1973 0.0000  0.0000  0.0000  666  GLN A CB  
6228  C CG  . GLN D 669  ? 1.1973 1.1973 1.1973 0.0000  0.0000  0.0000  666  GLN A CG  
6229  C CD  . GLN D 669  ? 1.1973 1.1973 1.1973 0.0000  0.0000  0.0000  666  GLN A CD  
6230  O OE1 . GLN D 669  ? 1.1973 1.1973 1.1973 0.0000  0.0000  0.0000  666  GLN A OE1 
6231  N NE2 . GLN D 669  ? 1.1973 1.1973 1.1973 0.0000  0.0000  0.0000  666  GLN A NE2 
6232  N N   . LYS D 670  ? 1.1847 1.1847 1.1847 0.0000  0.0000  0.0000  667  LYS A N   
6233  C CA  . LYS D 670  ? 1.1847 1.1847 1.1847 0.0000  0.0000  0.0000  667  LYS A CA  
6234  C C   . LYS D 670  ? 1.1847 1.1847 1.1847 0.0000  0.0000  0.0000  667  LYS A C   
6235  O O   . LYS D 670  ? 1.1847 1.1847 1.1847 0.0000  0.0000  0.0000  667  LYS A O   
6241  N N   . GLY D 671  ? 1.1439 1.1439 1.1439 0.0000  0.0000  0.0000  668  GLY A N   
6242  C CA  . GLY D 671  ? 1.1439 1.1439 1.1439 0.0000  0.0000  0.0000  668  GLY A CA  
6243  C C   . GLY D 671  ? 1.1439 1.1439 1.1439 0.0000  0.0000  0.0000  668  GLY A C   
6244  O O   . GLY D 671  ? 1.1439 1.1439 1.1439 0.0000  0.0000  0.0000  668  GLY A O   
6245  N N   . TYR D 672  ? 1.1137 1.1137 1.1137 0.0000  0.0000  0.0000  669  TYR A N   
6246  C CA  . TYR D 672  ? 1.1137 1.1137 1.1137 0.0000  0.0000  0.0000  669  TYR A CA  
6247  C C   . TYR D 672  ? 1.1137 1.1137 1.1137 0.0000  0.0000  0.0000  669  TYR A C   
6248  O O   . TYR D 672  ? 1.1137 1.1137 1.1137 0.0000  0.0000  0.0000  669  TYR A O   
6249  C CB  . TYR D 672  ? 1.1137 1.1137 1.1137 0.0000  0.0000  0.0000  669  TYR A CB  
6250  C CG  . TYR D 672  ? 1.1137 1.1137 1.1137 0.0000  0.0000  0.0000  669  TYR A CG  
6251  C CD1 . TYR D 672  ? 1.1137 1.1137 1.1137 0.0000  0.0000  0.0000  669  TYR A CD1 
6252  C CD2 . TYR D 672  ? 1.1137 1.1137 1.1137 0.0000  0.0000  0.0000  669  TYR A CD2 
6253  C CE1 . TYR D 672  ? 1.1137 1.1137 1.1137 0.0000  0.0000  0.0000  669  TYR A CE1 
6254  C CE2 . TYR D 672  ? 1.1137 1.1137 1.1137 0.0000  0.0000  0.0000  669  TYR A CE2 
6255  C CZ  . TYR D 672  ? 1.1137 1.1137 1.1137 0.0000  0.0000  0.0000  669  TYR A CZ  
6256  O OH  . TYR D 672  ? 1.1137 1.1137 1.1137 0.0000  0.0000  0.0000  669  TYR A OH  
6257  N N   . ARG D 673  ? 1.0531 1.0531 1.0531 0.0000  0.0000  0.0000  670  ARG A N   
6258  C CA  . ARG D 673  ? 1.0531 1.0531 1.0531 0.0000  0.0000  0.0000  670  ARG A CA  
6259  C C   . ARG D 673  ? 1.0531 1.0531 1.0531 0.0000  0.0000  0.0000  670  ARG A C   
6260  O O   . ARG D 673  ? 1.0531 1.0531 1.0531 0.0000  0.0000  0.0000  670  ARG A O   
6261  C CB  . ARG D 673  ? 1.0531 1.0531 1.0531 0.0000  0.0000  0.0000  670  ARG A CB  
6262  C CG  . ARG D 673  ? 1.0531 1.0531 1.0531 0.0000  0.0000  0.0000  670  ARG A CG  
6263  C CD  . ARG D 673  ? 1.0531 1.0531 1.0531 0.0000  0.0000  0.0000  670  ARG A CD  
6264  N NE  . ARG D 673  ? 1.0531 1.0531 1.0531 0.0000  0.0000  0.0000  670  ARG A NE  
6265  C CZ  . ARG D 673  ? 1.0531 1.0531 1.0531 0.0000  0.0000  0.0000  670  ARG A CZ  
6266  N NH1 . ARG D 673  ? 1.0531 1.0531 1.0531 0.0000  0.0000  0.0000  670  ARG A NH1 
6267  N NH2 . ARG D 673  ? 1.0531 1.0531 1.0531 0.0000  0.0000  0.0000  670  ARG A NH2 
6268  N N   . GLU D 674  ? 1.0252 1.0252 1.0252 0.0000  0.0000  0.0000  671  GLU A N   
6269  C CA  . GLU D 674  ? 1.0252 1.0252 1.0252 0.0000  0.0000  0.0000  671  GLU A CA  
6270  C C   . GLU D 674  ? 1.0252 1.0252 1.0252 0.0000  0.0000  0.0000  671  GLU A C   
6271  O O   . GLU D 674  ? 1.0252 1.0252 1.0252 0.0000  0.0000  0.0000  671  GLU A O   
6272  C CB  . GLU D 674  ? 1.0252 1.0252 1.0252 0.0000  0.0000  0.0000  671  GLU A CB  
6273  C CG  . GLU D 674  ? 1.0252 1.0252 1.0252 0.0000  0.0000  0.0000  671  GLU A CG  
6274  C CD  . GLU D 674  ? 1.0252 1.0252 1.0252 0.0000  0.0000  0.0000  671  GLU A CD  
6275  O OE1 . GLU D 674  ? 1.0252 1.0252 1.0252 0.0000  0.0000  0.0000  671  GLU A OE1 
6276  O OE2 . GLU D 674  ? 1.0252 1.0252 1.0252 0.0000  0.0000  0.0000  671  GLU A OE2 
6277  N N   . ALA D 675  ? 0.9748 0.9748 0.9748 0.0000  0.0000  0.0000  672  ALA A N   
6278  C CA  . ALA D 675  ? 0.9748 0.9748 0.9748 0.0000  0.0000  0.0000  672  ALA A CA  
6279  C C   . ALA D 675  ? 0.9748 0.9748 0.9748 0.0000  0.0000  0.0000  672  ALA A C   
6280  O O   . ALA D 675  ? 0.9748 0.9748 0.9748 0.0000  0.0000  0.0000  672  ALA A O   
6281  C CB  . ALA D 675  ? 0.9748 0.9748 0.9748 0.0000  0.0000  0.0000  672  ALA A CB  
6282  N N   . LEU D 676  ? 0.9491 0.9491 0.9491 0.0000  0.0000  0.0000  673  LEU A N   
6283  C CA  . LEU D 676  ? 0.9491 0.9491 0.9491 0.0000  0.0000  0.0000  673  LEU A CA  
6284  C C   . LEU D 676  ? 0.9491 0.9491 0.9491 0.0000  0.0000  0.0000  673  LEU A C   
6285  O O   . LEU D 676  ? 0.9491 0.9491 0.9491 0.0000  0.0000  0.0000  673  LEU A O   
6286  C CB  . LEU D 676  ? 0.9491 0.9491 0.9491 0.0000  0.0000  0.0000  673  LEU A CB  
6287  C CG  . LEU D 676  ? 0.9491 0.9491 0.9491 0.0000  0.0000  0.0000  673  LEU A CG  
6288  C CD1 . LEU D 676  ? 0.9491 0.9491 0.9491 0.0000  0.0000  0.0000  673  LEU A CD1 
6289  C CD2 . LEU D 676  ? 0.9491 0.9491 0.9491 0.0000  0.0000  0.0000  673  LEU A CD2 
6290  N N   . CYS D 677  ? 0.9098 0.9098 0.9098 0.0000  0.0000  0.0000  674  CYS A N   
6291  C CA  . CYS D 677  ? 0.9098 0.9098 0.9098 0.0000  0.0000  0.0000  674  CYS A CA  
6292  C C   . CYS D 677  ? 0.9098 0.9098 0.9098 0.0000  0.0000  0.0000  674  CYS A C   
6293  O O   . CYS D 677  ? 0.9098 0.9098 0.9098 0.0000  0.0000  0.0000  674  CYS A O   
6294  C CB  . CYS D 677  ? 0.9098 0.9098 0.9098 0.0000  0.0000  0.0000  674  CYS A CB  
6295  S SG  . CYS D 677  ? 0.9098 0.9098 0.9098 0.0000  0.0000  0.0000  674  CYS A SG  
6296  N N   . LYS D 678  ? 0.9335 0.9335 0.9335 0.0000  0.0000  0.0000  675  LYS A N   
6297  C CA  . LYS D 678  ? 0.9335 0.9335 0.9335 0.0000  0.0000  0.0000  675  LYS A CA  
6298  C C   . LYS D 678  ? 0.9335 0.9335 0.9335 0.0000  0.0000  0.0000  675  LYS A C   
6299  O O   . LYS D 678  ? 0.9335 0.9335 0.9335 0.0000  0.0000  0.0000  675  LYS A O   
6300  C CB  . LYS D 678  ? 0.9335 0.9335 0.9335 0.0000  0.0000  0.0000  675  LYS A CB  
6301  C CG  . LYS D 678  ? 0.9335 0.9335 0.9335 0.0000  0.0000  0.0000  675  LYS A CG  
6302  C CD  . LYS D 678  ? 0.9335 0.9335 0.9335 0.0000  0.0000  0.0000  675  LYS A CD  
6303  C CE  . LYS D 678  ? 0.9335 0.9335 0.9335 0.0000  0.0000  0.0000  675  LYS A CE  
6304  N NZ  . LYS D 678  ? 0.9335 0.9335 0.9335 0.0000  0.0000  0.0000  675  LYS A NZ  
6305  N N   . TRP D 679  ? 0.8525 0.8525 0.8525 0.0000  0.0000  0.0000  676  TRP A N   
6306  C CA  . TRP D 679  ? 0.8525 0.8525 0.8525 0.0000  0.0000  0.0000  676  TRP A CA  
6307  C C   . TRP D 679  ? 0.8525 0.8525 0.8525 0.0000  0.0000  0.0000  676  TRP A C   
6308  O O   . TRP D 679  ? 0.8525 0.8525 0.8525 0.0000  0.0000  0.0000  676  TRP A O   
6309  C CB  . TRP D 679  ? 0.8525 0.8525 0.8525 0.0000  0.0000  0.0000  676  TRP A CB  
6310  C CG  . TRP D 679  ? 0.8525 0.8525 0.8525 0.0000  0.0000  0.0000  676  TRP A CG  
6311  C CD1 . TRP D 679  ? 0.8525 0.8525 0.8525 0.0000  0.0000  0.0000  676  TRP A CD1 
6312  C CD2 . TRP D 679  ? 0.8525 0.8525 0.8525 0.0000  0.0000  0.0000  676  TRP A CD2 
6313  N NE1 . TRP D 679  ? 0.8525 0.8525 0.8525 0.0000  0.0000  0.0000  676  TRP A NE1 
6314  C CE2 . TRP D 679  ? 0.8525 0.8525 0.8525 0.0000  0.0000  0.0000  676  TRP A CE2 
6315  C CE3 . TRP D 679  ? 0.8525 0.8525 0.8525 0.0000  0.0000  0.0000  676  TRP A CE3 
6316  C CZ2 . TRP D 679  ? 0.8525 0.8525 0.8525 0.0000  0.0000  0.0000  676  TRP A CZ2 
6317  C CZ3 . TRP D 679  ? 0.8525 0.8525 0.8525 0.0000  0.0000  0.0000  676  TRP A CZ3 
6318  C CH2 . TRP D 679  ? 0.8525 0.8525 0.8525 0.0000  0.0000  0.0000  676  TRP A CH2 
6319  N N   . ILE D 680  ? 0.8493 0.8493 0.8493 0.0000  0.0000  0.0000  677  ILE A N   
6320  C CA  . ILE D 680  ? 0.8493 0.8493 0.8493 0.0000  0.0000  0.0000  677  ILE A CA  
6321  C C   . ILE D 680  ? 0.8493 0.8493 0.8493 0.0000  0.0000  0.0000  677  ILE A C   
6322  O O   . ILE D 680  ? 0.8493 0.8493 0.8493 0.0000  0.0000  0.0000  677  ILE A O   
6323  C CB  . ILE D 680  ? 0.8493 0.8493 0.8493 0.0000  0.0000  0.0000  677  ILE A CB  
6324  C CG1 . ILE D 680  ? 0.8493 0.8493 0.8493 0.0000  0.0000  0.0000  677  ILE A CG1 
6325  C CG2 . ILE D 680  ? 0.8493 0.8493 0.8493 0.0000  0.0000  0.0000  677  ILE A CG2 
6326  C CD1 . ILE D 680  ? 0.8493 0.8493 0.8493 0.0000  0.0000  0.0000  677  ILE A CD1 
6327  N N   . ASP D 681  ? 0.9022 0.9022 0.9022 0.0000  0.0000  0.0000  678  ASP A N   
6328  C CA  . ASP D 681  ? 0.9022 0.9022 0.9022 0.0000  0.0000  0.0000  678  ASP A CA  
6329  C C   . ASP D 681  ? 0.9022 0.9022 0.9022 0.0000  0.0000  0.0000  678  ASP A C   
6330  O O   . ASP D 681  ? 0.9022 0.9022 0.9022 0.0000  0.0000  0.0000  678  ASP A O   
6331  C CB  . ASP D 681  ? 0.9022 0.9022 0.9022 0.0000  0.0000  0.0000  678  ASP A CB  
6332  C CG  . ASP D 681  ? 0.9022 0.9022 0.9022 0.0000  0.0000  0.0000  678  ASP A CG  
6333  O OD1 . ASP D 681  ? 0.9022 0.9022 0.9022 0.0000  0.0000  0.0000  678  ASP A OD1 
6334  O OD2 . ASP D 681  ? 0.9022 0.9022 0.9022 0.0000  0.0000  0.0000  678  ASP A OD2 
6335  N N   . PHE D 682  ? 0.8412 0.8412 0.8412 0.0000  0.0000  0.0000  679  PHE A N   
6336  C CA  . PHE D 682  ? 0.8412 0.8412 0.8412 0.0000  0.0000  0.0000  679  PHE A CA  
6337  C C   . PHE D 682  ? 0.8412 0.8412 0.8412 0.0000  0.0000  0.0000  679  PHE A C   
6338  O O   . PHE D 682  ? 0.8412 0.8412 0.8412 0.0000  0.0000  0.0000  679  PHE A O   
6339  C CB  . PHE D 682  ? 0.8412 0.8412 0.8412 0.0000  0.0000  0.0000  679  PHE A CB  
6340  C CG  . PHE D 682  ? 0.8412 0.8412 0.8412 0.0000  0.0000  0.0000  679  PHE A CG  
6341  C CD1 . PHE D 682  ? 0.8412 0.8412 0.8412 0.0000  0.0000  0.0000  679  PHE A CD1 
6342  C CD2 . PHE D 682  ? 0.8412 0.8412 0.8412 0.0000  0.0000  0.0000  679  PHE A CD2 
6343  C CE1 . PHE D 682  ? 0.8412 0.8412 0.8412 0.0000  0.0000  0.0000  679  PHE A CE1 
6344  C CE2 . PHE D 682  ? 0.8412 0.8412 0.8412 0.0000  0.0000  0.0000  679  PHE A CE2 
6345  C CZ  . PHE D 682  ? 0.8412 0.8412 0.8412 0.0000  0.0000  0.0000  679  PHE A CZ  
6346  N N   . THR D 683  ? 0.8137 0.8137 0.8137 0.0000  0.0000  0.0000  680  THR A N   
6347  C CA  . THR D 683  ? 0.8137 0.8137 0.8137 0.0000  0.0000  0.0000  680  THR A CA  
6348  C C   . THR D 683  ? 0.8137 0.8137 0.8137 0.0000  0.0000  0.0000  680  THR A C   
6349  O O   . THR D 683  ? 0.8137 0.8137 0.8137 0.0000  0.0000  0.0000  680  THR A O   
6350  C CB  . THR D 683  ? 0.8137 0.8137 0.8137 0.0000  0.0000  0.0000  680  THR A CB  
6351  O OG1 . THR D 683  ? 0.8137 0.8137 0.8137 0.0000  0.0000  0.0000  680  THR A OG1 
6352  C CG2 . THR D 683  ? 0.8137 0.8137 0.8137 0.0000  0.0000  0.0000  680  THR A CG2 
6353  N N   . ARG D 684  ? 0.8671 0.8671 0.8671 0.0000  0.0000  0.0000  681  ARG A N   
6354  C CA  . ARG D 684  ? 0.8671 0.8671 0.8671 0.0000  0.0000  0.0000  681  ARG A CA  
6355  C C   . ARG D 684  ? 0.8671 0.8671 0.8671 0.0000  0.0000  0.0000  681  ARG A C   
6356  O O   . ARG D 684  ? 0.8671 0.8671 0.8671 0.0000  0.0000  0.0000  681  ARG A O   
6357  C CB  . ARG D 684  ? 0.8671 0.8671 0.8671 0.0000  0.0000  0.0000  681  ARG A CB  
6358  C CG  . ARG D 684  ? 0.8671 0.8671 0.8671 0.0000  0.0000  0.0000  681  ARG A CG  
6359  C CD  . ARG D 684  ? 0.8671 0.8671 0.8671 0.0000  0.0000  0.0000  681  ARG A CD  
6360  N NE  . ARG D 684  ? 0.8671 0.8671 0.8671 0.0000  0.0000  0.0000  681  ARG A NE  
6361  C CZ  . ARG D 684  ? 0.8671 0.8671 0.8671 0.0000  0.0000  0.0000  681  ARG A CZ  
6362  N NH1 . ARG D 684  ? 0.8671 0.8671 0.8671 0.0000  0.0000  0.0000  681  ARG A NH1 
6363  N NH2 . ARG D 684  ? 0.8671 0.8671 0.8671 0.0000  0.0000  0.0000  681  ARG A NH2 
6364  N N   . ASP D 685  ? 0.8562 0.8562 0.8562 0.0000  0.0000  0.0000  682  ASP A N   
6365  C CA  . ASP D 685  ? 0.8562 0.8562 0.8562 0.0000  0.0000  0.0000  682  ASP A CA  
6366  C C   . ASP D 685  ? 0.8562 0.8562 0.8562 0.0000  0.0000  0.0000  682  ASP A C   
6367  O O   . ASP D 685  ? 0.8562 0.8562 0.8562 0.0000  0.0000  0.0000  682  ASP A O   
6368  C CB  . ASP D 685  ? 0.8562 0.8562 0.8562 0.0000  0.0000  0.0000  682  ASP A CB  
6369  C CG  . ASP D 685  ? 0.8562 0.8562 0.8562 0.0000  0.0000  0.0000  682  ASP A CG  
6370  O OD1 . ASP D 685  ? 0.8562 0.8562 0.8562 0.0000  0.0000  0.0000  682  ASP A OD1 
6371  O OD2 . ASP D 685  ? 0.8562 0.8562 0.8562 0.0000  0.0000  0.0000  682  ASP A OD2 
6372  N N   . PHE D 686  ? 0.7688 0.7688 0.7688 0.0000  0.0000  0.0000  683  PHE A N   
6373  C CA  . PHE D 686  ? 0.7688 0.7688 0.7688 0.0000  0.0000  0.0000  683  PHE A CA  
6374  C C   . PHE D 686  ? 0.7688 0.7688 0.7688 0.0000  0.0000  0.0000  683  PHE A C   
6375  O O   . PHE D 686  ? 0.7688 0.7688 0.7688 0.0000  0.0000  0.0000  683  PHE A O   
6376  C CB  . PHE D 686  ? 0.7688 0.7688 0.7688 0.0000  0.0000  0.0000  683  PHE A CB  
6377  C CG  . PHE D 686  ? 0.7688 0.7688 0.7688 0.0000  0.0000  0.0000  683  PHE A CG  
6378  C CD1 . PHE D 686  ? 0.7688 0.7688 0.7688 0.0000  0.0000  0.0000  683  PHE A CD1 
6379  C CD2 . PHE D 686  ? 0.7688 0.7688 0.7688 0.0000  0.0000  0.0000  683  PHE A CD2 
6380  C CE1 . PHE D 686  ? 0.7688 0.7688 0.7688 0.0000  0.0000  0.0000  683  PHE A CE1 
6381  C CE2 . PHE D 686  ? 0.7688 0.7688 0.7688 0.0000  0.0000  0.0000  683  PHE A CE2 
6382  C CZ  . PHE D 686  ? 0.7688 0.7688 0.7688 0.0000  0.0000  0.0000  683  PHE A CZ  
6383  N N   . LEU D 687  ? 0.7741 0.7741 0.7741 0.0000  0.0000  0.0000  684  LEU A N   
6384  C CA  . LEU D 687  ? 0.7741 0.7741 0.7741 0.0000  0.0000  0.0000  684  LEU A CA  
6385  C C   . LEU D 687  ? 0.7741 0.7741 0.7741 0.0000  0.0000  0.0000  684  LEU A C   
6386  O O   . LEU D 687  ? 0.7741 0.7741 0.7741 0.0000  0.0000  0.0000  684  LEU A O   
6387  C CB  . LEU D 687  ? 0.7741 0.7741 0.7741 0.0000  0.0000  0.0000  684  LEU A CB  
6388  C CG  . LEU D 687  ? 0.7741 0.7741 0.7741 0.0000  0.0000  0.0000  684  LEU A CG  
6389  C CD1 . LEU D 687  ? 0.7741 0.7741 0.7741 0.0000  0.0000  0.0000  684  LEU A CD1 
6390  C CD2 . LEU D 687  ? 0.7741 0.7741 0.7741 0.0000  0.0000  0.0000  684  LEU A CD2 
6391  N N   . SER D 688  ? 0.8174 0.8174 0.8174 0.0000  0.0000  0.0000  685  SER A N   
6392  C CA  . SER D 688  ? 0.8174 0.8174 0.8174 0.0000  0.0000  0.0000  685  SER A CA  
6393  C C   . SER D 688  ? 0.8174 0.8174 0.8174 0.0000  0.0000  0.0000  685  SER A C   
6394  O O   . SER D 688  ? 0.8174 0.8174 0.8174 0.0000  0.0000  0.0000  685  SER A O   
6395  C CB  . SER D 688  ? 0.8174 0.8174 0.8174 0.0000  0.0000  0.0000  685  SER A CB  
6396  O OG  . SER D 688  ? 0.8174 0.8174 0.8174 0.0000  0.0000  0.0000  685  SER A OG  
6397  N N   . LYS D 689  ? 0.8572 0.8572 0.8572 0.0000  0.0000  0.0000  686  LYS A N   
6398  C CA  . LYS D 689  ? 0.8572 0.8572 0.8572 0.0000  0.0000  0.0000  686  LYS A CA  
6399  C C   . LYS D 689  ? 0.8572 0.8572 0.8572 0.0000  0.0000  0.0000  686  LYS A C   
6400  O O   . LYS D 689  ? 0.8572 0.8572 0.8572 0.0000  0.0000  0.0000  686  LYS A O   
6401  C CB  . LYS D 689  ? 0.8572 0.8572 0.8572 0.0000  0.0000  0.0000  686  LYS A CB  
6402  C CG  . LYS D 689  ? 0.8572 0.8572 0.8572 0.0000  0.0000  0.0000  686  LYS A CG  
6403  C CD  . LYS D 689  ? 0.8572 0.8572 0.8572 0.0000  0.0000  0.0000  686  LYS A CD  
6404  C CE  . LYS D 689  ? 0.8572 0.8572 0.8572 0.0000  0.0000  0.0000  686  LYS A CE  
6405  N NZ  . LYS D 689  ? 0.8572 0.8572 0.8572 0.0000  0.0000  0.0000  686  LYS A NZ  
6406  N N   . TYR D 690  ? 0.7469 0.7469 0.7469 0.0000  0.0000  0.0000  687  TYR A N   
6407  C CA  . TYR D 690  ? 0.7469 0.7469 0.7469 0.0000  0.0000  0.0000  687  TYR A CA  
6408  C C   . TYR D 690  ? 0.7469 0.7469 0.7469 0.0000  0.0000  0.0000  687  TYR A C   
6409  O O   . TYR D 690  ? 0.7469 0.7469 0.7469 0.0000  0.0000  0.0000  687  TYR A O   
6410  C CB  . TYR D 690  ? 0.7469 0.7469 0.7469 0.0000  0.0000  0.0000  687  TYR A CB  
6411  C CG  . TYR D 690  ? 0.7469 0.7469 0.7469 0.0000  0.0000  0.0000  687  TYR A CG  
6412  C CD1 . TYR D 690  ? 0.7469 0.7469 0.7469 0.0000  0.0000  0.0000  687  TYR A CD1 
6413  C CD2 . TYR D 690  ? 0.7469 0.7469 0.7469 0.0000  0.0000  0.0000  687  TYR A CD2 
6414  C CE1 . TYR D 690  ? 0.7469 0.7469 0.7469 0.0000  0.0000  0.0000  687  TYR A CE1 
6415  C CE2 . TYR D 690  ? 0.7469 0.7469 0.7469 0.0000  0.0000  0.0000  687  TYR A CE2 
6416  C CZ  . TYR D 690  ? 0.7469 0.7469 0.7469 0.0000  0.0000  0.0000  687  TYR A CZ  
6417  O OH  . TYR D 690  ? 0.7469 0.7469 0.7469 0.0000  0.0000  0.0000  687  TYR A OH  
6418  N N   . THR D 691  ? 0.7533 0.7533 0.7533 0.0000  0.0000  0.0000  688  THR A N   
6419  C CA  . THR D 691  ? 0.7533 0.7533 0.7533 0.0000  0.0000  0.0000  688  THR A CA  
6420  C C   . THR D 691  ? 0.7533 0.7533 0.7533 0.0000  0.0000  0.0000  688  THR A C   
6421  O O   . THR D 691  ? 0.7533 0.7533 0.7533 0.0000  0.0000  0.0000  688  THR A O   
6422  C CB  . THR D 691  ? 0.7533 0.7533 0.7533 0.0000  0.0000  0.0000  688  THR A CB  
6423  O OG1 . THR D 691  ? 0.7533 0.7533 0.7533 0.0000  0.0000  0.0000  688  THR A OG1 
6424  C CG2 . THR D 691  ? 0.7533 0.7533 0.7533 0.0000  0.0000  0.0000  688  THR A CG2 
6425  N N   . LYS D 692  ? 0.6745 0.6745 0.6745 0.0000  0.0000  0.0000  689  LYS A N   
6426  C CA  . LYS D 692  ? 0.6745 0.6745 0.6745 0.0000  0.0000  0.0000  689  LYS A CA  
6427  C C   . LYS D 692  ? 0.6745 0.6745 0.6745 0.0000  0.0000  0.0000  689  LYS A C   
6428  O O   . LYS D 692  ? 0.6745 0.6745 0.6745 0.0000  0.0000  0.0000  689  LYS A O   
6429  C CB  . LYS D 692  ? 0.6745 0.6745 0.6745 0.0000  0.0000  0.0000  689  LYS A CB  
6430  C CG  . LYS D 692  ? 0.6745 0.6745 0.6745 0.0000  0.0000  0.0000  689  LYS A CG  
6431  C CD  . LYS D 692  ? 0.6745 0.6745 0.6745 0.0000  0.0000  0.0000  689  LYS A CD  
6432  C CE  . LYS D 692  ? 0.6745 0.6745 0.6745 0.0000  0.0000  0.0000  689  LYS A CE  
6433  N NZ  . LYS D 692  ? 0.6745 0.6745 0.6745 0.0000  0.0000  0.0000  689  LYS A NZ  
6434  N N   . THR D 693  ? 0.7713 0.7713 0.7713 0.0000  0.0000  0.0000  690  THR A N   
6435  C CA  . THR D 693  ? 0.7713 0.7713 0.7713 0.0000  0.0000  0.0000  690  THR A CA  
6436  C C   . THR D 693  ? 0.7713 0.7713 0.7713 0.0000  0.0000  0.0000  690  THR A C   
6437  O O   . THR D 693  ? 0.7713 0.7713 0.7713 0.0000  0.0000  0.0000  690  THR A O   
6438  C CB  . THR D 693  ? 0.7713 0.7713 0.7713 0.0000  0.0000  0.0000  690  THR A CB  
6439  O OG1 . THR D 693  ? 0.7713 0.7713 0.7713 0.0000  0.0000  0.0000  690  THR A OG1 
6440  C CG2 . THR D 693  ? 0.7713 0.7713 0.7713 0.0000  0.0000  0.0000  690  THR A CG2 
6441  N N   . THR D 694  ? 0.8108 0.8108 0.8108 0.0000  0.0000  0.0000  691  THR A N   
6442  C CA  . THR D 694  ? 0.8108 0.8108 0.8108 0.0000  0.0000  0.0000  691  THR A CA  
6443  C C   . THR D 694  ? 0.8108 0.8108 0.8108 0.0000  0.0000  0.0000  691  THR A C   
6444  O O   . THR D 694  ? 0.8108 0.8108 0.8108 0.0000  0.0000  0.0000  691  THR A O   
6445  C CB  . THR D 694  ? 0.8108 0.8108 0.8108 0.0000  0.0000  0.0000  691  THR A CB  
6446  O OG1 . THR D 694  ? 0.8108 0.8108 0.8108 0.0000  0.0000  0.0000  691  THR A OG1 
6447  C CG2 . THR D 694  ? 0.8108 0.8108 0.8108 0.0000  0.0000  0.0000  691  THR A CG2 
6448  N N   . SER D 695  ? 0.8487 0.8487 0.8487 0.0000  0.0000  0.0000  692  SER A N   
6449  C CA  . SER D 695  ? 0.8487 0.8487 0.8487 0.0000  0.0000  0.0000  692  SER A CA  
6450  C C   . SER D 695  ? 0.8487 0.8487 0.8487 0.0000  0.0000  0.0000  692  SER A C   
6451  O O   . SER D 695  ? 0.8487 0.8487 0.8487 0.0000  0.0000  0.0000  692  SER A O   
6452  C CB  . SER D 695  ? 0.8487 0.8487 0.8487 0.0000  0.0000  0.0000  692  SER A CB  
6453  O OG  . SER D 695  ? 0.8487 0.8487 0.8487 0.0000  0.0000  0.0000  692  SER A OG  
6454  N N   . ILE D 696  ? 0.7923 0.7923 0.7923 0.0000  0.0000  0.0000  693  ILE A N   
6455  C CA  . ILE D 696  ? 0.7923 0.7923 0.7923 0.0000  0.0000  0.0000  693  ILE A CA  
6456  C C   . ILE D 696  ? 0.7923 0.7923 0.7923 0.0000  0.0000  0.0000  693  ILE A C   
6457  O O   . ILE D 696  ? 0.7923 0.7923 0.7923 0.0000  0.0000  0.0000  693  ILE A O   
6458  C CB  . ILE D 696  ? 0.7923 0.7923 0.7923 0.0000  0.0000  0.0000  693  ILE A CB  
6459  C CG1 . ILE D 696  ? 0.7923 0.7923 0.7923 0.0000  0.0000  0.0000  693  ILE A CG1 
6460  C CG2 . ILE D 696  ? 0.7923 0.7923 0.7923 0.0000  0.0000  0.0000  693  ILE A CG2 
6461  C CD1 . ILE D 696  ? 0.7923 0.7923 0.7923 0.0000  0.0000  0.0000  693  ILE A CD1 
6462  N N   . ASP D 697  ? 0.8969 0.8969 0.8969 0.0000  0.0000  0.0000  694  ASP A N   
6463  C CA  . ASP D 697  ? 0.8969 0.8969 0.8969 0.0000  0.0000  0.0000  694  ASP A CA  
6464  C C   . ASP D 697  ? 0.8969 0.8969 0.8969 0.0000  0.0000  0.0000  694  ASP A C   
6465  O O   . ASP D 697  ? 0.8969 0.8969 0.8969 0.0000  0.0000  0.0000  694  ASP A O   
6466  C CB  . ASP D 697  ? 0.8969 0.8969 0.8969 0.0000  0.0000  0.0000  694  ASP A CB  
6467  C CG  . ASP D 697  ? 0.8969 0.8969 0.8969 0.0000  0.0000  0.0000  694  ASP A CG  
6468  O OD1 . ASP D 697  ? 0.8969 0.8969 0.8969 0.0000  0.0000  0.0000  694  ASP A OD1 
6469  O OD2 . ASP D 697  ? 0.8969 0.8969 0.8969 0.0000  0.0000  0.0000  694  ASP A OD2 
6470  N N   . LEU D 698  ? 0.9337 0.9337 0.9337 0.0000  0.0000  0.0000  695  LEU A N   
6471  C CA  . LEU D 698  ? 0.9337 0.9337 0.9337 0.0000  0.0000  0.0000  695  LEU A CA  
6472  C C   . LEU D 698  ? 0.9337 0.9337 0.9337 0.0000  0.0000  0.0000  695  LEU A C   
6473  O O   . LEU D 698  ? 0.9337 0.9337 0.9337 0.0000  0.0000  0.0000  695  LEU A O   
6474  C CB  . LEU D 698  ? 0.9337 0.9337 0.9337 0.0000  0.0000  0.0000  695  LEU A CB  
6475  C CG  . LEU D 698  ? 0.9337 0.9337 0.9337 0.0000  0.0000  0.0000  695  LEU A CG  
6476  C CD1 . LEU D 698  ? 0.9337 0.9337 0.9337 0.0000  0.0000  0.0000  695  LEU A CD1 
6477  C CD2 . LEU D 698  ? 0.9337 0.9337 0.9337 0.0000  0.0000  0.0000  695  LEU A CD2 
6478  N N   . SER D 699  ? 1.0029 1.0029 1.0029 0.0000  0.0000  0.0000  696  SER A N   
6479  C CA  . SER D 699  ? 1.0029 1.0029 1.0029 0.0000  0.0000  0.0000  696  SER A CA  
6480  C C   . SER D 699  ? 1.0029 1.0029 1.0029 0.0000  0.0000  0.0000  696  SER A C   
6481  O O   . SER D 699  ? 1.0029 1.0029 1.0029 0.0000  0.0000  0.0000  696  SER A O   
6482  C CB  . SER D 699  ? 1.0029 1.0029 1.0029 0.0000  0.0000  0.0000  696  SER A CB  
6483  O OG  . SER D 699  ? 1.0029 1.0029 1.0029 0.0000  0.0000  0.0000  696  SER A OG  
6484  N N   . SER D 700  ? 0.9691 0.9691 0.9691 0.0000  0.0000  0.0000  697  SER A N   
6485  C CA  . SER D 700  ? 0.9691 0.9691 0.9691 0.0000  0.0000  0.0000  697  SER A CA  
6486  C C   . SER D 700  ? 0.9691 0.9691 0.9691 0.0000  0.0000  0.0000  697  SER A C   
6487  O O   . SER D 700  ? 0.9691 0.9691 0.9691 0.0000  0.0000  0.0000  697  SER A O   
6488  C CB  . SER D 700  ? 0.9691 0.9691 0.9691 0.0000  0.0000  0.0000  697  SER A CB  
6489  O OG  . SER D 700  ? 0.9691 0.9691 0.9691 0.0000  0.0000  0.0000  697  SER A OG  
6490  N N   . LEU D 701  ? 0.8983 0.8983 0.8983 0.0000  0.0000  0.0000  698  LEU A N   
6491  C CA  . LEU D 701  ? 0.8983 0.8983 0.8983 0.0000  0.0000  0.0000  698  LEU A CA  
6492  C C   . LEU D 701  ? 0.8983 0.8983 0.8983 0.0000  0.0000  0.0000  698  LEU A C   
6493  O O   . LEU D 701  ? 0.8983 0.8983 0.8983 0.0000  0.0000  0.0000  698  LEU A O   
6494  C CB  . LEU D 701  ? 0.8983 0.8983 0.8983 0.0000  0.0000  0.0000  698  LEU A CB  
6495  C CG  . LEU D 701  ? 0.8983 0.8983 0.8983 0.0000  0.0000  0.0000  698  LEU A CG  
6496  C CD1 . LEU D 701  ? 0.8983 0.8983 0.8983 0.0000  0.0000  0.0000  698  LEU A CD1 
6497  C CD2 . LEU D 701  ? 0.8983 0.8983 0.8983 0.0000  0.0000  0.0000  698  LEU A CD2 
6498  N N   . ARG D 702  ? 0.8830 0.8830 0.8830 0.0000  0.0000  0.0000  699  ARG A N   
6499  C CA  . ARG D 702  ? 0.8830 0.8830 0.8830 0.0000  0.0000  0.0000  699  ARG A CA  
6500  C C   . ARG D 702  ? 0.8830 0.8830 0.8830 0.0000  0.0000  0.0000  699  ARG A C   
6501  O O   . ARG D 702  ? 0.8830 0.8830 0.8830 0.0000  0.0000  0.0000  699  ARG A O   
6502  C CB  . ARG D 702  ? 0.8830 0.8830 0.8830 0.0000  0.0000  0.0000  699  ARG A CB  
6503  C CG  . ARG D 702  ? 0.8830 0.8830 0.8830 0.0000  0.0000  0.0000  699  ARG A CG  
6504  C CD  . ARG D 702  ? 0.8830 0.8830 0.8830 0.0000  0.0000  0.0000  699  ARG A CD  
6505  N NE  . ARG D 702  ? 0.8830 0.8830 0.8830 0.0000  0.0000  0.0000  699  ARG A NE  
6506  C CZ  . ARG D 702  ? 0.8830 0.8830 0.8830 0.0000  0.0000  0.0000  699  ARG A CZ  
6507  N NH1 . ARG D 702  ? 0.8830 0.8830 0.8830 0.0000  0.0000  0.0000  699  ARG A NH1 
6508  N NH2 . ARG D 702  ? 0.8830 0.8830 0.8830 0.0000  0.0000  0.0000  699  ARG A NH2 
6509  N N   . PRO D 703  ? 0.8910 0.8910 0.8910 0.0000  0.0000  0.0000  700  PRO A N   
6510  C CA  . PRO D 703  ? 0.8910 0.8910 0.8910 0.0000  0.0000  0.0000  700  PRO A CA  
6511  C C   . PRO D 703  ? 0.8910 0.8910 0.8910 0.0000  0.0000  0.0000  700  PRO A C   
6512  O O   . PRO D 703  ? 0.8910 0.8910 0.8910 0.0000  0.0000  0.0000  700  PRO A O   
6513  C CB  . PRO D 703  ? 0.8910 0.8910 0.8910 0.0000  0.0000  0.0000  700  PRO A CB  
6514  C CG  . PRO D 703  ? 0.8910 0.8910 0.8910 0.0000  0.0000  0.0000  700  PRO A CG  
6515  C CD  . PRO D 703  ? 0.8910 0.8910 0.8910 0.0000  0.0000  0.0000  700  PRO A CD  
6516  N N   . SER D 704  ? 0.8812 0.8812 0.8812 0.0000  0.0000  0.0000  701  SER A N   
6517  C CA  . SER D 704  ? 0.8812 0.8812 0.8812 0.0000  0.0000  0.0000  701  SER A CA  
6518  C C   . SER D 704  ? 0.8812 0.8812 0.8812 0.0000  0.0000  0.0000  701  SER A C   
6519  O O   . SER D 704  ? 0.8812 0.8812 0.8812 0.0000  0.0000  0.0000  701  SER A O   
6520  C CB  . SER D 704  ? 0.8812 0.8812 0.8812 0.0000  0.0000  0.0000  701  SER A CB  
6521  O OG  . SER D 704  ? 0.8812 0.8812 0.8812 0.0000  0.0000  0.0000  701  SER A OG  
6522  N N   . SER D 705  ? 0.8868 0.8868 0.8868 0.0000  0.0000  0.0000  702  SER A N   
6523  C CA  . SER D 705  ? 0.8868 0.8868 0.8868 0.0000  0.0000  0.0000  702  SER A CA  
6524  C C   . SER D 705  ? 0.8868 0.8868 0.8868 0.0000  0.0000  0.0000  702  SER A C   
6525  O O   . SER D 705  ? 0.8868 0.8868 0.8868 0.0000  0.0000  0.0000  702  SER A O   
6526  C CB  . SER D 705  ? 0.8868 0.8868 0.8868 0.0000  0.0000  0.0000  702  SER A CB  
6527  O OG  . SER D 705  ? 0.8868 0.8868 0.8868 0.0000  0.0000  0.0000  702  SER A OG  
6528  N N   . GLN D 706  ? 0.8468 0.8468 0.8468 0.0000  0.0000  0.0000  703  GLN A N   
6529  C CA  . GLN D 706  ? 0.8468 0.8468 0.8468 0.0000  0.0000  0.0000  703  GLN A CA  
6530  C C   . GLN D 706  ? 0.8468 0.8468 0.8468 0.0000  0.0000  0.0000  703  GLN A C   
6531  O O   . GLN D 706  ? 0.8468 0.8468 0.8468 0.0000  0.0000  0.0000  703  GLN A O   
6532  C CB  . GLN D 706  ? 0.8468 0.8468 0.8468 0.0000  0.0000  0.0000  703  GLN A CB  
6533  C CG  . GLN D 706  ? 0.8468 0.8468 0.8468 0.0000  0.0000  0.0000  703  GLN A CG  
6534  C CD  . GLN D 706  ? 0.8468 0.8468 0.8468 0.0000  0.0000  0.0000  703  GLN A CD  
6535  O OE1 . GLN D 706  ? 0.8468 0.8468 0.8468 0.0000  0.0000  0.0000  703  GLN A OE1 
6536  N NE2 . GLN D 706  ? 0.8468 0.8468 0.8468 0.0000  0.0000  0.0000  703  GLN A NE2 
6537  N N   . TYR D 707  ? 0.8775 0.8775 0.8775 0.0000  0.0000  0.0000  704  TYR A N   
6538  C CA  . TYR D 707  ? 0.8775 0.8775 0.8775 0.0000  0.0000  0.0000  704  TYR A CA  
6539  C C   . TYR D 707  ? 0.8775 0.8775 0.8775 0.0000  0.0000  0.0000  704  TYR A C   
6540  O O   . TYR D 707  ? 0.8775 0.8775 0.8775 0.0000  0.0000  0.0000  704  TYR A O   
6541  C CB  . TYR D 707  ? 0.8775 0.8775 0.8775 0.0000  0.0000  0.0000  704  TYR A CB  
6542  C CG  . TYR D 707  ? 0.8775 0.8775 0.8775 0.0000  0.0000  0.0000  704  TYR A CG  
6543  C CD1 . TYR D 707  ? 0.8775 0.8775 0.8775 0.0000  0.0000  0.0000  704  TYR A CD1 
6544  C CD2 . TYR D 707  ? 0.8775 0.8775 0.8775 0.0000  0.0000  0.0000  704  TYR A CD2 
6545  C CE1 . TYR D 707  ? 0.8775 0.8775 0.8775 0.0000  0.0000  0.0000  704  TYR A CE1 
6546  C CE2 . TYR D 707  ? 0.8775 0.8775 0.8775 0.0000  0.0000  0.0000  704  TYR A CE2 
6547  C CZ  . TYR D 707  ? 0.8775 0.8775 0.8775 0.0000  0.0000  0.0000  704  TYR A CZ  
6548  O OH  . TYR D 707  ? 0.8775 0.8775 0.8775 0.0000  0.0000  0.0000  704  TYR A OH  
6549  N N   . LYS D 708  ? 0.9026 0.9026 0.9026 0.0000  0.0000  0.0000  705  LYS A N   
6550  C CA  . LYS D 708  ? 0.9026 0.9026 0.9026 0.0000  0.0000  0.0000  705  LYS A CA  
6551  C C   . LYS D 708  ? 0.9026 0.9026 0.9026 0.0000  0.0000  0.0000  705  LYS A C   
6552  O O   . LYS D 708  ? 0.9026 0.9026 0.9026 0.0000  0.0000  0.0000  705  LYS A O   
6553  C CB  . LYS D 708  ? 0.9026 0.9026 0.9026 0.0000  0.0000  0.0000  705  LYS A CB  
6554  C CG  . LYS D 708  ? 0.9026 0.9026 0.9026 0.0000  0.0000  0.0000  705  LYS A CG  
6555  C CD  . LYS D 708  ? 0.9026 0.9026 0.9026 0.0000  0.0000  0.0000  705  LYS A CD  
6556  C CE  . LYS D 708  ? 0.9026 0.9026 0.9026 0.0000  0.0000  0.0000  705  LYS A CE  
6557  N NZ  . LYS D 708  ? 0.9026 0.9026 0.9026 0.0000  0.0000  0.0000  705  LYS A NZ  
6558  N N   . ASP D 709  ? 0.8960 0.8960 0.8960 0.0000  0.0000  0.0000  706  ASP A N   
6559  C CA  . ASP D 709  ? 0.8960 0.8960 0.8960 0.0000  0.0000  0.0000  706  ASP A CA  
6560  C C   . ASP D 709  ? 0.8960 0.8960 0.8960 0.0000  0.0000  0.0000  706  ASP A C   
6561  O O   . ASP D 709  ? 0.8960 0.8960 0.8960 0.0000  0.0000  0.0000  706  ASP A O   
6562  C CB  . ASP D 709  ? 0.8960 0.8960 0.8960 0.0000  0.0000  0.0000  706  ASP A CB  
6563  C CG  . ASP D 709  ? 0.8960 0.8960 0.8960 0.0000  0.0000  0.0000  706  ASP A CG  
6564  O OD1 . ASP D 709  ? 0.8960 0.8960 0.8960 0.0000  0.0000  0.0000  706  ASP A OD1 
6565  O OD2 . ASP D 709  ? 0.8960 0.8960 0.8960 0.0000  0.0000  0.0000  706  ASP A OD2 
6566  N N   . LEU D 710  ? 0.8460 0.8460 0.8460 0.0000  0.0000  0.0000  707  LEU A N   
6567  C CA  . LEU D 710  ? 0.8460 0.8460 0.8460 0.0000  0.0000  0.0000  707  LEU A CA  
6568  C C   . LEU D 710  ? 0.8460 0.8460 0.8460 0.0000  0.0000  0.0000  707  LEU A C   
6569  O O   . LEU D 710  ? 0.8460 0.8460 0.8460 0.0000  0.0000  0.0000  707  LEU A O   
6570  C CB  . LEU D 710  ? 0.8460 0.8460 0.8460 0.0000  0.0000  0.0000  707  LEU A CB  
6571  C CG  . LEU D 710  ? 0.8460 0.8460 0.8460 0.0000  0.0000  0.0000  707  LEU A CG  
6572  C CD1 . LEU D 710  ? 0.8460 0.8460 0.8460 0.0000  0.0000  0.0000  707  LEU A CD1 
6573  C CD2 . LEU D 710  ? 0.8460 0.8460 0.8460 0.0000  0.0000  0.0000  707  LEU A CD2 
6574  N N   . GLY D 711  ? 0.8476 0.8476 0.8476 0.0000  0.0000  0.0000  708  GLY A N   
6575  C CA  . GLY D 711  ? 0.8476 0.8476 0.8476 0.0000  0.0000  0.0000  708  GLY A CA  
6576  C C   . GLY D 711  ? 0.8476 0.8476 0.8476 0.0000  0.0000  0.0000  708  GLY A C   
6577  O O   . GLY D 711  ? 0.8476 0.8476 0.8476 0.0000  0.0000  0.0000  708  GLY A O   
6578  N N   . GLU D 712  ? 0.8492 0.8492 0.8492 0.0000  0.0000  0.0000  709  GLU A N   
6579  C CA  . GLU D 712  ? 0.8492 0.8492 0.8492 0.0000  0.0000  0.0000  709  GLU A CA  
6580  C C   . GLU D 712  ? 0.8492 0.8492 0.8492 0.0000  0.0000  0.0000  709  GLU A C   
6581  O O   . GLU D 712  ? 0.8492 0.8492 0.8492 0.0000  0.0000  0.0000  709  GLU A O   
6582  C CB  . GLU D 712  ? 0.8492 0.8492 0.8492 0.0000  0.0000  0.0000  709  GLU A CB  
6583  C CG  . GLU D 712  ? 0.8492 0.8492 0.8492 0.0000  0.0000  0.0000  709  GLU A CG  
6584  C CD  . GLU D 712  ? 0.8492 0.8492 0.8492 0.0000  0.0000  0.0000  709  GLU A CD  
6585  O OE1 . GLU D 712  ? 0.8492 0.8492 0.8492 0.0000  0.0000  0.0000  709  GLU A OE1 
6586  O OE2 . GLU D 712  ? 0.8492 0.8492 0.8492 0.0000  0.0000  0.0000  709  GLU A OE2 
6587  N N   . TYR D 713  ? 0.7581 0.7581 0.7581 0.0000  0.0000  0.0000  710  TYR A N   
6588  C CA  . TYR D 713  ? 0.7581 0.7581 0.7581 0.0000  0.0000  0.0000  710  TYR A CA  
6589  C C   . TYR D 713  ? 0.7581 0.7581 0.7581 0.0000  0.0000  0.0000  710  TYR A C   
6590  O O   . TYR D 713  ? 0.7581 0.7581 0.7581 0.0000  0.0000  0.0000  710  TYR A O   
6591  C CB  . TYR D 713  ? 0.7581 0.7581 0.7581 0.0000  0.0000  0.0000  710  TYR A CB  
6592  C CG  . TYR D 713  ? 0.7581 0.7581 0.7581 0.0000  0.0000  0.0000  710  TYR A CG  
6593  C CD1 . TYR D 713  ? 0.7581 0.7581 0.7581 0.0000  0.0000  0.0000  710  TYR A CD1 
6594  C CD2 . TYR D 713  ? 0.7581 0.7581 0.7581 0.0000  0.0000  0.0000  710  TYR A CD2 
6595  C CE1 . TYR D 713  ? 0.7581 0.7581 0.7581 0.0000  0.0000  0.0000  710  TYR A CE1 
6596  C CE2 . TYR D 713  ? 0.7581 0.7581 0.7581 0.0000  0.0000  0.0000  710  TYR A CE2 
6597  C CZ  . TYR D 713  ? 0.7581 0.7581 0.7581 0.0000  0.0000  0.0000  710  TYR A CZ  
6598  O OH  . TYR D 713  ? 0.7581 0.7581 0.7581 0.0000  0.0000  0.0000  710  TYR A OH  
6599  N N   . TYR D 714  ? 0.6960 0.6960 0.6960 0.0000  0.0000  0.0000  711  TYR A N   
6600  C CA  . TYR D 714  ? 0.6960 0.6960 0.6960 0.0000  0.0000  0.0000  711  TYR A CA  
6601  C C   . TYR D 714  ? 0.6960 0.6960 0.6960 0.0000  0.0000  0.0000  711  TYR A C   
6602  O O   . TYR D 714  ? 0.6960 0.6960 0.6960 0.0000  0.0000  0.0000  711  TYR A O   
6603  C CB  . TYR D 714  ? 0.6960 0.6960 0.6960 0.0000  0.0000  0.0000  711  TYR A CB  
6604  C CG  . TYR D 714  ? 0.6960 0.6960 0.6960 0.0000  0.0000  0.0000  711  TYR A CG  
6605  C CD1 . TYR D 714  ? 0.6960 0.6960 0.6960 0.0000  0.0000  0.0000  711  TYR A CD1 
6606  C CD2 . TYR D 714  ? 0.6960 0.6960 0.6960 0.0000  0.0000  0.0000  711  TYR A CD2 
6607  C CE1 . TYR D 714  ? 0.6960 0.6960 0.6960 0.0000  0.0000  0.0000  711  TYR A CE1 
6608  C CE2 . TYR D 714  ? 0.6960 0.6960 0.6960 0.0000  0.0000  0.0000  711  TYR A CE2 
6609  C CZ  . TYR D 714  ? 0.6960 0.6960 0.6960 0.0000  0.0000  0.0000  711  TYR A CZ  
6610  O OH  . TYR D 714  ? 0.6960 0.6960 0.6960 0.0000  0.0000  0.0000  711  TYR A OH  
6611  N N   . ALA D 715  ? 0.7051 0.7051 0.7051 0.0000  0.0000  0.0000  712  ALA A N   
6612  C CA  . ALA D 715  ? 0.7051 0.7051 0.7051 0.0000  0.0000  0.0000  712  ALA A CA  
6613  C C   . ALA D 715  ? 0.7051 0.7051 0.7051 0.0000  0.0000  0.0000  712  ALA A C   
6614  O O   . ALA D 715  ? 0.7051 0.7051 0.7051 0.0000  0.0000  0.0000  712  ALA A O   
6615  C CB  . ALA D 715  ? 0.7051 0.7051 0.7051 0.0000  0.0000  0.0000  712  ALA A CB  
6616  N N   . GLU D 716  ? 0.7181 0.7181 0.7181 0.0000  0.0000  0.0000  713  GLU A N   
6617  C CA  . GLU D 716  ? 0.7181 0.7181 0.7181 0.0000  0.0000  0.0000  713  GLU A CA  
6618  C C   . GLU D 716  ? 0.7181 0.7181 0.7181 0.0000  0.0000  0.0000  713  GLU A C   
6619  O O   . GLU D 716  ? 0.7181 0.7181 0.7181 0.0000  0.0000  0.0000  713  GLU A O   
6620  C CB  . GLU D 716  ? 0.7181 0.7181 0.7181 0.0000  0.0000  0.0000  713  GLU A CB  
6621  C CG  . GLU D 716  ? 0.7181 0.7181 0.7181 0.0000  0.0000  0.0000  713  GLU A CG  
6622  C CD  . GLU D 716  ? 0.7181 0.7181 0.7181 0.0000  0.0000  0.0000  713  GLU A CD  
6623  O OE1 . GLU D 716  ? 0.7181 0.7181 0.7181 0.0000  0.0000  0.0000  713  GLU A OE1 
6624  O OE2 . GLU D 716  ? 0.7181 0.7181 0.7181 0.0000  0.0000  0.0000  713  GLU A OE2 
6625  N N   . LEU D 717  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  714  LEU A N   
6626  C CA  . LEU D 717  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  714  LEU A CA  
6627  C C   . LEU D 717  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  714  LEU A C   
6628  O O   . LEU D 717  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  714  LEU A O   
6629  C CB  . LEU D 717  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  714  LEU A CB  
6630  C CG  . LEU D 717  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  714  LEU A CG  
6631  C CD1 . LEU D 717  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  714  LEU A CD1 
6632  C CD2 . LEU D 717  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  714  LEU A CD2 
6633  N N   . ASN D 718  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  715  ASN A N   
6634  C CA  . ASN D 718  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  715  ASN A CA  
6635  C C   . ASN D 718  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  715  ASN A C   
6636  O O   . ASN D 718  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  715  ASN A O   
6637  C CB  . ASN D 718  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  715  ASN A CB  
6638  C CG  . ASN D 718  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  715  ASN A CG  
6639  O OD1 . ASN D 718  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  715  ASN A OD1 
6640  N ND2 . ASN D 718  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  715  ASN A ND2 
6641  N N   . PRO D 719  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  716  PRO A N   
6642  C CA  . PRO D 719  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  716  PRO A CA  
6643  C C   . PRO D 719  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  716  PRO A C   
6644  O O   . PRO D 719  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  716  PRO A O   
6645  C CB  . PRO D 719  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  716  PRO A CB  
6646  C CG  . PRO D 719  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  716  PRO A CG  
6647  C CD  . PRO D 719  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  716  PRO A CD  
6648  N N   . LEU D 720  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  717  LEU A N   
6649  C CA  . LEU D 720  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  717  LEU A CA  
6650  C C   . LEU D 720  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  717  LEU A C   
6651  O O   . LEU D 720  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  717  LEU A O   
6652  C CB  . LEU D 720  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  717  LEU A CB  
6653  C CG  . LEU D 720  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  717  LEU A CG  
6654  C CD1 . LEU D 720  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  717  LEU A CD1 
6655  C CD2 . LEU D 720  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  717  LEU A CD2 
6656  N N   . LEU D 721  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  718  LEU A N   
6657  C CA  . LEU D 721  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  718  LEU A CA  
6658  C C   . LEU D 721  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  718  LEU A C   
6659  O O   . LEU D 721  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  718  LEU A O   
6660  C CB  . LEU D 721  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  718  LEU A CB  
6661  C CG  . LEU D 721  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  718  LEU A CG  
6662  C CD1 . LEU D 721  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  718  LEU A CD1 
6663  C CD2 . LEU D 721  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  718  LEU A CD2 
6664  N N   . TYR D 722  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  719  TYR A N   
6665  C CA  . TYR D 722  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  719  TYR A CA  
6666  C C   . TYR D 722  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  719  TYR A C   
6667  O O   . TYR D 722  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  719  TYR A O   
6668  C CB  . TYR D 722  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  719  TYR A CB  
6669  C CG  . TYR D 722  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  719  TYR A CG  
6670  C CD1 . TYR D 722  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  719  TYR A CD1 
6671  C CD2 . TYR D 722  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  719  TYR A CD2 
6672  C CE1 . TYR D 722  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  719  TYR A CE1 
6673  C CE2 . TYR D 722  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  719  TYR A CE2 
6674  C CZ  . TYR D 722  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  719  TYR A CZ  
6675  O OH  . TYR D 722  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  719  TYR A OH  
6676  N N   . HIS D 723  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  720  HIS A N   
6677  C CA  . HIS D 723  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  720  HIS A CA  
6678  C C   . HIS D 723  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  720  HIS A C   
6679  O O   . HIS D 723  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  720  HIS A O   
6680  C CB  . HIS D 723  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  720  HIS A CB  
6681  C CG  . HIS D 723  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  720  HIS A CG  
6682  N ND1 . HIS D 723  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  720  HIS A ND1 
6683  C CD2 . HIS D 723  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  720  HIS A CD2 
6684  C CE1 . HIS D 723  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  720  HIS A CE1 
6685  N NE2 . HIS D 723  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  720  HIS A NE2 
6686  N N   . ILE D 724  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  721  ILE A N   
6687  C CA  . ILE D 724  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  721  ILE A CA  
6688  C C   . ILE D 724  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  721  ILE A C   
6689  O O   . ILE D 724  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  721  ILE A O   
6690  C CB  . ILE D 724  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  721  ILE A CB  
6691  C CG1 . ILE D 724  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  721  ILE A CG1 
6692  C CG2 . ILE D 724  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  721  ILE A CG2 
6693  C CD1 . ILE D 724  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  721  ILE A CD1 
6694  N N   . SER D 725  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  722  SER A N   
6695  C CA  . SER D 725  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  722  SER A CA  
6696  C C   . SER D 725  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  722  SER A C   
6697  O O   . SER D 725  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  722  SER A O   
6698  C CB  . SER D 725  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  722  SER A CB  
6699  O OG  . SER D 725  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  722  SER A OG  
6700  N N   . PHE D 726  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  723  PHE A N   
6701  C CA  . PHE D 726  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  723  PHE A CA  
6702  C C   . PHE D 726  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  723  PHE A C   
6703  O O   . PHE D 726  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  723  PHE A O   
6704  C CB  . PHE D 726  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  723  PHE A CB  
6705  C CG  . PHE D 726  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  723  PHE A CG  
6706  C CD1 . PHE D 726  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  723  PHE A CD1 
6707  C CD2 . PHE D 726  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  723  PHE A CD2 
6708  C CE1 . PHE D 726  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  723  PHE A CE1 
6709  C CE2 . PHE D 726  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  723  PHE A CE2 
6710  C CZ  . PHE D 726  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  723  PHE A CZ  
6711  N N   . GLN D 727  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  724  GLN A N   
6712  C CA  . GLN D 727  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  724  GLN A CA  
6713  C C   . GLN D 727  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  724  GLN A C   
6714  O O   . GLN D 727  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  724  GLN A O   
6715  C CB  . GLN D 727  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  724  GLN A CB  
6716  C CG  . GLN D 727  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  724  GLN A CG  
6717  C CD  . GLN D 727  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  724  GLN A CD  
6718  O OE1 . GLN D 727  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  724  GLN A OE1 
6719  N NE2 . GLN D 727  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  724  GLN A NE2 
6720  N N   . ARG D 728  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  725  ARG A N   
6721  C CA  . ARG D 728  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  725  ARG A CA  
6722  C C   . ARG D 728  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  725  ARG A C   
6723  O O   . ARG D 728  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  725  ARG A O   
6724  C CB  . ARG D 728  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  725  ARG A CB  
6725  C CG  . ARG D 728  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  725  ARG A CG  
6726  C CD  . ARG D 728  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  725  ARG A CD  
6727  N NE  . ARG D 728  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  725  ARG A NE  
6728  C CZ  . ARG D 728  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  725  ARG A CZ  
6729  N NH1 . ARG D 728  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  725  ARG A NH1 
6730  N NH2 . ARG D 728  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  725  ARG A NH2 
6731  N N   . ILE D 729  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  726  ILE A N   
6732  C CA  . ILE D 729  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  726  ILE A CA  
6733  C C   . ILE D 729  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  726  ILE A C   
6734  O O   . ILE D 729  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  726  ILE A O   
6735  C CB  . ILE D 729  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  726  ILE A CB  
6736  C CG1 . ILE D 729  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  726  ILE A CG1 
6737  C CG2 . ILE D 729  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  726  ILE A CG2 
6738  C CD1 . ILE D 729  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  726  ILE A CD1 
6739  N N   . ALA D 730  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  727  ALA A N   
6740  C CA  . ALA D 730  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  727  ALA A CA  
6741  C C   . ALA D 730  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  727  ALA A C   
6742  O O   . ALA D 730  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  727  ALA A O   
6743  C CB  . ALA D 730  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  727  ALA A CB  
6744  N N   . GLU D 731  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  728  GLU A N   
6745  C CA  . GLU D 731  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  728  GLU A CA  
6746  C C   . GLU D 731  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  728  GLU A C   
6747  O O   . GLU D 731  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  728  GLU A O   
6748  C CB  . GLU D 731  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  728  GLU A CB  
6749  C CG  . GLU D 731  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  728  GLU A CG  
6750  C CD  . GLU D 731  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  728  GLU A CD  
6751  O OE1 . GLU D 731  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  728  GLU A OE1 
6752  O OE2 . GLU D 731  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  728  GLU A OE2 
6753  N N   . LYS D 732  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  729  LYS A N   
6754  C CA  . LYS D 732  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  729  LYS A CA  
6755  C C   . LYS D 732  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  729  LYS A C   
6756  O O   . LYS D 732  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  729  LYS A O   
6762  N N   . GLU D 733  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  730  GLU A N   
6763  C CA  . GLU D 733  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  730  GLU A CA  
6764  C C   . GLU D 733  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  730  GLU A C   
6765  O O   . GLU D 733  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  730  GLU A O   
6766  C CB  . GLU D 733  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  730  GLU A CB  
6767  C CG  . GLU D 733  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  730  GLU A CG  
6768  C CD  . GLU D 733  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  730  GLU A CD  
6769  O OE1 . GLU D 733  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  730  GLU A OE1 
6770  O OE2 . GLU D 733  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  730  GLU A OE2 
6771  N N   . ILE D 734  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  731  ILE A N   
6772  C CA  . ILE D 734  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  731  ILE A CA  
6773  C C   . ILE D 734  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  731  ILE A C   
6774  O O   . ILE D 734  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  731  ILE A O   
6775  C CB  . ILE D 734  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  731  ILE A CB  
6776  C CG1 . ILE D 734  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  731  ILE A CG1 
6777  C CG2 . ILE D 734  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  731  ILE A CG2 
6778  C CD1 . ILE D 734  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  731  ILE A CD1 
6779  N N   . MET D 735  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  732  MET A N   
6780  C CA  . MET D 735  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  732  MET A CA  
6781  C C   . MET D 735  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  732  MET A C   
6782  O O   . MET D 735  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  732  MET A O   
6783  C CB  . MET D 735  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  732  MET A CB  
6784  C CG  . MET D 735  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  732  MET A CG  
6785  S SD  . MET D 735  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  732  MET A SD  
6786  C CE  . MET D 735  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  732  MET A CE  
6787  N N   . ASP D 736  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  733  ASP A N   
6788  C CA  . ASP D 736  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  733  ASP A CA  
6789  C C   . ASP D 736  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  733  ASP A C   
6790  O O   . ASP D 736  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  733  ASP A O   
6791  C CB  . ASP D 736  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  733  ASP A CB  
6792  C CG  . ASP D 736  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  733  ASP A CG  
6793  O OD1 . ASP D 736  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  733  ASP A OD1 
6794  O OD2 . ASP D 736  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  733  ASP A OD2 
6795  N N   . ALA D 737  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  734  ALA A N   
6796  C CA  . ALA D 737  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  734  ALA A CA  
6797  C C   . ALA D 737  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  734  ALA A C   
6798  O O   . ALA D 737  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  734  ALA A O   
6799  C CB  . ALA D 737  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  734  ALA A CB  
6800  N N   . VAL D 738  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  735  VAL A N   
6801  C CA  . VAL D 738  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  735  VAL A CA  
6802  C C   . VAL D 738  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  735  VAL A C   
6803  O O   . VAL D 738  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  735  VAL A O   
6804  C CB  . VAL D 738  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  735  VAL A CB  
6805  C CG1 . VAL D 738  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  735  VAL A CG1 
6806  C CG2 . VAL D 738  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  735  VAL A CG2 
6807  N N   . GLU D 739  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  736  GLU A N   
6808  C CA  . GLU D 739  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  736  GLU A CA  
6809  C C   . GLU D 739  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  736  GLU A C   
6810  O O   . GLU D 739  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  736  GLU A O   
6811  C CB  . GLU D 739  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  736  GLU A CB  
6812  C CG  . GLU D 739  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  736  GLU A CG  
6813  C CD  . GLU D 739  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  736  GLU A CD  
6814  O OE1 . GLU D 739  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  736  GLU A OE1 
6815  O OE2 . GLU D 739  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  736  GLU A OE2 
6816  N N   . THR D 740  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  737  THR A N   
6817  C CA  . THR D 740  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  737  THR A CA  
6818  C C   . THR D 740  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  737  THR A C   
6819  O O   . THR D 740  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  737  THR A O   
6820  C CB  . THR D 740  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  737  THR A CB  
6821  O OG1 . THR D 740  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  737  THR A OG1 
6822  C CG2 . THR D 740  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  737  THR A CG2 
6823  N N   . GLY D 741  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  738  GLY A N   
6824  C CA  . GLY D 741  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  738  GLY A CA  
6825  C C   . GLY D 741  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  738  GLY A C   
6826  O O   . GLY D 741  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  738  GLY A O   
6827  N N   . LYS D 742  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  739  LYS A N   
6828  C CA  . LYS D 742  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  739  LYS A CA  
6829  C C   . LYS D 742  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  739  LYS A C   
6830  O O   . LYS D 742  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  739  LYS A O   
6836  N N   . LEU D 743  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  740  LEU A N   
6837  C CA  . LEU D 743  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  740  LEU A CA  
6838  C C   . LEU D 743  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  740  LEU A C   
6839  O O   . LEU D 743  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  740  LEU A O   
6840  C CB  . LEU D 743  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  740  LEU A CB  
6841  C CG  . LEU D 743  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  740  LEU A CG  
6842  C CD1 . LEU D 743  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  740  LEU A CD1 
6843  C CD2 . LEU D 743  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  740  LEU A CD2 
6844  N N   . TYR D 744  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  741  TYR A N   
6845  C CA  . TYR D 744  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  741  TYR A CA  
6846  C C   . TYR D 744  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  741  TYR A C   
6847  O O   . TYR D 744  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  741  TYR A O   
6848  C CB  . TYR D 744  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  741  TYR A CB  
6849  C CG  . TYR D 744  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  741  TYR A CG  
6850  C CD1 . TYR D 744  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  741  TYR A CD1 
6851  C CD2 . TYR D 744  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  741  TYR A CD2 
6852  C CE1 . TYR D 744  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  741  TYR A CE1 
6853  C CE2 . TYR D 744  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  741  TYR A CE2 
6854  C CZ  . TYR D 744  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  741  TYR A CZ  
6855  O OH  . TYR D 744  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  741  TYR A OH  
6856  N N   . LEU D 745  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  742  LEU A N   
6857  C CA  . LEU D 745  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  742  LEU A CA  
6858  C C   . LEU D 745  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  742  LEU A C   
6859  O O   . LEU D 745  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  742  LEU A O   
6860  C CB  . LEU D 745  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  742  LEU A CB  
6861  C CG  . LEU D 745  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  742  LEU A CG  
6862  C CD1 . LEU D 745  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  742  LEU A CD1 
6863  C CD2 . LEU D 745  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  742  LEU A CD2 
6864  N N   . PHE D 746  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  743  PHE A N   
6865  C CA  . PHE D 746  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  743  PHE A CA  
6866  C C   . PHE D 746  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  743  PHE A C   
6867  O O   . PHE D 746  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  743  PHE A O   
6868  C CB  . PHE D 746  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  743  PHE A CB  
6869  C CG  . PHE D 746  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  743  PHE A CG  
6870  C CD1 . PHE D 746  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  743  PHE A CD1 
6871  C CD2 . PHE D 746  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  743  PHE A CD2 
6872  C CE1 . PHE D 746  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  743  PHE A CE1 
6873  C CE2 . PHE D 746  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  743  PHE A CE2 
6874  C CZ  . PHE D 746  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  743  PHE A CZ  
6875  N N   . GLN D 747  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  744  GLN A N   
6876  C CA  . GLN D 747  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  744  GLN A CA  
6877  C C   . GLN D 747  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  744  GLN A C   
6878  O O   . GLN D 747  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  744  GLN A O   
6879  C CB  . GLN D 747  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  744  GLN A CB  
6880  C CG  . GLN D 747  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  744  GLN A CG  
6881  C CD  . GLN D 747  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  744  GLN A CD  
6882  O OE1 . GLN D 747  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  744  GLN A OE1 
6883  N NE2 . GLN D 747  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  744  GLN A NE2 
6884  N N   . ILE D 748  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  745  ILE A N   
6885  C CA  . ILE D 748  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  745  ILE A CA  
6886  C C   . ILE D 748  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  745  ILE A C   
6887  O O   . ILE D 748  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  745  ILE A O   
6888  C CB  . ILE D 748  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  745  ILE A CB  
6889  C CG1 . ILE D 748  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  745  ILE A CG1 
6890  C CG2 . ILE D 748  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  745  ILE A CG2 
6891  C CD1 . ILE D 748  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  745  ILE A CD1 
6892  N N   . TYR D 749  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  746  TYR A N   
6893  C CA  . TYR D 749  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  746  TYR A CA  
6894  C C   . TYR D 749  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  746  TYR A C   
6895  O O   . TYR D 749  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  746  TYR A O   
6896  C CB  . TYR D 749  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  746  TYR A CB  
6897  C CG  . TYR D 749  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  746  TYR A CG  
6898  C CD1 . TYR D 749  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  746  TYR A CD1 
6899  C CD2 . TYR D 749  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  746  TYR A CD2 
6900  C CE1 . TYR D 749  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  746  TYR A CE1 
6901  C CE2 . TYR D 749  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  746  TYR A CE2 
6902  C CZ  . TYR D 749  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  746  TYR A CZ  
6903  O OH  . TYR D 749  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  746  TYR A OH  
6904  N N   . ASN D 750  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  747  ASN A N   
6905  C CA  . ASN D 750  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  747  ASN A CA  
6906  C C   . ASN D 750  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  747  ASN A C   
6907  O O   . ASN D 750  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  747  ASN A O   
6908  C CB  . ASN D 750  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  747  ASN A CB  
6909  C CG  . ASN D 750  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  747  ASN A CG  
6910  O OD1 . ASN D 750  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  747  ASN A OD1 
6911  N ND2 . ASN D 750  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  747  ASN A ND2 
6912  N N   . LYS D 751  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  748  LYS A N   
6913  C CA  . LYS D 751  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  748  LYS A CA  
6914  C C   . LYS D 751  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  748  LYS A C   
6915  O O   . LYS D 751  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  748  LYS A O   
6921  N N   . ASP D 752  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  749  ASP A N   
6922  C CA  . ASP D 752  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  749  ASP A CA  
6923  C C   . ASP D 752  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  749  ASP A C   
6924  O O   . ASP D 752  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  749  ASP A O   
6925  C CB  . ASP D 752  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  749  ASP A CB  
6926  C CG  . ASP D 752  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  749  ASP A CG  
6927  O OD1 . ASP D 752  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  749  ASP A OD1 
6928  O OD2 . ASP D 752  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  749  ASP A OD2 
6929  N N   . PHE D 753  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  750  PHE A N   
6930  C CA  . PHE D 753  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  750  PHE A CA  
6931  C C   . PHE D 753  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  750  PHE A C   
6932  O O   . PHE D 753  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  750  PHE A O   
6933  C CB  . PHE D 753  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  750  PHE A CB  
6934  C CG  . PHE D 753  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  750  PHE A CG  
6935  C CD1 . PHE D 753  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  750  PHE A CD1 
6936  C CD2 . PHE D 753  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  750  PHE A CD2 
6937  C CE1 . PHE D 753  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  750  PHE A CE1 
6938  C CE2 . PHE D 753  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  750  PHE A CE2 
6939  C CZ  . PHE D 753  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  750  PHE A CZ  
6940  N N   . ALA D 754  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  751  ALA A N   
6941  C CA  . ALA D 754  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  751  ALA A CA  
6942  C C   . ALA D 754  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  751  ALA A C   
6943  O O   . ALA D 754  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  751  ALA A O   
6944  C CB  . ALA D 754  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  751  ALA A CB  
6945  N N   . LYS D 755  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  752  LYS A N   
6946  C CA  . LYS D 755  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  752  LYS A CA  
6947  C C   . LYS D 755  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  752  LYS A C   
6948  O O   . LYS D 755  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  752  LYS A O   
6954  N N   . GLY D 756  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  753  GLY A N   
6955  C CA  . GLY D 756  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  753  GLY A CA  
6956  C C   . GLY D 756  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  753  GLY A C   
6957  O O   . GLY D 756  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  753  GLY A O   
6958  N N   . HIS D 757  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  754  HIS A N   
6959  C CA  . HIS D 757  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  754  HIS A CA  
6960  C C   . HIS D 757  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  754  HIS A C   
6961  O O   . HIS D 757  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  754  HIS A O   
6962  C CB  . HIS D 757  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  754  HIS A CB  
6963  C CG  . HIS D 757  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  754  HIS A CG  
6964  N ND1 . HIS D 757  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  754  HIS A ND1 
6965  C CD2 . HIS D 757  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  754  HIS A CD2 
6966  C CE1 . HIS D 757  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  754  HIS A CE1 
6967  N NE2 . HIS D 757  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  754  HIS A NE2 
6968  N N   . HIS D 758  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  755  HIS A N   
6969  C CA  . HIS D 758  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  755  HIS A CA  
6970  C C   . HIS D 758  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  755  HIS A C   
6971  O O   . HIS D 758  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  755  HIS A O   
6972  C CB  . HIS D 758  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  755  HIS A CB  
6973  C CG  . HIS D 758  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  755  HIS A CG  
6974  N ND1 . HIS D 758  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  755  HIS A ND1 
6975  C CD2 . HIS D 758  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  755  HIS A CD2 
6976  C CE1 . HIS D 758  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  755  HIS A CE1 
6977  N NE2 . HIS D 758  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  755  HIS A NE2 
6978  N N   . GLY D 759  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  756  GLY A N   
6979  C CA  . GLY D 759  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  756  GLY A CA  
6980  C C   . GLY D 759  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  756  GLY A C   
6981  O O   . GLY D 759  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  756  GLY A O   
6982  N N   . LYS D 760  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  757  LYS A N   
6983  C CA  . LYS D 760  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  757  LYS A CA  
6984  C C   . LYS D 760  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  757  LYS A C   
6985  O O   . LYS D 760  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  757  LYS A O   
6986  C CB  . LYS D 760  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  757  LYS A CB  
6987  C CG  . LYS D 760  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  757  LYS A CG  
6988  C CD  . LYS D 760  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  757  LYS A CD  
6989  C CE  . LYS D 760  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  757  LYS A CE  
6990  N NZ  . LYS D 760  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  757  LYS A NZ  
6991  N N   . PRO D 761  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  758  PRO A N   
6992  C CA  . PRO D 761  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  758  PRO A CA  
6993  C C   . PRO D 761  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  758  PRO A C   
6994  O O   . PRO D 761  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  758  PRO A O   
6995  C CB  . PRO D 761  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  758  PRO A CB  
6996  C CG  . PRO D 761  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  758  PRO A CG  
6997  C CD  . PRO D 761  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  758  PRO A CD  
6998  N N   . ASN D 762  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  759  ASN A N   
6999  C CA  . ASN D 762  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  759  ASN A CA  
7000  C C   . ASN D 762  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  759  ASN A C   
7001  O O   . ASN D 762  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  759  ASN A O   
7002  C CB  . ASN D 762  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  759  ASN A CB  
7003  C CG  . ASN D 762  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  759  ASN A CG  
7004  O OD1 . ASN D 762  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  759  ASN A OD1 
7005  N ND2 . ASN D 762  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  759  ASN A ND2 
7006  N N   . LEU D 763  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  760  LEU A N   
7007  C CA  . LEU D 763  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  760  LEU A CA  
7008  C C   . LEU D 763  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  760  LEU A C   
7009  O O   . LEU D 763  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  760  LEU A O   
7010  C CB  . LEU D 763  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  760  LEU A CB  
7011  C CG  . LEU D 763  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  760  LEU A CG  
7012  C CD1 . LEU D 763  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  760  LEU A CD1 
7013  C CD2 . LEU D 763  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  760  LEU A CD2 
7014  N N   . HIS D 764  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  761  HIS A N   
7015  C CA  . HIS D 764  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  761  HIS A CA  
7016  C C   . HIS D 764  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  761  HIS A C   
7017  O O   . HIS D 764  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  761  HIS A O   
7018  C CB  . HIS D 764  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  761  HIS A CB  
7019  C CG  . HIS D 764  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  761  HIS A CG  
7020  N ND1 . HIS D 764  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  761  HIS A ND1 
7021  C CD2 . HIS D 764  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  761  HIS A CD2 
7022  C CE1 . HIS D 764  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  761  HIS A CE1 
7023  N NE2 . HIS D 764  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  761  HIS A NE2 
7024  N N   . THR D 765  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  762  THR A N   
7025  C CA  . THR D 765  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  762  THR A CA  
7026  C C   . THR D 765  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  762  THR A C   
7027  O O   . THR D 765  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  762  THR A O   
7028  C CB  . THR D 765  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  762  THR A CB  
7029  O OG1 . THR D 765  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  762  THR A OG1 
7030  C CG2 . THR D 765  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  762  THR A CG2 
7031  N N   . LEU D 766  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  763  LEU A N   
7032  C CA  . LEU D 766  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  763  LEU A CA  
7033  C C   . LEU D 766  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  763  LEU A C   
7034  O O   . LEU D 766  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  763  LEU A O   
7035  C CB  . LEU D 766  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  763  LEU A CB  
7036  C CG  . LEU D 766  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  763  LEU A CG  
7037  C CD1 . LEU D 766  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  763  LEU A CD1 
7038  C CD2 . LEU D 766  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  763  LEU A CD2 
7039  N N   . TYR D 767  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  764  TYR A N   
7040  C CA  . TYR D 767  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  764  TYR A CA  
7041  C C   . TYR D 767  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  764  TYR A C   
7042  O O   . TYR D 767  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  764  TYR A O   
7043  C CB  . TYR D 767  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  764  TYR A CB  
7044  C CG  . TYR D 767  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  764  TYR A CG  
7045  C CD1 . TYR D 767  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  764  TYR A CD1 
7046  C CD2 . TYR D 767  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  764  TYR A CD2 
7047  C CE1 . TYR D 767  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  764  TYR A CE1 
7048  C CE2 . TYR D 767  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  764  TYR A CE2 
7049  C CZ  . TYR D 767  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  764  TYR A CZ  
7050  O OH  . TYR D 767  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  764  TYR A OH  
7051  N N   . TRP D 768  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  765  TRP A N   
7052  C CA  . TRP D 768  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  765  TRP A CA  
7053  C C   . TRP D 768  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  765  TRP A C   
7054  O O   . TRP D 768  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  765  TRP A O   
7055  C CB  . TRP D 768  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  765  TRP A CB  
7056  C CG  . TRP D 768  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  765  TRP A CG  
7057  C CD1 . TRP D 768  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  765  TRP A CD1 
7058  C CD2 . TRP D 768  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  765  TRP A CD2 
7059  N NE1 . TRP D 768  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  765  TRP A NE1 
7060  C CE2 . TRP D 768  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  765  TRP A CE2 
7061  C CE3 . TRP D 768  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  765  TRP A CE3 
7062  C CZ2 . TRP D 768  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  765  TRP A CZ2 
7063  C CZ3 . TRP D 768  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  765  TRP A CZ3 
7064  C CH2 . TRP D 768  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  765  TRP A CH2 
7065  N N   . THR D 769  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  766  THR A N   
7066  C CA  . THR D 769  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  766  THR A CA  
7067  C C   . THR D 769  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  766  THR A C   
7068  O O   . THR D 769  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  766  THR A O   
7069  C CB  . THR D 769  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  766  THR A CB  
7070  O OG1 . THR D 769  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  766  THR A OG1 
7071  C CG2 . THR D 769  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  766  THR A CG2 
7072  N N   . GLY D 770  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  767  GLY A N   
7073  C CA  . GLY D 770  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  767  GLY A CA  
7074  C C   . GLY D 770  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  767  GLY A C   
7075  O O   . GLY D 770  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  767  GLY A O   
7076  N N   . LEU D 771  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  768  LEU A N   
7077  C CA  . LEU D 771  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  768  LEU A CA  
7078  C C   . LEU D 771  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  768  LEU A C   
7079  O O   . LEU D 771  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  768  LEU A O   
7080  C CB  . LEU D 771  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  768  LEU A CB  
7081  C CG  . LEU D 771  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  768  LEU A CG  
7082  C CD1 . LEU D 771  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  768  LEU A CD1 
7083  C CD2 . LEU D 771  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  768  LEU A CD2 
7084  N N   . PHE D 772  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  769  PHE A N   
7085  C CA  . PHE D 772  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  769  PHE A CA  
7086  C C   . PHE D 772  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  769  PHE A C   
7087  O O   . PHE D 772  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  769  PHE A O   
7088  C CB  . PHE D 772  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  769  PHE A CB  
7089  C CG  . PHE D 772  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  769  PHE A CG  
7090  C CD1 . PHE D 772  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  769  PHE A CD1 
7091  C CD2 . PHE D 772  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  769  PHE A CD2 
7092  C CE1 . PHE D 772  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  769  PHE A CE1 
7093  C CE2 . PHE D 772  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  769  PHE A CE2 
7094  C CZ  . PHE D 772  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  769  PHE A CZ  
7095  N N   . SER D 773  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  770  SER A N   
7096  C CA  . SER D 773  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  770  SER A CA  
7097  C C   . SER D 773  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  770  SER A C   
7098  O O   . SER D 773  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  770  SER A O   
7099  C CB  . SER D 773  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  770  SER A CB  
7100  O OG  . SER D 773  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  770  SER A OG  
7101  N N   . PRO D 774  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  771  PRO A N   
7102  C CA  . PRO D 774  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  771  PRO A CA  
7103  C C   . PRO D 774  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  771  PRO A C   
7104  O O   . PRO D 774  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  771  PRO A O   
7105  C CB  . PRO D 774  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  771  PRO A CB  
7106  C CG  . PRO D 774  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  771  PRO A CG  
7107  C CD  . PRO D 774  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  771  PRO A CD  
7108  N N   . GLU D 775  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  772  GLU A N   
7109  C CA  . GLU D 775  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  772  GLU A CA  
7110  C C   . GLU D 775  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  772  GLU A C   
7111  O O   . GLU D 775  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  772  GLU A O   
7112  C CB  . GLU D 775  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  772  GLU A CB  
7113  C CG  . GLU D 775  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  772  GLU A CG  
7114  C CD  . GLU D 775  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  772  GLU A CD  
7115  O OE1 . GLU D 775  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  772  GLU A OE1 
7116  O OE2 . GLU D 775  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  772  GLU A OE2 
7117  N N   . ASN D 776  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  773  ASN A N   
7118  C CA  . ASN D 776  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  773  ASN A CA  
7119  C C   . ASN D 776  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  773  ASN A C   
7120  O O   . ASN D 776  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  773  ASN A O   
7121  C CB  . ASN D 776  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  773  ASN A CB  
7122  C CG  . ASN D 776  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  773  ASN A CG  
7123  O OD1 . ASN D 776  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  773  ASN A OD1 
7124  N ND2 . ASN D 776  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  773  ASN A ND2 
7125  N N   . LEU D 777  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  774  LEU A N   
7126  C CA  . LEU D 777  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  774  LEU A CA  
7127  C C   . LEU D 777  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  774  LEU A C   
7128  O O   . LEU D 777  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  774  LEU A O   
7129  C CB  . LEU D 777  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  774  LEU A CB  
7130  C CG  . LEU D 777  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  774  LEU A CG  
7131  C CD1 . LEU D 777  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  774  LEU A CD1 
7132  C CD2 . LEU D 777  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  774  LEU A CD2 
7133  N N   . ALA D 778  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  775  ALA A N   
7134  C CA  . ALA D 778  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  775  ALA A CA  
7135  C C   . ALA D 778  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  775  ALA A C   
7136  O O   . ALA D 778  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  775  ALA A O   
7137  C CB  . ALA D 778  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  775  ALA A CB  
7138  N N   . LYS D 779  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  776  LYS A N   
7139  C CA  . LYS D 779  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  776  LYS A CA  
7140  C C   . LYS D 779  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  776  LYS A C   
7141  O O   . LYS D 779  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  776  LYS A O   
7142  C CB  . LYS D 779  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  776  LYS A CB  
7143  C CG  . LYS D 779  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  776  LYS A CG  
7144  C CD  . LYS D 779  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  776  LYS A CD  
7145  C CE  . LYS D 779  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  776  LYS A CE  
7146  N NZ  . LYS D 779  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  776  LYS A NZ  
7147  N N   . THR D 780  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  777  THR A N   
7148  C CA  . THR D 780  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  777  THR A CA  
7149  C C   . THR D 780  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  777  THR A C   
7150  O O   . THR D 780  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  777  THR A O   
7151  C CB  . THR D 780  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  777  THR A CB  
7152  O OG1 . THR D 780  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  777  THR A OG1 
7153  C CG2 . THR D 780  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  777  THR A CG2 
7154  N N   . SER D 781  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  778  SER A N   
7155  C CA  . SER D 781  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  778  SER A CA  
7156  C C   . SER D 781  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  778  SER A C   
7157  O O   . SER D 781  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  778  SER A O   
7158  C CB  . SER D 781  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  778  SER A CB  
7159  O OG  . SER D 781  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  778  SER A OG  
7160  N N   . ILE D 782  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  779  ILE A N   
7161  C CA  . ILE D 782  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  779  ILE A CA  
7162  C C   . ILE D 782  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  779  ILE A C   
7163  O O   . ILE D 782  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  779  ILE A O   
7164  C CB  . ILE D 782  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  779  ILE A CB  
7165  C CG1 . ILE D 782  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  779  ILE A CG1 
7166  C CG2 . ILE D 782  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  779  ILE A CG2 
7167  C CD1 . ILE D 782  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  779  ILE A CD1 
7168  N N   . LYS D 783  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  780  LYS A N   
7169  C CA  . LYS D 783  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  780  LYS A CA  
7170  C C   . LYS D 783  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  780  LYS A C   
7171  O O   . LYS D 783  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  780  LYS A O   
7172  C CB  . LYS D 783  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  780  LYS A CB  
7173  C CG  . LYS D 783  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  780  LYS A CG  
7174  C CD  . LYS D 783  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  780  LYS A CD  
7175  C CE  . LYS D 783  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  780  LYS A CE  
7176  N NZ  . LYS D 783  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  780  LYS A NZ  
7177  N N   . LEU D 784  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  781  LEU A N   
7178  C CA  . LEU D 784  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  781  LEU A CA  
7179  C C   . LEU D 784  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  781  LEU A C   
7180  O O   . LEU D 784  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  781  LEU A O   
7181  C CB  . LEU D 784  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  781  LEU A CB  
7182  C CG  . LEU D 784  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  781  LEU A CG  
7183  C CD1 . LEU D 784  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  781  LEU A CD1 
7184  C CD2 . LEU D 784  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  781  LEU A CD2 
7185  N N   . ASN D 785  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  782  ASN A N   
7186  C CA  . ASN D 785  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  782  ASN A CA  
7187  C C   . ASN D 785  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  782  ASN A C   
7188  O O   . ASN D 785  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  782  ASN A O   
7189  C CB  . ASN D 785  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  782  ASN A CB  
7190  C CG  . ASN D 785  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  782  ASN A CG  
7191  O OD1 . ASN D 785  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  782  ASN A OD1 
7192  N ND2 . ASN D 785  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  782  ASN A ND2 
7193  N N   . GLY D 786  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  783  GLY A N   
7194  C CA  . GLY D 786  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  783  GLY A CA  
7195  C C   . GLY D 786  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  783  GLY A C   
7196  O O   . GLY D 786  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  783  GLY A O   
7197  N N   . GLN D 787  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  784  GLN A N   
7198  C CA  . GLN D 787  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  784  GLN A CA  
7199  C C   . GLN D 787  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  784  GLN A C   
7200  O O   . GLN D 787  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  784  GLN A O   
7201  C CB  . GLN D 787  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  784  GLN A CB  
7202  C CG  . GLN D 787  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  784  GLN A CG  
7203  C CD  . GLN D 787  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  784  GLN A CD  
7204  O OE1 . GLN D 787  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  784  GLN A OE1 
7205  N NE2 . GLN D 787  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  784  GLN A NE2 
7206  N N   . ALA D 788  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  785  ALA A N   
7207  C CA  . ALA D 788  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  785  ALA A CA  
7208  C C   . ALA D 788  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  785  ALA A C   
7209  O O   . ALA D 788  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  785  ALA A O   
7210  C CB  . ALA D 788  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  785  ALA A CB  
7211  N N   . GLU D 789  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  786  GLU A N   
7212  C CA  . GLU D 789  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  786  GLU A CA  
7213  C C   . GLU D 789  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  786  GLU A C   
7214  O O   . GLU D 789  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  786  GLU A O   
7215  C CB  . GLU D 789  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  786  GLU A CB  
7216  C CG  . GLU D 789  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  786  GLU A CG  
7217  C CD  . GLU D 789  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  786  GLU A CD  
7218  O OE1 . GLU D 789  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  786  GLU A OE1 
7219  O OE2 . GLU D 789  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  786  GLU A OE2 
7220  N N   . LEU D 790  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  787  LEU A N   
7221  C CA  . LEU D 790  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  787  LEU A CA  
7222  C C   . LEU D 790  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  787  LEU A C   
7223  O O   . LEU D 790  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  787  LEU A O   
7224  C CB  . LEU D 790  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  787  LEU A CB  
7225  C CG  . LEU D 790  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  787  LEU A CG  
7226  C CD1 . LEU D 790  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  787  LEU A CD1 
7227  C CD2 . LEU D 790  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  787  LEU A CD2 
7228  N N   . PHE D 791  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  788  PHE A N   
7229  C CA  . PHE D 791  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  788  PHE A CA  
7230  C C   . PHE D 791  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  788  PHE A C   
7231  O O   . PHE D 791  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  788  PHE A O   
7232  C CB  . PHE D 791  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  788  PHE A CB  
7233  C CG  . PHE D 791  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  788  PHE A CG  
7234  C CD1 . PHE D 791  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  788  PHE A CD1 
7235  C CD2 . PHE D 791  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  788  PHE A CD2 
7236  C CE1 . PHE D 791  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  788  PHE A CE1 
7237  C CE2 . PHE D 791  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  788  PHE A CE2 
7238  C CZ  . PHE D 791  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  788  PHE A CZ  
7239  N N   . TYR D 792  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  789  TYR A N   
7240  C CA  . TYR D 792  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  789  TYR A CA  
7241  C C   . TYR D 792  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  789  TYR A C   
7242  O O   . TYR D 792  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  789  TYR A O   
7243  C CB  . TYR D 792  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  789  TYR A CB  
7244  C CG  . TYR D 792  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  789  TYR A CG  
7245  C CD1 . TYR D 792  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  789  TYR A CD1 
7246  C CD2 . TYR D 792  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  789  TYR A CD2 
7247  C CE1 . TYR D 792  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  789  TYR A CE1 
7248  C CE2 . TYR D 792  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  789  TYR A CE2 
7249  C CZ  . TYR D 792  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  789  TYR A CZ  
7250  O OH  . TYR D 792  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  789  TYR A OH  
7251  N N   . ARG D 793  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  790  ARG A N   
7252  C CA  . ARG D 793  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  790  ARG A CA  
7253  C C   . ARG D 793  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  790  ARG A C   
7254  O O   . ARG D 793  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  790  ARG A O   
7255  C CB  . ARG D 793  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  790  ARG A CB  
7256  C CG  . ARG D 793  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  790  ARG A CG  
7257  C CD  . ARG D 793  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  790  ARG A CD  
7258  N NE  . ARG D 793  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  790  ARG A NE  
7259  C CZ  . ARG D 793  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  790  ARG A CZ  
7260  N NH1 . ARG D 793  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  790  ARG A NH1 
7261  N NH2 . ARG D 793  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  790  ARG A NH2 
7262  N N   . PRO D 794  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  791  PRO A N   
7263  C CA  . PRO D 794  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  791  PRO A CA  
7264  C C   . PRO D 794  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  791  PRO A C   
7265  O O   . PRO D 794  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  791  PRO A O   
7266  C CB  . PRO D 794  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  791  PRO A CB  
7267  C CG  . PRO D 794  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  791  PRO A CG  
7268  C CD  . PRO D 794  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  791  PRO A CD  
7269  N N   . LYS D 795  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  792  LYS A N   
7270  C CA  . LYS D 795  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  792  LYS A CA  
7271  C C   . LYS D 795  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  792  LYS A C   
7272  O O   . LYS D 795  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  792  LYS A O   
7278  N N   . SER D 796  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  793  SER A N   
7279  C CA  . SER D 796  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  793  SER A CA  
7280  C C   . SER D 796  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  793  SER A C   
7281  O O   . SER D 796  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  793  SER A O   
7282  C CB  . SER D 796  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  793  SER A CB  
7283  O OG  . SER D 796  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  793  SER A OG  
7284  N N   . ARG D 797  ? 0.8046 0.8046 0.8046 0.0000  0.0000  0.0000  794  ARG A N   
7285  C CA  . ARG D 797  ? 0.8046 0.8046 0.8046 0.0000  0.0000  0.0000  794  ARG A CA  
7286  C C   . ARG D 797  ? 0.8046 0.8046 0.8046 0.0000  0.0000  0.0000  794  ARG A C   
7287  O O   . ARG D 797  ? 0.8046 0.8046 0.8046 0.0000  0.0000  0.0000  794  ARG A O   
7288  C CB  . ARG D 797  ? 0.8046 0.8046 0.8046 0.0000  0.0000  0.0000  794  ARG A CB  
7289  C CG  . ARG D 797  ? 0.8046 0.8046 0.8046 0.0000  0.0000  0.0000  794  ARG A CG  
7290  C CD  . ARG D 797  ? 0.8046 0.8046 0.8046 0.0000  0.0000  0.0000  794  ARG A CD  
7291  N NE  . ARG D 797  ? 0.8046 0.8046 0.8046 0.0000  0.0000  0.0000  794  ARG A NE  
7292  C CZ  . ARG D 797  ? 0.8046 0.8046 0.8046 0.0000  0.0000  0.0000  794  ARG A CZ  
7293  N NH1 . ARG D 797  ? 0.8046 0.8046 0.8046 0.0000  0.0000  0.0000  794  ARG A NH1 
7294  N NH2 . ARG D 797  ? 0.8046 0.8046 0.8046 0.0000  0.0000  0.0000  794  ARG A NH2 
7295  N N   . MET D 798  ? 0.9465 0.9465 0.9465 0.0000  0.0000  0.0000  795  MET A N   
7296  C CA  . MET D 798  ? 0.9465 0.9465 0.9465 0.0000  0.0000  0.0000  795  MET A CA  
7297  C C   . MET D 798  ? 0.9465 0.9465 0.9465 0.0000  0.0000  0.0000  795  MET A C   
7298  O O   . MET D 798  ? 0.9465 0.9465 0.9465 0.0000  0.0000  0.0000  795  MET A O   
7299  C CB  . MET D 798  ? 0.9465 0.9465 0.9465 0.0000  0.0000  0.0000  795  MET A CB  
7300  C CG  . MET D 798  ? 0.9465 0.9465 0.9465 0.0000  0.0000  0.0000  795  MET A CG  
7301  S SD  . MET D 798  ? 0.9465 0.9465 0.9465 0.0000  0.0000  0.0000  795  MET A SD  
7302  C CE  . MET D 798  ? 0.9465 0.9465 0.9465 0.0000  0.0000  0.0000  795  MET A CE  
7365  N N   . GLU D 807  ? 0.6712 0.6712 0.6712 0.0000  0.0000  0.0000  804  GLU A N   
7366  C CA  . GLU D 807  ? 0.6712 0.6712 0.6712 0.0000  0.0000  0.0000  804  GLU A CA  
7367  C C   . GLU D 807  ? 0.6712 0.6712 0.6712 0.0000  0.0000  0.0000  804  GLU A C   
7368  O O   . GLU D 807  ? 0.6712 0.6712 0.6712 0.0000  0.0000  0.0000  804  GLU A O   
7374  N N   . LYS D 808  ? 0.6485 0.6485 0.6485 0.0000  0.0000  0.0000  805  LYS A N   
7375  C CA  . LYS D 808  ? 0.6485 0.6485 0.6485 0.0000  0.0000  0.0000  805  LYS A CA  
7376  C C   . LYS D 808  ? 0.6485 0.6485 0.6485 0.0000  0.0000  0.0000  805  LYS A C   
7377  O O   . LYS D 808  ? 0.6485 0.6485 0.6485 0.0000  0.0000  0.0000  805  LYS A O   
7378  C CB  . LYS D 808  ? 0.6485 0.6485 0.6485 0.0000  0.0000  0.0000  805  LYS A CB  
7379  C CG  . LYS D 808  ? 0.6485 0.6485 0.6485 0.0000  0.0000  0.0000  805  LYS A CG  
7380  C CD  . LYS D 808  ? 0.6485 0.6485 0.6485 0.0000  0.0000  0.0000  805  LYS A CD  
7381  C CE  . LYS D 808  ? 0.6485 0.6485 0.6485 0.0000  0.0000  0.0000  805  LYS A CE  
7382  N NZ  . LYS D 808  ? 0.6485 0.6485 0.6485 0.0000  0.0000  0.0000  805  LYS A NZ  
7383  N N   . MET D 809  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  806  MET A N   
7384  C CA  . MET D 809  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  806  MET A CA  
7385  C C   . MET D 809  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  806  MET A C   
7386  O O   . MET D 809  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  806  MET A O   
7387  C CB  . MET D 809  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  806  MET A CB  
7388  C CG  . MET D 809  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  806  MET A CG  
7389  S SD  . MET D 809  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  806  MET A SD  
7390  C CE  . MET D 809  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  806  MET A CE  
7391  N N   . LEU D 810  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  807  LEU A N   
7392  C CA  . LEU D 810  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  807  LEU A CA  
7393  C C   . LEU D 810  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  807  LEU A C   
7394  O O   . LEU D 810  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  807  LEU A O   
7395  C CB  . LEU D 810  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  807  LEU A CB  
7396  C CG  . LEU D 810  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  807  LEU A CG  
7397  C CD1 . LEU D 810  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  807  LEU A CD1 
7398  C CD2 . LEU D 810  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  807  LEU A CD2 
7399  N N   . ASN D 811  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  808  ASN A N   
7400  C CA  . ASN D 811  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  808  ASN A CA  
7401  C C   . ASN D 811  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  808  ASN A C   
7402  O O   . ASN D 811  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  808  ASN A O   
7403  C CB  . ASN D 811  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  808  ASN A CB  
7404  C CG  . ASN D 811  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  808  ASN A CG  
7405  O OD1 . ASN D 811  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  808  ASN A OD1 
7406  N ND2 . ASN D 811  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  808  ASN A ND2 
7407  N N   . LYS D 812  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  809  LYS A N   
7408  C CA  . LYS D 812  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  809  LYS A CA  
7409  C C   . LYS D 812  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  809  LYS A C   
7410  O O   . LYS D 812  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  809  LYS A O   
7411  C CB  . LYS D 812  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  809  LYS A CB  
7412  C CG  . LYS D 812  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  809  LYS A CG  
7413  C CD  . LYS D 812  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  809  LYS A CD  
7414  C CE  . LYS D 812  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  809  LYS A CE  
7415  N NZ  . LYS D 812  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  809  LYS A NZ  
7416  N N   . LYS D 813  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  810  LYS A N   
7417  C CA  . LYS D 813  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  810  LYS A CA  
7418  C C   . LYS D 813  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  810  LYS A C   
7419  O O   . LYS D 813  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  810  LYS A O   
7425  N N   . LEU D 814  ? 0.6694 0.6694 0.6694 0.0000  0.0000  0.0000  811  LEU A N   
7426  C CA  . LEU D 814  ? 0.6694 0.6694 0.6694 0.0000  0.0000  0.0000  811  LEU A CA  
7427  C C   . LEU D 814  ? 0.6694 0.6694 0.6694 0.0000  0.0000  0.0000  811  LEU A C   
7428  O O   . LEU D 814  ? 0.6694 0.6694 0.6694 0.0000  0.0000  0.0000  811  LEU A O   
7429  C CB  . LEU D 814  ? 0.6694 0.6694 0.6694 0.0000  0.0000  0.0000  811  LEU A CB  
7430  C CG  . LEU D 814  ? 0.6694 0.6694 0.6694 0.0000  0.0000  0.0000  811  LEU A CG  
7431  C CD1 . LEU D 814  ? 0.6694 0.6694 0.6694 0.0000  0.0000  0.0000  811  LEU A CD1 
7432  C CD2 . LEU D 814  ? 0.6694 0.6694 0.6694 0.0000  0.0000  0.0000  811  LEU A CD2 
7433  N N   . LYS D 815  ? 0.7126 0.7126 0.7126 0.0000  0.0000  0.0000  812  LYS A N   
7434  C CA  . LYS D 815  ? 0.7126 0.7126 0.7126 0.0000  0.0000  0.0000  812  LYS A CA  
7435  C C   . LYS D 815  ? 0.7126 0.7126 0.7126 0.0000  0.0000  0.0000  812  LYS A C   
7436  O O   . LYS D 815  ? 0.7126 0.7126 0.7126 0.0000  0.0000  0.0000  812  LYS A O   
7437  C CB  . LYS D 815  ? 0.7126 0.7126 0.7126 0.0000  0.0000  0.0000  812  LYS A CB  
7438  C CG  . LYS D 815  ? 0.7126 0.7126 0.7126 0.0000  0.0000  0.0000  812  LYS A CG  
7439  C CD  . LYS D 815  ? 0.7126 0.7126 0.7126 0.0000  0.0000  0.0000  812  LYS A CD  
7440  C CE  . LYS D 815  ? 0.7126 0.7126 0.7126 0.0000  0.0000  0.0000  812  LYS A CE  
7441  N NZ  . LYS D 815  ? 0.7126 0.7126 0.7126 0.0000  0.0000  0.0000  812  LYS A NZ  
7442  N N   . ASP D 816  ? 0.6945 0.6945 0.6945 0.0000  0.0000  0.0000  813  ASP A N   
7443  C CA  . ASP D 816  ? 0.6945 0.6945 0.6945 0.0000  0.0000  0.0000  813  ASP A CA  
7444  C C   . ASP D 816  ? 0.6945 0.6945 0.6945 0.0000  0.0000  0.0000  813  ASP A C   
7445  O O   . ASP D 816  ? 0.6945 0.6945 0.6945 0.0000  0.0000  0.0000  813  ASP A O   
7446  C CB  . ASP D 816  ? 0.6945 0.6945 0.6945 0.0000  0.0000  0.0000  813  ASP A CB  
7447  C CG  . ASP D 816  ? 0.6945 0.6945 0.6945 0.0000  0.0000  0.0000  813  ASP A CG  
7448  O OD1 . ASP D 816  ? 0.6945 0.6945 0.6945 0.0000  0.0000  0.0000  813  ASP A OD1 
7449  O OD2 . ASP D 816  ? 0.6945 0.6945 0.6945 0.0000  0.0000  0.0000  813  ASP A OD2 
7450  N N   . GLN D 817  ? 0.6624 0.6624 0.6624 0.0000  0.0000  0.0000  814  GLN A N   
7451  C CA  . GLN D 817  ? 0.6624 0.6624 0.6624 0.0000  0.0000  0.0000  814  GLN A CA  
7452  C C   . GLN D 817  ? 0.6624 0.6624 0.6624 0.0000  0.0000  0.0000  814  GLN A C   
7453  O O   . GLN D 817  ? 0.6624 0.6624 0.6624 0.0000  0.0000  0.0000  814  GLN A O   
7454  C CB  . GLN D 817  ? 0.6624 0.6624 0.6624 0.0000  0.0000  0.0000  814  GLN A CB  
7455  C CG  . GLN D 817  ? 0.6624 0.6624 0.6624 0.0000  0.0000  0.0000  814  GLN A CG  
7456  C CD  . GLN D 817  ? 0.6624 0.6624 0.6624 0.0000  0.0000  0.0000  814  GLN A CD  
7457  O OE1 . GLN D 817  ? 0.6624 0.6624 0.6624 0.0000  0.0000  0.0000  814  GLN A OE1 
7458  N NE2 . GLN D 817  ? 0.6624 0.6624 0.6624 0.0000  0.0000  0.0000  814  GLN A NE2 
7459  N N   . LYS D 818  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  815  LYS A N   
7460  C CA  . LYS D 818  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  815  LYS A CA  
7461  C C   . LYS D 818  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  815  LYS A C   
7462  O O   . LYS D 818  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  815  LYS A O   
7468  N N   . THR D 819  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  816  THR A N   
7469  C CA  . THR D 819  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  816  THR A CA  
7470  C C   . THR D 819  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  816  THR A C   
7471  O O   . THR D 819  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  816  THR A O   
7472  C CB  . THR D 819  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  816  THR A CB  
7473  O OG1 . THR D 819  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  816  THR A OG1 
7474  C CG2 . THR D 819  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  816  THR A CG2 
7475  N N   . PRO D 820  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  817  PRO A N   
7476  C CA  . PRO D 820  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  817  PRO A CA  
7477  C C   . PRO D 820  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  817  PRO A C   
7478  O O   . PRO D 820  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  817  PRO A O   
7479  C CB  . PRO D 820  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  817  PRO A CB  
7480  C CG  . PRO D 820  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  817  PRO A CG  
7481  C CD  . PRO D 820  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  817  PRO A CD  
7482  N N   . ILE D 821  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  818  ILE A N   
7483  C CA  . ILE D 821  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  818  ILE A CA  
7484  C C   . ILE D 821  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  818  ILE A C   
7485  O O   . ILE D 821  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  818  ILE A O   
7486  C CB  . ILE D 821  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  818  ILE A CB  
7487  C CG1 . ILE D 821  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  818  ILE A CG1 
7488  C CG2 . ILE D 821  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  818  ILE A CG2 
7489  C CD1 . ILE D 821  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  818  ILE A CD1 
7490  N N   . PRO D 822  ? 0.6456 0.6456 0.6456 0.0000  0.0000  0.0000  819  PRO A N   
7491  C CA  . PRO D 822  ? 0.6456 0.6456 0.6456 0.0000  0.0000  0.0000  819  PRO A CA  
7492  C C   . PRO D 822  ? 0.6456 0.6456 0.6456 0.0000  0.0000  0.0000  819  PRO A C   
7493  O O   . PRO D 822  ? 0.6456 0.6456 0.6456 0.0000  0.0000  0.0000  819  PRO A O   
7494  C CB  . PRO D 822  ? 0.6456 0.6456 0.6456 0.0000  0.0000  0.0000  819  PRO A CB  
7495  C CG  . PRO D 822  ? 0.6456 0.6456 0.6456 0.0000  0.0000  0.0000  819  PRO A CG  
7496  C CD  . PRO D 822  ? 0.6456 0.6456 0.6456 0.0000  0.0000  0.0000  819  PRO A CD  
7497  N N   . ASP D 823  ? 0.7330 0.7330 0.7330 0.0000  0.0000  0.0000  820  ASP A N   
7498  C CA  . ASP D 823  ? 0.7330 0.7330 0.7330 0.0000  0.0000  0.0000  820  ASP A CA  
7499  C C   . ASP D 823  ? 0.7330 0.7330 0.7330 0.0000  0.0000  0.0000  820  ASP A C   
7500  O O   . ASP D 823  ? 0.7330 0.7330 0.7330 0.0000  0.0000  0.0000  820  ASP A O   
7501  C CB  . ASP D 823  ? 0.7330 0.7330 0.7330 0.0000  0.0000  0.0000  820  ASP A CB  
7502  C CG  . ASP D 823  ? 0.7330 0.7330 0.7330 0.0000  0.0000  0.0000  820  ASP A CG  
7503  O OD1 . ASP D 823  ? 0.7330 0.7330 0.7330 0.0000  0.0000  0.0000  820  ASP A OD1 
7504  O OD2 . ASP D 823  ? 0.7330 0.7330 0.7330 0.0000  0.0000  0.0000  820  ASP A OD2 
7505  N N   . THR D 824  ? 0.7217 0.7217 0.7217 0.0000  0.0000  0.0000  821  THR A N   
7506  C CA  . THR D 824  ? 0.7217 0.7217 0.7217 0.0000  0.0000  0.0000  821  THR A CA  
7507  C C   . THR D 824  ? 0.7217 0.7217 0.7217 0.0000  0.0000  0.0000  821  THR A C   
7508  O O   . THR D 824  ? 0.7217 0.7217 0.7217 0.0000  0.0000  0.0000  821  THR A O   
7509  C CB  . THR D 824  ? 0.7217 0.7217 0.7217 0.0000  0.0000  0.0000  821  THR A CB  
7510  O OG1 . THR D 824  ? 0.7217 0.7217 0.7217 0.0000  0.0000  0.0000  821  THR A OG1 
7511  C CG2 . THR D 824  ? 0.7217 0.7217 0.7217 0.0000  0.0000  0.0000  821  THR A CG2 
7512  N N   . LEU D 825  ? 0.7317 0.7317 0.7317 0.0000  0.0000  0.0000  822  LEU A N   
7513  C CA  . LEU D 825  ? 0.7317 0.7317 0.7317 0.0000  0.0000  0.0000  822  LEU A CA  
7514  C C   . LEU D 825  ? 0.7317 0.7317 0.7317 0.0000  0.0000  0.0000  822  LEU A C   
7515  O O   . LEU D 825  ? 0.7317 0.7317 0.7317 0.0000  0.0000  0.0000  822  LEU A O   
7516  C CB  . LEU D 825  ? 0.7317 0.7317 0.7317 0.0000  0.0000  0.0000  822  LEU A CB  
7517  C CG  . LEU D 825  ? 0.7317 0.7317 0.7317 0.0000  0.0000  0.0000  822  LEU A CG  
7518  C CD1 . LEU D 825  ? 0.7317 0.7317 0.7317 0.0000  0.0000  0.0000  822  LEU A CD1 
7519  C CD2 . LEU D 825  ? 0.7317 0.7317 0.7317 0.0000  0.0000  0.0000  822  LEU A CD2 
7520  N N   . TYR D 826  ? 0.6757 0.6757 0.6757 0.0000  0.0000  0.0000  823  TYR A N   
7521  C CA  . TYR D 826  ? 0.6757 0.6757 0.6757 0.0000  0.0000  0.0000  823  TYR A CA  
7522  C C   . TYR D 826  ? 0.6757 0.6757 0.6757 0.0000  0.0000  0.0000  823  TYR A C   
7523  O O   . TYR D 826  ? 0.6757 0.6757 0.6757 0.0000  0.0000  0.0000  823  TYR A O   
7524  C CB  . TYR D 826  ? 0.6757 0.6757 0.6757 0.0000  0.0000  0.0000  823  TYR A CB  
7525  C CG  . TYR D 826  ? 0.6757 0.6757 0.6757 0.0000  0.0000  0.0000  823  TYR A CG  
7526  C CD1 . TYR D 826  ? 0.6757 0.6757 0.6757 0.0000  0.0000  0.0000  823  TYR A CD1 
7527  C CD2 . TYR D 826  ? 0.6757 0.6757 0.6757 0.0000  0.0000  0.0000  823  TYR A CD2 
7528  C CE1 . TYR D 826  ? 0.6757 0.6757 0.6757 0.0000  0.0000  0.0000  823  TYR A CE1 
7529  C CE2 . TYR D 826  ? 0.6757 0.6757 0.6757 0.0000  0.0000  0.0000  823  TYR A CE2 
7530  C CZ  . TYR D 826  ? 0.6757 0.6757 0.6757 0.0000  0.0000  0.0000  823  TYR A CZ  
7531  O OH  . TYR D 826  ? 0.6757 0.6757 0.6757 0.0000  0.0000  0.0000  823  TYR A OH  
7532  N N   . GLN D 827  ? 0.7302 0.7302 0.7302 0.0000  0.0000  0.0000  824  GLN A N   
7533  C CA  . GLN D 827  ? 0.7302 0.7302 0.7302 0.0000  0.0000  0.0000  824  GLN A CA  
7534  C C   . GLN D 827  ? 0.7302 0.7302 0.7302 0.0000  0.0000  0.0000  824  GLN A C   
7535  O O   . GLN D 827  ? 0.7302 0.7302 0.7302 0.0000  0.0000  0.0000  824  GLN A O   
7536  C CB  . GLN D 827  ? 0.7302 0.7302 0.7302 0.0000  0.0000  0.0000  824  GLN A CB  
7537  C CG  . GLN D 827  ? 0.7302 0.7302 0.7302 0.0000  0.0000  0.0000  824  GLN A CG  
7538  C CD  . GLN D 827  ? 0.7302 0.7302 0.7302 0.0000  0.0000  0.0000  824  GLN A CD  
7539  O OE1 . GLN D 827  ? 0.7302 0.7302 0.7302 0.0000  0.0000  0.0000  824  GLN A OE1 
7540  N NE2 . GLN D 827  ? 0.7302 0.7302 0.7302 0.0000  0.0000  0.0000  824  GLN A NE2 
7541  N N   . GLU D 828  ? 0.7985 0.7985 0.7985 0.0000  0.0000  0.0000  825  GLU A N   
7542  C CA  . GLU D 828  ? 0.7985 0.7985 0.7985 0.0000  0.0000  0.0000  825  GLU A CA  
7543  C C   . GLU D 828  ? 0.7985 0.7985 0.7985 0.0000  0.0000  0.0000  825  GLU A C   
7544  O O   . GLU D 828  ? 0.7985 0.7985 0.7985 0.0000  0.0000  0.0000  825  GLU A O   
7545  C CB  . GLU D 828  ? 0.7985 0.7985 0.7985 0.0000  0.0000  0.0000  825  GLU A CB  
7546  C CG  . GLU D 828  ? 0.7985 0.7985 0.7985 0.0000  0.0000  0.0000  825  GLU A CG  
7547  C CD  . GLU D 828  ? 0.7985 0.7985 0.7985 0.0000  0.0000  0.0000  825  GLU A CD  
7548  O OE1 . GLU D 828  ? 0.7985 0.7985 0.7985 0.0000  0.0000  0.0000  825  GLU A OE1 
7549  O OE2 . GLU D 828  ? 0.7985 0.7985 0.7985 0.0000  0.0000  0.0000  825  GLU A OE2 
7550  N N   . LEU D 829  ? 0.7726 0.7726 0.7726 0.0000  0.0000  0.0000  826  LEU A N   
7551  C CA  . LEU D 829  ? 0.7726 0.7726 0.7726 0.0000  0.0000  0.0000  826  LEU A CA  
7552  C C   . LEU D 829  ? 0.7726 0.7726 0.7726 0.0000  0.0000  0.0000  826  LEU A C   
7553  O O   . LEU D 829  ? 0.7726 0.7726 0.7726 0.0000  0.0000  0.0000  826  LEU A O   
7554  C CB  . LEU D 829  ? 0.7726 0.7726 0.7726 0.0000  0.0000  0.0000  826  LEU A CB  
7555  C CG  . LEU D 829  ? 0.7726 0.7726 0.7726 0.0000  0.0000  0.0000  826  LEU A CG  
7556  C CD1 . LEU D 829  ? 0.7726 0.7726 0.7726 0.0000  0.0000  0.0000  826  LEU A CD1 
7557  C CD2 . LEU D 829  ? 0.7726 0.7726 0.7726 0.0000  0.0000  0.0000  826  LEU A CD2 
7558  N N   . TYR D 830  ? 0.7401 0.7401 0.7401 0.0000  0.0000  0.0000  827  TYR A N   
7559  C CA  . TYR D 830  ? 0.7401 0.7401 0.7401 0.0000  0.0000  0.0000  827  TYR A CA  
7560  C C   . TYR D 830  ? 0.7401 0.7401 0.7401 0.0000  0.0000  0.0000  827  TYR A C   
7561  O O   . TYR D 830  ? 0.7401 0.7401 0.7401 0.0000  0.0000  0.0000  827  TYR A O   
7562  C CB  . TYR D 830  ? 0.7401 0.7401 0.7401 0.0000  0.0000  0.0000  827  TYR A CB  
7563  C CG  . TYR D 830  ? 0.7401 0.7401 0.7401 0.0000  0.0000  0.0000  827  TYR A CG  
7564  C CD1 . TYR D 830  ? 0.7401 0.7401 0.7401 0.0000  0.0000  0.0000  827  TYR A CD1 
7565  C CD2 . TYR D 830  ? 0.7401 0.7401 0.7401 0.0000  0.0000  0.0000  827  TYR A CD2 
7566  C CE1 . TYR D 830  ? 0.7401 0.7401 0.7401 0.0000  0.0000  0.0000  827  TYR A CE1 
7567  C CE2 . TYR D 830  ? 0.7401 0.7401 0.7401 0.0000  0.0000  0.0000  827  TYR A CE2 
7568  C CZ  . TYR D 830  ? 0.7401 0.7401 0.7401 0.0000  0.0000  0.0000  827  TYR A CZ  
7569  O OH  . TYR D 830  ? 0.7401 0.7401 0.7401 0.0000  0.0000  0.0000  827  TYR A OH  
7570  N N   . ASP D 831  ? 0.8038 0.8038 0.8038 0.0000  0.0000  0.0000  828  ASP A N   
7571  C CA  . ASP D 831  ? 0.8038 0.8038 0.8038 0.0000  0.0000  0.0000  828  ASP A CA  
7572  C C   . ASP D 831  ? 0.8038 0.8038 0.8038 0.0000  0.0000  0.0000  828  ASP A C   
7573  O O   . ASP D 831  ? 0.8038 0.8038 0.8038 0.0000  0.0000  0.0000  828  ASP A O   
7574  C CB  . ASP D 831  ? 0.8038 0.8038 0.8038 0.0000  0.0000  0.0000  828  ASP A CB  
7575  C CG  . ASP D 831  ? 0.8038 0.8038 0.8038 0.0000  0.0000  0.0000  828  ASP A CG  
7576  O OD1 . ASP D 831  ? 0.8038 0.8038 0.8038 0.0000  0.0000  0.0000  828  ASP A OD1 
7577  O OD2 . ASP D 831  ? 0.8038 0.8038 0.8038 0.0000  0.0000  0.0000  828  ASP A OD2 
7578  N N   . TYR D 832  ? 0.8529 0.8529 0.8529 0.0000  0.0000  0.0000  829  TYR A N   
7579  C CA  . TYR D 832  ? 0.8529 0.8529 0.8529 0.0000  0.0000  0.0000  829  TYR A CA  
7580  C C   . TYR D 832  ? 0.8529 0.8529 0.8529 0.0000  0.0000  0.0000  829  TYR A C   
7581  O O   . TYR D 832  ? 0.8529 0.8529 0.8529 0.0000  0.0000  0.0000  829  TYR A O   
7582  C CB  . TYR D 832  ? 0.8529 0.8529 0.8529 0.0000  0.0000  0.0000  829  TYR A CB  
7583  C CG  . TYR D 832  ? 0.8529 0.8529 0.8529 0.0000  0.0000  0.0000  829  TYR A CG  
7584  C CD1 . TYR D 832  ? 0.8529 0.8529 0.8529 0.0000  0.0000  0.0000  829  TYR A CD1 
7585  C CD2 . TYR D 832  ? 0.8529 0.8529 0.8529 0.0000  0.0000  0.0000  829  TYR A CD2 
7586  C CE1 . TYR D 832  ? 0.8529 0.8529 0.8529 0.0000  0.0000  0.0000  829  TYR A CE1 
7587  C CE2 . TYR D 832  ? 0.8529 0.8529 0.8529 0.0000  0.0000  0.0000  829  TYR A CE2 
7588  C CZ  . TYR D 832  ? 0.8529 0.8529 0.8529 0.0000  0.0000  0.0000  829  TYR A CZ  
7589  O OH  . TYR D 832  ? 0.8529 0.8529 0.8529 0.0000  0.0000  0.0000  829  TYR A OH  
7590  N N   . VAL D 833  ? 0.7892 0.7892 0.7892 0.0000  0.0000  0.0000  830  VAL A N   
7591  C CA  . VAL D 833  ? 0.7892 0.7892 0.7892 0.0000  0.0000  0.0000  830  VAL A CA  
7592  C C   . VAL D 833  ? 0.7892 0.7892 0.7892 0.0000  0.0000  0.0000  830  VAL A C   
7593  O O   . VAL D 833  ? 0.7892 0.7892 0.7892 0.0000  0.0000  0.0000  830  VAL A O   
7594  C CB  . VAL D 833  ? 0.7892 0.7892 0.7892 0.0000  0.0000  0.0000  830  VAL A CB  
7595  C CG1 . VAL D 833  ? 0.7892 0.7892 0.7892 0.0000  0.0000  0.0000  830  VAL A CG1 
7596  C CG2 . VAL D 833  ? 0.7892 0.7892 0.7892 0.0000  0.0000  0.0000  830  VAL A CG2 
7597  N N   . ASN D 834  ? 0.7896 0.7896 0.7896 0.0000  0.0000  0.0000  831  ASN A N   
7598  C CA  . ASN D 834  ? 0.7896 0.7896 0.7896 0.0000  0.0000  0.0000  831  ASN A CA  
7599  C C   . ASN D 834  ? 0.7896 0.7896 0.7896 0.0000  0.0000  0.0000  831  ASN A C   
7600  O O   . ASN D 834  ? 0.7896 0.7896 0.7896 0.0000  0.0000  0.0000  831  ASN A O   
7601  C CB  . ASN D 834  ? 0.7896 0.7896 0.7896 0.0000  0.0000  0.0000  831  ASN A CB  
7602  C CG  . ASN D 834  ? 0.7896 0.7896 0.7896 0.0000  0.0000  0.0000  831  ASN A CG  
7603  O OD1 . ASN D 834  ? 0.7896 0.7896 0.7896 0.0000  0.0000  0.0000  831  ASN A OD1 
7604  N ND2 . ASN D 834  ? 0.7896 0.7896 0.7896 0.0000  0.0000  0.0000  831  ASN A ND2 
7605  N N   . HIS D 835  ? 0.8320 0.8320 0.8320 0.0000  0.0000  0.0000  832  HIS A N   
7606  C CA  . HIS D 835  ? 0.8320 0.8320 0.8320 0.0000  0.0000  0.0000  832  HIS A CA  
7607  C C   . HIS D 835  ? 0.8320 0.8320 0.8320 0.0000  0.0000  0.0000  832  HIS A C   
7608  O O   . HIS D 835  ? 0.8320 0.8320 0.8320 0.0000  0.0000  0.0000  832  HIS A O   
7609  C CB  . HIS D 835  ? 0.8320 0.8320 0.8320 0.0000  0.0000  0.0000  832  HIS A CB  
7610  C CG  . HIS D 835  ? 0.8320 0.8320 0.8320 0.0000  0.0000  0.0000  832  HIS A CG  
7611  N ND1 . HIS D 835  ? 0.8320 0.8320 0.8320 0.0000  0.0000  0.0000  832  HIS A ND1 
7612  C CD2 . HIS D 835  ? 0.8320 0.8320 0.8320 0.0000  0.0000  0.0000  832  HIS A CD2 
7613  C CE1 . HIS D 835  ? 0.8320 0.8320 0.8320 0.0000  0.0000  0.0000  832  HIS A CE1 
7614  N NE2 . HIS D 835  ? 0.8320 0.8320 0.8320 0.0000  0.0000  0.0000  832  HIS A NE2 
7615  N N   . ARG D 836  ? 0.8701 0.8701 0.8701 0.0000  0.0000  0.0000  833  ARG A N   
7616  C CA  . ARG D 836  ? 0.8701 0.8701 0.8701 0.0000  0.0000  0.0000  833  ARG A CA  
7617  C C   . ARG D 836  ? 0.8701 0.8701 0.8701 0.0000  0.0000  0.0000  833  ARG A C   
7618  O O   . ARG D 836  ? 0.8701 0.8701 0.8701 0.0000  0.0000  0.0000  833  ARG A O   
7619  C CB  . ARG D 836  ? 0.8701 0.8701 0.8701 0.0000  0.0000  0.0000  833  ARG A CB  
7620  C CG  . ARG D 836  ? 0.8701 0.8701 0.8701 0.0000  0.0000  0.0000  833  ARG A CG  
7621  C CD  . ARG D 836  ? 0.8701 0.8701 0.8701 0.0000  0.0000  0.0000  833  ARG A CD  
7622  N NE  . ARG D 836  ? 0.8701 0.8701 0.8701 0.0000  0.0000  0.0000  833  ARG A NE  
7623  C CZ  . ARG D 836  ? 0.8701 0.8701 0.8701 0.0000  0.0000  0.0000  833  ARG A CZ  
7624  N NH1 . ARG D 836  ? 0.8701 0.8701 0.8701 0.0000  0.0000  0.0000  833  ARG A NH1 
7625  N NH2 . ARG D 836  ? 0.8701 0.8701 0.8701 0.0000  0.0000  0.0000  833  ARG A NH2 
7626  N N   . LEU D 837  ? 1.0028 1.0028 1.0028 0.0000  0.0000  0.0000  834  LEU A N   
7627  C CA  . LEU D 837  ? 1.0028 1.0028 1.0028 0.0000  0.0000  0.0000  834  LEU A CA  
7628  C C   . LEU D 837  ? 1.0028 1.0028 1.0028 0.0000  0.0000  0.0000  834  LEU A C   
7629  O O   . LEU D 837  ? 1.0028 1.0028 1.0028 0.0000  0.0000  0.0000  834  LEU A O   
7630  C CB  . LEU D 837  ? 1.0028 1.0028 1.0028 0.0000  0.0000  0.0000  834  LEU A CB  
7631  C CG  . LEU D 837  ? 1.0028 1.0028 1.0028 0.0000  0.0000  0.0000  834  LEU A CG  
7632  C CD1 . LEU D 837  ? 1.0028 1.0028 1.0028 0.0000  0.0000  0.0000  834  LEU A CD1 
7633  C CD2 . LEU D 837  ? 1.0028 1.0028 1.0028 0.0000  0.0000  0.0000  834  LEU A CD2 
7634  N N   . SER D 838  ? 1.0859 1.0859 1.0859 0.0000  0.0000  0.0000  835  SER A N   
7635  C CA  . SER D 838  ? 1.0859 1.0859 1.0859 0.0000  0.0000  0.0000  835  SER A CA  
7636  C C   . SER D 838  ? 1.0859 1.0859 1.0859 0.0000  0.0000  0.0000  835  SER A C   
7637  O O   . SER D 838  ? 1.0859 1.0859 1.0859 0.0000  0.0000  0.0000  835  SER A O   
7638  C CB  . SER D 838  ? 1.0859 1.0859 1.0859 0.0000  0.0000  0.0000  835  SER A CB  
7639  O OG  . SER D 838  ? 1.0859 1.0859 1.0859 0.0000  0.0000  0.0000  835  SER A OG  
7640  N N   . HIS D 839  ? 1.1904 1.1904 1.1904 0.0000  0.0000  0.0000  836  HIS A N   
7641  C CA  . HIS D 839  ? 1.1904 1.1904 1.1904 0.0000  0.0000  0.0000  836  HIS A CA  
7642  C C   . HIS D 839  ? 1.1904 1.1904 1.1904 0.0000  0.0000  0.0000  836  HIS A C   
7643  O O   . HIS D 839  ? 1.1904 1.1904 1.1904 0.0000  0.0000  0.0000  836  HIS A O   
7644  C CB  . HIS D 839  ? 1.1904 1.1904 1.1904 0.0000  0.0000  0.0000  836  HIS A CB  
7645  C CG  . HIS D 839  ? 1.1904 1.1904 1.1904 0.0000  0.0000  0.0000  836  HIS A CG  
7646  N ND1 . HIS D 839  ? 1.1904 1.1904 1.1904 0.0000  0.0000  0.0000  836  HIS A ND1 
7647  C CD2 . HIS D 839  ? 1.1904 1.1904 1.1904 0.0000  0.0000  0.0000  836  HIS A CD2 
7648  C CE1 . HIS D 839  ? 1.1904 1.1904 1.1904 0.0000  0.0000  0.0000  836  HIS A CE1 
7649  N NE2 . HIS D 839  ? 1.1904 1.1904 1.1904 0.0000  0.0000  0.0000  836  HIS A NE2 
7650  N N   . ASP D 840  ? 1.1320 1.1320 1.1320 0.0000  0.0000  0.0000  837  ASP A N   
7651  C CA  . ASP D 840  ? 1.1320 1.1320 1.1320 0.0000  0.0000  0.0000  837  ASP A CA  
7652  C C   . ASP D 840  ? 1.1320 1.1320 1.1320 0.0000  0.0000  0.0000  837  ASP A C   
7653  O O   . ASP D 840  ? 1.1320 1.1320 1.1320 0.0000  0.0000  0.0000  837  ASP A O   
7654  C CB  . ASP D 840  ? 1.1320 1.1320 1.1320 0.0000  0.0000  0.0000  837  ASP A CB  
7655  C CG  . ASP D 840  ? 1.1320 1.1320 1.1320 0.0000  0.0000  0.0000  837  ASP A CG  
7656  O OD1 . ASP D 840  ? 1.1320 1.1320 1.1320 0.0000  0.0000  0.0000  837  ASP A OD1 
7657  O OD2 . ASP D 840  ? 1.1320 1.1320 1.1320 0.0000  0.0000  0.0000  837  ASP A OD2 
7658  N N   . LEU D 841  ? 1.0210 1.0210 1.0210 0.0000  0.0000  0.0000  838  LEU A N   
7659  C CA  . LEU D 841  ? 1.0210 1.0210 1.0210 0.0000  0.0000  0.0000  838  LEU A CA  
7660  C C   . LEU D 841  ? 1.0210 1.0210 1.0210 0.0000  0.0000  0.0000  838  LEU A C   
7661  O O   . LEU D 841  ? 1.0210 1.0210 1.0210 0.0000  0.0000  0.0000  838  LEU A O   
7662  C CB  . LEU D 841  ? 1.0210 1.0210 1.0210 0.0000  0.0000  0.0000  838  LEU A CB  
7663  C CG  . LEU D 841  ? 1.0210 1.0210 1.0210 0.0000  0.0000  0.0000  838  LEU A CG  
7664  C CD1 . LEU D 841  ? 1.0210 1.0210 1.0210 0.0000  0.0000  0.0000  838  LEU A CD1 
7665  C CD2 . LEU D 841  ? 1.0210 1.0210 1.0210 0.0000  0.0000  0.0000  838  LEU A CD2 
7666  N N   . SER D 842  ? 0.9610 0.9610 0.9610 0.0000  0.0000  0.0000  839  SER A N   
7667  C CA  . SER D 842  ? 0.9610 0.9610 0.9610 0.0000  0.0000  0.0000  839  SER A CA  
7668  C C   . SER D 842  ? 0.9610 0.9610 0.9610 0.0000  0.0000  0.0000  839  SER A C   
7669  O O   . SER D 842  ? 0.9610 0.9610 0.9610 0.0000  0.0000  0.0000  839  SER A O   
7670  C CB  . SER D 842  ? 0.9610 0.9610 0.9610 0.0000  0.0000  0.0000  839  SER A CB  
7671  O OG  . SER D 842  ? 0.9610 0.9610 0.9610 0.0000  0.0000  0.0000  839  SER A OG  
7672  N N   . ASP D 843  ? 0.9322 0.9322 0.9322 0.0000  0.0000  0.0000  840  ASP A N   
7673  C CA  . ASP D 843  ? 0.9322 0.9322 0.9322 0.0000  0.0000  0.0000  840  ASP A CA  
7674  C C   . ASP D 843  ? 0.9322 0.9322 0.9322 0.0000  0.0000  0.0000  840  ASP A C   
7675  O O   . ASP D 843  ? 0.9322 0.9322 0.9322 0.0000  0.0000  0.0000  840  ASP A O   
7676  C CB  . ASP D 843  ? 0.9322 0.9322 0.9322 0.0000  0.0000  0.0000  840  ASP A CB  
7677  C CG  . ASP D 843  ? 0.9322 0.9322 0.9322 0.0000  0.0000  0.0000  840  ASP A CG  
7678  O OD1 . ASP D 843  ? 0.9322 0.9322 0.9322 0.0000  0.0000  0.0000  840  ASP A OD1 
7679  O OD2 . ASP D 843  ? 0.9322 0.9322 0.9322 0.0000  0.0000  0.0000  840  ASP A OD2 
7680  N N   . GLU D 844  ? 0.9258 0.9258 0.9258 0.0000  0.0000  0.0000  841  GLU A N   
7681  C CA  . GLU D 844  ? 0.9258 0.9258 0.9258 0.0000  0.0000  0.0000  841  GLU A CA  
7682  C C   . GLU D 844  ? 0.9258 0.9258 0.9258 0.0000  0.0000  0.0000  841  GLU A C   
7683  O O   . GLU D 844  ? 0.9258 0.9258 0.9258 0.0000  0.0000  0.0000  841  GLU A O   
7684  C CB  . GLU D 844  ? 0.9258 0.9258 0.9258 0.0000  0.0000  0.0000  841  GLU A CB  
7685  C CG  . GLU D 844  ? 0.9258 0.9258 0.9258 0.0000  0.0000  0.0000  841  GLU A CG  
7686  C CD  . GLU D 844  ? 0.9258 0.9258 0.9258 0.0000  0.0000  0.0000  841  GLU A CD  
7687  O OE1 . GLU D 844  ? 0.9258 0.9258 0.9258 0.0000  0.0000  0.0000  841  GLU A OE1 
7688  O OE2 . GLU D 844  ? 0.9258 0.9258 0.9258 0.0000  0.0000  0.0000  841  GLU A OE2 
7689  N N   . ALA D 845  ? 0.8706 0.8706 0.8706 0.0000  0.0000  0.0000  842  ALA A N   
7690  C CA  . ALA D 845  ? 0.8706 0.8706 0.8706 0.0000  0.0000  0.0000  842  ALA A CA  
7691  C C   . ALA D 845  ? 0.8706 0.8706 0.8706 0.0000  0.0000  0.0000  842  ALA A C   
7692  O O   . ALA D 845  ? 0.8706 0.8706 0.8706 0.0000  0.0000  0.0000  842  ALA A O   
7693  C CB  . ALA D 845  ? 0.8706 0.8706 0.8706 0.0000  0.0000  0.0000  842  ALA A CB  
7694  N N   . ARG D 846  ? 0.9054 0.9054 0.9054 0.0000  0.0000  0.0000  843  ARG A N   
7695  C CA  . ARG D 846  ? 0.9054 0.9054 0.9054 0.0000  0.0000  0.0000  843  ARG A CA  
7696  C C   . ARG D 846  ? 0.9054 0.9054 0.9054 0.0000  0.0000  0.0000  843  ARG A C   
7697  O O   . ARG D 846  ? 0.9054 0.9054 0.9054 0.0000  0.0000  0.0000  843  ARG A O   
7698  C CB  . ARG D 846  ? 0.9054 0.9054 0.9054 0.0000  0.0000  0.0000  843  ARG A CB  
7699  C CG  . ARG D 846  ? 0.9054 0.9054 0.9054 0.0000  0.0000  0.0000  843  ARG A CG  
7700  C CD  . ARG D 846  ? 0.9054 0.9054 0.9054 0.0000  0.0000  0.0000  843  ARG A CD  
7701  N NE  . ARG D 846  ? 0.9054 0.9054 0.9054 0.0000  0.0000  0.0000  843  ARG A NE  
7702  C CZ  . ARG D 846  ? 0.9054 0.9054 0.9054 0.0000  0.0000  0.0000  843  ARG A CZ  
7703  N NH1 . ARG D 846  ? 0.9054 0.9054 0.9054 0.0000  0.0000  0.0000  843  ARG A NH1 
7704  N NH2 . ARG D 846  ? 0.9054 0.9054 0.9054 0.0000  0.0000  0.0000  843  ARG A NH2 
7705  N N   . ALA D 847  ? 0.8607 0.8607 0.8607 0.0000  0.0000  0.0000  844  ALA A N   
7706  C CA  . ALA D 847  ? 0.8607 0.8607 0.8607 0.0000  0.0000  0.0000  844  ALA A CA  
7707  C C   . ALA D 847  ? 0.8607 0.8607 0.8607 0.0000  0.0000  0.0000  844  ALA A C   
7708  O O   . ALA D 847  ? 0.8607 0.8607 0.8607 0.0000  0.0000  0.0000  844  ALA A O   
7709  C CB  . ALA D 847  ? 0.8607 0.8607 0.8607 0.0000  0.0000  0.0000  844  ALA A CB  
7710  N N   . LEU D 848  ? 0.7729 0.7729 0.7729 0.0000  0.0000  0.0000  845  LEU A N   
7711  C CA  . LEU D 848  ? 0.7729 0.7729 0.7729 0.0000  0.0000  0.0000  845  LEU A CA  
7712  C C   . LEU D 848  ? 0.7729 0.7729 0.7729 0.0000  0.0000  0.0000  845  LEU A C   
7713  O O   . LEU D 848  ? 0.7729 0.7729 0.7729 0.0000  0.0000  0.0000  845  LEU A O   
7714  C CB  . LEU D 848  ? 0.7729 0.7729 0.7729 0.0000  0.0000  0.0000  845  LEU A CB  
7715  C CG  . LEU D 848  ? 0.7729 0.7729 0.7729 0.0000  0.0000  0.0000  845  LEU A CG  
7716  C CD1 . LEU D 848  ? 0.7729 0.7729 0.7729 0.0000  0.0000  0.0000  845  LEU A CD1 
7717  C CD2 . LEU D 848  ? 0.7729 0.7729 0.7729 0.0000  0.0000  0.0000  845  LEU A CD2 
7718  N N   . LEU D 849  ? 0.7873 0.7873 0.7873 0.0000  0.0000  0.0000  846  LEU A N   
7719  C CA  . LEU D 849  ? 0.7873 0.7873 0.7873 0.0000  0.0000  0.0000  846  LEU A CA  
7720  C C   . LEU D 849  ? 0.7873 0.7873 0.7873 0.0000  0.0000  0.0000  846  LEU A C   
7721  O O   . LEU D 849  ? 0.7873 0.7873 0.7873 0.0000  0.0000  0.0000  846  LEU A O   
7722  C CB  . LEU D 849  ? 0.7873 0.7873 0.7873 0.0000  0.0000  0.0000  846  LEU A CB  
7723  C CG  . LEU D 849  ? 0.7873 0.7873 0.7873 0.0000  0.0000  0.0000  846  LEU A CG  
7724  C CD1 . LEU D 849  ? 0.7873 0.7873 0.7873 0.0000  0.0000  0.0000  846  LEU A CD1 
7725  C CD2 . LEU D 849  ? 0.7873 0.7873 0.7873 0.0000  0.0000  0.0000  846  LEU A CD2 
7726  N N   . PRO D 850  ? 0.7658 0.7658 0.7658 0.0000  0.0000  0.0000  847  PRO A N   
7727  C CA  . PRO D 850  ? 0.7658 0.7658 0.7658 0.0000  0.0000  0.0000  847  PRO A CA  
7728  C C   . PRO D 850  ? 0.7658 0.7658 0.7658 0.0000  0.0000  0.0000  847  PRO A C   
7729  O O   . PRO D 850  ? 0.7658 0.7658 0.7658 0.0000  0.0000  0.0000  847  PRO A O   
7730  C CB  . PRO D 850  ? 0.7658 0.7658 0.7658 0.0000  0.0000  0.0000  847  PRO A CB  
7731  C CG  . PRO D 850  ? 0.7658 0.7658 0.7658 0.0000  0.0000  0.0000  847  PRO A CG  
7732  C CD  . PRO D 850  ? 0.7658 0.7658 0.7658 0.0000  0.0000  0.0000  847  PRO A CD  
7733  N N   . ASN D 851  ? 0.7166 0.7166 0.7166 0.0000  0.0000  0.0000  848  ASN A N   
7734  C CA  . ASN D 851  ? 0.7166 0.7166 0.7166 0.0000  0.0000  0.0000  848  ASN A CA  
7735  C C   . ASN D 851  ? 0.7166 0.7166 0.7166 0.0000  0.0000  0.0000  848  ASN A C   
7736  O O   . ASN D 851  ? 0.7166 0.7166 0.7166 0.0000  0.0000  0.0000  848  ASN A O   
7737  C CB  . ASN D 851  ? 0.7166 0.7166 0.7166 0.0000  0.0000  0.0000  848  ASN A CB  
7738  C CG  . ASN D 851  ? 0.7166 0.7166 0.7166 0.0000  0.0000  0.0000  848  ASN A CG  
7739  O OD1 . ASN D 851  ? 0.7166 0.7166 0.7166 0.0000  0.0000  0.0000  848  ASN A OD1 
7740  N ND2 . ASN D 851  ? 0.7166 0.7166 0.7166 0.0000  0.0000  0.0000  848  ASN A ND2 
7741  N N   . VAL D 852  ? 0.6541 0.6541 0.6541 0.0000  0.0000  0.0000  849  VAL A N   
7742  C CA  . VAL D 852  ? 0.6541 0.6541 0.6541 0.0000  0.0000  0.0000  849  VAL A CA  
7743  C C   . VAL D 852  ? 0.6541 0.6541 0.6541 0.0000  0.0000  0.0000  849  VAL A C   
7744  O O   . VAL D 852  ? 0.6541 0.6541 0.6541 0.0000  0.0000  0.0000  849  VAL A O   
7745  C CB  . VAL D 852  ? 0.6541 0.6541 0.6541 0.0000  0.0000  0.0000  849  VAL A CB  
7746  C CG1 . VAL D 852  ? 0.6541 0.6541 0.6541 0.0000  0.0000  0.0000  849  VAL A CG1 
7747  C CG2 . VAL D 852  ? 0.6541 0.6541 0.6541 0.0000  0.0000  0.0000  849  VAL A CG2 
7748  N N   . ILE D 853  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  850  ILE A N   
7749  C CA  . ILE D 853  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  850  ILE A CA  
7750  C C   . ILE D 853  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  850  ILE A C   
7751  O O   . ILE D 853  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  850  ILE A O   
7752  C CB  . ILE D 853  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  850  ILE A CB  
7753  C CG1 . ILE D 853  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  850  ILE A CG1 
7754  C CG2 . ILE D 853  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  850  ILE A CG2 
7755  C CD1 . ILE D 853  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  850  ILE A CD1 
7756  N N   . THR D 854  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  851  THR A N   
7757  C CA  . THR D 854  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  851  THR A CA  
7758  C C   . THR D 854  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  851  THR A C   
7759  O O   . THR D 854  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  851  THR A O   
7760  C CB  . THR D 854  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  851  THR A CB  
7761  O OG1 . THR D 854  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  851  THR A OG1 
7762  C CG2 . THR D 854  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  851  THR A CG2 
7763  N N   . LYS D 855  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  852  LYS A N   
7764  C CA  . LYS D 855  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  852  LYS A CA  
7765  C C   . LYS D 855  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  852  LYS A C   
7766  O O   . LYS D 855  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  852  LYS A O   
7767  C CB  . LYS D 855  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  852  LYS A CB  
7768  C CG  . LYS D 855  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  852  LYS A CG  
7769  C CD  . LYS D 855  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  852  LYS A CD  
7770  C CE  . LYS D 855  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  852  LYS A CE  
7771  N NZ  . LYS D 855  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  852  LYS A NZ  
7772  N N   . GLU D 856  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  853  GLU A N   
7773  C CA  . GLU D 856  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  853  GLU A CA  
7774  C C   . GLU D 856  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  853  GLU A C   
7775  O O   . GLU D 856  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  853  GLU A O   
7781  N N   . VAL D 857  ? 0.6429 0.6429 0.6429 0.0000  0.0000  0.0000  854  VAL A N   
7782  C CA  . VAL D 857  ? 0.6429 0.6429 0.6429 0.0000  0.0000  0.0000  854  VAL A CA  
7783  C C   . VAL D 857  ? 0.6429 0.6429 0.6429 0.0000  0.0000  0.0000  854  VAL A C   
7784  O O   . VAL D 857  ? 0.6429 0.6429 0.6429 0.0000  0.0000  0.0000  854  VAL A O   
7785  C CB  . VAL D 857  ? 0.6429 0.6429 0.6429 0.0000  0.0000  0.0000  854  VAL A CB  
7786  C CG1 . VAL D 857  ? 0.6429 0.6429 0.6429 0.0000  0.0000  0.0000  854  VAL A CG1 
7787  C CG2 . VAL D 857  ? 0.6429 0.6429 0.6429 0.0000  0.0000  0.0000  854  VAL A CG2 
7788  N N   . SER D 858  ? 0.6430 0.6430 0.6430 0.0000  0.0000  0.0000  855  SER A N   
7789  C CA  . SER D 858  ? 0.6430 0.6430 0.6430 0.0000  0.0000  0.0000  855  SER A CA  
7790  C C   . SER D 858  ? 0.6430 0.6430 0.6430 0.0000  0.0000  0.0000  855  SER A C   
7791  O O   . SER D 858  ? 0.6430 0.6430 0.6430 0.0000  0.0000  0.0000  855  SER A O   
7792  C CB  . SER D 858  ? 0.6430 0.6430 0.6430 0.0000  0.0000  0.0000  855  SER A CB  
7793  O OG  . SER D 858  ? 0.6430 0.6430 0.6430 0.0000  0.0000  0.0000  855  SER A OG  
7794  N N   . HIS D 859  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  856  HIS A N   
7795  C CA  . HIS D 859  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  856  HIS A CA  
7796  C C   . HIS D 859  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  856  HIS A C   
7797  O O   . HIS D 859  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  856  HIS A O   
7798  C CB  . HIS D 859  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  856  HIS A CB  
7799  C CG  . HIS D 859  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  856  HIS A CG  
7800  N ND1 . HIS D 859  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  856  HIS A ND1 
7801  C CD2 . HIS D 859  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  856  HIS A CD2 
7802  C CE1 . HIS D 859  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  856  HIS A CE1 
7803  N NE2 . HIS D 859  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  856  HIS A NE2 
7804  N N   . GLU D 860  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  857  GLU A N   
7805  C CA  . GLU D 860  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  857  GLU A CA  
7806  C C   . GLU D 860  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  857  GLU A C   
7807  O O   . GLU D 860  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  857  GLU A O   
7808  C CB  . GLU D 860  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  857  GLU A CB  
7809  C CG  . GLU D 860  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  857  GLU A CG  
7810  C CD  . GLU D 860  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  857  GLU A CD  
7811  O OE1 . GLU D 860  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  857  GLU A OE1 
7812  O OE2 . GLU D 860  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  857  GLU A OE2 
7813  N N   . ILE D 861  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  858  ILE A N   
7814  C CA  . ILE D 861  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  858  ILE A CA  
7815  C C   . ILE D 861  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  858  ILE A C   
7816  O O   . ILE D 861  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  858  ILE A O   
7817  C CB  . ILE D 861  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  858  ILE A CB  
7818  C CG1 . ILE D 861  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  858  ILE A CG1 
7819  C CG2 . ILE D 861  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  858  ILE A CG2 
7820  C CD1 . ILE D 861  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  858  ILE A CD1 
7821  N N   . ILE D 862  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  859  ILE A N   
7822  C CA  . ILE D 862  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  859  ILE A CA  
7823  C C   . ILE D 862  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  859  ILE A C   
7824  O O   . ILE D 862  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  859  ILE A O   
7825  C CB  . ILE D 862  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  859  ILE A CB  
7826  C CG1 . ILE D 862  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  859  ILE A CG1 
7827  C CG2 . ILE D 862  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  859  ILE A CG2 
7828  C CD1 . ILE D 862  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  859  ILE A CD1 
7829  N N   . LYS D 863  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  860  LYS A N   
7830  C CA  . LYS D 863  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  860  LYS A CA  
7831  C C   . LYS D 863  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  860  LYS A C   
7832  O O   . LYS D 863  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  860  LYS A O   
7833  C CB  . LYS D 863  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  860  LYS A CB  
7834  C CG  . LYS D 863  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  860  LYS A CG  
7835  C CD  . LYS D 863  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  860  LYS A CD  
7836  C CE  . LYS D 863  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  860  LYS A CE  
7837  N NZ  . LYS D 863  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  860  LYS A NZ  
7838  N N   . ASP D 864  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  861  ASP A N   
7839  C CA  . ASP D 864  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  861  ASP A CA  
7840  C C   . ASP D 864  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  861  ASP A C   
7841  O O   . ASP D 864  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  861  ASP A O   
7846  N N   . ARG D 865  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  862  ARG A N   
7847  C CA  . ARG D 865  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  862  ARG A CA  
7848  C C   . ARG D 865  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  862  ARG A C   
7849  O O   . ARG D 865  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  862  ARG A O   
7857  N N   . ARG D 866  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  863  ARG A N   
7858  C CA  . ARG D 866  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  863  ARG A CA  
7859  C C   . ARG D 866  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  863  ARG A C   
7860  O O   . ARG D 866  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  863  ARG A O   
7861  C CB  . ARG D 866  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  863  ARG A CB  
7862  C CG  . ARG D 866  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  863  ARG A CG  
7863  C CD  . ARG D 866  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  863  ARG A CD  
7864  N NE  . ARG D 866  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  863  ARG A NE  
7865  C CZ  . ARG D 866  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  863  ARG A CZ  
7866  N NH1 . ARG D 866  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  863  ARG A NH1 
7867  N NH2 . ARG D 866  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  863  ARG A NH2 
7868  N N   . PHE D 867  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  864  PHE A N   
7869  C CA  . PHE D 867  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  864  PHE A CA  
7870  C C   . PHE D 867  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  864  PHE A C   
7871  O O   . PHE D 867  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  864  PHE A O   
7872  C CB  . PHE D 867  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  864  PHE A CB  
7873  C CG  . PHE D 867  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  864  PHE A CG  
7874  C CD1 . PHE D 867  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  864  PHE A CD1 
7875  C CD2 . PHE D 867  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  864  PHE A CD2 
7876  C CE1 . PHE D 867  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  864  PHE A CE1 
7877  C CE2 . PHE D 867  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  864  PHE A CE2 
7878  C CZ  . PHE D 867  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  864  PHE A CZ  
7879  N N   . THR D 868  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  865  THR A N   
7880  C CA  . THR D 868  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  865  THR A CA  
7881  C C   . THR D 868  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  865  THR A C   
7882  O O   . THR D 868  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  865  THR A O   
7883  C CB  . THR D 868  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  865  THR A CB  
7884  O OG1 . THR D 868  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  865  THR A OG1 
7885  C CG2 . THR D 868  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  865  THR A CG2 
7886  N N   . SER D 869  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  866  SER A N   
7887  C CA  . SER D 869  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  866  SER A CA  
7888  C C   . SER D 869  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  866  SER A C   
7889  O O   . SER D 869  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  866  SER A O   
7890  C CB  . SER D 869  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  866  SER A CB  
7891  O OG  . SER D 869  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  866  SER A OG  
7892  N N   . ASP D 870  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  867  ASP A N   
7893  C CA  . ASP D 870  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  867  ASP A CA  
7894  C C   . ASP D 870  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  867  ASP A C   
7895  O O   . ASP D 870  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  867  ASP A O   
7896  C CB  . ASP D 870  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  867  ASP A CB  
7897  C CG  . ASP D 870  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  867  ASP A CG  
7898  O OD1 . ASP D 870  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  867  ASP A OD1 
7899  O OD2 . ASP D 870  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  867  ASP A OD2 
7900  N N   . LYS D 871  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  868  LYS A N   
7901  C CA  . LYS D 871  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  868  LYS A CA  
7902  C C   . LYS D 871  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  868  LYS A C   
7903  O O   . LYS D 871  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  868  LYS A O   
7904  C CB  . LYS D 871  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  868  LYS A CB  
7905  C CG  . LYS D 871  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  868  LYS A CG  
7906  C CD  . LYS D 871  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  868  LYS A CD  
7907  C CE  . LYS D 871  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  868  LYS A CE  
7908  N NZ  . LYS D 871  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  868  LYS A NZ  
7909  N N   . PHE D 872  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  869  PHE A N   
7910  C CA  . PHE D 872  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  869  PHE A CA  
7911  C C   . PHE D 872  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  869  PHE A C   
7912  O O   . PHE D 872  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  869  PHE A O   
7913  C CB  . PHE D 872  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  869  PHE A CB  
7914  C CG  . PHE D 872  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  869  PHE A CG  
7915  C CD1 . PHE D 872  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  869  PHE A CD1 
7916  C CD2 . PHE D 872  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  869  PHE A CD2 
7917  C CE1 . PHE D 872  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  869  PHE A CE1 
7918  C CE2 . PHE D 872  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  869  PHE A CE2 
7919  C CZ  . PHE D 872  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  869  PHE A CZ  
7920  N N   . PHE D 873  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  870  PHE A N   
7921  C CA  . PHE D 873  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  870  PHE A CA  
7922  C C   . PHE D 873  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  870  PHE A C   
7923  O O   . PHE D 873  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  870  PHE A O   
7924  C CB  . PHE D 873  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  870  PHE A CB  
7925  C CG  . PHE D 873  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  870  PHE A CG  
7926  C CD1 . PHE D 873  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  870  PHE A CD1 
7927  C CD2 . PHE D 873  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  870  PHE A CD2 
7928  C CE1 . PHE D 873  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  870  PHE A CE1 
7929  C CE2 . PHE D 873  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  870  PHE A CE2 
7930  C CZ  . PHE D 873  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  870  PHE A CZ  
7931  N N   . PHE D 874  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  871  PHE A N   
7932  C CA  . PHE D 874  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  871  PHE A CA  
7933  C C   . PHE D 874  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  871  PHE A C   
7934  O O   . PHE D 874  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  871  PHE A O   
7935  C CB  . PHE D 874  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  871  PHE A CB  
7936  C CG  . PHE D 874  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  871  PHE A CG  
7937  C CD1 . PHE D 874  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  871  PHE A CD1 
7938  C CD2 . PHE D 874  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  871  PHE A CD2 
7939  C CE1 . PHE D 874  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  871  PHE A CE1 
7940  C CE2 . PHE D 874  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  871  PHE A CE2 
7941  C CZ  . PHE D 874  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  871  PHE A CZ  
7942  N N   . HIS D 875  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  872  HIS A N   
7943  C CA  . HIS D 875  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  872  HIS A CA  
7944  C C   . HIS D 875  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  872  HIS A C   
7945  O O   . HIS D 875  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  872  HIS A O   
7946  C CB  . HIS D 875  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  872  HIS A CB  
7947  C CG  . HIS D 875  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  872  HIS A CG  
7948  N ND1 . HIS D 875  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  872  HIS A ND1 
7949  C CD2 . HIS D 875  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  872  HIS A CD2 
7950  C CE1 . HIS D 875  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  872  HIS A CE1 
7951  N NE2 . HIS D 875  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  872  HIS A NE2 
7952  N N   . VAL D 876  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  873  VAL A N   
7953  C CA  . VAL D 876  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  873  VAL A CA  
7954  C C   . VAL D 876  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  873  VAL A C   
7955  O O   . VAL D 876  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  873  VAL A O   
7956  C CB  . VAL D 876  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  873  VAL A CB  
7957  C CG1 . VAL D 876  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  873  VAL A CG1 
7958  C CG2 . VAL D 876  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  873  VAL A CG2 
7959  N N   . PRO D 877  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  874  PRO A N   
7960  C CA  . PRO D 877  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  874  PRO A CA  
7961  C C   . PRO D 877  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  874  PRO A C   
7962  O O   . PRO D 877  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  874  PRO A O   
7963  C CB  . PRO D 877  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  874  PRO A CB  
7964  C CG  . PRO D 877  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  874  PRO A CG  
7965  C CD  . PRO D 877  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  874  PRO A CD  
7966  N N   . ILE D 878  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  875  ILE A N   
7967  C CA  . ILE D 878  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  875  ILE A CA  
7968  C C   . ILE D 878  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  875  ILE A C   
7969  O O   . ILE D 878  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  875  ILE A O   
7970  C CB  . ILE D 878  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  875  ILE A CB  
7971  C CG1 . ILE D 878  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  875  ILE A CG1 
7972  C CG2 . ILE D 878  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  875  ILE A CG2 
7973  C CD1 . ILE D 878  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  875  ILE A CD1 
7974  N N   . THR D 879  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  876  THR A N   
7975  C CA  . THR D 879  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  876  THR A CA  
7976  C C   . THR D 879  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  876  THR A C   
7977  O O   . THR D 879  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  876  THR A O   
7978  C CB  . THR D 879  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  876  THR A CB  
7979  O OG1 . THR D 879  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  876  THR A OG1 
7980  C CG2 . THR D 879  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  876  THR A CG2 
7981  N N   . LEU D 880  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  877  LEU A N   
7982  C CA  . LEU D 880  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  877  LEU A CA  
7983  C C   . LEU D 880  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  877  LEU A C   
7984  O O   . LEU D 880  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  877  LEU A O   
7985  C CB  . LEU D 880  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  877  LEU A CB  
7986  C CG  . LEU D 880  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  877  LEU A CG  
7987  C CD1 . LEU D 880  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  877  LEU A CD1 
7988  C CD2 . LEU D 880  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  877  LEU A CD2 
7989  N N   . ASN D 881  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  878  ASN A N   
7990  C CA  . ASN D 881  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  878  ASN A CA  
7991  C C   . ASN D 881  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  878  ASN A C   
7992  O O   . ASN D 881  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  878  ASN A O   
7993  C CB  . ASN D 881  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  878  ASN A CB  
7994  C CG  . ASN D 881  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  878  ASN A CG  
7995  O OD1 . ASN D 881  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  878  ASN A OD1 
7996  N ND2 . ASN D 881  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  878  ASN A ND2 
7997  N N   . TYR D 882  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  879  TYR A N   
7998  C CA  . TYR D 882  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  879  TYR A CA  
7999  C C   . TYR D 882  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  879  TYR A C   
8000  O O   . TYR D 882  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  879  TYR A O   
8001  C CB  . TYR D 882  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  879  TYR A CB  
8002  C CG  . TYR D 882  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  879  TYR A CG  
8003  C CD1 . TYR D 882  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  879  TYR A CD1 
8004  C CD2 . TYR D 882  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  879  TYR A CD2 
8005  C CE1 . TYR D 882  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  879  TYR A CE1 
8006  C CE2 . TYR D 882  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  879  TYR A CE2 
8007  C CZ  . TYR D 882  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  879  TYR A CZ  
8008  O OH  . TYR D 882  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  879  TYR A OH  
8009  N N   . GLN D 883  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  880  GLN A N   
8010  C CA  . GLN D 883  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  880  GLN A CA  
8011  C C   . GLN D 883  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  880  GLN A C   
8012  O O   . GLN D 883  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  880  GLN A O   
8013  C CB  . GLN D 883  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  880  GLN A CB  
8014  C CG  . GLN D 883  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  880  GLN A CG  
8015  C CD  . GLN D 883  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  880  GLN A CD  
8016  O OE1 . GLN D 883  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  880  GLN A OE1 
8017  N NE2 . GLN D 883  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  880  GLN A NE2 
8018  N N   . ALA D 884  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  881  ALA A N   
8019  C CA  . ALA D 884  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  881  ALA A CA  
8020  C C   . ALA D 884  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  881  ALA A C   
8021  O O   . ALA D 884  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  881  ALA A O   
8022  C CB  . ALA D 884  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  881  ALA A CB  
8023  N N   . ALA D 885  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  882  ALA A N   
8024  C CA  . ALA D 885  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  882  ALA A CA  
8025  C C   . ALA D 885  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  882  ALA A C   
8026  O O   . ALA D 885  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  882  ALA A O   
8027  C CB  . ALA D 885  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  882  ALA A CB  
8028  N N   . ASN D 886  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  883  ASN A N   
8029  C CA  . ASN D 886  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  883  ASN A CA  
8030  C C   . ASN D 886  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  883  ASN A C   
8031  O O   . ASN D 886  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  883  ASN A O   
8032  C CB  . ASN D 886  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  883  ASN A CB  
8033  C CG  . ASN D 886  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  883  ASN A CG  
8034  O OD1 . ASN D 886  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  883  ASN A OD1 
8035  N ND2 . ASN D 886  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  883  ASN A ND2 
8036  N N   . SER D 887  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  884  SER A N   
8037  C CA  . SER D 887  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  884  SER A CA  
8038  C C   . SER D 887  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  884  SER A C   
8039  O O   . SER D 887  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  884  SER A O   
8040  C CB  . SER D 887  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  884  SER A CB  
8041  O OG  . SER D 887  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  884  SER A OG  
8042  N N   . PRO D 888  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  885  PRO A N   
8043  C CA  . PRO D 888  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  885  PRO A CA  
8044  C C   . PRO D 888  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  885  PRO A C   
8045  O O   . PRO D 888  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  885  PRO A O   
8046  C CB  . PRO D 888  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  885  PRO A CB  
8047  C CG  . PRO D 888  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  885  PRO A CG  
8048  C CD  . PRO D 888  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  885  PRO A CD  
8049  N N   . SER D 889  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  886  SER A N   
8050  C CA  . SER D 889  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  886  SER A CA  
8051  C C   . SER D 889  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  886  SER A C   
8052  O O   . SER D 889  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  886  SER A O   
8053  C CB  . SER D 889  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  886  SER A CB  
8054  O OG  . SER D 889  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  886  SER A OG  
8055  N N   . LYS D 890  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  887  LYS A N   
8056  C CA  . LYS D 890  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  887  LYS A CA  
8057  C C   . LYS D 890  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  887  LYS A C   
8058  O O   . LYS D 890  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  887  LYS A O   
8059  C CB  . LYS D 890  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  887  LYS A CB  
8060  C CG  . LYS D 890  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  887  LYS A CG  
8061  C CD  . LYS D 890  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  887  LYS A CD  
8062  C CE  . LYS D 890  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  887  LYS A CE  
8063  N NZ  . LYS D 890  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  887  LYS A NZ  
8064  N N   . PHE D 891  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  888  PHE A N   
8065  C CA  . PHE D 891  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  888  PHE A CA  
8066  C C   . PHE D 891  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  888  PHE A C   
8067  O O   . PHE D 891  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  888  PHE A O   
8068  C CB  . PHE D 891  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  888  PHE A CB  
8069  C CG  . PHE D 891  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  888  PHE A CG  
8070  C CD1 . PHE D 891  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  888  PHE A CD1 
8071  C CD2 . PHE D 891  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  888  PHE A CD2 
8072  C CE1 . PHE D 891  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  888  PHE A CE1 
8073  C CE2 . PHE D 891  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  888  PHE A CE2 
8074  C CZ  . PHE D 891  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  888  PHE A CZ  
8075  N N   . ASN D 892  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  889  ASN A N   
8076  C CA  . ASN D 892  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  889  ASN A CA  
8077  C C   . ASN D 892  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  889  ASN A C   
8078  O O   . ASN D 892  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  889  ASN A O   
8079  C CB  . ASN D 892  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  889  ASN A CB  
8080  C CG  . ASN D 892  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  889  ASN A CG  
8081  O OD1 . ASN D 892  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  889  ASN A OD1 
8082  N ND2 . ASN D 892  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  889  ASN A ND2 
8083  N N   . GLN D 893  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  890  GLN A N   
8084  C CA  . GLN D 893  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  890  GLN A CA  
8085  C C   . GLN D 893  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  890  GLN A C   
8086  O O   . GLN D 893  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  890  GLN A O   
8087  C CB  . GLN D 893  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  890  GLN A CB  
8088  C CG  . GLN D 893  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  890  GLN A CG  
8089  C CD  . GLN D 893  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  890  GLN A CD  
8090  O OE1 . GLN D 893  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  890  GLN A OE1 
8091  N NE2 . GLN D 893  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  890  GLN A NE2 
8092  N N   . ARG D 894  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  891  ARG A N   
8093  C CA  . ARG D 894  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  891  ARG A CA  
8094  C C   . ARG D 894  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  891  ARG A C   
8095  O O   . ARG D 894  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  891  ARG A O   
8096  C CB  . ARG D 894  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  891  ARG A CB  
8097  C CG  . ARG D 894  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  891  ARG A CG  
8098  C CD  . ARG D 894  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  891  ARG A CD  
8099  N NE  . ARG D 894  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  891  ARG A NE  
8100  C CZ  . ARG D 894  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  891  ARG A CZ  
8101  N NH1 . ARG D 894  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  891  ARG A NH1 
8102  N NH2 . ARG D 894  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  891  ARG A NH2 
8103  N N   . VAL D 895  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  892  VAL A N   
8104  C CA  . VAL D 895  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  892  VAL A CA  
8105  C C   . VAL D 895  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  892  VAL A C   
8106  O O   . VAL D 895  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  892  VAL A O   
8107  C CB  . VAL D 895  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  892  VAL A CB  
8108  C CG1 . VAL D 895  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  892  VAL A CG1 
8109  C CG2 . VAL D 895  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  892  VAL A CG2 
8110  N N   . ASN D 896  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  893  ASN A N   
8111  C CA  . ASN D 896  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  893  ASN A CA  
8112  C C   . ASN D 896  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  893  ASN A C   
8113  O O   . ASN D 896  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  893  ASN A O   
8114  C CB  . ASN D 896  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  893  ASN A CB  
8115  C CG  . ASN D 896  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  893  ASN A CG  
8116  O OD1 . ASN D 896  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  893  ASN A OD1 
8117  N ND2 . ASN D 896  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  893  ASN A ND2 
8118  N N   . ALA D 897  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  894  ALA A N   
8119  C CA  . ALA D 897  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  894  ALA A CA  
8120  C C   . ALA D 897  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  894  ALA A C   
8121  O O   . ALA D 897  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  894  ALA A O   
8122  C CB  . ALA D 897  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  894  ALA A CB  
8123  N N   . TYR D 898  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  895  TYR A N   
8124  C CA  . TYR D 898  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  895  TYR A CA  
8125  C C   . TYR D 898  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  895  TYR A C   
8126  O O   . TYR D 898  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  895  TYR A O   
8127  C CB  . TYR D 898  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  895  TYR A CB  
8128  C CG  . TYR D 898  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  895  TYR A CG  
8129  C CD1 . TYR D 898  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  895  TYR A CD1 
8130  C CD2 . TYR D 898  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  895  TYR A CD2 
8131  C CE1 . TYR D 898  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  895  TYR A CE1 
8132  C CE2 . TYR D 898  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  895  TYR A CE2 
8133  C CZ  . TYR D 898  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  895  TYR A CZ  
8134  O OH  . TYR D 898  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  895  TYR A OH  
8135  N N   . LEU D 899  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  896  LEU A N   
8136  C CA  . LEU D 899  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  896  LEU A CA  
8137  C C   . LEU D 899  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  896  LEU A C   
8138  O O   . LEU D 899  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  896  LEU A O   
8139  C CB  . LEU D 899  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  896  LEU A CB  
8140  C CG  . LEU D 899  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  896  LEU A CG  
8141  C CD1 . LEU D 899  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  896  LEU A CD1 
8142  C CD2 . LEU D 899  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  896  LEU A CD2 
8143  N N   . LYS D 900  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  897  LYS A N   
8144  C CA  . LYS D 900  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  897  LYS A CA  
8145  C C   . LYS D 900  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  897  LYS A C   
8146  O O   . LYS D 900  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  897  LYS A O   
8147  C CB  . LYS D 900  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  897  LYS A CB  
8148  C CG  . LYS D 900  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  897  LYS A CG  
8149  C CD  . LYS D 900  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  897  LYS A CD  
8150  C CE  . LYS D 900  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  897  LYS A CE  
8151  N NZ  . LYS D 900  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  897  LYS A NZ  
8152  N N   . GLU D 901  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  898  GLU A N   
8153  C CA  . GLU D 901  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  898  GLU A CA  
8154  C C   . GLU D 901  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  898  GLU A C   
8155  O O   . GLU D 901  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  898  GLU A O   
8156  C CB  . GLU D 901  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  898  GLU A CB  
8157  C CG  . GLU D 901  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  898  GLU A CG  
8158  C CD  . GLU D 901  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  898  GLU A CD  
8159  O OE1 . GLU D 901  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  898  GLU A OE1 
8160  O OE2 . GLU D 901  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  898  GLU A OE2 
8161  N N   . HIS D 902  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  899  HIS A N   
8162  C CA  . HIS D 902  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  899  HIS A CA  
8163  C C   . HIS D 902  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  899  HIS A C   
8164  O O   . HIS D 902  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  899  HIS A O   
8165  C CB  . HIS D 902  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  899  HIS A CB  
8166  C CG  . HIS D 902  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  899  HIS A CG  
8167  N ND1 . HIS D 902  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  899  HIS A ND1 
8168  C CD2 . HIS D 902  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  899  HIS A CD2 
8169  C CE1 . HIS D 902  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  899  HIS A CE1 
8170  N NE2 . HIS D 902  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  899  HIS A NE2 
8171  N N   . PRO D 903  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  900  PRO A N   
8172  C CA  . PRO D 903  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  900  PRO A CA  
8173  C C   . PRO D 903  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  900  PRO A C   
8174  O O   . PRO D 903  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  900  PRO A O   
8175  C CB  . PRO D 903  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  900  PRO A CB  
8176  C CG  . PRO D 903  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  900  PRO A CG  
8177  C CD  . PRO D 903  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  900  PRO A CD  
8178  N N   . GLU D 904  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  901  GLU A N   
8179  C CA  . GLU D 904  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  901  GLU A CA  
8180  C C   . GLU D 904  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  901  GLU A C   
8181  O O   . GLU D 904  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  901  GLU A O   
8182  C CB  . GLU D 904  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  901  GLU A CB  
8183  C CG  . GLU D 904  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  901  GLU A CG  
8184  C CD  . GLU D 904  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  901  GLU A CD  
8185  O OE1 . GLU D 904  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  901  GLU A OE1 
8186  O OE2 . GLU D 904  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  901  GLU A OE2 
8187  N N   . THR D 905  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  902  THR A N   
8188  C CA  . THR D 905  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  902  THR A CA  
8189  C C   . THR D 905  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  902  THR A C   
8190  O O   . THR D 905  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  902  THR A O   
8191  C CB  . THR D 905  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  902  THR A CB  
8192  O OG1 . THR D 905  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  902  THR A OG1 
8193  C CG2 . THR D 905  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  902  THR A CG2 
8194  N N   . PRO D 906  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  903  PRO A N   
8195  C CA  . PRO D 906  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  903  PRO A CA  
8196  C C   . PRO D 906  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  903  PRO A C   
8197  O O   . PRO D 906  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  903  PRO A O   
8198  C CB  . PRO D 906  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  903  PRO A CB  
8199  C CG  . PRO D 906  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  903  PRO A CG  
8200  C CD  . PRO D 906  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  903  PRO A CD  
8201  N N   . ILE D 907  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  904  ILE A N   
8202  C CA  . ILE D 907  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  904  ILE A CA  
8203  C C   . ILE D 907  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  904  ILE A C   
8204  O O   . ILE D 907  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  904  ILE A O   
8205  C CB  . ILE D 907  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  904  ILE A CB  
8206  C CG1 . ILE D 907  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  904  ILE A CG1 
8207  C CG2 . ILE D 907  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  904  ILE A CG2 
8208  C CD1 . ILE D 907  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  904  ILE A CD1 
8209  N N   . ILE D 908  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  905  ILE A N   
8210  C CA  . ILE D 908  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  905  ILE A CA  
8211  C C   . ILE D 908  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  905  ILE A C   
8212  O O   . ILE D 908  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  905  ILE A O   
8213  C CB  . ILE D 908  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  905  ILE A CB  
8214  C CG1 . ILE D 908  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  905  ILE A CG1 
8215  C CG2 . ILE D 908  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  905  ILE A CG2 
8216  C CD1 . ILE D 908  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  905  ILE A CD1 
8217  N N   . GLY D 909  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  906  GLY A N   
8218  C CA  . GLY D 909  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  906  GLY A CA  
8219  C C   . GLY D 909  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  906  GLY A C   
8220  O O   . GLY D 909  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  906  GLY A O   
8221  N N   . ILE D 910  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  907  ILE A N   
8222  C CA  . ILE D 910  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  907  ILE A CA  
8223  C C   . ILE D 910  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  907  ILE A C   
8224  O O   . ILE D 910  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  907  ILE A O   
8225  C CB  . ILE D 910  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  907  ILE A CB  
8226  C CG1 . ILE D 910  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  907  ILE A CG1 
8227  C CG2 . ILE D 910  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  907  ILE A CG2 
8228  C CD1 . ILE D 910  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  907  ILE A CD1 
8229  N N   . ASP D 911  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  908  ASP A N   
8230  C CA  . ASP D 911  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  908  ASP A CA  
8231  C C   . ASP D 911  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  908  ASP A C   
8232  O O   . ASP D 911  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  908  ASP A O   
8233  C CB  . ASP D 911  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  908  ASP A CB  
8234  C CG  . ASP D 911  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  908  ASP A CG  
8235  O OD1 . ASP D 911  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  908  ASP A OD1 
8236  O OD2 . ASP D 911  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  908  ASP A OD2 
8237  N N   . ARG D 912  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  909  ARG A N   
8238  C CA  . ARG D 912  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  909  ARG A CA  
8239  C C   . ARG D 912  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  909  ARG A C   
8240  O O   . ARG D 912  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  909  ARG A O   
8241  C CB  . ARG D 912  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  909  ARG A CB  
8242  C CG  . ARG D 912  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  909  ARG A CG  
8243  C CD  . ARG D 912  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  909  ARG A CD  
8244  N NE  . ARG D 912  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  909  ARG A NE  
8245  C CZ  . ARG D 912  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  909  ARG A CZ  
8246  N NH1 . ARG D 912  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  909  ARG A NH1 
8247  N NH2 . ARG D 912  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  909  ARG A NH2 
8248  N N   . GLY D 913  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  910  GLY A N   
8249  C CA  . GLY D 913  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  910  GLY A CA  
8250  C C   . GLY D 913  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  910  GLY A C   
8251  O O   . GLY D 913  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  910  GLY A O   
8252  N N   . GLU D 914  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  911  GLU A N   
8253  C CA  . GLU D 914  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  911  GLU A CA  
8254  C C   . GLU D 914  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  911  GLU A C   
8255  O O   . GLU D 914  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  911  GLU A O   
8256  C CB  . GLU D 914  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  911  GLU A CB  
8257  C CG  . GLU D 914  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  911  GLU A CG  
8258  C CD  . GLU D 914  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  911  GLU A CD  
8259  O OE1 . GLU D 914  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  911  GLU A OE1 
8260  O OE2 . GLU D 914  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  911  GLU A OE2 
8261  N N   . ARG D 915  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  912  ARG A N   
8262  C CA  . ARG D 915  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  912  ARG A CA  
8263  C C   . ARG D 915  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  912  ARG A C   
8264  O O   . ARG D 915  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  912  ARG A O   
8265  C CB  . ARG D 915  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  912  ARG A CB  
8266  C CG  . ARG D 915  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  912  ARG A CG  
8267  C CD  . ARG D 915  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  912  ARG A CD  
8268  N NE  . ARG D 915  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  912  ARG A NE  
8269  C CZ  . ARG D 915  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  912  ARG A CZ  
8270  N NH1 . ARG D 915  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  912  ARG A NH1 
8271  N NH2 . ARG D 915  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  912  ARG A NH2 
8272  N N   . ASN D 916  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  913  ASN A N   
8273  C CA  . ASN D 916  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  913  ASN A CA  
8274  C C   . ASN D 916  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  913  ASN A C   
8275  O O   . ASN D 916  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  913  ASN A O   
8276  C CB  . ASN D 916  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  913  ASN A CB  
8277  C CG  . ASN D 916  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  913  ASN A CG  
8278  O OD1 . ASN D 916  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  913  ASN A OD1 
8279  N ND2 . ASN D 916  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  913  ASN A ND2 
8280  N N   . LEU D 917  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  914  LEU A N   
8281  C CA  . LEU D 917  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  914  LEU A CA  
8282  C C   . LEU D 917  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  914  LEU A C   
8283  O O   . LEU D 917  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  914  LEU A O   
8284  C CB  . LEU D 917  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  914  LEU A CB  
8285  C CG  . LEU D 917  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  914  LEU A CG  
8286  C CD1 . LEU D 917  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  914  LEU A CD1 
8287  C CD2 . LEU D 917  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  914  LEU A CD2 
8288  N N   . ILE D 918  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  915  ILE A N   
8289  C CA  . ILE D 918  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  915  ILE A CA  
8290  C C   . ILE D 918  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  915  ILE A C   
8291  O O   . ILE D 918  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  915  ILE A O   
8292  C CB  . ILE D 918  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  915  ILE A CB  
8293  C CG1 . ILE D 918  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  915  ILE A CG1 
8294  C CG2 . ILE D 918  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  915  ILE A CG2 
8295  C CD1 . ILE D 918  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  915  ILE A CD1 
8296  N N   . TYR D 919  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  916  TYR A N   
8297  C CA  . TYR D 919  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  916  TYR A CA  
8298  C C   . TYR D 919  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  916  TYR A C   
8299  O O   . TYR D 919  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  916  TYR A O   
8300  C CB  . TYR D 919  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  916  TYR A CB  
8301  C CG  . TYR D 919  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  916  TYR A CG  
8302  C CD1 . TYR D 919  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  916  TYR A CD1 
8303  C CD2 . TYR D 919  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  916  TYR A CD2 
8304  C CE1 . TYR D 919  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  916  TYR A CE1 
8305  C CE2 . TYR D 919  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  916  TYR A CE2 
8306  C CZ  . TYR D 919  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  916  TYR A CZ  
8307  O OH  . TYR D 919  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  916  TYR A OH  
8308  N N   . ILE D 920  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  917  ILE A N   
8309  C CA  . ILE D 920  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  917  ILE A CA  
8310  C C   . ILE D 920  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  917  ILE A C   
8311  O O   . ILE D 920  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  917  ILE A O   
8312  C CB  . ILE D 920  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  917  ILE A CB  
8313  C CG1 . ILE D 920  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  917  ILE A CG1 
8314  C CG2 . ILE D 920  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  917  ILE A CG2 
8315  C CD1 . ILE D 920  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  917  ILE A CD1 
8316  N N   . THR D 921  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  918  THR A N   
8317  C CA  . THR D 921  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  918  THR A CA  
8318  C C   . THR D 921  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  918  THR A C   
8319  O O   . THR D 921  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  918  THR A O   
8320  C CB  . THR D 921  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  918  THR A CB  
8321  O OG1 . THR D 921  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  918  THR A OG1 
8322  C CG2 . THR D 921  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  918  THR A CG2 
8323  N N   . VAL D 922  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  919  VAL A N   
8324  C CA  . VAL D 922  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  919  VAL A CA  
8325  C C   . VAL D 922  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  919  VAL A C   
8326  O O   . VAL D 922  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  919  VAL A O   
8327  C CB  . VAL D 922  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  919  VAL A CB  
8328  C CG1 . VAL D 922  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  919  VAL A CG1 
8329  C CG2 . VAL D 922  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  919  VAL A CG2 
8330  N N   . ILE D 923  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  920  ILE A N   
8331  C CA  . ILE D 923  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  920  ILE A CA  
8332  C C   . ILE D 923  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  920  ILE A C   
8333  O O   . ILE D 923  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  920  ILE A O   
8334  C CB  . ILE D 923  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  920  ILE A CB  
8335  C CG1 . ILE D 923  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  920  ILE A CG1 
8336  C CG2 . ILE D 923  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  920  ILE A CG2 
8337  C CD1 . ILE D 923  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  920  ILE A CD1 
8338  N N   . ASP D 924  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  921  ASP A N   
8339  C CA  . ASP D 924  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  921  ASP A CA  
8340  C C   . ASP D 924  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  921  ASP A C   
8341  O O   . ASP D 924  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  921  ASP A O   
8342  C CB  . ASP D 924  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  921  ASP A CB  
8343  C CG  . ASP D 924  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  921  ASP A CG  
8344  O OD1 . ASP D 924  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  921  ASP A OD1 
8345  O OD2 . ASP D 924  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  921  ASP A OD2 
8346  N N   . SER D 925  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  922  SER A N   
8347  C CA  . SER D 925  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  922  SER A CA  
8348  C C   . SER D 925  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  922  SER A C   
8349  O O   . SER D 925  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  922  SER A O   
8350  C CB  . SER D 925  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  922  SER A CB  
8351  O OG  . SER D 925  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  922  SER A OG  
8352  N N   . THR D 926  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  923  THR A N   
8353  C CA  . THR D 926  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  923  THR A CA  
8354  C C   . THR D 926  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  923  THR A C   
8355  O O   . THR D 926  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  923  THR A O   
8356  C CB  . THR D 926  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  923  THR A CB  
8357  O OG1 . THR D 926  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  923  THR A OG1 
8358  C CG2 . THR D 926  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  923  THR A CG2 
8359  N N   . GLY D 927  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  924  GLY A N   
8360  C CA  . GLY D 927  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  924  GLY A CA  
8361  C C   . GLY D 927  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  924  GLY A C   
8362  O O   . GLY D 927  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  924  GLY A O   
8363  N N   . LYS D 928  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  925  LYS A N   
8364  C CA  . LYS D 928  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  925  LYS A CA  
8365  C C   . LYS D 928  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  925  LYS A C   
8366  O O   . LYS D 928  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  925  LYS A O   
8372  N N   . ILE D 929  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  926  ILE A N   
8373  C CA  . ILE D 929  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  926  ILE A CA  
8374  C C   . ILE D 929  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  926  ILE A C   
8375  O O   . ILE D 929  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  926  ILE A O   
8376  C CB  . ILE D 929  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  926  ILE A CB  
8377  C CG1 . ILE D 929  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  926  ILE A CG1 
8378  C CG2 . ILE D 929  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  926  ILE A CG2 
8379  C CD1 . ILE D 929  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  926  ILE A CD1 
8380  N N   . LEU D 930  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  927  LEU A N   
8381  C CA  . LEU D 930  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  927  LEU A CA  
8382  C C   . LEU D 930  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  927  LEU A C   
8383  O O   . LEU D 930  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  927  LEU A O   
8384  C CB  . LEU D 930  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  927  LEU A CB  
8385  C CG  . LEU D 930  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  927  LEU A CG  
8386  C CD1 . LEU D 930  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  927  LEU A CD1 
8387  C CD2 . LEU D 930  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  927  LEU A CD2 
8388  N N   . GLU D 931  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  928  GLU A N   
8389  C CA  . GLU D 931  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  928  GLU A CA  
8390  C C   . GLU D 931  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  928  GLU A C   
8391  O O   . GLU D 931  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  928  GLU A O   
8392  C CB  . GLU D 931  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  928  GLU A CB  
8393  C CG  . GLU D 931  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  928  GLU A CG  
8394  C CD  . GLU D 931  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  928  GLU A CD  
8395  O OE1 . GLU D 931  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  928  GLU A OE1 
8396  O OE2 . GLU D 931  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  928  GLU A OE2 
8397  N N   . GLN D 932  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  929  GLN A N   
8398  C CA  . GLN D 932  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  929  GLN A CA  
8399  C C   . GLN D 932  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  929  GLN A C   
8400  O O   . GLN D 932  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  929  GLN A O   
8401  C CB  . GLN D 932  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  929  GLN A CB  
8402  C CG  . GLN D 932  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  929  GLN A CG  
8403  C CD  . GLN D 932  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  929  GLN A CD  
8404  O OE1 . GLN D 932  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  929  GLN A OE1 
8405  N NE2 . GLN D 932  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  929  GLN A NE2 
8406  N N   . ARG D 933  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  930  ARG A N   
8407  C CA  . ARG D 933  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  930  ARG A CA  
8408  C C   . ARG D 933  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  930  ARG A C   
8409  O O   . ARG D 933  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  930  ARG A O   
8410  C CB  . ARG D 933  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  930  ARG A CB  
8411  C CG  . ARG D 933  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  930  ARG A CG  
8412  C CD  . ARG D 933  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  930  ARG A CD  
8413  N NE  . ARG D 933  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  930  ARG A NE  
8414  C CZ  . ARG D 933  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  930  ARG A CZ  
8415  N NH1 . ARG D 933  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  930  ARG A NH1 
8416  N NH2 . ARG D 933  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  930  ARG A NH2 
8417  N N   . SER D 934  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  931  SER A N   
8418  C CA  . SER D 934  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  931  SER A CA  
8419  C C   . SER D 934  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  931  SER A C   
8420  O O   . SER D 934  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  931  SER A O   
8421  C CB  . SER D 934  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  931  SER A CB  
8422  O OG  . SER D 934  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  931  SER A OG  
8423  N N   . LEU D 935  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  932  LEU A N   
8424  C CA  . LEU D 935  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  932  LEU A CA  
8425  C C   . LEU D 935  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  932  LEU A C   
8426  O O   . LEU D 935  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  932  LEU A O   
8427  C CB  . LEU D 935  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  932  LEU A CB  
8428  C CG  . LEU D 935  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  932  LEU A CG  
8429  C CD1 . LEU D 935  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  932  LEU A CD1 
8430  C CD2 . LEU D 935  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  932  LEU A CD2 
8431  N N   . ASN D 936  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  933  ASN A N   
8432  C CA  . ASN D 936  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  933  ASN A CA  
8433  C C   . ASN D 936  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  933  ASN A C   
8434  O O   . ASN D 936  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  933  ASN A O   
8435  C CB  . ASN D 936  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  933  ASN A CB  
8436  C CG  . ASN D 936  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  933  ASN A CG  
8437  O OD1 . ASN D 936  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  933  ASN A OD1 
8438  N ND2 . ASN D 936  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  933  ASN A ND2 
8439  N N   . THR D 937  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  934  THR A N   
8440  C CA  . THR D 937  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  934  THR A CA  
8441  C C   . THR D 937  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  934  THR A C   
8442  O O   . THR D 937  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  934  THR A O   
8443  C CB  . THR D 937  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  934  THR A CB  
8444  O OG1 . THR D 937  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  934  THR A OG1 
8445  C CG2 . THR D 937  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  934  THR A CG2 
8446  N N   . ILE D 938  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  935  ILE A N   
8447  C CA  . ILE D 938  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  935  ILE A CA  
8448  C C   . ILE D 938  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  935  ILE A C   
8449  O O   . ILE D 938  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  935  ILE A O   
8450  C CB  . ILE D 938  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  935  ILE A CB  
8451  C CG1 . ILE D 938  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  935  ILE A CG1 
8452  C CG2 . ILE D 938  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  935  ILE A CG2 
8453  C CD1 . ILE D 938  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  935  ILE A CD1 
8454  N N   . GLN D 939  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  936  GLN A N   
8455  C CA  . GLN D 939  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  936  GLN A CA  
8456  C C   . GLN D 939  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  936  GLN A C   
8457  O O   . GLN D 939  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  936  GLN A O   
8458  C CB  . GLN D 939  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  936  GLN A CB  
8459  C CG  . GLN D 939  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  936  GLN A CG  
8460  C CD  . GLN D 939  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  936  GLN A CD  
8461  O OE1 . GLN D 939  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  936  GLN A OE1 
8462  N NE2 . GLN D 939  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  936  GLN A NE2 
8463  N N   . GLN D 940  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  937  GLN A N   
8464  C CA  . GLN D 940  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  937  GLN A CA  
8465  C C   . GLN D 940  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  937  GLN A C   
8466  O O   . GLN D 940  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  937  GLN A O   
8472  N N   . PHE D 941  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  938  PHE A N   
8473  C CA  . PHE D 941  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  938  PHE A CA  
8474  C C   . PHE D 941  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  938  PHE A C   
8475  O O   . PHE D 941  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  938  PHE A O   
8476  C CB  . PHE D 941  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  938  PHE A CB  
8477  C CG  . PHE D 941  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  938  PHE A CG  
8478  C CD1 . PHE D 941  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  938  PHE A CD1 
8479  C CD2 . PHE D 941  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  938  PHE A CD2 
8480  C CE1 . PHE D 941  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  938  PHE A CE1 
8481  C CE2 . PHE D 941  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  938  PHE A CE2 
8482  C CZ  . PHE D 941  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  938  PHE A CZ  
8483  N N   . ASP D 942  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  939  ASP A N   
8484  C CA  . ASP D 942  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  939  ASP A CA  
8485  C C   . ASP D 942  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  939  ASP A C   
8486  O O   . ASP D 942  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  939  ASP A O   
8487  C CB  . ASP D 942  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  939  ASP A CB  
8488  C CG  . ASP D 942  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  939  ASP A CG  
8489  O OD1 . ASP D 942  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  939  ASP A OD1 
8490  O OD2 . ASP D 942  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  939  ASP A OD2 
8491  N N   . TYR D 943  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  940  TYR A N   
8492  C CA  . TYR D 943  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  940  TYR A CA  
8493  C C   . TYR D 943  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  940  TYR A C   
8494  O O   . TYR D 943  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  940  TYR A O   
8495  C CB  . TYR D 943  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  940  TYR A CB  
8496  C CG  . TYR D 943  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  940  TYR A CG  
8497  C CD1 . TYR D 943  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  940  TYR A CD1 
8498  C CD2 . TYR D 943  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  940  TYR A CD2 
8499  C CE1 . TYR D 943  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  940  TYR A CE1 
8500  C CE2 . TYR D 943  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  940  TYR A CE2 
8501  C CZ  . TYR D 943  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  940  TYR A CZ  
8502  O OH  . TYR D 943  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  940  TYR A OH  
8503  N N   . GLN D 944  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  941  GLN A N   
8504  C CA  . GLN D 944  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  941  GLN A CA  
8505  C C   . GLN D 944  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  941  GLN A C   
8506  O O   . GLN D 944  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  941  GLN A O   
8507  C CB  . GLN D 944  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  941  GLN A CB  
8508  C CG  . GLN D 944  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  941  GLN A CG  
8509  C CD  . GLN D 944  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  941  GLN A CD  
8510  O OE1 . GLN D 944  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  941  GLN A OE1 
8511  N NE2 . GLN D 944  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  941  GLN A NE2 
8512  N N   . LYS D 945  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  942  LYS A N   
8513  C CA  . LYS D 945  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  942  LYS A CA  
8514  C C   . LYS D 945  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  942  LYS A C   
8515  O O   . LYS D 945  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  942  LYS A O   
8521  N N   . LYS D 946  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  943  LYS A N   
8522  C CA  . LYS D 946  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  943  LYS A CA  
8523  C C   . LYS D 946  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  943  LYS A C   
8524  O O   . LYS D 946  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  943  LYS A O   
8525  C CB  . LYS D 946  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  943  LYS A CB  
8526  C CG  . LYS D 946  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  943  LYS A CG  
8527  C CD  . LYS D 946  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  943  LYS A CD  
8528  C CE  . LYS D 946  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  943  LYS A CE  
8529  N NZ  . LYS D 946  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  943  LYS A NZ  
8530  N N   . LEU D 947  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  944  LEU A N   
8531  C CA  . LEU D 947  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  944  LEU A CA  
8532  C C   . LEU D 947  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  944  LEU A C   
8533  O O   . LEU D 947  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  944  LEU A O   
8534  C CB  . LEU D 947  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  944  LEU A CB  
8535  C CG  . LEU D 947  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  944  LEU A CG  
8536  C CD1 . LEU D 947  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  944  LEU A CD1 
8537  C CD2 . LEU D 947  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  944  LEU A CD2 
8538  N N   . ASP D 948  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  945  ASP A N   
8539  C CA  . ASP D 948  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  945  ASP A CA  
8540  C C   . ASP D 948  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  945  ASP A C   
8541  O O   . ASP D 948  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  945  ASP A O   
8542  C CB  . ASP D 948  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  945  ASP A CB  
8543  C CG  . ASP D 948  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  945  ASP A CG  
8544  O OD1 . ASP D 948  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  945  ASP A OD1 
8545  O OD2 . ASP D 948  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  945  ASP A OD2 
8546  N N   . ASN D 949  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  946  ASN A N   
8547  C CA  . ASN D 949  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  946  ASN A CA  
8548  C C   . ASN D 949  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  946  ASN A C   
8549  O O   . ASN D 949  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  946  ASN A O   
8550  C CB  . ASN D 949  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  946  ASN A CB  
8551  C CG  . ASN D 949  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  946  ASN A CG  
8552  O OD1 . ASN D 949  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  946  ASN A OD1 
8553  N ND2 . ASN D 949  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  946  ASN A ND2 
8554  N N   . ARG D 950  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  947  ARG A N   
8555  C CA  . ARG D 950  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  947  ARG A CA  
8556  C C   . ARG D 950  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  947  ARG A C   
8557  O O   . ARG D 950  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  947  ARG A O   
8558  C CB  . ARG D 950  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  947  ARG A CB  
8559  C CG  . ARG D 950  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  947  ARG A CG  
8560  C CD  . ARG D 950  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  947  ARG A CD  
8561  N NE  . ARG D 950  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  947  ARG A NE  
8562  C CZ  . ARG D 950  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  947  ARG A CZ  
8563  N NH1 . ARG D 950  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  947  ARG A NH1 
8564  N NH2 . ARG D 950  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  947  ARG A NH2 
8565  N N   . GLU D 951  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  948  GLU A N   
8566  C CA  . GLU D 951  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  948  GLU A CA  
8567  C C   . GLU D 951  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  948  GLU A C   
8568  O O   . GLU D 951  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  948  GLU A O   
8569  C CB  . GLU D 951  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  948  GLU A CB  
8570  C CG  . GLU D 951  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  948  GLU A CG  
8571  C CD  . GLU D 951  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  948  GLU A CD  
8572  O OE1 . GLU D 951  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  948  GLU A OE1 
8573  O OE2 . GLU D 951  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  948  GLU A OE2 
8574  N N   . LYS D 952  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  949  LYS A N   
8575  C CA  . LYS D 952  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  949  LYS A CA  
8576  C C   . LYS D 952  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  949  LYS A C   
8577  O O   . LYS D 952  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  949  LYS A O   
8578  C CB  . LYS D 952  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  949  LYS A CB  
8579  C CG  . LYS D 952  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  949  LYS A CG  
8580  C CD  . LYS D 952  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  949  LYS A CD  
8581  C CE  . LYS D 952  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  949  LYS A CE  
8582  N NZ  . LYS D 952  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  949  LYS A NZ  
8583  N N   . GLU D 953  ? 0.6508 0.6508 0.6508 0.0000  0.0000  0.0000  950  GLU A N   
8584  C CA  . GLU D 953  ? 0.6508 0.6508 0.6508 0.0000  0.0000  0.0000  950  GLU A CA  
8585  C C   . GLU D 953  ? 0.6508 0.6508 0.6508 0.0000  0.0000  0.0000  950  GLU A C   
8586  O O   . GLU D 953  ? 0.6508 0.6508 0.6508 0.0000  0.0000  0.0000  950  GLU A O   
8587  C CB  . GLU D 953  ? 0.6508 0.6508 0.6508 0.0000  0.0000  0.0000  950  GLU A CB  
8588  C CG  . GLU D 953  ? 0.6508 0.6508 0.6508 0.0000  0.0000  0.0000  950  GLU A CG  
8589  C CD  . GLU D 953  ? 0.6508 0.6508 0.6508 0.0000  0.0000  0.0000  950  GLU A CD  
8590  O OE1 . GLU D 953  ? 0.6508 0.6508 0.6508 0.0000  0.0000  0.0000  950  GLU A OE1 
8591  O OE2 . GLU D 953  ? 0.6508 0.6508 0.6508 0.0000  0.0000  0.0000  950  GLU A OE2 
8592  N N   . ARG D 954  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  951  ARG A N   
8593  C CA  . ARG D 954  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  951  ARG A CA  
8594  C C   . ARG D 954  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  951  ARG A C   
8595  O O   . ARG D 954  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  951  ARG A O   
8596  C CB  . ARG D 954  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  951  ARG A CB  
8597  C CG  . ARG D 954  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  951  ARG A CG  
8598  C CD  . ARG D 954  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  951  ARG A CD  
8599  N NE  . ARG D 954  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  951  ARG A NE  
8600  C CZ  . ARG D 954  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  951  ARG A CZ  
8601  N NH1 . ARG D 954  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  951  ARG A NH1 
8602  N NH2 . ARG D 954  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  951  ARG A NH2 
8603  N N   . VAL D 955  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  952  VAL A N   
8604  C CA  . VAL D 955  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  952  VAL A CA  
8605  C C   . VAL D 955  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  952  VAL A C   
8606  O O   . VAL D 955  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  952  VAL A O   
8607  C CB  . VAL D 955  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  952  VAL A CB  
8608  C CG1 . VAL D 955  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  952  VAL A CG1 
8609  C CG2 . VAL D 955  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  952  VAL A CG2 
8610  N N   . ALA D 956  ? 0.6869 0.6869 0.6869 0.0000  0.0000  0.0000  953  ALA A N   
8611  C CA  . ALA D 956  ? 0.6869 0.6869 0.6869 0.0000  0.0000  0.0000  953  ALA A CA  
8612  C C   . ALA D 956  ? 0.6869 0.6869 0.6869 0.0000  0.0000  0.0000  953  ALA A C   
8613  O O   . ALA D 956  ? 0.6869 0.6869 0.6869 0.0000  0.0000  0.0000  953  ALA A O   
8614  C CB  . ALA D 956  ? 0.6869 0.6869 0.6869 0.0000  0.0000  0.0000  953  ALA A CB  
8615  N N   . ALA D 957  ? 0.7272 0.7272 0.7272 0.0000  0.0000  0.0000  954  ALA A N   
8616  C CA  . ALA D 957  ? 0.7272 0.7272 0.7272 0.0000  0.0000  0.0000  954  ALA A CA  
8617  C C   . ALA D 957  ? 0.7272 0.7272 0.7272 0.0000  0.0000  0.0000  954  ALA A C   
8618  O O   . ALA D 957  ? 0.7272 0.7272 0.7272 0.0000  0.0000  0.0000  954  ALA A O   
8619  C CB  . ALA D 957  ? 0.7272 0.7272 0.7272 0.0000  0.0000  0.0000  954  ALA A CB  
8620  N N   . ARG D 958  ? 0.8520 0.8520 0.8520 0.0000  0.0000  0.0000  955  ARG A N   
8621  C CA  . ARG D 958  ? 0.8520 0.8520 0.8520 0.0000  0.0000  0.0000  955  ARG A CA  
8622  C C   . ARG D 958  ? 0.8520 0.8520 0.8520 0.0000  0.0000  0.0000  955  ARG A C   
8623  O O   . ARG D 958  ? 0.8520 0.8520 0.8520 0.0000  0.0000  0.0000  955  ARG A O   
8624  C CB  . ARG D 958  ? 0.8520 0.8520 0.8520 0.0000  0.0000  0.0000  955  ARG A CB  
8625  C CG  . ARG D 958  ? 0.8520 0.8520 0.8520 0.0000  0.0000  0.0000  955  ARG A CG  
8626  C CD  . ARG D 958  ? 0.8520 0.8520 0.8520 0.0000  0.0000  0.0000  955  ARG A CD  
8627  N NE  . ARG D 958  ? 0.8520 0.8520 0.8520 0.0000  0.0000  0.0000  955  ARG A NE  
8628  C CZ  . ARG D 958  ? 0.8520 0.8520 0.8520 0.0000  0.0000  0.0000  955  ARG A CZ  
8629  N NH1 . ARG D 958  ? 0.8520 0.8520 0.8520 0.0000  0.0000  0.0000  955  ARG A NH1 
8630  N NH2 . ARG D 958  ? 0.8520 0.8520 0.8520 0.0000  0.0000  0.0000  955  ARG A NH2 
8631  N N   . GLN D 959  ? 0.8101 0.8101 0.8101 0.0000  0.0000  0.0000  956  GLN A N   
8632  C CA  . GLN D 959  ? 0.8101 0.8101 0.8101 0.0000  0.0000  0.0000  956  GLN A CA  
8633  C C   . GLN D 959  ? 0.8101 0.8101 0.8101 0.0000  0.0000  0.0000  956  GLN A C   
8634  O O   . GLN D 959  ? 0.8101 0.8101 0.8101 0.0000  0.0000  0.0000  956  GLN A O   
8635  C CB  . GLN D 959  ? 0.8101 0.8101 0.8101 0.0000  0.0000  0.0000  956  GLN A CB  
8636  C CG  . GLN D 959  ? 0.8101 0.8101 0.8101 0.0000  0.0000  0.0000  956  GLN A CG  
8637  C CD  . GLN D 959  ? 0.8101 0.8101 0.8101 0.0000  0.0000  0.0000  956  GLN A CD  
8638  O OE1 . GLN D 959  ? 0.8101 0.8101 0.8101 0.0000  0.0000  0.0000  956  GLN A OE1 
8639  N NE2 . GLN D 959  ? 0.8101 0.8101 0.8101 0.0000  0.0000  0.0000  956  GLN A NE2 
8645  N N   . TRP D 961  ? 0.7985 0.7985 0.7985 0.0000  0.0000  0.0000  958  TRP A N   
8646  C CA  . TRP D 961  ? 0.7985 0.7985 0.7985 0.0000  0.0000  0.0000  958  TRP A CA  
8647  C C   . TRP D 961  ? 0.7985 0.7985 0.7985 0.0000  0.0000  0.0000  958  TRP A C   
8648  O O   . TRP D 961  ? 0.7985 0.7985 0.7985 0.0000  0.0000  0.0000  958  TRP A O   
8659  N N   . SER D 962  ? 0.6940 0.6940 0.6940 0.0000  0.0000  0.0000  959  SER A N   
8660  C CA  . SER D 962  ? 0.6940 0.6940 0.6940 0.0000  0.0000  0.0000  959  SER A CA  
8661  C C   . SER D 962  ? 0.6940 0.6940 0.6940 0.0000  0.0000  0.0000  959  SER A C   
8662  O O   . SER D 962  ? 0.6940 0.6940 0.6940 0.0000  0.0000  0.0000  959  SER A O   
8663  C CB  . SER D 962  ? 0.6940 0.6940 0.6940 0.0000  0.0000  0.0000  959  SER A CB  
8664  O OG  . SER D 962  ? 0.6940 0.6940 0.6940 0.0000  0.0000  0.0000  959  SER A OG  
8665  N N   . VAL D 963  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  960  VAL A N   
8666  C CA  . VAL D 963  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  960  VAL A CA  
8667  C C   . VAL D 963  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  960  VAL A C   
8668  O O   . VAL D 963  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  960  VAL A O   
8669  C CB  . VAL D 963  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  960  VAL A CB  
8670  C CG1 . VAL D 963  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  960  VAL A CG1 
8671  C CG2 . VAL D 963  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  960  VAL A CG2 
8672  N N   . VAL D 964  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  961  VAL A N   
8673  C CA  . VAL D 964  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  961  VAL A CA  
8674  C C   . VAL D 964  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  961  VAL A C   
8675  O O   . VAL D 964  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  961  VAL A O   
8676  C CB  . VAL D 964  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  961  VAL A CB  
8677  C CG1 . VAL D 964  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  961  VAL A CG1 
8678  C CG2 . VAL D 964  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  961  VAL A CG2 
8679  N N   . GLY D 965  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  962  GLY A N   
8680  C CA  . GLY D 965  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  962  GLY A CA  
8681  C C   . GLY D 965  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  962  GLY A C   
8682  O O   . GLY D 965  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  962  GLY A O   
8683  N N   . THR D 966  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  963  THR A N   
8684  C CA  . THR D 966  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  963  THR A CA  
8685  C C   . THR D 966  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  963  THR A C   
8686  O O   . THR D 966  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  963  THR A O   
8687  C CB  . THR D 966  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  963  THR A CB  
8688  O OG1 . THR D 966  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  963  THR A OG1 
8689  C CG2 . THR D 966  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  963  THR A CG2 
8690  N N   . ILE D 967  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  964  ILE A N   
8691  C CA  . ILE D 967  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  964  ILE A CA  
8692  C C   . ILE D 967  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  964  ILE A C   
8693  O O   . ILE D 967  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  964  ILE A O   
8694  C CB  . ILE D 967  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  964  ILE A CB  
8695  C CG1 . ILE D 967  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  964  ILE A CG1 
8696  C CG2 . ILE D 967  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  964  ILE A CG2 
8697  C CD1 . ILE D 967  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  964  ILE A CD1 
8698  N N   . LYS D 968  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  965  LYS A N   
8699  C CA  . LYS D 968  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  965  LYS A CA  
8700  C C   . LYS D 968  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  965  LYS A C   
8701  O O   . LYS D 968  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  965  LYS A O   
8702  C CB  . LYS D 968  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  965  LYS A CB  
8703  C CG  . LYS D 968  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  965  LYS A CG  
8704  C CD  . LYS D 968  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  965  LYS A CD  
8705  C CE  . LYS D 968  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  965  LYS A CE  
8706  N NZ  . LYS D 968  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  965  LYS A NZ  
8707  N N   . ASP D 969  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  966  ASP A N   
8708  C CA  . ASP D 969  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  966  ASP A CA  
8709  C C   . ASP D 969  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  966  ASP A C   
8710  O O   . ASP D 969  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  966  ASP A O   
8711  C CB  . ASP D 969  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  966  ASP A CB  
8712  C CG  . ASP D 969  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  966  ASP A CG  
8713  O OD1 . ASP D 969  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  966  ASP A OD1 
8714  O OD2 . ASP D 969  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  966  ASP A OD2 
8715  N N   . LEU D 970  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  967  LEU A N   
8716  C CA  . LEU D 970  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  967  LEU A CA  
8717  C C   . LEU D 970  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  967  LEU A C   
8718  O O   . LEU D 970  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  967  LEU A O   
8719  C CB  . LEU D 970  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  967  LEU A CB  
8720  C CG  . LEU D 970  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  967  LEU A CG  
8721  C CD1 . LEU D 970  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  967  LEU A CD1 
8722  C CD2 . LEU D 970  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  967  LEU A CD2 
8723  N N   . LYS D 971  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  968  LYS A N   
8724  C CA  . LYS D 971  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  968  LYS A CA  
8725  C C   . LYS D 971  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  968  LYS A C   
8726  O O   . LYS D 971  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  968  LYS A O   
8727  C CB  . LYS D 971  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  968  LYS A CB  
8728  C CG  . LYS D 971  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  968  LYS A CG  
8729  C CD  . LYS D 971  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  968  LYS A CD  
8730  C CE  . LYS D 971  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  968  LYS A CE  
8731  N NZ  . LYS D 971  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  968  LYS A NZ  
8732  N N   . GLN D 972  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  969  GLN A N   
8733  C CA  . GLN D 972  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  969  GLN A CA  
8734  C C   . GLN D 972  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  969  GLN A C   
8735  O O   . GLN D 972  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  969  GLN A O   
8741  N N   . GLY D 973  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  970  GLY A N   
8742  C CA  . GLY D 973  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  970  GLY A CA  
8743  C C   . GLY D 973  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  970  GLY A C   
8744  O O   . GLY D 973  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  970  GLY A O   
8745  N N   . TYR D 974  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  971  TYR A N   
8746  C CA  . TYR D 974  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  971  TYR A CA  
8747  C C   . TYR D 974  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  971  TYR A C   
8748  O O   . TYR D 974  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  971  TYR A O   
8749  C CB  . TYR D 974  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  971  TYR A CB  
8750  C CG  . TYR D 974  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  971  TYR A CG  
8751  C CD1 . TYR D 974  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  971  TYR A CD1 
8752  C CD2 . TYR D 974  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  971  TYR A CD2 
8753  C CE1 . TYR D 974  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  971  TYR A CE1 
8754  C CE2 . TYR D 974  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  971  TYR A CE2 
8755  C CZ  . TYR D 974  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  971  TYR A CZ  
8756  O OH  . TYR D 974  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  971  TYR A OH  
8757  N N   . LEU D 975  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  972  LEU A N   
8758  C CA  . LEU D 975  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  972  LEU A CA  
8759  C C   . LEU D 975  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  972  LEU A C   
8760  O O   . LEU D 975  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  972  LEU A O   
8761  C CB  . LEU D 975  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  972  LEU A CB  
8762  C CG  . LEU D 975  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  972  LEU A CG  
8763  C CD1 . LEU D 975  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  972  LEU A CD1 
8764  C CD2 . LEU D 975  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  972  LEU A CD2 
8765  N N   . SER D 976  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  973  SER A N   
8766  C CA  . SER D 976  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  973  SER A CA  
8767  C C   . SER D 976  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  973  SER A C   
8768  O O   . SER D 976  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  973  SER A O   
8769  C CB  . SER D 976  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  973  SER A CB  
8770  O OG  . SER D 976  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  973  SER A OG  
8771  N N   . GLN D 977  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  974  GLN A N   
8772  C CA  . GLN D 977  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  974  GLN A CA  
8773  C C   . GLN D 977  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  974  GLN A C   
8774  O O   . GLN D 977  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  974  GLN A O   
8775  C CB  . GLN D 977  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  974  GLN A CB  
8776  C CG  . GLN D 977  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  974  GLN A CG  
8777  C CD  . GLN D 977  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  974  GLN A CD  
8778  O OE1 . GLN D 977  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  974  GLN A OE1 
8779  N NE2 . GLN D 977  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  974  GLN A NE2 
8780  N N   . VAL D 978  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  975  VAL A N   
8781  C CA  . VAL D 978  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  975  VAL A CA  
8782  C C   . VAL D 978  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  975  VAL A C   
8783  O O   . VAL D 978  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  975  VAL A O   
8784  C CB  . VAL D 978  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  975  VAL A CB  
8785  C CG1 . VAL D 978  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  975  VAL A CG1 
8786  C CG2 . VAL D 978  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  975  VAL A CG2 
8787  N N   . ILE D 979  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  976  ILE A N   
8788  C CA  . ILE D 979  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  976  ILE A CA  
8789  C C   . ILE D 979  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  976  ILE A C   
8790  O O   . ILE D 979  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  976  ILE A O   
8791  C CB  . ILE D 979  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  976  ILE A CB  
8792  C CG1 . ILE D 979  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  976  ILE A CG1 
8793  C CG2 . ILE D 979  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  976  ILE A CG2 
8794  C CD1 . ILE D 979  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  976  ILE A CD1 
8795  N N   . HIS D 980  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  977  HIS A N   
8796  C CA  . HIS D 980  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  977  HIS A CA  
8797  C C   . HIS D 980  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  977  HIS A C   
8798  O O   . HIS D 980  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  977  HIS A O   
8799  C CB  . HIS D 980  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  977  HIS A CB  
8800  C CG  . HIS D 980  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  977  HIS A CG  
8801  N ND1 . HIS D 980  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  977  HIS A ND1 
8802  C CD2 . HIS D 980  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  977  HIS A CD2 
8803  C CE1 . HIS D 980  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  977  HIS A CE1 
8804  N NE2 . HIS D 980  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  977  HIS A NE2 
8805  N N   . GLU D 981  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  978  GLU A N   
8806  C CA  . GLU D 981  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  978  GLU A CA  
8807  C C   . GLU D 981  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  978  GLU A C   
8808  O O   . GLU D 981  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  978  GLU A O   
8809  C CB  . GLU D 981  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  978  GLU A CB  
8810  C CG  . GLU D 981  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  978  GLU A CG  
8811  C CD  . GLU D 981  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  978  GLU A CD  
8812  O OE1 . GLU D 981  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  978  GLU A OE1 
8813  O OE2 . GLU D 981  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  978  GLU A OE2 
8814  N N   . ILE D 982  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  979  ILE A N   
8815  C CA  . ILE D 982  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  979  ILE A CA  
8816  C C   . ILE D 982  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  979  ILE A C   
8817  O O   . ILE D 982  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  979  ILE A O   
8818  C CB  . ILE D 982  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  979  ILE A CB  
8819  C CG1 . ILE D 982  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  979  ILE A CG1 
8820  C CG2 . ILE D 982  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  979  ILE A CG2 
8821  C CD1 . ILE D 982  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  979  ILE A CD1 
8822  N N   . VAL D 983  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  980  VAL A N   
8823  C CA  . VAL D 983  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  980  VAL A CA  
8824  C C   . VAL D 983  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  980  VAL A C   
8825  O O   . VAL D 983  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  980  VAL A O   
8826  C CB  . VAL D 983  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  980  VAL A CB  
8827  C CG1 . VAL D 983  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  980  VAL A CG1 
8828  C CG2 . VAL D 983  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  980  VAL A CG2 
8829  N N   . ASP D 984  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  981  ASP A N   
8830  C CA  . ASP D 984  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  981  ASP A CA  
8831  C C   . ASP D 984  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  981  ASP A C   
8832  O O   . ASP D 984  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  981  ASP A O   
8833  C CB  . ASP D 984  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  981  ASP A CB  
8834  C CG  . ASP D 984  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  981  ASP A CG  
8835  O OD1 . ASP D 984  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  981  ASP A OD1 
8836  O OD2 . ASP D 984  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  981  ASP A OD2 
8837  N N   . LEU D 985  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  982  LEU A N   
8838  C CA  . LEU D 985  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  982  LEU A CA  
8839  C C   . LEU D 985  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  982  LEU A C   
8840  O O   . LEU D 985  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  982  LEU A O   
8841  C CB  . LEU D 985  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  982  LEU A CB  
8842  C CG  . LEU D 985  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  982  LEU A CG  
8843  C CD1 . LEU D 985  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  982  LEU A CD1 
8844  C CD2 . LEU D 985  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  982  LEU A CD2 
8845  N N   . MET D 986  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  983  MET A N   
8846  C CA  . MET D 986  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  983  MET A CA  
8847  C C   . MET D 986  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  983  MET A C   
8848  O O   . MET D 986  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  983  MET A O   
8849  C CB  . MET D 986  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  983  MET A CB  
8850  C CG  . MET D 986  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  983  MET A CG  
8851  S SD  . MET D 986  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  983  MET A SD  
8852  C CE  . MET D 986  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  983  MET A CE  
8853  N N   . ILE D 987  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  984  ILE A N   
8854  C CA  . ILE D 987  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  984  ILE A CA  
8855  C C   . ILE D 987  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  984  ILE A C   
8856  O O   . ILE D 987  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  984  ILE A O   
8857  C CB  . ILE D 987  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  984  ILE A CB  
8858  C CG1 . ILE D 987  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  984  ILE A CG1 
8859  C CG2 . ILE D 987  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  984  ILE A CG2 
8860  C CD1 . ILE D 987  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  984  ILE A CD1 
8861  N N   . HIS D 988  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  985  HIS A N   
8862  C CA  . HIS D 988  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  985  HIS A CA  
8863  C C   . HIS D 988  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  985  HIS A C   
8864  O O   . HIS D 988  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  985  HIS A O   
8865  C CB  . HIS D 988  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  985  HIS A CB  
8866  C CG  . HIS D 988  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  985  HIS A CG  
8867  N ND1 . HIS D 988  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  985  HIS A ND1 
8868  C CD2 . HIS D 988  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  985  HIS A CD2 
8869  C CE1 . HIS D 988  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  985  HIS A CE1 
8870  N NE2 . HIS D 988  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  985  HIS A NE2 
8871  N N   . TYR D 989  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  986  TYR A N   
8872  C CA  . TYR D 989  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  986  TYR A CA  
8873  C C   . TYR D 989  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  986  TYR A C   
8874  O O   . TYR D 989  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  986  TYR A O   
8875  C CB  . TYR D 989  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  986  TYR A CB  
8876  C CG  . TYR D 989  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  986  TYR A CG  
8877  C CD1 . TYR D 989  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  986  TYR A CD1 
8878  C CD2 . TYR D 989  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  986  TYR A CD2 
8879  C CE1 . TYR D 989  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  986  TYR A CE1 
8880  C CE2 . TYR D 989  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  986  TYR A CE2 
8881  C CZ  . TYR D 989  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  986  TYR A CZ  
8882  O OH  . TYR D 989  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  986  TYR A OH  
8883  N N   . GLN D 990  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  987  GLN A N   
8884  C CA  . GLN D 990  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  987  GLN A CA  
8885  C C   . GLN D 990  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  987  GLN A C   
8886  O O   . GLN D 990  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  987  GLN A O   
8887  C CB  . GLN D 990  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  987  GLN A CB  
8888  C CG  . GLN D 990  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  987  GLN A CG  
8889  C CD  . GLN D 990  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  987  GLN A CD  
8890  O OE1 . GLN D 990  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  987  GLN A OE1 
8891  N NE2 . GLN D 990  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  987  GLN A NE2 
8892  N N   . ALA D 991  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  988  ALA A N   
8893  C CA  . ALA D 991  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  988  ALA A CA  
8894  C C   . ALA D 991  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  988  ALA A C   
8895  O O   . ALA D 991  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  988  ALA A O   
8896  C CB  . ALA D 991  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  988  ALA A CB  
8897  N N   . VAL D 992  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  989  VAL A N   
8898  C CA  . VAL D 992  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  989  VAL A CA  
8899  C C   . VAL D 992  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  989  VAL A C   
8900  O O   . VAL D 992  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  989  VAL A O   
8901  C CB  . VAL D 992  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  989  VAL A CB  
8902  C CG1 . VAL D 992  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  989  VAL A CG1 
8903  C CG2 . VAL D 992  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  989  VAL A CG2 
8904  N N   . VAL D 993  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  990  VAL A N   
8905  C CA  . VAL D 993  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  990  VAL A CA  
8906  C C   . VAL D 993  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  990  VAL A C   
8907  O O   . VAL D 993  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  990  VAL A O   
8908  C CB  . VAL D 993  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  990  VAL A CB  
8909  C CG1 . VAL D 993  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  990  VAL A CG1 
8910  C CG2 . VAL D 993  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  990  VAL A CG2 
8911  N N   . VAL D 994  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  991  VAL A N   
8912  C CA  . VAL D 994  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  991  VAL A CA  
8913  C C   . VAL D 994  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  991  VAL A C   
8914  O O   . VAL D 994  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  991  VAL A O   
8915  C CB  . VAL D 994  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  991  VAL A CB  
8916  C CG1 . VAL D 994  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  991  VAL A CG1 
8917  C CG2 . VAL D 994  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  991  VAL A CG2 
8918  N N   . LEU D 995  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  992  LEU A N   
8919  C CA  . LEU D 995  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  992  LEU A CA  
8920  C C   . LEU D 995  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  992  LEU A C   
8921  O O   . LEU D 995  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  992  LEU A O   
8922  C CB  . LEU D 995  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  992  LEU A CB  
8923  C CG  . LEU D 995  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  992  LEU A CG  
8924  C CD1 . LEU D 995  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  992  LEU A CD1 
8925  C CD2 . LEU D 995  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  992  LEU A CD2 
8926  N N   . GLU D 996  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  993  GLU A N   
8927  C CA  . GLU D 996  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  993  GLU A CA  
8928  C C   . GLU D 996  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  993  GLU A C   
8929  O O   . GLU D 996  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  993  GLU A O   
8930  C CB  . GLU D 996  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  993  GLU A CB  
8931  C CG  . GLU D 996  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  993  GLU A CG  
8932  C CD  . GLU D 996  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  993  GLU A CD  
8933  O OE1 . GLU D 996  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  993  GLU A OE1 
8934  O OE2 . GLU D 996  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  993  GLU A OE2 
8935  N N   . ASN D 997  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  994  ASN A N   
8936  C CA  . ASN D 997  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  994  ASN A CA  
8937  C C   . ASN D 997  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  994  ASN A C   
8938  O O   . ASN D 997  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  994  ASN A O   
8939  C CB  . ASN D 997  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  994  ASN A CB  
8940  C CG  . ASN D 997  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  994  ASN A CG  
8941  O OD1 . ASN D 997  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  994  ASN A OD1 
8942  N ND2 . ASN D 997  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  994  ASN A ND2 
8943  N N   . LEU D 998  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  995  LEU A N   
8944  C CA  . LEU D 998  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  995  LEU A CA  
8945  C C   . LEU D 998  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  995  LEU A C   
8946  O O   . LEU D 998  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  995  LEU A O   
8947  C CB  . LEU D 998  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  995  LEU A CB  
8948  C CG  . LEU D 998  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  995  LEU A CG  
8949  C CD1 . LEU D 998  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  995  LEU A CD1 
8950  C CD2 . LEU D 998  ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  995  LEU A CD2 
9067  N N   . VAL D 1014 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1011 VAL A N   
9068  C CA  . VAL D 1014 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1011 VAL A CA  
9069  C C   . VAL D 1014 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1011 VAL A C   
9070  O O   . VAL D 1014 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1011 VAL A O   
9071  C CB  . VAL D 1014 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1011 VAL A CB  
9072  C CG1 . VAL D 1014 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1011 VAL A CG1 
9073  C CG2 . VAL D 1014 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1011 VAL A CG2 
9074  N N   . TYR D 1015 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1012 TYR A N   
9075  C CA  . TYR D 1015 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1012 TYR A CA  
9076  C C   . TYR D 1015 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1012 TYR A C   
9077  O O   . TYR D 1015 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1012 TYR A O   
9078  C CB  . TYR D 1015 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1012 TYR A CB  
9079  C CG  . TYR D 1015 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1012 TYR A CG  
9080  C CD1 . TYR D 1015 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1012 TYR A CD1 
9081  C CD2 . TYR D 1015 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1012 TYR A CD2 
9082  C CE1 . TYR D 1015 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1012 TYR A CE1 
9083  C CE2 . TYR D 1015 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1012 TYR A CE2 
9084  C CZ  . TYR D 1015 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1012 TYR A CZ  
9085  O OH  . TYR D 1015 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1012 TYR A OH  
9086  N N   . GLN D 1016 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1013 GLN A N   
9087  C CA  . GLN D 1016 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1013 GLN A CA  
9088  C C   . GLN D 1016 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1013 GLN A C   
9089  O O   . GLN D 1016 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1013 GLN A O   
9090  C CB  . GLN D 1016 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1013 GLN A CB  
9091  C CG  . GLN D 1016 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1013 GLN A CG  
9092  C CD  . GLN D 1016 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1013 GLN A CD  
9093  O OE1 . GLN D 1016 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1013 GLN A OE1 
9094  N NE2 . GLN D 1016 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1013 GLN A NE2 
9095  N N   . GLN D 1017 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1014 GLN A N   
9096  C CA  . GLN D 1017 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1014 GLN A CA  
9097  C C   . GLN D 1017 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1014 GLN A C   
9098  O O   . GLN D 1017 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1014 GLN A O   
9099  C CB  . GLN D 1017 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1014 GLN A CB  
9100  C CG  . GLN D 1017 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1014 GLN A CG  
9101  C CD  . GLN D 1017 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1014 GLN A CD  
9102  O OE1 . GLN D 1017 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1014 GLN A OE1 
9103  N NE2 . GLN D 1017 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1014 GLN A NE2 
9104  N N   . PHE D 1018 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1015 PHE A N   
9105  C CA  . PHE D 1018 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1015 PHE A CA  
9106  C C   . PHE D 1018 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1015 PHE A C   
9107  O O   . PHE D 1018 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1015 PHE A O   
9108  C CB  . PHE D 1018 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1015 PHE A CB  
9109  C CG  . PHE D 1018 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1015 PHE A CG  
9110  C CD1 . PHE D 1018 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1015 PHE A CD1 
9111  C CD2 . PHE D 1018 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1015 PHE A CD2 
9112  C CE1 . PHE D 1018 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1015 PHE A CE1 
9113  C CE2 . PHE D 1018 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1015 PHE A CE2 
9114  C CZ  . PHE D 1018 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1015 PHE A CZ  
9115  N N   . GLU D 1019 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1016 GLU A N   
9116  C CA  . GLU D 1019 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1016 GLU A CA  
9117  C C   . GLU D 1019 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1016 GLU A C   
9118  O O   . GLU D 1019 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1016 GLU A O   
9119  C CB  . GLU D 1019 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1016 GLU A CB  
9120  C CG  . GLU D 1019 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1016 GLU A CG  
9121  C CD  . GLU D 1019 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1016 GLU A CD  
9122  O OE1 . GLU D 1019 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1016 GLU A OE1 
9123  O OE2 . GLU D 1019 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1016 GLU A OE2 
9124  N N   . LYS D 1020 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1017 LYS A N   
9125  C CA  . LYS D 1020 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1017 LYS A CA  
9126  C C   . LYS D 1020 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1017 LYS A C   
9127  O O   . LYS D 1020 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1017 LYS A O   
9128  C CB  . LYS D 1020 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1017 LYS A CB  
9129  C CG  . LYS D 1020 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1017 LYS A CG  
9130  C CD  . LYS D 1020 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1017 LYS A CD  
9131  C CE  . LYS D 1020 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1017 LYS A CE  
9132  N NZ  . LYS D 1020 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1017 LYS A NZ  
9133  N N   . MET D 1021 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1018 MET A N   
9134  C CA  . MET D 1021 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1018 MET A CA  
9135  C C   . MET D 1021 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1018 MET A C   
9136  O O   . MET D 1021 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1018 MET A O   
9137  C CB  . MET D 1021 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1018 MET A CB  
9138  C CG  . MET D 1021 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1018 MET A CG  
9139  S SD  . MET D 1021 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1018 MET A SD  
9140  C CE  . MET D 1021 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1018 MET A CE  
9141  N N   . LEU D 1022 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1019 LEU A N   
9142  C CA  . LEU D 1022 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1019 LEU A CA  
9143  C C   . LEU D 1022 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1019 LEU A C   
9144  O O   . LEU D 1022 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1019 LEU A O   
9145  C CB  . LEU D 1022 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1019 LEU A CB  
9146  C CG  . LEU D 1022 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1019 LEU A CG  
9147  C CD1 . LEU D 1022 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1019 LEU A CD1 
9148  C CD2 . LEU D 1022 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1019 LEU A CD2 
9149  N N   . ILE D 1023 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1020 ILE A N   
9150  C CA  . ILE D 1023 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1020 ILE A CA  
9151  C C   . ILE D 1023 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1020 ILE A C   
9152  O O   . ILE D 1023 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1020 ILE A O   
9153  C CB  . ILE D 1023 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1020 ILE A CB  
9154  C CG1 . ILE D 1023 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1020 ILE A CG1 
9155  C CG2 . ILE D 1023 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1020 ILE A CG2 
9156  C CD1 . ILE D 1023 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1020 ILE A CD1 
9157  N N   . ASP D 1024 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1021 ASP A N   
9158  C CA  . ASP D 1024 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1021 ASP A CA  
9159  C C   . ASP D 1024 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1021 ASP A C   
9160  O O   . ASP D 1024 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1021 ASP A O   
9161  C CB  . ASP D 1024 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1021 ASP A CB  
9162  C CG  . ASP D 1024 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1021 ASP A CG  
9163  O OD1 . ASP D 1024 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1021 ASP A OD1 
9164  O OD2 . ASP D 1024 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1021 ASP A OD2 
9165  N N   . LYS D 1025 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1022 LYS A N   
9166  C CA  . LYS D 1025 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1022 LYS A CA  
9167  C C   . LYS D 1025 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1022 LYS A C   
9168  O O   . LYS D 1025 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1022 LYS A O   
9169  C CB  . LYS D 1025 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1022 LYS A CB  
9170  C CG  . LYS D 1025 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1022 LYS A CG  
9171  C CD  . LYS D 1025 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1022 LYS A CD  
9172  C CE  . LYS D 1025 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1022 LYS A CE  
9173  N NZ  . LYS D 1025 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1022 LYS A NZ  
9174  N N   . LEU D 1026 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1023 LEU A N   
9175  C CA  . LEU D 1026 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1023 LEU A CA  
9176  C C   . LEU D 1026 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1023 LEU A C   
9177  O O   . LEU D 1026 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1023 LEU A O   
9178  C CB  . LEU D 1026 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1023 LEU A CB  
9179  C CG  . LEU D 1026 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1023 LEU A CG  
9180  C CD1 . LEU D 1026 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1023 LEU A CD1 
9181  C CD2 . LEU D 1026 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1023 LEU A CD2 
9182  N N   . ASN D 1027 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1024 ASN A N   
9183  C CA  . ASN D 1027 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1024 ASN A CA  
9184  C C   . ASN D 1027 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1024 ASN A C   
9185  O O   . ASN D 1027 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1024 ASN A O   
9186  C CB  . ASN D 1027 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1024 ASN A CB  
9187  C CG  . ASN D 1027 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1024 ASN A CG  
9188  O OD1 . ASN D 1027 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1024 ASN A OD1 
9189  N ND2 . ASN D 1027 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1024 ASN A ND2 
9190  N N   . CYS D 1028 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1025 CYS A N   
9191  C CA  . CYS D 1028 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1025 CYS A CA  
9192  C C   . CYS D 1028 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1025 CYS A C   
9193  O O   . CYS D 1028 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1025 CYS A O   
9194  C CB  . CYS D 1028 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1025 CYS A CB  
9195  S SG  . CYS D 1028 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1025 CYS A SG  
9196  N N   . LEU D 1029 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1026 LEU A N   
9197  C CA  . LEU D 1029 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1026 LEU A CA  
9198  C C   . LEU D 1029 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1026 LEU A C   
9199  O O   . LEU D 1029 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1026 LEU A O   
9200  C CB  . LEU D 1029 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1026 LEU A CB  
9201  C CG  . LEU D 1029 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1026 LEU A CG  
9202  C CD1 . LEU D 1029 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1026 LEU A CD1 
9203  C CD2 . LEU D 1029 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1026 LEU A CD2 
9204  N N   . VAL D 1030 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1027 VAL A N   
9205  C CA  . VAL D 1030 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1027 VAL A CA  
9206  C C   . VAL D 1030 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1027 VAL A C   
9207  O O   . VAL D 1030 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1027 VAL A O   
9208  C CB  . VAL D 1030 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1027 VAL A CB  
9209  C CG1 . VAL D 1030 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1027 VAL A CG1 
9210  C CG2 . VAL D 1030 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1027 VAL A CG2 
9211  N N   . LEU D 1031 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1028 LEU A N   
9212  C CA  . LEU D 1031 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1028 LEU A CA  
9213  C C   . LEU D 1031 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1028 LEU A C   
9214  O O   . LEU D 1031 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1028 LEU A O   
9215  C CB  . LEU D 1031 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1028 LEU A CB  
9216  C CG  . LEU D 1031 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1028 LEU A CG  
9217  C CD1 . LEU D 1031 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1028 LEU A CD1 
9218  C CD2 . LEU D 1031 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1028 LEU A CD2 
9219  N N   . LYS D 1032 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1029 LYS A N   
9220  C CA  . LYS D 1032 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1029 LYS A CA  
9221  C C   . LYS D 1032 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1029 LYS A C   
9222  O O   . LYS D 1032 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1029 LYS A O   
9223  C CB  . LYS D 1032 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1029 LYS A CB  
9224  C CG  . LYS D 1032 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1029 LYS A CG  
9225  C CD  . LYS D 1032 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1029 LYS A CD  
9226  C CE  . LYS D 1032 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1029 LYS A CE  
9227  N NZ  . LYS D 1032 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1029 LYS A NZ  
9228  N N   . ASP D 1033 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1030 ASP A N   
9229  C CA  . ASP D 1033 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1030 ASP A CA  
9230  C C   . ASP D 1033 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1030 ASP A C   
9231  O O   . ASP D 1033 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1030 ASP A O   
9232  C CB  . ASP D 1033 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1030 ASP A CB  
9233  C CG  . ASP D 1033 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1030 ASP A CG  
9234  O OD1 . ASP D 1033 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1030 ASP A OD1 
9235  O OD2 . ASP D 1033 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1030 ASP A OD2 
9236  N N   . TYR D 1034 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1031 TYR A N   
9237  C CA  . TYR D 1034 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1031 TYR A CA  
9238  C C   . TYR D 1034 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1031 TYR A C   
9239  O O   . TYR D 1034 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1031 TYR A O   
9240  C CB  . TYR D 1034 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1031 TYR A CB  
9241  C CG  . TYR D 1034 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1031 TYR A CG  
9242  C CD1 . TYR D 1034 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1031 TYR A CD1 
9243  C CD2 . TYR D 1034 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1031 TYR A CD2 
9244  C CE1 . TYR D 1034 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1031 TYR A CE1 
9245  C CE2 . TYR D 1034 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1031 TYR A CE2 
9246  C CZ  . TYR D 1034 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1031 TYR A CZ  
9247  O OH  . TYR D 1034 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1031 TYR A OH  
9248  N N   . PRO D 1035 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1032 PRO A N   
9249  C CA  . PRO D 1035 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1032 PRO A CA  
9250  C C   . PRO D 1035 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1032 PRO A C   
9251  O O   . PRO D 1035 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1032 PRO A O   
9252  C CB  . PRO D 1035 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1032 PRO A CB  
9253  C CG  . PRO D 1035 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1032 PRO A CG  
9254  C CD  . PRO D 1035 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1032 PRO A CD  
9255  N N   . ALA D 1036 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1033 ALA A N   
9256  C CA  . ALA D 1036 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1033 ALA A CA  
9257  C C   . ALA D 1036 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1033 ALA A C   
9258  O O   . ALA D 1036 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1033 ALA A O   
9259  C CB  . ALA D 1036 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1033 ALA A CB  
9260  N N   . GLU D 1037 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1034 GLU A N   
9261  C CA  . GLU D 1037 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1034 GLU A CA  
9262  C C   . GLU D 1037 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1034 GLU A C   
9263  O O   . GLU D 1037 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1034 GLU A O   
9269  N N   . LYS D 1038 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1035 LYS A N   
9270  C CA  . LYS D 1038 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1035 LYS A CA  
9271  C C   . LYS D 1038 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1035 LYS A C   
9272  O O   . LYS D 1038 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1035 LYS A O   
9278  N N   . VAL D 1039 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1036 VAL A N   
9279  C CA  . VAL D 1039 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1036 VAL A CA  
9280  C C   . VAL D 1039 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1036 VAL A C   
9281  O O   . VAL D 1039 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1036 VAL A O   
9282  C CB  . VAL D 1039 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1036 VAL A CB  
9283  C CG1 . VAL D 1039 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1036 VAL A CG1 
9284  C CG2 . VAL D 1039 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1036 VAL A CG2 
9285  N N   . GLY D 1040 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1037 GLY A N   
9286  C CA  . GLY D 1040 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1037 GLY A CA  
9287  C C   . GLY D 1040 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1037 GLY A C   
9288  O O   . GLY D 1040 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1037 GLY A O   
9289  N N   . GLY D 1041 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1038 GLY A N   
9290  C CA  . GLY D 1041 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1038 GLY A CA  
9291  C C   . GLY D 1041 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1038 GLY A C   
9292  O O   . GLY D 1041 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1038 GLY A O   
9293  N N   . VAL D 1042 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1039 VAL A N   
9294  C CA  . VAL D 1042 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1039 VAL A CA  
9295  C C   . VAL D 1042 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1039 VAL A C   
9296  O O   . VAL D 1042 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1039 VAL A O   
9297  C CB  . VAL D 1042 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1039 VAL A CB  
9298  C CG1 . VAL D 1042 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1039 VAL A CG1 
9299  C CG2 . VAL D 1042 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1039 VAL A CG2 
9300  N N   . LEU D 1043 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1040 LEU A N   
9301  C CA  . LEU D 1043 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1040 LEU A CA  
9302  C C   . LEU D 1043 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1040 LEU A C   
9303  O O   . LEU D 1043 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1040 LEU A O   
9304  C CB  . LEU D 1043 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1040 LEU A CB  
9305  C CG  . LEU D 1043 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1040 LEU A CG  
9306  C CD1 . LEU D 1043 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1040 LEU A CD1 
9307  C CD2 . LEU D 1043 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1040 LEU A CD2 
9308  N N   . ASN D 1044 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1041 ASN A N   
9309  C CA  . ASN D 1044 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1041 ASN A CA  
9310  C C   . ASN D 1044 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1041 ASN A C   
9311  O O   . ASN D 1044 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1041 ASN A O   
9312  C CB  . ASN D 1044 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1041 ASN A CB  
9313  C CG  . ASN D 1044 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1041 ASN A CG  
9314  O OD1 . ASN D 1044 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1041 ASN A OD1 
9315  N ND2 . ASN D 1044 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1041 ASN A ND2 
9316  N N   . PRO D 1045 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1042 PRO A N   
9317  C CA  . PRO D 1045 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1042 PRO A CA  
9318  C C   . PRO D 1045 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1042 PRO A C   
9319  O O   . PRO D 1045 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1042 PRO A O   
9320  C CB  . PRO D 1045 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1042 PRO A CB  
9321  C CG  . PRO D 1045 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1042 PRO A CG  
9322  C CD  . PRO D 1045 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1042 PRO A CD  
9323  N N   . TYR D 1046 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1043 TYR A N   
9324  C CA  . TYR D 1046 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1043 TYR A CA  
9325  C C   . TYR D 1046 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1043 TYR A C   
9326  O O   . TYR D 1046 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1043 TYR A O   
9327  C CB  . TYR D 1046 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1043 TYR A CB  
9328  C CG  . TYR D 1046 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1043 TYR A CG  
9329  C CD1 . TYR D 1046 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1043 TYR A CD1 
9330  C CD2 . TYR D 1046 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1043 TYR A CD2 
9331  C CE1 . TYR D 1046 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1043 TYR A CE1 
9332  C CE2 . TYR D 1046 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1043 TYR A CE2 
9333  C CZ  . TYR D 1046 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1043 TYR A CZ  
9334  O OH  . TYR D 1046 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1043 TYR A OH  
9335  N N   . GLN D 1047 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1044 GLN A N   
9336  C CA  . GLN D 1047 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1044 GLN A CA  
9337  C C   . GLN D 1047 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1044 GLN A C   
9338  O O   . GLN D 1047 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1044 GLN A O   
9339  C CB  . GLN D 1047 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1044 GLN A CB  
9340  C CG  . GLN D 1047 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1044 GLN A CG  
9341  C CD  . GLN D 1047 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1044 GLN A CD  
9342  O OE1 . GLN D 1047 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1044 GLN A OE1 
9343  N NE2 . GLN D 1047 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1044 GLN A NE2 
9344  N N   . LEU D 1048 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1045 LEU A N   
9345  C CA  . LEU D 1048 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1045 LEU A CA  
9346  C C   . LEU D 1048 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1045 LEU A C   
9347  O O   . LEU D 1048 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1045 LEU A O   
9348  C CB  . LEU D 1048 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1045 LEU A CB  
9349  C CG  . LEU D 1048 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1045 LEU A CG  
9350  C CD1 . LEU D 1048 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1045 LEU A CD1 
9351  C CD2 . LEU D 1048 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1045 LEU A CD2 
9352  N N   . THR D 1049 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1046 THR A N   
9353  C CA  . THR D 1049 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1046 THR A CA  
9354  C C   . THR D 1049 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1046 THR A C   
9355  O O   . THR D 1049 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1046 THR A O   
9356  C CB  . THR D 1049 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1046 THR A CB  
9357  O OG1 . THR D 1049 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1046 THR A OG1 
9358  C CG2 . THR D 1049 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1046 THR A CG2 
9359  N N   . ASP D 1050 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1047 ASP A N   
9360  C CA  . ASP D 1050 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1047 ASP A CA  
9361  C C   . ASP D 1050 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1047 ASP A C   
9362  O O   . ASP D 1050 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1047 ASP A O   
9363  C CB  . ASP D 1050 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1047 ASP A CB  
9364  C CG  . ASP D 1050 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1047 ASP A CG  
9365  O OD1 . ASP D 1050 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1047 ASP A OD1 
9366  O OD2 . ASP D 1050 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1047 ASP A OD2 
9367  N N   . GLN D 1051 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1048 GLN A N   
9368  C CA  . GLN D 1051 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1048 GLN A CA  
9369  C C   . GLN D 1051 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1048 GLN A C   
9370  O O   . GLN D 1051 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1048 GLN A O   
9371  C CB  . GLN D 1051 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1048 GLN A CB  
9372  C CG  . GLN D 1051 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1048 GLN A CG  
9373  C CD  . GLN D 1051 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1048 GLN A CD  
9374  O OE1 . GLN D 1051 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1048 GLN A OE1 
9375  N NE2 . GLN D 1051 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1048 GLN A NE2 
9376  N N   . PHE D 1052 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1049 PHE A N   
9377  C CA  . PHE D 1052 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1049 PHE A CA  
9378  C C   . PHE D 1052 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1049 PHE A C   
9379  O O   . PHE D 1052 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1049 PHE A O   
9380  C CB  . PHE D 1052 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1049 PHE A CB  
9381  C CG  . PHE D 1052 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1049 PHE A CG  
9382  C CD1 . PHE D 1052 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1049 PHE A CD1 
9383  C CD2 . PHE D 1052 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1049 PHE A CD2 
9384  C CE1 . PHE D 1052 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1049 PHE A CE1 
9385  C CE2 . PHE D 1052 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1049 PHE A CE2 
9386  C CZ  . PHE D 1052 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1049 PHE A CZ  
9387  N N   . THR D 1053 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1050 THR A N   
9388  C CA  . THR D 1053 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1050 THR A CA  
9389  C C   . THR D 1053 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1050 THR A C   
9390  O O   . THR D 1053 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1050 THR A O   
9391  C CB  . THR D 1053 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1050 THR A CB  
9392  O OG1 . THR D 1053 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1050 THR A OG1 
9393  C CG2 . THR D 1053 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1050 THR A CG2 
9394  N N   . SER D 1054 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1051 SER A N   
9395  C CA  . SER D 1054 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1051 SER A CA  
9396  C C   . SER D 1054 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1051 SER A C   
9397  O O   . SER D 1054 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1051 SER A O   
9398  C CB  . SER D 1054 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1051 SER A CB  
9399  O OG  . SER D 1054 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1051 SER A OG  
9400  N N   . PHE D 1055 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1052 PHE A N   
9401  C CA  . PHE D 1055 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1052 PHE A CA  
9402  C C   . PHE D 1055 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1052 PHE A C   
9403  O O   . PHE D 1055 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1052 PHE A O   
9404  C CB  . PHE D 1055 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1052 PHE A CB  
9405  C CG  . PHE D 1055 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1052 PHE A CG  
9406  C CD1 . PHE D 1055 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1052 PHE A CD1 
9407  C CD2 . PHE D 1055 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1052 PHE A CD2 
9408  C CE1 . PHE D 1055 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1052 PHE A CE1 
9409  C CE2 . PHE D 1055 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1052 PHE A CE2 
9410  C CZ  . PHE D 1055 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1052 PHE A CZ  
9411  N N   . ALA D 1056 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1053 ALA A N   
9412  C CA  . ALA D 1056 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1053 ALA A CA  
9413  C C   . ALA D 1056 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1053 ALA A C   
9414  O O   . ALA D 1056 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1053 ALA A O   
9415  C CB  . ALA D 1056 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1053 ALA A CB  
9416  N N   . LYS D 1057 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1054 LYS A N   
9417  C CA  . LYS D 1057 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1054 LYS A CA  
9418  C C   . LYS D 1057 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1054 LYS A C   
9419  O O   . LYS D 1057 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1054 LYS A O   
9420  C CB  . LYS D 1057 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1054 LYS A CB  
9421  C CG  . LYS D 1057 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1054 LYS A CG  
9422  C CD  . LYS D 1057 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1054 LYS A CD  
9423  C CE  . LYS D 1057 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1054 LYS A CE  
9424  N NZ  . LYS D 1057 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1054 LYS A NZ  
9425  N N   . MET D 1058 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1055 MET A N   
9426  C CA  . MET D 1058 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1055 MET A CA  
9427  C C   . MET D 1058 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1055 MET A C   
9428  O O   . MET D 1058 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1055 MET A O   
9429  C CB  . MET D 1058 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1055 MET A CB  
9430  C CG  . MET D 1058 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1055 MET A CG  
9431  S SD  . MET D 1058 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1055 MET A SD  
9432  C CE  . MET D 1058 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1055 MET A CE  
9433  N N   . GLY D 1059 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1056 GLY A N   
9434  C CA  . GLY D 1059 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1056 GLY A CA  
9435  C C   . GLY D 1059 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1056 GLY A C   
9436  O O   . GLY D 1059 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1056 GLY A O   
9437  N N   . THR D 1060 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1057 THR A N   
9438  C CA  . THR D 1060 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1057 THR A CA  
9439  C C   . THR D 1060 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1057 THR A C   
9440  O O   . THR D 1060 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1057 THR A O   
9441  C CB  . THR D 1060 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1057 THR A CB  
9442  O OG1 . THR D 1060 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1057 THR A OG1 
9443  C CG2 . THR D 1060 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1057 THR A CG2 
9444  N N   . GLN D 1061 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1058 GLN A N   
9445  C CA  . GLN D 1061 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1058 GLN A CA  
9446  C C   . GLN D 1061 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1058 GLN A C   
9447  O O   . GLN D 1061 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1058 GLN A O   
9448  C CB  . GLN D 1061 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1058 GLN A CB  
9449  C CG  . GLN D 1061 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1058 GLN A CG  
9450  C CD  . GLN D 1061 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1058 GLN A CD  
9451  O OE1 . GLN D 1061 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1058 GLN A OE1 
9452  N NE2 . GLN D 1061 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1058 GLN A NE2 
9453  N N   . SER D 1062 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1059 SER A N   
9454  C CA  . SER D 1062 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1059 SER A CA  
9455  C C   . SER D 1062 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1059 SER A C   
9456  O O   . SER D 1062 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1059 SER A O   
9457  C CB  . SER D 1062 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1059 SER A CB  
9458  O OG  . SER D 1062 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1059 SER A OG  
9459  N N   . GLY D 1063 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1060 GLY A N   
9460  C CA  . GLY D 1063 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1060 GLY A CA  
9461  C C   . GLY D 1063 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1060 GLY A C   
9462  O O   . GLY D 1063 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1060 GLY A O   
9463  N N   . PHE D 1064 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1061 PHE A N   
9464  C CA  . PHE D 1064 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1061 PHE A CA  
9465  C C   . PHE D 1064 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1061 PHE A C   
9466  O O   . PHE D 1064 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1061 PHE A O   
9467  C CB  . PHE D 1064 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1061 PHE A CB  
9468  C CG  . PHE D 1064 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1061 PHE A CG  
9469  C CD1 . PHE D 1064 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1061 PHE A CD1 
9470  C CD2 . PHE D 1064 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1061 PHE A CD2 
9471  C CE1 . PHE D 1064 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1061 PHE A CE1 
9472  C CE2 . PHE D 1064 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1061 PHE A CE2 
9473  C CZ  . PHE D 1064 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1061 PHE A CZ  
9474  N N   . LEU D 1065 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1062 LEU A N   
9475  C CA  . LEU D 1065 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1062 LEU A CA  
9476  C C   . LEU D 1065 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1062 LEU A C   
9477  O O   . LEU D 1065 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1062 LEU A O   
9478  C CB  . LEU D 1065 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1062 LEU A CB  
9479  C CG  . LEU D 1065 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1062 LEU A CG  
9480  C CD1 . LEU D 1065 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1062 LEU A CD1 
9481  C CD2 . LEU D 1065 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1062 LEU A CD2 
9482  N N   . PHE D 1066 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1063 PHE A N   
9483  C CA  . PHE D 1066 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1063 PHE A CA  
9484  C C   . PHE D 1066 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1063 PHE A C   
9485  O O   . PHE D 1066 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1063 PHE A O   
9486  C CB  . PHE D 1066 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1063 PHE A CB  
9487  C CG  . PHE D 1066 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1063 PHE A CG  
9488  C CD1 . PHE D 1066 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1063 PHE A CD1 
9489  C CD2 . PHE D 1066 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1063 PHE A CD2 
9490  C CE1 . PHE D 1066 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1063 PHE A CE1 
9491  C CE2 . PHE D 1066 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1063 PHE A CE2 
9492  C CZ  . PHE D 1066 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1063 PHE A CZ  
9493  N N   . TYR D 1067 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1064 TYR A N   
9494  C CA  . TYR D 1067 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1064 TYR A CA  
9495  C C   . TYR D 1067 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1064 TYR A C   
9496  O O   . TYR D 1067 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1064 TYR A O   
9497  C CB  . TYR D 1067 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1064 TYR A CB  
9498  C CG  . TYR D 1067 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1064 TYR A CG  
9499  C CD1 . TYR D 1067 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1064 TYR A CD1 
9500  C CD2 . TYR D 1067 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1064 TYR A CD2 
9501  C CE1 . TYR D 1067 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1064 TYR A CE1 
9502  C CE2 . TYR D 1067 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1064 TYR A CE2 
9503  C CZ  . TYR D 1067 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1064 TYR A CZ  
9504  O OH  . TYR D 1067 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1064 TYR A OH  
9505  N N   . VAL D 1068 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1065 VAL A N   
9506  C CA  . VAL D 1068 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1065 VAL A CA  
9507  C C   . VAL D 1068 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1065 VAL A C   
9508  O O   . VAL D 1068 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1065 VAL A O   
9509  C CB  . VAL D 1068 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1065 VAL A CB  
9510  C CG1 . VAL D 1068 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1065 VAL A CG1 
9511  C CG2 . VAL D 1068 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1065 VAL A CG2 
9512  N N   . PRO D 1069 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1066 PRO A N   
9513  C CA  . PRO D 1069 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1066 PRO A CA  
9514  C C   . PRO D 1069 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1066 PRO A C   
9515  O O   . PRO D 1069 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1066 PRO A O   
9516  C CB  . PRO D 1069 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1066 PRO A CB  
9517  C CG  . PRO D 1069 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1066 PRO A CG  
9518  C CD  . PRO D 1069 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1066 PRO A CD  
9519  N N   . ALA D 1070 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1067 ALA A N   
9520  C CA  . ALA D 1070 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1067 ALA A CA  
9521  C C   . ALA D 1070 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1067 ALA A C   
9522  O O   . ALA D 1070 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1067 ALA A O   
9523  C CB  . ALA D 1070 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1067 ALA A CB  
9524  N N   . PRO D 1071 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1068 PRO A N   
9525  C CA  . PRO D 1071 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1068 PRO A CA  
9526  C C   . PRO D 1071 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1068 PRO A C   
9527  O O   . PRO D 1071 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1068 PRO A O   
9528  C CB  . PRO D 1071 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1068 PRO A CB  
9529  C CG  . PRO D 1071 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1068 PRO A CG  
9530  C CD  . PRO D 1071 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1068 PRO A CD  
9531  N N   . TYR D 1072 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1069 TYR A N   
9532  C CA  . TYR D 1072 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1069 TYR A CA  
9533  C C   . TYR D 1072 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1069 TYR A C   
9534  O O   . TYR D 1072 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1069 TYR A O   
9535  C CB  . TYR D 1072 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1069 TYR A CB  
9536  C CG  . TYR D 1072 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1069 TYR A CG  
9537  C CD1 . TYR D 1072 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1069 TYR A CD1 
9538  C CD2 . TYR D 1072 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1069 TYR A CD2 
9539  C CE1 . TYR D 1072 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1069 TYR A CE1 
9540  C CE2 . TYR D 1072 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1069 TYR A CE2 
9541  C CZ  . TYR D 1072 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1069 TYR A CZ  
9542  O OH  . TYR D 1072 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1069 TYR A OH  
9543  N N   . THR D 1073 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1070 THR A N   
9544  C CA  . THR D 1073 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1070 THR A CA  
9545  C C   . THR D 1073 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1070 THR A C   
9546  O O   . THR D 1073 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1070 THR A O   
9547  C CB  . THR D 1073 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1070 THR A CB  
9548  O OG1 . THR D 1073 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1070 THR A OG1 
9549  C CG2 . THR D 1073 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1070 THR A CG2 
9550  N N   . SER D 1074 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1071 SER A N   
9551  C CA  . SER D 1074 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1071 SER A CA  
9552  C C   . SER D 1074 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1071 SER A C   
9553  O O   . SER D 1074 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1071 SER A O   
9554  C CB  . SER D 1074 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1071 SER A CB  
9555  O OG  . SER D 1074 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1071 SER A OG  
9556  N N   . LYS D 1075 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1072 LYS A N   
9557  C CA  . LYS D 1075 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1072 LYS A CA  
9558  C C   . LYS D 1075 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1072 LYS A C   
9559  O O   . LYS D 1075 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1072 LYS A O   
9560  C CB  . LYS D 1075 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1072 LYS A CB  
9561  C CG  . LYS D 1075 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1072 LYS A CG  
9562  C CD  . LYS D 1075 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1072 LYS A CD  
9563  C CE  . LYS D 1075 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1072 LYS A CE  
9564  N NZ  . LYS D 1075 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1072 LYS A NZ  
9565  N N   . ILE D 1076 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1073 ILE A N   
9566  C CA  . ILE D 1076 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1073 ILE A CA  
9567  C C   . ILE D 1076 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1073 ILE A C   
9568  O O   . ILE D 1076 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1073 ILE A O   
9569  C CB  . ILE D 1076 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1073 ILE A CB  
9570  C CG1 . ILE D 1076 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1073 ILE A CG1 
9571  C CG2 . ILE D 1076 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1073 ILE A CG2 
9572  C CD1 . ILE D 1076 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1073 ILE A CD1 
9573  N N   . ASP D 1077 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1074 ASP A N   
9574  C CA  . ASP D 1077 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1074 ASP A CA  
9575  C C   . ASP D 1077 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1074 ASP A C   
9576  O O   . ASP D 1077 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1074 ASP A O   
9577  C CB  . ASP D 1077 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1074 ASP A CB  
9578  C CG  . ASP D 1077 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1074 ASP A CG  
9579  O OD1 . ASP D 1077 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1074 ASP A OD1 
9580  O OD2 . ASP D 1077 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1074 ASP A OD2 
9581  N N   . PRO D 1078 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1075 PRO A N   
9582  C CA  . PRO D 1078 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1075 PRO A CA  
9583  C C   . PRO D 1078 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1075 PRO A C   
9584  O O   . PRO D 1078 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1075 PRO A O   
9585  C CB  . PRO D 1078 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1075 PRO A CB  
9586  C CG  . PRO D 1078 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1075 PRO A CG  
9587  C CD  . PRO D 1078 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1075 PRO A CD  
9588  N N   . LEU D 1079 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1076 LEU A N   
9589  C CA  . LEU D 1079 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1076 LEU A CA  
9590  C C   . LEU D 1079 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1076 LEU A C   
9591  O O   . LEU D 1079 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1076 LEU A O   
9592  C CB  . LEU D 1079 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1076 LEU A CB  
9593  C CG  . LEU D 1079 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1076 LEU A CG  
9594  C CD1 . LEU D 1079 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1076 LEU A CD1 
9595  C CD2 . LEU D 1079 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1076 LEU A CD2 
9596  N N   . THR D 1080 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1077 THR A N   
9597  C CA  . THR D 1080 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1077 THR A CA  
9598  C C   . THR D 1080 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1077 THR A C   
9599  O O   . THR D 1080 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1077 THR A O   
9600  C CB  . THR D 1080 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1077 THR A CB  
9601  O OG1 . THR D 1080 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1077 THR A OG1 
9602  C CG2 . THR D 1080 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1077 THR A CG2 
9603  N N   . GLY D 1081 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1078 GLY A N   
9604  C CA  . GLY D 1081 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1078 GLY A CA  
9605  C C   . GLY D 1081 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1078 GLY A C   
9606  O O   . GLY D 1081 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1078 GLY A O   
9607  N N   . PHE D 1082 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1079 PHE A N   
9608  C CA  . PHE D 1082 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1079 PHE A CA  
9609  C C   . PHE D 1082 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1079 PHE A C   
9610  O O   . PHE D 1082 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1079 PHE A O   
9611  C CB  . PHE D 1082 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1079 PHE A CB  
9612  C CG  . PHE D 1082 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1079 PHE A CG  
9613  C CD1 . PHE D 1082 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1079 PHE A CD1 
9614  C CD2 . PHE D 1082 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1079 PHE A CD2 
9615  C CE1 . PHE D 1082 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1079 PHE A CE1 
9616  C CE2 . PHE D 1082 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1079 PHE A CE2 
9617  C CZ  . PHE D 1082 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1079 PHE A CZ  
9618  N N   . VAL D 1083 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1080 VAL A N   
9619  C CA  . VAL D 1083 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1080 VAL A CA  
9620  C C   . VAL D 1083 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1080 VAL A C   
9621  O O   . VAL D 1083 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1080 VAL A O   
9622  C CB  . VAL D 1083 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1080 VAL A CB  
9623  C CG1 . VAL D 1083 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1080 VAL A CG1 
9624  C CG2 . VAL D 1083 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1080 VAL A CG2 
9625  N N   . ASP D 1084 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1081 ASP A N   
9626  C CA  . ASP D 1084 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1081 ASP A CA  
9627  C C   . ASP D 1084 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1081 ASP A C   
9628  O O   . ASP D 1084 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1081 ASP A O   
9629  C CB  . ASP D 1084 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1081 ASP A CB  
9630  C CG  . ASP D 1084 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1081 ASP A CG  
9631  O OD1 . ASP D 1084 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1081 ASP A OD1 
9632  O OD2 . ASP D 1084 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1081 ASP A OD2 
9633  N N   . PRO D 1085 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1082 PRO A N   
9634  C CA  . PRO D 1085 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1082 PRO A CA  
9635  C C   . PRO D 1085 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1082 PRO A C   
9636  O O   . PRO D 1085 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1082 PRO A O   
9637  C CB  . PRO D 1085 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1082 PRO A CB  
9638  C CG  . PRO D 1085 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1082 PRO A CG  
9639  C CD  . PRO D 1085 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1082 PRO A CD  
9640  N N   . PHE D 1086 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1083 PHE A N   
9641  C CA  . PHE D 1086 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1083 PHE A CA  
9642  C C   . PHE D 1086 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1083 PHE A C   
9643  O O   . PHE D 1086 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1083 PHE A O   
9644  C CB  . PHE D 1086 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1083 PHE A CB  
9645  C CG  . PHE D 1086 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1083 PHE A CG  
9646  C CD1 . PHE D 1086 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1083 PHE A CD1 
9647  C CD2 . PHE D 1086 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1083 PHE A CD2 
9648  C CE1 . PHE D 1086 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1083 PHE A CE1 
9649  C CE2 . PHE D 1086 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1083 PHE A CE2 
9650  C CZ  . PHE D 1086 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1083 PHE A CZ  
9651  N N   . VAL D 1087 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1084 VAL A N   
9652  C CA  . VAL D 1087 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1084 VAL A CA  
9653  C C   . VAL D 1087 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1084 VAL A C   
9654  O O   . VAL D 1087 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1084 VAL A O   
9655  C CB  . VAL D 1087 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1084 VAL A CB  
9656  C CG1 . VAL D 1087 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1084 VAL A CG1 
9657  C CG2 . VAL D 1087 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1084 VAL A CG2 
9658  N N   . TRP D 1088 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1085 TRP A N   
9659  C CA  . TRP D 1088 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1085 TRP A CA  
9660  C C   . TRP D 1088 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1085 TRP A C   
9661  O O   . TRP D 1088 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1085 TRP A O   
9662  C CB  . TRP D 1088 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1085 TRP A CB  
9663  C CG  . TRP D 1088 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1085 TRP A CG  
9664  C CD1 . TRP D 1088 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1085 TRP A CD1 
9665  C CD2 . TRP D 1088 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1085 TRP A CD2 
9666  N NE1 . TRP D 1088 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1085 TRP A NE1 
9667  C CE2 . TRP D 1088 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1085 TRP A CE2 
9668  C CE3 . TRP D 1088 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1085 TRP A CE3 
9669  C CZ2 . TRP D 1088 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1085 TRP A CZ2 
9670  C CZ3 . TRP D 1088 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1085 TRP A CZ3 
9671  C CH2 . TRP D 1088 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1085 TRP A CH2 
9672  N N   . LYS D 1089 ? 0.7229 0.7229 0.7229 0.0000  0.0000  0.0000  1086 LYS A N   
9673  C CA  . LYS D 1089 ? 0.7229 0.7229 0.7229 0.0000  0.0000  0.0000  1086 LYS A CA  
9674  C C   . LYS D 1089 ? 0.7229 0.7229 0.7229 0.0000  0.0000  0.0000  1086 LYS A C   
9675  O O   . LYS D 1089 ? 0.7229 0.7229 0.7229 0.0000  0.0000  0.0000  1086 LYS A O   
9676  C CB  . LYS D 1089 ? 0.7229 0.7229 0.7229 0.0000  0.0000  0.0000  1086 LYS A CB  
9677  C CG  . LYS D 1089 ? 0.7229 0.7229 0.7229 0.0000  0.0000  0.0000  1086 LYS A CG  
9678  C CD  . LYS D 1089 ? 0.7229 0.7229 0.7229 0.0000  0.0000  0.0000  1086 LYS A CD  
9679  C CE  . LYS D 1089 ? 0.7229 0.7229 0.7229 0.0000  0.0000  0.0000  1086 LYS A CE  
9680  N NZ  . LYS D 1089 ? 0.7229 0.7229 0.7229 0.0000  0.0000  0.0000  1086 LYS A NZ  
9681  N N   . THR D 1090 ? 0.6796 0.6796 0.6796 0.0000  0.0000  0.0000  1087 THR A N   
9682  C CA  . THR D 1090 ? 0.6796 0.6796 0.6796 0.0000  0.0000  0.0000  1087 THR A CA  
9683  C C   . THR D 1090 ? 0.6796 0.6796 0.6796 0.0000  0.0000  0.0000  1087 THR A C   
9684  O O   . THR D 1090 ? 0.6796 0.6796 0.6796 0.0000  0.0000  0.0000  1087 THR A O   
9685  C CB  . THR D 1090 ? 0.6796 0.6796 0.6796 0.0000  0.0000  0.0000  1087 THR A CB  
9686  O OG1 . THR D 1090 ? 0.6796 0.6796 0.6796 0.0000  0.0000  0.0000  1087 THR A OG1 
9687  C CG2 . THR D 1090 ? 0.6796 0.6796 0.6796 0.0000  0.0000  0.0000  1087 THR A CG2 
9688  N N   . ILE D 1091 ? 0.7019 0.7019 0.7019 0.0000  0.0000  0.0000  1088 ILE A N   
9689  C CA  . ILE D 1091 ? 0.7019 0.7019 0.7019 0.0000  0.0000  0.0000  1088 ILE A CA  
9690  C C   . ILE D 1091 ? 0.7019 0.7019 0.7019 0.0000  0.0000  0.0000  1088 ILE A C   
9691  O O   . ILE D 1091 ? 0.7019 0.7019 0.7019 0.0000  0.0000  0.0000  1088 ILE A O   
9692  C CB  . ILE D 1091 ? 0.7019 0.7019 0.7019 0.0000  0.0000  0.0000  1088 ILE A CB  
9693  C CG1 . ILE D 1091 ? 0.7019 0.7019 0.7019 0.0000  0.0000  0.0000  1088 ILE A CG1 
9694  C CG2 . ILE D 1091 ? 0.7019 0.7019 0.7019 0.0000  0.0000  0.0000  1088 ILE A CG2 
9695  C CD1 . ILE D 1091 ? 0.7019 0.7019 0.7019 0.0000  0.0000  0.0000  1088 ILE A CD1 
9696  N N   . LYS D 1092 ? 0.7542 0.7542 0.7542 0.0000  0.0000  0.0000  1089 LYS A N   
9697  C CA  . LYS D 1092 ? 0.7542 0.7542 0.7542 0.0000  0.0000  0.0000  1089 LYS A CA  
9698  C C   . LYS D 1092 ? 0.7542 0.7542 0.7542 0.0000  0.0000  0.0000  1089 LYS A C   
9699  O O   . LYS D 1092 ? 0.7542 0.7542 0.7542 0.0000  0.0000  0.0000  1089 LYS A O   
9705  N N   . ASN D 1093 ? 0.7670 0.7670 0.7670 0.0000  0.0000  0.0000  1090 ASN A N   
9706  C CA  . ASN D 1093 ? 0.7670 0.7670 0.7670 0.0000  0.0000  0.0000  1090 ASN A CA  
9707  C C   . ASN D 1093 ? 0.7670 0.7670 0.7670 0.0000  0.0000  0.0000  1090 ASN A C   
9708  O O   . ASN D 1093 ? 0.7670 0.7670 0.7670 0.0000  0.0000  0.0000  1090 ASN A O   
9709  C CB  . ASN D 1093 ? 0.7670 0.7670 0.7670 0.0000  0.0000  0.0000  1090 ASN A CB  
9710  C CG  . ASN D 1093 ? 0.7670 0.7670 0.7670 0.0000  0.0000  0.0000  1090 ASN A CG  
9711  O OD1 . ASN D 1093 ? 0.7670 0.7670 0.7670 0.0000  0.0000  0.0000  1090 ASN A OD1 
9712  N ND2 . ASN D 1093 ? 0.7670 0.7670 0.7670 0.0000  0.0000  0.0000  1090 ASN A ND2 
9713  N N   . HIS D 1094 ? 0.7649 0.7649 0.7649 0.0000  0.0000  0.0000  1091 HIS A N   
9714  C CA  . HIS D 1094 ? 0.7649 0.7649 0.7649 0.0000  0.0000  0.0000  1091 HIS A CA  
9715  C C   . HIS D 1094 ? 0.7649 0.7649 0.7649 0.0000  0.0000  0.0000  1091 HIS A C   
9716  O O   . HIS D 1094 ? 0.7649 0.7649 0.7649 0.0000  0.0000  0.0000  1091 HIS A O   
9717  C CB  . HIS D 1094 ? 0.7649 0.7649 0.7649 0.0000  0.0000  0.0000  1091 HIS A CB  
9718  C CG  . HIS D 1094 ? 0.7649 0.7649 0.7649 0.0000  0.0000  0.0000  1091 HIS A CG  
9719  N ND1 . HIS D 1094 ? 0.7649 0.7649 0.7649 0.0000  0.0000  0.0000  1091 HIS A ND1 
9720  C CD2 . HIS D 1094 ? 0.7649 0.7649 0.7649 0.0000  0.0000  0.0000  1091 HIS A CD2 
9721  C CE1 . HIS D 1094 ? 0.7649 0.7649 0.7649 0.0000  0.0000  0.0000  1091 HIS A CE1 
9722  N NE2 . HIS D 1094 ? 0.7649 0.7649 0.7649 0.0000  0.0000  0.0000  1091 HIS A NE2 
9723  N N   . GLU D 1095 ? 0.7877 0.7877 0.7877 0.0000  0.0000  0.0000  1092 GLU A N   
9724  C CA  . GLU D 1095 ? 0.7877 0.7877 0.7877 0.0000  0.0000  0.0000  1092 GLU A CA  
9725  C C   . GLU D 1095 ? 0.7877 0.7877 0.7877 0.0000  0.0000  0.0000  1092 GLU A C   
9726  O O   . GLU D 1095 ? 0.7877 0.7877 0.7877 0.0000  0.0000  0.0000  1092 GLU A O   
9727  C CB  . GLU D 1095 ? 0.7877 0.7877 0.7877 0.0000  0.0000  0.0000  1092 GLU A CB  
9728  C CG  . GLU D 1095 ? 0.7877 0.7877 0.7877 0.0000  0.0000  0.0000  1092 GLU A CG  
9729  C CD  . GLU D 1095 ? 0.7877 0.7877 0.7877 0.0000  0.0000  0.0000  1092 GLU A CD  
9730  O OE1 . GLU D 1095 ? 0.7877 0.7877 0.7877 0.0000  0.0000  0.0000  1092 GLU A OE1 
9731  O OE2 . GLU D 1095 ? 0.7877 0.7877 0.7877 0.0000  0.0000  0.0000  1092 GLU A OE2 
9732  N N   . SER D 1096 ? 0.7585 0.7585 0.7585 0.0000  0.0000  0.0000  1093 SER A N   
9733  C CA  . SER D 1096 ? 0.7585 0.7585 0.7585 0.0000  0.0000  0.0000  1093 SER A CA  
9734  C C   . SER D 1096 ? 0.7585 0.7585 0.7585 0.0000  0.0000  0.0000  1093 SER A C   
9735  O O   . SER D 1096 ? 0.7585 0.7585 0.7585 0.0000  0.0000  0.0000  1093 SER A O   
9736  C CB  . SER D 1096 ? 0.7585 0.7585 0.7585 0.0000  0.0000  0.0000  1093 SER A CB  
9737  O OG  . SER D 1096 ? 0.7585 0.7585 0.7585 0.0000  0.0000  0.0000  1093 SER A OG  
9738  N N   . ARG D 1097 ? 0.7053 0.7053 0.7053 0.0000  0.0000  0.0000  1094 ARG A N   
9739  C CA  . ARG D 1097 ? 0.7053 0.7053 0.7053 0.0000  0.0000  0.0000  1094 ARG A CA  
9740  C C   . ARG D 1097 ? 0.7053 0.7053 0.7053 0.0000  0.0000  0.0000  1094 ARG A C   
9741  O O   . ARG D 1097 ? 0.7053 0.7053 0.7053 0.0000  0.0000  0.0000  1094 ARG A O   
9742  C CB  . ARG D 1097 ? 0.7053 0.7053 0.7053 0.0000  0.0000  0.0000  1094 ARG A CB  
9743  C CG  . ARG D 1097 ? 0.7053 0.7053 0.7053 0.0000  0.0000  0.0000  1094 ARG A CG  
9744  C CD  . ARG D 1097 ? 0.7053 0.7053 0.7053 0.0000  0.0000  0.0000  1094 ARG A CD  
9745  N NE  . ARG D 1097 ? 0.7053 0.7053 0.7053 0.0000  0.0000  0.0000  1094 ARG A NE  
9746  C CZ  . ARG D 1097 ? 0.7053 0.7053 0.7053 0.0000  0.0000  0.0000  1094 ARG A CZ  
9747  N NH1 . ARG D 1097 ? 0.7053 0.7053 0.7053 0.0000  0.0000  0.0000  1094 ARG A NH1 
9748  N NH2 . ARG D 1097 ? 0.7053 0.7053 0.7053 0.0000  0.0000  0.0000  1094 ARG A NH2 
9749  N N   . LYS D 1098 ? 0.7268 0.7268 0.7268 0.0000  0.0000  0.0000  1095 LYS A N   
9750  C CA  . LYS D 1098 ? 0.7268 0.7268 0.7268 0.0000  0.0000  0.0000  1095 LYS A CA  
9751  C C   . LYS D 1098 ? 0.7268 0.7268 0.7268 0.0000  0.0000  0.0000  1095 LYS A C   
9752  O O   . LYS D 1098 ? 0.7268 0.7268 0.7268 0.0000  0.0000  0.0000  1095 LYS A O   
9758  N N   . HIS D 1099 ? 0.7434 0.7434 0.7434 0.0000  0.0000  0.0000  1096 HIS A N   
9759  C CA  . HIS D 1099 ? 0.7434 0.7434 0.7434 0.0000  0.0000  0.0000  1096 HIS A CA  
9760  C C   . HIS D 1099 ? 0.7434 0.7434 0.7434 0.0000  0.0000  0.0000  1096 HIS A C   
9761  O O   . HIS D 1099 ? 0.7434 0.7434 0.7434 0.0000  0.0000  0.0000  1096 HIS A O   
9762  C CB  . HIS D 1099 ? 0.7434 0.7434 0.7434 0.0000  0.0000  0.0000  1096 HIS A CB  
9763  C CG  . HIS D 1099 ? 0.7434 0.7434 0.7434 0.0000  0.0000  0.0000  1096 HIS A CG  
9764  N ND1 . HIS D 1099 ? 0.7434 0.7434 0.7434 0.0000  0.0000  0.0000  1096 HIS A ND1 
9765  C CD2 . HIS D 1099 ? 0.7434 0.7434 0.7434 0.0000  0.0000  0.0000  1096 HIS A CD2 
9766  C CE1 . HIS D 1099 ? 0.7434 0.7434 0.7434 0.0000  0.0000  0.0000  1096 HIS A CE1 
9767  N NE2 . HIS D 1099 ? 0.7434 0.7434 0.7434 0.0000  0.0000  0.0000  1096 HIS A NE2 
9768  N N   . PHE D 1100 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1097 PHE A N   
9769  C CA  . PHE D 1100 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1097 PHE A CA  
9770  C C   . PHE D 1100 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1097 PHE A C   
9771  O O   . PHE D 1100 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1097 PHE A O   
9772  C CB  . PHE D 1100 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1097 PHE A CB  
9773  C CG  . PHE D 1100 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1097 PHE A CG  
9774  C CD1 . PHE D 1100 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1097 PHE A CD1 
9775  C CD2 . PHE D 1100 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1097 PHE A CD2 
9776  C CE1 . PHE D 1100 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1097 PHE A CE1 
9777  C CE2 . PHE D 1100 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1097 PHE A CE2 
9778  C CZ  . PHE D 1100 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1097 PHE A CZ  
9779  N N   . LEU D 1101 ? 0.6541 0.6541 0.6541 0.0000  0.0000  0.0000  1098 LEU A N   
9780  C CA  . LEU D 1101 ? 0.6541 0.6541 0.6541 0.0000  0.0000  0.0000  1098 LEU A CA  
9781  C C   . LEU D 1101 ? 0.6541 0.6541 0.6541 0.0000  0.0000  0.0000  1098 LEU A C   
9782  O O   . LEU D 1101 ? 0.6541 0.6541 0.6541 0.0000  0.0000  0.0000  1098 LEU A O   
9783  C CB  . LEU D 1101 ? 0.6541 0.6541 0.6541 0.0000  0.0000  0.0000  1098 LEU A CB  
9784  C CG  . LEU D 1101 ? 0.6541 0.6541 0.6541 0.0000  0.0000  0.0000  1098 LEU A CG  
9785  C CD1 . LEU D 1101 ? 0.6541 0.6541 0.6541 0.0000  0.0000  0.0000  1098 LEU A CD1 
9786  C CD2 . LEU D 1101 ? 0.6541 0.6541 0.6541 0.0000  0.0000  0.0000  1098 LEU A CD2 
9787  N N   . GLU D 1102 ? 0.7153 0.7153 0.7153 0.0000  0.0000  0.0000  1099 GLU A N   
9788  C CA  . GLU D 1102 ? 0.7153 0.7153 0.7153 0.0000  0.0000  0.0000  1099 GLU A CA  
9789  C C   . GLU D 1102 ? 0.7153 0.7153 0.7153 0.0000  0.0000  0.0000  1099 GLU A C   
9790  O O   . GLU D 1102 ? 0.7153 0.7153 0.7153 0.0000  0.0000  0.0000  1099 GLU A O   
9791  C CB  . GLU D 1102 ? 0.7153 0.7153 0.7153 0.0000  0.0000  0.0000  1099 GLU A CB  
9792  C CG  . GLU D 1102 ? 0.7153 0.7153 0.7153 0.0000  0.0000  0.0000  1099 GLU A CG  
9793  C CD  . GLU D 1102 ? 0.7153 0.7153 0.7153 0.0000  0.0000  0.0000  1099 GLU A CD  
9794  O OE1 . GLU D 1102 ? 0.7153 0.7153 0.7153 0.0000  0.0000  0.0000  1099 GLU A OE1 
9795  O OE2 . GLU D 1102 ? 0.7153 0.7153 0.7153 0.0000  0.0000  0.0000  1099 GLU A OE2 
9796  N N   . GLY D 1103 ? 0.6374 0.6374 0.6374 0.0000  0.0000  0.0000  1100 GLY A N   
9797  C CA  . GLY D 1103 ? 0.6374 0.6374 0.6374 0.0000  0.0000  0.0000  1100 GLY A CA  
9798  C C   . GLY D 1103 ? 0.6374 0.6374 0.6374 0.0000  0.0000  0.0000  1100 GLY A C   
9799  O O   . GLY D 1103 ? 0.6374 0.6374 0.6374 0.0000  0.0000  0.0000  1100 GLY A O   
9800  N N   . PHE D 1104 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1101 PHE A N   
9801  C CA  . PHE D 1104 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1101 PHE A CA  
9802  C C   . PHE D 1104 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1101 PHE A C   
9803  O O   . PHE D 1104 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1101 PHE A O   
9804  C CB  . PHE D 1104 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1101 PHE A CB  
9805  C CG  . PHE D 1104 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1101 PHE A CG  
9806  C CD1 . PHE D 1104 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1101 PHE A CD1 
9807  C CD2 . PHE D 1104 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1101 PHE A CD2 
9808  C CE1 . PHE D 1104 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1101 PHE A CE1 
9809  C CE2 . PHE D 1104 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1101 PHE A CE2 
9810  C CZ  . PHE D 1104 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1101 PHE A CZ  
9811  N N   . ASP D 1105 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1102 ASP A N   
9812  C CA  . ASP D 1105 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1102 ASP A CA  
9813  C C   . ASP D 1105 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1102 ASP A C   
9814  O O   . ASP D 1105 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1102 ASP A O   
9815  C CB  . ASP D 1105 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1102 ASP A CB  
9816  C CG  . ASP D 1105 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1102 ASP A CG  
9817  O OD1 . ASP D 1105 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1102 ASP A OD1 
9818  O OD2 . ASP D 1105 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1102 ASP A OD2 
9819  N N   . PHE D 1106 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1103 PHE A N   
9820  C CA  . PHE D 1106 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1103 PHE A CA  
9821  C C   . PHE D 1106 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1103 PHE A C   
9822  O O   . PHE D 1106 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1103 PHE A O   
9823  C CB  . PHE D 1106 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1103 PHE A CB  
9824  C CG  . PHE D 1106 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1103 PHE A CG  
9825  C CD1 . PHE D 1106 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1103 PHE A CD1 
9826  C CD2 . PHE D 1106 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1103 PHE A CD2 
9827  C CE1 . PHE D 1106 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1103 PHE A CE1 
9828  C CE2 . PHE D 1106 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1103 PHE A CE2 
9829  C CZ  . PHE D 1106 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1103 PHE A CZ  
9830  N N   . LEU D 1107 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1104 LEU A N   
9831  C CA  . LEU D 1107 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1104 LEU A CA  
9832  C C   . LEU D 1107 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1104 LEU A C   
9833  O O   . LEU D 1107 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1104 LEU A O   
9834  C CB  . LEU D 1107 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1104 LEU A CB  
9835  C CG  . LEU D 1107 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1104 LEU A CG  
9836  C CD1 . LEU D 1107 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1104 LEU A CD1 
9837  C CD2 . LEU D 1107 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1104 LEU A CD2 
9838  N N   . HIS D 1108 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1105 HIS A N   
9839  C CA  . HIS D 1108 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1105 HIS A CA  
9840  C C   . HIS D 1108 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1105 HIS A C   
9841  O O   . HIS D 1108 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1105 HIS A O   
9842  C CB  . HIS D 1108 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1105 HIS A CB  
9843  C CG  . HIS D 1108 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1105 HIS A CG  
9844  N ND1 . HIS D 1108 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1105 HIS A ND1 
9845  C CD2 . HIS D 1108 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1105 HIS A CD2 
9846  C CE1 . HIS D 1108 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1105 HIS A CE1 
9847  N NE2 . HIS D 1108 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1105 HIS A NE2 
9848  N N   . TYR D 1109 ? 0.6371 0.6371 0.6371 0.0000  0.0000  0.0000  1106 TYR A N   
9849  C CA  . TYR D 1109 ? 0.6371 0.6371 0.6371 0.0000  0.0000  0.0000  1106 TYR A CA  
9850  C C   . TYR D 1109 ? 0.6371 0.6371 0.6371 0.0000  0.0000  0.0000  1106 TYR A C   
9851  O O   . TYR D 1109 ? 0.6371 0.6371 0.6371 0.0000  0.0000  0.0000  1106 TYR A O   
9852  C CB  . TYR D 1109 ? 0.6371 0.6371 0.6371 0.0000  0.0000  0.0000  1106 TYR A CB  
9853  C CG  . TYR D 1109 ? 0.6371 0.6371 0.6371 0.0000  0.0000  0.0000  1106 TYR A CG  
9854  C CD1 . TYR D 1109 ? 0.6371 0.6371 0.6371 0.0000  0.0000  0.0000  1106 TYR A CD1 
9855  C CD2 . TYR D 1109 ? 0.6371 0.6371 0.6371 0.0000  0.0000  0.0000  1106 TYR A CD2 
9856  C CE1 . TYR D 1109 ? 0.6371 0.6371 0.6371 0.0000  0.0000  0.0000  1106 TYR A CE1 
9857  C CE2 . TYR D 1109 ? 0.6371 0.6371 0.6371 0.0000  0.0000  0.0000  1106 TYR A CE2 
9858  C CZ  . TYR D 1109 ? 0.6371 0.6371 0.6371 0.0000  0.0000  0.0000  1106 TYR A CZ  
9859  O OH  . TYR D 1109 ? 0.6371 0.6371 0.6371 0.0000  0.0000  0.0000  1106 TYR A OH  
9860  N N   . ASP D 1110 ? 0.6743 0.6743 0.6743 0.0000  0.0000  0.0000  1107 ASP A N   
9861  C CA  . ASP D 1110 ? 0.6743 0.6743 0.6743 0.0000  0.0000  0.0000  1107 ASP A CA  
9862  C C   . ASP D 1110 ? 0.6743 0.6743 0.6743 0.0000  0.0000  0.0000  1107 ASP A C   
9863  O O   . ASP D 1110 ? 0.6743 0.6743 0.6743 0.0000  0.0000  0.0000  1107 ASP A O   
9864  C CB  . ASP D 1110 ? 0.6743 0.6743 0.6743 0.0000  0.0000  0.0000  1107 ASP A CB  
9865  C CG  . ASP D 1110 ? 0.6743 0.6743 0.6743 0.0000  0.0000  0.0000  1107 ASP A CG  
9866  O OD1 . ASP D 1110 ? 0.6743 0.6743 0.6743 0.0000  0.0000  0.0000  1107 ASP A OD1 
9867  O OD2 . ASP D 1110 ? 0.6743 0.6743 0.6743 0.0000  0.0000  0.0000  1107 ASP A OD2 
9868  N N   . VAL D 1111 ? 0.6654 0.6654 0.6654 0.0000  0.0000  0.0000  1108 VAL A N   
9869  C CA  . VAL D 1111 ? 0.6654 0.6654 0.6654 0.0000  0.0000  0.0000  1108 VAL A CA  
9870  C C   . VAL D 1111 ? 0.6654 0.6654 0.6654 0.0000  0.0000  0.0000  1108 VAL A C   
9871  O O   . VAL D 1111 ? 0.6654 0.6654 0.6654 0.0000  0.0000  0.0000  1108 VAL A O   
9872  C CB  . VAL D 1111 ? 0.6654 0.6654 0.6654 0.0000  0.0000  0.0000  1108 VAL A CB  
9873  C CG1 . VAL D 1111 ? 0.6654 0.6654 0.6654 0.0000  0.0000  0.0000  1108 VAL A CG1 
9874  C CG2 . VAL D 1111 ? 0.6654 0.6654 0.6654 0.0000  0.0000  0.0000  1108 VAL A CG2 
9875  N N   . LYS D 1112 ? 0.6789 0.6789 0.6789 0.0000  0.0000  0.0000  1109 LYS A N   
9876  C CA  . LYS D 1112 ? 0.6789 0.6789 0.6789 0.0000  0.0000  0.0000  1109 LYS A CA  
9877  C C   . LYS D 1112 ? 0.6789 0.6789 0.6789 0.0000  0.0000  0.0000  1109 LYS A C   
9878  O O   . LYS D 1112 ? 0.6789 0.6789 0.6789 0.0000  0.0000  0.0000  1109 LYS A O   
9884  N N   . THR D 1113 ? 0.6473 0.6473 0.6473 0.0000  0.0000  0.0000  1110 THR A N   
9885  C CA  . THR D 1113 ? 0.6473 0.6473 0.6473 0.0000  0.0000  0.0000  1110 THR A CA  
9886  C C   . THR D 1113 ? 0.6473 0.6473 0.6473 0.0000  0.0000  0.0000  1110 THR A C   
9887  O O   . THR D 1113 ? 0.6473 0.6473 0.6473 0.0000  0.0000  0.0000  1110 THR A O   
9888  C CB  . THR D 1113 ? 0.6473 0.6473 0.6473 0.0000  0.0000  0.0000  1110 THR A CB  
9889  O OG1 . THR D 1113 ? 0.6473 0.6473 0.6473 0.0000  0.0000  0.0000  1110 THR A OG1 
9890  C CG2 . THR D 1113 ? 0.6473 0.6473 0.6473 0.0000  0.0000  0.0000  1110 THR A CG2 
9891  N N   . GLY D 1114 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1111 GLY A N   
9892  C CA  . GLY D 1114 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1111 GLY A CA  
9893  C C   . GLY D 1114 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1111 GLY A C   
9894  O O   . GLY D 1114 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1111 GLY A O   
9895  N N   . ASP D 1115 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1112 ASP A N   
9896  C CA  . ASP D 1115 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1112 ASP A CA  
9897  C C   . ASP D 1115 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1112 ASP A C   
9898  O O   . ASP D 1115 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1112 ASP A O   
9899  C CB  . ASP D 1115 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1112 ASP A CB  
9900  C CG  . ASP D 1115 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1112 ASP A CG  
9901  O OD1 . ASP D 1115 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1112 ASP A OD1 
9902  O OD2 . ASP D 1115 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1112 ASP A OD2 
9903  N N   . PHE D 1116 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1113 PHE A N   
9904  C CA  . PHE D 1116 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1113 PHE A CA  
9905  C C   . PHE D 1116 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1113 PHE A C   
9906  O O   . PHE D 1116 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1113 PHE A O   
9907  C CB  . PHE D 1116 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1113 PHE A CB  
9908  C CG  . PHE D 1116 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1113 PHE A CG  
9909  C CD1 . PHE D 1116 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1113 PHE A CD1 
9910  C CD2 . PHE D 1116 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1113 PHE A CD2 
9911  C CE1 . PHE D 1116 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1113 PHE A CE1 
9912  C CE2 . PHE D 1116 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1113 PHE A CE2 
9913  C CZ  . PHE D 1116 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1113 PHE A CZ  
9914  N N   . ILE D 1117 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1114 ILE A N   
9915  C CA  . ILE D 1117 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1114 ILE A CA  
9916  C C   . ILE D 1117 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1114 ILE A C   
9917  O O   . ILE D 1117 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1114 ILE A O   
9918  C CB  . ILE D 1117 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1114 ILE A CB  
9919  C CG1 . ILE D 1117 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1114 ILE A CG1 
9920  C CG2 . ILE D 1117 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1114 ILE A CG2 
9921  C CD1 . ILE D 1117 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1114 ILE A CD1 
9922  N N   . LEU D 1118 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1115 LEU A N   
9923  C CA  . LEU D 1118 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1115 LEU A CA  
9924  C C   . LEU D 1118 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1115 LEU A C   
9925  O O   . LEU D 1118 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1115 LEU A O   
9926  C CB  . LEU D 1118 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1115 LEU A CB  
9927  C CG  . LEU D 1118 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1115 LEU A CG  
9928  C CD1 . LEU D 1118 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1115 LEU A CD1 
9929  C CD2 . LEU D 1118 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1115 LEU A CD2 
9930  N N   . HIS D 1119 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1116 HIS A N   
9931  C CA  . HIS D 1119 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1116 HIS A CA  
9932  C C   . HIS D 1119 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1116 HIS A C   
9933  O O   . HIS D 1119 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1116 HIS A O   
9934  C CB  . HIS D 1119 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1116 HIS A CB  
9935  C CG  . HIS D 1119 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1116 HIS A CG  
9936  N ND1 . HIS D 1119 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1116 HIS A ND1 
9937  C CD2 . HIS D 1119 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1116 HIS A CD2 
9938  C CE1 . HIS D 1119 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1116 HIS A CE1 
9939  N NE2 . HIS D 1119 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1116 HIS A NE2 
9940  N N   . PHE D 1120 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1117 PHE A N   
9941  C CA  . PHE D 1120 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1117 PHE A CA  
9942  C C   . PHE D 1120 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1117 PHE A C   
9943  O O   . PHE D 1120 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1117 PHE A O   
9944  C CB  . PHE D 1120 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1117 PHE A CB  
9945  C CG  . PHE D 1120 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1117 PHE A CG  
9946  C CD1 . PHE D 1120 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1117 PHE A CD1 
9947  C CD2 . PHE D 1120 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1117 PHE A CD2 
9948  C CE1 . PHE D 1120 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1117 PHE A CE1 
9949  C CE2 . PHE D 1120 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1117 PHE A CE2 
9950  C CZ  . PHE D 1120 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1117 PHE A CZ  
9951  N N   . LYS D 1121 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1118 LYS A N   
9952  C CA  . LYS D 1121 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1118 LYS A CA  
9953  C C   . LYS D 1121 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1118 LYS A C   
9954  O O   . LYS D 1121 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1118 LYS A O   
9955  C CB  . LYS D 1121 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1118 LYS A CB  
9956  C CG  . LYS D 1121 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1118 LYS A CG  
9957  C CD  . LYS D 1121 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1118 LYS A CD  
9958  C CE  . LYS D 1121 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1118 LYS A CE  
9959  N NZ  . LYS D 1121 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1118 LYS A NZ  
9960  N N   . MET D 1122 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1119 MET A N   
9961  C CA  . MET D 1122 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1119 MET A CA  
9962  C C   . MET D 1122 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1119 MET A C   
9963  O O   . MET D 1122 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1119 MET A O   
9964  C CB  . MET D 1122 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1119 MET A CB  
9965  C CG  . MET D 1122 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1119 MET A CG  
9966  S SD  . MET D 1122 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1119 MET A SD  
9967  C CE  . MET D 1122 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1119 MET A CE  
9968  N N   . ASN D 1123 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1120 ASN A N   
9969  C CA  . ASN D 1123 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1120 ASN A CA  
9970  C C   . ASN D 1123 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1120 ASN A C   
9971  O O   . ASN D 1123 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1120 ASN A O   
9972  C CB  . ASN D 1123 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1120 ASN A CB  
9973  C CG  . ASN D 1123 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1120 ASN A CG  
9974  O OD1 . ASN D 1123 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1120 ASN A OD1 
9975  N ND2 . ASN D 1123 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1120 ASN A ND2 
9976  N N   . ARG D 1124 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1121 ARG A N   
9977  C CA  . ARG D 1124 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1121 ARG A CA  
9978  C C   . ARG D 1124 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1121 ARG A C   
9979  O O   . ARG D 1124 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1121 ARG A O   
9980  C CB  . ARG D 1124 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1121 ARG A CB  
9981  C CG  . ARG D 1124 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1121 ARG A CG  
9982  C CD  . ARG D 1124 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1121 ARG A CD  
9983  N NE  . ARG D 1124 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1121 ARG A NE  
9984  C CZ  . ARG D 1124 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1121 ARG A CZ  
9985  N NH1 . ARG D 1124 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1121 ARG A NH1 
9986  N NH2 . ARG D 1124 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1121 ARG A NH2 
9987  N N   . ASN D 1125 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1122 ASN A N   
9988  C CA  . ASN D 1125 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1122 ASN A CA  
9989  C C   . ASN D 1125 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1122 ASN A C   
9990  O O   . ASN D 1125 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1122 ASN A O   
9991  C CB  . ASN D 1125 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1122 ASN A CB  
9992  C CG  . ASN D 1125 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1122 ASN A CG  
9993  O OD1 . ASN D 1125 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1122 ASN A OD1 
9994  N ND2 . ASN D 1125 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1122 ASN A ND2 
9995  N N   . LEU D 1126 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1123 LEU A N   
9996  C CA  . LEU D 1126 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1123 LEU A CA  
9997  C C   . LEU D 1126 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1123 LEU A C   
9998  O O   . LEU D 1126 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1123 LEU A O   
9999  C CB  . LEU D 1126 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1123 LEU A CB  
10000 C CG  . LEU D 1126 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1123 LEU A CG  
10001 C CD1 . LEU D 1126 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1123 LEU A CD1 
10002 C CD2 . LEU D 1126 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1123 LEU A CD2 
10003 N N   . SER D 1127 ? 0.6495 0.6495 0.6495 0.0000  0.0000  0.0000  1124 SER A N   
10004 C CA  . SER D 1127 ? 0.6495 0.6495 0.6495 0.0000  0.0000  0.0000  1124 SER A CA  
10005 C C   . SER D 1127 ? 0.6495 0.6495 0.6495 0.0000  0.0000  0.0000  1124 SER A C   
10006 O O   . SER D 1127 ? 0.6495 0.6495 0.6495 0.0000  0.0000  0.0000  1124 SER A O   
10007 C CB  . SER D 1127 ? 0.6495 0.6495 0.6495 0.0000  0.0000  0.0000  1124 SER A CB  
10008 O OG  . SER D 1127 ? 0.6495 0.6495 0.6495 0.0000  0.0000  0.0000  1124 SER A OG  
10009 N N   . PHE D 1128 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1125 PHE A N   
10010 C CA  . PHE D 1128 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1125 PHE A CA  
10011 C C   . PHE D 1128 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1125 PHE A C   
10012 O O   . PHE D 1128 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1125 PHE A O   
10013 C CB  . PHE D 1128 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1125 PHE A CB  
10014 C CG  . PHE D 1128 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1125 PHE A CG  
10015 C CD1 . PHE D 1128 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1125 PHE A CD1 
10016 C CD2 . PHE D 1128 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1125 PHE A CD2 
10017 C CE1 . PHE D 1128 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1125 PHE A CE1 
10018 C CE2 . PHE D 1128 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1125 PHE A CE2 
10019 C CZ  . PHE D 1128 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1125 PHE A CZ  
10020 N N   . GLN D 1129 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1126 GLN A N   
10021 C CA  . GLN D 1129 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1126 GLN A CA  
10022 C C   . GLN D 1129 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1126 GLN A C   
10023 O O   . GLN D 1129 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1126 GLN A O   
10024 C CB  . GLN D 1129 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1126 GLN A CB  
10025 C CG  . GLN D 1129 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1126 GLN A CG  
10026 C CD  . GLN D 1129 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1126 GLN A CD  
10027 O OE1 . GLN D 1129 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1126 GLN A OE1 
10028 N NE2 . GLN D 1129 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1126 GLN A NE2 
10029 N N   . ARG D 1130 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1127 ARG A N   
10030 C CA  . ARG D 1130 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1127 ARG A CA  
10031 C C   . ARG D 1130 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1127 ARG A C   
10032 O O   . ARG D 1130 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1127 ARG A O   
10033 C CB  . ARG D 1130 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1127 ARG A CB  
10034 C CG  . ARG D 1130 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1127 ARG A CG  
10035 C CD  . ARG D 1130 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1127 ARG A CD  
10036 N NE  . ARG D 1130 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1127 ARG A NE  
10037 C CZ  . ARG D 1130 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1127 ARG A CZ  
10038 N NH1 . ARG D 1130 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1127 ARG A NH1 
10039 N NH2 . ARG D 1130 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1127 ARG A NH2 
10040 N N   . GLY D 1131 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1128 GLY A N   
10041 C CA  . GLY D 1131 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1128 GLY A CA  
10042 C C   . GLY D 1131 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1128 GLY A C   
10043 O O   . GLY D 1131 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1128 GLY A O   
10044 N N   . LEU D 1132 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1129 LEU A N   
10045 C CA  . LEU D 1132 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1129 LEU A CA  
10046 C C   . LEU D 1132 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1129 LEU A C   
10047 O O   . LEU D 1132 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1129 LEU A O   
10048 C CB  . LEU D 1132 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1129 LEU A CB  
10049 C CG  . LEU D 1132 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1129 LEU A CG  
10050 C CD1 . LEU D 1132 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1129 LEU A CD1 
10051 C CD2 . LEU D 1132 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1129 LEU A CD2 
10052 N N   . PRO D 1133 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1130 PRO A N   
10053 C CA  . PRO D 1133 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1130 PRO A CA  
10054 C C   . PRO D 1133 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1130 PRO A C   
10055 O O   . PRO D 1133 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1130 PRO A O   
10056 C CB  . PRO D 1133 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1130 PRO A CB  
10057 C CG  . PRO D 1133 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1130 PRO A CG  
10058 C CD  . PRO D 1133 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1130 PRO A CD  
10059 N N   . GLY D 1134 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1131 GLY A N   
10060 C CA  . GLY D 1134 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1131 GLY A CA  
10061 C C   . GLY D 1134 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1131 GLY A C   
10062 O O   . GLY D 1134 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1131 GLY A O   
10063 N N   . PHE D 1135 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1132 PHE A N   
10064 C CA  . PHE D 1135 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1132 PHE A CA  
10065 C C   . PHE D 1135 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1132 PHE A C   
10066 O O   . PHE D 1135 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1132 PHE A O   
10067 C CB  . PHE D 1135 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1132 PHE A CB  
10068 C CG  . PHE D 1135 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1132 PHE A CG  
10069 C CD1 . PHE D 1135 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1132 PHE A CD1 
10070 C CD2 . PHE D 1135 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1132 PHE A CD2 
10071 C CE1 . PHE D 1135 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1132 PHE A CE1 
10072 C CE2 . PHE D 1135 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1132 PHE A CE2 
10073 C CZ  . PHE D 1135 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1132 PHE A CZ  
10074 N N   . MET D 1136 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1133 MET A N   
10075 C CA  . MET D 1136 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1133 MET A CA  
10076 C C   . MET D 1136 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1133 MET A C   
10077 O O   . MET D 1136 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1133 MET A O   
10078 C CB  . MET D 1136 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1133 MET A CB  
10079 C CG  . MET D 1136 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1133 MET A CG  
10080 S SD  . MET D 1136 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1133 MET A SD  
10081 C CE  . MET D 1136 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1133 MET A CE  
10082 N N   . PRO D 1137 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1134 PRO A N   
10083 C CA  . PRO D 1137 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1134 PRO A CA  
10084 C C   . PRO D 1137 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1134 PRO A C   
10085 O O   . PRO D 1137 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1134 PRO A O   
10086 C CB  . PRO D 1137 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1134 PRO A CB  
10087 C CG  . PRO D 1137 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1134 PRO A CG  
10088 C CD  . PRO D 1137 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1134 PRO A CD  
10089 N N   . ALA D 1138 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1135 ALA A N   
10090 C CA  . ALA D 1138 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1135 ALA A CA  
10091 C C   . ALA D 1138 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1135 ALA A C   
10092 O O   . ALA D 1138 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1135 ALA A O   
10093 C CB  . ALA D 1138 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1135 ALA A CB  
10094 N N   . TRP D 1139 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1136 TRP A N   
10095 C CA  . TRP D 1139 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1136 TRP A CA  
10096 C C   . TRP D 1139 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1136 TRP A C   
10097 O O   . TRP D 1139 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1136 TRP A O   
10098 C CB  . TRP D 1139 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1136 TRP A CB  
10099 C CG  . TRP D 1139 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1136 TRP A CG  
10100 C CD1 . TRP D 1139 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1136 TRP A CD1 
10101 C CD2 . TRP D 1139 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1136 TRP A CD2 
10102 N NE1 . TRP D 1139 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1136 TRP A NE1 
10103 C CE2 . TRP D 1139 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1136 TRP A CE2 
10104 C CE3 . TRP D 1139 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1136 TRP A CE3 
10105 C CZ2 . TRP D 1139 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1136 TRP A CZ2 
10106 C CZ3 . TRP D 1139 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1136 TRP A CZ3 
10107 C CH2 . TRP D 1139 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1136 TRP A CH2 
10108 N N   . ASP D 1140 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1137 ASP A N   
10109 C CA  . ASP D 1140 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1137 ASP A CA  
10110 C C   . ASP D 1140 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1137 ASP A C   
10111 O O   . ASP D 1140 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1137 ASP A O   
10112 C CB  . ASP D 1140 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1137 ASP A CB  
10113 C CG  . ASP D 1140 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1137 ASP A CG  
10114 O OD1 . ASP D 1140 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1137 ASP A OD1 
10115 O OD2 . ASP D 1140 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1137 ASP A OD2 
10116 N N   . ILE D 1141 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1138 ILE A N   
10117 C CA  . ILE D 1141 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1138 ILE A CA  
10118 C C   . ILE D 1141 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1138 ILE A C   
10119 O O   . ILE D 1141 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1138 ILE A O   
10120 C CB  . ILE D 1141 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1138 ILE A CB  
10121 C CG1 . ILE D 1141 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1138 ILE A CG1 
10122 C CG2 . ILE D 1141 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1138 ILE A CG2 
10123 C CD1 . ILE D 1141 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1138 ILE A CD1 
10124 N N   . VAL D 1142 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1139 VAL A N   
10125 C CA  . VAL D 1142 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1139 VAL A CA  
10126 C C   . VAL D 1142 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1139 VAL A C   
10127 O O   . VAL D 1142 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1139 VAL A O   
10128 C CB  . VAL D 1142 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1139 VAL A CB  
10129 C CG1 . VAL D 1142 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1139 VAL A CG1 
10130 C CG2 . VAL D 1142 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1139 VAL A CG2 
10131 N N   . PHE D 1143 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1140 PHE A N   
10132 C CA  . PHE D 1143 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1140 PHE A CA  
10133 C C   . PHE D 1143 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1140 PHE A C   
10134 O O   . PHE D 1143 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1140 PHE A O   
10135 C CB  . PHE D 1143 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1140 PHE A CB  
10136 C CG  . PHE D 1143 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1140 PHE A CG  
10137 C CD1 . PHE D 1143 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1140 PHE A CD1 
10138 C CD2 . PHE D 1143 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1140 PHE A CD2 
10139 C CE1 . PHE D 1143 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1140 PHE A CE1 
10140 C CE2 . PHE D 1143 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1140 PHE A CE2 
10141 C CZ  . PHE D 1143 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1140 PHE A CZ  
10142 N N   . GLU D 1144 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1141 GLU A N   
10143 C CA  . GLU D 1144 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1141 GLU A CA  
10144 C C   . GLU D 1144 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1141 GLU A C   
10145 O O   . GLU D 1144 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1141 GLU A O   
10146 C CB  . GLU D 1144 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1141 GLU A CB  
10147 C CG  . GLU D 1144 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1141 GLU A CG  
10148 C CD  . GLU D 1144 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1141 GLU A CD  
10149 O OE1 . GLU D 1144 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1141 GLU A OE1 
10150 O OE2 . GLU D 1144 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1141 GLU A OE2 
10151 N N   . LYS D 1145 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1142 LYS A N   
10152 C CA  . LYS D 1145 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1142 LYS A CA  
10153 C C   . LYS D 1145 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1142 LYS A C   
10154 O O   . LYS D 1145 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1142 LYS A O   
10155 C CB  . LYS D 1145 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1142 LYS A CB  
10156 C CG  . LYS D 1145 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1142 LYS A CG  
10157 C CD  . LYS D 1145 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1142 LYS A CD  
10158 C CE  . LYS D 1145 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1142 LYS A CE  
10159 N NZ  . LYS D 1145 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1142 LYS A NZ  
10160 N N   . ASN D 1146 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1143 ASN A N   
10161 C CA  . ASN D 1146 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1143 ASN A CA  
10162 C C   . ASN D 1146 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1143 ASN A C   
10163 O O   . ASN D 1146 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1143 ASN A O   
10164 C CB  . ASN D 1146 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1143 ASN A CB  
10165 C CG  . ASN D 1146 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1143 ASN A CG  
10166 O OD1 . ASN D 1146 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1143 ASN A OD1 
10167 N ND2 . ASN D 1146 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1143 ASN A ND2 
10168 N N   . GLU D 1147 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1144 GLU A N   
10169 C CA  . GLU D 1147 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1144 GLU A CA  
10170 C C   . GLU D 1147 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1144 GLU A C   
10171 O O   . GLU D 1147 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1144 GLU A O   
10172 C CB  . GLU D 1147 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1144 GLU A CB  
10173 C CG  . GLU D 1147 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1144 GLU A CG  
10174 C CD  . GLU D 1147 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1144 GLU A CD  
10175 O OE1 . GLU D 1147 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1144 GLU A OE1 
10176 O OE2 . GLU D 1147 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1144 GLU A OE2 
10177 N N   . THR D 1148 ? 0.6814 0.6814 0.6814 0.0000  0.0000  0.0000  1145 THR A N   
10178 C CA  . THR D 1148 ? 0.6814 0.6814 0.6814 0.0000  0.0000  0.0000  1145 THR A CA  
10179 C C   . THR D 1148 ? 0.6814 0.6814 0.6814 0.0000  0.0000  0.0000  1145 THR A C   
10180 O O   . THR D 1148 ? 0.6814 0.6814 0.6814 0.0000  0.0000  0.0000  1145 THR A O   
10181 C CB  . THR D 1148 ? 0.6814 0.6814 0.6814 0.0000  0.0000  0.0000  1145 THR A CB  
10182 O OG1 . THR D 1148 ? 0.6814 0.6814 0.6814 0.0000  0.0000  0.0000  1145 THR A OG1 
10183 C CG2 . THR D 1148 ? 0.6814 0.6814 0.6814 0.0000  0.0000  0.0000  1145 THR A CG2 
10184 N N   . GLN D 1149 ? 0.6917 0.6917 0.6917 0.0000  0.0000  0.0000  1146 GLN A N   
10185 C CA  . GLN D 1149 ? 0.6917 0.6917 0.6917 0.0000  0.0000  0.0000  1146 GLN A CA  
10186 C C   . GLN D 1149 ? 0.6917 0.6917 0.6917 0.0000  0.0000  0.0000  1146 GLN A C   
10187 O O   . GLN D 1149 ? 0.6917 0.6917 0.6917 0.0000  0.0000  0.0000  1146 GLN A O   
10188 C CB  . GLN D 1149 ? 0.6917 0.6917 0.6917 0.0000  0.0000  0.0000  1146 GLN A CB  
10189 C CG  . GLN D 1149 ? 0.6917 0.6917 0.6917 0.0000  0.0000  0.0000  1146 GLN A CG  
10190 C CD  . GLN D 1149 ? 0.6917 0.6917 0.6917 0.0000  0.0000  0.0000  1146 GLN A CD  
10191 O OE1 . GLN D 1149 ? 0.6917 0.6917 0.6917 0.0000  0.0000  0.0000  1146 GLN A OE1 
10192 N NE2 . GLN D 1149 ? 0.6917 0.6917 0.6917 0.0000  0.0000  0.0000  1146 GLN A NE2 
10193 N N   . PHE D 1150 ? 0.7071 0.7071 0.7071 0.0000  0.0000  0.0000  1147 PHE A N   
10194 C CA  . PHE D 1150 ? 0.7071 0.7071 0.7071 0.0000  0.0000  0.0000  1147 PHE A CA  
10195 C C   . PHE D 1150 ? 0.7071 0.7071 0.7071 0.0000  0.0000  0.0000  1147 PHE A C   
10196 O O   . PHE D 1150 ? 0.7071 0.7071 0.7071 0.0000  0.0000  0.0000  1147 PHE A O   
10197 C CB  . PHE D 1150 ? 0.7071 0.7071 0.7071 0.0000  0.0000  0.0000  1147 PHE A CB  
10198 C CG  . PHE D 1150 ? 0.7071 0.7071 0.7071 0.0000  0.0000  0.0000  1147 PHE A CG  
10199 C CD1 . PHE D 1150 ? 0.7071 0.7071 0.7071 0.0000  0.0000  0.0000  1147 PHE A CD1 
10200 C CD2 . PHE D 1150 ? 0.7071 0.7071 0.7071 0.0000  0.0000  0.0000  1147 PHE A CD2 
10201 C CE1 . PHE D 1150 ? 0.7071 0.7071 0.7071 0.0000  0.0000  0.0000  1147 PHE A CE1 
10202 C CE2 . PHE D 1150 ? 0.7071 0.7071 0.7071 0.0000  0.0000  0.0000  1147 PHE A CE2 
10203 C CZ  . PHE D 1150 ? 0.7071 0.7071 0.7071 0.0000  0.0000  0.0000  1147 PHE A CZ  
10204 N N   . ASP D 1151 ? 0.7222 0.7222 0.7222 0.0000  0.0000  0.0000  1148 ASP A N   
10205 C CA  . ASP D 1151 ? 0.7222 0.7222 0.7222 0.0000  0.0000  0.0000  1148 ASP A CA  
10206 C C   . ASP D 1151 ? 0.7222 0.7222 0.7222 0.0000  0.0000  0.0000  1148 ASP A C   
10207 O O   . ASP D 1151 ? 0.7222 0.7222 0.7222 0.0000  0.0000  0.0000  1148 ASP A O   
10208 C CB  . ASP D 1151 ? 0.7222 0.7222 0.7222 0.0000  0.0000  0.0000  1148 ASP A CB  
10209 C CG  . ASP D 1151 ? 0.7222 0.7222 0.7222 0.0000  0.0000  0.0000  1148 ASP A CG  
10210 O OD1 . ASP D 1151 ? 0.7222 0.7222 0.7222 0.0000  0.0000  0.0000  1148 ASP A OD1 
10211 O OD2 . ASP D 1151 ? 0.7222 0.7222 0.7222 0.0000  0.0000  0.0000  1148 ASP A OD2 
10212 N N   . ALA D 1152 ? 0.7687 0.7687 0.7687 0.0000  0.0000  0.0000  1149 ALA A N   
10213 C CA  . ALA D 1152 ? 0.7687 0.7687 0.7687 0.0000  0.0000  0.0000  1149 ALA A CA  
10214 C C   . ALA D 1152 ? 0.7687 0.7687 0.7687 0.0000  0.0000  0.0000  1149 ALA A C   
10215 O O   . ALA D 1152 ? 0.7687 0.7687 0.7687 0.0000  0.0000  0.0000  1149 ALA A O   
10216 C CB  . ALA D 1152 ? 0.7687 0.7687 0.7687 0.0000  0.0000  0.0000  1149 ALA A CB  
10217 N N   . LYS D 1153 ? 0.8281 0.8281 0.8281 0.0000  0.0000  0.0000  1150 LYS A N   
10218 C CA  . LYS D 1153 ? 0.8281 0.8281 0.8281 0.0000  0.0000  0.0000  1150 LYS A CA  
10219 C C   . LYS D 1153 ? 0.8281 0.8281 0.8281 0.0000  0.0000  0.0000  1150 LYS A C   
10220 O O   . LYS D 1153 ? 0.8281 0.8281 0.8281 0.0000  0.0000  0.0000  1150 LYS A O   
10226 N N   . GLY D 1154 ? 0.7966 0.7966 0.7966 0.0000  0.0000  0.0000  1151 GLY A N   
10227 C CA  . GLY D 1154 ? 0.7966 0.7966 0.7966 0.0000  0.0000  0.0000  1151 GLY A CA  
10228 C C   . GLY D 1154 ? 0.7966 0.7966 0.7966 0.0000  0.0000  0.0000  1151 GLY A C   
10229 O O   . GLY D 1154 ? 0.7966 0.7966 0.7966 0.0000  0.0000  0.0000  1151 GLY A O   
10230 N N   . THR D 1155 ? 0.8009 0.8009 0.8009 0.0000  0.0000  0.0000  1152 THR A N   
10231 C CA  . THR D 1155 ? 0.8009 0.8009 0.8009 0.0000  0.0000  0.0000  1152 THR A CA  
10232 C C   . THR D 1155 ? 0.8009 0.8009 0.8009 0.0000  0.0000  0.0000  1152 THR A C   
10233 O O   . THR D 1155 ? 0.8009 0.8009 0.8009 0.0000  0.0000  0.0000  1152 THR A O   
10234 C CB  . THR D 1155 ? 0.8009 0.8009 0.8009 0.0000  0.0000  0.0000  1152 THR A CB  
10235 O OG1 . THR D 1155 ? 0.8009 0.8009 0.8009 0.0000  0.0000  0.0000  1152 THR A OG1 
10236 C CG2 . THR D 1155 ? 0.8009 0.8009 0.8009 0.0000  0.0000  0.0000  1152 THR A CG2 
10237 N N   . PRO D 1156 ? 0.7477 0.7477 0.7477 0.0000  0.0000  0.0000  1153 PRO A N   
10238 C CA  . PRO D 1156 ? 0.7477 0.7477 0.7477 0.0000  0.0000  0.0000  1153 PRO A CA  
10239 C C   . PRO D 1156 ? 0.7477 0.7477 0.7477 0.0000  0.0000  0.0000  1153 PRO A C   
10240 O O   . PRO D 1156 ? 0.7477 0.7477 0.7477 0.0000  0.0000  0.0000  1153 PRO A O   
10241 C CB  . PRO D 1156 ? 0.7477 0.7477 0.7477 0.0000  0.0000  0.0000  1153 PRO A CB  
10242 C CG  . PRO D 1156 ? 0.7477 0.7477 0.7477 0.0000  0.0000  0.0000  1153 PRO A CG  
10243 C CD  . PRO D 1156 ? 0.7477 0.7477 0.7477 0.0000  0.0000  0.0000  1153 PRO A CD  
10244 N N   . PHE D 1157 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1154 PHE A N   
10245 C CA  . PHE D 1157 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1154 PHE A CA  
10246 C C   . PHE D 1157 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1154 PHE A C   
10247 O O   . PHE D 1157 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1154 PHE A O   
10248 C CB  . PHE D 1157 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1154 PHE A CB  
10249 C CG  . PHE D 1157 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1154 PHE A CG  
10250 C CD1 . PHE D 1157 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1154 PHE A CD1 
10251 C CD2 . PHE D 1157 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1154 PHE A CD2 
10252 C CE1 . PHE D 1157 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1154 PHE A CE1 
10253 C CE2 . PHE D 1157 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1154 PHE A CE2 
10254 C CZ  . PHE D 1157 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1154 PHE A CZ  
10255 N N   . ILE D 1158 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1155 ILE A N   
10256 C CA  . ILE D 1158 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1155 ILE A CA  
10257 C C   . ILE D 1158 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1155 ILE A C   
10258 O O   . ILE D 1158 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1155 ILE A O   
10259 C CB  . ILE D 1158 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1155 ILE A CB  
10260 C CG1 . ILE D 1158 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1155 ILE A CG1 
10261 C CG2 . ILE D 1158 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1155 ILE A CG2 
10262 C CD1 . ILE D 1158 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1155 ILE A CD1 
10263 N N   . ALA D 1159 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1156 ALA A N   
10264 C CA  . ALA D 1159 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1156 ALA A CA  
10265 C C   . ALA D 1159 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1156 ALA A C   
10266 O O   . ALA D 1159 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1156 ALA A O   
10267 C CB  . ALA D 1159 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1156 ALA A CB  
10268 N N   . GLY D 1160 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1157 GLY A N   
10269 C CA  . GLY D 1160 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1157 GLY A CA  
10270 C C   . GLY D 1160 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1157 GLY A C   
10271 O O   . GLY D 1160 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1157 GLY A O   
10272 N N   . LYS D 1161 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1158 LYS A N   
10273 C CA  . LYS D 1161 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1158 LYS A CA  
10274 C C   . LYS D 1161 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1158 LYS A C   
10275 O O   . LYS D 1161 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1158 LYS A O   
10276 C CB  . LYS D 1161 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1158 LYS A CB  
10277 C CG  . LYS D 1161 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1158 LYS A CG  
10278 C CD  . LYS D 1161 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1158 LYS A CD  
10279 C CE  . LYS D 1161 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1158 LYS A CE  
10280 N NZ  . LYS D 1161 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1158 LYS A NZ  
10281 N N   . ARG D 1162 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1159 ARG A N   
10282 C CA  . ARG D 1162 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1159 ARG A CA  
10283 C C   . ARG D 1162 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1159 ARG A C   
10284 O O   . ARG D 1162 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1159 ARG A O   
10285 C CB  . ARG D 1162 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1159 ARG A CB  
10286 C CG  . ARG D 1162 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1159 ARG A CG  
10287 C CD  . ARG D 1162 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1159 ARG A CD  
10288 N NE  . ARG D 1162 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1159 ARG A NE  
10289 C CZ  . ARG D 1162 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1159 ARG A CZ  
10290 N NH1 . ARG D 1162 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1159 ARG A NH1 
10291 N NH2 . ARG D 1162 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1159 ARG A NH2 
10292 N N   . ILE D 1163 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1160 ILE A N   
10293 C CA  . ILE D 1163 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1160 ILE A CA  
10294 C C   . ILE D 1163 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1160 ILE A C   
10295 O O   . ILE D 1163 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1160 ILE A O   
10296 C CB  . ILE D 1163 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1160 ILE A CB  
10297 C CG1 . ILE D 1163 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1160 ILE A CG1 
10298 C CG2 . ILE D 1163 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1160 ILE A CG2 
10299 C CD1 . ILE D 1163 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1160 ILE A CD1 
10300 N N   . VAL D 1164 ? 0.6984 0.6984 0.6984 0.0000  0.0000  0.0000  1161 VAL A N   
10301 C CA  . VAL D 1164 ? 0.6984 0.6984 0.6984 0.0000  0.0000  0.0000  1161 VAL A CA  
10302 C C   . VAL D 1164 ? 0.6984 0.6984 0.6984 0.0000  0.0000  0.0000  1161 VAL A C   
10303 O O   . VAL D 1164 ? 0.6984 0.6984 0.6984 0.0000  0.0000  0.0000  1161 VAL A O   
10304 C CB  . VAL D 1164 ? 0.6984 0.6984 0.6984 0.0000  0.0000  0.0000  1161 VAL A CB  
10305 C CG1 . VAL D 1164 ? 0.6984 0.6984 0.6984 0.0000  0.0000  0.0000  1161 VAL A CG1 
10306 C CG2 . VAL D 1164 ? 0.6984 0.6984 0.6984 0.0000  0.0000  0.0000  1161 VAL A CG2 
10307 N N   . PRO D 1165 ? 0.9651 0.9651 0.9651 0.0000  0.0000  0.0000  1162 PRO A N   
10308 C CA  . PRO D 1165 ? 0.9651 0.9651 0.9651 0.0000  0.0000  0.0000  1162 PRO A CA  
10309 C C   . PRO D 1165 ? 0.9651 0.9651 0.9651 0.0000  0.0000  0.0000  1162 PRO A C   
10310 O O   . PRO D 1165 ? 0.9651 0.9651 0.9651 0.0000  0.0000  0.0000  1162 PRO A O   
10311 C CB  . PRO D 1165 ? 0.9651 0.9651 0.9651 0.0000  0.0000  0.0000  1162 PRO A CB  
10312 C CG  . PRO D 1165 ? 0.9651 0.9651 0.9651 0.0000  0.0000  0.0000  1162 PRO A CG  
10313 C CD  . PRO D 1165 ? 0.9651 0.9651 0.9651 0.0000  0.0000  0.0000  1162 PRO A CD  
10400 N N   . TYR D 1176 ? 0.8087 0.8087 0.8087 0.0000  0.0000  0.0000  1173 TYR A N   
10401 C CA  . TYR D 1176 ? 0.8087 0.8087 0.8087 0.0000  0.0000  0.0000  1173 TYR A CA  
10402 C C   . TYR D 1176 ? 0.8087 0.8087 0.8087 0.0000  0.0000  0.0000  1173 TYR A C   
10403 O O   . TYR D 1176 ? 0.8087 0.8087 0.8087 0.0000  0.0000  0.0000  1173 TYR A O   
10404 C CB  . TYR D 1176 ? 0.8087 0.8087 0.8087 0.0000  0.0000  0.0000  1173 TYR A CB  
10405 C CG  . TYR D 1176 ? 0.8087 0.8087 0.8087 0.0000  0.0000  0.0000  1173 TYR A CG  
10406 C CD1 . TYR D 1176 ? 0.8087 0.8087 0.8087 0.0000  0.0000  0.0000  1173 TYR A CD1 
10407 C CD2 . TYR D 1176 ? 0.8087 0.8087 0.8087 0.0000  0.0000  0.0000  1173 TYR A CD2 
10408 C CE1 . TYR D 1176 ? 0.8087 0.8087 0.8087 0.0000  0.0000  0.0000  1173 TYR A CE1 
10409 C CE2 . TYR D 1176 ? 0.8087 0.8087 0.8087 0.0000  0.0000  0.0000  1173 TYR A CE2 
10410 C CZ  . TYR D 1176 ? 0.8087 0.8087 0.8087 0.0000  0.0000  0.0000  1173 TYR A CZ  
10411 O OH  . TYR D 1176 ? 0.8087 0.8087 0.8087 0.0000  0.0000  0.0000  1173 TYR A OH  
10412 N N   . ARG D 1177 ? 0.6843 0.6843 0.6843 0.0000  0.0000  0.0000  1174 ARG A N   
10413 C CA  . ARG D 1177 ? 0.6843 0.6843 0.6843 0.0000  0.0000  0.0000  1174 ARG A CA  
10414 C C   . ARG D 1177 ? 0.6843 0.6843 0.6843 0.0000  0.0000  0.0000  1174 ARG A C   
10415 O O   . ARG D 1177 ? 0.6843 0.6843 0.6843 0.0000  0.0000  0.0000  1174 ARG A O   
10416 C CB  . ARG D 1177 ? 0.6843 0.6843 0.6843 0.0000  0.0000  0.0000  1174 ARG A CB  
10417 C CG  . ARG D 1177 ? 0.6843 0.6843 0.6843 0.0000  0.0000  0.0000  1174 ARG A CG  
10418 C CD  . ARG D 1177 ? 0.6843 0.6843 0.6843 0.0000  0.0000  0.0000  1174 ARG A CD  
10419 N NE  . ARG D 1177 ? 0.6843 0.6843 0.6843 0.0000  0.0000  0.0000  1174 ARG A NE  
10420 C CZ  . ARG D 1177 ? 0.6843 0.6843 0.6843 0.0000  0.0000  0.0000  1174 ARG A CZ  
10421 N NH1 . ARG D 1177 ? 0.6843 0.6843 0.6843 0.0000  0.0000  0.0000  1174 ARG A NH1 
10422 N NH2 . ARG D 1177 ? 0.6843 0.6843 0.6843 0.0000  0.0000  0.0000  1174 ARG A NH2 
10423 N N   . ASP D 1178 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1175 ASP A N   
10424 C CA  . ASP D 1178 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1175 ASP A CA  
10425 C C   . ASP D 1178 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1175 ASP A C   
10426 O O   . ASP D 1178 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1175 ASP A O   
10427 C CB  . ASP D 1178 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1175 ASP A CB  
10428 C CG  . ASP D 1178 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1175 ASP A CG  
10429 O OD1 . ASP D 1178 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1175 ASP A OD1 
10430 O OD2 . ASP D 1178 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1175 ASP A OD2 
10431 N N   . LEU D 1179 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1176 LEU A N   
10432 C CA  . LEU D 1179 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1176 LEU A CA  
10433 C C   . LEU D 1179 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1176 LEU A C   
10434 O O   . LEU D 1179 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1176 LEU A O   
10435 C CB  . LEU D 1179 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1176 LEU A CB  
10436 C CG  . LEU D 1179 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1176 LEU A CG  
10437 C CD1 . LEU D 1179 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1176 LEU A CD1 
10438 C CD2 . LEU D 1179 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1176 LEU A CD2 
10439 N N   . TYR D 1180 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1177 TYR A N   
10440 C CA  . TYR D 1180 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1177 TYR A CA  
10441 C C   . TYR D 1180 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1177 TYR A C   
10442 O O   . TYR D 1180 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1177 TYR A O   
10443 C CB  . TYR D 1180 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1177 TYR A CB  
10444 C CG  . TYR D 1180 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1177 TYR A CG  
10445 C CD1 . TYR D 1180 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1177 TYR A CD1 
10446 C CD2 . TYR D 1180 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1177 TYR A CD2 
10447 C CE1 . TYR D 1180 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1177 TYR A CE1 
10448 C CE2 . TYR D 1180 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1177 TYR A CE2 
10449 C CZ  . TYR D 1180 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1177 TYR A CZ  
10450 O OH  . TYR D 1180 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1177 TYR A OH  
10451 N N   . PRO D 1181 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1178 PRO A N   
10452 C CA  . PRO D 1181 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1178 PRO A CA  
10453 C C   . PRO D 1181 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1178 PRO A C   
10454 O O   . PRO D 1181 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1178 PRO A O   
10455 C CB  . PRO D 1181 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1178 PRO A CB  
10456 C CG  . PRO D 1181 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1178 PRO A CG  
10457 C CD  . PRO D 1181 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1178 PRO A CD  
10458 N N   . ALA D 1182 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1179 ALA A N   
10459 C CA  . ALA D 1182 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1179 ALA A CA  
10460 C C   . ALA D 1182 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1179 ALA A C   
10461 O O   . ALA D 1182 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1179 ALA A O   
10462 C CB  . ALA D 1182 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1179 ALA A CB  
10463 N N   . ASN D 1183 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1180 ASN A N   
10464 C CA  . ASN D 1183 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1180 ASN A CA  
10465 C C   . ASN D 1183 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1180 ASN A C   
10466 O O   . ASN D 1183 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1180 ASN A O   
10467 C CB  . ASN D 1183 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1180 ASN A CB  
10468 C CG  . ASN D 1183 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1180 ASN A CG  
10469 O OD1 . ASN D 1183 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1180 ASN A OD1 
10470 N ND2 . ASN D 1183 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1180 ASN A ND2 
10471 N N   . GLU D 1184 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1181 GLU A N   
10472 C CA  . GLU D 1184 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1181 GLU A CA  
10473 C C   . GLU D 1184 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1181 GLU A C   
10474 O O   . GLU D 1184 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1181 GLU A O   
10475 C CB  . GLU D 1184 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1181 GLU A CB  
10476 C CG  . GLU D 1184 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1181 GLU A CG  
10477 C CD  . GLU D 1184 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1181 GLU A CD  
10478 O OE1 . GLU D 1184 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1181 GLU A OE1 
10479 O OE2 . GLU D 1184 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1181 GLU A OE2 
10480 N N   . LEU D 1185 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1182 LEU A N   
10481 C CA  . LEU D 1185 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1182 LEU A CA  
10482 C C   . LEU D 1185 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1182 LEU A C   
10483 O O   . LEU D 1185 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1182 LEU A O   
10484 C CB  . LEU D 1185 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1182 LEU A CB  
10485 C CG  . LEU D 1185 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1182 LEU A CG  
10486 C CD1 . LEU D 1185 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1182 LEU A CD1 
10487 C CD2 . LEU D 1185 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1182 LEU A CD2 
10488 N N   . ILE D 1186 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1183 ILE A N   
10489 C CA  . ILE D 1186 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1183 ILE A CA  
10490 C C   . ILE D 1186 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1183 ILE A C   
10491 O O   . ILE D 1186 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1183 ILE A O   
10492 C CB  . ILE D 1186 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1183 ILE A CB  
10493 C CG1 . ILE D 1186 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1183 ILE A CG1 
10494 C CG2 . ILE D 1186 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1183 ILE A CG2 
10495 C CD1 . ILE D 1186 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1183 ILE A CD1 
10496 N N   . ALA D 1187 ? 0.6459 0.6459 0.6459 0.0000  0.0000  0.0000  1184 ALA A N   
10497 C CA  . ALA D 1187 ? 0.6459 0.6459 0.6459 0.0000  0.0000  0.0000  1184 ALA A CA  
10498 C C   . ALA D 1187 ? 0.6459 0.6459 0.6459 0.0000  0.0000  0.0000  1184 ALA A C   
10499 O O   . ALA D 1187 ? 0.6459 0.6459 0.6459 0.0000  0.0000  0.0000  1184 ALA A O   
10500 C CB  . ALA D 1187 ? 0.6459 0.6459 0.6459 0.0000  0.0000  0.0000  1184 ALA A CB  
10501 N N   . LEU D 1188 ? 0.6637 0.6637 0.6637 0.0000  0.0000  0.0000  1185 LEU A N   
10502 C CA  . LEU D 1188 ? 0.6637 0.6637 0.6637 0.0000  0.0000  0.0000  1185 LEU A CA  
10503 C C   . LEU D 1188 ? 0.6637 0.6637 0.6637 0.0000  0.0000  0.0000  1185 LEU A C   
10504 O O   . LEU D 1188 ? 0.6637 0.6637 0.6637 0.0000  0.0000  0.0000  1185 LEU A O   
10505 C CB  . LEU D 1188 ? 0.6637 0.6637 0.6637 0.0000  0.0000  0.0000  1185 LEU A CB  
10506 C CG  . LEU D 1188 ? 0.6637 0.6637 0.6637 0.0000  0.0000  0.0000  1185 LEU A CG  
10507 C CD1 . LEU D 1188 ? 0.6637 0.6637 0.6637 0.0000  0.0000  0.0000  1185 LEU A CD1 
10508 C CD2 . LEU D 1188 ? 0.6637 0.6637 0.6637 0.0000  0.0000  0.0000  1185 LEU A CD2 
10509 N N   . LEU D 1189 ? 0.7187 0.7187 0.7187 0.0000  0.0000  0.0000  1186 LEU A N   
10510 C CA  . LEU D 1189 ? 0.7187 0.7187 0.7187 0.0000  0.0000  0.0000  1186 LEU A CA  
10511 C C   . LEU D 1189 ? 0.7187 0.7187 0.7187 0.0000  0.0000  0.0000  1186 LEU A C   
10512 O O   . LEU D 1189 ? 0.7187 0.7187 0.7187 0.0000  0.0000  0.0000  1186 LEU A O   
10513 C CB  . LEU D 1189 ? 0.7187 0.7187 0.7187 0.0000  0.0000  0.0000  1186 LEU A CB  
10514 C CG  . LEU D 1189 ? 0.7187 0.7187 0.7187 0.0000  0.0000  0.0000  1186 LEU A CG  
10515 C CD1 . LEU D 1189 ? 0.7187 0.7187 0.7187 0.0000  0.0000  0.0000  1186 LEU A CD1 
10516 C CD2 . LEU D 1189 ? 0.7187 0.7187 0.7187 0.0000  0.0000  0.0000  1186 LEU A CD2 
10517 N N   . GLU D 1190 ? 0.7428 0.7428 0.7428 0.0000  0.0000  0.0000  1187 GLU A N   
10518 C CA  . GLU D 1190 ? 0.7428 0.7428 0.7428 0.0000  0.0000  0.0000  1187 GLU A CA  
10519 C C   . GLU D 1190 ? 0.7428 0.7428 0.7428 0.0000  0.0000  0.0000  1187 GLU A C   
10520 O O   . GLU D 1190 ? 0.7428 0.7428 0.7428 0.0000  0.0000  0.0000  1187 GLU A O   
10521 C CB  . GLU D 1190 ? 0.7428 0.7428 0.7428 0.0000  0.0000  0.0000  1187 GLU A CB  
10522 C CG  . GLU D 1190 ? 0.7428 0.7428 0.7428 0.0000  0.0000  0.0000  1187 GLU A CG  
10523 C CD  . GLU D 1190 ? 0.7428 0.7428 0.7428 0.0000  0.0000  0.0000  1187 GLU A CD  
10524 O OE1 . GLU D 1190 ? 0.7428 0.7428 0.7428 0.0000  0.0000  0.0000  1187 GLU A OE1 
10525 O OE2 . GLU D 1190 ? 0.7428 0.7428 0.7428 0.0000  0.0000  0.0000  1187 GLU A OE2 
10526 N N   . GLU D 1191 ? 0.7438 0.7438 0.7438 0.0000  0.0000  0.0000  1188 GLU A N   
10527 C CA  . GLU D 1191 ? 0.7438 0.7438 0.7438 0.0000  0.0000  0.0000  1188 GLU A CA  
10528 C C   . GLU D 1191 ? 0.7438 0.7438 0.7438 0.0000  0.0000  0.0000  1188 GLU A C   
10529 O O   . GLU D 1191 ? 0.7438 0.7438 0.7438 0.0000  0.0000  0.0000  1188 GLU A O   
10530 C CB  . GLU D 1191 ? 0.7438 0.7438 0.7438 0.0000  0.0000  0.0000  1188 GLU A CB  
10531 C CG  . GLU D 1191 ? 0.7438 0.7438 0.7438 0.0000  0.0000  0.0000  1188 GLU A CG  
10532 C CD  . GLU D 1191 ? 0.7438 0.7438 0.7438 0.0000  0.0000  0.0000  1188 GLU A CD  
10533 O OE1 . GLU D 1191 ? 0.7438 0.7438 0.7438 0.0000  0.0000  0.0000  1188 GLU A OE1 
10534 O OE2 . GLU D 1191 ? 0.7438 0.7438 0.7438 0.0000  0.0000  0.0000  1188 GLU A OE2 
10535 N N   . LYS D 1192 ? 0.7652 0.7652 0.7652 0.0000  0.0000  0.0000  1189 LYS A N   
10536 C CA  . LYS D 1192 ? 0.7652 0.7652 0.7652 0.0000  0.0000  0.0000  1189 LYS A CA  
10537 C C   . LYS D 1192 ? 0.7652 0.7652 0.7652 0.0000  0.0000  0.0000  1189 LYS A C   
10538 O O   . LYS D 1192 ? 0.7652 0.7652 0.7652 0.0000  0.0000  0.0000  1189 LYS A O   
10539 C CB  . LYS D 1192 ? 0.7652 0.7652 0.7652 0.0000  0.0000  0.0000  1189 LYS A CB  
10540 C CG  . LYS D 1192 ? 0.7652 0.7652 0.7652 0.0000  0.0000  0.0000  1189 LYS A CG  
10541 C CD  . LYS D 1192 ? 0.7652 0.7652 0.7652 0.0000  0.0000  0.0000  1189 LYS A CD  
10542 C CE  . LYS D 1192 ? 0.7652 0.7652 0.7652 0.0000  0.0000  0.0000  1189 LYS A CE  
10543 N NZ  . LYS D 1192 ? 0.7652 0.7652 0.7652 0.0000  0.0000  0.0000  1189 LYS A NZ  
10544 N N   . GLY D 1193 ? 0.7865 0.7865 0.7865 0.0000  0.0000  0.0000  1190 GLY A N   
10545 C CA  . GLY D 1193 ? 0.7865 0.7865 0.7865 0.0000  0.0000  0.0000  1190 GLY A CA  
10546 C C   . GLY D 1193 ? 0.7865 0.7865 0.7865 0.0000  0.0000  0.0000  1190 GLY A C   
10547 O O   . GLY D 1193 ? 0.7865 0.7865 0.7865 0.0000  0.0000  0.0000  1190 GLY A O   
10548 N N   . ILE D 1194 ? 0.7594 0.7594 0.7594 0.0000  0.0000  0.0000  1191 ILE A N   
10549 C CA  . ILE D 1194 ? 0.7594 0.7594 0.7594 0.0000  0.0000  0.0000  1191 ILE A CA  
10550 C C   . ILE D 1194 ? 0.7594 0.7594 0.7594 0.0000  0.0000  0.0000  1191 ILE A C   
10551 O O   . ILE D 1194 ? 0.7594 0.7594 0.7594 0.0000  0.0000  0.0000  1191 ILE A O   
10552 C CB  . ILE D 1194 ? 0.7594 0.7594 0.7594 0.0000  0.0000  0.0000  1191 ILE A CB  
10553 C CG1 . ILE D 1194 ? 0.7594 0.7594 0.7594 0.0000  0.0000  0.0000  1191 ILE A CG1 
10554 C CG2 . ILE D 1194 ? 0.7594 0.7594 0.7594 0.0000  0.0000  0.0000  1191 ILE A CG2 
10555 C CD1 . ILE D 1194 ? 0.7594 0.7594 0.7594 0.0000  0.0000  0.0000  1191 ILE A CD1 
10556 N N   . VAL D 1195 ? 0.8198 0.8198 0.8198 0.0000  0.0000  0.0000  1192 VAL A N   
10557 C CA  . VAL D 1195 ? 0.8198 0.8198 0.8198 0.0000  0.0000  0.0000  1192 VAL A CA  
10558 C C   . VAL D 1195 ? 0.8198 0.8198 0.8198 0.0000  0.0000  0.0000  1192 VAL A C   
10559 O O   . VAL D 1195 ? 0.8198 0.8198 0.8198 0.0000  0.0000  0.0000  1192 VAL A O   
10560 C CB  . VAL D 1195 ? 0.8198 0.8198 0.8198 0.0000  0.0000  0.0000  1192 VAL A CB  
10561 C CG1 . VAL D 1195 ? 0.8198 0.8198 0.8198 0.0000  0.0000  0.0000  1192 VAL A CG1 
10562 C CG2 . VAL D 1195 ? 0.8198 0.8198 0.8198 0.0000  0.0000  0.0000  1192 VAL A CG2 
10563 N N   . PHE D 1196 ? 0.7727 0.7727 0.7727 0.0000  0.0000  0.0000  1193 PHE A N   
10564 C CA  . PHE D 1196 ? 0.7727 0.7727 0.7727 0.0000  0.0000  0.0000  1193 PHE A CA  
10565 C C   . PHE D 1196 ? 0.7727 0.7727 0.7727 0.0000  0.0000  0.0000  1193 PHE A C   
10566 O O   . PHE D 1196 ? 0.7727 0.7727 0.7727 0.0000  0.0000  0.0000  1193 PHE A O   
10567 C CB  . PHE D 1196 ? 0.7727 0.7727 0.7727 0.0000  0.0000  0.0000  1193 PHE A CB  
10568 C CG  . PHE D 1196 ? 0.7727 0.7727 0.7727 0.0000  0.0000  0.0000  1193 PHE A CG  
10569 C CD1 . PHE D 1196 ? 0.7727 0.7727 0.7727 0.0000  0.0000  0.0000  1193 PHE A CD1 
10570 C CD2 . PHE D 1196 ? 0.7727 0.7727 0.7727 0.0000  0.0000  0.0000  1193 PHE A CD2 
10571 C CE1 . PHE D 1196 ? 0.7727 0.7727 0.7727 0.0000  0.0000  0.0000  1193 PHE A CE1 
10572 C CE2 . PHE D 1196 ? 0.7727 0.7727 0.7727 0.0000  0.0000  0.0000  1193 PHE A CE2 
10573 C CZ  . PHE D 1196 ? 0.7727 0.7727 0.7727 0.0000  0.0000  0.0000  1193 PHE A CZ  
10574 N N   . ARG D 1197 ? 0.7766 0.7766 0.7766 0.0000  0.0000  0.0000  1194 ARG A N   
10575 C CA  . ARG D 1197 ? 0.7766 0.7766 0.7766 0.0000  0.0000  0.0000  1194 ARG A CA  
10576 C C   . ARG D 1197 ? 0.7766 0.7766 0.7766 0.0000  0.0000  0.0000  1194 ARG A C   
10577 O O   . ARG D 1197 ? 0.7766 0.7766 0.7766 0.0000  0.0000  0.0000  1194 ARG A O   
10578 C CB  . ARG D 1197 ? 0.7766 0.7766 0.7766 0.0000  0.0000  0.0000  1194 ARG A CB  
10579 C CG  . ARG D 1197 ? 0.7766 0.7766 0.7766 0.0000  0.0000  0.0000  1194 ARG A CG  
10580 C CD  . ARG D 1197 ? 0.7766 0.7766 0.7766 0.0000  0.0000  0.0000  1194 ARG A CD  
10581 N NE  . ARG D 1197 ? 0.7766 0.7766 0.7766 0.0000  0.0000  0.0000  1194 ARG A NE  
10582 C CZ  . ARG D 1197 ? 0.7766 0.7766 0.7766 0.0000  0.0000  0.0000  1194 ARG A CZ  
10583 N NH1 . ARG D 1197 ? 0.7766 0.7766 0.7766 0.0000  0.0000  0.0000  1194 ARG A NH1 
10584 N NH2 . ARG D 1197 ? 0.7766 0.7766 0.7766 0.0000  0.0000  0.0000  1194 ARG A NH2 
10585 N N   . ASP D 1198 ? 0.8233 0.8233 0.8233 0.0000  0.0000  0.0000  1195 ASP A N   
10586 C CA  . ASP D 1198 ? 0.8233 0.8233 0.8233 0.0000  0.0000  0.0000  1195 ASP A CA  
10587 C C   . ASP D 1198 ? 0.8233 0.8233 0.8233 0.0000  0.0000  0.0000  1195 ASP A C   
10588 O O   . ASP D 1198 ? 0.8233 0.8233 0.8233 0.0000  0.0000  0.0000  1195 ASP A O   
10589 C CB  . ASP D 1198 ? 0.8233 0.8233 0.8233 0.0000  0.0000  0.0000  1195 ASP A CB  
10590 C CG  . ASP D 1198 ? 0.8233 0.8233 0.8233 0.0000  0.0000  0.0000  1195 ASP A CG  
10591 O OD1 . ASP D 1198 ? 0.8233 0.8233 0.8233 0.0000  0.0000  0.0000  1195 ASP A OD1 
10592 O OD2 . ASP D 1198 ? 0.8233 0.8233 0.8233 0.0000  0.0000  0.0000  1195 ASP A OD2 
10593 N N   . GLY D 1199 ? 0.7561 0.7561 0.7561 0.0000  0.0000  0.0000  1196 GLY A N   
10594 C CA  . GLY D 1199 ? 0.7561 0.7561 0.7561 0.0000  0.0000  0.0000  1196 GLY A CA  
10595 C C   . GLY D 1199 ? 0.7561 0.7561 0.7561 0.0000  0.0000  0.0000  1196 GLY A C   
10596 O O   . GLY D 1199 ? 0.7561 0.7561 0.7561 0.0000  0.0000  0.0000  1196 GLY A O   
10597 N N   . SER D 1200 ? 0.6945 0.6945 0.6945 0.0000  0.0000  0.0000  1197 SER A N   
10598 C CA  . SER D 1200 ? 0.6945 0.6945 0.6945 0.0000  0.0000  0.0000  1197 SER A CA  
10599 C C   . SER D 1200 ? 0.6945 0.6945 0.6945 0.0000  0.0000  0.0000  1197 SER A C   
10600 O O   . SER D 1200 ? 0.6945 0.6945 0.6945 0.0000  0.0000  0.0000  1197 SER A O   
10601 C CB  . SER D 1200 ? 0.6945 0.6945 0.6945 0.0000  0.0000  0.0000  1197 SER A CB  
10602 O OG  . SER D 1200 ? 0.6945 0.6945 0.6945 0.0000  0.0000  0.0000  1197 SER A OG  
10603 N N   . ASN D 1201 ? 0.6749 0.6749 0.6749 0.0000  0.0000  0.0000  1198 ASN A N   
10604 C CA  . ASN D 1201 ? 0.6749 0.6749 0.6749 0.0000  0.0000  0.0000  1198 ASN A CA  
10605 C C   . ASN D 1201 ? 0.6749 0.6749 0.6749 0.0000  0.0000  0.0000  1198 ASN A C   
10606 O O   . ASN D 1201 ? 0.6749 0.6749 0.6749 0.0000  0.0000  0.0000  1198 ASN A O   
10607 C CB  . ASN D 1201 ? 0.6749 0.6749 0.6749 0.0000  0.0000  0.0000  1198 ASN A CB  
10608 C CG  . ASN D 1201 ? 0.6749 0.6749 0.6749 0.0000  0.0000  0.0000  1198 ASN A CG  
10609 O OD1 . ASN D 1201 ? 0.6749 0.6749 0.6749 0.0000  0.0000  0.0000  1198 ASN A OD1 
10610 N ND2 . ASN D 1201 ? 0.6749 0.6749 0.6749 0.0000  0.0000  0.0000  1198 ASN A ND2 
10611 N N   . ILE D 1202 ? 0.6675 0.6675 0.6675 0.0000  0.0000  0.0000  1199 ILE A N   
10612 C CA  . ILE D 1202 ? 0.6675 0.6675 0.6675 0.0000  0.0000  0.0000  1199 ILE A CA  
10613 C C   . ILE D 1202 ? 0.6675 0.6675 0.6675 0.0000  0.0000  0.0000  1199 ILE A C   
10614 O O   . ILE D 1202 ? 0.6675 0.6675 0.6675 0.0000  0.0000  0.0000  1199 ILE A O   
10615 C CB  . ILE D 1202 ? 0.6675 0.6675 0.6675 0.0000  0.0000  0.0000  1199 ILE A CB  
10616 C CG1 . ILE D 1202 ? 0.6675 0.6675 0.6675 0.0000  0.0000  0.0000  1199 ILE A CG1 
10617 C CG2 . ILE D 1202 ? 0.6675 0.6675 0.6675 0.0000  0.0000  0.0000  1199 ILE A CG2 
10618 C CD1 . ILE D 1202 ? 0.6675 0.6675 0.6675 0.0000  0.0000  0.0000  1199 ILE A CD1 
10619 N N   . LEU D 1203 ? 0.6964 0.6964 0.6964 0.0000  0.0000  0.0000  1200 LEU A N   
10620 C CA  . LEU D 1203 ? 0.6964 0.6964 0.6964 0.0000  0.0000  0.0000  1200 LEU A CA  
10621 C C   . LEU D 1203 ? 0.6964 0.6964 0.6964 0.0000  0.0000  0.0000  1200 LEU A C   
10622 O O   . LEU D 1203 ? 0.6964 0.6964 0.6964 0.0000  0.0000  0.0000  1200 LEU A O   
10623 C CB  . LEU D 1203 ? 0.6964 0.6964 0.6964 0.0000  0.0000  0.0000  1200 LEU A CB  
10624 C CG  . LEU D 1203 ? 0.6964 0.6964 0.6964 0.0000  0.0000  0.0000  1200 LEU A CG  
10625 C CD1 . LEU D 1203 ? 0.6964 0.6964 0.6964 0.0000  0.0000  0.0000  1200 LEU A CD1 
10626 C CD2 . LEU D 1203 ? 0.6964 0.6964 0.6964 0.0000  0.0000  0.0000  1200 LEU A CD2 
10627 N N   . PRO D 1204 ? 0.7271 0.7271 0.7271 0.0000  0.0000  0.0000  1201 PRO A N   
10628 C CA  . PRO D 1204 ? 0.7271 0.7271 0.7271 0.0000  0.0000  0.0000  1201 PRO A CA  
10629 C C   . PRO D 1204 ? 0.7271 0.7271 0.7271 0.0000  0.0000  0.0000  1201 PRO A C   
10630 O O   . PRO D 1204 ? 0.7271 0.7271 0.7271 0.0000  0.0000  0.0000  1201 PRO A O   
10631 C CB  . PRO D 1204 ? 0.7271 0.7271 0.7271 0.0000  0.0000  0.0000  1201 PRO A CB  
10632 C CG  . PRO D 1204 ? 0.7271 0.7271 0.7271 0.0000  0.0000  0.0000  1201 PRO A CG  
10633 C CD  . PRO D 1204 ? 0.7271 0.7271 0.7271 0.0000  0.0000  0.0000  1201 PRO A CD  
10634 N N   . LYS D 1205 ? 0.7475 0.7475 0.7475 0.0000  0.0000  0.0000  1202 LYS A N   
10635 C CA  . LYS D 1205 ? 0.7475 0.7475 0.7475 0.0000  0.0000  0.0000  1202 LYS A CA  
10636 C C   . LYS D 1205 ? 0.7475 0.7475 0.7475 0.0000  0.0000  0.0000  1202 LYS A C   
10637 O O   . LYS D 1205 ? 0.7475 0.7475 0.7475 0.0000  0.0000  0.0000  1202 LYS A O   
10638 C CB  . LYS D 1205 ? 0.7475 0.7475 0.7475 0.0000  0.0000  0.0000  1202 LYS A CB  
10639 C CG  . LYS D 1205 ? 0.7475 0.7475 0.7475 0.0000  0.0000  0.0000  1202 LYS A CG  
10640 C CD  . LYS D 1205 ? 0.7475 0.7475 0.7475 0.0000  0.0000  0.0000  1202 LYS A CD  
10641 C CE  . LYS D 1205 ? 0.7475 0.7475 0.7475 0.0000  0.0000  0.0000  1202 LYS A CE  
10642 N NZ  . LYS D 1205 ? 0.7475 0.7475 0.7475 0.0000  0.0000  0.0000  1202 LYS A NZ  
10643 N N   . LEU D 1206 ? 0.7343 0.7343 0.7343 0.0000  0.0000  0.0000  1203 LEU A N   
10644 C CA  . LEU D 1206 ? 0.7343 0.7343 0.7343 0.0000  0.0000  0.0000  1203 LEU A CA  
10645 C C   . LEU D 1206 ? 0.7343 0.7343 0.7343 0.0000  0.0000  0.0000  1203 LEU A C   
10646 O O   . LEU D 1206 ? 0.7343 0.7343 0.7343 0.0000  0.0000  0.0000  1203 LEU A O   
10647 C CB  . LEU D 1206 ? 0.7343 0.7343 0.7343 0.0000  0.0000  0.0000  1203 LEU A CB  
10648 C CG  . LEU D 1206 ? 0.7343 0.7343 0.7343 0.0000  0.0000  0.0000  1203 LEU A CG  
10649 C CD1 . LEU D 1206 ? 0.7343 0.7343 0.7343 0.0000  0.0000  0.0000  1203 LEU A CD1 
10650 C CD2 . LEU D 1206 ? 0.7343 0.7343 0.7343 0.0000  0.0000  0.0000  1203 LEU A CD2 
10651 N N   . LEU D 1207 ? 0.7669 0.7669 0.7669 0.0000  0.0000  0.0000  1204 LEU A N   
10652 C CA  . LEU D 1207 ? 0.7669 0.7669 0.7669 0.0000  0.0000  0.0000  1204 LEU A CA  
10653 C C   . LEU D 1207 ? 0.7669 0.7669 0.7669 0.0000  0.0000  0.0000  1204 LEU A C   
10654 O O   . LEU D 1207 ? 0.7669 0.7669 0.7669 0.0000  0.0000  0.0000  1204 LEU A O   
10655 C CB  . LEU D 1207 ? 0.7669 0.7669 0.7669 0.0000  0.0000  0.0000  1204 LEU A CB  
10656 C CG  . LEU D 1207 ? 0.7669 0.7669 0.7669 0.0000  0.0000  0.0000  1204 LEU A CG  
10657 C CD1 . LEU D 1207 ? 0.7669 0.7669 0.7669 0.0000  0.0000  0.0000  1204 LEU A CD1 
10658 C CD2 . LEU D 1207 ? 0.7669 0.7669 0.7669 0.0000  0.0000  0.0000  1204 LEU A CD2 
10659 N N   . GLU D 1208 ? 0.7941 0.7941 0.7941 0.0000  0.0000  0.0000  1205 GLU A N   
10660 C CA  . GLU D 1208 ? 0.7941 0.7941 0.7941 0.0000  0.0000  0.0000  1205 GLU A CA  
10661 C C   . GLU D 1208 ? 0.7941 0.7941 0.7941 0.0000  0.0000  0.0000  1205 GLU A C   
10662 O O   . GLU D 1208 ? 0.7941 0.7941 0.7941 0.0000  0.0000  0.0000  1205 GLU A O   
10668 N N   . ASN D 1209 ? 0.8631 0.8631 0.8631 0.0000  0.0000  0.0000  1206 ASN A N   
10669 C CA  . ASN D 1209 ? 0.8631 0.8631 0.8631 0.0000  0.0000  0.0000  1206 ASN A CA  
10670 C C   . ASN D 1209 ? 0.8631 0.8631 0.8631 0.0000  0.0000  0.0000  1206 ASN A C   
10671 O O   . ASN D 1209 ? 0.8631 0.8631 0.8631 0.0000  0.0000  0.0000  1206 ASN A O   
10672 C CB  . ASN D 1209 ? 0.8631 0.8631 0.8631 0.0000  0.0000  0.0000  1206 ASN A CB  
10673 C CG  . ASN D 1209 ? 0.8631 0.8631 0.8631 0.0000  0.0000  0.0000  1206 ASN A CG  
10674 O OD1 . ASN D 1209 ? 0.8631 0.8631 0.8631 0.0000  0.0000  0.0000  1206 ASN A OD1 
10675 N ND2 . ASN D 1209 ? 0.8631 0.8631 0.8631 0.0000  0.0000  0.0000  1206 ASN A ND2 
10676 N N   . ASP D 1210 ? 0.9167 0.9167 0.9167 0.0000  0.0000  0.0000  1207 ASP A N   
10677 C CA  . ASP D 1210 ? 0.9167 0.9167 0.9167 0.0000  0.0000  0.0000  1207 ASP A CA  
10678 C C   . ASP D 1210 ? 0.9167 0.9167 0.9167 0.0000  0.0000  0.0000  1207 ASP A C   
10679 O O   . ASP D 1210 ? 0.9167 0.9167 0.9167 0.0000  0.0000  0.0000  1207 ASP A O   
10680 C CB  . ASP D 1210 ? 0.9167 0.9167 0.9167 0.0000  0.0000  0.0000  1207 ASP A CB  
10681 C CG  . ASP D 1210 ? 0.9167 0.9167 0.9167 0.0000  0.0000  0.0000  1207 ASP A CG  
10682 O OD1 . ASP D 1210 ? 0.9167 0.9167 0.9167 0.0000  0.0000  0.0000  1207 ASP A OD1 
10683 O OD2 . ASP D 1210 ? 0.9167 0.9167 0.9167 0.0000  0.0000  0.0000  1207 ASP A OD2 
10684 N N   . ASP D 1211 ? 0.8341 0.8341 0.8341 0.0000  0.0000  0.0000  1208 ASP A N   
10685 C CA  . ASP D 1211 ? 0.8341 0.8341 0.8341 0.0000  0.0000  0.0000  1208 ASP A CA  
10686 C C   . ASP D 1211 ? 0.8341 0.8341 0.8341 0.0000  0.0000  0.0000  1208 ASP A C   
10687 O O   . ASP D 1211 ? 0.8341 0.8341 0.8341 0.0000  0.0000  0.0000  1208 ASP A O   
10688 C CB  . ASP D 1211 ? 0.8341 0.8341 0.8341 0.0000  0.0000  0.0000  1208 ASP A CB  
10689 C CG  . ASP D 1211 ? 0.8341 0.8341 0.8341 0.0000  0.0000  0.0000  1208 ASP A CG  
10690 O OD1 . ASP D 1211 ? 0.8341 0.8341 0.8341 0.0000  0.0000  0.0000  1208 ASP A OD1 
10691 O OD2 . ASP D 1211 ? 0.8341 0.8341 0.8341 0.0000  0.0000  0.0000  1208 ASP A OD2 
10692 N N   . SER D 1212 ? 0.7972 0.7972 0.7972 0.0000  0.0000  0.0000  1209 SER A N   
10693 C CA  . SER D 1212 ? 0.7972 0.7972 0.7972 0.0000  0.0000  0.0000  1209 SER A CA  
10694 C C   . SER D 1212 ? 0.7972 0.7972 0.7972 0.0000  0.0000  0.0000  1209 SER A C   
10695 O O   . SER D 1212 ? 0.7972 0.7972 0.7972 0.0000  0.0000  0.0000  1209 SER A O   
10696 C CB  . SER D 1212 ? 0.7972 0.7972 0.7972 0.0000  0.0000  0.0000  1209 SER A CB  
10697 O OG  . SER D 1212 ? 0.7972 0.7972 0.7972 0.0000  0.0000  0.0000  1209 SER A OG  
10698 N N   . HIS D 1213 ? 0.7717 0.7717 0.7717 0.0000  0.0000  0.0000  1210 HIS A N   
10699 C CA  . HIS D 1213 ? 0.7717 0.7717 0.7717 0.0000  0.0000  0.0000  1210 HIS A CA  
10700 C C   . HIS D 1213 ? 0.7717 0.7717 0.7717 0.0000  0.0000  0.0000  1210 HIS A C   
10701 O O   . HIS D 1213 ? 0.7717 0.7717 0.7717 0.0000  0.0000  0.0000  1210 HIS A O   
10702 C CB  . HIS D 1213 ? 0.7717 0.7717 0.7717 0.0000  0.0000  0.0000  1210 HIS A CB  
10703 C CG  . HIS D 1213 ? 0.7717 0.7717 0.7717 0.0000  0.0000  0.0000  1210 HIS A CG  
10704 N ND1 . HIS D 1213 ? 0.7717 0.7717 0.7717 0.0000  0.0000  0.0000  1210 HIS A ND1 
10705 C CD2 . HIS D 1213 ? 0.7717 0.7717 0.7717 0.0000  0.0000  0.0000  1210 HIS A CD2 
10706 C CE1 . HIS D 1213 ? 0.7717 0.7717 0.7717 0.0000  0.0000  0.0000  1210 HIS A CE1 
10707 N NE2 . HIS D 1213 ? 0.7717 0.7717 0.7717 0.0000  0.0000  0.0000  1210 HIS A NE2 
10708 N N   . ALA D 1214 ? 0.7040 0.7040 0.7040 0.0000  0.0000  0.0000  1211 ALA A N   
10709 C CA  . ALA D 1214 ? 0.7040 0.7040 0.7040 0.0000  0.0000  0.0000  1211 ALA A CA  
10710 C C   . ALA D 1214 ? 0.7040 0.7040 0.7040 0.0000  0.0000  0.0000  1211 ALA A C   
10711 O O   . ALA D 1214 ? 0.7040 0.7040 0.7040 0.0000  0.0000  0.0000  1211 ALA A O   
10712 C CB  . ALA D 1214 ? 0.7040 0.7040 0.7040 0.0000  0.0000  0.0000  1211 ALA A CB  
10713 N N   . ILE D 1215 ? 0.6655 0.6655 0.6655 0.0000  0.0000  0.0000  1212 ILE A N   
10714 C CA  . ILE D 1215 ? 0.6655 0.6655 0.6655 0.0000  0.0000  0.0000  1212 ILE A CA  
10715 C C   . ILE D 1215 ? 0.6655 0.6655 0.6655 0.0000  0.0000  0.0000  1212 ILE A C   
10716 O O   . ILE D 1215 ? 0.6655 0.6655 0.6655 0.0000  0.0000  0.0000  1212 ILE A O   
10717 C CB  . ILE D 1215 ? 0.6655 0.6655 0.6655 0.0000  0.0000  0.0000  1212 ILE A CB  
10718 C CG1 . ILE D 1215 ? 0.6655 0.6655 0.6655 0.0000  0.0000  0.0000  1212 ILE A CG1 
10719 C CG2 . ILE D 1215 ? 0.6655 0.6655 0.6655 0.0000  0.0000  0.0000  1212 ILE A CG2 
10720 C CD1 . ILE D 1215 ? 0.6655 0.6655 0.6655 0.0000  0.0000  0.0000  1212 ILE A CD1 
10721 N N   . ASP D 1216 ? 0.6635 0.6635 0.6635 0.0000  0.0000  0.0000  1213 ASP A N   
10722 C CA  . ASP D 1216 ? 0.6635 0.6635 0.6635 0.0000  0.0000  0.0000  1213 ASP A CA  
10723 C C   . ASP D 1216 ? 0.6635 0.6635 0.6635 0.0000  0.0000  0.0000  1213 ASP A C   
10724 O O   . ASP D 1216 ? 0.6635 0.6635 0.6635 0.0000  0.0000  0.0000  1213 ASP A O   
10725 C CB  . ASP D 1216 ? 0.6635 0.6635 0.6635 0.0000  0.0000  0.0000  1213 ASP A CB  
10726 C CG  . ASP D 1216 ? 0.6635 0.6635 0.6635 0.0000  0.0000  0.0000  1213 ASP A CG  
10727 O OD1 . ASP D 1216 ? 0.6635 0.6635 0.6635 0.0000  0.0000  0.0000  1213 ASP A OD1 
10728 O OD2 . ASP D 1216 ? 0.6635 0.6635 0.6635 0.0000  0.0000  0.0000  1213 ASP A OD2 
10729 N N   . THR D 1217 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1214 THR A N   
10730 C CA  . THR D 1217 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1214 THR A CA  
10731 C C   . THR D 1217 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1214 THR A C   
10732 O O   . THR D 1217 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1214 THR A O   
10733 C CB  . THR D 1217 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1214 THR A CB  
10734 O OG1 . THR D 1217 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1214 THR A OG1 
10735 C CG2 . THR D 1217 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1214 THR A CG2 
10736 N N   . MET D 1218 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1215 MET A N   
10737 C CA  . MET D 1218 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1215 MET A CA  
10738 C C   . MET D 1218 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1215 MET A C   
10739 O O   . MET D 1218 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1215 MET A O   
10740 C CB  . MET D 1218 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1215 MET A CB  
10741 C CG  . MET D 1218 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1215 MET A CG  
10742 S SD  . MET D 1218 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1215 MET A SD  
10743 C CE  . MET D 1218 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1215 MET A CE  
10744 N N   . VAL D 1219 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1216 VAL A N   
10745 C CA  . VAL D 1219 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1216 VAL A CA  
10746 C C   . VAL D 1219 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1216 VAL A C   
10747 O O   . VAL D 1219 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1216 VAL A O   
10748 C CB  . VAL D 1219 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1216 VAL A CB  
10749 C CG1 . VAL D 1219 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1216 VAL A CG1 
10750 C CG2 . VAL D 1219 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1216 VAL A CG2 
10751 N N   . ALA D 1220 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1217 ALA A N   
10752 C CA  . ALA D 1220 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1217 ALA A CA  
10753 C C   . ALA D 1220 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1217 ALA A C   
10754 O O   . ALA D 1220 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1217 ALA A O   
10755 C CB  . ALA D 1220 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1217 ALA A CB  
10756 N N   . LEU D 1221 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1218 LEU A N   
10757 C CA  . LEU D 1221 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1218 LEU A CA  
10758 C C   . LEU D 1221 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1218 LEU A C   
10759 O O   . LEU D 1221 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1218 LEU A O   
10760 C CB  . LEU D 1221 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1218 LEU A CB  
10761 C CG  . LEU D 1221 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1218 LEU A CG  
10762 C CD1 . LEU D 1221 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1218 LEU A CD1 
10763 C CD2 . LEU D 1221 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1218 LEU A CD2 
10764 N N   . ILE D 1222 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1219 ILE A N   
10765 C CA  . ILE D 1222 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1219 ILE A CA  
10766 C C   . ILE D 1222 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1219 ILE A C   
10767 O O   . ILE D 1222 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1219 ILE A O   
10768 C CB  . ILE D 1222 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1219 ILE A CB  
10769 C CG1 . ILE D 1222 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1219 ILE A CG1 
10770 C CG2 . ILE D 1222 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1219 ILE A CG2 
10771 C CD1 . ILE D 1222 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1219 ILE A CD1 
10772 N N   . ARG D 1223 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1220 ARG A N   
10773 C CA  . ARG D 1223 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1220 ARG A CA  
10774 C C   . ARG D 1223 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1220 ARG A C   
10775 O O   . ARG D 1223 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1220 ARG A O   
10776 C CB  . ARG D 1223 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1220 ARG A CB  
10777 C CG  . ARG D 1223 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1220 ARG A CG  
10778 C CD  . ARG D 1223 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1220 ARG A CD  
10779 N NE  . ARG D 1223 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1220 ARG A NE  
10780 C CZ  . ARG D 1223 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1220 ARG A CZ  
10781 N NH1 . ARG D 1223 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1220 ARG A NH1 
10782 N NH2 . ARG D 1223 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1220 ARG A NH2 
10783 N N   . SER D 1224 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1221 SER A N   
10784 C CA  . SER D 1224 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1221 SER A CA  
10785 C C   . SER D 1224 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1221 SER A C   
10786 O O   . SER D 1224 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1221 SER A O   
10787 C CB  . SER D 1224 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1221 SER A CB  
10788 O OG  . SER D 1224 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1221 SER A OG  
10789 N N   . VAL D 1225 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1222 VAL A N   
10790 C CA  . VAL D 1225 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1222 VAL A CA  
10791 C C   . VAL D 1225 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1222 VAL A C   
10792 O O   . VAL D 1225 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1222 VAL A O   
10793 C CB  . VAL D 1225 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1222 VAL A CB  
10794 C CG1 . VAL D 1225 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1222 VAL A CG1 
10795 C CG2 . VAL D 1225 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1222 VAL A CG2 
10796 N N   . LEU D 1226 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1223 LEU A N   
10797 C CA  . LEU D 1226 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1223 LEU A CA  
10798 C C   . LEU D 1226 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1223 LEU A C   
10799 O O   . LEU D 1226 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1223 LEU A O   
10800 C CB  . LEU D 1226 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1223 LEU A CB  
10801 C CG  . LEU D 1226 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1223 LEU A CG  
10802 C CD1 . LEU D 1226 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1223 LEU A CD1 
10803 C CD2 . LEU D 1226 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1223 LEU A CD2 
10804 N N   . GLN D 1227 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1224 GLN A N   
10805 C CA  . GLN D 1227 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1224 GLN A CA  
10806 C C   . GLN D 1227 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1224 GLN A C   
10807 O O   . GLN D 1227 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1224 GLN A O   
10808 C CB  . GLN D 1227 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1224 GLN A CB  
10809 C CG  . GLN D 1227 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1224 GLN A CG  
10810 C CD  . GLN D 1227 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1224 GLN A CD  
10811 O OE1 . GLN D 1227 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1224 GLN A OE1 
10812 N NE2 . GLN D 1227 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1224 GLN A NE2 
10813 N N   . MET D 1228 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1225 MET A N   
10814 C CA  . MET D 1228 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1225 MET A CA  
10815 C C   . MET D 1228 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1225 MET A C   
10816 O O   . MET D 1228 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1225 MET A O   
10817 C CB  . MET D 1228 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1225 MET A CB  
10818 C CG  . MET D 1228 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1225 MET A CG  
10819 S SD  . MET D 1228 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1225 MET A SD  
10820 C CE  . MET D 1228 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1225 MET A CE  
10821 N N   . ARG D 1229 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1226 ARG A N   
10822 C CA  . ARG D 1229 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1226 ARG A CA  
10823 C C   . ARG D 1229 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1226 ARG A C   
10824 O O   . ARG D 1229 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1226 ARG A O   
10825 C CB  . ARG D 1229 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1226 ARG A CB  
10826 C CG  . ARG D 1229 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1226 ARG A CG  
10827 C CD  . ARG D 1229 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1226 ARG A CD  
10828 N NE  . ARG D 1229 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1226 ARG A NE  
10829 C CZ  . ARG D 1229 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1226 ARG A CZ  
10830 N NH1 . ARG D 1229 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1226 ARG A NH1 
10831 N NH2 . ARG D 1229 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1226 ARG A NH2 
10832 N N   . ASN D 1230 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1227 ASN A N   
10833 C CA  . ASN D 1230 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1227 ASN A CA  
10834 C C   . ASN D 1230 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1227 ASN A C   
10835 O O   . ASN D 1230 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1227 ASN A O   
10836 C CB  . ASN D 1230 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1227 ASN A CB  
10837 C CG  . ASN D 1230 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1227 ASN A CG  
10838 O OD1 . ASN D 1230 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1227 ASN A OD1 
10839 N ND2 . ASN D 1230 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1227 ASN A ND2 
10840 N N   . SER D 1231 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1228 SER A N   
10841 C CA  . SER D 1231 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1228 SER A CA  
10842 C C   . SER D 1231 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1228 SER A C   
10843 O O   . SER D 1231 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1228 SER A O   
10844 C CB  . SER D 1231 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1228 SER A CB  
10845 O OG  . SER D 1231 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1228 SER A OG  
10846 N N   . ASN D 1232 ? 0.7294 0.7294 0.7294 0.0000  0.0000  0.0000  1229 ASN A N   
10847 C CA  . ASN D 1232 ? 0.7294 0.7294 0.7294 0.0000  0.0000  0.0000  1229 ASN A CA  
10848 C C   . ASN D 1232 ? 0.7294 0.7294 0.7294 0.0000  0.0000  0.0000  1229 ASN A C   
10849 O O   . ASN D 1232 ? 0.7294 0.7294 0.7294 0.0000  0.0000  0.0000  1229 ASN A O   
10850 C CB  . ASN D 1232 ? 0.7294 0.7294 0.7294 0.0000  0.0000  0.0000  1229 ASN A CB  
10851 C CG  . ASN D 1232 ? 0.7294 0.7294 0.7294 0.0000  0.0000  0.0000  1229 ASN A CG  
10852 O OD1 . ASN D 1232 ? 0.7294 0.7294 0.7294 0.0000  0.0000  0.0000  1229 ASN A OD1 
10853 N ND2 . ASN D 1232 ? 0.7294 0.7294 0.7294 0.0000  0.0000  0.0000  1229 ASN A ND2 
10854 N N   . ALA D 1233 ? 0.7544 0.7544 0.7544 0.0000  0.0000  0.0000  1230 ALA A N   
10855 C CA  . ALA D 1233 ? 0.7544 0.7544 0.7544 0.0000  0.0000  0.0000  1230 ALA A CA  
10856 C C   . ALA D 1233 ? 0.7544 0.7544 0.7544 0.0000  0.0000  0.0000  1230 ALA A C   
10857 O O   . ALA D 1233 ? 0.7544 0.7544 0.7544 0.0000  0.0000  0.0000  1230 ALA A O   
10858 C CB  . ALA D 1233 ? 0.7544 0.7544 0.7544 0.0000  0.0000  0.0000  1230 ALA A CB  
10859 N N   . ALA D 1234 ? 0.7774 0.7774 0.7774 0.0000  0.0000  0.0000  1231 ALA A N   
10860 C CA  . ALA D 1234 ? 0.7774 0.7774 0.7774 0.0000  0.0000  0.0000  1231 ALA A CA  
10861 C C   . ALA D 1234 ? 0.7774 0.7774 0.7774 0.0000  0.0000  0.0000  1231 ALA A C   
10862 O O   . ALA D 1234 ? 0.7774 0.7774 0.7774 0.0000  0.0000  0.0000  1231 ALA A O   
10863 C CB  . ALA D 1234 ? 0.7774 0.7774 0.7774 0.0000  0.0000  0.0000  1231 ALA A CB  
10864 N N   . THR D 1235 ? 0.8021 0.8021 0.8021 0.0000  0.0000  0.0000  1232 THR A N   
10865 C CA  . THR D 1235 ? 0.8021 0.8021 0.8021 0.0000  0.0000  0.0000  1232 THR A CA  
10866 C C   . THR D 1235 ? 0.8021 0.8021 0.8021 0.0000  0.0000  0.0000  1232 THR A C   
10867 O O   . THR D 1235 ? 0.8021 0.8021 0.8021 0.0000  0.0000  0.0000  1232 THR A O   
10868 C CB  . THR D 1235 ? 0.8021 0.8021 0.8021 0.0000  0.0000  0.0000  1232 THR A CB  
10869 O OG1 . THR D 1235 ? 0.8021 0.8021 0.8021 0.0000  0.0000  0.0000  1232 THR A OG1 
10870 C CG2 . THR D 1235 ? 0.8021 0.8021 0.8021 0.0000  0.0000  0.0000  1232 THR A CG2 
10871 N N   . GLY D 1236 ? 0.7796 0.7796 0.7796 0.0000  0.0000  0.0000  1233 GLY A N   
10872 C CA  . GLY D 1236 ? 0.7796 0.7796 0.7796 0.0000  0.0000  0.0000  1233 GLY A CA  
10873 C C   . GLY D 1236 ? 0.7796 0.7796 0.7796 0.0000  0.0000  0.0000  1233 GLY A C   
10874 O O   . GLY D 1236 ? 0.7796 0.7796 0.7796 0.0000  0.0000  0.0000  1233 GLY A O   
10875 N N   . GLU D 1237 ? 0.7040 0.7040 0.7040 0.0000  0.0000  0.0000  1234 GLU A N   
10876 C CA  . GLU D 1237 ? 0.7040 0.7040 0.7040 0.0000  0.0000  0.0000  1234 GLU A CA  
10877 C C   . GLU D 1237 ? 0.7040 0.7040 0.7040 0.0000  0.0000  0.0000  1234 GLU A C   
10878 O O   . GLU D 1237 ? 0.7040 0.7040 0.7040 0.0000  0.0000  0.0000  1234 GLU A O   
10879 C CB  . GLU D 1237 ? 0.7040 0.7040 0.7040 0.0000  0.0000  0.0000  1234 GLU A CB  
10880 C CG  . GLU D 1237 ? 0.7040 0.7040 0.7040 0.0000  0.0000  0.0000  1234 GLU A CG  
10881 C CD  . GLU D 1237 ? 0.7040 0.7040 0.7040 0.0000  0.0000  0.0000  1234 GLU A CD  
10882 O OE1 . GLU D 1237 ? 0.7040 0.7040 0.7040 0.0000  0.0000  0.0000  1234 GLU A OE1 
10883 O OE2 . GLU D 1237 ? 0.7040 0.7040 0.7040 0.0000  0.0000  0.0000  1234 GLU A OE2 
10884 N N   . ASP D 1238 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1235 ASP A N   
10885 C CA  . ASP D 1238 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1235 ASP A CA  
10886 C C   . ASP D 1238 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1235 ASP A C   
10887 O O   . ASP D 1238 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1235 ASP A O   
10888 C CB  . ASP D 1238 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1235 ASP A CB  
10889 C CG  . ASP D 1238 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1235 ASP A CG  
10890 O OD1 . ASP D 1238 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1235 ASP A OD1 
10891 O OD2 . ASP D 1238 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1235 ASP A OD2 
10892 N N   . TYR D 1239 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1236 TYR A N   
10893 C CA  . TYR D 1239 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1236 TYR A CA  
10894 C C   . TYR D 1239 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1236 TYR A C   
10895 O O   . TYR D 1239 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1236 TYR A O   
10896 C CB  . TYR D 1239 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1236 TYR A CB  
10897 C CG  . TYR D 1239 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1236 TYR A CG  
10898 C CD1 . TYR D 1239 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1236 TYR A CD1 
10899 C CD2 . TYR D 1239 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1236 TYR A CD2 
10900 C CE1 . TYR D 1239 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1236 TYR A CE1 
10901 C CE2 . TYR D 1239 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1236 TYR A CE2 
10902 C CZ  . TYR D 1239 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1236 TYR A CZ  
10903 O OH  . TYR D 1239 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1236 TYR A OH  
10904 N N   . ILE D 1240 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1237 ILE A N   
10905 C CA  . ILE D 1240 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1237 ILE A CA  
10906 C C   . ILE D 1240 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1237 ILE A C   
10907 O O   . ILE D 1240 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1237 ILE A O   
10908 C CB  . ILE D 1240 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1237 ILE A CB  
10909 C CG1 . ILE D 1240 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1237 ILE A CG1 
10910 C CG2 . ILE D 1240 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1237 ILE A CG2 
10911 C CD1 . ILE D 1240 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1237 ILE A CD1 
10912 N N   . ASN D 1241 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1238 ASN A N   
10913 C CA  . ASN D 1241 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1238 ASN A CA  
10914 C C   . ASN D 1241 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1238 ASN A C   
10915 O O   . ASN D 1241 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1238 ASN A O   
10916 C CB  . ASN D 1241 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1238 ASN A CB  
10917 C CG  . ASN D 1241 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1238 ASN A CG  
10918 O OD1 . ASN D 1241 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1238 ASN A OD1 
10919 N ND2 . ASN D 1241 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1238 ASN A ND2 
10920 N N   . SER D 1242 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1239 SER A N   
10921 C CA  . SER D 1242 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1239 SER A CA  
10922 C C   . SER D 1242 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1239 SER A C   
10923 O O   . SER D 1242 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1239 SER A O   
10924 C CB  . SER D 1242 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1239 SER A CB  
10925 O OG  . SER D 1242 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1239 SER A OG  
10926 N N   . PRO D 1243 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1240 PRO A N   
10927 C CA  . PRO D 1243 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1240 PRO A CA  
10928 C C   . PRO D 1243 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1240 PRO A C   
10929 O O   . PRO D 1243 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1240 PRO A O   
10930 C CB  . PRO D 1243 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1240 PRO A CB  
10931 C CG  . PRO D 1243 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1240 PRO A CG  
10932 C CD  . PRO D 1243 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1240 PRO A CD  
10933 N N   . VAL D 1244 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1241 VAL A N   
10934 C CA  . VAL D 1244 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1241 VAL A CA  
10935 C C   . VAL D 1244 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1241 VAL A C   
10936 O O   . VAL D 1244 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1241 VAL A O   
10937 C CB  . VAL D 1244 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1241 VAL A CB  
10938 C CG1 . VAL D 1244 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1241 VAL A CG1 
10939 C CG2 . VAL D 1244 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1241 VAL A CG2 
10940 N N   . ARG D 1245 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1242 ARG A N   
10941 C CA  . ARG D 1245 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1242 ARG A CA  
10942 C C   . ARG D 1245 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1242 ARG A C   
10943 O O   . ARG D 1245 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1242 ARG A O   
10944 C CB  . ARG D 1245 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1242 ARG A CB  
10945 C CG  . ARG D 1245 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1242 ARG A CG  
10946 C CD  . ARG D 1245 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1242 ARG A CD  
10947 N NE  . ARG D 1245 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1242 ARG A NE  
10948 C CZ  . ARG D 1245 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1242 ARG A CZ  
10949 N NH1 . ARG D 1245 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1242 ARG A NH1 
10950 N NH2 . ARG D 1245 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1242 ARG A NH2 
10951 N N   . ASP D 1246 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1243 ASP A N   
10952 C CA  . ASP D 1246 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1243 ASP A CA  
10953 C C   . ASP D 1246 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1243 ASP A C   
10954 O O   . ASP D 1246 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1243 ASP A O   
10955 C CB  . ASP D 1246 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1243 ASP A CB  
10956 C CG  . ASP D 1246 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1243 ASP A CG  
10957 O OD1 . ASP D 1246 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1243 ASP A OD1 
10958 O OD2 . ASP D 1246 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1243 ASP A OD2 
10959 N N   . LEU D 1247 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1244 LEU A N   
10960 C CA  . LEU D 1247 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1244 LEU A CA  
10961 C C   . LEU D 1247 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1244 LEU A C   
10962 O O   . LEU D 1247 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1244 LEU A O   
10963 C CB  . LEU D 1247 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1244 LEU A CB  
10964 C CG  . LEU D 1247 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1244 LEU A CG  
10965 C CD1 . LEU D 1247 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1244 LEU A CD1 
10966 C CD2 . LEU D 1247 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1244 LEU A CD2 
10967 N N   . ASN D 1248 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1245 ASN A N   
10968 C CA  . ASN D 1248 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1245 ASN A CA  
10969 C C   . ASN D 1248 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1245 ASN A C   
10970 O O   . ASN D 1248 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1245 ASN A O   
10971 C CB  . ASN D 1248 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1245 ASN A CB  
10972 C CG  . ASN D 1248 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1245 ASN A CG  
10973 O OD1 . ASN D 1248 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1245 ASN A OD1 
10974 N ND2 . ASN D 1248 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1245 ASN A ND2 
10975 N N   . GLY D 1249 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1246 GLY A N   
10976 C CA  . GLY D 1249 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1246 GLY A CA  
10977 C C   . GLY D 1249 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1246 GLY A C   
10978 O O   . GLY D 1249 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1246 GLY A O   
10979 N N   . VAL D 1250 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1247 VAL A N   
10980 C CA  . VAL D 1250 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1247 VAL A CA  
10981 C C   . VAL D 1250 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1247 VAL A C   
10982 O O   . VAL D 1250 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1247 VAL A O   
10983 C CB  . VAL D 1250 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1247 VAL A CB  
10984 C CG1 . VAL D 1250 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1247 VAL A CG1 
10985 C CG2 . VAL D 1250 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1247 VAL A CG2 
10986 N N   . CYS D 1251 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1248 CYS A N   
10987 C CA  . CYS D 1251 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1248 CYS A CA  
10988 C C   . CYS D 1251 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1248 CYS A C   
10989 O O   . CYS D 1251 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1248 CYS A O   
10990 C CB  . CYS D 1251 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1248 CYS A CB  
10991 S SG  . CYS D 1251 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1248 CYS A SG  
10992 N N   . PHE D 1252 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1249 PHE A N   
10993 C CA  . PHE D 1252 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1249 PHE A CA  
10994 C C   . PHE D 1252 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1249 PHE A C   
10995 O O   . PHE D 1252 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1249 PHE A O   
10996 C CB  . PHE D 1252 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1249 PHE A CB  
10997 C CG  . PHE D 1252 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1249 PHE A CG  
10998 C CD1 . PHE D 1252 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1249 PHE A CD1 
10999 C CD2 . PHE D 1252 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1249 PHE A CD2 
11000 C CE1 . PHE D 1252 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1249 PHE A CE1 
11001 C CE2 . PHE D 1252 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1249 PHE A CE2 
11002 C CZ  . PHE D 1252 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1249 PHE A CZ  
11003 N N   . ASP D 1253 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1250 ASP A N   
11004 C CA  . ASP D 1253 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1250 ASP A CA  
11005 C C   . ASP D 1253 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1250 ASP A C   
11006 O O   . ASP D 1253 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1250 ASP A O   
11007 C CB  . ASP D 1253 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1250 ASP A CB  
11008 C CG  . ASP D 1253 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1250 ASP A CG  
11009 O OD1 . ASP D 1253 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1250 ASP A OD1 
11010 O OD2 . ASP D 1253 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1250 ASP A OD2 
11011 N N   . SER D 1254 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1251 SER A N   
11012 C CA  . SER D 1254 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1251 SER A CA  
11013 C C   . SER D 1254 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1251 SER A C   
11014 O O   . SER D 1254 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1251 SER A O   
11015 C CB  . SER D 1254 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1251 SER A CB  
11016 O OG  . SER D 1254 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1251 SER A OG  
11017 N N   . ARG D 1255 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1252 ARG A N   
11018 C CA  . ARG D 1255 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1252 ARG A CA  
11019 C C   . ARG D 1255 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1252 ARG A C   
11020 O O   . ARG D 1255 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1252 ARG A O   
11021 C CB  . ARG D 1255 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1252 ARG A CB  
11022 C CG  . ARG D 1255 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1252 ARG A CG  
11023 C CD  . ARG D 1255 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1252 ARG A CD  
11024 N NE  . ARG D 1255 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1252 ARG A NE  
11025 C CZ  . ARG D 1255 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1252 ARG A CZ  
11026 N NH1 . ARG D 1255 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1252 ARG A NH1 
11027 N NH2 . ARG D 1255 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1252 ARG A NH2 
11028 N N   . PHE D 1256 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1253 PHE A N   
11029 C CA  . PHE D 1256 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1253 PHE A CA  
11030 C C   . PHE D 1256 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1253 PHE A C   
11031 O O   . PHE D 1256 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1253 PHE A O   
11032 C CB  . PHE D 1256 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1253 PHE A CB  
11033 C CG  . PHE D 1256 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1253 PHE A CG  
11034 C CD1 . PHE D 1256 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1253 PHE A CD1 
11035 C CD2 . PHE D 1256 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1253 PHE A CD2 
11036 C CE1 . PHE D 1256 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1253 PHE A CE1 
11037 C CE2 . PHE D 1256 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1253 PHE A CE2 
11038 C CZ  . PHE D 1256 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1253 PHE A CZ  
11039 N N   . GLN D 1257 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1254 GLN A N   
11040 C CA  . GLN D 1257 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1254 GLN A CA  
11041 C C   . GLN D 1257 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1254 GLN A C   
11042 O O   . GLN D 1257 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1254 GLN A O   
11043 C CB  . GLN D 1257 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1254 GLN A CB  
11044 C CG  . GLN D 1257 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1254 GLN A CG  
11045 C CD  . GLN D 1257 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1254 GLN A CD  
11046 O OE1 . GLN D 1257 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1254 GLN A OE1 
11047 N NE2 . GLN D 1257 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1254 GLN A NE2 
11048 N N   . ASN D 1258 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1255 ASN A N   
11049 C CA  . ASN D 1258 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1255 ASN A CA  
11050 C C   . ASN D 1258 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1255 ASN A C   
11051 O O   . ASN D 1258 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1255 ASN A O   
11052 C CB  . ASN D 1258 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1255 ASN A CB  
11053 C CG  . ASN D 1258 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1255 ASN A CG  
11054 O OD1 . ASN D 1258 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1255 ASN A OD1 
11055 N ND2 . ASN D 1258 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1255 ASN A ND2 
11056 N N   . PRO D 1259 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1256 PRO A N   
11057 C CA  . PRO D 1259 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1256 PRO A CA  
11058 C C   . PRO D 1259 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1256 PRO A C   
11059 O O   . PRO D 1259 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1256 PRO A O   
11060 C CB  . PRO D 1259 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1256 PRO A CB  
11061 C CG  . PRO D 1259 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1256 PRO A CG  
11062 C CD  . PRO D 1259 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1256 PRO A CD  
11063 N N   . GLU D 1260 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1257 GLU A N   
11064 C CA  . GLU D 1260 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1257 GLU A CA  
11065 C C   . GLU D 1260 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1257 GLU A C   
11066 O O   . GLU D 1260 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1257 GLU A O   
11067 C CB  . GLU D 1260 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1257 GLU A CB  
11068 C CG  . GLU D 1260 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1257 GLU A CG  
11069 C CD  . GLU D 1260 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1257 GLU A CD  
11070 O OE1 . GLU D 1260 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1257 GLU A OE1 
11071 O OE2 . GLU D 1260 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1257 GLU A OE2 
11072 N N   . TRP D 1261 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1258 TRP A N   
11073 C CA  . TRP D 1261 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1258 TRP A CA  
11074 C C   . TRP D 1261 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1258 TRP A C   
11075 O O   . TRP D 1261 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1258 TRP A O   
11076 C CB  . TRP D 1261 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1258 TRP A CB  
11077 C CG  . TRP D 1261 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1258 TRP A CG  
11078 C CD1 . TRP D 1261 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1258 TRP A CD1 
11079 C CD2 . TRP D 1261 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1258 TRP A CD2 
11080 N NE1 . TRP D 1261 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1258 TRP A NE1 
11081 C CE2 . TRP D 1261 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1258 TRP A CE2 
11082 C CE3 . TRP D 1261 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1258 TRP A CE3 
11083 C CZ2 . TRP D 1261 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1258 TRP A CZ2 
11084 C CZ3 . TRP D 1261 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1258 TRP A CZ3 
11085 C CH2 . TRP D 1261 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1258 TRP A CH2 
11086 N N   . PRO D 1262 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1259 PRO A N   
11087 C CA  . PRO D 1262 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1259 PRO A CA  
11088 C C   . PRO D 1262 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1259 PRO A C   
11089 O O   . PRO D 1262 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1259 PRO A O   
11090 C CB  . PRO D 1262 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1259 PRO A CB  
11091 C CG  . PRO D 1262 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1259 PRO A CG  
11092 C CD  . PRO D 1262 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1259 PRO A CD  
11093 N N   . MET D 1263 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1260 MET A N   
11094 C CA  . MET D 1263 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1260 MET A CA  
11095 C C   . MET D 1263 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1260 MET A C   
11096 O O   . MET D 1263 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1260 MET A O   
11097 C CB  . MET D 1263 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1260 MET A CB  
11098 C CG  . MET D 1263 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1260 MET A CG  
11099 S SD  . MET D 1263 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1260 MET A SD  
11100 C CE  . MET D 1263 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1260 MET A CE  
11101 N N   . ASP D 1264 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1261 ASP A N   
11102 C CA  . ASP D 1264 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1261 ASP A CA  
11103 C C   . ASP D 1264 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1261 ASP A C   
11104 O O   . ASP D 1264 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1261 ASP A O   
11105 C CB  . ASP D 1264 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1261 ASP A CB  
11106 C CG  . ASP D 1264 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1261 ASP A CG  
11107 O OD1 . ASP D 1264 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1261 ASP A OD1 
11108 O OD2 . ASP D 1264 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1261 ASP A OD2 
11109 N N   . ALA D 1265 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1262 ALA A N   
11110 C CA  . ALA D 1265 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1262 ALA A CA  
11111 C C   . ALA D 1265 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1262 ALA A C   
11112 O O   . ALA D 1265 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1262 ALA A O   
11113 C CB  . ALA D 1265 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1262 ALA A CB  
11114 N N   . ASP D 1266 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1263 ASP A N   
11115 C CA  . ASP D 1266 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1263 ASP A CA  
11116 C C   . ASP D 1266 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1263 ASP A C   
11117 O O   . ASP D 1266 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1263 ASP A O   
11118 C CB  . ASP D 1266 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1263 ASP A CB  
11119 C CG  . ASP D 1266 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1263 ASP A CG  
11120 O OD1 . ASP D 1266 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1263 ASP A OD1 
11121 O OD2 . ASP D 1266 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1263 ASP A OD2 
11122 N N   . ALA D 1267 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1264 ALA A N   
11123 C CA  . ALA D 1267 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1264 ALA A CA  
11124 C C   . ALA D 1267 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1264 ALA A C   
11125 O O   . ALA D 1267 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1264 ALA A O   
11126 C CB  . ALA D 1267 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1264 ALA A CB  
11127 N N   . ASN D 1268 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1265 ASN A N   
11128 C CA  . ASN D 1268 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1265 ASN A CA  
11129 C C   . ASN D 1268 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1265 ASN A C   
11130 O O   . ASN D 1268 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1265 ASN A O   
11131 C CB  . ASN D 1268 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1265 ASN A CB  
11132 C CG  . ASN D 1268 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1265 ASN A CG  
11133 O OD1 . ASN D 1268 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1265 ASN A OD1 
11134 N ND2 . ASN D 1268 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1265 ASN A ND2 
11135 N N   . GLY D 1269 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1266 GLY A N   
11136 C CA  . GLY D 1269 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1266 GLY A CA  
11137 C C   . GLY D 1269 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1266 GLY A C   
11138 O O   . GLY D 1269 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1266 GLY A O   
11139 N N   . ALA D 1270 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1267 ALA A N   
11140 C CA  . ALA D 1270 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1267 ALA A CA  
11141 C C   . ALA D 1270 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1267 ALA A C   
11142 O O   . ALA D 1270 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1267 ALA A O   
11143 C CB  . ALA D 1270 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1267 ALA A CB  
11144 N N   . TYR D 1271 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1268 TYR A N   
11145 C CA  . TYR D 1271 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1268 TYR A CA  
11146 C C   . TYR D 1271 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1268 TYR A C   
11147 O O   . TYR D 1271 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1268 TYR A O   
11148 C CB  . TYR D 1271 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1268 TYR A CB  
11149 C CG  . TYR D 1271 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1268 TYR A CG  
11150 C CD1 . TYR D 1271 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1268 TYR A CD1 
11151 C CD2 . TYR D 1271 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1268 TYR A CD2 
11152 C CE1 . TYR D 1271 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1268 TYR A CE1 
11153 C CE2 . TYR D 1271 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1268 TYR A CE2 
11154 C CZ  . TYR D 1271 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1268 TYR A CZ  
11155 O OH  . TYR D 1271 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1268 TYR A OH  
11156 N N   . HIS D 1272 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1269 HIS A N   
11157 C CA  . HIS D 1272 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1269 HIS A CA  
11158 C C   . HIS D 1272 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1269 HIS A C   
11159 O O   . HIS D 1272 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1269 HIS A O   
11160 C CB  . HIS D 1272 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1269 HIS A CB  
11161 C CG  . HIS D 1272 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1269 HIS A CG  
11162 N ND1 . HIS D 1272 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1269 HIS A ND1 
11163 C CD2 . HIS D 1272 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1269 HIS A CD2 
11164 C CE1 . HIS D 1272 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1269 HIS A CE1 
11165 N NE2 . HIS D 1272 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1269 HIS A NE2 
11166 N N   . ILE D 1273 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1270 ILE A N   
11167 C CA  . ILE D 1273 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1270 ILE A CA  
11168 C C   . ILE D 1273 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1270 ILE A C   
11169 O O   . ILE D 1273 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1270 ILE A O   
11170 C CB  . ILE D 1273 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1270 ILE A CB  
11171 C CG1 . ILE D 1273 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1270 ILE A CG1 
11172 C CG2 . ILE D 1273 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1270 ILE A CG2 
11173 C CD1 . ILE D 1273 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1270 ILE A CD1 
11174 N N   . ALA D 1274 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1271 ALA A N   
11175 C CA  . ALA D 1274 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1271 ALA A CA  
11176 C C   . ALA D 1274 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1271 ALA A C   
11177 O O   . ALA D 1274 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1271 ALA A O   
11178 C CB  . ALA D 1274 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1271 ALA A CB  
11179 N N   . LEU D 1275 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1272 LEU A N   
11180 C CA  . LEU D 1275 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1272 LEU A CA  
11181 C C   . LEU D 1275 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1272 LEU A C   
11182 O O   . LEU D 1275 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1272 LEU A O   
11183 C CB  . LEU D 1275 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1272 LEU A CB  
11184 C CG  . LEU D 1275 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1272 LEU A CG  
11185 C CD1 . LEU D 1275 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1272 LEU A CD1 
11186 C CD2 . LEU D 1275 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1272 LEU A CD2 
11187 N N   . LYS D 1276 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1273 LYS A N   
11188 C CA  . LYS D 1276 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1273 LYS A CA  
11189 C C   . LYS D 1276 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1273 LYS A C   
11190 O O   . LYS D 1276 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1273 LYS A O   
11191 C CB  . LYS D 1276 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1273 LYS A CB  
11192 C CG  . LYS D 1276 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1273 LYS A CG  
11193 C CD  . LYS D 1276 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1273 LYS A CD  
11194 C CE  . LYS D 1276 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1273 LYS A CE  
11195 N NZ  . LYS D 1276 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1273 LYS A NZ  
11196 N N   . GLY D 1277 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1274 GLY A N   
11197 C CA  . GLY D 1277 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1274 GLY A CA  
11198 C C   . GLY D 1277 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1274 GLY A C   
11199 O O   . GLY D 1277 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1274 GLY A O   
11200 N N   . GLN D 1278 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1275 GLN A N   
11201 C CA  . GLN D 1278 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1275 GLN A CA  
11202 C C   . GLN D 1278 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1275 GLN A C   
11203 O O   . GLN D 1278 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1275 GLN A O   
11204 C CB  . GLN D 1278 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1275 GLN A CB  
11205 C CG  . GLN D 1278 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1275 GLN A CG  
11206 C CD  . GLN D 1278 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1275 GLN A CD  
11207 O OE1 . GLN D 1278 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1275 GLN A OE1 
11208 N NE2 . GLN D 1278 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1275 GLN A NE2 
11209 N N   . LEU D 1279 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1276 LEU A N   
11210 C CA  . LEU D 1279 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1276 LEU A CA  
11211 C C   . LEU D 1279 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1276 LEU A C   
11212 O O   . LEU D 1279 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1276 LEU A O   
11213 C CB  . LEU D 1279 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1276 LEU A CB  
11214 C CG  . LEU D 1279 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1276 LEU A CG  
11215 C CD1 . LEU D 1279 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1276 LEU A CD1 
11216 C CD2 . LEU D 1279 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1276 LEU A CD2 
11217 N N   . LEU D 1280 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1277 LEU A N   
11218 C CA  . LEU D 1280 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1277 LEU A CA  
11219 C C   . LEU D 1280 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1277 LEU A C   
11220 O O   . LEU D 1280 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1277 LEU A O   
11221 C CB  . LEU D 1280 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1277 LEU A CB  
11222 C CG  . LEU D 1280 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1277 LEU A CG  
11223 C CD1 . LEU D 1280 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1277 LEU A CD1 
11224 C CD2 . LEU D 1280 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1277 LEU A CD2 
11225 N N   . LEU D 1281 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1278 LEU A N   
11226 C CA  . LEU D 1281 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1278 LEU A CA  
11227 C C   . LEU D 1281 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1278 LEU A C   
11228 O O   . LEU D 1281 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1278 LEU A O   
11229 C CB  . LEU D 1281 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1278 LEU A CB  
11230 C CG  . LEU D 1281 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1278 LEU A CG  
11231 C CD1 . LEU D 1281 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1278 LEU A CD1 
11232 C CD2 . LEU D 1281 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1278 LEU A CD2 
11233 N N   . ASN D 1282 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1279 ASN A N   
11234 C CA  . ASN D 1282 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1279 ASN A CA  
11235 C C   . ASN D 1282 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1279 ASN A C   
11236 O O   . ASN D 1282 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1279 ASN A O   
11237 C CB  . ASN D 1282 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1279 ASN A CB  
11238 C CG  . ASN D 1282 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1279 ASN A CG  
11239 O OD1 . ASN D 1282 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1279 ASN A OD1 
11240 N ND2 . ASN D 1282 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1279 ASN A ND2 
11241 N N   . HIS D 1283 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1280 HIS A N   
11242 C CA  . HIS D 1283 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1280 HIS A CA  
11243 C C   . HIS D 1283 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1280 HIS A C   
11244 O O   . HIS D 1283 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1280 HIS A O   
11245 C CB  . HIS D 1283 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1280 HIS A CB  
11246 C CG  . HIS D 1283 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1280 HIS A CG  
11247 N ND1 . HIS D 1283 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1280 HIS A ND1 
11248 C CD2 . HIS D 1283 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1280 HIS A CD2 
11249 C CE1 . HIS D 1283 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1280 HIS A CE1 
11250 N NE2 . HIS D 1283 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1280 HIS A NE2 
11251 N N   . LEU D 1284 ? 0.6965 0.6965 0.6965 0.0000  0.0000  0.0000  1281 LEU A N   
11252 C CA  . LEU D 1284 ? 0.6965 0.6965 0.6965 0.0000  0.0000  0.0000  1281 LEU A CA  
11253 C C   . LEU D 1284 ? 0.6965 0.6965 0.6965 0.0000  0.0000  0.0000  1281 LEU A C   
11254 O O   . LEU D 1284 ? 0.6965 0.6965 0.6965 0.0000  0.0000  0.0000  1281 LEU A O   
11255 C CB  . LEU D 1284 ? 0.6965 0.6965 0.6965 0.0000  0.0000  0.0000  1281 LEU A CB  
11256 C CG  . LEU D 1284 ? 0.6965 0.6965 0.6965 0.0000  0.0000  0.0000  1281 LEU A CG  
11257 C CD1 . LEU D 1284 ? 0.6965 0.6965 0.6965 0.0000  0.0000  0.0000  1281 LEU A CD1 
11258 C CD2 . LEU D 1284 ? 0.6965 0.6965 0.6965 0.0000  0.0000  0.0000  1281 LEU A CD2 
11259 N N   . LYS D 1285 ? 0.7257 0.7257 0.7257 0.0000  0.0000  0.0000  1282 LYS A N   
11260 C CA  . LYS D 1285 ? 0.7257 0.7257 0.7257 0.0000  0.0000  0.0000  1282 LYS A CA  
11261 C C   . LYS D 1285 ? 0.7257 0.7257 0.7257 0.0000  0.0000  0.0000  1282 LYS A C   
11262 O O   . LYS D 1285 ? 0.7257 0.7257 0.7257 0.0000  0.0000  0.0000  1282 LYS A O   
11263 C CB  . LYS D 1285 ? 0.7257 0.7257 0.7257 0.0000  0.0000  0.0000  1282 LYS A CB  
11264 C CG  . LYS D 1285 ? 0.7257 0.7257 0.7257 0.0000  0.0000  0.0000  1282 LYS A CG  
11265 C CD  . LYS D 1285 ? 0.7257 0.7257 0.7257 0.0000  0.0000  0.0000  1282 LYS A CD  
11266 C CE  . LYS D 1285 ? 0.7257 0.7257 0.7257 0.0000  0.0000  0.0000  1282 LYS A CE  
11267 N NZ  . LYS D 1285 ? 0.7257 0.7257 0.7257 0.0000  0.0000  0.0000  1282 LYS A NZ  
11268 N N   . GLU D 1286 ? 0.8895 0.8895 0.8895 0.0000  0.0000  0.0000  1283 GLU A N   
11269 C CA  . GLU D 1286 ? 0.8895 0.8895 0.8895 0.0000  0.0000  0.0000  1283 GLU A CA  
11270 C C   . GLU D 1286 ? 0.8895 0.8895 0.8895 0.0000  0.0000  0.0000  1283 GLU A C   
11271 O O   . GLU D 1286 ? 0.8895 0.8895 0.8895 0.0000  0.0000  0.0000  1283 GLU A O   
11272 C CB  . GLU D 1286 ? 0.8895 0.8895 0.8895 0.0000  0.0000  0.0000  1283 GLU A CB  
11273 C CG  . GLU D 1286 ? 0.8895 0.8895 0.8895 0.0000  0.0000  0.0000  1283 GLU A CG  
11274 C CD  . GLU D 1286 ? 0.8895 0.8895 0.8895 0.0000  0.0000  0.0000  1283 GLU A CD  
11275 O OE1 . GLU D 1286 ? 0.8895 0.8895 0.8895 0.0000  0.0000  0.0000  1283 GLU A OE1 
11276 O OE2 . GLU D 1286 ? 0.8895 0.8895 0.8895 0.0000  0.0000  0.0000  1283 GLU A OE2 
11277 N N   . SER D 1287 ? 0.9253 0.9253 0.9253 0.0000  0.0000  0.0000  1284 SER A N   
11278 C CA  . SER D 1287 ? 0.9253 0.9253 0.9253 0.0000  0.0000  0.0000  1284 SER A CA  
11279 C C   . SER D 1287 ? 0.9253 0.9253 0.9253 0.0000  0.0000  0.0000  1284 SER A C   
11280 O O   . SER D 1287 ? 0.9253 0.9253 0.9253 0.0000  0.0000  0.0000  1284 SER A O   
11281 C CB  . SER D 1287 ? 0.9253 0.9253 0.9253 0.0000  0.0000  0.0000  1284 SER A CB  
11282 O OG  . SER D 1287 ? 0.9253 0.9253 0.9253 0.0000  0.0000  0.0000  1284 SER A OG  
11283 N N   . LYS D 1288 ? 0.9998 0.9998 0.9998 0.0000  0.0000  0.0000  1285 LYS A N   
11284 C CA  . LYS D 1288 ? 0.9998 0.9998 0.9998 0.0000  0.0000  0.0000  1285 LYS A CA  
11285 C C   . LYS D 1288 ? 0.9998 0.9998 0.9998 0.0000  0.0000  0.0000  1285 LYS A C   
11286 O O   . LYS D 1288 ? 0.9998 0.9998 0.9998 0.0000  0.0000  0.0000  1285 LYS A O   
11292 N N   . ASP D 1289 ? 0.9171 0.9171 0.9171 0.0000  0.0000  0.0000  1286 ASP A N   
11293 C CA  . ASP D 1289 ? 0.9171 0.9171 0.9171 0.0000  0.0000  0.0000  1286 ASP A CA  
11294 C C   . ASP D 1289 ? 0.9171 0.9171 0.9171 0.0000  0.0000  0.0000  1286 ASP A C   
11295 O O   . ASP D 1289 ? 0.9171 0.9171 0.9171 0.0000  0.0000  0.0000  1286 ASP A O   
11296 C CB  . ASP D 1289 ? 0.9171 0.9171 0.9171 0.0000  0.0000  0.0000  1286 ASP A CB  
11297 C CG  . ASP D 1289 ? 0.9171 0.9171 0.9171 0.0000  0.0000  0.0000  1286 ASP A CG  
11298 O OD1 . ASP D 1289 ? 0.9171 0.9171 0.9171 0.0000  0.0000  0.0000  1286 ASP A OD1 
11299 O OD2 . ASP D 1289 ? 0.9171 0.9171 0.9171 0.0000  0.0000  0.0000  1286 ASP A OD2 
11300 N N   . LEU D 1290 ? 0.7814 0.7814 0.7814 0.0000  0.0000  0.0000  1287 LEU A N   
11301 C CA  . LEU D 1290 ? 0.7814 0.7814 0.7814 0.0000  0.0000  0.0000  1287 LEU A CA  
11302 C C   . LEU D 1290 ? 0.7814 0.7814 0.7814 0.0000  0.0000  0.0000  1287 LEU A C   
11303 O O   . LEU D 1290 ? 0.7814 0.7814 0.7814 0.0000  0.0000  0.0000  1287 LEU A O   
11304 C CB  . LEU D 1290 ? 0.7814 0.7814 0.7814 0.0000  0.0000  0.0000  1287 LEU A CB  
11305 C CG  . LEU D 1290 ? 0.7814 0.7814 0.7814 0.0000  0.0000  0.0000  1287 LEU A CG  
11306 C CD1 . LEU D 1290 ? 0.7814 0.7814 0.7814 0.0000  0.0000  0.0000  1287 LEU A CD1 
11307 C CD2 . LEU D 1290 ? 0.7814 0.7814 0.7814 0.0000  0.0000  0.0000  1287 LEU A CD2 
11308 N N   . LYS D 1291 ? 0.8246 0.8246 0.8246 0.0000  0.0000  0.0000  1288 LYS A N   
11309 C CA  . LYS D 1291 ? 0.8246 0.8246 0.8246 0.0000  0.0000  0.0000  1288 LYS A CA  
11310 C C   . LYS D 1291 ? 0.8246 0.8246 0.8246 0.0000  0.0000  0.0000  1288 LYS A C   
11311 O O   . LYS D 1291 ? 0.8246 0.8246 0.8246 0.0000  0.0000  0.0000  1288 LYS A O   
11312 C CB  . LYS D 1291 ? 0.8246 0.8246 0.8246 0.0000  0.0000  0.0000  1288 LYS A CB  
11313 C CG  . LYS D 1291 ? 0.8246 0.8246 0.8246 0.0000  0.0000  0.0000  1288 LYS A CG  
11314 C CD  . LYS D 1291 ? 0.8246 0.8246 0.8246 0.0000  0.0000  0.0000  1288 LYS A CD  
11315 C CE  . LYS D 1291 ? 0.8246 0.8246 0.8246 0.0000  0.0000  0.0000  1288 LYS A CE  
11316 N NZ  . LYS D 1291 ? 0.8246 0.8246 0.8246 0.0000  0.0000  0.0000  1288 LYS A NZ  
11317 N N   . LEU D 1292 ? 0.7074 0.7074 0.7074 0.0000  0.0000  0.0000  1289 LEU A N   
11318 C CA  . LEU D 1292 ? 0.7074 0.7074 0.7074 0.0000  0.0000  0.0000  1289 LEU A CA  
11319 C C   . LEU D 1292 ? 0.7074 0.7074 0.7074 0.0000  0.0000  0.0000  1289 LEU A C   
11320 O O   . LEU D 1292 ? 0.7074 0.7074 0.7074 0.0000  0.0000  0.0000  1289 LEU A O   
11321 C CB  . LEU D 1292 ? 0.7074 0.7074 0.7074 0.0000  0.0000  0.0000  1289 LEU A CB  
11322 C CG  . LEU D 1292 ? 0.7074 0.7074 0.7074 0.0000  0.0000  0.0000  1289 LEU A CG  
11323 C CD1 . LEU D 1292 ? 0.7074 0.7074 0.7074 0.0000  0.0000  0.0000  1289 LEU A CD1 
11324 C CD2 . LEU D 1292 ? 0.7074 0.7074 0.7074 0.0000  0.0000  0.0000  1289 LEU A CD2 
11325 N N   . GLN D 1293 ? 0.7456 0.7456 0.7456 0.0000  0.0000  0.0000  1290 GLN A N   
11326 C CA  . GLN D 1293 ? 0.7456 0.7456 0.7456 0.0000  0.0000  0.0000  1290 GLN A CA  
11327 C C   . GLN D 1293 ? 0.7456 0.7456 0.7456 0.0000  0.0000  0.0000  1290 GLN A C   
11328 O O   . GLN D 1293 ? 0.7456 0.7456 0.7456 0.0000  0.0000  0.0000  1290 GLN A O   
11329 C CB  . GLN D 1293 ? 0.7456 0.7456 0.7456 0.0000  0.0000  0.0000  1290 GLN A CB  
11330 C CG  . GLN D 1293 ? 0.7456 0.7456 0.7456 0.0000  0.0000  0.0000  1290 GLN A CG  
11331 C CD  . GLN D 1293 ? 0.7456 0.7456 0.7456 0.0000  0.0000  0.0000  1290 GLN A CD  
11332 O OE1 . GLN D 1293 ? 0.7456 0.7456 0.7456 0.0000  0.0000  0.0000  1290 GLN A OE1 
11333 N NE2 . GLN D 1293 ? 0.7456 0.7456 0.7456 0.0000  0.0000  0.0000  1290 GLN A NE2 
11334 N N   . ASN D 1294 ? 0.8030 0.8030 0.8030 0.0000  0.0000  0.0000  1291 ASN A N   
11335 C CA  . ASN D 1294 ? 0.8030 0.8030 0.8030 0.0000  0.0000  0.0000  1291 ASN A CA  
11336 C C   . ASN D 1294 ? 0.8030 0.8030 0.8030 0.0000  0.0000  0.0000  1291 ASN A C   
11337 O O   . ASN D 1294 ? 0.8030 0.8030 0.8030 0.0000  0.0000  0.0000  1291 ASN A O   
11338 C CB  . ASN D 1294 ? 0.8030 0.8030 0.8030 0.0000  0.0000  0.0000  1291 ASN A CB  
11339 C CG  . ASN D 1294 ? 0.8030 0.8030 0.8030 0.0000  0.0000  0.0000  1291 ASN A CG  
11340 O OD1 . ASN D 1294 ? 0.8030 0.8030 0.8030 0.0000  0.0000  0.0000  1291 ASN A OD1 
11341 N ND2 . ASN D 1294 ? 0.8030 0.8030 0.8030 0.0000  0.0000  0.0000  1291 ASN A ND2 
11342 N N   . GLY D 1295 ? 0.6756 0.6756 0.6756 0.0000  0.0000  0.0000  1292 GLY A N   
11343 C CA  . GLY D 1295 ? 0.6756 0.6756 0.6756 0.0000  0.0000  0.0000  1292 GLY A CA  
11344 C C   . GLY D 1295 ? 0.6756 0.6756 0.6756 0.0000  0.0000  0.0000  1292 GLY A C   
11345 O O   . GLY D 1295 ? 0.6756 0.6756 0.6756 0.0000  0.0000  0.0000  1292 GLY A O   
11346 N N   . ILE D 1296 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1293 ILE A N   
11347 C CA  . ILE D 1296 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1293 ILE A CA  
11348 C C   . ILE D 1296 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1293 ILE A C   
11349 O O   . ILE D 1296 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1293 ILE A O   
11350 C CB  . ILE D 1296 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1293 ILE A CB  
11351 C CG1 . ILE D 1296 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1293 ILE A CG1 
11352 C CG2 . ILE D 1296 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1293 ILE A CG2 
11353 C CD1 . ILE D 1296 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1293 ILE A CD1 
11354 N N   . SER D 1297 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1294 SER A N   
11355 C CA  . SER D 1297 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1294 SER A CA  
11356 C C   . SER D 1297 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1294 SER A C   
11357 O O   . SER D 1297 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1294 SER A O   
11358 C CB  . SER D 1297 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1294 SER A CB  
11359 O OG  . SER D 1297 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1294 SER A OG  
11360 N N   . ASN D 1298 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1295 ASN A N   
11361 C CA  . ASN D 1298 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1295 ASN A CA  
11362 C C   . ASN D 1298 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1295 ASN A C   
11363 O O   . ASN D 1298 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1295 ASN A O   
11364 C CB  . ASN D 1298 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1295 ASN A CB  
11365 C CG  . ASN D 1298 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1295 ASN A CG  
11366 O OD1 . ASN D 1298 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1295 ASN A OD1 
11367 N ND2 . ASN D 1298 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1295 ASN A ND2 
11368 N N   . GLN D 1299 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1296 GLN A N   
11369 C CA  . GLN D 1299 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1296 GLN A CA  
11370 C C   . GLN D 1299 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1296 GLN A C   
11371 O O   . GLN D 1299 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1296 GLN A O   
11372 C CB  . GLN D 1299 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1296 GLN A CB  
11373 C CG  . GLN D 1299 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1296 GLN A CG  
11374 C CD  . GLN D 1299 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1296 GLN A CD  
11375 O OE1 . GLN D 1299 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1296 GLN A OE1 
11376 N NE2 . GLN D 1299 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1296 GLN A NE2 
11377 N N   . ASP D 1300 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1297 ASP A N   
11378 C CA  . ASP D 1300 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1297 ASP A CA  
11379 C C   . ASP D 1300 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1297 ASP A C   
11380 O O   . ASP D 1300 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1297 ASP A O   
11381 C CB  . ASP D 1300 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1297 ASP A CB  
11382 C CG  . ASP D 1300 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1297 ASP A CG  
11383 O OD1 . ASP D 1300 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1297 ASP A OD1 
11384 O OD2 . ASP D 1300 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1297 ASP A OD2 
11385 N N   . TRP D 1301 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1298 TRP A N   
11386 C CA  . TRP D 1301 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1298 TRP A CA  
11387 C C   . TRP D 1301 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1298 TRP A C   
11388 O O   . TRP D 1301 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1298 TRP A O   
11389 C CB  . TRP D 1301 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1298 TRP A CB  
11390 C CG  . TRP D 1301 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1298 TRP A CG  
11391 C CD1 . TRP D 1301 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1298 TRP A CD1 
11392 C CD2 . TRP D 1301 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1298 TRP A CD2 
11393 N NE1 . TRP D 1301 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1298 TRP A NE1 
11394 C CE2 . TRP D 1301 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1298 TRP A CE2 
11395 C CE3 . TRP D 1301 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1298 TRP A CE3 
11396 C CZ2 . TRP D 1301 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1298 TRP A CZ2 
11397 C CZ3 . TRP D 1301 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1298 TRP A CZ3 
11398 C CH2 . TRP D 1301 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1298 TRP A CH2 
11399 N N   . LEU D 1302 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1299 LEU A N   
11400 C CA  . LEU D 1302 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1299 LEU A CA  
11401 C C   . LEU D 1302 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1299 LEU A C   
11402 O O   . LEU D 1302 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1299 LEU A O   
11403 C CB  . LEU D 1302 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1299 LEU A CB  
11404 C CG  . LEU D 1302 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1299 LEU A CG  
11405 C CD1 . LEU D 1302 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1299 LEU A CD1 
11406 C CD2 . LEU D 1302 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1299 LEU A CD2 
11407 N N   . ALA D 1303 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1300 ALA A N   
11408 C CA  . ALA D 1303 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1300 ALA A CA  
11409 C C   . ALA D 1303 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1300 ALA A C   
11410 O O   . ALA D 1303 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1300 ALA A O   
11411 C CB  . ALA D 1303 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1300 ALA A CB  
11412 N N   . TYR D 1304 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1301 TYR A N   
11413 C CA  . TYR D 1304 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1301 TYR A CA  
11414 C C   . TYR D 1304 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1301 TYR A C   
11415 O O   . TYR D 1304 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1301 TYR A O   
11416 C CB  . TYR D 1304 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1301 TYR A CB  
11417 C CG  . TYR D 1304 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1301 TYR A CG  
11418 C CD1 . TYR D 1304 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1301 TYR A CD1 
11419 C CD2 . TYR D 1304 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1301 TYR A CD2 
11420 C CE1 . TYR D 1304 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1301 TYR A CE1 
11421 C CE2 . TYR D 1304 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1301 TYR A CE2 
11422 C CZ  . TYR D 1304 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1301 TYR A CZ  
11423 O OH  . TYR D 1304 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1301 TYR A OH  
11424 N N   . ILE D 1305 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1302 ILE A N   
11425 C CA  . ILE D 1305 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1302 ILE A CA  
11426 C C   . ILE D 1305 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1302 ILE A C   
11427 O O   . ILE D 1305 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1302 ILE A O   
11428 C CB  . ILE D 1305 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1302 ILE A CB  
11429 C CG1 . ILE D 1305 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1302 ILE A CG1 
11430 C CG2 . ILE D 1305 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1302 ILE A CG2 
11431 C CD1 . ILE D 1305 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1302 ILE A CD1 
11432 N N   . GLN D 1306 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1303 GLN A N   
11433 C CA  . GLN D 1306 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1303 GLN A CA  
11434 C C   . GLN D 1306 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1303 GLN A C   
11435 O O   . GLN D 1306 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1303 GLN A O   
11436 C CB  . GLN D 1306 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1303 GLN A CB  
11437 C CG  . GLN D 1306 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1303 GLN A CG  
11438 C CD  . GLN D 1306 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1303 GLN A CD  
11439 O OE1 . GLN D 1306 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1303 GLN A OE1 
11440 N NE2 . GLN D 1306 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1303 GLN A NE2 
11441 N N   . GLU D 1307 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1304 GLU A N   
11442 C CA  . GLU D 1307 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1304 GLU A CA  
11443 C C   . GLU D 1307 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1304 GLU A C   
11444 O O   . GLU D 1307 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1304 GLU A O   
11445 C CB  . GLU D 1307 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1304 GLU A CB  
11446 C CG  . GLU D 1307 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1304 GLU A CG  
11447 C CD  . GLU D 1307 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1304 GLU A CD  
11448 O OE1 . GLU D 1307 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1304 GLU A OE1 
11449 O OE2 . GLU D 1307 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1304 GLU A OE2 
11450 N N   . LEU D 1308 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1305 LEU A N   
11451 C CA  . LEU D 1308 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1305 LEU A CA  
11452 C C   . LEU D 1308 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1305 LEU A C   
11453 O O   . LEU D 1308 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1305 LEU A O   
11454 C CB  . LEU D 1308 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1305 LEU A CB  
11455 C CG  . LEU D 1308 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1305 LEU A CG  
11456 C CD1 . LEU D 1308 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1305 LEU A CD1 
11457 C CD2 . LEU D 1308 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1305 LEU A CD2 
11458 N N   . ARG D 1309 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1306 ARG A N   
11459 C CA  . ARG D 1309 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1306 ARG A CA  
11460 C C   . ARG D 1309 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1306 ARG A C   
11461 O O   . ARG D 1309 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1306 ARG A O   
11462 C CB  . ARG D 1309 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1306 ARG A CB  
11463 C CG  . ARG D 1309 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1306 ARG A CG  
11464 C CD  . ARG D 1309 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1306 ARG A CD  
11465 N NE  . ARG D 1309 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1306 ARG A NE  
11466 C CZ  . ARG D 1309 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1306 ARG A CZ  
11467 N NH1 . ARG D 1309 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1306 ARG A NH1 
11468 N NH2 . ARG D 1309 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1306 ARG A NH2 
11469 N N   . ASN D 1310 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1307 ASN A N   
11470 C CA  . ASN D 1310 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1307 ASN A CA  
11471 C C   . ASN D 1310 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1307 ASN A C   
11472 O O   . ASN D 1310 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1307 ASN A O   
11473 C CB  . ASN D 1310 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1307 ASN A CB  
11474 C CG  . ASN D 1310 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1307 ASN A CG  
11475 O OD1 . ASN D 1310 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1307 ASN A OD1 
11476 N ND2 . ASN D 1310 ? 0.6366 0.6366 0.6366 0.0000  0.0000  0.0000  1307 ASN A ND2 
# 
